data_9F38
# 
_entry.id   9F38 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9F38         pdb_00009f38 10.2210/pdb9f38/pdb 
WWPDB D_1292138103 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-02 
_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                        9F38 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-25 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 9EZ5 unspecified 
PDB . 9EZ7 unspecified 
PDB . 9EZD unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              marc.delarue@pasteur.fr 
_pdbx_contact_author.name_first         Marc 
_pdbx_contact_author.name_last          DELARUE 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0723-8102 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Sieskind, R.'    1  0000-0002-6511-6069 
'Missoury, S.'    2  0000-0001-7478-6956 
'Madru, C.'       3  0000-0002-5412-8822 
'Commenge, I.'    4  ?                   
'Niogret, G.'     5  0009-0002-6185-0183 
'Hollenstein, M.' 6  0000-0003-0263-9206 
'Rondelez, Y.'    7  0000-0002-2565-476X 
'Haouz, A.'       8  0000-0003-1196-1635 
'Sauguet, L.'     9  0000-0002-1259-6601 
'Legrand, P.'     10 0000-0003-2431-2255 
'Delarue, M.'     11 0000-0003-0723-8102 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Commun Biol' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2399-3642 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            8 
_citation.language                  ? 
_citation.page_first                387 
_citation.page_last                 387 
_citation.title                     
'Crystal structures of monomeric BsmI restriction endonuclease reveal coordinated sequential cleavage of two DNA strands.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s42003-025-07612-z 
_citation.pdbx_database_id_PubMed   40055548 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Sieskind, R.'    1  0000-0002-6511-6069 
primary 'Missoury, S.'    2  ?                   
primary 'Madru, C.'       3  ?                   
primary 'Commenge, I.'    4  ?                   
primary 'Niogret, G.'     5  ?                   
primary 'Hollenstein, M.' 6  0000-0003-0263-9206 
primary 'Rondelez, Y.'    7  0000-0002-2565-476X 
primary 'Sauguet, L.'     8  ?                   
primary 'Haouz, A.'       9  0000-0003-1196-1635 
primary 'Legrand, P.'     10 0000-0003-2431-2255 
primary 'Delarue, M.'     11 0000-0003-0723-8102 
# 
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 BsmI                                   78220.250 2   ? ? ? ? 
2 polymer     syn 'DNA (Bottom strand)'                  3893.534  2   ? ? ? ? 
3 polymer     syn 'DNA (Top strand)'                     4049.661  2   ? ? ? ? 
4 non-polymer syn 'CALCIUM ION'                          40.078    6   ? ? ? ? 
5 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' 195.237   1   ? ? ? ? 
6 non-polymer syn 'CHLORIDE ION'                         35.453    1   ? ? ? ? 
7 water       nat water                                  18.015    174 ? ? ? ? 
# 
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 
;MNVFRIHGDNIIECERVIDLILSKINPQKVKRGFISLSCPFIEIIFKEGHDYFHWRFDMFPGFNKNTNDRWNSNILDLLS
QKGSFLYETPDVIITSLNNGKEEILMAIEFCSALQAGNQAWQRSGRAYSVGRTGYPYIYIVDFVKYELNNSDRSRKNLRF
PNPAIPYSYISHSKNTGNFIVQAYFRGEEYQPKYDKKLKFFDETIFAEDDIADYIIAKLQHRDTSNIEQLLINKNLKMVE
FLSKNTKNDNNFTYSEWESIYNGTYRITNLPSLGRFKFRKKIAEKSLSGKVKEFNNIVQRYSVGLASSDLPFGVIRKESR
NDFINDVCKLYNINDMKIIKELKEDADLIVCMLKGFKPRGDDNRPDRGALPLVAMLAGENAQIFTFIYGPLIKGAINLID
QDINKLAKRNGLWKSFVSLSDFIVLDCPIIGESYNEFRLIINKNNKESILRKTSKQQNILVDPTPNHYQENDVDTVIYSI
FKYIVPNCFSGMCNPPGGDWSGLSIIRNGHEFRWLSLPRVSENGKRPDHVIQILDLFEKPLLLSIESKEKPNDLEPKIGV
QLIKYIEYLFDFTPSVQRKIAGGNWEFGNKSLVPNDFILLSAGAFIDYDNLTENDYEKIFEVTGCDLLIAIKNQNNPQKW
VIKFKPKNTIAEKLVNYIKLNFKSNIFDTGFFHIEG
;
;MNVFRIHGDNIIECERVIDLILSKINPQKVKRGFISLSCPFIEIIFKEGHDYFHWRFDMFPGFNKNTNDRWNSNILDLLS
QKGSFLYETPDVIITSLNNGKEEILMAIEFCSALQAGNQAWQRSGRAYSVGRTGYPYIYIVDFVKYELNNSDRSRKNLRF
PNPAIPYSYISHSKNTGNFIVQAYFRGEEYQPKYDKKLKFFDETIFAEDDIADYIIAKLQHRDTSNIEQLLINKNLKMVE
FLSKNTKNDNNFTYSEWESIYNGTYRITNLPSLGRFKFRKKIAEKSLSGKVKEFNNIVQRYSVGLASSDLPFGVIRKESR
NDFINDVCKLYNINDMKIIKELKEDADLIVCMLKGFKPRGDDNRPDRGALPLVAMLAGENAQIFTFIYGPLIKGAINLID
QDINKLAKRNGLWKSFVSLSDFIVLDCPIIGESYNEFRLIINKNNKESILRKTSKQQNILVDPTPNHYQENDVDTVIYSI
FKYIVPNCFSGMCNPPGGDWSGLSIIRNGHEFRWLSLPRVSENGKRPDHVIQILDLFEKPLLLSIESKEKPNDLEPKIGV
QLIKYIEYLFDFTPSVQRKIAGGNWEFGNKSLVPNDFILLSAGAFIDYDNLTENDYEKIFEVTGCDLLIAIKNQNNPQKW
VIKFKPKNTIAEKLVNYIKLNFKSNIFDTGFFHIEG
;
A,Z ? 
2 polydeoxyribonucleotide no no '(DG)(DT)(DC)(DT)(DG)(DC)(DA)(DT)(DT)(DC)(DC)(DT)(DC)' GTCTGCATTCCTC E,V ? 
3 polydeoxyribonucleotide no no '(DG)(DA)(DG)(DG)(DA)(DA)(DT)(DG)(DC)(DA)(DG)(DA)(DC)' GAGGAATGCAGAC F,U ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 'CALCIUM ION'                          CA  
5 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' MES 
6 'CHLORIDE ION'                         CL  
7 water                                  HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ASN n 
1 3   VAL n 
1 4   PHE n 
1 5   ARG n 
1 6   ILE n 
1 7   HIS n 
1 8   GLY n 
1 9   ASP n 
1 10  ASN n 
1 11  ILE n 
1 12  ILE n 
1 13  GLU n 
1 14  CYS n 
1 15  GLU n 
1 16  ARG n 
1 17  VAL n 
1 18  ILE n 
1 19  ASP n 
1 20  LEU n 
1 21  ILE n 
1 22  LEU n 
1 23  SER n 
1 24  LYS n 
1 25  ILE n 
1 26  ASN n 
1 27  PRO n 
1 28  GLN n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  ARG n 
1 33  GLY n 
1 34  PHE n 
1 35  ILE n 
1 36  SER n 
1 37  LEU n 
1 38  SER n 
1 39  CYS n 
1 40  PRO n 
1 41  PHE n 
1 42  ILE n 
1 43  GLU n 
1 44  ILE n 
1 45  ILE n 
1 46  PHE n 
1 47  LYS n 
1 48  GLU n 
1 49  GLY n 
1 50  HIS n 
1 51  ASP n 
1 52  TYR n 
1 53  PHE n 
1 54  HIS n 
1 55  TRP n 
1 56  ARG n 
1 57  PHE n 
1 58  ASP n 
1 59  MET n 
1 60  PHE n 
1 61  PRO n 
1 62  GLY n 
1 63  PHE n 
1 64  ASN n 
1 65  LYS n 
1 66  ASN n 
1 67  THR n 
1 68  ASN n 
1 69  ASP n 
1 70  ARG n 
1 71  TRP n 
1 72  ASN n 
1 73  SER n 
1 74  ASN n 
1 75  ILE n 
1 76  LEU n 
1 77  ASP n 
1 78  LEU n 
1 79  LEU n 
1 80  SER n 
1 81  GLN n 
1 82  LYS n 
1 83  GLY n 
1 84  SER n 
1 85  PHE n 
1 86  LEU n 
1 87  TYR n 
1 88  GLU n 
1 89  THR n 
1 90  PRO n 
1 91  ASP n 
1 92  VAL n 
1 93  ILE n 
1 94  ILE n 
1 95  THR n 
1 96  SER n 
1 97  LEU n 
1 98  ASN n 
1 99  ASN n 
1 100 GLY n 
1 101 LYS n 
1 102 GLU n 
1 103 GLU n 
1 104 ILE n 
1 105 LEU n 
1 106 MET n 
1 107 ALA n 
1 108 ILE n 
1 109 GLU n 
1 110 PHE n 
1 111 CYS n 
1 112 SER n 
1 113 ALA n 
1 114 LEU n 
1 115 GLN n 
1 116 ALA n 
1 117 GLY n 
1 118 ASN n 
1 119 GLN n 
1 120 ALA n 
1 121 TRP n 
1 122 GLN n 
1 123 ARG n 
1 124 SER n 
1 125 GLY n 
1 126 ARG n 
1 127 ALA n 
1 128 TYR n 
1 129 SER n 
1 130 VAL n 
1 131 GLY n 
1 132 ARG n 
1 133 THR n 
1 134 GLY n 
1 135 TYR n 
1 136 PRO n 
1 137 TYR n 
1 138 ILE n 
1 139 TYR n 
1 140 ILE n 
1 141 VAL n 
1 142 ASP n 
1 143 PHE n 
1 144 VAL n 
1 145 LYS n 
1 146 TYR n 
1 147 GLU n 
1 148 LEU n 
1 149 ASN n 
1 150 ASN n 
1 151 SER n 
1 152 ASP n 
1 153 ARG n 
1 154 SER n 
1 155 ARG n 
1 156 LYS n 
1 157 ASN n 
1 158 LEU n 
1 159 ARG n 
1 160 PHE n 
1 161 PRO n 
1 162 ASN n 
1 163 PRO n 
1 164 ALA n 
1 165 ILE n 
1 166 PRO n 
1 167 TYR n 
1 168 SER n 
1 169 TYR n 
1 170 ILE n 
1 171 SER n 
1 172 HIS n 
1 173 SER n 
1 174 LYS n 
1 175 ASN n 
1 176 THR n 
1 177 GLY n 
1 178 ASN n 
1 179 PHE n 
1 180 ILE n 
1 181 VAL n 
1 182 GLN n 
1 183 ALA n 
1 184 TYR n 
1 185 PHE n 
1 186 ARG n 
1 187 GLY n 
1 188 GLU n 
1 189 GLU n 
1 190 TYR n 
1 191 GLN n 
1 192 PRO n 
1 193 LYS n 
1 194 TYR n 
1 195 ASP n 
1 196 LYS n 
1 197 LYS n 
1 198 LEU n 
1 199 LYS n 
1 200 PHE n 
1 201 PHE n 
1 202 ASP n 
1 203 GLU n 
1 204 THR n 
1 205 ILE n 
1 206 PHE n 
1 207 ALA n 
1 208 GLU n 
1 209 ASP n 
1 210 ASP n 
1 211 ILE n 
1 212 ALA n 
1 213 ASP n 
1 214 TYR n 
1 215 ILE n 
1 216 ILE n 
1 217 ALA n 
1 218 LYS n 
1 219 LEU n 
1 220 GLN n 
1 221 HIS n 
1 222 ARG n 
1 223 ASP n 
1 224 THR n 
1 225 SER n 
1 226 ASN n 
1 227 ILE n 
1 228 GLU n 
1 229 GLN n 
1 230 LEU n 
1 231 LEU n 
1 232 ILE n 
1 233 ASN n 
1 234 LYS n 
1 235 ASN n 
1 236 LEU n 
1 237 LYS n 
1 238 MET n 
1 239 VAL n 
1 240 GLU n 
1 241 PHE n 
1 242 LEU n 
1 243 SER n 
1 244 LYS n 
1 245 ASN n 
1 246 THR n 
1 247 LYS n 
1 248 ASN n 
1 249 ASP n 
1 250 ASN n 
1 251 ASN n 
1 252 PHE n 
1 253 THR n 
1 254 TYR n 
1 255 SER n 
1 256 GLU n 
1 257 TRP n 
1 258 GLU n 
1 259 SER n 
1 260 ILE n 
1 261 TYR n 
1 262 ASN n 
1 263 GLY n 
1 264 THR n 
1 265 TYR n 
1 266 ARG n 
1 267 ILE n 
1 268 THR n 
1 269 ASN n 
1 270 LEU n 
1 271 PRO n 
1 272 SER n 
1 273 LEU n 
1 274 GLY n 
1 275 ARG n 
1 276 PHE n 
1 277 LYS n 
1 278 PHE n 
1 279 ARG n 
1 280 LYS n 
1 281 LYS n 
1 282 ILE n 
1 283 ALA n 
1 284 GLU n 
1 285 LYS n 
1 286 SER n 
1 287 LEU n 
1 288 SER n 
1 289 GLY n 
1 290 LYS n 
1 291 VAL n 
1 292 LYS n 
1 293 GLU n 
1 294 PHE n 
1 295 ASN n 
1 296 ASN n 
1 297 ILE n 
1 298 VAL n 
1 299 GLN n 
1 300 ARG n 
1 301 TYR n 
1 302 SER n 
1 303 VAL n 
1 304 GLY n 
1 305 LEU n 
1 306 ALA n 
1 307 SER n 
1 308 SER n 
1 309 ASP n 
1 310 LEU n 
1 311 PRO n 
1 312 PHE n 
1 313 GLY n 
1 314 VAL n 
1 315 ILE n 
1 316 ARG n 
1 317 LYS n 
1 318 GLU n 
1 319 SER n 
1 320 ARG n 
1 321 ASN n 
1 322 ASP n 
1 323 PHE n 
1 324 ILE n 
1 325 ASN n 
1 326 ASP n 
1 327 VAL n 
1 328 CYS n 
1 329 LYS n 
1 330 LEU n 
1 331 TYR n 
1 332 ASN n 
1 333 ILE n 
1 334 ASN n 
1 335 ASP n 
1 336 MET n 
1 337 LYS n 
1 338 ILE n 
1 339 ILE n 
1 340 LYS n 
1 341 GLU n 
1 342 LEU n 
1 343 LYS n 
1 344 GLU n 
1 345 ASP n 
1 346 ALA n 
1 347 ASP n 
1 348 LEU n 
1 349 ILE n 
1 350 VAL n 
1 351 CYS n 
1 352 MET n 
1 353 LEU n 
1 354 LYS n 
1 355 GLY n 
1 356 PHE n 
1 357 LYS n 
1 358 PRO n 
1 359 ARG n 
1 360 GLY n 
1 361 ASP n 
1 362 ASP n 
1 363 ASN n 
1 364 ARG n 
1 365 PRO n 
1 366 ASP n 
1 367 ARG n 
1 368 GLY n 
1 369 ALA n 
1 370 LEU n 
1 371 PRO n 
1 372 LEU n 
1 373 VAL n 
1 374 ALA n 
1 375 MET n 
1 376 LEU n 
1 377 ALA n 
1 378 GLY n 
1 379 GLU n 
1 380 ASN n 
1 381 ALA n 
1 382 GLN n 
1 383 ILE n 
1 384 PHE n 
1 385 THR n 
1 386 PHE n 
1 387 ILE n 
1 388 TYR n 
1 389 GLY n 
1 390 PRO n 
1 391 LEU n 
1 392 ILE n 
1 393 LYS n 
1 394 GLY n 
1 395 ALA n 
1 396 ILE n 
1 397 ASN n 
1 398 LEU n 
1 399 ILE n 
1 400 ASP n 
1 401 GLN n 
1 402 ASP n 
1 403 ILE n 
1 404 ASN n 
1 405 LYS n 
1 406 LEU n 
1 407 ALA n 
1 408 LYS n 
1 409 ARG n 
1 410 ASN n 
1 411 GLY n 
1 412 LEU n 
1 413 TRP n 
1 414 LYS n 
1 415 SER n 
1 416 PHE n 
1 417 VAL n 
1 418 SER n 
1 419 LEU n 
1 420 SER n 
1 421 ASP n 
1 422 PHE n 
1 423 ILE n 
1 424 VAL n 
1 425 LEU n 
1 426 ASP n 
1 427 CYS n 
1 428 PRO n 
1 429 ILE n 
1 430 ILE n 
1 431 GLY n 
1 432 GLU n 
1 433 SER n 
1 434 TYR n 
1 435 ASN n 
1 436 GLU n 
1 437 PHE n 
1 438 ARG n 
1 439 LEU n 
1 440 ILE n 
1 441 ILE n 
1 442 ASN n 
1 443 LYS n 
1 444 ASN n 
1 445 ASN n 
1 446 LYS n 
1 447 GLU n 
1 448 SER n 
1 449 ILE n 
1 450 LEU n 
1 451 ARG n 
1 452 LYS n 
1 453 THR n 
1 454 SER n 
1 455 LYS n 
1 456 GLN n 
1 457 GLN n 
1 458 ASN n 
1 459 ILE n 
1 460 LEU n 
1 461 VAL n 
1 462 ASP n 
1 463 PRO n 
1 464 THR n 
1 465 PRO n 
1 466 ASN n 
1 467 HIS n 
1 468 TYR n 
1 469 GLN n 
1 470 GLU n 
1 471 ASN n 
1 472 ASP n 
1 473 VAL n 
1 474 ASP n 
1 475 THR n 
1 476 VAL n 
1 477 ILE n 
1 478 TYR n 
1 479 SER n 
1 480 ILE n 
1 481 PHE n 
1 482 LYS n 
1 483 TYR n 
1 484 ILE n 
1 485 VAL n 
1 486 PRO n 
1 487 ASN n 
1 488 CYS n 
1 489 PHE n 
1 490 SER n 
1 491 GLY n 
1 492 MET n 
1 493 CYS n 
1 494 ASN n 
1 495 PRO n 
1 496 PRO n 
1 497 GLY n 
1 498 GLY n 
1 499 ASP n 
1 500 TRP n 
1 501 SER n 
1 502 GLY n 
1 503 LEU n 
1 504 SER n 
1 505 ILE n 
1 506 ILE n 
1 507 ARG n 
1 508 ASN n 
1 509 GLY n 
1 510 HIS n 
1 511 GLU n 
1 512 PHE n 
1 513 ARG n 
1 514 TRP n 
1 515 LEU n 
1 516 SER n 
1 517 LEU n 
1 518 PRO n 
1 519 ARG n 
1 520 VAL n 
1 521 SER n 
1 522 GLU n 
1 523 ASN n 
1 524 GLY n 
1 525 LYS n 
1 526 ARG n 
1 527 PRO n 
1 528 ASP n 
1 529 HIS n 
1 530 VAL n 
1 531 ILE n 
1 532 GLN n 
1 533 ILE n 
1 534 LEU n 
1 535 ASP n 
1 536 LEU n 
1 537 PHE n 
1 538 GLU n 
1 539 LYS n 
1 540 PRO n 
1 541 LEU n 
1 542 LEU n 
1 543 LEU n 
1 544 SER n 
1 545 ILE n 
1 546 GLU n 
1 547 SER n 
1 548 LYS n 
1 549 GLU n 
1 550 LYS n 
1 551 PRO n 
1 552 ASN n 
1 553 ASP n 
1 554 LEU n 
1 555 GLU n 
1 556 PRO n 
1 557 LYS n 
1 558 ILE n 
1 559 GLY n 
1 560 VAL n 
1 561 GLN n 
1 562 LEU n 
1 563 ILE n 
1 564 LYS n 
1 565 TYR n 
1 566 ILE n 
1 567 GLU n 
1 568 TYR n 
1 569 LEU n 
1 570 PHE n 
1 571 ASP n 
1 572 PHE n 
1 573 THR n 
1 574 PRO n 
1 575 SER n 
1 576 VAL n 
1 577 GLN n 
1 578 ARG n 
1 579 LYS n 
1 580 ILE n 
1 581 ALA n 
1 582 GLY n 
1 583 GLY n 
1 584 ASN n 
1 585 TRP n 
1 586 GLU n 
1 587 PHE n 
1 588 GLY n 
1 589 ASN n 
1 590 LYS n 
1 591 SER n 
1 592 LEU n 
1 593 VAL n 
1 594 PRO n 
1 595 ASN n 
1 596 ASP n 
1 597 PHE n 
1 598 ILE n 
1 599 LEU n 
1 600 LEU n 
1 601 SER n 
1 602 ALA n 
1 603 GLY n 
1 604 ALA n 
1 605 PHE n 
1 606 ILE n 
1 607 ASP n 
1 608 TYR n 
1 609 ASP n 
1 610 ASN n 
1 611 LEU n 
1 612 THR n 
1 613 GLU n 
1 614 ASN n 
1 615 ASP n 
1 616 TYR n 
1 617 GLU n 
1 618 LYS n 
1 619 ILE n 
1 620 PHE n 
1 621 GLU n 
1 622 VAL n 
1 623 THR n 
1 624 GLY n 
1 625 CYS n 
1 626 ASP n 
1 627 LEU n 
1 628 LEU n 
1 629 ILE n 
1 630 ALA n 
1 631 ILE n 
1 632 LYS n 
1 633 ASN n 
1 634 GLN n 
1 635 ASN n 
1 636 ASN n 
1 637 PRO n 
1 638 GLN n 
1 639 LYS n 
1 640 TRP n 
1 641 VAL n 
1 642 ILE n 
1 643 LYS n 
1 644 PHE n 
1 645 LYS n 
1 646 PRO n 
1 647 LYS n 
1 648 ASN n 
1 649 THR n 
1 650 ILE n 
1 651 ALA n 
1 652 GLU n 
1 653 LYS n 
1 654 LEU n 
1 655 VAL n 
1 656 ASN n 
1 657 TYR n 
1 658 ILE n 
1 659 LYS n 
1 660 LEU n 
1 661 ASN n 
1 662 PHE n 
1 663 LYS n 
1 664 SER n 
1 665 ASN n 
1 666 ILE n 
1 667 PHE n 
1 668 ASP n 
1 669 THR n 
1 670 GLY n 
1 671 PHE n 
1 672 PHE n 
1 673 HIS n 
1 674 ILE n 
1 675 GLU n 
1 676 GLY n 
2 1   DG  n 
2 2   DT  n 
2 3   DC  n 
2 4   DT  n 
2 5   DG  n 
2 6   DC  n 
2 7   DA  n 
2 8   DT  n 
2 9   DT  n 
2 10  DC  n 
2 11  DC  n 
2 12  DT  n 
2 13  DC  n 
3 1   DG  n 
3 2   DA  n 
3 3   DG  n 
3 4   DG  n 
3 5   DA  n 
3 6   DA  n 
3 7   DT  n 
3 8   DG  n 
3 9   DC  n 
3 10  DA  n 
3 11  DG  n 
3 12  DA  n 
3 13  DC  n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   676 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 bsmIR 
_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      'Geobacillus stearothermophilus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1422 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_pdbx_entity_src_syn.entity_id 
_pdbx_entity_src_syn.pdbx_src_id 
_pdbx_entity_src_syn.pdbx_alt_source_flag 
_pdbx_entity_src_syn.pdbx_beg_seq_num 
_pdbx_entity_src_syn.pdbx_end_seq_num 
_pdbx_entity_src_syn.organism_scientific 
_pdbx_entity_src_syn.organism_common_name 
_pdbx_entity_src_syn.ncbi_taxonomy_id 
_pdbx_entity_src_syn.details 
2 1 sample 1 13 'Geobacillus stearothermophilus' ? 1422 ? 
3 1 sample 1 13 'Geobacillus stearothermophilus' ? 1422 ? 
# 
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 
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  
CL  non-polymer         . 'CHLORIDE ION'                         ? 'Cl -1'           35.453  
CYS 'L-peptide linking' y CYSTEINE                               ? 'C3 H7 N O2 S'    121.158 
DA  'DNA linking'       y "2'-DEOXYADENOSINE-5'-MONOPHOSPHATE"   ? 'C10 H14 N5 O6 P' 331.222 
DC  'DNA linking'       y "2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE"    ? 'C9 H14 N3 O7 P'  307.197 
DG  'DNA linking'       y "2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE"   ? 'C10 H14 N5 O7 P' 347.221 
DT  'DNA linking'       y "THYMIDINE-5'-MONOPHOSPHATE"           ? 'C10 H15 N2 O8 P' 322.208 
GLN 'L-peptide linking' y GLUTAMINE                              ? 'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                        ? 'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE                                ? 'C2 H5 N O2'      75.067  
HIS 'L-peptide linking' y HISTIDINE                              ? 'C6 H10 N3 O2 1'  156.162 
HOH non-polymer         . WATER                                  ? 'H2 O'            18.015  
ILE 'L-peptide linking' y ISOLEUCINE                             ? 'C6 H13 N O2'     131.173 
LEU 'L-peptide linking' y LEUCINE                                ? 'C6 H13 N O2'     131.173 
LYS 'L-peptide linking' y LYSINE                                 ? 'C6 H15 N2 O2 1'  147.195 
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 
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   ASN 2   2   2   ASN ASN A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   PHE 4   4   4   PHE PHE A . n 
A 1 5   ARG 5   5   5   ARG ARG A . n 
A 1 6   ILE 6   6   6   ILE ILE A . n 
A 1 7   HIS 7   7   7   HIS HIS A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   ASP 9   9   9   ASP ASP A . n 
A 1 10  ASN 10  10  10  ASN ASN A . n 
A 1 11  ILE 11  11  11  ILE ILE A . n 
A 1 12  ILE 12  12  12  ILE ILE A . n 
A 1 13  GLU 13  13  13  GLU GLU A . n 
A 1 14  CYS 14  14  14  CYS CYS A . n 
A 1 15  GLU 15  15  15  GLU GLU A . n 
A 1 16  ARG 16  16  16  ARG ARG A . n 
A 1 17  VAL 17  17  17  VAL VAL A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  LEU 22  22  22  LEU LEU A . n 
A 1 23  SER 23  23  23  SER SER A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  ILE 25  25  25  ILE ILE A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  PRO 27  27  27  PRO PRO A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  ARG 32  32  32  ARG ARG A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  PHE 34  34  34  PHE PHE A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  SER 36  36  36  SER SER A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  SER 38  38  38  SER SER A . n 
A 1 39  CYS 39  39  39  CYS CYS A . n 
A 1 40  PRO 40  40  40  PRO PRO A . n 
A 1 41  PHE 41  41  41  PHE PHE A . n 
A 1 42  ILE 42  42  42  ILE ILE A . n 
A 1 43  GLU 43  43  43  GLU GLU A . n 
A 1 44  ILE 44  44  44  ILE ILE A . n 
A 1 45  ILE 45  45  45  ILE ILE A . n 
A 1 46  PHE 46  46  46  PHE PHE A . n 
A 1 47  LYS 47  47  47  LYS LYS A . n 
A 1 48  GLU 48  48  48  GLU GLU A . n 
A 1 49  GLY 49  49  49  GLY GLY A . n 
A 1 50  HIS 50  50  50  HIS HIS A . n 
A 1 51  ASP 51  51  51  ASP ASP A . n 
A 1 52  TYR 52  52  52  TYR TYR A . n 
A 1 53  PHE 53  53  53  PHE PHE A . n 
A 1 54  HIS 54  54  54  HIS HIS A . n 
A 1 55  TRP 55  55  55  TRP TRP A . n 
A 1 56  ARG 56  56  56  ARG ARG A . n 
A 1 57  PHE 57  57  57  PHE PHE A . n 
A 1 58  ASP 58  58  58  ASP ASP A . n 
A 1 59  MET 59  59  59  MET MET A . n 
A 1 60  PHE 60  60  60  PHE PHE A . n 
A 1 61  PRO 61  61  61  PRO PRO A . n 
A 1 62  GLY 62  62  62  GLY GLY A . n 
A 1 63  PHE 63  63  63  PHE PHE A . n 
A 1 64  ASN 64  64  64  ASN ASN A . n 
A 1 65  LYS 65  65  65  LYS LYS A . n 
A 1 66  ASN 66  66  66  ASN ASN A . n 
A 1 67  THR 67  67  67  THR THR A . n 
A 1 68  ASN 68  68  68  ASN ASN A . n 
A 1 69  ASP 69  69  69  ASP ASP A . n 
A 1 70  ARG 70  70  70  ARG ARG A . n 
A 1 71  TRP 71  71  71  TRP TRP A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  ASN 74  74  74  ASN ASN A . n 
A 1 75  ILE 75  75  75  ILE ILE A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  ASP 77  77  77  ASP ASP A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  GLN 81  81  81  GLN GLN A . n 
A 1 82  LYS 82  82  82  LYS LYS A . n 
A 1 83  GLY 83  83  83  GLY GLY A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  PHE 85  85  85  PHE PHE A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  TYR 87  87  87  TYR TYR A . n 
A 1 88  GLU 88  88  88  GLU GLU A . n 
A 1 89  THR 89  89  89  THR THR A . n 
A 1 90  PRO 90  90  90  PRO PRO A . n 
A 1 91  ASP 91  91  91  ASP ASP A . n 
A 1 92  VAL 92  92  92  VAL VAL A . n 
A 1 93  ILE 93  93  93  ILE ILE A . n 
A 1 94  ILE 94  94  94  ILE ILE A . n 
A 1 95  THR 95  95  95  THR THR A . n 
A 1 96  SER 96  96  96  SER SER A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  ASN 98  98  98  ASN ASN A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 LYS 101 101 101 LYS LYS A . n 
A 1 102 GLU 102 102 102 GLU GLU A . n 
A 1 103 GLU 103 103 103 GLU GLU A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 MET 106 106 106 MET MET A . n 
A 1 107 ALA 107 107 107 ALA ALA A . n 
A 1 108 ILE 108 108 108 ILE ILE A . n 
A 1 109 GLU 109 109 109 GLU GLU A . n 
A 1 110 PHE 110 110 110 PHE PHE A . n 
A 1 111 CYS 111 111 111 CYS CYS A . n 
A 1 112 SER 112 112 112 SER SER A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 LEU 114 114 114 LEU LEU A . n 
A 1 115 GLN 115 115 115 GLN GLN A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLY 117 117 117 GLY GLY A . n 
A 1 118 ASN 118 118 118 ASN ASN A . n 
A 1 119 GLN 119 119 119 GLN GLN A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 TRP 121 121 121 TRP TRP A . n 
A 1 122 GLN 122 122 122 GLN GLN A . n 
A 1 123 ARG 123 123 123 ARG ARG A . n 
A 1 124 SER 124 124 124 SER SER A . n 
A 1 125 GLY 125 125 125 GLY GLY A . n 
A 1 126 ARG 126 126 126 ARG ARG A . n 
A 1 127 ALA 127 127 127 ALA ALA A . n 
A 1 128 TYR 128 128 128 TYR TYR A . n 
A 1 129 SER 129 129 129 SER SER A . n 
A 1 130 VAL 130 130 130 VAL VAL A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 ARG 132 132 132 ARG ARG A . n 
A 1 133 THR 133 133 133 THR THR A . n 
A 1 134 GLY 134 134 134 GLY GLY A . n 
A 1 135 TYR 135 135 135 TYR TYR A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 TYR 137 137 137 TYR TYR A . n 
A 1 138 ILE 138 138 138 ILE ILE A . n 
A 1 139 TYR 139 139 139 TYR TYR A . n 
A 1 140 ILE 140 140 140 ILE ILE A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 ASP 142 142 142 ASP ASP A . n 
A 1 143 PHE 143 143 143 PHE PHE A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 LYS 145 145 145 LYS LYS A . n 
A 1 146 TYR 146 146 146 TYR TYR A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 LEU 148 148 148 LEU LEU A . n 
A 1 149 ASN 149 149 149 ASN ASN A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 SER 151 151 151 SER SER A . n 
A 1 152 ASP 152 152 152 ASP ASP A . n 
A 1 153 ARG 153 153 153 ARG ARG A . n 
A 1 154 SER 154 154 154 SER SER A . n 
A 1 155 ARG 155 155 155 ARG ARG A . n 
A 1 156 LYS 156 156 156 LYS LYS A . n 
A 1 157 ASN 157 157 157 ASN ASN A . n 
A 1 158 LEU 158 158 158 LEU LEU A . n 
A 1 159 ARG 159 159 159 ARG ARG A . n 
A 1 160 PHE 160 160 160 PHE PHE A . n 
A 1 161 PRO 161 161 161 PRO PRO A . n 
A 1 162 ASN 162 162 162 ASN ASN A . n 
A 1 163 PRO 163 163 163 PRO PRO A . n 
A 1 164 ALA 164 164 164 ALA ALA A . n 
A 1 165 ILE 165 165 165 ILE ILE A . n 
A 1 166 PRO 166 166 166 PRO PRO A . n 
A 1 167 TYR 167 167 167 TYR TYR A . n 
A 1 168 SER 168 168 168 SER SER A . n 
A 1 169 TYR 169 169 169 TYR TYR A . n 
A 1 170 ILE 170 170 170 ILE ILE A . n 
A 1 171 SER 171 171 171 SER SER A . n 
A 1 172 HIS 172 172 172 HIS HIS A . n 
A 1 173 SER 173 173 173 SER SER A . n 
A 1 174 LYS 174 174 174 LYS LYS A . n 
A 1 175 ASN 175 175 175 ASN ASN A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 GLY 177 177 177 GLY GLY A . n 
A 1 178 ASN 178 178 178 ASN ASN A . n 
A 1 179 PHE 179 179 179 PHE PHE A . n 
A 1 180 ILE 180 180 180 ILE ILE A . n 
A 1 181 VAL 181 181 181 VAL VAL A . n 
A 1 182 GLN 182 182 182 GLN GLN A . n 
A 1 183 ALA 183 183 183 ALA ALA A . n 
A 1 184 TYR 184 184 184 TYR TYR A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 ARG 186 186 186 ARG ARG A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 GLU 188 188 188 GLU GLU A . n 
A 1 189 GLU 189 189 189 GLU GLU A . n 
A 1 190 TYR 190 190 190 TYR TYR A . n 
A 1 191 GLN 191 191 191 GLN GLN A . n 
A 1 192 PRO 192 192 192 PRO PRO A . n 
A 1 193 LYS 193 193 193 LYS LYS A . n 
A 1 194 TYR 194 194 194 TYR TYR A . n 
A 1 195 ASP 195 195 195 ASP ASP A . n 
A 1 196 LYS 196 196 196 LYS LYS A . n 
A 1 197 LYS 197 197 197 LYS LYS A . n 
A 1 198 LEU 198 198 198 LEU LEU A . n 
A 1 199 LYS 199 199 199 LYS LYS A . n 
A 1 200 PHE 200 200 200 PHE PHE A . n 
A 1 201 PHE 201 201 201 PHE PHE A . n 
A 1 202 ASP 202 202 202 ASP ASP A . n 
A 1 203 GLU 203 203 203 GLU GLU A . n 
A 1 204 THR 204 204 204 THR THR A . n 
A 1 205 ILE 205 205 205 ILE ILE A . n 
A 1 206 PHE 206 206 206 PHE PHE A . n 
A 1 207 ALA 207 207 207 ALA ALA A . n 
A 1 208 GLU 208 208 208 GLU GLU A . n 
A 1 209 ASP 209 209 209 ASP ASP A . n 
A 1 210 ASP 210 210 210 ASP ASP A . n 
A 1 211 ILE 211 211 211 ILE ILE A . n 
A 1 212 ALA 212 212 212 ALA ALA A . n 
A 1 213 ASP 213 213 213 ASP ASP A . n 
A 1 214 TYR 214 214 214 TYR TYR A . n 
A 1 215 ILE 215 215 215 ILE ILE A . n 
A 1 216 ILE 216 216 216 ILE ILE A . n 
A 1 217 ALA 217 217 217 ALA ALA A . n 
A 1 218 LYS 218 218 218 LYS LYS A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 GLN 220 220 220 GLN GLN A . n 
A 1 221 HIS 221 221 221 HIS HIS A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 ASP 223 223 223 ASP ASP A . n 
A 1 224 THR 224 224 224 THR THR A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 ASN 226 226 226 ASN ASN A . n 
A 1 227 ILE 227 227 227 ILE ILE A . n 
A 1 228 GLU 228 228 228 GLU GLU A . n 
A 1 229 GLN 229 229 229 GLN GLN A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 LEU 231 231 231 LEU LEU A . n 
A 1 232 ILE 232 232 232 ILE ILE A . n 
A 1 233 ASN 233 233 233 ASN ASN A . n 
A 1 234 LYS 234 234 234 LYS LYS A . n 
A 1 235 ASN 235 235 235 ASN ASN A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 LYS 237 237 237 LYS LYS A . n 
A 1 238 MET 238 238 238 MET MET A . n 
A 1 239 VAL 239 239 239 VAL VAL A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 PHE 241 241 241 PHE PHE A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 SER 243 243 243 SER SER A . n 
A 1 244 LYS 244 244 244 LYS LYS A . n 
A 1 245 ASN 245 245 245 ASN ASN A . n 
A 1 246 THR 246 246 246 THR THR A . n 
A 1 247 LYS 247 247 247 LYS LYS A . n 
A 1 248 ASN 248 248 248 ASN ASN A . n 
A 1 249 ASP 249 249 249 ASP ASP A . n 
A 1 250 ASN 250 250 250 ASN ASN A . n 
A 1 251 ASN 251 251 251 ASN ASN A . n 
A 1 252 PHE 252 252 252 PHE PHE A . n 
A 1 253 THR 253 253 253 THR THR A . n 
A 1 254 TYR 254 254 254 TYR TYR A . n 
A 1 255 SER 255 255 255 SER SER A . n 
A 1 256 GLU 256 256 256 GLU GLU A . n 
A 1 257 TRP 257 257 257 TRP TRP A . n 
A 1 258 GLU 258 258 258 GLU GLU A . n 
A 1 259 SER 259 259 259 SER SER A . n 
A 1 260 ILE 260 260 260 ILE ILE A . n 
A 1 261 TYR 261 261 261 TYR TYR A . n 
A 1 262 ASN 262 262 262 ASN ASN A . n 
A 1 263 GLY 263 263 263 GLY GLY A . n 
A 1 264 THR 264 264 264 THR THR A . n 
A 1 265 TYR 265 265 265 TYR TYR A . n 
A 1 266 ARG 266 266 266 ARG ARG A . n 
A 1 267 ILE 267 267 267 ILE ILE A . n 
A 1 268 THR 268 268 268 THR THR A . n 
A 1 269 ASN 269 269 269 ASN ASN A . n 
A 1 270 LEU 270 270 270 LEU LEU A . n 
A 1 271 PRO 271 271 271 PRO PRO A . n 
A 1 272 SER 272 272 272 SER SER A . n 
A 1 273 LEU 273 273 273 LEU LEU A . n 
A 1 274 GLY 274 274 274 GLY GLY A . n 
A 1 275 ARG 275 275 275 ARG ARG A . n 
A 1 276 PHE 276 276 276 PHE PHE A . n 
A 1 277 LYS 277 277 277 LYS LYS A . n 
A 1 278 PHE 278 278 278 PHE PHE A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 LYS 280 280 280 LYS LYS A . n 
A 1 281 LYS 281 281 281 LYS LYS A . n 
A 1 282 ILE 282 282 282 ILE ILE A . n 
A 1 283 ALA 283 283 283 ALA ALA A . n 
A 1 284 GLU 284 284 284 GLU GLU A . n 
A 1 285 LYS 285 285 285 LYS LYS A . n 
A 1 286 SER 286 286 286 SER SER A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 SER 288 288 288 SER SER A . n 
A 1 289 GLY 289 289 289 GLY GLY A . n 
A 1 290 LYS 290 290 290 LYS LYS A . n 
A 1 291 VAL 291 291 291 VAL VAL A . n 
A 1 292 LYS 292 292 292 LYS LYS A . n 
A 1 293 GLU 293 293 293 GLU GLU A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 ASN 295 295 295 ASN ASN A . n 
A 1 296 ASN 296 296 296 ASN ASN A . n 
A 1 297 ILE 297 297 297 ILE ILE A . n 
A 1 298 VAL 298 298 298 VAL VAL A . n 
A 1 299 GLN 299 299 299 GLN GLN A . n 
A 1 300 ARG 300 300 300 ARG ARG A . n 
A 1 301 TYR 301 301 301 TYR TYR A . n 
A 1 302 SER 302 302 302 SER SER A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 GLY 304 304 304 GLY GLY A . n 
A 1 305 LEU 305 305 305 LEU LEU A . n 
A 1 306 ALA 306 306 306 ALA ALA A . n 
A 1 307 SER 307 307 307 SER SER A . n 
A 1 308 SER 308 308 308 SER SER A . n 
A 1 309 ASP 309 309 309 ASP ASP A . n 
A 1 310 LEU 310 310 310 LEU LEU A . n 
A 1 311 PRO 311 311 311 PRO PRO A . n 
A 1 312 PHE 312 312 312 PHE PHE A . n 
A 1 313 GLY 313 313 313 GLY GLY A . n 
A 1 314 VAL 314 314 314 VAL VAL A . n 
A 1 315 ILE 315 315 315 ILE ILE A . n 
A 1 316 ARG 316 316 316 ARG ARG A . n 
A 1 317 LYS 317 317 317 LYS LYS A . n 
A 1 318 GLU 318 318 318 GLU GLU A . n 
A 1 319 SER 319 319 319 SER SER A . n 
A 1 320 ARG 320 320 320 ARG ARG A . n 
A 1 321 ASN 321 321 321 ASN ASN A . n 
A 1 322 ASP 322 322 322 ASP ASP A . n 
A 1 323 PHE 323 323 323 PHE PHE A . n 
A 1 324 ILE 324 324 324 ILE ILE A . n 
A 1 325 ASN 325 325 325 ASN ASN A . n 
A 1 326 ASP 326 326 326 ASP ASP A . n 
A 1 327 VAL 327 327 327 VAL VAL A . n 
A 1 328 CYS 328 328 328 CYS CYS A . n 
A 1 329 LYS 329 329 329 LYS LYS A . n 
A 1 330 LEU 330 330 330 LEU LEU A . n 
A 1 331 TYR 331 331 331 TYR TYR A . n 
A 1 332 ASN 332 332 332 ASN ASN A . n 
A 1 333 ILE 333 333 333 ILE ILE A . n 
A 1 334 ASN 334 334 334 ASN ASN A . n 
A 1 335 ASP 335 335 335 ASP ASP A . n 
A 1 336 MET 336 336 336 MET MET A . n 
A 1 337 LYS 337 337 337 LYS LYS A . n 
A 1 338 ILE 338 338 338 ILE ILE A . n 
A 1 339 ILE 339 339 339 ILE ILE A . n 
A 1 340 LYS 340 340 340 LYS LYS A . n 
A 1 341 GLU 341 341 341 GLU GLU A . n 
A 1 342 LEU 342 342 342 LEU LEU A . n 
A 1 343 LYS 343 343 343 LYS LYS A . n 
A 1 344 GLU 344 344 344 GLU GLU A . n 
A 1 345 ASP 345 345 345 ASP ASP A . n 
A 1 346 ALA 346 346 346 ALA ALA A . n 
A 1 347 ASP 347 347 347 ASP ASP A . n 
A 1 348 LEU 348 348 348 LEU LEU A . n 
A 1 349 ILE 349 349 349 ILE ILE A . n 
A 1 350 VAL 350 350 350 VAL VAL A . n 
A 1 351 CYS 351 351 351 CYS CYS A . n 
A 1 352 MET 352 352 352 MET MET A . n 
A 1 353 LEU 353 353 353 LEU LEU A . n 
A 1 354 LYS 354 354 354 LYS LYS A . n 
A 1 355 GLY 355 355 355 GLY GLY A . n 
A 1 356 PHE 356 356 356 PHE PHE A . n 
A 1 357 LYS 357 357 357 LYS LYS A . n 
A 1 358 PRO 358 358 358 PRO PRO A . n 
A 1 359 ARG 359 359 359 ARG ARG A . n 
A 1 360 GLY 360 360 360 GLY GLY A . n 
A 1 361 ASP 361 361 361 ASP ASP A . n 
A 1 362 ASP 362 362 362 ASP ASP A . n 
A 1 363 ASN 363 363 363 ASN ASN A . n 
A 1 364 ARG 364 364 364 ARG ARG A . n 
A 1 365 PRO 365 365 365 PRO PRO A . n 
A 1 366 ASP 366 366 366 ASP ASP A . n 
A 1 367 ARG 367 367 367 ARG ARG A . n 
A 1 368 GLY 368 368 368 GLY GLY A . n 
A 1 369 ALA 369 369 369 ALA ALA A . n 
A 1 370 LEU 370 370 370 LEU LEU A . n 
A 1 371 PRO 371 371 371 PRO PRO A . n 
A 1 372 LEU 372 372 372 LEU LEU A . n 
A 1 373 VAL 373 373 373 VAL VAL A . n 
A 1 374 ALA 374 374 374 ALA ALA A . n 
A 1 375 MET 375 375 375 MET MET A . n 
A 1 376 LEU 376 376 376 LEU LEU A . n 
A 1 377 ALA 377 377 377 ALA ALA A . n 
A 1 378 GLY 378 378 378 GLY GLY A . n 
A 1 379 GLU 379 379 379 GLU GLU A . n 
A 1 380 ASN 380 380 380 ASN ASN A . n 
A 1 381 ALA 381 381 381 ALA ALA A . n 
A 1 382 GLN 382 382 382 GLN GLN A . n 
A 1 383 ILE 383 383 383 ILE ILE A . n 
A 1 384 PHE 384 384 384 PHE PHE A . n 
A 1 385 THR 385 385 385 THR THR A . n 
A 1 386 PHE 386 386 386 PHE PHE A . n 
A 1 387 ILE 387 387 387 ILE ILE A . n 
A 1 388 TYR 388 388 388 TYR TYR A . n 
A 1 389 GLY 389 389 389 GLY GLY A . n 
A 1 390 PRO 390 390 390 PRO PRO A . n 
A 1 391 LEU 391 391 391 LEU LEU A . n 
A 1 392 ILE 392 392 392 ILE ILE A . n 
A 1 393 LYS 393 393 393 LYS LYS A . n 
A 1 394 GLY 394 394 394 GLY GLY A . n 
A 1 395 ALA 395 395 395 ALA ALA A . n 
A 1 396 ILE 396 396 396 ILE ILE A . n 
A 1 397 ASN 397 397 397 ASN ASN A . n 
A 1 398 LEU 398 398 398 LEU LEU A . n 
A 1 399 ILE 399 399 399 ILE ILE A . n 
A 1 400 ASP 400 400 400 ASP ASP A . n 
A 1 401 GLN 401 401 401 GLN GLN A . n 
A 1 402 ASP 402 402 402 ASP ASP A . n 
A 1 403 ILE 403 403 403 ILE ILE A . n 
A 1 404 ASN 404 404 404 ASN ASN A . n 
A 1 405 LYS 405 405 405 LYS LYS A . n 
A 1 406 LEU 406 406 406 LEU LEU A . n 
A 1 407 ALA 407 407 407 ALA ALA A . n 
A 1 408 LYS 408 408 408 LYS LYS A . n 
A 1 409 ARG 409 409 409 ARG ARG A . n 
A 1 410 ASN 410 410 410 ASN ASN A . n 
A 1 411 GLY 411 411 411 GLY GLY A . n 
A 1 412 LEU 412 412 412 LEU LEU A . n 
A 1 413 TRP 413 413 413 TRP TRP A . n 
A 1 414 LYS 414 414 414 LYS LYS A . n 
A 1 415 SER 415 415 415 SER SER A . n 
A 1 416 PHE 416 416 416 PHE PHE A . n 
A 1 417 VAL 417 417 417 VAL VAL A . n 
A 1 418 SER 418 418 418 SER SER A . n 
A 1 419 LEU 419 419 419 LEU LEU A . n 
A 1 420 SER 420 420 420 SER SER A . n 
A 1 421 ASP 421 421 421 ASP ASP A . n 
A 1 422 PHE 422 422 422 PHE PHE A . n 
A 1 423 ILE 423 423 423 ILE ILE A . n 
A 1 424 VAL 424 424 424 VAL VAL A . n 
A 1 425 LEU 425 425 425 LEU LEU A . n 
A 1 426 ASP 426 426 426 ASP ASP A . n 
A 1 427 CYS 427 427 427 CYS CYS A . n 
A 1 428 PRO 428 428 428 PRO PRO A . n 
A 1 429 ILE 429 429 429 ILE ILE A . n 
A 1 430 ILE 430 430 430 ILE ILE A . n 
A 1 431 GLY 431 431 431 GLY GLY A . n 
A 1 432 GLU 432 432 432 GLU GLU A . n 
A 1 433 SER 433 433 433 SER SER A . n 
A 1 434 TYR 434 434 434 TYR TYR A . n 
A 1 435 ASN 435 435 435 ASN ASN A . n 
A 1 436 GLU 436 436 436 GLU GLU A . n 
A 1 437 PHE 437 437 437 PHE PHE A . n 
A 1 438 ARG 438 438 438 ARG ARG A . n 
A 1 439 LEU 439 439 439 LEU LEU A . n 
A 1 440 ILE 440 440 440 ILE ILE A . n 
A 1 441 ILE 441 441 441 ILE ILE A . n 
A 1 442 ASN 442 442 442 ASN ASN A . n 
A 1 443 LYS 443 443 443 LYS LYS A . n 
A 1 444 ASN 444 444 444 ASN ASN A . n 
A 1 445 ASN 445 445 445 ASN ASN A . n 
A 1 446 LYS 446 446 446 LYS LYS A . n 
A 1 447 GLU 447 447 447 GLU GLU A . n 
A 1 448 SER 448 448 448 SER SER A . n 
A 1 449 ILE 449 449 449 ILE ILE A . n 
A 1 450 LEU 450 450 450 LEU LEU A . n 
A 1 451 ARG 451 451 451 ARG ARG A . n 
A 1 452 LYS 452 452 452 LYS LYS A . n 
A 1 453 THR 453 453 453 THR THR A . n 
A 1 454 SER 454 454 454 SER SER A . n 
A 1 455 LYS 455 455 455 LYS LYS A . n 
A 1 456 GLN 456 456 456 GLN GLN A . n 
A 1 457 GLN 457 457 457 GLN GLN A . n 
A 1 458 ASN 458 458 458 ASN ASN A . n 
A 1 459 ILE 459 459 459 ILE ILE A . n 
A 1 460 LEU 460 460 460 LEU LEU A . n 
A 1 461 VAL 461 461 461 VAL VAL A . n 
A 1 462 ASP 462 462 462 ASP ASP A . n 
A 1 463 PRO 463 463 463 PRO PRO A . n 
A 1 464 THR 464 464 464 THR THR A . n 
A 1 465 PRO 465 465 465 PRO PRO A . n 
A 1 466 ASN 466 466 466 ASN ASN A . n 
A 1 467 HIS 467 467 467 HIS HIS A . n 
A 1 468 TYR 468 468 468 TYR TYR A . n 
A 1 469 GLN 469 469 469 GLN GLN A . n 
A 1 470 GLU 470 470 470 GLU GLU A . n 
A 1 471 ASN 471 471 471 ASN ASN A . n 
A 1 472 ASP 472 472 472 ASP ASP A . n 
A 1 473 VAL 473 473 473 VAL VAL A . n 
A 1 474 ASP 474 474 474 ASP ASP A . n 
A 1 475 THR 475 475 475 THR THR A . n 
A 1 476 VAL 476 476 476 VAL VAL A . n 
A 1 477 ILE 477 477 477 ILE ILE A . n 
A 1 478 TYR 478 478 478 TYR TYR A . n 
A 1 479 SER 479 479 479 SER SER A . n 
A 1 480 ILE 480 480 480 ILE ILE A . n 
A 1 481 PHE 481 481 481 PHE PHE A . n 
A 1 482 LYS 482 482 482 LYS LYS A . n 
A 1 483 TYR 483 483 483 TYR TYR A . n 
A 1 484 ILE 484 484 484 ILE ILE A . n 
A 1 485 VAL 485 485 485 VAL VAL A . n 
A 1 486 PRO 486 486 486 PRO PRO A . n 
A 1 487 ASN 487 487 487 ASN ASN A . n 
A 1 488 CYS 488 488 488 CYS CYS A . n 
A 1 489 PHE 489 489 489 PHE PHE A . n 
A 1 490 SER 490 490 490 SER SER A . n 
A 1 491 GLY 491 491 491 GLY GLY A . n 
A 1 492 MET 492 492 492 MET MET A . n 
A 1 493 CYS 493 493 493 CYS CYS A . n 
A 1 494 ASN 494 494 494 ASN ASN A . n 
A 1 495 PRO 495 495 495 PRO PRO A . n 
A 1 496 PRO 496 496 496 PRO PRO A . n 
A 1 497 GLY 497 497 497 GLY GLY A . n 
A 1 498 GLY 498 498 498 GLY GLY A . n 
A 1 499 ASP 499 499 499 ASP ASP A . n 
A 1 500 TRP 500 500 500 TRP TRP A . n 
A 1 501 SER 501 501 501 SER SER A . n 
A 1 502 GLY 502 502 502 GLY GLY A . n 
A 1 503 LEU 503 503 503 LEU LEU A . n 
A 1 504 SER 504 504 504 SER SER A . n 
A 1 505 ILE 505 505 505 ILE ILE A . n 
A 1 506 ILE 506 506 506 ILE ILE A . n 
A 1 507 ARG 507 507 507 ARG ARG A . n 
A 1 508 ASN 508 508 508 ASN ASN A . n 
A 1 509 GLY 509 509 509 GLY GLY A . n 
A 1 510 HIS 510 510 510 HIS HIS A . n 
A 1 511 GLU 511 511 511 GLU GLU A . n 
A 1 512 PHE 512 512 512 PHE PHE A . n 
A 1 513 ARG 513 513 513 ARG ARG A . n 
A 1 514 TRP 514 514 514 TRP TRP A . n 
A 1 515 LEU 515 515 515 LEU LEU A . n 
A 1 516 SER 516 516 516 SER SER A . n 
A 1 517 LEU 517 517 517 LEU LEU A . n 
A 1 518 PRO 518 518 518 PRO PRO A . n 
A 1 519 ARG 519 519 519 ARG ARG A . n 
A 1 520 VAL 520 520 520 VAL VAL A . n 
A 1 521 SER 521 521 521 SER SER A . n 
A 1 522 GLU 522 522 522 GLU GLU A . n 
A 1 523 ASN 523 523 523 ASN ASN A . n 
A 1 524 GLY 524 524 524 GLY GLY A . n 
A 1 525 LYS 525 525 525 LYS LYS A . n 
A 1 526 ARG 526 526 526 ARG ARG A . n 
A 1 527 PRO 527 527 527 PRO PRO A . n 
A 1 528 ASP 528 528 528 ASP ASP A . n 
A 1 529 HIS 529 529 529 HIS HIS A . n 
A 1 530 VAL 530 530 530 VAL VAL A . n 
A 1 531 ILE 531 531 531 ILE ILE A . n 
A 1 532 GLN 532 532 532 GLN GLN A . n 
A 1 533 ILE 533 533 533 ILE ILE A . n 
A 1 534 LEU 534 534 534 LEU LEU A . n 
A 1 535 ASP 535 535 535 ASP ASP A . n 
A 1 536 LEU 536 536 536 LEU LEU A . n 
A 1 537 PHE 537 537 537 PHE PHE A . n 
A 1 538 GLU 538 538 538 GLU GLU A . n 
A 1 539 LYS 539 539 539 LYS LYS A . n 
A 1 540 PRO 540 540 540 PRO PRO A . n 
A 1 541 LEU 541 541 541 LEU LEU A . n 
A 1 542 LEU 542 542 542 LEU LEU A . n 
A 1 543 LEU 543 543 543 LEU LEU A . n 
A 1 544 SER 544 544 544 SER SER A . n 
A 1 545 ILE 545 545 545 ILE ILE A . n 
A 1 546 GLU 546 546 546 GLU GLU A . n 
A 1 547 SER 547 547 547 SER SER A . n 
A 1 548 LYS 548 548 548 LYS LYS A . n 
A 1 549 GLU 549 549 549 GLU GLU A . n 
A 1 550 LYS 550 550 550 LYS LYS A . n 
A 1 551 PRO 551 551 551 PRO PRO A . n 
A 1 552 ASN 552 552 552 ASN ASN A . n 
A 1 553 ASP 553 553 553 ASP ASP A . n 
A 1 554 LEU 554 554 554 LEU LEU A . n 
A 1 555 GLU 555 555 555 GLU GLU A . n 
A 1 556 PRO 556 556 556 PRO PRO A . n 
A 1 557 LYS 557 557 557 LYS LYS A . n 
A 1 558 ILE 558 558 558 ILE ILE A . n 
A 1 559 GLY 559 559 559 GLY GLY A . n 
A 1 560 VAL 560 560 560 VAL VAL A . n 
A 1 561 GLN 561 561 561 GLN GLN A . n 
A 1 562 LEU 562 562 562 LEU LEU A . n 
A 1 563 ILE 563 563 563 ILE ILE A . n 
A 1 564 LYS 564 564 564 LYS LYS A . n 
A 1 565 TYR 565 565 565 TYR TYR A . n 
A 1 566 ILE 566 566 566 ILE ILE A . n 
A 1 567 GLU 567 567 567 GLU GLU A . n 
A 1 568 TYR 568 568 568 TYR TYR A . n 
A 1 569 LEU 569 569 569 LEU LEU A . n 
A 1 570 PHE 570 570 570 PHE PHE A . n 
A 1 571 ASP 571 571 571 ASP ASP A . n 
A 1 572 PHE 572 572 572 PHE PHE A . n 
A 1 573 THR 573 573 573 THR THR A . n 
A 1 574 PRO 574 574 574 PRO PRO A . n 
A 1 575 SER 575 575 575 SER SER A . n 
A 1 576 VAL 576 576 576 VAL VAL A . n 
A 1 577 GLN 577 577 577 GLN GLN A . n 
A 1 578 ARG 578 578 578 ARG ARG A . n 
A 1 579 LYS 579 579 579 LYS LYS A . n 
A 1 580 ILE 580 580 580 ILE ILE A . n 
A 1 581 ALA 581 581 581 ALA ALA A . n 
A 1 582 GLY 582 582 582 GLY GLY A . n 
A 1 583 GLY 583 583 583 GLY GLY A . n 
A 1 584 ASN 584 584 584 ASN ASN A . n 
A 1 585 TRP 585 585 585 TRP TRP A . n 
A 1 586 GLU 586 586 586 GLU GLU A . n 
A 1 587 PHE 587 587 587 PHE PHE A . n 
A 1 588 GLY 588 588 588 GLY GLY A . n 
A 1 589 ASN 589 589 589 ASN ASN A . n 
A 1 590 LYS 590 590 590 LYS LYS A . n 
A 1 591 SER 591 591 591 SER SER A . n 
A 1 592 LEU 592 592 592 LEU LEU A . n 
A 1 593 VAL 593 593 593 VAL VAL A . n 
A 1 594 PRO 594 594 594 PRO PRO A . n 
A 1 595 ASN 595 595 595 ASN ASN A . n 
A 1 596 ASP 596 596 596 ASP ASP A . n 
A 1 597 PHE 597 597 597 PHE PHE A . n 
A 1 598 ILE 598 598 598 ILE ILE A . n 
A 1 599 LEU 599 599 599 LEU LEU A . n 
A 1 600 LEU 600 600 600 LEU LEU A . n 
A 1 601 SER 601 601 601 SER SER A . n 
A 1 602 ALA 602 602 602 ALA ALA A . n 
A 1 603 GLY 603 603 603 GLY GLY A . n 
A 1 604 ALA 604 604 604 ALA ALA A . n 
A 1 605 PHE 605 605 605 PHE PHE A . n 
A 1 606 ILE 606 606 606 ILE ILE A . n 
A 1 607 ASP 607 607 607 ASP ASP A . n 
A 1 608 TYR 608 608 608 TYR TYR A . n 
A 1 609 ASP 609 609 609 ASP ASP A . n 
A 1 610 ASN 610 610 610 ASN ASN A . n 
A 1 611 LEU 611 611 611 LEU LEU A . n 
A 1 612 THR 612 612 612 THR THR A . n 
A 1 613 GLU 613 613 613 GLU GLU A . n 
A 1 614 ASN 614 614 614 ASN ASN A . n 
A 1 615 ASP 615 615 615 ASP ASP A . n 
A 1 616 TYR 616 616 616 TYR TYR A . n 
A 1 617 GLU 617 617 617 GLU GLU A . n 
A 1 618 LYS 618 618 618 LYS LYS A . n 
A 1 619 ILE 619 619 619 ILE ILE A . n 
A 1 620 PHE 620 620 620 PHE PHE A . n 
A 1 621 GLU 621 621 621 GLU GLU A . n 
A 1 622 VAL 622 622 622 VAL VAL A . n 
A 1 623 THR 623 623 623 THR THR A . n 
A 1 624 GLY 624 624 624 GLY GLY A . n 
A 1 625 CYS 625 625 625 CYS CYS A . n 
A 1 626 ASP 626 626 626 ASP ASP A . n 
A 1 627 LEU 627 627 627 LEU LEU A . n 
A 1 628 LEU 628 628 628 LEU LEU A . n 
A 1 629 ILE 629 629 629 ILE ILE A . n 
A 1 630 ALA 630 630 630 ALA ALA A . n 
A 1 631 ILE 631 631 631 ILE ILE A . n 
A 1 632 LYS 632 632 632 LYS LYS A . n 
A 1 633 ASN 633 633 633 ASN ASN A . n 
A 1 634 GLN 634 634 634 GLN GLN A . n 
A 1 635 ASN 635 635 635 ASN ASN A . n 
A 1 636 ASN 636 636 636 ASN ASN A . n 
A 1 637 PRO 637 637 637 PRO PRO A . n 
A 1 638 GLN 638 638 638 GLN GLN A . n 
A 1 639 LYS 639 639 639 LYS LYS A . n 
A 1 640 TRP 640 640 640 TRP TRP A . n 
A 1 641 VAL 641 641 641 VAL VAL A . n 
A 1 642 ILE 642 642 642 ILE ILE A . n 
A 1 643 LYS 643 643 643 LYS LYS A . n 
A 1 644 PHE 644 644 644 PHE PHE A . n 
A 1 645 LYS 645 645 645 LYS LYS A . n 
A 1 646 PRO 646 646 646 PRO PRO A . n 
A 1 647 LYS 647 647 647 LYS LYS A . n 
A 1 648 ASN 648 648 648 ASN ASN A . n 
A 1 649 THR 649 649 649 THR THR A . n 
A 1 650 ILE 650 650 650 ILE ILE A . n 
A 1 651 ALA 651 651 651 ALA ALA A . n 
A 1 652 GLU 652 652 652 GLU GLU A . n 
A 1 653 LYS 653 653 653 LYS LYS A . n 
A 1 654 LEU 654 654 654 LEU LEU A . n 
A 1 655 VAL 655 655 655 VAL VAL A . n 
A 1 656 ASN 656 656 656 ASN ASN A . n 
A 1 657 TYR 657 657 657 TYR TYR A . n 
A 1 658 ILE 658 658 658 ILE ILE A . n 
A 1 659 LYS 659 659 659 LYS LYS A . n 
A 1 660 LEU 660 660 660 LEU LEU A . n 
A 1 661 ASN 661 661 661 ASN ASN A . n 
A 1 662 PHE 662 662 662 PHE PHE A . n 
A 1 663 LYS 663 663 663 LYS LYS A . n 
A 1 664 SER 664 664 664 SER SER A . n 
A 1 665 ASN 665 665 665 ASN ASN A . n 
A 1 666 ILE 666 666 666 ILE ILE A . n 
A 1 667 PHE 667 667 667 PHE PHE A . n 
A 1 668 ASP 668 668 668 ASP ASP A . n 
A 1 669 THR 669 669 669 THR THR A . n 
A 1 670 GLY 670 670 670 GLY GLY A . n 
A 1 671 PHE 671 671 671 PHE PHE A . n 
A 1 672 PHE 672 672 672 PHE PHE A . n 
A 1 673 HIS 673 673 673 HIS HIS A . n 
A 1 674 ILE 674 674 674 ILE ILE A . n 
A 1 675 GLU 675 675 675 GLU GLU A . n 
A 1 676 GLY 676 676 676 GLY GLY A . n 
B 2 1   DG  1   1   1   DG  DG  E . n 
B 2 2   DT  2   2   2   DT  DT  E . n 
B 2 3   DC  3   3   3   DC  DC  E . n 
B 2 4   DT  4   4   4   DT  DT  E . n 
B 2 5   DG  5   5   5   DG  DG  E . n 
B 2 6   DC  6   6   6   DC  DC  E . n 
B 2 7   DA  7   7   7   DA  DA  E . n 
B 2 8   DT  8   8   8   DT  DT  E . n 
B 2 9   DT  9   9   9   DT  DT  E . n 
B 2 10  DC  10  10  10  DC  DC  E . n 
B 2 11  DC  11  11  11  DC  DC  E . n 
B 2 12  DT  12  12  12  DT  DT  E . n 
B 2 13  DC  13  13  13  DC  DC  E . n 
C 3 1   DG  1   1   1   DG  DG  F . n 
C 3 2   DA  2   2   2   DA  DA  F . n 
C 3 3   DG  3   3   3   DG  DG  F . n 
C 3 4   DG  4   4   4   DG  DG  F . n 
C 3 5   DA  5   5   5   DA  DA  F . n 
C 3 6   DA  6   6   6   DA  DA  F . n 
C 3 7   DT  7   7   7   DT  DT  F . n 
C 3 8   DG  8   8   8   DG  DG  F . n 
C 3 9   DC  9   9   9   DC  DC  F . n 
C 3 10  DA  10  10  10  DA  DA  F . n 
C 3 11  DG  11  11  11  DG  DG  F . n 
C 3 12  DA  12  12  12  DA  DA  F . n 
C 3 13  DC  13  13  13  DC  DC  F . n 
D 3 1   DG  1   1   1   DG  DG  U . n 
D 3 2   DA  2   2   2   DA  DA  U . n 
D 3 3   DG  3   3   3   DG  DG  U . n 
D 3 4   DG  4   4   4   DG  DG  U . n 
D 3 5   DA  5   5   5   DA  DA  U . n 
D 3 6   DA  6   6   6   DA  DA  U . n 
D 3 7   DT  7   7   7   DT  DT  U . n 
D 3 8   DG  8   8   8   DG  DG  U . n 
D 3 9   DC  9   9   9   DC  DC  U . n 
D 3 10  DA  10  10  10  DA  DA  U . n 
D 3 11  DG  11  11  11  DG  DG  U . n 
D 3 12  DA  12  12  12  DA  DA  U . n 
D 3 13  DC  13  13  13  DC  DC  U . n 
E 2 1   DG  1   1   1   DG  DG  V . n 
E 2 2   DT  2   2   2   DT  DT  V . n 
E 2 3   DC  3   3   3   DC  DC  V . n 
E 2 4   DT  4   4   4   DT  DT  V . n 
E 2 5   DG  5   5   5   DG  DG  V . n 
E 2 6   DC  6   6   6   DC  DC  V . n 
E 2 7   DA  7   7   7   DA  DA  V . n 
E 2 8   DT  8   8   8   DT  DT  V . n 
E 2 9   DT  9   9   9   DT  DT  V . n 
E 2 10  DC  10  10  10  DC  DC  V . n 
E 2 11  DC  11  11  11  DC  DC  V . n 
E 2 12  DT  12  12  12  DT  DT  V . n 
E 2 13  DC  13  13  13  DC  DC  V . n 
F 1 1   MET 1   1   1   MET MET Z . n 
F 1 2   ASN 2   2   2   ASN ASN Z . n 
F 1 3   VAL 3   3   3   VAL VAL Z . n 
F 1 4   PHE 4   4   4   PHE PHE Z . n 
F 1 5   ARG 5   5   5   ARG ARG Z . n 
F 1 6   ILE 6   6   6   ILE ILE Z . n 
F 1 7   HIS 7   7   7   HIS HIS Z . n 
F 1 8   GLY 8   8   8   GLY GLY Z . n 
F 1 9   ASP 9   9   9   ASP ASP Z . n 
F 1 10  ASN 10  10  10  ASN ASN Z . n 
F 1 11  ILE 11  11  11  ILE ILE Z . n 
F 1 12  ILE 12  12  12  ILE ILE Z . n 
F 1 13  GLU 13  13  13  GLU GLU Z . n 
F 1 14  CYS 14  14  14  CYS CYS Z . n 
F 1 15  GLU 15  15  15  GLU GLU Z . n 
F 1 16  ARG 16  16  16  ARG ARG Z . n 
F 1 17  VAL 17  17  17  VAL VAL Z . n 
F 1 18  ILE 18  18  18  ILE ILE Z . n 
F 1 19  ASP 19  19  19  ASP ASP Z . n 
F 1 20  LEU 20  20  20  LEU LEU Z . n 
F 1 21  ILE 21  21  21  ILE ILE Z . n 
F 1 22  LEU 22  22  22  LEU LEU Z . n 
F 1 23  SER 23  23  23  SER SER Z . n 
F 1 24  LYS 24  24  24  LYS LYS Z . n 
F 1 25  ILE 25  25  25  ILE ILE Z . n 
F 1 26  ASN 26  26  26  ASN ASN Z . n 
F 1 27  PRO 27  27  27  PRO PRO Z . n 
F 1 28  GLN 28  28  28  GLN GLN Z . n 
F 1 29  LYS 29  29  29  LYS LYS Z . n 
F 1 30  VAL 30  30  30  VAL VAL Z . n 
F 1 31  LYS 31  31  31  LYS LYS Z . n 
F 1 32  ARG 32  32  32  ARG ARG Z . n 
F 1 33  GLY 33  33  33  GLY GLY Z . n 
F 1 34  PHE 34  34  34  PHE PHE Z . n 
F 1 35  ILE 35  35  35  ILE ILE Z . n 
F 1 36  SER 36  36  36  SER SER Z . n 
F 1 37  LEU 37  37  37  LEU LEU Z . n 
F 1 38  SER 38  38  38  SER SER Z . n 
F 1 39  CYS 39  39  39  CYS CYS Z . n 
F 1 40  PRO 40  40  40  PRO PRO Z . n 
F 1 41  PHE 41  41  41  PHE PHE Z . n 
F 1 42  ILE 42  42  42  ILE ILE Z . n 
F 1 43  GLU 43  43  43  GLU GLU Z . n 
F 1 44  ILE 44  44  44  ILE ILE Z . n 
F 1 45  ILE 45  45  45  ILE ILE Z . n 
F 1 46  PHE 46  46  46  PHE PHE Z . n 
F 1 47  LYS 47  47  47  LYS LYS Z . n 
F 1 48  GLU 48  48  48  GLU GLU Z . n 
F 1 49  GLY 49  49  49  GLY GLY Z . n 
F 1 50  HIS 50  50  50  HIS HIS Z . n 
F 1 51  ASP 51  51  51  ASP ASP Z . n 
F 1 52  TYR 52  52  52  TYR TYR Z . n 
F 1 53  PHE 53  53  53  PHE PHE Z . n 
F 1 54  HIS 54  54  54  HIS HIS Z . n 
F 1 55  TRP 55  55  55  TRP TRP Z . n 
F 1 56  ARG 56  56  56  ARG ARG Z . n 
F 1 57  PHE 57  57  57  PHE PHE Z . n 
F 1 58  ASP 58  58  58  ASP ASP Z . n 
F 1 59  MET 59  59  59  MET MET Z . n 
F 1 60  PHE 60  60  60  PHE PHE Z . n 
F 1 61  PRO 61  61  61  PRO PRO Z . n 
F 1 62  GLY 62  62  62  GLY GLY Z . n 
F 1 63  PHE 63  63  63  PHE PHE Z . n 
F 1 64  ASN 64  64  64  ASN ASN Z . n 
F 1 65  LYS 65  65  65  LYS LYS Z . n 
F 1 66  ASN 66  66  66  ASN ASN Z . n 
F 1 67  THR 67  67  67  THR THR Z . n 
F 1 68  ASN 68  68  68  ASN ASN Z . n 
F 1 69  ASP 69  69  69  ASP ASP Z . n 
F 1 70  ARG 70  70  70  ARG ARG Z . n 
F 1 71  TRP 71  71  71  TRP TRP Z . n 
F 1 72  ASN 72  72  72  ASN ASN Z . n 
F 1 73  SER 73  73  73  SER SER Z . n 
F 1 74  ASN 74  74  74  ASN ASN Z . n 
F 1 75  ILE 75  75  75  ILE ILE Z . n 
F 1 76  LEU 76  76  76  LEU LEU Z . n 
F 1 77  ASP 77  77  77  ASP ASP Z . n 
F 1 78  LEU 78  78  78  LEU LEU Z . n 
F 1 79  LEU 79  79  79  LEU LEU Z . n 
F 1 80  SER 80  80  80  SER SER Z . n 
F 1 81  GLN 81  81  81  GLN GLN Z . n 
F 1 82  LYS 82  82  82  LYS LYS Z . n 
F 1 83  GLY 83  83  83  GLY GLY Z . n 
F 1 84  SER 84  84  84  SER SER Z . n 
F 1 85  PHE 85  85  85  PHE PHE Z . n 
F 1 86  LEU 86  86  86  LEU LEU Z . n 
F 1 87  TYR 87  87  87  TYR TYR Z . n 
F 1 88  GLU 88  88  88  GLU GLU Z . n 
F 1 89  THR 89  89  89  THR THR Z . n 
F 1 90  PRO 90  90  90  PRO PRO Z . n 
F 1 91  ASP 91  91  91  ASP ASP Z . n 
F 1 92  VAL 92  92  92  VAL VAL Z . n 
F 1 93  ILE 93  93  93  ILE ILE Z . n 
F 1 94  ILE 94  94  94  ILE ILE Z . n 
F 1 95  THR 95  95  95  THR THR Z . n 
F 1 96  SER 96  96  96  SER SER Z . n 
F 1 97  LEU 97  97  97  LEU LEU Z . n 
F 1 98  ASN 98  98  98  ASN ASN Z . n 
F 1 99  ASN 99  99  99  ASN ASN Z . n 
F 1 100 GLY 100 100 100 GLY GLY Z . n 
F 1 101 LYS 101 101 101 LYS LYS Z . n 
F 1 102 GLU 102 102 102 GLU GLU Z . n 
F 1 103 GLU 103 103 103 GLU GLU Z . n 
F 1 104 ILE 104 104 104 ILE ILE Z . n 
F 1 105 LEU 105 105 105 LEU LEU Z . n 
F 1 106 MET 106 106 106 MET MET Z . n 
F 1 107 ALA 107 107 107 ALA ALA Z . n 
F 1 108 ILE 108 108 108 ILE ILE Z . n 
F 1 109 GLU 109 109 109 GLU GLU Z . n 
F 1 110 PHE 110 110 110 PHE PHE Z . n 
F 1 111 CYS 111 111 111 CYS CYS Z . n 
F 1 112 SER 112 112 112 SER SER Z . n 
F 1 113 ALA 113 113 113 ALA ALA Z . n 
F 1 114 LEU 114 114 114 LEU LEU Z . n 
F 1 115 GLN 115 115 115 GLN GLN Z . n 
F 1 116 ALA 116 116 116 ALA ALA Z . n 
F 1 117 GLY 117 117 117 GLY GLY Z . n 
F 1 118 ASN 118 118 118 ASN ASN Z . n 
F 1 119 GLN 119 119 119 GLN GLN Z . n 
F 1 120 ALA 120 120 120 ALA ALA Z . n 
F 1 121 TRP 121 121 121 TRP TRP Z . n 
F 1 122 GLN 122 122 122 GLN GLN Z . n 
F 1 123 ARG 123 123 123 ARG ARG Z . n 
F 1 124 SER 124 124 124 SER SER Z . n 
F 1 125 GLY 125 125 125 GLY GLY Z . n 
F 1 126 ARG 126 126 126 ARG ARG Z . n 
F 1 127 ALA 127 127 127 ALA ALA Z . n 
F 1 128 TYR 128 128 128 TYR TYR Z . n 
F 1 129 SER 129 129 129 SER SER Z . n 
F 1 130 VAL 130 130 130 VAL VAL Z . n 
F 1 131 GLY 131 131 131 GLY GLY Z . n 
F 1 132 ARG 132 132 132 ARG ARG Z . n 
F 1 133 THR 133 133 133 THR THR Z . n 
F 1 134 GLY 134 134 134 GLY GLY Z . n 
F 1 135 TYR 135 135 135 TYR TYR Z . n 
F 1 136 PRO 136 136 136 PRO PRO Z . n 
F 1 137 TYR 137 137 137 TYR TYR Z . n 
F 1 138 ILE 138 138 138 ILE ILE Z . n 
F 1 139 TYR 139 139 139 TYR TYR Z . n 
F 1 140 ILE 140 140 140 ILE ILE Z . n 
F 1 141 VAL 141 141 141 VAL VAL Z . n 
F 1 142 ASP 142 142 142 ASP ASP Z . n 
F 1 143 PHE 143 143 143 PHE PHE Z . n 
F 1 144 VAL 144 144 144 VAL VAL Z . n 
F 1 145 LYS 145 145 145 LYS LYS Z . n 
F 1 146 TYR 146 146 146 TYR TYR Z . n 
F 1 147 GLU 147 147 147 GLU GLU Z . n 
F 1 148 LEU 148 148 148 LEU LEU Z . n 
F 1 149 ASN 149 149 149 ASN ASN Z . n 
F 1 150 ASN 150 150 150 ASN ASN Z . n 
F 1 151 SER 151 151 151 SER SER Z . n 
F 1 152 ASP 152 152 152 ASP ASP Z . n 
F 1 153 ARG 153 153 153 ARG ARG Z . n 
F 1 154 SER 154 154 154 SER SER Z . n 
F 1 155 ARG 155 155 155 ARG ARG Z . n 
F 1 156 LYS 156 156 156 LYS LYS Z . n 
F 1 157 ASN 157 157 157 ASN ASN Z . n 
F 1 158 LEU 158 158 158 LEU LEU Z . n 
F 1 159 ARG 159 159 159 ARG ARG Z . n 
F 1 160 PHE 160 160 160 PHE PHE Z . n 
F 1 161 PRO 161 161 161 PRO PRO Z . n 
F 1 162 ASN 162 162 162 ASN ASN Z . n 
F 1 163 PRO 163 163 163 PRO PRO Z . n 
F 1 164 ALA 164 164 164 ALA ALA Z . n 
F 1 165 ILE 165 165 165 ILE ILE Z . n 
F 1 166 PRO 166 166 166 PRO PRO Z . n 
F 1 167 TYR 167 167 167 TYR TYR Z . n 
F 1 168 SER 168 168 168 SER SER Z . n 
F 1 169 TYR 169 169 169 TYR TYR Z . n 
F 1 170 ILE 170 170 170 ILE ILE Z . n 
F 1 171 SER 171 171 171 SER SER Z . n 
F 1 172 HIS 172 172 172 HIS HIS Z . n 
F 1 173 SER 173 173 173 SER SER Z . n 
F 1 174 LYS 174 174 174 LYS LYS Z . n 
F 1 175 ASN 175 175 175 ASN ASN Z . n 
F 1 176 THR 176 176 176 THR THR Z . n 
F 1 177 GLY 177 177 177 GLY GLY Z . n 
F 1 178 ASN 178 178 178 ASN ASN Z . n 
F 1 179 PHE 179 179 179 PHE PHE Z . n 
F 1 180 ILE 180 180 180 ILE ILE Z . n 
F 1 181 VAL 181 181 181 VAL VAL Z . n 
F 1 182 GLN 182 182 182 GLN GLN Z . n 
F 1 183 ALA 183 183 183 ALA ALA Z . n 
F 1 184 TYR 184 184 184 TYR TYR Z . n 
F 1 185 PHE 185 185 185 PHE PHE Z . n 
F 1 186 ARG 186 186 186 ARG ARG Z . n 
F 1 187 GLY 187 187 187 GLY GLY Z . n 
F 1 188 GLU 188 188 188 GLU GLU Z . n 
F 1 189 GLU 189 189 189 GLU GLU Z . n 
F 1 190 TYR 190 190 190 TYR TYR Z . n 
F 1 191 GLN 191 191 191 GLN GLN Z . n 
F 1 192 PRO 192 192 192 PRO PRO Z . n 
F 1 193 LYS 193 193 193 LYS LYS Z . n 
F 1 194 TYR 194 194 194 TYR TYR Z . n 
F 1 195 ASP 195 195 195 ASP ASP Z . n 
F 1 196 LYS 196 196 196 LYS LYS Z . n 
F 1 197 LYS 197 197 197 LYS LYS Z . n 
F 1 198 LEU 198 198 198 LEU LEU Z . n 
F 1 199 LYS 199 199 199 LYS LYS Z . n 
F 1 200 PHE 200 200 200 PHE PHE Z . n 
F 1 201 PHE 201 201 201 PHE PHE Z . n 
F 1 202 ASP 202 202 202 ASP ASP Z . n 
F 1 203 GLU 203 203 203 GLU GLU Z . n 
F 1 204 THR 204 204 204 THR THR Z . n 
F 1 205 ILE 205 205 205 ILE ILE Z . n 
F 1 206 PHE 206 206 206 PHE PHE Z . n 
F 1 207 ALA 207 207 207 ALA ALA Z . n 
F 1 208 GLU 208 208 208 GLU GLU Z . n 
F 1 209 ASP 209 209 209 ASP ASP Z . n 
F 1 210 ASP 210 210 210 ASP ASP Z . n 
F 1 211 ILE 211 211 211 ILE ILE Z . n 
F 1 212 ALA 212 212 212 ALA ALA Z . n 
F 1 213 ASP 213 213 213 ASP ASP Z . n 
F 1 214 TYR 214 214 214 TYR TYR Z . n 
F 1 215 ILE 215 215 215 ILE ILE Z . n 
F 1 216 ILE 216 216 216 ILE ILE Z . n 
F 1 217 ALA 217 217 217 ALA ALA Z . n 
F 1 218 LYS 218 218 218 LYS LYS Z . n 
F 1 219 LEU 219 219 219 LEU LEU Z . n 
F 1 220 GLN 220 220 220 GLN GLN Z . n 
F 1 221 HIS 221 221 221 HIS HIS Z . n 
F 1 222 ARG 222 222 222 ARG ARG Z . n 
F 1 223 ASP 223 223 223 ASP ASP Z . n 
F 1 224 THR 224 224 224 THR THR Z . n 
F 1 225 SER 225 225 225 SER SER Z . n 
F 1 226 ASN 226 226 226 ASN ASN Z . n 
F 1 227 ILE 227 227 227 ILE ILE Z . n 
F 1 228 GLU 228 228 228 GLU GLU Z . n 
F 1 229 GLN 229 229 229 GLN GLN Z . n 
F 1 230 LEU 230 230 230 LEU LEU Z . n 
F 1 231 LEU 231 231 231 LEU LEU Z . n 
F 1 232 ILE 232 232 232 ILE ILE Z . n 
F 1 233 ASN 233 233 233 ASN ASN Z . n 
F 1 234 LYS 234 234 234 LYS LYS Z . n 
F 1 235 ASN 235 235 235 ASN ASN Z . n 
F 1 236 LEU 236 236 236 LEU LEU Z . n 
F 1 237 LYS 237 237 237 LYS LYS Z . n 
F 1 238 MET 238 238 238 MET MET Z . n 
F 1 239 VAL 239 239 239 VAL VAL Z . n 
F 1 240 GLU 240 240 240 GLU GLU Z . n 
F 1 241 PHE 241 241 241 PHE PHE Z . n 
F 1 242 LEU 242 242 242 LEU LEU Z . n 
F 1 243 SER 243 243 243 SER SER Z . n 
F 1 244 LYS 244 244 244 LYS LYS Z . n 
F 1 245 ASN 245 245 245 ASN ASN Z . n 
F 1 246 THR 246 246 246 THR THR Z . n 
F 1 247 LYS 247 247 247 LYS LYS Z . n 
F 1 248 ASN 248 248 248 ASN ASN Z . n 
F 1 249 ASP 249 249 249 ASP ASP Z . n 
F 1 250 ASN 250 250 250 ASN ASN Z . n 
F 1 251 ASN 251 251 251 ASN ASN Z . n 
F 1 252 PHE 252 252 252 PHE PHE Z . n 
F 1 253 THR 253 253 253 THR THR Z . n 
F 1 254 TYR 254 254 254 TYR TYR Z . n 
F 1 255 SER 255 255 255 SER SER Z . n 
F 1 256 GLU 256 256 256 GLU GLU Z . n 
F 1 257 TRP 257 257 257 TRP TRP Z . n 
F 1 258 GLU 258 258 258 GLU GLU Z . n 
F 1 259 SER 259 259 259 SER SER Z . n 
F 1 260 ILE 260 260 260 ILE ILE Z . n 
F 1 261 TYR 261 261 261 TYR TYR Z . n 
F 1 262 ASN 262 262 262 ASN ASN Z . n 
F 1 263 GLY 263 263 263 GLY GLY Z . n 
F 1 264 THR 264 264 264 THR THR Z . n 
F 1 265 TYR 265 265 265 TYR TYR Z . n 
F 1 266 ARG 266 266 266 ARG ARG Z . n 
F 1 267 ILE 267 267 267 ILE ILE Z . n 
F 1 268 THR 268 268 268 THR THR Z . n 
F 1 269 ASN 269 269 269 ASN ASN Z . n 
F 1 270 LEU 270 270 270 LEU LEU Z . n 
F 1 271 PRO 271 271 271 PRO PRO Z . n 
F 1 272 SER 272 272 272 SER SER Z . n 
F 1 273 LEU 273 273 273 LEU LEU Z . n 
F 1 274 GLY 274 274 274 GLY GLY Z . n 
F 1 275 ARG 275 275 275 ARG ARG Z . n 
F 1 276 PHE 276 276 276 PHE PHE Z . n 
F 1 277 LYS 277 277 277 LYS LYS Z . n 
F 1 278 PHE 278 278 278 PHE PHE Z . n 
F 1 279 ARG 279 279 279 ARG ARG Z . n 
F 1 280 LYS 280 280 280 LYS LYS Z . n 
F 1 281 LYS 281 281 281 LYS LYS Z . n 
F 1 282 ILE 282 282 282 ILE ILE Z . n 
F 1 283 ALA 283 283 283 ALA ALA Z . n 
F 1 284 GLU 284 284 284 GLU GLU Z . n 
F 1 285 LYS 285 285 285 LYS LYS Z . n 
F 1 286 SER 286 286 286 SER SER Z . n 
F 1 287 LEU 287 287 287 LEU LEU Z . n 
F 1 288 SER 288 288 288 SER SER Z . n 
F 1 289 GLY 289 289 289 GLY GLY Z . n 
F 1 290 LYS 290 290 290 LYS LYS Z . n 
F 1 291 VAL 291 291 291 VAL VAL Z . n 
F 1 292 LYS 292 292 292 LYS LYS Z . n 
F 1 293 GLU 293 293 293 GLU GLU Z . n 
F 1 294 PHE 294 294 294 PHE PHE Z . n 
F 1 295 ASN 295 295 295 ASN ASN Z . n 
F 1 296 ASN 296 296 296 ASN ASN Z . n 
F 1 297 ILE 297 297 297 ILE ILE Z . n 
F 1 298 VAL 298 298 298 VAL VAL Z . n 
F 1 299 GLN 299 299 299 GLN GLN Z . n 
F 1 300 ARG 300 300 300 ARG ARG Z . n 
F 1 301 TYR 301 301 301 TYR TYR Z . n 
F 1 302 SER 302 302 302 SER SER Z . n 
F 1 303 VAL 303 303 303 VAL VAL Z . n 
F 1 304 GLY 304 304 304 GLY GLY Z . n 
F 1 305 LEU 305 305 305 LEU LEU Z . n 
F 1 306 ALA 306 306 306 ALA ALA Z . n 
F 1 307 SER 307 307 307 SER SER Z . n 
F 1 308 SER 308 308 308 SER SER Z . n 
F 1 309 ASP 309 309 309 ASP ASP Z . n 
F 1 310 LEU 310 310 310 LEU LEU Z . n 
F 1 311 PRO 311 311 311 PRO PRO Z . n 
F 1 312 PHE 312 312 312 PHE PHE Z . n 
F 1 313 GLY 313 313 313 GLY GLY Z . n 
F 1 314 VAL 314 314 314 VAL VAL Z . n 
F 1 315 ILE 315 315 315 ILE ILE Z . n 
F 1 316 ARG 316 316 316 ARG ARG Z . n 
F 1 317 LYS 317 317 317 LYS LYS Z . n 
F 1 318 GLU 318 318 318 GLU GLU Z . n 
F 1 319 SER 319 319 319 SER SER Z . n 
F 1 320 ARG 320 320 320 ARG ARG Z . n 
F 1 321 ASN 321 321 321 ASN ASN Z . n 
F 1 322 ASP 322 322 322 ASP ASP Z . n 
F 1 323 PHE 323 323 323 PHE PHE Z . n 
F 1 324 ILE 324 324 324 ILE ILE Z . n 
F 1 325 ASN 325 325 325 ASN ASN Z . n 
F 1 326 ASP 326 326 326 ASP ASP Z . n 
F 1 327 VAL 327 327 327 VAL VAL Z . n 
F 1 328 CYS 328 328 328 CYS CYS Z . n 
F 1 329 LYS 329 329 329 LYS LYS Z . n 
F 1 330 LEU 330 330 330 LEU LEU Z . n 
F 1 331 TYR 331 331 331 TYR TYR Z . n 
F 1 332 ASN 332 332 332 ASN ASN Z . n 
F 1 333 ILE 333 333 333 ILE ILE Z . n 
F 1 334 ASN 334 334 334 ASN ASN Z . n 
F 1 335 ASP 335 335 335 ASP ASP Z . n 
F 1 336 MET 336 336 336 MET MET Z . n 
F 1 337 LYS 337 337 337 LYS LYS Z . n 
F 1 338 ILE 338 338 338 ILE ILE Z . n 
F 1 339 ILE 339 339 339 ILE ILE Z . n 
F 1 340 LYS 340 340 340 LYS LYS Z . n 
F 1 341 GLU 341 341 341 GLU GLU Z . n 
F 1 342 LEU 342 342 342 LEU LEU Z . n 
F 1 343 LYS 343 343 343 LYS LYS Z . n 
F 1 344 GLU 344 344 344 GLU GLU Z . n 
F 1 345 ASP 345 345 345 ASP ASP Z . n 
F 1 346 ALA 346 346 346 ALA ALA Z . n 
F 1 347 ASP 347 347 347 ASP ASP Z . n 
F 1 348 LEU 348 348 348 LEU LEU Z . n 
F 1 349 ILE 349 349 349 ILE ILE Z . n 
F 1 350 VAL 350 350 350 VAL VAL Z . n 
F 1 351 CYS 351 351 351 CYS CYS Z . n 
F 1 352 MET 352 352 352 MET MET Z . n 
F 1 353 LEU 353 353 353 LEU LEU Z . n 
F 1 354 LYS 354 354 354 LYS LYS Z . n 
F 1 355 GLY 355 355 355 GLY GLY Z . n 
F 1 356 PHE 356 356 356 PHE PHE Z . n 
F 1 357 LYS 357 357 357 LYS LYS Z . n 
F 1 358 PRO 358 358 358 PRO PRO Z . n 
F 1 359 ARG 359 359 359 ARG ARG Z . n 
F 1 360 GLY 360 360 360 GLY GLY Z . n 
F 1 361 ASP 361 361 361 ASP ASP Z . n 
F 1 362 ASP 362 362 362 ASP ASP Z . n 
F 1 363 ASN 363 363 363 ASN ASN Z . n 
F 1 364 ARG 364 364 364 ARG ARG Z . n 
F 1 365 PRO 365 365 365 PRO PRO Z . n 
F 1 366 ASP 366 366 366 ASP ASP Z . n 
F 1 367 ARG 367 367 367 ARG ARG Z . n 
F 1 368 GLY 368 368 368 GLY GLY Z . n 
F 1 369 ALA 369 369 369 ALA ALA Z . n 
F 1 370 LEU 370 370 370 LEU LEU Z . n 
F 1 371 PRO 371 371 371 PRO PRO Z . n 
F 1 372 LEU 372 372 372 LEU LEU Z . n 
F 1 373 VAL 373 373 373 VAL VAL Z . n 
F 1 374 ALA 374 374 374 ALA ALA Z . n 
F 1 375 MET 375 375 375 MET MET Z . n 
F 1 376 LEU 376 376 376 LEU LEU Z . n 
F 1 377 ALA 377 377 377 ALA ALA Z . n 
F 1 378 GLY 378 378 378 GLY GLY Z . n 
F 1 379 GLU 379 379 379 GLU GLU Z . n 
F 1 380 ASN 380 380 380 ASN ASN Z . n 
F 1 381 ALA 381 381 381 ALA ALA Z . n 
F 1 382 GLN 382 382 382 GLN GLN Z . n 
F 1 383 ILE 383 383 383 ILE ILE Z . n 
F 1 384 PHE 384 384 384 PHE PHE Z . n 
F 1 385 THR 385 385 385 THR THR Z . n 
F 1 386 PHE 386 386 386 PHE PHE Z . n 
F 1 387 ILE 387 387 387 ILE ILE Z . n 
F 1 388 TYR 388 388 388 TYR TYR Z . n 
F 1 389 GLY 389 389 389 GLY GLY Z . n 
F 1 390 PRO 390 390 390 PRO PRO Z . n 
F 1 391 LEU 391 391 391 LEU LEU Z . n 
F 1 392 ILE 392 392 392 ILE ILE Z . n 
F 1 393 LYS 393 393 393 LYS LYS Z . n 
F 1 394 GLY 394 394 394 GLY GLY Z . n 
F 1 395 ALA 395 395 395 ALA ALA Z . n 
F 1 396 ILE 396 396 396 ILE ILE Z . n 
F 1 397 ASN 397 397 397 ASN ASN Z . n 
F 1 398 LEU 398 398 398 LEU LEU Z . n 
F 1 399 ILE 399 399 399 ILE ILE Z . n 
F 1 400 ASP 400 400 400 ASP ASP Z . n 
F 1 401 GLN 401 401 401 GLN GLN Z . n 
F 1 402 ASP 402 402 402 ASP ASP Z . n 
F 1 403 ILE 403 403 403 ILE ILE Z . n 
F 1 404 ASN 404 404 404 ASN ASN Z . n 
F 1 405 LYS 405 405 405 LYS LYS Z . n 
F 1 406 LEU 406 406 406 LEU LEU Z . n 
F 1 407 ALA 407 407 407 ALA ALA Z . n 
F 1 408 LYS 408 408 408 LYS LYS Z . n 
F 1 409 ARG 409 409 409 ARG ARG Z . n 
F 1 410 ASN 410 410 410 ASN ASN Z . n 
F 1 411 GLY 411 411 411 GLY GLY Z . n 
F 1 412 LEU 412 412 412 LEU LEU Z . n 
F 1 413 TRP 413 413 413 TRP TRP Z . n 
F 1 414 LYS 414 414 414 LYS LYS Z . n 
F 1 415 SER 415 415 415 SER SER Z . n 
F 1 416 PHE 416 416 416 PHE PHE Z . n 
F 1 417 VAL 417 417 417 VAL VAL Z . n 
F 1 418 SER 418 418 418 SER SER Z . n 
F 1 419 LEU 419 419 419 LEU LEU Z . n 
F 1 420 SER 420 420 420 SER SER Z . n 
F 1 421 ASP 421 421 421 ASP ASP Z . n 
F 1 422 PHE 422 422 422 PHE PHE Z . n 
F 1 423 ILE 423 423 423 ILE ILE Z . n 
F 1 424 VAL 424 424 424 VAL VAL Z . n 
F 1 425 LEU 425 425 425 LEU LEU Z . n 
F 1 426 ASP 426 426 426 ASP ASP Z . n 
F 1 427 CYS 427 427 427 CYS CYS Z . n 
F 1 428 PRO 428 428 428 PRO PRO Z . n 
F 1 429 ILE 429 429 429 ILE ILE Z . n 
F 1 430 ILE 430 430 430 ILE ILE Z . n 
F 1 431 GLY 431 431 431 GLY GLY Z . n 
F 1 432 GLU 432 432 432 GLU GLU Z . n 
F 1 433 SER 433 433 433 SER SER Z . n 
F 1 434 TYR 434 434 434 TYR TYR Z . n 
F 1 435 ASN 435 435 435 ASN ASN Z . n 
F 1 436 GLU 436 436 436 GLU GLU Z . n 
F 1 437 PHE 437 437 437 PHE PHE Z . n 
F 1 438 ARG 438 438 438 ARG ARG Z . n 
F 1 439 LEU 439 439 439 LEU LEU Z . n 
F 1 440 ILE 440 440 440 ILE ILE Z . n 
F 1 441 ILE 441 441 441 ILE ILE Z . n 
F 1 442 ASN 442 442 442 ASN ASN Z . n 
F 1 443 LYS 443 443 443 LYS LYS Z . n 
F 1 444 ASN 444 444 444 ASN ASN Z . n 
F 1 445 ASN 445 445 445 ASN ASN Z . n 
F 1 446 LYS 446 446 446 LYS LYS Z . n 
F 1 447 GLU 447 447 447 GLU GLU Z . n 
F 1 448 SER 448 448 448 SER SER Z . n 
F 1 449 ILE 449 449 449 ILE ILE Z . n 
F 1 450 LEU 450 450 450 LEU LEU Z . n 
F 1 451 ARG 451 451 451 ARG ARG Z . n 
F 1 452 LYS 452 452 452 LYS LYS Z . n 
F 1 453 THR 453 453 453 THR THR Z . n 
F 1 454 SER 454 454 454 SER SER Z . n 
F 1 455 LYS 455 455 455 LYS LYS Z . n 
F 1 456 GLN 456 456 456 GLN GLN Z . n 
F 1 457 GLN 457 457 457 GLN GLN Z . n 
F 1 458 ASN 458 458 458 ASN ASN Z . n 
F 1 459 ILE 459 459 459 ILE ILE Z . n 
F 1 460 LEU 460 460 460 LEU LEU Z . n 
F 1 461 VAL 461 461 461 VAL VAL Z . n 
F 1 462 ASP 462 462 462 ASP ASP Z . n 
F 1 463 PRO 463 463 463 PRO PRO Z . n 
F 1 464 THR 464 464 464 THR THR Z . n 
F 1 465 PRO 465 465 465 PRO PRO Z . n 
F 1 466 ASN 466 466 466 ASN ASN Z . n 
F 1 467 HIS 467 467 467 HIS HIS Z . n 
F 1 468 TYR 468 468 468 TYR TYR Z . n 
F 1 469 GLN 469 469 469 GLN GLN Z . n 
F 1 470 GLU 470 470 470 GLU GLU Z . n 
F 1 471 ASN 471 471 471 ASN ASN Z . n 
F 1 472 ASP 472 472 472 ASP ASP Z . n 
F 1 473 VAL 473 473 473 VAL VAL Z . n 
F 1 474 ASP 474 474 474 ASP ASP Z . n 
F 1 475 THR 475 475 475 THR THR Z . n 
F 1 476 VAL 476 476 476 VAL VAL Z . n 
F 1 477 ILE 477 477 477 ILE ILE Z . n 
F 1 478 TYR 478 478 478 TYR TYR Z . n 
F 1 479 SER 479 479 479 SER SER Z . n 
F 1 480 ILE 480 480 480 ILE ILE Z . n 
F 1 481 PHE 481 481 481 PHE PHE Z . n 
F 1 482 LYS 482 482 482 LYS LYS Z . n 
F 1 483 TYR 483 483 483 TYR TYR Z . n 
F 1 484 ILE 484 484 484 ILE ILE Z . n 
F 1 485 VAL 485 485 485 VAL VAL Z . n 
F 1 486 PRO 486 486 486 PRO PRO Z . n 
F 1 487 ASN 487 487 487 ASN ASN Z . n 
F 1 488 CYS 488 488 488 CYS CYS Z . n 
F 1 489 PHE 489 489 489 PHE PHE Z . n 
F 1 490 SER 490 490 490 SER SER Z . n 
F 1 491 GLY 491 491 491 GLY GLY Z . n 
F 1 492 MET 492 492 492 MET MET Z . n 
F 1 493 CYS 493 493 493 CYS CYS Z . n 
F 1 494 ASN 494 494 494 ASN ASN Z . n 
F 1 495 PRO 495 495 495 PRO PRO Z . n 
F 1 496 PRO 496 496 496 PRO PRO Z . n 
F 1 497 GLY 497 497 497 GLY GLY Z . n 
F 1 498 GLY 498 498 498 GLY GLY Z . n 
F 1 499 ASP 499 499 499 ASP ASP Z . n 
F 1 500 TRP 500 500 500 TRP TRP Z . n 
F 1 501 SER 501 501 501 SER SER Z . n 
F 1 502 GLY 502 502 502 GLY GLY Z . n 
F 1 503 LEU 503 503 503 LEU LEU Z . n 
F 1 504 SER 504 504 504 SER SER Z . n 
F 1 505 ILE 505 505 505 ILE ILE Z . n 
F 1 506 ILE 506 506 506 ILE ILE Z . n 
F 1 507 ARG 507 507 507 ARG ARG Z . n 
F 1 508 ASN 508 508 508 ASN ASN Z . n 
F 1 509 GLY 509 509 509 GLY GLY Z . n 
F 1 510 HIS 510 510 510 HIS HIS Z . n 
F 1 511 GLU 511 511 511 GLU GLU Z . n 
F 1 512 PHE 512 512 512 PHE PHE Z . n 
F 1 513 ARG 513 513 513 ARG ARG Z . n 
F 1 514 TRP 514 514 514 TRP TRP Z . n 
F 1 515 LEU 515 515 515 LEU LEU Z . n 
F 1 516 SER 516 516 516 SER SER Z . n 
F 1 517 LEU 517 517 517 LEU LEU Z . n 
F 1 518 PRO 518 518 518 PRO PRO Z . n 
F 1 519 ARG 519 519 519 ARG ARG Z . n 
F 1 520 VAL 520 520 520 VAL VAL Z . n 
F 1 521 SER 521 521 521 SER SER Z . n 
F 1 522 GLU 522 522 522 GLU GLU Z . n 
F 1 523 ASN 523 523 523 ASN ASN Z . n 
F 1 524 GLY 524 524 524 GLY GLY Z . n 
F 1 525 LYS 525 525 525 LYS LYS Z . n 
F 1 526 ARG 526 526 526 ARG ARG Z . n 
F 1 527 PRO 527 527 527 PRO PRO Z . n 
F 1 528 ASP 528 528 528 ASP ASP Z . n 
F 1 529 HIS 529 529 529 HIS HIS Z . n 
F 1 530 VAL 530 530 530 VAL VAL Z . n 
F 1 531 ILE 531 531 531 ILE ILE Z . n 
F 1 532 GLN 532 532 532 GLN GLN Z . n 
F 1 533 ILE 533 533 533 ILE ILE Z . n 
F 1 534 LEU 534 534 534 LEU LEU Z . n 
F 1 535 ASP 535 535 535 ASP ASP Z . n 
F 1 536 LEU 536 536 536 LEU LEU Z . n 
F 1 537 PHE 537 537 537 PHE PHE Z . n 
F 1 538 GLU 538 538 538 GLU GLU Z . n 
F 1 539 LYS 539 539 539 LYS LYS Z . n 
F 1 540 PRO 540 540 540 PRO PRO Z . n 
F 1 541 LEU 541 541 541 LEU LEU Z . n 
F 1 542 LEU 542 542 542 LEU LEU Z . n 
F 1 543 LEU 543 543 543 LEU LEU Z . n 
F 1 544 SER 544 544 544 SER SER Z . n 
F 1 545 ILE 545 545 545 ILE ILE Z . n 
F 1 546 GLU 546 546 546 GLU GLU Z . n 
F 1 547 SER 547 547 547 SER SER Z . n 
F 1 548 LYS 548 548 548 LYS LYS Z . n 
F 1 549 GLU 549 549 549 GLU GLU Z . n 
F 1 550 LYS 550 550 550 LYS LYS Z . n 
F 1 551 PRO 551 551 551 PRO PRO Z . n 
F 1 552 ASN 552 552 552 ASN ASN Z . n 
F 1 553 ASP 553 553 553 ASP ASP Z . n 
F 1 554 LEU 554 554 554 LEU LEU Z . n 
F 1 555 GLU 555 555 555 GLU GLU Z . n 
F 1 556 PRO 556 556 556 PRO PRO Z . n 
F 1 557 LYS 557 557 557 LYS LYS Z . n 
F 1 558 ILE 558 558 558 ILE ILE Z . n 
F 1 559 GLY 559 559 559 GLY GLY Z . n 
F 1 560 VAL 560 560 560 VAL VAL Z . n 
F 1 561 GLN 561 561 561 GLN GLN Z . n 
F 1 562 LEU 562 562 562 LEU LEU Z . n 
F 1 563 ILE 563 563 563 ILE ILE Z . n 
F 1 564 LYS 564 564 564 LYS LYS Z . n 
F 1 565 TYR 565 565 565 TYR TYR Z . n 
F 1 566 ILE 566 566 566 ILE ILE Z . n 
F 1 567 GLU 567 567 567 GLU GLU Z . n 
F 1 568 TYR 568 568 568 TYR TYR Z . n 
F 1 569 LEU 569 569 569 LEU LEU Z . n 
F 1 570 PHE 570 570 570 PHE PHE Z . n 
F 1 571 ASP 571 571 571 ASP ASP Z . n 
F 1 572 PHE 572 572 572 PHE PHE Z . n 
F 1 573 THR 573 573 573 THR THR Z . n 
F 1 574 PRO 574 574 574 PRO PRO Z . n 
F 1 575 SER 575 575 575 SER SER Z . n 
F 1 576 VAL 576 576 576 VAL VAL Z . n 
F 1 577 GLN 577 577 577 GLN GLN Z . n 
F 1 578 ARG 578 578 578 ARG ARG Z . n 
F 1 579 LYS 579 579 579 LYS LYS Z . n 
F 1 580 ILE 580 580 580 ILE ILE Z . n 
F 1 581 ALA 581 581 581 ALA ALA Z . n 
F 1 582 GLY 582 582 582 GLY GLY Z . n 
F 1 583 GLY 583 583 583 GLY GLY Z . n 
F 1 584 ASN 584 584 584 ASN ASN Z . n 
F 1 585 TRP 585 585 585 TRP TRP Z . n 
F 1 586 GLU 586 586 586 GLU GLU Z . n 
F 1 587 PHE 587 587 587 PHE PHE Z . n 
F 1 588 GLY 588 588 588 GLY GLY Z . n 
F 1 589 ASN 589 589 589 ASN ASN Z . n 
F 1 590 LYS 590 590 590 LYS LYS Z . n 
F 1 591 SER 591 591 591 SER SER Z . n 
F 1 592 LEU 592 592 592 LEU LEU Z . n 
F 1 593 VAL 593 593 593 VAL VAL Z . n 
F 1 594 PRO 594 594 594 PRO PRO Z . n 
F 1 595 ASN 595 595 595 ASN ASN Z . n 
F 1 596 ASP 596 596 596 ASP ASP Z . n 
F 1 597 PHE 597 597 597 PHE PHE Z . n 
F 1 598 ILE 598 598 598 ILE ILE Z . n 
F 1 599 LEU 599 599 599 LEU LEU Z . n 
F 1 600 LEU 600 600 600 LEU LEU Z . n 
F 1 601 SER 601 601 601 SER SER Z . n 
F 1 602 ALA 602 602 602 ALA ALA Z . n 
F 1 603 GLY 603 603 603 GLY GLY Z . n 
F 1 604 ALA 604 604 604 ALA ALA Z . n 
F 1 605 PHE 605 605 605 PHE PHE Z . n 
F 1 606 ILE 606 606 606 ILE ILE Z . n 
F 1 607 ASP 607 607 607 ASP ASP Z . n 
F 1 608 TYR 608 608 608 TYR TYR Z . n 
F 1 609 ASP 609 609 609 ASP ASP Z . n 
F 1 610 ASN 610 610 610 ASN ASN Z . n 
F 1 611 LEU 611 611 611 LEU LEU Z . n 
F 1 612 THR 612 612 612 THR THR Z . n 
F 1 613 GLU 613 613 613 GLU GLU Z . n 
F 1 614 ASN 614 614 614 ASN ASN Z . n 
F 1 615 ASP 615 615 615 ASP ASP Z . n 
F 1 616 TYR 616 616 616 TYR TYR Z . n 
F 1 617 GLU 617 617 617 GLU GLU Z . n 
F 1 618 LYS 618 618 618 LYS LYS Z . n 
F 1 619 ILE 619 619 619 ILE ILE Z . n 
F 1 620 PHE 620 620 620 PHE PHE Z . n 
F 1 621 GLU 621 621 621 GLU GLU Z . n 
F 1 622 VAL 622 622 622 VAL VAL Z . n 
F 1 623 THR 623 623 623 THR THR Z . n 
F 1 624 GLY 624 624 624 GLY GLY Z . n 
F 1 625 CYS 625 625 625 CYS CYS Z . n 
F 1 626 ASP 626 626 626 ASP ASP Z . n 
F 1 627 LEU 627 627 627 LEU LEU Z . n 
F 1 628 LEU 628 628 628 LEU LEU Z . n 
F 1 629 ILE 629 629 629 ILE ILE Z . n 
F 1 630 ALA 630 630 630 ALA ALA Z . n 
F 1 631 ILE 631 631 631 ILE ILE Z . n 
F 1 632 LYS 632 632 632 LYS LYS Z . n 
F 1 633 ASN 633 633 633 ASN ASN Z . n 
F 1 634 GLN 634 634 634 GLN GLN Z . n 
F 1 635 ASN 635 635 635 ASN ASN Z . n 
F 1 636 ASN 636 636 636 ASN ASN Z . n 
F 1 637 PRO 637 637 637 PRO PRO Z . n 
F 1 638 GLN 638 638 638 GLN GLN Z . n 
F 1 639 LYS 639 639 639 LYS LYS Z . n 
F 1 640 TRP 640 640 640 TRP TRP Z . n 
F 1 641 VAL 641 641 641 VAL VAL Z . n 
F 1 642 ILE 642 642 642 ILE ILE Z . n 
F 1 643 LYS 643 643 643 LYS LYS Z . n 
F 1 644 PHE 644 644 644 PHE PHE Z . n 
F 1 645 LYS 645 645 645 LYS LYS Z . n 
F 1 646 PRO 646 646 646 PRO PRO Z . n 
F 1 647 LYS 647 647 647 LYS LYS Z . n 
F 1 648 ASN 648 648 648 ASN ASN Z . n 
F 1 649 THR 649 649 649 THR THR Z . n 
F 1 650 ILE 650 650 650 ILE ILE Z . n 
F 1 651 ALA 651 651 651 ALA ALA Z . n 
F 1 652 GLU 652 652 652 GLU GLU Z . n 
F 1 653 LYS 653 653 653 LYS LYS Z . n 
F 1 654 LEU 654 654 654 LEU LEU Z . n 
F 1 655 VAL 655 655 655 VAL VAL Z . n 
F 1 656 ASN 656 656 656 ASN ASN Z . n 
F 1 657 TYR 657 657 657 TYR TYR Z . n 
F 1 658 ILE 658 658 658 ILE ILE Z . n 
F 1 659 LYS 659 659 659 LYS LYS Z . n 
F 1 660 LEU 660 660 660 LEU LEU Z . n 
F 1 661 ASN 661 661 661 ASN ASN Z . n 
F 1 662 PHE 662 662 662 PHE PHE Z . n 
F 1 663 LYS 663 663 663 LYS LYS Z . n 
F 1 664 SER 664 664 664 SER SER Z . n 
F 1 665 ASN 665 665 665 ASN ASN Z . n 
F 1 666 ILE 666 666 666 ILE ILE Z . n 
F 1 667 PHE 667 667 667 PHE PHE Z . n 
F 1 668 ASP 668 668 668 ASP ASP Z . n 
F 1 669 THR 669 669 669 THR THR Z . n 
F 1 670 GLY 670 670 670 GLY GLY Z . n 
F 1 671 PHE 671 671 671 PHE PHE Z . n 
F 1 672 PHE 672 672 672 PHE PHE Z . n 
F 1 673 HIS 673 673 673 HIS HIS Z . n 
F 1 674 ILE 674 674 674 ILE ILE Z . n 
F 1 675 GLU 675 675 675 GLU GLU Z . n 
F 1 676 GLY 676 676 676 GLY GLY Z . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        CA 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   CA 
_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 4 CA  1  701 1   CA  CA  A . 
H 4 CA  1  702 2   CA  CA  A . 
I 4 CA  1  703 3   CA  CA  A . 
J 4 CA  1  701 1   CA  CA  Z . 
K 4 CA  1  702 2   CA  CA  Z . 
L 4 CA  1  703 3   CA  CA  Z . 
M 5 MES 1  704 1   MES MES Z . 
N 6 CL  1  705 1   CL  CL  Z . 
O 7 HOH 1  801 18  HOH HOH A . 
O 7 HOH 2  802 7   HOH HOH A . 
O 7 HOH 3  803 90  HOH HOH A . 
O 7 HOH 4  804 142 HOH HOH A . 
O 7 HOH 5  805 110 HOH HOH A . 
O 7 HOH 6  806 177 HOH HOH A . 
O 7 HOH 7  807 107 HOH HOH A . 
O 7 HOH 8  808 136 HOH HOH A . 
O 7 HOH 9  809 86  HOH HOH A . 
O 7 HOH 10 810 25  HOH HOH A . 
O 7 HOH 11 811 67  HOH HOH A . 
O 7 HOH 12 812 163 HOH HOH A . 
O 7 HOH 13 813 127 HOH HOH A . 
O 7 HOH 14 814 60  HOH HOH A . 
O 7 HOH 15 815 64  HOH HOH A . 
O 7 HOH 16 816 153 HOH HOH A . 
O 7 HOH 17 817 143 HOH HOH A . 
O 7 HOH 18 818 101 HOH HOH A . 
O 7 HOH 19 819 22  HOH HOH A . 
O 7 HOH 20 820 171 HOH HOH A . 
O 7 HOH 21 821 93  HOH HOH A . 
O 7 HOH 22 822 108 HOH HOH A . 
O 7 HOH 23 823 112 HOH HOH A . 
O 7 HOH 24 824 129 HOH HOH A . 
O 7 HOH 25 825 54  HOH HOH A . 
O 7 HOH 26 826 158 HOH HOH A . 
O 7 HOH 27 827 133 HOH HOH A . 
O 7 HOH 28 828 42  HOH HOH A . 
O 7 HOH 29 829 32  HOH HOH A . 
O 7 HOH 30 830 37  HOH HOH A . 
O 7 HOH 31 831 139 HOH HOH A . 
O 7 HOH 32 832 173 HOH HOH A . 
O 7 HOH 33 833 79  HOH HOH A . 
O 7 HOH 34 834 31  HOH HOH A . 
O 7 HOH 35 835 154 HOH HOH A . 
O 7 HOH 36 836 94  HOH HOH A . 
O 7 HOH 37 837 168 HOH HOH A . 
O 7 HOH 38 838 51  HOH HOH A . 
O 7 HOH 39 839 69  HOH HOH A . 
O 7 HOH 40 840 122 HOH HOH A . 
O 7 HOH 41 841 84  HOH HOH A . 
O 7 HOH 42 842 88  HOH HOH A . 
O 7 HOH 43 843 95  HOH HOH A . 
O 7 HOH 44 844 117 HOH HOH A . 
O 7 HOH 45 845 145 HOH HOH A . 
O 7 HOH 46 846 144 HOH HOH A . 
O 7 HOH 47 847 155 HOH HOH A . 
O 7 HOH 48 848 81  HOH HOH A . 
O 7 HOH 49 849 111 HOH HOH A . 
O 7 HOH 50 850 50  HOH HOH A . 
O 7 HOH 51 851 13  HOH HOH A . 
O 7 HOH 52 852 56  HOH HOH A . 
O 7 HOH 53 853 121 HOH HOH A . 
O 7 HOH 54 854 169 HOH HOH A . 
O 7 HOH 55 855 66  HOH HOH A . 
O 7 HOH 56 856 141 HOH HOH A . 
O 7 HOH 57 857 38  HOH HOH A . 
O 7 HOH 58 858 5   HOH HOH A . 
O 7 HOH 59 859 40  HOH HOH A . 
O 7 HOH 60 860 1   HOH HOH A . 
O 7 HOH 61 861 29  HOH HOH A . 
O 7 HOH 62 862 164 HOH HOH A . 
O 7 HOH 63 863 74  HOH HOH A . 
O 7 HOH 64 864 151 HOH HOH A . 
O 7 HOH 65 865 130 HOH HOH A . 
O 7 HOH 66 866 120 HOH HOH A . 
O 7 HOH 67 867 85  HOH HOH A . 
O 7 HOH 68 868 3   HOH HOH A . 
O 7 HOH 69 869 35  HOH HOH A . 
O 7 HOH 70 870 8   HOH HOH A . 
O 7 HOH 71 871 16  HOH HOH A . 
P 7 HOH 1  101 83  HOH HOH E . 
P 7 HOH 2  102 45  HOH HOH E . 
Q 7 HOH 1  101 6   HOH HOH F . 
Q 7 HOH 2  102 80  HOH HOH F . 
Q 7 HOH 3  103 115 HOH HOH F . 
Q 7 HOH 4  104 62  HOH HOH F . 
Q 7 HOH 5  105 109 HOH HOH F . 
Q 7 HOH 6  106 59  HOH HOH F . 
R 7 HOH 1  101 160 HOH HOH U . 
R 7 HOH 2  102 48  HOH HOH U . 
R 7 HOH 3  103 146 HOH HOH U . 
R 7 HOH 4  104 65  HOH HOH U . 
R 7 HOH 5  105 131 HOH HOH U . 
R 7 HOH 6  106 97  HOH HOH U . 
R 7 HOH 7  107 72  HOH HOH U . 
R 7 HOH 8  108 71  HOH HOH U . 
S 7 HOH 1  101 77  HOH HOH V . 
S 7 HOH 2  102 103 HOH HOH V . 
S 7 HOH 3  103 124 HOH HOH V . 
S 7 HOH 4  104 10  HOH HOH V . 
S 7 HOH 5  105 150 HOH HOH V . 
S 7 HOH 6  106 43  HOH HOH V . 
S 7 HOH 7  107 149 HOH HOH V . 
T 7 HOH 1  801 156 HOH HOH Z . 
T 7 HOH 2  802 170 HOH HOH Z . 
T 7 HOH 3  803 34  HOH HOH Z . 
T 7 HOH 4  804 20  HOH HOH Z . 
T 7 HOH 5  805 176 HOH HOH Z . 
T 7 HOH 6  806 89  HOH HOH Z . 
T 7 HOH 7  807 39  HOH HOH Z . 
T 7 HOH 8  808 15  HOH HOH Z . 
T 7 HOH 9  809 123 HOH HOH Z . 
T 7 HOH 10 810 162 HOH HOH Z . 
T 7 HOH 11 811 2   HOH HOH Z . 
T 7 HOH 12 812 23  HOH HOH Z . 
T 7 HOH 13 813 114 HOH HOH Z . 
T 7 HOH 14 814 46  HOH HOH Z . 
T 7 HOH 15 815 140 HOH HOH Z . 
T 7 HOH 16 816 30  HOH HOH Z . 
T 7 HOH 17 817 61  HOH HOH Z . 
T 7 HOH 18 818 137 HOH HOH Z . 
T 7 HOH 19 819 12  HOH HOH Z . 
T 7 HOH 20 820 76  HOH HOH Z . 
T 7 HOH 21 821 78  HOH HOH Z . 
T 7 HOH 22 822 172 HOH HOH Z . 
T 7 HOH 23 823 26  HOH HOH Z . 
T 7 HOH 24 824 14  HOH HOH Z . 
T 7 HOH 25 825 166 HOH HOH Z . 
T 7 HOH 26 826 28  HOH HOH Z . 
T 7 HOH 27 827 104 HOH HOH Z . 
T 7 HOH 28 828 157 HOH HOH Z . 
T 7 HOH 29 829 55  HOH HOH Z . 
T 7 HOH 30 830 47  HOH HOH Z . 
T 7 HOH 31 831 99  HOH HOH Z . 
T 7 HOH 32 832 87  HOH HOH Z . 
T 7 HOH 33 833 105 HOH HOH Z . 
T 7 HOH 34 834 116 HOH HOH Z . 
T 7 HOH 35 835 165 HOH HOH Z . 
T 7 HOH 36 836 174 HOH HOH Z . 
T 7 HOH 37 837 11  HOH HOH Z . 
T 7 HOH 38 838 147 HOH HOH Z . 
T 7 HOH 39 839 161 HOH HOH Z . 
T 7 HOH 40 840 52  HOH HOH Z . 
T 7 HOH 41 841 175 HOH HOH Z . 
T 7 HOH 42 842 36  HOH HOH Z . 
T 7 HOH 43 843 41  HOH HOH Z . 
T 7 HOH 44 844 152 HOH HOH Z . 
T 7 HOH 45 845 113 HOH HOH Z . 
T 7 HOH 46 846 49  HOH HOH Z . 
T 7 HOH 47 847 21  HOH HOH Z . 
T 7 HOH 48 848 68  HOH HOH Z . 
T 7 HOH 49 849 92  HOH HOH Z . 
T 7 HOH 50 850 102 HOH HOH Z . 
T 7 HOH 51 851 4   HOH HOH Z . 
T 7 HOH 52 852 27  HOH HOH Z . 
T 7 HOH 53 853 119 HOH HOH Z . 
T 7 HOH 54 854 128 HOH HOH Z . 
T 7 HOH 55 855 82  HOH HOH Z . 
T 7 HOH 56 856 98  HOH HOH Z . 
T 7 HOH 57 857 135 HOH HOH Z . 
T 7 HOH 58 858 58  HOH HOH Z . 
T 7 HOH 59 859 100 HOH HOH Z . 
T 7 HOH 60 860 91  HOH HOH Z . 
T 7 HOH 61 861 159 HOH HOH Z . 
T 7 HOH 62 862 106 HOH HOH Z . 
T 7 HOH 63 863 148 HOH HOH Z . 
T 7 HOH 64 864 126 HOH HOH Z . 
T 7 HOH 65 865 134 HOH HOH Z . 
T 7 HOH 66 866 73  HOH HOH Z . 
T 7 HOH 67 867 53  HOH HOH Z . 
T 7 HOH 68 868 132 HOH HOH Z . 
T 7 HOH 69 869 167 HOH HOH Z . 
T 7 HOH 70 870 57  HOH HOH Z . 
T 7 HOH 71 871 118 HOH HOH Z . 
T 7 HOH 72 872 125 HOH HOH Z . 
T 7 HOH 73 873 96  HOH HOH Z . 
T 7 HOH 74 874 19  HOH HOH Z . 
T 7 HOH 75 875 138 HOH HOH Z . 
T 7 HOH 76 876 24  HOH HOH Z . 
T 7 HOH 77 877 17  HOH HOH Z . 
T 7 HOH 78 878 44  HOH HOH Z . 
T 7 HOH 79 879 33  HOH HOH Z . 
T 7 HOH 80 880 9   HOH HOH Z . 
# 
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       ? ? ? ? ? ? ? ? ? ? ? BUSTER    ? ? ? 2.10.4 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? .      2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? STARANISO ? ? ? .      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP    ? ? ? .      4 
# 
_cell.angle_alpha                  90 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   95.5 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9F38 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     65.735 
_cell.length_a_esd                 ? 
_cell.length_b                     129.885 
_cell.length_b_esd                 ? 
_cell.length_c                     100.733 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9F38 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9F38 
_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             2.48 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.48 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;100 mM MES, pH 6.5
100 mM CaCl2
25 % PEG 400
35 % Guanidine HCl
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-09-23 
_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   0.97856 
_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                        'SOLEIL BEAMLINE PROXIMA 1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97856 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'PROXIMA 1' 
_diffrn_source.pdbx_synchrotron_site       SOLEIL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9F38 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.85 
_reflns.d_resolution_low                               48.7 
_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                                     24310 
_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                                5.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          4.5 
_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                                   0.957 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.345 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.85 
_reflns_shell.d_res_low                                     2.92 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.7 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             24310 
_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                                  0.531 
_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                                  1.292 
_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]                            9.396 
_refine.aniso_B[1][2]                            0 
_refine.aniso_B[1][3]                            9.1031 
_refine.aniso_B[2][2]                            0.3208 
_refine.aniso_B[2][3]                            0 
_refine.aniso_B[3][3]                            -9.7168 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               47.58 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.802 
_refine.correlation_coeff_Fo_to_Fc_free          0.759 
_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                                 9F38 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.85 
_refine.ls_d_res_low                             48.7 
_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                     24310 
_refine.ls_number_reflns_R_free                  1187 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    61.8 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2753 
_refine.ls_R_factor_R_free                       0.2934 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2744 
_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                    ? 
_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                          ? 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.672 
_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                            ? 
_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_analyze.entry_id                        9F38 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.54 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.85 
_refine_hist.d_res_low                        48.7 
_refine_hist.number_atoms_solvent             174 
_refine_hist.number_atoms_total               12289 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        11042 
_refine_hist.pdbx_number_atoms_nucleic_acid   1054 
_refine_hist.pdbx_number_atoms_ligand         19 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.005 ? 12505 ? t_bond_d                  2  HARMONIC     
'X-RAY DIFFRACTION' ? 0.8   ? 17125 ? t_angle_deg               2  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 4281  ? t_dihedral_angle_d        2  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? 1972  ? t_gen_planes              5  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 12492 ? t_it                      10 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1612  ? t_chiral_improper_torsion 5  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? 8748  ? t_ideal_dist_contact      4  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? 2.69  ? ?     ? t_omega_torsion           ?  ?            
'X-RAY DIFFRACTION' ? 18.52 ? ?     ? t_other_torsion           ?  ?            
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.85 
_refine_ls_shell.d_res_low                        2.93 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                487 
_refine_ls_shell.number_reflns_R_free             26 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.percent_reflns_obs               15.9 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     0.3208 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.3176 
_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                  0.3729 
# 
_struct.entry_id                     9F38 
_struct.title                        'BsmI (wild-type) crystallized with Ca2+ and cognate dsDNA' 
_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        9F38 
_struct_keywords.text            'restriction endonuclease, DNA cleavage, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 2 ? 
F N N 1 ? 
G N N 4 ? 
H N N 4 ? 
I N N 4 ? 
J N N 4 ? 
K N N 4 ? 
L N N 4 ? 
M N N 5 ? 
N N N 6 ? 
O N N 7 ? 
P N N 7 ? 
Q N N 7 ? 
R N N 7 ? 
S N N 7 ? 
T N N 7 ? 
# 
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 Q8RLN4_GEOSE Q8RLN4 ? 1 
;MNVFRIHGDNIIECERVIDLILSKINPQKVKRGFISLSCPFIEIIFKEGHDYFHWRFDMFPGFNKNTNDRWNSNILDLLS
QKGSFLYETPDVIITSLNNGKEEILMAIEFCSALQAGNQAWQRSGRAYSVGRTGYPYIYIVDFVKYELNNSDRSRKNLRF
PNPAIPYSYISHSKNTGNFIVQAYFRGEEYQPKYDKKLKFFDETIFAEDDIADYIIAKLQHRDTSNIEQLLINKNLKMVE
FLSKNTKNDNNFTYSEWESIYNGTYRITNLPSLGRFKFRKKIAEKSLSGKVKEFNNIVQRYSVGLASSDLPFGVIRKESR
NDFINDVCKLYNINDMKIIKELKEDADLIVCMLKGFKPRGDDNRPDRGALPLVAMLAGENAQIFTFIYGPLIKGAINLID
QDINKLAKRNGLWKSFVSLSDFIVLDCPIIGESYNEFRLIINKNNKESILRKTSKQQNILVDPTPNHYQENDVDTVIYSI
FKYIVPNCFSGMCNPPGGDWSGLSIIRNGHEFRWLSLPRVSENGKRPDHVIQILDLFEKPLLLSIESKEKPNDLEPKIGV
QLIKYIEYLFDFTPSVQRKIAGGNWEFGNKSLVPNDFILLSAGAFIDYDNLTENDYEKIFEVTGCDLLIAIKNQNNPQKW
VIKFKPKNTIAEKLVNYIKLNFKSNIFDTGFFHIEG
;
1 
2 PDB 9F38         9F38   ? 2 ? 1 
3 PDB 9F38         9F38   ? 3 ? 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 9F38 A 1 ? 676 ? Q8RLN4 1 ? 676 ? 1 676 
2 2 9F38 E 1 ? 13  ? 9F38   1 ? 13  ? 1 13  
3 3 9F38 F 1 ? 13  ? 9F38   1 ? 13  ? 1 13  
4 3 9F38 U 1 ? 13  ? 9F38   1 ? 13  ? 1 13  
5 2 9F38 V 1 ? 13  ? 9F38   1 ? 13  ? 1 13  
6 1 9F38 Z 1 ? 676 ? Q8RLN4 1 ? 676 ? 1 676 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? trimeric 3 
2 author_defined_assembly ? trimeric 3 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6490  ? 
1 MORE         -80   ? 
1 'SSA (A^2)'  28490 ? 
2 'ABSA (A^2)' 6810  ? 
2 MORE         -73   ? 
2 'SSA (A^2)'  28590 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,G,H,I,O,P,Q     
2 1 D,E,F,J,K,L,M,N,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   'equilibrium centrifugation' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASN A 10  ? ILE A 25  ? ASN A 10  ILE A 25  1 ? 16 
HELX_P HELX_P2  AA2 LEU A 76  ? GLN A 81  ? LEU A 76  GLN A 81  1 ? 6  
HELX_P HELX_P3  AA3 ALA A 116 ? TRP A 121 ? ALA A 116 TRP A 121 5 ? 6  
HELX_P HELX_P4  AA4 ARG A 123 ? ARG A 132 ? ARG A 123 ARG A 132 1 ? 10 
HELX_P HELX_P5  AA5 PRO A 163 ? GLY A 177 ? PRO A 163 GLY A 177 1 ? 15 
HELX_P HELX_P6  AA6 ASP A 195 ? LYS A 199 ? ASP A 195 LYS A 199 5 ? 5  
HELX_P HELX_P7  AA7 ASP A 202 ? PHE A 206 ? ASP A 202 PHE A 206 5 ? 5  
HELX_P HELX_P8  AA8 ALA A 207 ? GLN A 220 ? ALA A 207 GLN A 220 1 ? 14 
HELX_P HELX_P9  AA9 THR A 224 ? LYS A 244 ? THR A 224 LYS A 244 1 ? 21 
HELX_P HELX_P10 AB1 THR A 253 ? ASN A 262 ? THR A 253 ASN A 262 1 ? 10 
HELX_P HELX_P11 AB2 ALA A 283 ? LEU A 287 ? ALA A 283 LEU A 287 5 ? 5  
HELX_P HELX_P12 AB3 LYS A 290 ? SER A 302 ? LYS A 290 SER A 302 1 ? 13 
HELX_P HELX_P13 AB4 ARG A 316 ? ASN A 332 ? ARG A 316 ASN A 332 1 ? 17 
HELX_P HELX_P14 AB5 ASP A 335 ? LYS A 343 ? ASP A 335 LYS A 343 1 ? 9  
HELX_P HELX_P15 AB6 ARG A 364 ? ARG A 367 ? ARG A 364 ARG A 367 5 ? 4  
HELX_P HELX_P16 AB7 GLY A 368 ? GLY A 378 ? GLY A 368 GLY A 378 1 ? 11 
HELX_P HELX_P17 AB8 ILE A 392 ? ASP A 402 ? ILE A 392 ASP A 402 1 ? 11 
HELX_P HELX_P18 AB9 ASP A 402 ? ASN A 410 ? ASP A 402 ASN A 410 1 ? 9  
HELX_P HELX_P19 AC1 ASN A 410 ? SER A 420 ? ASN A 410 SER A 420 1 ? 11 
HELX_P HELX_P20 AC2 ASN A 442 ? ARG A 451 ? ASN A 442 ARG A 451 1 ? 10 
HELX_P HELX_P21 AC3 GLN A 469 ? TYR A 483 ? GLN A 469 TYR A 483 1 ? 15 
HELX_P HELX_P22 AC4 LYS A 550 ? LEU A 554 ? LYS A 550 LEU A 554 5 ? 5  
HELX_P HELX_P23 AC5 LYS A 557 ? ASP A 571 ? LYS A 557 ASP A 571 1 ? 15 
HELX_P HELX_P24 AC6 VAL A 593 ? PHE A 597 ? VAL A 593 PHE A 597 5 ? 5  
HELX_P HELX_P25 AC7 THR A 612 ? GLY A 624 ? THR A 612 GLY A 624 1 ? 13 
HELX_P HELX_P26 AC8 ASN A 648 ? ASN A 661 ? ASN A 648 ASN A 661 1 ? 14 
HELX_P HELX_P27 AC9 ASP A 668 ? GLY A 670 ? ASP A 668 GLY A 670 5 ? 3  
HELX_P HELX_P28 AD1 ASN F 10  ? ILE F 25  ? ASN Z 10  ILE Z 25  1 ? 16 
HELX_P HELX_P29 AD2 LEU F 76  ? GLN F 81  ? LEU Z 76  GLN Z 81  1 ? 6  
HELX_P HELX_P30 AD3 ALA F 116 ? TRP F 121 ? ALA Z 116 TRP Z 121 5 ? 6  
HELX_P HELX_P31 AD4 ARG F 123 ? ARG F 132 ? ARG Z 123 ARG Z 132 1 ? 10 
HELX_P HELX_P32 AD5 PRO F 163 ? GLY F 177 ? PRO Z 163 GLY Z 177 1 ? 15 
HELX_P HELX_P33 AD6 ASP F 195 ? LYS F 199 ? ASP Z 195 LYS Z 199 5 ? 5  
HELX_P HELX_P34 AD7 ASP F 202 ? PHE F 206 ? ASP Z 202 PHE Z 206 5 ? 5  
HELX_P HELX_P35 AD8 ALA F 207 ? GLN F 220 ? ALA Z 207 GLN Z 220 1 ? 14 
HELX_P HELX_P36 AD9 THR F 224 ? LYS F 244 ? THR Z 224 LYS Z 244 1 ? 21 
HELX_P HELX_P37 AE1 THR F 253 ? ASN F 262 ? THR Z 253 ASN Z 262 1 ? 10 
HELX_P HELX_P38 AE2 ALA F 283 ? LEU F 287 ? ALA Z 283 LEU Z 287 5 ? 5  
HELX_P HELX_P39 AE3 LYS F 290 ? SER F 302 ? LYS Z 290 SER Z 302 1 ? 13 
HELX_P HELX_P40 AE4 ARG F 316 ? ASN F 332 ? ARG Z 316 ASN Z 332 1 ? 17 
HELX_P HELX_P41 AE5 ASP F 335 ? LYS F 343 ? ASP Z 335 LYS Z 343 1 ? 9  
HELX_P HELX_P42 AE6 ARG F 364 ? ARG F 367 ? ARG Z 364 ARG Z 367 5 ? 4  
HELX_P HELX_P43 AE7 GLY F 368 ? GLY F 378 ? GLY Z 368 GLY Z 378 1 ? 11 
HELX_P HELX_P44 AE8 ILE F 392 ? ASP F 402 ? ILE Z 392 ASP Z 402 1 ? 11 
HELX_P HELX_P45 AE9 ASP F 402 ? ASN F 410 ? ASP Z 402 ASN Z 410 1 ? 9  
HELX_P HELX_P46 AF1 ASN F 410 ? SER F 420 ? ASN Z 410 SER Z 420 1 ? 11 
HELX_P HELX_P47 AF2 ASN F 442 ? ARG F 451 ? ASN Z 442 ARG Z 451 1 ? 10 
HELX_P HELX_P48 AF3 GLN F 469 ? TYR F 483 ? GLN Z 469 TYR Z 483 1 ? 15 
HELX_P HELX_P49 AF4 LYS F 550 ? LEU F 554 ? LYS Z 550 LEU Z 554 5 ? 5  
HELX_P HELX_P50 AF5 LYS F 557 ? ASP F 571 ? LYS Z 557 ASP Z 571 1 ? 15 
HELX_P HELX_P51 AF6 VAL F 593 ? PHE F 597 ? VAL Z 593 PHE Z 597 5 ? 5  
HELX_P HELX_P52 AF7 THR F 612 ? GLY F 624 ? THR Z 612 GLY Z 624 1 ? 13 
HELX_P HELX_P53 AF8 ASN F 648 ? ASN F 661 ? ASN Z 648 ASN Z 661 1 ? 14 
HELX_P HELX_P54 AF9 ASP F 668 ? GLY F 670 ? ASP Z 668 GLY Z 670 5 ? 3  
# 
_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 9   OD2   ? ? ? 1_555 G CA  .  CA    ? ? A ASP 9   A CA  701 1_555 ? ? ? ? ? ? ?            2.100 ? ? 
metalc2  metalc ? ? A ASP 91  OD1   ? ? ? 1_555 G CA  .  CA    ? ? A ASP 91  A CA  701 1_555 ? ? ? ? ? ? ?            2.432 ? ? 
metalc3  metalc ? ? A ASP 91  OD2   ? ? ? 1_555 H CA  .  CA    ? ? A ASP 91  A CA  702 1_555 ? ? ? ? ? ? ?            2.561 ? ? 
metalc4  metalc ? ? A PHE 110 O     ? ? ? 1_555 H CA  .  CA    ? ? A PHE 110 A CA  702 1_555 ? ? ? ? ? ? ?            2.196 ? ? 
metalc5  metalc ? ? A GLU 470 OE1   ? ? ? 1_555 I CA  .  CA    ? ? A GLU 470 A CA  703 1_555 ? ? ? ? ? ? ?            2.487 ? ? 
metalc6  metalc ? ? A ASP 499 OD1   ? ? ? 1_555 H CA  .  CA    ? ? A ASP 499 A CA  702 1_555 ? ? ? ? ? ? ?            2.893 ? ? 
metalc7  metalc ? ? A ASP 499 OD2   ? ? ? 1_555 H CA  .  CA    ? ? A ASP 499 A CA  702 1_555 ? ? ? ? ? ? ?            2.988 ? ? 
metalc8  metalc ? ? A ASP 528 OD1   ? ? ? 1_555 I CA  .  CA    ? ? A ASP 528 A CA  703 1_555 ? ? ? ? ? ? ?            2.616 ? ? 
metalc9  metalc ? ? A ASP 528 OD2   ? ? ? 1_555 I CA  .  CA    ? ? A ASP 528 A CA  703 1_555 ? ? ? ? ? ? ?            2.144 ? ? 
metalc10 metalc ? ? G CA  .   CA    ? ? ? 1_555 B DG  5  "O3'" ? ? A CA  701 E DG  5   1_555 ? ? ? ? ? ? ?            2.837 ? ? 
metalc11 metalc ? ? G CA  .   CA    ? ? ? 1_555 B DC  6  OP1   ? ? A CA  701 E DC  6   1_555 ? ? ? ? ? ? ?            2.941 ? ? 
metalc12 metalc ? ? H CA  .   CA    ? ? ? 1_555 B DC  6  OP1   ? ? A CA  702 E DC  6   1_555 ? ? ? ? ? ? ?            2.846 ? ? 
metalc13 metalc ? ? E DG  5   "O3'" ? ? ? 1_555 K CA  .  CA    ? ? V DG  5   Z CA  702 1_555 ? ? ? ? ? ? ?            2.843 ? ? 
metalc14 metalc ? ? E DC  6   OP1   ? ? ? 1_555 J CA  .  CA    ? ? V DC  6   Z CA  701 1_555 ? ? ? ? ? ? ?            2.691 ? ? 
metalc15 metalc ? ? E DC  6   OP1   ? ? ? 1_555 K CA  .  CA    ? ? V DC  6   Z CA  702 1_555 ? ? ? ? ? ? ?            2.834 ? ? 
metalc16 metalc ? ? F ASP 9   OD2   ? ? ? 1_555 K CA  .  CA    ? ? Z ASP 9   Z CA  702 1_555 ? ? ? ? ? ? ?            2.091 ? ? 
metalc17 metalc ? ? F ASP 91  OD1   ? ? ? 1_555 J CA  .  CA    ? ? Z ASP 91  Z CA  701 1_555 ? ? ? ? ? ? ?            3.153 ? ? 
metalc18 metalc ? ? F ASP 91  OD2   ? ? ? 1_555 J CA  .  CA    ? ? Z ASP 91  Z CA  701 1_555 ? ? ? ? ? ? ?            2.224 ? ? 
metalc19 metalc ? ? F ASP 91  OD1   ? ? ? 1_555 K CA  .  CA    ? ? Z ASP 91  Z CA  702 1_555 ? ? ? ? ? ? ?            2.221 ? ? 
metalc20 metalc ? ? F GLU 109 OE2   ? ? ? 1_555 J CA  .  CA    ? ? Z GLU 109 Z CA  701 1_555 ? ? ? ? ? ? ?            2.700 ? ? 
metalc21 metalc ? ? F PHE 110 O     ? ? ? 1_555 J CA  .  CA    ? ? Z PHE 110 Z CA  701 1_555 ? ? ? ? ? ? ?            2.150 ? ? 
metalc22 metalc ? ? F GLU 470 OE1   ? ? ? 1_555 L CA  .  CA    ? ? Z GLU 470 Z CA  703 1_555 ? ? ? ? ? ? ?            2.155 ? ? 
metalc23 metalc ? ? F ASP 528 OD1   ? ? ? 1_555 L CA  .  CA    ? ? Z ASP 528 Z CA  703 1_555 ? ? ? ? ? ? ?            3.154 ? ? 
metalc24 metalc ? ? F ASP 528 OD2   ? ? ? 1_555 L CA  .  CA    ? ? Z ASP 528 Z CA  703 1_555 ? ? ? ? ? ? ?            2.266 ? ? 
metalc25 metalc ? ? F SER 547 O     ? ? ? 1_555 L CA  .  CA    ? ? Z SER 547 Z CA  703 1_555 ? ? ? ? ? ? ?            3.004 ? ? 
metalc26 metalc ? ? K CA  .   CA    ? ? ? 1_555 T HOH .  O     ? ? Z CA  702 Z HOH 809 1_555 ? ? ? ? ? ? ?            2.915 ? ? 
hydrog1  hydrog ? ? B DG  1   N1    ? ? ? 1_555 C DC  13 N3    ? ? E DG  1   F DC  13  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog2  hydrog ? ? B DG  1   N2    ? ? ? 1_555 C DC  13 O2    ? ? E DG  1   F DC  13  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog3  hydrog ? ? B DG  1   O6    ? ? ? 1_555 C DC  13 N4    ? ? E DG  1   F DC  13  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog4  hydrog ? ? B DT  2   N3    ? ? ? 1_555 C DA  12 N1    ? ? E DT  2   F DA  12  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog5  hydrog ? ? B DT  2   O4    ? ? ? 1_555 C DA  12 N6    ? ? E DT  2   F DA  12  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog6  hydrog ? ? B DC  3   N3    ? ? ? 1_555 C DG  11 N1    ? ? E DC  3   F DG  11  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog7  hydrog ? ? B DC  3   N4    ? ? ? 1_555 C DG  11 O6    ? ? E DC  3   F DG  11  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog8  hydrog ? ? B DC  3   O2    ? ? ? 1_555 C DG  11 N2    ? ? E DC  3   F DG  11  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog9  hydrog ? ? B DT  4   N3    ? ? ? 1_555 C DA  10 N1    ? ? E DT  4   F DA  10  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog10 hydrog ? ? B DT  4   O4    ? ? ? 1_555 C DA  10 N6    ? ? E DT  4   F DA  10  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog11 hydrog ? ? B DG  5   N1    ? ? ? 1_555 C DC  9  N3    ? ? E DG  5   F DC  9   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog12 hydrog ? ? B DG  5   N2    ? ? ? 1_555 C DC  9  O2    ? ? E DG  5   F DC  9   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog13 hydrog ? ? B DG  5   O6    ? ? ? 1_555 C DC  9  N4    ? ? E DG  5   F DC  9   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog14 hydrog ? ? B DC  6   N3    ? ? ? 1_555 C DG  8  N1    ? ? E DC  6   F DG  8   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog15 hydrog ? ? B DC  6   N4    ? ? ? 1_555 C DG  8  O6    ? ? E DC  6   F DG  8   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog16 hydrog ? ? B DC  6   O2    ? ? ? 1_555 C DG  8  N2    ? ? E DC  6   F DG  8   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog17 hydrog ? ? B DA  7   N1    ? ? ? 1_555 C DT  7  N3    ? ? E DA  7   F DT  7   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog18 hydrog ? ? B DA  7   N6    ? ? ? 1_555 C DT  7  O4    ? ? E DA  7   F DT  7   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog19 hydrog ? ? B DT  8   N3    ? ? ? 1_555 C DA  6  N1    ? ? E DT  8   F DA  6   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog20 hydrog ? ? B DT  8   O4    ? ? ? 1_555 C DA  6  N6    ? ? E DT  8   F DA  6   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog21 hydrog ? ? B DT  9   N3    ? ? ? 1_555 C DA  5  N1    ? ? E DT  9   F DA  5   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog22 hydrog ? ? B DT  9   O4    ? ? ? 1_555 C DA  5  N6    ? ? E DT  9   F DA  5   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog23 hydrog ? ? B DC  10  N3    ? ? ? 1_555 C DG  4  N1    ? ? E DC  10  F DG  4   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog24 hydrog ? ? B DC  10  N4    ? ? ? 1_555 C DG  4  O6    ? ? E DC  10  F DG  4   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog25 hydrog ? ? B DC  10  O2    ? ? ? 1_555 C DG  4  N2    ? ? E DC  10  F DG  4   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog26 hydrog ? ? B DC  11  N3    ? ? ? 1_555 C DG  3  N1    ? ? E DC  11  F DG  3   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog27 hydrog ? ? B DC  11  N4    ? ? ? 1_555 C DG  3  O6    ? ? E DC  11  F DG  3   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog28 hydrog ? ? B DC  11  O2    ? ? ? 1_555 C DG  3  N2    ? ? E DC  11  F DG  3   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog29 hydrog ? ? B DT  12  N3    ? ? ? 1_555 C DA  2  N1    ? ? E DT  12  F DA  2   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog30 hydrog ? ? B DT  12  O4    ? ? ? 1_555 C DA  2  N6    ? ? E DT  12  F DA  2   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog31 hydrog ? ? B DC  13  N3    ? ? ? 1_555 C DG  1  N1    ? ? E DC  13  F DG  1   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog32 hydrog ? ? B DC  13  N4    ? ? ? 1_555 C DG  1  O6    ? ? E DC  13  F DG  1   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog33 hydrog ? ? B DC  13  O2    ? ? ? 1_555 C DG  1  N2    ? ? E DC  13  F DG  1   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog34 hydrog ? ? D DG  1   N1    ? ? ? 1_555 E DC  13 N3    ? ? U DG  1   V DC  13  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog35 hydrog ? ? D DG  1   N2    ? ? ? 1_555 E DC  13 O2    ? ? U DG  1   V DC  13  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog36 hydrog ? ? D DG  1   O6    ? ? ? 1_555 E DC  13 N4    ? ? U DG  1   V DC  13  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog37 hydrog ? ? D DA  2   N1    ? ? ? 1_555 E DT  12 N3    ? ? U DA  2   V DT  12  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog38 hydrog ? ? D DA  2   N6    ? ? ? 1_555 E DT  12 O4    ? ? U DA  2   V DT  12  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog39 hydrog ? ? D DG  3   N1    ? ? ? 1_555 E DC  11 N3    ? ? U DG  3   V DC  11  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog40 hydrog ? ? D DG  3   N2    ? ? ? 1_555 E DC  11 O2    ? ? U DG  3   V DC  11  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog41 hydrog ? ? D DG  3   O6    ? ? ? 1_555 E DC  11 N4    ? ? U DG  3   V DC  11  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog42 hydrog ? ? D DG  4   N1    ? ? ? 1_555 E DC  10 N3    ? ? U DG  4   V DC  10  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog43 hydrog ? ? D DG  4   N2    ? ? ? 1_555 E DC  10 O2    ? ? U DG  4   V DC  10  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog44 hydrog ? ? D DG  4   O6    ? ? ? 1_555 E DC  10 N4    ? ? U DG  4   V DC  10  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog45 hydrog ? ? D DA  5   N1    ? ? ? 1_555 E DT  9  N3    ? ? U DA  5   V DT  9   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog46 hydrog ? ? D DA  5   N6    ? ? ? 1_555 E DT  9  O4    ? ? U DA  5   V DT  9   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog47 hydrog ? ? D DA  6   N1    ? ? ? 1_555 E DT  8  N3    ? ? U DA  6   V DT  8   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog48 hydrog ? ? D DA  6   N6    ? ? ? 1_555 E DT  8  O4    ? ? U DA  6   V DT  8   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog49 hydrog ? ? D DT  7   N3    ? ? ? 1_555 E DA  7  N1    ? ? U DT  7   V DA  7   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog50 hydrog ? ? D DT  7   O4    ? ? ? 1_555 E DA  7  N6    ? ? U DT  7   V DA  7   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog51 hydrog ? ? D DG  8   N1    ? ? ? 1_555 E DC  6  N3    ? ? U DG  8   V DC  6   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog52 hydrog ? ? D DG  8   N2    ? ? ? 1_555 E DC  6  O2    ? ? U DG  8   V DC  6   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog53 hydrog ? ? D DG  8   O6    ? ? ? 1_555 E DC  6  N4    ? ? U DG  8   V DC  6   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog54 hydrog ? ? D DC  9   N3    ? ? ? 1_555 E DG  5  N1    ? ? U DC  9   V DG  5   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog55 hydrog ? ? D DC  9   N4    ? ? ? 1_555 E DG  5  O6    ? ? U DC  9   V DG  5   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog56 hydrog ? ? D DC  9   O2    ? ? ? 1_555 E DG  5  N2    ? ? U DC  9   V DG  5   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog57 hydrog ? ? D DA  10  N1    ? ? ? 1_555 E DT  4  N3    ? ? U DA  10  V DT  4   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog58 hydrog ? ? D DA  10  N6    ? ? ? 1_555 E DT  4  O4    ? ? U DA  10  V DT  4   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog59 hydrog ? ? D DG  11  N1    ? ? ? 1_555 E DC  3  N3    ? ? U DG  11  V DC  3   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog60 hydrog ? ? D DG  11  N2    ? ? ? 1_555 E DC  3  O2    ? ? U DG  11  V DC  3   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog61 hydrog ? ? D DG  11  O6    ? ? ? 1_555 E DC  3  N4    ? ? U DG  11  V DC  3   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog62 hydrog ? ? D DA  12  N1    ? ? ? 1_555 E DT  2  N3    ? ? U DA  12  V DT  2   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog63 hydrog ? ? D DA  12  N6    ? ? ? 1_555 E DT  2  O4    ? ? U DA  12  V DT  2   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog64 hydrog ? ? D DC  13  N3    ? ? ? 1_555 E DG  1  N1    ? ? U DC  13  V DG  1   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog65 hydrog ? ? D DC  13  N4    ? ? ? 1_555 E DG  1  O6    ? ? U DC  13  V DG  1   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog66 hydrog ? ? D DC  13  O2    ? ? ? 1_555 E DG  1  N2    ? ? U DC  13  V DG  1   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
metalc ? ? 
hydrog ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD2   ? A ASP 9   ? A ASP 9   ? 1_555 CA ? G CA . ? A CA 701 ? 1_555 OD1   ? A ASP 91  ? A ASP 91  ? 1_555 82.0  ? 
2  OD2   ? A ASP 9   ? A ASP 9   ? 1_555 CA ? G CA . ? A CA 701 ? 1_555 "O3'" ? B DG  5   ? E DG  5   ? 1_555 165.8 ? 
3  OD1   ? A ASP 91  ? A ASP 91  ? 1_555 CA ? G CA . ? A CA 701 ? 1_555 "O3'" ? B DG  5   ? E DG  5   ? 1_555 112.1 ? 
4  OD2   ? A ASP 9   ? A ASP 9   ? 1_555 CA ? G CA . ? A CA 701 ? 1_555 OP1   ? B DC  6   ? E DC  6   ? 1_555 142.0 ? 
5  OD1   ? A ASP 91  ? A ASP 91  ? 1_555 CA ? G CA . ? A CA 701 ? 1_555 OP1   ? B DC  6   ? E DC  6   ? 1_555 66.0  ? 
6  "O3'" ? B DG  5   ? E DG  5   ? 1_555 CA ? G CA . ? A CA 701 ? 1_555 OP1   ? B DC  6   ? E DC  6   ? 1_555 51.2  ? 
7  OD2   ? A ASP 91  ? A ASP 91  ? 1_555 CA ? H CA . ? A CA 702 ? 1_555 O     ? A PHE 110 ? A PHE 110 ? 1_555 77.4  ? 
8  OD2   ? A ASP 91  ? A ASP 91  ? 1_555 CA ? H CA . ? A CA 702 ? 1_555 OD1   ? A ASP 499 ? A ASP 499 ? 1_555 95.4  ? 
9  O     ? A PHE 110 ? A PHE 110 ? 1_555 CA ? H CA . ? A CA 702 ? 1_555 OD1   ? A ASP 499 ? A ASP 499 ? 1_555 109.6 ? 
10 OD2   ? A ASP 91  ? A ASP 91  ? 1_555 CA ? H CA . ? A CA 702 ? 1_555 OD2   ? A ASP 499 ? A ASP 499 ? 1_555 101.7 ? 
11 O     ? A PHE 110 ? A PHE 110 ? 1_555 CA ? H CA . ? A CA 702 ? 1_555 OD2   ? A ASP 499 ? A ASP 499 ? 1_555 69.0  ? 
12 OD1   ? A ASP 499 ? A ASP 499 ? 1_555 CA ? H CA . ? A CA 702 ? 1_555 OD2   ? A ASP 499 ? A ASP 499 ? 1_555 43.8  ? 
13 OD2   ? A ASP 91  ? A ASP 91  ? 1_555 CA ? H CA . ? A CA 702 ? 1_555 OP1   ? B DC  6   ? E DC  6   ? 1_555 93.4  ? 
14 O     ? A PHE 110 ? A PHE 110 ? 1_555 CA ? H CA . ? A CA 702 ? 1_555 OP1   ? B DC  6   ? E DC  6   ? 1_555 146.0 ? 
15 OD1   ? A ASP 499 ? A ASP 499 ? 1_555 CA ? H CA . ? A CA 702 ? 1_555 OP1   ? B DC  6   ? E DC  6   ? 1_555 103.7 ? 
16 OD2   ? A ASP 499 ? A ASP 499 ? 1_555 CA ? H CA . ? A CA 702 ? 1_555 OP1   ? B DC  6   ? E DC  6   ? 1_555 144.8 ? 
17 OE1   ? A GLU 470 ? A GLU 470 ? 1_555 CA ? I CA . ? A CA 703 ? 1_555 OD1   ? A ASP 528 ? A ASP 528 ? 1_555 172.1 ? 
18 OE1   ? A GLU 470 ? A GLU 470 ? 1_555 CA ? I CA . ? A CA 703 ? 1_555 OD2   ? A ASP 528 ? A ASP 528 ? 1_555 129.8 ? 
19 OD1   ? A ASP 528 ? A ASP 528 ? 1_555 CA ? I CA . ? A CA 703 ? 1_555 OD2   ? A ASP 528 ? A ASP 528 ? 1_555 53.8  ? 
20 "O3'" ? E DG  5   ? V DG  5   ? 1_555 CA ? K CA . ? Z CA 702 ? 1_555 OP1   ? E DC  6   ? V DC  6   ? 1_555 52.2  ? 
21 "O3'" ? E DG  5   ? V DG  5   ? 1_555 CA ? K CA . ? Z CA 702 ? 1_555 OD2   ? F ASP 9   ? Z ASP 9   ? 1_555 155.9 ? 
22 OP1   ? E DC  6   ? V DC  6   ? 1_555 CA ? K CA . ? Z CA 702 ? 1_555 OD2   ? F ASP 9   ? Z ASP 9   ? 1_555 151.1 ? 
23 "O3'" ? E DG  5   ? V DG  5   ? 1_555 CA ? K CA . ? Z CA 702 ? 1_555 OD1   ? F ASP 91  ? Z ASP 91  ? 1_555 115.8 ? 
24 OP1   ? E DC  6   ? V DC  6   ? 1_555 CA ? K CA . ? Z CA 702 ? 1_555 OD1   ? F ASP 91  ? Z ASP 91  ? 1_555 69.7  ? 
25 OD2   ? F ASP 9   ? Z ASP 9   ? 1_555 CA ? K CA . ? Z CA 702 ? 1_555 OD1   ? F ASP 91  ? Z ASP 91  ? 1_555 87.2  ? 
26 "O3'" ? E DG  5   ? V DG  5   ? 1_555 CA ? K CA . ? Z CA 702 ? 1_555 O     ? T HOH .   ? Z HOH 809 ? 1_555 76.5  ? 
27 OP1   ? E DC  6   ? V DC  6   ? 1_555 CA ? K CA . ? Z CA 702 ? 1_555 O     ? T HOH .   ? Z HOH 809 ? 1_555 119.0 ? 
28 OD2   ? F ASP 9   ? Z ASP 9   ? 1_555 CA ? K CA . ? Z CA 702 ? 1_555 O     ? T HOH .   ? Z HOH 809 ? 1_555 86.7  ? 
29 OD1   ? F ASP 91  ? Z ASP 91  ? 1_555 CA ? K CA . ? Z CA 702 ? 1_555 O     ? T HOH .   ? Z HOH 809 ? 1_555 118.0 ? 
30 OP1   ? E DC  6   ? V DC  6   ? 1_555 CA ? J CA . ? Z CA 701 ? 1_555 OD1   ? F ASP 91  ? Z ASP 91  ? 1_555 59.6  ? 
31 OP1   ? E DC  6   ? V DC  6   ? 1_555 CA ? J CA . ? Z CA 701 ? 1_555 OD2   ? F ASP 91  ? Z ASP 91  ? 1_555 103.7 ? 
32 OD1   ? F ASP 91  ? Z ASP 91  ? 1_555 CA ? J CA . ? Z CA 701 ? 1_555 OD2   ? F ASP 91  ? Z ASP 91  ? 1_555 44.2  ? 
33 OP1   ? E DC  6   ? V DC  6   ? 1_555 CA ? J CA . ? Z CA 701 ? 1_555 OE2   ? F GLU 109 ? Z GLU 109 ? 1_555 61.7  ? 
34 OD1   ? F ASP 91  ? Z ASP 91  ? 1_555 CA ? J CA . ? Z CA 701 ? 1_555 OE2   ? F GLU 109 ? Z GLU 109 ? 1_555 66.9  ? 
35 OD2   ? F ASP 91  ? Z ASP 91  ? 1_555 CA ? J CA . ? Z CA 701 ? 1_555 OE2   ? F GLU 109 ? Z GLU 109 ? 1_555 84.2  ? 
36 OP1   ? E DC  6   ? V DC  6   ? 1_555 CA ? J CA . ? Z CA 701 ? 1_555 O     ? F PHE 110 ? Z PHE 110 ? 1_555 162.9 ? 
37 OD1   ? F ASP 91  ? Z ASP 91  ? 1_555 CA ? J CA . ? Z CA 701 ? 1_555 O     ? F PHE 110 ? Z PHE 110 ? 1_555 130.6 ? 
38 OD2   ? F ASP 91  ? Z ASP 91  ? 1_555 CA ? J CA . ? Z CA 701 ? 1_555 O     ? F PHE 110 ? Z PHE 110 ? 1_555 87.2  ? 
39 OE2   ? F GLU 109 ? Z GLU 109 ? 1_555 CA ? J CA . ? Z CA 701 ? 1_555 O     ? F PHE 110 ? Z PHE 110 ? 1_555 107.2 ? 
40 OE1   ? F GLU 470 ? Z GLU 470 ? 1_555 CA ? L CA . ? Z CA 703 ? 1_555 OD1   ? F ASP 528 ? Z ASP 528 ? 1_555 146.6 ? 
41 OE1   ? F GLU 470 ? Z GLU 470 ? 1_555 CA ? L CA . ? Z CA 703 ? 1_555 OD2   ? F ASP 528 ? Z ASP 528 ? 1_555 142.8 ? 
42 OD1   ? F ASP 528 ? Z ASP 528 ? 1_555 CA ? L CA . ? Z CA 703 ? 1_555 OD2   ? F ASP 528 ? Z ASP 528 ? 1_555 44.1  ? 
43 OE1   ? F GLU 470 ? Z GLU 470 ? 1_555 CA ? L CA . ? Z CA 703 ? 1_555 O     ? F SER 547 ? Z SER 547 ? 1_555 82.7  ? 
44 OD1   ? F ASP 528 ? Z ASP 528 ? 1_555 CA ? L CA . ? Z CA 703 ? 1_555 O     ? F SER 547 ? Z SER 547 ? 1_555 121.2 ? 
45 OD2   ? F ASP 528 ? Z ASP 528 ? 1_555 CA ? L CA . ? Z CA 703 ? 1_555 O     ? F SER 547 ? Z SER 547 ? 1_555 77.5  ? 
# 
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 PHE 143 A . ? PHE 143 A VAL 144 A ? VAL 144 A 1 2.23  
2 ASN 636 A . ? ASN 636 A PRO 637 A ? PRO 637 A 1 -7.06 
3 PHE 143 F . ? PHE 143 Z VAL 144 F ? VAL 144 Z 1 2.67  
4 ASN 636 F . ? ASN 636 Z PRO 637 F ? PRO 637 Z 1 -6.93 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 6 ? 
AA3 ? 7 ? 
AA4 ? 4 ? 
AA5 ? 8 ? 
AA6 ? 6 ? 
AA7 ? 7 ? 
AA8 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? anti-parallel 
AA3 6 7 ? parallel      
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? parallel      
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA5 6 7 ? parallel      
AA5 7 8 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA6 5 6 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? parallel      
AA7 4 5 ? parallel      
AA7 5 6 ? anti-parallel 
AA7 6 7 ? parallel      
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? 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 LYS A 29  ? PHE A 34  ? LYS A 29  PHE A 34  
AA1 2 PRO A 40  ? GLU A 48  ? PRO A 40  GLU A 48  
AA1 3 ASP A 51  ? PRO A 61  ? ASP A 51  PRO A 61  
AA1 4 ASN A 2   ? GLY A 8   ? ASN A 2   GLY A 8   
AA1 5 VAL A 92  ? ASN A 98  ? VAL A 92  ASN A 98  
AA1 6 LYS A 101 ? CYS A 111 ? LYS A 101 CYS A 111 
AA1 7 TYR A 137 ? PHE A 143 ? TYR A 137 PHE A 143 
AA1 8 ILE A 180 ? ARG A 186 ? ILE A 180 ARG A 186 
AA2 1 VAL A 303 ? GLY A 304 ? VAL A 303 GLY A 304 
AA2 2 PHE A 312 ? ILE A 315 ? PHE A 312 ILE A 315 
AA2 3 LEU A 348 ? LEU A 353 ? LEU A 348 LEU A 353 
AA2 4 GLN A 382 ? ILE A 387 ? GLN A 382 ILE A 387 
AA2 5 PHE A 422 ? CYS A 427 ? PHE A 422 CYS A 427 
AA2 6 GLU A 436 ? ILE A 441 ? GLU A 436 ILE A 441 
AA3 1 CYS A 488 ? CYS A 493 ? CYS A 488 CYS A 493 
AA3 2 HIS A 529 ? ILE A 533 ? HIS A 529 ILE A 533 
AA3 3 LEU A 541 ? SER A 547 ? LEU A 541 SER A 547 
AA3 4 ILE A 598 ? ILE A 606 ? ILE A 598 ILE A 606 
AA3 5 LEU A 627 ? GLN A 634 ? LEU A 627 GLN A 634 
AA3 6 LYS A 639 ? PRO A 646 ? LYS A 639 PRO A 646 
AA3 7 PHE A 672 ? GLY A 676 ? PHE A 672 GLY A 676 
AA4 1 LEU A 503 ? ARG A 507 ? LEU A 503 ARG A 507 
AA4 2 HIS A 510 ? TRP A 514 ? HIS A 510 TRP A 514 
AA4 3 VAL A 576 ? LYS A 579 ? VAL A 576 LYS A 579 
AA4 4 GLU A 586 ? PHE A 587 ? GLU A 586 PHE A 587 
AA5 1 LYS F 29  ? PHE F 34  ? LYS Z 29  PHE Z 34  
AA5 2 PRO F 40  ? GLU F 48  ? PRO Z 40  GLU Z 48  
AA5 3 ASP F 51  ? PRO F 61  ? ASP Z 51  PRO Z 61  
AA5 4 ASN F 2   ? GLY F 8   ? ASN Z 2   GLY Z 8   
AA5 5 VAL F 92  ? ASN F 98  ? VAL Z 92  ASN Z 98  
AA5 6 LYS F 101 ? CYS F 111 ? LYS Z 101 CYS Z 111 
AA5 7 TYR F 137 ? PHE F 143 ? TYR Z 137 PHE Z 143 
AA5 8 ILE F 180 ? ARG F 186 ? ILE Z 180 ARG Z 186 
AA6 1 VAL F 303 ? GLY F 304 ? VAL Z 303 GLY Z 304 
AA6 2 PHE F 312 ? ILE F 315 ? PHE Z 312 ILE Z 315 
AA6 3 LEU F 348 ? LEU F 353 ? LEU Z 348 LEU Z 353 
AA6 4 GLN F 382 ? ILE F 387 ? GLN Z 382 ILE Z 387 
AA6 5 PHE F 422 ? CYS F 427 ? PHE Z 422 CYS Z 427 
AA6 6 GLU F 436 ? ILE F 441 ? GLU Z 436 ILE Z 441 
AA7 1 CYS F 488 ? CYS F 493 ? CYS Z 488 CYS Z 493 
AA7 2 HIS F 529 ? ILE F 533 ? HIS Z 529 ILE Z 533 
AA7 3 LEU F 541 ? SER F 547 ? LEU Z 541 SER Z 547 
AA7 4 ILE F 598 ? ILE F 606 ? ILE Z 598 ILE Z 606 
AA7 5 LEU F 627 ? GLN F 634 ? LEU Z 627 GLN Z 634 
AA7 6 LYS F 639 ? PRO F 646 ? LYS Z 639 PRO Z 646 
AA7 7 PHE F 672 ? GLY F 676 ? PHE Z 672 GLY Z 676 
AA8 1 LEU F 503 ? ARG F 507 ? LEU Z 503 ARG Z 507 
AA8 2 HIS F 510 ? TRP F 514 ? HIS Z 510 TRP Z 514 
AA8 3 VAL F 576 ? LYS F 579 ? VAL Z 576 LYS Z 579 
AA8 4 GLU F 586 ? PHE F 587 ? GLU Z 586 PHE Z 587 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LYS A 31  ? N LYS A 31  O GLU A 43  ? O GLU A 43  
AA1 2 3 N PRO A 40  ? N PRO A 40  O MET A 59  ? O MET A 59  
AA1 3 4 O ARG A 56  ? O ARG A 56  N PHE A 4   ? N PHE A 4   
AA1 4 5 N HIS A 7   ? N HIS A 7   O ILE A 93  ? O ILE A 93  
AA1 5 6 N ILE A 94  ? N ILE A 94  O LEU A 105 ? O LEU A 105 
AA1 6 7 N CYS A 111 ? N CYS A 111 O ILE A 140 ? O ILE A 140 
AA1 7 8 N PHE A 143 ? N PHE A 143 O PHE A 185 ? O PHE A 185 
AA2 1 2 N VAL A 303 ? N VAL A 303 O VAL A 314 ? O VAL A 314 
AA2 2 3 N ILE A 315 ? N ILE A 315 O LEU A 348 ? O LEU A 348 
AA2 3 4 N CYS A 351 ? N CYS A 351 O PHE A 386 ? O PHE A 386 
AA2 4 5 N THR A 385 ? N THR A 385 O VAL A 424 ? O VAL A 424 
AA2 5 6 N ILE A 423 ? N ILE A 423 O ILE A 440 ? O ILE A 440 
AA3 1 2 N PHE A 489 ? N PHE A 489 O GLN A 532 ? O GLN A 532 
AA3 2 3 N HIS A 529 ? N HIS A 529 O ILE A 545 ? O ILE A 545 
AA3 3 4 N LEU A 542 ? N LEU A 542 O ILE A 598 ? O ILE A 598 
AA3 4 5 N GLY A 603 ? N GLY A 603 O ILE A 629 ? O ILE A 629 
AA3 5 6 N LYS A 632 ? N LYS A 632 O VAL A 641 ? O VAL A 641 
AA3 6 7 N PHE A 644 ? N PHE A 644 O GLY A 676 ? O GLY A 676 
AA4 1 2 N ILE A 505 ? N ILE A 505 O PHE A 512 ? O PHE A 512 
AA4 2 3 N ARG A 513 ? N ARG A 513 O VAL A 576 ? O VAL A 576 
AA4 3 4 N GLN A 577 ? N GLN A 577 O GLU A 586 ? O GLU A 586 
AA5 1 2 N LYS F 31  ? N LYS Z 31  O GLU F 43  ? O GLU Z 43  
AA5 2 3 N PRO F 40  ? N PRO Z 40  O MET F 59  ? O MET Z 59  
AA5 3 4 O ARG F 56  ? O ARG Z 56  N PHE F 4   ? N PHE Z 4   
AA5 4 5 N HIS F 7   ? N HIS Z 7   O ILE F 93  ? O ILE Z 93  
AA5 5 6 N ILE F 94  ? N ILE Z 94  O LEU F 105 ? O LEU Z 105 
AA5 6 7 N CYS F 111 ? N CYS Z 111 O ILE F 140 ? O ILE Z 140 
AA5 7 8 N PHE F 143 ? N PHE Z 143 O PHE F 185 ? O PHE Z 185 
AA6 1 2 N VAL F 303 ? N VAL Z 303 O VAL F 314 ? O VAL Z 314 
AA6 2 3 N ILE F 315 ? N ILE Z 315 O LEU F 348 ? O LEU Z 348 
AA6 3 4 N CYS F 351 ? N CYS Z 351 O PHE F 386 ? O PHE Z 386 
AA6 4 5 N THR F 385 ? N THR Z 385 O VAL F 424 ? O VAL Z 424 
AA6 5 6 N ILE F 423 ? N ILE Z 423 O ILE F 440 ? O ILE Z 440 
AA7 1 2 N PHE F 489 ? N PHE Z 489 O GLN F 532 ? O GLN Z 532 
AA7 2 3 N HIS F 529 ? N HIS Z 529 O ILE F 545 ? O ILE Z 545 
AA7 3 4 N LEU F 542 ? N LEU Z 542 O ILE F 598 ? O ILE Z 598 
AA7 4 5 N GLY F 603 ? N GLY Z 603 O ILE F 629 ? O ILE Z 629 
AA7 5 6 N LYS F 632 ? N LYS Z 632 O VAL F 641 ? O VAL Z 641 
AA7 6 7 N PHE F 644 ? N PHE Z 644 O GLY F 676 ? O GLY Z 676 
AA8 1 2 N ILE F 505 ? N ILE Z 505 O PHE F 512 ? O PHE Z 512 
AA8 2 3 N ARG F 513 ? N ARG Z 513 O VAL F 576 ? O VAL Z 576 
AA8 3 4 N GLN F 577 ? N GLN Z 577 O GLU F 586 ? O GLU Z 586 
# 
_pdbx_entry_details.entry_id                   9F38 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 "O4'" F DG 3 ? ? "C1'" F DG 3 ? ? N9 F DG 3 ? ? 110.88 108.30 2.58 0.30 N 
2 1 "O4'" U DG 3 ? ? "C1'" U DG 3 ? ? N9 U DG 3 ? ? 111.10 108.30 2.80 0.30 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 66  ? ? -98.75  -97.15  
2  1 THR A 67  ? ? -142.62 -44.42  
3  1 ARG A 70  ? ? -106.11 -69.48  
4  1 TYR A 87  ? ? -86.80  48.45   
5  1 ALA A 113 ? ? -39.51  149.33  
6  1 ASN A 150 ? ? 69.42   -31.34  
7  1 ALA A 306 ? ? 74.29   -47.22  
8  1 LYS A 343 ? ? -90.71  32.59   
9  1 GLN A 469 ? ? -116.38 -163.65 
10 1 ASN Z 66  ? ? -98.92  -96.91  
11 1 THR Z 67  ? ? -142.93 -44.50  
12 1 ARG Z 70  ? ? -105.79 -69.56  
13 1 TYR Z 87  ? ? -87.16  47.87   
14 1 ASN Z 150 ? ? 70.81   -32.48  
15 1 ALA Z 306 ? ? 74.21   -46.77  
16 1 LYS Z 343 ? ? -90.99  33.75   
17 1 GLN Z 469 ? ? -115.98 -163.50 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           ? 
_pdbx_refine_tls.origin_x         7.3266 
_pdbx_refine_tls.origin_y         -21.486 
_pdbx_refine_tls.origin_z         26.0662 
_pdbx_refine_tls.T[1][1]          0.1881 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0492 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.1933 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          -0.1374 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.018 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          -0.208 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.0237 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.027 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.1488 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.2909 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.2489 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.541 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0274 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0143 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0245 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0143 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0062 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.1173 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0245 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.1173 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0336 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1 ? ? A 1 ? ? ? A 676 ? ? '{ *|* }' 
2  'X-RAY DIFFRACTION' 1 ? ? E 1 ? ? ? E 13  ? ? '{ *|* }' 
3  'X-RAY DIFFRACTION' 1 ? ? F 1 ? ? ? F 13  ? ? '{ *|* }' 
4  'X-RAY DIFFRACTION' 1 ? ? M 1 ? ? ? M 3   ? ? '{ *|* }' 
5  'X-RAY DIFFRACTION' 1 ? ? N 1 ? ? ? N 3   ? ? '{ *|* }' 
6  'X-RAY DIFFRACTION' 1 ? ? O 1 ? ? ? O 1   ? ? '{ *|* }' 
7  'X-RAY DIFFRACTION' 1 ? ? U 1 ? ? ? U 13  ? ? '{ *|* }' 
8  'X-RAY DIFFRACTION' 1 ? ? V 1 ? ? ? V 13  ? ? '{ *|* }' 
9  'X-RAY DIFFRACTION' 1 ? ? W 1 ? ? ? W 177 ? ? '{ *|* }' 
10 'X-RAY DIFFRACTION' 1 ? ? X 1 ? ? ? X 1   ? ? '{ *|* }' 
11 'X-RAY DIFFRACTION' 1 ? ? Z 1 ? ? ? Z 676 ? ? '{ *|* }' 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      Z 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       880 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.56 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
CA  CA     CA N N 74  
CL  CL     CL N N 75  
CYS N      N  N N 76  
CYS CA     C  N R 77  
CYS C      C  N N 78  
CYS O      O  N N 79  
CYS CB     C  N N 80  
CYS SG     S  N N 81  
CYS OXT    O  N N 82  
CYS H      H  N N 83  
CYS H2     H  N N 84  
CYS HA     H  N N 85  
CYS HB2    H  N N 86  
CYS HB3    H  N N 87  
CYS HG     H  N N 88  
CYS HXT    H  N N 89  
DA  OP3    O  N N 90  
DA  P      P  N N 91  
DA  OP1    O  N N 92  
DA  OP2    O  N N 93  
DA  "O5'"  O  N N 94  
DA  "C5'"  C  N N 95  
DA  "C4'"  C  N R 96  
DA  "O4'"  O  N N 97  
DA  "C3'"  C  N S 98  
DA  "O3'"  O  N N 99  
DA  "C2'"  C  N N 100 
DA  "C1'"  C  N R 101 
DA  N9     N  Y N 102 
DA  C8     C  Y N 103 
DA  N7     N  Y N 104 
DA  C5     C  Y N 105 
DA  C6     C  Y N 106 
DA  N6     N  N N 107 
DA  N1     N  Y N 108 
DA  C2     C  Y N 109 
DA  N3     N  Y N 110 
DA  C4     C  Y N 111 
DA  HOP3   H  N N 112 
DA  HOP2   H  N N 113 
DA  "H5'"  H  N N 114 
DA  "H5''" H  N N 115 
DA  "H4'"  H  N N 116 
DA  "H3'"  H  N N 117 
DA  "HO3'" H  N N 118 
DA  "H2'"  H  N N 119 
DA  "H2''" H  N N 120 
DA  "H1'"  H  N N 121 
DA  H8     H  N N 122 
DA  H61    H  N N 123 
DA  H62    H  N N 124 
DA  H2     H  N N 125 
DC  OP3    O  N N 126 
DC  P      P  N N 127 
DC  OP1    O  N N 128 
DC  OP2    O  N N 129 
DC  "O5'"  O  N N 130 
DC  "C5'"  C  N N 131 
DC  "C4'"  C  N R 132 
DC  "O4'"  O  N N 133 
DC  "C3'"  C  N S 134 
DC  "O3'"  O  N N 135 
DC  "C2'"  C  N N 136 
DC  "C1'"  C  N R 137 
DC  N1     N  N N 138 
DC  C2     C  N N 139 
DC  O2     O  N N 140 
DC  N3     N  N N 141 
DC  C4     C  N N 142 
DC  N4     N  N N 143 
DC  C5     C  N N 144 
DC  C6     C  N N 145 
DC  HOP3   H  N N 146 
DC  HOP2   H  N N 147 
DC  "H5'"  H  N N 148 
DC  "H5''" H  N N 149 
DC  "H4'"  H  N N 150 
DC  "H3'"  H  N N 151 
DC  "HO3'" H  N N 152 
DC  "H2'"  H  N N 153 
DC  "H2''" H  N N 154 
DC  "H1'"  H  N N 155 
DC  H41    H  N N 156 
DC  H42    H  N N 157 
DC  H5     H  N N 158 
DC  H6     H  N N 159 
DG  OP3    O  N N 160 
DG  P      P  N N 161 
DG  OP1    O  N N 162 
DG  OP2    O  N N 163 
DG  "O5'"  O  N N 164 
DG  "C5'"  C  N N 165 
DG  "C4'"  C  N R 166 
DG  "O4'"  O  N N 167 
DG  "C3'"  C  N S 168 
DG  "O3'"  O  N N 169 
DG  "C2'"  C  N N 170 
DG  "C1'"  C  N R 171 
DG  N9     N  Y N 172 
DG  C8     C  Y N 173 
DG  N7     N  Y N 174 
DG  C5     C  Y N 175 
DG  C6     C  N N 176 
DG  O6     O  N N 177 
DG  N1     N  N N 178 
DG  C2     C  N N 179 
DG  N2     N  N N 180 
DG  N3     N  N N 181 
DG  C4     C  Y N 182 
DG  HOP3   H  N N 183 
DG  HOP2   H  N N 184 
DG  "H5'"  H  N N 185 
DG  "H5''" H  N N 186 
DG  "H4'"  H  N N 187 
DG  "H3'"  H  N N 188 
DG  "HO3'" H  N N 189 
DG  "H2'"  H  N N 190 
DG  "H2''" H  N N 191 
DG  "H1'"  H  N N 192 
DG  H8     H  N N 193 
DG  H1     H  N N 194 
DG  H21    H  N N 195 
DG  H22    H  N N 196 
DT  OP3    O  N N 197 
DT  P      P  N N 198 
DT  OP1    O  N N 199 
DT  OP2    O  N N 200 
DT  "O5'"  O  N N 201 
DT  "C5'"  C  N N 202 
DT  "C4'"  C  N R 203 
DT  "O4'"  O  N N 204 
DT  "C3'"  C  N S 205 
DT  "O3'"  O  N N 206 
DT  "C2'"  C  N N 207 
DT  "C1'"  C  N R 208 
DT  N1     N  N N 209 
DT  C2     C  N N 210 
DT  O2     O  N N 211 
DT  N3     N  N N 212 
DT  C4     C  N N 213 
DT  O4     O  N N 214 
DT  C5     C  N N 215 
DT  C7     C  N N 216 
DT  C6     C  N N 217 
DT  HOP3   H  N N 218 
DT  HOP2   H  N N 219 
DT  "H5'"  H  N N 220 
DT  "H5''" H  N N 221 
DT  "H4'"  H  N N 222 
DT  "H3'"  H  N N 223 
DT  "HO3'" H  N N 224 
DT  "H2'"  H  N N 225 
DT  "H2''" H  N N 226 
DT  "H1'"  H  N N 227 
DT  H3     H  N N 228 
DT  H71    H  N N 229 
DT  H72    H  N N 230 
DT  H73    H  N N 231 
DT  H6     H  N N 232 
GLN N      N  N N 233 
GLN CA     C  N S 234 
GLN C      C  N N 235 
GLN O      O  N N 236 
GLN CB     C  N N 237 
GLN CG     C  N N 238 
GLN CD     C  N N 239 
GLN OE1    O  N N 240 
GLN NE2    N  N N 241 
GLN OXT    O  N N 242 
GLN H      H  N N 243 
GLN H2     H  N N 244 
GLN HA     H  N N 245 
GLN HB2    H  N N 246 
GLN HB3    H  N N 247 
GLN HG2    H  N N 248 
GLN HG3    H  N N 249 
GLN HE21   H  N N 250 
GLN HE22   H  N N 251 
GLN HXT    H  N N 252 
GLU N      N  N N 253 
GLU CA     C  N S 254 
GLU C      C  N N 255 
GLU O      O  N N 256 
GLU CB     C  N N 257 
GLU CG     C  N N 258 
GLU CD     C  N N 259 
GLU OE1    O  N N 260 
GLU OE2    O  N N 261 
GLU OXT    O  N N 262 
GLU H      H  N N 263 
GLU H2     H  N N 264 
GLU HA     H  N N 265 
GLU HB2    H  N N 266 
GLU HB3    H  N N 267 
GLU HG2    H  N N 268 
GLU HG3    H  N N 269 
GLU HE2    H  N N 270 
GLU HXT    H  N N 271 
GLY N      N  N N 272 
GLY CA     C  N N 273 
GLY C      C  N N 274 
GLY O      O  N N 275 
GLY OXT    O  N N 276 
GLY H      H  N N 277 
GLY H2     H  N N 278 
GLY HA2    H  N N 279 
GLY HA3    H  N N 280 
GLY HXT    H  N N 281 
HIS N      N  N N 282 
HIS CA     C  N S 283 
HIS C      C  N N 284 
HIS O      O  N N 285 
HIS CB     C  N N 286 
HIS CG     C  Y N 287 
HIS ND1    N  Y N 288 
HIS CD2    C  Y N 289 
HIS CE1    C  Y N 290 
HIS NE2    N  Y N 291 
HIS OXT    O  N N 292 
HIS H      H  N N 293 
HIS H2     H  N N 294 
HIS HA     H  N N 295 
HIS HB2    H  N N 296 
HIS HB3    H  N N 297 
HIS HD1    H  N N 298 
HIS HD2    H  N N 299 
HIS HE1    H  N N 300 
HIS HE2    H  N N 301 
HIS HXT    H  N N 302 
HOH O      O  N N 303 
HOH H1     H  N N 304 
HOH H2     H  N N 305 
ILE N      N  N N 306 
ILE CA     C  N S 307 
ILE C      C  N N 308 
ILE O      O  N N 309 
ILE CB     C  N S 310 
ILE CG1    C  N N 311 
ILE CG2    C  N N 312 
ILE CD1    C  N N 313 
ILE OXT    O  N N 314 
ILE H      H  N N 315 
ILE H2     H  N N 316 
ILE HA     H  N N 317 
ILE HB     H  N N 318 
ILE HG12   H  N N 319 
ILE HG13   H  N N 320 
ILE HG21   H  N N 321 
ILE HG22   H  N N 322 
ILE HG23   H  N N 323 
ILE HD11   H  N N 324 
ILE HD12   H  N N 325 
ILE HD13   H  N N 326 
ILE HXT    H  N N 327 
LEU N      N  N N 328 
LEU CA     C  N S 329 
LEU C      C  N N 330 
LEU O      O  N N 331 
LEU CB     C  N N 332 
LEU CG     C  N N 333 
LEU CD1    C  N N 334 
LEU CD2    C  N N 335 
LEU OXT    O  N N 336 
LEU H      H  N N 337 
LEU H2     H  N N 338 
LEU HA     H  N N 339 
LEU HB2    H  N N 340 
LEU HB3    H  N N 341 
LEU HG     H  N N 342 
LEU HD11   H  N N 343 
LEU HD12   H  N N 344 
LEU HD13   H  N N 345 
LEU HD21   H  N N 346 
LEU HD22   H  N N 347 
LEU HD23   H  N N 348 
LEU HXT    H  N N 349 
LYS N      N  N N 350 
LYS CA     C  N S 351 
LYS C      C  N N 352 
LYS O      O  N N 353 
LYS CB     C  N N 354 
LYS CG     C  N N 355 
LYS CD     C  N N 356 
LYS CE     C  N N 357 
LYS NZ     N  N N 358 
LYS OXT    O  N N 359 
LYS H      H  N N 360 
LYS H2     H  N N 361 
LYS HA     H  N N 362 
LYS HB2    H  N N 363 
LYS HB3    H  N N 364 
LYS HG2    H  N N 365 
LYS HG3    H  N N 366 
LYS HD2    H  N N 367 
LYS HD3    H  N N 368 
LYS HE2    H  N N 369 
LYS HE3    H  N N 370 
LYS HZ1    H  N N 371 
LYS HZ2    H  N N 372 
LYS HZ3    H  N N 373 
LYS HXT    H  N N 374 
MES O1     O  N N 375 
MES C2     C  N N 376 
MES C3     C  N N 377 
MES N4     N  N N 378 
MES C5     C  N N 379 
MES C6     C  N N 380 
MES C7     C  N N 381 
MES C8     C  N N 382 
MES S      S  N N 383 
MES O1S    O  N N 384 
MES O2S    O  N N 385 
MES O3S    O  N N 386 
MES H21    H  N N 387 
MES H22    H  N N 388 
MES H31    H  N N 389 
MES H32    H  N N 390 
MES HN4    H  N N 391 
MES H51    H  N N 392 
MES H52    H  N N 393 
MES H61    H  N N 394 
MES H62    H  N N 395 
MES H71    H  N N 396 
MES H72    H  N N 397 
MES H81    H  N N 398 
MES H82    H  N N 399 
MET N      N  N N 400 
MET CA     C  N S 401 
MET C      C  N N 402 
MET O      O  N N 403 
MET CB     C  N N 404 
MET CG     C  N N 405 
MET SD     S  N N 406 
MET CE     C  N N 407 
MET OXT    O  N N 408 
MET H      H  N N 409 
MET H2     H  N N 410 
MET HA     H  N N 411 
MET HB2    H  N N 412 
MET HB3    H  N N 413 
MET HG2    H  N N 414 
MET HG3    H  N N 415 
MET HE1    H  N N 416 
MET HE2    H  N N 417 
MET HE3    H  N N 418 
MET HXT    H  N N 419 
PHE N      N  N N 420 
PHE CA     C  N S 421 
PHE C      C  N N 422 
PHE O      O  N N 423 
PHE CB     C  N N 424 
PHE CG     C  Y N 425 
PHE CD1    C  Y N 426 
PHE CD2    C  Y N 427 
PHE CE1    C  Y N 428 
PHE CE2    C  Y N 429 
PHE CZ     C  Y N 430 
PHE OXT    O  N N 431 
PHE H      H  N N 432 
PHE H2     H  N N 433 
PHE HA     H  N N 434 
PHE HB2    H  N N 435 
PHE HB3    H  N N 436 
PHE HD1    H  N N 437 
PHE HD2    H  N N 438 
PHE HE1    H  N N 439 
PHE HE2    H  N N 440 
PHE HZ     H  N N 441 
PHE HXT    H  N N 442 
PRO N      N  N N 443 
PRO CA     C  N S 444 
PRO C      C  N N 445 
PRO O      O  N N 446 
PRO CB     C  N N 447 
PRO CG     C  N N 448 
PRO CD     C  N N 449 
PRO OXT    O  N N 450 
PRO H      H  N N 451 
PRO HA     H  N N 452 
PRO HB2    H  N N 453 
PRO HB3    H  N N 454 
PRO HG2    H  N N 455 
PRO HG3    H  N N 456 
PRO HD2    H  N N 457 
PRO HD3    H  N N 458 
PRO HXT    H  N N 459 
SER N      N  N N 460 
SER CA     C  N S 461 
SER C      C  N N 462 
SER O      O  N N 463 
SER CB     C  N N 464 
SER OG     O  N N 465 
SER OXT    O  N N 466 
SER H      H  N N 467 
SER H2     H  N N 468 
SER HA     H  N N 469 
SER HB2    H  N N 470 
SER HB3    H  N N 471 
SER HG     H  N N 472 
SER HXT    H  N N 473 
THR N      N  N N 474 
THR CA     C  N S 475 
THR C      C  N N 476 
THR O      O  N N 477 
THR CB     C  N R 478 
THR OG1    O  N N 479 
THR CG2    C  N N 480 
THR OXT    O  N N 481 
THR H      H  N N 482 
THR H2     H  N N 483 
THR HA     H  N N 484 
THR HB     H  N N 485 
THR HG1    H  N N 486 
THR HG21   H  N N 487 
THR HG22   H  N N 488 
THR HG23   H  N N 489 
THR HXT    H  N N 490 
TRP N      N  N N 491 
TRP CA     C  N S 492 
TRP C      C  N N 493 
TRP O      O  N N 494 
TRP CB     C  N N 495 
TRP CG     C  Y N 496 
TRP CD1    C  Y N 497 
TRP CD2    C  Y N 498 
TRP NE1    N  Y N 499 
TRP CE2    C  Y N 500 
TRP CE3    C  Y N 501 
TRP CZ2    C  Y N 502 
TRP CZ3    C  Y N 503 
TRP CH2    C  Y N 504 
TRP OXT    O  N N 505 
TRP H      H  N N 506 
TRP H2     H  N N 507 
TRP HA     H  N N 508 
TRP HB2    H  N N 509 
TRP HB3    H  N N 510 
TRP HD1    H  N N 511 
TRP HE1    H  N N 512 
TRP HE3    H  N N 513 
TRP HZ2    H  N N 514 
TRP HZ3    H  N N 515 
TRP HH2    H  N N 516 
TRP HXT    H  N N 517 
TYR N      N  N N 518 
TYR CA     C  N S 519 
TYR C      C  N N 520 
TYR O      O  N N 521 
TYR CB     C  N N 522 
TYR CG     C  Y N 523 
TYR CD1    C  Y N 524 
TYR CD2    C  Y N 525 
TYR CE1    C  Y N 526 
TYR CE2    C  Y N 527 
TYR CZ     C  Y N 528 
TYR OH     O  N N 529 
TYR OXT    O  N N 530 
TYR H      H  N N 531 
TYR H2     H  N N 532 
TYR HA     H  N N 533 
TYR HB2    H  N N 534 
TYR HB3    H  N N 535 
TYR HD1    H  N N 536 
TYR HD2    H  N N 537 
TYR HE1    H  N N 538 
TYR HE2    H  N N 539 
TYR HH     H  N N 540 
TYR HXT    H  N N 541 
VAL N      N  N N 542 
VAL CA     C  N S 543 
VAL C      C  N N 544 
VAL O      O  N N 545 
VAL CB     C  N N 546 
VAL CG1    C  N N 547 
VAL CG2    C  N N 548 
VAL OXT    O  N N 549 
VAL H      H  N N 550 
VAL H2     H  N N 551 
VAL HA     H  N N 552 
VAL HB     H  N N 553 
VAL HG11   H  N N 554 
VAL HG12   H  N N 555 
VAL HG13   H  N N 556 
VAL HG21   H  N N 557 
VAL HG22   H  N N 558 
VAL HG23   H  N N 559 
VAL HXT    H  N N 560 
# 
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 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
DA  OP3   P      sing N N 83  
DA  OP3   HOP3   sing N N 84  
DA  P     OP1    doub N N 85  
DA  P     OP2    sing N N 86  
DA  P     "O5'"  sing N N 87  
DA  OP2   HOP2   sing N N 88  
DA  "O5'" "C5'"  sing N N 89  
DA  "C5'" "C4'"  sing N N 90  
DA  "C5'" "H5'"  sing N N 91  
DA  "C5'" "H5''" sing N N 92  
DA  "C4'" "O4'"  sing N N 93  
DA  "C4'" "C3'"  sing N N 94  
DA  "C4'" "H4'"  sing N N 95  
DA  "O4'" "C1'"  sing N N 96  
DA  "C3'" "O3'"  sing N N 97  
DA  "C3'" "C2'"  sing N N 98  
DA  "C3'" "H3'"  sing N N 99  
DA  "O3'" "HO3'" sing N N 100 
DA  "C2'" "C1'"  sing N N 101 
DA  "C2'" "H2'"  sing N N 102 
DA  "C2'" "H2''" sing N N 103 
DA  "C1'" N9     sing N N 104 
DA  "C1'" "H1'"  sing N N 105 
DA  N9    C8     sing Y N 106 
DA  N9    C4     sing Y N 107 
DA  C8    N7     doub Y N 108 
DA  C8    H8     sing N N 109 
DA  N7    C5     sing Y N 110 
DA  C5    C6     sing Y N 111 
DA  C5    C4     doub Y N 112 
DA  C6    N6     sing N N 113 
DA  C6    N1     doub Y N 114 
DA  N6    H61    sing N N 115 
DA  N6    H62    sing N N 116 
DA  N1    C2     sing Y N 117 
DA  C2    N3     doub Y N 118 
DA  C2    H2     sing N N 119 
DA  N3    C4     sing Y N 120 
DC  OP3   P      sing N N 121 
DC  OP3   HOP3   sing N N 122 
DC  P     OP1    doub N N 123 
DC  P     OP2    sing N N 124 
DC  P     "O5'"  sing N N 125 
DC  OP2   HOP2   sing N N 126 
DC  "O5'" "C5'"  sing N N 127 
DC  "C5'" "C4'"  sing N N 128 
DC  "C5'" "H5'"  sing N N 129 
DC  "C5'" "H5''" sing N N 130 
DC  "C4'" "O4'"  sing N N 131 
DC  "C4'" "C3'"  sing N N 132 
DC  "C4'" "H4'"  sing N N 133 
DC  "O4'" "C1'"  sing N N 134 
DC  "C3'" "O3'"  sing N N 135 
DC  "C3'" "C2'"  sing N N 136 
DC  "C3'" "H3'"  sing N N 137 
DC  "O3'" "HO3'" sing N N 138 
DC  "C2'" "C1'"  sing N N 139 
DC  "C2'" "H2'"  sing N N 140 
DC  "C2'" "H2''" sing N N 141 
DC  "C1'" N1     sing N N 142 
DC  "C1'" "H1'"  sing N N 143 
DC  N1    C2     sing N N 144 
DC  N1    C6     sing N N 145 
DC  C2    O2     doub N N 146 
DC  C2    N3     sing N N 147 
DC  N3    C4     doub N N 148 
DC  C4    N4     sing N N 149 
DC  C4    C5     sing N N 150 
DC  N4    H41    sing N N 151 
DC  N4    H42    sing N N 152 
DC  C5    C6     doub N N 153 
DC  C5    H5     sing N N 154 
DC  C6    H6     sing N N 155 
DG  OP3   P      sing N N 156 
DG  OP3   HOP3   sing N N 157 
DG  P     OP1    doub N N 158 
DG  P     OP2    sing N N 159 
DG  P     "O5'"  sing N N 160 
DG  OP2   HOP2   sing N N 161 
DG  "O5'" "C5'"  sing N N 162 
DG  "C5'" "C4'"  sing N N 163 
DG  "C5'" "H5'"  sing N N 164 
DG  "C5'" "H5''" sing N N 165 
DG  "C4'" "O4'"  sing N N 166 
DG  "C4'" "C3'"  sing N N 167 
DG  "C4'" "H4'"  sing N N 168 
DG  "O4'" "C1'"  sing N N 169 
DG  "C3'" "O3'"  sing N N 170 
DG  "C3'" "C2'"  sing N N 171 
DG  "C3'" "H3'"  sing N N 172 
DG  "O3'" "HO3'" sing N N 173 
DG  "C2'" "C1'"  sing N N 174 
DG  "C2'" "H2'"  sing N N 175 
DG  "C2'" "H2''" sing N N 176 
DG  "C1'" N9     sing N N 177 
DG  "C1'" "H1'"  sing N N 178 
DG  N9    C8     sing Y N 179 
DG  N9    C4     sing Y N 180 
DG  C8    N7     doub Y N 181 
DG  C8    H8     sing N N 182 
DG  N7    C5     sing Y N 183 
DG  C5    C6     sing N N 184 
DG  C5    C4     doub Y N 185 
DG  C6    O6     doub N N 186 
DG  C6    N1     sing N N 187 
DG  N1    C2     sing N N 188 
DG  N1    H1     sing N N 189 
DG  C2    N2     sing N N 190 
DG  C2    N3     doub N N 191 
DG  N2    H21    sing N N 192 
DG  N2    H22    sing N N 193 
DG  N3    C4     sing N N 194 
DT  OP3   P      sing N N 195 
DT  OP3   HOP3   sing N N 196 
DT  P     OP1    doub N N 197 
DT  P     OP2    sing N N 198 
DT  P     "O5'"  sing N N 199 
DT  OP2   HOP2   sing N N 200 
DT  "O5'" "C5'"  sing N N 201 
DT  "C5'" "C4'"  sing N N 202 
DT  "C5'" "H5'"  sing N N 203 
DT  "C5'" "H5''" sing N N 204 
DT  "C4'" "O4'"  sing N N 205 
DT  "C4'" "C3'"  sing N N 206 
DT  "C4'" "H4'"  sing N N 207 
DT  "O4'" "C1'"  sing N N 208 
DT  "C3'" "O3'"  sing N N 209 
DT  "C3'" "C2'"  sing N N 210 
DT  "C3'" "H3'"  sing N N 211 
DT  "O3'" "HO3'" sing N N 212 
DT  "C2'" "C1'"  sing N N 213 
DT  "C2'" "H2'"  sing N N 214 
DT  "C2'" "H2''" sing N N 215 
DT  "C1'" N1     sing N N 216 
DT  "C1'" "H1'"  sing N N 217 
DT  N1    C2     sing N N 218 
DT  N1    C6     sing N N 219 
DT  C2    O2     doub N N 220 
DT  C2    N3     sing N N 221 
DT  N3    C4     sing N N 222 
DT  N3    H3     sing N N 223 
DT  C4    O4     doub N N 224 
DT  C4    C5     sing N N 225 
DT  C5    C7     sing N N 226 
DT  C5    C6     doub N N 227 
DT  C7    H71    sing N N 228 
DT  C7    H72    sing N N 229 
DT  C7    H73    sing N N 230 
DT  C6    H6     sing N N 231 
GLN N     CA     sing N N 232 
GLN N     H      sing N N 233 
GLN N     H2     sing N N 234 
GLN CA    C      sing N N 235 
GLN CA    CB     sing N N 236 
GLN CA    HA     sing N N 237 
GLN C     O      doub N N 238 
GLN C     OXT    sing N N 239 
GLN CB    CG     sing N N 240 
GLN CB    HB2    sing N N 241 
GLN CB    HB3    sing N N 242 
GLN CG    CD     sing N N 243 
GLN CG    HG2    sing N N 244 
GLN CG    HG3    sing N N 245 
GLN CD    OE1    doub N N 246 
GLN CD    NE2    sing N N 247 
GLN NE2   HE21   sing N N 248 
GLN NE2   HE22   sing N N 249 
GLN OXT   HXT    sing N N 250 
GLU N     CA     sing N N 251 
GLU N     H      sing N N 252 
GLU N     H2     sing N N 253 
GLU CA    C      sing N N 254 
GLU CA    CB     sing N N 255 
GLU CA    HA     sing N N 256 
GLU C     O      doub N N 257 
GLU C     OXT    sing N N 258 
GLU CB    CG     sing N N 259 
GLU CB    HB2    sing N N 260 
GLU CB    HB3    sing N N 261 
GLU CG    CD     sing N N 262 
GLU CG    HG2    sing N N 263 
GLU CG    HG3    sing N N 264 
GLU CD    OE1    doub N N 265 
GLU CD    OE2    sing N N 266 
GLU OE2   HE2    sing N N 267 
GLU OXT   HXT    sing N N 268 
GLY N     CA     sing N N 269 
GLY N     H      sing N N 270 
GLY N     H2     sing N N 271 
GLY CA    C      sing N N 272 
GLY CA    HA2    sing N N 273 
GLY CA    HA3    sing N N 274 
GLY C     O      doub N N 275 
GLY C     OXT    sing N N 276 
GLY OXT   HXT    sing N N 277 
HIS N     CA     sing N N 278 
HIS N     H      sing N N 279 
HIS N     H2     sing N N 280 
HIS CA    C      sing N N 281 
HIS CA    CB     sing N N 282 
HIS CA    HA     sing N N 283 
HIS C     O      doub N N 284 
HIS C     OXT    sing N N 285 
HIS CB    CG     sing N N 286 
HIS CB    HB2    sing N N 287 
HIS CB    HB3    sing N N 288 
HIS CG    ND1    sing Y N 289 
HIS CG    CD2    doub Y N 290 
HIS ND1   CE1    doub Y N 291 
HIS ND1   HD1    sing N N 292 
HIS CD2   NE2    sing Y N 293 
HIS CD2   HD2    sing N N 294 
HIS CE1   NE2    sing Y N 295 
HIS CE1   HE1    sing N N 296 
HIS NE2   HE2    sing N N 297 
HIS OXT   HXT    sing N N 298 
HOH O     H1     sing N N 299 
HOH O     H2     sing N N 300 
ILE N     CA     sing N N 301 
ILE N     H      sing N N 302 
ILE N     H2     sing N N 303 
ILE CA    C      sing N N 304 
ILE CA    CB     sing N N 305 
ILE CA    HA     sing N N 306 
ILE C     O      doub N N 307 
ILE C     OXT    sing N N 308 
ILE CB    CG1    sing N N 309 
ILE CB    CG2    sing N N 310 
ILE CB    HB     sing N N 311 
ILE CG1   CD1    sing N N 312 
ILE CG1   HG12   sing N N 313 
ILE CG1   HG13   sing N N 314 
ILE CG2   HG21   sing N N 315 
ILE CG2   HG22   sing N N 316 
ILE CG2   HG23   sing N N 317 
ILE CD1   HD11   sing N N 318 
ILE CD1   HD12   sing N N 319 
ILE CD1   HD13   sing N N 320 
ILE OXT   HXT    sing N N 321 
LEU N     CA     sing N N 322 
LEU N     H      sing N N 323 
LEU N     H2     sing N N 324 
LEU CA    C      sing N N 325 
LEU CA    CB     sing N N 326 
LEU CA    HA     sing N N 327 
LEU C     O      doub N N 328 
LEU C     OXT    sing N N 329 
LEU CB    CG     sing N N 330 
LEU CB    HB2    sing N N 331 
LEU CB    HB3    sing N N 332 
LEU CG    CD1    sing N N 333 
LEU CG    CD2    sing N N 334 
LEU CG    HG     sing N N 335 
LEU CD1   HD11   sing N N 336 
LEU CD1   HD12   sing N N 337 
LEU CD1   HD13   sing N N 338 
LEU CD2   HD21   sing N N 339 
LEU CD2   HD22   sing N N 340 
LEU CD2   HD23   sing N N 341 
LEU OXT   HXT    sing N N 342 
LYS N     CA     sing N N 343 
LYS N     H      sing N N 344 
LYS N     H2     sing N N 345 
LYS CA    C      sing N N 346 
LYS CA    CB     sing N N 347 
LYS CA    HA     sing N N 348 
LYS C     O      doub N N 349 
LYS C     OXT    sing N N 350 
LYS CB    CG     sing N N 351 
LYS CB    HB2    sing N N 352 
LYS CB    HB3    sing N N 353 
LYS CG    CD     sing N N 354 
LYS CG    HG2    sing N N 355 
LYS CG    HG3    sing N N 356 
LYS CD    CE     sing N N 357 
LYS CD    HD2    sing N N 358 
LYS CD    HD3    sing N N 359 
LYS CE    NZ     sing N N 360 
LYS CE    HE2    sing N N 361 
LYS CE    HE3    sing N N 362 
LYS NZ    HZ1    sing N N 363 
LYS NZ    HZ2    sing N N 364 
LYS NZ    HZ3    sing N N 365 
LYS OXT   HXT    sing N N 366 
MES O1    C2     sing N N 367 
MES O1    C6     sing N N 368 
MES C2    C3     sing N N 369 
MES C2    H21    sing N N 370 
MES C2    H22    sing N N 371 
MES C3    N4     sing N N 372 
MES C3    H31    sing N N 373 
MES C3    H32    sing N N 374 
MES N4    C5     sing N N 375 
MES N4    C7     sing N N 376 
MES N4    HN4    sing N N 377 
MES C5    C6     sing N N 378 
MES C5    H51    sing N N 379 
MES C5    H52    sing N N 380 
MES C6    H61    sing N N 381 
MES C6    H62    sing N N 382 
MES C7    C8     sing N N 383 
MES C7    H71    sing N N 384 
MES C7    H72    sing N N 385 
MES C8    S      sing N N 386 
MES C8    H81    sing N N 387 
MES C8    H82    sing N N 388 
MES S     O1S    doub N N 389 
MES S     O2S    doub N N 390 
MES S     O3S    sing N N 391 
MET N     CA     sing N N 392 
MET N     H      sing N N 393 
MET N     H2     sing N N 394 
MET CA    C      sing N N 395 
MET CA    CB     sing N N 396 
MET CA    HA     sing N N 397 
MET C     O      doub N N 398 
MET C     OXT    sing N N 399 
MET CB    CG     sing N N 400 
MET CB    HB2    sing N N 401 
MET CB    HB3    sing N N 402 
MET CG    SD     sing N N 403 
MET CG    HG2    sing N N 404 
MET CG    HG3    sing N N 405 
MET SD    CE     sing N N 406 
MET CE    HE1    sing N N 407 
MET CE    HE2    sing N N 408 
MET CE    HE3    sing N N 409 
MET OXT   HXT    sing N N 410 
PHE N     CA     sing N N 411 
PHE N     H      sing N N 412 
PHE N     H2     sing N N 413 
PHE CA    C      sing N N 414 
PHE CA    CB     sing N N 415 
PHE CA    HA     sing N N 416 
PHE C     O      doub N N 417 
PHE C     OXT    sing N N 418 
PHE CB    CG     sing N N 419 
PHE CB    HB2    sing N N 420 
PHE CB    HB3    sing N N 421 
PHE CG    CD1    doub Y N 422 
PHE CG    CD2    sing Y N 423 
PHE CD1   CE1    sing Y N 424 
PHE CD1   HD1    sing N N 425 
PHE CD2   CE2    doub Y N 426 
PHE CD2   HD2    sing N N 427 
PHE CE1   CZ     doub Y N 428 
PHE CE1   HE1    sing N N 429 
PHE CE2   CZ     sing Y N 430 
PHE CE2   HE2    sing N N 431 
PHE CZ    HZ     sing N N 432 
PHE OXT   HXT    sing N N 433 
PRO N     CA     sing N N 434 
PRO N     CD     sing N N 435 
PRO N     H      sing N N 436 
PRO CA    C      sing N N 437 
PRO CA    CB     sing N N 438 
PRO CA    HA     sing N N 439 
PRO C     O      doub N N 440 
PRO C     OXT    sing N N 441 
PRO CB    CG     sing N N 442 
PRO CB    HB2    sing N N 443 
PRO CB    HB3    sing N N 444 
PRO CG    CD     sing N N 445 
PRO CG    HG2    sing N N 446 
PRO CG    HG3    sing N N 447 
PRO CD    HD2    sing N N 448 
PRO CD    HD3    sing N N 449 
PRO OXT   HXT    sing N N 450 
SER N     CA     sing N N 451 
SER N     H      sing N N 452 
SER N     H2     sing N N 453 
SER CA    C      sing N N 454 
SER CA    CB     sing N N 455 
SER CA    HA     sing N N 456 
SER C     O      doub N N 457 
SER C     OXT    sing N N 458 
SER CB    OG     sing N N 459 
SER CB    HB2    sing N N 460 
SER CB    HB3    sing N N 461 
SER OG    HG     sing N N 462 
SER OXT   HXT    sing N N 463 
THR N     CA     sing N N 464 
THR N     H      sing N N 465 
THR N     H2     sing N N 466 
THR CA    C      sing N N 467 
THR CA    CB     sing N N 468 
THR CA    HA     sing N N 469 
THR C     O      doub N N 470 
THR C     OXT    sing N N 471 
THR CB    OG1    sing N N 472 
THR CB    CG2    sing N N 473 
THR CB    HB     sing N N 474 
THR OG1   HG1    sing N N 475 
THR CG2   HG21   sing N N 476 
THR CG2   HG22   sing N N 477 
THR CG2   HG23   sing N N 478 
THR OXT   HXT    sing N N 479 
TRP N     CA     sing N N 480 
TRP N     H      sing N N 481 
TRP N     H2     sing N N 482 
TRP CA    C      sing N N 483 
TRP CA    CB     sing N N 484 
TRP CA    HA     sing N N 485 
TRP C     O      doub N N 486 
TRP C     OXT    sing N N 487 
TRP CB    CG     sing N N 488 
TRP CB    HB2    sing N N 489 
TRP CB    HB3    sing N N 490 
TRP CG    CD1    doub Y N 491 
TRP CG    CD2    sing Y N 492 
TRP CD1   NE1    sing Y N 493 
TRP CD1   HD1    sing N N 494 
TRP CD2   CE2    doub Y N 495 
TRP CD2   CE3    sing Y N 496 
TRP NE1   CE2    sing Y N 497 
TRP NE1   HE1    sing N N 498 
TRP CE2   CZ2    sing Y N 499 
TRP CE3   CZ3    doub Y N 500 
TRP CE3   HE3    sing N N 501 
TRP CZ2   CH2    doub Y N 502 
TRP CZ2   HZ2    sing N N 503 
TRP CZ3   CH2    sing Y N 504 
TRP CZ3   HZ3    sing N N 505 
TRP CH2   HH2    sing N N 506 
TRP OXT   HXT    sing N N 507 
TYR N     CA     sing N N 508 
TYR N     H      sing N N 509 
TYR N     H2     sing N N 510 
TYR CA    C      sing N N 511 
TYR CA    CB     sing N N 512 
TYR CA    HA     sing N N 513 
TYR C     O      doub N N 514 
TYR C     OXT    sing N N 515 
TYR CB    CG     sing N N 516 
TYR CB    HB2    sing N N 517 
TYR CB    HB3    sing N N 518 
TYR CG    CD1    doub Y N 519 
TYR CG    CD2    sing Y N 520 
TYR CD1   CE1    sing Y N 521 
TYR CD1   HD1    sing N N 522 
TYR CD2   CE2    doub Y N 523 
TYR CD2   HD2    sing N N 524 
TYR CE1   CZ     doub Y N 525 
TYR CE1   HE1    sing N N 526 
TYR CE2   CZ     sing Y N 527 
TYR CE2   HE2    sing N N 528 
TYR CZ    OH     sing N N 529 
TYR OH    HH     sing N N 530 
TYR OXT   HXT    sing N N 531 
VAL N     CA     sing N N 532 
VAL N     H      sing N N 533 
VAL N     H2     sing N N 534 
VAL CA    C      sing N N 535 
VAL CA    CB     sing N N 536 
VAL CA    HA     sing N N 537 
VAL C     O      doub N N 538 
VAL C     OXT    sing N N 539 
VAL CB    CG1    sing N N 540 
VAL CB    CG2    sing N N 541 
VAL CB    HB     sing N N 542 
VAL CG1   HG11   sing N N 543 
VAL CG1   HG12   sing N N 544 
VAL CG1   HG13   sing N N 545 
VAL CG2   HG21   sing N N 546 
VAL CG2   HG22   sing N N 547 
VAL CG2   HG23   sing N N 548 
VAL OXT   HXT    sing N N 549 
# 
loop_
_ndb_struct_conf_na.entry_id 
_ndb_struct_conf_na.feature 
9F38 'double helix'        
9F38 'a-form double helix' 
9F38 'b-form double helix' 
# 
loop_
_ndb_struct_na_base_pair.model_number 
_ndb_struct_na_base_pair.i_label_asym_id 
_ndb_struct_na_base_pair.i_label_comp_id 
_ndb_struct_na_base_pair.i_label_seq_id 
_ndb_struct_na_base_pair.i_symmetry 
_ndb_struct_na_base_pair.j_label_asym_id 
_ndb_struct_na_base_pair.j_label_comp_id 
_ndb_struct_na_base_pair.j_label_seq_id 
_ndb_struct_na_base_pair.j_symmetry 
_ndb_struct_na_base_pair.shear 
_ndb_struct_na_base_pair.stretch 
_ndb_struct_na_base_pair.stagger 
_ndb_struct_na_base_pair.buckle 
_ndb_struct_na_base_pair.propeller 
_ndb_struct_na_base_pair.opening 
_ndb_struct_na_base_pair.pair_number 
_ndb_struct_na_base_pair.pair_name 
_ndb_struct_na_base_pair.i_auth_asym_id 
_ndb_struct_na_base_pair.i_auth_seq_id 
_ndb_struct_na_base_pair.i_PDB_ins_code 
_ndb_struct_na_base_pair.j_auth_asym_id 
_ndb_struct_na_base_pair.j_auth_seq_id 
_ndb_struct_na_base_pair.j_PDB_ins_code 
_ndb_struct_na_base_pair.hbond_type_28 
_ndb_struct_na_base_pair.hbond_type_12 
1 B DG 1  1_555 C DC 13 1_555 -0.038 -0.214 0.642  -7.549  -28.536 -7.112 1  E_DG1:DC13_F E 1  ? F 13 ? 19 1 
1 B DT 2  1_555 C DA 12 1_555 0.322  -0.047 -0.146 -6.703  -13.032 -5.346 2  E_DT2:DA12_F E 2  ? F 12 ? 20 1 
1 B DC 3  1_555 C DG 11 1_555 -0.991 -0.255 0.411  -20.463 -16.598 -0.397 3  E_DC3:DG11_F E 3  ? F 11 ? 19 1 
1 B DT 4  1_555 C DA 10 1_555 0.735  -0.183 0.250  -16.261 11.814  2.124  4  E_DT4:DA10_F E 4  ? F 10 ? 20 1 
1 B DG 5  1_555 C DC 9  1_555 -0.983 -0.359 0.395  -10.274 -15.120 0.469  5  E_DG5:DC9_F  E 5  ? F 9  ? 19 1 
1 B DC 6  1_555 C DG 8  1_555 -0.221 -0.105 0.287  -15.659 -8.631  -2.324 6  E_DC6:DG8_F  E 6  ? F 8  ? 19 1 
1 B DA 7  1_555 C DT 7  1_555 0.214  -0.218 0.084  0.959   -3.575  1.225  7  E_DA7:DT7_F  E 7  ? F 7  ? 20 1 
1 B DT 8  1_555 C DA 6  1_555 -0.368 0.180  0.027  16.156  -16.405 -2.503 8  E_DT8:DA6_F  E 8  ? F 6  ? 20 1 
1 B DT 9  1_555 C DA 5  1_555 -0.651 -0.282 0.053  5.698   -19.377 3.291  9  E_DT9:DA5_F  E 9  ? F 5  ? 20 1 
1 B DC 10 1_555 C DG 4  1_555 0.272  -0.140 -0.157 -5.145  -7.595  -2.426 10 E_DC10:DG4_F E 10 ? F 4  ? 19 1 
1 B DC 11 1_555 C DG 3  1_555 -0.954 -0.185 0.388  -7.328  3.766   0.642  11 E_DC11:DG3_F E 11 ? F 3  ? 19 1 
1 B DT 12 1_555 C DA 2  1_555 -0.774 0.061  0.566  5.652   -19.877 6.612  12 E_DT12:DA2_F E 12 ? F 2  ? 20 1 
1 B DC 13 1_555 C DG 1  1_555 -1.068 0.195  0.244  -8.759  -17.364 -2.401 13 E_DC13:DG1_F E 13 ? F 1  ? 19 1 
1 D DG 1  1_555 E DC 13 1_555 0.806  -0.072 0.240  8.956   -16.900 -2.519 14 U_DG1:DC13_V U 1  ? V 13 ? 19 1 
1 D DA 2  1_555 E DT 12 1_555 0.413  0.013  0.537  -5.392  -19.817 6.743  15 U_DA2:DT12_V U 2  ? V 12 ? 20 1 
1 D DG 3  1_555 E DC 11 1_555 0.633  -0.046 0.395  7.786   4.517   0.902  16 U_DG3:DC11_V U 3  ? V 11 ? 19 1 
1 D DG 4  1_555 E DC 10 1_555 -0.449 0.083  -0.098 6.220   -6.339  -1.785 17 U_DG4:DC10_V U 4  ? V 10 ? 19 1 
1 D DA 5  1_555 E DT 9  1_555 0.718  -0.144 0.118  -3.368  -19.343 3.760  18 U_DA5:DT9_V  U 5  ? V 9  ? 20 1 
1 D DA 6  1_555 E DT 8  1_555 0.456  0.134  0.006  -15.105 -18.079 -1.979 19 U_DA6:DT8_V  U 6  ? V 8  ? 20 1 
1 D DT 7  1_555 E DA 7  1_555 -0.264 -0.278 0.012  -1.012  -5.141  1.813  20 U_DT7:DA7_V  U 7  ? V 7  ? 20 1 
1 D DG 8  1_555 E DC 6  1_555 0.123  -0.155 0.156  15.447  -9.061  -2.202 21 U_DG8:DC6_V  U 8  ? V 6  ? 19 1 
1 D DC 9  1_555 E DG 5  1_555 0.919  -0.325 0.255  10.042  -15.005 0.358  22 U_DC9:DG5_V  U 9  ? V 5  ? 19 1 
1 D DA 10 1_555 E DT 4  1_555 -0.743 -0.131 0.123  15.682  11.953  1.951  23 U_DA10:DT4_V U 10 ? V 4  ? 20 1 
1 D DG 11 1_555 E DC 3  1_555 1.108  -0.211 0.336  19.608  -15.932 -0.269 24 U_DG11:DC3_V U 11 ? V 3  ? 19 1 
1 D DA 12 1_555 E DT 2  1_555 -0.136 -0.029 -0.222 6.029   -11.692 -5.406 25 U_DA12:DT2_V U 12 ? V 2  ? 20 1 
1 D DC 13 1_555 E DG 1  1_555 0.285  -0.323 0.510  7.800   -26.872 -7.157 26 U_DC13:DG1_V U 13 ? V 1  ? 19 1 
# 
loop_
_ndb_struct_na_base_pair_step.model_number 
_ndb_struct_na_base_pair_step.i_label_asym_id_1 
_ndb_struct_na_base_pair_step.i_label_comp_id_1 
_ndb_struct_na_base_pair_step.i_label_seq_id_1 
_ndb_struct_na_base_pair_step.i_symmetry_1 
_ndb_struct_na_base_pair_step.j_label_asym_id_1 
_ndb_struct_na_base_pair_step.j_label_comp_id_1 
_ndb_struct_na_base_pair_step.j_label_seq_id_1 
_ndb_struct_na_base_pair_step.j_symmetry_1 
_ndb_struct_na_base_pair_step.i_label_asym_id_2 
_ndb_struct_na_base_pair_step.i_label_comp_id_2 
_ndb_struct_na_base_pair_step.i_label_seq_id_2 
_ndb_struct_na_base_pair_step.i_symmetry_2 
_ndb_struct_na_base_pair_step.j_label_asym_id_2 
_ndb_struct_na_base_pair_step.j_label_comp_id_2 
_ndb_struct_na_base_pair_step.j_label_seq_id_2 
_ndb_struct_na_base_pair_step.j_symmetry_2 
_ndb_struct_na_base_pair_step.shift 
_ndb_struct_na_base_pair_step.slide 
_ndb_struct_na_base_pair_step.rise 
_ndb_struct_na_base_pair_step.tilt 
_ndb_struct_na_base_pair_step.roll 
_ndb_struct_na_base_pair_step.twist 
_ndb_struct_na_base_pair_step.x_displacement 
_ndb_struct_na_base_pair_step.y_displacement 
_ndb_struct_na_base_pair_step.helical_rise 
_ndb_struct_na_base_pair_step.inclination 
_ndb_struct_na_base_pair_step.tip 
_ndb_struct_na_base_pair_step.helical_twist 
_ndb_struct_na_base_pair_step.step_number 
_ndb_struct_na_base_pair_step.step_name 
_ndb_struct_na_base_pair_step.i_auth_asym_id_1 
_ndb_struct_na_base_pair_step.i_auth_seq_id_1 
_ndb_struct_na_base_pair_step.i_PDB_ins_code_1 
_ndb_struct_na_base_pair_step.j_auth_asym_id_1 
_ndb_struct_na_base_pair_step.j_auth_seq_id_1 
_ndb_struct_na_base_pair_step.j_PDB_ins_code_1 
_ndb_struct_na_base_pair_step.i_auth_asym_id_2 
_ndb_struct_na_base_pair_step.i_auth_seq_id_2 
_ndb_struct_na_base_pair_step.i_PDB_ins_code_2 
_ndb_struct_na_base_pair_step.j_auth_asym_id_2 
_ndb_struct_na_base_pair_step.j_auth_seq_id_2 
_ndb_struct_na_base_pair_step.j_PDB_ins_code_2 
1 B DG 1  1_555 C DC 13 1_555 B DT 2  1_555 C DA 12 1_555 -0.319 -0.089 3.420 3.262  -10.052 35.589 1.270  0.959  3.284 -16.015 
-5.198  37.076 1  EE_DG1DT2:DA12DC13_FF E 1  ? F 13 ? E 2  ? F 12 ? 
1 B DT 2  1_555 C DA 12 1_555 B DC 3  1_555 C DG 11 1_555 -0.047 -0.049 3.652 -4.158 -1.247  31.426 0.166  -0.770 3.627 -2.289  
7.630   31.717 2  EE_DT2DC3:DG11DA12_FF E 2  ? F 12 ? E 3  ? F 11 ? 
1 B DC 3  1_555 C DG 11 1_555 B DT 4  1_555 C DA 10 1_555 1.135  1.577  3.531 -1.068 13.129  38.933 0.597  -1.754 3.816 19.047  
1.549   41.019 3  EE_DC3DT4:DA10DG11_FF E 3  ? F 11 ? E 4  ? F 10 ? 
1 B DT 4  1_555 C DA 10 1_555 B DG 5  1_555 C DC 9  1_555 -0.241 0.038  3.311 -2.980 -5.113  31.812 0.986  -0.103 3.274 -9.228  
5.379   32.344 4  EE_DT4DG5:DC9DA10_FF  E 4  ? F 10 ? E 5  ? F 9  ? 
1 B DG 5  1_555 C DC 9  1_555 B DC 6  1_555 C DG 8  1_555 0.445  -1.291 3.531 4.430  2.695   38.915 -2.267 -0.096 3.466 4.024   
-6.613  39.246 5  EE_DG5DC6:DG8DC9_FF   E 5  ? F 9  ? E 6  ? F 8  ? 
1 B DC 6  1_555 C DG 8  1_555 B DA 7  1_555 C DT 7  1_555 0.726  -1.650 3.187 0.249  7.079   23.404 -5.888 -1.645 2.590 16.960  
-0.595  24.438 6  EE_DC6DA7:DT7DG8_FF   E 6  ? F 8  ? E 7  ? F 7  ? 
1 B DA 7  1_555 C DT 7  1_555 B DT 8  1_555 C DA 6  1_555 -0.362 -0.696 3.459 6.690  -11.479 29.500 0.966  1.943  3.335 -21.238 
-12.378 32.294 7  EE_DA7DT8:DA6DT7_FF   E 7  ? F 7  ? E 8  ? F 6  ? 
1 B DT 8  1_555 C DA 6  1_555 B DT 9  1_555 C DA 5  1_555 0.156  -0.791 3.605 1.781  -6.293  32.771 -0.203 0.061  3.692 -11.017 
-3.119  33.399 8  EE_DT8DT9:DA5DA6_FF   E 8  ? F 6  ? E 9  ? F 5  ? 
1 B DT 9  1_555 C DA 5  1_555 B DC 10 1_555 C DG 4  1_555 -0.012 -0.191 3.776 -1.949 -10.303 49.922 0.613  -0.144 3.742 -12.054 
2.281   50.942 9  EE_DT9DC10:DG4DA5_FF  E 9  ? F 5  ? E 10 ? F 4  ? 
1 B DC 10 1_555 C DG 4  1_555 B DC 11 1_555 C DG 3  1_555 0.529  -0.283 3.462 -2.264 -1.123  30.161 -0.303 -1.495 3.422 -2.153  
4.341   30.265 10 EE_DC10DC11:DG3DG4_FF E 10 ? F 4  ? E 11 ? F 3  ? 
1 B DC 11 1_555 C DG 3  1_555 B DT 12 1_555 C DA 2  1_555 -0.523 0.092  3.176 1.867  -6.367  33.293 1.143  1.184  3.073 -10.977 
-3.218  33.929 11 EE_DC11DT12:DA2DG3_FF E 11 ? F 3  ? E 12 ? F 2  ? 
1 B DT 12 1_555 C DA 2  1_555 B DC 13 1_555 C DG 1  1_555 -0.177 0.131  3.603 1.444  2.236   42.772 -0.065 0.401  3.597 3.062   
-1.978  42.850 12 EE_DT12DC13:DG1DA2_FF E 12 ? F 2  ? E 13 ? F 1  ? 
1 D DG 1  1_555 E DC 13 1_555 D DA 2  1_555 E DT 12 1_555 0.185  0.141  3.610 -1.288 2.170   42.838 -0.045 -0.394 3.606 2.968   
1.762   42.909 13 UU_DG1DA2:DT12DC13_VV U 1  ? V 13 ? U 2  ? V 12 ? 
1 D DA 2  1_555 E DT 12 1_555 D DG 3  1_555 E DC 11 1_555 0.539  0.089  3.176 -1.831 -6.897  33.448 1.202  -1.195 3.065 -11.817 
3.136   34.180 14 UU_DA2DG3:DC11DT12_VV U 2  ? V 12 ? U 3  ? V 11 ? 
1 D DG 3  1_555 E DC 11 1_555 D DG 4  1_555 E DC 10 1_555 -0.515 -0.282 3.465 1.716  -1.439  30.143 -0.233 1.356  3.440 -2.761  
-3.293  30.224 15 UU_DG3DG4:DC10DC11_VV U 3  ? V 11 ? U 4  ? V 10 ? 
1 D DG 4  1_555 E DC 10 1_555 D DA 5  1_555 E DT 9  1_555 0.024  -0.183 3.763 1.867  -10.401 49.834 0.629  0.124  3.727 -12.186 
-2.187  50.872 16 UU_DG4DA5:DT9DC10_VV  U 4  ? V 10 ? U 5  ? V 9  ? 
1 D DA 5  1_555 E DT 9  1_555 D DA 6  1_555 E DT 8  1_555 -0.149 -0.770 3.644 -1.465 -6.421  33.177 -0.144 -0.014 3.726 -11.108 
2.534   33.806 17 UU_DA5DA6:DT8DT9_VV   U 5  ? V 9  ? U 6  ? V 8  ? 
1 D DA 6  1_555 E DT 8  1_555 D DT 7  1_555 E DA 7  1_555 0.383  -0.698 3.464 -6.458 -11.841 29.677 1.012  -1.915 3.341 -21.758 
11.867  32.535 18 UU_DA6DT7:DA7DT8_VV   U 6  ? V 8  ? U 7  ? V 7  ? 
1 D DT 7  1_555 E DA 7  1_555 D DG 8  1_555 E DC 6  1_555 -0.761 -1.649 3.174 -0.277 7.542   23.457 -5.936 1.708  2.536 17.965  
0.659   24.625 19 UU_DT7DG8:DC6DA7_VV   U 7  ? V 7  ? U 8  ? V 6  ? 
1 D DG 8  1_555 E DC 6  1_555 D DC 9  1_555 E DG 5  1_555 -0.451 -1.290 3.528 -4.343 2.959   39.068 -2.288 0.119  3.453 4.400   
6.458   39.406 20 UU_DG8DC9:DG5DC6_VV   U 8  ? V 6  ? U 9  ? V 5  ? 
1 D DC 9  1_555 E DG 5  1_555 D DA 10 1_555 E DT 4  1_555 0.241  0.029  3.314 3.051  -4.933  32.081 0.925  0.110  3.282 -8.837  
-5.464  32.588 21 UU_DC9DA10:DT4DG5_VV  U 9  ? V 5  ? U 10 ? V 4  ? 
1 D DA 10 1_555 E DT 4  1_555 D DG 11 1_555 E DC 3  1_555 -1.128 1.574  3.538 0.576  13.012  39.313 0.614  1.670  3.833 18.727  
-0.829  41.333 22 UU_DA10DG11:DC3DT4_VV U 10 ? V 4  ? U 11 ? V 3  ? 
1 D DG 11 1_555 E DC 3  1_555 D DA 12 1_555 E DT 2  1_555 0.038  -0.053 3.665 4.010  -1.074  31.283 0.126  0.765  3.641 -1.981  
-7.396  31.550 23 UU_DG11DA12:DT2DC3_VV U 11 ? V 3  ? U 12 ? V 2  ? 
1 D DA 12 1_555 E DT 2  1_555 D DC 13 1_555 E DG 1  1_555 0.324  -0.094 3.421 -3.225 -9.837  35.524 1.242  -0.966 3.290 -15.716 
5.152   36.954 24 UU_DA12DC13:DG1DT2_VV U 12 ? V 2  ? U 13 ? V 1  ? 
# 
_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      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'Model obtained by experimental phasing' 
# 
_atom_sites.entry_id                    9F38 
_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]   0.015213 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001465 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007699 
_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]   0.009973 
_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 
CL 
H  
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   ? 4.69    -32.259 -0.677  1 27.82 ? 1   MET A N     1 
ATOM   2     C  CA    . MET A 1 1   ? 5.382   -30.996 -0.439  1 28.21 ? 1   MET A CA    1 
ATOM   3     C  C     . MET A 1 1   ? 4.398   -29.829 -0.372  1 28.62 ? 1   MET A C     1 
ATOM   4     O  O     . MET A 1 1   ? 3.379   -29.833 -1.058  1 28.88 ? 1   MET A O     1 
ATOM   5     C  CB    . MET A 1 1   ? 6.436   -30.734 -1.544  1 28.47 ? 1   MET A CB    1 
ATOM   6     C  CG    . MET A 1 1   ? 7.205   -29.432 -1.361  1 30.02 ? 1   MET A CG    1 
ATOM   7     S  SD    . MET A 1 1   ? 8.547   -29.149 -2.535  1 31.42 ? 1   MET A SD    1 
ATOM   8     C  CE    . MET A 1 1   ? 7.63    -29.061 -4.045  1 31.16 ? 1   MET A CE    1 
ATOM   9     N  N     . ASN A 1 2   ? 4.707   -28.827 0.449   1 28.4  ? 2   ASN A N     1 
ATOM   10    C  CA    . ASN A 1 2   ? 3.916   -27.613 0.536   1 28.52 ? 2   ASN A CA    1 
ATOM   11    C  C     . ASN A 1 2   ? 4.809   -26.445 0.142   1 28.94 ? 2   ASN A C     1 
ATOM   12    O  O     . ASN A 1 2   ? 5.962   -26.38  0.567   1 29    ? 2   ASN A O     1 
ATOM   13    C  CB    . ASN A 1 2   ? 3.344   -27.428 1.932   1 28.91 ? 2   ASN A CB    1 
ATOM   14    C  CG    . ASN A 1 2   ? 2.05    -28.166 2.122   1 30.91 ? 2   ASN A CG    1 
ATOM   15    O  OD1   . ASN A 1 2   ? 1.292   -28.386 1.175   1 31.48 ? 2   ASN A OD1   1 
ATOM   16    N  ND2   . ASN A 1 2   ? 1.764   -28.559 3.352   1 31.57 ? 2   ASN A ND2   1 
ATOM   17    N  N     . VAL A 1 3   ? 4.303   -25.549 -0.709  1 29.12 ? 3   VAL A N     1 
ATOM   18    C  CA    . VAL A 1 3   ? 5.08    -24.402 -1.161  1 29.74 ? 3   VAL A CA    1 
ATOM   19    C  C     . VAL A 1 3   ? 4.49    -23.105 -0.633  1 30.09 ? 3   VAL A C     1 
ATOM   20    O  O     . VAL A 1 3   ? 3.288   -22.88  -0.726  1 30.33 ? 3   VAL A O     1 
ATOM   21    C  CB    . VAL A 1 3   ? 5.235   -24.37  -2.701  1 30.59 ? 3   VAL A CB    1 
ATOM   22    C  CG1   . VAL A 1 3   ? 6.024   -23.146 -3.15   1 31.15 ? 3   VAL A CG1   1 
ATOM   23    C  CG2   . VAL A 1 3   ? 5.896   -25.643 -3.21   1 31.2  ? 3   VAL A CG2   1 
ATOM   24    N  N     . PHE A 1 4   ? 5.338   -22.261 -0.07   1 29.95 ? 4   PHE A N     1 
ATOM   25    C  CA    . PHE A 1 4   ? 4.947   -20.962 0.451   1 30.33 ? 4   PHE A CA    1 
ATOM   26    C  C     . PHE A 1 4   ? 5.765   -19.892 -0.238  1 29.97 ? 4   PHE A C     1 
ATOM   27    O  O     . PHE A 1 4   ? 6.89    -20.157 -0.659  1 29.88 ? 4   PHE A O     1 
ATOM   28    C  CB    . PHE A 1 4   ? 5.216   -20.886 1.96    1 30.69 ? 4   PHE A CB    1 
ATOM   29    C  CG    . PHE A 1 4   ? 4.548   -21.986 2.743   1 31.78 ? 4   PHE A CG    1 
ATOM   30    C  CD1   . PHE A 1 4   ? 3.211   -21.903 3.076   1 32.85 ? 4   PHE A CD1   1 
ATOM   31    C  CD2   . PHE A 1 4   ? 5.255   -23.11  3.134   1 32.72 ? 4   PHE A CD2   1 
ATOM   32    C  CE1   . PHE A 1 4   ? 2.594   -22.92  3.798   1 33.68 ? 4   PHE A CE1   1 
ATOM   33    C  CE2   . PHE A 1 4   ? 4.636   -24.127 3.852   1 33.52 ? 4   PHE A CE2   1 
ATOM   34    C  CZ    . PHE A 1 4   ? 3.31    -24.025 4.18    1 33.42 ? 4   PHE A CZ    1 
ATOM   35    N  N     . ARG A 1 5   ? 5.225   -18.677 -0.33   1 29.61 ? 5   ARG A N     1 
ATOM   36    C  CA    . ARG A 1 5   ? 5.966   -17.575 -0.924  1 29.64 ? 5   ARG A CA    1 
ATOM   37    C  C     . ARG A 1 5   ? 6.159   -16.469 0.079   1 29.73 ? 5   ARG A C     1 
ATOM   38    O  O     . ARG A 1 5   ? 5.245   -16.145 0.83    1 29.84 ? 5   ARG A O     1 
ATOM   39    C  CB    . ARG A 1 5   ? 5.312   -17.067 -2.206  1 30.8  ? 5   ARG A CB    1 
ATOM   40    C  CG    . ARG A 1 5   ? 5.559   -17.983 -3.383  1 34.11 ? 5   ARG A CG    1 
ATOM   41    C  CD    . ARG A 1 5   ? 4.703   -17.608 -4.571  1 37.36 ? 5   ARG A CD    1 
ATOM   42    N  NE    . ARG A 1 5   ? 5.061   -18.376 -5.766  1 39.71 ? 5   ARG A NE    1 
ATOM   43    C  CZ    . ARG A 1 5   ? 4.718   -18.039 -7.004  1 41.78 ? 5   ARG A CZ    1 
ATOM   44    N  NH1   . ARG A 1 5   ? 4.013   -16.938 -7.23   1 41.84 ? 5   ARG A NH1   1 
ATOM   45    N  NH2   . ARG A 1 5   ? 5.093   -18.79  -8.028  1 41.73 ? 5   ARG A NH2   1 
ATOM   46    N  N     . ILE A 1 6   ? 7.364   -15.917 0.125   1 29.61 ? 6   ILE A N     1 
ATOM   47    C  CA    . ILE A 1 6   ? 7.666   -14.812 1.017   1 29.93 ? 6   ILE A CA    1 
ATOM   48    C  C     . ILE A 1 6   ? 7.911   -13.601 0.151   1 29.91 ? 6   ILE A C     1 
ATOM   49    O  O     . ILE A 1 6   ? 8.954   -13.505 -0.487  1 29.78 ? 6   ILE A O     1 
ATOM   50    C  CB    . ILE A 1 6   ? 8.887   -15.096 1.92    1 30.51 ? 6   ILE A CB    1 
ATOM   51    C  CG1   . ILE A 1 6   ? 8.747   -16.422 2.671   1 31.3  ? 6   ILE A CG1   1 
ATOM   52    C  CG2   . ILE A 1 6   ? 9.136   -13.929 2.877   1 31.05 ? 6   ILE A CG2   1 
ATOM   53    C  CD1   . ILE A 1 6   ? 7.59    -16.496 3.564   1 32.7  ? 6   ILE A CD1   1 
ATOM   54    N  N     . HIS A 1 7   ? 6.94    -12.703 0.091   1 29.89 ? 7   HIS A N     1 
ATOM   55    C  CA    . HIS A 1 7   ? 7.071   -11.487 -0.688  1 30.47 ? 7   HIS A CA    1 
ATOM   56    C  C     . HIS A 1 7   ? 7.585   -10.428 0.284   1 30.73 ? 7   HIS A C     1 
ATOM   57    O  O     . HIS A 1 7   ? 6.961   -10.216 1.315   1 30.77 ? 7   HIS A O     1 
ATOM   58    C  CB    . HIS A 1 7   ? 5.699   -11.092 -1.259  1 31.36 ? 7   HIS A CB    1 
ATOM   59    C  CG    . HIS A 1 7   ? 5.088   -12.129 -2.157  1 33.33 ? 7   HIS A CG    1 
ATOM   60    N  ND1   . HIS A 1 7   ? 5.212   -12.054 -3.534  1 35.02 ? 7   HIS A ND1   1 
ATOM   61    C  CD2   . HIS A 1 7   ? 4.348   -13.22  -1.846  1 34.29 ? 7   HIS A CD2   1 
ATOM   62    C  CE1   . HIS A 1 7   ? 4.561   -13.103 -4.012  1 35.44 ? 7   HIS A CE1   1 
ATOM   63    N  NE2   . HIS A 1 7   ? 4.022   -13.832 -3.034  1 35.32 ? 7   HIS A NE2   1 
ATOM   64    N  N     . GLY A 1 8   ? 8.735   -9.825  -0.002  1 30.7  ? 8   GLY A N     1 
ATOM   65    C  CA    . GLY A 1 8   ? 9.305   -8.819  0.889   1 31.29 ? 8   GLY A CA    1 
ATOM   66    C  C     . GLY A 1 8   ? 9.799   -7.573  0.188   1 31.6  ? 8   GLY A C     1 
ATOM   67    O  O     . GLY A 1 8   ? 9.772   -7.519  -1.037  1 31.95 ? 8   GLY A O     1 
ATOM   68    N  N     . ASP A 1 9   ? 10.23   -6.544  0.946   1 31.33 ? 9   ASP A N     1 
ATOM   69    C  CA    . ASP A 1 9   ? 10.776  -5.314  0.346   1 31.51 ? 9   ASP A CA    1 
ATOM   70    C  C     . ASP A 1 9   ? 12.094  -5.626  -0.374  1 31.09 ? 9   ASP A C     1 
ATOM   71    O  O     . ASP A 1 9   ? 12.351  -5.097  -1.451  1 30.97 ? 9   ASP A O     1 
ATOM   72    C  CB    . ASP A 1 9   ? 11.083  -4.253  1.418   1 33.4  ? 9   ASP A CB    1 
ATOM   73    C  CG    . ASP A 1 9   ? 9.905   -3.746  2.207   1 37.99 ? 9   ASP A CG    1 
ATOM   74    O  OD1   . ASP A 1 9   ? 8.858   -3.44   1.589   1 38.73 ? 9   ASP A OD1   1 
ATOM   75    O  OD2   . ASP A 1 9   ? 10.035  -3.626  3.437   1 40.11 ? 9   ASP A OD2   1 
ATOM   76    N  N     . ASN A 1 10  ? 12.925  -6.48   0.232   1 30.8  ? 10  ASN A N     1 
ATOM   77    C  CA    . ASN A 1 10  ? 14.215  -6.916  -0.297  1 31.2  ? 10  ASN A CA    1 
ATOM   78    C  C     . ASN A 1 10  ? 14.596  -8.313  0.248   1 31.56 ? 10  ASN A C     1 
ATOM   79    O  O     . ASN A 1 10  ? 13.839  -8.886  1.035   1 31.73 ? 10  ASN A O     1 
ATOM   80    C  CB    . ASN A 1 10  ? 15.304  -5.866  -0.03   1 32.24 ? 10  ASN A CB    1 
ATOM   81    C  CG    . ASN A 1 10  ? 15.308  -5.302  1.359   1 35.17 ? 10  ASN A CG    1 
ATOM   82    O  OD1   . ASN A 1 10  ? 14.831  -4.189  1.605   1 35.9  ? 10  ASN A OD1   1 
ATOM   83    N  ND2   . ASN A 1 10  ? 15.848  -6.045  2.295   1 36.05 ? 10  ASN A ND2   1 
ATOM   84    N  N     . ILE A 1 11  ? 15.744  -8.874  -0.172  1 31.57 ? 11  ILE A N     1 
ATOM   85    C  CA    . ILE A 1 11  ? 16.161  -10.199 0.28    1 32.3  ? 11  ILE A CA    1 
ATOM   86    C  C     . ILE A 1 11  ? 16.33   -10.298 1.801   1 33.01 ? 11  ILE A C     1 
ATOM   87    O  O     . ILE A 1 11  ? 16.014  -11.336 2.383   1 33.58 ? 11  ILE A O     1 
ATOM   88    C  CB    . ILE A 1 11  ? 17.427  -10.698 -0.47   1 32.98 ? 11  ILE A CB    1 
ATOM   89    C  CG1   . ILE A 1 11  ? 17.662  -12.199 -0.242  1 34.09 ? 11  ILE A CG1   1 
ATOM   90    C  CG2   . ILE A 1 11  ? 18.67   -9.879  -0.126  1 33.49 ? 11  ILE A CG2   1 
ATOM   91    C  CD1   . ILE A 1 11  ? 16.469  -13.081 -0.575  1 35.55 ? 11  ILE A CD1   1 
ATOM   92    N  N     . ILE A 1 12  ? 16.792  -9.223  2.448   1 32.66 ? 12  ILE A N     1 
ATOM   93    C  CA    . ILE A 1 12  ? 17.006  -9.217  3.884   1 32.73 ? 12  ILE A CA    1 
ATOM   94    C  C     . ILE A 1 12  ? 15.685  -9.403  4.63    1 32.95 ? 12  ILE A C     1 
ATOM   95    O  O     . ILE A 1 12  ? 15.632  -10.208 5.556   1 33.08 ? 12  ILE A O     1 
ATOM   96    C  CB    . ILE A 1 12  ? 17.816  -7.955  4.286   1 33.08 ? 12  ILE A CB    1 
ATOM   97    C  CG1   . ILE A 1 12  ? 19.314  -8.272  4.302   1 33.97 ? 12  ILE A CG1   1 
ATOM   98    C  CG2   . ILE A 1 12  ? 17.346  -7.269  5.577   1 33.63 ? 12  ILE A CG2   1 
ATOM   99    C  CD1   . ILE A 1 12  ? 19.764  -9.183  5.409   1 35.33 ? 12  ILE A CD1   1 
ATOM   100   N  N     . GLU A 1 13  ? 14.61   -8.728  4.19    1 32.8  ? 13  GLU A N     1 
ATOM   101   C  CA    . GLU A 1 13  ? 13.313  -8.856  4.857   1 33.07 ? 13  GLU A CA    1 
ATOM   102   C  C     . GLU A 1 13  ? 12.785  -10.275 4.717   1 33.37 ? 13  GLU A C     1 
ATOM   103   O  O     . GLU A 1 13  ? 12.284  -10.835 5.684   1 33.41 ? 13  GLU A O     1 
ATOM   104   C  CB    . GLU A 1 13  ? 12.284  -7.847  4.306   1 34.75 ? 13  GLU A CB    1 
ATOM   105   C  CG    . GLU A 1 13  ? 12.802  -6.433  4.091   1 38.37 ? 13  GLU A CG    1 
ATOM   106   C  CD    . GLU A 1 13  ? 12.952  -5.542  5.306   1 41.96 ? 13  GLU A CD    1 
ATOM   107   O  OE1   . GLU A 1 13  ? 12.124  -5.656  6.237   1 42.41 ? 13  GLU A OE1   1 
ATOM   108   O  OE2   . GLU A 1 13  ? 13.889  -4.711  5.317   1 42.84 ? 13  GLU A OE2   1 
ATOM   109   N  N     . CYS A 1 14  ? 12.926  -10.867 3.524   1 33.41 ? 14  CYS A N     1 
ATOM   110   C  CA    . CYS A 1 14  ? 12.484  -12.236 3.261   1 33.95 ? 14  CYS A CA    1 
ATOM   111   C  C     . CYS A 1 14  ? 13.227  -13.217 4.158   1 34.28 ? 14  CYS A C     1 
ATOM   112   O  O     . CYS A 1 14  ? 12.61   -14.07  4.792   1 34.38 ? 14  CYS A O     1 
ATOM   113   C  CB    . CYS A 1 14  ? 12.668  -12.59  1.787   1 34.54 ? 14  CYS A CB    1 
ATOM   114   S  SG    . CYS A 1 14  ? 11.817  -11.475 0.641   1 37.46 ? 14  CYS A SG    1 
ATOM   115   N  N     . GLU A 1 15  ? 14.552  -13.064 4.24    1 34.38 ? 15  GLU A N     1 
ATOM   116   C  CA    . GLU A 1 15  ? 15.393  -13.935 5.041   1 34.92 ? 15  GLU A CA    1 
ATOM   117   C  C     . GLU A 1 15  ? 15.11   -13.846 6.525   1 34.79 ? 15  GLU A C     1 
ATOM   118   O  O     . GLU A 1 15  ? 15.278  -14.843 7.221   1 35.11 ? 15  GLU A O     1 
ATOM   119   C  CB    . GLU A 1 15  ? 16.879  -13.705 4.743   1 37.78 ? 15  GLU A CB    1 
ATOM   120   C  CG    . GLU A 1 15  ? 17.303  -14.235 3.388   1 43.25 ? 15  GLU A CG    1 
ATOM   121   C  CD    . GLU A 1 15  ? 17.26   -15.745 3.253   1 50.58 ? 15  GLU A CD    1 
ATOM   122   O  OE1   . GLU A 1 15  ? 17.209  -16.446 4.291   1 50.52 ? 15  GLU A OE1   1 
ATOM   123   O  OE2   . GLU A 1 15  ? 17.305  -16.227 2.096   1 54.32 ? 15  GLU A OE2   1 
ATOM   124   N  N     . ARG A 1 16  ? 14.641  -12.69  7.014   1 34.25 ? 16  ARG A N     1 
ATOM   125   C  CA    . ARG A 1 16  ? 14.308  -12.548 8.431   1 33.95 ? 16  ARG A CA    1 
ATOM   126   C  C     . ARG A 1 16  ? 13.173  -13.487 8.835   1 33.35 ? 16  ARG A C     1 
ATOM   127   O  O     . ARG A 1 16  ? 13.206  -14.035 9.929   1 33.3  ? 16  ARG A O     1 
ATOM   128   C  CB    . ARG A 1 16  ? 14.012  -11.091 8.796   1 35.19 ? 16  ARG A CB    1 
ATOM   129   C  CG    . ARG A 1 16  ? 15.268  -10.234 8.788   1 38.47 ? 16  ARG A CG    1 
ATOM   130   C  CD    . ARG A 1 16  ? 15.271  -9.19   9.884   1 42.13 ? 16  ARG A CD    1 
ATOM   131   N  NE    . ARG A 1 16  ? 14.479  -8.011  9.541   1 44.82 ? 16  ARG A NE    1 
ATOM   132   C  CZ    . ARG A 1 16  ? 14.994  -6.83   9.21    1 46.62 ? 16  ARG A CZ    1 
ATOM   133   N  NH1   . ARG A 1 16  ? 16.31   -6.652  9.197   1 45.99 ? 16  ARG A NH1   1 
ATOM   134   N  NH2   . ARG A 1 16  ? 14.198  -5.815  8.901   1 46.43 ? 16  ARG A NH2   1 
ATOM   135   N  N     . VAL A 1 17  ? 12.218  -13.734 7.935   1 32.91 ? 17  VAL A N     1 
ATOM   136   C  CA    . VAL A 1 17  ? 11.131  -14.669 8.203   1 33.07 ? 17  VAL A CA    1 
ATOM   137   C  C     . VAL A 1 17  ? 11.666  -16.103 8.268   1 33.09 ? 17  VAL A C     1 
ATOM   138   O  O     . VAL A 1 17  ? 11.293  -16.871 9.152   1 33.02 ? 17  VAL A O     1 
ATOM   139   C  CB    . VAL A 1 17  ? 10.001  -14.487 7.174   1 33.84 ? 17  VAL A CB    1 
ATOM   140   C  CG1   . VAL A 1 17  ? 9.028   -15.665 7.187   1 34.52 ? 17  VAL A CG1   1 
ATOM   141   C  CG2   . VAL A 1 17  ? 9.267   -13.182 7.439   1 34.22 ? 17  VAL A CG2   1 
ATOM   142   N  N     . ILE A 1 18  ? 12.586  -16.442 7.369   1 33.03 ? 18  ILE A N     1 
ATOM   143   C  CA    . ILE A 1 18  ? 13.215  -17.757 7.355   1 33.46 ? 18  ILE A CA    1 
ATOM   144   C  C     . ILE A 1 18  ? 13.989  -17.988 8.654   1 33.74 ? 18  ILE A C     1 
ATOM   145   O  O     . ILE A 1 18  ? 13.869  -19.052 9.243   1 33.34 ? 18  ILE A O     1 
ATOM   146   C  CB    . ILE A 1 18  ? 14.116  -17.913 6.1     1 33.83 ? 18  ILE A CB    1 
ATOM   147   C  CG1   . ILE A 1 18  ? 13.31   -17.694 4.812   1 34.74 ? 18  ILE A CG1   1 
ATOM   148   C  CG2   . ILE A 1 18  ? 14.83   -19.263 6.075   1 34.21 ? 18  ILE A CG2   1 
ATOM   149   C  CD1   . ILE A 1 18  ? 12.151  -18.65  4.632   1 35.88 ? 18  ILE A CD1   1 
ATOM   150   N  N     . ASP A 1 19  ? 14.719  -16.97  9.131   1 34.29 ? 19  ASP A N     1 
ATOM   151   C  CA    . ASP A 1 19  ? 15.494  -17.069 10.368  1 35.49 ? 19  ASP A CA    1 
ATOM   152   C  C     . ASP A 1 19  ? 14.61   -17.32  11.604  1 36.07 ? 19  ASP A C     1 
ATOM   153   O  O     . ASP A 1 19  ? 15.021  -18.046 12.509  1 36.22 ? 19  ASP A O     1 
ATOM   154   C  CB    . ASP A 1 19  ? 16.406  -15.843 10.551  1 37.84 ? 19  ASP A CB    1 
ATOM   155   C  CG    . ASP A 1 19  ? 17.462  -15.682 9.461   1 43.53 ? 19  ASP A CG    1 
ATOM   156   O  OD1   . ASP A 1 19  ? 17.702  -16.661 8.709   1 44.34 ? 19  ASP A OD1   1 
ATOM   157   O  OD2   . ASP A 1 19  ? 18.039  -14.572 9.348   1 46.07 ? 19  ASP A OD2   1 
ATOM   158   N  N     . LEU A 1 20  ? 13.388  -16.756 11.624  1 36.1  ? 20  LEU A N     1 
ATOM   159   C  CA    . LEU A 1 20  ? 12.423  -16.993 12.696  1 36.47 ? 20  LEU A CA    1 
ATOM   160   C  C     . LEU A 1 20  ? 11.992  -18.47  12.664  1 37.33 ? 20  LEU A C     1 
ATOM   161   O  O     . LEU A 1 20  ? 11.991  -19.125 13.701  1 37.69 ? 20  LEU A O     1 
ATOM   162   C  CB    . LEU A 1 20  ? 11.189  -16.105 12.504  1 36.53 ? 20  LEU A CB    1 
ATOM   163   C  CG    . LEU A 1 20  ? 11.344  -14.67  12.922  1 38.39 ? 20  LEU A CG    1 
ATOM   164   C  CD1   . LEU A 1 20  ? 10.157  -13.842 12.464  1 38.87 ? 20  LEU A CD1   1 
ATOM   165   C  CD2   . LEU A 1 20  ? 11.534  -14.569 14.422  1 39.41 ? 20  LEU A CD2   1 
ATOM   166   N  N     . ILE A 1 21  ? 11.651  -18.996 11.47   1 37.47 ? 21  ILE A N     1 
ATOM   167   C  CA    . ILE A 1 21  ? 11.232  -20.384 11.282  1 37.78 ? 21  ILE A CA    1 
ATOM   168   C  C     . ILE A 1 21  ? 12.354  -21.334 11.704  1 37.94 ? 21  ILE A C     1 
ATOM   169   O  O     . ILE A 1 21  ? 12.137  -22.209 12.537  1 37.99 ? 21  ILE A O     1 
ATOM   170   C  CB    . ILE A 1 21  ? 10.783  -20.61  9.808   1 38.28 ? 21  ILE A CB    1 
ATOM   171   C  CG1   . ILE A 1 21  ? 9.467   -19.874 9.515   1 39.34 ? 21  ILE A CG1   1 
ATOM   172   C  CG2   . ILE A 1 21  ? 10.67   -22.092 9.467   1 38.62 ? 21  ILE A CG2   1 
ATOM   173   C  CD1   . ILE A 1 21  ? 9.152   -19.753 8.072   1 40.58 ? 21  ILE A CD1   1 
ATOM   174   N  N     . LEU A 1 22  ? 13.562  -21.107 11.181  1 37.93 ? 22  LEU A N     1 
ATOM   175   C  CA    . LEU A 1 22  ? 14.763  -21.893 11.444  1 38.6  ? 22  LEU A CA    1 
ATOM   176   C  C     . LEU A 1 22  ? 15.185  -21.882 12.911  1 39.15 ? 22  LEU A C     1 
ATOM   177   O  O     . LEU A 1 22  ? 15.889  -22.791 13.339  1 39.38 ? 22  LEU A O     1 
ATOM   178   C  CB    . LEU A 1 22  ? 15.913  -21.369 10.574  1 39    ? 22  LEU A CB    1 
ATOM   179   C  CG    . LEU A 1 22  ? 16.201  -22.067 9.246   1 40.74 ? 22  LEU A CG    1 
ATOM   180   C  CD1   . LEU A 1 22  ? 16.928  -23.363 9.469   1 41.46 ? 22  LEU A CD1   1 
ATOM   181   C  CD2   . LEU A 1 22  ? 14.953  -22.266 8.397   1 41.44 ? 22  LEU A CD2   1 
ATOM   182   N  N     . SER A 1 23  ? 14.777  -20.866 13.681  1 39.31 ? 23  SER A N     1 
ATOM   183   C  CA    . SER A 1 23  ? 15.107  -20.793 15.106  1 39.98 ? 23  SER A CA    1 
ATOM   184   C  C     . SER A 1 23  ? 14.361  -21.853 15.929  1 40.15 ? 23  SER A C     1 
ATOM   185   O  O     . SER A 1 23  ? 14.825  -22.226 17.001  1 40.39 ? 23  SER A O     1 
ATOM   186   C  CB    . SER A 1 23  ? 14.811  -19.401 15.665  1 41.63 ? 23  SER A CB    1 
ATOM   187   O  OG    . SER A 1 23  ? 13.427  -19.182 15.893  1 44.07 ? 23  SER A OG    1 
ATOM   188   N  N     . LYS A 1 24  ? 13.198  -22.31  15.453  1 39.95 ? 24  LYS A N     1 
ATOM   189   C  CA    . LYS A 1 24  ? 12.416  -23.314 16.16   1 40.34 ? 24  LYS A CA    1 
ATOM   190   C  C     . LYS A 1 24  ? 12.461  -24.67  15.417  1 40.87 ? 24  LYS A C     1 
ATOM   191   O  O     . LYS A 1 24  ? 12.489  -25.728 16.048  1 41.12 ? 24  LYS A O     1 
ATOM   192   C  CB    . LYS A 1 24  ? 10.977  -22.814 16.378  1 41.58 ? 24  LYS A CB    1 
ATOM   193   C  CG    . LYS A 1 24  ? 10.529  -22.859 17.834  1 44.91 ? 24  LYS A CG    1 
ATOM   194   C  CD    . LYS A 1 24  ? 10.313  -24.299 18.299  1 49.08 ? 24  LYS A CD    1 
ATOM   195   C  CE    . LYS A 1 24  ? 9.689   -24.406 19.667  1 52.27 ? 24  LYS A CE    1 
ATOM   196   N  NZ    . LYS A 1 24  ? 9.136   -25.764 19.913  1 53.84 ? 24  LYS A NZ    1 
ATOM   197   N  N     . ILE A 1 25  ? 12.495  -24.634 14.084  1 40.77 ? 25  ILE A N     1 
ATOM   198   C  CA    . ILE A 1 25  ? 12.584  -25.842 13.279  1 41.29 ? 25  ILE A CA    1 
ATOM   199   C  C     . ILE A 1 25  ? 14.045  -26.235 13.206  1 41.79 ? 25  ILE A C     1 
ATOM   200   O  O     . ILE A 1 25  ? 14.88   -25.402 12.86   1 42.13 ? 25  ILE A O     1 
ATOM   201   C  CB    . ILE A 1 25  ? 12.064  -25.555 11.845  1 41.89 ? 25  ILE A CB    1 
ATOM   202   C  CG1   . ILE A 1 25  ? 10.575  -25.19  11.828  1 42.75 ? 25  ILE A CG1   1 
ATOM   203   C  CG2   . ILE A 1 25  ? 12.381  -26.695 10.873  1 42.5  ? 25  ILE A CG2   1 
ATOM   204   C  CD1   . ILE A 1 25  ? 9.645   -26.289 12.216  1 44.01 ? 25  ILE A CD1   1 
ATOM   205   N  N     . ASN A 1 26  ? 14.362  -27.493 13.499  1 41.71 ? 26  ASN A N     1 
ATOM   206   C  CA    . ASN A 1 26  ? 15.729  -27.985 13.36   1 42    ? 26  ASN A CA    1 
ATOM   207   C  C     . ASN A 1 26  ? 15.66   -28.911 12.155  1 41.48 ? 26  ASN A C     1 
ATOM   208   O  O     . ASN A 1 26  ? 15.226  -30.05  12.294  1 41.77 ? 26  ASN A O     1 
ATOM   209   C  CB    . ASN A 1 26  ? 16.16   -28.743 14.621  1 43.52 ? 26  ASN A CB    1 
ATOM   210   C  CG    . ASN A 1 26  ? 17.647  -28.7   14.868  1 46.93 ? 26  ASN A CG    1 
ATOM   211   O  OD1   . ASN A 1 26  ? 18.457  -28.677 13.928  1 48.25 ? 26  ASN A OD1   1 
ATOM   212   N  ND2   . ASN A 1 26  ? 18.034  -28.678 16.139  1 47.35 ? 26  ASN A ND2   1 
ATOM   213   N  N     . PRO A 1 27  ? 15.956  -28.411 10.945  1 40.57 ? 27  PRO A N     1 
ATOM   214   C  CA    . PRO A 1 27  ? 15.785  -29.247 9.751   1 40.19 ? 27  PRO A CA    1 
ATOM   215   C  C     . PRO A 1 27  ? 16.829  -30.328 9.548   1 39.86 ? 27  PRO A C     1 
ATOM   216   O  O     . PRO A 1 27  ? 18.001  -30.15  9.867   1 40.08 ? 27  PRO A O     1 
ATOM   217   C  CB    . PRO A 1 27  ? 15.787  -28.245 8.596   1 40.93 ? 27  PRO A CB    1 
ATOM   218   C  CG    . PRO A 1 27  ? 15.861  -26.886 9.225   1 41.4  ? 27  PRO A CG    1 
ATOM   219   C  CD    . PRO A 1 27  ? 16.423  -27.065 10.59   1 39.92 ? 27  PRO A CD    1 
ATOM   220   N  N     . GLN A 1 28  ? 16.386  -31.453 8.997   1 39.07 ? 28  GLN A N     1 
ATOM   221   C  CA    . GLN A 1 28  ? 17.233  -32.593 8.716   1 38.66 ? 28  GLN A CA    1 
ATOM   222   C  C     . GLN A 1 28  ? 18.03   -32.302 7.452   1 37.99 ? 28  GLN A C     1 
ATOM   223   O  O     . GLN A 1 28  ? 19.241  -32.509 7.43    1 38.39 ? 28  GLN A O     1 
ATOM   224   C  CB    . GLN A 1 28  ? 16.369  -33.853 8.535   1 40.4  ? 28  GLN A CB    1 
ATOM   225   C  CG    . GLN A 1 28  ? 15.36   -34.072 9.651   1 44.27 ? 28  GLN A CG    1 
ATOM   226   C  CD    . GLN A 1 28  ? 16.061  -34.356 10.954  1 49.15 ? 28  GLN A CD    1 
ATOM   227   O  OE1   . GLN A 1 28  ? 16.7    -35.401 11.131  1 50.74 ? 28  GLN A OE1   1 
ATOM   228   N  NE2   . GLN A 1 28  ? 15.955  -33.432 11.9    1 49.57 ? 28  GLN A NE2   1 
ATOM   229   N  N     . LYS A 1 29  ? 17.353  -31.811 6.397   1 36.84 ? 29  LYS A N     1 
ATOM   230   C  CA    . LYS A 1 29  ? 17.98   -31.508 5.11    1 35.96 ? 29  LYS A CA    1 
ATOM   231   C  C     . LYS A 1 29  ? 17.587  -30.111 4.652   1 35.35 ? 29  LYS A C     1 
ATOM   232   O  O     . LYS A 1 29  ? 16.408  -29.771 4.671   1 35.51 ? 29  LYS A O     1 
ATOM   233   C  CB    . LYS A 1 29  ? 17.543  -32.538 4.052   1 36.64 ? 29  LYS A CB    1 
ATOM   234   C  CG    . LYS A 1 29  ? 18.045  -33.949 4.325   1 38.95 ? 29  LYS A CG    1 
ATOM   235   C  CD    . LYS A 1 29  ? 17.197  -35.025 3.646   1 41.62 ? 29  LYS A CD    1 
ATOM   236   C  CE    . LYS A 1 29  ? 17.547  -35.257 2.198   1 43.81 ? 29  LYS A CE    1 
ATOM   237   N  NZ    . LYS A 1 29  ? 16.687  -36.299 1.579   1 45.17 ? 29  LYS A NZ    1 
ATOM   238   N  N     . VAL A 1 30  ? 18.567  -29.293 4.262   1 34.55 ? 30  VAL A N     1 
ATOM   239   C  CA    . VAL A 1 30  ? 18.291  -27.943 3.781   1 34.42 ? 30  VAL A CA    1 
ATOM   240   C  C     . VAL A 1 30  ? 18.945  -27.75  2.419   1 34.18 ? 30  VAL A C     1 
ATOM   241   O  O     . VAL A 1 30  ? 20.122  -28.05  2.252   1 34.21 ? 30  VAL A O     1 
ATOM   242   C  CB    . VAL A 1 30  ? 18.728  -26.837 4.781   1 35    ? 30  VAL A CB    1 
ATOM   243   C  CG1   . VAL A 1 30  ? 18.581  -25.452 4.171   1 35.52 ? 30  VAL A CG1   1 
ATOM   244   C  CG2   . VAL A 1 30  ? 17.937  -26.922 6.074   1 35.4  ? 30  VAL A CG2   1 
ATOM   245   N  N     . LYS A 1 31  ? 18.183  -27.274 1.445   1 33.74 ? 31  LYS A N     1 
ATOM   246   C  CA    . LYS A 1 31  ? 18.702  -26.987 0.121   1 33.81 ? 31  LYS A CA    1 
ATOM   247   C  C     . LYS A 1 31  ? 18.326  -25.551 -0.22   1 33.92 ? 31  LYS A C     1 
ATOM   248   O  O     . LYS A 1 31  ? 17.22   -25.116 0.083   1 33.94 ? 31  LYS A O     1 
ATOM   249   C  CB    . LYS A 1 31  ? 18.12   -27.952 -0.924  1 35.22 ? 31  LYS A CB    1 
ATOM   250   C  CG    . LYS A 1 31  ? 18.59   -27.67  -2.347  1 38.65 ? 31  LYS A CG    1 
ATOM   251   C  CD    . LYS A 1 31  ? 17.933  -28.576 -3.38   1 42.76 ? 31  LYS A CD    1 
ATOM   252   C  CE    . LYS A 1 31  ? 18.773  -29.791 -3.698  1 46.23 ? 31  LYS A CE    1 
ATOM   253   N  NZ    . LYS A 1 31  ? 18.16   -30.624 -4.768  1 48.31 ? 31  LYS A NZ    1 
ATOM   254   N  N     . ARG A 1 32  ? 19.247  -24.804 -0.814  1 33.68 ? 32  ARG A N     1 
ATOM   255   C  CA    . ARG A 1 32  ? 18.977  -23.439 -1.232  1 33.87 ? 32  ARG A CA    1 
ATOM   256   C  C     . ARG A 1 32  ? 19.318  -23.281 -2.72   1 33.85 ? 32  ARG A C     1 
ATOM   257   O  O     . ARG A 1 32  ? 20.062  -24.085 -3.291  1 33.83 ? 32  ARG A O     1 
ATOM   258   C  CB    . ARG A 1 32  ? 19.771  -22.444 -0.378  1 35.23 ? 32  ARG A CB    1 
ATOM   259   C  CG    . ARG A 1 32  ? 19.187  -22.126 0.986   1 37.83 ? 32  ARG A CG    1 
ATOM   260   C  CD    . ARG A 1 32  ? 20.094  -21.142 1.675   1 40.29 ? 32  ARG A CD    1 
ATOM   261   N  NE    . ARG A 1 32  ? 19.6    -20.727 2.991   1 43.1  ? 32  ARG A NE    1 
ATOM   262   C  CZ    . ARG A 1 32  ? 18.772  -19.706 3.195   1 45.41 ? 32  ARG A CZ    1 
ATOM   263   N  NH1   . ARG A 1 32  ? 18.3    -19.009 2.168   1 45.78 ? 32  ARG A NH1   1 
ATOM   264   N  NH2   . ARG A 1 32  ? 18.397  -19.384 4.426   1 44.89 ? 32  ARG A NH2   1 
ATOM   265   N  N     . GLY A 1 33  ? 18.767  -22.249 -3.34   1 33.61 ? 33  GLY A N     1 
ATOM   266   C  CA    . GLY A 1 33  ? 19.017  -21.98  -4.748  1 33.72 ? 33  GLY A CA    1 
ATOM   267   C  C     . GLY A 1 33  ? 18.107  -20.905 -5.284  1 33.55 ? 33  GLY A C     1 
ATOM   268   O  O     . GLY A 1 33  ? 17.679  -20.034 -4.531  1 33.69 ? 33  GLY A O     1 
ATOM   269   N  N     . PHE A 1 34  ? 17.791  -20.966 -6.576  1 33.1  ? 34  PHE A N     1 
ATOM   270   C  CA    . PHE A 1 34  ? 16.908  -19.998 -7.209  1 33.14 ? 34  PHE A CA    1 
ATOM   271   C  C     . PHE A 1 34  ? 15.852  -20.725 -8.041  1 33.14 ? 34  PHE A C     1 
ATOM   272   O  O     . PHE A 1 34  ? 16.184  -21.675 -8.745  1 33.12 ? 34  PHE A O     1 
ATOM   273   C  CB    . PHE A 1 34  ? 17.717  -19.091 -8.153  1 33.02 ? 34  PHE A CB    1 
ATOM   274   C  CG    . PHE A 1 34  ? 18.472  -17.936 -7.536  1 33.7  ? 34  PHE A CG    1 
ATOM   275   C  CD1   . PHE A 1 34  ? 17.833  -16.742 -7.249  1 34.43 ? 34  PHE A CD1   1 
ATOM   276   C  CD2   . PHE A 1 34  ? 19.835  -18.01  -7.335  1 34.48 ? 34  PHE A CD2   1 
ATOM   277   C  CE1   . PHE A 1 34  ? 18.534  -15.669 -6.718  1 35    ? 34  PHE A CE1   1 
ATOM   278   C  CE2   . PHE A 1 34  ? 20.532  -16.932 -6.804  1 35.11 ? 34  PHE A CE2   1 
ATOM   279   C  CZ    . PHE A 1 34  ? 19.878  -15.773 -6.492  1 34.77 ? 34  PHE A CZ    1 
ATOM   280   N  N     . ILE A 1 35  ? 14.59   -20.282 -7.979  1 33.07 ? 35  ILE A N     1 
ATOM   281   C  CA    . ILE A 1 35  ? 13.538  -20.828 -8.853  1 33.52 ? 35  ILE A CA    1 
ATOM   282   C  C     . ILE A 1 35  ? 13.475  -20.029 -10.199 1 34.13 ? 35  ILE A C     1 
ATOM   283   O  O     . ILE A 1 35  ? 12.981  -20.521 -11.214 1 34.61 ? 35  ILE A O     1 
ATOM   284   C  CB    . ILE A 1 35  ? 12.15   -20.919 -8.172  1 33.87 ? 35  ILE A CB    1 
ATOM   285   C  CG1   . ILE A 1 35  ? 11.607  -19.537 -7.806  1 34.5  ? 35  ILE A CG1   1 
ATOM   286   C  CG2   . ILE A 1 35  ? 12.159  -21.871 -6.977  1 34.38 ? 35  ILE A CG2   1 
ATOM   287   C  CD1   . ILE A 1 35  ? 10.123  -19.494 -7.773  1 35.58 ? 35  ILE A CD1   1 
ATOM   288   N  N     . SER A 1 36  ? 13.971  -18.795 -10.179 1 33.95 ? 36  SER A N     1 
ATOM   289   C  CA    . SER A 1 36  ? 14.097  -17.87  -11.289 1 34.34 ? 36  SER A CA    1 
ATOM   290   C  C     . SER A 1 36  ? 15.275  -16.938 -10.953 1 34.27 ? 36  SER A C     1 
ATOM   291   O  O     . SER A 1 36  ? 15.773  -16.972 -9.828  1 34.51 ? 36  SER A O     1 
ATOM   292   C  CB    . SER A 1 36  ? 12.814  -17.065 -11.45  1 36    ? 36  SER A CB    1 
ATOM   293   O  OG    . SER A 1 36  ? 12.675  -16.078 -10.439 1 38.41 ? 36  SER A OG    1 
ATOM   294   N  N     . LEU A 1 37  ? 15.695  -16.087 -11.891 1 33.84 ? 37  LEU A N     1 
ATOM   295   C  CA    . LEU A 1 37  ? 16.804  -15.173 -11.646 1 34.24 ? 37  LEU A CA    1 
ATOM   296   C  C     . LEU A 1 37  ? 16.587  -14.242 -10.431 1 34.2  ? 37  LEU A C     1 
ATOM   297   O  O     . LEU A 1 37  ? 17.533  -13.966 -9.693  1 34.31 ? 37  LEU A O     1 
ATOM   298   C  CB    . LEU A 1 37  ? 17.1    -14.379 -12.917 1 34.71 ? 37  LEU A CB    1 
ATOM   299   C  CG    . LEU A 1 37  ? 17.651  -15.231 -14.042 1 36.55 ? 37  LEU A CG    1 
ATOM   300   C  CD1   . LEU A 1 37  ? 17.326  -14.642 -15.39  1 37.25 ? 37  LEU A CD1   1 
ATOM   301   C  CD2   . LEU A 1 37  ? 19.128  -15.461 -13.862 1 37.24 ? 37  LEU A CD2   1 
ATOM   302   N  N     . SER A 1 38  ? 15.345  -13.807 -10.193 1 33.82 ? 38  SER A N     1 
ATOM   303   C  CA    . SER A 1 38  ? 15.033  -12.904 -9.085  1 34.06 ? 38  SER A CA    1 
ATOM   304   C  C     . SER A 1 38  ? 14.634  -13.578 -7.799  1 34.24 ? 38  SER A C     1 
ATOM   305   O  O     . SER A 1 38  ? 14.663  -12.936 -6.754  1 34.54 ? 38  SER A O     1 
ATOM   306   C  CB    . SER A 1 38  ? 13.866  -12.009 -9.47   1 35.43 ? 38  SER A CB    1 
ATOM   307   O  OG    . SER A 1 38  ? 14.31   -10.906 -10.232 1 37.91 ? 38  SER A OG    1 
ATOM   308   N  N     . CYS A 1 39  ? 14.159  -14.823 -7.875  1 33.85 ? 39  CYS A N     1 
ATOM   309   C  CA    . CYS A 1 39  ? 13.589  -15.492 -6.725  1 33.64 ? 39  CYS A CA    1 
ATOM   310   C  C     . CYS A 1 39  ? 14.424  -16.589 -6.126  1 33.14 ? 39  CYS A C     1 
ATOM   311   O  O     . CYS A 1 39  ? 14.38   -17.722 -6.606  1 33.09 ? 39  CYS A O     1 
ATOM   312   C  CB    . CYS A 1 39  ? 12.2    -16.01  -7.075  1 34.46 ? 39  CYS A CB    1 
ATOM   313   S  SG    . CYS A 1 39  ? 11.059  -14.731 -7.664  1 38    ? 39  CYS A SG    1 
ATOM   314   N  N     . PRO A 1 40  ? 15.064  -16.321 -4.977  1 32.66 ? 40  PRO A N     1 
ATOM   315   C  CA    . PRO A 1 40  ? 15.761  -17.405 -4.271  1 32.36 ? 40  PRO A CA    1 
ATOM   316   C  C     . PRO A 1 40  ? 14.776  -18.316 -3.538  1 32.09 ? 40  PRO A C     1 
ATOM   317   O  O     . PRO A 1 40  ? 13.62   -17.946 -3.329  1 31.96 ? 40  PRO A O     1 
ATOM   318   C  CB    . PRO A 1 40  ? 16.669  -16.672 -3.272  1 33    ? 40  PRO A CB    1 
ATOM   319   C  CG    . PRO A 1 40  ? 16.445  -15.213 -3.5    1 33.58 ? 40  PRO A CG    1 
ATOM   320   C  CD    . PRO A 1 40  ? 15.163  -15.049 -4.243  1 32.09 ? 40  PRO A CD    1 
ATOM   321   N  N     . PHE A 1 41  ? 15.231  -19.502 -3.151  1 31.93 ? 41  PHE A N     1 
ATOM   322   C  CA    . PHE A 1 41  ? 14.391  -20.422 -2.405  1 32.34 ? 41  PHE A CA    1 
ATOM   323   C  C     . PHE A 1 41  ? 15.152  -21.112 -1.294  1 32.48 ? 41  PHE A C     1 
ATOM   324   O  O     . PHE A 1 41  ? 16.375  -21.237 -1.351  1 32.76 ? 41  PHE A O     1 
ATOM   325   C  CB    . PHE A 1 41  ? 13.702  -21.455 -3.332  1 32.33 ? 41  PHE A CB    1 
ATOM   326   C  CG    . PHE A 1 41  ? 14.562  -22.614 -3.786  1 32.99 ? 41  PHE A CG    1 
ATOM   327   C  CD1   . PHE A 1 41  ? 14.766  -23.714 -2.967  1 33.69 ? 41  PHE A CD1   1 
ATOM   328   C  CD2   . PHE A 1 41  ? 15.117  -22.63  -5.051  1 33.88 ? 41  PHE A CD2   1 
ATOM   329   C  CE1   . PHE A 1 41  ? 15.58   -24.762 -3.373  1 34.35 ? 41  PHE A CE1   1 
ATOM   330   C  CE2   . PHE A 1 41  ? 15.901  -23.698 -5.468  1 34.48 ? 41  PHE A CE2   1 
ATOM   331   C  CZ    . PHE A 1 41  ? 16.134  -24.752 -4.624  1 34.16 ? 41  PHE A CZ    1 
ATOM   332   N  N     . ILE A 1 42  ? 14.42   -21.582 -0.293  1 32.1  ? 42  ILE A N     1 
ATOM   333   C  CA    . ILE A 1 42  ? 14.963  -22.421 0.746   1 32.47 ? 42  ILE A CA    1 
ATOM   334   C  C     . ILE A 1 42  ? 14.013  -23.602 0.874   1 32.92 ? 42  ILE A C     1 
ATOM   335   O  O     . ILE A 1 42  ? 12.812  -23.422 1.065   1 33.42 ? 42  ILE A O     1 
ATOM   336   C  CB    . ILE A 1 42  ? 15.286  -21.727 2.091   1 33.01 ? 42  ILE A CB    1 
ATOM   337   C  CG1   . ILE A 1 42  ? 15.821  -22.756 3.104   1 33.89 ? 42  ILE A CG1   1 
ATOM   338   C  CG2   . ILE A 1 42  ? 14.086  -20.975 2.647   1 33.59 ? 42  ILE A CG2   1 
ATOM   339   C  CD1   . ILE A 1 42  ? 16.376  -22.195 4.34    1 35.03 ? 42  ILE A CD1   1 
ATOM   340   N  N     . GLU A 1 43  ? 14.529  -24.801 0.654   1 32.43 ? 43  GLU A N     1 
ATOM   341   C  CA    . GLU A 1 43  ? 13.753  -26.017 0.719   1 32.5  ? 43  GLU A CA    1 
ATOM   342   C  C     . GLU A 1 43  ? 14.204  -26.745 1.957   1 32.66 ? 43  GLU A C     1 
ATOM   343   O  O     . GLU A 1 43  ? 15.398  -26.972 2.124   1 32.8  ? 43  GLU A O     1 
ATOM   344   C  CB    . GLU A 1 43  ? 14.028  -26.863 -0.527  1 34.62 ? 43  GLU A CB    1 
ATOM   345   C  CG    . GLU A 1 43  ? 13.077  -28.029 -0.699  1 38.82 ? 43  GLU A CG    1 
ATOM   346   C  CD    . GLU A 1 43  ? 13.141  -28.727 -2.047  1 43.57 ? 43  GLU A CD    1 
ATOM   347   O  OE1   . GLU A 1 43  ? 13.819  -28.211 -2.964  1 44.69 ? 43  GLU A OE1   1 
ATOM   348   O  OE2   . GLU A 1 43  ? 12.507  -29.796 -2.185  1 44.82 ? 43  GLU A OE2   1 
ATOM   349   N  N     . ILE A 1 44  ? 13.273  -27.058 2.862   1 32.58 ? 44  ILE A N     1 
ATOM   350   C  CA    . ILE A 1 44  ? 13.616  -27.755 4.092   1 32.9  ? 44  ILE A CA    1 
ATOM   351   C  C     . ILE A 1 44  ? 12.83   -29.041 4.279   1 33.53 ? 44  ILE A C     1 
ATOM   352   O  O     . ILE A 1 44  ? 11.653  -29.127 3.926   1 33.89 ? 44  ILE A O     1 
ATOM   353   C  CB    . ILE A 1 44  ? 13.511  -26.854 5.342   1 33.12 ? 44  ILE A CB    1 
ATOM   354   C  CG1   . ILE A 1 44  ? 12.058  -26.447 5.628   1 33.66 ? 44  ILE A CG1   1 
ATOM   355   C  CG2   . ILE A 1 44  ? 14.431  -25.646 5.245   1 33.77 ? 44  ILE A CG2   1 
ATOM   356   C  CD1   . ILE A 1 44  ? 11.855  -25.889 6.989   1 34.61 ? 44  ILE A CD1   1 
ATOM   357   N  N     . ILE A 1 45  ? 13.502  -30.05  4.824   1 33.43 ? 45  ILE A N     1 
ATOM   358   C  CA    . ILE A 1 45  ? 12.904  -31.326 5.171   1 33.7  ? 45  ILE A CA    1 
ATOM   359   C  C     . ILE A 1 45  ? 13.104  -31.412 6.666   1 34.08 ? 45  ILE A C     1 
ATOM   360   O  O     . ILE A 1 45  ? 14.244  -31.41  7.12    1 34.17 ? 45  ILE A O     1 
ATOM   361   C  CB    . ILE A 1 45  ? 13.597  -32.513 4.462   1 34.02 ? 45  ILE A CB    1 
ATOM   362   C  CG1   . ILE A 1 45  ? 13.468  -32.391 2.941   1 34.88 ? 45  ILE A CG1   1 
ATOM   363   C  CG2   . ILE A 1 45  ? 13.022  -33.832 4.962   1 34.47 ? 45  ILE A CG2   1 
ATOM   364   C  CD1   . ILE A 1 45  ? 14.231  -33.399 2.164   1 36.32 ? 45  ILE A CD1   1 
ATOM   365   N  N     . PHE A 1 46  ? 12.023  -31.421 7.436   1 34.13 ? 46  PHE A N     1 
ATOM   366   C  CA    . PHE A 1 46  ? 12.122  -31.492 8.893   1 34.44 ? 46  PHE A CA    1 
ATOM   367   C  C     . PHE A 1 46  ? 11.136  -32.51  9.456   1 35.11 ? 46  PHE A C     1 
ATOM   368   O  O     . PHE A 1 46  ? 10.312  -33.041 8.709   1 35.61 ? 46  PHE A O     1 
ATOM   369   C  CB    . PHE A 1 46  ? 11.915  -30.101 9.516   1 34.13 ? 46  PHE A CB    1 
ATOM   370   C  CG    . PHE A 1 46  ? 10.51   -29.562 9.404   1 34.67 ? 46  PHE A CG    1 
ATOM   371   C  CD1   . PHE A 1 46  ? 10.098  -28.892 8.268   1 35.55 ? 46  PHE A CD1   1 
ATOM   372   C  CD2   . PHE A 1 46  ? 9.619   -29.677 10.454  1 35.37 ? 46  PHE A CD2   1 
ATOM   373   C  CE1   . PHE A 1 46  ? 8.813   -28.381 8.173   1 36.25 ? 46  PHE A CE1   1 
ATOM   374   C  CE2   . PHE A 1 46  ? 8.328   -29.179 10.349  1 36.03 ? 46  PHE A CE2   1 
ATOM   375   C  CZ    . PHE A 1 46  ? 7.939   -28.52  9.217   1 35.94 ? 46  PHE A CZ    1 
ATOM   376   N  N     . LYS A 1 47  ? 11.213  -32.794 10.765  1 35.02 ? 47  LYS A N     1 
ATOM   377   C  CA    . LYS A 1 47  ? 10.29   -33.737 11.374  1 35.56 ? 47  LYS A CA    1 
ATOM   378   C  C     . LYS A 1 47  ? 9.761   -33.28  12.722  1 36.09 ? 47  LYS A C     1 
ATOM   379   O  O     . LYS A 1 47  ? 10.39   -32.486 13.419  1 36.16 ? 47  LYS A O     1 
ATOM   380   C  CB    . LYS A 1 47  ? 10.922  -35.133 11.485  1 37.31 ? 47  LYS A CB    1 
ATOM   381   C  CG    . LYS A 1 47  ? 12.148  -35.163 12.385  1 40.92 ? 47  LYS A CG    1 
ATOM   382   C  CD    . LYS A 1 47  ? 12.771  -36.545 12.441  1 44.39 ? 47  LYS A CD    1 
ATOM   383   C  CE    . LYS A 1 47  ? 14.09   -36.554 13.18   1 47.1  ? 47  LYS A CE    1 
ATOM   384   N  NZ    . LYS A 1 47  ? 14.038  -35.909 14.525  1 48.37 ? 47  LYS A NZ    1 
ATOM   385   N  N     . GLU A 1 48  ? 8.586   -33.777 13.073  1 36.24 ? 48  GLU A N     1 
ATOM   386   C  CA    . GLU A 1 48  ? 7.959   -33.551 14.355  1 36.84 ? 48  GLU A CA    1 
ATOM   387   C  C     . GLU A 1 48  ? 7.784   -34.961 14.889  1 37.36 ? 48  GLU A C     1 
ATOM   388   O  O     . GLU A 1 48  ? 6.722   -35.564 14.734  1 37.76 ? 48  GLU A O     1 
ATOM   389   C  CB    . GLU A 1 48  ? 6.605   -32.866 14.173  1 38.98 ? 48  GLU A CB    1 
ATOM   390   C  CG    . GLU A 1 48  ? 6.722   -31.447 13.652  1 43.16 ? 48  GLU A CG    1 
ATOM   391   C  CD    . GLU A 1 48  ? 5.406   -30.708 13.516  1 48.58 ? 48  GLU A CD    1 
ATOM   392   O  OE1   . GLU A 1 48  ? 4.343   -31.364 13.599  1 50.11 ? 48  GLU A OE1   1 
ATOM   393   O  OE2   . GLU A 1 48  ? 5.435   -29.472 13.319  1 50.02 ? 48  GLU A OE2   1 
ATOM   394   N  N     . GLY A 1 49  ? 8.865   -35.516 15.421  1 37.11 ? 49  GLY A N     1 
ATOM   395   C  CA    . GLY A 1 49  ? 8.872   -36.891 15.89   1 37.14 ? 49  GLY A CA    1 
ATOM   396   C  C     . GLY A 1 49  ? 8.908   -37.848 14.715  1 37.08 ? 49  GLY A C     1 
ATOM   397   O  O     . GLY A 1 49  ? 9.894   -37.893 13.979  1 37.05 ? 49  GLY A O     1 
ATOM   398   N  N     . HIS A 1 50  ? 7.829   -38.6   14.511  1 36.91 ? 50  HIS A N     1 
ATOM   399   C  CA    . HIS A 1 50  ? 7.728   -39.532 13.385  1 37.11 ? 50  HIS A CA    1 
ATOM   400   C  C     . HIS A 1 50  ? 7.162   -38.867 12.119  1 37.19 ? 50  HIS A C     1 
ATOM   401   O  O     . HIS A 1 50  ? 7.177   -39.494 11.065  1 37.35 ? 50  HIS A O     1 
ATOM   402   C  CB    . HIS A 1 50  ? 6.814   -40.718 13.747  1 38.07 ? 50  HIS A CB    1 
ATOM   403   C  CG    . HIS A 1 50  ? 7.369   -41.69  14.746  1 40.44 ? 50  HIS A CG    1 
ATOM   404   N  ND1   . HIS A 1 50  ? 7.967   -42.871 14.344  1 42.15 ? 50  HIS A ND1   1 
ATOM   405   C  CD2   . HIS A 1 50  ? 7.332   -41.66  16.101  1 41.55 ? 50  HIS A CD2   1 
ATOM   406   C  CE1   . HIS A 1 50  ? 8.3     -43.502 15.457  1 42.63 ? 50  HIS A CE1   1 
ATOM   407   N  NE2   . HIS A 1 50  ? 7.946   -42.81  16.539  1 42.58 ? 50  HIS A NE2   1 
ATOM   408   N  N     . ASP A 1 51  ? 6.621   -37.641 12.217  1 37.18 ? 51  ASP A N     1 
ATOM   409   C  CA    . ASP A 1 51  ? 6.002   -36.958 11.085  1 37.89 ? 51  ASP A CA    1 
ATOM   410   C  C     . ASP A 1 51  ? 6.957   -36.082 10.288  1 38.38 ? 51  ASP A C     1 
ATOM   411   O  O     . ASP A 1 51  ? 7.379   -35.044 10.783  1 38.54 ? 51  ASP A O     1 
ATOM   412   C  CB    . ASP A 1 51  ? 4.813   -36.117 11.564  1 39.8  ? 51  ASP A CB    1 
ATOM   413   C  CG    . ASP A 1 51  ? 3.468   -36.74  11.262  1 44.26 ? 51  ASP A CG    1 
ATOM   414   O  OD1   . ASP A 1 51  ? 3.22    -37.069 10.074  1 44.63 ? 51  ASP A OD1   1 
ATOM   415   O  OD2   . ASP A 1 51  ? 2.65    -36.882 12.213  1 46.21 ? 51  ASP A OD2   1 
ATOM   416   N  N     . TYR A 1 52  ? 7.257   -36.462 9.038   1 38.49 ? 52  TYR A N     1 
ATOM   417   C  CA    . TYR A 1 52  ? 8.131   -35.66  8.184   1 39.09 ? 52  TYR A CA    1 
ATOM   418   C  C     . TYR A 1 52  ? 7.337   -34.618 7.409   1 38.28 ? 52  TYR A C     1 
ATOM   419   O  O     . TYR A 1 52  ? 6.18    -34.846 7.058   1 38.11 ? 52  TYR A O     1 
ATOM   420   C  CB    . TYR A 1 52  ? 8.922   -36.539 7.203   1 40.2  ? 52  TYR A CB    1 
ATOM   421   C  CG    . TYR A 1 52  ? 10.178  -37.146 7.791   1 42.36 ? 52  TYR A CG    1 
ATOM   422   C  CD1   . TYR A 1 52  ? 11.385  -36.459 7.766   1 43.75 ? 52  TYR A CD1   1 
ATOM   423   C  CD2   . TYR A 1 52  ? 10.166  -38.419 8.345   1 43.87 ? 52  TYR A CD2   1 
ATOM   424   C  CE1   . TYR A 1 52  ? 12.542  -37.014 8.301   1 45.04 ? 52  TYR A CE1   1 
ATOM   425   C  CE2   . TYR A 1 52  ? 11.315  -38.985 8.884   1 45.06 ? 52  TYR A CE2   1 
ATOM   426   C  CZ    . TYR A 1 52  ? 12.502  -38.279 8.861   1 46.19 ? 52  TYR A CZ    1 
ATOM   427   O  OH    . TYR A 1 52  ? 13.639  -38.834 9.397   1 48.01 ? 52  TYR A OH    1 
ATOM   428   N  N     . PHE A 1 53  ? 7.97    -33.478 7.13    1 37.76 ? 53  PHE A N     1 
ATOM   429   C  CA    . PHE A 1 53  ? 7.37    -32.383 6.373   1 37.83 ? 53  PHE A CA    1 
ATOM   430   C  C     . PHE A 1 53  ? 8.366   -31.855 5.364   1 37.17 ? 53  PHE A C     1 
ATOM   431   O  O     . PHE A 1 53  ? 9.56    -31.773 5.649   1 37.3  ? 53  PHE A O     1 
ATOM   432   C  CB    . PHE A 1 53  ? 6.908   -31.249 7.295   1 38.29 ? 53  PHE A CB    1 
ATOM   433   C  CG    . PHE A 1 53  ? 5.826   -31.657 8.263   1 39.52 ? 53  PHE A CG    1 
ATOM   434   C  CD1   . PHE A 1 53  ? 4.502   -31.705 7.866   1 40.52 ? 53  PHE A CD1   1 
ATOM   435   C  CD2   . PHE A 1 53  ? 6.138   -32.041 9.555   1 40.47 ? 53  PHE A CD2   1 
ATOM   436   C  CE1   . PHE A 1 53  ? 3.512   -32.129 8.741   1 41.24 ? 53  PHE A CE1   1 
ATOM   437   C  CE2   . PHE A 1 53  ? 5.142   -32.443 10.436  1 41.26 ? 53  PHE A CE2   1 
ATOM   438   C  CZ    . PHE A 1 53  ? 3.835   -32.476 10.026  1 41.08 ? 53  PHE A CZ    1 
ATOM   439   N  N     . HIS A 1 54  ? 7.879   -31.505 4.179   1 36.36 ? 54  HIS A N     1 
ATOM   440   C  CA    . HIS A 1 54  ? 8.724   -31.004 3.107   1 36.09 ? 54  HIS A CA    1 
ATOM   441   C  C     . HIS A 1 54  ? 8.18    -29.664 2.671   1 35.76 ? 54  HIS A C     1 
ATOM   442   O  O     . HIS A 1 54  ? 7.128   -29.608 2.043   1 35.98 ? 54  HIS A O     1 
ATOM   443   C  CB    . HIS A 1 54  ? 8.688   -31.987 1.933   1 36.77 ? 54  HIS A CB    1 
ATOM   444   C  CG    . HIS A 1 54  ? 9.697   -31.729 0.858   1 38.48 ? 54  HIS A CG    1 
ATOM   445   N  ND1   . HIS A 1 54  ? 9.921   -32.65  -0.14   1 40.2  ? 54  HIS A ND1   1 
ATOM   446   C  CD2   . HIS A 1 54  ? 10.512  -30.669 0.661   1 39.58 ? 54  HIS A CD2   1 
ATOM   447   C  CE1   . HIS A 1 54  ? 10.856  -32.128 -0.909  1 40.75 ? 54  HIS A CE1   1 
ATOM   448   N  NE2   . HIS A 1 54  ? 11.236  -30.935 -0.471  1 40.73 ? 54  HIS A NE2   1 
ATOM   449   N  N     . TRP A 1 55  ? 8.882   -28.583 3.011   1 35.04 ? 55  TRP A N     1 
ATOM   450   C  CA    . TRP A 1 55  ? 8.438   -27.239 2.672   1 34.59 ? 55  TRP A CA    1 
ATOM   451   C  C     . TRP A 1 55  ? 9.414   -26.538 1.768   1 34.15 ? 55  TRP A C     1 
ATOM   452   O  O     . TRP A 1 55  ? 10.617  -26.753 1.875   1 34.43 ? 55  TRP A O     1 
ATOM   453   C  CB    . TRP A 1 55  ? 8.316   -26.387 3.944   1 34.46 ? 55  TRP A CB    1 
ATOM   454   C  CG    . TRP A 1 55  ? 7.17    -26.705 4.858   1 34.97 ? 55  TRP A CG    1 
ATOM   455   C  CD1   . TRP A 1 55  ? 6.115   -27.537 4.615   1 35.9  ? 55  TRP A CD1   1 
ATOM   456   C  CD2   . TRP A 1 55  ? 6.942   -26.133 6.15    1 34.95 ? 55  TRP A CD2   1 
ATOM   457   N  NE1   . TRP A 1 55  ? 5.263   -27.544 5.694   1 36.22 ? 55  TRP A NE1   1 
ATOM   458   C  CE2   . TRP A 1 55  ? 5.747   -26.686 6.648   1 35.82 ? 55  TRP A CE2   1 
ATOM   459   C  CE3   . TRP A 1 55  ? 7.646   -25.222 6.945   1 35.2  ? 55  TRP A CE3   1 
ATOM   460   C  CZ2   . TRP A 1 55  ? 5.238   -26.344 7.894   1 36.33 ? 55  TRP A CZ2   1 
ATOM   461   C  CZ3   . TRP A 1 55  ? 7.148   -24.9   8.185   1 35.91 ? 55  TRP A CZ3   1 
ATOM   462   C  CH2   . TRP A 1 55  ? 5.954   -25.451 8.645   1 36.23 ? 55  TRP A CH2   1 
ATOM   463   N  N     . ARG A 1 56  ? 8.908   -25.646 0.915   1 33.28 ? 56  ARG A N     1 
ATOM   464   C  CA    . ARG A 1 56  ? 9.763   -24.81  0.093   1 32.74 ? 56  ARG A CA    1 
ATOM   465   C  C     . ARG A 1 56  ? 9.253   -23.384 0.172   1 32.18 ? 56  ARG A C     1 
ATOM   466   O  O     . ARG A 1 56  ? 8.055   -23.149 0.049   1 32.05 ? 56  ARG A O     1 
ATOM   467   C  CB    . ARG A 1 56  ? 9.865   -25.286 -1.357  1 33.79 ? 56  ARG A CB    1 
ATOM   468   C  CG    . ARG A 1 56  ? 11.057  -24.64  -2.059  1 36.74 ? 56  ARG A CG    1 
ATOM   469   C  CD    . ARG A 1 56  ? 11.119  -24.933 -3.54   1 39.58 ? 56  ARG A CD    1 
ATOM   470   N  NE    . ARG A 1 56  ? 10.039  -24.272 -4.269  1 41.96 ? 56  ARG A NE    1 
ATOM   471   C  CZ    . ARG A 1 56  ? 9.44    -24.778 -5.341  1 44.11 ? 56  ARG A CZ    1 
ATOM   472   N  NH1   . ARG A 1 56  ? 9.802   -25.963 -5.818  1 43.84 ? 56  ARG A NH1   1 
ATOM   473   N  NH2   . ARG A 1 56  ? 8.459   -24.112 -5.934  1 44.36 ? 56  ARG A NH2   1 
ATOM   474   N  N     . PHE A 1 57  ? 10.155  -22.44  0.43    1 31.69 ? 57  PHE A N     1 
ATOM   475   C  CA    . PHE A 1 57  ? 9.815   -21.031 0.524   1 31.86 ? 57  PHE A CA    1 
ATOM   476   C  C     . PHE A 1 57  ? 10.46   -20.305 -0.637  1 32.18 ? 57  PHE A C     1 
ATOM   477   O  O     . PHE A 1 57  ? 11.681  -20.251 -0.714  1 32.46 ? 57  PHE A O     1 
ATOM   478   C  CB    . PHE A 1 57  ? 10.314  -20.429 1.85    1 31.73 ? 57  PHE A CB    1 
ATOM   479   C  CG    . PHE A 1 57  ? 9.643   -20.989 3.083   1 32.21 ? 57  PHE A CG    1 
ATOM   480   C  CD1   . PHE A 1 57  ? 10.14   -22.119 3.709   1 33.03 ? 57  PHE A CD1   1 
ATOM   481   C  CD2   . PHE A 1 57  ? 8.513   -20.39  3.609   1 32.66 ? 57  PHE A CD2   1 
ATOM   482   C  CE1   . PHE A 1 57  ? 9.513   -22.647 4.829   1 33.62 ? 57  PHE A CE1   1 
ATOM   483   C  CE2   . PHE A 1 57  ? 7.886   -20.921 4.728   1 33.43 ? 57  PHE A CE2   1 
ATOM   484   C  CZ    . PHE A 1 57  ? 8.392   -22.044 5.332   1 33.34 ? 57  PHE A CZ    1 
ATOM   485   N  N     . ASP A 1 58  ? 9.649   -19.775 -1.557  1 31.98 ? 58  ASP A N     1 
ATOM   486   C  CA    . ASP A 1 58  ? 10.137  -19.018 -2.706  1 32.04 ? 58  ASP A CA    1 
ATOM   487   C  C     . ASP A 1 58  ? 10.039  -17.541 -2.361  1 32.04 ? 58  ASP A C     1 
ATOM   488   O  O     . ASP A 1 58  ? 8.967   -17.053 -2.013  1 32.03 ? 58  ASP A O     1 
ATOM   489   C  CB    . ASP A 1 58  ? 9.317   -19.345 -3.958  1 33.59 ? 58  ASP A CB    1 
ATOM   490   C  CG    . ASP A 1 58  ? 9.389   -20.804 -4.369  1 38.39 ? 58  ASP A CG    1 
ATOM   491   O  OD1   . ASP A 1 58  ? 10.327  -21.504 -3.923  1 39.09 ? 58  ASP A OD1   1 
ATOM   492   O  OD2   . ASP A 1 58  ? 8.517   -21.245 -5.147  1 40.73 ? 58  ASP A OD2   1 
ATOM   493   N  N     . MET A 1 59  ? 11.165  -16.84  -2.406  1 31.74 ? 59  MET A N     1 
ATOM   494   C  CA    . MET A 1 59  ? 11.22   -15.442 -2.019  1 31.75 ? 59  MET A CA    1 
ATOM   495   C  C     . MET A 1 59  ? 11.099  -14.481 -3.197  1 31.99 ? 59  MET A C     1 
ATOM   496   O  O     . MET A 1 59  ? 11.748  -14.66  -4.221  1 32.01 ? 59  MET A O     1 
ATOM   497   C  CB    . MET A 1 59  ? 12.486  -15.188 -1.197  1 31.78 ? 59  MET A CB    1 
ATOM   498   C  CG    . MET A 1 59  ? 12.502  -15.967 0.084   1 32.68 ? 59  MET A CG    1 
ATOM   499   S  SD    . MET A 1 59  ? 14.151  -16.048 0.788   1 34.96 ? 59  MET A SD    1 
ATOM   500   C  CE    . MET A 1 59  ? 14.552  -17.724 0.46    1 34.68 ? 59  MET A CE    1 
ATOM   501   N  N     . PHE A 1 60  ? 10.246  -13.464 -3.047  1 31.87 ? 60  PHE A N     1 
ATOM   502   C  CA    . PHE A 1 60  ? 9.986   -12.465 -4.072  1 32.21 ? 60  PHE A CA    1 
ATOM   503   C  C     . PHE A 1 60  ? 10.415  -11.093 -3.564  1 32.73 ? 60  PHE A C     1 
ATOM   504   O  O     . PHE A 1 60  ? 9.614   -10.359 -2.98   1 32.87 ? 60  PHE A O     1 
ATOM   505   C  CB    . PHE A 1 60  ? 8.497   -12.473 -4.442  1 31.98 ? 60  PHE A CB    1 
ATOM   506   C  CG    . PHE A 1 60  ? 8.099   -13.632 -5.328  1 32.55 ? 60  PHE A CG    1 
ATOM   507   C  CD1   . PHE A 1 60  ? 8.058   -14.925 -4.834  1 33.17 ? 60  PHE A CD1   1 
ATOM   508   C  CD2   . PHE A 1 60  ? 7.762   -13.427 -6.654  1 33.25 ? 60  PHE A CD2   1 
ATOM   509   C  CE1   . PHE A 1 60  ? 7.718   -15.989 -5.658  1 33.75 ? 60  PHE A CE1   1 
ATOM   510   C  CE2   . PHE A 1 60  ? 7.398   -14.491 -7.469  1 33.66 ? 60  PHE A CE2   1 
ATOM   511   C  CZ    . PHE A 1 60  ? 7.383   -15.764 -6.967  1 33.4  ? 60  PHE A CZ    1 
ATOM   512   N  N     . PRO A 1 61  ? 11.7    -10.744 -3.752  1 32.86 ? 61  PRO A N     1 
ATOM   513   C  CA    . PRO A 1 61  ? 12.191  -9.456  -3.244  1 33.11 ? 61  PRO A CA    1 
ATOM   514   C  C     . PRO A 1 61  ? 11.749  -8.256  -4.068  1 33.99 ? 61  PRO A C     1 
ATOM   515   O  O     . PRO A 1 61  ? 11.951  -8.232  -5.267  1 34.54 ? 61  PRO A O     1 
ATOM   516   C  CB    . PRO A 1 61  ? 13.722  -9.616  -3.279  1 33.67 ? 61  PRO A CB    1 
ATOM   517   C  CG    . PRO A 1 61  ? 13.994  -11.063 -3.669  1 34.06 ? 61  PRO A CG    1 
ATOM   518   C  CD    . PRO A 1 61  ? 12.777  -11.518 -4.394  1 32.41 ? 61  PRO A CD    1 
ATOM   519   N  N     . GLY A 1 62  ? 11.182  -7.264  -3.41   1 34.26 ? 62  GLY A N     1 
ATOM   520   C  CA    . GLY A 1 62  ? 10.742  -6.024  -4.033  1 35.16 ? 62  GLY A CA    1 
ATOM   521   C  C     . GLY A 1 62  ? 9.275   -5.992  -4.397  1 35.93 ? 62  GLY A C     1 
ATOM   522   O  O     . GLY A 1 62  ? 8.866   -6.642  -5.357  1 35.96 ? 62  GLY A O     1 
ATOM   523   N  N     . PHE A 1 63  ? 8.472   -5.226  -3.653  1 36.4  ? 63  PHE A N     1 
ATOM   524   C  CA    . PHE A 1 63  ? 7.048   -5.093  -3.964  1 37.24 ? 63  PHE A CA    1 
ATOM   525   C  C     . PHE A 1 63  ? 6.845   -4.133  -5.142  1 38.33 ? 63  PHE A C     1 
ATOM   526   O  O     . PHE A 1 63  ? 7.716   -3.31   -5.433  1 38.39 ? 63  PHE A O     1 
ATOM   527   C  CB    . PHE A 1 63  ? 6.286   -4.537  -2.754  1 36.88 ? 63  PHE A CB    1 
ATOM   528   C  CG    . PHE A 1 63  ? 6.118   -5.474  -1.593  1 37.2  ? 63  PHE A CG    1 
ATOM   529   C  CD1   . PHE A 1 63  ? 5.209   -6.515  -1.647  1 37.74 ? 63  PHE A CD1   1 
ATOM   530   C  CD2   . PHE A 1 63  ? 6.815   -5.274  -0.42   1 37.81 ? 63  PHE A CD2   1 
ATOM   531   C  CE1   . PHE A 1 63  ? 5.029   -7.357  -0.559  1 38.08 ? 63  PHE A CE1   1 
ATOM   532   C  CE2   . PHE A 1 63  ? 6.63    -6.114  0.664   1 38.21 ? 63  PHE A CE2   1 
ATOM   533   C  CZ    . PHE A 1 63  ? 5.737   -7.148  0.588   1 37.76 ? 63  PHE A CZ    1 
ATOM   534   N  N     . ASN A 1 64  ? 5.678   -4.206  -5.794  1 38.98 ? 64  ASN A N     1 
ATOM   535   C  CA    . ASN A 1 64  ? 5.347   -3.276  -6.868  1 40.19 ? 64  ASN A CA    1 
ATOM   536   C  C     . ASN A 1 64  ? 4.921   -1.933  -6.279  1 41.39 ? 64  ASN A C     1 
ATOM   537   O  O     . ASN A 1 64  ? 4.329   -1.883  -5.199  1 41.75 ? 64  ASN A O     1 
ATOM   538   C  CB    . ASN A 1 64  ? 4.206   -3.816  -7.722  1 41.16 ? 64  ASN A CB    1 
ATOM   539   C  CG    . ASN A 1 64  ? 4.635   -4.791  -8.774  1 43.95 ? 64  ASN A CG    1 
ATOM   540   O  OD1   . ASN A 1 64  ? 5.805   -5.158  -8.884  1 44.92 ? 64  ASN A OD1   1 
ATOM   541   N  ND2   . ASN A 1 64  ? 3.693   -5.232  -9.575  1 44.54 ? 64  ASN A ND2   1 
ATOM   542   N  N     . LYS A 1 65  ? 5.204   -0.849  -6.993  1 41.75 ? 65  LYS A N     1 
ATOM   543   C  CA    . LYS A 1 65  ? 4.825   0.49    -6.562  1 42.58 ? 65  LYS A CA    1 
ATOM   544   C  C     . LYS A 1 65  ? 3.613   0.988   -7.355  1 43.82 ? 65  LYS A C     1 
ATOM   545   O  O     . LYS A 1 65  ? 2.755   1.664   -6.801  1 43.71 ? 65  LYS A O     1 
ATOM   546   C  CB    . LYS A 1 65  ? 6.019   1.439   -6.691  1 43.78 ? 65  LYS A CB    1 
ATOM   547   C  CG    . LYS A 1 65  ? 7.116   1.103   -5.695  1 46.59 ? 65  LYS A CG    1 
ATOM   548   C  CD    . LYS A 1 65  ? 8.504   1.185   -6.291  1 50.14 ? 65  LYS A CD    1 
ATOM   549   C  CE    . LYS A 1 65  ? 9.55    0.954   -5.23   1 52.96 ? 65  LYS A CE    1 
ATOM   550   N  NZ    . LYS A 1 65  ? 10.909  1.282   -5.721  1 55.03 ? 65  LYS A NZ    1 
ATOM   551   N  N     . ASN A 1 66  ? 3.533   0.642   -8.647  1 44.89 ? 66  ASN A N     1 
ATOM   552   C  CA    . ASN A 1 66  ? 2.412   1.021   -9.498  1 46.34 ? 66  ASN A CA    1 
ATOM   553   C  C     . ASN A 1 66  ? 1.43    -0.182  -9.589  1 47.73 ? 66  ASN A C     1 
ATOM   554   O  O     . ASN A 1 66  ? 0.637   -0.36   -8.668  1 47.83 ? 66  ASN A O     1 
ATOM   555   C  CB    . ASN A 1 66  ? 2.922   1.553   -10.861 1 47.34 ? 66  ASN A CB    1 
ATOM   556   C  CG    . ASN A 1 66  ? 1.864   2.083   -11.799 1 49.96 ? 66  ASN A CG    1 
ATOM   557   O  OD1   . ASN A 1 66  ? 0.655   1.969   -11.562 1 50.99 ? 66  ASN A OD1   1 
ATOM   558   N  ND2   . ASN A 1 66  ? 2.305   2.676   -12.898 1 50.22 ? 66  ASN A ND2   1 
ATOM   559   N  N     . THR A 1 67  ? 1.495   -1.014  -10.644 1 48.62 ? 67  THR A N     1 
ATOM   560   C  CA    . THR A 1 67  ? 0.622   -2.182  -10.78  1 50.04 ? 67  THR A CA    1 
ATOM   561   C  C     . THR A 1 67  ? 1.378   -3.371  -11.405 1 50.34 ? 67  THR A C     1 
ATOM   562   O  O     . THR A 1 67  ? 1.248   -4.494  -10.914 1 50.53 ? 67  THR A O     1 
ATOM   563   C  CB    . THR A 1 67  ? -0.698  -1.833  -11.503 1 52.31 ? 67  THR A CB    1 
ATOM   564   O  OG1   . THR A 1 67  ? -1.461  -3.028  -11.72  1 53.93 ? 67  THR A OG1   1 
ATOM   565   C  CG2   . THR A 1 67  ? -0.478  -1.093  -12.824 1 52.85 ? 67  THR A CG2   1 
ATOM   566   N  N     . ASN A 1 68  ? 2.17    -3.132  -12.472 1 50.06 ? 68  ASN A N     1 
ATOM   567   C  CA    . ASN A 1 68  ? 2.963   -4.179  -13.122 1 50.33 ? 68  ASN A CA    1 
ATOM   568   C  C     . ASN A 1 68  ? 4.386   -3.668  -13.439 1 49.65 ? 68  ASN A C     1 
ATOM   569   O  O     . ASN A 1 68  ? 4.979   -4.091  -14.437 1 49.69 ? 68  ASN A O     1 
ATOM   570   C  CB    . ASN A 1 68  ? 2.293   -4.666  -14.42  1 52.35 ? 68  ASN A CB    1 
ATOM   571   C  CG    . ASN A 1 68  ? 0.8     -4.889  -14.367 1 56.74 ? 68  ASN A CG    1 
ATOM   572   O  OD1   . ASN A 1 68  ? 0.302   -5.957  -13.979 1 58.1  ? 68  ASN A OD1   1 
ATOM   573   N  ND2   . ASN A 1 68  ? 0.051   -3.897  -14.812 1 57.91 ? 68  ASN A ND2   1 
ATOM   574   N  N     . ASP A 1 69  ? 4.937   -2.766  -12.59  1 48.69 ? 69  ASP A N     1 
ATOM   575   C  CA    . ASP A 1 69  ? 6.271   -2.195  -12.815 1 48.01 ? 69  ASP A CA    1 
ATOM   576   C  C     . ASP A 1 69  ? 7.413   -3.18   -12.561 1 47.09 ? 69  ASP A C     1 
ATOM   577   O  O     . ASP A 1 69  ? 8.379   -3.196  -13.331 1 47.29 ? 69  ASP A O     1 
ATOM   578   C  CB    . ASP A 1 69  ? 6.485   -0.893  -12.036 1 49    ? 69  ASP A CB    1 
ATOM   579   C  CG    . ASP A 1 69  ? 6.302   -1.029  -10.549 1 52.37 ? 69  ASP A CG    1 
ATOM   580   O  OD1   . ASP A 1 69  ? 5.22    -1.484  -10.126 1 52.76 ? 69  ASP A OD1   1 
ATOM   581   O  OD2   . ASP A 1 69  ? 7.23    -0.653  -9.799  1 54.37 ? 69  ASP A OD2   1 
ATOM   582   N  N     . ARG A 1 70  ? 7.311   -3.999  -11.502 1 45.65 ? 70  ARG A N     1 
ATOM   583   C  CA    . ARG A 1 70  ? 8.341   -4.99   -11.228 1 44.47 ? 70  ARG A CA    1 
ATOM   584   C  C     . ARG A 1 70  ? 7.815   -6.384  -11.59  1 42.85 ? 70  ARG A C     1 
ATOM   585   O  O     . ARG A 1 70  ? 8.236   -6.945  -12.583 1 42.84 ? 70  ARG A O     1 
ATOM   586   C  CB    . ARG A 1 70  ? 8.882   -4.873  -9.786  1 45.62 ? 70  ARG A CB    1 
ATOM   587   C  CG    . ARG A 1 70  ? 9.767   -6.036  -9.373  1 47.96 ? 70  ARG A CG    1 
ATOM   588   C  CD    . ARG A 1 70  ? 10.748  -5.643  -8.293  1 50.06 ? 70  ARG A CD    1 
ATOM   589   N  NE    . ARG A 1 70  ? 11.512  -6.791  -7.807  1 51.68 ? 70  ARG A NE    1 
ATOM   590   C  CZ    . ARG A 1 70  ? 12.627  -7.248  -8.368  1 53.09 ? 70  ARG A CZ    1 
ATOM   591   N  NH1   . ARG A 1 70  ? 13.115  -6.673  -9.458  1 52.82 ? 70  ARG A NH1   1 
ATOM   592   N  NH2   . ARG A 1 70  ? 13.257  -8.292  -7.847  1 52.71 ? 70  ARG A NH2   1 
ATOM   593   N  N     . TRP A 1 71  ? 6.859   -6.909  -10.838 1 41.5  ? 71  TRP A N     1 
ATOM   594   C  CA    . TRP A 1 71  ? 6.265   -8.213  -11.101 1 40.62 ? 71  TRP A CA    1 
ATOM   595   C  C     . TRP A 1 71  ? 5.071   -8.067  -12.048 1 40.5  ? 71  TRP A C     1 
ATOM   596   O  O     . TRP A 1 71  ? 4.505   -6.979  -12.158 1 40.62 ? 71  TRP A O     1 
ATOM   597   C  CB    . TRP A 1 71  ? 5.827   -8.863  -9.773  1 39.77 ? 71  TRP A CB    1 
ATOM   598   C  CG    . TRP A 1 71  ? 6.921   -8.915  -8.747  1 39.07 ? 71  TRP A CG    1 
ATOM   599   C  CD1   . TRP A 1 71  ? 7.082   -8.088  -7.679  1 39.5  ? 71  TRP A CD1   1 
ATOM   600   C  CD2   . TRP A 1 71  ? 8.048   -9.798  -8.743  1 38.78 ? 71  TRP A CD2   1 
ATOM   601   N  NE1   . TRP A 1 71  ? 8.23    -8.414  -6.998  1 39.63 ? 71  TRP A NE1   1 
ATOM   602   C  CE2   . TRP A 1 71  ? 8.842   -9.462  -7.631  1 39.31 ? 71  TRP A CE2   1 
ATOM   603   C  CE3   . TRP A 1 71  ? 8.452   -10.855 -9.56   1 39.21 ? 71  TRP A CE3   1 
ATOM   604   C  CZ2   . TRP A 1 71  ? 10.013  -10.148 -7.315  1 39.79 ? 71  TRP A CZ2   1 
ATOM   605   C  CZ3   . TRP A 1 71  ? 9.609   -11.536 -9.241  1 39.92 ? 71  TRP A CZ3   1 
ATOM   606   C  CH2   . TRP A 1 71  ? 10.381  -11.173 -8.138  1 39.92 ? 71  TRP A CH2   1 
ATOM   607   N  N     . ASN A 1 72  ? 4.68    -9.159  -12.724 1 40.19 ? 72  ASN A N     1 
ATOM   608   C  CA    . ASN A 1 72  ? 3.538   -9.144  -13.648 1 40.6  ? 72  ASN A CA    1 
ATOM   609   C  C     . ASN A 1 72  ? 2.203   -8.844  -12.956 1 40.61 ? 72  ASN A C     1 
ATOM   610   O  O     . ASN A 1 72  ? 1.27    -8.355  -13.589 1 40.6  ? 72  ASN A O     1 
ATOM   611   C  CB    . ASN A 1 72  ? 3.456   -10.445 -14.459 1 42.2  ? 72  ASN A CB    1 
ATOM   612   C  CG    . ASN A 1 72  ? 2.862   -11.641 -13.74  1 46.24 ? 72  ASN A CG    1 
ATOM   613   O  OD1   . ASN A 1 72  ? 3.05    -11.844 -12.534 1 47.68 ? 72  ASN A OD1   1 
ATOM   614   N  ND2   . ASN A 1 72  ? 2.137   -12.477 -14.476 1 47.07 ? 72  ASN A ND2   1 
ATOM   615   N  N     . SER A 1 73  ? 2.11    -9.179  -11.668 1 40.55 ? 73  SER A N     1 
ATOM   616   C  CA    . SER A 1 73  ? 0.934   -8.944  -10.851 1 40.97 ? 73  SER A CA    1 
ATOM   617   C  C     . SER A 1 73  ? 1.357   -8.558  -9.437  1 41.03 ? 73  SER A C     1 
ATOM   618   O  O     . SER A 1 73  ? 2.437   -8.935  -8.976  1 41.14 ? 73  SER A O     1 
ATOM   619   C  CB    . SER A 1 73  ? 0.019   -10.165 -10.841 1 42.5  ? 73  SER A CB    1 
ATOM   620   O  OG    . SER A 1 73  ? 0.719   -11.342 -10.479 1 45.2  ? 73  SER A OG    1 
ATOM   621   N  N     . ASN A 1 74  ? 0.513   -7.778  -8.76   1 40.74 ? 74  ASN A N     1 
ATOM   622   C  CA    . ASN A 1 74  ? 0.801   -7.27   -7.426  1 41.07 ? 74  ASN A CA    1 
ATOM   623   C  C     . ASN A 1 74  ? 0.162   -8.117  -6.331  1 41.21 ? 74  ASN A C     1 
ATOM   624   O  O     . ASN A 1 74  ? -1.061  -8.152  -6.23   1 41.67 ? 74  ASN A O     1 
ATOM   625   C  CB    . ASN A 1 74  ? 0.299   -5.823  -7.325  1 42.12 ? 74  ASN A CB    1 
ATOM   626   C  CG    . ASN A 1 74  ? 0.837   -5.037  -6.158  1 44.49 ? 74  ASN A CG    1 
ATOM   627   O  OD1   . ASN A 1 74  ? 1.549   -5.553  -5.291  1 45.5  ? 74  ASN A OD1   1 
ATOM   628   N  ND2   . ASN A 1 74  ? 0.512   -3.757  -6.118  1 44.82 ? 74  ASN A ND2   1 
ATOM   629   N  N     . ILE A 1 75  ? 0.978   -8.738  -5.465  1 40.6  ? 75  ILE A N     1 
ATOM   630   C  CA    . ILE A 1 75  ? 0.445   -9.532  -4.355  1 40.49 ? 75  ILE A CA    1 
ATOM   631   C  C     . ILE A 1 75  ? -0.351  -8.675  -3.349  1 40.01 ? 75  ILE A C     1 
ATOM   632   O  O     . ILE A 1 75  ? -1.265  -9.185  -2.699  1 40.19 ? 75  ILE A O     1 
ATOM   633   C  CB    . ILE A 1 75  ? 1.555   -10.353 -3.665  1 41.15 ? 75  ILE A CB    1 
ATOM   634   C  CG1   . ILE A 1 75  ? 0.962   -11.504 -2.837  1 42.12 ? 75  ILE A CG1   1 
ATOM   635   C  CG2   . ILE A 1 75  ? 2.459   -9.462  -2.821  1 41.72 ? 75  ILE A CG2   1 
ATOM   636   C  CD1   . ILE A 1 75  ? 0.221   -12.506 -3.652  1 43.45 ? 75  ILE A CD1   1 
ATOM   637   N  N     . LEU A 1 76  ? -0.031  -7.369  -3.253  1 39.13 ? 76  LEU A N     1 
ATOM   638   C  CA    . LEU A 1 76  ? -0.737  -6.432  -2.385  1 38.69 ? 76  LEU A CA    1 
ATOM   639   C  C     . LEU A 1 76  ? -2.203  -6.229  -2.816  1 38.62 ? 76  LEU A C     1 
ATOM   640   O  O     . LEU A 1 76  ? -3.01   -5.774  -2.007  1 38.71 ? 76  LEU A O     1 
ATOM   641   C  CB    . LEU A 1 76  ? 0.001   -5.094  -2.335  1 38.58 ? 76  LEU A CB    1 
ATOM   642   C  CG    . LEU A 1 76  ? 1.386   -5.124  -1.706  1 39.77 ? 76  LEU A CG    1 
ATOM   643   C  CD1   . LEU A 1 76  ? 2.151   -3.867  -2.019  1 40.39 ? 76  LEU A CD1   1 
ATOM   644   C  CD2   . LEU A 1 76  ? 1.287   -5.257  -0.227  1 40.42 ? 76  LEU A CD2   1 
ATOM   645   N  N     . ASP A 1 77  ? -2.559  -6.589  -4.069  1 38.37 ? 77  ASP A N     1 
ATOM   646   C  CA    . ASP A 1 77  ? -3.943  -6.492  -4.519  1 38.64 ? 77  ASP A CA    1 
ATOM   647   C  C     . ASP A 1 77  ? -4.86   -7.446  -3.731  1 38.46 ? 77  ASP A C     1 
ATOM   648   O  O     . ASP A 1 77  ? -6.033  -7.126  -3.536  1 38.72 ? 77  ASP A O     1 
ATOM   649   C  CB    . ASP A 1 77  ? -4.085  -6.727  -6.028  1 40.4  ? 77  ASP A CB    1 
ATOM   650   C  CG    . ASP A 1 77  ? -5.514  -6.508  -6.501  1 45.22 ? 77  ASP A CG    1 
ATOM   651   O  OD1   . ASP A 1 77  ? -5.956  -5.339  -6.531  1 46.47 ? 77  ASP A OD1   1 
ATOM   652   O  OD2   . ASP A 1 77  ? -6.204  -7.511  -6.793  1 46.99 ? 77  ASP A OD2   1 
ATOM   653   N  N     . LEU A 1 78  ? -4.329  -8.58   -3.237  1 37.78 ? 78  LEU A N     1 
ATOM   654   C  CA    . LEU A 1 78  ? -5.127  -9.496  -2.419  1 37.65 ? 78  LEU A CA    1 
ATOM   655   C  C     . LEU A 1 78  ? -5.612  -8.841  -1.114  1 37.56 ? 78  LEU A C     1 
ATOM   656   O  O     . LEU A 1 78  ? -6.658  -9.222  -0.584  1 37.77 ? 78  LEU A O     1 
ATOM   657   C  CB    . LEU A 1 78  ? -4.352  -10.779 -2.114  1 37.65 ? 78  LEU A CB    1 
ATOM   658   C  CG    . LEU A 1 78  ? -4.033  -11.661 -3.309  1 38.66 ? 78  LEU A CG    1 
ATOM   659   C  CD1   . LEU A 1 78  ? -3.28   -12.885 -2.863  1 39.23 ? 78  LEU A CD1   1 
ATOM   660   C  CD2   . LEU A 1 78  ? -5.303  -12.071 -4.046  1 39.1  ? 78  LEU A CD2   1 
ATOM   661   N  N     . LEU A 1 79  ? -4.859  -7.847  -0.611  1 37.03 ? 79  LEU A N     1 
ATOM   662   C  CA    . LEU A 1 79  ? -5.231  -7.101  0.575   1 36.95 ? 79  LEU A CA    1 
ATOM   663   C  C     . LEU A 1 79  ? -6.315  -6.1    0.203   1 36.96 ? 79  LEU A C     1 
ATOM   664   O  O     . LEU A 1 79  ? -7.309  -5.994  0.918   1 37.05 ? 79  LEU A O     1 
ATOM   665   C  CB    . LEU A 1 79  ? -4.01   -6.382  1.152   1 37.04 ? 79  LEU A CB    1 
ATOM   666   C  CG    . LEU A 1 79  ? -2.897  -7.287  1.635   1 38.52 ? 79  LEU A CG    1 
ATOM   667   C  CD1   . LEU A 1 79  ? -1.661  -6.489  1.986   1 39.18 ? 79  LEU A CD1   1 
ATOM   668   C  CD2   . LEU A 1 79  ? -3.349  -8.102  2.826   1 39.02 ? 79  LEU A CD2   1 
ATOM   669   N  N     . SER A 1 80  ? -6.161  -5.394  -0.933  1 36.82 ? 80  SER A N     1 
ATOM   670   C  CA    . SER A 1 80  ? -7.167  -4.422  -1.375  1 37.14 ? 80  SER A CA    1 
ATOM   671   C  C     . SER A 1 80  ? -8.507  -5.076  -1.741  1 37.23 ? 80  SER A C     1 
ATOM   672   O  O     . SER A 1 80  ? -9.55   -4.436  -1.619  1 37.25 ? 80  SER A O     1 
ATOM   673   C  CB    . SER A 1 80  ? -6.642  -3.548  -2.509  1 38.24 ? 80  SER A CB    1 
ATOM   674   O  OG    . SER A 1 80  ? -6.41   -4.305  -3.684  1 40.17 ? 80  SER A OG    1 
ATOM   675   N  N     . GLN A 1 81  ? -8.486  -6.357  -2.149  1 37.07 ? 81  GLN A N     1 
ATOM   676   C  CA    . GLN A 1 81  ? -9.715  -7.104  -2.433  1 37.43 ? 81  GLN A CA    1 
ATOM   677   C  C     . GLN A 1 81  ? -10.526 -7.376  -1.147  1 37.8  ? 81  GLN A C     1 
ATOM   678   O  O     . GLN A 1 81  ? -11.729 -7.614  -1.221  1 38.15 ? 81  GLN A O     1 
ATOM   679   C  CB    . GLN A 1 81  ? -9.392  -8.436  -3.13   1 38.72 ? 81  GLN A CB    1 
ATOM   680   C  CG    . GLN A 1 81  ? -8.908  -8.272  -4.565  1 41.27 ? 81  GLN A CG    1 
ATOM   681   C  CD    . GLN A 1 81  ? -8.492  -9.581  -5.176  1 44.51 ? 81  GLN A CD    1 
ATOM   682   O  OE1   . GLN A 1 81  ? -9.076  -10.634 -4.904  1 46.1  ? 81  GLN A OE1   1 
ATOM   683   N  NE2   . GLN A 1 81  ? -7.492  -9.539  -6.042  1 44.34 ? 81  GLN A NE2   1 
ATOM   684   N  N     . LYS A 1 82  ? -9.871  -7.354  0.024   1 37.46 ? 82  LYS A N     1 
ATOM   685   C  CA    . LYS A 1 82  ? -10.526 -7.601  1.296   1 37.49 ? 82  LYS A CA    1 
ATOM   686   C  C     . LYS A 1 82  ? -10.697 -6.341  2.172   1 37.27 ? 82  LYS A C     1 
ATOM   687   O  O     . LYS A 1 82  ? -11.014 -6.458  3.357   1 37.71 ? 82  LYS A O     1 
ATOM   688   C  CB    . LYS A 1 82  ? -9.798  -8.72   2.053   1 39.52 ? 82  LYS A CB    1 
ATOM   689   C  CG    . LYS A 1 82  ? -9.843  -10.067 1.334   1 43.76 ? 82  LYS A CG    1 
ATOM   690   C  CD    . LYS A 1 82  ? -11.173 -10.779 1.563   1 48.65 ? 82  LYS A CD    1 
ATOM   691   C  CE    . LYS A 1 82  ? -11.256 -11.331 2.973   1 52.76 ? 82  LYS A CE    1 
ATOM   692   N  NZ    . LYS A 1 82  ? -12.615 -11.815 3.339   1 55.08 ? 82  LYS A NZ    1 
ATOM   693   N  N     . GLY A 1 83  ? -10.51  -5.158  1.597   1 36.54 ? 83  GLY A N     1 
ATOM   694   C  CA    . GLY A 1 83  ? -10.724 -3.915  2.326   1 36.34 ? 83  GLY A CA    1 
ATOM   695   C  C     . GLY A 1 83  ? -9.517  -3.089  2.726   1 35.86 ? 83  GLY A C     1 
ATOM   696   O  O     . GLY A 1 83  ? -9.683  -2.102  3.449   1 36.26 ? 83  GLY A O     1 
ATOM   697   N  N     . SER A 1 84  ? -8.304  -3.456  2.282   1 34.8  ? 84  SER A N     1 
ATOM   698   C  CA    . SER A 1 84  ? -7.122  -2.661  2.621   1 34.33 ? 84  SER A CA    1 
ATOM   699   C  C     . SER A 1 84  ? -7.016  -1.517  1.623   1 34.37 ? 84  SER A C     1 
ATOM   700   O  O     . SER A 1 84  ? -6.307  -1.633  0.623   1 34.57 ? 84  SER A O     1 
ATOM   701   C  CB    . SER A 1 84  ? -5.861  -3.512  2.604   1 34.84 ? 84  SER A CB    1 
ATOM   702   O  OG    . SER A 1 84  ? -4.737  -2.794  3.08    1 36.27 ? 84  SER A OG    1 
ATOM   703   N  N     . PHE A 1 85  ? -7.751  -0.416  1.881   1 33.99 ? 85  PHE A N     1 
ATOM   704   C  CA    . PHE A 1 85  ? -7.798  0.752   0.999   1 33.96 ? 85  PHE A CA    1 
ATOM   705   C  C     . PHE A 1 85  ? -6.638  1.731   1.168   1 33.78 ? 85  PHE A C     1 
ATOM   706   O  O     . PHE A 1 85  ? -6.588  2.714   0.438   1 34.05 ? 85  PHE A O     1 
ATOM   707   C  CB    . PHE A 1 85  ? -9.138  1.49    1.115   1 33.82 ? 85  PHE A CB    1 
ATOM   708   C  CG    . PHE A 1 85  ? -9.485  1.925   2.513   1 34.46 ? 85  PHE A CG    1 
ATOM   709   C  CD1   . PHE A 1 85  ? -8.823  2.978   3.114   1 35.33 ? 85  PHE A CD1   1 
ATOM   710   C  CD2   . PHE A 1 85  ? -10.503 1.307   3.215   1 35.15 ? 85  PHE A CD2   1 
ATOM   711   C  CE1   . PHE A 1 85  ? -9.127  3.358   4.413   1 35.99 ? 85  PHE A CE1   1 
ATOM   712   C  CE2   . PHE A 1 85  ? -10.829 1.717   4.501   1 35.74 ? 85  PHE A CE2   1 
ATOM   713   C  CZ    . PHE A 1 85  ? -10.144 2.744   5.088   1 35.55 ? 85  PHE A CZ    1 
ATOM   714   N  N     . LEU A 1 86  ? -5.739  1.504   2.131   1 33.3  ? 86  LEU A N     1 
ATOM   715   C  CA    . LEU A 1 86  ? -4.567  2.358   2.287   1 33.52 ? 86  LEU A CA    1 
ATOM   716   C  C     . LEU A 1 86  ? -3.392  1.662   1.611   1 33.68 ? 86  LEU A C     1 
ATOM   717   O  O     . LEU A 1 86  ? -3.217  0.455   1.78    1 33.5  ? 86  LEU A O     1 
ATOM   718   C  CB    . LEU A 1 86  ? -4.246  2.64    3.759   1 33.64 ? 86  LEU A CB    1 
ATOM   719   C  CG    . LEU A 1 86  ? -5.309  3.372   4.566   1 34.84 ? 86  LEU A CG    1 
ATOM   720   C  CD1   . LEU A 1 86  ? -4.857  3.565   5.997   1 35.28 ? 86  LEU A CD1   1 
ATOM   721   C  CD2   . LEU A 1 86  ? -5.666  4.701   3.938   1 35.35 ? 86  LEU A CD2   1 
ATOM   722   N  N     . TYR A 1 87  ? -2.587  2.409   0.839   1 33.8  ? 87  TYR A N     1 
ATOM   723   C  CA    . TYR A 1 87  ? -1.446  1.807   0.155   1 34.14 ? 87  TYR A CA    1 
ATOM   724   C  C     . TYR A 1 87  ? -0.216  1.781   1.035   1 33.98 ? 87  TYR A C     1 
ATOM   725   O  O     . TYR A 1 87  ? 0.876   2.178   0.623   1 34.12 ? 87  TYR A O     1 
ATOM   726   C  CB    . TYR A 1 87  ? -1.17   2.441   -1.217  1 34.37 ? 87  TYR A CB    1 
ATOM   727   C  CG    . TYR A 1 87  ? -0.411  1.524   -2.156  1 35.17 ? 87  TYR A CG    1 
ATOM   728   C  CD1   . TYR A 1 87  ? -0.584  0.146   -2.107  1 35.94 ? 87  TYR A CD1   1 
ATOM   729   C  CD2   . TYR A 1 87  ? 0.46    2.036   -3.108  1 35.93 ? 87  TYR A CD2   1 
ATOM   730   C  CE1   . TYR A 1 87  ? 0.108   -0.7    -2.964  1 36.66 ? 87  TYR A CE1   1 
ATOM   731   C  CE2   . TYR A 1 87  ? 1.158   1.198   -3.971  1 36.64 ? 87  TYR A CE2   1 
ATOM   732   C  CZ    . TYR A 1 87  ? 0.973   -0.17   -3.9    1 37.31 ? 87  TYR A CZ    1 
ATOM   733   O  OH    . TYR A 1 87  ? 1.655   -1.011  -4.739  1 38.47 ? 87  TYR A OH    1 
ATOM   734   N  N     . GLU A 1 88  ? -0.406  1.312   2.26    1 33.5  ? 88  GLU A N     1 
ATOM   735   C  CA    . GLU A 1 88  ? 0.665   1.144   3.213   1 33.72 ? 88  GLU A CA    1 
ATOM   736   C  C     . GLU A 1 88  ? 1.17    -0.273  3.013   1 33.53 ? 88  GLU A C     1 
ATOM   737   O  O     . GLU A 1 88  ? 0.383   -1.221  2.962   1 33.66 ? 88  GLU A O     1 
ATOM   738   C  CB    . GLU A 1 88  ? 0.143   1.363   4.625   1 36.4  ? 88  GLU A CB    1 
ATOM   739   C  CG    . GLU A 1 88  ? -0.279  2.798   4.887   1 42.32 ? 88  GLU A CG    1 
ATOM   740   C  CD    . GLU A 1 88  ? 0.493   3.508   5.983   1 49.68 ? 88  GLU A CD    1 
ATOM   741   O  OE1   . GLU A 1 88  ? 1.225   2.826   6.737   1 50.83 ? 88  GLU A OE1   1 
ATOM   742   O  OE2   . GLU A 1 88  ? 0.345   4.746   6.105   1 52.3  ? 88  GLU A OE2   1 
ATOM   743   N  N     . THR A 1 89  ? 2.474   -0.41   2.831   1 33.13 ? 89  THR A N     1 
ATOM   744   C  CA    . THR A 1 89  ? 3.084   -1.685  2.517   1 33.29 ? 89  THR A CA    1 
ATOM   745   C  C     . THR A 1 89  ? 3.82    -2.319  3.684   1 33.83 ? 89  THR A C     1 
ATOM   746   O  O     . THR A 1 89  ? 4.773   -1.736  4.203   1 33.87 ? 89  THR A O     1 
ATOM   747   C  CB    . THR A 1 89  ? 3.999   -1.487  1.317   1 34.16 ? 89  THR A CB    1 
ATOM   748   O  OG1   . THR A 1 89  ? 3.211   -0.991  0.236   1 35.02 ? 89  THR A OG1   1 
ATOM   749   C  CG2   . THR A 1 89  ? 4.698   -2.752  0.903   1 34.53 ? 89  THR A CG2   1 
ATOM   750   N  N     . PRO A 1 90  ? 3.42    -3.543  4.093   1 33.96 ? 90  PRO A N     1 
ATOM   751   C  CA    . PRO A 1 90  ? 4.165   -4.228  5.158   1 34.16 ? 90  PRO A CA    1 
ATOM   752   C  C     . PRO A 1 90  ? 5.539   -4.707  4.666   1 34.68 ? 90  PRO A C     1 
ATOM   753   O  O     . PRO A 1 90  ? 5.802   -4.699  3.461   1 34.7  ? 90  PRO A O     1 
ATOM   754   C  CB    . PRO A 1 90  ? 3.258   -5.407  5.508   1 34.69 ? 90  PRO A CB    1 
ATOM   755   C  CG    . PRO A 1 90  ? 2.572   -5.726  4.232   1 35.1  ? 90  PRO A CG    1 
ATOM   756   C  CD    . PRO A 1 90  ? 2.338   -4.394  3.555   1 33.48 ? 90  PRO A CD    1 
ATOM   757   N  N     . ASP A 1 91  ? 6.416   -5.124  5.587   1 34.73 ? 91  ASP A N     1 
ATOM   758   C  CA    . ASP A 1 91  ? 7.751   -5.573  5.194   1 34.95 ? 91  ASP A CA    1 
ATOM   759   C  C     . ASP A 1 91  ? 7.718   -6.914  4.484   1 34.3  ? 91  ASP A C     1 
ATOM   760   O  O     . ASP A 1 91  ? 8.448   -7.104  3.515   1 34.01 ? 91  ASP A O     1 
ATOM   761   C  CB    . ASP A 1 91  ? 8.713   -5.575  6.386   1 37.24 ? 91  ASP A CB    1 
ATOM   762   C  CG    . ASP A 1 91  ? 9.089   -4.186  6.885   1 42.75 ? 91  ASP A CG    1 
ATOM   763   O  OD1   . ASP A 1 91  ? 8.856   -3.194  6.143   1 43.67 ? 91  ASP A OD1   1 
ATOM   764   O  OD2   . ASP A 1 91  ? 9.621   -4.088  8.007   1 44.97 ? 91  ASP A OD2   1 
ATOM   765   N  N     . VAL A 1 92  ? 6.843   -7.825  4.939   1 33.97 ? 92  VAL A N     1 
ATOM   766   C  CA    . VAL A 1 92  ? 6.703   -9.163  4.373   1 34.22 ? 92  VAL A CA    1 
ATOM   767   C  C     . VAL A 1 92  ? 5.225   -9.583  4.278   1 34.46 ? 92  VAL A C     1 
ATOM   768   O  O     . VAL A 1 92  ? 4.415   -9.181  5.101   1 34.23 ? 92  VAL A O     1 
ATOM   769   C  CB    . VAL A 1 92  ? 7.517   -10.184 5.223   1 34.9  ? 92  VAL A CB    1 
ATOM   770   C  CG1   . VAL A 1 92  ? 7.169   -11.626 4.875   1 35.58 ? 92  VAL A CG1   1 
ATOM   771   C  CG2   . VAL A 1 92  ? 9.017   -9.963  5.092   1 35.38 ? 92  VAL A CG2   1 
ATOM   772   N  N     . ILE A 1 93  ? 4.889   -10.393 3.261   1 34.86 ? 93  ILE A N     1 
ATOM   773   C  CA    . ILE A 1 93  ? 3.591   -11.037 3.065   1 35.66 ? 93  ILE A CA    1 
ATOM   774   C  C     . ILE A 1 93  ? 3.903   -12.52  2.85    1 36.16 ? 93  ILE A C     1 
ATOM   775   O  O     . ILE A 1 93  ? 4.635   -12.851 1.918   1 36.33 ? 93  ILE A O     1 
ATOM   776   C  CB    . ILE A 1 93  ? 2.792   -10.495 1.855   1 36.33 ? 93  ILE A CB    1 
ATOM   777   C  CG1   . ILE A 1 93  ? 2.4     -9.026  2.038   1 37.21 ? 93  ILE A CG1   1 
ATOM   778   C  CG2   . ILE A 1 93  ? 1.553   -11.374 1.59    1 36.91 ? 93  ILE A CG2   1 
ATOM   779   C  CD1   . ILE A 1 93  ? 1.825   -8.44   0.788   1 38.42 ? 93  ILE A CD1   1 
ATOM   780   N  N     . ILE A 1 94  ? 3.388   -13.405 3.711   1 36.27 ? 94  ILE A N     1 
ATOM   781   C  CA    . ILE A 1 94  ? 3.611   -14.84  3.553   1 36.82 ? 94  ILE A CA    1 
ATOM   782   C  C     . ILE A 1 94  ? 2.372   -15.424 2.912   1 37.54 ? 94  ILE A C     1 
ATOM   783   O  O     . ILE A 1 94  ? 1.274   -15.186 3.4     1 37.75 ? 94  ILE A O     1 
ATOM   784   C  CB    . ILE A 1 94  ? 3.896   -15.532 4.909   1 37.11 ? 94  ILE A CB    1 
ATOM   785   C  CG1   . ILE A 1 94  ? 5.072   -14.866 5.649   1 37.89 ? 94  ILE A CG1   1 
ATOM   786   C  CG2   . ILE A 1 94  ? 4.099   -17.042 4.723   1 37.49 ? 94  ILE A CG2   1 
ATOM   787   C  CD1   . ILE A 1 94  ? 5.366   -15.427 7.01    1 39.01 ? 94  ILE A CD1   1 
ATOM   788   N  N     . THR A 1 95  ? 2.527   -16.143 1.804   1 37.85 ? 95  THR A N     1 
ATOM   789   C  CA    . THR A 1 95  ? 1.392   -16.766 1.138   1 38.87 ? 95  THR A CA    1 
ATOM   790   C  C     . THR A 1 95  ? 1.564   -18.285 1.048   1 39.84 ? 95  THR A C     1 
ATOM   791   O  O     . THR A 1 95  ? 2.673   -18.798 1.146   1 39.85 ? 95  THR A O     1 
ATOM   792   C  CB    . THR A 1 95  ? 1.164   -16.157 -0.252  1 40.2  ? 95  THR A CB    1 
ATOM   793   O  OG1   . THR A 1 95  ? 2.211   -16.578 -1.122  1 41.49 ? 95  THR A OG1   1 
ATOM   794   C  CG2   . THR A 1 95  ? 1.07    -14.652 -0.229  1 40.48 ? 95  THR A CG2   1 
ATOM   795   N  N     . SER A 1 96  ? 0.458   -18.993 0.847   1 40.47 ? 96  SER A N     1 
ATOM   796   C  CA    . SER A 1 96  ? 0.445   -20.428 0.649   1 41.63 ? 96  SER A CA    1 
ATOM   797   C  C     . SER A 1 96  ? 0.018   -20.687 -0.802  1 42.34 ? 96  SER A C     1 
ATOM   798   O  O     . SER A 1 96  ? -0.877  -20.009 -1.312  1 42.44 ? 96  SER A O     1 
ATOM   799   C  CB    . SER A 1 96  ? -0.546  -21.082 1.604   1 43.36 ? 96  SER A CB    1 
ATOM   800   O  OG    . SER A 1 96  ? -0.648  -22.472 1.346   1 46.3  ? 96  SER A OG    1 
ATOM   801   N  N     . LEU A 1 97  ? 0.661   -21.648 -1.473  1 42.69 ? 97  LEU A N     1 
ATOM   802   C  CA    . LEU A 1 97  ? 0.298   -21.984 -2.846  1 43.46 ? 97  LEU A CA    1 
ATOM   803   C  C     . LEU A 1 97  ? -0.669  -23.152 -2.853  1 44.35 ? 97  LEU A C     1 
ATOM   804   O  O     . LEU A 1 97  ? -0.277  -24.266 -2.523  1 44.61 ? 97  LEU A O     1 
ATOM   805   C  CB    . LEU A 1 97  ? 1.533   -22.352 -3.678  1 43.63 ? 97  LEU A CB    1 
ATOM   806   C  CG    . LEU A 1 97  ? 2.384   -21.215 -4.238  1 45.14 ? 97  LEU A CG    1 
ATOM   807   C  CD1   . LEU A 1 97  ? 3.403   -21.752 -5.211  1 45.97 ? 97  LEU A CD1   1 
ATOM   808   C  CD2   . LEU A 1 97  ? 1.544   -20.209 -4.977  1 45.69 ? 97  LEU A CD2   1 
ATOM   809   N  N     . ASN A 1 98  ? -1.922  -22.905 -3.228  1 44.72 ? 98  ASN A N     1 
ATOM   810   C  CA    . ASN A 1 98  ? -2.929  -23.951 -3.306  1 45.51 ? 98  ASN A CA    1 
ATOM   811   C  C     . ASN A 1 98  ? -3.758  -23.773 -4.56   1 45.7  ? 98  ASN A C     1 
ATOM   812   O  O     . ASN A 1 98  ? -4.148  -22.654 -4.86   1 46.12 ? 98  ASN A O     1 
ATOM   813   C  CB    . ASN A 1 98  ? -3.819  -23.948 -2.07   1 47.12 ? 98  ASN A CB    1 
ATOM   814   C  CG    . ASN A 1 98  ? -3.411  -25.048 -1.133  1 50.98 ? 98  ASN A CG    1 
ATOM   815   O  OD1   . ASN A 1 98  ? -3.099  -24.841 0.043   1 52.17 ? 98  ASN A OD1   1 
ATOM   816   N  ND2   . ASN A 1 98  ? -3.416  -26.269 -1.655  1 51.94 ? 98  ASN A ND2   1 
ATOM   817   N  N     . ASN A 1 99  ? -4.048  -24.871 -5.272  1 45.25 ? 99  ASN A N     1 
ATOM   818   C  CA    . ASN A 1 99  ? -4.84   -24.922 -6.509  1 45.25 ? 99  ASN A CA    1 
ATOM   819   C  C     . ASN A 1 99  ? -4.475  -23.833 -7.551  1 44.67 ? 99  ASN A C     1 
ATOM   820   O  O     . ASN A 1 99  ? -5.361  -23.201 -8.125  1 45.02 ? 99  ASN A O     1 
ATOM   821   C  CB    . ASN A 1 99  ? -6.369  -24.955 -6.241  1 46.64 ? 99  ASN A CB    1 
ATOM   822   C  CG    . ASN A 1 99  ? -6.935  -23.928 -5.277  1 50    ? 99  ASN A CG    1 
ATOM   823   O  OD1   . ASN A 1 99  ? -7.055  -22.74  -5.597  1 51.49 ? 99  ASN A OD1   1 
ATOM   824   N  ND2   . ASN A 1 99  ? -7.309  -24.363 -4.078  1 50.36 ? 99  ASN A ND2   1 
ATOM   825   N  N     . GLY A 1 100 ? -3.179  -23.663 -7.81   1 43.57 ? 100 GLY A N     1 
ATOM   826   C  CA    . GLY A 1 100 ? -2.681  -22.717 -8.804  1 42.79 ? 100 GLY A CA    1 
ATOM   827   C  C     . GLY A 1 100 ? -2.801  -21.244 -8.462  1 41.82 ? 100 GLY A C     1 
ATOM   828   O  O     . GLY A 1 100 ? -2.7    -20.396 -9.35   1 41.98 ? 100 GLY A O     1 
ATOM   829   N  N     . LYS A 1 101 ? -3.005  -20.914 -7.182  1 40.71 ? 101 LYS A N     1 
ATOM   830   C  CA    . LYS A 1 101 ? -3.122  -19.52  -6.755  1 40.08 ? 101 LYS A CA    1 
ATOM   831   C  C     . LYS A 1 101 ? -2.501  -19.294 -5.366  1 39.01 ? 101 LYS A C     1 
ATOM   832   O  O     . LYS A 1 101 ? -2.27   -20.248 -4.619  1 38.99 ? 101 LYS A O     1 
ATOM   833   C  CB    . LYS A 1 101 ? -4.594  -19.069 -6.775  1 42.03 ? 101 LYS A CB    1 
ATOM   834   C  CG    . LYS A 1 101 ? -5.425  -19.673 -5.646  1 46.12 ? 101 LYS A CG    1 
ATOM   835   C  CD    . LYS A 1 101 ? -6.872  -19.229 -5.68   1 50.56 ? 101 LYS A CD    1 
ATOM   836   C  CE    . LYS A 1 101 ? -7.571  -19.466 -4.364  1 54.21 ? 101 LYS A CE    1 
ATOM   837   N  NZ    . LYS A 1 101 ? -8.867  -18.738 -4.286  1 56.24 ? 101 LYS A NZ    1 
ATOM   838   N  N     . GLU A 1 102 ? -2.249  -18.027 -5.012  1 37.96 ? 102 GLU A N     1 
ATOM   839   C  CA    . GLU A 1 102 ? -1.679  -17.698 -3.713  1 37.51 ? 102 GLU A CA    1 
ATOM   840   C  C     . GLU A 1 102 ? -2.766  -17.288 -2.73   1 36.98 ? 102 GLU A C     1 
ATOM   841   O  O     . GLU A 1 102 ? -3.749  -16.659 -3.117  1 37.33 ? 102 GLU A O     1 
ATOM   842   C  CB    . GLU A 1 102 ? -0.662  -16.561 -3.843  1 39.16 ? 102 GLU A CB    1 
ATOM   843   C  CG    . GLU A 1 102 ? 0.421   -16.827 -4.861  1 42.53 ? 102 GLU A CG    1 
ATOM   844   C  CD    . GLU A 1 102 ? 1.587   -15.873 -4.748  1 47.34 ? 102 GLU A CD    1 
ATOM   845   O  OE1   . GLU A 1 102 ? 2.056   -15.635 -3.612  1 48.2  ? 102 GLU A OE1   1 
ATOM   846   O  OE2   . GLU A 1 102 ? 2.034   -15.365 -5.801  1 49.02 ? 102 GLU A OE2   1 
ATOM   847   N  N     . GLU A 1 103 ? -2.585  -17.63  -1.455  1 35.84 ? 103 GLU A N     1 
ATOM   848   C  CA    . GLU A 1 103 ? -3.531  -17.263 -0.412  1 35.26 ? 103 GLU A CA    1 
ATOM   849   C  C     . GLU A 1 103 ? -2.727  -16.664 0.737   1 34.09 ? 103 GLU A C     1 
ATOM   850   O  O     . GLU A 1 103 ? -1.824  -17.324 1.238   1 34.45 ? 103 GLU A O     1 
ATOM   851   C  CB    . GLU A 1 103 ? -4.31   -18.503 0.06    1 37.89 ? 103 GLU A CB    1 
ATOM   852   C  CG    . GLU A 1 103 ? -5.294  -19.028 -0.973  1 43.58 ? 103 GLU A CG    1 
ATOM   853   C  CD    . GLU A 1 103 ? -5.638  -20.503 -0.865  1 50.32 ? 103 GLU A CD    1 
ATOM   854   O  OE1   . GLU A 1 103 ? -5.835  -21.144 -1.924  1 51.22 ? 103 GLU A OE1   1 
ATOM   855   O  OE2   . GLU A 1 103 ? -5.707  -21.019 0.275   1 52.29 ? 103 GLU A OE2   1 
ATOM   856   N  N     . ILE A 1 104 ? -3.021  -15.421 1.141   1 32.44 ? 104 ILE A N     1 
ATOM   857   C  CA    . ILE A 1 104 ? -2.279  -14.778 2.23    1 31.3  ? 104 ILE A CA    1 
ATOM   858   C  C     . ILE A 1 104 ? -2.464  -15.492 3.571   1 30.11 ? 104 ILE A C     1 
ATOM   859   O  O     . ILE A 1 104 ? -3.587  -15.793 3.963   1 30.1  ? 104 ILE A O     1 
ATOM   860   C  CB    . ILE A 1 104 ? -2.604  -13.26  2.326   1 31.53 ? 104 ILE A CB    1 
ATOM   861   C  CG1   . ILE A 1 104 ? -2.086  -12.518 1.077   1 32.28 ? 104 ILE A CG1   1 
ATOM   862   C  CG2   . ILE A 1 104 ? -2.053  -12.638 3.625   1 31.81 ? 104 ILE A CG2   1 
ATOM   863   C  CD1   . ILE A 1 104 ? -2.362  -11.07  1.027   1 33.31 ? 104 ILE A CD1   1 
ATOM   864   N  N     . LEU A 1 105 ? -1.355  -15.757 4.267   1 29.01 ? 105 LEU A N     1 
ATOM   865   C  CA    . LEU A 1 105 ? -1.352  -16.365 5.595   1 28.29 ? 105 LEU A CA    1 
ATOM   866   C  C     . LEU A 1 105 ? -1.203  -15.291 6.667   1 27.72 ? 105 LEU A C     1 
ATOM   867   O  O     . LEU A 1 105 ? -1.836  -15.397 7.712   1 27.53 ? 105 LEU A O     1 
ATOM   868   C  CB    . LEU A 1 105 ? -0.206  -17.371 5.745   1 27.99 ? 105 LEU A CB    1 
ATOM   869   C  CG    . LEU A 1 105 ? -0.276  -18.614 4.899   1 28.67 ? 105 LEU A CG    1 
ATOM   870   C  CD1   . LEU A 1 105 ? 0.934   -19.46  5.134   1 28.98 ? 105 LEU A CD1   1 
ATOM   871   C  CD2   . LEU A 1 105 ? -1.53   -19.413 5.192   1 29.12 ? 105 LEU A CD2   1 
ATOM   872   N  N     . MET A 1 106 ? -0.336  -14.281 6.417   1 27.48 ? 106 MET A N     1 
ATOM   873   C  CA    . MET A 1 106 ? -0.081  -13.159 7.333   1 27.64 ? 106 MET A CA    1 
ATOM   874   C  C     . MET A 1 106 ? 0.757   -12.04  6.686   1 26.82 ? 106 MET A C     1 
ATOM   875   O  O     . MET A 1 106 ? 1.428   -12.266 5.679   1 26.77 ? 106 MET A O     1 
ATOM   876   C  CB    . MET A 1 106 ? 0.598   -13.637 8.64    1 28.69 ? 106 MET A CB    1 
ATOM   877   C  CG    . MET A 1 106 ? 2.058   -13.964 8.477   1 31.66 ? 106 MET A CG    1 
ATOM   878   S  SD    . MET A 1 106 ? 2.679   -14.807 9.928   1 38.9  ? 106 MET A SD    1 
ATOM   879   C  CE    . MET A 1 106 ? 1.988   -16.409 9.658   1 37.26 ? 106 MET A CE    1 
ATOM   880   N  N     . ALA A 1 107 ? 0.73    -10.847 7.302   1 25.92 ? 107 ALA A N     1 
ATOM   881   C  CA    . ALA A 1 107 ? 1.516   -9.674  6.926   1 25.34 ? 107 ALA A CA    1 
ATOM   882   C  C     . ALA A 1 107 ? 2.415   -9.343  8.123   1 24.62 ? 107 ALA A C     1 
ATOM   883   O  O     . ALA A 1 107 ? 1.952   -9.371  9.262   1 24.93 ? 107 ALA A O     1 
ATOM   884   C  CB    . ALA A 1 107 ? 0.598   -8.504  6.626   1 25.42 ? 107 ALA A CB    1 
ATOM   885   N  N     . ILE A 1 108 ? 3.705   -9.092  7.883   1 23.66 ? 108 ILE A N     1 
ATOM   886   C  CA    . ILE A 1 108 ? 4.663   -8.816  8.954   1 23.46 ? 108 ILE A CA    1 
ATOM   887   C  C     . ILE A 1 108 ? 5.421   -7.507  8.726   1 23.86 ? 108 ILE A C     1 
ATOM   888   O  O     . ILE A 1 108 ? 5.852   -7.223  7.607   1 24.06 ? 108 ILE A O     1 
ATOM   889   C  CB    . ILE A 1 108 ? 5.655   -9.998  9.085   1 23.55 ? 108 ILE A CB    1 
ATOM   890   C  CG1   . ILE A 1 108 ? 4.932   -11.319 9.378   1 24.61 ? 108 ILE A CG1   1 
ATOM   891   C  CG2   . ILE A 1 108 ? 6.733   -9.717  10.119  1 23.79 ? 108 ILE A CG2   1 
ATOM   892   C  CD1   . ILE A 1 108 ? 5.796   -12.509 9.181   1 26.06 ? 108 ILE A CD1   1 
ATOM   893   N  N     . GLU A 1 109 ? 5.611   -6.722  9.792   1 23.76 ? 109 GLU A N     1 
ATOM   894   C  CA    . GLU A 1 109 ? 6.362   -5.475  9.723   1 24.06 ? 109 GLU A CA    1 
ATOM   895   C  C     . GLU A 1 109 ? 7.45    -5.505  10.795  1 24.87 ? 109 GLU A C     1 
ATOM   896   O  O     . GLU A 1 109 ? 7.162   -5.834  11.937  1 25.32 ? 109 GLU A O     1 
ATOM   897   C  CB    . GLU A 1 109 ? 5.423   -4.288  9.932   1 24.94 ? 109 GLU A CB    1 
ATOM   898   C  CG    . GLU A 1 109 ? 6.122   -2.949  9.986   1 27.72 ? 109 GLU A CG    1 
ATOM   899   C  CD    . GLU A 1 109 ? 6.546   -2.396  8.644   1 31.52 ? 109 GLU A CD    1 
ATOM   900   O  OE1   . GLU A 1 109 ? 7.431   -1.511  8.616   1 31.89 ? 109 GLU A OE1   1 
ATOM   901   O  OE2   . GLU A 1 109 ? 5.98    -2.829  7.618   1 33.26 ? 109 GLU A OE2   1 
ATOM   902   N  N     . PHE A 1 110 ? 8.688   -5.198  10.427  1 25.04 ? 110 PHE A N     1 
ATOM   903   C  CA    . PHE A 1 110 ? 9.832   -5.185  11.331  1 25.92 ? 110 PHE A CA    1 
ATOM   904   C  C     . PHE A 1 110 ? 10.227  -3.738  11.597  1 27.05 ? 110 PHE A C     1 
ATOM   905   O  O     . PHE A 1 110 ? 10.527  -3.017  10.645  1 27.55 ? 110 PHE A O     1 
ATOM   906   C  CB    . PHE A 1 110 ? 11.036  -5.896  10.683  1 25.77 ? 110 PHE A CB    1 
ATOM   907   C  CG    . PHE A 1 110 ? 10.785  -7.288  10.148  1 26.19 ? 110 PHE A CG    1 
ATOM   908   C  CD1   . PHE A 1 110 ? 10.413  -7.488  8.835   1 26.52 ? 110 PHE A CD1   1 
ATOM   909   C  CD2   . PHE A 1 110 ? 11.025  -8.395  10.927  1 27.06 ? 110 PHE A CD2   1 
ATOM   910   C  CE1   . PHE A 1 110 ? 10.199  -8.767  8.342   1 27.01 ? 110 PHE A CE1   1 
ATOM   911   C  CE2   . PHE A 1 110 ? 10.79   -9.668  10.436  1 27.57 ? 110 PHE A CE2   1 
ATOM   912   C  CZ    . PHE A 1 110 ? 10.387  -9.847  9.143   1 27    ? 110 PHE A CZ    1 
ATOM   913   N  N     . CYS A 1 111 ? 10.267  -3.31   12.868  1 27.31 ? 111 CYS A N     1 
ATOM   914   C  CA    . CYS A 1 111 ? 10.637  -1.934  13.186  1 28.04 ? 111 CYS A CA    1 
ATOM   915   C  C     . CYS A 1 111 ? 11.706  -1.829  14.249  1 28.19 ? 111 CYS A C     1 
ATOM   916   O  O     . CYS A 1 111 ? 11.455  -2.057  15.424  1 27.94 ? 111 CYS A O     1 
ATOM   917   C  CB    . CYS A 1 111 ? 9.415   -1.094  13.544  1 29.14 ? 111 CYS A CB    1 
ATOM   918   S  SG    . CYS A 1 111 ? 9.686   0.699   13.447  1 33.29 ? 111 CYS A SG    1 
ATOM   919   N  N     . SER A 1 112 ? 12.898  -1.44   13.828  1 28.47 ? 112 SER A N     1 
ATOM   920   C  CA    . SER A 1 112 ? 14.024  -1.212  14.722  1 29.15 ? 112 SER A CA    1 
ATOM   921   C  C     . SER A 1 112 ? 14.022  0.229   15.247  1 29.38 ? 112 SER A C     1 
ATOM   922   O  O     . SER A 1 112 ? 14.486  0.462   16.359  1 29.92 ? 112 SER A O     1 
ATOM   923   C  CB    . SER A 1 112 ? 15.343  -1.507  14.01   1 30.89 ? 112 SER A CB    1 
ATOM   924   O  OG    . SER A 1 112 ? 15.386  -1.075  12.654  1 33.14 ? 112 SER A OG    1 
ATOM   925   N  N     . ALA A 1 113 ? 13.503  1.182   14.443  1 28.89 ? 113 ALA A N     1 
ATOM   926   C  CA    . ALA A 1 113 ? 13.391  2.615   14.716  1 29.12 ? 113 ALA A CA    1 
ATOM   927   C  C     . ALA A 1 113 ? 13.005  2.995   16.137  1 29.02 ? 113 ALA A C     1 
ATOM   928   O  O     . ALA A 1 113 ? 12.242  2.283   16.795  1 28.92 ? 113 ALA A O     1 
ATOM   929   C  CB    . ALA A 1 113 ? 12.4    3.239   13.752  1 29.41 ? 113 ALA A CB    1 
ATOM   930   N  N     . LEU A 1 114 ? 13.488  4.162   16.591  1 28.85 ? 114 LEU A N     1 
ATOM   931   C  CA    . LEU A 1 114 ? 13.16   4.675   17.92   1 29.09 ? 114 LEU A CA    1 
ATOM   932   C  C     . LEU A 1 114 ? 11.676  4.989   17.961  1 29.28 ? 114 LEU A C     1 
ATOM   933   O  O     . LEU A 1 114 ? 11.152  5.634   17.046  1 29.77 ? 114 LEU A O     1 
ATOM   934   C  CB    . LEU A 1 114 ? 13.936  5.963   18.247  1 29.11 ? 114 LEU A CB    1 
ATOM   935   C  CG    . LEU A 1 114 ? 15.459  5.863   18.282  1 30.3  ? 114 LEU A CG    1 
ATOM   936   C  CD1   . LEU A 1 114 ? 16.065  7.207   18.485  1 30.59 ? 114 LEU A CD1   1 
ATOM   937   C  CD2   . LEU A 1 114 ? 15.928  4.919   19.354  1 31.03 ? 114 LEU A CD2   1 
ATOM   938   N  N     . GLN A 1 115 ? 10.99   4.494   18.985  1 28.61 ? 115 GLN A N     1 
ATOM   939   C  CA    . GLN A 1 115 ? 9.569   4.76    19.143  1 28.45 ? 115 GLN A CA    1 
ATOM   940   C  C     . GLN A 1 115 ? 9.504   6.119   19.82   1 28    ? 115 GLN A C     1 
ATOM   941   O  O     . GLN A 1 115 ? 9.244   6.208   21.016  1 28.5  ? 115 GLN A O     1 
ATOM   942   C  CB    . GLN A 1 115 ? 8.918   3.669   20.007  1 30.04 ? 115 GLN A CB    1 
ATOM   943   C  CG    . GLN A 1 115 ? 9.206   2.25    19.521  1 33.49 ? 115 GLN A CG    1 
ATOM   944   C  CD    . GLN A 1 115 ? 8.231   1.788   18.466  1 37.51 ? 115 GLN A CD    1 
ATOM   945   O  OE1   . GLN A 1 115 ? 7.112   1.359   18.78   1 38.95 ? 115 GLN A OE1   1 
ATOM   946   N  NE2   . GLN A 1 115 ? 8.63    1.853   17.192  1 37.14 ? 115 GLN A NE2   1 
ATOM   947   N  N     . ALA A 1 116 ? 9.827   7.169   19.076  1 27.14 ? 116 ALA A N     1 
ATOM   948   C  CA    . ALA A 1 116 ? 9.861   8.517   19.609  1 27.27 ? 116 ALA A CA    1 
ATOM   949   C  C     . ALA A 1 116 ? 8.636   9.317   19.184  1 26.95 ? 116 ALA A C     1 
ATOM   950   O  O     . ALA A 1 116 ? 8.554   9.786   18.054  1 27.19 ? 116 ALA A O     1 
ATOM   951   C  CB    . ALA A 1 116 ? 11.134  9.221   19.157  1 27.66 ? 116 ALA A CB    1 
ATOM   952   N  N     . GLY A 1 117 ? 7.692   9.455   20.091  1 26.38 ? 117 GLY A N     1 
ATOM   953   C  CA    . GLY A 1 117 ? 6.471   10.201  19.834  1 26.39 ? 117 GLY A CA    1 
ATOM   954   C  C     . GLY A 1 117 ? 5.617   9.711   18.687  1 26.17 ? 117 GLY A C     1 
ATOM   955   O  O     . GLY A 1 117 ? 4.996   8.649   18.77   1 26.15 ? 117 GLY A O     1 
ATOM   956   N  N     . ASN A 1 118 ? 5.576   10.494  17.606  1 26.05 ? 118 ASN A N     1 
ATOM   957   C  CA    . ASN A 1 118 ? 4.765   10.138  16.446  1 26.53 ? 118 ASN A CA    1 
ATOM   958   C  C     . ASN A 1 118 ? 5.371   9.032   15.582  1 25.9  ? 118 ASN A C     1 
ATOM   959   O  O     . ASN A 1 118 ? 4.672   8.501   14.724  1 26.09 ? 118 ASN A O     1 
ATOM   960   C  CB    . ASN A 1 118 ? 4.39    11.354  15.609  1 28.84 ? 118 ASN A CB    1 
ATOM   961   C  CG    . ASN A 1 118 ? 5.546   12.124  15.057  1 34.34 ? 118 ASN A CG    1 
ATOM   962   O  OD1   . ASN A 1 118 ? 6.695   11.676  15.1    1 36.37 ? 118 ASN A OD1   1 
ATOM   963   N  ND2   . ASN A 1 118 ? 5.253   13.298  14.502  1 35.6  ? 118 ASN A ND2   1 
ATOM   964   N  N     . GLN A 1 119 ? 6.642   8.656   15.814  1 25.1  ? 119 GLN A N     1 
ATOM   965   C  CA    . GLN A 1 119 ? 7.248   7.544   15.088  1 24.92 ? 119 GLN A CA    1 
ATOM   966   C  C     . GLN A 1 119 ? 6.566   6.212   15.44   1 24.87 ? 119 GLN A C     1 
ATOM   967   O  O     . GLN A 1 119 ? 6.526   5.317   14.606  1 25.01 ? 119 GLN A O     1 
ATOM   968   C  CB    . GLN A 1 119 ? 8.752   7.474   15.35   1 26.24 ? 119 GLN A CB    1 
ATOM   969   C  CG    . GLN A 1 119 ? 9.557   7.435   14.063  1 29.85 ? 119 GLN A CG    1 
ATOM   970   C  CD    . GLN A 1 119 ? 9.719   6.037   13.526  1 34.47 ? 119 GLN A CD    1 
ATOM   971   O  OE1   . GLN A 1 119 ? 9.69    5.057   14.273  1 36.07 ? 119 GLN A OE1   1 
ATOM   972   N  NE2   . GLN A 1 119 ? 9.901   5.918   12.216  1 35.03 ? 119 GLN A NE2   1 
ATOM   973   N  N     . ALA A 1 120 ? 5.985   6.102   16.648  1 24.8  ? 120 ALA A N     1 
ATOM   974   C  CA    . ALA A 1 120 ? 5.262   4.925   17.125  1 25.28 ? 120 ALA A CA    1 
ATOM   975   C  C     . ALA A 1 120 ? 4.019   4.631   16.275  1 25.2  ? 120 ALA A C     1 
ATOM   976   O  O     . ALA A 1 120 ? 3.688   3.464   16.05   1 25.12 ? 120 ALA A O     1 
ATOM   977   C  CB    . ALA A 1 120 ? 4.857   5.125   18.576  1 25.52 ? 120 ALA A CB    1 
ATOM   978   N  N     . TRP A 1 121 ? 3.328   5.683   15.818  1 25.04 ? 121 TRP A N     1 
ATOM   979   C  CA    . TRP A 1 121 ? 2.146   5.499   14.987  1 25.49 ? 121 TRP A CA    1 
ATOM   980   C  C     . TRP A 1 121 ? 2.374   5.808   13.517  1 26.3  ? 121 TRP A C     1 
ATOM   981   O  O     . TRP A 1 121 ? 1.423   5.753   12.75   1 26.54 ? 121 TRP A O     1 
ATOM   982   C  CB    . TRP A 1 121 ? 0.932   6.271   15.519  1 25.29 ? 121 TRP A CB    1 
ATOM   983   C  CG    . TRP A 1 121 ? 1.051   7.769   15.539  1 25.52 ? 121 TRP A CG    1 
ATOM   984   C  CD1   . TRP A 1 121 ? 0.839   8.623   14.496  1 26.31 ? 121 TRP A CD1   1 
ATOM   985   C  CD2   . TRP A 1 121 ? 1.218   8.593   16.702  1 25.47 ? 121 TRP A CD2   1 
ATOM   986   N  NE1   . TRP A 1 121 ? 0.934   9.926   14.925  1 26.61 ? 121 TRP A NE1   1 
ATOM   987   C  CE2   . TRP A 1 121 ? 1.156   9.935   16.279  1 26.28 ? 121 TRP A CE2   1 
ATOM   988   C  CE3   . TRP A 1 121 ? 1.457   8.327   18.055  1 25.82 ? 121 TRP A CE3   1 
ATOM   989   C  CZ2   . TRP A 1 121 ? 1.293   11.001  17.169  1 26.76 ? 121 TRP A CZ2   1 
ATOM   990   C  CZ3   . TRP A 1 121 ? 1.603   9.385   18.93   1 26.54 ? 121 TRP A CZ3   1 
ATOM   991   C  CH2   . TRP A 1 121 ? 1.539   10.702  18.483  1 26.7  ? 121 TRP A CH2   1 
ATOM   992   N  N     . GLN A 1 122 ? 3.617   6.076   13.089  1 26.55 ? 122 GLN A N     1 
ATOM   993   C  CA    . GLN A 1 122 ? 3.911   6.361   11.687  1 27.33 ? 122 GLN A CA    1 
ATOM   994   C  C     . GLN A 1 122 ? 3.424   5.234   10.767  1 28.2  ? 122 GLN A C     1 
ATOM   995   O  O     . GLN A 1 122 ? 2.829   5.5     9.717   1 28.52 ? 122 GLN A O     1 
ATOM   996   C  CB    . GLN A 1 122 ? 5.421   6.594   11.488  1 28.84 ? 122 GLN A CB    1 
ATOM   997   C  CG    . GLN A 1 122 ? 5.802   6.822   10.028  1 32.31 ? 122 GLN A CG    1 
ATOM   998   C  CD    . GLN A 1 122 ? 7.229   7.23    9.855   1 36.83 ? 122 GLN A CD    1 
ATOM   999   O  OE1   . GLN A 1 122 ? 7.549   8.422   9.864   1 37.96 ? 122 GLN A OE1   1 
ATOM   1000  N  NE2   . GLN A 1 122 ? 8.108   6.248   9.667   1 37.99 ? 122 GLN A NE2   1 
ATOM   1001  N  N     . ARG A 1 123 ? 3.615   3.979   11.206  1 28.3  ? 123 ARG A N     1 
ATOM   1002  C  CA    . ARG A 1 123 ? 3.178   2.829   10.425  1 28.72 ? 123 ARG A CA    1 
ATOM   1003  C  C     . ARG A 1 123 ? 1.937   2.161   11.013  1 29.18 ? 123 ARG A C     1 
ATOM   1004  O  O     . ARG A 1 123 ? 1.787   0.945   10.905  1 29.69 ? 123 ARG A O     1 
ATOM   1005  C  CB    . ARG A 1 123 ? 4.316   1.817   10.162  1 29.49 ? 123 ARG A CB    1 
ATOM   1006  C  CG    . ARG A 1 123 ? 5.372   1.694   11.267  1 31.81 ? 123 ARG A CG    1 
ATOM   1007  C  CD    . ARG A 1 123 ? 6.578   2.666   11.179  1 34.36 ? 123 ARG A CD    1 
ATOM   1008  N  NE    . ARG A 1 123 ? 7.608   1.904   10.53   1 36.06 ? 123 ARG A NE    1 
ATOM   1009  C  CZ    . ARG A 1 123 ? 8.903   2.143   10.393  1 37.63 ? 123 ARG A CZ    1 
ATOM   1010  N  NH1   . ARG A 1 123 ? 9.426   3.286   10.813  1 36.46 ? 123 ARG A NH1   1 
ATOM   1011  N  NH2   . ARG A 1 123 ? 9.679   1.25    9.789   1 37.92 ? 123 ARG A NH2   1 
ATOM   1012  N  N     . SER A 1 124 ? 1.047   2.953   11.621  1 28.89 ? 124 SER A N     1 
ATOM   1013  C  CA    . SER A 1 124 ? -0.223  2.422   12.104  1 29.33 ? 124 SER A CA    1 
ATOM   1014  C  C     . SER A 1 124 ? -1.232  2.251   10.942  1 29.52 ? 124 SER A C     1 
ATOM   1015  O  O     . SER A 1 124 ? -2.159  1.461   11.061  1 29.63 ? 124 SER A O     1 
ATOM   1016  C  CB    . SER A 1 124 ? -0.808  3.29    13.212  1 30.77 ? 124 SER A CB    1 
ATOM   1017  O  OG    . SER A 1 124 ? -0.183  2.995   14.451  1 33.08 ? 124 SER A OG    1 
ATOM   1018  N  N     . GLY A 1 125 ? -1.026  2.95    9.826   1 29.46 ? 125 GLY A N     1 
ATOM   1019  C  CA    . GLY A 1 125 ? -1.879  2.832   8.656   1 30.12 ? 125 GLY A CA    1 
ATOM   1020  C  C     . GLY A 1 125 ? -1.895  1.425   8.098   1 30.58 ? 125 GLY A C     1 
ATOM   1021  O  O     . GLY A 1 125 ? -2.961  0.92    7.74    1 30.78 ? 125 GLY A O     1 
ATOM   1022  N  N     . ARG A 1 126 ? -0.718  0.765   8.054   1 30.51 ? 126 ARG A N     1 
ATOM   1023  C  CA    . ARG A 1 126 ? -0.676  -0.607  7.559   1 30.99 ? 126 ARG A CA    1 
ATOM   1024  C  C     . ARG A 1 126 ? -1.349  -1.533  8.525   1 31.44 ? 126 ARG A C     1 
ATOM   1025  O  O     . ARG A 1 126 ? -2.076  -2.402  8.083   1 31.76 ? 126 ARG A O     1 
ATOM   1026  C  CB    . ARG A 1 126 ? 0.724   -1.096  7.15    1 32.13 ? 126 ARG A CB    1 
ATOM   1027  C  CG    . ARG A 1 126 ? 1.836   -0.765  8.114   1 34.5  ? 126 ARG A CG    1 
ATOM   1028  C  CD    . ARG A 1 126 ? 3.179   -0.851  7.42    1 36.57 ? 126 ARG A CD    1 
ATOM   1029  N  NE    . ARG A 1 126 ? 3.373   0.319   6.568   1 38.12 ? 126 ARG A NE    1 
ATOM   1030  C  CZ    . ARG A 1 126 ? 4.492   1.028   6.506   1 39.7  ? 126 ARG A CZ    1 
ATOM   1031  N  NH1   . ARG A 1 126 ? 5.562   0.653   7.194   1 39.35 ? 126 ARG A NH1   1 
ATOM   1032  N  NH2   . ARG A 1 126 ? 4.562   2.097   5.728   1 39.58 ? 126 ARG A NH2   1 
ATOM   1033  N  N     . ALA A 1 127 ? -1.192  -1.316  9.835   1 31.46 ? 127 ALA A N     1 
ATOM   1034  C  CA    . ALA A 1 127 ? -1.859  -2.146  10.831  1 32.22 ? 127 ALA A CA    1 
ATOM   1035  C  C     . ALA A 1 127 ? -3.38   -2.01   10.716  1 32.5  ? 127 ALA A C     1 
ATOM   1036  O  O     . ALA A 1 127 ? -4.094  -3.008  10.776  1 32.73 ? 127 ALA A O     1 
ATOM   1037  C  CB    . ALA A 1 127 ? -1.397  -1.755  12.228  1 32.59 ? 127 ALA A CB    1 
ATOM   1038  N  N     . TYR A 1 128 ? -3.867  -0.784  10.51   1 32.22 ? 128 TYR A N     1 
ATOM   1039  C  CA    . TYR A 1 128 ? -5.294  -0.544  10.376  1 32.33 ? 128 TYR A CA    1 
ATOM   1040  C  C     . TYR A 1 128 ? -5.852  -1.174  9.085   1 32.11 ? 128 TYR A C     1 
ATOM   1041  O  O     . TYR A 1 128 ? -6.825  -1.927  9.141   1 32.32 ? 128 TYR A O     1 
ATOM   1042  C  CB    . TYR A 1 128 ? -5.602  0.968   10.445  1 32.43 ? 128 TYR A CB    1 
ATOM   1043  C  CG    . TYR A 1 128 ? -6.985  1.299   9.931   1 33.29 ? 128 TYR A CG    1 
ATOM   1044  C  CD1   . TYR A 1 128 ? -8.116  0.956   10.656  1 34.16 ? 128 TYR A CD1   1 
ATOM   1045  C  CD2   . TYR A 1 128 ? -7.165  1.845   8.668   1 34.31 ? 128 TYR A CD2   1 
ATOM   1046  C  CE1   . TYR A 1 128 ? -9.39   1.182   10.155  1 35.09 ? 128 TYR A CE1   1 
ATOM   1047  C  CE2   . TYR A 1 128 ? -8.433  2.056   8.148   1 35.27 ? 128 TYR A CE2   1 
ATOM   1048  C  CZ    . TYR A 1 128 ? -9.545  1.732   8.899   1 36.12 ? 128 TYR A CZ    1 
ATOM   1049  O  OH    . TYR A 1 128 ? -10.801 1.969   8.397   1 37.67 ? 128 TYR A OH    1 
ATOM   1050  N  N     . SER A 1 129 ? -5.265  -0.82   7.93    1 31.35 ? 129 SER A N     1 
ATOM   1051  C  CA    . SER A 1 129 ? -5.737  -1.267  6.632   1 31.01 ? 129 SER A CA    1 
ATOM   1052  C  C     . SER A 1 129 ? -5.642  -2.764  6.46    1 30.84 ? 129 SER A C     1 
ATOM   1053  O  O     . SER A 1 129 ? -6.615  -3.376  6.042   1 31.1  ? 129 SER A O     1 
ATOM   1054  C  CB    . SER A 1 129 ? -5.013  -0.531  5.513   1 32.01 ? 129 SER A CB    1 
ATOM   1055  O  OG    . SER A 1 129 ? -3.611  -0.738  5.557   1 33.92 ? 129 SER A OG    1 
ATOM   1056  N  N     . VAL A 1 130 ? -4.494  -3.366  6.804   1 30.29 ? 130 VAL A N     1 
ATOM   1057  C  CA    . VAL A 1 130 ? -4.33   -4.814  6.706   1 30.16 ? 130 VAL A CA    1 
ATOM   1058  C  C     . VAL A 1 130 ? -5.199  -5.521  7.753   1 30.12 ? 130 VAL A C     1 
ATOM   1059  O  O     . VAL A 1 130 ? -5.821  -6.532  7.449   1 30.38 ? 130 VAL A O     1 
ATOM   1060  C  CB    . VAL A 1 130 ? -2.844  -5.245  6.781   1 30.75 ? 130 VAL A CB    1 
ATOM   1061  C  CG1   . VAL A 1 130 ? -2.707  -6.758  6.795   1 31.44 ? 130 VAL A CG1   1 
ATOM   1062  C  CG2   . VAL A 1 130 ? -2.045  -4.652  5.633   1 31.15 ? 130 VAL A CG2   1 
ATOM   1063  N  N     . GLY A 1 131 ? -5.29   -4.95   8.947   1 29.65 ? 131 GLY A N     1 
ATOM   1064  C  CA    . GLY A 1 131 ? -6.108  -5.503  10.018  1 29.73 ? 131 GLY A CA    1 
ATOM   1065  C  C     . GLY A 1 131 ? -7.586  -5.65   9.701   1 29.52 ? 131 GLY A C     1 
ATOM   1066  O  O     . GLY A 1 131 ? -8.213  -6.6    10.162  1 29.66 ? 131 GLY A O     1 
ATOM   1067  N  N     . ARG A 1 132 ? -8.16   -4.744  8.888   1 29.01 ? 132 ARG A N     1 
ATOM   1068  C  CA    . ARG A 1 132 ? -9.582  -4.837  8.533   1 28.72 ? 132 ARG A CA    1 
ATOM   1069  C  C     . ARG A 1 132 ? -9.878  -5.857  7.399   1 28.95 ? 132 ARG A C     1 
ATOM   1070  O  O     . ARG A 1 132 ? -11.039 -6.035  7.031   1 29.21 ? 132 ARG A O     1 
ATOM   1071  C  CB    . ARG A 1 132 ? -10.174 -3.45   8.213   1 28.8  ? 132 ARG A CB    1 
ATOM   1072  C  CG    . ARG A 1 132 ? -9.774  -2.891  6.853   1 29.13 ? 132 ARG A CG    1 
ATOM   1073  C  CD    . ARG A 1 132 ? -10.088 -1.412  6.708   1 29.21 ? 132 ARG A CD    1 
ATOM   1074  N  NE    . ARG A 1 132 ? -11.508 -1.102  6.896   1 28.75 ? 132 ARG A NE    1 
ATOM   1075  C  CZ    . ARG A 1 132 ? -12.425 -1.156  5.935   1 27.9  ? 132 ARG A CZ    1 
ATOM   1076  N  NH1   . ARG A 1 132 ? -13.686 -0.846  6.196   1 26.97 ? 132 ARG A NH1   1 
ATOM   1077  N  NH2   . ARG A 1 132 ? -12.089 -1.529  4.709   1 26.22 ? 132 ARG A NH2   1 
ATOM   1078  N  N     . THR A 1 133 ? -8.85   -6.546  6.872   1 28.64 ? 133 THR A N     1 
ATOM   1079  C  CA    . THR A 1 133 ? -9.021  -7.533  5.802   1 28.8  ? 133 THR A CA    1 
ATOM   1080  C  C     . THR A 1 133 ? -9.33   -8.954  6.285   1 29.6  ? 133 THR A C     1 
ATOM   1081  O  O     . THR A 1 133 ? -9.78   -9.784  5.493   1 29.94 ? 133 THR A O     1 
ATOM   1082  C  CB    . THR A 1 133 ? -7.747  -7.612  4.954   1 29.35 ? 133 THR A CB    1 
ATOM   1083  O  OG1   . THR A 1 133 ? -6.66   -8.086  5.746   1 29.86 ? 133 THR A OG1   1 
ATOM   1084  C  CG2   . THR A 1 133 ? -7.379  -6.301  4.349   1 29.83 ? 133 THR A CG2   1 
ATOM   1085  N  N     . GLY A 1 134 ? -9.012  -9.252  7.538   1 29.52 ? 134 GLY A N     1 
ATOM   1086  C  CA    . GLY A 1 134 ? -9.15   -10.608 8.052   1 29.79 ? 134 GLY A CA    1 
ATOM   1087  C  C     . GLY A 1 134 ? -7.843  -11.387 8.004   1 29.67 ? 134 GLY A C     1 
ATOM   1088  O  O     . GLY A 1 134 ? -7.753  -12.472 8.579   1 29.84 ? 134 GLY A O     1 
ATOM   1089  N  N     . TYR A 1 135 ? -6.806  -10.839 7.341   1 29.21 ? 135 TYR A N     1 
ATOM   1090  C  CA    . TYR A 1 135 ? -5.487  -11.455 7.281   1 29.34 ? 135 TYR A CA    1 
ATOM   1091  C  C     . TYR A 1 135 ? -4.67   -10.945 8.47    1 29.13 ? 135 TYR A C     1 
ATOM   1092  O  O     . TYR A 1 135 ? -4.652  -9.75   8.747   1 29.06 ? 135 TYR A O     1 
ATOM   1093  C  CB    . TYR A 1 135 ? -4.775  -11.117 5.965   1 29.54 ? 135 TYR A CB    1 
ATOM   1094  C  CG    . TYR A 1 135 ? -5.475  -11.652 4.736   1 30.63 ? 135 TYR A CG    1 
ATOM   1095  C  CD1   . TYR A 1 135 ? -5.701  -13.011 4.577   1 31.75 ? 135 TYR A CD1   1 
ATOM   1096  C  CD2   . TYR A 1 135 ? -5.862  -10.803 3.708   1 31.72 ? 135 TYR A CD2   1 
ATOM   1097  C  CE1   . TYR A 1 135 ? -6.337  -13.509 3.448   1 32.81 ? 135 TYR A CE1   1 
ATOM   1098  C  CE2   . TYR A 1 135 ? -6.486  -11.29  2.567   1 32.76 ? 135 TYR A CE2   1 
ATOM   1099  C  CZ    . TYR A 1 135 ? -6.724  -12.645 2.441   1 33.89 ? 135 TYR A CZ    1 
ATOM   1100  O  OH    . TYR A 1 135 ? -7.341  -13.133 1.316   1 35.75 ? 135 TYR A OH    1 
ATOM   1101  N  N     . PRO A 1 136 ? -4.006  -11.845 9.197   1 28.81 ? 136 PRO A N     1 
ATOM   1102  C  CA    . PRO A 1 136 ? -3.257  -11.424 10.39   1 28.65 ? 136 PRO A CA    1 
ATOM   1103  C  C     . PRO A 1 136 ? -2.139  -10.437 10.142  1 28.23 ? 136 PRO A C     1 
ATOM   1104  O  O     . PRO A 1 136 ? -1.469  -10.483 9.123   1 28.05 ? 136 PRO A O     1 
ATOM   1105  C  CB    . PRO A 1 136 ? -2.708  -12.734 10.943  1 29.63 ? 136 PRO A CB    1 
ATOM   1106  C  CG    . PRO A 1 136 ? -3.587  -13.788 10.373  1 30.09 ? 136 PRO A CG    1 
ATOM   1107  C  CD    . PRO A 1 136 ? -3.964  -13.305 9.019   1 28.28 ? 136 PRO A CD    1 
ATOM   1108  N  N     . TYR A 1 137 ? -1.931  -9.556  11.104  1 28.23 ? 137 TYR A N     1 
ATOM   1109  C  CA    . TYR A 1 137 ? -0.914  -8.522  11.015  1 28.68 ? 137 TYR A CA    1 
ATOM   1110  C  C     . TYR A 1 137 ? -0.007  -8.574  12.25   1 28.92 ? 137 TYR A C     1 
ATOM   1111  O  O     . TYR A 1 137 ? -0.483  -8.427  13.373  1 28.85 ? 137 TYR A O     1 
ATOM   1112  C  CB    . TYR A 1 137 ? -1.58   -7.142  10.871  1 28.51 ? 137 TYR A CB    1 
ATOM   1113  C  CG    . TYR A 1 137 ? -0.578  -6.045  10.637  1 29.13 ? 137 TYR A CG    1 
ATOM   1114  C  CD1   . TYR A 1 137 ? -0.146  -5.736  9.359   1 30.24 ? 137 TYR A CD1   1 
ATOM   1115  C  CD2   . TYR A 1 137 ? -0.02   -5.35   11.698  1 30.14 ? 137 TYR A CD2   1 
ATOM   1116  C  CE1   . TYR A 1 137 ? 0.807   -4.753  9.138   1 31.24 ? 137 TYR A CE1   1 
ATOM   1117  C  CE2   . TYR A 1 137 ? 0.948   -4.379  11.494  1 31.21 ? 137 TYR A CE2   1 
ATOM   1118  C  CZ    . TYR A 1 137 ? 1.345   -4.068  10.208  1 32.18 ? 137 TYR A CZ    1 
ATOM   1119  O  OH    . TYR A 1 137 ? 2.299   -3.107  9.997   1 33.71 ? 137 TYR A OH    1 
ATOM   1120  N  N     . ILE A 1 138 ? 1.298   -8.785  12.038  1 28.86 ? 138 ILE A N     1 
ATOM   1121  C  CA    . ILE A 1 138 ? 2.269   -8.903  13.125  1 29.02 ? 138 ILE A CA    1 
ATOM   1122  C  C     . ILE A 1 138 ? 3.297   -7.78   13.05   1 29.1  ? 138 ILE A C     1 
ATOM   1123  O  O     . ILE A 1 138 ? 4.035   -7.681  12.076  1 28.97 ? 138 ILE A O     1 
ATOM   1124  C  CB    . ILE A 1 138 ? 2.976   -10.281 13.078  1 29.47 ? 138 ILE A CB    1 
ATOM   1125  C  CG1   . ILE A 1 138 ? 1.992   -11.452 12.878  1 30.17 ? 138 ILE A CG1   1 
ATOM   1126  C  CG2   . ILE A 1 138 ? 3.844   -10.479 14.301  1 30.03 ? 138 ILE A CG2   1 
ATOM   1127  C  CD1   . ILE A 1 138 ? 0.962   -11.57  13.901  1 31.17 ? 138 ILE A CD1   1 
ATOM   1128  N  N     . TYR A 1 139 ? 3.363   -6.951  14.08   1 29.24 ? 139 TYR A N     1 
ATOM   1129  C  CA    . TYR A 1 139 ? 4.301   -5.836  14.122  1 29.81 ? 139 TYR A CA    1 
ATOM   1130  C  C     . TYR A 1 139 ? 5.393   -6.156  15.13   1 29.89 ? 139 TYR A C     1 
ATOM   1131  O  O     . TYR A 1 139 ? 5.145   -6.114  16.327  1 29.81 ? 139 TYR A O     1 
ATOM   1132  C  CB    . TYR A 1 139 ? 3.542   -4.571  14.517  1 30.2  ? 139 TYR A CB    1 
ATOM   1133  C  CG    . TYR A 1 139 ? 4.354   -3.295  14.514  1 31.51 ? 139 TYR A CG    1 
ATOM   1134  C  CD1   . TYR A 1 139 ? 5.261   -3.024  13.499  1 32.58 ? 139 TYR A CD1   1 
ATOM   1135  C  CD2   . TYR A 1 139 ? 4.154   -2.322  15.479  1 32.54 ? 139 TYR A CD2   1 
ATOM   1136  C  CE1   . TYR A 1 139 ? 5.974   -1.833  13.468  1 33.5  ? 139 TYR A CE1   1 
ATOM   1137  C  CE2   . TYR A 1 139 ? 4.865   -1.133  15.464  1 33.58 ? 139 TYR A CE2   1 
ATOM   1138  C  CZ    . TYR A 1 139 ? 5.78    -0.891  14.461  1 34.56 ? 139 TYR A CZ    1 
ATOM   1139  O  OH    . TYR A 1 139 ? 6.482   0.291   14.476  1 36.2  ? 139 TYR A OH    1 
ATOM   1140  N  N     . ILE A 1 140 ? 6.591   -6.51   14.646  1 29.73 ? 140 ILE A N     1 
ATOM   1141  C  CA    . ILE A 1 140 ? 7.729   -6.885  15.485  1 29.82 ? 140 ILE A CA    1 
ATOM   1142  C  C     . ILE A 1 140 ? 8.63    -5.661  15.71   1 30.24 ? 140 ILE A C     1 
ATOM   1143  O  O     . ILE A 1 140 ? 9.145   -5.099  14.75   1 30.38 ? 140 ILE A O     1 
ATOM   1144  C  CB    . ILE A 1 140 ? 8.493   -8.054  14.811  1 29.94 ? 140 ILE A CB    1 
ATOM   1145  C  CG1   . ILE A 1 140 ? 7.557   -9.235  14.481  1 30.34 ? 140 ILE A CG1   1 
ATOM   1146  C  CG2   . ILE A 1 140 ? 9.661   -8.504  15.661  1 30.45 ? 140 ILE A CG2   1 
ATOM   1147  C  CD1   . ILE A 1 140 ? 8.145   -10.234 13.567  1 31    ? 140 ILE A CD1   1 
ATOM   1148  N  N     . VAL A 1 141 ? 8.803   -5.238  16.973  1 30.13 ? 141 VAL A N     1 
ATOM   1149  C  CA    . VAL A 1 141 ? 9.594   -4.05   17.309  1 30.39 ? 141 VAL A CA    1 
ATOM   1150  C  C     . VAL A 1 141 ? 10.664  -4.35   18.377  1 31.05 ? 141 VAL A C     1 
ATOM   1151  O  O     . VAL A 1 141 ? 10.364  -4.959  19.401  1 31.09 ? 141 VAL A O     1 
ATOM   1152  C  CB    . VAL A 1 141 ? 8.688   -2.832  17.683  1 30.55 ? 141 VAL A CB    1 
ATOM   1153  C  CG1   . VAL A 1 141 ? 7.527   -3.229  18.584  1 30.9  ? 141 VAL A CG1   1 
ATOM   1154  C  CG2   . VAL A 1 141 ? 9.484   -1.694  18.305  1 30.79 ? 141 VAL A CG2   1 
ATOM   1155  N  N     . ASP A 1 142 ? 11.912  -3.922  18.116  1 31.46 ? 142 ASP A N     1 
ATOM   1156  C  CA    . ASP A 1 142 ? 13.076  -4.087  18.987  1 32.32 ? 142 ASP A CA    1 
ATOM   1157  C  C     . ASP A 1 142 ? 12.923  -3.264  20.259  1 32.72 ? 142 ASP A C     1 
ATOM   1158  O  O     . ASP A 1 142 ? 12.75   -2.05   20.175  1 32.7  ? 142 ASP A O     1 
ATOM   1159  C  CB    . ASP A 1 142 ? 14.323  -3.574  18.25   1 34.39 ? 142 ASP A CB    1 
ATOM   1160  C  CG    . ASP A 1 142 ? 15.534  -4.482  18.309  1 39.45 ? 142 ASP A CG    1 
ATOM   1161  O  OD1   . ASP A 1 142 ? 15.396  -5.686  17.973  1 40.08 ? 142 ASP A OD1   1 
ATOM   1162  O  OD2   . ASP A 1 142 ? 16.63   -3.984  18.653  1 41.82 ? 142 ASP A OD2   1 
ATOM   1163  N  N     . PHE A 1 143 ? 13.032  -3.905  21.427  1 32.87 ? 143 PHE A N     1 
ATOM   1164  C  CA    . PHE A 1 143 ? 12.94   -3.226  22.718  1 33.51 ? 143 PHE A CA    1 
ATOM   1165  C  C     . PHE A 1 143 ? 14.241  -3.54   23.464  1 34.77 ? 143 PHE A C     1 
ATOM   1166  O  O     . PHE A 1 143 ? 14.433  -4.698  23.824  1 35.06 ? 143 PHE A O     1 
ATOM   1167  C  CB    . PHE A 1 143 ? 11.724  -3.775  23.504  1 33.05 ? 143 PHE A CB    1 
ATOM   1168  C  CG    . PHE A 1 143 ? 11.445  -3.086  24.818  1 33.28 ? 143 PHE A CG    1 
ATOM   1169  C  CD1   . PHE A 1 143 ? 12.091  -3.477  25.977  1 33.87 ? 143 PHE A CD1   1 
ATOM   1170  C  CD2   . PHE A 1 143 ? 10.537  -2.048  24.894  1 33.84 ? 143 PHE A CD2   1 
ATOM   1171  C  CE1   . PHE A 1 143 ? 11.869  -2.807  27.171  1 34.39 ? 143 PHE A CE1   1 
ATOM   1172  C  CE2   . PHE A 1 143 ? 10.3    -1.398  26.097  1 34.25 ? 143 PHE A CE2   1 
ATOM   1173  C  CZ    . PHE A 1 143 ? 10.966  -1.782  27.226  1 33.99 ? 143 PHE A CZ    1 
ATOM   1174  N  N     . VAL A 1 144 ? 15.166  -2.584  23.67   1 35.48 ? 144 VAL A N     1 
ATOM   1175  C  CA    . VAL A 1 144 ? 15.124  -1.167  23.31   1 36.82 ? 144 VAL A CA    1 
ATOM   1176  C  C     . VAL A 1 144 ? 16.4    -0.769  22.526  1 38.48 ? 144 VAL A C     1 
ATOM   1177  O  O     . VAL A 1 144 ? 17.384  -1.509  22.511  1 38.58 ? 144 VAL A O     1 
ATOM   1178  C  CB    . VAL A 1 144 ? 15.057  -0.299  24.595  1 37.49 ? 144 VAL A CB    1 
ATOM   1179  C  CG1   . VAL A 1 144 ? 13.686  -0.329  25.243  1 38.12 ? 144 VAL A CG1   1 
ATOM   1180  C  CG2   . VAL A 1 144 ? 16.166  -0.671  25.577  1 37.97 ? 144 VAL A CG2   1 
ATOM   1181  N  N     . LYS A 1 145 ? 16.392  0.431   21.921  1 39.7  ? 145 LYS A N     1 
ATOM   1182  C  CA    . LYS A 1 145 ? 17.532  1.031   21.245  1 41.43 ? 145 LYS A CA    1 
ATOM   1183  C  C     . LYS A 1 145 ? 17.667  2.477   21.769  1 43.02 ? 145 LYS A C     1 
ATOM   1184  O  O     . LYS A 1 145 ? 16.657  3.151   22.003  1 42.97 ? 145 LYS A O     1 
ATOM   1185  C  CB    . LYS A 1 145 ? 17.34   1.007   19.719  1 43.53 ? 145 LYS A CB    1 
ATOM   1186  C  CG    . LYS A 1 145 ? 18.589  1.42    18.938  1 47.57 ? 145 LYS A CG    1 
ATOM   1187  C  CD    . LYS A 1 145 ? 18.506  1.067   17.454  1 51.71 ? 145 LYS A CD    1 
ATOM   1188  C  CE    . LYS A 1 145 ? 17.5    1.931   16.705  1 55.14 ? 145 LYS A CE    1 
ATOM   1189  N  NZ    . LYS A 1 145 ? 17.847  3.372   16.757  1 57.28 ? 145 LYS A NZ    1 
ATOM   1190  N  N     . TYR A 1 146 ? 18.899  2.932   22.012  1 44.41 ? 146 TYR A N     1 
ATOM   1191  C  CA    . TYR A 1 146 ? 19.131  4.282   22.516  1 46.53 ? 146 TYR A CA    1 
ATOM   1192  C  C     . TYR A 1 146 ? 19.272  5.305   21.4    1 48.7  ? 146 TYR A C     1 
ATOM   1193  O  O     . TYR A 1 146 ? 19.768  4.988   20.322  1 49.11 ? 146 TYR A O     1 
ATOM   1194  C  CB    . TYR A 1 146 ? 20.421  4.328   23.345  1 46.69 ? 146 TYR A CB    1 
ATOM   1195  C  CG    . TYR A 1 146 ? 20.279  3.775   24.739  1 47.64 ? 146 TYR A CG    1 
ATOM   1196  C  CD1   . TYR A 1 146 ? 20.365  2.412   24.977  1 48.73 ? 146 TYR A CD1   1 
ATOM   1197  C  CD2   . TYR A 1 146 ? 20.121  4.617   25.829  1 48.46 ? 146 TYR A CD2   1 
ATOM   1198  C  CE1   . TYR A 1 146 ? 20.256  1.896   26.26   1 49.65 ? 146 TYR A CE1   1 
ATOM   1199  C  CE2   . TYR A 1 146 ? 20.018  4.115   27.118  1 49.41 ? 146 TYR A CE2   1 
ATOM   1200  C  CZ    . TYR A 1 146 ? 20.091  2.752   27.329  1 50.48 ? 146 TYR A CZ    1 
ATOM   1201  O  OH    . TYR A 1 146 ? 19.996  2.243   28.594  1 52.13 ? 146 TYR A OH    1 
ATOM   1202  N  N     . GLU A 1 147 ? 18.9    6.553   21.682  1 49.92 ? 147 GLU A N     1 
ATOM   1203  C  CA    . GLU A 1 147 ? 19.121  7.648   20.744  1 51.51 ? 147 GLU A CA    1 
ATOM   1204  C  C     . GLU A 1 147 ? 20.54   8.158   21.012  1 52.72 ? 147 GLU A C     1 
ATOM   1205  O  O     . GLU A 1 147 ? 20.97   8.203   22.169  1 52.9  ? 147 GLU A O     1 
ATOM   1206  C  CB    . GLU A 1 147 ? 18.126  8.805   20.982  1 54    ? 147 GLU A CB    1 
ATOM   1207  C  CG    . GLU A 1 147 ? 18.214  9.883   19.908  1 58.51 ? 147 GLU A CG    1 
ATOM   1208  C  CD    . GLU A 1 147 ? 17.937  11.302  20.368  1 64.01 ? 147 GLU A CD    1 
ATOM   1209  O  OE1   . GLU A 1 147 ? 18.17   12.239  19.569  1 64.42 ? 147 GLU A OE1   1 
ATOM   1210  O  OE2   . GLU A 1 147 ? 17.484  11.477  21.525  1 66.08 ? 147 GLU A OE2   1 
ATOM   1211  N  N     . LEU A 1 148 ? 21.263  8.551   19.966  1 53.37 ? 148 LEU A N     1 
ATOM   1212  C  CA    . LEU A 1 148 ? 22.612  9.088   20.137  1 54.63 ? 148 LEU A CA    1 
ATOM   1213  C  C     . LEU A 1 148 ? 22.633  10.591  19.849  1 55.85 ? 148 LEU A C     1 
ATOM   1214  O  O     . LEU A 1 148 ? 21.759  11.097  19.135  1 56.15 ? 148 LEU A O     1 
ATOM   1215  C  CB    . LEU A 1 148 ? 23.625  8.325   19.284  1 54.97 ? 148 LEU A CB    1 
ATOM   1216  C  CG    . LEU A 1 148 ? 23.605  6.809   19.48   1 56.64 ? 148 LEU A CG    1 
ATOM   1217  C  CD1   . LEU A 1 148 ? 24.475  6.114   18.466  1 57.29 ? 148 LEU A CD1   1 
ATOM   1218  C  CD2   . LEU A 1 148 ? 24.011  6.429   20.882  1 57.27 ? 148 LEU A CD2   1 
ATOM   1219  N  N     . ASN A 1 149 ? 23.604  11.311  20.419  1 56.41 ? 149 ASN A N     1 
ATOM   1220  C  CA    . ASN A 1 149 ? 23.652  12.76   20.24   1 57.57 ? 149 ASN A CA    1 
ATOM   1221  C  C     . ASN A 1 149 ? 24.255  13.224  18.905  1 58.31 ? 149 ASN A C     1 
ATOM   1222  O  O     . ASN A 1 149 ? 24.144  14.407  18.576  1 58.61 ? 149 ASN A O     1 
ATOM   1223  C  CB    . ASN A 1 149 ? 24.356  13.427  21.414  1 59.05 ? 149 ASN A CB    1 
ATOM   1224  C  CG    . ASN A 1 149 ? 25.809  13.072  21.532  1 62.55 ? 149 ASN A CG    1 
ATOM   1225  O  OD1   . ASN A 1 149 ? 26.315  12.152  20.874  1 63.47 ? 149 ASN A OD1   1 
ATOM   1226  N  ND2   . ASN A 1 149 ? 26.511  13.783  22.403  1 63.48 ? 149 ASN A ND2   1 
ATOM   1227  N  N     . ASN A 1 150 ? 24.92   12.309  18.169  1 58.33 ? 150 ASN A N     1 
ATOM   1228  C  CA    . ASN A 1 150 ? 25.602  12.505  16.883  1 58.8  ? 150 ASN A CA    1 
ATOM   1229  C  C     . ASN A 1 150 ? 26.881  13.367  16.979  1 58.79 ? 150 ASN A C     1 
ATOM   1230  O  O     . ASN A 1 150 ? 27.815  13.109  16.224  1 58.91 ? 150 ASN A O     1 
ATOM   1231  C  CB    . ASN A 1 150 ? 24.676  12.998  15.768  1 60.26 ? 150 ASN A CB    1 
ATOM   1232  C  CG    . ASN A 1 150 ? 24.323  11.905  14.784  1 63.78 ? 150 ASN A CG    1 
ATOM   1233  O  OD1   . ASN A 1 150 ? 23.868  10.81   15.161  1 65.15 ? 150 ASN A OD1   1 
ATOM   1234  N  ND2   . ASN A 1 150 ? 24.505  12.184  13.5    1 64.34 ? 150 ASN A ND2   1 
ATOM   1235  N  N     . SER A 1 151 ? 26.957  14.34   17.907  1 58.48 ? 151 SER A N     1 
ATOM   1236  C  CA    . SER A 1 151 ? 28.162  15.153  18.068  1 58.75 ? 151 SER A CA    1 
ATOM   1237  C  C     . SER A 1 151 ? 29.332  14.282  18.533  1 58.77 ? 151 SER A C     1 
ATOM   1238  O  O     . SER A 1 151 ? 30.429  14.397  17.996  1 58.9  ? 151 SER A O     1 
ATOM   1239  C  CB    . SER A 1 151 ? 27.918  16.295  19.048  1 60.25 ? 151 SER A CB    1 
ATOM   1240  O  OG    . SER A 1 151 ? 27.684  15.815  20.363  1 62.65 ? 151 SER A OG    1 
ATOM   1241  N  N     . ASP A 1 152 ? 29.092  13.381  19.495  1 58.57 ? 152 ASP A N     1 
ATOM   1242  C  CA    . ASP A 1 152 ? 30.137  12.465  19.96   1 58.87 ? 152 ASP A CA    1 
ATOM   1243  C  C     . ASP A 1 152 ? 29.65   11.008  20.136  1 58.64 ? 152 ASP A C     1 
ATOM   1244  O  O     . ASP A 1 152 ? 30.329  10.207  20.777  1 58.8  ? 152 ASP A O     1 
ATOM   1245  C  CB    . ASP A 1 152 ? 30.82   12.988  21.232  1 60.81 ? 152 ASP A CB    1 
ATOM   1246  C  CG    . ASP A 1 152 ? 29.956  12.976  22.471  1 65.27 ? 152 ASP A CG    1 
ATOM   1247  O  OD1   . ASP A 1 152 ? 29.104  13.883  22.609  1 66.09 ? 152 ASP A OD1   1 
ATOM   1248  O  OD2   . ASP A 1 152 ? 30.154  12.081  23.32   1 67.17 ? 152 ASP A OD2   1 
ATOM   1249  N  N     . ARG A 1 153 ? 28.485  10.674  19.548  1 58.08 ? 153 ARG A N     1 
ATOM   1250  C  CA    . ARG A 1 153 ? 27.865  9.351   19.561  1 58.07 ? 153 ARG A CA    1 
ATOM   1251  C  C     . ARG A 1 153 ? 27.595  8.795   20.955  1 57.57 ? 153 ARG A C     1 
ATOM   1252  O  O     . ARG A 1 153 ? 27.601  7.577   21.14   1 57.73 ? 153 ARG A O     1 
ATOM   1253  C  CB    . ARG A 1 153 ? 28.671  8.349   18.723  1 59.71 ? 153 ARG A CB    1 
ATOM   1254  C  CG    . ARG A 1 153 ? 27.813  7.602   17.714  1 63.01 ? 153 ARG A CG    1 
ATOM   1255  C  CD    . ARG A 1 153 ? 28.622  6.618   16.898  1 65.84 ? 153 ARG A CD    1 
ATOM   1256  N  NE    . ARG A 1 153 ? 27.772  5.859   15.98   1 67.79 ? 153 ARG A NE    1 
ATOM   1257  C  CZ    . ARG A 1 153 ? 27.276  4.654   16.237  1 69.05 ? 153 ARG A CZ    1 
ATOM   1258  N  NH1   . ARG A 1 153 ? 27.546  4.049   17.386  1 68.36 ? 153 ARG A NH1   1 
ATOM   1259  N  NH2   . ARG A 1 153 ? 26.514  4.041   15.344  1 68.79 ? 153 ARG A NH2   1 
ATOM   1260  N  N     . SER A 1 154 ? 27.344  9.674   21.932  1 56.71 ? 154 SER A N     1 
ATOM   1261  C  CA    . SER A 1 154 ? 27.019  9.236   23.29   1 56.21 ? 154 SER A CA    1 
ATOM   1262  C  C     . SER A 1 154 ? 25.502  9.027   23.429  1 55.17 ? 154 SER A C     1 
ATOM   1263  O  O     . SER A 1 154 ? 24.724  9.587   22.659  1 55.35 ? 154 SER A O     1 
ATOM   1264  C  CB    . SER A 1 154 ? 27.519  10.24   24.323  1 57.68 ? 154 SER A CB    1 
ATOM   1265  O  OG    . SER A 1 154 ? 26.821  11.471  24.232  1 60.09 ? 154 SER A OG    1 
ATOM   1266  N  N     . ARG A 1 155 ? 25.08   8.227   24.408  1 54.05 ? 155 ARG A N     1 
ATOM   1267  C  CA    . ARG A 1 155 ? 23.663  7.927   24.6    1 53.39 ? 155 ARG A CA    1 
ATOM   1268  C  C     . ARG A 1 155 ? 22.829  8.983   25.313  1 52.07 ? 155 ARG A C     1 
ATOM   1269  O  O     . ARG A 1 155 ? 23.237  9.546   26.327  1 52.11 ? 155 ARG A O     1 
ATOM   1270  C  CB    . ARG A 1 155 ? 23.492  6.6     25.333  1 54.78 ? 155 ARG A CB    1 
ATOM   1271  C  CG    . ARG A 1 155 ? 23.888  5.413   24.497  1 57.78 ? 155 ARG A CG    1 
ATOM   1272  C  CD    . ARG A 1 155 ? 23.832  4.162   25.318  1 61.01 ? 155 ARG A CD    1 
ATOM   1273  N  NE    . ARG A 1 155 ? 24.34   3.02    24.566  1 64.25 ? 155 ARG A NE    1 
ATOM   1274  C  CZ    . ARG A 1 155 ? 25.611  2.627   24.563  1 67.1  ? 155 ARG A CZ    1 
ATOM   1275  N  NH1   . ARG A 1 155 ? 26.519  3.286   25.273  1 67.16 ? 155 ARG A NH1   1 
ATOM   1276  N  NH2   . ARG A 1 155 ? 25.984  1.57    23.853  1 67.26 ? 155 ARG A NH2   1 
ATOM   1277  N  N     . LYS A 1 156 ? 21.619  9.184   24.8    1 50.63 ? 156 LYS A N     1 
ATOM   1278  C  CA    . LYS A 1 156 ? 20.603  10.062  25.366  1 49.62 ? 156 LYS A CA    1 
ATOM   1279  C  C     . LYS A 1 156 ? 19.461  9.173   25.931  1 48    ? 156 LYS A C     1 
ATOM   1280  O  O     . LYS A 1 156 ? 19.492  7.951   25.763  1 47.94 ? 156 LYS A O     1 
ATOM   1281  C  CB    . LYS A 1 156 ? 20.1    11.053  24.301  1 51.66 ? 156 LYS A CB    1 
ATOM   1282  C  CG    . LYS A 1 156 ? 21.177  12.032  23.84   1 55.76 ? 156 LYS A CG    1 
ATOM   1283  C  CD    . LYS A 1 156 ? 20.903  12.568  22.44   1 60.17 ? 156 LYS A CD    1 
ATOM   1284  C  CE    . LYS A 1 156 ? 19.968  13.747  22.408  1 64.17 ? 156 LYS A CE    1 
ATOM   1285  N  NZ    . LYS A 1 156 ? 19.763  14.235  21.015  1 66.69 ? 156 LYS A NZ    1 
ATOM   1286  N  N     . ASN A 1 157 ? 18.474  9.768   26.614  1 46.5  ? 157 ASN A N     1 
ATOM   1287  C  CA    . ASN A 1 157 ? 17.396  9.001   27.241  1 45.41 ? 157 ASN A CA    1 
ATOM   1288  C  C     . ASN A 1 157 ? 16.665  8.026   26.313  1 43.23 ? 157 ASN A C     1 
ATOM   1289  O  O     . ASN A 1 157 ? 16.48   8.308   25.127  1 43.25 ? 157 ASN A O     1 
ATOM   1290  C  CB    . ASN A 1 157 ? 16.391  9.93    27.924  1 46.99 ? 157 ASN A CB    1 
ATOM   1291  C  CG    . ASN A 1 157 ? 16.992  10.792  29      1 50.57 ? 157 ASN A CG    1 
ATOM   1292  O  OD1   . ASN A 1 157 ? 17.192  12.001  28.819  1 51.92 ? 157 ASN A OD1   1 
ATOM   1293  N  ND2   . ASN A 1 157 ? 17.286  10.193  30.147  1 51.2  ? 157 ASN A ND2   1 
ATOM   1294  N  N     . LEU A 1 158 ? 16.271  6.867   26.866  1 41.21 ? 158 LEU A N     1 
ATOM   1295  C  CA    . LEU A 1 158 ? 15.527  5.846   26.132  1 39.79 ? 158 LEU A CA    1 
ATOM   1296  C  C     . LEU A 1 158 ? 14.18   6.396   25.685  1 38.24 ? 158 LEU A C     1 
ATOM   1297  O  O     . LEU A 1 158 ? 13.58   7.188   26.408  1 38.6  ? 158 LEU A O     1 
ATOM   1298  C  CB    . LEU A 1 158 ? 15.269  4.639   27.038  1 39.85 ? 158 LEU A CB    1 
ATOM   1299  C  CG    . LEU A 1 158 ? 16.364  3.591   27.124  1 41.24 ? 158 LEU A CG    1 
ATOM   1300  C  CD1   . LEU A 1 158 ? 15.939  2.455   28.03   1 41.6  ? 158 LEU A CD1   1 
ATOM   1301  C  CD2   . LEU A 1 158 ? 16.704  3.033   25.754  1 42.04 ? 158 LEU A CD2   1 
ATOM   1302  N  N     . ARG A 1 159 ? 13.687  5.967   24.523  1 36.49 ? 159 ARG A N     1 
ATOM   1303  C  CA    . ARG A 1 159 ? 12.39   6.43    24.04   1 35.24 ? 159 ARG A CA    1 
ATOM   1304  C  C     . ARG A 1 159 ? 11.38   5.297   24.024  1 34.3  ? 159 ARG A C     1 
ATOM   1305  O  O     . ARG A 1 159 ? 11.656  4.233   23.468  1 34.22 ? 159 ARG A O     1 
ATOM   1306  C  CB    . ARG A 1 159 ? 12.509  7.078   22.654  1 35.73 ? 159 ARG A CB    1 
ATOM   1307  C  CG    . ARG A 1 159 ? 13.358  8.347   22.626  1 37.1  ? 159 ARG A CG    1 
ATOM   1308  C  CD    . ARG A 1 159 ? 12.765  9.465   23.472  1 38.41 ? 159 ARG A CD    1 
ATOM   1309  N  NE    . ARG A 1 159 ? 11.718  10.237  22.789  1 38.74 ? 159 ARG A NE    1 
ATOM   1310  C  CZ    . ARG A 1 159 ? 10.411  10.065  22.97   1 39.15 ? 159 ARG A CZ    1 
ATOM   1311  N  NH1   . ARG A 1 159 ? 9.967   9.125   23.791  1 39.06 ? 159 ARG A NH1   1 
ATOM   1312  N  NH2   . ARG A 1 159 ? 9.54    10.822  22.32   1 38.03 ? 159 ARG A NH2   1 
ATOM   1313  N  N     . PHE A 1 160 ? 10.214  5.522   24.64   1 33.43 ? 160 PHE A N     1 
ATOM   1314  C  CA    . PHE A 1 160 ? 9.153   4.52    24.693  1 33.12 ? 160 PHE A CA    1 
ATOM   1315  C  C     . PHE A 1 160 ? 7.886   5.036   24.021  1 32.38 ? 160 PHE A C     1 
ATOM   1316  O  O     . PHE A 1 160 ? 7.595   6.231   24.095  1 32.58 ? 160 PHE A O     1 
ATOM   1317  C  CB    . PHE A 1 160 ? 8.826   4.147   26.15   1 33.14 ? 160 PHE A CB    1 
ATOM   1318  C  CG    . PHE A 1 160 ? 9.98    3.582   26.941  1 33.79 ? 160 PHE A CG    1 
ATOM   1319  C  CD1   . PHE A 1 160 ? 10.49   2.327   26.656  1 34.43 ? 160 PHE A CD1   1 
ATOM   1320  C  CD2   . PHE A 1 160 ? 10.538  4.294   27.988  1 34.64 ? 160 PHE A CD2   1 
ATOM   1321  C  CE1   . PHE A 1 160 ? 11.558  1.813   27.383  1 35.06 ? 160 PHE A CE1   1 
ATOM   1322  C  CE2   . PHE A 1 160 ? 11.595  3.771   28.721  1 35.27 ? 160 PHE A CE2   1 
ATOM   1323  C  CZ    . PHE A 1 160 ? 12.103  2.539   28.408  1 34.96 ? 160 PHE A CZ    1 
ATOM   1324  N  N     . PRO A 1 161 ? 7.087   4.145   23.402  1 31.37 ? 161 PRO A N     1 
ATOM   1325  C  CA    . PRO A 1 161 ? 5.823   4.598   22.808  1 31.27 ? 161 PRO A CA    1 
ATOM   1326  C  C     . PRO A 1 161 ? 4.777   4.967   23.864  1 31.6  ? 161 PRO A C     1 
ATOM   1327  O  O     . PRO A 1 161 ? 4.867   4.536   25.012  1 32.09 ? 161 PRO A O     1 
ATOM   1328  C  CB    . PRO A 1 161 ? 5.351   3.369   22.028  1 31.55 ? 161 PRO A CB    1 
ATOM   1329  C  CG    . PRO A 1 161 ? 5.911   2.228   22.769  1 31.67 ? 161 PRO A CG    1 
ATOM   1330  C  CD    . PRO A 1 161 ? 7.264   2.687   23.243  1 30.32 ? 161 PRO A CD    1 
ATOM   1331  N  N     . ASN A 1 162 ? 3.747   5.721   23.468  1 31.18 ? 162 ASN A N     1 
ATOM   1332  C  CA    . ASN A 1 162 ? 2.633   6.039   24.359  1 31.37 ? 162 ASN A CA    1 
ATOM   1333  C  C     . ASN A 1 162 ? 1.861   4.738   24.584  1 31.73 ? 162 ASN A C     1 
ATOM   1334  O  O     . ASN A 1 162 ? 1.689   3.974   23.636  1 31.86 ? 162 ASN A O     1 
ATOM   1335  C  CB    . ASN A 1 162 ? 1.706   7.039   23.683  1 32.26 ? 162 ASN A CB    1 
ATOM   1336  C  CG    . ASN A 1 162 ? 0.559   7.502   24.539  1 34.78 ? 162 ASN A CG    1 
ATOM   1337  O  OD1   . ASN A 1 162 ? -0.373  6.752   24.853  1 35.47 ? 162 ASN A OD1   1 
ATOM   1338  N  ND2   . ASN A 1 162 ? 0.597   8.763   24.928  1 35.4  ? 162 ASN A ND2   1 
ATOM   1339  N  N     . PRO A 1 163 ? 1.396   4.451   25.815  1 31.53 ? 163 PRO A N     1 
ATOM   1340  C  CA    . PRO A 1 163 ? 0.668   3.182   26.046  1 31.44 ? 163 PRO A CA    1 
ATOM   1341  C  C     . PRO A 1 163 ? -0.482  2.886   25.071  1 31.5  ? 163 PRO A C     1 
ATOM   1342  O  O     . PRO A 1 163 ? -0.801  1.73    24.821  1 31.45 ? 163 PRO A O     1 
ATOM   1343  C  CB    . PRO A 1 163 ? 0.159   3.317   27.483  1 32.14 ? 163 PRO A CB    1 
ATOM   1344  C  CG    . PRO A 1 163 ? 1.064   4.318   28.129  1 32.55 ? 163 PRO A CG    1 
ATOM   1345  C  CD    . PRO A 1 163 ? 1.545   5.244   27.054  1 30.91 ? 163 PRO A CD    1 
ATOM   1346  N  N     . ALA A 1 164 ? -1.088  3.93    24.5    1 31.59 ? 164 ALA A N     1 
ATOM   1347  C  CA    . ALA A 1 164 ? -2.186  3.784   23.551  1 31.96 ? 164 ALA A CA    1 
ATOM   1348  C  C     . ALA A 1 164 ? -1.772  3.136   22.244  1 32.07 ? 164 ALA A C     1 
ATOM   1349  O  O     . ALA A 1 164 ? -2.623  2.567   21.568  1 32.16 ? 164 ALA A O     1 
ATOM   1350  C  CB    . ALA A 1 164 ? -2.824  5.133   23.272  1 32.21 ? 164 ALA A CB    1 
ATOM   1351  N  N     . ILE A 1 165 ? -0.488  3.229   21.866  1 32.09 ? 165 ILE A N     1 
ATOM   1352  C  CA    . ILE A 1 165 ? -0.014  2.61    20.62   1 32.49 ? 165 ILE A CA    1 
ATOM   1353  C  C     . ILE A 1 165 ? -0.079  1.1     20.712  1 32.25 ? 165 ILE A C     1 
ATOM   1354  O  O     . ILE A 1 165 ? -0.872  0.513   19.984  1 32.15 ? 165 ILE A O     1 
ATOM   1355  C  CB    . ILE A 1 165 ? 1.366   3.101   20.138  1 33.19 ? 165 ILE A CB    1 
ATOM   1356  C  CG1   . ILE A 1 165 ? 1.527   4.62    20.302  1 34.51 ? 165 ILE A CG1   1 
ATOM   1357  C  CG2   . ILE A 1 165 ? 1.626   2.632   18.728  1 33.56 ? 165 ILE A CG2   1 
ATOM   1358  C  CD1   . ILE A 1 165 ? 0.452   5.441   19.692  1 35.95 ? 165 ILE A CD1   1 
ATOM   1359  N  N     . PRO A 1 166 ? 0.622   0.443   21.67   1 31.95 ? 166 PRO A N     1 
ATOM   1360  C  CA    . PRO A 1 166 ? 0.467   -1.014  21.806  1 31.67 ? 166 PRO A CA    1 
ATOM   1361  C  C     . PRO A 1 166 ? -0.987  -1.421  22.001  1 31.29 ? 166 PRO A C     1 
ATOM   1362  O  O     . PRO A 1 166 ? -1.409  -2.428  21.444  1 31.33 ? 166 PRO A O     1 
ATOM   1363  C  CB    . PRO A 1 166 ? 1.279   -1.34   23.066  1 32.38 ? 166 PRO A CB    1 
ATOM   1364  C  CG    . PRO A 1 166 ? 2.263   -0.248  23.187  1 32.93 ? 166 PRO A CG    1 
ATOM   1365  C  CD    . PRO A 1 166 ? 1.585   0.971   22.663  1 31.46 ? 166 PRO A CD    1 
ATOM   1366  N  N     . TYR A 1 167 ? -1.759  -0.612  22.751  1 30.77 ? 167 TYR A N     1 
ATOM   1367  C  CA    . TYR A 1 167 ? -3.152  -0.93   22.991  1 30.75 ? 167 TYR A CA    1 
ATOM   1368  C  C     . TYR A 1 167 ? -3.992  -0.903  21.735  1 29.96 ? 167 TYR A C     1 
ATOM   1369  O  O     . TYR A 1 167 ? -4.865  -1.755  21.585  1 30.06 ? 167 TYR A O     1 
ATOM   1370  C  CB    . TYR A 1 167 ? -3.788  -0.078  24.088  1 31.28 ? 167 TYR A CB    1 
ATOM   1371  C  CG    . TYR A 1 167 ? -5.094  -0.707  24.508  1 32.82 ? 167 TYR A CG    1 
ATOM   1372  C  CD1   . TYR A 1 167 ? -5.113  -1.883  25.249  1 34.09 ? 167 TYR A CD1   1 
ATOM   1373  C  CD2   . TYR A 1 167 ? -6.304  -0.233  24.016  1 33.94 ? 167 TYR A CD2   1 
ATOM   1374  C  CE1   . TYR A 1 167 ? -6.305  -2.526  25.556  1 35.14 ? 167 TYR A CE1   1 
ATOM   1375  C  CE2   . TYR A 1 167 ? -7.503  -0.864  24.319  1 35.13 ? 167 TYR A CE2   1 
ATOM   1376  C  CZ    . TYR A 1 167 ? -7.501  -2.012  25.092  1 36.11 ? 167 TYR A CZ    1 
ATOM   1377  O  OH    . TYR A 1 167 ? -8.686  -2.64   25.386  1 37.39 ? 167 TYR A OH    1 
ATOM   1378  N  N     . SER A 1 168 ? -3.712  0.017   20.808  1 29.04 ? 168 SER A N     1 
ATOM   1379  C  CA    . SER A 1 168 ? -4.477  0.112   19.57   1 28.93 ? 168 SER A CA    1 
ATOM   1380  C  C     . SER A 1 168 ? -4.537  -1.191  18.775  1 28.4  ? 168 SER A C     1 
ATOM   1381  O  O     . SER A 1 168 ? -5.545  -1.475  18.137  1 28.42 ? 168 SER A O     1 
ATOM   1382  C  CB    . SER A 1 168 ? -3.963  1.251   18.701  1 30.9  ? 168 SER A CB    1 
ATOM   1383  O  OG    . SER A 1 168 ? -2.687  0.981   18.142  1 33.89 ? 168 SER A OG    1 
ATOM   1384  N  N     . TYR A 1 169 ? -3.483  -1.998  18.858  1 27.77 ? 169 TYR A N     1 
ATOM   1385  C  CA    . TYR A 1 169 ? -3.413  -3.283  18.186  1 27.62 ? 169 TYR A CA    1 
ATOM   1386  C  C     . TYR A 1 169 ? -4.402  -4.27   18.83   1 27.23 ? 169 TYR A C     1 
ATOM   1387  O  O     . TYR A 1 169 ? -5.105  -4.991  18.127  1 27.26 ? 169 TYR A O     1 
ATOM   1388  C  CB    . TYR A 1 169 ? -1.965  -3.804  18.217  1 27.66 ? 169 TYR A CB    1 
ATOM   1389  C  CG    . TYR A 1 169 ? -1.058  -3.042  17.272  1 28.31 ? 169 TYR A CG    1 
ATOM   1390  C  CD1   . TYR A 1 169 ? -0.656  -1.748  17.555  1 29.19 ? 169 TYR A CD1   1 
ATOM   1391  C  CD2   . TYR A 1 169 ? -0.637  -3.603  16.075  1 29.08 ? 169 TYR A CD2   1 
ATOM   1392  C  CE1   . TYR A 1 169 ? 0.132   -1.025  16.668  1 29.8  ? 169 TYR A CE1   1 
ATOM   1393  C  CE2   . TYR A 1 169 ? 0.165   -2.896  15.189  1 29.74 ? 169 TYR A CE2   1 
ATOM   1394  C  CZ    . TYR A 1 169 ? 0.546   -1.607  15.488  1 30.38 ? 169 TYR A CZ    1 
ATOM   1395  O  OH    . TYR A 1 169 ? 1.329   -0.913  14.605  1 31.77 ? 169 TYR A OH    1 
ATOM   1396  N  N     . ILE A 1 170 ? -4.498  -4.258  20.16   1 26.72 ? 170 ILE A N     1 
ATOM   1397  C  CA    . ILE A 1 170 ? -5.431  -5.116  20.88   1 26.69 ? 170 ILE A CA    1 
ATOM   1398  C  C     . ILE A 1 170 ? -6.867  -4.703  20.584  1 27.49 ? 170 ILE A C     1 
ATOM   1399  O  O     . ILE A 1 170 ? -7.701  -5.565  20.317  1 27.74 ? 170 ILE A O     1 
ATOM   1400  C  CB    . ILE A 1 170 ? -5.15   -5.096  22.395  1 26.31 ? 170 ILE A CB    1 
ATOM   1401  C  CG1   . ILE A 1 170 ? -3.741  -5.592  22.711  1 26.72 ? 170 ILE A CG1   1 
ATOM   1402  C  CG2   . ILE A 1 170 ? -6.197  -5.904  23.143  1 26.52 ? 170 ILE A CG2   1 
ATOM   1403  C  CD1   . ILE A 1 170 ? -3.324  -5.322  24.107  1 27.83 ? 170 ILE A CD1   1 
ATOM   1404  N  N     . SER A 1 171 ? -7.162  -3.394  20.616  1 27.7  ? 171 SER A N     1 
ATOM   1405  C  CA    . SER A 1 171 ? -8.518  -2.918  20.348  1 28.32 ? 171 SER A CA    1 
ATOM   1406  C  C     . SER A 1 171 ? -8.928  -3.134  18.898  1 28.68 ? 171 SER A C     1 
ATOM   1407  O  O     . SER A 1 171 ? -10.082 -3.469  18.656  1 29.02 ? 171 SER A O     1 
ATOM   1408  C  CB    . SER A 1 171 ? -8.686  -1.458  20.747  1 29.62 ? 171 SER A CB    1 
ATOM   1409  O  OG    . SER A 1 171 ? -7.728  -0.647  20.093  1 32    ? 171 SER A OG    1 
ATOM   1410  N  N     . HIS A 1 172 ? -7.998  -2.985  17.938  1 28.45 ? 172 HIS A N     1 
ATOM   1411  C  CA    . HIS A 1 172 ? -8.316  -3.25   16.531  1 29.04 ? 172 HIS A CA    1 
ATOM   1412  C  C     . HIS A 1 172 ? -8.634  -4.738  16.353  1 30.21 ? 172 HIS A C     1 
ATOM   1413  O  O     . HIS A 1 172 ? -9.542  -5.08   15.601  1 30.5  ? 172 HIS A O     1 
ATOM   1414  C  CB    . HIS A 1 172 ? -7.158  -2.849  15.606  1 29.29 ? 172 HIS A CB    1 
ATOM   1415  C  CG    . HIS A 1 172 ? -7.567  -2.642  14.18   1 30.89 ? 172 HIS A CG    1 
ATOM   1416  N  ND1   . HIS A 1 172 ? -8.824  -2.171  13.852  1 32.59 ? 172 HIS A ND1   1 
ATOM   1417  C  CD2   . HIS A 1 172 ? -6.849  -2.793  13.043  1 31.99 ? 172 HIS A CD2   1 
ATOM   1418  C  CE1   . HIS A 1 172 ? -8.84   -2.075  12.531  1 33.06 ? 172 HIS A CE1   1 
ATOM   1419  N  NE2   . HIS A 1 172 ? -7.674  -2.44   12      1 32.99 ? 172 HIS A NE2   1 
ATOM   1420  N  N     . SER A 1 173 ? -7.909  -5.618  17.077  1 30.59 ? 173 SER A N     1 
ATOM   1421  C  CA    . SER A 1 173 ? -8.148  -7.053  17.066  1 31.29 ? 173 SER A CA    1 
ATOM   1422  C  C     . SER A 1 173 ? -9.557  -7.361  17.576  1 31.92 ? 173 SER A C     1 
ATOM   1423  O  O     . SER A 1 173 ? -10.265 -8.13   16.942  1 32.11 ? 173 SER A O     1 
ATOM   1424  C  CB    . SER A 1 173 ? -7.116  -7.773  17.925  1 32.49 ? 173 SER A CB    1 
ATOM   1425  O  OG    . SER A 1 173 ? -5.827  -7.704  17.342  1 34.69 ? 173 SER A OG    1 
ATOM   1426  N  N     . LYS A 1 174 ? -9.975  -6.752  18.689  1 32.29 ? 174 LYS A N     1 
ATOM   1427  C  CA    . LYS A 1 174 ? -11.314 -6.98   19.226  1 33.32 ? 174 LYS A CA    1 
ATOM   1428  C  C     . LYS A 1 174 ? -12.396 -6.491  18.267  1 33.99 ? 174 LYS A C     1 
ATOM   1429  O  O     . LYS A 1 174 ? -13.345 -7.224  17.997  1 34.28 ? 174 LYS A O     1 
ATOM   1430  C  CB    . LYS A 1 174 ? -11.484 -6.291  20.583  1 35.46 ? 174 LYS A CB    1 
ATOM   1431  C  CG    . LYS A 1 174 ? -10.524 -6.768  21.641  1 40.22 ? 174 LYS A CG    1 
ATOM   1432  C  CD    . LYS A 1 174 ? -10.964 -6.247  22.97   1 45.68 ? 174 LYS A CD    1 
ATOM   1433  C  CE    . LYS A 1 174 ? -9.828  -6.269  23.94   1 50.61 ? 174 LYS A CE    1 
ATOM   1434  N  NZ    . LYS A 1 174 ? -10.031 -5.27   25.002  1 53.99 ? 174 LYS A NZ    1 
ATOM   1435  N  N     . ASN A 1 175 ? -12.249 -5.263  17.748  1 34.01 ? 175 ASN A N     1 
ATOM   1436  C  CA    . ASN A 1 175 ? -13.214 -4.657  16.838  1 34.43 ? 175 ASN A CA    1 
ATOM   1437  C  C     . ASN A 1 175 ? -13.388 -5.432  15.536  1 34.65 ? 175 ASN A C     1 
ATOM   1438  O  O     . ASN A 1 175 ? -14.504 -5.535  15.04   1 35.07 ? 175 ASN A O     1 
ATOM   1439  C  CB    . ASN A 1 175 ? -12.819 -3.209  16.531  1 35.66 ? 175 ASN A CB    1 
ATOM   1440  C  CG    . ASN A 1 175 ? -12.927 -2.27   17.705  1 38.8  ? 175 ASN A CG    1 
ATOM   1441  O  OD1   . ASN A 1 175 ? -13.726 -2.464  18.628  1 39.76 ? 175 ASN A OD1   1 
ATOM   1442  N  ND2   . ASN A 1 175 ? -12.112 -1.228  17.692  1 39.58 ? 175 ASN A ND2   1 
ATOM   1443  N  N     . THR A 1 176 ? -12.3   -5.968  14.977  1 34.26 ? 176 THR A N     1 
ATOM   1444  C  CA    . THR A 1 176 ? -12.364 -6.675  13.7    1 34.37 ? 176 THR A CA    1 
ATOM   1445  C  C     . THR A 1 176 ? -12.567 -8.177  13.801  1 34.07 ? 176 THR A C     1 
ATOM   1446  O  O     . THR A 1 176 ? -12.998 -8.801  12.836  1 34.43 ? 176 THR A O     1 
ATOM   1447  C  CB    . THR A 1 176 ? -11.069 -6.442  12.923  1 35.78 ? 176 THR A CB    1 
ATOM   1448  O  OG1   . THR A 1 176 ? -9.975  -6.913  13.713  1 36.75 ? 176 THR A OG1   1 
ATOM   1449  C  CG2   . THR A 1 176 ? -10.867 -4.983  12.542  1 36.23 ? 176 THR A CG2   1 
ATOM   1450  N  N     . GLY A 1 177 ? -12.186 -8.759  14.922  1 33.36 ? 177 GLY A N     1 
ATOM   1451  C  CA    . GLY A 1 177 ? -12.205 -10.21  15.08   1 33.18 ? 177 GLY A CA    1 
ATOM   1452  C  C     . GLY A 1 177 ? -10.965 -10.874 14.492  1 32.7  ? 177 GLY A C     1 
ATOM   1453  O  O     . GLY A 1 177 ? -10.857 -12.102 14.491  1 32.85 ? 177 GLY A O     1 
ATOM   1454  N  N     . ASN A 1 178 ? -10.009 -10.064 13.992  1 31.95 ? 178 ASN A N     1 
ATOM   1455  C  CA    . ASN A 1 178 ? -8.763  -10.496 13.367  1 31.64 ? 178 ASN A CA    1 
ATOM   1456  C  C     . ASN A 1 178 ? -7.594  -10.452 14.373  1 30.77 ? 178 ASN A C     1 
ATOM   1457  O  O     . ASN A 1 178 ? -7.732  -9.914  15.467  1 30.63 ? 178 ASN A O     1 
ATOM   1458  C  CB    . ASN A 1 178 ? -8.48   -9.589  12.151  1 32.82 ? 178 ASN A CB    1 
ATOM   1459  C  CG    . ASN A 1 178 ? -7.378  -10.048 11.223  1 36.3  ? 178 ASN A CG    1 
ATOM   1460  O  OD1   . ASN A 1 178 ? -6.961  -11.215 11.215  1 37.6  ? 178 ASN A OD1   1 
ATOM   1461  N  ND2   . ASN A 1 178 ? -6.885  -9.129  10.412  1 36.94 ? 178 ASN A ND2   1 
ATOM   1462  N  N     . PHE A 1 179 ? -6.454  -11.042 14.012  1 30.01 ? 179 PHE A N     1 
ATOM   1463  C  CA    . PHE A 1 179 ? -5.277  -11.039 14.858  1 29.69 ? 179 PHE A CA    1 
ATOM   1464  C  C     . PHE A 1 179 ? -4.308  -9.962  14.404  1 29.7  ? 179 PHE A C     1 
ATOM   1465  O  O     . PHE A 1 179 ? -3.61   -10.133 13.408  1 29.93 ? 179 PHE A O     1 
ATOM   1466  C  CB    . PHE A 1 179 ? -4.593  -12.396 14.817  1 29.27 ? 179 PHE A CB    1 
ATOM   1467  C  CG    . PHE A 1 179 ? -3.426  -12.508 15.76   1 29.48 ? 179 PHE A CG    1 
ATOM   1468  C  CD1   . PHE A 1 179 ? -3.579  -12.252 17.111  1 30.12 ? 179 PHE A CD1   1 
ATOM   1469  C  CD2   . PHE A 1 179 ? -2.191  -12.918 15.308  1 30.06 ? 179 PHE A CD2   1 
ATOM   1470  C  CE1   . PHE A 1 179 ? -2.507  -12.372 17.981  1 30.67 ? 179 PHE A CE1   1 
ATOM   1471  C  CE2   . PHE A 1 179 ? -1.131  -13.067 16.187  1 30.62 ? 179 PHE A CE2   1 
ATOM   1472  C  CZ    . PHE A 1 179 ? -1.292  -12.785 17.515  1 30.36 ? 179 PHE A CZ    1 
ATOM   1473  N  N     . ILE A 1 180 ? -4.292  -8.837  15.117  1 29.27 ? 180 ILE A N     1 
ATOM   1474  C  CA    . ILE A 1 180 ? -3.398  -7.713  14.863  1 29.25 ? 180 ILE A CA    1 
ATOM   1475  C  C     . ILE A 1 180 ? -2.648  -7.507  16.17   1 29.59 ? 180 ILE A C     1 
ATOM   1476  O  O     . ILE A 1 180 ? -3.289  -7.254  17.19   1 29.68 ? 180 ILE A O     1 
ATOM   1477  C  CB    . ILE A 1 180 ? -4.215  -6.466  14.484  1 29.19 ? 180 ILE A CB    1 
ATOM   1478  C  CG1   . ILE A 1 180 ? -5.119  -6.751  13.28   1 29.76 ? 180 ILE A CG1   1 
ATOM   1479  C  CG2   . ILE A 1 180 ? -3.294  -5.295  14.22   1 29.47 ? 180 ILE A CG2   1 
ATOM   1480  C  CD1   . ILE A 1 180 ? -6.571  -6.6    13.562  1 30.75 ? 180 ILE A CD1   1 
ATOM   1481  N  N     . VAL A 1 181 ? -1.317  -7.674  16.172  1 29.63 ? 181 VAL A N     1 
ATOM   1482  C  CA    . VAL A 1 181 ? -0.559  -7.6    17.419  1 30.14 ? 181 VAL A CA    1 
ATOM   1483  C  C     . VAL A 1 181 ? 0.799   -6.9    17.283  1 30.74 ? 181 VAL A C     1 
ATOM   1484  O  O     . VAL A 1 181 ? 1.351   -6.769  16.19   1 30.84 ? 181 VAL A O     1 
ATOM   1485  C  CB    . VAL A 1 181 ? -0.399  -9.039  17.981  1 30.64 ? 181 VAL A CB    1 
ATOM   1486  C  CG1   . VAL A 1 181 ? 0.665   -9.805  17.206  1 31.29 ? 181 VAL A CG1   1 
ATOM   1487  C  CG2   . VAL A 1 181 ? -0.102  -9.049  19.478  1 30.89 ? 181 VAL A CG2   1 
ATOM   1488  N  N     . GLN A 1 182 ? 1.321   -6.431  18.413  1 30.92 ? 182 GLN A N     1 
ATOM   1489  C  CA    . GLN A 1 182 ? 2.643   -5.848  18.508  1 31.28 ? 182 GLN A CA    1 
ATOM   1490  C  C     . GLN A 1 182 ? 3.452   -6.845  19.35   1 31.49 ? 182 GLN A C     1 
ATOM   1491  O  O     . GLN A 1 182 ? 3.031   -7.243  20.441  1 31.55 ? 182 GLN A O     1 
ATOM   1492  C  CB    . GLN A 1 182 ? 2.585   -4.472  19.181  1 32.45 ? 182 GLN A CB    1 
ATOM   1493  C  CG    . GLN A 1 182 ? 3.765   -3.582  18.841  1 34.83 ? 182 GLN A CG    1 
ATOM   1494  C  CD    . GLN A 1 182 ? 3.506   -2.186  19.328  1 37.83 ? 182 GLN A CD    1 
ATOM   1495  O  OE1   . GLN A 1 182 ? 3.348   -1.951  20.512  1 38.61 ? 182 GLN A OE1   1 
ATOM   1496  N  NE2   . GLN A 1 182 ? 3.44    -1.225  18.438  1 38.55 ? 182 GLN A NE2   1 
ATOM   1497  N  N     . ALA A 1 183 ? 4.559   -7.318  18.791  1 31.31 ? 183 ALA A N     1 
ATOM   1498  C  CA    . ALA A 1 183 ? 5.45    -8.282  19.418  1 31.48 ? 183 ALA A CA    1 
ATOM   1499  C  C     . ALA A 1 183 ? 6.792   -7.611  19.663  1 31.52 ? 183 ALA A C     1 
ATOM   1500  O  O     . ALA A 1 183 ? 7.255   -6.844  18.821  1 31.71 ? 183 ALA A O     1 
ATOM   1501  C  CB    . ALA A 1 183 ? 5.628   -9.48   18.504  1 31.54 ? 183 ALA A CB    1 
ATOM   1502  N  N     . TYR A 1 184 ? 7.423   -7.9    20.796  1 31.26 ? 184 TYR A N     1 
ATOM   1503  C  CA    . TYR A 1 184 ? 8.675   -7.244  21.153  1 31.7  ? 184 TYR A CA    1 
ATOM   1504  C  C     . TYR A 1 184 ? 9.81    -8.216  21.217  1 32.25 ? 184 TYR A C     1 
ATOM   1505  O  O     . TYR A 1 184 ? 9.708   -9.25   21.861  1 32.28 ? 184 TYR A O     1 
ATOM   1506  C  CB    . TYR A 1 184 ? 8.539   -6.467  22.482  1 31.68 ? 184 TYR A CB    1 
ATOM   1507  C  CG    . TYR A 1 184 ? 7.268   -5.653  22.527  1 32.36 ? 184 TYR A CG    1 
ATOM   1508  C  CD1   . TYR A 1 184 ? 7.211   -4.388  21.96   1 33.18 ? 184 TYR A CD1   1 
ATOM   1509  C  CD2   . TYR A 1 184 ? 6.09    -6.2    23.011  1 33.19 ? 184 TYR A CD2   1 
ATOM   1510  C  CE1   . TYR A 1 184 ? 6.023   -3.676  21.909  1 33.94 ? 184 TYR A CE1   1 
ATOM   1511  C  CE2   . TYR A 1 184 ? 4.896   -5.504  22.956  1 33.97 ? 184 TYR A CE2   1 
ATOM   1512  C  CZ    . TYR A 1 184 ? 4.868   -4.24   22.411  1 34.8  ? 184 TYR A CZ    1 
ATOM   1513  O  OH    . TYR A 1 184 ? 3.689   -3.55   22.386  1 36.3  ? 184 TYR A OH    1 
ATOM   1514  N  N     . PHE A 1 185 ? 10.891  -7.893  20.534  1 32.68 ? 185 PHE A N     1 
ATOM   1515  C  CA    . PHE A 1 185 ? 12.083  -8.722  20.543  1 33.73 ? 185 PHE A CA    1 
ATOM   1516  C  C     . PHE A 1 185 ? 13.148  -8.003  21.364  1 35.37 ? 185 PHE A C     1 
ATOM   1517  O  O     . PHE A 1 185 ? 13.196  -6.771  21.39   1 35.29 ? 185 PHE A O     1 
ATOM   1518  C  CB    . PHE A 1 185 ? 12.589  -8.982  19.111  1 33.32 ? 185 PHE A CB    1 
ATOM   1519  C  CG    . PHE A 1 185 ? 11.875  -10.053 18.317  1 33.48 ? 185 PHE A CG    1 
ATOM   1520  C  CD1   . PHE A 1 185 ? 10.624  -10.502 18.693  1 34.11 ? 185 PHE A CD1   1 
ATOM   1521  C  CD2   . PHE A 1 185 ? 12.441  -10.584 17.177  1 34.02 ? 185 PHE A CD2   1 
ATOM   1522  C  CE1   . PHE A 1 185 ? 9.97    -11.478 17.96   1 34.56 ? 185 PHE A CE1   1 
ATOM   1523  C  CE2   . PHE A 1 185 ? 11.781  -11.556 16.447  1 34.6  ? 185 PHE A CE2   1 
ATOM   1524  C  CZ    . PHE A 1 185 ? 10.551  -11.998 16.844  1 34.26 ? 185 PHE A CZ    1 
ATOM   1525  N  N     . ARG A 1 186 ? 13.988  -8.773  22.052  1 36.59 ? 186 ARG A N     1 
ATOM   1526  C  CA    . ARG A 1 186 ? 15.05   -8.237  22.885  1 38.22 ? 186 ARG A CA    1 
ATOM   1527  C  C     . ARG A 1 186 ? 16.144  -7.588  22.058  1 39.57 ? 186 ARG A C     1 
ATOM   1528  O  O     . ARG A 1 186 ? 16.898  -8.271  21.369  1 39.59 ? 186 ARG A O     1 
ATOM   1529  C  CB    . ARG A 1 186 ? 15.645  -9.327  23.785  1 39.8  ? 186 ARG A CB    1 
ATOM   1530  C  CG    . ARG A 1 186 ? 16.66   -8.774  24.752  1 43.52 ? 186 ARG A CG    1 
ATOM   1531  C  CD    . ARG A 1 186 ? 17.635  -9.819  25.211  1 47.45 ? 186 ARG A CD    1 
ATOM   1532  N  NE    . ARG A 1 186 ? 18.029  -9.505  26.567  1 51.27 ? 186 ARG A NE    1 
ATOM   1533  C  CZ    . ARG A 1 186 ? 17.651  -10.182 27.645  1 53.66 ? 186 ARG A CZ    1 
ATOM   1534  N  NH1   . ARG A 1 186 ? 18.067  -9.809  28.845  1 53.63 ? 186 ARG A NH1   1 
ATOM   1535  N  NH2   . ARG A 1 186 ? 16.901  -11.273 27.528  1 53.45 ? 186 ARG A NH2   1 
ATOM   1536  N  N     . GLY A 1 187 ? 16.231  -6.275  22.154  1 40.58 ? 187 GLY A N     1 
ATOM   1537  C  CA    . GLY A 1 187 ? 17.258  -5.511  21.469  1 42.16 ? 187 GLY A CA    1 
ATOM   1538  C  C     . GLY A 1 187 ? 18.6    -5.676  22.146  1 43.75 ? 187 GLY A C     1 
ATOM   1539  O  O     . GLY A 1 187 ? 18.666  -5.996  23.336  1 43.77 ? 187 GLY A O     1 
ATOM   1540  N  N     . GLU A 1 188 ? 19.682  -5.469  21.398  1 45    ? 188 GLU A N     1 
ATOM   1541  C  CA    . GLU A 1 188 ? 21.029  -5.596  21.948  1 46.7  ? 188 GLU A CA    1 
ATOM   1542  C  C     . GLU A 1 188 ? 21.273  -4.577  23.06   1 48.23 ? 188 GLU A C     1 
ATOM   1543  O  O     . GLU A 1 188 ? 22      -4.878  24.008  1 48.58 ? 188 GLU A O     1 
ATOM   1544  C  CB    . GLU A 1 188 ? 22.081  -5.435  20.847  1 49.03 ? 188 GLU A CB    1 
ATOM   1545  C  CG    . GLU A 1 188 ? 21.922  -6.404  19.69   1 53.58 ? 188 GLU A CG    1 
ATOM   1546  C  CD    . GLU A 1 188 ? 21.204  -5.832  18.483  1 59.18 ? 188 GLU A CD    1 
ATOM   1547  O  OE1   . GLU A 1 188 ? 20.288  -4.997  18.665  1 59.97 ? 188 GLU A OE1   1 
ATOM   1548  O  OE2   . GLU A 1 188 ? 21.561  -6.222  17.349  1 61.62 ? 188 GLU A OE2   1 
ATOM   1549  N  N     . GLU A 1 189 ? 20.648  -3.386  22.967  1 48.87 ? 189 GLU A N     1 
ATOM   1550  C  CA    . GLU A 1 189 ? 20.815  -2.356  23.985  1 49.88 ? 189 GLU A CA    1 
ATOM   1551  C  C     . GLU A 1 189 ? 19.834  -2.474  25.171  1 50.63 ? 189 GLU A C     1 
ATOM   1552  O  O     . GLU A 1 189 ? 19.766  -1.556  25.993  1 50.77 ? 189 GLU A O     1 
ATOM   1553  C  CB    . GLU A 1 189 ? 20.789  -0.958  23.365  1 52.1  ? 189 GLU A CB    1 
ATOM   1554  C  CG    . GLU A 1 189 ? 22.155  -0.569  22.834  1 56.71 ? 189 GLU A CG    1 
ATOM   1555  C  CD    . GLU A 1 189 ? 22.237  0.812   22.217  1 62.74 ? 189 GLU A CD    1 
ATOM   1556  O  OE1   . GLU A 1 189 ? 21.209  1.294   21.687  1 63.94 ? 189 GLU A OE1   1 
ATOM   1557  O  OE2   . GLU A 1 189 ? 23.336  1.41    22.257  1 64.64 ? 189 GLU A OE2   1 
ATOM   1558  N  N     . TYR A 1 190 ? 19.112  -3.606  25.288  1 50.89 ? 190 TYR A N     1 
ATOM   1559  C  CA    . TYR A 1 190 ? 18.254  -3.836  26.447  1 51.57 ? 190 TYR A CA    1 
ATOM   1560  C  C     . TYR A 1 190 ? 19.224  -4.242  27.555  1 52.13 ? 190 TYR A C     1 
ATOM   1561  O  O     . TYR A 1 190 ? 19.712  -5.372  27.559  1 52.47 ? 190 TYR A O     1 
ATOM   1562  C  CB    . TYR A 1 190 ? 17.229  -4.966  26.199  1 51.56 ? 190 TYR A CB    1 
ATOM   1563  C  CG    . TYR A 1 190 ? 16.468  -5.357  27.449  1 52.16 ? 190 TYR A CG    1 
ATOM   1564  C  CD1   . TYR A 1 190 ? 15.564  -4.484  28.037  1 52.99 ? 190 TYR A CD1   1 
ATOM   1565  C  CD2   . TYR A 1 190 ? 16.679  -6.584  28.063  1 53    ? 190 TYR A CD2   1 
ATOM   1566  C  CE1   . TYR A 1 190 ? 14.889  -4.821  29.204  1 53.82 ? 190 TYR A CE1   1 
ATOM   1567  C  CE2   . TYR A 1 190 ? 16.001  -6.936  29.224  1 53.83 ? 190 TYR A CE2   1 
ATOM   1568  C  CZ    . TYR A 1 190 ? 15.111  -6.047  29.795  1 54.63 ? 190 TYR A CZ    1 
ATOM   1569  O  OH    . TYR A 1 190 ? 14.453  -6.364  30.955  1 55.97 ? 190 TYR A OH    1 
ATOM   1570  N  N     . GLN A 1 191 ? 19.569  -3.306  28.437  1 52.02 ? 191 GLN A N     1 
ATOM   1571  C  CA    . GLN A 1 191 ? 20.516  -3.576  29.513  1 52.37 ? 191 GLN A CA    1 
ATOM   1572  C  C     . GLN A 1 191 ? 19.883  -3.106  30.814  1 52.57 ? 191 GLN A C     1 
ATOM   1573  O  O     . GLN A 1 191 ? 20.14   -1.992  31.263  1 52.81 ? 191 GLN A O     1 
ATOM   1574  C  CB    . GLN A 1 191 ? 21.811  -2.81   29.235  1 53.81 ? 191 GLN A CB    1 
ATOM   1575  C  CG    . GLN A 1 191 ? 23.08   -3.632  29.391  1 56.71 ? 191 GLN A CG    1 
ATOM   1576  C  CD    . GLN A 1 191 ? 23.126  -4.81   28.453  1 60.55 ? 191 GLN A CD    1 
ATOM   1577  O  OE1   . GLN A 1 191 ? 22.962  -4.686  27.233  1 61.53 ? 191 GLN A OE1   1 
ATOM   1578  N  NE2   . GLN A 1 191 ? 23.353  -5.989  29.008  1 61.44 ? 191 GLN A NE2   1 
ATOM   1579  N  N     . PRO A 1 192 ? 19.003  -3.927  31.41   1 52.38 ? 192 PRO A N     1 
ATOM   1580  C  CA    . PRO A 1 192 ? 18.277  -3.489  32.619  1 52.39 ? 192 PRO A CA    1 
ATOM   1581  C  C     . PRO A 1 192 ? 19.124  -3.265  33.865  1 52.44 ? 192 PRO A C     1 
ATOM   1582  O  O     . PRO A 1 192 ? 18.711  -2.529  34.759  1 52.6  ? 192 PRO A O     1 
ATOM   1583  C  CB    . PRO A 1 192 ? 17.241  -4.595  32.829  1 53.05 ? 192 PRO A CB    1 
ATOM   1584  C  CG    . PRO A 1 192 ? 17.833  -5.788  32.167  1 53.46 ? 192 PRO A CG    1 
ATOM   1585  C  CD    . PRO A 1 192 ? 18.57   -5.266  30.975  1 51.83 ? 192 PRO A CD    1 
ATOM   1586  N  N     . LYS A 1 193 ? 20.304  -3.88   33.925  1 52.22 ? 193 LYS A N     1 
ATOM   1587  C  CA    . LYS A 1 193 ? 21.211  -3.693  35.053  1 52.59 ? 193 LYS A CA    1 
ATOM   1588  C  C     . LYS A 1 193 ? 21.815  -2.273  35.083  1 52.79 ? 193 LYS A C     1 
ATOM   1589  O  O     . LYS A 1 193 ? 22.3    -1.845  36.128  1 53.08 ? 193 LYS A O     1 
ATOM   1590  C  CB    . LYS A 1 193 ? 22.344  -4.732  34.997  1 54.42 ? 193 LYS A CB    1 
ATOM   1591  C  CG    . LYS A 1 193 ? 21.855  -6.172  34.902  1 58.44 ? 193 LYS A CG    1 
ATOM   1592  C  CD    . LYS A 1 193 ? 23.001  -7.159  34.715  1 62.64 ? 193 LYS A CD    1 
ATOM   1593  C  CE    . LYS A 1 193 ? 22.51   -8.59   34.672  1 66.13 ? 193 LYS A CE    1 
ATOM   1594  N  NZ    . LYS A 1 193 ? 23.624  -9.557  34.483  1 68.21 ? 193 LYS A NZ    1 
ATOM   1595  N  N     . TYR A 1 194 ? 21.787  -1.544  33.95   1 52.49 ? 194 TYR A N     1 
ATOM   1596  C  CA    . TYR A 1 194 ? 22.384  -0.217  33.844  1 52.65 ? 194 TYR A CA    1 
ATOM   1597  C  C     . TYR A 1 194 ? 21.388  0.934   33.716  1 51.84 ? 194 TYR A C     1 
ATOM   1598  O  O     . TYR A 1 194 ? 21.759  2.073   33.997  1 52.04 ? 194 TYR A O     1 
ATOM   1599  C  CB    . TYR A 1 194 ? 23.388  -0.188  32.682  1 53.21 ? 194 TYR A CB    1 
ATOM   1600  C  CG    . TYR A 1 194 ? 24.548  -1.129  32.917  1 54.73 ? 194 TYR A CG    1 
ATOM   1601  C  CD1   . TYR A 1 194 ? 25.617  -0.757  33.718  1 56    ? 194 TYR A CD1   1 
ATOM   1602  C  CD2   . TYR A 1 194 ? 24.534  -2.421  32.411  1 55.91 ? 194 TYR A CD2   1 
ATOM   1603  C  CE1   . TYR A 1 194 ? 26.659  -1.637  33.985  1 57.11 ? 194 TYR A CE1   1 
ATOM   1604  C  CE2   . TYR A 1 194 ? 25.572  -3.309  32.668  1 57.01 ? 194 TYR A CE2   1 
ATOM   1605  C  CZ    . TYR A 1 194 ? 26.636  -2.913  33.456  1 58.03 ? 194 TYR A CZ    1 
ATOM   1606  O  OH    . TYR A 1 194 ? 27.669  -3.785  33.708  1 59.57 ? 194 TYR A OH    1 
ATOM   1607  N  N     . ASP A 1 195 ? 20.143  0.664   33.291  1 50.76 ? 195 ASP A N     1 
ATOM   1608  C  CA    . ASP A 1 195 ? 19.156  1.732   33.124  1 50.11 ? 195 ASP A CA    1 
ATOM   1609  C  C     . ASP A 1 195 ? 17.969  1.603   34.056  1 48.81 ? 195 ASP A C     1 
ATOM   1610  O  O     . ASP A 1 195 ? 17.224  0.628   33.989  1 48.91 ? 195 ASP A O     1 
ATOM   1611  C  CB    . ASP A 1 195 ? 18.686  1.83    31.671  1 52.06 ? 195 ASP A CB    1 
ATOM   1612  C  CG    . ASP A 1 195 ? 18.149  3.199   31.292  1 57.18 ? 195 ASP A CG    1 
ATOM   1613  O  OD1   . ASP A 1 195 ? 17.428  3.805   32.114  1 58.37 ? 195 ASP A OD1   1 
ATOM   1614  O  OD2   . ASP A 1 195 ? 18.451  3.666   30.173  1 59.24 ? 195 ASP A OD2   1 
ATOM   1615  N  N     . LYS A 1 196 ? 17.759  2.631   34.879  1 47.54 ? 196 LYS A N     1 
ATOM   1616  C  CA    . LYS A 1 196 ? 16.672  2.674   35.845  1 46.84 ? 196 LYS A CA    1 
ATOM   1617  C  C     . LYS A 1 196 ? 15.289  2.718   35.204  1 46.04 ? 196 LYS A C     1 
ATOM   1618  O  O     . LYS A 1 196 ? 14.326  2.294   35.836  1 46.36 ? 196 LYS A O     1 
ATOM   1619  C  CB    . LYS A 1 196 ? 16.863  3.838   36.823  1 48.29 ? 196 LYS A CB    1 
ATOM   1620  C  CG    . LYS A 1 196 ? 18.205  3.826   37.568  1 51.51 ? 196 LYS A CG    1 
ATOM   1621  C  CD    . LYS A 1 196 ? 18.463  2.54    38.348  1 55.12 ? 196 LYS A CD    1 
ATOM   1622  C  CE    . LYS A 1 196 ? 19.442  2.768   39.467  1 58.29 ? 196 LYS A CE    1 
ATOM   1623  N  NZ    . LYS A 1 196 ? 18.819  3.556   40.557  1 59.96 ? 196 LYS A NZ    1 
ATOM   1624  N  N     . LYS A 1 197 ? 15.178  3.194   33.958  1 44.93 ? 197 LYS A N     1 
ATOM   1625  C  CA    . LYS A 1 197 ? 13.885  3.224   33.269  1 44.56 ? 197 LYS A CA    1 
ATOM   1626  C  C     . LYS A 1 197 ? 13.314  1.813   33.03   1 43.96 ? 197 LYS A C     1 
ATOM   1627  O  O     . LYS A 1 197 ? 12.095  1.647   32.935  1 44.03 ? 197 LYS A O     1 
ATOM   1628  C  CB    . LYS A 1 197 ? 13.999  3.966   31.931  1 46.38 ? 197 LYS A CB    1 
ATOM   1629  C  CG    . LYS A 1 197 ? 14.235  5.46    32.072  1 50.2  ? 197 LYS A CG    1 
ATOM   1630  C  CD    . LYS A 1 197 ? 14.303  6.145   30.716  1 54.42 ? 197 LYS A CD    1 
ATOM   1631  C  CE    . LYS A 1 197 ? 14.395  7.641   30.862  1 57.71 ? 197 LYS A CE    1 
ATOM   1632  N  NZ    . LYS A 1 197 ? 13.218  8.185   31.592  1 59.37 ? 197 LYS A NZ    1 
ATOM   1633  N  N     . LEU A 1 198 ? 14.198  0.807   32.93   1 43.21 ? 198 LEU A N     1 
ATOM   1634  C  CA    . LEU A 1 198 ? 13.812  -0.58   32.683  1 42.89 ? 198 LEU A CA    1 
ATOM   1635  C  C     . LEU A 1 198 ? 13.696  -1.424  33.947  1 42.33 ? 198 LEU A C     1 
ATOM   1636  O  O     . LEU A 1 198 ? 13.471  -2.627  33.827  1 42.73 ? 198 LEU A O     1 
ATOM   1637  C  CB    . LEU A 1 198 ? 14.829  -1.25   31.749  1 43.1  ? 198 LEU A CB    1 
ATOM   1638  C  CG    . LEU A 1 198 ? 15.109  -0.531  30.45   1 44.72 ? 198 LEU A CG    1 
ATOM   1639  C  CD1   . LEU A 1 198 ? 16.332  -1.109  29.767  1 45.37 ? 198 LEU A CD1   1 
ATOM   1640  C  CD2   . LEU A 1 198 ? 13.893  -0.557  29.543  1 45.43 ? 198 LEU A CD2   1 
ATOM   1641  N  N     . LYS A 1 199 ? 13.866  -0.83   35.143  1 41.32 ? 199 LYS A N     1 
ATOM   1642  C  CA    . LYS A 1 199 ? 13.807  -1.561  36.406  1 41.01 ? 199 LYS A CA    1 
ATOM   1643  C  C     . LYS A 1 199 ? 12.557  -2.416  36.567  1 40.68 ? 199 LYS A C     1 
ATOM   1644  O  O     . LYS A 1 199 ? 12.648  -3.534  37.076  1 41.04 ? 199 LYS A O     1 
ATOM   1645  C  CB    . LYS A 1 199 ? 13.963  -0.617  37.604  1 42.5  ? 199 LYS A CB    1 
ATOM   1646  C  CG    . LYS A 1 199 ? 15.417  -0.331  37.955  1 46.64 ? 199 LYS A CG    1 
ATOM   1647  C  CD    . LYS A 1 199 ? 15.645  -0.374  39.468  1 51.44 ? 199 LYS A CD    1 
ATOM   1648  C  CE    . LYS A 1 199 ? 14.994  0.77    40.213  1 55.22 ? 199 LYS A CE    1 
ATOM   1649  N  NZ    . LYS A 1 199 ? 15.792  2.027   40.111  1 57.37 ? 199 LYS A NZ    1 
ATOM   1650  N  N     . PHE A 1 200 ? 11.404  -1.919  36.106  1 39.74 ? 200 PHE A N     1 
ATOM   1651  C  CA    . PHE A 1 200 ? 10.161  -2.669  36.249  1 39.18 ? 200 PHE A CA    1 
ATOM   1652  C  C     . PHE A 1 200 ? 9.647   -3.264  34.943  1 38.42 ? 200 PHE A C     1 
ATOM   1653  O  O     . PHE A 1 200 ? 8.44    -3.348  34.753  1 38.63 ? 200 PHE A O     1 
ATOM   1654  C  CB    . PHE A 1 200 ? 9.098   -1.813  36.938  1 39.08 ? 200 PHE A CB    1 
ATOM   1655  C  CG    . PHE A 1 200 ? 9.568   -1.33   38.285  1 39.69 ? 200 PHE A CG    1 
ATOM   1656  C  CD1   . PHE A 1 200 ? 9.766   -2.219  39.324  1 40.59 ? 200 PHE A CD1   1 
ATOM   1657  C  CD2   . PHE A 1 200 ? 9.882   0.001   38.492  1 40.3  ? 200 PHE A CD2   1 
ATOM   1658  C  CE1   . PHE A 1 200 ? 10.232  -1.781  40.553  1 41.29 ? 200 PHE A CE1   1 
ATOM   1659  C  CE2   . PHE A 1 200 ? 10.349  0.436   39.721  1 41.02 ? 200 PHE A CE2   1 
ATOM   1660  C  CZ    . PHE A 1 200 ? 10.52   -0.455  40.745  1 40.96 ? 200 PHE A CZ    1 
ATOM   1661  N  N     . PHE A 1 201 ? 10.55   -3.7    34.056  1 37.38 ? 201 PHE A N     1 
ATOM   1662  C  CA    . PHE A 1 201 ? 10.139  -4.341  32.808  1 36.83 ? 201 PHE A CA    1 
ATOM   1663  C  C     . PHE A 1 201 ? 10.07   -5.855  33.039  1 36.49 ? 201 PHE A C     1 
ATOM   1664  O  O     . PHE A 1 201 ? 10.991  -6.42   33.631  1 36.76 ? 201 PHE A O     1 
ATOM   1665  C  CB    . PHE A 1 201 ? 11.121  -4.027  31.672  1 36.36 ? 201 PHE A CB    1 
ATOM   1666  C  CG    . PHE A 1 201 ? 10.675  -4.611  30.355  1 36.71 ? 201 PHE A CG    1 
ATOM   1667  C  CD1   . PHE A 1 201 ? 9.556   -4.125  29.709  1 37.26 ? 201 PHE A CD1   1 
ATOM   1668  C  CD2   . PHE A 1 201 ? 11.362  -5.663  29.775  1 37.49 ? 201 PHE A CD2   1 
ATOM   1669  C  CE1   . PHE A 1 201 ? 9.143   -4.668  28.499  1 37.79 ? 201 PHE A CE1   1 
ATOM   1670  C  CE2   . PHE A 1 201 ? 10.937  -6.213  28.573  1 37.99 ? 201 PHE A CE2   1 
ATOM   1671  C  CZ    . PHE A 1 201 ? 9.835   -5.708  27.94   1 37.6  ? 201 PHE A CZ    1 
ATOM   1672  N  N     . ASP A 1 202 ? 8.986   -6.515  32.594  1 35.66 ? 202 ASP A N     1 
ATOM   1673  C  CA    . ASP A 1 202 ? 8.856   -7.967  32.755  1 35.24 ? 202 ASP A CA    1 
ATOM   1674  C  C     . ASP A 1 202 ? 9.414   -8.648  31.504  1 34.81 ? 202 ASP A C     1 
ATOM   1675  O  O     . ASP A 1 202 ? 8.847   -8.498  30.425  1 34.98 ? 202 ASP A O     1 
ATOM   1676  C  CB    . ASP A 1 202 ? 7.387   -8.367  32.968  1 36.42 ? 202 ASP A CB    1 
ATOM   1677  C  CG    . ASP A 1 202 ? 7.173   -9.778  33.497  1 40.55 ? 202 ASP A CG    1 
ATOM   1678  O  OD1   . ASP A 1 202 ? 8.172   -10.432 33.876  1 41.14 ? 202 ASP A OD1   1 
ATOM   1679  O  OD2   . ASP A 1 202 ? 6.005   -10.22  33.557  1 42.64 ? 202 ASP A OD2   1 
ATOM   1680  N  N     . GLU A 1 203 ? 10.515  -9.402  31.638  1 34.05 ? 203 GLU A N     1 
ATOM   1681  C  CA    . GLU A 1 203 ? 11.136  -10.059 30.489  1 33.78 ? 203 GLU A CA    1 
ATOM   1682  C  C     . GLU A 1 203 ? 10.276  -11.128 29.831  1 33.23 ? 203 GLU A C     1 
ATOM   1683  O  O     . GLU A 1 203 ? 10.626  -11.579 28.746  1 33.47 ? 203 GLU A O     1 
ATOM   1684  C  CB    . GLU A 1 203 ? 12.518  -10.61  30.833  1 36.02 ? 203 GLU A CB    1 
ATOM   1685  C  CG    . GLU A 1 203 ? 13.517  -9.494  31.047  1 40.44 ? 203 GLU A CG    1 
ATOM   1686  C  CD    . GLU A 1 203 ? 14.913  -9.923  31.438  1 45.83 ? 203 GLU A CD    1 
ATOM   1687  O  OE1   . GLU A 1 203 ? 15.258  -11.11  31.234  1 46.59 ? 203 GLU A OE1   1 
ATOM   1688  O  OE2   . GLU A 1 203 ? 15.668  -9.058  31.939  1 47.95 ? 203 GLU A OE2   1 
ATOM   1689  N  N     . THR A 1 204 ? 9.138   -11.503 30.436  1 32.54 ? 204 THR A N     1 
ATOM   1690  C  CA    . THR A 1 204 ? 8.216   -12.435 29.785  1 32.56 ? 204 THR A CA    1 
ATOM   1691  C  C     . THR A 1 204 ? 7.501   -11.765 28.588  1 32.48 ? 204 THR A C     1 
ATOM   1692  O  O     . THR A 1 204 ? 6.9     -12.473 27.786  1 32.79 ? 204 THR A O     1 
ATOM   1693  C  CB    . THR A 1 204 ? 7.226   -13.063 30.778  1 33.7  ? 204 THR A CB    1 
ATOM   1694  O  OG1   . THR A 1 204 ? 6.202   -12.122 31.102  1 34.66 ? 204 THR A OG1   1 
ATOM   1695  C  CG2   . THR A 1 204 ? 7.906   -13.579 32.038  1 34.04 ? 204 THR A CG2   1 
ATOM   1696  N  N     . ILE A 1 205 ? 7.566   -10.413 28.469  1 31.83 ? 205 ILE A N     1 
ATOM   1697  C  CA    . ILE A 1 205 ? 6.985   -9.645  27.372  1 31.61 ? 205 ILE A CA    1 
ATOM   1698  C  C     . ILE A 1 205 ? 7.656   -9.999  26.043  1 31.15 ? 205 ILE A C     1 
ATOM   1699  O  O     . ILE A 1 205 ? 6.983   -10.004 25.017  1 31.13 ? 205 ILE A O     1 
ATOM   1700  C  CB    . ILE A 1 205 ? 7.043   -8.124  27.692  1 32.13 ? 205 ILE A CB    1 
ATOM   1701  C  CG1   . ILE A 1 205 ? 6.055   -7.766  28.809  1 32.67 ? 205 ILE A CG1   1 
ATOM   1702  C  CG2   . ILE A 1 205 ? 6.801   -7.262  26.45   1 32.84 ? 205 ILE A CG2   1 
ATOM   1703  C  CD1   . ILE A 1 205 ? 6.169   -6.378  29.339  1 33.75 ? 205 ILE A CD1   1 
ATOM   1704  N  N     . PHE A 1 206 ? 8.961   -10.337 26.056  1 30.84 ? 206 PHE A N     1 
ATOM   1705  C  CA    . PHE A 1 206 ? 9.677   -10.715 24.833  1 31.26 ? 206 PHE A CA    1 
ATOM   1706  C  C     . PHE A 1 206 ? 8.994   -11.898 24.119  1 31.75 ? 206 PHE A C     1 
ATOM   1707  O  O     . PHE A 1 206 ? 8.595   -12.868 24.767  1 31.67 ? 206 PHE A O     1 
ATOM   1708  C  CB    . PHE A 1 206 ? 11.16   -10.992 25.113  1 31.08 ? 206 PHE A CB    1 
ATOM   1709  C  CG    . PHE A 1 206 ? 11.93   -9.797  25.616  1 31.58 ? 206 PHE A CG    1 
ATOM   1710  C  CD1   . PHE A 1 206 ? 11.888  -8.591  24.94   1 32.4  ? 206 PHE A CD1   1 
ATOM   1711  C  CD2   . PHE A 1 206 ? 12.73   -9.894  26.739  1 32.27 ? 206 PHE A CD2   1 
ATOM   1712  C  CE1   . PHE A 1 206 ? 12.595  -7.496  25.403  1 33.13 ? 206 PHE A CE1   1 
ATOM   1713  C  CE2   . PHE A 1 206 ? 13.45   -8.804  27.192  1 33.05 ? 206 PHE A CE2   1 
ATOM   1714  C  CZ    . PHE A 1 206 ? 13.388  -7.614  26.513  1 32.95 ? 206 PHE A CZ    1 
ATOM   1715  N  N     . ALA A 1 207 ? 8.798   -11.778 22.795  1 31.99 ? 207 ALA A N     1 
ATOM   1716  C  CA    . ALA A 1 207 ? 8.052   -12.767 22.027  1 32.46 ? 207 ALA A CA    1 
ATOM   1717  C  C     . ALA A 1 207 ? 8.834   -13.514 20.936  1 32.65 ? 207 ALA A C     1 
ATOM   1718  O  O     . ALA A 1 207 ? 8.21    -13.977 19.982  1 32.72 ? 207 ALA A O     1 
ATOM   1719  C  CB    . ALA A 1 207 ? 6.823   -12.103 21.421  1 32.57 ? 207 ALA A CB    1 
ATOM   1720  N  N     . GLU A 1 208 ? 10.16   -13.685 21.08   1 32.68 ? 208 GLU A N     1 
ATOM   1721  C  CA    . GLU A 1 208 ? 10.937  -14.415 20.069  1 33.36 ? 208 GLU A CA    1 
ATOM   1722  C  C     . GLU A 1 208 ? 10.423  -15.838 19.824  1 33.53 ? 208 GLU A C     1 
ATOM   1723  O  O     . GLU A 1 208 ? 10.173  -16.204 18.675  1 33.76 ? 208 GLU A O     1 
ATOM   1724  C  CB    . GLU A 1 208 ? 12.429  -14.456 20.418  1 35.81 ? 208 GLU A CB    1 
ATOM   1725  C  CG    . GLU A 1 208 ? 13.146  -13.153 20.149  1 40.04 ? 208 GLU A CG    1 
ATOM   1726  C  CD    . GLU A 1 208 ? 13.378  -12.321 21.39   1 44.74 ? 208 GLU A CD    1 
ATOM   1727  O  OE1   . GLU A 1 208 ? 12.648  -12.502 22.392  1 44.69 ? 208 GLU A OE1   1 
ATOM   1728  O  OE2   . GLU A 1 208 ? 14.298  -11.476 21.352  1 46.78 ? 208 GLU A OE2   1 
ATOM   1729  N  N     . ASP A 1 209 ? 10.243  -16.626 20.892  1 33.22 ? 209 ASP A N     1 
ATOM   1730  C  CA    . ASP A 1 209 ? 9.762   -17.991 20.75   1 33.56 ? 209 ASP A CA    1 
ATOM   1731  C  C     . ASP A 1 209 ? 8.313   -18.062 20.287  1 32.98 ? 209 ASP A C     1 
ATOM   1732  O  O     . ASP A 1 209 ? 7.984   -18.908 19.466  1 33.2  ? 209 ASP A O     1 
ATOM   1733  C  CB    . ASP A 1 209 ? 9.94    -18.771 22.058  1 36.24 ? 209 ASP A CB    1 
ATOM   1734  C  CG    . ASP A 1 209 ? 11.352  -19.265 22.293  1 42.19 ? 209 ASP A CG    1 
ATOM   1735  O  OD1   . ASP A 1 209 ? 12.294  -18.678 21.707  1 43.02 ? 209 ASP A OD1   1 
ATOM   1736  O  OD2   . ASP A 1 209 ? 11.519  -20.243 23.062  1 44.94 ? 209 ASP A OD2   1 
ATOM   1737  N  N     . ASP A 1 210 ? 7.452   -17.179 20.797  1 32.18 ? 210 ASP A N     1 
ATOM   1738  C  CA    . ASP A 1 210 ? 6.037   -17.202 20.441  1 31.85 ? 210 ASP A CA    1 
ATOM   1739  C  C     . ASP A 1 210 ? 5.743   -16.761 19.016  1 30.91 ? 210 ASP A C     1 
ATOM   1740  O  O     . ASP A 1 210 ? 4.772   -17.236 18.433  1 31.09 ? 210 ASP A O     1 
ATOM   1741  C  CB    . ASP A 1 210 ? 5.215   -16.402 21.446  1 33.84 ? 210 ASP A CB    1 
ATOM   1742  C  CG    . ASP A 1 210 ? 5.141   -17.054 22.815  1 38.97 ? 210 ASP A CG    1 
ATOM   1743  O  OD1   . ASP A 1 210 ? 5.396   -18.279 22.912  1 39.68 ? 210 ASP A OD1   1 
ATOM   1744  O  OD2   . ASP A 1 210 ? 4.815   -16.351 23.784  1 41.44 ? 210 ASP A OD2   1 
ATOM   1745  N  N     . ILE A 1 211 ? 6.57    -15.878 18.446  1 29.75 ? 211 ILE A N     1 
ATOM   1746  C  CA    . ILE A 1 211 ? 6.391   -15.456 17.058  1 29.08 ? 211 ILE A CA    1 
ATOM   1747  C  C     . ILE A 1 211 ? 6.746   -16.614 16.132  1 27.68 ? 211 ILE A C     1 
ATOM   1748  O  O     . ILE A 1 211 ? 5.997   -16.899 15.202  1 27.53 ? 211 ILE A O     1 
ATOM   1749  C  CB    . ILE A 1 211 ? 7.18    -14.157 16.745  1 29.97 ? 211 ILE A CB    1 
ATOM   1750  C  CG1   . ILE A 1 211 ? 6.505   -12.944 17.4    1 31.14 ? 211 ILE A CG1   1 
ATOM   1751  C  CG2   . ILE A 1 211 ? 7.346   -13.927 15.237  1 30.57 ? 211 ILE A CG2   1 
ATOM   1752  C  CD1   . ILE A 1 211 ? 5.073   -12.711 16.955  1 32.58 ? 211 ILE A CD1   1 
ATOM   1753  N  N     . ALA A 1 212 ? 7.847   -17.324 16.428  1 26.62 ? 212 ALA A N     1 
ATOM   1754  C  CA    . ALA A 1 212 ? 8.26    -18.494 15.659  1 26.22 ? 212 ALA A CA    1 
ATOM   1755  C  C     . ALA A 1 212 ? 7.174   -19.577 15.716  1 25.7  ? 212 ALA A C     1 
ATOM   1756  O  O     . ALA A 1 212 ? 6.81    -20.12  14.679  1 25.96 ? 212 ALA A O     1 
ATOM   1757  C  CB    . ALA A 1 212 ? 9.58    -19.038 16.193  1 26.24 ? 212 ALA A CB    1 
ATOM   1758  N  N     . ASP A 1 213 ? 6.607   -19.824 16.911  1 24.86 ? 213 ASP A N     1 
ATOM   1759  C  CA    . ASP A 1 213 ? 5.539   -20.8   17.13   1 24.78 ? 213 ASP A CA    1 
ATOM   1760  C  C     . ASP A 1 213 ? 4.286   -20.44  16.346  1 24.65 ? 213 ASP A C     1 
ATOM   1761  O  O     . ASP A 1 213 ? 3.651   -21.316 15.773  1 24.6  ? 213 ASP A O     1 
ATOM   1762  C  CB    . ASP A 1 213 ? 5.191   -20.906 18.629  1 26.23 ? 213 ASP A CB    1 
ATOM   1763  C  CG    . ASP A 1 213 ? 6.212   -21.642 19.475  1 29.89 ? 213 ASP A CG    1 
ATOM   1764  O  OD1   . ASP A 1 213 ? 7.122   -22.271 18.895  1 30.5  ? 213 ASP A OD1   1 
ATOM   1765  O  OD2   . ASP A 1 213 ? 6.107   -21.58  20.717  1 31.53 ? 213 ASP A OD2   1 
ATOM   1766  N  N     . TYR A 1 214 ? 3.927   -19.158 16.326  1 24.75 ? 214 TYR A N     1 
ATOM   1767  C  CA    . TYR A 1 214 ? 2.757   -18.681 15.604  1 25.49 ? 214 TYR A CA    1 
ATOM   1768  C  C     . TYR A 1 214 ? 2.921   -18.934 14.105  1 25.72 ? 214 TYR A C     1 
ATOM   1769  O  O     . TYR A 1 214 ? 2.011   -19.474 13.48   1 25.97 ? 214 TYR A O     1 
ATOM   1770  C  CB    . TYR A 1 214 ? 2.518   -17.178 15.882  1 25.89 ? 214 TYR A CB    1 
ATOM   1771  C  CG    . TYR A 1 214 ? 1.388   -16.604 15.061  1 27.1  ? 214 TYR A CG    1 
ATOM   1772  C  CD1   . TYR A 1 214 ? 0.067   -16.863 15.39   1 28.15 ? 214 TYR A CD1   1 
ATOM   1773  C  CD2   . TYR A 1 214 ? 1.641   -15.869 13.909  1 28.23 ? 214 TYR A CD2   1 
ATOM   1774  C  CE1   . TYR A 1 214 ? -0.975  -16.381 14.614  1 29.14 ? 214 TYR A CE1   1 
ATOM   1775  C  CE2   . TYR A 1 214 ? 0.605   -15.393 13.117  1 29.18 ? 214 TYR A CE2   1 
ATOM   1776  C  CZ    . TYR A 1 214 ? -0.703  -15.65  13.477  1 30.06 ? 214 TYR A CZ    1 
ATOM   1777  O  OH    . TYR A 1 214 ? -1.741  -15.18  12.722  1 31.46 ? 214 TYR A OH    1 
ATOM   1778  N  N     . ILE A 1 215 ? 4.072   -18.538 13.533  1 25.38 ? 215 ILE A N     1 
ATOM   1779  C  CA    . ILE A 1 215 ? 4.345   -18.708 12.114  1 25.64 ? 215 ILE A CA    1 
ATOM   1780  C  C     . ILE A 1 215 ? 4.291   -20.175 11.715  1 25.88 ? 215 ILE A C     1 
ATOM   1781  O  O     . ILE A 1 215 ? 3.561   -20.519 10.791  1 26.29 ? 215 ILE A O     1 
ATOM   1782  C  CB    . ILE A 1 215 ? 5.676   -18.028 11.707  1 26.09 ? 215 ILE A CB    1 
ATOM   1783  C  CG1   . ILE A 1 215 ? 5.612   -16.508 11.929  1 26.94 ? 215 ILE A CG1   1 
ATOM   1784  C  CG2   . ILE A 1 215 ? 6.04    -18.343 10.265  1 26.39 ? 215 ILE A CG2   1 
ATOM   1785  C  CD1   . ILE A 1 215 ? 6.951   -15.823 11.839  1 28.06 ? 215 ILE A CD1   1 
ATOM   1786  N  N     . ILE A 1 216 ? 4.987   -21.044 12.451  1 25.55 ? 216 ILE A N     1 
ATOM   1787  C  CA    . ILE A 1 216 ? 4.985   -22.469 12.146  1 25.92 ? 216 ILE A CA    1 
ATOM   1788  C  C     . ILE A 1 216 ? 3.584   -23.08  12.232  1 26.74 ? 216 ILE A C     1 
ATOM   1789  O  O     . ILE A 1 216 ? 3.212   -23.849 11.346  1 27    ? 216 ILE A O     1 
ATOM   1790  C  CB    . ILE A 1 216 ? 6.02    -23.217 13.002  1 26.04 ? 216 ILE A CB    1 
ATOM   1791  C  CG1   . ILE A 1 216 ? 7.424   -22.702 12.672  1 26.8  ? 216 ILE A CG1   1 
ATOM   1792  C  CG2   . ILE A 1 216 ? 5.942   -24.721 12.773  1 26.36 ? 216 ILE A CG2   1 
ATOM   1793  C  CD1   . ILE A 1 216 ? 8.418   -23.046 13.663  1 27.95 ? 216 ILE A CD1   1 
ATOM   1794  N  N     . ALA A 1 217 ? 2.781   -22.687 13.23   1 27.16 ? 217 ALA A N     1 
ATOM   1795  C  CA    . ALA A 1 217 ? 1.414   -23.207 13.351  1 28.36 ? 217 ALA A CA    1 
ATOM   1796  C  C     . ALA A 1 217 ? 0.522   -22.751 12.193  1 29.39 ? 217 ALA A C     1 
ATOM   1797  O  O     . ALA A 1 217 ? -0.311  -23.526 11.72   1 29.75 ? 217 ALA A O     1 
ATOM   1798  C  CB    . ALA A 1 217 ? 0.801   -22.805 14.681  1 28.6  ? 217 ALA A CB    1 
ATOM   1799  N  N     . LYS A 1 218 ? 0.714   -21.518 11.713  1 29.72 ? 218 LYS A N     1 
ATOM   1800  C  CA    . LYS A 1 218 ? -0.049  -21.012 10.573  1 30.49 ? 218 LYS A CA    1 
ATOM   1801  C  C     . LYS A 1 218 ? 0.332   -21.783 9.315   1 31.05 ? 218 LYS A C     1 
ATOM   1802  O  O     . LYS A 1 218 ? -0.555  -22.194 8.572   1 30.92 ? 218 LYS A O     1 
ATOM   1803  C  CB    . LYS A 1 218 ? 0.201   -19.511 10.372  1 32.14 ? 218 LYS A CB    1 
ATOM   1804  C  CG    . LYS A 1 218 ? -0.871  -18.627 10.982  1 35.96 ? 218 LYS A CG    1 
ATOM   1805  C  CD    . LYS A 1 218 ? -2.155  -18.721 10.175  1 40.07 ? 218 LYS A CD    1 
ATOM   1806  C  CE    . LYS A 1 218 ? -3.04   -17.519 10.381  1 43.48 ? 218 LYS A CE    1 
ATOM   1807  N  NZ    . LYS A 1 218 ? -3.357  -17.285 11.815  1 45.43 ? 218 LYS A NZ    1 
ATOM   1808  N  N     . LEU A 1 219 ? 1.644   -22.029 9.109   1 31.59 ? 219 LEU A N     1 
ATOM   1809  C  CA    . LEU A 1 219 ? 2.164   -22.781 7.961   1 32.68 ? 219 LEU A CA    1 
ATOM   1810  C  C     . LEU A 1 219 ? 1.635   -24.223 7.953   1 33.89 ? 219 LEU A C     1 
ATOM   1811  O  O     . LEU A 1 219 ? 1.351   -24.776 6.891   1 34.09 ? 219 LEU A O     1 
ATOM   1812  C  CB    . LEU A 1 219 ? 3.7     -22.78  7.967   1 32.79 ? 219 LEU A CB    1 
ATOM   1813  C  CG    . LEU A 1 219 ? 4.379   -21.424 7.786   1 34.24 ? 219 LEU A CG    1 
ATOM   1814  C  CD1   . LEU A 1 219 ? 5.868   -21.526 7.991   1 34.87 ? 219 LEU A CD1   1 
ATOM   1815  C  CD2   . LEU A 1 219 ? 4.097   -20.848 6.431   1 34.8  ? 219 LEU A CD2   1 
ATOM   1816  N  N     . GLN A 1 220 ? 1.474   -24.815 9.141   1 34.42 ? 220 GLN A N     1 
ATOM   1817  C  CA    . GLN A 1 220 ? 0.947   -26.164 9.307   1 35.42 ? 220 GLN A CA    1 
ATOM   1818  C  C     . GLN A 1 220 ? -0.593  -26.237 9.289   1 36.13 ? 220 GLN A C     1 
ATOM   1819  O  O     . GLN A 1 220 ? -1.137  -27.338 9.38    1 36.4  ? 220 GLN A O     1 
ATOM   1820  C  CB    . GLN A 1 220 ? 1.437   -26.728 10.645  1 37.47 ? 220 GLN A CB    1 
ATOM   1821  C  CG    . GLN A 1 220 ? 2.915   -27.09  10.666  1 41.68 ? 220 GLN A CG    1 
ATOM   1822  C  CD    . GLN A 1 220 ? 3.209   -28.503 10.192  1 47.26 ? 220 GLN A CD    1 
ATOM   1823  O  OE1   . GLN A 1 220 ? 4.368   -28.896 10.004  1 49    ? 220 GLN A OE1   1 
ATOM   1824  N  NE2   . GLN A 1 220 ? 2.177   -29.324 10.016  1 48.3  ? 220 GLN A NE2   1 
ATOM   1825  N  N     . HIS A 1 221 ? -1.284  -25.088 9.203   1 36.34 ? 221 HIS A N     1 
ATOM   1826  C  CA    . HIS A 1 221 ? -2.739  -24.96  9.267   1 37.01 ? 221 HIS A CA    1 
ATOM   1827  C  C     . HIS A 1 221 ? -3.285  -25.593 10.534  1 36.67 ? 221 HIS A C     1 
ATOM   1828  O  O     . HIS A 1 221 ? -4.075  -26.534 10.477  1 36.86 ? 221 HIS A O     1 
ATOM   1829  C  CB    . HIS A 1 221 ? -3.479  -25.451 8.008   1 38.66 ? 221 HIS A CB    1 
ATOM   1830  C  CG    . HIS A 1 221 ? -4.909  -24.985 7.969   1 42.08 ? 221 HIS A CG    1 
ATOM   1831  N  ND1   . HIS A 1 221 ? -5.231  -23.643 7.8     1 44.18 ? 221 HIS A ND1   1 
ATOM   1832  C  CD2   . HIS A 1 221 ? -6.056  -25.687 8.139   1 43.44 ? 221 HIS A CD2   1 
ATOM   1833  C  CE1   . HIS A 1 221 ? -6.553  -23.578 7.853   1 44.72 ? 221 HIS A CE1   1 
ATOM   1834  N  NE2   . HIS A 1 221 ? -7.095  -24.78  8.059   1 44.64 ? 221 HIS A NE2   1 
ATOM   1835  N  N     . ARG A 1 222 ? -2.807  -25.111 11.679  1 36    ? 222 ARG A N     1 
ATOM   1836  C  CA    . ARG A 1 222 ? -3.244  -25.589 12.985  1 35.72 ? 222 ARG A CA    1 
ATOM   1837  C  C     . ARG A 1 222 ? -3.96   -24.464 13.739  1 35.66 ? 222 ARG A C     1 
ATOM   1838  O  O     . ARG A 1 222 ? -3.878  -23.303 13.328  1 36    ? 222 ARG A O     1 
ATOM   1839  C  CB    . ARG A 1 222 ? -2.04   -26.093 13.789  1 36.54 ? 222 ARG A CB    1 
ATOM   1840  C  CG    . ARG A 1 222 ? -1.437  -27.339 13.201  1 38.82 ? 222 ARG A CG    1 
ATOM   1841  C  CD    . ARG A 1 222 ? -0.189  -27.764 13.925  1 41.57 ? 222 ARG A CD    1 
ATOM   1842  N  NE    . ARG A 1 222 ? 0.225   -29.086 13.462  1 44.93 ? 222 ARG A NE    1 
ATOM   1843  C  CZ    . ARG A 1 222 ? 1.47    -29.541 13.502  1 47.55 ? 222 ARG A CZ    1 
ATOM   1844  N  NH1   . ARG A 1 222 ? 2.45    -28.775 13.97   1 47.28 ? 222 ARG A NH1   1 
ATOM   1845  N  NH2   . ARG A 1 222 ? 1.753   -30.755 13.048  1 47.65 ? 222 ARG A NH2   1 
ATOM   1846  N  N     . ASP A 1 223 ? -4.668  -24.794 14.833  1 35.1  ? 223 ASP A N     1 
ATOM   1847  C  CA    . ASP A 1 223 ? -5.351  -23.774 15.624  1 35.02 ? 223 ASP A CA    1 
ATOM   1848  C  C     . ASP A 1 223 ? -4.325  -22.896 16.32   1 34.56 ? 223 ASP A C     1 
ATOM   1849  O  O     . ASP A 1 223 ? -3.526  -23.384 17.116  1 34.53 ? 223 ASP A O     1 
ATOM   1850  C  CB    . ASP A 1 223 ? -6.315  -24.393 16.649  1 36.74 ? 223 ASP A CB    1 
ATOM   1851  C  CG    . ASP A 1 223 ? -7.031  -23.356 17.501  1 41.5  ? 223 ASP A CG    1 
ATOM   1852  O  OD1   . ASP A 1 223 ? -7.395  -22.29  16.96   1 41.86 ? 223 ASP A OD1   1 
ATOM   1853  O  OD2   . ASP A 1 223 ? -7.182  -23.589 18.719  1 44.32 ? 223 ASP A OD2   1 
ATOM   1854  N  N     . THR A 1 224 ? -4.349  -21.6   16.009  1 34.13 ? 224 THR A N     1 
ATOM   1855  C  CA    . THR A 1 224 ? -3.428  -20.641 16.604  1 34.16 ? 224 THR A CA    1 
ATOM   1856  C  C     . THR A 1 224 ? -4.051  -19.825 17.752  1 33.87 ? 224 THR A C     1 
ATOM   1857  O  O     . THR A 1 224 ? -3.4    -18.908 18.23   1 33.91 ? 224 THR A O     1 
ATOM   1858  C  CB    . THR A 1 224 ? -2.848  -19.708 15.522  1 35.26 ? 224 THR A CB    1 
ATOM   1859  O  OG1   . THR A 1 224 ? -3.913  -19.151 14.75   1 36.06 ? 224 THR A OG1   1 
ATOM   1860  C  CG2   . THR A 1 224 ? -1.871  -20.409 14.61   1 35.59 ? 224 THR A CG2   1 
ATOM   1861  N  N     . SER A 1 225 ? -5.284  -20.145 18.196  1 33.27 ? 225 SER A N     1 
ATOM   1862  C  CA    . SER A 1 225 ? -5.971  -19.41  19.265  1 33.06 ? 225 SER A CA    1 
ATOM   1863  C  C     . SER A 1 225 ? -5.155  -19.278 20.536  1 32.33 ? 225 SER A C     1 
ATOM   1864  O  O     . SER A 1 225 ? -5.128  -18.207 21.132  1 32.29 ? 225 SER A O     1 
ATOM   1865  C  CB    . SER A 1 225 ? -7.316  -20.053 19.588  1 34.78 ? 225 SER A CB    1 
ATOM   1866  O  OG    . SER A 1 225 ? -8.189  -19.986 18.475  1 37.78 ? 225 SER A OG    1 
ATOM   1867  N  N     . ASN A 1 226 ? -4.492  -20.361 20.955  1 31.81 ? 226 ASN A N     1 
ATOM   1868  C  CA    . ASN A 1 226 ? -3.676  -20.354 22.164  1 31.75 ? 226 ASN A CA    1 
ATOM   1869  C  C     . ASN A 1 226 ? -2.457  -19.448 22.013  1 30.93 ? 226 ASN A C     1 
ATOM   1870  O  O     . ASN A 1 226 ? -2.185  -18.652 22.911  1 30.82 ? 226 ASN A O     1 
ATOM   1871  C  CB    . ASN A 1 226 ? -3.258  -21.78  22.546  1 33.28 ? 226 ASN A CB    1 
ATOM   1872  C  CG    . ASN A 1 226 ? -4.403  -22.65  23.004  1 37.15 ? 226 ASN A CG    1 
ATOM   1873  O  OD1   . ASN A 1 226 ? -5.491  -22.171 23.354  1 38.47 ? 226 ASN A OD1   1 
ATOM   1874  N  ND2   . ASN A 1 226 ? -4.179  -23.954 23.022  1 38.11 ? 226 ASN A ND2   1 
ATOM   1875  N  N     . ILE A 1 227 ? -1.739  -19.553 20.872  1 30.16 ? 227 ILE A N     1 
ATOM   1876  C  CA    . ILE A 1 227 ? -0.559  -18.724 20.593  1 29.6  ? 227 ILE A CA    1 
ATOM   1877  C  C     . ILE A 1 227 ? -0.961  -17.265 20.475  1 28.67 ? 227 ILE A C     1 
ATOM   1878  O  O     . ILE A 1 227 ? -0.269  -16.394 20.997  1 28.68 ? 227 ILE A O     1 
ATOM   1879  C  CB    . ILE A 1 227 ? 0.22    -19.198 19.34   1 30.13 ? 227 ILE A CB    1 
ATOM   1880  C  CG1   . ILE A 1 227 ? 0.452   -20.715 19.371  1 31.29 ? 227 ILE A CG1   1 
ATOM   1881  C  CG2   . ILE A 1 227 ? 1.544   -18.449 19.214  1 30.57 ? 227 ILE A CG2   1 
ATOM   1882  C  CD1   . ILE A 1 227 ? 1.023   -21.27  18.094  1 32.8  ? 227 ILE A CD1   1 
ATOM   1883  N  N     . GLU A 1 228 ? -2.11   -16.998 19.84   1 27.73 ? 228 GLU A N     1 
ATOM   1884  C  CA    . GLU A 1 228 ? -2.636  -15.652 19.689  1 27.3  ? 228 GLU A CA    1 
ATOM   1885  C  C     . GLU A 1 228 ? -2.912  -15.045 21.052  1 27.8  ? 228 GLU A C     1 
ATOM   1886  O  O     . GLU A 1 228 ? -2.497  -13.922 21.289  1 28.07 ? 228 GLU A O     1 
ATOM   1887  C  CB    . GLU A 1 228 ? -3.897  -15.639 18.807  1 27.54 ? 228 GLU A CB    1 
ATOM   1888  C  CG    . GLU A 1 228 ? -3.608  -15.879 17.331  1 27.38 ? 228 GLU A CG    1 
ATOM   1889  C  CD    . GLU A 1 228 ? -4.827  -15.971 16.434  1 27.07 ? 228 GLU A CD    1 
ATOM   1890  O  OE1   . GLU A 1 228 ? -5.778  -15.183 16.633  1 25.77 ? 228 GLU A OE1   1 
ATOM   1891  O  OE2   . GLU A 1 228 ? -4.822  -16.812 15.51   1 28.12 ? 228 GLU A OE2   1 
ATOM   1892  N  N     . GLN A 1 229 ? -3.519  -15.805 21.981  1 27.84 ? 229 GLN A N     1 
ATOM   1893  C  CA    . GLN A 1 229 ? -3.777  -15.307 23.33   1 28.31 ? 229 GLN A CA    1 
ATOM   1894  C  C     . GLN A 1 229 ? -2.502  -15.001 24.106  1 28.27 ? 229 GLN A C     1 
ATOM   1895  O  O     . GLN A 1 229 ? -2.471  -14.026 24.846  1 28.48 ? 229 GLN A O     1 
ATOM   1896  C  CB    . GLN A 1 229 ? -4.69   -16.252 24.123  1 30.26 ? 229 GLN A CB    1 
ATOM   1897  C  CG    . GLN A 1 229 ? -6.112  -15.716 24.303  1 34.29 ? 229 GLN A CG    1 
ATOM   1898  C  CD    . GLN A 1 229 ? -6.153  -14.338 24.96   1 39.29 ? 229 GLN A CD    1 
ATOM   1899  O  OE1   . GLN A 1 229 ? -6.689  -13.367 24.402  1 40.8  ? 229 GLN A OE1   1 
ATOM   1900  N  NE2   . GLN A 1 229 ? -5.578  -14.22  26.149  1 40.03 ? 229 GLN A NE2   1 
ATOM   1901  N  N     . LEU A 1 230 ? -1.448  -15.803 23.919  1 27.99 ? 230 LEU A N     1 
ATOM   1902  C  CA    . LEU A 1 230 ? -0.17   -15.563 24.583  1 28.31 ? 230 LEU A CA    1 
ATOM   1903  C  C     . LEU A 1 230 ? 0.433   -14.264 24.067  1 28.11 ? 230 LEU A C     1 
ATOM   1904  O  O     . LEU A 1 230 ? 0.914   -13.46  24.865  1 28.29 ? 230 LEU A O     1 
ATOM   1905  C  CB    . LEU A 1 230 ? 0.815   -16.721 24.347  1 28.95 ? 230 LEU A CB    1 
ATOM   1906  C  CG    . LEU A 1 230 ? 0.501   -18.056 25.043  1 31.12 ? 230 LEU A CG    1 
ATOM   1907  C  CD1   . LEU A 1 230 ? 1.537   -19.115 24.688  1 31.93 ? 230 LEU A CD1   1 
ATOM   1908  C  CD2   . LEU A 1 230 ? 0.445   -17.896 26.543  1 31.9  ? 230 LEU A CD2   1 
ATOM   1909  N  N     . LEU A 1 231 ? 0.364   -14.036 22.742  1 27.61 ? 231 LEU A N     1 
ATOM   1910  C  CA    . LEU A 1 231 ? 0.876   -12.818 22.109  1 27.61 ? 231 LEU A CA    1 
ATOM   1911  C  C     . LEU A 1 231 ? 0.058   -11.563 22.476  1 27.65 ? 231 LEU A C     1 
ATOM   1912  O  O     . LEU A 1 231 ? 0.64    -10.492 22.664  1 28.09 ? 231 LEU A O     1 
ATOM   1913  C  CB    . LEU A 1 231 ? 0.976   -12.998 20.593  1 27.62 ? 231 LEU A CB    1 
ATOM   1914  C  CG    . LEU A 1 231 ? 2.07    -13.959 20.146  1 28.84 ? 231 LEU A CG    1 
ATOM   1915  C  CD1   . LEU A 1 231 ? 1.896   -14.35  18.704  1 29.08 ? 231 LEU A CD1   1 
ATOM   1916  C  CD2   . LEU A 1 231 ? 3.436   -13.357 20.364  1 29.6  ? 231 LEU A CD2   1 
ATOM   1917  N  N     . ILE A 1 232 ? -1.276  -11.696 22.601  1 26.94 ? 232 ILE A N     1 
ATOM   1918  C  CA    . ILE A 1 232 ? -2.15   -10.6   23.022  1 26.72 ? 232 ILE A CA    1 
ATOM   1919  C  C     . ILE A 1 232 ? -1.821  -10.253 24.472  1 26.59 ? 232 ILE A C     1 
ATOM   1920  O  O     . ILE A 1 232 ? -1.705  -9.078  24.799  1 26.31 ? 232 ILE A O     1 
ATOM   1921  C  CB    . ILE A 1 232 ? -3.644  -10.979 22.861  1 27.16 ? 232 ILE A CB    1 
ATOM   1922  C  CG1   . ILE A 1 232 ? -4.026  -11.172 21.391  1 28.21 ? 232 ILE A CG1   1 
ATOM   1923  C  CG2   . ILE A 1 232 ? -4.559  -9.965  23.521  1 27.6  ? 232 ILE A CG2   1 
ATOM   1924  C  CD1   . ILE A 1 232 ? -3.77   -9.994  20.516  1 29.79 ? 232 ILE A CD1   1 
ATOM   1925  N  N     . ASN A 1 233 ? -1.612  -11.274 25.33   1 26.64 ? 233 ASN A N     1 
ATOM   1926  C  CA    . ASN A 1 233 ? -1.257  -11.069 26.734  1 27.13 ? 233 ASN A CA    1 
ATOM   1927  C  C     . ASN A 1 233 ? 0.074   -10.332 26.889  1 26.72 ? 233 ASN A C     1 
ATOM   1928  O  O     . ASN A 1 233 ? 0.202   -9.506  27.788  1 26.91 ? 233 ASN A O     1 
ATOM   1929  C  CB    . ASN A 1 233 ? -1.251  -12.385 27.513  1 28.91 ? 233 ASN A CB    1 
ATOM   1930  C  CG    . ASN A 1 233 ? -2.634  -12.895 27.853  1 32.53 ? 233 ASN A CG    1 
ATOM   1931  O  OD1   . ASN A 1 233 ? -3.64   -12.189 27.716  1 33.54 ? 233 ASN A OD1   1 
ATOM   1932  N  ND2   . ASN A 1 233 ? -2.714  -14.144 28.289  1 33.25 ? 233 ASN A ND2   1 
ATOM   1933  N  N     . LYS A 1 234 ? 1.044   -10.592 26.002  1 25.95 ? 234 LYS A N     1 
ATOM   1934  C  CA    . LYS A 1 234 ? 2.323   -9.881  26.042  1 25.71 ? 234 LYS A CA    1 
ATOM   1935  C  C     . LYS A 1 234 ? 2.165   -8.432  25.569  1 25.9  ? 234 LYS A C     1 
ATOM   1936  O  O     . LYS A 1 234 ? 2.795   -7.528  26.122  1 26.14 ? 234 LYS A O     1 
ATOM   1937  C  CB    . LYS A 1 234 ? 3.38    -10.613 25.22   1 26.57 ? 234 LYS A CB    1 
ATOM   1938  C  CG    . LYS A 1 234 ? 3.735   -11.947 25.832  1 28.72 ? 234 LYS A CG    1 
ATOM   1939  C  CD    . LYS A 1 234 ? 4.782   -12.646 25.046  1 31.36 ? 234 LYS A CD    1 
ATOM   1940  C  CE    . LYS A 1 234 ? 5.097   -13.953 25.686  1 34.29 ? 234 LYS A CE    1 
ATOM   1941  N  NZ    . LYS A 1 234 ? 6.371   -14.492 25.164  1 36.82 ? 234 LYS A NZ    1 
ATOM   1942  N  N     . ASN A 1 235 ? 1.289   -8.203  24.587  1 25.61 ? 235 ASN A N     1 
ATOM   1943  C  CA    . ASN A 1 235 ? 0.969   -6.862  24.105  1 25.85 ? 235 ASN A CA    1 
ATOM   1944  C  C     . ASN A 1 235 ? 0.286   -6.082  25.245  1 25.33 ? 235 ASN A C     1 
ATOM   1945  O  O     . ASN A 1 235 ? 0.59    -4.915  25.444  1 25.26 ? 235 ASN A O     1 
ATOM   1946  C  CB    . ASN A 1 235 ? 0.045   -6.957  22.883  1 27.55 ? 235 ASN A CB    1 
ATOM   1947  C  CG    . ASN A 1 235 ? -0.07   -5.692  22.062  1 31.03 ? 235 ASN A CG    1 
ATOM   1948  O  OD1   . ASN A 1 235 ? 0.135   -4.577  22.548  1 31.88 ? 235 ASN A OD1   1 
ATOM   1949  N  ND2   . ASN A 1 235 ? -0.412  -5.84   20.788  1 31.82 ? 235 ASN A ND2   1 
ATOM   1950  N  N     . LEU A 1 236 ? -0.595  -6.743  26.018  1 24.99 ? 236 LEU A N     1 
ATOM   1951  C  CA    . LEU A 1 236 ? -1.287  -6.151  27.165  1 25.07 ? 236 LEU A CA    1 
ATOM   1952  C  C     . LEU A 1 236 ? -0.306  -5.853  28.298  1 25.21 ? 236 LEU A C     1 
ATOM   1953  O  O     . LEU A 1 236 ? -0.395  -4.805  28.928  1 25.15 ? 236 LEU A O     1 
ATOM   1954  C  CB    . LEU A 1 236 ? -2.403  -7.08   27.66   1 24.91 ? 236 LEU A CB    1 
ATOM   1955  C  CG    . LEU A 1 236 ? -3.353  -6.453  28.643  1 25.85 ? 236 LEU A CG    1 
ATOM   1956  C  CD1   . LEU A 1 236 ? -4.153  -5.351  27.987  1 26.49 ? 236 LEU A CD1   1 
ATOM   1957  C  CD2   . LEU A 1 236 ? -4.265  -7.479  29.233  1 26.14 ? 236 LEU A CD2   1 
ATOM   1958  N  N     . LYS A 1 237 ? 0.659   -6.747  28.52   1 25.28 ? 237 LYS A N     1 
ATOM   1959  C  CA    . LYS A 1 237 ? 1.701   -6.561  29.517  1 25.89 ? 237 LYS A CA    1 
ATOM   1960  C  C     . LYS A 1 237 ? 2.576   -5.353  29.179  1 26.47 ? 237 LYS A C     1 
ATOM   1961  O  O     . LYS A 1 237 ? 3.024   -4.662  30.094  1 26.82 ? 237 LYS A O     1 
ATOM   1962  C  CB    . LYS A 1 237 ? 2.549   -7.823  29.643  1 27.77 ? 237 LYS A CB    1 
ATOM   1963  C  CG    . LYS A 1 237 ? 2.005   -8.824  30.653  1 32.07 ? 237 LYS A CG    1 
ATOM   1964  C  CD    . LYS A 1 237 ? 2.318   -8.457  32.146  1 36.35 ? 237 LYS A CD    1 
ATOM   1965  C  CE    . LYS A 1 237 ? 3.705   -7.897  32.372  1 39.39 ? 237 LYS A CE    1 
ATOM   1966  N  NZ    . LYS A 1 237 ? 3.856   -7.303  33.723  1 41.39 ? 237 LYS A NZ    1 
ATOM   1967  N  N     . MET A 1 238 ? 2.79    -5.064  27.881  1 26.46 ? 238 MET A N     1 
ATOM   1968  C  CA    . MET A 1 238 ? 3.543   -3.877  27.493  1 27.21 ? 238 MET A CA    1 
ATOM   1969  C  C     . MET A 1 238 ? 2.734   -2.617  27.813  1 28.11 ? 238 MET A C     1 
ATOM   1970  O  O     . MET A 1 238 ? 3.306   -1.626  28.271  1 28.62 ? 238 MET A O     1 
ATOM   1971  C  CB    . MET A 1 238 ? 3.916   -3.904  26.012  1 27.55 ? 238 MET A CB    1 
ATOM   1972  C  CG    . MET A 1 238 ? 4.655   -2.658  25.554  1 28.66 ? 238 MET A CG    1 
ATOM   1973  S  SD    . MET A 1 238 ? 6.232   -2.421  26.399  1 29.7  ? 238 MET A SD    1 
ATOM   1974  C  CE    . MET A 1 238 ? 7.214   -3.596  25.555  1 28.3  ? 238 MET A CE    1 
ATOM   1975  N  N     . VAL A 1 239 ? 1.403   -2.655  27.607  1 28.03 ? 239 VAL A N     1 
ATOM   1976  C  CA    . VAL A 1 239 ? 0.51    -1.543  27.95   1 28.32 ? 239 VAL A CA    1 
ATOM   1977  C  C     . VAL A 1 239 ? 0.594   -1.274  29.46   1 29.18 ? 239 VAL A C     1 
ATOM   1978  O  O     . VAL A 1 239 ? 0.677   -0.126  29.878  1 29.52 ? 239 VAL A O     1 
ATOM   1979  C  CB    . VAL A 1 239 ? -0.942  -1.832  27.503  1 28.47 ? 239 VAL A CB    1 
ATOM   1980  C  CG1   . VAL A 1 239 ? -1.897  -0.771  28.016  1 28.8  ? 239 VAL A CG1   1 
ATOM   1981  C  CG2   . VAL A 1 239 ? -1.031  -1.932  25.994  1 28.82 ? 239 VAL A CG2   1 
ATOM   1982  N  N     . GLU A 1 240 ? 0.648   -2.346  30.264  1 29.49 ? 240 GLU A N     1 
ATOM   1983  C  CA    . GLU A 1 240 ? 0.798   -2.273  31.71   1 30.13 ? 240 GLU A CA    1 
ATOM   1984  C  C     . GLU A 1 240 ? 2.127   -1.614  32.063  1 30.54 ? 240 GLU A C     1 
ATOM   1985  O  O     . GLU A 1 240 ? 2.137   -0.668  32.838  1 30.57 ? 240 GLU A O     1 
ATOM   1986  C  CB    . GLU A 1 240 ? 0.701   -3.679  32.335  1 32.37 ? 240 GLU A CB    1 
ATOM   1987  C  CG    . GLU A 1 240 ? 0.448   -3.666  33.832  1 36.87 ? 240 GLU A CG    1 
ATOM   1988  C  CD    . GLU A 1 240 ? 1.577   -4.195  34.694  1 42.03 ? 240 GLU A CD    1 
ATOM   1989  O  OE1   . GLU A 1 240 ? 2.741   -3.811  34.445  1 42.46 ? 240 GLU A OE1   1 
ATOM   1990  O  OE2   . GLU A 1 240 ? 1.297   -4.974  35.633  1 44.33 ? 240 GLU A OE2   1 
ATOM   1991  N  N     . PHE A 1 241 ? 3.24    -2.079  31.469  1 30.76 ? 241 PHE A N     1 
ATOM   1992  C  CA    . PHE A 1 241 ? 4.564   -1.512  31.726  1 31.41 ? 241 PHE A CA    1 
ATOM   1993  C  C     . PHE A 1 241 ? 4.618   -0.014  31.448  1 31.98 ? 241 PHE A C     1 
ATOM   1994  O  O     . PHE A 1 241 ? 5.125   0.745   32.269  1 31.99 ? 241 PHE A O     1 
ATOM   1995  C  CB    . PHE A 1 241 ? 5.651   -2.245  30.909  1 31.21 ? 241 PHE A CB    1 
ATOM   1996  C  CG    . PHE A 1 241 ? 7.001   -1.558  30.942  1 31.68 ? 241 PHE A CG    1 
ATOM   1997  C  CD1   . PHE A 1 241 ? 7.751   -1.523  32.102  1 32.34 ? 241 PHE A CD1   1 
ATOM   1998  C  CD2   . PHE A 1 241 ? 7.489   -0.896  29.832  1 32.49 ? 241 PHE A CD2   1 
ATOM   1999  C  CE1   . PHE A 1 241 ? 8.982   -0.883  32.139  1 32.95 ? 241 PHE A CE1   1 
ATOM   2000  C  CE2   . PHE A 1 241 ? 8.714   -0.241  29.878  1 33.21 ? 241 PHE A CE2   1 
ATOM   2001  C  CZ    . PHE A 1 241 ? 9.45    -0.234  31.034  1 32.87 ? 241 PHE A CZ    1 
ATOM   2002  N  N     . LEU A 1 242 ? 4.125   0.397   30.283  1 32.3  ? 242 LEU A N     1 
ATOM   2003  C  CA    . LEU A 1 242 ? 4.163   1.788   29.878  1 33.21 ? 242 LEU A CA    1 
ATOM   2004  C  C     . LEU A 1 242 ? 3.221   2.685   30.68   1 34.54 ? 242 LEU A C     1 
ATOM   2005  O  O     . LEU A 1 242 ? 3.627   3.774   31.084  1 34.99 ? 242 LEU A O     1 
ATOM   2006  C  CB    . LEU A 1 242 ? 3.875   1.898   28.383  1 33.27 ? 242 LEU A CB    1 
ATOM   2007  C  CG    . LEU A 1 242 ? 4.858   1.175   27.466  1 34.39 ? 242 LEU A CG    1 
ATOM   2008  C  CD1   . LEU A 1 242 ? 4.355   1.163   26.052  1 34.79 ? 242 LEU A CD1   1 
ATOM   2009  C  CD2   . LEU A 1 242 ? 6.249   1.797   27.533  1 34.86 ? 242 LEU A CD2   1 
ATOM   2010  N  N     . SER A 1 243 ? 1.98    2.236   30.931  1 34.92 ? 243 SER A N     1 
ATOM   2011  C  CA    . SER A 1 243 ? 1.012   3.049   31.667  1 35.62 ? 243 SER A CA    1 
ATOM   2012  C  C     . SER A 1 243 ? 1.372   3.204   33.137  1 36.67 ? 243 SER A C     1 
ATOM   2013  O  O     . SER A 1 243 ? 1.161   4.277   33.705  1 37.37 ? 243 SER A O     1 
ATOM   2014  C  CB    . SER A 1 243 ? -0.409  2.525   31.486  1 36.48 ? 243 SER A CB    1 
ATOM   2015  O  OG    . SER A 1 243 ? -0.553  1.194   31.953  1 38.5  ? 243 SER A OG    1 
ATOM   2016  N  N     . LYS A 1 244 ? 1.966   2.167   33.745  1 36.68 ? 244 LYS A N     1 
ATOM   2017  C  CA    . LYS A 1 244 ? 2.404   2.262   35.137  1 37.1  ? 244 LYS A CA    1 
ATOM   2018  C  C     . LYS A 1 244 ? 3.673   3.128   35.312  1 38.13 ? 244 LYS A C     1 
ATOM   2019  O  O     . LYS A 1 244 ? 4.018   3.481   36.433  1 38.31 ? 244 LYS A O     1 
ATOM   2020  C  CB    . LYS A 1 244 ? 2.563   0.876   35.766  1 38.08 ? 244 LYS A CB    1 
ATOM   2021  C  CG    . LYS A 1 244 ? 1.238   0.139   35.928  1 40.96 ? 244 LYS A CG    1 
ATOM   2022  C  CD    . LYS A 1 244 ? 1.435   -1.245  36.537  1 44.5  ? 244 LYS A CD    1 
ATOM   2023  C  CE    . LYS A 1 244 ? 1.273   -1.287  38.036  1 47.93 ? 244 LYS A CE    1 
ATOM   2024  N  NZ    . LYS A 1 244 ? 1.822   -2.54   38.626  1 49.55 ? 244 LYS A NZ    1 
ATOM   2025  N  N     . ASN A 1 245 ? 4.34    3.506   34.212  1 38.76 ? 245 ASN A N     1 
ATOM   2026  C  CA    . ASN A 1 245 ? 5.505   4.382   34.25   1 39.88 ? 245 ASN A CA    1 
ATOM   2027  C  C     . ASN A 1 245 ? 5.175   5.86    33.941  1 40.66 ? 245 ASN A C     1 
ATOM   2028  O  O     . ASN A 1 245 ? 6.064   6.707   34.037  1 41.01 ? 245 ASN A O     1 
ATOM   2029  C  CB    . ASN A 1 245 ? 6.591   3.879   33.307  1 41.25 ? 245 ASN A CB    1 
ATOM   2030  C  CG    . ASN A 1 245 ? 7.637   3.061   34.001  1 44.83 ? 245 ASN A CG    1 
ATOM   2031  O  OD1   . ASN A 1 245 ? 7.883   3.222   35.191  1 46.47 ? 245 ASN A OD1   1 
ATOM   2032  N  ND2   . ASN A 1 245 ? 8.299   2.191   33.274  1 45.42 ? 245 ASN A ND2   1 
ATOM   2033  N  N     . THR A 1 246 ? 3.925   6.179   33.562  1 40.71 ? 246 THR A N     1 
ATOM   2034  C  CA    . THR A 1 246 ? 3.546   7.563   33.265  1 41.17 ? 246 THR A CA    1 
ATOM   2035  C  C     . THR A 1 246 ? 2.743   8.181   34.407  1 41.33 ? 246 THR A C     1 
ATOM   2036  O  O     . THR A 1 246 ? 2.094   7.449   35.157  1 41.39 ? 246 THR A O     1 
ATOM   2037  C  CB    . THR A 1 246 ? 2.736   7.635   31.965  1 42.54 ? 246 THR A CB    1 
ATOM   2038  O  OG1   . THR A 1 246 ? 1.553   6.848   32.106  1 43.51 ? 246 THR A OG1   1 
ATOM   2039  C  CG2   . THR A 1 246 ? 3.531   7.188   30.753  1 43.03 ? 246 THR A CG2   1 
ATOM   2040  N  N     . LYS A 1 247 ? 2.753   9.53    34.513  1 41.23 ? 247 LYS A N     1 
ATOM   2041  C  CA    . LYS A 1 247 ? 1.991   10.269  35.528  1 41.5  ? 247 LYS A CA    1 
ATOM   2042  C  C     . LYS A 1 247 ? 0.514   10.048  35.238  1 41.85 ? 247 LYS A C     1 
ATOM   2043  O  O     . LYS A 1 247 ? 0.05    10.356  34.139  1 41.72 ? 247 LYS A O     1 
ATOM   2044  C  CB    . LYS A 1 247 ? 2.29    11.775  35.459  1 43.22 ? 247 LYS A CB    1 
ATOM   2045  C  CG    . LYS A 1 247 ? 3.754   12.132  35.272  1 47.24 ? 247 LYS A CG    1 
ATOM   2046  C  CD    . LYS A 1 247 ? 3.933   13.278  34.276  1 51.2  ? 247 LYS A CD    1 
ATOM   2047  C  CE    . LYS A 1 247 ? 3.639   12.834  32.867  1 54.84 ? 247 LYS A CE    1 
ATOM   2048  N  NZ    . LYS A 1 247 ? 2.299   13.263  32.377  1 56.96 ? 247 LYS A NZ    1 
ATOM   2049  N  N     . ASN A 1 248 ? -0.217  9.491   36.212  1 42.14 ? 248 ASN A N     1 
ATOM   2050  C  CA    . ASN A 1 248 ? -1.625  9.134   36.058  1 42.7  ? 248 ASN A CA    1 
ATOM   2051  C  C     . ASN A 1 248 ? -2.568  10.334  35.89   1 42.89 ? 248 ASN A C     1 
ATOM   2052  O  O     . ASN A 1 248 ? -3.653  10.154  35.351  1 42.95 ? 248 ASN A O     1 
ATOM   2053  C  CB    . ASN A 1 248 ? -2.081  8.219   37.206  1 43.91 ? 248 ASN A CB    1 
ATOM   2054  C  CG    . ASN A 1 248 ? -1.366  6.866   37.277  1 47.19 ? 248 ASN A CG    1 
ATOM   2055  O  OD1   . ASN A 1 248 ? -1.373  6.198   38.317  1 48.23 ? 248 ASN A OD1   1 
ATOM   2056  N  ND2   . ASN A 1 248 ? -0.736  6.413   36.187  1 47.85 ? 248 ASN A ND2   1 
ATOM   2057  N  N     . ASP A 1 249 ? -2.168  11.545  36.315  1 42.76 ? 249 ASP A N     1 
ATOM   2058  C  CA    . ASP A 1 249 ? -3.043  12.714  36.209  1 43.23 ? 249 ASP A CA    1 
ATOM   2059  C  C     . ASP A 1 249 ? -3.31   13.179  34.774  1 43.48 ? 249 ASP A C     1 
ATOM   2060  O  O     . ASP A 1 249 ? -4.329  13.816  34.539  1 43.58 ? 249 ASP A O     1 
ATOM   2061  C  CB    . ASP A 1 249 ? -2.545  13.88   37.073  1 45.11 ? 249 ASP A CB    1 
ATOM   2062  C  CG    . ASP A 1 249 ? -1.061  14.156  36.972  1 50.11 ? 249 ASP A CG    1 
ATOM   2063  O  OD1   . ASP A 1 249 ? -0.576  14.385  35.84   1 50.81 ? 249 ASP A OD1   1 
ATOM   2064  O  OD2   . ASP A 1 249 ? -0.385  14.158  38.028  1 52.55 ? 249 ASP A OD2   1 
ATOM   2065  N  N     . ASN A 1 250 ? -2.411  12.873  33.822  1 43.36 ? 250 ASN A N     1 
ATOM   2066  C  CA    . ASN A 1 250 ? -2.573  13.274  32.417  1 43.76 ? 250 ASN A CA    1 
ATOM   2067  C  C     . ASN A 1 250 ? -2.66   12.092  31.433  1 43.43 ? 250 ASN A C     1 
ATOM   2068  O  O     . ASN A 1 250 ? -2.765  12.319  30.228  1 43.56 ? 250 ASN A O     1 
ATOM   2069  C  CB    . ASN A 1 250 ? -1.415  14.183  31.977  1 45.37 ? 250 ASN A CB    1 
ATOM   2070  C  CG    . ASN A 1 250 ? -1.592  15.647  32.284  1 48.85 ? 250 ASN A CG    1 
ATOM   2071  O  OD1   . ASN A 1 250 ? -1.564  16.501  31.39   1 50.09 ? 250 ASN A OD1   1 
ATOM   2072  N  ND2   . ASN A 1 250 ? -1.757  15.979  33.549  1 49.66 ? 250 ASN A ND2   1 
ATOM   2073  N  N     . ASN A 1 251 ? -2.547  10.849  31.918  1 42.67 ? 251 ASN A N     1 
ATOM   2074  C  CA    . ASN A 1 251 ? -2.583  9.662   31.062  1 42.36 ? 251 ASN A CA    1 
ATOM   2075  C  C     . ASN A 1 251 ? -3.503  8.593   31.666  1 42.11 ? 251 ASN A C     1 
ATOM   2076  O  O     . ASN A 1 251 ? -3.751  8.611   32.875  1 42.55 ? 251 ASN A O     1 
ATOM   2077  C  CB    . ASN A 1 251 ? -1.175  9.063   30.928  1 42.97 ? 251 ASN A CB    1 
ATOM   2078  C  CG    . ASN A 1 251 ? -0.106  10.016  30.461  1 45.33 ? 251 ASN A CG    1 
ATOM   2079  O  OD1   . ASN A 1 251 ? 0.576   10.674  31.255  1 46.28 ? 251 ASN A OD1   1 
ATOM   2080  N  ND2   . ASN A 1 251 ? 0.088   10.091  29.161  1 45.73 ? 251 ASN A ND2   1 
ATOM   2081  N  N     . PHE A 1 252 ? -3.972  7.634   30.844  1 41.11 ? 252 PHE A N     1 
ATOM   2082  C  CA    . PHE A 1 252 ? -4.805  6.541   31.344  1 40.5  ? 252 PHE A CA    1 
ATOM   2083  C  C     . PHE A 1 252 ? -3.984  5.669   32.288  1 40.06 ? 252 PHE A C     1 
ATOM   2084  O  O     . PHE A 1 252 ? -2.806  5.432   32.032  1 40.02 ? 252 PHE A O     1 
ATOM   2085  C  CB    . PHE A 1 252 ? -5.313  5.649   30.194  1 40.13 ? 252 PHE A CB    1 
ATOM   2086  C  CG    . PHE A 1 252 ? -6.604  6.036   29.506  1 40.44 ? 252 PHE A CG    1 
ATOM   2087  C  CD1   . PHE A 1 252 ? -7.254  7.214   29.825  1 41.24 ? 252 PHE A CD1   1 
ATOM   2088  C  CD2   . PHE A 1 252 ? -7.15   5.233   28.521  1 40.9  ? 252 PHE A CD2   1 
ATOM   2089  C  CE1   . PHE A 1 252 ? -8.43   7.574   29.176  1 41.87 ? 252 PHE A CE1   1 
ATOM   2090  C  CE2   . PHE A 1 252 ? -8.322  5.595   27.875  1 41.53 ? 252 PHE A CE2   1 
ATOM   2091  C  CZ    . PHE A 1 252 ? -8.952  6.765   28.201  1 41.52 ? 252 PHE A CZ    1 
ATOM   2092  N  N     . THR A 1 253 ? -4.596  5.197   33.375  1 39.71 ? 253 THR A N     1 
ATOM   2093  C  CA    . THR A 1 253 ? -3.902  4.283   34.293  1 39.9  ? 253 THR A CA    1 
ATOM   2094  C  C     . THR A 1 253 ? -4.122  2.865   33.767  1 39.63 ? 253 THR A C     1 
ATOM   2095  O  O     . THR A 1 253 ? -5.014  2.658   32.933  1 39.88 ? 253 THR A O     1 
ATOM   2096  C  CB    . THR A 1 253 ? -4.429  4.423   35.735  1 41.53 ? 253 THR A CB    1 
ATOM   2097  O  OG1   . THR A 1 253 ? -4.607  5.804   36.063  1 42.88 ? 253 THR A OG1   1 
ATOM   2098  C  CG2   . THR A 1 253 ? -3.499  3.779   36.765  1 41.96 ? 253 THR A CG2   1 
ATOM   2099  N  N     . TYR A 1 254 ? -3.342  1.874   34.246  1 39.06 ? 254 TYR A N     1 
ATOM   2100  C  CA    . TYR A 1 254 ? -3.545  0.499   33.799  1 38.96 ? 254 TYR A CA    1 
ATOM   2101  C  C     . TYR A 1 254 ? -4.954  -0.007  34.143  1 38.84 ? 254 TYR A C     1 
ATOM   2102  O  O     . TYR A 1 254 ? -5.541  -0.714  33.342  1 38.79 ? 254 TYR A O     1 
ATOM   2103  C  CB    . TYR A 1 254 ? -2.463  -0.462  34.294  1 38.93 ? 254 TYR A CB    1 
ATOM   2104  C  CG    . TYR A 1 254 ? -2.685  -1.831  33.702  1 39.76 ? 254 TYR A CG    1 
ATOM   2105  C  CD1   . TYR A 1 254 ? -2.662  -2.023  32.328  1 40.74 ? 254 TYR A CD1   1 
ATOM   2106  C  CD2   . TYR A 1 254 ? -3.091  -2.893  34.495  1 40.64 ? 254 TYR A CD2   1 
ATOM   2107  C  CE1   . TYR A 1 254 ? -2.937  -3.261  31.767  1 41.67 ? 254 TYR A CE1   1 
ATOM   2108  C  CE2   . TYR A 1 254 ? -3.373  -4.136  33.947  1 41.62 ? 254 TYR A CE2   1 
ATOM   2109  C  CZ    . TYR A 1 254 ? -3.299  -4.317  32.58   1 42.68 ? 254 TYR A CZ    1 
ATOM   2110  O  OH    . TYR A 1 254 ? -3.568  -5.549  32.036  1 44.33 ? 254 TYR A OH    1 
ATOM   2111  N  N     . SER A 1 255 ? -5.528  0.417   35.282  1 38.67 ? 255 SER A N     1 
ATOM   2112  C  CA    . SER A 1 255 ? -6.886  0.009   35.651  1 38.84 ? 255 SER A CA    1 
ATOM   2113  C  C     . SER A 1 255 ? -7.91   0.446   34.592  1 39.04 ? 255 SER A C     1 
ATOM   2114  O  O     . SER A 1 255 ? -8.849  -0.296  34.311  1 39.28 ? 255 SER A O     1 
ATOM   2115  C  CB    . SER A 1 255 ? -7.265  0.556   37.022  1 39.8  ? 255 SER A CB    1 
ATOM   2116  O  OG    . SER A 1 255 ? -8.628  0.298   37.311  1 41.73 ? 255 SER A OG    1 
ATOM   2117  N  N     . GLU A 1 256 ? -7.702  1.625   33.98   1 38.66 ? 256 GLU A N     1 
ATOM   2118  C  CA    . GLU A 1 256 ? -8.574  2.129   32.922  1 38.62 ? 256 GLU A CA    1 
ATOM   2119  C  C     . GLU A 1 256 ? -8.421  1.303   31.644  1 38.1  ? 256 GLU A C     1 
ATOM   2120  O  O     . GLU A 1 256 ? -9.425  0.924   31.047  1 38.07 ? 256 GLU A O     1 
ATOM   2121  C  CB    . GLU A 1 256 ? -8.314  3.614   32.662  1 40.9  ? 256 GLU A CB    1 
ATOM   2122  C  CG    . GLU A 1 256 ? -8.877  4.482   33.767  1 45.49 ? 256 GLU A CG    1 
ATOM   2123  C  CD    . GLU A 1 256 ? -8.379  5.908   33.772  1 51.99 ? 256 GLU A CD    1 
ATOM   2124  O  OE1   . GLU A 1 256 ? -9.034  6.761   34.411  1 54.12 ? 256 GLU A OE1   1 
ATOM   2125  O  OE2   . GLU A 1 256 ? -7.335  6.177   33.14   1 53.45 ? 256 GLU A OE2   1 
ATOM   2126  N  N     . TRP A 1 257 ? -7.179  0.979   31.251  1 37.59 ? 257 TRP A N     1 
ATOM   2127  C  CA    . TRP A 1 257 ? -6.938  0.153   30.071  1 37.77 ? 257 TRP A CA    1 
ATOM   2128  C  C     . TRP A 1 257 ? -7.495  -1.254  30.262  1 37.96 ? 257 TRP A C     1 
ATOM   2129  O  O     . TRP A 1 257 ? -8.045  -1.829  29.326  1 38.07 ? 257 TRP A O     1 
ATOM   2130  C  CB    . TRP A 1 257 ? -5.439  0.052   29.76   1 37.68 ? 257 TRP A CB    1 
ATOM   2131  C  CG    . TRP A 1 257 ? -4.806  1.295   29.206  1 38.03 ? 257 TRP A CG    1 
ATOM   2132  C  CD1   . TRP A 1 257 ? -3.743  1.97    29.729  1 38.82 ? 257 TRP A CD1   1 
ATOM   2133  C  CD2   . TRP A 1 257 ? -5.131  1.953   27.972  1 38.1  ? 257 TRP A CD2   1 
ATOM   2134  N  NE1   . TRP A 1 257 ? -3.405  3.026   28.916  1 39.08 ? 257 TRP A NE1   1 
ATOM   2135  C  CE2   . TRP A 1 257 ? -4.245  3.04    27.831  1 38.83 ? 257 TRP A CE2   1 
ATOM   2136  C  CE3   . TRP A 1 257 ? -6.106  1.749   26.987  1 38.62 ? 257 TRP A CE3   1 
ATOM   2137  C  CZ2   . TRP A 1 257 ? -4.293  3.905   26.736  1 39.3  ? 257 TRP A CZ2   1 
ATOM   2138  C  CZ3   . TRP A 1 257 ? -6.165  2.626   25.918  1 39.33 ? 257 TRP A CZ3   1 
ATOM   2139  C  CH2   . TRP A 1 257 ? -5.259  3.677   25.793  1 39.28 ? 257 TRP A CH2   1 
ATOM   2140  N  N     . GLU A 1 258 ? -7.353  -1.803  31.476  1 37.9  ? 258 GLU A N     1 
ATOM   2141  C  CA    . GLU A 1 258 ? -7.83   -3.134  31.835  1 38.1  ? 258 GLU A CA    1 
ATOM   2142  C  C     . GLU A 1 258 ? -9.347  -3.187  31.768  1 38.59 ? 258 GLU A C     1 
ATOM   2143  O  O     . GLU A 1 258 ? -9.886  -4.16   31.262  1 38.37 ? 258 GLU A O     1 
ATOM   2144  C  CB    . GLU A 1 258 ? -7.35   -3.501  33.238  1 39.51 ? 258 GLU A CB    1 
ATOM   2145  C  CG    . GLU A 1 258 ? -7.655  -4.927  33.638  1 42.8  ? 258 GLU A CG    1 
ATOM   2146  C  CD    . GLU A 1 258 ? -7.2    -5.242  35.046  1 47.54 ? 258 GLU A CD    1 
ATOM   2147  O  OE1   . GLU A 1 258 ? -7.503  -4.445  35.963  1 47.72 ? 258 GLU A OE1   1 
ATOM   2148  O  OE2   . GLU A 1 258 ? -6.531  -6.283  35.234  1 49.89 ? 258 GLU A OE2   1 
ATOM   2149  N  N     . SER A 1 259 ? -10.036 -2.121  32.218  1 39.15 ? 259 SER A N     1 
ATOM   2150  C  CA    . SER A 1 259 ? -11.501 -2.055  32.166  1 40.21 ? 259 SER A CA    1 
ATOM   2151  C  C     . SER A 1 259 ? -12.039 -1.987  30.725  1 40.98 ? 259 SER A C     1 
ATOM   2152  O  O     . SER A 1 259 ? -13.149 -2.444  30.467  1 41.3  ? 259 SER A O     1 
ATOM   2153  C  CB    . SER A 1 259 ? -12.036 -0.896  33.004  1 41.85 ? 259 SER A CB    1 
ATOM   2154  O  OG    . SER A 1 259 ? -11.79  0.376   32.425  1 44.47 ? 259 SER A OG    1 
ATOM   2155  N  N     . ILE A 1 260 ? -11.247 -1.439  29.791  1 41.03 ? 260 ILE A N     1 
ATOM   2156  C  CA    . ILE A 1 260 ? -11.608 -1.389  28.374  1 41.49 ? 260 ILE A CA    1 
ATOM   2157  C  C     . ILE A 1 260 ? -11.335 -2.774  27.773  1 41.73 ? 260 ILE A C     1 
ATOM   2158  O  O     . ILE A 1 260 ? -12.18  -3.312  27.063  1 41.92 ? 260 ILE A O     1 
ATOM   2159  C  CB    . ILE A 1 260 ? -10.81  -0.276  27.637  1 42.05 ? 260 ILE A CB    1 
ATOM   2160  C  CG1   . ILE A 1 260 ? -11.124 1.115   28.199  1 42.75 ? 260 ILE A CG1   1 
ATOM   2161  C  CG2   . ILE A 1 260 ? -11.065 -0.311  26.139  1 42.56 ? 260 ILE A CG2   1 
ATOM   2162  C  CD1   . ILE A 1 260 ? -10.134 2.156   27.776  1 43.8  ? 260 ILE A CD1   1 
ATOM   2163  N  N     . TYR A 1 261 ? -10.169 -3.363  28.095  1 41.68 ? 261 TYR A N     1 
ATOM   2164  C  CA    . TYR A 1 261 ? -9.759  -4.686  27.634  1 42.18 ? 261 TYR A CA    1 
ATOM   2165  C  C     . TYR A 1 261 ? -10.752 -5.785  28.001  1 42.59 ? 261 TYR A C     1 
ATOM   2166  O  O     . TYR A 1 261 ? -11.143 -6.567  27.135  1 42.69 ? 261 TYR A O     1 
ATOM   2167  C  CB    . TYR A 1 261 ? -8.344  -5.032  28.139  1 42.21 ? 261 TYR A CB    1 
ATOM   2168  C  CG    . TYR A 1 261 ? -7.886  -6.426  27.768  1 42.87 ? 261 TYR A CG    1 
ATOM   2169  C  CD1   . TYR A 1 261 ? -7.385  -6.7    26.506  1 43.45 ? 261 TYR A CD1   1 
ATOM   2170  C  CD2   . TYR A 1 261 ? -7.955  -7.469  28.68   1 43.9  ? 261 TYR A CD2   1 
ATOM   2171  C  CE1   . TYR A 1 261 ? -6.975  -7.979  26.156  1 44.32 ? 261 TYR A CE1   1 
ATOM   2172  C  CE2   . TYR A 1 261 ? -7.565  -8.755  28.335  1 44.76 ? 261 TYR A CE2   1 
ATOM   2173  C  CZ    . TYR A 1 261 ? -7.066  -9.006  27.073  1 45.4  ? 261 TYR A CZ    1 
ATOM   2174  O  OH    . TYR A 1 261 ? -6.665  -10.277 26.735  1 46.89 ? 261 TYR A OH    1 
ATOM   2175  N  N     . ASN A 1 262 ? -11.151 -5.863  29.279  1 42.74 ? 262 ASN A N     1 
ATOM   2176  C  CA    . ASN A 1 262 ? -12.082 -6.908  29.71   1 43.22 ? 262 ASN A CA    1 
ATOM   2177  C  C     . ASN A 1 262 ? -13.56  -6.627  29.345  1 43.57 ? 262 ASN A C     1 
ATOM   2178  O  O     . ASN A 1 262 ? -14.439 -7.362  29.781  1 43.74 ? 262 ASN A O     1 
ATOM   2179  C  CB    . ASN A 1 262 ? -11.925 -7.237  31.198  1 44.22 ? 262 ASN A CB    1 
ATOM   2180  C  CG    . ASN A 1 262 ? -12.225 -6.103  32.144  1 47.54 ? 262 ASN A CG    1 
ATOM   2181  O  OD1   . ASN A 1 262 ? -12.961 -5.158  31.827  1 48.84 ? 262 ASN A OD1   1 
ATOM   2182  N  ND2   . ASN A 1 262 ? -11.649 -6.167  33.337  1 48.12 ? 262 ASN A ND2   1 
ATOM   2183  N  N     . GLY A 1 263 ? -13.815 -5.588  28.554  1 43.49 ? 263 GLY A N     1 
ATOM   2184  C  CA    . GLY A 1 263 ? -15.151 -5.265  28.082  1 43.87 ? 263 GLY A CA    1 
ATOM   2185  C  C     . GLY A 1 263 ? -16.083 -4.603  29.068  1 44.14 ? 263 GLY A C     1 
ATOM   2186  O  O     . GLY A 1 263 ? -17.29  -4.577  28.826  1 44.24 ? 263 GLY A O     1 
ATOM   2187  N  N     . THR A 1 264 ? -15.556 -4.054  30.174  1 44.25 ? 264 THR A N     1 
ATOM   2188  C  CA    . THR A 1 264 ? -16.408 -3.359  31.146  1 44.91 ? 264 THR A CA    1 
ATOM   2189  C  C     . THR A 1 264 ? -16.912 -2.037  30.54   1 45.41 ? 264 THR A C     1 
ATOM   2190  O  O     . THR A 1 264 ? -18.092 -1.713  30.648  1 45.55 ? 264 THR A O     1 
ATOM   2191  C  CB    . THR A 1 264 ? -15.671 -3.126  32.472  1 46.1  ? 264 THR A CB    1 
ATOM   2192  O  OG1   . THR A 1 264 ? -15.114 -4.351  32.935  1 47.12 ? 264 THR A OG1   1 
ATOM   2193  C  CG2   . THR A 1 264 ? -16.577 -2.552  33.54   1 46.41 ? 264 THR A CG2   1 
ATOM   2194  N  N     . TYR A 1 265 ? -16.024 -1.295  29.877  1 45.52 ? 265 TYR A N     1 
ATOM   2195  C  CA    . TYR A 1 265 ? -16.381 -0.027  29.24   1 46.22 ? 265 TYR A CA    1 
ATOM   2196  C  C     . TYR A 1 265 ? -15.754 0.092   27.845  1 46.4  ? 265 TYR A C     1 
ATOM   2197  O  O     . TYR A 1 265 ? -14.752 -0.561  27.555  1 46.57 ? 265 TYR A O     1 
ATOM   2198  C  CB    . TYR A 1 265 ? -15.853 1.164   30.075  1 46.53 ? 265 TYR A CB    1 
ATOM   2199  C  CG    . TYR A 1 265 ? -16.201 1.134   31.544  1 47.51 ? 265 TYR A CG    1 
ATOM   2200  C  CD1   . TYR A 1 265 ? -17.489 1.406   31.979  1 48.48 ? 265 TYR A CD1   1 
ATOM   2201  C  CD2   . TYR A 1 265 ? -15.224 0.917   32.505  1 48.42 ? 265 TYR A CD2   1 
ATOM   2202  C  CE1   . TYR A 1 265 ? -17.811 1.397   33.33   1 49.44 ? 265 TYR A CE1   1 
ATOM   2203  C  CE2   . TYR A 1 265 ? -15.531 0.912   33.858  1 49.39 ? 265 TYR A CE2   1 
ATOM   2204  C  CZ    . TYR A 1 265 ? -16.829 1.142   34.269  1 50.39 ? 265 TYR A CZ    1 
ATOM   2205  O  OH    . TYR A 1 265 ? -17.13  1.14    35.611  1 51.94 ? 265 TYR A OH    1 
ATOM   2206  N  N     . ARG A 1 266 ? -16.314 0.966   26.999  1 46.16 ? 266 ARG A N     1 
ATOM   2207  C  CA    . ARG A 1 266 ? -15.7   1.309   25.721  1 46.47 ? 266 ARG A CA    1 
ATOM   2208  C  C     . ARG A 1 266 ? -14.794 2.539   26      1 46.28 ? 266 ARG A C     1 
ATOM   2209  O  O     . ARG A 1 266 ? -14.983 3.227   27.013  1 46.45 ? 266 ARG A O     1 
ATOM   2210  C  CB    . ARG A 1 266 ? -16.75  1.576   24.619  1 48.18 ? 266 ARG A CB    1 
ATOM   2211  C  CG    . ARG A 1 266 ? -17.447 2.926   24.709  1 52.1  ? 266 ARG A CG    1 
ATOM   2212  C  CD    . ARG A 1 266 ? -18.604 3.083   23.739  1 56.01 ? 266 ARG A CD    1 
ATOM   2213  N  NE    . ARG A 1 266 ? -19.046 4.478   23.658  1 59.33 ? 266 ARG A NE    1 
ATOM   2214  C  CZ    . ARG A 1 266 ? -20.163 4.949   24.205  1 61.76 ? 266 ARG A CZ    1 
ATOM   2215  N  NH1   . ARG A 1 266 ? -20.981 4.138   24.866  1 61.29 ? 266 ARG A NH1   1 
ATOM   2216  N  NH2   . ARG A 1 266 ? -20.475 6.234   24.09   1 61.94 ? 266 ARG A NH2   1 
ATOM   2217  N  N     . ILE A 1 267 ? -13.802 2.807   25.139  1 45.72 ? 267 ILE A N     1 
ATOM   2218  C  CA    . ILE A 1 267 ? -12.859 3.904   25.375  1 45.56 ? 267 ILE A CA    1 
ATOM   2219  C  C     . ILE A 1 267 ? -13.529 5.292   25.445  1 45.2  ? 267 ILE A C     1 
ATOM   2220  O  O     . ILE A 1 267 ? -12.987 6.193   26.087  1 45.31 ? 267 ILE A O     1 
ATOM   2221  C  CB    . ILE A 1 267 ? -11.701 3.869   24.362  1 46.12 ? 267 ILE A CB    1 
ATOM   2222  C  CG1   . ILE A 1 267 ? -10.464 4.613   24.893  1 47.06 ? 267 ILE A CG1   1 
ATOM   2223  C  CG2   . ILE A 1 267 ? -12.143 4.375   22.996  1 46.68 ? 267 ILE A CG2   1 
ATOM   2224  C  CD1   . ILE A 1 267 ? -9.22   4.337   24.133  1 48.37 ? 267 ILE A CD1   1 
ATOM   2225  N  N     . THR A 1 268 ? -14.725 5.45    24.856  1 44.64 ? 268 THR A N     1 
ATOM   2226  C  CA    . THR A 1 268 ? -15.427 6.734   24.89   1 44.59 ? 268 THR A CA    1 
ATOM   2227  C  C     . THR A 1 268 ? -16.462 6.849   26.026  1 44.03 ? 268 THR A C     1 
ATOM   2228  O  O     . THR A 1 268 ? -16.972 7.945   26.263  1 43.87 ? 268 THR A O     1 
ATOM   2229  C  CB    . THR A 1 268 ? -16.048 7.052   23.525  1 45.95 ? 268 THR A CB    1 
ATOM   2230  O  OG1   . THR A 1 268 ? -16.817 5.93    23.084  1 47.02 ? 268 THR A OG1   1 
ATOM   2231  C  CG2   . THR A 1 268 ? -15     7.419   22.485  1 46.22 ? 268 THR A CG2   1 
ATOM   2232  N  N     . ASN A 1 269 ? -16.779 5.742   26.721  1 43.56 ? 269 ASN A N     1 
ATOM   2233  C  CA    . ASN A 1 269 ? -17.732 5.796   27.83   1 43.69 ? 269 ASN A CA    1 
ATOM   2234  C  C     . ASN A 1 269 ? -17.088 5.448   29.181  1 43.06 ? 269 ASN A C     1 
ATOM   2235  O  O     . ASN A 1 269 ? -17.782 5.01    30.099  1 43.13 ? 269 ASN A O     1 
ATOM   2236  C  CB    . ASN A 1 269 ? -19.001 4.967   27.561  1 45.61 ? 269 ASN A CB    1 
ATOM   2237  C  CG    . ASN A 1 269 ? -18.934 3.46    27.777  1 50.34 ? 269 ASN A CG    1 
ATOM   2238  O  OD1   . ASN A 1 269 ? -17.982 2.902   28.342  1 51.96 ? 269 ASN A OD1   1 
ATOM   2239  N  ND2   . ASN A 1 269 ? -19.967 2.753   27.331  1 51.33 ? 269 ASN A ND2   1 
ATOM   2240  N  N     . LEU A 1 270 ? -15.765 5.657   29.31   1 42.37 ? 270 LEU A N     1 
ATOM   2241  C  CA    . LEU A 1 270 ? -15.017 5.411   30.543  1 42.2  ? 270 LEU A CA    1 
ATOM   2242  C  C     . LEU A 1 270 ? -15.563 6.37    31.605  1 41.89 ? 270 LEU A C     1 
ATOM   2243  O  O     . LEU A 1 270 ? -15.725 7.558   31.317  1 42.26 ? 270 LEU A O     1 
ATOM   2244  C  CB    . LEU A 1 270 ? -13.528 5.705   30.284  1 42.31 ? 270 LEU A CB    1 
ATOM   2245  C  CG    . LEU A 1 270 ? -12.507 4.852   31.031  1 43.64 ? 270 LEU A CG    1 
ATOM   2246  C  CD1   . LEU A 1 270 ? -12.677 3.382   30.712  1 44.11 ? 270 LEU A CD1   1 
ATOM   2247  C  CD2   . LEU A 1 270 ? -11.102 5.278   30.684  1 44.24 ? 270 LEU A CD2   1 
ATOM   2248  N  N     . PRO A 1 271 ? -15.948 5.872   32.791  1 41.01 ? 271 PRO A N     1 
ATOM   2249  C  CA    . PRO A 1 271 ? -16.531 6.77    33.804  1 40.6  ? 271 PRO A CA    1 
ATOM   2250  C  C     . PRO A 1 271 ? -15.613 7.911   34.225  1 40.05 ? 271 PRO A C     1 
ATOM   2251  O  O     . PRO A 1 271 ? -16.086 8.983   34.578  1 40.1  ? 271 PRO A O     1 
ATOM   2252  C  CB    . PRO A 1 271 ? -16.854 5.835   34.972  1 41.51 ? 271 PRO A CB    1 
ATOM   2253  C  CG    . PRO A 1 271 ? -15.999 4.631   34.757  1 42.02 ? 271 PRO A CG    1 
ATOM   2254  C  CD    . PRO A 1 271 ? -15.858 4.485   33.274  1 40.42 ? 271 PRO A CD    1 
ATOM   2255  N  N     . SER A 1 272 ? -14.304 7.695   34.141  1 39.48 ? 272 SER A N     1 
ATOM   2256  C  CA    . SER A 1 272 ? -13.306 8.687   34.506  1 39.5  ? 272 SER A CA    1 
ATOM   2257  C  C     . SER A 1 272 ? -12.924 9.639   33.378  1 39.85 ? 272 SER A C     1 
ATOM   2258  O  O     . SER A 1 272 ? -12.068 10.49   33.598  1 40.29 ? 272 SER A O     1 
ATOM   2259  C  CB    . SER A 1 272 ? -12.05  7.989   35.003  1 40.37 ? 272 SER A CB    1 
ATOM   2260  O  OG    . SER A 1 272 ? -11.615 7.042   34.041  1 41.99 ? 272 SER A OG    1 
ATOM   2261  N  N     . LEU A 1 273 ? -13.523 9.51    32.175  1 39.5  ? 273 LEU A N     1 
ATOM   2262  C  CA    . LEU A 1 273 ? -13.21  10.388  31.045  1 39.5  ? 273 LEU A CA    1 
ATOM   2263  C  C     . LEU A 1 273 ? -13.515 11.841  31.405  1 39.41 ? 273 LEU A C     1 
ATOM   2264  O  O     . LEU A 1 273 ? -14.601 12.149  31.89   1 39.52 ? 273 LEU A O     1 
ATOM   2265  C  CB    . LEU A 1 273 ? -13.993 9.971   29.795  1 39.73 ? 273 LEU A CB    1 
ATOM   2266  C  CG    . LEU A 1 273 ? -13.248 10.117  28.475  1 41.38 ? 273 LEU A CG    1 
ATOM   2267  C  CD1   . LEU A 1 273 ? -12.041 9.206   28.434  1 41.9  ? 273 LEU A CD1   1 
ATOM   2268  C  CD2   . LEU A 1 273 ? -14.153 9.79    27.301  1 42.11 ? 273 LEU A CD2   1 
ATOM   2269  N  N     . GLY A 1 274 ? -12.523 12.697  31.254  1 39.06 ? 274 GLY A N     1 
ATOM   2270  C  CA    . GLY A 1 274 ? -12.669 14.097  31.616  1 38.96 ? 274 GLY A CA    1 
ATOM   2271  C  C     . GLY A 1 274 ? -11.749 14.533  32.736  1 38.51 ? 274 GLY A C     1 
ATOM   2272  O  O     . GLY A 1 274 ? -11.529 15.735  32.898  1 38.73 ? 274 GLY A O     1 
ATOM   2273  N  N     . ARG A 1 275 ? -11.185 13.58   33.512  1 37.74 ? 275 ARG A N     1 
ATOM   2274  C  CA    . ARG A 1 275 ? -10.244 13.947  34.581  1 37.7  ? 275 ARG A CA    1 
ATOM   2275  C  C     . ARG A 1 275 ? -9.018  14.704  34.032  1 37.91 ? 275 ARG A C     1 
ATOM   2276  O  O     . ARG A 1 275 ? -8.423  15.517  34.738  1 38    ? 275 ARG A O     1 
ATOM   2277  C  CB    . ARG A 1 275 ? -9.855  12.755  35.456  1 38.33 ? 275 ARG A CB    1 
ATOM   2278  C  CG    . ARG A 1 275 ? -9.243  11.617  34.688  1 39.97 ? 275 ARG A CG    1 
ATOM   2279  C  CD    . ARG A 1 275 ? -9.057  10.417  35.591  1 41.31 ? 275 ARG A CD    1 
ATOM   2280  N  NE    . ARG A 1 275 ? -8.152  9.424   35.008  1 42.19 ? 275 ARG A NE    1 
ATOM   2281  C  CZ    . ARG A 1 275 ? -6.826  9.495   35.062  1 43.09 ? 275 ARG A CZ    1 
ATOM   2282  N  NH1   . ARG A 1 275 ? -6.234  10.526  35.646  1 43.19 ? 275 ARG A NH1   1 
ATOM   2283  N  NH2   . ARG A 1 275 ? -6.082  8.547   34.512  1 42.19 ? 275 ARG A NH2   1 
ATOM   2284  N  N     . PHE A 1 276 ? -8.681  14.477  32.759  1 37.74 ? 276 PHE A N     1 
ATOM   2285  C  CA    . PHE A 1 276 ? -7.685  15.251  32.042  1 38.15 ? 276 PHE A CA    1 
ATOM   2286  C  C     . PHE A 1 276 ? -8.279  15.686  30.688  1 38.41 ? 276 PHE A C     1 
ATOM   2287  O  O     . PHE A 1 276 ? -9.186  15.032  30.174  1 38.59 ? 276 PHE A O     1 
ATOM   2288  C  CB    . PHE A 1 276 ? -6.333  14.542  31.919  1 38.08 ? 276 PHE A CB    1 
ATOM   2289  C  CG    . PHE A 1 276 ? -6.352  13.22   31.209  1 38.8  ? 276 PHE A CG    1 
ATOM   2290  C  CD1   . PHE A 1 276 ? -6.21   13.153  29.835  1 39.72 ? 276 PHE A CD1   1 
ATOM   2291  C  CD2   . PHE A 1 276 ? -6.457  12.038  31.919  1 39.54 ? 276 PHE A CD2   1 
ATOM   2292  C  CE1   . PHE A 1 276 ? -6.219  11.934  29.183  1 40.47 ? 276 PHE A CE1   1 
ATOM   2293  C  CE2   . PHE A 1 276 ? -6.454  10.818  31.265  1 40.26 ? 276 PHE A CE2   1 
ATOM   2294  C  CZ    . PHE A 1 276 ? -6.338  10.773  29.902  1 40.23 ? 276 PHE A CZ    1 
ATOM   2295  N  N     . LYS A 1 277 ? -7.828  16.824  30.153  1 38.21 ? 277 LYS A N     1 
ATOM   2296  C  CA    . LYS A 1 277 ? -8.35   17.368  28.899  1 38.35 ? 277 LYS A CA    1 
ATOM   2297  C  C     . LYS A 1 277 ? -7.421  17.101  27.719  1 38.27 ? 277 LYS A C     1 
ATOM   2298  O  O     . LYS A 1 277 ? -6.266  16.745  27.915  1 38.15 ? 277 LYS A O     1 
ATOM   2299  C  CB    . LYS A 1 277 ? -8.568  18.891  29.038  1 40.12 ? 277 LYS A CB    1 
ATOM   2300  C  CG    . LYS A 1 277 ? -9.807  19.28   29.817  1 43.62 ? 277 LYS A CG    1 
ATOM   2301  C  CD    . LYS A 1 277 ? -10.106 20.757  29.635  1 47.8  ? 277 LYS A CD    1 
ATOM   2302  C  CE    . LYS A 1 277 ? -11.499 21.141  30.057  1 51.85 ? 277 LYS A CE    1 
ATOM   2303  N  NZ    . LYS A 1 277 ? -11.681 21.012  31.526  1 54.29 ? 277 LYS A NZ    1 
ATOM   2304  N  N     . PHE A 1 278 ? -7.924  17.282  26.492  1 38.29 ? 278 PHE A N     1 
ATOM   2305  C  CA    . PHE A 1 278 ? -7.103  17.131  25.307  1 38.91 ? 278 PHE A CA    1 
ATOM   2306  C  C     . PHE A 1 278 ? -6.445  18.48   25.077  1 38.36 ? 278 PHE A C     1 
ATOM   2307  O  O     . PHE A 1 278 ? -7.132  19.472  24.844  1 38.55 ? 278 PHE A O     1 
ATOM   2308  C  CB    . PHE A 1 278 ? -7.949  16.678  24.101  1 39.73 ? 278 PHE A CB    1 
ATOM   2309  C  CG    . PHE A 1 278 ? -7.361  16.921  22.722  1 41.31 ? 278 PHE A CG    1 
ATOM   2310  C  CD1   . PHE A 1 278 ? -6.042  16.613  22.448  1 42.47 ? 278 PHE A CD1   1 
ATOM   2311  C  CD2   . PHE A 1 278 ? -8.144  17.411  21.691  1 42.39 ? 278 PHE A CD2   1 
ATOM   2312  C  CE1   . PHE A 1 278 ? -5.502  16.87   21.195  1 43.36 ? 278 PHE A CE1   1 
ATOM   2313  C  CE2   . PHE A 1 278 ? -7.608  17.626  20.429  1 43.26 ? 278 PHE A CE2   1 
ATOM   2314  C  CZ    . PHE A 1 278 ? -6.291  17.351  20.188  1 43.18 ? 278 PHE A CZ    1 
ATOM   2315  N  N     . ARG A 1 279 ? -5.115  18.527  25.203  1 37.7  ? 279 ARG A N     1 
ATOM   2316  C  CA    . ARG A 1 279 ? -4.338  19.747  25.021  1 37.68 ? 279 ARG A CA    1 
ATOM   2317  C  C     . ARG A 1 279 ? -3.228  19.507  24.006  1 37.11 ? 279 ARG A C     1 
ATOM   2318  O  O     . ARG A 1 279 ? -2.117  19.138  24.377  1 37.11 ? 279 ARG A O     1 
ATOM   2319  C  CB    . ARG A 1 279 ? -3.764  20.239  26.363  1 39.32 ? 279 ARG A CB    1 
ATOM   2320  C  CG    . ARG A 1 279 ? -4.83   20.393  27.458  1 42.59 ? 279 ARG A CG    1 
ATOM   2321  C  CD    . ARG A 1 279 ? -4.318  21.079  28.712  1 45.27 ? 279 ARG A CD    1 
ATOM   2322  N  NE    . ARG A 1 279 ? -5.358  21.17   29.74   1 47.55 ? 279 ARG A NE    1 
ATOM   2323  C  CZ    . ARG A 1 279 ? -6.209  22.184  29.86   1 48.99 ? 279 ARG A CZ    1 
ATOM   2324  N  NH1   . ARG A 1 279 ? -6.155  23.208  29.017  1 49.18 ? 279 ARG A NH1   1 
ATOM   2325  N  NH2   . ARG A 1 279 ? -7.117  22.184  30.824  1 47.99 ? 279 ARG A NH2   1 
ATOM   2326  N  N     . LYS A 1 280 ? -3.544  19.705  22.723  1 36.52 ? 280 LYS A N     1 
ATOM   2327  C  CA    . LYS A 1 280 ? -2.617  19.523  21.612  1 36.58 ? 280 LYS A CA    1 
ATOM   2328  C  C     . LYS A 1 280 ? -1.422  20.456  21.732  1 36.72 ? 280 LYS A C     1 
ATOM   2329  O  O     . LYS A 1 280 ? -1.597  21.649  21.964  1 36.8  ? 280 LYS A O     1 
ATOM   2330  C  CB    . LYS A 1 280 ? -3.356  19.771  20.283  1 38.13 ? 280 LYS A CB    1 
ATOM   2331  C  CG    . LYS A 1 280 ? -2.472  19.883  19.033  1 41.59 ? 280 LYS A CG    1 
ATOM   2332  C  CD    . LYS A 1 280 ? -1.938  18.542  18.567  1 44.89 ? 280 LYS A CD    1 
ATOM   2333  C  CE    . LYS A 1 280 ? -1.081  18.661  17.342  1 47.92 ? 280 LYS A CE    1 
ATOM   2334  N  NZ    . LYS A 1 280 ? -0.14   19.786  17.445  1 50.46 ? 280 LYS A NZ    1 
ATOM   2335  N  N     . LYS A 1 281 ? -0.211  19.922  21.55   1 36.72 ? 281 LYS A N     1 
ATOM   2336  C  CA    . LYS A 1 281 ? 0.998   20.736  21.599  1 37.28 ? 281 LYS A CA    1 
ATOM   2337  C  C     . LYS A 1 281 ? 1.405   21.182  20.197  1 37.46 ? 281 LYS A C     1 
ATOM   2338  O  O     . LYS A 1 281 ? 1.73    20.347  19.367  1 37.69 ? 281 LYS A O     1 
ATOM   2339  C  CB    . LYS A 1 281 ? 2.149   19.958  22.249  1 39.25 ? 281 LYS A CB    1 
ATOM   2340  C  CG    . LYS A 1 281 ? 2.044   19.869  23.762  1 43.35 ? 281 LYS A CG    1 
ATOM   2341  C  CD    . LYS A 1 281 ? 3.414   19.768  24.402  1 47.79 ? 281 LYS A CD    1 
ATOM   2342  C  CE    . LYS A 1 281 ? 3.98    18.369  24.365  1 51.75 ? 281 LYS A CE    1 
ATOM   2343  N  NZ    . LYS A 1 281 ? 3.264   17.451  25.288  1 54.03 ? 281 LYS A NZ    1 
ATOM   2344  N  N     . ILE A 1 282 ? 1.405   22.49   19.934  1 37.24 ? 282 ILE A N     1 
ATOM   2345  C  CA    . ILE A 1 282 ? 1.783   23.015  18.624  1 37.64 ? 282 ILE A CA    1 
ATOM   2346  C  C     . ILE A 1 282 ? 3.03    23.882  18.759  1 38.5  ? 282 ILE A C     1 
ATOM   2347  O  O     . ILE A 1 282 ? 3.046   24.795  19.583  1 38.61 ? 282 ILE A O     1 
ATOM   2348  C  CB    . ILE A 1 282 ? 0.613   23.818  18.001  1 37.63 ? 282 ILE A CB    1 
ATOM   2349  C  CG1   . ILE A 1 282 ? -0.652  22.957  17.877  1 38.21 ? 282 ILE A CG1   1 
ATOM   2350  C  CG2   . ILE A 1 282 ? 1.01    24.404  16.662  1 37.97 ? 282 ILE A CG2   1 
ATOM   2351  C  CD1   . ILE A 1 282 ? -1.888  23.708  17.462  1 39.19 ? 282 ILE A CD1   1 
ATOM   2352  N  N     . ALA A 1 283 ? 4.078   23.601  17.965  1 38.84 ? 283 ALA A N     1 
ATOM   2353  C  CA    . ALA A 1 283 ? 5.3     24.408  18.006  1 39.58 ? 283 ALA A CA    1 
ATOM   2354  C  C     . ALA A 1 283 ? 4.993   25.82   17.519  1 40.33 ? 283 ALA A C     1 
ATOM   2355  O  O     . ALA A 1 283 ? 4.18    25.984  16.611  1 40.73 ? 283 ALA A O     1 
ATOM   2356  C  CB    . ALA A 1 283 ? 6.368   23.787  17.122  1 39.63 ? 283 ALA A CB    1 
ATOM   2357  N  N     . GLU A 1 284 ? 5.643   26.84   18.098  1 40.3  ? 284 GLU A N     1 
ATOM   2358  C  CA    . GLU A 1 284 ? 5.414   28.236  17.707  1 40.63 ? 284 GLU A CA    1 
ATOM   2359  C  C     . GLU A 1 284 ? 5.66    28.463  16.225  1 40.7  ? 284 GLU A C     1 
ATOM   2360  O  O     . GLU A 1 284 ? 4.912   29.204  15.591  1 40.9  ? 284 GLU A O     1 
ATOM   2361  C  CB    . GLU A 1 284 ? 6.273   29.195  18.538  1 42.79 ? 284 GLU A CB    1 
ATOM   2362  C  CG    . GLU A 1 284 ? 5.579   29.701  19.782  1 47.56 ? 284 GLU A CG    1 
ATOM   2363  C  CD    . GLU A 1 284 ? 6.411   30.673  20.59   1 54.33 ? 284 GLU A CD    1 
ATOM   2364  O  OE1   . GLU A 1 284 ? 6.512   30.477  21.822  1 55.9  ? 284 GLU A OE1   1 
ATOM   2365  O  OE2   . GLU A 1 284 ? 6.966   31.626  19.994  1 56.16 ? 284 GLU A OE2   1 
ATOM   2366  N  N     . LYS A 1 285 ? 6.673   27.784  15.662  1 40.4  ? 285 LYS A N     1 
ATOM   2367  C  CA    . LYS A 1 285 ? 6.992   27.897  14.241  1 40.74 ? 285 LYS A CA    1 
ATOM   2368  C  C     . LYS A 1 285 ? 5.869   27.379  13.327  1 40.66 ? 285 LYS A C     1 
ATOM   2369  O  O     . LYS A 1 285 ? 5.79    27.785  12.172  1 40.85 ? 285 LYS A O     1 
ATOM   2370  C  CB    . LYS A 1 285 ? 8.323   27.194  13.92   1 42.86 ? 285 LYS A CB    1 
ATOM   2371  C  CG    . LYS A 1 285 ? 8.31    25.687  14.164  1 47.07 ? 285 LYS A CG    1 
ATOM   2372  C  CD    . LYS A 1 285 ? 9.63    25.02   13.768  1 51.23 ? 285 LYS A CD    1 
ATOM   2373  C  CE    . LYS A 1 285 ? 9.608   23.527  13.996  1 55.3  ? 285 LYS A CE    1 
ATOM   2374  N  NZ    . LYS A 1 285 ? 10.803  22.858  13.418  1 57.98 ? 285 LYS A NZ    1 
ATOM   2375  N  N     . SER A 1 286 ? 4.998   26.499  13.843  1 40.25 ? 286 SER A N     1 
ATOM   2376  C  CA    . SER A 1 286 ? 3.885   25.934  13.087  1 40.33 ? 286 SER A CA    1 
ATOM   2377  C  C     . SER A 1 286 ? 2.622   26.795  13.124  1 40.25 ? 286 SER A C     1 
ATOM   2378  O  O     . SER A 1 286 ? 1.699   26.524  12.359  1 40.23 ? 286 SER A O     1 
ATOM   2379  C  CB    . SER A 1 286 ? 3.543   24.547  13.617  1 41.63 ? 286 SER A CB    1 
ATOM   2380  O  OG    . SER A 1 286 ? 4.676   23.697  13.659  1 43.94 ? 286 SER A OG    1 
ATOM   2381  N  N     . LEU A 1 287 ? 2.552   27.798  14.017  1 40.09 ? 287 LEU A N     1 
ATOM   2382  C  CA    . LEU A 1 287 ? 1.365   28.636  14.146  1 40.51 ? 287 LEU A CA    1 
ATOM   2383  C  C     . LEU A 1 287 ? 1.148   29.587  12.985  1 41.12 ? 287 LEU A C     1 
ATOM   2384  O  O     . LEU A 1 287 ? 2.1     30.139  12.436  1 41.32 ? 287 LEU A O     1 
ATOM   2385  C  CB    . LEU A 1 287 ? 1.364   29.409  15.468  1 40.61 ? 287 LEU A CB    1 
ATOM   2386  C  CG    . LEU A 1 287 ? 1.148   28.583  16.72   1 41.82 ? 287 LEU A CG    1 
ATOM   2387  C  CD1   . LEU A 1 287 ? 1.282   29.433  17.949  1 42.23 ? 287 LEU A CD1   1 
ATOM   2388  C  CD2   . LEU A 1 287 ? -0.216  27.922  16.707  1 42.52 ? 287 LEU A CD2   1 
ATOM   2389  N  N     . SER A 1 288 ? -0.122  29.775  12.623  1 41.25 ? 288 SER A N     1 
ATOM   2390  C  CA    . SER A 1 288 ? -0.594  30.647  11.543  1 41.8  ? 288 SER A CA    1 
ATOM   2391  C  C     . SER A 1 288 ? -2.116  30.857  11.695  1 42.26 ? 288 SER A C     1 
ATOM   2392  O  O     . SER A 1 288 ? -2.752  30.183  12.502  1 42.14 ? 288 SER A O     1 
ATOM   2393  C  CB    . SER A 1 288 ? -0.288  30.023  10.184  1 42.93 ? 288 SER A CB    1 
ATOM   2394  O  OG    . SER A 1 288 ? 1.099   30.017  9.9     1 45.29 ? 288 SER A OG    1 
ATOM   2395  N  N     . GLY A 1 289 ? -2.682  31.799  10.944  1 42.54 ? 289 GLY A N     1 
ATOM   2396  C  CA    . GLY A 1 289 ? -4.115  32.089  10.955  1 43.17 ? 289 GLY A CA    1 
ATOM   2397  C  C     . GLY A 1 289 ? -4.792  32.113  12.314  1 43.45 ? 289 GLY A C     1 
ATOM   2398  O  O     . GLY A 1 289 ? -4.335  32.8    13.228  1 43.47 ? 289 GLY A O     1 
ATOM   2399  N  N     . LYS A 1 290 ? -5.87   31.336  12.464  1 43.56 ? 290 LYS A N     1 
ATOM   2400  C  CA    . LYS A 1 290 ? -6.604  31.252  13.726  1 44.13 ? 290 LYS A CA    1 
ATOM   2401  C  C     . LYS A 1 290 ? -6.369  29.92   14.452  1 44.72 ? 290 LYS A C     1 
ATOM   2402  O  O     . LYS A 1 290 ? -7.211  29.509  15.243  1 44.89 ? 290 LYS A O     1 
ATOM   2403  C  CB    . LYS A 1 290 ? -8.106  31.46   13.482  1 45.63 ? 290 LYS A CB    1 
ATOM   2404  C  CG    . LYS A 1 290 ? -8.428  32.812  12.866  1 48.96 ? 290 LYS A CG    1 
ATOM   2405  C  CD    . LYS A 1 290 ? -9.847  32.861  12.325  1 52.89 ? 290 LYS A CD    1 
ATOM   2406  C  CE    . LYS A 1 290 ? -10.12  34.142  11.582  1 56.43 ? 290 LYS A CE    1 
ATOM   2407  N  NZ    . LYS A 1 290 ? -11.354 34.049  10.76   1 58.6  ? 290 LYS A NZ    1 
ATOM   2408  N  N     . VAL A 1 291 ? -5.232  29.253  14.185  1 44.89 ? 291 VAL A N     1 
ATOM   2409  C  CA    . VAL A 1 291 ? -4.874  27.959  14.763  1 45.5  ? 291 VAL A CA    1 
ATOM   2410  C  C     . VAL A 1 291 ? -4.778  27.99   16.287  1 45.71 ? 291 VAL A C     1 
ATOM   2411  O  O     . VAL A 1 291 ? -5.365  27.132  16.941  1 45.51 ? 291 VAL A O     1 
ATOM   2412  C  CB    . VAL A 1 291 ? -3.592  27.406  14.105  1 46.54 ? 291 VAL A CB    1 
ATOM   2413  C  CG1   . VAL A 1 291 ? -3.122  26.129  14.794  1 47.4  ? 291 VAL A CG1   1 
ATOM   2414  C  CG2   . VAL A 1 291 ? -3.82   27.165  12.616  1 46.86 ? 291 VAL A CG2   1 
ATOM   2415  N  N     . LYS A 1 292 ? -4.095  28.997  16.857  1 46.11 ? 292 LYS A N     1 
ATOM   2416  C  CA    . LYS A 1 292 ? -3.991  29.127  18.316  1 46.91 ? 292 LYS A CA    1 
ATOM   2417  C  C     . LYS A 1 292 ? -5.38   29.325  18.942  1 47.2  ? 292 LYS A C     1 
ATOM   2418  O  O     . LYS A 1 292 ? -5.683  28.726  19.971  1 47.42 ? 292 LYS A O     1 
ATOM   2419  C  CB    . LYS A 1 292 ? -3.055  30.281  18.714  1 48.97 ? 292 LYS A CB    1 
ATOM   2420  C  CG    . LYS A 1 292 ? -2.754  30.308  20.211  1 53.38 ? 292 LYS A CG    1 
ATOM   2421  C  CD    . LYS A 1 292 ? -1.978  31.546  20.633  1 58.45 ? 292 LYS A CD    1 
ATOM   2422  C  CE    . LYS A 1 292 ? -1.584  31.498  22.094  1 62.75 ? 292 LYS A CE    1 
ATOM   2423  N  NZ    . LYS A 1 292 ? -2.755  31.312  22.993  1 64.97 ? 292 LYS A NZ    1 
ATOM   2424  N  N     . GLU A 1 293 ? -6.236  30.111  18.278  1 46.95 ? 293 GLU A N     1 
ATOM   2425  C  CA    . GLU A 1 293 ? -7.609  30.384  18.696  1 47.24 ? 293 GLU A CA    1 
ATOM   2426  C  C     . GLU A 1 293 ? -8.46   29.103  18.666  1 46.91 ? 293 GLU A C     1 
ATOM   2427  O  O     . GLU A 1 293 ? -9.224  28.842  19.601  1 47.06 ? 293 GLU A O     1 
ATOM   2428  C  CB    . GLU A 1 293 ? -8.224  31.467  17.793  1 50    ? 293 GLU A CB    1 
ATOM   2429  C  CG    . GLU A 1 293 ? -7.526  32.818  17.887  1 55.81 ? 293 GLU A CG    1 
ATOM   2430  C  CD    . GLU A 1 293 ? -6.447  33.101  16.856  1 63.26 ? 293 GLU A CD    1 
ATOM   2431  O  OE1   . GLU A 1 293 ? -6.618  34.061  16.07   1 64.6  ? 293 GLU A OE1   1 
ATOM   2432  O  OE2   . GLU A 1 293 ? -5.43   32.37   16.833  1 65.82 ? 293 GLU A OE2   1 
ATOM   2433  N  N     . PHE A 1 294 ? -8.305  28.295  17.604  1 46.25 ? 294 PHE A N     1 
ATOM   2434  C  CA    . PHE A 1 294 ? -9.023  27.033  17.464  1 46.16 ? 294 PHE A CA    1 
ATOM   2435  C  C     . PHE A 1 294 ? -8.588  26.066  18.555  1 46.23 ? 294 PHE A C     1 
ATOM   2436  O  O     . PHE A 1 294 ? -9.432  25.393  19.144  1 46.28 ? 294 PHE A O     1 
ATOM   2437  C  CB    . PHE A 1 294 ? -8.802  26.408  16.075  1 45.91 ? 294 PHE A CB    1 
ATOM   2438  C  CG    . PHE A 1 294 ? -9.464  25.057  15.923  1 46.31 ? 294 PHE A CG    1 
ATOM   2439  C  CD1   . PHE A 1 294 ? -10.813 24.957  15.64   1 46.9  ? 294 PHE A CD1   1 
ATOM   2440  C  CD2   . PHE A 1 294 ? -8.746  23.889  16.112  1 46.98 ? 294 PHE A CD2   1 
ATOM   2441  C  CE1   . PHE A 1 294 ? -11.425 23.718  15.533  1 47.46 ? 294 PHE A CE1   1 
ATOM   2442  C  CE2   . PHE A 1 294 ? -9.365  22.654  16.019  1 47.54 ? 294 PHE A CE2   1 
ATOM   2443  C  CZ    . PHE A 1 294 ? -10.695 22.575  15.718  1 47.26 ? 294 PHE A CZ    1 
ATOM   2444  N  N     . ASN A 1 295 ? -7.282  26.006  18.845  1 46.21 ? 295 ASN A N     1 
ATOM   2445  C  CA    . ASN A 1 295 ? -6.776  25.118  19.887  1 46.87 ? 295 ASN A CA    1 
ATOM   2446  C  C     . ASN A 1 295 ? -7.361  25.487  21.252  1 47.29 ? 295 ASN A C     1 
ATOM   2447  O  O     . ASN A 1 295 ? -7.718  24.596  22.017  1 47.45 ? 295 ASN A O     1 
ATOM   2448  C  CB    . ASN A 1 295 ? -5.247  25.11   19.92   1 47.94 ? 295 ASN A CB    1 
ATOM   2449  C  CG    . ASN A 1 295 ? -4.662  23.875  20.565  1 50.71 ? 295 ASN A CG    1 
ATOM   2450  O  OD1   . ASN A 1 295 ? -5.364  22.905  20.871  1 51.85 ? 295 ASN A OD1   1 
ATOM   2451  N  ND2   . ASN A 1 295 ? -3.358  23.88   20.789  1 51.05 ? 295 ASN A ND2   1 
ATOM   2452  N  N     . ASN A 1 296 ? -7.537  26.792  21.52   1 47.24 ? 296 ASN A N     1 
ATOM   2453  C  CA    . ASN A 1 296 ? -8.144  27.251  22.766  1 47.75 ? 296 ASN A CA    1 
ATOM   2454  C  C     . ASN A 1 296 ? -9.591  26.787  22.86   1 47.42 ? 296 ASN A C     1 
ATOM   2455  O  O     . ASN A 1 296 ? -10.028 26.389  23.935  1 47.62 ? 296 ASN A O     1 
ATOM   2456  C  CB    . ASN A 1 296 ? -8.078  28.773  22.882  1 49.65 ? 296 ASN A CB    1 
ATOM   2457  C  CG    . ASN A 1 296 ? -6.679  29.335  22.938  1 54.06 ? 296 ASN A CG    1 
ATOM   2458  O  OD1   . ASN A 1 296 ? -6.409  30.439  22.443  1 55.7  ? 296 ASN A OD1   1 
ATOM   2459  N  ND2   . ASN A 1 296 ? -5.749  28.592  23.525  1 54.95 ? 296 ASN A ND2   1 
ATOM   2460  N  N     . ILE A 1 297 ? -10.332 26.82   21.738  1 46.75 ? 297 ILE A N     1 
ATOM   2461  C  CA    . ILE A 1 297 ? -11.724 26.371  21.699  1 46.53 ? 297 ILE A CA    1 
ATOM   2462  C  C     . ILE A 1 297 ? -11.798 24.881  22.003  1 46.62 ? 297 ILE A C     1 
ATOM   2463  O  O     . ILE A 1 297 ? -12.642 24.457  22.788  1 46.71 ? 297 ILE A O     1 
ATOM   2464  C  CB    . ILE A 1 297 ? -12.381 26.717  20.342  1 46.62 ? 297 ILE A CB    1 
ATOM   2465  C  CG1   . ILE A 1 297 ? -12.538 28.234  20.187  1 47.17 ? 297 ILE A CG1   1 
ATOM   2466  C  CG2   . ILE A 1 297 ? -13.721 25.994  20.159  1 47.03 ? 297 ILE A CG2   1 
ATOM   2467  C  CD1   . ILE A 1 297 ? -12.91  28.658  18.826  1 48.29 ? 297 ILE A CD1   1 
ATOM   2468  N  N     . VAL A 1 298 ? -10.891 24.085  21.422  1 46.36 ? 298 VAL A N     1 
ATOM   2469  C  CA    . VAL A 1 298 ? -10.855 22.643  21.678  1 46.35 ? 298 VAL A CA    1 
ATOM   2470  C  C     . VAL A 1 298 ? -10.61  22.358  23.164  1 46.42 ? 298 VAL A C     1 
ATOM   2471  O  O     . VAL A 1 298 ? -11.355 21.591  23.766  1 46.61 ? 298 VAL A O     1 
ATOM   2472  C  CB    . VAL A 1 298 ? -9.812  21.945  20.787  1 46.7  ? 298 VAL A CB    1 
ATOM   2473  C  CG1   . VAL A 1 298 ? -9.666  20.487  21.17   1 47.06 ? 298 VAL A CG1   1 
ATOM   2474  C  CG2   . VAL A 1 298 ? -10.196 22.071  19.325  1 47.12 ? 298 VAL A CG2   1 
ATOM   2475  N  N     . GLN A 1 299 ? -9.62   23.038  23.768  1 46.04 ? 299 GLN A N     1 
ATOM   2476  C  CA    . GLN A 1 299 ? -9.286  22.879  25.185  1 46.01 ? 299 GLN A CA    1 
ATOM   2477  C  C     . GLN A 1 299 ? -10.391 23.359  26.14   1 46.11 ? 299 GLN A C     1 
ATOM   2478  O  O     . GLN A 1 299 ? -10.373 23.016  27.317  1 46.49 ? 299 GLN A O     1 
ATOM   2479  C  CB    . GLN A 1 299 ? -7.938  23.54   25.504  1 47.23 ? 299 GLN A CB    1 
ATOM   2480  C  CG    . GLN A 1 299 ? -6.815  22.938  24.671  1 50.18 ? 299 GLN A CG    1 
ATOM   2481  C  CD    . GLN A 1 299 ? -5.433  23.358  25.096  1 53.65 ? 299 GLN A CD    1 
ATOM   2482  O  OE1   . GLN A 1 299 ? -5.187  23.702  26.252  1 54.81 ? 299 GLN A OE1   1 
ATOM   2483  N  NE2   . GLN A 1 299 ? -4.49   23.311  24.17   1 54.16 ? 299 GLN A NE2   1 
ATOM   2484  N  N     . ARG A 1 300 ? -11.371 24.105  25.635  1 45.67 ? 300 ARG A N     1 
ATOM   2485  C  CA    . ARG A 1 300 ? -12.495 24.58   26.43   1 45.66 ? 300 ARG A CA    1 
ATOM   2486  C  C     . ARG A 1 300 ? -13.525 23.463  26.65   1 44.92 ? 300 ARG A C     1 
ATOM   2487  O  O     . ARG A 1 300 ? -14.172 23.441  27.692  1 45.16 ? 300 ARG A O     1 
ATOM   2488  C  CB    . ARG A 1 300 ? -13.16  25.755  25.701  1 47.61 ? 300 ARG A CB    1 
ATOM   2489  C  CG    . ARG A 1 300 ? -14.118 26.613  26.518  1 51.96 ? 300 ARG A CG    1 
ATOM   2490  C  CD    . ARG A 1 300 ? -14.67  27.795  25.723  1 56.1  ? 300 ARG A CD    1 
ATOM   2491  N  NE    . ARG A 1 300 ? -13.646 28.796  25.448  1 59.37 ? 300 ARG A NE    1 
ATOM   2492  C  CZ    . ARG A 1 300 ? -13.533 29.469  24.309  1 61.76 ? 300 ARG A CZ    1 
ATOM   2493  N  NH1   . ARG A 1 300 ? -14.396 29.268  23.323  1 61.34 ? 300 ARG A NH1   1 
ATOM   2494  N  NH2   . ARG A 1 300 ? -12.558 30.355  24.149  1 61.95 ? 300 ARG A NH2   1 
ATOM   2495  N  N     . TYR A 1 301 ? -13.68  22.536  25.678  1 43.7  ? 301 TYR A N     1 
ATOM   2496  C  CA    . TYR A 1 301 ? -14.709 21.497  25.755  1 42.85 ? 301 TYR A CA    1 
ATOM   2497  C  C     . TYR A 1 301 ? -14.221 20.069  25.719  1 41.79 ? 301 TYR A C     1 
ATOM   2498  O  O     . TYR A 1 301 ? -15.012 19.154  25.966  1 41.73 ? 301 TYR A O     1 
ATOM   2499  C  CB    . TYR A 1 301 ? -15.689 21.656  24.592  1 42.79 ? 301 TYR A CB    1 
ATOM   2500  C  CG    . TYR A 1 301 ? -16.323 23.019  24.518  1 43.47 ? 301 TYR A CG    1 
ATOM   2501  C  CD1   . TYR A 1 301 ? -17.426 23.334  25.292  1 44.26 ? 301 TYR A CD1   1 
ATOM   2502  C  CD2   . TYR A 1 301 ? -15.86  23.971  23.629  1 44.46 ? 301 TYR A CD2   1 
ATOM   2503  C  CE1   . TYR A 1 301 ? -18.015 24.587  25.229  1 45.07 ? 301 TYR A CE1   1 
ATOM   2504  C  CE2   . TYR A 1 301 ? -16.435 25.228  23.56   1 45.42 ? 301 TYR A CE2   1 
ATOM   2505  C  CZ    . TYR A 1 301 ? -17.511 25.537  24.365  1 46.09 ? 301 TYR A CZ    1 
ATOM   2506  O  OH    . TYR A 1 301 ? -18.089 26.777  24.274  1 47.64 ? 301 TYR A OH    1 
ATOM   2507  N  N     . SER A 1 302 ? -12.965 19.857  25.348  1 40.78 ? 302 SER A N     1 
ATOM   2508  C  CA    . SER A 1 302 ? -12.432 18.516  25.185  1 40.3  ? 302 SER A CA    1 
ATOM   2509  C  C     . SER A 1 302 ? -12.2   17.733  26.473  1 39.92 ? 302 SER A C     1 
ATOM   2510  O  O     . SER A 1 302 ? -12.035 18.3    27.551  1 40.35 ? 302 SER A O     1 
ATOM   2511  C  CB    . SER A 1 302 ? -11.143 18.552  24.37   1 40.7  ? 302 SER A CB    1 
ATOM   2512  O  OG    . SER A 1 302 ? -10.078 19.13   25.107  1 41.86 ? 302 SER A OG    1 
ATOM   2513  N  N     . VAL A 1 303 ? -12.231 16.412  26.336  1 38.77 ? 303 VAL A N     1 
ATOM   2514  C  CA    . VAL A 1 303 ? -11.878 15.444  27.348  1 38.34 ? 303 VAL A CA    1 
ATOM   2515  C  C     . VAL A 1 303 ? -10.75  14.615  26.706  1 38.08 ? 303 VAL A C     1 
ATOM   2516  O  O     . VAL A 1 303 ? -10.745 14.372  25.492  1 38.5  ? 303 VAL A O     1 
ATOM   2517  C  CB    . VAL A 1 303 ? -13.067 14.595  27.862  1 39.02 ? 303 VAL A CB    1 
ATOM   2518  C  CG1   . VAL A 1 303 ? -14.104 15.472  28.548  1 39.58 ? 303 VAL A CG1   1 
ATOM   2519  C  CG2   . VAL A 1 303 ? -13.71  13.787  26.746  1 39.55 ? 303 VAL A CG2   1 
ATOM   2520  N  N     . GLY A 1 304 ? -9.753  14.278  27.5    1 37.19 ? 304 GLY A N     1 
ATOM   2521  C  CA    . GLY A 1 304 ? -8.588  13.555  27.016  1 36.69 ? 304 GLY A CA    1 
ATOM   2522  C  C     . GLY A 1 304 ? -8.88   12.127  26.626  1 36.14 ? 304 GLY A C     1 
ATOM   2523  O  O     . GLY A 1 304 ? -9.637  11.436  27.3    1 36.46 ? 304 GLY A O     1 
ATOM   2524  N  N     . LEU A 1 305 ? -8.296  11.68   25.523  1 35.48 ? 305 LEU A N     1 
ATOM   2525  C  CA    . LEU A 1 305 ? -8.459  10.309  25.056  1 35.16 ? 305 LEU A CA    1 
ATOM   2526  C  C     . LEU A 1 305 ? -7.092  9.646   25.159  1 34.4  ? 305 LEU A C     1 
ATOM   2527  O  O     . LEU A 1 305 ? -6.208  9.952   24.357  1 34.53 ? 305 LEU A O     1 
ATOM   2528  C  CB    . LEU A 1 305 ? -8.947  10.293  23.601  1 35.51 ? 305 LEU A CB    1 
ATOM   2529  C  CG    . LEU A 1 305 ? -9.405  8.935   23.086  1 37.29 ? 305 LEU A CG    1 
ATOM   2530  C  CD1   . LEU A 1 305 ? -10.675 8.474   23.796  1 37.92 ? 305 LEU A CD1   1 
ATOM   2531  C  CD2   . LEU A 1 305 ? -9.628  8.969   21.586  1 37.93 ? 305 LEU A CD2   1 
ATOM   2532  N  N     . ALA A 1 306 ? -6.9    8.783   26.179  1 33.43 ? 306 ALA A N     1 
ATOM   2533  C  CA    . ALA A 1 306 ? -5.663  8.047   26.494  1 33.12 ? 306 ALA A CA    1 
ATOM   2534  C  C     . ALA A 1 306 ? -4.564  8.91    27.113  1 32.54 ? 306 ALA A C     1 
ATOM   2535  O  O     . ALA A 1 306 ? -3.95   8.504   28.093  1 32.7  ? 306 ALA A O     1 
ATOM   2536  C  CB    . ALA A 1 306 ? -5.13   7.285   25.283  1 33.3  ? 306 ALA A CB    1 
ATOM   2537  N  N     . SER A 1 307 ? -4.29   10.074  26.535  1 31.79 ? 307 SER A N     1 
ATOM   2538  C  CA    . SER A 1 307 ? -3.281  10.989  27.056  1 31.56 ? 307 SER A CA    1 
ATOM   2539  C  C     . SER A 1 307 ? -3.666  12.418  26.712  1 31.16 ? 307 SER A C     1 
ATOM   2540  O  O     . SER A 1 307 ? -4.183  12.671  25.622  1 31.27 ? 307 SER A O     1 
ATOM   2541  C  CB    . SER A 1 307 ? -1.913  10.683  26.462  1 32.69 ? 307 SER A CB    1 
ATOM   2542  O  OG    . SER A 1 307 ? -1.359  9.5     27.013  1 34.67 ? 307 SER A OG    1 
ATOM   2543  N  N     . SER A 1 308 ? -3.396  13.359  27.622  1 30.47 ? 308 SER A N     1 
ATOM   2544  C  CA    . SER A 1 308 ? -3.718  14.759  27.386  1 30.16 ? 308 SER A CA    1 
ATOM   2545  C  C     . SER A 1 308 ? -2.977  15.326  26.175  1 29.51 ? 308 SER A C     1 
ATOM   2546  O  O     . SER A 1 308 ? -3.535  16.156  25.46   1 29.77 ? 308 SER A O     1 
ATOM   2547  C  CB    . SER A 1 308 ? -3.409  15.599  28.623  1 31.37 ? 308 SER A CB    1 
ATOM   2548  O  OG    . SER A 1 308 ? -2.014  15.725  28.844  1 33.31 ? 308 SER A OG    1 
ATOM   2549  N  N     . ASP A 1 309 ? -1.735  14.871  25.93   1 28.57 ? 309 ASP A N     1 
ATOM   2550  C  CA    . ASP A 1 309 ? -0.947  15.417  24.833  1 28.1  ? 309 ASP A CA    1 
ATOM   2551  C  C     . ASP A 1 309 ? -0.882  14.554  23.579  1 27.31 ? 309 ASP A C     1 
ATOM   2552  O  O     . ASP A 1 309 ? -0.061  14.841  22.715  1 27.35 ? 309 ASP A O     1 
ATOM   2553  C  CB    . ASP A 1 309 ? 0.463   15.813  25.283  1 29.78 ? 309 ASP A CB    1 
ATOM   2554  C  CG    . ASP A 1 309 ? 1.332   14.683  25.791  1 34.25 ? 309 ASP A CG    1 
ATOM   2555  O  OD1   . ASP A 1 309 ? 0.774   13.652  26.239  1 34.21 ? 309 ASP A OD1   1 
ATOM   2556  O  OD2   . ASP A 1 309 ? 2.57    14.835  25.762  1 37    ? 309 ASP A OD2   1 
ATOM   2557  N  N     . LEU A 1 310 ? -1.77   13.566  23.43   1 26.62 ? 310 LEU A N     1 
ATOM   2558  C  CA    . LEU A 1 310 ? -1.854  12.829  22.169  1 26.75 ? 310 LEU A CA    1 
ATOM   2559  C  C     . LEU A 1 310 ? -2.548  13.78   21.169  1 27.47 ? 310 LEU A C     1 
ATOM   2560  O  O     . LEU A 1 310 ? -3.268  14.679  21.607  1 27.55 ? 310 LEU A O     1 
ATOM   2561  C  CB    . LEU A 1 310 ? -2.638  11.522  22.335  1 26.53 ? 310 LEU A CB    1 
ATOM   2562  C  CG    . LEU A 1 310 ? -1.816  10.34   22.822  1 27.49 ? 310 LEU A CG    1 
ATOM   2563  C  CD1   . LEU A 1 310 ? -2.685  9.146   23.039  1 27.78 ? 310 LEU A CD1   1 
ATOM   2564  C  CD2   . LEU A 1 310 ? -0.692  10      21.853  1 28.27 ? 310 LEU A CD2   1 
ATOM   2565  N  N     . PRO A 1 311 ? -2.343  13.65   19.837  1 27.84 ? 311 PRO A N     1 
ATOM   2566  C  CA    . PRO A 1 311 ? -2.941  14.629  18.9    1 28.2  ? 311 PRO A CA    1 
ATOM   2567  C  C     . PRO A 1 311 ? -4.449  14.554  18.689  1 28.78 ? 311 PRO A C     1 
ATOM   2568  O  O     . PRO A 1 311 ? -4.952  15.129  17.733  1 28.87 ? 311 PRO A O     1 
ATOM   2569  C  CB    . PRO A 1 311 ? -2.2    14.352  17.59   1 28.74 ? 311 PRO A CB    1 
ATOM   2570  C  CG    . PRO A 1 311 ? -1.864  12.905  17.674  1 29.03 ? 311 PRO A CG    1 
ATOM   2571  C  CD    . PRO A 1 311 ? -1.502  12.671  19.119  1 27.35 ? 311 PRO A CD    1 
ATOM   2572  N  N     . PHE A 1 312 ? -5.166  13.863  19.564  1 29.08 ? 312 PHE A N     1 
ATOM   2573  C  CA    . PHE A 1 312 ? -6.608  13.722  19.447  1 29.81 ? 312 PHE A CA    1 
ATOM   2574  C  C     . PHE A 1 312 ? -7.287  13.681  20.811  1 31.32 ? 312 PHE A C     1 
ATOM   2575  O  O     . PHE A 1 312 ? -6.68   13.309  21.815  1 31.58 ? 312 PHE A O     1 
ATOM   2576  C  CB    . PHE A 1 312 ? -6.983  12.49   18.604  1 29.23 ? 312 PHE A CB    1 
ATOM   2577  C  CG    . PHE A 1 312 ? -6.244  11.238  18.999  1 29.53 ? 312 PHE A CG    1 
ATOM   2578  C  CD1   . PHE A 1 312 ? -5.009  10.94   18.452  1 30.09 ? 312 PHE A CD1   1 
ATOM   2579  C  CD2   . PHE A 1 312 ? -6.78   10.361  19.922  1 30.29 ? 312 PHE A CD2   1 
ATOM   2580  C  CE1   . PHE A 1 312 ? -4.322  9.801   18.834  1 30.75 ? 312 PHE A CE1   1 
ATOM   2581  C  CE2   . PHE A 1 312 ? -6.089  9.221   20.303  1 30.87 ? 312 PHE A CE2   1 
ATOM   2582  C  CZ    . PHE A 1 312 ? -4.863  8.953   19.762  1 30.62 ? 312 PHE A CZ    1 
ATOM   2583  N  N     . GLY A 1 313 ? -8.545  14.069  20.829  1 32.14 ? 313 GLY A N     1 
ATOM   2584  C  CA    . GLY A 1 313 ? -9.361  14.062  22.032  1 33.52 ? 313 GLY A CA    1 
ATOM   2585  C  C     . GLY A 1 313 ? -10.828 13.92   21.7    1 34.88 ? 313 GLY A C     1 
ATOM   2586  O  O     . GLY A 1 313 ? -11.185 13.707  20.537  1 34.92 ? 313 GLY A O     1 
ATOM   2587  N  N     . VAL A 1 314 ? -11.696 14.011  22.715  1 35.84 ? 314 VAL A N     1 
ATOM   2588  C  CA    . VAL A 1 314 ? -13.128 13.859  22.484  1 37.28 ? 314 VAL A CA    1 
ATOM   2589  C  C     . VAL A 1 314 ? -13.899 15.089  22.898  1 38.44 ? 314 VAL A C     1 
ATOM   2590  O  O     . VAL A 1 314 ? -13.57  15.717  23.894  1 38.42 ? 314 VAL A O     1 
ATOM   2591  C  CB    . VAL A 1 314 ? -13.695 12.599  23.188  1 38.35 ? 314 VAL A CB    1 
ATOM   2592  C  CG1   . VAL A 1 314 ? -15.173 12.4    22.865  1 38.95 ? 314 VAL A CG1   1 
ATOM   2593  C  CG2   . VAL A 1 314 ? -12.895 11.351  22.83   1 39.16 ? 314 VAL A CG2   1 
ATOM   2594  N  N     . ILE A 1 315 ? -14.915 15.44   22.116  1 39.35 ? 315 ILE A N     1 
ATOM   2595  C  CA    . ILE A 1 315 ? -15.876 16.479  22.422  1 40.75 ? 315 ILE A CA    1 
ATOM   2596  C  C     . ILE A 1 315 ? -17.153 15.667  22.607  1 42.05 ? 315 ILE A C     1 
ATOM   2597  O  O     . ILE A 1 315 ? -17.676 15.132  21.626  1 42.21 ? 315 ILE A O     1 
ATOM   2598  C  CB    . ILE A 1 315 ? -16.049 17.496  21.28   1 41.36 ? 315 ILE A CB    1 
ATOM   2599  C  CG1   . ILE A 1 315 ? -14.72  18.185  20.909  1 42.45 ? 315 ILE A CG1   1 
ATOM   2600  C  CG2   . ILE A 1 315 ? -17.151 18.498  21.627  1 41.8  ? 315 ILE A CG2   1 
ATOM   2601  C  CD1   . ILE A 1 315 ? -14.158 19.119  21.918  1 43.99 ? 315 ILE A CD1   1 
ATOM   2602  N  N     . ARG A 1 316 ? -17.596 15.484  23.863  1 42.63 ? 316 ARG A N     1 
ATOM   2603  C  CA    . ARG A 1 316 ? -18.796 14.705  24.154  1 43.63 ? 316 ARG A CA    1 
ATOM   2604  C  C     . ARG A 1 316 ? -20.032 15.332  23.509  1 44.21 ? 316 ARG A C     1 
ATOM   2605  O  O     . ARG A 1 316 ? -20.061 16.545  23.306  1 44.35 ? 316 ARG A O     1 
ATOM   2606  C  CB    . ARG A 1 316 ? -18.987 14.548  25.669  1 45.41 ? 316 ARG A CB    1 
ATOM   2607  C  CG    . ARG A 1 316 ? -17.826 13.836  26.361  1 48.91 ? 316 ARG A CG    1 
ATOM   2608  C  CD    . ARG A 1 316 ? -18.197 13.31   27.736  1 52.17 ? 316 ARG A CD    1 
ATOM   2609  N  NE    . ARG A 1 316 ? -18.52  14.382  28.679  1 55.42 ? 316 ARG A NE    1 
ATOM   2610  C  CZ    . ARG A 1 316 ? -17.996 14.492  29.897  1 58.4  ? 316 ARG A CZ    1 
ATOM   2611  N  NH1   . ARG A 1 316 ? -17.091 13.616  30.322  1 57.88 ? 316 ARG A NH1   1 
ATOM   2612  N  NH2   . ARG A 1 316 ? -18.362 15.486  30.695  1 59.14 ? 316 ARG A NH2   1 
ATOM   2613  N  N     . LYS A 1 317 ? -21.05  14.523  23.177  1 44.48 ? 317 LYS A N     1 
ATOM   2614  C  CA    . LYS A 1 317 ? -22.261 15.048  22.538  1 45.33 ? 317 LYS A CA    1 
ATOM   2615  C  C     . LYS A 1 317 ? -22.936 16.16   23.345  1 45.88 ? 317 LYS A C     1 
ATOM   2616  O  O     . LYS A 1 317 ? -23.524 17.073  22.763  1 45.94 ? 317 LYS A O     1 
ATOM   2617  C  CB    . LYS A 1 317 ? -23.25  13.925  22.192  1 47.41 ? 317 LYS A CB    1 
ATOM   2618  C  CG    . LYS A 1 317 ? -23.685 13.084  23.379  1 52.01 ? 317 LYS A CG    1 
ATOM   2619  C  CD    . LYS A 1 317 ? -24.602 11.958  22.941  1 57.16 ? 317 LYS A CD    1 
ATOM   2620  C  CE    . LYS A 1 317 ? -24.857 10.985  24.062  1 61.46 ? 317 LYS A CE    1 
ATOM   2621  N  NZ    . LYS A 1 317 ? -23.604 10.308  24.5    1 63.93 ? 317 LYS A NZ    1 
ATOM   2622  N  N     . GLU A 1 318 ? -22.783 16.116  24.68   1 46.12 ? 318 GLU A N     1 
ATOM   2623  C  CA    . GLU A 1 318 ? -23.323 17.104  25.613  1 46.9  ? 318 GLU A CA    1 
ATOM   2624  C  C     . GLU A 1 318 ? -22.669 18.495  25.457  1 47.62 ? 318 GLU A C     1 
ATOM   2625  O  O     . GLU A 1 318 ? -23.269 19.496  25.843  1 47.85 ? 318 GLU A O     1 
ATOM   2626  C  CB    . GLU A 1 318 ? -23.191 16.6    27.059  1 48.8  ? 318 GLU A CB    1 
ATOM   2627  C  CG    . GLU A 1 318 ? -24.047 15.384  27.377  1 52.6  ? 318 GLU A CG    1 
ATOM   2628  C  CD    . GLU A 1 318 ? -23.483 14.038  26.96   1 57.12 ? 318 GLU A CD    1 
ATOM   2629  O  OE1   . GLU A 1 318 ? -22.258 13.957  26.712  1 58.17 ? 318 GLU A OE1   1 
ATOM   2630  O  OE2   . GLU A 1 318 ? -24.266 13.064  26.879  1 58.3  ? 318 GLU A OE2   1 
ATOM   2631  N  N     . SER A 1 319 ? -21.45  18.556  24.894  1 47.77 ? 319 SER A N     1 
ATOM   2632  C  CA    . SER A 1 319 ? -20.73  19.811  24.658  1 48.35 ? 319 SER A CA    1 
ATOM   2633  C  C     . SER A 1 319 ? -20.552 20.139  23.172  1 48.81 ? 319 SER A C     1 
ATOM   2634  O  O     . SER A 1 319 ? -20.01  21.2    22.869  1 49.09 ? 319 SER A O     1 
ATOM   2635  C  CB    . SER A 1 319 ? -19.348 19.767  25.302  1 49.79 ? 319 SER A CB    1 
ATOM   2636  O  OG    . SER A 1 319 ? -19.414 19.589  26.705  1 52.44 ? 319 SER A OG    1 
ATOM   2637  N  N     . ARG A 1 320 ? -20.947 19.23   22.253  1 48.74 ? 320 ARG A N     1 
ATOM   2638  C  CA    . ARG A 1 320 ? -20.793 19.404  20.809  1 49.1  ? 320 ARG A CA    1 
ATOM   2639  C  C     . ARG A 1 320 ? -21.467 20.66   20.28   1 49.53 ? 320 ARG A C     1 
ATOM   2640  O  O     . ARG A 1 320 ? -20.856 21.372  19.493  1 49.63 ? 320 ARG A O     1 
ATOM   2641  C  CB    . ARG A 1 320 ? -21.271 18.152  20.046  1 50.23 ? 320 ARG A CB    1 
ATOM   2642  C  CG    . ARG A 1 320 ? -21.287 18.296  18.518  1 52.57 ? 320 ARG A CG    1 
ATOM   2643  C  CD    . ARG A 1 320 ? -20.054 17.75   17.834  1 55.14 ? 320 ARG A CD    1 
ATOM   2644  N  NE    . ARG A 1 320 ? -20.231 16.329  17.612  1 57.73 ? 320 ARG A NE    1 
ATOM   2645  C  CZ    . ARG A 1 320 ? -20.551 15.737  16.467  1 59.85 ? 320 ARG A CZ    1 
ATOM   2646  N  NH1   . ARG A 1 320 ? -20.728 14.421  16.428  1 59.46 ? 320 ARG A NH1   1 
ATOM   2647  N  NH2   . ARG A 1 320 ? -20.607 16.432  15.343  1 59.6  ? 320 ARG A NH2   1 
ATOM   2648  N  N     . ASN A 1 321 ? -22.7   20.954  20.721  1 49.62 ? 321 ASN A N     1 
ATOM   2649  C  CA    . ASN A 1 321 ? -23.416 22.146  20.264  1 50.08 ? 321 ASN A CA    1 
ATOM   2650  C  C     . ASN A 1 321 ? -22.631 23.43   20.547  1 50.42 ? 321 ASN A C     1 
ATOM   2651  O  O     . ASN A 1 321 ? -22.451 24.247  19.646  1 50.55 ? 321 ASN A O     1 
ATOM   2652  C  CB    . ASN A 1 321 ? -24.817 22.213  20.877  1 50.94 ? 321 ASN A CB    1 
ATOM   2653  C  CG    . ASN A 1 321 ? -25.919 22.285  19.85   1 53.8  ? 321 ASN A CG    1 
ATOM   2654  O  OD1   . ASN A 1 321 ? -26.393 21.264  19.343  1 54.99 ? 321 ASN A OD1   1 
ATOM   2655  N  ND2   . ASN A 1 321 ? -26.354 23.49   19.523  1 54.28 ? 321 ASN A ND2   1 
ATOM   2656  N  N     . ASP A 1 322 ? -22.115 23.575  21.774  1 50.36 ? 322 ASP A N     1 
ATOM   2657  C  CA    . ASP A 1 322 ? -21.348 24.756  22.161  1 50.79 ? 322 ASP A CA    1 
ATOM   2658  C  C     . ASP A 1 322 ? -19.999 24.829  21.454  1 50.54 ? 322 ASP A C     1 
ATOM   2659  O  O     . ASP A 1 322 ? -19.572 25.924  21.083  1 50.71 ? 322 ASP A O     1 
ATOM   2660  C  CB    . ASP A 1 322 ? -21.165 24.811  23.681  1 52.79 ? 322 ASP A CB    1 
ATOM   2661  C  CG    . ASP A 1 322 ? -22.423 25.173  24.436  1 57.78 ? 322 ASP A CG    1 
ATOM   2662  O  OD1   . ASP A 1 322 ? -23.255 25.915  23.878  1 58.51 ? 322 ASP A OD1   1 
ATOM   2663  O  OD2   . ASP A 1 322 ? -22.571 24.723  25.593  1 60.28 ? 322 ASP A OD2   1 
ATOM   2664  N  N     . PHE A 1 323 ? -19.338 23.671  21.256  1 49.87 ? 323 PHE A N     1 
ATOM   2665  C  CA    . PHE A 1 323 ? -18.06  23.62   20.551  1 49.88 ? 323 PHE A CA    1 
ATOM   2666  C  C     . PHE A 1 323 ? -18.268 24.086  19.098  1 49.85 ? 323 PHE A C     1 
ATOM   2667  O  O     . PHE A 1 323 ? -17.561 24.984  18.643  1 49.95 ? 323 PHE A O     1 
ATOM   2668  C  CB    . PHE A 1 323 ? -17.455 22.204  20.61   1 49.74 ? 323 PHE A CB    1 
ATOM   2669  C  CG    . PHE A 1 323 ? -16.339 21.933  19.622  1 50.41 ? 323 PHE A CG    1 
ATOM   2670  C  CD1   . PHE A 1 323 ? -15.067 22.432  19.834  1 51.17 ? 323 PHE A CD1   1 
ATOM   2671  C  CD2   . PHE A 1 323 ? -16.562 21.166  18.491  1 51.13 ? 323 PHE A CD2   1 
ATOM   2672  C  CE1   . PHE A 1 323 ? -14.044 22.181  18.926  1 51.75 ? 323 PHE A CE1   1 
ATOM   2673  C  CE2   . PHE A 1 323 ? -15.537 20.916  17.586  1 51.69 ? 323 PHE A CE2   1 
ATOM   2674  C  CZ    . PHE A 1 323 ? -14.286 21.424  17.81   1 51.44 ? 323 PHE A CZ    1 
ATOM   2675  N  N     . ILE A 1 324 ? -19.285 23.531  18.408  1 49.5  ? 324 ILE A N     1 
ATOM   2676  C  CA    . ILE A 1 324 ? -19.61  23.895  17.028  1 49.5  ? 324 ILE A CA    1 
ATOM   2677  C  C     . ILE A 1 324 ? -19.944 25.381  16.906  1 49.67 ? 324 ILE A C     1 
ATOM   2678  O  O     . ILE A 1 324 ? -19.446 26.029  15.99   1 50.06 ? 324 ILE A O     1 
ATOM   2679  C  CB    . ILE A 1 324 ? -20.705 22.973  16.428  1 49.78 ? 324 ILE A CB    1 
ATOM   2680  C  CG1   . ILE A 1 324 ? -20.222 21.51   16.34   1 50.55 ? 324 ILE A CG1   1 
ATOM   2681  C  CG2   . ILE A 1 324 ? -21.186 23.47   15.072  1 50.18 ? 324 ILE A CG2   1 
ATOM   2682  C  CD1   . ILE A 1 324 ? -18.929 21.299  15.59   1 51.73 ? 324 ILE A CD1   1 
ATOM   2683  N  N     . ASN A 1 325 ? -20.707 25.942  17.865  1 49.33 ? 325 ASN A N     1 
ATOM   2684  C  CA    . ASN A 1 325 ? -21.046 27.369  17.87   1 49.6  ? 325 ASN A CA    1 
ATOM   2685  C  C     . ASN A 1 325 ? -19.779 28.23   17.917  1 49.47 ? 325 ASN A C     1 
ATOM   2686  O  O     . ASN A 1 325 ? -19.668 29.213  17.181  1 49.44 ? 325 ASN A O     1 
ATOM   2687  C  CB    . ASN A 1 325 ? -21.942 27.71   19.063  1 50.89 ? 325 ASN A CB    1 
ATOM   2688  C  CG    . ASN A 1 325 ? -23.401 27.388  18.875  1 54.04 ? 325 ASN A CG    1 
ATOM   2689  O  OD1   . ASN A 1 325 ? -23.86  27.11   17.765  1 55.12 ? 325 ASN A OD1   1 
ATOM   2690  N  ND2   . ASN A 1 325 ? -24.157 27.429  19.97   1 54.63 ? 325 ASN A ND2   1 
ATOM   2691  N  N     . ASP A 1 326 ? -18.817 27.839  18.765  1 49.22 ? 326 ASP A N     1 
ATOM   2692  C  CA    . ASP A 1 326 ? -17.557 28.557  18.908  1 49.53 ? 326 ASP A CA    1 
ATOM   2693  C  C     . ASP A 1 326 ? -16.695 28.465  17.66   1 49.69 ? 326 ASP A C     1 
ATOM   2694  O  O     . ASP A 1 326 ? -16.09  29.462  17.265  1 49.94 ? 326 ASP A O     1 
ATOM   2695  C  CB    . ASP A 1 326 ? -16.793 28.076  20.15   1 51.01 ? 326 ASP A CB    1 
ATOM   2696  C  CG    . ASP A 1 326 ? -17.238 28.728  21.446  1 55.03 ? 326 ASP A CG    1 
ATOM   2697  O  OD1   . ASP A 1 326 ? -17.963 29.738  21.384  1 55.94 ? 326 ASP A OD1   1 
ATOM   2698  O  OD2   . ASP A 1 326 ? -16.817 28.257  22.522  1 56.46 ? 326 ASP A OD2   1 
ATOM   2699  N  N     . VAL A 1 327 ? -16.655 27.288  17.021  1 49.4  ? 327 VAL A N     1 
ATOM   2700  C  CA    . VAL A 1 327 ? -15.891 27.128  15.79   1 49.68 ? 327 VAL A CA    1 
ATOM   2701  C  C     . VAL A 1 327 ? -16.516 27.982  14.679  1 49.88 ? 327 VAL A C     1 
ATOM   2702  O  O     . VAL A 1 327 ? -15.79  28.66   13.953  1 50.15 ? 327 VAL A O     1 
ATOM   2703  C  CB    . VAL A 1 327 ? -15.747 25.647  15.378  1 50.34 ? 327 VAL A CB    1 
ATOM   2704  C  CG1   . VAL A 1 327 ? -15.05  25.519  14.027  1 50.96 ? 327 VAL A CG1   1 
ATOM   2705  C  CG2   . VAL A 1 327 ? -14.99  24.864  16.438  1 50.74 ? 327 VAL A CG2   1 
ATOM   2706  N  N     . CYS A 1 328 ? -17.86  28.013  14.605  1 49.55 ? 328 CYS A N     1 
ATOM   2707  C  CA    . CYS A 1 328 ? -18.599 28.801  13.618  1 49.75 ? 328 CYS A CA    1 
ATOM   2708  C  C     . CYS A 1 328 ? -18.348 30.284  13.786  1 50.12 ? 328 CYS A C     1 
ATOM   2709  O  O     . CYS A 1 328 ? -18.213 31      12.798  1 50.18 ? 328 CYS A O     1 
ATOM   2710  C  CB    . CYS A 1 328 ? -20.089 28.48   13.662  1 50.06 ? 328 CYS A CB    1 
ATOM   2711  S  SG    . CYS A 1 328 ? -20.509 26.832  13.039  1 52.74 ? 328 CYS A SG    1 
ATOM   2712  N  N     . LYS A 1 329 ? -18.274 30.748  15.035  1 50.34 ? 329 LYS A N     1 
ATOM   2713  C  CA    . LYS A 1 329 ? -18.016 32.157  15.329  1 50.84 ? 329 LYS A CA    1 
ATOM   2714  C  C     . LYS A 1 329 ? -16.592 32.529  14.884  1 51.34 ? 329 LYS A C     1 
ATOM   2715  O  O     . LYS A 1 329 ? -16.387 33.574  14.266  1 51.57 ? 329 LYS A O     1 
ATOM   2716  C  CB    . LYS A 1 329 ? -18.195 32.432  16.834  1 52.03 ? 329 LYS A CB    1 
ATOM   2717  C  CG    . LYS A 1 329 ? -19.002 33.684  17.142  1 55.3  ? 329 LYS A CG    1 
ATOM   2718  C  CD    . LYS A 1 329 ? -20.492 33.432  16.974  1 59.08 ? 329 LYS A CD    1 
ATOM   2719  C  CE    . LYS A 1 329 ? -21.324 34.664  17.211  1 62.45 ? 329 LYS A CE    1 
ATOM   2720  N  NZ    . LYS A 1 329 ? -22.772 34.376  17.041  1 64.48 ? 329 LYS A NZ    1 
ATOM   2721  N  N     . LEU A 1 330 ? -15.618 31.659  15.176  1 51.3  ? 330 LEU A N     1 
ATOM   2722  C  CA    . LEU A 1 330 ? -14.218 31.901  14.837  1 51.65 ? 330 LEU A CA    1 
ATOM   2723  C  C     . LEU A 1 330 ? -13.972 31.978  13.338  1 51.67 ? 330 LEU A C     1 
ATOM   2724  O  O     . LEU A 1 330 ? -13.255 32.864  12.877  1 51.6  ? 330 LEU A O     1 
ATOM   2725  C  CB    . LEU A 1 330 ? -13.323 30.813  15.464  1 52.01 ? 330 LEU A CB    1 
ATOM   2726  C  CG    . LEU A 1 330 ? -11.826 30.93   15.177  1 53.59 ? 330 LEU A CG    1 
ATOM   2727  C  CD1   . LEU A 1 330 ? -11.26  32.22   15.745  1 54.34 ? 330 LEU A CD1   1 
ATOM   2728  C  CD2   . LEU A 1 330 ? -11.072 29.742  15.717  1 54.1  ? 330 LEU A CD2   1 
ATOM   2729  N  N     . TYR A 1 331 ? -14.558 31.055  12.58   1 51.81 ? 331 TYR A N     1 
ATOM   2730  C  CA    . TYR A 1 331 ? -14.322 30.977  11.147  1 52.55 ? 331 TYR A CA    1 
ATOM   2731  C  C     . TYR A 1 331 ? -15.444 31.537  10.268  1 53.73 ? 331 TYR A C     1 
ATOM   2732  O  O     . TYR A 1 331 ? -15.398 31.358  9.05    1 53.86 ? 331 TYR A O     1 
ATOM   2733  C  CB    . TYR A 1 331 ? -14.001 29.531  10.758  1 52.22 ? 331 TYR A CB    1 
ATOM   2734  C  CG    . TYR A 1 331 ? -12.66  29.07   11.284  1 52.56 ? 331 TYR A CG    1 
ATOM   2735  C  CD1   . TYR A 1 331 ? -11.484 29.669  10.861  1 53.31 ? 331 TYR A CD1   1 
ATOM   2736  C  CD2   . TYR A 1 331 ? -12.567 28.023  12.189  1 53.41 ? 331 TYR A CD2   1 
ATOM   2737  C  CE1   . TYR A 1 331 ? -10.248 29.238  11.323  1 54.15 ? 331 TYR A CE1   1 
ATOM   2738  C  CE2   . TYR A 1 331 ? -11.336 27.585  12.661  1 54.24 ? 331 TYR A CE2   1 
ATOM   2739  C  CZ    . TYR A 1 331 ? -10.177 28.195  12.223  1 55.03 ? 331 TYR A CZ    1 
ATOM   2740  O  OH    . TYR A 1 331 ? -8.953  27.779  12.686  1 56.43 ? 331 TYR A OH    1 
ATOM   2741  N  N     . ASN A 1 332 ? -16.415 32.239  10.869  1 54.39 ? 332 ASN A N     1 
ATOM   2742  C  CA    . ASN A 1 332 ? -17.536 32.851  10.155  1 55.58 ? 332 ASN A CA    1 
ATOM   2743  C  C     . ASN A 1 332 ? -18.346 31.843  9.334   1 56.41 ? 332 ASN A C     1 
ATOM   2744  O  O     . ASN A 1 332 ? -18.666 32.099  8.174   1 56.33 ? 332 ASN A O     1 
ATOM   2745  C  CB    . ASN A 1 332 ? -17.084 34.043  9.303   1 56.86 ? 332 ASN A CB    1 
ATOM   2746  C  CG    . ASN A 1 332 ? -18.145 35.098  9.132   1 60.25 ? 332 ASN A CG    1 
ATOM   2747  O  OD1   . ASN A 1 332 ? -18.936 35.373  10.043  1 61.62 ? 332 ASN A OD1   1 
ATOM   2748  N  ND2   . ASN A 1 332 ? -18.18  35.718  7.961   1 60.88 ? 332 ASN A ND2   1 
ATOM   2749  N  N     . ILE A 1 333 ? -18.678 30.7    9.94    1 57.1  ? 333 ILE A N     1 
ATOM   2750  C  CA    . ILE A 1 333 ? -19.491 29.695  9.271   1 58.45 ? 333 ILE A CA    1 
ATOM   2751  C  C     . ILE A 1 333 ? -20.95  30.052  9.525   1 59.76 ? 333 ILE A C     1 
ATOM   2752  O  O     . ILE A 1 333 ? -21.384 30.062  10.675  1 59.96 ? 333 ILE A O     1 
ATOM   2753  C  CB    . ILE A 1 333 ? -19.146 28.275  9.769   1 59.06 ? 333 ILE A CB    1 
ATOM   2754  C  CG1   . ILE A 1 333 ? -17.646 27.987  9.6     1 60.06 ? 333 ILE A CG1   1 
ATOM   2755  C  CG2   . ILE A 1 333 ? -19.997 27.232  9.047   1 59.64 ? 333 ILE A CG2   1 
ATOM   2756  C  CD1   . ILE A 1 333 ? -17.189 26.712  10.238  1 61.46 ? 333 ILE A CD1   1 
ATOM   2757  N  N     . ASN A 1 334 ? -21.697 30.395  8.467   1 60.52 ? 334 ASN A N     1 
ATOM   2758  C  CA    . ASN A 1 334 ? -23.095 30.795  8.62    1 61.77 ? 334 ASN A CA    1 
ATOM   2759  C  C     . ASN A 1 334 ? -24.103 29.909  7.877   1 62.32 ? 334 ASN A C     1 
ATOM   2760  O  O     . ASN A 1 334 ? -25.306 30.106  8.038   1 62.51 ? 334 ASN A O     1 
ATOM   2761  C  CB    . ASN A 1 334 ? -23.282 32.254  8.213   1 63.6  ? 334 ASN A CB    1 
ATOM   2762  C  CG    . ASN A 1 334 ? -22.741 33.247  9.215   1 67.61 ? 334 ASN A CG    1 
ATOM   2763  O  OD1   . ASN A 1 334 ? -21.824 34.027  8.915   1 69.24 ? 334 ASN A OD1   1 
ATOM   2764  N  ND2   . ASN A 1 334 ? -23.299 33.246  10.424  1 68.08 ? 334 ASN A ND2   1 
ATOM   2765  N  N     . ASP A 1 335 ? -23.633 28.949  7.069   1 62.37 ? 335 ASP A N     1 
ATOM   2766  C  CA    . ASP A 1 335 ? -24.531 28.075  6.319   1 62.92 ? 335 ASP A CA    1 
ATOM   2767  C  C     . ASP A 1 335 ? -25.302 27.123  7.229   1 63.43 ? 335 ASP A C     1 
ATOM   2768  O  O     . ASP A 1 335 ? -24.697 26.29   7.902   1 63.57 ? 335 ASP A O     1 
ATOM   2769  C  CB    . ASP A 1 335 ? -23.763 27.291  5.247   1 64.28 ? 335 ASP A CB    1 
ATOM   2770  C  CG    . ASP A 1 335 ? -24.678 26.649  4.232   1 68.03 ? 335 ASP A CG    1 
ATOM   2771  O  OD1   . ASP A 1 335 ? -25.263 27.386  3.412   1 68.63 ? 335 ASP A OD1   1 
ATOM   2772  O  OD2   . ASP A 1 335 ? -24.817 25.412  4.261   1 69.79 ? 335 ASP A OD2   1 
ATOM   2773  N  N     . MET A 1 336 ? -26.639 27.251  7.242   1 63.56 ? 336 MET A N     1 
ATOM   2774  C  CA    . MET A 1 336 ? -27.534 26.43   8.062   1 64.17 ? 336 MET A CA    1 
ATOM   2775  C  C     . MET A 1 336 ? -27.362 24.922  7.836   1 63.66 ? 336 MET A C     1 
ATOM   2776  O  O     . MET A 1 336 ? -27.329 24.162  8.805   1 63.79 ? 336 MET A O     1 
ATOM   2777  C  CB    . MET A 1 336 ? -29.005 26.839  7.85    1 65.77 ? 336 MET A CB    1 
ATOM   2778  C  CG    . MET A 1 336 ? -29.973 26.131  8.797   1 69.48 ? 336 MET A CG    1 
ATOM   2779  S  SD    . MET A 1 336 ? -31.716 26.472  8.443   1 77.17 ? 336 MET A SD    1 
ATOM   2780  C  CE    . MET A 1 336 ? -32.504 25.584  9.784   1 75.55 ? 336 MET A CE    1 
ATOM   2781  N  N     . LYS A 1 337 ? -27.25  24.491  6.572   1 62.93 ? 337 LYS A N     1 
ATOM   2782  C  CA    . LYS A 1 337 ? -27.086 23.075  6.24    1 62.75 ? 337 LYS A CA    1 
ATOM   2783  C  C     . LYS A 1 337 ? -25.803 22.494  6.837   1 62.29 ? 337 LYS A C     1 
ATOM   2784  O  O     . LYS A 1 337 ? -25.825 21.406  7.406   1 62.37 ? 337 LYS A O     1 
ATOM   2785  C  CB    . LYS A 1 337 ? -27.102 22.861  4.715   1 64.53 ? 337 LYS A CB    1 
ATOM   2786  C  CG    . LYS A 1 337 ? -28.361 23.367  4.021   1 68.4  ? 337 LYS A CG    1 
ATOM   2787  C  CD    . LYS A 1 337 ? -28.488 22.8    2.611   1 72.73 ? 337 LYS A CD    1 
ATOM   2788  C  CE    . LYS A 1 337 ? -27.395 23.263  1.678   1 76.52 ? 337 LYS A CE    1 
ATOM   2789  N  NZ    . LYS A 1 337 ? -27.635 24.644  1.186   1 78.9  ? 337 LYS A NZ    1 
ATOM   2790  N  N     . ILE A 1 338 ? -24.695 23.231  6.719   1 61.67 ? 338 ILE A N     1 
ATOM   2791  C  CA    . ILE A 1 338 ? -23.393 22.824  7.233   1 61.53 ? 338 ILE A CA    1 
ATOM   2792  C  C     . ILE A 1 338 ? -23.408 22.713  8.759   1 61.27 ? 338 ILE A C     1 
ATOM   2793  O  O     . ILE A 1 338 ? -22.913 21.727  9.303   1 61.33 ? 338 ILE A O     1 
ATOM   2794  C  CB    . ILE A 1 338 ? -22.31  23.808  6.725   1 61.97 ? 338 ILE A CB    1 
ATOM   2795  C  CG1   . ILE A 1 338 ? -22.095 23.645  5.212   1 62.94 ? 338 ILE A CG1   1 
ATOM   2796  C  CG2   . ILE A 1 338 ? -21.004 23.653  7.487   1 62.38 ? 338 ILE A CG2   1 
ATOM   2797  C  CD1   . ILE A 1 338 ? -21.092 24.631  4.578   1 64.19 ? 338 ILE A CD1   1 
ATOM   2798  N  N     . ILE A 1 339 ? -23.986 23.714  9.439   1 60.82 ? 339 ILE A N     1 
ATOM   2799  C  CA    . ILE A 1 339 ? -24.087 23.751  10.897  1 60.86 ? 339 ILE A CA    1 
ATOM   2800  C  C     . ILE A 1 339 ? -24.906 22.572  11.427  1 60.68 ? 339 ILE A C     1 
ATOM   2801  O  O     . ILE A 1 339 ? -24.522 21.958  12.421  1 60.7  ? 339 ILE A O     1 
ATOM   2802  C  CB    . ILE A 1 339 ? -24.657 25.115  11.349  1 61.42 ? 339 ILE A CB    1 
ATOM   2803  C  CG1   . ILE A 1 339 ? -23.708 26.259  10.959  1 62.44 ? 339 ILE A CG1   1 
ATOM   2804  C  CG2   . ILE A 1 339 ? -24.947 25.131  12.839  1 61.88 ? 339 ILE A CG2   1 
ATOM   2805  C  CD1   . ILE A 1 339 ? -24.282 27.649  11.169  1 63.77 ? 339 ILE A CD1   1 
ATOM   2806  N  N     . LYS A 1 340 ? -25.996 22.215  10.728  1 60.33 ? 340 LYS A N     1 
ATOM   2807  C  CA    . LYS A 1 340 ? -26.84  21.085  11.119  1 60.42 ? 340 LYS A CA    1 
ATOM   2808  C  C     . LYS A 1 340 ? -26.072 19.764  11.017  1 60.21 ? 340 LYS A C     1 
ATOM   2809  O  O     . LYS A 1 340 ? -26.232 18.895  11.874  1 60.33 ? 340 LYS A O     1 
ATOM   2810  C  CB    . LYS A 1 340 ? -28.118 21.036  10.267  1 62.18 ? 340 LYS A CB    1 
ATOM   2811  C  CG    . LYS A 1 340 ? -29.276 20.333  10.968  1 65.96 ? 340 LYS A CG    1 
ATOM   2812  C  CD    . LYS A 1 340 ? -30.572 20.431  10.176  1 70.03 ? 340 LYS A CD    1 
ATOM   2813  C  CE    . LYS A 1 340 ? -31.77  19.996  10.99   1 73.34 ? 340 LYS A CE    1 
ATOM   2814  N  NZ    . LYS A 1 340 ? -32.102 20.981  12.052  1 75.34 ? 340 LYS A NZ    1 
ATOM   2815  N  N     . GLU A 1 341 ? -25.223 19.625  9.99    1 59.75 ? 341 GLU A N     1 
ATOM   2816  C  CA    . GLU A 1 341 ? -24.404 18.431  9.81    1 59.85 ? 341 GLU A CA    1 
ATOM   2817  C  C     . GLU A 1 341 ? -23.368 18.322  10.924  1 59.44 ? 341 GLU A C     1 
ATOM   2818  O  O     . GLU A 1 341 ? -23.153 17.241  11.462  1 59.62 ? 341 GLU A O     1 
ATOM   2819  C  CB    . GLU A 1 341 ? -23.712 18.457  8.441   1 62.59 ? 341 GLU A CB    1 
ATOM   2820  C  CG    . GLU A 1 341 ? -24.664 18.252  7.275   1 68.17 ? 341 GLU A CG    1 
ATOM   2821  C  CD    . GLU A 1 341 ? -25.404 16.929  7.295   1 75.05 ? 341 GLU A CD    1 
ATOM   2822  O  OE1   . GLU A 1 341 ? -24.808 15.91   6.873   1 76.45 ? 341 GLU A OE1   1 
ATOM   2823  O  OE2   . GLU A 1 341 ? -26.579 16.907  7.728   1 77.2  ? 341 GLU A OE2   1 
ATOM   2824  N  N     . LEU A 1 342 ? -22.754 19.449  11.29   1 58.84 ? 342 LEU A N     1 
ATOM   2825  C  CA    . LEU A 1 342 ? -21.758 19.515  12.355  1 58.86 ? 342 LEU A CA    1 
ATOM   2826  C  C     . LEU A 1 342 ? -22.365 19.212  13.727  1 58.58 ? 342 LEU A C     1 
ATOM   2827  O  O     . LEU A 1 342 ? -21.681 18.668  14.589  1 58.75 ? 342 LEU A O     1 
ATOM   2828  C  CB    . LEU A 1 342 ? -21.131 20.913  12.394  1 59.2  ? 342 LEU A CB    1 
ATOM   2829  C  CG    . LEU A 1 342 ? -20.2   21.274  11.251  1 60.86 ? 342 LEU A CG    1 
ATOM   2830  C  CD1   . LEU A 1 342 ? -19.798 22.722  11.334  1 61.46 ? 342 LEU A CD1   1 
ATOM   2831  C  CD2   . LEU A 1 342 ? -18.971 20.401  11.261  1 61.58 ? 342 LEU A CD2   1 
ATOM   2832  N  N     . LYS A 1 343 ? -23.638 19.57   13.94   1 57.91 ? 343 LYS A N     1 
ATOM   2833  C  CA    . LYS A 1 343 ? -24.297 19.379  15.229  1 57.67 ? 343 LYS A CA    1 
ATOM   2834  C  C     . LYS A 1 343 ? -25.032 18.039  15.405  1 57.21 ? 343 LYS A C     1 
ATOM   2835  O  O     . LYS A 1 343 ? -26.031 17.983  16.123  1 57.39 ? 343 LYS A O     1 
ATOM   2836  C  CB    . LYS A 1 343 ? -25.247 20.547  15.52   1 59.28 ? 343 LYS A CB    1 
ATOM   2837  C  CG    . LYS A 1 343 ? -24.533 21.861  15.775  1 63.1  ? 343 LYS A CG    1 
ATOM   2838  C  CD    . LYS A 1 343 ? -25.527 22.935  16.149  1 67.35 ? 343 LYS A CD    1 
ATOM   2839  C  CE    . LYS A 1 343 ? -24.887 24.281  16.345  1 70.98 ? 343 LYS A CE    1 
ATOM   2840  N  NZ    . LYS A 1 343 ? -25.778 25.185  17.107  1 73.29 ? 343 LYS A NZ    1 
ATOM   2841  N  N     . GLU A 1 344 ? -24.531 16.963  14.792  1 56.44 ? 344 GLU A N     1 
ATOM   2842  C  CA    . GLU A 1 344 ? -25.131 15.639  14.955  1 56.15 ? 344 GLU A CA    1 
ATOM   2843  C  C     . GLU A 1 344 ? -24.989 15.182  16.415  1 55.13 ? 344 GLU A C     1 
ATOM   2844  O  O     . GLU A 1 344 ? -23.951 15.424  17.023  1 55.26 ? 344 GLU A O     1 
ATOM   2845  C  CB    . GLU A 1 344 ? -24.477 14.63   13.996  1 58.83 ? 344 GLU A CB    1 
ATOM   2846  C  CG    . GLU A 1 344 ? -25.141 13.267  14.012  1 64.46 ? 344 GLU A CG    1 
ATOM   2847  C  CD    . GLU A 1 344 ? -24.818 12.409  12.81   1 72.51 ? 344 GLU A CD    1 
ATOM   2848  O  OE1   . GLU A 1 344 ? -24.632 12.979  11.709  1 73.45 ? 344 GLU A OE1   1 
ATOM   2849  O  OE2   . GLU A 1 344 ? -24.755 11.166  12.964  1 75.86 ? 344 GLU A OE2   1 
ATOM   2850  N  N     . ASP A 1 345 ? -26.036 14.574  16.999  1 53.94 ? 345 ASP A N     1 
ATOM   2851  C  CA    . ASP A 1 345 ? -25.996 14.152  18.402  1 53.18 ? 345 ASP A CA    1 
ATOM   2852  C  C     . ASP A 1 345 ? -25.184 12.885  18.656  1 51.68 ? 345 ASP A C     1 
ATOM   2853  O  O     . ASP A 1 345 ? -25.749 11.813  18.879  1 51.78 ? 345 ASP A O     1 
ATOM   2854  C  CB    . ASP A 1 345 ? -27.413 14.005  18.986  1 55.22 ? 345 ASP A CB    1 
ATOM   2855  C  CG    . ASP A 1 345 ? -27.433 13.92   20.503  1 59.87 ? 345 ASP A CG    1 
ATOM   2856  O  OD1   . ASP A 1 345 ? -26.689 14.69   21.149  1 60.78 ? 345 ASP A OD1   1 
ATOM   2857  O  OD2   . ASP A 1 345 ? -28.192 13.081  21.043  1 61.79 ? 345 ASP A OD2   1 
ATOM   2858  N  N     . ALA A 1 346 ? -23.861 13.018  18.662  1 50.16 ? 346 ALA A N     1 
ATOM   2859  C  CA    . ALA A 1 346 ? -22.944 11.915  18.928  1 49.26 ? 346 ALA A CA    1 
ATOM   2860  C  C     . ALA A 1 346 ? -21.598 12.469  19.398  1 48.04 ? 346 ALA A C     1 
ATOM   2861  O  O     . ALA A 1 346 ? -21.288 13.634  19.146  1 48.02 ? 346 ALA A O     1 
ATOM   2862  C  CB    . ALA A 1 346 ? -22.75  11.076  17.672  1 49.4  ? 346 ALA A CB    1 
ATOM   2863  N  N     . ASP A 1 347 ? -20.794 11.649  20.091  1 46.88 ? 347 ASP A N     1 
ATOM   2864  C  CA    . ASP A 1 347 ? -19.465 12.079  20.531  1 46.17 ? 347 ASP A CA    1 
ATOM   2865  C  C     . ASP A 1 347 ? -18.59  12.325  19.297  1 45.02 ? 347 ASP A C     1 
ATOM   2866  O  O     . ASP A 1 347 ? -18.712 11.615  18.296  1 44.88 ? 347 ASP A O     1 
ATOM   2867  C  CB    . ASP A 1 347 ? -18.809 11.023  21.441  1 47.84 ? 347 ASP A CB    1 
ATOM   2868  C  CG    . ASP A 1 347 ? -19.472 10.841  22.786  1 51.95 ? 347 ASP A CG    1 
ATOM   2869  O  OD1   . ASP A 1 347 ? -20.227 11.741  23.198  1 52.67 ? 347 ASP A OD1   1 
ATOM   2870  O  OD2   . ASP A 1 347 ? -19.232 9.796   23.429  1 54.19 ? 347 ASP A OD2   1 
ATOM   2871  N  N     . LEU A 1 348 ? -17.739 13.341  19.361  1 44.15 ? 348 LEU A N     1 
ATOM   2872  C  CA    . LEU A 1 348 ? -16.897 13.705  18.232  1 43.68 ? 348 LEU A CA    1 
ATOM   2873  C  C     . LEU A 1 348 ? -15.435 13.619  18.617  1 42.91 ? 348 LEU A C     1 
ATOM   2874  O  O     . LEU A 1 348 ? -15.042 14.228  19.604  1 43.34 ? 348 LEU A O     1 
ATOM   2875  C  CB    . LEU A 1 348 ? -17.222 15.144  17.836  1 43.86 ? 348 LEU A CB    1 
ATOM   2876  C  CG    . LEU A 1 348 ? -16.469 15.671  16.648  1 45.29 ? 348 LEU A CG    1 
ATOM   2877  C  CD1   . LEU A 1 348 ? -16.936 14.979  15.395  1 45.9  ? 348 LEU A CD1   1 
ATOM   2878  C  CD2   . LEU A 1 348 ? -16.644 17.179  16.532  1 45.88 ? 348 LEU A CD2   1 
ATOM   2879  N  N     . ILE A 1 349 ? -14.627 12.883  17.852  1 41.66 ? 349 ILE A N     1 
ATOM   2880  C  CA    . ILE A 1 349 ? -13.199 12.811  18.129  1 41.04 ? 349 ILE A CA    1 
ATOM   2881  C  C     . ILE A 1 349 ? -12.53  13.896  17.307  1 40.3  ? 349 ILE A C     1 
ATOM   2882  O  O     . ILE A 1 349 ? -12.736 13.945  16.101  1 40.75 ? 349 ILE A O     1 
ATOM   2883  C  CB    . ILE A 1 349 ? -12.625 11.408  17.844  1 41.6  ? 349 ILE A CB    1 
ATOM   2884  C  CG1   . ILE A 1 349 ? -13.209 10.393  18.845  1 42.83 ? 349 ILE A CG1   1 
ATOM   2885  C  CG2   . ILE A 1 349 ? -11.098 11.43   17.899  1 41.91 ? 349 ILE A CG2   1 
ATOM   2886  C  CD1   . ILE A 1 349 ? -12.786 8.963   18.646  1 44.14 ? 349 ILE A CD1   1 
ATOM   2887  N  N     . VAL A 1 350 ? -11.791 14.808  17.946  1 39.03 ? 350 VAL A N     1 
ATOM   2888  C  CA    . VAL A 1 350 ? -11.108 15.878  17.221  1 38.32 ? 350 VAL A CA    1 
ATOM   2889  C  C     . VAL A 1 350 ? -9.639  15.527  17.116  1 37.39 ? 350 VAL A C     1 
ATOM   2890  O  O     . VAL A 1 350 ? -9.015  15.263  18.136  1 37.65 ? 350 VAL A O     1 
ATOM   2891  C  CB    . VAL A 1 350 ? -11.299 17.249  17.903  1 38.86 ? 350 VAL A CB    1 
ATOM   2892  C  CG1   . VAL A 1 350 ? -10.438 18.317  17.234  1 39.41 ? 350 VAL A CG1   1 
ATOM   2893  C  CG2   . VAL A 1 350 ? -12.766 17.655  17.903  1 39.19 ? 350 VAL A CG2   1 
ATOM   2894  N  N     . CYS A 1 351 ? -9.092  15.494  15.897  1 36.07 ? 351 CYS A N     1 
ATOM   2895  C  CA    . CYS A 1 351 ? -7.683  15.187  15.685  1 35.34 ? 351 CYS A CA    1 
ATOM   2896  C  C     . CYS A 1 351 ? -7.032  16.42   15.091  1 34.12 ? 351 CYS A C     1 
ATOM   2897  O  O     . CYS A 1 351 ? -7.526  16.933  14.1    1 34.07 ? 351 CYS A O     1 
ATOM   2898  C  CB    . CYS A 1 351 ? -7.53   13.981  14.762  1 36.1  ? 351 CYS A CB    1 
ATOM   2899  S  SG    . CYS A 1 351 ? -5.852  13.303  14.7    1 39.6  ? 351 CYS A SG    1 
ATOM   2900  N  N     . MET A 1 352 ? -5.957  16.922  15.699  1 32.98 ? 352 MET A N     1 
ATOM   2901  C  CA    . MET A 1 352 ? -5.276  18.107  15.192  1 32.36 ? 352 MET A CA    1 
ATOM   2902  C  C     . MET A 1 352 ? -3.896  17.699  14.729  1 31.86 ? 352 MET A C     1 
ATOM   2903  O  O     . MET A 1 352 ? -3.14   17.13   15.516  1 32.04 ? 352 MET A O     1 
ATOM   2904  C  CB    . MET A 1 352 ? -5.197  19.189  16.28   1 32.68 ? 352 MET A CB    1 
ATOM   2905  C  CG    . MET A 1 352 ? -6.564  19.717  16.693  1 34.33 ? 352 MET A CG    1 
ATOM   2906  S  SD    . MET A 1 352 ? -6.591  21.026  17.957  1 36.69 ? 352 MET A SD    1 
ATOM   2907  C  CE    . MET A 1 352 ? -5.461  22.191  17.277  1 34.78 ? 352 MET A CE    1 
ATOM   2908  N  N     . LEU A 1 353 ? -3.583  17.921  13.44   1 30.99 ? 353 LEU A N     1 
ATOM   2909  C  CA    . LEU A 1 353 ? -2.293  17.531  12.868  1 30.65 ? 353 LEU A CA    1 
ATOM   2910  C  C     . LEU A 1 353 ? -1.748  18.612  11.964  1 30.54 ? 353 LEU A C     1 
ATOM   2911  O  O     . LEU A 1 353 ? -2.519  19.229  11.236  1 30.68 ? 353 LEU A O     1 
ATOM   2912  C  CB    . LEU A 1 353 ? -2.459  16.269  12.017  1 30.57 ? 353 LEU A CB    1 
ATOM   2913  C  CG    . LEU A 1 353 ? -2.905  15.009  12.72   1 31.53 ? 353 LEU A CG    1 
ATOM   2914  C  CD1   . LEU A 1 353 ? -3.382  13.997  11.715  1 31.94 ? 353 LEU A CD1   1 
ATOM   2915  C  CD2   . LEU A 1 353 ? -1.796  14.449  13.582  1 32.02 ? 353 LEU A CD2   1 
ATOM   2916  N  N     . LYS A 1 354 ? -0.422  18.823  11.965  1 30.2  ? 354 LYS A N     1 
ATOM   2917  C  CA    . LYS A 1 354 ? 0.176   19.799  11.054  1 30.49 ? 354 LYS A CA    1 
ATOM   2918  C  C     . LYS A 1 354 ? 0.045   19.298  9.624   1 31.15 ? 354 LYS A C     1 
ATOM   2919  O  O     . LYS A 1 354 ? -0.316  20.051  8.734   1 31.25 ? 354 LYS A O     1 
ATOM   2920  C  CB    . LYS A 1 354 ? 1.642   20.078  11.399  1 31.8  ? 354 LYS A CB    1 
ATOM   2921  C  CG    . LYS A 1 354 ? 2.23    21.214  10.57   1 34.85 ? 354 LYS A CG    1 
ATOM   2922  C  CD    . LYS A 1 354 ? 3.574   21.662  11.105  1 38.32 ? 354 LYS A CD    1 
ATOM   2923  C  CE    . LYS A 1 354 ? 4.075   22.899  10.411  1 41.43 ? 354 LYS A CE    1 
ATOM   2924  N  NZ    . LYS A 1 354 ? 4.955   22.579  9.264   1 43.53 ? 354 LYS A NZ    1 
ATOM   2925  N  N     . GLY A 1 355 ? 0.306   18.017  9.421   1 31.46 ? 355 GLY A N     1 
ATOM   2926  C  CA    . GLY A 1 355 ? 0.171   17.375  8.128   1 31.97 ? 355 GLY A CA    1 
ATOM   2927  C  C     . GLY A 1 355 ? 1.305   17.604  7.16    1 32.49 ? 355 GLY A C     1 
ATOM   2928  O  O     . GLY A 1 355 ? 1.708   16.678  6.46    1 32.68 ? 355 GLY A O     1 
ATOM   2929  N  N     . PHE A 1 356 ? 1.788   18.85   7.05    1 32.49 ? 356 PHE A N     1 
ATOM   2930  C  CA    . PHE A 1 356 ? 2.781   19.19   6.033   1 32.8  ? 356 PHE A CA    1 
ATOM   2931  C  C     . PHE A 1 356 ? 3.974   19.981  6.553   1 33.61 ? 356 PHE A C     1 
ATOM   2932  O  O     . PHE A 1 356 ? 3.829   20.85   7.407   1 33.88 ? 356 PHE A O     1 
ATOM   2933  C  CB    . PHE A 1 356 ? 2.089   19.946  4.879   1 32.22 ? 356 PHE A CB    1 
ATOM   2934  C  CG    . PHE A 1 356 ? 0.916   19.187  4.304   1 32.23 ? 356 PHE A CG    1 
ATOM   2935  C  CD1   . PHE A 1 356 ? 1.095   18.292  3.275   1 32.87 ? 356 PHE A CD1   1 
ATOM   2936  C  CD2   . PHE A 1 356 ? -0.342  19.276  4.877   1 32.59 ? 356 PHE A CD2   1 
ATOM   2937  C  CE1   . PHE A 1 356 ? 0.035   17.545  2.793   1 33.25 ? 356 PHE A CE1   1 
ATOM   2938  C  CE2   . PHE A 1 356 ? -1.39   18.501  4.412   1 33.05 ? 356 PHE A CE2   1 
ATOM   2939  C  CZ    . PHE A 1 356 ? -1.193  17.643  3.377   1 32.74 ? 356 PHE A CZ    1 
ATOM   2940  N  N     . LYS A 1 357 ? 5.157   19.67   6.023   1 33.8  ? 357 LYS A N     1 
ATOM   2941  C  CA    . LYS A 1 357 ? 6.416   20.333  6.35    1 34.51 ? 357 LYS A CA    1 
ATOM   2942  C  C     . LYS A 1 357 ? 6.501   21.728  5.658   1 35.3  ? 357 LYS A C     1 
ATOM   2943  O  O     . LYS A 1 357 ? 5.626   22.048  4.849   1 35.75 ? 357 LYS A O     1 
ATOM   2944  C  CB    . LYS A 1 357 ? 7.581   19.4    5.962   1 35.77 ? 357 LYS A CB    1 
ATOM   2945  C  CG    . LYS A 1 357 ? 7.913   18.39   7.051   1 38.75 ? 357 LYS A CG    1 
ATOM   2946  C  CD    . LYS A 1 357 ? 8.74    17.242  6.527   1 42.42 ? 357 LYS A CD    1 
ATOM   2947  C  CE    . LYS A 1 357 ? 7.861   16.226  5.843   1 45.9  ? 357 LYS A CE    1 
ATOM   2948  N  NZ    . LYS A 1 357 ? 8.648   15.138  5.193   1 47.55 ? 357 LYS A NZ    1 
ATOM   2949  N  N     . PRO A 1 358 ? 7.502   22.591  5.963   1 35.24 ? 358 PRO A N     1 
ATOM   2950  C  CA    . PRO A 1 358 ? 7.537   23.927  5.337   1 35.06 ? 358 PRO A CA    1 
ATOM   2951  C  C     . PRO A 1 358 ? 7.413   23.959  3.817   1 35.3  ? 358 PRO A C     1 
ATOM   2952  O  O     . PRO A 1 358 ? 6.791   24.873  3.294   1 35.61 ? 358 PRO A O     1 
ATOM   2953  C  CB    . PRO A 1 358 ? 8.871   24.503  5.807   1 35.77 ? 358 PRO A CB    1 
ATOM   2954  C  CG    . PRO A 1 358 ? 9.137   23.824  7.095   1 36.4  ? 358 PRO A CG    1 
ATOM   2955  C  CD    . PRO A 1 358 ? 8.604   22.426  6.932   1 34.86 ? 358 PRO A CD    1 
ATOM   2956  N  N     . ARG A 1 359 ? 7.974   22.973  3.105   1 35.2  ? 359 ARG A N     1 
ATOM   2957  C  CA    . ARG A 1 359 ? 7.886   22.94   1.635   1 35.41 ? 359 ARG A CA    1 
ATOM   2958  C  C     . ARG A 1 359 ? 6.59    22.317  1.084   1 35.15 ? 359 ARG A C     1 
ATOM   2959  O  O     . ARG A 1 359 ? 6.445   22.188  -0.131  1 35.23 ? 359 ARG A O     1 
ATOM   2960  C  CB    . ARG A 1 359 ? 9.112   22.235  1.027   1 36.76 ? 359 ARG A CB    1 
ATOM   2961  C  CG    . ARG A 1 359 ? 10.431  22.86   1.444   1 39.87 ? 359 ARG A CG    1 
ATOM   2962  C  CD    . ARG A 1 359 ? 11.436  21.803  1.841   1 43.16 ? 359 ARG A CD    1 
ATOM   2963  N  NE    . ARG A 1 359 ? 12.101  21.24   0.67    1 46.17 ? 359 ARG A NE    1 
ATOM   2964  C  CZ    . ARG A 1 359 ? 13.209  20.506  0.711   1 48.73 ? 359 ARG A CZ    1 
ATOM   2965  N  NH1   . ARG A 1 359 ? 13.767  20.2    1.877   1 48.26 ? 359 ARG A NH1   1 
ATOM   2966  N  NH2   . ARG A 1 359 ? 13.743  20.041  -0.408  1 49.22 ? 359 ARG A NH2   1 
ATOM   2967  N  N     . GLY A 1 360 ? 5.669   21.94   1.963   1 34.65 ? 360 GLY A N     1 
ATOM   2968  C  CA    . GLY A 1 360 ? 4.414   21.327  1.558   1 34.78 ? 360 GLY A CA    1 
ATOM   2969  C  C     . GLY A 1 360 ? 4.46    19.811  1.461   1 34.79 ? 360 GLY A C     1 
ATOM   2970  O  O     . GLY A 1 360 ? 3.455   19.188  1.117   1 35.15 ? 360 GLY A O     1 
ATOM   2971  N  N     . ASP A 1 361 ? 5.626   19.195  1.737   1 34.05 ? 361 ASP A N     1 
ATOM   2972  C  CA    . ASP A 1 361 ? 5.766   17.742  1.698   1 33.65 ? 361 ASP A CA    1 
ATOM   2973  C  C     . ASP A 1 361 ? 5.103   17.142  2.933   1 33.87 ? 361 ASP A C     1 
ATOM   2974  O  O     . ASP A 1 361 ? 5.293   17.643  4.037   1 33.91 ? 361 ASP A O     1 
ATOM   2975  C  CB    . ASP A 1 361 ? 7.24    17.297  1.53    1 34.23 ? 361 ASP A CB    1 
ATOM   2976  C  CG    . ASP A 1 361 ? 8.284   17.971  2.414   1 36.72 ? 361 ASP A CG    1 
ATOM   2977  O  OD1   . ASP A 1 361 ? 8.252   19.215  2.538   1 37.01 ? 361 ASP A OD1   1 
ATOM   2978  O  OD2   . ASP A 1 361 ? 9.172   17.262  2.931   1 38.17 ? 361 ASP A OD2   1 
ATOM   2979  N  N     . ASP A 1 362 ? 4.274   16.116  2.744   1 33.84 ? 362 ASP A N     1 
ATOM   2980  C  CA    . ASP A 1 362 ? 3.512   15.519  3.839   1 34.15 ? 362 ASP A CA    1 
ATOM   2981  C  C     . ASP A 1 362 ? 4.343   14.839  4.922   1 33.82 ? 362 ASP A C     1 
ATOM   2982  O  O     . ASP A 1 362 ? 5.386   14.253  4.642   1 34.09 ? 362 ASP A O     1 
ATOM   2983  C  CB    . ASP A 1 362 ? 2.463   14.546  3.296   1 36.09 ? 362 ASP A CB    1 
ATOM   2984  C  CG    . ASP A 1 362 ? 3.049   13.406  2.498   1 40.65 ? 362 ASP A CG    1 
ATOM   2985  O  OD1   . ASP A 1 362 ? 3.427   13.635  1.32    1 41.02 ? 362 ASP A OD1   1 
ATOM   2986  O  OD2   . ASP A 1 362 ? 3.134   12.288  3.044   1 43.07 ? 362 ASP A OD2   1 
ATOM   2987  N  N     . ASN A 1 363 ? 3.863   14.927  6.163   1 33.06 ? 363 ASN A N     1 
ATOM   2988  C  CA    . ASN A 1 363 ? 4.502   14.337  7.324   1 33.25 ? 363 ASN A CA    1 
ATOM   2989  C  C     . ASN A 1 363 ? 4.188   12.869  7.314   1 33.08 ? 363 ASN A C     1 
ATOM   2990  O  O     . ASN A 1 363 ? 3.018   12.508  7.453   1 33.55 ? 363 ASN A O     1 
ATOM   2991  C  CB    . ASN A 1 363 ? 3.926   14.924  8.622   1 34.72 ? 363 ASN A CB    1 
ATOM   2992  C  CG    . ASN A 1 363 ? 4.112   16.408  8.803   1 38.26 ? 363 ASN A CG    1 
ATOM   2993  O  OD1   . ASN A 1 363 ? 4.853   17.063  8.071   1 40.19 ? 363 ASN A OD1   1 
ATOM   2994  N  ND2   . ASN A 1 363 ? 3.448   16.978  9.785   1 38.65 ? 363 ASN A ND2   1 
ATOM   2995  N  N     . ARG A 1 364 ? 5.213   12.014  7.183   1 32.11 ? 364 ARG A N     1 
ATOM   2996  C  CA    . ARG A 1 364 ? 5.008   10.565  7.211   1 31.42 ? 364 ARG A CA    1 
ATOM   2997  C  C     . ARG A 1 364 ? 4.319   10.062  8.488   1 30.73 ? 364 ARG A C     1 
ATOM   2998  O  O     . ARG A 1 364 ? 3.38    9.28    8.357   1 30.82 ? 364 ARG A O     1 
ATOM   2999  C  CB    . ARG A 1 364 ? 6.309   9.798   6.957   1 32.34 ? 364 ARG A CB    1 
ATOM   3000  C  CG    . ARG A 1 364 ? 6.077   8.487   6.234   1 34.68 ? 364 ARG A CG    1 
ATOM   3001  C  CD    . ARG A 1 364 ? 5.719   8.703   4.771   1 37.4  ? 364 ARG A CD    1 
ATOM   3002  N  NE    . ARG A 1 364 ? 6.788   9.389   4.041   1 39.74 ? 364 ARG A NE    1 
ATOM   3003  C  CZ    . ARG A 1 364 ? 6.721   10.647  3.616   1 41.59 ? 364 ARG A CZ    1 
ATOM   3004  N  NH1   . ARG A 1 364 ? 5.624   11.365  3.814   1 41.29 ? 364 ARG A NH1   1 
ATOM   3005  N  NH2   . ARG A 1 364 ? 7.748   11.194  2.981   1 41.47 ? 364 ARG A NH2   1 
ATOM   3006  N  N     . PRO A 1 365 ? 4.698   10.506  9.715   1 29.82 ? 365 PRO A N     1 
ATOM   3007  C  CA    . PRO A 1 365 ? 4.003   10.008  10.909  1 29.6  ? 365 PRO A CA    1 
ATOM   3008  C  C     . PRO A 1 365 ? 2.513   10.319  10.949  1 29.85 ? 365 PRO A C     1 
ATOM   3009  O  O     . PRO A 1 365 ? 1.744   9.517   11.466  1 30.17 ? 365 PRO A O     1 
ATOM   3010  C  CB    . PRO A 1 365 ? 4.726   10.71   12.057  1 30.01 ? 365 PRO A CB    1 
ATOM   3011  C  CG    . PRO A 1 365 ? 6.054   11.063  11.522  1 30.47 ? 365 PRO A CG    1 
ATOM   3012  C  CD    . PRO A 1 365 ? 5.793   11.42   10.095  1 29.08 ? 365 PRO A CD    1 
ATOM   3013  N  N     . ASP A 1 366 ? 2.098   11.468  10.403  1 29.74 ? 366 ASP A N     1 
ATOM   3014  C  CA    . ASP A 1 366 ? 0.686   11.861  10.403  1 30    ? 366 ASP A CA    1 
ATOM   3015  C  C     . ASP A 1 366 ? -0.225  10.911  9.653   1 29.86 ? 366 ASP A C     1 
ATOM   3016  O  O     . ASP A 1 366 ? -1.418  10.836  9.959   1 29.68 ? 366 ASP A O     1 
ATOM   3017  C  CB    . ASP A 1 366 ? 0.519   13.285  9.878   1 31.63 ? 366 ASP A CB    1 
ATOM   3018  C  CG    . ASP A 1 366 ? 1.148   14.344  10.757  1 36.69 ? 366 ASP A CG    1 
ATOM   3019  O  OD1   . ASP A 1 366 ? 1.866   13.982  11.728  1 37.53 ? 366 ASP A OD1   1 
ATOM   3020  O  OD2   . ASP A 1 366 ? 0.938   15.523  10.482  1 39.16 ? 366 ASP A OD2   1 
ATOM   3021  N  N     . ARG A 1 367 ? 0.327   10.167  8.686   1 29.63 ? 367 ARG A N     1 
ATOM   3022  C  CA    . ARG A 1 367 ? -0.451  9.19    7.939   1 29.81 ? 367 ARG A CA    1 
ATOM   3023  C  C     . ARG A 1 367 ? -1.032  8.091   8.856   1 29.66 ? 367 ARG A C     1 
ATOM   3024  O  O     . ARG A 1 367 ? -2.009  7.453   8.478   1 30.3  ? 367 ARG A O     1 
ATOM   3025  C  CB    . ARG A 1 367 ? 0.401   8.56    6.833   1 31.3  ? 367 ARG A CB    1 
ATOM   3026  C  CG    . ARG A 1 367 ? 0.984   9.55    5.834   1 34.16 ? 367 ARG A CG    1 
ATOM   3027  C  CD    . ARG A 1 367 ? 1.902   8.815   4.884   1 36.86 ? 367 ARG A CD    1 
ATOM   3028  N  NE    . ARG A 1 367 ? 2.27    9.61    3.715   1 39.17 ? 367 ARG A NE    1 
ATOM   3029  C  CZ    . ARG A 1 367 ? 2.415   9.111   2.492   1 42.04 ? 367 ARG A CZ    1 
ATOM   3030  N  NH1   . ARG A 1 367 ? 2.203   7.819   2.263   1 42.6  ? 367 ARG A NH1   1 
ATOM   3031  N  NH2   . ARG A 1 367 ? 2.751   9.901   1.484   1 42.18 ? 367 ARG A NH2   1 
ATOM   3032  N  N     . GLY A 1 368 ? -0.44   7.878   10.032  1 28.52 ? 368 GLY A N     1 
ATOM   3033  C  CA    . GLY A 1 368 ? -0.922  6.877   10.963  1 28.02 ? 368 GLY A CA    1 
ATOM   3034  C  C     . GLY A 1 368 ? -1.755  7.423   12.108  1 27.56 ? 368 GLY A C     1 
ATOM   3035  O  O     . GLY A 1 368 ? -2.237  6.635   12.923  1 28.13 ? 368 GLY A O     1 
ATOM   3036  N  N     . ALA A 1 369 ? -1.96   8.756   12.19   1 26.25 ? 369 ALA A N     1 
ATOM   3037  C  CA    . ALA A 1 369 ? -2.738  9.333   13.293  1 25.48 ? 369 ALA A CA    1 
ATOM   3038  C  C     . ALA A 1 369 ? -4.216  8.969   13.244  1 24.73 ? 369 ALA A C     1 
ATOM   3039  O  O     . ALA A 1 369 ? -4.738  8.49    14.249  1 24.71 ? 369 ALA A O     1 
ATOM   3040  C  CB    . ALA A 1 369 ? -2.545  10.834  13.376  1 25.47 ? 369 ALA A CB    1 
ATOM   3041  N  N     . LEU A 1 370 ? -4.884  9.146   12.09   1 24.09 ? 370 LEU A N     1 
ATOM   3042  C  CA    . LEU A 1 370 ? -6.28   8.725   11.964  1 24.25 ? 370 LEU A CA    1 
ATOM   3043  C  C     . LEU A 1 370 ? -6.425  7.199   12.098  1 24.66 ? 370 LEU A C     1 
ATOM   3044  O  O     . LEU A 1 370 ? -7.219  6.755   12.93   1 24.8  ? 370 LEU A O     1 
ATOM   3045  C  CB    . LEU A 1 370 ? -6.959  9.276   10.707  1 24.24 ? 370 LEU A CB    1 
ATOM   3046  C  CG    . LEU A 1 370 ? -7.079  10.781  10.642  1 25.66 ? 370 LEU A CG    1 
ATOM   3047  C  CD1   . LEU A 1 370 ? -7.866  11.176  9.452   1 26.16 ? 370 LEU A CD1   1 
ATOM   3048  C  CD2   . LEU A 1 370 ? -7.746  11.354  11.902  1 26.43 ? 370 LEU A CD2   1 
ATOM   3049  N  N     . PRO A 1 371 ? -5.586  6.374   11.424  1 24.53 ? 371 PRO A N     1 
ATOM   3050  C  CA    . PRO A 1 371 ? -5.64   4.925   11.653  1 24.62 ? 371 PRO A CA    1 
ATOM   3051  C  C     . PRO A 1 371 ? -5.498  4.534   13.127  1 24.87 ? 371 PRO A C     1 
ATOM   3052  O  O     . PRO A 1 371 ? -6.154  3.596   13.543  1 25.08 ? 371 PRO A O     1 
ATOM   3053  C  CB    . PRO A 1 371 ? -4.458  4.411   10.831  1 25.36 ? 371 PRO A CB    1 
ATOM   3054  C  CG    . PRO A 1 371 ? -4.341  5.388   9.72    1 25.71 ? 371 PRO A CG    1 
ATOM   3055  C  CD    . PRO A 1 371 ? -4.58   6.702   10.396  1 24.06 ? 371 PRO A CD    1 
ATOM   3056  N  N     . LEU A 1 372 ? -4.695  5.269   13.922  1 24.75 ? 372 LEU A N     1 
ATOM   3057  C  CA    . LEU A 1 372 ? -4.536  5.012   15.357  1 25.08 ? 372 LEU A CA    1 
ATOM   3058  C  C     . LEU A 1 372 ? -5.868  5.256   16.08   1 25.32 ? 372 LEU A C     1 
ATOM   3059  O  O     . LEU A 1 372 ? -6.304  4.415   16.868  1 25.25 ? 372 LEU A O     1 
ATOM   3060  C  CB    . LEU A 1 372 ? -3.422  5.901   15.941  1 25.28 ? 372 LEU A CB    1 
ATOM   3061  C  CG    . LEU A 1 372 ? -3.265  5.908   17.455  1 26.83 ? 372 LEU A CG    1 
ATOM   3062  C  CD1   . LEU A 1 372 ? -2.81   4.574   17.958  1 27.71 ? 372 LEU A CD1   1 
ATOM   3063  C  CD2   . LEU A 1 372 ? -2.265  6.933   17.874  1 27.38 ? 372 LEU A CD2   1 
ATOM   3064  N  N     . VAL A 1 373 ? -6.536  6.374   15.766  1 25.36 ? 373 VAL A N     1 
ATOM   3065  C  CA    . VAL A 1 373 ? -7.842  6.724   16.325  1 25.79 ? 373 VAL A CA    1 
ATOM   3066  C  C     . VAL A 1 373 ? -8.869  5.64    15.976  1 26.42 ? 373 VAL A C     1 
ATOM   3067  O  O     . VAL A 1 373 ? -9.601  5.176   16.852  1 26.44 ? 373 VAL A O     1 
ATOM   3068  C  CB    . VAL A 1 373 ? -8.282  8.104   15.79   1 26.32 ? 373 VAL A CB    1 
ATOM   3069  C  CG1   . VAL A 1 373 ? -9.737  8.397   16.127  1 26.83 ? 373 VAL A CG1   1 
ATOM   3070  C  CG2   . VAL A 1 373 ? -7.376  9.197   16.32   1 26.75 ? 373 VAL A CG2   1 
ATOM   3071  N  N     . ALA A 1 374 ? -8.891  5.214   14.696  1 26.63 ? 374 ALA A N     1 
ATOM   3072  C  CA    . ALA A 1 374 ? -9.797  4.184   14.189  1 27.16 ? 374 ALA A CA    1 
ATOM   3073  C  C     . ALA A 1 374 ? -9.532  2.82    14.84   1 27.65 ? 374 ALA A C     1 
ATOM   3074  O  O     . ALA A 1 374 ? -10.461 2.052   15.074  1 27.66 ? 374 ALA A O     1 
ATOM   3075  C  CB    . ALA A 1 374 ? -9.671  4.084   12.679  1 27.19 ? 374 ALA A CB    1 
ATOM   3076  N  N     . MET A 1 375 ? -8.271  2.522   15.134  1 27.89 ? 375 MET A N     1 
ATOM   3077  C  CA    . MET A 1 375 ? -7.91   1.274   15.783  1 28.69 ? 375 MET A CA    1 
ATOM   3078  C  C     . MET A 1 375 ? -8.336  1.271   17.265  1 29.44 ? 375 MET A C     1 
ATOM   3079  O  O     . MET A 1 375 ? -8.672  0.215   17.799  1 29.69 ? 375 MET A O     1 
ATOM   3080  C  CB    . MET A 1 375 ? -6.409  1.012   15.63   1 29.36 ? 375 MET A CB    1 
ATOM   3081  C  CG    . MET A 1 375 ? -6.02   0.619   14.224  1 31.83 ? 375 MET A CG    1 
ATOM   3082  S  SD    . MET A 1 375 ? -4.234  0.494   14.028  1 36.95 ? 375 MET A SD    1 
ATOM   3083  C  CE    . MET A 1 375 ? -3.905  -0.908  15.079  1 36.91 ? 375 MET A CE    1 
ATOM   3084  N  N     . LEU A 1 376 ? -8.347  2.444   17.922  1 29.4  ? 376 LEU A N     1 
ATOM   3085  C  CA    . LEU A 1 376 ? -8.735  2.55    19.326  1 29.71 ? 376 LEU A CA    1 
ATOM   3086  C  C     . LEU A 1 376 ? -10.252 2.588   19.522  1 30.41 ? 376 LEU A C     1 
ATOM   3087  O  O     . LEU A 1 376 ? -10.781 1.875   20.375  1 30.4  ? 376 LEU A O     1 
ATOM   3088  C  CB    . LEU A 1 376 ? -8.113  3.809   19.954  1 29.65 ? 376 LEU A CB    1 
ATOM   3089  C  CG    . LEU A 1 376 ? -6.627  3.762   20.216  1 30.79 ? 376 LEU A CG    1 
ATOM   3090  C  CD1   . LEU A 1 376 ? -6.099  5.131   20.566  1 31.3  ? 376 LEU A CD1   1 
ATOM   3091  C  CD2   . LEU A 1 376 ? -6.32   2.813   21.324  1 31.35 ? 376 LEU A CD2   1 
ATOM   3092  N  N     . ALA A 1 377 ? -10.951 3.438   18.757  1 30.87 ? 377 ALA A N     1 
ATOM   3093  C  CA    . ALA A 1 377 ? -12.387 3.626   18.941  1 31.66 ? 377 ALA A CA    1 
ATOM   3094  C  C     . ALA A 1 377 ? -13.284 3.113   17.82   1 32.1  ? 377 ALA A C     1 
ATOM   3095  O  O     . ALA A 1 377 ? -14.481 3.395   17.828  1 32.11 ? 377 ALA A O     1 
ATOM   3096  C  CB    . ALA A 1 377 ? -12.678 5.096   19.189  1 31.89 ? 377 ALA A CB    1 
ATOM   3097  N  N     . GLY A 1 378 ? -12.724 2.378   16.872  1 32.35 ? 378 GLY A N     1 
ATOM   3098  C  CA    . GLY A 1 378 ? -13.5   1.853   15.758  1 33.19 ? 378 GLY A CA    1 
ATOM   3099  C  C     . GLY A 1 378 ? -13.582 2.859   14.633  1 33.96 ? 378 GLY A C     1 
ATOM   3100  O  O     . GLY A 1 378 ? -13.719 4.058   14.881  1 34.27 ? 378 GLY A O     1 
ATOM   3101  N  N     . GLU A 1 379 ? -13.472 2.39    13.384  1 34.17 ? 379 GLU A N     1 
ATOM   3102  C  CA    . GLU A 1 379 ? -13.515 3.271   12.216  1 34.81 ? 379 GLU A CA    1 
ATOM   3103  C  C     . GLU A 1 379 ? -14.84  4.028   12.068  1 35.07 ? 379 GLU A C     1 
ATOM   3104  O  O     . GLU A 1 379 ? -14.868 5.101   11.47   1 35.17 ? 379 GLU A O     1 
ATOM   3105  C  CB    . GLU A 1 379 ? -13.2   2.484   10.942  1 37.18 ? 379 GLU A CB    1 
ATOM   3106  C  CG    . GLU A 1 379 ? -14.184 1.366   10.663  1 41.9  ? 379 GLU A CG    1 
ATOM   3107  C  CD    . GLU A 1 379 ? -13.854 0.586   9.41    1 48.1  ? 379 GLU A CD    1 
ATOM   3108  O  OE1   . GLU A 1 379 ? -12.657 0.29    9.193   1 48.95 ? 379 GLU A OE1   1 
ATOM   3109  O  OE2   . GLU A 1 379 ? -14.791 0.275   8.64    1 50.51 ? 379 GLU A OE2   1 
ATOM   3110  N  N     . ASN A 1 380 ? -15.922 3.483   12.642  1 34.92 ? 380 ASN A N     1 
ATOM   3111  C  CA    . ASN A 1 380 ? -17.266 4.051   12.632  1 35.18 ? 380 ASN A CA    1 
ATOM   3112  C  C     . ASN A 1 380 ? -17.409 5.328   13.476  1 35.03 ? 380 ASN A C     1 
ATOM   3113  O  O     . ASN A 1 380 ? -18.414 6.023   13.338  1 35.11 ? 380 ASN A O     1 
ATOM   3114  C  CB    . ASN A 1 380 ? -18.293 2.988   13.069  1 36.54 ? 380 ASN A CB    1 
ATOM   3115  C  CG    . ASN A 1 380 ? -17.858 2.119   14.244  1 39.86 ? 380 ASN A CG    1 
ATOM   3116  O  OD1   . ASN A 1 380 ? -17.423 2.618   15.292  1 41.01 ? 380 ASN A OD1   1 
ATOM   3117  N  ND2   . ASN A 1 380 ? -17.965 0.795   14.096  1 40.33 ? 380 ASN A ND2   1 
ATOM   3118  N  N     . ALA A 1 381 ? -16.429 5.634   14.349  1 34.71 ? 381 ALA A N     1 
ATOM   3119  C  CA    . ALA A 1 381 ? -16.489 6.824   15.202  1 34.89 ? 381 ALA A CA    1 
ATOM   3120  C  C     . ALA A 1 381 ? -16.439 8.091   14.37   1 34.76 ? 381 ALA A C     1 
ATOM   3121  O  O     . ALA A 1 381 ? -15.805 8.098   13.316  1 34.93 ? 381 ALA A O     1 
ATOM   3122  C  CB    . ALA A 1 381 ? -15.344 6.814   16.203  1 35.1  ? 381 ALA A CB    1 
ATOM   3123  N  N     . GLN A 1 382 ? -17.113 9.159   14.821  1 34.33 ? 382 GLN A N     1 
ATOM   3124  C  CA    . GLN A 1 382 ? -17.111 10.42   14.08   1 34.4  ? 382 GLN A CA    1 
ATOM   3125  C  C     . GLN A 1 382 ? -15.826 11.183  14.331  1 34.21 ? 382 GLN A C     1 
ATOM   3126  O  O     . GLN A 1 382 ? -15.531 11.516  15.472  1 34.36 ? 382 GLN A O     1 
ATOM   3127  C  CB    . GLN A 1 382 ? -18.335 11.269  14.417  1 35.98 ? 382 GLN A CB    1 
ATOM   3128  C  CG    . GLN A 1 382 ? -19.623 10.612  13.975  1 40.13 ? 382 GLN A CG    1 
ATOM   3129  C  CD    . GLN A 1 382 ? -20.786 11.553  14.042  1 46.18 ? 382 GLN A CD    1 
ATOM   3130  O  OE1   . GLN A 1 382 ? -20.655 12.768  13.84   1 47.96 ? 382 GLN A OE1   1 
ATOM   3131  N  NE2   . GLN A 1 382 ? -21.957 11.004  14.327  1 47.65 ? 382 GLN A NE2   1 
ATOM   3132  N  N     . ILE A 1 383 ? -15.039 11.428  13.276  1 33.77 ? 383 ILE A N     1 
ATOM   3133  C  CA    . ILE A 1 383 ? -13.753 12.106  13.402  1 33.96 ? 383 ILE A CA    1 
ATOM   3134  C  C     . ILE A 1 383 ? -13.722 13.47   12.693  1 34.18 ? 383 ILE A C     1 
ATOM   3135  O  O     . ILE A 1 383 ? -14.083 13.578  11.525  1 34.55 ? 383 ILE A O     1 
ATOM   3136  C  CB    . ILE A 1 383 ? -12.619 11.167  12.925  1 34.41 ? 383 ILE A CB    1 
ATOM   3137  C  CG1   . ILE A 1 383 ? -12.637 9.842   13.704  1 35.37 ? 383 ILE A CG1   1 
ATOM   3138  C  CG2   . ILE A 1 383 ? -11.255 11.834  13.027  1 34.83 ? 383 ILE A CG2   1 
ATOM   3139  C  CD1   . ILE A 1 383 ? -11.799 8.747   13.08   1 36.64 ? 383 ILE A CD1   1 
ATOM   3140  N  N     . PHE A 1 384 ? -13.301 14.512  13.421  1 33.67 ? 384 PHE A N     1 
ATOM   3141  C  CA    . PHE A 1 384 ? -13.169 15.89   12.957  1 33.48 ? 384 PHE A CA    1 
ATOM   3142  C  C     . PHE A 1 384 ? -11.671 16.117  12.862  1 33.01 ? 384 PHE A C     1 
ATOM   3143  O  O     . PHE A 1 384 ? -11.011 16.176  13.896  1 33.24 ? 384 PHE A O     1 
ATOM   3144  C  CB    . PHE A 1 384 ? -13.749 16.814  14.038  1 33.32 ? 384 PHE A CB    1 
ATOM   3145  C  CG    . PHE A 1 384 ? -13.836 18.292  13.736  1 33.86 ? 384 PHE A CG    1 
ATOM   3146  C  CD1   . PHE A 1 384 ? -12.713 19.099  13.801  1 34.62 ? 384 PHE A CD1   1 
ATOM   3147  C  CD2   . PHE A 1 384 ? -15.057 18.892  13.495  1 34.57 ? 384 PHE A CD2   1 
ATOM   3148  C  CE1   . PHE A 1 384 ? -12.807 20.464  13.57   1 35.35 ? 384 PHE A CE1   1 
ATOM   3149  C  CE2   . PHE A 1 384 ? -15.144 20.252  13.254  1 35.29 ? 384 PHE A CE2   1 
ATOM   3150  C  CZ    . PHE A 1 384 ? -14.025 21.03   13.315  1 35.17 ? 384 PHE A CZ    1 
ATOM   3151  N  N     . THR A 1 385 ? -11.126 16.201  11.648  1 32.12 ? 385 THR A N     1 
ATOM   3152  C  CA    . THR A 1 385 ? -9.689  16.356  11.447  1 32    ? 385 THR A CA    1 
ATOM   3153  C  C     . THR A 1 385 ? -9.302  17.794  11.12   1 31.44 ? 385 THR A C     1 
ATOM   3154  O  O     . THR A 1 385 ? -9.702  18.302  10.08   1 31.6  ? 385 THR A O     1 
ATOM   3155  C  CB    . THR A 1 385 ? -9.249  15.416  10.324  1 33.4  ? 385 THR A CB    1 
ATOM   3156  O  OG1   . THR A 1 385 ? -9.596  14.079  10.682  1 34.42 ? 385 THR A OG1   1 
ATOM   3157  C  CG2   . THR A 1 385 ? -7.764  15.503  10.028  1 33.83 ? 385 THR A CG2   1 
ATOM   3158  N  N     . PHE A 1 386 ? -8.504  18.44   11.984  1 30.49 ? 386 PHE A N     1 
ATOM   3159  C  CA    . PHE A 1 386 ? -8.057  19.816  11.78   1 30.05 ? 386 PHE A CA    1 
ATOM   3160  C  C     . PHE A 1 386 ? -6.586  19.846  11.346  1 30.22 ? 386 PHE A C     1 
ATOM   3161  O  O     . PHE A 1 386 ? -5.721  19.356  12.073  1 30.45 ? 386 PHE A O     1 
ATOM   3162  C  CB    . PHE A 1 386 ? -8.267  20.632  13.059  1 29.21 ? 386 PHE A CB    1 
ATOM   3163  C  CG    . PHE A 1 386 ? -7.841  22.074  12.963  1 28.98 ? 386 PHE A CG    1 
ATOM   3164  C  CD1   . PHE A 1 386 ? -8.724  23.045  12.535  1 29.42 ? 386 PHE A CD1   1 
ATOM   3165  C  CD2   . PHE A 1 386 ? -6.577  22.468  13.364  1 29.35 ? 386 PHE A CD2   1 
ATOM   3166  C  CE1   . PHE A 1 386 ? -8.337  24.372  12.467  1 29.93 ? 386 PHE A CE1   1 
ATOM   3167  C  CE2   . PHE A 1 386 ? -6.19   23.794  13.289  1 29.78 ? 386 PHE A CE2   1 
ATOM   3168  C  CZ    . PHE A 1 386 ? -7.074  24.739  12.848  1 29.62 ? 386 PHE A CZ    1 
ATOM   3169  N  N     . ILE A 1 387 ? -6.315  20.425  10.157  1 29.85 ? 387 ILE A N     1 
ATOM   3170  C  CA    . ILE A 1 387 ? -4.985  20.51   9.548   1 30.14 ? 387 ILE A CA    1 
ATOM   3171  C  C     . ILE A 1 387 ? -4.511  21.959  9.477   1 30.13 ? 387 ILE A C     1 
ATOM   3172  O  O     . ILE A 1 387 ? -5.294  22.834  9.115   1 30.29 ? 387 ILE A O     1 
ATOM   3173  C  CB    . ILE A 1 387 ? -5.02   19.84   8.146   1 30.99 ? 387 ILE A CB    1 
ATOM   3174  C  CG1   . ILE A 1 387 ? -5.567  18.405  8.217   1 32.2  ? 387 ILE A CG1   1 
ATOM   3175  C  CG2   . ILE A 1 387 ? -3.664  19.876  7.444   1 31.5  ? 387 ILE A CG2   1 
ATOM   3176  C  CD1   . ILE A 1 387 ? -4.82   17.495  9.206   1 33.7  ? 387 ILE A CD1   1 
ATOM   3177  N  N     . TYR A 1 388 ? -3.234  22.223  9.811   1 29.89 ? 388 TYR A N     1 
ATOM   3178  C  CA    . TYR A 1 388 ? -2.728  23.593  9.826   1 30.18 ? 388 TYR A CA    1 
ATOM   3179  C  C     . TYR A 1 388 ? -1.364  23.809  9.158   1 30.26 ? 388 TYR A C     1 
ATOM   3180  O  O     . TYR A 1 388 ? -0.803  24.892  9.276   1 30.12 ? 388 TYR A O     1 
ATOM   3181  C  CB    . TYR A 1 388 ? -2.694  24.121  11.273  1 30.34 ? 388 TYR A CB    1 
ATOM   3182  C  CG    . TYR A 1 388 ? -1.948  23.235  12.248  1 30.95 ? 388 TYR A CG    1 
ATOM   3183  C  CD1   . TYR A 1 388 ? -2.602  22.234  12.948  1 31.77 ? 388 TYR A CD1   1 
ATOM   3184  C  CD2   . TYR A 1 388 ? -0.597  23.421  12.493  1 31.72 ? 388 TYR A CD2   1 
ATOM   3185  C  CE1   . TYR A 1 388 ? -1.922  21.415  13.84   1 32.6  ? 388 TYR A CE1   1 
ATOM   3186  C  CE2   . TYR A 1 388 ? 0.093   22.61   13.382  1 32.51 ? 388 TYR A CE2   1 
ATOM   3187  C  CZ    . TYR A 1 388 ? -0.57   21.601  14.048  1 33.37 ? 388 TYR A CZ    1 
ATOM   3188  O  OH    . TYR A 1 388 ? 0.119   20.78   14.904  1 34.72 ? 388 TYR A OH    1 
ATOM   3189  N  N     . GLY A 1 389 ? -0.853  22.804  8.463   1 30.48 ? 389 GLY A N     1 
ATOM   3190  C  CA    . GLY A 1 389 ? 0.44    22.887  7.791   1 31.32 ? 389 GLY A CA    1 
ATOM   3191  C  C     . GLY A 1 389 ? 0.379   23.517  6.414   1 31.9  ? 389 GLY A C     1 
ATOM   3192  O  O     . GLY A 1 389 ? -0.702  23.647  5.843   1 32.17 ? 389 GLY A O     1 
ATOM   3193  N  N     . PRO A 1 390 ? 1.532   23.913  5.844   1 31.81 ? 390 PRO A N     1 
ATOM   3194  C  CA    . PRO A 1 390 ? 1.509   24.593  4.539   1 31.89 ? 390 PRO A CA    1 
ATOM   3195  C  C     . PRO A 1 390 ? 1.137   23.736  3.342   1 31.92 ? 390 PRO A C     1 
ATOM   3196  O  O     . PRO A 1 390 ? 1.669   22.645  3.162   1 32.49 ? 390 PRO A O     1 
ATOM   3197  C  CB    . PRO A 1 390 ? 2.928   25.159  4.391   1 32.64 ? 390 PRO A CB    1 
ATOM   3198  C  CG    . PRO A 1 390 ? 3.595   24.964  5.709   1 33.08 ? 390 PRO A CG    1 
ATOM   3199  C  CD    . PRO A 1 390 ? 2.894   23.847  6.398   1 31.38 ? 390 PRO A CD    1 
ATOM   3200  N  N     . LEU A 1 391 ? 0.248   24.254  2.496   1 31.3  ? 391 LEU A N     1 
ATOM   3201  C  CA    . LEU A 1 391 ? -0.19   23.536  1.313   1 31.32 ? 391 LEU A CA    1 
ATOM   3202  C  C     . LEU A 1 391 ? 0.401   24.116  0.053   1 31.38 ? 391 LEU A C     1 
ATOM   3203  O  O     . LEU A 1 391 ? 0.441   25.334  -0.109  1 31.46 ? 391 LEU A O     1 
ATOM   3204  C  CB    . LEU A 1 391 ? -1.717  23.602  1.193   1 31.37 ? 391 LEU A CB    1 
ATOM   3205  C  CG    . LEU A 1 391 ? -2.525  23.043  2.345   1 32.56 ? 391 LEU A CG    1 
ATOM   3206  C  CD1   . LEU A 1 391 ? -4.01   23.195  2.075   1 32.78 ? 391 LEU A CD1   1 
ATOM   3207  C  CD2   . LEU A 1 391 ? -2.189  21.582  2.581   1 33.35 ? 391 LEU A CD2   1 
ATOM   3208  N  N     . ILE A 1 392 ? 0.807   23.244  -0.873  1 31.24 ? 392 ILE A N     1 
ATOM   3209  C  CA    . ILE A 1 392 ? 1.268   23.687  -2.184  1 31.43 ? 392 ILE A CA    1 
ATOM   3210  C  C     . ILE A 1 392 ? 0.017   24.158  -2.948  1 31.54 ? 392 ILE A C     1 
ATOM   3211  O  O     . ILE A 1 392 ? -1.078  23.645  -2.711  1 31.5  ? 392 ILE A O     1 
ATOM   3212  C  CB    . ILE A 1 392 ? 2.027   22.554  -2.919  1 31.81 ? 392 ILE A CB    1 
ATOM   3213  C  CG1   . ILE A 1 392 ? 1.169   21.284  -2.983  1 32.97 ? 392 ILE A CG1   1 
ATOM   3214  C  CG2   . ILE A 1 392 ? 3.364   22.277  -2.232  1 32.15 ? 392 ILE A CG2   1 
ATOM   3215  C  CD1   . ILE A 1 392 ? 1.752   20.151  -3.761  1 34.71 ? 392 ILE A CD1   1 
ATOM   3216  N  N     . LYS A 1 393 ? 0.153   25.162  -3.815  1 31.63 ? 393 LYS A N     1 
ATOM   3217  C  CA    . LYS A 1 393 ? -0.989  25.705  -4.554  1 32.17 ? 393 LYS A CA    1 
ATOM   3218  C  C     . LYS A 1 393 ? -1.785  24.632  -5.325  1 32.57 ? 393 LYS A C     1 
ATOM   3219  O  O     . LYS A 1 393 ? -3.011  24.694  -5.364  1 32.88 ? 393 LYS A O     1 
ATOM   3220  C  CB    . LYS A 1 393 ? -0.551  26.86   -5.47   1 33.94 ? 393 LYS A CB    1 
ATOM   3221  C  CG    . LYS A 1 393 ? -1.698  27.571  -6.184  1 37.86 ? 393 LYS A CG    1 
ATOM   3222  C  CD    . LYS A 1 393 ? -2.682  28.231  -5.221  1 41.79 ? 393 LYS A CD    1 
ATOM   3223  C  CE    . LYS A 1 393 ? -2.634  29.732  -5.28   1 45.22 ? 393 LYS A CE    1 
ATOM   3224  N  NZ    . LYS A 1 393 ? -3.14   30.249  -6.578  1 47.68 ? 393 LYS A NZ    1 
ATOM   3225  N  N     . GLY A 1 394 ? -1.097  23.629  -5.859  1 32.33 ? 394 GLY A N     1 
ATOM   3226  C  CA    . GLY A 1 394 ? -1.752  22.541  -6.571  1 32.73 ? 394 GLY A CA    1 
ATOM   3227  C  C     . GLY A 1 394 ? -2.675  21.709  -5.699  1 33.2  ? 394 GLY A C     1 
ATOM   3228  O  O     . GLY A 1 394 ? -3.708  21.23   -6.173  1 33.29 ? 394 GLY A O     1 
ATOM   3229  N  N     . ALA A 1 395 ? -2.32   21.544  -4.404  1 33.32 ? 395 ALA A N     1 
ATOM   3230  C  CA    . ALA A 1 395 ? -3.119  20.771  -3.448  1 33.75 ? 395 ALA A CA    1 
ATOM   3231  C  C     . ALA A 1 395 ? -4.404  21.486  -3.079  1 33.88 ? 395 ALA A C     1 
ATOM   3232  O  O     . ALA A 1 395 ? -5.456  20.855  -3.071  1 33.9  ? 395 ALA A O     1 
ATOM   3233  C  CB    . ALA A 1 395 ? -2.312  20.458  -2.192  1 33.97 ? 395 ALA A CB    1 
ATOM   3234  N  N     . ILE A 1 396 ? -4.342  22.799  -2.815  1 34.01 ? 396 ILE A N     1 
ATOM   3235  C  CA    . ILE A 1 396 ? -5.544  23.557  -2.472  1 34.69 ? 396 ILE A CA    1 
ATOM   3236  C  C     . ILE A 1 396 ? -6.498  23.67   -3.674  1 35.47 ? 396 ILE A C     1 
ATOM   3237  O  O     . ILE A 1 396 ? -7.714  23.641  -3.488  1 35.79 ? 396 ILE A O     1 
ATOM   3238  C  CB    . ILE A 1 396 ? -5.227  24.923  -1.81   1 34.94 ? 396 ILE A CB    1 
ATOM   3239  C  CG1   . ILE A 1 396 ? -6.432  25.452  -1.017  1 35.71 ? 396 ILE A CG1   1 
ATOM   3240  C  CG2   . ILE A 1 396 ? -4.694  25.949  -2.802  1 35.21 ? 396 ILE A CG2   1 
ATOM   3241  C  CD1   . ILE A 1 396 ? -6.897  24.534  0.105   1 36.59 ? 396 ILE A CD1   1 
ATOM   3242  N  N     . ASN A 1 397 ? -5.96   23.705  -4.902  1 35.51 ? 397 ASN A N     1 
ATOM   3243  C  CA    . ASN A 1 397 ? -6.791  23.732  -6.1    1 35.94 ? 397 ASN A CA    1 
ATOM   3244  C  C     . ASN A 1 397 ? -7.544  22.411  -6.241  1 36.35 ? 397 ASN A C     1 
ATOM   3245  O  O     . ASN A 1 397 ? -8.718  22.419  -6.601  1 36.43 ? 397 ASN A O     1 
ATOM   3246  C  CB    . ASN A 1 397 ? -5.951  24.024  -7.335  1 36.88 ? 397 ASN A CB    1 
ATOM   3247  C  CG    . ASN A 1 397 ? -5.506  25.464  -7.415  1 39.85 ? 397 ASN A CG    1 
ATOM   3248  O  OD1   . ASN A 1 397 ? -6.059  26.356  -6.762  1 40.97 ? 397 ASN A OD1   1 
ATOM   3249  N  ND2   . ASN A 1 397 ? -4.48   25.724  -8.202  1 40.66 ? 397 ASN A ND2   1 
ATOM   3250  N  N     . LEU A 1 398 ? -6.894  21.282  -5.91   1 36.59 ? 398 LEU A N     1 
ATOM   3251  C  CA    . LEU A 1 398 ? -7.537  19.967  -5.948  1 37.31 ? 398 LEU A CA    1 
ATOM   3252  C  C     . LEU A 1 398 ? -8.575  19.811  -4.848  1 37.79 ? 398 LEU A C     1 
ATOM   3253  O  O     . LEU A 1 398 ? -9.589  19.162  -5.059  1 37.95 ? 398 LEU A O     1 
ATOM   3254  C  CB    . LEU A 1 398 ? -6.512  18.834  -5.867  1 37.59 ? 398 LEU A CB    1 
ATOM   3255  C  CG    . LEU A 1 398 ? -5.91   18.394  -7.196  1 39.26 ? 398 LEU A CG    1 
ATOM   3256  C  CD1   . LEU A 1 398 ? -4.932  17.254  -6.988  1 40.12 ? 398 LEU A CD1   1 
ATOM   3257  C  CD2   . LEU A 1 398 ? -6.996  17.964  -8.184  1 39.76 ? 398 LEU A CD2   1 
ATOM   3258  N  N     . ILE A 1 399 ? -8.343  20.422  -3.687  1 37.81 ? 399 ILE A N     1 
ATOM   3259  C  CA    . ILE A 1 399 ? -9.306  20.405  -2.592  1 38.38 ? 399 ILE A CA    1 
ATOM   3260  C  C     . ILE A 1 399 ? -10.604 21.113  -3.026  1 38.71 ? 399 ILE A C     1 
ATOM   3261  O  O     . ILE A 1 399 ? -11.696 20.653  -2.699  1 38.95 ? 399 ILE A O     1 
ATOM   3262  C  CB    . ILE A 1 399 ? -8.657  21.045  -1.341  1 39.01 ? 399 ILE A CB    1 
ATOM   3263  C  CG1   . ILE A 1 399 ? -7.648  20.076  -0.711  1 40.09 ? 399 ILE A CG1   1 
ATOM   3264  C  CG2   . ILE A 1 399 ? -9.691  21.5    -0.312  1 39.48 ? 399 ILE A CG2   1 
ATOM   3265  C  CD1   . ILE A 1 399 ? -6.703  20.71   0.21    1 41.49 ? 399 ILE A CD1   1 
ATOM   3266  N  N     . ASP A 1 400 ? -10.485 22.183  -3.82   1 38.6  ? 400 ASP A N     1 
ATOM   3267  C  CA    . ASP A 1 400 ? -11.642 22.925  -4.303  1 39.07 ? 400 ASP A CA    1 
ATOM   3268  C  C     . ASP A 1 400 ? -12.333 22.302  -5.531  1 39.26 ? 400 ASP A C     1 
ATOM   3269  O  O     . ASP A 1 400 ? -13.438 22.723  -5.87   1 39.52 ? 400 ASP A O     1 
ATOM   3270  C  CB    . ASP A 1 400 ? -11.263 24.388  -4.572  1 40.78 ? 400 ASP A CB    1 
ATOM   3271  C  CG    . ASP A 1 400 ? -10.848 25.145  -3.329  1 44.99 ? 400 ASP A CG    1 
ATOM   3272  O  OD1   . ASP A 1 400 ? -11.278 24.754  -2.228  1 45.85 ? 400 ASP A OD1   1 
ATOM   3273  O  OD2   . ASP A 1 400 ? -10.095 26.135  -3.456  1 47.06 ? 400 ASP A OD2   1 
ATOM   3274  N  N     . GLN A 1 401 ? -11.711 21.312  -6.192  1 39.03 ? 401 GLN A N     1 
ATOM   3275  C  CA    . GLN A 1 401 ? -12.319 20.681  -7.368  1 39.35 ? 401 GLN A CA    1 
ATOM   3276  C  C     . GLN A 1 401 ? -12.739 19.224  -7.104  1 39.26 ? 401 GLN A C     1 
ATOM   3277  O  O     . GLN A 1 401 ? -13.895 18.867  -7.334  1 39.41 ? 401 GLN A O     1 
ATOM   3278  C  CB    . GLN A 1 401 ? -11.386 20.777  -8.595  1 41.16 ? 401 GLN A CB    1 
ATOM   3279  C  CG    . GLN A 1 401 ? -11.872 19.964  -9.8    1 45.19 ? 401 GLN A CG    1 
ATOM   3280  C  CD    . GLN A 1 401 ? -10.755 19.561  -10.729 1 49.87 ? 401 GLN A CD    1 
ATOM   3281  O  OE1   . GLN A 1 401 ? -9.694  20.197  -10.775 1 51.8  ? 401 GLN A OE1   1 
ATOM   3282  N  NE2   . GLN A 1 401 ? -10.972 18.493  -11.494 1 49.85 ? 401 GLN A NE2   1 
ATOM   3283  N  N     . ASP A 1 402 ? -11.798 18.388  -6.65   1 38.81 ? 402 ASP A N     1 
ATOM   3284  C  CA    . ASP A 1 402 ? -12.042 16.978  -6.391  1 38.72 ? 402 ASP A CA    1 
ATOM   3285  C  C     . ASP A 1 402 ? -11.037 16.498  -5.364  1 37.89 ? 402 ASP A C     1 
ATOM   3286  O  O     . ASP A 1 402 ? -9.886  16.249  -5.713  1 37.71 ? 402 ASP A O     1 
ATOM   3287  C  CB    . ASP A 1 402 ? -11.87  16.184  -7.695  1 41.04 ? 402 ASP A CB    1 
ATOM   3288  C  CG    . ASP A 1 402 ? -12.43  14.773  -7.671  1 46.38 ? 402 ASP A CG    1 
ATOM   3289  O  OD1   . ASP A 1 402 ? -12.819 14.304  -6.577  1 47.36 ? 402 ASP A OD1   1 
ATOM   3290  O  OD2   . ASP A 1 402 ? -12.487 14.14   -8.748  1 48.65 ? 402 ASP A OD2   1 
ATOM   3291  N  N     . ILE A 1 403 ? -11.458 16.386  -4.098  1 37.37 ? 403 ILE A N     1 
ATOM   3292  C  CA    . ILE A 1 403 ? -10.58  15.929  -3.022  1 37.36 ? 403 ILE A CA    1 
ATOM   3293  C  C     . ILE A 1 403 ? -10.13  14.468  -3.217  1 37.34 ? 403 ILE A C     1 
ATOM   3294  O  O     . ILE A 1 403 ? -9.023  14.113  -2.822  1 37.53 ? 403 ILE A O     1 
ATOM   3295  C  CB    . ILE A 1 403 ? -11.228 16.181  -1.638  1 37.93 ? 403 ILE A CB    1 
ATOM   3296  C  CG1   . ILE A 1 403 ? -10.24  15.974  -0.478  1 38.89 ? 403 ILE A CG1   1 
ATOM   3297  C  CG2   . ILE A 1 403 ? -12.492 15.354  -1.443  1 38.47 ? 403 ILE A CG2   1 
ATOM   3298  C  CD1   . ILE A 1 403 ? -9.02   16.767  -0.547  1 40.2  ? 403 ILE A CD1   1 
ATOM   3299  N  N     . ASN A 1 404 ? -10.953 13.645  -3.886  1 36.92 ? 404 ASN A N     1 
ATOM   3300  C  CA    . ASN A 1 404 ? -10.639 12.241  -4.157  1 36.89 ? 404 ASN A CA    1 
ATOM   3301  C  C     . ASN A 1 404 ? -9.458  12.087  -5.114  1 36.82 ? 404 ASN A C     1 
ATOM   3302  O  O     . ASN A 1 404 ? -8.737  11.095  -5.023  1 37.21 ? 404 ASN A O     1 
ATOM   3303  C  CB    . ASN A 1 404 ? -11.862 11.516  -4.694  1 38    ? 404 ASN A CB    1 
ATOM   3304  C  CG    . ASN A 1 404 ? -13.057 11.704  -3.814  1 41.69 ? 404 ASN A CG    1 
ATOM   3305  O  OD1   . ASN A 1 404 ? -13.045 11.325  -2.643  1 43.02 ? 404 ASN A OD1   1 
ATOM   3306  N  ND2   . ASN A 1 404 ? -14.091 12.348  -4.338  1 42.6  ? 404 ASN A ND2   1 
ATOM   3307  N  N     . LYS A 1 405 ? -9.253  13.063  -6.022  1 36.09 ? 405 LYS A N     1 
ATOM   3308  C  CA    . LYS A 1 405 ? -8.12   13.072  -6.953  1 35.77 ? 405 LYS A CA    1 
ATOM   3309  C  C     . LYS A 1 405 ? -6.812  13.261  -6.166  1 35.35 ? 405 LYS A C     1 
ATOM   3310  O  O     . LYS A 1 405 ? -5.798  12.653  -6.495  1 35.59 ? 405 LYS A O     1 
ATOM   3311  C  CB    . LYS A 1 405 ? -8.258  14.23   -7.953  1 37.26 ? 405 LYS A CB    1 
ATOM   3312  C  CG    . LYS A 1 405 ? -9.135  13.956  -9.156  1 40.79 ? 405 LYS A CG    1 
ATOM   3313  C  CD    . LYS A 1 405 ? -9.115  15.157  -10.098 1 44.3  ? 405 LYS A CD    1 
ATOM   3314  C  CE    . LYS A 1 405 ? -10.055 15.017  -11.265 1 47.34 ? 405 LYS A CE    1 
ATOM   3315  N  NZ    . LYS A 1 405 ? -10.16  16.289  -12.024 1 49.52 ? 405 LYS A NZ    1 
ATOM   3316  N  N     . LEU A 1 406 ? -6.838  14.121  -5.143  1 34.57 ? 406 LEU A N     1 
ATOM   3317  C  CA    . LEU A 1 406 ? -5.689  14.378  -4.294  1 34.34 ? 406 LEU A CA    1 
ATOM   3318  C  C     . LEU A 1 406 ? -5.409  13.136  -3.434  1 34.23 ? 406 LEU A C     1 
ATOM   3319  O  O     . LEU A 1 406 ? -4.261  12.714  -3.321  1 34.27 ? 406 LEU A O     1 
ATOM   3320  C  CB    . LEU A 1 406 ? -5.984  15.609  -3.425  1 34.38 ? 406 LEU A CB    1 
ATOM   3321  C  CG    . LEU A 1 406 ? -4.873  16.119  -2.524  1 35.83 ? 406 LEU A CG    1 
ATOM   3322  C  CD1   . LEU A 1 406 ? -3.619  16.42   -3.307  1 36.38 ? 406 LEU A CD1   1 
ATOM   3323  C  CD2   . LEU A 1 406 ? -5.316  17.363  -1.789  1 36.64 ? 406 LEU A CD2   1 
ATOM   3324  N  N     . ALA A 1 407 ? -6.463  12.518  -2.884  1 33.97 ? 407 ALA A N     1 
ATOM   3325  C  CA    . ALA A 1 407 ? -6.346  11.309  -2.072  1 34.22 ? 407 ALA A CA    1 
ATOM   3326  C  C     . ALA A 1 407 ? -5.772  10.145  -2.874  1 34.35 ? 407 ALA A C     1 
ATOM   3327  O  O     . ALA A 1 407 ? -5.037  9.333   -2.319  1 34.4  ? 407 ALA A O     1 
ATOM   3328  C  CB    . ALA A 1 407 ? -7.704  10.929  -1.517  1 34.47 ? 407 ALA A CB    1 
ATOM   3329  N  N     . LYS A 1 408 ? -6.096  10.074  -4.176  1 34.29 ? 408 LYS A N     1 
ATOM   3330  C  CA    . LYS A 1 408 ? -5.625  9.035   -5.086  1 34.73 ? 408 LYS A CA    1 
ATOM   3331  C  C     . LYS A 1 408 ? -4.106  9.081   -5.279  1 34.88 ? 408 LYS A C     1 
ATOM   3332  O  O     . LYS A 1 408 ? -3.46   8.031   -5.336  1 35.03 ? 408 LYS A O     1 
ATOM   3333  C  CB    . LYS A 1 408 ? -6.319  9.166   -6.456  1 36.55 ? 408 LYS A CB    1 
ATOM   3334  C  CG    . LYS A 1 408 ? -5.998  8.019   -7.414  1 40.62 ? 408 LYS A CG    1 
ATOM   3335  C  CD    . LYS A 1 408 ? -6.463  8.288   -8.839  1 44.86 ? 408 LYS A CD    1 
ATOM   3336  C  CE    . LYS A 1 408 ? -5.465  9.114   -9.619  1 48.25 ? 408 LYS A CE    1 
ATOM   3337  N  NZ    . LYS A 1 408 ? -4.191  8.376   -9.868  1 49.85 ? 408 LYS A NZ    1 
ATOM   3338  N  N     . ARG A 1 409 ? -3.532  10.286  -5.367  1 34.65 ? 409 ARG A N     1 
ATOM   3339  C  CA    . ARG A 1 409 ? -2.096  10.415  -5.589  1 34.87 ? 409 ARG A CA    1 
ATOM   3340  C  C     . ARG A 1 409 ? -1.25   10.53   -4.308  1 34.52 ? 409 ARG A C     1 
ATOM   3341  O  O     . ARG A 1 409 ? -0.071  10.184  -4.351  1 34.83 ? 409 ARG A O     1 
ATOM   3342  C  CB    . ARG A 1 409 ? -1.789  11.583  -6.543  1 36.62 ? 409 ARG A CB    1 
ATOM   3343  C  CG    . ARG A 1 409 ? -2.295  12.934  -6.057  1 40.3  ? 409 ARG A CG    1 
ATOM   3344  C  CD    . ARG A 1 409 ? -1.922  14.066  -7.003  1 44.1  ? 409 ARG A CD    1 
ATOM   3345  N  NE    . ARG A 1 409 ? -0.473  14.217  -7.184  1 47.54 ? 409 ARG A NE    1 
ATOM   3346  C  CZ    . ARG A 1 409 ? 0.239   15.259  -6.75   1 50.41 ? 409 ARG A CZ    1 
ATOM   3347  N  NH1   . ARG A 1 409 ? -0.347  16.237  -6.07   1 50.3  ? 409 ARG A NH1   1 
ATOM   3348  N  NH2   . ARG A 1 409 ? 1.548   15.315  -6.972  1 50.57 ? 409 ARG A NH2   1 
ATOM   3349  N  N     . ASN A 1 410 ? -1.826  10.99   -3.185  1 33.55 ? 410 ASN A N     1 
ATOM   3350  C  CA    . ASN A 1 410 ? -1.056  11.171  -1.96   1 33.41 ? 410 ASN A CA    1 
ATOM   3351  C  C     . ASN A 1 410 ? -1.571  10.319  -0.786  1 33.31 ? 410 ASN A C     1 
ATOM   3352  O  O     . ASN A 1 410 ? -2.766  10.301  -0.506  1 33.55 ? 410 ASN A O     1 
ATOM   3353  C  CB    . ASN A 1 410 ? -1.027  12.652  -1.6    1 34.42 ? 410 ASN A CB    1 
ATOM   3354  C  CG    . ASN A 1 410 ? -0.107  12.994  -0.466  1 37.32 ? 410 ASN A CG    1 
ATOM   3355  O  OD1   . ASN A 1 410 ? -0.469  12.888  0.705   1 38.34 ? 410 ASN A OD1   1 
ATOM   3356  N  ND2   . ASN A 1 410 ? 1.105   13.423  -0.788  1 37.96 ? 410 ASN A ND2   1 
ATOM   3357  N  N     . GLY A 1 411 ? -0.659  9.636   -0.104  1 32.61 ? 411 GLY A N     1 
ATOM   3358  C  CA    . GLY A 1 411 ? -0.988  8.778   1.026   1 32.45 ? 411 GLY A CA    1 
ATOM   3359  C  C     . GLY A 1 411 ? -1.502  9.478   2.27    1 32.08 ? 411 GLY A C     1 
ATOM   3360  O  O     . GLY A 1 411 ? -2.291  8.891   3.021   1 32    ? 411 GLY A O     1 
ATOM   3361  N  N     . LEU A 1 412 ? -1.061  10.728  2.515   1 31.49 ? 412 LEU A N     1 
ATOM   3362  C  CA    . LEU A 1 412 ? -1.555  11.468  3.677   1 31.43 ? 412 LEU A CA    1 
ATOM   3363  C  C     . LEU A 1 412 ? -2.984  11.927  3.427   1 31.27 ? 412 LEU A C     1 
ATOM   3364  O  O     . LEU A 1 412 ? -3.841  11.774  4.304   1 31.6  ? 412 LEU A O     1 
ATOM   3365  C  CB    . LEU A 1 412 ? -0.669  12.654  4.075   1 31.31 ? 412 LEU A CB    1 
ATOM   3366  C  CG    . LEU A 1 412 ? -1.161  13.392  5.322   1 31.95 ? 412 LEU A CG    1 
ATOM   3367  C  CD1   . LEU A 1 412 ? -1.164  12.511  6.534   1 32.16 ? 412 LEU A CD1   1 
ATOM   3368  C  CD2   . LEU A 1 412 ? -0.363  14.591  5.597   1 32.4  ? 412 LEU A CD2   1 
ATOM   3369  N  N     . TRP A 1 413 ? -3.253  12.443  2.221   1 30.51 ? 413 TRP A N     1 
ATOM   3370  C  CA    . TRP A 1 413 ? -4.609  12.829  1.862   1 30.42 ? 413 TRP A CA    1 
ATOM   3371  C  C     . TRP A 1 413 ? -5.531  11.614  1.81    1 30.28 ? 413 TRP A C     1 
ATOM   3372  O  O     . TRP A 1 413 ? -6.689  11.738  2.164   1 30.29 ? 413 TRP A O     1 
ATOM   3373  C  CB    . TRP A 1 413 ? -4.646  13.638  0.562   1 30.5  ? 413 TRP A CB    1 
ATOM   3374  C  CG    . TRP A 1 413 ? -4.162  15.047  0.741   1 30.97 ? 413 TRP A CG    1 
ATOM   3375  C  CD1   . TRP A 1 413 ? -3.002  15.584  0.269   1 31.88 ? 413 TRP A CD1   1 
ATOM   3376  C  CD2   . TRP A 1 413 ? -4.808  16.081  1.492   1 30.93 ? 413 TRP A CD2   1 
ATOM   3377  N  NE1   . TRP A 1 413 ? -2.892  16.894  0.672   1 32.08 ? 413 TRP A NE1   1 
ATOM   3378  C  CE2   . TRP A 1 413 ? -3.987  17.221  1.429   1 31.61 ? 413 TRP A CE2   1 
ATOM   3379  C  CE3   . TRP A 1 413 ? -5.993  16.148  2.23    1 31.48 ? 413 TRP A CE3   1 
ATOM   3380  C  CZ2   . TRP A 1 413 ? -4.314  18.408  2.074   1 32.09 ? 413 TRP A CZ2   1 
ATOM   3381  C  CZ3   . TRP A 1 413 ? -6.309  17.323  2.873   1 32.25 ? 413 TRP A CZ3   1 
ATOM   3382  C  CH2   . TRP A 1 413 ? -5.473  18.435  2.793   1 32.24 ? 413 TRP A CH2   1 
ATOM   3383  N  N     . LYS A 1 414 ? -5.004  10.428  1.454   1 30.09 ? 414 LYS A N     1 
ATOM   3384  C  CA    . LYS A 1 414 ? -5.748  9.166   1.439   1 30.05 ? 414 LYS A CA    1 
ATOM   3385  C  C     . LYS A 1 414 ? -6.18   8.786   2.873   1 29.86 ? 414 LYS A C     1 
ATOM   3386  O  O     . LYS A 1 414 ? -7.304  8.341   3.076   1 29.63 ? 414 LYS A O     1 
ATOM   3387  C  CB    . LYS A 1 414 ? -4.875  8.056   0.835   1 31.35 ? 414 LYS A CB    1 
ATOM   3388  C  CG    . LYS A 1 414 ? -5.656  6.892   0.252   1 34.48 ? 414 LYS A CG    1 
ATOM   3389  C  CD    . LYS A 1 414 ? -4.725  5.725   -0.13   1 38.3  ? 414 LYS A CD    1 
ATOM   3390  C  CE    . LYS A 1 414 ? -3.649  6.125   -1.123  1 41.4  ? 414 LYS A CE    1 
ATOM   3391  N  NZ    . LYS A 1 414 ? -2.799  4.997   -1.572  1 42.95 ? 414 LYS A NZ    1 
ATOM   3392  N  N     . SER A 1 415 ? -5.297  8.986   3.861   1 29.83 ? 415 SER A N     1 
ATOM   3393  C  CA    . SER A 1 415 ? -5.589  8.719   5.274   1 30.35 ? 415 SER A CA    1 
ATOM   3394  C  C     . SER A 1 415 ? -6.681  9.669   5.787   1 30.75 ? 415 SER A C     1 
ATOM   3395  O  O     . SER A 1 415 ? -7.591  9.233   6.488   1 30.78 ? 415 SER A O     1 
ATOM   3396  C  CB    . SER A 1 415 ? -4.324  8.886   6.116   1 31.46 ? 415 SER A CB    1 
ATOM   3397  O  OG    . SER A 1 415 ? -4.59   8.81    7.507   1 33.37 ? 415 SER A OG    1 
ATOM   3398  N  N     . PHE A 1 416 ? -6.589  10.962  5.43    1 30.87 ? 416 PHE A N     1 
ATOM   3399  C  CA    . PHE A 1 416 ? -7.548  11.983  5.846   1 31.49 ? 416 PHE A CA    1 
ATOM   3400  C  C     . PHE A 1 416 ? -8.927  11.806  5.216   1 32.11 ? 416 PHE A C     1 
ATOM   3401  O  O     . PHE A 1 416 ? -9.935  11.92   5.906   1 32.42 ? 416 PHE A O     1 
ATOM   3402  C  CB    . PHE A 1 416 ? -7.024  13.384  5.518   1 31.29 ? 416 PHE A CB    1 
ATOM   3403  C  CG    . PHE A 1 416 ? -5.787  13.823  6.256   1 31.91 ? 416 PHE A CG    1 
ATOM   3404  C  CD1   . PHE A 1 416 ? -5.449  13.259  7.473   1 32.84 ? 416 PHE A CD1   1 
ATOM   3405  C  CD2   . PHE A 1 416 ? -5.005  14.85   5.771   1 32.75 ? 416 PHE A CD2   1 
ATOM   3406  C  CE1   . PHE A 1 416 ? -4.327  13.684  8.165   1 33.66 ? 416 PHE A CE1   1 
ATOM   3407  C  CE2   . PHE A 1 416 ? -3.895  15.285  6.47    1 33.6  ? 416 PHE A CE2   1 
ATOM   3408  C  CZ    . PHE A 1 416 ? -3.562  14.698  7.665   1 33.52 ? 416 PHE A CZ    1 
ATOM   3409  N  N     . VAL A 1 417 ? -8.972  11.567  3.906   1 32.14 ? 417 VAL A N     1 
ATOM   3410  C  CA    . VAL A 1 417 ? -10.213 11.409  3.156   1 32.77 ? 417 VAL A CA    1 
ATOM   3411  C  C     . VAL A 1 417 ? -10.938 10.109  3.513   1 33.61 ? 417 VAL A C     1 
ATOM   3412  O  O     . VAL A 1 417 ? -12.165 10.075  3.535   1 33.69 ? 417 VAL A O     1 
ATOM   3413  C  CB    . VAL A 1 417 ? -9.922  11.551  1.637   1 33.31 ? 417 VAL A CB    1 
ATOM   3414  C  CG1   . VAL A 1 417 ? -11.112 11.146  0.781   1 33.69 ? 417 VAL A CG1   1 
ATOM   3415  C  CG2   . VAL A 1 417 ? -9.481  12.968  1.311   1 33.79 ? 417 VAL A CG2   1 
ATOM   3416  N  N     . SER A 1 418 ? -10.189 9.058   3.845   1 34.11 ? 418 SER A N     1 
ATOM   3417  C  CA    . SER A 1 418 ? -10.782 7.771   4.185   1 34.93 ? 418 SER A CA    1 
ATOM   3418  C  C     . SER A 1 418 ? -11.377 7.7     5.582   1 35.77 ? 418 SER A C     1 
ATOM   3419  O  O     . SER A 1 418 ? -12.319 6.934   5.79    1 36.11 ? 418 SER A O     1 
ATOM   3420  C  CB    . SER A 1 418 ? -9.74   6.671   4.069   1 36    ? 418 SER A CB    1 
ATOM   3421  O  OG    . SER A 1 418 ? -9.14   6.643   2.787   1 38.16 ? 418 SER A OG    1 
ATOM   3422  N  N     . LEU A 1 419 ? -10.796 8.421   6.556   1 35.87 ? 419 LEU A N     1 
ATOM   3423  C  CA    . LEU A 1 419 ? -11.236 8.278   7.94    1 36.42 ? 419 LEU A CA    1 
ATOM   3424  C  C     . LEU A 1 419 ? -11.868 9.495   8.594   1 36.66 ? 419 LEU A C     1 
ATOM   3425  O  O     . LEU A 1 419 ? -12.364 9.352   9.714   1 36.89 ? 419 LEU A O     1 
ATOM   3426  C  CB    . LEU A 1 419 ? -10.071 7.795   8.799   1 36.79 ? 419 LEU A CB    1 
ATOM   3427  C  CG    . LEU A 1 419 ? -9.627  6.385   8.489   1 38.52 ? 419 LEU A CG    1 
ATOM   3428  C  CD1   . LEU A 1 419 ? -8.308  6.075   9.147   1 39.3  ? 419 LEU A CD1   1 
ATOM   3429  C  CD2   . LEU A 1 419 ? -10.692 5.385   8.889   1 39.2  ? 419 LEU A CD2   1 
ATOM   3430  N  N     . SER A 1 420 ? -11.871 10.665  7.936   1 36.33 ? 420 SER A N     1 
ATOM   3431  C  CA    . SER A 1 420 ? -12.474 11.845  8.552   1 36.49 ? 420 SER A CA    1 
ATOM   3432  C  C     . SER A 1 420 ? -13.909 12.036  8.142   1 36.88 ? 420 SER A C     1 
ATOM   3433  O  O     . SER A 1 420 ? -14.216 12.001  6.958   1 37    ? 420 SER A O     1 
ATOM   3434  C  CB    . SER A 1 420 ? -11.716 13.112  8.179   1 37.12 ? 420 SER A CB    1 
ATOM   3435  O  OG    . SER A 1 420 ? -10.311 12.982  8.29    1 38.58 ? 420 SER A OG    1 
ATOM   3436  N  N     . ASP A 1 421 ? -14.781 12.298  9.107   1 36.96 ? 421 ASP A N     1 
ATOM   3437  C  CA    . ASP A 1 421 ? -16.161 12.67   8.815   1 37.62 ? 421 ASP A CA    1 
ATOM   3438  C  C     . ASP A 1 421 ? -16.202 14.181  8.448   1 37.94 ? 421 ASP A C     1 
ATOM   3439  O  O     . ASP A 1 421 ? -17.034 14.602  7.65    1 37.99 ? 421 ASP A O     1 
ATOM   3440  C  CB    . ASP A 1 421 ? -17.073 12.362  10.006  1 39.52 ? 421 ASP A CB    1 
ATOM   3441  C  CG    . ASP A 1 421 ? -17.238 10.878  10.241  1 44.73 ? 421 ASP A CG    1 
ATOM   3442  O  OD1   . ASP A 1 421 ? -16.34  10.276  10.862  1 45.86 ? 421 ASP A OD1   1 
ATOM   3443  O  OD2   . ASP A 1 421 ? -18.258 10.315  9.79    1 46.94 ? 421 ASP A OD2   1 
ATOM   3444  N  N     . PHE A 1 422 ? -15.291 14.988  9.019   1 37.88 ? 422 PHE A N     1 
ATOM   3445  C  CA    . PHE A 1 422 ? -15.191 16.412  8.746   1 38.08 ? 422 PHE A CA    1 
ATOM   3446  C  C     . PHE A 1 422 ? -13.715 16.747  8.584   1 38.55 ? 422 PHE A C     1 
ATOM   3447  O  O     . PHE A 1 422 ? -12.9   16.315  9.398   1 38.68 ? 422 PHE A O     1 
ATOM   3448  C  CB    . PHE A 1 422 ? -15.776 17.223  9.911   1 37.74 ? 422 PHE A CB    1 
ATOM   3449  C  CG    . PHE A 1 422 ? -17.133 16.76   10.387  1 38.12 ? 422 PHE A CG    1 
ATOM   3450  C  CD1   . PHE A 1 422 ? -18.281 17.114  9.705   1 38.89 ? 422 PHE A CD1   1 
ATOM   3451  C  CD2   . PHE A 1 422 ? -17.255 15.953  11.505  1 38.62 ? 422 PHE A CD2   1 
ATOM   3452  C  CE1   . PHE A 1 422 ? -19.527 16.682  10.141  1 39.46 ? 422 PHE A CE1   1 
ATOM   3453  C  CE2   . PHE A 1 422 ? -18.503 15.527  11.941  1 39.24 ? 422 PHE A CE2   1 
ATOM   3454  C  CZ    . PHE A 1 422 ? -19.629 15.896  11.26   1 39.1  ? 422 PHE A CZ    1 
ATOM   3455  N  N     . ILE A 1 423 ? -13.361 17.487  7.525   1 38.75 ? 423 ILE A N     1 
ATOM   3456  C  CA    . ILE A 1 423 ? -11.98  17.902  7.298   1 39.42 ? 423 ILE A CA    1 
ATOM   3457  C  C     . ILE A 1 423 ? -11.924 19.409  7.369   1 40.36 ? 423 ILE A C     1 
ATOM   3458  O  O     . ILE A 1 423 ? -12.556 20.077  6.56    1 40.75 ? 423 ILE A O     1 
ATOM   3459  C  CB    . ILE A 1 423 ? -11.427 17.407  5.946   1 39.74 ? 423 ILE A CB    1 
ATOM   3460  C  CG1   . ILE A 1 423 ? -11.427 15.878  5.88    1 40.62 ? 423 ILE A CG1   1 
ATOM   3461  C  CG2   . ILE A 1 423 ? -10.025 17.965  5.709   1 40.17 ? 423 ILE A CG2   1 
ATOM   3462  C  CD1   . ILE A 1 423 ? -11.124 15.303  4.526   1 41.71 ? 423 ILE A CD1   1 
ATOM   3463  N  N     . VAL A 1 424 ? -11.188 19.952  8.335   1 40.56 ? 424 VAL A N     1 
ATOM   3464  C  CA    . VAL A 1 424 ? -11.065 21.389  8.497   1 41.21 ? 424 VAL A CA    1 
ATOM   3465  C  C     . VAL A 1 424 ? -9.643  21.812  8.253   1 41.69 ? 424 VAL A C     1 
ATOM   3466  O  O     . VAL A 1 424 ? -8.725  21.252  8.842   1 41.74 ? 424 VAL A O     1 
ATOM   3467  C  CB    . VAL A 1 424 ? -11.532 21.821  9.887   1 42.12 ? 424 VAL A CB    1 
ATOM   3468  C  CG1   . VAL A 1 424 ? -11.371 23.323  10.067  1 42.89 ? 424 VAL A CG1   1 
ATOM   3469  C  CG2   . VAL A 1 424 ? -12.972 21.405  10.108  1 42.62 ? 424 VAL A CG2   1 
ATOM   3470  N  N     . LEU A 1 425 ? -9.452  22.792  7.378   1 41.91 ? 425 LEU A N     1 
ATOM   3471  C  CA    . LEU A 1 425 ? -8.124  23.29   7.071   1 42.6  ? 425 LEU A CA    1 
ATOM   3472  C  C     . LEU A 1 425 ? -8.017  24.743  7.482   1 42.99 ? 425 LEU A C     1 
ATOM   3473  O  O     . LEU A 1 425 ? -8.936  25.51   7.253   1 43.09 ? 425 LEU A O     1 
ATOM   3474  C  CB    . LEU A 1 425 ? -7.856  23.207  5.558   1 43    ? 425 LEU A CB    1 
ATOM   3475  C  CG    . LEU A 1 425 ? -8.184  21.893  4.868   1 44.7  ? 425 LEU A CG    1 
ATOM   3476  C  CD1   . LEU A 1 425 ? -8.056  22.019  3.368   1 45.21 ? 425 LEU A CD1   1 
ATOM   3477  C  CD2   . LEU A 1 425 ? -7.307  20.786  5.376   1 45.5  ? 425 LEU A CD2   1 
ATOM   3478  N  N     . ASP A 1 426 ? -6.897  25.127  8.068   1 43.04 ? 426 ASP A N     1 
ATOM   3479  C  CA    . ASP A 1 426 ? -6.577  26.518  8.368   1 43.56 ? 426 ASP A CA    1 
ATOM   3480  C  C     . ASP A 1 426 ? -5.112  26.521  8.015   1 43.51 ? 426 ASP A C     1 
ATOM   3481  O  O     . ASP A 1 426 ? -4.252  26.438  8.888   1 43.7  ? 426 ASP A O     1 
ATOM   3482  C  CB    . ASP A 1 426 ? -6.797  26.878  9.844   1 45.67 ? 426 ASP A CB    1 
ATOM   3483  C  CG    . ASP A 1 426 ? -6.625  28.361  10.157  1 51.01 ? 426 ASP A CG    1 
ATOM   3484  O  OD1   . ASP A 1 426 ? -6.226  29.129  9.245   1 51.6  ? 426 ASP A OD1   1 
ATOM   3485  O  OD2   . ASP A 1 426 ? -6.892  28.756  11.309  1 53.77 ? 426 ASP A OD2   1 
ATOM   3486  N  N     . CYS A 1 427 ? -4.837  26.52   6.711   1 43.11 ? 427 CYS A N     1 
ATOM   3487  C  CA    . CYS A 1 427 ? -3.499  26.328  6.187   1 43.25 ? 427 CYS A CA    1 
ATOM   3488  C  C     . CYS A 1 427 ? -2.893  27.494  5.433   1 43.27 ? 427 CYS A C     1 
ATOM   3489  O  O     . CYS A 1 427 ? -3.512  28.023  4.509   1 43.5  ? 427 CYS A O     1 
ATOM   3490  C  CB    . CYS A 1 427 ? -3.491  25.084  5.301   1 43.59 ? 427 CYS A CB    1 
ATOM   3491  S  SG    . CYS A 1 427 ? -4.056  23.576  6.126   1 45.26 ? 427 CYS A SG    1 
ATOM   3492  N  N     . PRO A 1 428 ? -1.593  27.755  5.668   1 42.77 ? 428 PRO A N     1 
ATOM   3493  C  CA    . PRO A 1 428 ? -0.883  28.711  4.808   1 42.54 ? 428 PRO A CA    1 
ATOM   3494  C  C     . PRO A 1 428 ? -0.735  28.12   3.402   1 42.38 ? 428 PRO A C     1 
ATOM   3495  O  O     . PRO A 1 428 ? -0.692  26.898  3.248   1 42.61 ? 428 PRO A O     1 
ATOM   3496  C  CB    . PRO A 1 428 ? 0.5     28.827  5.464   1 43.27 ? 428 PRO A CB    1 
ATOM   3497  C  CG    . PRO A 1 428 ? 0.385   28.159  6.801   1 43.73 ? 428 PRO A CG    1 
ATOM   3498  C  CD    . PRO A 1 428 ? -0.688  27.136  6.654   1 42.2  ? 428 PRO A CD    1 
ATOM   3499  N  N     . ILE A 1 429 ? -0.667  28.97   2.38    1 42    ? 429 ILE A N     1 
ATOM   3500  C  CA    . ILE A 1 429 ? -0.498  28.492  1.009   1 42.16 ? 429 ILE A CA    1 
ATOM   3501  C  C     . ILE A 1 429 ? 0.859   28.941  0.509   1 42.17 ? 429 ILE A C     1 
ATOM   3502  O  O     . ILE A 1 429 ? 1.158   30.131  0.574   1 42.38 ? 429 ILE A O     1 
ATOM   3503  C  CB    . ILE A 1 429 ? -1.636  28.978  0.08    1 42.53 ? 429 ILE A CB    1 
ATOM   3504  C  CG1   . ILE A 1 429 ? -3.011  28.622  0.653   1 43.41 ? 429 ILE A CG1   1 
ATOM   3505  C  CG2   . ILE A 1 429 ? -1.464  28.43   -1.331  1 42.88 ? 429 ILE A CG2   1 
ATOM   3506  C  CD1   . ILE A 1 429 ? -3.263  27.155  0.842   1 44.64 ? 429 ILE A CD1   1 
ATOM   3507  N  N     . ILE A 1 430 ? 1.69    28.001  0.019   1 41.74 ? 430 ILE A N     1 
ATOM   3508  C  CA    . ILE A 1 430 ? 3.02    28.303  -0.52   1 41.72 ? 430 ILE A CA    1 
ATOM   3509  C  C     . ILE A 1 430 ? 2.917   29.341  -1.645  1 41.99 ? 430 ILE A C     1 
ATOM   3510  O  O     . ILE A 1 430 ? 2.246   29.098  -2.644  1 42.23 ? 430 ILE A O     1 
ATOM   3511  C  CB    . ILE A 1 430 ? 3.71    27.008  -1.011  1 41.74 ? 430 ILE A CB    1 
ATOM   3512  C  CG1   . ILE A 1 430 ? 3.78    25.943  0.102   1 42.23 ? 430 ILE A CG1   1 
ATOM   3513  C  CG2   . ILE A 1 430 ? 5.082   27.305  -1.608  1 42.15 ? 430 ILE A CG2   1 
ATOM   3514  C  CD1   . ILE A 1 430 ? 4.566   26.333  1.269   1 43.22 ? 430 ILE A CD1   1 
ATOM   3515  N  N     . GLY A 1 431 ? 3.519   30.505  -1.435  1 41.79 ? 431 GLY A N     1 
ATOM   3516  C  CA    . GLY A 1 431 ? 3.467   31.592  -2.406  1 42.12 ? 431 GLY A CA    1 
ATOM   3517  C  C     . GLY A 1 431 ? 2.416   32.652  -2.119  1 42.15 ? 431 GLY A C     1 
ATOM   3518  O  O     . GLY A 1 431 ? 2.307   33.629  -2.86   1 42.28 ? 431 GLY A O     1 
ATOM   3519  N  N     . GLU A 1 432 ? 1.618   32.468  -1.059  1 41.82 ? 432 GLU A N     1 
ATOM   3520  C  CA    . GLU A 1 432 ? 0.58    33.415  -0.672  1 42.18 ? 432 GLU A CA    1 
ATOM   3521  C  C     . GLU A 1 432 ? 0.819   33.958  0.739   1 42.61 ? 432 GLU A C     1 
ATOM   3522  O  O     . GLU A 1 432 ? 1.5     33.324  1.539   1 42.83 ? 432 GLU A O     1 
ATOM   3523  C  CB    . GLU A 1 432 ? -0.808  32.789  -0.806  1 44.25 ? 432 GLU A CB    1 
ATOM   3524  C  CG    . GLU A 1 432 ? -1.111  32.349  -2.223  1 49.28 ? 432 GLU A CG    1 
ATOM   3525  C  CD    . GLU A 1 432 ? -2.586  32.158  -2.504  1 56.28 ? 432 GLU A CD    1 
ATOM   3526  O  OE1   . GLU A 1 432 ? -3.293  31.62   -1.622  1 57.88 ? 432 GLU A OE1   1 
ATOM   3527  O  OE2   . GLU A 1 432 ? -3.041  32.565  -3.598  1 58.3  ? 432 GLU A OE2   1 
ATOM   3528  N  N     . SER A 1 433 ? 0.269   35.135  1.044   1 42.63 ? 433 SER A N     1 
ATOM   3529  C  CA    . SER A 1 433 ? 0.501   35.793  2.327   1 43.24 ? 433 SER A CA    1 
ATOM   3530  C  C     . SER A 1 433 ? -0.328  35.283  3.505   1 43.58 ? 433 SER A C     1 
ATOM   3531  O  O     . SER A 1 433 ? 0.153   35.34   4.637   1 43.66 ? 433 SER A O     1 
ATOM   3532  C  CB    . SER A 1 433 ? 0.309   37.304  2.208   1 44.63 ? 433 SER A CB    1 
ATOM   3533  O  OG    . SER A 1 433 ? 0.854   37.86   1.023   1 47.04 ? 433 SER A OG    1 
ATOM   3534  N  N     . TYR A 1 434 ? -1.584  34.87   3.273   1 43.49 ? 434 TYR A N     1 
ATOM   3535  C  CA    . TYR A 1 434 ? -2.45   34.453  4.372   1 43.89 ? 434 TYR A CA    1 
ATOM   3536  C  C     . TYR A 1 434 ? -3.077  33.061  4.17    1 44.18 ? 434 TYR A C     1 
ATOM   3537  O  O     . TYR A 1 434 ? -3.005  32.481  3.084   1 44.34 ? 434 TYR A O     1 
ATOM   3538  C  CB    . TYR A 1 434 ? -3.507  35.533  4.679   1 43.97 ? 434 TYR A CB    1 
ATOM   3539  C  CG    . TYR A 1 434 ? -2.865  36.833  5.111   1 44.89 ? 434 TYR A CG    1 
ATOM   3540  C  CD1   . TYR A 1 434 ? -2.388  37      6.403   1 45.83 ? 434 TYR A CD1   1 
ATOM   3541  C  CD2   . TYR A 1 434 ? -2.624  37.847  4.196   1 45.84 ? 434 TYR A CD2   1 
ATOM   3542  C  CE1   . TYR A 1 434 ? -1.733  38.164  6.786   1 46.77 ? 434 TYR A CE1   1 
ATOM   3543  C  CE2   . TYR A 1 434 ? -1.967  39.014  4.566   1 46.7  ? 434 TYR A CE2   1 
ATOM   3544  C  CZ    . TYR A 1 434 ? -1.531  39.174  5.866   1 47.65 ? 434 TYR A CZ    1 
ATOM   3545  O  OH    . TYR A 1 434 ? -0.883  40.325  6.237   1 49.26 ? 434 TYR A OH    1 
ATOM   3546  N  N     . ASN A 1 435 ? -3.634  32.505  5.258   1 43.9  ? 435 ASN A N     1 
ATOM   3547  C  CA    . ASN A 1 435 ? -4.227  31.176  5.295   1 43.98 ? 435 ASN A CA    1 
ATOM   3548  C  C     . ASN A 1 435 ? -5.544  31.034  4.554   1 43.83 ? 435 ASN A C     1 
ATOM   3549  O  O     . ASN A 1 435 ? -6.264  32.007  4.329   1 43.75 ? 435 ASN A O     1 
ATOM   3550  C  CB    . ASN A 1 435 ? -4.426  30.737  6.741   1 45.16 ? 435 ASN A CB    1 
ATOM   3551  C  CG    . ASN A 1 435 ? -3.157  30.348  7.43    1 48.47 ? 435 ASN A CG    1 
ATOM   3552  O  OD1   . ASN A 1 435 ? -2.061  30.772  7.055   1 49.39 ? 435 ASN A OD1   1 
ATOM   3553  N  ND2   . ASN A 1 435 ? -3.286  29.538  8.464   1 49.48 ? 435 ASN A ND2   1 
ATOM   3554  N  N     . GLU A 1 436 ? -5.865  29.784  4.212   1 43.64 ? 436 GLU A N     1 
ATOM   3555  C  CA    . GLU A 1 436 ? -7.111  29.391  3.579   1 43.62 ? 436 GLU A CA    1 
ATOM   3556  C  C     . GLU A 1 436 ? -7.883  28.573  4.587   1 43    ? 436 GLU A C     1 
ATOM   3557  O  O     . GLU A 1 436 ? -7.32   27.653  5.18    1 42.91 ? 436 GLU A O     1 
ATOM   3558  C  CB    . GLU A 1 436 ? -6.838  28.512  2.352   1 45.77 ? 436 GLU A CB    1 
ATOM   3559  C  CG    . GLU A 1 436 ? -6.412  29.29   1.132   1 50.7  ? 436 GLU A CG    1 
ATOM   3560  C  CD    . GLU A 1 436 ? -7.51   30.13   0.525   1 57.61 ? 436 GLU A CD    1 
ATOM   3561  O  OE1   . GLU A 1 436 ? -7.74   31.264  1.003   1 59.11 ? 436 GLU A OE1   1 
ATOM   3562  O  OE2   . GLU A 1 436 ? -8.152  29.647  -0.434  1 60.19 ? 436 GLU A OE2   1 
ATOM   3563  N  N     . PHE A 1 437 ? -9.168  28.883  4.776   1 42.42 ? 437 PHE A N     1 
ATOM   3564  C  CA    . PHE A 1 437 ? -10.009 28.094  5.659   1 42.5  ? 437 PHE A CA    1 
ATOM   3565  C  C     . PHE A 1 437 ? -10.987 27.265  4.828   1 42.23 ? 437 PHE A C     1 
ATOM   3566  O  O     . PHE A 1 437 ? -11.69  27.812  3.983   1 42.35 ? 437 PHE A O     1 
ATOM   3567  C  CB    . PHE A 1 437 ? -10.757 28.952  6.706   1 42.52 ? 437 PHE A CB    1 
ATOM   3568  C  CG    . PHE A 1 437 ? -11.861 28.186  7.408   1 43.21 ? 437 PHE A CG    1 
ATOM   3569  C  CD1   . PHE A 1 437 ? -11.563 27.21   8.342   1 43.96 ? 437 PHE A CD1   1 
ATOM   3570  C  CD2   . PHE A 1 437 ? -13.184 28.362  7.047   1 44.13 ? 437 PHE A CD2   1 
ATOM   3571  C  CE1   . PHE A 1 437 ? -12.57  26.456  8.925   1 44.74 ? 437 PHE A CE1   1 
ATOM   3572  C  CE2   . PHE A 1 437 ? -14.188 27.607  7.638   1 44.91 ? 437 PHE A CE2   1 
ATOM   3573  C  CZ    . PHE A 1 437 ? -13.874 26.661  8.574   1 44.63 ? 437 PHE A CZ    1 
ATOM   3574  N  N     . ARG A 1 438 ? -11.064 25.959  5.106   1 41.68 ? 438 ARG A N     1 
ATOM   3575  C  CA    . ARG A 1 438 ? -11.992 25.07   4.423   1 41.67 ? 438 ARG A CA    1 
ATOM   3576  C  C     . ARG A 1 438 ? -12.676 24.161  5.433   1 41.87 ? 438 ARG A C     1 
ATOM   3577  O  O     . ARG A 1 438 ? -12.043 23.692  6.376   1 42.22 ? 438 ARG A O     1 
ATOM   3578  C  CB    . ARG A 1 438 ? -11.25  24.191  3.401   1 42.57 ? 438 ARG A CB    1 
ATOM   3579  C  CG    . ARG A 1 438 ? -10.517 24.97   2.317   1 44.8  ? 438 ARG A CG    1 
ATOM   3580  C  CD    . ARG A 1 438 ? -11.428 25.338  1.169   1 47.1  ? 438 ARG A CD    1 
ATOM   3581  N  NE    . ARG A 1 438 ? -11.459 26.765  0.842   1 49.16 ? 438 ARG A NE    1 
ATOM   3582  C  CZ    . ARG A 1 438 ? -10.597 27.398  0.052   1 50.48 ? 438 ARG A CZ    1 
ATOM   3583  N  NH1   . ARG A 1 438 ? -10.701 28.706  -0.136  1 49.86 ? 438 ARG A NH1   1 
ATOM   3584  N  NH2   . ARG A 1 438 ? -9.57   26.758  -0.463  1 50.02 ? 438 ARG A NH2   1 
ATOM   3585  N  N     . LEU A 1 439 ? -13.961 23.888  5.226   1 41.37 ? 439 LEU A N     1 
ATOM   3586  C  CA    . LEU A 1 439 ? -14.702 22.943  6.052   1 41.09 ? 439 LEU A CA    1 
ATOM   3587  C  C     . LEU A 1 439 ? -15.341 21.964  5.082   1 40.8  ? 439 LEU A C     1 
ATOM   3588  O  O     . LEU A 1 439 ? -16.222 22.336  4.31    1 40.79 ? 439 LEU A O     1 
ATOM   3589  C  CB    . LEU A 1 439 ? -15.762 23.628  6.929   1 41.08 ? 439 LEU A CB    1 
ATOM   3590  C  CG    . LEU A 1 439 ? -16.794 22.715  7.606   1 42.17 ? 439 LEU A CG    1 
ATOM   3591  C  CD1   . LEU A 1 439 ? -16.139 21.646  8.448   1 42.68 ? 439 LEU A CD1   1 
ATOM   3592  C  CD2   . LEU A 1 439 ? -17.705 23.511  8.473   1 42.69 ? 439 LEU A CD2   1 
ATOM   3593  N  N     . ILE A 1 440 ? -14.87  20.728  5.092   1 40.49 ? 440 ILE A N     1 
ATOM   3594  C  CA    . ILE A 1 440 ? -15.36  19.704  4.19    1 40.71 ? 440 ILE A CA    1 
ATOM   3595  C  C     . ILE A 1 440 ? -16.209 18.682  4.926   1 40.67 ? 440 ILE A C     1 
ATOM   3596  O  O     . ILE A 1 440 ? -15.702 17.997  5.807   1 40.75 ? 440 ILE A O     1 
ATOM   3597  C  CB    . ILE A 1 440 ? -14.166 19.02   3.482   1 41.43 ? 440 ILE A CB    1 
ATOM   3598  C  CG1   . ILE A 1 440 ? -13.242 20.058  2.791   1 42.51 ? 440 ILE A CG1   1 
ATOM   3599  C  CG2   . ILE A 1 440 ? -14.66  17.958  2.507   1 42.02 ? 440 ILE A CG2   1 
ATOM   3600  C  CD1   . ILE A 1 440 ? -12.024 19.479  2.041   1 43.7  ? 440 ILE A CD1   1 
ATOM   3601  N  N     . ILE A 1 441 ? -17.493 18.568  4.571   1 40.51 ? 441 ILE A N     1 
ATOM   3602  C  CA    . ILE A 1 441 ? -18.371 17.567  5.171   1 40.98 ? 441 ILE A CA    1 
ATOM   3603  C  C     . ILE A 1 441 ? -18.131 16.272  4.391   1 41.35 ? 441 ILE A C     1 
ATOM   3604  O  O     . ILE A 1 441 ? -18.695 16.053  3.319   1 41.45 ? 441 ILE A O     1 
ATOM   3605  C  CB    . ILE A 1 441 ? -19.842 18.025  5.131   1 41.51 ? 441 ILE A CB    1 
ATOM   3606  C  CG1   . ILE A 1 441 ? -20     19.412  5.774   1 42.55 ? 441 ILE A CG1   1 
ATOM   3607  C  CG2   . ILE A 1 441 ? -20.761 16.996  5.786   1 41.91 ? 441 ILE A CG2   1 
ATOM   3608  C  CD1   . ILE A 1 441 ? -19.636 19.472  7.242   1 43.92 ? 441 ILE A CD1   1 
ATOM   3609  N  N     . ASN A 1 442 ? -17.236 15.448  4.912   1 41.35 ? 442 ASN A N     1 
ATOM   3610  C  CA    . ASN A 1 442 ? -16.778 14.229  4.272   1 41.83 ? 442 ASN A CA    1 
ATOM   3611  C  C     . ASN A 1 442 ? -17.507 12.947  4.723   1 42.31 ? 442 ASN A C     1 
ATOM   3612  O  O     . ASN A 1 442 ? -17.087 11.853  4.349   1 42.59 ? 442 ASN A O     1 
ATOM   3613  C  CB    . ASN A 1 442 ? -15.277 14.116  4.528   1 42.77 ? 442 ASN A CB    1 
ATOM   3614  C  CG    . ASN A 1 442 ? -14.537 13.227  3.583   1 45.62 ? 442 ASN A CG    1 
ATOM   3615  O  OD1   . ASN A 1 442 ? -14.587 13.389  2.365   1 46.92 ? 442 ASN A OD1   1 
ATOM   3616  N  ND2   . ASN A 1 442 ? -13.832 12.268  4.134   1 46.02 ? 442 ASN A ND2   1 
ATOM   3617  N  N     . LYS A 1 443 ? -18.594 13.076  5.506   1 42.2  ? 443 LYS A N     1 
ATOM   3618  C  CA    . LYS A 1 443 ? -19.359 11.94   6.039   1 42.53 ? 443 LYS A CA    1 
ATOM   3619  C  C     . LYS A 1 443 ? -19.74  10.861  5.013   1 42.89 ? 443 LYS A C     1 
ATOM   3620  O  O     . LYS A 1 443 ? -19.402 9.695   5.217   1 43.05 ? 443 LYS A O     1 
ATOM   3621  C  CB    . LYS A 1 443 ? -20.613 12.421  6.783   1 44.25 ? 443 LYS A CB    1 
ATOM   3622  C  CG    . LYS A 1 443 ? -20.357 12.761  8.233   1 48.09 ? 443 LYS A CG    1 
ATOM   3623  C  CD    . LYS A 1 443 ? -21.652 12.903  8.993   1 52.47 ? 443 LYS A CD    1 
ATOM   3624  C  CE    . LYS A 1 443 ? -21.427 12.899  10.485  1 56.32 ? 443 LYS A CE    1 
ATOM   3625  N  NZ    . LYS A 1 443 ? -21.018 11.56   10.994  1 58.53 ? 443 LYS A NZ    1 
ATOM   3626  N  N     . ASN A 1 444 ? -20.436 11.231  3.925   1 43.02 ? 444 ASN A N     1 
ATOM   3627  C  CA    . ASN A 1 444 ? -20.846 10.252  2.92    1 43.69 ? 444 ASN A CA    1 
ATOM   3628  C  C     . ASN A 1 444 ? -19.666 9.675   2.144   1 44.02 ? 444 ASN A C     1 
ATOM   3629  O  O     . ASN A 1 444 ? -19.694 8.502   1.769   1 44.16 ? 444 ASN A O     1 
ATOM   3630  C  CB    . ASN A 1 444 ? -21.9   10.816  1.974   1 45    ? 444 ASN A CB    1 
ATOM   3631  C  CG    . ASN A 1 444 ? -22.687 9.752   1.232   1 48.41 ? 444 ASN A CG    1 
ATOM   3632  O  OD1   . ASN A 1 444 ? -23.049 9.917   0.062   1 49.66 ? 444 ASN A OD1   1 
ATOM   3633  N  ND2   . ASN A 1 444 ? -22.975 8.63    1.887   1 49.15 ? 444 ASN A ND2   1 
ATOM   3634  N  N     . ASN A 1 445 ? -18.625 10.484  1.93    1 44.02 ? 445 ASN A N     1 
ATOM   3635  C  CA    . ASN A 1 445 ? -17.437 10.035  1.223   1 44.65 ? 445 ASN A CA    1 
ATOM   3636  C  C     . ASN A 1 445 ? -16.69  8.985   2.041   1 45.11 ? 445 ASN A C     1 
ATOM   3637  O  O     . ASN A 1 445 ? -16.278 7.961   1.499   1 45.24 ? 445 ASN A O     1 
ATOM   3638  C  CB    . ASN A 1 445 ? -16.537 11.213  0.916   1 45.68 ? 445 ASN A CB    1 
ATOM   3639  C  CG    . ASN A 1 445 ? -15.442 10.873  -0.051  1 48.74 ? 445 ASN A CG    1 
ATOM   3640  O  OD1   . ASN A 1 445 ? -15.569 9.964   -0.874  1 49.83 ? 445 ASN A OD1   1 
ATOM   3641  N  ND2   . ASN A 1 445 ? -14.348 11.604  0.016   1 49.44 ? 445 ASN A ND2   1 
ATOM   3642  N  N     . LYS A 1 446 ? -16.559 9.215   3.353   1 45.23 ? 446 LYS A N     1 
ATOM   3643  C  CA    . LYS A 1 446 ? -15.896 8.286   4.259   1 45.96 ? 446 LYS A CA    1 
ATOM   3644  C  C     . LYS A 1 446 ? -16.635 6.95    4.273   1 46.99 ? 446 LYS A C     1 
ATOM   3645  O  O     . LYS A 1 446 ? -15.997 5.903   4.179   1 47.22 ? 446 LYS A O     1 
ATOM   3646  C  CB    . LYS A 1 446 ? -15.814 8.878   5.678   1 47.33 ? 446 LYS A CB    1 
ATOM   3647  C  CG    . LYS A 1 446 ? -15.41  7.871   6.751   1 50.63 ? 446 LYS A CG    1 
ATOM   3648  C  CD    . LYS A 1 446 ? -15.318 8.484   8.129   1 54.27 ? 446 LYS A CD    1 
ATOM   3649  C  CE    . LYS A 1 446 ? -15.042 7.426   9.166   1 56.95 ? 446 LYS A CE    1 
ATOM   3650  N  NZ    . LYS A 1 446 ? -14.803 8.014   10.505  1 58.34 ? 446 LYS A NZ    1 
ATOM   3651  N  N     . GLU A 1 447 ? -17.976 6.988   4.345   1 47.44 ? 447 GLU A N     1 
ATOM   3652  C  CA    . GLU A 1 447 ? -18.796 5.777   4.35    1 48.4  ? 447 GLU A CA    1 
ATOM   3653  C  C     . GLU A 1 447 ? -18.55  4.925   3.106   1 48.99 ? 447 GLU A C     1 
ATOM   3654  O  O     . GLU A 1 447 ? -18.398 3.708   3.211   1 49.22 ? 447 GLU A O     1 
ATOM   3655  C  CB    . GLU A 1 447 ? -20.284 6.129   4.459   1 50.97 ? 447 GLU A CB    1 
ATOM   3656  C  CG    . GLU A 1 447 ? -20.714 6.541   5.856   1 56.75 ? 447 GLU A CG    1 
ATOM   3657  C  CD    . GLU A 1 447 ? -22.165 6.969   5.983   1 63.86 ? 447 GLU A CD    1 
ATOM   3658  O  OE1   . GLU A 1 447 ? -22.878 6.986   4.954   1 65.42 ? 447 GLU A OE1   1 
ATOM   3659  O  OE2   . GLU A 1 447 ? -22.589 7.292   7.117   1 66.12 ? 447 GLU A OE2   1 
ATOM   3660  N  N     . SER A 1 448 ? -18.476 5.567   1.937   1 48.98 ? 448 SER A N     1 
ATOM   3661  C  CA    . SER A 1 448 ? -18.24  4.875   0.681   1 49.42 ? 448 SER A CA    1 
ATOM   3662  C  C     . SER A 1 448 ? -16.853 4.263   0.635   1 49.93 ? 448 SER A C     1 
ATOM   3663  O  O     . SER A 1 448 ? -16.703 3.143   0.16    1 50.15 ? 448 SER A O     1 
ATOM   3664  C  CB    . SER A 1 448 ? -18.436 5.827   -0.49   1 50.54 ? 448 SER A CB    1 
ATOM   3665  O  OG    . SER A 1 448 ? -19.758 6.338   -0.483  1 52.79 ? 448 SER A OG    1 
ATOM   3666  N  N     . ILE A 1 449 ? -15.846 4.974   1.146   1 50.12 ? 449 ILE A N     1 
ATOM   3667  C  CA    . ILE A 1 449 ? -14.482 4.46    1.155   1 51    ? 449 ILE A CA    1 
ATOM   3668  C  C     . ILE A 1 449 ? -14.339 3.241   2.056   1 52.08 ? 449 ILE A C     1 
ATOM   3669  O  O     . ILE A 1 449 ? -13.664 2.285   1.679   1 52.33 ? 449 ILE A O     1 
ATOM   3670  C  CB    . ILE A 1 449 ? -13.466 5.568   1.483   1 51.48 ? 449 ILE A CB    1 
ATOM   3671  C  CG1   . ILE A 1 449 ? -13.472 6.633   0.384   1 52.34 ? 449 ILE A CG1   1 
ATOM   3672  C  CG2   . ILE A 1 449 ? -12.064 4.994   1.663   1 51.97 ? 449 ILE A CG2   1 
ATOM   3673  C  CD1   . ILE A 1 449 ? -12.835 7.889   0.791   1 53.5  ? 449 ILE A CD1   1 
ATOM   3674  N  N     . LEU A 1 450 ? -15.019 3.235   3.214   1 52.62 ? 450 LEU A N     1 
ATOM   3675  C  CA    . LEU A 1 450 ? -14.95  2.09    4.127   1 53.6  ? 450 LEU A CA    1 
ATOM   3676  C  C     . LEU A 1 450 ? -15.57  0.804   3.562   1 54.74 ? 450 LEU A C     1 
ATOM   3677  O  O     . LEU A 1 450 ? -15.311 -0.273  4.089   1 54.9  ? 450 LEU A O     1 
ATOM   3678  C  CB    . LEU A 1 450 ? -15.542 2.417   5.503   1 53.71 ? 450 LEU A CB    1 
ATOM   3679  C  CG    . LEU A 1 450 ? -14.869 3.552   6.276   1 55.12 ? 450 LEU A CG    1 
ATOM   3680  C  CD1   . LEU A 1 450 ? -15.531 3.752   7.614   1 55.68 ? 450 LEU A CD1   1 
ATOM   3681  C  CD2   . LEU A 1 450 ? -13.403 3.282   6.495   1 55.75 ? 450 LEU A CD2   1 
ATOM   3682  N  N     . ARG A 1 451 ? -16.36  0.902   2.491   1 55.35 ? 451 ARG A N     1 
ATOM   3683  C  CA    . ARG A 1 451 ? -16.949 -0.282  1.862   1 56.49 ? 451 ARG A CA    1 
ATOM   3684  C  C     . ARG A 1 451 ? -16.323 -0.581  0.484   1 57.46 ? 451 ARG A C     1 
ATOM   3685  O  O     . ARG A 1 451 ? -16.914 -1.312  -0.306  1 57.61 ? 451 ARG A O     1 
ATOM   3686  C  CB    . ARG A 1 451 ? -18.472 -0.134  1.735   1 58.04 ? 451 ARG A CB    1 
ATOM   3687  C  CG    . ARG A 1 451 ? -19.14  0.424   2.984   1 61.64 ? 451 ARG A CG    1 
ATOM   3688  C  CD    . ARG A 1 451 ? -20.633 0.192   3.006   1 65.4  ? 451 ARG A CD    1 
ATOM   3689  N  NE    . ARG A 1 451 ? -21.353 1.449   2.811   1 68.82 ? 451 ARG A NE    1 
ATOM   3690  C  CZ    . ARG A 1 451 ? -21.816 1.878   1.64    1 71.37 ? 451 ARG A CZ    1 
ATOM   3691  N  NH1   . ARG A 1 451 ? -22.451 3.041   1.557   1 71.15 ? 451 ARG A NH1   1 
ATOM   3692  N  NH2   . ARG A 1 451 ? -21.666 1.137   0.546   1 71.33 ? 451 ARG A NH2   1 
ATOM   3693  N  N     . LYS A 1 452 ? -15.145 -0.016  0.189   1 58.04 ? 452 LYS A N     1 
ATOM   3694  C  CA    . LYS A 1 452 ? -14.497 -0.206  -1.102  1 59.15 ? 452 LYS A CA    1 
ATOM   3695  C  C     . LYS A 1 452 ? -13.547 -1.402  -1.114  1 59.98 ? 452 LYS A C     1 
ATOM   3696  O  O     . LYS A 1 452 ? -12.695 -1.522  -0.233  1 60.16 ? 452 LYS A O     1 
ATOM   3697  C  CB    . LYS A 1 452 ? -13.747 1.076   -1.512  1 61.1  ? 452 LYS A CB    1 
ATOM   3698  C  CG    . LYS A 1 452 ? -13.422 1.153   -3      1 65.21 ? 452 LYS A CG    1 
ATOM   3699  C  CD    . LYS A 1 452 ? -12.923 2.532   -3.417  1 69.19 ? 452 LYS A CD    1 
ATOM   3700  C  CE    . LYS A 1 452 ? -12.728 2.621   -4.911  1 72.48 ? 452 LYS A CE    1 
ATOM   3701  N  NZ    . LYS A 1 452 ? -12.198 3.947   -5.32   1 74.46 ? 452 LYS A NZ    1 
ATOM   3702  N  N     . THR A 1 453 ? -13.705 -2.295  -2.111  1 60.2  ? 453 THR A N     1 
ATOM   3703  C  CA    . THR A 1 453 ? -12.842 -3.464  -2.33   1 60.8  ? 453 THR A CA    1 
ATOM   3704  C  C     . THR A 1 453 ? -12.524 -3.57   -3.818  1 61.07 ? 453 THR A C     1 
ATOM   3705  O  O     . THR A 1 453 ? -13.423 -3.39   -4.64   1 61.15 ? 453 THR A O     1 
ATOM   3706  C  CB    . THR A 1 453 ? -13.497 -4.779  -1.863  1 62.07 ? 453 THR A CB    1 
ATOM   3707  O  OG1   . THR A 1 453 ? -14.673 -5.042  -2.63   1 62.93 ? 453 THR A OG1   1 
ATOM   3708  C  CG2   . THR A 1 453 ? -13.811 -4.796  -0.375  1 62.54 ? 453 THR A CG2   1 
ATOM   3709  N  N     . SER A 1 454 ? -11.268 -3.886  -4.17   1 61.09 ? 454 SER A N     1 
ATOM   3710  C  CA    . SER A 1 454 ? -10.898 -4.034  -5.579  1 61.63 ? 454 SER A CA    1 
ATOM   3711  C  C     . SER A 1 454 ? -11.455 -5.348  -6.175  1 61.84 ? 454 SER A C     1 
ATOM   3712  O  O     . SER A 1 454 ? -11.898 -6.224  -5.426  1 62.09 ? 454 SER A O     1 
ATOM   3713  C  CB    . SER A 1 454 ? -9.386  -3.92   -5.764  1 63.05 ? 454 SER A CB    1 
ATOM   3714  O  OG    . SER A 1 454 ? -8.683  -4.984  -5.144  1 65.34 ? 454 SER A OG    1 
ATOM   3715  N  N     . LYS A 1 455 ? -11.476 -5.461  -7.517  1 61.59 ? 455 LYS A N     1 
ATOM   3716  C  CA    . LYS A 1 455 ? -11.994 -6.626  -8.246  1 61.82 ? 455 LYS A CA    1 
ATOM   3717  C  C     . LYS A 1 455 ? -11.501 -7.968  -7.682  1 61.66 ? 455 LYS A C     1 
ATOM   3718  O  O     . LYS A 1 455 ? -10.299 -8.144  -7.504  1 62.06 ? 455 LYS A O     1 
ATOM   3719  C  CB    . LYS A 1 455 ? -11.631 -6.507  -9.74   1 63.73 ? 455 LYS A CB    1 
ATOM   3720  C  CG    . LYS A 1 455 ? -12.07  -7.691  -10.597 1 67.78 ? 455 LYS A CG    1 
ATOM   3721  C  CD    . LYS A 1 455 ? -11.566 -7.565  -12.033 1 71.98 ? 455 LYS A CD    1 
ATOM   3722  C  CE    . LYS A 1 455 ? -12.071 -8.682  -12.916 1 75.3  ? 455 LYS A CE    1 
ATOM   3723  N  NZ    . LYS A 1 455 ? -11.499 -8.612  -14.284 1 77.25 ? 455 LYS A NZ    1 
ATOM   3724  N  N     . GLN A 1 456 ? -12.424 -8.902  -7.396  1 60.82 ? 456 GLN A N     1 
ATOM   3725  C  CA    . GLN A 1 456 ? -12.057 -10.218 -6.874  1 60.49 ? 456 GLN A CA    1 
ATOM   3726  C  C     . GLN A 1 456 ? -11.439 -11.082 -7.971  1 59.62 ? 456 GLN A C     1 
ATOM   3727  O  O     . GLN A 1 456 ? -12.107 -11.392 -8.956  1 59.88 ? 456 GLN A O     1 
ATOM   3728  C  CB    . GLN A 1 456 ? -13.29  -10.931 -6.314  1 62.29 ? 456 GLN A CB    1 
ATOM   3729  C  CG    . GLN A 1 456 ? -14.008 -10.133 -5.25   1 66.29 ? 456 GLN A CG    1 
ATOM   3730  C  CD    . GLN A 1 456 ? -13.178 -10.005 -4.002  1 71.03 ? 456 GLN A CD    1 
ATOM   3731  O  OE1   . GLN A 1 456 ? -12.548 -10.966 -3.536  1 72.54 ? 456 GLN A OE1   1 
ATOM   3732  N  NE2   . GLN A 1 456 ? -13.17  -8.811  -3.43   1 71.57 ? 456 GLN A NE2   1 
ATOM   3733  N  N     . GLN A 1 457 ? -10.179 -11.487 -7.797  1 58.32 ? 457 GLN A N     1 
ATOM   3734  C  CA    . GLN A 1 457 ? -9.482  -12.323 -8.766  1 57.46 ? 457 GLN A CA    1 
ATOM   3735  C  C     . GLN A 1 457 ? -8.276  -13.005 -8.143  1 56.17 ? 457 GLN A C     1 
ATOM   3736  O  O     . GLN A 1 457 ? -7.628  -12.457 -7.252  1 56.25 ? 457 GLN A O     1 
ATOM   3737  C  CB    . GLN A 1 457 ? -9.07   -11.527 -10.014 1 59.02 ? 457 GLN A CB    1 
ATOM   3738  C  CG    . GLN A 1 457 ? -8.098  -10.39  -9.735  1 62.22 ? 457 GLN A CG    1 
ATOM   3739  C  CD    . GLN A 1 457 ? -7.703  -9.653  -10.989 1 66.29 ? 457 GLN A CD    1 
ATOM   3740  O  OE1   . GLN A 1 457 ? -7.712  -8.419  -11.036 1 67.54 ? 457 GLN A OE1   1 
ATOM   3741  N  NE2   . GLN A 1 457 ? -7.34   -10.388 -12.031 1 67.08 ? 457 GLN A NE2   1 
ATOM   3742  N  N     . ASN A 1 458 ? -7.987  -14.216 -8.605  1 54.93 ? 458 ASN A N     1 
ATOM   3743  C  CA    . ASN A 1 458 ? -6.863  -14.985 -8.1    1 54.14 ? 458 ASN A CA    1 
ATOM   3744  C  C     . ASN A 1 458 ? -5.549  -14.387 -8.578  1 52.8  ? 458 ASN A C     1 
ATOM   3745  O  O     . ASN A 1 458 ? -5.479  -13.822 -9.669  1 52.99 ? 458 ASN A O     1 
ATOM   3746  C  CB    . ASN A 1 458 ? -6.966  -16.444 -8.555  1 55.36 ? 458 ASN A CB    1 
ATOM   3747  C  CG    . ASN A 1 458 ? -8.265  -17.132 -8.203  1 58.71 ? 458 ASN A CG    1 
ATOM   3748  O  OD1   . ASN A 1 458 ? -8.744  -18.004 -8.933  1 60    ? 458 ASN A OD1   1 
ATOM   3749  N  ND2   . ASN A 1 458 ? -8.863  -16.775 -7.072  1 59.48 ? 458 ASN A ND2   1 
ATOM   3750  N  N     . ILE A 1 459 ? -4.507  -14.499 -7.756  1 51.28 ? 459 ILE A N     1 
ATOM   3751  C  CA    . ILE A 1 459 ? -3.193  -13.981 -8.111  1 50.31 ? 459 ILE A CA    1 
ATOM   3752  C  C     . ILE A 1 459 ? -2.115  -15.047 -7.937  1 49.01 ? 459 ILE A C     1 
ATOM   3753  O  O     . ILE A 1 459 ? -2.1    -15.78  -6.952  1 49.1  ? 459 ILE A O     1 
ATOM   3754  C  CB    . ILE A 1 459 ? -2.865  -12.681 -7.326  1 50.78 ? 459 ILE A CB    1 
ATOM   3755  C  CG1   . ILE A 1 459 ? -3.785  -11.532 -7.758  1 51.72 ? 459 ILE A CG1   1 
ATOM   3756  C  CG2   . ILE A 1 459 ? -1.383  -12.281 -7.456  1 51.21 ? 459 ILE A CG2   1 
ATOM   3757  C  CD1   . ILE A 1 459 ? -3.726  -10.351 -6.881  1 52.97 ? 459 ILE A CD1   1 
ATOM   3758  N  N     . LEU A 1 460 ? -1.229  -15.142 -8.915  1 47.74 ? 460 LEU A N     1 
ATOM   3759  C  CA    . LEU A 1 460 ? -0.092  -16.039 -8.885  1 47.06 ? 460 LEU A CA    1 
ATOM   3760  C  C     . LEU A 1 460 ? 1.02    -15.239 -9.528  1 46.13 ? 460 LEU A C     1 
ATOM   3761  O  O     . LEU A 1 460 ? 1.001   -15.023 -10.739 1 46.24 ? 460 LEU A O     1 
ATOM   3762  C  CB    . LEU A 1 460 ? -0.37   -17.311 -9.692  1 47.28 ? 460 LEU A CB    1 
ATOM   3763  C  CG    . LEU A 1 460 ? 0.757   -18.327 -9.699  1 48.64 ? 460 LEU A CG    1 
ATOM   3764  C  CD1   . LEU A 1 460 ? 1.005   -18.878 -8.305  1 49.22 ? 460 LEU A CD1   1 
ATOM   3765  C  CD2   . LEU A 1 460 ? 0.454   -19.45  -10.652 1 49.22 ? 460 LEU A CD2   1 
ATOM   3766  N  N     . VAL A 1 461 ? 1.933   -14.714 -8.713  1 45.05 ? 461 VAL A N     1 
ATOM   3767  C  CA    . VAL A 1 461 ? 3.012   -13.878 -9.217  1 44.42 ? 461 VAL A CA    1 
ATOM   3768  C  C     . VAL A 1 461 ? 4.034   -14.655 -10.037 1 43.62 ? 461 VAL A C     1 
ATOM   3769  O  O     . VAL A 1 461 ? 4.615   -15.611 -9.536  1 43.77 ? 461 VAL A O     1 
ATOM   3770  C  CB    . VAL A 1 461 ? 3.683   -13.089 -8.078  1 44.94 ? 461 VAL A CB    1 
ATOM   3771  C  CG1   . VAL A 1 461 ? 4.767   -12.171 -8.627  1 45.55 ? 461 VAL A CG1   1 
ATOM   3772  C  CG2   . VAL A 1 461 ? 2.649   -12.297 -7.285  1 45.19 ? 461 VAL A CG2   1 
ATOM   3773  N  N     . ASP A 1 462 ? 4.253   -14.249 -11.297 1 42.61 ? 462 ASP A N     1 
ATOM   3774  C  CA    . ASP A 1 462 ? 5.238   -14.893 -12.162 1 42.28 ? 462 ASP A CA    1 
ATOM   3775  C  C     . ASP A 1 462 ? 6.626   -14.599 -11.602 1 41.63 ? 462 ASP A C     1 
ATOM   3776  O  O     . ASP A 1 462 ? 6.95    -13.446 -11.321 1 41.87 ? 462 ASP A O     1 
ATOM   3777  C  CB    . ASP A 1 462 ? 5.112   -14.361 -13.599 1 44.01 ? 462 ASP A CB    1 
ATOM   3778  C  CG    . ASP A 1 462 ? 6.034   -15.017 -14.609 1 48.04 ? 462 ASP A CG    1 
ATOM   3779  O  OD1   . ASP A 1 462 ? 6.028   -16.269 -14.696 1 48.55 ? 462 ASP A OD1   1 
ATOM   3780  O  OD2   . ASP A 1 462 ? 6.749   -14.281 -15.322 1 49.85 ? 462 ASP A OD2   1 
ATOM   3781  N  N     . PRO A 1 463 ? 7.458   -15.633 -11.416 1 40.68 ? 463 PRO A N     1 
ATOM   3782  C  CA    . PRO A 1 463 ? 8.781   -15.416 -10.81  1 40.32 ? 463 PRO A CA    1 
ATOM   3783  C  C     . PRO A 1 463 ? 9.783   -14.589 -11.619 1 40.31 ? 463 PRO A C     1 
ATOM   3784  O  O     . PRO A 1 463 ? 10.879  -14.328 -11.127 1 40.2  ? 463 PRO A O     1 
ATOM   3785  C  CB    . PRO A 1 463 ? 9.294   -16.839 -10.57  1 40.86 ? 463 PRO A CB    1 
ATOM   3786  C  CG    . PRO A 1 463 ? 8.093   -17.72  -10.659 1 41.39 ? 463 PRO A CG    1 
ATOM   3787  C  CD    . PRO A 1 463 ? 7.199   -17.063 -11.648 1 39.93 ? 463 PRO A CD    1 
ATOM   3788  N  N     . THR A 1 464 ? 9.427   -14.175 -12.839 1 40.3  ? 464 THR A N     1 
ATOM   3789  C  CA    . THR A 1 464 ? 10.319  -13.373 -13.663 1 40.77 ? 464 THR A CA    1 
ATOM   3790  C  C     . THR A 1 464 ? 9.795   -11.952 -13.749 1 41.1  ? 464 THR A C     1 
ATOM   3791  O  O     . THR A 1 464 ? 8.673   -11.723 -14.198 1 41.06 ? 464 THR A O     1 
ATOM   3792  C  CB    . THR A 1 464 ? 10.55   -14.047 -15.013 1 42.07 ? 464 THR A CB    1 
ATOM   3793  O  OG1   . THR A 1 464 ? 11.325  -15.226 -14.785 1 43.19 ? 464 THR A OG1   1 
ATOM   3794  C  CG2   . THR A 1 464 ? 11.269  -13.144 -16.002 1 42.37 ? 464 THR A CG2   1 
ATOM   3795  N  N     . PRO A 1 465 ? 10.584  -10.981 -13.267 1 41.26 ? 465 PRO A N     1 
ATOM   3796  C  CA    . PRO A 1 465 ? 10.126  -9.588  -13.3   1 41.73 ? 465 PRO A CA    1 
ATOM   3797  C  C     . PRO A 1 465 ? 10.266  -8.916  -14.674 1 42.45 ? 465 PRO A C     1 
ATOM   3798  O  O     . PRO A 1 465 ? 10.821  -9.503  -15.601 1 42.61 ? 465 PRO A O     1 
ATOM   3799  C  CB    . PRO A 1 465 ? 11.022  -8.919  -12.253 1 42.19 ? 465 PRO A CB    1 
ATOM   3800  C  CG    . PRO A 1 465 ? 12.304  -9.647  -12.379 1 42.4  ? 465 PRO A CG    1 
ATOM   3801  C  CD    . PRO A 1 465 ? 11.933  -11.088 -12.674 1 40.74 ? 465 PRO A CD    1 
ATOM   3802  N  N     . ASN A 1 466 ? 9.757   -7.675  -14.786 1 42.71 ? 466 ASN A N     1 
ATOM   3803  C  CA    . ASN A 1 466 ? 9.798   -6.823  -15.969 1 43.56 ? 466 ASN A CA    1 
ATOM   3804  C  C     . ASN A 1 466 ? 11.258  -6.598  -16.355 1 43.65 ? 466 ASN A C     1 
ATOM   3805  O  O     . ASN A 1 466 ? 11.621  -6.755  -17.518 1 43.68 ? 466 ASN A O     1 
ATOM   3806  C  CB    . ASN A 1 466 ? 9.126   -5.483  -15.655 1 45.51 ? 466 ASN A CB    1 
ATOM   3807  C  CG    . ASN A 1 466 ? 8.195   -4.99   -16.726 1 49.94 ? 466 ASN A CG    1 
ATOM   3808  O  OD1   . ASN A 1 466 ? 6.972   -5.058  -16.58  1 51.67 ? 466 ASN A OD1   1 
ATOM   3809  N  ND2   . ASN A 1 466 ? 8.739   -4.455  -17.814 1 50.71 ? 466 ASN A ND2   1 
ATOM   3810  N  N     . HIS A 1 467 ? 12.096  -6.265  -15.365 1 43.6  ? 467 HIS A N     1 
ATOM   3811  C  CA    . HIS A 1 467 ? 13.525  -6.063  -15.549 1 44.09 ? 467 HIS A CA    1 
ATOM   3812  C  C     . HIS A 1 467 ? 14.278  -6.223  -14.222 1 43.65 ? 467 HIS A C     1 
ATOM   3813  O  O     . HIS A 1 467 ? 13.678  -6.172  -13.15  1 43.54 ? 467 HIS A O     1 
ATOM   3814  C  CB    . HIS A 1 467 ? 13.829  -4.724  -16.244 1 45.54 ? 467 HIS A CB    1 
ATOM   3815  C  CG    . HIS A 1 467 ? 13.618  -3.518  -15.392 1 48.58 ? 467 HIS A CG    1 
ATOM   3816  N  ND1   . HIS A 1 467 ? 12.351  -3.127  -14.991 1 50.73 ? 467 HIS A ND1   1 
ATOM   3817  C  CD2   . HIS A 1 467 ? 14.523  -2.622  -14.935 1 50.05 ? 467 HIS A CD2   1 
ATOM   3818  C  CE1   . HIS A 1 467 ? 12.529  -2.026  -14.278 1 51.51 ? 467 HIS A CE1   1 
ATOM   3819  N  NE2   . HIS A 1 467 ? 13.818  -1.674  -14.231 1 51.45 ? 467 HIS A NE2   1 
ATOM   3820  N  N     . TYR A 1 468 ? 15.586  -6.467  -14.301 1 43.24 ? 468 TYR A N     1 
ATOM   3821  C  CA    . TYR A 1 468 ? 16.415  -6.688  -13.125 1 43.2  ? 468 TYR A CA    1 
ATOM   3822  C  C     . TYR A 1 468 ? 17.055  -5.381  -12.678 1 42.89 ? 468 TYR A C     1 
ATOM   3823  O  O     . TYR A 1 468 ? 17.713  -4.72   -13.48  1 43.11 ? 468 TYR A O     1 
ATOM   3824  C  CB    . TYR A 1 468 ? 17.447  -7.796  -13.399 1 43.28 ? 468 TYR A CB    1 
ATOM   3825  C  CG    . TYR A 1 468 ? 16.772  -9.082  -13.822 1 44.15 ? 468 TYR A CG    1 
ATOM   3826  C  CD1   . TYR A 1 468 ? 16.243  -9.951  -12.882 1 45.05 ? 468 TYR A CD1   1 
ATOM   3827  C  CD2   . TYR A 1 468 ? 16.557  -9.371  -15.163 1 45.12 ? 468 TYR A CD2   1 
ATOM   3828  C  CE1   . TYR A 1 468 ? 15.568  -11.102 -13.263 1 46.04 ? 468 TYR A CE1   1 
ATOM   3829  C  CE2   . TYR A 1 468 ? 15.869  -10.512 -15.556 1 46.08 ? 468 TYR A CE2   1 
ATOM   3830  C  CZ    . TYR A 1 468 ? 15.381  -11.381 -14.603 1 47.1  ? 468 TYR A CZ    1 
ATOM   3831  O  OH    . TYR A 1 468 ? 14.711  -12.516 -14.993 1 48.87 ? 468 TYR A OH    1 
ATOM   3832  N  N     . GLN A 1 469 ? 16.822  -4.979  -11.415 1 42.21 ? 469 GLN A N     1 
ATOM   3833  C  CA    . GLN A 1 469 ? 17.316  -3.705  -10.882 1 42.12 ? 469 GLN A CA    1 
ATOM   3834  C  C     . GLN A 1 469 ? 18.332  -3.897  -9.714  1 41.66 ? 469 GLN A C     1 
ATOM   3835  O  O     . GLN A 1 469 ? 18.851  -4.999  -9.522  1 41.72 ? 469 GLN A O     1 
ATOM   3836  C  CB    . GLN A 1 469 ? 16.116  -2.827  -10.424 1 43.76 ? 469 GLN A CB    1 
ATOM   3837  C  CG    . GLN A 1 469 ? 14.907  -2.823  -11.332 1 47.17 ? 469 GLN A CG    1 
ATOM   3838  C  CD    . GLN A 1 469 ? 13.631  -3.137  -10.589 1 51.64 ? 469 GLN A CD    1 
ATOM   3839  O  OE1   . GLN A 1 469 ? 12.969  -4.152  -10.839 1 53.15 ? 469 GLN A OE1   1 
ATOM   3840  N  NE2   . GLN A 1 469 ? 13.252  -2.27   -9.664  1 52.14 ? 469 GLN A NE2   1 
ATOM   3841  N  N     . GLU A 1 470 ? 18.591  -2.82   -8.929  1 40.99 ? 470 GLU A N     1 
ATOM   3842  C  CA    . GLU A 1 470 ? 19.461  -2.787  -7.754  1 40.61 ? 470 GLU A CA    1 
ATOM   3843  C  C     . GLU A 1 470 ? 19.065  -3.839  -6.71   1 39.58 ? 470 GLU A C     1 
ATOM   3844  O  O     . GLU A 1 470 ? 19.948  -4.406  -6.065  1 39.67 ? 470 GLU A O     1 
ATOM   3845  C  CB    . GLU A 1 470 ? 19.439  -1.385  -7.128  1 42.89 ? 470 GLU A CB    1 
ATOM   3846  C  CG    . GLU A 1 470 ? 20.456  -1.18   -6.023  1 47.99 ? 470 GLU A CG    1 
ATOM   3847  C  CD    . GLU A 1 470 ? 20.463  0.228   -5.466  1 55.07 ? 470 GLU A CD    1 
ATOM   3848  O  OE1   . GLU A 1 470 ? 20.559  0.379   -4.227  1 56.39 ? 470 GLU A OE1   1 
ATOM   3849  O  OE2   . GLU A 1 470 ? 20.384  1.182   -6.274  1 57.41 ? 470 GLU A OE2   1 
ATOM   3850  N  N     . ASN A 1 471 ? 17.757  -4.132  -6.568  1 38.47 ? 471 ASN A N     1 
ATOM   3851  C  CA    . ASN A 1 471 ? 17.325  -5.157  -5.619  1 37.99 ? 471 ASN A CA    1 
ATOM   3852  C  C     . ASN A 1 471 ? 17.826  -6.542  -6.043  1 37.63 ? 471 ASN A C     1 
ATOM   3853  O  O     . ASN A 1 471 ? 18.215  -7.334  -5.184  1 38.05 ? 471 ASN A O     1 
ATOM   3854  C  CB    . ASN A 1 471 ? 15.815  -5.149  -5.405  1 38.37 ? 471 ASN A CB    1 
ATOM   3855  C  CG    . ASN A 1 471 ? 15.439  -5.414  -3.967  1 40.33 ? 471 ASN A CG    1 
ATOM   3856  O  OD1   . ASN A 1 471 ? 14.631  -4.7    -3.37   1 41.27 ? 471 ASN A OD1   1 
ATOM   3857  N  ND2   . ASN A 1 471 ? 16.032  -6.439  -3.371  1 40.61 ? 471 ASN A ND2   1 
ATOM   3858  N  N     . ASP A 1 472 ? 17.866  -6.814  -7.356  1 36.62 ? 472 ASP A N     1 
ATOM   3859  C  CA    . ASP A 1 472 ? 18.372  -8.083  -7.857  1 36.29 ? 472 ASP A CA    1 
ATOM   3860  C  C     . ASP A 1 472 ? 19.881  -8.18   -7.72   1 35.64 ? 472 ASP A C     1 
ATOM   3861  O  O     . ASP A 1 472 ? 20.388  -9.253  -7.41   1 35.44 ? 472 ASP A O     1 
ATOM   3862  C  CB    . ASP A 1 472 ? 17.909  -8.324  -9.283  1 38.26 ? 472 ASP A CB    1 
ATOM   3863  C  CG    . ASP A 1 472 ? 16.408  -8.375  -9.338  1 43.33 ? 472 ASP A CG    1 
ATOM   3864  O  OD1   . ASP A 1 472 ? 15.822  -9.267  -8.69   1 43.97 ? 472 ASP A OD1   1 
ATOM   3865  O  OD2   . ASP A 1 472 ? 15.815  -7.506  -9.992  1 46.16 ? 472 ASP A OD2   1 
ATOM   3866  N  N     . VAL A 1 473 ? 20.602  -7.051  -7.861  1 35.31 ? 473 VAL A N     1 
ATOM   3867  C  CA    . VAL A 1 473 ? 22.056  -7.014  -7.647  1 35.55 ? 473 VAL A CA    1 
ATOM   3868  C  C     . VAL A 1 473 ? 22.339  -7.389  -6.187  1 35.68 ? 473 VAL A C     1 
ATOM   3869  O  O     . VAL A 1 473 ? 23.178  -8.245  -5.924  1 35.97 ? 473 VAL A O     1 
ATOM   3870  C  CB    . VAL A 1 473 ? 22.666  -5.629  -7.986  1 36.29 ? 473 VAL A CB    1 
ATOM   3871  C  CG1   . VAL A 1 473 ? 24.151  -5.584  -7.64   1 36.87 ? 473 VAL A CG1   1 
ATOM   3872  C  CG2   . VAL A 1 473 ? 22.442  -5.274  -9.449  1 36.72 ? 473 VAL A CG2   1 
ATOM   3873  N  N     . ASP A 1 474 ? 21.56   -6.808  -5.255  1 35.27 ? 474 ASP A N     1 
ATOM   3874  C  CA    . ASP A 1 474 ? 21.649  -7.065  -3.823  1 35.34 ? 474 ASP A CA    1 
ATOM   3875  C  C     . ASP A 1 474 ? 21.342  -8.524  -3.469  1 35.42 ? 474 ASP A C     1 
ATOM   3876  O  O     . ASP A 1 474 ? 22.042  -9.095  -2.641  1 35.54 ? 474 ASP A O     1 
ATOM   3877  C  CB    . ASP A 1 474 ? 20.726  -6.113  -3.052  1 36.72 ? 474 ASP A CB    1 
ATOM   3878  C  CG    . ASP A 1 474 ? 21.355  -4.762  -2.787  1 40.44 ? 474 ASP A CG    1 
ATOM   3879  O  OD1   . ASP A 1 474 ? 22.42   -4.718  -2.143  1 40.79 ? 474 ASP A OD1   1 
ATOM   3880  O  OD2   . ASP A 1 474 ? 20.791  -3.75   -3.233  1 42.55 ? 474 ASP A OD2   1 
ATOM   3881  N  N     . THR A 1 475 ? 20.317  -9.129  -4.099  1 35.15 ? 475 THR A N     1 
ATOM   3882  C  CA    . THR A 1 475 ? 19.936  -10.529 -3.874  1 35.16 ? 475 THR A CA    1 
ATOM   3883  C  C     . THR A 1 475 ? 21.094  -11.456 -4.258  1 35.32 ? 475 THR A C     1 
ATOM   3884  O  O     . THR A 1 475 ? 21.448  -12.356 -3.499  1 35.2  ? 475 THR A O     1 
ATOM   3885  C  CB    . THR A 1 475 ? 18.66   -10.864 -4.671  1 36.07 ? 475 THR A CB    1 
ATOM   3886  O  OG1   . THR A 1 475 ? 17.544  -10.157 -4.13   1 36.81 ? 475 THR A OG1   1 
ATOM   3887  C  CG2   . THR A 1 475 ? 18.356  -12.343 -4.685  1 36.48 ? 475 THR A CG2   1 
ATOM   3888  N  N     . VAL A 1 476 ? 21.705  -11.204 -5.422  1 35.55 ? 476 VAL A N     1 
ATOM   3889  C  CA    . VAL A 1 476 ? 22.834  -11.984 -5.924  1 36.28 ? 476 VAL A CA    1 
ATOM   3890  C  C     . VAL A 1 476 ? 24.057  -11.813 -5.016  1 37.02 ? 476 VAL A C     1 
ATOM   3891  O  O     . VAL A 1 476 ? 24.656  -12.809 -4.619  1 37.32 ? 476 VAL A O     1 
ATOM   3892  C  CB    . VAL A 1 476 ? 23.137  -11.641 -7.406  1 36.94 ? 476 VAL A CB    1 
ATOM   3893  C  CG1   . VAL A 1 476 ? 24.478  -12.213 -7.854  1 37.41 ? 476 VAL A CG1   1 
ATOM   3894  C  CG2   . VAL A 1 476 ? 22.016  -12.13  -8.317  1 37.41 ? 476 VAL A CG2   1 
ATOM   3895  N  N     . ILE A 1 477 ? 24.395  -10.57  -4.647  1 37.24 ? 477 ILE A N     1 
ATOM   3896  C  CA    . ILE A 1 477 ? 25.533  -10.297 -3.766  1 38.12 ? 477 ILE A CA    1 
ATOM   3897  C  C     . ILE A 1 477 ? 25.343  -10.97  -2.4    1 38.86 ? 477 ILE A C     1 
ATOM   3898  O  O     . ILE A 1 477 ? 26.268  -11.596 -1.885  1 39.07 ? 477 ILE A O     1 
ATOM   3899  C  CB    . ILE A 1 477 ? 25.783  -8.771  -3.652  1 38.87 ? 477 ILE A CB    1 
ATOM   3900  C  CG1   . ILE A 1 477 ? 26.344  -8.192  -4.97   1 40.23 ? 477 ILE A CG1   1 
ATOM   3901  C  CG2   . ILE A 1 477 ? 26.692  -8.423  -2.481  1 39.34 ? 477 ILE A CG2   1 
ATOM   3902  C  CD1   . ILE A 1 477 ? 27.679  -8.774  -5.409  1 41.67 ? 477 ILE A CD1   1 
ATOM   3903  N  N     . TYR A 1 478 ? 24.135  -10.879 -1.843  1 39.07 ? 478 TYR A N     1 
ATOM   3904  C  CA    . TYR A 1 478 ? 23.809  -11.488 -0.56   1 39.9  ? 478 TYR A CA    1 
ATOM   3905  C  C     . TYR A 1 478 ? 23.95   -13.007 -0.629  1 40.84 ? 478 TYR A C     1 
ATOM   3906  O  O     . TYR A 1 478 ? 24.541  -13.601 0.262   1 41    ? 478 TYR A O     1 
ATOM   3907  C  CB    . TYR A 1 478 ? 22.38   -11.101 -0.13   1 39.89 ? 478 TYR A CB    1 
ATOM   3908  C  CG    . TYR A 1 478 ? 21.992  -11.61  1.24    1 40.64 ? 478 TYR A CG    1 
ATOM   3909  C  CD1   . TYR A 1 478 ? 22.442  -10.98  2.388   1 41.55 ? 478 TYR A CD1   1 
ATOM   3910  C  CD2   . TYR A 1 478 ? 21.146  -12.699 1.386   1 41.48 ? 478 TYR A CD2   1 
ATOM   3911  C  CE1   . TYR A 1 478 ? 22.09   -11.439 3.648   1 42.44 ? 478 TYR A CE1   1 
ATOM   3912  C  CE2   . TYR A 1 478 ? 20.791  -13.171 2.641   1 42.44 ? 478 TYR A CE2   1 
ATOM   3913  C  CZ    . TYR A 1 478 ? 21.259  -12.532 3.771   1 43.43 ? 478 TYR A CZ    1 
ATOM   3914  O  OH    . TYR A 1 478 ? 20.908  -12.979 5.022   1 45.08 ? 478 TYR A OH    1 
ATOM   3915  N  N     . SER A 1 479 ? 23.418  -13.631 -1.682  1 41.24 ? 479 SER A N     1 
ATOM   3916  C  CA    . SER A 1 479 ? 23.476  -15.076 -1.822  1 42.3  ? 479 SER A CA    1 
ATOM   3917  C  C     . SER A 1 479 ? 24.912  -15.581 -1.93   1 43.26 ? 479 SER A C     1 
ATOM   3918  O  O     . SER A 1 479 ? 25.277  -16.545 -1.262  1 43.44 ? 479 SER A O     1 
ATOM   3919  C  CB    . SER A 1 479 ? 22.656  -15.521 -3.028  1 43.89 ? 479 SER A CB    1 
ATOM   3920  O  OG    . SER A 1 479 ? 21.319  -15.057 -2.92   1 46.23 ? 479 SER A OG    1 
ATOM   3921  N  N     . ILE A 1 480 ? 25.732  -14.914 -2.746  1 43.69 ? 480 ILE A N     1 
ATOM   3922  C  CA    . ILE A 1 480 ? 27.125  -15.294 -2.959  1 44.54 ? 480 ILE A CA    1 
ATOM   3923  C  C     . ILE A 1 480 ? 27.965  -15.187 -1.686  1 45.36 ? 480 ILE A C     1 
ATOM   3924  O  O     . ILE A 1 480 ? 28.646  -16.143 -1.32   1 45.64 ? 480 ILE A O     1 
ATOM   3925  C  CB    . ILE A 1 480 ? 27.722  -14.457 -4.124  1 45.13 ? 480 ILE A CB    1 
ATOM   3926  C  CG1   . ILE A 1 480 ? 27.123  -14.889 -5.469  1 46.1  ? 480 ILE A CG1   1 
ATOM   3927  C  CG2   . ILE A 1 480 ? 29.258  -14.506 -4.157  1 45.7  ? 480 ILE A CG2   1 
ATOM   3928  C  CD1   . ILE A 1 480 ? 27.479  -13.977 -6.626  1 47.37 ? 480 ILE A CD1   1 
ATOM   3929  N  N     . PHE A 1 481 ? 27.921  -14.035 -1.019  1 45.54 ? 481 PHE A N     1 
ATOM   3930  C  CA    . PHE A 1 481 ? 28.754  -13.802 0.143   1 46.17 ? 481 PHE A CA    1 
ATOM   3931  C  C     . PHE A 1 481 ? 28.189  -14.341 1.453   1 47.12 ? 481 PHE A C     1 
ATOM   3932  O  O     . PHE A 1 481 ? 28.936  -14.428 2.419   1 47.54 ? 481 PHE A O     1 
ATOM   3933  C  CB    . PHE A 1 481 ? 29.091  -12.315 0.253   1 45.86 ? 481 PHE A CB    1 
ATOM   3934  C  CG    . PHE A 1 481 ? 30.041  -11.859 -0.827  1 46.1  ? 481 PHE A CG    1 
ATOM   3935  C  CD1   . PHE A 1 481 ? 31.372  -12.23  -0.801  1 46.7  ? 481 PHE A CD1   1 
ATOM   3936  C  CD2   . PHE A 1 481 ? 29.6    -11.072 -1.874  1 46.67 ? 481 PHE A CD2   1 
ATOM   3937  C  CE1   . PHE A 1 481 ? 32.242  -11.818 -1.795  1 47.29 ? 481 PHE A CE1   1 
ATOM   3938  C  CE2   . PHE A 1 481 ? 30.472  -10.666 -2.869  1 47.32 ? 481 PHE A CE2   1 
ATOM   3939  C  CZ    . PHE A 1 481 ? 31.788  -11.042 -2.824  1 47.11 ? 481 PHE A CZ    1 
ATOM   3940  N  N     . LYS A 1 482 ? 26.905  -14.721 1.504   1 47.23 ? 482 LYS A N     1 
ATOM   3941  C  CA    . LYS A 1 482 ? 26.33   -15.243 2.749   1 47.64 ? 482 LYS A CA    1 
ATOM   3942  C  C     . LYS A 1 482 ? 26.145  -16.76  2.72    1 48.06 ? 482 LYS A C     1 
ATOM   3943  O  O     . LYS A 1 482 ? 26.224  -17.398 3.769   1 48.45 ? 482 LYS A O     1 
ATOM   3944  C  CB    . LYS A 1 482 ? 25.011  -14.52  3.106   1 49.17 ? 482 LYS A CB    1 
ATOM   3945  C  CG    . LYS A 1 482 ? 24.522  -14.725 4.535   1 52.78 ? 482 LYS A CG    1 
ATOM   3946  C  CD    . LYS A 1 482 ? 25.536  -14.271 5.566   1 56.8  ? 482 LYS A CD    1 
ATOM   3947  C  CE    . LYS A 1 482 ? 24.989  -14.264 6.97    1 60.15 ? 482 LYS A CE    1 
ATOM   3948  N  NZ    . LYS A 1 482 ? 26.049  -13.938 7.957   1 62.24 ? 482 LYS A NZ    1 
ATOM   3949  N  N     . TYR A 1 483 ? 25.924  -17.347 1.531   1 47.89 ? 483 TYR A N     1 
ATOM   3950  C  CA    . TYR A 1 483 ? 25.67   -18.78  1.446   1 48.16 ? 483 TYR A CA    1 
ATOM   3951  C  C     . TYR A 1 483 ? 26.696  -19.581 0.648   1 48.75 ? 483 TYR A C     1 
ATOM   3952  O  O     . TYR A 1 483 ? 26.948  -20.733 0.995   1 48.77 ? 483 TYR A O     1 
ATOM   3953  C  CB    . TYR A 1 483 ? 24.254  -19.028 0.909   1 47.97 ? 483 TYR A CB    1 
ATOM   3954  C  CG    . TYR A 1 483 ? 23.198  -18.396 1.792   1 48.5  ? 483 TYR A CG    1 
ATOM   3955  C  CD1   . TYR A 1 483 ? 23.066  -18.766 3.121   1 49.39 ? 483 TYR A CD1   1 
ATOM   3956  C  CD2   . TYR A 1 483 ? 22.379  -17.382 1.317   1 49.25 ? 483 TYR A CD2   1 
ATOM   3957  C  CE1   . TYR A 1 483 ? 22.126  -18.163 3.95    1 50.29 ? 483 TYR A CE1   1 
ATOM   3958  C  CE2   . TYR A 1 483 ? 21.435  -16.769 2.137   1 50.14 ? 483 TYR A CE2   1 
ATOM   3959  C  CZ    . TYR A 1 483 ? 21.312  -17.161 3.457   1 51.2  ? 483 TYR A CZ    1 
ATOM   3960  O  OH    . TYR A 1 483 ? 20.385  -16.57  4.29    1 52.96 ? 483 TYR A OH    1 
ATOM   3961  N  N     . ILE A 1 484 ? 27.279  -19.003 -0.406  1 49.17 ? 484 ILE A N     1 
ATOM   3962  C  CA    . ILE A 1 484 ? 28.235  -19.738 -1.236  1 50.24 ? 484 ILE A CA    1 
ATOM   3963  C  C     . ILE A 1 484 ? 29.687  -19.648 -0.728  1 51.16 ? 484 ILE A C     1 
ATOM   3964  O  O     . ILE A 1 484 ? 30.277  -20.679 -0.417  1 51.31 ? 484 ILE A O     1 
ATOM   3965  C  CB    . ILE A 1 484 ? 28.113  -19.336 -2.726  1 50.9  ? 484 ILE A CB    1 
ATOM   3966  C  CG1   . ILE A 1 484 ? 26.698  -19.62  -3.24   1 51.97 ? 484 ILE A CG1   1 
ATOM   3967  C  CG2   . ILE A 1 484 ? 29.171  -20.05  -3.574  1 51.38 ? 484 ILE A CG2   1 
ATOM   3968  C  CD1   . ILE A 1 484 ? 26.411  -19.067 -4.583  1 53.37 ? 484 ILE A CD1   1 
ATOM   3969  N  N     . VAL A 1 485 ? 30.262  -18.439 -0.649  1 51.67 ? 485 VAL A N     1 
ATOM   3970  C  CA    . VAL A 1 485 ? 31.645  -18.241 -0.221  1 52.6  ? 485 VAL A CA    1 
ATOM   3971  C  C     . VAL A 1 485 ? 31.849  -18.53  1.27    1 53.83 ? 485 VAL A C     1 
ATOM   3972  O  O     . VAL A 1 485 ? 31.214  -17.909 2.124   1 54.01 ? 485 VAL A O     1 
ATOM   3973  C  CB    . VAL A 1 485 ? 32.159  -16.846 -0.62   1 53    ? 485 VAL A CB    1 
ATOM   3974  C  CG1   . VAL A 1 485 ? 33.59   -16.639 -0.15   1 53.45 ? 485 VAL A CG1   1 
ATOM   3975  C  CG2   . VAL A 1 485 ? 32.048  -16.645 -2.129  1 53.34 ? 485 VAL A CG2   1 
ATOM   3976  N  N     . PRO A 1 486 ? 32.745  -19.479 1.593   1 54.52 ? 486 PRO A N     1 
ATOM   3977  C  CA    . PRO A 1 486 ? 32.951  -19.859 2.997   1 55.32 ? 486 PRO A CA    1 
ATOM   3978  C  C     . PRO A 1 486 ? 33.668  -18.845 3.879   1 56.49 ? 486 PRO A C     1 
ATOM   3979  O  O     . PRO A 1 486 ? 34.377  -17.972 3.382   1 56.54 ? 486 PRO A O     1 
ATOM   3980  C  CB    . PRO A 1 486 ? 33.757  -21.151 2.888   1 55.87 ? 486 PRO A CB    1 
ATOM   3981  C  CG    . PRO A 1 486 ? 34.505  -21.004 1.625   1 56.05 ? 486 PRO A CG    1 
ATOM   3982  C  CD    . PRO A 1 486 ? 33.553  -20.314 0.69    1 54.2  ? 486 PRO A CD    1 
ATOM   3983  N  N     . ASN A 1 487 ? 33.486  -19.001 5.208   1 57.26 ? 487 ASN A N     1 
ATOM   3984  C  CA    . ASN A 1 487 ? 34.047  -18.159 6.263   1 58.41 ? 487 ASN A CA    1 
ATOM   3985  C  C     . ASN A 1 487 ? 33.784  -16.69  6.008   1 59.31 ? 487 ASN A C     1 
ATOM   3986  O  O     . ASN A 1 487 ? 34.692  -15.865 6.048   1 59.37 ? 487 ASN A O     1 
ATOM   3987  C  CB    . ASN A 1 487 ? 35.516  -18.458 6.503   1 59.61 ? 487 ASN A CB    1 
ATOM   3988  C  CG    . ASN A 1 487 ? 35.755  -19.867 6.988   1 62.81 ? 487 ASN A CG    1 
ATOM   3989  O  OD1   . ASN A 1 487 ? 35.725  -20.149 8.19    1 64.18 ? 487 ASN A OD1   1 
ATOM   3990  N  ND2   . ASN A 1 487 ? 35.991  -20.786 6.062   1 63.19 ? 487 ASN A ND2   1 
ATOM   3991  N  N     . CYS A 1 488 ? 32.519  -16.383 5.721   1 59.87 ? 488 CYS A N     1 
ATOM   3992  C  CA    . CYS A 1 488 ? 32.028  -15.046 5.431   1 60.91 ? 488 CYS A CA    1 
ATOM   3993  C  C     . CYS A 1 488 ? 31.041  -14.57  6.494   1 61.65 ? 488 CYS A C     1 
ATOM   3994  O  O     . CYS A 1 488 ? 30.409  -15.383 7.165   1 61.79 ? 488 CYS A O     1 
ATOM   3995  C  CB    . CYS A 1 488 ? 31.397  -15.012 4.046   1 61.89 ? 488 CYS A CB    1 
ATOM   3996  S  SG    . CYS A 1 488 ? 32.542  -14.589 2.712   1 66.32 ? 488 CYS A SG    1 
ATOM   3997  N  N     . PHE A 1 489 ? 30.884  -13.253 6.623   1 62.02 ? 489 PHE A N     1 
ATOM   3998  C  CA    . PHE A 1 489 ? 29.965  -12.692 7.601   1 62.92 ? 489 PHE A CA    1 
ATOM   3999  C  C     . PHE A 1 489 ? 29.279  -11.424 7.086   1 63.84 ? 489 PHE A C     1 
ATOM   4000  O  O     . PHE A 1 489 ? 29.942  -10.524 6.571   1 64.09 ? 489 PHE A O     1 
ATOM   4001  C  CB    . PHE A 1 489 ? 30.694  -12.437 8.923   1 62.87 ? 489 PHE A CB    1 
ATOM   4002  C  CG    . PHE A 1 489 ? 29.787  -11.919 10.008  1 63.53 ? 489 PHE A CG    1 
ATOM   4003  C  CD1   . PHE A 1 489 ? 28.853  -12.745 10.607  1 64.3  ? 489 PHE A CD1   1 
ATOM   4004  C  CD2   . PHE A 1 489 ? 29.86   -10.603 10.423  1 64.26 ? 489 PHE A CD2   1 
ATOM   4005  C  CE1   . PHE A 1 489 ? 28.012  -12.264 11.604  1 64.96 ? 489 PHE A CE1   1 
ATOM   4006  C  CE2   . PHE A 1 489 ? 29.017  -10.127 11.416  1 64.99 ? 489 PHE A CE2   1 
ATOM   4007  C  CZ    . PHE A 1 489 ? 28.099  -10.959 12.001  1 64.78 ? 489 PHE A CZ    1 
ATOM   4008  N  N     . SER A 1 490 ? 27.948  -11.352 7.222   1 64.13 ? 490 SER A N     1 
ATOM   4009  C  CA    . SER A 1 490 ? 27.181  -10.193 6.768   1 64.83 ? 490 SER A CA    1 
ATOM   4010  C  C     . SER A 1 490 ? 26.908  -9.224  7.909   1 65.27 ? 490 SER A C     1 
ATOM   4011  O  O     . SER A 1 490 ? 25.832  -9.253  8.508   1 65.42 ? 490 SER A O     1 
ATOM   4012  C  CB    . SER A 1 490 ? 25.864  -10.63  6.133   1 66.21 ? 490 SER A CB    1 
ATOM   4013  O  OG    . SER A 1 490 ? 25.061  -9.52   5.765   1 68.51 ? 490 SER A OG    1 
ATOM   4014  N  N     . GLY A 1 491 ? 27.876  -8.37   8.193   1 65.38 ? 491 GLY A N     1 
ATOM   4015  C  CA    . GLY A 1 491 ? 27.727  -7.374  9.241   1 66.08 ? 491 GLY A CA    1 
ATOM   4016  C  C     . GLY A 1 491 ? 26.736  -6.296  8.854   1 66.63 ? 491 GLY A C     1 
ATOM   4017  O  O     . GLY A 1 491 ? 25.923  -5.868  9.676   1 66.96 ? 491 GLY A O     1 
ATOM   4018  N  N     . MET A 1 492 ? 26.773  -5.871  7.585   1 66.65 ? 492 MET A N     1 
ATOM   4019  C  CA    . MET A 1 492 ? 25.872  -4.837  7.089   1 67.15 ? 492 MET A CA    1 
ATOM   4020  C  C     . MET A 1 492 ? 25.162  -5.254  5.813   1 67.19 ? 492 MET A C     1 
ATOM   4021  O  O     . MET A 1 492 ? 25.767  -5.882  4.948   1 67.19 ? 492 MET A O     1 
ATOM   4022  C  CB    . MET A 1 492 ? 26.643  -3.538  6.823   1 68.07 ? 492 MET A CB    1 
ATOM   4023  C  CG    . MET A 1 492 ? 26.471  -2.504  7.899   1 70.48 ? 492 MET A CG    1 
ATOM   4024  S  SD    . MET A 1 492 ? 26.215  -0.855  7.221   1 75.28 ? 492 MET A SD    1 
ATOM   4025  C  CE    . MET A 1 492 ? 24.635  -1.066  6.466   1 73.54 ? 492 MET A CE    1 
ATOM   4026  N  N     . CYS A 1 493 ? 23.884  -4.87   5.684   1 67.12 ? 493 CYS A N     1 
ATOM   4027  C  CA    . CYS A 1 493 ? 23.093  -5.125  4.49    1 67.62 ? 493 CYS A CA    1 
ATOM   4028  C  C     . CYS A 1 493 ? 21.923  -4.158  4.4     1 67.94 ? 493 CYS A C     1 
ATOM   4029  O  O     . CYS A 1 493 ? 20.927  -4.319  5.104   1 68.1  ? 493 CYS A O     1 
ATOM   4030  C  CB    . CYS A 1 493 ? 22.636  -6.575  4.405   1 68.34 ? 493 CYS A CB    1 
ATOM   4031  S  SG    . CYS A 1 493 ? 22.37   -7.157  2.71    1 71.52 ? 493 CYS A SG    1 
ATOM   4032  N  N     . ASN A 1 494 ? 22.06   -3.137  3.542   1 67.92 ? 494 ASN A N     1 
ATOM   4033  C  CA    . ASN A 1 494 ? 21.052  -2.105  3.321   1 68.4  ? 494 ASN A CA    1 
ATOM   4034  C  C     . ASN A 1 494 ? 20.601  -2.013  1.856   1 68.66 ? 494 ASN A C     1 
ATOM   4035  O  O     . ASN A 1 494 ? 20.977  -1.082  1.143   1 68.81 ? 494 ASN A O     1 
ATOM   4036  C  CB    . ASN A 1 494 ? 21.553  -0.745  3.813   1 69.47 ? 494 ASN A CB    1 
ATOM   4037  C  CG    . ASN A 1 494 ? 20.882  -0.282  5.085   1 72.68 ? 494 ASN A CG    1 
ATOM   4038  O  OD1   . ASN A 1 494 ? 21.249  -0.68   6.196   1 73.77 ? 494 ASN A OD1   1 
ATOM   4039  N  ND2   . ASN A 1 494 ? 19.871  0.565   4.953   1 73.35 ? 494 ASN A ND2   1 
ATOM   4040  N  N     . PRO A 1 495 ? 19.746  -2.948  1.403   1 68.57 ? 495 PRO A N     1 
ATOM   4041  C  CA    . PRO A 1 495 ? 19.238  -2.878  0.021   1 68.71 ? 495 PRO A CA    1 
ATOM   4042  C  C     . PRO A 1 495 ? 18.175  -1.767  -0.182  1 69.03 ? 495 PRO A C     1 
ATOM   4043  O  O     . PRO A 1 495 ? 17.805  -1.11   0.793   1 69.06 ? 495 PRO A O     1 
ATOM   4044  C  CB    . PRO A 1 495 ? 18.668  -4.296  -0.206  1 69.29 ? 495 PRO A CB    1 
ATOM   4045  C  CG    . PRO A 1 495 ? 19.025  -5.1    1.025   1 69.59 ? 495 PRO A CG    1 
ATOM   4046  C  CD    . PRO A 1 495 ? 19.188  -4.11   2.116   1 68.02 ? 495 PRO A CD    1 
ATOM   4047  N  N     . PRO A 1 496 ? 17.671  -1.507  -1.416  1 69.16 ? 496 PRO A N     1 
ATOM   4048  C  CA    . PRO A 1 496 ? 16.657  -0.446  -1.579  1 69.39 ? 496 PRO A CA    1 
ATOM   4049  C  C     . PRO A 1 496 ? 15.385  -0.695  -0.767  1 69.66 ? 496 PRO A C     1 
ATOM   4050  O  O     . PRO A 1 496 ? 14.754  -1.743  -0.897  1 69.8  ? 496 PRO A O     1 
ATOM   4051  C  CB    . PRO A 1 496 ? 16.365  -0.455  -3.086  1 70.03 ? 496 PRO A CB    1 
ATOM   4052  C  CG    . PRO A 1 496 ? 17.52   -1.137  -3.704  1 70.32 ? 496 PRO A CG    1 
ATOM   4053  C  CD    . PRO A 1 496 ? 17.982  -2.146  -2.707  1 68.67 ? 496 PRO A CD    1 
ATOM   4054  N  N     . GLY A 1 497 ? 15.032  0.273   0.071   1 69.58 ? 497 GLY A N     1 
ATOM   4055  C  CA    . GLY A 1 497 ? 13.85   0.198   0.923   1 70.01 ? 497 GLY A CA    1 
ATOM   4056  C  C     . GLY A 1 497 ? 14.053  -0.652  2.159   1 70.28 ? 497 GLY A C     1 
ATOM   4057  O  O     . GLY A 1 497 ? 13.114  -1.29   2.639   1 70.44 ? 497 GLY A O     1 
ATOM   4058  N  N     . GLY A 1 498 ? 15.277  -0.648  2.675   1 70.24 ? 498 GLY A N     1 
ATOM   4059  C  CA    . GLY A 1 498 ? 15.645  -1.449  3.832   1 70.76 ? 498 GLY A CA    1 
ATOM   4060  C  C     . GLY A 1 498 ? 15.764  -0.696  5.138   1 71.09 ? 498 GLY A C     1 
ATOM   4061  O  O     . GLY A 1 498 ? 15.939  0.525   5.153   1 71.12 ? 498 GLY A O     1 
ATOM   4062  N  N     . ASP A 1 499 ? 15.687  -1.449  6.248   1 71.16 ? 499 ASP A N     1 
ATOM   4063  C  CA    . ASP A 1 499 ? 15.782  -0.954  7.621   1 71.59 ? 499 ASP A CA    1 
ATOM   4064  C  C     . ASP A 1 499 ? 17.208  -0.474  7.972   1 71.96 ? 499 ASP A C     1 
ATOM   4065  O  O     . ASP A 1 499 ? 18.158  -0.716  7.227   1 72.33 ? 499 ASP A O     1 
ATOM   4066  C  CB    . ASP A 1 499 ? 15.361  -2.068  8.604   1 72.99 ? 499 ASP A CB    1 
ATOM   4067  C  CG    . ASP A 1 499 ? 13.884  -2.425  8.616   1 77.08 ? 499 ASP A CG    1 
ATOM   4068  O  OD1   . ASP A 1 499 ? 13.251  -2.376  7.543   1 77.62 ? 499 ASP A OD1   1 
ATOM   4069  O  OD2   . ASP A 1 499 ? 13.371  -2.791  9.694   1 79.21 ? 499 ASP A OD2   1 
ATOM   4070  N  N     . TRP A 1 500 ? 17.351  0.207   9.112   1 71.72 ? 500 TRP A N     1 
ATOM   4071  C  CA    . TRP A 1 500 ? 18.644  0.656   9.606   1 72.03 ? 500 TRP A CA    1 
ATOM   4072  C  C     . TRP A 1 500 ? 19.16   -0.523  10.415  1 72.52 ? 500 TRP A C     1 
ATOM   4073  O  O     . TRP A 1 500 ? 18.847  -0.65   11.597  1 72.69 ? 500 TRP A O     1 
ATOM   4074  C  CB    . TRP A 1 500 ? 18.441  1.885   10.501  1 71.83 ? 500 TRP A CB    1 
ATOM   4075  C  CG    . TRP A 1 500 ? 18.898  3.2     9.934   1 72.07 ? 500 TRP A CG    1 
ATOM   4076  C  CD1   . TRP A 1 500 ? 19.688  4.116   10.556  1 72.89 ? 500 TRP A CD1   1 
ATOM   4077  C  CD2   . TRP A 1 500 ? 18.519  3.787   8.679   1 72.06 ? 500 TRP A CD2   1 
ATOM   4078  N  NE1   . TRP A 1 500 ? 19.855  5.221   9.758   1 73.14 ? 500 TRP A NE1   1 
ATOM   4079  C  CE2   . TRP A 1 500 ? 19.154  5.042   8.596   1 72.8  ? 500 TRP A CE2   1 
ATOM   4080  C  CE3   . TRP A 1 500 ? 17.727  3.365   7.606   1 72.46 ? 500 TRP A CE3   1 
ATOM   4081  C  CZ2   . TRP A 1 500 ? 19.016  5.877   7.49    1 73.3  ? 500 TRP A CZ2   1 
ATOM   4082  C  CZ3   . TRP A 1 500 ? 17.596  4.192   6.51    1 73.24 ? 500 TRP A CZ3   1 
ATOM   4083  C  CH2   . TRP A 1 500 ? 18.229  5.436   6.463   1 73.31 ? 500 TRP A CH2   1 
ATOM   4084  N  N     . SER A 1 501 ? 19.878  -1.433  9.751   1 72.62 ? 501 SER A N     1 
ATOM   4085  C  CA    . SER A 1 501 ? 20.368  -2.667  10.354  1 73.18 ? 501 SER A CA    1 
ATOM   4086  C  C     . SER A 1 501 ? 21.467  -2.48   11.411  1 73.41 ? 501 SER A C     1 
ATOM   4087  O  O     . SER A 1 501 ? 21.295  -2.921  12.544  1 73.54 ? 501 SER A O     1 
ATOM   4088  C  CB    . SER A 1 501 ? 20.824  -3.647  9.27    1 74.55 ? 501 SER A CB    1 
ATOM   4089  O  OG    . SER A 1 501 ? 21.354  -4.845  9.814   1 76.72 ? 501 SER A OG    1 
ATOM   4090  N  N     . GLY A 1 502 ? 22.58   -1.862  11.037  1 73.3  ? 502 GLY A N     1 
ATOM   4091  C  CA    . GLY A 1 502 ? 23.729  -1.714  11.919  1 73.69 ? 502 GLY A CA    1 
ATOM   4092  C  C     . GLY A 1 502 ? 24.922  -2.505  11.41   1 73.88 ? 502 GLY A C     1 
ATOM   4093  O  O     . GLY A 1 502 ? 24.773  -3.342  10.516  1 74.06 ? 502 GLY A O     1 
ATOM   4094  N  N     . LEU A 1 503 ? 26.116  -2.26   11.964  1 73.72 ? 503 LEU A N     1 
ATOM   4095  C  CA    . LEU A 1 503 ? 27.32   -2.954  11.509  1 74.05 ? 503 LEU A CA    1 
ATOM   4096  C  C     . LEU A 1 503 ? 27.902  -3.89   12.558  1 74.23 ? 503 LEU A C     1 
ATOM   4097  O  O     . LEU A 1 503 ? 28.184  -3.461  13.666  1 74.25 ? 503 LEU A O     1 
ATOM   4098  C  CB    . LEU A 1 503 ? 28.385  -1.942  11.047  1 74.26 ? 503 LEU A CB    1 
ATOM   4099  C  CG    . LEU A 1 503 ? 29.754  -2.521  10.668  1 75.63 ? 503 LEU A CG    1 
ATOM   4100  C  CD1   . LEU A 1 503 ? 29.673  -3.363  9.417   1 76.05 ? 503 LEU A CD1   1 
ATOM   4101  C  CD2   . LEU A 1 503 ? 30.786  -1.437  10.53   1 76.35 ? 503 LEU A CD2   1 
ATOM   4102  N  N     . SER A 1 504 ? 28.151  -5.145  12.183  1 74.19 ? 504 SER A N     1 
ATOM   4103  C  CA    . SER A 1 504 ? 28.775  -6.111  13.073  1 74.64 ? 504 SER A CA    1 
ATOM   4104  C  C     . SER A 1 504 ? 30.164  -6.491  12.565  1 74.91 ? 504 SER A C     1 
ATOM   4105  O  O     . SER A 1 504 ? 30.342  -6.734  11.375  1 75.05 ? 504 SER A O     1 
ATOM   4106  C  CB    . SER A 1 504 ? 27.922  -7.365  13.186  1 76    ? 504 SER A CB    1 
ATOM   4107  O  OG    . SER A 1 504 ? 26.695  -7.111  13.844  1 78.43 ? 504 SER A OG    1 
ATOM   4108  N  N     . ILE A 1 505 ? 31.146  -6.54   13.47   1 74.87 ? 505 ILE A N     1 
ATOM   4109  C  CA    . ILE A 1 505 ? 32.525  -6.921  13.173  1 75.37 ? 505 ILE A CA    1 
ATOM   4110  C  C     . ILE A 1 505 ? 32.906  -8.019  14.149  1 75.79 ? 505 ILE A C     1 
ATOM   4111  O  O     . ILE A 1 505 ? 32.727  -7.839  15.348  1 76.08 ? 505 ILE A O     1 
ATOM   4112  C  CB    . ILE A 1 505 ? 33.487  -5.725  13.373  1 75.97 ? 505 ILE A CB    1 
ATOM   4113  C  CG1   . ILE A 1 505 ? 33.078  -4.494  12.546  1 76.98 ? 505 ILE A CG1   1 
ATOM   4114  C  CG2   . ILE A 1 505 ? 34.933  -6.133  13.107  1 76.46 ? 505 ILE A CG2   1 
ATOM   4115  C  CD1   . ILE A 1 505 ? 33.126  -4.669  11.08   1 78.28 ? 505 ILE A CD1   1 
ATOM   4116  N  N     . ILE A 1 506 ? 33.441  -9.138  13.665  1 75.7  ? 506 ILE A N     1 
ATOM   4117  C  CA    . ILE A 1 506 ? 33.873  -10.223 14.54   1 76.21 ? 506 ILE A CA    1 
ATOM   4118  C  C     . ILE A 1 506 ? 35.394  -10.193 14.691  1 76.7  ? 506 ILE A C     1 
ATOM   4119  O  O     . ILE A 1 506 ? 36.111  -10.217 13.696  1 76.83 ? 506 ILE A O     1 
ATOM   4120  C  CB    . ILE A 1 506 ? 33.357  -11.58  14.038  1 76.67 ? 506 ILE A CB    1 
ATOM   4121  C  CG1   . ILE A 1 506 ? 31.821  -11.604 14.038  1 77.63 ? 506 ILE A CG1   1 
ATOM   4122  C  CG2   . ILE A 1 506 ? 33.931  -12.717 14.872  1 77.14 ? 506 ILE A CG2   1 
ATOM   4123  C  CD1   . ILE A 1 506 ? 31.23   -12.786 13.351  1 78.87 ? 506 ILE A CD1   1 
ATOM   4124  N  N     . ARG A 1 507 ? 35.884  -10.091 15.931  1 76.86 ? 507 ARG A N     1 
ATOM   4125  C  CA    . ARG A 1 507 ? 37.317  -10.016 16.192  1 77.41 ? 507 ARG A CA    1 
ATOM   4126  C  C     . ARG A 1 507 ? 37.663  -10.672 17.533  1 77.43 ? 507 ARG A C     1 
ATOM   4127  O  O     . ARG A 1 507 ? 37.08   -10.313 18.558  1 77.55 ? 507 ARG A O     1 
ATOM   4128  C  CB    . ARG A 1 507 ? 37.77   -8.546  16.18   1 79.03 ? 507 ARG A CB    1 
ATOM   4129  C  CG    . ARG A 1 507 ? 39.254  -8.351  16.441  1 82.29 ? 507 ARG A CG    1 
ATOM   4130  C  CD    . ARG A 1 507 ? 40.112  -8.912  15.321  1 85.45 ? 507 ARG A CD    1 
ATOM   4131  N  NE    . ARG A 1 507 ? 41.535  -8.725  15.6    1 88.16 ? 507 ARG A NE    1 
ATOM   4132  C  CZ    . ARG A 1 507 ? 42.516  -9.381  14.987  1 90.24 ? 507 ARG A CZ    1 
ATOM   4133  N  NH1   . ARG A 1 507 ? 42.239  -10.281 14.05   1 89.85 ? 507 ARG A NH1   1 
ATOM   4134  N  NH2   . ARG A 1 507 ? 43.78   -9.146  15.307  1 90.25 ? 507 ARG A NH2   1 
ATOM   4135  N  N     . ASN A 1 508 ? 38.614  -11.633 17.512  1 77.12 ? 508 ASN A N     1 
ATOM   4136  C  CA    . ASN A 1 508 ? 39.113  -12.379 18.675  1 77.28 ? 508 ASN A CA    1 
ATOM   4137  C  C     . ASN A 1 508 ? 38.036  -13.179 19.425  1 76.93 ? 508 ASN A C     1 
ATOM   4138  O  O     . ASN A 1 508 ? 38.074  -13.277 20.651  1 77.03 ? 508 ASN A O     1 
ATOM   4139  C  CB    . ASN A 1 508 ? 39.877  -11.466 19.638  1 78.65 ? 508 ASN A CB    1 
ATOM   4140  C  CG    . ASN A 1 508 ? 41.022  -10.72  18.997  1 81.85 ? 508 ASN A CG    1 
ATOM   4141  O  OD1   . ASN A 1 508 ? 41.653  -11.189 18.041  1 82.89 ? 508 ASN A OD1   1 
ATOM   4142  N  ND2   . ASN A 1 508 ? 41.313  -9.539  19.521  1 82.53 ? 508 ASN A ND2   1 
ATOM   4143  N  N     . GLY A 1 509 ? 37.097  -13.75  18.688  1 76.38 ? 509 GLY A N     1 
ATOM   4144  C  CA    . GLY A 1 509 ? 36.02   -14.533 19.288  1 76.39 ? 509 GLY A CA    1 
ATOM   4145  C  C     . GLY A 1 509 ? 34.85   -13.721 19.819  1 76.19 ? 509 GLY A C     1 
ATOM   4146  O  O     . GLY A 1 509 ? 33.946  -14.273 20.452  1 76.38 ? 509 GLY A O     1 
ATOM   4147  N  N     . HIS A 1 510 ? 34.851  -12.402 19.571  1 75.61 ? 510 HIS A N     1 
ATOM   4148  C  CA    . HIS A 1 510 ? 33.779  -11.51  20.011  1 75.55 ? 510 HIS A CA    1 
ATOM   4149  C  C     . HIS A 1 510 ? 33.104  -10.839 18.821  1 74.98 ? 510 HIS A C     1 
ATOM   4150  O  O     . HIS A 1 510 ? 33.734  -10.646 17.786  1 74.98 ? 510 HIS A O     1 
ATOM   4151  C  CB    . HIS A 1 510 ? 34.332  -10.428 20.952  1 76.58 ? 510 HIS A CB    1 
ATOM   4152  C  CG    . HIS A 1 510 ? 34.807  -10.956 22.268  1 78.88 ? 510 HIS A CG    1 
ATOM   4153  N  ND1   . HIS A 1 510 ? 36.152  -11.181 22.514  1 80.76 ? 510 HIS A ND1   1 
ATOM   4154  C  CD2   . HIS A 1 510 ? 34.099  -11.283 23.373  1 79.98 ? 510 HIS A CD2   1 
ATOM   4155  C  CE1   . HIS A 1 510 ? 36.216  -11.64  23.753  1 81.24 ? 510 HIS A CE1   1 
ATOM   4156  N  NE2   . HIS A 1 510 ? 35.006  -11.718 24.31   1 81.09 ? 510 HIS A NE2   1 
ATOM   4157  N  N     . GLU A 1 511 ? 31.831  -10.47  18.969  1 74.33 ? 511 GLU A N     1 
ATOM   4158  C  CA    . GLU A 1 511 ? 31.115  -9.764  17.917  1 74.18 ? 511 GLU A CA    1 
ATOM   4159  C  C     . GLU A 1 511 ? 30.801  -8.371  18.437  1 73.78 ? 511 GLU A C     1 
ATOM   4160  O  O     . GLU A 1 511 ? 30.148  -8.231  19.462  1 73.87 ? 511 GLU A O     1 
ATOM   4161  C  CB    . GLU A 1 511 ? 29.821  -10.491 17.533  1 76.24 ? 511 GLU A CB    1 
ATOM   4162  C  CG    . GLU A 1 511 ? 29.021  -9.764  16.466  1 80.37 ? 511 GLU A CG    1 
ATOM   4163  C  CD    . GLU A 1 511 ? 27.659  -10.357 16.161  1 85.42 ? 511 GLU A CD    1 
ATOM   4164  O  OE1   . GLU A 1 511 ? 26.918  -9.75   15.357  1 86.07 ? 511 GLU A OE1   1 
ATOM   4165  O  OE2   . GLU A 1 511 ? 27.331  -11.43  16.718  1 87.24 ? 511 GLU A OE2   1 
ATOM   4166  N  N     . PHE A 1 512 ? 31.305  -7.349  17.762  1 73.28 ? 512 PHE A N     1 
ATOM   4167  C  CA    . PHE A 1 512 ? 31.097  -5.95   18.128  1 73.3  ? 512 PHE A CA    1 
ATOM   4168  C  C     . PHE A 1 512 ? 30.046  -5.377  17.19   1 72.81 ? 512 PHE A C     1 
ATOM   4169  O  O     . PHE A 1 512 ? 30.081  -5.673  15.997  1 72.9  ? 512 PHE A O     1 
ATOM   4170  C  CB    . PHE A 1 512 ? 32.417  -5.168  17.998  1 73.45 ? 512 PHE A CB    1 
ATOM   4171  C  CG    . PHE A 1 512 ? 33.563  -5.786  18.768  1 74.29 ? 512 PHE A CG    1 
ATOM   4172  C  CD1   . PHE A 1 512 ? 33.73   -5.529  20.116  1 75.17 ? 512 PHE A CD1   1 
ATOM   4173  C  CD2   . PHE A 1 512 ? 34.466  -6.632  18.143  1 75.1  ? 512 PHE A CD2   1 
ATOM   4174  C  CE1   . PHE A 1 512 ? 34.771  -6.116  20.826  1 75.89 ? 512 PHE A CE1   1 
ATOM   4175  C  CE2   . PHE A 1 512 ? 35.503  -7.22   18.858  1 75.81 ? 512 PHE A CE2   1 
ATOM   4176  C  CZ    . PHE A 1 512 ? 35.65   -6.957  20.193  1 75.64 ? 512 PHE A CZ    1 
ATOM   4177  N  N     . ARG A 1 513 ? 29.111  -4.571  17.707  1 72.14 ? 513 ARG A N     1 
ATOM   4178  C  CA    . ARG A 1 513 ? 28.044  -4.034  16.872  1 72.08 ? 513 ARG A CA    1 
ATOM   4179  C  C     . ARG A 1 513 ? 27.733  -2.563  17.116  1 72.05 ? 513 ARG A C     1 
ATOM   4180  O  O     . ARG A 1 513 ? 27.589  -2.139  18.259  1 72.08 ? 513 ARG A O     1 
ATOM   4181  C  CB    . ARG A 1 513 ? 26.785  -4.895  17.024  1 73.12 ? 513 ARG A CB    1 
ATOM   4182  C  CG    . ARG A 1 513 ? 25.667  -4.548  16.065  1 75.58 ? 513 ARG A CG    1 
ATOM   4183  C  CD    . ARG A 1 513 ? 24.692  -5.7    15.981  1 78.1  ? 513 ARG A CD    1 
ATOM   4184  N  NE    . ARG A 1 513 ? 23.537  -5.402  15.138  1 80.44 ? 513 ARG A NE    1 
ATOM   4185  C  CZ    . ARG A 1 513 ? 23.511  -5.542  13.816  1 82.35 ? 513 ARG A CZ    1 
ATOM   4186  N  NH1   . ARG A 1 513 ? 24.592  -5.949  13.161  1 81.92 ? 513 ARG A NH1   1 
ATOM   4187  N  NH2   . ARG A 1 513 ? 22.406  -5.272  13.138  1 82.21 ? 513 ARG A NH2   1 
ATOM   4188  N  N     . TRP A 1 514 ? 27.636  -1.786  16.024  1 71.93 ? 514 TRP A N     1 
ATOM   4189  C  CA    . TRP A 1 514 ? 27.295  -0.366  16.045  1 72.3  ? 514 TRP A CA    1 
ATOM   4190  C  C     . TRP A 1 514 ? 25.841  -0.254  15.641  1 72.67 ? 514 TRP A C     1 
ATOM   4191  O  O     . TRP A 1 514 ? 25.476  -0.701  14.561  1 72.78 ? 514 TRP A O     1 
ATOM   4192  C  CB    . TRP A 1 514 ? 28.133  0.423   15.024  1 72.17 ? 514 TRP A CB    1 
ATOM   4193  C  CG    . TRP A 1 514 ? 29.532  0.733   15.456  1 72.61 ? 514 TRP A CG    1 
ATOM   4194  C  CD1   . TRP A 1 514 ? 29.989  1.907   15.978  1 73.56 ? 514 TRP A CD1   1 
ATOM   4195  C  CD2   . TRP A 1 514 ? 30.672  -0.122  15.333  1 72.68 ? 514 TRP A CD2   1 
ATOM   4196  N  NE1   . TRP A 1 514 ? 31.34   1.822   16.218  1 73.83 ? 514 TRP A NE1   1 
ATOM   4197  C  CE2   . TRP A 1 514 ? 31.783  0.582   15.835  1 73.51 ? 514 TRP A CE2   1 
ATOM   4198  C  CE3   . TRP A 1 514 ? 30.862  -1.422  14.855  1 73.12 ? 514 TRP A CE3   1 
ATOM   4199  C  CZ2   . TRP A 1 514 ? 33.058  0.023   15.883  1 74.07 ? 514 TRP A CZ2   1 
ATOM   4200  C  CZ3   . TRP A 1 514 ? 32.123  -1.974  14.911  1 73.9  ? 514 TRP A CZ3   1 
ATOM   4201  C  CH2   . TRP A 1 514 ? 33.202  -1.258  15.423  1 74.08 ? 514 TRP A CH2   1 
ATOM   4202  N  N     . LEU A 1 515 ? 25.011  0.329   16.496  1 72.69 ? 515 LEU A N     1 
ATOM   4203  C  CA    . LEU A 1 515 ? 23.589  0.521   16.209  1 73.22 ? 515 LEU A CA    1 
ATOM   4204  C  C     . LEU A 1 515 ? 23.309  2.012   15.934  1 73.56 ? 515 LEU A C     1 
ATOM   4205  O  O     . LEU A 1 515 ? 24.183  2.849   16.168  1 73.54 ? 515 LEU A O     1 
ATOM   4206  C  CB    . LEU A 1 515 ? 22.732  0.017   17.386  1 73.47 ? 515 LEU A CB    1 
ATOM   4207  C  CG    . LEU A 1 515 ? 23.02   -1.4    17.866  1 74.89 ? 515 LEU A CG    1 
ATOM   4208  C  CD1   . LEU A 1 515 ? 22.403  -1.641  19.223  1 75.48 ? 515 LEU A CD1   1 
ATOM   4209  C  CD2   . LEU A 1 515 ? 22.542  -2.424  16.858  1 75.45 ? 515 LEU A CD2   1 
ATOM   4210  N  N     . SER A 1 516 ? 22.098  2.342   15.429  1 73.77 ? 516 SER A N     1 
ATOM   4211  C  CA    . SER A 1 516 ? 21.692  3.715   15.121  1 74.52 ? 516 SER A CA    1 
ATOM   4212  C  C     . SER A 1 516 ? 22.721  4.423   14.22   1 75.15 ? 516 SER A C     1 
ATOM   4213  O  O     . SER A 1 516 ? 23.253  5.467   14.586  1 75.24 ? 516 SER A O     1 
ATOM   4214  C  CB    . SER A 1 516 ? 21.448  4.509   16.403  1 75.96 ? 516 SER A CB    1 
ATOM   4215  O  OG    . SER A 1 516 ? 20.59   3.841   17.312  1 78.27 ? 516 SER A OG    1 
ATOM   4216  N  N     . LEU A 1 517 ? 23.036  3.822   13.064  1 75.48 ? 517 LEU A N     1 
ATOM   4217  C  CA    . LEU A 1 517 ? 24.014  4.379   12.129  1 76.31 ? 517 LEU A CA    1 
ATOM   4218  C  C     . LEU A 1 517 ? 23.469  5.61    11.433  1 77.35 ? 517 LEU A C     1 
ATOM   4219  O  O     . LEU A 1 517 ? 22.515  5.488   10.668  1 77.56 ? 517 LEU A O     1 
ATOM   4220  C  CB    . LEU A 1 517 ? 24.382  3.347   11.052  1 76.4  ? 517 LEU A CB    1 
ATOM   4221  C  CG    . LEU A 1 517 ? 24.91   2.001   11.515  1 77.8  ? 517 LEU A CG    1 
ATOM   4222  C  CD1   . LEU A 1 517 ? 25.245  1.12    10.335  1 78.28 ? 517 LEU A CD1   1 
ATOM   4223  C  CD2   . LEU A 1 517 ? 26.134  2.17    12.368  1 78.5  ? 517 LEU A CD2   1 
ATOM   4224  N  N     . PRO A 1 518 ? 24.069  6.798   11.635  1 77.79 ? 518 PRO A N     1 
ATOM   4225  C  CA    . PRO A 1 518 ? 23.565  7.986   10.927  1 78.01 ? 518 PRO A CA    1 
ATOM   4226  C  C     . PRO A 1 518 ? 23.954  7.963   9.451   1 78.16 ? 518 PRO A C     1 
ATOM   4227  O  O     . PRO A 1 518 ? 25.032  7.478   9.106   1 78.25 ? 518 PRO A O     1 
ATOM   4228  C  CB    . PRO A 1 518 ? 24.219  9.149   11.675  1 78.78 ? 518 PRO A CB    1 
ATOM   4229  C  CG    . PRO A 1 518 ? 25.476  8.579   12.225  1 79.22 ? 518 PRO A CG    1 
ATOM   4230  C  CD    . PRO A 1 518 ? 25.225  7.117   12.498  1 77.52 ? 518 PRO A CD    1 
ATOM   4231  N  N     . ARG A 1 519 ? 23.059  8.438   8.579   1 78.08 ? 519 ARG A N     1 
ATOM   4232  C  CA    . ARG A 1 519 ? 23.353  8.487   7.15    1 78.52 ? 519 ARG A CA    1 
ATOM   4233  C  C     . ARG A 1 519 ? 24.42   9.554   6.885   1 78.85 ? 519 ARG A C     1 
ATOM   4234  O  O     . ARG A 1 519 ? 25.314  9.346   6.064   1 79.01 ? 519 ARG A O     1 
ATOM   4235  C  CB    . ARG A 1 519 ? 22.085  8.79    6.335   1 79.62 ? 519 ARG A CB    1 
ATOM   4236  C  CG    . ARG A 1 519 ? 22.236  8.512   4.847   1 82.06 ? 519 ARG A CG    1 
ATOM   4237  C  CD    . ARG A 1 519 ? 21.29   9.363   4.018   1 84.61 ? 519 ARG A CD    1 
ATOM   4238  N  NE    . ARG A 1 519 ? 21.592  10.79   4.138   1 86.61 ? 519 ARG A NE    1 
ATOM   4239  C  CZ    . ARG A 1 519 ? 22.43   11.451  3.345   1 88.12 ? 519 ARG A CZ    1 
ATOM   4240  N  NH1   . ARG A 1 519 ? 23.064  10.82   2.364   1 87.68 ? 519 ARG A NH1   1 
ATOM   4241  N  NH2   . ARG A 1 519 ? 22.639  12.748  3.523   1 87.74 ? 519 ARG A NH2   1 
ATOM   4242  N  N     . VAL A 1 520 ? 24.329  10.692  7.588   1 78.7  ? 520 VAL A N     1 
ATOM   4243  C  CA    . VAL A 1 520 ? 25.26   11.795  7.413   1 78.88 ? 520 VAL A CA    1 
ATOM   4244  C  C     . VAL A 1 520 ? 26.651  11.516  8.027   1 78.73 ? 520 VAL A C     1 
ATOM   4245  O  O     . VAL A 1 520 ? 26.81   11.387  9.244   1 78.86 ? 520 VAL A O     1 
ATOM   4246  C  CB    . VAL A 1 520 ? 24.665  13.145  7.894   1 79.6  ? 520 VAL A CB    1 
ATOM   4247  C  CG1   . VAL A 1 520 ? 23.664  13.688  6.882   1 80.14 ? 520 VAL A CG1   1 
ATOM   4248  C  CG2   . VAL A 1 520 ? 24.019  13.017  9.273   1 80.04 ? 520 VAL A CG2   1 
ATOM   4249  N  N     . SER A 1 521 ? 27.652  11.399  7.148   1 78.17 ? 521 SER A N     1 
ATOM   4250  C  CA    . SER A 1 521 ? 29.059  11.22   7.502   1 78.05 ? 521 SER A CA    1 
ATOM   4251  C  C     . SER A 1 521 ? 29.841  12.274  6.713   1 77.78 ? 521 SER A C     1 
ATOM   4252  O  O     . SER A 1 521 ? 29.608  12.442  5.511   1 78.2  ? 521 SER A O     1 
ATOM   4253  C  CB    . SER A 1 521 ? 29.542  9.814   7.159   1 79.1  ? 521 SER A CB    1 
ATOM   4254  O  OG    . SER A 1 521 ? 30.951  9.696   7.292   1 81.01 ? 521 SER A OG    1 
ATOM   4255  N  N     . GLU A 1 522 ? 30.726  13.015  7.394   1 76.88 ? 522 GLU A N     1 
ATOM   4256  C  CA    . GLU A 1 522 ? 31.507  14.093  6.794   1 76.47 ? 522 GLU A CA    1 
ATOM   4257  C  C     . GLU A 1 522 ? 32.293  13.665  5.56    1 75.84 ? 522 GLU A C     1 
ATOM   4258  O  O     . GLU A 1 522 ? 32.259  14.361  4.546   1 75.96 ? 522 GLU A O     1 
ATOM   4259  C  CB    . GLU A 1 522 ? 32.419  14.752  7.836   1 78.55 ? 522 GLU A CB    1 
ATOM   4260  C  CG    . GLU A 1 522 ? 31.641  15.264  9.032   1 82.86 ? 522 GLU A CG    1 
ATOM   4261  C  CD    . GLU A 1 522 ? 31.519  14.308  10.203  1 88.37 ? 522 GLU A CD    1 
ATOM   4262  O  OE1   . GLU A 1 522 ? 30.589  13.469  10.195  1 89.09 ? 522 GLU A OE1   1 
ATOM   4263  O  OE2   . GLU A 1 522 ? 32.341  14.413  11.141  1 90.43 ? 522 GLU A OE2   1 
ATOM   4264  N  N     . ASN A 1 523 ? 32.966  12.506  5.619   1 75.03 ? 523 ASN A N     1 
ATOM   4265  C  CA    . ASN A 1 523 ? 33.746  12.009  4.481   1 74.64 ? 523 ASN A CA    1 
ATOM   4266  C  C     . ASN A 1 523 ? 33.258  10.667  3.907   1 73.91 ? 523 ASN A C     1 
ATOM   4267  O  O     . ASN A 1 523 ? 33.771  10.235  2.876   1 74.07 ? 523 ASN A O     1 
ATOM   4268  C  CB    . ASN A 1 523 ? 35.221  11.877  4.861   1 75.73 ? 523 ASN A CB    1 
ATOM   4269  C  CG    . ASN A 1 523 ? 35.818  13.122  5.453   1 78.9  ? 523 ASN A CG    1 
ATOM   4270  O  OD1   . ASN A 1 523 ? 36.074  13.2    6.659   1 80.26 ? 523 ASN A OD1   1 
ATOM   4271  N  ND2   . ASN A 1 523 ? 36.057  14.119  4.616   1 79.41 ? 523 ASN A ND2   1 
ATOM   4272  N  N     . GLY A 1 524 ? 32.308  10.01   4.572   1 72.94 ? 524 GLY A N     1 
ATOM   4273  C  CA    . GLY A 1 524 ? 31.844  8.703   4.129   1 72.44 ? 524 GLY A CA    1 
ATOM   4274  C  C     . GLY A 1 524 ? 30.391  8.551   3.73    1 71.66 ? 524 GLY A C     1 
ATOM   4275  O  O     . GLY A 1 524 ? 29.576  9.451   3.936   1 71.73 ? 524 GLY A O     1 
ATOM   4276  N  N     . LYS A 1 525 ? 30.074  7.393   3.129   1 70.78 ? 525 LYS A N     1 
ATOM   4277  C  CA    . LYS A 1 525 ? 28.729  6.997   2.708   1 70.42 ? 525 LYS A CA    1 
ATOM   4278  C  C     . LYS A 1 525 ? 28.487  5.563   3.182   1 69.69 ? 525 LYS A C     1 
ATOM   4279  O  O     . LYS A 1 525 ? 29.372  4.72    3.047   1 69.8  ? 525 LYS A O     1 
ATOM   4280  C  CB    . LYS A 1 525 ? 28.554  7.094   1.185   1 72.25 ? 525 LYS A CB    1 
ATOM   4281  C  CG    . LYS A 1 525 ? 27.092  6.969   0.758   1 76.02 ? 525 LYS A CG    1 
ATOM   4282  C  CD    . LYS A 1 525 ? 26.84   7.449   -0.658  1 79.79 ? 525 LYS A CD    1 
ATOM   4283  C  CE    . LYS A 1 525 ? 25.364  7.515   -0.952  1 83.1  ? 525 LYS A CE    1 
ATOM   4284  N  NZ    . LYS A 1 525 ? 24.686  8.518   -0.094  1 85.15 ? 525 LYS A NZ    1 
ATOM   4285  N  N     . ARG A 1 526 ? 27.307  5.29    3.757   1 68.75 ? 526 ARG A N     1 
ATOM   4286  C  CA    . ARG A 1 526 ? 26.98   3.97    4.291   1 68.32 ? 526 ARG A CA    1 
ATOM   4287  C  C     . ARG A 1 526 ? 26.945  2.904   3.211   1 67.35 ? 526 ARG A C     1 
ATOM   4288  O  O     . ARG A 1 526 ? 26.19   3.029   2.25    1 67.45 ? 526 ARG A O     1 
ATOM   4289  C  CB    . ARG A 1 526 ? 25.644  4.002   5.049   1 69.89 ? 526 ARG A CB    1 
ATOM   4290  C  CG    . ARG A 1 526 ? 25.3    2.68    5.714   1 73.03 ? 526 ARG A CG    1 
ATOM   4291  C  CD    . ARG A 1 526 ? 24.089  2.79    6.613   1 76.17 ? 526 ARG A CD    1 
ATOM   4292  N  NE    . ARG A 1 526 ? 22.882  3.161   5.875   1 79    ? 526 ARG A NE    1 
ATOM   4293  C  CZ    . ARG A 1 526 ? 21.671  3.254   6.418   1 81.39 ? 526 ARG A CZ    1 
ATOM   4294  N  NH1   . ARG A 1 526 ? 21.489  2.988   7.708   1 81.12 ? 526 ARG A NH1   1 
ATOM   4295  N  NH2   . ARG A 1 526 ? 20.629  3.595   5.674   1 81.52 ? 526 ARG A NH2   1 
ATOM   4296  N  N     . PRO A 1 527 ? 27.755  1.839   3.356   1 66.33 ? 527 PRO A N     1 
ATOM   4297  C  CA    . PRO A 1 527 ? 27.762  0.785   2.335   1 65.79 ? 527 PRO A CA    1 
ATOM   4298  C  C     . PRO A 1 527 ? 26.489  -0.044  2.314   1 65.26 ? 527 PRO A C     1 
ATOM   4299  O  O     . PRO A 1 527 ? 25.81   -0.175  3.33    1 65.44 ? 527 PRO A O     1 
ATOM   4300  C  CB    . PRO A 1 527 ? 28.967  -0.086  2.717   1 66.5  ? 527 PRO A CB    1 
ATOM   4301  C  CG    . PRO A 1 527 ? 29.736  0.703   3.73    1 67.04 ? 527 PRO A CG    1 
ATOM   4302  C  CD    . PRO A 1 527 ? 28.725  1.557   4.426   1 65.65 ? 527 PRO A CD    1 
ATOM   4303  N  N     . ASP A 1 528 ? 26.162  -0.593  1.147   1 64.52 ? 528 ASP A N     1 
ATOM   4304  C  CA    . ASP A 1 528 ? 24.989  -1.448  0.992   1 64.3  ? 528 ASP A CA    1 
ATOM   4305  C  C     . ASP A 1 528 ? 25.246  -2.861  1.543   1 63.86 ? 528 ASP A C     1 
ATOM   4306  O  O     . ASP A 1 528 ? 24.299  -3.57   1.849   1 63.74 ? 528 ASP A O     1 
ATOM   4307  C  CB    . ASP A 1 528 ? 24.56   -1.515  -0.479  1 65.72 ? 528 ASP A CB    1 
ATOM   4308  C  CG    . ASP A 1 528 ? 24.174  -0.173  -1.065  1 69.33 ? 528 ASP A CG    1 
ATOM   4309  O  OD1   . ASP A 1 528 ? 23.772  0.717   -0.293  1 69.7  ? 528 ASP A OD1   1 
ATOM   4310  O  OD2   . ASP A 1 528 ? 24.265  -0.019  -2.299  1 71.23 ? 528 ASP A OD2   1 
ATOM   4311  N  N     . HIS A 1 529 ? 26.511  -3.288  1.63    1 63.47 ? 529 HIS A N     1 
ATOM   4312  C  CA    . HIS A 1 529 ? 26.898  -4.588  2.166   1 63.63 ? 529 HIS A CA    1 
ATOM   4313  C  C     . HIS A 1 529 ? 28.285  -4.472  2.77    1 64.1  ? 529 HIS A C     1 
ATOM   4314  O  O     . HIS A 1 529 ? 29.144  -3.852  2.165   1 64.11 ? 529 HIS A O     1 
ATOM   4315  C  CB    . HIS A 1 529 ? 27.007  -5.643  1.048   1 64.01 ? 529 HIS A CB    1 
ATOM   4316  C  CG    . HIS A 1 529 ? 25.807  -5.774  0.169   1 65.6  ? 529 HIS A CG    1 
ATOM   4317  N  ND1   . HIS A 1 529 ? 24.684  -6.452  0.585   1 67.29 ? 529 HIS A ND1   1 
ATOM   4318  C  CD2   . HIS A 1 529 ? 25.612  -5.34   -1.097  1 66.64 ? 529 HIS A CD2   1 
ATOM   4319  C  CE1   . HIS A 1 529 ? 23.835  -6.398  -0.428  1 67.73 ? 529 HIS A CE1   1 
ATOM   4320  N  NE2   . HIS A 1 529 ? 24.351  -5.738  -1.462  1 67.67 ? 529 HIS A NE2   1 
ATOM   4321  N  N     . VAL A 1 530 ? 28.534  -5.09   3.922   1 64.49 ? 530 VAL A N     1 
ATOM   4322  C  CA    . VAL A 1 530 ? 29.887  -5.154  4.481   1 65.34 ? 530 VAL A CA    1 
ATOM   4323  C  C     . VAL A 1 530 ? 30.149  -6.628  4.761   1 66.44 ? 530 VAL A C     1 
ATOM   4324  O  O     . VAL A 1 530 ? 29.475  -7.222  5.595   1 66.52 ? 530 VAL A O     1 
ATOM   4325  C  CB    . VAL A 1 530 ? 30.166  -4.263  5.711   1 65.75 ? 530 VAL A CB    1 
ATOM   4326  C  CG1   . VAL A 1 530 ? 31.614  -4.429  6.166   1 66.19 ? 530 VAL A CG1   1 
ATOM   4327  C  CG2   . VAL A 1 530 ? 29.872  -2.8    5.409   1 66.11 ? 530 VAL A CG2   1 
ATOM   4328  N  N     . ILE A 1 531 ? 31.062  -7.241  4.011   1 67.13 ? 531 ILE A N     1 
ATOM   4329  C  CA    . ILE A 1 531 ? 31.342  -8.668  4.144   1 68.34 ? 531 ILE A CA    1 
ATOM   4330  C  C     . ILE A 1 531 ? 32.648  -8.88   4.869   1 69.4  ? 531 ILE A C     1 
ATOM   4331  O  O     . ILE A 1 531 ? 33.639  -8.25   4.515   1 69.69 ? 531 ILE A O     1 
ATOM   4332  C  CB    . ILE A 1 531 ? 31.389  -9.337  2.746   1 68.97 ? 531 ILE A CB    1 
ATOM   4333  C  CG1   . ILE A 1 531 ? 30.153  -8.98   1.897   1 70.07 ? 531 ILE A CG1   1 
ATOM   4334  C  CG2   . ILE A 1 531 ? 31.589  -10.846 2.85    1 69.37 ? 531 ILE A CG2   1 
ATOM   4335  C  CD1   . ILE A 1 531 ? 28.823  -9.366  2.522   1 71.43 ? 531 ILE A CD1   1 
ATOM   4336  N  N     . GLN A 1 532 ? 32.67   -9.775  5.86    1 69.84 ? 532 GLN A N     1 
ATOM   4337  C  CA    . GLN A 1 532 ? 33.899  -10.05  6.583   1 70.94 ? 532 GLN A CA    1 
ATOM   4338  C  C     . GLN A 1 532 ? 34.453  -11.416 6.243   1 72.09 ? 532 GLN A C     1 
ATOM   4339  O  O     . GLN A 1 532 ? 33.74   -12.406 6.346   1 72.35 ? 532 GLN A O     1 
ATOM   4340  C  CB    . GLN A 1 532 ? 33.703  -9.902  8.089   1 72.39 ? 532 GLN A CB    1 
ATOM   4341  C  CG    . GLN A 1 532 ? 35.003  -10.072 8.861   1 75.19 ? 532 GLN A CG    1 
ATOM   4342  C  CD    . GLN A 1 532 ? 34.903  -9.612  10.29   1 78.75 ? 532 GLN A CD    1 
ATOM   4343  O  OE1   . GLN A 1 532 ? 33.814  -9.394  10.84   1 80.28 ? 532 GLN A OE1   1 
ATOM   4344  N  NE2   . GLN A 1 532 ? 36.051  -9.457  10.924  1 78.89 ? 532 GLN A NE2   1 
ATOM   4345  N  N     . ILE A 1 533 ? 35.72   -11.475 5.816   1 72.66 ? 533 ILE A N     1 
ATOM   4346  C  CA    . ILE A 1 533 ? 36.381  -12.737 5.486   1 73.75 ? 533 ILE A CA    1 
ATOM   4347  C  C     . ILE A 1 533 ? 37.595  -12.893 6.389   1 74.58 ? 533 ILE A C     1 
ATOM   4348  O  O     . ILE A 1 533 ? 38.486  -12.047 6.361   1 74.63 ? 533 ILE A O     1 
ATOM   4349  C  CB    . ILE A 1 533 ? 36.745  -12.797 3.992   1 74.46 ? 533 ILE A CB    1 
ATOM   4350  C  CG1   . ILE A 1 533 ? 35.483  -12.592 3.137   1 75.45 ? 533 ILE A CG1   1 
ATOM   4351  C  CG2   . ILE A 1 533 ? 37.441  -14.119 3.669   1 74.99 ? 533 ILE A CG2   1 
ATOM   4352  C  CD1   . ILE A 1 533 ? 35.702  -12.412 1.732   1 76.65 ? 533 ILE A CD1   1 
ATOM   4353  N  N     . LEU A 1 534 ? 37.623  -13.949 7.21    1 75.09 ? 534 LEU A N     1 
ATOM   4354  C  CA    . LEU A 1 534 ? 38.693  -14.116 8.186   1 76.14 ? 534 LEU A CA    1 
ATOM   4355  C  C     . LEU A 1 534 ? 39.744  -15.171 7.869   1 76.89 ? 534 LEU A C     1 
ATOM   4356  O  O     . LEU A 1 534 ? 40.76   -15.212 8.563   1 77.06 ? 534 LEU A O     1 
ATOM   4357  C  CB    . LEU A 1 534 ? 38.094  -14.39  9.571   1 76.57 ? 534 LEU A CB    1 
ATOM   4358  C  CG    . LEU A 1 534 ? 37.195  -13.28  10.111  1 78.32 ? 534 LEU A CG    1 
ATOM   4359  C  CD1   . LEU A 1 534 ? 35.751  -13.724 10.163  1 78.94 ? 534 LEU A CD1   1 
ATOM   4360  C  CD2   . LEU A 1 534 ? 37.653  -12.809 11.482  1 79.08 ? 534 LEU A CD2   1 
ATOM   4361  N  N     . ASP A 1 535 ? 39.524  -16.018 6.858   1 77.21 ? 535 ASP A N     1 
ATOM   4362  C  CA    . ASP A 1 535 ? 40.496  -17.069 6.546   1 78.11 ? 535 ASP A CA    1 
ATOM   4363  C  C     . ASP A 1 535 ? 41.278  -16.826 5.251   1 78.31 ? 535 ASP A C     1 
ATOM   4364  O  O     . ASP A 1 535 ? 41.75   -17.781 4.63    1 78.49 ? 535 ASP A O     1 
ATOM   4365  C  CB    . ASP A 1 535 ? 39.828  -18.45  6.542   1 80.5  ? 535 ASP A CB    1 
ATOM   4366  C  CG    . ASP A 1 535 ? 38.823  -18.645 5.425   1 86.11 ? 535 ASP A CG    1 
ATOM   4367  O  OD1   . ASP A 1 535 ? 38.245  -17.632 4.959   1 87.02 ? 535 ASP A OD1   1 
ATOM   4368  O  OD2   . ASP A 1 535 ? 38.61   -19.811 5.016   1 88.6  ? 535 ASP A OD2   1 
ATOM   4369  N  N     . LEU A 1 536 ? 41.44   -15.558 4.855   1 78.07 ? 536 LEU A N     1 
ATOM   4370  C  CA    . LEU A 1 536 ? 42.17   -15.233 3.635   1 78.29 ? 536 LEU A CA    1 
ATOM   4371  C  C     . LEU A 1 536 ? 43.513  -14.57  3.959   1 78.32 ? 536 LEU A C     1 
ATOM   4372  O  O     . LEU A 1 536 ? 44.558  -15.068 3.543   1 78.45 ? 536 LEU A O     1 
ATOM   4373  C  CB    . LEU A 1 536 ? 41.294  -14.367 2.718   1 78.58 ? 536 LEU A CB    1 
ATOM   4374  C  CG    . LEU A 1 536 ? 41.91   -13.879 1.411   1 80.18 ? 536 LEU A CG    1 
ATOM   4375  C  CD1   . LEU A 1 536 ? 42.415  -15.034 0.561   1 80.72 ? 536 LEU A CD1   1 
ATOM   4376  C  CD2   . LEU A 1 536 ? 40.9    -13.086 0.622   1 80.92 ? 536 LEU A CD2   1 
ATOM   4377  N  N     . PHE A 1 537 ? 43.493  -13.479 4.727   1 78.1  ? 537 PHE A N     1 
ATOM   4378  C  CA    . PHE A 1 537 ? 44.716  -12.791 5.137   1 78.47 ? 537 PHE A CA    1 
ATOM   4379  C  C     . PHE A 1 537 ? 44.91   -12.923 6.663   1 78.43 ? 537 PHE A C     1 
ATOM   4380  O  O     . PHE A 1 537 ? 43.987  -13.346 7.365   1 78.58 ? 537 PHE A O     1 
ATOM   4381  C  CB    . PHE A 1 537 ? 44.649  -11.3   4.746   1 78.61 ? 537 PHE A CB    1 
ATOM   4382  C  CG    . PHE A 1 537 ? 44.332  -11.027 3.295   1 79.43 ? 537 PHE A CG    1 
ATOM   4383  C  CD1   . PHE A 1 537 ? 45.24   -11.339 2.297   1 80.27 ? 537 PHE A CD1   1 
ATOM   4384  C  CD2   . PHE A 1 537 ? 43.144  -10.42  2.933   1 80.3  ? 537 PHE A CD2   1 
ATOM   4385  C  CE1   . PHE A 1 537 ? 44.95   -11.078 0.962   1 81.02 ? 537 PHE A CE1   1 
ATOM   4386  C  CE2   . PHE A 1 537 ? 42.86   -10.154 1.598   1 81.07 ? 537 PHE A CE2   1 
ATOM   4387  C  CZ    . PHE A 1 537 ? 43.763  -10.487 0.621   1 80.87 ? 537 PHE A CZ    1 
ATOM   4388  N  N     . GLU A 1 538 ? 46.095  -12.538 7.187   1 78.03 ? 538 GLU A N     1 
ATOM   4389  C  CA    . GLU A 1 538 ? 46.336  -12.57  8.632   1 78.04 ? 538 GLU A CA    1 
ATOM   4390  C  C     . GLU A 1 538 ? 45.364  -11.62  9.351   1 77.63 ? 538 GLU A C     1 
ATOM   4391  O  O     . GLU A 1 538 ? 44.817  -11.963 10.397  1 77.81 ? 538 GLU A O     1 
ATOM   4392  C  CB    . GLU A 1 538 ? 47.806  -12.261 8.982   1 80.36 ? 538 GLU A CB    1 
ATOM   4393  C  CG    . GLU A 1 538 ? 48.405  -11.037 8.299   1 84.97 ? 538 GLU A CG    1 
ATOM   4394  C  CD    . GLU A 1 538 ? 49.131  -11.302 6.992   1 90.75 ? 538 GLU A CD    1 
ATOM   4395  O  OE1   . GLU A 1 538 ? 49.476  -10.318 6.301   1 91.76 ? 538 GLU A OE1   1 
ATOM   4396  O  OE2   . GLU A 1 538 ? 49.345  -12.488 6.652   1 92.8  ? 538 GLU A OE2   1 
ATOM   4397  N  N     . LYS A 1 539 ? 45.114  -10.452 8.755   1 76.95 ? 539 LYS A N     1 
ATOM   4398  C  CA    . LYS A 1 539 ? 44.149  -9.494  9.265   1 76.82 ? 539 LYS A CA    1 
ATOM   4399  C  C     . LYS A 1 539 ? 42.808  -9.811  8.609   1 76.27 ? 539 LYS A C     1 
ATOM   4400  O  O     . LYS A 1 539 ? 42.766  -10.183 7.43    1 76.31 ? 539 LYS A O     1 
ATOM   4401  C  CB    . LYS A 1 539 ? 44.56   -8.065  8.882   1 78.7  ? 539 LYS A CB    1 
ATOM   4402  C  CG    . LYS A 1 539 ? 45.852  -7.589  9.514   1 82.69 ? 539 LYS A CG    1 
ATOM   4403  C  CD    . LYS A 1 539 ? 46.115  -6.141  9.14    1 86.69 ? 539 LYS A CD    1 
ATOM   4404  C  CE    . LYS A 1 539 ? 47.292  -5.566  9.885   1 90.07 ? 539 LYS A CE    1 
ATOM   4405  N  NZ    . LYS A 1 539 ? 47.571  -4.169  9.468   1 92.03 ? 539 LYS A NZ    1 
ATOM   4406  N  N     . PRO A 1 540 ? 41.694  -9.652  9.338   1 75.58 ? 540 PRO A N     1 
ATOM   4407  C  CA    . PRO A 1 540 ? 40.384  -9.906  8.721   1 75.11 ? 540 PRO A CA    1 
ATOM   4408  C  C     . PRO A 1 540 ? 40.087  -8.897  7.614   1 74.41 ? 540 PRO A C     1 
ATOM   4409  O  O     . PRO A 1 540 ? 40.496  -7.742  7.705   1 74.49 ? 540 PRO A O     1 
ATOM   4410  C  CB    . PRO A 1 540 ? 39.398  -9.759  9.889   1 76    ? 540 PRO A CB    1 
ATOM   4411  C  CG    . PRO A 1 540 ? 40.232  -9.749  11.132  1 76.57 ? 540 PRO A CG    1 
ATOM   4412  C  CD    . PRO A 1 540 ? 41.561  -9.203  10.736  1 75.05 ? 540 PRO A CD    1 
ATOM   4413  N  N     . LEU A 1 541 ? 39.403  -9.335  6.559   1 73.56 ? 541 LEU A N     1 
ATOM   4414  C  CA    . LEU A 1 541 ? 39.053  -8.452  5.453   1 73.29 ? 541 LEU A CA    1 
ATOM   4415  C  C     . LEU A 1 541 ? 37.637  -7.915  5.645   1 72.66 ? 541 LEU A C     1 
ATOM   4416  O  O     . LEU A 1 541 ? 36.729  -8.687  5.919   1 72.9  ? 541 LEU A O     1 
ATOM   4417  C  CB    . LEU A 1 541 ? 39.155  -9.209  4.107   1 73.5  ? 541 LEU A CB    1 
ATOM   4418  C  CG    . LEU A 1 541 ? 38.472  -8.558  2.889   1 74.86 ? 541 LEU A CG    1 
ATOM   4419  C  CD1   . LEU A 1 541 ? 39.212  -7.344  2.439   1 75.34 ? 541 LEU A CD1   1 
ATOM   4420  C  CD2   . LEU A 1 541 ? 38.286  -9.536  1.771   1 75.51 ? 541 LEU A CD2   1 
ATOM   4421  N  N     . LEU A 1 542 ? 37.445  -6.611  5.447   1 71.62 ? 542 LEU A N     1 
ATOM   4422  C  CA    . LEU A 1 542 ? 36.126  -6.005  5.469   1 71.03 ? 542 LEU A CA    1 
ATOM   4423  C  C     . LEU A 1 542 ? 35.914  -5.453  4.074   1 70.18 ? 542 LEU A C     1 
ATOM   4424  O  O     . LEU A 1 542 ? 36.618  -4.54   3.654   1 70.42 ? 542 LEU A O     1 
ATOM   4425  C  CB    . LEU A 1 542 ? 36.032  -4.889  6.509   1 71.24 ? 542 LEU A CB    1 
ATOM   4426  C  CG    . LEU A 1 542 ? 36.125  -5.345  7.951   1 72.87 ? 542 LEU A CG    1 
ATOM   4427  C  CD1   . LEU A 1 542 ? 36.196  -4.163  8.887   1 73.5  ? 542 LEU A CD1   1 
ATOM   4428  C  CD2   . LEU A 1 542 ? 34.963  -6.255  8.315   1 73.6  ? 542 LEU A CD2   1 
ATOM   4429  N  N     . LEU A 1 543 ? 35.003  -6.062  3.329   1 69.02 ? 543 LEU A N     1 
ATOM   4430  C  CA    . LEU A 1 543 ? 34.711  -5.657  1.967   1 68.44 ? 543 LEU A CA    1 
ATOM   4431  C  C     . LEU A 1 543 ? 33.421  -4.854  1.959   1 67.8  ? 543 LEU A C     1 
ATOM   4432  O  O     . LEU A 1 543 ? 32.36   -5.405  2.231   1 68.02 ? 543 LEU A O     1 
ATOM   4433  C  CB    . LEU A 1 543 ? 34.562  -6.905  1.092   1 68.51 ? 543 LEU A CB    1 
ATOM   4434  C  CG    . LEU A 1 543 ? 34.218  -6.654  -0.363  1 69.79 ? 543 LEU A CG    1 
ATOM   4435  C  CD1   . LEU A 1 543 ? 35.336  -5.906  -1.058  1 70.39 ? 543 LEU A CD1   1 
ATOM   4436  C  CD2   . LEU A 1 543 ? 33.93   -7.951  -1.076  1 70.34 ? 543 LEU A CD2   1 
ATOM   4437  N  N     . SER A 1 544 ? 33.507  -3.55   1.68    1 66.85 ? 544 SER A N     1 
ATOM   4438  C  CA    . SER A 1 544 ? 32.333  -2.684  1.64    1 66.31 ? 544 SER A CA    1 
ATOM   4439  C  C     . SER A 1 544 ? 31.841  -2.589  0.212   1 65.61 ? 544 SER A C     1 
ATOM   4440  O  O     . SER A 1 544 ? 32.597  -2.204  -0.665  1 65.74 ? 544 SER A O     1 
ATOM   4441  C  CB    . SER A 1 544 ? 32.672  -1.299  2.173   1 67.37 ? 544 SER A CB    1 
ATOM   4442  O  OG    . SER A 1 544 ? 32.975  -1.358  3.556   1 69.39 ? 544 SER A OG    1 
ATOM   4443  N  N     . ILE A 1 545 ? 30.587  -2.955  -0.029  1 64.79 ? 545 ILE A N     1 
ATOM   4444  C  CA    . ILE A 1 545 ? 30.011  -2.993  -1.368  1 64.51 ? 545 ILE A CA    1 
ATOM   4445  C  C     . ILE A 1 545 ? 28.874  -1.993  -1.553  1 63.91 ? 545 ILE A C     1 
ATOM   4446  O  O     . ILE A 1 545 ? 27.997  -1.884  -0.7    1 63.94 ? 545 ILE A O     1 
ATOM   4447  C  CB    . ILE A 1 545 ? 29.519  -4.438  -1.689  1 65.05 ? 545 ILE A CB    1 
ATOM   4448  C  CG1   . ILE A 1 545 ? 30.575  -5.514  -1.351  1 66.02 ? 545 ILE A CG1   1 
ATOM   4449  C  CG2   . ILE A 1 545 ? 29.049  -4.564  -3.132  1 65.52 ? 545 ILE A CG2   1 
ATOM   4450  C  CD1   . ILE A 1 545 ? 30.045  -6.93   -1.384  1 67.38 ? 545 ILE A CD1   1 
ATOM   4451  N  N     . GLU A 1 546 ? 28.879  -1.28   -2.68   1 63.21 ? 546 GLU A N     1 
ATOM   4452  C  CA    . GLU A 1 546 ? 27.802  -0.371  -3.046  1 63.08 ? 546 GLU A CA    1 
ATOM   4453  C  C     . GLU A 1 546 ? 27.207  -0.948  -4.32   1 62.37 ? 546 GLU A C     1 
ATOM   4454  O  O     . GLU A 1 546 ? 27.938  -1.208  -5.273  1 62.35 ? 546 GLU A O     1 
ATOM   4455  C  CB    . GLU A 1 546 ? 28.322  1.05    -3.287  1 65.68 ? 546 GLU A CB    1 
ATOM   4456  C  CG    . GLU A 1 546 ? 27.229  2.081   -3.515  1 71.32 ? 546 GLU A CG    1 
ATOM   4457  C  CD    . GLU A 1 546 ? 26.765  2.839   -2.283  1 78.66 ? 546 GLU A CD    1 
ATOM   4458  O  OE1   . GLU A 1 546 ? 26.794  2.258   -1.174  1 79.79 ? 546 GLU A OE1   1 
ATOM   4459  O  OE2   . GLU A 1 546 ? 26.361  4.016   -2.429  1 81.22 ? 546 GLU A OE2   1 
ATOM   4460  N  N     . SER A 1 547 ? 25.901  -1.214  -4.318  1 61.65 ? 547 SER A N     1 
ATOM   4461  C  CA    . SER A 1 547 ? 25.236  -1.826  -5.462  1 61.32 ? 547 SER A CA    1 
ATOM   4462  C  C     . SER A 1 547 ? 24.395  -0.817  -6.215  1 60.36 ? 547 SER A C     1 
ATOM   4463  O  O     . SER A 1 547 ? 23.727  0.01    -5.602  1 60.55 ? 547 SER A O     1 
ATOM   4464  C  CB    . SER A 1 547 ? 24.354  -2.983  -5.003  1 62.83 ? 547 SER A CB    1 
ATOM   4465  O  OG    . SER A 1 547 ? 23.418  -2.535  -4.037  1 65.13 ? 547 SER A OG    1 
ATOM   4466  N  N     . LYS A 1 548 ? 24.439  -0.876  -7.543  1 59.19 ? 548 LYS A N     1 
ATOM   4467  C  CA    . LYS A 1 548 ? 23.675  0       -8.425  1 58.56 ? 548 LYS A CA    1 
ATOM   4468  C  C     . LYS A 1 548 ? 23.109  -0.823  -9.603  1 57.87 ? 548 LYS A C     1 
ATOM   4469  O  O     . LYS A 1 548 ? 23.533  -1.961  -9.825  1 57.9  ? 548 LYS A O     1 
ATOM   4470  C  CB    . LYS A 1 548 ? 24.572  1.135   -8.956  1 60.12 ? 548 LYS A CB    1 
ATOM   4471  C  CG    . LYS A 1 548 ? 25.036  2.135   -7.902  1 64.04 ? 548 LYS A CG    1 
ATOM   4472  C  CD    . LYS A 1 548 ? 23.882  2.925   -7.291  1 68.19 ? 548 LYS A CD    1 
ATOM   4473  C  CE    . LYS A 1 548 ? 24.215  3.515   -5.935  1 71.01 ? 548 LYS A CE    1 
ATOM   4474  N  NZ    . LYS A 1 548 ? 25.036  4.746   -6.029  1 72.53 ? 548 LYS A NZ    1 
ATOM   4475  N  N     . GLU A 1 549 ? 22.149  -0.259  -10.351 1 57.09 ? 549 GLU A N     1 
ATOM   4476  C  CA    . GLU A 1 549 ? 21.594  -0.956  -11.51  1 56.75 ? 549 GLU A CA    1 
ATOM   4477  C  C     . GLU A 1 549 ? 22.614  -0.929  -12.643 1 56.57 ? 549 GLU A C     1 
ATOM   4478  O  O     . GLU A 1 549 ? 22.862  -1.955  -13.268 1 56.66 ? 549 GLU A O     1 
ATOM   4479  C  CB    . GLU A 1 549 ? 20.267  -0.323  -11.964 1 58.01 ? 549 GLU A CB    1 
ATOM   4480  C  CG    . GLU A 1 549 ? 19.664  -0.998  -13.183 1 60.17 ? 549 GLU A CG    1 
ATOM   4481  C  CD    . GLU A 1 549 ? 18.213  -0.657  -13.45  1 63.4  ? 549 GLU A CD    1 
ATOM   4482  O  OE1   . GLU A 1 549 ? 17.528  -0.189  -12.513 1 63.96 ? 549 GLU A OE1   1 
ATOM   4483  O  OE2   . GLU A 1 549 ? 17.751  -0.878  -14.591 1 64.73 ? 549 GLU A OE2   1 
ATOM   4484  N  N     . LYS A 1 550 ? 23.237  0.234   -12.882 1 56.24 ? 550 LYS A N     1 
ATOM   4485  C  CA    . LYS A 1 550 ? 24.207  0.402   -13.959 1 56.44 ? 550 LYS A CA    1 
ATOM   4486  C  C     . LYS A 1 550 ? 25.575  0.876   -13.463 1 56.65 ? 550 LYS A C     1 
ATOM   4487  O  O     . LYS A 1 550 ? 25.653  1.551   -12.442 1 56.55 ? 550 LYS A O     1 
ATOM   4488  C  CB    . LYS A 1 550 ? 23.643  1.382   -15     1 58.02 ? 550 LYS A CB    1 
ATOM   4489  C  CG    . LYS A 1 550 ? 22.346  0.894   -15.635 1 61.88 ? 550 LYS A CG    1 
ATOM   4490  C  CD    . LYS A 1 550 ? 21.981  1.688   -16.864 1 66.1  ? 550 LYS A CD    1 
ATOM   4491  C  CE    . LYS A 1 550 ? 20.705  1.195   -17.492 1 69.78 ? 550 LYS A CE    1 
ATOM   4492  N  NZ    . LYS A 1 550 ? 20.896  -0.09   -18.212 1 72.09 ? 550 LYS A NZ    1 
ATOM   4493  N  N     . PRO A 1 551 ? 26.669  0.572   -14.191 1 56.91 ? 551 PRO A N     1 
ATOM   4494  C  CA    . PRO A 1 551 ? 27.998  1.03    -13.739 1 57.22 ? 551 PRO A CA    1 
ATOM   4495  C  C     . PRO A 1 551 ? 28.153  2.552   -13.698 1 57.65 ? 551 PRO A C     1 
ATOM   4496  O  O     . PRO A 1 551 ? 28.897  3.07    -12.867 1 57.69 ? 551 PRO A O     1 
ATOM   4497  C  CB    . PRO A 1 551 ? 28.972  0.372   -14.728 1 57.8  ? 551 PRO A CB    1 
ATOM   4498  C  CG    . PRO A 1 551 ? 28.154  0.017   -15.911 1 58.13 ? 551 PRO A CG    1 
ATOM   4499  C  CD    . PRO A 1 551 ? 26.759  -0.234  -15.425 1 56.48 ? 551 PRO A CD    1 
ATOM   4500  N  N     . ASN A 1 552 ? 27.427  3.273   -14.568 1 57.81 ? 552 ASN A N     1 
ATOM   4501  C  CA    . ASN A 1 552 ? 27.453  4.74    -14.588 1 58.36 ? 552 ASN A CA    1 
ATOM   4502  C  C     . ASN A 1 552 ? 26.775  5.365   -13.354 1 58.54 ? 552 ASN A C     1 
ATOM   4503  O  O     . ASN A 1 552 ? 27.003  6.538   -13.067 1 58.62 ? 552 ASN A O     1 
ATOM   4504  C  CB    . ASN A 1 552 ? 26.833  5.276   -15.876 1 59.8  ? 552 ASN A CB    1 
ATOM   4505  C  CG    . ASN A 1 552 ? 27.639  4.935   -17.1   1 63.8  ? 552 ASN A CG    1 
ATOM   4506  O  OD1   . ASN A 1 552 ? 28.866  4.803   -17.041 1 65.34 ? 552 ASN A OD1   1 
ATOM   4507  N  ND2   . ASN A 1 552 ? 26.97   4.781   -18.237 1 64.57 ? 552 ASN A ND2   1 
ATOM   4508  N  N     . ASP A 1 553 ? 25.953  4.586   -12.624 1 58.48 ? 553 ASP A N     1 
ATOM   4509  C  CA    . ASP A 1 553 ? 25.288  5.039   -11.403 1 58.86 ? 553 ASP A CA    1 
ATOM   4510  C  C     . ASP A 1 553 ? 26.256  5.125   -10.205 1 58.62 ? 553 ASP A C     1 
ATOM   4511  O  O     . ASP A 1 553 ? 25.914  5.748   -9.204  1 58.72 ? 553 ASP A O     1 
ATOM   4512  C  CB    . ASP A 1 553 ? 24.094  4.129   -11.054 1 60.99 ? 553 ASP A CB    1 
ATOM   4513  C  CG    . ASP A 1 553 ? 23.044  4.04    -12.142 1 66.42 ? 553 ASP A CG    1 
ATOM   4514  O  OD1   . ASP A 1 553 ? 22.929  5.003   -12.936 1 67.41 ? 553 ASP A OD1   1 
ATOM   4515  O  OD2   . ASP A 1 553 ? 22.333  3.007   -12.199 1 68.75 ? 553 ASP A OD2   1 
ATOM   4516  N  N     . LEU A 1 554 ? 27.443  4.487   -10.289 1 58.15 ? 554 LEU A N     1 
ATOM   4517  C  CA    . LEU A 1 554 ? 28.436  4.543   -9.22   1 58.13 ? 554 LEU A CA    1 
ATOM   4518  C  C     . LEU A 1 554 ? 28.985  5.963   -9.166  1 58.44 ? 554 LEU A C     1 
ATOM   4519  O  O     . LEU A 1 554 ? 29.59   6.434   -10.13  1 58.53 ? 554 LEU A O     1 
ATOM   4520  C  CB    . LEU A 1 554 ? 29.565  3.534   -9.464  1 57.97 ? 554 LEU A CB    1 
ATOM   4521  C  CG    . LEU A 1 554 ? 29.181  2.066   -9.333  1 58.95 ? 554 LEU A CG    1 
ATOM   4522  C  CD1   . LEU A 1 554 ? 30.316  1.171   -9.767  1 59.32 ? 554 LEU A CD1   1 
ATOM   4523  C  CD2   . LEU A 1 554 ? 28.785  1.737   -7.923  1 59.51 ? 554 LEU A CD2   1 
ATOM   4524  N  N     . GLU A 1 555 ? 28.704  6.662   -8.063  1 58.47 ? 555 GLU A N     1 
ATOM   4525  C  CA    . GLU A 1 555 ? 29.086  8.055   -7.855  1 59.08 ? 555 GLU A CA    1 
ATOM   4526  C  C     . GLU A 1 555 ? 30.592  8.264   -7.786  1 59.04 ? 555 GLU A C     1 
ATOM   4527  O  O     . GLU A 1 555 ? 31.318  7.378   -7.343  1 59.3  ? 555 GLU A O     1 
ATOM   4528  C  CB    . GLU A 1 555 ? 28.425  8.587   -6.571  1 61.69 ? 555 GLU A CB    1 
ATOM   4529  C  CG    . GLU A 1 555 ? 26.91   8.579   -6.619  1 66.89 ? 555 GLU A CG    1 
ATOM   4530  C  CD    . GLU A 1 555 ? 26.245  7.471   -5.827  1 73.79 ? 555 GLU A CD    1 
ATOM   4531  O  OE1   . GLU A 1 555 ? 26.957  6.585   -5.301  1 75.02 ? 555 GLU A OE1   1 
ATOM   4532  O  OE2   . GLU A 1 555 ? 24.998  7.499   -5.724  1 76.38 ? 555 GLU A OE2   1 
ATOM   4533  N  N     . PRO A 1 556 ? 31.084  9.45    -8.181  1 58.52 ? 556 PRO A N     1 
ATOM   4534  C  CA    . PRO A 1 556 ? 32.527  9.707   -8.084  1 58.29 ? 556 PRO A CA    1 
ATOM   4535  C  C     . PRO A 1 556 ? 33.018  9.606   -6.64   1 58.06 ? 556 PRO A C     1 
ATOM   4536  O  O     . PRO A 1 556 ? 32.356  10.094  -5.723  1 57.96 ? 556 PRO A O     1 
ATOM   4537  C  CB    . PRO A 1 556 ? 32.675  11.127  -8.639  1 59.1  ? 556 PRO A CB    1 
ATOM   4538  C  CG    . PRO A 1 556 ? 31.438  11.357  -9.455  1 59.57 ? 556 PRO A CG    1 
ATOM   4539  C  CD    . PRO A 1 556 ? 30.363  10.612  -8.733  1 57.99 ? 556 PRO A CD    1 
ATOM   4540  N  N     . LYS A 1 557 ? 34.136  8.889   -6.448  1 57.77 ? 557 LYS A N     1 
ATOM   4541  C  CA    . LYS A 1 557 ? 34.777  8.628   -5.157  1 57.9  ? 557 LYS A CA    1 
ATOM   4542  C  C     . LYS A 1 557 ? 33.95   7.751   -4.223  1 57.64 ? 557 LYS A C     1 
ATOM   4543  O  O     . LYS A 1 557 ? 34.219  7.746   -3.025  1 57.79 ? 557 LYS A O     1 
ATOM   4544  C  CB    . LYS A 1 557 ? 35.204  9.926   -4.447  1 59.91 ? 557 LYS A CB    1 
ATOM   4545  C  CG    . LYS A 1 557 ? 36.173  10.763  -5.266  1 64.49 ? 557 LYS A CG    1 
ATOM   4546  C  CD    . LYS A 1 557 ? 36.472  12.101  -4.616  1 68.93 ? 557 LYS A CD    1 
ATOM   4547  C  CE    . LYS A 1 557 ? 37.29   11.942  -3.36   1 72.77 ? 557 LYS A CE    1 
ATOM   4548  N  NZ    . LYS A 1 557 ? 37.786  13.248  -2.857  1 75.24 ? 557 LYS A NZ    1 
ATOM   4549  N  N     . ILE A 1 558 ? 32.98   6.978   -4.757  1 57.12 ? 558 ILE A N     1 
ATOM   4550  C  CA    . ILE A 1 558 ? 32.155  6.109   -3.919  1 57.12 ? 558 ILE A CA    1 
ATOM   4551  C  C     . ILE A 1 558 ? 33.007  5.067   -3.196  1 57.15 ? 558 ILE A C     1 
ATOM   4552  O  O     . ILE A 1 558 ? 32.79   4.834   -2.012  1 57.31 ? 558 ILE A O     1 
ATOM   4553  C  CB    . ILE A 1 558 ? 30.944  5.483   -4.668  1 57.49 ? 558 ILE A CB    1 
ATOM   4554  C  CG1   . ILE A 1 558 ? 29.959  4.813   -3.693  1 58.35 ? 558 ILE A CG1   1 
ATOM   4555  C  CG2   . ILE A 1 558 ? 31.381  4.502   -5.75   1 57.92 ? 558 ILE A CG2   1 
ATOM   4556  C  CD1   . ILE A 1 558 ? 29.387  5.711   -2.678  1 59.63 ? 558 ILE A CD1   1 
ATOM   4557  N  N     . GLY A 1 559 ? 34.019  4.53    -3.874  1 56.83 ? 559 GLY A N     1 
ATOM   4558  C  CA    . GLY A 1 559 ? 34.927  3.549   -3.293  1 57.04 ? 559 GLY A CA    1 
ATOM   4559  C  C     . GLY A 1 559 ? 35.65   4.084   -2.075  1 57.12 ? 559 GLY A C     1 
ATOM   4560  O  O     . GLY A 1 559 ? 35.665  3.441   -1.024  1 57.23 ? 559 GLY A O     1 
ATOM   4561  N  N     . VAL A 1 560 ? 36.195  5.298   -2.189  1 56.95 ? 560 VAL A N     1 
ATOM   4562  C  CA    . VAL A 1 560 ? 36.89   5.946   -1.082  1 57.2  ? 560 VAL A CA    1 
ATOM   4563  C  C     . VAL A 1 560 ? 35.922  6.286   0.062   1 57.38 ? 560 VAL A C     1 
ATOM   4564  O  O     . VAL A 1 560 ? 36.238  6.04    1.226   1 57.33 ? 560 VAL A O     1 
ATOM   4565  C  CB    . VAL A 1 560 ? 37.671  7.181   -1.582  1 57.87 ? 560 VAL A CB    1 
ATOM   4566  C  CG1   . VAL A 1 560 ? 38.373  7.894   -0.43   1 58.48 ? 560 VAL A CG1   1 
ATOM   4567  C  CG2   . VAL A 1 560 ? 38.667  6.784   -2.664  1 58.27 ? 560 VAL A CG2   1 
ATOM   4568  N  N     . GLN A 1 561 ? 34.721  6.781   -0.278  1 57.45 ? 561 GLN A N     1 
ATOM   4569  C  CA    . GLN A 1 561 ? 33.696  7.131   0.705   1 58.04 ? 561 GLN A CA    1 
ATOM   4570  C  C     . GLN A 1 561 ? 33.222  5.928   1.521   1 58.73 ? 561 GLN A C     1 
ATOM   4571  O  O     . GLN A 1 561 ? 32.903  6.082   2.699   1 58.92 ? 561 GLN A O     1 
ATOM   4572  C  CB    . GLN A 1 561 ? 32.501  7.817   0.032   1 59.19 ? 561 GLN A CB    1 
ATOM   4573  C  CG    . GLN A 1 561 ? 32.815  9.198   -0.509  1 61.67 ? 561 GLN A CG    1 
ATOM   4574  C  CD    . GLN A 1 561 ? 31.626  9.768   -1.233  1 65.14 ? 561 GLN A CD    1 
ATOM   4575  O  OE1   . GLN A 1 561 ? 31.491  9.649   -2.455  1 66.36 ? 561 GLN A OE1   1 
ATOM   4576  N  NE2   . GLN A 1 561 ? 30.728  10.393  -0.489  1 65.53 ? 561 GLN A NE2   1 
ATOM   4577  N  N     . LEU A 1 562 ? 33.183  4.738   0.912   1 58.99 ? 562 LEU A N     1 
ATOM   4578  C  CA    . LEU A 1 562 ? 32.772  3.536   1.63    1 59.81 ? 562 LEU A CA    1 
ATOM   4579  C  C     . LEU A 1 562 ? 33.782  3.207   2.727   1 60.53 ? 562 LEU A C     1 
ATOM   4580  O  O     . LEU A 1 562 ? 33.386  2.898   3.851   1 60.67 ? 562 LEU A O     1 
ATOM   4581  C  CB    . LEU A 1 562 ? 32.619  2.345   0.673   1 60.02 ? 562 LEU A CB    1 
ATOM   4582  C  CG    . LEU A 1 562 ? 31.533  2.454   -0.389  1 61.4  ? 562 LEU A CG    1 
ATOM   4583  C  CD1   . LEU A 1 562 ? 31.494  1.211   -1.245  1 61.88 ? 562 LEU A CD1   1 
ATOM   4584  C  CD2   . LEU A 1 562 ? 30.17   2.737   0.221   1 62.16 ? 562 LEU A CD2   1 
ATOM   4585  N  N     . ILE A 1 563 ? 35.082  3.318   2.409   1 60.78 ? 563 ILE A N     1 
ATOM   4586  C  CA    . ILE A 1 563 ? 36.158  3.056   3.361   1 61.51 ? 563 ILE A CA    1 
ATOM   4587  C  C     . ILE A 1 563 ? 36.114  4.084   4.489   1 62.36 ? 563 ILE A C     1 
ATOM   4588  O  O     . ILE A 1 563 ? 36.195  3.718   5.664   1 62.55 ? 563 ILE A O     1 
ATOM   4589  C  CB    . ILE A 1 563 ? 37.525  3.053   2.636   1 61.86 ? 563 ILE A CB    1 
ATOM   4590  C  CG1   . ILE A 1 563 ? 37.563  1.997   1.516   1 62.66 ? 563 ILE A CG1   1 
ATOM   4591  C  CG2   . ILE A 1 563 ? 38.678  2.872   3.619   1 62.35 ? 563 ILE A CG2   1 
ATOM   4592  C  CD1   . ILE A 1 563 ? 37.383  0.592   1.977   1 63.88 ? 563 ILE A CD1   1 
ATOM   4593  N  N     . LYS A 1 564 ? 35.921  5.362   4.132   1 62.64 ? 564 LYS A N     1 
ATOM   4594  C  CA    . LYS A 1 564 ? 35.845  6.442   5.11    1 63.42 ? 564 LYS A CA    1 
ATOM   4595  C  C     . LYS A 1 564 ? 34.657  6.295   6.058   1 64.09 ? 564 LYS A C     1 
ATOM   4596  O  O     . LYS A 1 564 ? 34.746  6.744   7.197   1 64.29 ? 564 LYS A O     1 
ATOM   4597  C  CB    . LYS A 1 564 ? 35.83   7.816   4.423   1 65.35 ? 564 LYS A CB    1 
ATOM   4598  C  CG    . LYS A 1 564 ? 37.079  8.122   3.595   1 69.72 ? 564 LYS A CG    1 
ATOM   4599  C  CD    . LYS A 1 564 ? 38.355  8.157   4.43    1 74.27 ? 564 LYS A CD    1 
ATOM   4600  C  CE    . LYS A 1 564 ? 39.56   8.559   3.608   1 78.16 ? 564 LYS A CE    1 
ATOM   4601  N  NZ    . LYS A 1 564 ? 39.953  7.507   2.631   1 80.58 ? 564 LYS A NZ    1 
ATOM   4602  N  N     . TYR A 1 565 ? 33.563  5.654   5.615   1 64.34 ? 565 TYR A N     1 
ATOM   4603  C  CA    . TYR A 1 565 ? 32.409  5.438   6.489   1 65.16 ? 565 TYR A CA    1 
ATOM   4604  C  C     . TYR A 1 565 ? 32.757  4.422   7.569   1 65.69 ? 565 TYR A C     1 
ATOM   4605  O  O     . TYR A 1 565 ? 32.39   4.611   8.727   1 65.83 ? 565 TYR A O     1 
ATOM   4606  C  CB    . TYR A 1 565 ? 31.185  4.961   5.705   1 65.33 ? 565 TYR A CB    1 
ATOM   4607  C  CG    . TYR A 1 565 ? 29.906  4.99    6.518   1 66.15 ? 565 TYR A CG    1 
ATOM   4608  C  CD1   . TYR A 1 565 ? 29.145  6.146   6.614   1 66.99 ? 565 TYR A CD1   1 
ATOM   4609  C  CD2   . TYR A 1 565 ? 29.456  3.859   7.184   1 67.08 ? 565 TYR A CD2   1 
ATOM   4610  C  CE1   . TYR A 1 565 ? 27.967  6.177   7.349   1 67.87 ? 565 TYR A CE1   1 
ATOM   4611  C  CE2   . TYR A 1 565 ? 28.286  3.882   7.934   1 67.96 ? 565 TYR A CE2   1 
ATOM   4612  C  CZ    . TYR A 1 565 ? 27.541  5.042   8.008   1 68.84 ? 565 TYR A CZ    1 
ATOM   4613  O  OH    . TYR A 1 565 ? 26.376  5.069   8.735   1 70.38 ? 565 TYR A OH    1 
ATOM   4614  N  N     . ILE A 1 566 ? 33.471  3.351   7.197   1 65.87 ? 566 ILE A N     1 
ATOM   4615  C  CA    . ILE A 1 566 ? 33.904  2.328   8.147   1 66.61 ? 566 ILE A CA    1 
ATOM   4616  C  C     . ILE A 1 566 ? 34.883  2.953   9.148   1 67.47 ? 566 ILE A C     1 
ATOM   4617  O  O     . ILE A 1 566 ? 34.765  2.721   10.351  1 67.41 ? 566 ILE A O     1 
ATOM   4618  C  CB    . ILE A 1 566 ? 34.523  1.123   7.394   1 67    ? 566 ILE A CB    1 
ATOM   4619  C  CG1   . ILE A 1 566 ? 33.544  0.56    6.356   1 67.91 ? 566 ILE A CG1   1 
ATOM   4620  C  CG2   . ILE A 1 566 ? 34.988  0.038   8.35    1 67.35 ? 566 ILE A CG2   1 
ATOM   4621  C  CD1   . ILE A 1 566 ? 32.236  0.059   6.93    1 69.12 ? 566 ILE A CD1   1 
ATOM   4622  N  N     . GLU A 1 567 ? 35.803  3.799   8.652   1 68.09 ? 567 GLU A N     1 
ATOM   4623  C  CA    . GLU A 1 567 ? 36.77   4.509   9.485   1 69.15 ? 567 GLU A CA    1 
ATOM   4624  C  C     . GLU A 1 567 ? 36.068  5.44    10.485  1 69.84 ? 567 GLU A C     1 
ATOM   4625  O  O     . GLU A 1 567 ? 36.523  5.572   11.619  1 69.9  ? 567 GLU A O     1 
ATOM   4626  C  CB    . GLU A 1 567 ? 37.756  5.289   8.605   1 71.52 ? 567 GLU A CB    1 
ATOM   4627  C  CG    . GLU A 1 567 ? 38.627  4.377   7.759   1 76.11 ? 567 GLU A CG    1 
ATOM   4628  C  CD    . GLU A 1 567 ? 39.712  5.061   6.954   1 82.38 ? 567 GLU A CD    1 
ATOM   4629  O  OE1   . GLU A 1 567 ? 39.783  6.312   6.979   1 83.73 ? 567 GLU A OE1   1 
ATOM   4630  O  OE2   . GLU A 1 567 ? 40.495  4.342   6.294   1 84.44 ? 567 GLU A OE2   1 
ATOM   4631  N  N     . TYR A 1 568 ? 34.941  6.046   10.073  1 70.17 ? 568 TYR A N     1 
ATOM   4632  C  CA    . TYR A 1 568 ? 34.114  6.932   10.892  1 70.91 ? 568 TYR A CA    1 
ATOM   4633  C  C     . TYR A 1 568 ? 33.527  6.168   12.078  1 70.95 ? 568 TYR A C     1 
ATOM   4634  O  O     . TYR A 1 568 ? 33.609  6.65    13.202  1 70.87 ? 568 TYR A O     1 
ATOM   4635  C  CB    . TYR A 1 568 ? 33.015  7.575   10.019  1 71.36 ? 568 TYR A CB    1 
ATOM   4636  C  CG    . TYR A 1 568 ? 31.854  8.197   10.761  1 72.62 ? 568 TYR A CG    1 
ATOM   4637  C  CD1   . TYR A 1 568 ? 32.003  9.392   11.447  1 73.73 ? 568 TYR A CD1   1 
ATOM   4638  C  CD2   . TYR A 1 568 ? 30.587  7.634   10.704  1 73.73 ? 568 TYR A CD2   1 
ATOM   4639  C  CE1   . TYR A 1 568 ? 30.933  9.983   12.107  1 74.77 ? 568 TYR A CE1   1 
ATOM   4640  C  CE2   . TYR A 1 568 ? 29.507  8.219   11.353  1 74.75 ? 568 TYR A CE2   1 
ATOM   4641  C  CZ    . TYR A 1 568 ? 29.685  9.394   12.054  1 75.7  ? 568 TYR A CZ    1 
ATOM   4642  O  OH    . TYR A 1 568 ? 28.623  9.985   12.691  1 77.23 ? 568 TYR A OH    1 
ATOM   4643  N  N     . LEU A 1 569 ? 32.975  4.97    11.844  1 70.96 ? 569 LEU A N     1 
ATOM   4644  C  CA    . LEU A 1 569 ? 32.42   4.165   12.931  1 71.43 ? 569 LEU A CA    1 
ATOM   4645  C  C     . LEU A 1 569 ? 33.506  3.68    13.875  1 72.1  ? 569 LEU A C     1 
ATOM   4646  O  O     . LEU A 1 569 ? 33.297  3.657   15.087  1 72.26 ? 569 LEU A O     1 
ATOM   4647  C  CB    . LEU A 1 569 ? 31.625  2.978   12.391  1 71.39 ? 569 LEU A CB    1 
ATOM   4648  C  CG    . LEU A 1 569 ? 30.415  3.342   11.556  1 72.59 ? 569 LEU A CG    1 
ATOM   4649  C  CD1   . LEU A 1 569 ? 29.764  2.112   11.009  1 73.14 ? 569 LEU A CD1   1 
ATOM   4650  C  CD2   . LEU A 1 569 ? 29.406  4.136   12.358  1 73.16 ? 569 LEU A CD2   1 
ATOM   4651  N  N     . PHE A 1 570 ? 34.675  3.32    13.33   1 72.32 ? 570 PHE A N     1 
ATOM   4652  C  CA    . PHE A 1 570 ? 35.805  2.88    14.143  1 73    ? 570 PHE A CA    1 
ATOM   4653  C  C     . PHE A 1 570 ? 36.309  3.976   15.092  1 73.54 ? 570 PHE A C     1 
ATOM   4654  O  O     . PHE A 1 570 ? 36.943  3.653   16.094  1 73.62 ? 570 PHE A O     1 
ATOM   4655  C  CB    . PHE A 1 570 ? 36.941  2.34    13.268  1 73.02 ? 570 PHE A CB    1 
ATOM   4656  C  CG    . PHE A 1 570 ? 36.739  0.929   12.767  1 73.7  ? 570 PHE A CG    1 
ATOM   4657  C  CD1   . PHE A 1 570 ? 36.096  -0.015  13.544  1 74.43 ? 570 PHE A CD1   1 
ATOM   4658  C  CD2   . PHE A 1 570 ? 37.21   0.543   11.525  1 74.5  ? 570 PHE A CD2   1 
ATOM   4659  C  CE1   . PHE A 1 570 ? 35.932  -1.319  13.089  1 75.04 ? 570 PHE A CE1   1 
ATOM   4660  C  CE2   . PHE A 1 570 ? 37.061  -0.765  11.082  1 75.1  ? 570 PHE A CE2   1 
ATOM   4661  C  CZ    . PHE A 1 570 ? 36.41   -1.683  11.86   1 74.8  ? 570 PHE A CZ    1 
ATOM   4662  N  N     . ASP A 1 571 ? 36.009  5.262   14.801  1 73.81 ? 571 ASP A N     1 
ATOM   4663  C  CA    . ASP A 1 571 ? 36.362  6.384   15.68   1 74.63 ? 571 ASP A CA    1 
ATOM   4664  C  C     . ASP A 1 571 ? 35.522  6.41    16.976  1 74.85 ? 571 ASP A C     1 
ATOM   4665  O  O     . ASP A 1 571 ? 35.809  7.207   17.867  1 75.18 ? 571 ASP A O     1 
ATOM   4666  C  CB    . ASP A 1 571 ? 36.212  7.732   14.954  1 76.81 ? 571 ASP A CB    1 
ATOM   4667  C  CG    . ASP A 1 571 ? 37.309  8.048   13.953  1 81.94 ? 571 ASP A CG    1 
ATOM   4668  O  OD1   . ASP A 1 571 ? 38.344  7.343   13.962  1 82.83 ? 571 ASP A OD1   1 
ATOM   4669  O  OD2   . ASP A 1 571 ? 37.134  9.001   13.16   1 84.12 ? 571 ASP A OD2   1 
ATOM   4670  N  N     . PHE A 1 572 ? 34.484  5.568   17.076  1 74.5  ? 572 PHE A N     1 
ATOM   4671  C  CA    . PHE A 1 572 ? 33.629  5.503   18.248  1 74.64 ? 572 PHE A CA    1 
ATOM   4672  C  C     . PHE A 1 572 ? 33.576  4.091   18.795  1 74.46 ? 572 PHE A C     1 
ATOM   4673  O  O     . PHE A 1 572 ? 33.722  3.123   18.046  1 74.64 ? 572 PHE A O     1 
ATOM   4674  C  CB    . PHE A 1 572 ? 32.212  5.977   17.902  1 74.75 ? 572 PHE A CB    1 
ATOM   4675  C  CG    . PHE A 1 572 ? 32.19   7.37    17.335  1 75.71 ? 572 PHE A CG    1 
ATOM   4676  C  CD1   . PHE A 1 572 ? 32.318  8.471   18.159  1 76.69 ? 572 PHE A CD1   1 
ATOM   4677  C  CD2   . PHE A 1 572 ? 32.064  7.58    15.974  1 76.61 ? 572 PHE A CD2   1 
ATOM   4678  C  CE1   . PHE A 1 572 ? 32.319  9.754   17.631  1 77.52 ? 572 PHE A CE1   1 
ATOM   4679  C  CE2   . PHE A 1 572 ? 32.072  8.863   15.449  1 77.42 ? 572 PHE A CE2   1 
ATOM   4680  C  CZ    . PHE A 1 572 ? 32.2    9.941   16.279  1 77.31 ? 572 PHE A CZ    1 
ATOM   4681  N  N     . THR A 1 573 ? 33.348  3.97    20.103  1 73.95 ? 573 THR A N     1 
ATOM   4682  C  CA    . THR A 1 573 ? 33.224  2.682   20.775  1 73.88 ? 573 THR A CA    1 
ATOM   4683  C  C     . THR A 1 573 ? 31.98   1.972   20.235  1 73.73 ? 573 THR A C     1 
ATOM   4684  O  O     . THR A 1 573 ? 30.937  2.612   20.107  1 73.72 ? 573 THR A O     1 
ATOM   4685  C  CB    . THR A 1 573 ? 33.082  2.937   22.28   1 75.1  ? 573 THR A CB    1 
ATOM   4686  O  OG1   . THR A 1 573 ? 34.265  3.572   22.766  1 75.98 ? 573 THR A OG1   1 
ATOM   4687  C  CG2   . THR A 1 573 ? 32.809  1.673   23.065  1 75.59 ? 573 THR A CG2   1 
ATOM   4688  N  N     . PRO A 1 574 ? 32.056  0.674   19.872  1 73.56 ? 574 PRO A N     1 
ATOM   4689  C  CA    . PRO A 1 574 ? 30.852  -0.019  19.37   1 73.63 ? 574 PRO A CA    1 
ATOM   4690  C  C     . PRO A 1 574 ? 29.696  0.057   20.359  1 73.9  ? 574 PRO A C     1 
ATOM   4691  O  O     . PRO A 1 574 ? 29.941  0.057   21.562  1 74.12 ? 574 PRO A O     1 
ATOM   4692  C  CB    . PRO A 1 574 ? 31.308  -1.477  19.217  1 74.25 ? 574 PRO A CB    1 
ATOM   4693  C  CG    . PRO A 1 574 ? 32.779  -1.437  19.18   1 74.65 ? 574 PRO A CG    1 
ATOM   4694  C  CD    . PRO A 1 574 ? 33.219  -0.228  19.946  1 73.08 ? 574 PRO A CD    1 
ATOM   4695  N  N     . SER A 1 575 ? 28.449  0.129   19.875  1 73.77 ? 575 SER A N     1 
ATOM   4696  C  CA    . SER A 1 575 ? 27.291  0.216   20.768  1 74.22 ? 575 SER A CA    1 
ATOM   4697  C  C     . SER A 1 575 ? 27.213  -0.97   21.724  1 74.38 ? 575 SER A C     1 
ATOM   4698  O  O     . SER A 1 575 ? 27.066  -0.783  22.93   1 74.36 ? 575 SER A O     1 
ATOM   4699  C  CB    . SER A 1 575 ? 25.996  0.329   19.971  1 75.54 ? 575 SER A CB    1 
ATOM   4700  O  OG    . SER A 1 575 ? 26.047  1.428   19.077  1 77.79 ? 575 SER A OG    1 
ATOM   4701  N  N     . VAL A 1 576 ? 27.389  -2.178  21.198  1 74.38 ? 576 VAL A N     1 
ATOM   4702  C  CA    . VAL A 1 576 ? 27.317  -3.399  21.989  1 74.99 ? 576 VAL A CA    1 
ATOM   4703  C  C     . VAL A 1 576 ? 28.409  -4.416  21.596  1 75.48 ? 576 VAL A C     1 
ATOM   4704  O  O     . VAL A 1 576 ? 29.056  -4.268  20.56   1 75.72 ? 576 VAL A O     1 
ATOM   4705  C  CB    . VAL A 1 576 ? 25.899  -4.025  21.886  1 75.8  ? 576 VAL A CB    1 
ATOM   4706  C  CG1   . VAL A 1 576 ? 24.873  -3.252  22.714  1 76.41 ? 576 VAL A CG1   1 
ATOM   4707  C  CG2   . VAL A 1 576 ? 25.454  -4.15   20.433  1 76.38 ? 576 VAL A CG2   1 
ATOM   4708  N  N     . GLN A 1 577 ? 28.613  -5.445  22.434  1 75.52 ? 577 GLN A N     1 
ATOM   4709  C  CA    . GLN A 1 577 ? 29.564  -6.529  22.196  1 76.08 ? 577 GLN A CA    1 
ATOM   4710  C  C     . GLN A 1 577 ? 29.13   -7.806  22.93   1 76.53 ? 577 GLN A C     1 
ATOM   4711  O  O     . GLN A 1 577 ? 28.423  -7.73   23.936  1 76.77 ? 577 GLN A O     1 
ATOM   4712  C  CB    . GLN A 1 577 ? 30.994  -6.125  22.601  1 77.5  ? 577 GLN A CB    1 
ATOM   4713  C  CG    . GLN A 1 577 ? 31.228  -6.012  24.11   1 80.38 ? 577 GLN A CG    1 
ATOM   4714  C  CD    . GLN A 1 577 ? 32.005  -7.189  24.665  1 83.94 ? 577 GLN A CD    1 
ATOM   4715  O  OE1   . GLN A 1 577 ? 32.74   -7.883  23.946  1 85.23 ? 577 GLN A OE1   1 
ATOM   4716  N  NE2   . GLN A 1 577 ? 31.85   -7.442  25.963  1 84.1  ? 577 GLN A NE2   1 
ATOM   4717  N  N     . ARG A 1 578 ? 29.56   -8.976  22.437  1 76.53 ? 578 ARG A N     1 
ATOM   4718  C  CA    . ARG A 1 578 ? 29.226  -10.247 23.076  1 77.14 ? 578 ARG A CA    1 
ATOM   4719  C  C     . ARG A 1 578 ? 30.219  -11.352 22.703  1 77.75 ? 578 ARG A C     1 
ATOM   4720  O  O     . ARG A 1 578 ? 30.864  -11.282 21.654  1 77.95 ? 578 ARG A O     1 
ATOM   4721  C  CB    . ARG A 1 578 ? 27.79   -10.684 22.732  1 78.23 ? 578 ARG A CB    1 
ATOM   4722  C  CG    . ARG A 1 578 ? 27.582  -11.044 21.267  1 80.67 ? 578 ARG A CG    1 
ATOM   4723  C  CD    . ARG A 1 578 ? 26.403  -11.976 21.094  1 83.22 ? 578 ARG A CD    1 
ATOM   4724  N  NE    . ARG A 1 578 ? 26.231  -12.398 19.704  1 85.49 ? 578 ARG A NE    1 
ATOM   4725  C  CZ    . ARG A 1 578 ? 25.385  -13.343 19.305  1 87.46 ? 578 ARG A CZ    1 
ATOM   4726  N  NH1   . ARG A 1 578 ? 24.627  -13.982 20.188  1 86.9  ? 578 ARG A NH1   1 
ATOM   4727  N  NH2   . ARG A 1 578 ? 25.295  -13.663 18.022  1 87.58 ? 578 ARG A NH2   1 
ATOM   4728  N  N     . LYS A 1 579 ? 30.345  -12.373 23.558  1 77.88 ? 579 LYS A N     1 
ATOM   4729  C  CA    . LYS A 1 579 ? 31.22   -13.506 23.258  1 78.52 ? 579 LYS A CA    1 
ATOM   4730  C  C     . LYS A 1 579 ? 30.448  -14.489 22.369  1 79.02 ? 579 LYS A C     1 
ATOM   4731  O  O     . LYS A 1 579 ? 29.238  -14.652 22.546  1 79.27 ? 579 LYS A O     1 
ATOM   4732  C  CB    . LYS A 1 579 ? 31.703  -14.192 24.549  1 80.22 ? 579 LYS A CB    1 
ATOM   4733  C  CG    . LYS A 1 579 ? 32.672  -15.347 24.304  1 84    ? 579 LYS A CG    1 
ATOM   4734  C  CD    . LYS A 1 579 ? 33.257  -15.909 25.59   1 88.14 ? 579 LYS A CD    1 
ATOM   4735  C  CE    . LYS A 1 579 ? 34.391  -15.059 26.107  1 91.81 ? 579 LYS A CE    1 
ATOM   4736  N  NZ    . LYS A 1 579 ? 35.464  -14.896 25.09   1 94.12 ? 579 LYS A NZ    1 
ATOM   4737  N  N     . ILE A 1 580 ? 31.131  -15.129 21.405  1 78.95 ? 580 ILE A N     1 
ATOM   4738  C  CA    . ILE A 1 580 ? 30.489  -16.079 20.497  1 79.39 ? 580 ILE A CA    1 
ATOM   4739  C  C     . ILE A 1 580 ? 29.972  -17.345 21.22   1 79.51 ? 580 ILE A C     1 
ATOM   4740  O  O     . ILE A 1 580 ? 29.064  -18.006 20.718  1 79.58 ? 580 ILE A O     1 
ATOM   4741  C  CB    . ILE A 1 580 ? 31.418  -16.409 19.3    1 80.14 ? 580 ILE A CB    1 
ATOM   4742  C  CG1   . ILE A 1 580 ? 30.626  -16.885 18.07   1 81.23 ? 580 ILE A CG1   1 
ATOM   4743  C  CG2   . ILE A 1 580 ? 32.525  -17.388 19.684  1 80.71 ? 580 ILE A CG2   1 
ATOM   4744  C  CD1   . ILE A 1 580 ? 29.584  -15.91  17.577  1 82.56 ? 580 ILE A CD1   1 
ATOM   4745  N  N     . ALA A 1 581 ? 30.507  -17.656 22.41   1 79.42 ? 581 ALA A N     1 
ATOM   4746  C  CA    . ALA A 1 581 ? 30.058  -18.813 23.175  1 79.86 ? 581 ALA A CA    1 
ATOM   4747  C  C     . ALA A 1 581 ? 28.948  -18.428 24.162  1 80.02 ? 581 ALA A C     1 
ATOM   4748  O  O     . ALA A 1 581 ? 27.966  -19.157 24.291  1 80.17 ? 581 ALA A O     1 
ATOM   4749  C  CB    . ALA A 1 581 ? 31.229  -19.448 23.91   1 80.09 ? 581 ALA A CB    1 
ATOM   4750  N  N     . GLY A 1 582 ? 29.107  -17.288 24.832  1 79.79 ? 582 GLY A N     1 
ATOM   4751  C  CA    . GLY A 1 582 ? 28.129  -16.793 25.794  1 80.04 ? 582 GLY A CA    1 
ATOM   4752  C  C     . GLY A 1 582 ? 26.837  -16.352 25.138  1 80.1  ? 582 GLY A C     1 
ATOM   4753  O  O     . GLY A 1 582 ? 25.762  -16.863 25.459  1 80.2  ? 582 GLY A O     1 
ATOM   4754  N  N     . GLY A 1 583 ? 26.947  -15.409 24.21   1 79.88 ? 583 GLY A N     1 
ATOM   4755  C  CA    . GLY A 1 583 ? 25.801  -14.906 23.464  1 80.14 ? 583 GLY A CA    1 
ATOM   4756  C  C     . GLY A 1 583 ? 25.045  -13.759 24.108  1 80.15 ? 583 GLY A C     1 
ATOM   4757  O  O     . GLY A 1 583 ? 24.152  -13.182 23.482  1 80.3  ? 583 GLY A O     1 
ATOM   4758  N  N     . ASN A 1 584 ? 25.379  -13.419 25.359  1 79.79 ? 584 ASN A N     1 
ATOM   4759  C  CA    . ASN A 1 584 ? 24.695  -12.337 26.059  1 79.97 ? 584 ASN A CA    1 
ATOM   4760  C  C     . ASN A 1 584 ? 25.306  -10.986 25.693  1 79.87 ? 584 ASN A C     1 
ATOM   4761  O  O     . ASN A 1 584 ? 26.493  -10.765 25.925  1 80.05 ? 584 ASN A O     1 
ATOM   4762  C  CB    . ASN A 1 584 ? 24.733  -12.563 27.566  1 81.14 ? 584 ASN A CB    1 
ATOM   4763  C  CG    . ASN A 1 584 ? 24.225  -13.922 27.983  1 84.36 ? 584 ASN A CG    1 
ATOM   4764  O  OD1   . ASN A 1 584 ? 23.412  -14.554 27.298  1 85.55 ? 584 ASN A OD1   1 
ATOM   4765  N  ND2   . ASN A 1 584 ? 24.694  -14.404 29.121  1 85.02 ? 584 ASN A ND2   1 
ATOM   4766  N  N     . TRP A 1 585 ? 24.504  -10.091 25.101  1 79.42 ? 585 TRP A N     1 
ATOM   4767  C  CA    . TRP A 1 585 ? 24.985  -8.772  24.695  1 79.46 ? 585 TRP A CA    1 
ATOM   4768  C  C     . TRP A 1 585 ? 25.246  -7.864  25.888  1 79.7  ? 585 TRP A C     1 
ATOM   4769  O  O     . TRP A 1 585 ? 24.444  -7.806  26.816  1 79.89 ? 585 TRP A O     1 
ATOM   4770  C  CB    . TRP A 1 585 ? 23.98   -8.072  23.762  1 79.15 ? 585 TRP A CB    1 
ATOM   4771  C  CG    . TRP A 1 585 ? 23.857  -8.661  22.392  1 79.26 ? 585 TRP A CG    1 
ATOM   4772  C  CD1   . TRP A 1 585 ? 22.839  -9.435  21.925  1 80.05 ? 585 TRP A CD1   1 
ATOM   4773  C  CD2   . TRP A 1 585 ? 24.745  -8.453  21.286  1 79.26 ? 585 TRP A CD2   1 
ATOM   4774  N  NE1   . TRP A 1 585 ? 23.053  -9.749  20.603  1 80.34 ? 585 TRP A NE1   1 
ATOM   4775  C  CE2   . TRP A 1 585 ? 24.219  -9.16   20.187  1 80.02 ? 585 TRP A CE2   1 
ATOM   4776  C  CE3   . TRP A 1 585 ? 25.946  -7.755  21.122  1 79.74 ? 585 TRP A CE3   1 
ATOM   4777  C  CZ2   . TRP A 1 585 ? 24.853  -9.186  18.943  1 80.6  ? 585 TRP A CZ2   1 
ATOM   4778  C  CZ3   . TRP A 1 585 ? 26.569  -7.782  19.889  1 80.55 ? 585 TRP A CZ3   1 
ATOM   4779  C  CH2   . TRP A 1 585 ? 26.021  -8.487  18.816  1 80.67 ? 585 TRP A CH2   1 
ATOM   4780  N  N     . GLU A 1 586 ? 26.35   -7.127  25.833  1 79.58 ? 586 GLU A N     1 
ATOM   4781  C  CA    . GLU A 1 586 ? 26.753  -6.136  26.829  1 79.95 ? 586 GLU A CA    1 
ATOM   4782  C  C     . GLU A 1 586 ? 27.072  -4.81   26.116  1 80.04 ? 586 GLU A C     1 
ATOM   4783  O  O     . GLU A 1 586 ? 27.236  -4.797  24.896  1 80.14 ? 586 GLU A O     1 
ATOM   4784  C  CB    . GLU A 1 586 ? 28.009  -6.617  27.58   1 82.21 ? 586 GLU A CB    1 
ATOM   4785  C  CG    . GLU A 1 586 ? 27.74   -7.691  28.616  1 86.98 ? 586 GLU A CG    1 
ATOM   4786  C  CD    . GLU A 1 586 ? 28.736  -7.75   29.76   1 92.8  ? 586 GLU A CD    1 
ATOM   4787  O  OE1   . GLU A 1 586 ? 29.669  -6.915  29.792  1 93.96 ? 586 GLU A OE1   1 
ATOM   4788  O  OE2   . GLU A 1 586 ? 28.579  -8.638  30.628  1 94.6  ? 586 GLU A OE2   1 
ATOM   4789  N  N     . PHE A 1 587 ? 27.182  -3.702  26.866  1 79.85 ? 587 PHE A N     1 
ATOM   4790  C  CA    . PHE A 1 587 ? 27.559  -2.42   26.273  1 80.11 ? 587 PHE A CA    1 
ATOM   4791  C  C     . PHE A 1 587 ? 29.02   -2.494  25.807  1 80.42 ? 587 PHE A C     1 
ATOM   4792  O  O     . PHE A 1 587 ? 29.828  -3.207  26.404  1 80.43 ? 587 PHE A O     1 
ATOM   4793  C  CB    . PHE A 1 587 ? 27.4    -1.279  27.285  1 79.89 ? 587 PHE A CB    1 
ATOM   4794  C  CG    . PHE A 1 587 ? 25.987  -0.803  27.493  1 80.26 ? 587 PHE A CG    1 
ATOM   4795  C  CD1   . PHE A 1 587 ? 25.172  -0.508  26.417  1 80.89 ? 587 PHE A CD1   1 
ATOM   4796  C  CD2   . PHE A 1 587 ? 25.49   -0.598  28.765  1 80.92 ? 587 PHE A CD2   1 
ATOM   4797  C  CE1   . PHE A 1 587 ? 23.875  -0.05   26.612  1 81.48 ? 587 PHE A CE1   1 
ATOM   4798  C  CE2   . PHE A 1 587 ? 24.197  -0.132  28.955  1 81.53 ? 587 PHE A CE2   1 
ATOM   4799  C  CZ    . PHE A 1 587 ? 23.398  0.139   27.878  1 81.25 ? 587 PHE A CZ    1 
ATOM   4800  N  N     . GLY A 1 588 ? 29.34   -1.774  24.74   1 80.51 ? 588 GLY A N     1 
ATOM   4801  C  CA    . GLY A 1 588 ? 30.692  -1.753  24.2    1 81.09 ? 588 GLY A CA    1 
ATOM   4802  C  C     . GLY A 1 588 ? 31.685  -1.133  25.16   1 81.46 ? 588 GLY A C     1 
ATOM   4803  O  O     . GLY A 1 588 ? 31.414  -0.081  25.741  1 81.54 ? 588 GLY A O     1 
ATOM   4804  N  N     . ASN A 1 589 ? 32.833  -1.792  25.356  1 81.51 ? 589 ASN A N     1 
ATOM   4805  C  CA    . ASN A 1 589 ? 33.85   -1.318  26.289  1 82.05 ? 589 ASN A CA    1 
ATOM   4806  C  C     . ASN A 1 589 ? 35.135  -0.902  25.576  1 82.27 ? 589 ASN A C     1 
ATOM   4807  O  O     . ASN A 1 589 ? 35.723  0.124   25.918  1 82.37 ? 589 ASN A O     1 
ATOM   4808  C  CB    . ASN A 1 589 ? 34.139  -2.4    27.344  1 83.24 ? 589 ASN A CB    1 
ATOM   4809  C  CG    . ASN A 1 589 ? 35.262  -2.077  28.305  1 86.3  ? 589 ASN A CG    1 
ATOM   4810  O  OD1   . ASN A 1 589 ? 35.382  -0.958  28.816  1 87.33 ? 589 ASN A OD1   1 
ATOM   4811  N  ND2   . ASN A 1 589 ? 36.113  -3.057  28.571  1 86.94 ? 589 ASN A ND2   1 
ATOM   4812  N  N     . LYS A 1 590 ? 35.592  -1.712  24.616  1 82.18 ? 590 LYS A N     1 
ATOM   4813  C  CA    . LYS A 1 590 ? 36.834  -1.432  23.905  1 82.61 ? 590 LYS A CA    1 
ATOM   4814  C  C     . LYS A 1 590 ? 36.59   -0.884  22.509  1 82.74 ? 590 LYS A C     1 
ATOM   4815  O  O     . LYS A 1 590 ? 35.648  -1.299  21.839  1 82.89 ? 590 LYS A O     1 
ATOM   4816  C  CB    . LYS A 1 590 ? 37.697  -2.697  23.816  1 84.54 ? 590 LYS A CB    1 
ATOM   4817  C  CG    . LYS A 1 590 ? 38.038  -3.317  25.16   1 88.74 ? 590 LYS A CG    1 
ATOM   4818  C  CD    . LYS A 1 590 ? 38.703  -4.677  24.976  1 93.18 ? 590 LYS A CD    1 
ATOM   4819  C  CE    . LYS A 1 590 ? 39      -5.355  26.29   1 97.03 ? 590 LYS A CE    1 
ATOM   4820  N  NZ    . LYS A 1 590 ? 39.537  -6.726  26.09   1 99.32 ? 590 LYS A NZ    1 
ATOM   4821  N  N     . SER A 1 591 ? 37.461  0.024   22.056  1 82.5  ? 591 SER A N     1 
ATOM   4822  C  CA    . SER A 1 591 ? 37.358  0.611   20.723  1 82.67 ? 591 SER A CA    1 
ATOM   4823  C  C     . SER A 1 591 ? 38.038  -0.261  19.67   1 82.37 ? 591 SER A C     1 
ATOM   4824  O  O     . SER A 1 591 ? 38.965  -1.008  19.982  1 82.45 ? 591 SER A O     1 
ATOM   4825  C  CB    . SER A 1 591 ? 37.978  2.005   20.706  1 84.21 ? 591 SER A CB    1 
ATOM   4826  O  OG    . SER A 1 591 ? 36.986  3.018   20.679  1 86.67 ? 591 SER A OG    1 
ATOM   4827  N  N     . LEU A 1 592 ? 37.59   -0.152  18.416  1 81.86 ? 592 LEU A N     1 
ATOM   4828  C  CA    . LEU A 1 592 ? 38.192  -0.901  17.316  1 81.72 ? 592 LEU A CA    1 
ATOM   4829  C  C     . LEU A 1 592 ? 38.963  0.061   16.408  1 81.27 ? 592 LEU A C     1 
ATOM   4830  O  O     . LEU A 1 592 ? 38.543  1.203   16.213  1 81.42 ? 592 LEU A O     1 
ATOM   4831  C  CB    . LEU A 1 592 ? 37.131  -1.663  16.516  1 82.02 ? 592 LEU A CB    1 
ATOM   4832  C  CG    . LEU A 1 592 ? 36.799  -3.081  16.97   1 83.64 ? 592 LEU A CG    1 
ATOM   4833  C  CD1   . LEU A 1 592 ? 36.085  -3.08   18.306  1 84.22 ? 592 LEU A CD1   1 
ATOM   4834  C  CD2   . LEU A 1 592 ? 35.935  -3.779  15.943  1 84.39 ? 592 LEU A CD2   1 
ATOM   4835  N  N     . VAL A 1 593 ? 40.102  -0.395  15.87   1 80.58 ? 593 VAL A N     1 
ATOM   4836  C  CA    . VAL A 1 593 ? 40.964  0.429   15.022  1 80.41 ? 593 VAL A CA    1 
ATOM   4837  C  C     . VAL A 1 593 ? 40.999  -0.087  13.569  1 79.96 ? 593 VAL A C     1 
ATOM   4838  O  O     . VAL A 1 593 ? 41.137  -1.29   13.344  1 80    ? 593 VAL A O     1 
ATOM   4839  C  CB    . VAL A 1 593 ? 42.376  0.535   15.655  1 81.15 ? 593 VAL A CB    1 
ATOM   4840  C  CG1   . VAL A 1 593 ? 43.348  1.266   14.739  1 81.8  ? 593 VAL A CG1   1 
ATOM   4841  C  CG2   . VAL A 1 593 ? 42.317  1.214   17.017  1 81.59 ? 593 VAL A CG2   1 
ATOM   4842  N  N     . PRO A 1 594 ? 40.853  0.814   12.572  1 79.41 ? 594 PRO A N     1 
ATOM   4843  C  CA    . PRO A 1 594 ? 40.844  0.367   11.166  1 79.17 ? 594 PRO A CA    1 
ATOM   4844  C  C     . PRO A 1 594 ? 42.076  -0.398  10.691  1 78.89 ? 594 PRO A C     1 
ATOM   4845  O  O     . PRO A 1 594 ? 41.941  -1.273  9.84    1 79.1  ? 594 PRO A O     1 
ATOM   4846  C  CB    . PRO A 1 594 ? 40.661  1.668   10.364  1 79.91 ? 594 PRO A CB    1 
ATOM   4847  C  CG    . PRO A 1 594 ? 40.16   2.664   11.323  1 80.4  ? 594 PRO A CG    1 
ATOM   4848  C  CD    . PRO A 1 594 ? 40.656  2.271   12.684  1 78.87 ? 594 PRO A CD    1 
ATOM   4849  N  N     . ASN A 1 595 ? 43.268  -0.088  11.23   1 78.25 ? 595 ASN A N     1 
ATOM   4850  C  CA    . ASN A 1 595 ? 44.492  -0.784  10.814  1 78.05 ? 595 ASN A CA    1 
ATOM   4851  C  C     . ASN A 1 595 ? 44.559  -2.253  11.263  1 77.21 ? 595 ASN A C     1 
ATOM   4852  O  O     . ASN A 1 595 ? 45.438  -2.983  10.811  1 77.2  ? 595 ASN A O     1 
ATOM   4853  C  CB    . ASN A 1 595 ? 45.745  -0.024  11.233  1 79.42 ? 595 ASN A CB    1 
ATOM   4854  C  CG    . ASN A 1 595 ? 46.772  0.047   10.135  1 82.72 ? 595 ASN A CG    1 
ATOM   4855  O  OD1   . ASN A 1 595 ? 47.032  -0.936  9.434   1 84.1  ? 595 ASN A OD1   1 
ATOM   4856  N  ND2   . ASN A 1 595 ? 47.374  1.215   9.953   1 83.23 ? 595 ASN A ND2   1 
ATOM   4857  N  N     . ASP A 1 596 ? 43.627  -2.698  12.116  1 76.35 ? 596 ASP A N     1 
ATOM   4858  C  CA    . ASP A 1 596 ? 43.561  -4.107  12.511  1 75.99 ? 596 ASP A CA    1 
ATOM   4859  C  C     . ASP A 1 596 ? 42.864  -4.975  11.423  1 74.93 ? 596 ASP A C     1 
ATOM   4860  O  O     . ASP A 1 596 ? 42.784  -6.195  11.574  1 74.89 ? 596 ASP A O     1 
ATOM   4861  C  CB    . ASP A 1 596 ? 42.803  -4.237  13.845  1 78    ? 596 ASP A CB    1 
ATOM   4862  C  CG    . ASP A 1 596 ? 43.258  -5.383  14.728  1 82.9  ? 596 ASP A CG    1 
ATOM   4863  O  OD1   . ASP A 1 596 ? 44.048  -6.23   14.246  1 83.66 ? 596 ASP A OD1   1 
ATOM   4864  O  OD2   . ASP A 1 596 ? 42.827  -5.431  15.902  1 85.19 ? 596 ASP A OD2   1 
ATOM   4865  N  N     . PHE A 1 597 ? 42.351  -4.341  10.346  1 73.88 ? 597 PHE A N     1 
ATOM   4866  C  CA    . PHE A 1 597 ? 41.624  -4.983  9.264   1 73.27 ? 597 PHE A CA    1 
ATOM   4867  C  C     . PHE A 1 597 ? 42.12   -4.523  7.894   1 72.37 ? 597 PHE A C     1 
ATOM   4868  O  O     . PHE A 1 597 ? 42.708  -3.451  7.763   1 72.45 ? 597 PHE A O     1 
ATOM   4869  C  CB    . PHE A 1 597 ? 40.125  -4.642  9.387   1 73.2  ? 597 PHE A CB    1 
ATOM   4870  C  CG    . PHE A 1 597 ? 39.523  -4.958  10.738  1 73.79 ? 597 PHE A CG    1 
ATOM   4871  C  CD1   . PHE A 1 597 ? 39.252  -6.262  11.108  1 74.47 ? 597 PHE A CD1   1 
ATOM   4872  C  CD2   . PHE A 1 597 ? 39.244  -3.95   11.641  1 74.56 ? 597 PHE A CD2   1 
ATOM   4873  C  CE1   . PHE A 1 597 ? 38.714  -6.551  12.355  1 75.15 ? 597 PHE A CE1   1 
ATOM   4874  C  CE2   . PHE A 1 597 ? 38.705  -4.243  12.885  1 75.21 ? 597 PHE A CE2   1 
ATOM   4875  C  CZ    . PHE A 1 597 ? 38.448  -5.539  13.234  1 74.98 ? 597 PHE A CZ    1 
ATOM   4876  N  N     . ILE A 1 598 ? 41.862  -5.326  6.868   1 71.39 ? 598 ILE A N     1 
ATOM   4877  C  CA    . ILE A 1 598 ? 42.175  -4.956  5.497   1 70.97 ? 598 ILE A CA    1 
ATOM   4878  C  C     . ILE A 1 598 ? 40.864  -4.401  4.958   1 70.3  ? 598 ILE A C     1 
ATOM   4879  O  O     . ILE A 1 598 ? 39.868  -5.121  4.957   1 70.45 ? 598 ILE A O     1 
ATOM   4880  C  CB    . ILE A 1 598 ? 42.626  -6.187  4.678   1 71.5  ? 598 ILE A CB    1 
ATOM   4881  C  CG1   . ILE A 1 598 ? 43.829  -6.891  5.328   1 72.46 ? 598 ILE A CG1   1 
ATOM   4882  C  CG2   . ILE A 1 598 ? 42.906  -5.808  3.228   1 71.96 ? 598 ILE A CG2   1 
ATOM   4883  C  CD1   . ILE A 1 598 ? 45.055  -6.043  5.467   1 73.72 ? 598 ILE A CD1   1 
ATOM   4884  N  N     . LEU A 1 599 ? 40.827  -3.118  4.574   1 69.39 ? 599 LEU A N     1 
ATOM   4885  C  CA    . LEU A 1 599 ? 39.592  -2.518  4.077   1 68.95 ? 599 LEU A CA    1 
ATOM   4886  C  C     . LEU A 1 599 ? 39.599  -2.425  2.559   1 68.29 ? 599 LEU A C     1 
ATOM   4887  O  O     . LEU A 1 599 ? 40.495  -1.813  1.982   1 68.48 ? 599 LEU A O     1 
ATOM   4888  C  CB    . LEU A 1 599 ? 39.359  -1.124  4.69    1 69.17 ? 599 LEU A CB    1 
ATOM   4889  C  CG    . LEU A 1 599 ? 39.285  -1.036  6.218   1 70.78 ? 599 LEU A CG    1 
ATOM   4890  C  CD1   . LEU A 1 599 ? 39.068  0.389   6.669   1 71.36 ? 599 LEU A CD1   1 
ATOM   4891  C  CD2   . LEU A 1 599 ? 38.168  -1.887  6.763   1 71.59 ? 599 LEU A CD2   1 
ATOM   4892  N  N     . LEU A 1 600 ? 38.607  -3.032  1.909   1 67.33 ? 600 LEU A N     1 
ATOM   4893  C  CA    . LEU A 1 600 ? 38.48   -2.966  0.457   1 66.88 ? 600 LEU A CA    1 
ATOM   4894  C  C     . LEU A 1 600 ? 37.084  -2.485  0.086   1 66.3  ? 600 LEU A C     1 
ATOM   4895  O  O     . LEU A 1 600 ? 36.129  -2.751  0.81    1 66.39 ? 600 LEU A O     1 
ATOM   4896  C  CB    . LEU A 1 600 ? 38.723  -4.337  -0.19   1 67.05 ? 600 LEU A CB    1 
ATOM   4897  C  CG    . LEU A 1 600 ? 40.131  -4.919  -0.112  1 68.5  ? 600 LEU A CG    1 
ATOM   4898  C  CD1   . LEU A 1 600 ? 40.195  -6.249  -0.827  1 68.97 ? 600 LEU A CD1   1 
ATOM   4899  C  CD2   . LEU A 1 600 ? 41.158  -3.981  -0.71   1 69.29 ? 600 LEU A CD2   1 
ATOM   4900  N  N     . SER A 1 601 ? 36.959  -1.79   -1.042  1 65.6  ? 601 SER A N     1 
ATOM   4901  C  CA    . SER A 1 601 ? 35.657  -1.331  -1.517  1 65.45 ? 601 SER A CA    1 
ATOM   4902  C  C     . SER A 1 601 ? 35.324  -1.982  -2.861  1 64.92 ? 601 SER A C     1 
ATOM   4903  O  O     . SER A 1 601 ? 36.218  -2.292  -3.645  1 65.04 ? 601 SER A O     1 
ATOM   4904  C  CB    . SER A 1 601 ? 35.617  0.186   -1.632  1 66.74 ? 601 SER A CB    1 
ATOM   4905  O  OG    . SER A 1 601 ? 36.596  0.651   -2.545  1 68.92 ? 601 SER A OG    1 
ATOM   4906  N  N     . ALA A 1 602 ? 34.039  -2.21   -3.116  1 64.09 ? 602 ALA A N     1 
ATOM   4907  C  CA    . ALA A 1 602 ? 33.593  -2.845  -4.342  1 63.54 ? 602 ALA A CA    1 
ATOM   4908  C  C     . ALA A 1 602 ? 32.31   -2.226  -4.863  1 62.87 ? 602 ALA A C     1 
ATOM   4909  O  O     . ALA A 1 602 ? 31.46   -1.793  -4.091  1 63.03 ? 602 ALA A O     1 
ATOM   4910  C  CB    . ALA A 1 602 ? 33.397  -4.334  -4.116  1 63.56 ? 602 ALA A CB    1 
ATOM   4911  N  N     . GLY A 1 603 ? 32.176  -2.193  -6.174  1 62.02 ? 603 GLY A N     1 
ATOM   4912  C  CA    . GLY A 1 603 ? 30.976  -1.683  -6.813  1 61.79 ? 603 GLY A CA    1 
ATOM   4913  C  C     . GLY A 1 603 ? 30.325  -2.804  -7.587  1 61.34 ? 603 GLY A C     1 
ATOM   4914  O  O     . GLY A 1 603 ? 30.987  -3.438  -8.402  1 61.3  ? 603 GLY A O     1 
ATOM   4915  N  N     . ALA A 1 604 ? 29.052  -3.104  -7.309  1 60.96 ? 604 ALA A N     1 
ATOM   4916  C  CA    . ALA A 1 604 ? 28.348  -4.18   -8.007  1 61.05 ? 604 ALA A CA    1 
ATOM   4917  C  C     . ALA A 1 604 ? 27.24   -3.592  -8.868  1 60.91 ? 604 ALA A C     1 
ATOM   4918  O  O     . ALA A 1 604 ? 26.552  -2.672  -8.435  1 61.18 ? 604 ALA A O     1 
ATOM   4919  C  CB    . ALA A 1 604 ? 27.77   -5.168  -7.008  1 61.26 ? 604 ALA A CB    1 
ATOM   4920  N  N     . PHE A 1 605 ? 27.068  -4.108  -10.079 1 60.36 ? 605 PHE A N     1 
ATOM   4921  C  CA    . PHE A 1 605 ? 26.077  -3.571  -11.01  1 60.59 ? 605 PHE A CA    1 
ATOM   4922  C  C     . PHE A 1 605 ? 25.712  -4.583  -12.098 1 61.07 ? 605 PHE A C     1 
ATOM   4923  O  O     . PHE A 1 605 ? 26.389  -5.598  -12.247 1 61.08 ? 605 PHE A O     1 
ATOM   4924  C  CB    . PHE A 1 605 ? 26.625  -2.278  -11.663 1 60.33 ? 605 PHE A CB    1 
ATOM   4925  C  CG    . PHE A 1 605 ? 28.013  -2.437  -12.24  1 60.88 ? 605 PHE A CG    1 
ATOM   4926  C  CD1   . PHE A 1 605 ? 28.202  -3.014  -13.481 1 61.7  ? 605 PHE A CD1   1 
ATOM   4927  C  CD2   . PHE A 1 605 ? 29.129  -2.046  -11.523 1 61.59 ? 605 PHE A CD2   1 
ATOM   4928  C  CE1   . PHE A 1 605 ? 29.478  -3.197  -13.99  1 62.32 ? 605 PHE A CE1   1 
ATOM   4929  C  CE2   . PHE A 1 605 ? 30.406  -2.225  -12.04  1 62.21 ? 605 PHE A CE2   1 
ATOM   4930  C  CZ    . PHE A 1 605 ? 30.571  -2.794  -13.27  1 62.06 ? 605 PHE A CZ    1 
ATOM   4931  N  N     . ILE A 1 606 ? 24.672  -4.29   -12.889 1 61.22 ? 606 ILE A N     1 
ATOM   4932  C  CA    . ILE A 1 606 ? 24.291  -5.153  -13.996 1 61.91 ? 606 ILE A CA    1 
ATOM   4933  C  C     . ILE A 1 606 ? 24.877  -4.605  -15.295 1 62.6  ? 606 ILE A C     1 
ATOM   4934  O  O     . ILE A 1 606 ? 24.682  -3.434  -15.611 1 62.62 ? 606 ILE A O     1 
ATOM   4935  C  CB    . ILE A 1 606 ? 22.757  -5.373  -14.074 1 62.51 ? 606 ILE A CB    1 
ATOM   4936  C  CG1   . ILE A 1 606 ? 22.277  -6.258  -12.909 1 63.6  ? 606 ILE A CG1   1 
ATOM   4937  C  CG2   . ILE A 1 606 ? 22.34   -5.982  -15.417 1 62.96 ? 606 ILE A CG2   1 
ATOM   4938  C  CD1   . ILE A 1 606 ? 20.79   -6.222  -12.654 1 64.94 ? 606 ILE A CD1   1 
ATOM   4939  N  N     . ASP A 1 607 ? 25.611  -5.442  -16.038 1 63.05 ? 607 ASP A N     1 
ATOM   4940  C  CA    . ASP A 1 607 ? 26.202  -5.043  -17.313 1 63.87 ? 607 ASP A CA    1 
ATOM   4941  C  C     . ASP A 1 607 ? 26.084  -6.185  -18.31  1 64.35 ? 607 ASP A C     1 
ATOM   4942  O  O     . ASP A 1 607 ? 26.582  -7.27   -18.045 1 64.37 ? 607 ASP A O     1 
ATOM   4943  C  CB    . ASP A 1 607 ? 27.678  -4.653  -17.141 1 65.79 ? 607 ASP A CB    1 
ATOM   4944  C  CG    . ASP A 1 607 ? 28.345  -4.302  -18.451 1 70.98 ? 607 ASP A CG    1 
ATOM   4945  O  OD1   . ASP A 1 607 ? 27.925  -3.31   -19.08  1 71.9  ? 607 ASP A OD1   1 
ATOM   4946  O  OD2   . ASP A 1 607 ? 29.259  -5.045  -18.87  1 73.43 ? 607 ASP A OD2   1 
ATOM   4947  N  N     . TYR A 1 608 ? 25.488  -5.931  -19.474 1 64.63 ? 608 TYR A N     1 
ATOM   4948  C  CA    . TYR A 1 608 ? 25.334  -6.96   -20.499 1 65.4  ? 608 TYR A CA    1 
ATOM   4949  C  C     . TYR A 1 608 ? 26.499  -6.955  -21.491 1 65.85 ? 608 TYR A C     1 
ATOM   4950  O  O     . TYR A 1 608 ? 26.303  -6.748  -22.687 1 65.99 ? 608 TYR A O     1 
ATOM   4951  C  CB    . TYR A 1 608 ? 23.985  -6.81   -21.215 1 65.65 ? 608 TYR A CB    1 
ATOM   4952  C  CG    . TYR A 1 608 ? 22.811  -6.956  -20.275 1 66.65 ? 608 TYR A CG    1 
ATOM   4953  C  CD1   . TYR A 1 608 ? 22.382  -8.204  -19.86  1 67.71 ? 608 TYR A CD1   1 
ATOM   4954  C  CD2   . TYR A 1 608 ? 22.139  -5.843  -19.791 1 67.7  ? 608 TYR A CD2   1 
ATOM   4955  C  CE1   . TYR A 1 608 ? 21.306  -8.345  -18.997 1 68.86 ? 608 TYR A CE1   1 
ATOM   4956  C  CE2   . TYR A 1 608 ? 21.068  -5.97   -18.917 1 68.75 ? 608 TYR A CE2   1 
ATOM   4957  C  CZ    . TYR A 1 608 ? 20.654  -7.224  -18.518 1 69.88 ? 608 TYR A CZ    1 
ATOM   4958  O  OH    . TYR A 1 608 ? 19.597  -7.357  -17.646 1 71.63 ? 608 TYR A OH    1 
ATOM   4959  N  N     . ASP A 1 609 ? 27.709  -7.204  -20.972 1 65.98 ? 609 ASP A N     1 
ATOM   4960  C  CA    . ASP A 1 609 ? 28.996  -7.248  -21.67  1 66.59 ? 609 ASP A CA    1 
ATOM   4961  C  C     . ASP A 1 609 ? 29.275  -6.006  -22.54  1 66.71 ? 609 ASP A C     1 
ATOM   4962  O  O     . ASP A 1 609 ? 29.851  -6.128  -23.621 1 66.72 ? 609 ASP A O     1 
ATOM   4963  C  CB    . ASP A 1 609 ? 29.271  -8.552  -22.453 1 68.41 ? 609 ASP A CB    1 
ATOM   4964  C  CG    . ASP A 1 609 ? 28.145  -9.333  -23.114 1 72.92 ? 609 ASP A CG    1 
ATOM   4965  O  OD1   . ASP A 1 609 ? 27.454  -10.087 -22.405 1 73.45 ? 609 ASP A OD1   1 
ATOM   4966  O  OD2   . ASP A 1 609 ? 28.006  -9.24   -24.356 1 75.23 ? 609 ASP A OD2   1 
ATOM   4967  N  N     . ASN A 1 610 ? 28.914  -4.816  -22.047 1 66.64 ? 610 ASN A N     1 
ATOM   4968  C  CA    . ASN A 1 610 ? 29.19   -3.576  -22.765 1 67.15 ? 610 ASN A CA    1 
ATOM   4969  C  C     . ASN A 1 610 ? 30.451  -2.87   -22.26  1 67.38 ? 610 ASN A C     1 
ATOM   4970  O  O     . ASN A 1 610 ? 30.781  -1.81   -22.792 1 67.47 ? 610 ASN A O     1 
ATOM   4971  C  CB    . ASN A 1 610 ? 28.027  -2.587  -22.689 1 68.25 ? 610 ASN A CB    1 
ATOM   4972  C  CG    . ASN A 1 610 ? 26.679  -3.129  -23.054 1 71.42 ? 610 ASN A CG    1 
ATOM   4973  O  OD1   . ASN A 1 610 ? 26.163  -2.977  -24.173 1 72.49 ? 610 ASN A OD1   1 
ATOM   4974  N  ND2   . ASN A 1 610 ? 26.051  -3.739  -22.087 1 72.18 ? 610 ASN A ND2   1 
ATOM   4975  N  N     . LEU A 1 611 ? 31.146  -3.414  -21.241 1 67.29 ? 611 LEU A N     1 
ATOM   4976  C  CA    . LEU A 1 611 ? 32.338  -2.766  -20.716 1 67.83 ? 611 LEU A CA    1 
ATOM   4977  C  C     . LEU A 1 611 ? 33.624  -3.392  -21.234 1 68.35 ? 611 LEU A C     1 
ATOM   4978  O  O     . LEU A 1 611 ? 33.836  -4.597  -21.101 1 68.43 ? 611 LEU A O     1 
ATOM   4979  C  CB    . LEU A 1 611 ? 32.33   -2.755  -19.185 1 68.05 ? 611 LEU A CB    1 
ATOM   4980  C  CG    . LEU A 1 611 ? 31.19   -1.991  -18.525 1 69.59 ? 611 LEU A CG    1 
ATOM   4981  C  CD1   . LEU A 1 611 ? 31.166  -2.24   -17.046 1 70.14 ? 611 LEU A CD1   1 
ATOM   4982  C  CD2   . LEU A 1 611 ? 31.291  -0.511  -18.786 1 70.25 ? 611 LEU A CD2   1 
ATOM   4983  N  N     . THR A 1 612 ? 34.479  -2.566  -21.829 1 68.53 ? 612 THR A N     1 
ATOM   4984  C  CA    . THR A 1 612 ? 35.789  -2.971  -22.331 1 69.17 ? 612 THR A CA    1 
ATOM   4985  C  C     . THR A 1 612 ? 36.828  -2.821  -21.191 1 69.95 ? 612 THR A C     1 
ATOM   4986  O  O     . THR A 1 612 ? 36.501  -2.279  -20.135 1 70.05 ? 612 THR A O     1 
ATOM   4987  C  CB    . THR A 1 612 ? 36.144  -2.105  -23.558 1 70.12 ? 612 THR A CB    1 
ATOM   4988  O  OG1   . THR A 1 612 ? 36.372  -0.761  -23.136 1 70.83 ? 612 THR A OG1   1 
ATOM   4989  C  CG2   . THR A 1 612 ? 35.065  -2.131  -24.624 1 70.52 ? 612 THR A CG2   1 
ATOM   4990  N  N     . GLU A 1 613 ? 38.081  -3.257  -21.403 1 70.37 ? 613 GLU A N     1 
ATOM   4991  C  CA    . GLU A 1 613 ? 39.147  -3.12   -20.406 1 71.33 ? 613 GLU A CA    1 
ATOM   4992  C  C     . GLU A 1 613 ? 39.353  -1.639  -20.021 1 72.15 ? 613 GLU A C     1 
ATOM   4993  O  O     . GLU A 1 613 ? 39.533  -1.324  -18.843 1 72.22 ? 613 GLU A O     1 
ATOM   4994  C  CB    . GLU A 1 613 ? 40.448  -3.728  -20.964 1 73.51 ? 613 GLU A CB    1 
ATOM   4995  C  CG    . GLU A 1 613 ? 41.681  -3.512  -20.105 1 77.9  ? 613 GLU A CG    1 
ATOM   4996  C  CD    . GLU A 1 613 ? 42.982  -3.924  -20.77  1 83.18 ? 613 GLU A CD    1 
ATOM   4997  O  OE1   . GLU A 1 613 ? 44.047  -3.409  -20.359 1 84.12 ? 613 GLU A OE1   1 
ATOM   4998  O  OE2   . GLU A 1 613 ? 42.938  -4.752  -21.708 1 84.92 ? 613 GLU A OE2   1 
ATOM   4999  N  N     . ASN A 1 614 ? 39.282  -0.738  -21.016 1 72.56 ? 614 ASN A N     1 
ATOM   5000  C  CA    . ASN A 1 614 ? 39.44   0.703   -20.818 1 73.43 ? 614 ASN A CA    1 
ATOM   5001  C  C     . ASN A 1 614 ? 38.264  1.307   -20.051 1 73.75 ? 614 ASN A C     1 
ATOM   5002  O  O     . ASN A 1 614 ? 38.463  2.235   -19.268 1 73.79 ? 614 ASN A O     1 
ATOM   5003  C  CB    . ASN A 1 614 ? 39.636  1.416   -22.159 1 74.98 ? 614 ASN A CB    1 
ATOM   5004  C  CG    . ASN A 1 614 ? 41.007  1.212   -22.759 1 78.56 ? 614 ASN A CG    1 
ATOM   5005  O  OD1   . ASN A 1 614 ? 41.992  0.968   -22.053 1 79.93 ? 614 ASN A OD1   1 
ATOM   5006  N  ND2   . ASN A 1 614 ? 41.104  1.315   -24.078 1 79.21 ? 614 ASN A ND2   1 
ATOM   5007  N  N     . ASP A 1 615 ? 37.05   0.775   -20.256 1 73.84 ? 615 ASP A N     1 
ATOM   5008  C  CA    . ASP A 1 615 ? 35.861  1.237   -19.541 1 74.44 ? 615 ASP A CA    1 
ATOM   5009  C  C     . ASP A 1 615 ? 36.012  0.923   -18.065 1 74.58 ? 615 ASP A C     1 
ATOM   5010  O  O     . ASP A 1 615 ? 35.731  1.782   -17.234 1 74.61 ? 615 ASP A O     1 
ATOM   5011  C  CB    . ASP A 1 615 ? 34.59   0.569   -20.083 1 76.52 ? 615 ASP A CB    1 
ATOM   5012  C  CG    . ASP A 1 615 ? 34.039  1.178   -21.354 1 81.82 ? 615 ASP A CG    1 
ATOM   5013  O  OD1   . ASP A 1 615 ? 34.448  2.308   -21.696 1 82.69 ? 615 ASP A OD1   1 
ATOM   5014  O  OD2   . ASP A 1 615 ? 33.193  0.526   -22.005 1 84.26 ? 615 ASP A OD2   1 
ATOM   5015  N  N     . TYR A 1 616 ? 36.505  -0.287  -17.734 1 74.57 ? 616 TYR A N     1 
ATOM   5016  C  CA    . TYR A 1 616 ? 36.744  -0.682  -16.349 1 75.02 ? 616 TYR A CA    1 
ATOM   5017  C  C     . TYR A 1 616 ? 37.789  0.224   -15.719 1 75.05 ? 616 TYR A C     1 
ATOM   5018  O  O     . TYR A 1 616 ? 37.597  0.679   -14.599 1 75.09 ? 616 TYR A O     1 
ATOM   5019  C  CB    . TYR A 1 616 ? 37.181  -2.147  -16.255 1 75.3  ? 616 TYR A CB    1 
ATOM   5020  C  CG    . TYR A 1 616 ? 36.021  -3.111  -16.317 1 76.3  ? 616 TYR A CG    1 
ATOM   5021  C  CD1   . TYR A 1 616 ? 35.082  -3.165  -15.299 1 77.26 ? 616 TYR A CD1   1 
ATOM   5022  C  CD2   . TYR A 1 616 ? 35.866  -3.973  -17.389 1 77.35 ? 616 TYR A CD2   1 
ATOM   5023  C  CE1   . TYR A 1 616 ? 34.005  -4.038  -15.358 1 78.24 ? 616 TYR A CE1   1 
ATOM   5024  C  CE2   . TYR A 1 616 ? 34.798  -4.854  -17.458 1 78.34 ? 616 TYR A CE2   1 
ATOM   5025  C  CZ    . TYR A 1 616 ? 33.866  -4.883  -16.441 1 79.3  ? 616 TYR A CZ    1 
ATOM   5026  O  OH    . TYR A 1 616 ? 32.81   -5.757  -16.518 1 81    ? 616 TYR A OH    1 
ATOM   5027  N  N     . GLU A 1 617 ? 38.851  0.547   -16.463 1 74.89 ? 617 GLU A N     1 
ATOM   5028  C  CA    . GLU A 1 617 ? 39.903  1.457   -16.018 1 75.18 ? 617 GLU A CA    1 
ATOM   5029  C  C     . GLU A 1 617 ? 39.315  2.839   -15.672 1 74.97 ? 617 GLU A C     1 
ATOM   5030  O  O     . GLU A 1 617 ? 39.703  3.431   -14.667 1 75.04 ? 617 GLU A O     1 
ATOM   5031  C  CB    . GLU A 1 617 ? 41.015  1.518   -17.081 1 77.64 ? 617 GLU A CB    1 
ATOM   5032  C  CG    . GLU A 1 617 ? 41.894  2.749   -17.085 1 82.55 ? 617 GLU A CG    1 
ATOM   5033  C  CD    . GLU A 1 617 ? 42.305  3.166   -18.485 1 88.9  ? 617 GLU A CD    1 
ATOM   5034  O  OE1   . GLU A 1 617 ? 43.253  2.559   -19.033 1 89.97 ? 617 GLU A OE1   1 
ATOM   5035  O  OE2   . GLU A 1 617 ? 41.667  4.091   -19.039 1 91.23 ? 617 GLU A OE2   1 
ATOM   5036  N  N     . LYS A 1 618 ? 38.354  3.328   -16.476 1 74.58 ? 618 LYS A N     1 
ATOM   5037  C  CA    . LYS A 1 618 ? 37.705  4.617   -16.236 1 74.66 ? 618 LYS A CA    1 
ATOM   5038  C  C     . LYS A 1 618 ? 36.813  4.56    -14.993 1 74.35 ? 618 LYS A C     1 
ATOM   5039  O  O     . LYS A 1 618 ? 36.766  5.527   -14.236 1 74.38 ? 618 LYS A O     1 
ATOM   5040  C  CB    . LYS A 1 618 ? 36.954  5.086   -17.493 1 76.55 ? 618 LYS A CB    1 
ATOM   5041  C  CG    . LYS A 1 618 ? 36.235  6.415   -17.338 1 80.53 ? 618 LYS A CG    1 
ATOM   5042  C  CD    . LYS A 1 618 ? 34.746  6.218   -17.232 1 84.78 ? 618 LYS A CD    1 
ATOM   5043  C  CE    . LYS A 1 618 ? 34.03   7.526   -17.003 1 88.39 ? 618 LYS A CE    1 
ATOM   5044  N  NZ    . LYS A 1 618 ? 32.567  7.327   -16.835 1 90.52 ? 618 LYS A NZ    1 
ATOM   5045  N  N     . ILE A 1 619 ? 36.112  3.438   -14.774 1 73.94 ? 619 ILE A N     1 
ATOM   5046  C  CA    . ILE A 1 619 ? 35.263  3.288   -13.59  1 74.02 ? 619 ILE A CA    1 
ATOM   5047  C  C     . ILE A 1 619 ? 36.129  3.286   -12.325 1 73.57 ? 619 ILE A C     1 
ATOM   5048  O  O     . ILE A 1 619 ? 35.787  3.955   -11.354 1 73.67 ? 619 ILE A O     1 
ATOM   5049  C  CB    . ILE A 1 619 ? 34.344  2.04    -13.678 1 74.72 ? 619 ILE A CB    1 
ATOM   5050  C  CG1   . ILE A 1 619 ? 33.459  2.084   -14.936 1 75.76 ? 619 ILE A CG1   1 
ATOM   5051  C  CG2   . ILE A 1 619 ? 33.483  1.905   -12.423 1 75.2  ? 619 ILE A CG2   1 
ATOM   5052  C  CD1   . ILE A 1 619 ? 32.714  0.794   -15.221 1 76.98 ? 619 ILE A CD1   1 
ATOM   5053  N  N     . PHE A 1 620 ? 37.284  2.596   -12.362 1 72.91 ? 620 PHE A N     1 
ATOM   5054  C  CA    . PHE A 1 620 ? 38.219  2.567   -11.234 1 72.75 ? 620 PHE A CA    1 
ATOM   5055  C  C     . PHE A 1 620 ? 38.743  3.97    -10.928 1 72.12 ? 620 PHE A C     1 
ATOM   5056  O  O     . PHE A 1 620 ? 38.932  4.311   -9.765  1 72.1  ? 620 PHE A O     1 
ATOM   5057  C  CB    . PHE A 1 620 ? 39.414  1.644   -11.527 1 72.93 ? 620 PHE A CB    1 
ATOM   5058  C  CG    . PHE A 1 620 ? 39.148  0.163   -11.426 1 73.91 ? 620 PHE A CG    1 
ATOM   5059  C  CD1   . PHE A 1 620 ? 38.549  -0.373  -10.303 1 74.83 ? 620 PHE A CD1   1 
ATOM   5060  C  CD2   . PHE A 1 620 ? 39.567  -0.701  -12.421 1 74.8  ? 620 PHE A CD2   1 
ATOM   5061  C  CE1   . PHE A 1 620 ? 38.335  -1.739  -10.196 1 75.56 ? 620 PHE A CE1   1 
ATOM   5062  C  CE2   . PHE A 1 620 ? 39.331  -2.063  -12.323 1 75.53 ? 620 PHE A CE2   1 
ATOM   5063  C  CZ    . PHE A 1 620 ? 38.718  -2.572  -11.211 1 75.37 ? 620 PHE A CZ    1 
ATOM   5064  N  N     . GLU A 1 621 ? 38.99   4.776   -11.97  1 71.44 ? 621 GLU A N     1 
ATOM   5065  C  CA    . GLU A 1 621 ? 39.491  6.134   -11.815 1 71.27 ? 621 GLU A CA    1 
ATOM   5066  C  C     . GLU A 1 621 ? 38.42   7.027   -11.193 1 70.79 ? 621 GLU A C     1 
ATOM   5067  O  O     . GLU A 1 621 ? 38.718  7.798   -10.28  1 70.96 ? 621 GLU A O     1 
ATOM   5068  C  CB    . GLU A 1 621 ? 39.94   6.69    -13.173 1 73.51 ? 621 GLU A CB    1 
ATOM   5069  C  CG    . GLU A 1 621 ? 40.974  7.797   -13.073 1 78.2  ? 621 GLU A CG    1 
ATOM   5070  C  CD    . GLU A 1 621 ? 41.534  8.279   -14.398 1 84.24 ? 621 GLU A CD    1 
ATOM   5071  O  OE1   . GLU A 1 621 ? 41.131  7.742   -15.455 1 85.11 ? 621 GLU A OE1   1 
ATOM   5072  O  OE2   . GLU A 1 621 ? 42.386  9.196   -14.377 1 86.44 ? 621 GLU A OE2   1 
ATOM   5073  N  N     . VAL A 1 622 ? 37.171  6.899   -11.657 1 70.01 ? 622 VAL A N     1 
ATOM   5074  C  CA    . VAL A 1 622 ? 36.058  7.693   -11.141 1 69.76 ? 622 VAL A CA    1 
ATOM   5075  C  C     . VAL A 1 622 ? 35.708  7.344   -9.676  1 69.19 ? 622 VAL A C     1 
ATOM   5076  O  O     . VAL A 1 622 ? 35.64   8.231   -8.824  1 69.27 ? 622 VAL A O     1 
ATOM   5077  C  CB    . VAL A 1 622 ? 34.822  7.563   -12.074 1 70.45 ? 622 VAL A CB    1 
ATOM   5078  C  CG1   . VAL A 1 622 ? 33.555  8.113   -11.428 1 71.16 ? 622 VAL A CG1   1 
ATOM   5079  C  CG2   . VAL A 1 622 ? 35.066  8.231   -13.426 1 70.83 ? 622 VAL A CG2   1 
ATOM   5080  N  N     . THR A 1 623 ? 35.501  6.055   -9.39   1 68.35 ? 623 THR A N     1 
ATOM   5081  C  CA    . THR A 1 623 ? 35.062  5.585   -8.081  1 67.93 ? 623 THR A CA    1 
ATOM   5082  C  C     . THR A 1 623 ? 36.14   5.36    -7.026  1 67.38 ? 623 THR A C     1 
ATOM   5083  O  O     . THR A 1 623 ? 35.892  5.579   -5.844  1 67.39 ? 623 THR A O     1 
ATOM   5084  C  CB    . THR A 1 623 ? 34.272  4.29    -8.258  1 69.07 ? 623 THR A CB    1 
ATOM   5085  O  OG1   . THR A 1 623 ? 35.154  3.263   -8.712  1 70.05 ? 623 THR A OG1   1 
ATOM   5086  C  CG2   . THR A 1 623 ? 33.106  4.442   -9.219  1 69.39 ? 623 THR A CG2   1 
ATOM   5087  N  N     . GLY A 1 624 ? 37.284  4.843   -7.437  1 66.81 ? 624 GLY A N     1 
ATOM   5088  C  CA    . GLY A 1 624 ? 38.34   4.481   -6.497  1 66.72 ? 624 GLY A CA    1 
ATOM   5089  C  C     . GLY A 1 624 ? 38.119  3.116   -5.862  1 66.31 ? 624 GLY A C     1 
ATOM   5090  O  O     . GLY A 1 624 ? 38.767  2.781   -4.869  1 66.44 ? 624 GLY A O     1 
ATOM   5091  N  N     . CYS A 1 625 ? 37.197  2.314   -6.427  1 65.73 ? 625 CYS A N     1 
ATOM   5092  C  CA    . CYS A 1 625 ? 36.871  0.984   -5.937  1 65.71 ? 625 CYS A CA    1 
ATOM   5093  C  C     . CYS A 1 625 ? 38.033  0.027   -6.114  1 65.48 ? 625 CYS A C     1 
ATOM   5094  O  O     . CYS A 1 625 ? 38.759  0.121   -7.094  1 65.56 ? 625 CYS A O     1 
ATOM   5095  C  CB    . CYS A 1 625 ? 35.618  0.453   -6.629  1 66.37 ? 625 CYS A CB    1 
ATOM   5096  S  SG    . CYS A 1 625 ? 34.082  1.254   -6.105  1 69.49 ? 625 CYS A SG    1 
ATOM   5097  N  N     . ASP A 1 626 ? 38.204  -0.902  -5.18   1 65.12 ? 626 ASP A N     1 
ATOM   5098  C  CA    . ASP A 1 626 ? 39.238  -1.929  -5.293  1 65.27 ? 626 ASP A CA    1 
ATOM   5099  C  C     . ASP A 1 626 ? 38.757  -3.117  -6.155  1 64.87 ? 626 ASP A C     1 
ATOM   5100  O  O     . ASP A 1 626 ? 39.576  -3.858  -6.679  1 65.08 ? 626 ASP A O     1 
ATOM   5101  C  CB    . ASP A 1 626 ? 39.655  -2.435  -3.902  1 67.24 ? 626 ASP A CB    1 
ATOM   5102  C  CG    . ASP A 1 626 ? 40.278  -1.365  -3.031  1 72.36 ? 626 ASP A CG    1 
ATOM   5103  O  OD1   . ASP A 1 626 ? 41.451  -1.014  -3.272  1 73.17 ? 626 ASP A OD1   1 
ATOM   5104  O  OD2   . ASP A 1 626 ? 39.594  -0.885  -2.101  1 74.74 ? 626 ASP A OD2   1 
ATOM   5105  N  N     . LEU A 1 627 ? 37.439  -3.306  -6.292  1 64.14 ? 627 LEU A N     1 
ATOM   5106  C  CA    . LEU A 1 627 ? 36.88   -4.414  -7.051  1 63.92 ? 627 LEU A CA    1 
ATOM   5107  C  C     . LEU A 1 627 ? 35.592  -3.988  -7.75   1 63.47 ? 627 LEU A C     1 
ATOM   5108  O  O     . LEU A 1 627 ? 34.826  -3.207  -7.199  1 63.46 ? 627 LEU A O     1 
ATOM   5109  C  CB    . LEU A 1 627 ? 36.573  -5.562  -6.071  1 64.15 ? 627 LEU A CB    1 
ATOM   5110  C  CG    . LEU A 1 627 ? 35.922  -6.815  -6.651  1 65.59 ? 627 LEU A CG    1 
ATOM   5111  C  CD1   . LEU A 1 627 ? 36.854  -7.512  -7.595  1 66.05 ? 627 LEU A CD1   1 
ATOM   5112  C  CD2   . LEU A 1 627 ? 35.493  -7.767  -5.551  1 66.31 ? 627 LEU A CD2   1 
ATOM   5113  N  N     . LEU A 1 628 ? 35.349  -4.494  -8.957  1 62.9  ? 628 LEU A N     1 
ATOM   5114  C  CA    . LEU A 1 628 ? 34.101  -4.231  -9.661  1 62.76 ? 628 LEU A CA    1 
ATOM   5115  C  C     . LEU A 1 628 ? 33.443  -5.572  -9.945  1 62.7  ? 628 LEU A C     1 
ATOM   5116  O  O     . LEU A 1 628 ? 34.102  -6.489  -10.426 1 62.84 ? 628 LEU A O     1 
ATOM   5117  C  CB    . LEU A 1 628 ? 34.327  -3.435  -10.947 1 62.77 ? 628 LEU A CB    1 
ATOM   5118  C  CG    . LEU A 1 628 ? 34.822  -2.013  -10.75  1 64.05 ? 628 LEU A CG    1 
ATOM   5119  C  CD1   . LEU A 1 628 ? 35.182  -1.381  -12.062 1 64.55 ? 628 LEU A CD1   1 
ATOM   5120  C  CD2   . LEU A 1 628 ? 33.808  -1.167  -10.019 1 64.75 ? 628 LEU A CD2   1 
ATOM   5121  N  N     . ILE A 1 629 ? 32.172  -5.719  -9.577  1 62.32 ? 629 ILE A N     1 
ATOM   5122  C  CA    . ILE A 1 629 ? 31.448  -6.962  -9.793  1 62.39 ? 629 ILE A CA    1 
ATOM   5123  C  C     . ILE A 1 629 ? 30.351  -6.727  -10.816 1 62.25 ? 629 ILE A C     1 
ATOM   5124  O  O     . ILE A 1 629 ? 29.327  -6.12   -10.502 1 62.46 ? 629 ILE A O     1 
ATOM   5125  C  CB    . ILE A 1 629 ? 30.9    -7.542  -8.47   1 62.9  ? 629 ILE A CB    1 
ATOM   5126  C  CG1   . ILE A 1 629 ? 32.014  -7.643  -7.411  1 63.79 ? 629 ILE A CG1   1 
ATOM   5127  C  CG2   . ILE A 1 629 ? 30.24   -8.898  -8.715  1 63.4  ? 629 ILE A CG2   1 
ATOM   5128  C  CD1   . ILE A 1 629 ? 31.54   -8.068  -6.046  1 64.98 ? 629 ILE A CD1   1 
ATOM   5129  N  N     . ALA A 1 630 ? 30.592  -7.162  -12.056 1 61.66 ? 630 ALA A N     1 
ATOM   5130  C  CA    . ALA A 1 630 ? 29.632  -7.002  -13.137 1 61.59 ? 630 ALA A CA    1 
ATOM   5131  C  C     . ALA A 1 630 ? 28.795  -8.263  -13.258 1 61.19 ? 630 ALA A C     1 
ATOM   5132  O  O     . ALA A 1 630 ? 29.313  -9.346  -13.525 1 61.24 ? 630 ALA A O     1 
ATOM   5133  C  CB    . ALA A 1 630 ? 30.353  -6.724  -14.439 1 61.84 ? 630 ALA A CB    1 
ATOM   5134  N  N     . ILE A 1 631 ? 27.498  -8.114  -13.055 1 60.61 ? 631 ILE A N     1 
ATOM   5135  C  CA    . ILE A 1 631 ? 26.541  -9.205  -13.054 1 60.49 ? 631 ILE A CA    1 
ATOM   5136  C  C     . ILE A 1 631 ? 25.636  -9.132  -14.284 1 60.28 ? 631 ILE A C     1 
ATOM   5137  O  O     . ILE A 1 631 ? 25.261  -8.04   -14.695 1 60.3  ? 631 ILE A O     1 
ATOM   5138  C  CB    . ILE A 1 631 ? 25.753  -9.042  -11.734 1 60.89 ? 631 ILE A CB    1 
ATOM   5139  C  CG1   . ILE A 1 631 ? 26.645  -9.343  -10.524 1 61.74 ? 631 ILE A CG1   1 
ATOM   5140  C  CG2   . ILE A 1 631 ? 24.482  -9.851  -11.706 1 61.29 ? 631 ILE A CG2   1 
ATOM   5141  C  CD1   . ILE A 1 631 ? 26.155  -8.724  -9.268  1 63.04 ? 631 ILE A CD1   1 
ATOM   5142  N  N     . LYS A 1 632 ? 25.313  -10.276 -14.895 1 59.91 ? 632 LYS A N     1 
ATOM   5143  C  CA    . LYS A 1 632 ? 24.424  -10.29  -16.054 1 60.06 ? 632 LYS A CA    1 
ATOM   5144  C  C     . LYS A 1 632 ? 23.587  -11.537 -16.049 1 59.97 ? 632 LYS A C     1 
ATOM   5145  O  O     . LYS A 1 632 ? 24.091  -12.61  -15.728 1 60.03 ? 632 LYS A O     1 
ATOM   5146  C  CB    . LYS A 1 632 ? 25.202  -10.157 -17.37  1 61.95 ? 632 LYS A CB    1 
ATOM   5147  C  CG    . LYS A 1 632 ? 26.189  -11.288 -17.615 1 66.2  ? 632 LYS A CG    1 
ATOM   5148  C  CD    . LYS A 1 632 ? 27.247  -10.931 -18.648 1 70.94 ? 632 LYS A CD    1 
ATOM   5149  C  CE    . LYS A 1 632 ? 28.292  -10.003 -18.067 1 74.76 ? 632 LYS A CE    1 
ATOM   5150  N  NZ    . LYS A 1 632 ? 28.834  -10.495 -16.771 1 76.94 ? 632 LYS A NZ    1 
ATOM   5151  N  N     . ASN A 1 633 ? 22.3    -11.402 -16.366 1 59.8  ? 633 ASN A N     1 
ATOM   5152  C  CA    . ASN A 1 633 ? 21.427  -12.564 -16.399 1 60.29 ? 633 ASN A CA    1 
ATOM   5153  C  C     . ASN A 1 633 ? 21.418  -13.184 -17.773 1 61    ? 633 ASN A C     1 
ATOM   5154  O  O     . ASN A 1 633 ? 21.436  -12.487 -18.788 1 61.27 ? 633 ASN A O     1 
ATOM   5155  C  CB    . ASN A 1 633 ? 20.012  -12.225 -15.974 1 60.92 ? 633 ASN A CB    1 
ATOM   5156  C  CG    . ASN A 1 633 ? 19.403  -11.116 -16.775 1 62.99 ? 633 ASN A CG    1 
ATOM   5157  O  OD1   . ASN A 1 633 ? 19.776  -9.955  -16.631 1 63.67 ? 633 ASN A OD1   1 
ATOM   5158  N  ND2   . ASN A 1 633 ? 18.452  -11.447 -17.633 1 63.43 ? 633 ASN A ND2   1 
ATOM   5159  N  N     . GLN A 1 634 ? 21.407  -14.507 -17.79  1 61.05 ? 634 GLN A N     1 
ATOM   5160  C  CA    . GLN A 1 634 ? 21.305  -15.345 -18.972 1 61.51 ? 634 GLN A CA    1 
ATOM   5161  C  C     . GLN A 1 634 ? 19.914  -15.95  -18.844 1 61.95 ? 634 GLN A C     1 
ATOM   5162  O  O     . GLN A 1 634 ? 19.603  -16.531 -17.804 1 62.19 ? 634 GLN A O     1 
ATOM   5163  C  CB    . GLN A 1 634 ? 22.37   -16.446 -18.914 1 62.76 ? 634 GLN A CB    1 
ATOM   5164  C  CG    . GLN A 1 634 ? 22.303  -17.446 -20.047 1 65.41 ? 634 GLN A CG    1 
ATOM   5165  C  CD    . GLN A 1 634 ? 23.429  -18.429 -19.906 1 69.6  ? 634 GLN A CD    1 
ATOM   5166  O  OE1   . GLN A 1 634 ? 24.588  -18.132 -20.21  1 71.01 ? 634 GLN A OE1   1 
ATOM   5167  N  NE2   . GLN A 1 634 ? 23.118  -19.617 -19.419 1 70.44 ? 634 GLN A NE2   1 
ATOM   5168  N  N     . ASN A 1 635 ? 19.055  -15.761 -19.845 1 61.93 ? 635 ASN A N     1 
ATOM   5169  C  CA    . ASN A 1 635 ? 17.684  -16.255 -19.766 1 62.39 ? 635 ASN A CA    1 
ATOM   5170  C  C     . ASN A 1 635 ? 17.516  -17.703 -20.214 1 62.56 ? 635 ASN A C     1 
ATOM   5171  O  O     . ASN A 1 635 ? 16.601  -18.379 -19.741 1 62.8  ? 635 ASN A O     1 
ATOM   5172  C  CB    . ASN A 1 635 ? 16.74   -15.341 -20.541 1 63.58 ? 635 ASN A CB    1 
ATOM   5173  C  CG    . ASN A 1 635 ? 16.683  -13.95  -19.983 1 66.7  ? 635 ASN A CG    1 
ATOM   5174  O  OD1   . ASN A 1 635 ? 16.781  -13.744 -18.772 1 67.9  ? 635 ASN A OD1   1 
ATOM   5175  N  ND2   . ASN A 1 635 ? 16.52   -12.966 -20.857 1 67.34 ? 635 ASN A ND2   1 
ATOM   5176  N  N     . ASN A 1 636 ? 18.37   -18.178 -21.135 1 62.23 ? 636 ASN A N     1 
ATOM   5177  C  CA    . ASN A 1 636 ? 18.225  -19.538 -21.656 1 62.44 ? 636 ASN A CA    1 
ATOM   5178  C  C     . ASN A 1 636 ? 19.527  -20.346 -21.644 1 62.29 ? 636 ASN A C     1 
ATOM   5179  O  O     . ASN A 1 636 ? 20.31   -20.218 -22.587 1 62.46 ? 636 ASN A O     1 
ATOM   5180  C  CB    . ASN A 1 636 ? 17.68   -19.49  -23.097 1 63.52 ? 636 ASN A CB    1 
ATOM   5181  C  CG    . ASN A 1 636 ? 16.542  -18.519 -23.326 1 66.17 ? 636 ASN A CG    1 
ATOM   5182  O  OD1   . ASN A 1 636 ? 15.375  -18.825 -23.068 1 67.28 ? 636 ASN A OD1   1 
ATOM   5183  N  ND2   . ASN A 1 636 ? 16.858  -17.324 -23.809 1 66.49 ? 636 ASN A ND2   1 
ATOM   5184  N  N     . PRO A 1 637 ? 19.754  -21.251 -20.668 1 61.75 ? 637 PRO A N     1 
ATOM   5185  C  CA    . PRO A 1 637 ? 18.949  -21.503 -19.461 1 61.47 ? 637 PRO A CA    1 
ATOM   5186  C  C     . PRO A 1 637 ? 19.238  -20.47  -18.361 1 61.18 ? 637 PRO A C     1 
ATOM   5187  O  O     . PRO A 1 637 ? 20.31   -19.86  -18.363 1 61.43 ? 637 PRO A O     1 
ATOM   5188  C  CB    . PRO A 1 637 ? 19.399  -22.909 -19.053 1 62.25 ? 637 PRO A CB    1 
ATOM   5189  C  CG    . PRO A 1 637 ? 20.856  -22.952 -19.442 1 62.76 ? 637 PRO A CG    1 
ATOM   5190  C  CD    . PRO A 1 637 ? 20.988  -22.071 -20.675 1 61.25 ? 637 PRO A CD    1 
ATOM   5191  N  N     . GLN A 1 638 ? 18.291  -20.249 -17.444 1 60.51 ? 638 GLN A N     1 
ATOM   5192  C  CA    . GLN A 1 638 ? 18.464  -19.241 -16.399 1 60.36 ? 638 GLN A CA    1 
ATOM   5193  C  C     . GLN A 1 638 ? 19.74   -19.417 -15.567 1 59.61 ? 638 GLN A C     1 
ATOM   5194  O  O     . GLN A 1 638 ? 19.929  -20.45  -14.928 1 59.7  ? 638 GLN A O     1 
ATOM   5195  C  CB    . GLN A 1 638 ? 17.224  -19.146 -15.508 1 62.17 ? 638 GLN A CB    1 
ATOM   5196  C  CG    . GLN A 1 638 ? 16.121  -18.313 -16.145 1 65.68 ? 638 GLN A CG    1 
ATOM   5197  C  CD    . GLN A 1 638 ? 14.893  -18.281 -15.285 1 70.39 ? 638 GLN A CD    1 
ATOM   5198  O  OE1   . GLN A 1 638 ? 14.229  -19.305 -15.06  1 71.99 ? 638 GLN A OE1   1 
ATOM   5199  N  NE2   . GLN A 1 638 ? 14.568  -17.099 -14.782 1 71.1  ? 638 GLN A NE2   1 
ATOM   5200  N  N     . LYS A 1 639 ? 20.623  -18.398 -15.611 1 58.67 ? 639 LYS A N     1 
ATOM   5201  C  CA    . LYS A 1 639 ? 21.9    -18.371 -14.897 1 58.26 ? 639 LYS A CA    1 
ATOM   5202  C  C     . LYS A 1 639 ? 22.363  -16.935 -14.652 1 57.89 ? 639 LYS A C     1 
ATOM   5203  O  O     . LYS A 1 639 ? 22.126  -16.059 -15.48  1 57.83 ? 639 LYS A O     1 
ATOM   5204  C  CB    . LYS A 1 639 ? 22.988  -19.079 -15.721 1 59.54 ? 639 LYS A CB    1 
ATOM   5205  C  CG    . LYS A 1 639 ? 23.193  -20.544 -15.385 1 62.57 ? 639 LYS A CG    1 
ATOM   5206  C  CD    . LYS A 1 639 ? 24.18   -21.177 -16.343 1 65.98 ? 639 LYS A CD    1 
ATOM   5207  C  CE    . LYS A 1 639 ? 25.413  -21.678 -15.637 1 69.15 ? 639 LYS A CE    1 
ATOM   5208  N  NZ    . LYS A 1 639 ? 25.23   -23.059 -15.118 1 71.16 ? 639 LYS A NZ    1 
ATOM   5209  N  N     . TRP A 1 640 ? 23.062  -16.703 -13.54  1 57.43 ? 640 TRP A N     1 
ATOM   5210  C  CA    . TRP A 1 640 ? 23.636  -15.394 -13.259 1 57.38 ? 640 TRP A CA    1 
ATOM   5211  C  C     . TRP A 1 640 ? 25.116  -15.488 -13.596 1 57.12 ? 640 TRP A C     1 
ATOM   5212  O  O     . TRP A 1 640 ? 25.834  -16.287 -13.001 1 57.21 ? 640 TRP A O     1 
ATOM   5213  C  CB    . TRP A 1 640 ? 23.464  -15.003 -11.783 1 57.31 ? 640 TRP A CB    1 
ATOM   5214  C  CG    . TRP A 1 640 ? 22.125  -14.429 -11.429 1 57.59 ? 640 TRP A CG    1 
ATOM   5215  C  CD1   . TRP A 1 640 ? 21.195  -14.979 -10.599 1 58.45 ? 640 TRP A CD1   1 
ATOM   5216  C  CD2   . TRP A 1 640 ? 21.596  -13.158 -11.838 1 57.55 ? 640 TRP A CD2   1 
ATOM   5217  N  NE1   . TRP A 1 640 ? 20.113  -14.14  -10.477 1 58.7  ? 640 TRP A NE1   1 
ATOM   5218  C  CE2   . TRP A 1 640 ? 20.33   -13.018 -11.236 1 58.34 ? 640 TRP A CE2   1 
ATOM   5219  C  CE3   . TRP A 1 640 ? 22.051  -12.143 -12.687 1 57.89 ? 640 TRP A CE3   1 
ATOM   5220  C  CZ2   . TRP A 1 640 ? 19.529  -11.894 -11.438 1 58.79 ? 640 TRP A CZ2   1 
ATOM   5221  C  CZ3   . TRP A 1 640 ? 21.264  -11.022 -12.867 1 58.54 ? 640 TRP A CZ3   1 
ATOM   5222  C  CH2   . TRP A 1 640 ? 20.012  -10.915 -12.263 1 58.7  ? 640 TRP A CH2   1 
ATOM   5223  N  N     . VAL A 1 641 ? 25.564  -14.716 -14.572 1 56.8  ? 641 VAL A N     1 
ATOM   5224  C  CA    . VAL A 1 641 ? 26.961  -14.709 -14.981 1 57.16 ? 641 VAL A CA    1 
ATOM   5225  C  C     . VAL A 1 641 ? 27.671  -13.592 -14.226 1 57.56 ? 641 VAL A C     1 
ATOM   5226  O  O     . VAL A 1 641 ? 27.273  -12.43  -14.314 1 57.8  ? 641 VAL A O     1 
ATOM   5227  C  CB    . VAL A 1 641 ? 27.097  -14.556 -16.511 1 57.73 ? 641 VAL A CB    1 
ATOM   5228  C  CG1   . VAL A 1 641 ? 28.555  -14.64  -16.936 1 58.19 ? 641 VAL A CG1   1 
ATOM   5229  C  CG2   . VAL A 1 641 ? 26.26   -15.605 -17.238 1 58.19 ? 641 VAL A CG2   1 
ATOM   5230  N  N     . ILE A 1 642 ? 28.699  -13.949 -13.452 1 57.46 ? 642 ILE A N     1 
ATOM   5231  C  CA    . ILE A 1 642 ? 29.418  -12.981 -12.627 1 57.87 ? 642 ILE A CA    1 
ATOM   5232  C  C     . ILE A 1 642 ? 30.83   -12.74  -13.156 1 58.12 ? 642 ILE A C     1 
ATOM   5233  O  O     . ILE A 1 642 ? 31.576  -13.692 -13.374 1 58.19 ? 642 ILE A O     1 
ATOM   5234  C  CB    . ILE A 1 642 ? 29.466  -13.433 -11.137 1 58.39 ? 642 ILE A CB    1 
ATOM   5235  C  CG1   . ILE A 1 642 ? 28.132  -14.045 -10.638 1 59.34 ? 642 ILE A CG1   1 
ATOM   5236  C  CG2   . ILE A 1 642 ? 29.93   -12.299 -10.232 1 58.82 ? 642 ILE A CG2   1 
ATOM   5237  C  CD1   . ILE A 1 642 ? 26.964  -13.091 -10.575 1 60.59 ? 642 ILE A CD1   1 
ATOM   5238  N  N     . LYS A 1 643 ? 31.209  -11.475 -13.332 1 58.06 ? 643 LYS A N     1 
ATOM   5239  C  CA    . LYS A 1 643 ? 32.547  -11.126 -13.782 1 58.68 ? 643 LYS A CA    1 
ATOM   5240  C  C     . LYS A 1 643 ? 33.209  -10.25  -12.714 1 59.3  ? 643 LYS A C     1 
ATOM   5241  O  O     . LYS A 1 643 ? 32.718  -9.162  -12.424 1 59.51 ? 643 LYS A O     1 
ATOM   5242  C  CB    . LYS A 1 643 ? 32.484  -10.403 -15.133 1 60.53 ? 643 LYS A CB    1 
ATOM   5243  C  CG    . LYS A 1 643 ? 33.85   -10.182 -15.769 1 64.77 ? 643 LYS A CG    1 
ATOM   5244  C  CD    . LYS A 1 643 ? 33.749  -9.443  -17.106 1 69.07 ? 643 LYS A CD    1 
ATOM   5245  C  CE    . LYS A 1 643 ? 35.071  -9.407  -17.841 1 72.63 ? 643 LYS A CE    1 
ATOM   5246  N  NZ    . LYS A 1 643 ? 34.942  -8.823  -19.204 1 74.76 ? 643 LYS A NZ    1 
ATOM   5247  N  N     . PHE A 1 644 ? 34.286  -10.742 -12.09  1 59.5  ? 644 PHE A N     1 
ATOM   5248  C  CA    . PHE A 1 644 ? 34.993  -10.001 -11.045 1 60.19 ? 644 PHE A CA    1 
ATOM   5249  C  C     . PHE A 1 644 ? 36.2    -9.299  -11.632 1 60.67 ? 644 PHE A C     1 
ATOM   5250  O  O     . PHE A 1 644 ? 37.074  -9.954  -12.195 1 60.74 ? 644 PHE A O     1 
ATOM   5251  C  CB    . PHE A 1 644 ? 35.469  -10.943 -9.93   1 60.23 ? 644 PHE A CB    1 
ATOM   5252  C  CG    . PHE A 1 644 ? 34.38   -11.598 -9.118  1 60.96 ? 644 PHE A CG    1 
ATOM   5253  C  CD1   . PHE A 1 644 ? 33.828  -10.955 -8.024  1 61.82 ? 644 PHE A CD1   1 
ATOM   5254  C  CD2   . PHE A 1 644 ? 33.939  -12.873 -9.421  1 61.7  ? 644 PHE A CD2   1 
ATOM   5255  C  CE1   . PHE A 1 644 ? 32.84   -11.569 -7.264  1 62.52 ? 644 PHE A CE1   1 
ATOM   5256  C  CE2   . PHE A 1 644 ? 32.954  -13.484 -8.658  1 62.39 ? 644 PHE A CE2   1 
ATOM   5257  C  CZ    . PHE A 1 644 ? 32.408  -12.827 -7.587  1 62.24 ? 644 PHE A CZ    1 
ATOM   5258  N  N     . LYS A 1 645 ? 36.27   -7.981  -11.477 1 60.83 ? 645 LYS A N     1 
ATOM   5259  C  CA    . LYS A 1 645 ? 37.392  -7.212  -11.987 1 61.57 ? 645 LYS A CA    1 
ATOM   5260  C  C     . LYS A 1 645 ? 38.155  -6.541  -10.852 1 62.26 ? 645 LYS A C     1 
ATOM   5261  O  O     . LYS A 1 645 ? 37.71   -5.529  -10.319 1 62.33 ? 645 LYS A O     1 
ATOM   5262  C  CB    . LYS A 1 645 ? 36.914  -6.165  -12.996 1 63.31 ? 645 LYS A CB    1 
ATOM   5263  C  CG    . LYS A 1 645 ? 38.047  -5.531  -13.788 1 67.41 ? 645 LYS A CG    1 
ATOM   5264  C  CD    . LYS A 1 645 ? 38.456  -6.379  -14.994 1 71.57 ? 645 LYS A CD    1 
ATOM   5265  C  CE    . LYS A 1 645 ? 39.496  -5.678  -15.84  1 74.93 ? 645 LYS A CE    1 
ATOM   5266  N  NZ    . LYS A 1 645 ? 39.704  -6.357  -17.146 1 76.98 ? 645 LYS A NZ    1 
ATOM   5267  N  N     . PRO A 1 646 ? 39.318  -7.089  -10.47  1 62.69 ? 646 PRO A N     1 
ATOM   5268  C  CA    . PRO A 1 646 ? 40.101  -6.466  -9.388  1 63.17 ? 646 PRO A CA    1 
ATOM   5269  C  C     . PRO A 1 646 ? 40.974  -5.291  -9.853  1 63.97 ? 646 PRO A C     1 
ATOM   5270  O  O     . PRO A 1 646 ? 41.493  -5.311  -10.968 1 64.17 ? 646 PRO A O     1 
ATOM   5271  C  CB    . PRO A 1 646 ? 40.962  -7.621  -8.877  1 63.74 ? 646 PRO A CB    1 
ATOM   5272  C  CG    . PRO A 1 646 ? 41.146  -8.511  -10.065 1 64.01 ? 646 PRO A CG    1 
ATOM   5273  C  CD    . PRO A 1 646 ? 39.964  -8.313  -10.988 1 62.29 ? 646 PRO A CD    1 
ATOM   5274  N  N     . LYS A 1 647 ? 41.15   -4.275  -9.001  1 64.21 ? 647 LYS A N     1 
ATOM   5275  C  CA    . LYS A 1 647 ? 41.994  -3.127  -9.335  1 64.98 ? 647 LYS A CA    1 
ATOM   5276  C  C     . LYS A 1 647 ? 43.447  -3.407  -8.956  1 65.7  ? 647 LYS A C     1 
ATOM   5277  O  O     . LYS A 1 647 ? 44.363  -3.018  -9.676  1 66.01 ? 647 LYS A O     1 
ATOM   5278  C  CB    . LYS A 1 647 ? 41.518  -1.857  -8.604  1 66.61 ? 647 LYS A CB    1 
ATOM   5279  C  CG    . LYS A 1 647 ? 42.309  -0.602  -8.97   1 70.3  ? 647 LYS A CG    1 
ATOM   5280  C  CD    . LYS A 1 647 ? 41.914  0.624   -8.144  1 74.54 ? 647 LYS A CD    1 
ATOM   5281  C  CE    . LYS A 1 647 ? 42.172  0.444   -6.663  1 78.13 ? 647 LYS A CE    1 
ATOM   5282  N  NZ    . LYS A 1 647 ? 41.996  1.711   -5.907  1 80.2  ? 647 LYS A NZ    1 
ATOM   5283  N  N     . ASN A 1 648 ? 43.659  -4.078  -7.823  1 65.9  ? 648 ASN A N     1 
ATOM   5284  C  CA    . ASN A 1 648 ? 44.994  -4.352  -7.308  1 66.76 ? 648 ASN A CA    1 
ATOM   5285  C  C     . ASN A 1 648 ? 45.212  -5.831  -6.928  1 67.56 ? 648 ASN A C     1 
ATOM   5286  O  O     . ASN A 1 648 ? 44.274  -6.624  -6.986  1 67.84 ? 648 ASN A O     1 
ATOM   5287  C  CB    . ASN A 1 648 ? 45.272  -3.42   -6.119  1 67.86 ? 648 ASN A CB    1 
ATOM   5288  C  CG    . ASN A 1 648 ? 44.16   -3.405  -5.101  1 70.83 ? 648 ASN A CG    1 
ATOM   5289  O  OD1   . ASN A 1 648 ? 43.652  -4.449  -4.685  1 71.94 ? 648 ASN A OD1   1 
ATOM   5290  N  ND2   . ASN A 1 648 ? 43.746  -2.219  -4.692  1 71.44 ? 648 ASN A ND2   1 
ATOM   5291  N  N     . THR A 1 649 ? 46.448  -6.192  -6.528  1 67.77 ? 649 THR A N     1 
ATOM   5292  C  CA    . THR A 1 649 ? 46.836  -7.549  -6.142  1 68.36 ? 649 THR A CA    1 
ATOM   5293  C  C     . THR A 1 649 ? 46.113  -8.081  -4.89   1 68.42 ? 649 THR A C     1 
ATOM   5294  O  O     . THR A 1 649 ? 45.909  -9.29   -4.788  1 68.46 ? 649 THR A O     1 
ATOM   5295  C  CB    . THR A 1 649 ? 48.352  -7.628  -5.995  1 70    ? 649 THR A CB    1 
ATOM   5296  O  OG1   . THR A 1 649 ? 48.762  -6.689  -5      1 71.39 ? 649 THR A OG1   1 
ATOM   5297  C  CG2   . THR A 1 649 ? 49.073  -7.341  -7.302  1 70.31 ? 649 THR A CG2   1 
ATOM   5298  N  N     . ILE A 1 650 ? 45.712  -7.202  -3.955  1 68.2  ? 650 ILE A N     1 
ATOM   5299  C  CA    . ILE A 1 650 ? 44.974  -7.642  -2.766  1 68.55 ? 650 ILE A CA    1 
ATOM   5300  C  C     . ILE A 1 650 ? 43.584  -8.105  -3.201  1 68.51 ? 650 ILE A C     1 
ATOM   5301  O  O     . ILE A 1 650 ? 43.142  -9.187  -2.815  1 68.46 ? 650 ILE A O     1 
ATOM   5302  C  CB    . ILE A 1 650 ? 44.91   -6.524  -1.69   1 69.27 ? 650 ILE A CB    1 
ATOM   5303  C  CG1   . ILE A 1 650 ? 46.292  -6.274  -1.059  1 70.46 ? 650 ILE A CG1   1 
ATOM   5304  C  CG2   . ILE A 1 650 ? 43.86   -6.825  -0.618  1 69.74 ? 650 ILE A CG2   1 
ATOM   5305  C  CD1   . ILE A 1 650 ? 46.869  -7.45   -0.287  1 71.88 ? 650 ILE A CD1   1 
ATOM   5306  N  N     . ALA A 1 651 ? 42.918  -7.308  -4.05   1 68.43 ? 651 ALA A N     1 
ATOM   5307  C  CA    . ALA A 1 651 ? 41.603  -7.671  -4.571  1 68.89 ? 651 ALA A CA    1 
ATOM   5308  C  C     . ALA A 1 651 ? 41.681  -8.917  -5.452  1 69.4  ? 651 ALA A C     1 
ATOM   5309  O  O     . ALA A 1 651 ? 40.744  -9.704  -5.454  1 69.62 ? 651 ALA A O     1 
ATOM   5310  C  CB    . ALA A 1 651 ? 41.004  -6.52   -5.35   1 68.97 ? 651 ALA A CB    1 
ATOM   5311  N  N     . GLU A 1 652 ? 42.804  -9.125  -6.157  1 69.47 ? 652 GLU A N     1 
ATOM   5312  C  CA    . GLU A 1 652 ? 43.013  -10.299 -7.001  1 70.08 ? 652 GLU A CA    1 
ATOM   5313  C  C     . GLU A 1 652 ? 43.072  -11.564 -6.148  1 70.46 ? 652 GLU A C     1 
ATOM   5314  O  O     . GLU A 1 652 ? 42.522  -12.586 -6.549  1 70.58 ? 652 GLU A O     1 
ATOM   5315  C  CB    . GLU A 1 652 ? 44.289  -10.149 -7.837  1 72.37 ? 652 GLU A CB    1 
ATOM   5316  C  CG    . GLU A 1 652 ? 44.478  -11.247 -8.868  1 77.32 ? 652 GLU A CG    1 
ATOM   5317  C  CD    . GLU A 1 652 ? 45.634  -11.019 -9.821  1 83.78 ? 652 GLU A CD    1 
ATOM   5318  O  OE1   . GLU A 1 652 ? 45.996  -9.842  -10.048 1 84.93 ? 652 GLU A OE1   1 
ATOM   5319  O  OE2   . GLU A 1 652 ? 46.173  -12.018 -10.35  1 86.05 ? 652 GLU A OE2   1 
ATOM   5320  N  N     . LYS A 1 653 ? 43.686  -11.488 -4.953  1 70.49 ? 653 LYS A N     1 
ATOM   5321  C  CA    . LYS A 1 653 ? 43.74   -12.624 -4.028  1 70.93 ? 653 LYS A CA    1 
ATOM   5322  C  C     . LYS A 1 653 ? 42.331  -12.987 -3.542  1 70.93 ? 653 LYS A C     1 
ATOM   5323  O  O     . LYS A 1 653 ? 42.024  -14.167 -3.383  1 71    ? 653 LYS A O     1 
ATOM   5324  C  CB    . LYS A 1 653 ? 44.671  -12.332 -2.841  1 73.01 ? 653 LYS A CB    1 
ATOM   5325  C  CG    . LYS A 1 653 ? 46.144  -12.326 -3.224  1 77.32 ? 653 LYS A CG    1 
ATOM   5326  C  CD    . LYS A 1 653 ? 47.049  -12.26  -2.004  1 81.94 ? 653 LYS A CD    1 
ATOM   5327  C  CE    . LYS A 1 653 ? 48.484  -12.011 -2.393  1 85.82 ? 653 LYS A CE    1 
ATOM   5328  N  NZ    . LYS A 1 653 ? 49.342  -11.777 -1.201  1 88.25 ? 653 LYS A NZ    1 
ATOM   5329  N  N     . LEU A 1 654 ? 41.471  -11.976 -3.338  1 70.73 ? 654 LEU A N     1 
ATOM   5330  C  CA    . LEU A 1 654 ? 40.083  -12.173 -2.941  1 70.96 ? 654 LEU A CA    1 
ATOM   5331  C  C     . LEU A 1 654 ? 39.326  -12.849 -4.087  1 71.1  ? 654 LEU A C     1 
ATOM   5332  O  O     . LEU A 1 654 ? 38.612  -13.817 -3.847  1 71.2  ? 654 LEU A O     1 
ATOM   5333  C  CB    . LEU A 1 654 ? 39.432  -10.825 -2.57   1 71.09 ? 654 LEU A CB    1 
ATOM   5334  C  CG    . LEU A 1 654 ? 37.916  -10.823 -2.368  1 72.37 ? 654 LEU A CG    1 
ATOM   5335  C  CD1   . LEU A 1 654 ? 37.522  -11.741 -1.251  1 72.85 ? 654 LEU A CD1   1 
ATOM   5336  C  CD2   . LEU A 1 654 ? 37.403  -9.426  -2.092  1 73.04 ? 654 LEU A CD2   1 
ATOM   5337  N  N     . VAL A 1 655 ? 39.511  -12.371 -5.327  1 70.97 ? 655 VAL A N     1 
ATOM   5338  C  CA    . VAL A 1 655 ? 38.858  -12.943 -6.504  1 71.43 ? 655 VAL A CA    1 
ATOM   5339  C  C     . VAL A 1 655 ? 39.232  -14.416 -6.68   1 72.06 ? 655 VAL A C     1 
ATOM   5340  O  O     . VAL A 1 655 ? 38.347  -15.248 -6.874  1 72.23 ? 655 VAL A O     1 
ATOM   5341  C  CB    . VAL A 1 655 ? 39.133  -12.103 -7.772  1 71.89 ? 655 VAL A CB    1 
ATOM   5342  C  CG1   . VAL A 1 655 ? 38.698  -12.832 -9.037  1 72.42 ? 655 VAL A CG1   1 
ATOM   5343  C  CG2   . VAL A 1 655 ? 38.44   -10.757 -7.676  1 72.26 ? 655 VAL A CG2   1 
ATOM   5344  N  N     . ASN A 1 656 ? 40.522  -14.749 -6.547  1 72.2  ? 656 ASN A N     1 
ATOM   5345  C  CA    . ASN A 1 656 ? 40.981  -16.133 -6.67   1 72.72 ? 656 ASN A CA    1 
ATOM   5346  C  C     . ASN A 1 656 ? 40.387  -17.029 -5.583  1 72.78 ? 656 ASN A C     1 
ATOM   5347  O  O     . ASN A 1 656 ? 40.071  -18.186 -5.852  1 72.91 ? 656 ASN A O     1 
ATOM   5348  C  CB    . ASN A 1 656 ? 42.504  -16.202 -6.661  1 74.08 ? 656 ASN A CB    1 
ATOM   5349  C  CG    . ASN A 1 656 ? 43.126  -15.631 -7.907  1 77.62 ? 656 ASN A CG    1 
ATOM   5350  O  OD1   . ASN A 1 656 ? 42.48   -15.511 -8.956  1 78.93 ? 656 ASN A OD1   1 
ATOM   5351  N  ND2   . ASN A 1 656 ? 44.394  -15.258 -7.819  1 78.4  ? 656 ASN A ND2   1 
ATOM   5352  N  N     . TYR A 1 657 ? 40.214  -16.484 -4.37   1 72.5  ? 657 TYR A N     1 
ATOM   5353  C  CA    . TYR A 1 657 ? 39.62   -17.18  -3.232  1 72.81 ? 657 TYR A CA    1 
ATOM   5354  C  C     . TYR A 1 657 ? 38.147  -17.477 -3.524  1 72.63 ? 657 TYR A C     1 
ATOM   5355  O  O     . TYR A 1 657 ? 37.696  -18.591 -3.27   1 72.82 ? 657 TYR A O     1 
ATOM   5356  C  CB    . TYR A 1 657 ? 39.783  -16.325 -1.956  1 73.04 ? 657 TYR A CB    1 
ATOM   5357  C  CG    . TYR A 1 657 ? 39.007  -16.791 -0.743  1 73.92 ? 657 TYR A CG    1 
ATOM   5358  C  CD1   . TYR A 1 657 ? 39.46   -17.847 0.033   1 74.9  ? 657 TYR A CD1   1 
ATOM   5359  C  CD2   . TYR A 1 657 ? 37.88   -16.108 -0.312  1 74.9  ? 657 TYR A CD2   1 
ATOM   5360  C  CE1   . TYR A 1 657 ? 38.77   -18.256 1.169   1 75.89 ? 657 TYR A CE1   1 
ATOM   5361  C  CE2   . TYR A 1 657 ? 37.187  -16.501 0.826   1 75.88 ? 657 TYR A CE2   1 
ATOM   5362  C  CZ    . TYR A 1 657 ? 37.639  -17.573 1.57    1 76.82 ? 657 TYR A CZ    1 
ATOM   5363  O  OH    . TYR A 1 657 ? 36.949  -17.965 2.691   1 78.29 ? 657 TYR A OH    1 
ATOM   5364  N  N     . ILE A 1 658 ? 37.41   -16.495 -4.083  1 72.05 ? 658 ILE A N     1 
ATOM   5365  C  CA    . ILE A 1 658 ? 35.997  -16.654 -4.438  1 71.95 ? 658 ILE A CA    1 
ATOM   5366  C  C     . ILE A 1 658 ? 35.854  -17.721 -5.523  1 72.11 ? 658 ILE A C     1 
ATOM   5367  O  O     . ILE A 1 658 ? 35.007  -18.604 -5.408  1 72.23 ? 658 ILE A O     1 
ATOM   5368  C  CB    . ILE A 1 658 ? 35.369  -15.304 -4.88   1 72.08 ? 658 ILE A CB    1 
ATOM   5369  C  CG1   . ILE A 1 658 ? 35.338  -14.291 -3.726  1 72.9  ? 658 ILE A CG1   1 
ATOM   5370  C  CG2   . ILE A 1 658 ? 33.971  -15.501 -5.456  1 72.4  ? 658 ILE A CG2   1 
ATOM   5371  C  CD1   . ILE A 1 658 ? 35.011  -12.881 -4.16   1 73.99 ? 658 ILE A CD1   1 
ATOM   5372  N  N     . LYS A 1 659 ? 36.711  -17.665 -6.55   1 71.93 ? 659 LYS A N     1 
ATOM   5373  C  CA    . LYS A 1 659 ? 36.69   -18.626 -7.649  1 72.35 ? 659 LYS A CA    1 
ATOM   5374  C  C     . LYS A 1 659 ? 36.919  -20.059 -7.184  1 72.51 ? 659 LYS A C     1 
ATOM   5375  O  O     . LYS A 1 659 ? 36.174  -20.956 -7.574  1 72.67 ? 659 LYS A O     1 
ATOM   5376  C  CB    . LYS A 1 659 ? 37.727  -18.254 -8.719  1 74.32 ? 659 LYS A CB    1 
ATOM   5377  C  CG    . LYS A 1 659 ? 37.278  -17.147 -9.655  1 78.6  ? 659 LYS A CG    1 
ATOM   5378  C  CD    . LYS A 1 659 ? 38.246  -16.961 -10.821 1 83.01 ? 659 LYS A CD    1 
ATOM   5379  C  CE    . LYS A 1 659 ? 38.305  -18.176 -11.717 1 86.87 ? 659 LYS A CE    1 
ATOM   5380  N  NZ    . LYS A 1 659 ? 39.138  -17.937 -12.927 1 89.03 ? 659 LYS A NZ    1 
ATOM   5381  N  N     . LEU A 1 660 ? 37.938  -20.273 -6.348  1 72.33 ? 660 LEU A N     1 
ATOM   5382  C  CA    . LEU A 1 660 ? 38.287  -21.598 -5.85   1 72.63 ? 660 LEU A CA    1 
ATOM   5383  C  C     . LEU A 1 660 ? 37.247  -22.144 -4.878  1 72.67 ? 660 LEU A C     1 
ATOM   5384  O  O     . LEU A 1 660 ? 36.973  -23.341 -4.878  1 72.85 ? 660 LEU A O     1 
ATOM   5385  C  CB    . LEU A 1 660 ? 39.661  -21.549 -5.169  1 72.96 ? 660 LEU A CB    1 
ATOM   5386  C  CG    . LEU A 1 660 ? 40.817  -22.179 -5.932  1 74.62 ? 660 LEU A CG    1 
ATOM   5387  C  CD1   . LEU A 1 660 ? 41.048  -21.478 -7.259  1 75.22 ? 660 LEU A CD1   1 
ATOM   5388  C  CD2   . LEU A 1 660 ? 42.082  -22.16  -5.1    1 75.38 ? 660 LEU A CD2   1 
ATOM   5389  N  N     . ASN A 1 661 ? 36.672  -21.272 -4.052  1 72.39 ? 661 ASN A N     1 
ATOM   5390  C  CA    . ASN A 1 661 ? 35.697  -21.693 -3.059  1 72.71 ? 661 ASN A CA    1 
ATOM   5391  C  C     . ASN A 1 661 ? 34.25   -21.468 -3.473  1 72.7  ? 661 ASN A C     1 
ATOM   5392  O  O     . ASN A 1 661 ? 33.378  -21.326 -2.609  1 72.9  ? 661 ASN A O     1 
ATOM   5393  C  CB    . ASN A 1 661 ? 35.993  -21.039 -1.727  1 73.95 ? 661 ASN A CB    1 
ATOM   5394  C  CG    . ASN A 1 661 ? 37.307  -21.486 -1.152  1 77.05 ? 661 ASN A CG    1 
ATOM   5395  O  OD1   . ASN A 1 661 ? 38.3    -20.752 -1.168  1 78.15 ? 661 ASN A OD1   1 
ATOM   5396  N  ND2   . ASN A 1 661 ? 37.347  -22.71  -0.652  1 77.67 ? 661 ASN A ND2   1 
ATOM   5397  N  N     . PHE A 1 662 ? 33.98   -21.462 -4.79   1 72.27 ? 662 PHE A N     1 
ATOM   5398  C  CA    . PHE A 1 662 ? 32.612  -21.309 -5.269  1 72.47 ? 662 PHE A CA    1 
ATOM   5399  C  C     . PHE A 1 662 ? 31.981  -22.691 -5.341  1 72.8  ? 662 PHE A C     1 
ATOM   5400  O  O     . PHE A 1 662 ? 31.721  -23.219 -6.42   1 72.95 ? 662 PHE A O     1 
ATOM   5401  C  CB    . PHE A 1 662 ? 32.556  -20.605 -6.624  1 72.21 ? 662 PHE A CB    1 
ATOM   5402  C  CG    . PHE A 1 662 ? 31.262  -19.854 -6.834  1 72.73 ? 662 PHE A CG    1 
ATOM   5403  C  CD1   . PHE A 1 662 ? 31.136  -18.534 -6.439  1 73.43 ? 662 PHE A CD1   1 
ATOM   5404  C  CD2   . PHE A 1 662 ? 30.168  -20.473 -7.409  1 73.45 ? 662 PHE A CD2   1 
ATOM   5405  C  CE1   . PHE A 1 662 ? 29.944  -17.845 -6.629  1 74.07 ? 662 PHE A CE1   1 
ATOM   5406  C  CE2   . PHE A 1 662 ? 28.978  -19.787 -7.587  1 74.12 ? 662 PHE A CE2   1 
ATOM   5407  C  CZ    . PHE A 1 662 ? 28.876  -18.474 -7.208  1 73.89 ? 662 PHE A CZ    1 
ATOM   5408  N  N     . LYS A 1 663 ? 31.78   -23.291 -4.171  1 72.78 ? 663 LYS A N     1 
ATOM   5409  C  CA    . LYS A 1 663 ? 31.192  -24.613 -4.013  1 73.14 ? 663 LYS A CA    1 
ATOM   5410  C  C     . LYS A 1 663 ? 30.439  -24.637 -2.681  1 73.16 ? 663 LYS A C     1 
ATOM   5411  O  O     . LYS A 1 663 ? 30.887  -24.032 -1.702  1 73.13 ? 663 LYS A O     1 
ATOM   5412  C  CB    . LYS A 1 663 ? 32.284  -25.697 -4.049  1 75.04 ? 663 LYS A CB    1 
ATOM   5413  C  CG    . LYS A 1 663 ? 31.741  -27.117 -4.12   1 79.2  ? 663 LYS A CG    1 
ATOM   5414  C  CD    . LYS A 1 663 ? 32.789  -28.152 -3.725  1 83.59 ? 663 LYS A CD    1 
ATOM   5415  C  CE    . LYS A 1 663 ? 32.177  -29.483 -3.347  1 87.08 ? 663 LYS A CE    1 
ATOM   5416  N  NZ    . LYS A 1 663 ? 31.412  -29.4   -2.073  1 89.08 ? 663 LYS A NZ    1 
ATOM   5417  N  N     . SER A 1 664 ? 29.283  -25.302 -2.649  1 73.02 ? 664 SER A N     1 
ATOM   5418  C  CA    . SER A 1 664 ? 28.486  -25.362 -1.434  1 73.43 ? 664 SER A CA    1 
ATOM   5419  C  C     . SER A 1 664 ? 27.718  -26.66  -1.314  1 73.64 ? 664 SER A C     1 
ATOM   5420  O  O     . SER A 1 664 ? 27.274  -27.22  -2.315  1 73.86 ? 664 SER A O     1 
ATOM   5421  C  CB    . SER A 1 664 ? 27.512  -24.19  -1.384  1 74.74 ? 664 SER A CB    1 
ATOM   5422  O  OG    . SER A 1 664 ? 26.683  -24.241 -0.235  1 77.07 ? 664 SER A OG    1 
ATOM   5423  N  N     . ASN A 1 665 ? 27.538  -27.122 -0.081  1 73.4  ? 665 ASN A N     1 
ATOM   5424  C  CA    . ASN A 1 665 ? 26.734  -28.307 0.189   1 73.67 ? 665 ASN A CA    1 
ATOM   5425  C  C     . ASN A 1 665 ? 25.244  -27.952 0.392   1 73.45 ? 665 ASN A C     1 
ATOM   5426  O  O     . ASN A 1 665 ? 24.402  -28.847 0.377   1 73.67 ? 665 ASN A O     1 
ATOM   5427  C  CB    . ASN A 1 665 ? 27.277  -29.054 1.401   1 75.03 ? 665 ASN A CB    1 
ATOM   5428  C  CG    . ASN A 1 665 ? 28.651  -29.642 1.179   1 78.43 ? 665 ASN A CG    1 
ATOM   5429  O  OD1   . ASN A 1 665 ? 29.178  -29.676 0.055   1 79.58 ? 665 ASN A OD1   1 
ATOM   5430  N  ND2   . ASN A 1 665 ? 29.264  -30.121 2.248   1 79.16 ? 665 ASN A ND2   1 
ATOM   5431  N  N     . ILE A 1 666 ? 24.917  -26.659 0.578   1 72.89 ? 666 ILE A N     1 
ATOM   5432  C  CA    . ILE A 1 666 ? 23.555  -26.198 0.788   1 72.89 ? 666 ILE A CA    1 
ATOM   5433  C  C     . ILE A 1 666 ? 23.026  -25.439 -0.436  1 72.69 ? 666 ILE A C     1 
ATOM   5434  O  O     . ILE A 1 666 ? 21.959  -25.769 -0.942  1 72.76 ? 666 ILE A O     1 
ATOM   5435  C  CB    . ILE A 1 666 ? 23.494  -25.335 2.069   1 73.47 ? 666 ILE A CB    1 
ATOM   5436  C  CG1   . ILE A 1 666 ? 23.977  -26.126 3.291   1 74.6  ? 666 ILE A CG1   1 
ATOM   5437  C  CG2   . ILE A 1 666 ? 22.098  -24.768 2.281   1 73.9  ? 666 ILE A CG2   1 
ATOM   5438  C  CD1   . ILE A 1 666 ? 24.188  -25.27  4.521   1 76.02 ? 666 ILE A CD1   1 
ATOM   5439  N  N     . PHE A 1 667 ? 23.778  -24.444 -0.925  1 72.34 ? 667 PHE A N     1 
ATOM   5440  C  CA    . PHE A 1 667 ? 23.357  -23.626 -2.06   1 72.5  ? 667 PHE A CA    1 
ATOM   5441  C  C     . PHE A 1 667 ? 23.69   -24.244 -3.412  1 72.44 ? 667 PHE A C     1 
ATOM   5442  O  O     . PHE A 1 667 ? 24.811  -24.694 -3.633  1 72.57 ? 667 PHE A O     1 
ATOM   5443  C  CB    . PHE A 1 667 ? 23.947  -22.212 -1.954  1 72.47 ? 667 PHE A CB    1 
ATOM   5444  C  CG    . PHE A 1 667 ? 23.062  -21.119 -2.508  1 73.12 ? 667 PHE A CG    1 
ATOM   5445  C  CD1   . PHE A 1 667 ? 22.027  -20.594 -1.757  1 73.95 ? 667 PHE A CD1   1 
ATOM   5446  C  CD2   . PHE A 1 667 ? 23.289  -20.591 -3.757  1 73.85 ? 667 PHE A CD2   1 
ATOM   5447  C  CE1   . PHE A 1 667 ? 21.195  -19.614 -2.279  1 74.63 ? 667 PHE A CE1   1 
ATOM   5448  C  CE2   . PHE A 1 667 ? 22.499  -19.56  -4.248  1 74.53 ? 667 PHE A CE2   1 
ATOM   5449  C  CZ    . PHE A 1 667 ? 21.448  -19.09  -3.516  1 74.36 ? 667 PHE A CZ    1 
ATOM   5450  N  N     . ASP A 1 668 ? 22.713  -24.251 -4.319  1 72.13 ? 668 ASP A N     1 
ATOM   5451  C  CA    . ASP A 1 668 ? 22.876  -24.783 -5.663  1 72.38 ? 668 ASP A CA    1 
ATOM   5452  C  C     . ASP A 1 668 ? 23.715  -23.805 -6.461  1 72.51 ? 668 ASP A C     1 
ATOM   5453  O  O     . ASP A 1 668 ? 23.18   -22.846 -7.012  1 72.56 ? 668 ASP A O     1 
ATOM   5454  C  CB    . ASP A 1 668 ? 21.506  -24.96  -6.332  1 73.93 ? 668 ASP A CB    1 
ATOM   5455  C  CG    . ASP A 1 668 ? 21.521  -25.793 -7.597  1 78.5  ? 668 ASP A CG    1 
ATOM   5456  O  OD1   . ASP A 1 668 ? 22.573  -25.83  -8.275  1 79.34 ? 668 ASP A OD1   1 
ATOM   5457  O  OD2   . ASP A 1 668 ? 20.482  -26.41  -7.911  1 80.59 ? 668 ASP A OD2   1 
ATOM   5458  N  N     . THR A 1 669 ? 25.027  -24.051 -6.535  1 72.43 ? 669 THR A N     1 
ATOM   5459  C  CA    . THR A 1 669 ? 25.937  -23.191 -7.291  1 72.89 ? 669 THR A CA    1 
ATOM   5460  C  C     . THR A 1 669 ? 25.809  -23.322 -8.821  1 73.09 ? 669 THR A C     1 
ATOM   5461  O  O     . THR A 1 669 ? 26.452  -22.565 -9.547  1 73.27 ? 669 THR A O     1 
ATOM   5462  C  CB    . THR A 1 669 ? 27.372  -23.417 -6.836  1 74.24 ? 669 THR A CB    1 
ATOM   5463  O  OG1   . THR A 1 669 ? 27.721  -24.779 -7.085  1 75.27 ? 669 THR A OG1   1 
ATOM   5464  C  CG2   . THR A 1 669 ? 27.565  -23.101 -5.363  1 74.66 ? 669 THR A CG2   1 
ATOM   5465  N  N     . GLY A 1 670 ? 24.986  -24.262 -9.291  1 72.95 ? 670 GLY A N     1 
ATOM   5466  C  CA    . GLY A 1 670 ? 24.734  -24.482 -10.71  1 73.38 ? 670 GLY A CA    1 
ATOM   5467  C  C     . GLY A 1 670 ? 24.003  -23.339 -11.388 1 73.62 ? 670 GLY A C     1 
ATOM   5468  O  O     . GLY A 1 670 ? 24.031  -23.227 -12.615 1 73.69 ? 670 GLY A O     1 
ATOM   5469  N  N     . PHE A 1 671 ? 23.343  -22.475 -10.597 1 73.56 ? 671 PHE A N     1 
ATOM   5470  C  CA    . PHE A 1 671 ? 22.643  -21.298 -11.11  1 74.01 ? 671 PHE A CA    1 
ATOM   5471  C  C     . PHE A 1 671 ? 23.614  -20.121 -11.419 1 74.19 ? 671 PHE A C     1 
ATOM   5472  O  O     . PHE A 1 671 ? 23.183  -19.089 -11.922 1 74.28 ? 671 PHE A O     1 
ATOM   5473  C  CB    . PHE A 1 671 ? 21.56   -20.858 -10.109 1 74.12 ? 671 PHE A CB    1 
ATOM   5474  C  CG    . PHE A 1 671 ? 20.327  -20.265 -10.742 1 75.12 ? 671 PHE A CG    1 
ATOM   5475  C  CD1   . PHE A 1 671 ? 19.313  -21.078 -11.216 1 76    ? 671 PHE A CD1   1 
ATOM   5476  C  CD2   . PHE A 1 671 ? 20.174  -18.893 -10.847 1 76.18 ? 671 PHE A CD2   1 
ATOM   5477  C  CE1   . PHE A 1 671 ? 18.182  -20.531 -11.804 1 76.84 ? 671 PHE A CE1   1 
ATOM   5478  C  CE2   . PHE A 1 671 ? 19.047  -18.348 -11.446 1 77    ? 671 PHE A CE2   1 
ATOM   5479  C  CZ    . PHE A 1 671 ? 18.054  -19.17  -11.909 1 76.79 ? 671 PHE A CZ    1 
ATOM   5480  N  N     . PHE A 1 672 ? 24.915  -20.277 -11.14  1 74.05 ? 672 PHE A N     1 
ATOM   5481  C  CA    . PHE A 1 672 ? 25.895  -19.23  -11.376 1 74.33 ? 672 PHE A CA    1 
ATOM   5482  C  C     . PHE A 1 672 ? 27.005  -19.682 -12.297 1 74.53 ? 672 PHE A C     1 
ATOM   5483  O  O     . PHE A 1 672 ? 27.396  -20.845 -12.287 1 74.53 ? 672 PHE A O     1 
ATOM   5484  C  CB    . PHE A 1 672 ? 26.543  -18.816 -10.056 1 74.28 ? 672 PHE A CB    1 
ATOM   5485  C  CG    . PHE A 1 672 ? 25.627  -18.14  -9.077  1 74.95 ? 672 PHE A CG    1 
ATOM   5486  C  CD1   . PHE A 1 672 ? 24.914  -18.876 -8.151  1 75.78 ? 672 PHE A CD1   1 
ATOM   5487  C  CD2   . PHE A 1 672 ? 25.509  -16.763 -9.054  1 75.75 ? 672 PHE A CD2   1 
ATOM   5488  C  CE1   . PHE A 1 672 ? 24.072  -18.249 -7.245  1 76.48 ? 672 PHE A CE1   1 
ATOM   5489  C  CE2   . PHE A 1 672 ? 24.675  -16.138 -8.14   1 76.48 ? 672 PHE A CE2   1 
ATOM   5490  C  CZ    . PHE A 1 672 ? 23.972  -16.884 -7.235  1 76.29 ? 672 PHE A CZ    1 
ATOM   5491  N  N     . HIS A 1 673 ? 27.563  -18.74  -13.041 1 74.62 ? 673 HIS A N     1 
ATOM   5492  C  CA    . HIS A 1 673 ? 28.704  -19.002 -13.892 1 75.18 ? 673 HIS A CA    1 
ATOM   5493  C  C     . HIS A 1 673 ? 29.674  -17.877 -13.638 1 75.45 ? 673 HIS A C     1 
ATOM   5494  O  O     . HIS A 1 673 ? 29.374  -16.735 -13.982 1 75.58 ? 673 HIS A O     1 
ATOM   5495  C  CB    . HIS A 1 673 ? 28.314  -19.029 -15.37  1 76.17 ? 673 HIS A CB    1 
ATOM   5496  C  CG    . HIS A 1 673 ? 29.499  -19.177 -16.273 1 78.91 ? 673 HIS A CG    1 
ATOM   5497  N  ND1   . HIS A 1 673 ? 30.008  -18.101 -16.979 1 80.87 ? 673 HIS A ND1   1 
ATOM   5498  C  CD2   . HIS A 1 673 ? 30.279  -20.258 -16.503 1 80.18 ? 673 HIS A CD2   1 
ATOM   5499  C  CE1   . HIS A 1 673 ? 31.054  -18.568 -17.642 1 81.4  ? 673 HIS A CE1   1 
ATOM   5500  N  NE2   . HIS A 1 673 ? 31.256  -19.861 -17.388 1 81.32 ? 673 HIS A NE2   1 
ATOM   5501  N  N     . ILE A 1 674 ? 30.81   -18.174 -13.005 1 75.43 ? 674 ILE A N     1 
ATOM   5502  C  CA    . ILE A 1 674 ? 31.799  -17.141 -12.737 1 75.94 ? 674 ILE A CA    1 
ATOM   5503  C  C     . ILE A 1 674 ? 32.843  -17.136 -13.851 1 76.45 ? 674 ILE A C     1 
ATOM   5504  O  O     . ILE A 1 674 ? 33.656  -18.053 -13.97  1 76.5  ? 674 ILE A O     1 
ATOM   5505  C  CB    . ILE A 1 674 ? 32.373  -17.209 -11.304 1 76.38 ? 674 ILE A CB    1 
ATOM   5506  C  CG1   . ILE A 1 674 ? 32.903  -18.612 -10.976 1 77.31 ? 674 ILE A CG1   1 
ATOM   5507  C  CG2   . ILE A 1 674 ? 31.302  -16.777 -10.301 1 76.8  ? 674 ILE A CG2   1 
ATOM   5508  C  CD1   . ILE A 1 674 ? 33.606  -18.709 -9.683  1 78.6  ? 674 ILE A CD1   1 
ATOM   5509  N  N     . GLU A 1 675 ? 32.742  -16.124 -14.725 1 76.64 ? 675 GLU A N     1 
ATOM   5510  C  CA    . GLU A 1 675 ? 33.61   -15.922 -15.885 1 77.26 ? 675 GLU A CA    1 
ATOM   5511  C  C     . GLU A 1 675 ? 35.077  -15.782 -15.478 1 77.71 ? 675 GLU A C     1 
ATOM   5512  O  O     . GLU A 1 675 ? 35.963  -16.31  -16.151 1 77.84 ? 675 GLU A O     1 
ATOM   5513  C  CB    . GLU A 1 675 ? 33.146  -14.677 -16.653 1 79.34 ? 675 GLU A CB    1 
ATOM   5514  C  CG    . GLU A 1 675 ? 33.943  -14.373 -17.907 1 83.65 ? 675 GLU A CG    1 
ATOM   5515  C  CD    . GLU A 1 675 ? 33.635  -13.024 -18.529 1 88.72 ? 675 GLU A CD    1 
ATOM   5516  O  OE1   . GLU A 1 675 ? 32.574  -12.442 -18.206 1 89.67 ? 675 GLU A OE1   1 
ATOM   5517  O  OE2   . GLU A 1 675 ? 34.46   -12.547 -19.341 1 90.28 ? 675 GLU A OE2   1 
ATOM   5518  N  N     . GLY A 1 676 ? 35.311  -15.096 -14.368 1 77.78 ? 676 GLY A N     1 
ATOM   5519  C  CA    . GLY A 1 676 ? 36.646  -14.886 -13.828 1 78.33 ? 676 GLY A CA    1 
ATOM   5520  C  C     . GLY A 1 676 ? 36.636  -14.015 -12.592 1 78.63 ? 676 GLY A C     1 
ATOM   5521  O  O     . GLY A 1 676 ? 35.699  -13.243 -12.388 1 78.79 ? 676 GLY A O     1 
ATOM   5522  O  "O5'" . DG  B 2 1   ? 11.483  18.46   -10.285 1 46.73 ? 1   DG  E "O5'" 1 
ATOM   5523  C  "C5'" . DG  B 2 1   ? 10.215  18.991  -10.686 1 46.81 ? 1   DG  E "C5'" 1 
ATOM   5524  C  "C4'" . DG  B 2 1   ? 9.063   18.081  -10.27  1 46.91 ? 1   DG  E "C4'" 1 
ATOM   5525  O  "O4'" . DG  B 2 1   ? 9.292   16.737  -10.768 1 46.82 ? 1   DG  E "O4'" 1 
ATOM   5526  C  "C3'" . DG  B 2 1   ? 8.854   17.943  -8.765  1 47.12 ? 1   DG  E "C3'" 1 
ATOM   5527  O  "O3'" . DG  B 2 1   ? 7.467   17.859  -8.452  1 47.42 ? 1   DG  E "O3'" 1 
ATOM   5528  C  "C2'" . DG  B 2 1   ? 9.568   16.644  -8.439  1 46.93 ? 1   DG  E "C2'" 1 
ATOM   5529  C  "C1'" . DG  B 2 1   ? 9.323   15.828  -9.692  1 46.63 ? 1   DG  E "C1'" 1 
ATOM   5530  N  N9    . DG  B 2 1   ? 10.375  14.862  -9.933  1 46.37 ? 1   DG  E N9    1 
ATOM   5531  C  C8    . DG  B 2 1   ? 11.728  15.103  -9.951  1 46.2  ? 1   DG  E C8    1 
ATOM   5532  N  N7    . DG  B 2 1   ? 12.444  14.022  -10.083 1 46.15 ? 1   DG  E N7    1 
ATOM   5533  C  C5    . DG  B 2 1   ? 11.505  12.996  -10.107 1 46.28 ? 1   DG  E C5    1 
ATOM   5534  C  C6    . DG  B 2 1   ? 11.678  11.597  -10.25  1 46.4  ? 1   DG  E C6    1 
ATOM   5535  O  O6    . DG  B 2 1   ? 12.738  10.96   -10.374 1 46.42 ? 1   DG  E O6    1 
ATOM   5536  N  N1    . DG  B 2 1   ? 10.454  10.922  -10.23  1 46.47 ? 1   DG  E N1    1 
ATOM   5537  C  C2    . DG  B 2 1   ? 9.223   11.526  -10.106 1 46.3  ? 1   DG  E C2    1 
ATOM   5538  N  N2    . DG  B 2 1   ? 8.157   10.712  -10.066 1 46.29 ? 1   DG  E N2    1 
ATOM   5539  N  N3    . DG  B 2 1   ? 9.051   12.831  -9.977  1 46.31 ? 1   DG  E N3    1 
ATOM   5540  C  C4    . DG  B 2 1   ? 10.23   13.501  -9.984  1 46.32 ? 1   DG  E C4    1 
ATOM   5541  P  P     . DT  B 2 2   ? 6.979   18.116  -6.943  1 47.53 ? 2   DT  E P     1 
ATOM   5542  O  OP1   . DT  B 2 2   ? 5.822   19.04   -6.99   1 47.73 ? 2   DT  E OP1   1 
ATOM   5543  O  OP2   . DT  B 2 2   ? 8.167   18.463  -6.125  1 47.37 ? 2   DT  E OP2   1 
ATOM   5544  O  "O5'" . DT  B 2 2   ? 6.449   16.684  -6.482  1 47.3  ? 2   DT  E "O5'" 1 
ATOM   5545  C  "C5'" . DT  B 2 2   ? 5.338   16.085  -7.122  1 47.14 ? 2   DT  E "C5'" 1 
ATOM   5546  C  "C4'" . DT  B 2 2   ? 5.269   14.619  -6.763  1 47.09 ? 2   DT  E "C4'" 1 
ATOM   5547  O  "O4'" . DT  B 2 2   ? 6.466   13.959  -7.258  1 47.06 ? 2   DT  E "O4'" 1 
ATOM   5548  C  "C3'" . DT  B 2 2   ? 5.217   14.334  -5.254  1 47.21 ? 2   DT  E "C3'" 1 
ATOM   5549  O  "O3'" . DT  B 2 2   ? 4.155   13.424  -4.948  1 47.24 ? 2   DT  E "O3'" 1 
ATOM   5550  C  "C2'" . DT  B 2 2   ? 6.587   13.723  -4.955  1 47.26 ? 2   DT  E "C2'" 1 
ATOM   5551  C  "C1'" . DT  B 2 2   ? 6.938   13.074  -6.279  1 47.16 ? 2   DT  E "C1'" 1 
ATOM   5552  N  N1    . DT  B 2 2   ? 8.416   12.863  -6.459  1 47.25 ? 2   DT  E N1    1 
ATOM   5553  C  C2    . DT  B 2 2   ? 8.88    11.608  -6.795  1 47.45 ? 2   DT  E C2    1 
ATOM   5554  O  O2    . DT  B 2 2   ? 8.144   10.661  -7.019  1 47.64 ? 2   DT  E O2    1 
ATOM   5555  N  N3    . DT  B 2 2   ? 10.248  11.494  -6.841  1 47.39 ? 2   DT  E N3    1 
ATOM   5556  C  C4    . DT  B 2 2   ? 11.18   12.489  -6.593  1 47.28 ? 2   DT  E C4    1 
ATOM   5557  O  O4    . DT  B 2 2   ? 12.379  12.235  -6.685  1 47.24 ? 2   DT  E O4    1 
ATOM   5558  C  C5    . DT  B 2 2   ? 10.628  13.774  -6.234  1 47.14 ? 2   DT  E C5    1 
ATOM   5559  C  C7    . DT  B 2 2   ? 11.541  14.925  -5.935  1 47.04 ? 2   DT  E C7    1 
ATOM   5560  C  C6    . DT  B 2 2   ? 9.29    13.892  -6.164  1 47.16 ? 2   DT  E C6    1 
ATOM   5561  P  P     . DC  B 2 3   ? 3.641   13.226  -3.428  1 47.29 ? 3   DC  E P     1 
ATOM   5562  O  OP1   . DC  B 2 3   ? 2.255   13.738  -3.342  1 47.34 ? 3   DC  E OP1   1 
ATOM   5563  O  OP2   . DC  B 2 3   ? 4.677   13.732  -2.492  1 47.22 ? 3   DC  E OP2   1 
ATOM   5564  O  "O5'" . DC  B 2 3   ? 3.57    11.642  -3.312  1 47.04 ? 3   DC  E "O5'" 1 
ATOM   5565  C  "C5'" . DC  B 2 3   ? 3.014   10.91   -4.379  1 46.65 ? 3   DC  E "C5'" 1 
ATOM   5566  C  "C4'" . DC  B 2 3   ? 3.723   9.594   -4.539  1 46.28 ? 3   DC  E "C4'" 1 
ATOM   5567  O  "O4'" . DC  B 2 3   ? 5.082   9.843   -4.918  1 46.57 ? 3   DC  E "O4'" 1 
ATOM   5568  C  "C3'" . DC  B 2 3   ? 3.831   8.787   -3.268  1 45.78 ? 3   DC  E "C3'" 1 
ATOM   5569  O  "O3'" . DC  B 2 3   ? 2.653   7.979   -3.11   1 44.63 ? 3   DC  E "O3'" 1 
ATOM   5570  C  "C2'" . DC  B 2 3   ? 5.081   7.93    -3.518  1 46.27 ? 3   DC  E "C2'" 1 
ATOM   5571  C  "C1'" . DC  B 2 3   ? 5.867   8.73    -4.562  1 46.68 ? 3   DC  E "C1'" 1 
ATOM   5572  N  N1    . DC  B 2 3   ? 7.202   9.219   -4.1    1 47.17 ? 3   DC  E N1    1 
ATOM   5573  C  C2    . DC  B 2 3   ? 8.311   8.372   -4.173  1 47.38 ? 3   DC  E C2    1 
ATOM   5574  O  O2    . DC  B 2 3   ? 8.147   7.203   -4.536  1 47.56 ? 3   DC  E O2    1 
ATOM   5575  N  N3    . DC  B 2 3   ? 9.534   8.857   -3.83   1 47.34 ? 3   DC  E N3    1 
ATOM   5576  C  C4    . DC  B 2 3   ? 9.665   10.132  -3.454  1 47.27 ? 3   DC  E C4    1 
ATOM   5577  N  N4    . DC  B 2 3   ? 10.885  10.568  -3.12   1 47.15 ? 3   DC  E N4    1 
ATOM   5578  C  C5    . DC  B 2 3   ? 8.551   11.02   -3.414  1 47.28 ? 3   DC  E C5    1 
ATOM   5579  C  C6    . DC  B 2 3   ? 7.348   10.519  -3.716  1 47.26 ? 3   DC  E C6    1 
ATOM   5580  P  P     . DT  B 2 4   ? 1.809   8.028   -1.747  1 43.17 ? 4   DT  E P     1 
ATOM   5581  O  OP1   . DT  B 2 4   ? 0.465   7.467   -2.026  1 43.06 ? 4   DT  E OP1   1 
ATOM   5582  O  OP2   . DT  B 2 4   ? 1.937   9.388   -1.177  1 43.09 ? 4   DT  E OP2   1 
ATOM   5583  O  "O5'" . DT  B 2 4   ? 2.612   7.018   -0.803  1 42.07 ? 4   DT  E "O5'" 1 
ATOM   5584  C  "C5'" . DT  B 2 4   ? 2.896   5.703   -1.256  1 41.01 ? 4   DT  E "C5'" 1 
ATOM   5585  C  "C4'" . DT  B 2 4   ? 4.179   5.182   -0.644  1 39.94 ? 4   DT  E "C4'" 1 
ATOM   5586  O  "O4'" . DT  B 2 4   ? 5.287   6.028   -1.022  1 39.46 ? 4   DT  E "O4'" 1 
ATOM   5587  C  "C3'" . DT  B 2 4   ? 4.189   5.108   0.877   1 39.42 ? 4   DT  E "C3'" 1 
ATOM   5588  O  "O3'" . DT  B 2 4   ? 4.684   3.857   1.292   1 39.02 ? 4   DT  E "O3'" 1 
ATOM   5589  C  "C2'" . DT  B 2 4   ? 5.126   6.236   1.281   1 39.36 ? 4   DT  E "C2'" 1 
ATOM   5590  C  "C1'" . DT  B 2 4   ? 6.077   6.294   0.103   1 39.39 ? 4   DT  E "C1'" 1 
ATOM   5591  N  N1    . DT  B 2 4   ? 6.696   7.631   -0.059  1 39.58 ? 4   DT  E N1    1 
ATOM   5592  C  C2    . DT  B 2 4   ? 8.06    7.759   0.057   1 39.61 ? 4   DT  E C2    1 
ATOM   5593  O  O2    . DT  B 2 4   ? 8.813   6.813   0.193   1 39.45 ? 4   DT  E O2    1 
ATOM   5594  N  N3    . DT  B 2 4   ? 8.517   9.045   -0.029  1 39.69 ? 4   DT  E N3    1 
ATOM   5595  C  C4    . DT  B 2 4   ? 7.759   10.195  -0.158  1 39.61 ? 4   DT  E C4    1 
ATOM   5596  O  O4    . DT  B 2 4   ? 8.32    11.281  -0.213  1 39.68 ? 4   DT  E O4    1 
ATOM   5597  C  C5    . DT  B 2 4   ? 6.336   9.992   -0.26   1 39.5  ? 4   DT  E C5    1 
ATOM   5598  C  C7    . DT  B 2 4   ? 5.414   11.161  -0.434  1 39.49 ? 4   DT  E C7    1 
ATOM   5599  C  C6    . DT  B 2 4   ? 5.877   8.74    -0.161  1 39.59 ? 4   DT  E C6    1 
ATOM   5600  P  P     . DG  B 2 5   ? 4.282   3.286   2.724   1 38.51 ? 5   DG  E P     1 
ATOM   5601  O  OP1   . DG  B 2 5   ? 3.414   2.102   2.509   1 38.57 ? 5   DG  E OP1   1 
ATOM   5602  O  OP2   . DG  B 2 5   ? 3.793   4.423   3.543   1 38.47 ? 5   DG  E OP2   1 
ATOM   5603  O  "O5'" . DG  B 2 5   ? 5.688   2.809   3.33    1 37.74 ? 5   DG  E "O5'" 1 
ATOM   5604  C  "C5'" . DG  B 2 5   ? 6.315   1.615   2.844   1 36.91 ? 5   DG  E "C5'" 1 
ATOM   5605  C  "C4'" . DG  B 2 5   ? 7.816   1.795   2.702   1 36.08 ? 5   DG  E "C4'" 1 
ATOM   5606  O  "O4'" . DG  B 2 5   ? 8.084   2.932   1.848   1 35.56 ? 5   DG  E "O4'" 1 
ATOM   5607  C  "C3'" . DG  B 2 5   ? 8.576   2.126   3.977   1 35.84 ? 5   DG  E "C3'" 1 
ATOM   5608  O  "O3'" . DG  B 2 5   ? 8.849   0.948   4.733   1 36.15 ? 5   DG  E "O3'" 1 
ATOM   5609  C  "C2'" . DG  B 2 5   ? 9.855   2.701   3.394   1 35.37 ? 5   DG  E "C2'" 1 
ATOM   5610  C  "C1'" . DG  B 2 5   ? 9.317   3.518   2.23    1 35.11 ? 5   DG  E "C1'" 1 
ATOM   5611  N  N9    . DG  B 2 5   ? 9.117   4.924   2.571   1 34.38 ? 5   DG  E N9    1 
ATOM   5612  C  C8    . DG  B 2 5   ? 7.948   5.545   2.934   1 34.05 ? 5   DG  E C8    1 
ATOM   5613  N  N7    . DG  B 2 5   ? 8.102   6.811   3.205   1 33.8  ? 5   DG  E N7    1 
ATOM   5614  C  C5    . DG  B 2 5   ? 9.473   7.007   3.107   1 33.72 ? 5   DG  E C5    1 
ATOM   5615  C  C6    . DG  B 2 5   ? 10.247  8.162   3.321   1 33.59 ? 5   DG  E C6    1 
ATOM   5616  O  O6    . DG  B 2 5   ? 9.865   9.286   3.656   1 33.68 ? 5   DG  E O6    1 
ATOM   5617  N  N1    . DG  B 2 5   ? 11.605  7.919   3.114   1 33.48 ? 5   DG  E N1    1 
ATOM   5618  C  C2    . DG  B 2 5   ? 12.139  6.705   2.761   1 33.44 ? 5   DG  E C2    1 
ATOM   5619  N  N2    . DG  B 2 5   ? 13.465  6.657   2.584   1 33.33 ? 5   DG  E N2    1 
ATOM   5620  N  N3    . DG  B 2 5   ? 11.42   5.633   2.527   1 33.65 ? 5   DG  E N3    1 
ATOM   5621  C  C4    . DG  B 2 5   ? 10.104  5.851   2.733   1 33.92 ? 5   DG  E C4    1 
ATOM   5622  P  P     . DC  B 2 6   ? 9.085   1.035   6.323   1 36.2  ? 6   DC  E P     1 
ATOM   5623  O  OP1   . DC  B 2 6   ? 9.283   -0.347  6.823   1 36.06 ? 6   DC  E OP1   1 
ATOM   5624  O  OP2   . DC  B 2 6   ? 8.016   1.885   6.893   1 36.15 ? 6   DC  E OP2   1 
ATOM   5625  O  "O5'" . DC  B 2 6   ? 10.47   1.839   6.459   1 36.38 ? 6   DC  E "O5'" 1 
ATOM   5626  C  "C5'" . DC  B 2 6   ? 11.673  1.305   5.887   1 36.28 ? 6   DC  E "C5'" 1 
ATOM   5627  C  "C4'" . DC  B 2 6   ? 12.837  2.278   6.034   1 35.91 ? 6   DC  E "C4'" 1 
ATOM   5628  O  "O4'" . DC  B 2 6   ? 12.587  3.469   5.247   1 35.63 ? 6   DC  E "O4'" 1 
ATOM   5629  C  "C3'" . DC  B 2 6   ? 13.059  2.822   7.43    1 35.76 ? 6   DC  E "C3'" 1 
ATOM   5630  O  "O3'" . DC  B 2 6   ? 13.751  1.894   8.243   1 36.02 ? 6   DC  E "O3'" 1 
ATOM   5631  C  "C2'" . DC  B 2 6   ? 13.901  4.051   7.134   1 35.51 ? 6   DC  E "C2'" 1 
ATOM   5632  C  "C1'" . DC  B 2 6   ? 13.231  4.579   5.865   1 35.51 ? 6   DC  E "C1'" 1 
ATOM   5633  N  N1    . DC  B 2 6   ? 12.217  5.66    6.135   1 35.52 ? 6   DC  E N1    1 
ATOM   5634  C  C2    . DC  B 2 6   ? 12.647  6.985   6.299   1 35.58 ? 6   DC  E C2    1 
ATOM   5635  O  O2    . DC  B 2 6   ? 13.849  7.25    6.171   1 35.78 ? 6   DC  E O2    1 
ATOM   5636  N  N3    . DC  B 2 6   ? 11.73   7.948   6.563   1 35.37 ? 6   DC  E N3    1 
ATOM   5637  C  C4    . DC  B 2 6   ? 10.444  7.624   6.686   1 35.28 ? 6   DC  E C4    1 
ATOM   5638  N  N4    . DC  B 2 6   ? 9.578   8.603   6.952   1 35.07 ? 6   DC  E N4    1 
ATOM   5639  C  C5    . DC  B 2 6   ? 9.988   6.277   6.548   1 35.4  ? 6   DC  E C5    1 
ATOM   5640  C  C6    . DC  B 2 6   ? 10.897  5.341   6.267   1 35.45 ? 6   DC  E C6    1 
ATOM   5641  P  P     . DA  B 2 7   ? 13.588  1.995   9.824   1 36.4  ? 7   DA  E P     1 
ATOM   5642  O  OP1   . DA  B 2 7   ? 13.901  0.673   10.426  1 36.39 ? 7   DA  E OP1   1 
ATOM   5643  O  OP2   . DA  B 2 7   ? 12.274  2.628   10.089  1 36.56 ? 7   DA  E OP2   1 
ATOM   5644  O  "O5'" . DA  B 2 7   ? 14.75   3.031   10.205  1 36.63 ? 7   DA  E "O5'" 1 
ATOM   5645  C  "C5'" . DA  B 2 7   ? 14.528  4.034   11.177  1 36.81 ? 7   DA  E "C5'" 1 
ATOM   5646  C  "C4'" . DA  B 2 7   ? 15.254  5.31    10.823  1 36.96 ? 7   DA  E "C4'" 1 
ATOM   5647  O  "O4'" . DA  B 2 7   ? 14.5    6.032   9.827   1 36.78 ? 7   DA  E "O4'" 1 
ATOM   5648  C  "C3'" . DA  B 2 7   ? 15.417  6.251   11.99   1 37.21 ? 7   DA  E "C3'" 1 
ATOM   5649  O  "O3'" . DA  B 2 7   ? 16.666  6.011   12.577  1 37.89 ? 7   DA  E "O3'" 1 
ATOM   5650  C  "C2'" . DA  B 2 7   ? 15.361  7.639   11.356  1 36.93 ? 7   DA  E "C2'" 1 
ATOM   5651  C  "C1'" . DA  B 2 7   ? 14.562  7.419   10.072  1 36.61 ? 7   DA  E "C1'" 1 
ATOM   5652  N  N9    . DA  B 2 7   ? 13.196  7.93    10.116  1 36.16 ? 7   DA  E N9    1 
ATOM   5653  C  C8    . DA  B 2 7   ? 12.046  7.191   10.083  1 36.12 ? 7   DA  E C8    1 
ATOM   5654  N  N7    . DA  B 2 7   ? 10.952  7.914   10.075  1 35.95 ? 7   DA  E N7    1 
ATOM   5655  C  C5    . DA  B 2 7   ? 11.416  9.216   10.079  1 35.54 ? 7   DA  E C5    1 
ATOM   5656  C  C6    . DA  B 2 7   ? 10.753  10.451  10.059  1 35.17 ? 7   DA  E C6    1 
ATOM   5657  N  N6    . DA  B 2 7   ? 9.424   10.57   10.045  1 35.03 ? 7   DA  E N6    1 
ATOM   5658  N  N1    . DA  B 2 7   ? 11.51   11.563  10.064  1 35.15 ? 7   DA  E N1    1 
ATOM   5659  C  C2    . DA  B 2 7   ? 12.844  11.436  10.09   1 35.22 ? 7   DA  E C2    1 
ATOM   5660  N  N3    . DA  B 2 7   ? 13.581  10.331  10.105  1 35.33 ? 7   DA  E N3    1 
ATOM   5661  C  C4    . DA  B 2 7   ? 12.799  9.245   10.095  1 35.64 ? 7   DA  E C4    1 
ATOM   5662  P  P     . DT  B 2 8   ? 16.82   6.023   14.157  1 38.57 ? 8   DT  E P     1 
ATOM   5663  O  OP1   . DT  B 2 8   ? 17.792  4.965   14.526  1 38.52 ? 8   DT  E OP1   1 
ATOM   5664  O  OP2   . DT  B 2 8   ? 15.461  6.017   14.748  1 38.63 ? 8   DT  E OP2   1 
ATOM   5665  O  "O5'" . DT  B 2 8   ? 17.477  7.463   14.415  1 39.14 ? 8   DT  E "O5'" 1 
ATOM   5666  C  "C5'" . DT  B 2 8   ? 18.479  7.965   13.517  1 39.61 ? 8   DT  E "C5'" 1 
ATOM   5667  C  "C4'" . DT  B 2 8   ? 18.399  9.48    13.373  1 40.27 ? 8   DT  E "C4'" 1 
ATOM   5668  O  "O4'" . DT  B 2 8   ? 17.062  9.874   12.965  1 40.34 ? 8   DT  E "O4'" 1 
ATOM   5669  C  "C3'" . DT  B 2 8   ? 18.709  10.287  14.64   1 40.89 ? 8   DT  E "C3'" 1 
ATOM   5670  O  "O3'" . DT  B 2 8   ? 19.487  11.419  14.307  1 41.76 ? 8   DT  E "O3'" 1 
ATOM   5671  C  "C2'" . DT  B 2 8   ? 17.328  10.698  15.138  1 40.6  ? 8   DT  E "C2'" 1 
ATOM   5672  C  "C1'" . DT  B 2 8   ? 16.584  10.885  13.831  1 40.36 ? 8   DT  E "C1'" 1 
ATOM   5673  N  N1    . DT  B 2 8   ? 15.12   10.729  13.979  1 40.18 ? 8   DT  E N1    1 
ATOM   5674  C  C2    . DT  B 2 8   ? 14.297  11.769  13.636  1 40.17 ? 8   DT  E C2    1 
ATOM   5675  O  O2    . DT  B 2 8   ? 14.707  12.809  13.156  1 40.26 ? 8   DT  E O2    1 
ATOM   5676  N  N3    . DT  B 2 8   ? 12.962  11.53   13.828  1 40.11 ? 8   DT  E N3    1 
ATOM   5677  C  C4    . DT  B 2 8   ? 12.385  10.383  14.341  1 40.02 ? 8   DT  E C4    1 
ATOM   5678  O  O4    . DT  B 2 8   ? 11.166  10.323  14.461  1 39.95 ? 8   DT  E O4    1 
ATOM   5679  C  C5    . DT  B 2 8   ? 13.314  9.338   14.702  1 40.03 ? 8   DT  E C5    1 
ATOM   5680  C  C7    . DT  B 2 8   ? 12.819  8.047   15.27   1 40.11 ? 8   DT  E C7    1 
ATOM   5681  C  C6    . DT  B 2 8   ? 14.619  9.566   14.52   1 40.08 ? 8   DT  E C6    1 
ATOM   5682  P  P     . DT  B 2 9   ? 20.128  12.326  15.461  1 42.64 ? 9   DT  E P     1 
ATOM   5683  O  OP1   . DT  B 2 9   ? 21.462  12.767  14.997  1 42.89 ? 9   DT  E OP1   1 
ATOM   5684  O  OP2   . DT  B 2 9   ? 19.997  11.607  16.749  1 42.56 ? 9   DT  E OP2   1 
ATOM   5685  O  "O5'" . DT  B 2 9   ? 19.151  13.597  15.498  1 43.04 ? 9   DT  E "O5'" 1 
ATOM   5686  C  "C5'" . DT  B 2 9   ? 19.106  14.488  14.387  1 43.25 ? 9   DT  E "C5'" 1 
ATOM   5687  C  "C4'" . DT  B 2 9   ? 18.033  15.544  14.567  1 43.5  ? 9   DT  E "C4'" 1 
ATOM   5688  O  "O4'" . DT  B 2 9   ? 16.726  14.925  14.687  1 43.34 ? 9   DT  E "O4'" 1 
ATOM   5689  C  "C3'" . DT  B 2 9   ? 18.19   16.444  15.794  1 44.1  ? 9   DT  E "C3'" 1 
ATOM   5690  O  "O3'" . DT  B 2 9   ? 17.979  17.799  15.399  1 45.05 ? 9   DT  E "O3'" 1 
ATOM   5691  C  "C2'" . DT  B 2 9   ? 17.073  15.952  16.713  1 43.74 ? 9   DT  E "C2'" 1 
ATOM   5692  C  "C1'" . DT  B 2 9   ? 16.017  15.588  15.696  1 43.35 ? 9   DT  E "C1'" 1 
ATOM   5693  N  N1    . DT  B 2 9   ? 14.96   14.688  16.224  1 43.23 ? 9   DT  E N1    1 
ATOM   5694  C  C2    . DT  B 2 9   ? 13.65   15.085  16.142  1 43.09 ? 9   DT  E C2    1 
ATOM   5695  O  O2    . DT  B 2 9   ? 13.309  16.142  15.65   1 42.93 ? 9   DT  E O2    1 
ATOM   5696  N  N3    . DT  B 2 9   ? 12.747  14.204  16.68   1 43.27 ? 9   DT  E N3    1 
ATOM   5697  C  C4    . DT  B 2 9   ? 13.023  12.985  17.283  1 43.4  ? 9   DT  E C4    1 
ATOM   5698  O  O4    . DT  B 2 9   ? 12.1    12.301  17.72   1 43.4  ? 9   DT  E O4    1 
ATOM   5699  C  C5    . DT  B 2 9   ? 14.423  12.628  17.338  1 43.43 ? 9   DT  E C5    1 
ATOM   5700  C  C7    . DT  B 2 9   ? 14.847  11.326  17.957  1 43.36 ? 9   DT  E C7    1 
ATOM   5701  C  C6    . DT  B 2 9   ? 15.315  13.493  16.822  1 43.38 ? 9   DT  E C6    1 
ATOM   5702  P  P     . DC  B 2 10  ? 18.258  19.025  16.399  1 45.83 ? 10  DC  E P     1 
ATOM   5703  O  OP1   . DC  B 2 10  ? 19.189  19.957  15.719  1 45.93 ? 10  DC  E OP1   1 
ATOM   5704  O  OP2   . DC  B 2 10  ? 18.597  18.489  17.739  1 45.73 ? 10  DC  E OP2   1 
ATOM   5705  O  "O5'" . DC  B 2 10  ? 16.818  19.711  16.492  1 46.43 ? 10  DC  E "O5'" 1 
ATOM   5706  C  "C5'" . DC  B 2 10  ? 16.065  19.935  15.297  1 47    ? 10  DC  E "C5'" 1 
ATOM   5707  C  "C4'" . DC  B 2 10  ? 14.654  20.415  15.607  1 47.51 ? 10  DC  E "C4'" 1 
ATOM   5708  O  "O4'" . DC  B 2 10  ? 13.851  19.307  16.08   1 47.44 ? 10  DC  E "O4'" 1 
ATOM   5709  C  "C3'" . DC  B 2 10  ? 14.545  21.5    16.674  1 48    ? 10  DC  E "C3'" 1 
ATOM   5710  O  "O3'" . DC  B 2 10  ? 13.52   22.415  16.327  1 48.78 ? 10  DC  E "O3'" 1 
ATOM   5711  C  "C2'" . DC  B 2 10  ? 14.184  20.714  17.928  1 47.64 ? 10  DC  E "C2'" 1 
ATOM   5712  C  "C1'" . DC  B 2 10  ? 13.316  19.61   17.353  1 47.27 ? 10  DC  E "C1'" 1 
ATOM   5713  N  N1    . DC  B 2 10  ? 13.337  18.378  18.155  1 46.65 ? 10  DC  E N1    1 
ATOM   5714  C  C2    . DC  B 2 10  ? 12.142  17.842  18.614  1 46.37 ? 10  DC  E C2    1 
ATOM   5715  O  O2    . DC  B 2 10  ? 11.086  18.432  18.36   1 46.14 ? 10  DC  E O2    1 
ATOM   5716  N  N3    . DC  B 2 10  ? 12.173  16.694  19.334  1 46.49 ? 10  DC  E N3    1 
ATOM   5717  C  C4    . DC  B 2 10  ? 13.342  16.1    19.593  1 46.56 ? 10  DC  E C4    1 
ATOM   5718  N  N4    . DC  B 2 10  ? 13.331  14.969  20.307  1 46.59 ? 10  DC  E N4    1 
ATOM   5719  C  C5    . DC  B 2 10  ? 14.575  16.65   19.146  1 46.54 ? 10  DC  E C5    1 
ATOM   5720  C  C6    . DC  B 2 10  ? 14.524  17.774  18.428  1 46.54 ? 10  DC  E C6    1 
ATOM   5721  P  P     . DC  B 2 11  ? 13.439  23.833  17.056  1 49.57 ? 11  DC  E P     1 
ATOM   5722  O  OP1   . DC  B 2 11  ? 13.056  24.842  16.042  1 49.61 ? 11  DC  E OP1   1 
ATOM   5723  O  OP2   . DC  B 2 11  ? 14.676  24.015  17.85   1 49.63 ? 11  DC  E OP2   1 
ATOM   5724  O  "O5'" . DC  B 2 11  ? 12.23   23.631  18.077  1 50.21 ? 11  DC  E "O5'" 1 
ATOM   5725  C  "C5'" . DC  B 2 11  ? 10.908  23.479  17.586  1 50.91 ? 11  DC  E "C5'" 1 
ATOM   5726  C  "C4'" . DC  B 2 11  ? 9.952   23.107  18.705  1 51.63 ? 11  DC  E "C4'" 1 
ATOM   5727  O  "O4'" . DC  B 2 11  ? 10.284  21.788  19.218  1 51.57 ? 11  DC  E "O4'" 1 
ATOM   5728  C  "C3'" . DC  B 2 11  ? 9.95    24.049  19.922  1 52.26 ? 11  DC  E "C3'" 1 
ATOM   5729  O  "O3'" . DC  B 2 11  ? 8.602   24.313  20.31   1 53.33 ? 11  DC  E "O3'" 1 
ATOM   5730  C  "C2'" . DC  B 2 11  ? 10.676  23.221  20.983  1 51.86 ? 11  DC  E "C2'" 1 
ATOM   5731  C  "C1'" . DC  B 2 11  ? 10.193  21.833  20.616  1 51.47 ? 11  DC  E "C1'" 1 
ATOM   5732  N  N1    . DC  B 2 11  ? 10.996  20.731  21.191  1 50.99 ? 11  DC  E N1    1 
ATOM   5733  C  C2    . DC  B 2 11  ? 10.357  19.761  21.957  1 50.7  ? 11  DC  E C2    1 
ATOM   5734  O  O2    . DC  B 2 11  ? 9.135   19.844  22.116  1 50.51 ? 11  DC  E O2    1 
ATOM   5735  N  N3    . DC  B 2 11  ? 11.088  18.745  22.474  1 50.63 ? 11  DC  E N3    1 
ATOM   5736  C  C4    . DC  B 2 11  ? 12.408  18.703  22.269  1 50.64 ? 11  DC  E C4    1 
ATOM   5737  N  N4    . DC  B 2 11  ? 13.094  17.69   22.804  1 50.67 ? 11  DC  E N4    1 
ATOM   5738  C  C5    . DC  B 2 11  ? 13.082  19.703  21.512  1 50.68 ? 11  DC  E C5    1 
ATOM   5739  C  C6    . DC  B 2 11  ? 12.343  20.689  20.994  1 50.82 ? 11  DC  E C6    1 
ATOM   5740  P  P     . DT  B 2 12  ? 8.21    25.654  21.092  1 54.54 ? 12  DT  E P     1 
ATOM   5741  O  OP1   . DT  B 2 12  ? 7.724   26.63   20.095  1 54.62 ? 12  DT  E OP1   1 
ATOM   5742  O  OP2   . DT  B 2 12  ? 9.327   26.015  22      1 54.41 ? 12  DT  E OP2   1 
ATOM   5743  O  "O5'" . DT  B 2 12  ? 6.973   25.177  21.99   1 55.98 ? 12  DT  E "O5'" 1 
ATOM   5744  C  "C5'" . DT  B 2 12  ? 5.988   24.296  21.429  1 57.4  ? 12  DT  E "C5'" 1 
ATOM   5745  C  "C4'" . DT  B 2 12  ? 5.413   23.35   22.479  1 58.65 ? 12  DT  E "C4'" 1 
ATOM   5746  O  "O4'" . DT  B 2 12  ? 6.4     22.338  22.82   1 59.01 ? 12  DT  E "O4'" 1 
ATOM   5747  C  "C3'" . DT  B 2 12  ? 4.995   24.014  23.795  1 59.53 ? 12  DT  E "C3'" 1 
ATOM   5748  O  "O3'" . DT  B 2 12  ? 3.696   23.58   24.187  1 60.53 ? 12  DT  E "O3'" 1 
ATOM   5749  C  "C2'" . DT  B 2 12  ? 6.063   23.56   24.785  1 59.48 ? 12  DT  E "C2'" 1 
ATOM   5750  C  "C1'" . DT  B 2 12  ? 6.473   22.209  24.221  1 59.4  ? 12  DT  E "C1'" 1 
ATOM   5751  N  N1    . DT  B 2 12  ? 7.865   21.816  24.601  1 59.65 ? 12  DT  E N1    1 
ATOM   5752  C  C2    . DT  B 2 12  ? 8.072   20.608  25.226  1 59.82 ? 12  DT  E C2    1 
ATOM   5753  O  O2    . DT  B 2 12  ? 7.191   19.782  25.39   1 59.78 ? 12  DT  E O2    1 
ATOM   5754  N  N3    . DT  B 2 12  ? 9.378   20.359  25.563  1 59.96 ? 12  DT  E N3    1 
ATOM   5755  C  C4    . DT  B 2 12  ? 10.463  21.208  25.4    1 59.96 ? 12  DT  E C4    1 
ATOM   5756  O  O4    . DT  B 2 12  ? 11.577  20.848  25.768  1 60.15 ? 12  DT  E O4    1 
ATOM   5757  C  C5    . DT  B 2 12  ? 10.164  22.482  24.793  1 59.65 ? 12  DT  E C5    1 
ATOM   5758  C  C7    . DT  B 2 12  ? 11.255  23.487  24.579  1 59.47 ? 12  DT  E C7    1 
ATOM   5759  C  C6    . DT  B 2 12  ? 8.894   22.729  24.441  1 59.61 ? 12  DT  E C6    1 
ATOM   5760  P  P     . DC  B 2 13  ? 2.843   24.441  25.246  1 61.64 ? 13  DC  E P     1 
ATOM   5761  O  OP1   . DC  B 2 13  ? 1.454   24.534  24.734  1 61.9  ? 13  DC  E OP1   1 
ATOM   5762  O  OP2   . DC  B 2 13  ? 3.594   25.688  25.542  1 61.68 ? 13  DC  E OP2   1 
ATOM   5763  O  "O5'" . DC  B 2 13  ? 2.864   23.522  26.573  1 62.08 ? 13  DC  E "O5'" 1 
ATOM   5764  C  "C5'" . DC  B 2 13  ? 1.917   22.448  26.735  1 62.56 ? 13  DC  E "C5'" 1 
ATOM   5765  C  "C4'" . DC  B 2 13  ? 2.358   21.472  27.814  1 63.07 ? 13  DC  E "C4'" 1 
ATOM   5766  O  "O4'" . DC  B 2 13  ? 3.662   20.952  27.493  1 63.37 ? 13  DC  E "O4'" 1 
ATOM   5767  C  "C3'" . DC  B 2 13  ? 2.523   22.069  29.201  1 63.27 ? 13  DC  E "C3'" 1 
ATOM   5768  O  "O3'" . DC  B 2 13  ? 1.268   22.097  29.876  1 63.27 ? 13  DC  E "O3'" 1 
ATOM   5769  C  "C2'" . DC  B 2 13  ? 3.493   21.088  29.867  1 63.42 ? 13  DC  E "C2'" 1 
ATOM   5770  C  "C1'" . DC  B 2 13  ? 4.305   20.537  28.684  1 63.58 ? 13  DC  E "C1'" 1 
ATOM   5771  N  N1    . DC  B 2 13  ? 5.726   21.01   28.656  1 63.85 ? 13  DC  E N1    1 
ATOM   5772  C  C2    . DC  B 2 13  ? 6.735   20.19   29.173  1 63.88 ? 13  DC  E C2    1 
ATOM   5773  O  O2    . DC  B 2 13  ? 6.434   19.079  29.629  1 63.86 ? 13  DC  E O2    1 
ATOM   5774  N  N3    . DC  B 2 13  ? 8.019   20.631  29.145  1 63.89 ? 13  DC  E N3    1 
ATOM   5775  C  C4    . DC  B 2 13  ? 8.303   21.833  28.637  1 63.85 ? 13  DC  E C4    1 
ATOM   5776  N  N4    . DC  B 2 13  ? 9.582   22.226  28.632  1 63.8  ? 13  DC  E N4    1 
ATOM   5777  C  C5    . DC  B 2 13  ? 7.286   22.69   28.122  1 63.86 ? 13  DC  E C5    1 
ATOM   5778  C  C6    . DC  B 2 13  ? 6.025   22.245  28.154  1 63.87 ? 13  DC  E C6    1 
ATOM   5779  O  "O5'" . DG  C 3 1   ? 17.465  13.977  34.054  1 55.98 ? 1   DG  F "O5'" 1 
ATOM   5780  C  "C5'" . DG  C 3 1   ? 16.909  15.049  33.287  1 55.85 ? 1   DG  F "C5'" 1 
ATOM   5781  C  "C4'" . DG  C 3 1   ? 15.412  14.864  33.104  1 55.6  ? 1   DG  F "C4'" 1 
ATOM   5782  O  "O4'" . DG  C 3 1   ? 14.803  16.116  32.676  1 55.51 ? 1   DG  F "O4'" 1 
ATOM   5783  C  "C3'" . DG  C 3 1   ? 15.006  13.831  32.05   1 55.32 ? 1   DG  F "C3'" 1 
ATOM   5784  O  "O3'" . DG  C 3 1   ? 13.831  13.178  32.48   1 55.03 ? 1   DG  F "O3'" 1 
ATOM   5785  C  "C2'" . DG  C 3 1   ? 14.722  14.706  30.837  1 55.35 ? 1   DG  F "C2'" 1 
ATOM   5786  C  "C1'" . DG  C 3 1   ? 14.037  15.869  31.518  1 55.31 ? 1   DG  F "C1'" 1 
ATOM   5787  N  N9    . DG  C 3 1   ? 13.976  17.081  30.714  1 54.98 ? 1   DG  F N9    1 
ATOM   5788  C  C8    . DG  C 3 1   ? 15.017  17.718  30.083  1 54.88 ? 1   DG  F C8    1 
ATOM   5789  N  N7    . DG  C 3 1   ? 14.651  18.789  29.434  1 54.8  ? 1   DG  F N7    1 
ATOM   5790  C  C5    . DG  C 3 1   ? 13.282  18.876  29.67   1 54.76 ? 1   DG  F C5    1 
ATOM   5791  C  C6    . DG  C 3 1   ? 12.334  19.833  29.229  1 54.73 ? 1   DG  F C6    1 
ATOM   5792  O  O6    . DG  C 3 1   ? 12.523  20.837  28.521  1 54.68 ? 1   DG  F O6    1 
ATOM   5793  N  N1    . DG  C 3 1   ? 11.054  19.545  29.706  1 54.64 ? 1   DG  F N1    1 
ATOM   5794  C  C2    . DG  C 3 1   ? 10.73   18.461  30.487  1 54.54 ? 1   DG  F C2    1 
ATOM   5795  N  N2    . DG  C 3 1   ? 9.442   18.342  30.835  1 54.54 ? 1   DG  F N2    1 
ATOM   5796  N  N3    . DG  C 3 1   ? 11.606  17.558  30.9    1 54.58 ? 1   DG  F N3    1 
ATOM   5797  C  C4    . DG  C 3 1   ? 12.856  17.827  30.452  1 54.74 ? 1   DG  F C4    1 
ATOM   5798  P  P     . DA  C 3 2   ? 13.469  11.718  31.937  1 54.74 ? 2   DA  F P     1 
ATOM   5799  O  OP1   . DA  C 3 2   ? 13.41   10.809  33.114  1 55.14 ? 2   DA  F OP1   1 
ATOM   5800  O  OP2   . DA  C 3 2   ? 14.376  11.403  30.805  1 54.7  ? 2   DA  F OP2   1 
ATOM   5801  O  "O5'" . DA  C 3 2   ? 11.986  11.917  31.345  1 53.52 ? 2   DA  F "O5'" 1 
ATOM   5802  C  "C5'" . DA  C 3 2   ? 10.859  12.029  32.238  1 52.17 ? 2   DA  F "C5'" 1 
ATOM   5803  C  "C4'" . DA  C 3 2   ? 9.612   12.534  31.523  1 50.71 ? 2   DA  F "C4'" 1 
ATOM   5804  O  "O4'" . DA  C 3 2   ? 9.902   13.78   30.84   1 50.38 ? 2   DA  F "O4'" 1 
ATOM   5805  C  "C3'" . DA  C 3 2   ? 9.025   11.599  30.468  1 49.63 ? 2   DA  F "C3'" 1 
ATOM   5806  O  "O3'" . DA  C 3 2   ? 7.593   11.693  30.485  1 48.56 ? 2   DA  F "O3'" 1 
ATOM   5807  C  "C2'" . DA  C 3 2   ? 9.61    12.154  29.173  1 49.76 ? 2   DA  F "C2'" 1 
ATOM   5808  C  "C1'" . DA  C 3 2   ? 9.61    13.649  29.465  1 49.98 ? 2   DA  F "C1'" 1 
ATOM   5809  N  N9    . DA  C 3 2   ? 10.613  14.401  28.722  1 49.73 ? 2   DA  F N9    1 
ATOM   5810  C  C8    . DA  C 3 2   ? 11.958  14.159  28.67   1 49.56 ? 2   DA  F C8    1 
ATOM   5811  N  N7    . DA  C 3 2   ? 12.63   15.045  27.975  1 49.38 ? 2   DA  F N7    1 
ATOM   5812  C  C5    . DA  C 3 2   ? 11.656  15.932  27.545  1 49.4  ? 2   DA  F C5    1 
ATOM   5813  C  C6    . DA  C 3 2   ? 11.712  17.096  26.747  1 49.29 ? 2   DA  F C6    1 
ATOM   5814  N  N6    . DA  C 3 2   ? 12.844  17.581  26.229  1 49.26 ? 2   DA  F N6    1 
ATOM   5815  N  N1    . DA  C 3 2   ? 10.551  17.738  26.495  1 49.24 ? 2   DA  F N1    1 
ATOM   5816  C  C2    . DA  C 3 2   ? 9.421   17.259  27.03   1 49.38 ? 2   DA  F C2    1 
ATOM   5817  N  N3    . DA  C 3 2   ? 9.242   16.174  27.783  1 49.52 ? 2   DA  F N3    1 
ATOM   5818  C  C4    . DA  C 3 2   ? 10.41   15.551  28.004  1 49.56 ? 2   DA  F C4    1 
ATOM   5819  P  P     . DG  C 3 3   ? 6.691   10.43   30.074  1 47.75 ? 3   DG  F P     1 
ATOM   5820  O  OP1   . DG  C 3 3   ? 5.451   10.459  30.885  1 47.62 ? 3   DG  F OP1   1 
ATOM   5821  O  OP2   . DG  C 3 3   ? 7.552   9.226   30.109  1 47.88 ? 3   DG  F OP2   1 
ATOM   5822  O  "O5'" . DG  C 3 3   ? 6.328   10.736  28.533  1 46.79 ? 3   DG  F "O5'" 1 
ATOM   5823  C  "C5'" . DG  C 3 3   ? 5.378   11.759  28.206  1 45.59 ? 3   DG  F "C5'" 1 
ATOM   5824  C  "C4'" . DG  C 3 3   ? 5.57    12.281  26.784  1 44.28 ? 3   DG  F "C4'" 1 
ATOM   5825  O  "O4'" . DG  C 3 3   ? 6.815   13.036  26.684  1 44.04 ? 3   DG  F "O4'" 1 
ATOM   5826  C  "C3'" . DG  C 3 3   ? 5.632   11.215  25.666  1 43.08 ? 3   DG  F "C3'" 1 
ATOM   5827  O  "O3'" . DG  C 3 3   ? 4.742   11.578  24.579  1 41.79 ? 3   DG  F "O3'" 1 
ATOM   5828  C  "C2'" . DG  C 3 3   ? 7.089   11.295  25.217  1 43.3  ? 3   DG  F "C2'" 1 
ATOM   5829  C  "C1'" . DG  C 3 3   ? 7.347   12.773  25.421  1 43.56 ? 3   DG  F "C1'" 1 
ATOM   5830  N  N9    . DG  C 3 3   ? 8.754   13.15   25.361  1 43.46 ? 3   DG  F N9    1 
ATOM   5831  C  C8    . DG  C 3 3   ? 9.832   12.349  25.649  1 43.51 ? 3   DG  F C8    1 
ATOM   5832  N  N7    . DG  C 3 3   ? 10.981  12.887  25.342  1 43.43 ? 3   DG  F N7    1 
ATOM   5833  C  C5    . DG  C 3 3   ? 10.641  14.092  24.744  1 43.3  ? 3   DG  F C5    1 
ATOM   5834  C  C6    . DG  C 3 3   ? 11.465  15.107  24.193  1 43.06 ? 3   DG  F C6    1 
ATOM   5835  O  O6    . DG  C 3 3   ? 12.705  15.138  24.118  1 42.81 ? 3   DG  F O6    1 
ATOM   5836  N  N1    . DG  C 3 3   ? 10.707  16.153  23.667  1 43.1  ? 3   DG  F N1    1 
ATOM   5837  C  C2    . DG  C 3 3   ? 9.331   16.21   23.683  1 43.2  ? 3   DG  F C2    1 
ATOM   5838  N  N2    . DG  C 3 3   ? 8.772   17.295  23.144  1 43.17 ? 3   DG  F N2    1 
ATOM   5839  N  N3    . DG  C 3 3   ? 8.554   15.273  24.202  1 43.33 ? 3   DG  F N3    1 
ATOM   5840  C  C4    . DG  C 3 3   ? 9.272   14.25   24.718  1 43.37 ? 3   DG  F C4    1 
ATOM   5841  P  P     . DG  C 3 4   ? 4.111   10.448  23.625  1 40.65 ? 4   DG  F P     1 
ATOM   5842  O  OP1   . DG  C 3 4   ? 3.108   9.705   24.417  1 40.59 ? 4   DG  F OP1   1 
ATOM   5843  O  OP2   . DG  C 3 4   ? 5.222   9.726   22.96   1 40.66 ? 4   DG  F OP2   1 
ATOM   5844  O  "O5'" . DG  C 3 4   ? 3.351   11.282  22.502  1 39.8  ? 4   DG  F "O5'" 1 
ATOM   5845  C  "C5'" . DG  C 3 4   ? 2.428   12.28   22.877  1 39.08 ? 4   DG  F "C5'" 1 
ATOM   5846  C  "C4'" . DG  C 3 4   ? 2.797   13.626  22.275  1 38.28 ? 4   DG  F "C4'" 1 
ATOM   5847  O  "O4'" . DG  C 3 4   ? 4.171   13.974  22.598  1 38.05 ? 4   DG  F "O4'" 1 
ATOM   5848  C  "C3'" . DG  C 3 4   ? 2.677   13.732  20.754  1 37.67 ? 4   DG  F "C3'" 1 
ATOM   5849  O  "O3'" . DG  C 3 4   ? 2.148   15.01   20.43   1 37.24 ? 4   DG  F "O3'" 1 
ATOM   5850  C  "C2'" . DG  C 3 4   ? 4.124   13.602  20.301  1 37.57 ? 4   DG  F "C2'" 1 
ATOM   5851  C  "C1'" . DG  C 3 4   ? 4.834   14.345  21.413  1 37.73 ? 4   DG  F "C1'" 1 
ATOM   5852  N  N9    . DG  C 3 4   ? 6.238   13.993  21.521  1 37.56 ? 4   DG  F N9    1 
ATOM   5853  C  C8    . DG  C 3 4   ? 6.763   12.808  21.968  1 37.39 ? 4   DG  F C8    1 
ATOM   5854  N  N7    . DG  C 3 4   ? 8.058   12.745  21.863  1 37.33 ? 4   DG  F N7    1 
ATOM   5855  C  C5    . DG  C 3 4   ? 8.409   13.961  21.292  1 37.51 ? 4   DG  F C5    1 
ATOM   5856  C  C6    . DG  C 3 4   ? 9.681   14.481  20.964  1 37.79 ? 4   DG  F C6    1 
ATOM   5857  O  O6    . DG  C 3 4   ? 10.781  13.932  21.075  1 37.89 ? 4   DG  F O6    1 
ATOM   5858  N  N1    . DG  C 3 4   ? 9.593   15.759  20.414  1 38.01 ? 4   DG  F N1    1 
ATOM   5859  C  C2    . DG  C 3 4   ? 8.423   16.463  20.245  1 38.08 ? 4   DG  F C2    1 
ATOM   5860  N  N2    . DG  C 3 4   ? 8.531   17.682  19.693  1 38.04 ? 4   DG  F N2    1 
ATOM   5861  N  N3    . DG  C 3 4   ? 7.226   15.985  20.551  1 38.04 ? 4   DG  F N3    1 
ATOM   5862  C  C4    . DG  C 3 4   ? 7.299   14.736  21.077  1 37.68 ? 4   DG  F C4    1 
ATOM   5863  P  P     . DA  C 3 5   ? 1.813   15.408  18.921  1 36.8  ? 5   DA  F P     1 
ATOM   5864  O  OP1   . DA  C 3 5   ? 0.59    16.242  18.932  1 36.69 ? 5   DA  F OP1   1 
ATOM   5865  O  OP2   . DA  C 3 5   ? 1.865   14.188  18.092  1 36.79 ? 5   DA  F OP2   1 
ATOM   5866  O  "O5'" . DA  C 3 5   ? 3.057   16.322  18.52   1 36.99 ? 5   DA  F "O5'" 1 
ATOM   5867  C  "C5'" . DA  C 3 5   ? 3.258   17.574  19.166  1 36.95 ? 5   DA  F "C5'" 1 
ATOM   5868  C  "C4'" . DA  C 3 5   ? 4.266   18.432  18.416  1 36.96 ? 5   DA  F "C4'" 1 
ATOM   5869  O  "O4'" . DA  C 3 5   ? 5.558   17.782  18.407  1 36.66 ? 5   DA  F "O4'" 1 
ATOM   5870  C  "C3'" . DA  C 3 5   ? 3.934   18.732  16.958  1 37.5  ? 5   DA  F "C3'" 1 
ATOM   5871  O  "O3'" . DA  C 3 5   ? 4.39    20.055  16.629  1 38.41 ? 5   DA  F "O3'" 1 
ATOM   5872  C  "C2'" . DA  C 3 5   ? 4.709   17.652  16.197  1 37.07 ? 5   DA  F "C2'" 1 
ATOM   5873  C  "C1'" . DA  C 3 5   ? 5.938   17.455  17.079  1 36.61 ? 5   DA  F "C1'" 1 
ATOM   5874  N  N9    . DA  C 3 5   ? 6.454   16.087  17.088  1 35.99 ? 5   DA  F N9    1 
ATOM   5875  C  C8    . DA  C 3 5   ? 5.748   14.938  17.319  1 35.58 ? 5   DA  F C8    1 
ATOM   5876  N  N7    . DA  C 3 5   ? 6.495   13.859  17.361  1 35.38 ? 5   DA  F N7    1 
ATOM   5877  C  C5    . DA  C 3 5   ? 7.782   14.338  17.172  1 35.47 ? 5   DA  F C5    1 
ATOM   5878  C  C6    . DA  C 3 5   ? 9.037   13.698  17.106  1 35.45 ? 5   DA  F C6    1 
ATOM   5879  N  N6    . DA  C 3 5   ? 9.201   12.385  17.234  1 35.44 ? 5   DA  F N6    1 
ATOM   5880  N  N1    . DA  C 3 5   ? 10.121  14.464  16.884  1 35.6  ? 5   DA  F N1    1 
ATOM   5881  C  C2    . DA  C 3 5   ? 9.96    15.782  16.76   1 35.74 ? 5   DA  F C2    1 
ATOM   5882  N  N3    . DA  C 3 5   ? 8.836   16.497  16.775  1 35.82 ? 5   DA  F N3    1 
ATOM   5883  C  C4    . DA  C 3 5   ? 7.772   15.705  16.987  1 35.78 ? 5   DA  F C4    1 
ATOM   5884  P  P     . DA  C 3 6   ? 4.005   20.736  15.226  1 38.89 ? 6   DA  F P     1 
ATOM   5885  O  OP1   . DA  C 3 6   ? 3.805   22.184  15.463  1 38.82 ? 6   DA  F OP1   1 
ATOM   5886  O  OP2   . DA  C 3 6   ? 2.928   19.93   14.603  1 38.85 ? 6   DA  F OP2   1 
ATOM   5887  O  "O5'" . DA  C 3 6   ? 5.341   20.533  14.37   1 39.46 ? 6   DA  F "O5'" 1 
ATOM   5888  C  "C5'" . DA  C 3 6   ? 6.581   21.032  14.863  1 39.89 ? 6   DA  F "C5'" 1 
ATOM   5889  C  "C4'" . DA  C 3 6   ? 7.75    20.409  14.126  1 40.36 ? 6   DA  F "C4'" 1 
ATOM   5890  O  "O4'" . DA  C 3 6   ? 7.908   19.035  14.548  1 40.37 ? 6   DA  F "O4'" 1 
ATOM   5891  C  "C3'" . DA  C 3 6   ? 7.6     20.353  12.595  1 40.77 ? 6   DA  F "C3'" 1 
ATOM   5892  O  "O3'" . DA  C 3 6   ? 8.409   21.365  11.962  1 41.39 ? 6   DA  F "O3'" 1 
ATOM   5893  C  "C2'" . DA  C 3 6   ? 8.059   18.933  12.217  1 40.5  ? 6   DA  F "C2'" 1 
ATOM   5894  C  "C1'" . DA  C 3 6   ? 8.595   18.36   13.529  1 40.24 ? 6   DA  F "C1'" 1 
ATOM   5895  N  N9    . DA  C 3 6   ? 8.381   16.919  13.65   1 39.73 ? 6   DA  F N9    1 
ATOM   5896  C  C8    . DA  C 3 6   ? 7.179   16.265  13.676  1 39.45 ? 6   DA  F C8    1 
ATOM   5897  N  N7    . DA  C 3 6   ? 7.287   14.955  13.654  1 39.31 ? 6   DA  F N7    1 
ATOM   5898  C  C5    . DA  C 3 6   ? 8.653   14.734  13.561  1 39.29 ? 6   DA  F C5    1 
ATOM   5899  C  C6    . DA  C 3 6   ? 9.431   13.555  13.505  1 38.98 ? 6   DA  F C6    1 
ATOM   5900  N  N6    . DA  C 3 6   ? 8.917   12.324  13.526  1 38.66 ? 6   DA  F N6    1 
ATOM   5901  N  N1    . DA  C 3 6   ? 10.766  13.694  13.415  1 39.1  ? 6   DA  F N1    1 
ATOM   5902  C  C2    . DA  C 3 6   ? 11.285  14.923  13.399  1 39.33 ? 6   DA  F C2    1 
ATOM   5903  N  N3    . DA  C 3 6   ? 10.665  16.1    13.431  1 39.49 ? 6   DA  F N3    1 
ATOM   5904  C  C4    . DA  C 3 6   ? 9.335   15.936  13.496  1 39.54 ? 6   DA  F C4    1 
ATOM   5905  P  P     . DT  C 3 7   ? 8.306   21.623  10.371  1 41.93 ? 7   DT  F P     1 
ATOM   5906  O  OP1   . DT  C 3 7   ? 8.633   23.04   10.112  1 41.81 ? 7   DT  F OP1   1 
ATOM   5907  O  OP2   . DT  C 3 7   ? 7.02    21.071  9.891   1 42.07 ? 7   DT  F OP2   1 
ATOM   5908  O  "O5'" . DT  C 3 7   ? 9.487   20.708  9.793   1 42.5  ? 7   DT  F "O5'" 1 
ATOM   5909  C  "C5'" . DT  C 3 7   ? 10.837  21.027  10.109  1 43.13 ? 7   DT  F "C5'" 1 
ATOM   5910  C  "C4'" . DT  C 3 7   ? 11.771  19.844  9.886   1 43.77 ? 7   DT  F "C4'" 1 
ATOM   5911  O  "O4'" . DT  C 3 7   ? 11.336  18.706  10.653  1 43.75 ? 7   DT  F "O4'" 1 
ATOM   5912  C  "C3'" . DT  C 3 7   ? 11.838  19.293  8.48    1 44.48 ? 7   DT  F "C3'" 1 
ATOM   5913  O  "O3'" . DT  C 3 7   ? 12.668  20.104  7.652   1 45.59 ? 7   DT  F "O3'" 1 
ATOM   5914  C  "C2'" . DT  C 3 7   ? 12.477  17.926  8.733   1 44.12 ? 7   DT  F "C2'" 1 
ATOM   5915  C  "C1'" . DT  C 3 7   ? 11.999  17.567  10.147  1 43.68 ? 7   DT  F "C1'" 1 
ATOM   5916  N  N1    . DT  C 3 7   ? 11.077  16.419  10.154  1 43.32 ? 7   DT  F N1    1 
ATOM   5917  C  C2    . DT  C 3 7   ? 11.598  15.15   10.09   1 43.18 ? 7   DT  F C2    1 
ATOM   5918  O  O2    . DT  C 3 7   ? 12.785  14.913  10.212  1 43.14 ? 7   DT  F O2    1 
ATOM   5919  N  N3    . DT  C 3 7   ? 10.664  14.153  10.034  1 43.11 ? 7   DT  F N3    1 
ATOM   5920  C  C4    . DT  C 3 7   ? 9.299   14.302  9.935   1 43.09 ? 7   DT  F C4    1 
ATOM   5921  O  O4    . DT  C 3 7   ? 8.583   13.313  9.864   1 42.91 ? 7   DT  F O4    1 
ATOM   5922  C  C5    . DT  C 3 7   ? 8.829   15.659  9.932   1 43.26 ? 7   DT  F C5    1 
ATOM   5923  C  C7    . DT  C 3 7   ? 7.367   15.938  9.856   1 43.36 ? 7   DT  F C7    1 
ATOM   5924  C  C6    . DT  C 3 7   ? 9.732   16.642  10.009  1 43.25 ? 7   DT  F C6    1 
ATOM   5925  P  P     . DG  C 3 8   ? 12.541  20.001  6.054   1 46.72 ? 8   DG  F P     1 
ATOM   5926  O  OP1   . DG  C 3 8   ? 13.076  21.254  5.471   1 46.93 ? 8   DG  F OP1   1 
ATOM   5927  O  OP2   . DG  C 3 8   ? 11.161  19.576  5.735   1 46.87 ? 8   DG  F OP2   1 
ATOM   5928  O  "O5'" . DG  C 3 8   ? 13.525  18.79   5.681   1 47.06 ? 8   DG  F "O5'" 1 
ATOM   5929  C  "C5'" . DG  C 3 8   ? 14.86   18.764  6.187   1 47.59 ? 8   DG  F "C5'" 1 
ATOM   5930  C  "C4'" . DG  C 3 8   ? 15.482  17.391  6.01    1 48.31 ? 8   DG  F "C4'" 1 
ATOM   5931  O  "O4'" . DG  C 3 8   ? 14.648  16.38   6.646   1 48.37 ? 8   DG  F "O4'" 1 
ATOM   5932  C  "C3'" . DG  C 3 8   ? 15.657  16.951  4.555   1 49.08 ? 8   DG  F "C3'" 1 
ATOM   5933  O  "O3'" . DG  C 3 8   ? 16.993  16.512  4.329   1 50.09 ? 8   DG  F "O3'" 1 
ATOM   5934  C  "C2'" . DG  C 3 8   ? 14.653  15.812  4.392   1 48.72 ? 8   DG  F "C2'" 1 
ATOM   5935  C  "C1'" . DG  C 3 8   ? 14.56   15.26   5.803   1 48.38 ? 8   DG  F "C1'" 1 
ATOM   5936  N  N9    . DG  C 3 8   ? 13.299  14.567  6.052   1 48.01 ? 8   DG  F N9    1 
ATOM   5937  C  C8    . DG  C 3 8   ? 12.036  15.102  5.967   1 47.86 ? 8   DG  F C8    1 
ATOM   5938  N  N7    . DG  C 3 8   ? 11.085  14.225  6.118   1 47.79 ? 8   DG  F N7    1 
ATOM   5939  C  C5    . DG  C 3 8   ? 11.755  13.018  6.263   1 47.77 ? 8   DG  F C5    1 
ATOM   5940  C  C6    . DG  C 3 8   ? 11.245  11.712  6.471   1 47.45 ? 8   DG  F C6    1 
ATOM   5941  O  O6    . DG  C 3 8   ? 10.061  11.361  6.565   1 47.22 ? 8   DG  F O6    1 
ATOM   5942  N  N1    . DG  C 3 8   ? 12.266  10.767  6.58    1 47.36 ? 8   DG  F N1    1 
ATOM   5943  C  C2    . DG  C 3 8   ? 13.612  11.054  6.497   1 47.42 ? 8   DG  F C2    1 
ATOM   5944  N  N2    . DG  C 3 8   ? 14.45   10.017  6.624   1 47.24 ? 8   DG  F N2    1 
ATOM   5945  N  N3    . DG  C 3 8   ? 14.103  12.276  6.304   1 47.73 ? 8   DG  F N3    1 
ATOM   5946  C  C4    . DG  C 3 8   ? 13.12   13.208  6.209   1 47.88 ? 8   DG  F C4    1 
ATOM   5947  P  P     . DC  C 3 9   ? 17.509  16.227  2.838   1 51.01 ? 9   DC  F P     1 
ATOM   5948  O  OP1   . DC  C 3 9   ? 18.916  16.678  2.742   1 51    ? 9   DC  F OP1   1 
ATOM   5949  O  OP2   . DC  C 3 9   ? 16.5    16.755  1.89    1 50.86 ? 9   DC  F OP2   1 
ATOM   5950  O  "O5'" . DC  C 3 9   ? 17.473  14.634  2.762   1 52.19 ? 9   DC  F "O5'" 1 
ATOM   5951  C  "C5'" . DC  C 3 9   ? 18.395  13.863  3.527   1 53.33 ? 9   DC  F "C5'" 1 
ATOM   5952  C  "C4'" . DC  C 3 9   ? 18.246  12.388  3.217   1 54.44 ? 9   DC  F "C4'" 1 
ATOM   5953  O  "O4'" . DC  C 3 9   ? 16.943  11.94   3.66    1 54.63 ? 9   DC  F "O4'" 1 
ATOM   5954  C  "C3'" . DC  C 3 9   ? 18.346  12.028  1.735   1 55.43 ? 9   DC  F "C3'" 1 
ATOM   5955  O  "O3'" . DC  C 3 9   ? 19.167  10.881  1.562   1 56.8  ? 9   DC  F "O3'" 1 
ATOM   5956  C  "C2'" . DC  C 3 9   ? 16.901  11.749  1.33    1 55.11 ? 9   DC  F "C2'" 1 
ATOM   5957  C  "C1'" . DC  C 3 9   ? 16.299  11.239  2.624   1 54.84 ? 9   DC  F "C1'" 1 
ATOM   5958  N  N1    . DC  C 3 9   ? 14.841  11.495  2.726   1 54.81 ? 9   DC  F N1    1 
ATOM   5959  C  C2    . DC  C 3 9   ? 13.968  10.422  2.82    1 54.71 ? 9   DC  F C2    1 
ATOM   5960  O  O2    . DC  C 3 9   ? 14.435  9.283   2.871   1 54.63 ? 9   DC  F O2    1 
ATOM   5961  N  N3    . DC  C 3 9   ? 12.634  10.662  2.899   1 54.76 ? 9   DC  F N3    1 
ATOM   5962  C  C4    . DC  C 3 9   ? 12.178  11.915  2.858   1 54.79 ? 9   DC  F C4    1 
ATOM   5963  N  N4    . DC  C 3 9   ? 10.857  12.106  2.931   1 54.79 ? 9   DC  F N4    1 
ATOM   5964  C  C5    . DC  C 3 9   ? 13.057  13.025  2.728   1 54.82 ? 9   DC  F C5    1 
ATOM   5965  C  C6    . DC  C 3 9   ? 14.369  12.771  2.665   1 54.85 ? 9   DC  F C6    1 
ATOM   5966  P  P     . DA  C 3 10  ? 19.959  10.654  0.189   1 58.19 ? 10  DA  F P     1 
ATOM   5967  O  OP1   . DA  C 3 10  ? 21.397  10.911  0.449   1 58.36 ? 10  DA  F OP1   1 
ATOM   5968  O  OP2   . DA  C 3 10  ? 19.254  11.399  -0.887  1 58.33 ? 10  DA  F OP2   1 
ATOM   5969  O  "O5'" . DA  C 3 10  ? 19.752  9.091   -0.085  1 58.84 ? 10  DA  F "O5'" 1 
ATOM   5970  C  "C5'" . DA  C 3 10  ? 18.622  8.429   0.449   1 59.55 ? 10  DA  F "C5'" 1 
ATOM   5971  C  "C4'" . DA  C 3 10  ? 18.204  7.252   -0.417  1 60.36 ? 10  DA  F "C4'" 1 
ATOM   5972  O  "O4'" . DA  C 3 10  ? 16.76   7.167   -0.422  1 60.29 ? 10  DA  F "O4'" 1 
ATOM   5973  C  "C3'" . DA  C 3 10  ? 18.579  7.351   -1.886  1 61.36 ? 10  DA  F "C3'" 1 
ATOM   5974  O  "O3'" . DA  C 3 10  ? 18.572  6.055   -2.466  1 62.9  ? 10  DA  F "O3'" 1 
ATOM   5975  C  "C2'" . DA  C 3 10  ? 17.446  8.208   -2.432  1 60.82 ? 10  DA  F "C2'" 1 
ATOM   5976  C  "C1'" . DA  C 3 10  ? 16.256  7.662   -1.653  1 60.3  ? 10  DA  F "C1'" 1 
ATOM   5977  N  N9    . DA  C 3 10  ? 15.244  8.667   -1.36   1 59.93 ? 10  DA  F N9    1 
ATOM   5978  C  C8    . DA  C 3 10  ? 15.42   10.02   -1.306  1 59.81 ? 10  DA  F C8    1 
ATOM   5979  N  N7    . DA  C 3 10  ? 14.335  10.679  -0.974  1 59.79 ? 10  DA  F N7    1 
ATOM   5980  C  C5    . DA  C 3 10  ? 13.381  9.687   -0.806  1 59.77 ? 10  DA  F C5    1 
ATOM   5981  C  C6    . DA  C 3 10  ? 12.016  9.727   -0.452  1 59.67 ? 10  DA  F C6    1 
ATOM   5982  N  N6    . DA  C 3 10  ? 11.354  10.862  -0.199  1 59.57 ? 10  DA  F N6    1 
ATOM   5983  N  N1    . DA  C 3 10  ? 11.357  8.548   -0.367  1 59.65 ? 10  DA  F N1    1 
ATOM   5984  C  C2    . DA  C 3 10  ? 12.022  7.416   -0.633  1 59.63 ? 10  DA  F C2    1 
ATOM   5985  N  N3    . DA  C 3 10  ? 13.305  7.253   -0.947  1 59.71 ? 10  DA  F N3    1 
ATOM   5986  C  C4    . DA  C 3 10  ? 13.931  8.44    -1.029  1 59.81 ? 10  DA  F C4    1 
ATOM   5987  P  P     . DG  C 3 11  ? 19.577  5.7     -3.658  1 64.4  ? 11  DG  F P     1 
ATOM   5988  O  OP1   . DG  C 3 11  ? 20.667  4.863   -3.099  1 64.45 ? 11  DG  F OP1   1 
ATOM   5989  O  OP2   . DG  C 3 11  ? 19.897  6.956   -4.375  1 64.28 ? 11  DG  F OP2   1 
ATOM   5990  O  "O5'" . DG  C 3 11  ? 18.675  4.794   -4.623  1 65.73 ? 11  DG  F "O5'" 1 
ATOM   5991  C  "C5'" . DG  C 3 11  ? 18.246  3.504   -4.192  1 66.96 ? 11  DG  F "C5'" 1 
ATOM   5992  C  "C4'" . DG  C 3 11  ? 16.971  3.078   -4.904  1 68.16 ? 11  DG  F "C4'" 1 
ATOM   5993  O  "O4'" . DG  C 3 11  ? 15.901  4.007   -4.602  1 68.38 ? 11  DG  F "O4'" 1 
ATOM   5994  C  "C3'" . DG  C 3 11  ? 17.05   3.003   -6.423  1 69.11 ? 11  DG  F "C3'" 1 
ATOM   5995  O  "O3'" . DG  C 3 11  ? 16.272  1.899   -6.876  1 70.33 ? 11  DG  F "O3'" 1 
ATOM   5996  C  "C2'" . DG  C 3 11  ? 16.456  4.341   -6.869  1 68.78 ? 11  DG  F "C2'" 1 
ATOM   5997  C  "C1'" . DG  C 3 11  ? 15.421  4.612   -5.787  1 68.53 ? 11  DG  F "C1'" 1 
ATOM   5998  N  N9    . DG  C 3 11  ? 15.222  6.032   -5.515  1 68.52 ? 11  DG  F N9    1 
ATOM   5999  C  C8    . DG  C 3 11  ? 16.159  7.031   -5.6    1 68.46 ? 11  DG  F C8    1 
ATOM   6000  N  N7    . DG  C 3 11  ? 15.707  8.199   -5.242  1 68.47 ? 11  DG  F N7    1 
ATOM   6001  C  C5    . DG  C 3 11  ? 14.39   7.957   -4.879  1 68.58 ? 11  DG  F C5    1 
ATOM   6002  C  C6    . DG  C 3 11  ? 13.392  8.847   -4.41   1 68.74 ? 11  DG  F C6    1 
ATOM   6003  O  O6    . DG  C 3 11  ? 13.484  10.066  -4.207  1 68.84 ? 11  DG  F O6    1 
ATOM   6004  N  N1    . DG  C 3 11  ? 12.194  8.182   -4.148  1 68.73 ? 11  DG  F N1    1 
ATOM   6005  C  C2    . DG  C 3 11  ? 11.992  6.83    -4.324  1 68.73 ? 11  DG  F C2    1 
ATOM   6006  N  N2    . DG  C 3 11  ? 10.778  6.36    -4.017  1 68.73 ? 11  DG  F N2    1 
ATOM   6007  N  N3    . DG  C 3 11  ? 12.913  5.996   -4.775  1 68.69 ? 11  DG  F N3    1 
ATOM   6008  C  C4    . DG  C 3 11  ? 14.082  6.625   -5.031  1 68.61 ? 11  DG  F C4    1 
ATOM   6009  P  P     . DA  C 3 12  ? 16.473  1.289   -8.349  1 71.49 ? 12  DA  F P     1 
ATOM   6010  O  OP1   . DA  C 3 12  ? 17.01   -0.086  -8.211  1 71.61 ? 12  DA  F OP1   1 
ATOM   6011  O  OP2   . DA  C 3 12  ? 17.193  2.283   -9.181  1 71.53 ? 12  DA  F OP2   1 
ATOM   6012  O  "O5'" . DA  C 3 12  ? 14.966  1.201   -8.872  1 72.01 ? 12  DA  F "O5'" 1 
ATOM   6013  C  "C5'" . DA  C 3 12  ? 13.906  0.982   -7.929  1 72.31 ? 12  DA  F "C5'" 1 
ATOM   6014  C  "C4'" . DA  C 3 12  ? 12.605  1.603   -8.405  1 72.54 ? 12  DA  F "C4'" 1 
ATOM   6015  O  "O4'" . DA  C 3 12  ? 12.506  2.96    -7.907  1 72.56 ? 12  DA  F "O4'" 1 
ATOM   6016  C  "C3'" . DA  C 3 12  ? 12.446  1.687   -9.925  1 72.77 ? 12  DA  F "C3'" 1 
ATOM   6017  O  "O3'" . DA  C 3 12  ? 11.177  1.193   -10.318 1 73.12 ? 12  DA  F "O3'" 1 
ATOM   6018  C  "C2'" . DA  C 3 12  ? 12.597  3.175   -10.224 1 72.69 ? 12  DA  F "C2'" 1 
ATOM   6019  C  "C1'" . DA  C 3 12  ? 12.077  3.803   -8.946  1 72.66 ? 12  DA  F "C1'" 1 
ATOM   6020  N  N9    . DA  C 3 12  ? 12.602  5.143   -8.708  1 72.74 ? 12  DA  F N9    1 
ATOM   6021  C  C8    . DA  C 3 12  ? 13.865  5.59    -8.972  1 72.75 ? 12  DA  F C8    1 
ATOM   6022  N  N7    . DA  C 3 12  ? 14.048  6.856   -8.685  1 72.76 ? 12  DA  F N7    1 
ATOM   6023  C  C5    . DA  C 3 12  ? 12.811  7.276   -8.229  1 72.74 ? 12  DA  F C5    1 
ATOM   6024  C  C6    . DA  C 3 12  ? 12.345  8.519   -7.762  1 72.71 ? 12  DA  F C6    1 
ATOM   6025  N  N6    . DA  C 3 12  ? 13.113  9.607   -7.675  1 72.69 ? 12  DA  F N6    1 
ATOM   6026  N  N1    . DA  C 3 12  ? 11.055  8.601   -7.383  1 72.75 ? 12  DA  F N1    1 
ATOM   6027  C  C2    . DA  C 3 12  ? 10.298  7.499   -7.433  1 72.79 ? 12  DA  F C2    1 
ATOM   6028  N  N3    . DA  C 3 12  ? 10.617  6.282   -7.873  1 72.78 ? 12  DA  F N3    1 
ATOM   6029  C  C4    . DA  C 3 12  ? 11.904  6.236   -8.25   1 72.75 ? 12  DA  F C4    1 
ATOM   6030  P  P     . DC  C 3 13  ? 10.961  0.652   -11.814 1 73.4  ? 13  DC  F P     1 
ATOM   6031  O  OP1   . DC  C 3 13  ? 9.929   -0.416  -11.768 1 73.58 ? 13  DC  F OP1   1 
ATOM   6032  O  OP2   . DC  C 3 13  ? 12.298  0.357   -12.386 1 73.32 ? 13  DC  F OP2   1 
ATOM   6033  O  "O5'" . DC  C 3 13  ? 10.374  1.948   -12.575 1 73.3  ? 13  DC  F "O5'" 1 
ATOM   6034  C  "C5'" . DC  C 3 13  ? 8.935   2.181   -12.693 1 73.03 ? 13  DC  F "C5'" 1 
ATOM   6035  C  "C4'" . DC  C 3 13  ? 8.309   2.723   -11.399 1 72.64 ? 13  DC  F "C4'" 1 
ATOM   6036  O  "O4'" . DC  C 3 13  ? 9.165   3.73    -10.793 1 72.48 ? 13  DC  F "O4'" 1 
ATOM   6037  C  "C3'" . DC  C 3 13  ? 6.959   3.407   -11.579 1 72.39 ? 13  DC  F "C3'" 1 
ATOM   6038  O  "O3'" . DC  C 3 13  ? 6.174   3.258   -10.397 1 72.22 ? 13  DC  F "O3'" 1 
ATOM   6039  C  "C2'" . DC  C 3 13  ? 7.363   4.862   -11.812 1 72.32 ? 13  DC  F "C2'" 1 
ATOM   6040  C  "C1'" . DC  C 3 13  ? 8.55    5.004   -10.862 1 72.27 ? 13  DC  F "C1'" 1 
ATOM   6041  N  N1    . DC  C 3 13  ? 9.587   6.005   -11.304 1 71.87 ? 13  DC  F N1    1 
ATOM   6042  C  C2    . DC  C 3 13  ? 9.507   7.331   -10.87  1 71.72 ? 13  DC  F C2    1 
ATOM   6043  O  O2    . DC  C 3 13  ? 8.544   7.682   -10.176 1 71.79 ? 13  DC  F O2    1 
ATOM   6044  N  N3    . DC  C 3 13  ? 10.473  8.206   -11.251 1 71.52 ? 13  DC  F N3    1 
ATOM   6045  C  C4    . DC  C 3 13  ? 11.494  7.791   -11.998 1 71.41 ? 13  DC  F C4    1 
ATOM   6046  N  N4    . DC  C 3 13  ? 12.416  8.688   -12.354 1 71.39 ? 13  DC  F N4    1 
ATOM   6047  C  C5    . DC  C 3 13  ? 11.605  6.443   -12.429 1 71.5  ? 13  DC  F C5    1 
ATOM   6048  C  C6    . DC  C 3 13  ? 10.642  5.593   -12.059 1 71.67 ? 13  DC  F C6    1 
ATOM   6049  O  "O5'" . DG  D 3 1   ? 18.417  -56.838 19.901  1 48.06 ? 1   DG  U "O5'" 1 
ATOM   6050  C  "C5'" . DG  D 3 1   ? 17.716  -57.871 20.599  1 47.92 ? 1   DG  U "C5'" 1 
ATOM   6051  C  "C4'" . DG  D 3 1   ? 16.215  -57.661 20.493  1 47.69 ? 1   DG  U "C4'" 1 
ATOM   6052  O  "O4'" . DG  D 3 1   ? 15.513  -58.897 20.801  1 47.32 ? 1   DG  U "O4'" 1 
ATOM   6053  C  "C3'" . DG  D 3 1   ? 15.633  -56.612 21.443  1 47.65 ? 1   DG  U "C3'" 1 
ATOM   6054  O  "O3'" . DG  D 3 1   ? 14.569  -55.941 20.789  1 47.91 ? 1   DG  U "O3'" 1 
ATOM   6055  C  "C2'" . DG  D 3 1   ? 15.109  -57.474 22.583  1 47.29 ? 1   DG  U "C2'" 1 
ATOM   6056  C  "C1'" . DG  D 3 1   ? 14.541  -58.628 21.783  1 46.97 ? 1   DG  U "C1'" 1 
ATOM   6057  N  N9    . DG  D 3 1   ? 14.305  -59.834 22.558  1 46.38 ? 1   DG  U N9    1 
ATOM   6058  C  C8    . DG  D 3 1   ? 15.196  -60.492 23.368  1 46.26 ? 1   DG  U C8    1 
ATOM   6059  N  N7    . DG  D 3 1   ? 14.694  -61.557 23.93   1 46.24 ? 1   DG  U N7    1 
ATOM   6060  C  C5    . DG  D 3 1   ? 13.392  -61.612 23.448  1 46.16 ? 1   DG  U C5    1 
ATOM   6061  C  C6    . DG  D 3 1   ? 12.359  -62.547 23.706  1 46.1  ? 1   DG  U C6    1 
ATOM   6062  O  O6    . DG  D 3 1   ? 12.394  -63.556 24.431  1 45.93 ? 1   DG  U O6    1 
ATOM   6063  N  N1    . DG  D 3 1   ? 11.195  -62.23  23.005  1 46.13 ? 1   DG  U N1    1 
ATOM   6064  C  C2    . DG  D 3 1   ? 11.046  -61.136 22.177  1 46.03 ? 1   DG  U C2    1 
ATOM   6065  N  N2    . DG  D 3 1   ? 9.847   -60.985 21.595  1 46.01 ? 1   DG  U N2    1 
ATOM   6066  N  N3    . DG  D 3 1   ? 12.004  -60.256 21.935  1 45.96 ? 1   DG  U N3    1 
ATOM   6067  C  C4    . DG  D 3 1   ? 13.141  -60.553 22.605  1 46.1  ? 1   DG  U C4    1 
ATOM   6068  P  P     . DA  D 3 2   ? 14.144  -54.471 21.236  1 48.1  ? 2   DA  U P     1 
ATOM   6069  O  OP1   . DA  D 3 2   ? 14.317  -53.579 20.064  1 48.08 ? 2   DA  U OP1   1 
ATOM   6070  O  OP2   . DA  D 3 2   ? 14.832  -54.159 22.511  1 48.43 ? 2   DA  U OP2   1 
ATOM   6071  O  "O5'" . DA  D 3 2   ? 12.575  -54.639 21.558  1 47.32 ? 2   DA  U "O5'" 1 
ATOM   6072  C  "C5'" . DA  D 3 2   ? 11.623  -54.727 20.485  1 46.13 ? 2   DA  U "C5'" 1 
ATOM   6073  C  "C4'" . DA  D 3 2   ? 10.257  -55.198 20.974  1 44.71 ? 2   DA  U "C4'" 1 
ATOM   6074  O  "O4'" . DA  D 3 2   ? 10.392  -56.444 21.697  1 44.01 ? 2   DA  U "O4'" 1 
ATOM   6075  C  "C3'" . DA  D 3 2   ? 9.515   -54.243 21.908  1 43.88 ? 2   DA  U "C3'" 1 
ATOM   6076  O  "O3'" . DA  D 3 2   ? 8.108   -54.296 21.631  1 43.37 ? 2   DA  U "O3'" 1 
ATOM   6077  C  "C2'" . DA  D 3 2   ? 9.839   -54.814 23.286  1 43.58 ? 2   DA  U "C2'" 1 
ATOM   6078  C  "C1'" . DA  D 3 2   ? 9.86    -56.305 22.994  1 43.29 ? 2   DA  U "C1'" 1 
ATOM   6079  N  N9    . DA  D 3 2   ? 10.693  -57.075 23.904  1 42.42 ? 2   DA  U N9    1 
ATOM   6080  C  C8    . DA  D 3 2   ? 12.009  -56.857 24.202  1 42.1  ? 2   DA  U C8    1 
ATOM   6081  N  N7    . DA  D 3 2   ? 12.522  -57.757 25.008  1 41.97 ? 2   DA  U N7    1 
ATOM   6082  C  C5    . DA  D 3 2   ? 11.467  -58.626 25.251  1 41.94 ? 2   DA  U C5    1 
ATOM   6083  C  C6    . DA  D 3 2   ? 11.354  -59.788 26.041  1 41.83 ? 2   DA  U C6    1 
ATOM   6084  N  N6    . DA  D 3 2   ? 12.363  -60.293 26.757  1 41.73 ? 2   DA  U N6    1 
ATOM   6085  N  N1    . DA  D 3 2   ? 10.154  -60.409 26.072  1 41.83 ? 2   DA  U N1    1 
ATOM   6086  C  C2    . DA  D 3 2   ? 9.151   -59.911 25.339  1 41.84 ? 2   DA  U C2    1 
ATOM   6087  N  N3    . DA  D 3 2   ? 9.136   -58.826 24.569  1 41.9  ? 2   DA  U N3    1 
ATOM   6088  C  C4    . DA  D 3 2   ? 10.337  -58.224 24.57   1 42.05 ? 2   DA  U C4    1 
ATOM   6089  P  P     . DG  D 3 3   ? 7.177   -53.013 21.887  1 42.9  ? 3   DG  U P     1 
ATOM   6090  O  OP1   . DG  D 3 3   ? 6.118   -53.005 20.849  1 43.07 ? 3   DG  U OP1   1 
ATOM   6091  O  OP2   . DG  D 3 3   ? 8.061   -51.833 22.046  1 42.95 ? 3   DG  U OP2   1 
ATOM   6092  O  "O5'" . DG  D 3 3   ? 6.511   -53.335 23.317  1 41.96 ? 3   DG  U "O5'" 1 
ATOM   6093  C  "C5'" . DG  D 3 3   ? 5.502   -54.352 23.44   1 40.85 ? 3   DG  U "C5'" 1 
ATOM   6094  C  "C4'" . DG  D 3 3   ? 5.408   -54.886 24.867  1 39.85 ? 3   DG  U "C4'" 1 
ATOM   6095  O  "O4'" . DG  D 3 3   ? 6.6     -55.656 25.196  1 39.52 ? 3   DG  U "O4'" 1 
ATOM   6096  C  "C3'" . DG  D 3 3   ? 5.27    -53.824 25.987  1 39.29 ? 3   DG  U "C3'" 1 
ATOM   6097  O  "O3'" . DG  D 3 3   ? 4.187   -54.173 26.886  1 38.59 ? 3   DG  U "O3'" 1 
ATOM   6098  C  "C2'" . DG  D 3 3   ? 6.616   -53.923 26.703  1 39.38 ? 3   DG  U "C2'" 1 
ATOM   6099  C  "C1'" . DG  D 3 3   ? 6.891   -55.403 26.542  1 39.42 ? 3   DG  U "C1'" 1 
ATOM   6100  N  N9    . DG  D 3 3   ? 8.256   -55.798 26.867  1 39.29 ? 3   DG  U N9    1 
ATOM   6101  C  C8    . DG  D 3 3   ? 9.379   -55.012 26.788  1 39.32 ? 3   DG  U C8    1 
ATOM   6102  N  N7    . DG  D 3 3   ? 10.442  -55.569 27.301  1 39.36 ? 3   DG  U N7    1 
ATOM   6103  C  C5    . DG  D 3 3   ? 9.979   -56.77  27.822  1 39.27 ? 3   DG  U C5    1 
ATOM   6104  C  C6    . DG  D 3 3   ? 10.673  -57.799 28.513  1 39.24 ? 3   DG  U C6    1 
ATOM   6105  O  O6    . DG  D 3 3   ? 11.876  -57.849 28.815  1 39.11 ? 3   DG  U O6    1 
ATOM   6106  N  N1    . DG  D 3 3   ? 9.818   -58.831 28.893  1 39.35 ? 3   DG  U N1    1 
ATOM   6107  C  C2    . DG  D 3 3   ? 8.47    -58.87  28.626  1 39.41 ? 3   DG  U C2    1 
ATOM   6108  N  N2    . DG  D 3 3   ? 7.81    -59.948 29.061  1 39.31 ? 3   DG  U N2    1 
ATOM   6109  N  N3    . DG  D 3 3   ? 7.813   -57.921 27.966  1 39.42 ? 3   DG  U N3    1 
ATOM   6110  C  C4    . DG  D 3 3   ? 8.629   -56.908 27.593  1 39.29 ? 3   DG  U C4    1 
ATOM   6111  P  P     . DG  D 3 4   ? 3.41    -53.036 27.713  1 38.17 ? 4   DG  U P     1 
ATOM   6112  O  OP1   . DG  D 3 4   ? 2.589   -52.271 26.76   1 38.52 ? 4   DG  U OP1   1 
ATOM   6113  O  OP2   . DG  D 3 4   ? 4.387   -52.333 28.576  1 38.18 ? 4   DG  U OP2   1 
ATOM   6114  O  "O5'" . DG  D 3 4   ? 2.435   -53.862 28.662  1 37.61 ? 4   DG  U "O5'" 1 
ATOM   6115  C  "C5'" . DG  D 3 4   ? 1.589   -54.858 28.115  1 37.02 ? 4   DG  U "C5'" 1 
ATOM   6116  C  "C4'" . DG  D 3 4   ? 1.817   -56.202 28.785  1 36.4  ? 4   DG  U "C4'" 1 
ATOM   6117  O  "O4'" . DG  D 3 4   ? 3.222   -56.568 28.727  1 36.03 ? 4   DG  U "O4'" 1 
ATOM   6118  C  "C3'" . DG  D 3 4   ? 1.417   -56.291 30.258  1 36.22 ? 4   DG  U "C3'" 1 
ATOM   6119  O  "O3'" . DG  D 3 4   ? 0.817   -57.554 30.493  1 36.74 ? 4   DG  U "O3'" 1 
ATOM   6120  C  "C2'" . DG  D 3 4   ? 2.756   -56.178 30.969  1 35.82 ? 4   DG  U "C2'" 1 
ATOM   6121  C  "C1'" . DG  D 3 4   ? 3.649   -56.942 30.013  1 35.69 ? 4   DG  U "C1'" 1 
ATOM   6122  N  N9    . DG  D 3 4   ? 5.054   -56.61  30.163  1 35.35 ? 4   DG  U N9    1 
ATOM   6123  C  C8    . DG  D 3 4   ? 5.668   -55.436 29.818  1 35.16 ? 4   DG  U C8    1 
ATOM   6124  N  N7    . DG  D 3 4   ? 6.921   -55.385 30.166  1 35.08 ? 4   DG  U N7    1 
ATOM   6125  C  C5    . DG  D 3 4   ? 7.146   -56.594 30.798  1 35.19 ? 4   DG  U C5    1 
ATOM   6126  C  C6    . DG  D 3 4   ? 8.33    -57.124 31.36   1 35.34 ? 4   DG  U C6    1 
ATOM   6127  O  O6    . DG  D 3 4   ? 9.442   -56.591 31.454  1 35.27 ? 4   DG  U O6    1 
ATOM   6128  N  N1    . DG  D 3 4   ? 8.123   -58.393 31.891  1 35.67 ? 4   DG  U N1    1 
ATOM   6129  C  C2    . DG  D 3 4   ? 6.933   -59.081 31.847  1 35.68 ? 4   DG  U C2    1 
ATOM   6130  N  N2    . DG  D 3 4   ? 6.922   -60.294 32.419  1 35.57 ? 4   DG  U N2    1 
ATOM   6131  N  N3    . DG  D 3 4   ? 5.819   -58.595 31.321  1 35.62 ? 4   DG  U N3    1 
ATOM   6132  C  C4    . DG  D 3 4   ? 6.004   -57.358 30.805  1 35.37 ? 4   DG  U C4    1 
ATOM   6133  P  P     . DA  D 3 5   ? 0.208   -57.931 31.927  1 37.27 ? 5   DA  U P     1 
ATOM   6134  O  OP1   . DA  D 3 5   ? -1.004  -58.748 31.697  1 37.39 ? 5   DA  U OP1   1 
ATOM   6135  O  OP2   . DA  D 3 5   ? 0.124   -56.703 32.745  1 37.25 ? 5   DA  U OP2   1 
ATOM   6136  O  "O5'" . DA  D 3 5   ? 1.344   -58.859 32.558  1 37.49 ? 5   DA  U "O5'" 1 
ATOM   6137  C  "C5'" . DA  D 3 5   ? 1.64    -60.121 31.969  1 37.6  ? 5   DA  U "C5'" 1 
ATOM   6138  C  "C4'" . DA  D 3 5   ? 2.483   -60.984 32.897  1 37.79 ? 5   DA  U "C4'" 1 
ATOM   6139  O  "O4'" . DA  D 3 5   ? 3.759   -60.347 33.137  1 37.68 ? 5   DA  U "O4'" 1 
ATOM   6140  C  "C3'" . DA  D 3 5   ? 1.887   -61.263 34.274  1 38.19 ? 5   DA  U "C3'" 1 
ATOM   6141  O  "O3'" . DA  D 3 5   ? 2.252   -62.586 34.697  1 38.77 ? 5   DA  U "O3'" 1 
ATOM   6142  C  "C2'" . DA  D 3 5   ? 2.528   -60.185 35.153  1 37.91 ? 5   DA  U "C2'" 1 
ATOM   6143  C  "C1'" . DA  D 3 5   ? 3.896   -60.012 34.509  1 37.66 ? 5   DA  U "C1'" 1 
ATOM   6144  N  N9    . DA  D 3 5   ? 4.418   -58.652 34.586  1 37.51 ? 5   DA  U N9    1 
ATOM   6145  C  C8    . DA  D 3 5   ? 3.78    -57.496 34.217  1 37.32 ? 5   DA  U C8    1 
ATOM   6146  N  N7    . DA  D 3 5   ? 4.535   -56.424 34.301  1 37.27 ? 5   DA  U N7    1 
ATOM   6147  C  C5    . DA  D 3 5   ? 5.76    -56.913 34.731  1 37.38 ? 5   DA  U C5    1 
ATOM   6148  C  C6    . DA  D 3 5   ? 6.991   -56.285 35.023  1 37.26 ? 5   DA  U C6    1 
ATOM   6149  N  N6    . DA  D 3 5   ? 7.19    -54.978 34.916  1 37.07 ? 5   DA  U N6    1 
ATOM   6150  N  N1    . DA  D 3 5   ? 8.007   -57.059 35.45   1 37.43 ? 5   DA  U N1    1 
ATOM   6151  C  C2    . DA  D 3 5   ? 7.813   -58.379 35.548  1 37.57 ? 5   DA  U C2    1 
ATOM   6152  N  N3    . DA  D 3 5   ? 6.7     -59.083 35.334  1 37.6  ? 5   DA  U N3    1 
ATOM   6153  C  C4    . DA  D 3 5   ? 5.7     -58.282 34.924  1 37.54 ? 5   DA  U C4    1 
ATOM   6154  P  P     . DA  D 3 6   ? 1.616   -63.233 36.022  1 39.11 ? 6   DA  U P     1 
ATOM   6155  O  OP1   . DA  D 3 6   ? 1.424   -64.682 35.772  1 38.9  ? 6   DA  U OP1   1 
ATOM   6156  O  OP2   . DA  D 3 6   ? 0.469   -62.39  36.449  1 38.98 ? 6   DA  U OP2   1 
ATOM   6157  O  "O5'" . DA  D 3 6   ? 2.787   -63.053 37.093  1 39.75 ? 6   DA  U "O5'" 1 
ATOM   6158  C  "C5'" . DA  D 3 6   ? 4.082   -63.58  36.821  1 40.37 ? 6   DA  U "C5'" 1 
ATOM   6159  C  "C4'" . DA  D 3 6   ? 5.122   -62.964 37.742  1 40.96 ? 6   DA  U "C4'" 1 
ATOM   6160  O  "O4'" . DA  D 3 6   ? 5.365   -61.589 37.355  1 41.24 ? 6   DA  U "O4'" 1 
ATOM   6161  C  "C3'" . DA  D 3 6   ? 4.728   -62.909 39.223  1 41.13 ? 6   DA  U "C3'" 1 
ATOM   6162  O  "O3'" . DA  D 3 6   ? 5.431   -63.917 39.975  1 41.06 ? 6   DA  U "O3'" 1 
ATOM   6163  C  "C2'" . DA  D 3 6   ? 5.114   -61.487 39.673  1 41.32 ? 6   DA  U "C2'" 1 
ATOM   6164  C  "C1'" . DA  D 3 6   ? 5.872   -60.919 38.476  1 41.42 ? 6   DA  U "C1'" 1 
ATOM   6165  N  N9    . DA  D 3 6   ? 5.689   -59.477 38.317  1 41.61 ? 6   DA  U N9    1 
ATOM   6166  C  C8    . DA  D 3 6   ? 4.512   -58.818 38.074  1 41.71 ? 6   DA  U C8    1 
ATOM   6167  N  N7    . DA  D 3 6   ? 4.618   -57.507 38.106  1 41.59 ? 6   DA  U N7    1 
ATOM   6168  C  C5    . DA  D 3 6   ? 5.942   -57.29  38.444  1 41.42 ? 6   DA  U C5    1 
ATOM   6169  C  C6    . DA  D 3 6   ? 6.693   -56.112 38.635  1 41.16 ? 6   DA  U C6    1 
ATOM   6170  N  N6    . DA  D 3 6   ? 6.186   -54.882 38.506  1 40.83 ? 6   DA  U N6    1 
ATOM   6171  N  N1    . DA  D 3 6   ? 7.99    -56.25  38.967  1 41.33 ? 6   DA  U N1    1 
ATOM   6172  C  C2    . DA  D 3 6   ? 8.502   -57.483 39.077  1 41.39 ? 6   DA  U C2    1 
ATOM   6173  N  N3    . DA  D 3 6   ? 7.898   -58.66  38.937  1 41.43 ? 6   DA  U N3    1 
ATOM   6174  C  C4    . DA  D 3 6   ? 6.601   -58.495 38.637  1 41.51 ? 6   DA  U C4    1 
ATOM   6175  P  P     . DT  D 3 7   ? 5.062   -64.189 41.516  1 41.04 ? 7   DT  U P     1 
ATOM   6176  O  OP1   . DT  D 3 7   ? 5.361   -65.608 41.813  1 40.95 ? 7   DT  U OP1   1 
ATOM   6177  O  OP2   . DT  D 3 7   ? 3.702   -63.657 41.771  1 41.18 ? 7   DT  U OP2   1 
ATOM   6178  O  "O5'" . DT  D 3 7   ? 6.11    -63.26  42.3    1 41.17 ? 7   DT  U "O5'" 1 
ATOM   6179  C  "C5'" . DT  D 3 7   ? 7.492   -63.57  42.241  1 41.19 ? 7   DT  U "C5'" 1 
ATOM   6180  C  "C4'" . DT  D 3 7   ? 8.361   -62.38  42.626  1 41.17 ? 7   DT  U "C4'" 1 
ATOM   6181  O  "O4'" . DT  D 3 7   ? 8.068   -61.25  41.789  1 40.98 ? 7   DT  U "O4'" 1 
ATOM   6182  C  "C3'" . DT  D 3 7   ? 8.173   -61.822 44.021  1 41.38 ? 7   DT  U "C3'" 1 
ATOM   6183  O  "O3'" . DT  D 3 7   ? 8.85    -62.62  44.982  1 41.93 ? 7   DT  U "O3'" 1 
ATOM   6184  C  "C2'" . DT  D 3 7   ? 8.845   -60.456 43.88   1 41.21 ? 7   DT  U "C2'" 1 
ATOM   6185  C  "C1'" . DT  D 3 7   ? 8.632   -60.108 42.401  1 40.99 ? 7   DT  U "C1'" 1 
ATOM   6186  N  N1    . DT  D 3 7   ? 7.723   -58.963 42.223  1 40.98 ? 7   DT  U N1    1 
ATOM   6187  C  C2    . DT  D 3 7   ? 8.225   -57.692 42.375  1 40.95 ? 7   DT  U C2    1 
ATOM   6188  O  O2    . DT  D 3 7   ? 9.421   -57.451 42.464  1 40.95 ? 7   DT  U O2    1 
ATOM   6189  N  N3    . DT  D 3 7   ? 7.286   -56.696 42.261  1 40.82 ? 7   DT  U N3    1 
ATOM   6190  C  C4    . DT  D 3 7   ? 5.917   -56.851 42.118  1 40.64 ? 7   DT  U C4    1 
ATOM   6191  O  O4    . DT  D 3 7   ? 5.194   -55.865 42.052  1 40.51 ? 7   DT  U O4    1 
ATOM   6192  C  C5    . DT  D 3 7   ? 5.459   -58.209 42.043  1 40.68 ? 7   DT  U C5    1 
ATOM   6193  C  C7    . DT  D 3 7   ? 4.007   -58.493 41.86   1 40.57 ? 7   DT  U C7    1 
ATOM   6194  C  C6    . DT  D 3 7   ? 6.368   -59.189 42.13   1 40.9  ? 7   DT  U C6    1 
ATOM   6195  P  P     . DG  D 3 8   ? 8.447   -62.519 46.527  1 42.51 ? 8   DG  U P     1 
ATOM   6196  O  OP1   . DG  D 3 8   ? 8.886   -63.768 47.199  1 42.7  ? 8   DG  U OP1   1 
ATOM   6197  O  OP2   . DG  D 3 8   ? 7.026   -62.104 46.597  1 42.79 ? 8   DG  U OP2   1 
ATOM   6198  O  "O5'" . DG  D 3 8   ? 9.336   -61.299 47.064  1 42.41 ? 8   DG  U "O5'" 1 
ATOM   6199  C  "C5'" . DG  D 3 8   ? 10.742  -61.26  46.812  1 42.24 ? 8   DG  U "C5'" 1 
ATOM   6200  C  "C4'" . DG  D 3 8   ? 11.307  -59.881 47.108  1 42.21 ? 8   DG  U "C4'" 1 
ATOM   6201  O  "O4'" . DG  D 3 8   ? 10.599  -58.88  46.326  1 41.77 ? 8   DG  U "O4'" 1 
ATOM   6202  C  "C3'" . DG  D 3 8   ? 11.193  -59.441 48.571  1 42.77 ? 8   DG  U "C3'" 1 
ATOM   6203  O  "O3'" . DG  D 3 8   ? 12.451  -58.995 49.055  1 43.77 ? 8   DG  U "O3'" 1 
ATOM   6204  C  "C2'" . DG  D 3 8   ? 10.172  -58.31  48.536  1 42.26 ? 8   DG  U "C2'" 1 
ATOM   6205  C  "C1'" . DG  D 3 8   ? 10.352  -57.76  47.134  1 41.72 ? 8   DG  U "C1'" 1 
ATOM   6206  N  N9    . DG  D 3 8   ? 9.16    -57.072 46.644  1 41.16 ? 8   DG  U N9    1 
ATOM   6207  C  C8    . DG  D 3 8   ? 7.905   -57.611 46.494  1 41.07 ? 8   DG  U C8    1 
ATOM   6208  N  N7    . DG  D 3 8   ? 6.996   -56.733 46.165  1 40.78 ? 8   DG  U N7    1 
ATOM   6209  C  C5    . DG  D 3 8   ? 7.681   -55.527 46.142  1 40.5  ? 8   DG  U C5    1 
ATOM   6210  C  C6    . DG  D 3 8   ? 7.225   -54.227 45.827  1 40.11 ? 8   DG  U C6    1 
ATOM   6211  O  O6    . DG  D 3 8   ? 6.082   -53.878 45.506  1 40.07 ? 8   DG  U O6    1 
ATOM   6212  N  N1    . DG  D 3 8   ? 8.254   -53.286 45.907  1 39.84 ? 8   DG  U N1    1 
ATOM   6213  C  C2    . DG  D 3 8   ? 9.555   -53.572 46.26   1 39.74 ? 8   DG  U C2    1 
ATOM   6214  N  N2    . DG  D 3 8   ? 10.406  -52.544 46.295  1 39.51 ? 8   DG  U N2    1 
ATOM   6215  N  N3    . DG  D 3 8   ? 9.993   -54.783 46.551  1 40.16 ? 8   DG  U N3    1 
ATOM   6216  C  C4    . DG  D 3 8   ? 9.01    -55.714 46.455  1 40.63 ? 8   DG  U C4    1 
ATOM   6217  P  P     . DC  D 3 9   ? 12.657  -58.716 50.62   1 44.66 ? 9   DC  U P     1 
ATOM   6218  O  OP1   . DC  D 3 9   ? 14.023  -59.167 50.986  1 44.71 ? 9   DC  U OP1   1 
ATOM   6219  O  OP2   . DC  D 3 9   ? 11.481  -59.255 51.35   1 44.74 ? 9   DC  U OP2   1 
ATOM   6220  O  "O5'" . DC  D 3 9   ? 12.595  -57.123 50.698  1 45.2  ? 9   DC  U "O5'" 1 
ATOM   6221  C  "C5'" . DC  D 3 9   ? 13.647  -56.345 50.148  1 45.93 ? 9   DC  U "C5'" 1 
ATOM   6222  C  "C4'" . DC  D 3 9   ? 13.429  -54.876 50.432  1 46.72 ? 9   DC  U "C4'" 1 
ATOM   6223  O  "O4'" . DC  D 3 9   ? 12.248  -54.427 49.726  1 46.81 ? 9   DC  U "O4'" 1 
ATOM   6224  C  "C3'" . DC  D 3 9   ? 13.216  -54.532 51.908  1 47.52 ? 9   DC  U "C3'" 1 
ATOM   6225  O  "O3'" . DC  D 3 9   ? 13.994  -53.399 52.271  1 48.51 ? 9   DC  U "O3'" 1 
ATOM   6226  C  "C2'" . DC  D 3 9   ? 11.72   -54.244 52      1 47.27 ? 9   DC  U "C2'" 1 
ATOM   6227  C  "C1'" . DC  D 3 9   ? 11.402  -53.731 50.606  1 47    ? 9   DC  U "C1'" 1 
ATOM   6228  N  N1    . DC  D 3 9   ? 10.001  -53.99  50.206  1 47.03 ? 9   DC  U N1    1 
ATOM   6229  C  C2    . DC  D 3 9   ? 9.163   -52.917 49.933  1 46.93 ? 9   DC  U C2    1 
ATOM   6230  O  O2    . DC  D 3 9   ? 9.629   -51.778 49.971  1 46.87 ? 9   DC  U O2    1 
ATOM   6231  N  N3    . DC  D 3 9   ? 7.873   -53.158 49.59   1 47.01 ? 9   DC  U N3    1 
ATOM   6232  C  C4    . DC  D 3 9   ? 7.418   -54.412 49.544  1 47.18 ? 9   DC  U C4    1 
ATOM   6233  N  N4    . DC  D 3 9   ? 6.135   -54.602 49.21   1 47.25 ? 9   DC  U N4    1 
ATOM   6234  C  C5    . DC  D 3 9   ? 8.255   -55.525 49.853  1 47.24 ? 9   DC  U C5    1 
ATOM   6235  C  C6    . DC  D 3 9   ? 9.527   -55.268 50.178  1 47.2  ? 9   DC  U C6    1 
ATOM   6236  P  P     . DA  D 3 10  ? 14.454  -53.183 53.8    1 49.33 ? 10  DA  U P     1 
ATOM   6237  O  OP1   . DA  D 3 10  ? 15.906  -53.458 53.884  1 49.42 ? 10  DA  U OP1   1 
ATOM   6238  O  OP2   . DA  D 3 10  ? 13.516  -53.912 54.679  1 49.16 ? 10  DA  U OP2   1 
ATOM   6239  O  "O5'" . DA  D 3 10  ? 14.208  -51.622 54.021  1 50.01 ? 10  DA  U "O5'" 1 
ATOM   6240  C  "C5'" . DA  D 3 10  ? 13.242  -50.942 53.217  1 50.65 ? 10  DA  U "C5'" 1 
ATOM   6241  C  "C4'" . DA  D 3 10  ? 12.652  -49.743 53.936  1 51.21 ? 10  DA  U "C4'" 1 
ATOM   6242  O  "O4'" . DA  D 3 10  ? 11.236  -49.658 53.636  1 51.08 ? 10  DA  U "O4'" 1 
ATOM   6243  C  "C3'" . DA  D 3 10  ? 12.714  -49.804 55.449  1 51.95 ? 10  DA  U "C3'" 1 
ATOM   6244  O  "O3'" . DA  D 3 10  ? 12.586  -48.491 55.981  1 53.03 ? 10  DA  U "O3'" 1 
ATOM   6245  C  "C2'" . DA  D 3 10  ? 11.491  -50.657 55.764  1 51.56 ? 10  DA  U "C2'" 1 
ATOM   6246  C  "C1'" . DA  D 3 10  ? 10.483  -50.127 54.747  1 51.08 ? 10  DA  U "C1'" 1 
ATOM   6247  N  N9    . DA  D 3 10  ? 9.548   -51.137 54.27   1 50.56 ? 10  DA  U N9    1 
ATOM   6248  C  C8    . DA  D 3 10  ? 9.732   -52.489 54.259  1 50.39 ? 10  DA  U C8    1 
ATOM   6249  N  N7    . DA  D 3 10  ? 8.74    -53.154 53.719  1 50.26 ? 10  DA  U N7    1 
ATOM   6250  C  C5    . DA  D 3 10  ? 7.839   -52.168 53.362  1 50.2  ? 10  DA  U C5    1 
ATOM   6251  C  C6    . DA  D 3 10  ? 6.579   -52.217 52.743  1 50.05 ? 10  DA  U C6    1 
ATOM   6252  N  N6    . DA  D 3 10  ? 5.991   -53.355 52.365  1 50.01 ? 10  DA  U N6    1 
ATOM   6253  N  N1    . DA  D 3 10  ? 5.943   -51.047 52.526  1 49.98 ? 10  DA  U N1    1 
ATOM   6254  C  C2    . DA  D 3 10  ? 6.531   -49.914 52.919  1 50.01 ? 10  DA  U C2    1 
ATOM   6255  N  N3    . DA  D 3 10  ? 7.726   -49.74  53.475  1 50.14 ? 10  DA  U N3    1 
ATOM   6256  C  C4    . DA  D 3 10  ? 8.328   -50.919 53.684  1 50.28 ? 10  DA  U C4    1 
ATOM   6257  P  P     . DG  D 3 11  ? 13.329  -48.096 57.341  1 53.92 ? 11  DG  U P     1 
ATOM   6258  O  OP1   . DG  D 3 11  ? 14.5    -47.256 56.992  1 53.86 ? 11  DG  U OP1   1 
ATOM   6259  O  OP2   . DG  D 3 11  ? 13.509  -49.334 58.141  1 53.72 ? 11  DG  U OP2   1 
ATOM   6260  O  "O5'" . DG  D 3 11  ? 12.242  -47.184 58.08   1 54.84 ? 11  DG  U "O5'" 1 
ATOM   6261  C  "C5'" . DG  D 3 11  ? 11.885  -45.912 57.54   1 55.65 ? 11  DG  U "C5'" 1 
ATOM   6262  C  "C4'" . DG  D 3 11  ? 10.491  -45.491 57.985  1 56.44 ? 11  DG  U "C4'" 1 
ATOM   6263  O  "O4'" . DG  D 3 11  ? 9.509   -46.439 57.501  1 56.48 ? 11  DG  U "O4'" 1 
ATOM   6264  C  "C3'" . DG  D 3 11  ? 10.278  -45.394 59.491  1 57.23 ? 11  DG  U "C3'" 1 
ATOM   6265  O  "O3'" . DG  D 3 11  ? 9.417   -44.3   59.775  1 58.37 ? 11  DG  U "O3'" 1 
ATOM   6266  C  "C2'" . DG  D 3 11  ? 9.628   -46.735 59.836  1 56.86 ? 11  DG  U "C2'" 1 
ATOM   6267  C  "C1'" . DG  D 3 11  ? 8.819   -47.034 58.583  1 56.52 ? 11  DG  U "C1'" 1 
ATOM   6268  N  N9    . DG  D 3 11  ? 8.693   -48.46  58.301  1 56.31 ? 11  DG  U N9    1 
ATOM   6269  C  C8    . DG  D 3 11  ? 9.611   -49.445 58.578  1 56.28 ? 11  DG  U C8    1 
ATOM   6270  N  N7    . DG  D 3 11  ? 9.252   -50.627 58.153  1 56.26 ? 11  DG  U N7    1 
ATOM   6271  C  C5    . DG  D 3 11  ? 8.022   -50.408 57.541  1 56.2  ? 11  DG  U C5    1 
ATOM   6272  C  C6    . DG  D 3 11  ? 7.138   -51.319 56.899  1 56.12 ? 11  DG  U C6    1 
ATOM   6273  O  O6    . DG  D 3 11  ? 7.277   -52.543 56.725  1 55.98 ? 11  DG  U O6    1 
ATOM   6274  N  N1    . DG  D 3 11  ? 6.005   -50.675 56.412  1 56.04 ? 11  DG  U N1    1 
ATOM   6275  C  C2    . DG  D 3 11  ? 5.751   -49.33  56.536  1 55.94 ? 11  DG  U C2    1 
ATOM   6276  N  N2    . DG  D 3 11  ? 4.603   -48.894 56.008  1 55.81 ? 11  DG  U N2    1 
ATOM   6277  N  N3    . DG  D 3 11  ? 6.559   -48.473 57.143  1 56.03 ? 11  DG  U N3    1 
ATOM   6278  C  C4    . DG  D 3 11  ? 7.672   -49.077 57.617  1 56.18 ? 11  DG  U C4    1 
ATOM   6279  P  P     . DA  D 3 12  ? 9.336   -43.671 61.25   1 59.44 ? 12  DA  U P     1 
ATOM   6280  O  OP1   . DA  D 3 12  ? 9.86    -42.285 61.189  1 59.49 ? 12  DA  U OP1   1 
ATOM   6281  O  OP2   . DA  D 3 12  ? 9.912   -44.642 62.214  1 59.5  ? 12  DA  U OP2   1 
ATOM   6282  O  "O5'" . DA  D 3 12  ? 7.761   -43.608 61.495  1 59.85 ? 12  DA  U "O5'" 1 
ATOM   6283  C  "C5'" . DA  D 3 12  ? 6.883   -43.417 60.377  1 60    ? 12  DA  U "C5'" 1 
ATOM   6284  C  "C4'" . DA  D 3 12  ? 5.528   -44.058 60.622  1 60.01 ? 12  DA  U "C4'" 1 
ATOM   6285  O  "O4'" . DA  D 3 12  ? 5.54    -45.421 60.127  1 59.87 ? 12  DA  U "O4'" 1 
ATOM   6286  C  "C3'" . DA  D 3 12  ? 5.104   -44.133 62.091  1 60.05 ? 12  DA  U "C3'" 1 
ATOM   6287  O  "O3'" . DA  D 3 12  ? 3.775   -43.653 62.246  1 60.22 ? 12  DA  U "O3'" 1 
ATOM   6288  C  "C2'" . DA  D 3 12  ? 5.221   -45.618 62.426  1 59.92 ? 12  DA  U "C2'" 1 
ATOM   6289  C  "C1'" . DA  D 3 12  ? 4.946   -46.263 61.078  1 59.87 ? 12  DA  U "C1'" 1 
ATOM   6290  N  N9    . DA  D 3 12  ? 5.524   -47.592 60.946  1 59.88 ? 12  DA  U N9    1 
ATOM   6291  C  C8    . DA  D 3 12  ? 6.724   -48.017 61.438  1 59.9  ? 12  DA  U C8    1 
ATOM   6292  N  N7    . DA  D 3 12  ? 6.975   -49.282 61.201  1 59.88 ? 12  DA  U N7    1 
ATOM   6293  C  C5    . DA  D 3 12  ? 5.846   -49.724 60.534  1 59.88 ? 12  DA  U C5    1 
ATOM   6294  C  C6    . DA  D 3 12  ? 5.49    -50.975 60.006  1 60    ? 12  DA  U C6    1 
ATOM   6295  N  N6    . DA  D 3 12  ? 6.277   -52.052 60.072  1 60.1  ? 12  DA  U N6    1 
ATOM   6296  N  N1    . DA  D 3 12  ? 4.29    -51.078 59.402  1 59.99 ? 12  DA  U N1    1 
ATOM   6297  C  C2    . DA  D 3 12  ? 3.523   -49.988 59.304  1 59.9  ? 12  DA  U C2    1 
ATOM   6298  N  N3    . DA  D 3 12  ? 3.739   -48.767 59.78   1 59.81 ? 12  DA  U N3    1 
ATOM   6299  C  C4    . DA  D 3 12  ? 4.936   -48.698 60.38   1 59.84 ? 12  DA  U C4    1 
ATOM   6300  P  P     . DC  D 3 13  ? 3.291   -43.103 63.67   1 60.29 ? 13  DC  U P     1 
ATOM   6301  O  OP1   . DC  D 3 13  ? 2.265   -42.06  63.426  1 60.37 ? 13  DC  U OP1   1 
ATOM   6302  O  OP2   . DC  D 3 13  ? 4.5     -42.772 64.462  1 60.26 ? 13  DC  U OP2   1 
ATOM   6303  O  "O5'" . DC  D 3 13  ? 2.608   -44.406 64.337  1 60.17 ? 13  DC  U "O5'" 1 
ATOM   6304  C  "C5'" . DC  D 3 13  ? 1.179   -44.67  64.215  1 59.96 ? 13  DC  U "C5'" 1 
ATOM   6305  C  "C4'" . DC  D 3 13  ? 0.789   -45.235 62.844  1 59.76 ? 13  DC  U "C4'" 1 
ATOM   6306  O  "O4'" . DC  D 3 13  ? 1.753   -46.229 62.4    1 59.67 ? 13  DC  U "O4'" 1 
ATOM   6307  C  "C3'" . DC  D 3 13  ? -0.561  -45.941 62.804  1 59.62 ? 13  DC  U "C3'" 1 
ATOM   6308  O  "O3'" . DC  D 3 13  ? -1.148  -45.805 61.514  1 59.6  ? 13  DC  U "O3'" 1 
ATOM   6309  C  "C2'" . DC  D 3 13  ? -0.178  -47.388 63.097  1 59.56 ? 13  DC  U "C2'" 1 
ATOM   6310  C  "C1'" . DC  D 3 13  ? 1.156   -47.51  62.365  1 59.55 ? 13  DC  U "C1'" 1 
ATOM   6311  N  N1    . DC  D 3 13  ? 2.115   -48.491 62.982  1 59.4  ? 13  DC  U N1    1 
ATOM   6312  C  C2    . DC  D 3 13  ? 2.128   -49.825 62.551  1 59.19 ? 13  DC  U C2    1 
ATOM   6313  O  O2    . DC  D 3 13  ? 1.31    -50.194 61.696  1 59.1  ? 13  DC  U O2    1 
ATOM   6314  N  N3    . DC  D 3 13  ? 3.029   -50.682 63.1    1 59.06 ? 13  DC  U N3    1 
ATOM   6315  C  C4    . DC  D 3 13  ? 3.896   -50.245 64.017  1 59    ? 13  DC  U C4    1 
ATOM   6316  N  N4    . DC  D 3 13  ? 4.758   -51.124 64.536  1 58.9  ? 13  DC  U N4    1 
ATOM   6317  C  C5    . DC  D 3 13  ? 3.913   -48.891 64.447  1 59.16 ? 13  DC  U C5    1 
ATOM   6318  C  C6    . DC  D 3 13  ? 3.018   -48.056 63.909  1 59.32 ? 13  DC  U C6    1 
ATOM   6319  O  "O5'" . DG  E 2 1   ? 4.039   -60.843 62.414  1 45.43 ? 1   DG  V "O5'" 1 
ATOM   6320  C  "C5'" . DG  E 2 1   ? 2.716   -61.388 62.572  1 45.58 ? 1   DG  V "C5'" 1 
ATOM   6321  C  "C4'" . DG  E 2 1   ? 1.654   -60.499 61.928  1 45.68 ? 1   DG  V "C4'" 1 
ATOM   6322  O  "O4'" . DG  E 2 1   ? 1.762   -59.152 62.452  1 45.75 ? 1   DG  V "O4'" 1 
ATOM   6323  C  "C3'" . DG  E 2 1   ? 1.747   -60.368 60.41   1 45.7  ? 1   DG  V "C3'" 1 
ATOM   6324  O  "O3'" . DG  E 2 1   ? 0.454   -60.299 59.825  1 45.68 ? 1   DG  V "O3'" 1 
ATOM   6325  C  "C2'" . DG  E 2 1   ? 2.5     -59.065 60.227  1 45.7  ? 1   DG  V "C2'" 1 
ATOM   6326  C  "C1'" . DG  E 2 1   ? 1.996   -58.247 61.399  1 45.74 ? 1   DG  V "C1'" 1 
ATOM   6327  N  N9    . DG  E 2 1   ? 2.966   -57.266 61.843  1 45.79 ? 1   DG  V N9    1 
ATOM   6328  C  C8    . DG  E 2 1   ? 4.289   -57.491 62.141  1 45.78 ? 1   DG  V C8    1 
ATOM   6329  N  N7    . DG  E 2 1   ? 4.954   -56.4   62.402  1 45.83 ? 1   DG  V N7    1 
ATOM   6330  C  C5    . DG  E 2 1   ? 4.017   -55.386 62.229  1 45.84 ? 1   DG  V C5    1 
ATOM   6331  C  C6    . DG  E 2 1   ? 4.149   -53.99  62.389  1 45.87 ? 1   DG  V C6    1 
ATOM   6332  O  O6    . DG  E 2 1   ? 5.158   -53.349 62.72   1 45.75 ? 1   DG  V O6    1 
ATOM   6333  N  N1    . DG  E 2 1   ? 2.95    -53.328 62.114  1 46.02 ? 1   DG  V N1    1 
ATOM   6334  C  C2    . DG  E 2 1   ? 1.773   -53.945 61.747  1 45.98 ? 1   DG  V C2    1 
ATOM   6335  N  N2    . DG  E 2 1   ? 0.733   -53.142 61.479  1 46.08 ? 1   DG  V N2    1 
ATOM   6336  N  N3    . DG  E 2 1   ? 1.64    -55.25  61.599  1 45.84 ? 1   DG  V N3    1 
ATOM   6337  C  C4    . DG  E 2 1   ? 2.798   -55.905 61.855  1 45.83 ? 1   DG  V C4    1 
ATOM   6338  P  P     . DT  E 2 2   ? 0.283   -60.579 58.255  1 45.6  ? 2   DT  V P     1 
ATOM   6339  O  OP1   . DT  E 2 2   ? -0.852  -61.514 58.075  1 45.74 ? 2   DT  V OP1   1 
ATOM   6340  O  OP2   . DT  E 2 2   ? 1.615   -60.92  57.698  1 45.61 ? 2   DT  V OP2   1 
ATOM   6341  O  "O5'" . DT  E 2 2   ? -0.155  -59.157 57.679  1 45.07 ? 2   DT  V "O5'" 1 
ATOM   6342  C  "C5'" . DT  E 2 2   ? -1.379  -58.563 58.067  1 44.46 ? 2   DT  V "C5'" 1 
ATOM   6343  C  "C4'" . DT  E 2 2   ? -1.38   -57.1   57.679  1 44.03 ? 2   DT  V "C4'" 1 
ATOM   6344  O  "O4'" . DT  E 2 2   ? -0.317  -56.425 58.405  1 43.78 ? 2   DT  V "O4'" 1 
ATOM   6345  C  "C3'" . DT  E 2 2   ? -1.114  -56.832 56.187  1 43.99 ? 2   DT  V "C3'" 1 
ATOM   6346  O  "O3'" . DT  E 2 2   ? -2.095  -55.939 55.653  1 44.18 ? 2   DT  V "O3'" 1 
ATOM   6347  C  "C2'" . DT  E 2 2   ? 0.28    -56.207 56.175  1 43.73 ? 2   DT  V "C2'" 1 
ATOM   6348  C  "C1'" . DT  E 2 2   ? 0.34    -55.542 57.538  1 43.48 ? 2   DT  V "C1'" 1 
ATOM   6349  N  N1    . DT  E 2 2   ? 1.744   -55.313 58.021  1 43.02 ? 2   DT  V N1    1 
ATOM   6350  C  C2    . DT  E 2 2   ? 2.117   -54.051 58.432  1 42.81 ? 2   DT  V C2    1 
ATOM   6351  O  O2    . DT  E 2 2   ? 1.342   -53.11  58.49   1 42.68 ? 2   DT  V O2    1 
ATOM   6352  N  N3    . DT  E 2 2   ? 3.447   -53.926 58.756  1 42.73 ? 2   DT  V N3    1 
ATOM   6353  C  C4    . DT  E 2 2   ? 4.418   -54.917 58.713  1 42.6  ? 2   DT  V C4    1 
ATOM   6354  O  O4    . DT  E 2 2   ? 5.571   -54.658 59.041  1 42.45 ? 2   DT  V O4    1 
ATOM   6355  C  C5    . DT  E 2 2   ? 3.962   -56.204 58.265  1 42.7  ? 2   DT  V C5    1 
ATOM   6356  C  C7    . DT  E 2 2   ? 4.927   -57.346 58.17   1 42.82 ? 2   DT  V C7    1 
ATOM   6357  C  C6    . DT  E 2 2   ? 2.67    -56.335 57.924  1 42.82 ? 2   DT  V C6    1 
ATOM   6358  P  P     . DC  E 2 3   ? -2.278  -55.761 54.058  1 44.35 ? 3   DC  V P     1 
ATOM   6359  O  OP1   . DC  E 2 3   ? -3.606  -56.297 53.685  1 44.59 ? 3   DC  V OP1   1 
ATOM   6360  O  OP2   . DC  E 2 3   ? -1.065  -56.263 53.371  1 44.41 ? 3   DC  V OP2   1 
ATOM   6361  O  "O5'" . DC  E 2 3   ? -2.346  -54.177 53.905  1 43.87 ? 3   DC  V "O5'" 1 
ATOM   6362  C  "C5'" . DC  E 2 3   ? -3.12   -53.444 54.82   1 43.32 ? 3   DC  V "C5'" 1 
ATOM   6363  C  "C4'" . DC  E 2 3   ? -2.471  -52.119 55.117  1 42.7  ? 3   DC  V "C4'" 1 
ATOM   6364  O  "O4'" . DC  E 2 3   ? -1.219  -52.348 55.78   1 42.33 ? 3   DC  V "O4'" 1 
ATOM   6365  C  "C3'" . DC  E 2 3   ? -2.112  -51.315 53.891  1 42.38 ? 3   DC  V "C3'" 1 
ATOM   6366  O  "O3'" . DC  E 2 3   ? -3.239  -50.519 53.488  1 42.19 ? 3   DC  V "O3'" 1 
ATOM   6367  C  "C2'" . DC  E 2 3   ? -0.95   -50.443 54.392  1 42.18 ? 3   DC  V "C2'" 1 
ATOM   6368  C  "C1'" . DC  E 2 3   ? -0.391  -51.228 55.586  1 41.93 ? 3   DC  V "C1'" 1 
ATOM   6369  N  N1    . DC  E 2 3   ? 1.017   -51.705 55.42   1 41.27 ? 3   DC  V N1    1 
ATOM   6370  C  C2    . DC  E 2 3   ? 2.083   -50.845 55.709  1 40.97 ? 3   DC  V C2    1 
ATOM   6371  O  O2    . DC  E 2 3   ? 1.843   -49.671 56.016  1 40.96 ? 3   DC  V O2    1 
ATOM   6372  N  N3    . DC  E 2 3   ? 3.353   -51.321 55.631  1 40.69 ? 3   DC  V N3    1 
ATOM   6373  C  C4    . DC  E 2 3   ? 3.57    -52.597 55.306  1 40.47 ? 3   DC  V C4    1 
ATOM   6374  N  N4    . DC  E 2 3   ? 4.837   -53.023 55.24   1 40.17 ? 3   DC  V N4    1 
ATOM   6375  C  C5    . DC  E 2 3   ? 2.495   -53.496 55.048  1 40.67 ? 3   DC  V C5    1 
ATOM   6376  C  C6    . DC  E 2 3   ? 1.251   -53.005 55.092  1 40.95 ? 3   DC  V C6    1 
ATOM   6377  P  P     . DT  E 2 4   ? -3.786  -50.587 51.978  1 41.84 ? 4   DT  V P     1 
ATOM   6378  O  OP1   . DT  E 2 4   ? -5.163  -50.034 51.968  1 41.54 ? 4   DT  V OP1   1 
ATOM   6379  O  OP2   . DT  E 2 4   ? -3.531  -51.957 51.464  1 41.91 ? 4   DT  V OP2   1 
ATOM   6380  O  "O5'" . DT  E 2 4   ? -2.812  -49.579 51.2    1 41.29 ? 4   DT  V "O5'" 1 
ATOM   6381  C  "C5'" . DT  E 2 4   ? -2.643  -48.256 51.684  1 40.61 ? 4   DT  V "C5'" 1 
ATOM   6382  C  "C4'" . DT  E 2 4   ? -1.262  -47.723 51.359  1 39.88 ? 4   DT  V "C4'" 1 
ATOM   6383  O  "O4'" . DT  E 2 4   ? -0.25   -48.556 51.975  1 39.57 ? 4   DT  V "O4'" 1 
ATOM   6384  C  "C3'" . DT  E 2 4   ? -0.928  -47.665 49.878  1 39.6  ? 4   DT  V "C3'" 1 
ATOM   6385  O  "O3'" . DT  E 2 4   ? -0.363  -46.412 49.561  1 39.52 ? 4   DT  V "O3'" 1 
ATOM   6386  C  "C2'" . DT  E 2 4   ? 0.079   -48.788 49.694  1 39.49 ? 4   DT  V "C2'" 1 
ATOM   6387  C  "C1'" . DT  E 2 4   ? 0.761   -48.825 51.046  1 39.53 ? 4   DT  V "C1'" 1 
ATOM   6388  N  N1    . DT  E 2 4   ? 1.342   -50.159 51.35   1 39.74 ? 4   DT  V N1    1 
ATOM   6389  C  C2    . DT  E 2 4   ? 2.703   -50.279 51.52   1 39.82 ? 4   DT  V C2    1 
ATOM   6390  O  O2    . DT  E 2 4   ? 3.463   -49.327 51.533  1 39.85 ? 4   DT  V O2    1 
ATOM   6391  N  N3    . DT  E 2 4   ? 3.142   -51.564 51.712  1 39.71 ? 4   DT  V N3    1 
ATOM   6392  C  C4    . DT  E 2 4   ? 2.382   -52.718 51.69   1 39.63 ? 4   DT  V C4    1 
ATOM   6393  O  O4    . DT  E 2 4   ? 2.926   -53.803 51.867  1 39.74 ? 4   DT  V O4    1 
ATOM   6394  C  C5    . DT  E 2 4   ? 0.969   -52.524 51.491  1 39.5  ? 4   DT  V C5    1 
ATOM   6395  C  C7    . DT  E 2 4   ? 0.044   -53.702 51.48   1 39.38 ? 4   DT  V C7    1 
ATOM   6396  C  C6    . DT  E 2 4   ? 0.529   -51.276 51.286  1 39.62 ? 4   DT  V C6    1 
ATOM   6397  P  P     . DG  E 2 5   ? -0.455  -45.86  48.063  1 39.12 ? 5   DG  V P     1 
ATOM   6398  O  OP1   . DG  E 2 5   ? -1.354  -44.68  48.071  1 39.05 ? 5   DG  V OP1   1 
ATOM   6399  O  OP2   . DG  E 2 5   ? -0.753  -47.008 47.174  1 38.93 ? 5   DG  V OP2   1 
ATOM   6400  O  "O5'" . DG  E 2 5   ? 1.045   -45.382 47.766  1 38.76 ? 5   DG  V "O5'" 1 
ATOM   6401  C  "C5'" . DG  E 2 5   ? 1.549   -44.181 48.353  1 38.41 ? 5   DG  V "C5'" 1 
ATOM   6402  C  "C4'" . DG  E 2 5   ? 2.988   -44.349 48.812  1 38.08 ? 5   DG  V "C4'" 1 
ATOM   6403  O  "O4'" . DG  E 2 5   ? 3.08    -45.467 49.729  1 37.95 ? 5   DG  V "O4'" 1 
ATOM   6404  C  "C3'" . DG  E 2 5   ? 4.002   -44.688 47.733  1 37.88 ? 5   DG  V "C3'" 1 
ATOM   6405  O  "O3'" . DG  E 2 5   ? 4.417   -43.524 47.024  1 37.72 ? 5   DG  V "O3'" 1 
ATOM   6406  C  "C2'" . DG  E 2 5   ? 5.134   -45.244 48.581  1 37.8  ? 5   DG  V "C2'" 1 
ATOM   6407  C  "C1'" . DG  E 2 5   ? 4.371   -46.049 49.622  1 37.83 ? 5   DG  V "C1'" 1 
ATOM   6408  N  N9    . DG  E 2 5   ? 4.251   -47.459 49.267  1 37.83 ? 5   DG  V N9    1 
ATOM   6409  C  C8    . DG  E 2 5   ? 3.183   -48.089 48.68   1 37.77 ? 5   DG  V C8    1 
ATOM   6410  N  N7    . DG  E 2 5   ? 3.391   -49.356 48.459  1 37.83 ? 5   DG  V N7    1 
ATOM   6411  C  C5    . DG  E 2 5   ? 4.713   -49.548 48.836  1 38.01 ? 5   DG  V C5    1 
ATOM   6412  C  C6    . DG  E 2 5   ? 5.516   -50.707 48.79   1 38.32 ? 5   DG  V C6    1 
ATOM   6413  O  O6    . DG  E 2 5   ? 5.211   -51.84  48.386  1 38.59 ? 5   DG  V O6    1 
ATOM   6414  N  N1    . DG  E 2 5   ? 6.802   -50.458 49.267  1 38.32 ? 5   DG  V N1    1 
ATOM   6415  C  C2    . DG  E 2 5   ? 7.251   -49.239 49.707  1 38.25 ? 5   DG  V C2    1 
ATOM   6416  N  N2    . DG  E 2 5   ? 8.513   -49.189 50.149  1 38.31 ? 5   DG  V N2    1 
ATOM   6417  N  N3    . DG  E 2 5   ? 6.498   -48.161 49.783  1 38.13 ? 5   DG  V N3    1 
ATOM   6418  C  C4    . DG  E 2 5   ? 5.252   -48.385 49.32   1 37.96 ? 5   DG  V C4    1 
ATOM   6419  P  P     . DC  E 2 6   ? 4.976   -43.645 45.516  1 37.44 ? 6   DC  V P     1 
ATOM   6420  O  OP1   . DC  E 2 6   ? 5.263   -42.274 45.037  1 37.64 ? 6   DC  V OP1   1 
ATOM   6421  O  OP2   . DC  E 2 6   ? 4.051   -44.511 44.753  1 37.22 ? 6   DC  V OP2   1 
ATOM   6422  O  "O5'" . DC  E 2 6   ? 6.364   -44.434 45.681  1 37.34 ? 6   DC  V "O5'" 1 
ATOM   6423  C  "C5'" . DC  E 2 6   ? 7.416   -43.881 46.472  1 37.6  ? 6   DC  V "C5'" 1 
ATOM   6424  C  "C4'" . DC  E 2 6   ? 8.589   -44.847 46.586  1 37.87 ? 6   DC  V "C4'" 1 
ATOM   6425  O  "O4'" . DC  E 2 6   ? 8.192   -46.033 47.329  1 37.88 ? 6   DC  V "O4'" 1 
ATOM   6426  C  "C3'" . DC  E 2 6   ? 9.098   -45.404 45.276  1 38.12 ? 6   DC  V "C3'" 1 
ATOM   6427  O  "O3'" . DC  E 2 6   ? 9.954   -44.487 44.627  1 38.65 ? 6   DC  V "O3'" 1 
ATOM   6428  C  "C2'" . DC  E 2 6   ? 9.848   -46.64  45.742  1 37.87 ? 6   DC  V "C2'" 1 
ATOM   6429  C  "C1'" . DC  E 2 6   ? 8.944   -47.154 46.861  1 37.79 ? 6   DC  V "C1'" 1 
ATOM   6430  N  N1    . DC  E 2 6   ? 8.005   -48.236 46.407  1 37.63 ? 6   DC  V N1    1 
ATOM   6431  C  C2    . DC  E 2 6   ? 8.454   -49.557 46.343  1 37.53 ? 6   DC  V C2    1 
ATOM   6432  O  O2    . DC  E 2 6   ? 9.604   -49.82  46.711  1 37.5  ? 6   DC  V O2    1 
ATOM   6433  N  N3    . DC  E 2 6   ? 7.602   -50.52  45.907  1 37.48 ? 6   DC  V N3    1 
ATOM   6434  C  C4    . DC  E 2 6   ? 6.366   -50.194 45.526  1 37.43 ? 6   DC  V C4    1 
ATOM   6435  N  N4    . DC  E 2 6   ? 5.563   -51.165 45.096  1 37.33 ? 6   DC  V N4    1 
ATOM   6436  C  C5    . DC  E 2 6   ? 5.902   -48.855 45.56   1 37.52 ? 6   DC  V C5    1 
ATOM   6437  C  C6    . DC  E 2 6   ? 6.74    -47.919 46.009  1 37.61 ? 6   DC  V C6    1 
ATOM   6438  P  P     . DA  E 2 7   ? 10.133  -44.597 43.048  1 39.01 ? 7   DA  V P     1 
ATOM   6439  O  OP1   . DA  E 2 7   ? 10.585  -43.277 42.535  1 39.13 ? 7   DA  V OP1   1 
ATOM   6440  O  OP2   . DA  E 2 7   ? 8.895   -45.216 42.508  1 38.97 ? 7   DA  V OP2   1 
ATOM   6441  O  "O5'" . DA  E 2 7   ? 11.335  -45.65  42.923  1 39.45 ? 7   DA  V "O5'" 1 
ATOM   6442  C  "C5'" . DA  E 2 7   ? 11.307  -46.649 41.923  1 40.13 ? 7   DA  V "C5'" 1 
ATOM   6443  C  "C4'" . DA  E 2 7   ? 11.919  -47.933 42.42   1 40.79 ? 7   DA  V "C4'" 1 
ATOM   6444  O  "O4'" . DA  E 2 7   ? 10.961  -48.639 43.234  1 40.94 ? 7   DA  V "O4'" 1 
ATOM   6445  C  "C3'" . DA  E 2 7   ? 12.304  -48.881 41.314  1 41.31 ? 7   DA  V "C3'" 1 
ATOM   6446  O  "O3'" . DA  E 2 7   ? 13.65   -48.652 40.991  1 42.09 ? 7   DA  V "O3'" 1 
ATOM   6447  C  "C2'" . DA  E 2 7   ? 12.101  -50.264 41.931  1 41.15 ? 7   DA  V "C2'" 1 
ATOM   6448  C  "C1'" . DA  E 2 7   ? 11.06   -50.027 43.021  1 40.96 ? 7   DA  V "C1'" 1 
ATOM   6449  N  N9    . DA  E 2 7   ? 9.732   -50.531 42.699  1 40.87 ? 7   DA  V N9    1 
ATOM   6450  C  C8    . DA  E 2 7   ? 8.607   -49.786 42.499  1 40.92 ? 7   DA  V C8    1 
ATOM   6451  N  N7    . DA  E 2 7   ? 7.531   -50.502 42.292  1 40.9  ? 7   DA  V N7    1 
ATOM   6452  C  C5    . DA  E 2 7   ? 7.976   -51.808 42.389  1 40.63 ? 7   DA  V C5    1 
ATOM   6453  C  C6    . DA  E 2 7   ? 7.313   -53.04  42.291  1 40.27 ? 7   DA  V C6    1 
ATOM   6454  N  N6    . DA  E 2 7   ? 6.011   -53.149 42.041  1 40.07 ? 7   DA  V N6    1 
ATOM   6455  N  N1    . DA  E 2 7   ? 8.044   -54.159 42.449  1 40.23 ? 7   DA  V N1    1 
ATOM   6456  C  C2    . DA  E 2 7   ? 9.352   -54.044 42.693  1 40.37 ? 7   DA  V C2    1 
ATOM   6457  N  N3    . DA  E 2 7   ? 10.086  -52.94  42.816  1 40.59 ? 7   DA  V N3    1 
ATOM   6458  C  C4    . DA  E 2 7   ? 9.329   -51.845 42.651  1 40.73 ? 7   DA  V C4    1 
ATOM   6459  P  P     . DT  E 2 8   ? 14.128  -48.7   39.477  1 42.92 ? 8   DT  V P     1 
ATOM   6460  O  OP1   . DT  E 2 8   ? 15.164  -47.659 39.286  1 42.91 ? 8   DT  V OP1   1 
ATOM   6461  O  OP2   . DT  E 2 8   ? 12.92   -48.7   38.62   1 42.85 ? 8   DT  V OP2   1 
ATOM   6462  O  "O5'" . DT  E 2 8   ? 14.814  -50.149 39.4    1 43.62 ? 8   DT  V "O5'" 1 
ATOM   6463  C  "C5'" . DT  E 2 8   ? 15.599  -50.632 40.509  1 44.13 ? 8   DT  V "C5'" 1 
ATOM   6464  C  "C4'" . DT  E 2 8   ? 15.473  -52.144 40.675  1 44.82 ? 8   DT  V "C4'" 1 
ATOM   6465  O  "O4'" . DT  E 2 8   ? 14.078  -52.527 40.772  1 45.09 ? 8   DT  V "O4'" 1 
ATOM   6466  C  "C3'" . DT  E 2 8   ? 16.055  -52.985 39.544  1 45.26 ? 8   DT  V "C3'" 1 
ATOM   6467  O  "O3'" . DT  E 2 8   ? 16.709  -54.119 40.083  1 45.75 ? 8   DT  V "O3'" 1 
ATOM   6468  C  "C2'" . DT  E 2 8   ? 14.821  -53.388 38.739  1 45.22 ? 8   DT  V "C2'" 1 
ATOM   6469  C  "C1'" . DT  E 2 8   ? 13.799  -53.551 39.839  1 45.24 ? 8   DT  V "C1'" 1 
ATOM   6470  N  N1    . DT  E 2 8   ? 12.402  -53.393 39.364  1 45.37 ? 8   DT  V N1    1 
ATOM   6471  C  C2    . DT  E 2 8   ? 11.515  -54.43  39.531  1 45.47 ? 8   DT  V C2    1 
ATOM   6472  O  O2    . DT  E 2 8   ? 11.801  -55.472 40.093  1 45.58 ? 8   DT  V O2    1 
ATOM   6473  N  N3    . DT  E 2 8   ? 10.257  -54.187 39.056  1 45.36 ? 8   DT  V N3    1 
ATOM   6474  C  C4    . DT  E 2 8   ? 9.811   -53.047 38.425  1 45.21 ? 8   DT  V C4    1 
ATOM   6475  O  O4    . DT  E 2 8   ? 8.649   -52.985 38.052  1 45.1  ? 8   DT  V O4    1 
ATOM   6476  C  C5    . DT  E 2 8   ? 10.8    -52.008 38.258  1 45.2  ? 8   DT  V C5    1 
ATOM   6477  C  C7    . DT  E 2 8   ? 10.434  -50.72  37.587  1 45.16 ? 8   DT  V C7    1 
ATOM   6478  C  C6    . DT  E 2 8   ? 12.037  -52.235 38.716  1 45.28 ? 8   DT  V C6    1 
ATOM   6479  P  P     . DT  E 2 9   ? 17.604  -55.05  39.138  1 46.51 ? 9   DT  V P     1 
ATOM   6480  O  OP1   . DT  E 2 9   ? 18.773  -55.498 39.934  1 46.7  ? 9   DT  V OP1   1 
ATOM   6481  O  OP2   . DT  E 2 9   ? 17.811  -54.344 37.839  1 46.58 ? 9   DT  V OP2   1 
ATOM   6482  O  "O5'" . DT  E 2 9   ? 16.645  -56.303 38.864  1 46.45 ? 9   DT  V "O5'" 1 
ATOM   6483  C  "C5'" . DT  E 2 9   ? 16.328  -57.187 39.921  1 46.32 ? 9   DT  V "C5'" 1 
ATOM   6484  C  "C4'" . DT  E 2 9   ? 15.329  -58.234 39.476  1 46.19 ? 9   DT  V "C4'" 1 
ATOM   6485  O  "O4'" . DT  E 2 9   ? 14.096  -57.601 39.051  1 46.07 ? 9   DT  V "O4'" 1 
ATOM   6486  C  "C3'" . DT  E 2 9   ? 15.77   -59.13  38.313  1 46.26 ? 9   DT  V "C3'" 1 
ATOM   6487  O  "O3'" . DT  E 2 9   ? 15.47   -60.477 38.651  1 46.74 ? 9   DT  V "O3'" 1 
ATOM   6488  C  "C2'" . DT  E 2 9   ? 14.898  -58.636 37.16   1 46.07 ? 9   DT  V "C2'" 1 
ATOM   6489  C  "C1'" . DT  E 2 9   ? 13.639  -58.26  37.904  1 46.11 ? 9   DT  V "C1'" 1 
ATOM   6490  N  N1    . DT  E 2 9   ? 12.737  -57.359 37.149  1 46.4  ? 9   DT  V N1    1 
ATOM   6491  C  C2    . DT  E 2 9   ? 11.438  -57.748 36.936  1 46.54 ? 9   DT  V C2    1 
ATOM   6492  O  O2    . DT  E 2 9   ? 10.988  -58.801 37.338  1 46.67 ? 9   DT  V O2    1 
ATOM   6493  N  N3    . DT  E 2 9   ? 10.683  -56.866 36.213  1 46.62 ? 9   DT  V N3    1 
ATOM   6494  C  C4    . DT  E 2 9   ? 11.091  -55.655 35.687  1 46.7  ? 9   DT  V C4    1 
ATOM   6495  O  O4    . DT  E 2 9   ? 10.291  -54.969 35.054  1 46.73 ? 9   DT  V O4    1 
ATOM   6496  C  C5    . DT  E 2 9   ? 12.472  -55.303 35.947  1 46.65 ? 9   DT  V C5    1 
ATOM   6497  C  C7    . DT  E 2 9   ? 13.027  -54.007 35.444  1 46.56 ? 9   DT  V C7    1 
ATOM   6498  C  C6    . DT  E 2 9   ? 13.223  -56.169 36.649  1 46.59 ? 9   DT  V C6    1 
ATOM   6499  P  P     . DC  E 2 10  ? 15.964  -61.708 37.754  1 47.22 ? 10  DC  V P     1 
ATOM   6500  O  OP1   . DC  E 2 10  ? 16.707  -62.641 38.634  1 47.34 ? 10  DC  V OP1   1 
ATOM   6501  O  OP2   . DC  E 2 10  ? 16.607  -61.181 36.525  1 47.42 ? 10  DC  V OP2   1 
ATOM   6502  O  "O5'" . DC  E 2 10  ? 14.579  -62.39  37.335  1 47.14 ? 10  DC  V "O5'" 1 
ATOM   6503  C  "C5'" . DC  E 2 10  ? 13.577  -62.609 38.322  1 47.06 ? 10  DC  V "C5'" 1 
ATOM   6504  C  "C4'" . DC  E 2 10  ? 12.274  -63.081 37.701  1 47.07 ? 10  DC  V "C4'" 1 
ATOM   6505  O  "O4'" . DC  E 2 10  ? 11.605  -61.973 37.054  1 46.83 ? 10  DC  V "O4'" 1 
ATOM   6506  C  "C3'" . DC  E 2 10  ? 12.405  -64.17  36.643  1 47.37 ? 10  DC  V "C3'" 1 
ATOM   6507  O  "O3'" . DC  E 2 10  ? 11.328  -65.085 36.767  1 47.78 ? 10  DC  V "O3'" 1 
ATOM   6508  C  "C2'" . DC  E 2 10  ? 12.332  -63.39  35.332  1 47.11 ? 10  DC  V "C2'" 1 
ATOM   6509  C  "C1'" . DC  E 2 10  ? 11.368  -62.278 35.697  1 46.8  ? 10  DC  V "C1'" 1 
ATOM   6510  N  N1    . DC  E 2 10  ? 11.571  -61.055 34.917  1 46.55 ? 10  DC  V N1    1 
ATOM   6511  C  C2    . DC  E 2 10  ? 10.504  -60.511 34.212  1 46.44 ? 10  DC  V C2    1 
ATOM   6512  O  O2    . DC  E 2 10  ? 9.41    -61.09  34.24   1 46.42 ? 10  DC  V O2    1 
ATOM   6513  N  N3    . DC  E 2 10  ? 10.7    -59.366 33.509  1 46.39 ? 10  DC  V N3    1 
ATOM   6514  C  C4    . DC  E 2 10  ? 11.901  -58.782 33.507  1 46.29 ? 10  DC  V C4    1 
ATOM   6515  N  N4    . DC  E 2 10  ? 12.05   -57.655 32.808  1 46.08 ? 10  DC  V N4    1 
ATOM   6516  C  C5    . DC  E 2 10  ? 13.003  -59.335 34.215  1 46.39 ? 10  DC  V C5    1 
ATOM   6517  C  C6    . DC  E 2 10  ? 12.792  -60.457 34.906  1 46.48 ? 10  DC  V C6    1 
ATOM   6518  P  P     . DC  E 2 11  ? 11.398  -66.503 36.039  1 48.23 ? 11  DC  V P     1 
ATOM   6519  O  OP1   . DC  E 2 11  ? 10.814  -67.51  36.949  1 48.42 ? 11  DC  V OP1   1 
ATOM   6520  O  OP2   . DC  E 2 11  ? 12.772  -66.686 35.523  1 48.24 ? 11  DC  V OP2   1 
ATOM   6521  O  "O5'" . DC  E 2 11  ? 10.425  -66.304 34.789  1 48.91 ? 11  DC  V "O5'" 1 
ATOM   6522  C  "C5'" . DC  E 2 11  ? 9.036   -66.141 34.998  1 49.76 ? 11  DC  V "C5'" 1 
ATOM   6523  C  "C4'" . DC  E 2 11  ? 8.331   -65.757 33.714  1 50.71 ? 11  DC  V "C4'" 1 
ATOM   6524  O  "O4'" . DC  E 2 11  ? 8.78    -64.448 33.271  1 50.79 ? 11  DC  V "O4'" 1 
ATOM   6525  C  "C3'" . DC  E 2 11  ? 8.554   -66.705 32.527  1 51.6  ? 11  DC  V "C3'" 1 
ATOM   6526  O  "O3'" . DC  E 2 11  ? 7.301   -66.948 31.889  1 52.81 ? 11  DC  V "O3'" 1 
ATOM   6527  C  "C2'" . DC  E 2 11  ? 9.489   -65.896 31.622  1 51.2  ? 11  DC  V "C2'" 1 
ATOM   6528  C  "C1'" . DC  E 2 11  ? 8.971   -64.501 31.883  1 50.83 ? 11  DC  V "C1'" 1 
ATOM   6529  N  N1    . DC  E 2 11  ? 9.892   -63.413 31.471  1 50.47 ? 11  DC  V N1    1 
ATOM   6530  C  C2    . DC  E 2 11  ? 9.43    -62.433 30.592  1 50.14 ? 11  DC  V C2    1 
ATOM   6531  O  O2    . DC  E 2 11  ? 8.262   -62.491 30.201  1 50.14 ? 11  DC  V O2    1 
ATOM   6532  N  N3    . DC  E 2 11  ? 10.261  -61.429 30.228  1 49.84 ? 11  DC  V N3    1 
ATOM   6533  C  C4    . DC  E 2 11  ? 11.507  -61.402 30.692  1 49.81 ? 11  DC  V C4    1 
ATOM   6534  N  N4    . DC  E 2 11  ? 12.293  -60.396 30.308  1 49.67 ? 11  DC  V N4    1 
ATOM   6535  C  C5    . DC  E 2 11  ? 12.006  -62.407 31.572  1 50.09 ? 11  DC  V C5    1 
ATOM   6536  C  C6    . DC  E 2 11  ? 11.17   -63.384 31.935  1 50.31 ? 11  DC  V C6    1 
ATOM   6537  P  P     . DT  E 2 12  ? 7.034   -68.286 31.045  1 53.92 ? 12  DT  V P     1 
ATOM   6538  O  OP1   . DT  E 2 12  ? 6.35    -69.249 31.931  1 54.01 ? 12  DT  V OP1   1 
ATOM   6539  O  OP2   . DT  E 2 12  ? 8.292   -68.67  30.362  1 53.75 ? 12  DT  V OP2   1 
ATOM   6540  O  "O5'" . DT  E 2 12  ? 5.992   -67.782 29.938  1 55.19 ? 12  DT  V "O5'" 1 
ATOM   6541  C  "C5'" . DT  E 2 12  ? 4.939   -66.875 30.314  1 56.4  ? 12  DT  V "C5'" 1 
ATOM   6542  C  "C4'" . DT  E 2 12  ? 4.591   -65.915 29.182  1 57.49 ? 12  DT  V "C4'" 1 
ATOM   6543  O  "O4'" . DT  E 2 12  ? 5.648   -64.929 29.025  1 57.69 ? 12  DT  V "O4'" 1 
ATOM   6544  C  "C3'" . DT  E 2 12  ? 4.4     -66.569 27.812  1 58.42 ? 12  DT  V "C3'" 1 
ATOM   6545  O  "O3'" . DT  E 2 12  ? 3.206   -66.096 27.194  1 59.52 ? 12  DT  V "O3'" 1 
ATOM   6546  C  "C2'" . DT  E 2 12  ? 5.643   -66.149 27.033  1 58.23 ? 12  DT  V "C2'" 1 
ATOM   6547  C  "C1'" . DT  E 2 12  ? 5.977   -64.807 27.662  1 58.03 ? 12  DT  V "C1'" 1 
ATOM   6548  N  N1    . DT  E 2 12  ? 7.426   -64.447 27.543  1 58.16 ? 12  DT  V N1    1 
ATOM   6549  C  C2    . DT  E 2 12  ? 7.774   -63.246 26.963  1 58.25 ? 12  DT  V C2    1 
ATOM   6550  O  O2    . DT  E 2 12  ? 6.957   -62.4   26.636  1 58.24 ? 12  DT  V O2    1 
ATOM   6551  N  N3    . DT  E 2 12  ? 9.127   -63.026 26.874  1 58.25 ? 12  DT  V N3    1 
ATOM   6552  C  C4    . DT  E 2 12  ? 10.144  -63.894 27.239  1 58.12 ? 12  DT  V C4    1 
ATOM   6553  O  O4    . DT  E 2 12  ? 11.315  -63.557 27.085  1 58.05 ? 12  DT  V O4    1 
ATOM   6554  C  C5    . DT  E 2 12  ? 9.709   -65.159 27.782  1 58.02 ? 12  DT  V C5    1 
ATOM   6555  C  C7    . DT  E 2 12  ? 10.72   -66.184 28.199  1 57.93 ? 12  DT  V C7    1 
ATOM   6556  C  C6    . DT  E 2 12  ? 8.388   -65.379 27.891  1 58.08 ? 12  DT  V C6    1 
ATOM   6557  P  P     . DC  E 2 13  ? 2.521   -66.943 26.012  1 60.65 ? 13  DC  V P     1 
ATOM   6558  O  OP1   . DC  E 2 13  ? 1.058   -66.971 26.274  1 60.69 ? 13  DC  V OP1   1 
ATOM   6559  O  OP2   . DC  E 2 13  ? 3.267   -68.223 25.863  1 60.73 ? 13  DC  V OP2   1 
ATOM   6560  O  "O5'" . DC  E 2 13  ? 2.819   -66.049 24.701  1 61.3  ? 13  DC  V "O5'" 1 
ATOM   6561  C  "C5'" . DC  E 2 13  ? 1.951   -64.956 24.353  1 61.86 ? 13  DC  V "C5'" 1 
ATOM   6562  C  "C4'" . DC  E 2 13  ? 2.613   -64.006 23.369  1 62.35 ? 13  DC  V "C4'" 1 
ATOM   6563  O  "O4'" . DC  E 2 13  ? 3.851   -63.52  23.921  1 62.57 ? 13  DC  V "O4'" 1 
ATOM   6564  C  "C3'" . DC  E 2 13  ? 3.011   -64.625 22.048  1 62.7  ? 13  DC  V "C3'" 1 
ATOM   6565  O  "O3'" . DC  E 2 13  ? 1.9     -64.628 21.155  1 62.86 ? 13  DC  V "O3'" 1 
ATOM   6566  C  "C2'" . DC  E 2 13  ? 4.118   -63.684 21.563  1 62.85 ? 13  DC  V "C2'" 1 
ATOM   6567  C  "C1'" . DC  E 2 13  ? 4.71    -63.136 22.869  1 62.97 ? 13  DC  V "C1'" 1 
ATOM   6568  N  N1    . DC  E 2 13  ? 6.087   -63.635 23.163  1 63.49 ? 13  DC  V N1    1 
ATOM   6569  C  C2    . DC  E 2 13  ? 7.192   -62.841 22.839  1 63.9  ? 13  DC  V C2    1 
ATOM   6570  O  O2    . DC  E 2 13  ? 7.006   -61.726 22.331  1 64.14 ? 13  DC  V O2    1 
ATOM   6571  N  N3    . DC  E 2 13  ? 8.438   -63.307 23.104  1 63.94 ? 13  DC  V N3    1 
ATOM   6572  C  C4    . DC  E 2 13  ? 8.598   -64.507 23.661  1 63.89 ? 13  DC  V C4    1 
ATOM   6573  N  N4    . DC  E 2 13  ? 9.848   -64.92  23.903  1 63.91 ? 13  DC  V N4    1 
ATOM   6574  C  C5    . DC  E 2 13  ? 7.484   -65.339 23.985  1 63.78 ? 13  DC  V C5    1 
ATOM   6575  C  C6    . DC  E 2 13  ? 6.259   -64.869 23.718  1 63.64 ? 13  DC  V C6    1 
ATOM   6576  N  N     . MET F 1 1   ? -0.008  -10.309 51.543  1 26.6  ? 1   MET Z N     1 
ATOM   6577  C  CA    . MET F 1 1   ? 0.68    -11.592 51.441  1 26.95 ? 1   MET Z CA    1 
ATOM   6578  C  C     . MET F 1 1   ? -0.297  -12.738 51.187  1 27.18 ? 1   MET Z C     1 
ATOM   6579  O  O     . MET F 1 1   ? -1.427  -12.709 51.663  1 27.32 ? 1   MET Z O     1 
ATOM   6580  C  CB    . MET F 1 1   ? 1.499   -11.87  52.723  1 27.46 ? 1   MET Z CB    1 
ATOM   6581  C  CG    . MET F 1 1   ? 2.267   -13.184 52.692  1 29.02 ? 1   MET Z CG    1 
ATOM   6582  S  SD    . MET F 1 1   ? 3.354   -13.478 54.112  1 29.7  ? 1   MET Z SD    1 
ATOM   6583  C  CE    . MET F 1 1   ? 2.17    -13.555 55.402  1 26.17 ? 1   MET Z CE    1 
ATOM   6584  N  N     . ASN F 1 2   ? 0.139   -13.744 50.439  1 27.11 ? 2   ASN Z N     1 
ATOM   6585  C  CA    . ASN F 1 2   ? -0.648  -14.941 50.201  1 27.65 ? 2   ASN Z CA    1 
ATOM   6586  C  C     . ASN F 1 2   ? 0.128   -16.134 50.754  1 28.09 ? 2   ASN Z C     1 
ATOM   6587  O  O     . ASN F 1 2   ? 1.338   -16.229 50.549  1 28.41 ? 2   ASN Z O     1 
ATOM   6588  C  CB    . ASN F 1 2   ? -0.949  -15.117 48.72   1 28.47 ? 2   ASN Z CB    1 
ATOM   6589  C  CG    . ASN F 1 2   ? -2.175  -14.355 48.294  1 31.27 ? 2   ASN Z CG    1 
ATOM   6590  O  OD1   . ASN F 1 2   ? -3.088  -14.104 49.09   1 32.46 ? 2   ASN Z OD1   1 
ATOM   6591  N  ND2   . ASN F 1 2   ? -2.228  -13.976 47.031  1 31.76 ? 2   ASN Z ND2   1 
ATOM   6592  N  N     . VAL F 1 3   ? -0.551  -17.015 51.495  1 27.81 ? 3   VAL Z N     1 
ATOM   6593  C  CA    . VAL F 1 3   ? 0.106   -18.172 52.084  1 28.19 ? 3   VAL Z CA    1 
ATOM   6594  C  C     . VAL F 1 3   ? -0.403  -19.46  51.456  1 28.32 ? 3   VAL Z C     1 
ATOM   6595  O  O     . VAL F 1 3   ? -1.606  -19.665 51.32   1 28.28 ? 3   VAL Z O     1 
ATOM   6596  C  CB    . VAL F 1 3   ? -0.027  -18.197 53.629  1 29.06 ? 3   VAL Z CB    1 
ATOM   6597  C  CG1   . VAL F 1 3   ? 0.643   -19.428 54.219  1 29.63 ? 3   VAL Z CG1   1 
ATOM   6598  C  CG2   . VAL F 1 3   ? 0.555   -16.936 54.252  1 29.6  ? 3   VAL Z CG2   1 
ATOM   6599  N  N     . PHE F 1 4   ? 0.518   -20.317 51.062  1 28.39 ? 4   PHE Z N     1 
ATOM   6600  C  CA    . PHE F 1 4   ? 0.206   -21.609 50.476  1 29.04 ? 4   PHE Z CA    1 
ATOM   6601  C  C     . PHE F 1 4   ? 0.858   -22.69  51.304  1 29.39 ? 4   PHE Z C     1 
ATOM   6602  O  O     . PHE F 1 4   ? 1.891   -22.446 51.932  1 29.53 ? 4   PHE Z O     1 
ATOM   6603  C  CB    . PHE F 1 4   ? 0.75    -21.7   49.043  1 29.17 ? 4   PHE Z CB    1 
ATOM   6604  C  CG    . PHE F 1 4   ? 0.266   -20.595 48.145  1 29.98 ? 4   PHE Z CG    1 
ATOM   6605  C  CD1   . PHE F 1 4   ? -0.985  -20.654 47.564  1 30.87 ? 4   PHE Z CD1   1 
ATOM   6606  C  CD2   . PHE F 1 4   ? 1.055   -19.488 47.896  1 30.79 ? 4   PHE Z CD2   1 
ATOM   6607  C  CE1   . PHE F 1 4   ? -1.433  -19.631 46.74   1 31.61 ? 4   PHE Z CE1   1 
ATOM   6608  C  CE2   . PHE F 1 4   ? 0.602   -18.465 47.075  1 31.51 ? 4   PHE Z CE2   1 
ATOM   6609  C  CZ    . PHE F 1 4   ? -0.638  -18.542 46.502  1 31.35 ? 4   PHE Z CZ    1 
ATOM   6610  N  N     . ARG F 1 5   ? 0.284   -23.893 51.287  1 29.39 ? 5   ARG Z N     1 
ATOM   6611  C  CA    . ARG F 1 5   ? 0.873   -25.002 52.011  1 29.93 ? 5   ARG Z CA    1 
ATOM   6612  C  C     . ARG F 1 5   ? 1.225   -26.12  51.07   1 30.56 ? 5   ARG Z C     1 
ATOM   6613  O  O     . ARG F 1 5   ? 0.459   -26.435 50.163  1 30.93 ? 5   ARG Z O     1 
ATOM   6614  C  CB    . ARG F 1 5   ? -0.026  -25.481 53.148  1 31.2  ? 5   ARG Z CB    1 
ATOM   6615  C  CG    . ARG F 1 5   ? 0.021   -24.565 54.352  1 34.26 ? 5   ARG Z CG    1 
ATOM   6616  C  CD    . ARG F 1 5   ? -1.061  -24.905 55.348  1 37.62 ? 5   ARG Z CD    1 
ATOM   6617  N  NE    . ARG F 1 5   ? -0.919  -24.132 56.583  1 40.69 ? 5   ARG Z NE    1 
ATOM   6618  C  CZ    . ARG F 1 5   ? -1.499  -24.447 57.736  1 42.4  ? 5   ARG Z CZ    1 
ATOM   6619  N  NH1   . ARG F 1 5   ? -2.26   -25.531 57.83   1 41.83 ? 5   ARG Z NH1   1 
ATOM   6620  N  NH2   . ARG F 1 5   ? -1.308  -23.691 58.809  1 42.24 ? 5   ARG Z NH2   1 
ATOM   6621  N  N     . ILE F 1 6   ? 2.412   -26.692 51.252  1 30.54 ? 6   ILE Z N     1 
ATOM   6622  C  CA    . ILE F 1 6   ? 2.85    -27.808 50.435  1 30.99 ? 6   ILE Z CA    1 
ATOM   6623  C  C     . ILE F 1 6   ? 2.901   -29.016 51.335  1 31.42 ? 6   ILE Z C     1 
ATOM   6624  O  O     . ILE F 1 6   ? 3.806   -29.133 52.157  1 31.47 ? 6   ILE Z O     1 
ATOM   6625  C  CB    . ILE F 1 6   ? 4.226   -27.555 49.78   1 31.48 ? 6   ILE Z CB    1 
ATOM   6626  C  CG1   . ILE F 1 6   ? 4.251   -26.233 49.01   1 32.18 ? 6   ILE Z CG1   1 
ATOM   6627  C  CG2   . ILE F 1 6   ? 4.627   -28.73  48.889  1 32.06 ? 6   ILE Z CG2   1 
ATOM   6628  C  CD1   . ILE F 1 6   ? 3.277   -26.142 47.909  1 33.28 ? 6   ILE Z CD1   1 
ATOM   6629  N  N     . HIS F 1 7   ? 1.913   -29.889 51.216  1 31.63 ? 7   HIS Z N     1 
ATOM   6630  C  CA    . HIS F 1 7   ? 1.867   -31.104 52.014  1 32.31 ? 7   HIS Z CA    1 
ATOM   6631  C  C     . HIS F 1 7   ? 2.531   -32.181 51.158  1 32.78 ? 7   HIS Z C     1 
ATOM   6632  O  O     . HIS F 1 7   ? 2.11    -32.389 50.027  1 33.09 ? 7   HIS Z O     1 
ATOM   6633  C  CB    . HIS F 1 7   ? 0.404   -31.469 52.32   1 33.11 ? 7   HIS Z CB    1 
ATOM   6634  C  CG    . HIS F 1 7   ? -0.342  -30.411 53.08   1 35.36 ? 7   HIS Z CG    1 
ATOM   6635  N  ND1   . HIS F 1 7   ? -0.483  -30.474 54.457  1 37.13 ? 7   HIS Z ND1   1 
ATOM   6636  C  CD2   . HIS F 1 7   ? -0.987  -29.309 52.628  1 36.34 ? 7   HIS Z CD2   1 
ATOM   6637  C  CE1   . HIS F 1 7   ? -1.189  -29.407 54.796  1 37.46 ? 7   HIS Z CE1   1 
ATOM   6638  N  NE2   . HIS F 1 7   ? -1.518  -28.678 53.73   1 37.26 ? 7   HIS Z NE2   1 
ATOM   6639  N  N     . GLY F 1 8   ? 3.593   -32.803 51.657  1 32.5  ? 8   GLY Z N     1 
ATOM   6640  C  CA    . GLY F 1 8   ? 4.296   -33.83  50.896  1 32.61 ? 8   GLY Z CA    1 
ATOM   6641  C  C     . GLY F 1 8   ? 4.615   -35.079 51.691  1 32.72 ? 8   GLY Z C     1 
ATOM   6642  O  O     . GLY F 1 8   ? 4.35    -35.124 52.889  1 33.11 ? 8   GLY Z O     1 
ATOM   6643  N  N     . ASP F 1 9   ? 5.159   -36.12  51.034  1 32.3  ? 9   ASP Z N     1 
ATOM   6644  C  CA    . ASP F 1 9   ? 5.544   -37.359 51.727  1 32.26 ? 9   ASP Z CA    1 
ATOM   6645  C  C     . ASP F 1 9   ? 6.701   -37.072 52.689  1 31.57 ? 9   ASP Z C     1 
ATOM   6646  O  O     . ASP F 1 9   ? 6.725   -37.592 53.805  1 31.68 ? 9   ASP Z O     1 
ATOM   6647  C  CB    . ASP F 1 9   ? 6.022   -38.429 50.732  1 34.35 ? 9   ASP Z CB    1 
ATOM   6648  C  CG    . ASP F 1 9   ? 5.005   -38.906 49.735  1 39.7  ? 9   ASP Z CG    1 
ATOM   6649  O  OD1   . ASP F 1 9   ? 3.86    -39.178 50.145  1 40.54 ? 9   ASP Z OD1   1 
ATOM   6650  O  OD2   . ASP F 1 9   ? 5.364   -39.042 48.547  1 42.17 ? 9   ASP Z OD2   1 
ATOM   6651  N  N     . ASN F 1 10  ? 7.661   -36.247 52.245  1 30.6  ? 10  ASN Z N     1 
ATOM   6652  C  CA    . ASN F 1 10  ? 8.836   -35.84  53.01   1 30.25 ? 10  ASN Z CA    1 
ATOM   6653  C  C     . ASN F 1 10  ? 9.349   -34.461 52.541  1 29.73 ? 10  ASN Z C     1 
ATOM   6654  O  O     . ASN F 1 10  ? 8.769   -33.874 51.623  1 30.27 ? 10  ASN Z O     1 
ATOM   6655  C  CB    . ASN F 1 10  ? 9.925   -36.922 52.957  1 31.29 ? 10  ASN Z CB    1 
ATOM   6656  C  CG    . ASN F 1 10  ? 10.168  -37.506 51.597  1 34.53 ? 10  ASN Z CG    1 
ATOM   6657  O  OD1   . ASN F 1 10  ? 9.712   -38.606 51.268  1 35.66 ? 10  ASN Z OD1   1 
ATOM   6658  N  ND2   . ASN F 1 10  ? 10.896  -36.787 50.782  1 35.71 ? 10  ASN Z ND2   1 
ATOM   6659  N  N     . ILE F 1 11  ? 10.412  -33.927 53.169  1 28.56 ? 11  ILE Z N     1 
ATOM   6660  C  CA    . ILE F 1 11  ? 10.941  -32.616 52.79   1 27.9  ? 11  ILE Z CA    1 
ATOM   6661  C  C     . ILE F 1 11  ? 11.393  -32.538 51.322  1 27.24 ? 11  ILE Z C     1 
ATOM   6662  O  O     . ILE F 1 11  ? 11.217  -31.502 50.687  1 27.46 ? 11  ILE Z O     1 
ATOM   6663  C  CB    . ILE F 1 11  ? 12.055  -32.143 53.755  1 28.14 ? 11  ILE Z CB    1 
ATOM   6664  C  CG1   . ILE F 1 11  ? 12.375  -30.652 53.559  1 28.99 ? 11  ILE Z CG1   1 
ATOM   6665  C  CG2   . ILE F 1 11  ? 13.315  -33.006 53.648  1 28.42 ? 11  ILE Z CG2   1 
ATOM   6666  C  CD1   . ILE F 1 11  ? 11.167  -29.733 53.664  1 30.32 ? 11  ILE Z CD1   1 
ATOM   6667  N  N     . ILE F 1 12  ? 11.942  -33.629 50.781  1 26.31 ? 12  ILE Z N     1 
ATOM   6668  C  CA    . ILE F 1 12  ? 12.425  -33.661 49.413  1 25.92 ? 12  ILE Z CA    1 
ATOM   6669  C  C     . ILE F 1 12  ? 11.274  -33.44  48.432  1 26.13 ? 12  ILE Z C     1 
ATOM   6670  O  O     . ILE F 1 12  ? 11.417  -32.639 47.511  1 26.38 ? 12  ILE Z O     1 
ATOM   6671  C  CB    . ILE F 1 12  ? 13.253  -34.958 49.184  1 25.9  ? 12  ILE Z CB    1 
ATOM   6672  C  CG1   . ILE F 1 12  ? 14.732  -34.713 49.44   1 26.74 ? 12  ILE Z CG1   1 
ATOM   6673  C  CG2   . ILE F 1 12  ? 13.019  -35.635 47.835  1 26.35 ? 12  ILE Z CG2   1 
ATOM   6674  C  CD1   . ILE F 1 12  ? 15.407  -33.823 48.436  1 28.28 ? 12  ILE Z CD1   1 
ATOM   6675  N  N     . GLU F 1 13  ? 10.118  -34.081 48.665  1 25.88 ? 13  GLU Z N     1 
ATOM   6676  C  CA    . GLU F 1 13  ? 8.976   -33.926 47.765  1 26    ? 13  GLU Z CA    1 
ATOM   6677  C  C     . GLU F 1 13  ? 8.467   -32.491 47.794  1 25.66 ? 13  GLU Z C     1 
ATOM   6678  O  O     . GLU F 1 13  ? 8.17    -31.93  46.748  1 25.4  ? 13  GLU Z O     1 
ATOM   6679  C  CB    . GLU F 1 13  ? 7.839   -34.904 48.121  1 28.17 ? 13  GLU Z CB    1 
ATOM   6680  C  CG    . GLU F 1 13  ? 8.276   -36.327 48.439  1 33.08 ? 13  GLU Z CG    1 
ATOM   6681  C  CD    . GLU F 1 13  ? 8.639   -37.234 47.277  1 39.85 ? 13  GLU Z CD    1 
ATOM   6682  O  OE1   . GLU F 1 13  ? 8.012   -37.107 46.201  1 42.31 ? 13  GLU Z OE1   1 
ATOM   6683  O  OE2   . GLU F 1 13  ? 9.538   -38.089 47.449  1 41.27 ? 13  GLU Z OE2   1 
ATOM   6684  N  N     . CYS F 1 14  ? 8.394   -31.895 48.987  1 25.64 ? 14  CYS Z N     1 
ATOM   6685  C  CA    . CYS F 1 14  ? 7.942   -30.516 49.156  1 26.11 ? 14  CYS Z CA    1 
ATOM   6686  C  C     . CYS F 1 14  ? 8.868   -29.555 48.414  1 26.49 ? 14  CYS Z C     1 
ATOM   6687  O  O     . CYS F 1 14  ? 8.403   -28.683 47.678  1 26.68 ? 14  CYS Z O     1 
ATOM   6688  C  CB    . CYS F 1 14  ? 7.851   -30.157 50.638  1 26.68 ? 14  CYS Z CB    1 
ATOM   6689  S  SG    . CYS F 1 14  ? 6.776   -31.245 51.61   1 29.11 ? 14  CYS Z SG    1 
ATOM   6690  N  N     . GLU F 1 15  ? 10.181  -29.74  48.585  1 26.43 ? 15  GLU Z N     1 
ATOM   6691  C  CA    . GLU F 1 15  ? 11.18   -28.895 47.953  1 26.81 ? 15  GLU Z CA    1 
ATOM   6692  C  C     . GLU F 1 15  ? 11.177  -28.98  46.443  1 27.12 ? 15  GLU Z C     1 
ATOM   6693  O  O     . GLU F 1 15  ? 11.495  -27.99  45.79   1 27.47 ? 15  GLU Z O     1 
ATOM   6694  C  CB    . GLU F 1 15  ? 12.576  -29.171 48.517  1 29.09 ? 15  GLU Z CB    1 
ATOM   6695  C  CG    . GLU F 1 15  ? 12.755  -28.645 49.926  1 34.64 ? 15  GLU Z CG    1 
ATOM   6696  C  CD    . GLU F 1 15  ? 12.728  -27.134 50.049  1 42.79 ? 15  GLU Z CD    1 
ATOM   6697  O  OE1   . GLU F 1 15  ? 12.892  -26.44  49.017  1 44.73 ? 15  GLU Z OE1   1 
ATOM   6698  O  OE2   . GLU F 1 15  ? 12.562  -26.642 51.189  1 45.1  ? 15  GLU Z OE2   1 
ATOM   6699  N  N     . ARG F 1 16  ? 10.784  -30.129 45.878  1 26.85 ? 16  ARG Z N     1 
ATOM   6700  C  CA    . ARG F 1 16  ? 10.722  -30.272 44.428  1 26.9  ? 16  ARG Z CA    1 
ATOM   6701  C  C     . ARG F 1 16  ? 9.706   -29.308 43.813  1 26.63 ? 16  ARG Z C     1 
ATOM   6702  O  O     . ARG F 1 16  ? 9.959   -28.762 42.743  1 26.97 ? 16  ARG Z O     1 
ATOM   6703  C  CB    . ARG F 1 16  ? 10.475  -31.729 44.018  1 28.54 ? 16  ARG Z CB    1 
ATOM   6704  C  CG    . ARG F 1 16  ? 11.697  -32.604 44.269  1 32.66 ? 16  ARG Z CG    1 
ATOM   6705  C  CD    . ARG F 1 16  ? 11.883  -33.663 43.2    1 37.34 ? 16  ARG Z CD    1 
ATOM   6706  N  NE    . ARG F 1 16  ? 11.014  -34.823 43.396  1 41.42 ? 16  ARG Z NE    1 
ATOM   6707  C  CZ    . ARG F 1 16  ? 11.432  -36.013 43.824  1 44.08 ? 16  ARG Z CZ    1 
ATOM   6708  N  NH1   . ARG F 1 16  ? 12.719  -36.221 44.084  1 43.99 ? 16  ARG Z NH1   1 
ATOM   6709  N  NH2   . ARG F 1 16  ? 10.567  -37.004 43.99   1 44.03 ? 16  ARG Z NH2   1 
ATOM   6710  N  N     . VAL F 1 17  ? 8.603   -29.037 44.513  1 26.05 ? 17  VAL Z N     1 
ATOM   6711  C  CA    . VAL F 1 17  ? 7.608   -28.083 44.038  1 26.26 ? 17  VAL Z CA    1 
ATOM   6712  C  C     . VAL F 1 17  ? 8.179   -26.659 44.071  1 26.73 ? 17  VAL Z C     1 
ATOM   6713  O  O     . VAL F 1 17  ? 7.996   -25.89  43.127  1 26.67 ? 17  VAL Z O     1 
ATOM   6714  C  CB    . VAL F 1 17  ? 6.297   -28.229 44.832  1 26.63 ? 17  VAL Z CB    1 
ATOM   6715  C  CG1   . VAL F 1 17  ? 5.374   -27.026 44.641  1 27.08 ? 17  VAL Z CG1   1 
ATOM   6716  C  CG2   . VAL F 1 17  ? 5.595   -29.513 44.431  1 26.97 ? 17  VAL Z CG2   1 
ATOM   6717  N  N     . ILE F 1 18  ? 8.92    -26.331 45.13   1 26.91 ? 18  ILE Z N     1 
ATOM   6718  C  CA    . ILE F 1 18  ? 9.566   -25.03  45.263  1 27.35 ? 18  ILE Z CA    1 
ATOM   6719  C  C     . ILE F 1 18  ? 10.575  -24.82  44.136  1 27.5  ? 18  ILE Z C     1 
ATOM   6720  O  O     . ILE F 1 18  ? 10.593  -23.755 43.537  1 27.3  ? 18  ILE Z O     1 
ATOM   6721  C  CB    . ILE F 1 18  ? 10.217  -24.894 46.666  1 27.89 ? 18  ILE Z CB    1 
ATOM   6722  C  CG1   . ILE F 1 18  ? 9.173   -25.081 47.772  1 28.89 ? 18  ILE Z CG1   1 
ATOM   6723  C  CG2   . ILE F 1 18  ? 10.944  -23.566 46.826  1 28.36 ? 18  ILE Z CG2   1 
ATOM   6724  C  CD1   . ILE F 1 18  ? 8.015   -24.086 47.721  1 30.01 ? 18  ILE Z CD1   1 
ATOM   6725  N  N     . ASP F 1 19  ? 11.357  -25.856 43.804  1 27.89 ? 19  ASP Z N     1 
ATOM   6726  C  CA    . ASP F 1 19  ? 12.356  -25.784 42.733  1 28.81 ? 19  ASP Z CA    1 
ATOM   6727  C  C     . ASP F 1 19  ? 11.731  -25.518 41.349  1 29    ? 19  ASP Z C     1 
ATOM   6728  O  O     . ASP F 1 19  ? 12.324  -24.803 40.539  1 29.04 ? 19  ASP Z O     1 
ATOM   6729  C  CB    . ASP F 1 19  ? 13.255  -27.038 42.73   1 30.88 ? 19  ASP Z CB    1 
ATOM   6730  C  CG    . ASP F 1 19  ? 14.08   -27.215 43.999  1 35.84 ? 19  ASP Z CG    1 
ATOM   6731  O  OD1   . ASP F 1 19  ? 14.196  -26.245 44.774  1 36.92 ? 19  ASP Z OD1   1 
ATOM   6732  O  OD2   . ASP F 1 19  ? 14.601  -28.328 44.218  1 38.12 ? 19  ASP Z OD2   1 
ATOM   6733  N  N     . LEU F 1 20  ? 10.523  -26.053 41.101  1 28.86 ? 20  LEU Z N     1 
ATOM   6734  C  CA    . LEU F 1 20  ? 9.787   -25.803 39.866  1 29.22 ? 20  LEU Z CA    1 
ATOM   6735  C  C     . LEU F 1 20  ? 9.386   -24.319 39.814  1 29.51 ? 20  LEU Z C     1 
ATOM   6736  O  O     . LEU F 1 20  ? 9.597   -23.667 38.794  1 29.93 ? 20  LEU Z O     1 
ATOM   6737  C  CB    . LEU F 1 20  ? 8.523   -26.667 39.822  1 29.73 ? 20  LEU Z CB    1 
ATOM   6738  C  CG    . LEU F 1 20  ? 8.726   -28.112 39.446  1 31.93 ? 20  LEU Z CG    1 
ATOM   6739  C  CD1   . LEU F 1 20  ? 7.454   -28.915 39.669  1 32.41 ? 20  LEU Z CD1   1 
ATOM   6740  C  CD2   . LEU F 1 20  ? 9.201   -28.225 38.01   1 32.97 ? 20  LEU Z CD2   1 
ATOM   6741  N  N     . ILE F 1 21  ? 8.831   -23.781 40.921  1 29.02 ? 21  ILE Z N     1 
ATOM   6742  C  CA    . ILE F 1 21  ? 8.409   -22.388 41.023  1 28.95 ? 21  ILE Z CA    1 
ATOM   6743  C  C     . ILE F 1 21  ? 9.606   -21.459 40.825  1 28.94 ? 21  ILE Z C     1 
ATOM   6744  O  O     . ILE F 1 21  ? 9.564   -20.58  39.971  1 28.87 ? 21  ILE Z O     1 
ATOM   6745  C  CB    . ILE F 1 21  ? 7.691   -22.15  42.385  1 29.43 ? 21  ILE Z CB    1 
ATOM   6746  C  CG1   . ILE F 1 21  ? 6.33    -22.86  42.423  1 30.25 ? 21  ILE Z CG1   1 
ATOM   6747  C  CG2   . ILE F 1 21  ? 7.541   -20.661 42.7    1 29.89 ? 21  ILE Z CG2   1 
ATOM   6748  C  CD1   . ILE F 1 21  ? 5.744   -22.958 43.776  1 31.37 ? 21  ILE Z CD1   1 
ATOM   6749  N  N     . LEU F 1 22  ? 10.689  -21.705 41.567  1 29.03 ? 22  LEU Z N     1 
ATOM   6750  C  CA    . LEU F 1 22  ? 11.931  -20.94  41.54   1 29.96 ? 22  LEU Z CA    1 
ATOM   6751  C  C     . LEU F 1 22  ? 12.624  -20.955 40.178  1 31.36 ? 22  LEU Z C     1 
ATOM   6752  O  O     . LEU F 1 22  ? 13.409  -20.053 39.889  1 31.42 ? 22  LEU Z O     1 
ATOM   6753  C  CB    . LEU F 1 22  ? 12.884  -21.485 42.612  1 29.97 ? 22  LEU Z CB    1 
ATOM   6754  C  CG    . LEU F 1 22  ? 12.936  -20.77  43.961  1 31.16 ? 22  LEU Z CG    1 
ATOM   6755  C  CD1   . LEU F 1 22  ? 13.708  -19.478 43.863  1 31.74 ? 22  LEU Z CD1   1 
ATOM   6756  C  CD2   . LEU F 1 22  ? 11.553  -20.56  44.56   1 31.67 ? 22  LEU Z CD2   1 
ATOM   6757  N  N     . SER F 1 23  ? 12.352  -21.97  39.344  1 32.27 ? 23  SER Z N     1 
ATOM   6758  C  CA    . SER F 1 23  ? 12.943  -22.048 38.01   1 33.55 ? 23  SER Z CA    1 
ATOM   6759  C  C     . SER F 1 23  ? 12.383  -20.975 37.067  1 34.58 ? 23  SER Z C     1 
ATOM   6760  O  O     . SER F 1 23  ? 13.055  -20.596 36.114  1 35    ? 23  SER Z O     1 
ATOM   6761  C  CB    . SER F 1 23  ? 12.742  -23.437 37.404  1 35.12 ? 23  SER Z CB    1 
ATOM   6762  O  OG    . SER F 1 23  ? 11.424  -23.637 36.916  1 37.53 ? 23  SER Z OG    1 
ATOM   6763  N  N     . LYS F 1 24  ? 11.154  -20.507 37.31   1 34.98 ? 24  LYS Z N     1 
ATOM   6764  C  CA    . LYS F 1 24  ? 10.537  -19.49  36.471  1 36.1  ? 24  LYS Z CA    1 
ATOM   6765  C  C     . LYS F 1 24  ? 10.458  -18.136 37.209  1 37.26 ? 24  LYS Z C     1 
ATOM   6766  O  O     . LYS F 1 24  ? 10.621  -17.082 36.595  1 37.41 ? 24  LYS Z O     1 
ATOM   6767  C  CB    . LYS F 1 24  ? 9.162   -19.968 35.982  1 37.7  ? 24  LYS Z CB    1 
ATOM   6768  C  CG    . LYS F 1 24  ? 9.004   -19.92  34.467  1 41.48 ? 24  LYS Z CG    1 
ATOM   6769  C  CD    . LYS F 1 24  ? 8.899   -18.48  33.968  1 46.04 ? 24  LYS Z CD    1 
ATOM   6770  C  CE    . LYS F 1 24  ? 8.571   -18.38  32.498  1 49.92 ? 24  LYS Z CE    1 
ATOM   6771  N  NZ    . LYS F 1 24  ? 8.11    -17.015 32.132  1 51.99 ? 24  LYS Z NZ    1 
ATOM   6772  N  N     . ILE F 1 25  ? 10.236  -18.169 38.522  1 38    ? 25  ILE Z N     1 
ATOM   6773  C  CA    . ILE F 1 25  ? 10.19   -16.959 39.329  1 39.32 ? 25  ILE Z CA    1 
ATOM   6774  C  C     . ILE F 1 25  ? 11.616  -16.582 39.671  1 39.97 ? 25  ILE Z C     1 
ATOM   6775  O  O     . ILE F 1 25  ? 12.364  -17.422 40.165  1 40.12 ? 25  ILE Z O     1 
ATOM   6776  C  CB    . ILE F 1 25  ? 9.406   -17.225 40.64   1 40.55 ? 25  ILE Z CB    1 
ATOM   6777  C  CG1   . ILE F 1 25  ? 7.935   -17.563 40.377  1 41.96 ? 25  ILE Z CG1   1 
ATOM   6778  C  CG2   . ILE F 1 25  ? 9.554   -16.076 41.645  1 41.16 ? 25  ILE Z CG2   1 
ATOM   6779  C  CD1   . ILE F 1 25  ? 7.115   -16.435 39.803  1 43.48 ? 25  ILE Z CD1   1 
ATOM   6780  N  N     . ASN F 1 26  ? 11.994  -15.328 39.44   1 40.27 ? 26  ASN Z N     1 
ATOM   6781  C  CA    . ASN F 1 26  ? 13.316  -14.842 39.815  1 40.97 ? 26  ASN Z CA    1 
ATOM   6782  C  C     . ASN F 1 26  ? 13.036  -13.907 40.976  1 40.58 ? 26  ASN Z C     1 
ATOM   6783  O  O     . ASN F 1 26  ? 12.653  -12.759 40.756  1 40.66 ? 26  ASN Z O     1 
ATOM   6784  C  CB    . ASN F 1 26  ? 13.964  -14.087 38.648  1 43.04 ? 26  ASN Z CB    1 
ATOM   6785  C  CG    . ASN F 1 26  ? 15.472  -14.115 38.67   1 47.23 ? 26  ASN Z CG    1 
ATOM   6786  O  OD1   . ASN F 1 26  ? 16.102  -14.181 39.74   1 48.95 ? 26  ASN Z OD1   1 
ATOM   6787  N  ND2   . ASN F 1 26  ? 16.083  -14.056 37.486  1 47.7  ? 26  ASN Z ND2   1 
ATOM   6788  N  N     . PRO F 1 27  ? 13.101  -14.407 42.221  1 40.03 ? 27  PRO Z N     1 
ATOM   6789  C  CA    . PRO F 1 27  ? 12.729  -13.562 43.363  1 39.73 ? 27  PRO Z CA    1 
ATOM   6790  C  C     . PRO F 1 27  ? 13.739  -12.496 43.752  1 39.33 ? 27  PRO Z C     1 
ATOM   6791  O  O     . PRO F 1 27  ? 14.946  -12.694 43.651  1 39.51 ? 27  PRO Z O     1 
ATOM   6792  C  CB    . PRO F 1 27  ? 12.497  -14.564 44.498  1 40.51 ? 27  PRO Z CB    1 
ATOM   6793  C  CG    . PRO F 1 27  ? 12.669  -15.931 43.897  1 41.07 ? 27  PRO Z CG    1 
ATOM   6794  C  CD    . PRO F 1 27  ? 13.476  -15.762 42.656  1 39.54 ? 27  PRO Z CD    1 
ATOM   6795  N  N     . GLN F 1 28  ? 13.224  -11.364 44.211  1 38.66 ? 28  GLN Z N     1 
ATOM   6796  C  CA    . GLN F 1 28  ? 14.029  -10.242 44.644  1 38.64 ? 28  GLN Z CA    1 
ATOM   6797  C  C     . GLN F 1 28  ? 14.579  -10.545 46.034  1 38.3  ? 28  GLN Z C     1 
ATOM   6798  O  O     . GLN F 1 28  ? 15.769  -10.367 46.275  1 38.31 ? 28  GLN Z O     1 
ATOM   6799  C  CB    . GLN F 1 28  ? 13.17   -8.962  44.665  1 40.39 ? 28  GLN Z CB    1 
ATOM   6800  C  CG    . GLN F 1 28  ? 12.38   -8.724  43.38   1 44    ? 28  GLN Z CG    1 
ATOM   6801  C  CD    . GLN F 1 28  ? 13.305  -8.455  42.227  1 48.6  ? 28  GLN Z CD    1 
ATOM   6802  O  OE1   . GLN F 1 28  ? 13.993  -7.426  42.184  1 50.17 ? 28  GLN Z OE1   1 
ATOM   6803  N  NE2   . GLN F 1 28  ? 13.354  -9.383  41.277  1 48.99 ? 28  GLN Z NE2   1 
ATOM   6804  N  N     . LYS F 1 29  ? 13.714  -11.021 46.947  1 37.91 ? 29  LYS Z N     1 
ATOM   6805  C  CA    . LYS F 1 29  ? 14.09   -11.338 48.324  1 38.05 ? 29  LYS Z CA    1 
ATOM   6806  C  C     . LYS F 1 29  ? 13.597  -12.731 48.701  1 37.99 ? 29  LYS Z C     1 
ATOM   6807  O  O     . LYS F 1 29  ? 12.432  -13.046 48.478  1 38.11 ? 29  LYS Z O     1 
ATOM   6808  C  CB    . LYS F 1 29  ? 13.486  -10.302 49.292  1 39.73 ? 29  LYS Z CB    1 
ATOM   6809  C  CG    . LYS F 1 29  ? 14.061  -8.904  49.128  1 43.65 ? 29  LYS Z CG    1 
ATOM   6810  C  CD    . LYS F 1 29  ? 13.117  -7.807  49.613  1 48    ? 29  LYS Z CD    1 
ATOM   6811  C  CE    . LYS F 1 29  ? 13.2    -7.55   51.094  1 51.89 ? 29  LYS Z CE    1 
ATOM   6812  N  NZ    . LYS F 1 29  ? 12.269  -6.465  51.509  1 54.33 ? 29  LYS Z NZ    1 
ATOM   6813  N  N     . VAL F 1 30  ? 14.477  -13.571 49.257  1 37.63 ? 30  VAL Z N     1 
ATOM   6814  C  CA    . VAL F 1 30  ? 14.097  -14.916 49.679  1 37.76 ? 30  VAL Z CA    1 
ATOM   6815  C  C     . VAL F 1 30  ? 14.502  -15.128 51.132  1 37.89 ? 30  VAL Z C     1 
ATOM   6816  O  O     . VAL F 1 30  ? 15.644  -14.866 51.507  1 38.07 ? 30  VAL Z O     1 
ATOM   6817  C  CB    . VAL F 1 30  ? 14.678  -16.03  48.77   1 38.37 ? 30  VAL Z CB    1 
ATOM   6818  C  CG1   . VAL F 1 30  ? 14.398  -17.418 49.34   1 38.88 ? 30  VAL Z CG1   1 
ATOM   6819  C  CG2   . VAL F 1 30  ? 14.13   -15.926 47.359  1 38.85 ? 30  VAL Z CG2   1 
ATOM   6820  N  N     . LYS F 1 31  ? 13.56   -15.585 51.952  1 37.62 ? 31  LYS Z N     1 
ATOM   6821  C  CA    . LYS F 1 31  ? 13.825  -15.887 53.345  1 37.82 ? 31  LYS Z CA    1 
ATOM   6822  C  C     . LYS F 1 31  ? 13.361  -17.312 53.604  1 38.01 ? 31  LYS Z C     1 
ATOM   6823  O  O     . LYS F 1 31  ? 12.316  -17.719 53.108  1 38.19 ? 31  LYS Z O     1 
ATOM   6824  C  CB    . LYS F 1 31  ? 13.079  -14.907 54.268  1 39.43 ? 31  LYS Z CB    1 
ATOM   6825  C  CG    . LYS F 1 31  ? 13.285  -15.196 55.753  1 43.2  ? 31  LYS Z CG    1 
ATOM   6826  C  CD    . LYS F 1 31  ? 12.458  -14.278 56.655  1 47.34 ? 31  LYS Z CD    1 
ATOM   6827  C  CE    . LYS F 1 31  ? 13.237  -13.07  57.13   1 50.84 ? 31  LYS Z CE    1 
ATOM   6828  N  NZ    . LYS F 1 31  ? 12.425  -12.173 58.002  1 52.64 ? 31  LYS Z NZ    1 
ATOM   6829  N  N     . ARG F 1 32  ? 14.144  -18.082 54.35   1 37.77 ? 32  ARG Z N     1 
ATOM   6830  C  CA    . ARG F 1 32  ? 13.768  -19.441 54.709  1 37.95 ? 32  ARG Z CA    1 
ATOM   6831  C  C     . ARG F 1 32  ? 13.833  -19.606 56.233  1 37.83 ? 32  ARG Z C     1 
ATOM   6832  O  O     . ARG F 1 32  ? 14.486  -18.823 56.926  1 37.91 ? 32  ARG Z O     1 
ATOM   6833  C  CB    . ARG F 1 32  ? 14.68   -20.457 54.014  1 39.24 ? 32  ARG Z CB    1 
ATOM   6834  C  CG    . ARG F 1 32  ? 14.346  -20.774 52.571  1 42.09 ? 32  ARG Z CG    1 
ATOM   6835  C  CD    . ARG F 1 32  ? 15.355  -21.797 52.072  1 45.12 ? 32  ARG Z CD    1 
ATOM   6836  N  NE    . ARG F 1 32  ? 15.105  -22.218 50.697  1 47.89 ? 32  ARG Z NE    1 
ATOM   6837  C  CZ    . ARG F 1 32  ? 14.299  -23.216 50.355  1 50.19 ? 32  ARG Z CZ    1 
ATOM   6838  N  NH1   . ARG F 1 32  ? 13.63   -23.888 51.284  1 50.02 ? 32  ARG Z NH1   1 
ATOM   6839  N  NH2   . ARG F 1 32  ? 14.14   -23.539 49.081  1 50.28 ? 32  ARG Z NH2   1 
ATOM   6840  N  N     . GLY F 1 33  ? 13.149  -20.617 56.742  1 37.46 ? 33  GLY Z N     1 
ATOM   6841  C  CA    . GLY F 1 33  ? 13.139  -20.89  58.168  1 37.68 ? 33  GLY Z CA    1 
ATOM   6842  C  C     . GLY F 1 33  ? 12.106  -21.926 58.534  1 37.68 ? 33  GLY Z C     1 
ATOM   6843  O  O     . GLY F 1 33  ? 11.79   -22.79  57.724  1 37.95 ? 33  GLY Z O     1 
ATOM   6844  N  N     . PHE F 1 34  ? 11.555  -21.84  59.742  1 37.27 ? 34  PHE Z N     1 
ATOM   6845  C  CA    . PHE F 1 34  ? 10.539  -22.774 60.205  1 37.37 ? 34  PHE Z CA    1 
ATOM   6846  C  C     . PHE F 1 34  ? 9.368   -22.009 60.832  1 37.28 ? 34  PHE Z C     1 
ATOM   6847  O  O     . PHE F 1 34  ? 9.593   -21.06  61.583  1 37.27 ? 34  PHE Z O     1 
ATOM   6848  C  CB    . PHE F 1 34  ? 11.138  -23.69  61.285  1 37.38 ? 34  PHE Z CB    1 
ATOM   6849  C  CG    . PHE F 1 34  ? 11.96   -24.873 60.825  1 38.2  ? 34  PHE Z CG    1 
ATOM   6850  C  CD1   . PHE F 1 34  ? 11.349  -26.053 60.437  1 39.11 ? 34  PHE Z CD1   1 
ATOM   6851  C  CD2   . PHE F 1 34  ? 13.342  -24.84  60.876  1 39.02 ? 34  PHE Z CD2   1 
ATOM   6852  C  CE1   . PHE F 1 34  ? 12.104  -27.154 60.051  1 39.82 ? 34  PHE Z CE1   1 
ATOM   6853  C  CE2   . PHE F 1 34  ? 14.094  -25.943 60.489  1 39.77 ? 34  PHE Z CE2   1 
ATOM   6854  C  CZ    . PHE F 1 34  ? 13.472  -27.091 60.075  1 39.6  ? 34  PHE Z CZ    1 
ATOM   6855  N  N     . ILE F 1 35  ? 8.123   -22.419 60.542  1 36.96 ? 35  ILE Z N     1 
ATOM   6856  C  CA    . ILE F 1 35  ? 6.944   -21.832 61.209  1 37.03 ? 35  ILE Z CA    1 
ATOM   6857  C  C     . ILE F 1 35  ? 6.612   -22.61  62.524  1 36.97 ? 35  ILE Z C     1 
ATOM   6858  O  O     . ILE F 1 35  ? 5.958   -22.088 63.427  1 37.25 ? 35  ILE Z O     1 
ATOM   6859  C  CB    . ILE F 1 35  ? 5.704   -21.713 60.287  1 37.43 ? 35  ILE Z CB    1 
ATOM   6860  C  CG1   . ILE F 1 35  ? 5.199   -23.085 59.833  1 38.12 ? 35  ILE Z CG1   1 
ATOM   6861  C  CG2   . ILE F 1 35  ? 5.956   -20.781 59.112  1 37.94 ? 35  ILE Z CG2   1 
ATOM   6862  C  CD1   . ILE F 1 35  ? 3.739   -23.098 59.523  1 39.24 ? 35  ILE Z CD1   1 
ATOM   6863  N  N     . SER F 1 36  ? 7.066   -23.859 62.603  1 36.39 ? 36  SER Z N     1 
ATOM   6864  C  CA    . SER F 1 36  ? 6.958   -24.777 63.72   1 36.33 ? 36  SER Z CA    1 
ATOM   6865  C  C     . SER F 1 36  ? 8.157   -25.738 63.608  1 36.02 ? 36  SER Z C     1 
ATOM   6866  O  O     . SER F 1 36  ? 8.855   -25.729 62.594  1 36.1  ? 36  SER Z O     1 
ATOM   6867  C  CB    . SER F 1 36  ? 5.639   -25.544 63.65   1 37.64 ? 36  SER Z CB    1 
ATOM   6868  O  OG    . SER F 1 36  ? 5.657   -26.537 62.638  1 39.91 ? 36  SER Z OG    1 
ATOM   6869  N  N     . LEU F 1 37  ? 8.377   -26.584 64.61   1 35.63 ? 37  LEU Z N     1 
ATOM   6870  C  CA    . LEU F 1 37  ? 9.485   -27.53  64.578  1 35.93 ? 37  LEU Z CA    1 
ATOM   6871  C  C     . LEU F 1 37  ? 9.466   -28.469 63.351  1 35.86 ? 37  LEU Z C     1 
ATOM   6872  O  O     . LEU F 1 37  ? 10.522  -28.776 62.796  1 36.01 ? 37  LEU Z O     1 
ATOM   6873  C  CB    . LEU F 1 37  ? 9.523   -28.313 65.887  1 36.44 ? 37  LEU Z CB    1 
ATOM   6874  C  CG    . LEU F 1 37  ? 9.886   -27.457 67.087  1 38.27 ? 37  LEU Z CG    1 
ATOM   6875  C  CD1   . LEU F 1 37  ? 9.295   -28.013 68.361  1 38.86 ? 37  LEU Z CD1   1 
ATOM   6876  C  CD2   . LEU F 1 37  ? 11.377  -27.27  67.18   1 39.01 ? 37  LEU Z CD2   1 
ATOM   6877  N  N     . SER F 1 38  ? 8.273   -28.872 62.893  1 35.37 ? 38  SER Z N     1 
ATOM   6878  C  CA    . SER F 1 38  ? 8.139   -29.778 61.749  1 35.24 ? 38  SER Z CA    1 
ATOM   6879  C  C     . SER F 1 38  ? 8.008   -29.108 60.408  1 34.5  ? 38  SER Z C     1 
ATOM   6880  O  O     . SER F 1 38  ? 8.219   -29.759 59.392  1 34.46 ? 38  SER Z O     1 
ATOM   6881  C  CB    . SER F 1 38  ? 6.894   -30.637 61.917  1 36.88 ? 38  SER Z CB    1 
ATOM   6882  O  OG    . SER F 1 38  ? 7.165   -31.747 62.748  1 39.79 ? 38  SER Z OG    1 
ATOM   6883  N  N     . CYS F 1 39  ? 7.559   -27.859 60.39   1 33.87 ? 39  CYS Z N     1 
ATOM   6884  C  CA    . CYS F 1 39  ? 7.228   -27.189 59.15   1 33.7  ? 39  CYS Z CA    1 
ATOM   6885  C  C     . CYS F 1 39  ? 8.193   -26.119 58.707  1 32.82 ? 39  CYS Z C     1 
ATOM   6886  O  O     . CYS F 1 39  ? 8.097   -24.978 59.168  1 32.97 ? 39  CYS Z O     1 
ATOM   6887  C  CB    . CYS F 1 39  ? 5.811   -26.63  59.229  1 34.91 ? 39  CYS Z CB    1 
ATOM   6888  S  SG    . CYS F 1 39  ? 4.543   -27.872 59.592  1 40.03 ? 39  CYS Z SG    1 
ATOM   6889  N  N     . PRO F 1 40  ? 9.028   -26.42  57.694  1 31.49 ? 40  PRO Z N     1 
ATOM   6890  C  CA    . PRO F 1 40  ? 9.876   -25.365 57.128  1 30.54 ? 40  PRO Z CA    1 
ATOM   6891  C  C     . PRO F 1 40  ? 9.069   -24.438 56.218  1 29.59 ? 40  PRO Z C     1 
ATOM   6892  O  O     . PRO F 1 40  ? 7.962   -24.779 55.801  1 29.36 ? 40  PRO Z O     1 
ATOM   6893  C  CB    . PRO F 1 40  ? 10.934  -26.135 56.325  1 31.31 ? 40  PRO Z CB    1 
ATOM   6894  C  CG    . PRO F 1 40  ? 10.631  -27.583 56.514  1 31.92 ? 40  PRO Z CG    1 
ATOM   6895  C  CD    . PRO F 1 40  ? 9.227   -27.703 56.999  1 30.69 ? 40  PRO Z CD    1 
ATOM   6896  N  N     . PHE F 1 41  ? 9.62    -23.267 55.914  1 28.98 ? 41  PHE Z N     1 
ATOM   6897  C  CA    . PHE F 1 41  ? 8.955   -22.33  55.028  1 29    ? 41  PHE Z CA    1 
ATOM   6898  C  C     . PHE F 1 41  ? 9.926   -21.663 54.077  1 29.1  ? 41  PHE Z C     1 
ATOM   6899  O  O     . PHE F 1 41  ? 11.121  -21.565 54.354  1 29.28 ? 41  PHE Z O     1 
ATOM   6900  C  CB    . PHE F 1 41  ? 8.134   -21.276 55.812  1 28.88 ? 41  PHE Z CB    1 
ATOM   6901  C  CG    . PHE F 1 41  ? 8.929   -20.132 56.415  1 29.37 ? 41  PHE Z CG    1 
ATOM   6902  C  CD1   . PHE F 1 41  ? 9.307   -19.044 55.647  1 30.01 ? 41  PHE Z CD1   1 
ATOM   6903  C  CD2   . PHE F 1 41  ? 9.246   -20.119 57.758  1 29.84 ? 41  PHE Z CD2   1 
ATOM   6904  C  CE1   . PHE F 1 41  ? 10.058  -18.017 56.195  1 30.51 ? 41  PHE Z CE1   1 
ATOM   6905  C  CE2   . PHE F 1 41  ? 9.971   -19.073 58.308  1 30.36 ? 41  PHE Z CE2   1 
ATOM   6906  C  CZ    . PHE F 1 41  ? 10.375  -18.033 57.524  1 30.18 ? 41  PHE Z CZ    1 
ATOM   6907  N  N     . ILE F 1 42  ? 9.401   -21.186 52.957  1 28.89 ? 42  ILE Z N     1 
ATOM   6908  C  CA    . ILE F 1 42  ? 10.15   -20.367 52.034  1 29.24 ? 42  ILE Z CA    1 
ATOM   6909  C  C     . ILE F 1 42  ? 9.261   -19.162 51.735  1 29.45 ? 42  ILE Z C     1 
ATOM   6910  O  O     . ILE F 1 42  ? 8.111   -19.314 51.326  1 29.62 ? 42  ILE Z O     1 
ATOM   6911  C  CB    . ILE F 1 42  ? 10.701  -21.077 50.778  1 29.8  ? 42  ILE Z CB    1 
ATOM   6912  C  CG1   . ILE F 1 42  ? 11.444  -20.068 49.886  1 30.66 ? 42  ILE Z CG1   1 
ATOM   6913  C  CG2   . ILE F 1 42  ? 9.606   -21.798 50.012  1 30.36 ? 42  ILE Z CG2   1 
ATOM   6914  C  CD1   . ILE F 1 42  ? 12.21   -20.656 48.794  1 31.91 ? 42  ILE Z CD1   1 
ATOM   6915  N  N     . GLU F 1 43  ? 9.753   -17.976 52.057  1 29.19 ? 43  GLU Z N     1 
ATOM   6916  C  CA    . GLU F 1 43  ? 9.029   -16.741 51.858  1 29.48 ? 43  GLU Z CA    1 
ATOM   6917  C  C     . GLU F 1 43  ? 9.716   -16.025 50.728  1 29.9  ? 43  GLU Z C     1 
ATOM   6918  O  O     . GLU F 1 43  ? 10.926  -15.823 50.785  1 30.19 ? 43  GLU Z O     1 
ATOM   6919  C  CB    . GLU F 1 43  ? 9.091   -15.894 53.132  1 31.56 ? 43  GLU Z CB    1 
ATOM   6920  C  CG    . GLU F 1 43  ? 8.142   -14.712 53.129  1 35.86 ? 43  GLU Z CG    1 
ATOM   6921  C  CD    . GLU F 1 43  ? 7.974   -14.005 54.461  1 40.72 ? 43  GLU Z CD    1 
ATOM   6922  O  OE1   . GLU F 1 43  ? 8.47    -14.529 55.484  1 41.77 ? 43  GLU Z OE1   1 
ATOM   6923  O  OE2   . GLU F 1 43  ? 7.333   -12.929 54.482  1 42.02 ? 43  GLU Z OE2   1 
ATOM   6924  N  N     . ILE F 1 44  ? 8.973   -15.696 49.668  1 29.78 ? 44  ILE Z N     1 
ATOM   6925  C  CA    . ILE F 1 44  ? 9.548   -15.008 48.524  1 30.07 ? 44  ILE Z CA    1 
ATOM   6926  C  C     . ILE F 1 44  ? 8.832   -13.706 48.202  1 30.73 ? 44  ILE Z C     1 
ATOM   6927  O  O     . ILE F 1 44  ? 7.612   -13.598 48.332  1 30.88 ? 44  ILE Z O     1 
ATOM   6928  C  CB    . ILE F 1 44  ? 9.654   -15.912 47.275  1 30.26 ? 44  ILE Z CB    1 
ATOM   6929  C  CG1   . ILE F 1 44  ? 8.271   -16.295 46.731  1 31    ? 44  ILE Z CG1   1 
ATOM   6930  C  CG2   . ILE F 1 44  ? 10.518  -17.137 47.538  1 30.71 ? 44  ILE Z CG2   1 
ATOM   6931  C  CD1   . ILE F 1 44  ? 8.306   -16.859 45.362  1 32.19 ? 44  ILE Z CD1   1 
ATOM   6932  N  N     . ILE F 1 45  ? 9.61    -12.709 47.792  1 30.94 ? 45  ILE Z N     1 
ATOM   6933  C  CA    . ILE F 1 45  ? 9.108   -11.422 47.341  1 31.61 ? 45  ILE Z CA    1 
ATOM   6934  C  C     . ILE F 1 45  ? 9.577   -11.334 45.907  1 32    ? 45  ILE Z C     1 
ATOM   6935  O  O     . ILE F 1 45  ? 10.78   -11.348 45.668  1 32.16 ? 45  ILE Z O     1 
ATOM   6936  C  CB    . ILE F 1 45  ? 9.679   -10.252 48.169  1 32.34 ? 45  ILE Z CB    1 
ATOM   6937  C  CG1   . ILE F 1 45  ? 9.277   -10.374 49.643  1 33.49 ? 45  ILE Z CG1   1 
ATOM   6938  C  CG2   . ILE F 1 45  ? 9.223   -8.923  47.577  1 32.91 ? 45  ILE Z CG2   1 
ATOM   6939  C  CD1   . ILE F 1 45  ? 9.91    -9.369  50.548  1 35.02 ? 45  ILE Z CD1   1 
ATOM   6940  N  N     . PHE F 1 46  ? 8.655   -11.317 44.953  1 32.01 ? 46  PHE Z N     1 
ATOM   6941  C  CA    . PHE F 1 46  ? 9.016   -11.251 43.539  1 32.35 ? 46  PHE Z CA    1 
ATOM   6942  C  C     . PHE F 1 46  ? 8.163   -10.219 42.803  1 33.01 ? 46  PHE Z C     1 
ATOM   6943  O  O     . PHE F 1 46  ? 7.227   -9.674  43.383  1 32.96 ? 46  PHE Z O     1 
ATOM   6944  C  CB    . PHE F 1 46  ? 8.904   -12.646 42.893  1 31.95 ? 46  PHE Z CB    1 
ATOM   6945  C  CG    . PHE F 1 46  ? 7.496   -13.162 42.742  1 32.19 ? 46  PHE Z CG    1 
ATOM   6946  C  CD1   . PHE F 1 46  ? 6.869   -13.816 43.78   1 32.71 ? 46  PHE Z CD1   1 
ATOM   6947  C  CD2   . PHE F 1 46  ? 6.819   -13.036 41.543  1 32.9  ? 46  PHE Z CD2   1 
ATOM   6948  C  CE1   . PHE F 1 46  ? 5.58    -14.302 43.633  1 33.33 ? 46  PHE Z CE1   1 
ATOM   6949  C  CE2   . PHE F 1 46  ? 5.524   -13.511 41.405  1 33.47 ? 46  PHE Z CE2   1 
ATOM   6950  C  CZ    . PHE F 1 46  ? 4.918   -14.153 42.445  1 33.15 ? 46  PHE Z CZ    1 
ATOM   6951  N  N     . LYS F 1 47  ? 8.48    -9.945  41.534  1 33.73 ? 47  LYS Z N     1 
ATOM   6952  C  CA    . LYS F 1 47  ? 7.7     -8.988  40.762  1 35.09 ? 47  LYS Z CA    1 
ATOM   6953  C  C     . LYS F 1 47  ? 7.419   -9.44   39.343  1 35.89 ? 47  LYS Z C     1 
ATOM   6954  O  O     . LYS F 1 47  ? 8.148   -10.25  38.776  1 36.21 ? 47  LYS Z O     1 
ATOM   6955  C  CB    . LYS F 1 47  ? 8.366   -7.603  40.765  1 37.4  ? 47  LYS Z CB    1 
ATOM   6956  C  CG    . LYS F 1 47  ? 9.736   -7.602  40.105  1 41.78 ? 47  LYS Z CG    1 
ATOM   6957  C  CD    . LYS F 1 47  ? 10.374  -6.232  40.171  1 46.82 ? 47  LYS Z CD    1 
ATOM   6958  C  CE    . LYS F 1 47  ? 11.792  -6.25   39.662  1 50.61 ? 47  LYS Z CE    1 
ATOM   6959  N  NZ    . LYS F 1 47  ? 12.286  -4.873  39.461  1 52.71 ? 47  LYS Z NZ    1 
ATOM   6960  N  N     . GLU F 1 48  ? 6.336   -8.922  38.784  1 36.12 ? 48  GLU Z N     1 
ATOM   6961  C  CA    . GLU F 1 48  ? 5.952   -9.142  37.406  1 36.93 ? 48  GLU Z CA    1 
ATOM   6962  C  C     . GLU F 1 48  ? 5.899   -7.734  36.841  1 37.11 ? 48  GLU Z C     1 
ATOM   6963  O  O     . GLU F 1 48  ? 4.832   -7.117  36.79   1 37.39 ? 48  GLU Z O     1 
ATOM   6964  C  CB    . GLU F 1 48  ? 4.582   -9.81   37.335  1 39.47 ? 48  GLU Z CB    1 
ATOM   6965  C  CG    . GLU F 1 48  ? 4.591   -11.233 37.859  1 44.59 ? 48  GLU Z CG    1 
ATOM   6966  C  CD    . GLU F 1 48  ? 3.264   -11.956 37.748  1 51.32 ? 48  GLU Z CD    1 
ATOM   6967  O  OE1   . GLU F 1 48  ? 2.244   -11.284 37.468  1 53.1  ? 48  GLU Z OE1   1 
ATOM   6968  O  OE2   . GLU F 1 48  ? 3.239   -13.193 37.947  1 52.82 ? 48  GLU Z OE2   1 
ATOM   6969  N  N     . GLY F 1 49  ? 7.07    -7.201  36.524  1 36.69 ? 49  GLY Z N     1 
ATOM   6970  C  CA    . GLY F 1 49  ? 7.185   -5.829  36.064  1 36.76 ? 49  GLY Z CA    1 
ATOM   6971  C  C     . GLY F 1 49  ? 7.014   -4.867  37.224  1 36.53 ? 49  GLY Z C     1 
ATOM   6972  O  O     . GLY F 1 49  ? 7.842   -4.83   38.134  1 36.81 ? 49  GLY Z O     1 
ATOM   6973  N  N     . HIS F 1 50  ? 5.921   -4.101  37.216  1 35.95 ? 50  HIS Z N     1 
ATOM   6974  C  CA    . HIS F 1 50  ? 5.628   -3.161  38.301  1 35.9  ? 50  HIS Z CA    1 
ATOM   6975  C  C     . HIS F 1 50  ? 4.832   -3.809  39.447  1 35.78 ? 50  HIS Z C     1 
ATOM   6976  O  O     . HIS F 1 50  ? 4.672   -3.18   40.489  1 35.92 ? 50  HIS Z O     1 
ATOM   6977  C  CB    . HIS F 1 50  ? 4.826   -1.954  37.78   1 36.46 ? 50  HIS Z CB    1 
ATOM   6978  C  CG    . HIS F 1 50  ? 5.58    -1.004  36.893  1 38.37 ? 50  HIS Z CG    1 
ATOM   6979  N  ND1   . HIS F 1 50  ? 6.146   0.157   37.394  1 39.99 ? 50  HIS Z ND1   1 
ATOM   6980  C  CD2   . HIS F 1 50  ? 5.774   -1.037  35.552  1 39.25 ? 50  HIS Z CD2   1 
ATOM   6981  C  CE1   . HIS F 1 50  ? 6.686   0.771   36.354  1 40.32 ? 50  HIS Z CE1   1 
ATOM   6982  N  NE2   . HIS F 1 50  ? 6.488   0.093   35.226  1 40.21 ? 50  HIS Z NE2   1 
ATOM   6983  N  N     . ASP F 1 51  ? 4.299   -5.03   39.252  1 35.4  ? 51  ASP Z N     1 
ATOM   6984  C  CA    . ASP F 1 51  ? 3.475   -5.708  40.255  1 35.34 ? 51  ASP Z CA    1 
ATOM   6985  C  C     . ASP F 1 51  ? 4.254   -6.593  41.215  1 34.97 ? 51  ASP Z C     1 
ATOM   6986  O  O     . ASP F 1 51  ? 4.744   -7.637  40.806  1 34.78 ? 51  ASP Z O     1 
ATOM   6987  C  CB    . ASP F 1 51  ? 2.38    -6.534  39.566  1 36.69 ? 51  ASP Z CB    1 
ATOM   6988  C  CG    . ASP F 1 51  ? 1.012   -5.89   39.622  1 40.57 ? 51  ASP Z CG    1 
ATOM   6989  O  OD1   . ASP F 1 51  ? 0.56    -5.546  40.746  1 41.18 ? 51  ASP Z OD1   1 
ATOM   6990  O  OD2   . ASP F 1 51  ? 0.382   -5.741  38.548  1 42.13 ? 51  ASP Z OD2   1 
ATOM   6991  N  N     . TYR F 1 52  ? 4.324   -6.21   42.499  1 34.8  ? 52  TYR Z N     1 
ATOM   6992  C  CA    . TYR F 1 52  ? 5.013   -7.02   43.505  1 35.14 ? 52  TYR Z CA    1 
ATOM   6993  C  C     . TYR F 1 52  ? 4.075   -8.052  44.122  1 34.1  ? 52  TYR Z C     1 
ATOM   6994  O  O     . TYR F 1 52  ? 2.876   -7.814  44.254  1 33.87 ? 52  TYR Z O     1 
ATOM   6995  C  CB    . TYR F 1 52  ? 5.624   -6.15   44.618  1 36.05 ? 52  TYR Z CB    1 
ATOM   6996  C  CG    . TYR F 1 52  ? 6.974   -5.566  44.271  1 38.16 ? 52  TYR Z CG    1 
ATOM   6997  C  CD1   . TYR F 1 52  ? 8.144   -6.273  44.513  1 39.67 ? 52  TYR Z CD1   1 
ATOM   6998  C  CD2   . TYR F 1 52  ? 7.083   -4.295  43.723  1 39.8  ? 52  TYR Z CD2   1 
ATOM   6999  C  CE1   . TYR F 1 52  ? 9.389   -5.741  44.195  1 41.16 ? 52  TYR Z CE1   1 
ATOM   7000  C  CE2   . TYR F 1 52  ? 8.321   -3.752  43.401  1 41.24 ? 52  TYR Z CE2   1 
ATOM   7001  C  CZ    . TYR F 1 52  ? 9.473   -4.479  43.635  1 42.54 ? 52  TYR Z CZ    1 
ATOM   7002  O  OH    . TYR F 1 52  ? 10.699  -3.946  43.307  1 44.64 ? 52  TYR Z OH    1 
ATOM   7003  N  N     . PHE F 1 53  ? 4.633   -9.198  44.506  1 33.38 ? 53  PHE Z N     1 
ATOM   7004  C  CA    . PHE F 1 53  ? 3.893   -10.284 45.135  1 33.15 ? 53  PHE Z CA    1 
ATOM   7005  C  C     . PHE F 1 53  ? 4.685   -10.826 46.31   1 32.2  ? 53  PHE Z C     1 
ATOM   7006  O  O     . PHE F 1 53  ? 5.909   -10.933 46.249  1 32.08 ? 53  PHE Z O     1 
ATOM   7007  C  CB    . PHE F 1 53  ? 3.589   -11.411 44.139  1 33.44 ? 53  PHE Z CB    1 
ATOM   7008  C  CG    . PHE F 1 53  ? 2.711   -10.99  42.991  1 34.47 ? 53  PHE Z CG    1 
ATOM   7009  C  CD1   . PHE F 1 53  ? 1.337   -10.922 43.138  1 35.4  ? 53  PHE Z CD1   1 
ATOM   7010  C  CD2   . PHE F 1 53  ? 3.26    -10.619 41.78   1 35.48 ? 53  PHE Z CD2   1 
ATOM   7011  C  CE1   . PHE F 1 53  ? 0.532   -10.493 42.094  1 36.17 ? 53  PHE Z CE1   1 
ATOM   7012  C  CE2   . PHE F 1 53  ? 2.451   -10.206 40.732  1 36.35 ? 53  PHE Z CE2   1 
ATOM   7013  C  CZ    . PHE F 1 53  ? 1.091   -10.153 40.893  1 36.12 ? 53  PHE Z CZ    1 
ATOM   7014  N  N     . HIS F 1 54  ? 3.986   -11.158 47.386  1 31.42 ? 54  HIS Z N     1 
ATOM   7015  C  CA    . HIS F 1 54  ? 4.618   -11.664 48.591  1 31.27 ? 54  HIS Z CA    1 
ATOM   7016  C  C     . HIS F 1 54  ? 3.979   -12.996 48.916  1 30.99 ? 54  HIS Z C     1 
ATOM   7017  O  O     . HIS F 1 54  ? 2.83    -13.034 49.347  1 31.35 ? 54  HIS Z O     1 
ATOM   7018  C  CB    . HIS F 1 54  ? 4.385   -10.672 49.738  1 32.12 ? 54  HIS Z CB    1 
ATOM   7019  C  CG    . HIS F 1 54  ? 5.172   -10.942 50.981  1 34.37 ? 54  HIS Z CG    1 
ATOM   7020  N  ND1   . HIS F 1 54  ? 5.226   -10.016 52.001  1 36.02 ? 54  HIS Z ND1   1 
ATOM   7021  C  CD2   . HIS F 1 54  ? 5.913   -12.02  51.329  1 35.65 ? 54  HIS Z CD2   1 
ATOM   7022  C  CE1   . HIS F 1 54  ? 5.989   -10.556 52.935  1 36.7  ? 54  HIS Z CE1   1 
ATOM   7023  N  NE2   . HIS F 1 54  ? 6.42    -11.762 52.577  1 36.72 ? 54  HIS Z NE2   1 
ATOM   7024  N  N     . TRP F 1 55  ? 4.71    -14.089 48.702  1 30.11 ? 55  TRP Z N     1 
ATOM   7025  C  CA    . TRP F 1 55  ? 4.184   -15.42  48.951  1 29.62 ? 55  TRP Z CA    1 
ATOM   7026  C  C     . TRP F 1 55  ? 4.963   -16.13  50.028  1 29.81 ? 55  TRP Z C     1 
ATOM   7027  O  O     . TRP F 1 55  ? 6.169   -15.937 50.151  1 29.98 ? 55  TRP Z O     1 
ATOM   7028  C  CB    . TRP F 1 55  ? 4.285   -16.275 47.68   1 29.1  ? 55  TRP Z CB    1 
ATOM   7029  C  CG    . TRP F 1 55  ? 3.332   -15.948 46.57   1 29.06 ? 55  TRP Z CG    1 
ATOM   7030  C  CD1   . TRP F 1 55  ? 2.264   -15.099 46.613  1 29.84 ? 55  TRP Z CD1   1 
ATOM   7031  C  CD2   . TRP F 1 55  ? 3.336   -16.521 45.257  1 28.89 ? 55  TRP Z CD2   1 
ATOM   7032  N  NE1   . TRP F 1 55  ? 1.623   -15.086 45.394  1 30.03 ? 55  TRP Z NE1   1 
ATOM   7033  C  CE2   . TRP F 1 55  ? 2.26    -15.954 44.545  1 29.63 ? 55  TRP Z CE2   1 
ATOM   7034  C  CE3   . TRP F 1 55  ? 4.158   -17.448 44.607  1 29.22 ? 55  TRP Z CE3   1 
ATOM   7035  C  CZ2   . TRP F 1 55  ? 1.982   -16.292 43.222  1 30.04 ? 55  TRP Z CZ2   1 
ATOM   7036  C  CZ3   . TRP F 1 55  ? 3.889   -17.767 43.293  1 29.95 ? 55  TRP Z CZ3   1 
ATOM   7037  C  CH2   . TRP F 1 55  ? 2.812   -17.194 42.615  1 30.04 ? 55  TRP Z CH2   1 
ATOM   7038  N  N     . ARG F 1 56  ? 4.29    -17.011 50.768  1 29.53 ? 56  ARG Z N     1 
ATOM   7039  C  CA    . ARG F 1 56  ? 4.96    -17.86  51.731  1 29.47 ? 56  ARG Z CA    1 
ATOM   7040  C  C     . ARG F 1 56  ? 4.444   -19.274 51.558  1 29.69 ? 56  ARG Z C     1 
ATOM   7041  O  O     . ARG F 1 56  ? 3.237   -19.484 51.458  1 29.66 ? 56  ARG Z O     1 
ATOM   7042  C  CB    . ARG F 1 56  ? 4.803   -17.379 53.172  1 30.16 ? 56  ARG Z CB    1 
ATOM   7043  C  CG    . ARG F 1 56  ? 5.833   -18.047 54.079  1 32.38 ? 56  ARG Z CG    1 
ATOM   7044  C  CD    . ARG F 1 56  ? 5.624   -17.751 55.546  1 34.7  ? 56  ARG Z CD    1 
ATOM   7045  N  NE    . ARG F 1 56  ? 4.403   -18.375 56.058  1 36.07 ? 56  ARG Z NE    1 
ATOM   7046  C  CZ    . ARG F 1 56  ? 3.625   -17.848 56.997  1 36.89 ? 56  ARG Z CZ    1 
ATOM   7047  N  NH1   . ARG F 1 56  ? 3.934   -16.68  57.546  1 35.87 ? 56  ARG Z NH1   1 
ATOM   7048  N  NH2   . ARG F 1 56  ? 2.532   -18.482 57.393  1 36.82 ? 56  ARG Z NH2   1 
ATOM   7049  N  N     . PHE F 1 57  ? 5.361   -20.236 51.464  1 29.83 ? 57  PHE Z N     1 
ATOM   7050  C  CA    . PHE F 1 57  ? 5.012   -21.639 51.311  1 30.49 ? 57  PHE Z CA    1 
ATOM   7051  C  C     . PHE F 1 57  ? 5.413   -22.373 52.571  1 31    ? 57  PHE Z C     1 
ATOM   7052  O  O     . PHE F 1 57  ? 6.599   -22.457 52.869  1 31.03 ? 57  PHE Z O     1 
ATOM   7053  C  CB    . PHE F 1 57  ? 5.731   -22.258 50.104  1 30.5  ? 57  PHE Z CB    1 
ATOM   7054  C  CG    . PHE F 1 57  ? 5.31    -21.692 48.771  1 31.27 ? 57  PHE Z CG    1 
ATOM   7055  C  CD1   . PHE F 1 57  ? 5.941   -20.577 48.244  1 32.13 ? 57  PHE Z CD1   1 
ATOM   7056  C  CD2   . PHE F 1 57  ? 4.287   -22.274 48.044  1 31.98 ? 57  PHE Z CD2   1 
ATOM   7057  C  CE1   . PHE F 1 57  ? 5.544   -20.047 47.024  1 32.79 ? 57  PHE Z CE1   1 
ATOM   7058  C  CE2   . PHE F 1 57  ? 3.894   -21.743 46.824  1 32.73 ? 57  PHE Z CE2   1 
ATOM   7059  C  CZ    . PHE F 1 57  ? 4.526   -20.635 46.32   1 32.57 ? 57  PHE Z CZ    1 
ATOM   7060  N  N     . ASP F 1 58  ? 4.428   -22.875 53.328  1 31.27 ? 58  ASP Z N     1 
ATOM   7061  C  CA    . ASP F 1 58  ? 4.674   -23.636 54.55   1 31.84 ? 58  ASP Z CA    1 
ATOM   7062  C  C     . ASP F 1 58  ? 4.607   -25.11  54.196  1 32.29 ? 58  ASP Z C     1 
ATOM   7063  O  O     . ASP F 1 58  ? 3.604   -25.575 53.658  1 32.62 ? 58  ASP Z O     1 
ATOM   7064  C  CB    . ASP F 1 58  ? 3.644   -23.283 55.626  1 33.13 ? 58  ASP Z CB    1 
ATOM   7065  C  CG    . ASP F 1 58  ? 3.675   -21.83  56.045  1 37.62 ? 58  ASP Z CG    1 
ATOM   7066  O  OD1   . ASP F 1 58  ? 4.7     -21.153 55.779  1 38.43 ? 58  ASP Z OD1   1 
ATOM   7067  O  OD2   . ASP F 1 58  ? 2.68    -21.365 56.646  1 39.75 ? 58  ASP Z OD2   1 
ATOM   7068  N  N     . MET F 1 59  ? 5.691   -25.836 54.449  1 31.92 ? 59  MET Z N     1 
ATOM   7069  C  CA    . MET F 1 59  ? 5.783   -27.239 54.083  1 31.73 ? 59  MET Z CA    1 
ATOM   7070  C  C     . MET F 1 59  ? 5.421   -28.182 55.221  1 31.56 ? 59  MET Z C     1 
ATOM   7071  O  O     . MET F 1 59  ? 5.87    -28.006 56.347  1 31.49 ? 59  MET Z O     1 
ATOM   7072  C  CB    . MET F 1 59  ? 7.172   -27.533 53.509  1 31.89 ? 59  MET Z CB    1 
ATOM   7073  C  CG    . MET F 1 59  ? 7.449   -26.755 52.254  1 32.98 ? 59  MET Z CG    1 
ATOM   7074  S  SD    . MET F 1 59  ? 9.203   -26.711 51.862  1 35.67 ? 59  MET Z SD    1 
ATOM   7075  C  CE    . MET F 1 59  ? 9.576   -25.054 52.256  1 34.64 ? 59  MET Z CE    1 
ATOM   7076  N  N     . PHE F 1 60  ? 4.584   -29.176 54.92   1 31.31 ? 60  PHE Z N     1 
ATOM   7077  C  CA    . PHE F 1 60  ? 4.109   -30.156 55.886  1 31.55 ? 60  PHE Z CA    1 
ATOM   7078  C  C     . PHE F 1 60  ? 4.591   -31.544 55.477  1 32.09 ? 60  PHE Z C     1 
ATOM   7079  O  O     . PHE F 1 60  ? 3.894   -32.268 54.759  1 32.27 ? 60  PHE Z O     1 
ATOM   7080  C  CB    . PHE F 1 60  ? 2.577   -30.11  55.97   1 31.25 ? 60  PHE Z CB    1 
ATOM   7081  C  CG    . PHE F 1 60  ? 2.048   -28.934 56.757  1 31.75 ? 60  PHE Z CG    1 
ATOM   7082  C  CD1   . PHE F 1 60  ? 2.131   -27.648 56.257  1 32.4  ? 60  PHE Z CD1   1 
ATOM   7083  C  CD2   . PHE F 1 60  ? 1.463   -29.115 57.995  1 32.53 ? 60  PHE Z CD2   1 
ATOM   7084  C  CE1   . PHE F 1 60  ? 1.667   -26.568 56.993  1 32.88 ? 60  PHE Z CE1   1 
ATOM   7085  C  CE2   . PHE F 1 60  ? 0.979   -28.032 58.718  1 33.05 ? 60  PHE Z CE2   1 
ATOM   7086  C  CZ    . PHE F 1 60  ? 1.086   -26.767 58.213  1 32.65 ? 60  PHE Z CZ    1 
ATOM   7087  N  N     . PRO F 1 61  ? 5.808   -31.919 55.906  1 32.08 ? 61  PRO Z N     1 
ATOM   7088  C  CA    . PRO F 1 61  ? 6.352   -33.221 55.507  1 32.16 ? 61  PRO Z CA    1 
ATOM   7089  C  C     . PRO F 1 61  ? 5.729   -34.397 56.24   1 32.44 ? 61  PRO Z C     1 
ATOM   7090  O  O     . PRO F 1 61  ? 5.7     -34.409 57.456  1 32.67 ? 61  PRO Z O     1 
ATOM   7091  C  CB    . PRO F 1 61  ? 7.854   -33.098 55.828  1 32.8  ? 61  PRO Z CB    1 
ATOM   7092  C  CG    . PRO F 1 61  ? 8.087   -31.662 56.254  1 33.09 ? 61  PRO Z CG    1 
ATOM   7093  C  CD    . PRO F 1 61  ? 6.768   -31.163 56.732  1 31.53 ? 61  PRO Z CD    1 
ATOM   7094  N  N     . GLY F 1 62  ? 5.268   -35.383 55.493  1 32.55 ? 62  GLY Z N     1 
ATOM   7095  C  CA    . GLY F 1 62  ? 4.69    -36.602 56.033  1 33.25 ? 62  GLY Z CA    1 
ATOM   7096  C  C     . GLY F 1 62  ? 3.183   -36.604 56.112  1 33.84 ? 62  GLY Z C     1 
ATOM   7097  O  O     . GLY F 1 62  ? 2.613   -35.941 56.975  1 34.15 ? 62  GLY Z O     1 
ATOM   7098  N  N     . PHE F 1 63  ? 2.525   -37.357 55.232  1 33.99 ? 63  PHE Z N     1 
ATOM   7099  C  CA    . PHE F 1 63  ? 1.07    -37.464 55.263  1 34.61 ? 63  PHE Z CA    1 
ATOM   7100  C  C     . PHE F 1 63  ? 0.629   -38.412 56.387  1 35.42 ? 63  PHE Z C     1 
ATOM   7101  O  O     . PHE F 1 63  ? 1.414   -39.247 56.846  1 35.6  ? 63  PHE Z O     1 
ATOM   7102  C  CB    . PHE F 1 63  ? 0.547   -38.015 53.929  1 34.33 ? 63  PHE Z CB    1 
ATOM   7103  C  CG    . PHE F 1 63  ? 0.623   -37.081 52.75   1 34.67 ? 63  PHE Z CG    1 
ATOM   7104  C  CD1   . PHE F 1 63  ? -0.26   -36.028 52.622  1 35.3  ? 63  PHE Z CD1   1 
ATOM   7105  C  CD2   . PHE F 1 63  ? 1.53    -37.299 51.734  1 35.4  ? 63  PHE Z CD2   1 
ATOM   7106  C  CE1   . PHE F 1 63  ? -0.213  -35.192 51.511  1 35.79 ? 63  PHE Z CE1   1 
ATOM   7107  C  CE2   . PHE F 1 63  ? 1.573   -36.462 50.626  1 35.92 ? 63  PHE Z CE2   1 
ATOM   7108  C  CZ    . PHE F 1 63  ? 0.7     -35.418 50.521  1 35.51 ? 63  PHE Z CZ    1 
ATOM   7109  N  N     . ASN F 1 64  ? -0.639  -38.311 56.805  1 35.76 ? 64  ASN Z N     1 
ATOM   7110  C  CA    . ASN F 1 64  ? -1.188  -39.22  57.807  1 36.57 ? 64  ASN Z CA    1 
ATOM   7111  C  C     . ASN F 1 64  ? -1.521  -40.563 57.165  1 38.3  ? 64  ASN Z C     1 
ATOM   7112  O  O     . ASN F 1 64  ? -1.888  -40.62  55.99   1 38.68 ? 64  ASN Z O     1 
ATOM   7113  C  CB    . ASN F 1 64  ? -2.459  -38.643 58.424  1 36.27 ? 64  ASN Z CB    1 
ATOM   7114  C  CG    . ASN F 1 64  ? -2.218  -37.666 59.531  1 36.74 ? 64  ASN Z CG    1 
ATOM   7115  O  OD1   . ASN F 1 64  ? -1.086  -37.326 59.862  1 37.01 ? 64  ASN Z OD1   1 
ATOM   7116  N  ND2   . ASN F 1 64  ? -3.283  -37.19  60.128  1 36.69 ? 64  ASN Z ND2   1 
ATOM   7117  N  N     . LYS F 1 65  ? -1.414  -41.64  57.936  1 39.19 ? 65  LYS Z N     1 
ATOM   7118  C  CA    . LYS F 1 65  ? -1.733  -42.976 57.454  1 40.63 ? 65  LYS Z CA    1 
ATOM   7119  C  C     . LYS F 1 65  ? -3.089  -43.434 57.995  1 42.14 ? 65  LYS Z C     1 
ATOM   7120  O  O     . LYS F 1 65  ? -3.84   -44.096 57.286  1 42.3  ? 65  LYS Z O     1 
ATOM   7121  C  CB    . LYS F 1 65  ? -0.616  -43.953 57.829  1 42.45 ? 65  LYS Z CB    1 
ATOM   7122  C  CG    . LYS F 1 65  ? 0.665   -43.657 57.071  1 46.76 ? 65  LYS Z CG    1 
ATOM   7123  C  CD    . LYS F 1 65  ? 1.901   -43.783 57.936  1 51.4  ? 65  LYS Z CD    1 
ATOM   7124  C  CE    . LYS F 1 65  ? 3.145   -43.596 57.1    1 55.27 ? 65  LYS Z CE    1 
ATOM   7125  N  NZ    . LYS F 1 65  ? 4.353   -44.144 57.773  1 57.77 ? 65  LYS Z NZ    1 
ATOM   7126  N  N     . ASN F 1 66  ? -3.412  -43.068 59.242  1 43.03 ? 66  ASN Z N     1 
ATOM   7127  C  CA    . ASN F 1 66  ? -4.686  -43.413 59.862  1 44.24 ? 66  ASN Z CA    1 
ATOM   7128  C  C     . ASN F 1 66  ? -5.636  -42.185 59.748  1 45.34 ? 66  ASN Z C     1 
ATOM   7129  O  O     . ASN F 1 66  ? -6.229  -42.004 58.685  1 45.46 ? 66  ASN Z O     1 
ATOM   7130  C  CB    . ASN F 1 66  ? -4.465  -43.936 61.306  1 45.16 ? 66  ASN Z CB    1 
ATOM   7131  C  CG    . ASN F 1 66  ? -5.704  -44.428 62.015  1 47.71 ? 66  ASN Z CG    1 
ATOM   7132  O  OD1   . ASN F 1 66  ? -6.838  -44.294 61.539  1 48.46 ? 66  ASN Z OD1   1 
ATOM   7133  N  ND2   . ASN F 1 66  ? -5.509  -45.017 63.185  1 48.38 ? 66  ASN Z ND2   1 
ATOM   7134  N  N     . THR F 1 67  ? -5.753  -41.334 60.791  1 45.95 ? 67  THR Z N     1 
ATOM   7135  C  CA    . THR F 1 67  ? -6.605  -40.151 60.741  1 47.25 ? 67  THR Z CA    1 
ATOM   7136  C  C     . THR F 1 67  ? -5.956  -38.972 61.49   1 47.56 ? 67  THR Z C     1 
ATOM   7137  O  O     . THR F 1 67  ? -5.96   -37.855 60.973  1 47.73 ? 67  THR Z O     1 
ATOM   7138  C  CB    . THR F 1 67  ? -8.05   -40.463 61.197  1 49.43 ? 67  THR Z CB    1 
ATOM   7139  O  OG1   . THR F 1 67  ? -8.81   -39.248 61.258  1 50.86 ? 67  THR Z OG1   1 
ATOM   7140  C  CG2   . THR F 1 67  ? -8.109  -41.184 62.547  1 49.92 ? 67  THR Z CG2   1 
ATOM   7141  N  N     . ASN F 1 68  ? -5.395  -39.213 62.694  1 47.26 ? 68  ASN Z N     1 
ATOM   7142  C  CA    . ASN F 1 68  ? -4.719  -38.176 63.479  1 47.26 ? 68  ASN Z CA    1 
ATOM   7143  C  C     . ASN F 1 68  ? -3.393  -38.709 64.07   1 46.38 ? 68  ASN Z C     1 
ATOM   7144  O  O     . ASN F 1 68  ? -2.991  -38.279 65.154  1 46.65 ? 68  ASN Z O     1 
ATOM   7145  C  CB    . ASN F 1 68  ? -5.611  -37.661 64.615  1 49.36 ? 68  ASN Z CB    1 
ATOM   7146  C  CG    . ASN F 1 68  ? -7.058  -37.406 64.269  1 53.84 ? 68  ASN Z CG    1 
ATOM   7147  O  OD1   . ASN F 1 68  ? -7.961  -37.861 64.97   1 55.5  ? 68  ASN Z OD1   1 
ATOM   7148  N  ND2   . ASN F 1 68  ? -7.323  -36.66  63.204  1 54.76 ? 68  ASN Z ND2   1 
ATOM   7149  N  N     . ASP F 1 69  ? -2.714  -39.639 63.363  1 45.18 ? 69  ASP Z N     1 
ATOM   7150  C  CA    . ASP F 1 69  ? -1.464  -40.232 63.85   1 44.34 ? 69  ASP Z CA    1 
ATOM   7151  C  C     . ASP F 1 69  ? -0.27   -39.276 63.806  1 43.24 ? 69  ASP Z C     1 
ATOM   7152  O  O     . ASP F 1 69  ? 0.533   -39.269 64.74   1 43.32 ? 69  ASP Z O     1 
ATOM   7153  C  CB    . ASP F 1 69  ? -1.14   -41.552 63.136  1 45.74 ? 69  ASP Z CB    1 
ATOM   7154  C  CG    . ASP F 1 69  ? -1.025  -41.432 61.638  1 49.71 ? 69  ASP Z CG    1 
ATOM   7155  O  OD1   . ASP F 1 69  ? -1.993  -40.957 61.007  1 50.15 ? 69  ASP Z OD1   1 
ATOM   7156  O  OD2   . ASP F 1 69  ? 0.026   -41.837 61.088  1 51.92 ? 69  ASP Z OD2   1 
ATOM   7157  N  N     . ARG F 1 70  ? -0.146  -38.473 62.739  1 42    ? 70  ARG Z N     1 
ATOM   7158  C  CA    . ARG F 1 70  ? 0.942   -37.505 62.651  1 41.01 ? 70  ARG Z CA    1 
ATOM   7159  C  C     . ARG F 1 70  ? 0.395   -36.091 62.894  1 40.14 ? 70  ARG Z C     1 
ATOM   7160  O  O     . ARG F 1 70  ? 0.635   -35.523 63.946  1 40.18 ? 70  ARG Z O     1 
ATOM   7161  C  CB    . ARG F 1 70  ? 1.746   -37.652 61.339  1 41.42 ? 70  ARG Z CB    1 
ATOM   7162  C  CG    . ARG F 1 70  ? 2.723   -36.512 61.09   1 42.83 ? 70  ARG Z CG    1 
ATOM   7163  C  CD    . ARG F 1 70  ? 3.88    -36.937 60.22   1 44.39 ? 70  ARG Z CD    1 
ATOM   7164  N  NE    . ARG F 1 70  ? 4.749   -35.81  59.879  1 45.46 ? 70  ARG Z NE    1 
ATOM   7165  C  CZ    . ARG F 1 70  ? 5.752   -35.376 60.634  1 46.38 ? 70  ARG Z CZ    1 
ATOM   7166  N  NH1   . ARG F 1 70  ? 6.011   -35.952 61.8    1 45.99 ? 70  ARG Z NH1   1 
ATOM   7167  N  NH2   . ARG F 1 70  ? 6.494   -34.349 60.237  1 45.59 ? 70  ARG Z NH2   1 
ATOM   7168  N  N     . TRP F 1 71  ? -0.389  -35.558 61.968  1 39.14 ? 71  TRP Z N     1 
ATOM   7169  C  CA    . TRP F 1 71  ? -0.987  -34.239 62.102  1 38.63 ? 71  TRP Z CA    1 
ATOM   7170  C  C     . TRP F 1 71  ? -2.343  -34.349 62.799  1 38.3  ? 71  TRP Z C     1 
ATOM   7171  O  O     . TRP F 1 71  ? -2.949  -35.42  62.808  1 38.24 ? 71  TRP Z O     1 
ATOM   7172  C  CB    . TRP F 1 71  ? -1.147  -33.595 60.713  1 38.29 ? 71  TRP Z CB    1 
ATOM   7173  C  CG    . TRP F 1 71  ? 0.119   -33.58  59.911  1 38.25 ? 71  TRP Z CG    1 
ATOM   7174  C  CD1   . TRP F 1 71  ? 0.458   -34.426 58.898  1 38.85 ? 71  TRP Z CD1   1 
ATOM   7175  C  CD2   . TRP F 1 71  ? 1.25    -32.724 60.115  1 38.24 ? 71  TRP Z CD2   1 
ATOM   7176  N  NE1   . TRP F 1 71  ? 1.721   -34.136 58.446  1 39.09 ? 71  TRP Z NE1   1 
ATOM   7177  C  CE2   . TRP F 1 71  ? 2.229   -33.091 59.175  1 38.87 ? 71  TRP Z CE2   1 
ATOM   7178  C  CE3   . TRP F 1 71  ? 1.524   -31.666 60.992  1 38.85 ? 71  TRP Z CE3   1 
ATOM   7179  C  CZ2   . TRP F 1 71  ? 3.459   -32.436 59.084  1 39.46 ? 71  TRP Z CZ2   1 
ATOM   7180  C  CZ3   . TRP F 1 71  ? 2.739   -31.014 60.893  1 39.63 ? 71  TRP Z CZ3   1 
ATOM   7181  C  CH2   . TRP F 1 71  ? 3.694   -31.406 59.956  1 39.6  ? 71  TRP Z CH2   1 
ATOM   7182  N  N     . ASN F 1 72  ? -2.827  -33.24  63.376  1 38.11 ? 72  ASN Z N     1 
ATOM   7183  C  CA    . ASN F 1 72  ? -4.124  -33.222 64.064  1 38.52 ? 72  ASN Z CA    1 
ATOM   7184  C  C     . ASN F 1 72  ? -5.31   -33.502 63.133  1 38.2  ? 72  ASN Z C     1 
ATOM   7185  O  O     . ASN F 1 72  ? -6.356  -33.966 63.578  1 38.22 ? 72  ASN Z O     1 
ATOM   7186  C  CB    . ASN F 1 72  ? -4.323  -31.913 64.843  1 40.14 ? 72  ASN Z CB    1 
ATOM   7187  C  CG    . ASN F 1 72  ? -4.727  -30.714 64.017  1 43.63 ? 72  ASN Z CG    1 
ATOM   7188  O  OD1   . ASN F 1 72  ? -4.306  -30.533 62.874  1 44.3  ? 72  ASN Z OD1   1 
ATOM   7189  N  ND2   . ASN F 1 72  ? -5.55   -29.853 64.597  1 45.06 ? 72  ASN Z ND2   1 
ATOM   7190  N  N     . SER F 1 73  ? -5.146  -33.184 61.851  1 37.79 ? 73  SER Z N     1 
ATOM   7191  C  CA    . SER F 1 73  ? -6.148  -33.407 60.825  1 37.93 ? 73  SER Z CA    1 
ATOM   7192  C  C     . SER F 1 73  ? -5.471  -33.817 59.518  1 37.36 ? 73  SER Z C     1 
ATOM   7193  O  O     . SER F 1 73  ? -4.319  -33.46  59.269  1 37.21 ? 73  SER Z O     1 
ATOM   7194  C  CB    . SER F 1 73  ? -7.017  -32.17  60.635  1 39.78 ? 73  SER Z CB    1 
ATOM   7195  O  OG    . SER F 1 73  ? -6.236  -31.008 60.41   1 42.35 ? 73  SER Z OG    1 
ATOM   7196  N  N     . ASN F 1 74  ? -6.181  -34.592 58.699  1 36.96 ? 74  ASN Z N     1 
ATOM   7197  C  CA    . ASN F 1 74  ? -5.653  -35.124 57.446  1 37.11 ? 74  ASN Z CA    1 
ATOM   7198  C  C     . ASN F 1 74  ? -6.051  -34.278 56.242  1 36.43 ? 74  ASN Z C     1 
ATOM   7199  O  O     . ASN F 1 74  ? -7.231  -34.22  55.91   1 36.72 ? 74  ASN Z O     1 
ATOM   7200  C  CB    . ASN F 1 74  ? -6.155  -36.565 57.261  1 38.62 ? 74  ASN Z CB    1 
ATOM   7201  C  CG    . ASN F 1 74  ? -5.421  -37.378 56.225  1 42.18 ? 74  ASN Z CG    1 
ATOM   7202  O  OD1   . ASN F 1 74  ? -4.544  -36.884 55.51   1 43.6  ? 74  ASN Z OD1   1 
ATOM   7203  N  ND2   . ASN F 1 74  ? -5.764  -38.655 56.129  1 42.83 ? 74  ASN Z ND2   1 
ATOM   7204  N  N     . ILE F 1 75  ? -5.074  -33.686 55.544  1 35.41 ? 75  ILE Z N     1 
ATOM   7205  C  CA    . ILE F 1 75  ? -5.369  -32.895 54.345  1 35.06 ? 75  ILE Z CA    1 
ATOM   7206  C  C     . ILE F 1 75  ? -5.969  -33.747 53.206  1 34.26 ? 75  ILE Z C     1 
ATOM   7207  O  O     . ILE F 1 75  ? -6.733  -33.228 52.388  1 34.35 ? 75  ILE Z O     1 
ATOM   7208  C  CB    . ILE F 1 75  ? -4.134  -32.097 53.883  1 35.66 ? 75  ILE Z CB    1 
ATOM   7209  C  CG1   . ILE F 1 75  ? -4.539  -30.942 52.955  1 36.49 ? 75  ILE Z CG1   1 
ATOM   7210  C  CG2   . ILE F 1 75  ? -3.102  -33.013 53.232  1 36.2  ? 75  ILE Z CG2   1 
ATOM   7211  C  CD1   . ILE F 1 75  ? -5.4    -29.921 53.607  1 37.65 ? 75  ILE Z CD1   1 
ATOM   7212  N  N     . LEU F 1 76  ? -5.659  -35.06  53.183  1 33.15 ? 76  LEU Z N     1 
ATOM   7213  C  CA    . LEU F 1 76  ? -6.202  -35.996 52.204  1 32.53 ? 76  LEU Z CA    1 
ATOM   7214  C  C     . LEU F 1 76  ? -7.723  -36.171 52.348  1 32.21 ? 76  LEU Z C     1 
ATOM   7215  O  O     . LEU F 1 76  ? -8.364  -36.629 51.407  1 32.04 ? 76  LEU Z O     1 
ATOM   7216  C  CB    . LEU F 1 76  ? -5.501  -37.352 52.317  1 32.55 ? 76  LEU Z CB    1 
ATOM   7217  C  CG    . LEU F 1 76  ? -4.029  -37.36  51.956  1 33.77 ? 76  LEU Z CG    1 
ATOM   7218  C  CD1   . LEU F 1 76  ? -3.364  -38.627 52.43   1 34.32 ? 76  LEU Z CD1   1 
ATOM   7219  C  CD2   . LEU F 1 76  ? -3.848  -37.247 50.474  1 34.32 ? 76  LEU Z CD2   1 
ATOM   7220  N  N     . ASP F 1 77  ? -8.308  -35.797 53.508  1 32.08 ? 77  ASP Z N     1 
ATOM   7221  C  CA    . ASP F 1 77  ? -9.754  -35.875 53.686  1 32.35 ? 77  ASP Z CA    1 
ATOM   7222  C  C     . ASP F 1 77  ? -10.487 -34.923 52.73   1 32.27 ? 77  ASP Z C     1 
ATOM   7223  O  O     . ASP F 1 77  ? -11.601 -35.236 52.313  1 32.63 ? 77  ASP Z O     1 
ATOM   7224  C  CB    . ASP F 1 77  ? -10.179 -35.62  55.136  1 33.94 ? 77  ASP Z CB    1 
ATOM   7225  C  CG    . ASP F 1 77  ? -11.669 -35.82  55.339  1 38.29 ? 77  ASP Z CG    1 
ATOM   7226  O  OD1   . ASP F 1 77  ? -12.121 -36.986 55.302  1 39.64 ? 77  ASP Z OD1   1 
ATOM   7227  O  OD2   . ASP F 1 77  ? -12.389 -34.808 55.488  1 39.65 ? 77  ASP Z OD2   1 
ATOM   7228  N  N     . LEU F 1 78  ? -9.86   -33.8   52.336  1 31.57 ? 78  LEU Z N     1 
ATOM   7229  C  CA    . LEU F 1 78  ? -10.474 -32.884 51.377  1 31.36 ? 78  LEU Z CA    1 
ATOM   7230  C  C     . LEU F 1 78  ? -10.712 -33.549 50.012  1 31.37 ? 78  LEU Z C     1 
ATOM   7231  O  O     . LEU F 1 78  ? -11.632 -33.158 49.292  1 31.56 ? 78  LEU Z O     1 
ATOM   7232  C  CB    . LEU F 1 78  ? -9.632  -31.614 51.222  1 31.3  ? 78  LEU Z CB    1 
ATOM   7233  C  CG    . LEU F 1 78  ? -9.535  -30.725 52.449  1 32.47 ? 78  LEU Z CG    1 
ATOM   7234  C  CD1   . LEU F 1 78  ? -8.689  -29.51  52.155  1 33.02 ? 78  LEU Z CD1   1 
ATOM   7235  C  CD2   . LEU F 1 78  ? -10.916 -30.295 52.929  1 32.97 ? 78  LEU Z CD2   1 
ATOM   7236  N  N     . LEU F 1 79  ? -9.891  -34.559 49.664  1 30.95 ? 79  LEU Z N     1 
ATOM   7237  C  CA    . LEU F 1 79  ? -10.036 -35.318 48.433  1 30.72 ? 79  LEU Z CA    1 
ATOM   7238  C  C     . LEU F 1 79  ? -11.18  -36.312 48.601  1 30.54 ? 79  LEU Z C     1 
ATOM   7239  O  O     . LEU F 1 79  ? -12.021 -36.42  47.714  1 30.26 ? 79  LEU Z O     1 
ATOM   7240  C  CB    . LEU F 1 79  ? -8.737  -36.052 48.109  1 30.88 ? 79  LEU Z CB    1 
ATOM   7241  C  CG    . LEU F 1 79  ? -7.546  -35.16  47.836  1 32.5  ? 79  LEU Z CG    1 
ATOM   7242  C  CD1   . LEU F 1 79  ? -6.277  -35.974 47.737  1 33.15 ? 79  LEU Z CD1   1 
ATOM   7243  C  CD2   . LEU F 1 79  ? -7.751  -34.36  46.571  1 33.18 ? 79  LEU Z CD2   1 
ATOM   7244  N  N     . SER F 1 80  ? -11.249 -37.005 49.754  1 30.63 ? 80  SER Z N     1 
ATOM   7245  C  CA    . SER F 1 80  ? -12.327 -37.965 50.011  1 31.11 ? 80  SER Z CA    1 
ATOM   7246  C  C     . SER F 1 80  ? -13.704 -37.299 50.115  1 31.4  ? 80  SER Z C     1 
ATOM   7247  O  O     . SER F 1 80  ? -14.709 -37.939 49.811  1 31.87 ? 80  SER Z O     1 
ATOM   7248  C  CB    . SER F 1 80  ? -12.031 -38.825 51.236  1 32.07 ? 80  SER Z CB    1 
ATOM   7249  O  OG    . SER F 1 80  ? -12.03  -38.054 52.424  1 33.86 ? 80  SER Z OG    1 
ATOM   7250  N  N     . GLN F 1 81  ? -13.752 -36.011 50.504  1 30.9  ? 81  GLN Z N     1 
ATOM   7251  C  CA    . GLN F 1 81  ? -15.006 -35.254 50.545  1 30.96 ? 81  GLN Z CA    1 
ATOM   7252  C  C     . GLN F 1 81  ? -15.558 -34.996 49.124  1 30.72 ? 81  GLN Z C     1 
ATOM   7253  O  O     . GLN F 1 81  ? -16.753 -34.755 48.967  1 30.99 ? 81  GLN Z O     1 
ATOM   7254  C  CB    . GLN F 1 81  ? -14.81  -33.914 51.272  1 32.59 ? 81  GLN Z CB    1 
ATOM   7255  C  CG    . GLN F 1 81  ? -14.606 -34.058 52.771  1 36.59 ? 81  GLN Z CG    1 
ATOM   7256  C  CD    . GLN F 1 81  ? -14.3   -32.739 53.435  1 41.41 ? 81  GLN Z CD    1 
ATOM   7257  O  OE1   . GLN F 1 81  ? -14.809 -31.682 53.042  1 43.16 ? 81  GLN Z OE1   1 
ATOM   7258  N  NE2   . GLN F 1 81  ? -13.485 -32.775 54.482  1 41.83 ? 81  GLN Z NE2   1 
ATOM   7259  N  N     . LYS F 1 82  ? -14.695 -35.034 48.1    1 30.03 ? 82  LYS Z N     1 
ATOM   7260  C  CA    . LYS F 1 82  ? -15.095 -34.789 46.727  1 29.95 ? 82  LYS Z CA    1 
ATOM   7261  C  C     . LYS F 1 82  ? -15.108 -36.056 45.842  1 29.92 ? 82  LYS Z C     1 
ATOM   7262  O  O     . LYS F 1 82  ? -15.191 -35.942 44.617  1 30.23 ? 82  LYS Z O     1 
ATOM   7263  C  CB    . LYS F 1 82  ? -14.221 -33.677 46.117  1 31.44 ? 82  LYS Z CB    1 
ATOM   7264  C  CG    . LYS F 1 82  ? -14.378 -32.321 46.81   1 34.34 ? 82  LYS Z CG    1 
ATOM   7265  C  CD    . LYS F 1 82  ? -15.626 -31.594 46.327  1 38.08 ? 82  LYS Z CD    1 
ATOM   7266  C  CE    . LYS F 1 82  ? -15.437 -31.053 44.93   1 41.5  ? 82  LYS Z CE    1 
ATOM   7267  N  NZ    . LYS F 1 82  ? -16.705 -30.571 44.316  1 43.63 ? 82  LYS Z NZ    1 
ATOM   7268  N  N     . GLY F 1 83  ? -15.043 -37.239 46.452  1 29.28 ? 83  GLY Z N     1 
ATOM   7269  C  CA    . GLY F 1 83  ? -15.124 -38.486 45.701  1 29.24 ? 83  GLY Z CA    1 
ATOM   7270  C  C     . GLY F 1 83  ? -13.873 -39.327 45.544  1 28.83 ? 83  GLY Z C     1 
ATOM   7271  O  O     . GLY F 1 83  ? -13.907 -40.317 44.806  1 28.95 ? 83  GLY Z O     1 
ATOM   7272  N  N     . SER F 1 84  ? -12.765 -38.967 46.213  1 28.11 ? 84  SER Z N     1 
ATOM   7273  C  CA    . SER F 1 84  ? -11.548 -39.776 46.112  1 27.93 ? 84  SER Z CA    1 
ATOM   7274  C  C     . SER F 1 84  ? -11.645 -40.917 47.124  1 27.92 ? 84  SER Z C     1 
ATOM   7275  O  O     . SER F 1 84  ? -11.135 -40.798 48.236  1 27.87 ? 84  SER Z O     1 
ATOM   7276  C  CB    . SER F 1 84  ? -10.305 -38.934 46.36   1 28.76 ? 84  SER Z CB    1 
ATOM   7277  O  OG    . SER F 1 84  ? -9.12   -39.666 46.107  1 30.54 ? 84  SER Z OG    1 
ATOM   7278  N  N     . PHE F 1 85  ? -12.325 -42.018 46.736  1 27.74 ? 85  PHE Z N     1 
ATOM   7279  C  CA    . PHE F 1 85  ? -12.548 -43.187 47.588  1 27.71 ? 85  PHE Z CA    1 
ATOM   7280  C  C     . PHE F 1 85  ? -11.385 -44.18  47.643  1 27.91 ? 85  PHE Z C     1 
ATOM   7281  O  O     . PHE F 1 85  ? -11.486 -45.178 48.358  1 28.23 ? 85  PHE Z O     1 
ATOM   7282  C  CB    . PHE F 1 85  ? -13.842 -43.914 47.209  1 27.48 ? 85  PHE Z CB    1 
ATOM   7283  C  CG    . PHE F 1 85  ? -13.917 -44.356 45.771  1 28    ? 85  PHE Z CG    1 
ATOM   7284  C  CD1   . PHE F 1 85  ? -13.164 -45.421 45.316  1 28.87 ? 85  PHE Z CD1   1 
ATOM   7285  C  CD2   . PHE F 1 85  ? -14.775 -43.738 44.887  1 28.76 ? 85  PHE Z CD2   1 
ATOM   7286  C  CE1   . PHE F 1 85  ? -13.219 -45.813 43.988  1 29.63 ? 85  PHE Z CE1   1 
ATOM   7287  C  CE2   . PHE F 1 85  ? -14.85  -44.153 43.568  1 29.56 ? 85  PHE Z CE2   1 
ATOM   7288  C  CZ    . PHE F 1 85  ? -14.078 -45.193 43.129  1 29.42 ? 85  PHE Z CZ    1 
ATOM   7289  N  N     . LEU F 1 86  ? -10.319 -43.954 46.873  1 27.79 ? 86  LEU Z N     1 
ATOM   7290  C  CA    . LEU F 1 86  ? -9.153  -44.826 46.938  1 28.45 ? 86  LEU Z CA    1 
ATOM   7291  C  C     . LEU F 1 86  ? -8.126  -44.143 47.82   1 29.2  ? 86  LEU Z C     1 
ATOM   7292  O  O     . LEU F 1 86  ? -7.913  -42.936 47.685  1 29.3  ? 86  LEU Z O     1 
ATOM   7293  C  CB    . LEU F 1 86  ? -8.562  -45.108 45.55   1 28.62 ? 86  LEU Z CB    1 
ATOM   7294  C  CG    . LEU F 1 86  ? -9.457  -45.851 44.562  1 29.87 ? 86  LEU Z CG    1 
ATOM   7295  C  CD1   . LEU F 1 86  ? -8.747  -46.048 43.24   1 30.39 ? 86  LEU Z CD1   1 
ATOM   7296  C  CD2   . LEU F 1 86  ? -9.919  -47.195 45.13   1 30.37 ? 86  LEU Z CD2   1 
ATOM   7297  N  N     . TYR F 1 87  ? -7.491  -44.897 48.734  1 29.66 ? 87  TYR Z N     1 
ATOM   7298  C  CA    . TYR F 1 87  ? -6.495  -44.302 49.62   1 30.49 ? 87  TYR Z CA    1 
ATOM   7299  C  C     . TYR F 1 87  ? -5.118  -44.297 49.001  1 29.83 ? 87  TYR Z C     1 
ATOM   7300  O  O     . TYR F 1 87  ? -4.131  -44.689 49.627  1 29.78 ? 87  TYR Z O     1 
ATOM   7301  C  CB    . TYR F 1 87  ? -6.493  -44.921 51.021  1 31.61 ? 87  TYR Z CB    1 
ATOM   7302  C  CG    . TYR F 1 87  ? -5.939  -43.994 52.083  1 33.46 ? 87  TYR Z CG    1 
ATOM   7303  C  CD1   . TYR F 1 87  ? -6.096  -42.616 51.986  1 34.86 ? 87  TYR Z CD1   1 
ATOM   7304  C  CD2   . TYR F 1 87  ? -5.286  -44.496 53.199  1 34.71 ? 87  TYR Z CD2   1 
ATOM   7305  C  CE1   . TYR F 1 87  ? -5.596  -41.761 52.96   1 36.07 ? 87  TYR Z CE1   1 
ATOM   7306  C  CE2   . TYR F 1 87  ? -4.789  -43.652 54.183  1 35.93 ? 87  TYR Z CE2   1 
ATOM   7307  C  CZ    . TYR F 1 87  ? -4.946  -42.284 54.06   1 37.18 ? 87  TYR Z CZ    1 
ATOM   7308  O  OH    . TYR F 1 87  ? -4.447  -41.439 55.022  1 39.18 ? 87  TYR Z OH    1 
ATOM   7309  N  N     . GLU F 1 88  ? -5.066  -43.846 47.751  1 29.07 ? 88  GLU Z N     1 
ATOM   7310  C  CA    . GLU F 1 88  ? -3.839  -43.677 47.012  1 28.74 ? 88  GLU Z CA    1 
ATOM   7311  C  C     . GLU F 1 88  ? -3.382  -42.255 47.298  1 28.02 ? 88  GLU Z C     1 
ATOM   7312  O  O     . GLU F 1 88  ? -4.158  -41.304 47.191  1 27.77 ? 88  GLU Z O     1 
ATOM   7313  C  CB    . GLU F 1 88  ? -4.088  -43.897 45.525  1 31.17 ? 88  GLU Z CB    1 
ATOM   7314  C  CG    . GLU F 1 88  ? -4.46   -45.328 45.193  1 35.47 ? 88  GLU Z CG    1 
ATOM   7315  C  CD    . GLU F 1 88  ? -3.497  -46.042 44.264  1 41.12 ? 88  GLU Z CD    1 
ATOM   7316  O  OE1   . GLU F 1 88  ? -2.632  -45.367 43.657  1 41.75 ? 88  GLU Z OE1   1 
ATOM   7317  O  OE2   . GLU F 1 88  ? -3.625  -47.279 44.123  1 43.36 ? 88  GLU Z OE2   1 
ATOM   7318  N  N     . THR F 1 89  ? -2.141  -42.122 47.726  1 27.6  ? 89  THR Z N     1 
ATOM   7319  C  CA    . THR F 1 89  ? -1.601  -40.847 48.145  1 27.74 ? 89  THR Z CA    1 
ATOM   7320  C  C     . THR F 1 89  ? -0.648  -40.228 47.135  1 28.14 ? 89  THR Z C     1 
ATOM   7321  O  O     . THR F 1 89  ? 0.379   -40.826 46.804  1 28.28 ? 89  THR Z O     1 
ATOM   7322  C  CB    . THR F 1 89  ? -0.939  -41.043 49.502  1 28.54 ? 89  THR Z CB    1 
ATOM   7323  O  OG1   . THR F 1 89  ? -1.92   -41.522 50.418  1 29.53 ? 89  THR Z OG1   1 
ATOM   7324  C  CG2   . THR F 1 89  ? -0.336  -39.784 50.034  1 28.73 ? 89  THR Z CG2   1 
ATOM   7325  N  N     . PRO F 1 90  ? -0.95   -39.003 46.653  1 27.99 ? 90  PRO Z N     1 
ATOM   7326  C  CA    . PRO F 1 90  ? -0.008  -38.332 45.74   1 27.96 ? 90  PRO Z CA    1 
ATOM   7327  C  C     . PRO F 1 90  ? 1.247   -37.868 46.48   1 28.26 ? 90  PRO Z C     1 
ATOM   7328  O  O     . PRO F 1 90  ? 1.269   -37.858 47.714  1 28.05 ? 90  PRO Z O     1 
ATOM   7329  C  CB    . PRO F 1 90  ? -0.811  -37.146 45.217  1 28.46 ? 90  PRO Z CB    1 
ATOM   7330  C  CG    . PRO F 1 90  ? -1.725  -36.818 46.338  1 28.91 ? 90  PRO Z CG    1 
ATOM   7331  C  CD    . PRO F 1 90  ? -2.104  -38.14  46.971  1 27.34 ? 90  PRO Z CD    1 
ATOM   7332  N  N     . ASP F 1 91  ? 2.294   -37.488 45.738  1 28.64 ? 91  ASP Z N     1 
ATOM   7333  C  CA    . ASP F 1 91  ? 3.535   -37.06  46.374  1 29.48 ? 91  ASP Z CA    1 
ATOM   7334  C  C     . ASP F 1 91  ? 3.392   -35.713 47.065  1 30.44 ? 91  ASP Z C     1 
ATOM   7335  O  O     . ASP F 1 91  ? 3.919   -35.531 48.161  1 30.67 ? 91  ASP Z O     1 
ATOM   7336  C  CB    . ASP F 1 91  ? 4.708   -37.085 45.386  1 30.5  ? 91  ASP Z CB    1 
ATOM   7337  C  CG    . ASP F 1 91  ? 5.146   -38.48  44.977  1 33.7  ? 91  ASP Z CG    1 
ATOM   7338  O  OD1   . ASP F 1 91  ? 4.758   -39.456 45.663  1 34.23 ? 91  ASP Z OD1   1 
ATOM   7339  O  OD2   . ASP F 1 91  ? 5.881   -38.597 43.979  1 35.27 ? 91  ASP Z OD2   1 
ATOM   7340  N  N     . VAL F 1 92  ? 2.642   -34.787 46.448  1 30.68 ? 92  VAL Z N     1 
ATOM   7341  C  CA    . VAL F 1 92  ? 2.422   -33.448 46.98   1 31.32 ? 92  VAL Z CA    1 
ATOM   7342  C  C     . VAL F 1 92  ? 0.957   -33.003 46.793  1 31.74 ? 92  VAL Z C     1 
ATOM   7343  O  O     . VAL F 1 92  ? 0.309   -33.393 45.828  1 31.98 ? 92  VAL Z O     1 
ATOM   7344  C  CB    . VAL F 1 92  ? 3.401   -32.449 46.295  1 32.25 ? 92  VAL Z CB    1 
ATOM   7345  C  CG1   . VAL F 1 92  ? 3.021   -30.998 46.563  1 32.98 ? 92  VAL Z CG1   1 
ATOM   7346  C  CG2   . VAL F 1 92  ? 4.843   -32.7   46.711  1 32.73 ? 92  VAL Z CG2   1 
ATOM   7347  N  N     . ILE F 1 93  ? 0.45    -32.185 47.725  1 31.78 ? 93  ILE Z N     1 
ATOM   7348  C  CA    . ILE F 1 93  ? -0.848  -31.518 47.671  1 32.33 ? 93  ILE Z CA    1 
ATOM   7349  C  C     . ILE F 1 93  ? -0.554  -30.037 47.936  1 32.49 ? 93  ILE Z C     1 
ATOM   7350  O  O     . ILE F 1 93  ? -0.009  -29.708 48.993  1 32.47 ? 93  ILE Z O     1 
ATOM   7351  C  CB    . ILE F 1 93  ? -1.871  -32.04  48.713  1 32.89 ? 93  ILE Z CB    1 
ATOM   7352  C  CG1   . ILE F 1 93  ? -2.25   -33.499 48.46   1 33.86 ? 93  ILE Z CG1   1 
ATOM   7353  C  CG2   . ILE F 1 93  ? -3.121  -31.141 48.738  1 33.37 ? 93  ILE Z CG2   1 
ATOM   7354  C  CD1   . ILE F 1 93  ? -3.059  -34.07  49.572  1 35.02 ? 93  ILE Z CD1   1 
ATOM   7355  N  N     . ILE F 1 94  ? -0.88   -29.154 46.983  1 32.37 ? 94  ILE Z N     1 
ATOM   7356  C  CA    . ILE F 1 94  ? -0.663  -27.726 47.175  1 32.84 ? 94  ILE Z CA    1 
ATOM   7357  C  C     . ILE F 1 94  ? -1.988  -27.117 47.566  1 33    ? 94  ILE Z C     1 
ATOM   7358  O  O     . ILE F 1 94  ? -2.98   -27.338 46.882  1 32.73 ? 94  ILE Z O     1 
ATOM   7359  C  CB    . ILE F 1 94  ? -0.112  -27.049 45.896  1 33.61 ? 94  ILE Z CB    1 
ATOM   7360  C  CG1   . ILE F 1 94  ? 1.169   -27.745 45.393  1 34.61 ? 94  ILE Z CG1   1 
ATOM   7361  C  CG2   . ILE F 1 94  ? 0.087   -25.54  46.113  1 34.02 ? 94  ILE Z CG2   1 
ATOM   7362  C  CD1   . ILE F 1 94  ? 1.727   -27.188 44.107  1 35.75 ? 94  ILE Z CD1   1 
ATOM   7363  N  N     . THR F 1 95  ? -2.027  -26.39  48.683  1 33.38 ? 95  THR Z N     1 
ATOM   7364  C  CA    . THR F 1 95  ? -3.254  -25.741 49.123  1 34    ? 95  THR Z CA    1 
ATOM   7365  C  C     . THR F 1 95  ? -3.066  -24.228 49.24   1 34.83 ? 95  THR Z C     1 
ATOM   7366  O  O     . THR F 1 95  ? -1.944  -23.738 49.35   1 34.81 ? 95  THR Z O     1 
ATOM   7367  C  CB    . THR F 1 95  ? -3.749  -26.335 50.444  1 34.83 ? 95  THR Z CB    1 
ATOM   7368  O  OG1   . THR F 1 95  ? -2.871  -25.93  51.49   1 35.78 ? 95  THR Z OG1   1 
ATOM   7369  C  CG2   . THR F 1 95  ? -3.877  -27.84  50.406  1 35.1  ? 95  THR Z CG2   1 
ATOM   7370  N  N     . SER F 1 96  ? -4.175  -23.497 49.23   1 35.38 ? 96  SER Z N     1 
ATOM   7371  C  CA    . SER F 1 96  ? -4.191  -22.06  49.421  1 36.3  ? 96  SER Z CA    1 
ATOM   7372  C  C     . SER F 1 96  ? -4.881  -21.777 50.759  1 36.72 ? 96  SER Z C     1 
ATOM   7373  O  O     . SER F 1 96  ? -5.873  -22.429 51.085  1 36.61 ? 96  SER Z O     1 
ATOM   7374  C  CB    . SER F 1 96  ? -4.959  -21.389 48.288  1 37.86 ? 96  SER Z CB    1 
ATOM   7375  O  OG    . SER F 1 96  ? -5.084  -19.995 48.521  1 40.48 ? 96  SER Z OG    1 
ATOM   7376  N  N     . LEU F 1 97  ? -4.354  -20.826 51.538  1 37.08 ? 97  LEU Z N     1 
ATOM   7377  C  CA    . LEU F 1 97  ? -4.965  -20.467 52.816  1 38.04 ? 97  LEU Z CA    1 
ATOM   7378  C  C     . LEU F 1 97  ? -5.888  -19.279 52.643  1 38.88 ? 97  LEU Z C     1 
ATOM   7379  O  O     . LEU F 1 97  ? -5.42   -18.171 52.391  1 38.96 ? 97  LEU Z O     1 
ATOM   7380  C  CB    . LEU F 1 97  ? -3.907  -20.117 53.87   1 38.34 ? 97  LEU Z CB    1 
ATOM   7381  C  CG    . LEU F 1 97  ? -3.207  -21.264 54.585  1 39.85 ? 97  LEU Z CG    1 
ATOM   7382  C  CD1   . LEU F 1 97  ? -2.37   -20.741 55.731  1 40.34 ? 97  LEU Z CD1   1 
ATOM   7383  C  CD2   . LEU F 1 97  ? -4.199  -22.244 55.152  1 40.56 ? 97  LEU Z CD2   1 
ATOM   7384  N  N     . ASN F 1 98  ? -7.199  -19.503 52.748  1 39.3  ? 98  ASN Z N     1 
ATOM   7385  C  CA    . ASN F 1 98  ? -8.172  -18.422 52.605  1 40.23 ? 98  ASN Z CA    1 
ATOM   7386  C  C     . ASN F 1 98  ? -9.231  -18.58  53.681  1 40.75 ? 98  ASN Z C     1 
ATOM   7387  O  O     . ASN F 1 98  ? -9.696  -19.692 53.917  1 41.04 ? 98  ASN Z O     1 
ATOM   7388  C  CB    . ASN F 1 98  ? -8.857  -18.431 51.224  1 41.8  ? 98  ASN Z CB    1 
ATOM   7389  C  CG    . ASN F 1 98  ? -7.994  -18.534 49.977  1 45.24 ? 98  ASN Z CG    1 
ATOM   7390  O  OD1   . ASN F 1 98  ? -7.667  -17.544 49.312  1 46.5  ? 98  ASN Z OD1   1 
ATOM   7391  N  ND2   . ASN F 1 98  ? -7.627  -19.749 49.608  1 45.62 ? 98  ASN Z ND2   1 
ATOM   7392  N  N     . ASN F 1 99  ? -9.628  -17.468 54.321  1 40.72 ? 99  ASN Z N     1 
ATOM   7393  C  CA    . ASN F 1 99  ? -10.64  -17.383 55.386  1 40.97 ? 99  ASN Z CA    1 
ATOM   7394  C  C     . ASN F 1 99  ? -10.504 -18.467 56.486  1 40.41 ? 99  ASN Z C     1 
ATOM   7395  O  O     . ASN F 1 99  ? -11.5   -19.069 56.886  1 40.85 ? 99  ASN Z O     1 
ATOM   7396  C  CB    . ASN F 1 99  ? -12.092 -17.322 54.833  1 42.64 ? 99  ASN Z CB    1 
ATOM   7397  C  CG    . ASN F 1 99  ? -12.482 -18.35  53.78   1 46.45 ? 99  ASN Z CG    1 
ATOM   7398  O  OD1   . ASN F 1 99  ? -12.704 -19.527 54.083  1 47.81 ? 99  ASN Z OD1   1 
ATOM   7399  N  ND2   . ASN F 1 99  ? -12.58  -17.927 52.513  1 47.12 ? 99  ASN Z ND2   1 
ATOM   7400  N  N     . GLY F 1 100 ? -9.286  -18.669 56.985  1 39.22 ? 100 GLY Z N     1 
ATOM   7401  C  CA    . GLY F 1 100 ? -9.021  -19.617 58.064  1 38.53 ? 100 GLY Z CA    1 
ATOM   7402  C  C     . GLY F 1 100 ? -9.115  -21.093 57.717  1 37.47 ? 100 GLY Z C     1 
ATOM   7403  O  O     . GLY F 1 100 ? -9.208  -21.934 58.614  1 37.55 ? 100 GLY Z O     1 
ATOM   7404  N  N     . LYS F 1 101 ? -9.075  -21.432 56.424  1 36.31 ? 101 LYS Z N     1 
ATOM   7405  C  CA    . LYS F 1 101 ? -9.142  -22.827 55.989  1 35.53 ? 101 LYS Z CA    1 
ATOM   7406  C  C     . LYS F 1 101 ? -8.268  -23.077 54.742  1 34.41 ? 101 LYS Z C     1 
ATOM   7407  O  O     . LYS F 1 101 ? -7.876  -22.135 54.049  1 34.3  ? 101 LYS Z O     1 
ATOM   7408  C  CB    . LYS F 1 101 ? -10.604 -23.241 55.727  1 37.36 ? 101 LYS Z CB    1 
ATOM   7409  C  CG    . LYS F 1 101 ? -11.184 -22.631 54.455  1 41.64 ? 101 LYS Z CG    1 
ATOM   7410  C  CD    . LYS F 1 101 ? -12.615 -23.05  54.202  1 46.26 ? 101 LYS Z CD    1 
ATOM   7411  C  CE    . LYS F 1 101 ? -13.038 -22.797 52.774  1 50.24 ? 101 LYS Z CE    1 
ATOM   7412  N  NZ    . LYS F 1 101 ? -14.337 -23.444 52.455  1 52.74 ? 101 LYS Z NZ    1 
ATOM   7413  N  N     . GLU F 1 102 ? -7.978  -24.349 54.451  1 33.41 ? 102 GLU Z N     1 
ATOM   7414  C  CA    . GLU F 1 102 ? -7.176  -24.706 53.288  1 32.8  ? 102 GLU Z CA    1 
ATOM   7415  C  C     . GLU F 1 102 ? -8.062  -25.104 52.118  1 32.16 ? 102 GLU Z C     1 
ATOM   7416  O  O     . GLU F 1 102 ? -9.116  -25.712 52.31   1 32.51 ? 102 GLU Z O     1 
ATOM   7417  C  CB    . GLU F 1 102 ? -6.224  -25.86  53.618  1 34.36 ? 102 GLU Z CB    1 
ATOM   7418  C  CG    . GLU F 1 102 ? -5.346  -25.597 54.819  1 37.91 ? 102 GLU Z CG    1 
ATOM   7419  C  CD    . GLU F 1 102 ? -4.198  -26.57  54.938  1 43.23 ? 102 GLU Z CD    1 
ATOM   7420  O  OE1   . GLU F 1 102 ? -3.525  -26.827 53.914  1 43.6  ? 102 GLU Z OE1   1 
ATOM   7421  O  OE2   . GLU F 1 102 ? -3.969  -27.076 56.059  1 45.63 ? 102 GLU Z OE2   1 
ATOM   7422  N  N     . GLU F 1 103 ? -7.631  -24.779 50.9    1 31.05 ? 103 GLU Z N     1 
ATOM   7423  C  CA    . GLU F 1 103 ? -8.368  -25.136 49.697  1 30.53 ? 103 GLU Z CA    1 
ATOM   7424  C  C     . GLU F 1 103 ? -7.377  -25.765 48.729  1 29.98 ? 103 GLU Z C     1 
ATOM   7425  O  O     . GLU F 1 103 ? -6.38   -25.131 48.409  1 30.26 ? 103 GLU Z O     1 
ATOM   7426  C  CB    . GLU F 1 103 ? -9.009  -23.882 49.077  1 32.33 ? 103 GLU Z CB    1 
ATOM   7427  C  CG    . GLU F 1 103 ? -10.166 -23.328 49.892  1 36.3  ? 103 GLU Z CG    1 
ATOM   7428  C  CD    . GLU F 1 103 ? -10.446 -21.849 49.711  1 40.32 ? 103 GLU Z CD    1 
ATOM   7429  O  OE1   . GLU F 1 103 ? -10.828 -21.192 50.707  1 41.26 ? 103 GLU Z OE1   1 
ATOM   7430  O  OE2   . GLU F 1 103 ? -10.276 -21.344 48.578  1 40.85 ? 103 GLU Z OE2   1 
ATOM   7431  N  N     . ILE F 1 104 ? -7.618  -27.007 48.28   1 29.08 ? 104 ILE Z N     1 
ATOM   7432  C  CA    . ILE F 1 104 ? -6.698  -27.676 47.353  1 28.61 ? 104 ILE Z CA    1 
ATOM   7433  C  C     . ILE F 1 104 ? -6.614  -26.974 46.003  1 28.12 ? 104 ILE Z C     1 
ATOM   7434  O  O     . ILE F 1 104 ? -7.64   -26.666 45.404  1 28.08 ? 104 ILE Z O     1 
ATOM   7435  C  CB    . ILE F 1 104 ? -7.028  -29.191 47.199  1 28.8  ? 104 ILE Z CB    1 
ATOM   7436  C  CG1   . ILE F 1 104 ? -6.762  -29.932 48.519  1 29.46 ? 104 ILE Z CG1   1 
ATOM   7437  C  CG2   . ILE F 1 104 ? -6.255  -29.831 46.029  1 29.09 ? 104 ILE Z CG2   1 
ATOM   7438  C  CD1   . ILE F 1 104 ? -7.075  -31.383 48.515  1 30.54 ? 104 ILE Z CD1   1 
ATOM   7439  N  N     . LEU F 1 105 ? -5.386  -26.728 45.531  1 27.74 ? 105 LEU Z N     1 
ATOM   7440  C  CA    . LEU F 1 105 ? -5.121  -26.127 44.227  1 27.95 ? 105 LEU Z CA    1 
ATOM   7441  C  C     . LEU F 1 105 ? -4.796  -27.208 43.205  1 28.1  ? 105 LEU Z C     1 
ATOM   7442  O  O     . LEU F 1 105 ? -5.224  -27.098 42.058  1 28.12 ? 105 LEU Z O     1 
ATOM   7443  C  CB    . LEU F 1 105 ? -3.946  -25.144 44.298  1 28.05 ? 105 LEU Z CB    1 
ATOM   7444  C  CG    . LEU F 1 105 ? -4.148  -23.892 45.115  1 29.22 ? 105 LEU Z CG    1 
ATOM   7445  C  CD1   . LEU F 1 105 ? -2.892  -23.072 45.117  1 29.71 ? 105 LEU Z CD1   1 
ATOM   7446  C  CD2   . LEU F 1 105 ? -5.317  -23.073 44.589  1 29.73 ? 105 LEU Z CD2   1 
ATOM   7447  N  N     . MET F 1 106 ? -4.009  -28.232 43.614  1 28.12 ? 106 MET Z N     1 
ATOM   7448  C  CA    . MET F 1 106 ? -3.607  -29.363 42.768  1 28.58 ? 106 MET Z CA    1 
ATOM   7449  C  C     . MET F 1 106 ? -2.924  -30.495 43.568  1 28.66 ? 106 MET Z C     1 
ATOM   7450  O  O     . MET F 1 106 ? -2.454  -30.277 44.688  1 28.7  ? 106 MET Z O     1 
ATOM   7451  C  CB    . MET F 1 106 ? -2.69   -28.902 41.614  1 29.23 ? 106 MET Z CB    1 
ATOM   7452  C  CG    . MET F 1 106 ? -1.276  -28.596 42.048  1 31.31 ? 106 MET Z CG    1 
ATOM   7453  S  SD    . MET F 1 106 ? -0.369  -27.762 40.744  1 34.48 ? 106 MET Z SD    1 
ATOM   7454  C  CE    . MET F 1 106 ? -1.064  -26.165 40.878  1 32.58 ? 106 MET Z CE    1 
ATOM   7455  N  N     . ALA F 1 107 ? -2.852  -31.692 42.956  1 28.28 ? 107 ALA Z N     1 
ATOM   7456  C  CA    . ALA F 1 107 ? -2.174  -32.873 43.479  1 28.27 ? 107 ALA Z CA    1 
ATOM   7457  C  C     . ALA F 1 107 ? -1.067  -33.222 42.475  1 28.26 ? 107 ALA Z C     1 
ATOM   7458  O  O     . ALA F 1 107 ? -1.302  -33.198 41.268  1 28.3  ? 107 ALA Z O     1 
ATOM   7459  C  CB    . ALA F 1 107 ? -3.151  -34.026 43.598  1 28.33 ? 107 ALA Z CB    1 
ATOM   7460  N  N     . ILE F 1 108 ? 0.15    -33.489 42.961  1 28    ? 108 ILE Z N     1 
ATOM   7461  C  CA    . ILE F 1 108 ? 1.29    -33.781 42.094  1 28.22 ? 108 ILE Z CA    1 
ATOM   7462  C  C     . ILE F 1 108 ? 1.981   -35.093 42.463  1 28.1  ? 108 ILE Z C     1 
ATOM   7463  O  O     . ILE F 1 108 ? 2.174   -35.378 43.645  1 28.24 ? 108 ILE Z O     1 
ATOM   7464  C  CB    . ILE F 1 108 ? 2.3     -32.61  42.152  1 28.99 ? 108 ILE Z CB    1 
ATOM   7465  C  CG1   . ILE F 1 108 ? 1.669   -31.285 41.718  1 29.75 ? 108 ILE Z CG1   1 
ATOM   7466  C  CG2   . ILE F 1 108 ? 3.552   -32.911 41.33   1 29.74 ? 108 ILE Z CG2   1 
ATOM   7467  C  CD1   . ILE F 1 108 ? 2.501   -30.114 42.068  1 30.96 ? 108 ILE Z CD1   1 
ATOM   7468  N  N     . GLU F 1 109 ? 2.366   -35.886 41.452  1 27.66 ? 109 GLU Z N     1 
ATOM   7469  C  CA    . GLU F 1 109 ? 3.06    -37.147 41.662  1 27.71 ? 109 GLU Z CA    1 
ATOM   7470  C  C     . GLU F 1 109 ? 4.322   -37.153 40.81   1 28.51 ? 109 GLU Z C     1 
ATOM   7471  O  O     . GLU F 1 109 ? 4.27    -36.823 39.632  1 28.55 ? 109 GLU Z O     1 
ATOM   7472  C  CB    . GLU F 1 109 ? 2.149   -38.316 41.284  1 28.74 ? 109 GLU Z CB    1 
ATOM   7473  C  CG    . GLU F 1 109 ? 2.823   -39.668 41.362  1 32.71 ? 109 GLU Z CG    1 
ATOM   7474  C  CD    . GLU F 1 109 ? 2.98    -40.218 42.763  1 38.53 ? 109 GLU Z CD    1 
ATOM   7475  O  OE1   . GLU F 1 109 ? 2.19    -39.824 43.649  1 39.96 ? 109 GLU Z OE1   1 
ATOM   7476  O  OE2   . GLU F 1 109 ? 3.887   -41.053 42.973  1 40.3  ? 109 GLU Z OE2   1 
ATOM   7477  N  N     . PHE F 1 110 ? 5.463   -37.477 41.411  1 28.9  ? 110 PHE Z N     1 
ATOM   7478  C  CA    . PHE F 1 110 ? 6.762   -37.524 40.741  1 29.58 ? 110 PHE Z CA    1 
ATOM   7479  C  C     . PHE F 1 110 ? 7.178   -38.976 40.549  1 30.34 ? 110 PHE Z C     1 
ATOM   7480  O  O     . PHE F 1 110 ? 7.27    -39.695 41.538  1 30.55 ? 110 PHE Z O     1 
ATOM   7481  C  CB    . PHE F 1 110 ? 7.819   -36.833 41.616  1 29.35 ? 110 PHE Z CB    1 
ATOM   7482  C  CG    . PHE F 1 110 ? 7.48    -35.444 42.109  1 29.55 ? 110 PHE Z CG    1 
ATOM   7483  C  CD1   . PHE F 1 110 ? 7.203   -34.429 41.221  1 30.33 ? 110 PHE Z CD1   1 
ATOM   7484  C  CD2   . PHE F 1 110 ? 7.468   -35.152 43.459  1 29.74 ? 110 PHE Z CD2   1 
ATOM   7485  C  CE1   . PHE F 1 110 ? 6.933   -33.152 41.672  1 30.71 ? 110 PHE Z CE1   1 
ATOM   7486  C  CE2   . PHE F 1 110 ? 7.213   -33.865 43.904  1 30.24 ? 110 PHE Z CE2   1 
ATOM   7487  C  CZ    . PHE F 1 110 ? 6.947   -32.875 43.008  1 30.14 ? 110 PHE Z CZ    1 
ATOM   7488  N  N     . CYS F 1 111 ? 7.454   -39.412 39.311  1 30.81 ? 111 CYS Z N     1 
ATOM   7489  C  CA    . CYS F 1 111 ? 7.853   -40.8   39.075  1 31.88 ? 111 CYS Z CA    1 
ATOM   7490  C  C     . CYS F 1 111 ? 9.101   -40.942 38.233  1 32.04 ? 111 CYS Z C     1 
ATOM   7491  O  O     . CYS F 1 111 ? 9.07    -40.726 37.027  1 31.93 ? 111 CYS Z O     1 
ATOM   7492  C  CB    . CYS F 1 111 ? 6.705   -41.622 38.498  1 33.36 ? 111 CYS Z CB    1 
ATOM   7493  S  SG    . CYS F 1 111 ? 6.929   -43.422 38.63   1 38.44 ? 111 CYS Z SG    1 
ATOM   7494  N  N     . SER F 1 112 ? 10.182  -41.364 38.868  1 32.12 ? 112 SER Z N     1 
ATOM   7495  C  CA    . SER F 1 112 ? 11.436  -41.628 38.183  1 32.6  ? 112 SER Z CA    1 
ATOM   7496  C  C     . SER F 1 112 ? 11.51   -43.065 37.666  1 32.6  ? 112 SER Z C     1 
ATOM   7497  O  O     . SER F 1 112 ? 12.155  -43.323 36.65   1 32.99 ? 112 SER Z O     1 
ATOM   7498  C  CB    . SER F 1 112 ? 12.61   -41.349 39.108  1 34.46 ? 112 SER Z CB    1 
ATOM   7499  O  OG    . SER F 1 112 ? 13.16   -40.101 38.725  1 37.13 ? 112 SER Z OG    1 
ATOM   7500  N  N     . ALA F 1 113 ? 10.834  -43.995 38.362  1 32.02 ? 113 ALA Z N     1 
ATOM   7501  C  CA    . ALA F 1 113 ? 10.762  -45.427 38.079  1 31.96 ? 113 ALA Z CA    1 
ATOM   7502  C  C     . ALA F 1 113 ? 10.636  -45.824 36.615  1 31.44 ? 113 ALA Z C     1 
ATOM   7503  O  O     . ALA F 1 113 ? 10.025  -45.102 35.827  1 31.64 ? 113 ALA Z O     1 
ATOM   7504  C  CB    . ALA F 1 113 ? 9.613   -46.023 38.853  1 32.24 ? 113 ALA Z CB    1 
ATOM   7505  N  N     . LEU F 1 114 ? 11.176  -47.011 36.26   1 30.62 ? 114 LEU Z N     1 
ATOM   7506  C  CA    . LEU F 1 114 ? 11.094  -47.53  34.889  1 30.2  ? 114 LEU Z CA    1 
ATOM   7507  C  C     . LEU F 1 114 ? 9.652   -47.788 34.56   1 30.22 ? 114 LEU Z C     1 
ATOM   7508  O  O     . LEU F 1 114 ? 8.953   -48.404 35.359  1 30.63 ? 114 LEU Z O     1 
ATOM   7509  C  CB    . LEU F 1 114 ? 11.855  -48.859 34.728  1 29.84 ? 114 LEU Z CB    1 
ATOM   7510  C  CG    . LEU F 1 114 ? 13.337  -48.845 34.959  1 30.77 ? 114 LEU Z CG    1 
ATOM   7511  C  CD1   . LEU F 1 114 ? 13.908  -50.227 34.844  1 31.15 ? 114 LEU Z CD1   1 
ATOM   7512  C  CD2   . LEU F 1 114 ? 14.016  -47.943 33.982  1 31.29 ? 114 LEU Z CD2   1 
ATOM   7513  N  N     . GLN F 1 115 ? 9.192   -47.283 33.426  1 29.76 ? 115 GLN Z N     1 
ATOM   7514  C  CA    . GLN F 1 115 ? 7.827   -47.508 33.001  1 29.73 ? 115 GLN Z CA    1 
ATOM   7515  C  C     . GLN F 1 115 ? 7.862   -48.867 32.324  1 29.06 ? 115 GLN Z C     1 
ATOM   7516  O  O     . GLN F 1 115 ? 7.823   -48.953 31.096  1 29.54 ? 115 GLN Z O     1 
ATOM   7517  C  CB    . GLN F 1 115 ? 7.382   -46.401 32.029  1 31.66 ? 115 GLN Z CB    1 
ATOM   7518  C  CG    . GLN F 1 115 ? 7.605   -44.982 32.568  1 35.31 ? 115 GLN Z CG    1 
ATOM   7519  C  CD    . GLN F 1 115 ? 6.455   -44.496 33.418  1 40.29 ? 115 GLN Z CD    1 
ATOM   7520  O  OE1   . GLN F 1 115 ? 5.427   -44.045 32.902  1 41.93 ? 115 GLN Z OE1   1 
ATOM   7521  N  NE2   . GLN F 1 115 ? 6.605   -44.564 34.743  1 41.13 ? 115 GLN Z NE2   1 
ATOM   7522  N  N     . ALA F 1 116 ? 8.028   -49.928 33.123  1 27.9  ? 116 ALA Z N     1 
ATOM   7523  C  CA    . ALA F 1 116 ? 8.124   -51.283 32.603  1 27.55 ? 116 ALA Z CA    1 
ATOM   7524  C  C     . ALA F 1 116 ? 6.835   -52.036 32.808  1 27.01 ? 116 ALA Z C     1 
ATOM   7525  O  O     . ALA F 1 116 ? 6.549   -52.48  33.912  1 26.81 ? 116 ALA Z O     1 
ATOM   7526  C  CB    . ALA F 1 116 ? 9.264   -52.026 33.271  1 27.56 ? 116 ALA Z CB    1 
ATOM   7527  N  N     . GLY F 1 117 ? 6.063   -52.161 31.744  1 26.64 ? 117 GLY Z N     1 
ATOM   7528  C  CA    . GLY F 1 117 ? 4.804   -52.883 31.773  1 26.65 ? 117 GLY Z CA    1 
ATOM   7529  C  C     . GLY F 1 117 ? 3.791   -52.372 32.761  1 26.28 ? 117 GLY Z C     1 
ATOM   7530  O  O     . GLY F 1 117 ? 3.217   -51.3   32.564  1 26.28 ? 117 GLY Z O     1 
ATOM   7531  N  N     . ASN F 1 118 ? 3.555   -53.147 33.825  1 25.93 ? 118 ASN Z N     1 
ATOM   7532  C  CA    . ASN F 1 118 ? 2.558   -52.772 34.817  1 26.19 ? 118 ASN Z CA    1 
ATOM   7533  C  C     . ASN F 1 118 ? 3.01    -51.667 35.768  1 26.09 ? 118 ASN Z C     1 
ATOM   7534  O  O     . ASN F 1 118 ? 2.174   -51.119 36.481  1 26.22 ? 118 ASN Z O     1 
ATOM   7535  C  CB    . ASN F 1 118 ? 2.031   -53.98  35.58   1 27.75 ? 118 ASN Z CB    1 
ATOM   7536  C  CG    . ASN F 1 118 ? 3.066   -54.759 36.339  1 31.63 ? 118 ASN Z CG    1 
ATOM   7537  O  OD1   . ASN F 1 118 ? 4.21    -54.334 36.497  1 32.92 ? 118 ASN Z OD1   1 
ATOM   7538  N  ND2   . ASN F 1 118 ? 2.673   -55.918 36.851  1 32.45 ? 118 ASN Z ND2   1 
ATOM   7539  N  N     . GLN F 1 119 ? 4.298   -51.31  35.764  1 25.77 ? 119 GLN Z N     1 
ATOM   7540  C  CA    . GLN F 1 119 ? 4.782   -50.21  36.593  1 25.94 ? 119 GLN Z CA    1 
ATOM   7541  C  C     . GLN F 1 119 ? 4.202   -48.862 36.127  1 25.9  ? 119 GLN Z C     1 
ATOM   7542  O  O     . GLN F 1 119 ? 4.026   -47.965 36.949  1 26.07 ? 119 GLN Z O     1 
ATOM   7543  C  CB    . GLN F 1 119 ? 6.309   -50.19  36.618  1 27.6  ? 119 GLN Z CB    1 
ATOM   7544  C  CG    . GLN F 1 119 ? 6.856   -50.17  38.037  1 31.83 ? 119 GLN Z CG    1 
ATOM   7545  C  CD    . GLN F 1 119 ? 6.941   -48.784 38.594  1 37.37 ? 119 GLN Z CD    1 
ATOM   7546  O  OE1   . GLN F 1 119 ? 7.052   -47.802 37.846  1 40.04 ? 119 GLN Z OE1   1 
ATOM   7547  N  NE2   . GLN F 1 119 ? 6.9     -48.665 39.919  1 37.18 ? 119 GLN Z NE2   1 
ATOM   7548  N  N     . ALA F 1 120 ? 3.851   -48.746 34.826  1 25.61 ? 120 ALA Z N     1 
ATOM   7549  C  CA    . ALA F 1 120 ? 3.247   -47.564 34.215  1 25.64 ? 120 ALA Z CA    1 
ATOM   7550  C  C     . ALA F 1 120 ? 1.877   -47.252 34.816  1 25.53 ? 120 ALA Z C     1 
ATOM   7551  O  O     . ALA F 1 120 ? 1.528   -46.083 34.979  1 25.93 ? 120 ALA Z O     1 
ATOM   7552  C  CB    . ALA F 1 120 ? 3.113   -47.769 32.716  1 25.93 ? 120 ALA Z CB    1 
ATOM   7553  N  N     . TRP F 1 121 ? 1.1     -48.29  35.141  1 24.89 ? 121 TRP Z N     1 
ATOM   7554  C  CA    . TRP F 1 121 ? -0.211  -48.09  35.738  1 24.63 ? 121 TRP Z CA    1 
ATOM   7555  C  C     . TRP F 1 121 ? -0.258  -48.394 37.227  1 24.66 ? 121 TRP Z C     1 
ATOM   7556  O  O     . TRP F 1 121 ? -1.334  -48.327 37.802  1 24.73 ? 121 TRP Z O     1 
ATOM   7557  C  CB    . TRP F 1 121 ? -1.314  -48.849 34.99   1 24.39 ? 121 TRP Z CB    1 
ATOM   7558  C  CG    . TRP F 1 121 ? -1.213  -50.348 35      1 24.67 ? 121 TRP Z CG    1 
ATOM   7559  C  CD1   . TRP F 1 121 ? -1.616  -51.193 35.993  1 25.54 ? 121 TRP Z CD1   1 
ATOM   7560  C  CD2   . TRP F 1 121 ? -0.847  -51.18  33.89   1 24.7  ? 121 TRP Z CD2   1 
ATOM   7561  N  NE1   . TRP F 1 121 ? -1.456  -52.503 35.595  1 25.75 ? 121 TRP Z NE1   1 
ATOM   7562  C  CE2   . TRP F 1 121 ? -1      -52.521 34.301  1 25.4  ? 121 TRP Z CE2   1 
ATOM   7563  C  CE3   . TRP F 1 121 ? -0.364  -50.924 32.604  1 25.03 ? 121 TRP Z CE3   1 
ATOM   7564  C  CZ2   . TRP F 1 121 ? -0.709  -53.592 33.46   1 25.83 ? 121 TRP Z CZ2   1 
ATOM   7565  C  CZ3   . TRP F 1 121 ? -0.074  -51.985 31.777  1 25.67 ? 121 TRP Z CZ3   1 
ATOM   7566  C  CH2   . TRP F 1 121 ? -0.225  -53.299 32.213  1 25.81 ? 121 TRP Z CH2   1 
ATOM   7567  N  N     . GLN F 1 122 ? 0.884   -48.654 37.884  1 24.55 ? 122 GLN Z N     1 
ATOM   7568  C  CA    . GLN F 1 122 ? 0.909   -48.934 39.319  1 25.27 ? 122 GLN Z CA    1 
ATOM   7569  C  C     . GLN F 1 122 ? 0.266   -47.801 40.119  1 26.31 ? 122 GLN Z C     1 
ATOM   7570  O  O     . GLN F 1 122 ? -0.513  -48.054 41.044  1 27.05 ? 122 GLN Z O     1 
ATOM   7571  C  CB    . GLN F 1 122 ? 2.348   -49.178 39.804  1 26.51 ? 122 GLN Z CB    1 
ATOM   7572  C  CG    . GLN F 1 122 ? 2.442   -49.403 41.315  1 29.38 ? 122 GLN Z CG    1 
ATOM   7573  C  CD    . GLN F 1 122 ? 3.807   -49.83  41.769  1 34.1  ? 122 GLN Z CD    1 
ATOM   7574  O  OE1   . GLN F 1 122 ? 4.118   -51.018 41.823  1 36.64 ? 122 GLN Z OE1   1 
ATOM   7575  N  NE2   . GLN F 1 122 ? 4.651   -48.876 42.12   1 34.08 ? 122 GLN Z NE2   1 
ATOM   7576  N  N     . ARG F 1 123 ? 0.552   -46.551 39.719  1 26.18 ? 123 ARG Z N     1 
ATOM   7577  C  CA    . ARG F 1 123 ? -0.018  -45.395 40.399  1 26.43 ? 123 ARG Z CA    1 
ATOM   7578  C  C     . ARG F 1 123 ? -1.115  -44.714 39.584  1 26.74 ? 123 ARG Z C     1 
ATOM   7579  O  O     . ARG F 1 123 ? -1.286  -43.498 39.662  1 26.79 ? 123 ARG Z O     1 
ATOM   7580  C  CB    . ARG F 1 123 ? 1.039   -44.397 40.887  1 27.28 ? 123 ARG Z CB    1 
ATOM   7581  C  CG    . ARG F 1 123 ? 2.282   -44.251 40.045  1 29.79 ? 123 ARG Z CG    1 
ATOM   7582  C  CD    . ARG F 1 123 ? 3.406   -43.738 40.952  1 32.35 ? 123 ARG Z CD    1 
ATOM   7583  N  NE    . ARG F 1 123 ? 4.367   -44.804 40.939  1 34.71 ? 123 ARG Z NE    1 
ATOM   7584  C  CZ    . ARG F 1 123 ? 5.583   -44.871 41.46   1 36.89 ? 123 ARG Z CZ    1 
ATOM   7585  N  NH1   . ARG F 1 123 ? 6.317   -45.963 41.291  1 36.2  ? 123 ARG Z NH1   1 
ATOM   7586  N  NH2   . ARG F 1 123 ? 6.068   -43.865 42.173  1 37.17 ? 123 ARG Z NH2   1 
ATOM   7587  N  N     . SER F 1 124 ? -1.886  -45.505 38.825  1 26.7  ? 124 SER Z N     1 
ATOM   7588  C  CA    . SER F 1 124 ? -3.041  -44.97  38.112  1 27.28 ? 124 SER Z CA    1 
ATOM   7589  C  C     . SER F 1 124 ? -4.247  -44.786 39.063  1 27.67 ? 124 SER Z C     1 
ATOM   7590  O  O     . SER F 1 124 ? -5.128  -43.987 38.77   1 27.99 ? 124 SER Z O     1 
ATOM   7591  C  CB    . SER F 1 124 ? -3.414  -45.841 36.921  1 28.81 ? 124 SER Z CB    1 
ATOM   7592  O  OG    . SER F 1 124 ? -2.572  -45.55  35.817  1 31.83 ? 124 SER Z OG    1 
ATOM   7593  N  N     . GLY F 1 125 ? -4.259  -45.482 40.2    1 27.35 ? 125 GLY Z N     1 
ATOM   7594  C  CA    . GLY F 1 125 ? -5.315  -45.348 41.185  1 27.82 ? 125 GLY Z CA    1 
ATOM   7595  C  C     . GLY F 1 125 ? -5.423  -43.939 41.727  1 28.13 ? 125 GLY Z C     1 
ATOM   7596  O  O     . GLY F 1 125 ? -6.534  -43.424 41.874  1 28.21 ? 125 GLY Z O     1 
ATOM   7597  N  N     . ARG F 1 126 ? -4.274  -43.288 41.992  1 28.12 ? 126 ARG Z N     1 
ATOM   7598  C  CA    . ARG F 1 126 ? -4.316  -41.914 42.483  1 28.64 ? 126 ARG Z CA    1 
ATOM   7599  C  C     . ARG F 1 126 ? -4.783  -40.982 41.4    1 29.18 ? 126 ARG Z C     1 
ATOM   7600  O  O     . ARG F 1 126 ? -5.571  -40.102 41.687  1 29.27 ? 126 ARG Z O     1 
ATOM   7601  C  CB    . ARG F 1 126 ? -3.019  -41.439 43.15   1 29.56 ? 126 ARG Z CB    1 
ATOM   7602  C  CG    . ARG F 1 126 ? -1.748  -41.786 42.417  1 31.27 ? 126 ARG Z CG    1 
ATOM   7603  C  CD    . ARG F 1 126 ? -0.559  -41.706 43.354  1 32.62 ? 126 ARG Z CD    1 
ATOM   7604  N  NE    . ARG F 1 126 ? -0.536  -42.865 44.24   1 33.52 ? 126 ARG Z NE    1 
ATOM   7605  C  CZ    . ARG F 1 126 ? 0.54    -43.596 44.507  1 34.15 ? 126 ARG Z CZ    1 
ATOM   7606  N  NH1   . ARG F 1 126 ? 1.722   -43.248 44.024  1 33.46 ? 126 ARG Z NH1   1 
ATOM   7607  N  NH2   . ARG F 1 126 ? 0.449   -44.655 45.295  1 33.78 ? 126 ARG Z NH2   1 
ATOM   7608  N  N     . ALA F 1 127 ? -4.382  -41.21  40.149  1 29.54 ? 127 ALA Z N     1 
ATOM   7609  C  CA    . ALA F 1 127 ? -4.839  -40.381 39.036  1 30.45 ? 127 ALA Z CA    1 
ATOM   7610  C  C     . ALA F 1 127 ? -6.355  -40.502 38.863  1 30.89 ? 127 ALA Z C     1 
ATOM   7611  O  O     . ALA F 1 127 ? -7.033  -39.495 38.663  1 31.06 ? 127 ALA Z O     1 
ATOM   7612  C  CB    . ALA F 1 127 ? -4.13   -40.785 37.752  1 30.68 ? 127 ALA Z CB    1 
ATOM   7613  N  N     . TYR F 1 128 ? -6.887  -41.724 38.984  1 30.73 ? 128 TYR Z N     1 
ATOM   7614  C  CA    . TYR F 1 128 ? -8.316  -41.951 38.847  1 30.9  ? 128 TYR Z CA    1 
ATOM   7615  C  C     . TYR F 1 128 ? -9.1    -41.314 40.007  1 31.15 ? 128 TYR Z C     1 
ATOM   7616  O  O     . TYR F 1 128 ? -10.037 -40.552 39.767  1 31.49 ? 128 TYR Z O     1 
ATOM   7617  C  CB    . TYR F 1 128 ? -8.619  -43.462 38.721  1 30.7  ? 128 TYR Z CB    1 
ATOM   7618  C  CG    . TYR F 1 128 ? -10.073 -43.783 38.964  1 31.18 ? 128 TYR Z CG    1 
ATOM   7619  C  CD1   . TYR F 1 128 ? -11.044 -43.436 38.038  1 31.96 ? 128 TYR Z CD1   1 
ATOM   7620  C  CD2   . TYR F 1 128 ? -10.491 -44.327 40.169  1 32.12 ? 128 TYR Z CD2   1 
ATOM   7621  C  CE1   . TYR F 1 128 ? -12.389 -43.654 38.289  1 32.81 ? 128 TYR Z CE1   1 
ATOM   7622  C  CE2   . TYR F 1 128 ? -11.833 -44.535 40.438  1 33    ? 128 TYR Z CE2   1 
ATOM   7623  C  CZ    . TYR F 1 128 ? -12.78  -44.207 39.491  1 33.83 ? 128 TYR Z CZ    1 
ATOM   7624  O  OH    . TYR F 1 128 ? -14.106 -44.439 39.748  1 35.37 ? 128 TYR Z OH    1 
ATOM   7625  N  N     . SER F 1 129 ? -8.744  -41.667 41.249  1 30.77 ? 129 SER Z N     1 
ATOM   7626  C  CA    . SER F 1 129 ? -9.449  -41.203 42.435  1 30.89 ? 129 SER Z CA    1 
ATOM   7627  C  C     . SER F 1 129 ? -9.373  -39.699 42.613  1 30.43 ? 129 SER Z C     1 
ATOM   7628  O  O     . SER F 1 129 ? -10.401 -39.075 42.838  1 30.44 ? 129 SER Z O     1 
ATOM   7629  C  CB    . SER F 1 129 ? -8.961  -41.938 43.679  1 32.5  ? 129 SER Z CB    1 
ATOM   7630  O  OG    . SER F 1 129 ? -7.573  -41.744 43.894  1 35.12 ? 129 SER Z OG    1 
ATOM   7631  N  N     . VAL F 1 130 ? -8.176  -39.111 42.487  1 29.87 ? 130 VAL Z N     1 
ATOM   7632  C  CA    . VAL F 1 130 ? -8.014  -37.661 42.602  1 29.69 ? 130 VAL Z CA    1 
ATOM   7633  C  C     . VAL F 1 130 ? -8.657  -36.952 41.406  1 29.53 ? 130 VAL Z C     1 
ATOM   7634  O  O     . VAL F 1 130 ? -9.308  -35.927 41.577  1 29.75 ? 130 VAL Z O     1 
ATOM   7635  C  CB    . VAL F 1 130 ? -6.537  -37.249 42.805  1 30.24 ? 130 VAL Z CB    1 
ATOM   7636  C  CG1   . VAL F 1 130 ? -6.377  -35.738 42.8    1 30.88 ? 130 VAL Z CG1   1 
ATOM   7637  C  CG2   . VAL F 1 130 ? -5.983  -37.839 44.093  1 30.74 ? 130 VAL Z CG2   1 
ATOM   7638  N  N     . GLY F 1 131 ? -8.531  -37.534 40.221  1 29.04 ? 131 GLY Z N     1 
ATOM   7639  C  CA    . GLY F 1 131 ? -9.123  -36.979 39.013  1 29.05 ? 131 GLY Z CA    1 
ATOM   7640  C  C     . GLY F 1 131 ? -10.63  -36.816 39.045  1 28.9  ? 131 GLY Z C     1 
ATOM   7641  O  O     . GLY F 1 131 ? -11.15  -35.861 38.469  1 28.86 ? 131 GLY Z O     1 
ATOM   7642  N  N     . ARG F 1 132 ? -11.356 -37.715 39.742  1 28.62 ? 132 ARG Z N     1 
ATOM   7643  C  CA    . ARG F 1 132 ? -12.819 -37.612 39.822  1 28.55 ? 132 ARG Z CA    1 
ATOM   7644  C  C     . ARG F 1 132 ? -13.317 -36.582 40.874  1 28.61 ? 132 ARG Z C     1 
ATOM   7645  O  O     . ARG F 1 132 ? -14.522 -36.396 41.013  1 28.75 ? 132 ARG Z O     1 
ATOM   7646  C  CB    . ARG F 1 132 ? -13.471 -38.997 40.028  1 29.1  ? 132 ARG Z CB    1 
ATOM   7647  C  CG    . ARG F 1 132 ? -13.342 -39.548 41.436  1 31.08 ? 132 ARG Z CG    1 
ATOM   7648  C  CD    . ARG F 1 132 ? -13.686 -41.027 41.529  1 33.42 ? 132 ARG Z CD    1 
ATOM   7649  N  NE    . ARG F 1 132 ? -15.043 -41.334 41.075  1 35.03 ? 132 ARG Z NE    1 
ATOM   7650  C  CZ    . ARG F 1 132 ? -16.125 -41.275 41.843  1 35.8  ? 132 ARG Z CZ    1 
ATOM   7651  N  NH1   . ARG F 1 132 ? -17.315 -41.584 41.346  1 35.01 ? 132 ARG Z NH1   1 
ATOM   7652  N  NH2   . ARG F 1 132 ? -16.029 -40.898 43.111  1 35.26 ? 132 ARG Z NH2   1 
ATOM   7653  N  N     . THR F 1 133 ? -12.402 -35.891 41.577  1 28.38 ? 133 THR Z N     1 
ATOM   7654  C  CA    . THR F 1 133 ? -12.762 -34.898 42.592  1 28.69 ? 133 THR Z CA    1 
ATOM   7655  C  C     . THR F 1 133 ? -12.951 -33.474 42.053  1 29.3  ? 133 THR Z C     1 
ATOM   7656  O  O     . THR F 1 133 ? -13.533 -32.634 42.741  1 29.85 ? 133 THR Z O     1 
ATOM   7657  C  CB    . THR F 1 133 ? -11.671 -34.83  43.668  1 29.58 ? 133 THR Z CB    1 
ATOM   7658  O  OG1   . THR F 1 133 ? -10.445 -34.368 43.094  1 30.52 ? 133 THR Z OG1   1 
ATOM   7659  C  CG2   . THR F 1 133 ? -11.445 -36.144 44.335  1 29.84 ? 133 THR Z CG2   1 
ATOM   7660  N  N     . GLY F 1 134 ? -12.393 -33.185 40.888  1 28.96 ? 134 GLY Z N     1 
ATOM   7661  C  CA    . GLY F 1 134 ? -12.415 -31.832 40.352  1 29.26 ? 134 GLY Z CA    1 
ATOM   7662  C  C     . GLY F 1 134 ? -11.132 -31.066 40.643  1 29.56 ? 134 GLY Z C     1 
ATOM   7663  O  O     . GLY F 1 134 ? -10.918 -29.987 40.087  1 29.78 ? 134 GLY Z O     1 
ATOM   7664  N  N     . TYR F 1 135 ? -10.246 -31.62  41.494  1 29.45 ? 135 TYR Z N     1 
ATOM   7665  C  CA    . TYR F 1 135 ? -8.957  -31.011 41.797  1 29.98 ? 135 TYR Z CA    1 
ATOM   7666  C  C     . TYR F 1 135 ? -7.932  -31.534 40.787  1 29.98 ? 135 TYR Z C     1 
ATOM   7667  O  O     . TYR F 1 135 ? -7.877  -32.735 40.52   1 30.13 ? 135 TYR Z O     1 
ATOM   7668  C  CB    . TYR F 1 135 ? -8.508  -31.343 43.226  1 30.33 ? 135 TYR Z CB    1 
ATOM   7669  C  CG    . TYR F 1 135 ? -9.421  -30.788 44.296  1 31.55 ? 135 TYR Z CG    1 
ATOM   7670  C  CD1   . TYR F 1 135 ? -9.648  -29.425 44.404  1 32.64 ? 135 TYR Z CD1   1 
ATOM   7671  C  CD2   . TYR F 1 135 ? -10.016 -31.623 45.232  1 32.68 ? 135 TYR Z CD2   1 
ATOM   7672  C  CE1   . TYR F 1 135 ? -10.482 -28.908 45.386  1 33.72 ? 135 TYR Z CE1   1 
ATOM   7673  C  CE2   . TYR F 1 135 ? -10.84  -31.118 46.228  1 33.73 ? 135 TYR Z CE2   1 
ATOM   7674  C  CZ    . TYR F 1 135 ? -11.072 -29.757 46.303  1 34.86 ? 135 TYR Z CZ    1 
ATOM   7675  O  OH    . TYR F 1 135 ? -11.883 -29.245 47.29   1 36.63 ? 135 TYR Z OH    1 
ATOM   7676  N  N     . PRO F 1 136 ? -7.13   -30.642 40.198  1 29.57 ? 136 PRO Z N     1 
ATOM   7677  C  CA    . PRO F 1 136 ? -6.175  -31.076 39.171  1 29.42 ? 136 PRO Z CA    1 
ATOM   7678  C  C     . PRO F 1 136 ? -5.136  -32.078 39.627  1 29.06 ? 136 PRO Z C     1 
ATOM   7679  O  O     . PRO F 1 136 ? -4.668  -32.034 40.756  1 28.7  ? 136 PRO Z O     1 
ATOM   7680  C  CB    . PRO F 1 136 ? -5.515  -29.772 38.728  1 30.34 ? 136 PRO Z CB    1 
ATOM   7681  C  CG    . PRO F 1 136 ? -6.471  -28.707 39.12   1 30.78 ? 136 PRO Z CG    1 
ATOM   7682  C  CD    . PRO F 1 136 ? -7.102  -29.183 40.381  1 29.06 ? 136 PRO Z CD    1 
ATOM   7683  N  N     . TYR F 1 137 ? -4.762  -32.97  38.719  1 29.1  ? 137 TYR Z N     1 
ATOM   7684  C  CA    . TYR F 1 137 ? -3.794  -34.014 39.001  1 29.68 ? 137 TYR Z CA    1 
ATOM   7685  C  C     . TYR F 1 137 ? -2.668  -33.977 37.967  1 30.27 ? 137 TYR Z C     1 
ATOM   7686  O  O     . TYR F 1 137 ? -2.922  -34.119 36.774  1 30.52 ? 137 TYR Z O     1 
ATOM   7687  C  CB    . TYR F 1 137 ? -4.492  -35.385 39.021  1 29.52 ? 137 TYR Z CB    1 
ATOM   7688  C  CG    . TYR F 1 137 ? -3.567  -36.493 39.448  1 30.1  ? 137 TYR Z CG    1 
ATOM   7689  C  CD1   . TYR F 1 137 ? -3.39   -36.798 40.787  1 30.89 ? 137 TYR Z CD1   1 
ATOM   7690  C  CD2   . TYR F 1 137 ? -2.827  -37.204 38.516  1 31    ? 137 TYR Z CD2   1 
ATOM   7691  C  CE1   . TYR F 1 137 ? -2.511  -37.792 41.189  1 31.76 ? 137 TYR Z CE1   1 
ATOM   7692  C  CE2   . TYR F 1 137 ? -1.927  -38.183 38.906  1 31.88 ? 137 TYR Z CE2   1 
ATOM   7693  C  CZ    . TYR F 1 137 ? -1.788  -38.488 40.244  1 32.73 ? 137 TYR Z CZ    1 
ATOM   7694  O  OH    . TYR F 1 137 ? -0.906  -39.455 40.635  1 34.43 ? 137 TYR Z OH    1 
ATOM   7695  N  N     . ILE F 1 138 ? -1.422  -33.785 38.423  1 30.37 ? 138 ILE Z N     1 
ATOM   7696  C  CA    . ILE F 1 138 ? -0.259  -33.69  37.539  1 30.91 ? 138 ILE Z CA    1 
ATOM   7697  C  C     . ILE F 1 138 ? 0.719   -34.825 37.809  1 31.58 ? 138 ILE Z C     1 
ATOM   7698  O  O     . ILE F 1 138 ? 1.259   -34.928 38.905  1 31.51 ? 138 ILE Z O     1 
ATOM   7699  C  CB    . ILE F 1 138 ? 0.451   -32.326 37.707  1 31.41 ? 138 ILE Z CB    1 
ATOM   7700  C  CG1   . ILE F 1 138 ? -0.535  -31.136 37.719  1 32.41 ? 138 ILE Z CG1   1 
ATOM   7701  C  CG2   . ILE F 1 138 ? 1.54    -32.152 36.666  1 31.82 ? 138 ILE Z CG2   1 
ATOM   7702  C  CD1   . ILE F 1 138 ? -1.351  -31.01  36.515  1 33.67 ? 138 ILE Z CD1   1 
ATOM   7703  N  N     . TYR F 1 139 ? 0.966   -35.663 36.811  1 32.15 ? 139 TYR Z N     1 
ATOM   7704  C  CA    . TYR F 1 139 ? 1.877   -36.793 36.947  1 33.06 ? 139 TYR Z CA    1 
ATOM   7705  C  C     . TYR F 1 139 ? 3.146   -36.502 36.164  1 33.52 ? 139 TYR Z C     1 
ATOM   7706  O  O     . TYR F 1 139 ? 3.129   -36.556 34.943  1 33.6  ? 139 TYR Z O     1 
ATOM   7707  C  CB    . TYR F 1 139 ? 1.186   -38.051 36.417  1 33.42 ? 139 TYR Z CB    1 
ATOM   7708  C  CG    . TYR F 1 139 ? 1.964   -39.338 36.58   1 34.57 ? 139 TYR Z CG    1 
ATOM   7709  C  CD1   . TYR F 1 139 ? 2.649   -39.619 37.754  1 35.52 ? 139 TYR Z CD1   1 
ATOM   7710  C  CD2   . TYR F 1 139 ? 1.941   -40.31  35.597  1 35.65 ? 139 TYR Z CD2   1 
ATOM   7711  C  CE1   . TYR F 1 139 ? 3.327   -40.82  37.921  1 36.48 ? 139 TYR Z CE1   1 
ATOM   7712  C  CE2   . TYR F 1 139 ? 2.618   -41.51  35.749  1 36.73 ? 139 TYR Z CE2   1 
ATOM   7713  C  CZ    . TYR F 1 139 ? 3.323   -41.759 36.906  1 37.68 ? 139 TYR Z CZ    1 
ATOM   7714  O  OH    . TYR F 1 139 ? 3.99    -42.958 37.022  1 39.46 ? 139 TYR Z OH    1 
ATOM   7715  N  N     . ILE F 1 140 ? 4.234   -36.162 36.863  1 33.67 ? 140 ILE Z N     1 
ATOM   7716  C  CA    . ILE F 1 140 ? 5.521   -35.815 36.255  1 34.18 ? 140 ILE Z CA    1 
ATOM   7717  C  C     . ILE F 1 140 ? 6.428   -37.055 36.205  1 34.82 ? 140 ILE Z C     1 
ATOM   7718  O  O     . ILE F 1 140 ? 6.744   -37.616 37.248  1 35.01 ? 140 ILE Z O     1 
ATOM   7719  C  CB    . ILE F 1 140 ? 6.168   -34.655 37.058  1 34.48 ? 140 ILE Z CB    1 
ATOM   7720  C  CG1   . ILE F 1 140 ? 5.209   -33.458 37.205  1 34.95 ? 140 ILE Z CG1   1 
ATOM   7721  C  CG2   . ILE F 1 140 ? 7.485   -34.233 36.435  1 35.04 ? 140 ILE Z CG2   1 
ATOM   7722  C  CD1   . ILE F 1 140 ? 5.633   -32.472 38.228  1 35.77 ? 140 ILE Z CD1   1 
ATOM   7723  N  N     . VAL F 1 141 ? 6.829   -37.493 34.998  1 35.02 ? 141 VAL Z N     1 
ATOM   7724  C  CA    . VAL F 1 141 ? 7.645   -38.699 34.817  1 35.64 ? 141 VAL Z CA    1 
ATOM   7725  C  C     . VAL F 1 141 ? 8.899   -38.445 33.962  1 36.24 ? 141 VAL Z C     1 
ATOM   7726  O  O     . VAL F 1 141 ? 8.811   -37.843 32.897  1 36.53 ? 141 VAL Z O     1 
ATOM   7727  C  CB    . VAL F 1 141 ? 6.798   -39.894 34.287  1 36.34 ? 141 VAL Z CB    1 
ATOM   7728  C  CG1   . VAL F 1 141 ? 5.839   -39.475 33.181  1 36.8  ? 141 VAL Z CG1   1 
ATOM   7729  C  CG2   . VAL F 1 141 ? 7.67    -41.054 33.829  1 37.02 ? 141 VAL Z CG2   1 
ATOM   7730  N  N     . ASP F 1 142 ? 10.063  -38.907 34.448  1 36.5  ? 142 ASP Z N     1 
ATOM   7731  C  CA    . ASP F 1 142 ? 11.373  -38.788 33.806  1 37.57 ? 142 ASP Z CA    1 
ATOM   7732  C  C     . ASP F 1 142 ? 11.439  -39.611 32.524  1 38.63 ? 142 ASP Z C     1 
ATOM   7733  O  O     . ASP F 1 142 ? 11.211  -40.815 32.566  1 38.98 ? 142 ASP Z O     1 
ATOM   7734  C  CB    . ASP F 1 142 ? 12.444  -39.325 34.765  1 39.08 ? 142 ASP Z CB    1 
ATOM   7735  C  CG    . ASP F 1 142 ? 13.675  -38.466 34.924  1 43.35 ? 142 ASP Z CG    1 
ATOM   7736  O  OD1   . ASP F 1 142 ? 13.522  -37.259 35.238  1 44.04 ? 142 ASP Z OD1   1 
ATOM   7737  O  OD2   . ASP F 1 142 ? 14.796  -39.01  34.784  1 45.09 ? 142 ASP Z OD2   1 
ATOM   7738  N  N     . PHE F 1 143 ? 11.785  -38.982 31.401  1 39.1  ? 143 PHE Z N     1 
ATOM   7739  C  CA    . PHE F 1 143 ? 11.917  -39.665 30.116  1 40.22 ? 143 PHE Z CA    1 
ATOM   7740  C  C     . PHE F 1 143 ? 13.346  -39.394 29.627  1 41.48 ? 143 PHE Z C     1 
ATOM   7741  O  O     . PHE F 1 143 ? 13.642  -38.239 29.316  1 41.57 ? 143 PHE Z O     1 
ATOM   7742  C  CB    . PHE F 1 143 ? 10.889  -39.081 29.119  1 40.1  ? 143 PHE Z CB    1 
ATOM   7743  C  CG    . PHE F 1 143 ? 10.846  -39.763 27.769  1 40.83 ? 143 PHE Z CG    1 
ATOM   7744  C  CD1   . PHE F 1 143 ? 11.712  -39.388 26.753  1 41.63 ? 143 PHE Z CD1   1 
ATOM   7745  C  CD2   . PHE F 1 143 ? 9.94    -40.775 27.515  1 41.56 ? 143 PHE Z CD2   1 
ATOM   7746  C  CE1   . PHE F 1 143 ? 11.706  -40.049 25.533  1 42.2  ? 143 PHE Z CE1   1 
ATOM   7747  C  CE2   . PHE F 1 143 ? 9.922   -41.417 26.283  1 42.17 ? 143 PHE Z CE2   1 
ATOM   7748  C  CZ    . PHE F 1 143 ? 10.803  -41.048 25.301  1 41.94 ? 143 PHE Z CZ    1 
ATOM   7749  N  N     . VAL F 1 144 ? 14.262  -40.39  29.594  1 42.18 ? 144 VAL Z N     1 
ATOM   7750  C  CA    . VAL F 1 144 ? 14.103  -41.81  29.925  1 43.36 ? 144 VAL Z CA    1 
ATOM   7751  C  C     . VAL F 1 144 ? 15.186  -42.263 30.93   1 44.37 ? 144 VAL Z C     1 
ATOM   7752  O  O     . VAL F 1 144 ? 16.172  -41.558 31.145  1 44.27 ? 144 VAL Z O     1 
ATOM   7753  C  CB    . VAL F 1 144 ? 14.255  -42.672 28.638  1 44.47 ? 144 VAL Z CB    1 
ATOM   7754  C  CG1   . VAL F 1 144 ? 13.043  -42.583 27.743  1 45.27 ? 144 VAL Z CG1   1 
ATOM   7755  C  CG2   . VAL F 1 144 ? 15.538  -42.337 27.882  1 45.02 ? 144 VAL Z CG2   1 
ATOM   7756  N  N     . LYS F 1 145 ? 15.026  -43.478 31.491  1 45.25 ? 145 LYS Z N     1 
ATOM   7757  C  CA    . LYS F 1 145 ? 15.994  -44.125 32.366  1 46.64 ? 145 LYS Z CA    1 
ATOM   7758  C  C     . LYS F 1 145 ? 16.182  -45.57  31.867  1 47.81 ? 145 LYS Z C     1 
ATOM   7759  O  O     . LYS F 1 145 ? 15.219  -46.198 31.445  1 47.87 ? 145 LYS Z O     1 
ATOM   7760  C  CB    . LYS F 1 145 ? 15.52   -44.084 33.833  1 48.7  ? 145 LYS Z CB    1 
ATOM   7761  C  CG    . LYS F 1 145 ? 16.576  -44.549 34.831  1 53    ? 145 LYS Z CG    1 
ATOM   7762  C  CD    . LYS F 1 145 ? 16.23   -44.148 36.261  1 57.35 ? 145 LYS Z CD    1 
ATOM   7763  C  CE    . LYS F 1 145 ? 15.108  -44.931 36.844  1 60.76 ? 145 LYS Z CE    1 
ATOM   7764  N  NZ    . LYS F 1 145 ? 15.429  -46.378 36.862  1 63.28 ? 145 LYS Z NZ    1 
ATOM   7765  N  N     . TYR F 1 146 ? 17.414  -46.078 31.863  1 48.66 ? 146 TYR Z N     1 
ATOM   7766  C  CA    . TYR F 1 146 ? 17.693  -47.439 31.396  1 49.99 ? 146 TYR Z CA    1 
ATOM   7767  C  C     . TYR F 1 146 ? 17.584  -48.469 32.502  1 51.14 ? 146 TYR Z C     1 
ATOM   7768  O  O     . TYR F 1 146 ? 17.87   -48.174 33.668  1 51.34 ? 146 TYR Z O     1 
ATOM   7769  C  CB    . TYR F 1 146 ? 19.118  -47.537 30.83   1 50.22 ? 146 TYR Z CB    1 
ATOM   7770  C  CG    . TYR F 1 146 ? 19.278  -46.974 29.44   1 51.28 ? 146 TYR Z CG    1 
ATOM   7771  C  CD1   . TYR F 1 146 ? 19.445  -45.613 29.236  1 52.29 ? 146 TYR Z CD1   1 
ATOM   7772  C  CD2   . TYR F 1 146 ? 19.33   -47.808 28.333  1 52.21 ? 146 TYR Z CD2   1 
ATOM   7773  C  CE1   . TYR F 1 146 ? 19.604  -45.09  27.96   1 53.22 ? 146 TYR Z CE1   1 
ATOM   7774  C  CE2   . TYR F 1 146 ? 19.498  -47.298 27.052  1 53.09 ? 146 TYR Z CE2   1 
ATOM   7775  C  CZ    . TYR F 1 146 ? 19.633  -45.936 26.869  1 54.02 ? 146 TYR Z CZ    1 
ATOM   7776  O  OH    . TYR F 1 146 ? 19.806  -45.42  25.608  1 55.4  ? 146 TYR Z OH    1 
ATOM   7777  N  N     . GLU F 1 147 ? 17.233  -49.706 32.122  1 51.72 ? 147 GLU Z N     1 
ATOM   7778  C  CA    . GLU F 1 147 ? 17.22   -50.822 33.059  1 52.69 ? 147 GLU Z CA    1 
ATOM   7779  C  C     . GLU F 1 147 ? 18.635  -51.398 33.077  1 53.05 ? 147 GLU Z C     1 
ATOM   7780  O  O     . GLU F 1 147 ? 19.287  -51.457 32.035  1 53.25 ? 147 GLU Z O     1 
ATOM   7781  C  CB    . GLU F 1 147 ? 16.249  -51.928 32.607  1 55.31 ? 147 GLU Z CB    1 
ATOM   7782  C  CG    . GLU F 1 147 ? 16.061  -53.019 33.653  1 60.11 ? 147 GLU Z CG    1 
ATOM   7783  C  CD    . GLU F 1 147 ? 15.823  -54.421 33.128  1 65.61 ? 147 GLU Z CD    1 
ATOM   7784  O  OE1   . GLU F 1 147 ? 15.843  -55.374 33.941  1 66.5  ? 147 GLU Z OE1   1 
ATOM   7785  O  OE2   . GLU F 1 147 ? 15.624  -54.569 31.901  1 67.58 ? 147 GLU Z OE2   1 
ATOM   7786  N  N     . LEU F 1 148 ? 19.109  -51.824 34.244  1 52.95 ? 148 LEU Z N     1 
ATOM   7787  C  CA    . LEU F 1 148 ? 20.431  -52.424 34.353  1 53.39 ? 148 LEU Z CA    1 
ATOM   7788  C  C     . LEU F 1 148 ? 20.325  -53.932 34.608  1 53.98 ? 148 LEU Z C     1 
ATOM   7789  O  O     . LEU F 1 148 ? 19.303  -54.406 35.109  1 54.37 ? 148 LEU Z O     1 
ATOM   7790  C  CB    . LEU F 1 148 ? 21.257  -51.711 35.425  1 53.55 ? 148 LEU Z CB    1 
ATOM   7791  C  CG    . LEU F 1 148 ? 21.343  -50.193 35.264  1 55.02 ? 148 LEU Z CG    1 
ATOM   7792  C  CD1   . LEU F 1 148 ? 21.982  -49.551 36.479  1 55.75 ? 148 LEU Z CD1   1 
ATOM   7793  C  CD2   . LEU F 1 148 ? 22.055  -49.808 33.971  1 55.58 ? 148 LEU Z CD2   1 
ATOM   7794  N  N     . ASN F 1 149 ? 21.357  -54.692 34.232  1 54.06 ? 149 ASN Z N     1 
ATOM   7795  C  CA    . ASN F 1 149 ? 21.31   -56.147 34.377  1 54.88 ? 149 ASN Z CA    1 
ATOM   7796  C  C     . ASN F 1 149 ? 21.591  -56.658 35.792  1 55.41 ? 149 ASN Z C     1 
ATOM   7797  O  O     . ASN F 1 149 ? 21.368  -57.841 36.054  1 55.51 ? 149 ASN Z O     1 
ATOM   7798  C  CB    . ASN F 1 149 ? 22.226  -56.828 33.375  1 56.26 ? 149 ASN Z CB    1 
ATOM   7799  C  CG    . ASN F 1 149 ? 23.684  -56.528 33.586  1 59.74 ? 149 ASN Z CG    1 
ATOM   7800  O  OD1   . ASN F 1 149 ? 24.067  -55.641 34.363  1 60.88 ? 149 ASN Z OD1   1 
ATOM   7801  N  ND2   . ASN F 1 149 ? 24.536  -57.253 32.876  1 60.47 ? 149 ASN Z ND2   1 
ATOM   7802  N  N     . ASN F 1 150 ? 22.105  -55.785 36.683  1 55.55 ? 150 ASN Z N     1 
ATOM   7803  C  CA    . ASN F 1 150 ? 22.459  -56.03  38.089  1 56.05 ? 150 ASN Z CA    1 
ATOM   7804  C  C     . ASN F 1 150 ? 23.708  -56.925 38.262  1 55.97 ? 150 ASN Z C     1 
ATOM   7805  O  O     . ASN F 1 150 ? 24.453  -56.715 39.22   1 56.28 ? 150 ASN Z O     1 
ATOM   7806  C  CB    . ASN F 1 150 ? 21.27   -56.517 38.956  1 57.54 ? 150 ASN Z CB    1 
ATOM   7807  C  CG    . ASN F 1 150 ? 20.723  -57.906 38.695  1 61.27 ? 150 ASN Z CG    1 
ATOM   7808  O  OD1   . ASN F 1 150 ? 21.403  -58.916 38.896  1 62.66 ? 150 ASN Z OD1   1 
ATOM   7809  N  ND2   . ASN F 1 150 ? 19.473  -57.99  38.257  1 62.02 ? 150 ASN Z ND2   1 
ATOM   7810  N  N     . SER F 1 151 ? 23.954  -57.885 37.352  1 55.32 ? 151 SER Z N     1 
ATOM   7811  C  CA    . SER F 1 151 ? 25.132  -58.743 37.447  1 55.31 ? 151 SER Z CA    1 
ATOM   7812  C  C     . SER F 1 151 ? 26.404  -57.911 37.273  1 54.99 ? 151 SER Z C     1 
ATOM   7813  O  O     . SER F 1 151 ? 27.346  -58.068 38.047  1 55.13 ? 151 SER Z O     1 
ATOM   7814  C  CB    . SER F 1 151 ? 25.072  -59.864 36.413  1 56.84 ? 151 SER Z CB    1 
ATOM   7815  O  OG    . SER F 1 151 ? 25.156  -59.363 35.089  1 59.3  ? 151 SER Z OG    1 
ATOM   7816  N  N     . ASP F 1 152 ? 26.418  -56.995 36.298  1 54.45 ? 152 ASP Z N     1 
ATOM   7817  C  CA    . ASP F 1 152 ? 27.571  -56.119 36.092  1 54.57 ? 152 ASP Z CA    1 
ATOM   7818  C  C     . ASP F 1 152 ? 27.191  -54.644 35.84   1 54.44 ? 152 ASP Z C     1 
ATOM   7819  O  O     . ASP F 1 152 ? 28.026  -53.865 35.38   1 54.43 ? 152 ASP Z O     1 
ATOM   7820  C  CB    . ASP F 1 152 ? 28.499  -56.655 34.992  1 56.44 ? 152 ASP Z CB    1 
ATOM   7821  C  CG    . ASP F 1 152 ? 27.932  -56.592 33.589  1 60.9  ? 152 ASP Z CG    1 
ATOM   7822  O  OD1   . ASP F 1 152 ? 27.097  -57.461 33.247  1 61.49 ? 152 ASP Z OD1   1 
ATOM   7823  O  OD2   . ASP F 1 152 ? 28.344  -55.691 32.821  1 62.93 ? 152 ASP Z OD2   1 
ATOM   7824  N  N     . ARG F 1 153 ? 25.94   -54.268 36.162  1 54.24 ? 153 ARG Z N     1 
ATOM   7825  C  CA    . ARG F 1 153 ? 25.391  -52.919 36.047  1 54.47 ? 153 ARG Z CA    1 
ATOM   7826  C  C     . ARG F 1 153 ? 25.456  -52.333 34.633  1 54.3  ? 153 ARG Z C     1 
ATOM   7827  O  O     . ARG F 1 153 ? 25.542  -51.117 34.478  1 54.49 ? 153 ARG Z O     1 
ATOM   7828  C  CB    . ARG F 1 153 ? 26.026  -51.966 37.072  1 55.85 ? 153 ARG Z CB    1 
ATOM   7829  C  CG    . ARG F 1 153 ? 25.003  -51.187 37.885  1 58.65 ? 153 ARG Z CG    1 
ATOM   7830  C  CD    . ARG F 1 153 ? 25.663  -50.239 38.865  1 61.69 ? 153 ARG Z CD    1 
ATOM   7831  N  NE    . ARG F 1 153 ? 24.686  -49.432 39.599  1 64.63 ? 153 ARG Z NE    1 
ATOM   7832  C  CZ    . ARG F 1 153 ? 24.319  -48.2   39.256  1 66.9  ? 153 ARG Z CZ    1 
ATOM   7833  N  NH1   . ARG F 1 153 ? 24.842  -47.617 38.183  1 66.71 ? 153 ARG Z NH1   1 
ATOM   7834  N  NH2   . ARG F 1 153 ? 23.428  -47.541 39.983  1 66.97 ? 153 ARG Z NH2   1 
ATOM   7835  N  N     . SER F 1 154 ? 25.392  -53.185 33.607  1 53.87 ? 154 SER Z N     1 
ATOM   7836  C  CA    . SER F 1 154 ? 25.383  -52.719 32.218  1 53.91 ? 154 SER Z CA    1 
ATOM   7837  C  C     . SER F 1 154 ? 23.94   -52.448 31.753  1 53.67 ? 154 SER Z C     1 
ATOM   7838  O  O     . SER F 1 154 ? 22.995  -52.982 32.333  1 54    ? 154 SER Z O     1 
ATOM   7839  C  CB    . SER F 1 154 ? 26.062  -53.73  31.299  1 55.07 ? 154 SER Z CB    1 
ATOM   7840  O  OG    . SER F 1 154 ? 25.318  -54.933 31.209  1 57.09 ? 154 SER Z OG    1 
ATOM   7841  N  N     . ARG F 1 155 ? 23.765  -51.628 30.712  1 52.91 ? 155 ARG Z N     1 
ATOM   7842  C  CA    . ARG F 1 155 ? 22.432  -51.277 30.225  1 52.56 ? 155 ARG Z CA    1 
ATOM   7843  C  C     . ARG F 1 155 ? 21.733  -52.299 29.341  1 51.97 ? 155 ARG Z C     1 
ATOM   7844  O  O     . ARG F 1 155 ? 22.326  -52.875 28.429  1 52.06 ? 155 ARG Z O     1 
ATOM   7845  C  CB    . ARG F 1 155 ? 22.457  -49.944 29.483  1 53.72 ? 155 ARG Z CB    1 
ATOM   7846  C  CG    . ARG F 1 155 ? 22.695  -48.775 30.388  1 56.32 ? 155 ARG Z CG    1 
ATOM   7847  C  CD    . ARG F 1 155 ? 22.839  -47.526 29.563  1 58.88 ? 155 ARG Z CD    1 
ATOM   7848  N  NE    . ARG F 1 155 ? 23.23   -46.403 30.404  1 61.34 ? 155 ARG Z NE    1 
ATOM   7849  C  CZ    . ARG F 1 155 ? 24.486  -46.063 30.661  1 63.02 ? 155 ARG Z CZ    1 
ATOM   7850  N  NH1   . ARG F 1 155 ? 25.492  -46.755 30.137  1 62.52 ? 155 ARG Z NH1   1 
ATOM   7851  N  NH2   . ARG F 1 155 ? 24.747  -45.035 31.449  1 62.65 ? 155 ARG Z NH2   1 
ATOM   7852  N  N     . LYS F 1 156 ? 20.433  -52.451 29.582  1 51.1  ? 156 LYS Z N     1 
ATOM   7853  C  CA    . LYS F 1 156 ? 19.524  -53.279 28.8    1 50.65 ? 156 LYS Z CA    1 
ATOM   7854  C  C     . LYS F 1 156 ? 18.561  -52.337 28.027  1 49.59 ? 156 LYS Z C     1 
ATOM   7855  O  O     . LYS F 1 156 ? 18.595  -51.118 28.231  1 49.82 ? 156 LYS Z O     1 
ATOM   7856  C  CB    . LYS F 1 156 ? 18.766  -54.25  29.721  1 52.82 ? 156 LYS Z CB    1 
ATOM   7857  C  CG    . LYS F 1 156 ? 19.678  -55.278 30.379  1 57.26 ? 156 LYS Z CG    1 
ATOM   7858  C  CD    . LYS F 1 156 ? 19.089  -55.812 31.677  1 62.09 ? 156 LYS Z CD    1 
ATOM   7859  C  CE    . LYS F 1 156 ? 18.115  -56.95  31.491  1 66.07 ? 156 LYS Z CE    1 
ATOM   7860  N  NZ    . LYS F 1 156 ? 17.598  -57.44  32.8    1 68.45 ? 156 LYS Z NZ    1 
ATOM   7861  N  N     . ASN F 1 157 ? 17.725  -52.879 27.13   1 48.25 ? 157 ASN Z N     1 
ATOM   7862  C  CA    . ASN F 1 157 ? 16.816  -52.059 26.322  1 47.49 ? 157 ASN Z CA    1 
ATOM   7863  C  C     . ASN F 1 157 ? 15.948  -51.068 27.116  1 45.9  ? 157 ASN Z C     1 
ATOM   7864  O  O     . ASN F 1 157 ? 15.531  -51.361 28.232  1 46.15 ? 157 ASN Z O     1 
ATOM   7865  C  CB    . ASN F 1 157 ? 15.942  -52.936 25.438  1 49.08 ? 157 ASN Z CB    1 
ATOM   7866  C  CG    . ASN F 1 157 ? 16.734  -53.776 24.467  1 53.23 ? 157 ASN Z CG    1 
ATOM   7867  O  OD1   . ASN F 1 157 ? 16.882  -54.994 24.631  1 54.72 ? 157 ASN Z OD1   1 
ATOM   7868  N  ND2   . ASN F 1 157 ? 17.252  -53.148 23.419  1 54.18 ? 157 ASN Z ND2   1 
ATOM   7869  N  N     . LEU F 1 158 ? 15.704  -49.886 26.537  1 44.15 ? 158 LEU Z N     1 
ATOM   7870  C  CA    . LEU F 1 158 ? 14.879  -48.847 27.14   1 43.03 ? 158 LEU Z CA    1 
ATOM   7871  C  C     . LEU F 1 158 ? 13.468  -49.348 27.341  1 41.92 ? 158 LEU Z C     1 
ATOM   7872  O  O     . LEU F 1 158 ? 12.969  -50.121 26.523  1 42.27 ? 158 LEU Z O     1 
ATOM   7873  C  CB    . LEU F 1 158 ? 14.82   -47.618 26.224  1 43.25 ? 158 LEU Z CB    1 
ATOM   7874  C  CG    . LEU F 1 158 ? 15.93   -46.593 26.357  1 44.67 ? 158 LEU Z CG    1 
ATOM   7875  C  CD1   . LEU F 1 158 ? 15.718  -45.442 25.4    1 45.06 ? 158 LEU Z CD1   1 
ATOM   7876  C  CD2   . LEU F 1 158 ? 16.012  -46.058 27.768  1 45.44 ? 158 LEU Z CD2   1 
ATOM   7877  N  N     . ARG F 1 159 ? 12.805  -48.891 28.407  1 40.57 ? 159 ARG Z N     1 
ATOM   7878  C  CA    . ARG F 1 159 ? 11.433  -49.296 28.676  1 39.72 ? 159 ARG Z CA    1 
ATOM   7879  C  C     . ARG F 1 159 ? 10.476  -48.132 28.51   1 39.25 ? 159 ARG Z C     1 
ATOM   7880  O  O     . ARG F 1 159 ? 10.669  -47.075 29.106  1 39.42 ? 159 ARG Z O     1 
ATOM   7881  C  CB    . ARG F 1 159 ? 11.293  -49.925 30.07   1 40.05 ? 159 ARG Z CB    1 
ATOM   7882  C  CG    . ARG F 1 159 ? 12.068  -51.222 30.232  1 41.51 ? 159 ARG Z CG    1 
ATOM   7883  C  CD    . ARG F 1 159 ? 11.61   -52.332 29.299  1 43.29 ? 159 ARG Z CD    1 
ATOM   7884  N  NE    . ARG F 1 159 ? 10.452  -53.072 29.797  1 44.4  ? 159 ARG Z NE    1 
ATOM   7885  C  CZ    . ARG F 1 159 ? 9.202   -52.866 29.395  1 45.73 ? 159 ARG Z CZ    1 
ATOM   7886  N  NH1   . ARG F 1 159 ? 8.931   -51.924 28.5    1 45.93 ? 159 ARG Z NH1   1 
ATOM   7887  N  NH2   . ARG F 1 159 ? 8.215   -53.595 29.885  1 44.77 ? 159 ARG Z NH2   1 
ATOM   7888  N  N     . PHE F 1 160 ? 9.445   -48.325 27.693  1 38.51 ? 160 PHE Z N     1 
ATOM   7889  C  CA    . PHE F 1 160 ? 8.446   -47.292 27.451  1 38.36 ? 160 PHE Z CA    1 
ATOM   7890  C  C     . PHE F 1 160 ? 7.072   -47.769 27.899  1 37.94 ? 160 PHE Z C     1 
ATOM   7891  O  O     . PHE F 1 160 ? 6.763   -48.962 27.782  1 38.22 ? 160 PHE Z O     1 
ATOM   7892  C  CB    . PHE F 1 160 ? 8.39    -46.94  25.951  1 38.12 ? 160 PHE Z CB    1 
ATOM   7893  C  CG    . PHE F 1 160 ? 9.671   -46.396 25.375  1 38.54 ? 160 PHE Z CG    1 
ATOM   7894  C  CD1   . PHE F 1 160 ? 10.146  -45.153 25.751  1 39.11 ? 160 PHE Z CD1   1 
ATOM   7895  C  CD2   . PHE F 1 160 ? 10.388  -47.118 24.444  1 39.23 ? 160 PHE Z CD2   1 
ATOM   7896  C  CE1   . PHE F 1 160 ? 11.331  -44.663 25.23   1 39.72 ? 160 PHE Z CE1   1 
ATOM   7897  C  CE2   . PHE F 1 160 ? 11.565  -46.619 23.914  1 39.8  ? 160 PHE Z CE2   1 
ATOM   7898  C  CZ    . PHE F 1 160 ? 12.035  -45.401 24.318  1 39.55 ? 160 PHE Z CZ    1 
ATOM   7899  N  N     . PRO F 1 161 ? 6.204   -46.853 28.367  1 37.09 ? 161 PRO Z N     1 
ATOM   7900  C  CA    . PRO F 1 161 ? 4.845   -47.275 28.727  1 36.63 ? 161 PRO Z CA    1 
ATOM   7901  C  C     . PRO F 1 161 ? 4.014   -47.629 27.497  1 36.23 ? 161 PRO Z C     1 
ATOM   7902  O  O     . PRO F 1 161 ? 4.321   -47.197 26.386  1 36.61 ? 161 PRO Z O     1 
ATOM   7903  C  CB    . PRO F 1 161 ? 4.265   -46.029 29.401  1 37.31 ? 161 PRO Z CB    1 
ATOM   7904  C  CG    . PRO F 1 161 ? 4.98    -44.9   28.762  1 37.72 ? 161 PRO Z CG    1 
ATOM   7905  C  CD    . PRO F 1 161 ? 6.385   -45.396 28.541  1 36.29 ? 161 PRO Z CD    1 
ATOM   7906  N  N     . ASN F 1 162 ? 2.931   -48.374 27.694  1 35.36 ? 162 ASN Z N     1 
ATOM   7907  C  CA    . ASN F 1 162 ? 2.001   -48.682 26.613  1 35.29 ? 162 ASN Z CA    1 
ATOM   7908  C  C     . ASN F 1 162 ? 1.304   -47.373 26.237  1 35.12 ? 162 ASN Z C     1 
ATOM   7909  O  O     . ASN F 1 162 ? 0.969   -46.596 27.133  1 35.46 ? 162 ASN Z O     1 
ATOM   7910  C  CB    . ASN F 1 162 ? 0.965   -49.665 27.115  1 36.74 ? 162 ASN Z CB    1 
ATOM   7911  C  CG    . ASN F 1 162 ? 0.002   -50.123 26.061  1 40.62 ? 162 ASN Z CG    1 
ATOM   7912  O  OD1   . ASN F 1 162 ? -0.844  -49.37  25.578  1 41.67 ? 162 ASN Z OD1   1 
ATOM   7913  N  ND2   . ASN F 1 162 ? 0.118   -51.38  25.683  1 41.92 ? 162 ASN Z ND2   1 
ATOM   7914  N  N     . PRO F 1 163 ? 1.089   -47.087 24.94   1 34.47 ? 163 PRO Z N     1 
ATOM   7915  C  CA    . PRO F 1 163 ? 0.436   -45.813 24.571  1 34.09 ? 163 PRO Z CA    1 
ATOM   7916  C  C     . PRO F 1 163 ? -0.872  -45.499 25.318  1 33.8  ? 163 PRO Z C     1 
ATOM   7917  O  O     . PRO F 1 163 ? -1.214  -44.337 25.501  1 33.72 ? 163 PRO Z O     1 
ATOM   7918  C  CB    . PRO F 1 163 ? 0.209   -45.954 23.065  1 34.85 ? 163 PRO Z CB    1 
ATOM   7919  C  CG    . PRO F 1 163 ? 1.208   -46.974 22.605  1 35.32 ? 163 PRO Z CG    1 
ATOM   7920  C  CD    . PRO F 1 163 ? 1.464   -47.888 23.755  1 33.85 ? 163 PRO Z CD    1 
ATOM   7921  N  N     . ALA F 1 164 ? -1.586  -46.534 25.773  1 33.55 ? 164 ALA Z N     1 
ATOM   7922  C  CA    . ALA F 1 164 ? -2.841  -46.378 26.502  1 33.57 ? 164 ALA Z CA    1 
ATOM   7923  C  C     . ALA F 1 164 ? -2.667  -45.725 27.866  1 33.36 ? 164 ALA Z C     1 
ATOM   7924  O  O     . ALA F 1 164 ? -3.623  -45.146 28.373  1 33.54 ? 164 ALA Z O     1 
ATOM   7925  C  CB    . ALA F 1 164 ? -3.531  -47.724 26.66   1 33.74 ? 164 ALA Z CB    1 
ATOM   7926  N  N     . ILE F 1 165 ? -1.477  -45.827 28.476  1 32.87 ? 165 ILE Z N     1 
ATOM   7927  C  CA    . ILE F 1 165 ? -1.241  -45.209 29.783  1 32.96 ? 165 ILE Z CA    1 
ATOM   7928  C  C     . ILE F 1 165 ? -1.27   -43.699 29.674  1 33.25 ? 165 ILE Z C     1 
ATOM   7929  O  O     . ILE F 1 165 ? -2.177  -43.098 30.237  1 33.34 ? 165 ILE Z O     1 
ATOM   7930  C  CB    . ILE F 1 165 ? 0.016   -45.715 30.516  1 33.21 ? 165 ILE Z CB    1 
ATOM   7931  C  CG1   . ILE F 1 165 ? 0.187   -47.233 30.393  1 34.35 ? 165 ILE Z CG1   1 
ATOM   7932  C  CG2   . ILE F 1 165 ? 0.025   -45.242 31.951  1 33.43 ? 165 ILE Z CG2   1 
ATOM   7933  C  CD1   . ILE F 1 165 ? -0.984  -48.037 30.799  1 35.82 ? 165 ILE Z CD1   1 
ATOM   7934  N  N     . PRO F 1 166 ? -0.393  -43.053 28.864  1 33.22 ? 166 PRO Z N     1 
ATOM   7935  C  CA    . PRO F 1 166 ? -0.502  -41.595 28.698  1 33.03 ? 166 PRO Z CA    1 
ATOM   7936  C  C     . PRO F 1 166 ? -1.892  -41.171 28.236  1 32.68 ? 166 PRO Z C     1 
ATOM   7937  O  O     . PRO F 1 166 ? -2.399  -40.157 28.696  1 32.45 ? 166 PRO Z O     1 
ATOM   7938  C  CB    . PRO F 1 166 ? 0.534   -41.285 27.605  1 33.95 ? 166 PRO Z CB    1 
ATOM   7939  C  CG    . PRO F 1 166 ? 1.507   -42.388 27.669  1 34.47 ? 166 PRO Z CG    1 
ATOM   7940  C  CD    . PRO F 1 166 ? 0.727   -43.598 28.065  1 32.83 ? 166 PRO Z CD    1 
ATOM   7941  N  N     . TYR F 1 167 ? -2.519  -41.974 27.361  1 32.5  ? 167 TYR Z N     1 
ATOM   7942  C  CA    . TYR F 1 167 ? -3.837  -41.648 26.858  1 32.55 ? 167 TYR Z CA    1 
ATOM   7943  C  C     . TYR F 1 167 ? -4.896  -41.661 27.932  1 32.19 ? 167 TYR Z C     1 
ATOM   7944  O  O     . TYR F 1 167 ? -5.771  -40.802 27.915  1 32.3  ? 167 TYR Z O     1 
ATOM   7945  C  CB    . TYR F 1 167 ? -4.259  -42.507 25.659  1 32.56 ? 167 TYR Z CB    1 
ATOM   7946  C  CG    . TYR F 1 167 ? -5.455  -41.875 24.995  1 33.32 ? 167 TYR Z CG    1 
ATOM   7947  C  CD1   . TYR F 1 167 ? -5.324  -40.703 24.267  1 34.23 ? 167 TYR Z CD1   1 
ATOM   7948  C  CD2   . TYR F 1 167 ? -6.738  -42.338 25.25   1 34.2  ? 167 TYR Z CD2   1 
ATOM   7949  C  CE1   . TYR F 1 167 ? -6.427  -40.056 23.737  1 35.13 ? 167 TYR Z CE1   1 
ATOM   7950  C  CE2   . TYR F 1 167 ? -7.85   -41.7   24.727  1 35.13 ? 167 TYR Z CE2   1 
ATOM   7951  C  CZ    . TYR F 1 167 ? -7.69   -40.561 23.967  1 36.03 ? 167 TYR Z CZ    1 
ATOM   7952  O  OH    . TYR F 1 167 ? -8.788  -39.93  23.449  1 37.59 ? 167 TYR Z OH    1 
ATOM   7953  N  N     . SER F 1 168 ? -4.804  -42.577 28.893  1 31.86 ? 168 SER Z N     1 
ATOM   7954  C  CA    . SER F 1 168 ? -5.789  -42.661 29.97   1 32.44 ? 168 SER Z CA    1 
ATOM   7955  C  C     . SER F 1 168 ? -5.985  -41.35  30.734  1 32.1  ? 168 SER Z C     1 
ATOM   7956  O  O     . SER F 1 168 ? -7.091  -41.054 31.167  1 32.05 ? 168 SER Z O     1 
ATOM   7957  C  CB    . SER F 1 168 ? -5.463  -43.804 30.925  1 34.49 ? 168 SER Z CB    1 
ATOM   7958  O  OG    . SER F 1 168 ? -4.316  -43.54  31.716  1 37.5  ? 168 SER Z OG    1 
ATOM   7959  N  N     . TYR F 1 169 ? -4.927  -40.551 30.842  1 31.66 ? 169 TYR Z N     1 
ATOM   7960  C  CA    . TYR F 1 169 ? -4.967  -39.261 31.508  1 31.83 ? 169 TYR Z CA    1 
ATOM   7961  C  C     . TYR F 1 169 ? -5.801  -38.27  30.689  1 32.02 ? 169 TYR Z C     1 
ATOM   7962  O  O     . TYR F 1 169 ? -6.61   -37.537 31.246  1 32.23 ? 169 TYR Z O     1 
ATOM   7963  C  CB    . TYR F 1 169 ? -3.534  -38.758 31.753  1 31.85 ? 169 TYR Z CB    1 
ATOM   7964  C  CG    . TYR F 1 169 ? -2.836  -39.529 32.857  1 32.67 ? 169 TYR Z CG    1 
ATOM   7965  C  CD1   . TYR F 1 169 ? -2.401  -40.831 32.658  1 33.44 ? 169 TYR Z CD1   1 
ATOM   7966  C  CD2   . TYR F 1 169 ? -2.643  -38.966 34.111  1 33.43 ? 169 TYR Z CD2   1 
ATOM   7967  C  CE1   . TYR F 1 169 ? -1.805  -41.559 33.681  1 34.13 ? 169 TYR Z CE1   1 
ATOM   7968  C  CE2   . TYR F 1 169 ? -2.029  -39.677 35.134  1 34.1  ? 169 TYR Z CE2   1 
ATOM   7969  C  CZ    . TYR F 1 169 ? -1.615  -40.974 34.916  1 34.85 ? 169 TYR Z CZ    1 
ATOM   7970  O  OH    . TYR F 1 169 ? -1.02   -41.678 35.927  1 36.23 ? 169 TYR Z OH    1 
ATOM   7971  N  N     . ILE F 1 170 ? -5.648  -38.288 29.365  1 31.95 ? 170 ILE Z N     1 
ATOM   7972  C  CA    . ILE F 1 170 ? -6.421  -37.425 28.477  1 32.27 ? 170 ILE Z CA    1 
ATOM   7973  C  C     . ILE F 1 170 ? -7.893  -37.823 28.491  1 32.68 ? 170 ILE Z C     1 
ATOM   7974  O  O     . ILE F 1 170 ? -8.752  -36.952 28.595  1 32.99 ? 170 ILE Z O     1 
ATOM   7975  C  CB    . ILE F 1 170 ? -5.86   -37.456 27.04   1 32.57 ? 170 ILE Z CB    1 
ATOM   7976  C  CG1   . ILE F 1 170 ? -4.404  -36.973 26.999  1 33.43 ? 170 ILE Z CG1   1 
ATOM   7977  C  CG2   . ILE F 1 170 ? -6.73   -36.642 26.105  1 32.94 ? 170 ILE Z CG2   1 
ATOM   7978  C  CD1   . ILE F 1 170 ? -3.73   -37.259 25.713  1 34.82 ? 170 ILE Z CD1   1 
ATOM   7979  N  N     . SER F 1 171 ? -8.19   -39.131 28.416  1 32.48 ? 171 SER Z N     1 
ATOM   7980  C  CA    . SER F 1 171 ? -9.576  -39.596 28.429  1 32.79 ? 171 SER Z CA    1 
ATOM   7981  C  C     . SER F 1 171 ? -10.249 -39.367 29.771  1 32.83 ? 171 SER Z C     1 
ATOM   7982  O  O     . SER F 1 171 ? -11.424 -39.021 29.79   1 32.87 ? 171 SER Z O     1 
ATOM   7983  C  CB    . SER F 1 171 ? -9.679  -41.057 28.011  1 34.25 ? 171 SER Z CB    1 
ATOM   7984  O  OG    . SER F 1 171 ? -8.876  -41.876 28.841  1 36.59 ? 171 SER Z OG    1 
ATOM   7985  N  N     . HIS F 1 172 ? -9.517  -39.518 30.89   1 32.81 ? 172 HIS Z N     1 
ATOM   7986  C  CA    . HIS F 1 172 ? -10.091 -39.244 32.216  1 33.27 ? 172 HIS Z CA    1 
ATOM   7987  C  C     . HIS F 1 172 ? -10.42  -37.749 32.327  1 33.68 ? 172 HIS Z C     1 
ATOM   7988  O  O     . HIS F 1 172 ? -11.446 -37.391 32.898  1 33.78 ? 172 HIS Z O     1 
ATOM   7989  C  CB    . HIS F 1 172 ? -9.133  -39.655 33.339  1 33.98 ? 172 HIS Z CB    1 
ATOM   7990  C  CG    . HIS F 1 172 ? -9.803  -39.855 34.661  1 36.49 ? 172 HIS Z CG    1 
ATOM   7991  N  ND1   . HIS F 1 172 ? -11.103 -40.314 34.747  1 38.48 ? 172 HIS Z ND1   1 
ATOM   7992  C  CD2   . HIS F 1 172 ? -9.309  -39.705 35.914  1 37.81 ? 172 HIS Z CD2   1 
ATOM   7993  C  CE1   . HIS F 1 172 ? -11.368 -40.402 36.043  1 39.03 ? 172 HIS Z CE1   1 
ATOM   7994  N  NE2   . HIS F 1 172 ? -10.319 -40.044 36.784  1 38.93 ? 172 HIS Z NE2   1 
ATOM   7995  N  N     . SER F 1 173 ? -9.565  -36.88  31.747  1 33.55 ? 173 SER Z N     1 
ATOM   7996  C  CA    . SER F 1 173 ? -9.783  -35.444 31.709  1 33.74 ? 173 SER Z CA    1 
ATOM   7997  C  C     . SER F 1 173 ? -11.065 -35.125 30.941  1 34.16 ? 173 SER Z C     1 
ATOM   7998  O  O     . SER F 1 173 ? -11.869 -34.342 31.427  1 34.49 ? 173 SER Z O     1 
ATOM   7999  C  CB    . SER F 1 173 ? -8.598  -34.741 31.058  1 34.64 ? 173 SER Z CB    1 
ATOM   8000  O  OG    . SER F 1 173 ? -7.447  -34.823 31.878  1 36.29 ? 173 SER Z OG    1 
ATOM   8001  N  N     . LYS F 1 174 ? -11.278 -35.739 29.769  1 34.08 ? 174 LYS Z N     1 
ATOM   8002  C  CA    . LYS F 1 174 ? -12.491 -35.501 28.991  1 34.63 ? 174 LYS Z CA    1 
ATOM   8003  C  C     . LYS F 1 174 ? -13.739 -35.976 29.732  1 34.64 ? 174 LYS Z C     1 
ATOM   8004  O  O     . LYS F 1 174 ? -14.715 -35.233 29.818  1 34.93 ? 174 LYS Z O     1 
ATOM   8005  C  CB    . LYS F 1 174 ? -12.415 -36.196 27.634  1 37.11 ? 174 LYS Z CB    1 
ATOM   8006  C  CG    . LYS F 1 174 ? -11.272 -35.728 26.77   1 42.2  ? 174 LYS Z CG    1 
ATOM   8007  C  CD    . LYS F 1 174 ? -11.444 -36.273 25.377  1 47.76 ? 174 LYS Z CD    1 
ATOM   8008  C  CE    . LYS F 1 174 ? -10.142 -36.289 24.635  1 53.09 ? 174 LYS Z CE    1 
ATOM   8009  N  NZ    . LYS F 1 174 ? -9.959  -35.085 23.784  1 56.42 ? 174 LYS Z NZ    1 
ATOM   8010  N  N     . ASN F 1 175 ? -13.703 -37.201 30.273  1 34.17 ? 175 ASN Z N     1 
ATOM   8011  C  CA    . ASN F 1 175 ? -14.828 -37.793 30.988  1 34.2  ? 175 ASN Z CA    1 
ATOM   8012  C  C     . ASN F 1 175 ? -15.236 -37.001 32.235  1 33.98 ? 175 ASN Z C     1 
ATOM   8013  O  O     . ASN F 1 175 ? -16.426 -36.88  32.516  1 34.07 ? 175 ASN Z O     1 
ATOM   8014  C  CB    . ASN F 1 175 ? -14.511 -39.246 31.377  1 35.1  ? 175 ASN Z CB    1 
ATOM   8015  C  CG    . ASN F 1 175 ? -14.406 -40.197 30.216  1 37.63 ? 175 ASN Z CG    1 
ATOM   8016  O  OD1   . ASN F 1 175 ? -15.019 -40.004 29.165  1 38.68 ? 175 ASN Z OD1   1 
ATOM   8017  N  ND2   . ASN F 1 175 ? -13.619 -41.245 30.381  1 38.18 ? 175 ASN Z ND2   1 
ATOM   8018  N  N     . THR F 1 176 ? -14.262 -36.471 32.981  1 33.52 ? 176 THR Z N     1 
ATOM   8019  C  CA    . THR F 1 176 ? -14.554 -35.755 34.221  1 33.7  ? 176 THR Z CA    1 
ATOM   8020  C  C     . THR F 1 176 ? -14.715 -34.252 34.078  1 33.72 ? 176 THR Z C     1 
ATOM   8021  O  O     . THR F 1 176 ? -15.315 -33.616 34.942  1 34.13 ? 176 THR Z O     1 
ATOM   8022  C  CB    . THR F 1 176 ? -13.43  -35.999 35.229  1 34.85 ? 176 THR Z CB    1 
ATOM   8023  O  OG1   . THR F 1 176 ? -12.201 -35.548 34.654  1 35.85 ? 176 THR Z OG1   1 
ATOM   8024  C  CG2   . THR F 1 176 ? -13.324 -37.456 35.651  1 35.12 ? 176 THR Z CG2   1 
ATOM   8025  N  N     . GLY F 1 177 ? -14.122 -33.681 33.045  1 33.12 ? 177 GLY Z N     1 
ATOM   8026  C  CA    . GLY F 1 177 ? -14.093 -32.232 32.882  1 32.98 ? 177 GLY Z CA    1 
ATOM   8027  C  C     . GLY F 1 177 ? -12.982 -31.576 33.696  1 32.5  ? 177 GLY Z C     1 
ATOM   8028  O  O     . GLY F 1 177 ? -12.867 -30.351 33.715  1 32.64 ? 177 GLY Z O     1 
ATOM   8029  N  N     . ASN F 1 178 ? -12.145 -32.39  34.368  1 31.88 ? 178 ASN Z N     1 
ATOM   8030  C  CA    . ASN F 1 178 ? -11.034 -31.965 35.21   1 32.03 ? 178 ASN Z CA    1 
ATOM   8031  C  C     . ASN F 1 178 ? -9.696  -32.022 34.44   1 31.97 ? 178 ASN Z C     1 
ATOM   8032  O  O     . ASN F 1 178 ? -9.631  -32.571 33.343  1 32.18 ? 178 ASN Z O     1 
ATOM   8033  C  CB    . ASN F 1 178 ? -10.99  -32.873 36.455  1 33.18 ? 178 ASN Z CB    1 
ATOM   8034  C  CG    . ASN F 1 178 ? -10.079 -32.425 37.575  1 36.18 ? 178 ASN Z CG    1 
ATOM   8035  O  OD1   . ASN F 1 178 ? -9.657  -31.266 37.66   1 37.55 ? 178 ASN Z OD1   1 
ATOM   8036  N  ND2   . ASN F 1 178 ? -9.76   -33.347 38.465  1 36.5  ? 178 ASN Z ND2   1 
ATOM   8037  N  N     . PHE F 1 179 ? -8.636  -31.434 35.003  1 31.48 ? 179 PHE Z N     1 
ATOM   8038  C  CA    . PHE F 1 179 ? -7.32   -31.456 34.392  1 31.39 ? 179 PHE Z CA    1 
ATOM   8039  C  C     . PHE F 1 179 ? -6.466  -32.544 35.03   1 31.51 ? 179 PHE Z C     1 
ATOM   8040  O  O     . PHE F 1 179 ? -5.961  -32.371 36.14   1 31.76 ? 179 PHE Z O     1 
ATOM   8041  C  CB    . PHE F 1 179 ? -6.635  -30.106 34.558  1 31.13 ? 179 PHE Z CB    1 
ATOM   8042  C  CG    . PHE F 1 179 ? -5.306  -30.019 33.857  1 31.73 ? 179 PHE Z CG    1 
ATOM   8043  C  CD1   . PHE F 1 179 ? -5.201  -30.284 32.504  1 32.55 ? 179 PHE Z CD1   1 
ATOM   8044  C  CD2   . PHE F 1 179 ? -4.17   -29.626 34.54   1 32.6  ? 179 PHE Z CD2   1 
ATOM   8045  C  CE1   . PHE F 1 179 ? -3.977  -30.185 31.854  1 33.2  ? 179 PHE Z CE1   1 
ATOM   8046  C  CE2   . PHE F 1 179 ? -2.954  -29.5   33.879  1 33.4  ? 179 PHE Z CE2   1 
ATOM   8047  C  CZ    . PHE F 1 179 ? -2.864  -29.788 32.543  1 33.09 ? 179 PHE Z CZ    1 
ATOM   8048  N  N     . ILE F 1 180 ? -6.335  -33.682 34.339  1 31.01 ? 180 ILE Z N     1 
ATOM   8049  C  CA    . ILE F 1 180 ? -5.521  -34.818 34.765  1 30.7  ? 180 ILE Z CA    1 
ATOM   8050  C  C     . ILE F 1 180 ? -4.54   -35.041 33.627  1 30.68 ? 180 ILE Z C     1 
ATOM   8051  O  O     . ILE F 1 180 ? -4.98   -35.29  32.505  1 30.87 ? 180 ILE Z O     1 
ATOM   8052  C  CB    . ILE F 1 180 ? -6.411  -36.051 34.99   1 30.77 ? 180 ILE Z CB    1 
ATOM   8053  C  CG1   . ILE F 1 180 ? -7.522  -35.752 35.995  1 31.06 ? 180 ILE Z CG1   1 
ATOM   8054  C  CG2   . ILE F 1 180 ? -5.574  -37.232 35.43   1 31.37 ? 180 ILE Z CG2   1 
ATOM   8055  C  CD1   . ILE F 1 180 ? -8.887  -35.89  35.443  1 31.96 ? 180 ILE Z CD1   1 
ATOM   8056  N  N     . VAL F 1 181 ? -3.23   -34.892 33.878  1 30.48 ? 181 VAL Z N     1 
ATOM   8057  C  CA    . VAL F 1 181 ? -2.251  -34.984 32.796  1 31    ? 181 VAL Z CA    1 
ATOM   8058  C  C     . VAL F 1 181 ? -0.952  -35.702 33.186  1 31.27 ? 181 VAL Z C     1 
ATOM   8059  O  O     . VAL F 1 181 ? -0.622  -35.838 34.365  1 31.38 ? 181 VAL Z O     1 
ATOM   8060  C  CB    . VAL F 1 181 ? -1.968  -33.55  32.268  1 31.65 ? 181 VAL Z CB    1 
ATOM   8061  C  CG1   . VAL F 1 181 ? -1.049  -32.791 33.219  1 32.4  ? 181 VAL Z CG1   1 
ATOM   8062  C  CG2   . VAL F 1 181 ? -1.401  -33.56  30.854  1 32    ? 181 VAL Z CG2   1 
ATOM   8063  N  N     . GLN F 1 182 ? -0.227  -36.175 32.174  1 31.05 ? 182 GLN Z N     1 
ATOM   8064  C  CA    . GLN F 1 182 ? 1.078   -36.777 32.331  1 31.23 ? 182 GLN Z CA    1 
ATOM   8065  C  C     . GLN F 1 182 ? 2.051   -35.795 31.656  1 31.22 ? 182 GLN Z C     1 
ATOM   8066  O  O     . GLN F 1 182 ? 1.854   -35.399 30.503  1 31.37 ? 182 GLN Z O     1 
ATOM   8067  C  CB    . GLN F 1 182 ? 1.126   -38.156 31.664  1 32.67 ? 182 GLN Z CB    1 
ATOM   8068  C  CG    . GLN F 1 182 ? 2.201   -39.065 32.226  1 35.47 ? 182 GLN Z CG    1 
ATOM   8069  C  CD    . GLN F 1 182 ? 2.021   -40.458 31.7    1 39.28 ? 182 GLN Z CD    1 
ATOM   8070  O  OE1   . GLN F 1 182 ? 2.091   -40.698 30.502  1 41.24 ? 182 GLN Z OE1   1 
ATOM   8071  N  NE2   . GLN F 1 182 ? 1.772   -41.414 32.562  1 39.15 ? 182 GLN Z NE2   1 
ATOM   8072  N  N     . ALA F 1 183 ? 3.041   -35.336 32.416  1 30.71 ? 183 ALA Z N     1 
ATOM   8073  C  CA    . ALA F 1 183 ? 4.06    -34.398 31.968  1 30.61 ? 183 ALA Z CA    1 
ATOM   8074  C  C     . ALA F 1 183 ? 5.414   -35.096 31.976  1 30.35 ? 183 ALA Z C     1 
ATOM   8075  O  O     . ALA F 1 183 ? 5.692   -35.872 32.888  1 30.65 ? 183 ALA Z O     1 
ATOM   8076  C  CB    . ALA F 1 183 ? 4.091   -33.207 32.9    1 30.67 ? 183 ALA Z CB    1 
ATOM   8077  N  N     . TYR F 1 184 ? 6.257   -34.825 30.981  1 29.69 ? 184 TYR Z N     1 
ATOM   8078  C  CA    . TYR F 1 184 ? 7.542   -35.513 30.866  1 29.58 ? 184 TYR Z CA    1 
ATOM   8079  C  C     . TYR F 1 184 ? 8.698   -34.575 31.013  1 29.44 ? 184 TYR Z C     1 
ATOM   8080  O  O     . TYR F 1 184 ? 8.748   -33.543 30.361  1 29.18 ? 184 TYR Z O     1 
ATOM   8081  C  CB    . TYR F 1 184 ? 7.641   -36.294 29.537  1 29.6  ? 184 TYR Z CB    1 
ATOM   8082  C  CG    . TYR F 1 184 ? 6.383   -37.08  29.255  1 30.04 ? 184 TYR Z CG    1 
ATOM   8083  C  CD1   . TYR F 1 184 ? 6.191   -38.338 29.804  1 30.64 ? 184 TYR Z CD1   1 
ATOM   8084  C  CD2   . TYR F 1 184 ? 5.33    -36.51  28.556  1 30.81 ? 184 TYR Z CD2   1 
ATOM   8085  C  CE1   . TYR F 1 184 ? 5.001   -39.023 29.631  1 31.34 ? 184 TYR Z CE1   1 
ATOM   8086  C  CE2   . TYR F 1 184 ? 4.132   -37.18  28.388  1 31.49 ? 184 TYR Z CE2   1 
ATOM   8087  C  CZ    . TYR F 1 184 ? 3.975   -38.439 28.921  1 32.21 ? 184 TYR Z CZ    1 
ATOM   8088  O  OH    . TYR F 1 184 ? 2.8     -39.11  28.727  1 33.72 ? 184 TYR Z OH    1 
ATOM   8089  N  N     . PHE F 1 185 ? 9.625   -34.925 31.886  1 29.46 ? 185 PHE Z N     1 
ATOM   8090  C  CA    . PHE F 1 185 ? 10.82   -34.126 32.104  1 30.11 ? 185 PHE Z CA    1 
ATOM   8091  C  C     . PHE F 1 185 ? 12.008  -34.879 31.496  1 31.25 ? 185 PHE Z C     1 
ATOM   8092  O  O     . PHE F 1 185 ? 12.028  -36.112 31.478  1 31.07 ? 185 PHE Z O     1 
ATOM   8093  C  CB    . PHE F 1 185 ? 11.052  -33.869 33.607  1 29.63 ? 185 PHE Z CB    1 
ATOM   8094  C  CG    . PHE F 1 185 ? 10.218  -32.778 34.251  1 29.69 ? 185 PHE Z CG    1 
ATOM   8095  C  CD1   . PHE F 1 185 ? 9.067   -32.307 33.645  1 30.31 ? 185 PHE Z CD1   1 
ATOM   8096  C  CD2   . PHE F 1 185 ? 10.572  -32.246 35.474  1 30.25 ? 185 PHE Z CD2   1 
ATOM   8097  C  CE1   . PHE F 1 185 ? 8.301   -31.309 34.241  1 30.84 ? 185 PHE Z CE1   1 
ATOM   8098  C  CE2   . PHE F 1 185 ? 9.801   -31.251 36.068  1 30.89 ? 185 PHE Z CE2   1 
ATOM   8099  C  CZ    . PHE F 1 185 ? 8.674   -30.788 35.445  1 30.58 ? 185 PHE Z CZ    1 
ATOM   8100  N  N     . ARG F 1 186 ? 12.987  -34.135 30.985  1 32.2  ? 186 ARG Z N     1 
ATOM   8101  C  CA    . ARG F 1 186 ? 14.171  -34.712 30.37   1 33.62 ? 186 ARG Z CA    1 
ATOM   8102  C  C     . ARG F 1 186 ? 15.081  -35.399 31.377  1 34.51 ? 186 ARG Z C     1 
ATOM   8103  O  O     . ARG F 1 186 ? 15.715  -34.743 32.199  1 34.53 ? 186 ARG Z O     1 
ATOM   8104  C  CB    . ARG F 1 186 ? 14.957  -33.645 29.599  1 35.48 ? 186 ARG Z CB    1 
ATOM   8105  C  CG    . ARG F 1 186 ? 16.121  -34.237 28.808  1 39.09 ? 186 ARG Z CG    1 
ATOM   8106  C  CD    . ARG F 1 186 ? 17.266  -33.265 28.561  1 42.59 ? 186 ARG Z CD    1 
ATOM   8107  N  NE    . ARG F 1 186 ? 16.889  -32.067 27.809  1 45.97 ? 186 ARG Z NE    1 
ATOM   8108  C  CZ    . ARG F 1 186 ? 16.976  -31.938 26.49   1 48.48 ? 186 ARG Z CZ    1 
ATOM   8109  N  NH1   . ARG F 1 186 ? 17.409  -32.947 25.742  1 47.93 ? 186 ARG Z NH1   1 
ATOM   8110  N  NH2   . ARG F 1 186 ? 16.588  -30.817 25.906  1 48.94 ? 186 ARG Z NH2   1 
ATOM   8111  N  N     . GLY F 1 187 ? 15.145  -36.715 31.288  1 35.17 ? 187 GLY Z N     1 
ATOM   8112  C  CA    . GLY F 1 187 ? 15.997  -37.518 32.149  1 36.31 ? 187 GLY Z CA    1 
ATOM   8113  C  C     . GLY F 1 187 ? 17.45   -37.426 31.746  1 37.17 ? 187 GLY Z C     1 
ATOM   8114  O  O     . GLY F 1 187 ? 17.758  -37.107 30.598  1 37.3  ? 187 GLY Z O     1 
ATOM   8115  N  N     . GLU F 1 188 ? 18.354  -37.709 32.684  1 37.56 ? 188 GLU Z N     1 
ATOM   8116  C  CA    . GLU F 1 188 ? 19.785  -37.663 32.409  1 38.39 ? 188 GLU Z CA    1 
ATOM   8117  C  C     . GLU F 1 188 ? 20.196  -38.69  31.365  1 39.1  ? 188 GLU Z C     1 
ATOM   8118  O  O     . GLU F 1 188 ? 21.113  -38.429 30.588  1 39.37 ? 188 GLU Z O     1 
ATOM   8119  C  CB    . GLU F 1 188 ? 20.594  -37.88  33.691  1 40.62 ? 188 GLU Z CB    1 
ATOM   8120  C  CG    . GLU F 1 188 ? 20.264  -36.902 34.799  1 45.2  ? 188 GLU Z CG    1 
ATOM   8121  C  CD    . GLU F 1 188 ? 19.3    -37.439 35.838  1 50.85 ? 188 GLU Z CD    1 
ATOM   8122  O  OE1   . GLU F 1 188 ? 18.407  -38.24  35.477  1 51.24 ? 188 GLU Z OE1   1 
ATOM   8123  O  OE2   . GLU F 1 188 ? 19.438  -37.053 37.02   1 53.28 ? 188 GLU Z OE2   1 
ATOM   8124  N  N     . GLU F 1 189 ? 19.514  -39.843 31.321  1 39.34 ? 189 GLU Z N     1 
ATOM   8125  C  CA    . GLU F 1 189 ? 19.844  -40.871 30.343  1 40.14 ? 189 GLU Z CA    1 
ATOM   8126  C  C     . GLU F 1 189 ? 19.116  -40.706 28.992  1 40.54 ? 189 GLU Z C     1 
ATOM   8127  O  O     . GLU F 1 189 ? 19.172  -41.618 28.161  1 40.58 ? 189 GLU Z O     1 
ATOM   8128  C  CB    . GLU F 1 189 ? 19.658  -42.271 30.921  1 42.63 ? 189 GLU Z CB    1 
ATOM   8129  C  CG    . GLU F 1 189 ? 20.879  -42.722 31.701  1 47.98 ? 189 GLU Z CG    1 
ATOM   8130  C  CD    . GLU F 1 189 ? 20.787  -44.103 32.314  1 54.78 ? 189 GLU Z CD    1 
ATOM   8131  O  OE1   . GLU F 1 189 ? 19.658  -44.533 32.637  1 55.51 ? 189 GLU Z OE1   1 
ATOM   8132  O  OE2   . GLU F 1 189 ? 21.843  -44.755 32.481  1 57.44 ? 189 GLU Z OE2   1 
ATOM   8133  N  N     . TYR F 1 190 ? 18.473  -39.538 28.752  1 40.52 ? 190 TYR Z N     1 
ATOM   8134  C  CA    . TYR F 1 190 ? 17.863  -39.26  27.455  1 40.94 ? 190 TYR Z CA    1 
ATOM   8135  C  C     . TYR F 1 190 ? 19.042  -38.887 26.561  1 41.36 ? 190 TYR Z C     1 
ATOM   8136  O  O     . TYR F 1 190 ? 19.567  -37.778 26.66   1 41.6  ? 190 TYR Z O     1 
ATOM   8137  C  CB    . TYR F 1 190 ? 16.846  -38.095 27.519  1 40.89 ? 190 TYR Z CB    1 
ATOM   8138  C  CG    . TYR F 1 190 ? 16.351  -37.669 26.151  1 41.52 ? 190 TYR Z CG    1 
ATOM   8139  C  CD1   . TYR F 1 190 ? 15.546  -38.503 25.392  1 42.34 ? 190 TYR Z CD1   1 
ATOM   8140  C  CD2   . TYR F 1 190 ? 16.713  -36.445 25.607  1 42.41 ? 190 TYR Z CD2   1 
ATOM   8141  C  CE1   . TYR F 1 190 ? 15.118  -38.135 24.124  1 43.21 ? 190 TYR Z CE1   1 
ATOM   8142  C  CE2   . TYR F 1 190 ? 16.277  -36.058 24.344  1 43.24 ? 190 TYR Z CE2   1 
ATOM   8143  C  CZ    . TYR F 1 190 ? 15.487  -36.911 23.602  1 44.11 ? 190 TYR Z CZ    1 
ATOM   8144  O  OH    . TYR F 1 190 ? 15.071  -36.558 22.345  1 45.6  ? 190 TYR Z OH    1 
ATOM   8145  N  N     . GLN F 1 191 ? 19.514  -39.839 25.753  1 41.18 ? 191 GLN Z N     1 
ATOM   8146  C  CA    . GLN F 1 191 ? 20.66   -39.61  24.883  1 41.41 ? 191 GLN Z CA    1 
ATOM   8147  C  C     . GLN F 1 191 ? 20.267  -40.035 23.475  1 41.32 ? 191 GLN Z C     1 
ATOM   8148  O  O     . GLN F 1 191 ? 20.563  -41.156 23.065  1 41.55 ? 191 GLN Z O     1 
ATOM   8149  C  CB    . GLN F 1 191 ? 21.843  -40.448 25.391  1 43.07 ? 191 GLN Z CB    1 
ATOM   8150  C  CG    . GLN F 1 191 ? 23.155  -39.695 25.49   1 46.48 ? 191 GLN Z CG    1 
ATOM   8151  C  CD    . GLN F 1 191 ? 23.076  -38.538 26.44   1 50.96 ? 191 GLN Z CD    1 
ATOM   8152  O  OE1   . GLN F 1 191 ? 22.682  -38.679 27.603  1 52.36 ? 191 GLN Z OE1   1 
ATOM   8153  N  NE2   . GLN F 1 191 ? 23.451  -37.364 25.959  1 51.61 ? 191 GLN Z NE2   1 
ATOM   8154  N  N     . PRO F 1 192 ? 19.55   -39.17  22.736  1 40.87 ? 192 PRO Z N     1 
ATOM   8155  C  CA    . PRO F 1 192 ? 19.053  -39.567 21.407  1 40.71 ? 192 PRO Z CA    1 
ATOM   8156  C  C     . PRO F 1 192 ? 20.116  -39.817 20.34   1 40.6  ? 192 PRO Z C     1 
ATOM   8157  O  O     . PRO F 1 192 ? 19.86   -40.532 19.371  1 40.53 ? 192 PRO Z O     1 
ATOM   8158  C  CB    . PRO F 1 192 ? 18.119  -38.417 21.021  1 41.41 ? 192 PRO Z CB    1 
ATOM   8159  C  CG    . PRO F 1 192 ? 18.611  -37.255 21.798  1 41.84 ? 192 PRO Z CG    1 
ATOM   8160  C  CD    . PRO F 1 192 ? 19.094  -37.818 23.102  1 40.3  ? 192 PRO Z CD    1 
ATOM   8161  N  N     . LYS F 1 193 ? 21.307  -39.245 20.517  1 40.35 ? 193 LYS Z N     1 
ATOM   8162  C  CA    . LYS F 1 193 ? 22.405  -39.454 19.578  1 40.37 ? 193 LYS Z CA    1 
ATOM   8163  C  C     . LYS F 1 193 ? 22.953  -40.892 19.642  1 40.44 ? 193 LYS Z C     1 
ATOM   8164  O  O     . LYS F 1 193 ? 23.61   -41.321 18.701  1 40.72 ? 193 LYS Z O     1 
ATOM   8165  C  CB    . LYS F 1 193 ? 23.54   -38.46  19.868  1 41.83 ? 193 LYS Z CB    1 
ATOM   8166  C  CG    . LYS F 1 193 ? 23.095  -37.003 19.893  1 45.29 ? 193 LYS Z CG    1 
ATOM   8167  C  CD    . LYS F 1 193 ? 24.231  -36.073 20.327  1 49.19 ? 193 LYS Z CD    1 
ATOM   8168  C  CE    . LYS F 1 193 ? 23.828  -34.616 20.333  1 52.3  ? 193 LYS Z CE    1 
ATOM   8169  N  NZ    . LYS F 1 193 ? 24.823  -33.765 21.047  1 53.98 ? 193 LYS Z NZ    1 
ATOM   8170  N  N     . TYR F 1 194 ? 22.688  -41.634 20.737  1 40.14 ? 194 TYR Z N     1 
ATOM   8171  C  CA    . TYR F 1 194 ? 23.207  -42.983 20.933  1 40.24 ? 194 TYR Z CA    1 
ATOM   8172  C  C     . TYR F 1 194 ? 22.169  -44.096 20.847  1 39.94 ? 194 TYR Z C     1 
ATOM   8173  O  O     . TYR F 1 194 ? 22.549  -45.242 20.602  1 40.2  ? 194 TYR Z O     1 
ATOM   8174  C  CB    . TYR F 1 194 ? 23.968  -43.066 22.265  1 40.41 ? 194 TYR Z CB    1 
ATOM   8175  C  CG    . TYR F 1 194 ? 25.185  -42.174 22.27   1 41.5  ? 194 TYR Z CG    1 
ATOM   8176  C  CD1   . TYR F 1 194 ? 26.367  -42.578 21.669  1 42.78 ? 194 TYR Z CD1   1 
ATOM   8177  C  CD2   . TYR F 1 194 ? 25.127  -40.892 22.79   1 42.42 ? 194 TYR Z CD2   1 
ATOM   8178  C  CE1   . TYR F 1 194 ? 27.47   -41.736 21.606  1 43.82 ? 194 TYR Z CE1   1 
ATOM   8179  C  CE2   . TYR F 1 194 ? 26.226  -40.045 22.744  1 43.5  ? 194 TYR Z CE2   1 
ATOM   8180  C  CZ    . TYR F 1 194 ? 27.399  -40.472 22.152  1 44.61 ? 194 TYR Z CZ    1 
ATOM   8181  O  OH    . TYR F 1 194 ? 28.495  -39.647 22.081  1 46.11 ? 194 TYR Z OH    1 
ATOM   8182  N  N     . ASP F 1 195 ? 20.878  -43.787 21.05   1 39.29 ? 195 ASP Z N     1 
ATOM   8183  C  CA    . ASP F 1 195 ? 19.845  -44.821 21.008  1 39.24 ? 195 ASP Z CA    1 
ATOM   8184  C  C     . ASP F 1 195 ? 18.865  -44.647 19.87   1 38.72 ? 195 ASP Z C     1 
ATOM   8185  O  O     . ASP F 1 195 ? 18.158  -43.647 19.805  1 38.49 ? 195 ASP Z O     1 
ATOM   8186  C  CB    . ASP F 1 195 ? 19.105  -44.917 22.344  1 41.33 ? 195 ASP Z CB    1 
ATOM   8187  C  CG    . ASP F 1 195 ? 18.472  -46.274 22.596  1 46.35 ? 195 ASP Z CG    1 
ATOM   8188  O  OD1   . ASP F 1 195 ? 17.901  -46.853 21.644  1 47.07 ? 195 ASP Z OD1   1 
ATOM   8189  O  OD2   . ASP F 1 195 ? 18.544  -46.755 23.746  1 48.7  ? 195 ASP Z OD2   1 
ATOM   8190  N  N     . LYS F 1 196 ? 18.78   -45.665 19.011  1 38.53 ? 196 LYS Z N     1 
ATOM   8191  C  CA    . LYS F 1 196 ? 17.893  -45.665 17.856  1 38.83 ? 196 LYS Z CA    1 
ATOM   8192  C  C     . LYS F 1 196 ? 16.413  -45.656 18.218  1 38.7  ? 196 LYS Z C     1 
ATOM   8193  O  O     . LYS F 1 196 ? 15.605  -45.201 17.414  1 38.95 ? 196 LYS Z O     1 
ATOM   8194  C  CB    . LYS F 1 196 ? 18.223  -46.833 16.917  1 40.88 ? 196 LYS Z CB    1 
ATOM   8195  C  CG    . LYS F 1 196 ? 19.674  -46.88  16.454  1 45.24 ? 196 LYS Z CG    1 
ATOM   8196  C  CD    . LYS F 1 196 ? 20.129  -45.613 15.73   1 49.08 ? 196 LYS Z CD    1 
ATOM   8197  C  CE    . LYS F 1 196 ? 21.318  -45.881 14.842  1 52.29 ? 196 LYS Z CE    1 
ATOM   8198  N  NZ    . LYS F 1 196 ? 22.429  -46.547 15.578  1 54.32 ? 196 LYS Z NZ    1 
ATOM   8199  N  N     . LYS F 1 197 ? 16.052  -46.129 19.418  1 38.14 ? 197 LYS Z N     1 
ATOM   8200  C  CA    . LYS F 1 197 ? 14.653  -46.118 19.85   1 38.34 ? 197 LYS Z CA    1 
ATOM   8201  C  C     . LYS F 1 197 ? 14.112  -44.691 19.997  1 38.39 ? 197 LYS Z C     1 
ATOM   8202  O  O     . LYS F 1 197 ? 12.91   -44.48  19.872  1 38.62 ? 197 LYS Z O     1 
ATOM   8203  C  CB    . LYS F 1 197 ? 14.487  -46.871 21.181  1 40.31 ? 197 LYS Z CB    1 
ATOM   8204  C  CG    . LYS F 1 197 ? 14.701  -48.37  21.073  1 44.38 ? 197 LYS Z CG    1 
ATOM   8205  C  CD    . LYS F 1 197 ? 14.486  -49.06  22.408  1 48.46 ? 197 LYS Z CD    1 
ATOM   8206  C  CE    . LYS F 1 197 ? 14.542  -50.561 22.257  1 52.13 ? 197 LYS Z CE    1 
ATOM   8207  N  NZ    . LYS F 1 197 ? 13.499  -51.062 21.321  1 54.09 ? 197 LYS Z NZ    1 
ATOM   8208  N  N     . LEU F 1 198 ? 14.992  -43.715 20.275  1 37.96 ? 198 LEU Z N     1 
ATOM   8209  C  CA    . LEU F 1 198 ? 14.609  -42.316 20.462  1 37.77 ? 198 LEU Z CA    1 
ATOM   8210  C  C     . LEU F 1 198 ? 14.771  -41.461 19.208  1 37.5  ? 198 LEU Z C     1 
ATOM   8211  O  O     . LEU F 1 198 ? 14.565  -40.25  19.296  1 37.93 ? 198 LEU Z O     1 
ATOM   8212  C  CB    . LEU F 1 198 ? 15.441  -41.688 21.582  1 37.9  ? 198 LEU Z CB    1 
ATOM   8213  C  CG    . LEU F 1 198 ? 15.448  -42.429 22.902  1 39.64 ? 198 LEU Z CG    1 
ATOM   8214  C  CD1   . LEU F 1 198 ? 16.532  -41.902 23.809  1 40.21 ? 198 LEU Z CD1   1 
ATOM   8215  C  CD2   . LEU F 1 198 ? 14.093  -42.36  23.569  1 40.51 ? 198 LEU Z CD2   1 
ATOM   8216  N  N     . LYS F 1 199 ? 15.152  -42.054 18.058  1 36.54 ? 199 LYS Z N     1 
ATOM   8217  C  CA    . LYS F 1 199 ? 15.361  -41.311 16.818  1 36.16 ? 199 LYS Z CA    1 
ATOM   8218  C  C     . LYS F 1 199 ? 14.187  -40.424 16.428  1 35.66 ? 199 LYS Z C     1 
ATOM   8219  O  O     . LYS F 1 199 ? 14.401  -39.308 15.957  1 35.89 ? 199 LYS Z O     1 
ATOM   8220  C  CB    . LYS F 1 199 ? 15.725  -42.249 15.659  1 37.69 ? 199 LYS Z CB    1 
ATOM   8221  C  CG    . LYS F 1 199 ? 17.205  -42.593 15.594  1 41.43 ? 199 LYS Z CG    1 
ATOM   8222  C  CD    . LYS F 1 199 ? 17.741  -42.545 14.163  1 45.75 ? 199 LYS Z CD    1 
ATOM   8223  C  CE    . LYS F 1 199 ? 17.203  -43.647 13.274  1 49.37 ? 199 LYS Z CE    1 
ATOM   8224  N  NZ    . LYS F 1 199 ? 17.884  -44.956 13.505  1 51.32 ? 199 LYS Z NZ    1 
ATOM   8225  N  N     . PHE F 1 200 ? 12.954  -40.893 16.656  1 34.85 ? 200 PHE Z N     1 
ATOM   8226  C  CA    . PHE F 1 200 ? 11.779  -40.119 16.288  1 34.61 ? 200 PHE Z CA    1 
ATOM   8227  C  C     . PHE F 1 200 ? 11.033  -39.525 17.474  1 34.31 ? 200 PHE Z C     1 
ATOM   8228  O  O     . PHE F 1 200 ? 9.811   -39.424 17.436  1 34.53 ? 200 PHE Z O     1 
ATOM   8229  C  CB    . PHE F 1 200 ? 10.852  -40.947 15.395  1 34.51 ? 200 PHE Z CB    1 
ATOM   8230  C  CG    . PHE F 1 200 ? 11.566  -41.413 14.15   1 34.95 ? 200 PHE Z CG    1 
ATOM   8231  C  CD1   . PHE F 1 200 ? 11.98   -40.506 13.189  1 35.69 ? 200 PHE Z CD1   1 
ATOM   8232  C  CD2   . PHE F 1 200 ? 11.889  -42.744 13.976  1 35.63 ? 200 PHE Z CD2   1 
ATOM   8233  C  CE1   . PHE F 1 200 ? 12.67   -40.929 12.062  1 36.3  ? 200 PHE Z CE1   1 
ATOM   8234  C  CE2   . PHE F 1 200 ? 12.58   -43.163 12.848  1 36.33 ? 200 PHE Z CE2   1 
ATOM   8235  C  CZ    . PHE F 1 200 ? 12.968  -42.253 11.899  1 36.09 ? 200 PHE Z CZ    1 
ATOM   8236  N  N     . PHE F 1 201 ? 11.761  -39.101 18.515  1 33.69 ? 201 PHE Z N     1 
ATOM   8237  C  CA    . PHE F 1 201 ? 11.134  -38.458 19.668  1 33.5  ? 201 PHE Z CA    1 
ATOM   8238  C  C     . PHE F 1 201 ? 11.141  -36.943 19.439  1 33.72 ? 201 PHE Z C     1 
ATOM   8239  O  O     . PHE F 1 201 ? 12.168  -36.397 19.036  1 34.03 ? 201 PHE Z O     1 
ATOM   8240  C  CB    . PHE F 1 201 ? 11.873  -38.802 20.972  1 32.95 ? 201 PHE Z CB    1 
ATOM   8241  C  CG    . PHE F 1 201 ? 11.2    -38.21  22.184  1 33.23 ? 201 PHE Z CG    1 
ATOM   8242  C  CD1   . PHE F 1 201 ? 9.965   -38.668 22.603  1 33.95 ? 201 PHE Z CD1   1 
ATOM   8243  C  CD2   . PHE F 1 201 ? 11.789  -37.182 22.89   1 33.95 ? 201 PHE Z CD2   1 
ATOM   8244  C  CE1   . PHE F 1 201 ? 9.341   -38.114 23.713  1 34.67 ? 201 PHE Z CE1   1 
ATOM   8245  C  CE2   . PHE F 1 201 ? 11.154  -36.62  23.991  1 34.64 ? 201 PHE Z CE2   1 
ATOM   8246  C  CZ    . PHE F 1 201 ? 9.938   -37.093 24.399  1 34.45 ? 201 PHE Z CZ    1 
ATOM   8247  N  N     . ASP F 1 202 ? 10.006  -36.262 19.668  1 33.34 ? 202 ASP Z N     1 
ATOM   8248  C  CA    . ASP F 1 202 ? 9.939   -34.81  19.493  1 33.41 ? 202 ASP Z CA    1 
ATOM   8249  C  C     . ASP F 1 202 ? 10.269  -34.145 20.83   1 33.17 ? 202 ASP Z C     1 
ATOM   8250  O  O     . ASP F 1 202 ? 9.502   -34.286 21.781  1 33.62 ? 202 ASP Z O     1 
ATOM   8251  C  CB    . ASP F 1 202 ? 8.537   -34.377 19.01   1 35.17 ? 202 ASP Z CB    1 
ATOM   8252  C  CG    . ASP F 1 202 ? 8.467   -32.96  18.452  1 39.54 ? 202 ASP Z CG    1 
ATOM   8253  O  OD1   . ASP F 1 202 ? 9.538   -32.332 18.272  1 40.35 ? 202 ASP Z OD1   1 
ATOM   8254  O  OD2   . ASP F 1 202 ? 7.339   -32.481 18.185  1 41.31 ? 202 ASP Z OD2   1 
ATOM   8255  N  N     . GLU F 1 203 ? 11.398  -33.416 20.913  1 32.23 ? 203 GLU Z N     1 
ATOM   8256  C  CA    . GLU F 1 203 ? 11.803  -32.779 22.162  1 31.79 ? 203 GLU Z CA    1 
ATOM   8257  C  C     . GLU F 1 203 ? 10.857  -31.687 22.648  1 31.52 ? 203 GLU Z C     1 
ATOM   8258  O  O     . GLU F 1 203 ? 11.011  -31.238 23.778  1 31.71 ? 203 GLU Z O     1 
ATOM   8259  C  CB    . GLU F 1 203 ? 13.238  -32.274 22.088  1 33.65 ? 203 GLU Z CB    1 
ATOM   8260  C  CG    . GLU F 1 203 ? 14.242  -33.412 22.066  1 38.22 ? 203 GLU Z CG    1 
ATOM   8261  C  CD    . GLU F 1 203 ? 15.702  -33     22.013  1 44.57 ? 203 GLU Z CD    1 
ATOM   8262  O  OE1   . GLU F 1 203 ? 15.989  -31.799 22.208  1 46.18 ? 203 GLU Z OE1   1 
ATOM   8263  O  OE2   . GLU F 1 203 ? 16.564  -33.873 21.774  1 46.5  ? 203 GLU Z OE2   1 
ATOM   8264  N  N     . THR F 1 204 ? 9.856   -31.292 21.845  1 31.31 ? 204 THR Z N     1 
ATOM   8265  C  CA    . THR F 1 204 ? 8.848   -30.337 22.315  1 31.96 ? 204 THR Z CA    1 
ATOM   8266  C  C     . THR F 1 204 ? 7.898   -30.99  23.347  1 32.35 ? 204 THR Z C     1 
ATOM   8267  O  O     . THR F 1 204 ? 7.168   -30.268 24.019  1 32.88 ? 204 THR Z O     1 
ATOM   8268  C  CB    . THR F 1 204 ? 8.076   -29.693 21.16   1 33.67 ? 204 THR Z CB    1 
ATOM   8269  O  OG1   . THR F 1 204 ? 7.111   -30.614 20.643  1 35.03 ? 204 THR Z OG1   1 
ATOM   8270  C  CG2   . THR F 1 204 ? 8.987   -29.19  20.053  1 34.13 ? 204 THR Z CG2   1 
ATOM   8271  N  N     . ILE F 1 205 ? 7.908   -32.347 23.471  1 31.73 ? 205 ILE Z N     1 
ATOM   8272  C  CA    . ILE F 1 205 ? 7.111   -33.103 24.43   1 31.47 ? 205 ILE Z CA    1 
ATOM   8273  C  C     . ILE F 1 205 ? 7.528   -32.76  25.863  1 31.18 ? 205 ILE Z C     1 
ATOM   8274  O  O     . ILE F 1 205 ? 6.672   -32.743 26.743  1 31.29 ? 205 ILE Z O     1 
ATOM   8275  C  CB    . ILE F 1 205 ? 7.198   -34.622 24.122  1 32.12 ? 205 ILE Z CB    1 
ATOM   8276  C  CG1   . ILE F 1 205 ? 6.426   -34.957 22.836  1 33.2  ? 205 ILE Z CG1   1 
ATOM   8277  C  CG2   . ILE F 1 205 ? 6.706   -35.482 25.29   1 32.71 ? 205 ILE Z CG2   1 
ATOM   8278  C  CD1   . ILE F 1 205 ? 6.606   -36.348 22.333  1 34.54 ? 205 ILE Z CD1   1 
ATOM   8279  N  N     . PHE F 1 206 ? 8.822   -32.449 26.1    1 30.91 ? 206 PHE Z N     1 
ATOM   8280  C  CA    . PHE F 1 206 ? 9.304   -32.086 27.434  1 31.59 ? 206 PHE Z CA    1 
ATOM   8281  C  C     . PHE F 1 206 ? 8.519   -30.885 28.011  1 32.37 ? 206 PHE Z C     1 
ATOM   8282  O  O     . PHE F 1 206 ? 8.263   -29.913 27.301  1 32.45 ? 206 PHE Z O     1 
ATOM   8283  C  CB    . PHE F 1 206 ? 10.821  -31.846 27.44   1 31.42 ? 206 PHE Z CB    1 
ATOM   8284  C  CG    . PHE F 1 206 ? 11.649  -33.064 27.095  1 32.07 ? 206 PHE Z CG    1 
ATOM   8285  C  CD1   . PHE F 1 206 ? 11.452  -34.266 27.751  1 32.89 ? 206 PHE Z CD1   1 
ATOM   8286  C  CD2   . PHE F 1 206 ? 12.654  -32.993 26.149  1 32.81 ? 206 PHE Z CD2   1 
ATOM   8287  C  CE1   . PHE F 1 206 ? 12.213  -35.385 27.427  1 33.48 ? 206 PHE Z CE1   1 
ATOM   8288  C  CE2   . PHE F 1 206 ? 13.415  -34.111 25.836  1 33.41 ? 206 PHE Z CE2   1 
ATOM   8289  C  CZ    . PHE F 1 206 ? 13.207  -35.29  26.492  1 33.19 ? 206 PHE Z CZ    1 
ATOM   8290  N  N     . ALA F 1 207 ? 8.069   -30.998 29.275  1 32.56 ? 207 ALA Z N     1 
ATOM   8291  C  CA    . ALA F 1 207 ? 7.207   -29.992 29.887  1 32.93 ? 207 ALA Z CA    1 
ATOM   8292  C  C     . ALA F 1 207 ? 7.782   -29.259 31.108  1 33.16 ? 207 ALA Z C     1 
ATOM   8293  O  O     . ALA F 1 207 ? 6.999   -28.786 31.932  1 33.22 ? 207 ALA Z O     1 
ATOM   8294  C  CB    . ALA F 1 207 ? 5.869   -30.628 30.248  1 32.94 ? 207 ALA Z CB    1 
ATOM   8295  N  N     . GLU F 1 208 ? 9.116   -29.111 31.213  1 33.15 ? 208 GLU Z N     1 
ATOM   8296  C  CA    . GLU F 1 208 ? 9.705   -28.397 32.351  1 33.74 ? 208 GLU Z CA    1 
ATOM   8297  C  C     . GLU F 1 208 ? 9.174   -26.963 32.504  1 34.35 ? 208 GLU Z C     1 
ATOM   8298  O  O     . GLU F 1 208 ? 8.719   -26.587 33.587  1 34.57 ? 208 GLU Z O     1 
ATOM   8299  C  CB    . GLU F 1 208 ? 11.238  -28.39  32.281  1 35.57 ? 208 GLU Z CB    1 
ATOM   8300  C  CG    . GLU F 1 208 ? 11.873  -29.705 32.68   1 39.48 ? 208 GLU Z CG    1 
ATOM   8301  C  CD    . GLU F 1 208 ? 12.324  -30.554 31.511  1 45.19 ? 208 GLU Z CD    1 
ATOM   8302  O  OE1   . GLU F 1 208 ? 11.794  -30.357 30.394  1 45.9  ? 208 GLU Z OE1   1 
ATOM   8303  O  OE2   . GLU F 1 208 ? 13.207  -31.421 31.712  1 47.79 ? 208 GLU Z OE2   1 
ATOM   8304  N  N     . ASP F 1 209 ? 9.209   -26.175 31.423  1 34.46 ? 209 ASP Z N     1 
ATOM   8305  C  CA    . ASP F 1 209 ? 8.732   -24.797 31.471  1 35.06 ? 209 ASP Z CA    1 
ATOM   8306  C  C     . ASP F 1 209 ? 7.221   -24.695 31.647  1 34.72 ? 209 ASP Z C     1 
ATOM   8307  O  O     . ASP F 1 209 ? 6.758   -23.835 32.384  1 34.76 ? 209 ASP Z O     1 
ATOM   8308  C  CB    . ASP F 1 209 ? 9.174   -24.019 30.224  1 37.61 ? 209 ASP Z CB    1 
ATOM   8309  C  CG    . ASP F 1 209 ? 10.619  -23.559 30.267  1 43    ? 209 ASP Z CG    1 
ATOM   8310  O  OD1   . ASP F 1 209 ? 11.423  -24.19  30.994  1 43.92 ? 209 ASP Z OD1   1 
ATOM   8311  O  OD2   . ASP F 1 209 ? 10.947  -22.567 29.575  1 45.13 ? 209 ASP Z OD2   1 
ATOM   8312  N  N     . ASP F 1 210 ? 6.456   -25.565 30.987  1 34.24 ? 210 ASP Z N     1 
ATOM   8313  C  CA    . ASP F 1 210 ? 4.998   -25.514 31.065  1 34.11 ? 210 ASP Z CA    1 
ATOM   8314  C  C     . ASP F 1 210 ? 4.429   -25.945 32.405  1 33.17 ? 210 ASP Z C     1 
ATOM   8315  O  O     . ASP F 1 210 ? 3.371   -25.455 32.791  1 33.27 ? 210 ASP Z O     1 
ATOM   8316  C  CB    . ASP F 1 210 ? 4.365   -26.302 29.921  1 36.43 ? 210 ASP Z CB    1 
ATOM   8317  C  CG    . ASP F 1 210 ? 4.566   -25.655 28.562  1 41.7  ? 210 ASP Z CG    1 
ATOM   8318  O  OD1   . ASP F 1 210 ? 4.856   -24.432 28.516  1 42.41 ? 210 ASP Z OD1   1 
ATOM   8319  O  OD2   . ASP F 1 210 ? 4.416   -26.358 27.546  1 44.15 ? 210 ASP Z OD2   1 
ATOM   8320  N  N     . ILE F 1 211 ? 5.12    -26.838 33.121  1 32.2  ? 211 ILE Z N     1 
ATOM   8321  C  CA    . ILE F 1 211 ? 4.673   -27.254 34.45   1 31.68 ? 211 ILE Z CA    1 
ATOM   8322  C  C     . ILE F 1 211 ? 4.861   -26.097 35.427  1 30.55 ? 211 ILE Z C     1 
ATOM   8323  O  O     . ILE F 1 211 ? 3.95    -25.795 36.193  1 30.53 ? 211 ILE Z O     1 
ATOM   8324  C  CB    . ILE F 1 211 ? 5.372   -28.564 34.905  1 32.53 ? 211 ILE Z CB    1 
ATOM   8325  C  CG1   . ILE F 1 211 ? 4.811   -29.766 34.132  1 33.78 ? 211 ILE Z CG1   1 
ATOM   8326  C  CG2   . ILE F 1 211 ? 5.243   -28.79  36.416  1 33.06 ? 211 ILE Z CG2   1 
ATOM   8327  C  CD1   . ILE F 1 211 ? 3.304   -29.965 34.296  1 35.3  ? 211 ILE Z CD1   1 
ATOM   8328  N  N     . ALA F 1 212 ? 6.01    -25.406 35.346  1 29.58 ? 212 ALA Z N     1 
ATOM   8329  C  CA    . ALA F 1 212 ? 6.29    -24.24  36.176  1 29.3  ? 212 ALA Z CA    1 
ATOM   8330  C  C     . ALA F 1 212 ? 5.252   -23.137 35.914  1 28.78 ? 212 ALA Z C     1 
ATOM   8331  O  O     . ALA F 1 212 ? 4.709   -22.575 36.859  1 28.87 ? 212 ALA Z O     1 
ATOM   8332  C  CB    . ALA F 1 212 ? 7.698   -23.725 35.898  1 29.48 ? 212 ALA Z CB    1 
ATOM   8333  N  N     . ASP F 1 213 ? 4.927   -22.886 34.635  1 28.22 ? 213 ASP Z N     1 
ATOM   8334  C  CA    . ASP F 1 213 ? 3.939   -21.89  34.217  1 28.02 ? 213 ASP Z CA    1 
ATOM   8335  C  C     . ASP F 1 213 ? 2.551   -22.225 34.751  1 27.58 ? 213 ASP Z C     1 
ATOM   8336  O  O     . ASP F 1 213 ? 1.834   -21.332 35.19   1 27.75 ? 213 ASP Z O     1 
ATOM   8337  C  CB    . ASP F 1 213 ? 3.886   -21.784 32.678  1 29.39 ? 213 ASP Z CB    1 
ATOM   8338  C  CG    . ASP F 1 213 ? 5.062   -21.075 32.043  1 33.52 ? 213 ASP Z CG    1 
ATOM   8339  O  OD1   . ASP F 1 213 ? 5.861   -20.47  32.785  1 34.13 ? 213 ASP Z OD1   1 
ATOM   8340  O  OD2   . ASP F 1 213 ? 5.188   -21.132 30.806  1 35.88 ? 213 ASP Z OD2   1 
ATOM   8341  N  N     . TYR F 1 214 ? 2.172   -23.505 34.705  1 26.88 ? 214 TYR Z N     1 
ATOM   8342  C  CA    . TYR F 1 214 ? 0.875   -23.956 35.189  1 26.74 ? 214 TYR Z CA    1 
ATOM   8343  C  C     . TYR F 1 214 ? 0.75    -23.693 36.686  1 25.99 ? 214 TYR Z C     1 
ATOM   8344  O  O     . TYR F 1 214 ? -0.253  -23.134 37.124  1 26.1  ? 214 TYR Z O     1 
ATOM   8345  C  CB    . TYR F 1 214 ? 0.665   -25.457 34.876  1 27.11 ? 214 TYR Z CB    1 
ATOM   8346  C  CG    . TYR F 1 214 ? -0.616  -26.004 35.464  1 28.22 ? 214 TYR Z CG    1 
ATOM   8347  C  CD1   . TYR F 1 214 ? -1.843  -25.727 34.882  1 29.34 ? 214 TYR Z CD1   1 
ATOM   8348  C  CD2   . TYR F 1 214 ? -0.608  -26.728 36.648  1 29.31 ? 214 TYR Z CD2   1 
ATOM   8349  C  CE1   . TYR F 1 214 ? -3.028  -26.18  35.445  1 30.41 ? 214 TYR Z CE1   1 
ATOM   8350  C  CE2   . TYR F 1 214 ? -1.788  -27.179 37.226  1 30.35 ? 214 TYR Z CE2   1 
ATOM   8351  C  CZ    . TYR F 1 214 ? -2.998  -26.904 36.62   1 31.31 ? 214 TYR Z CZ    1 
ATOM   8352  O  OH    . TYR F 1 214 ? -4.175  -27.352 37.166  1 32.56 ? 214 TYR Z OH    1 
ATOM   8353  N  N     . ILE F 1 215 ? 1.763   -24.103 37.466  1 25.24 ? 215 ILE Z N     1 
ATOM   8354  C  CA    . ILE F 1 215 ? 1.769   -23.933 38.913  1 24.89 ? 215 ILE Z CA    1 
ATOM   8355  C  C     . ILE F 1 215 ? 1.665   -22.464 39.292  1 24.76 ? 215 ILE Z C     1 
ATOM   8356  O  O     . ILE F 1 215 ? 0.778   -22.102 40.06   1 25.47 ? 215 ILE Z O     1 
ATOM   8357  C  CB    . ILE F 1 215 ? 2.989   -24.634 39.562  1 25.13 ? 215 ILE Z CB    1 
ATOM   8358  C  CG1   . ILE F 1 215 ? 2.941   -26.153 39.332  1 25.83 ? 215 ILE Z CG1   1 
ATOM   8359  C  CG2   . ILE F 1 215 ? 3.083   -24.318 41.044  1 25.56 ? 215 ILE Z CG2   1 
ATOM   8360  C  CD1   . ILE F 1 215 ? 4.226   -26.862 39.673  1 26.94 ? 215 ILE Z CD1   1 
ATOM   8361  N  N     . ILE F 1 216 ? 2.504   -21.611 38.704  1 23.89 ? 216 ILE Z N     1 
ATOM   8362  C  CA    . ILE F 1 216 ? 2.471   -20.185 39.006  1 23.69 ? 216 ILE Z CA    1 
ATOM   8363  C  C     . ILE F 1 216 ? 1.123   -19.549 38.658  1 24.28 ? 216 ILE Z C     1 
ATOM   8364  O  O     . ILE F 1 216 ? 0.606   -18.769 39.454  1 24.35 ? 216 ILE Z O     1 
ATOM   8365  C  CB    . ILE F 1 216 ? 3.666   -19.46  38.362  1 23.53 ? 216 ILE Z CB    1 
ATOM   8366  C  CG1   . ILE F 1 216 ? 4.973   -19.999 38.944  1 23.77 ? 216 ILE Z CG1   1 
ATOM   8367  C  CG2   . ILE F 1 216 ? 3.57    -17.955 38.583  1 24.01 ? 216 ILE Z CG2   1 
ATOM   8368  C  CD1   . ILE F 1 216 ? 6.138   -19.685 38.165  1 24.63 ? 216 ILE Z CD1   1 
ATOM   8369  N  N     . ALA F 1 217 ? 0.517   -19.927 37.522  1 24.74 ? 217 ALA Z N     1 
ATOM   8370  C  CA    . ALA F 1 217 ? -0.789  -19.379 37.141  1 25.71 ? 217 ALA Z CA    1 
ATOM   8371  C  C     . ALA F 1 217 ? -1.897  -19.821 38.107  1 26.78 ? 217 ALA Z C     1 
ATOM   8372  O  O     . ALA F 1 217 ? -2.794  -19.031 38.411  1 27.25 ? 217 ALA Z O     1 
ATOM   8373  C  CB    . ALA F 1 217 ? -1.14   -19.77  35.716  1 25.84 ? 217 ALA Z CB    1 
ATOM   8374  N  N     . LYS F 1 218 ? -1.821  -21.057 38.615  1 26.9  ? 218 LYS Z N     1 
ATOM   8375  C  CA    . LYS F 1 218 ? -2.8    -21.543 39.581  1 27.79 ? 218 LYS Z CA    1 
ATOM   8376  C  C     . LYS F 1 218 ? -2.649  -20.776 40.896  1 28.55 ? 218 LYS Z C     1 
ATOM   8377  O  O     . LYS F 1 218 ? -3.655  -20.348 41.46   1 28.68 ? 218 LYS Z O     1 
ATOM   8378  C  CB    . LYS F 1 218 ? -2.624  -23.042 39.826  1 29.66 ? 218 LYS Z CB    1 
ATOM   8379  C  CG    . LYS F 1 218 ? -3.583  -23.908 39.033  1 33.72 ? 218 LYS Z CG    1 
ATOM   8380  C  CD    . LYS F 1 218 ? -4.997  -23.792 39.58   1 37.91 ? 218 LYS Z CD    1 
ATOM   8381  C  CE    . LYS F 1 218 ? -5.853  -24.981 39.214  1 41.5  ? 218 LYS Z CE    1 
ATOM   8382  N  NZ    . LYS F 1 218 ? -5.887  -25.22  37.744  1 43.9  ? 218 LYS Z NZ    1 
ATOM   8383  N  N     . LEU F 1 219 ? -1.397  -20.553 41.35   1 28.86 ? 219 LEU Z N     1 
ATOM   8384  C  CA    . LEU F 1 219 ? -1.091  -19.805 42.576  1 29.66 ? 219 LEU Z CA    1 
ATOM   8385  C  C     . LEU F 1 219 ? -1.588  -18.351 42.483  1 30.89 ? 219 LEU Z C     1 
ATOM   8386  O  O     . LEU F 1 219 ? -2.055  -17.787 43.473  1 31.18 ? 219 LEU Z O     1 
ATOM   8387  C  CB    . LEU F 1 219 ? 0.42    -19.83  42.86   1 29.59 ? 219 LEU Z CB    1 
ATOM   8388  C  CG    . LEU F 1 219 ? 1.027   -21.193 43.164  1 30.79 ? 219 LEU Z CG    1 
ATOM   8389  C  CD1   . LEU F 1 219 ? 2.531   -21.119 43.243  1 31.24 ? 219 LEU Z CD1   1 
ATOM   8390  C  CD2   . LEU F 1 219 ? 0.489   -21.751 44.444  1 31.55 ? 219 LEU Z CD2   1 
ATOM   8391  N  N     . GLN F 1 220 ? -1.515  -17.763 41.287  1 31.41 ? 220 GLN Z N     1 
ATOM   8392  C  CA    . GLN F 1 220 ? -1.979  -16.407 41.021  1 32.55 ? 220 GLN Z CA    1 
ATOM   8393  C  C     . GLN F 1 220 ? -3.49   -16.306 40.741  1 32.91 ? 220 GLN Z C     1 
ATOM   8394  O  O     . GLN F 1 220 ? -3.987  -15.196 40.549  1 32.75 ? 220 GLN Z O     1 
ATOM   8395  C  CB    . GLN F 1 220 ? -1.233  -15.858 39.801  1 35.35 ? 220 GLN Z CB    1 
ATOM   8396  C  CG    . GLN F 1 220 ? 0.23    -15.516 40.067  1 40.88 ? 220 GLN Z CG    1 
ATOM   8397  C  CD    . GLN F 1 220 ? 0.45    -14.103 40.585  1 47.14 ? 220 GLN Z CD    1 
ATOM   8398  O  OE1   . GLN F 1 220 ? 1.561   -13.731 40.992  1 49.09 ? 220 GLN Z OE1   1 
ATOM   8399  N  NE2   . GLN F 1 220 ? -0.59   -13.268 40.57   1 48.22 ? 220 GLN Z NE2   1 
ATOM   8400  N  N     . HIS F 1 221 ? -4.205  -17.445 40.691  1 33.38 ? 221 HIS Z N     1 
ATOM   8401  C  CA    . HIS F 1 221 ? -5.625  -17.559 40.35   1 34.44 ? 221 HIS Z CA    1 
ATOM   8402  C  C     . HIS F 1 221 ? -5.911  -16.92  39.006  1 34.42 ? 221 HIS Z C     1 
ATOM   8403  O  O     . HIS F 1 221 ? -6.676  -15.958 38.915  1 34.88 ? 221 HIS Z O     1 
ATOM   8404  C  CB    . HIS F 1 221 ? -6.581  -17.047 41.441  1 36.33 ? 221 HIS Z CB    1 
ATOM   8405  C  CG    . HIS F 1 221 ? -8.002  -17.474 41.202  1 40.33 ? 221 HIS Z CG    1 
ATOM   8406  N  ND1   . HIS F 1 221 ? -8.387  -18.804 41.322  1 42.7  ? 221 HIS Z ND1   1 
ATOM   8407  C  CD2   . HIS F 1 221 ? -9.076  -16.743 40.815  1 41.82 ? 221 HIS Z CD2   1 
ATOM   8408  C  CE1   . HIS F 1 221 ? -9.677  -18.832 41.026  1 43.35 ? 221 HIS Z CE1   1 
ATOM   8409  N  NE2   . HIS F 1 221 ? -10.136 -17.618 40.71   1 43.21 ? 221 HIS Z NE2   1 
ATOM   8410  N  N     . ARG F 1 222 ? -5.237  -17.416 37.967  1 33.53 ? 222 ARG Z N     1 
ATOM   8411  C  CA    . ARG F 1 222 ? -5.41   -16.926 36.602  1 32.88 ? 222 ARG Z CA    1 
ATOM   8412  C  C     . ARG F 1 222 ? -5.981  -18.037 35.721  1 32.36 ? 222 ARG Z C     1 
ATOM   8413  O  O     . ARG F 1 222 ? -5.998  -19.195 36.139  1 32.59 ? 222 ARG Z O     1 
ATOM   8414  C  CB    . ARG F 1 222 ? -4.069  -16.439 36.048  1 33.69 ? 222 ARG Z CB    1 
ATOM   8415  C  CG    . ARG F 1 222 ? -3.569  -15.205 36.746  1 35.99 ? 222 ARG Z CG    1 
ATOM   8416  C  CD    . ARG F 1 222 ? -2.196  -14.809 36.27   1 39.19 ? 222 ARG Z CD    1 
ATOM   8417  N  NE    . ARG F 1 222 ? -1.846  -13.498 36.803  1 42.22 ? 222 ARG Z NE    1 
ATOM   8418  C  CZ    . ARG F 1 222 ? -0.608  -13.072 37.009  1 44.17 ? 222 ARG Z CZ    1 
ATOM   8419  N  NH1   . ARG F 1 222 ? 0.428   -13.859 36.739  1 43.19 ? 222 ARG Z NH1   1 
ATOM   8420  N  NH2   . ARG F 1 222 ? -0.393  -11.861 37.508  1 44.48 ? 222 ARG Z NH2   1 
ATOM   8421  N  N     . ASP F 1 223 ? -6.46   -17.698 34.51   1 31.64 ? 223 ASP Z N     1 
ATOM   8422  C  CA    . ASP F 1 223 ? -6.989  -18.711 33.601  1 31.44 ? 223 ASP Z CA    1 
ATOM   8423  C  C     . ASP F 1 223 ? -5.862  -19.61  33.118  1 31.38 ? 223 ASP Z C     1 
ATOM   8424  O  O     . ASP F 1 223 ? -4.919  -19.141 32.485  1 31.44 ? 223 ASP Z O     1 
ATOM   8425  C  CB    . ASP F 1 223 ? -7.726  -18.088 32.406  1 32.56 ? 223 ASP Z CB    1 
ATOM   8426  C  CG    . ASP F 1 223 ? -8.285  -19.124 31.445  1 36.49 ? 223 ASP Z CG    1 
ATOM   8427  O  OD1   . ASP F 1 223 ? -8.77   -20.17  31.917  1 37.17 ? 223 ASP Z OD1   1 
ATOM   8428  O  OD2   . ASP F 1 223 ? -8.205  -18.904 30.223  1 38.74 ? 223 ASP Z OD2   1 
ATOM   8429  N  N     . THR F 1 224 ? -5.961  -20.904 33.426  1 31.1  ? 224 THR Z N     1 
ATOM   8430  C  CA    . THR F 1 224 ? -4.957  -21.882 33.022  1 31.23 ? 224 THR Z CA    1 
ATOM   8431  C  C     . THR F 1 224 ? -5.361  -22.694 31.776  1 31.3  ? 224 THR Z C     1 
ATOM   8432  O  O     . THR F 1 224 ? -4.648  -23.623 31.436  1 31.15 ? 224 THR Z O     1 
ATOM   8433  C  CB    . THR F 1 224 ? -4.617  -22.815 34.199  1 32.21 ? 224 THR Z CB    1 
ATOM   8434  O  OG1   . THR F 1 224 ? -5.822  -23.342 34.76   1 33.15 ? 224 THR Z OG1   1 
ATOM   8435  C  CG2   . THR F 1 224 ? -3.82   -22.128 35.275  1 32.36 ? 224 THR Z CG2   1 
ATOM   8436  N  N     . SER F 1 225 ? -6.478  -22.356 31.102  1 31.35 ? 225 SER Z N     1 
ATOM   8437  C  CA    . SER F 1 225 ? -6.964  -23.086 29.928  1 31.94 ? 225 SER Z CA    1 
ATOM   8438  C  C     . SER F 1 225 ? -5.928  -23.236 28.835  1 32.48 ? 225 SER Z C     1 
ATOM   8439  O  O     . SER F 1 225 ? -5.81   -24.311 28.255  1 32.28 ? 225 SER Z O     1 
ATOM   8440  C  CB    . SER F 1 225 ? -8.217  -22.433 29.36   1 33.33 ? 225 SER Z CB    1 
ATOM   8441  O  OG    . SER F 1 225 ? -9.286  -22.487 30.29   1 35.73 ? 225 SER Z OG    1 
ATOM   8442  N  N     . ASN F 1 226 ? -5.178  -22.169 28.55   1 33.16 ? 226 ASN Z N     1 
ATOM   8443  C  CA    . ASN F 1 226 ? -4.147  -22.2   27.516  1 34.3  ? 226 ASN Z CA    1 
ATOM   8444  C  C     . ASN F 1 226 ? -2.995  -23.13  27.899  1 34.47 ? 226 ASN Z C     1 
ATOM   8445  O  O     . ASN F 1 226 ? -2.573  -23.938 27.074  1 34.49 ? 226 ASN Z O     1 
ATOM   8446  C  CB    . ASN F 1 226 ? -3.631  -20.788 27.214  1 36.27 ? 226 ASN Z CB    1 
ATOM   8447  C  CG    . ASN F 1 226 ? -4.649  -19.886 26.557  1 40.34 ? 226 ASN Z CG    1 
ATOM   8448  O  OD1   . ASN F 1 226 ? -5.66   -20.341 26.005  1 42.06 ? 226 ASN Z OD1   1 
ATOM   8449  N  ND2   . ASN F 1 226 ? -4.398  -18.586 26.594  1 40.81 ? 226 ASN Z ND2   1 
ATOM   8450  N  N     . ILE F 1 227 ? -2.504  -23.034 29.152  1 34.37 ? 227 ILE Z N     1 
ATOM   8451  C  CA    . ILE F 1 227 ? -1.417  -23.884 29.651  1 34.61 ? 227 ILE Z CA    1 
ATOM   8452  C  C     . ILE F 1 227 ? -1.869  -25.335 29.699  1 34.6  ? 227 ILE Z C     1 
ATOM   8453  O  O     . ILE F 1 227 ? -1.109  -26.226 29.327  1 35.08 ? 227 ILE Z O     1 
ATOM   8454  C  CB    . ILE F 1 227 ? -0.881  -23.416 31.03   1 35.26 ? 227 ILE Z CB    1 
ATOM   8455  C  CG1   . ILE F 1 227 ? -0.62   -21.9   31.043  1 36.49 ? 227 ILE Z CG1   1 
ATOM   8456  C  CG2   . ILE F 1 227 ? 0.378   -24.187 31.41   1 35.61 ? 227 ILE Z CG2   1 
ATOM   8457  C  CD1   . ILE F 1 227 ? -0.297  -21.345 32.407  1 38.01 ? 227 ILE Z CD1   1 
ATOM   8458  N  N     . GLU F 1 228 ? -3.123  -25.574 30.102  1 33.98 ? 228 GLU Z N     1 
ATOM   8459  C  CA    . GLU F 1 228 ? -3.699  -26.908 30.154  1 33.93 ? 228 GLU Z CA    1 
ATOM   8460  C  C     . GLU F 1 228 ? -3.727  -27.519 28.759  1 33.78 ? 228 GLU Z C     1 
ATOM   8461  O  O     . GLU F 1 228 ? -3.299  -28.653 28.606  1 33.99 ? 228 GLU Z O     1 
ATOM   8462  C  CB    . GLU F 1 228 ? -5.105  -26.886 30.782  1 35.91 ? 228 GLU Z CB    1 
ATOM   8463  C  CG    . GLU F 1 228 ? -5.098  -26.646 32.286  1 39.44 ? 228 GLU Z CG    1 
ATOM   8464  C  CD    . GLU F 1 228 ? -6.463  -26.528 32.937  1 44.09 ? 228 GLU Z CD    1 
ATOM   8465  O  OE1   . GLU F 1 228 ? -7.375  -27.297 32.559  1 45.33 ? 228 GLU Z OE1   1 
ATOM   8466  O  OE2   . GLU F 1 228 ? -6.615  -25.682 33.847  1 45.53 ? 228 GLU Z OE2   1 
ATOM   8467  N  N     . GLN F 1 229 ? -4.119  -26.75  27.737  1 33.29 ? 229 GLN Z N     1 
ATOM   8468  C  CA    . GLN F 1 229 ? -4.136  -27.251 26.357  1 33.17 ? 229 GLN Z CA    1 
ATOM   8469  C  C     . GLN F 1 229 ? -2.742  -27.59  25.84   1 32.41 ? 229 GLN Z C     1 
ATOM   8470  O  O     . GLN F 1 229 ? -2.595  -28.567 25.117  1 32.14 ? 229 GLN Z O     1 
ATOM   8471  C  CB    . GLN F 1 229 ? -4.836  -26.275 25.404  1 34.95 ? 229 GLN Z CB    1 
ATOM   8472  C  CG    . GLN F 1 229 ? -6.212  -26.735 24.96   1 38.54 ? 229 GLN Z CG    1 
ATOM   8473  C  CD    . GLN F 1 229 ? -7.209  -25.625 25.169  1 42.86 ? 229 GLN Z CD    1 
ATOM   8474  O  OE1   . GLN F 1 229 ? -6.925  -24.442 24.925  1 44.11 ? 229 GLN Z OE1   1 
ATOM   8475  N  NE2   . GLN F 1 229 ? -8.404  -25.984 25.62   1 43.49 ? 229 GLN Z NE2   1 
ATOM   8476  N  N     . LEU F 1 230 ? -1.724  -26.807 26.222  1 32    ? 230 LEU Z N     1 
ATOM   8477  C  CA    . LEU F 1 230 ? -0.346  -27.073 25.816  1 32.18 ? 230 LEU Z CA    1 
ATOM   8478  C  C     . LEU F 1 230 ? 0.118   -28.38  26.442  1 32    ? 230 LEU Z C     1 
ATOM   8479  O  O     . LEU F 1 230 ? 0.727   -29.196 25.753  1 32.15 ? 230 LEU Z O     1 
ATOM   8480  C  CB    . LEU F 1 230 ? 0.599   -25.929 26.229  1 32.62 ? 230 LEU Z CB    1 
ATOM   8481  C  CG    . LEU F 1 230 ? 0.45    -24.597 25.478  1 34.37 ? 230 LEU Z CG    1 
ATOM   8482  C  CD1   . LEU F 1 230 ? 1.414   -23.548 26.016  1 34.92 ? 230 LEU Z CD1   1 
ATOM   8483  C  CD2   . LEU F 1 230 ? 0.676   -24.776 23.992  1 35.19 ? 230 LEU Z CD2   1 
ATOM   8484  N  N     . LEU F 1 231 ? -0.207  -28.597 27.732  1 31.49 ? 231 LEU Z N     1 
ATOM   8485  C  CA    . LEU F 1 231 ? 0.147   -29.821 28.454  1 31.77 ? 231 LEU Z CA    1 
ATOM   8486  C  C     . LEU F 1 231 ? -0.611  -31.066 27.946  1 31.5  ? 231 LEU Z C     1 
ATOM   8487  O  O     . LEU F 1 231 ? -0.025  -32.147 27.875  1 31.68 ? 231 LEU Z O     1 
ATOM   8488  C  CB    . LEU F 1 231 ? -0.035  -29.629 29.963  1 32.15 ? 231 LEU Z CB    1 
ATOM   8489  C  CG    . LEU F 1 231 ? 0.975   -28.683 30.606  1 33.61 ? 231 LEU Z CG    1 
ATOM   8490  C  CD1   . LEU F 1 231 ? 0.539   -28.283 31.989  1 33.93 ? 231 LEU Z CD1   1 
ATOM   8491  C  CD2   . LEU F 1 231 ? 2.353   -29.309 30.649  1 34.49 ? 231 LEU Z CD2   1 
ATOM   8492  N  N     . ILE F 1 232 ? -1.894  -30.91  27.569  1 30.8  ? 232 ILE Z N     1 
ATOM   8493  C  CA    . ILE F 1 232 ? -2.695  -31.991 26.99   1 30.51 ? 232 ILE Z CA    1 
ATOM   8494  C  C     . ILE F 1 232 ? -2.103  -32.348 25.627  1 30.34 ? 232 ILE Z C     1 
ATOM   8495  O  O     . ILE F 1 232 ? -1.948  -33.526 25.332  1 30.41 ? 232 ILE Z O     1 
ATOM   8496  C  CB    . ILE F 1 232 ? -4.185  -31.582 26.859  1 30.87 ? 232 ILE Z CB    1 
ATOM   8497  C  CG1   . ILE F 1 232 ? -4.833  -31.372 28.225  1 32.03 ? 232 ILE Z CG1   1 
ATOM   8498  C  CG2   . ILE F 1 232 ? -4.98   -32.588 26.033  1 31.21 ? 232 ILE Z CG2   1 
ATOM   8499  C  CD1   . ILE F 1 232 ? -4.781  -32.569 29.134  1 33.59 ? 232 ILE Z CD1   1 
ATOM   8500  N  N     . ASN F 1 233 ? -1.716  -31.333 24.82   1 29.9  ? 233 ASN Z N     1 
ATOM   8501  C  CA    . ASN F 1 233 ? -1.104  -31.554 23.509  1 29.75 ? 233 ASN Z CA    1 
ATOM   8502  C  C     . ASN F 1 233 ? 0.223   -32.308 23.611  1 28.92 ? 233 ASN Z C     1 
ATOM   8503  O  O     . ASN F 1 233 ? 0.505   -33.138 22.753  1 29.08 ? 233 ASN Z O     1 
ATOM   8504  C  CB    . ASN F 1 233 ? -0.932  -30.251 22.738  1 31.19 ? 233 ASN Z CB    1 
ATOM   8505  C  CG    . ASN F 1 233 ? -2.218  -29.728 22.139  1 34.91 ? 233 ASN Z CG    1 
ATOM   8506  O  OD1   . ASN F 1 233 ? -3.247  -30.423 22.086  1 35.88 ? 233 ASN Z OD1   1 
ATOM   8507  N  ND2   . ASN F 1 233 ? -2.189  -28.475 21.688  1 36.07 ? 233 ASN Z ND2   1 
ATOM   8508  N  N     . LYS F 1 234 ? 1.016   -32.06  24.665  1 27.9  ? 234 LYS Z N     1 
ATOM   8509  C  CA    . LYS F 1 234 ? 2.267   -32.791 24.868  1 27.43 ? 234 LYS Z CA    1 
ATOM   8510  C  C     . LYS F 1 234 ? 1.997   -34.233 25.304  1 27.46 ? 234 LYS Z C     1 
ATOM   8511  O  O     . LYS F 1 234 ? 2.709   -35.146 24.887  1 27.74 ? 234 LYS Z O     1 
ATOM   8512  C  CB    . LYS F 1 234 ? 3.165   -32.074 25.869  1 28.3  ? 234 LYS Z CB    1 
ATOM   8513  C  CG    . LYS F 1 234 ? 3.654   -30.754 25.339  1 30.63 ? 234 LYS Z CG    1 
ATOM   8514  C  CD    . LYS F 1 234 ? 4.553   -30.078 26.316  1 33.58 ? 234 LYS Z CD    1 
ATOM   8515  C  CE    . LYS F 1 234 ? 5.011   -28.775 25.755  1 36.65 ? 234 LYS Z CE    1 
ATOM   8516  N  NZ    . LYS F 1 234 ? 6.172   -28.255 26.513  1 38.74 ? 234 LYS Z NZ    1 
ATOM   8517  N  N     . ASN F 1 235 ? 0.942   -34.445 26.1    1 27.07 ? 235 ASN Z N     1 
ATOM   8518  C  CA    . ASN F 1 235 ? 0.51    -35.778 26.515  1 27.12 ? 235 ASN Z CA    1 
ATOM   8519  C  C     . ASN F 1 235 ? 0.043   -36.551 25.264  1 26.98 ? 235 ASN Z C     1 
ATOM   8520  O  O     . ASN F 1 235 ? 0.359   -37.725 25.129  1 27.11 ? 235 ASN Z O     1 
ATOM   8521  C  CB    . ASN F 1 235 ? -0.628  -35.664 27.545  1 27.93 ? 235 ASN Z CB    1 
ATOM   8522  C  CG    . ASN F 1 235 ? -0.916  -36.919 28.33   1 30.06 ? 235 ASN Z CG    1 
ATOM   8523  O  OD1   . ASN F 1 235 ? -0.639  -38.035 27.897  1 30.75 ? 235 ASN Z OD1   1 
ATOM   8524  N  ND2   . ASN F 1 235 ? -1.49   -36.762 29.512  1 30.78 ? 235 ASN Z ND2   1 
ATOM   8525  N  N     . LEU F 1 236 ? -0.665  -35.88  24.337  1 26.59 ? 236 LEU Z N     1 
ATOM   8526  C  CA    . LEU F 1 236 ? -1.141  -36.465 23.087  1 26.69 ? 236 LEU Z CA    1 
ATOM   8527  C  C     . LEU F 1 236 ? 0.028   -36.78  22.156  1 27.21 ? 236 LEU Z C     1 
ATOM   8528  O  O     . LEU F 1 236 ? 0.038   -37.834 21.52   1 27.57 ? 236 LEU Z O     1 
ATOM   8529  C  CB    . LEU F 1 236 ? -2.128  -35.524 22.395  1 26.52 ? 236 LEU Z CB    1 
ATOM   8530  C  CG    . LEU F 1 236 ? -2.888  -36.15  21.249  1 27.7  ? 236 LEU Z CG    1 
ATOM   8531  C  CD1   . LEU F 1 236 ? -3.815  -37.236 21.748  1 28.35 ? 236 LEU Z CD1   1 
ATOM   8532  C  CD2   . LEU F 1 236 ? -3.661  -35.12  20.492  1 28.14 ? 236 LEU Z CD2   1 
ATOM   8533  N  N     . LYS F 1 237 ? 1.036   -35.898 22.116  1 26.94 ? 237 LYS Z N     1 
ATOM   8534  C  CA    . LYS F 1 237 ? 2.249   -36.098 21.332  1 27.11 ? 237 LYS Z CA    1 
ATOM   8535  C  C     . LYS F 1 237 ? 3.024   -37.319 21.825  1 26.82 ? 237 LYS Z C     1 
ATOM   8536  O  O     . LYS F 1 237 ? 3.62    -38.018 21.006  1 27.19 ? 237 LYS Z O     1 
ATOM   8537  C  CB    . LYS F 1 237 ? 3.131   -34.851 21.368  1 29.31 ? 237 LYS Z CB    1 
ATOM   8538  C  CG    . LYS F 1 237 ? 2.792   -33.851 20.282  1 33.91 ? 237 LYS Z CG    1 
ATOM   8539  C  CD    . LYS F 1 237 ? 3.675   -32.622 20.357  1 37.9  ? 237 LYS Z CD    1 
ATOM   8540  C  CE    . LYS F 1 237 ? 3.585   -31.861 21.659  1 41.13 ? 237 LYS Z CE    1 
ATOM   8541  N  NZ    . LYS F 1 237 ? 3.945   -30.427 21.496  1 42.96 ? 237 LYS Z NZ    1 
ATOM   8542  N  N     . MET F 1 238 ? 2.988   -37.605 23.137  1 25.97 ? 238 MET Z N     1 
ATOM   8543  C  CA    . MET F 1 238 ? 3.631   -38.803 23.665  1 25.97 ? 238 MET Z CA    1 
ATOM   8544  C  C     . MET F 1 238 ? 2.873   -40.052 23.203  1 26.42 ? 238 MET Z C     1 
ATOM   8545  O  O     . MET F 1 238 ? 3.504   -41.052 22.865  1 26.67 ? 238 MET Z O     1 
ATOM   8546  C  CB    . MET F 1 238 ? 3.723   -38.774 25.192  1 26.19 ? 238 MET Z CB    1 
ATOM   8547  C  CG    . MET F 1 238 ? 4.339   -40.026 25.785  1 27.24 ? 238 MET Z CG    1 
ATOM   8548  S  SD    . MET F 1 238 ? 6.04    -40.275 25.239  1 28.58 ? 238 MET Z SD    1 
ATOM   8549  C  CE    . MET F 1 238 ? 6.863   -39.121 26.253  1 26.75 ? 238 MET Z CE    1 
ATOM   8550  N  N     . VAL F 1 239 ? 1.529   -39.992 23.152  1 26.45 ? 239 VAL Z N     1 
ATOM   8551  C  CA    . VAL F 1 239 ? 0.7     -41.096 22.656  1 27.19 ? 239 VAL Z CA    1 
ATOM   8552  C  C     . VAL F 1 239 ? 1.057   -41.376 21.188  1 28.23 ? 239 VAL Z C     1 
ATOM   8553  O  O     . VAL F 1 239 ? 1.201   -42.533 20.797  1 28.42 ? 239 VAL Z O     1 
ATOM   8554  C  CB    . VAL F 1 239 ? -0.805  -40.792 22.826  1 27.81 ? 239 VAL Z CB    1 
ATOM   8555  C  CG1   . VAL F 1 239 ? -1.659  -41.853 22.148  1 28.32 ? 239 VAL Z CG1   1 
ATOM   8556  C  CG2   . VAL F 1 239 ? -1.171  -40.678 24.297  1 28.39 ? 239 VAL Z CG2   1 
ATOM   8557  N  N     . GLU F 1 240 ? 1.274   -40.306 20.402  1 28.6  ? 240 GLU Z N     1 
ATOM   8558  C  CA    . GLU F 1 240 ? 1.692   -40.388 19.012  1 29.3  ? 240 GLU Z CA    1 
ATOM   8559  C  C     . GLU F 1 240 ? 3.052   -41.067 18.915  1 29.47 ? 240 GLU Z C     1 
ATOM   8560  O  O     . GLU F 1 240 ? 3.193   -42.016 18.155  1 29.59 ? 240 GLU Z O     1 
ATOM   8561  C  CB    . GLU F 1 240 ? 1.728   -38.985 18.376  1 32.09 ? 240 GLU Z CB    1 
ATOM   8562  C  CG    . GLU F 1 240 ? 1.749   -38.999 16.858  1 38.18 ? 240 GLU Z CG    1 
ATOM   8563  C  CD    . GLU F 1 240 ? 3.027   -38.496 16.212  1 46.4  ? 240 GLU Z CD    1 
ATOM   8564  O  OE1   . GLU F 1 240 ? 4.122   -38.892 16.671  1 47.93 ? 240 GLU Z OE1   1 
ATOM   8565  O  OE2   . GLU F 1 240 ? 2.934   -37.729 15.225  1 49.4  ? 240 GLU Z OE2   1 
ATOM   8566  N  N     . PHE F 1 241 ? 4.041   -40.613 19.701  1 29.45 ? 241 PHE Z N     1 
ATOM   8567  C  CA    . PHE F 1 241 ? 5.382   -41.195 19.694  1 30.11 ? 241 PHE Z CA    1 
ATOM   8568  C  C     . PHE F 1 241 ? 5.364   -42.687 19.985  1 30.85 ? 241 PHE Z C     1 
ATOM   8569  O  O     . PHE F 1 241 ? 6.007   -43.456 19.278  1 31.07 ? 241 PHE Z O     1 
ATOM   8570  C  CB    . PHE F 1 241 ? 6.31    -40.47  20.694  1 30    ? 241 PHE Z CB    1 
ATOM   8571  C  CG    . PHE F 1 241 ? 7.631   -41.171 20.912  1 30.58 ? 241 PHE Z CG    1 
ATOM   8572  C  CD1   . PHE F 1 241 ? 8.583   -41.217 19.909  1 31.42 ? 241 PHE Z CD1   1 
ATOM   8573  C  CD2   . PHE F 1 241 ? 7.891   -41.838 22.092  1 31.26 ? 241 PHE Z CD2   1 
ATOM   8574  C  CE1   . PHE F 1 241 ? 9.786   -41.88  20.101  1 32.1  ? 241 PHE Z CE1   1 
ATOM   8575  C  CE2   . PHE F 1 241 ? 9.088   -42.517 22.273  1 32.04 ? 241 PHE Z CE2   1 
ATOM   8576  C  CZ    . PHE F 1 241 ? 10.024  -42.54  21.274  1 31.86 ? 241 PHE Z CZ    1 
ATOM   8577  N  N     . LEU F 1 242 ? 4.657   -43.087 21.039  1 31.28 ? 242 LEU Z N     1 
ATOM   8578  C  CA    . LEU F 1 242 ? 4.604   -44.479 21.453  1 32.17 ? 242 LEU Z CA    1 
ATOM   8579  C  C     . LEU F 1 242 ? 3.824   -45.372 20.492  1 33.23 ? 242 LEU Z C     1 
ATOM   8580  O  O     . LEU F 1 242 ? 4.291   -46.465 20.175  1 33.35 ? 242 LEU Z O     1 
ATOM   8581  C  CB    . LEU F 1 242 ? 4.042   -44.58  22.874  1 32.19 ? 242 LEU Z CB    1 
ATOM   8582  C  CG    . LEU F 1 242 ? 4.84    -43.861 23.95   1 33.22 ? 242 LEU Z CG    1 
ATOM   8583  C  CD1   . LEU F 1 242 ? 4.086   -43.842 25.246  1 33.89 ? 242 LEU Z CD1   1 
ATOM   8584  C  CD2   . LEU F 1 242 ? 6.184   -44.498 24.147  1 33.65 ? 242 LEU Z CD2   1 
ATOM   8585  N  N     . SER F 1 243 ? 2.659   -44.912 20.013  1 33.82 ? 243 SER Z N     1 
ATOM   8586  C  CA    . SER F 1 243 ? 1.843   -45.719 19.11   1 34.88 ? 243 SER Z CA    1 
ATOM   8587  C  C     . SER F 1 243 ? 2.469   -45.885 17.734  1 35.82 ? 243 SER Z C     1 
ATOM   8588  O  O     . SER F 1 243 ? 2.359   -46.96  17.143  1 36.35 ? 243 SER Z O     1 
ATOM   8589  C  CB    . SER F 1 243 ? 0.421   -45.178 19.016  1 36.27 ? 243 SER Z CB    1 
ATOM   8590  O  OG    . SER F 1 243 ? 0.382   -43.845 18.534  1 38.34 ? 243 SER Z OG    1 
ATOM   8591  N  N     . LYS F 1 244 ? 3.169   -44.856 17.242  1 35.98 ? 244 LYS Z N     1 
ATOM   8592  C  CA    . LYS F 1 244 ? 3.855   -44.961 15.956  1 36.79 ? 244 LYS Z CA    1 
ATOM   8593  C  C     . LYS F 1 244 ? 5.123   -45.835 16.017  1 37.6  ? 244 LYS Z C     1 
ATOM   8594  O  O     . LYS F 1 244 ? 5.661   -46.196 14.976  1 37.93 ? 244 LYS Z O     1 
ATOM   8595  C  CB    . LYS F 1 244 ? 4.143   -43.579 15.363  1 38.81 ? 244 LYS Z CB    1 
ATOM   8596  C  CG    . LYS F 1 244 ? 2.878   -42.832 14.953  1 43.16 ? 244 LYS Z CG    1 
ATOM   8597  C  CD    . LYS F 1 244 ? 3.192   -41.455 14.388  1 48.18 ? 244 LYS Z CD    1 
ATOM   8598  C  CE    . LYS F 1 244 ? 3.313   -41.438 12.881  1 52.59 ? 244 LYS Z CE    1 
ATOM   8599  N  NZ    . LYS F 1 244 ? 3.988   -40.204 12.386  1 55.02 ? 244 LYS Z NZ    1 
ATOM   8600  N  N     . ASN F 1 245 ? 5.577   -46.21  17.223  1 37.95 ? 245 ASN Z N     1 
ATOM   8601  C  CA    . ASN F 1 245 ? 6.726   -47.095 17.404  1 38.7  ? 245 ASN Z CA    1 
ATOM   8602  C  C     . ASN F 1 245 ? 6.344   -48.57  17.645  1 39.18 ? 245 ASN Z C     1 
ATOM   8603  O  O     . ASN F 1 245 ? 7.232   -49.42  17.698  1 39.43 ? 245 ASN Z O     1 
ATOM   8604  C  CB    . ASN F 1 245 ? 7.619   -46.6   18.526  1 39.71 ? 245 ASN Z CB    1 
ATOM   8605  C  CG    . ASN F 1 245 ? 8.783   -45.803 18.023  1 42.98 ? 245 ASN Z CG    1 
ATOM   8606  O  OD1   . ASN F 1 245 ? 9.236   -45.96  16.882  1 44.43 ? 245 ASN Z OD1   1 
ATOM   8607  N  ND2   . ASN F 1 245 ? 9.3     -44.94  18.869  1 43.55 ? 245 ASN Z ND2   1 
ATOM   8608  N  N     . THR F 1 246 ? 5.047   -48.878 17.807  1 39.18 ? 246 THR Z N     1 
ATOM   8609  C  CA    . THR F 1 246 ? 4.614   -50.258 18.038  1 39.64 ? 246 THR Z CA    1 
ATOM   8610  C  C     . THR F 1 246 ? 4.032   -50.878 16.774  1 39.68 ? 246 THR Z C     1 
ATOM   8611  O  O     . THR F 1 246 ? 3.533   -50.153 15.907  1 39.9  ? 246 THR Z O     1 
ATOM   8612  C  CB    . THR F 1 246 ? 3.58    -50.32  19.164  1 41.12 ? 246 THR Z CB    1 
ATOM   8613  O  OG1   . THR F 1 246 ? 2.446   -49.527 18.804  1 42.1  ? 246 THR Z OG1   1 
ATOM   8614  C  CG2   . THR F 1 246 ? 4.141   -49.868 20.498  1 41.72 ? 246 THR Z CG2   1 
ATOM   8615  N  N     . LYS F 1 247 ? 4.059   -52.224 16.686  1 39.32 ? 247 LYS Z N     1 
ATOM   8616  C  CA    . LYS F 1 247 ? 3.5     -52.958 15.548  1 39.63 ? 247 LYS Z CA    1 
ATOM   8617  C  C     . LYS F 1 247 ? 1.992   -52.732 15.55   1 39.93 ? 247 LYS Z C     1 
ATOM   8618  O  O     . LYS F 1 247 ? 1.335   -53.032 16.542  1 40.05 ? 247 LYS Z O     1 
ATOM   8619  C  CB    . LYS F 1 247 ? 3.789   -54.462 15.647  1 41.13 ? 247 LYS Z CB    1 
ATOM   8620  C  CG    . LYS F 1 247 ? 5.18    -54.824 16.158  1 44.43 ? 247 LYS Z CG    1 
ATOM   8621  C  CD    . LYS F 1 247 ? 5.195   -55.957 17.214  1 48.07 ? 247 LYS Z CD    1 
ATOM   8622  C  CE    . LYS F 1 247 ? 3.873   -56.597 17.613  1 51.04 ? 247 LYS Z CE    1 
ATOM   8623  N  NZ    . LYS F 1 247 ? 3.217   -55.906 18.749  1 52.47 ? 247 LYS Z NZ    1 
ATOM   8624  N  N     . ASN F 1 248 ? 1.456   -52.173 14.463  1 39.95 ? 248 ASN Z N     1 
ATOM   8625  C  CA    . ASN F 1 248 ? 0.043   -51.826 14.342  1 40.42 ? 248 ASN Z CA    1 
ATOM   8626  C  C     . ASN F 1 248 ? -0.907  -53.032 14.365  1 40.89 ? 248 ASN Z C     1 
ATOM   8627  O  O     . ASN F 1 248 ? -2.073  -52.844 14.688  1 40.88 ? 248 ASN Z O     1 
ATOM   8628  C  CB    . ASN F 1 248 ? -0.192  -50.933 13.084  1 41.32 ? 248 ASN Z CB    1 
ATOM   8629  C  CG    . ASN F 1 248 ? -1.266  -51.372 12.08   1 43.77 ? 248 ASN Z CG    1 
ATOM   8630  O  OD1   . ASN F 1 248 ? -1.075  -52.291 11.269  1 44.39 ? 248 ASN Z OD1   1 
ATOM   8631  N  ND2   . ASN F 1 248 ? -2.43   -50.741 12.137  1 44.38 ? 248 ASN Z ND2   1 
ATOM   8632  N  N     . ASP F 1 249 ? -0.438  -54.239 14.012  1 41.16 ? 249 ASP Z N     1 
ATOM   8633  C  CA    . ASP F 1 249 ? -1.317  -55.408 13.96   1 41.87 ? 249 ASP Z CA    1 
ATOM   8634  C  C     . ASP F 1 249 ? -1.845  -55.864 15.321  1 41.79 ? 249 ASP Z C     1 
ATOM   8635  O  O     . ASP F 1 249 ? -2.893  -56.498 15.364  1 41.64 ? 249 ASP Z O     1 
ATOM   8636  C  CB    . ASP F 1 249 ? -0.66   -56.578 13.206  1 44.27 ? 249 ASP Z CB    1 
ATOM   8637  C  CG    . ASP F 1 249 ? 0.781   -56.857 13.59   1 49.32 ? 249 ASP Z CG    1 
ATOM   8638  O  OD1   . ASP F 1 249 ? 1.045   -57.072 14.797  1 50.18 ? 249 ASP Z OD1   1 
ATOM   8639  O  OD2   . ASP F 1 249 ? 1.643   -56.878 12.681  1 51.22 ? 249 ASP Z OD2   1 
ATOM   8640  N  N     . ASN F 1 250 ? -1.137  -55.553 16.421  1 41.89 ? 250 ASN Z N     1 
ATOM   8641  C  CA    . ASN F 1 250 ? -1.558  -55.941 17.777  1 42.45 ? 250 ASN Z CA    1 
ATOM   8642  C  C     . ASN F 1 250 ? -1.827  -54.752 18.715  1 42.31 ? 250 ASN Z C     1 
ATOM   8643  O  O     . ASN F 1 250 ? -2.17   -54.971 19.872  1 42.69 ? 250 ASN Z O     1 
ATOM   8644  C  CB    . ASN F 1 250 ? -0.504  -56.837 18.432  1 44.24 ? 250 ASN Z CB    1 
ATOM   8645  C  CG    . ASN F 1 250 ? -0.618  -58.304 18.111  1 48.65 ? 250 ASN Z CG    1 
ATOM   8646  O  OD1   . ASN F 1 250 ? -0.757  -59.144 19.007  1 50.25 ? 250 ASN Z OD1   1 
ATOM   8647  N  ND2   . ASN F 1 250 ? -0.543  -58.655 16.834  1 49.65 ? 250 ASN Z ND2   1 
ATOM   8648  N  N     . ASN F 1 251 ? -1.617  -53.512 18.255  1 41.6  ? 251 ASN Z N     1 
ATOM   8649  C  CA    . ASN F 1 251 ? -1.813  -52.318 19.082  1 41.41 ? 251 ASN Z CA    1 
ATOM   8650  C  C     . ASN F 1 251 ? -2.602  -51.251 18.312  1 41.44 ? 251 ASN Z C     1 
ATOM   8651  O  O     . ASN F 1 251 ? -2.63   -51.284 17.083  1 41.7  ? 251 ASN Z O     1 
ATOM   8652  C  CB    . ASN F 1 251 ? -0.453  -51.722 19.482  1 42    ? 251 ASN Z CB    1 
ATOM   8653  C  CG    . ASN F 1 251 ? 0.507   -52.675 20.143  1 44.4  ? 251 ASN Z CG    1 
ATOM   8654  O  OD1   . ASN F 1 251 ? 1.317   -53.344 19.493  1 45.47 ? 251 ASN Z OD1   1 
ATOM   8655  N  ND2   . ASN F 1 251 ? 0.455   -52.733 21.457  1 44.94 ? 251 ASN Z ND2   1 
ATOM   8656  N  N     . PHE F 1 252 ? -3.205  -50.282 19.024  1 41.06 ? 252 PHE Z N     1 
ATOM   8657  C  CA    . PHE F 1 252 ? -3.923  -49.187 18.376  1 41.11 ? 252 PHE Z CA    1 
ATOM   8658  C  C     . PHE F 1 252 ? -2.939  -48.322 17.594  1 41.06 ? 252 PHE Z C     1 
ATOM   8659  O  O     . PHE F 1 252 ? -1.83   -48.083 18.066  1 41.05 ? 252 PHE Z O     1 
ATOM   8660  C  CB    . PHE F 1 252 ? -4.631  -48.288 19.412  1 40.93 ? 252 PHE Z CB    1 
ATOM   8661  C  CG    . PHE F 1 252 ? -6.033  -48.665 19.84   1 41.31 ? 252 PHE Z CG    1 
ATOM   8662  C  CD1   . PHE F 1 252 ? -6.618  -49.841 19.406  1 41.98 ? 252 PHE Z CD1   1 
ATOM   8663  C  CD2   . PHE F 1 252 ? -6.757  -47.848 20.689  1 41.86 ? 252 PHE Z CD2   1 
ATOM   8664  C  CE1   . PHE F 1 252 ? -7.899  -50.189 19.815  1 42.57 ? 252 PHE Z CE1   1 
ATOM   8665  C  CE2   . PHE F 1 252 ? -8.035  -48.198 21.094  1 42.5  ? 252 PHE Z CE2   1 
ATOM   8666  C  CZ    . PHE F 1 252 ? -8.596  -49.368 20.66   1 42.29 ? 252 PHE Z CZ    1 
ATOM   8667  N  N     . THR F 1 253 ? -3.33   -47.86  16.403  1 40.97 ? 253 THR Z N     1 
ATOM   8668  C  CA    . THR F 1 253 ? -2.479  -46.952 15.63   1 41.53 ? 253 THR Z CA    1 
ATOM   8669  C  C     . THR F 1 253 ? -2.789  -45.525 16.096  1 41.65 ? 253 THR Z C     1 
ATOM   8670  O  O     . THR F 1 253 ? -3.819  -45.312 16.748  1 42.02 ? 253 THR Z O     1 
ATOM   8671  C  CB    . THR F 1 253 ? -2.725  -47.105 14.12   1 43.26 ? 253 THR Z CB    1 
ATOM   8672  O  OG1   . THR F 1 253 ? -2.834  -48.492 13.782  1 44.32 ? 253 THR Z OG1   1 
ATOM   8673  C  CG2   . THR F 1 253 ? -1.618  -46.46  13.272  1 43.86 ? 253 THR Z CG2   1 
ATOM   8674  N  N     . TYR F 1 254 ? -1.932  -44.538 15.763  1 41.3  ? 254 TYR Z N     1 
ATOM   8675  C  CA    . TYR F 1 254 ? -2.207  -43.159 16.158  1 41.48 ? 254 TYR Z CA    1 
ATOM   8676  C  C     . TYR F 1 254 ? -3.518  -42.65  15.558  1 41.73 ? 254 TYR Z C     1 
ATOM   8677  O  O     . TYR F 1 254 ? -4.236  -41.932 16.237  1 41.92 ? 254 TYR Z O     1 
ATOM   8678  C  CB    . TYR F 1 254 ? -1.048  -42.198 15.873  1 41.4  ? 254 TYR Z CB    1 
ATOM   8679  C  CG    . TYR F 1 254 ? -1.366  -40.826 16.412  1 42.11 ? 254 TYR Z CG    1 
ATOM   8680  C  CD1   . TYR F 1 254 ? -1.597  -40.63  17.767  1 43.16 ? 254 TYR Z CD1   1 
ATOM   8681  C  CD2   . TYR F 1 254 ? -1.608  -39.765 15.557  1 42.99 ? 254 TYR Z CD2   1 
ATOM   8682  C  CE1   . TYR F 1 254 ? -1.964  -39.388 18.266  1 44.07 ? 254 TYR Z CE1   1 
ATOM   8683  C  CE2   . TYR F 1 254 ? -1.978  -38.517 16.042  1 44.01 ? 254 TYR Z CE2   1 
ATOM   8684  C  CZ    . TYR F 1 254 ? -2.161  -38.334 17.398  1 45.01 ? 254 TYR Z CZ    1 
ATOM   8685  O  OH    . TYR F 1 254 ? -2.526  -37.106 17.887  1 46.61 ? 254 TYR Z OH    1 
ATOM   8686  N  N     . SER F 1 255 ? -3.875  -43.084 14.336  1 41.64 ? 255 SER Z N     1 
ATOM   8687  C  CA    . SER F 1 255 ? -5.138  -42.674 13.715  1 42.05 ? 255 SER Z CA    1 
ATOM   8688  C  C     . SER F 1 255 ? -6.342  -43.098 14.566  1 42.27 ? 255 SER Z C     1 
ATOM   8689  O  O     . SER F 1 255 ? -7.314  -42.352 14.663  1 42.53 ? 255 SER Z O     1 
ATOM   8690  C  CB    . SER F 1 255 ? -5.262  -43.239 12.304  1 43.34 ? 255 SER Z CB    1 
ATOM   8691  O  OG    . SER F 1 255 ? -4.239  -42.759 11.448  1 45.7  ? 255 SER Z OG    1 
ATOM   8692  N  N     . GLU F 1 256 ? -6.258  -44.269 15.214  1 42.09 ? 256 GLU Z N     1 
ATOM   8693  C  CA    . GLU F 1 256 ? -7.316  -44.761 16.096  1 42.42 ? 256 GLU Z CA    1 
ATOM   8694  C  C     . GLU F 1 256 ? -7.399  -43.932 17.377  1 42.43 ? 256 GLU Z C     1 
ATOM   8695  O  O     . GLU F 1 256 ? -8.495  -43.551 17.777  1 42.53 ? 256 GLU Z O     1 
ATOM   8696  C  CB    . GLU F 1 256 ? -7.114  -46.245 16.409  1 44.57 ? 256 GLU Z CB    1 
ATOM   8697  C  CG    . GLU F 1 256 ? -7.466  -47.119 15.223  1 49.22 ? 256 GLU Z CG    1 
ATOM   8698  C  CD    . GLU F 1 256 ? -6.979  -48.547 15.313  1 55.25 ? 256 GLU Z CD    1 
ATOM   8699  O  OE1   . GLU F 1 256 ? -7.504  -49.403 14.566  1 56.31 ? 256 GLU Z OE1   1 
ATOM   8700  O  OE2   . GLU F 1 256 ? -6.07   -48.814 16.127  1 57.44 ? 256 GLU Z OE2   1 
ATOM   8701  N  N     . TRP F 1 257 ? -6.249  -43.608 17.991  1 42.18 ? 257 TRP Z N     1 
ATOM   8702  C  CA    . TRP F 1 257 ? -6.222  -42.771 19.19   1 42.4  ? 257 TRP Z CA    1 
ATOM   8703  C  C     . TRP F 1 257 ? -6.719  -41.363 18.892  1 42.16 ? 257 TRP Z C     1 
ATOM   8704  O  O     . TRP F 1 257 ? -7.42   -40.774 19.712  1 42.35 ? 257 TRP Z O     1 
ATOM   8705  C  CB    . TRP F 1 257 ? -4.808  -42.678 19.776  1 42.56 ? 257 TRP Z CB    1 
ATOM   8706  C  CG    . TRP F 1 257 ? -4.302  -43.921 20.446  1 43.21 ? 257 TRP Z CG    1 
ATOM   8707  C  CD1   . TRP F 1 257 ? -3.168  -44.609 20.134  1 44.06 ? 257 TRP Z CD1   1 
ATOM   8708  C  CD2   . TRP F 1 257 ? -4.861  -44.569 21.598  1 43.44 ? 257 TRP Z CD2   1 
ATOM   8709  N  NE1   . TRP F 1 257 ? -3.002  -45.662 21      1 44.37 ? 257 TRP Z NE1   1 
ATOM   8710  C  CE2   . TRP F 1 257 ? -4.032  -45.664 21.905  1 44.15 ? 257 TRP Z CE2   1 
ATOM   8711  C  CE3   . TRP F 1 257 ? -6      -44.349 22.382  1 44.08 ? 257 TRP Z CE3   1 
ATOM   8712  C  CZ2   . TRP F 1 257 ? -4.294  -46.52  22.974  1 44.79 ? 257 TRP Z CZ2   1 
ATOM   8713  C  CZ3   . TRP F 1 257 ? -6.276  -45.221 23.417  1 44.87 ? 257 TRP Z CZ3   1 
ATOM   8714  C  CH2   . TRP F 1 257 ? -5.419  -46.278 23.717  1 44.89 ? 257 TRP Z CH2   1 
ATOM   8715  N  N     . GLU F 1 258 ? -6.357  -40.827 17.722  1 41.66 ? 258 GLU Z N     1 
ATOM   8716  C  CA    . GLU F 1 258 ? -6.748  -39.496 17.269  1 41.76 ? 258 GLU Z CA    1 
ATOM   8717  C  C     . GLU F 1 258 ? -8.247  -39.431 17.055  1 41.78 ? 258 GLU Z C     1 
ATOM   8718  O  O     . GLU F 1 258 ? -8.862  -38.449 17.447  1 41.87 ? 258 GLU Z O     1 
ATOM   8719  C  CB    . GLU F 1 258 ? -6.016  -39.14  15.974  1 43.67 ? 258 GLU Z CB    1 
ATOM   8720  C  CG    . GLU F 1 258 ? -6.227  -37.714 15.516  1 47.83 ? 258 GLU Z CG    1 
ATOM   8721  C  CD    . GLU F 1 258 ? -5.52   -37.411 14.212  1 53.66 ? 258 GLU Z CD    1 
ATOM   8722  O  OE1   . GLU F 1 258 ? -5.659  -38.213 13.26   1 54.71 ? 258 GLU Z OE1   1 
ATOM   8723  O  OE2   . GLU F 1 258 ? -4.817  -36.377 14.144  1 55.59 ? 258 GLU Z OE2   1 
ATOM   8724  N  N     . SER F 1 259 ? -8.85   -40.496 16.493  1 41.61 ? 259 SER Z N     1 
ATOM   8725  C  CA    . SER F 1 259 ? -10.297 -40.551 16.275  1 42    ? 259 SER Z CA    1 
ATOM   8726  C  C     . SER F 1 259 ? -11.091 -40.603 17.592  1 42.31 ? 259 SER Z C     1 
ATOM   8727  O  O     . SER F 1 259 ? -12.224 -40.132 17.64   1 42.52 ? 259 SER Z O     1 
ATOM   8728  C  CB    . SER F 1 259 ? -10.677 -41.712 15.36   1 43.13 ? 259 SER Z CB    1 
ATOM   8729  O  OG    . SER F 1 259 ? -10.55  -42.981 15.981  1 45.13 ? 259 SER Z OG    1 
ATOM   8730  N  N     . ILE F 1 260 ? -10.492 -41.152 18.66   1 42.12 ? 260 ILE Z N     1 
ATOM   8731  C  CA    . ILE F 1 260 ? -11.107 -41.191 19.984  1 42.24 ? 260 ILE Z CA    1 
ATOM   8732  C  C     . ILE F 1 260 ? -10.935 -39.803 20.617  1 42.44 ? 260 ILE Z C     1 
ATOM   8733  O  O     . ILE F 1 260 ? -11.892 -39.256 21.161  1 42.83 ? 260 ILE Z O     1 
ATOM   8734  C  CB    . ILE F 1 260 ? -10.474 -42.305 20.86   1 42.67 ? 260 ILE Z CB    1 
ATOM   8735  C  CG1   . ILE F 1 260 ? -10.689 -43.699 20.253  1 43.25 ? 260 ILE Z CG1   1 
ATOM   8736  C  CG2   . ILE F 1 260 ? -11.011 -42.261 22.283  1 43.32 ? 260 ILE Z CG2   1 
ATOM   8737  C  CD1   . ILE F 1 260 ? -9.813  -44.745 20.859  1 44.29 ? 260 ILE Z CD1   1 
ATOM   8738  N  N     . TYR F 1 261 ? -9.722  -39.222 20.513  1 42.15 ? 261 TYR Z N     1 
ATOM   8739  C  CA    . TYR F 1 261 ? -9.391  -37.896 21.038  1 42.53 ? 261 TYR Z CA    1 
ATOM   8740  C  C     . TYR F 1 261 ? -10.291 -36.794 20.493  1 42.99 ? 261 TYR Z C     1 
ATOM   8741  O  O     . TYR F 1 261 ? -10.827 -36.008 21.274  1 43.07 ? 261 TYR Z O     1 
ATOM   8742  C  CB    . TYR F 1 261 ? -7.903  -37.559 20.794  1 42.46 ? 261 TYR Z CB    1 
ATOM   8743  C  CG    . TYR F 1 261 ? -7.51   -36.163 21.238  1 43.06 ? 261 TYR Z CG    1 
ATOM   8744  C  CD1   . TYR F 1 261 ? -7.239  -35.884 22.569  1 43.69 ? 261 TYR Z CD1   1 
ATOM   8745  C  CD2   . TYR F 1 261 ? -7.396  -35.125 20.322  1 43.82 ? 261 TYR Z CD2   1 
ATOM   8746  C  CE1   . TYR F 1 261 ? -6.901  -34.601 22.987  1 44.46 ? 261 TYR Z CE1   1 
ATOM   8747  C  CE2   . TYR F 1 261 ? -7.068  -33.833 20.73   1 44.59 ? 261 TYR Z CE2   1 
ATOM   8748  C  CZ    . TYR F 1 261 ? -6.808  -33.577 22.064  1 45.27 ? 261 TYR Z CZ    1 
ATOM   8749  O  OH    . TYR F 1 261 ? -6.447  -32.312 22.476  1 46.45 ? 261 TYR Z OH    1 
ATOM   8750  N  N     . ASN F 1 262 ? -10.451 -36.72  19.163  1 43.15 ? 262 ASN Z N     1 
ATOM   8751  C  CA    . ASN F 1 262 ? -11.281 -35.674 18.568  1 43.89 ? 262 ASN Z CA    1 
ATOM   8752  C  C     . ASN F 1 262 ? -12.802 -35.945 18.656  1 44.37 ? 262 ASN Z C     1 
ATOM   8753  O  O     . ASN F 1 262 ? -13.583 -35.202 18.064  1 44.8  ? 262 ASN Z O     1 
ATOM   8754  C  CB    . ASN F 1 262 ? -10.853 -35.351 17.132  1 45.1  ? 262 ASN Z CB    1 
ATOM   8755  C  CG    . ASN F 1 262 ? -10.975 -36.488 16.152  1 48.57 ? 262 ASN Z CG    1 
ATOM   8756  O  OD1   . ASN F 1 262 ? -11.761 -37.429 16.327  1 49.95 ? 262 ASN Z OD1   1 
ATOM   8757  N  ND2   . ASN F 1 262 ? -10.19  -36.426 15.09   1 49.2  ? 262 ASN Z ND2   1 
ATOM   8758  N  N     . GLY F 1 263 ? -13.204 -36.98  19.387  1 44.11 ? 263 GLY Z N     1 
ATOM   8759  C  CA    . GLY F 1 263 ? -14.607 -37.294 19.605  1 44.49 ? 263 GLY Z CA    1 
ATOM   8760  C  C     . GLY F 1 263 ? -15.348 -37.951 18.464  1 44.84 ? 263 GLY Z C     1 
ATOM   8761  O  O     . GLY F 1 263 ? -16.58  -37.966 18.478  1 44.87 ? 263 GLY Z O     1 
ATOM   8762  N  N     . THR F 1 264 ? -14.63  -38.509 17.475  1 45.08 ? 264 THR Z N     1 
ATOM   8763  C  CA    . THR F 1 264 ? -15.293 -39.201 16.363  1 45.89 ? 264 THR Z CA    1 
ATOM   8764  C  C     . THR F 1 264 ? -15.912 -40.517 16.864  1 46.62 ? 264 THR Z C     1 
ATOM   8765  O  O     . THR F 1 264 ? -17.053 -40.833 16.533  1 46.81 ? 264 THR Z O     1 
ATOM   8766  C  CB    . THR F 1 264 ? -14.325 -39.449 15.203  1 47.14 ? 264 THR Z CB    1 
ATOM   8767  O  OG1   . THR F 1 264 ? -13.679 -38.231 14.85   1 48.24 ? 264 THR Z OG1   1 
ATOM   8768  C  CG2   . THR F 1 264 ? -15.022 -40.015 13.984  1 47.56 ? 264 THR Z CG2   1 
ATOM   8769  N  N     . TYR F 1 265 ? -15.168 -41.266 17.687  1 46.79 ? 265 TYR Z N     1 
ATOM   8770  C  CA    . TYR F 1 265 ? -15.647 -42.529 18.248  1 47.42 ? 265 TYR Z CA    1 
ATOM   8771  C  C     . TYR F 1 265 ? -15.294 -42.648 19.733  1 47.93 ? 265 TYR Z C     1 
ATOM   8772  O  O     . TYR F 1 265 ? -14.356 -42.005 20.203  1 47.94 ? 265 TYR Z O     1 
ATOM   8773  C  CB    . TYR F 1 265 ? -14.986 -43.728 17.528  1 47.41 ? 265 TYR Z CB    1 
ATOM   8774  C  CG    . TYR F 1 265 ? -15.049 -43.699 16.019  1 48.01 ? 265 TYR Z CG    1 
ATOM   8775  C  CD1   . TYR F 1 265 ? -16.234 -43.961 15.349  1 48.86 ? 265 TYR Z CD1   1 
ATOM   8776  C  CD2   . TYR F 1 265 ? -13.907 -43.492 15.261  1 48.79 ? 265 TYR Z CD2   1 
ATOM   8777  C  CE1   . TYR F 1 265 ? -16.293 -43.958 13.962  1 49.74 ? 265 TYR Z CE1   1 
ATOM   8778  C  CE2   . TYR F 1 265 ? -13.952 -43.491 13.875  1 49.7  ? 265 TYR Z CE2   1 
ATOM   8779  C  CZ    . TYR F 1 265 ? -15.15  -43.715 13.227  1 50.68 ? 265 TYR Z CZ    1 
ATOM   8780  O  OH    . TYR F 1 265 ? -15.195 -43.715 11.854  1 52.34 ? 265 TYR Z OH    1 
ATOM   8781  N  N     . ARG F 1 266 ? -16.014 -43.513 20.46   1 48.27 ? 266 ARG Z N     1 
ATOM   8782  C  CA    . ARG F 1 266 ? -15.655 -43.86  21.833  1 49.18 ? 266 ARG Z CA    1 
ATOM   8783  C  C     . ARG F 1 266 ? -14.721 -45.101 21.731  1 49.21 ? 266 ARG Z C     1 
ATOM   8784  O  O     . ARG F 1 266 ? -14.723 -45.791 20.701  1 49.47 ? 266 ARG Z O     1 
ATOM   8785  C  CB    . ARG F 1 266 ? -16.897 -44.117 22.718  1 51.34 ? 266 ARG Z CB    1 
ATOM   8786  C  CG    . ARG F 1 266 ? -17.569 -45.467 22.506  1 55.86 ? 266 ARG Z CG    1 
ATOM   8787  C  CD    . ARG F 1 266 ? -18.889 -45.617 23.246  1 60.21 ? 266 ARG Z CD    1 
ATOM   8788  N  NE    . ARG F 1 266 ? -19.348 -47.01  23.241  1 63.82 ? 266 ARG Z NE    1 
ATOM   8789  C  CZ    . ARG F 1 266 ? -20.345 -47.474 22.491  1 66.29 ? 266 ARG Z CZ    1 
ATOM   8790  N  NH1   . ARG F 1 266 ? -21.017 -46.658 21.687  1 65.9  ? 266 ARG Z NH1   1 
ATOM   8791  N  NH2   . ARG F 1 266 ? -20.683 -48.757 22.545  1 66.34 ? 266 ARG Z NH2   1 
ATOM   8792  N  N     . ILE F 1 267 ? -13.911 -45.374 22.765  1 48.66 ? 267 ILE Z N     1 
ATOM   8793  C  CA    . ILE F 1 267 ? -12.948 -46.476 22.706  1 48.65 ? 267 ILE Z CA    1 
ATOM   8794  C  C     . ILE F 1 267 ? -13.602 -47.857 22.514  1 48.67 ? 267 ILE Z C     1 
ATOM   8795  O  O     . ILE F 1 267 ? -12.955 -48.764 21.991  1 48.8  ? 267 ILE Z O     1 
ATOM   8796  C  CB    . ILE F 1 267 ? -11.995 -46.443 23.914  1 49.12 ? 267 ILE Z CB    1 
ATOM   8797  C  CG1   . ILE F 1 267 ? -10.686 -47.193 23.623  1 50.11 ? 267 ILE Z CG1   1 
ATOM   8798  C  CG2   . ILE F 1 267 ? -12.678 -46.939 25.173  1 49.61 ? 267 ILE Z CG2   1 
ATOM   8799  C  CD1   . ILE F 1 267 ? -9.603  -46.917 24.601  1 51.5  ? 267 ILE Z CD1   1 
ATOM   8800  N  N     . THR F 1 268 ? -14.886 -48.006 22.868  1 48.44 ? 268 THR Z N     1 
ATOM   8801  C  CA    . THR F 1 268 ? -15.579 -49.288 22.708  1 48.63 ? 268 THR Z CA    1 
ATOM   8802  C  C     . THR F 1 268 ? -16.385 -49.4   21.398  1 48.41 ? 268 THR Z C     1 
ATOM   8803  O  O     . THR F 1 268 ? -16.845 -50.493 21.068  1 48.46 ? 268 THR Z O     1 
ATOM   8804  C  CB    . THR F 1 268 ? -16.442 -49.601 23.935  1 50.01 ? 268 THR Z CB    1 
ATOM   8805  O  OG1   . THR F 1 268 ? -17.268 -48.472 24.234  1 51.3  ? 268 THR Z OG1   1 
ATOM   8806  C  CG2   . THR F 1 268 ? -15.607 -49.972 25.151  1 50.2  ? 268 THR Z CG2   1 
ATOM   8807  N  N     . ASN F 1 269 ? -16.56  -48.293 20.655  1 48.05 ? 269 ASN Z N     1 
ATOM   8808  C  CA    . ASN F 1 269 ? -17.289 -48.343 19.386  1 48.18 ? 269 ASN Z CA    1 
ATOM   8809  C  C     . ASN F 1 269 ? -16.402 -48.004 18.178  1 47.46 ? 269 ASN Z C     1 
ATOM   8810  O  O     . ASN F 1 269 ? -16.909 -47.562 17.147  1 47.55 ? 269 ASN Z O     1 
ATOM   8811  C  CB    . ASN F 1 269 ? -18.58  -47.501 19.412  1 49.89 ? 269 ASN Z CB    1 
ATOM   8812  C  CG    . ASN F 1 269 ? -18.46  -45.995 19.218  1 53.77 ? 269 ASN Z CG    1 
ATOM   8813  O  OD1   . ASN F 1 269 ? -17.415 -45.448 18.841  1 55    ? 269 ASN Z OD1   1 
ATOM   8814  N  ND2   . ASN F 1 269 ? -19.55  -45.28  19.47   1 54.58 ? 269 ASN Z ND2   1 
ATOM   8815  N  N     . LEU F 1 270 ? -15.079 -48.225 18.301  1 46.57 ? 270 LEU Z N     1 
ATOM   8816  C  CA    . LEU F 1 270 ? -14.109 -47.991 17.23   1 46.07 ? 270 LEU Z CA    1 
ATOM   8817  C  C     . LEU F 1 270 ? -14.451 -48.952 16.088  1 45.55 ? 270 LEU Z C     1 
ATOM   8818  O  O     . LEU F 1 270 ? -14.675 -50.139 16.338  1 45.6  ? 270 LEU Z O     1 
ATOM   8819  C  CB    . LEU F 1 270 ? -12.696 -48.29  17.763  1 46.06 ? 270 LEU Z CB    1 
ATOM   8820  C  CG    . LEU F 1 270 ? -11.55  -47.448 17.22   1 47.14 ? 270 LEU Z CG    1 
ATOM   8821  C  CD1   . LEU F 1 270 ? -11.769 -45.979 17.504  1 47.82 ? 270 LEU Z CD1   1 
ATOM   8822  C  CD2   . LEU F 1 270 ? -10.235 -47.882 17.821  1 47.58 ? 270 LEU Z CD2   1 
ATOM   8823  N  N     . PRO F 1 271 ? -14.598 -48.45  14.85   1 44.73 ? 271 PRO Z N     1 
ATOM   8824  C  CA    . PRO F 1 271 ? -14.981 -49.342 13.743  1 44.24 ? 271 PRO Z CA    1 
ATOM   8825  C  C     . PRO F 1 271 ? -14.007 -50.49  13.503  1 43.72 ? 271 PRO Z C     1 
ATOM   8826  O  O     . PRO F 1 271 ? -14.41  -51.555 13.057  1 43.84 ? 271 PRO Z O     1 
ATOM   8827  C  CB    . PRO F 1 271 ? -15.067 -48.403 12.538  1 45.01 ? 271 PRO Z CB    1 
ATOM   8828  C  CG    . PRO F 1 271 ? -14.26  -47.212 12.913  1 45.55 ? 271 PRO Z CG    1 
ATOM   8829  C  CD    . PRO F 1 271 ? -14.409 -47.063 14.394  1 44.09 ? 271 PRO Z CD    1 
ATOM   8830  N  N     . SER F 1 272 ? -12.739 -50.284 13.835  1 43.13 ? 272 SER Z N     1 
ATOM   8831  C  CA    . SER F 1 272 ? -11.699 -51.286 13.665  1 43.22 ? 272 SER Z CA    1 
ATOM   8832  C  C     . SER F 1 272 ? -11.549 -52.248 14.842  1 43.32 ? 272 SER Z C     1 
ATOM   8833  O  O     . SER F 1 272 ? -10.679 -53.114 14.782  1 43.56 ? 272 SER Z O     1 
ATOM   8834  C  CB    . SER F 1 272 ? -10.366 -50.601 13.418  1 44.37 ? 272 SER Z CB    1 
ATOM   8835  O  OG    . SER F 1 272 ? -10.112 -49.663 14.45   1 46.63 ? 272 SER Z OG    1 
ATOM   8836  N  N     . LEU F 1 273 ? -12.363 -52.109 15.91   1 42.88 ? 273 LEU Z N     1 
ATOM   8837  C  CA    . LEU F 1 273 ? -12.275 -52.987 17.083  1 42.69 ? 273 LEU Z CA    1 
ATOM   8838  C  C     . LEU F 1 273 ? -12.51  -54.436 16.681  1 42.06 ? 273 LEU Z C     1 
ATOM   8839  O  O     . LEU F 1 273 ? -13.486 -54.742 15.996  1 42.32 ? 273 LEU Z O     1 
ATOM   8840  C  CB    . LEU F 1 273 ? -13.272 -52.559 18.166  1 43.04 ? 273 LEU Z CB    1 
ATOM   8841  C  CG    . LEU F 1 273 ? -12.782 -52.696 19.601  1 44.83 ? 273 LEU Z CG    1 
ATOM   8842  C  CD1   . LEU F 1 273 ? -11.594 -51.795 19.858  1 45.45 ? 273 LEU Z CD1   1 
ATOM   8843  C  CD2   . LEU F 1 273 ? -13.888 -52.358 20.584  1 45.63 ? 273 LEU Z CD2   1 
ATOM   8844  N  N     . GLY F 1 274 ? -11.565 -55.294 17.028  1 41.02 ? 274 GLY Z N     1 
ATOM   8845  C  CA    . GLY F 1 274 ? -11.643 -56.696 16.656  1 40.38 ? 274 GLY Z CA    1 
ATOM   8846  C  C     . GLY F 1 274 ? -10.529 -57.146 15.735  1 39.36 ? 274 GLY Z C     1 
ATOM   8847  O  O     . GLY F 1 274 ? -10.293 -58.348 15.622  1 39.44 ? 274 GLY Z O     1 
ATOM   8848  N  N     . ARG F 1 275 ? -9.823  -56.202 15.074  1 38.26 ? 275 ARG Z N     1 
ATOM   8849  C  CA    . ARG F 1 275 ? -8.702  -56.579 14.203  1 37.74 ? 275 ARG Z CA    1 
ATOM   8850  C  C     . ARG F 1 275 ? -7.605  -57.338 14.969  1 37.4  ? 275 ARG Z C     1 
ATOM   8851  O  O     . ARG F 1 275 ? -6.888  -58.15  14.386  1 37.67 ? 275 ARG Z O     1 
ATOM   8852  C  CB    . ARG F 1 275 ? -8.152  -55.391 13.414  1 38.4  ? 275 ARG Z CB    1 
ATOM   8853  C  CG    . ARG F 1 275 ? -7.692  -54.251 14.28   1 40.17 ? 275 ARG Z CG    1 
ATOM   8854  C  CD    . ARG F 1 275 ? -7.336  -53.058 13.426  1 41.59 ? 275 ARG Z CD    1 
ATOM   8855  N  NE    . ARG F 1 275 ? -6.55   -52.072 14.168  1 42.81 ? 275 ARG Z NE    1 
ATOM   8856  C  CZ    . ARG F 1 275 ? -5.237  -52.152 14.361  1 44.02 ? 275 ARG Z CZ    1 
ATOM   8857  N  NH1   . ARG F 1 275 ? -4.551  -53.188 13.894  1 43.65 ? 275 ARG Z NH1   1 
ATOM   8858  N  NH2   . ARG F 1 275 ? -4.603  -51.207 15.038  1 43.51 ? 275 ARG Z NH2   1 
ATOM   8859  N  N     . PHE F 1 276 ? -7.509  -57.109 16.28   1 36.68 ? 276 PHE Z N     1 
ATOM   8860  C  CA    . PHE F 1 276 ? -6.665  -57.884 17.171  1 36.54 ? 276 PHE Z CA    1 
ATOM   8861  C  C     . PHE F 1 276 ? -7.506  -58.311 18.391  1 36.52 ? 276 PHE Z C     1 
ATOM   8862  O  O     . PHE F 1 276 ? -8.492  -57.654 18.725  1 36.6  ? 276 PHE Z O     1 
ATOM   8863  C  CB    . PHE F 1 276 ? -5.355  -57.177 17.548  1 36.13 ? 276 PHE Z CB    1 
ATOM   8864  C  CG    . PHE F 1 276 ? -5.505  -55.851 18.236  1 36.47 ? 276 PHE Z CG    1 
ATOM   8865  C  CD1   . PHE F 1 276 ? -5.624  -55.776 19.61   1 37.13 ? 276 PHE Z CD1   1 
ATOM   8866  C  CD2   . PHE F 1 276 ? -5.474  -54.675 17.515  1 37.27 ? 276 PHE Z CD2   1 
ATOM   8867  C  CE1   . PHE F 1 276 ? -5.751  -54.556 20.243  1 37.8  ? 276 PHE Z CE1   1 
ATOM   8868  C  CE2   . PHE F 1 276 ? -5.588  -53.451 18.152  1 38    ? 276 PHE Z CE2   1 
ATOM   8869  C  CZ    . PHE F 1 276 ? -5.729  -53.4   19.512  1 37.8  ? 276 PHE Z CZ    1 
ATOM   8870  N  N     . LYS F 1 277 ? -7.166  -59.443 19.005  1 36.18 ? 277 LYS Z N     1 
ATOM   8871  C  CA    . LYS F 1 277 ? -7.915  -59.977 20.139  1 36.26 ? 277 LYS Z CA    1 
ATOM   8872  C  C     . LYS F 1 277 ? -7.223  -59.713 21.472  1 35.87 ? 277 LYS Z C     1 
ATOM   8873  O  O     . LYS F 1 277 ? -6.05   -59.363 21.498  1 35.78 ? 277 LYS Z O     1 
ATOM   8874  C  CB    . LYS F 1 277 ? -8.112  -61.499 19.963  1 38.25 ? 277 LYS Z CB    1 
ATOM   8875  C  CG    . LYS F 1 277 ? -9.202  -61.889 18.975  1 42.41 ? 277 LYS Z CG    1 
ATOM   8876  C  CD    . LYS F 1 277 ? -9.518  -63.368 19.08   1 46.68 ? 277 LYS Z CD    1 
ATOM   8877  C  CE    . LYS F 1 277 ? -10.806 -63.751 18.388  1 50.4  ? 277 LYS Z CE    1 
ATOM   8878  N  NZ    . LYS F 1 277 ? -12.004 -63.525 19.237  1 52.8  ? 277 LYS Z NZ    1 
ATOM   8879  N  N     . PHE F 1 278 ? -7.951  -59.885 22.582  1 35.43 ? 278 PHE Z N     1 
ATOM   8880  C  CA    . PHE F 1 278 ? -7.366  -59.734 23.902  1 35.36 ? 278 PHE Z CA    1 
ATOM   8881  C  C     . PHE F 1 278 ? -6.769  -61.089 24.256  1 34.48 ? 278 PHE Z C     1 
ATOM   8882  O  O     . PHE F 1 278 ? -7.49   -62.08  24.355  1 34.33 ? 278 PHE Z O     1 
ATOM   8883  C  CB    . PHE F 1 278 ? -8.423  -59.27  24.924  1 35.78 ? 278 PHE Z CB    1 
ATOM   8884  C  CG    . PHE F 1 278 ? -8.107  -59.514 26.387  1 37.11 ? 278 PHE Z CG    1 
ATOM   8885  C  CD1   . PHE F 1 278 ? -6.865  -59.206 26.907  1 38.14 ? 278 PHE Z CD1   1 
ATOM   8886  C  CD2   . PHE F 1 278 ? -9.072  -60.001 27.249  1 38.14 ? 278 PHE Z CD2   1 
ATOM   8887  C  CE1   . PHE F 1 278 ? -6.572  -59.464 28.238  1 38.94 ? 278 PHE Z CE1   1 
ATOM   8888  C  CE2   . PHE F 1 278 ? -8.786  -60.214 28.591  1 38.98 ? 278 PHE Z CE2   1 
ATOM   8889  C  CZ    . PHE F 1 278 ? -7.539  -59.943 29.076  1 38.85 ? 278 PHE Z CZ    1 
ATOM   8890  N  N     . ARG F 1 279 ? -5.44   -61.141 24.381  1 33.77 ? 279 ARG Z N     1 
ATOM   8891  C  CA    . ARG F 1 279 ? -4.717  -62.361 24.712  1 33.7  ? 279 ARG Z CA    1 
ATOM   8892  C  C     . ARG F 1 279 ? -3.813  -62.118 25.919  1 33.27 ? 279 ARG Z C     1 
ATOM   8893  O  O     . ARG F 1 279 ? -2.652  -61.747 25.766  1 33.24 ? 279 ARG Z O     1 
ATOM   8894  C  CB    . ARG F 1 279 ? -3.903  -62.859 23.505  1 35.19 ? 279 ARG Z CB    1 
ATOM   8895  C  CG    . ARG F 1 279 ? -4.738  -63.009 22.228  1 38    ? 279 ARG Z CG    1 
ATOM   8896  C  CD    . ARG F 1 279 ? -4      -63.696 21.09   1 39.95 ? 279 ARG Z CD    1 
ATOM   8897  N  NE    . ARG F 1 279 ? -4.825  -63.778 19.882  1 41.14 ? 279 ARG Z NE    1 
ATOM   8898  C  CZ    . ARG F 1 279 ? -5.649  -64.782 19.603  1 42.49 ? 279 ARG Z CZ    1 
ATOM   8899  N  NH1   . ARG F 1 279 ? -5.767  -65.805 20.439  1 42.57 ? 279 ARG Z NH1   1 
ATOM   8900  N  NH2   . ARG F 1 279 ? -6.356  -64.774 18.483  1 41.89 ? 279 ARG Z NH2   1 
ATOM   8901  N  N     . LYS F 1 280 ? -4.366  -62.311 27.12   1 32.9  ? 280 LYS Z N     1 
ATOM   8902  C  CA    . LYS F 1 280 ? -3.664  -62.12  28.386  1 33.22 ? 280 LYS Z CA    1 
ATOM   8903  C  C     . LYS F 1 280 ? -2.469  -63.055 28.5    1 33.42 ? 280 LYS Z C     1 
ATOM   8904  O  O     . LYS F 1 280 ? -2.598  -64.25  28.245  1 33.72 ? 280 LYS Z O     1 
ATOM   8905  C  CB    . LYS F 1 280 ? -4.641  -62.357 29.554  1 35.01 ? 280 LYS Z CB    1 
ATOM   8906  C  CG    . LYS F 1 280 ? -4.012  -62.469 30.944  1 39.04 ? 280 LYS Z CG    1 
ATOM   8907  C  CD    . LYS F 1 280 ? -3.573  -61.128 31.495  1 43.25 ? 280 LYS Z CD    1 
ATOM   8908  C  CE    . LYS F 1 280 ? -2.96   -61.238 32.868  1 46.48 ? 280 LYS Z CE    1 
ATOM   8909  N  NZ    . LYS F 1 280 ? -2.011  -62.367 32.95   1 48.91 ? 280 LYS Z NZ    1 
ATOM   8910  N  N     . LYS F 1 281 ? -1.314  -62.52  28.901  1 33.21 ? 281 LYS Z N     1 
ATOM   8911  C  CA    . LYS F 1 281 ? -0.115  -63.326 29.084  1 33.55 ? 281 LYS Z CA    1 
ATOM   8912  C  C     . LYS F 1 281 ? 0.024   -63.772 30.542  1 33.4  ? 281 LYS Z C     1 
ATOM   8913  O  O     . LYS F 1 281 ? 0.194   -62.937 31.422  1 33.38 ? 281 LYS Z O     1 
ATOM   8914  C  CB    . LYS F 1 281 ? 1.131   -62.54  28.666  1 35.64 ? 281 LYS Z CB    1 
ATOM   8915  C  CG    . LYS F 1 281 ? 1.333   -62.475 27.167  1 40.29 ? 281 LYS Z CG    1 
ATOM   8916  C  CD    . LYS F 1 281 ? 2.818   -62.352 26.839  1 45.52 ? 281 LYS Z CD    1 
ATOM   8917  C  CE    . LYS F 1 281 ? 3.343   -60.945 26.984  1 50.13 ? 281 LYS Z CE    1 
ATOM   8918  N  NZ    . LYS F 1 281 ? 2.836   -60.053 25.904  1 52.92 ? 281 LYS Z NZ    1 
ATOM   8919  N  N     . ILE F 1 282 ? -0.03   -65.083 30.798  1 33.05 ? 282 ILE Z N     1 
ATOM   8920  C  CA    . ILE F 1 282 ? 0.101   -65.607 32.153  1 33.11 ? 282 ILE Z CA    1 
ATOM   8921  C  C     . ILE F 1 282 ? 1.352   -66.478 32.252  1 33.33 ? 282 ILE Z C     1 
ATOM   8922  O  O     . ILE F 1 282 ? 1.522   -67.39  31.446  1 33.52 ? 282 ILE Z O     1 
ATOM   8923  C  CB    . ILE F 1 282 ? -1.168  -66.405 32.549  1 33.42 ? 282 ILE Z CB    1 
ATOM   8924  C  CG1   . ILE F 1 282 ? -2.436  -65.545 32.428  1 34.35 ? 282 ILE Z CG1   1 
ATOM   8925  C  CG2   . ILE F 1 282 ? -1.031  -66.986 33.947  1 33.8  ? 282 ILE Z CG2   1 
ATOM   8926  C  CD1   . ILE F 1 282 ? -3.728  -66.297 32.598  1 35.6  ? 282 ILE Z CD1   1 
ATOM   8927  N  N     . ALA F 1 283 ? 2.232   -66.203 33.225  1 33.3  ? 283 ALA Z N     1 
ATOM   8928  C  CA    . ALA F 1 283 ? 3.435   -67.013 33.424  1 33.71 ? 283 ALA Z CA    1 
ATOM   8929  C  C     . ALA F 1 283 ? 3.034   -68.416 33.867  1 34.03 ? 283 ALA Z C     1 
ATOM   8930  O  O     . ALA F 1 283 ? 2.061   -68.567 34.606  1 33.84 ? 283 ALA Z O     1 
ATOM   8931  C  CB    . ALA F 1 283 ? 4.322   -66.38  34.481  1 33.83 ? 283 ALA Z CB    1 
ATOM   8932  N  N     . GLU F 1 284 ? 3.778   -69.446 33.433  1 34.31 ? 284 GLU Z N     1 
ATOM   8933  C  CA    . GLU F 1 284 ? 3.471   -70.835 33.789  1 34.92 ? 284 GLU Z CA    1 
ATOM   8934  C  C     . GLU F 1 284 ? 3.433   -71.052 35.289  1 34.78 ? 284 GLU Z C     1 
ATOM   8935  O  O     . GLU F 1 284 ? 2.576   -71.787 35.779  1 34.7  ? 284 GLU Z O     1 
ATOM   8936  C  CB    . GLU F 1 284 ? 4.455   -71.817 33.137  1 37.73 ? 284 GLU Z CB    1 
ATOM   8937  C  CG    . GLU F 1 284 ? 3.991   -72.315 31.783  1 43.69 ? 284 GLU Z CG    1 
ATOM   8938  C  CD    . GLU F 1 284 ? 4.927   -73.325 31.155  1 52.17 ? 284 GLU Z CD    1 
ATOM   8939  O  OE1   . GLU F 1 284 ? 5.397   -73.089 30.015  1 54.36 ? 284 GLU Z OE1   1 
ATOM   8940  O  OE2   . GLU F 1 284 ? 5.2     -74.352 31.816  1 54.35 ? 284 GLU Z OE2   1 
ATOM   8941  N  N     . LYS F 1 285 ? 4.324   -70.371 36.023  1 34.6  ? 285 LYS Z N     1 
ATOM   8942  C  CA    . LYS F 1 285 ? 4.376   -70.466 37.48   1 34.98 ? 285 LYS Z CA    1 
ATOM   8943  C  C     . LYS F 1 285 ? 3.105   -69.935 38.161  1 35.6  ? 285 LYS Z C     1 
ATOM   8944  O  O     . LYS F 1 285 ? 2.805   -70.338 39.281  1 36.11 ? 285 LYS Z O     1 
ATOM   8945  C  CB    . LYS F 1 285 ? 5.629   -69.763 38.032  1 36.37 ? 285 LYS Z CB    1 
ATOM   8946  C  CG    . LYS F 1 285 ? 5.67    -68.26  37.765  1 39.83 ? 285 LYS Z CG    1 
ATOM   8947  C  CD    . LYS F 1 285 ? 6.919   -67.592 38.339  1 43.12 ? 285 LYS Z CD    1 
ATOM   8948  C  CE    . LYS F 1 285 ? 6.931   -66.096 38.113  1 45.81 ? 285 LYS Z CE    1 
ATOM   8949  N  NZ    . LYS F 1 285 ? 8.079   -65.439 38.795  1 47.46 ? 285 LYS Z NZ    1 
ATOM   8950  N  N     . SER F 1 286 ? 2.351   -69.056 37.486  1 35.58 ? 286 SER Z N     1 
ATOM   8951  C  CA    . SER F 1 286 ? 1.116   -68.484 38.012  1 36.14 ? 286 SER Z CA    1 
ATOM   8952  C  C     . SER F 1 286 ? -0.123  -69.348 37.745  1 36.97 ? 286 SER Z C     1 
ATOM   8953  O  O     . SER F 1 286 ? -1.176  -69.073 38.32   1 37.22 ? 286 SER Z O     1 
ATOM   8954  C  CB    . SER F 1 286 ? 0.882   -67.103 37.413  1 37.17 ? 286 SER Z CB    1 
ATOM   8955  O  OG    . SER F 1 286 ? 2.008   -66.259 37.579  1 39.42 ? 286 SER Z OG    1 
ATOM   8956  N  N     . LEU F 1 287 ? -0.026  -70.358 36.859  1 37.13 ? 287 LEU Z N     1 
ATOM   8957  C  CA    . LEU F 1 287 ? -1.173  -71.19  36.511  1 37.73 ? 287 LEU Z CA    1 
ATOM   8958  C  C     . LEU F 1 287 ? -1.614  -72.124 37.614  1 38.8  ? 287 LEU Z C     1 
ATOM   8959  O  O     . LEU F 1 287 ? -0.787  -72.671 38.343  1 39.1  ? 287 LEU Z O     1 
ATOM   8960  C  CB    . LEU F 1 287 ? -0.925  -71.973 35.219  1 37.65 ? 287 LEU Z CB    1 
ATOM   8961  C  CG    . LEU F 1 287 ? -0.914  -71.15  33.943  1 38.93 ? 287 LEU Z CG    1 
ATOM   8962  C  CD1   . LEU F 1 287 ? -0.556  -72.004 32.762  1 39.47 ? 287 LEU Z CD1   1 
ATOM   8963  C  CD2   . LEU F 1 287 ? -2.255  -70.502 33.696  1 39.5  ? 287 LEU Z CD2   1 
ATOM   8964  N  N     . SER F 1 288 ? -2.934  -72.312 37.719  1 39.25 ? 288 SER Z N     1 
ATOM   8965  C  CA    . SER F 1 288 ? -3.607  -73.184 38.685  1 40.09 ? 288 SER Z CA    1 
ATOM   8966  C  C     . SER F 1 288 ? -5.073  -73.398 38.246  1 40.39 ? 288 SER Z C     1 
ATOM   8967  O  O     . SER F 1 288 ? -5.546  -72.726 37.336  1 40.32 ? 288 SER Z O     1 
ATOM   8968  C  CB    . SER F 1 288 ? -3.561  -72.562 40.08   1 41.85 ? 288 SER Z CB    1 
ATOM   8969  O  OG    . SER F 1 288 ? -2.252  -72.559 40.624  1 44.64 ? 288 SER Z OG    1 
ATOM   8970  N  N     . GLY F 1 289 ? -5.769  -74.341 38.874  1 40.72 ? 289 GLY Z N     1 
ATOM   8971  C  CA    . GLY F 1 289 ? -7.174  -74.633 38.595  1 41.67 ? 289 GLY Z CA    1 
ATOM   8972  C  C     . GLY F 1 289 ? -7.588  -74.658 37.136  1 42.42 ? 289 GLY Z C     1 
ATOM   8973  O  O     . GLY F 1 289 ? -6.972  -75.352 36.327  1 42.71 ? 289 GLY Z O     1 
ATOM   8974  N  N     . LYS F 1 290 ? -8.619  -73.878 36.785  1 42.65 ? 290 LYS Z N     1 
ATOM   8975  C  CA    . LYS F 1 290 ? -9.104  -73.795 35.407  1 43.47 ? 290 LYS Z CA    1 
ATOM   8976  C  C     . LYS F 1 290 ? -8.732  -72.467 34.734  1 44.21 ? 290 LYS Z C     1 
ATOM   8977  O  O     . LYS F 1 290 ? -9.41   -72.056 33.797  1 44.4  ? 290 LYS Z O     1 
ATOM   8978  C  CB    . LYS F 1 290 ? -10.625 -73.999 35.363  1 45.19 ? 290 LYS Z CB    1 
ATOM   8979  C  CG    . LYS F 1 290 ? -11.064 -75.345 35.909  1 49.21 ? 290 LYS Z CG    1 
ATOM   8980  C  CD    . LYS F 1 290 ? -12.559 -75.387 36.166  1 53.96 ? 290 LYS Z CD    1 
ATOM   8981  C  CE    . LYS F 1 290 ? -12.969 -76.659 36.87   1 58.33 ? 290 LYS Z CE    1 
ATOM   8982  N  NZ    . LYS F 1 290 ? -14.336 -76.559 37.446  1 60.9  ? 290 LYS Z NZ    1 
ATOM   8983  N  N     . VAL F 1 291 ? -7.661  -71.804 35.207  1 44.41 ? 291 VAL Z N     1 
ATOM   8984  C  CA    . VAL F 1 291 ? -7.197  -70.51  34.704  1 44.94 ? 291 VAL Z CA    1 
ATOM   8985  C  C     . VAL F 1 291 ? -6.816  -70.548 33.226  1 45.33 ? 291 VAL Z C     1 
ATOM   8986  O  O     . VAL F 1 291 ? -7.267  -69.689 32.47   1 45.24 ? 291 VAL Z O     1 
ATOM   8987  C  CB    . VAL F 1 291 ? -6.062  -69.956 35.592  1 45.67 ? 291 VAL Z CB    1 
ATOM   8988  C  CG1   . VAL F 1 291 ? -5.466  -68.685 35.003  1 46.37 ? 291 VAL Z CG1   1 
ATOM   8989  C  CG2   . VAL F 1 291 ? -6.564  -69.708 37.007  1 45.97 ? 291 VAL Z CG2   1 
ATOM   8990  N  N     . LYS F 1 292 ? -6.039  -71.559 32.8    1 45.75 ? 292 LYS Z N     1 
ATOM   8991  C  CA    . LYS F 1 292 ? -5.658  -71.694 31.389  1 46.54 ? 292 LYS Z CA    1 
ATOM   8992  C  C     . LYS F 1 292 ? -6.905  -71.89  30.512  1 47.22 ? 292 LYS Z C     1 
ATOM   8993  O  O     . LYS F 1 292 ? -7.008  -71.292 29.444  1 47.48 ? 292 LYS Z O     1 
ATOM   8994  C  CB    . LYS F 1 292 ? -4.667  -72.853 31.184  1 48.23 ? 292 LYS Z CB    1 
ATOM   8995  C  CG    . LYS F 1 292 ? -4.085  -72.886 29.772  1 52.44 ? 292 LYS Z CG    1 
ATOM   8996  C  CD    . LYS F 1 292 ? -3.268  -74.138 29.481  1 56.9  ? 292 LYS Z CD    1 
ATOM   8997  C  CE    . LYS F 1 292 ? -2.574  -74.068 28.142  1 60.63 ? 292 LYS Z CE    1 
ATOM   8998  N  NZ    . LYS F 1 292 ? -3.497  -73.764 27.021  1 62.84 ? 292 LYS Z NZ    1 
ATOM   8999  N  N     . GLU F 1 293 ? -7.874  -72.676 31.003  1 47.33 ? 293 GLU Z N     1 
ATOM   9000  C  CA    . GLU F 1 293 ? -9.144  -72.947 30.332  1 47.93 ? 293 GLU Z CA    1 
ATOM   9001  C  C     . GLU F 1 293 ? -9.988  -71.666 30.198  1 47.76 ? 293 GLU Z C     1 
ATOM   9002  O  O     . GLU F 1 293 ? -10.565 -71.409 29.138  1 47.65 ? 293 GLU Z O     1 
ATOM   9003  C  CB    . GLU F 1 293 ? -9.921  -74.025 31.106  1 51.02 ? 293 GLU Z CB    1 
ATOM   9004  C  CG    . GLU F 1 293 ? -9.223  -75.376 31.149  1 57.31 ? 293 GLU Z CG    1 
ATOM   9005  C  CD    . GLU F 1 293 ? -8.361  -75.658 32.366  1 65.26 ? 293 GLU Z CD    1 
ATOM   9006  O  OE1   . GLU F 1 293 ? -8.683  -76.614 33.11   1 67.22 ? 293 GLU Z OE1   1 
ATOM   9007  O  OE2   . GLU F 1 293 ? -7.363  -74.931 32.578  1 67.67 ? 293 GLU Z OE2   1 
ATOM   9008  N  N     . PHE F 1 294 ? -10.034 -70.854 31.267  1 47.51 ? 294 PHE Z N     1 
ATOM   9009  C  CA    . PHE F 1 294 ? -10.766 -69.593 31.263  1 47.71 ? 294 PHE Z CA    1 
ATOM   9010  C  C     . PHE F 1 294 ? -10.129 -68.63  30.27   1 47.56 ? 294 PHE Z C     1 
ATOM   9011  O  O     . PHE F 1 294 ? -10.845 -67.956 29.531  1 47.79 ? 294 PHE Z O     1 
ATOM   9012  C  CB    . PHE F 1 294 ? -10.809 -68.963 32.668  1 47.78 ? 294 PHE Z CB    1 
ATOM   9013  C  CG    . PHE F 1 294 ? -11.483 -67.61  32.688  1 48.59 ? 294 PHE Z CG    1 
ATOM   9014  C  CD1   . PHE F 1 294 ? -12.861 -67.505 32.71   1 49.38 ? 294 PHE Z CD1   1 
ATOM   9015  C  CD2   . PHE F 1 294 ? -10.738 -66.444 32.635  1 49.49 ? 294 PHE Z CD2   1 
ATOM   9016  C  CE1   . PHE F 1 294 ? -13.478 -66.263 32.7    1 50.12 ? 294 PHE Z CE1   1 
ATOM   9017  C  CE2   . PHE F 1 294 ? -11.359 -65.205 32.607  1 50.19 ? 294 PHE Z CE2   1 
ATOM   9018  C  CZ    . PHE F 1 294 ? -12.722 -65.122 32.652  1 49.98 ? 294 PHE Z CZ    1 
ATOM   9019  N  N     . ASN F 1 295 ? -8.789  -68.572 30.233  1 46.92 ? 295 ASN Z N     1 
ATOM   9020  C  CA    . ASN F 1 295 ? -8.095  -67.686 29.304  1 46.84 ? 295 ASN Z CA    1 
ATOM   9021  C  C     . ASN F 1 295 ? -8.413  -68.057 27.857  1 46.88 ? 295 ASN Z C     1 
ATOM   9022  O  O     . ASN F 1 295 ? -8.62   -67.167 27.04   1 47.04 ? 295 ASN Z O     1 
ATOM   9023  C  CB    . ASN F 1 295 ? -6.588  -67.681 29.563  1 47.58 ? 295 ASN Z CB    1 
ATOM   9024  C  CG    . ASN F 1 295 ? -5.888  -66.45  29.037  1 50.04 ? 295 ASN Z CG    1 
ATOM   9025  O  OD1   . ASN F 1 295 ? -6.516  -65.482 28.595  1 50.83 ? 295 ASN Z OD1   1 
ATOM   9026  N  ND2   . ASN F 1 295 ? -4.564  -66.458 29.071  1 50.54 ? 295 ASN Z ND2   1 
ATOM   9027  N  N     . ASN F 1 296 ? -8.539  -69.362 27.562  1 46.69 ? 296 ASN Z N     1 
ATOM   9028  C  CA    . ASN F 1 296 ? -8.9    -69.827 26.225  1 47.05 ? 296 ASN Z CA    1 
ATOM   9029  C  C     . ASN F 1 296 ? -10.307 -69.366 25.853  1 46.78 ? 296 ASN Z C     1 
ATOM   9030  O  O     . ASN F 1 296 ? -10.531 -68.976 24.715  1 46.93 ? 296 ASN Z O     1 
ATOM   9031  C  CB    . ASN F 1 296 ? -8.807  -71.347 26.126  1 48.78 ? 296 ASN Z CB    1 
ATOM   9032  C  CG    . ASN F 1 296 ? -7.421  -71.903 26.342  1 52.97 ? 296 ASN Z CG    1 
ATOM   9033  O  OD1   . ASN F 1 296 ? -7.248  -73     26.885  1 54.74 ? 296 ASN Z OD1   1 
ATOM   9034  N  ND2   . ASN F 1 296 ? -6.4    -71.163 25.936  1 53.74 ? 296 ASN Z ND2   1 
ATOM   9035  N  N     . ILE F 1 297 ? -11.244 -69.392 26.813  1 46.26 ? 297 ILE Z N     1 
ATOM   9036  C  CA    . ILE F 1 297 ? -12.618 -68.945 26.589  1 46.18 ? 297 ILE Z CA    1 
ATOM   9037  C  C     . ILE F 1 297 ? -12.632 -67.459 26.267  1 46.26 ? 297 ILE Z C     1 
ATOM   9038  O  O     . ILE F 1 297 ? -13.314 -67.047 25.333  1 46.38 ? 297 ILE Z O     1 
ATOM   9039  C  CB    . ILE F 1 297 ? -13.521 -69.285 27.799  1 46.38 ? 297 ILE Z CB    1 
ATOM   9040  C  CG1   . ILE F 1 297 ? -13.707 -70.799 27.931  1 46.9  ? 297 ILE Z CG1   1 
ATOM   9041  C  CG2   . ILE F 1 297 ? -14.872 -68.559 27.721  1 46.9  ? 297 ILE Z CG2   1 
ATOM   9042  C  CD1   . ILE F 1 297 ? -14.33  -71.212 29.192  1 48.03 ? 297 ILE Z CD1   1 
ATOM   9043  N  N     . VAL F 1 298 ? -11.849 -66.658 27.007  1 46.07 ? 298 VAL Z N     1 
ATOM   9044  C  CA    . VAL F 1 298 ? -11.761 -65.217 26.763  1 46.24 ? 298 VAL Z CA    1 
ATOM   9045  C  C     . VAL F 1 298 ? -11.239 -64.937 25.351  1 46.6  ? 298 VAL Z C     1 
ATOM   9046  O  O     . VAL F 1 298 ? -11.857 -64.173 24.616  1 46.75 ? 298 VAL Z O     1 
ATOM   9047  C  CB    . VAL F 1 298 ? -10.907 -64.518 27.837  1 46.62 ? 298 VAL Z CB    1 
ATOM   9048  C  CG1   . VAL F 1 298 ? -10.685 -63.062 27.485  1 47.03 ? 298 VAL Z CG1   1 
ATOM   9049  C  CG2   . VAL F 1 298 ? -11.562 -64.635 29.198  1 47    ? 298 VAL Z CG2   1 
ATOM   9050  N  N     . GLN F 1 299 ? -10.149 -65.618 24.948  1 46.41 ? 299 GLN Z N     1 
ATOM   9051  C  CA    . GLN F 1 299 ? -9.553  -65.465 23.617  1 46.44 ? 299 GLN Z CA    1 
ATOM   9052  C  C     . GLN F 1 299 ? -10.46  -65.943 22.471  1 47    ? 299 GLN Z C     1 
ATOM   9053  O  O     . GLN F 1 299 ? -10.214 -65.612 21.317  1 47.22 ? 299 GLN Z O     1 
ATOM   9054  C  CB    . GLN F 1 299 ? -8.173  -66.135 23.56   1 47.15 ? 299 GLN Z CB    1 
ATOM   9055  C  CG    . GLN F 1 299 ? -7.224  -65.537 24.587  1 49.58 ? 299 GLN Z CG    1 
ATOM   9056  C  CD    . GLN F 1 299 ? -5.79   -65.961 24.43   1 53.04 ? 299 GLN Z CD    1 
ATOM   9057  O  OE1   . GLN F 1 299 ? -5.336  -66.31  23.339  1 54.37 ? 299 GLN Z OE1   1 
ATOM   9058  N  NE2   . GLN F 1 299 ? -5.036  -65.915 25.523  1 53.39 ? 299 GLN Z NE2   1 
ATOM   9059  N  N     . ARG F 1 300 ? -11.522 -66.68  22.784  1 47.16 ? 300 ARG Z N     1 
ATOM   9060  C  CA    . ARG F 1 300 ? -12.479 -67.143 21.793  1 47.74 ? 300 ARG Z CA    1 
ATOM   9061  C  C     . ARG F 1 300 ? -13.444 -66.043 21.376  1 47.69 ? 300 ARG Z C     1 
ATOM   9062  O  O     . ARG F 1 300 ? -13.872 -66.031 20.225  1 48.11 ? 300 ARG Z O     1 
ATOM   9063  C  CB    . ARG F 1 300 ? -13.27  -68.318 22.36   1 49.48 ? 300 ARG Z CB    1 
ATOM   9064  C  CG    . ARG F 1 300 ? -12.398 -69.495 22.492  1 53.41 ? 300 ARG Z CG    1 
ATOM   9065  C  CD    . ARG F 1 300 ? -13.012 -70.589 21.712  1 57.5  ? 300 ARG Z CD    1 
ATOM   9066  N  NE    . ARG F 1 300 ? -13.909 -71.362 22.557  1 61.28 ? 300 ARG Z NE    1 
ATOM   9067  C  CZ    . ARG F 1 300 ? -15.012 -71.966 22.121  1 64.05 ? 300 ARG Z CZ    1 
ATOM   9068  N  NH1   . ARG F 1 300 ? -15.345 -71.914 20.834  1 63.47 ? 300 ARG Z NH1   1 
ATOM   9069  N  NH2   . ARG F 1 300 ? -15.781 -72.643 22.965  1 64.4  ? 300 ARG Z NH2   1 
ATOM   9070  N  N     . TYR F 1 301 ? -13.784 -65.12  22.296  1 46.85 ? 301 TYR Z N     1 
ATOM   9071  C  CA    . TYR F 1 301 ? -14.773 -64.075 22.02   1 46.54 ? 301 TYR Z CA    1 
ATOM   9072  C  C     . TYR F 1 301 ? -14.293 -62.644 22.151  1 46.01 ? 301 TYR Z C     1 
ATOM   9073  O  O     . TYR F 1 301 ? -15.017 -61.725 21.761  1 46.05 ? 301 TYR Z O     1 
ATOM   9074  C  CB    . TYR F 1 301 ? -15.96  -64.229 22.969  1 46.58 ? 301 TYR Z CB    1 
ATOM   9075  C  CG    . TYR F 1 301 ? -16.603 -65.59  22.918  1 47.35 ? 301 TYR Z CG    1 
ATOM   9076  C  CD1   . TYR F 1 301 ? -16.103 -66.645 23.663  1 48.3  ? 301 TYR Z CD1   1 
ATOM   9077  C  CD2   . TYR F 1 301 ? -17.728 -65.82  22.142  1 48.18 ? 301 TYR Z CD2   1 
ATOM   9078  C  CE1   . TYR F 1 301 ? -16.68  -67.903 23.61   1 49.13 ? 301 TYR Z CE1   1 
ATOM   9079  C  CE2   . TYR F 1 301 ? -18.318 -67.072 22.088  1 49.1  ? 301 TYR Z CE2   1 
ATOM   9080  C  CZ    . TYR F 1 301 ? -17.82  -68.101 22.861  1 49.93 ? 301 TYR Z CZ    1 
ATOM   9081  O  OH    . TYR F 1 301 ? -18.426 -69.332 22.846  1 51.28 ? 301 TYR Z OH    1 
ATOM   9082  N  N     . SER F 1 302 ? -13.133 -62.437 22.759  1 45.32 ? 302 SER Z N     1 
ATOM   9083  C  CA    . SER F 1 302 ? -12.631 -61.099 23.018  1 45.14 ? 302 SER Z CA    1 
ATOM   9084  C  C     . SER F 1 302 ? -12.155 -60.326 21.799  1 45.1  ? 302 SER Z C     1 
ATOM   9085  O  O     . SER F 1 302 ? -11.788 -60.899 20.775  1 45.33 ? 302 SER Z O     1 
ATOM   9086  C  CB    . SER F 1 302 ? -11.519 -61.137 24.063  1 45.93 ? 302 SER Z CB    1 
ATOM   9087  O  OG    . SER F 1 302 ? -10.338 -61.726 23.544  1 47.69 ? 302 SER Z OG    1 
ATOM   9088  N  N     . VAL F 1 303 ? -12.209 -59.002 21.923  1 44.48 ? 303 VAL Z N     1 
ATOM   9089  C  CA    . VAL F 1 303 ? -11.669 -58.035 20.993  1 44.46 ? 303 VAL Z CA    1 
ATOM   9090  C  C     . VAL F 1 303 ? -10.679 -57.209 21.827  1 44.35 ? 303 VAL Z C     1 
ATOM   9091  O  O     . VAL F 1 303 ? -10.904 -56.961 23.018  1 44.87 ? 303 VAL Z O     1 
ATOM   9092  C  CB    . VAL F 1 303 ? -12.736 -57.183 20.26   1 45.24 ? 303 VAL Z CB    1 
ATOM   9093  C  CG1   . VAL F 1 303 ? -13.631 -58.059 19.401  1 45.97 ? 303 VAL Z CG1   1 
ATOM   9094  C  CG2   . VAL F 1 303 ? -13.572 -56.366 21.227  1 45.68 ? 303 VAL Z CG2   1 
ATOM   9095  N  N     . GLY F 1 304 ? -9.548  -56.882 21.237  1 43.6  ? 304 GLY Z N     1 
ATOM   9096  C  CA    . GLY F 1 304 ? -8.493  -56.16  21.929  1 43.33 ? 304 GLY Z CA    1 
ATOM   9097  C  C     . GLY F 1 304 ? -8.847  -54.727 22.249  1 42.86 ? 304 GLY Z C     1 
ATOM   9098  O  O     . GLY F 1 304 ? -9.459  -54.034 21.437  1 42.93 ? 304 GLY Z O     1 
ATOM   9099  N  N     . LEU F 1 305 ? -8.479  -54.281 23.446  1 42.33 ? 305 LEU Z N     1 
ATOM   9100  C  CA    . LEU F 1 305 ? -8.721  -52.91  23.869  1 42.28 ? 305 LEU Z CA    1 
ATOM   9101  C  C     . LEU F 1 305 ? -7.359  -52.249 24.023  1 41.83 ? 305 LEU Z C     1 
ATOM   9102  O  O     . LEU F 1 305 ? -6.649  -52.546 24.983  1 42    ? 305 LEU Z O     1 
ATOM   9103  C  CB    . LEU F 1 305 ? -9.476  -52.884 25.204  1 42.61 ? 305 LEU Z CB    1 
ATOM   9104  C  CG    . LEU F 1 305 ? -10.017 -51.522 25.613  1 44.57 ? 305 LEU Z CG    1 
ATOM   9105  C  CD1   . LEU F 1 305 ? -11.119 -51.057 24.667  1 45.35 ? 305 LEU Z CD1   1 
ATOM   9106  C  CD2   . LEU F 1 305 ? -10.522 -51.541 27.036  1 45.38 ? 305 LEU Z CD2   1 
ATOM   9107  N  N     . ALA F 1 306 ? -6.972  -51.389 23.053  1 40.98 ? 306 ALA Z N     1 
ATOM   9108  C  CA    . ALA F 1 306 ? -5.698  -50.656 22.976  1 40.74 ? 306 ALA Z CA    1 
ATOM   9109  C  C     . ALA F 1 306 ? -4.507  -51.526 22.584  1 40.18 ? 306 ALA Z C     1 
ATOM   9110  O  O     . ALA F 1 306 ? -3.717  -51.127 21.737  1 40.36 ? 306 ALA Z O     1 
ATOM   9111  C  CB    . ALA F 1 306 ? -5.406  -49.888 24.263  1 41.04 ? 306 ALA Z CB    1 
ATOM   9112  N  N     . SER F 1 307 ? -4.357  -52.692 23.204  1 39.47 ? 307 SER Z N     1 
ATOM   9113  C  CA    . SER F 1 307 ? -3.272  -53.617 22.888  1 39.34 ? 307 SER Z CA    1 
ATOM   9114  C  C     . SER F 1 307 ? -3.72   -55.04  23.16   1 39.03 ? 307 SER Z C     1 
ATOM   9115  O  O     . SER F 1 307 ? -4.436  -55.287 24.133  1 39.3  ? 307 SER Z O     1 
ATOM   9116  C  CB    . SER F 1 307 ? -2.037  -53.311 23.724  1 40.6  ? 307 SER Z CB    1 
ATOM   9117  O  OG    . SER F 1 307 ? -1.383  -52.136 23.277  1 42.93 ? 307 SER Z OG    1 
ATOM   9118  N  N     . SER F 1 308 ? -3.285  -55.985 22.324  1 38.21 ? 308 SER Z N     1 
ATOM   9119  C  CA    . SER F 1 308 ? -3.649  -57.384 22.5    1 37.79 ? 308 SER Z CA    1 
ATOM   9120  C  C     . SER F 1 308 ? -3.146  -57.949 23.829  1 36.96 ? 308 SER Z C     1 
ATOM   9121  O  O     . SER F 1 308 ? -3.831  -58.771 24.433  1 37.02 ? 308 SER Z O     1 
ATOM   9122  C  CB    . SER F 1 308 ? -3.117  -58.226 21.343  1 39.25 ? 308 SER Z CB    1 
ATOM   9123  O  OG    . SER F 1 308 ? -1.708  -58.368 21.393  1 41.75 ? 308 SER Z OG    1 
ATOM   9124  N  N     . ASP F 1 309 ? -1.967  -57.5   24.296  1 36.02 ? 309 ASP Z N     1 
ATOM   9125  C  CA    . ASP F 1 309 ? -1.396  -58.039 25.521  1 35.61 ? 309 ASP Z CA    1 
ATOM   9126  C  C     . ASP F 1 309 ? -1.572  -57.17  26.76   1 35.05 ? 309 ASP Z C     1 
ATOM   9127  O  O     . ASP F 1 309 ? -0.927  -57.45  27.767  1 35.36 ? 309 ASP Z O     1 
ATOM   9128  C  CB    . ASP F 1 309 ? 0.074   -58.43  25.348  1 37.18 ? 309 ASP Z CB    1 
ATOM   9129  C  CG    . ASP F 1 309 ? 1.02    -57.302 25.006  1 41.63 ? 309 ASP Z CG    1 
ATOM   9130  O  OD1   . ASP F 1 309 ? 0.555   -56.282 24.452  1 42.54 ? 309 ASP Z OD1   1 
ATOM   9131  O  OD2   . ASP F 1 309 ? 2.23    -57.447 25.272  1 43.64 ? 309 ASP Z OD2   1 
ATOM   9132  N  N     . LEU F 1 310 ? -2.476  -56.181 26.732  1 34.12 ? 310 LEU Z N     1 
ATOM   9133  C  CA    . LEU F 1 310 ? -2.798  -55.437 27.951  1 33.76 ? 310 LEU Z CA    1 
ATOM   9134  C  C     . LEU F 1 310 ? -3.67   -56.385 28.81   1 33.73 ? 310 LEU Z C     1 
ATOM   9135  O  O     . LEU F 1 310 ? -4.296  -57.287 28.251  1 33.61 ? 310 LEU Z O     1 
ATOM   9136  C  CB    . LEU F 1 310 ? -3.531  -54.132 27.635  1 33.64 ? 310 LEU Z CB    1 
ATOM   9137  C  CG    . LEU F 1 310 ? -2.631  -52.957 27.306  1 34.87 ? 310 LEU Z CG    1 
ATOM   9138  C  CD1   . LEU F 1 310 ? -3.443  -51.754 26.926  1 35.53 ? 310 LEU Z CD1   1 
ATOM   9139  C  CD2   . LEU F 1 310 ? -1.714  -52.615 28.465  1 35.45 ? 310 LEU Z CD2   1 
ATOM   9140  N  N     . PRO F 1 311 ? -3.72   -56.249 30.156  1 33.61 ? 311 PRO Z N     1 
ATOM   9141  C  CA    . PRO F 1 311 ? -4.485  -57.22  30.966  1 33.61 ? 311 PRO Z CA    1 
ATOM   9142  C  C     . PRO F 1 311 ? -6.003  -57.136 30.886  1 33.69 ? 311 PRO Z C     1 
ATOM   9143  O  O     . PRO F 1 311 ? -6.678  -57.712 31.728  1 33.75 ? 311 PRO Z O     1 
ATOM   9144  C  CB    . PRO F 1 311 ? -4.004  -56.94  32.387  1 34.27 ? 311 PRO Z CB    1 
ATOM   9145  C  CG    . PRO F 1 311 ? -3.66   -55.494 32.361  1 34.62 ? 311 PRO Z CG    1 
ATOM   9146  C  CD    . PRO F 1 311 ? -3.031  -55.269 31.015  1 33    ? 311 PRO Z CD    1 
ATOM   9147  N  N     . PHE F 1 312 ? -6.539  -56.442 29.888  1 33.51 ? 312 PHE Z N     1 
ATOM   9148  C  CA    . PHE F 1 312 ? -7.976  -56.296 29.729  1 33.74 ? 312 PHE Z CA    1 
ATOM   9149  C  C     . PHE F 1 312 ? -8.385  -56.261 28.267  1 34.7  ? 312 PHE Z C     1 
ATOM   9150  O  O     . PHE F 1 312 ? -7.6    -55.893 27.396  1 34.85 ? 312 PHE Z O     1 
ATOM   9151  C  CB    . PHE F 1 312 ? -8.499  -55.059 30.486  1 33.01 ? 312 PHE Z CB    1 
ATOM   9152  C  CG    . PHE F 1 312 ? -7.697  -53.81  30.234  1 33.15 ? 312 PHE Z CG    1 
ATOM   9153  C  CD1   . PHE F 1 312 ? -6.587  -53.515 31.001  1 33.71 ? 312 PHE Z CD1   1 
ATOM   9154  C  CD2   . PHE F 1 312 ? -8.049  -52.933 29.225  1 33.79 ? 312 PHE Z CD2   1 
ATOM   9155  C  CE1   . PHE F 1 312 ? -5.84   -52.375 30.753  1 34.35 ? 312 PHE Z CE1   1 
ATOM   9156  C  CE2   . PHE F 1 312 ? -7.297  -51.796 28.977  1 34.23 ? 312 PHE Z CE2   1 
ATOM   9157  C  CZ    . PHE F 1 312 ? -6.196  -51.526 29.739  1 34.02 ? 312 PHE Z CZ    1 
ATOM   9158  N  N     . GLY F 1 313 ? -9.616  -56.652 28.014  1 35.25 ? 313 GLY Z N     1 
ATOM   9159  C  CA    . GLY F 1 313 ? -10.192 -56.651 26.678  1 36.49 ? 313 GLY Z CA    1 
ATOM   9160  C  C     . GLY F 1 313 ? -11.693 -56.496 26.723  1 37.61 ? 313 GLY Z C     1 
ATOM   9161  O  O     . GLY F 1 313 ? -12.262 -56.268 27.793  1 37.86 ? 313 GLY Z O     1 
ATOM   9162  N  N     . VAL F 1 314 ? -12.352 -56.586 25.562  1 38.1  ? 314 VAL Z N     1 
ATOM   9163  C  CA    . VAL F 1 314 ? -13.802 -56.42  25.514  1 39.15 ? 314 VAL Z CA    1 
ATOM   9164  C  C     . VAL F 1 314 ? -14.488 -57.648 24.964  1 39.75 ? 314 VAL Z C     1 
ATOM   9165  O  O     . VAL F 1 314 ? -13.979 -58.283 24.053  1 39.89 ? 314 VAL Z O     1 
ATOM   9166  C  CB    . VAL F 1 314 ? -14.217 -55.157 24.713  1 40.16 ? 314 VAL Z CB    1 
ATOM   9167  C  CG1   . VAL F 1 314 ? -15.729 -54.948 24.744  1 40.85 ? 314 VAL Z CG1   1 
ATOM   9168  C  CG2   . VAL F 1 314 ? -13.495 -53.914 25.218  1 40.69 ? 314 VAL Z CG2   1 
ATOM   9169  N  N     . ILE F 1 315 ? -15.636 -57.992 25.539  1 39.96 ? 315 ILE Z N     1 
ATOM   9170  C  CA    . ILE F 1 315 ? -16.525 -59.03  25.061  1 40.57 ? 315 ILE Z CA    1 
ATOM   9171  C  C     . ILE F 1 315 ? -17.738 -58.214 24.634  1 41.65 ? 315 ILE Z C     1 
ATOM   9172  O  O     . ILE F 1 315 ? -18.431 -57.667 25.491  1 41.85 ? 315 ILE Z O     1 
ATOM   9173  C  CB    . ILE F 1 315 ? -16.91  -60.043 26.157  1 40.68 ? 315 ILE Z CB    1 
ATOM   9174  C  CG1   . ILE F 1 315 ? -15.681 -60.731 26.777  1 41.35 ? 315 ILE Z CG1   1 
ATOM   9175  C  CG2   . ILE F 1 315 ? -17.929 -61.045 25.621  1 41.16 ? 315 ILE Z CG2   1 
ATOM   9176  C  CD1   . ILE F 1 315 ? -14.948 -61.675 25.9    1 42.78 ? 315 ILE Z CD1   1 
ATOM   9177  N  N     . ARG F 1 316 ? -17.937 -58.037 23.323  1 42.22 ? 316 ARG Z N     1 
ATOM   9178  C  CA    . ARG F 1 316 ? -19.057 -57.253 22.806  1 43.2  ? 316 ARG Z CA    1 
ATOM   9179  C  C     . ARG F 1 316 ? -20.393 -57.874 23.204  1 43.7  ? 316 ARG Z C     1 
ATOM   9180  O  O     . ARG F 1 316 ? -20.464 -59.086 23.403  1 43.71 ? 316 ARG Z O     1 
ATOM   9181  C  CB    . ARG F 1 316 ? -18.958 -57.104 21.279  1 45.09 ? 316 ARG Z CB    1 
ATOM   9182  C  CG    . ARG F 1 316 ? -17.684 -56.397 20.814  1 48.53 ? 316 ARG Z CG    1 
ATOM   9183  C  CD    . ARG F 1 316 ? -17.782 -55.901 19.382  1 51.49 ? 316 ARG Z CD    1 
ATOM   9184  N  NE    . ARG F 1 316 ? -17.924 -56.991 18.413  1 54.28 ? 316 ARG Z NE    1 
ATOM   9185  C  CZ    . ARG F 1 316 ? -17.174 -57.13  17.323  1 56.57 ? 316 ARG Z CZ    1 
ATOM   9186  N  NH1   . ARG F 1 316 ? -16.208 -56.258 17.056  1 55.98 ? 316 ARG Z NH1   1 
ATOM   9187  N  NH2   . ARG F 1 316 ? -17.384 -58.14  16.49   1 56.86 ? 316 ARG Z NH2   1 
ATOM   9188  N  N     . LYS F 1 317 ? -21.452 -57.056 23.33   1 43.98 ? 317 LYS Z N     1 
ATOM   9189  C  CA    . LYS F 1 317 ? -22.767 -57.57  23.73   1 44.79 ? 317 LYS Z CA    1 
ATOM   9190  C  C     . LYS F 1 317 ? -23.282 -58.69  22.816  1 45.59 ? 317 LYS Z C     1 
ATOM   9191  O  O     . LYS F 1 317 ? -23.98  -59.594 23.282  1 45.81 ? 317 LYS Z O     1 
ATOM   9192  C  CB    . LYS F 1 317 ? -23.8   -56.441 23.87   1 46.33 ? 317 LYS Z CB    1 
ATOM   9193  C  CG    . LYS F 1 317 ? -23.988 -55.604 22.619  1 50.02 ? 317 LYS Z CG    1 
ATOM   9194  C  CD    . LYS F 1 317 ? -24.97  -54.474 22.865  1 54.26 ? 317 LYS Z CD    1 
ATOM   9195  C  CE    . LYS F 1 317 ? -25     -53.499 21.713  1 57.86 ? 317 LYS Z CE    1 
ATOM   9196  N  NZ    . LYS F 1 317 ? -23.684 -52.834 21.513  1 60.03 ? 317 LYS Z NZ    1 
ATOM   9197  N  N     . GLU F 1 318 ? -22.875 -58.659 21.533  1 45.68 ? 318 GLU Z N     1 
ATOM   9198  C  CA    . GLU F 1 318 ? -23.236 -59.651 20.526  1 46.26 ? 318 GLU Z CA    1 
ATOM   9199  C  C     . GLU F 1 318 ? -22.629 -61.04  20.811  1 46.59 ? 318 GLU Z C     1 
ATOM   9200  O  O     . GLU F 1 318 ? -23.146 -62.041 20.321  1 46.91 ? 318 GLU Z O     1 
ATOM   9201  C  CB    . GLU F 1 318 ? -22.833 -59.159 19.126  1 48.74 ? 318 GLU Z CB    1 
ATOM   9202  C  CG    . GLU F 1 318 ? -23.605 -57.94  18.644  1 53.53 ? 318 GLU Z CG    1 
ATOM   9203  C  CD    . GLU F 1 318 ? -23.118 -56.594 19.147  1 59.34 ? 318 GLU Z CD    1 
ATOM   9204  O  OE1   . GLU F 1 318 ? -21.961 -56.515 19.619  1 60.46 ? 318 GLU Z OE1   1 
ATOM   9205  O  OE2   . GLU F 1 318 ? -23.895 -55.615 19.07   1 61.37 ? 318 GLU Z OE2   1 
ATOM   9206  N  N     . SER F 1 319 ? -21.539 -61.102 21.598  1 46.29 ? 319 SER Z N     1 
ATOM   9207  C  CA    . SER F 1 319 ? -20.881 -62.357 21.973  1 46.37 ? 319 SER Z CA    1 
ATOM   9208  C  C     . SER F 1 319 ? -20.986 -62.677 23.468  1 46.37 ? 319 SER Z C     1 
ATOM   9209  O  O     . SER F 1 319 ? -20.519 -63.739 23.872  1 46.43 ? 319 SER Z O     1 
ATOM   9210  C  CB    . SER F 1 319 ? -19.404 -62.322 21.596  1 47.56 ? 319 SER Z CB    1 
ATOM   9211  O  OG    . SER F 1 319 ? -19.213 -62.158 20.202  1 49.75 ? 319 SER Z OG    1 
ATOM   9212  N  N     . ARG F 1 320 ? -21.545 -61.76  24.29   1 46.17 ? 320 ARG Z N     1 
ATOM   9213  C  CA    . ARG F 1 320 ? -21.668 -61.919 25.742  1 46.37 ? 320 ARG Z CA    1 
ATOM   9214  C  C     . ARG F 1 320 ? -22.435 -63.172 26.136  1 46.9  ? 320 ARG Z C     1 
ATOM   9215  O  O     . ARG F 1 320 ? -21.985 -63.892 27.019  1 47.15 ? 320 ARG Z O     1 
ATOM   9216  C  CB    . ARG F 1 320 ? -22.289 -60.662 26.383  1 47.27 ? 320 ARG Z CB    1 
ATOM   9217  C  CG    . ARG F 1 320 ? -22.594 -60.776 27.882  1 49.4  ? 320 ARG Z CG    1 
ATOM   9218  C  CD    . ARG F 1 320 ? -21.472 -60.228 28.735  1 51.31 ? 320 ARG Z CD    1 
ATOM   9219  N  NE    . ARG F 1 320 ? -21.923 -59.595 29.967  1 53.08 ? 320 ARG Z NE    1 
ATOM   9220  C  CZ    . ARG F 1 320 ? -22.238 -58.31  30.1    1 54.89 ? 320 ARG Z CZ    1 
ATOM   9221  N  NH1   . ARG F 1 320 ? -22.281 -57.528 29.049  1 54.74 ? 320 ARG Z NH1   1 
ATOM   9222  N  NH2   . ARG F 1 320 ? -22.642 -57.842 31.274  1 54.44 ? 320 ARG Z NH2   1 
ATOM   9223  N  N     . ASN F 1 321 ? -23.566 -63.46  25.475  1 46.95 ? 321 ASN Z N     1 
ATOM   9224  C  CA    . ASN F 1 321 ? -24.363 -64.646 25.796  1 47.46 ? 321 ASN Z CA    1 
ATOM   9225  C  C     . ASN F 1 321 ? -23.55  -65.939 25.661  1 48.04 ? 321 ASN Z C     1 
ATOM   9226  O  O     . ASN F 1 321 ? -23.544 -66.757 26.576  1 48.09 ? 321 ASN Z O     1 
ATOM   9227  C  CB    . ASN F 1 321 ? -25.625 -64.698 24.936  1 48.34 ? 321 ASN Z CB    1 
ATOM   9228  C  CG    . ASN F 1 321 ? -26.898 -64.76  25.737  1 51.15 ? 321 ASN Z CG    1 
ATOM   9229  O  OD1   . ASN F 1 321 ? -27.453 -63.738 26.144  1 51.94 ? 321 ASN Z OD1   1 
ATOM   9230  N  ND2   . ASN F 1 321 ? -27.391 -65.967 25.978  1 51.98 ? 321 ASN Z ND2   1 
ATOM   9231  N  N     . ASP F 1 322 ? -22.816 -66.088 24.552  1 48.37 ? 322 ASP Z N     1 
ATOM   9232  C  CA    . ASP F 1 322 ? -22     -67.275 24.32   1 49.2  ? 322 ASP Z CA    1 
ATOM   9233  C  C     . ASP F 1 322 ? -20.803 -67.358 25.266  1 49.22 ? 322 ASP Z C     1 
ATOM   9234  O  O     . ASP F 1 322 ? -20.468 -68.452 25.718  1 49.42 ? 322 ASP Z O     1 
ATOM   9235  C  CB    . ASP F 1 322 ? -21.546 -67.34  22.861  1 51.49 ? 322 ASP Z CB    1 
ATOM   9236  C  CG    . ASP F 1 322 ? -22.643 -67.71  21.89   1 57.04 ? 322 ASP Z CG    1 
ATOM   9237  O  OD1   . ASP F 1 322 ? -23.557 -68.455 22.289  1 57.74 ? 322 ASP Z OD1   1 
ATOM   9238  O  OD2   . ASP F 1 322 ? -22.578 -67.264 20.722  1 59.96 ? 322 ASP Z OD2   1 
ATOM   9239  N  N     . PHE F 1 323 ? -20.177 -66.207 25.577  1 48.78 ? 323 PHE Z N     1 
ATOM   9240  C  CA    . PHE F 1 323 ? -19.056 -66.159 26.512  1 48.95 ? 323 PHE Z CA    1 
ATOM   9241  C  C     . PHE F 1 323 ? -19.534 -66.616 27.901  1 49.36 ? 323 PHE Z C     1 
ATOM   9242  O  O     . PHE F 1 323 ? -18.926 -67.514 28.482  1 49.7  ? 323 PHE Z O     1 
ATOM   9243  C  CB    . PHE F 1 323 ? -18.439 -64.747 26.564  1 48.69 ? 323 PHE Z CB    1 
ATOM   9244  C  CG    . PHE F 1 323 ? -17.525 -64.478 27.743  1 49.19 ? 323 PHE Z CG    1 
ATOM   9245  C  CD1   . PHE F 1 323 ? -16.242 -64.99  27.776  1 49.85 ? 323 PHE Z CD1   1 
ATOM   9246  C  CD2   . PHE F 1 323 ? -17.95  -63.701 28.811  1 49.88 ? 323 PHE Z CD2   1 
ATOM   9247  C  CE1   . PHE F 1 323 ? -15.405 -64.739 28.858  1 50.42 ? 323 PHE Z CE1   1 
ATOM   9248  C  CE2   . PHE F 1 323 ? -17.11  -63.45  29.887  1 50.45 ? 323 PHE Z CE2   1 
ATOM   9249  C  CZ    . PHE F 1 323 ? -15.845 -63.97  29.905  1 50.18 ? 323 PHE Z CZ    1 
ATOM   9250  N  N     . ILE F 1 324 ? -20.657 -66.05  28.392  1 49.09 ? 324 ILE Z N     1 
ATOM   9251  C  CA    . ILE F 1 324 ? -21.235 -66.402 29.69   1 49.13 ? 324 ILE Z CA    1 
ATOM   9252  C  C     . ILE F 1 324 ? -21.595 -67.886 29.757  1 49.16 ? 324 ILE Z C     1 
ATOM   9253  O  O     . ILE F 1 324 ? -21.279 -68.531 30.754  1 49.27 ? 324 ILE Z O     1 
ATOM   9254  C  CB    . ILE F 1 324 ? -22.419 -65.468 30.066  1 49.6  ? 324 ILE Z CB    1 
ATOM   9255  C  CG1   . ILE F 1 324 ? -21.955 -64.005 30.232  1 50.56 ? 324 ILE Z CG1   1 
ATOM   9256  C  CG2   . ILE F 1 324 ? -23.145 -65.952 31.314  1 50.05 ? 324 ILE Z CG2   1 
ATOM   9257  C  CD1   . ILE F 1 324 ? -20.829 -63.796 31.209  1 51.84 ? 324 ILE Z CD1   1 
ATOM   9258  N  N     . ASN F 1 325 ? -22.168 -68.45  28.674  1 48.9  ? 325 ASN Z N     1 
ATOM   9259  C  CA    . ASN F 1 325 ? -22.51  -69.876 28.61   1 48.98 ? 325 ASN Z CA    1 
ATOM   9260  C  C     . ASN F 1 325 ? -21.262 -70.744 28.801  1 48.74 ? 325 ASN Z C     1 
ATOM   9261  O  O     . ASN F 1 325 ? -21.296 -71.726 29.544  1 48.66 ? 325 ASN Z O     1 
ATOM   9262  C  CB    . ASN F 1 325 ? -23.174 -70.219 27.27   1 50.07 ? 325 ASN Z CB    1 
ATOM   9263  C  CG    . ASN F 1 325 ? -24.641 -69.895 27.194  1 52.93 ? 325 ASN Z CG    1 
ATOM   9264  O  OD1   . ASN F 1 325 ? -25.295 -69.61  28.201  1 53.84 ? 325 ASN Z OD1   1 
ATOM   9265  N  ND2   . ASN F 1 325 ? -25.189 -69.917 25.992  1 53.54 ? 325 ASN Z ND2   1 
ATOM   9266  N  N     . ASP F 1 326 ? -20.155 -70.361 28.146  1 48.48 ? 326 ASP Z N     1 
ATOM   9267  C  CA    . ASP F 1 326 ? -18.894 -71.087 28.237  1 48.69 ? 326 ASP Z CA    1 
ATOM   9268  C  C     . ASP F 1 326 ? -18.277 -70.994 29.624  1 48.86 ? 326 ASP Z C     1 
ATOM   9269  O  O     . ASP F 1 326 ? -17.762 -71.992 30.128  1 48.96 ? 326 ASP Z O     1 
ATOM   9270  C  CB    . ASP F 1 326 ? -17.908 -70.616 27.155  1 50.03 ? 326 ASP Z CB    1 
ATOM   9271  C  CG    . ASP F 1 326 ? -18.106 -71.268 25.799  1 53.48 ? 326 ASP Z CG    1 
ATOM   9272  O  OD1   . ASP F 1 326 ? -18.865 -72.262 25.717  1 54.12 ? 326 ASP Z OD1   1 
ATOM   9273  O  OD2   . ASP F 1 326 ? -17.494 -70.801 24.828  1 54.93 ? 326 ASP Z OD2   1 
ATOM   9274  N  N     . VAL F 1 327 ? -18.35  -69.814 30.256  1 48.73 ? 327 VAL Z N     1 
ATOM   9275  C  CA    . VAL F 1 327 ? -17.828 -69.652 31.61   1 49.11 ? 327 VAL Z CA    1 
ATOM   9276  C  C     . VAL F 1 327 ? -18.65  -70.496 32.587  1 49.48 ? 327 VAL Z C     1 
ATOM   9277  O  O     . VAL F 1 327 ? -18.076 -71.174 33.438  1 49.7  ? 327 VAL Z O     1 
ATOM   9278  C  CB    . VAL F 1 327 ? -17.752 -68.17  32.033  1 49.78 ? 327 VAL Z CB    1 
ATOM   9279  C  CG1   . VAL F 1 327 ? -17.308 -68.037 33.484  1 50.39 ? 327 VAL Z CG1   1 
ATOM   9280  C  CG2   . VAL F 1 327 ? -16.808 -67.402 31.123  1 50.29 ? 327 VAL Z CG2   1 
ATOM   9281  N  N     . CYS F 1 328 ? -19.986 -70.519 32.41   1 49.49 ? 328 CYS Z N     1 
ATOM   9282  C  CA    . CYS F 1 328 ? -20.901 -71.301 33.244  1 49.96 ? 328 CYS Z CA    1 
ATOM   9283  C  C     . CYS F 1 328 ? -20.633 -72.795 33.126  1 50.07 ? 328 CYS Z C     1 
ATOM   9284  O  O     . CYS F 1 328 ? -20.693 -73.509 34.12   1 50.03 ? 328 CYS Z O     1 
ATOM   9285  C  CB    . CYS F 1 328 ? -22.355 -70.97  32.919  1 50.78 ? 328 CYS Z CB    1 
ATOM   9286  S  SG    . CYS F 1 328 ? -22.878 -69.32  33.451  1 54.19 ? 328 CYS Z SG    1 
ATOM   9287  N  N     . LYS F 1 329 ? -20.327 -73.261 31.918  1 50.09 ? 329 LYS Z N     1 
ATOM   9288  C  CA    . LYS F 1 329 ? -20.024 -74.666 31.684  1 50.79 ? 329 LYS Z CA    1 
ATOM   9289  C  C     . LYS F 1 329 ? -18.712 -75.044 32.391  1 51.56 ? 329 LYS Z C     1 
ATOM   9290  O  O     . LYS F 1 329 ? -18.632 -76.092 33.036  1 51.87 ? 329 LYS Z O     1 
ATOM   9291  C  CB    . LYS F 1 329 ? -19.912 -74.944 30.167  1 52.09 ? 329 LYS Z CB    1 
ATOM   9292  C  CG    . LYS F 1 329 ? -20.634 -76.198 29.695  1 54.83 ? 329 LYS Z CG    1 
ATOM   9293  C  CD    . LYS F 1 329 ? -22.132 -75.965 29.578  1 58.19 ? 329 LYS Z CD    1 
ATOM   9294  C  CE    . LYS F 1 329 ? -22.879 -77.239 29.257  1 61.06 ? 329 LYS Z CE    1 
ATOM   9295  N  NZ    . LYS F 1 329 ? -24.354 -77.051 29.302  1 62.84 ? 329 LYS Z NZ    1 
ATOM   9296  N  N     . LEU F 1 330 ? -17.694 -74.178 32.285  1 51.66 ? 330 LEU Z N     1 
ATOM   9297  C  CA    . LEU F 1 330 ? -16.382 -74.426 32.877  1 52.2  ? 330 LEU Z CA    1 
ATOM   9298  C  C     . LEU F 1 330 ? -16.421 -74.5   34.399  1 52.88 ? 330 LEU Z C     1 
ATOM   9299  O  O     . LEU F 1 330 ? -15.808 -75.389 34.989  1 52.8  ? 330 LEU Z O     1 
ATOM   9300  C  CB    . LEU F 1 330 ? -15.379 -73.345 32.424  1 52.17 ? 330 LEU Z CB    1 
ATOM   9301  C  CG    . LEU F 1 330 ? -13.962 -73.467 32.989  1 53.36 ? 330 LEU Z CG    1 
ATOM   9302  C  CD1   . LEU F 1 330 ? -13.303 -74.757 32.547  1 53.86 ? 330 LEU Z CD1   1 
ATOM   9303  C  CD2   . LEU F 1 330 ? -13.116 -72.284 32.6    1 53.86 ? 330 LEU Z CD2   1 
ATOM   9304  N  N     . TYR F 1 331 ? -17.136 -73.57  35.031  1 53.38 ? 331 TYR Z N     1 
ATOM   9305  C  CA    . TYR F 1 331 ? -17.174 -73.489 36.481  1 54.41 ? 331 TYR Z CA    1 
ATOM   9306  C  C     . TYR F 1 331 ? -18.444 -74.04  37.136  1 55.9  ? 331 TYR Z C     1 
ATOM   9307  O  O     . TYR F 1 331 ? -18.629 -73.856 38.339  1 56.03 ? 331 TYR Z O     1 
ATOM   9308  C  CB    . TYR F 1 331 ? -16.924 -72.046 36.917  1 54.19 ? 331 TYR Z CB    1 
ATOM   9309  C  CG    . TYR F 1 331 ? -15.507 -71.593 36.65   1 54.63 ? 331 TYR Z CG    1 
ATOM   9310  C  CD1   . TYR F 1 331 ? -14.433 -72.193 37.288  1 55.46 ? 331 TYR Z CD1   1 
ATOM   9311  C  CD2   . TYR F 1 331 ? -15.241 -70.549 35.775  1 55.35 ? 331 TYR Z CD2   1 
ATOM   9312  C  CE1   . TYR F 1 331 ? -13.13  -71.766 37.068  1 56.29 ? 331 TYR Z CE1   1 
ATOM   9313  C  CE2   . TYR F 1 331 ? -13.942 -70.115 35.544  1 56.16 ? 331 TYR Z CE2   1 
ATOM   9314  C  CZ    . TYR F 1 331 ? -12.888 -70.726 36.194  1 57.06 ? 331 TYR Z CZ    1 
ATOM   9315  O  OH    . TYR F 1 331 ? -11.598 -70.312 35.969  1 58.51 ? 331 TYR Z OH    1 
ATOM   9316  N  N     . ASN F 1 332 ? -19.29  -74.739 36.367  1 56.84 ? 332 ASN Z N     1 
ATOM   9317  C  CA    . ASN F 1 332 ? -20.531 -75.342 36.856  1 58.16 ? 332 ASN Z CA    1 
ATOM   9318  C  C     . ASN F 1 332 ? -21.475 -74.326 37.508  1 59.2  ? 332 ASN Z C     1 
ATOM   9319  O  O     . ASN F 1 332 ? -22.005 -74.573 38.59   1 59.3  ? 332 ASN Z O     1 
ATOM   9320  C  CB    . ASN F 1 332 ? -20.256 -76.535 37.777  1 59.47 ? 332 ASN Z CB    1 
ATOM   9321  C  CG    . ASN F 1 332 ? -21.338 -77.585 37.742  1 62.91 ? 332 ASN Z CG    1 
ATOM   9322  O  OD1   . ASN F 1 332 ? -21.947 -77.857 36.699  1 64.03 ? 332 ASN Z OD1   1 
ATOM   9323  N  ND2   . ASN F 1 332 ? -21.598 -78.205 38.885  1 63.69 ? 332 ASN Z ND2   1 
ATOM   9324  N  N     . ILE F 1 333 ? -21.679 -73.184 36.849  1 59.84 ? 333 ILE Z N     1 
ATOM   9325  C  CA    . ILE F 1 333 ? -22.594 -72.168 37.35   1 60.98 ? 333 ILE Z CA    1 
ATOM   9326  C  C     . ILE F 1 333 ? -23.985 -72.517 36.831  1 62.32 ? 333 ILE Z C     1 
ATOM   9327  O  O     . ILE F 1 333 ? -24.201 -72.536 35.62   1 62.44 ? 333 ILE Z O     1 
ATOM   9328  C  CB    . ILE F 1 333 ? -22.15  -70.753 36.914  1 61.35 ? 333 ILE Z CB    1 
ATOM   9329  C  CG1   . ILE F 1 333 ? -20.704 -70.475 37.355  1 62.08 ? 333 ILE Z CG1   1 
ATOM   9330  C  CG2   . ILE F 1 333 ? -23.113 -69.695 37.453  1 61.91 ? 333 ILE Z CG2   1 
ATOM   9331  C  CD1   . ILE F 1 333 ? -20.13  -69.206 36.807  1 63.27 ? 333 ILE Z CD1   1 
ATOM   9332  N  N     . ASN F 1 334 ? -24.917 -72.841 37.736  1 63.2  ? 334 ASN Z N     1 
ATOM   9333  C  CA    . ASN F 1 334 ? -26.268 -73.232 37.335  1 64.57 ? 334 ASN Z CA    1 
ATOM   9334  C  C     . ASN F 1 334 ? -27.386 -72.328 37.87   1 65.66 ? 334 ASN Z C     1 
ATOM   9335  O  O     . ASN F 1 334 ? -28.542 -72.52  37.496  1 65.94 ? 334 ASN Z O     1 
ATOM   9336  C  CB    . ASN F 1 334 ? -26.541 -74.688 37.721  1 65.87 ? 334 ASN Z CB    1 
ATOM   9337  C  CG    . ASN F 1 334 ? -25.832 -75.696 36.851  1 69.41 ? 334 ASN Z CG    1 
ATOM   9338  O  OD1   . ASN F 1 334 ? -24.994 -76.476 37.319  1 70.66 ? 334 ASN Z OD1   1 
ATOM   9339  N  ND2   . ASN F 1 334 ? -26.156 -75.706 35.561  1 70.11 ? 334 ASN Z ND2   1 
ATOM   9340  N  N     . ASP F 1 335 ? -27.062 -71.365 38.743  1 66.09 ? 335 ASP Z N     1 
ATOM   9341  C  CA    . ASP F 1 335 ? -28.075 -70.482 39.311  1 67.02 ? 335 ASP Z CA    1 
ATOM   9342  C  C     . ASP F 1 335 ? -28.661 -69.531 38.269  1 67.82 ? 335 ASP Z C     1 
ATOM   9343  O  O     . ASP F 1 335 ? -27.938 -68.709 37.712  1 67.97 ? 335 ASP Z O     1 
ATOM   9344  C  CB    . ASP F 1 335 ? -27.514 -69.698 40.504  1 68.5  ? 335 ASP Z CB    1 
ATOM   9345  C  CG    . ASP F 1 335 ? -28.596 -69.043 41.333  1 72.43 ? 335 ASP Z CG    1 
ATOM   9346  O  OD1   . ASP F 1 335 ? -29.327 -69.772 42.035  1 72.82 ? 335 ASP Z OD1   1 
ATOM   9347  O  OD2   . ASP F 1 335 ? -28.718 -67.805 41.273  1 74.63 ? 335 ASP Z OD2   1 
ATOM   9348  N  N     . MET F 1 336 ? -29.974 -69.649 38.014  1 68.13 ? 336 MET Z N     1 
ATOM   9349  C  CA    . MET F 1 336 ? -30.71  -68.831 37.046  1 68.85 ? 336 MET Z CA    1 
ATOM   9350  C  C     . MET F 1 336 ? -30.562 -67.32  37.289  1 68.25 ? 336 MET Z C     1 
ATOM   9351  O  O     . MET F 1 336 ? -30.35  -66.575 36.334  1 68.35 ? 336 MET Z O     1 
ATOM   9352  C  CB    . MET F 1 336 ? -32.203 -69.233 37.041  1 70.62 ? 336 MET Z CB    1 
ATOM   9353  C  CG    . MET F 1 336 ? -33.041 -68.503 35.995  1 74.47 ? 336 MET Z CG    1 
ATOM   9354  S  SD    . MET F 1 336 ? -34.839 -68.694 36.221  1 82.49 ? 336 MET Z SD    1 
ATOM   9355  C  CE    . MET F 1 336 ? -35.426 -67.95  34.71   1 81.2  ? 336 MET Z CE    1 
ATOM   9356  N  N     . LYS F 1 337 ? -30.669 -66.875 38.554  1 67.48 ? 337 LYS Z N     1 
ATOM   9357  C  CA    . LYS F 1 337 ? -30.56  -65.459 38.904  1 67.28 ? 337 LYS Z CA    1 
ATOM   9358  C  C     . LYS F 1 337 ? -29.189 -64.895 38.545  1 66.85 ? 337 LYS Z C     1 
ATOM   9359  O  O     . LYS F 1 337 ? -29.099 -63.814 37.973  1 66.8  ? 337 LYS Z O     1 
ATOM   9360  C  CB    . LYS F 1 337 ? -30.851 -65.234 40.399  1 69.05 ? 337 LYS Z CB    1 
ATOM   9361  C  CG    . LYS F 1 337 ? -32.221 -65.72  40.849  1 73.01 ? 337 LYS Z CG    1 
ATOM   9362  C  CD    . LYS F 1 337 ? -32.601 -65.145 42.208  1 77.25 ? 337 LYS Z CD    1 
ATOM   9363  C  CE    . LYS F 1 337 ? -31.717 -65.636 43.329  1 81    ? 337 LYS Z CE    1 
ATOM   9364  N  NZ    . LYS F 1 337 ? -32.074 -67.017 43.754  1 83.29 ? 337 LYS Z NZ    1 
ATOM   9365  N  N     . ILE F 1 338 ? -28.127 -65.639 38.865  1 66.43 ? 338 ILE Z N     1 
ATOM   9366  C  CA    . ILE F 1 338 ? -26.752 -65.242 38.594  1 66.51 ? 338 ILE Z CA    1 
ATOM   9367  C  C     . ILE F 1 338 ? -26.491 -65.137 37.095  1 66.5  ? 338 ILE Z C     1 
ATOM   9368  O  O     . ILE F 1 338 ? -25.905 -64.154 36.646  1 66.65 ? 338 ILE Z O     1 
ATOM   9369  C  CB    . ILE F 1 338 ? -25.786 -66.233 39.293  1 67.08 ? 338 ILE Z CB    1 
ATOM   9370  C  CG1   . ILE F 1 338 ? -25.844 -66.068 40.823  1 68.11 ? 338 ILE Z CG1   1 
ATOM   9371  C  CG2   . ILE F 1 338 ? -24.366 -66.088 38.78   1 67.48 ? 338 ILE Z CG2   1 
ATOM   9372  C  CD1   . ILE F 1 338 ? -24.988 -67.066 41.622  1 69.39 ? 338 ILE Z CD1   1 
ATOM   9373  N  N     . ILE F 1 339 ? -26.939 -66.142 36.325  1 66.23 ? 339 ILE Z N     1 
ATOM   9374  C  CA    . ILE F 1 339 ? -26.774 -66.189 34.873  1 66.4  ? 339 ILE Z CA    1 
ATOM   9375  C  C     . ILE F 1 339 ? -27.476 -65.009 34.195  1 66.28 ? 339 ILE Z C     1 
ATOM   9376  O  O     . ILE F 1 339 ? -26.912 -64.402 33.287  1 66.27 ? 339 ILE Z O     1 
ATOM   9377  C  CB    . ILE F 1 339 ? -27.258 -67.556 34.332  1 67.03 ? 339 ILE Z CB    1 
ATOM   9378  C  CG1   . ILE F 1 339 ? -26.399 -68.7   34.893  1 68.11 ? 339 ILE Z CG1   1 
ATOM   9379  C  CG2   . ILE F 1 339 ? -27.256 -67.58  32.812  1 67.58 ? 339 ILE Z CG2   1 
ATOM   9380  C  CD1   . ILE F 1 339 ? -26.935 -70.09  34.591  1 69.55 ? 339 ILE Z CD1   1 
ATOM   9381  N  N     . LYS F 1 340 ? -28.673 -64.644 34.676  1 66.09 ? 340 LYS Z N     1 
ATOM   9382  C  CA    . LYS F 1 340 ? -29.427 -63.515 34.129  1 66.37 ? 340 LYS Z CA    1 
ATOM   9383  C  C     . LYS F 1 340 ? -28.688 -62.195 34.362  1 66.17 ? 340 LYS Z C     1 
ATOM   9384  O  O     . LYS F 1 340 ? -28.69  -61.33  33.487  1 66.36 ? 340 LYS Z O     1 
ATOM   9385  C  CB    . LYS F 1 340 ? -30.836 -63.455 34.738  1 68.5  ? 340 LYS Z CB    1 
ATOM   9386  C  CG    . LYS F 1 340 ? -31.857 -62.752 33.851  1 72.83 ? 340 LYS Z CG    1 
ATOM   9387  C  CD    . LYS F 1 340 ? -33.263 -62.828 34.449  1 77.43 ? 340 LYS Z CD    1 
ATOM   9388  C  CE    . LYS F 1 340 ? -34.345 -62.486 33.45   1 81.41 ? 340 LYS Z CE    1 
ATOM   9389  N  NZ    . LYS F 1 340 ? -34.465 -63.505 32.368  1 83.74 ? 340 LYS Z NZ    1 
ATOM   9390  N  N     . GLU F 1 341 ? -28.038 -62.05  35.528  1 65.6  ? 341 GLU Z N     1 
ATOM   9391  C  CA    . GLU F 1 341 ? -27.264 -60.854 35.851  1 65.39 ? 341 GLU Z CA    1 
ATOM   9392  C  C     . GLU F 1 341 ? -26.038 -60.755 34.945  1 64.79 ? 341 GLU Z C     1 
ATOM   9393  O  O     . GLU F 1 341 ? -25.721 -59.676 34.446  1 64.92 ? 341 GLU Z O     1 
ATOM   9394  C  CB    . GLU F 1 341 ? -26.836 -60.871 37.323  1 67.67 ? 341 GLU Z CB    1 
ATOM   9395  C  CG    . GLU F 1 341 ? -27.987 -60.666 38.29   1 72.58 ? 341 GLU Z CG    1 
ATOM   9396  C  CD    . GLU F 1 341 ? -28.713 -59.347 38.135  1 78.81 ? 341 GLU Z CD    1 
ATOM   9397  O  OE1   . GLU F 1 341 ? -28.211 -58.328 38.663  1 80.12 ? 341 GLU Z OE1   1 
ATOM   9398  O  OE2   . GLU F 1 341 ? -29.789 -59.331 37.496  1 80.85 ? 341 GLU Z OE2   1 
ATOM   9399  N  N     . LEU F 1 342 ? -25.369 -61.889 34.708  1 63.98 ? 342 LEU Z N     1 
ATOM   9400  C  CA    . LEU F 1 342 ? -24.195 -61.965 33.846  1 63.67 ? 342 LEU Z CA    1 
ATOM   9401  C  C     . LEU F 1 342 ? -24.539 -61.676 32.385  1 63.18 ? 342 LEU Z C     1 
ATOM   9402  O  O     . LEU F 1 342 ? -23.705 -61.145 31.662  1 63.44 ? 342 LEU Z O     1 
ATOM   9403  C  CB    . LEU F 1 342 ? -23.573 -63.363 33.934  1 63.85 ? 342 LEU Z CB    1 
ATOM   9404  C  CG    . LEU F 1 342 ? -22.876 -63.722 35.231  1 65.25 ? 342 LEU Z CG    1 
ATOM   9405  C  CD1   . LEU F 1 342 ? -22.472 -65.177 35.227  1 65.9  ? 342 LEU Z CD1   1 
ATOM   9406  C  CD2   . LEU F 1 342 ? -21.666 -62.855 35.451  1 65.8  ? 342 LEU Z CD2   1 
ATOM   9407  N  N     . LYS F 1 343 ? -25.753 -62.031 31.943  1 62.3  ? 343 LYS Z N     1 
ATOM   9408  C  CA    . LYS F 1 343 ? -26.157 -61.843 30.551  1 61.82 ? 343 LYS Z CA    1 
ATOM   9409  C  C     . LYS F 1 343 ? -26.846 -60.498 30.239  1 60.83 ? 343 LYS Z C     1 
ATOM   9410  O  O     . LYS F 1 343 ? -27.706 -60.45  29.354  1 60.96 ? 343 LYS Z O     1 
ATOM   9411  C  CB    . LYS F 1 343 ? -27.039 -63.011 30.096  1 63.68 ? 343 LYS Z CB    1 
ATOM   9412  C  CG    . LYS F 1 343 ? -26.294 -64.331 29.989  1 67.65 ? 343 LYS Z CG    1 
ATOM   9413  C  CD    . LYS F 1 343 ? -27.206 -65.404 29.433  1 72    ? 343 LYS Z CD    1 
ATOM   9414  C  CE    . LYS F 1 343 ? -26.576 -66.774 29.394  1 75.73 ? 343 LYS Z CE    1 
ATOM   9415  N  NZ    . LYS F 1 343 ? -25.276 -66.813 28.703  1 78.09 ? 343 LYS Z NZ    1 
ATOM   9416  N  N     . GLU F 1 344 ? -26.452 -59.412 30.919  1 59.65 ? 344 GLU Z N     1 
ATOM   9417  C  CA    . GLU F 1 344 ? -27.029 -58.094 30.64   1 59.07 ? 344 GLU Z CA    1 
ATOM   9418  C  C     . GLU F 1 344 ? -26.619 -57.652 29.216  1 58.12 ? 344 GLU Z C     1 
ATOM   9419  O  O     . GLU F 1 344 ? -25.487 -57.91  28.807  1 58.35 ? 344 GLU Z O     1 
ATOM   9420  C  CB    . GLU F 1 344 ? -26.555 -57.083 31.692  1 61.17 ? 344 GLU Z CB    1 
ATOM   9421  C  CG    . GLU F 1 344 ? -27.189 -55.714 31.549  1 65.76 ? 344 GLU Z CG    1 
ATOM   9422  C  CD    . GLU F 1 344 ? -27.091 -54.855 32.792  1 71.73 ? 344 GLU Z CD    1 
ATOM   9423  O  OE1   . GLU F 1 344 ? -27.119 -55.421 33.909  1 72.62 ? 344 GLU Z OE1   1 
ATOM   9424  O  OE2   . GLU F 1 344 ? -26.99  -53.615 32.652  1 73.93 ? 344 GLU Z OE2   1 
ATOM   9425  N  N     . ASP F 1 345 ? -27.539 -57.036 28.445  1 56.81 ? 345 ASP Z N     1 
ATOM   9426  C  CA    . ASP F 1 345 ? -27.237 -56.63  27.068  1 55.93 ? 345 ASP Z CA    1 
ATOM   9427  C  C     . ASP F 1 345 ? -26.379 -55.368 26.963  1 54.55 ? 345 ASP Z C     1 
ATOM   9428  O  O     . ASP F 1 345 ? -26.879 -54.296 26.632  1 54.72 ? 345 ASP Z O     1 
ATOM   9429  C  CB    . ASP F 1 345 ? -28.51  -56.489 26.22   1 57.73 ? 345 ASP Z CB    1 
ATOM   9430  C  CG    . ASP F 1 345 ? -28.231 -56.411 24.726  1 62.17 ? 345 ASP Z CG    1 
ATOM   9431  O  OD1   . ASP F 1 345 ? -27.38  -57.187 24.24   1 62.92 ? 345 ASP Z OD1   1 
ATOM   9432  O  OD2   . ASP F 1 345 ? -28.864 -55.572 24.045  1 64.15 ? 345 ASP Z OD2   1 
ATOM   9433  N  N     . ALA F 1 346 ? -25.076 -55.511 27.206  1 53.04 ? 346 ALA Z N     1 
ATOM   9434  C  CA    . ALA F 1 346 ? -24.107 -54.421 27.123  1 52.04 ? 346 ALA Z CA    1 
ATOM   9435  C  C     . ALA F 1 346 ? -22.699 -54.981 26.911  1 50.71 ? 346 ALA Z C     1 
ATOM   9436  O  O     . ALA F 1 346 ? -22.45  -56.144 27.215  1 50.64 ? 346 ALA Z O     1 
ATOM   9437  C  CB    . ALA F 1 346 ? -24.14  -53.597 28.401  1 52.15 ? 346 ALA Z CB    1 
ATOM   9438  N  N     . ASP F 1 347 ? -21.771 -54.164 26.391  1 49.53 ? 347 ASP Z N     1 
ATOM   9439  C  CA    . ASP F 1 347 ? -20.384 -54.599 26.214  1 48.7  ? 347 ASP Z CA    1 
ATOM   9440  C  C     . ASP F 1 347 ? -19.76  -54.85  27.596  1 47.05 ? 347 ASP Z C     1 
ATOM   9441  O  O     . ASP F 1 347 ? -20.078 -54.153 28.561  1 47.03 ? 347 ASP Z O     1 
ATOM   9442  C  CB    . ASP F 1 347 ? -19.564 -53.55  25.443  1 50.67 ? 347 ASP Z CB    1 
ATOM   9443  C  CG    . ASP F 1 347 ? -19.964 -53.376 23.993  1 55.53 ? 347 ASP Z CG    1 
ATOM   9444  O  OD1   . ASP F 1 347 ? -20.63  -54.281 23.448  1 56.3  ? 347 ASP Z OD1   1 
ATOM   9445  O  OD2   . ASP F 1 347 ? -19.604 -52.334 23.399  1 57.91 ? 347 ASP Z OD2   1 
ATOM   9446  N  N     . LEU F 1 348 ? -18.909 -55.863 27.698  1 45.53 ? 348 LEU Z N     1 
ATOM   9447  C  CA    . LEU F 1 348 ? -18.294 -56.222 28.965  1 44.63 ? 348 LEU Z CA    1 
ATOM   9448  C  C     . LEU F 1 348 ? -16.791 -56.148 28.869  1 43.27 ? 348 LEU Z C     1 
ATOM   9449  O  O     . LEU F 1 348 ? -16.223 -56.767 27.98   1 43.37 ? 348 LEU Z O     1 
ATOM   9450  C  CB    . LEU F 1 348 ? -18.698 -57.658 29.305  1 44.92 ? 348 LEU Z CB    1 
ATOM   9451  C  CG    . LEU F 1 348 ? -18.191 -58.18  30.622  1 46.53 ? 348 LEU Z CG    1 
ATOM   9452  C  CD1   . LEU F 1 348 ? -18.867 -57.467 31.761  1 47.3  ? 348 LEU Z CD1   1 
ATOM   9453  C  CD2   . LEU F 1 348 ? -18.364 -59.693 30.719  1 47.16 ? 348 LEU Z CD2   1 
ATOM   9454  N  N     . ILE F 1 349 ? -16.139 -55.413 29.773  1 41.74 ? 349 ILE Z N     1 
ATOM   9455  C  CA    . ILE F 1 349 ? -14.682 -55.349 29.773  1 40.72 ? 349 ILE Z CA    1 
ATOM   9456  C  C     . ILE F 1 349 ? -14.185 -56.432 30.714  1 39.6  ? 349 ILE Z C     1 
ATOM   9457  O  O     . ILE F 1 349 ? -14.613 -56.469 31.858  1 39.87 ? 349 ILE Z O     1 
ATOM   9458  C  CB    . ILE F 1 349 ? -14.163 -53.947 30.154  1 41.07 ? 349 ILE Z CB    1 
ATOM   9459  C  CG1   . ILE F 1 349 ? -14.54  -52.932 29.063  1 42.08 ? 349 ILE Z CG1   1 
ATOM   9460  C  CG2   . ILE F 1 349 ? -12.657 -53.975 30.394  1 41.4  ? 349 ILE Z CG2   1 
ATOM   9461  C  CD1   . ILE F 1 349 ? -14.164 -51.492 29.344  1 43.37 ? 349 ILE Z CD1   1 
ATOM   9462  N  N     . VAL F 1 350 ? -13.349 -57.355 30.229  1 38.17 ? 350 VAL Z N     1 
ATOM   9463  C  CA    . VAL F 1 350 ? -12.819 -58.424 31.074  1 37.25 ? 350 VAL Z CA    1 
ATOM   9464  C  C     . VAL F 1 350 ? -11.394 -58.081 31.453  1 36.33 ? 350 VAL Z C     1 
ATOM   9465  O  O     . VAL F 1 350 ? -10.587 -57.83  30.569  1 36.55 ? 350 VAL Z O     1 
ATOM   9466  C  CB    . VAL F 1 350 ? -12.885 -59.799 30.375  1 37.64 ? 350 VAL Z CB    1 
ATOM   9467  C  CG1   . VAL F 1 350 ? -12.172 -60.868 31.199  1 38.03 ? 350 VAL Z CG1   1 
ATOM   9468  C  CG2   . VAL F 1 350 ? -14.327 -60.197 30.101  1 38.06 ? 350 VAL Z CG2   1 
ATOM   9469  N  N     . CYS F 1 351 ? -11.083 -58.043 32.751  1 35.11 ? 351 CYS Z N     1 
ATOM   9470  C  CA    . CYS F 1 351 ? -9.738  -57.738 33.225  1 34.54 ? 351 CYS Z CA    1 
ATOM   9471  C  C     . CYS F 1 351 ? -9.215  -58.973 33.933  1 33.72 ? 351 CYS Z C     1 
ATOM   9472  O  O     . CYS F 1 351 ? -9.886  -59.474 34.819  1 34.15 ? 351 CYS Z O     1 
ATOM   9473  C  CB    . CYS F 1 351 ? -9.758  -56.525 34.155  1 35.23 ? 351 CYS Z CB    1 
ATOM   9474  S  SG    . CYS F 1 351 ? -8.121  -55.843 34.533  1 37.99 ? 351 CYS Z SG    1 
ATOM   9475  N  N     . MET F 1 352 ? -8.054  -59.488 33.538  1 32.5  ? 352 MET Z N     1 
ATOM   9476  C  CA    . MET F 1 352 ? -7.482  -60.669 34.171  1 31.8  ? 352 MET Z CA    1 
ATOM   9477  C  C     . MET F 1 352 ? -6.212  -60.262 34.888  1 31.02 ? 352 MET Z C     1 
ATOM   9478  O  O     . MET F 1 352 ? -5.317  -59.7   34.259  1 31.22 ? 352 MET Z O     1 
ATOM   9479  C  CB    . MET F 1 352 ? -7.204  -61.755 33.121  1 32.32 ? 352 MET Z CB    1 
ATOM   9480  C  CG    . MET F 1 352 ? -8.474  -62.294 32.469  1 33.43 ? 352 MET Z CG    1 
ATOM   9481  S  SD    . MET F 1 352 ? -8.264  -63.62  31.237  1 30.77 ? 352 MET Z SD    1 
ATOM   9482  C  CE    . MET F 1 352 ? -7.283  -64.758 32.123  1 26.74 ? 352 MET Z CE    1 
ATOM   9483  N  N     . LEU F 1 353 ? -6.15   -60.48  36.21   1 30.03 ? 353 LEU Z N     1 
ATOM   9484  C  CA    . LEU F 1 353 ? -4.989  -60.09  37.012  1 29.7  ? 353 LEU Z CA    1 
ATOM   9485  C  C     . LEU F 1 353 ? -4.624  -61.175 38.006  1 29.1  ? 353 LEU Z C     1 
ATOM   9486  O  O     . LEU F 1 353 ? -5.52   -61.794 38.57   1 29.04 ? 353 LEU Z O     1 
ATOM   9487  C  CB    . LEU F 1 353 ? -5.308  -58.822 37.816  1 29.96 ? 353 LEU Z CB    1 
ATOM   9488  C  CG    . LEU F 1 353 ? -5.614  -57.564 37.042  1 31.6  ? 353 LEU Z CG    1 
ATOM   9489  C  CD1   . LEU F 1 353 ? -6.265  -56.539 37.937  1 32.04 ? 353 LEU Z CD1   1 
ATOM   9490  C  CD2   . LEU F 1 353 ? -4.366  -57.009 36.403  1 32.51 ? 353 LEU Z CD2   1 
ATOM   9491  N  N     . LYS F 1 354 ? -3.323  -61.384 38.26   1 28.53 ? 354 LYS Z N     1 
ATOM   9492  C  CA    . LYS F 1 354 ? -2.906  -62.357 39.272  1 28.44 ? 354 LYS Z CA    1 
ATOM   9493  C  C     . LYS F 1 354 ? -3.303  -61.849 40.649  1 28.31 ? 354 LYS Z C     1 
ATOM   9494  O  O     . LYS F 1 354 ? -3.833  -62.594 41.455  1 28.04 ? 354 LYS Z O     1 
ATOM   9495  C  CB    . LYS F 1 354 ? -1.399  -62.638 39.212  1 29.85 ? 354 LYS Z CB    1 
ATOM   9496  C  CG    . LYS F 1 354 ? -0.978  -63.769 40.14   1 32.8  ? 354 LYS Z CG    1 
ATOM   9497  C  CD    . LYS F 1 354 ? 0.442   -64.214 39.875  1 36.07 ? 354 LYS Z CD    1 
ATOM   9498  C  CE    . LYS F 1 354 ? 0.802   -65.447 40.66   1 39.05 ? 354 LYS Z CE    1 
ATOM   9499  N  NZ    . LYS F 1 354 ? 1.462   -65.125 41.946  1 40.89 ? 354 LYS Z NZ    1 
ATOM   9500  N  N     . GLY F 1 355 ? -3.076  -60.57  40.893  1 28.48 ? 355 GLY Z N     1 
ATOM   9501  C  CA    . GLY F 1 355 ? -3.452  -59.921 42.134  1 29.2  ? 355 GLY Z CA    1 
ATOM   9502  C  C     . GLY F 1 355 ? -2.523  -60.152 43.3    1 29.89 ? 355 GLY Z C     1 
ATOM   9503  O  O     . GLY F 1 355 ? -2.261  -59.226 44.063  1 30.07 ? 355 GLY Z O     1 
ATOM   9504  N  N     . PHE F 1 356 ? -2.069  -61.397 43.501  1 30.17 ? 356 PHE Z N     1 
ATOM   9505  C  CA    . PHE F 1 356 ? -1.289  -61.737 44.69   1 30.81 ? 356 PHE Z CA    1 
ATOM   9506  C  C     . PHE F 1 356 ? -0.019  -62.528 44.411  1 32.1  ? 356 PHE Z C     1 
ATOM   9507  O  O     . PHE F 1 356 ? 0.002   -63.403 43.548  1 32.28 ? 356 PHE Z O     1 
ATOM   9508  C  CB    . PHE F 1 356 ? -2.19   -62.489 45.693  1 30.15 ? 356 PHE Z CB    1 
ATOM   9509  C  CG    . PHE F 1 356 ? -3.448  -61.728 46.032  1 30.23 ? 356 PHE Z CG    1 
ATOM   9510  C  CD1   . PHE F 1 356 ? -4.562  -61.791 45.21   1 30.76 ? 356 PHE Z CD1   1 
ATOM   9511  C  CD2   . PHE F 1 356 ? -3.479  -60.867 47.104  1 31.04 ? 356 PHE Z CD2   1 
ATOM   9512  C  CE1   . PHE F 1 356 ? -5.675  -61.01  45.464  1 31.55 ? 356 PHE Z CE1   1 
ATOM   9513  C  CE2   . PHE F 1 356 ? -4.613  -60.124 47.385  1 31.75 ? 356 PHE Z CE2   1 
ATOM   9514  C  CZ    . PHE F 1 356 ? -5.693  -60.182 46.551  1 31.45 ? 356 PHE Z CZ    1 
ATOM   9515  N  N     . LYS F 1 357 ? 1.041   -62.215 45.155  1 32.79 ? 357 LYS Z N     1 
ATOM   9516  C  CA    . LYS F 1 357 ? 2.341   -62.878 45.076  1 34.06 ? 357 LYS Z CA    1 
ATOM   9517  C  C     . LYS F 1 357 ? 2.295   -64.268 45.776  1 35.2  ? 357 LYS Z C     1 
ATOM   9518  O  O     . LYS F 1 357 ? 1.284   -64.586 46.408  1 35.57 ? 357 LYS Z O     1 
ATOM   9519  C  CB    . LYS F 1 357 ? 3.407   -61.94  45.678  1 36.02 ? 357 LYS Z CB    1 
ATOM   9520  C  CG    . LYS F 1 357 ? 3.948   -60.94  44.667  1 39.82 ? 357 LYS Z CG    1 
ATOM   9521  C  CD    . LYS F 1 357 ? 4.654   -59.788 45.341  1 43.96 ? 357 LYS Z CD    1 
ATOM   9522  C  CE    . LYS F 1 357 ? 3.66    -58.774 45.843  1 47.81 ? 357 LYS Z CE    1 
ATOM   9523  N  NZ    . LYS F 1 357 ? 4.316   -57.683 46.611  1 50.2  ? 357 LYS Z NZ    1 
ATOM   9524  N  N     . PRO F 1 358 ? 3.336   -65.128 45.671  1 35.69 ? 358 PRO Z N     1 
ATOM   9525  C  CA    . PRO F 1 358 ? 3.255   -66.46  46.302  1 35.95 ? 358 PRO Z CA    1 
ATOM   9526  C  C     . PRO F 1 358 ? 2.848   -66.483 47.772  1 36.5  ? 358 PRO Z C     1 
ATOM   9527  O  O     . PRO F 1 358 ? 2.139   -67.398 48.175  1 37.02 ? 358 PRO Z O     1 
ATOM   9528  C  CB    . PRO F 1 358 ? 4.656   -67.039 46.098  1 36.66 ? 358 PRO Z CB    1 
ATOM   9529  C  CG    . PRO F 1 358 ? 5.163   -66.365 44.878  1 37.14 ? 358 PRO Z CG    1 
ATOM   9530  C  CD    . PRO F 1 358 ? 4.601   -64.966 44.925  1 35.43 ? 358 PRO Z CD    1 
ATOM   9531  N  N     . ARG F 1 359 ? 3.265   -65.49  48.572  1 36.26 ? 359 ARG Z N     1 
ATOM   9532  C  CA    . ARG F 1 359 ? 2.901   -65.449 49.998  1 36.36 ? 359 ARG Z CA    1 
ATOM   9533  C  C     . ARG F 1 359 ? 1.52    -64.83  50.291  1 35.83 ? 359 ARG Z C     1 
ATOM   9534  O  O     . ARG F 1 359 ? 1.146   -64.697 51.46   1 36.08 ? 359 ARG Z O     1 
ATOM   9535  C  CB    . ARG F 1 359 ? 3.989   -64.737 50.824  1 38.12 ? 359 ARG Z CB    1 
ATOM   9536  C  CG    . ARG F 1 359 ? 5.363   -65.365 50.678  1 41.97 ? 359 ARG Z CG    1 
ATOM   9537  C  CD    . ARG F 1 359 ? 6.43    -64.318 50.429  1 45.9  ? 359 ARG Z CD    1 
ATOM   9538  N  NE    . ARG F 1 359 ? 6.914   -63.736 51.676  1 49.11 ? 359 ARG Z NE    1 
ATOM   9539  C  CZ    . ARG F 1 359 ? 7.996   -62.969 51.778  1 51.62 ? 359 ARG Z CZ    1 
ATOM   9540  N  NH1   . ARG F 1 359 ? 8.718   -62.678 50.7    1 51.16 ? 359 ARG Z NH1   1 
ATOM   9541  N  NH2   . ARG F 1 359 ? 8.365   -62.486 52.956  1 51.88 ? 359 ARG Z NH2   1 
ATOM   9542  N  N     . GLY F 1 360 ? 0.78    -64.464 49.25   1 34.96 ? 360 GLY Z N     1 
ATOM   9543  C  CA    . GLY F 1 360 ? -0.531  -63.853 49.403  1 34.93 ? 360 GLY Z CA    1 
ATOM   9544  C  C     . GLY F 1 360 ? -0.507  -62.339 49.502  1 34.77 ? 360 GLY Z C     1 
ATOM   9545  O  O     . GLY F 1 360 ? -1.56   -61.718 49.646  1 34.93 ? 360 GLY Z O     1 
ATOM   9546  N  N     . ASP F 1 361 ? 0.687   -61.724 49.452  1 34.32 ? 361 ASP Z N     1 
ATOM   9547  C  CA    . ASP F 1 361 ? 0.817   -60.271 49.51   1 34.27 ? 361 ASP Z CA    1 
ATOM   9548  C  C     . ASP F 1 361 ? 0.404   -59.679 48.166  1 33.7  ? 361 ASP Z C     1 
ATOM   9549  O  O     . ASP F 1 361 ? 0.808   -60.179 47.119  1 33.6  ? 361 ASP Z O     1 
ATOM   9550  C  CB    . ASP F 1 361 ? 2.229   -59.819 49.956  1 36.36 ? 361 ASP Z CB    1 
ATOM   9551  C  CG    . ASP F 1 361 ? 3.423   -60.492 49.29   1 42.11 ? 361 ASP Z CG    1 
ATOM   9552  O  OD1   . ASP F 1 361 ? 3.416   -61.737 49.165  1 43.13 ? 361 ASP Z OD1   1 
ATOM   9553  O  OD2   . ASP F 1 361 ? 4.387   -59.778 48.941  1 44.83 ? 361 ASP Z OD2   1 
ATOM   9554  N  N     . ASP F 1 362 ? -0.454  -58.658 48.19   1 33.11 ? 362 ASP Z N     1 
ATOM   9555  C  CA    . ASP F 1 362 ? -0.992  -58.062 46.97   1 32.8  ? 362 ASP Z CA    1 
ATOM   9556  C  C     . ASP F 1 362 ? 0.029   -57.387 46.066  1 31.53 ? 362 ASP Z C     1 
ATOM   9557  O  O     . ASP F 1 362 ? 0.995   -56.801 46.54   1 31.66 ? 362 ASP Z O     1 
ATOM   9558  C  CB    . ASP F 1 362 ? -2.119  -57.086 47.308  1 35.1  ? 362 ASP Z CB    1 
ATOM   9559  C  CG    . ASP F 1 362 ? -1.69   -55.949 48.204  1 40.11 ? 362 ASP Z CG    1 
ATOM   9560  O  OD1   . ASP F 1 362 ? -1.55   -56.178 49.432  1 40.79 ? 362 ASP Z OD1   1 
ATOM   9561  O  OD2   . ASP F 1 362 ? -1.498  -54.832 47.684  1 42.35 ? 362 ASP Z OD2   1 
ATOM   9562  N  N     . ASN F 1 363 ? -0.201  -57.477 44.755  1 30.27 ? 363 ASN Z N     1 
ATOM   9563  C  CA    . ASN F 1 363 ? 0.649   -56.888 43.733  1 29.67 ? 363 ASN Z CA    1 
ATOM   9564  C  C     . ASN F 1 363 ? 0.338   -55.427 43.681  1 28.44 ? 363 ASN Z C     1 
ATOM   9565  O  O     . ASN F 1 363 ? -0.784  -55.067 43.327  1 28.58 ? 363 ASN Z O     1 
ATOM   9566  C  CB    . ASN F 1 363 ? 0.328   -57.477 42.353  1 31.54 ? 363 ASN Z CB    1 
ATOM   9567  C  CG    . ASN F 1 363 ? 0.548   -58.964 42.215  1 36.25 ? 363 ASN Z CG    1 
ATOM   9568  O  OD1   . ASN F 1 363 ? 1.13    -59.623 43.082  1 38.04 ? 363 ASN Z OD1   1 
ATOM   9569  N  ND2   . ASN F 1 363 ? 0.086   -59.536 41.118  1 37.26 ? 363 ASN Z ND2   1 
ATOM   9570  N  N     . ARG F 1 364 ? 1.318   -54.574 44.003  1 27.25 ? 364 ARG Z N     1 
ATOM   9571  C  CA    . ARG F 1 364 ? 1.125   -53.124 43.943  1 26.43 ? 364 ARG Z CA    1 
ATOM   9572  C  C     . ARG F 1 364 ? 0.688   -52.618 42.559  1 26.34 ? 364 ARG Z C     1 
ATOM   9573  O  O     . ARG F 1 364 ? -0.254  -51.832 42.512  1 26.52 ? 364 ARG Z O     1 
ATOM   9574  C  CB    . ARG F 1 364 ? 2.358   -52.366 44.44   1 26.4  ? 364 ARG Z CB    1 
ATOM   9575  C  CG    . ARG F 1 364 ? 2.005   -51.056 45.109  1 27.42 ? 364 ARG Z CG    1 
ATOM   9576  C  CD    . ARG F 1 364 ? 1.378   -51.267 46.479  1 28.83 ? 364 ARG Z CD    1 
ATOM   9577  N  NE    . ARG F 1 364 ? 2.288   -51.957 47.396  1 28.98 ? 364 ARG Z NE    1 
ATOM   9578  C  CZ    . ARG F 1 364 ? 2.134   -53.211 47.804  1 29.2  ? 364 ARG Z CZ    1 
ATOM   9579  N  NH1   . ARG F 1 364 ? 1.088   -53.921 47.406  1 28.44 ? 364 ARG Z NH1   1 
ATOM   9580  N  NH2   . ARG F 1 364 ? 3.019   -53.761 48.622  1 28.55 ? 364 ARG Z NH2   1 
ATOM   9581  N  N     . PRO F 1 365 ? 1.289   -53.068 41.421  1 25.81 ? 365 PRO Z N     1 
ATOM   9582  C  CA    . PRO F 1 365 ? 0.831   -52.569 40.119  1 25.59 ? 365 PRO Z CA    1 
ATOM   9583  C  C     . PRO F 1 365 ? -0.628  -52.87  39.803  1 25.88 ? 365 PRO Z C     1 
ATOM   9584  O  O     . PRO F 1 365 ? -1.284  -52.063 39.153  1 26.09 ? 365 PRO Z O     1 
ATOM   9585  C  CB    . PRO F 1 365 ? 1.751   -53.282 39.13   1 26.02 ? 365 PRO Z CB    1 
ATOM   9586  C  CG    . PRO F 1 365 ? 2.95    -53.64  39.902  1 26.46 ? 365 PRO Z CG    1 
ATOM   9587  C  CD    . PRO F 1 365 ? 2.431   -53.989 41.25   1 25.18 ? 365 PRO Z CD    1 
ATOM   9588  N  N     . ASP F 1 366 ? -1.141  -54.018 40.258  1 25.93 ? 366 ASP Z N     1 
ATOM   9589  C  CA    . ASP F 1 366 ? -2.528  -54.408 39.995  1 26.4  ? 366 ASP Z CA    1 
ATOM   9590  C  C     . ASP F 1 366 ? -3.559  -53.452 40.555  1 26.52 ? 366 ASP Z C     1 
ATOM   9591  O  O     . ASP F 1 366 ? -4.666  -53.369 40.024  1 26.18 ? 366 ASP Z O     1 
ATOM   9592  C  CB    . ASP F 1 366 ? -2.789  -55.835 40.482  1 28.16 ? 366 ASP Z CB    1 
ATOM   9593  C  CG    . ASP F 1 366 ? -2.01   -56.894 39.739  1 33.17 ? 366 ASP Z CG    1 
ATOM   9594  O  OD1   . ASP F 1 366 ? -1.13   -56.535 38.929  1 34.2  ? 366 ASP Z OD1   1 
ATOM   9595  O  OD2   . ASP F 1 366 ? -2.271  -58.073 39.966  1 35.78 ? 366 ASP Z OD2   1 
ATOM   9596  N  N     . ARG F 1 367 ? -3.197  -52.713 41.606  1 26.89 ? 367 ARG Z N     1 
ATOM   9597  C  CA    . ARG F 1 367 ? -4.092  -51.725 42.192  1 27.78 ? 367 ARG Z CA    1 
ATOM   9598  C  C     . ARG F 1 367 ? -4.484  -50.615 41.179  1 28.3  ? 367 ARG Z C     1 
ATOM   9599  O  O     . ARG F 1 367 ? -5.506  -49.961 41.364  1 28.75 ? 367 ARG Z O     1 
ATOM   9600  C  CB    . ARG F 1 367 ? -3.456  -51.104 43.441  1 29.16 ? 367 ARG Z CB    1 
ATOM   9601  C  CG    . ARG F 1 367 ? -3.081  -52.098 44.531  1 31.73 ? 367 ARG Z CG    1 
ATOM   9602  C  CD    . ARG F 1 367 ? -2.354  -51.366 45.633  1 34.47 ? 367 ARG Z CD    1 
ATOM   9603  N  NE    . ARG F 1 367 ? -2.217  -52.155 46.853  1 36.97 ? 367 ARG Z NE    1 
ATOM   9604  C  CZ    . ARG F 1 367 ? -2.301  -51.649 48.079  1 40.36 ? 367 ARG Z CZ    1 
ATOM   9605  N  NH1   . ARG F 1 367 ? -2.551  -50.355 48.257  1 40.45 ? 367 ARG Z NH1   1 
ATOM   9606  N  NH2   . ARG F 1 367 ? -2.165  -52.436 49.139  1 40.81 ? 367 ARG Z NH2   1 
ATOM   9607  N  N     . GLY F 1 368 ? -3.684  -50.418 40.133  1 27.81 ? 368 GLY Z N     1 
ATOM   9608  C  CA    . GLY F 1 368 ? -3.98   -49.419 39.125  1 27.94 ? 368 GLY Z CA    1 
ATOM   9609  C  C     . GLY F 1 368 ? -4.582  -49.967 37.845  1 28.12 ? 368 GLY Z C     1 
ATOM   9610  O  O     . GLY F 1 368 ? -4.893  -49.182 36.948  1 28.7  ? 368 GLY Z O     1 
ATOM   9611  N  N     . ALA F 1 369 ? -4.778  -51.296 37.733  1 27.64 ? 369 ALA Z N     1 
ATOM   9612  C  CA    . ALA F 1 369 ? -5.334  -51.877 36.502  1 27.78 ? 369 ALA Z CA    1 
ATOM   9613  C  C     . ALA F 1 369 ? -6.789  -51.5   36.262  1 27.76 ? 369 ALA Z C     1 
ATOM   9614  O  O     . ALA F 1 369 ? -7.107  -51.029 35.173  1 27.86 ? 369 ALA Z O     1 
ATOM   9615  C  CB    . ALA F 1 369 ? -5.14   -53.385 36.463  1 27.95 ? 369 ALA Z CB    1 
ATOM   9616  N  N     . LEU F 1 370 ? -7.659  -51.661 37.266  1 27.67 ? 370 LEU Z N     1 
ATOM   9617  C  CA    . LEU F 1 370 ? -9.05   -51.235 37.123  1 28.19 ? 370 LEU Z CA    1 
ATOM   9618  C  C     . LEU F 1 370 ? -9.157  -49.71  36.959  1 28.62 ? 370 LEU Z C     1 
ATOM   9619  O  O     . LEU F 1 370 ? -9.769  -49.269 35.986  1 28.82 ? 370 LEU Z O     1 
ATOM   9620  C  CB    . LEU F 1 370 ? -9.952  -51.782 38.235  1 28.36 ? 370 LEU Z CB    1 
ATOM   9621  C  CG    . LEU F 1 370 ? -10.083 -53.289 38.279  1 29.87 ? 370 LEU Z CG    1 
ATOM   9622  C  CD1   . LEU F 1 370 ? -11.064 -53.676 39.3    1 30.67 ? 370 LEU Z CD1   1 
ATOM   9623  C  CD2   . LEU F 1 370 ? -10.513 -53.866 36.92   1 30.62 ? 370 LEU Z CD2   1 
ATOM   9624  N  N     . PRO F 1 371 ? -8.459  -48.885 37.78   1 28.53 ? 371 PRO Z N     1 
ATOM   9625  C  CA    . PRO F 1 371 ? -8.459  -47.435 37.538  1 28.53 ? 371 PRO Z CA    1 
ATOM   9626  C  C     . PRO F 1 371 ? -8.039  -47.049 36.116  1 28.49 ? 371 PRO Z C     1 
ATOM   9627  O  O     . PRO F 1 371 ? -8.593  -46.105 35.581  1 28.69 ? 371 PRO Z O     1 
ATOM   9628  C  CB    . PRO F 1 371 ? -7.453  -46.92  38.57   1 29.29 ? 371 PRO Z CB    1 
ATOM   9629  C  CG    . PRO F 1 371 ? -7.547  -47.895 39.684  1 29.72 ? 371 PRO Z CG    1 
ATOM   9630  C  CD    . PRO F 1 371 ? -7.667  -49.213 38.983  1 28.06 ? 371 PRO Z CD    1 
ATOM   9631  N  N     . LEU F 1 372 ? -7.108  -47.797 35.492  1 28.13 ? 372 LEU Z N     1 
ATOM   9632  C  CA    . LEU F 1 372 ? -6.677  -47.546 34.114  1 28.26 ? 372 LEU Z CA    1 
ATOM   9633  C  C     . LEU F 1 372 ? -7.85   -47.784 33.151  1 28.22 ? 372 LEU Z C     1 
ATOM   9634  O  O     . LEU F 1 372 ? -8.118  -46.943 32.292  1 28.54 ? 372 LEU Z O     1 
ATOM   9635  C  CB    . LEU F 1 372 ? -5.485  -48.45  33.753  1 28.4  ? 372 LEU Z CB    1 
ATOM   9636  C  CG    . LEU F 1 372 ? -5.049  -48.467 32.293  1 29.61 ? 372 LEU Z CG    1 
ATOM   9637  C  CD1   . LEU F 1 372 ? -4.495  -47.133 31.88   1 30.23 ? 372 LEU Z CD1   1 
ATOM   9638  C  CD2   . LEU F 1 372 ? -4.009  -49.509 32.074  1 29.99 ? 372 LEU Z CD2   1 
ATOM   9639  N  N     . VAL F 1 373 ? -8.574  -48.9   33.332  1 27.63 ? 373 VAL Z N     1 
ATOM   9640  C  CA    . VAL F 1 373 ? -9.748  -49.245 32.536  1 27.65 ? 373 VAL Z CA    1 
ATOM   9641  C  C     . VAL F 1 373 ? -10.817 -48.154 32.683  1 27.81 ? 373 VAL Z C     1 
ATOM   9642  O  O     . VAL F 1 373 ? -11.364 -47.691 31.684  1 27.99 ? 373 VAL Z O     1 
ATOM   9643  C  CB    . VAL F 1 373 ? -10.286 -50.621 32.982  1 28.32 ? 373 VAL Z CB    1 
ATOM   9644  C  CG1   . VAL F 1 373 ? -11.652 -50.912 32.374  1 28.87 ? 373 VAL Z CG1   1 
ATOM   9645  C  CG2   . VAL F 1 373 ? -9.299  -51.721 32.64   1 28.86 ? 373 VAL Z CG2   1 
ATOM   9646  N  N     . ALA F 1 374 ? -11.075 -47.719 33.928  1 27.65 ? 374 ALA Z N     1 
ATOM   9647  C  CA    . ALA F 1 374 ? -12.051 -46.679 34.254  1 27.88 ? 374 ALA Z CA    1 
ATOM   9648  C  C     . ALA F 1 374 ? -11.656 -45.312 33.665  1 27.84 ? 374 ALA Z C     1 
ATOM   9649  O  O     . ALA F 1 374 ? -12.519 -44.535 33.263  1 27.83 ? 374 ALA Z O     1 
ATOM   9650  C  CB    . ALA F 1 374 ? -12.213 -46.576 35.765  1 27.95 ? 374 ALA Z CB    1 
ATOM   9651  N  N     . MET F 1 375 ? -10.362 -45.027 33.609  1 27.64 ? 375 MET Z N     1 
ATOM   9652  C  CA    . MET F 1 375 ? -9.876  -43.782 33.039  1 28.2  ? 375 MET Z CA    1 
ATOM   9653  C  C     . MET F 1 375 ? -10.011 -43.78  31.502  1 28.68 ? 375 MET Z C     1 
ATOM   9654  O  O     . MET F 1 375 ? -10.226 -42.724 30.908  1 28.9  ? 375 MET Z O     1 
ATOM   9655  C  CB    . MET F 1 375 ? -8.432  -43.529 33.474  1 28.9  ? 375 MET Z CB    1 
ATOM   9656  C  CG    . MET F 1 375 ? -8.315  -43.131 34.926  1 31.13 ? 375 MET Z CG    1 
ATOM   9657  S  SD    . MET F 1 375 ? -6.599  -43.014 35.463  1 35.64 ? 375 MET Z SD    1 
ATOM   9658  C  CE    . MET F 1 375 ? -6.063  -41.621 34.489  1 35.04 ? 375 MET Z CE    1 
ATOM   9659  N  N     . LEU F 1 376 ? -9.912  -44.958 30.86   1 28.5  ? 376 LEU Z N     1 
ATOM   9660  C  CA    . LEU F 1 376 ? -10.027 -45.074 29.408  1 28.66 ? 376 LEU Z CA    1 
ATOM   9661  C  C     . LEU F 1 376 ? -11.477 -45.103 28.924  1 29.09 ? 376 LEU Z C     1 
ATOM   9662  O  O     . LEU F 1 376 ? -11.824 -44.388 27.985  1 29.28 ? 376 LEU Z O     1 
ATOM   9663  C  CB    . LEU F 1 376 ? -9.307  -46.338 28.917  1 28.61 ? 376 LEU Z CB    1 
ATOM   9664  C  CG    . LEU F 1 376 ? -7.802  -46.306 28.941  1 29.79 ? 376 LEU Z CG    1 
ATOM   9665  C  CD1   . LEU F 1 376 ? -7.233  -47.691 28.7    1 30.06 ? 376 LEU Z CD1   1 
ATOM   9666  C  CD2   . LEU F 1 376 ? -7.288  -45.357 27.905  1 30.59 ? 376 LEU Z CD2   1 
ATOM   9667  N  N     . ALA F 1 377 ? -12.317 -45.946 29.542  1 29.16 ? 377 ALA Z N     1 
ATOM   9668  C  CA    . ALA F 1 377 ? -13.692 -46.129 29.089  1 29.75 ? 377 ALA Z CA    1 
ATOM   9669  C  C     . ALA F 1 377 ? -14.778 -45.6   30.019  1 30.38 ? 377 ALA Z C     1 
ATOM   9670  O  O     . ALA F 1 377 ? -15.953 -45.882 29.791  1 30.55 ? 377 ALA Z O     1 
ATOM   9671  C  CB    . ALA F 1 377 ? -13.943 -47.604 28.797  1 29.77 ? 377 ALA Z CB    1 
ATOM   9672  N  N     . GLY F 1 378 ? -14.402 -44.863 31.054  1 30.64 ? 378 GLY Z N     1 
ATOM   9673  C  CA    . GLY F 1 378 ? -15.371 -44.333 32.004  1 31.4  ? 378 GLY Z CA    1 
ATOM   9674  C  C     . GLY F 1 378 ? -15.672 -45.338 33.096  1 31.98 ? 378 GLY Z C     1 
ATOM   9675  O  O     . GLY F 1 378 ? -15.764 -46.541 32.829  1 32.19 ? 378 GLY Z O     1 
ATOM   9676  N  N     . GLU F 1 379 ? -15.795 -44.865 34.341  1 32.02 ? 379 GLU Z N     1 
ATOM   9677  C  CA    . GLU F 1 379 ? -16.06  -45.745 35.485  1 32.55 ? 379 GLU Z CA    1 
ATOM   9678  C  C     . GLU F 1 379 ? -17.393 -46.497 35.381  1 33.15 ? 379 GLU Z C     1 
ATOM   9679  O  O     . GLU F 1 379 ? -17.541 -47.567 35.962  1 33.37 ? 379 GLU Z O     1 
ATOM   9680  C  CB    . GLU F 1 379 ? -15.983 -44.958 36.795  1 34.16 ? 379 GLU Z CB    1 
ATOM   9681  C  CG    . GLU F 1 379 ? -16.986 -43.826 36.874  1 37.72 ? 379 GLU Z CG    1 
ATOM   9682  C  CD    . GLU F 1 379 ? -16.894 -43.043 38.164  1 43.05 ? 379 GLU Z CD    1 
ATOM   9683  O  OE1   . GLU F 1 379 ? -15.758 -42.746 38.597  1 43.96 ? 379 GLU Z OE1   1 
ATOM   9684  O  OE2   . GLU F 1 379 ? -17.958 -42.73  38.747  1 45.14 ? 379 GLU Z OE2   1 
ATOM   9685  N  N     . ASN F 1 380 ? -18.343 -45.95  34.612  1 33.24 ? 380 ASN Z N     1 
ATOM   9686  C  CA    . ASN F 1 380 ? -19.667 -46.512 34.366  1 33.55 ? 380 ASN Z CA    1 
ATOM   9687  C  C     . ASN F 1 380 ? -19.655 -47.791 33.503  1 32.95 ? 380 ASN Z C     1 
ATOM   9688  O  O     . ASN F 1 380 ? -20.669 -48.482 33.446  1 33    ? 380 ASN Z O     1 
ATOM   9689  C  CB    . ASN F 1 380 ? -20.59  -45.44  33.752  1 35.26 ? 380 ASN Z CB    1 
ATOM   9690  C  CG    . ASN F 1 380 ? -19.94  -44.577 32.676  1 39    ? 380 ASN Z CG    1 
ATOM   9691  O  OD1   . ASN F 1 380 ? -19.314 -45.074 31.729  1 40.57 ? 380 ASN Z OD1   1 
ATOM   9692  N  ND2   . ASN F 1 380 ? -20.074 -43.259 32.797  1 39.3  ? 380 ASN Z ND2   1 
ATOM   9693  N  N     . ALA F 1 381 ? -18.531 -48.103 32.838  1 32.31 ? 381 ALA Z N     1 
ATOM   9694  C  CA    . ALA F 1 381 ? -18.436 -49.298 32      1 32.48 ? 381 ALA Z CA    1 
ATOM   9695  C  C     . ALA F 1 381 ? -18.54  -50.569 32.834  1 32.57 ? 381 ALA Z C     1 
ATOM   9696  O  O     . ALA F 1 381 ? -18.115 -50.575 33.989  1 32.76 ? 381 ALA Z O     1 
ATOM   9697  C  CB    . ALA F 1 381 ? -17.129 -49.294 31.23   1 32.68 ? 381 ALA Z CB    1 
ATOM   9698  N  N     . GLN F 1 382 ? -19.12  -51.641 32.265  1 32.18 ? 382 GLN Z N     1 
ATOM   9699  C  CA    . GLN F 1 382 ? -19.265 -52.899 32.994  1 32.18 ? 382 GLN Z CA    1 
ATOM   9700  C  C     . GLN F 1 382 ? -17.963 -53.671 32.996  1 32.03 ? 382 GLN Z C     1 
ATOM   9701  O  O     . GLN F 1 382 ? -17.463 -54.019 31.934  1 32.25 ? 382 GLN Z O     1 
ATOM   9702  C  CB    . GLN F 1 382 ? -20.411 -53.741 32.432  1 33.68 ? 382 GLN Z CB    1 
ATOM   9703  C  CG    . GLN F 1 382 ? -21.758 -53.077 32.621  1 37.01 ? 382 GLN Z CG    1 
ATOM   9704  C  CD    . GLN F 1 382 ? -22.893 -54.018 32.338  1 41.79 ? 382 GLN Z CD    1 
ATOM   9705  O  OE1   . GLN F 1 382 ? -22.811 -55.234 32.577  1 43.76 ? 382 GLN Z OE1   1 
ATOM   9706  N  NE2   . GLN F 1 382 ? -23.984 -53.467 31.83   1 42.09 ? 382 GLN Z NE2   1 
ATOM   9707  N  N     . ILE F 1 383 ? -17.39  -53.912 34.184  1 31.62 ? 383 ILE Z N     1 
ATOM   9708  C  CA    . ILE F 1 383 ? -16.107 -54.601 34.31   1 31.85 ? 383 ILE Z CA    1 
ATOM   9709  C  C     . ILE F 1 383 ? -16.215 -55.963 35.016  1 31.94 ? 383 ILE Z C     1 
ATOM   9710  O  O     . ILE F 1 383 ? -16.785 -56.064 36.095  1 32.31 ? 383 ILE Z O     1 
ATOM   9711  C  CB    . ILE F 1 383 ? -15.079 -53.664 34.99   1 32.4  ? 383 ILE Z CB    1 
ATOM   9712  C  CG1   . ILE F 1 383 ? -14.948 -52.341 34.215  1 33.6  ? 383 ILE Z CG1   1 
ATOM   9713  C  CG2   . ILE F 1 383 ? -13.723 -54.338 35.145  1 32.83 ? 383 ILE Z CG2   1 
ATOM   9714  C  CD1   . ILE F 1 383 ? -14.245 -51.246 34.978  1 35.09 ? 383 ILE Z CD1   1 
ATOM   9715  N  N     . PHE F 1 384 ? -15.668 -57.007 34.39   1 31.45 ? 384 PHE Z N     1 
ATOM   9716  C  CA    . PHE F 1 384 ? -15.636 -58.385 34.873  1 31.47 ? 384 PHE Z CA    1 
ATOM   9717  C  C     . PHE F 1 384 ? -14.185 -58.628 35.25   1 31.27 ? 384 PHE Z C     1 
ATOM   9718  O  O     . PHE F 1 384 ? -13.343 -58.696 34.363  1 31.49 ? 384 PHE Z O     1 
ATOM   9719  C  CB    . PHE F 1 384 ? -16.017 -59.311 33.702  1 31.33 ? 384 PHE Z CB    1 
ATOM   9720  C  CG    . PHE F 1 384 ? -16.155 -60.786 33.981  1 31.75 ? 384 PHE Z CG    1 
ATOM   9721  C  CD1   . PHE F 1 384 ? -17.35  -61.312 34.428  1 32.57 ? 384 PHE Z CD1   1 
ATOM   9722  C  CD2   . PHE F 1 384 ? -15.132 -61.659 33.679  1 32.5  ? 384 PHE Z CD2   1 
ATOM   9723  C  CE1   . PHE F 1 384 ? -17.485 -62.671 34.659  1 33.36 ? 384 PHE Z CE1   1 
ATOM   9724  C  CE2   . PHE F 1 384 ? -15.278 -63.022 33.884  1 33.34 ? 384 PHE Z CE2   1 
ATOM   9725  C  CZ    . PHE F 1 384 ? -16.454 -63.523 34.365  1 33.17 ? 384 PHE Z CZ    1 
ATOM   9726  N  N     . THR F 1 385 ? -13.877 -58.709 36.541  1 30.59 ? 385 THR Z N     1 
ATOM   9727  C  CA    . THR F 1 385 ? -12.504 -58.874 37.008  1 30.69 ? 385 THR Z CA    1 
ATOM   9728  C  C     . THR F 1 385 ? -12.189 -60.312 37.405  1 30.16 ? 385 THR Z C     1 
ATOM   9729  O  O     . THR F 1 385 ? -12.772 -60.811 38.357  1 30.68 ? 385 THR Z O     1 
ATOM   9730  C  CB    . THR F 1 385 ? -12.279 -57.93  38.194  1 32.67 ? 385 THR Z CB    1 
ATOM   9731  O  OG1   . THR F 1 385 ? -12.553 -56.59  37.788  1 33.77 ? 385 THR Z OG1   1 
ATOM   9732  C  CG2   . THR F 1 385 ? -10.881 -58.025 38.766  1 33.4  ? 385 THR Z CG2   1 
ATOM   9733  N  N     . PHE F 1 386 ? -11.255 -60.969 36.711  1 29.15 ? 386 PHE Z N     1 
ATOM   9734  C  CA    . PHE F 1 386 ? -10.853 -62.347 37.004  1 28.7  ? 386 PHE Z CA    1 
ATOM   9735  C  C     . PHE F 1 386 ? -9.49   -62.385 37.709  1 29.21 ? 386 PHE Z C     1 
ATOM   9736  O  O     . PHE F 1 386 ? -8.499  -61.915 37.152  1 29.17 ? 386 PHE Z O     1 
ATOM   9737  C  CB    . PHE F 1 386 ? -10.821 -63.173 35.718  1 27.74 ? 386 PHE Z CB    1 
ATOM   9738  C  CG    . PHE F 1 386 ? -10.427 -64.618 35.902  1 27.47 ? 386 PHE Z CG    1 
ATOM   9739  C  CD1   . PHE F 1 386 ? -11.379 -65.583 36.149  1 27.91 ? 386 PHE Z CD1   1 
ATOM   9740  C  CD2   . PHE F 1 386 ? -9.114  -65.019 35.75   1 27.81 ? 386 PHE Z CD2   1 
ATOM   9741  C  CE1   . PHE F 1 386 ? -11.017 -66.912 36.292  1 28.34 ? 386 PHE Z CE1   1 
ATOM   9742  C  CE2   . PHE F 1 386 ? -8.757  -66.346 35.901  1 28.16 ? 386 PHE Z CE2   1 
ATOM   9743  C  CZ    . PHE F 1 386 ? -9.71   -67.284 36.162  1 27.95 ? 386 PHE Z CZ    1 
ATOM   9744  N  N     . ILE F 1 387 ? -9.45   -62.952 38.931  1 29.45 ? 387 ILE Z N     1 
ATOM   9745  C  CA    . ILE F 1 387 ? -8.259  -63.044 39.781  1 30.43 ? 387 ILE Z CA    1 
ATOM   9746  C  C     . ILE F 1 387 ? -7.81   -64.499 39.948  1 31.66 ? 387 ILE Z C     1 
ATOM   9747  O  O     . ILE F 1 387 ? -8.649  -65.374 40.163  1 31.88 ? 387 ILE Z O     1 
ATOM   9748  C  CB    . ILE F 1 387 ? -8.551  -62.365 41.146  1 30.97 ? 387 ILE Z CB    1 
ATOM   9749  C  CG1   . ILE F 1 387 ? -9.075  -60.926 40.964  1 32.09 ? 387 ILE Z CG1   1 
ATOM   9750  C  CG2   . ILE F 1 387 ? -7.35   -62.405 42.089  1 31.35 ? 387 ILE Z CG2   1 
ATOM   9751  C  CD1   . ILE F 1 387 ? -8.16   -60.025 40.131  1 33.42 ? 387 ILE Z CD1   1 
ATOM   9752  N  N     . TYR F 1 388 ? -6.496  -64.767 39.861  1 32.2  ? 388 TYR Z N     1 
ATOM   9753  C  CA    . TYR F 1 388 ? -5.998  -66.14  39.945  1 32.96 ? 388 TYR Z CA    1 
ATOM   9754  C  C     . TYR F 1 388 ? -4.782  -66.353 40.858  1 33.21 ? 388 TYR Z C     1 
ATOM   9755  O  O     . TYR F 1 388 ? -4.203  -67.434 40.849  1 33.22 ? 388 TYR Z O     1 
ATOM   9756  C  CB    . TYR F 1 388 ? -5.695  -66.674 38.534  1 33.46 ? 388 TYR Z CB    1 
ATOM   9757  C  CG    . TYR F 1 388 ? -4.776  -65.794 37.714  1 34.64 ? 388 TYR Z CG    1 
ATOM   9758  C  CD1   . TYR F 1 388 ? -5.283  -64.796 36.893  1 35.6  ? 388 TYR Z CD1   1 
ATOM   9759  C  CD2   . TYR F 1 388 ? -3.401  -65.985 37.728  1 35.7  ? 388 TYR Z CD2   1 
ATOM   9760  C  CE1   . TYR F 1 388 ? -4.446  -63.986 36.144  1 36.48 ? 388 TYR Z CE1   1 
ATOM   9761  C  CE2   . TYR F 1 388 ? -2.555  -65.182 36.979  1 36.53 ? 388 TYR Z CE2   1 
ATOM   9762  C  CZ    . TYR F 1 388 ? -3.081  -64.176 36.198  1 37.53 ? 388 TYR Z CZ    1 
ATOM   9763  O  OH    . TYR F 1 388 ? -2.242  -63.363 35.483  1 39.6  ? 388 TYR Z OH    1 
ATOM   9764  N  N     . GLY F 1 389 ? -4.411  -65.348 41.636  1 33.29 ? 389 GLY Z N     1 
ATOM   9765  C  CA    . GLY F 1 389 ? -3.263  -65.432 42.536  1 33.67 ? 389 GLY Z CA    1 
ATOM   9766  C  C     . GLY F 1 389 ? -3.579  -66.062 43.876  1 33.54 ? 389 GLY Z C     1 
ATOM   9767  O  O     . GLY F 1 389 ? -4.747  -66.188 44.235  1 33.66 ? 389 GLY Z O     1 
ATOM   9768  N  N     . PRO F 1 390 ? -2.554  -66.458 44.651  1 33.17 ? 390 PRO Z N     1 
ATOM   9769  C  CA    . PRO F 1 390 ? -2.82   -67.13  45.931  1 33.32 ? 390 PRO Z CA    1 
ATOM   9770  C  C     . PRO F 1 390 ? -3.414  -66.265 47.038  1 33.77 ? 390 PRO Z C     1 
ATOM   9771  O  O     . PRO F 1 390 ? -2.916  -65.182 47.321  1 34.32 ? 390 PRO Z O     1 
ATOM   9772  C  CB    . PRO F 1 390 ? -1.453  -67.692 46.341  1 33.88 ? 390 PRO Z CB    1 
ATOM   9773  C  CG    . PRO F 1 390 ? -0.553  -67.503 45.175  1 34.17 ? 390 PRO Z CG    1 
ATOM   9774  C  CD    . PRO F 1 390 ? -1.111  -66.391 44.367  1 32.58 ? 390 PRO Z CD    1 
ATOM   9775  N  N     . LEU F 1 391 ? -4.455  -66.774 47.697  1 33.39 ? 391 LEU Z N     1 
ATOM   9776  C  CA    . LEU F 1 391 ? -5.107  -66.054 48.773  1 33.58 ? 391 LEU Z CA    1 
ATOM   9777  C  C     . LEU F 1 391 ? -4.767  -66.636 50.125  1 33.65 ? 391 LEU Z C     1 
ATOM   9778  O  O     . LEU F 1 391 ? -4.758  -67.853 50.293  1 33.62 ? 391 LEU Z O     1 
ATOM   9779  C  CB    . LEU F 1 391 ? -6.628  -66.122 48.603  1 33.94 ? 391 LEU Z CB    1 
ATOM   9780  C  CG    . LEU F 1 391 ? -7.199  -65.562 47.324  1 35.85 ? 391 LEU Z CG    1 
ATOM   9781  C  CD1   . LEU F 1 391 ? -8.709  -65.718 47.307  1 36.64 ? 391 LEU Z CD1   1 
ATOM   9782  C  CD2   . LEU F 1 391 ? -6.829  -64.1   47.16   1 36.67 ? 391 LEU Z CD2   1 
ATOM   9783  N  N     . ILE F 1 392 ? -4.551  -65.765 51.113  1 33.44 ? 392 ILE Z N     1 
ATOM   9784  C  CA    . ILE F 1 392 ? -4.348  -66.207 52.485  1 33.44 ? 392 ILE Z CA    1 
ATOM   9785  C  C     . ILE F 1 392 ? -5.723  -66.675 52.995  1 33.77 ? 392 ILE Z C     1 
ATOM   9786  O  O     . ILE F 1 392 ? -6.756  -66.161 52.554  1 33.72 ? 392 ILE Z O     1 
ATOM   9787  C  CB    . ILE F 1 392 ? -3.744  -65.067 53.343  1 33.61 ? 392 ILE Z CB    1 
ATOM   9788  C  CG1   . ILE F 1 392 ? -4.603  -63.792 53.238  1 34.29 ? 392 ILE Z CG1   1 
ATOM   9789  C  CG2   . ILE F 1 392 ? -2.294  -64.796 52.922  1 33.98 ? 392 ILE Z CG2   1 
ATOM   9790  C  CD1   . ILE F 1 392 ? -4.179  -62.66  54.089  1 35.41 ? 392 ILE Z CD1   1 
ATOM   9791  N  N     . LYS F 1 393 ? -5.751  -67.682 53.874  1 34.01 ? 393 LYS Z N     1 
ATOM   9792  C  CA    . LYS F 1 393 ? -7.015  -68.225 54.383  1 34.57 ? 393 LYS Z CA    1 
ATOM   9793  C  C     . LYS F 1 393 ? -7.948  -67.149 54.987  1 35.47 ? 393 LYS Z C     1 
ATOM   9794  O  O     . LYS F 1 393 ? -9.16   -67.21  54.793  1 35.89 ? 393 LYS Z O     1 
ATOM   9795  C  CB    . LYS F 1 393 ? -6.756  -69.375 55.369  1 35.63 ? 393 LYS Z CB    1 
ATOM   9796  C  CG    . LYS F 1 393 ? -8.016  -70.081 55.861  1 38.81 ? 393 LYS Z CG    1 
ATOM   9797  C  CD    . LYS F 1 393 ? -8.803  -70.741 54.742  1 42.2  ? 393 LYS Z CD    1 
ATOM   9798  C  CE    . LYS F 1 393 ? -8.75   -72.248 54.831  1 45    ? 393 LYS Z CE    1 
ATOM   9799  N  NZ    . LYS F 1 393 ? -9.503  -72.762 56.005  1 46.72 ? 393 LYS Z NZ    1 
ATOM   9800  N  N     . GLY F 1 394 ? -7.373  -66.146 55.642  1 35.45 ? 394 GLY Z N     1 
ATOM   9801  C  CA    . GLY F 1 394 ? -8.155  -65.061 56.212  1 36.22 ? 394 GLY Z CA    1 
ATOM   9802  C  C     . GLY F 1 394 ? -8.892  -64.233 55.175  1 37.13 ? 394 GLY Z C     1 
ATOM   9803  O  O     . GLY F 1 394 ? -9.996  -63.754 55.446  1 37.41 ? 394 GLY Z O     1 
ATOM   9804  N  N     . ALA F 1 395 ? -8.296  -64.068 53.97   1 37.31 ? 395 ALA Z N     1 
ATOM   9805  C  CA    . ALA F 1 395 ? -8.899  -63.296 52.881  1 37.8  ? 395 ALA Z CA    1 
ATOM   9806  C  C     . ALA F 1 395 ? -10.089 -64.01  52.27   1 38.37 ? 395 ALA Z C     1 
ATOM   9807  O  O     . ALA F 1 395 ? -11.116 -63.373 52.055  1 38.44 ? 395 ALA Z O     1 
ATOM   9808  C  CB    . ALA F 1 395 ? -7.87   -62.979 51.809  1 37.81 ? 395 ALA Z CB    1 
ATOM   9809  N  N     . ILE F 1 396 ? -9.982  -65.331 52.027  1 38.7  ? 396 ILE Z N     1 
ATOM   9810  C  CA    . ILE F 1 396 ? -11.103 -66.09  51.461  1 39.71 ? 396 ILE Z CA    1 
ATOM   9811  C  C     . ILE F 1 396 ? -12.27  -66.201 52.457  1 40.72 ? 396 ILE Z C     1 
ATOM   9812  O  O     . ILE F 1 396 ? -13.43  -66.174 52.043  1 41.06 ? 396 ILE Z O     1 
ATOM   9813  C  CB    . ILE F 1 396 ? -10.674 -67.456 50.877  1 40.2  ? 396 ILE Z CB    1 
ATOM   9814  C  CG1   . ILE F 1 396 ? -11.713 -67.984 49.869  1 41.03 ? 396 ILE Z CG1   1 
ATOM   9815  C  CG2   . ILE F 1 396 ? -10.334 -68.477 51.965  1 40.66 ? 396 ILE Z CG2   1 
ATOM   9816  C  CD1   . ILE F 1 396 ? -11.927 -67.062 48.678  1 42.08 ? 396 ILE Z CD1   1 
ATOM   9817  N  N     . ASN F 1 397 ? -11.973 -66.228 53.767  1 40.96 ? 397 ASN Z N     1 
ATOM   9818  C  CA    . ASN F 1 397 ? -13.015 -66.249 54.785  1 41.56 ? 397 ASN Z CA    1 
ATOM   9819  C  C     . ASN F 1 397 ? -13.779 -64.922 54.782  1 41.96 ? 397 ASN Z C     1 
ATOM   9820  O  O     . ASN F 1 397 ? -14.999 -64.923 54.915  1 42.15 ? 397 ASN Z O     1 
ATOM   9821  C  CB    . ASN F 1 397 ? -12.422 -66.544 56.155  1 42.82 ? 397 ASN Z CB    1 
ATOM   9822  C  CG    . ASN F 1 397 ? -11.997 -67.984 56.316  1 46.28 ? 397 ASN Z CG    1 
ATOM   9823  O  OD1   . ASN F 1 397 ? -12.412 -68.875 55.564  1 47.43 ? 397 ASN Z OD1   1 
ATOM   9824  N  ND2   . ASN F 1 397 ? -11.144 -68.246 57.295  1 47.09 ? 397 ASN Z ND2   1 
ATOM   9825  N  N     . LEU F 1 398 ? -13.074 -63.798 54.578  1 42    ? 398 LEU Z N     1 
ATOM   9826  C  CA    . LEU F 1 398 ? -13.705 -62.481 54.493  1 42.59 ? 398 LEU Z CA    1 
ATOM   9827  C  C     . LEU F 1 398 ? -14.514 -62.322 53.218  1 42.68 ? 398 LEU Z C     1 
ATOM   9828  O  O     . LEU F 1 398 ? -15.544 -61.66  53.235  1 42.91 ? 398 LEU Z O     1 
ATOM   9829  C  CB    . LEU F 1 398 ? -12.678 -61.35  54.605  1 43.08 ? 398 LEU Z CB    1 
ATOM   9830  C  CG    . LEU F 1 398 ? -12.34  -60.903 56.022  1 44.96 ? 398 LEU Z CG    1 
ATOM   9831  C  CD1   . LEU F 1 398 ? -11.332 -59.773 55.999  1 45.69 ? 398 LEU Z CD1   1 
ATOM   9832  C  CD2   . LEU F 1 398 ? -13.587 -60.464 56.781  1 45.67 ? 398 LEU Z CD2   1 
ATOM   9833  N  N     . ILE F 1 399 ? -14.068 -62.936 52.12   1 42.23 ? 399 ILE Z N     1 
ATOM   9834  C  CA    . ILE F 1 399 ? -14.803 -62.915 50.86   1 42.18 ? 399 ILE Z CA    1 
ATOM   9835  C  C     . ILE F 1 399 ? -16.165 -63.617 51.04   1 41.72 ? 399 ILE Z C     1 
ATOM   9836  O  O     . ILE F 1 399 ? -17.171 -63.153 50.511  1 41.9  ? 399 ILE Z O     1 
ATOM   9837  C  CB    . ILE F 1 399 ? -13.929 -63.559 49.759  1 42.92 ? 399 ILE Z CB    1 
ATOM   9838  C  CG1   . ILE F 1 399 ? -12.814 -62.594 49.334  1 43.86 ? 399 ILE Z CG1   1 
ATOM   9839  C  CG2   . ILE F 1 399 ? -14.749 -64.015 48.554  1 43.53 ? 399 ILE Z CG2   1 
ATOM   9840  C  CD1   . ILE F 1 399 ? -11.709 -63.233 48.611  1 45.15 ? 399 ILE Z CD1   1 
ATOM   9841  N  N     . ASP F 1 400 ? -16.207 -64.683 51.843  1 41.11 ? 400 ASP Z N     1 
ATOM   9842  C  CA    . ASP F 1 400 ? -17.443 -65.411 52.096  1 41.25 ? 400 ASP Z CA    1 
ATOM   9843  C  C     . ASP F 1 400 ? -18.359 -64.775 53.168  1 41.11 ? 400 ASP Z C     1 
ATOM   9844  O  O     . ASP F 1 400 ? -19.518 -65.18  53.288  1 41.43 ? 400 ASP Z O     1 
ATOM   9845  C  CB    . ASP F 1 400 ? -17.134 -66.877 52.444  1 42.71 ? 400 ASP Z CB    1 
ATOM   9846  C  CG    . ASP F 1 400 ? -16.493 -67.643 51.308  1 46.46 ? 400 ASP Z CG    1 
ATOM   9847  O  OD1   . ASP F 1 400 ? -16.695 -67.246 50.143  1 47.09 ? 400 ASP Z OD1   1 
ATOM   9848  O  OD2   . ASP F 1 400 ? -15.787 -68.637 51.588  1 48.29 ? 400 ASP Z OD2   1 
ATOM   9849  N  N     . GLN F 1 401 ? -17.86  -63.797 53.942  1 40.28 ? 401 GLN Z N     1 
ATOM   9850  C  CA    . GLN F 1 401 ? -18.673 -63.16  54.979  1 40.01 ? 401 GLN Z CA    1 
ATOM   9851  C  C     . GLN F 1 401 ? -19.029 -61.706 54.639  1 39.13 ? 401 GLN Z C     1 
ATOM   9852  O  O     . GLN F 1 401 ? -20.205 -61.342 54.655  1 39.17 ? 401 GLN Z O     1 
ATOM   9853  C  CB    . GLN F 1 401 ? -17.99  -63.258 56.361  1 41.98 ? 401 GLN Z CB    1 
ATOM   9854  C  CG    . GLN F 1 401 ? -18.692 -62.444 57.459  1 45.63 ? 401 GLN Z CG    1 
ATOM   9855  C  CD    . GLN F 1 401 ? -17.761 -62.034 58.573  1 49.65 ? 401 GLN Z CD    1 
ATOM   9856  O  OE1   . GLN F 1 401 ? -16.728 -62.67  58.817  1 51.52 ? 401 GLN Z OE1   1 
ATOM   9857  N  NE2   . GLN F 1 401 ? -18.112 -60.964 59.276  1 49.34 ? 401 GLN Z NE2   1 
ATOM   9858  N  N     . ASP F 1 402 ? -18.016 -60.878 54.366  1 38.2  ? 402 ASP Z N     1 
ATOM   9859  C  CA    . ASP F 1 402 ? -18.201 -59.471 54.058  1 37.83 ? 402 ASP Z CA    1 
ATOM   9860  C  C     . ASP F 1 402 ? -17.019 -58.997 53.236  1 36.77 ? 402 ASP Z C     1 
ATOM   9861  O  O     . ASP F 1 402 ? -15.953 -58.754 53.797  1 36.94 ? 402 ASP Z O     1 
ATOM   9862  C  CB    . ASP F 1 402 ? -18.274 -58.669 55.368  1 39.98 ? 402 ASP Z CB    1 
ATOM   9863  C  CG    . ASP F 1 402 ? -18.821 -57.259 55.231  1 45.2  ? 402 ASP Z CG    1 
ATOM   9864  O  OD1   . ASP F 1 402 ? -18.993 -56.795 54.08   1 46.4  ? 402 ASP Z OD1   1 
ATOM   9865  O  OD2   . ASP F 1 402 ? -19.088 -56.622 56.275  1 47.3  ? 402 ASP Z OD2   1 
ATOM   9866  N  N     . ILE F 1 403 ? -17.193 -58.88  51.913  1 35.53 ? 403 ILE Z N     1 
ATOM   9867  C  CA    . ILE F 1 403 ? -16.122 -58.424 51.022  1 34.74 ? 403 ILE Z CA    1 
ATOM   9868  C  C     . ILE F 1 403 ? -15.712 -56.961 51.303  1 33.71 ? 403 ILE Z C     1 
ATOM   9869  O  O     . ILE F 1 403 ? -14.55  -56.604 51.122  1 33.86 ? 403 ILE Z O     1 
ATOM   9870  C  CB    . ILE F 1 403 ? -16.49  -58.672 49.531  1 35    ? 403 ILE Z CB    1 
ATOM   9871  C  CG1   . ILE F 1 403 ? -15.296 -58.468 48.586  1 35.66 ? 403 ILE Z CG1   1 
ATOM   9872  C  CG2   . ILE F 1 403 ? -17.686 -57.834 49.097  1 35.41 ? 403 ILE Z CG2   1 
ATOM   9873  C  CD1   . ILE F 1 403 ? -14.117 -59.277 48.891  1 36.82 ? 403 ILE Z CD1   1 
ATOM   9874  N  N     . ASN F 1 404 ? -16.645 -56.141 51.803  1 32.5  ? 404 ASN Z N     1 
ATOM   9875  C  CA    . ASN F 1 404 ? -16.385 -54.74  52.13   1 32.06 ? 404 ASN Z CA    1 
ATOM   9876  C  C     . ASN F 1 404 ? -15.407 -54.588 53.295  1 32.19 ? 404 ASN Z C     1 
ATOM   9877  O  O     . ASN F 1 404 ? -14.681 -53.599 53.347  1 32.33 ? 404 ASN Z O     1 
ATOM   9878  C  CB    . ASN F 1 404 ? -17.687 -54.016 52.423  1 32.46 ? 404 ASN Z CB    1 
ATOM   9879  C  CG    . ASN F 1 404 ? -18.69  -54.201 51.323  1 34.88 ? 404 ASN Z CG    1 
ATOM   9880  O  OD1   . ASN F 1 404 ? -18.456 -53.803 50.184  1 35.86 ? 404 ASN Z OD1   1 
ATOM   9881  N  ND2   . ASN F 1 404 ? -19.806 -54.849 51.625  1 35.48 ? 404 ASN Z ND2   1 
ATOM   9882  N  N     . LYS F 1 405 ? -15.378 -55.567 54.221  1 32.06 ? 405 LYS Z N     1 
ATOM   9883  C  CA    . LYS F 1 405 ? -14.444 -55.587 55.352  1 32.19 ? 405 LYS Z CA    1 
ATOM   9884  C  C     . LYS F 1 405 ? -13.014 -55.778 54.835  1 32.04 ? 405 LYS Z C     1 
ATOM   9885  O  O     . LYS F 1 405 ? -12.08  -55.176 55.357  1 32.25 ? 405 LYS Z O     1 
ATOM   9886  C  CB    . LYS F 1 405 ? -14.777 -56.744 56.305  1 34.08 ? 405 LYS Z CB    1 
ATOM   9887  C  CG    . LYS F 1 405 ? -15.865 -56.453 57.317  1 38.38 ? 405 LYS Z CG    1 
ATOM   9888  C  CD    . LYS F 1 405 ? -16.028 -57.645 58.252  1 42.38 ? 405 LYS Z CD    1 
ATOM   9889  C  CE    . LYS F 1 405 ? -17.172 -57.496 59.217  1 45.62 ? 405 LYS Z CE    1 
ATOM   9890  N  NZ    . LYS F 1 405 ? -17.411 -58.765 59.947  1 47.88 ? 405 LYS Z NZ    1 
ATOM   9891  N  N     . LEU F 1 406 ? -12.846 -56.634 53.824  1 31.54 ? 406 LEU Z N     1 
ATOM   9892  C  CA    . LEU F 1 406 ? -11.556 -56.893 53.216  1 31.84 ? 406 LEU Z CA    1 
ATOM   9893  C  C     . LEU F 1 406 ? -11.112 -55.653 52.424  1 32.29 ? 406 LEU Z C     1 
ATOM   9894  O  O     . LEU F 1 406 ? -9.961  -55.236 52.532  1 32.51 ? 406 LEU Z O     1 
ATOM   9895  C  CB    . LEU F 1 406 ? -11.684 -58.123 52.302  1 31.89 ? 406 LEU Z CB    1 
ATOM   9896  C  CG    . LEU F 1 406 ? -10.426 -58.639 51.633  1 33.05 ? 406 LEU Z CG    1 
ATOM   9897  C  CD1   . LEU F 1 406 ? -9.341  -58.937 52.649  1 33.39 ? 406 LEU Z CD1   1 
ATOM   9898  C  CD2   . LEU F 1 406 ? -10.73  -59.88  50.827  1 33.89 ? 406 LEU Z CD2   1 
ATOM   9899  N  N     . ALA F 1 407 ? -12.039 -55.03  51.679  1 32.19 ? 407 ALA Z N     1 
ATOM   9900  C  CA    . ALA F 1 407 ? -11.764 -53.82  50.905  1 32.56 ? 407 ALA Z CA    1 
ATOM   9901  C  C     . ALA F 1 407 ? -11.35  -52.661 51.805  1 33.02 ? 407 ALA Z C     1 
ATOM   9902  O  O     . ALA F 1 407 ? -10.525 -51.85  51.4    1 33.37 ? 407 ALA Z O     1 
ATOM   9903  C  CB    . ALA F 1 407 ? -12.987 -53.43  50.097  1 32.59 ? 407 ALA Z CB    1 
ATOM   9904  N  N     . LYS F 1 408 ? -11.916 -52.59  53.024  1 33.07 ? 408 LYS Z N     1 
ATOM   9905  C  CA    . LYS F 1 408 ? -11.629 -51.552 54.013  1 33.77 ? 408 LYS Z CA    1 
ATOM   9906  C  C     . LYS F 1 408 ? -10.175 -51.601 54.483  1 34.3  ? 408 LYS Z C     1 
ATOM   9907  O  O     . LYS F 1 408 ? -9.549  -50.554 54.657  1 34.42 ? 408 LYS Z O     1 
ATOM   9908  C  CB    . LYS F 1 408 ? -12.572 -51.689 55.225  1 35.68 ? 408 LYS Z CB    1 
ATOM   9909  C  CG    . LYS F 1 408 ? -12.407 -50.583 56.266  1 40.15 ? 408 LYS Z CG    1 
ATOM   9910  C  CD    . LYS F 1 408 ? -13.163 -50.859 57.557  1 44.98 ? 408 LYS Z CD    1 
ATOM   9911  C  CE    . LYS F 1 408 ? -14.64  -50.58  57.432  1 49.02 ? 408 LYS Z CE    1 
ATOM   9912  N  NZ    . LYS F 1 408 ? -15.453 -51.566 58.199  1 51.44 ? 408 LYS Z NZ    1 
ATOM   9913  N  N     . ARG F 1 409 ? -9.629  -52.808 54.672  1 34.53 ? 409 ARG Z N     1 
ATOM   9914  C  CA    . ARG F 1 409 ? -8.26   -52.947 55.167  1 35.31 ? 409 ARG Z CA    1 
ATOM   9915  C  C     . ARG F 1 409 ? -7.188  -53.068 54.076  1 34.77 ? 409 ARG Z C     1 
ATOM   9916  O  O     . ARG F 1 409 ? -6.04   -52.725 54.338  1 34.83 ? 409 ARG Z O     1 
ATOM   9917  C  CB    . ARG F 1 409 ? -8.151  -54.111 56.166  1 37.97 ? 409 ARG Z CB    1 
ATOM   9918  C  CG    . ARG F 1 409 ? -8.554  -55.465 55.6    1 43.22 ? 409 ARG Z CG    1 
ATOM   9919  C  CD    . ARG F 1 409 ? -8.445  -56.545 56.641  1 48.41 ? 409 ARG Z CD    1 
ATOM   9920  N  NE    . ARG F 1 409 ? -7.059  -56.741 57.059  1 53.24 ? 409 ARG Z NE    1 
ATOM   9921  C  CZ    . ARG F 1 409 ? -6.677  -57.581 58.01   1 56.86 ? 409 ARG Z CZ    1 
ATOM   9922  N  NH1   . ARG F 1 409 ? -7.575  -58.318 58.658  1 56.74 ? 409 ARG Z NH1   1 
ATOM   9923  N  NH2   . ARG F 1 409 ? -5.393  -57.704 58.317  1 57.52 ? 409 ARG Z NH2   1 
ATOM   9924  N  N     . ASN F 1 410 ? -7.542  -53.529 52.87   1 34.09 ? 410 ASN Z N     1 
ATOM   9925  C  CA    . ASN F 1 410 ? -6.555  -53.709 51.807  1 34.04 ? 410 ASN Z CA    1 
ATOM   9926  C  C     . ASN F 1 410 ? -6.834  -52.851 50.56   1 34.24 ? 410 ASN Z C     1 
ATOM   9927  O  O     . ASN F 1 410 ? -7.956  -52.817 50.06   1 34.6  ? 410 ASN Z O     1 
ATOM   9928  C  CB    . ASN F 1 410 ? -6.466  -55.187 51.454  1 34.88 ? 410 ASN Z CB    1 
ATOM   9929  C  CG    . ASN F 1 410 ? -5.347  -55.53  50.52   1 37.71 ? 410 ASN Z CG    1 
ATOM   9930  O  OD1   . ASN F 1 410 ? -5.48   -55.427 49.302  1 38.87 ? 410 ASN Z OD1   1 
ATOM   9931  N  ND2   . ASN F 1 410 ? -4.221  -55.962 51.068  1 38.2  ? 410 ASN Z ND2   1 
ATOM   9932  N  N     . GLY F 1 411 ? -5.801  -52.185 50.06   1 33.82 ? 411 GLY Z N     1 
ATOM   9933  C  CA    . GLY F 1 411 ? -5.915  -51.316 48.896  1 33.9  ? 411 GLY Z CA    1 
ATOM   9934  C  C     . GLY F 1 411 ? -6.186  -52.013 47.575  1 33.75 ? 411 GLY Z C     1 
ATOM   9935  O  O     . GLY F 1 411 ? -6.813  -51.422 46.689  1 34.1  ? 411 GLY Z O     1 
ATOM   9936  N  N     . LEU F 1 412 ? -5.713  -53.263 47.412  1 33.1  ? 412 LEU Z N     1 
ATOM   9937  C  CA    . LEU F 1 412 ? -5.979  -54     46.172  1 32.91 ? 412 LEU Z CA    1 
ATOM   9938  C  C     . LEU F 1 412 ? -7.431  -54.451 46.145  1 32.82 ? 412 LEU Z C     1 
ATOM   9939  O  O     . LEU F 1 412 ? -8.102  -54.3   45.121  1 33.09 ? 412 LEU Z O     1 
ATOM   9940  C  CB    . LEU F 1 412 ? -5.037  -55.191 45.946  1 32.76 ? 412 LEU Z CB    1 
ATOM   9941  C  CG    . LEU F 1 412 ? -5.291  -55.932 44.639  1 33.75 ? 412 LEU Z CG    1 
ATOM   9942  C  CD1   . LEU F 1 412 ? -5.062  -55.05  43.446  1 34.33 ? 412 LEU Z CD1   1 
ATOM   9943  C  CD2   . LEU F 1 412 ? -4.464  -57.141 44.524  1 34.24 ? 412 LEU Z CD2   1 
ATOM   9944  N  N     . TRP F 1 413 ? -7.929  -54.965 47.278  1 32.2  ? 413 TRP Z N     1 
ATOM   9945  C  CA    . TRP F 1 413 ? -9.328  -55.347 47.371  1 32.04 ? 413 TRP Z CA    1 
ATOM   9946  C  C     . TRP F 1 413 ? -10.234 -54.122 47.241  1 31.99 ? 413 TRP Z C     1 
ATOM   9947  O  O     . TRP F 1 413 ? -11.301 -54.243 46.666  1 32.06 ? 413 TRP Z O     1 
ATOM   9948  C  CB    . TRP F 1 413 ? -9.611  -56.156 48.642  1 31.91 ? 413 TRP Z CB    1 
ATOM   9949  C  CG    . TRP F 1 413 ? -9.104  -57.567 48.561  1 32.4  ? 413 TRP Z CG    1 
ATOM   9950  C  CD1   . TRP F 1 413 ? -8.061  -58.109 49.253  1 33.25 ? 413 TRP Z CD1   1 
ATOM   9951  C  CD2   . TRP F 1 413 ? -9.594  -58.601 47.698  1 32.45 ? 413 TRP Z CD2   1 
ATOM   9952  N  NE1   . TRP F 1 413 ? -7.883  -59.423 48.888  1 33.46 ? 413 TRP Z NE1   1 
ATOM   9953  C  CE2   . TRP F 1 413 ? -8.807  -59.746 47.928  1 33.16 ? 413 TRP Z CE2   1 
ATOM   9954  C  CE3   . TRP F 1 413 ? -10.616 -58.665 46.744  1 32.91 ? 413 TRP Z CE3   1 
ATOM   9955  C  CZ2   . TRP F 1 413 ? -9.006  -60.935 47.231  1 33.7  ? 413 TRP Z CZ2   1 
ATOM   9956  C  CZ3   . TRP F 1 413 ? -10.804 -59.842 46.054  1 33.65 ? 413 TRP Z CZ3   1 
ATOM   9957  C  CH2   . TRP F 1 413 ? -10.003 -60.958 46.297  1 33.69 ? 413 TRP Z CH2   1 
ATOM   9958  N  N     . LYS F 1 414 ? -9.776  -52.93  47.692  1 31.59 ? 414 LYS Z N     1 
ATOM   9959  C  CA    . LYS F 1 414 ? -10.499 -51.665 47.569  1 31.63 ? 414 LYS Z CA    1 
ATOM   9960  C  C     . LYS F 1 414 ? -10.648 -51.283 46.08   1 31.79 ? 414 LYS Z C     1 
ATOM   9961  O  O     . LYS F 1 414 ? -11.706 -50.823 45.667  1 31.73 ? 414 LYS Z O     1 
ATOM   9962  C  CB    . LYS F 1 414 ? -9.749  -50.565 48.331  1 33.03 ? 414 LYS Z CB    1 
ATOM   9963  C  CG    . LYS F 1 414 ? -10.615 -49.385 48.756  1 36.7  ? 414 LYS Z CG    1 
ATOM   9964  C  CD    . LYS F 1 414 ? -9.773  -48.217 49.292  1 40.71 ? 414 LYS Z CD    1 
ATOM   9965  C  CE    . LYS F 1 414 ? -8.909  -48.618 50.47   1 43.98 ? 414 LYS Z CE    1 
ATOM   9966  N  NZ    . LYS F 1 414 ? -9.718  -49.109 51.608  1 45.75 ? 414 LYS Z NZ    1 
ATOM   9967  N  N     . SER F 1 415 ? -9.597  -51.495 45.277  1 31.84 ? 415 SER Z N     1 
ATOM   9968  C  CA    . SER F 1 415 ? -9.615  -51.222 43.837  1 32.35 ? 415 SER Z CA    1 
ATOM   9969  C  C     . SER F 1 415 ? -10.592 -52.165 43.12   1 33.18 ? 415 SER Z C     1 
ATOM   9970  O  O     . SER F 1 415 ? -11.342 -51.724 42.249  1 33.38 ? 415 SER Z O     1 
ATOM   9971  C  CB    . SER F 1 415 ? -8.218  -51.392 43.246  1 33.07 ? 415 SER Z CB    1 
ATOM   9972  O  OG    . SER F 1 415 ? -8.226  -51.335 41.828  1 34.65 ? 415 SER Z OG    1 
ATOM   9973  N  N     . PHE F 1 416 ? -10.581 -53.46  43.49   1 33.42 ? 416 PHE Z N     1 
ATOM   9974  C  CA    . PHE F 1 416 ? -11.448 -54.479 42.896  1 33.82 ? 416 PHE Z CA    1 
ATOM   9975  C  C     . PHE F 1 416 ? -12.919 -54.291 43.253  1 34.18 ? 416 PHE Z C     1 
ATOM   9976  O  O     . PHE F 1 416 ? -13.777 -54.398 42.384  1 34.25 ? 416 PHE Z O     1 
ATOM   9977  C  CB    . PHE F 1 416 ? -11.002 -55.881 43.32   1 33.77 ? 416 PHE Z CB    1 
ATOM   9978  C  CG    . PHE F 1 416 ? -9.654  -56.33  42.831  1 34.51 ? 416 PHE Z CG    1 
ATOM   9979  C  CD1   . PHE F 1 416 ? -9.089  -55.773 41.701  1 35.53 ? 416 PHE Z CD1   1 
ATOM   9980  C  CD2   . PHE F 1 416 ? -8.982  -57.361 43.461  1 35.42 ? 416 PHE Z CD2   1 
ATOM   9981  C  CE1   . PHE F 1 416 ? -7.863  -56.209 41.236  1 36.47 ? 416 PHE Z CE1   1 
ATOM   9982  C  CE2   . PHE F 1 416 ? -7.764  -57.804 42.986  1 36.3  ? 416 PHE Z CE2   1 
ATOM   9983  C  CZ    . PHE F 1 416 ? -7.211  -57.225 41.877  1 36.32 ? 416 PHE Z CZ    1 
ATOM   9984  N  N     . VAL F 1 417 ? -13.21  -54.044 44.535  1 34.13 ? 417 VAL Z N     1 
ATOM   9985  C  CA    . VAL F 1 417 ? -14.567 -53.871 45.037  1 34.6  ? 417 VAL Z CA    1 
ATOM   9986  C  C     . VAL F 1 417 ? -15.202 -52.566 44.549  1 35.05 ? 417 VAL Z C     1 
ATOM   9987  O  O     . VAL F 1 417 ? -16.402 -52.523 44.293  1 35.2  ? 417 VAL Z O     1 
ATOM   9988  C  CB    . VAL F 1 417 ? -14.568 -54.014 46.581  1 35.3  ? 417 VAL Z CB    1 
ATOM   9989  C  CG1   . VAL F 1 417 ? -15.891 -53.592 47.198  1 35.7  ? 417 VAL Z CG1   1 
ATOM   9990  C  CG2   . VAL F 1 417 ? -14.216 -55.44  46.986  1 35.91 ? 417 VAL Z CG2   1 
ATOM   9991  N  N     . SER F 1 418 ? -14.396 -51.522 44.359  1 35.14 ? 418 SER Z N     1 
ATOM   9992  C  CA    . SER F 1 418 ? -14.903 -50.231 43.911  1 35.74 ? 418 SER Z CA    1 
ATOM   9993  C  C     . SER F 1 418 ? -15.226 -50.159 42.427  1 36.16 ? 418 SER Z C     1 
ATOM   9994  O  O     . SER F 1 418 ? -16.108 -49.386 42.046  1 36.34 ? 418 SER Z O     1 
ATOM   9995  C  CB    . SER F 1 418 ? -13.893 -49.134 44.22   1 37.1  ? 418 SER Z CB    1 
ATOM   9996  O  OG    . SER F 1 418 ? -13.54  -49.106 45.591  1 39.45 ? 418 SER Z OG    1 
ATOM   9997  N  N     . LEU F 1 419 ? -14.479 -50.888 41.579  1 36.03 ? 419 LEU Z N     1 
ATOM   9998  C  CA    . LEU F 1 419 ? -14.654 -50.749 40.136  1 36.17 ? 419 LEU Z CA    1 
ATOM   9999  C  C     . LEU F 1 419 ? -15.154 -51.967 39.379  1 36.1  ? 419 LEU Z C     1 
ATOM   10000 O  O     . LEU F 1 419 ? -15.429 -51.826 38.186  1 36.33 ? 419 LEU Z O     1 
ATOM   10001 C  CB    . LEU F 1 419 ? -13.349 -50.273 39.512  1 36.36 ? 419 LEU Z CB    1 
ATOM   10002 C  CG    . LEU F 1 419 ? -12.965 -48.861 39.898  1 37.85 ? 419 LEU Z CG    1 
ATOM   10003 C  CD1   . LEU F 1 419 ? -11.543 -48.559 39.506  1 38.44 ? 419 LEU Z CD1   1 
ATOM   10004 C  CD2   . LEU F 1 419 ? -13.92  -47.859 39.293  1 38.59 ? 419 LEU Z CD2   1 
ATOM   10005 N  N     . SER F 1 420 ? -15.282 -53.137 40.027  1 35.65 ? 420 SER Z N     1 
ATOM   10006 C  CA    . SER F 1 420 ? -15.762 -54.318 39.311  1 35.95 ? 420 SER Z CA    1 
ATOM   10007 C  C     . SER F 1 420 ? -17.249 -54.503 39.444  1 36.31 ? 420 SER Z C     1 
ATOM   10008 O  O     . SER F 1 420 ? -17.775 -54.463 40.548  1 36.53 ? 420 SER Z O     1 
ATOM   10009 C  CB    . SER F 1 420 ? -15.092 -55.589 39.817  1 37.08 ? 420 SER Z CB    1 
ATOM   10010 O  OG    . SER F 1 420 ? -13.692 -55.464 39.98   1 38.86 ? 420 SER Z OG    1 
ATOM   10011 N  N     . ASP F 1 421 ? -17.924 -54.768 38.334  1 36.26 ? 421 ASP Z N     1 
ATOM   10012 C  CA    . ASP F 1 421 ? -19.336 -55.133 38.361  1 36.75 ? 421 ASP Z CA    1 
ATOM   10013 C  C     . ASP F 1 421 ? -19.453 -56.64  38.72   1 36.56 ? 421 ASP Z C     1 
ATOM   10014 O  O     . ASP F 1 421 ? -20.427 -57.051 39.343  1 36.56 ? 421 ASP Z O     1 
ATOM   10015 C  CB    . ASP F 1 421 ? -20.007 -54.825 37.014  1 38.99 ? 421 ASP Z CB    1 
ATOM   10016 C  CG    . ASP F 1 421 ? -20.123 -53.34  36.745  1 44.69 ? 421 ASP Z CG    1 
ATOM   10017 O  OD1   . ASP F 1 421 ? -19.123 -52.74  36.306  1 45.92 ? 421 ASP Z OD1   1 
ATOM   10018 O  OD2   . ASP F 1 421 ? -21.21  -52.773 36.992  1 47.06 ? 421 ASP Z OD2   1 
ATOM   10019 N  N     . PHE F 1 422 ? -18.454 -57.454 38.338  1 36.24 ? 422 PHE Z N     1 
ATOM   10020 C  CA    . PHE F 1 422 ? -18.412 -58.879 38.629  1 36.46 ? 422 PHE Z CA    1 
ATOM   10021 C  C     . PHE F 1 422 ? -16.995 -59.226 39.068  1 36.43 ? 422 PHE Z C     1 
ATOM   10022 O  O     . PHE F 1 422 ? -16.04  -58.798 38.425  1 36.68 ? 422 PHE Z O     1 
ATOM   10023 C  CB    . PHE F 1 422 ? -18.774 -59.694 37.376  1 36.45 ? 422 PHE Z CB    1 
ATOM   10024 C  CG    . PHE F 1 422 ? -20.013 -59.224 36.649  1 36.97 ? 422 PHE Z CG    1 
ATOM   10025 C  CD1   . PHE F 1 422 ? -21.271 -59.568 37.102  1 37.82 ? 422 PHE Z CD1   1 
ATOM   10026 C  CD2   . PHE F 1 422 ? -19.916 -58.424 35.526  1 37.43 ? 422 PHE Z CD2   1 
ATOM   10027 C  CE1   . PHE F 1 422 ? -22.408 -59.132 36.436  1 38.4  ? 422 PHE Z CE1   1 
ATOM   10028 C  CE2   . PHE F 1 422 ? -21.056 -57.988 34.866  1 38.02 ? 422 PHE Z CE2   1 
ATOM   10029 C  CZ    . PHE F 1 422 ? -22.292 -58.35  35.322  1 37.93 ? 422 PHE Z CZ    1 
ATOM   10030 N  N     . ILE F 1 423 ? -16.851 -59.969 40.167  1 36.04 ? 423 ILE Z N     1 
ATOM   10031 C  CA    . ILE F 1 423 ? -15.539 -60.386 40.655  1 36.38 ? 423 ILE Z CA    1 
ATOM   10032 C  C     . ILE F 1 423 ? -15.473 -61.898 40.603  1 37.15 ? 423 ILE Z C     1 
ATOM   10033 O  O     . ILE F 1 423 ? -16.245 -62.562 41.283  1 37.62 ? 423 ILE Z O     1 
ATOM   10034 C  CB    . ILE F 1 423 ? -15.249 -59.885 42.087  1 36.52 ? 423 ILE Z CB    1 
ATOM   10035 C  CG1   . ILE F 1 423 ? -15.259 -58.354 42.147  1 37.42 ? 423 ILE Z CG1   1 
ATOM   10036 C  CG2   . ILE F 1 423 ? -13.925 -60.45  42.595  1 36.8  ? 423 ILE Z CG2   1 
ATOM   10037 C  CD1   . ILE F 1 423 ? -15.213 -57.775 43.529  1 38.57 ? 423 ILE Z CD1   1 
ATOM   10038 N  N     . VAL F 1 424 ? -14.572 -62.449 39.797  1 37.09 ? 424 VAL Z N     1 
ATOM   10039 C  CA    . VAL F 1 424 ? -14.428 -63.888 39.666  1 37.37 ? 424 VAL Z CA    1 
ATOM   10040 C  C     . VAL F 1 424 ? -13.083 -64.317 40.175  1 37.71 ? 424 VAL Z C     1 
ATOM   10041 O  O     . VAL F 1 424 ? -12.07  -63.761 39.77   1 37.69 ? 424 VAL Z O     1 
ATOM   10042 C  CB    . VAL F 1 424 ? -14.626 -64.327 38.21   1 38.04 ? 424 VAL Z CB    1 
ATOM   10043 C  CG1   . VAL F 1 424 ? -14.445 -65.831 38.07   1 38.67 ? 424 VAL Z CG1   1 
ATOM   10044 C  CG2   . VAL F 1 424 ? -15.991 -63.901 37.711  1 38.51 ? 424 VAL Z CG2   1 
ATOM   10045 N  N     . LEU F 1 425 ? -13.062 -65.299 41.065  1 37.99 ? 425 LEU Z N     1 
ATOM   10046 C  CA    . LEU F 1 425 ? -11.817 -65.805 41.619  1 38.69 ? 425 LEU Z CA    1 
ATOM   10047 C  C     . LEU F 1 425 ? -11.64  -67.261 41.244  1 39.23 ? 425 LEU Z C     1 
ATOM   10048 O  O     . LEU F 1 425 ? -12.588 -68.025 41.295  1 39.37 ? 425 LEU Z O     1 
ATOM   10049 C  CB    . LEU F 1 425 ? -11.835 -65.713 43.157  1 38.85 ? 425 LEU Z CB    1 
ATOM   10050 C  CG    . LEU F 1 425 ? -12.279 -64.402 43.767  1 40.14 ? 425 LEU Z CG    1 
ATOM   10051 C  CD1   . LEU F 1 425 ? -12.432 -64.534 45.259  1 40.8  ? 425 LEU Z CD1   1 
ATOM   10052 C  CD2   . LEU F 1 425 ? -11.32  -63.304 43.435  1 40.65 ? 425 LEU Z CD2   1 
ATOM   10053 N  N     . ASP F 1 426 ? -10.429 -67.652 40.892  1 39.46 ? 426 ASP Z N     1 
ATOM   10054 C  CA    . ASP F 1 426 ? -10.064 -69.047 40.661  1 40.18 ? 426 ASP Z CA    1 
ATOM   10055 C  C     . ASP F 1 426 ? -8.693  -69.053 41.284  1 40.67 ? 426 ASP Z C     1 
ATOM   10056 O  O     . ASP F 1 426 ? -7.682  -68.978 40.586  1 40.98 ? 426 ASP Z O     1 
ATOM   10057 C  CB    . ASP F 1 426 ? -10.002 -69.409 39.169  1 41.76 ? 426 ASP Z CB    1 
ATOM   10058 C  CG    . ASP F 1 426 ? -9.786  -70.892 38.895  1 46.45 ? 426 ASP Z CG    1 
ATOM   10059 O  OD1   . ASP F 1 426 ? -9.57   -71.66  39.866  1 47.13 ? 426 ASP Z OD1   1 
ATOM   10060 O  OD2   . ASP F 1 426 ? -9.835  -71.288 37.716  1 48.86 ? 426 ASP Z OD2   1 
ATOM   10061 N  N     . CYS F 1 427 ? -8.669  -69.042 42.617  1 40.53 ? 427 CYS Z N     1 
ATOM   10062 C  CA    . CYS F 1 427 ? -7.451  -68.852 43.381  1 40.88 ? 427 CYS Z CA    1 
ATOM   10063 C  C     . CYS F 1 427 ? -7.002  -70.018 44.239  1 40.45 ? 427 CYS Z C     1 
ATOM   10064 O  O     . CYS F 1 427 ? -7.786  -70.546 45.027  1 40.58 ? 427 CYS Z O     1 
ATOM   10065 C  CB    . CYS F 1 427 ? -7.604  -67.601 44.244  1 42.1  ? 427 CYS Z CB    1 
ATOM   10066 S  SG    . CYS F 1 427 ? -7.992  -66.093 43.316  1 46.86 ? 427 CYS Z SG    1 
ATOM   10067 N  N     . PRO F 1 428 ? -5.683  -70.283 44.254  1 39.72 ? 428 PRO Z N     1 
ATOM   10068 C  CA    . PRO F 1 428 ? -5.151  -71.243 45.232  1 39.33 ? 428 PRO Z CA    1 
ATOM   10069 C  C     . PRO F 1 428 ? -5.261  -70.646 46.64   1 39.15 ? 428 PRO Z C     1 
ATOM   10070 O  O     . PRO F 1 428 ? -5.242  -69.423 46.797  1 39.31 ? 428 PRO Z O     1 
ATOM   10071 C  CB    . PRO F 1 428 ? -3.671  -71.372 44.849  1 40.02 ? 428 PRO Z CB    1 
ATOM   10072 C  CG    . PRO F 1 428 ? -3.529  -70.695 43.517  1 40.66 ? 428 PRO Z CG    1 
ATOM   10073 C  CD    . PRO F 1 428 ? -4.606  -69.667 43.456  1 39.13 ? 428 PRO Z CD    1 
ATOM   10074 N  N     . ILE F 1 429 ? -5.384  -71.49  47.662  1 38.69 ? 429 ILE Z N     1 
ATOM   10075 C  CA    . ILE F 1 429 ? -5.468  -71.004 49.037  1 38.56 ? 429 ILE Z CA    1 
ATOM   10076 C  C     . ILE F 1 429 ? -4.227  -71.451 49.779  1 38.32 ? 429 ILE Z C     1 
ATOM   10077 O  O     . ILE F 1 429 ? -3.924  -72.64  49.776  1 38.49 ? 429 ILE Z O     1 
ATOM   10078 C  CB    . ILE F 1 429 ? -6.76   -71.491 49.734  1 39.02 ? 429 ILE Z CB    1 
ATOM   10079 C  CG1   . ILE F 1 429 ? -8.008  -71.141 48.91   1 39.9  ? 429 ILE Z CG1   1 
ATOM   10080 C  CG2   . ILE F 1 429 ? -6.856  -70.939 51.149  1 39.48 ? 429 ILE Z CG2   1 
ATOM   10081 C  CD1   . ILE F 1 429 ? -8.222  -69.669 48.67   1 41.04 ? 429 ILE Z CD1   1 
ATOM   10082 N  N     . ILE F 1 430 ? -3.498  -70.511 50.407  1 37.85 ? 430 ILE Z N     1 
ATOM   10083 C  CA    . ILE F 1 430 ? -2.293  -70.811 51.187  1 37.87 ? 430 ILE Z CA    1 
ATOM   10084 C  C     . ILE F 1 430 ? -2.606  -71.839 52.284  1 38.01 ? 430 ILE Z C     1 
ATOM   10085 O  O     . ILE F 1 430 ? -3.45   -71.588 53.144  1 37.87 ? 430 ILE Z O     1 
ATOM   10086 C  CB    . ILE F 1 430 ? -1.702  -69.516 51.794  1 38.06 ? 430 ILE Z CB    1 
ATOM   10087 C  CG1   . ILE F 1 430 ? -1.432  -68.453 50.719  1 38.75 ? 430 ILE Z CG1   1 
ATOM   10088 C  CG2   . ILE F 1 430 ? -0.459  -69.817 52.63   1 38.44 ? 430 ILE Z CG2   1 
ATOM   10089 C  CD1   . ILE F 1 430 ? -0.44   -68.845 49.723  1 39.98 ? 430 ILE Z CD1   1 
ATOM   10090 N  N     . GLY F 1 431 ? -1.981  -73.006 52.191  1 38.03 ? 431 GLY Z N     1 
ATOM   10091 C  CA    . GLY F 1 431 ? -2.209  -74.094 53.137  1 38.42 ? 431 GLY Z CA    1 
ATOM   10092 C  C     . GLY F 1 431 ? -3.193  -75.149 52.667  1 38.4  ? 431 GLY Z C     1 
ATOM   10093 O  O     . GLY F 1 431 ? -3.448  -76.115 53.383  1 38.09 ? 431 GLY Z O     1 
ATOM   10094 N  N     . GLU F 1 432 ? -3.773  -74.969 51.475  1 38.62 ? 432 GLU Z N     1 
ATOM   10095 C  CA    . GLU F 1 432 ? -4.725  -75.915 50.905  1 39.42 ? 432 GLU Z CA    1 
ATOM   10096 C  C     . GLU F 1 432 ? -4.228  -76.462 49.566  1 39.89 ? 432 GLU Z C     1 
ATOM   10097 O  O     . GLU F 1 432 ? -3.414  -75.828 48.899  1 39.91 ? 432 GLU Z O     1 
ATOM   10098 C  CB    . GLU F 1 432 ? -6.113  -75.286 50.773  1 42.06 ? 432 GLU Z CB    1 
ATOM   10099 C  CG    . GLU F 1 432 ? -6.677  -74.843 52.109  1 47.74 ? 432 GLU Z CG    1 
ATOM   10100 C  CD    . GLU F 1 432 ? -8.178  -74.654 52.112  1 54.72 ? 432 GLU Z CD    1 
ATOM   10101 O  OE1   . GLU F 1 432 ? -8.707  -74.106 51.118  1 55.54 ? 432 GLU Z OE1   1 
ATOM   10102 O  OE2   . GLU F 1 432 ? -8.829  -75.07  53.099  1 57.26 ? 432 GLU Z OE2   1 
ATOM   10103 N  N     . SER F 1 433 ? -4.706  -77.647 49.176  1 40.17 ? 433 SER Z N     1 
ATOM   10104 C  CA    . SER F 1 433 ? -4.233  -78.304 47.957  1 40.8  ? 433 SER Z CA    1 
ATOM   10105 C  C     . SER F 1 433 ? -4.846  -77.812 46.652  1 40.94 ? 433 SER Z C     1 
ATOM   10106 O  O     . SER F 1 433 ? -4.175  -77.893 45.628  1 41.25 ? 433 SER Z O     1 
ATOM   10107 C  CB    . SER F 1 433 ? -4.407  -79.817 48.05   1 42.49 ? 433 SER Z CB    1 
ATOM   10108 O  OG    . SER F 1 433 ? -4.044  -80.348 49.316  1 45.17 ? 433 SER Z OG    1 
ATOM   10109 N  N     . TYR F 1 434 ? -6.122  -77.389 46.649  1 40.66 ? 434 TYR Z N     1 
ATOM   10110 C  CA    . TYR F 1 434 ? -6.77   -76.978 45.4    1 40.85 ? 434 TYR Z CA    1 
ATOM   10111 C  C     . TYR F 1 434 ? -7.421  -75.583 45.469  1 40.58 ? 434 TYR Z C     1 
ATOM   10112 O  O     . TYR F 1 434 ? -7.555  -75.003 46.545  1 40.4  ? 434 TYR Z O     1 
ATOM   10113 C  CB    . TYR F 1 434 ? -7.759  -78.056 44.908  1 40.97 ? 434 TYR Z CB    1 
ATOM   10114 C  CG    . TYR F 1 434 ? -7.066  -79.365 44.616  1 41.76 ? 434 TYR Z CG    1 
ATOM   10115 C  CD1   . TYR F 1 434 ? -6.882  -80.31  45.612  1 42.71 ? 434 TYR Z CD1   1 
ATOM   10116 C  CD2   . TYR F 1 434 ? -6.523  -79.624 43.367  1 42.62 ? 434 TYR Z CD2   1 
ATOM   10117 C  CE1   . TYR F 1 434 ? -6.178  -81.481 45.375  1 43.58 ? 434 TYR Z CE1   1 
ATOM   10118 C  CE2   . TYR F 1 434 ? -5.83   -80.8   43.113  1 43.53 ? 434 TYR Z CE2   1 
ATOM   10119 C  CZ    . TYR F 1 434 ? -5.654  -81.724 44.125  1 44.46 ? 434 TYR Z CZ    1 
ATOM   10120 O  OH    . TYR F 1 434 ? -4.976  -82.892 43.891  1 46.07 ? 434 TYR Z OH    1 
ATOM   10121 N  N     . ASN F 1 435 ? -7.762  -75.032 44.29   1 40.23 ? 435 ASN Z N     1 
ATOM   10122 C  CA    . ASN F 1 435 ? -8.341  -73.703 44.124  1 40.23 ? 435 ASN Z CA    1 
ATOM   10123 C  C     . ASN F 1 435 ? -9.776  -73.558 44.595  1 39.74 ? 435 ASN Z C     1 
ATOM   10124 O  O     . ASN F 1 435 ? -10.526 -74.533 44.685  1 39.76 ? 435 ASN Z O     1 
ATOM   10125 C  CB    . ASN F 1 435 ? -8.263  -73.272 42.667  1 41.55 ? 435 ASN Z CB    1 
ATOM   10126 C  CG    . ASN F 1 435 ? -6.889  -72.885 42.235  1 45.07 ? 435 ASN Z CG    1 
ATOM   10127 O  OD1   . ASN F 1 435 ? -5.886  -73.312 42.813  1 46.13 ? 435 ASN Z OD1   1 
ATOM   10128 N  ND2   . ASN F 1 435 ? -6.818  -72.076 41.191  1 46.03 ? 435 ASN Z ND2   1 
ATOM   10129 N  N     . GLU F 1 436 ? -10.154 -72.304 44.863  1 39.04 ? 436 GLU Z N     1 
ATOM   10130 C  CA    . GLU F 1 436 ? -11.488 -71.909 45.254  1 38.76 ? 436 GLU Z CA    1 
ATOM   10131 C  C     . GLU F 1 436 ? -12.068 -71.075 44.135  1 38.13 ? 436 GLU Z C     1 
ATOM   10132 O  O     . GLU F 1 436 ? -11.405 -70.154 43.662  1 38.16 ? 436 GLU Z O     1 
ATOM   10133 C  CB    . GLU F 1 436 ? -11.43  -71.052 46.521  1 40.86 ? 436 GLU Z CB    1 
ATOM   10134 C  CG    . GLU F 1 436 ? -11.248 -71.858 47.79   1 45.13 ? 436 GLU Z CG    1 
ATOM   10135 C  CD    . GLU F 1 436 ? -12.455 -72.68  48.184  1 50.84 ? 436 GLU Z CD    1 
ATOM   10136 O  OE1   . GLU F 1 436 ? -12.602 -73.812 47.676  1 51.67 ? 436 GLU Z OE1   1 
ATOM   10137 O  OE2   . GLU F 1 436 ? -13.256 -72.194 49.011  1 53.47 ? 436 GLU Z OE2   1 
ATOM   10138 N  N     . PHE F 1 437 ? -13.29  -71.391 43.702  1 37.55 ? 437 PHE Z N     1 
ATOM   10139 C  CA    . PHE F 1 437 ? -13.951 -70.601 42.673  1 37.7  ? 437 PHE Z CA    1 
ATOM   10140 C  C     . PHE F 1 437 ? -15.062 -69.765 43.301  1 37.64 ? 437 PHE Z C     1 
ATOM   10141 O  O     . PHE F 1 437 ? -15.909 -70.301 44.011  1 37.91 ? 437 PHE Z O     1 
ATOM   10142 C  CB    . PHE F 1 437 ? -14.493 -71.46  41.506  1 37.8  ? 437 PHE Z CB    1 
ATOM   10143 C  CG    . PHE F 1 437 ? -15.441 -70.693 40.604  1 38.74 ? 437 PHE Z CG    1 
ATOM   10144 C  CD1   . PHE F 1 437 ? -14.969 -69.72  39.742  1 39.54 ? 437 PHE Z CD1   1 
ATOM   10145 C  CD2   . PHE F 1 437 ? -16.811 -70.862 40.708  1 39.79 ? 437 PHE Z CD2   1 
ATOM   10146 C  CE1   . PHE F 1 437 ? -15.843 -68.961 38.978  1 40.3  ? 437 PHE Z CE1   1 
ATOM   10147 C  CE2   . PHE F 1 437 ? -17.682 -70.105 39.934  1 40.55 ? 437 PHE Z CE2   1 
ATOM   10148 C  CZ    . PHE F 1 437 ? -17.192 -69.161 39.074  1 40.23 ? 437 PHE Z CZ    1 
ATOM   10149 N  N     . ARG F 1 438 ? -15.084 -68.461 43.003  1 37.25 ? 438 ARG Z N     1 
ATOM   10150 C  CA    . ARG F 1 438 ? -16.12  -67.56  43.492  1 37.4  ? 438 ARG Z CA    1 
ATOM   10151 C  C     . ARG F 1 438 ? -16.6   -66.651 42.367  1 37.65 ? 438 ARG Z C     1 
ATOM   10152 O  O     . ARG F 1 438 ? -15.798 -66.191 41.562  1 38.02 ? 438 ARG Z O     1 
ATOM   10153 C  CB    . ARG F 1 438 ? -15.583 -66.678 44.627  1 38.2  ? 438 ARG Z CB    1 
ATOM   10154 C  CG    . ARG F 1 438 ? -15.07  -67.436 45.818  1 40.29 ? 438 ARG Z CG    1 
ATOM   10155 C  CD    . ARG F 1 438 ? -16.168 -67.869 46.757  1 42.66 ? 438 ARG Z CD    1 
ATOM   10156 N  NE    . ARG F 1 438 ? -15.53  -68.415 47.934  1 44.24 ? 438 ARG Z NE    1 
ATOM   10157 C  CZ    . ARG F 1 438 ? -15.333 -69.702 48.177  1 45.05 ? 438 ARG Z CZ    1 
ATOM   10158 N  NH1   . ARG F 1 438 ? -15.823 -70.621 47.361  1 43.91 ? 438 ARG Z NH1   1 
ATOM   10159 N  NH2   . ARG F 1 438 ? -14.705 -70.08  49.282  1 44.86 ? 438 ARG Z NH2   1 
ATOM   10160 N  N     . LEU F 1 439 ? -17.898 -66.365 42.327  1 37.38 ? 439 LEU Z N     1 
ATOM   10161 C  CA    . LEU F 1 439 ? -18.466 -65.415 41.377  1 37.51 ? 439 LEU Z CA    1 
ATOM   10162 C  C     . LEU F 1 439 ? -19.272 -64.428 42.2    1 37.32 ? 439 LEU Z C     1 
ATOM   10163 O  O     . LEU F 1 439 ? -20.282 -64.792 42.798  1 37.74 ? 439 LEU Z O     1 
ATOM   10164 C  CB    . LEU F 1 439 ? -19.343 -66.101 40.321  1 37.86 ? 439 LEU Z CB    1 
ATOM   10165 C  CG    . LEU F 1 439 ? -20.222 -65.185 39.452  1 39.29 ? 439 LEU Z CG    1 
ATOM   10166 C  CD1   . LEU F 1 439 ? -19.414 -64.121 38.749  1 39.77 ? 439 LEU Z CD1   1 
ATOM   10167 C  CD2   . LEU F 1 439 ? -20.94  -65.983 38.42   1 40.05 ? 439 LEU Z CD2   1 
ATOM   10168 N  N     . ILE F 1 440 ? -18.8   -63.193 42.275  1 36.64 ? 440 ILE Z N     1 
ATOM   10169 C  CA    . ILE F 1 440 ? -19.446 -62.163 43.067  1 36.63 ? 440 ILE Z CA    1 
ATOM   10170 C  C     . ILE F 1 440 ? -20.139 -61.137 42.188  1 36.83 ? 440 ILE Z C     1 
ATOM   10171 O  O     . ILE F 1 440 ? -19.474 -60.458 41.421  1 37.08 ? 440 ILE Z O     1 
ATOM   10172 C  CB    . ILE F 1 440 ? -18.406 -61.485 43.992  1 36.87 ? 440 ILE Z CB    1 
ATOM   10173 C  CG1   . ILE F 1 440 ? -17.642 -62.53  44.847  1 37.46 ? 440 ILE Z CG1   1 
ATOM   10174 C  CG2   . ILE F 1 440 ? -19.069 -60.415 44.851  1 37.36 ? 440 ILE Z CG2   1 
ATOM   10175 C  CD1   . ILE F 1 440 ? -16.577 -61.972 45.796  1 38.42 ? 440 ILE Z CD1   1 
ATOM   10176 N  N     . ILE F 1 441 ? -21.465 -61.014 42.295  1 36.81 ? 441 ILE Z N     1 
ATOM   10177 C  CA    . ILE F 1 441 ? -22.211 -60.01  41.542  1 37.41 ? 441 ILE Z CA    1 
ATOM   10178 C  C     . ILE F 1 441 ? -22.116 -58.713 42.346  1 38.14 ? 441 ILE Z C     1 
ATOM   10179 O  O     . ILE F 1 441 ? -22.877 -58.483 43.283  1 38.39 ? 441 ILE Z O     1 
ATOM   10180 C  CB    . ILE F 1 441 ? -23.665 -60.461 41.301  1 37.9  ? 441 ILE Z CB    1 
ATOM   10181 C  CG1   . ILE F 1 441 ? -23.7   -61.847 40.64   1 39.04 ? 441 ILE Z CG1   1 
ATOM   10182 C  CG2   . ILE F 1 441 ? -24.439 -59.434 40.484  1 38.34 ? 441 ILE Z CG2   1 
ATOM   10183 C  CD1   . ILE F 1 441 ? -23.059 -61.915 39.266  1 40.48 ? 441 ILE Z CD1   1 
ATOM   10184 N  N     . ASN F 1 442 ? -21.133 -57.894 42.003  1 38.42 ? 442 ASN Z N     1 
ATOM   10185 C  CA    . ASN F 1 442 ? -20.799 -56.672 42.711  1 39.32 ? 442 ASN Z CA    1 
ATOM   10186 C  C     . ASN F 1 442 ? -21.428 -55.386 42.123  1 40.28 ? 442 ASN Z C     1 
ATOM   10187 O  O     . ASN F 1 442 ? -21.08  -54.288 42.559  1 40.45 ? 442 ASN Z O     1 
ATOM   10188 C  CB    . ASN F 1 442 ? -19.278 -56.571 42.739  1 40.37 ? 442 ASN Z CB    1 
ATOM   10189 C  CG    . ASN F 1 442 ? -18.728 -55.68  43.804  1 43.84 ? 442 ASN Z CG    1 
ATOM   10190 O  OD1   . ASN F 1 442 ? -19.011 -55.837 44.99   1 45.18 ? 442 ASN Z OD1   1 
ATOM   10191 N  ND2   . ASN F 1 442 ? -17.929 -54.721 43.393  1 44.57 ? 442 ASN Z ND2   1 
ATOM   10192 N  N     . LYS F 1 443 ? -22.35  -55.52  41.15   1 40.63 ? 443 LYS Z N     1 
ATOM   10193 C  CA    . LYS F 1 443 ? -22.996 -54.386 40.479  1 41.47 ? 443 LYS Z CA    1 
ATOM   10194 C  C     . LYS F 1 443 ? -23.555 -53.297 41.415  1 42.14 ? 443 LYS Z C     1 
ATOM   10195 O  O     . LYS F 1 443 ? -23.177 -52.131 41.271  1 42.38 ? 443 LYS Z O     1 
ATOM   10196 C  CB    . LYS F 1 443 ? -24.091 -54.868 39.518  1 43.33 ? 443 LYS Z CB    1 
ATOM   10197 C  CG    . LYS F 1 443 ? -23.571 -55.211 38.144  1 47.66 ? 443 LYS Z CG    1 
ATOM   10198 C  CD    . LYS F 1 443 ? -24.704 -55.351 37.148  1 52.65 ? 443 LYS Z CD    1 
ATOM   10199 C  CE    . LYS F 1 443 ? -24.206 -55.349 35.719  1 56.87 ? 443 LYS Z CE    1 
ATOM   10200 N  NZ    . LYS F 1 443 ? -23.696 -54.014 35.293  1 59.11 ? 443 LYS Z NZ    1 
ATOM   10201 N  N     . ASN F 1 444 ? -24.446 -53.658 42.356  1 42.24 ? 444 ASN Z N     1 
ATOM   10202 C  CA    . ASN F 1 444 ? -25.031 -52.665 43.258  1 42.84 ? 444 ASN Z CA    1 
ATOM   10203 C  C     . ASN F 1 444 ? -24.016 -52.083 44.241  1 42.91 ? 444 ASN Z C     1 
ATOM   10204 O  O     . ASN F 1 444 ? -24.108 -50.905 44.601  1 43.06 ? 444 ASN Z O     1 
ATOM   10205 C  CB    . ASN F 1 444 ? -26.255 -53.218 43.987  1 44.15 ? 444 ASN Z CB    1 
ATOM   10206 C  CG    . ASN F 1 444 ? -27.153 -52.143 44.564  1 48.06 ? 444 ASN Z CG    1 
ATOM   10207 O  OD1   . ASN F 1 444 ? -27.725 -52.296 45.651  1 49.6  ? 444 ASN Z OD1   1 
ATOM   10208 N  ND2   . ASN F 1 444 ? -27.304 -51.022 43.858  1 48.86 ? 444 ASN Z ND2   1 
ATOM   10209 N  N     . ASN F 1 445 ? -23.039 -52.895 44.65   1 42.53 ? 445 ASN Z N     1 
ATOM   10210 C  CA    . ASN F 1 445 ? -22.002 -52.448 45.563  1 42.74 ? 445 ASN Z CA    1 
ATOM   10211 C  C     . ASN F 1 445 ? -21.109 -51.403 44.897  1 42.92 ? 445 ASN Z C     1 
ATOM   10212 O  O     . ASN F 1 445 ? -20.802 -50.377 45.502  1 42.97 ? 445 ASN Z O     1 
ATOM   10213 C  CB    . ASN F 1 445 ? -21.181 -53.633 46.031  1 43.77 ? 445 ASN Z CB    1 
ATOM   10214 C  CG    . ASN F 1 445 ? -20.281 -53.296 47.18   1 47.21 ? 445 ASN Z CG    1 
ATOM   10215 O  OD1   . ASN F 1 445 ? -20.542 -52.374 47.96   1 48.87 ? 445 ASN Z OD1   1 
ATOM   10216 N  ND2   . ASN F 1 445 ? -19.21  -54.047 47.32   1 47.56 ? 445 ASN Z ND2   1 
ATOM   10217 N  N     . LYS F 1 446 ? -20.736 -51.641 43.633  1 42.87 ? 446 LYS Z N     1 
ATOM   10218 C  CA    . LYS F 1 446 ? -19.908 -50.719 42.864  1 43.31 ? 446 LYS Z CA    1 
ATOM   10219 C  C     . LYS F 1 446 ? -20.619 -49.378 42.709  1 43.95 ? 446 LYS Z C     1 
ATOM   10220 O  O     . LYS F 1 446 ? -20.002 -48.334 42.917  1 44.05 ? 446 LYS Z O     1 
ATOM   10221 C  CB    . LYS F 1 446 ? -19.567 -51.323 41.486  1 44.46 ? 446 LYS Z CB    1 
ATOM   10222 C  CG    . LYS F 1 446 ? -18.958 -50.325 40.506  1 47.07 ? 446 LYS Z CG    1 
ATOM   10223 C  CD    . LYS F 1 446 ? -18.623 -50.943 39.171  1 49.95 ? 446 LYS Z CD    1 
ATOM   10224 C  CE    . LYS F 1 446 ? -18.151 -49.889 38.205  1 52.22 ? 446 LYS Z CE    1 
ATOM   10225 N  NZ    . LYS F 1 446 ? -17.672 -50.482 36.934  1 53.54 ? 446 LYS Z NZ    1 
ATOM   10226 N  N     . GLU F 1 447 ? -21.921 -49.41  42.382  1 44.27 ? 447 GLU Z N     1 
ATOM   10227 C  CA    . GLU F 1 447 ? -22.718 -48.197 42.208  1 45.12 ? 447 GLU Z CA    1 
ATOM   10228 C  C     . GLU F 1 447 ? -22.707 -47.328 43.467  1 45.2  ? 447 GLU Z C     1 
ATOM   10229 O  O     . GLU F 1 447 ? -22.526 -46.114 43.383  1 45.43 ? 447 GLU Z O     1 
ATOM   10230 C  CB    . GLU F 1 447 ? -24.162 -48.55  41.818  1 48.06 ? 447 GLU Z CB    1 
ATOM   10231 C  CG    . GLU F 1 447 ? -24.32  -48.98  40.371  1 53.86 ? 447 GLU Z CG    1 
ATOM   10232 C  CD    . GLU F 1 447 ? -25.719 -49.41  39.972  1 61.41 ? 447 GLU Z CD    1 
ATOM   10233 O  OE1   . GLU F 1 447 ? -26.618 -49.422 40.845  1 63.14 ? 447 GLU Z OE1   1 
ATOM   10234 O  OE2   . GLU F 1 447 ? -25.917 -49.74  38.78   1 63.96 ? 447 GLU Z OE2   1 
ATOM   10235 N  N     . SER F 1 448 ? -22.858 -47.966 44.636  1 44.82 ? 448 SER Z N     1 
ATOM   10236 C  CA    . SER F 1 448 ? -22.864 -47.265 45.909  1 44.89 ? 448 SER Z CA    1 
ATOM   10237 C  C     . SER F 1 448 ? -21.505 -46.658 46.219  1 44.63 ? 448 SER Z C     1 
ATOM   10238 O  O     . SER F 1 448 ? -21.438 -45.533 46.707  1 44.72 ? 448 SER Z O     1 
ATOM   10239 C  CB    . SER F 1 448 ? -23.288 -48.209 47.024  1 46.39 ? 448 SER Z CB    1 
ATOM   10240 O  OG    . SER F 1 448 ? -24.586 -48.711 46.755  1 48.93 ? 448 SER Z OG    1 
ATOM   10241 N  N     . ILE F 1 449 ? -20.423 -47.382 45.917  1 44.18 ? 449 ILE Z N     1 
ATOM   10242 C  CA    . ILE F 1 449 ? -19.08  -46.875 46.174  1 44.31 ? 449 ILE Z CA    1 
ATOM   10243 C  C     . ILE F 1 449 ? -18.759 -45.663 45.314  1 44.57 ? 449 ILE Z C     1 
ATOM   10244 O  O     . ILE F 1 449 ? -18.168 -44.706 45.815  1 44.8  ? 449 ILE Z O     1 
ATOM   10245 C  CB    . ILE F 1 449 ? -18.028 -47.992 46.047  1 44.66 ? 449 ILE Z CB    1 
ATOM   10246 C  CG1   . ILE F 1 449 ? -18.255 -49.06  47.118  1 45.46 ? 449 ILE Z CG1   1 
ATOM   10247 C  CG2   . ILE F 1 449 ? -16.614 -47.43  46.145  1 45.13 ? 449 ILE Z CG2   1 
ATOM   10248 C  CD1   . ILE F 1 449 ? -17.556 -50.321 46.846  1 46.67 ? 449 ILE Z CD1   1 
ATOM   10249 N  N     . LEU F 1 450 ? -19.2   -45.661 44.044  1 44.47 ? 450 LEU Z N     1 
ATOM   10250 C  CA    . LEU F 1 450 ? -18.95  -44.523 43.154  1 44.82 ? 450 LEU Z CA    1 
ATOM   10251 C  C     . LEU F 1 450 ? -19.65  -43.224 43.588  1 45.64 ? 450 LEU Z C     1 
ATOM   10252 O  O     . LEU F 1 450 ? -19.284 -42.15  43.115  1 45.96 ? 450 LEU Z O     1 
ATOM   10253 C  CB    . LEU F 1 450 ? -19.279 -44.855 41.692  1 44.58 ? 450 LEU Z CB    1 
ATOM   10254 C  CG    . LEU F 1 450 ? -18.486 -45.992 41.064  1 45.54 ? 450 LEU Z CG    1 
ATOM   10255 C  CD1   . LEU F 1 450 ? -18.891 -46.194 39.628  1 46.12 ? 450 LEU Z CD1   1 
ATOM   10256 C  CD2   . LEU F 1 450 ? -17.007 -45.729 41.122  1 45.85 ? 450 LEU Z CD2   1 
ATOM   10257 N  N     . ARG F 1 451 ? -20.636 -43.308 44.487  1 45.75 ? 451 ARG Z N     1 
ATOM   10258 C  CA    . ARG F 1 451 ? -21.318 -42.115 44.979  1 46.41 ? 451 ARG Z CA    1 
ATOM   10259 C  C     . ARG F 1 451 ? -20.971 -41.808 46.442  1 46.84 ? 451 ARG Z C     1 
ATOM   10260 O  O     . ARG F 1 451 ? -21.692 -41.053 47.086  1 47.15 ? 451 ARG Z O     1 
ATOM   10261 C  CB    . ARG F 1 451 ? -22.839 -42.24  44.79   1 48.07 ? 451 ARG Z CB    1 
ATOM   10262 C  CG    . ARG F 1 451 ? -23.245 -42.83  43.449  1 51.89 ? 451 ARG Z CG    1 
ATOM   10263 C  CD    . ARG F 1 451 ? -24.666 -42.513 43.039  1 55.93 ? 451 ARG Z CD    1 
ATOM   10264 N  NE    . ARG F 1 451 ? -24.725 -41.437 42.05   1 59.81 ? 451 ARG Z NE    1 
ATOM   10265 C  CZ    . ARG F 1 451 ? -24.625 -41.618 40.736  1 62.79 ? 451 ARG Z CZ    1 
ATOM   10266 N  NH1   . ARG F 1 451 ? -24.678 -40.579 39.912  1 62.72 ? 451 ARG Z NH1   1 
ATOM   10267 N  NH2   . ARG F 1 451 ? -24.478 -42.842 40.234  1 62.88 ? 451 ARG Z NH2   1 
ATOM   10268 N  N     . LYS F 1 452 ? -19.872 -42.368 46.968  1 46.8  ? 452 LYS Z N     1 
ATOM   10269 C  CA    . LYS F 1 452 ? -19.491 -42.166 48.361  1 47.22 ? 452 LYS Z CA    1 
ATOM   10270 C  C     . LYS F 1 452 ? -18.547 -40.973 48.56   1 47.48 ? 452 LYS Z C     1 
ATOM   10271 O  O     . LYS F 1 452 ? -17.542 -40.868 47.863  1 47.58 ? 452 LYS Z O     1 
ATOM   10272 C  CB    . LYS F 1 452 ? -18.864 -43.454 48.925  1 48.93 ? 452 LYS Z CB    1 
ATOM   10273 C  CG    . LYS F 1 452 ? -18.821 -43.501 50.448  1 52.57 ? 452 LYS Z CG    1 
ATOM   10274 C  CD    . LYS F 1 452 ? -18.455 -44.885 50.976  1 56.62 ? 452 LYS Z CD    1 
ATOM   10275 C  CE    . LYS F 1 452 ? -18.547 -44.944 52.485  1 60.19 ? 452 LYS Z CE    1 
ATOM   10276 N  NZ    . LYS F 1 452 ? -18.354 -46.323 53.011  1 62.16 ? 452 LYS Z NZ    1 
ATOM   10277 N  N     . THR F 1 453 ? -18.888 -40.065 49.502  1 47.4  ? 453 THR Z N     1 
ATOM   10278 C  CA    . THR F 1 453 ? -18.077 -38.898 49.875  1 47.7  ? 453 THR Z CA    1 
ATOM   10279 C  C     . THR F 1 453 ? -18.05  -38.771 51.398  1 47.95 ? 453 THR Z C     1 
ATOM   10280 O  O     . THR F 1 453 ? -19.087 -38.945 52.036  1 47.98 ? 453 THR Z O     1 
ATOM   10281 C  CB    . THR F 1 453 ? -18.626 -37.586 49.28   1 48.81 ? 453 THR Z CB    1 
ATOM   10282 O  OG1   . THR F 1 453 ? -19.917 -37.306 49.808  1 49.54 ? 453 THR Z OG1   1 
ATOM   10283 C  CG2   . THR F 1 453 ? -18.655 -37.581 47.764  1 49.35 ? 453 THR Z CG2   1 
ATOM   10284 N  N     . SER F 1 454 ? -16.889 -38.441 51.983  1 48.07 ? 454 SER Z N     1 
ATOM   10285 C  CA    . SER F 1 454 ? -16.795 -38.273 53.437  1 48.74 ? 454 SER Z CA    1 
ATOM   10286 C  C     . SER F 1 454 ? -17.436 -36.947 53.903  1 49.19 ? 454 SER Z C     1 
ATOM   10287 O  O     . SER F 1 454 ? -17.716 -36.081 53.075  1 49.42 ? 454 SER Z O     1 
ATOM   10288 C  CB    . SER F 1 454 ? -15.347 -38.397 53.909  1 50.05 ? 454 SER Z CB    1 
ATOM   10289 O  OG    . SER F 1 454 ? -14.532 -37.344 53.426  1 52.4  ? 454 SER Z OG    1 
ATOM   10290 N  N     . LYS F 1 455 ? -17.712 -36.816 55.213  1 49.18 ? 455 LYS Z N     1 
ATOM   10291 C  CA    . LYS F 1 455 ? -18.339 -35.634 55.825  1 49.65 ? 455 LYS Z CA    1 
ATOM   10292 C  C     . LYS F 1 455 ? -17.739 -34.301 55.351  1 49.54 ? 455 LYS Z C     1 
ATOM   10293 O  O     . LYS F 1 455 ? -16.526 -34.129 55.403  1 49.88 ? 455 LYS Z O     1 
ATOM   10294 C  CB    . LYS F 1 455 ? -18.253 -35.735 57.359  1 51.77 ? 455 LYS Z CB    1 
ATOM   10295 C  CG    . LYS F 1 455 ? -18.84  -34.543 58.108  1 56.38 ? 455 LYS Z CG    1 
ATOM   10296 C  CD    . LYS F 1 455 ? -18.622 -34.669 59.611  1 61.32 ? 455 LYS Z CD    1 
ATOM   10297 C  CE    . LYS F 1 455 ? -19.277 -33.554 60.39   1 65.43 ? 455 LYS Z CE    1 
ATOM   10298 N  NZ    . LYS F 1 455 ? -18.99  -33.666 61.847  1 67.79 ? 455 LYS Z NZ    1 
ATOM   10299 N  N     . GLN F 1 456 ? -18.583 -33.367 54.892  1 48.89 ? 456 GLN Z N     1 
ATOM   10300 C  CA    . GLN F 1 456 ? -18.117 -32.06  54.43   1 48.86 ? 456 GLN Z CA    1 
ATOM   10301 C  C     . GLN F 1 456 ? -17.709 -31.174 55.604  1 48.2  ? 456 GLN Z C     1 
ATOM   10302 O  O     . GLN F 1 456 ? -18.55  -30.844 56.44   1 48.49 ? 456 GLN Z O     1 
ATOM   10303 C  CB    . GLN F 1 456 ? -19.219 -31.355 53.634  1 50.84 ? 456 GLN Z CB    1 
ATOM   10304 C  CG    . GLN F 1 456 ? -19.728 -32.176 52.472  1 54.79 ? 456 GLN Z CG    1 
ATOM   10305 C  CD    . GLN F 1 456 ? -18.685 -32.325 51.396  1 59.33 ? 456 GLN Z CD    1 
ATOM   10306 O  OE1   . GLN F 1 456 ? -17.977 -31.372 51.042  1 60.68 ? 456 GLN Z OE1   1 
ATOM   10307 N  NE2   . GLN F 1 456 ? -18.576 -33.528 50.849  1 59.83 ? 456 GLN Z NE2   1 
ATOM   10308 N  N     . GLN F 1 457 ? -16.432 -30.772 55.659  1 47.06 ? 457 GLN Z N     1 
ATOM   10309 C  CA    . GLN F 1 457 ? -15.921 -29.92  56.727  1 46.39 ? 457 GLN Z CA    1 
ATOM   10310 C  C     . GLN F 1 457 ? -14.605 -29.261 56.343  1 45.22 ? 457 GLN Z C     1 
ATOM   10311 O  O     . GLN F 1 457 ? -13.807 -29.834 55.607  1 45.07 ? 457 GLN Z O     1 
ATOM   10312 C  CB    . GLN F 1 457 ? -15.772 -30.696 58.049  1 48.09 ? 457 GLN Z CB    1 
ATOM   10313 C  CG    . GLN F 1 457 ? -14.776 -31.847 57.985  1 51.39 ? 457 GLN Z CG    1 
ATOM   10314 C  CD    . GLN F 1 457 ? -14.641 -32.568 59.301  1 55.21 ? 457 GLN Z CD    1 
ATOM   10315 O  OE1   . GLN F 1 457 ? -14.66  -33.8   59.358  1 56.85 ? 457 GLN Z OE1   1 
ATOM   10316 N  NE2   . GLN F 1 457 ? -14.497 -31.821 60.388  1 55.38 ? 457 GLN Z NE2   1 
ATOM   10317 N  N     . ASN F 1 458 ? -14.386 -28.047 56.839  1 44.37 ? 458 ASN Z N     1 
ATOM   10318 C  CA    . ASN F 1 458 ? -13.167 -27.297 56.562  1 43.93 ? 458 ASN Z CA    1 
ATOM   10319 C  C     . ASN F 1 458 ? -11.98  -27.906 57.295  1 42.9  ? 458 ASN Z C     1 
ATOM   10320 O  O     . ASN F 1 458 ? -12.137 -28.46  58.384  1 43.26 ? 458 ASN Z O     1 
ATOM   10321 C  CB    . ASN F 1 458 ? -13.332 -25.834 56.976  1 45.32 ? 458 ASN Z CB    1 
ATOM   10322 C  CG    . ASN F 1 458 ? -14.526 -25.13  56.371  1 48.84 ? 458 ASN Z CG    1 
ATOM   10323 O  OD1   . ASN F 1 458 ? -15.127 -24.243 56.992  1 50.2  ? 458 ASN Z OD1   1 
ATOM   10324 N  ND2   . ASN F 1 458 ? -14.889 -25.485 55.142  1 49.54 ? 458 ASN Z ND2   1 
ATOM   10325 N  N     . ILE F 1 459 ? -10.79  -27.813 56.698  1 41.45 ? 459 ILE Z N     1 
ATOM   10326 C  CA    . ILE F 1 459 ? -9.581  -28.35  57.311  1 40.54 ? 459 ILE Z CA    1 
ATOM   10327 C  C     . ILE F 1 459 ? -8.467  -27.307 57.356  1 39.4  ? 459 ILE Z C     1 
ATOM   10328 O  O     . ILE F 1 459 ? -8.246  -26.586 56.389  1 39.45 ? 459 ILE Z O     1 
ATOM   10329 C  CB    . ILE F 1 459 ? -9.132  -29.663 56.614  1 40.97 ? 459 ILE Z CB    1 
ATOM   10330 C  CG1   . ILE F 1 459 ? -10.14  -30.796 56.866  1 41.95 ? 459 ILE Z CG1   1 
ATOM   10331 C  CG2   . ILE F 1 459 ? -7.716  -30.084 57.033  1 41.41 ? 459 ILE Z CG2   1 
ATOM   10332 C  CD1   . ILE F 1 459 ? -9.938  -31.995 56.023  1 43.17 ? 459 ILE Z CD1   1 
ATOM   10333 N  N     . LEU F 1 460 ? -7.782  -27.22  58.488  1 38.29 ? 460 LEU Z N     1 
ATOM   10334 C  CA    . LEU F 1 460 ? -6.64   -26.346 58.675  1 37.87 ? 460 LEU Z CA    1 
ATOM   10335 C  C     . LEU F 1 460 ? -5.681  -27.156 59.518  1 37.56 ? 460 LEU Z C     1 
ATOM   10336 O  O     . LEU F 1 460 ? -5.932  -27.361 60.702  1 37.69 ? 460 LEU Z O     1 
ATOM   10337 C  CB    . LEU F 1 460 ? -7.041  -25.064 59.404  1 37.98 ? 460 LEU Z CB    1 
ATOM   10338 C  CG    . LEU F 1 460 ? -5.914  -24.067 59.628  1 39.16 ? 460 LEU Z CG    1 
ATOM   10339 C  CD1   . LEU F 1 460 ? -5.396  -23.532 58.309  1 39.7  ? 460 LEU Z CD1   1 
ATOM   10340 C  CD2   . LEU F 1 460 ? -6.372  -22.932 60.497  1 39.69 ? 460 LEU Z CD2   1 
ATOM   10341 N  N     . VAL F 1 461 ? -4.635  -27.694 58.898  1 37.15 ? 461 VAL Z N     1 
ATOM   10342 C  CA    . VAL F 1 461 ? -3.682  -28.542 59.602  1 37.23 ? 461 VAL Z CA    1 
ATOM   10343 C  C     . VAL F 1 461 ? -2.812  -27.777 60.594  1 37.23 ? 461 VAL Z C     1 
ATOM   10344 O  O     . VAL F 1 461 ? -2.124  -26.844 60.204  1 37.48 ? 461 VAL Z O     1 
ATOM   10345 C  CB    . VAL F 1 461 ? -2.825  -29.354 58.613  1 37.85 ? 461 VAL Z CB    1 
ATOM   10346 C  CG1   . VAL F 1 461 ? -1.882  -30.284 59.361  1 38.33 ? 461 VAL Z CG1   1 
ATOM   10347 C  CG2   . VAL F 1 461 ? -3.704  -30.137 57.642  1 38.31 ? 461 VAL Z CG2   1 
ATOM   10348 N  N     . ASP F 1 462 ? -2.842  -28.166 61.874  1 36.87 ? 462 ASP Z N     1 
ATOM   10349 C  CA    . ASP F 1 462 ? -2.022  -27.531 62.903  1 36.98 ? 462 ASP Z CA    1 
ATOM   10350 C  C     . ASP F 1 462 ? -0.556  -27.86  62.618  1 36.65 ? 462 ASP Z C     1 
ATOM   10351 O  O     . ASP F 1 462 ? -0.212  -29.022 62.414  1 36.78 ? 462 ASP Z O     1 
ATOM   10352 C  CB    . ASP F 1 462 ? -2.427  -28.045 64.295  1 38.78 ? 462 ASP Z CB    1 
ATOM   10353 C  CG    . ASP F 1 462 ? -1.693  -27.396 65.452  1 43.52 ? 462 ASP Z CG    1 
ATOM   10354 O  OD1   . ASP F 1 462 ? -1.689  -26.145 65.529  1 44.31 ? 462 ASP Z OD1   1 
ATOM   10355 O  OD2   . ASP F 1 462 ? -1.139  -28.137 66.29   1 45.76 ? 462 ASP Z OD2   1 
ATOM   10356 N  N     . PRO F 1 463 ? 0.321   -26.845 62.584  1 36.07 ? 463 PRO Z N     1 
ATOM   10357 C  CA    . PRO F 1 463 ? 1.733   -27.092 62.246  1 35.93 ? 463 PRO Z CA    1 
ATOM   10358 C  C     . PRO F 1 463 ? 2.546   -27.929 63.235  1 36.25 ? 463 PRO Z C     1 
ATOM   10359 O  O     . PRO F 1 463 ? 3.709   -28.222 62.958  1 36.41 ? 463 PRO Z O     1 
ATOM   10360 C  CB    . PRO F 1 463 ? 2.317   -25.682 62.11   1 36.42 ? 463 PRO Z CB    1 
ATOM   10361 C  CG    . PRO F 1 463 ? 1.138   -24.779 61.952  1 36.82 ? 463 PRO Z CG    1 
ATOM   10362 C  CD    . PRO F 1 463 ? 0.05    -25.408 62.749  1 35.39 ? 463 PRO Z CD    1 
ATOM   10363 N  N     . THR F 1 464 ? 1.956   -28.316 64.371  1 36.15 ? 464 THR Z N     1 
ATOM   10364 C  CA    . THR F 1 464 ? 2.657   -29.13  65.352  1 36.55 ? 464 THR Z CA    1 
ATOM   10365 C  C     . THR F 1 464 ? 2.092   -30.543 65.348  1 37.01 ? 464 THR Z C     1 
ATOM   10366 O  O     . THR F 1 464 ? 0.898   -30.745 65.574  1 36.96 ? 464 THR Z O     1 
ATOM   10367 C  CB    . THR F 1 464 ? 2.652   -28.449 66.719  1 37.55 ? 464 THR Z CB    1 
ATOM   10368 O  OG1   . THR F 1 464 ? 3.49    -27.294 66.641  1 38.42 ? 464 THR Z OG1   1 
ATOM   10369 C  CG2   . THR F 1 464 ? 3.146   -29.366 67.829  1 37.88 ? 464 THR Z CG2   1 
ATOM   10370 N  N     . PRO F 1 465 ? 2.933   -31.538 65.026  1 37.26 ? 465 PRO Z N     1 
ATOM   10371 C  CA    . PRO F 1 465 ? 2.437   -32.919 64.978  1 37.71 ? 465 PRO Z CA    1 
ATOM   10372 C  C     . PRO F 1 465 ? 2.302   -33.572 66.36   1 38.48 ? 465 PRO Z C     1 
ATOM   10373 O  O     . PRO F 1 465 ? 2.701   -32.987 67.373  1 38.61 ? 465 PRO Z O     1 
ATOM   10374 C  CB    . PRO F 1 465 ? 3.494   -33.62  64.125  1 38.22 ? 465 PRO Z CB    1 
ATOM   10375 C  CG    . PRO F 1 465 ? 4.752   -32.917 64.489  1 38.5  ? 465 PRO Z CG    1 
ATOM   10376 C  CD    . PRO F 1 465 ? 4.372   -31.466 64.697  1 36.78 ? 465 PRO Z CD    1 
ATOM   10377 N  N     . ASN F 1 466 ? 1.739   -34.796 66.386  1 38.73 ? 466 ASN Z N     1 
ATOM   10378 C  CA    . ASN F 1 466 ? 1.532   -35.629 67.566  1 39.31 ? 466 ASN Z CA    1 
ATOM   10379 C  C     . ASN F 1 466 ? 2.889   -35.886 68.22   1 39.41 ? 466 ASN Z C     1 
ATOM   10380 O  O     . ASN F 1 466 ? 3.039   -35.707 69.423  1 39.61 ? 466 ASN Z O     1 
ATOM   10381 C  CB    . ASN F 1 466 ? 0.887   -36.954 67.139  1 40.76 ? 466 ASN Z CB    1 
ATOM   10382 C  CG    . ASN F 1 466 ? -0.239  -37.414 68.013  1 44.63 ? 466 ASN Z CG    1 
ATOM   10383 O  OD1   . ASN F 1 466 ? -1.411  -37.296 67.64   1 46.14 ? 466 ASN Z OD1   1 
ATOM   10384 N  ND2   . ASN F 1 466 ? 0.084   -37.965 69.181  1 45.41 ? 466 ASN Z ND2   1 
ATOM   10385 N  N     . HIS F 1 467 ? 3.886   -36.253 67.411  1 39.19 ? 467 HIS Z N     1 
ATOM   10386 C  CA    . HIS F 1 467 ? 5.249   -36.491 67.864  1 39.47 ? 467 HIS Z CA    1 
ATOM   10387 C  C     . HIS F 1 467 ? 6.244   -36.369 66.7    1 39.17 ? 467 HIS Z C     1 
ATOM   10388 O  O     . HIS F 1 467 ? 5.856   -36.417 65.531  1 39.19 ? 467 HIS Z O     1 
ATOM   10389 C  CB    . HIS F 1 467 ? 5.374   -37.831 68.609  1 40.64 ? 467 HIS Z CB    1 
ATOM   10390 C  CG    . HIS F 1 467 ? 5.282   -39.041 67.736  1 43.42 ? 467 HIS Z CG    1 
ATOM   10391 N  ND1   . HIS F 1 467 ? 4.102   -39.394 67.108  1 45.5  ? 467 HIS Z ND1   1 
ATOM   10392 C  CD2   . HIS F 1 467 ? 6.218   -39.976 67.462  1 44.72 ? 467 HIS Z CD2   1 
ATOM   10393 C  CE1   . HIS F 1 467 ? 4.367   -40.511 66.447  1 46.12 ? 467 HIS Z CE1   1 
ATOM   10394 N  NE2   . HIS F 1 467 ? 5.622   -40.905 66.639  1 46.01 ? 467 HIS Z NE2   1 
ATOM   10395 N  N     . TYR F 1 468 ? 7.52    -36.163 67.023  1 38.65 ? 468 TYR Z N     1 
ATOM   10396 C  CA    . TYR F 1 468 ? 8.557   -35.979 66.018  1 38.57 ? 468 TYR Z CA    1 
ATOM   10397 C  C     . TYR F 1 468 ? 9.229   -37.306 65.707  1 38.2  ? 468 TYR Z C     1 
ATOM   10398 O  O     . TYR F 1 468 ? 9.706   -37.971 66.62   1 38.47 ? 468 TYR Z O     1 
ATOM   10399 C  CB    . TYR F 1 468 ? 9.554   -34.895 66.468  1 38.73 ? 468 TYR Z CB    1 
ATOM   10400 C  CG    . TYR F 1 468 ? 8.855   -33.584 66.75   1 39.72 ? 468 TYR Z CG    1 
ATOM   10401 C  CD1   . TYR F 1 468 ? 8.537   -32.711 65.722  1 40.63 ? 468 TYR Z CD1   1 
ATOM   10402 C  CD2   . TYR F 1 468 ? 8.407   -33.272 68.026  1 40.81 ? 468 TYR Z CD2   1 
ATOM   10403 C  CE1   . TYR F 1 468 ? 7.838   -31.536 65.963  1 41.64 ? 468 TYR Z CE1   1 
ATOM   10404 C  CE2   . TYR F 1 468 ? 7.696   -32.106 68.277  1 41.84 ? 468 TYR Z CE2   1 
ATOM   10405 C  CZ    . TYR F 1 468 ? 7.417   -31.236 67.243  1 42.82 ? 468 TYR Z CZ    1 
ATOM   10406 O  OH    . TYR F 1 468 ? 6.721   -30.075 67.489  1 44.74 ? 468 TYR Z OH    1 
ATOM   10407 N  N     . GLN F 1 469 ? 9.217   -37.721 64.427  1 37.48 ? 469 GLN Z N     1 
ATOM   10408 C  CA    . GLN F 1 469 ? 9.76    -39.015 64.004  1 37.45 ? 469 GLN Z CA    1 
ATOM   10409 C  C     . GLN F 1 469 ? 10.975  -38.868 63.051  1 36.76 ? 469 GLN Z C     1 
ATOM   10410 O  O     . GLN F 1 469 ? 11.561  -37.787 62.958  1 36.94 ? 469 GLN Z O     1 
ATOM   10411 C  CB    . GLN F 1 469 ? 8.642   -39.865 63.335  1 39.63 ? 469 GLN Z CB    1 
ATOM   10412 C  CG    . GLN F 1 469 ? 7.286   -39.821 64.004  1 44.17 ? 469 GLN Z CG    1 
ATOM   10413 C  CD    . GLN F 1 469 ? 6.188   -39.485 63.031  1 49.31 ? 469 GLN Z CD    1 
ATOM   10414 O  OE1   . GLN F 1 469 ? 5.524   -38.445 63.145  1 50.56 ? 469 GLN Z OE1   1 
ATOM   10415 N  NE2   . GLN F 1 469 ? 5.965   -40.361 62.057  1 50.3  ? 469 GLN Z NE2   1 
ATOM   10416 N  N     . GLU F 1 470 ? 11.336  -39.961 62.335  1 35.83 ? 470 GLU Z N     1 
ATOM   10417 C  CA    . GLU F 1 470 ? 12.409  -40.04  61.347  1 35.3  ? 470 GLU Z CA    1 
ATOM   10418 C  C     . GLU F 1 470 ? 12.255  -38.992 60.239  1 34.31 ? 470 GLU Z C     1 
ATOM   10419 O  O     . GLU F 1 470 ? 13.263  -38.467 59.766  1 34.52 ? 470 GLU Z O     1 
ATOM   10420 C  CB    . GLU F 1 470 ? 12.449  -41.45  60.74   1 37.4  ? 470 GLU Z CB    1 
ATOM   10421 C  CG    . GLU F 1 470 ? 13.64   -41.707 59.845  1 41.67 ? 470 GLU Z CG    1 
ATOM   10422 C  CD    . GLU F 1 470 ? 13.689  -43.123 59.32   1 47.39 ? 470 GLU Z CD    1 
ATOM   10423 O  OE1   . GLU F 1 470 ? 14.009  -43.303 58.122  1 48.49 ? 470 GLU Z OE1   1 
ATOM   10424 O  OE2   . GLU F 1 470 ? 13.419  -44.054 60.111  1 49.4  ? 470 GLU Z OE2   1 
ATOM   10425 N  N     . ASN F 1 471 ? 11.009  -38.657 59.85   1 33.13 ? 471 ASN Z N     1 
ATOM   10426 C  CA    . ASN F 1 471 ? 10.8    -37.634 58.831  1 32.6  ? 471 ASN Z CA    1 
ATOM   10427 C  C     . ASN F 1 471 ? 11.257  -36.26  59.329  1 32.12 ? 471 ASN Z C     1 
ATOM   10428 O  O     . ASN F 1 471 ? 11.826  -35.491 58.554  1 32.51 ? 471 ASN Z O     1 
ATOM   10429 C  CB    . ASN F 1 471 ? 9.363   -37.601 58.334  1 33.24 ? 471 ASN Z CB    1 
ATOM   10430 C  CG    . ASN F 1 471 ? 9.279   -37.342 56.843  1 35.56 ? 471 ASN Z CG    1 
ATOM   10431 O  OD1   . ASN F 1 471 ? 8.576   -38.04  56.103  1 36.38 ? 471 ASN Z OD1   1 
ATOM   10432 N  ND2   . ASN F 1 471 ? 10.013  -36.341 56.362  1 35.8  ? 471 ASN Z ND2   1 
ATOM   10433 N  N     . ASP F 1 472 ? 11.062  -35.971 60.62   1 31.13 ? 472 ASP Z N     1 
ATOM   10434 C  CA    . ASP F 1 472 ? 11.507  -34.71  61.196  1 30.79 ? 472 ASP Z CA    1 
ATOM   10435 C  C     . ASP F 1 472 ? 13.017  -34.664 61.345  1 30.75 ? 472 ASP Z C     1 
ATOM   10436 O  O     . ASP F 1 472 ? 13.608  -33.61  61.127  1 30.94 ? 472 ASP Z O     1 
ATOM   10437 C  CB    . ASP F 1 472 ? 10.796  -34.429 62.509  1 31.65 ? 472 ASP Z CB    1 
ATOM   10438 C  CG    . ASP F 1 472 ? 9.314   -34.33  62.281  1 35.01 ? 472 ASP Z CG    1 
ATOM   10439 O  OD1   . ASP F 1 472 ? 8.89    -33.434 61.525  1 34.59 ? 472 ASP Z OD1   1 
ATOM   10440 O  OD2   . ASP F 1 472 ? 8.578   -35.173 62.819  1 37.96 ? 472 ASP Z OD2   1 
ATOM   10441 N  N     . VAL F 1 473 ? 13.662  -35.815 61.623  1 30.36 ? 473 VAL Z N     1 
ATOM   10442 C  CA    . VAL F 1 473 ? 15.126  -35.9   61.687  1 30.56 ? 473 VAL Z CA    1 
ATOM   10443 C  C     . VAL F 1 473 ? 15.69   -35.556 60.3    1 30.73 ? 473 VAL Z C     1 
ATOM   10444 O  O     . VAL F 1 473 ? 16.593  -34.732 60.191  1 30.86 ? 473 VAL Z O     1 
ATOM   10445 C  CB    . VAL F 1 473 ? 15.607  -37.298 62.142  1 31.32 ? 473 VAL Z CB    1 
ATOM   10446 C  CG1   . VAL F 1 473 ? 17.125  -37.398 62.083  1 31.94 ? 473 VAL Z CG1   1 
ATOM   10447 C  CG2   . VAL F 1 473 ? 15.1    -37.629 63.537  1 31.91 ? 473 VAL Z CG2   1 
ATOM   10448 N  N     . ASP F 1 474 ? 15.079  -36.124 59.246  1 30.64 ? 474 ASP Z N     1 
ATOM   10449 C  CA    . ASP F 1 474 ? 15.441  -35.891 57.851  1 30.95 ? 474 ASP Z CA    1 
ATOM   10450 C  C     . ASP F 1 474 ? 15.254  -34.431 57.432  1 30.93 ? 474 ASP Z C     1 
ATOM   10451 O  O     . ASP F 1 474 ? 16.114  -33.899 56.739  1 31.09 ? 474 ASP Z O     1 
ATOM   10452 C  CB    . ASP F 1 474 ? 14.652  -36.826 56.929  1 32.68 ? 474 ASP Z CB    1 
ATOM   10453 C  CG    . ASP F 1 474 ? 15.269  -38.205 56.808  1 37.24 ? 474 ASP Z CG    1 
ATOM   10454 O  OD1   . ASP F 1 474 ? 16.437  -38.297 56.378  1 38.22 ? 474 ASP Z OD1   1 
ATOM   10455 O  OD2   . ASP F 1 474 ? 14.59   -39.191 57.149  1 39.09 ? 474 ASP Z OD2   1 
ATOM   10456 N  N     . THR F 1 475 ? 14.152  -33.782 57.861  1 30.55 ? 475 THR Z N     1 
ATOM   10457 C  CA    . THR F 1 475 ? 13.865  -32.371 57.557  1 30.54 ? 475 THR Z CA    1 
ATOM   10458 C  C     . THR F 1 475 ? 14.965  -31.475 58.137  1 30.39 ? 475 THR Z C     1 
ATOM   10459 O  O     . THR F 1 475 ? 15.483  -30.6   57.449  1 30.03 ? 475 THR Z O     1 
ATOM   10460 C  CB    . THR F 1 475 ? 12.475  -31.982 58.106  1 31.67 ? 475 THR Z CB    1 
ATOM   10461 O  OG1   . THR F 1 475 ? 11.456  -32.657 57.373  1 32.58 ? 475 THR Z OG1   1 
ATOM   10462 C  CG2   . THR F 1 475 ? 12.223  -30.495 58.052  1 32.12 ? 475 THR Z CG2   1 
ATOM   10463 N  N     . VAL F 1 476 ? 15.339  -31.729 59.394  1 30.54 ? 476 VAL Z N     1 
ATOM   10464 C  CA    . VAL F 1 476 ? 16.381  -30.978 60.085  1 31    ? 476 VAL Z CA    1 
ATOM   10465 C  C     . VAL F 1 476 ? 17.746  -31.203 59.418  1 31.11 ? 476 VAL Z C     1 
ATOM   10466 O  O     . VAL F 1 476 ? 18.441  -30.234 59.127  1 31.38 ? 476 VAL Z O     1 
ATOM   10467 C  CB    . VAL F 1 476 ? 16.388  -31.305 61.602  1 31.84 ? 476 VAL Z CB    1 
ATOM   10468 C  CG1   . VAL F 1 476 ? 17.639  -30.767 62.283  1 32.55 ? 476 VAL Z CG1   1 
ATOM   10469 C  CG2   . VAL F 1 476 ? 15.135  -30.769 62.285  1 32.24 ? 476 VAL Z CG2   1 
ATOM   10470 N  N     . ILE F 1 477 ? 18.105  -32.462 59.13   1 30.75 ? 477 ILE Z N     1 
ATOM   10471 C  CA    . ILE F 1 477 ? 19.375  -32.787 58.479  1 30.95 ? 477 ILE Z CA    1 
ATOM   10472 C  C     . ILE F 1 477 ? 19.462  -32.13  57.096  1 30.84 ? 477 ILE Z C     1 
ATOM   10473 O  O     . ILE F 1 477 ? 20.486  -31.544 56.753  1 30.77 ? 477 ILE Z O     1 
ATOM   10474 C  CB    . ILE F 1 477 ? 19.588  -34.327 58.433  1 31.74 ? 477 ILE Z CB    1 
ATOM   10475 C  CG1   . ILE F 1 477 ? 19.873  -34.9   59.84   1 32.77 ? 477 ILE Z CG1   1 
ATOM   10476 C  CG2   . ILE F 1 477 ? 20.685  -34.735 57.448  1 32.36 ? 477 ILE Z CG2   1 
ATOM   10477 C  CD1   . ILE F 1 477 ? 21.117  -34.357 60.506  1 34.04 ? 477 ILE Z CD1   1 
ATOM   10478 N  N     . TYR F 1 478 ? 18.372  -32.185 56.33   1 30.72 ? 478 TYR Z N     1 
ATOM   10479 C  CA    . TYR F 1 478 ? 18.314  -31.584 55.002  1 31.1  ? 478 TYR Z CA    1 
ATOM   10480 C  C     . TYR F 1 478 ? 18.49   -30.071 55.077  1 31.5  ? 478 TYR Z C     1 
ATOM   10481 O  O     . TYR F 1 478 ? 19.255  -29.51  54.303  1 31.88 ? 478 TYR Z O     1 
ATOM   10482 C  CB    . TYR F 1 478 ? 16.981  -31.928 54.313  1 31.14 ? 478 TYR Z CB    1 
ATOM   10483 C  CG    . TYR F 1 478 ? 16.879  -31.417 52.893  1 32.01 ? 478 TYR Z CG    1 
ATOM   10484 C  CD1   . TYR F 1 478 ? 17.518  -32.074 51.85   1 32.98 ? 478 TYR Z CD1   1 
ATOM   10485 C  CD2   . TYR F 1 478 ? 16.115  -30.298 52.587  1 32.94 ? 478 TYR Z CD2   1 
ATOM   10486 C  CE1   . TYR F 1 478 ? 17.421  -31.616 50.542  1 33.9  ? 478 TYR Z CE1   1 
ATOM   10487 C  CE2   . TYR F 1 478 ? 16.017  -29.825 51.282  1 33.85 ? 478 TYR Z CE2   1 
ATOM   10488 C  CZ    . TYR F 1 478 ? 16.669  -30.49  50.261  1 34.8  ? 478 TYR Z CZ    1 
ATOM   10489 O  OH    . TYR F 1 478 ? 16.567  -30.04  48.966  1 36.37 ? 478 TYR Z OH    1 
ATOM   10490 N  N     . SER F 1 479 ? 17.797  -29.413 56.007  1 31.37 ? 479 SER Z N     1 
ATOM   10491 C  CA    . SER F 1 479 ? 17.877  -27.965 56.143  1 31.61 ? 479 SER Z CA    1 
ATOM   10492 C  C     . SER F 1 479 ? 19.286  -27.508 56.502  1 31.8  ? 479 SER Z C     1 
ATOM   10493 O  O     . SER F 1 479 ? 19.8    -26.57  55.901  1 31.65 ? 479 SER Z O     1 
ATOM   10494 C  CB    . SER F 1 479 ? 16.866  -27.478 57.175  1 32.79 ? 479 SER Z CB    1 
ATOM   10495 O  OG    . SER F 1 479 ? 15.552  -27.892 56.838  1 34.96 ? 479 SER Z OG    1 
ATOM   10496 N  N     . ILE F 1 480 ? 19.919  -28.192 57.459  1 32.04 ? 480 ILE Z N     1 
ATOM   10497 C  CA    . ILE F 1 480 ? 21.261  -27.861 57.921  1 32.85 ? 480 ILE Z CA    1 
ATOM   10498 C  C     . ILE F 1 480 ? 22.316  -28.013 56.828  1 33.63 ? 480 ILE Z C     1 
ATOM   10499 O  O     . ILE F 1 480 ? 23.083  -27.086 56.581  1 33.72 ? 480 ILE Z O     1 
ATOM   10500 C  CB    . ILE F 1 480 ? 21.601  -28.698 59.19   1 33.34 ? 480 ILE Z CB    1 
ATOM   10501 C  CG1   . ILE F 1 480 ? 20.778  -28.22  60.399  1 34.25 ? 480 ILE Z CG1   1 
ATOM   10502 C  CG2   . ILE F 1 480 ? 23.103  -28.703 59.506  1 33.81 ? 480 ILE Z CG2   1 
ATOM   10503 C  CD1   . ILE F 1 480 ? 20.877  -29.126 61.614  1 35.36 ? 480 ILE Z CD1   1 
ATOM   10504 N  N     . PHE F 1 481 ? 22.357  -29.173 56.177  1 34.05 ? 481 PHE Z N     1 
ATOM   10505 C  CA    . PHE F 1 481 ? 23.379  -29.459 55.191  1 34.76 ? 481 PHE Z CA    1 
ATOM   10506 C  C     . PHE F 1 481 ? 23.083  -28.922 53.795  1 35.99 ? 481 PHE Z C     1 
ATOM   10507 O  O     . PHE F 1 481 ? 23.998  -28.889 52.979  1 36.48 ? 481 PHE Z O     1 
ATOM   10508 C  CB    . PHE F 1 481 ? 23.678  -30.959 55.161  1 34.41 ? 481 PHE Z CB    1 
ATOM   10509 C  CG    . PHE F 1 481 ? 24.392  -31.432 56.404  1 34.58 ? 481 PHE Z CG    1 
ATOM   10510 C  CD1   . PHE F 1 481 ? 25.715  -31.108 56.626  1 35.15 ? 481 PHE Z CD1   1 
ATOM   10511 C  CD2   . PHE F 1 481 ? 23.737  -32.19  57.352  1 35.26 ? 481 PHE Z CD2   1 
ATOM   10512 C  CE1   . PHE F 1 481 ? 26.369  -31.538 57.767  1 35.79 ? 481 PHE Z CE1   1 
ATOM   10513 C  CE2   . PHE F 1 481 ? 24.394  -32.615 58.495  1 36.04 ? 481 PHE Z CE2   1 
ATOM   10514 C  CZ    . PHE F 1 481 ? 25.705  -32.286 58.695  1 35.76 ? 481 PHE Z CZ    1 
ATOM   10515 N  N     . LYS F 1 482 ? 21.846  -28.48  53.507  1 36.46 ? 482 LYS Z N     1 
ATOM   10516 C  CA    . LYS F 1 482 ? 21.53   -27.952 52.172  1 37.42 ? 482 LYS Z CA    1 
ATOM   10517 C  C     . LYS F 1 482 ? 21.392  -26.437 52.146  1 38.45 ? 482 LYS Z C     1 
ATOM   10518 O  O     . LYS F 1 482 ? 21.683  -25.818 51.125  1 38.33 ? 482 LYS Z O     1 
ATOM   10519 C  CB    . LYS F 1 482 ? 20.277  -28.629 51.579  1 39.08 ? 482 LYS Z CB    1 
ATOM   10520 C  CG    . LYS F 1 482 ? 20.088  -28.444 50.073  1 42.93 ? 482 LYS Z CG    1 
ATOM   10521 C  CD    . LYS F 1 482 ? 21.282  -28.996 49.274  1 46.95 ? 482 LYS Z CD    1 
ATOM   10522 C  CE    . LYS F 1 482 ? 21.036  -29.033 47.791  1 50.47 ? 482 LYS Z CE    1 
ATOM   10523 N  NZ    . LYS F 1 482 ? 22.263  -29.413 47.036  1 52.55 ? 482 LYS Z NZ    1 
ATOM   10524 N  N     . TYR F 1 483 ? 20.975  -25.827 53.268  1 39.35 ? 483 TYR Z N     1 
ATOM   10525 C  CA    . TYR F 1 483 ? 20.758  -24.379 53.301  1 40.41 ? 483 TYR Z CA    1 
ATOM   10526 C  C     . TYR F 1 483 ? 21.651  -23.605 54.268  1 41.17 ? 483 TYR Z C     1 
ATOM   10527 O  O     . TYR F 1 483 ? 21.993  -22.466 53.971  1 40.96 ? 483 TYR Z O     1 
ATOM   10528 C  CB    . TYR F 1 483 ? 19.278  -24.071 53.573  1 40.6  ? 483 TYR Z CB    1 
ATOM   10529 C  CG    . TYR F 1 483 ? 18.381  -24.674 52.519  1 41.65 ? 483 TYR Z CG    1 
ATOM   10530 C  CD1   . TYR F 1 483 ? 18.502  -24.308 51.187  1 42.63 ? 483 TYR Z CD1   1 
ATOM   10531 C  CD2   . TYR F 1 483 ? 17.458  -25.656 52.842  1 42.66 ? 483 TYR Z CD2   1 
ATOM   10532 C  CE1   . TYR F 1 483 ? 17.713  -24.888 50.207  1 43.61 ? 483 TYR Z CE1   1 
ATOM   10533 C  CE2   . TYR F 1 483 ? 16.661  -26.242 51.87   1 43.63 ? 483 TYR Z CE2   1 
ATOM   10534 C  CZ    . TYR F 1 483 ? 16.789  -25.85  50.552  1 44.59 ? 483 TYR Z CZ    1 
ATOM   10535 O  OH    . TYR F 1 483 ? 16.012  -26.416 49.573  1 46.3  ? 483 TYR Z OH    1 
ATOM   10536 N  N     . ILE F 1 484 ? 22.017  -24.19  55.409  1 42.1  ? 484 ILE Z N     1 
ATOM   10537 C  CA    . ILE F 1 484 ? 22.835  -23.48  56.39   1 43.57 ? 484 ILE Z CA    1 
ATOM   10538 C  C     . ILE F 1 484 ? 24.355  -23.636 56.146  1 45.13 ? 484 ILE Z C     1 
ATOM   10539 O  O     . ILE F 1 484 ? 25.033  -22.631 55.918  1 45.32 ? 484 ILE Z O     1 
ATOM   10540 C  CB    . ILE F 1 484 ? 22.421  -23.855 57.832  1 43.97 ? 484 ILE Z CB    1 
ATOM   10541 C  CG1   . ILE F 1 484 ? 20.94   -23.512 58.073  1 44.94 ? 484 ILE Z CG1   1 
ATOM   10542 C  CG2   . ILE F 1 484 ? 23.326  -23.169 58.848  1 44.39 ? 484 ILE Z CG2   1 
ATOM   10543 C  CD1   . ILE F 1 484 ? 20.384  -24.037 59.345  1 46.22 ? 484 ILE Z CD1   1 
ATOM   10544 N  N     . VAL F 1 485 ? 24.887  -24.869 56.193  1 46.03 ? 485 VAL Z N     1 
ATOM   10545 C  CA    . VAL F 1 485 ? 26.316  -25.128 56.024  1 47.44 ? 485 VAL Z CA    1 
ATOM   10546 C  C     . VAL F 1 485 ? 26.806  -24.885 54.588  1 49.01 ? 485 VAL Z C     1 
ATOM   10547 O  O     . VAL F 1 485 ? 26.316  -25.497 53.638  1 49.13 ? 485 VAL Z O     1 
ATOM   10548 C  CB    . VAL F 1 485 ? 26.695  -26.532 56.539  1 48.04 ? 485 VAL Z CB    1 
ATOM   10549 C  CG1   . VAL F 1 485 ? 28.184  -26.803 56.351  1 48.53 ? 485 VAL Z CG1   1 
ATOM   10550 C  CG2   . VAL F 1 485 ? 26.298  -26.696 58.003  1 48.43 ? 485 VAL Z CG2   1 
ATOM   10551 N  N     . PRO F 1 486 ? 27.793  -23.985 54.429  1 50.02 ? 486 PRO Z N     1 
ATOM   10552 C  CA    . PRO F 1 486 ? 28.283  -23.651 53.081  1 50.81 ? 486 PRO Z CA    1 
ATOM   10553 C  C     . PRO F 1 486 ? 29.115  -24.718 52.373  1 51.92 ? 486 PRO Z C     1 
ATOM   10554 O  O     . PRO F 1 486 ? 29.683  -25.601 53.015  1 52.05 ? 486 PRO Z O     1 
ATOM   10555 C  CB    . PRO F 1 486 ? 29.111  -22.388 53.32   1 51.37 ? 486 PRO Z CB    1 
ATOM   10556 C  CG    . PRO F 1 486 ? 29.597  -22.532 54.712  1 51.63 ? 486 PRO Z CG    1 
ATOM   10557 C  CD    . PRO F 1 486 ? 28.449  -23.156 55.458  1 49.77 ? 486 PRO Z CD    1 
ATOM   10558 N  N     . ASN F 1 487 ? 29.202  -24.591 51.032  1 52.47 ? 487 ASN Z N     1 
ATOM   10559 C  CA    . ASN F 1 487 ? 29.922  -25.483 50.122  1 53.41 ? 487 ASN Z CA    1 
ATOM   10560 C  C     . ASN F 1 487 ? 29.565  -26.935 50.351  1 54.37 ? 487 ASN Z C     1 
ATOM   10561 O  O     . ASN F 1 487 ? 30.437  -27.793 50.489  1 54.38 ? 487 ASN Z O     1 
ATOM   10562 C  CB    . ASN F 1 487 ? 31.42   -25.242 50.155  1 54.46 ? 487 ASN Z CB    1 
ATOM   10563 C  CG    . ASN F 1 487 ? 31.801  -23.855 49.7    1 57.63 ? 487 ASN Z CG    1 
ATOM   10564 O  OD1   . ASN F 1 487 ? 32.012  -23.604 48.51   1 58.82 ? 487 ASN Z OD1   1 
ATOM   10565 N  ND2   . ASN F 1 487 ? 31.894  -22.919 50.638  1 58.18 ? 487 ASN Z ND2   1 
ATOM   10566 N  N     . CYS F 1 488 ? 28.258  -27.19  50.407  1 55.07 ? 488 CYS Z N     1 
ATOM   10567 C  CA    . CYS F 1 488 ? 27.666  -28.5   50.623  1 56.23 ? 488 CYS Z CA    1 
ATOM   10568 C  C     . CYS F 1 488 ? 26.885  -28.962 49.402  1 57.07 ? 488 CYS Z C     1 
ATOM   10569 O  O     . CYS F 1 488 ? 26.421  -28.141 48.61   1 57.24 ? 488 CYS Z O     1 
ATOM   10570 C  CB    . CYS F 1 488 ? 26.78   -28.475 51.86   1 57.19 ? 488 CYS Z CB    1 
ATOM   10571 S  SG    . CYS F 1 488 ? 27.637  -28.906 53.392  1 61.39 ? 488 CYS Z SG    1 
ATOM   10572 N  N     . PHE F 1 489 ? 26.708  -30.277 49.267  1 57.53 ? 489 PHE Z N     1 
ATOM   10573 C  CA    . PHE F 1 489 ? 25.976  -30.822 48.135  1 58.57 ? 489 PHE Z CA    1 
ATOM   10574 C  C     . PHE F 1 489 ? 25.15   -32.049 48.521  1 59.35 ? 489 PHE Z C     1 
ATOM   10575 O  O     . PHE F 1 489 ? 25.665  -32.963 49.165  1 59.4  ? 489 PHE Z O     1 
ATOM   10576 C  CB    . PHE F 1 489 ? 26.943  -31.137 46.987  1 58.67 ? 489 PHE Z CB    1 
ATOM   10577 C  CG    . PHE F 1 489 ? 26.252  -31.637 45.751  1 59.48 ? 489 PHE Z CG    1 
ATOM   10578 C  CD1   . PHE F 1 489 ? 25.491  -30.785 44.973  1 60.39 ? 489 PHE Z CD1   1 
ATOM   10579 C  CD2   . PHE F 1 489 ? 26.353  -32.962 45.374  1 60.28 ? 489 PHE Z CD2   1 
ATOM   10580 C  CE1   . PHE F 1 489 ? 24.847  -31.249 43.842  1 61.15 ? 489 PHE Z CE1   1 
ATOM   10581 C  CE2   . PHE F 1 489 ? 25.708  -33.422 44.245  1 61.08 ? 489 PHE Z CE2   1 
ATOM   10582 C  CZ    . PHE F 1 489 ? 24.956  -32.565 43.486  1 60.96 ? 489 PHE Z CZ    1 
ATOM   10583 N  N     . SER F 1 490 ? 23.867  -32.067 48.13   1 59.75 ? 490 SER Z N     1 
ATOM   10584 C  CA    . SER F 1 490 ? 22.977  -33.183 48.438  1 60.54 ? 490 SER Z CA    1 
ATOM   10585 C  C     . SER F 1 490 ? 22.897  -34.168 47.275  1 61.05 ? 490 SER Z C     1 
ATOM   10586 O  O     . SER F 1 490 ? 21.963  -34.107 46.478  1 61.18 ? 490 SER Z O     1 
ATOM   10587 C  CB    . SER F 1 490 ? 21.582  -32.677 48.798  1 61.94 ? 490 SER Z CB    1 
ATOM   10588 O  OG    . SER F 1 490 ? 20.668  -33.743 49.003  1 64.11 ? 490 SER Z OG    1 
ATOM   10589 N  N     . GLY F 1 491 ? 23.87   -35.067 47.195  1 61.22 ? 491 GLY Z N     1 
ATOM   10590 C  CA    . GLY F 1 491 ? 23.901  -36.078 46.15   1 61.96 ? 491 GLY Z CA    1 
ATOM   10591 C  C     . GLY F 1 491 ? 22.813  -37.111 46.347  1 62.55 ? 491 GLY Z C     1 
ATOM   10592 O  O     . GLY F 1 491 ? 22.164  -37.527 45.388  1 62.75 ? 491 GLY Z O     1 
ATOM   10593 N  N     . MET F 1 492 ? 22.586  -37.51  47.601  1 62.7  ? 492 MET Z N     1 
ATOM   10594 C  CA    . MET F 1 492 ? 21.564  -38.498 47.932  1 63.31 ? 492 MET Z CA    1 
ATOM   10595 C  C     . MET F 1 492 ? 20.642  -38.026 49.052  1 63.53 ? 492 MET Z C     1 
ATOM   10596 O  O     . MET F 1 492 ? 21.098  -37.406 50.009  1 63.55 ? 492 MET Z O     1 
ATOM   10597 C  CB    . MET F 1 492 ? 22.215  -39.823 48.353  1 64.13 ? 492 MET Z CB    1 
ATOM   10598 C  CG    . MET F 1 492 ? 22.213  -40.868 47.271  1 66.37 ? 492 MET Z CG    1 
ATOM   10599 S  SD    . MET F 1 492 ? 21.763  -42.496 47.898  1 69.88 ? 492 MET Z SD    1 
ATOM   10600 C  CE    . MET F 1 492 ? 20.082  -42.195 48.346  1 68.11 ? 492 MET Z CE    1 
ATOM   10601 N  N     . CYS F 1 493 ? 19.35   -38.344 48.941  1 63.5  ? 493 CYS Z N     1 
ATOM   10602 C  CA    . CYS F 1 493 ? 18.359  -38.026 49.962  1 63.99 ? 493 CYS Z CA    1 
ATOM   10603 C  C     . CYS F 1 493 ? 17.154  -38.944 49.832  1 64.33 ? 493 CYS Z C     1 
ATOM   10604 O  O     . CYS F 1 493 ? 16.311  -38.75  48.952  1 64.38 ? 493 CYS Z O     1 
ATOM   10605 C  CB    . CYS F 1 493 ? 17.956  -36.555 49.947  1 64.7  ? 493 CYS Z CB    1 
ATOM   10606 S  SG    . CYS F 1 493 ? 17.397  -35.932 51.557  1 68.03 ? 493 CYS Z SG    1 
ATOM   10607 N  N     . ASN F 1 494 ? 17.088  -39.959 50.712  1 64.34 ? 494 ASN Z N     1 
ATOM   10608 C  CA    . ASN F 1 494 ? 16.019  -40.951 50.75   1 64.71 ? 494 ASN Z CA    1 
ATOM   10609 C  C     . ASN F 1 494 ? 15.304  -40.998 52.109  1 64.78 ? 494 ASN Z C     1 
ATOM   10610 O  O     . ASN F 1 494 ? 15.501  -41.932 52.887  1 64.86 ? 494 ASN Z O     1 
ATOM   10611 C  CB    . ASN F 1 494 ? 16.553  -42.341 50.369  1 65.83 ? 494 ASN Z CB    1 
ATOM   10612 C  CG    . ASN F 1 494 ? 16.126  -42.801 48.997  1 68.75 ? 494 ASN Z CG    1 
ATOM   10613 O  OD1   . ASN F 1 494 ? 16.709  -42.43  47.975  1 69.7  ? 494 ASN Z OD1   1 
ATOM   10614 N  ND2   . ASN F 1 494 ? 15.081  -43.613 48.941  1 69.44 ? 494 ASN Z ND2   1 
ATOM   10615 N  N     . PRO F 1 495 ? 14.423  -40.026 52.391  1 64.61 ? 495 PRO Z N     1 
ATOM   10616 C  CA    . PRO F 1 495 ? 13.667  -40.058 53.659  1 64.73 ? 495 PRO Z CA    1 
ATOM   10617 C  C     . PRO F 1 495 ? 12.544  -41.128 53.669  1 65.03 ? 495 PRO Z C     1 
ATOM   10618 O  O     . PRO F 1 495 ? 12.34   -41.785 52.644  1 65.19 ? 495 PRO Z O     1 
ATOM   10619 C  CB    . PRO F 1 495 ? 13.12   -38.618 53.767  1 65.33 ? 495 PRO Z CB    1 
ATOM   10620 C  CG    . PRO F 1 495 ? 13.73   -37.838 52.616  1 65.64 ? 495 PRO Z CG    1 
ATOM   10621 C  CD    . PRO F 1 495 ? 14.054  -38.854 51.578  1 64.05 ? 495 PRO Z CD    1 
ATOM   10622 N  N     . PRO F 1 496 ? 11.806  -41.355 54.785  1 65.02 ? 496 PRO Z N     1 
ATOM   10623 C  CA    . PRO F 1 496 ? 10.74   -42.376 54.758  1 65.21 ? 496 PRO Z CA    1 
ATOM   10624 C  C     . PRO F 1 496 ? 9.661   -42.095 53.71   1 65.55 ? 496 PRO Z C     1 
ATOM   10625 O  O     . PRO F 1 496 ? 9.059   -41.027 53.712  1 65.7  ? 496 PRO Z O     1 
ATOM   10626 C  CB    . PRO F 1 496 ? 10.164  -42.337 56.181  1 65.82 ? 496 PRO Z CB    1 
ATOM   10627 C  CG    . PRO F 1 496 ? 11.204  -41.687 57.006  1 66.19 ? 496 PRO Z CG    1 
ATOM   10628 C  CD    . PRO F 1 496 ? 11.888  -40.71  56.108  1 64.56 ? 496 PRO Z CD    1 
ATOM   10629 N  N     . GLY F 1 497 ? 9.441   -43.058 52.821  1 65.5  ? 497 GLY Z N     1 
ATOM   10630 C  CA    . GLY F 1 497 ? 8.449   -42.952 51.758  1 65.91 ? 497 GLY Z CA    1 
ATOM   10631 C  C     . GLY F 1 497 ? 8.919   -42.133 50.577  1 66.15 ? 497 GLY Z C     1 
ATOM   10632 O  O     . GLY F 1 497 ? 8.119   -41.472 49.916  1 66.05 ? 497 GLY Z O     1 
ATOM   10633 N  N     . GLY F 1 498 ? 10.214  -42.184 50.305  1 66.39 ? 498 GLY Z N     1 
ATOM   10634 C  CA    . GLY F 1 498 ? 10.813  -41.409 49.232  1 67.19 ? 498 GLY Z CA    1 
ATOM   10635 C  C     . GLY F 1 498 ? 11.153  -42.177 47.973  1 67.9  ? 498 GLY Z C     1 
ATOM   10636 O  O     . GLY F 1 498 ? 11.275  -43.404 47.992  1 67.99 ? 498 GLY Z O     1 
ATOM   10637 N  N     . ASP F 1 499 ? 11.33   -41.431 46.87   1 68.22 ? 499 ASP Z N     1 
ATOM   10638 C  CA    . ASP F 1 499 ? 11.667  -41.936 45.538  1 68.93 ? 499 ASP Z CA    1 
ATOM   10639 C  C     . ASP F 1 499 ? 13.1    -42.496 45.466  1 69.63 ? 499 ASP Z C     1 
ATOM   10640 O  O     . ASP F 1 499 ? 13.902  -42.287 46.372  1 69.77 ? 499 ASP Z O     1 
ATOM   10641 C  CB    . ASP F 1 499 ? 11.518  -40.799 44.497  1 70.29 ? 499 ASP Z CB    1 
ATOM   10642 C  CG    . ASP F 1 499 ? 10.102  -40.379 44.188  1 73.99 ? 499 ASP Z CG    1 
ATOM   10643 O  OD1   . ASP F 1 499 ? 9.264   -40.396 45.112  1 74.31 ? 499 ASP Z OD1   1 
ATOM   10644 O  OD2   . ASP F 1 499 ? 9.839   -40.003 43.024  1 76.08 ? 499 ASP Z OD2   1 
ATOM   10645 N  N     . TRP F 1 500 ? 13.422  -43.197 44.373  1 69.87 ? 500 TRP Z N     1 
ATOM   10646 C  CA    . TRP F 1 500 ? 14.759  -43.712 44.131  1 70.56 ? 500 TRP Z CA    1 
ATOM   10647 C  C     . TRP F 1 500 ? 15.469  -42.566 43.43   1 71.19 ? 500 TRP Z C     1 
ATOM   10648 O  O     . TRP F 1 500 ? 15.387  -42.443 42.207  1 71.47 ? 500 TRP Z O     1 
ATOM   10649 C  CB    . TRP F 1 500 ? 14.666  -44.937 43.211  1 70.57 ? 500 TRP Z CB    1 
ATOM   10650 C  CG    . TRP F 1 500 ? 14.95   -46.266 43.851  1 71.03 ? 500 TRP Z CG    1 
ATOM   10651 C  CD1   . TRP F 1 500 ? 15.803  -47.223 43.388  1 71.93 ? 500 TRP Z CD1   1 
ATOM   10652 C  CD2   . TRP F 1 500 ? 14.317  -46.823 45.015  1 71.06 ? 500 TRP Z CD2   1 
ATOM   10653 N  NE1   . TRP F 1 500 ? 15.765  -48.327 44.207  1 72.2  ? 500 TRP Z NE1   1 
ATOM   10654 C  CE2   . TRP F 1 500 ? 14.864  -48.105 45.217  1 71.86 ? 500 TRP Z CE2   1 
ATOM   10655 C  CE3   . TRP F 1 500 ? 13.36   -46.352 45.921  1 71.52 ? 500 TRP Z CE3   1 
ATOM   10656 C  CZ2   . TRP F 1 500 ? 14.483  -48.919 46.281  1 72.4  ? 500 TRP Z CZ2   1 
ATOM   10657 C  CZ3   . TRP F 1 500 ? 12.991  -47.158 46.977  1 72.36 ? 500 TRP Z CZ3   1 
ATOM   10658 C  CH2   . TRP F 1 500 ? 13.538  -48.43  47.14   1 72.48 ? 500 TRP Z CH2   1 
ATOM   10659 N  N     . SER F 1 501 ? 16.091  -41.678 44.214  1 71.23 ? 501 SER Z N     1 
ATOM   10660 C  CA    . SER F 1 501 ? 16.739  -40.476 43.698  1 71.78 ? 501 SER Z CA    1 
ATOM   10661 C  C     . SER F 1 501 ? 18.005  -40.729 42.866  1 72.31 ? 501 SER Z C     1 
ATOM   10662 O  O     . SER F 1 501 ? 18.069  -40.306 41.712  1 72.51 ? 501 SER Z O     1 
ATOM   10663 C  CB    . SER F 1 501 ? 17.025  -39.498 44.837  1 72.91 ? 501 SER Z CB    1 
ATOM   10664 O  OG    . SER F 1 501 ? 17.692  -38.331 44.382  1 74.88 ? 501 SER Z OG    1 
ATOM   10665 N  N     . GLY F 1 502 ? 18.992  -41.399 43.445  1 72.41 ? 502 GLY Z N     1 
ATOM   10666 C  CA    . GLY F 1 502 ? 20.276  -41.617 42.79   1 73.02 ? 502 GLY Z CA    1 
ATOM   10667 C  C     . GLY F 1 502 ? 21.382  -40.871 43.517  1 73.49 ? 502 GLY Z C     1 
ATOM   10668 O  O     . GLY F 1 502 ? 21.103  -40.009 44.358  1 73.63 ? 502 GLY Z O     1 
ATOM   10669 N  N     . LEU F 1 503 ? 22.647  -41.18  43.203  1 73.58 ? 503 LEU Z N     1 
ATOM   10670 C  CA    . LEU F 1 503 ? 23.768  -40.529 43.878  1 74.19 ? 503 LEU Z CA    1 
ATOM   10671 C  C     . LEU F 1 503 ? 24.581  -39.632 42.957  1 74.51 ? 503 LEU Z C     1 
ATOM   10672 O  O     . LEU F 1 503 ? 25.054  -40.086 41.923  1 74.76 ? 503 LEU Z O     1 
ATOM   10673 C  CB    . LEU F 1 503 ? 24.675  -41.578 44.542  1 74.56 ? 503 LEU Z CB    1 
ATOM   10674 C  CG    . LEU F 1 503 ? 25.964  -41.053 45.18   1 76.34 ? 503 LEU Z CG    1 
ATOM   10675 C  CD1   . LEU F 1 503 ? 25.674  -40.181 46.394  1 77.02 ? 503 LEU Z CD1   1 
ATOM   10676 C  CD2   . LEU F 1 503 ? 26.899  -42.181 45.518  1 77.08 ? 503 LEU Z CD2   1 
ATOM   10677 N  N     . SER F 1 504 ? 24.808  -38.383 43.37   1 74.44 ? 504 SER Z N     1 
ATOM   10678 C  CA    . SER F 1 504 ? 25.632  -37.456 42.61   1 74.92 ? 504 SER Z CA    1 
ATOM   10679 C  C     . SER F 1 504 ? 26.906  -37.127 43.376  1 75.27 ? 504 SER Z C     1 
ATOM   10680 O  O     . SER F 1 504 ? 26.855  -36.867 44.576  1 75.48 ? 504 SER Z O     1 
ATOM   10681 C  CB    . SER F 1 504 ? 24.874  -36.168 42.325  1 76.16 ? 504 SER Z CB    1 
ATOM   10682 O  OG    . SER F 1 504 ? 23.794  -36.381 41.436  1 78.36 ? 504 SER Z OG    1 
ATOM   10683 N  N     . ILE F 1 505 ? 28.047  -37.144 42.68   1 75.19 ? 505 ILE Z N     1 
ATOM   10684 C  CA    . ILE F 1 505 ? 29.357  -36.822 43.236  1 75.68 ? 505 ILE Z CA    1 
ATOM   10685 C  C     . ILE F 1 505 ? 29.976  -35.754 42.347  1 76.47 ? 505 ILE Z C     1 
ATOM   10686 O  O     . ILE F 1 505 ? 30.036  -35.947 41.138  1 76.65 ? 505 ILE Z O     1 
ATOM   10687 C  CB    . ILE F 1 505 ? 30.278  -38.065 43.236  1 75.89 ? 505 ILE Z CB    1 
ATOM   10688 C  CG1   . ILE F 1 505 ? 29.662  -39.259 43.973  1 76.68 ? 505 ILE Z CG1   1 
ATOM   10689 C  CG2   . ILE F 1 505 ? 31.655  -37.717 43.769  1 76.3  ? 505 ILE Z CG2   1 
ATOM   10690 C  CD1   . ILE F 1 505 ? 29.432  -39.062 45.415  1 77.96 ? 505 ILE Z CD1   1 
ATOM   10691 N  N     . ILE F 1 506 ? 30.454  -34.652 42.919  1 76.82 ? 506 ILE Z N     1 
ATOM   10692 C  CA    . ILE F 1 506 ? 31.101  -33.604 42.139  1 77.75 ? 506 ILE Z CA    1 
ATOM   10693 C  C     . ILE F 1 506 ? 32.617  -33.71  42.285  1 78.67 ? 506 ILE Z C     1 
ATOM   10694 O  O     . ILE F 1 506 ? 33.123  -33.696 43.396  1 78.87 ? 506 ILE Z O     1 
ATOM   10695 C  CB    . ILE F 1 506 ? 30.558  -32.216 42.522  1 78.27 ? 506 ILE Z CB    1 
ATOM   10696 C  CG1   . ILE F 1 506 ? 29.055  -32.123 42.227  1 79.26 ? 506 ILE Z CG1   1 
ATOM   10697 C  CG2   . ILE F 1 506 ? 31.338  -31.117 41.811  1 78.73 ? 506 ILE Z CG2   1 
ATOM   10698 C  CD1   . ILE F 1 506 ? 28.4    -30.904 42.784  1 80.66 ? 506 ILE Z CD1   1 
ATOM   10699 N  N     . ARG F 1 507 ? 33.34   -33.854 41.17   1 79.06 ? 507 ARG Z N     1 
ATOM   10700 C  CA    . ARG F 1 507 ? 34.792  -33.991 41.197  1 79.88 ? 507 ARG Z CA    1 
ATOM   10701 C  C     . ARG F 1 507 ? 35.433  -33.371 39.951  1 80.05 ? 507 ARG Z C     1 
ATOM   10702 O  O     . ARG F 1 507 ? 35.046  -33.714 38.834  1 80.2  ? 507 ARG Z O     1 
ATOM   10703 C  CB    . ARG F 1 507 ? 35.163  -35.476 41.307  1 81.82 ? 507 ARG Z CB    1 
ATOM   10704 C  CG    . ARG F 1 507 ? 36.656  -35.746 41.33   1 86    ? 507 ARG Z CG    1 
ATOM   10705 C  CD    . ARG F 1 507 ? 37.309  -35.209 42.582  1 90.17 ? 507 ARG Z CD    1 
ATOM   10706 N  NE    . ARG F 1 507 ? 38.75   -35.465 42.585  1 93.91 ? 507 ARG Z NE    1 
ATOM   10707 C  CZ    . ARG F 1 507 ? 39.623  -34.839 43.37   1 96.55 ? 507 ARG Z CZ    1 
ATOM   10708 N  NH1   . ARG F 1 507 ? 39.214  -33.901 44.213  1 96.25 ? 507 ARG Z NH1   1 
ATOM   10709 N  NH2   . ARG F 1 507 ? 40.915  -35.135 43.302  1 96.7  ? 507 ARG Z NH2   1 
ATOM   10710 N  N     . ASN F 1 508 ? 36.406  -32.457 40.152  1 79.88 ? 508 ASN Z N     1 
ATOM   10711 C  CA    . ASN F 1 508 ? 37.162  -31.755 39.107  1 80.22 ? 508 ASN Z CA    1 
ATOM   10712 C  C     . ASN F 1 508 ? 36.294  -30.908 38.175  1 80.25 ? 508 ASN Z C     1 
ATOM   10713 O  O     . ASN F 1 508 ? 36.577  -30.816 36.981  1 80.54 ? 508 ASN Z O     1 
ATOM   10714 C  CB    . ASN F 1 508 ? 38.046  -32.721 38.301  1 81.44 ? 508 ASN Z CB    1 
ATOM   10715 C  CG    . ASN F 1 508 ? 39.005  -33.52  39.137  1 84.72 ? 508 ASN Z CG    1 
ATOM   10716 O  OD1   . ASN F 1 508 ? 39.473  -33.075 40.19   1 85.91 ? 508 ASN Z OD1   1 
ATOM   10717 N  ND2   . ASN F 1 508 ? 39.324  -34.721 38.683  1 85.38 ? 508 ASN Z ND2   1 
ATOM   10718 N  N     . GLY F 1 509 ? 35.255  -30.291 38.719  1 79.81 ? 509 GLY Z N     1 
ATOM   10719 C  CA    . GLY F 1 509 ? 34.357  -29.461 37.924  1 79.89 ? 509 GLY Z CA    1 
ATOM   10720 C  C     . GLY F 1 509 ? 33.282  -30.222 37.167  1 79.59 ? 509 GLY Z C     1 
ATOM   10721 O  O     . GLY F 1 509 ? 32.551  -29.631 36.37   1 79.78 ? 509 GLY Z O     1 
ATOM   10722 N  N     . HIS F 1 510 ? 33.168  -31.536 37.407  1 78.91 ? 510 HIS Z N     1 
ATOM   10723 C  CA    . HIS F 1 510 ? 32.169  -32.384 36.761  1 78.79 ? 510 HIS Z CA    1 
ATOM   10724 C  C     . HIS F 1 510 ? 31.242  -33.019 37.793  1 78.32 ? 510 HIS Z C     1 
ATOM   10725 O  O     . HIS F 1 510 ? 31.643  -33.227 38.931  1 78.41 ? 510 HIS Z O     1 
ATOM   10726 C  CB    . HIS F 1 510 ? 32.849  -33.499 35.952  1 79.65 ? 510 HIS Z CB    1 
ATOM   10727 C  CG    . HIS F 1 510 ? 33.598  -33.006 34.755  1 81.84 ? 510 HIS Z CG    1 
ATOM   10728 N  ND1   . HIS F 1 510 ? 34.971  -32.844 34.779  1 83.63 ? 510 HIS Z ND1   1 
ATOM   10729 C  CD2   . HIS F 1 510 ? 33.138  -32.652 33.534  1 82.95 ? 510 HIS Z CD2   1 
ATOM   10730 C  CE1   . HIS F 1 510 ? 35.301  -32.399 33.579  1 84.13 ? 510 HIS Z CE1   1 
ATOM   10731 N  NE2   . HIS F 1 510 ? 34.232  -32.268 32.795  1 84.09 ? 510 HIS Z NE2   1 
ATOM   10732 N  N     . GLU F 1 511 ? 30.006  -33.324 37.402  1 77.61 ? 511 GLU Z N     1 
ATOM   10733 C  CA    . GLU F 1 511 ? 29.061  -33.983 38.295  1 77.4  ? 511 GLU Z CA    1 
ATOM   10734 C  C     . GLU F 1 511 ? 28.791  -35.361 37.736  1 77    ? 511 GLU Z C     1 
ATOM   10735 O  O     . GLU F 1 511 ? 28.341  -35.48  36.606  1 77.18 ? 511 GLU Z O     1 
ATOM   10736 C  CB    . GLU F 1 511 ? 27.755  -33.189 38.417  1 79.4  ? 511 GLU Z CB    1 
ATOM   10737 C  CG    . GLU F 1 511 ? 26.724  -33.864 39.309  1 83.41 ? 511 GLU Z CG    1 
ATOM   10738 C  CD    . GLU F 1 511 ? 25.361  -33.201 39.343  1 88.65 ? 511 GLU Z CD    1 
ATOM   10739 O  OE1   . GLU F 1 511 ? 24.444  -33.766 39.98   1 89.56 ? 511 GLU Z OE1   1 
ATOM   10740 O  OE2   . GLU F 1 511 ? 25.207  -32.118 38.733  1 90.51 ? 511 GLU Z OE2   1 
ATOM   10741 N  N     . PHE F 1 512 ? 29.105  -36.399 38.501  1 76.4  ? 512 PHE Z N     1 
ATOM   10742 C  CA    . PHE F 1 512 ? 28.907  -37.792 38.108  1 76.33 ? 512 PHE Z CA    1 
ATOM   10743 C  C     . PHE F 1 512 ? 27.665  -38.302 38.823  1 76.02 ? 512 PHE Z C     1 
ATOM   10744 O  O     . PHE F 1 512 ? 27.475  -37.992 39.996  1 76.08 ? 512 PHE Z O     1 
ATOM   10745 C  CB    . PHE F 1 512 ? 30.137  -38.635 38.494  1 76.33 ? 512 PHE Z CB    1 
ATOM   10746 C  CG    . PHE F 1 512 ? 31.439  -38.083 37.962  1 77.06 ? 512 PHE Z CG    1 
ATOM   10747 C  CD1   . PHE F 1 512 ? 31.855  -38.365 36.674  1 77.84 ? 512 PHE Z CD1   1 
ATOM   10748 C  CD2   . PHE F 1 512 ? 32.237  -37.27  38.745  1 77.9  ? 512 PHE Z CD2   1 
ATOM   10749 C  CE1   . PHE F 1 512 ? 33.043  -37.843 36.181  1 78.57 ? 512 PHE Z CE1   1 
ATOM   10750 C  CE2   . PHE F 1 512 ? 33.419  -36.74  38.245  1 78.59 ? 512 PHE Z CE2   1 
ATOM   10751 C  CZ    . PHE F 1 512 ? 33.815  -37.031 36.969  1 78.39 ? 512 PHE Z CZ    1 
ATOM   10752 N  N     . ARG F 1 513 ? 26.815  -39.069 38.134  1 75.54 ? 513 ARG Z N     1 
ATOM   10753 C  CA    . ARG F 1 513 ? 25.58   -39.545 38.745  1 75.56 ? 513 ARG Z CA    1 
ATOM   10754 C  C     . ARG F 1 513 ? 25.26   -41.004 38.448  1 75.36 ? 513 ARG Z C     1 
ATOM   10755 O  O     . ARG F 1 513 ? 25.329  -41.431 37.297  1 75.45 ? 513 ARG Z O     1 
ATOM   10756 C  CB    . ARG F 1 513 ? 24.417  -38.63  38.347  1 76.89 ? 513 ARG Z CB    1 
ATOM   10757 C  CG    . ARG F 1 513 ? 23.119  -38.914 39.075  1 79.92 ? 513 ARG Z CG    1 
ATOM   10758 C  CD    . ARG F 1 513 ? 22.196  -37.723 38.962  1 83.14 ? 513 ARG Z CD    1 
ATOM   10759 N  NE    . ARG F 1 513 ? 20.884  -37.964 39.566  1 86.2  ? 513 ARG Z NE    1 
ATOM   10760 C  CZ    . ARG F 1 513 ? 20.606  -37.803 40.857  1 88.55 ? 513 ARG Z CZ    1 
ATOM   10761 N  NH1   . ARG F 1 513 ? 21.556  -37.431 41.707  1 88.2  ? 513 ARG Z NH1   1 
ATOM   10762 N  NH2   . ARG F 1 513 ? 19.379  -38.017 41.309  1 88.61 ? 513 ARG Z NH2   1 
ATOM   10763 N  N     . TRP F 1 514 ? 24.917  -41.765 39.505  1 74.93 ? 514 TRP Z N     1 
ATOM   10764 C  CA    . TRP F 1 514 ? 24.524  -43.169 39.423  1 74.92 ? 514 TRP Z CA    1 
ATOM   10765 C  C     . TRP F 1 514 ? 23.017  -43.213 39.533  1 75.17 ? 514 TRP Z C     1 
ATOM   10766 O  O     . TRP F 1 514 ? 22.461  -42.738 40.52   1 75.2  ? 514 TRP Z O     1 
ATOM   10767 C  CB    . TRP F 1 514 ? 25.104  -43.98  40.591  1 74.66 ? 514 TRP Z CB    1 
ATOM   10768 C  CG    . TRP F 1 514 ? 26.539  -44.363 40.444  1 74.87 ? 514 TRP Z CG    1 
ATOM   10769 C  CD1   . TRP F 1 514 ? 27.032  -45.564 40.03   1 75.68 ? 514 TRP Z CD1   1 
ATOM   10770 C  CD2   . TRP F 1 514 ? 27.67   -43.56  40.785  1 74.93 ? 514 TRP Z CD2   1 
ATOM   10771 N  NE1   . TRP F 1 514 ? 28.405  -45.546 40.063  1 75.98 ? 514 TRP Z NE1   1 
ATOM   10772 C  CE2   . TRP F 1 514 ? 28.822  -44.323 40.517  1 75.7  ? 514 TRP Z CE2   1 
ATOM   10773 C  CE3   . TRP F 1 514 ? 27.821  -42.26  41.281  1 75.45 ? 514 TRP Z CE3   1 
ATOM   10774 C  CZ2   . TRP F 1 514 ? 30.104  -43.827 40.721  1 76.32 ? 514 TRP Z CZ2   1 
ATOM   10775 C  CZ3   . TRP F 1 514 ? 29.092  -41.767 41.47   1 76.26 ? 514 TRP Z CZ3   1 
ATOM   10776 C  CH2   . TRP F 1 514 ? 30.215  -42.544 41.189  1 76.41 ? 514 TRP Z CH2   1 
ATOM   10777 N  N     . LEU F 1 515 ? 22.355  -43.767 38.532  1 75.31 ? 515 LEU Z N     1 
ATOM   10778 C  CA    . LEU F 1 515 ? 20.904  -43.894 38.528  1 76.06 ? 515 LEU Z CA    1 
ATOM   10779 C  C     . LEU F 1 515 ? 20.514  -45.375 38.75   1 76.89 ? 515 LEU Z C     1 
ATOM   10780 O  O     . LEU F 1 515 ? 21.379  -46.251 38.69   1 77.04 ? 515 LEU Z O     1 
ATOM   10781 C  CB    . LEU F 1 515 ? 20.35   -43.375 37.185  1 76.25 ? 515 LEU Z CB    1 
ATOM   10782 C  CG    . LEU F 1 515 ? 20.766  -41.958 36.783  1 77.84 ? 515 LEU Z CG    1 
ATOM   10783 C  CD1   . LEU F 1 515 ? 20.445  -41.684 35.327  1 78.47 ? 515 LEU Z CD1   1 
ATOM   10784 C  CD2   . LEU F 1 515 ? 20.129  -40.91  37.689  1 78.59 ? 515 LEU Z CD2   1 
ATOM   10785 N  N     . SER F 1 516 ? 19.224  -45.651 39.011  1 77.25 ? 516 SER Z N     1 
ATOM   10786 C  CA    . SER F 1 516 ? 18.702  -47.007 39.226  1 78.08 ? 516 SER Z CA    1 
ATOM   10787 C  C     . SER F 1 516 ? 19.485  -47.745 40.327  1 78.68 ? 516 SER Z C     1 
ATOM   10788 O  O     . SER F 1 516 ? 20.027  -48.822 40.079  1 78.77 ? 516 SER Z O     1 
ATOM   10789 C  CB    . SER F 1 516 ? 18.692  -47.803 37.913  1 79.56 ? 516 SER Z CB    1 
ATOM   10790 O  OG    . SER F 1 516 ? 18.137  -47.086 36.817  1 81.96 ? 516 SER Z OG    1 
ATOM   10791 N  N     . LEU F 1 517 ? 19.587  -47.137 41.523  1 79.05 ? 517 LEU Z N     1 
ATOM   10792 C  CA    . LEU F 1 517 ? 20.327  -47.72  42.647  1 79.89 ? 517 LEU Z CA    1 
ATOM   10793 C  C     . LEU F 1 517 ? 19.599  -48.915 43.232  1 80.77 ? 517 LEU Z C     1 
ATOM   10794 O  O     . LEU F 1 517 ? 18.526  -48.735 43.805  1 81.05 ? 517 LEU Z O     1 
ATOM   10795 C  CB    . LEU F 1 517 ? 20.522  -46.687 43.773  1 80.03 ? 517 LEU Z CB    1 
ATOM   10796 C  CG    . LEU F 1 517 ? 21.193  -45.374 43.414  1 81.56 ? 517 LEU Z CG    1 
ATOM   10797 C  CD1   . LEU F 1 517 ? 21.327  -44.49  44.644  1 82.2  ? 517 LEU Z CD1   1 
ATOM   10798 C  CD2   . LEU F 1 517 ? 22.556  -45.61  42.819  1 82.25 ? 517 LEU Z CD2   1 
ATOM   10799 N  N     . PRO F 1 518 ? 20.173  -50.131 43.168  1 80.93 ? 518 PRO Z N     1 
ATOM   10800 C  CA    . PRO F 1 518 ? 19.488  -51.283 43.778  1 81.33 ? 518 PRO Z CA    1 
ATOM   10801 C  C     . PRO F 1 518 ? 19.582  -51.254 45.305  1 82.02 ? 518 PRO Z C     1 
ATOM   10802 O  O     . PRO F 1 518 ? 20.595  -50.809 45.852  1 82.26 ? 518 PRO Z O     1 
ATOM   10803 C  CB    . PRO F 1 518 ? 20.224  -52.485 43.19   1 81.85 ? 518 PRO Z CB    1 
ATOM   10804 C  CG    . PRO F 1 518 ? 21.588  -51.977 42.889  1 82.16 ? 518 PRO Z CG    1 
ATOM   10805 C  CD    . PRO F 1 518 ? 21.46   -50.514 42.553  1 80.46 ? 518 PRO Z CD    1 
ATOM   10806 N  N     . ARG F 1 519 ? 18.514  -51.678 45.993  1 82.18 ? 519 ARG Z N     1 
ATOM   10807 C  CA    . ARG F 1 519 ? 18.528  -51.709 47.456  1 82.81 ? 519 ARG Z CA    1 
ATOM   10808 C  C     . ARG F 1 519 ? 19.473  -52.815 47.934  1 83.31 ? 519 ARG Z C     1 
ATOM   10809 O  O     . ARG F 1 519 ? 20.208  -52.623 48.904  1 83.52 ? 519 ARG Z O     1 
ATOM   10810 C  CB    . ARG F 1 519 ? 17.117  -51.946 48.026  1 83.88 ? 519 ARG Z CB    1 
ATOM   10811 C  CG    . ARG F 1 519 ? 17.01   -51.643 49.518  1 86.1  ? 519 ARG Z CG    1 
ATOM   10812 C  CD    . ARG F 1 519 ? 15.907  -52.439 50.188  1 88.57 ? 519 ARG Z CD    1 
ATOM   10813 N  NE    . ARG F 1 519 ? 16.175  -53.878 50.163  1 90.61 ? 519 ARG Z NE    1 
ATOM   10814 C  CZ    . ARG F 1 519 ? 16.845  -54.54  51.103  1 92.15 ? 519 ARG Z CZ    1 
ATOM   10815 N  NH1   . ARG F 1 519 ? 17.32   -53.899 52.164  1 91.68 ? 519 ARG Z NH1   1 
ATOM   10816 N  NH2   . ARG F 1 519 ? 17.034  -55.848 50.996  1 91.88 ? 519 ARG Z NH2   1 
ATOM   10817 N  N     . VAL F 1 520 ? 19.465  -53.963 47.242  1 83.31 ? 520 VAL Z N     1 
ATOM   10818 C  CA    . VAL F 1 520 ? 20.291  -55.104 47.606  1 83.73 ? 520 VAL Z CA    1 
ATOM   10819 C  C     . VAL F 1 520 ? 21.785  -54.898 47.281  1 83.95 ? 520 VAL Z C     1 
ATOM   10820 O  O     . VAL F 1 520 ? 22.188  -54.802 46.116  1 84.13 ? 520 VAL Z O     1 
ATOM   10821 C  CB    . VAL F 1 520 ? 19.737  -56.432 47.03   1 84.43 ? 520 VAL Z CB    1 
ATOM   10822 C  CG1   . VAL F 1 520 ? 18.53   -56.904 47.835  1 84.99 ? 520 VAL Z CG1   1 
ATOM   10823 C  CG2   . VAL F 1 520 ? 19.38   -56.3   45.55   1 84.89 ? 520 VAL Z CG2   1 
ATOM   10824 N  N     . SER F 1 521 ? 22.595  -54.806 48.347  1 83.61 ? 521 SER Z N     1 
ATOM   10825 C  CA    . SER F 1 521 ? 24.049  -54.689 48.284  1 83.65 ? 521 SER Z CA    1 
ATOM   10826 C  C     . SER F 1 521 ? 24.612  -55.759 49.223  1 83.38 ? 521 SER Z C     1 
ATOM   10827 O  O     . SER F 1 521 ? 24.143  -55.896 50.353  1 83.56 ? 521 SER Z O     1 
ATOM   10828 C  CB    . SER F 1 521 ? 24.515  -53.298 48.703  1 84.87 ? 521 SER Z CB    1 
ATOM   10829 O  OG    . SER F 1 521 ? 25.926  -53.243 48.84   1 87.04 ? 521 SER Z OG    1 
ATOM   10830 N  N     . GLU F 1 522 ? 25.575  -56.547 48.737  1 82.74 ? 522 GLU Z N     1 
ATOM   10831 C  CA    . GLU F 1 522 ? 26.174  -57.648 49.492  1 82.54 ? 522 GLU Z CA    1 
ATOM   10832 C  C     . GLU F 1 522 ? 26.725  -57.229 50.861  1 82.16 ? 522 GLU Z C     1 
ATOM   10833 O  O     . GLU F 1 522 ? 26.474  -57.909 51.855  1 82.24 ? 522 GLU Z O     1 
ATOM   10834 C  CB    . GLU F 1 522 ? 27.247  -58.408 48.671  1 84.38 ? 522 GLU Z CB    1 
ATOM   10835 C  CG    . GLU F 1 522 ? 27.764  -57.764 47.384  1 87.94 ? 522 GLU Z CG    1 
ATOM   10836 C  CD    . GLU F 1 522 ? 26.874  -57.913 46.163  1 92.44 ? 522 GLU Z CD    1 
ATOM   10837 O  OE1   . GLU F 1 522 ? 25.984  -57.053 45.971  1 92.96 ? 522 GLU Z OE1   1 
ATOM   10838 O  OE2   . GLU F 1 522 ? 27.074  -58.879 45.391  1 94.05 ? 522 GLU Z OE2   1 
ATOM   10839 N  N     . ASN F 1 523 ? 27.449  -56.103 50.917  1 81.48 ? 523 ASN Z N     1 
ATOM   10840 C  CA    . ASN F 1 523 ? 28.022  -55.614 52.173  1 81.04 ? 523 ASN Z CA    1 
ATOM   10841 C  C     . ASN F 1 523 ? 27.496  -54.24  52.626  1 79.83 ? 523 ASN Z C     1 
ATOM   10842 O  O     . ASN F 1 523 ? 27.825  -53.809 53.731  1 80.07 ? 523 ASN Z O     1 
ATOM   10843 C  CB    . ASN F 1 523 ? 29.55   -55.554 52.075  1 82.42 ? 523 ASN Z CB    1 
ATOM   10844 C  CG    . ASN F 1 523 ? 30.191  -56.842 51.632  1 85.6  ? 523 ASN Z CG    1 
ATOM   10845 O  OD1   . ASN F 1 523 ? 30.668  -56.966 50.497  1 86.75 ? 523 ASN Z OD1   1 
ATOM   10846 N  ND2   . ASN F 1 523 ? 30.218  -57.829 52.518  1 86.09 ? 523 ASN Z ND2   1 
ATOM   10847 N  N     . GLY F 1 524 ? 26.722  -53.558 51.785  1 78.36 ? 524 GLY Z N     1 
ATOM   10848 C  CA    . GLY F 1 524 ? 26.242  -52.224 52.116  1 77.4  ? 524 GLY Z CA    1 
ATOM   10849 C  C     . GLY F 1 524 ? 24.749  -52.007 52.228  1 76.02 ? 524 GLY Z C     1 
ATOM   10850 O  O     . GLY F 1 524 ? 23.946  -52.876 51.879  1 76.09 ? 524 GLY Z O     1 
ATOM   10851 N  N     . LYS F 1 525 ? 24.378  -50.821 52.74   1 74.57 ? 525 LYS Z N     1 
ATOM   10852 C  CA    . LYS F 1 525 ? 22.998  -50.359 52.892  1 73.48 ? 525 LYS Z CA    1 
ATOM   10853 C  C     . LYS F 1 525 ? 22.917  -48.925 52.362  1 71.97 ? 525 LYS Z C     1 
ATOM   10854 O  O     . LYS F 1 525 ? 23.795  -48.116 52.66   1 72.09 ? 525 LYS Z O     1 
ATOM   10855 C  CB    . LYS F 1 525 ? 22.535  -50.421 54.357  1 75.15 ? 525 LYS Z CB    1 
ATOM   10856 C  CG    . LYS F 1 525 ? 21.031  -50.213 54.502  1 78.93 ? 525 LYS Z CG    1 
ATOM   10857 C  CD    . LYS F 1 525 ? 20.503  -50.651 55.857  1 83.1  ? 525 LYS Z CD    1 
ATOM   10858 C  CE    . LYS F 1 525 ? 18.994  -50.657 55.892  1 86.56 ? 525 LYS Z CE    1 
ATOM   10859 N  NZ    . LYS F 1 525 ? 18.423  -51.6   54.892  1 88.66 ? 525 LYS Z NZ    1 
ATOM   10860 N  N     . ARG F 1 526 ? 21.888  -48.616 51.563  1 70.43 ? 526 ARG Z N     1 
ATOM   10861 C  CA    . ARG F 1 526 ? 21.731  -47.291 50.969  1 69.47 ? 526 ARG Z CA    1 
ATOM   10862 C  C     . ARG F 1 526 ? 21.534  -46.2   52.016  1 68.01 ? 526 ARG Z C     1 
ATOM   10863 O  O     . ARG F 1 526 ? 20.603  -46.273 52.819  1 68.14 ? 526 ARG Z O     1 
ATOM   10864 C  CB    . ARG F 1 526 ? 20.575  -47.282 49.959  1 70.83 ? 526 ARG Z CB    1 
ATOM   10865 C  CG    . ARG F 1 526 ? 20.429  -45.953 49.23   1 73.79 ? 526 ARG Z CG    1 
ATOM   10866 C  CD    . ARG F 1 526 ? 19.42   -46.03  48.104  1 76.89 ? 526 ARG Z CD    1 
ATOM   10867 N  NE    . ARG F 1 526 ? 18.079  -46.341 48.595  1 79.65 ? 526 ARG Z NE    1 
ATOM   10868 C  CZ    . ARG F 1 526 ? 16.994  -46.394 47.831  1 81.82 ? 526 ARG Z CZ    1 
ATOM   10869 N  NH1   . ARG F 1 526 ? 17.076  -46.14  46.531  1 81.4  ? 526 ARG Z NH1   1 
ATOM   10870 N  NH2   . ARG F 1 526 ? 15.815  -46.679 48.365  1 81.94 ? 526 ARG Z NH2   1 
ATOM   10871 N  N     . PRO F 1 527 ? 22.406  -45.176 52.023  1 66.42 ? 527 PRO Z N     1 
ATOM   10872 C  CA    . PRO F 1 527 ? 22.268  -44.103 53.018  1 65.32 ? 527 PRO Z CA    1 
ATOM   10873 C  C     . PRO F 1 527 ? 21.055  -43.218 52.79   1 63.96 ? 527 PRO Z C     1 
ATOM   10874 O  O     . PRO F 1 527 ? 20.59   -43.076 51.662  1 63.96 ? 527 PRO Z O     1 
ATOM   10875 C  CB    . PRO F 1 527 ? 23.563  -43.292 52.865  1 66.16 ? 527 PRO Z CB    1 
ATOM   10876 C  CG    . PRO F 1 527 ? 24.47   -44.133 52.026  1 66.87 ? 527 PRO Z CG    1 
ATOM   10877 C  CD    . PRO F 1 527 ? 23.575  -44.959 51.157  1 65.66 ? 527 PRO Z CD    1 
ATOM   10878 N  N     . ASP F 1 528 ? 20.541  -42.63  53.873  1 62.58 ? 528 ASP Z N     1 
ATOM   10879 C  CA    . ASP F 1 528 ? 19.402  -41.722 53.797  1 61.76 ? 528 ASP Z CA    1 
ATOM   10880 C  C     . ASP F 1 528 ? 19.817  -40.33  53.291  1 60.63 ? 528 ASP Z C     1 
ATOM   10881 O  O     . ASP F 1 528 ? 18.978  -39.586 52.801  1 60.7  ? 528 ASP Z O     1 
ATOM   10882 C  CB    . ASP F 1 528 ? 18.707  -41.615 55.161  1 63.3  ? 528 ASP Z CB    1 
ATOM   10883 C  CG    . ASP F 1 528 ? 18.161  -42.931 55.675  1 67.15 ? 528 ASP Z CG    1 
ATOM   10884 O  OD1   . ASP F 1 528 ? 17.874  -43.817 54.846  1 67.49 ? 528 ASP Z OD1   1 
ATOM   10885 O  OD2   . ASP F 1 528 ? 18.012  -43.07  56.907  1 69.31 ? 528 ASP Z OD2   1 
ATOM   10886 N  N     . HIS F 1 529 ? 21.09   -39.959 53.444  1 59.41 ? 529 HIS Z N     1 
ATOM   10887 C  CA    . HIS F 1 529 ? 21.619  -38.684 52.976  1 58.77 ? 529 HIS Z CA    1 
ATOM   10888 C  C     . HIS F 1 529 ? 23.088  -38.867 52.646  1 58.15 ? 529 HIS Z C     1 
ATOM   10889 O  O     . HIS F 1 529 ? 23.792  -39.511 53.411  1 58.28 ? 529 HIS Z O     1 
ATOM   10890 C  CB    . HIS F 1 529 ? 21.556  -37.613 54.081  1 59.21 ? 529 HIS Z CB    1 
ATOM   10891 C  CG    . HIS F 1 529 ? 20.218  -37.417 54.715  1 60.79 ? 529 HIS Z CG    1 
ATOM   10892 N  ND1   . HIS F 1 529 ? 19.222  -36.693 54.089  1 62.45 ? 529 HIS Z ND1   1 
ATOM   10893 C  CD2   . HIS F 1 529 ? 19.774  -37.814 55.929  1 61.72 ? 529 HIS Z CD2   1 
ATOM   10894 C  CE1   . HIS F 1 529 ? 18.199  -36.693 54.927  1 62.83 ? 529 HIS Z CE1   1 
ATOM   10895 N  NE2   . HIS F 1 529 ? 18.486  -37.353 56.048  1 62.7  ? 529 HIS Z NE2   1 
ATOM   10896 N  N     . VAL F 1 530 ? 23.576  -38.281 51.549  1 57.27 ? 530 VAL Z N     1 
ATOM   10897 C  CA    . VAL F 1 530 ? 25.008  -38.285 51.258  1 57.02 ? 530 VAL Z CA    1 
ATOM   10898 C  C     . VAL F 1 530 ? 25.377  -36.83  51.018  1 56.97 ? 530 VAL Z C     1 
ATOM   10899 O  O     . VAL F 1 530 ? 24.902  -36.226 50.06   1 57.15 ? 530 VAL Z O     1 
ATOM   10900 C  CB    . VAL F 1 530 ? 25.474  -39.215 50.115  1 57.54 ? 530 VAL Z CB    1 
ATOM   10901 C  CG1   . VAL F 1 530 ? 26.984  -39.114 49.937  1 58.15 ? 530 VAL Z CG1   1 
ATOM   10902 C  CG2   . VAL F 1 530 ? 25.071  -40.662 50.372  1 57.8  ? 530 VAL Z CG2   1 
ATOM   10903 N  N     . ILE F 1 531 ? 26.144  -36.236 51.931  1 56.67 ? 531 ILE Z N     1 
ATOM   10904 C  CA    . ILE F 1 531 ? 26.5    -34.822 51.841  1 56.89 ? 531 ILE Z CA    1 
ATOM   10905 C  C     . ILE F 1 531 ? 27.929  -34.676 51.377  1 57.13 ? 531 ILE Z C     1 
ATOM   10906 O  O     . ILE F 1 531 ? 28.807  -35.34  51.915  1 57.38 ? 531 ILE Z O     1 
ATOM   10907 C  CB    . ILE F 1 531 ? 26.3    -34.122 53.213  1 57.21 ? 531 ILE Z CB    1 
ATOM   10908 C  CG1   . ILE F 1 531 ? 24.91   -34.412 53.805  1 58.04 ? 531 ILE Z CG1   1 
ATOM   10909 C  CG2   . ILE F 1 531 ? 26.57   -32.619 53.127  1 57.61 ? 531 ILE Z CG2   1 
ATOM   10910 C  CD1   . ILE F 1 531 ? 23.748  -33.978 52.93   1 59.19 ? 531 ILE Z CD1   1 
ATOM   10911 N  N     . GLN F 1 532 ? 28.174  -33.802 50.4    1 56.98 ? 532 GLN Z N     1 
ATOM   10912 C  CA    . GLN F 1 532 ? 29.528  -33.589 49.92   1 57.43 ? 532 GLN Z CA    1 
ATOM   10913 C  C     . GLN F 1 532 ? 30.063  -32.235 50.336  1 57.39 ? 532 GLN Z C     1 
ATOM   10914 O  O     . GLN F 1 532 ? 29.426  -31.22  50.081  1 57.4  ? 532 GLN Z O     1 
ATOM   10915 C  CB    . GLN F 1 532 ? 29.617  -33.775 48.408  1 59.32 ? 532 GLN Z CB    1 
ATOM   10916 C  CG    . GLN F 1 532 ? 31.049  -33.674 47.9    1 63.28 ? 532 GLN Z CG    1 
ATOM   10917 C  CD    . GLN F 1 532 ? 31.219  -34.176 46.498  1 68.08 ? 532 GLN Z CD    1 
ATOM   10918 O  OE1   . GLN F 1 532 ? 30.255  -34.367 45.751  1 69.84 ? 532 GLN Z OE1   1 
ATOM   10919 N  NE2   . GLN F 1 532 ? 32.458  -34.396 46.099  1 68.63 ? 532 GLN Z NE2   1 
ATOM   10920 N  N     . ILE F 1 533 ? 31.226  -32.216 50.997  1 57.23 ? 533 ILE Z N     1 
ATOM   10921 C  CA    . ILE F 1 533 ? 31.867  -30.975 51.423  1 57.6  ? 533 ILE Z CA    1 
ATOM   10922 C  C     . ILE F 1 533 ? 33.239  -30.889 50.766  1 57.96 ? 533 ILE Z C     1 
ATOM   10923 O  O     . ILE F 1 533 ? 34.075  -31.767 50.978  1 58    ? 533 ILE Z O     1 
ATOM   10924 C  CB    . ILE F 1 533 ? 31.942  -30.89  52.955  1 57.96 ? 533 ILE Z CB    1 
ATOM   10925 C  CG1   . ILE F 1 533 ? 30.532  -31.032 53.553  1 58.76 ? 533 ILE Z CG1   1 
ATOM   10926 C  CG2   . ILE F 1 533 ? 32.608  -29.58  53.377  1 58.45 ? 533 ILE Z CG2   1 
ATOM   10927 C  CD1   . ILE F 1 533 ? 30.463  -31.17  54.97   1 59.93 ? 533 ILE Z CD1   1 
ATOM   10928 N  N     . LEU F 1 534 ? 33.464  -29.856 49.947  1 58.07 ? 534 LEU Z N     1 
ATOM   10929 C  CA    . LEU F 1 534 ? 34.707  -29.755 49.191  1 58.77 ? 534 LEU Z CA    1 
ATOM   10930 C  C     . LEU F 1 534 ? 35.713  -28.717 49.671  1 59.17 ? 534 LEU Z C     1 
ATOM   10931 O  O     . LEU F 1 534 ? 36.843  -28.719 49.176  1 59.25 ? 534 LEU Z O     1 
ATOM   10932 C  CB    . LEU F 1 534 ? 34.394  -29.509 47.714  1 59.11 ? 534 LEU Z CB    1 
ATOM   10933 C  CG    . LEU F 1 534 ? 33.574  -30.594 47.042  1 60.66 ? 534 LEU Z CG    1 
ATOM   10934 C  CD1   . LEU F 1 534 ? 32.184  -30.091 46.708  1 61.25 ? 534 LEU Z CD1   1 
ATOM   10935 C  CD2   . LEU F 1 534 ? 34.281  -31.113 45.813  1 61.37 ? 534 LEU Z CD2   1 
ATOM   10936 N  N     . ASP F 1 535 ? 35.333  -27.834 50.603  1 59.23 ? 535 ASP Z N     1 
ATOM   10937 C  CA    . ASP F 1 535 ? 36.266  -26.806 51.07   1 59.89 ? 535 ASP Z CA    1 
ATOM   10938 C  C     . ASP F 1 535 ? 36.785  -27.045 52.492  1 59.83 ? 535 ASP Z C     1 
ATOM   10939 O  O     . ASP F 1 535 ? 37.171  -26.094 53.176  1 60.06 ? 535 ASP Z O     1 
ATOM   10940 C  CB    . ASP F 1 535 ? 35.657  -25.404 50.928  1 62.22 ? 535 ASP Z CB    1 
ATOM   10941 C  CG    . ASP F 1 535 ? 34.47   -25.148 51.835  1 67.74 ? 535 ASP Z CG    1 
ATOM   10942 O  OD1   . ASP F 1 535 ? 33.777  -26.129 52.203  1 68.76 ? 535 ASP Z OD1   1 
ATOM   10943 O  OD2   . ASP F 1 535 ? 34.226  -23.966 52.174  1 70.07 ? 535 ASP Z OD2   1 
ATOM   10944 N  N     . LEU F 1 536 ? 36.82   -28.309 52.929  1 59.29 ? 536 LEU Z N     1 
ATOM   10945 C  CA    . LEU F 1 536 ? 37.294  -28.634 54.268  1 59.24 ? 536 LEU Z CA    1 
ATOM   10946 C  C     . LEU F 1 536 ? 38.641  -29.363 54.207  1 59.05 ? 536 LEU Z C     1 
ATOM   10947 O  O     . LEU F 1 536 ? 39.61   -28.901 54.803  1 59.19 ? 536 LEU Z O     1 
ATOM   10948 C  CB    . LEU F 1 536 ? 36.224  -29.437 55.024  1 59.42 ? 536 LEU Z CB    1 
ATOM   10949 C  CG    . LEU F 1 536 ? 36.56   -29.917 56.419  1 60.85 ? 536 LEU Z CG    1 
ATOM   10950 C  CD1   . LEU F 1 536 ? 36.931  -28.765 57.325  1 61.47 ? 536 LEU Z CD1   1 
ATOM   10951 C  CD2   . LEU F 1 536 ? 35.388  -30.655 57.01   1 61.51 ? 536 LEU Z CD2   1 
ATOM   10952 N  N     . PHE F 1 537 ? 38.717  -30.471 53.462  1 58.6  ? 537 PHE Z N     1 
ATOM   10953 C  CA    . PHE F 1 537 ? 39.963  -31.218 53.298  1 58.77 ? 537 PHE Z CA    1 
ATOM   10954 C  C     . PHE F 1 537 ? 40.446  -31.136 51.836  1 58.54 ? 537 PHE Z C     1 
ATOM   10955 O  O     . PHE F 1 537 ? 39.685  -30.702 50.965  1 58.65 ? 537 PHE Z O     1 
ATOM   10956 C  CB    . PHE F 1 537 ? 39.764  -32.694 53.698  1 58.88 ? 537 PHE Z CB    1 
ATOM   10957 C  CG    . PHE F 1 537 ? 39.171  -32.919 55.065  1 59.79 ? 537 PHE Z CG    1 
ATOM   10958 C  CD1   . PHE F 1 537 ? 39.886  -32.609 56.207  1 60.68 ? 537 PHE Z CD1   1 
ATOM   10959 C  CD2   . PHE F 1 537 ? 37.913  -33.474 55.208  1 60.66 ? 537 PHE Z CD2   1 
ATOM   10960 C  CE1   . PHE F 1 537 ? 39.341  -32.822 57.465  1 61.43 ? 537 PHE Z CE1   1 
ATOM   10961 C  CE2   . PHE F 1 537 ? 37.372  -33.69  56.464  1 61.4  ? 537 PHE Z CE2   1 
ATOM   10962 C  CZ    . PHE F 1 537 ? 38.089  -33.363 57.585  1 61.24 ? 537 PHE Z CZ    1 
ATOM   10963 N  N     . GLU F 1 538 ? 41.694  -31.575 51.55   1 58.01 ? 538 GLU Z N     1 
ATOM   10964 C  CA    . GLU F 1 538 ? 42.184  -31.58  50.168  1 57.98 ? 538 GLU Z CA    1 
ATOM   10965 C  C     . GLU F 1 538 ? 41.35   -32.535 49.319  1 57.53 ? 538 GLU Z C     1 
ATOM   10966 O  O     . GLU F 1 538 ? 41.018  -32.213 48.18   1 57.86 ? 538 GLU Z O     1 
ATOM   10967 C  CB    . GLU F 1 538 ? 43.67   -31.93  50.076  1 60.33 ? 538 GLU Z CB    1 
ATOM   10968 C  CG    . GLU F 1 538 ? 44.394  -31.101 49.03   1 65.07 ? 538 GLU Z CG    1 
ATOM   10969 C  CD    . GLU F 1 538 ? 44.525  -31.711 47.646  1 70.84 ? 538 GLU Z CD    1 
ATOM   10970 O  OE1   . GLU F 1 538 ? 44.961  -30.986 46.721  1 72    ? 538 GLU Z OE1   1 
ATOM   10971 O  OE2   . GLU F 1 538 ? 44.212  -32.912 47.486  1 72.64 ? 538 GLU Z OE2   1 
ATOM   10972 N  N     . LYS F 1 539 ? 40.971  -33.686 49.888  1 56.56 ? 539 LYS Z N     1 
ATOM   10973 C  CA    . LYS F 1 539 ? 40.077  -34.631 49.231  1 56.04 ? 539 LYS Z CA    1 
ATOM   10974 C  C     . LYS F 1 539 ? 38.645  -34.245 49.617  1 55.45 ? 539 LYS Z C     1 
ATOM   10975 O  O     . LYS F 1 539 ? 38.397  -33.833 50.754  1 55.61 ? 539 LYS Z O     1 
ATOM   10976 C  CB    . LYS F 1 539 ? 40.351  -36.062 49.711  1 57.42 ? 539 LYS Z CB    1 
ATOM   10977 C  CG    . LYS F 1 539 ? 41.712  -36.605 49.335  1 60.67 ? 539 LYS Z CG    1 
ATOM   10978 C  CD    . LYS F 1 539 ? 41.835  -38.055 49.78   1 64.21 ? 539 LYS Z CD    1 
ATOM   10979 C  CE    . LYS F 1 539 ? 43.1    -38.701 49.283  1 67.21 ? 539 LYS Z CE    1 
ATOM   10980 N  NZ    . LYS F 1 539 ? 43.237  -40.097 49.772  1 69.11 ? 539 LYS Z NZ    1 
ATOM   10981 N  N     . PRO F 1 540 ? 37.684  -34.382 48.697  1 54.63 ? 540 PRO Z N     1 
ATOM   10982 C  CA    . PRO F 1 540 ? 36.295  -34.051 49.046  1 54.18 ? 540 PRO Z CA    1 
ATOM   10983 C  C     . PRO F 1 540 ? 35.747  -35.019 50.091  1 53.73 ? 540 PRO Z C     1 
ATOM   10984 O  O     . PRO F 1 540 ? 36.109  -36.195 50.093  1 53.96 ? 540 PRO Z O     1 
ATOM   10985 C  CB    . PRO F 1 540 ? 35.548  -34.19  47.718  1 54.95 ? 540 PRO Z CB    1 
ATOM   10986 C  CG    . PRO F 1 540 ? 36.605  -34.269 46.66   1 55.6  ? 540 PRO Z CG    1 
ATOM   10987 C  CD    . PRO F 1 540 ? 37.8    -34.866 47.312  1 54.08 ? 540 PRO Z CD    1 
ATOM   10988 N  N     . LEU F 1 541 ? 34.894  -34.525 50.989  1 52.9  ? 541 LEU Z N     1 
ATOM   10989 C  CA    . LEU F 1 541 ? 34.299  -35.367 52.017  1 52.6  ? 541 LEU Z CA    1 
ATOM   10990 C  C     . LEU F 1 541 ? 32.926  -35.855 51.567  1 52.25 ? 541 LEU Z C     1 
ATOM   10991 O  O     . LEU F 1 541 ? 32.115  -35.055 51.122  1 52.29 ? 541 LEU Z O     1 
ATOM   10992 C  CB    . LEU F 1 541 ? 34.171  -34.582 53.344  1 52.61 ? 541 LEU Z CB    1 
ATOM   10993 C  CG    . LEU F 1 541 ? 33.251  -35.179 54.418  1 53.72 ? 541 LEU Z CG    1 
ATOM   10994 C  CD1   . LEU F 1 541 ? 33.847  -36.413 55.017  1 54    ? 541 LEU Z CD1   1 
ATOM   10995 C  CD2   . LEU F 1 541 ? 32.905  -34.166 55.463  1 54.51 ? 541 LEU Z CD2   1 
ATOM   10996 N  N     . LEU F 1 542 ? 32.649  -37.151 51.741  1 51.7  ? 542 LEU Z N     1 
ATOM   10997 C  CA    . LEU F 1 542 ? 31.338  -37.711 51.475  1 51.59 ? 542 LEU Z CA    1 
ATOM   10998 C  C     . LEU F 1 542 ? 30.844  -38.224 52.808  1 51.43 ? 542 LEU Z C     1 
ATOM   10999 O  O     . LEU F 1 542 ? 31.417  -39.156 53.367  1 51.5  ? 542 LEU Z O     1 
ATOM   11000 C  CB    . LEU F 1 542 ? 31.399  -38.848 50.458  1 51.79 ? 542 LEU Z CB    1 
ATOM   11001 C  CG    . LEU F 1 542 ? 31.782  -38.43  49.055  1 53.5  ? 542 LEU Z CG    1 
ATOM   11002 C  CD1   . LEU F 1 542 ? 31.981  -39.638 48.165  1 54.11 ? 542 LEU Z CD1   1 
ATOM   11003 C  CD2   . LEU F 1 542 ? 30.75   -37.482 48.466  1 54.25 ? 542 LEU Z CD2   1 
ATOM   11004 N  N     . LEU F 1 543 ? 29.834  -37.566 53.358  1 51.03 ? 543 LEU Z N     1 
ATOM   11005 C  CA    . LEU F 1 543 ? 29.272  -37.928 54.644  1 51.07 ? 543 LEU Z CA    1 
ATOM   11006 C  C     . LEU F 1 543 ? 27.975  -38.68  54.414  1 50.92 ? 543 LEU Z C     1 
ATOM   11007 O  O     . LEU F 1 543 ? 27.008  -38.094 53.941  1 51.07 ? 543 LEU Z O     1 
ATOM   11008 C  CB    . LEU F 1 543 ? 29.008  -36.654 55.453  1 51.26 ? 543 LEU Z CB    1 
ATOM   11009 C  CG    . LEU F 1 543 ? 28.394  -36.858 56.82   1 52.68 ? 543 LEU Z CG    1 
ATOM   11010 C  CD1   . LEU F 1 543 ? 29.329  -37.64  57.721  1 53.14 ? 543 LEU Z CD1   1 
ATOM   11011 C  CD2   . LEU F 1 543 ? 28.022  -35.519 57.442  1 53.36 ? 543 LEU Z CD2   1 
ATOM   11012 N  N     . SER F 1 544 ? 27.957  -39.982 54.713  1 50.52 ? 544 SER Z N     1 
ATOM   11013 C  CA    . SER F 1 544 ? 26.764  -40.805 54.535  1 50.72 ? 544 SER Z CA    1 
ATOM   11014 C  C     . SER F 1 544 ? 26.01   -40.853 55.845  1 50.67 ? 544 SER Z C     1 
ATOM   11015 O  O     . SER F 1 544 ? 26.569  -41.259 56.853  1 50.89 ? 544 SER Z O     1 
ATOM   11016 C  CB    . SER F 1 544 ? 27.141  -42.214 54.091  1 52.1  ? 544 SER Z CB    1 
ATOM   11017 O  OG    . SER F 1 544 ? 27.707  -42.197 52.79   1 54.32 ? 544 SER Z OG    1 
ATOM   11018 N  N     . ILE F 1 545 ? 24.751  -40.419 55.842  1 50.2  ? 545 ILE Z N     1 
ATOM   11019 C  CA    . ILE F 1 545 ? 23.937  -40.331 57.048  1 50.1  ? 545 ILE Z CA    1 
ATOM   11020 C  C     . ILE F 1 545 ? 22.748  -41.288 57.024  1 49.75 ? 545 ILE Z C     1 
ATOM   11021 O  O     . ILE F 1 545 ? 22.044  -41.377 56.021  1 49.88 ? 545 ILE Z O     1 
ATOM   11022 C  CB    . ILE F 1 545 ? 23.452  -38.863 57.254  1 50.65 ? 545 ILE Z CB    1 
ATOM   11023 C  CG1   . ILE F 1 545 ? 24.593  -37.837 57.114  1 51.69 ? 545 ILE Z CG1   1 
ATOM   11024 C  CG2   . ILE F 1 545 ? 22.727  -38.689 58.581  1 51.15 ? 545 ILE Z CG2   1 
ATOM   11025 C  CD1   . ILE F 1 545 ? 24.123  -36.392 57.029  1 53.04 ? 545 ILE Z CD1   1 
ATOM   11026 N  N     . GLU F 1 546 ? 22.515  -41.985 58.14   1 49.13 ? 546 GLU Z N     1 
ATOM   11027 C  CA    . GLU F 1 546 ? 21.355  -42.845 58.305  1 49.1  ? 546 GLU Z CA    1 
ATOM   11028 C  C     . GLU F 1 546 ? 20.557  -42.223 59.439  1 48.85 ? 546 GLU Z C     1 
ATOM   11029 O  O     . GLU F 1 546 ? 21.105  -41.977 60.512  1 48.97 ? 546 GLU Z O     1 
ATOM   11030 C  CB    . GLU F 1 546 ? 21.762  -44.281 58.654  1 51.32 ? 546 GLU Z CB    1 
ATOM   11031 C  CG    . GLU F 1 546 ? 20.599  -45.262 58.681  1 55.83 ? 546 GLU Z CG    1 
ATOM   11032 C  CD    . GLU F 1 546 ? 20.339  -46.021 57.392  1 61.18 ? 546 GLU Z CD    1 
ATOM   11033 O  OE1   . GLU F 1 546 ? 20.599  -45.464 56.3    1 61.48 ? 546 GLU Z OE1   1 
ATOM   11034 O  OE2   . GLU F 1 546 ? 19.862  -47.176 57.477  1 63.32 ? 546 GLU Z OE2   1 
ATOM   11035 N  N     . SER F 1 547 ? 19.289  -41.903 59.187  1 48.41 ? 547 SER Z N     1 
ATOM   11036 C  CA    . SER F 1 547 ? 18.451  -41.246 60.182  1 48.46 ? 547 SER Z CA    1 
ATOM   11037 C  C     . SER F 1 547 ? 17.447  -42.207 60.774  1 48.09 ? 547 SER Z C     1 
ATOM   11038 O  O     . SER F 1 547 ? 16.873  -43.018 60.055  1 48.21 ? 547 SER Z O     1 
ATOM   11039 C  CB    . SER F 1 547 ? 17.719  -40.064 59.554  1 49.94 ? 547 SER Z CB    1 
ATOM   11040 O  OG    . SER F 1 547 ? 16.966  -40.489 58.43   1 52.3  ? 547 SER Z OG    1 
ATOM   11041 N  N     . LYS F 1 548 ? 17.247  -42.127 62.088  1 47.52 ? 548 LYS Z N     1 
ATOM   11042 C  CA    . LYS F 1 548 ? 16.298  -42.956 62.828  1 47.46 ? 548 LYS Z CA    1 
ATOM   11043 C  C     . LYS F 1 548 ? 15.561  -42.092 63.869  1 47.21 ? 548 LYS Z C     1 
ATOM   11044 O  O     . LYS F 1 548 ? 15.979  -40.962 64.149  1 47.26 ? 548 LYS Z O     1 
ATOM   11045 C  CB    . LYS F 1 548 ? 17.032  -44.115 63.531  1 49.26 ? 548 LYS Z CB    1 
ATOM   11046 C  CG    . LYS F 1 548 ? 17.636  -45.159 62.594  1 53.45 ? 548 LYS Z CG    1 
ATOM   11047 C  CD    . LYS F 1 548 ? 16.581  -45.908 61.793  1 57.86 ? 548 LYS Z CD    1 
ATOM   11048 C  CE    . LYS F 1 548 ? 17.135  -46.527 60.528  1 61.74 ? 548 LYS Z CE    1 
ATOM   11049 N  NZ    . LYS F 1 548 ? 17.873  -47.787 60.793  1 64.27 ? 548 LYS Z NZ    1 
ATOM   11050 N  N     . GLU F 1 549 ? 14.463  -42.612 64.44   1 46.72 ? 549 GLU Z N     1 
ATOM   11051 C  CA    . GLU F 1 549 ? 13.729  -41.876 65.469  1 46.56 ? 549 GLU Z CA    1 
ATOM   11052 C  C     . GLU F 1 549 ? 14.519  -41.911 66.772  1 46.81 ? 549 GLU Z C     1 
ATOM   11053 O  O     . GLU F 1 549 ? 14.68   -40.884 67.42   1 46.71 ? 549 GLU Z O     1 
ATOM   11054 C  CB    . GLU F 1 549 ? 12.32   -42.458 65.673  1 47.35 ? 549 GLU Z CB    1 
ATOM   11055 C  CG    . GLU F 1 549 ? 11.523  -41.745 66.75   1 48.38 ? 549 GLU Z CG    1 
ATOM   11056 C  CD    . GLU F 1 549 ? 10.04   -42.043 66.737  1 50.26 ? 549 GLU Z CD    1 
ATOM   11057 O  OE1   . GLU F 1 549 ? 9.53    -42.507 65.694  1 50.49 ? 549 GLU Z OE1   1 
ATOM   11058 O  OE2   . GLU F 1 549 ? 9.38    -41.794 67.769  1 51.37 ? 549 GLU Z OE2   1 
ATOM   11059 N  N     . LYS F 1 550 ? 15.04   -43.087 67.137  1 47.09 ? 550 LYS Z N     1 
ATOM   11060 C  CA    . LYS F 1 550 ? 15.783  -43.266 68.379  1 47.93 ? 550 LYS Z CA    1 
ATOM   11061 C  C     . LYS F 1 550 ? 17.201  -43.796 68.149  1 48.86 ? 550 LYS Z C     1 
ATOM   11062 O  O     . LYS F 1 550 ? 17.44   -44.491 67.164  1 48.89 ? 550 LYS Z O     1 
ATOM   11063 C  CB    . LYS F 1 550 ? 15.001  -44.21  69.311  1 49.34 ? 550 LYS Z CB    1 
ATOM   11064 C  CG    . LYS F 1 550 ? 13.632  -43.666 69.681  1 52.8  ? 550 LYS Z CG    1 
ATOM   11065 C  CD    . LYS F 1 550 ? 13.007  -44.387 70.855  1 56.53 ? 550 LYS Z CD    1 
ATOM   11066 C  CE    . LYS F 1 550 ? 11.732  -43.703 71.294  1 59.58 ? 550 LYS Z CE    1 
ATOM   11067 N  NZ    . LYS F 1 550 ? 10.669  -43.8   70.261  1 61.55 ? 550 LYS Z NZ    1 
ATOM   11068 N  N     . PRO F 1 551 ? 18.153  -43.519 69.065  1 49.51 ? 551 PRO Z N     1 
ATOM   11069 C  CA    . PRO F 1 551 ? 19.523  -44.032 68.874  1 50.18 ? 551 PRO Z CA    1 
ATOM   11070 C  C     . PRO F 1 551 ? 19.623  -45.561 68.883  1 51.23 ? 551 PRO Z C     1 
ATOM   11071 O  O     . PRO F 1 551 ? 20.486  -46.123 68.21   1 51.33 ? 551 PRO Z O     1 
ATOM   11072 C  CB    . PRO F 1 551 ? 20.319  -43.388 70.018  1 50.68 ? 551 PRO Z CB    1 
ATOM   11073 C  CG    . PRO F 1 551 ? 19.313  -42.986 71.025  1 50.91 ? 551 PRO Z CG    1 
ATOM   11074 C  CD    . PRO F 1 551 ? 18.044  -42.696 70.286  1 49.17 ? 551 PRO Z CD    1 
ATOM   11075 N  N     . ASN F 1 552 ? 18.719  -46.237 69.613  1 51.78 ? 552 ASN Z N     1 
ATOM   11076 C  CA    . ASN F 1 552 ? 18.682  -47.702 69.658  1 52.7  ? 552 ASN Z CA    1 
ATOM   11077 C  C     . ASN F 1 552 ? 18.219  -48.328 68.327  1 53.62 ? 552 ASN Z C     1 
ATOM   11078 O  O     . ASN F 1 552 ? 18.45   -49.513 68.103  1 53.82 ? 552 ASN Z O     1 
ATOM   11079 C  CB    . ASN F 1 552 ? 17.817  -48.184 70.816  1 53.6  ? 552 ASN Z CB    1 
ATOM   11080 C  CG    . ASN F 1 552 ? 18.41   -47.856 72.16   1 56.56 ? 552 ASN Z CG    1 
ATOM   11081 O  OD1   . ASN F 1 552 ? 19.633  -47.782 72.32   1 57.59 ? 552 ASN Z OD1   1 
ATOM   11082 N  ND2   . ASN F 1 552 ? 17.558  -47.651 73.156  1 57.24 ? 552 ASN Z ND2   1 
ATOM   11083 N  N     . ASP F 1 553 ? 17.575  -47.536 67.446  1 54.06 ? 553 ASP Z N     1 
ATOM   11084 C  CA    . ASP F 1 553 ? 17.128  -47.989 66.129  1 54.87 ? 553 ASP Z CA    1 
ATOM   11085 C  C     . ASP F 1 553 ? 18.292  -48.132 65.132  1 55.31 ? 553 ASP Z C     1 
ATOM   11086 O  O     . ASP F 1 553 ? 18.113  -48.754 64.087  1 55.54 ? 553 ASP Z O     1 
ATOM   11087 C  CB    . ASP F 1 553 ? 16.058  -47.047 65.554  1 56.86 ? 553 ASP Z CB    1 
ATOM   11088 C  CG    . ASP F 1 553 ? 14.83   -46.897 66.426  1 62.13 ? 553 ASP Z CG    1 
ATOM   11089 O  OD1   . ASP F 1 553 ? 14.531  -47.833 67.196  1 63.04 ? 553 ASP Z OD1   1 
ATOM   11090 O  OD2   . ASP F 1 553 ? 14.164  -45.841 66.336  1 64.61 ? 553 ASP Z OD2   1 
ATOM   11091 N  N     . LEU F 1 554 ? 19.466  -47.54  65.426  1 55.26 ? 554 LEU Z N     1 
ATOM   11092 C  CA    . LEU F 1 554 ? 20.629  -47.652 64.555  1 55.62 ? 554 LEU Z CA    1 
ATOM   11093 C  C     . LEU F 1 554 ? 21.119  -49.094 64.625  1 55.94 ? 554 LEU Z C     1 
ATOM   11094 O  O     . LEU F 1 554 ? 21.517  -49.565 65.691  1 55.89 ? 554 LEU Z O     1 
ATOM   11095 C  CB    . LEU F 1 554 ? 21.735  -46.678 64.985  1 55.75 ? 554 LEU Z CB    1 
ATOM   11096 C  CG    . LEU F 1 554 ? 21.442  -45.2   64.769  1 56.97 ? 554 LEU Z CG    1 
ATOM   11097 C  CD1   . LEU F 1 554 ? 22.511  -44.339 65.398  1 57.49 ? 554 LEU Z CD1   1 
ATOM   11098 C  CD2   . LEU F 1 554 ? 21.325  -44.886 63.308  1 57.5  ? 554 LEU Z CD2   1 
ATOM   11099 N  N     . GLU F 1 555 ? 21.013  -49.808 63.501  1 56.06 ? 555 GLU Z N     1 
ATOM   11100 C  CA    . GLU F 1 555 ? 21.367  -51.218 63.384  1 56.59 ? 555 GLU Z CA    1 
ATOM   11101 C  C     . GLU F 1 555 ? 22.849  -51.481 63.602  1 56.91 ? 555 GLU Z C     1 
ATOM   11102 O  O     . GLU F 1 555 ? 23.677  -50.629 63.29   1 56.96 ? 555 GLU Z O     1 
ATOM   11103 C  CB    . GLU F 1 555 ? 20.939  -51.75  62.006  1 58.76 ? 555 GLU Z CB    1 
ATOM   11104 C  CG    . GLU F 1 555 ? 19.444  -51.674 61.765  1 63.22 ? 555 GLU Z CG    1 
ATOM   11105 C  CD    . GLU F 1 555 ? 18.991  -50.552 60.85   1 69.04 ? 555 GLU Z CD    1 
ATOM   11106 O  OE1   . GLU F 1 555 ? 17.798  -50.552 60.471  1 70.48 ? 555 GLU Z OE1   1 
ATOM   11107 O  OE2   . GLU F 1 555 ? 19.821  -49.678 60.507  1 70.55 ? 555 GLU Z OE2   1 
ATOM   11108 N  N     . PRO F 1 556 ? 23.213  -52.675 64.105  1 56.94 ? 556 PRO Z N     1 
ATOM   11109 C  CA    . PRO F 1 556 ? 24.639  -52.983 64.284  1 57.08 ? 556 PRO Z CA    1 
ATOM   11110 C  C     . PRO F 1 556 ? 25.389  -52.934 62.953  1 57.4  ? 556 PRO Z C     1 
ATOM   11111 O  O     . PRO F 1 556 ? 24.882  -53.412 61.935  1 57.44 ? 556 PRO Z O     1 
ATOM   11112 C  CB    . PRO F 1 556 ? 24.627  -54.393 64.886  1 57.68 ? 556 PRO Z CB    1 
ATOM   11113 C  CG    . PRO F 1 556 ? 23.254  -54.563 65.456  1 58.05 ? 556 PRO Z CG    1 
ATOM   11114 C  CD    . PRO F 1 556 ? 22.36   -53.799 64.534  1 56.48 ? 556 PRO Z CD    1 
ATOM   11115 N  N     . LYS F 1 557 ? 26.551  -52.264 62.957  1 57.47 ? 557 LYS Z N     1 
ATOM   11116 C  CA    . LYS F 1 557 ? 27.423  -52.062 61.801  1 58.01 ? 557 LYS Z CA    1 
ATOM   11117 C  C     . LYS F 1 557 ? 26.815  -51.175 60.718  1 58.3  ? 557 LYS Z C     1 
ATOM   11118 O  O     . LYS F 1 557 ? 27.294  -51.209 59.588  1 58.33 ? 557 LYS Z O     1 
ATOM   11119 C  CB    . LYS F 1 557 ? 27.914  -53.392 61.205  1 59.82 ? 557 LYS Z CB    1 
ATOM   11120 C  CG    . LYS F 1 557 ? 28.699  -54.238 62.198  1 64.15 ? 557 LYS Z CG    1 
ATOM   11121 C  CD    . LYS F 1 557 ? 29.048  -55.607 61.639  1 68.99 ? 557 LYS Z CD    1 
ATOM   11122 C  CE    . LYS F 1 557 ? 30.031  -55.533 60.497  1 73.14 ? 557 LYS Z CE    1 
ATOM   11123 N  NZ    . LYS F 1 557 ? 30.417  -56.889 60.017  1 75.59 ? 557 LYS Z NZ    1 
ATOM   11124 N  N     . ILE F 1 558 ? 25.802  -50.35  61.054  1 58.33 ? 558 ILE Z N     1 
ATOM   11125 C  CA    . ILE F 1 558 ? 25.183  -49.465 60.066  1 58.75 ? 558 ILE Z CA    1 
ATOM   11126 C  C     . ILE F 1 558 ? 26.196  -48.475 59.501  1 59.12 ? 558 ILE Z C     1 
ATOM   11127 O  O     . ILE F 1 558 ? 26.212  -48.262 58.295  1 59.31 ? 558 ILE Z O     1 
ATOM   11128 C  CB    . ILE F 1 558 ? 23.884  -48.773 60.569  1 59.19 ? 558 ILE Z CB    1 
ATOM   11129 C  CG1   . ILE F 1 558 ? 23.123  -48.085 59.421  1 60.09 ? 558 ILE Z CG1   1 
ATOM   11130 C  CG2   . ILE F 1 558 ? 24.159  -47.79  61.696  1 59.64 ? 558 ILE Z CG2   1 
ATOM   11131 C  CD1   . ILE F 1 558 ? 22.71   -48.986 58.315  1 61.39 ? 558 ILE Z CD1   1 
ATOM   11132 N  N     . GLY F 1 559 ? 27.088  -47.964 60.349  1 59.19 ? 559 GLY Z N     1 
ATOM   11133 C  CA    . GLY F 1 559 ? 28.13   -47.033 59.936  1 59.83 ? 559 GLY Z CA    1 
ATOM   11134 C  C     . GLY F 1 559 ? 29.04   -47.623 58.883  1 60.27 ? 559 GLY Z C     1 
ATOM   11135 O  O     . GLY F 1 559 ? 29.276  -47.005 57.847  1 60.39 ? 559 GLY Z O     1 
ATOM   11136 N  N     . VAL F 1 560 ? 29.494  -48.857 59.11   1 60.43 ? 560 VAL Z N     1 
ATOM   11137 C  CA    . VAL F 1 560 ? 30.352  -49.559 58.16   1 61.1  ? 560 VAL Z CA    1 
ATOM   11138 C  C     . VAL F 1 560 ? 29.598  -49.888 56.861  1 61.41 ? 560 VAL Z C     1 
ATOM   11139 O  O     . VAL F 1 560 ? 30.137  -49.686 55.774  1 61.49 ? 560 VAL Z O     1 
ATOM   11140 C  CB    . VAL F 1 560 ? 30.976  -50.812 58.811  1 61.98 ? 560 VAL Z CB    1 
ATOM   11141 C  CG1   . VAL F 1 560 ? 31.852  -51.57  57.82   1 62.59 ? 560 VAL Z CG1   1 
ATOM   11142 C  CG2   . VAL F 1 560 ? 31.771  -50.431 60.058  1 62.52 ? 560 VAL Z CG2   1 
ATOM   11143 N  N     . GLN F 1 561 ? 28.334  -50.325 56.974  1 61.44 ? 561 GLN Z N     1 
ATOM   11144 C  CA    . GLN F 1 561 ? 27.494  -50.654 55.819  1 61.99 ? 561 GLN Z CA    1 
ATOM   11145 C  C     . GLN F 1 561 ? 27.232  -49.453 54.915  1 62.57 ? 561 GLN Z C     1 
ATOM   11146 O  O     . GLN F 1 561 ? 27.133  -49.619 53.698  1 62.87 ? 561 GLN Z O     1 
ATOM   11147 C  CB    . GLN F 1 561 ? 26.166  -51.272 56.264  1 63.26 ? 561 GLN Z CB    1 
ATOM   11148 C  CG    . GLN F 1 561 ? 26.311  -52.655 56.864  1 65.8  ? 561 GLN Z CG    1 
ATOM   11149 C  CD    . GLN F 1 561 ? 24.983  -53.15  57.361  1 69.51 ? 561 GLN Z CD    1 
ATOM   11150 O  OE1   . GLN F 1 561 ? 24.633  -52.997 58.537  1 71.04 ? 561 GLN Z OE1   1 
ATOM   11151 N  NE2   . GLN F 1 561 ? 24.208  -53.748 56.467  1 69.73 ? 561 GLN Z NE2   1 
ATOM   11152 N  N     . LEU F 1 562 ? 27.133  -48.248 55.493  1 62.58 ? 562 LEU Z N     1 
ATOM   11153 C  CA    . LEU F 1 562 ? 26.918  -47.044 54.695  1 63.15 ? 562 LEU Z CA    1 
ATOM   11154 C  C     . LEU F 1 562 ? 28.128  -46.782 53.803  1 63.64 ? 562 LEU Z C     1 
ATOM   11155 O  O     . LEU F 1 562 ? 27.964  -46.486 52.621  1 63.74 ? 562 LEU Z O     1 
ATOM   11156 C  CB    . LEU F 1 562 ? 26.646  -45.826 55.59   1 63.32 ? 562 LEU Z CB    1 
ATOM   11157 C  CG    . LEU F 1 562 ? 25.38   -45.867 56.43   1 64.7  ? 562 LEU Z CG    1 
ATOM   11158 C  CD1   . LEU F 1 562 ? 25.241  -44.604 57.253  1 65.21 ? 562 LEU Z CD1   1 
ATOM   11159 C  CD2   . LEU F 1 562 ? 24.14   -46.113 55.574  1 65.38 ? 562 LEU Z CD2   1 
ATOM   11160 N  N     . ILE F 1 563 ? 29.34   -46.936 54.362  1 63.8  ? 563 ILE Z N     1 
ATOM   11161 C  CA    . ILE F 1 563 ? 30.586  -46.741 53.631  1 64.46 ? 563 ILE Z CA    1 
ATOM   11162 C  C     . ILE F 1 563 ? 30.708  -47.792 52.528  1 64.99 ? 563 ILE Z C     1 
ATOM   11163 O  O     . ILE F 1 563 ? 31.027  -47.454 51.388  1 65.01 ? 563 ILE Z O     1 
ATOM   11164 C  CB    . ILE F 1 563 ? 31.79   -46.777 54.605  1 64.96 ? 563 ILE Z CB    1 
ATOM   11165 C  CG1   . ILE F 1 563 ? 31.662  -45.694 55.697  1 65.84 ? 563 ILE Z CG1   1 
ATOM   11166 C  CG2   . ILE F 1 563 ? 33.115  -46.662 53.863  1 65.5  ? 563 ILE Z CG2   1 
ATOM   11167 C  CD1   . ILE F 1 563 ? 31.631  -44.291 55.199  1 67.11 ? 563 ILE Z CD1   1 
ATOM   11168 N  N     . LYS F 1 564 ? 30.391  -49.053 52.855  1 65.26 ? 564 LYS Z N     1 
ATOM   11169 C  CA    . LYS F 1 564 ? 30.45   -50.153 51.895  1 66.06 ? 564 LYS Z CA    1 
ATOM   11170 C  C     . LYS F 1 564 ? 29.474  -49.979 50.733  1 66.52 ? 564 LYS Z C     1 
ATOM   11171 O  O     . LYS F 1 564 ? 29.758  -50.456 49.637  1 66.64 ? 564 LYS Z O     1 
ATOM   11172 C  CB    . LYS F 1 564 ? 30.244  -51.511 52.581  1 68.06 ? 564 LYS Z CB    1 
ATOM   11173 C  CG    . LYS F 1 564 ? 31.3    -51.849 53.631  1 72.57 ? 564 LYS Z CG    1 
ATOM   11174 C  CD    . LYS F 1 564 ? 32.706  -51.963 53.053  1 77.31 ? 564 LYS Z CD    1 
ATOM   11175 C  CE    . LYS F 1 564 ? 33.716  -52.404 54.088  1 81.38 ? 564 LYS Z CE    1 
ATOM   11176 N  NZ    . LYS F 1 564 ? 33.967  -51.351 55.109  1 83.82 ? 564 LYS Z NZ    1 
ATOM   11177 N  N     . TYR F 1 565 ? 28.346  -49.281 50.951  1 66.57 ? 565 TYR Z N     1 
ATOM   11178 C  CA    . TYR F 1 565 ? 27.394  -49.037 49.866  1 67.06 ? 565 TYR Z CA    1 
ATOM   11179 C  C     . TYR F 1 565 ? 27.985  -48.057 48.859  1 67.14 ? 565 TYR Z C     1 
ATOM   11180 O  O     . TYR F 1 565 ? 27.836  -48.249 47.654  1 67.03 ? 565 TYR Z O     1 
ATOM   11181 C  CB    . TYR F 1 565 ? 26.063  -48.496 50.397  1 67.22 ? 565 TYR Z CB    1 
ATOM   11182 C  CG    . TYR F 1 565 ? 24.966  -48.486 49.35   1 68.02 ? 565 TYR Z CG    1 
ATOM   11183 C  CD1   . TYR F 1 565 ? 24.188  -49.61  49.119  1 68.86 ? 565 TYR Z CD1   1 
ATOM   11184 C  CD2   . TYR F 1 565 ? 24.707  -47.35  48.594  1 68.85 ? 565 TYR Z CD2   1 
ATOM   11185 C  CE1   . TYR F 1 565 ? 23.173  -49.603 48.169  1 69.68 ? 565 TYR Z CE1   1 
ATOM   11186 C  CE2   . TYR F 1 565 ? 23.705  -47.335 47.631  1 69.67 ? 565 TYR Z CE2   1 
ATOM   11187 C  CZ    . TYR F 1 565 ? 22.938  -48.464 47.421  1 70.52 ? 565 TYR Z CZ    1 
ATOM   11188 O  OH    . TYR F 1 565 ? 21.94   -48.45  46.474  1 71.94 ? 565 TYR Z OH    1 
ATOM   11189 N  N     . ILE F 1 566 ? 28.661  -47.01  49.351  1 67.24 ? 566 ILE Z N     1 
ATOM   11190 C  CA    . ILE F 1 566 ? 29.313  -46.024 48.495  1 67.84 ? 566 ILE Z CA    1 
ATOM   11191 C  C     . ILE F 1 566 ? 30.435  -46.71  47.708  1 68.59 ? 566 ILE Z C     1 
ATOM   11192 O  O     . ILE F 1 566 ? 30.559  -46.498 46.503  1 68.66 ? 566 ILE Z O     1 
ATOM   11193 C  CB    . ILE F 1 566 ? 29.827  -44.832 49.347  1 68.14 ? 566 ILE Z CB    1 
ATOM   11194 C  CG1   . ILE F 1 566 ? 28.691  -44.207 50.168  1 68.92 ? 566 ILE Z CG1   1 
ATOM   11195 C  CG2   . ILE F 1 566 ? 30.52   -43.783 48.498  1 68.51 ? 566 ILE Z CG2   1 
ATOM   11196 C  CD1   . ILE F 1 566 ? 27.547  -43.66  49.35   1 70.09 ? 566 ILE Z CD1   1 
ATOM   11197 N  N     . GLU F 1 567 ? 31.205  -47.584 48.38   1 68.99 ? 567 GLU Z N     1 
ATOM   11198 C  CA    . GLU F 1 567 ? 32.279  -48.352 47.758  1 69.89 ? 567 GLU Z CA    1 
ATOM   11199 C  C     . GLU F 1 567 ? 31.744  -49.274 46.653  1 70.76 ? 567 GLU Z C     1 
ATOM   11200 O  O     . GLU F 1 567 ? 32.405  -49.453 45.634  1 70.87 ? 567 GLU Z O     1 
ATOM   11201 C  CB    . GLU F 1 567 ? 33.046  -49.149 48.822  1 71.85 ? 567 GLU Z CB    1 
ATOM   11202 C  CG    . GLU F 1 567 ? 33.777  -48.257 49.812  1 75.81 ? 567 GLU Z CG    1 
ATOM   11203 C  CD    . GLU F 1 567 ? 34.657  -48.969 50.82   1 80.79 ? 567 GLU Z CD    1 
ATOM   11204 O  OE1   . GLU F 1 567 ? 34.679  -50.221 50.814  1 81.79 ? 567 GLU Z OE1   1 
ATOM   11205 O  OE2   . GLU F 1 567 ? 35.329  -48.275 51.616  1 82.4  ? 567 GLU Z OE2   1 
ATOM   11206 N  N     . TYR F 1 568 ? 30.535  -49.82  46.844  1 71.27 ? 568 TYR Z N     1 
ATOM   11207 C  CA    . TYR F 1 568 ? 29.845  -50.688 45.891  1 72.28 ? 568 TYR Z CA    1 
ATOM   11208 C  C     . TYR F 1 568 ? 29.532  -49.927 44.602  1 72.31 ? 568 TYR Z C     1 
ATOM   11209 O  O     . TYR F 1 568 ? 29.807  -50.437 43.52   1 72.33 ? 568 TYR Z O     1 
ATOM   11210 C  CB    . TYR F 1 568 ? 28.57   -51.267 46.543  1 73.02 ? 568 TYR Z CB    1 
ATOM   11211 C  CG    . TYR F 1 568 ? 27.55   -51.858 45.594  1 74.6  ? 568 TYR Z CG    1 
ATOM   11212 C  CD1   . TYR F 1 568 ? 27.783  -53.069 44.956  1 75.78 ? 568 TYR Z CD1   1 
ATOM   11213 C  CD2   . TYR F 1 568 ? 26.321  -51.245 45.396  1 75.87 ? 568 TYR Z CD2   1 
ATOM   11214 C  CE1   . TYR F 1 568 ? 26.838  -53.631 44.106  1 76.9  ? 568 TYR Z CE1   1 
ATOM   11215 C  CE2   . TYR F 1 568 ? 25.366  -51.799 44.548  1 76.97 ? 568 TYR Z CE2   1 
ATOM   11216 C  CZ    . TYR F 1 568 ? 25.628  -52.996 43.906  1 77.94 ? 568 TYR Z CZ    1 
ATOM   11217 O  OH    . TYR F 1 568 ? 24.693  -53.557 43.061  1 79.53 ? 568 TYR Z OH    1 
ATOM   11218 N  N     . LEU F 1 569 ? 29.001  -48.701 44.71   1 72.18 ? 569 LEU Z N     1 
ATOM   11219 C  CA    . LEU F 1 569 ? 28.704  -47.895 43.525  1 72.56 ? 569 LEU Z CA    1 
ATOM   11220 C  C     . LEU F 1 569 ? 29.973  -47.471 42.808  1 72.63 ? 569 LEU Z C     1 
ATOM   11221 O  O     . LEU F 1 569 ? 30.006  -47.457 41.581  1 72.69 ? 569 LEU Z O     1 
ATOM   11222 C  CB    . LEU F 1 569 ? 27.872  -46.666 43.886  1 72.94 ? 569 LEU Z CB    1 
ATOM   11223 C  CG    . LEU F 1 569 ? 26.509  -46.962 44.469  1 74.64 ? 569 LEU Z CG    1 
ATOM   11224 C  CD1   . LEU F 1 569 ? 25.824  -45.688 44.872  1 75.41 ? 569 LEU Z CD1   1 
ATOM   11225 C  CD2   . LEU F 1 569 ? 25.644  -47.732 43.484  1 75.23 ? 569 LEU Z CD2   1 
ATOM   11226 N  N     . PHE F 1 570 ? 31.027  -47.152 43.57   1 72.51 ? 570 PHE Z N     1 
ATOM   11227 C  CA    . PHE F 1 570 ? 32.314  -46.774 42.996  1 72.89 ? 570 PHE Z CA    1 
ATOM   11228 C  C     . PHE F 1 570 ? 32.946  -47.908 42.173  1 73.13 ? 570 PHE Z C     1 
ATOM   11229 O  O     . PHE F 1 570 ? 33.774  -47.632 41.308  1 73.32 ? 570 PHE Z O     1 
ATOM   11230 C  CB    . PHE F 1 570 ? 33.277  -46.266 44.075  1 72.86 ? 570 PHE Z CB    1 
ATOM   11231 C  CG    . PHE F 1 570 ? 33.04   -44.838 44.514  1 73.52 ? 570 PHE Z CG    1 
ATOM   11232 C  CD1   . PHE F 1 570 ? 32.606  -43.883 43.617  1 74.3  ? 570 PHE Z CD1   1 
ATOM   11233 C  CD2   . PHE F 1 570 ? 33.279  -44.448 45.818  1 74.22 ? 570 PHE Z CD2   1 
ATOM   11234 C  CE1   . PHE F 1 570 ? 32.412  -42.566 44.02   1 74.95 ? 570 PHE Z CE1   1 
ATOM   11235 C  CE2   . PHE F 1 570 ? 33.104  -43.127 46.21   1 74.84 ? 570 PHE Z CE2   1 
ATOM   11236 C  CZ    . PHE F 1 570 ? 32.652  -42.2   45.316  1 74.64 ? 570 PHE Z CZ    1 
ATOM   11237 N  N     . ASP F 1 571 ? 32.535  -49.174 42.409  1 72.97 ? 571 ASP Z N     1 
ATOM   11238 C  CA    . ASP F 1 571 ? 33.003  -50.324 41.626  1 73.33 ? 571 ASP Z CA    1 
ATOM   11239 C  C     . ASP F 1 571 ? 32.433  -50.335 40.188  1 72.88 ? 571 ASP Z C     1 
ATOM   11240 O  O     . ASP F 1 571 ? 32.847  -51.161 39.38   1 73.04 ? 571 ASP Z O     1 
ATOM   11241 C  CB    . ASP F 1 571 ? 32.649  -51.653 42.322  1 75.64 ? 571 ASP Z CB    1 
ATOM   11242 C  CG    . ASP F 1 571 ? 33.512  -51.997 43.522  1 81.21 ? 571 ASP Z CG    1 
ATOM   11243 O  OD1   . ASP F 1 571 ? 34.559  -51.338 43.71   1 82.38 ? 571 ASP Z OD1   1 
ATOM   11244 O  OD2   . ASP F 1 571 ? 33.142  -52.927 44.273  1 83.49 ? 571 ASP Z OD2   1 
ATOM   11245 N  N     . PHE F 1 572 ? 31.478  -49.447 39.877  1 72.16 ? 572 PHE Z N     1 
ATOM   11246 C  CA    . PHE F 1 572 ? 30.873  -49.361 38.559  1 71.94 ? 572 PHE Z CA    1 
ATOM   11247 C  C     . PHE F 1 572 ? 30.988  -47.956 38.001  1 71.6  ? 572 PHE Z C     1 
ATOM   11248 O  O     . PHE F 1 572 ? 31.035  -46.986 38.756  1 71.6  ? 572 PHE Z O     1 
ATOM   11249 C  CB    . PHE F 1 572 ? 29.402  -49.766 38.628  1 71.87 ? 572 PHE Z CB    1 
ATOM   11250 C  CG    . PHE F 1 572 ? 29.202  -51.15  39.186  1 72.57 ? 572 PHE Z CG    1 
ATOM   11251 C  CD1   . PHE F 1 572 ? 29.446  -52.267 38.41   1 73.4  ? 572 PHE Z CD1   1 
ATOM   11252 C  CD2   . PHE F 1 572 ? 28.79   -51.334 40.493  1 73.4  ? 572 PHE Z CD2   1 
ATOM   11253 C  CE1   . PHE F 1 572 ? 29.269  -53.541 38.927  1 74.16 ? 572 PHE Z CE1   1 
ATOM   11254 C  CE2   . PHE F 1 572 ? 28.629  -52.609 41.013  1 74.14 ? 572 PHE Z CE2   1 
ATOM   11255 C  CZ    . PHE F 1 572 ? 28.855  -53.705 40.221  1 73.97 ? 572 PHE Z CZ    1 
ATOM   11256 N  N     . THR F 1 573 ? 31.021  -47.847 36.672  1 71.23 ? 573 THR Z N     1 
ATOM   11257 C  CA    . THR F 1 573 ? 31.094  -46.569 35.975  1 71.36 ? 573 THR Z CA    1 
ATOM   11258 C  C     . THR F 1 573 ? 29.809  -45.788 36.254  1 71.43 ? 573 THR Z C     1 
ATOM   11259 O  O     . THR F 1 573 ? 28.73   -46.373 36.172  1 71.59 ? 573 THR Z O     1 
ATOM   11260 C  CB    . THR F 1 573 ? 31.236  -46.843 34.472  1 72.42 ? 573 THR Z CB    1 
ATOM   11261 O  OG1   . THR F 1 573 ? 32.455  -47.545 34.234  1 73.21 ? 573 THR Z OG1   1 
ATOM   11262 C  CG2   . THR F 1 573 ? 31.188  -45.577 33.635  1 72.92 ? 573 THR Z CG2   1 
ATOM   11263 N  N     . PRO F 1 574 ? 29.881  -44.486 36.612  1 71.16 ? 574 PRO Z N     1 
ATOM   11264 C  CA    . PRO F 1 574 ? 28.64   -43.723 36.861  1 71.24 ? 574 PRO Z CA    1 
ATOM   11265 C  C     . PRO F 1 574 ? 27.705  -43.747 35.659  1 71.53 ? 574 PRO Z C     1 
ATOM   11266 O  O     . PRO F 1 574 ? 28.185  -43.769 34.53   1 71.72 ? 574 PRO Z O     1 
ATOM   11267 C  CB    . PRO F 1 574 ? 29.13   -42.29  37.1    1 71.86 ? 574 PRO Z CB    1 
ATOM   11268 C  CG    . PRO F 1 574 ? 30.558  -42.405 37.422  1 72.23 ? 574 PRO Z CG    1 
ATOM   11269 C  CD    . PRO F 1 574 ? 31.08   -43.645 36.765  1 70.6  ? 574 PRO Z CD    1 
ATOM   11270 N  N     . SER F 1 575 ? 26.385  -43.753 35.883  1 71.48 ? 575 SER Z N     1 
ATOM   11271 C  CA    . SER F 1 575 ? 25.431  -43.788 34.777  1 71.93 ? 575 SER Z CA    1 
ATOM   11272 C  C     . SER F 1 575 ? 25.605  -42.596 33.824  1 72.19 ? 575 SER Z C     1 
ATOM   11273 O  O     . SER F 1 575 ? 25.691  -42.773 32.61   1 72.15 ? 575 SER Z O     1 
ATOM   11274 C  CB    . SER F 1 575 ? 24.001  -43.847 35.302  1 73.19 ? 575 SER Z CB    1 
ATOM   11275 O  OG    . SER F 1 575 ? 23.826  -44.941 36.187  1 75.34 ? 575 SER Z OG    1 
ATOM   11276 N  N     . VAL F 1 576 ? 25.719  -41.396 34.381  1 72.27 ? 576 VAL Z N     1 
ATOM   11277 C  CA    . VAL F 1 576 ? 25.86   -40.183 33.586  1 72.89 ? 576 VAL Z CA    1 
ATOM   11278 C  C     . VAL F 1 576 ? 26.9    -39.219 34.183  1 73.48 ? 576 VAL Z C     1 
ATOM   11279 O  O     . VAL F 1 576 ? 27.319  -39.39  35.325  1 73.57 ? 576 VAL Z O     1 
ATOM   11280 C  CB    . VAL F 1 576 ? 24.483  -39.483 33.408  1 73.61 ? 576 VAL Z CB    1 
ATOM   11281 C  CG1   . VAL F 1 576 ? 23.609  -40.197 32.384  1 74.16 ? 576 VAL Z CG1   1 
ATOM   11282 C  CG2   . VAL F 1 576 ? 23.763  -39.329 34.744  1 74.09 ? 576 VAL Z CG2   1 
ATOM   11283 N  N     . GLN F 1 577 ? 27.315  -38.206 33.398  1 73.76 ? 577 GLN Z N     1 
ATOM   11284 C  CA    . GLN F 1 577 ? 28.252  -37.167 33.814  1 74.62 ? 577 GLN Z CA    1 
ATOM   11285 C  C     . GLN F 1 577 ? 28.031  -35.877 33.009  1 75.46 ? 577 GLN Z C     1 
ATOM   11286 O  O     . GLN F 1 577 ? 27.533  -35.927 31.887  1 75.66 ? 577 GLN Z O     1 
ATOM   11287 C  CB    . GLN F 1 577 ? 29.713  -37.648 33.7    1 75.98 ? 577 GLN Z CB    1 
ATOM   11288 C  CG    . GLN F 1 577 ? 30.238  -37.785 32.27   1 78.92 ? 577 GLN Z CG    1 
ATOM   11289 C  CD    . GLN F 1 577 ? 31.158  -36.651 31.873  1 82.67 ? 577 GLN Z CD    1 
ATOM   11290 O  OE1   . GLN F 1 577 ? 31.766  -35.985 32.715  1 83.89 ? 577 GLN Z OE1   1 
ATOM   11291 N  NE2   . GLN F 1 577 ? 31.279  -36.401 30.578  1 83.13 ? 577 GLN Z NE2   1 
ATOM   11292 N  N     . ARG F 1 578 ? 28.403  -34.725 33.573  1 75.77 ? 578 ARG Z N     1 
ATOM   11293 C  CA    . ARG F 1 578 ? 28.263  -33.445 32.88   1 76.58 ? 578 ARG Z CA    1 
ATOM   11294 C  C     . ARG F 1 578 ? 29.212  -32.387 33.434  1 77.32 ? 578 ARG Z C     1 
ATOM   11295 O  O     . ARG F 1 578 ? 29.633  -32.477 34.587  1 77.51 ? 578 ARG Z O     1 
ATOM   11296 C  CB    . ARG F 1 578 ? 26.81   -32.933 32.938  1 77.88 ? 578 ARG Z CB    1 
ATOM   11297 C  CG    . ARG F 1 578 ? 26.335  -32.549 34.333  1 80.7  ? 578 ARG Z CG    1 
ATOM   11298 C  CD    . ARG F 1 578 ? 25.192  -31.557 34.272  1 83.38 ? 578 ARG Z CD    1 
ATOM   11299 N  NE    . ARG F 1 578 ? 24.773  -31.114 35.604  1 85.57 ? 578 ARG Z NE    1 
ATOM   11300 C  CZ    . ARG F 1 578 ? 23.913  -30.126 35.829  1 87.48 ? 578 ARG Z CZ    1 
ATOM   11301 N  NH1   . ARG F 1 578 ? 23.378  -29.457 34.815  1 87.08 ? 578 ARG Z NH1   1 
ATOM   11302 N  NH2   . ARG F 1 578 ? 23.586  -29.794 37.07   1 87.45 ? 578 ARG Z NH2   1 
ATOM   11303 N  N     . LYS F 1 579 ? 29.552  -31.381 32.62   1 77.66 ? 579 LYS Z N     1 
ATOM   11304 C  CA    . LYS F 1 579 ? 30.404  -30.29  33.086  1 78.62 ? 579 LYS Z CA    1 
ATOM   11305 C  C     . LYS F 1 579 ? 29.522  -29.261 33.807  1 79.35 ? 579 LYS Z C     1 
ATOM   11306 O  O     . LYS F 1 579 ? 28.381  -29.041 33.396  1 79.52 ? 579 LYS Z O     1 
ATOM   11307 C  CB    . LYS F 1 579 ? 31.167  -29.643 31.915  1 80.62 ? 579 LYS Z CB    1 
ATOM   11308 C  CG    . LYS F 1 579 ? 32.125  -28.533 32.345  1 84.71 ? 579 LYS Z CG    1 
ATOM   11309 C  CD    . LYS F 1 579 ? 32.98   -28.016 31.199  1 89.07 ? 579 LYS Z CD    1 
ATOM   11310 C  CE    . LYS F 1 579 ? 34.149  -28.925 30.919  1 92.67 ? 579 LYS Z CE    1 
ATOM   11311 N  NZ    . LYS F 1 579 ? 34.99   -29.119 32.129  1 94.74 ? 579 LYS Z NZ    1 
ATOM   11312 N  N     . ILE F 1 580 ? 30.032  -28.643 34.884  1 79.57 ? 580 ILE Z N     1 
ATOM   11313 C  CA    . ILE F 1 580 ? 29.275  -27.648 35.645  1 80.24 ? 580 ILE Z CA    1 
ATOM   11314 C  C     . ILE F 1 580 ? 28.976  -26.368 34.828  1 80.68 ? 580 ILE Z C     1 
ATOM   11315 O  O     . ILE F 1 580 ? 28.021  -25.656 35.139  1 80.93 ? 580 ILE Z O     1 
ATOM   11316 C  CB    . ILE F 1 580 ? 29.968  -27.342 36.998  1 80.87 ? 580 ILE Z CB    1 
ATOM   11317 C  CG1   . ILE F 1 580 ? 28.975  -26.807 38.047  1 81.85 ? 580 ILE Z CG1   1 
ATOM   11318 C  CG2   . ILE F 1 580 ? 31.179  -26.43  36.836  1 81.4  ? 580 ILE Z CG2   1 
ATOM   11319 C  CD1   . ILE F 1 580 ? 27.8    -27.724 38.328  1 83.19 ? 580 ILE Z CD1   1 
ATOM   11320 N  N     . ALA F 1 581 ? 29.751  -26.101 33.765  1 80.59 ? 581 ALA Z N     1 
ATOM   11321 C  CA    . ALA F 1 581 ? 29.521  -24.932 32.924  1 81.07 ? 581 ALA Z CA    1 
ATOM   11322 C  C     . ALA F 1 581 ? 28.607  -25.274 31.743  1 81.18 ? 581 ALA Z C     1 
ATOM   11323 O  O     . ALA F 1 581 ? 27.707  -24.5   31.423  1 81.35 ? 581 ALA Z O     1 
ATOM   11324 C  CB    . ALA F 1 581 ? 30.846  -24.369 32.429  1 81.39 ? 581 ALA Z CB    1 
ATOM   11325 N  N     . GLY F 1 582 ? 28.838  -26.428 31.119  1 80.97 ? 582 GLY Z N     1 
ATOM   11326 C  CA    . GLY F 1 582 ? 28.046  -26.888 29.985  1 81.27 ? 582 GLY Z CA    1 
ATOM   11327 C  C     . GLY F 1 582 ? 26.629  -27.255 30.375  1 81.37 ? 582 GLY Z C     1 
ATOM   11328 O  O     . GLY F 1 582 ? 25.668  -26.696 29.844  1 81.5  ? 582 GLY Z O     1 
ATOM   11329 N  N     . GLY F 1 583 ? 26.502  -28.187 31.314  1 81.17 ? 583 GLY Z N     1 
ATOM   11330 C  CA    . GLY F 1 583 ? 25.208  -28.624 31.824  1 81.37 ? 583 GLY Z CA    1 
ATOM   11331 C  C     . GLY F 1 583 ? 24.537  -29.74  31.047  1 81.23 ? 583 GLY Z C     1 
ATOM   11332 O  O     . GLY F 1 583 ? 23.513  -30.267 31.486  1 81.33 ? 583 GLY Z O     1 
ATOM   11333 N  N     . ASN F 1 584 ? 25.092  -30.109 29.885  1 80.81 ? 584 ASN Z N     1 
ATOM   11334 C  CA    . ASN F 1 584 ? 24.512  -31.166 29.062  1 80.77 ? 584 ASN Z CA    1 
ATOM   11335 C  C     . ASN F 1 584 ? 24.977  -32.535 29.547  1 80.13 ? 584 ASN Z C     1 
ATOM   11336 O  O     . ASN F 1 584 ? 26.176  -32.812 29.551  1 80.21 ? 584 ASN Z O     1 
ATOM   11337 C  CB    . ASN F 1 584 ? 24.873  -30.959 27.593  1 82.23 ? 584 ASN Z CB    1 
ATOM   11338 C  CG    . ASN F 1 584 ? 24.522  -29.584 27.076  1 85.75 ? 584 ASN Z CG    1 
ATOM   11339 O  OD1   . ASN F 1 584 ? 23.619  -28.908 27.586  1 87.06 ? 584 ASN Z OD1   1 
ATOM   11340 N  ND2   . ASN F 1 584 ? 25.232  -29.139 26.05   1 86.38 ? 584 ASN Z ND2   1 
ATOM   11341 N  N     . TRP F 1 585 ? 24.033  -33.387 29.972  1 79.33 ? 585 TRP Z N     1 
ATOM   11342 C  CA    . TRP F 1 585 ? 24.364  -34.718 30.475  1 78.97 ? 585 TRP Z CA    1 
ATOM   11343 C  C     . TRP F 1 585 ? 24.817  -35.647 29.362  1 78.34 ? 585 TRP Z C     1 
ATOM   11344 O  O     . TRP F 1 585 ? 24.218  -35.668 28.294  1 78.54 ? 585 TRP Z O     1 
ATOM   11345 C  CB    . TRP F 1 585 ? 23.159  -35.36  31.186  1 78.93 ? 585 TRP Z CB    1 
ATOM   11346 C  CG    . TRP F 1 585 ? 22.798  -34.753 32.505  1 79.4  ? 585 TRP Z CG    1 
ATOM   11347 C  CD1   . TRP F 1 585 ? 21.747  -33.924 32.765  1 80.31 ? 585 TRP Z CD1   1 
ATOM   11348 C  CD2   . TRP F 1 585 ? 23.439  -34.995 33.761  1 79.53 ? 585 TRP Z CD2   1 
ATOM   11349 N  NE1   . TRP F 1 585 ? 21.711  -33.613 34.102  1 80.61 ? 585 TRP Z NE1   1 
ATOM   11350 C  CE2   . TRP F 1 585 ? 22.74   -34.258 34.737  1 80.35 ? 585 TRP Z CE2   1 
ATOM   11351 C  CE3   . TRP F 1 585 ? 24.547  -35.754 34.153  1 80.1  ? 585 TRP Z CE3   1 
ATOM   11352 C  CZ2   . TRP F 1 585 ? 23.114  -34.256 36.077  1 81.03 ? 585 TRP Z CZ2   1 
ATOM   11353 C  CZ3   . TRP F 1 585 ? 24.912  -35.755 35.483  1 81.04 ? 585 TRP Z CZ3   1 
ATOM   11354 C  CH2   . TRP F 1 585 ? 24.2    -35.014 36.428  1 81.18 ? 585 TRP Z CH2   1 
ATOM   11355 N  N     . GLU F 1 586 ? 25.852  -36.435 29.631  1 77.48 ? 586 GLU Z N     1 
ATOM   11356 C  CA    . GLU F 1 586 ? 26.4    -37.446 28.73   1 77.16 ? 586 GLU Z CA    1 
ATOM   11357 C  C     . GLU F 1 586 ? 26.509  -38.778 29.489  1 76.48 ? 586 GLU Z C     1 
ATOM   11358 O  O     . GLU F 1 586 ? 26.422  -38.797 30.715  1 76.52 ? 586 GLU Z O     1 
ATOM   11359 C  CB    . GLU F 1 586 ? 27.798  -37.029 28.236  1 79.24 ? 586 GLU Z CB    1 
ATOM   11360 C  CG    . GLU F 1 586 ? 27.792  -35.967 27.153  1 83.4  ? 586 GLU Z CG    1 
ATOM   11361 C  CD    . GLU F 1 586 ? 28.995  -35.985 26.226  1 88.24 ? 586 GLU Z CD    1 
ATOM   11362 O  OE1   . GLU F 1 586 ? 29.896  -36.833 26.425  1 88.93 ? 586 GLU Z OE1   1 
ATOM   11363 O  OE2   . GLU F 1 586 ? 29.034  -35.153 25.292  1 89.86 ? 586 GLU Z OE2   1 
ATOM   11364 N  N     . PHE F 1 587 ? 26.725  -39.885 28.774  1 75.73 ? 587 PHE Z N     1 
ATOM   11365 C  CA    . PHE F 1 587 ? 26.92   -41.183 29.413  1 75.45 ? 587 PHE Z CA    1 
ATOM   11366 C  C     . PHE F 1 587 ? 28.256  -41.191 30.173  1 75.38 ? 587 PHE Z C     1 
ATOM   11367 O  O     . PHE F 1 587 ? 29.206  -40.529 29.756  1 75.5  ? 587 PHE Z O     1 
ATOM   11368 C  CB    . PHE F 1 587 ? 26.92   -42.299 28.358  1 75.06 ? 587 PHE Z CB    1 
ATOM   11369 C  CG    . PHE F 1 587 ? 25.547  -42.69  27.867  1 75.34 ? 587 PHE Z CG    1 
ATOM   11370 C  CD1   . PHE F 1 587 ? 24.524  -42.941 28.761  1 76.07 ? 587 PHE Z CD1   1 
ATOM   11371 C  CD2   . PHE F 1 587 ? 25.296  -42.851 26.517  1 75.9  ? 587 PHE Z CD2   1 
ATOM   11372 C  CE1   . PHE F 1 587 ? 23.272  -43.321 28.315  1 76.67 ? 587 PHE Z CE1   1 
ATOM   11373 C  CE2   . PHE F 1 587 ? 24.044  -43.238 26.074  1 76.5  ? 587 PHE Z CE2   1 
ATOM   11374 C  CZ    . PHE F 1 587 ? 23.041  -43.472 26.976  1 76.32 ? 587 PHE Z CZ    1 
ATOM   11375 N  N     . GLY F 1 588 ? 28.314  -41.925 31.279  1 75.07 ? 588 GLY Z N     1 
ATOM   11376 C  CA    . GLY F 1 588 ? 29.523  -42.023 32.087  1 75.25 ? 588 GLY Z CA    1 
ATOM   11377 C  C     . GLY F 1 588 ? 30.647  -42.72  31.353  1 75.24 ? 588 GLY Z C     1 
ATOM   11378 O  O     . GLY F 1 588 ? 30.432  -43.766 30.74   1 75.28 ? 588 GLY Z O     1 
ATOM   11379 N  N     . ASN F 1 589 ? 31.848  -42.133 31.383  1 75.06 ? 589 ASN Z N     1 
ATOM   11380 C  CA    . ASN F 1 589 ? 32.997  -42.691 30.672  1 75.29 ? 589 ASN Z CA    1 
ATOM   11381 C  C     . ASN F 1 589 ? 34.093  -43.172 31.627  1 74.88 ? 589 ASN Z C     1 
ATOM   11382 O  O     . ASN F 1 589 ? 34.669  -44.239 31.416  1 74.86 ? 589 ASN Z O     1 
ATOM   11383 C  CB    . ASN F 1 589 ? 33.556  -41.65  29.684  1 76.71 ? 589 ASN Z CB    1 
ATOM   11384 C  CG    . ASN F 1 589 ? 34.818  -42.065 28.96   1 80.16 ? 589 ASN Z CG    1 
ATOM   11385 O  OD1   . ASN F 1 589 ? 34.96   -43.202 28.495  1 81.28 ? 589 ASN Z OD1   1 
ATOM   11386 N  ND2   . ASN F 1 589 ? 35.763  -41.142 28.854  1 80.94 ? 589 ASN Z ND2   1 
ATOM   11387 N  N     . LYS F 1 590 ? 34.406  -42.37  32.65   1 74.33 ? 590 LYS Z N     1 
ATOM   11388 C  CA    . LYS F 1 590 ? 35.465  -42.703 33.594  1 74.21 ? 590 LYS Z CA    1 
ATOM   11389 C  C     . LYS F 1 590 ? 34.917  -43.205 34.918  1 73.79 ? 590 LYS Z C     1 
ATOM   11390 O  O     . LYS F 1 590 ? 33.886  -42.725 35.384  1 73.96 ? 590 LYS Z O     1 
ATOM   11391 C  CB    . LYS F 1 590 ? 36.362  -41.483 33.839  1 76.04 ? 590 LYS Z CB    1 
ATOM   11392 C  CG    . LYS F 1 590 ? 37.007  -40.932 32.575  1 80.04 ? 590 LYS Z CG    1 
ATOM   11393 C  CD    . LYS F 1 590 ? 37.746  -39.636 32.861  1 84.14 ? 590 LYS Z CD    1 
ATOM   11394 C  CE    . LYS F 1 590 ? 38.351  -39.032 31.623  1 87.48 ? 590 LYS Z CE    1 
ATOM   11395 N  NZ    . LYS F 1 590 ? 39.078  -37.775 31.936  1 89.59 ? 590 LYS Z NZ    1 
ATOM   11396 N  N     . SER F 1 591 ? 35.629  -44.146 35.543  1 73.06 ? 591 SER Z N     1 
ATOM   11397 C  CA    . SER F 1 591 ? 35.234  -44.701 36.834  1 72.76 ? 591 SER Z CA    1 
ATOM   11398 C  C     . SER F 1 591 ? 35.732  -43.844 37.998  1 72.11 ? 591 SER Z C     1 
ATOM   11399 O  O     . SER F 1 591 ? 36.738  -43.147 37.875  1 72.16 ? 591 SER Z O     1 
ATOM   11400 C  CB    . SER F 1 591 ? 35.768  -46.123 36.984  1 74.06 ? 591 SER Z CB    1 
ATOM   11401 O  OG    . SER F 1 591 ? 34.745  -47.088 36.803  1 76.21 ? 591 SER Z OG    1 
ATOM   11402 N  N     . LEU F 1 592 ? 35.04   -43.91  39.135  1 71.39 ? 592 LEU Z N     1 
ATOM   11403 C  CA    . LEU F 1 592 ? 35.446  -43.168 40.325  1 71.17 ? 592 LEU Z CA    1 
ATOM   11404 C  C     . LEU F 1 592 ? 35.976  -44.145 41.381  1 70.59 ? 592 LEU Z C     1 
ATOM   11405 O  O     . LEU F 1 592 ? 35.472  -45.261 41.5    1 70.52 ? 592 LEU Z O     1 
ATOM   11406 C  CB    . LEU F 1 592 ? 34.283  -42.344 40.889  1 71.46 ? 592 LEU Z CB    1 
ATOM   11407 C  CG    . LEU F 1 592 ? 34.124  -40.916 40.371  1 73.07 ? 592 LEU Z CG    1 
ATOM   11408 C  CD1   . LEU F 1 592 ? 33.696  -40.901 38.919  1 73.71 ? 592 LEU Z CD1   1 
ATOM   11409 C  CD2   . LEU F 1 592 ? 33.105  -40.157 41.199  1 73.72 ? 592 LEU Z CD2   1 
ATOM   11410 N  N     . VAL F 1 593 ? 37.011  -43.737 42.126  1 69.94 ? 593 VAL Z N     1 
ATOM   11411 C  CA    . VAL F 1 593 ? 37.642  -44.584 43.139  1 69.74 ? 593 VAL Z CA    1 
ATOM   11412 C  C     . VAL F 1 593 ? 37.413  -44.031 44.558  1 69.29 ? 593 VAL Z C     1 
ATOM   11413 O  O     . VAL F 1 593 ? 37.557  -42.827 44.786  1 69.52 ? 593 VAL Z O     1 
ATOM   11414 C  CB    . VAL F 1 593 ? 39.144  -44.787 42.81   1 70.51 ? 593 VAL Z CB    1 
ATOM   11415 C  CG1   . VAL F 1 593 ? 39.864  -45.553 43.915  1 71.08 ? 593 VAL Z CG1   1 
ATOM   11416 C  CG2   . VAL F 1 593 ? 39.314  -45.493 41.469  1 71.04 ? 593 VAL Z CG2   1 
ATOM   11417 N  N     . PRO F 1 594 ? 37.029  -44.898 45.521  1 68.43 ? 594 PRO Z N     1 
ATOM   11418 C  CA    . PRO F 1 594 ? 36.765  -44.415 46.889  1 67.85 ? 594 PRO Z CA    1 
ATOM   11419 C  C     . PRO F 1 594 ? 37.911  -43.688 47.587  1 67.13 ? 594 PRO Z C     1 
ATOM   11420 O  O     . PRO F 1 594 ? 37.65   -42.788 48.383  1 67.38 ? 594 PRO Z O     1 
ATOM   11421 C  CB    . PRO F 1 594 ? 36.371  -45.683 47.654  1 68.69 ? 594 PRO Z CB    1 
ATOM   11422 C  CG    . PRO F 1 594 ? 36.027  -46.686 46.623  1 69.25 ? 594 PRO Z CG    1 
ATOM   11423 C  CD    . PRO F 1 594 ? 36.794  -46.349 45.395  1 67.79 ? 594 PRO Z CD    1 
ATOM   11424 N  N     . ASN F 1 595 ? 39.168  -44.062 47.304  1 66.1  ? 595 ASN Z N     1 
ATOM   11425 C  CA    . ASN F 1 595 ? 40.312  -43.408 47.944  1 65.55 ? 595 ASN Z CA    1 
ATOM   11426 C  C     . ASN F 1 595 ? 40.534  -41.954 47.489  1 64.67 ? 595 ASN Z C     1 
ATOM   11427 O  O     . ASN F 1 595 ? 41.337  -41.248 48.093  1 64.71 ? 595 ASN Z O     1 
ATOM   11428 C  CB    . ASN F 1 595 ? 41.58   -44.233 47.806  1 66.64 ? 595 ASN Z CB    1 
ATOM   11429 C  CG    . ASN F 1 595 ? 42.363  -44.307 49.091  1 69.69 ? 595 ASN Z CG    1 
ATOM   11430 O  OD1   . ASN F 1 595 ? 42.546  -43.307 49.791  1 70.87 ? 595 ASN Z OD1   1 
ATOM   11431 N  ND2   . ASN F 1 595 ? 42.843  -45.497 49.427  1 70.27 ? 595 ASN Z ND2   1 
ATOM   11432 N  N     . ASP F 1 596 ? 39.807  -41.493 46.463  1 63.82 ? 596 ASP Z N     1 
ATOM   11433 C  CA    . ASP F 1 596 ? 39.885  -40.094 46.037  1 63.74 ? 596 ASP Z CA    1 
ATOM   11434 C  C     . ASP F 1 596 ? 39.035  -39.167 46.952  1 63.25 ? 596 ASP Z C     1 
ATOM   11435 O  O     . ASP F 1 596 ? 39.048  -37.949 46.773  1 63.47 ? 596 ASP Z O     1 
ATOM   11436 C  CB    . ASP F 1 596 ? 39.404  -39.96  44.582  1 65.44 ? 596 ASP Z CB    1 
ATOM   11437 C  CG    . ASP F 1 596 ? 40.085  -38.866 43.782  1 69.46 ? 596 ASP Z CG    1 
ATOM   11438 O  OD1   . ASP F 1 596 ? 40.808  -38.047 44.389  1 70.08 ? 596 ASP Z OD1   1 
ATOM   11439 O  OD2   . ASP F 1 596 ? 39.893  -38.826 42.548  1 71.39 ? 596 ASP Z OD2   1 
ATOM   11440 N  N     . PHE F 1 597 ? 38.292  -39.748 47.917  1 62.43 ? 597 PHE Z N     1 
ATOM   11441 C  CA    . PHE F 1 597 ? 37.403  -39.041 48.826  1 61.96 ? 597 PHE Z CA    1 
ATOM   11442 C  C     . PHE F 1 597 ? 37.608  -39.484 50.271  1 61.1  ? 597 PHE Z C     1 
ATOM   11443 O  O     . PHE F 1 597 ? 38.109  -40.577 50.532  1 61.11 ? 597 PHE Z O     1 
ATOM   11444 C  CB    . PHE F 1 597 ? 35.94   -39.325 48.425  1 61.95 ? 597 PHE Z CB    1 
ATOM   11445 C  CG    . PHE F 1 597 ? 35.626  -39.023 46.983  1 62.74 ? 597 PHE Z CG    1 
ATOM   11446 C  CD1   . PHE F 1 597 ? 35.49   -37.72  46.548  1 63.62 ? 597 PHE Z CD1   1 
ATOM   11447 C  CD2   . PHE F 1 597 ? 35.487  -40.043 46.059  1 63.49 ? 597 PHE Z CD2   1 
ATOM   11448 C  CE1   . PHE F 1 597 ? 35.223  -37.442 45.22   1 64.33 ? 597 PHE Z CE1   1 
ATOM   11449 C  CE2   . PHE F 1 597 ? 35.217  -39.761 44.731  1 64.22 ? 597 PHE Z CE2   1 
ATOM   11450 C  CZ    . PHE F 1 597 ? 35.091  -38.463 44.319  1 64.09 ? 597 PHE Z CZ    1 
ATOM   11451 N  N     . ILE F 1 598 ? 37.196  -38.639 51.213  1 60.27 ? 598 ILE Z N     1 
ATOM   11452 C  CA    . ILE F 1 598 ? 37.228  -38.983 52.621  1 60.01 ? 598 ILE Z CA    1 
ATOM   11453 C  C     . ILE F 1 598 ? 35.818  -39.482 52.905  1 59.49 ? 598 ILE Z C     1 
ATOM   11454 O  O     . ILE F 1 598 ? 34.868  -38.726 52.71   1 59.69 ? 598 ILE Z O     1 
ATOM   11455 C  CB    . ILE F 1 598 ? 37.566  -37.749 53.485  1 60.53 ? 598 ILE Z CB    1 
ATOM   11456 C  CG1   . ILE F 1 598 ? 38.899  -37.109 53.066  1 61.41 ? 598 ILE Z CG1   1 
ATOM   11457 C  CG2   . ILE F 1 598 ? 37.552  -38.104 54.963  1 61.06 ? 598 ILE Z CG2   1 
ATOM   11458 C  CD1   . ILE F 1 598 ? 40.093  -38.004 53.182  1 62.68 ? 598 ILE Z CD1   1 
ATOM   11459 N  N     . LEU F 1 599 ? 35.662  -40.759 53.283  1 58.65 ? 599 LEU Z N     1 
ATOM   11460 C  CA    . LEU F 1 599 ? 34.333  -41.308 53.542  1 58.22 ? 599 LEU Z CA    1 
ATOM   11461 C  C     . LEU F 1 599 ? 34.051  -41.368 55.032  1 57.58 ? 599 LEU Z C     1 
ATOM   11462 O  O     . LEU F 1 599 ? 34.792  -42.005 55.777  1 57.62 ? 599 LEU Z O     1 
ATOM   11463 C  CB    . LEU F 1 599 ? 34.165  -42.707 52.915  1 58.35 ? 599 LEU Z CB    1 
ATOM   11464 C  CG    . LEU F 1 599 ? 34.361  -42.822 51.403  1 59.64 ? 599 LEU Z CG    1 
ATOM   11465 C  CD1   . LEU F 1 599 ? 34.172  -44.25  50.939  1 60.14 ? 599 LEU Z CD1   1 
ATOM   11466 C  CD2   . LEU F 1 599 ? 33.402  -41.939 50.654  1 60.26 ? 599 LEU Z CD2   1 
ATOM   11467 N  N     . LEU F 1 600 ? 32.984  -40.704 55.469  1 56.86 ? 600 LEU Z N     1 
ATOM   11468 C  CA    . LEU F 1 600 ? 32.582  -40.727 56.868  1 56.67 ? 600 LEU Z CA    1 
ATOM   11469 C  C     . LEU F 1 600 ? 31.123  -41.149 56.968  1 56.29 ? 600 LEU Z C     1 
ATOM   11470 O  O     . LEU F 1 600 ? 30.33   -40.857 56.075  1 56.38 ? 600 LEU Z O     1 
ATOM   11471 C  CB    . LEU F 1 600 ? 32.753  -39.349 57.533  1 56.85 ? 600 LEU Z CB    1 
ATOM   11472 C  CG    . LEU F 1 600 ? 34.171  -38.819 57.716  1 58.36 ? 600 LEU Z CG    1 
ATOM   11473 C  CD1   . LEU F 1 600 ? 34.15   -37.471 58.408  1 58.86 ? 600 LEU Z CD1   1 
ATOM   11474 C  CD2   . LEU F 1 600 ? 35.033  -39.78  58.497  1 59.06 ? 600 LEU Z CD2   1 
ATOM   11475 N  N     . SER F 1 601 ? 30.763  -41.827 58.056  1 55.68 ? 601 SER Z N     1 
ATOM   11476 C  CA    . SER F 1 601 ? 29.379  -42.227 58.282  1 55.41 ? 601 SER Z CA    1 
ATOM   11477 C  C     . SER F 1 601 ? 28.827  -41.537 59.528  1 54.78 ? 601 SER Z C     1 
ATOM   11478 O  O     . SER F 1 601 ? 29.57   -41.24  60.461  1 54.74 ? 601 SER Z O     1 
ATOM   11479 C  CB    . SER F 1 601 ? 29.259  -43.74  58.408  1 56.61 ? 601 SER Z CB    1 
ATOM   11480 O  OG    . SER F 1 601 ? 30.036  -44.222 59.492  1 58.4  ? 601 SER Z OG    1 
ATOM   11481 N  N     . ALA F 1 602 ? 27.53   -41.253 59.528  1 54.19 ? 602 ALA Z N     1 
ATOM   11482 C  CA    . ALA F 1 602 ? 26.89   -40.57  60.639  1 54.04 ? 602 ALA Z CA    1 
ATOM   11483 C  C     . ALA F 1 602 ? 25.505  -41.126 60.919  1 53.6  ? 602 ALA Z C     1 
ATOM   11484 O  O     . ALA F 1 602 ? 24.797  -41.548 60.008  1 53.85 ? 602 ALA Z O     1 
ATOM   11485 C  CB    . ALA F 1 602 ? 26.805  -39.076 60.361  1 54.16 ? 602 ALA Z CB    1 
ATOM   11486 N  N     . GLY F 1 603 ? 25.13   -41.12  62.182  1 52.81 ? 603 GLY Z N     1 
ATOM   11487 C  CA    . GLY F 1 603 ? 23.813  -41.569 62.591  1 52.57 ? 603 GLY Z CA    1 
ATOM   11488 C  C     . GLY F 1 603 ? 23.078  -40.406 63.211  1 52.1  ? 603 GLY Z C     1 
ATOM   11489 O  O     . GLY F 1 603 ? 23.599  -39.782 64.131  1 52.09 ? 603 GLY Z O     1 
ATOM   11490 N  N     . ALA F 1 604 ? 21.897  -40.062 62.689  1 51.64 ? 604 ALA Z N     1 
ATOM   11491 C  CA    . ALA F 1 604 ? 21.118  -38.948 63.227  1 51.8  ? 604 ALA Z CA    1 
ATOM   11492 C  C     . ALA F 1 604 ? 19.85   -39.48  63.879  1 51.83 ? 604 ALA Z C     1 
ATOM   11493 O  O     . ALA F 1 604 ? 19.216  -40.38  63.335  1 52.19 ? 604 ALA Z O     1 
ATOM   11494 C  CB    . ALA F 1 604 ? 20.774  -37.961 62.125  1 51.96 ? 604 ALA Z CB    1 
ATOM   11495 N  N     . PHE F 1 605 ? 19.481  -38.939 65.036  1 51.3  ? 605 PHE Z N     1 
ATOM   11496 C  CA    . PHE F 1 605 ? 18.317  -39.423 65.774  1 51.49 ? 605 PHE Z CA    1 
ATOM   11497 C  C     . PHE F 1 605 ? 17.795  -38.378 66.764  1 51.98 ? 605 PHE Z C     1 
ATOM   11498 O  O     . PHE F 1 605 ? 18.469  -37.386 67.025  1 52.07 ? 605 PHE Z O     1 
ATOM   11499 C  CB    . PHE F 1 605 ? 18.688  -40.723 66.532  1 51.19 ? 605 PHE Z CB    1 
ATOM   11500 C  CG    . PHE F 1 605 ? 19.949  -40.601 67.356  1 51.45 ? 605 PHE Z CG    1 
ATOM   11501 C  CD1   . PHE F 1 605 ? 19.926  -40.007 68.604  1 52.04 ? 605 PHE Z CD1   1 
ATOM   11502 C  CD2   . PHE F 1 605 ? 21.161  -41.045 66.864  1 51.96 ? 605 PHE Z CD2   1 
ATOM   11503 C  CE1   . PHE F 1 605 ? 21.09   -39.857 69.339  1 52.6  ? 605 PHE Z CE1   1 
ATOM   11504 C  CE2   . PHE F 1 605 ? 22.322  -40.899 67.606  1 52.55 ? 605 PHE Z CE2   1 
ATOM   11505 C  CZ    . PHE F 1 605 ? 22.279  -40.311 68.841  1 52.35 ? 605 PHE Z CZ    1 
ATOM   11506 N  N     . ILE F 1 606 ? 16.617  -38.621 67.353  1 52.17 ? 606 ILE Z N     1 
ATOM   11507 C  CA    . ILE F 1 606 ? 16.069  -37.725 68.361  1 52.86 ? 606 ILE Z CA    1 
ATOM   11508 C  C     . ILE F 1 606 ? 16.387  -38.265 69.755  1 53.66 ? 606 ILE Z C     1 
ATOM   11509 O  O     . ILE F 1 606 ? 16.09   -39.42  70.048  1 53.89 ? 606 ILE Z O     1 
ATOM   11510 C  CB    . ILE F 1 606 ? 14.557  -37.455 68.146  1 53.28 ? 606 ILE Z CB    1 
ATOM   11511 C  CG1   . ILE F 1 606 ? 14.334  -36.578 66.905  1 54.09 ? 606 ILE Z CG1   1 
ATOM   11512 C  CG2   . ILE F 1 606 ? 13.923  -36.807 69.379  1 53.81 ? 606 ILE Z CG2   1 
ATOM   11513 C  CD1   . ILE F 1 606 ? 12.922  -36.575 66.382  1 55.23 ? 606 ILE Z CD1   1 
ATOM   11514 N  N     . ASP F 1 607 ? 17.007  -37.44  70.606  1 54.01 ? 607 ASP Z N     1 
ATOM   11515 C  CA    . ASP F 1 607 ? 17.338  -37.834 71.972  1 54.97 ? 607 ASP Z CA    1 
ATOM   11516 C  C     . ASP F 1 607 ? 17.083  -36.669 72.917  1 55.83 ? 607 ASP Z C     1 
ATOM   11517 O  O     . ASP F 1 607 ? 17.663  -35.605 72.735  1 55.94 ? 607 ASP Z O     1 
ATOM   11518 C  CB    . ASP F 1 607 ? 18.801  -38.28  72.084  1 56.54 ? 607 ASP Z CB    1 
ATOM   11519 C  CG    . ASP F 1 607 ? 19.203  -38.629 73.502  1 60.7  ? 607 ASP Z CG    1 
ATOM   11520 O  OD1   . ASP F 1 607 ? 18.639  -39.595 74.058  1 61.35 ? 607 ASP Z OD1   1 
ATOM   11521 O  OD2   . ASP F 1 607 ? 20.053  -37.91  74.071  1 62.75 ? 607 ASP Z OD2   1 
ATOM   11522 N  N     . TYR F 1 608 ? 16.272  -36.882 73.957  1 56.21 ? 608 TYR Z N     1 
ATOM   11523 C  CA    . TYR F 1 608 ? 15.968  -35.828 74.921  1 56.99 ? 608 TYR Z CA    1 
ATOM   11524 C  C     . TYR F 1 608 ? 16.932  -35.844 76.111  1 57.8  ? 608 TYR Z C     1 
ATOM   11525 O  O     . TYR F 1 608 ? 16.511  -36.02  77.254  1 57.99 ? 608 TYR Z O     1 
ATOM   11526 C  CB    . TYR F 1 608 ? 14.509  -35.925 75.373  1 56.98 ? 608 TYR Z CB    1 
ATOM   11527 C  CG    . TYR F 1 608 ? 13.537  -35.77  74.227  1 57.73 ? 608 TYR Z CG    1 
ATOM   11528 C  CD1   . TYR F 1 608 ? 13.226  -34.521 73.721  1 58.7  ? 608 TYR Z CD1   1 
ATOM   11529 C  CD2   . TYR F 1 608 ? 12.925  -36.875 73.655  1 58.69 ? 608 TYR Z CD2   1 
ATOM   11530 C  CE1   . TYR F 1 608 ? 12.328  -34.371 72.675  1 59.69 ? 608 TYR Z CE1   1 
ATOM   11531 C  CE2   . TYR F 1 608 ? 12.032  -36.739 72.6    1 59.66 ? 608 TYR Z CE2   1 
ATOM   11532 C  CZ    . TYR F 1 608 ? 11.739  -35.485 72.107  1 60.57 ? 608 TYR Z CZ    1 
ATOM   11533 O  OH    . TYR F 1 608 ? 10.863  -35.35  71.055  1 62    ? 608 TYR Z OH    1 
ATOM   11534 N  N     . ASP F 1 609 ? 18.231  -35.651 75.819  1 58.17 ? 609 ASP Z N     1 
ATOM   11535 C  CA    . ASP F 1 609 ? 19.368  -35.641 76.741  1 58.96 ? 609 ASP Z CA    1 
ATOM   11536 C  C     . ASP F 1 609 ? 19.437  -36.859 77.667  1 59.54 ? 609 ASP Z C     1 
ATOM   11537 O  O     . ASP F 1 609 ? 19.8    -36.728 78.837  1 59.84 ? 609 ASP Z O     1 
ATOM   11538 C  CB    . ASP F 1 609 ? 19.479  -34.326 77.542  1 60.57 ? 609 ASP Z CB    1 
ATOM   11539 C  CG    . ASP F 1 609 ? 20.741  -33.561 77.212  1 64.74 ? 609 ASP Z CG    1 
ATOM   11540 O  OD1   . ASP F 1 609 ? 20.762  -32.873 76.16   1 65.2  ? 609 ASP Z OD1   1 
ATOM   11541 O  OD2   . ASP F 1 609 ? 21.712  -33.652 77.997  1 66.87 ? 609 ASP Z OD2   1 
ATOM   11542 N  N     . ASN F 1 610 ? 19.125  -38.044 77.139  1 59.52 ? 610 ASN Z N     1 
ATOM   11543 C  CA    . ASN F 1 610 ? 19.225  -39.277 77.921  1 60.08 ? 610 ASN Z CA    1 
ATOM   11544 C  C     . ASN F 1 610 ? 20.531  -40.039 77.668  1 60.61 ? 610 ASN Z C     1 
ATOM   11545 O  O     . ASN F 1 610 ? 20.718  -41.102 78.261  1 61    ? 610 ASN Z O     1 
ATOM   11546 C  CB    . ASN F 1 610 ? 18.07   -40.225 77.65   1 61    ? 610 ASN Z CB    1 
ATOM   11547 C  CG    . ASN F 1 610 ? 16.695  -39.648 77.743  1 63.74 ? 610 ASN Z CG    1 
ATOM   11548 O  OD1   . ASN F 1 610 ? 15.833  -40.05  76.983  1 64.78 ? 610 ASN Z OD1   1 
ATOM   11549 N  ND2   . ASN F 1 610 ? 16.436  -38.74  78.681  1 64.18 ? 610 ASN Z ND2   1 
ATOM   11550 N  N     . LEU F 1 611 ? 21.413  -39.542 76.787  1 60.46 ? 611 LEU Z N     1 
ATOM   11551 C  CA    . LEU F 1 611 ? 22.659  -40.239 76.494  1 60.88 ? 611 LEU Z CA    1 
ATOM   11552 C  C     . LEU F 1 611 ? 23.853  -39.645 77.227  1 61.18 ? 611 LEU Z C     1 
ATOM   11553 O  O     . LEU F 1 611 ? 24.127  -38.454 77.119  1 61.25 ? 611 LEU Z O     1 
ATOM   11554 C  CB    . LEU F 1 611 ? 22.927  -40.286 74.984  1 61.11 ? 611 LEU Z CB    1 
ATOM   11555 C  CG    . LEU F 1 611 ? 21.896  -41.028 74.138  1 62.55 ? 611 LEU Z CG    1 
ATOM   11556 C  CD1   . LEU F 1 611 ? 22.15   -40.813 72.674  1 63.02 ? 611 LEU Z CD1   1 
ATOM   11557 C  CD2   . LEU F 1 611 ? 21.891  -42.501 74.441  1 63.28 ? 611 LEU Z CD2   1 
ATOM   11558 N  N     . THR F 1 612 ? 24.558  -40.487 77.977  1 61.23 ? 612 THR Z N     1 
ATOM   11559 C  CA    . THR F 1 612 ? 25.772  -40.118 78.7    1 61.76 ? 612 THR Z CA    1 
ATOM   11560 C  C     . THR F 1 612 ? 26.994  -40.331 77.769  1 62.14 ? 612 THR Z C     1 
ATOM   11561 O  O     . THR F 1 612 ? 26.839  -40.882 76.68   1 62.17 ? 612 THR Z O     1 
ATOM   11562 C  CB    . THR F 1 612 ? 25.869  -40.966 79.986  1 62.98 ? 612 THR Z CB    1 
ATOM   11563 O  OG1   . THR F 1 612 ? 26.126  -42.326 79.637  1 63.95 ? 612 THR Z OG1   1 
ATOM   11564 C  CG2   . THR F 1 612 ? 24.614  -40.878 80.838  1 63.36 ? 612 THR Z CG2   1 
ATOM   11565 N  N     . GLU F 1 613 ? 28.205  -39.933 78.197  1 62.28 ? 613 GLU Z N     1 
ATOM   11566 C  CA    . GLU F 1 613 ? 29.424  -40.13  77.407  1 62.88 ? 613 GLU Z CA    1 
ATOM   11567 C  C     . GLU F 1 613 ? 29.642  -41.625 77.086  1 63.16 ? 613 GLU Z C     1 
ATOM   11568 O  O     . GLU F 1 613 ? 30.018  -41.974 75.966  1 63.23 ? 613 GLU Z O     1 
ATOM   11569 C  CB    . GLU F 1 613 ? 30.63   -39.554 78.171  1 65.12 ? 613 GLU Z CB    1 
ATOM   11570 C  CG    . GLU F 1 613 ? 31.985  -39.835 77.545  1 69.48 ? 613 GLU Z CG    1 
ATOM   11571 C  CD    . GLU F 1 613 ? 33.16   -39.429 78.412  1 75.19 ? 613 GLU Z CD    1 
ATOM   11572 O  OE1   . GLU F 1 613 ? 34.257  -40.009 78.242  1 76.14 ? 613 GLU Z OE1   1 
ATOM   11573 O  OE2   . GLU F 1 613 ? 32.984  -38.526 79.261  1 77.34 ? 613 GLU Z OE2   1 
ATOM   11574 N  N     . ASN F 1 614 ? 29.362  -42.498 78.066  1 63.17 ? 614 ASN Z N     1 
ATOM   11575 C  CA    . ASN F 1 614 ? 29.501  -43.947 77.917  1 63.59 ? 614 ASN Z CA    1 
ATOM   11576 C  C     . ASN F 1 614 ? 28.457  -44.526 76.962  1 63.42 ? 614 ASN Z C     1 
ATOM   11577 O  O     . ASN F 1 614 ? 28.75   -45.483 76.248  1 63.34 ? 614 ASN Z O     1 
ATOM   11578 C  CB    . ASN F 1 614 ? 29.434  -44.641 79.279  1 65.1  ? 614 ASN Z CB    1 
ATOM   11579 C  CG    . ASN F 1 614 ? 30.686  -44.47  80.106  1 68.63 ? 614 ASN Z CG    1 
ATOM   11580 O  OD1   . ASN F 1 614 ? 31.789  -44.281 79.58   1 69.7  ? 614 ASN Z OD1   1 
ATOM   11581 N  ND2   . ASN F 1 614 ? 30.542  -44.539 81.423  1 69.59 ? 614 ASN Z ND2   1 
ATOM   11582 N  N     . ASP F 1 615 ? 27.244  -43.948 76.944  1 63.22 ? 615 ASP Z N     1 
ATOM   11583 C  CA    . ASP F 1 615 ? 26.181  -44.384 76.038  1 63.54 ? 615 ASP Z CA    1 
ATOM   11584 C  C     . ASP F 1 615 ? 26.6    -44.108 74.606  1 63.44 ? 615 ASP Z C     1 
ATOM   11585 O  O     . ASP F 1 615 ? 26.431  -44.971 73.749  1 63.59 ? 615 ASP Z O     1 
ATOM   11586 C  CB    . ASP F 1 615 ? 24.861  -43.661 76.333  1 65.51 ? 615 ASP Z CB    1 
ATOM   11587 C  CG    . ASP F 1 615 ? 24.072  -44.223 77.494  1 70.73 ? 615 ASP Z CG    1 
ATOM   11588 O  OD1   . ASP F 1 615 ? 24.375  -45.358 77.925  1 71.77 ? 615 ASP Z OD1   1 
ATOM   11589 O  OD2   . ASP F 1 615 ? 23.147  -43.531 77.971  1 73.09 ? 615 ASP Z OD2   1 
ATOM   11590 N  N     . TYR F 1 616 ? 27.193  -42.926 74.349  1 63.02 ? 616 TYR Z N     1 
ATOM   11591 C  CA    . TYR F 1 616 ? 27.688  -42.569 73.024  1 63.07 ? 616 TYR Z CA    1 
ATOM   11592 C  C     . TYR F 1 616 ? 28.787  -43.53  72.605  1 63.03 ? 616 TYR Z C     1 
ATOM   11593 O  O     . TYR F 1 616 ? 28.774  -44.007 71.477  1 63.05 ? 616 TYR Z O     1 
ATOM   11594 C  CB    . TYR F 1 616 ? 28.194  -41.12  72.994  1 63.07 ? 616 TYR Z CB    1 
ATOM   11595 C  CG    . TYR F 1 616 ? 27.079  -40.113 72.834  1 63.74 ? 616 TYR Z CG    1 
ATOM   11596 C  CD1   . TYR F 1 616 ? 26.338  -40.047 71.665  1 64.53 ? 616 TYR Z CD1   1 
ATOM   11597 C  CD2   . TYR F 1 616 ? 26.771  -39.22  73.851  1 64.57 ? 616 TYR Z CD2   1 
ATOM   11598 C  CE1   . TYR F 1 616 ? 25.303  -39.133 71.518  1 65.37 ? 616 TYR Z CE1   1 
ATOM   11599 C  CE2   . TYR F 1 616 ? 25.74   -38.301 73.716  1 65.38 ? 616 TYR Z CE2   1 
ATOM   11600 C  CZ    . TYR F 1 616 ? 25.007  -38.261 72.547  1 66.21 ? 616 TYR Z CZ    1 
ATOM   11601 O  OH    . TYR F 1 616 ? 23.987  -37.353 72.415  1 67.6  ? 616 TYR Z OH    1 
ATOM   11602 N  N     . GLU F 1 617 ? 29.69   -43.871 73.531  1 62.89 ? 617 GLU Z N     1 
ATOM   11603 C  CA    . GLU F 1 617 ? 30.761  -44.826 73.29   1 63.32 ? 617 GLU Z CA    1 
ATOM   11604 C  C     . GLU F 1 617 ? 30.205  -46.202 72.883  1 63.31 ? 617 GLU Z C     1 
ATOM   11605 O  O     . GLU F 1 617 ? 30.748  -46.839 71.983  1 63.34 ? 617 GLU Z O     1 
ATOM   11606 C  CB    . GLU F 1 617 ? 31.68   -44.934 74.528  1 65.9  ? 617 GLU Z CB    1 
ATOM   11607 C  CG    . GLU F 1 617 ? 32.94   -44.08  74.471  1 70.89 ? 617 GLU Z CG    1 
ATOM   11608 C  CD    . GLU F 1 617 ? 34.247  -44.85  74.472  1 77.07 ? 617 GLU Z CD    1 
ATOM   11609 O  OE1   . GLU F 1 617 ? 34.638  -45.363 75.547  1 78.38 ? 617 GLU Z OE1   1 
ATOM   11610 O  OE2   . GLU F 1 617 ? 34.893  -44.922 73.402  1 78.87 ? 617 GLU Z OE2   1 
ATOM   11611 N  N     . LYS F 1 618 ? 29.091  -46.63  73.5    1 63.12 ? 618 LYS Z N     1 
ATOM   11612 C  CA    . LYS F 1 618 ? 28.444  -47.901 73.171  1 63.31 ? 618 LYS Z CA    1 
ATOM   11613 C  C     . LYS F 1 618 ? 27.775  -47.856 71.793  1 63.27 ? 618 LYS Z C     1 
ATOM   11614 O  O     . LYS F 1 618 ? 27.851  -48.82  71.041  1 63.42 ? 618 LYS Z O     1 
ATOM   11615 C  CB    . LYS F 1 618 ? 27.451  -48.323 74.274  1 65.12 ? 618 LYS Z CB    1 
ATOM   11616 C  CG    . LYS F 1 618 ? 26.634  -49.584 73.982  1 68.95 ? 618 LYS Z CG    1 
ATOM   11617 C  CD    . LYS F 1 618 ? 27.45   -50.871 73.949  1 73.1  ? 618 LYS Z CD    1 
ATOM   11618 C  CE    . LYS F 1 618 ? 26.596  -52.058 73.579  1 76.59 ? 618 LYS Z CE    1 
ATOM   11619 N  NZ    . LYS F 1 618 ? 27.422  -53.249 73.246  1 78.64 ? 618 LYS Z NZ    1 
ATOM   11620 N  N     . ILE F 1 619 ? 27.188  -46.705 71.422  1 62.95 ? 619 ILE Z N     1 
ATOM   11621 C  CA    . ILE F 1 619 ? 26.575  -46.547 70.1    1 63    ? 619 ILE Z CA    1 
ATOM   11622 C  C     . ILE F 1 619 ? 27.657  -46.608 69.02   1 62.95 ? 619 ILE Z C     1 
ATOM   11623 O  O     . ILE F 1 619 ? 27.471  -47.284 68.013  1 63.03 ? 619 ILE Z O     1 
ATOM   11624 C  CB    . ILE F 1 619 ? 25.712  -45.262 69.998  1 63.46 ? 619 ILE Z CB    1 
ATOM   11625 C  CG1   . ILE F 1 619 ? 24.613  -45.239 71.077  1 64.35 ? 619 ILE Z CG1   1 
ATOM   11626 C  CG2   . ILE F 1 619 ? 25.102  -45.125 68.604  1 63.86 ? 619 ILE Z CG2   1 
ATOM   11627 C  CD1   . ILE F 1 619 ? 23.883  -43.923 71.201  1 65.43 ? 619 ILE Z CD1   1 
ATOM   11628 N  N     . PHE F 1 620 ? 28.812  -45.961 69.259  1 62.72 ? 620 PHE Z N     1 
ATOM   11629 C  CA    . PHE F 1 620 ? 29.942  -45.989 68.325  1 62.99 ? 620 PHE Z CA    1 
ATOM   11630 C  C     . PHE F 1 620 ? 30.456  -47.42  68.145  1 62.86 ? 620 PHE Z C     1 
ATOM   11631 O  O     . PHE F 1 620 ? 30.841  -47.794 67.044  1 62.91 ? 620 PHE Z O     1 
ATOM   11632 C  CB    . PHE F 1 620 ? 31.098  -45.101 68.823  1 63.04 ? 620 PHE Z CB    1 
ATOM   11633 C  CG    . PHE F 1 620 ? 30.913  -43.61  68.658  1 63.83 ? 620 PHE Z CG    1 
ATOM   11634 C  CD1   . PHE F 1 620 ? 30.55   -43.074 67.44   1 64.69 ? 620 PHE Z CD1   1 
ATOM   11635 C  CD2   . PHE F 1 620 ? 31.177  -42.742 69.701  1 64.57 ? 620 PHE Z CD2   1 
ATOM   11636 C  CE1   . PHE F 1 620 ? 30.415  -41.701 67.28   1 65.34 ? 620 PHE Z CE1   1 
ATOM   11637 C  CE2   . PHE F 1 620 ? 31.017  -41.371 69.544  1 65.26 ? 620 PHE Z CE2   1 
ATOM   11638 C  CZ    . PHE F 1 620 ? 30.639  -40.861 68.335  1 65.12 ? 620 PHE Z CZ    1 
ATOM   11639 N  N     . GLU F 1 621 ? 30.474  -48.21  69.225  1 62.55 ? 621 GLU Z N     1 
ATOM   11640 C  CA    . GLU F 1 621 ? 30.937  -49.591 69.186  1 62.75 ? 621 GLU Z CA    1 
ATOM   11641 C  C     . GLU F 1 621 ? 29.961  -50.457 68.389  1 62.47 ? 621 GLU Z C     1 
ATOM   11642 O  O     . GLU F 1 621 ? 30.392  -51.258 67.558  1 62.89 ? 621 GLU Z O     1 
ATOM   11643 C  CB    . GLU F 1 621 ? 31.106  -50.133 70.612  1 65.32 ? 621 GLU Z CB    1 
ATOM   11644 C  CG    . GLU F 1 621 ? 32.081  -51.294 70.726  1 70.81 ? 621 GLU Z CG    1 
ATOM   11645 C  CD    . GLU F 1 621 ? 32.303  -51.818 72.135  1 77.87 ? 621 GLU Z CD    1 
ATOM   11646 O  OE1   . GLU F 1 621 ? 31.756  -51.222 73.092  1 78.78 ? 621 GLU Z OE1   1 
ATOM   11647 O  OE2   . GLU F 1 621 ? 33.024  -52.832 72.281  1 80.47 ? 621 GLU Z OE2   1 
ATOM   11648 N  N     . VAL F 1 622 ? 28.653  -50.272 68.612  1 61.6  ? 622 VAL Z N     1 
ATOM   11649 C  CA    . VAL F 1 622 ? 27.623  -51.035 67.913  1 61.43 ? 622 VAL Z CA    1 
ATOM   11650 C  C     . VAL F 1 622 ? 27.563  -50.71  66.404  1 61.25 ? 622 VAL Z C     1 
ATOM   11651 O  O     . VAL F 1 622 ? 27.618  -51.615 65.567  1 61.26 ? 622 VAL Z O     1 
ATOM   11652 C  CB    . VAL F 1 622 ? 26.246  -50.84  68.603  1 62.08 ? 622 VAL Z CB    1 
ATOM   11653 C  CG1   . VAL F 1 622 ? 25.102  -51.361 67.737  1 62.64 ? 622 VAL Z CG1   1 
ATOM   11654 C  CG2   . VAL F 1 622 ? 26.217  -51.498 69.964  1 62.62 ? 622 VAL Z CG2   1 
ATOM   11655 N  N     . THR F 1 623 ? 27.463  -49.421 66.065  1 60.83 ? 623 THR Z N     1 
ATOM   11656 C  CA    . THR F 1 623 ? 27.292  -48.963 64.689  1 60.77 ? 623 THR Z CA    1 
ATOM   11657 C  C     . THR F 1 623 ? 28.555  -48.802 63.852  1 60.56 ? 623 THR Z C     1 
ATOM   11658 O  O     . THR F 1 623 ? 28.524  -49.042 62.649  1 60.74 ? 623 THR Z O     1 
ATOM   11659 C  CB    . THR F 1 623 ? 26.537  -47.636 64.697  1 61.82 ? 623 THR Z CB    1 
ATOM   11660 O  OG1   . THR F 1 623 ? 27.359  -46.633 65.297  1 62.69 ? 623 THR Z OG1   1 
ATOM   11661 C  CG2   . THR F 1 623 ? 25.212  -47.726 65.425  1 62.17 ? 623 THR Z CG2   1 
ATOM   11662 N  N     . GLY F 1 624 ? 29.622  -48.315 64.462  1 60.03 ? 624 GLY Z N     1 
ATOM   11663 C  CA    . GLY F 1 624 ? 30.85   -48.014 63.735  1 60.02 ? 624 GLY Z CA    1 
ATOM   11664 C  C     . GLY F 1 624 ? 30.811  -46.654 63.055  1 59.72 ? 624 GLY Z C     1 
ATOM   11665 O  O     . GLY F 1 624 ? 31.644  -46.367 62.193  1 60.08 ? 624 GLY Z O     1 
ATOM   11666 N  N     . CYS F 1 625 ? 29.838  -45.806 63.431  1 58.92 ? 625 CYS Z N     1 
ATOM   11667 C  CA    . CYS F 1 625 ? 29.66   -44.476 62.874  1 58.7  ? 625 CYS Z CA    1 
ATOM   11668 C  C     . CYS F 1 625 ? 30.805  -43.557 63.254  1 58.28 ? 625 CYS Z C     1 
ATOM   11669 O  O     . CYS F 1 625 ? 31.334  -43.657 64.352  1 58.44 ? 625 CYS Z O     1 
ATOM   11670 C  CB    . CYS F 1 625 ? 28.321  -43.886 63.31   1 59.27 ? 625 CYS Z CB    1 
ATOM   11671 S  SG    . CYS F 1 625 ? 26.88   -44.637 62.513  1 62.18 ? 625 CYS Z SG    1 
ATOM   11672 N  N     . ASP F 1 626 ? 31.182  -42.654 62.355  1 57.57 ? 626 ASP Z N     1 
ATOM   11673 C  CA    . ASP F 1 626 ? 32.217  -41.661 62.644  1 57.32 ? 626 ASP Z CA    1 
ATOM   11674 C  C     . ASP F 1 626 ? 31.633  -40.432 63.378  1 56.36 ? 626 ASP Z C     1 
ATOM   11675 O  O     . ASP F 1 626 ? 32.37   -39.707 64.033  1 56.34 ? 626 ASP Z O     1 
ATOM   11676 C  CB    . ASP F 1 626 ? 32.909  -41.21  61.352  1 59.35 ? 626 ASP Z CB    1 
ATOM   11677 C  CG    . ASP F 1 626 ? 33.641  -42.324 60.638  1 64.43 ? 626 ASP Z CG    1 
ATOM   11678 O  OD1   . ASP F 1 626 ? 34.739  -42.704 61.102  1 65.22 ? 626 ASP Z OD1   1 
ATOM   11679 O  OD2   . ASP F 1 626 ? 33.123  -42.81  59.606  1 66.86 ? 626 ASP Z OD2   1 
ATOM   11680 N  N     . LEU F 1 627 ? 30.322  -40.191 63.26   1 55.37 ? 627 LEU Z N     1 
ATOM   11681 C  CA    . LEU F 1 627 ? 29.676  -39.046 63.882  1 54.85 ? 627 LEU Z CA    1 
ATOM   11682 C  C     . LEU F 1 627 ? 28.265  -39.409 64.336  1 54.02 ? 627 LEU Z C     1 
ATOM   11683 O  O     . LEU F 1 627 ? 27.584  -40.174 63.666  1 54.04 ? 627 LEU Z O     1 
ATOM   11684 C  CB    . LEU F 1 627 ? 29.605  -37.908 62.844  1 55.13 ? 627 LEU Z CB    1 
ATOM   11685 C  CG    . LEU F 1 627 ? 28.901  -36.62  63.275  1 56.73 ? 627 LEU Z CG    1 
ATOM   11686 C  CD1   . LEU F 1 627 ? 29.665  -35.928 64.367  1 57.32 ? 627 LEU Z CD1   1 
ATOM   11687 C  CD2   . LEU F 1 627 ? 28.714  -35.675 62.112  1 57.43 ? 627 LEU Z CD2   1 
ATOM   11688 N  N     . LEU F 1 628 ? 27.823  -38.866 65.467  1 53.22 ? 628 LEU Z N     1 
ATOM   11689 C  CA    . LEU F 1 628 ? 26.459  -39.069 65.929  1 53.07 ? 628 LEU Z CA    1 
ATOM   11690 C  C     . LEU F 1 628 ? 25.81   -37.702 66.07   1 52.9  ? 628 LEU Z C     1 
ATOM   11691 O  O     . LEU F 1 628 ? 26.398  -36.802 66.659  1 53.01 ? 628 LEU Z O     1 
ATOM   11692 C  CB    . LEU F 1 628 ? 26.415  -39.843 67.249  1 53.21 ? 628 LEU Z CB    1 
ATOM   11693 C  CG    . LEU F 1 628 ? 26.88   -41.289 67.165  1 54.53 ? 628 LEU Z CG    1 
ATOM   11694 C  CD1   . LEU F 1 628 ? 26.968  -41.907 68.53   1 55.02 ? 628 LEU Z CD1   1 
ATOM   11695 C  CD2   . LEU F 1 628 ? 25.985  -42.113 66.268  1 55.16 ? 628 LEU Z CD2   1 
ATOM   11696 N  N     . ILE F 1 629 ? 24.639  -37.518 65.465  1 52.53 ? 629 ILE Z N     1 
ATOM   11697 C  CA    . ILE F 1 629 ? 23.934  -36.248 65.527  1 52.78 ? 629 ILE Z CA    1 
ATOM   11698 C  C     . ILE F 1 629 ? 22.659  -36.422 66.333  1 52.89 ? 629 ILE Z C     1 
ATOM   11699 O  O     . ILE F 1 629 ? 21.687  -36.996 65.842  1 52.83 ? 629 ILE Z O     1 
ATOM   11700 C  CB    . ILE F 1 629 ? 23.663  -35.672 64.118  1 53.22 ? 629 ILE Z CB    1 
ATOM   11701 C  CG1   . ILE F 1 629 ? 24.956  -35.632 63.283  1 53.98 ? 629 ILE Z CG1   1 
ATOM   11702 C  CG2   . ILE F 1 629 ? 23.02   -34.288 64.224  1 53.75 ? 629 ILE Z CG2   1 
ATOM   11703 C  CD1   . ILE F 1 629 ? 24.765  -35.216 61.856  1 55.24 ? 629 ILE Z CD1   1 
ATOM   11704 N  N     . ALA F 1 630 ? 22.684  -35.971 67.593  1 52.84 ? 630 ALA Z N     1 
ATOM   11705 C  CA    . ALA F 1 630 ? 21.537  -36.075 68.481  1 53.25 ? 630 ALA Z CA    1 
ATOM   11706 C  C     . ALA F 1 630 ? 20.739  -34.784 68.426  1 53.5  ? 630 ALA Z C     1 
ATOM   11707 O  O     . ALA F 1 630 ? 21.237  -33.714 68.771  1 53.58 ? 630 ALA Z O     1 
ATOM   11708 C  CB    . ALA F 1 630 ? 21.996  -36.351 69.897  1 53.49 ? 630 ALA Z CB    1 
ATOM   11709 N  N     . ILE F 1 631 ? 19.498  -34.892 67.984  1 53.46 ? 631 ILE Z N     1 
ATOM   11710 C  CA    . ILE F 1 631 ? 18.596  -33.77  67.794  1 53.93 ? 631 ILE Z CA    1 
ATOM   11711 C  C     . ILE F 1 631 ? 17.479  -33.788 68.839  1 54.35 ? 631 ILE Z C     1 
ATOM   11712 O  O     . ILE F 1 631 ? 16.998  -34.86  69.187  1 54.62 ? 631 ILE Z O     1 
ATOM   11713 C  CB    . ILE F 1 631 ? 18.057  -33.928 66.353  1 54.38 ? 631 ILE Z CB    1 
ATOM   11714 C  CG1   . ILE F 1 631 ? 19.168  -33.68  65.327  1 55.34 ? 631 ILE Z CG1   1 
ATOM   11715 C  CG2   . ILE F 1 631 ? 16.849  -33.072 66.084  1 54.79 ? 631 ILE Z CG2   1 
ATOM   11716 C  CD1   . ILE F 1 631 ? 18.9    -34.303 64.016  1 56.68 ? 631 ILE Z CD1   1 
ATOM   11717 N  N     . LYS F 1 632 ? 17.092  -32.624 69.369  1 54.21 ? 632 LYS Z N     1 
ATOM   11718 C  CA    . LYS F 1 632 ? 16.008  -32.563 70.347  1 54.7  ? 632 LYS Z CA    1 
ATOM   11719 C  C     . LYS F 1 632 ? 15.223  -31.292 70.173  1 55    ? 632 LYS Z C     1 
ATOM   11720 O  O     . LYS F 1 632 ? 15.811  -30.239 69.934  1 55.1  ? 632 LYS Z O     1 
ATOM   11721 C  CB    . LYS F 1 632 ? 16.531  -32.694 71.785  1 56.58 ? 632 LYS Z CB    1 
ATOM   11722 C  CG    . LYS F 1 632 ? 17.492  -31.589 72.201  1 60.69 ? 632 LYS Z CG    1 
ATOM   11723 C  CD    . LYS F 1 632 ? 18.33   -31.962 73.401  1 64.87 ? 632 LYS Z CD    1 
ATOM   11724 C  CE    . LYS F 1 632 ? 19.425  -32.936 73.037  1 68.51 ? 632 LYS Z CE    1 
ATOM   11725 N  NZ    . LYS F 1 632 ? 20.21   -32.485 71.858  1 70.71 ? 632 LYS Z NZ    1 
ATOM   11726 N  N     . ASN F 1 633 ? 13.895  -31.385 70.259  1 54.97 ? 633 ASN Z N     1 
ATOM   11727 C  CA    . ASN F 1 633 ? 13.068  -30.199 70.116  1 55.44 ? 633 ASN Z CA    1 
ATOM   11728 C  C     . ASN F 1 633 ? 12.827  -29.555 71.456  1 55.97 ? 633 ASN Z C     1 
ATOM   11729 O  O     . ASN F 1 633 ? 12.632  -30.235 72.464  1 56.18 ? 633 ASN Z O     1 
ATOM   11730 C  CB    . ASN F 1 633 ? 11.743  -30.508 69.438  1 56.16 ? 633 ASN Z CB    1 
ATOM   11731 C  CG    . ASN F 1 633 ? 10.958  -31.585 70.127  1 58.27 ? 633 ASN Z CG    1 
ATOM   11732 O  OD1   . ASN F 1 633 ? 11.31   -32.758 70.063  1 59    ? 633 ASN Z OD1   1 
ATOM   11733 N  ND2   . ASN F 1 633 ? 9.88    -31.209 70.798  1 58.67 ? 633 ASN Z ND2   1 
ATOM   11734 N  N     . GLN F 1 634 ? 12.86   -28.233 71.456  1 56.01 ? 634 GLN Z N     1 
ATOM   11735 C  CA    . GLN F 1 634 ? 12.573  -27.371 72.588  1 56.44 ? 634 GLN Z CA    1 
ATOM   11736 C  C     . GLN F 1 634 ? 11.253  -26.721 72.205  1 56.88 ? 634 GLN Z C     1 
ATOM   11737 O  O     . GLN F 1 634 ? 11.157  -26.144 71.123  1 57.07 ? 634 GLN Z O     1 
ATOM   11738 C  CB    . GLN F 1 634 ? 13.671  -26.31  72.714  1 57.86 ? 634 GLN Z CB    1 
ATOM   11739 C  CG    . GLN F 1 634 ? 13.436  -25.289 73.806  1 61.05 ? 634 GLN Z CG    1 
ATOM   11740 C  CD    . GLN F 1 634 ? 14.604  -24.348 73.868  1 65.33 ? 634 GLN Z CD    1 
ATOM   11741 O  OE1   . GLN F 1 634 ? 15.673  -24.682 74.388  1 66.72 ? 634 GLN Z OE1   1 
ATOM   11742 N  NE2   . GLN F 1 634 ? 14.435  -23.158 73.318  1 66.14 ? 634 GLN Z NE2   1 
ATOM   11743 N  N     . ASN F 1 635 ? 10.22   -26.87  73.033  1 57.03 ? 635 ASN Z N     1 
ATOM   11744 C  CA    . ASN F 1 635 ? 8.903   -26.331 72.704  1 57.74 ? 635 ASN Z CA    1 
ATOM   11745 C  C     . ASN F 1 635 ? 8.711   -24.869 73.099  1 58.36 ? 635 ASN Z C     1 
ATOM   11746 O  O     . ASN F 1 635 ? 7.923   -24.167 72.462  1 58.48 ? 635 ASN Z O     1 
ATOM   11747 C  CB    . ASN F 1 635 ? 7.804   -27.201 73.307  1 58.76 ? 635 ASN Z CB    1 
ATOM   11748 C  CG    . ASN F 1 635 ? 7.798   -28.603 72.766  1 61.54 ? 635 ASN Z CG    1 
ATOM   11749 O  OD1   . ASN F 1 635 ? 8.105   -28.842 71.593  1 62.82 ? 635 ASN Z OD1   1 
ATOM   11750 N  ND2   . ASN F 1 635 ? 7.442   -29.56  73.608  1 61.83 ? 635 ASN Z ND2   1 
ATOM   11751 N  N     . ASN F 1 636 ? 9.401   -24.408 74.154  1 58.52 ? 636 ASN Z N     1 
ATOM   11752 C  CA    . ASN F 1 636 ? 9.216   -23.036 74.627  1 59.02 ? 636 ASN Z CA    1 
ATOM   11753 C  C     . ASN F 1 636 ? 10.527  -22.272 74.845  1 59.31 ? 636 ASN Z C     1 
ATOM   11754 O  O     . ASN F 1 636 ? 11.117  -22.406 75.916  1 59.43 ? 636 ASN Z O     1 
ATOM   11755 C  CB    . ASN F 1 636 ? 8.416   -23.043 75.944  1 60.1  ? 636 ASN Z CB    1 
ATOM   11756 C  CG    . ASN F 1 636 ? 7.226   -23.978 75.979  1 62.87 ? 636 ASN Z CG    1 
ATOM   11757 O  OD1   . ASN F 1 636 ? 6.132   -23.643 75.52   1 64.05 ? 636 ASN Z OD1   1 
ATOM   11758 N  ND2   . ASN F 1 636 ? 7.416   -25.174 76.522  1 63.2  ? 636 ASN Z ND2   1 
ATOM   11759 N  N     . PRO F 1 637 ? 10.963  -21.392 73.921  1 59.41 ? 637 PRO Z N     1 
ATOM   11760 C  CA    . PRO F 1 637 ? 10.401  -21.13  72.584  1 59.72 ? 637 PRO Z CA    1 
ATOM   11761 C  C     . PRO F 1 637 ? 10.843  -22.19  71.562  1 60.18 ? 637 PRO Z C     1 
ATOM   11762 O  O     . PRO F 1 637 ? 11.872  -22.838 71.765  1 60.46 ? 637 PRO Z O     1 
ATOM   11763 C  CB    . PRO F 1 637 ? 10.972  -19.747 72.252  1 60.34 ? 637 PRO Z CB    1 
ATOM   11764 C  CG    . PRO F 1 637 ? 12.332  -19.748 72.903  1 60.66 ? 637 PRO Z CG    1 
ATOM   11765 C  CD    . PRO F 1 637 ? 12.201  -20.612 74.148  1 59.01 ? 637 PRO Z CD    1 
ATOM   11766 N  N     . GLN F 1 638 ? 10.068  -22.39  70.489  1 60.07 ? 638 GLN Z N     1 
ATOM   11767 C  CA    . GLN F 1 638 ? 10.389  -23.424 69.504  1 60.45 ? 638 GLN Z CA    1 
ATOM   11768 C  C     . GLN F 1 638 ? 11.803  -23.303 68.916  1 59.79 ? 638 GLN Z C     1 
ATOM   11769 O  O     . GLN F 1 638 ? 12.141  -22.287 68.313  1 59.89 ? 638 GLN Z O     1 
ATOM   11770 C  CB    . GLN F 1 638 ? 9.325   -23.5   68.405  1 62.79 ? 638 GLN Z CB    1 
ATOM   11771 C  CG    . GLN F 1 638 ? 8.104   -24.298 68.845  1 67.14 ? 638 GLN Z CG    1 
ATOM   11772 C  CD    . GLN F 1 638 ? 7.038   -24.329 67.786  1 72.55 ? 638 GLN Z CD    1 
ATOM   11773 O  OE1   . GLN F 1 638 ? 6.454   -23.295 67.435  1 74.53 ? 638 GLN Z OE1   1 
ATOM   11774 N  NE2   . GLN F 1 638 ? 6.76    -25.516 67.255  1 73.14 ? 638 GLN Z NE2   1 
ATOM   11775 N  N     . LYS F 1 639 ? 12.63   -24.348 69.131  1 58.9  ? 639 LYS Z N     1 
ATOM   11776 C  CA    . LYS F 1 639 ? 14.015  -24.427 68.664  1 58.53 ? 639 LYS Z CA    1 
ATOM   11777 C  C     . LYS F 1 639 ? 14.465  -25.879 68.523  1 58.12 ? 639 LYS Z C     1 
ATOM   11778 O  O     . LYS F 1 639 ? 14.05   -26.735 69.302  1 58.28 ? 639 LYS Z O     1 
ATOM   11779 C  CB    . LYS F 1 639 ? 14.957  -23.743 69.665  1 60.07 ? 639 LYS Z CB    1 
ATOM   11780 C  CG    . LYS F 1 639 ? 15.277  -22.295 69.356  1 63.85 ? 639 LYS Z CG    1 
ATOM   11781 C  CD    . LYS F 1 639 ? 16.098  -21.681 70.476  1 68.02 ? 639 LYS Z CD    1 
ATOM   11782 C  CE    . LYS F 1 639 ? 17.459  -21.234 70.006  1 71.38 ? 639 LYS Z CE    1 
ATOM   11783 N  NZ    . LYS F 1 639 ? 17.426  -19.856 69.451  1 73.38 ? 639 LYS Z NZ    1 
ATOM   11784 N  N     . TRP F 1 640 ? 15.35   -26.151 67.557  1 57.34 ? 640 TRP Z N     1 
ATOM   11785 C  CA    . TRP F 1 640 ? 15.921  -27.482 67.398  1 56.97 ? 640 TRP Z CA    1 
ATOM   11786 C  C     . TRP F 1 640 ? 17.318  -27.435 67.998  1 56.61 ? 640 TRP Z C     1 
ATOM   11787 O  O     . TRP F 1 640 ? 18.162  -26.674 67.533  1 56.59 ? 640 TRP Z O     1 
ATOM   11788 C  CB    . TRP F 1 640 ? 16.006  -27.891 65.921  1 56.7  ? 640 TRP Z CB    1 
ATOM   11789 C  CG    . TRP F 1 640 ? 14.735  -28.43  65.337  1 56.93 ? 640 TRP Z CG    1 
ATOM   11790 C  CD1   . TRP F 1 640 ? 13.989  -27.865 64.348  1 57.76 ? 640 TRP Z CD1   1 
ATOM   11791 C  CD2   . TRP F 1 640 ? 14.098  -29.678 65.657  1 56.94 ? 640 TRP Z CD2   1 
ATOM   11792 N  NE1   . TRP F 1 640 ? 12.92   -28.673 64.04   1 58.03 ? 640 TRP Z NE1   1 
ATOM   11793 C  CE2   . TRP F 1 640 ? 12.96   -29.79  64.835  1 57.71 ? 640 TRP Z CE2   1 
ATOM   11794 C  CE3   . TRP F 1 640 ? 14.355  -30.692 66.586  1 57.35 ? 640 TRP Z CE3   1 
ATOM   11795 C  CZ2   . TRP F 1 640 ? 12.096  -30.884 64.901  1 58.2  ? 640 TRP Z CZ2   1 
ATOM   11796 C  CZ3   . TRP F 1 640 ? 13.511  -31.785 66.63   1 58.05 ? 640 TRP Z CZ3   1 
ATOM   11797 C  CH2   . TRP F 1 640 ? 12.387  -31.864 65.809  1 58.16 ? 640 TRP Z CH2   1 
ATOM   11798 N  N     . VAL F 1 641 ? 17.551  -28.202 69.052  1 56.26 ? 641 VAL Z N     1 
ATOM   11799 C  CA    . VAL F 1 641 ? 18.848  -28.249 69.708  1 56.48 ? 641 VAL Z CA    1 
ATOM   11800 C  C     . VAL F 1 641 ? 19.644  -29.403 69.107  1 56.81 ? 641 VAL Z C     1 
ATOM   11801 O  O     . VAL F 1 641 ? 19.195  -30.549 69.132  1 56.85 ? 641 VAL Z O     1 
ATOM   11802 C  CB    . VAL F 1 641 ? 18.698  -28.378 71.237  1 57.04 ? 641 VAL Z CB    1 
ATOM   11803 C  CG1   . VAL F 1 641 ? 20.057  -28.331 71.92   1 57.56 ? 641 VAL Z CG1   1 
ATOM   11804 C  CG2   . VAL F 1 641 ? 17.779  -27.292 71.786  1 57.5  ? 641 VAL Z CG2   1 
ATOM   11805 N  N     . ILE F 1 642 ? 20.81   -29.095 68.533  1 56.83 ? 642 ILE Z N     1 
ATOM   11806 C  CA    . ILE F 1 642 ? 21.636  -30.101 67.867  1 57.2  ? 642 ILE Z CA    1 
ATOM   11807 C  C     . ILE F 1 642 ? 22.916  -30.381 68.654  1 57.53 ? 642 ILE Z C     1 
ATOM   11808 O  O     . ILE F 1 642 ? 23.645  -29.453 68.996  1 57.74 ? 642 ILE Z O     1 
ATOM   11809 C  CB    . ILE F 1 642 ? 21.975  -29.678 66.406  1 57.58 ? 642 ILE Z CB    1 
ATOM   11810 C  CG1   . ILE F 1 642 ? 20.779  -29.027 65.663  1 58.46 ? 642 ILE Z CG1   1 
ATOM   11811 C  CG2   . ILE F 1 642 ? 22.552  -30.848 65.618  1 58.06 ? 642 ILE Z CG2   1 
ATOM   11812 C  CD1   . ILE F 1 642 ? 19.605  -29.94  65.399  1 59.76 ? 642 ILE Z CD1   1 
ATOM   11813 N  N     . LYS F 1 643 ? 23.207  -31.653 68.915  1 57.46 ? 643 LYS Z N     1 
ATOM   11814 C  CA    . LYS F 1 643 ? 24.425  -32.038 69.609  1 58.1  ? 643 LYS Z CA    1 
ATOM   11815 C  C     . LYS F 1 643 ? 25.239  -32.961 68.69   1 58.61 ? 643 LYS Z C     1 
ATOM   11816 O  O     . LYS F 1 643 ? 24.773  -34.041 68.333  1 58.82 ? 643 LYS Z O     1 
ATOM   11817 C  CB    . LYS F 1 643 ? 24.089  -32.731 70.935  1 60.11 ? 643 LYS Z CB    1 
ATOM   11818 C  CG    . LYS F 1 643 ? 25.305  -32.978 71.819  1 64.54 ? 643 LYS Z CG    1 
ATOM   11819 C  CD    . LYS F 1 643 ? 24.929  -33.688 73.12   1 69.27 ? 643 LYS Z CD    1 
ATOM   11820 C  CE    . LYS F 1 643 ? 26.077  -33.757 74.103  1 73.12 ? 643 LYS Z CE    1 
ATOM   11821 N  NZ    . LYS F 1 643 ? 25.65   -34.303 75.424  1 75.18 ? 643 LYS Z NZ    1 
ATOM   11822 N  N     . PHE F 1 644 ? 26.43   -32.517 68.268  1 58.61 ? 644 PHE Z N     1 
ATOM   11823 C  CA    . PHE F 1 644 ? 27.286  -33.304 67.383  1 59    ? 644 PHE Z CA    1 
ATOM   11824 C  C     . PHE F 1 644 ? 28.337  -34.036 68.191  1 59.07 ? 644 PHE Z C     1 
ATOM   11825 O  O     . PHE F 1 644 ? 29.114  -33.402 68.902  1 59.22 ? 644 PHE Z O     1 
ATOM   11826 C  CB    . PHE F 1 644 ? 27.994  -32.403 66.364  1 59.13 ? 644 PHE Z CB    1 
ATOM   11827 C  CG    . PHE F 1 644 ? 27.1    -31.728 65.356  1 60.03 ? 644 PHE Z CG    1 
ATOM   11828 C  CD1   . PHE F 1 644 ? 26.742  -32.369 64.184  1 60.93 ? 644 PHE Z CD1   1 
ATOM   11829 C  CD2   . PHE F 1 644 ? 26.659  -30.431 65.557  1 60.92 ? 644 PHE Z CD2   1 
ATOM   11830 C  CE1   . PHE F 1 644 ? 25.94   -31.736 63.244  1 61.69 ? 644 PHE Z CE1   1 
ATOM   11831 C  CE2   . PHE F 1 644 ? 25.859  -29.8   64.615  1 61.69 ? 644 PHE Z CE2   1 
ATOM   11832 C  CZ    . PHE F 1 644 ? 25.501  -30.457 63.467  1 61.51 ? 644 PHE Z CZ    1 
ATOM   11833 N  N     . LYS F 1 645 ? 28.387  -35.356 68.064  1 58.88 ? 645 LYS Z N     1 
ATOM   11834 C  CA    . LYS F 1 645 ? 29.367  -36.154 68.783  1 59.33 ? 645 LYS Z CA    1 
ATOM   11835 C  C     . LYS F 1 645 ? 30.302  -36.876 67.818  1 59.58 ? 645 LYS Z C     1 
ATOM   11836 O  O     . LYS F 1 645 ? 29.926  -37.886 67.229  1 59.73 ? 645 LYS Z O     1 
ATOM   11837 C  CB    . LYS F 1 645 ? 28.674  -37.161 69.704  1 61.03 ? 645 LYS Z CB    1 
ATOM   11838 C  CG    . LYS F 1 645 ? 29.622  -37.821 70.698  1 64.87 ? 645 LYS Z CG    1 
ATOM   11839 C  CD    . LYS F 1 645 ? 29.837  -36.963 71.937  1 69.12 ? 645 LYS Z CD    1 
ATOM   11840 C  CE    . LYS F 1 645 ? 30.682  -37.675 72.962  1 72.89 ? 645 LYS Z CE    1 
ATOM   11841 N  NZ    . LYS F 1 645 ? 30.672  -36.968 74.268  1 75.19 ? 645 LYS Z NZ    1 
ATOM   11842 N  N     . PRO F 1 646 ? 31.534  -36.377 67.653  1 59.46 ? 646 PRO Z N     1 
ATOM   11843 C  CA    . PRO F 1 646 ? 32.478  -37.05  66.748  1 59.56 ? 646 PRO Z CA    1 
ATOM   11844 C  C     . PRO F 1 646 ? 33.204  -38.245 67.383  1 59.85 ? 646 PRO Z C     1 
ATOM   11845 O  O     . PRO F 1 646 ? 33.507  -38.219 68.574  1 60    ? 646 PRO Z O     1 
ATOM   11846 C  CB    . PRO F 1 646 ? 33.459  -35.935 66.393  1 60.17 ? 646 PRO Z CB    1 
ATOM   11847 C  CG    . PRO F 1 646 ? 33.452  -35.026 67.581  1 60.51 ? 646 PRO Z CG    1 
ATOM   11848 C  CD    . PRO F 1 646 ? 32.116  -35.163 68.261  1 58.94 ? 646 PRO Z CD    1 
ATOM   11849 N  N     . LYS F 1 647 ? 33.497  -39.286 66.595  1 59.72 ? 647 LYS Z N     1 
ATOM   11850 C  CA    . LYS F 1 647 ? 34.222  -40.454 67.1    1 60.1  ? 647 LYS Z CA    1 
ATOM   11851 C  C     . LYS F 1 647 ? 35.729  -40.231 66.998  1 60.26 ? 647 LYS Z C     1 
ATOM   11852 O  O     . LYS F 1 647 ? 36.479  -40.628 67.886  1 60.37 ? 647 LYS Z O     1 
ATOM   11853 C  CB    . LYS F 1 647 ? 33.841  -41.723 66.315  1 61.96 ? 647 LYS Z CB    1 
ATOM   11854 C  CG    . LYS F 1 647 ? 34.505  -42.998 66.842  1 66.04 ? 647 LYS Z CG    1 
ATOM   11855 C  CD    . LYS F 1 647 ? 34.22   -44.232 65.979  1 70.36 ? 647 LYS Z CD    1 
ATOM   11856 C  CE    . LYS F 1 647 ? 34.757  -44.096 64.576  1 74.08 ? 647 LYS Z CE    1 
ATOM   11857 N  NZ    . LYS F 1 647 ? 34.664  -45.379 63.83   1 76.37 ? 647 LYS Z NZ    1 
ATOM   11858 N  N     . ASN F 1 648 ? 36.173  -39.595 65.912  1 60.15 ? 648 ASN Z N     1 
ATOM   11859 C  CA    . ASN F 1 648 ? 37.591  -39.373 65.651  1 60.5  ? 648 ASN Z CA    1 
ATOM   11860 C  C     . ASN F 1 648 ? 37.93   -37.906 65.307  1 60.58 ? 648 ASN Z C     1 
ATOM   11861 O  O     . ASN F 1 648 ? 37.029  -37.079 65.181  1 60.65 ? 648 ASN Z O     1 
ATOM   11862 C  CB    . ASN F 1 648 ? 38.054  -40.336 64.548  1 61.51 ? 648 ASN Z CB    1 
ATOM   11863 C  CG    . ASN F 1 648 ? 37.149  -40.338 63.343  1 64.22 ? 648 ASN Z CG    1 
ATOM   11864 O  OD1   . ASN F 1 648 ? 36.762  -39.286 62.827  1 65.1  ? 648 ASN Z OD1   1 
ATOM   11865 N  ND2   . ASN F 1 648 ? 36.776  -41.524 62.884  1 64.8  ? 648 ASN Z ND2   1 
ATOM   11866 N  N     . THR F 1 649 ? 39.23   -37.595 65.146  1 60.46 ? 649 THR Z N     1 
ATOM   11867 C  CA    . THR F 1 649 ? 39.733  -36.26  64.828  1 60.86 ? 649 THR Z CA    1 
ATOM   11868 C  C     . THR F 1 649 ? 39.281  -35.727 63.454  1 60.9  ? 649 THR Z C     1 
ATOM   11869 O  O     . THR F 1 649 ? 39.148  -34.513 63.297  1 60.93 ? 649 THR Z O     1 
ATOM   11870 C  CB    . THR F 1 649 ? 41.252  -36.233 64.974  1 62.31 ? 649 THR Z CB    1 
ATOM   11871 O  OG1   . THR F 1 649 ? 41.813  -37.199 64.083  1 63.54 ? 649 THR Z OG1   1 
ATOM   11872 C  CG2   . THR F 1 649 ? 41.7    -36.526 66.399  1 62.6  ? 649 THR Z CG2   1 
ATOM   11873 N  N     . ILE F 1 650 ? 39.03   -36.611 62.472  1 60.7  ? 650 ILE Z N     1 
ATOM   11874 C  CA    . ILE F 1 650 ? 38.547  -36.174 61.16   1 61    ? 650 ILE Z CA    1 
ATOM   11875 C  C     . ILE F 1 650 ? 37.116  -35.651 61.317  1 61.19 ? 650 ILE Z C     1 
ATOM   11876 O  O     . ILE F 1 650 ? 36.799  -34.56  60.841  1 61.36 ? 650 ILE Z O     1 
ATOM   11877 C  CB    . ILE F 1 650 ? 38.643  -37.315 60.113  1 61.54 ? 650 ILE Z CB    1 
ATOM   11878 C  CG1   . ILE F 1 650 ? 40.11   -37.624 59.759  1 62.58 ? 650 ILE Z CG1   1 
ATOM   11879 C  CG2   . ILE F 1 650 ? 37.821  -37.011 58.86   1 61.96 ? 650 ILE Z CG2   1 
ATOM   11880 C  CD1   . ILE F 1 650 ? 40.863  -36.488 59.09   1 63.85 ? 650 ILE Z CD1   1 
ATOM   11881 N  N     . ALA F 1 651 ? 36.273  -36.405 62.035  1 60.97 ? 651 ALA Z N     1 
ATOM   11882 C  CA    . ALA F 1 651 ? 34.9    -35.985 62.291  1 61.21 ? 651 ALA Z CA    1 
ATOM   11883 C  C     . ALA F 1 651 ? 34.855  -34.724 63.156  1 61.38 ? 651 ALA Z C     1 
ATOM   11884 O  O     . ALA F 1 651 ? 33.964  -33.904 62.973  1 61.44 ? 651 ALA Z O     1 
ATOM   11885 C  CB    . ALA F 1 651 ? 34.122  -37.106 62.952  1 61.38 ? 651 ALA Z CB    1 
ATOM   11886 N  N     . GLU F 1 652 ? 35.832  -34.543 64.058  1 61.36 ? 652 GLU Z N     1 
ATOM   11887 C  CA    . GLU F 1 652 ? 35.923  -33.362 64.912  1 61.86 ? 652 GLU Z CA    1 
ATOM   11888 C  C     . GLU F 1 652 ? 36.185  -32.114 64.074  1 61.97 ? 652 GLU Z C     1 
ATOM   11889 O  O     . GLU F 1 652 ? 35.607  -31.067 64.354  1 62.1  ? 652 GLU Z O     1 
ATOM   11890 C  CB    . GLU F 1 652 ? 37.015  -33.543 65.976  1 64.38 ? 652 GLU Z CB    1 
ATOM   11891 C  CG    . GLU F 1 652 ? 37.059  -32.428 67.005  1 69.79 ? 652 GLU Z CG    1 
ATOM   11892 C  CD    . GLU F 1 652 ? 38.014  -32.679 68.154  1 77.02 ? 652 GLU Z CD    1 
ATOM   11893 O  OE1   . GLU F 1 652 ? 38.259  -33.865 68.475  1 78.5  ? 652 GLU Z OE1   1 
ATOM   11894 O  OE2   . GLU F 1 652 ? 38.517  -31.69  68.735  1 79.42 ? 652 GLU Z OE2   1 
ATOM   11895 N  N     . LYS F 1 653 ? 37.009  -32.233 63.017  1 61.75 ? 653 LYS Z N     1 
ATOM   11896 C  CA    . LYS F 1 653 ? 37.278  -31.117 62.11   1 62.06 ? 653 LYS Z CA    1 
ATOM   11897 C  C     . LYS F 1 653 ? 36      -30.709 61.362  1 61.63 ? 653 LYS Z C     1 
ATOM   11898 O  O     . LYS F 1 653 ? 35.775  -29.52  61.131  1 61.68 ? 653 LYS Z O     1 
ATOM   11899 C  CB    . LYS F 1 653 ? 38.405  -31.463 61.124  1 64.45 ? 653 LYS Z CB    1 
ATOM   11900 C  CG    . LYS F 1 653 ? 39.781  -31.516 61.775  1 69.07 ? 653 LYS Z CG    1 
ATOM   11901 C  CD    . LYS F 1 653 ? 40.895  -31.654 60.744  1 73.66 ? 653 LYS Z CD    1 
ATOM   11902 C  CE    . LYS F 1 653 ? 42.226  -31.939 61.396  1 77.49 ? 653 LYS Z CE    1 
ATOM   11903 N  NZ    . LYS F 1 653 ? 43.279  -32.237 60.39   1 79.81 ? 653 LYS Z NZ    1 
ATOM   11904 N  N     . LEU F 1 654 ? 35.155  -31.694 61.012  1 60.99 ? 654 LEU Z N     1 
ATOM   11905 C  CA    . LEU F 1 654 ? 33.874  -31.457 60.356  1 60.83 ? 654 LEU Z CA    1 
ATOM   11906 C  C     . LEU F 1 654 ? 32.938  -30.734 61.329  1 60.67 ? 654 LEU Z C     1 
ATOM   11907 O  O     . LEU F 1 654 ? 32.316  -29.746 60.947  1 60.76 ? 654 LEU Z O     1 
ATOM   11908 C  CB    . LEU F 1 654 ? 33.257  -32.789 59.884  1 60.92 ? 654 LEU Z CB    1 
ATOM   11909 C  CG    . LEU F 1 654 ? 31.805  -32.747 59.407  1 62.12 ? 654 LEU Z CG    1 
ATOM   11910 C  CD1   . LEU F 1 654 ? 31.653  -31.841 58.232  1 62.41 ? 654 LEU Z CD1   1 
ATOM   11911 C  CD2   . LEU F 1 654 ? 31.298  -34.134 59.063  1 62.82 ? 654 LEU Z CD2   1 
ATOM   11912 N  N     . VAL F 1 655 ? 32.868  -31.197 62.589  1 60.23 ? 655 VAL Z N     1 
ATOM   11913 C  CA    . VAL F 1 655 ? 32.027  -30.582 63.614  1 60.16 ? 655 VAL Z CA    1 
ATOM   11914 C  C     . VAL F 1 655 ? 32.413  -29.119 63.844  1 60.11 ? 655 VAL Z C     1 
ATOM   11915 O  O     . VAL F 1 655 ? 31.539  -28.254 63.858  1 60.27 ? 655 VAL Z O     1 
ATOM   11916 C  CB    . VAL F 1 655 ? 32.033  -31.412 64.916  1 60.75 ? 655 VAL Z CB    1 
ATOM   11917 C  CG1   . VAL F 1 655 ? 31.4    -30.647 66.072  1 61.41 ? 655 VAL Z CG1   1 
ATOM   11918 C  CG2   . VAL F 1 655 ? 31.322  -32.738 64.705  1 61.13 ? 655 VAL Z CG2   1 
ATOM   11919 N  N     . ASN F 1 656 ? 33.718  -28.834 63.953  1 59.74 ? 656 ASN Z N     1 
ATOM   11920 C  CA    . ASN F 1 656 ? 34.197  -27.466 64.147  1 59.81 ? 656 ASN Z CA    1 
ATOM   11921 C  C     . ASN F 1 656 ? 33.853  -26.566 62.961  1 59.67 ? 656 ASN Z C     1 
ATOM   11922 O  O     . ASN F 1 656 ? 33.537  -25.393 63.152  1 59.74 ? 656 ASN Z O     1 
ATOM   11923 C  CB    . ASN F 1 656 ? 35.695  -27.453 64.428  1 60.87 ? 656 ASN Z CB    1 
ATOM   11924 C  CG    . ASN F 1 656 ? 36.049  -28.026 65.777  1 63.82 ? 656 ASN Z CG    1 
ATOM   11925 O  OD1   . ASN F 1 656 ? 35.214  -28.107 66.686  1 64.74 ? 656 ASN Z OD1   1 
ATOM   11926 N  ND2   . ASN F 1 656 ? 37.296  -28.442 65.934  1 64.48 ? 656 ASN Z ND2   1 
ATOM   11927 N  N     . TYR F 1 657 ? 33.889  -27.128 61.745  1 59.4  ? 657 TYR Z N     1 
ATOM   11928 C  CA    . TYR F 1 657 ? 33.549  -26.432 60.505  1 59.64 ? 657 TYR Z CA    1 
ATOM   11929 C  C     . TYR F 1 657 ? 32.059  -26.076 60.508  1 59.8  ? 657 TYR Z C     1 
ATOM   11930 O  O     . TYR F 1 657 ? 31.706  -24.952 60.161  1 59.94 ? 657 TYR Z O     1 
ATOM   11931 C  CB    . TYR F 1 657 ? 33.921  -27.317 59.295  1 59.59 ? 657 TYR Z CB    1 
ATOM   11932 C  CG    . TYR F 1 657 ? 33.405  -26.849 57.951  1 60.14 ? 657 TYR Z CG    1 
ATOM   11933 C  CD1   . TYR F 1 657 ? 34.041  -25.831 57.257  1 60.91 ? 657 TYR Z CD1   1 
ATOM   11934 C  CD2   . TYR F 1 657 ? 32.355  -27.502 57.323  1 60.93 ? 657 TYR Z CD2   1 
ATOM   11935 C  CE1   . TYR F 1 657 ? 33.597  -25.424 56.005  1 61.75 ? 657 TYR Z CE1   1 
ATOM   11936 C  CE2   . TYR F 1 657 ? 31.904  -27.108 56.071  1 61.75 ? 657 TYR Z CE2   1 
ATOM   11937 C  CZ    . TYR F 1 657 ? 32.532  -26.071 55.41   1 62.55 ? 657 TYR Z CZ    1 
ATOM   11938 O  OH    . TYR F 1 657 ? 32.082  -25.681 54.174  1 63.8  ? 657 TYR Z OH    1 
ATOM   11939 N  N     . ILE F 1 658 ? 31.195  -27.019 60.932  1 59.62 ? 658 ILE Z N     1 
ATOM   11940 C  CA    . ILE F 1 658 ? 29.748  -26.8   61.011  1 59.91 ? 658 ILE Z CA    1 
ATOM   11941 C  C     . ILE F 1 658 ? 29.44   -25.71  62.037  1 59.92 ? 658 ILE Z C     1 
ATOM   11942 O  O     . ILE F 1 658 ? 28.658  -24.802 61.757  1 60.06 ? 658 ILE Z O     1 
ATOM   11943 C  CB    . ILE F 1 658 ? 28.997  -28.119 61.338  1 60.54 ? 658 ILE Z CB    1 
ATOM   11944 C  CG1   . ILE F 1 658 ? 29.149  -29.15  60.204  1 61.65 ? 658 ILE Z CG1   1 
ATOM   11945 C  CG2   . ILE F 1 658 ? 27.521  -27.86  61.645  1 60.98 ? 658 ILE Z CG2   1 
ATOM   11946 C  CD1   . ILE F 1 658 ? 28.694  -30.543 60.582  1 63.07 ? 658 ILE Z CD1   1 
ATOM   11947 N  N     . LYS F 1 659 ? 30.089  -25.777 63.205  1 59.67 ? 659 LYS Z N     1 
ATOM   11948 C  CA    . LYS F 1 659 ? 29.898  -24.798 64.272  1 59.94 ? 659 LYS Z CA    1 
ATOM   11949 C  C     . LYS F 1 659 ? 30.26   -23.382 63.843  1 60.04 ? 659 LYS Z C     1 
ATOM   11950 O  O     . LYS F 1 659 ? 29.487  -22.456 64.072  1 60.13 ? 659 LYS Z O     1 
ATOM   11951 C  CB    . LYS F 1 659 ? 30.703  -25.188 65.523  1 61.75 ? 659 LYS Z CB    1 
ATOM   11952 C  CG    . LYS F 1 659 ? 30.048  -26.266 66.367  1 65.81 ? 659 LYS Z CG    1 
ATOM   11953 C  CD    . LYS F 1 659 ? 30.778  -26.463 67.695  1 70.25 ? 659 LYS Z CD    1 
ATOM   11954 C  CE    . LYS F 1 659 ? 30.718  -25.238 68.579  1 73.94 ? 659 LYS Z CE    1 
ATOM   11955 N  NZ    . LYS F 1 659 ? 31.306  -25.493 69.923  1 75.86 ? 659 LYS Z NZ    1 
ATOM   11956 N  N     . LEU F 1 660 ? 31.426  -23.217 63.214  1 59.92 ? 660 LEU Z N     1 
ATOM   11957 C  CA    . LEU F 1 660 ? 31.91   -21.915 62.774  1 60.35 ? 660 LEU Z CA    1 
ATOM   11958 C  C     . LEU F 1 660 ? 31.095  -21.351 61.613  1 60.55 ? 660 LEU Z C     1 
ATOM   11959 O  O     . LEU F 1 660 ? 30.87   -20.143 61.548  1 60.65 ? 660 LEU Z O     1 
ATOM   11960 C  CB    . LEU F 1 660 ? 33.385  -22.024 62.367  1 60.64 ? 660 LEU Z CB    1 
ATOM   11961 C  CG    . LEU F 1 660 ? 34.395  -21.427 63.34   1 62.11 ? 660 LEU Z CG    1 
ATOM   11962 C  CD1   . LEU F 1 660 ? 34.351  -22.127 64.682  1 62.53 ? 660 LEU Z CD1   1 
ATOM   11963 C  CD2   . LEU F 1 660 ? 35.794  -21.487 62.767  1 62.85 ? 660 LEU Z CD2   1 
ATOM   11964 N  N     . ASN F 1 661 ? 30.651  -22.216 60.702  1 60.41 ? 661 ASN Z N     1 
ATOM   11965 C  CA    . ASN F 1 661 ? 29.897  -21.778 59.536  1 60.73 ? 661 ASN Z CA    1 
ATOM   11966 C  C     . ASN F 1 661 ? 28.39   -21.936 59.672  1 60.89 ? 661 ASN Z C     1 
ATOM   11967 O  O     . ASN F 1 661 ? 27.694  -22.059 58.662  1 60.91 ? 661 ASN Z O     1 
ATOM   11968 C  CB    . ASN F 1 661 ? 30.412  -22.475 58.295  1 61.95 ? 661 ASN Z CB    1 
ATOM   11969 C  CG    . ASN F 1 661 ? 31.829  -22.094 57.974  1 65.43 ? 661 ASN Z CG    1 
ATOM   11970 O  OD1   . ASN F 1 661 ? 32.768  -22.863 58.187  1 66.61 ? 661 ASN Z OD1   1 
ATOM   11971 N  ND2   . ASN F 1 661 ? 32.016  -20.883 57.471  1 66.24 ? 661 ASN Z ND2   1 
ATOM   11972 N  N     . PHE F 1 662 ? 27.876  -21.91  60.912  1 60.86 ? 662 PHE Z N     1 
ATOM   11973 C  CA    . PHE F 1 662 ? 26.437  -22.004 61.13   1 61.23 ? 662 PHE Z CA    1 
ATOM   11974 C  C     . PHE F 1 662 ? 25.85   -20.601 61.065  1 61.38 ? 662 PHE Z C     1 
ATOM   11975 O  O     . PHE F 1 662 ? 25.42   -20.043 62.073  1 61.46 ? 662 PHE Z O     1 
ATOM   11976 C  CB    . PHE F 1 662 ? 26.102  -22.68  62.465  1 61.18 ? 662 PHE Z CB    1 
ATOM   11977 C  CG    . PHE F 1 662 ? 24.765  -23.382 62.441  1 61.87 ? 662 PHE Z CG    1 
ATOM   11978 C  CD1   . PHE F 1 662 ? 24.665  -24.703 62.045  1 62.62 ? 662 PHE Z CD1   1 
ATOM   11979 C  CD2   . PHE F 1 662 ? 23.606  -22.715 62.799  1 62.71 ? 662 PHE Z CD2   1 
ATOM   11980 C  CE1   . PHE F 1 662 ? 23.433  -25.345 62.019  1 63.32 ? 662 PHE Z CE1   1 
ATOM   11981 C  CE2   . PHE F 1 662 ? 22.376  -23.357 62.763  1 63.43 ? 662 PHE Z CE2   1 
ATOM   11982 C  CZ    . PHE F 1 662 ? 22.299  -24.67  62.384  1 63.19 ? 662 PHE Z CZ    1 
ATOM   11983 N  N     . LYS F 1 663 ? 25.883  -20.019 59.871  1 61.24 ? 663 LYS Z N     1 
ATOM   11984 C  CA    . LYS F 1 663 ? 25.377  -18.681 59.595  1 61.47 ? 663 LYS Z CA    1 
ATOM   11985 C  C     . LYS F 1 663 ? 24.87   -18.65  58.152  1 61.25 ? 663 LYS Z C     1 
ATOM   11986 O  O     . LYS F 1 663 ? 25.467  -19.274 57.273  1 61.23 ? 663 LYS Z O     1 
ATOM   11987 C  CB    . LYS F 1 663 ? 26.486  -17.635 59.809  1 63.4  ? 663 LYS Z CB    1 
ATOM   11988 C  CG    . LYS F 1 663 ? 25.985  -16.195 59.774  1 67.53 ? 663 LYS Z CG    1 
ATOM   11989 C  CD    . LYS F 1 663 ? 27.122  -15.201 59.571  1 71.86 ? 663 LYS Z CD    1 
ATOM   11990 C  CE    . LYS F 1 663 ? 26.642  -13.86  59.059  1 75.31 ? 663 LYS Z CE    1 
ATOM   11991 N  NZ    . LYS F 1 663 ? 26.125  -13.943 57.665  1 77.2  ? 663 LYS Z NZ    1 
ATOM   11992 N  N     . SER F 1 664 ? 23.754  -17.953 57.913  1 61.02 ? 664 SER Z N     1 
ATOM   11993 C  CA    . SER F 1 664 ? 23.181  -17.873 56.577  1 61.42 ? 664 SER Z CA    1 
ATOM   11994 C  C     . SER F 1 664 ? 22.49   -16.548 56.324  1 61.79 ? 664 SER Z C     1 
ATOM   11995 O  O     . SER F 1 664 ? 21.906  -15.963 57.229  1 61.85 ? 664 SER Z O     1 
ATOM   11996 C  CB    . SER F 1 664 ? 22.191  -19.01  56.349  1 62.54 ? 664 SER Z CB    1 
ATOM   11997 O  OG    . SER F 1 664 ? 21.57   -18.93  55.075  1 64.44 ? 664 SER Z OG    1 
ATOM   11998 N  N     . ASN F 1 665 ? 22.536  -16.087 55.081  1 61.91 ? 665 ASN Z N     1 
ATOM   11999 C  CA    . ASN F 1 665 ? 21.84   -14.867 54.683  1 62.48 ? 665 ASN Z CA    1 
ATOM   12000 C  C     . ASN F 1 665 ? 20.387  -15.157 54.235  1 62.44 ? 665 ASN Z C     1 
ATOM   12001 O  O     . ASN F 1 665 ? 19.591  -14.228 54.122  1 62.5  ? 665 ASN Z O     1 
ATOM   12002 C  CB    . ASN F 1 665 ? 22.606  -14.156 53.567  1 64.06 ? 665 ASN Z CB    1 
ATOM   12003 C  CG    . ASN F 1 665 ? 23.967  -13.664 53.986  1 67.91 ? 665 ASN Z CG    1 
ATOM   12004 O  OD1   . ASN F 1 665 ? 24.317  -13.65  55.174  1 69.37 ? 665 ASN Z OD1   1 
ATOM   12005 N  ND2   . ASN F 1 665 ? 24.765  -13.243 53.016  1 68.64 ? 665 ASN Z ND2   1 
ATOM   12006 N  N     . ILE F 1 666 ? 20.044  -16.436 53.981  1 62.16 ? 666 ILE Z N     1 
ATOM   12007 C  CA    . ILE F 1 666 ? 18.718  -16.84  53.54   1 62.23 ? 666 ILE Z CA    1 
ATOM   12008 C  C     . ILE F 1 666 ? 17.961  -17.579 54.645  1 62.03 ? 666 ILE Z C     1 
ATOM   12009 O  O     . ILE F 1 666 ? 16.828  -17.208 54.958  1 62.13 ? 666 ILE Z O     1 
ATOM   12010 C  CB    . ILE F 1 666 ? 18.845  -17.695 52.259  1 62.77 ? 666 ILE Z CB    1 
ATOM   12011 C  CG1   . ILE F 1 666 ? 19.559  -16.921 51.145  1 63.83 ? 666 ILE Z CG1   1 
ATOM   12012 C  CG2   . ILE F 1 666 ? 17.491  -18.207 51.806  1 63.24 ? 666 ILE Z CG2   1 
ATOM   12013 C  CD1   . ILE F 1 666 ? 19.949  -17.775 49.959  1 65.27 ? 666 ILE Z CD1   1 
ATOM   12014 N  N     . PHE F 1 667 ? 18.588  -18.609 55.248  1 61.63 ? 667 PHE Z N     1 
ATOM   12015 C  CA    . PHE F 1 667 ? 17.953  -19.417 56.29   1 61.71 ? 667 PHE Z CA    1 
ATOM   12016 C  C     . PHE F 1 667 ? 18.064  -18.801 57.674  1 61.86 ? 667 PHE Z C     1 
ATOM   12017 O  O     . PHE F 1 667 ? 19.147  -18.393 58.091  1 62.02 ? 667 PHE Z O     1 
ATOM   12018 C  CB    . PHE F 1 667 ? 18.514  -20.85  56.291  1 61.46 ? 667 PHE Z CB    1 
ATOM   12019 C  CG    . PHE F 1 667 ? 17.511  -21.911 56.681  1 61.9  ? 667 PHE Z CG    1 
ATOM   12020 C  CD1   . PHE F 1 667 ? 17.344  -22.276 57.998  1 62.44 ? 667 PHE Z CD1   1 
ATOM   12021 C  CD2   . PHE F 1 667 ? 16.766  -22.572 55.72   1 62.66 ? 667 PHE Z CD2   1 
ATOM   12022 C  CE1   . PHE F 1 667 ? 16.433  -23.263 58.351  1 62.99 ? 667 PHE Z CE1   1 
ATOM   12023 C  CE2   . PHE F 1 667 ? 15.831  -23.533 56.081  1 63.18 ? 667 PHE Z CE2   1 
ATOM   12024 C  CZ    . PHE F 1 667 ? 15.671  -23.871 57.395  1 62.8  ? 667 PHE Z CZ    1 
ATOM   12025 N  N     . ASP F 1 668 ? 16.938  -18.745 58.392  1 61.66 ? 668 ASP Z N     1 
ATOM   12026 C  CA    . ASP F 1 668 ? 16.875  -18.199 59.738  1 61.93 ? 668 ASP Z CA    1 
ATOM   12027 C  C     . ASP F 1 668 ? 17.531  -19.187 60.678  1 62.04 ? 668 ASP Z C     1 
ATOM   12028 O  O     . ASP F 1 668 ? 16.876  -20.119 61.133  1 62.07 ? 668 ASP Z O     1 
ATOM   12029 C  CB    . ASP F 1 668 ? 15.41   -17.979 60.148  1 63.52 ? 668 ASP Z CB    1 
ATOM   12030 C  CG    . ASP F 1 668 ? 15.226  -17.124 61.384  1 68.31 ? 668 ASP Z CG    1 
ATOM   12031 O  OD1   . ASP F 1 668 ? 16.145  -17.095 62.229  1 69.22 ? 668 ASP Z OD1   1 
ATOM   12032 O  OD2   . ASP F 1 668 ? 14.157  -16.489 61.511  1 70.55 ? 668 ASP Z OD2   1 
ATOM   12033 N  N     . THR F 1 669 ? 18.819  -18.982 60.98   1 61.96 ? 669 THR Z N     1 
ATOM   12034 C  CA    . THR F 1 669 ? 19.553  -19.86  61.893  1 62.4  ? 669 THR Z CA    1 
ATOM   12035 C  C     . THR F 1 669 ? 19.156  -19.7   63.375  1 62.7  ? 669 THR Z C     1 
ATOM   12036 O  O     . THR F 1 669 ? 19.632  -20.464 64.212  1 62.83 ? 669 THR Z O     1 
ATOM   12037 C  CB    . THR F 1 669 ? 21.057  -19.693 61.698  1 63.74 ? 669 THR Z CB    1 
ATOM   12038 O  OG1   . THR F 1 669 ? 21.405  -18.342 61.992  1 64.89 ? 669 THR Z OG1   1 
ATOM   12039 C  CG2   . THR F 1 669 ? 21.502  -20.042 60.288  1 64.02 ? 669 THR Z CG2   1 
ATOM   12040 N  N     . GLY F 1 670 ? 18.29   -18.732 63.679  1 62.7  ? 670 GLY Z N     1 
ATOM   12041 C  CA    . GLY F 1 670 ? 17.79   -18.484 65.025  1 63.2  ? 670 GLY Z CA    1 
ATOM   12042 C  C     . GLY F 1 670 ? 16.902  -19.59  65.562  1 63.56 ? 670 GLY Z C     1 
ATOM   12043 O  O     . GLY F 1 670 ? 16.699  -19.683 66.772  1 63.83 ? 670 GLY Z O     1 
ATOM   12044 N  N     . PHE F 1 671 ? 16.367  -20.444 64.672  1 63.45 ? 671 PHE Z N     1 
ATOM   12045 C  CA    . PHE F 1 671 ? 15.543  -21.591 65.055  1 63.93 ? 671 PHE Z CA    1 
ATOM   12046 C  C     . PHE F 1 671 ? 16.401  -22.793 65.542  1 63.96 ? 671 PHE Z C     1 
ATOM   12047 O  O     . PHE F 1 671 ? 15.849  -23.801 65.966  1 64.11 ? 671 PHE Z O     1 
ATOM   12048 C  CB    . PHE F 1 671 ? 14.642  -22.008 63.878  1 64.15 ? 671 PHE Z CB    1 
ATOM   12049 C  CG    . PHE F 1 671 ? 13.289  -22.552 64.281  1 65.26 ? 671 PHE Z CG    1 
ATOM   12050 C  CD1   . PHE F 1 671 ? 12.235  -21.7   64.558  1 66.26 ? 671 PHE Z CD1   1 
ATOM   12051 C  CD2   . PHE F 1 671 ? 13.07   -23.916 64.37   1 66.31 ? 671 PHE Z CD2   1 
ATOM   12052 C  CE1   . PHE F 1 671 ? 10.99   -22.205 64.934  1 67.12 ? 671 PHE Z CE1   1 
ATOM   12053 C  CE2   . PHE F 1 671 ? 11.83   -24.418 64.76   1 67.15 ? 671 PHE Z CE2   1 
ATOM   12054 C  CZ    . PHE F 1 671 ? 10.795  -23.56  65.028  1 66.99 ? 671 PHE Z CZ    1 
ATOM   12055 N  N     . PHE F 1 672 ? 17.739  -22.685 65.503  1 63.69 ? 672 PHE Z N     1 
ATOM   12056 C  CA    . PHE F 1 672 ? 18.624  -23.76  65.923  1 64.01 ? 672 PHE Z CA    1 
ATOM   12057 C  C     . PHE F 1 672 ? 19.562  -23.333 67.024  1 64.51 ? 672 PHE Z C     1 
ATOM   12058 O  O     . PHE F 1 672 ? 19.992  -22.185 67.071  1 64.7  ? 672 PHE Z O     1 
ATOM   12059 C  CB    . PHE F 1 672 ? 19.488  -24.213 64.746  1 63.82 ? 672 PHE Z CB    1 
ATOM   12060 C  CG    . PHE F 1 672 ? 18.742  -24.874 63.623  1 64.34 ? 672 PHE Z CG    1 
ATOM   12061 C  CD1   . PHE F 1 672 ? 18.235  -24.129 62.575  1 65.01 ? 672 PHE Z CD1   1 
ATOM   12062 C  CD2   . PHE F 1 672 ? 18.581  -26.246 63.592  1 65.1  ? 672 PHE Z CD2   1 
ATOM   12063 C  CE1   . PHE F 1 672 ? 17.551  -24.74  61.54   1 65.66 ? 672 PHE Z CE1   1 
ATOM   12064 C  CE2   . PHE F 1 672 ? 17.907  -26.855 62.549  1 65.75 ? 672 PHE Z CE2   1 
ATOM   12065 C  CZ    . PHE F 1 672 ? 17.408  -26.1   61.525  1 65.48 ? 672 PHE Z CZ    1 
ATOM   12066 N  N     . HIS F 1 673 ? 19.942  -24.279 67.866  1 64.72 ? 673 HIS Z N     1 
ATOM   12067 C  CA    . HIS F 1 673 ? 20.921  -24.039 68.905  1 65.57 ? 673 HIS Z CA    1 
ATOM   12068 C  C     . HIS F 1 673 ? 21.879  -25.2   68.851  1 65.98 ? 673 HIS Z C     1 
ATOM   12069 O  O     . HIS F 1 673 ? 21.479  -26.322 69.152  1 66.1  ? 673 HIS Z O     1 
ATOM   12070 C  CB    . HIS F 1 673 ? 20.27   -23.965 70.286  1 66.87 ? 673 HIS Z CB    1 
ATOM   12071 C  CG    . HIS F 1 673 ? 21.274  -23.841 71.389  1 70.05 ? 673 HIS Z CG    1 
ATOM   12072 N  ND1   . HIS F 1 673 ? 21.601  -24.92  72.192  1 72.18 ? 673 HIS Z ND1   1 
ATOM   12073 C  CD2   . HIS F 1 673 ? 22.039  -22.783 71.745  1 71.48 ? 673 HIS Z CD2   1 
ATOM   12074 C  CE1   . HIS F 1 673 ? 22.523  -24.476 73.03   1 72.85 ? 673 HIS Z CE1   1 
ATOM   12075 N  NE2   . HIS F 1 673 ? 22.82   -23.195 72.799  1 72.77 ? 673 HIS Z NE2   1 
ATOM   12076 N  N     . ILE F 1 674 ? 23.123  -24.956 68.434  1 66.14 ? 674 ILE Z N     1 
ATOM   12077 C  CA    . ILE F 1 674 ? 24.107  -26.026 68.369  1 66.87 ? 674 ILE Z CA    1 
ATOM   12078 C  C     . ILE F 1 674 ? 24.927  -26.046 69.657  1 67.72 ? 674 ILE Z C     1 
ATOM   12079 O  O     . ILE F 1 674 ? 25.737  -25.156 69.912  1 67.82 ? 674 ILE Z O     1 
ATOM   12080 C  CB    . ILE F 1 674 ? 24.94   -26.001 67.069  1 67.35 ? 674 ILE Z CB    1 
ATOM   12081 C  CG1   . ILE F 1 674 ? 25.56   -24.616 66.828  1 68.37 ? 674 ILE Z CG1   1 
ATOM   12082 C  CG2   . ILE F 1 674 ? 24.062  -26.417 65.885  1 67.8  ? 674 ILE Z CG2   1 
ATOM   12083 C  CD1   . ILE F 1 674 ? 26.499  -24.556 65.691  1 69.7  ? 674 ILE Z CD1   1 
ATOM   12084 N  N     . GLU F 1 675 ? 24.631  -27.035 70.512  1 68.21 ? 675 GLU Z N     1 
ATOM   12085 C  CA    . GLU F 1 675 ? 25.26   -27.245 71.817  1 68.99 ? 675 GLU Z CA    1 
ATOM   12086 C  C     . GLU F 1 675 ? 26.77   -27.447 71.694  1 69.51 ? 675 GLU Z C     1 
ATOM   12087 O  O     . GLU F 1 675 ? 27.534  -26.941 72.517  1 69.6  ? 675 GLU Z O     1 
ATOM   12088 C  CB    . GLU F 1 675 ? 24.615  -28.457 72.5    1 71.28 ? 675 GLU Z CB    1 
ATOM   12089 C  CG    . GLU F 1 675 ? 25.148  -28.761 73.888  1 76.11 ? 675 GLU Z CG    1 
ATOM   12090 C  CD    . GLU F 1 675 ? 24.678  -30.084 74.461  1 82.39 ? 675 GLU Z CD    1 
ATOM   12091 O  OE1   . GLU F 1 675 ? 23.675  -30.634 73.95   1 83.76 ? 675 GLU Z OE1   1 
ATOM   12092 O  OE2   . GLU F 1 675 ? 25.312  -30.572 75.424  1 84.31 ? 675 GLU Z OE2   1 
ATOM   12093 N  N     . GLY F 1 676 ? 27.181  -28.164 70.653  1 69.64 ? 676 GLY Z N     1 
ATOM   12094 C  CA    . GLY F 1 676 ? 28.584  -28.436 70.374  1 70.14 ? 676 GLY Z CA    1 
ATOM   12095 C  C     . GLY F 1 676 ? 28.77   -29.319 69.159  1 70.33 ? 676 GLY Z C     1 
ATOM   12096 O  O     . GLY F 1 676 ? 27.86   -30.056 68.782  1 70.4  ? 676 GLY Z O     1 
HETATM 12097 CA CA    . CA  G 4 .   ? 9.469   -1.78   4.262   1 24.04 2 701 CA  A CA    1 
HETATM 12098 CA CA    . CA  H 4 .   ? 10.678  -1.884  8.77    1 35.22 2 702 CA  A CA    1 
HETATM 12099 CA CA    . CA  I 4 .   ? 22.23   0.647   -2.405  1 50.36 2 703 CA  A CA    1 
HETATM 12100 CA CA    . CA  J 4 .   ? 6.529   -40.623 43.33   1 20.84 2 701 CA  Z CA    1 
HETATM 12101 CA CA    . CA  K 4 .   ? 5.02    -40.776 47.43   1 31.63 2 702 CA  Z CA    1 
HETATM 12102 CA CA    . CA  L 4 .   ? 15.933  -43.865 57.331  1 68.21 2 703 CA  Z CA    1 
HETATM 12103 O  O1    . MES M 5 .   ? 11.988  -35.102 78.564  1 62.12 ? 704 MES Z O1    1 
HETATM 12104 C  C2    . MES M 5 .   ? 11.616  -33.769 78.234  1 62.22 ? 704 MES Z C2    1 
HETATM 12105 C  C3    . MES M 5 .   ? 11.65   -33.545 76.742  1 62.38 ? 704 MES Z C3    1 
HETATM 12106 N  N4    . MES M 5 .   ? 10.761  -34.544 76.041  1 62.45 ? 704 MES Z N4    1 
HETATM 12107 C  C5    . MES M 5 .   ? 11.017  -35.96  76.511  1 62.38 ? 704 MES Z C5    1 
HETATM 12108 C  C6    . MES M 5 .   ? 11.045  -36.023 78.021  1 62.21 ? 704 MES Z C6    1 
HETATM 12109 C  C7    . MES M 5 .   ? 9.304   -34.147 75.969  1 62.48 ? 704 MES Z C7    1 
HETATM 12110 C  C8    . MES M 5 .   ? 8.56    -34.809 74.825  1 62.51 ? 704 MES Z C8    1 
HETATM 12111 S  S     . MES M 5 .   ? 7.615   -33.639 73.876  1 62.6  ? 704 MES Z S     1 
HETATM 12112 O  O1S   . MES M 5 .   ? 8.579   -32.851 73.126  1 62.6  ? 704 MES Z O1S   1 
HETATM 12113 O  O2S   . MES M 5 .   ? 6.865   -32.847 74.837  1 62.56 ? 704 MES Z O2S   1 
HETATM 12114 O  O3S   . MES M 5 .   ? 6.749   -34.43  73.01   1 62.59 ? 704 MES Z O3S   1 
HETATM 12115 H  H21   . MES M 5 .   ? 10.632  -33.545 78.655  0 64.37 ? 704 MES Z H21   1 
HETATM 12116 H  H22   . MES M 5 .   ? 12.334  -33.102 78.716  0 64.88 ? 704 MES Z H22   1 
HETATM 12117 H  H31   . MES M 5 .   ? 12.663  -33.695 76.359  0 64.5  ? 704 MES Z H31   1 
HETATM 12118 H  H32   . MES M 5 .   ? 11.305  -32.54  76.486  0 64.31 ? 704 MES Z H32   1 
HETATM 12119 H  HN4   . MES M 5 .   ? 11.09   -34.508 75.068  0 63.8  ? 704 MES Z HN4   1 
HETATM 12120 H  H51   . MES M 5 .   ? 11.989  -36.247 76.106  0 64.02 ? 704 MES Z H51   1 
HETATM 12121 H  H52   . MES M 5 .   ? 10.244  -36.629 76.127  0 63.57 ? 704 MES Z H52   1 
HETATM 12122 H  H61   . MES M 5 .   ? 10.057  -35.83  78.447  0 63.93 ? 704 MES Z H61   1 
HETATM 12123 H  H62   . MES M 5 .   ? 11.348  -37.024 78.338  0 64.12 ? 704 MES Z H62   1 
HETATM 12124 H  H71   . MES M 5 .   ? 9.296   -33.057 75.881  0 63.73 ? 704 MES Z H71   1 
HETATM 12125 H  H72   . MES M 5 .   ? 8.859   -34.391 76.937  0 63.73 ? 704 MES Z H72   1 
HETATM 12126 H  H81   . MES M 5 .   ? 7.849   -35.55  75.198  0 63.07 ? 704 MES Z H81   1 
HETATM 12127 H  H82   . MES M 5 .   ? 9.233   -35.315 74.129  0 63.16 ? 704 MES Z H82   1 
HETATM 12128 CL CL    . CL  N 6 .   ? -17.954 -73.536 20.807  1 63.51 ? 705 CL  Z CL    1 
HETATM 12129 O  O     . HOH O 7 .   ? 4.967   -3.747  34.496  1 18.08 ? 801 HOH A O     1 
HETATM 12130 O  O     . HOH O 7 .   ? 25.813  7.469   4.892   1 30.75 ? 802 HOH A O     1 
HETATM 12131 O  O     . HOH O 7 .   ? 4.836   1.327   18.991  1 17.6  ? 803 HOH A O     1 
HETATM 12132 O  O     . HOH O 7 .   ? 26.921  12.421  11.284  1 27.06 ? 804 HOH A O     1 
HETATM 12133 O  O     . HOH O 7 .   ? 33.517  -6.875  -20.664 1 38.17 ? 805 HOH A O     1 
HETATM 12134 O  O     . HOH O 7 .   ? -5.949  13.84   24.52   1 26.62 ? 806 HOH A O     1 
HETATM 12135 O  O     . HOH O 7 .   ? 6.382   2.865   14.416  1 20.8  ? 807 HOH A O     1 
HETATM 12136 O  O     . HOH O 7 .   ? -16.004 35.285  12.452  1 35.77 ? 808 HOH A O     1 
HETATM 12137 O  O     . HOH O 7 .   ? 24.244  -8.519  10.473  1 21.37 ? 809 HOH A O     1 
HETATM 12138 O  O     . HOH O 7 .   ? -8.343  -24.204 21.008  1 13.98 ? 810 HOH A O     1 
HETATM 12139 O  O     . HOH O 7 .   ? 51.951  -9.382  5.843   1 34.45 ? 811 HOH A O     1 
HETATM 12140 O  O     . HOH O 7 .   ? -2.528  -16.826 27.885  1 20.9  ? 812 HOH A O     1 
HETATM 12141 O  O     . HOH O 7 .   ? 9.796   -1.955  -17.596 1 41.39 ? 813 HOH A O     1 
HETATM 12142 O  O     . HOH O 7 .   ? 3.141   2.031   -0.926  1 17.15 ? 814 HOH A O     1 
HETATM 12143 O  O     . HOH O 7 .   ? -7.999  -21.197 23.935  1 13.92 ? 815 HOH A O     1 
HETATM 12144 O  O     . HOH O 7 .   ? 14.599  -37.332 3.126   1 24.78 ? 816 HOH A O     1 
HETATM 12145 O  O     . HOH O 7 .   ? 30.254  -1.553  -25.539 1 43.69 ? 817 HOH A O     1 
HETATM 12146 O  O     . HOH O 7 .   ? -19.377 0.004   27.11   1 22.05 ? 818 HOH A O     1 
HETATM 12147 O  O     . HOH O 7 .   ? 16.708  -10.565 19.72   1 15.92 ? 819 HOH A O     1 
HETATM 12148 O  O     . HOH O 7 .   ? 1.613   -27.45  5.987   1 20.14 ? 820 HOH A O     1 
HETATM 12149 O  O     . HOH O 7 .   ? -14.664 15.126  -4.456  1 24.19 ? 821 HOH A O     1 
HETATM 12150 O  O     . HOH O 7 .   ? 6.664   -2.234  -16.357 1 19.28 ? 822 HOH A O     1 
HETATM 12151 O  O     . HOH O 7 .   ? -7.597  31.625  8.945   1 32.49 ? 823 HOH A O     1 
HETATM 12152 O  O     . HOH O 7 .   ? -1.613  -7.059  -15.807 1 31.25 ? 824 HOH A O     1 
HETATM 12153 O  O     . HOH O 7 .   ? 23.581  4.179   1.883   1 24.87 ? 825 HOH A O     1 
HETATM 12154 O  O     . HOH O 7 .   ? 1.62    -7.685  -16.379 1 27.11 ? 826 HOH A O     1 
HETATM 12155 O  O     . HOH O 7 .   ? 15.742  -3.739  11.579  1 22.69 ? 827 HOH A O     1 
HETATM 12156 O  O     . HOH O 7 .   ? -10.426 31.157  3.495   1 31.75 ? 828 HOH A O     1 
HETATM 12157 O  O     . HOH O 7 .   ? 5.281   30.753  0.906   1 34.53 ? 829 HOH A O     1 
HETATM 12158 O  O     . HOH O 7 .   ? -8.774  22.971  -9.49   1 26.96 ? 830 HOH A O     1 
HETATM 12159 O  O     . HOH O 7 .   ? -2.521  6.082   3.888   1 19.62 ? 831 HOH A O     1 
HETATM 12160 O  O     . HOH O 7 .   ? -0.236  -32.554 14.297  1 17.27 ? 832 HOH A O     1 
HETATM 12161 O  O     . HOH O 7 .   ? 18.528  -8.597  8.868   1 18.32 ? 833 HOH A O     1 
HETATM 12162 O  O     . HOH O 7 .   ? -18.832 8.799   17.314  1 24.07 ? 834 HOH A O     1 
HETATM 12163 O  O     . HOH O 7 .   ? 2.358   -16.896 -12.712 1 18.82 ? 835 HOH A O     1 
HETATM 12164 O  O     . HOH O 7 .   ? 5.92    -5.282  32.76   1 25.88 ? 836 HOH A O     1 
HETATM 12165 O  O     . HOH O 7 .   ? -9.731  8.219   -5.416  1 21.11 ? 837 HOH A O     1 
HETATM 12166 O  O     . HOH O 7 .   ? -16.742 12.786  34.098  1 28.28 ? 838 HOH A O     1 
HETATM 12167 O  O     . HOH O 7 .   ? 6.299   -9.147  -4.04   1 16.21 ? 839 HOH A O     1 
HETATM 12168 O  O     . HOH O 7 .   ? 10.945  9.375   26.784  1 25.43 ? 840 HOH A O     1 
HETATM 12169 O  O     . HOH O 7 .   ? 38.946  7.766   10.886  1 39.14 ? 841 HOH A O     1 
HETATM 12170 O  O     . HOH O 7 .   ? -3.175  33.832  24.875  1 35.94 ? 842 HOH A O     1 
HETATM 12171 O  O     . HOH O 7 .   ? -11.798 -9.495  26.102  1 15.37 ? 843 HOH A O     1 
HETATM 12172 O  O     . HOH O 7 .   ? 7.008   -12.934 35.453  1 28.92 ? 844 HOH A O     1 
HETATM 12173 O  O     . HOH O 7 .   ? 3.045   26.418  -4.572  1 28.74 ? 845 HOH A O     1 
HETATM 12174 O  O     . HOH O 7 .   ? -25.992 29.98   19.148  1 35.37 ? 846 HOH A O     1 
HETATM 12175 O  O     . HOH O 7 .   ? -6.373  -16.293 28.538  1 14.38 ? 847 HOH A O     1 
HETATM 12176 O  O     . HOH O 7 .   ? -20.615 10.908  26.335  1 26.5  ? 848 HOH A O     1 
HETATM 12177 O  O     . HOH O 7 .   ? 4.123   -18.732 -11.161 1 18.82 ? 849 HOH A O     1 
HETATM 12178 O  O     . HOH O 7 .   ? 10.366  -1.425  -8.323  1 17.8  ? 850 HOH A O     1 
HETATM 12179 O  O     . HOH O 7 .   ? 26.308  -18.868 -22.973 1 28.58 ? 851 HOH A O     1 
HETATM 12180 O  O     . HOH O 7 .   ? -12.418 35.561  14.741  1 35.93 ? 852 HOH A O     1 
HETATM 12181 O  O     . HOH O 7 .   ? -8.655  21.159  33.762  1 31.39 ? 853 HOH A O     1 
HETATM 12182 O  O     . HOH O 7 .   ? 20.117  -13.674 -22.507 1 26.06 ? 854 HOH A O     1 
HETATM 12183 O  O     . HOH O 7 .   ? 32.403  6.045   24.557  1 27.5  ? 855 HOH A O     1 
HETATM 12184 O  O     . HOH O 7 .   ? 14.7    21.746  -3.434  1 27.48 ? 856 HOH A O     1 
HETATM 12185 O  O     . HOH O 7 .   ? 31.863  -26.27  -8.469  1 30.81 ? 857 HOH A O     1 
HETATM 12186 O  O     . HOH O 7 .   ? -7.885  -19.827 14.225  1 16.18 ? 858 HOH A O     1 
HETATM 12187 O  O     . HOH O 7 .   ? -9.802  -13.696 5.094   1 14.62 ? 859 HOH A O     1 
HETATM 12188 O  O     . HOH O 7 .   ? 5.996   28.442  4.759   1 30.12 ? 860 HOH A O     1 
HETATM 12189 O  O     . HOH O 7 .   ? -6.113  27.087  28.314  1 33.13 ? 861 HOH A O     1 
HETATM 12190 O  O     . HOH O 7 .   ? -22.027 16.908  30.289  1 30.01 ? 862 HOH A O     1 
HETATM 12191 O  O     . HOH O 7 .   ? 32.77   3.65    26.576  1 27.23 ? 863 HOH A O     1 
HETATM 12192 O  O     . HOH O 7 .   ? -11.838 7.448   -3.268  1 26.09 ? 864 HOH A O     1 
HETATM 12193 O  O     . HOH O 7 .   ? 20.947  -17.756 28.058  1 23.98 ? 865 HOH A O     1 
HETATM 12194 O  O     . HOH O 7 .   ? -10.243 -10.411 24.468  1 14.99 ? 866 HOH A O     1 
HETATM 12195 O  O     . HOH O 7 .   ? -13.96  36.568  8.014   1 38.96 ? 867 HOH A O     1 
HETATM 12196 O  O     . HOH O 7 .   ? 3.382   23.348  -6.213  1 27.56 ? 868 HOH A O     1 
HETATM 12197 O  O     . HOH O 7 .   ? 29.242  -12.848 31.917  1 35.62 ? 869 HOH A O     1 
HETATM 12198 O  O     . HOH O 7 .   ? 16.282  -40.964 4.223   1 27.37 ? 870 HOH A O     1 
HETATM 12199 O  O     . HOH O 7 .   ? -15.019 4.341   -10.306 1 20.69 ? 871 HOH A O     1 
HETATM 12200 O  O     . HOH P 7 .   ? 9.456   19.779  17.327  1 27.92 ? 101 HOH E O     1 
HETATM 12201 O  O     . HOH P 7 .   ? 5.343   9.497   -8.185  1 20.11 ? 102 HOH E O     1 
HETATM 12202 O  O     . HOH Q 7 .   ? 6.709   8.037   22.401  1 21.75 ? 101 HOH F O     1 
HETATM 12203 O  O     . HOH Q 7 .   ? 15.299  15.66   27.65   1 33.4  ? 102 HOH F O     1 
HETATM 12204 O  O     . HOH Q 7 .   ? 14.328  23.673  3.745   1 28.23 ? 103 HOH F O     1 
HETATM 12205 O  O     . HOH Q 7 .   ? 13.895  11.361  26.09   1 26.33 ? 104 HOH F O     1 
HETATM 12206 O  O     . HOH Q 7 .   ? 20.13   11.201  -4.219  1 24.15 ? 105 HOH F O     1 
HETATM 12207 O  O     . HOH Q 7 .   ? 5.197   7.509   27.422  1 23    ? 106 HOH F O     1 
HETATM 12208 O  O     . HOH R 7 .   ? -1.1    -59.682 29.611  1 27.04 ? 101 HOH U O     1 
HETATM 12209 O  O     . HOH R 7 .   ? 12.733  -65.999 23.766  1 34.79 ? 102 HOH U O     1 
HETATM 12210 O  O     . HOH R 7 .   ? 7.691   -66.077 47.63   1 39.83 ? 103 HOH U O     1 
HETATM 12211 O  O     . HOH R 7 .   ? 15.049  -58.445 26.008  1 32.15 ? 104 HOH U O     1 
HETATM 12212 O  O     . HOH R 7 .   ? 12.75   -53.969 26.391  1 29.59 ? 105 HOH U O     1 
HETATM 12213 O  O     . HOH R 7 .   ? -0.375  -47.788 59.261  1 20.81 ? 106 HOH U O     1 
HETATM 12214 O  O     . HOH R 7 .   ? 9.486   -65.867 49.64   1 33.83 ? 107 HOH U O     1 
HETATM 12215 O  O     . HOH R 7 .   ? 12.229  -49.729 50.307  1 24.7  ? 108 HOH U O     1 
HETATM 12216 O  O     . HOH S 7 .   ? 8.084   -45.792 49.913  1 21.37 ? 101 HOH V O     1 
HETATM 12217 O  O     . HOH S 7 .   ? 1.978   -66.714 19.398  1 31.18 ? 102 HOH V O     1 
HETATM 12218 O  O     . HOH S 7 .   ? 0.397   -64.182 57.272  1 31.06 ? 103 HOH V O     1 
HETATM 12219 O  O     . HOH S 7 .   ? -2.082  -61.266 61.579  1 29.03 ? 104 HOH V O     1 
HETATM 12220 O  O     . HOH S 7 .   ? 11.199  -65.516 20.935  1 34.09 ? 105 HOH V O     1 
HETATM 12221 O  O     . HOH S 7 .   ? -1.552  -56.417 61.56   1 26.03 ? 106 HOH V O     1 
HETATM 12222 O  O     . HOH S 7 .   ? 4.593   -67.908 21.874  1 43.43 ? 107 HOH V O     1 
HETATM 12223 O  O     . HOH T 7 .   ? 4.814   -22.009 66.288  1 25.79 ? 801 HOH Z O     1 
HETATM 12224 O  O     . HOH T 7 .   ? 3.741   -37.856 64.637  1 21.69 ? 802 HOH Z O     1 
HETATM 12225 O  O     . HOH T 7 .   ? -25.246 -61.649 23.166  1 25.84 ? 803 HOH Z O     1 
HETATM 12226 O  O     . HOH T 7 .   ? 6.509   -38.843 17.192  1 17.47 ? 804 HOH Z O     1 
HETATM 12227 O  O     . HOH T 7 .   ? 12.22   -21.924 27.533  1 22.92 ? 805 HOH Z O     1 
HETATM 12228 O  O     . HOH T 7 .   ? -18.551 -74.718 25.431  1 29.02 ? 806 HOH Z O     1 
HETATM 12229 O  O     . HOH T 7 .   ? 28.282  -25.823 74.634  1 30.07 ? 807 HOH Z O     1 
HETATM 12230 O  O     . HOH T 7 .   ? 4.462   -32.849 69.205  1 24.18 ? 808 HOH Z O     1 
HETATM 12231 O  O     . HOH T 7 .   ? 2.712   -41.228 49.153  1 16.52 ? 809 HOH Z O     1 
HETATM 12232 O  O     . HOH T 7 .   ? -7.833  -18.675 27.678  1 14.15 ? 810 HOH Z O     1 
HETATM 12233 O  O     . HOH T 7 .   ? -7.142  -63.319 27.213  1 26.22 ? 811 HOH Z O     1 
HETATM 12234 O  O     . HOH T 7 .   ? 8.693   -63.081 37.728  1 31.84 ? 812 HOH Z O     1 
HETATM 12235 O  O     . HOH T 7 .   ? 7.97    -50.654 26.083  1 24.72 ? 813 HOH Z O     1 
HETATM 12236 O  O     . HOH T 7 .   ? 13.086  -20.947 29.74   1 14.51 ? 814 HOH Z O     1 
HETATM 12237 O  O     . HOH T 7 .   ? -20.539 -72.743 23.661  1 28.81 ? 815 HOH Z O     1 
HETATM 12238 O  O     . HOH T 7 .   ? 17.191  -30.674 46.417  1 19.51 ? 816 HOH Z O     1 
HETATM 12239 O  O     . HOH T 7 .   ? -3.132  -79.932 51.823  1 36.02 ? 817 HOH Z O     1 
HETATM 12240 O  O     . HOH T 7 .   ? 21.923  -19.447 52.444  1 63.46 ? 818 HOH Z O     1 
HETATM 12241 O  O     . HOH T 7 .   ? 7.835   -21.434 66.024  1 25.75 ? 819 HOH Z O     1 
HETATM 12242 O  O     . HOH T 7 .   ? 3.201   -48.296 13.921  1 24.27 ? 820 HOH Z O     1 
HETATM 12243 O  O     . HOH T 7 .   ? 14.805  -35.067 36.314  1 17.47 ? 821 HOH Z O     1 
HETATM 12244 O  O     . HOH T 7 .   ? 12.596  -52.172 24.7    1 28.63 ? 822 HOH Z O     1 
HETATM 12245 O  O     . HOH T 7 .   ? 11.325  -30.258 17.728  1 15.57 ? 823 HOH Z O     1 
HETATM 12246 O  O     . HOH T 7 .   ? -17.534 -42.179 33.234  1 16.58 ? 824 HOH Z O     1 
HETATM 12247 O  O     . HOH T 7 .   ? 16.525  -44.321 40.43   1 33.28 ? 825 HOH Z O     1 
HETATM 12248 O  O     . HOH T 7 .   ? -18.519 -52.835 20.83   1 37.98 ? 826 HOH Z O     1 
HETATM 12249 O  O     . HOH T 7 .   ? 11.255  -63.444 49.668  1 33.3  ? 827 HOH Z O     1 
HETATM 12250 O  O     . HOH T 7 .   ? 17.804  -46.227 52.291  1 26.2  ? 828 HOH Z O     1 
HETATM 12251 O  O     . HOH T 7 .   ? -11.084 -28.124 33.593  1 14.28 ? 829 HOH Z O     1 
HETATM 12252 O  O     . HOH T 7 .   ? 18.558  -58.271 35.485  1 33.12 ? 830 HOH Z O     1 
HETATM 12253 O  O     . HOH T 7 .   ? 0.433   -73.83  50.772  1 34.42 ? 831 HOH Z O     1 
HETATM 12254 O  O     . HOH T 7 .   ? -3.862  -35.632 11.487  1 20.57 ? 832 HOH Z O     1 
HETATM 12255 O  O     . HOH T 7 .   ? 7.612   -37.792 18.992  1 21.14 ? 833 HOH Z O     1 
HETATM 12256 O  O     . HOH T 7 .   ? 4.363   -70.462 29.121  1 33.46 ? 834 HOH Z O     1 
HETATM 12257 O  O     . HOH T 7 .   ? 11.08   -44.143 33.212  1 39.09 ? 835 HOH Z O     1 
HETATM 12258 O  O     . HOH T 7 .   ? 15.602  -36.368 45.208  1 19.4  ? 836 HOH Z O     1 
HETATM 12259 O  O     . HOH T 7 .   ? -7.176  -78.296 36.804  1 32.54 ? 837 HOH Z O     1 
HETATM 12260 O  O     . HOH T 7 .   ? -16.018 -56.958 14.089  1 23.3  ? 838 HOH Z O     1 
HETATM 12261 O  O     . HOH T 7 .   ? -9.879  -35.559 64.687  1 20.54 ? 839 HOH Z O     1 
HETATM 12262 O  O     . HOH T 7 .   ? -15.754 -65.694 57.735  1 27.1  ? 840 HOH Z O     1 
HETATM 12263 O  O     . HOH T 7 .   ? -21.314 -52.717 19.615  1 25.64 ? 841 HOH Z O     1 
HETATM 12264 O  O     . HOH T 7 .   ? -10.48  -32.321 22.422  1 14.68 ? 842 HOH Z O     1 
HETATM 12265 O  O     . HOH T 7 .   ? -12.541 -71.618 52.005  1 29    ? 843 HOH Z O     1 
HETATM 12266 O  O     . HOH T 7 .   ? 17.629  -57.776 25.97   1 32.79 ? 844 HOH Z O     1 
HETATM 12267 O  O     . HOH T 7 .   ? -24.837 -64.437 21.583  1 26.64 ? 845 HOH Z O     1 
HETATM 12268 O  O     . HOH T 7 .   ? -6.444  -14.733 33.238  1 14.98 ? 846 HOH Z O     1 
HETATM 12269 O  O     . HOH T 7 .   ? 10.915  -19.3   68.041  1 28.75 ? 847 HOH Z O     1 
HETATM 12270 O  O     . HOH T 7 .   ? 35.635  -47.283 33.435  1 34.77 ? 848 HOH Z O     1 
HETATM 12271 O  O     . HOH T 7 .   ? -4.162  -74.456 34.847  1 31.93 ? 849 HOH Z O     1 
HETATM 12272 O  O     . HOH T 7 .   ? -13.678 -29.303 42.558  1 19.5  ? 850 HOH Z O     1 
HETATM 12273 O  O     . HOH T 7 .   ? -4.802  -62.676 49.86   1 31.31 ? 851 HOH Z O     1 
HETATM 12274 O  O     . HOH T 7 .   ? 0.925   -15.808 58.779  1 22.86 ? 852 HOH Z O     1 
HETATM 12275 O  O     . HOH T 7 .   ? 30.11   -30.219 38.762  1 31.88 ? 853 HOH Z O     1 
HETATM 12276 O  O     . HOH T 7 .   ? -22.02  -66.664 51.529  1 25.35 ? 854 HOH Z O     1 
HETATM 12277 O  O     . HOH T 7 .   ? 43.148  -34.721 52.304  1 32.97 ? 855 HOH Z O     1 
HETATM 12278 O  O     . HOH T 7 .   ? 7.387   -58.875 50.38   1 32.18 ? 856 HOH Z O     1 
HETATM 12279 O  O     . HOH T 7 .   ? 7.433   -49.436 14.222  1 26.43 ? 857 HOH Z O     1 
HETATM 12280 O  O     . HOH T 7 .   ? -1.552  -64.919 24.824  1 28.85 ? 858 HOH Z O     1 
HETATM 12281 O  O     . HOH T 7 .   ? -17.377 -32.596 41.537  1 21.37 ? 859 HOH Z O     1 
HETATM 12282 O  O     . HOH T 7 .   ? 16.35   -54.414 45.513  1 30.24 ? 860 HOH Z O     1 
HETATM 12283 O  O     . HOH T 7 .   ? 23.135  -47.974 72.73   1 31.87 ? 861 HOH Z O     1 
HETATM 12284 O  O     . HOH T 7 .   ? 26.651  -22.245 50.086  1 26.46 ? 862 HOH Z O     1 
HETATM 12285 O  O     . HOH T 7 .   ? -0.67   -33.88  55.593  1 41.51 ? 863 HOH Z O     1 
HETATM 12286 O  O     . HOH T 7 .   ? -17.989 -33.793 31.47   1 16.6  ? 864 HOH Z O     1 
HETATM 12287 O  O     . HOH T 7 .   ? -4.676  -52.221 57.681  1 21.88 ? 865 HOH Z O     1 
HETATM 12288 O  O     . HOH T 7 .   ? 11.174  -37.053 39.166  1 17.59 ? 866 HOH Z O     1 
HETATM 12289 O  O     . HOH T 7 .   ? -20.67  -28.838 51.606  1 25.29 ? 867 HOH Z O     1 
HETATM 12290 O  O     . HOH T 7 .   ? 11.219  -26.02  27.721  1 25.39 ? 868 HOH Z O     1 
HETATM 12291 O  O     . HOH T 7 .   ? -13.648 -19.655 48.232  1 17.02 ? 869 HOH Z O     1 
HETATM 12292 O  O     . HOH T 7 .   ? -17.821 -34.377 18.589  1 22.61 ? 870 HOH Z O     1 
HETATM 12293 O  O     . HOH T 7 .   ? -12.408 -22.765 32.676  1 14.31 ? 871 HOH Z O     1 
HETATM 12294 O  O     . HOH T 7 .   ? -11.836 -36.519 61.793  1 18.8  ? 872 HOH Z O     1 
HETATM 12295 O  O     . HOH T 7 .   ? 7.941   -19.318 68.61   1 32.42 ? 873 HOH Z O     1 
HETATM 12296 O  O     . HOH T 7 .   ? -0.007  -60.555 53.429  1 27.93 ? 874 HOH Z O     1 
HETATM 12297 O  O     . HOH T 7 .   ? -24.212 -61.996 53.445  1 24.43 ? 875 HOH Z O     1 
HETATM 12298 O  O     . HOH T 7 .   ? -7.126  -66.551 60.067  1 30.32 ? 876 HOH Z O     1 
HETATM 12299 O  O     . HOH T 7 .   ? -22.215 -58.548 47.959  1 23.28 ? 877 HOH Z O     1 
HETATM 12300 O  O     . HOH T 7 .   ? 2.788   -48.122 10.545  1 25.06 ? 878 HOH Z O     1 
HETATM 12301 O  O     . HOH T 7 .   ? -10.994 -77.294 25.883  1 30.77 ? 879 HOH Z O     1 
HETATM 12302 O  O     . HOH T 7 .   ? -22.718 -47.089 57.851  1 21.51 ? 880 HOH Z O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N  N     . MET A 1   ? 0.6851 0.2058 0.1661 -0.0531 0.1867 -0.0221 1   MET A N     
2     C  CA    . MET A 1   ? 0.6838 0.2151 0.1731 -0.0513 0.1872 -0.0216 1   MET A CA    
3     C  C     . MET A 1   ? 0.6839 0.2219 0.1816 -0.0548 0.1823 -0.0227 1   MET A C     
4     O  O     . MET A 1   ? 0.6899 0.2227 0.1848 -0.0582 0.1784 -0.0237 1   MET A O     
5     C  CB    . MET A 1   ? 0.6911 0.2175 0.1732 -0.0486 0.1896 -0.0207 1   MET A CB    
6     C  CG    . MET A 1   ? 0.7046 0.2415 0.1945 -0.0471 0.1902 -0.02   1   MET A CG    
7     S  SD    . MET A 1   ? 0.7263 0.2587 0.2088 -0.0436 0.1937 -0.0185 1   MET A SD    
8     C  CE    . MET A 1   ? 0.7301 0.2502 0.2035 -0.0468 0.1897 -0.0202 1   MET A CE    
9     N  N     . ASN A 2   ? 0.674  0.2234 0.1817 -0.0539 0.1826 -0.0224 2   ASN A N     
10    C  CA    . ASN A 2   ? 0.6709 0.2266 0.1861 -0.0564 0.1787 -0.0232 2   ASN A CA    
11    C  C     . ASN A 2   ? 0.6743 0.234  0.1911 -0.0549 0.1797 -0.0228 2   ASN A C     
12    O  O     . ASN A 2   ? 0.6733 0.2372 0.1913 -0.0521 0.1833 -0.0218 2   ASN A O     
13    C  CB    . ASN A 2   ? 0.6696 0.2343 0.1947 -0.0572 0.178  -0.0233 2   ASN A CB    
14    C  CG    . ASN A 2   ? 0.6957 0.2575 0.2211 -0.06   0.1753 -0.0238 2   ASN A CG    
15    O  OD1   . ASN A 2   ? 0.7069 0.2619 0.2272 -0.0626 0.1723 -0.0242 2   ASN A OD1   
16    N  ND2   . ASN A 2   ? 0.7005 0.2674 0.2316 -0.0598 0.1762 -0.0235 2   ASN A ND2   
17    N  N     . VAL A 3   ? 0.6774 0.2355 0.1937 -0.0567 0.1767 -0.0235 3   VAL A N     
18    C  CA    . VAL A 3   ? 0.6839 0.2449 0.2011 -0.0556 0.1775 -0.0232 3   VAL A CA    
19    C  C     . VAL A 3   ? 0.683  0.2518 0.2086 -0.0571 0.1751 -0.0237 3   VAL A C     
20    O  O     . VAL A 3   ? 0.6854 0.2539 0.2131 -0.0594 0.1716 -0.0243 3   VAL A O     
21    C  CB    . VAL A 3   ? 0.7009 0.2525 0.2088 -0.0556 0.1769 -0.0234 3   VAL A CB    
22    C  CG1   . VAL A 3   ? 0.7065 0.2612 0.2156 -0.0545 0.1779 -0.0231 3   VAL A CG1   
23    C  CG2   . VAL A 3   ? 0.7147 0.2576 0.2132 -0.0535 0.18   -0.0227 3   VAL A CG2   
24    N  N     . PHE A 4   ? 0.6774 0.2532 0.2076 -0.0559 0.1771 -0.0233 4   PHE A N     
25    C  CA    . PHE A 4   ? 0.6777 0.26   0.2146 -0.0571 0.1756 -0.0236 4   PHE A CA    
26    C  C     . PHE A 4   ? 0.6737 0.2561 0.2089 -0.0566 0.1765 -0.0235 4   PHE A C     
27    O  O     . PHE A 4   ? 0.6744 0.2553 0.2056 -0.0549 0.1793 -0.0227 4   PHE A O     
28    C  CB    . PHE A 4   ? 0.6771 0.2677 0.2211 -0.0566 0.1771 -0.0233 4   PHE A CB    
29    C  CG    . PHE A 4   ? 0.6902 0.281  0.2362 -0.0568 0.1768 -0.0233 4   PHE A CG    
30    C  CD1   . PHE A 4   ? 0.7023 0.2939 0.2521 -0.0586 0.1739 -0.0237 4   PHE A CD1   
31    C  CD2   . PHE A 4   ? 0.7029 0.2933 0.2469 -0.055  0.1797 -0.0226 4   PHE A CD2   
32    C  CE1   . PHE A 4   ? 0.7121 0.3039 0.2637 -0.059  0.1737 -0.0236 4   PHE A CE1   
33    C  CE2   . PHE A 4   ? 0.7128 0.3028 0.2581 -0.0552 0.1796 -0.0226 4   PHE A CE2   
34    C  CZ    . PHE A 4   ? 0.7099 0.3006 0.2591 -0.0573 0.1765 -0.0232 4   PHE A CZ    
35    N  N     . ARG A 5   ? 0.6675 0.2518 0.2055 -0.0579 0.1745 -0.024  5   ARG A N     
36    C  CA    . ARG A 5   ? 0.6685 0.2529 0.2048 -0.0577 0.1755 -0.024  5   ARG A CA    
37    C  C     . ARG A 5   ? 0.6653 0.2568 0.2075 -0.0585 0.1761 -0.024  5   ARG A C     
38    O  O     . ARG A 5   ? 0.6642 0.2585 0.2109 -0.0594 0.1744 -0.0244 5   ARG A O     
39    C  CB    . ARG A 5   ? 0.6868 0.2649 0.2186 -0.0585 0.173  -0.0246 5   ARG A CB    
40    C  CG    . ARG A 5   ? 0.7341 0.304  0.2579 -0.0576 0.1733 -0.0244 5   ARG A CG    
41    C  CD    . ARG A 5   ? 0.7788 0.3425 0.2982 -0.0587 0.1702 -0.025  5   ARG A CD    
42    N  NE    . ARG A 5   ? 0.8145 0.3693 0.325  -0.0579 0.1706 -0.025  5   ARG A NE    
43    C  CZ    . ARG A 5   ? 0.8448 0.3931 0.3495 -0.0583 0.1688 -0.0253 5   ARG A CZ    
44    N  NH1   . ARG A 5   ? 0.8442 0.3942 0.3514 -0.0593 0.1663 -0.0257 5   ARG A NH1   
45    N  NH2   . ARG A 5   ? 0.85   0.3896 0.3459 -0.0574 0.1695 -0.0252 5   ARG A NH2   
46    N  N     . ILE A 6   ? 0.663  0.2573 0.2049 -0.0581 0.1785 -0.0234 6   ILE A N     
47    C  CA    . ILE A 6   ? 0.6636 0.2638 0.2098 -0.0593 0.1791 -0.0235 6   ILE A CA    
48    C  C     . ILE A 6   ? 0.6652 0.2627 0.2084 -0.06   0.179  -0.0238 6   ILE A C     
49    O  O     . ILE A 6   ? 0.6649 0.2616 0.2049 -0.0595 0.1809 -0.0231 6   ILE A O     
50    C  CB    . ILE A 6   ? 0.6679 0.2746 0.2167 -0.0589 0.1818 -0.0224 6   ILE A CB    
51    C  CG1   . ILE A 6   ? 0.6766 0.2852 0.2274 -0.0576 0.1824 -0.0219 6   ILE A CG1   
52    C  CG2   . ILE A 6   ? 0.6718 0.2838 0.2243 -0.0607 0.1821 -0.0225 6   ILE A CG2   
53    C  CD1   . ILE A 6   ? 0.6925 0.3024 0.2474 -0.0584 0.1805 -0.0227 6   ILE A CD1   
54    N  N     . HIS A 7   ? 0.6654 0.2611 0.2092 -0.0609 0.177  -0.0246 7   HIS A N     
55    C  CA    . HIS A 7   ? 0.6748 0.2674 0.2154 -0.0615 0.177  -0.0249 7   HIS A CA    
56    C  C     . HIS A 7   ? 0.6757 0.2729 0.2189 -0.0631 0.1784 -0.0249 7   HIS A C     
57    O  O     . HIS A 7   ? 0.6741 0.274  0.2209 -0.0636 0.1778 -0.0251 7   HIS A O     
58    C  CB    . HIS A 7   ? 0.6878 0.2762 0.2274 -0.0615 0.1742 -0.0255 7   HIS A CB    
59    C  CG    . HIS A 7   ? 0.7152 0.2991 0.2521 -0.0607 0.1723 -0.0255 7   HIS A CG    
60    N  ND1   . HIS A 7   ? 0.7407 0.3184 0.2716 -0.0602 0.1718 -0.0256 7   HIS A ND1   
61    C  CD2   . HIS A 7   ? 0.7267 0.3109 0.2654 -0.0606 0.1708 -0.0254 7   HIS A CD2   
62    C  CE1   . HIS A 7   ? 0.7478 0.3221 0.2768 -0.0599 0.1699 -0.0256 7   HIS A CE1   
63    N  NE2   . HIS A 7   ? 0.7434 0.3214 0.277  -0.0603 0.1692 -0.0255 7   HIS A NE2   
64    N  N     . GLY A 8   ? 0.6759 0.2738 0.217  -0.0639 0.1803 -0.0245 8   GLY A N     
65    C  CA    . GLY A 8   ? 0.6815 0.2833 0.2242 -0.066  0.1815 -0.0245 8   GLY A CA    
66    C  C     . GLY A 8   ? 0.6878 0.2865 0.2265 -0.0673 0.1824 -0.0247 8   GLY A C     
67    O  O     . GLY A 8   ? 0.6951 0.2889 0.2299 -0.0663 0.1822 -0.0248 8   GLY A O     
68    N  N     . ASP A 9   ? 0.6835 0.2843 0.2224 -0.0698 0.1833 -0.0248 9   ASP A N     
69    C  CA    . ASP A 9   ? 0.6883 0.286  0.2229 -0.0715 0.1844 -0.025  9   ASP A CA    
70    C  C     . ASP A 9   ? 0.6827 0.2825 0.2162 -0.0717 0.1861 -0.0238 9   ASP A C     
71    O  O     . ASP A 9   ? 0.684  0.2794 0.2134 -0.0715 0.1868 -0.0238 9   ASP A O     
72    C  CB    . ASP A 9   ? 0.7118 0.3112 0.2463 -0.0746 0.1852 -0.0253 9   ASP A CB    
73    C  CG    . ASP A 9   ? 0.7706 0.3675 0.3054 -0.0745 0.1842 -0.0262 9   ASP A CG    
74    O  OD1   . ASP A 9   ? 0.7824 0.3739 0.3152 -0.0726 0.1832 -0.0267 9   ASP A OD1   
75    O  OD2   . ASP A 9   ? 0.7956 0.396  0.3324 -0.0761 0.1844 -0.0262 9   ASP A OD2   
76    N  N     . ASN A 10  ? 0.6756 0.2822 0.2126 -0.0717 0.1871 -0.0225 10  ASN A N     
77    C  CA    . ASN A 10  ? 0.6795 0.2896 0.2164 -0.0714 0.189  -0.0207 10  ASN A CA    
78    C  C     . ASN A 10  ? 0.6808 0.2968 0.2216 -0.0695 0.1896 -0.0194 10  ASN A C     
79    O  O     . ASN A 10  ? 0.6817 0.2988 0.2252 -0.0688 0.1884 -0.0201 10  ASN A O     
80    C  CB    . ASN A 10  ? 0.6916 0.3054 0.228  -0.0749 0.1905 -0.0199 10  ASN A CB    
81    C  CG    . ASN A 10  ? 0.7265 0.3445 0.2654 -0.0781 0.1899 -0.0203 10  ASN A CG    
82    O  OD1   . ASN A 10  ? 0.7381 0.3519 0.2742 -0.0803 0.1893 -0.0217 10  ASN A OD1   
83    N  ND2   . ASN A 10  ? 0.7336 0.3593 0.2769 -0.0783 0.1902 -0.0191 10  ASN A ND2   
84    N  N     . ILE A 11  ? 0.6796 0.2994 0.2205 -0.0684 0.1918 -0.0173 11  ILE A N     
85    C  CA    . ILE A 11  ? 0.6861 0.3111 0.23   -0.0661 0.1928 -0.0157 11  ILE A CA    
86    C  C     . ILE A 11  ? 0.6908 0.3237 0.2398 -0.0678 0.1925 -0.0153 11  ILE A C     
87    O  O     . ILE A 11  ? 0.6966 0.3313 0.2479 -0.0659 0.1923 -0.0152 11  ILE A O     
88    C  CB    . ILE A 11  ? 0.6942 0.3219 0.237  -0.0643 0.1956 -0.013  11  ILE A CB    
89    C  CG1   . ILE A 11  ? 0.707  0.3372 0.251  -0.0608 0.197  -0.0114 11  ILE A CG1   
90    C  CG2   . ILE A 11  ? 0.6973 0.3327 0.2423 -0.0672 0.1971 -0.0111 11  ILE A CG2   
91    C  CD1   . ILE A 11  ? 0.729  0.3514 0.2704 -0.0584 0.1956 -0.0131 11  ILE A CD1   
92    N  N     . ILE A 12  ? 0.6846 0.3214 0.2348 -0.0715 0.1923 -0.0153 12  ILE A N     
93    C  CA    . ILE A 12  ? 0.6818 0.3256 0.236  -0.0736 0.1919 -0.015  12  ILE A CA    
94    C  C     . ILE A 12  ? 0.6855 0.3258 0.2407 -0.073  0.1899 -0.0171 12  ILE A C     
95    O  O     . ILE A 12  ? 0.6844 0.3293 0.2431 -0.072  0.1899 -0.0166 12  ILE A O     
96    C  CB    . ILE A 12  ? 0.6851 0.3327 0.2391 -0.0782 0.192  -0.0145 12  ILE A CB    
97    C  CG1   . ILE A 12  ? 0.6923 0.3494 0.2489 -0.0788 0.1939 -0.0112 12  ILE A CG1   
98    C  CG2   . ILE A 12  ? 0.6915 0.3399 0.2463 -0.0814 0.1905 -0.0159 12  ILE A CG2   
99    C  CD1   . ILE A 12  ? 0.7048 0.371  0.2663 -0.0782 0.1942 -0.0095 12  ILE A CD1   
100   N  N     . GLU A 13  ? 0.6872 0.3197 0.2395 -0.0732 0.1885 -0.0191 13  GLU A N     
101   C  CA    . GLU A 13  ? 0.6912 0.3207 0.2447 -0.0724 0.1868 -0.0208 13  GLU A CA    
102   C  C     . GLU A 13  ? 0.6945 0.3236 0.2497 -0.069  0.1866 -0.0206 13  GLU A C     
103   O  O     . GLU A 13  ? 0.6932 0.3247 0.2515 -0.0684 0.186  -0.0208 13  GLU A O     
104   C  CB    . GLU A 13  ? 0.7162 0.3378 0.2662 -0.0729 0.1856 -0.0225 13  GLU A CB    
105   C  CG    . GLU A 13  ? 0.764  0.3836 0.3104 -0.0759 0.1862 -0.0227 13  GLU A CG    
106   C  CD    . GLU A 13  ? 0.8088 0.4305 0.3552 -0.0793 0.1863 -0.023  13  GLU A CD    
107   O  OE1   . GLU A 13  ? 0.814  0.4354 0.3621 -0.0788 0.1855 -0.0237 13  GLU A OE1   
108   O  OE2   . GLU A 13  ? 0.82   0.4432 0.3643 -0.0824 0.1872 -0.0226 13  GLU A OE2   
109   N  N     . CYS A 14  ? 0.697  0.3228 0.2497 -0.0669 0.1871 -0.0201 14  CYS A N     
110   C  CA    . CYS A 14  ? 0.7044 0.3284 0.2572 -0.0639 0.187  -0.0199 14  CYS A CA    
111   C  C     . CYS A 14  ? 0.705  0.3361 0.2613 -0.0628 0.1886 -0.0183 14  CYS A C     
112   O  O     . CYS A 14  ? 0.7055 0.337  0.2638 -0.0616 0.188  -0.0186 14  CYS A O     
113   C  CB    . CYS A 14  ? 0.7153 0.3337 0.2635 -0.062  0.1876 -0.0195 14  CYS A CB    
114   S  SG    . CYS A 14  ? 0.7565 0.3665 0.3002 -0.0629 0.1858 -0.0211 14  CYS A SG    
115   N  N     . GLU A 15  ? 0.7041 0.3411 0.2611 -0.0634 0.1905 -0.0164 15  GLU A N     
116   C  CA    . GLU A 15  ? 0.7073 0.352  0.2675 -0.0622 0.1922 -0.0144 15  GLU A CA    
117   C  C     . GLU A 15  ? 0.7026 0.3523 0.267  -0.0638 0.1913 -0.0149 15  GLU A C     
118   O  O     . GLU A 15  ? 0.7045 0.3583 0.2713 -0.0619 0.1921 -0.0139 15  GLU A O     
119   C  CB    . GLU A 15  ? 0.7414 0.3923 0.3019 -0.0627 0.1944 -0.0118 15  GLU A CB    
120   C  CG    . GLU A 15  ? 0.8134 0.4601 0.3698 -0.0598 0.1963 -0.0106 15  GLU A CG    
121   C  CD    . GLU A 15  ? 0.9072 0.5523 0.4625 -0.0557 0.1979 -0.0095 15  GLU A CD    
122   O  OE1   . GLU A 15  ? 0.9037 0.5534 0.4623 -0.0548 0.1981 -0.0091 15  GLU A OE1   
123   O  OE2   . GLU A 15  ? 0.9582 0.597  0.5088 -0.0532 0.1991 -0.0091 15  GLU A OE2   
124   N  N     . ARG A 16  ? 0.6961 0.3447 0.2607 -0.0668 0.1896 -0.0164 16  ARG A N     
125   C  CA    . ARG A 16  ? 0.69   0.3423 0.2577 -0.0683 0.1888 -0.017  16  ARG A CA    
126   C  C     . ARG A 16  ? 0.6829 0.3323 0.2521 -0.0658 0.188  -0.018  16  ARG A C     
127   O  O     . ARG A 16  ? 0.6797 0.3335 0.2519 -0.0654 0.1883 -0.0176 16  ARG A O     
128   C  CB    . ARG A 16  ? 0.7069 0.3569 0.2731 -0.0718 0.1876 -0.0184 16  ARG A CB    
129   C  CG    . ARG A 16  ? 0.7472 0.4019 0.3126 -0.0751 0.1883 -0.0171 16  ARG A CG    
130   C  CD    . ARG A 16  ? 0.7934 0.4491 0.3583 -0.0789 0.1875 -0.0179 16  ARG A CD    
131   N  NE    . ARG A 16  ? 0.8315 0.4792 0.3924 -0.0805 0.1866 -0.0198 16  ARG A NE    
132   C  CZ    . ARG A 16  ? 0.856  0.5019 0.4133 -0.0839 0.1868 -0.0199 16  ARG A CZ    
133   N  NH1   . ARG A 16  ? 0.8458 0.4981 0.4036 -0.0864 0.1876 -0.0182 16  ARG A NH1   
134   N  NH2   . ARG A 16  ? 0.8578 0.4956 0.4109 -0.0847 0.1863 -0.0216 16  ARG A NH2   
135   N  N     . VAL A 17  ? 0.6803 0.3226 0.2474 -0.0643 0.1871 -0.0191 17  VAL A N     
136   C  CA    . VAL A 17  ? 0.6829 0.3224 0.2513 -0.0624 0.1862 -0.0199 17  VAL A CA    
137   C  C     . VAL A 17  ? 0.6821 0.3241 0.251  -0.0597 0.1879 -0.0185 17  VAL A C     
138   O  O     . VAL A 17  ? 0.6798 0.3236 0.2513 -0.0586 0.188  -0.0185 17  VAL A O     
139   C  CB    . VAL A 17  ? 0.6961 0.3278 0.2618 -0.062  0.1845 -0.0212 17  VAL A CB    
140   C  CG1   . VAL A 17  ? 0.7055 0.3343 0.2719 -0.0601 0.1837 -0.0216 17  VAL A CG1   
141   C  CG2   . VAL A 17  ? 0.7017 0.3312 0.2673 -0.064  0.1831 -0.0224 17  VAL A CG2   
142   N  N     . ILE A 18  ? 0.6822 0.3242 0.2485 -0.0585 0.1896 -0.0172 18  ILE A N     
143   C  CA    . ILE A 18  ? 0.6872 0.3311 0.253  -0.0555 0.1918 -0.0154 18  ILE A CA    
144   C  C     . ILE A 18  ? 0.6863 0.3392 0.2563 -0.0554 0.1931 -0.0139 18  ILE A C     
145   O  O     . ILE A 18  ? 0.6805 0.3346 0.2516 -0.0533 0.194  -0.0134 18  ILE A O     
146   C  CB    . ILE A 18  ? 0.6939 0.3359 0.2557 -0.054  0.1936 -0.014  18  ILE A CB    
147   C  CG1   . ILE A 18  ? 0.7101 0.3425 0.2672 -0.0541 0.1921 -0.0155 18  ILE A CG1   
148   C  CG2   . ILE A 18  ? 0.6986 0.3421 0.2591 -0.0505 0.1965 -0.0118 18  ILE A CG2   
149   C  CD1   . ILE A 18  ? 0.7275 0.3532 0.2827 -0.0529 0.1909 -0.0168 18  ILE A CD1   
150   N  N     . ASP A 19  ? 0.6906 0.3495 0.2626 -0.058  0.1929 -0.0133 19  ASP A N     
151   C  CA    . ASP A 19  ? 0.7015 0.3695 0.2773 -0.0586 0.1938 -0.0118 19  ASP A CA    
152   C  C     . ASP A 19  ? 0.7079 0.3762 0.2864 -0.0587 0.1926 -0.0131 19  ASP A C     
153   O  O     . ASP A 19  ? 0.7072 0.381  0.2881 -0.0573 0.1937 -0.0118 19  ASP A O     
154   C  CB    . ASP A 19  ? 0.7291 0.4028 0.3058 -0.0622 0.1934 -0.011  19  ASP A CB    
155   C  CG    . ASP A 19  ? 0.8013 0.4766 0.3761 -0.0619 0.195  -0.009  19  ASP A CG    
156   O  OD1   . ASP A 19  ? 0.8126 0.4861 0.3858 -0.0583 0.1969 -0.0077 19  ASP A OD1   
157   O  OD2   . ASP A 19  ? 0.8326 0.5105 0.4073 -0.0652 0.1946 -0.0087 19  ASP A OD2   
158   N  N     . LEU A 20  ? 0.7105 0.3727 0.2885 -0.0601 0.1905 -0.0155 20  LEU A N     
159   C  CA    . LEU A 20  ? 0.7146 0.3762 0.295  -0.0599 0.1896 -0.0167 20  LEU A CA    
160   C  C     . LEU A 20  ? 0.7261 0.3857 0.3067 -0.0566 0.1905 -0.0164 20  LEU A C     
161   O  O     . LEU A 20  ? 0.7286 0.3918 0.3116 -0.0555 0.1912 -0.0159 20  LEU A O     
162   C  CB    . LEU A 20  ? 0.7178 0.3729 0.2971 -0.0615 0.1875 -0.0188 20  LEU A CB    
163   C  CG    . LEU A 20  ? 0.7414 0.3973 0.3202 -0.0648 0.1867 -0.0193 20  LEU A CG    
164   C  CD1   . LEU A 20  ? 0.7504 0.3992 0.3274 -0.0655 0.1851 -0.021  20  LEU A CD1   
165   C  CD2   . LEU A 20  ? 0.7518 0.4126 0.3329 -0.0658 0.1868 -0.0191 20  LEU A CD2   
166   N  N     . ILE A 21  ? 0.7309 0.3844 0.3083 -0.0551 0.1906 -0.0167 21  ILE A N     
167   C  CA    . ILE A 21  ? 0.7364 0.3864 0.3126 -0.0524 0.1915 -0.0165 21  ILE A CA    
168   C  C     . ILE A 21  ? 0.7366 0.3919 0.3129 -0.0498 0.1944 -0.0142 21  ILE A C     
169   O  O     . ILE A 21  ? 0.7363 0.393  0.3142 -0.0482 0.1953 -0.014  21  ILE A O     
170   C  CB    . ILE A 21  ? 0.747  0.3888 0.3185 -0.0519 0.1909 -0.0171 21  ILE A CB    
171   C  CG1   . ILE A 21  ? 0.7621 0.3989 0.3339 -0.054  0.188  -0.0191 21  ILE A CG1   
172   C  CG2   . ILE A 21  ? 0.7539 0.3914 0.3222 -0.0492 0.1924 -0.0166 21  ILE A CG2   
173   C  CD1   . ILE A 21  ? 0.7815 0.4115 0.3488 -0.0541 0.187  -0.0196 21  ILE A CD1   
174   N  N     . LEU A 22  ? 0.7357 0.3947 0.3109 -0.0494 0.1959 -0.0124 22  LEU A N     
175   C  CA    . LEU A 22  ? 0.742  0.4071 0.3174 -0.0467 0.1989 -0.0097 22  LEU A CA    
176   C  C     . LEU A 22  ? 0.7445 0.4184 0.3246 -0.0471 0.1992 -0.0087 22  LEU A C     
177   O  O     . LEU A 22  ? 0.7457 0.4242 0.3263 -0.0442 0.2016 -0.0065 22  LEU A O     
178   C  CB    . LEU A 22  ? 0.7466 0.4146 0.3205 -0.0469 0.2002 -0.0078 22  LEU A CB    
179   C  CG    . LEU A 22  ? 0.7725 0.4344 0.3411 -0.044  0.2022 -0.0067 22  LEU A CG    
180   C  CD1   . LEU A 22  ? 0.7811 0.4457 0.3486 -0.0397 0.2057 -0.004  22  LEU A CD1   
181   C  CD2   . LEU A 22  ? 0.7864 0.4371 0.3508 -0.0442 0.2005 -0.0093 22  LEU A CD2   
182   N  N     . SER A 23  ? 0.7449 0.4209 0.3278 -0.0504 0.1969 -0.0102 23  SER A N     
183   C  CA    . SER A 23  ? 0.7497 0.4331 0.3363 -0.0511 0.1969 -0.0095 23  SER A CA    
184   C  C     . SER A 23  ? 0.7521 0.4338 0.3398 -0.0487 0.1974 -0.0101 23  SER A C     
185   O  O     . SER A 23  ? 0.7521 0.4402 0.3422 -0.0478 0.1983 -0.0088 23  SER A O     
186   C  CB    . SER A 23  ? 0.7698 0.4541 0.3577 -0.0553 0.1944 -0.011  23  SER A CB    
187   O  OG    . SER A 23  ? 0.803  0.4805 0.3908 -0.056  0.1927 -0.0135 23  SER A OG    
188   N  N     . LYS A 24  ? 0.7529 0.4262 0.3388 -0.0479 0.1968 -0.0118 24  LYS A N     
189   C  CA    . LYS A 24  ? 0.7583 0.4293 0.345  -0.0459 0.1973 -0.0124 24  LYS A CA    
190   C  C     . LYS A 24  ? 0.7679 0.4342 0.3509 -0.0426 0.1995 -0.0116 24  LYS A C     
191   O  O     . LYS A 24  ? 0.7709 0.4378 0.3539 -0.04   0.2014 -0.0108 24  LYS A O     
192   C  CB    . LYS A 24  ? 0.7754 0.4411 0.3633 -0.0479 0.1948 -0.0149 24  LYS A CB    
193   C  CG    . LYS A 24  ? 0.8154 0.4841 0.4068 -0.048  0.1946 -0.0153 24  LYS A CG    
194   C  CD    . LYS A 24  ? 0.8685 0.5363 0.4599 -0.0449 0.1965 -0.0147 24  LYS A CD    
195   C  CE    . LYS A 24  ? 0.9073 0.5767 0.5019 -0.0448 0.1963 -0.0152 24  LYS A CE    
196   N  NZ    . LYS A 24  ? 0.9285 0.5946 0.5226 -0.0422 0.1978 -0.0152 24  LYS A NZ    
197   N  N     . ILE A 25  ? 0.7698 0.4306 0.3489 -0.0425 0.1995 -0.0117 25  ILE A N     
198   C  CA    . ILE A 25  ? 0.78   0.4348 0.354  -0.0396 0.2017 -0.0109 25  ILE A CA    
199   C  C     . ILE A 25  ? 0.7847 0.4454 0.3577 -0.0367 0.2049 -0.0079 25  ILE A C     
200   O  O     . ILE A 25  ? 0.787  0.4525 0.361  -0.0378 0.2048 -0.0068 25  ILE A O     
201   C  CB    . ILE A 25  ? 0.7918 0.4382 0.3615 -0.0408 0.2002 -0.0122 25  ILE A CB    
202   C  CG1   . ILE A 25  ? 0.8041 0.4453 0.375  -0.0435 0.1969 -0.0148 25  ILE A CG1   
203   C  CG2   . ILE A 25  ? 0.8041 0.4437 0.367  -0.0379 0.2027 -0.0111 25  ILE A CG2   
204   C  CD1   . ILE A 25  ? 0.8219 0.4585 0.3919 -0.0427 0.197  -0.0155 25  ILE A CD1   
205   N  N     . ASN A 26  ? 0.7846 0.4447 0.3555 -0.033  0.2079 -0.0063 26  ASN A N     
206   C  CA    . ASN A 26  ? 0.7869 0.4523 0.3564 -0.0295 0.2115 -0.0029 26  ASN A CA    
207   C  C     . ASN A 26  ? 0.7863 0.4416 0.348  -0.0268 0.2137 -0.0025 26  ASN A C     
208   O  O     . ASN A 26  ? 0.7933 0.4426 0.3513 -0.0245 0.2154 -0.0027 26  ASN A O     
209   C  CB    . ASN A 26  ? 0.8032 0.4753 0.3752 -0.0268 0.2137 -0.0011 26  ASN A CB    
210   C  CG    . ASN A 26  ? 0.8421 0.5248 0.4161 -0.0245 0.2162 0.0027  26  ASN A CG    
211   O  OD1   . ASN A 26  ? 0.8596 0.5427 0.431  -0.023  0.2181 0.0048  26  ASN A OD1   
212   N  ND2   . ASN A 26  ? 0.8427 0.5347 0.4215 -0.0243 0.2163 0.0039  26  ASN A ND2   
213   N  N     . PRO A 27  ? 0.777  0.4289 0.3355 -0.0274 0.2135 -0.0023 27  PRO A N     
214   C  CA    . PRO A 27  ? 0.7788 0.4194 0.3289 -0.0252 0.2153 -0.0023 27  PRO A CA    
215   C  C     . PRO A 27  ? 0.7762 0.4167 0.3215 -0.0199 0.2204 0.0012  27  PRO A C     
216   O  O     . PRO A 27  ? 0.7747 0.425  0.3232 -0.0179 0.2226 0.0043  27  PRO A O     
217   C  CB    . PRO A 27  ? 0.7896 0.4273 0.3382 -0.0276 0.2134 -0.0032 27  PRO A CB    
218   C  CG    . PRO A 27  ? 0.79   0.4369 0.3462 -0.0313 0.2105 -0.0039 27  PRO A CG    
219   C  CD    . PRO A 27  ? 0.7659 0.4231 0.3276 -0.0303 0.2117 -0.0023 27  PRO A CD    
220   N  N     . GLN A 28  ? 0.7727 0.4018 0.31   -0.0177 0.2223 0.0008  28  GLN A N     
221   C  CA    . GLN A 28  ? 0.7708 0.3968 0.3015 -0.0122 0.2275 0.004   28  GLN A CA    
222   C  C     . GLN A 28  ? 0.7647 0.3881 0.2908 -0.0106 0.2293 0.0059  28  GLN A C     
223   O  O     . GLN A 28  ? 0.7678 0.3973 0.2937 -0.0066 0.2332 0.0098  28  GLN A O     
224   C  CB    . GLN A 28  ? 0.7999 0.4126 0.3224 -0.0111 0.2286 0.0025  28  GLN A CB    
225   C  CG    . GLN A 28  ? 0.8471 0.4608 0.374  -0.0134 0.2263 0.0001  28  GLN A CG    
226   C  CD    . GLN A 28  ? 0.9035 0.5281 0.4359 -0.0106 0.2286 0.0025  28  GLN A CD    
227   O  OE1   . GLN A 28  ? 0.9255 0.5489 0.4534 -0.0057 0.2332 0.0051  28  GLN A OE1   
228   N  NE2   . GLN A 28  ? 0.9021 0.5373 0.444  -0.0134 0.2256 0.0016  28  GLN A NE2   
229   N  N     . LYS A 29  ? 0.7542 0.369  0.2766 -0.0137 0.2265 0.0034  29  LYS A N     
230   C  CA    . LYS A 29  ? 0.7461 0.3569 0.2634 -0.0124 0.228  0.0048  29  LYS A CA    
231   C  C     . LYS A 29  ? 0.7362 0.349  0.2578 -0.0172 0.2235 0.0025  29  LYS A C     
232   O  O     . LYS A 29  ? 0.7394 0.3478 0.262  -0.0212 0.2194 -0.001  29  LYS A O     
233   C  CB    . LYS A 29  ? 0.7643 0.3586 0.2691 -0.0105 0.2298 0.0042  29  LYS A CB    
234   C  CG    . LYS A 29  ? 0.7971 0.3874 0.2955 -0.005  0.2352 0.0068  29  LYS A CG    
235   C  CD    . LYS A 29  ? 0.8406 0.4136 0.3271 -0.0048 0.2358 0.005   29  LYS A CD    
236   C  CE    . LYS A 29  ? 0.8759 0.4372 0.3514 -0.0028 0.238  0.006   29  LYS A CE    
237   N  NZ    . LYS A 29  ? 0.9031 0.447  0.3664 -0.0033 0.2383 0.004   29  LYS A NZ    
238   N  N     . VAL A 30  ? 0.7229 0.3426 0.2471 -0.0169 0.2244 0.0046  30  VAL A N     
239   C  CA    . VAL A 30  ? 0.7197 0.3409 0.2472 -0.0212 0.2207 0.0026  30  VAL A CA    
240   C  C     . VAL A 30  ? 0.7204 0.3365 0.2419 -0.0194 0.2228 0.0042  30  VAL A C     
241   O  O     . VAL A 30  ? 0.7196 0.34   0.2401 -0.0155 0.2269 0.008   30  VAL A O     
242   C  CB    . VAL A 30  ? 0.7188 0.3543 0.2566 -0.024  0.2189 0.0031  30  VAL A CB    
243   C  CG1   . VAL A 30  ? 0.7245 0.3607 0.2644 -0.0279 0.2159 0.0015  30  VAL A CG1   
244   C  CG2   . VAL A 30  ? 0.7209 0.36   0.2641 -0.0261 0.2164 0.001   30  VAL A CG2   
245   N  N     . LYS A 31  ? 0.7192 0.3262 0.2366 -0.022  0.22   0.0016  31  LYS A N     
246   C  CA    . LYS A 31  ? 0.7239 0.3254 0.2355 -0.0207 0.2215 0.0027  31  LYS A CA    
247   C  C     . LYS A 31  ? 0.7232 0.3268 0.2388 -0.0252 0.2176 0.0005  31  LYS A C     
248   O  O     . LYS A 31  ? 0.7231 0.3252 0.2413 -0.0289 0.2134 -0.0028 31  LYS A O     
249   C  CB    . LYS A 31  ? 0.751  0.3363 0.2508 -0.0189 0.2224 0.0017  31  LYS A CB    
250   C  CG    . LYS A 31  ? 0.7992 0.3773 0.2919 -0.0174 0.224  0.0027  31  LYS A CG    
251   C  CD    . LYS A 31  ? 0.8611 0.4222 0.3413 -0.0164 0.2243 0.0013  31  LYS A CD    
252   C  CE    . LYS A 31  ? 0.91   0.4651 0.3815 -0.0106 0.2302 0.0047  31  LYS A CE    
253   N  NZ    . LYS A 31  ? 0.9468 0.484  0.4048 -0.0099 0.2305 0.0033  31  LYS A NZ    
254   N  N     . ARG A 32  ? 0.7186 0.3261 0.2349 -0.0247 0.219  0.0024  32  ARG A N     
255   C  CA    . ARG A 32  ? 0.7198 0.3284 0.2389 -0.0287 0.2158 0.0005  32  ARG A CA    
256   C  C     . ARG A 32  ? 0.7249 0.325  0.2364 -0.0271 0.2173 0.0012  32  ARG A C     
257   O  O     . ARG A 32  ? 0.7278 0.3242 0.2335 -0.0228 0.2215 0.004   32  ARG A O     
258   C  CB    . ARG A 32  ? 0.7292 0.352  0.2575 -0.0308 0.2156 0.002   32  ARG A CB    
259   C  CG    . ARG A 32  ? 0.7572 0.3871 0.2929 -0.034  0.2126 0.0002  32  ARG A CG    
260   C  CD    . ARG A 32  ? 0.7817 0.4244 0.3247 -0.0362 0.2126 0.0019  32  ARG A CD    
261   N  NE    . ARG A 32  ? 0.813  0.4621 0.3624 -0.0394 0.2099 0.0002  32  ARG A NE    
262   C  CZ    . ARG A 32  ? 0.842  0.4897 0.3935 -0.0436 0.2062 -0.0028 32  ARG A CZ    
263   N  NH1   . ARG A 32  ? 0.8504 0.4908 0.3983 -0.045  0.2047 -0.0046 32  ARG A NH1   
264   N  NH2   . ARG A 32  ? 0.8319 0.4852 0.3887 -0.046  0.2042 -0.004  32  ARG A NH2   
265   N  N     . GLY A 33  ? 0.723  0.3197 0.2343 -0.0304 0.2142 -0.0012 33  GLY A N     
266   C  CA    . GLY A 33  ? 0.7296 0.318  0.2338 -0.0292 0.2153 -0.0008 33  GLY A CA    
267   C  C     . GLY A 33  ? 0.7289 0.3129 0.2329 -0.0331 0.211  -0.004  33  GLY A C     
268   O  O     . GLY A 33  ? 0.7261 0.3167 0.2371 -0.0367 0.2081 -0.0057 33  GLY A O     
269   N  N     . PHE A 34  ? 0.7299 0.3024 0.2255 -0.0323 0.2108 -0.0049 34  PHE A N     
270   C  CA    . PHE A 34  ? 0.7323 0.3    0.2268 -0.0355 0.207  -0.0077 34  PHE A CA    
271   C  C     . PHE A 34  ? 0.7397 0.294  0.2255 -0.0353 0.2049 -0.0097 34  PHE A C     
272   O  O     . PHE A 34  ? 0.7449 0.2909 0.2224 -0.0322 0.2076 -0.0084 34  PHE A O     
273   C  CB    . PHE A 34  ? 0.7315 0.2988 0.2241 -0.035  0.2087 -0.0064 34  PHE A CB    
274   C  CG    . PHE A 34  ? 0.7334 0.3126 0.2343 -0.0371 0.2091 -0.0054 34  PHE A CG    
275   C  CD1   . PHE A 34  ? 0.7404 0.3221 0.2456 -0.0411 0.2056 -0.0078 34  PHE A CD1   
276   C  CD2   . PHE A 34  ? 0.7399 0.327  0.2433 -0.0351 0.2131 -0.0018 34  PHE A CD2   
277   C  CE1   . PHE A 34  ? 0.7423 0.3336 0.2537 -0.0435 0.206  -0.0069 34  PHE A CE1   
278   C  CE2   . PHE A 34  ? 0.7419 0.3397 0.2524 -0.0377 0.2132 -0.0007 34  PHE A CE2   
279   C  CZ    . PHE A 34  ? 0.7359 0.3353 0.2501 -0.042  0.2096 -0.0034 34  PHE A CZ    
280   N  N     . ILE A 35  ? 0.7392 0.2911 0.2264 -0.0387 0.2003 -0.0127 35  ILE A N     
281   C  CA    . ILE A 35  ? 0.7517 0.2914 0.2307 -0.0393 0.1977 -0.0145 35  ILE A CA    
282   C  C     . ILE A 35  ? 0.7636 0.2962 0.2369 -0.0396 0.1967 -0.0151 35  ILE A C     
283   O  O     . ILE A 35  ? 0.7764 0.2977 0.2407 -0.0392 0.1957 -0.0159 35  ILE A O     
284   C  CB    . ILE A 35  ? 0.7544 0.295  0.2374 -0.0425 0.1932 -0.0169 35  ILE A CB    
285   C  CG1   . ILE A 35  ? 0.7577 0.3049 0.2481 -0.0455 0.1901 -0.0183 35  ILE A CG1   
286   C  CG2   . ILE A 35  ? 0.758  0.3033 0.2449 -0.0419 0.1944 -0.0163 35  ILE A CG2   
287   C  CD1   . ILE A 35  ? 0.7721 0.3165 0.2632 -0.0483 0.1855 -0.0204 35  ILE A CD1   
288   N  N     . SER A 36  ? 0.7575 0.2967 0.2358 -0.0404 0.1971 -0.0148 36  SER A N     
289   C  CA    . SER A 36  ? 0.7653 0.2998 0.2396 -0.0406 0.1968 -0.0151 36  SER A CA    
290   C  C     . SER A 36  ? 0.7594 0.3033 0.2395 -0.0403 0.1996 -0.0133 36  SER A C     
291   O  O     . SER A 36  ? 0.7566 0.3106 0.244  -0.0407 0.2009 -0.0122 36  SER A O     
292   C  CB    . SER A 36  ? 0.7865 0.3192 0.2622 -0.0438 0.1919 -0.0178 36  SER A CB    
293   O  OG    . SER A 36  ? 0.8106 0.3532 0.2955 -0.0461 0.1907 -0.0184 36  SER A OG    
294   N  N     . LEU A 37  ? 0.7559 0.2969 0.233  -0.0401 0.2005 -0.013  37  LEU A N     
295   C  CA    . LEU A 37  ? 0.7564 0.306  0.2385 -0.0404 0.2031 -0.0112 37  LEU A CA    
296   C  C     . LEU A 37  ? 0.7493 0.3093 0.2409 -0.044  0.2011 -0.0123 37  LEU A C     
297   O  O     . LEU A 37  ? 0.7456 0.3152 0.243  -0.0445 0.2032 -0.0104 37  LEU A O     
298   C  CB    . LEU A 37  ? 0.7663 0.3096 0.2429 -0.0399 0.2039 -0.0111 37  LEU A CB    
299   C  CG    . LEU A 37  ? 0.7958 0.3299 0.2631 -0.0359 0.207  -0.0094 37  LEU A CG    
300   C  CD1   . LEU A 37  ? 0.8105 0.3345 0.2703 -0.0357 0.206  -0.0105 37  LEU A CD1   
301   C  CD2   . LEU A 37  ? 0.8015 0.3424 0.271  -0.0333 0.212  -0.0056 37  LEU A CD2   
302   N  N     . SER A 38  ? 0.7447 0.3027 0.2376 -0.0464 0.197  -0.015  38  SER A N     
303   C  CA    . SER A 38  ? 0.7424 0.3085 0.243  -0.0496 0.1952 -0.016  38  SER A CA    
304   C  C     . SER A 38  ? 0.7409 0.3129 0.2471 -0.0502 0.1942 -0.0163 38  SER A C     
305   O  O     . SER A 38  ? 0.7402 0.3197 0.2526 -0.0525 0.1936 -0.0166 38  SER A O     
306   C  CB    . SER A 38  ? 0.7619 0.3231 0.2611 -0.0515 0.1918 -0.0185 38  SER A CB    
307   O  OG    . SER A 38  ? 0.7949 0.3539 0.2916 -0.052  0.1927 -0.0183 38  SER A OG    
308   N  N     . CYS A 39  ? 0.7384 0.306  0.2417 -0.0485 0.1938 -0.0164 39  CYS A N     
309   C  CA    . CYS A 39  ? 0.7327 0.3046 0.2408 -0.0491 0.1925 -0.017  39  CYS A CA    
310   C  C     . CYS A 39  ? 0.7246 0.3006 0.2338 -0.0469 0.1955 -0.0149 39  CYS A C     
311   O  O     . CYS A 39  ? 0.728  0.2976 0.2316 -0.0446 0.1966 -0.0144 39  CYS A O     
312   C  CB    . CYS A 39  ? 0.7467 0.3111 0.2515 -0.0497 0.1891 -0.0189 39  CYS A CB    
313   S  SG    . CYS A 39  ? 0.7931 0.3536 0.2972 -0.052  0.1852 -0.021  39  CYS A SG    
314   N  N     . PRO A 40  ? 0.7127 0.2991 0.2289 -0.0477 0.1967 -0.0138 40  PRO A N     
315   C  CA    . PRO A 40  ? 0.7067 0.2981 0.2248 -0.0455 0.1994 -0.0117 40  PRO A CA    
316   C  C     . PRO A 40  ? 0.7034 0.2933 0.2225 -0.0455 0.1976 -0.0131 40  PRO A C     
317   O  O     . PRO A 40  ? 0.7019 0.2898 0.2226 -0.0478 0.1942 -0.0154 40  PRO A O     
318   C  CB    . PRO A 40  ? 0.7084 0.3117 0.2337 -0.047  0.2006 -0.0103 40  PRO A CB    
319   C  CG    . PRO A 40  ? 0.7153 0.3188 0.2419 -0.0503 0.1986 -0.0117 40  PRO A CG    
320   C  CD    . PRO A 40  ? 0.701  0.2948 0.2233 -0.0508 0.1956 -0.0144 40  PRO A CD    
321   N  N     . PHE A 41  ? 0.7013 0.2922 0.2196 -0.0429 0.2001 -0.0115 41  PHE A N     
322   C  CA    . PHE A 41  ? 0.7066 0.2964 0.2259 -0.0429 0.1988 -0.0125 41  PHE A CA    
323   C  C     . PHE A 41  ? 0.7042 0.3022 0.2277 -0.0411 0.2015 -0.0105 41  PHE A C     
324   O  O     . PHE A 41  ? 0.7062 0.3087 0.2298 -0.0388 0.205  -0.0077 41  PHE A O     
325   C  CB    . PHE A 41  ? 0.7134 0.291  0.2241 -0.0416 0.1984 -0.0133 41  PHE A CB    
326   C  CG    . PHE A 41  ? 0.7255 0.2986 0.2296 -0.0375 0.2025 -0.011  41  PHE A CG    
327   C  CD1   . PHE A 41  ? 0.7334 0.3085 0.238  -0.0355 0.2047 -0.0099 41  PHE A CD1   
328   C  CD2   . PHE A 41  ? 0.7416 0.3075 0.2382 -0.0355 0.2045 -0.0099 41  PHE A CD2   
329   C  CE1   . PHE A 41  ? 0.7454 0.3161 0.2435 -0.0313 0.209  -0.0074 41  PHE A CE1   
330   C  CE2   . PHE A 41  ? 0.753  0.3142 0.2428 -0.0314 0.2088 -0.0075 41  PHE A CE2   
331   C  CZ    . PHE A 41  ? 0.7479 0.3115 0.2384 -0.0292 0.2111 -0.0062 41  PHE A CZ    
332   N  N     . ILE A 42  ? 0.6976 0.2975 0.2246 -0.0419 0.2001 -0.0116 42  ILE A N     
333   C  CA    . ILE A 42  ? 0.6992 0.3053 0.2292 -0.0399 0.2025 -0.0099 42  ILE A CA    
334   C  C     . ILE A 42  ? 0.7084 0.3073 0.2349 -0.0391 0.2018 -0.0111 42  ILE A C     
335   O  O     . ILE A 42  ? 0.7152 0.3114 0.2431 -0.0417 0.1984 -0.0134 42  ILE A O     
336   C  CB    . ILE A 42  ? 0.6991 0.3172 0.238  -0.0417 0.2019 -0.0095 42  ILE A CB    
337   C  CG1   . ILE A 42  ? 0.7076 0.3314 0.2488 -0.0391 0.2045 -0.0076 42  ILE A CG1   
338   C  CG2   . ILE A 42  ? 0.705  0.3233 0.2479 -0.0453 0.1979 -0.0123 42  ILE A CG2   
339   C  CD1   . ILE A 42  ? 0.7155 0.3512 0.2643 -0.0405 0.2045 -0.0066 42  ILE A CD1   
340   N  N     . GLU A 43  ? 0.7054 0.3003 0.2265 -0.0356 0.2052 -0.0093 43  GLU A N     
341   C  CA    . GLU A 43  ? 0.7105 0.2975 0.2268 -0.0348 0.2051 -0.0102 43  GLU A CA    
342   C  C     . GLU A 43  ? 0.7089 0.3029 0.2292 -0.0327 0.2076 -0.0086 43  GLU A C     
343   O  O     . GLU A 43  ? 0.7088 0.3081 0.2295 -0.0296 0.2113 -0.0058 43  GLU A O     
344   C  CB    . GLU A 43  ? 0.7449 0.3203 0.2502 -0.0321 0.2076 -0.0093 43  GLU A CB    
345   C  CG    . GLU A 43  ? 0.804  0.3685 0.3025 -0.0324 0.2068 -0.0107 43  GLU A CG    
346   C  CD    . GLU A 43  ? 0.8729 0.4237 0.3591 -0.0307 0.2083 -0.0104 43  GLU A CD    
347   O  OE1   . GLU A 43  ? 0.8887 0.4377 0.3717 -0.0294 0.2096 -0.0094 43  GLU A OE1   
348   O  OE2   . GLU A 43  ? 0.8942 0.4354 0.3735 -0.0308 0.2083 -0.0112 43  GLU A OE2   
349   N  N     . ILE A 44  ? 0.7064 0.3012 0.2302 -0.0344 0.2055 -0.0103 44  ILE A N     
350   C  CA    . ILE A 44  ? 0.707  0.3082 0.2346 -0.0325 0.2077 -0.009  44  ILE A CA    
351   C  C     . ILE A 44  ? 0.7193 0.3125 0.2422 -0.0318 0.208  -0.0099 44  ILE A C     
352   O  O     . ILE A 44  ? 0.727  0.313  0.2477 -0.0345 0.2049 -0.0122 44  ILE A O     
353   C  CB    . ILE A 44  ? 0.7027 0.3153 0.2404 -0.0349 0.2056 -0.0096 44  ILE A CB    
354   C  CG1   . ILE A 44  ? 0.7095 0.3196 0.25   -0.0386 0.2013 -0.0126 44  ILE A CG1   
355   C  CG2   . ILE A 44  ? 0.7068 0.3275 0.2486 -0.0357 0.2057 -0.0085 44  ILE A CG2   
356   C  CD1   . ILE A 44  ? 0.7156 0.3349 0.2646 -0.0402 0.2    -0.0131 44  ILE A CD1   
357   N  N     . ILE A 45  ? 0.7182 0.3126 0.2393 -0.028  0.212  -0.0078 45  ILE A N     
358   C  CA    . ILE A 45  ? 0.7254 0.3129 0.242  -0.027  0.2131 -0.0083 45  ILE A CA    
359   C  C     . ILE A 45  ? 0.7242 0.3221 0.2487 -0.0262 0.2138 -0.0075 45  ILE A C     
360   O  O     . ILE A 45  ? 0.7218 0.3278 0.2488 -0.0232 0.2169 -0.0049 45  ILE A O     
361   C  CB    . ILE A 45  ? 0.7361 0.3146 0.2421 -0.0226 0.2178 -0.0061 45  ILE A CB    
362   C  CG1   . ILE A 45  ? 0.7535 0.321  0.2508 -0.0233 0.2171 -0.0068 45  ILE A CG1   
363   C  CG2   . ILE A 45  ? 0.7457 0.3172 0.247  -0.0216 0.2193 -0.0066 45  ILE A CG2   
364   C  CD1   . ILE A 45  ? 0.7784 0.3367 0.2647 -0.0188 0.222  -0.0045 45  ILE A CD1   
365   N  N     . PHE A 46  ? 0.7232 0.3217 0.2519 -0.029  0.211  -0.0097 46  PHE A N     
366   C  CA    . PHE A 46  ? 0.7217 0.3294 0.2576 -0.0283 0.2116 -0.0092 46  PHE A CA    
367   C  C     . PHE A 46  ? 0.7327 0.3346 0.2669 -0.0287 0.2114 -0.0104 46  PHE A C     
368   O  O     . PHE A 46  ? 0.7445 0.3359 0.2725 -0.0302 0.2103 -0.0118 46  PHE A O     
369   C  CB    . PHE A 46  ? 0.7115 0.3287 0.2566 -0.0316 0.2082 -0.0102 46  PHE A CB    
370   C  CG    . PHE A 46  ? 0.7189 0.3323 0.2661 -0.0358 0.2038 -0.0131 46  PHE A CG    
371   C  CD1   . PHE A 46  ? 0.7325 0.3409 0.2772 -0.0381 0.2013 -0.0143 46  PHE A CD1   
372   C  CD2   . PHE A 46  ? 0.7253 0.341  0.2775 -0.0372 0.2022 -0.0143 46  PHE A CD2   
373   C  CE1   . PHE A 46  ? 0.7414 0.3474 0.2885 -0.0416 0.1973 -0.0164 46  PHE A CE1   
374   C  CE2   . PHE A 46  ? 0.7339 0.3469 0.2883 -0.0407 0.1984 -0.0163 46  PHE A CE2   
375   C  CZ    . PHE A 46  ? 0.735  0.3435 0.2871 -0.0428 0.196  -0.0173 46  PHE A CZ    
376   N  N     . LYS A 47  ? 0.7275 0.3363 0.2669 -0.0275 0.2125 -0.0099 47  LYS A N     
377   C  CA    . LYS A 47  ? 0.7364 0.3402 0.2746 -0.0279 0.2125 -0.011  47  LYS A CA    
378   C  C     . LYS A 47  ? 0.7373 0.3494 0.2845 -0.0295 0.2106 -0.0118 47  LYS A C     
379   O  O     . LYS A 47  ? 0.7327 0.3549 0.2862 -0.0292 0.2105 -0.011  47  LYS A O     
380   C  CB    . LYS A 47  ? 0.7625 0.3616 0.2937 -0.0234 0.2174 -0.009  47  LYS A CB    
381   C  CG    . LYS A 47  ? 0.8033 0.413  0.3384 -0.0194 0.2208 -0.0063 47  LYS A CG    
382   C  CD    . LYS A 47  ? 0.8515 0.4561 0.3791 -0.0144 0.226  -0.004  47  LYS A CD    
383   C  CE    . LYS A 47  ? 0.8808 0.4966 0.4121 -0.01   0.2295 -0.0007 47  LYS A CE    
384   N  NZ    . LYS A 47  ? 0.8896 0.5173 0.431  -0.0114 0.2275 -0.001  47  LYS A NZ    
385   N  N     . GLU A 48  ? 0.7408 0.3481 0.2882 -0.0314 0.2091 -0.0135 48  GLU A N     
386   C  CA    . GLU A 48  ? 0.7439 0.3572 0.2987 -0.0326 0.2078 -0.0142 48  GLU A CA    
387   C  C     . GLU A 48  ? 0.7534 0.3618 0.3043 -0.0303 0.2107 -0.0137 48  GLU A C     
388   O  O     . GLU A 48  ? 0.7616 0.3628 0.3101 -0.0324 0.2095 -0.015  48  GLU A O     
389   C  CB    . GLU A 48  ? 0.7704 0.382  0.3288 -0.037  0.2033 -0.0163 48  GLU A CB    
390   C  CG    . GLU A 48  ? 0.8208 0.4365 0.3826 -0.039  0.2006 -0.0168 48  GLU A CG    
391   C  CD    . GLU A 48  ? 0.8884 0.5033 0.4541 -0.0428 0.1965 -0.0184 48  GLU A CD    
392   O  OE1   . GLU A 48  ? 0.9094 0.5197 0.4747 -0.0443 0.1954 -0.0191 48  GLU A OE1   
393   O  OE2   . GLU A 48  ? 0.9042 0.523  0.4733 -0.0443 0.1945 -0.0188 48  GLU A OE2   
394   N  N     . GLY A 49  ? 0.7495 0.3616 0.2991 -0.0261 0.2147 -0.0117 49  GLY A N     
395   C  CA    . GLY A 49  ? 0.7531 0.3601 0.2978 -0.0232 0.2183 -0.0109 49  GLY A CA    
396   C  C     . GLY A 49  ? 0.7602 0.3548 0.2939 -0.0223 0.2203 -0.0107 49  GLY A C     
397   O  O     . GLY A 49  ? 0.7617 0.3552 0.2906 -0.0197 0.2226 -0.009  49  GLY A O     
398   N  N     . HIS A 50  ? 0.7628 0.3477 0.2921 -0.0246 0.2194 -0.0123 50  HIS A N     
399   C  CA    . HIS A 50  ? 0.7737 0.345  0.2913 -0.0246 0.2209 -0.0123 50  HIS A CA    
400   C  C     . HIS A 50  ? 0.777  0.3434 0.2926 -0.0287 0.2169 -0.0139 50  HIS A C     
401   O  O     . HIS A 50  ? 0.7863 0.3414 0.2916 -0.0288 0.2179 -0.0139 50  HIS A O     
402   C  CB    . HIS A 50  ? 0.7904 0.3528 0.3032 -0.0257 0.2217 -0.0133 50  HIS A CB    
403   C  CG    . HIS A 50  ? 0.8208 0.384  0.3319 -0.0212 0.2266 -0.0117 50  HIS A CG    
404   N  ND1   . HIS A 50  ? 0.8495 0.4028 0.3492 -0.0174 0.2314 -0.0103 50  HIS A ND1   
405   C  CD2   . HIS A 50  ? 0.8293 0.4011 0.3481 -0.0199 0.2272 -0.0114 50  HIS A CD2   
406   C  CE1   . HIS A 50  ? 0.8539 0.4107 0.355  -0.0138 0.2349 -0.0091 50  HIS A CE1   
407   N  NE2   . HIS A 50  ? 0.8458 0.4138 0.3584 -0.0152 0.2324 -0.0097 50  HIS A NE2   
408   N  N     . ASP A 51  ? 0.7714 0.3453 0.2958 -0.0321 0.2125 -0.0151 51  ASP A N     
409   C  CA    . ASP A 51  ? 0.7822 0.3521 0.3054 -0.036  0.2084 -0.0165 51  ASP A CA    
410   C  C     . ASP A 51  ? 0.7875 0.3604 0.3102 -0.0347 0.2086 -0.0157 51  ASP A C     
411   O  O     . ASP A 51  ? 0.7833 0.3668 0.3141 -0.0344 0.2077 -0.0153 51  ASP A O     
412   C  CB    . ASP A 51  ? 0.8015 0.377  0.3339 -0.0402 0.2038 -0.018  51  ASP A CB    
413   C  CG    . ASP A 51  ? 0.8616 0.4291 0.391  -0.0443 0.2012 -0.0193 51  ASP A CG    
414   O  OD1   . ASP A 51  ? 0.8722 0.4301 0.3934 -0.0462 0.2001 -0.0198 51  ASP A OD1   
415   O  OD2   . ASP A 51  ? 0.8831 0.454  0.4184 -0.0457 0.2002 -0.0197 51  ASP A OD2   
416   N  N     . TYR A 52  ? 0.7954 0.3587 0.3084 -0.0342 0.2096 -0.0154 52  TYR A N     
417   C  CA    . TYR A 52  ? 0.8026 0.368  0.3147 -0.033  0.2098 -0.0145 52  TYR A CA    
418   C  C     . TYR A 52  ? 0.7916 0.3565 0.3062 -0.0374 0.2049 -0.0163 52  TYR A C     
419   O  O     . TYR A 52  ? 0.7922 0.3509 0.3048 -0.0411 0.2017 -0.0179 52  TYR A O     
420   C  CB    . TYR A 52  ? 0.8241 0.3791 0.3241 -0.0297 0.2138 -0.0131 52  TYR A CB    
421   C  CG    . TYR A 52  ? 0.8507 0.4095 0.3493 -0.024  0.2193 -0.0103 52  TYR A CG    
422   C  CD1   . TYR A 52  ? 0.8641 0.4319 0.3665 -0.0211 0.2212 -0.0082 52  TYR A CD1   
423   C  CD2   . TYR A 52  ? 0.8733 0.4268 0.3668 -0.0216 0.2228 -0.0096 52  TYR A CD2   
424   C  CE1   . TYR A 52  ? 0.8791 0.4515 0.3808 -0.0157 0.2263 -0.0052 52  TYR A CE1   
425   C  CE2   . TYR A 52  ? 0.8874 0.4448 0.3797 -0.0159 0.2281 -0.0067 52  TYR A CE2   
426   C  CZ    . TYR A 52  ? 0.897  0.4643 0.3936 -0.013  0.2297 -0.0044 52  TYR A CZ    
427   O  OH    . TYR A 52  ? 0.9186 0.4908 0.4145 -0.0073 0.2348 -0.0011 52  TYR A OH    
428   N  N     . PHE A 53  ? 0.7815 0.3531 0.3002 -0.0371 0.2042 -0.0159 53  PHE A N     
429   C  CA    . PHE A 53  ? 0.7816 0.3534 0.3026 -0.0406 0.1999 -0.0173 53  PHE A CA    
430   C  C     . PHE A 53  ? 0.7748 0.3456 0.2918 -0.0389 0.2012 -0.0163 53  PHE A C     
431   O  O     . PHE A 53  ? 0.7743 0.3506 0.2924 -0.0355 0.2046 -0.0143 53  PHE A O     
432   C  CB    . PHE A 53  ? 0.78   0.3626 0.3122 -0.0426 0.1971 -0.018  53  PHE A CB    
433   C  CG    . PHE A 53  ? 0.7937 0.3775 0.3303 -0.0445 0.1955 -0.0189 53  PHE A CG    
434   C  CD1   . PHE A 53  ? 0.8081 0.3871 0.3444 -0.0482 0.1918 -0.0203 53  PHE A CD1   
435   C  CD2   . PHE A 53  ? 0.8023 0.3921 0.3433 -0.0424 0.1978 -0.0182 53  PHE A CD2   
436   C  CE1   . PHE A 53  ? 0.8154 0.3957 0.3559 -0.0498 0.1907 -0.0208 53  PHE A CE1   
437   C  CE2   . PHE A 53  ? 0.8107 0.4013 0.3557 -0.0439 0.1967 -0.0189 53  PHE A CE2   
438   C  CZ    . PHE A 53  ? 0.81   0.396  0.3549 -0.0476 0.1931 -0.0202 53  PHE A CZ    
439   N  N     . HIS A 54  ? 0.7684 0.3323 0.2809 -0.0412 0.1986 -0.0174 54  HIS A N     
440   C  CA    . HIS A 54  ? 0.7673 0.3289 0.2753 -0.0398 0.1997 -0.0165 54  HIS A CA    
441   C  C     . HIS A 54  ? 0.7603 0.3252 0.2732 -0.043  0.1956 -0.0179 54  HIS A C     
442   O  O     . HIS A 54  ? 0.7659 0.3249 0.2763 -0.0461 0.192  -0.0194 54  HIS A O     
443   C  CB    . HIS A 54  ? 0.7847 0.3322 0.28   -0.0391 0.201  -0.0165 54  HIS A CB    
444   C  CG    . HIS A 54  ? 0.8096 0.3535 0.2988 -0.0365 0.2033 -0.0151 54  HIS A CG    
445   N  ND1   . HIS A 54  ? 0.8399 0.3709 0.3166 -0.0348 0.2056 -0.0145 54  HIS A ND1   
446   C  CD2   . HIS A 54  ? 0.8197 0.371  0.3133 -0.0355 0.2039 -0.0142 54  HIS A CD2   
447   C  CE1   . HIS A 54  ? 0.8477 0.3788 0.3219 -0.0325 0.2076 -0.0132 54  HIS A CE1   
448   N  NE2   . HIS A 54  ? 0.8399 0.3833 0.3243 -0.033  0.2065 -0.0129 54  HIS A NE2   
449   N  N     . TRP A 55  ? 0.7458 0.3202 0.2652 -0.0424 0.196  -0.0172 55  TRP A N     
450   C  CA    . TRP A 55  ? 0.7377 0.3153 0.2614 -0.0451 0.1925 -0.0184 55  TRP A CA    
451   C  C     . TRP A 55  ? 0.733  0.3105 0.254  -0.0439 0.1938 -0.0174 55  TRP A C     
452   O  O     . TRP A 55  ? 0.7358 0.3165 0.256  -0.0409 0.1975 -0.0155 55  TRP A O     
453   C  CB    . TRP A 55  ? 0.7289 0.3176 0.263  -0.0462 0.1914 -0.0186 55  TRP A CB    
454   C  CG    . TRP A 55  ? 0.7334 0.3235 0.272  -0.048  0.1894 -0.0197 55  TRP A CG    
455   C  CD1   . TRP A 55  ? 0.7485 0.3316 0.2838 -0.0495 0.1876 -0.0205 55  TRP A CD1   
456   C  CD2   . TRP A 55  ? 0.7273 0.3263 0.2745 -0.0487 0.1887 -0.0198 55  TRP A CD2   
457   N  NE1   . TRP A 55  ? 0.7488 0.3366 0.2907 -0.0509 0.1862 -0.0211 55  TRP A NE1   
458   C  CE2   . TRP A 55  ? 0.7383 0.3354 0.2873 -0.0502 0.1869 -0.0207 55  TRP A CE2   
459   C  CE3   . TRP A 55  ? 0.7256 0.3335 0.2785 -0.0483 0.1895 -0.0193 55  TRP A CE3   
460   C  CZ2   . TRP A 55  ? 0.74   0.3438 0.2965 -0.0509 0.1861 -0.021  55  TRP A CZ2   
461   C  CZ3   . TRP A 55  ? 0.7303 0.3442 0.29   -0.0492 0.1886 -0.0197 55  TRP A CZ3   
462   C  CH2   . TRP A 55  ? 0.7345 0.3462 0.2959 -0.0503 0.187  -0.0205 55  TRP A CH2   
463   N  N     . ARG A 56  ? 0.7231 0.2979 0.2433 -0.0461 0.1909 -0.0186 56  ARG A N     
464   C  CA    . ARG A 56  ? 0.7168 0.292  0.2352 -0.0453 0.1919 -0.0179 56  ARG A CA    
465   C  C     . ARG A 56  ? 0.7061 0.2861 0.2304 -0.048  0.1887 -0.0191 56  ARG A C     
466   O  O     . ARG A 56  ? 0.7049 0.2825 0.2302 -0.0505 0.1852 -0.0206 56  ARG A O     
467   C  CB    . ARG A 56  ? 0.7373 0.3012 0.2454 -0.0443 0.1925 -0.0178 56  ARG A CB    
468   C  CG    . ARG A 56  ? 0.7748 0.34   0.281  -0.0424 0.195  -0.0163 56  ARG A CG    
469   C  CD    . ARG A 56  ? 0.8181 0.3717 0.3139 -0.0415 0.1954 -0.0163 56  ARG A CD    
470   N  NE    . ARG A 56  ? 0.8502 0.3992 0.3448 -0.0447 0.191  -0.0183 56  ARG A NE    
471   C  CZ    . ARG A 56  ? 0.8843 0.4219 0.37   -0.0454 0.1894 -0.0192 56  ARG A CZ    
472   N  NH1   . ARG A 56  ? 0.8869 0.4155 0.3634 -0.0432 0.1921 -0.0183 56  ARG A NH1   
473   N  NH2   . ARG A 56  ? 0.8884 0.4232 0.3738 -0.0483 0.1852 -0.0208 56  ARG A NH2   
474   N  N     . PHE A 57  ? 0.6962 0.2835 0.2245 -0.0477 0.1901 -0.0183 57  PHE A N     
475   C  CA    . PHE A 57  ? 0.6954 0.2867 0.2284 -0.0501 0.1877 -0.0193 57  PHE A CA    
476   C  C     . PHE A 57  ? 0.7019 0.2902 0.2307 -0.0498 0.1884 -0.0189 57  PHE A C     
477   O  O     . PHE A 57  ? 0.7045 0.296  0.2327 -0.0481 0.1914 -0.0172 57  PHE A O     
478   C  CB    . PHE A 57  ? 0.6878 0.2895 0.2283 -0.0507 0.1886 -0.0187 57  PHE A CB    
479   C  CG    . PHE A 57  ? 0.6912 0.2963 0.2364 -0.051  0.1878 -0.0192 57  PHE A CG    
480   C  CD1   . PHE A 57  ? 0.701  0.3079 0.2461 -0.0488 0.1903 -0.018  57  PHE A CD1   
481   C  CD2   . PHE A 57  ? 0.6951 0.3013 0.2445 -0.0532 0.1849 -0.0206 57  PHE A CD2   
482   C  CE1   . PHE A 57  ? 0.7062 0.3158 0.2554 -0.0491 0.1898 -0.0184 57  PHE A CE1   
483   C  CE2   . PHE A 57  ? 0.7025 0.3116 0.2561 -0.0533 0.1845 -0.0209 57  PHE A CE2   
484   C  CZ    . PHE A 57  ? 0.7008 0.3115 0.2543 -0.0514 0.1869 -0.0199 57  PHE A CZ    
485   N  N     . ASP A 58  ? 0.7023 0.2846 0.228  -0.0513 0.1857 -0.0202 58  ASP A N     
486   C  CA    . ASP A 58  ? 0.7057 0.2844 0.2272 -0.0511 0.1861 -0.02   58  ASP A CA    
487   C  C     . ASP A 58  ? 0.7022 0.2862 0.2288 -0.0531 0.1848 -0.0207 58  ASP A C     
488   O  O     . ASP A 58  ? 0.701  0.2856 0.2306 -0.0549 0.1819 -0.022  58  ASP A O     
489   C  CB    . ASP A 58  ? 0.7313 0.2996 0.2456 -0.0514 0.1839 -0.021  58  ASP A CB    
490   C  CG    . ASP A 58  ? 0.7966 0.3577 0.3041 -0.0496 0.1852 -0.0205 58  ASP A CG    
491   O  OD1   . ASP A 58  ? 0.8048 0.3683 0.3121 -0.0473 0.1887 -0.0189 58  ASP A OD1   
492   O  OD2   . ASP A 58  ? 0.831  0.3838 0.333  -0.0506 0.1828 -0.0215 58  ASP A OD2   
493   N  N     . MET A 59  ? 0.6969 0.285  0.2243 -0.0529 0.187  -0.0196 59  MET A N     
494   C  CA    . MET A 59  ? 0.6941 0.2869 0.2254 -0.055  0.1863 -0.0201 59  MET A CA    
495   C  C     . MET A 59  ? 0.7003 0.2876 0.2274 -0.0556 0.1854 -0.0208 59  MET A C     
496   O  O     . MET A 59  ? 0.7037 0.2868 0.2257 -0.0542 0.1871 -0.02   59  MET A O     
497   C  CB    . MET A 59  ? 0.6903 0.2918 0.2256 -0.0552 0.189  -0.0185 59  MET A CB    
498   C  CG    . MET A 59  ? 0.6981 0.3056 0.2381 -0.0548 0.1895 -0.018  59  MET A CG    
499   S  SD    . MET A 59  ? 0.7226 0.3398 0.2658 -0.0541 0.1929 -0.0153 59  MET A SD    
500   C  CE    . MET A 59  ? 0.7212 0.3358 0.2609 -0.0501 0.1955 -0.0136 59  MET A CE    
501   N  N     . PHE A 60  ? 0.6983 0.2853 0.2272 -0.0575 0.1831 -0.0221 60  PHE A N     
502   C  CA    . PHE A 60  ? 0.7056 0.2875 0.2307 -0.058  0.1822 -0.0228 60  PHE A CA    
503   C  C     . PHE A 60  ? 0.71   0.2961 0.2376 -0.0599 0.1829 -0.0229 60  PHE A C     
504   O  O     . PHE A 60  ? 0.7106 0.2977 0.2408 -0.0613 0.1813 -0.0239 60  PHE A O     
505   C  CB    . PHE A 60  ? 0.7047 0.2817 0.2287 -0.0583 0.1787 -0.0241 60  PHE A CB    
506   C  CG    . PHE A 60  ? 0.7158 0.2863 0.2348 -0.0571 0.1777 -0.0241 60  PHE A CG    
507   C  CD1   . PHE A 60  ? 0.7231 0.2943 0.2429 -0.0564 0.178  -0.0237 60  PHE A CD1   
508   C  CD2   . PHE A 60  ? 0.7292 0.2922 0.2421 -0.0567 0.1764 -0.0245 60  PHE A CD2   
509   C  CE1   . PHE A 60  ? 0.7348 0.2987 0.2487 -0.0556 0.1771 -0.0238 60  PHE A CE1   
510   C  CE2   . PHE A 60  ? 0.7385 0.2946 0.2458 -0.056  0.1753 -0.0246 60  PHE A CE2   
511   C  CZ    . PHE A 60  ? 0.735  0.2913 0.2426 -0.0555 0.1757 -0.0242 60  PHE A CZ    
512   N  N     . PRO A 61  ? 0.711  0.2996 0.2378 -0.0601 0.1855 -0.0218 61  PRO A N     
513   C  CA    . PRO A 61  ? 0.7124 0.3047 0.2411 -0.0625 0.1863 -0.0218 61  PRO A CA    
514   C  C     . PRO A 61  ? 0.7267 0.3132 0.2515 -0.0633 0.1855 -0.0229 61  PRO A C     
515   O  O     . PRO A 61  ? 0.737  0.3183 0.2571 -0.0621 0.1859 -0.0227 61  PRO A O     
516   C  CB    . PRO A 61  ? 0.7177 0.315  0.2468 -0.0625 0.1893 -0.0198 61  PRO A CB    
517   C  CG    . PRO A 61  ? 0.7233 0.3196 0.251  -0.0595 0.1904 -0.0186 61  PRO A CG    
518   C  CD    . PRO A 61  ? 0.7065 0.2946 0.2305 -0.0582 0.1881 -0.0201 61  PRO A CD    
519   N  N     . GLY A 62  ? 0.7295 0.3166 0.2558 -0.0652 0.1845 -0.0238 62  GLY A N     
520   C  CA    . GLY A 62  ? 0.7439 0.3257 0.2665 -0.0658 0.1841 -0.0247 62  GLY A CA    
521   C  C     . GLY A 62  ? 0.7556 0.3325 0.277  -0.0645 0.1815 -0.0257 62  GLY A C     
522   O  O     . GLY A 62  ? 0.7583 0.331  0.2771 -0.0627 0.1803 -0.0257 62  GLY A O     
523   N  N     . PHE A 63  ? 0.7608 0.3381 0.284  -0.0653 0.1806 -0.0263 63  PHE A N     
524   C  CA    . PHE A 63  ? 0.7729 0.3466 0.2956 -0.0639 0.1782 -0.0267 63  PHE A CA    
525   C  C     . PHE A 63  ? 0.7907 0.3578 0.3077 -0.0633 0.1782 -0.027  63  PHE A C     
526   O  O     . PHE A 63  ? 0.7931 0.3586 0.307  -0.0644 0.1802 -0.0271 63  PHE A O     
527   C  CB    . PHE A 63  ? 0.7664 0.3425 0.2924 -0.0645 0.1779 -0.0269 63  PHE A CB    
528   C  CG    . PHE A 63  ? 0.7667 0.3484 0.2982 -0.0647 0.1774 -0.0266 63  PHE A CG    
529   C  CD1   . PHE A 63  ? 0.7724 0.3549 0.3066 -0.0633 0.1753 -0.0264 63  PHE A CD1   
530   C  CD2   . PHE A 63  ? 0.7722 0.3584 0.3061 -0.0664 0.179  -0.0266 63  PHE A CD2   
531   C  CE1   . PHE A 63  ? 0.7734 0.3608 0.3126 -0.0634 0.175  -0.0262 63  PHE A CE1   
532   C  CE2   . PHE A 63  ? 0.7739 0.3651 0.3128 -0.0663 0.1786 -0.0264 63  PHE A CE2   
533   C  CZ    . PHE A 63  ? 0.7672 0.3589 0.3087 -0.0647 0.1768 -0.0262 63  PHE A CZ    
534   N  N     . ASN A 64  ? 0.8005 0.3642 0.3164 -0.0616 0.1759 -0.027  64  ASN A N     
535   C  CA    . ASN A 64  ? 0.8196 0.3773 0.3301 -0.0607 0.1757 -0.0272 64  ASN A CA    
536   C  C     . ASN A 64  ? 0.8352 0.392  0.3453 -0.061  0.1767 -0.0273 64  ASN A C     
537   O  O     . ASN A 64  ? 0.8374 0.3976 0.3514 -0.0612 0.1764 -0.027  64  ASN A O     
538   C  CB    . ASN A 64  ? 0.8331 0.3881 0.3427 -0.059  0.1726 -0.0269 64  ASN A CB    
539   C  CG    . ASN A 64  ? 0.8705 0.4225 0.3768 -0.0585 0.1718 -0.0269 64  ASN A CG    
540   O  OD1   . ASN A 64  ? 0.8831 0.4352 0.3882 -0.0589 0.1739 -0.027  64  ASN A OD1   
541   N  ND2   . ASN A 64  ? 0.8796 0.4286 0.3841 -0.0575 0.1689 -0.0267 64  ASN A ND2   
542   N  N     . LYS A 65  ? 0.8433 0.395  0.348  -0.0609 0.1781 -0.0275 65  LYS A N     
543   C  CA    . LYS A 65  ? 0.8554 0.4045 0.3579 -0.0611 0.1795 -0.0275 65  LYS A CA    
544   C  C     . LYS A 65  ? 0.8734 0.4183 0.3732 -0.0584 0.178  -0.027  65  LYS A C     
545   O  O     . LYS A 65  ? 0.872  0.4165 0.3722 -0.0574 0.1782 -0.0264 65  LYS A O     
546   C  CB    . LYS A 65  ? 0.8731 0.4193 0.371  -0.0631 0.1825 -0.0281 65  LYS A CB    
547   C  CG    . LYS A 65  ? 0.9059 0.4574 0.407  -0.066  0.1839 -0.0282 65  LYS A CG    
548   C  CD    . LYS A 65  ? 0.9517 0.5029 0.4503 -0.0677 0.1857 -0.0282 65  LYS A CD    
549   C  CE    . LYS A 65  ? 0.9842 0.5417 0.4863 -0.0707 0.187  -0.028  65  LYS A CE    
550   N  NZ    . LYS A 65  ? 1.0112 0.5688 0.5108 -0.0728 0.1892 -0.0276 65  LYS A NZ    
551   N  N     . ASN A 66  ? 0.889  0.4308 0.3859 -0.0571 0.1766 -0.0269 66  ASN A N     
552   C  CA    . ASN A 66  ? 0.9093 0.4477 0.4037 -0.0547 0.1747 -0.0262 66  ASN A CA    
553   C  C     . ASN A 66  ? 0.9242 0.4664 0.423  -0.0538 0.171  -0.0254 66  ASN A C     
554   O  O     . ASN A 66  ? 0.9222 0.4689 0.426  -0.0536 0.1701 -0.0246 66  ASN A O     
555   C  CB    . ASN A 66  ? 0.9265 0.4582 0.4139 -0.0539 0.1756 -0.0266 66  ASN A CB    
556   C  CG    . ASN A 66  ? 0.9621 0.49   0.4461 -0.0513 0.1739 -0.0257 66  ASN A CG    
557   O  OD1   . ASN A 66  ? 0.9732 0.5039 0.4603 -0.0499 0.1717 -0.0246 66  ASN A OD1   
558   N  ND2   . ASN A 66  ? 0.9696 0.4914 0.4472 -0.0506 0.175  -0.0261 66  ASN A ND2   
559   N  N     . THR A 67  ? 0.9368 0.477  0.4335 -0.0536 0.169  -0.0256 67  THR A N     
560   C  CA    . THR A 67  ? 0.9528 0.4958 0.4528 -0.0535 0.1653 -0.0249 67  THR A CA    
561   C  C     . THR A 67  ? 0.9579 0.499  0.4558 -0.0544 0.1647 -0.0256 67  THR A C     
562   O  O     . THR A 67  ? 0.9579 0.5024 0.4595 -0.0554 0.1634 -0.0256 67  THR A O     
563   C  CB    . THR A 67  ? 0.9823 0.5242 0.4812 -0.0517 0.1625 -0.0236 67  THR A CB    
564   O  OG1   . THR A 67  ? 1.0012 0.5455 0.5026 -0.0523 0.1587 -0.0229 67  THR A OG1   
565   C  CG2   . THR A 67  ? 0.9939 0.5289 0.4854 -0.0504 0.1629 -0.0238 67  THR A CG2   
566   N  N     . ASN A 68  ? 0.9584 0.4936 0.4499 -0.054  0.1659 -0.0262 68  ASN A N     
567   C  CA    . ASN A 68  ? 0.9638 0.4961 0.4522 -0.0544 0.166  -0.0267 68  ASN A CA    
568   C  C     . ASN A 68  ? 0.9575 0.4869 0.4422 -0.0544 0.1698 -0.0272 68  ASN A C     
569   O  O     . ASN A 68  ? 0.9615 0.4858 0.4408 -0.0538 0.1702 -0.0273 68  ASN A O     
570   C  CB    . ASN A 68  ? 0.9931 0.5199 0.4762 -0.0536 0.1628 -0.0265 68  ASN A CB    
571   C  CG    . ASN A 68  ? 1.0468 0.5762 0.5328 -0.0536 0.1588 -0.0256 68  ASN A CG    
572   O  OD1   . ASN A 68  ? 1.0619 0.5944 0.5513 -0.0548 0.1565 -0.0253 68  ASN A OD1   
573   N  ND2   . ASN A 68  ? 1.0625 0.5908 0.5471 -0.0523 0.1578 -0.0249 68  ASN A ND2   
574   N  N     . ASP A 69  ? 0.9435 0.4759 0.4306 -0.0553 0.1725 -0.0273 69  ASP A N     
575   C  CA    . ASP A 69  ? 0.9365 0.4671 0.4206 -0.0559 0.1761 -0.0276 69  ASP A CA    
576   C  C     . ASP A 69  ? 0.9233 0.4568 0.409  -0.0566 0.1777 -0.0273 69  ASP A C     
577   O  O     . ASP A 69  ? 0.9283 0.4585 0.4099 -0.0562 0.1797 -0.027  69  ASP A O     
578   C  CB    . ASP A 69  ? 0.9481 0.4803 0.4333 -0.0571 0.1783 -0.0278 69  ASP A CB    
579   C  CG    . ASP A 69  ? 0.9864 0.5253 0.478  -0.0586 0.1783 -0.0277 69  ASP A CG    
580   O  OD1   . ASP A 69  ? 0.9894 0.5307 0.4845 -0.0579 0.1759 -0.0275 69  ASP A OD1   
581   O  OD2   . ASP A 69  ? 1.0104 0.5522 0.5034 -0.0606 0.1808 -0.0278 69  ASP A OD2   
582   N  N     . ARG A 70  ? 0.9012 0.4407 0.3926 -0.0575 0.1771 -0.0271 70  ARG A N     
583   C  CA    . ARG A 70  ? 0.8847 0.4272 0.3776 -0.0577 0.1788 -0.0266 70  ARG A CA    
584   C  C     . ARG A 70  ? 0.8651 0.4058 0.3572 -0.0566 0.1766 -0.0265 70  ARG A C     
585   O  O     . ARG A 70  ? 0.8684 0.404  0.3553 -0.0554 0.1771 -0.0262 70  ARG A O     
586   C  CB    . ARG A 70  ? 0.8947 0.445  0.3937 -0.0596 0.1804 -0.0263 70  ARG A CB    
587   C  CG    . ARG A 70  ? 0.9221 0.4766 0.4235 -0.0595 0.1818 -0.0255 70  ARG A CG    
588   C  CD    . ARG A 70  ? 0.9449 0.5064 0.4506 -0.0614 0.1841 -0.0249 70  ARG A CD    
589   N  NE    . ARG A 70  ? 0.9629 0.5294 0.4715 -0.061  0.1854 -0.0238 70  ARG A NE    
590   C  CZ    . ARG A 70  ? 0.9813 0.548  0.488  -0.06   0.1878 -0.0224 70  ARG A CZ    
591   N  NH1   . ARG A 70  ? 0.9811 0.543  0.4828 -0.0595 0.1892 -0.0221 70  ARG A NH1   
592   N  NH2   . ARG A 70  ? 0.9739 0.5454 0.4833 -0.0592 0.1891 -0.0212 70  ARG A NH2   
593   N  N     . TRP A 71  ? 0.8455 0.3894 0.3419 -0.0571 0.1742 -0.0267 71  TRP A N     
594   C  CA    . TRP A 71  ? 0.8353 0.3774 0.3308 -0.0566 0.1719 -0.0266 71  TRP A CA    
595   C  C     . TRP A 71  ? 0.8367 0.3736 0.3286 -0.0562 0.1685 -0.0268 71  TRP A C     
596   O  O     . TRP A 71  ? 0.8381 0.3749 0.3302 -0.0561 0.1677 -0.0269 71  TRP A O     
597   C  CB    . TRP A 71  ? 0.82   0.3687 0.3224 -0.0575 0.1711 -0.0265 71  TRP A CB    
598   C  CG    . TRP A 71  ? 0.8078 0.3625 0.3142 -0.0581 0.1742 -0.0261 71  TRP A CG    
599   C  CD1   . TRP A 71  ? 0.8098 0.37   0.3209 -0.0592 0.1753 -0.0262 71  TRP A CD1   
600   C  CD2   . TRP A 71  ? 0.8042 0.3596 0.3096 -0.0574 0.1767 -0.0254 71  TRP A CD2   
601   N  NE1   . TRP A 71  ? 0.809  0.374  0.3226 -0.0597 0.1779 -0.0256 71  TRP A NE1   
602   C  CE2   . TRP A 71  ? 0.8068 0.3694 0.3173 -0.0584 0.1789 -0.025  71  TRP A CE2   
603   C  CE3   . TRP A 71  ? 0.813  0.3635 0.3133 -0.0559 0.1773 -0.0249 71  TRP A CE3   
604   C  CZ2   . TRP A 71  ? 0.8114 0.3775 0.3228 -0.0578 0.1816 -0.0238 71  TRP A CZ2   
605   C  CZ3   . TRP A 71  ? 0.8209 0.3742 0.3218 -0.0551 0.1804 -0.0238 71  TRP A CZ3   
606   C  CH2   . TRP A 71  ? 0.8163 0.3778 0.3229 -0.0559 0.1824 -0.0232 71  TRP A CH2   
607   N  N     . ASN A 72  ? 0.8355 0.3679 0.3235 -0.056  0.1664 -0.0268 72  ASN A N     
608   C  CA    . ASN A 72  ? 0.8435 0.3713 0.3278 -0.0561 0.1626 -0.0269 72  ASN A CA    
609   C  C     . ASN A 72  ? 0.8398 0.373  0.3302 -0.0569 0.1596 -0.0265 72  ASN A C     
610   O  O     . ASN A 72  ? 0.8408 0.3722 0.3296 -0.0567 0.1569 -0.0261 72  ASN A O     
611   C  CB    . ASN A 72  ? 0.868  0.3894 0.3462 -0.0562 0.161  -0.0269 72  ASN A CB    
612   C  CG    . ASN A 72  ? 0.9171 0.4412 0.3986 -0.0576 0.1592 -0.0268 72  ASN A CG    
613   O  OD1   . ASN A 72  ? 0.9309 0.4617 0.419  -0.058  0.1605 -0.0267 72  ASN A OD1   
614   N  ND2   . ASN A 72  ? 0.9311 0.4497 0.4076 -0.0586 0.1559 -0.0268 72  ASN A ND2   
615   N  N     . SER A 73  ? 0.8344 0.3744 0.3318 -0.0577 0.1602 -0.0264 73  SER A N     
616   C  CA    . SER A 73  ? 0.8358 0.3815 0.3395 -0.0583 0.158  -0.0257 73  SER A CA    
617   C  C     . SER A 73  ? 0.8322 0.3844 0.3423 -0.0584 0.1606 -0.0258 73  SER A C     
618   O  O     . SER A 73  ? 0.833  0.3864 0.3436 -0.0586 0.1633 -0.0262 73  SER A O     
619   C  CB    . SER A 73  ? 0.8546 0.4008 0.3595 -0.0596 0.1546 -0.0253 73  SER A CB    
620   O  OG    . SER A 73  ? 0.8891 0.4347 0.3935 -0.0601 0.156  -0.0258 73  SER A OG    
621   N  N     . ASN A 74  ? 0.8257 0.382  0.3404 -0.0582 0.16   -0.0252 74  ASN A N     
622   C  CA    . ASN A 74  ? 0.8264 0.388  0.3462 -0.0584 0.1623 -0.0252 74  ASN A CA    
623   C  C     . ASN A 74  ? 0.8241 0.3913 0.3504 -0.059  0.1612 -0.0247 74  ASN A C     
624   O  O     . ASN A 74  ? 0.8283 0.3976 0.3575 -0.0589 0.1587 -0.0237 74  ASN A O     
625   C  CB    . ASN A 74  ? 0.8396 0.4012 0.3596 -0.0574 0.163  -0.0247 74  ASN A CB    
626   C  CG    . ASN A 74  ? 0.8679 0.4323 0.3903 -0.0577 0.166  -0.025  74  ASN A CG    
627   O  OD1   . ASN A 74  ? 0.8786 0.4463 0.4038 -0.0588 0.1675 -0.0254 74  ASN A OD1   
628   N  ND2   . ASN A 74  ? 0.873  0.4359 0.3939 -0.0568 0.1671 -0.0246 74  ASN A ND2   
629   N  N     . ILE A 75  ? 0.8147 0.3847 0.3434 -0.0597 0.1632 -0.0252 75  ILE A N     
630   C  CA    . ILE A 75  ? 0.8096 0.3848 0.3442 -0.0602 0.1625 -0.0247 75  ILE A CA    
631   C  C     . ILE A 75  ? 0.8004 0.3799 0.34   -0.0597 0.1626 -0.024  75  ILE A C     
632   O  O     . ILE A 75  ? 0.7998 0.3829 0.3441 -0.0598 0.1611 -0.0232 75  ILE A O     
633   C  CB    . ILE A 75  ? 0.8169 0.3941 0.3525 -0.0607 0.1648 -0.0253 75  ILE A CB    
634   C  CG1   . ILE A 75  ? 0.8265 0.4073 0.3668 -0.0611 0.1636 -0.0249 75  ILE A CG1   
635   C  CG2   . ILE A 75  ? 0.8227 0.4028 0.3598 -0.0608 0.1678 -0.0256 75  ILE A CG2   
636   C  CD1   . ILE A 75  ? 0.8451 0.4226 0.3831 -0.0617 0.1607 -0.0247 75  ILE A CD1   
637   N  N     . LEU A 76  ? 0.7902 0.3685 0.3281 -0.0592 0.1646 -0.0241 76  LEU A N     
638   C  CA    . LEU A 76  ? 0.7828 0.3635 0.3237 -0.0584 0.1653 -0.0233 76  LEU A CA    
639   C  C     . LEU A 76  ? 0.7813 0.3624 0.3236 -0.0571 0.1626 -0.0218 76  LEU A C     
640   O  O     . LEU A 76  ? 0.7803 0.3644 0.3263 -0.0561 0.1629 -0.0205 76  LEU A O     
641   C  CB    . LEU A 76  ? 0.7837 0.3614 0.3206 -0.0584 0.1681 -0.0239 76  LEU A CB    
642   C  CG    . LEU A 76  ? 0.7986 0.3774 0.335  -0.06   0.1707 -0.025  76  LEU A CG    
643   C  CD1   . LEU A 76  ? 0.8095 0.3844 0.3409 -0.0605 0.1729 -0.0256 76  LEU A CD1   
644   C  CD2   . LEU A 76  ? 0.8038 0.3871 0.3448 -0.0604 0.1716 -0.0248 76  LEU A CD2   
645   N  N     . ASP A 77  ? 0.78   0.3584 0.3194 -0.0571 0.1601 -0.0215 77  ASP A N     
646   C  CA    . ASP A 77  ? 0.7824 0.3622 0.3235 -0.0562 0.1571 -0.0197 77  ASP A CA    
647   C  C     . ASP A 77  ? 0.776  0.3615 0.3238 -0.0568 0.1552 -0.0185 77  ASP A C     
648   O  O     . ASP A 77  ? 0.7769 0.366  0.3284 -0.0557 0.1538 -0.0165 77  ASP A O     
649   C  CB    . ASP A 77  ? 0.8079 0.3833 0.3439 -0.0565 0.1545 -0.0198 77  ASP A CB    
650   C  CG    . ASP A 77  ? 0.8675 0.4452 0.4054 -0.0556 0.1514 -0.0176 77  ASP A CG    
651   O  OD1   . ASP A 77  ? 0.8835 0.4613 0.421  -0.0535 0.1523 -0.0164 77  ASP A OD1   
652   O  OD2   . ASP A 77  ? 0.8888 0.4683 0.4285 -0.057  0.148  -0.0168 77  ASP A OD2   
653   N  N     . LEU A 78  ? 0.7665 0.3532 0.3159 -0.0584 0.1554 -0.0195 78  LEU A N     
654   C  CA    . LEU A 78  ? 0.761  0.3528 0.3165 -0.0591 0.1539 -0.0185 78  LEU A CA    
655   C  C     . LEU A 78  ? 0.7566 0.3531 0.3175 -0.0576 0.1558 -0.0173 78  LEU A C     
656   O  O     . LEU A 78  ? 0.7558 0.357  0.3222 -0.0575 0.1544 -0.0156 78  LEU A O     
657   C  CB    . LEU A 78  ? 0.7613 0.3526 0.3166 -0.0607 0.1544 -0.0199 78  LEU A CB    
658   C  CG    . LEU A 78  ? 0.7776 0.3638 0.3274 -0.062  0.1526 -0.0207 78  LEU A CG    
659   C  CD1   . LEU A 78  ? 0.7852 0.3708 0.3346 -0.063  0.1538 -0.0218 78  LEU A CD1   
660   C  CD2   . LEU A 78  ? 0.783  0.3695 0.3332 -0.0631 0.1484 -0.0193 78  LEU A CD2   
661   N  N     . LEU A 79  ? 0.751  0.3459 0.31   -0.0567 0.1591 -0.0182 79  LEU A N     
662   C  CA    . LEU A 79  ? 0.748  0.3455 0.3102 -0.0552 0.1612 -0.0172 79  LEU A CA    
663   C  C     . LEU A 79  ? 0.7481 0.3457 0.3104 -0.053  0.1607 -0.015  79  LEU A C     
664   O  O     . LEU A 79  ? 0.7464 0.348  0.3134 -0.0516 0.1606 -0.0129 79  LEU A O     
665   C  CB    . LEU A 79  ? 0.7512 0.3461 0.3101 -0.0555 0.1647 -0.0188 79  LEU A CB    
666   C  CG    . LEU A 79  ? 0.7695 0.3654 0.3289 -0.0573 0.1656 -0.0205 79  LEU A CG    
667   C  CD1   . LEU A 79  ? 0.7798 0.3733 0.3354 -0.058  0.1686 -0.0219 79  LEU A CD1   
668   C  CD2   . LEU A 79  ? 0.7722 0.3729 0.3375 -0.0573 0.1656 -0.0199 79  LEU A CD2   
669   N  N     . SER A 80  ? 0.7496 0.3429 0.3065 -0.0525 0.1603 -0.0152 80  SER A N     
670   C  CA    . SER A 80  ? 0.7538 0.3471 0.3103 -0.05   0.1598 -0.013  80  SER A CA    
671   C  C     . SER A 80  ? 0.7515 0.35   0.313  -0.0498 0.1561 -0.0105 80  SER A C     
672   O  O     . SER A 80  ? 0.7501 0.3514 0.3139 -0.0474 0.1561 -0.0077 80  SER A O     
673   C  CB    . SER A 80  ? 0.7722 0.3594 0.3215 -0.0495 0.1604 -0.0139 80  SER A CB    
674   O  OG    . SER A 80  ? 0.798  0.3835 0.345  -0.0511 0.1575 -0.0148 80  SER A OG    
675   N  N     . GLN A 81  ? 0.7486 0.3485 0.3115 -0.0523 0.1532 -0.0111 81  GLN A N     
676   C  CA    . GLN A 81  ? 0.7499 0.3549 0.3175 -0.0531 0.1493 -0.0088 81  GLN A CA    
677   C  C     . GLN A 81  ? 0.7497 0.3614 0.3251 -0.0523 0.1499 -0.0068 81  GLN A C     
678   O  O     . GLN A 81  ? 0.7507 0.3679 0.3309 -0.0521 0.1474 -0.0039 81  GLN A O     
679   C  CB    . GLN A 81  ? 0.7673 0.3706 0.3332 -0.0563 0.1464 -0.0103 81  GLN A CB    
680   C  CG    . GLN A 81  ? 0.8042 0.4013 0.3626 -0.0569 0.145  -0.0116 81  GLN A CG    
681   C  CD    . GLN A 81  ? 0.8472 0.4412 0.4026 -0.0599 0.1427 -0.0132 81  GLN A CD    
682   O  OE1   . GLN A 81  ? 0.8652 0.4623 0.4241 -0.0619 0.1404 -0.0124 81  GLN A OE1   
683   N  NE2   . GLN A 81  ? 0.8497 0.4369 0.398  -0.0602 0.1435 -0.0152 81  GLN A NE2   
684   N  N     . LYS A 82  ? 0.7451 0.3565 0.3216 -0.052  0.1532 -0.0081 82  LYS A N     
685   C  CA    . LYS A 82  ? 0.7416 0.3583 0.3247 -0.0512 0.1542 -0.0064 82  LYS A CA    
686   C  C     . LYS A 82  ? 0.7389 0.3553 0.322  -0.0479 0.1579 -0.0052 82  LYS A C     
687   O  O     . LYS A 82  ? 0.7419 0.3614 0.3293 -0.0469 0.1596 -0.0042 82  LYS A O     
688   C  CB    . LYS A 82  ? 0.7666 0.3836 0.3512 -0.0534 0.1548 -0.0085 82  LYS A CB    
689   C  CG    . LYS A 82  ? 0.8202 0.4374 0.4049 -0.0564 0.1513 -0.0092 82  LYS A CG    
690   C  CD    . LYS A 82  ? 0.8778 0.5015 0.4693 -0.0572 0.1486 -0.0065 82  LYS A CD    
691   C  CE    . LYS A 82  ? 0.9269 0.5542 0.5237 -0.057  0.1504 -0.0063 82  LYS A CE    
692   N  NZ    . LYS A 82  ? 0.9515 0.5857 0.5556 -0.0572 0.1484 -0.0031 82  LYS A NZ    
693   N  N     . GLY A 83  ? 0.7328 0.3448 0.3106 -0.0461 0.1593 -0.0052 83  GLY A N     
694   C  CA    . GLY A 83  ? 0.7314 0.3416 0.3077 -0.0429 0.163  -0.0038 83  GLY A CA    
695   C  C     . GLY A 83  ? 0.7298 0.3332 0.2995 -0.0431 0.1666 -0.0065 83  GLY A C     
696   O  O     . GLY A 83  ? 0.7363 0.3374 0.304  -0.0407 0.1699 -0.0055 83  GLY A O     
697   N  N     . SER A 84  ? 0.7188 0.3188 0.2847 -0.0459 0.1663 -0.0096 84  SER A N     
698   C  CA    . SER A 84  ? 0.7168 0.311  0.2766 -0.0465 0.1695 -0.0119 84  SER A CA    
699   C  C     . SER A 84  ? 0.7213 0.3099 0.2745 -0.0453 0.1703 -0.0118 84  SER A C     
700   O  O     . SER A 84  ? 0.726  0.3119 0.2756 -0.0469 0.1692 -0.0135 84  SER A O     
701   C  CB    . SER A 84  ? 0.7236 0.3174 0.2826 -0.0498 0.1691 -0.0147 84  SER A CB    
702   O  OG    . SER A 84  ? 0.7448 0.3343 0.2989 -0.0508 0.172  -0.0166 84  SER A OG    
703   N  N     . PHE A 85  ? 0.7177 0.3045 0.2691 -0.0422 0.1724 -0.0097 85  PHE A N     
704   C  CA    . PHE A 85  ? 0.7215 0.3026 0.2664 -0.0404 0.1736 -0.0093 85  PHE A CA    
705   C  C     . PHE A 85  ? 0.7243 0.2978 0.2613 -0.0416 0.177  -0.0116 85  PHE A C     
706   O  O     . PHE A 85  ? 0.7316 0.2996 0.2624 -0.0403 0.1782 -0.0115 85  PHE A O     
707   C  CB    . PHE A 85  ? 0.7188 0.3012 0.2648 -0.0361 0.1746 -0.0056 85  PHE A CB    
708   C  CG    . PHE A 85  ? 0.7268 0.3089 0.2736 -0.0342 0.1778 -0.0043 85  PHE A CG    
709   C  CD1   . PHE A 85  ? 0.7429 0.3173 0.2823 -0.034  0.1819 -0.0055 85  PHE A CD1   
710   C  CD2   . PHE A 85  ? 0.7307 0.3198 0.2852 -0.0327 0.1769 -0.0017 85  PHE A CD2   
711   C  CE1   . PHE A 85  ? 0.7517 0.3248 0.2909 -0.0324 0.1849 -0.0044 85  PHE A CE1   
712   C  CE2   . PHE A 85  ? 0.7383 0.3266 0.2931 -0.0307 0.1802 -0.0004 85  PHE A CE2   
713   C  CZ    . PHE A 85  ? 0.7414 0.3213 0.2882 -0.0305 0.1842 -0.0018 85  PHE A CZ    
714   N  N     . LEU A 86  ? 0.7186 0.2914 0.2553 -0.0441 0.1785 -0.0136 86  LEU A N     
715   C  CA    . LEU A 86  ? 0.726  0.2922 0.2554 -0.0461 0.1812 -0.0158 86  LEU A CA    
716   C  C     . LEU A 86  ? 0.7278 0.2948 0.257  -0.0494 0.1796 -0.0182 86  LEU A C     
717   O  O     . LEU A 86  ? 0.7219 0.2943 0.2566 -0.0508 0.1775 -0.0187 86  LEU A O     
718   C  CB    . LEU A 86  ? 0.7284 0.2932 0.2568 -0.047  0.1839 -0.0162 86  LEU A CB    
719   C  CG    . LEU A 86  ? 0.7444 0.3074 0.272  -0.0434 0.1863 -0.0138 86  LEU A CG    
720   C  CD1   . LEU A 86  ? 0.7514 0.3122 0.2771 -0.0448 0.1887 -0.0146 86  LEU A CD1   
721   C  CD2   . LEU A 86  ? 0.7557 0.3115 0.2759 -0.0408 0.1885 -0.0127 86  LEU A CD2   
722   N  N     . TYR A 87  ? 0.7335 0.2948 0.256  -0.0506 0.1808 -0.0195 87  TYR A N     
723   C  CA    . TYR A 87  ? 0.7377 0.2996 0.2597 -0.0534 0.1797 -0.0214 87  TYR A CA    
724   C  C     . TYR A 87  ? 0.736  0.2981 0.257  -0.0567 0.1814 -0.0231 87  TYR A C     
725   O  O     . TYR A 87  ? 0.7402 0.2993 0.2568 -0.059  0.1825 -0.0244 87  TYR A O     
726   C  CB    . TYR A 87  ? 0.7443 0.301  0.2605 -0.053  0.1797 -0.0218 87  TYR A CB    
727   C  CG    . TYR A 87  ? 0.7536 0.3119 0.2707 -0.0547 0.1778 -0.023  87  TYR A CG    
728   C  CD1   . TYR A 87  ? 0.7595 0.3235 0.2826 -0.0551 0.1752 -0.0229 87  TYR A CD1   
729   C  CD2   . TYR A 87  ? 0.7667 0.3203 0.2781 -0.0557 0.1787 -0.024  87  TYR A CD2   
730   C  CE1   . TYR A 87  ? 0.7685 0.333  0.2914 -0.0563 0.1738 -0.0238 87  TYR A CE1   
731   C  CE2   . TYR A 87  ? 0.7753 0.3298 0.287  -0.0568 0.1773 -0.0249 87  TYR A CE2   
732   C  CZ    . TYR A 87  ? 0.7802 0.3399 0.2973 -0.057  0.1749 -0.0247 87  TYR A CZ    
733   O  OH    . TYR A 87  ? 0.7952 0.3549 0.3117 -0.0578 0.1739 -0.0254 87  TYR A OH    
734   N  N     . GLU A 88  ? 0.7272 0.2931 0.2524 -0.057  0.1816 -0.0228 88  GLU A N     
735   C  CA    . GLU A 88  ? 0.7295 0.297  0.2548 -0.0601 0.1828 -0.0241 88  GLU A CA    
736   C  C     . GLU A 88  ? 0.7232 0.2969 0.2541 -0.0612 0.1807 -0.0246 88  GLU A C     
737   O  O     . GLU A 88  ? 0.7217 0.2994 0.2579 -0.0596 0.1786 -0.0238 88  GLU A O     
738   C  CB    . GLU A 88  ? 0.7629 0.3308 0.2894 -0.0595 0.1841 -0.0234 88  GLU A CB    
739   C  CG    . GLU A 88  ? 0.8426 0.403  0.3622 -0.0582 0.1868 -0.0228 88  GLU A CG    
740   C  CD    . GLU A 88  ? 0.9389 0.4954 0.4534 -0.061  0.1893 -0.0238 88  GLU A CD    
741   O  OE1   . GLU A 88  ? 0.9509 0.5119 0.4685 -0.0636 0.1888 -0.0246 88  GLU A OE1   
742   O  OE2   . GLU A 88  ? 0.9771 0.5259 0.4841 -0.0606 0.1918 -0.0236 88  GLU A OE2   
743   N  N     . THR A 89  ? 0.7184 0.2926 0.2476 -0.0639 0.1812 -0.0258 89  THR A N     
744   C  CA    . THR A 89  ? 0.7175 0.2966 0.2506 -0.0647 0.1798 -0.0261 89  THR A CA    
745   C  C     . THR A 89  ? 0.7215 0.3057 0.2581 -0.0665 0.1804 -0.0264 89  THR A C     
746   O  O     . THR A 89  ? 0.723  0.307  0.257  -0.0691 0.182  -0.027  89  THR A O     
747   C  CB    . THR A 89  ? 0.7307 0.3073 0.2598 -0.0657 0.1801 -0.0267 89  THR A CB    
748   O  OG1   . THR A 89  ? 0.7441 0.316  0.2703 -0.0637 0.1794 -0.0264 89  THR A OG1   
749   C  CG2   . THR A 89  ? 0.7331 0.3136 0.2651 -0.0661 0.1792 -0.0268 89  THR A CG2   
750   N  N     . PRO A 90  ? 0.7197 0.3088 0.262  -0.0655 0.179  -0.026  90  PRO A N     
751   C  CA    . PRO A 90  ? 0.7194 0.3137 0.2649 -0.067  0.1796 -0.0262 90  PRO A CA    
752   C  C     . PRO A 90  ? 0.7254 0.322  0.2702 -0.0686 0.1801 -0.0265 90  PRO A C     
753   O  O     . PRO A 90  ? 0.7273 0.3215 0.2696 -0.0683 0.1798 -0.0266 90  PRO A O     
754   C  CB    . PRO A 90  ? 0.7231 0.3209 0.2742 -0.0651 0.178  -0.0256 90  PRO A CB    
755   C  CG    . PRO A 90  ? 0.7292 0.3247 0.2799 -0.0635 0.1762 -0.0253 90  PRO A CG    
756   C  CD    . PRO A 90  ? 0.7121 0.3022 0.2578 -0.0632 0.1768 -0.0253 90  PRO A CD    
757   N  N     . ASP A 91  ? 0.7237 0.3253 0.2707 -0.0702 0.1809 -0.0264 91  ASP A N     
758   C  CA    . ASP A 91  ? 0.7254 0.3303 0.2722 -0.0715 0.1817 -0.0262 91  ASP A CA    
759   C  C     . ASP A 91  ? 0.7159 0.3224 0.265  -0.0694 0.1808 -0.0258 91  ASP A C     
760   O  O     . ASP A 91  ? 0.7131 0.3189 0.2601 -0.0693 0.1813 -0.0255 91  ASP A O     
761   C  CB    . ASP A 91  ? 0.7522 0.3623 0.3005 -0.0738 0.1828 -0.0259 91  ASP A CB    
762   C  CG    . ASP A 91  ? 0.8242 0.4318 0.3684 -0.0769 0.1838 -0.0263 91  ASP A CG    
763   O  OD1   . ASP A 91  ? 0.8393 0.441  0.3789 -0.0772 0.1841 -0.0268 91  ASP A OD1   
764   O  OD2   . ASP A 91  ? 0.8509 0.4619 0.3958 -0.079  0.1843 -0.0262 91  ASP A OD2   
765   N  N     . VAL A 92  ? 0.7101 0.318  0.2629 -0.0677 0.1797 -0.0256 92  VAL A N     
766   C  CA    . VAL A 92  ? 0.7125 0.321  0.2667 -0.066  0.1788 -0.0253 92  VAL A CA    
767   C  C     . VAL A 92  ? 0.7156 0.322  0.2717 -0.0644 0.1768 -0.0254 92  VAL A C     
768   O  O     . VAL A 92  ? 0.7117 0.3188 0.2701 -0.0643 0.1764 -0.0254 92  VAL A O     
769   C  CB    . VAL A 92  ? 0.718  0.3324 0.2755 -0.0659 0.18   -0.0247 92  VAL A CB    
770   C  CG1   . VAL A 92  ? 0.7264 0.3406 0.2851 -0.064  0.1793 -0.0244 92  VAL A CG1   
771   C  CG2   . VAL A 92  ? 0.7237 0.3411 0.2797 -0.0672 0.1818 -0.024  92  VAL A CG2   
772   N  N     . ILE A 93  ? 0.722  0.3258 0.2769 -0.0633 0.1755 -0.0253 93  ILE A N     
773   C  CA    . ILE A 93  ? 0.7319 0.3344 0.2886 -0.0623 0.1733 -0.0251 93  ILE A CA    
774   C  C     . ILE A 93  ? 0.7381 0.3409 0.2948 -0.0618 0.1732 -0.025  93  ILE A C     
775   O  O     . ILE A 93  ? 0.7424 0.3426 0.2952 -0.0615 0.1738 -0.025  93  ILE A O     
776   C  CB    . ILE A 93  ? 0.743  0.3406 0.2966 -0.0619 0.1714 -0.0251 93  ILE A CB    
777   C  CG1   . ILE A 93  ? 0.7549 0.3513 0.3077 -0.062  0.1718 -0.0251 93  ILE A CG1   
778   C  CG2   . ILE A 93  ? 0.7499 0.3469 0.3054 -0.0614 0.1688 -0.0247 93  ILE A CG2   
779   C  CD1   . ILE A 93  ? 0.7729 0.3647 0.3222 -0.0614 0.1704 -0.025  93  ILE A CD1   
780   N  N     . ILE A 94  ? 0.7373 0.3429 0.2979 -0.0615 0.1728 -0.0247 94  ILE A N     
781   C  CA    . ILE A 94  ? 0.7446 0.3497 0.3046 -0.0609 0.173  -0.0245 94  ILE A CA    
782   C  C     . ILE A 94  ? 0.7551 0.3567 0.3146 -0.061  0.1702 -0.0245 94  ILE A C     
783   O  O     . ILE A 94  ? 0.7559 0.3592 0.3192 -0.0613 0.1687 -0.0242 94  ILE A O     
784   C  CB    . ILE A 94  ? 0.7453 0.3554 0.3094 -0.0605 0.1745 -0.0242 94  ILE A CB    
785   C  CG1   . ILE A 94  ? 0.7534 0.3678 0.3184 -0.0608 0.1768 -0.0241 94  ILE A CG1   
786   C  CG2   . ILE A 94  ? 0.751  0.3597 0.3137 -0.0596 0.1749 -0.024  94  ILE A CG2   
787   C  CD1   . ILE A 94  ? 0.7646 0.3842 0.3335 -0.0605 0.1781 -0.0237 94  ILE A CD1   
788   N  N     . THR A 95  ? 0.7624 0.3589 0.3169 -0.0609 0.1696 -0.0246 95  THR A N     
789   C  CA    . THR A 95  ? 0.7769 0.3698 0.3301 -0.0617 0.1667 -0.0245 95  THR A CA    
790   C  C     . THR A 95  ? 0.791  0.381  0.3416 -0.0617 0.1671 -0.0245 95  THR A C     
791   O  O     . THR A 95  ? 0.7921 0.3817 0.3403 -0.0605 0.1697 -0.0245 95  THR A O     
792   C  CB    . THR A 95  ? 0.7971 0.3849 0.3455 -0.062  0.1649 -0.0247 95  THR A CB    
793   O  OG1   . THR A 95  ? 0.8171 0.4002 0.3592 -0.0614 0.1665 -0.025  95  THR A OG1   
794   C  CG2   . THR A 95  ? 0.7995 0.3891 0.3494 -0.0618 0.165  -0.0247 95  THR A CG2   
795   N  N     . SER A 96  ? 0.7997 0.3877 0.3504 -0.0629 0.1644 -0.0243 96  SER A N     
796   C  CA    . SER A 96  ? 0.8171 0.4007 0.364  -0.0634 0.1645 -0.0244 96  SER A CA    
797   C  C     . SER A 96  ? 0.8309 0.407  0.3709 -0.0647 0.1619 -0.0246 96  SER A C     
798   O  O     . SER A 96  ? 0.8318 0.4081 0.3728 -0.0659 0.1589 -0.0244 96  SER A O     
799   C  CB    . SER A 96  ? 0.8361 0.4231 0.3883 -0.0644 0.1633 -0.024  96  SER A CB    
800   O  OG    . SER A 96  ? 0.8766 0.4583 0.4242 -0.0652 0.1631 -0.0241 96  SER A OG    
801   N  N     . LEU A 97  ? 0.8402 0.4093 0.3726 -0.0643 0.1632 -0.0249 97  LEU A N     
802   C  CA    . LEU A 97  ? 0.8554 0.4161 0.3799 -0.0656 0.1608 -0.0251 97  LEU A CA    
803   C  C     . LEU A 97  ? 0.8685 0.4256 0.3911 -0.0681 0.1585 -0.0251 97  LEU A C     
804   O  O     . LEU A 97  ? 0.8739 0.4277 0.3933 -0.0677 0.1605 -0.0252 97  LEU A O     
805   C  CB    . LEU A 97  ? 0.8627 0.4163 0.3786 -0.0637 0.1637 -0.0253 97  LEU A CB    
806   C  CG    . LEU A 97  ? 0.882  0.4363 0.3969 -0.062  0.1652 -0.0253 97  LEU A CG    
807   C  CD1   . LEU A 97  ? 0.8983 0.4444 0.4038 -0.0603 0.1677 -0.0252 97  LEU A CD1   
808   C  CD2   . LEU A 97  ? 0.889  0.4429 0.4043 -0.0635 0.1617 -0.0256 97  LEU A CD2   
809   N  N     . ASN A 98  ? 0.8724 0.43   0.3967 -0.0707 0.1542 -0.0248 98  ASN A N     
810   C  CA    . ASN A 98  ? 0.884  0.4386 0.4066 -0.0738 0.1514 -0.0245 98  ASN A CA    
811   C  C     . ASN A 98  ? 0.8895 0.4395 0.4074 -0.0765 0.147  -0.0243 98  ASN A C     
812   O  O     . ASN A 98  ? 0.8922 0.4464 0.4138 -0.0762 0.1452 -0.0238 98  ASN A O     
813   C  CB    . ASN A 98  ? 0.8983 0.4615 0.4307 -0.0747 0.1505 -0.0237 98  ASN A CB    
814   C  CG    . ASN A 98  ? 0.9473 0.51   0.4799 -0.0741 0.1533 -0.0239 98  ASN A CG    
815   O  OD1   . ASN A 98  ? 0.9579 0.5273 0.4972 -0.0722 0.1558 -0.0237 98  ASN A OD1   
816   N  ND2   . ASN A 98  ? 0.965  0.5191 0.4894 -0.0758 0.1531 -0.0243 98  ASN A ND2   
817   N  N     . ASN A 99  ? 0.8895 0.4308 0.3991 -0.0791 0.1452 -0.0246 99  ASN A N     
818   C  CA    . ASN A 99  ? 0.8934 0.4289 0.3968 -0.0823 0.1407 -0.0244 99  ASN A CA    
819   C  C     . ASN A 99  ? 0.8878 0.4215 0.3881 -0.0807 0.1402 -0.0246 99  ASN A C     
820   O  O     . ASN A 99  ? 0.8909 0.4268 0.3928 -0.0824 0.1363 -0.0239 99  ASN A O     
821   C  CB    . ASN A 99  ? 0.9068 0.4486 0.4169 -0.0861 0.136  -0.0231 99  ASN A CB    
822   C  CG    . ASN A 99  ? 0.9408 0.4952 0.4637 -0.0847 0.1358 -0.0218 99  ASN A CG    
823   O  OD1   . ASN A 99  ? 0.9573 0.5157 0.4833 -0.0832 0.135  -0.0213 99  ASN A OD1   
824   N  ND2   . ASN A 99  ? 0.9411 0.5013 0.471  -0.0851 0.1366 -0.0212 99  ASN A ND2   
825   N  N     . GLY A 100 ? 0.8769 0.4064 0.3724 -0.0774 0.1442 -0.0254 100 GLY A N     
826   C  CA    . GLY A 100 ? 0.8693 0.3958 0.3607 -0.0757 0.1444 -0.0257 100 GLY A CA    
827   C  C     . GLY A 100 ? 0.851  0.3867 0.3511 -0.0741 0.1444 -0.0252 100 GLY A C     
828   O  O     . GLY A 100 ? 0.8548 0.3884 0.352  -0.0733 0.1435 -0.0253 100 GLY A O     
829   N  N     . LYS A 101 ? 0.8305 0.3757 0.3406 -0.0734 0.1455 -0.0247 101 LYS A N     
830   C  CA    . LYS A 101 ? 0.8174 0.3705 0.335  -0.0717 0.1459 -0.0242 101 LYS A CA    
831   C  C     . LYS A 101 ? 0.7991 0.3592 0.3239 -0.0697 0.1496 -0.0243 101 LYS A C     
832   O  O     . LYS A 101 ? 0.7984 0.3589 0.3241 -0.0699 0.1511 -0.0245 101 LYS A O     
833   C  CB    . LYS A 101 ? 0.8385 0.3968 0.3615 -0.0736 0.1415 -0.0229 101 LYS A CB    
834   C  CG    . LYS A 101 ? 0.8858 0.4504 0.4162 -0.0751 0.1406 -0.022  101 LYS A CG    
835   C  CD    . LYS A 101 ? 0.9381 0.5087 0.4743 -0.0768 0.1365 -0.0201 101 LYS A CD    
836   C  CE    . LYS A 101 ? 0.9785 0.5572 0.5239 -0.0772 0.1367 -0.0189 101 LYS A CE    
837   N  NZ    . LYS A 101 ? 0.9995 0.5856 0.5518 -0.0776 0.1337 -0.0166 101 LYS A NZ    
838   N  N     . GLU A 102 ? 0.7826 0.3478 0.312  -0.068  0.151  -0.0241 102 GLU A N     
839   C  CA    . GLU A 102 ? 0.7727 0.3443 0.3083 -0.0664 0.1542 -0.0242 102 GLU A CA    
840   C  C     . GLU A 102 ? 0.7607 0.3397 0.3048 -0.0669 0.1527 -0.0232 102 GLU A C     
841   O  O     . GLU A 102 ? 0.764  0.3446 0.3099 -0.0674 0.15   -0.0222 102 GLU A O     
842   C  CB    . GLU A 102 ? 0.7937 0.3658 0.3284 -0.0645 0.1569 -0.0246 102 GLU A CB    
843   C  CG    . GLU A 102 ? 0.8414 0.4066 0.3681 -0.0637 0.1585 -0.0253 102 GLU A CG    
844   C  CD    . GLU A 102 ? 0.9017 0.4685 0.4284 -0.0621 0.1618 -0.0255 102 GLU A CD    
845   O  OE1   . GLU A 102 ? 0.9089 0.4817 0.4409 -0.0616 0.164  -0.0254 102 GLU A OE1   
846   O  OE2   . GLU A 102 ? 0.9264 0.4886 0.4477 -0.0615 0.1621 -0.0257 102 GLU A OE2   
847   N  N     . GLU A 103 ? 0.7429 0.3266 0.2922 -0.0664 0.1547 -0.0231 103 GLU A N     
848   C  CA    . GLU A 103 ? 0.7307 0.3213 0.2879 -0.0664 0.154  -0.022  103 GLU A CA    
849   C  C     . GLU A 103 ? 0.7133 0.308  0.2741 -0.0646 0.1575 -0.0224 103 GLU A C     
850   O  O     . GLU A 103 ? 0.7181 0.3127 0.2781 -0.0642 0.1599 -0.0231 103 GLU A O     
851   C  CB    . GLU A 103 ? 0.7628 0.3545 0.3225 -0.0681 0.1525 -0.0215 103 GLU A CB    
852   C  CG    . GLU A 103 ? 0.8369 0.4253 0.3937 -0.0706 0.1484 -0.0208 103 GLU A CG    
853   C  CD    . GLU A 103 ? 0.9237 0.5095 0.4789 -0.0728 0.1473 -0.0209 103 GLU A CD    
854   O  OE1   . GLU A 103 ? 0.9393 0.5188 0.4879 -0.0749 0.145  -0.0211 103 GLU A OE1   
855   O  OE2   . GLU A 103 ? 0.9457 0.5352 0.5056 -0.0726 0.1489 -0.0207 103 GLU A OE2   
856   N  N     . ILE A 104 ? 0.6901 0.2883 0.2543 -0.0637 0.158  -0.0218 104 ILE A N     
857   C  CA    . ILE A 104 ? 0.6736 0.2751 0.2404 -0.0625 0.1611 -0.0222 104 ILE A CA    
858   C  C     . ILE A 104 ? 0.6554 0.2613 0.2274 -0.0624 0.1621 -0.0219 104 ILE A C     
859   O  O     . ILE A 104 ? 0.653  0.2615 0.2293 -0.0627 0.1605 -0.0208 104 ILE A O     
860   C  CB    . ILE A 104 ? 0.6758 0.2785 0.2437 -0.0615 0.1615 -0.0217 104 ILE A CB    
861   C  CG1   . ILE A 104 ? 0.6889 0.2868 0.2508 -0.0614 0.1613 -0.0223 104 ILE A CG1   
862   C  CG2   . ILE A 104 ? 0.6775 0.2833 0.2479 -0.0607 0.1644 -0.0219 104 ILE A CG2   
863   C  CD1   . ILE A 104 ? 0.702  0.2998 0.2637 -0.0604 0.1618 -0.0218 104 ILE A CD1   
864   N  N     . LEU A 105 ? 0.6412 0.2481 0.2129 -0.0619 0.1649 -0.0227 105 LEU A N     
865   C  CA    . LEU A 105 ? 0.6292 0.2402 0.2053 -0.0615 0.1663 -0.0225 105 LEU A CA    
866   C  C     . LEU A 105 ? 0.6199 0.2344 0.199  -0.0607 0.168  -0.0223 105 LEU A C     
867   O  O     . LEU A 105 ? 0.6149 0.2326 0.1986 -0.0602 0.1683 -0.0217 105 LEU A O     
868   C  CB    . LEU A 105 ? 0.6265 0.2368 0.2002 -0.0612 0.1682 -0.0232 105 LEU A CB    
869   C  CG    . LEU A 105 ? 0.6379 0.2437 0.2077 -0.0618 0.1672 -0.0233 105 LEU A CG    
870   C  CD1   . LEU A 105 ? 0.6429 0.2481 0.2101 -0.0608 0.1699 -0.0236 105 LEU A CD1   
871   C  CD2   . LEU A 105 ? 0.6424 0.2488 0.2154 -0.0628 0.1651 -0.0227 105 LEU A CD2   
872   N  N     . MET A 106 ? 0.6183 0.2316 0.1943 -0.0607 0.1693 -0.0229 106 MET A N     
873   C  CA    . MET A 106 ? 0.6193 0.2345 0.1964 -0.0604 0.1711 -0.023  106 MET A CA    
874   C  C     . MET A 106 ? 0.6113 0.224  0.1838 -0.0609 0.172  -0.0236 106 MET A C     
875   O  O     . MET A 106 ? 0.6127 0.223  0.1816 -0.0613 0.1718 -0.024  106 MET A O     
876   C  CB    . MET A 106 ? 0.6305 0.2495 0.21   -0.0603 0.173  -0.0232 106 MET A CB    
877   C  CG    . MET A 106 ? 0.6689 0.2885 0.2456 -0.0608 0.1746 -0.0238 106 MET A CG    
878   S  SD    . MET A 106 ? 0.7578 0.3824 0.3378 -0.0604 0.1765 -0.0236 106 MET A SD    
879   C  CE    . MET A 106 ? 0.7368 0.3605 0.3183 -0.0596 0.1754 -0.0233 106 MET A CE    
880   N  N     . ALA A 107 ? 0.6001 0.2127 0.1722 -0.061  0.1731 -0.0235 107 ALA A N     
881   C  CA    . ALA A 107 ? 0.5951 0.2051 0.1627 -0.0618 0.1743 -0.0241 107 ALA A CA    
882   C  C     . ALA A 107 ? 0.5851 0.1976 0.1529 -0.0629 0.1764 -0.0245 107 ALA A C     
883   O  O     . ALA A 107 ? 0.5873 0.2019 0.1579 -0.0625 0.1769 -0.0241 107 ALA A O     
884   C  CB    . ALA A 107 ? 0.5977 0.2045 0.1638 -0.0611 0.1739 -0.0236 107 ALA A CB    
885   N  N     . ILE A 108 ? 0.5738 0.1866 0.1387 -0.0644 0.1775 -0.025  108 ILE A N     
886   C  CA    . ILE A 108 ? 0.5701 0.1861 0.135  -0.066  0.1791 -0.0252 108 ILE A CA    
887   C  C     . ILE A 108 ? 0.5777 0.1911 0.1378 -0.0681 0.1802 -0.0256 108 ILE A C     
888   O  O     . ILE A 108 ? 0.582  0.1931 0.1392 -0.0685 0.1801 -0.0257 108 ILE A O     
889   C  CB    . ILE A 108 ? 0.5691 0.1898 0.136  -0.0661 0.1796 -0.0249 108 ILE A CB    
890   C  CG1   . ILE A 108 ? 0.5806 0.203  0.1515 -0.0642 0.1788 -0.0245 108 ILE A CG1   
891   C  CG2   . ILE A 108 ? 0.5707 0.1955 0.1377 -0.0679 0.1811 -0.0248 108 ILE A CG2   
892   C  CD1   . ILE A 108 ? 0.5977 0.2231 0.1693 -0.0636 0.1795 -0.0242 108 ILE A CD1   
893   N  N     . GLU A 109 ? 0.5769 0.1903 0.1357 -0.0696 0.1812 -0.0257 109 GLU A N     
894   C  CA    . GLU A 109 ? 0.5833 0.1938 0.137  -0.0722 0.1823 -0.0262 109 GLU A CA    
895   C  C     . GLU A 109 ? 0.5921 0.2071 0.146  -0.0748 0.1831 -0.0261 109 GLU A C     
896   O  O     . GLU A 109 ? 0.5962 0.2134 0.1524 -0.0745 0.1832 -0.026  109 GLU A O     
897   C  CB    . GLU A 109 ? 0.5978 0.202  0.1478 -0.0718 0.1828 -0.0264 109 GLU A CB    
898   C  CG    . GLU A 109 ? 0.6365 0.2366 0.1801 -0.0748 0.1841 -0.0269 109 GLU A CG    
899   C  CD    . GLU A 109 ? 0.6871 0.2838 0.2269 -0.0754 0.1842 -0.0272 109 GLU A CD    
900   O  OE1   . GLU A 109 ? 0.694  0.2886 0.229  -0.0785 0.1853 -0.0276 109 GLU A OE1   
901   O  OE2   . GLU A 109 ? 0.7089 0.3048 0.2502 -0.073  0.1832 -0.027  109 GLU A OE2   
902   N  N     . PHE A 110 ? 0.5942 0.2111 0.146  -0.0774 0.1837 -0.026  110 PHE A N     
903   C  CA    . PHE A 110 ? 0.6035 0.2257 0.1556 -0.0804 0.1842 -0.0255 110 PHE A CA    
904   C  C     . PHE A 110 ? 0.6213 0.2392 0.1674 -0.0841 0.1849 -0.0261 110 PHE A C     
905   O  O     . PHE A 110 ? 0.6299 0.2444 0.1723 -0.0852 0.1853 -0.0263 110 PHE A O     
906   C  CB    . PHE A 110 ? 0.5987 0.2271 0.1531 -0.0808 0.1845 -0.0245 110 PHE A CB    
907   C  CG    . PHE A 110 ? 0.602  0.2329 0.1604 -0.0772 0.1841 -0.0239 110 PHE A CG    
908   C  CD1   . PHE A 110 ? 0.6078 0.2348 0.165  -0.0754 0.1838 -0.0241 110 PHE A CD1   
909   C  CD2   . PHE A 110 ? 0.6096 0.2462 0.1724 -0.0759 0.1842 -0.0232 110 PHE A CD2   
910   C  CE1   . PHE A 110 ? 0.6128 0.241  0.1726 -0.0725 0.1835 -0.0237 110 PHE A CE1   
911   C  CE2   . PHE A 110 ? 0.6148 0.2526 0.1802 -0.0728 0.1841 -0.0227 110 PHE A CE2   
912   C  CZ    . PHE A 110 ? 0.6096 0.243  0.1733 -0.0713 0.1838 -0.023  110 PHE A CZ    
913   N  N     . CYS A 111 ? 0.6253 0.2428 0.1696 -0.0861 0.1852 -0.0263 111 CYS A N     
914   C  CA    . CYS A 111 ? 0.6386 0.2508 0.1759 -0.09   0.1859 -0.0268 111 CYS A CA    
915   C  C     . CYS A 111 ? 0.6391 0.2562 0.1757 -0.0942 0.1857 -0.0264 111 CYS A C     
916   O  O     . CYS A 111 ? 0.6354 0.2535 0.1727 -0.0942 0.1856 -0.0264 111 CYS A O     
917   C  CB    . CYS A 111 ? 0.6571 0.2602 0.1897 -0.0886 0.1866 -0.0276 111 CYS A CB    
918   S  SG    . CYS A 111 ? 0.7164 0.3099 0.2385 -0.0927 0.188  -0.0285 111 CYS A SG    
919   N  N     . SER A 112 ? 0.6422 0.2624 0.1772 -0.098  0.1857 -0.0258 112 SER A N     
920   C  CA    . SER A 112 ? 0.6494 0.2748 0.1834 -0.1028 0.1853 -0.0251 112 SER A CA    
921   C  C     . SER A 112 ? 0.6582 0.2751 0.1831 -0.1073 0.1858 -0.0262 112 SER A C     
922   O  O     . SER A 112 ? 0.6652 0.2836 0.1879 -0.1109 0.1853 -0.026  112 SER A O     
923   C  CB    . SER A 112 ? 0.6678 0.3012 0.2046 -0.1049 0.1852 -0.0236 112 SER A CB    
924   O  OG    . SER A 112 ? 0.6989 0.3277 0.2327 -0.1051 0.1859 -0.0239 112 SER A OG    
925   N  N     . ALA A 113 ? 0.657  0.2647 0.1763 -0.1071 0.1868 -0.0272 113 ALA A N     
926   C  CA    . ALA A 113 ? 0.6665 0.264  0.1759 -0.1107 0.1877 -0.0282 113 ALA A CA    
927   C  C     . ALA A 113 ? 0.6684 0.2611 0.173  -0.1122 0.1879 -0.0288 113 ALA A C     
928   O  O     . ALA A 113 ? 0.6654 0.2595 0.1739 -0.1085 0.1877 -0.0287 113 ALA A O     
929   C  CB    . ALA A 113 ? 0.6746 0.2627 0.1803 -0.1074 0.189  -0.0291 113 ALA A CB    
930   N  N     . LEU A 114 ? 0.6716 0.2577 0.167  -0.1176 0.1884 -0.0294 114 LEU A N     
931   C  CA    . LEU A 114 ? 0.679  0.2587 0.1677 -0.1196 0.1887 -0.03   114 LEU A CA    
932   C  C     . LEU A 114 ? 0.6859 0.2554 0.1712 -0.1143 0.1905 -0.0307 114 LEU A C     
933   O  O     . LEU A 114 ? 0.6956 0.258  0.1773 -0.1124 0.1919 -0.0311 114 LEU A O     
934   C  CB    . LEU A 114 ? 0.6851 0.2578 0.163  -0.1268 0.189  -0.0305 114 LEU A CB    
935   C  CG    . LEU A 114 ? 0.6963 0.2788 0.1763 -0.1332 0.1872 -0.0295 114 LEU A CG    
936   C  CD1   . LEU A 114 ? 0.7065 0.2806 0.175  -0.1404 0.1875 -0.0301 114 LEU A CD1   
937   C  CD2   . LEU A 114 ? 0.7001 0.2929 0.1861 -0.134  0.1853 -0.0285 114 LEU A CD2   
938   N  N     . GLN A 115 ? 0.6769 0.2464 0.164  -0.1115 0.1906 -0.0306 115 GLN A N     
939   C  CA    . GLN A 115 ? 0.6786 0.2394 0.1631 -0.1063 0.1925 -0.0308 115 GLN A CA    
940   C  C     . GLN A 115 ? 0.6817 0.2294 0.1528 -0.1097 0.1943 -0.0315 115 GLN A C     
941   O  O     . GLN A 115 ? 0.6907 0.2345 0.1578 -0.11   0.1948 -0.0316 115 GLN A O     
942   C  CB    . GLN A 115 ? 0.6946 0.2607 0.1862 -0.1023 0.192  -0.0302 115 GLN A CB    
943   C  CG    . GLN A 115 ? 0.7299 0.3091 0.2336 -0.1    0.1901 -0.0295 115 GLN A CG    
944   C  CD    . GLN A 115 ? 0.7787 0.3584 0.288  -0.0945 0.1904 -0.0291 115 GLN A CD    
945   O  OE1   . GLN A 115 ? 0.7963 0.3748 0.3086 -0.0899 0.191  -0.0287 115 GLN A OE1   
946   N  NE2   . GLN A 115 ? 0.773  0.3545 0.2837 -0.0949 0.19   -0.0292 115 GLN A NE2   
947   N  N     . ALA A 116 ? 0.6756 0.2163 0.1392 -0.1125 0.1953 -0.0321 116 ALA A N     
948   C  CA    . ALA A 116 ? 0.6865 0.2136 0.1361 -0.1162 0.1972 -0.0329 116 ALA A CA    
949   C  C     . ALA A 116 ? 0.6887 0.2036 0.1318 -0.1113 0.2003 -0.0328 116 ALA A C     
950   O  O     . ALA A 116 ? 0.6931 0.2052 0.1349 -0.1104 0.2011 -0.0329 116 ALA A O     
951   C  CB    . ALA A 116 ? 0.6933 0.22   0.1376 -0.1235 0.1965 -0.0334 116 ALA A CB    
952   N  N     . GLY A 117 ? 0.685  0.1931 0.1242 -0.1079 0.2021 -0.0325 117 GLY A N     
953   C  CA    . GLY A 117 ? 0.691  0.1878 0.124  -0.1026 0.2053 -0.0319 117 GLY A CA    
954   C  C     . GLY A 117 ? 0.6835 0.1853 0.1254 -0.0963 0.2053 -0.0309 117 GLY A C     
955   O  O     . GLY A 117 ? 0.6769 0.1873 0.1294 -0.0919 0.2042 -0.03   117 GLY A O     
956   N  N     . ASN A 118 ? 0.6855 0.1817 0.1228 -0.0961 0.2066 -0.031  118 ASN A N     
957   C  CA    . ASN A 118 ? 0.6878 0.1879 0.1323 -0.0904 0.2065 -0.03   118 ASN A CA    
958   C  C     . ASN A 118 ? 0.6712 0.185  0.1279 -0.091  0.2032 -0.0303 118 ASN A C     
959   O  O     . ASN A 118 ? 0.6698 0.1881 0.1336 -0.0863 0.2026 -0.0294 118 ASN A O     
960   C  CB    . ASN A 118 ? 0.7239 0.2128 0.159  -0.089  0.2093 -0.0299 118 ASN A CB    
961   C  CG    . ASN A 118 ? 0.7973 0.2822 0.2253 -0.0952 0.2092 -0.0314 118 ASN A CG    
962   O  OD1   . ASN A 118 ? 0.8193 0.3117 0.251  -0.1005 0.2068 -0.0323 118 ASN A OD1   
963   N  ND2   . ASN A 118 ? 0.8207 0.2938 0.2383 -0.0944 0.2121 -0.0314 118 ASN A ND2   
964   N  N     . GLN A 119 ? 0.6582 0.1785 0.117  -0.0966 0.2012 -0.0312 119 GLN A N     
965   C  CA    . GLN A 119 ? 0.6479 0.181  0.1178 -0.0969 0.1984 -0.0311 119 GLN A CA    
966   C  C     . GLN A 119 ? 0.6406 0.1828 0.1215 -0.0924 0.197  -0.0302 119 GLN A C     
967   O  O     . GLN A 119 ? 0.6369 0.187  0.1264 -0.0901 0.1954 -0.0298 119 GLN A O     
968   C  CB    . GLN A 119 ? 0.6629 0.2015 0.1325 -0.1037 0.1969 -0.0317 119 GLN A CB    
969   C  CG    . GLN A 119 ? 0.7063 0.2493 0.1786 -0.1055 0.196  -0.0318 119 GLN A CG    
970   C  CD    . GLN A 119 ? 0.7566 0.3121 0.2411 -0.1028 0.1939 -0.0311 119 GLN A CD    
971   O  OE1   . GLN A 119 ? 0.7722 0.335  0.2633 -0.1017 0.1926 -0.0306 119 GLN A OE1   
972   N  NE2   . GLN A 119 ? 0.7621 0.3197 0.2493 -0.1016 0.1936 -0.0309 119 GLN A NE2   
973   N  N     . ALA A 120 ? 0.6408 0.1808 0.1206 -0.0909 0.1977 -0.0298 120 ALA A N     
974   C  CA    . ALA A 120 ? 0.6413 0.1885 0.1305 -0.0867 0.1968 -0.029  120 ALA A CA    
975   C  C     . ALA A 120 ? 0.6385 0.1862 0.1327 -0.0807 0.197  -0.0278 120 ALA A C     
976   O  O     . ALA A 120 ? 0.6314 0.1878 0.1354 -0.0781 0.1953 -0.0272 120 ALA A O     
977   C  CB    . ALA A 120 ? 0.6475 0.1899 0.1323 -0.0865 0.1981 -0.0287 120 ALA A CB    
978   N  N     . TRP A 121 ? 0.6419 0.1803 0.1292 -0.0786 0.1992 -0.0274 121 TRP A N     
979   C  CA    . TRP A 121 ? 0.6459 0.185  0.1376 -0.0731 0.1993 -0.026  121 TRP A CA    
980   C  C     . TRP A 121 ? 0.6564 0.1951 0.1476 -0.0732 0.1988 -0.0263 121 TRP A C     
981   O  O     . TRP A 121 ? 0.6584 0.1974 0.1524 -0.0689 0.1987 -0.0251 121 TRP A O     
982   C  CB    . TRP A 121 ? 0.6481 0.1786 0.1343 -0.0688 0.2023 -0.0245 121 TRP A CB    
983   C  CG    . TRP A 121 ? 0.6596 0.1773 0.1327 -0.0702 0.2053 -0.0248 121 TRP A CG    
984   C  CD1   . TRP A 121 ? 0.6733 0.185  0.1412 -0.0689 0.2066 -0.0246 121 TRP A CD1   
985   C  CD2   . TRP A 121 ? 0.6656 0.1737 0.1284 -0.0722 0.2078 -0.0252 121 TRP A CD2   
986   N  NE1   . TRP A 121 ? 0.6859 0.1847 0.1406 -0.0703 0.2098 -0.0249 121 TRP A NE1   
987   C  CE2   . TRP A 121 ? 0.6838 0.1798 0.1349 -0.0724 0.2106 -0.0253 121 TRP A CE2   
988   C  CE3   . TRP A 121 ? 0.6706 0.1785 0.1321 -0.0741 0.2079 -0.0255 121 TRP A CE3   
989   C  CZ2   . TRP A 121 ? 0.6985 0.1819 0.1364 -0.0745 0.2136 -0.0256 121 TRP A CZ2   
990   C  CZ3   . TRP A 121 ? 0.688  0.1837 0.1367 -0.0762 0.2106 -0.026  121 TRP A CZ3   
991   C  CH2   . TRP A 121 ? 0.6981 0.1815 0.1349 -0.0766 0.2134 -0.0261 121 TRP A CH2   
992   N  N     . GLN A 122 ? 0.6606 0.1994 0.1487 -0.078  0.1981 -0.0277 122 GLN A N     
993   C  CA    . GLN A 122 ? 0.6709 0.2092 0.1582 -0.0783 0.1977 -0.028  122 GLN A CA    
994   C  C     . GLN A 122 ? 0.6757 0.2225 0.1731 -0.0748 0.1954 -0.0273 122 GLN A C     
995   O  O     . GLN A 122 ? 0.6807 0.2252 0.1776 -0.072  0.1955 -0.0267 122 GLN A O     
996   C  CB    . GLN A 122 ? 0.6906 0.2302 0.1751 -0.0843 0.1972 -0.0294 122 GLN A CB    
997   C  CG    . GLN A 122 ? 0.7347 0.2741 0.2187 -0.0845 0.1968 -0.0297 122 GLN A CG    
998   C  CD    . GLN A 122 ? 0.7933 0.3328 0.2734 -0.0903 0.1968 -0.0306 122 GLN A CD    
999   O  OE1   . GLN A 122 ? 0.8137 0.3444 0.2842 -0.0932 0.1987 -0.0312 122 GLN A OE1   
1000  N  NE2   . GLN A 122 ? 0.8022 0.3517 0.2896 -0.0921 0.1948 -0.0306 122 GLN A NE2   
1001  N  N     . ARG A 123 ? 0.6712 0.2271 0.177  -0.0749 0.1934 -0.0273 123 ARG A N     
1002  C  CA    . ARG A 123 ? 0.6712 0.2343 0.1856 -0.0721 0.1913 -0.0267 123 ARG A CA    
1003  C  C     . ARG A 123 ? 0.6742 0.2401 0.1944 -0.068  0.1909 -0.0253 123 ARG A C     
1004  O  O     . ARG A 123 ? 0.6756 0.2489 0.2036 -0.067  0.1889 -0.025  123 ARG A O     
1005  C  CB    . ARG A 123 ? 0.6765 0.2477 0.1962 -0.0747 0.1894 -0.0274 123 ARG A CB    
1006  C  CG    . ARG A 123 ? 0.7052 0.2793 0.2243 -0.0787 0.1896 -0.028  123 ARG A CG    
1007  C  CD    . ARG A 123 ? 0.741  0.3117 0.253  -0.0836 0.1906 -0.0288 123 ARG A CD    
1008  N  NE    . ARG A 123 ? 0.7585 0.3365 0.275  -0.0853 0.1892 -0.0288 123 ARG A NE    
1009  C  CZ    . ARG A 123 ? 0.7782 0.3587 0.293  -0.0895 0.1893 -0.0291 123 ARG A CZ    
1010  N  NH1   . ARG A 123 ? 0.7678 0.3428 0.2749 -0.0936 0.1905 -0.0296 123 ARG A NH1   
1011  N  NH2   . ARG A 123 ? 0.7775 0.3655 0.2976 -0.0897 0.1883 -0.0286 123 ARG A NH2   
1012  N  N     . SER A 124 ? 0.674  0.2337 0.19   -0.0657 0.1929 -0.0244 124 SER A N     
1013  C  CA    . SER A 124 ? 0.6769 0.2392 0.1983 -0.0616 0.1928 -0.0226 124 SER A CA    
1014  C  C     . SER A 124 ? 0.6775 0.2415 0.2027 -0.0579 0.1916 -0.0212 124 SER A C     
1015  O  O     . SER A 124 ? 0.6749 0.244  0.207  -0.0551 0.1904 -0.0197 124 SER A O     
1016  C  CB    . SER A 124 ? 0.6993 0.2547 0.215  -0.0601 0.1957 -0.0217 124 SER A CB    
1017  O  OG    . SER A 124 ? 0.7284 0.2849 0.2436 -0.0627 0.1959 -0.0226 124 SER A OG    
1018  N  N     . GLY A 125 ? 0.6796 0.2396 0.2003 -0.0581 0.1918 -0.0215 125 GLY A N     
1019  C  CA    . GLY A 125 ? 0.6865 0.2479 0.21   -0.055  0.1904 -0.0202 125 GLY A CA    
1020  C  C     . GLY A 125 ? 0.6867 0.2565 0.2186 -0.0552 0.1871 -0.0203 125 GLY A C     
1021  O  O     . GLY A 125 ? 0.6863 0.2598 0.2235 -0.0524 0.1856 -0.0186 125 GLY A O     
1022  N  N     . ARG A 126 ? 0.6844 0.2574 0.2176 -0.0586 0.1861 -0.0221 126 ARG A N     
1023  C  CA    . ARG A 126 ? 0.6857 0.2657 0.226  -0.0587 0.1833 -0.0222 126 ARG A CA    
1024  C  C     . ARG A 126 ? 0.6876 0.2727 0.2344 -0.0574 0.1827 -0.0213 126 ARG A C     
1025  O  O     . ARG A 126 ? 0.6884 0.2776 0.2406 -0.0559 0.1806 -0.0203 126 ARG A O     
1026  C  CB    . ARG A 126 ? 0.6997 0.2816 0.2394 -0.062  0.1827 -0.0239 126 ARG A CB    
1027  C  CG    . ARG A 126 ? 0.7308 0.3123 0.2676 -0.0651 0.1844 -0.025  126 ARG A CG    
1028  C  CD    . ARG A 126 ? 0.7573 0.3399 0.2924 -0.0681 0.1841 -0.0261 126 ARG A CD    
1029  N  NE    . ARG A 126 ? 0.7812 0.3574 0.3097 -0.0686 0.1852 -0.0265 126 ARG A NE    
1030  C  CZ    . ARG A 126 ? 0.8037 0.3775 0.3272 -0.0719 0.1864 -0.0273 126 ARG A CZ    
1031  N  NH1   . ARG A 126 ? 0.7976 0.3754 0.3221 -0.075  0.1867 -0.0278 126 ARG A NH1   
1032  N  NH2   . ARG A 126 ? 0.8064 0.3739 0.3236 -0.0722 0.1875 -0.0276 126 ARG A NH2   
1033  N  N     . ALA A 127 ? 0.6883 0.2728 0.2343 -0.058  0.1844 -0.0214 127 ALA A N     
1034  C  CA    . ALA A 127 ? 0.6944 0.2835 0.2464 -0.0566 0.1841 -0.0204 127 ALA A CA    
1035  C  C     . ALA A 127 ? 0.6969 0.2861 0.2517 -0.0528 0.184  -0.018  127 ALA A C     
1036  O  O     . ALA A 127 ? 0.6957 0.2904 0.2574 -0.0515 0.1823 -0.0169 127 ALA A O     
1037  C  CB    . ALA A 127 ? 0.7007 0.2878 0.2499 -0.0578 0.1862 -0.0209 127 ALA A CB    
1038  N  N     . TYR A 128 ? 0.697  0.2805 0.2465 -0.051  0.1857 -0.017  128 TYR A N     
1039  C  CA    . TYR A 128 ? 0.6975 0.2815 0.2495 -0.047  0.1859 -0.0142 128 TYR A CA    
1040  C  C     . TYR A 128 ? 0.6917 0.2801 0.2483 -0.0463 0.1828 -0.0134 128 TYR A C     
1041  O  O     . TYR A 128 ? 0.6903 0.2842 0.2536 -0.0446 0.1812 -0.0115 128 TYR A O     
1042  C  CB    . TYR A 128 ? 0.7041 0.2799 0.2481 -0.045  0.1891 -0.0133 128 TYR A CB    
1043  C  CG    . TYR A 128 ? 0.7141 0.2908 0.2601 -0.0407 0.1891 -0.0101 128 TYR A CG    
1044  C  CD1   . TYR A 128 ? 0.7218 0.3026 0.2735 -0.0375 0.1896 -0.0073 128 TYR A CD1   
1045  C  CD2   . TYR A 128 ? 0.7286 0.3033 0.2719 -0.0397 0.1884 -0.0096 128 TYR A CD2   
1046  C  CE1   . TYR A 128 ? 0.7318 0.315  0.2864 -0.0336 0.1893 -0.004  128 TYR A CE1   
1047  C  CE2   . TYR A 128 ? 0.7391 0.316  0.2851 -0.0358 0.188  -0.0064 128 TYR A CE2   
1048  C  CZ    . TYR A 128 ? 0.7463 0.3278 0.2981 -0.0328 0.1885 -0.0035 128 TYR A CZ    
1049  O  OH    . TYR A 128 ? 0.7639 0.3485 0.3188 -0.0288 0.1881 0.0002  128 TYR A OH    
1050  N  N     . SER A 129 ? 0.6844 0.27   0.2369 -0.0476 0.182  -0.0146 129 SER A N     
1051  C  CA    . SER A 129 ? 0.6783 0.2666 0.2334 -0.047  0.1791 -0.0139 129 SER A CA    
1052  C  C     . SER A 129 ? 0.672  0.2664 0.2334 -0.0487 0.1762 -0.0145 129 SER A C     
1053  O  O     . SER A 129 ? 0.6722 0.2708 0.2386 -0.0475 0.1739 -0.0128 129 SER A O     
1054  C  CB    . SER A 129 ? 0.6949 0.2779 0.2434 -0.048  0.1793 -0.0153 129 SER A CB    
1055  O  OG    . SER A 129 ? 0.7204 0.3021 0.2663 -0.0514 0.1797 -0.0179 129 SER A OG    
1056  N  N     . VAL A 130 ? 0.6649 0.26   0.2261 -0.0515 0.1763 -0.0167 130 VAL A N     
1057  C  CA    . VAL A 130 ? 0.6599 0.2599 0.2262 -0.0529 0.174  -0.0173 130 VAL A CA    
1058  C  C     . VAL A 130 ? 0.6557 0.2605 0.2284 -0.0517 0.1738 -0.0158 130 VAL A C     
1059  O  O     . VAL A 130 ? 0.656  0.2648 0.2336 -0.0518 0.1714 -0.015  130 VAL A O     
1060  C  CB    . VAL A 130 ? 0.6681 0.2678 0.2323 -0.0556 0.1746 -0.0197 130 VAL A CB    
1061  C  CG1   . VAL A 130 ? 0.6739 0.2781 0.2427 -0.0566 0.1728 -0.02   130 VAL A CG1   
1062  C  CG2   . VAL A 130 ? 0.6766 0.2721 0.235  -0.0567 0.1746 -0.0208 130 VAL A CG2   
1063  N  N     . GLY A 131 ? 0.6502 0.254  0.2224 -0.0507 0.1763 -0.0154 131 GLY A N     
1064  C  CA    . GLY A 131 ? 0.6481 0.2558 0.2259 -0.0493 0.1766 -0.0138 131 GLY A CA    
1065  C  C     . GLY A 131 ? 0.6425 0.2537 0.2252 -0.0469 0.1752 -0.0109 131 GLY A C     
1066  O  O     . GLY A 131 ? 0.6406 0.2568 0.2295 -0.0467 0.1741 -0.0098 131 GLY A O     
1067  N  N     . ARG A 132 ? 0.6376 0.2466 0.2178 -0.0452 0.1751 -0.0094 132 ARG A N     
1068  C  CA    . ARG A 132 ? 0.631  0.2442 0.2161 -0.0428 0.1736 -0.0061 132 ARG A CA    
1069  C  C     . ARG A 132 ? 0.6314 0.2486 0.22   -0.0447 0.1694 -0.0061 132 ARG A C     
1070  O  O     . ARG A 132 ? 0.6318 0.2534 0.2249 -0.0435 0.1675 -0.0033 132 ARG A O     
1071  C  CB    . ARG A 132 ? 0.6345 0.2442 0.2156 -0.0397 0.1754 -0.0041 132 ARG A CB    
1072  C  CG    . ARG A 132 ? 0.6417 0.2476 0.2175 -0.0403 0.1743 -0.0051 132 ARG A CG    
1073  C  CD    . ARG A 132 ? 0.6465 0.247  0.2165 -0.0373 0.177  -0.0036 132 ARG A CD    
1074  N  NE    . ARG A 132 ? 0.638  0.2423 0.212  -0.0333 0.1775 0.0005  132 ARG A NE    
1075  C  CZ    . ARG A 132 ? 0.6249 0.2333 0.202  -0.0319 0.1751 0.0031  132 ARG A CZ    
1076  N  NH1   . ARG A 132 ? 0.6104 0.223  0.1915 -0.0282 0.1758 0.0073  132 ARG A NH1   
1077  N  NH2   . ARG A 132 ? 0.6038 0.2125 0.18   -0.0341 0.1719 0.0017  132 ARG A NH2   
1078  N  N     . THR A 133 ? 0.6287 0.2444 0.2152 -0.0477 0.1681 -0.0089 133 THR A N     
1079  C  CA    . THR A 133 ? 0.6295 0.2472 0.2175 -0.0496 0.1644 -0.0091 133 THR A CA    
1080  C  C     . THR A 133 ? 0.6362 0.2586 0.23   -0.0512 0.1628 -0.0089 133 THR A C     
1081  O  O     . THR A 133 ? 0.6393 0.2635 0.2347 -0.0528 0.1596 -0.0085 133 THR A O     
1082  C  CB    . THR A 133 ? 0.64   0.253  0.2221 -0.0517 0.1642 -0.012  133 THR A CB    
1083  O  OG1   . THR A 133 ? 0.6469 0.2593 0.2283 -0.0531 0.1659 -0.0142 133 THR A OG1   
1084  C  CG2   . THR A 133 ? 0.6498 0.2578 0.2258 -0.0506 0.1656 -0.0124 133 THR A CG2   
1085  N  N     . GLY A 134 ? 0.6341 0.2577 0.23   -0.051  0.1649 -0.0095 134 GLY A N     
1086  C  CA    . GLY A 134 ? 0.6347 0.2619 0.2353 -0.0525 0.1638 -0.0096 134 GLY A CA    
1087  C  C     . GLY A 134 ? 0.6351 0.2598 0.2325 -0.0546 0.1642 -0.0126 134 GLY A C     
1088  O  O     . GLY A 134 ? 0.6356 0.2623 0.2358 -0.0556 0.1641 -0.013  134 GLY A O     
1089  N  N     . TYR A 135 ? 0.6327 0.2531 0.2242 -0.0552 0.1648 -0.0144 135 TYR A N     
1090  C  CA    . TYR A 135 ? 0.636  0.2544 0.2243 -0.0568 0.1656 -0.0168 135 TYR A CA    
1091  C  C     . TYR A 135 ? 0.6337 0.252  0.2212 -0.0564 0.1687 -0.0177 135 TYR A C     
1092  O  O     . TYR A 135 ? 0.6341 0.2507 0.2195 -0.0554 0.1703 -0.0175 135 TYR A O     
1093  C  CB    . TYR A 135 ? 0.6419 0.2561 0.2244 -0.0577 0.1648 -0.018  135 TYR A CB    
1094  C  CG    . TYR A 135 ? 0.6561 0.2695 0.2382 -0.0584 0.1616 -0.0173 135 TYR A CG    
1095  C  CD1   . TYR A 135 ? 0.6695 0.2839 0.2532 -0.0599 0.1598 -0.0174 135 TYR A CD1   
1096  C  CD2   . TYR A 135 ? 0.6716 0.2827 0.2508 -0.0579 0.1604 -0.0167 135 TYR A CD2   
1097  C  CE1   . TYR A 135 ? 0.6838 0.2968 0.2662 -0.0611 0.1566 -0.0168 135 TYR A CE1   
1098  C  CE2   . TYR A 135 ? 0.6854 0.2957 0.2638 -0.0588 0.1571 -0.016  135 TYR A CE2   
1099  C  CZ    . TYR A 135 ? 0.6989 0.3101 0.2788 -0.0607 0.1551 -0.0161 135 TYR A CZ    
1100  O  OH    . TYR A 135 ? 0.7235 0.3333 0.3016 -0.0621 0.1517 -0.0155 135 TYR A OH    
1101  N  N     . PRO A 136 ? 0.6285 0.2486 0.2174 -0.0571 0.1696 -0.0187 136 PRO A N     
1102  C  CA    . PRO A 136 ? 0.6265 0.2472 0.2149 -0.0569 0.1722 -0.0194 136 PRO A CA    
1103  C  C     . PRO A 136 ? 0.624  0.2416 0.2069 -0.0578 0.1736 -0.0206 136 PRO A C     
1104  O  O     . PRO A 136 ? 0.6234 0.2392 0.2031 -0.0588 0.173  -0.0215 136 PRO A O     
1105  C  CB    . PRO A 136 ? 0.6374 0.2606 0.2279 -0.0576 0.1725 -0.0201 136 PRO A CB    
1106  C  CG    . PRO A 136 ? 0.6419 0.2661 0.2352 -0.0577 0.1703 -0.0193 136 PRO A CG    
1107  C  CD    . PRO A 136 ? 0.6208 0.2423 0.2115 -0.0581 0.1683 -0.019  136 PRO A CD    
1108  N  N     . TYR A 137 ? 0.6247 0.2415 0.2063 -0.0576 0.1757 -0.0207 137 TYR A N     
1109  C  CA    . TYR A 137 ? 0.6333 0.2471 0.2094 -0.0589 0.1771 -0.0217 137 TYR A CA    
1110  C  C     . TYR A 137 ? 0.6359 0.2514 0.2117 -0.06   0.1788 -0.0225 137 TYR A C     
1111  O  O     . TYR A 137 ? 0.6343 0.2503 0.2116 -0.0591 0.1798 -0.0219 137 TYR A O     
1112  C  CB    . TYR A 137 ? 0.6337 0.2431 0.2065 -0.0578 0.1779 -0.021  137 TYR A CB    
1113  C  CG    . TYR A 137 ? 0.645  0.2504 0.2115 -0.0595 0.1792 -0.0221 137 TYR A CG    
1114  C  CD1   . TYR A 137 ? 0.6609 0.264  0.2241 -0.0603 0.1785 -0.0227 137 TYR A CD1   
1115  C  CD2   . TYR A 137 ? 0.6594 0.2631 0.2228 -0.0606 0.1812 -0.0226 137 TYR A CD2   
1116  C  CE1   . TYR A 137 ? 0.6767 0.2762 0.2341 -0.0621 0.1798 -0.0237 137 TYR A CE1   
1117  C  CE2   . TYR A 137 ? 0.6761 0.2762 0.2334 -0.0629 0.1824 -0.0237 137 TYR A CE2   
1118  C  CZ    . TYR A 137 ? 0.6901 0.2881 0.2446 -0.0636 0.1817 -0.0241 137 TYR A CZ    
1119  O  OH    . TYR A 137 ? 0.7125 0.307  0.2611 -0.066  0.1829 -0.025  137 TYR A OH    
1120  N  N     . ILE A 138 ? 0.6354 0.2521 0.2092 -0.0619 0.1791 -0.0235 138 ILE A N     
1121  C  CA    . ILE A 138 ? 0.6366 0.256  0.2102 -0.0633 0.1804 -0.024  138 ILE A CA    
1122  C  C     . ILE A 138 ? 0.6401 0.2573 0.2083 -0.0657 0.1814 -0.0247 138 ILE A C     
1123  O  O     . ILE A 138 ? 0.6392 0.2562 0.2054 -0.0669 0.1812 -0.025  138 ILE A O     
1124  C  CB    . ILE A 138 ? 0.6397 0.2639 0.2163 -0.0633 0.1801 -0.0241 138 ILE A CB    
1125  C  CG1   . ILE A 138 ? 0.6467 0.272  0.2277 -0.0614 0.1789 -0.0235 138 ILE A CG1   
1126  C  CG2   . ILE A 138 ? 0.6453 0.2733 0.2226 -0.0644 0.1813 -0.0242 138 ILE A CG2   
1127  C  CD1   . ILE A 138 ? 0.658  0.2841 0.2423 -0.0601 0.1791 -0.0228 138 ILE A CD1   
1128  N  N     . TYR A 139 ? 0.6434 0.2587 0.209  -0.0667 0.1827 -0.0248 139 TYR A N     
1129  C  CA    . TYR A 139 ? 0.6535 0.2661 0.2133 -0.0697 0.1836 -0.0254 139 TYR A CA    
1130  C  C     . TYR A 139 ? 0.6528 0.27   0.213  -0.0719 0.184  -0.0256 139 TYR A C     
1131  O  O     . TYR A 139 ? 0.6517 0.2689 0.2121 -0.0718 0.1847 -0.0255 139 TYR A O     
1132  C  CB    . TYR A 139 ? 0.6622 0.2679 0.2172 -0.0693 0.1848 -0.0253 139 TYR A CB    
1133  C  CG    . TYR A 139 ? 0.6829 0.284  0.2305 -0.0725 0.1859 -0.0261 139 TYR A CG    
1134  C  CD1   . TYR A 139 ? 0.697  0.2983 0.2425 -0.0746 0.1855 -0.0266 139 TYR A CD1   
1135  C  CD2   . TYR A 139 ? 0.6996 0.2952 0.2418 -0.0734 0.1874 -0.0262 139 TYR A CD2   
1136  C  CE1   . TYR A 139 ? 0.7125 0.3092 0.2511 -0.0779 0.1865 -0.0272 139 TYR A CE1   
1137  C  CE2   . TYR A 139 ? 0.717  0.3074 0.2516 -0.0767 0.1884 -0.0269 139 TYR A CE2   
1138  C  CZ    . TYR A 139 ? 0.7297 0.3208 0.2626 -0.0792 0.1879 -0.0274 139 TYR A CZ    
1139  O  OH    . TYR A 139 ? 0.7548 0.3406 0.28   -0.0829 0.1889 -0.028  139 TYR A OH    
1140  N  N     . ILE A 140 ? 0.6492 0.2705 0.2097 -0.0738 0.1838 -0.0256 140 ILE A N     
1141  C  CA    . ILE A 140 ? 0.6481 0.2753 0.2096 -0.0759 0.184  -0.0253 140 ILE A CA    
1142  C  C     . ILE A 140 ? 0.656  0.2813 0.2118 -0.08   0.1845 -0.0257 140 ILE A C     
1143  O  O     . ILE A 140 ? 0.6592 0.283  0.2123 -0.0816 0.1846 -0.0258 140 ILE A O     
1144  C  CB    . ILE A 140 ? 0.6462 0.2796 0.2117 -0.075  0.1837 -0.0247 140 ILE A CB    
1145  C  CG1   . ILE A 140 ? 0.6496 0.2835 0.2195 -0.0714 0.1832 -0.0245 140 ILE A CG1   
1146  C  CG2   . ILE A 140 ? 0.6498 0.2903 0.2168 -0.0768 0.1841 -0.0239 140 ILE A CG2   
1147  C  CD1   . ILE A 140 ? 0.6563 0.2934 0.228  -0.0703 0.1831 -0.0239 140 ILE A CD1   
1148  N  N     . VAL A 141 ? 0.6554 0.2803 0.2089 -0.082  0.1849 -0.0258 141 VAL A N     
1149  C  CA    . VAL A 141 ? 0.6618 0.2839 0.2088 -0.0865 0.1852 -0.0261 141 VAL A CA    
1150  C  C     . VAL A 141 ? 0.6678 0.2964 0.2156 -0.0896 0.1848 -0.0256 141 VAL A C     
1151  O  O     . VAL A 141 ? 0.6667 0.2977 0.217  -0.0881 0.1848 -0.0253 141 VAL A O     
1152  C  CB    . VAL A 141 ? 0.6695 0.2814 0.2098 -0.0867 0.1862 -0.0269 141 VAL A CB    
1153  C  CG1   . VAL A 141 ? 0.674  0.284  0.2163 -0.0833 0.1867 -0.0268 141 VAL A CG1   
1154  C  CG2   . VAL A 141 ? 0.6763 0.2845 0.209  -0.0918 0.1866 -0.0274 141 VAL A CG2   
1155  N  N     . ASP A 142 ? 0.6725 0.3045 0.2182 -0.0937 0.1845 -0.0251 142 ASP A N     
1156  C  CA    . ASP A 142 ? 0.6808 0.3202 0.2272 -0.0973 0.1838 -0.0241 142 ASP A CA    
1157  C  C     . ASP A 142 ? 0.6896 0.3238 0.2299 -0.1003 0.1838 -0.0249 142 ASP A C     
1158  O  O     . ASP A 142 ? 0.6946 0.3204 0.2275 -0.103  0.1843 -0.0258 142 ASP A O     
1159  C  CB    . ASP A 142 ? 0.7063 0.3493 0.2512 -0.1014 0.1836 -0.0233 142 ASP A CB    
1160  C  CG    . ASP A 142 ? 0.7644 0.4196 0.315  -0.102  0.1831 -0.0213 142 ASP A CG    
1161  O  OD1   . ASP A 142 ? 0.7687 0.4288 0.3254 -0.0976 0.1834 -0.0205 142 ASP A OD1   
1162  O  OD2   . ASP A 142 ? 0.7936 0.4532 0.3423 -0.107  0.1824 -0.0203 142 ASP A OD2   
1163  N  N     . PHE A 143 ? 0.6892 0.3279 0.2317 -0.1    0.1834 -0.0244 143 PHE A N     
1164  C  CA    . PHE A 143 ? 0.7009 0.3348 0.2374 -0.1028 0.1833 -0.0249 143 PHE A CA    
1165  C  C     . PHE A 143 ? 0.7133 0.3567 0.2511 -0.1068 0.182  -0.0236 143 PHE A C     
1166  O  O     . PHE A 143 ? 0.712  0.3637 0.2564 -0.1041 0.1817 -0.0226 143 PHE A O     
1167  C  CB    . PHE A 143 ? 0.6958 0.3262 0.2339 -0.0981 0.1841 -0.0254 143 PHE A CB    
1168  C  CG    . PHE A 143 ? 0.7032 0.3269 0.2344 -0.1001 0.1845 -0.026  143 PHE A CG    
1169  C  CD1   . PHE A 143 ? 0.7088 0.3377 0.2402 -0.1022 0.1836 -0.0254 143 PHE A CD1   
1170  C  CD2   . PHE A 143 ? 0.7168 0.3285 0.2406 -0.0997 0.1858 -0.027  143 PHE A CD2   
1171  C  CE1   . PHE A 143 ? 0.7203 0.3421 0.2442 -0.1042 0.1839 -0.026  143 PHE A CE1   
1172  C  CE2   . PHE A 143 ? 0.7269 0.3313 0.2432 -0.1014 0.1865 -0.0275 143 PHE A CE2   
1173  C  CZ    . PHE A 143 ? 0.722  0.3312 0.2381 -0.1038 0.1854 -0.0271 143 PHE A CZ    
1174  N  N     . VAL A 144 ? 0.7245 0.3674 0.2564 -0.113  0.1811 -0.0235 144 VAL A N     
1175  C  CA    . VAL A 144 ? 0.7477 0.3807 0.2707 -0.117  0.1815 -0.0246 144 VAL A CA    
1176  C  C     . VAL A 144 ? 0.7667 0.4055 0.2897 -0.1219 0.1806 -0.0236 144 VAL A C     
1177  O  O     . VAL A 144 ? 0.762  0.4128 0.2912 -0.1228 0.1796 -0.0217 144 VAL A O     
1178  C  CB    . VAL A 144 ? 0.7618 0.3871 0.2755 -0.1211 0.1812 -0.0255 144 VAL A CB    
1179  C  CG1   . VAL A 144 ? 0.7736 0.3898 0.2849 -0.1165 0.1827 -0.0266 144 VAL A CG1   
1180  C  CG2   . VAL A 144 ? 0.7643 0.3991 0.2793 -0.1253 0.1793 -0.0241 144 VAL A CG2   
1181  N  N     . LYS A 145 ? 0.7875 0.4177 0.3031 -0.1251 0.1812 -0.0245 145 LYS A N     
1182  C  CA    . LYS A 145 ? 0.8088 0.4425 0.3228 -0.1305 0.1806 -0.0237 145 LYS A CA    
1183  C  C     . LYS A 145 ? 0.8364 0.4596 0.3385 -0.1369 0.1805 -0.0249 145 LYS A C     
1184  O  O     . LYS A 145 ? 0.8425 0.4529 0.3373 -0.1354 0.1819 -0.0266 145 LYS A O     
1185  C  CB    . LYS A 145 ? 0.8348 0.4676 0.3517 -0.1273 0.1817 -0.0237 145 LYS A CB    
1186  C  CG    . LYS A 145 ? 0.8841 0.5225 0.401  -0.1321 0.1813 -0.0224 145 LYS A CG    
1187  C  CD    . LYS A 145 ? 0.9345 0.5744 0.4561 -0.1282 0.1824 -0.022  145 LYS A CD    
1188  C  CE    . LYS A 145 ? 0.9844 0.6109 0.4996 -0.1264 0.1838 -0.0241 145 LYS A CE    
1189  N  NZ    . LYS A 145 ? 1.0176 0.6359 0.5229 -0.1326 0.1841 -0.0249 145 LYS A NZ    
1190  N  N     . TYR A 146 ? 0.8531 0.4814 0.3527 -0.144  0.179  -0.0237 146 TYR A N     
1191  C  CA    . TYR A 146 ? 0.8874 0.5057 0.3749 -0.151  0.1788 -0.0248 146 TYR A CA    
1192  C  C     . TYR A 146 ? 0.9191 0.5303 0.4011 -0.1535 0.18   -0.0254 146 TYR A C     
1193  O  O     . TYR A 146 ? 0.9197 0.5381 0.408  -0.1526 0.1801 -0.0243 146 TYR A O     
1194  C  CB    . TYR A 146 ? 0.8866 0.514  0.3735 -0.1584 0.1762 -0.0231 146 TYR A CB    
1195  C  CG    . TYR A 146 ? 0.8976 0.5275 0.3849 -0.158  0.175  -0.0229 146 TYR A CG    
1196  C  CD1   . TYR A 146 ? 0.9036 0.5459 0.4019 -0.1532 0.1744 -0.0214 146 TYR A CD1   
1197  C  CD2   . TYR A 146 ? 0.9152 0.5349 0.3912 -0.1627 0.1745 -0.0242 146 TYR A CD2   
1198  C  CE1   . TYR A 146 ? 0.9145 0.5592 0.413  -0.1527 0.1734 -0.0212 146 TYR A CE1   
1199  C  CE2   . TYR A 146 ? 0.9266 0.5483 0.4024 -0.1624 0.1734 -0.024  146 TYR A CE2   
1200  C  CZ    . TYR A 146 ? 0.932  0.5666 0.4194 -0.1574 0.1728 -0.0225 146 TYR A CZ    
1201  O  OH    . TYR A 146 ? 0.9522 0.5889 0.4396 -0.1569 0.1718 -0.0223 146 TYR A OH    
1202  N  N     . GLU A 147 ? 0.9436 0.5401 0.413  -0.1571 0.181  -0.0272 147 GLU A N     
1203  C  CA    . GLU A 147 ? 0.9687 0.5574 0.4311 -0.1605 0.1821 -0.0278 147 GLU A CA    
1204  C  C     . GLU A 147 ? 0.983  0.5775 0.4424 -0.1699 0.1801 -0.0265 147 GLU A C     
1205  O  O     . GLU A 147 ? 0.9858 0.5821 0.442  -0.1746 0.1783 -0.0262 147 GLU A O     
1206  C  CB    . GLU A 147 ? 1.011  0.5807 0.46   -0.1603 0.1844 -0.0301 147 GLU A CB    
1207  C  CG    . GLU A 147 ? 1.0735 0.6341 0.5154 -0.1624 0.1862 -0.0308 147 GLU A CG    
1208  C  CD    . GLU A 147 ? 1.1545 0.6976 0.58   -0.1669 0.1878 -0.0324 147 GLU A CD    
1209  O  OE1   . GLU A 147 ? 1.1642 0.7002 0.5831 -0.1699 0.1891 -0.0329 147 GLU A OE1   
1210  O  OE2   . GLU A 147 ? 1.1853 0.7212 0.6041 -0.1674 0.188  -0.0332 147 GLU A OE2   
1211  N  N     . LEU A 148 ? 0.99   0.5874 0.4503 -0.1728 0.1803 -0.0257 148 LEU A N     
1212  C  CA    . LEU A 148 ? 1.005  0.6082 0.4626 -0.1821 0.1784 -0.0242 148 LEU A CA    
1213  C  C     . LEU A 148 ? 1.0299 0.6183 0.4738 -0.188  0.1797 -0.0258 148 LEU A C     
1214  O  O     . LEU A 148 ? 1.0393 0.6157 0.4784 -0.1839 0.1824 -0.0275 148 LEU A O     
1215  C  CB    . LEU A 148 ? 0.9995 0.6197 0.4693 -0.1818 0.1776 -0.0214 148 LEU A CB    
1216  C  CG    . LEU A 148 ? 1.0117 0.6459 0.4946 -0.1754 0.1768 -0.0197 148 LEU A CG    
1217  C  CD1   . LEU A 148 ? 1.0116 0.66   0.5053 -0.1739 0.1768 -0.0169 148 LEU A CD1   
1218  C  CD2   . LEU A 148 ? 1.0172 0.6581 0.5007 -0.1788 0.1744 -0.0187 148 LEU A CD2   
1219  N  N     . ASN A 149 ? 1.0393 0.6277 0.4761 -0.1977 0.1779 -0.0251 149 ASN A N     
1220  C  CA    . ASN A 149 ? 1.064  0.6371 0.4863 -0.204  0.1792 -0.0267 149 ASN A CA    
1221  C  C     . ASN A 149 ? 1.0723 0.6472 0.4959 -0.2061 0.1803 -0.0259 149 ASN A C     
1222  O  O     . ASN A 149 ? 1.0848 0.6457 0.4965 -0.2099 0.182  -0.0274 149 ASN A O     
1223  C  CB    . ASN A 149 ? 1.087  0.6572 0.4993 -0.2141 0.1769 -0.0266 149 ASN A CB    
1224  C  CG    . ASN A 149 ? 1.1229 0.7109 0.5428 -0.2211 0.1736 -0.0235 149 ASN A CG    
1225  O  OD1   . ASN A 149 ? 1.1245 0.7287 0.5584 -0.2177 0.173  -0.0211 149 ASN A OD1   
1226  N  ND2   . ASN A 149 ? 1.1387 0.724  0.5492 -0.2311 0.1713 -0.0232 149 ASN A ND2   
1227  N  N     . ASN A 150 ? 1.0623 0.6541 0.4999 -0.2036 0.1794 -0.0234 150 ASN A N     
1228  C  CA    . ASN A 150 ? 1.0653 0.6621 0.5068 -0.2048 0.1804 -0.022  150 ASN A CA    
1229  C  C     . ASN A 150 ? 1.066  0.6655 0.5021 -0.216  0.1788 -0.0205 150 ASN A C     
1230  O  O     . ASN A 150 ? 1.0609 0.6726 0.505  -0.2177 0.1785 -0.0179 150 ASN A O     
1231  C  CB    . ASN A 150 ? 1.0895 0.6733 0.5267 -0.1991 0.1837 -0.0241 150 ASN A CB    
1232  C  CG    . ASN A 150 ? 1.1271 0.7195 0.5769 -0.1897 0.1846 -0.0233 150 ASN A CG    
1233  O  OD1   . ASN A 150 ? 1.1394 0.7387 0.5974 -0.1838 0.1839 -0.0229 150 ASN A OD1   
1234  N  ND2   . ASN A 150 ? 1.1342 0.7255 0.585  -0.1883 0.1863 -0.023  150 ASN A ND2   
1235  N  N     . SER A 151 ? 1.0701 0.6588 0.493  -0.2239 0.1779 -0.0218 151 SER A N     
1236  C  CA    . SER A 151 ? 1.0746 0.6658 0.492  -0.2354 0.1761 -0.0203 151 SER A CA    
1237  C  C     . SER A 151 ? 1.0635 0.6766 0.4928 -0.2391 0.1726 -0.0165 151 SER A C     
1238  O  O     . SER A 151 ? 1.06   0.684  0.494  -0.2444 0.1717 -0.0137 151 SER A O     
1239  C  CB    . SER A 151 ? 1.1052 0.6791 0.505  -0.2427 0.1759 -0.0227 151 SER A CB    
1240  O  OG    . SER A 151 ? 1.1352 0.7108 0.5345 -0.2427 0.1738 -0.023  151 SER A OG    
1241  N  N     . ASP A 152 ? 1.0568 0.677  0.4916 -0.2358 0.1709 -0.0161 152 ASP A N     
1242  C  CA    . ASP A 152 ? 1.0495 0.691  0.4962 -0.2381 0.1678 -0.0122 152 ASP A CA    
1243  C  C     . ASP A 152 ? 1.0389 0.6908 0.4983 -0.228  0.1679 -0.0114 152 ASP A C     
1244  O  O     . ASP A 152 ? 1.0329 0.7005 0.5006 -0.229  0.1654 -0.0086 152 ASP A O     
1245  C  CB    . ASP A 152 ? 1.0765 0.7187 0.5154 -0.2487 0.1643 -0.0115 152 ASP A CB    
1246  C  CG    . ASP A 152 ? 1.1392 0.7707 0.5702 -0.2473 0.1637 -0.0141 152 ASP A CG    
1247  O  OD1   . ASP A 152 ? 1.1609 0.7721 0.5781 -0.2476 0.1656 -0.0176 152 ASP A OD1   
1248  O  OD2   . ASP A 152 ? 1.1569 0.8002 0.5952 -0.2459 0.1614 -0.0125 152 ASP A OD2   
1249  N  N     . ARG A 153 ? 1.0343 0.6776 0.4949 -0.2183 0.1707 -0.0138 153 ARG A N     
1250  C  CA    . ARG A 153 ? 1.0282 0.6787 0.4997 -0.2083 0.1713 -0.0135 153 ARG A CA    
1251  C  C     . ARG A 153 ? 1.021  0.6738 0.4926 -0.2078 0.1694 -0.0138 153 ARG A C     
1252  O  O     . ARG A 153 ? 1.0154 0.6802 0.4979 -0.2021 0.1689 -0.0121 153 ARG A O     
1253  C  CB    . ARG A 153 ? 1.0381 0.7068 0.5239 -0.2048 0.1714 -0.0099 153 ARG A CB    
1254  C  CG    . ARG A 153 ? 1.0783 0.7451 0.5706 -0.1942 0.1741 -0.0109 153 ARG A CG    
1255  C  CD    . ARG A 153 ? 1.1043 0.7878 0.6095 -0.1907 0.1745 -0.0072 153 ARG A CD    
1256  N  NE    . ARG A 153 ? 1.1282 0.809  0.6386 -0.1808 0.1769 -0.0082 153 ARG A NE    
1257  C  CZ    . ARG A 153 ? 1.1399 0.8259 0.6576 -0.1735 0.177  -0.008  153 ARG A CZ    
1258  N  NH1   . ARG A 153 ? 1.1274 0.8218 0.6484 -0.1745 0.1751 -0.0067 153 ARG A NH1   
1259  N  NH2   . ARG A 153 ? 1.1366 0.8192 0.658  -0.1654 0.1791 -0.009  153 ARG A NH2   
1260  N  N     . SER A 154 ? 1.0184 0.6589 0.4773 -0.2136 0.1684 -0.0158 154 SER A N     
1261  C  CA    . SER A 154 ? 1.0125 0.6531 0.47   -0.2132 0.1668 -0.0163 154 SER A CA    
1262  C  C     . SER A 154 ? 1.0048 0.6321 0.4593 -0.2045 0.1693 -0.0194 154 SER A C     
1263  O  O     . SER A 154 ? 1.013  0.6277 0.4625 -0.2013 0.172  -0.0215 154 SER A O     
1264  C  CB    . SER A 154 ? 1.0377 0.6715 0.4824 -0.2238 0.1645 -0.0167 154 SER A CB    
1265  O  OG    . SER A 154 ? 1.0803 0.6931 0.51   -0.2261 0.1665 -0.02   154 SER A OG    
1266  N  N     . ARG A 155 ? 0.9885 0.619  0.4463 -0.2007 0.1685 -0.0194 155 ARG A N     
1267  C  CA    . ARG A 155 ? 0.9841 0.6039 0.4405 -0.1923 0.1707 -0.0219 155 ARG A CA    
1268  C  C     . ARG A 155 ? 0.9792 0.5791 0.4201 -0.1944 0.1719 -0.0247 155 ARG A C     
1269  O  O     . ARG A 155 ? 0.9842 0.5799 0.416  -0.2015 0.1702 -0.0249 155 ARG A O     
1270  C  CB    . ARG A 155 ? 0.9949 0.6256 0.4611 -0.1868 0.1697 -0.0207 155 ARG A CB    
1271  C  CG    . ARG A 155 ? 1.0225 0.6693 0.5037 -0.1814 0.1698 -0.0184 155 ARG A CG    
1272  C  CD    . ARG A 155 ? 1.057  0.7143 0.5466 -0.177  0.1688 -0.0171 155 ARG A CD    
1273  N  NE    . ARG A 155 ? 1.0884 0.7613 0.5914 -0.1723 0.169  -0.0145 155 ARG A NE    
1274  C  CZ    . ARG A 155 ? 1.1171 0.8058 0.6268 -0.1759 0.1672 -0.0111 155 ARG A CZ    
1275  N  NH1   . ARG A 155 ? 1.1184 0.8103 0.623  -0.1847 0.1647 -0.0099 155 ARG A NH1   
1276  N  NH2   . ARG A 155 ? 1.1111 0.8125 0.6322 -0.1706 0.168  -0.0087 155 ARG A NH2   
1277  N  N     . LYS A 156 ? 0.9659 0.5537 0.4041 -0.1876 0.175  -0.0268 156 LYS A N     
1278  C  CA    . LYS A 156 ? 0.9642 0.5326 0.3886 -0.187  0.1771 -0.0292 156 LYS A CA    
1279  C  C     . LYS A 156 ? 0.9422 0.5098 0.3716 -0.1782 0.1782 -0.0298 156 LYS A C     
1280  O  O     . LYS A 156 ? 0.9324 0.5138 0.3753 -0.1731 0.1774 -0.0285 156 LYS A O     
1281  C  CB    . LYS A 156 ? 0.9967 0.5521 0.414  -0.186  0.1801 -0.0307 156 LYS A CB    
1282  C  CG    . LYS A 156 ? 1.0516 0.6053 0.4618 -0.1952 0.1792 -0.0304 156 LYS A CG    
1283  C  CD    . LYS A 156 ? 1.1096 0.6575 0.519  -0.1928 0.1818 -0.031  156 LYS A CD    
1284  C  CE    . LYS A 156 ? 1.1724 0.699  0.5668 -0.1919 0.1851 -0.0333 156 LYS A CE    
1285  N  NZ    . LYS A 156 ? 1.206  0.728  0.6    -0.1894 0.1874 -0.0337 156 LYS A NZ    
1286  N  N     . ASN A 157 ? 0.9322 0.4839 0.3507 -0.1764 0.1803 -0.0316 157 ASN A N     
1287  C  CA    . ASN A 157 ? 0.9174 0.4679 0.3399 -0.1686 0.1814 -0.0319 157 ASN A CA    
1288  C  C     . ASN A 157 ? 0.8829 0.4408 0.3187 -0.1594 0.1827 -0.0314 157 ASN A C     
1289  O  O     . ASN A 157 ? 0.8833 0.4394 0.3205 -0.1575 0.184  -0.0317 157 ASN A O     
1290  C  CB    . ASN A 157 ? 0.9489 0.4797 0.3568 -0.1676 0.1841 -0.0336 157 ASN A CB    
1291  C  CG    . ASN A 157 ? 1.0019 0.5239 0.3956 -0.1762 0.1829 -0.0341 157 ASN A CG    
1292  O  OD1   . ASN A 157 ? 1.0274 0.5371 0.4082 -0.1817 0.1839 -0.0351 157 ASN A OD1   
1293  N  ND2   . ASN A 157 ? 1.0074 0.5352 0.4027 -0.1777 0.1808 -0.0336 157 ASN A ND2   
1294  N  N     . LEU A 158 ? 0.8517 0.4176 0.2965 -0.1541 0.1821 -0.0308 158 LEU A N     
1295  C  CA    . LEU A 158 ? 0.8274 0.4    0.2843 -0.1457 0.1831 -0.0303 158 LEU A CA    
1296  C  C     . LEU A 158 ? 0.814  0.3731 0.2659 -0.1402 0.1863 -0.0315 158 LEU A C     
1297  O  O     . LEU A 158 ? 0.8267 0.3724 0.2676 -0.1406 0.1879 -0.0325 158 LEU A O     
1298  C  CB    . LEU A 158 ? 0.8227 0.4036 0.2876 -0.1416 0.1822 -0.0296 158 LEU A CB    
1299  C  CG    . LEU A 158 ? 0.8311 0.4293 0.3064 -0.1433 0.1796 -0.0278 158 LEU A CG    
1300  C  CD1   . LEU A 158 ? 0.8315 0.4356 0.3134 -0.1386 0.1793 -0.0273 158 LEU A CD1   
1301  C  CD2   . LEU A 158 ? 0.8347 0.4426 0.3199 -0.1409 0.1795 -0.0268 158 LEU A CD2   
1302  N  N     . ARG A 159 ? 0.7881 0.3506 0.2478 -0.1348 0.1872 -0.0313 159 ARG A N     
1303  C  CA    . ARG A 159 ? 0.7771 0.3286 0.2333 -0.1292 0.19   -0.032  159 ARG A CA    
1304  C  C     . ARG A 159 ? 0.7599 0.3168 0.2265 -0.1213 0.1904 -0.0314 159 ARG A C     
1305  O  O     . ARG A 159 ? 0.7511 0.3202 0.229  -0.1191 0.189  -0.0306 159 ARG A O     
1306  C  CB    . ARG A 159 ? 0.7848 0.3333 0.2395 -0.1297 0.1908 -0.0323 159 ARG A CB    
1307  C  CG    . ARG A 159 ? 0.8086 0.3494 0.2516 -0.1375 0.1909 -0.033  159 ARG A CG    
1308  C  CD    . ARG A 159 ? 0.8358 0.3597 0.264  -0.1389 0.1931 -0.034  159 ARG A CD    
1309  N  NE    . ARG A 159 ? 0.8461 0.3576 0.2682 -0.1343 0.1964 -0.0345 159 ARG A NE    
1310  C  CZ    . ARG A 159 ? 0.8528 0.3592 0.2757 -0.1271 0.1985 -0.0342 159 ARG A CZ    
1311  N  NH1   . ARG A 159 ? 0.8475 0.3597 0.2771 -0.1236 0.1978 -0.0336 159 ARG A NH1   
1312  N  NH2   . ARG A 159 ? 0.844  0.3398 0.2611 -0.1232 0.2014 -0.0343 159 ARG A NH2   
1313  N  N     . PHE A 160 ? 0.7534 0.301  0.2157 -0.117  0.1925 -0.0316 160 PHE A N     
1314  C  CA    . PHE A 160 ? 0.745  0.2969 0.2165 -0.1097 0.1931 -0.0309 160 PHE A CA    
1315  C  C     . PHE A 160 ? 0.7393 0.2824 0.2085 -0.1043 0.1956 -0.0308 160 PHE A C     
1316  O  O     . PHE A 160 ? 0.7499 0.2802 0.2077 -0.1054 0.1978 -0.0312 160 PHE A O     
1317  C  CB    . PHE A 160 ? 0.7461 0.2967 0.2162 -0.1087 0.1933 -0.0307 160 PHE A CB    
1318  C  CG    . PHE A 160 ? 0.7506 0.3102 0.2231 -0.1134 0.1908 -0.0306 160 PHE A CG    
1319  C  CD1   . PHE A 160 ? 0.7498 0.3239 0.2344 -0.1122 0.1887 -0.0298 160 PHE A CD1   
1320  C  CD2   . PHE A 160 ? 0.7669 0.3202 0.229  -0.119  0.1904 -0.0311 160 PHE A CD2   
1321  C  CE1   . PHE A 160 ? 0.7541 0.3371 0.241  -0.1162 0.1866 -0.0293 160 PHE A CE1   
1322  C  CE2   . PHE A 160 ? 0.7711 0.3334 0.2355 -0.1233 0.1879 -0.0307 160 PHE A CE2   
1323  C  CZ    . PHE A 160 ? 0.7578 0.3354 0.235  -0.1218 0.186  -0.0297 160 PHE A CZ    
1324  N  N     . PRO A 161 ? 0.721  0.2704 0.2005 -0.0984 0.1955 -0.03   161 PRO A N     
1325  C  CA    . PRO A 161 ? 0.7227 0.2648 0.2006 -0.0931 0.1978 -0.0294 161 PRO A CA    
1326  C  C     . PRO A 161 ? 0.7318 0.2648 0.2041 -0.0897 0.2004 -0.0287 161 PRO A C     
1327  O  O     . PRO A 161 ? 0.7374 0.2718 0.21   -0.0902 0.2001 -0.0287 161 PRO A O     
1328  C  CB    . PRO A 161 ? 0.7184 0.2711 0.2094 -0.0886 0.1964 -0.0286 161 PRO A CB    
1329  C  CG    . PRO A 161 ? 0.7141 0.2768 0.2123 -0.0895 0.1945 -0.0285 161 PRO A CG    
1330  C  CD    . PRO A 161 ? 0.6989 0.2618 0.1912 -0.0963 0.1935 -0.0294 161 PRO A CD    
1331  N  N     . ASN A 162 ? 0.7311 0.2551 0.1987 -0.0857 0.203  -0.028  162 ASN A N     
1332  C  CA    . ASN A 162 ? 0.7377 0.2535 0.2007 -0.0813 0.2059 -0.0268 162 ASN A CA    
1333  C  C     . ASN A 162 ? 0.7348 0.2605 0.2104 -0.0763 0.205  -0.0255 162 ASN A C     
1334  O  O     . ASN A 162 ? 0.7301 0.2648 0.2158 -0.0743 0.2033 -0.0251 162 ASN A O     
1335  C  CB    . ASN A 162 ? 0.7544 0.2602 0.2111 -0.0775 0.2089 -0.0257 162 ASN A CB    
1336  C  CG    . ASN A 162 ? 0.7915 0.2878 0.2423 -0.0726 0.2125 -0.0241 162 ASN A CG    
1337  O  OD1   . ASN A 162 ? 0.7958 0.2972 0.2546 -0.0674 0.2129 -0.0224 162 ASN A OD1   
1338  N  ND2   . ASN A 162 ? 0.809  0.291  0.2452 -0.0741 0.2154 -0.0243 162 ASN A ND2   
1339  N  N     . PRO A 163 ? 0.7331 0.2569 0.208  -0.0743 0.2062 -0.0248 163 PRO A N     
1340  C  CA    . PRO A 163 ? 0.7248 0.2581 0.2118 -0.0697 0.2054 -0.0235 163 PRO A CA    
1341  C  C     . PRO A 163 ? 0.7218 0.2585 0.2165 -0.0642 0.2059 -0.0218 163 PRO A C     
1342  O  O     . PRO A 163 ? 0.714  0.2608 0.22   -0.062  0.2041 -0.0211 163 PRO A O     
1343  C  CB    . PRO A 163 ? 0.7376 0.2643 0.2194 -0.0678 0.2078 -0.0227 163 PRO A CB    
1344  C  CG    . PRO A 163 ? 0.7504 0.2673 0.2188 -0.0732 0.2084 -0.0242 163 PRO A CG    
1345  C  CD    . PRO A 163 ? 0.7331 0.2457 0.1958 -0.0763 0.2083 -0.0251 163 PRO A CD    
1346  N  N     . ALA A 164 ? 0.7279 0.2562 0.2162 -0.0621 0.2081 -0.0209 164 ALA A N     
1347  C  CA    . ALA A 164 ? 0.7295 0.2608 0.2242 -0.057  0.2085 -0.0189 164 ALA A CA    
1348  C  C     . ALA A 164 ? 0.7249 0.2656 0.2279 -0.0584 0.2053 -0.0197 164 ALA A C     
1349  O  O     . ALA A 164 ? 0.7214 0.2679 0.2326 -0.0547 0.2045 -0.0182 164 ALA A O     
1350  C  CB    . ALA A 164 ? 0.7399 0.2595 0.2245 -0.0545 0.2119 -0.0177 164 ALA A CB    
1351  N  N     . ILE A 165 ? 0.7256 0.2676 0.2262 -0.0638 0.2035 -0.0219 165 ILE A N     
1352  C  CA    . ILE A 165 ? 0.7254 0.2757 0.2332 -0.0651 0.2007 -0.0226 165 ILE A CA    
1353  C  C     . ILE A 165 ? 0.7147 0.2764 0.2341 -0.0639 0.1983 -0.0224 165 ILE A C     
1354  O  O     . ILE A 165 ? 0.7094 0.2759 0.2361 -0.0606 0.1974 -0.0212 165 ILE A O     
1355  C  CB    . ILE A 165 ? 0.7364 0.2856 0.2389 -0.0708 0.1996 -0.0246 165 ILE A CB    
1356  C  CG1   . ILE A 165 ? 0.7618 0.2983 0.251  -0.0728 0.2021 -0.025  165 ILE A CG1   
1357  C  CG2   . ILE A 165 ? 0.7369 0.2926 0.2456 -0.0709 0.1975 -0.0249 165 ILE A CG2   
1358  C  CD1   . ILE A 165 ? 0.7838 0.313  0.2691 -0.0684 0.2045 -0.0236 165 ILE A CD1   
1359  N  N     . PRO A 166 ? 0.709  0.2748 0.2302 -0.0663 0.1975 -0.0232 166 PRO A N     
1360  C  CA    . PRO A 166 ? 0.6985 0.2744 0.2304 -0.0647 0.1957 -0.0228 166 PRO A CA    
1361  C  C     . PRO A 166 ? 0.6917 0.2683 0.2288 -0.0594 0.1966 -0.0208 166 PRO A C     
1362  O  O     . PRO A 166 ? 0.6869 0.2707 0.2327 -0.0576 0.195  -0.0202 166 PRO A O     
1363  C  CB    . PRO A 166 ? 0.7075 0.2849 0.2378 -0.0674 0.1956 -0.0236 166 PRO A CB    
1364  C  CG    . PRO A 166 ? 0.7198 0.2911 0.2404 -0.0721 0.196  -0.0249 166 PRO A CG    
1365  C  CD    . PRO A 166 ? 0.7067 0.2684 0.2202 -0.0706 0.198  -0.0244 166 PRO A CD    
1366  N  N     . TYR A 167 ? 0.6896 0.2584 0.221  -0.057  0.1994 -0.0196 167 TYR A N     
1367  C  CA    . TYR A 167 ? 0.6873 0.2571 0.2238 -0.0519 0.2006 -0.0172 167 TYR A CA    
1368  C  C     . TYR A 167 ? 0.6751 0.2472 0.216  -0.0492 0.1999 -0.0158 167 TYR A C     
1369  O  O     . TYR A 167 ? 0.6715 0.2498 0.2209 -0.0463 0.199  -0.0141 167 TYR A O     
1370  C  CB    . TYR A 167 ? 0.6995 0.2603 0.2287 -0.0495 0.2041 -0.0159 167 TYR A CB    
1371  C  CG    . TYR A 167 ? 0.7154 0.2798 0.2518 -0.0444 0.2051 -0.0133 167 TYR A CG    
1372  C  CD1   . TYR A 167 ? 0.7268 0.2979 0.2704 -0.0441 0.2041 -0.0132 167 TYR A CD1   
1373  C  CD2   . TYR A 167 ? 0.7299 0.2924 0.2673 -0.04   0.2067 -0.0106 167 TYR A CD2   
1374  C  CE1   . TYR A 167 ? 0.7364 0.3115 0.2874 -0.0398 0.2049 -0.0107 167 TYR A CE1   
1375  C  CE2   . TYR A 167 ? 0.7407 0.3081 0.2859 -0.0356 0.2073 -0.0078 167 TYR A CE2   
1376  C  CZ    . TYR A 167 ? 0.7488 0.3224 0.3009 -0.0357 0.2064 -0.0079 167 TYR A CZ    
1377  O  OH    . TYR A 167 ? 0.7607 0.3392 0.3206 -0.0316 0.2071 -0.005  167 TYR A OH    
1378  N  N     . SER A 168 ? 0.6669 0.2343 0.2021 -0.0504 0.2001 -0.0163 168 SER A N     
1379  C  CA    . SER A 168 ? 0.6639 0.2331 0.2024 -0.0479 0.1993 -0.0149 168 SER A CA    
1380  C  C     . SER A 168 ? 0.6504 0.2297 0.1992 -0.0481 0.196  -0.015  168 SER A C     
1381  O  O     . SER A 168 ? 0.6476 0.2304 0.2019 -0.0452 0.1952 -0.0131 168 SER A O     
1382  C  CB    . SER A 168 ? 0.6937 0.2562 0.224  -0.0496 0.1999 -0.0159 168 SER A CB    
1383  O  OG    . SER A 168 ? 0.7307 0.296  0.2609 -0.0542 0.1977 -0.0184 168 SER A OG    
1384  N  N     . TYR A 169 ? 0.6399 0.2239 0.1912 -0.0515 0.1941 -0.0171 169 TYR A N     
1385  C  CA    . TYR A 169 ? 0.6324 0.2248 0.1921 -0.052  0.1913 -0.0173 169 TYR A CA    
1386  C  C     . TYR A 169 ? 0.6233 0.2207 0.1907 -0.0492 0.1911 -0.0156 169 TYR A C     
1387  O  O     . TYR A 169 ? 0.6199 0.2222 0.1937 -0.0478 0.1893 -0.0145 169 TYR A O     
1388  C  CB    . TYR A 169 ? 0.6321 0.2274 0.1913 -0.056  0.19   -0.0196 169 TYR A CB    
1389  C  CG    . TYR A 169 ? 0.6433 0.2355 0.1969 -0.0587 0.1896 -0.021  169 TYR A CG    
1390  C  CD1   . TYR A 169 ? 0.6599 0.2445 0.2046 -0.0603 0.1915 -0.0216 169 TYR A CD1   
1391  C  CD2   . TYR A 169 ? 0.6507 0.2468 0.2073 -0.0597 0.1876 -0.0216 169 TYR A CD2   
1392  C  CE1   . TYR A 169 ? 0.6704 0.252  0.21   -0.0629 0.1913 -0.0227 169 TYR A CE1   
1393  C  CE2   . TYR A 169 ? 0.6617 0.2548 0.2133 -0.062  0.1874 -0.0227 169 TYR A CE2   
1394  C  CZ    . TYR A 169 ? 0.6749 0.2611 0.2183 -0.0637 0.1893 -0.0232 169 TYR A CZ    
1395  O  OH    . TYR A 169 ? 0.6951 0.2783 0.2335 -0.0661 0.1892 -0.0242 169 TYR A OH    
1396  N  N     . ILE A 170 ? 0.6177 0.2135 0.184  -0.0484 0.1929 -0.0153 170 ILE A N     
1397  C  CA    . ILE A 170 ? 0.6137 0.2138 0.1868 -0.0457 0.1932 -0.0135 170 ILE A CA    
1398  C  C     . ILE A 170 ? 0.6232 0.2226 0.1986 -0.0417 0.1942 -0.0106 170 ILE A C     
1399  O  O     . ILE A 170 ? 0.6217 0.2272 0.2049 -0.0402 0.1928 -0.0089 170 ILE A O     
1400  C  CB    . ILE A 170 ? 0.6106 0.2082 0.181  -0.0457 0.1953 -0.0139 170 ILE A CB    
1401  C  CG1   . ILE A 170 ? 0.6155 0.2153 0.1845 -0.0495 0.1941 -0.0164 170 ILE A CG1   
1402  C  CG2   . ILE A 170 ? 0.6097 0.2112 0.1869 -0.0425 0.1959 -0.0118 170 ILE A CG2   
1403  C  CD1   . ILE A 170 ? 0.6322 0.2285 0.1966 -0.0502 0.1959 -0.0169 170 ILE A CD1   
1404  N  N     . SER A 171 ? 0.6306 0.2228 0.199  -0.0401 0.1965 -0.0096 171 SER A N     
1405  C  CA    . SER A 171 ? 0.6381 0.2298 0.2083 -0.0358 0.1978 -0.0063 171 SER A CA    
1406  C  C     . SER A 171 ? 0.6397 0.2359 0.2143 -0.0357 0.1952 -0.0055 171 SER A C     
1407  O  O     . SER A 171 ? 0.6402 0.2412 0.2212 -0.033  0.1946 -0.0027 171 SER A O     
1408  C  CB    . SER A 171 ? 0.661  0.2429 0.2215 -0.0338 0.2014 -0.0054 171 SER A CB    
1409  O  OG    . SER A 171 ? 0.6956 0.272  0.2483 -0.0368 0.2012 -0.0077 171 SER A OG    
1410  N  N     . HIS A 172 ? 0.6381 0.2333 0.2095 -0.0389 0.1934 -0.0079 172 HIS A N     
1411  C  CA    . HIS A 172 ? 0.6431 0.2422 0.2182 -0.039  0.1906 -0.0074 172 HIS A CA    
1412  C  C     . HIS A 172 ? 0.652  0.2596 0.2363 -0.0398 0.1877 -0.0072 172 HIS A C     
1413  O  O     . HIS A 172 ? 0.6525 0.2644 0.242  -0.0385 0.1859 -0.0052 172 HIS A O     
1414  C  CB    . HIS A 172 ? 0.6491 0.245  0.2186 -0.0423 0.1896 -0.0102 172 HIS A CB    
1415  C  CG    . HIS A 172 ? 0.6689 0.2657 0.2391 -0.0416 0.1877 -0.0094 172 HIS A CG    
1416  N  ND1   . HIS A 172 ? 0.6898 0.2871 0.2616 -0.038  0.1883 -0.0062 172 HIS A ND1   
1417  C  CD2   . HIS A 172 ? 0.6832 0.2803 0.2521 -0.0441 0.1856 -0.0112 172 HIS A CD2   
1418  C  CE1   . HIS A 172 ? 0.6956 0.2935 0.2671 -0.0385 0.1862 -0.0063 172 HIS A CE1   
1419  N  NE2   . HIS A 172 ? 0.6955 0.2929 0.265  -0.0421 0.1846 -0.0093 172 HIS A NE2   
1420  N  N     . SER A 173 ? 0.6554 0.2652 0.2416 -0.0419 0.1874 -0.009  173 SER A N     
1421  C  CA    . SER A 173 ? 0.6595 0.2761 0.2534 -0.0426 0.1852 -0.0089 173 SER A CA    
1422  C  C     . SER A 173 ? 0.664  0.2844 0.2642 -0.0396 0.1857 -0.0056 173 SER A C     
1423  O  O     . SER A 173 ? 0.6627 0.2884 0.2689 -0.0396 0.1833 -0.0043 173 SER A O     
1424  C  CB    . SER A 173 ? 0.6745 0.2919 0.2681 -0.0448 0.1855 -0.0111 173 SER A CB    
1425  O  OG    . SER A 173 ? 0.7043 0.3201 0.2936 -0.0477 0.1847 -0.0137 173 SER A OG    
1426  N  N     . LYS A 174 ? 0.6703 0.2878 0.2688 -0.037  0.1888 -0.0041 174 LYS A N     
1427  C  CA    . LYS A 174 ? 0.68   0.3013 0.2846 -0.0337 0.1897 -0.0006 174 LYS A CA    
1428  C  C     . LYS A 174 ? 0.6871 0.3105 0.294  -0.0315 0.1889 0.0025  174 LYS A C     
1429  O  O     . LYS A 174 ? 0.686  0.3161 0.3005 -0.0308 0.1871 0.0049  174 LYS A O     
1430  C  CB    . LYS A 174 ? 0.7101 0.3265 0.3108 -0.031  0.1937 0.0004  174 LYS A CB    
1431  C  CG    . LYS A 174 ? 0.7716 0.3862 0.3702 -0.0329 0.1945 -0.0022 174 LYS A CG    
1432  C  CD    . LYS A 174 ? 0.8433 0.4535 0.4389 -0.0298 0.1982 -0.0006 174 LYS A CD    
1433  C  CE    . LYS A 174 ? 0.9086 0.5151 0.4992 -0.0321 0.1992 -0.0034 174 LYS A CE    
1434  N  NZ    . LYS A 174 ? 0.9566 0.5551 0.5398 -0.0298 0.2029 -0.0025 174 LYS A NZ    
1435  N  N     . ASN A 175 ? 0.6914 0.3092 0.2915 -0.0304 0.1901 0.0025  175 ASN A N     
1436  C  CA    . ASN A 175 ? 0.6958 0.3151 0.2971 -0.0279 0.1897 0.0056  175 ASN A CA    
1437  C  C     . ASN A 175 ? 0.6949 0.3202 0.3013 -0.0302 0.1853 0.0055  175 ASN A C     
1438  O  O     . ASN A 175 ? 0.6966 0.3273 0.3084 -0.0285 0.184  0.0088  175 ASN A O     
1439  C  CB    . ASN A 175 ? 0.7174 0.3283 0.3092 -0.0268 0.192  0.005   175 ASN A CB    
1440  C  CG    . ASN A 175 ? 0.7616 0.3654 0.3472 -0.0238 0.1966 0.0061  175 ASN A CG    
1441  O  OD1   . ASN A 175 ? 0.7718 0.3776 0.3611 -0.0209 0.1985 0.0087  175 ASN A OD1   
1442  N  ND2   . ASN A 175 ? 0.7778 0.3726 0.3534 -0.0246 0.1986 0.004   175 ASN A ND2   
1443  N  N     . THR A 176 ? 0.6909 0.3154 0.2954 -0.0342 0.1831 0.0018  176 THR A N     
1444  C  CA    . THR A 176 ? 0.69   0.3185 0.2975 -0.0365 0.1791 0.0014  176 THR A CA    
1445  C  C     . THR A 176 ? 0.6818 0.3164 0.2963 -0.0387 0.1765 0.0012  176 THR A C     
1446  O  O     . THR A 176 ? 0.6839 0.3224 0.3018 -0.0402 0.1732 0.0019  176 THR A O     
1447  C  CB    . THR A 176 ? 0.7117 0.3353 0.3126 -0.0393 0.1783 -0.0022 176 THR A CB    
1448  O  OG1   . THR A 176 ? 0.725  0.347  0.3242 -0.0414 0.1792 -0.0051 176 THR A OG1   
1449  C  CG2   . THR A 176 ? 0.7219 0.3392 0.3155 -0.0377 0.1803 -0.0022 176 THR A CG2   
1450  N  N     . GLY A 177 ? 0.6723 0.3071 0.2881 -0.0391 0.178  0.0001  177 GLY A N     
1451  C  CA    . GLY A 177 ? 0.6667 0.3061 0.2879 -0.0414 0.176  -0.0005 177 GLY A CA    
1452  C  C     . GLY A 177 ? 0.6624 0.2997 0.2802 -0.0448 0.1744 -0.0042 177 GLY A C     
1453  O  O     . GLY A 177 ? 0.6625 0.3024 0.2833 -0.0467 0.1728 -0.005  177 GLY A O     
1454  N  N     . ASN A 178 ? 0.6569 0.2893 0.268  -0.0454 0.175  -0.0062 178 ASN A N     
1455  C  CA    . ASN A 178 ? 0.655  0.2852 0.2622 -0.0482 0.1739 -0.0093 178 ASN A CA    
1456  C  C     . ASN A 178 ? 0.6458 0.2737 0.2498 -0.0488 0.1762 -0.0115 178 ASN A C     
1457  O  O     . ASN A 178 ? 0.6444 0.2713 0.248  -0.0473 0.1787 -0.0109 178 ASN A O     
1458  C  CB    . ASN A 178 ? 0.6728 0.2994 0.2749 -0.0485 0.1731 -0.0099 178 ASN A CB    
1459  C  CG    . ASN A 178 ? 0.7186 0.3433 0.3171 -0.0511 0.1716 -0.0124 178 ASN A CG    
1460  O  OD1   . ASN A 178 ? 0.734  0.3605 0.3342 -0.0528 0.1705 -0.0135 178 ASN A OD1   
1461  N  ND2   . ASN A 178 ? 0.7298 0.3506 0.323  -0.0513 0.1717 -0.0132 178 ASN A ND2   
1462  N  N     . PHE A 179 ? 0.637  0.2644 0.2387 -0.0511 0.1756 -0.0139 179 PHE A N     
1463  C  CA    . PHE A 179 ? 0.6343 0.2606 0.2332 -0.052  0.1774 -0.0157 179 PHE A CA    
1464  C  C     . PHE A 179 ? 0.6379 0.2601 0.2303 -0.0531 0.1782 -0.0171 179 PHE A C     
1465  O  O     . PHE A 179 ? 0.6418 0.2633 0.232  -0.0546 0.177  -0.0183 179 PHE A O     
1466  C  CB    . PHE A 179 ? 0.6276 0.2564 0.2282 -0.0535 0.1766 -0.017  179 PHE A CB    
1467  C  CG    . PHE A 179 ? 0.6308 0.2599 0.2294 -0.0542 0.1784 -0.0184 179 PHE A CG    
1468  C  CD1   . PHE A 179 ? 0.6386 0.268  0.238  -0.0531 0.1803 -0.0179 179 PHE A CD1   
1469  C  CD2   . PHE A 179 ? 0.6389 0.2683 0.235  -0.0558 0.1782 -0.0199 179 PHE A CD2   
1470  C  CE1   . PHE A 179 ? 0.6458 0.2759 0.2434 -0.054  0.1817 -0.0191 179 PHE A CE1   
1471  C  CE2   . PHE A 179 ? 0.646  0.2767 0.2408 -0.0565 0.1797 -0.0208 179 PHE A CE2   
1472  C  CZ    . PHE A 179 ? 0.6423 0.2734 0.2378 -0.0557 0.1813 -0.0205 179 PHE A CZ    
1473  N  N     . ILE A 180 ? 0.6348 0.2537 0.2238 -0.0523 0.1803 -0.0169 180 ILE A N     
1474  C  CA    . ILE A 180 ? 0.6382 0.2526 0.2204 -0.0537 0.1814 -0.0181 180 ILE A CA    
1475  C  C     . ILE A 180 ? 0.6436 0.2572 0.2235 -0.0546 0.1834 -0.019  180 ILE A C     
1476  O  O     . ILE A 180 ? 0.645  0.2574 0.2253 -0.0529 0.1849 -0.0179 180 ILE A O     
1477  C  CB    . ILE A 180 ? 0.6401 0.25   0.2191 -0.0519 0.1822 -0.0168 180 ILE A CB    
1478  C  CG1   . ILE A 180 ? 0.6456 0.2575 0.2279 -0.0507 0.18   -0.0155 180 ILE A CG1   
1479  C  CG2   . ILE A 180 ? 0.648  0.2525 0.2193 -0.0536 0.1835 -0.0182 180 ILE A CG2   
1480  C  CD1   . ILE A 180 ? 0.6563 0.2696 0.2424 -0.0477 0.1803 -0.0127 180 ILE A CD1   
1481  N  N     . VAL A 181 ? 0.6446 0.259  0.2221 -0.0572 0.1833 -0.0207 181 VAL A N     
1482  C  CA    . VAL A 181 ? 0.6516 0.2662 0.2272 -0.0585 0.1847 -0.0214 181 VAL A CA    
1483  C  C     . VAL A 181 ? 0.6618 0.2747 0.2317 -0.0617 0.1851 -0.0228 181 VAL A C     
1484  O  O     . VAL A 181 ? 0.6635 0.2764 0.2319 -0.063  0.1842 -0.0234 181 VAL A O     
1485  C  CB    . VAL A 181 ? 0.6541 0.2746 0.2354 -0.0582 0.1841 -0.0214 181 VAL A CB    
1486  C  CG1   . VAL A 181 ? 0.661  0.2849 0.2429 -0.0599 0.183  -0.0224 181 VAL A CG1   
1487  C  CG2   . VAL A 181 ? 0.6574 0.2783 0.238  -0.0583 0.1856 -0.0215 181 VAL A CG2   
1488  N  N     . GLN A 182 ? 0.6657 0.277  0.232  -0.0631 0.1864 -0.0232 182 GLN A N     
1489  C  CA    . GLN A 182 ? 0.6721 0.2828 0.2334 -0.0668 0.1866 -0.0243 182 GLN A CA    
1490  C  C     . GLN A 182 ? 0.6716 0.2887 0.2363 -0.0678 0.1863 -0.0245 182 GLN A C     
1491  O  O     . GLN A 182 ? 0.6715 0.2894 0.238  -0.0665 0.1869 -0.024  182 GLN A O     
1492  C  CB    . GLN A 182 ? 0.692  0.2954 0.2457 -0.068  0.1883 -0.0245 182 GLN A CB    
1493  C  CG    . GLN A 182 ? 0.725  0.326  0.2723 -0.0721 0.1883 -0.0255 182 GLN A CG    
1494  C  CD    . GLN A 182 ? 0.7689 0.3608 0.3077 -0.0731 0.1901 -0.0256 182 GLN A CD    
1495  O  OE1   . GLN A 182 ? 0.7807 0.3698 0.3165 -0.0733 0.1912 -0.0256 182 GLN A OE1   
1496  N  NE2   . GLN A 182 ? 0.7816 0.3679 0.3154 -0.0736 0.1906 -0.0259 182 GLN A NE2   
1497  N  N     . ALA A 183 ? 0.6674 0.2892 0.2332 -0.0697 0.1855 -0.0248 183 ALA A N     
1498  C  CA    . ALA A 183 ? 0.6663 0.2948 0.2351 -0.0704 0.1852 -0.0247 183 ALA A CA    
1499  C  C     . ALA A 183 ? 0.6677 0.2976 0.2323 -0.0744 0.1853 -0.025  183 ALA A C     
1500  O  O     . ALA A 183 ? 0.672  0.2998 0.2332 -0.0764 0.1851 -0.0253 183 ALA A O     
1501  C  CB    . ALA A 183 ? 0.6637 0.297  0.2375 -0.0689 0.1844 -0.0243 183 ALA A CB    
1502  N  N     . TYR A 184 ? 0.663  0.2968 0.2279 -0.0757 0.1854 -0.0247 184 TYR A N     
1503  C  CA    . TYR A 184 ? 0.6693 0.3049 0.2301 -0.08   0.1852 -0.0247 184 TYR A CA    
1504  C  C     . TYR A 184 ? 0.6718 0.3169 0.2368 -0.0806 0.1847 -0.0238 184 TYR A C     
1505  O  O     . TYR A 184 ? 0.6693 0.3187 0.2385 -0.0784 0.1849 -0.0232 184 TYR A O     
1506  C  CB    . TYR A 184 ? 0.6723 0.3035 0.228  -0.0819 0.1857 -0.0251 184 TYR A CB    
1507  C  CG    . TYR A 184 ? 0.6853 0.3071 0.2372 -0.0801 0.1868 -0.0257 184 TYR A CG    
1508  C  CD1   . TYR A 184 ? 0.7003 0.3149 0.2457 -0.082  0.1872 -0.0262 184 TYR A CD1   
1509  C  CD2   . TYR A 184 ? 0.6952 0.3155 0.2503 -0.0761 0.1875 -0.0253 184 TYR A CD2   
1510  C  CE1   . TYR A 184 ? 0.7137 0.32   0.2558 -0.0797 0.1885 -0.0263 184 TYR A CE1   
1511  C  CE2   . TYR A 184 ? 0.7085 0.3212 0.261  -0.0739 0.1886 -0.0253 184 TYR A CE2   
1512  C  CZ    . TYR A 184 ? 0.7236 0.3293 0.2694 -0.0755 0.1891 -0.0257 184 TYR A CZ    
1513  O  OH    . TYR A 184 ? 0.7461 0.3443 0.289  -0.0729 0.1906 -0.0253 184 TYR A OH    
1514  N  N     . PHE A 185 ? 0.6766 0.3248 0.2404 -0.0834 0.1844 -0.0233 185 PHE A N     
1515  C  CA    . PHE A 185 ? 0.6855 0.3433 0.253  -0.084  0.1842 -0.0219 185 PHE A CA    
1516  C  C     . PHE A 185 ? 0.7062 0.3672 0.2704 -0.0888 0.1836 -0.0214 185 PHE A C     
1517  O  O     . PHE A 185 ? 0.7091 0.3644 0.2673 -0.0924 0.1833 -0.0222 185 PHE A O     
1518  C  CB    . PHE A 185 ? 0.679  0.339  0.2481 -0.0834 0.1843 -0.0213 185 PHE A CB    
1519  C  CG    . PHE A 185 ? 0.6799 0.3393 0.2529 -0.0788 0.1847 -0.0213 185 PHE A CG    
1520  C  CD1   . PHE A 185 ? 0.6886 0.3442 0.2633 -0.0758 0.1847 -0.0221 185 PHE A CD1   
1521  C  CD2   . PHE A 185 ? 0.6853 0.3475 0.2599 -0.0777 0.185  -0.0204 185 PHE A CD2   
1522  C  CE1   . PHE A 185 ? 0.6935 0.3482 0.2713 -0.0723 0.1848 -0.022  185 PHE A CE1   
1523  C  CE2   . PHE A 185 ? 0.6924 0.3529 0.2693 -0.0739 0.1853 -0.0205 185 PHE A CE2   
1524  C  CZ    . PHE A 185 ? 0.6888 0.3456 0.2673 -0.0715 0.185  -0.0214 185 PHE A CZ    
1525  N  N     . ARG A 186 ? 0.7176 0.3874 0.2851 -0.0891 0.1834 -0.0199 186 ARG A N     
1526  C  CA    . ARG A 186 ? 0.7375 0.412  0.3025 -0.0938 0.1825 -0.019  186 ARG A CA    
1527  C  C     . ARG A 186 ? 0.754  0.4318 0.3175 -0.0978 0.182  -0.0181 186 ARG A C     
1528  O  O     . ARG A 186 ? 0.7502 0.4357 0.3182 -0.0965 0.1824 -0.0163 186 ARG A O     
1529  C  CB    . ARG A 186 ? 0.7529 0.4369 0.3225 -0.0924 0.1824 -0.0173 186 ARG A CB    
1530  C  CG    . ARG A 186 ? 0.7993 0.4882 0.3662 -0.0976 0.1811 -0.0163 186 ARG A CG    
1531  C  CD    . ARG A 186 ? 0.8431 0.5444 0.4153 -0.0966 0.181  -0.0138 186 ARG A CD    
1532  N  NE    . ARG A 186 ? 0.8917 0.5953 0.4612 -0.1    0.1797 -0.0134 186 ARG A NE    
1533  C  CZ    . ARG A 186 ? 0.9212 0.6256 0.492  -0.0974 0.1799 -0.0135 186 ARG A CZ    
1534  N  NH1   . ARG A 186 ? 0.9213 0.6276 0.4889 -0.101  0.1786 -0.0131 186 ARG A NH1   
1535  N  NH2   . ARG A 186 ? 0.9174 0.621  0.4925 -0.0915 0.1815 -0.0138 186 ARG A NH2   
1536  N  N     . GLY A 187 ? 0.7711 0.4429 0.328  -0.1025 0.1814 -0.019  187 GLY A N     
1537  C  CA    . GLY A 187 ? 0.7909 0.4652 0.3457 -0.107  0.1809 -0.0182 187 GLY A CA    
1538  C  C     . GLY A 187 ? 0.8068 0.4922 0.3634 -0.1109 0.1798 -0.0159 187 GLY A C     
1539  O  O     . GLY A 187 ? 0.8058 0.4943 0.3627 -0.1114 0.1791 -0.0155 187 GLY A O     
1540  N  N     . GLU A 188 ? 0.82   0.5119 0.3779 -0.1137 0.1796 -0.0141 188 GLU A N     
1541  C  CA    . GLU A 188 ? 0.8367 0.5406 0.397  -0.1176 0.1785 -0.0113 188 GLU A CA    
1542  C  C     . GLU A 188 ? 0.8594 0.5604 0.4129 -0.1242 0.1767 -0.012  188 GLU A C     
1543  O  O     . GLU A 188 ? 0.8604 0.5699 0.4155 -0.1265 0.1754 -0.0102 188 GLU A O     
1544  C  CB    . GLU A 188 ? 0.8632 0.5738 0.4258 -0.1195 0.1788 -0.0091 188 GLU A CB    
1545  C  CG    . GLU A 188 ? 0.9183 0.631  0.4864 -0.1132 0.1807 -0.0083 188 GLU A CG    
1546  C  CD    . GLU A 188 ? 0.9939 0.6961 0.5586 -0.112  0.1817 -0.0104 188 GLU A CD    
1547  O  OE1   . GLU A 188 ? 1.0096 0.7007 0.5685 -0.1132 0.1813 -0.0132 188 GLU A OE1   
1548  O  OE2   . GLU A 188 ? 1.0229 0.7278 0.5905 -0.1095 0.1829 -0.0092 188 GLU A OE2   
1549  N  N     . GLU A 189 ? 0.8743 0.5627 0.4197 -0.1271 0.1767 -0.0145 189 GLU A N     
1550  C  CA    . GLU A 189 ? 0.8916 0.5749 0.4289 -0.1334 0.1753 -0.0154 189 GLU A CA    
1551  C  C     . GLU A 189 ? 0.9047 0.5806 0.4385 -0.1314 0.1753 -0.0172 189 GLU A C     
1552  O  O     . GLU A 189 ? 0.9117 0.5803 0.4371 -0.1361 0.1745 -0.0183 189 GLU A O     
1553  C  CB    . GLU A 189 ? 0.9258 0.5989 0.4547 -0.1382 0.1755 -0.0169 189 GLU A CB    
1554  C  CG    . GLU A 189 ? 0.981  0.6629 0.511  -0.1438 0.1745 -0.0146 189 GLU A CG    
1555  C  CD    . GLU A 189 ? 1.0633 0.7356 0.5849 -0.149  0.1747 -0.0159 189 GLU A CD    
1556  O  OE1   . GLU A 189 ? 1.0842 0.7441 0.6013 -0.1462 0.1764 -0.0183 189 GLU A OE1   
1557  O  OE2   . GLU A 189 ? 1.0864 0.7637 0.6059 -0.156  0.1734 -0.0144 189 GLU A OE2   
1558  N  N     . TYR A 190 ? 0.9052 0.583  0.4452 -0.1245 0.1763 -0.0173 190 TYR A N     
1559  C  CA    . TYR A 190 ? 0.9164 0.5888 0.4541 -0.1223 0.1765 -0.0185 190 TYR A CA    
1560  C  C     . TYR A 190 ? 0.9197 0.6021 0.4588 -0.1253 0.1748 -0.0166 190 TYR A C     
1561  O  O     . TYR A 190 ? 0.9175 0.6114 0.4647 -0.1223 0.1747 -0.0146 190 TYR A O     
1562  C  CB    . TYR A 190 ? 0.9143 0.5864 0.4585 -0.1144 0.1781 -0.019  190 TYR A CB    
1563  C  CG    . TYR A 190 ? 0.9233 0.592  0.4665 -0.1119 0.1784 -0.0197 190 TYR A CG    
1564  C  CD1   . TYR A 190 ? 0.9406 0.5968 0.476  -0.1126 0.1789 -0.0217 190 TYR A CD1   
1565  C  CD2   . TYR A 190 ? 0.9288 0.6064 0.4784 -0.1087 0.1783 -0.0184 190 TYR A CD2   
1566  C  CE1   . TYR A 190 ? 0.9526 0.6055 0.4868 -0.1102 0.1794 -0.0222 190 TYR A CE1   
1567  C  CE2   . TYR A 190 ? 0.9408 0.6152 0.4893 -0.1064 0.1786 -0.019  190 TYR A CE2   
1568  C  CZ    . TYR A 190 ? 0.9575 0.6196 0.4985 -0.1072 0.1792 -0.0209 190 TYR A CZ    
1569  O  OH    . TYR A 190 ? 0.9762 0.6347 0.5157 -0.1049 0.1797 -0.0214 190 TYR A OH    
1570  N  N     . GLN A 191 ? 0.9223 0.6007 0.4534 -0.1316 0.1733 -0.0171 191 GLN A N     
1571  C  CA    . GLN A 191 ? 0.9235 0.6113 0.4551 -0.1353 0.1712 -0.0152 191 GLN A CA    
1572  C  C     . GLN A 191 ? 0.9322 0.6098 0.4554 -0.1367 0.1709 -0.017  191 GLN A C     
1573  O  O     . GLN A 191 ? 0.9408 0.6114 0.4544 -0.1432 0.1697 -0.0178 191 GLN A O     
1574  C  CB    . GLN A 191 ? 0.9404 0.6343 0.4697 -0.1431 0.1692 -0.0135 191 GLN A CB    
1575  C  CG    . GLN A 191 ? 0.9685 0.6803 0.5059 -0.1442 0.1678 -0.0099 191 GLN A CG    
1576  C  CD    . GLN A 191 ? 1.0107 0.7313 0.5587 -0.1372 0.1696 -0.0082 191 GLN A CD    
1577  O  OE1   . GLN A 191 ? 1.0233 0.7415 0.5729 -0.1354 0.171  -0.0086 191 GLN A OE1   
1578  N  NE2   . GLN A 191 ? 1.0164 0.747  0.571  -0.1332 0.1697 -0.0063 191 GLN A NE2   
1579  N  N     . PRO A 192 ? 0.9294 0.6052 0.4555 -0.1307 0.1721 -0.0176 192 PRO A N     
1580  C  CA    . PRO A 192 ? 0.9359 0.6008 0.4538 -0.1312 0.1723 -0.0193 192 PRO A CA    
1581  C  C     . PRO A 192 ? 0.9369 0.6055 0.4499 -0.137  0.1698 -0.0183 192 PRO A C     
1582  O  O     . PRO A 192 ? 0.946  0.6035 0.4491 -0.1395 0.1697 -0.0198 192 PRO A O     
1583  C  CB    . PRO A 192 ? 0.9423 0.6069 0.4665 -0.123  0.1742 -0.0197 192 PRO A CB    
1584  C  CG    . PRO A 192 ? 0.939  0.6178 0.4744 -0.1196 0.1742 -0.0176 192 PRO A CG    
1585  C  CD    . PRO A 192 ? 0.9169 0.5992 0.4532 -0.123  0.1736 -0.0169 192 PRO A CD    
1586  N  N     . LYS A 193 ? 0.927  0.6109 0.4464 -0.139  0.1679 -0.0156 193 LYS A N     
1587  C  CA    . LYS A 193 ? 0.9312 0.6203 0.4466 -0.145  0.1651 -0.0143 193 LYS A CA    
1588  C  C     . LYS A 193 ? 0.9393 0.6224 0.4442 -0.1543 0.1632 -0.0148 193 LYS A C     
1589  O  O     . LYS A 193 ? 0.9455 0.628  0.4435 -0.1601 0.1609 -0.0144 193 LYS A O     
1590  C  CB    . LYS A 193 ? 0.9445 0.653  0.4704 -0.1443 0.1638 -0.0107 193 LYS A CB    
1591  C  CG    . LYS A 193 ? 0.9901 0.7046 0.5258 -0.1354 0.1659 -0.01   193 LYS A CG    
1592  C  CD    . LYS A 193 ? 1.0339 0.7668 0.5793 -0.1343 0.1651 -0.0062 193 LYS A CD    
1593  C  CE    . LYS A 193 ? 1.0737 0.8113 0.6275 -0.1255 0.1674 -0.0056 193 LYS A CE    
1594  N  NZ    . LYS A 193 ? 1.0914 0.8464 0.654  -0.1239 0.1672 -0.0017 193 LYS A NZ    
1595  N  N     . TYR A 194 ? 0.9376 0.616  0.4408 -0.156  0.164  -0.0156 194 TYR A N     
1596  C  CA    . TYR A 194 ? 0.9447 0.6173 0.4383 -0.1649 0.1624 -0.016  194 TYR A CA    
1597  C  C     . TYR A 194 ? 0.9451 0.5978 0.4269 -0.1656 0.1643 -0.0192 194 TYR A C     
1598  O  O     . TYR A 194 ? 0.9539 0.5986 0.4245 -0.1733 0.1631 -0.0199 194 TYR A O     
1599  C  CB    . TYR A 194 ? 0.9458 0.6299 0.446  -0.1677 0.1617 -0.0138 194 TYR A CB    
1600  C  CG    . TYR A 194 ? 0.9552 0.659  0.4652 -0.1683 0.1596 -0.0101 194 TYR A CG    
1601  C  CD1   . TYR A 194 ? 0.9701 0.681  0.4766 -0.1764 0.1563 -0.0082 194 TYR A CD1   
1602  C  CD2   . TYR A 194 ? 0.9623 0.6774 0.4846 -0.1607 0.1611 -0.0084 194 TYR A CD2   
1603  C  CE1   . TYR A 194 ? 0.9748 0.7045 0.4905 -0.1766 0.1545 -0.0043 194 TYR A CE1   
1604  C  CE2   . TYR A 194 ? 0.9674 0.7003 0.4983 -0.1607 0.1597 -0.0046 194 TYR A CE2   
1605  C  CZ    . TYR A 194 ? 0.9788 0.7195 0.5067 -0.1685 0.1564 -0.0025 194 TYR A CZ    
1606  O  OH    . TYR A 194 ? 0.9892 0.7484 0.526  -0.1682 0.155  0.0016  194 TYR A OH    
1607  N  N     . ASP A 195 ? 0.9335 0.5781 0.4172 -0.158  0.1674 -0.0209 195 ASP A N     
1608  C  CA    . ASP A 195 ? 0.9349 0.5611 0.4078 -0.1578 0.1696 -0.0235 195 ASP A CA    
1609  C  C     . ASP A 195 ? 0.9237 0.5389 0.392  -0.1528 0.1715 -0.025  195 ASP A C     
1610  O  O     . ASP A 195 ? 0.921  0.5396 0.3977 -0.1452 0.173  -0.0249 195 ASP A O     
1611  C  CB    . ASP A 195 ? 0.9588 0.5831 0.4362 -0.1538 0.1717 -0.0241 195 ASP A CB    
1612  C  CG    . ASP A 195 ? 1.0333 0.6408 0.4985 -0.1564 0.1734 -0.0261 195 ASP A CG    
1613  O  OD1   . ASP A 195 ? 1.0563 0.6501 0.5112 -0.1564 0.1746 -0.0276 195 ASP A OD1   
1614  O  OD2   . ASP A 195 ? 1.059  0.6668 0.5248 -0.1582 0.1737 -0.026  195 ASP A OD2   
1615  N  N     . LYS A 196 ? 0.9168 0.5181 0.3712 -0.1572 0.1716 -0.0263 196 LYS A N     
1616  C  CA    . LYS A 196 ? 0.9142 0.5035 0.3622 -0.1531 0.1736 -0.0276 196 LYS A CA    
1617  C  C     . LYS A 196 ? 0.9067 0.4866 0.3559 -0.1454 0.1773 -0.0287 196 LYS A C     
1618  O  O     . LYS A 196 ? 0.9123 0.4874 0.3618 -0.1396 0.1792 -0.0291 196 LYS A O     
1619  C  CB    . LYS A 196 ? 0.9428 0.5182 0.3739 -0.1601 0.173  -0.0287 196 LYS A CB    
1620  C  CG    . LYS A 196 ? 0.9811 0.5656 0.4102 -0.1684 0.1689 -0.0274 196 LYS A CG    
1621  C  CD    . LYS A 196 ? 1.0193 0.6172 0.458  -0.1652 0.1674 -0.0259 196 LYS A CD    
1622  C  CE    . LYS A 196 ? 1.0607 0.6616 0.4926 -0.173  0.1638 -0.025  196 LYS A CE    
1623  N  NZ    . LYS A 196 ? 1.0932 0.6759 0.5093 -0.1749 0.1648 -0.0268 196 LYS A NZ    
1624  N  N     . LYS A 197 ? 0.8931 0.4709 0.3432 -0.1451 0.1784 -0.0291 197 LYS A N     
1625  C  CA    . LYS A 197 ? 0.8904 0.4606 0.3423 -0.1378 0.1816 -0.0299 197 LYS A CA    
1626  C  C     . LYS A 197 ? 0.8744 0.4553 0.3407 -0.13   0.1821 -0.029  197 LYS A C     
1627  O  O     . LYS A 197 ? 0.8767 0.4516 0.3445 -0.1235 0.1846 -0.0294 197 LYS A O     
1628  C  CB    . LYS A 197 ? 0.9147 0.482  0.3654 -0.1394 0.1823 -0.0303 197 LYS A CB    
1629  C  CG    . LYS A 197 ? 0.9731 0.5261 0.4081 -0.1459 0.1829 -0.0314 197 LYS A CG    
1630  C  CD    . LYS A 197 ? 1.028  0.5779 0.462  -0.1468 0.1838 -0.0318 197 LYS A CD    
1631  C  CE    . LYS A 197 ? 1.0805 0.6144 0.4979 -0.1527 0.1849 -0.033  197 LYS A CE    
1632  N  NZ    . LYS A 197 ? 1.1106 0.6279 0.5174 -0.1489 0.1881 -0.0339 197 LYS A NZ    
1633  N  N     . LEU A 198 ? 0.8562 0.4529 0.3328 -0.1306 0.1799 -0.0277 198 LEU A N     
1634  C  CA    . LEU A 198 ? 0.8443 0.4513 0.3339 -0.1238 0.1802 -0.0268 198 LEU A CA    
1635  C  C     . LEU A 198 ? 0.8352 0.446  0.3271 -0.1216 0.1799 -0.0262 198 LEU A C     
1636  O  O     . LEU A 198 ? 0.8338 0.4535 0.3362 -0.1164 0.1802 -0.0254 198 LEU A O     
1637  C  CB    . LEU A 198 ? 0.8388 0.4605 0.3382 -0.1249 0.1785 -0.0254 198 LEU A CB    
1638  C  CG    . LEU A 198 ? 0.8603 0.4802 0.3585 -0.1272 0.1787 -0.0257 198 LEU A CG    
1639  C  CD1   . LEU A 198 ? 0.861  0.4956 0.3674 -0.1295 0.1769 -0.0239 198 LEU A CD1   
1640  C  CD2   . LEU A 198 ? 0.8707 0.4841 0.3713 -0.1211 0.1811 -0.0266 198 LEU A CD2   
1641  N  N     . LYS A 199 ? 0.8281 0.4319 0.3101 -0.1255 0.1793 -0.0267 199 LYS A N     
1642  C  CA    . LYS A 199 ? 0.8228 0.4295 0.3059 -0.1237 0.1789 -0.0261 199 LYS A CA    
1643  C  C     . LYS A 199 ? 0.8171 0.4222 0.3064 -0.1153 0.1814 -0.0262 199 LYS A C     
1644  O  O     . LYS A 199 ? 0.8162 0.4303 0.313  -0.1122 0.181  -0.0253 199 LYS A O     
1645  C  CB    . LYS A 199 ? 0.85   0.4457 0.3191 -0.1289 0.1784 -0.0269 199 LYS A CB    
1646  C  CG    . LYS A 199 ? 0.9011 0.504  0.3669 -0.1372 0.1749 -0.0261 199 LYS A CG    
1647  C  CD    . LYS A 199 ? 0.965  0.5655 0.424  -0.1397 0.1736 -0.026  199 LYS A CD    
1648  C  CE    . LYS A 199 ? 1.0246 0.6059 0.4677 -0.1417 0.1752 -0.0276 199 LYS A CE    
1649  N  NZ    . LYS A 199 ? 1.058  0.6326 0.4893 -0.1508 0.1735 -0.0282 199 LYS A NZ    
1650  N  N     . PHE A 200 ? 0.8097 0.4041 0.2962 -0.1116 0.1841 -0.0271 200 PHE A N     
1651  C  CA    . PHE A 200 ? 0.8012 0.394  0.2936 -0.1039 0.1864 -0.0269 200 PHE A CA    
1652  C  C     . PHE A 200 ? 0.7862 0.3846 0.2889 -0.0994 0.1872 -0.0266 200 PHE A C     
1653  O  O     . PHE A 200 ? 0.7901 0.3831 0.2946 -0.0941 0.1894 -0.0266 200 PHE A O     
1654  C  CB    . PHE A 200 ? 0.8086 0.3856 0.2907 -0.1021 0.1891 -0.0276 200 PHE A CB    
1655  C  CG    . PHE A 200 ? 0.8219 0.3928 0.2933 -0.1063 0.1884 -0.0279 200 PHE A CG    
1656  C  CD1   . PHE A 200 ? 0.8302 0.407  0.3049 -0.1051 0.1876 -0.0273 200 PHE A CD1   
1657  C  CD2   . PHE A 200 ? 0.838  0.3974 0.2957 -0.1119 0.1884 -0.0288 200 PHE A CD2   
1658  C  CE1   . PHE A 200 ? 0.8443 0.4156 0.3088 -0.1092 0.1867 -0.0276 200 PHE A CE1   
1659  C  CE2   . PHE A 200 ? 0.8528 0.4061 0.2998 -0.1164 0.1875 -0.0291 200 PHE A CE2   
1660  C  CZ    . PHE A 200 ? 0.8488 0.4083 0.2994 -0.115  0.1866 -0.0285 200 PHE A CZ    
1661  N  N     . PHE A 201 ? 0.7672 0.3764 0.2766 -0.1013 0.1853 -0.0261 201 PHE A N     
1662  C  CA    . PHE A 201 ? 0.7554 0.3698 0.2741 -0.0972 0.1858 -0.0258 201 PHE A CA    
1663  C  C     . PHE A 201 ? 0.7443 0.369  0.2733 -0.0928 0.1857 -0.0248 201 PHE A C     
1664  O  O     . PHE A 201 ? 0.7442 0.3771 0.2753 -0.0947 0.1843 -0.024  201 PHE A O     
1665  C  CB    . PHE A 201 ? 0.7472 0.367  0.2672 -0.1012 0.1843 -0.0256 201 PHE A CB    
1666  C  CG    . PHE A 201 ? 0.7477 0.3714 0.2759 -0.0971 0.1849 -0.0254 201 PHE A CG    
1667  C  CD1   . PHE A 201 ? 0.7579 0.3732 0.2845 -0.0941 0.1865 -0.0261 201 PHE A CD1   
1668  C  CD2   . PHE A 201 ? 0.7507 0.3863 0.2876 -0.0961 0.1839 -0.0244 201 PHE A CD2   
1669  C  CE1   . PHE A 201 ? 0.7612 0.38   0.2949 -0.0907 0.1867 -0.0258 201 PHE A CE1   
1670  C  CE2   . PHE A 201 ? 0.754  0.3921 0.2973 -0.0925 0.1844 -0.0243 201 PHE A CE2   
1671  C  CZ    . PHE A 201 ? 0.7524 0.3821 0.2941 -0.09   0.1856 -0.0251 201 PHE A CZ    
1672  N  N     . ASP A 202 ? 0.7318 0.356  0.2671 -0.0871 0.1872 -0.0247 202 ASP A N     
1673  C  CA    . ASP A 202 ? 0.7206 0.3533 0.2651 -0.0829 0.1874 -0.0239 202 ASP A CA    
1674  C  C     . ASP A 202 ? 0.7099 0.3514 0.2615 -0.0826 0.1865 -0.0234 202 ASP A C     
1675  O  O     . ASP A 202 ? 0.7122 0.3512 0.2657 -0.081  0.1869 -0.0237 202 ASP A O     
1676  C  CB    . ASP A 202 ? 0.7364 0.364  0.2836 -0.0774 0.1894 -0.0239 202 ASP A CB    
1677  C  CG    . ASP A 202 ? 0.784  0.4183 0.3387 -0.0734 0.1899 -0.0231 202 ASP A CG    
1678  O  OD1   . ASP A 202 ? 0.788  0.4304 0.3449 -0.0747 0.1888 -0.0226 202 ASP A OD1   
1679  O  OD2   . ASP A 202 ? 0.8103 0.4417 0.3683 -0.0691 0.1914 -0.0229 202 ASP A OD2   
1680  N  N     . GLU A 203 ? 0.6954 0.3472 0.251  -0.0837 0.1853 -0.0223 203 GLU A N     
1681  C  CA    . GLU A 203 ? 0.6873 0.3472 0.2489 -0.0832 0.1848 -0.0215 203 GLU A CA    
1682  C  C     . GLU A 203 ? 0.6777 0.3386 0.2462 -0.0778 0.186  -0.0214 203 GLU A C     
1683  O  O     . GLU A 203 ? 0.678  0.3433 0.2503 -0.0771 0.1858 -0.021  203 GLU A O     
1684  C  CB    . GLU A 203 ? 0.7113 0.3821 0.2752 -0.0853 0.1836 -0.02   203 GLU A CB    
1685  C  CG    . GLU A 203 ? 0.7692 0.4403 0.3269 -0.0916 0.182  -0.0198 203 GLU A CG    
1686  C  CD    . GLU A 203 ? 0.8328 0.5156 0.3928 -0.0943 0.1806 -0.0179 203 GLU A CD    
1687  O  OE1   . GLU A 203 ? 0.8372 0.5288 0.4042 -0.0908 0.1811 -0.0164 203 GLU A OE1   
1688  O  OE2   . GLU A 203 ? 0.8614 0.5445 0.4159 -0.0999 0.179  -0.0176 203 GLU A OE2   
1689  N  N     . THR A 204 ? 0.6701 0.3265 0.2397 -0.0742 0.1872 -0.0218 204 THR A N     
1690  C  CA    . THR A 204 ? 0.6683 0.3248 0.2439 -0.0697 0.1881 -0.0217 204 THR A CA    
1691  C  C     . THR A 204 ? 0.6696 0.3203 0.2443 -0.0696 0.1881 -0.0224 204 THR A C     
1692  O  O     . THR A 204 ? 0.6717 0.3232 0.251  -0.0668 0.1883 -0.0223 204 THR A O     
1693  C  CB    . THR A 204 ? 0.683  0.3371 0.2605 -0.0661 0.1894 -0.0216 204 THR A CB    
1694  O  OG1   . THR A 204 ? 0.6995 0.3446 0.2728 -0.0658 0.1902 -0.0222 204 THR A OG1   
1695  C  CG2   . THR A 204 ? 0.6859 0.3446 0.2631 -0.0663 0.1895 -0.0211 204 THR A CG2   
1696  N  N     . ILE A 205 ? 0.6653 0.3102 0.2337 -0.0727 0.1878 -0.0231 205 ILE A N     
1697  C  CA    . ILE A 205 ? 0.665  0.3043 0.2317 -0.0728 0.1878 -0.0236 205 ILE A CA    
1698  C  C     . ILE A 205 ? 0.6565 0.3008 0.2262 -0.0735 0.1869 -0.0234 205 ILE A C     
1699  O  O     . ILE A 205 ? 0.6565 0.2984 0.2279 -0.0718 0.1869 -0.0236 205 ILE A O     
1700  C  CB    . ILE A 205 ? 0.6772 0.3085 0.2351 -0.0761 0.188  -0.0243 205 ILE A CB    
1701  C  CG1   . ILE A 205 ? 0.6875 0.3117 0.242  -0.0742 0.1895 -0.0243 205 ILE A CG1   
1702  C  CG2   . ILE A 205 ? 0.6886 0.3151 0.244  -0.0769 0.1879 -0.0248 205 ILE A CG2   
1703  C  CD1   . ILE A 205 ? 0.7073 0.3229 0.252  -0.0774 0.19   -0.0249 205 ILE A CD1   
1704  N  N     . PHE A 206 ? 0.6498 0.3015 0.2204 -0.0757 0.1861 -0.0228 206 PHE A N     
1705  C  CA    . PHE A 206 ? 0.6526 0.3092 0.226  -0.0761 0.1856 -0.0223 206 PHE A CA    
1706  C  C     . PHE A 206 ? 0.6566 0.3144 0.2355 -0.0718 0.1861 -0.0221 206 PHE A C     
1707  O  O     . PHE A 206 ? 0.6537 0.3136 0.2361 -0.069  0.1867 -0.0217 206 PHE A O     
1708  C  CB    . PHE A 206 ? 0.6472 0.3125 0.2212 -0.0786 0.185  -0.0211 206 PHE A CB    
1709  C  CG    . PHE A 206 ? 0.6558 0.3201 0.224  -0.0837 0.1842 -0.0212 206 PHE A CG    
1710  C  CD1   . PHE A 206 ? 0.6699 0.3281 0.2331 -0.0866 0.1839 -0.0221 206 PHE A CD1   
1711  C  CD2   . PHE A 206 ? 0.6631 0.3326 0.2304 -0.086  0.1836 -0.0204 206 PHE A CD2   
1712  C  CE1   . PHE A 206 ? 0.6817 0.3382 0.2387 -0.0918 0.1831 -0.0222 206 PHE A CE1   
1713  C  CE2   . PHE A 206 ? 0.6753 0.3437 0.2367 -0.0913 0.1825 -0.0205 206 PHE A CE2   
1714  C  CZ    . PHE A 206 ? 0.678  0.3397 0.2341 -0.0944 0.1823 -0.0214 206 PHE A CZ    
1715  N  N     . ALA A 207 ? 0.6601 0.316  0.2394 -0.0714 0.1858 -0.0223 207 ALA A N     
1716  C  CA    . ALA A 207 ? 0.6649 0.3204 0.2482 -0.0679 0.1859 -0.0222 207 ALA A CA    
1717  C  C     . ALA A 207 ? 0.6653 0.325  0.2504 -0.0674 0.1859 -0.0215 207 ALA A C     
1718  O  O     . ALA A 207 ? 0.6666 0.3237 0.253  -0.0655 0.1857 -0.0218 207 ALA A O     
1719  C  CB    . ALA A 207 ? 0.6691 0.3174 0.2511 -0.0671 0.1856 -0.023  207 ALA A CB    
1720  N  N     . GLU A 208 ? 0.6634 0.3296 0.2486 -0.0688 0.1862 -0.0205 208 GLU A N     
1721  C  CA    . GLU A 208 ? 0.6703 0.3403 0.2568 -0.0678 0.1866 -0.0195 208 GLU A CA    
1722  C  C     . GLU A 208 ? 0.6715 0.3415 0.261  -0.0639 0.1874 -0.0191 208 GLU A C     
1723  O  O     . GLU A 208 ? 0.6754 0.3426 0.2646 -0.0626 0.1874 -0.0193 208 GLU A O     
1724  C  CB    . GLU A 208 ? 0.6985 0.3767 0.2853 -0.0695 0.187  -0.0178 208 GLU A CB    
1725  C  CG    . GLU A 208 ? 0.7532 0.4315 0.3367 -0.0738 0.1862 -0.0178 208 GLU A CG    
1726  C  CD    . GLU A 208 ? 0.8132 0.4923 0.3943 -0.0772 0.1855 -0.0181 208 GLU A CD    
1727  O  OE1   . GLU A 208 ? 0.8133 0.4901 0.3947 -0.076  0.1855 -0.0188 208 GLU A OE1   
1728  O  OE2   . GLU A 208 ? 0.839  0.5206 0.4177 -0.0811 0.1849 -0.0175 208 GLU A OE2   
1729  N  N     . ASP A 209 ? 0.666  0.3385 0.2578 -0.0621 0.1881 -0.0188 209 ASP A N     
1730  C  CA    . ASP A 209 ? 0.6696 0.3417 0.2637 -0.0587 0.1891 -0.0185 209 ASP A CA    
1731  C  C     . ASP A 209 ? 0.6645 0.3297 0.259  -0.0577 0.1883 -0.0197 209 ASP A C     
1732  O  O     . ASP A 209 ? 0.6678 0.3309 0.2627 -0.056  0.1885 -0.0197 209 ASP A O     
1733  C  CB    . ASP A 209 ? 0.7015 0.3779 0.2978 -0.0571 0.1901 -0.0177 209 ASP A CB    
1734  C  CG    . ASP A 209 ? 0.774  0.4583 0.3708 -0.0567 0.1912 -0.0159 209 ASP A CG    
1735  O  OD1   . ASP A 209 ? 0.784  0.4712 0.3794 -0.0586 0.191  -0.0151 209 ASP A OD1   
1736  O  OD2   . ASP A 209 ? 0.8072 0.4948 0.4057 -0.0543 0.1925 -0.015  209 ASP A OD2   
1737  N  N     . ASP A 210 ? 0.6556 0.3173 0.2499 -0.0588 0.1875 -0.0206 210 ASP A N     
1738  C  CA    . ASP A 210 ? 0.6528 0.3092 0.2481 -0.0578 0.1867 -0.0213 210 ASP A CA    
1739  C  C     . ASP A 210 ? 0.6428 0.2953 0.2364 -0.0585 0.1856 -0.0217 210 ASP A C     
1740  O  O     . ASP A 210 ? 0.6457 0.2951 0.2406 -0.0574 0.1849 -0.0219 210 ASP A O     
1741  C  CB    . ASP A 210 ? 0.6787 0.3327 0.2742 -0.0581 0.1866 -0.0217 210 ASP A CB    
1742  C  CG    . ASP A 210 ? 0.7421 0.3987 0.3397 -0.0567 0.1877 -0.0213 210 ASP A CG    
1743  O  OD1   . ASP A 210 ? 0.7495 0.4091 0.3492 -0.055  0.1885 -0.0208 210 ASP A OD1   
1744  O  OD2   . ASP A 210 ? 0.7743 0.4294 0.3709 -0.0572 0.188  -0.0215 210 ASP A OD2   
1745  N  N     . ILE A 211 ? 0.629  0.2817 0.2197 -0.0605 0.1854 -0.0219 211 ILE A N     
1746  C  CA    . ILE A 211 ? 0.6224 0.2714 0.211  -0.061  0.1844 -0.0222 211 ILE A CA    
1747  C  C     . ILE A 211 ? 0.6044 0.254  0.1932 -0.0596 0.1847 -0.0218 211 ILE A C     
1748  O  O     . ILE A 211 ? 0.6041 0.2496 0.1924 -0.0589 0.1838 -0.0221 211 ILE A O     
1749  C  CB    . ILE A 211 ? 0.6349 0.2836 0.2201 -0.0637 0.1843 -0.0225 211 ILE A CB    
1750  C  CG1   . ILE A 211 ? 0.6515 0.2966 0.235  -0.0649 0.184  -0.0231 211 ILE A CG1   
1751  C  CG2   . ILE A 211 ? 0.6443 0.2901 0.2271 -0.064  0.1837 -0.0226 211 ILE A CG2   
1752  C  CD1   . ILE A 211 ? 0.6713 0.3113 0.2554 -0.0635 0.1832 -0.0234 211 ILE A CD1   
1753  N  N     . ALA A 212 ? 0.5893 0.2437 0.1783 -0.0589 0.1861 -0.0208 212 ALA A N     
1754  C  CA    . ALA A 212 ? 0.5845 0.2389 0.1728 -0.057  0.187  -0.0201 212 ALA A CA    
1755  C  C     . ALA A 212 ? 0.5786 0.2297 0.1682 -0.0552 0.1869 -0.0204 212 ALA A C     
1756  O  O     . ALA A 212 ? 0.584  0.2308 0.1717 -0.0545 0.1864 -0.0206 212 ALA A O     
1757  C  CB    . ALA A 212 ? 0.5824 0.2433 0.1712 -0.0562 0.1889 -0.0186 212 ALA A CB    
1758  N  N     . ASP A 213 ? 0.5665 0.2191 0.1591 -0.0546 0.1871 -0.0205 213 ASP A N     
1759  C  CA    . ASP A 213 ? 0.5658 0.2158 0.1601 -0.0532 0.1869 -0.0207 213 ASP A CA    
1760  C  C     . ASP A 213 ? 0.5658 0.2108 0.1601 -0.0541 0.1849 -0.0214 213 ASP A C     
1761  O  O     . ASP A 213 ? 0.5664 0.2081 0.1603 -0.0536 0.1843 -0.0214 213 ASP A O     
1762  C  CB    . ASP A 213 ? 0.5821 0.2349 0.1796 -0.0526 0.1876 -0.0206 213 ASP A CB    
1763  C  CG    . ASP A 213 ? 0.6267 0.2844 0.2246 -0.0511 0.1896 -0.0197 213 ASP A CG    
1764  O  OD1   . ASP A 213 ? 0.6347 0.2937 0.2306 -0.0501 0.1908 -0.0189 213 ASP A OD1   
1765  O  OD2   . ASP A 213 ? 0.646  0.3063 0.2459 -0.0508 0.1902 -0.0196 213 ASP A OD2   
1766  N  N     . TYR A 214 ? 0.5673 0.2115 0.1618 -0.0555 0.1838 -0.0218 214 TYR A N     
1767  C  CA    . TYR A 214 ? 0.5779 0.2181 0.1726 -0.0561 0.1819 -0.0221 214 TYR A CA    
1768  C  C     . TYR A 214 ? 0.5829 0.2198 0.1743 -0.0565 0.1809 -0.0223 214 TYR A C     
1769  O  O     . TYR A 214 ? 0.5871 0.2209 0.1787 -0.0566 0.1795 -0.0223 214 TYR A O     
1770  C  CB    . TYR A 214 ? 0.5832 0.223  0.1776 -0.0572 0.1814 -0.0223 214 TYR A CB    
1771  C  CG    . TYR A 214 ? 0.5997 0.2359 0.1941 -0.0575 0.1797 -0.0223 214 TYR A CG    
1772  C  CD1   . TYR A 214 ? 0.612  0.2477 0.2098 -0.0567 0.1789 -0.0216 214 TYR A CD1   
1773  C  CD2   . TYR A 214 ? 0.616  0.2496 0.2071 -0.0584 0.1788 -0.0226 214 TYR A CD2   
1774  C  CE1   . TYR A 214 ? 0.6251 0.2586 0.2234 -0.0568 0.1772 -0.0211 214 TYR A CE1   
1775  C  CE2   . TYR A 214 ? 0.629  0.2596 0.2201 -0.0585 0.1771 -0.0224 214 TYR A CE2   
1776  C  CZ    . TYR A 214 ? 0.6388 0.2696 0.2335 -0.0577 0.1762 -0.0215 214 TYR A CZ    
1777  O  OH    . TYR A 214 ? 0.6571 0.286  0.2522 -0.0576 0.1745 -0.0209 214 TYR A OH    
1778  N  N     . ILE A 215 ? 0.5796 0.217  0.1679 -0.057  0.1816 -0.0224 215 ILE A N     
1779  C  CA    . ILE A 215 ? 0.5853 0.2191 0.1698 -0.0572 0.181  -0.0225 215 ILE A CA    
1780  C  C     . ILE A 215 ? 0.5896 0.221  0.1726 -0.056  0.1814 -0.0222 215 ILE A C     
1781  O  O     . ILE A 215 ? 0.5969 0.2238 0.1781 -0.0564 0.1799 -0.0225 215 ILE A O     
1782  C  CB    . ILE A 215 ? 0.5914 0.2268 0.1731 -0.0578 0.1821 -0.0223 215 ILE A CB    
1783  C  CG1   . ILE A 215 ? 0.602  0.2378 0.1839 -0.0595 0.1815 -0.0228 215 ILE A CG1   
1784  C  CG2   . ILE A 215 ? 0.5979 0.2293 0.1754 -0.0575 0.182  -0.0223 215 ILE A CG2   
1785  C  CD1   . ILE A 215 ? 0.6159 0.2544 0.1957 -0.0606 0.1827 -0.0224 215 ILE A CD1   
1786  N  N     . ILE A 216 ? 0.5843 0.2187 0.1679 -0.0546 0.1835 -0.0216 216 ILE A N     
1787  C  CA    . ILE A 216 ? 0.5907 0.2222 0.1721 -0.0532 0.1845 -0.0213 216 ILE A CA    
1788  C  C     . ILE A 216 ? 0.6016 0.2299 0.1845 -0.0538 0.1828 -0.0217 216 ILE A C     
1789  O  O     . ILE A 216 ? 0.6078 0.2307 0.1871 -0.054  0.1821 -0.0219 216 ILE A O     
1790  C  CB    . ILE A 216 ? 0.5906 0.2265 0.1724 -0.0512 0.1873 -0.0203 216 ILE A CB    
1791  C  CG1   . ILE A 216 ? 0.5997 0.2388 0.1796 -0.0508 0.1888 -0.0195 216 ILE A CG1   
1792  C  CG2   . ILE A 216 ? 0.5969 0.2288 0.1757 -0.0495 0.1886 -0.02   216 ILE A CG2   
1793  C  CD1   . ILE A 216 ? 0.6116 0.2571 0.1933 -0.0494 0.191  -0.0182 216 ILE A CD1   
1794  N  N     . ALA A 217 ? 0.6044 0.2355 0.1921 -0.0542 0.1821 -0.0218 217 ALA A N     
1795  C  CA    . ALA A 217 ? 0.6195 0.2485 0.2095 -0.0549 0.1805 -0.0218 217 ALA A CA    
1796  C  C     . ALA A 217 ? 0.6342 0.2595 0.223  -0.0566 0.1777 -0.022  217 ALA A C     
1797  O  O     . ALA A 217 ? 0.6402 0.2621 0.2282 -0.0576 0.1763 -0.0219 217 ALA A O     
1798  C  CB    . ALA A 217 ? 0.6193 0.2524 0.2148 -0.0546 0.1808 -0.0215 217 ALA A CB    
1799  N  N     . LYS A 218 ? 0.6385 0.2642 0.2267 -0.0572 0.1769 -0.0222 218 LYS A N     
1800  C  CA    . LYS A 218 ? 0.6497 0.2721 0.2365 -0.0585 0.1743 -0.0223 218 LYS A CA    
1801  C  C     . LYS A 218 ? 0.6606 0.2776 0.2415 -0.0589 0.1739 -0.0226 218 LYS A C     
1802  O  O     . LYS A 218 ? 0.6607 0.2741 0.2402 -0.0603 0.1716 -0.0225 218 LYS A O     
1803  C  CB    . LYS A 218 ? 0.6703 0.2938 0.2571 -0.0587 0.1741 -0.0225 218 LYS A CB    
1804  C  CG    . LYS A 218 ? 0.7166 0.3422 0.3076 -0.0588 0.1731 -0.0219 218 LYS A CG    
1805  C  CD    . LYS A 218 ? 0.769  0.3927 0.3609 -0.0597 0.1703 -0.0212 218 LYS A CD    
1806  C  CE    . LYS A 218 ? 0.8106 0.4359 0.4054 -0.0594 0.1695 -0.0203 218 LYS A CE    
1807  N  NZ    . LYS A 218 ? 0.8327 0.4615 0.4319 -0.0583 0.171  -0.0197 218 LYS A NZ    
1808  N  N     . LEU A 219 ? 0.669  0.2854 0.2461 -0.0578 0.1761 -0.0228 219 LEU A N     
1809  C  CA    . LEU A 219 ? 0.6868 0.2974 0.2574 -0.0576 0.1764 -0.0229 219 LEU A CA    
1810  C  C     . LEU A 219 ? 0.7043 0.3108 0.2727 -0.0578 0.1763 -0.0228 219 LEU A C     
1811  O  O     . LEU A 219 ? 0.7107 0.3108 0.2738 -0.0588 0.1751 -0.023  219 LEU A O     
1812  C  CB    . LEU A 219 ? 0.6885 0.3007 0.2565 -0.0558 0.1794 -0.0225 219 LEU A CB    
1813  C  CG    . LEU A 219 ? 0.7057 0.3209 0.2744 -0.0561 0.1796 -0.0226 219 LEU A CG    
1814  C  CD1   . LEU A 219 ? 0.713  0.3315 0.2804 -0.0545 0.1826 -0.0218 219 LEU A CD1   
1815  C  CD2   . LEU A 219 ? 0.7157 0.3259 0.2805 -0.0571 0.1777 -0.023  219 LEU A CD2   
1816  N  N     . GLN A 220 ? 0.7086 0.3184 0.2808 -0.0571 0.1776 -0.0225 220 GLN A N     
1817  C  CA    . GLN A 220 ? 0.7231 0.3293 0.2936 -0.0574 0.1778 -0.0224 220 GLN A CA    
1818  C  C     . GLN A 220 ? 0.7311 0.3367 0.3048 -0.0599 0.1747 -0.0224 220 GLN A C     
1819  O  O     . GLN A 220 ? 0.7363 0.3385 0.3084 -0.0608 0.1745 -0.0223 220 GLN A O     
1820  C  CB    . GLN A 220 ? 0.7466 0.357  0.3201 -0.0553 0.1807 -0.022  220 GLN A CB    
1821  C  CG    . GLN A 220 ? 0.8011 0.4119 0.3708 -0.0527 0.1841 -0.0216 220 GLN A CG    
1822  C  CD    . GLN A 220 ? 0.8764 0.4803 0.4391 -0.0516 0.186  -0.0213 220 GLN A CD    
1823  O  OE1   . GLN A 220 ? 0.9    0.5032 0.4587 -0.0492 0.1889 -0.0205 220 GLN A OE1   
1824  N  NE2   . GLN A 220 ? 0.8918 0.4905 0.4529 -0.0534 0.1846 -0.0217 220 GLN A NE2   
1825  N  N     . HIS A 221 ? 0.7313 0.3401 0.3093 -0.0609 0.1724 -0.0222 221 HIS A N     
1826  C  CA    . HIS A 221 ? 0.7379 0.3482 0.3203 -0.0629 0.1695 -0.0216 221 HIS A CA    
1827  C  C     . HIS A 221 ? 0.7308 0.3443 0.3182 -0.0626 0.1705 -0.021  221 HIS A C     
1828  O  O     . HIS A 221 ? 0.734  0.3453 0.3212 -0.0643 0.1693 -0.0206 221 HIS A O     
1829  C  CB    . HIS A 221 ? 0.7621 0.3667 0.3401 -0.0656 0.1664 -0.0215 221 HIS A CB    
1830  C  CG    . HIS A 221 ? 0.8026 0.4103 0.3859 -0.0675 0.1631 -0.0204 221 HIS A CG    
1831  N  ND1   . HIS A 221 ? 0.8268 0.4382 0.4135 -0.0671 0.1618 -0.0199 221 HIS A ND1   
1832  C  CD2   . HIS A 221 ? 0.8189 0.4271 0.4048 -0.0697 0.1611 -0.0195 221 HIS A CD2   
1833  C  CE1   . HIS A 221 ? 0.8311 0.4454 0.4225 -0.0687 0.1592 -0.0184 221 HIS A CE1   
1834  N  NE2   . HIS A 221 ? 0.8306 0.4436 0.4221 -0.0705 0.1586 -0.0181 221 HIS A NE2   
1835  N  N     . ARG A 222 ? 0.7192 0.3378 0.3106 -0.0605 0.1727 -0.0209 222 ARG A N     
1836  C  CA    . ARG A 222 ? 0.713  0.335  0.3093 -0.0598 0.174  -0.0204 222 ARG A CA    
1837  C  C     . ARG A 222 ? 0.7084 0.3356 0.3111 -0.0593 0.1734 -0.0196 222 ARG A C     
1838  O  O     . ARG A 222 ? 0.7124 0.3405 0.3151 -0.0593 0.1726 -0.0196 222 ARG A O     
1839  C  CB    . ARG A 222 ? 0.7236 0.3465 0.3183 -0.0575 0.1775 -0.0208 222 ARG A CB    
1840  C  CG    . ARG A 222 ? 0.7564 0.3738 0.3446 -0.0573 0.1787 -0.0212 222 ARG A CG    
1841  C  CD    . ARG A 222 ? 0.7913 0.4103 0.378  -0.0546 0.1822 -0.0212 222 ARG A CD    
1842  N  NE    . ARG A 222 ? 0.8379 0.451  0.4182 -0.054  0.1838 -0.0213 222 ARG A NE    
1843  C  CZ    . ARG A 222 ? 0.8726 0.4852 0.449  -0.0515 0.1869 -0.021  222 ARG A CZ    
1844  N  NH1   . ARG A 222 ? 0.8664 0.4849 0.445  -0.0498 0.1882 -0.0207 222 ARG A NH1   
1845  N  NH2   . ARG A 222 ? 0.8781 0.4843 0.4479 -0.0507 0.1886 -0.0209 222 ARG A NH2   
1846  N  N     . ASP A 223 ? 0.6986 0.3288 0.3063 -0.0588 0.1741 -0.0187 223 ASP A N     
1847  C  CA    . ASP A 223 ? 0.6943 0.3289 0.3076 -0.058  0.174  -0.0177 223 ASP A CA    
1848  C  C     . ASP A 223 ? 0.688  0.3245 0.3006 -0.0561 0.1762 -0.0184 223 ASP A C     
1849  O  O     . ASP A 223 ? 0.6876 0.3249 0.2995 -0.0548 0.1785 -0.0189 223 ASP A O     
1850  C  CB    . ASP A 223 ? 0.7135 0.3505 0.332  -0.0577 0.1746 -0.0165 223 ASP A CB    
1851  C  CG    . ASP A 223 ? 0.7706 0.4117 0.3945 -0.0563 0.175  -0.0151 223 ASP A CG    
1852  O  OD1   . ASP A 223 ? 0.7748 0.4165 0.3991 -0.0564 0.1736 -0.0145 223 ASP A OD1   
1853  O  OD2   . ASP A 223 ? 0.8045 0.4477 0.4315 -0.0548 0.177  -0.0146 223 ASP A OD2   
1854  N  N     . THR A 224 ? 0.6825 0.3194 0.2949 -0.056  0.1755 -0.0183 224 THR A N     
1855  C  CA    . THR A 224 ? 0.6829 0.3211 0.294  -0.0549 0.1773 -0.0189 224 THR A CA    
1856  C  C     . THR A 224 ? 0.6773 0.3177 0.292  -0.0537 0.1783 -0.018  224 THR A C     
1857  O  O     . THR A 224 ? 0.6783 0.3189 0.2912 -0.0532 0.1795 -0.0184 224 THR A O     
1858  C  CB    . THR A 224 ? 0.6988 0.335  0.3059 -0.0558 0.1764 -0.0196 224 THR A CB    
1859  O  OG1   . THR A 224 ? 0.709  0.3441 0.3172 -0.0564 0.1742 -0.0187 224 THR A OG1   
1860  C  CG2   . THR A 224 ? 0.7053 0.3392 0.3079 -0.0564 0.1763 -0.0205 224 THR A CG2   
1861  N  N     . SER A 225 ? 0.6676 0.3094 0.287  -0.0532 0.1779 -0.0165 225 SER A N     
1862  C  CA    . SER A 225 ? 0.6633 0.3068 0.2859 -0.0516 0.1791 -0.0153 225 SER A CA    
1863  C  C     . SER A 225 ? 0.6543 0.2983 0.2758 -0.0503 0.1817 -0.016  225 SER A C     
1864  O  O     . SER A 225 ? 0.6543 0.2977 0.2748 -0.0494 0.1828 -0.0158 225 SER A O     
1865  C  CB    . SER A 225 ? 0.6826 0.3281 0.3107 -0.0512 0.1786 -0.0134 225 SER A CB    
1866  O  OG    . SER A 225 ? 0.7201 0.3658 0.3496 -0.0525 0.176  -0.0122 225 SER A OG    
1867  N  N     . ASN A 226 ? 0.6476 0.2924 0.2688 -0.0502 0.1827 -0.0168 226 ASN A N     
1868  C  CA    . ASN A 226 ? 0.6468 0.2927 0.267  -0.0491 0.1849 -0.0174 226 ASN A CA    
1869  C  C     . ASN A 226 ? 0.638  0.2835 0.2536 -0.0499 0.1852 -0.0185 226 ASN A C     
1870  O  O     . ASN A 226 ? 0.6371 0.2826 0.2515 -0.0494 0.1864 -0.0186 226 ASN A O     
1871  C  CB    . ASN A 226 ? 0.6656 0.3126 0.2863 -0.0486 0.1859 -0.0177 226 ASN A CB    
1872  C  CG    . ASN A 226 ? 0.713  0.3604 0.338  -0.048  0.1861 -0.0166 226 ASN A CG    
1873  O  OD1   . ASN A 226 ? 0.7284 0.3764 0.3569 -0.0474 0.1859 -0.0153 226 ASN A OD1   
1874  N  ND2   . ASN A 226 ? 0.7254 0.3726 0.3502 -0.048  0.1866 -0.0169 226 ASN A ND2   
1875  N  N     . ILE A 227 ? 0.6294 0.2742 0.2422 -0.0512 0.1841 -0.0193 227 ILE A N     
1876  C  CA    . ILE A 227 ? 0.6237 0.2684 0.2324 -0.0522 0.1843 -0.0202 227 ILE A CA    
1877  C  C     . ILE A 227 ? 0.6132 0.2557 0.2204 -0.0528 0.1838 -0.02   227 ILE A C     
1878  O  O     . ILE A 227 ? 0.6143 0.2566 0.2187 -0.0534 0.1847 -0.0205 227 ILE A O     
1879  C  CB    . ILE A 227 ? 0.6315 0.2757 0.2375 -0.0532 0.1835 -0.0208 227 ILE A CB    
1880  C  CG1   . ILE A 227 ? 0.6457 0.2907 0.2523 -0.0523 0.1842 -0.0207 227 ILE A CG1   
1881  C  CG2   . ILE A 227 ? 0.638  0.2833 0.2404 -0.0542 0.184  -0.0214 227 ILE A CG2   
1882  C  CD1   . ILE A 227 ? 0.6665 0.3097 0.27   -0.0529 0.1836 -0.021  227 ILE A CD1   
1883  N  N     . GLU A 228 ? 0.6013 0.2421 0.2102 -0.0525 0.1826 -0.0193 228 GLU A N     
1884  C  CA    . GLU A 228 ? 0.5972 0.2355 0.2046 -0.0524 0.1824 -0.0188 228 GLU A CA    
1885  C  C     . GLU A 228 ? 0.6036 0.2414 0.2111 -0.0512 0.1843 -0.0182 228 GLU A C     
1886  O  O     . GLU A 228 ? 0.6093 0.2446 0.2127 -0.0517 0.1851 -0.0186 228 GLU A O     
1887  C  CB    . GLU A 228 ? 0.5995 0.2372 0.2096 -0.052  0.1807 -0.0175 228 GLU A CB    
1888  C  CG    . GLU A 228 ? 0.5985 0.2352 0.2067 -0.0535 0.1788 -0.0182 228 GLU A CG    
1889  C  CD    . GLU A 228 ? 0.5937 0.2303 0.2044 -0.0535 0.1767 -0.0169 228 GLU A CD    
1890  O  OE1   . GLU A 228 ? 0.5767 0.2133 0.1891 -0.0523 0.1768 -0.0153 228 GLU A OE1   
1891  O  OE2   . GLU A 228 ? 0.6072 0.2435 0.2177 -0.0547 0.175  -0.0172 228 GLU A OE2   
1892  N  N     . GLN A 229 ? 0.6023 0.2419 0.2137 -0.0497 0.1852 -0.0174 229 GLN A N     
1893  C  CA    . GLN A 229 ? 0.6087 0.2473 0.2198 -0.0483 0.1871 -0.0168 229 GLN A CA    
1894  C  C     . GLN A 229 ? 0.6097 0.248  0.2165 -0.0493 0.1882 -0.0181 229 GLN A C     
1895  O  O     . GLN A 229 ? 0.6145 0.2497 0.2178 -0.0492 0.1895 -0.018  229 GLN A O     
1896  C  CB    . GLN A 229 ? 0.631  0.2716 0.2473 -0.0464 0.1879 -0.0155 229 GLN A CB    
1897  C  CG    . GLN A 229 ? 0.6813 0.3211 0.3005 -0.0444 0.1884 -0.0133 229 GLN A CG    
1898  C  CD    . GLN A 229 ? 0.7475 0.3831 0.3623 -0.0433 0.1902 -0.0129 229 GLN A CD    
1899  O  OE1   . GLN A 229 ? 0.7679 0.4012 0.3812 -0.0428 0.1901 -0.0119 229 GLN A OE1   
1900  N  NE2   . GLN A 229 ? 0.7583 0.3925 0.3703 -0.043  0.192  -0.0136 229 GLN A NE2   
1901  N  N     . LEU A 230 ? 0.6052 0.2464 0.2117 -0.0505 0.1878 -0.0191 230 LEU A N     
1902  C  CA    . LEU A 230 ? 0.6102 0.2524 0.2131 -0.0518 0.1885 -0.02   230 LEU A CA    
1903  C  C     . LEU A 230 ? 0.6103 0.2498 0.2081 -0.0539 0.1881 -0.0207 230 LEU A C     
1904  O  O     . LEU A 230 ? 0.6145 0.2523 0.2083 -0.055  0.1889 -0.021  230 LEU A O     
1905  C  CB    . LEU A 230 ? 0.6165 0.263  0.2205 -0.0521 0.1883 -0.0205 230 LEU A CB    
1906  C  CG    . LEU A 230 ? 0.6418 0.2908 0.2497 -0.0502 0.1892 -0.02   230 LEU A CG    
1907  C  CD1   . LEU A 230 ? 0.651  0.3034 0.2589 -0.0503 0.1894 -0.0203 230 LEU A CD1   
1908  C  CD2   . LEU A 230 ? 0.6518 0.3009 0.2595 -0.0492 0.1907 -0.0197 230 LEU A CD2   
1909  N  N     . LEU A 231 ? 0.6044 0.243  0.2018 -0.0547 0.1868 -0.0209 231 LEU A N     
1910  C  CA    . LEU A 231 ? 0.607  0.2427 0.1994 -0.0567 0.1864 -0.0215 231 LEU A CA    
1911  C  C     . LEU A 231 ? 0.6103 0.2406 0.1998 -0.0561 0.1873 -0.021  231 LEU A C     
1912  O  O     . LEU A 231 ? 0.6188 0.2459 0.2027 -0.0579 0.1878 -0.0216 231 LEU A O     
1913  C  CB    . LEU A 231 ? 0.607  0.2428 0.1998 -0.0573 0.1849 -0.0217 231 LEU A CB    
1914  C  CG    . LEU A 231 ? 0.6208 0.2607 0.2143 -0.0581 0.1845 -0.0222 231 LEU A CG    
1915  C  CD1   . LEU A 231 ? 0.624  0.2631 0.2179 -0.058  0.1832 -0.0222 231 LEU A CD1   
1916  C  CD2   . LEU A 231 ? 0.6312 0.2726 0.221  -0.0604 0.185  -0.0227 231 LEU A CD2   
1917  N  N     . ILE A 232 ? 0.6005 0.2297 0.1933 -0.0536 0.1876 -0.0197 232 ILE A N     
1918  C  CA    . ILE A 232 ? 0.6003 0.2244 0.1904 -0.0522 0.1889 -0.0187 232 ILE A CA    
1919  C  C     . ILE A 232 ? 0.6005 0.2225 0.1872 -0.0522 0.1907 -0.0189 232 ILE A C     
1920  O  O     . ILE A 232 ? 0.601  0.2174 0.1814 -0.0529 0.1919 -0.0191 232 ILE A O     
1921  C  CB    . ILE A 232 ? 0.6037 0.2288 0.1993 -0.0493 0.1889 -0.0168 232 ILE A CB    
1922  C  CG1   . ILE A 232 ? 0.6158 0.2423 0.2138 -0.0495 0.1868 -0.0165 232 ILE A CG1   
1923  C  CG2   . ILE A 232 ? 0.6117 0.2321 0.205  -0.047  0.1909 -0.0152 232 ILE A CG2   
1924  C  CD1   . ILE A 232 ? 0.6388 0.2613 0.2316 -0.0505 0.1866 -0.0169 232 ILE A CD1   
1925  N  N     . ASN A 233 ? 0.5988 0.2246 0.1888 -0.0517 0.191  -0.019  233 ASN A N     
1926  C  CA    . ASN A 233 ? 0.6066 0.2307 0.1934 -0.0517 0.1925 -0.0192 233 ASN A CA    
1927  C  C     . ASN A 233 ? 0.6041 0.2267 0.1843 -0.0552 0.1922 -0.0206 233 ASN A C     
1928  O  O     . ASN A 233 ? 0.61   0.2279 0.1845 -0.0559 0.1935 -0.0207 233 ASN A O     
1929  C  CB    . ASN A 233 ? 0.6259 0.2548 0.2178 -0.0504 0.1928 -0.019  233 ASN A CB    
1930  C  CG    . ASN A 233 ? 0.67   0.299  0.267  -0.0471 0.1938 -0.0173 233 ASN A CG    
1931  O  OD1   . ASN A 233 ? 0.684  0.3095 0.2807 -0.0454 0.1945 -0.016  233 ASN A OD1   
1932  N  ND2   . ASN A 233 ? 0.6761 0.3093 0.278  -0.046  0.1939 -0.0171 233 ASN A ND2   
1933  N  N     . LYS A 234 ? 0.5929 0.2194 0.1737 -0.0575 0.1907 -0.0215 234 LYS A N     
1934  C  CA    . LYS A 234 ? 0.5919 0.218  0.167  -0.0612 0.1902 -0.0225 234 LYS A CA    
1935  C  C     . LYS A 234 ? 0.5988 0.2178 0.1674 -0.0627 0.1906 -0.0228 234 LYS A C     
1936  O  O     . LYS A 234 ? 0.6054 0.2206 0.1673 -0.0654 0.191  -0.0234 234 LYS A O     
1937  C  CB    . LYS A 234 ? 0.5997 0.2322 0.1776 -0.0628 0.1888 -0.0229 234 LYS A CB    
1938  C  CG    . LYS A 234 ? 0.6232 0.2621 0.2059 -0.0616 0.1888 -0.0225 234 LYS A CG    
1939  C  CD    . LYS A 234 ? 0.654  0.2988 0.2388 -0.0626 0.1879 -0.0226 234 LYS A CD    
1940  C  CE    . LYS A 234 ? 0.6879 0.3383 0.2766 -0.061  0.1884 -0.0221 234 LYS A CE    
1941  N  NZ    . LYS A 234 ? 0.7177 0.374  0.3071 -0.0621 0.188  -0.0217 234 LYS A NZ    
1942  N  N     . ASN A 235 ? 0.5954 0.2122 0.1656 -0.0609 0.1905 -0.0223 235 ASN A N     
1943  C  CA    . ASN A 235 ? 0.6027 0.2124 0.1669 -0.0614 0.1912 -0.0223 235 ASN A CA    
1944  C  C     . ASN A 235 ? 0.6002 0.203  0.1593 -0.06   0.1934 -0.0216 235 ASN A C     
1945  O  O     . ASN A 235 ? 0.6042 0.2002 0.1552 -0.0619 0.1943 -0.0221 235 ASN A O     
1946  C  CB    . ASN A 235 ? 0.623  0.2329 0.1909 -0.0591 0.1905 -0.0215 235 ASN A CB    
1947  C  CG    . ASN A 235 ? 0.671  0.2748 0.2332 -0.0598 0.1909 -0.0216 235 ASN A CG    
1948  O  OD1   . ASN A 235 ? 0.6864 0.2837 0.2411 -0.0611 0.1924 -0.0219 235 ASN A OD1   
1949  N  ND2   . ASN A 235 ? 0.6795 0.2848 0.2446 -0.059  0.1897 -0.0213 235 ASN A ND2   
1950  N  N     . LEU A 236 ? 0.594  0.1981 0.1575 -0.0567 0.1943 -0.0205 236 LEU A N     
1951  C  CA    . LEU A 236 ? 0.5985 0.1962 0.1577 -0.0548 0.1967 -0.0196 236 LEU A CA    
1952  C  C     . LEU A 236 ? 0.6033 0.1985 0.1561 -0.0577 0.1971 -0.0207 236 LEU A C     
1953  O  O     . LEU A 236 ? 0.6081 0.1949 0.1525 -0.0581 0.1989 -0.0207 236 LEU A O     
1954  C  CB    . LEU A 236 ? 0.5931 0.194  0.1596 -0.0507 0.1975 -0.0179 236 LEU A CB    
1955  C  CG    . LEU A 236 ? 0.6083 0.2026 0.1711 -0.0476 0.2004 -0.0163 236 LEU A CG    
1956  C  CD1   . LEU A 236 ? 0.6198 0.208  0.1789 -0.0458 0.2017 -0.015  236 LEU A CD1   
1957  C  CD2   . LEU A 236 ? 0.608  0.2066 0.1785 -0.0441 0.201  -0.0147 236 LEU A CD2   
1958  N  N     . LYS A 237 ? 0.6007 0.2029 0.1569 -0.0598 0.1955 -0.0216 237 LYS A N     
1959  C  CA    . LYS A 237 ? 0.6104 0.2121 0.1613 -0.063  0.1953 -0.0225 237 LYS A CA    
1960  C  C     . LYS A 237 ? 0.6222 0.219  0.1646 -0.0675 0.1949 -0.0236 237 LYS A C     
1961  O  O     . LYS A 237 ? 0.631  0.2226 0.1656 -0.07   0.1954 -0.0241 237 LYS A O     
1962  C  CB    . LYS A 237 ? 0.6289 0.2403 0.1861 -0.0639 0.1937 -0.0228 237 LYS A CB    
1963  C  CG    . LYS A 237 ? 0.6808 0.2949 0.2427 -0.0606 0.1946 -0.0221 237 LYS A CG    
1964  C  CD    . LYS A 237 ? 0.7384 0.3486 0.2941 -0.0617 0.1956 -0.0222 237 LYS A CD    
1965  C  CE    . LYS A 237 ? 0.7787 0.3895 0.3283 -0.0668 0.1942 -0.0233 237 LYS A CE    
1966  N  NZ    . LYS A 237 ? 0.8089 0.4134 0.3504 -0.0682 0.1951 -0.0235 237 LYS A NZ    
1967  N  N     . MET A 238 ? 0.6215 0.2194 0.1647 -0.0686 0.1939 -0.0239 238 MET A N     
1968  C  CA    . MET A 238 ? 0.6353 0.2281 0.1703 -0.0728 0.1937 -0.0248 238 MET A CA    
1969  C  C     . MET A 238 ? 0.6537 0.2346 0.1799 -0.0718 0.196  -0.0246 238 MET A C     
1970  O  O     . MET A 238 ? 0.6655 0.2396 0.1822 -0.0754 0.1965 -0.0253 238 MET A O     
1971  C  CB    . MET A 238 ? 0.6374 0.2339 0.1755 -0.0738 0.1923 -0.0251 238 MET A CB    
1972  C  CG    . MET A 238 ? 0.6561 0.2471 0.1858 -0.0782 0.1922 -0.026  238 MET A CG    
1973  S  SD    . MET A 238 ? 0.6701 0.2637 0.1948 -0.0845 0.1909 -0.0268 238 MET A SD    
1974  C  CE    . MET A 238 ? 0.6448 0.2515 0.1789 -0.0852 0.1888 -0.0265 238 MET A CE    
1975  N  N     . VAL A 239 ? 0.6525 0.2308 0.1816 -0.0669 0.1976 -0.0233 239 VAL A N     
1976  C  CA    . VAL A 239 ? 0.6626 0.2298 0.1838 -0.0647 0.2004 -0.0224 239 VAL A CA    
1977  C  C     . VAL A 239 ? 0.6777 0.239  0.1921 -0.0653 0.2019 -0.0225 239 VAL A C     
1978  O  O     . VAL A 239 ? 0.6892 0.24   0.1925 -0.0669 0.2037 -0.0228 239 VAL A O     
1979  C  CB    . VAL A 239 ? 0.6621 0.2301 0.1896 -0.0589 0.2016 -0.0204 239 VAL A CB    
1980  C  CG1   . VAL A 239 ? 0.6725 0.2296 0.1922 -0.0559 0.205  -0.019  239 VAL A CG1   
1981  C  CG2   . VAL A 239 ? 0.6635 0.2357 0.1958 -0.0587 0.2001 -0.0204 239 VAL A CG2   
1982  N  N     . GLU A 240 ? 0.6774 0.2451 0.1978 -0.0643 0.2013 -0.0223 240 GLU A N     
1983  C  CA    . GLU A 240 ? 0.6889 0.2522 0.2037 -0.0648 0.2024 -0.0224 240 GLU A CA    
1984  C  C     . GLU A 240 ? 0.698  0.2584 0.2039 -0.0711 0.2011 -0.024  240 GLU A C     
1985  O  O     . GLU A 240 ? 0.7056 0.2556 0.2005 -0.0726 0.2027 -0.0243 240 GLU A O     
1986  C  CB    . GLU A 240 ? 0.7111 0.2834 0.2352 -0.0626 0.2016 -0.0219 240 GLU A CB    
1987  C  CG    . GLU A 240 ? 0.7715 0.3387 0.2909 -0.0614 0.2034 -0.0215 240 GLU A CG    
1988  C  CD    . GLU A 240 ? 0.8355 0.4072 0.354  -0.0649 0.2016 -0.0226 240 GLU A CD    
1989  O  OE1   . GLU A 240 ? 0.8418 0.415  0.3564 -0.0702 0.1996 -0.0238 240 GLU A OE1   
1990  O  OE2   . GLU A 240 ? 0.8628 0.4369 0.3845 -0.0625 0.2022 -0.022  240 GLU A OE2   
1991  N  N     . PHE A 241 ? 0.6964 0.2658 0.2067 -0.0749 0.1982 -0.025  241 PHE A N     
1992  C  CA    . PHE A 241 ? 0.7071 0.2758 0.2103 -0.0814 0.1966 -0.0262 241 PHE A CA    
1993  C  C     . PHE A 241 ? 0.7223 0.2792 0.2137 -0.0843 0.1979 -0.0268 241 PHE A C     
1994  O  O     . PHE A 241 ? 0.7283 0.2779 0.2092 -0.0883 0.1981 -0.0275 241 PHE A O     
1995  C  CB    . PHE A 241 ? 0.698  0.2788 0.2089 -0.0841 0.1938 -0.0265 241 PHE A CB    
1996  C  CG    . PHE A 241 ? 0.7062 0.2871 0.2104 -0.091  0.1921 -0.0274 241 PHE A CG    
1997  C  CD1   . PHE A 241 ? 0.716  0.2972 0.2155 -0.0947 0.1911 -0.0276 241 PHE A CD1   
1998  C  CD2   . PHE A 241 ? 0.7173 0.2976 0.2196 -0.094  0.1914 -0.0278 241 PHE A CD2   
1999  C  CE1   . PHE A 241 ? 0.7256 0.3074 0.219  -0.1016 0.1893 -0.0281 241 PHE A CE1   
2000  C  CE2   . PHE A 241 ? 0.7283 0.3089 0.2245 -0.1006 0.1899 -0.0284 241 PHE A CE2   
2001  C  CZ    . PHE A 241 ? 0.7252 0.3067 0.2171 -0.1046 0.1887 -0.0284 241 PHE A CZ    
2002  N  N     . LEU A 242 ? 0.7267 0.2816 0.2191 -0.0825 0.1986 -0.0266 242 LEU A N     
2003  C  CA    . LEU A 242 ? 0.7455 0.2893 0.2269 -0.0849 0.1999 -0.0271 242 LEU A CA    
2004  C  C     . LEU A 242 ? 0.7705 0.3003 0.2416 -0.0823 0.2034 -0.0265 242 LEU A C     
2005  O  O     . LEU A 242 ? 0.784  0.3031 0.2423 -0.0862 0.2044 -0.0273 242 LEU A O     
2006  C  CB    . LEU A 242 ? 0.7439 0.2901 0.23   -0.0832 0.1998 -0.0269 242 LEU A CB    
2007  C  CG    . LEU A 242 ? 0.7514 0.3095 0.2459 -0.086  0.1968 -0.0275 242 LEU A CG    
2008  C  CD1   . LEU A 242 ? 0.7542 0.3141 0.2536 -0.0832 0.1968 -0.0271 242 LEU A CD1   
2009  C  CD2   . LEU A 242 ? 0.7598 0.3174 0.2475 -0.0931 0.1953 -0.0286 242 LEU A CD2   
2010  N  N     . SER A 243 ? 0.7738 0.3033 0.2498 -0.0758 0.2054 -0.025  243 SER A N     
2011  C  CA    . SER A 243 ? 0.79   0.3066 0.2567 -0.0724 0.2092 -0.0239 243 SER A CA    
2012  C  C     . SER A 243 ? 0.8083 0.3186 0.2665 -0.0746 0.2098 -0.0244 243 SER A C     
2013  O  O     . SER A 243 ? 0.8262 0.3226 0.2711 -0.0751 0.2124 -0.0243 243 SER A O     
2014  C  CB    . SER A 243 ? 0.7973 0.3164 0.2724 -0.0649 0.2111 -0.0216 243 SER A CB    
2015  O  OG    . SER A 243 ? 0.8157 0.3453 0.3018 -0.0628 0.2097 -0.0211 243 SER A OG    
2016  N  N     . LYS A 244 ? 0.8029 0.3229 0.2679 -0.0761 0.2074 -0.0249 244 LYS A N     
2017  C  CA    . LYS A 244 ? 0.8125 0.3274 0.2696 -0.0787 0.2075 -0.0254 244 LYS A CA    
2018  C  C     . LYS A 244 ? 0.8311 0.3408 0.2768 -0.0868 0.2058 -0.0271 244 LYS A C     
2019  O  O     . LYS A 244 ? 0.8389 0.3416 0.275  -0.0896 0.206  -0.0276 244 LYS A O     
2020  C  CB    . LYS A 244 ? 0.8176 0.3442 0.2852 -0.0773 0.2057 -0.0251 244 LYS A CB    
2021  C  CG    . LYS A 244 ? 0.8504 0.3793 0.3265 -0.0698 0.2079 -0.0233 244 LYS A CG    
2022  C  CD    . LYS A 244 ? 0.8883 0.4282 0.3743 -0.0686 0.2063 -0.0231 244 LYS A CD    
2023  C  CE    . LYS A 244 ? 0.9359 0.4696 0.4157 -0.0675 0.2079 -0.0228 244 LYS A CE    
2024  N  NZ    . LYS A 244 ? 0.9502 0.4947 0.4378 -0.068  0.2058 -0.0231 244 LYS A NZ    
2025  N  N     . ASN A 245 ? 0.8379 0.3507 0.2843 -0.0905 0.2041 -0.0279 245 ASN A N     
2026  C  CA    . ASN A 245 ? 0.857  0.3652 0.293  -0.0984 0.2025 -0.0293 245 ASN A CA    
2027  C  C     . ASN A 245 ? 0.8771 0.3691 0.2989 -0.0996 0.2053 -0.0297 245 ASN A C     
2028  O  O     . ASN A 245 ? 0.8871 0.3729 0.2983 -0.1064 0.2043 -0.0309 245 ASN A O     
2029  C  CB    . ASN A 245 ? 0.8669 0.3886 0.3118 -0.1025 0.1989 -0.0299 245 ASN A CB    
2030  C  CG    . ASN A 245 ? 0.9071 0.4397 0.3566 -0.1063 0.1957 -0.03   245 ASN A CG    
2031  O  OD1   . ASN A 245 ? 0.932  0.4597 0.374  -0.1088 0.1956 -0.0303 245 ASN A OD1   
2032  N  ND2   . ASN A 245 ? 0.9059 0.4529 0.367  -0.107  0.1932 -0.0298 245 ASN A ND2   
2033  N  N     . THR A 246 ? 0.88   0.3653 0.3014 -0.0931 0.2087 -0.0285 246 THR A N     
2034  C  CA    . THR A 246 ? 0.8957 0.3652 0.3034 -0.0933 0.2119 -0.0286 246 THR A CA    
2035  C  C     . THR A 246 ? 0.907  0.3612 0.3023 -0.0903 0.2159 -0.0278 246 THR A C     
2036  O  O     . THR A 246 ? 0.905  0.3621 0.3056 -0.0856 0.2167 -0.0266 246 THR A O     
2037  C  CB    . THR A 246 ? 0.9101 0.3818 0.3245 -0.0881 0.2134 -0.0275 246 THR A CB    
2038  O  OG1   . THR A 246 ? 0.9176 0.394  0.3416 -0.0803 0.2149 -0.0256 246 THR A OG1   
2039  C  CG2   . THR A 246 ? 0.9088 0.3932 0.3332 -0.0911 0.21   -0.0283 246 THR A CG2   
2040  N  N     . LYS A 247 ? 0.9169 0.3543 0.2953 -0.0926 0.2186 -0.0282 247 LYS A N     
2041  C  CA    . LYS A 247 ? 0.9308 0.3511 0.295  -0.0896 0.223  -0.0273 247 LYS A CA    
2042  C  C     . LYS A 247 ? 0.9329 0.3533 0.3039 -0.0797 0.2266 -0.0247 247 LYS A C     
2043  O  O     . LYS A 247 ? 0.9299 0.3512 0.3042 -0.0768 0.2278 -0.0238 247 LYS A O     
2044  C  CB    . LYS A 247 ? 0.9652 0.3672 0.31   -0.0939 0.2253 -0.0282 247 LYS A CB    
2045  C  CG    . LYS A 247 ? 1.0174 0.4206 0.3568 -0.1041 0.2215 -0.0306 247 LYS A CG    
2046  C  CD    . LYS A 247 ? 1.0735 0.4678 0.4041 -0.1066 0.223  -0.0312 247 LYS A CD    
2047  C  CE    . LYS A 247 ? 1.1104 0.5172 0.4559 -0.1026 0.2222 -0.0305 247 LYS A CE    
2048  N  NZ    . LYS A 247 ? 1.1405 0.5394 0.4842 -0.0943 0.2269 -0.0285 247 LYS A NZ    
2049  N  N     . ASN A 248 ? 0.9359 0.3559 0.3091 -0.0747 0.2284 -0.0232 248 ASN A N     
2050  C  CA    . ASN A 248 ? 0.9397 0.3618 0.3209 -0.0655 0.2316 -0.0203 248 ASN A CA    
2051  C  C     . ASN A 248 ? 0.9514 0.3576 0.3204 -0.0606 0.2372 -0.0183 248 ASN A C     
2052  O  O     . ASN A 248 ? 0.9483 0.3583 0.3253 -0.0534 0.2394 -0.0157 248 ASN A O     
2053  C  CB    . ASN A 248 ? 0.9519 0.3779 0.3385 -0.0619 0.2321 -0.0192 248 ASN A CB    
2054  C  CG    . ASN A 248 ? 0.9827 0.4263 0.384  -0.0647 0.2271 -0.0204 248 ASN A CG    
2055  O  OD1   . ASN A 248 ? 0.9944 0.4403 0.3977 -0.064  0.2268 -0.0203 248 ASN A OD1   
2056  N  ND2   . ASN A 248 ? 0.9834 0.4396 0.3951 -0.0678 0.2234 -0.0216 248 ASN A ND2   
2057  N  N     . ASP A 249 ? 0.9621 0.3506 0.3118 -0.0644 0.2394 -0.0194 249 ASP A N     
2058  C  CA    . ASP A 249 ? 0.978  0.3499 0.3146 -0.0595 0.2452 -0.0173 249 ASP A CA    
2059  C  C     . ASP A 249 ? 0.9794 0.3535 0.3193 -0.0577 0.2458 -0.0167 249 ASP A C     
2060  O  O     . ASP A 249 ? 0.9851 0.3507 0.3201 -0.051  0.2506 -0.014  249 ASP A O     
2061  C  CB    . ASP A 249 ? 1.0165 0.3674 0.33   -0.0642 0.2477 -0.0187 249 ASP A CB    
2062  C  CG    . ASP A 249 ? 1.0819 0.4326 0.3893 -0.075  0.2433 -0.0223 249 ASP A CG    
2063  O  OD1   . ASP A 249 ? 1.088  0.4438 0.3989 -0.0782 0.2413 -0.0234 249 ASP A OD1   
2064  O  OD2   . ASP A 249 ? 1.1175 0.4628 0.4163 -0.0803 0.2419 -0.0238 249 ASP A OD2   
2065  N  N     . ASN A 250 ? 0.9714 0.3567 0.3194 -0.0632 0.2412 -0.0189 250 ASN A N     
2066  C  CA    . ASN A 250 ? 0.9744 0.3623 0.3259 -0.062  0.2413 -0.0185 250 ASN A CA    
2067  C  C     . ASN A 250 ? 0.9563 0.365  0.329  -0.0603 0.2373 -0.0182 250 ASN A C     
2068  O  O     . ASN A 250 ? 0.9555 0.3676 0.3321 -0.0593 0.2369 -0.0179 250 ASN A O     
2069  C  CB    . ASN A 250 ? 1.0013 0.3815 0.3411 -0.0703 0.2399 -0.0213 250 ASN A CB    
2070  C  CG    . ASN A 250 ? 1.0599 0.4179 0.3781 -0.0705 0.2449 -0.0211 250 ASN A CG    
2071  O  OD1   . ASN A 250 ? 1.08   0.4314 0.3917 -0.0711 0.2464 -0.0213 250 ASN A OD1   
2072  N  ND2   . ASN A 250 ? 1.0786 0.4237 0.3844 -0.07   0.2478 -0.0207 250 ASN A ND2   
2073  N  N     . ASN A 251 ? 0.938  0.3599 0.3233 -0.0603 0.2342 -0.0184 251 ASN A N     
2074  C  CA    . ASN A 251 ? 0.9215 0.3621 0.3258 -0.0591 0.2304 -0.0182 251 ASN A CA    
2075  C  C     . ASN A 251 ? 0.9117 0.3608 0.3276 -0.0531 0.2308 -0.016  251 ASN A C     
2076  O  O     . ASN A 251 ? 0.9214 0.3639 0.3314 -0.0518 0.2329 -0.0154 251 ASN A O     
2077  C  CB    . ASN A 251 ? 0.9243 0.3749 0.3336 -0.0669 0.2253 -0.0212 251 ASN A CB    
2078  C  CG    . ASN A 251 ? 0.9602 0.4036 0.3586 -0.0739 0.2244 -0.0234 251 ASN A CG    
2079  O  OD1   . ASN A 251 ? 0.98   0.4132 0.3653 -0.0791 0.2248 -0.0248 251 ASN A OD1   
2080  N  ND2   . ASN A 251 ? 0.9618 0.4106 0.3653 -0.0746 0.223  -0.0237 251 ASN A ND2   
2081  N  N     . PHE A 252 ? 0.8888 0.3524 0.3208 -0.05   0.2287 -0.0149 252 PHE A N     
2082  C  CA    . PHE A 252 ? 0.8741 0.3468 0.318  -0.045  0.2287 -0.0129 252 PHE A CA    
2083  C  C     . PHE A 252 ? 0.8657 0.344  0.3126 -0.049  0.2259 -0.0148 252 PHE A C     
2084  O  O     . PHE A 252 ? 0.8632 0.3464 0.3109 -0.0552 0.2224 -0.0175 252 PHE A O     
2085  C  CB    . PHE A 252 ? 0.8591 0.3465 0.3191 -0.0423 0.2262 -0.0118 252 PHE A CB    
2086  C  CG    . PHE A 252 ? 0.8625 0.3489 0.325  -0.0357 0.2289 -0.0084 252 PHE A CG    
2087  C  CD1   . PHE A 252 ? 0.8814 0.3539 0.3317 -0.032  0.2338 -0.0064 252 PHE A CD1   
2088  C  CD2   . PHE A 252 ? 0.8594 0.3586 0.336  -0.0333 0.2266 -0.0071 252 PHE A CD2   
2089  C  CE1   . PHE A 252 ? 0.8885 0.361  0.3415 -0.0256 0.2364 -0.003  252 PHE A CE1   
2090  C  CE2   . PHE A 252 ? 0.8666 0.3658 0.3457 -0.0275 0.2288 -0.0038 252 PHE A CE2   
2091  C  CZ    . PHE A 252 ? 0.8745 0.3608 0.3422 -0.0236 0.2337 -0.0016 252 PHE A CZ    
2092  N  N     . THR A 253 ? 0.8609 0.3386 0.3093 -0.0454 0.2277 -0.0134 253 THR A N     
2093  C  CA    . THR A 253 ? 0.8601 0.3438 0.3121 -0.0484 0.2252 -0.0149 253 THR A CA    
2094  C  C     . THR A 253 ? 0.8452 0.3457 0.315  -0.0467 0.2223 -0.0144 253 THR A C     
2095  O  O     . THR A 253 ? 0.8438 0.3495 0.3218 -0.0424 0.2227 -0.0125 253 THR A O     
2096  C  CB    . THR A 253 ? 0.8862 0.3607 0.3309 -0.0454 0.2287 -0.0136 253 THR A CB    
2097  O  OG1   . THR A 253 ? 0.9147 0.3719 0.3426 -0.0451 0.2325 -0.0132 253 THR A OG1   
2098  C  CG2   . THR A 253 ? 0.8909 0.3683 0.335  -0.0497 0.2262 -0.0156 253 THR A CG2   
2099  N  N     . TYR A 254 ? 0.8331 0.3422 0.3088 -0.0498 0.2192 -0.016  254 TYR A N     
2100  C  CA    . TYR A 254 ? 0.8216 0.3455 0.3131 -0.0481 0.2167 -0.0156 254 TYR A CA    
2101  C  C     . TYR A 254 ? 0.8172 0.343  0.3157 -0.0412 0.2193 -0.0126 254 TYR A C     
2102  O  O     . TYR A 254 ? 0.8096 0.3447 0.3195 -0.0388 0.2181 -0.0114 254 TYR A O     
2103  C  CB    . TYR A 254 ? 0.817  0.3492 0.3128 -0.0522 0.2135 -0.0176 254 TYR A CB    
2104  C  CG    . TYR A 254 ? 0.8178 0.364  0.3288 -0.0504 0.2113 -0.0171 254 TYR A CG    
2105  C  CD1   . TYR A 254 ? 0.8259 0.3786 0.3435 -0.0509 0.2094 -0.0173 254 TYR A CD1   
2106  C  CD2   . TYR A 254 ? 0.8248 0.3764 0.3428 -0.0476 0.2115 -0.0162 254 TYR A CD2   
2107  C  CE1   . TYR A 254 ? 0.8296 0.3937 0.3599 -0.0492 0.2075 -0.0168 254 TYR A CE1   
2108  C  CE2   . TYR A 254 ? 0.8291 0.3922 0.36   -0.0459 0.2098 -0.0157 254 TYR A CE2   
2109  C  CZ    . TYR A 254 ? 0.8386 0.4077 0.3754 -0.0468 0.2077 -0.016  254 TYR A CZ    
2110  O  OH    . TYR A 254 ? 0.8522 0.4316 0.4006 -0.0454 0.206  -0.0155 254 TYR A OH    
2111  N  N     . SER A 255 ? 0.8206 0.3369 0.3117 -0.0382 0.2229 -0.0112 255 SER A N     
2112  C  CA    . SER A 255 ? 0.8203 0.338  0.3176 -0.0314 0.2257 -0.0079 255 SER A CA    
2113  C  C     . SER A 255 ? 0.8212 0.3398 0.3222 -0.0274 0.2271 -0.0053 255 SER A C     
2114  O  O     . SER A 255 ? 0.8177 0.3447 0.33   -0.0233 0.2272 -0.0029 255 SER A O     
2115  C  CB    . SER A 255 ? 0.8399 0.3456 0.3266 -0.0288 0.2297 -0.0067 255 SER A CB    
2116  O  OG    . SER A 255 ? 0.8623 0.3689 0.3545 -0.0219 0.233  -0.0029 255 SER A OG    
2117  N  N     . GLU A 256 ? 0.8225 0.3326 0.314  -0.0287 0.2281 -0.0057 256 GLU A N     
2118  C  CA    . GLU A 256 ? 0.821  0.3316 0.315  -0.025  0.2293 -0.0033 256 GLU A CA    
2119  C  C     . GLU A 256 ? 0.8056 0.3297 0.3123 -0.0267 0.2251 -0.0041 256 GLU A C     
2120  O  O     . GLU A 256 ? 0.7999 0.3307 0.3158 -0.0227 0.2252 -0.0014 256 GLU A O     
2121  C  CB    . GLU A 256 ? 0.8592 0.3562 0.3385 -0.0261 0.2317 -0.0038 256 GLU A CB    
2122  C  CG    . GLU A 256 ? 0.9262 0.409  0.3931 -0.0223 0.2369 -0.0019 256 GLU A CG    
2123  C  CD    . GLU A 256 ? 1.0196 0.4867 0.4691 -0.0247 0.2393 -0.0031 256 GLU A CD    
2124  O  OE1   . GLU A 256 ? 1.0545 0.5087 0.4931 -0.0206 0.2442 -0.0009 256 GLU A OE1   
2125  O  OE2   . GLU A 256 ? 1.039  0.5062 0.4854 -0.0307 0.2364 -0.0062 256 GLU A OE2   
2126  N  N     . TRP A 257 ? 0.7976 0.3258 0.3049 -0.0327 0.2214 -0.0075 257 TRP A N     
2127  C  CA    . TRP A 257 ? 0.7922 0.3323 0.3105 -0.0345 0.2175 -0.0083 257 TRP A CA    
2128  C  C     . TRP A 257 ? 0.7865 0.3378 0.318  -0.0323 0.2161 -0.0071 257 TRP A C     
2129  O  O     . TRP A 257 ? 0.782  0.3415 0.323  -0.0309 0.2144 -0.006  257 TRP A O     
2130  C  CB    . TRP A 257 ? 0.7912 0.3333 0.3071 -0.0411 0.2143 -0.0119 257 TRP A CB    
2131  C  CG    . TRP A 257 ? 0.8022 0.3356 0.3072 -0.0442 0.2147 -0.0133 257 TRP A CG    
2132  C  CD1   . TRP A 257 ? 0.8182 0.3443 0.3125 -0.049  0.2147 -0.0155 257 TRP A CD1   
2133  C  CD2   . TRP A 257 ? 0.8038 0.3358 0.3081 -0.0432 0.2149 -0.0126 257 TRP A CD2   
2134  N  NE1   . TRP A 257 ? 0.8262 0.3458 0.3127 -0.0512 0.2151 -0.0163 257 TRP A NE1   
2135  C  CE2   . TRP A 257 ? 0.82   0.3429 0.3124 -0.0474 0.2154 -0.0146 257 TRP A CE2   
2136  C  CE3   . TRP A 257 ? 0.806  0.3433 0.3181 -0.0393 0.2147 -0.0105 257 TRP A CE3   
2137  C  CZ2   . TRP A 257 ? 0.8288 0.3476 0.317  -0.0475 0.2158 -0.0145 257 TRP A CZ2   
2138  C  CZ3   . TRP A 257 ? 0.8178 0.3511 0.3256 -0.0392 0.2151 -0.0103 257 TRP A CZ3   
2139  C  CH2   . TRP A 257 ? 0.8241 0.3482 0.3202 -0.0432 0.2157 -0.0124 257 TRP A CH2   
2140  N  N     . GLU A 258 ? 0.7857 0.337  0.3173 -0.0321 0.2167 -0.0074 258 GLU A N     
2141  C  CA    . GLU A 258 ? 0.7813 0.342  0.3242 -0.0302 0.2158 -0.0064 258 GLU A CA    
2142  C  C     . GLU A 258 ? 0.7851 0.3474 0.3338 -0.0244 0.2181 -0.0025 258 GLU A C     
2143  O  O     . GLU A 258 ? 0.7753 0.3474 0.3352 -0.0233 0.2163 -0.0014 258 GLU A O     
2144  C  CB    . GLU A 258 ? 0.8011 0.3594 0.3407 -0.031  0.2167 -0.0075 258 GLU A CB    
2145  C  CG    . GLU A 258 ? 0.836  0.4038 0.3865 -0.0296 0.2156 -0.0069 258 GLU A CG    
2146  C  CD    . GLU A 258 ? 0.8982 0.4631 0.4449 -0.03   0.2166 -0.0078 258 GLU A CD    
2147  O  OE1   . GLU A 258 ? 0.9068 0.4618 0.4446 -0.0281 0.2199 -0.0068 258 GLU A OE1   
2148  O  OE2   . GLU A 258 ? 0.9239 0.4959 0.4758 -0.0322 0.2144 -0.0093 258 GLU A OE2   
2149  N  N     . SER A 259 ? 0.7979 0.3507 0.3388 -0.0207 0.2221 -0.0002 259 SER A N     
2150  C  CA    . SER A 259 ? 0.8091 0.3635 0.3552 -0.0147 0.2247 0.0041  259 SER A CA    
2151  C  C     . SER A 259 ? 0.8146 0.3753 0.3672 -0.014  0.2229 0.0056  259 SER A C     
2152  O  O     . SER A 259 ? 0.8132 0.3809 0.3749 -0.0103 0.2232 0.009   259 SER A O     
2153  C  CB    . SER A 259 ? 0.8378 0.3796 0.3727 -0.0107 0.2298 0.0064  259 SER A CB    
2154  O  OG    . SER A 259 ? 0.8775 0.4103 0.402  -0.0113 0.2311 0.0059  259 SER A OG    
2155  N  N     . ILE A 260 ? 0.8175 0.3761 0.3653 -0.0176 0.221  0.0032  260 ILE A N     
2156  C  CA    . ILE A 260 ? 0.8196 0.3838 0.3728 -0.0174 0.2189 0.0041  260 ILE A CA    
2157  C  C     . ILE A 260 ? 0.8148 0.3911 0.3796 -0.0204 0.2144 0.0026  260 ILE A C     
2158  O  O     . ILE A 260 ? 0.8116 0.3958 0.3855 -0.0186 0.213  0.0049  260 ILE A O     
2159  C  CB    . ILE A 260 ? 0.8326 0.3892 0.3757 -0.0202 0.2187 0.0019  260 ILE A CB    
2160  C  CG1   . ILE A 260 ? 0.8501 0.3935 0.3806 -0.0172 0.2235 0.0035  260 ILE A CG1   
2161  C  CG2   . ILE A 260 ? 0.8353 0.398  0.384  -0.0204 0.2162 0.0025  260 ILE A CG2   
2162  C  CD1   . ILE A 260 ? 0.8703 0.4046 0.3892 -0.021  0.2235 0.0007  260 ILE A CD1   
2163  N  N     . TYR A 261 ? 0.8141 0.3915 0.378  -0.0248 0.2123 -0.0009 261 TYR A N     
2164  C  CA    . TYR A 261 ? 0.8141 0.4015 0.3872 -0.0275 0.2086 -0.0025 261 TYR A CA    
2165  C  C     . TYR A 261 ? 0.8133 0.4083 0.3968 -0.0248 0.2085 0       261 TYR A C     
2166  O  O     . TYR A 261 ? 0.8091 0.412  0.401  -0.0252 0.2059 0.0006  261 TYR A O     
2167  C  CB    . TYR A 261 ? 0.816  0.4026 0.3853 -0.032  0.2072 -0.0061 261 TYR A CB    
2168  C  CG    . TYR A 261 ? 0.8183 0.4144 0.3962 -0.0343 0.204  -0.0075 261 TYR A CG    
2169  C  CD1   . TYR A 261 ? 0.8234 0.4237 0.4038 -0.037  0.201  -0.0089 261 TYR A CD1   
2170  C  CD2   . TYR A 261 ? 0.8284 0.4285 0.4112 -0.0336 0.2041 -0.0074 261 TYR A CD2   
2171  C  CE1   . TYR A 261 ? 0.8296 0.4375 0.4168 -0.0388 0.1984 -0.0101 261 TYR A CE1   
2172  C  CE2   . TYR A 261 ? 0.8343 0.4423 0.4242 -0.0355 0.2015 -0.0086 261 TYR A CE2   
2173  C  CZ    . TYR A 261 ? 0.8405 0.452  0.4323 -0.0381 0.1988 -0.0099 261 TYR A CZ    
2174  O  OH    . TYR A 261 ? 0.8553 0.4735 0.453  -0.0397 0.1966 -0.011  261 TYR A OH    
2175  N  N     . ASN A 262 ? 0.8163 0.4087 0.3989 -0.0222 0.2113 0.0013  262 ASN A N     
2176  C  CA    . ASN A 262 ? 0.8169 0.4162 0.4092 -0.0197 0.2115 0.0037  262 ASN A CA    
2177  C  C     . ASN A 262 ? 0.8186 0.4207 0.4162 -0.0152 0.2129 0.0083  262 ASN A C     
2178  O  O     . ASN A 262 ? 0.8163 0.4239 0.4217 -0.0129 0.2136 0.0108  262 ASN A O     
2179  C  CB    . ASN A 262 ? 0.8312 0.4276 0.4214 -0.0186 0.2138 0.0034  262 ASN A CB    
2180  C  CG    . ASN A 262 ? 0.8798 0.4659 0.4607 -0.0154 0.2181 0.0049  262 ASN A CG    
2181  O  OD1   . ASN A 262 ? 0.8985 0.4806 0.4764 -0.0123 0.2202 0.0075  262 ASN A OD1   
2182  N  ND2   . ASN A 262 ? 0.8905 0.4717 0.466  -0.016  0.2195 0.0034  262 ASN A ND2   
2183  N  N     . GLY A 263 ? 0.82   0.4187 0.4135 -0.0141 0.2135 0.0094  263 GLY A N     
2184  C  CA    . GLY A 263 ? 0.8221 0.4241 0.4205 -0.01   0.2146 0.0139  263 GLY A CA    
2185  C  C     . GLY A 263 ? 0.8281 0.4252 0.4237 -0.0044 0.2195 0.0178  263 GLY A C     
2186  O  O     . GLY A 263 ? 0.8255 0.4277 0.4275 -0.0005 0.2205 0.0223  263 GLY A O     
2187  N  N     . THR A 264 ? 0.836  0.4233 0.422  -0.0038 0.2226 0.0165  264 THR A N     
2188  C  CA    . THR A 264 ? 0.848  0.4289 0.4297 0.0018  0.2278 0.0202  264 THR A CA    
2189  C  C     . THR A 264 ? 0.8584 0.4333 0.4336 0.0052  0.2303 0.0228  264 THR A C     
2190  O  O     . THR A 264 ? 0.8589 0.4351 0.4369 0.0106  0.2334 0.0277  264 THR A O     
2191  C  CB    . THR A 264 ? 0.8695 0.4405 0.4414 0.0012  0.2303 0.0179  264 THR A CB    
2192  O  OG1   . THR A 264 ? 0.8785 0.4554 0.4563 -0.002  0.2277 0.0154  264 THR A OG1   
2193  C  CG2   . THR A 264 ? 0.8771 0.4413 0.4447 0.0072  0.2357 0.0218  264 THR A CG2   
2194  N  N     . TYR A 265 ? 0.8646 0.4335 0.4314 0.002   0.2292 0.0196  265 TYR A N     
2195  C  CA    . TYR A 265 ? 0.878  0.4405 0.4377 0.0047  0.2315 0.0216  265 TYR A CA    
2196  C  C     . TYR A 265 ? 0.8792 0.4446 0.4394 0.0006  0.2275 0.019   265 TYR A C     
2197  O  O     . TYR A 265 ? 0.8796 0.4483 0.4416 -0.0048 0.2237 0.0149  265 TYR A O     
2198  C  CB    . TYR A 265 ? 0.8926 0.4392 0.4361 0.0055  0.2357 0.0204  265 TYR A CB    
2199  C  CG    . TYR A 265 ? 0.9081 0.4489 0.4481 0.0087  0.2397 0.022   265 TYR A CG    
2200  C  CD1   . TYR A 265 ? 0.92   0.4604 0.4618 0.0157  0.2441 0.0274  265 TYR A CD1   
2201  C  CD2   . TYR A 265 ? 0.9236 0.4587 0.4573 0.005   0.2394 0.0183  265 TYR A CD2   
2202  C  CE1   . TYR A 265 ? 0.9353 0.4698 0.4733 0.0189  0.248  0.029   265 TYR A CE1   
2203  C  CE2   . TYR A 265 ? 0.9394 0.4684 0.4689 0.0081  0.2431 0.0197  265 TYR A CE2   
2204  C  CZ    . TYR A 265 ? 0.9515 0.4799 0.4831 0.0151  0.2475 0.025   265 TYR A CZ    
2205  O  OH    . TYR A 265 ? 0.9749 0.4967 0.5019 0.0183  0.2514 0.0264  265 TYR A OH    
2206  N  N     . ARG A 266 ? 0.8775 0.4412 0.4353 0.0035  0.2288 0.0215  266 ARG A N     
2207  C  CA    . ARG A 266 ? 0.882  0.4459 0.4378 0.0001  0.2258 0.0191  266 ARG A CA    
2208  C  C     . ARG A 266 ? 0.8897 0.4389 0.4297 -0.0014 0.2285 0.0164  266 ARG A C     
2209  O  O     . ARG A 266 ? 0.8981 0.4374 0.4292 0.0015  0.233  0.0176  266 ARG A O     
2210  C  CB    . ARG A 266 ? 0.8998 0.4698 0.4612 0.0038  0.2255 0.0232  266 ARG A CB    
2211  C  CG    . ARG A 266 ? 0.9552 0.5163 0.5079 0.0096  0.2307 0.0269  266 ARG A CG    
2212  C  CD    . ARG A 266 ? 0.9998 0.5687 0.5596 0.0138  0.2304 0.0318  266 ARG A CD    
2213  N  NE    . ARG A 266 ? 1.0485 0.6076 0.598  0.019   0.2354 0.0347  266 ARG A NE    
2214  C  CZ    . ARG A 266 ? 1.0798 0.6377 0.629  0.0259  0.2401 0.0403  266 ARG A CZ    
2215  N  NH1   . ARG A 266 ? 1.0677 0.6342 0.627  0.0284  0.2404 0.0436  266 ARG A NH1   
2216  N  NH2   . ARG A 266 ? 1.089  0.6368 0.6275 0.0306  0.2448 0.0427  266 ARG A NH2   
2217  N  N     . ILE A 267 ? 0.8846 0.432  0.4205 -0.0061 0.2259 0.0128  267 ILE A N     
2218  C  CA    . ILE A 267 ? 0.892  0.426  0.4132 -0.0086 0.2279 0.01    267 ILE A CA    
2219  C  C     . ILE A 267 ? 0.8949 0.4174 0.4052 -0.0035 0.2331 0.013   267 ILE A C     
2220  O  O     . ILE A 267 ? 0.9051 0.4145 0.4019 -0.0045 0.2361 0.0115  267 ILE A O     
2221  C  CB    . ILE A 267 ? 0.8989 0.4344 0.419  -0.0145 0.224  0.0059  267 ILE A CB    
2222  C  CG1   . ILE A 267 ? 0.9191 0.4432 0.426  -0.0191 0.225  0.0022  267 ILE A CG1   
2223  C  CG2   . ILE A 267 ? 0.905  0.4423 0.4263 -0.0128 0.2234 0.0074  267 ILE A CG2   
2224  C  CD1   . ILE A 267 ? 0.9341 0.4618 0.4419 -0.0254 0.2209 -0.0018 267 ILE A CD1   
2225  N  N     . THR A 268 ? 0.8844 0.4116 0.4002 0.002   0.2344 0.0175  268 THR A N     
2226  C  CA    . THR A 268 ? 0.8905 0.4074 0.3964 0.0076  0.2397 0.021   268 THR A CA    
2227  C  C     . THR A 268 ? 0.8846 0.3986 0.3898 0.014   0.2446 0.0255  268 THR A C     
2228  O  O     . THR A 268 ? 0.8895 0.3928 0.3845 0.019   0.2498 0.0284  268 THR A O     
2229  C  CB    . THR A 268 ? 0.9045 0.4269 0.4147 0.0102  0.2388 0.0235  268 THR A CB    
2230  O  OG1   . THR A 268 ? 0.9073 0.4455 0.4336 0.0114  0.2354 0.026   268 THR A OG1   
2231  C  CG2   . THR A 268 ? 0.9103 0.43   0.4157 0.0049  0.2359 0.0194  268 THR A CG2   
2232  N  N     . ASN A 269 ? 0.8722 0.3951 0.3878 0.0142  0.2432 0.0262  269 ASN A N     
2233  C  CA    . ASN A 269 ? 0.8747 0.3951 0.39   0.0202  0.2479 0.0305  269 ASN A CA    
2234  C  C     . ASN A 269 ? 0.8705 0.3848 0.3809 0.0177  0.2487 0.0277  269 ASN A C     
2235  O  O     . ASN A 269 ? 0.8693 0.3856 0.3837 0.0214  0.251  0.0306  269 ASN A O     
2236  C  CB    . ASN A 269 ? 0.8888 0.4242 0.42   0.0244  0.2469 0.0355  269 ASN A CB    
2237  C  CG    . ASN A 269 ? 0.9398 0.4882 0.4848 0.0211  0.2425 0.0342  269 ASN A CG    
2238  O  OD1   . ASN A 269 ? 0.9613 0.508  0.5049 0.0162  0.2405 0.0298  269 ASN A OD1   
2239  N  ND2   . ASN A 269 ? 0.9433 0.505  0.502  0.0236  0.2409 0.0382  269 ASN A ND2   
2240  N  N     . LEU A 270 ? 0.8671 0.374  0.3686 0.0114  0.2469 0.0224  270 LEU A N     
2241  C  CA    . LEU A 270 ? 0.8691 0.3697 0.3646 0.0083  0.2473 0.0194  270 LEU A CA    
2242  C  C     . LEU A 270 ? 0.8743 0.3603 0.3569 0.0136  0.2539 0.0222  270 LEU A C     
2243  O  O     . LEU A 270 ? 0.8864 0.3615 0.3577 0.016   0.2575 0.0235  270 LEU A O     
2244  C  CB    . LEU A 270 ? 0.8753 0.3702 0.3623 0.0007  0.2444 0.0138  270 LEU A CB    
2245  C  CG    . LEU A 270 ? 0.8906 0.3882 0.3792 -0.0049 0.2413 0.0098  270 LEU A CG    
2246  C  CD1   . LEU A 270 ? 0.8853 0.3996 0.3911 -0.0059 0.237  0.0098  270 LEU A CD1   
2247  C  CD2   . LEU A 270 ? 0.9028 0.3952 0.383  -0.0121 0.2387 0.0051  270 LEU A CD2   
2248  N  N     . PRO A 271 ? 0.8628 0.3485 0.347  0.0161  0.2559 0.0237  271 PRO A N     
2249  C  CA    . PRO A 271 ? 0.8666 0.3379 0.3382 0.0217  0.2626 0.0268  271 PRO A CA    
2250  C  C     . PRO A 271 ? 0.8724 0.3252 0.3242 0.0185  0.2648 0.0236  271 PRO A C     
2251  O  O     . PRO A 271 ? 0.882  0.3209 0.3208 0.0231  0.2705 0.0262  271 PRO A O     
2252  C  CB    . PRO A 271 ? 0.8746 0.3501 0.3526 0.0234  0.2632 0.0279  271 PRO A CB    
2253  C  CG    . PRO A 271 ? 0.8733 0.361  0.3621 0.0167  0.2568 0.0236  271 PRO A CG    
2254  C  CD    . PRO A 271 ? 0.8472 0.3446 0.344  0.0141  0.2526 0.0227  271 PRO A CD    
2255  N  N     . SER A 272 ? 0.8661 0.3187 0.3152 0.0104  0.2604 0.0181  272 SER A N     
2256  C  CA    . SER A 272 ? 0.8778 0.3142 0.3088 0.0058  0.2616 0.0147  272 SER A CA    
2257  C  C     . SER A 272 ? 0.8864 0.3176 0.3103 0.0037  0.2613 0.0135  272 SER A C     
2258  O  O     . SER A 272 ? 0.9015 0.3192 0.3102 -0.0007 0.2622 0.0106  272 SER A O     
2259  C  CB    . SER A 272 ? 0.8876 0.327  0.3192 -0.002  0.257  0.0098  272 SER A CB    
2260  O  OG    . SER A 272 ? 0.8977 0.3534 0.3442 -0.0058 0.2512 0.0078  272 SER A OG    
2261  N  N     . LEU A 273 ? 0.875  0.3165 0.3094 0.0064  0.2601 0.0157  273 LEU A N     
2262  C  CA    . LEU A 273 ? 0.8784 0.3155 0.3068 0.0049  0.2599 0.0147  273 LEU A CA    
2263  C  C     . LEU A 273 ? 0.8901 0.3077 0.2995 0.0086  0.2664 0.0166  273 LEU A C     
2264  O  O     . LEU A 273 ? 0.8937 0.307  0.301  0.0162  0.2715 0.0212  273 LEU A O     
2265  C  CB    . LEU A 273 ? 0.8717 0.3231 0.3146 0.0083  0.2579 0.0175  273 LEU A CB    
2266  C  CG    . LEU A 273 ? 0.8907 0.3461 0.3352 0.0033  0.2539 0.0145  273 LEU A CG    
2267  C  CD1   . LEU A 273 ? 0.8927 0.356  0.3433 -0.0047 0.2481 0.0096  273 LEU A CD1   
2268  C  CD2   . LEU A 273 ? 0.8915 0.3595 0.3489 0.0074  0.2525 0.0178  273 LEU A CD2   
2269  N  N     . GLY A 274 ? 0.8944 0.2999 0.2898 0.0031  0.2664 0.013   274 GLY A N     
2270  C  CA    . GLY A 274 ? 0.9067 0.2917 0.2819 0.0056  0.2725 0.0141  274 GLY A CA    
2271  C  C     . GLY A 274 ? 0.9114 0.2813 0.2705 0.0001  0.2734 0.0107  274 GLY A C     
2272  O  O     . GLY A 274 ? 0.9265 0.2782 0.2669 -0.0006 0.2772 0.0102  274 GLY A O     
2273  N  N     . ARG A 275 ? 0.8974 0.2741 0.2626 -0.0042 0.2697 0.0083  275 ARG A N     
2274  C  CA    . ARG A 275 ? 0.9064 0.2697 0.2566 -0.0101 0.2699 0.005   275 ARG A CA    
2275  C  C     . ARG A 275 ? 0.9152 0.2708 0.2543 -0.0185 0.2677 0.0007  275 ARG A C     
2276  O  O     . ARG A 275 ? 0.928  0.2669 0.249  -0.0224 0.2696 -0.0011 275 ARG A O     
2277  C  CB    . ARG A 275 ? 0.9078 0.2811 0.2675 -0.0131 0.2662 0.0033  275 ARG A CB    
2278  C  CG    . ARG A 275 ? 0.9159 0.3091 0.2936 -0.0178 0.2594 0.0009  275 ARG A CG    
2279  C  CD    . ARG A 275 ? 0.9266 0.3293 0.3138 -0.019  0.2566 0       275 ARG A CD    
2280  N  NE    . ARG A 275 ? 0.928  0.3467 0.3285 -0.025  0.2501 -0.0031 275 ARG A NE    
2281  C  CZ    . ARG A 275 ? 0.9415 0.359  0.3368 -0.0332 0.2466 -0.0071 275 ARG A CZ    
2282  N  NH1   . ARG A 275 ? 0.9543 0.3554 0.3313 -0.0371 0.2485 -0.0087 275 ARG A NH1   
2283  N  NH2   . ARG A 275 ? 0.9208 0.3534 0.3288 -0.0377 0.2411 -0.0093 275 ARG A NH2   
2284  N  N     . PHE A 276 ? 0.9059 0.273  0.2551 -0.021  0.2638 -0.0005 276 PHE A N     
2285  C  CA    . PHE A 276 ? 0.9163 0.277  0.2562 -0.0277 0.2623 -0.0037 276 PHE A CA    
2286  C  C     . PHE A 276 ? 0.9174 0.281  0.2612 -0.0234 0.2635 -0.0017 276 PHE A C     
2287  O  O     . PHE A 276 ? 0.9104 0.2869 0.269  -0.0175 0.2631 0.0013  276 PHE A O     
2288  C  CB    . PHE A 276 ? 0.9098 0.2809 0.2563 -0.037  0.2557 -0.0081 276 PHE A CB    
2289  C  CG    . PHE A 276 ? 0.9043 0.2973 0.2727 -0.0368 0.2506 -0.0082 276 PHE A CG    
2290  C  CD1   . PHE A 276 ? 0.9104 0.3122 0.2868 -0.0376 0.2481 -0.0087 276 PHE A CD1   
2291  C  CD2   . PHE A 276 ? 0.9061 0.3102 0.2861 -0.0361 0.2483 -0.008  276 PHE A CD2   
2292  C  CE1   . PHE A 276 ? 0.9071 0.3279 0.3025 -0.0375 0.2436 -0.0088 276 PHE A CE1   
2293  C  CE2   . PHE A 276 ? 0.9025 0.3256 0.3014 -0.0361 0.2438 -0.0082 276 PHE A CE2   
2294  C  CZ    . PHE A 276 ? 0.897  0.3282 0.3032 -0.0368 0.2415 -0.0086 276 PHE A CZ    
2295  N  N     . LYS A 277 ? 0.9237 0.2746 0.2535 -0.0262 0.2653 -0.003  277 LYS A N     
2296  C  CA    . LYS A 277 ? 0.9248 0.2764 0.256  -0.0221 0.2669 -0.0011 277 LYS A CA    
2297  C  C     . LYS A 277 ? 0.9177 0.2797 0.2567 -0.0285 0.2615 -0.0043 277 LYS A C     
2298  O  O     . LYS A 277 ? 0.9149 0.2801 0.2545 -0.0366 0.2573 -0.008  277 LYS A O     
2299  C  CB    . LYS A 277 ? 0.962  0.2911 0.2712 -0.0199 0.2734 0       277 LYS A CB    
2300  C  CG    . LYS A 277 ? 1.0119 0.3312 0.3143 -0.0108 0.28   0.0047  277 LYS A CG    
2301  C  CD    . LYS A 277 ? 1.0784 0.3771 0.3608 -0.0075 0.2866 0.0063  277 LYS A CD    
2302  C  CE    . LYS A 277 ? 1.1332 0.4252 0.4118 0.0035  0.2934 0.012   277 LYS A CE    
2303  N  NZ    . LYS A 277 ? 1.1694 0.4528 0.4407 0.0047  0.2961 0.0127  277 LYS A NZ    
2304  N  N     . PHE A 278 ? 0.9144 0.2815 0.2591 -0.0247 0.2618 -0.0025 278 PHE A N     
2305  C  CA    . PHE A 278 ? 0.9175 0.2927 0.2681 -0.03   0.2574 -0.0053 278 PHE A CA    
2306  C  C     . PHE A 278 ? 0.9227 0.2804 0.2544 -0.034  0.2601 -0.0072 278 PHE A C     
2307  O  O     . PHE A 278 ? 0.9327 0.2782 0.2536 -0.0288 0.2653 -0.0047 278 PHE A O     
2308  C  CB    . PHE A 278 ? 0.9186 0.3073 0.2838 -0.0243 0.2562 -0.0026 278 PHE A CB    
2309  C  CG    . PHE A 278 ? 0.9368 0.3289 0.3038 -0.0276 0.2536 -0.0045 278 PHE A CG    
2310  C  CD1   . PHE A 278 ? 0.9495 0.3459 0.3181 -0.0362 0.2491 -0.0087 278 PHE A CD1   
2311  C  CD2   . PHE A 278 ? 0.9503 0.3424 0.3181 -0.0219 0.2557 -0.0018 278 PHE A CD2   
2312  C  CE1   . PHE A 278 ? 0.9596 0.3584 0.3293 -0.039  0.2471 -0.0102 278 PHE A CE1   
2313  C  CE2   . PHE A 278 ? 0.9598 0.3547 0.329  -0.0248 0.2534 -0.0035 278 PHE A CE2   
2314  C  CZ    . PHE A 278 ? 0.9575 0.3556 0.3275 -0.0333 0.2492 -0.0077 278 PHE A CZ    
2315  N  N     . ARG A 279 ? 0.9165 0.2724 0.2434 -0.0433 0.2569 -0.0113 279 ARG A N     
2316  C  CA    . ARG A 279 ? 0.9276 0.2674 0.2366 -0.0487 0.2588 -0.0135 279 ARG A CA    
2317  C  C     . ARG A 279 ? 0.9151 0.2642 0.2306 -0.0559 0.2539 -0.0166 279 ARG A C     
2318  O  O     . ARG A 279 ? 0.9136 0.2665 0.2299 -0.0638 0.25   -0.0196 279 ARG A O     
2319  C  CB    . ARG A 279 ? 0.9587 0.2837 0.2517 -0.0538 0.2604 -0.0152 279 ARG A CB    
2320  C  CG    . ARG A 279 ? 1.0053 0.321  0.2919 -0.0467 0.2654 -0.0121 279 ARG A CG    
2321  C  CD    . ARG A 279 ? 1.0517 0.3492 0.319  -0.0514 0.2678 -0.0137 279 ARG A CD    
2322  N  NE    . ARG A 279 ? 1.0854 0.3743 0.347  -0.044  0.2727 -0.0105 279 ARG A NE    
2323  C  CZ    . ARG A 279 ? 1.114  0.3861 0.3611 -0.0375 0.2796 -0.0076 279 ARG A CZ    
2324  N  NH1   . ARG A 279 ? 1.1234 0.3851 0.36   -0.0374 0.2824 -0.0077 279 ARG A NH1   
2325  N  NH2   . ARG A 279 ? 1.105  0.3704 0.348  -0.0307 0.284  -0.0045 279 ARG A NH2   
2326  N  N     . LYS A 280 ? 0.9048 0.2578 0.225  -0.0528 0.254  -0.0156 280 LYS A N     
2327  C  CA    . LYS A 280 ? 0.9006 0.2621 0.227  -0.0582 0.2499 -0.0181 280 LYS A CA    
2328  C  C     . LYS A 280 ? 0.9119 0.2606 0.2226 -0.0669 0.2502 -0.0212 280 LYS A C     
2329  O  O     . LYS A 280 ? 0.9249 0.2554 0.218  -0.0664 0.2551 -0.0208 280 LYS A O     
2330  C  CB    . LYS A 280 ? 0.9179 0.2822 0.2487 -0.0521 0.2513 -0.016  280 LYS A CB    
2331  C  CG    . LYS A 280 ? 0.9592 0.3281 0.2927 -0.0571 0.2483 -0.0183 280 LYS A CG    
2332  C  CD    . LYS A 280 ? 0.9883 0.3771 0.3402 -0.06   0.2421 -0.0196 280 LYS A CD    
2333  C  CE    . LYS A 280 ? 1.0247 0.4174 0.3786 -0.0644 0.2396 -0.0216 280 LYS A CE    
2334  N  NZ    . LYS A 280 ? 1.067  0.4454 0.4047 -0.071  0.2415 -0.0238 280 LYS A NZ    
2335  N  N     . LYS A 281 ? 0.9066 0.2649 0.2237 -0.0749 0.2452 -0.024  281 LYS A N     
2336  C  CA    . LYS A 281 ? 0.9214 0.2699 0.2253 -0.084  0.2449 -0.0268 281 LYS A CA    
2337  C  C     . LYS A 281 ? 0.9233 0.2726 0.2274 -0.0855 0.2445 -0.0276 281 LYS A C     
2338  O  O     . LYS A 281 ? 0.916  0.2811 0.2351 -0.0861 0.2405 -0.028  281 LYS A O     
2339  C  CB    . LYS A 281 ? 0.9411 0.2994 0.2509 -0.0921 0.2399 -0.0291 281 LYS A CB    
2340  C  CG    . LYS A 281 ? 0.9974 0.3492 0.3004 -0.093  0.2408 -0.029  281 LYS A CG    
2341  C  CD    . LYS A 281 ? 1.0541 0.4077 0.3539 -0.1034 0.237  -0.0316 281 LYS A CD    
2342  C  CE    . LYS A 281 ? 1.0908 0.4658 0.4097 -0.1052 0.2315 -0.0321 281 LYS A CE    
2343  N  NZ    . LYS A 281 ? 1.115  0.4961 0.4418 -0.1002 0.2312 -0.0308 281 LYS A NZ    
2344  N  N     . ILE A 282 ? 0.932  0.2639 0.2191 -0.0862 0.2487 -0.0278 282 ILE A N     
2345  C  CA    . ILE A 282 ? 0.9378 0.2688 0.2236 -0.0877 0.2488 -0.0285 282 ILE A CA    
2346  C  C     . ILE A 282 ? 0.9572 0.2771 0.2285 -0.0977 0.2488 -0.0312 282 ILE A C     
2347  O  O     . ILE A 282 ? 0.9703 0.2727 0.2239 -0.1    0.2523 -0.0316 282 ILE A O     
2348  C  CB    . ILE A 282 ? 0.9434 0.2642 0.2223 -0.0789 0.2541 -0.0259 282 ILE A CB    
2349  C  CG1   . ILE A 282 ? 0.9419 0.2745 0.2355 -0.0693 0.254  -0.0228 282 ILE A CG1   
2350  C  CG2   . ILE A 282 ? 0.949  0.268  0.2257 -0.0803 0.2544 -0.0267 282 ILE A CG2   
2351  C  CD1   . ILE A 282 ? 0.9596 0.2828 0.2467 -0.0601 0.2594 -0.0196 282 ILE A CD1   
2352  N  N     . ALA A 283 ? 0.9558 0.2857 0.2343 -0.1039 0.2448 -0.033  283 ALA A N     
2353  C  CA    . ALA A 283 ? 0.9723 0.2933 0.2384 -0.1139 0.2445 -0.0353 283 ALA A CA    
2354  C  C     . ALA A 283 ? 0.9944 0.2957 0.2424 -0.1126 0.2499 -0.0351 283 ALA A C     
2355  O  O     . ALA A 283 ? 0.9986 0.2995 0.2493 -0.1051 0.2523 -0.0336 283 ALA A O     
2356  C  CB    . ALA A 283 ? 0.9634 0.3003 0.2422 -0.1192 0.2397 -0.0366 283 ALA A CB    
2357  N  N     . GLU A 284 ? 1.0057 0.2904 0.2351 -0.12   0.2519 -0.0367 284 GLU A N     
2358  C  CA    . GLU A 284 ? 1.0232 0.2872 0.2334 -0.1194 0.2574 -0.0367 284 GLU A CA    
2359  C  C     . GLU A 284 ? 1.0212 0.2894 0.2359 -0.1189 0.2573 -0.0369 284 GLU A C     
2360  O  O     . GLU A 284 ? 1.0298 0.2874 0.2368 -0.1126 0.2619 -0.0357 284 GLU A O     
2361  C  CB    . GLU A 284 ? 1.063  0.3098 0.253  -0.1294 0.2586 -0.0387 284 GLU A CB    
2362  C  CG    . GLU A 284 ? 1.1343 0.364  0.3088 -0.1268 0.2628 -0.0379 284 GLU A CG    
2363  C  CD    . GLU A 284 ? 1.2333 0.4446 0.3865 -0.137  0.264  -0.0399 284 GLU A CD    
2364  O  OE1   . GLU A 284 ? 1.2559 0.4638 0.4043 -0.1399 0.263  -0.0403 284 GLU A OE1   
2365  O  OE2   . GLU A 284 ? 1.2643 0.4644 0.4052 -0.1422 0.2657 -0.0412 284 GLU A OE2   
2366  N  N     . LYS A 285 ? 1.0077 0.292  0.2355 -0.1247 0.2521 -0.0382 285 LYS A N     
2367  C  CA    . LYS A 285 ? 1.0084 0.298  0.2416 -0.1245 0.2516 -0.0385 285 LYS A CA    
2368  C  C     . LYS A 285 ? 1.0004 0.2986 0.2459 -0.1134 0.2523 -0.0363 285 LYS A C     
2369  O  O     . LYS A 285 ? 1.0035 0.3001 0.2486 -0.1111 0.2537 -0.0361 285 LYS A O     
2370  C  CB    . LYS A 285 ? 1.0258 0.3316 0.271  -0.1328 0.246  -0.0399 285 LYS A CB    
2371  C  CG    . LYS A 285 ? 1.0652 0.3923 0.3309 -0.1307 0.241  -0.0393 285 LYS A CG    
2372  C  CD    . LYS A 285 ? 1.1089 0.4516 0.3859 -0.1382 0.236  -0.0404 285 LYS A CD    
2373  C  CE    . LYS A 285 ? 1.1472 0.5102 0.4437 -0.1358 0.2315 -0.0397 285 LYS A CE    
2374  N  NZ    . LYS A 285 ? 1.172  0.5507 0.4803 -0.1414 0.2273 -0.0401 285 LYS A NZ    
2375  N  N     . SER A 286 ? 0.9887 0.2958 0.2449 -0.1069 0.2513 -0.0347 286 SER A N     
2376  C  CA    . SER A 286 ? 0.9826 0.2988 0.251  -0.0968 0.2516 -0.0324 286 SER A CA    
2377  C  C     . SER A 286 ? 0.9903 0.2917 0.2472 -0.0883 0.2576 -0.0301 286 SER A C     
2378  O  O     . SER A 286 ? 0.9853 0.2927 0.2504 -0.0801 0.2582 -0.0279 286 SER A O     
2379  C  CB    . SER A 286 ? 0.9875 0.3209 0.2733 -0.094  0.2476 -0.0316 286 SER A CB    
2380  O  OG    . SER A 286 ? 1.0086 0.3559 0.305  -0.1012 0.2423 -0.0334 286 SER A OG    
2381  N  N     . LEU A 287 ? 1.001  0.2833 0.239  -0.09   0.262  -0.0303 287 LEU A N     
2382  C  CA    . LEU A 287 ? 1.0153 0.2827 0.2413 -0.0816 0.2683 -0.0277 287 LEU A CA    
2383  C  C     . LEU A 287 ? 1.0291 0.2867 0.2464 -0.0784 0.2721 -0.0271 287 LEU A C     
2384  O  O     . LEU A 287 ? 1.0357 0.2881 0.2462 -0.0853 0.2717 -0.0293 287 LEU A O     
2385  C  CB    . LEU A 287 ? 1.029  0.2777 0.2363 -0.0842 0.2722 -0.028  287 LEU A CB    
2386  C  CG    . LEU A 287 ? 1.0401 0.2952 0.2537 -0.084  0.2701 -0.0276 287 LEU A CG    
2387  C  CD1   . LEU A 287 ? 1.0589 0.2937 0.2519 -0.0875 0.2739 -0.0282 287 LEU A CD1   
2388  C  CD2   . LEU A 287 ? 1.0419 0.3062 0.2676 -0.0728 0.2711 -0.0241 287 LEU A CD2   
2389  N  N     . SER A 288 ? 1.0313 0.287  0.2492 -0.0679 0.2757 -0.0238 288 SER A N     
2390  C  CA    . SER A 288 ? 1.0436 0.2906 0.2539 -0.0626 0.2799 -0.0224 288 SER A CA    
2391  C  C     . SER A 288 ? 1.0514 0.2943 0.26   -0.0507 0.2846 -0.018  288 SER A C     
2392  O  O     . SER A 288 ? 1.045  0.2948 0.2613 -0.047  0.2839 -0.0163 288 SER A O     
2393  C  CB    . SER A 288 ? 1.0475 0.3105 0.2732 -0.0626 0.2755 -0.023  288 SER A CB    
2394  O  OG    . SER A 288 ? 1.077  0.3418 0.3022 -0.0728 0.2722 -0.0265 288 SER A OG    
2395  N  N     . GLY A 289 ? 1.0619 0.2939 0.2605 -0.0448 0.2897 -0.0161 289 GLY A N     
2396  C  CA    . GLY A 289 ? 1.0717 0.3001 0.2684 -0.0331 0.2946 -0.0115 289 GLY A CA    
2397  C  C     . GLY A 289 ? 1.0795 0.3009 0.2704 -0.0295 0.2978 -0.0093 289 GLY A C     
2398  O  O     . GLY A 289 ? 1.0912 0.2956 0.265  -0.0342 0.3009 -0.011  289 GLY A O     
2399  N  N     . LYS A 290 ? 1.0719 0.3065 0.2768 -0.0214 0.297  -0.0057 290 LYS A N     
2400  C  CA    . LYS A 290 ? 1.0818 0.3118 0.2833 -0.017  0.3001 -0.0032 290 LYS A CA    
2401  C  C     . LYS A 290 ? 1.0779 0.3249 0.2962 -0.0207 0.294  -0.0045 290 LYS A C     
2402  O  O     . LYS A 290 ? 1.0775 0.3279 0.3003 -0.0152 0.2952 -0.0016 290 LYS A O     
2403  C  CB    . LYS A 290 ? 1.0998 0.3306 0.3032 -0.0042 0.3048 0.0026  290 LYS A CB    
2404  C  CG    . LYS A 290 ? 1.1539 0.3669 0.3395 0.0006  0.3116 0.0044  290 LYS A CG    
2405  C  CD    . LYS A 290 ? 1.1996 0.4186 0.3914 0.0131  0.3149 0.0104  290 LYS A CD    
2406  C  CE    . LYS A 290 ? 1.2554 0.4581 0.4306 0.0181  0.3214 0.0122  290 LYS A CE    
2407  N  NZ    . LYS A 290 ? 1.276  0.4894 0.4611 0.0292  0.3228 0.0177  290 LYS A NZ    
2408  N  N     . VAL A 291 ? 1.0735 0.3311 0.301  -0.0299 0.2876 -0.0086 291 VAL A N     
2409  C  CA    . VAL A 291 ? 1.0703 0.3447 0.314  -0.0341 0.2815 -0.0101 291 VAL A CA    
2410  C  C     . VAL A 291 ? 1.0787 0.3442 0.3138 -0.0365 0.2831 -0.0105 291 VAL A C     
2411  O  O     . VAL A 291 ? 1.0692 0.3448 0.3153 -0.033  0.2817 -0.0088 291 VAL A O     
2412  C  CB    . VAL A 291 ? 1.0769 0.362  0.3293 -0.0433 0.2753 -0.0142 291 VAL A CB    
2413  C  CG1   . VAL A 291 ? 1.0778 0.3785 0.3448 -0.048  0.2695 -0.0158 291 VAL A CG1   
2414  C  CG2   . VAL A 291 ? 1.0736 0.3699 0.3371 -0.0399 0.2732 -0.0133 291 VAL A CG2   
2415  N  N     . LYS A 292 ? 1.0971 0.343  0.312  -0.0423 0.2863 -0.0127 292 LYS A N     
2416  C  CA    . LYS A 292 ? 1.1145 0.3494 0.3186 -0.0449 0.2882 -0.0133 292 LYS A CA    
2417  C  C     . LYS A 292 ? 1.1215 0.3501 0.3217 -0.0342 0.2938 -0.0086 292 LYS A C     
2418  O  O     . LYS A 292 ? 1.1218 0.3539 0.3262 -0.033  0.2932 -0.0078 292 LYS A O     
2419  C  CB    . LYS A 292 ? 1.1556 0.3686 0.3365 -0.0529 0.291  -0.0162 292 LYS A CB    
2420  C  CG    . LYS A 292 ? 1.2179 0.4215 0.3888 -0.0576 0.2915 -0.0174 292 LYS A CG    
2421  C  CD    . LYS A 292 ? 1.2988 0.478  0.4442 -0.0645 0.2953 -0.0197 292 LYS A CD    
2422  C  CE    . LYS A 292 ? 1.3594 0.5299 0.4951 -0.0702 0.2949 -0.0212 292 LYS A CE    
2423  N  NZ    . LYS A 292 ? 1.388  0.5565 0.5242 -0.0613 0.2983 -0.0177 292 LYS A NZ    
2424  N  N     . GLU A 293 ? 1.1232 0.3439 0.3168 -0.0259 0.2992 -0.0054 293 GLU A N     
2425  C  CA    . GLU A 293 ? 1.1299 0.3451 0.32   -0.0147 0.3051 -0.0002 293 GLU A CA    
2426  C  C     . GLU A 293 ? 1.1103 0.3483 0.3239 -0.0086 0.3015 0.0028  293 GLU A C     
2427  O  O     . GLU A 293 ? 1.112  0.3497 0.3266 -0.0033 0.3039 0.0057  293 GLU A O     
2428  C  CB    . GLU A 293 ? 1.1723 0.3761 0.3514 -0.0077 0.3111 0.0026  293 GLU A CB    
2429  C  CG    . GLU A 293 ? 1.2627 0.4414 0.4163 -0.0127 0.3158 0.0002  293 GLU A CG    
2430  C  CD    . GLU A 293 ? 1.3575 0.5365 0.5098 -0.0207 0.3126 -0.0038 293 GLU A CD    
2431  O  OE1   . GLU A 293 ? 1.382  0.5495 0.5229 -0.0176 0.317  -0.0028 293 GLU A OE1   
2432  O  OE2   . GLU A 293 ? 1.3824 0.5733 0.5451 -0.0299 0.3059 -0.0077 293 GLU A OE2   
2433  N  N     . PHE A 294 ? 1.0892 0.3468 0.3214 -0.0097 0.2957 0.002   294 PHE A N     
2434  C  CA    . PHE A 294 ? 1.0731 0.3528 0.3279 -0.0051 0.2915 0.0044  294 PHE A CA    
2435  C  C     . PHE A 294 ? 1.069  0.3563 0.3314 -0.0102 0.2876 0.0024  294 PHE A C     
2436  O  O     . PHE A 294 ? 1.0636 0.3592 0.3356 -0.0048 0.2877 0.0054  294 PHE A O     
2437  C  CB    . PHE A 294 ? 1.0589 0.3558 0.3297 -0.0065 0.286  0.0035  294 PHE A CB    
2438  C  CG    . PHE A 294 ? 1.0489 0.3683 0.3424 -0.003  0.2813 0.0056  294 PHE A CG    
2439  C  CD1   . PHE A 294 ? 1.0519 0.3777 0.3525 0.0069  0.2835 0.0109  294 PHE A CD1   
2440  C  CD2   . PHE A 294 ? 1.048  0.3817 0.3552 -0.0096 0.2747 0.0024  294 PHE A CD2   
2441  C  CE1   . PHE A 294 ? 1.0455 0.3915 0.3664 0.0096  0.2791 0.0129  294 PHE A CE1   
2442  C  CE2   . PHE A 294 ? 1.0422 0.3951 0.369  -0.0065 0.2706 0.0043  294 PHE A CE2   
2443  C  CZ    . PHE A 294 ? 1.0344 0.3933 0.3679 0.0027  0.2727 0.0094  294 PHE A CZ    
2444  N  N     . ASN A 295 ? 1.0711 0.3555 0.3292 -0.0205 0.2842 -0.0025 295 ASN A N     
2445  C  CA    . ASN A 295 ? 1.075  0.3663 0.3397 -0.0258 0.2803 -0.0046 295 ASN A CA    
2446  C  C     . ASN A 295 ? 1.0887 0.3666 0.3415 -0.0221 0.2854 -0.0025 295 ASN A C     
2447  O  O     . ASN A 295 ? 1.0841 0.3716 0.3473 -0.0203 0.2836 -0.0015 295 ASN A O     
2448  C  CB    . ASN A 295 ? 1.0903 0.3801 0.351  -0.0375 0.2762 -0.0098 295 ASN A CB    
2449  C  CG    . ASN A 295 ? 1.1159 0.4205 0.3903 -0.0428 0.2703 -0.0118 295 ASN A CG    
2450  O  OD1   . ASN A 295 ? 1.1213 0.4389 0.4099 -0.038  0.2687 -0.0098 295 ASN A OD1   
2451  N  ND2   . ASN A 295 ? 1.1222 0.4252 0.3924 -0.0528 0.267  -0.0158 295 ASN A ND2   
2452  N  N     . ASN A 296 ? 1.1026 0.3584 0.3339 -0.0201 0.2921 -0.0016 296 ASN A N     
2453  C  CA    . ASN A 296 ? 1.1185 0.3594 0.3365 -0.0158 0.2977 0.0007  296 ASN A CA    
2454  C  C     . ASN A 296 ? 1.1076 0.3576 0.3367 -0.0044 0.3003 0.0063  296 ASN A C     
2455  O  O     . ASN A 296 ? 1.1099 0.3596 0.34   -0.0017 0.3015 0.0079  296 ASN A O     
2456  C  CB    . ASN A 296 ? 1.16   0.3746 0.3519 -0.0155 0.3047 0.0008  296 ASN A CB    
2457  C  CG    . ASN A 296 ? 1.2241 0.4274 0.4025 -0.0272 0.3027 -0.0044 296 ASN A CG    
2458  O  OD1   . ASN A 296 ? 1.2555 0.443  0.4178 -0.0287 0.3063 -0.0052 296 ASN A OD1   
2459  N  ND2   . ASN A 296 ? 1.2306 0.4419 0.4154 -0.0359 0.2969 -0.0079 296 ASN A ND2   
2460  N  N     . ILE A 297 ? 1.0933 0.3518 0.3311 0.0023  0.3009 0.0094  297 ILE A N     
2461  C  CA    . ILE A 297 ? 1.083  0.3522 0.3328 0.013   0.303  0.0151  297 ILE A CA    
2462  C  C     . ILE A 297 ? 1.0695 0.3604 0.3413 0.0115  0.2967 0.0148  297 ILE A C     
2463  O  O     . ILE A 297 ? 1.0679 0.3623 0.3446 0.0172  0.2986 0.0182  297 ILE A O     
2464  C  CB    . ILE A 297 ? 1.0806 0.3554 0.3354 0.0192  0.3041 0.0182  297 ILE A CB    
2465  C  CG1   . ILE A 297 ? 1.1029 0.3547 0.3348 0.0228  0.3118 0.0196  297 ILE A CG1   
2466  C  CG2   . ILE A 297 ? 1.0744 0.366  0.3465 0.0287  0.3041 0.0239  297 ILE A CG2   
2467  C  CD1   . ILE A 297 ? 1.1149 0.3704 0.3494 0.0271  0.3125 0.0215  297 ILE A CD1   
2468  N  N     . VAL A 298 ? 1.0576 0.3622 0.3416 0.0038  0.2895 0.0107  298 VAL A N     
2469  C  CA    . VAL A 298 ? 1.0442 0.3687 0.3482 0.0017  0.2835 0.01    298 VAL A CA    
2470  C  C     . VAL A 298 ? 1.0486 0.3675 0.3478 -0.0009 0.2841 0.0089  298 VAL A C     
2471  O  O     . VAL A 298 ? 1.0444 0.3724 0.3541 0.0036  0.2839 0.0115  298 VAL A O     
2472  C  CB    . VAL A 298 ? 1.0405 0.3782 0.3559 -0.0063 0.2763 0.0056  298 VAL A CB    
2473  C  CG1   . VAL A 298 ? 1.0329 0.3888 0.3664 -0.0089 0.2704 0.0046  298 VAL A CG1   
2474  C  CG2   . VAL A 298 ? 1.041  0.3862 0.3632 -0.0028 0.2754 0.0072  298 VAL A CG2   
2475  N  N     . GLN A 299 ? 1.0547 0.3577 0.337  -0.0079 0.2851 0.0052  299 GLN A N     
2476  C  CA    . GLN A 299 ? 1.0591 0.3547 0.3344 -0.0111 0.2857 0.0038  299 GLN A CA    
2477  C  C     . GLN A 299 ? 1.0677 0.351  0.3331 -0.0025 0.2927 0.0082  299 GLN A C     
2478  O  O     . GLN A 299 ? 1.0742 0.3547 0.3375 -0.0032 0.2931 0.008   299 GLN A O     
2479  C  CB    . GLN A 299 ? 1.0847 0.3661 0.3437 -0.0213 0.2848 -0.0011 299 GLN A CB    
2480  C  CG    . GLN A 299 ? 1.1137 0.4089 0.3839 -0.0297 0.2777 -0.0052 299 GLN A CG    
2481  C  CD    . GLN A 299 ? 1.165  0.4505 0.4228 -0.0405 0.2758 -0.0098 299 GLN A CD    
2482  O  OE1   . GLN A 299 ? 1.1884 0.4611 0.4331 -0.0433 0.2777 -0.0106 299 GLN A OE1   
2483  N  NE2   . GLN A 299 ? 1.168  0.4599 0.4299 -0.0471 0.2717 -0.0127 299 GLN A NE2   
2484  N  N     . ARG A 300 ? 1.066  0.343  0.3262 0.0061  0.2982 0.0125  300 ARG A N     
2485  C  CA    . ARG A 300 ? 1.0724 0.3386 0.3239 0.0154  0.3054 0.0176  300 ARG A CA    
2486  C  C     . ARG A 300 ? 1.0499 0.335  0.3217 0.0221  0.304  0.0216  300 ARG A C     
2487  O  O     . ARG A 300 ? 1.0562 0.3357 0.3241 0.027   0.3079 0.0245  300 ARG A O     
2488  C  CB    . ARG A 300 ? 1.1049 0.3592 0.3447 0.0225  0.3118 0.0211  300 ARG A CB    
2489  C  CG    . ARG A 300 ? 1.1713 0.4079 0.3952 0.0314  0.3207 0.0259  300 ARG A CG    
2490  C  CD    . ARG A 300 ? 1.232  0.4563 0.4434 0.0381  0.327  0.0292  300 ARG A CD    
2491  N  NE    . ARG A 300 ? 1.2857 0.4921 0.478  0.0308  0.3279 0.0248  300 ARG A NE    
2492  C  CZ    . ARG A 300 ? 1.3183 0.5218 0.5066 0.0312  0.3288 0.0246  300 ARG A CZ    
2493  N  NH1   . ARG A 300 ? 1.3038 0.5212 0.5056 0.0387  0.3288 0.0287  300 ARG A NH1   
2494  N  NH2   . ARG A 300 ? 1.3324 0.5188 0.5027 0.024   0.3297 0.0204  300 ARG A NH2   
2495  N  N     . TYR A 301 ? 1.0203 0.3272 0.3131 0.0221  0.2984 0.0219  301 TYR A N     
2496  C  CA    . TYR A 301 ? 0.9969 0.3221 0.3091 0.0283  0.297  0.026   301 TYR A CA    
2497  C  C     . TYR A 301 ? 0.9704 0.3154 0.302  0.0225  0.2891 0.0231  301 TYR A C     
2498  O  O     . TYR A 301 ? 0.9599 0.3189 0.3066 0.0268  0.2879 0.0262  301 TYR A O     
2499  C  CB    . TYR A 301 ? 0.9903 0.3246 0.3111 0.0358  0.2982 0.0307  301 TYR A CB    
2500  C  CG    . TYR A 301 ? 1.0105 0.3272 0.3139 0.0431  0.3063 0.0346  301 TYR A CG    
2501  C  CD1   . TYR A 301 ? 1.0242 0.3347 0.3229 0.0523  0.3128 0.0403  301 TYR A CD1   
2502  C  CD2   . TYR A 301 ? 1.0302 0.3368 0.3222 0.0413  0.3075 0.0329  301 TYR A CD2   
2503  C  CE1   . TYR A 301 ? 1.0455 0.3393 0.3275 0.0596  0.3207 0.0442  301 TYR A CE1   
2504  C  CE2   . TYR A 301 ? 1.0537 0.3433 0.3288 0.0482  0.3153 0.0365  301 TYR A CE2   
2505  C  CZ    . TYR A 301 ? 1.0661 0.3492 0.3361 0.0575  0.322  0.0422  301 TYR A CZ    
2506  O  OH    . TYR A 301 ? 1.097  0.3632 0.35   0.0649  0.33   0.0461  301 TYR A OH    
2507  N  N     . SER A 302 ? 0.9569 0.3038 0.2887 0.0131  0.2839 0.0175  302 SER A N     
2508  C  CA    . SER A 302 ? 0.9386 0.3042 0.2884 0.0076  0.2766 0.0147  302 SER A CA    
2509  C  C     . SER A 302 ? 0.932  0.2998 0.2848 0.0051  0.2752 0.0135  302 SER A C     
2510  O  O     . SER A 302 ? 0.9475 0.3    0.2856 0.0046  0.279  0.013   302 SER A O     
2511  C  CB    . SER A 302 ? 0.9435 0.3106 0.2924 -0.0013 0.2718 0.0095  302 SER A CB    
2512  O  OG    . SER A 302 ? 0.9683 0.3208 0.3016 -0.0082 0.2725 0.0057  302 SER A OG    
2513  N  N     . VAL A 303 ? 0.9049 0.2915 0.2766 0.0038  0.2699 0.0131  303 VAL A N     
2514  C  CA    . VAL A 303 ? 0.8954 0.2879 0.2733 0.0005  0.2672 0.0113  303 VAL A CA    
2515  C  C     . VAL A 303 ? 0.8846 0.2895 0.2727 -0.0077 0.2601 0.0067  303 VAL A C     
2516  O  O     . VAL A 303 ? 0.8836 0.2985 0.2808 -0.0081 0.257  0.0066  303 VAL A O     
2517  C  CB    . VAL A 303 ? 0.8961 0.2994 0.287  0.0075  0.2681 0.0157  303 VAL A CB    
2518  C  CG1   . VAL A 303 ? 0.9114 0.3014 0.2911 0.0157  0.2757 0.0205  303 VAL A CG1   
2519  C  CG2   . VAL A 303 ? 0.8904 0.3124 0.3    0.0102  0.2646 0.0179  303 VAL A CG2   
2520  N  N     . GLY A 304 ? 0.875  0.2781 0.26   -0.0143 0.2577 0.003   304 GLY A N     
2521  C  CA    . GLY A 304 ? 0.8626 0.2762 0.2555 -0.0222 0.2515 -0.0012 304 GLY A CA    
2522  C  C     . GLY A 304 ? 0.8421 0.2757 0.2555 -0.0213 0.2469 -0.0006 304 GLY A C     
2523  O  O     . GLY A 304 ? 0.8417 0.281  0.2627 -0.0171 0.2476 0.0018  304 GLY A O     
2524  N  N     . LEU A 305 ? 0.8275 0.2713 0.2494 -0.025  0.2424 -0.0026 305 LEU A N     
2525  C  CA    . LEU A 305 ? 0.8113 0.2731 0.2515 -0.0249 0.2378 -0.0025 305 LEU A CA    
2526  C  C     . LEU A 305 ? 0.7988 0.2663 0.2418 -0.0328 0.2332 -0.0067 305 LEU A C     
2527  O  O     . LEU A 305 ? 0.8015 0.2686 0.2419 -0.0376 0.2312 -0.0092 305 LEU A O     
2528  C  CB    . LEU A 305 ? 0.8108 0.28   0.2585 -0.0224 0.2364 -0.001  305 LEU A CB    
2529  C  CG    . LEU A 305 ? 0.8214 0.3081 0.2872 -0.021  0.2324 0.0001  305 LEU A CG    
2530  C  CD1   . LEU A 305 ? 0.8258 0.3165 0.2982 -0.0147 0.2345 0.0042  305 LEU A CD1   
2531  C  CD2   . LEU A 305 ? 0.8257 0.3184 0.2969 -0.02   0.2304 0.0008  305 LEU A CD2   
2532  N  N     . ALA A 306 ? 0.7834 0.2556 0.2312 -0.0341 0.2319 -0.0074 306 ALA A N     
2533  C  CA    . ALA A 306 ? 0.7763 0.2546 0.2273 -0.0409 0.2278 -0.0108 306 ALA A CA    
2534  C  C     . ALA A 306 ? 0.778  0.2443 0.2141 -0.0469 0.2286 -0.0136 306 ALA A C     
2535  O  O     . ALA A 306 ? 0.7804 0.247  0.2152 -0.0502 0.2274 -0.015  306 ALA A O     
2536  C  CB    . ALA A 306 ? 0.7707 0.2618 0.2329 -0.0437 0.2232 -0.0123 306 ALA A CB    
2537  N  N     . SER A 307 ? 0.7757 0.2317 0.2006 -0.0485 0.2303 -0.0142 307 SER A N     
2538  C  CA    . SER A 307 ? 0.782  0.2256 0.1917 -0.0547 0.2311 -0.0166 307 SER A CA    
2539  C  C     . SER A 307 ? 0.7869 0.2148 0.182  -0.0527 0.2356 -0.0157 307 SER A C     
2540  O  O     . SER A 307 ? 0.7867 0.2165 0.185  -0.0493 0.2362 -0.0143 307 SER A O     
2541  C  CB    . SER A 307 ? 0.7927 0.2437 0.2057 -0.0623 0.2266 -0.0197 307 SER A CB    
2542  O  OG    . SER A 307 ? 0.8106 0.2733 0.2335 -0.0649 0.223  -0.0208 307 SER A OG    
2543  N  N     . SER A 308 ? 0.7891 0.2011 0.1675 -0.055  0.2386 -0.0164 308 SER A N     
2544  C  CA    . SER A 308 ? 0.7961 0.1912 0.1586 -0.0533 0.2433 -0.0155 308 SER A CA    
2545  C  C     . SER A 308 ? 0.789  0.1835 0.1489 -0.0577 0.2419 -0.0174 308 SER A C     
2546  O  O     . SER A 308 ? 0.7966 0.1837 0.1507 -0.0539 0.2451 -0.0159 308 SER A O     
2547  C  CB    . SER A 308 ? 0.8235 0.2009 0.1675 -0.0562 0.2464 -0.0164 308 SER A CB    
2548  O  OG    . SER A 308 ? 0.8504 0.2264 0.1887 -0.0658 0.2431 -0.0199 308 SER A OG    
2549  N  N     . ASP A 309 ? 0.7728 0.1754 0.1372 -0.0654 0.2371 -0.0204 309 ASP A N     
2550  C  CA    . ASP A 309 ? 0.7682 0.17   0.1296 -0.07   0.2358 -0.0222 309 ASP A CA    
2551  C  C     . ASP A 309 ? 0.747  0.1655 0.125  -0.069  0.232  -0.0222 309 ASP A C     
2552  O  O     . ASP A 309 ? 0.7475 0.1671 0.1244 -0.0737 0.2303 -0.0239 309 ASP A O     
2553  C  CB    . ASP A 309 ? 0.7943 0.191  0.1461 -0.0798 0.2338 -0.0252 309 ASP A CB    
2554  C  CG    . ASP A 309 ? 0.8427 0.2534 0.2053 -0.0847 0.2289 -0.0267 309 ASP A CG    
2555  O  OD1   . ASP A 309 ? 0.8351 0.2556 0.2091 -0.0804 0.2278 -0.0255 309 ASP A OD1   
2556  O  OD2   . ASP A 309 ? 0.8783 0.29   0.2376 -0.0927 0.2262 -0.029  309 ASP A OD2   
2557  N  N     . LEU A 310 ? 0.7297 0.1599 0.122  -0.063  0.2311 -0.0201 310 LEU A N     
2558  C  CA    . LEU A 310 ? 0.722  0.166  0.1283 -0.0616 0.228  -0.0199 310 LEU A CA    
2559  C  C     . LEU A 310 ? 0.7355 0.172  0.1362 -0.0572 0.231  -0.0183 310 LEU A C     
2560  O  O     . LEU A 310 ? 0.7444 0.1682 0.1341 -0.0533 0.2356 -0.0165 310 LEU A O     
2561  C  CB    . LEU A 310 ? 0.7094 0.1672 0.1315 -0.0568 0.2261 -0.0181 310 LEU A CB    
2562  C  CG    . LEU A 310 ? 0.7144 0.184  0.1461 -0.0612 0.2219 -0.0199 310 LEU A CG    
2563  C  CD1   . LEU A 310 ? 0.7097 0.1907 0.1552 -0.0562 0.2207 -0.018  310 LEU A CD1   
2564  C  CD2   . LEU A 310 ? 0.72   0.1975 0.1565 -0.0666 0.2181 -0.0221 310 LEU A CD2   
2565  N  N     . PRO A 311 ? 0.7358 0.1791 0.1427 -0.0576 0.2289 -0.0187 311 PRO A N     
2566  C  CA    . PRO A 311 ? 0.7452 0.1806 0.1456 -0.0537 0.2319 -0.0173 311 PRO A CA    
2567  C  C     . PRO A 311 ? 0.7502 0.1876 0.1557 -0.0448 0.2342 -0.0134 311 PRO A C     
2568  O  O     . PRO A 311 ? 0.7529 0.1877 0.1564 -0.0413 0.2358 -0.012  311 PRO A O     
2569  C  CB    . PRO A 311 ? 0.7473 0.1908 0.154  -0.0571 0.2284 -0.019  311 PRO A CB    
2570  C  CG    . PRO A 311 ? 0.7406 0.1999 0.1624 -0.0589 0.2238 -0.0198 311 PRO A CG    
2571  C  CD    . PRO A 311 ? 0.7209 0.1783 0.1398 -0.0617 0.2239 -0.0206 311 PRO A CD    
2572  N  N     . PHE A 312 ? 0.7503 0.1926 0.1622 -0.0412 0.2345 -0.0116 312 PHE A N     
2573  C  CA    . PHE A 312 ? 0.7565 0.202  0.1742 -0.033  0.2365 -0.0075 312 PHE A CA    
2574  C  C     . PHE A 312 ? 0.778  0.219  0.193  -0.0294 0.2396 -0.0054 312 PHE A C     
2575  O  O     . PHE A 312 ? 0.782  0.2224 0.1956 -0.0333 0.2386 -0.0073 312 PHE A O     
2576  C  CB    . PHE A 312 ? 0.7373 0.2004 0.1728 -0.0314 0.2321 -0.0066 312 PHE A CB    
2577  C  CG    . PHE A 312 ? 0.734  0.2082 0.1797 -0.0362 0.2276 -0.009  312 PHE A CG    
2578  C  CD1   . PHE A 312 ? 0.7392 0.2175 0.1866 -0.0426 0.224  -0.0124 312 PHE A CD1   
2579  C  CD2   . PHE A 312 ? 0.7389 0.2195 0.1924 -0.0339 0.2272 -0.0076 312 PHE A CD2   
2580  C  CE1   . PHE A 312 ? 0.7412 0.2296 0.1975 -0.0465 0.2203 -0.0142 312 PHE A CE1   
2581  C  CE2   . PHE A 312 ? 0.7402 0.2305 0.2023 -0.0381 0.2233 -0.0098 312 PHE A CE2   
2582  C  CZ    . PHE A 312 ? 0.7354 0.2294 0.1986 -0.0442 0.22   -0.013  312 PHE A CZ    
2583  N  N     . GLY A 313 ? 0.7896 0.2278 0.2037 -0.0218 0.2434 -0.0013 313 GLY A N     
2584  C  CA    . GLY A 313 ? 0.8092 0.2433 0.2212 -0.017  0.247  0.0014  313 GLY A CA    
2585  C  C     . GLY A 313 ? 0.8217 0.262  0.2417 -0.0084 0.249  0.0065  313 GLY A C     
2586  O  O     . GLY A 313 ? 0.8165 0.2655 0.2447 -0.0067 0.2469 0.0077  313 GLY A O     
2587  N  N     . VAL A 314 ? 0.8358 0.2721 0.2537 -0.003  0.2529 0.0098  314 VAL A N     
2588  C  CA    . VAL A 314 ? 0.849  0.2922 0.2751 0.0053  0.255  0.0153  314 VAL A CA    
2589  C  C     . VAL A 314 ? 0.8734 0.3017 0.2856 0.012   0.2621 0.0191  314 VAL A C     
2590  O  O     . VAL A 314 ? 0.8826 0.2964 0.2809 0.0112  0.2658 0.0181  314 VAL A O     
2591  C  CB    . VAL A 314 ? 0.8535 0.3096 0.2939 0.007   0.2529 0.017   314 VAL A CB    
2592  C  CG1   . VAL A 314 ? 0.8548 0.3199 0.3051 0.0151  0.2546 0.023   314 VAL A CG1   
2593  C  CG2   . VAL A 314 ? 0.8549 0.3248 0.3081 0.0004  0.2461 0.0132  314 VAL A CG2   
2594  N  N     . ILE A 315 ? 0.8827 0.3144 0.2981 0.0187  0.2642 0.0235  315 ILE A N     
2595  C  CA    . ILE A 315 ? 0.9077 0.3282 0.3127 0.0268  0.2712 0.0284  315 ILE A CA    
2596  C  C     . ILE A 315 ? 0.9142 0.3491 0.3345 0.0334  0.2712 0.0338  315 ILE A C     
2597  O  O     . ILE A 315 ? 0.9068 0.3563 0.3406 0.0349  0.2678 0.0358  315 ILE A O     
2598  C  CB    . ILE A 315 ? 0.9197 0.3344 0.3174 0.0296  0.2734 0.0297  315 ILE A CB    
2599  C  CG1   . ILE A 315 ? 0.9418 0.3445 0.3264 0.0221  0.2725 0.0241  315 ILE A CG1   
2600  C  CG2   . ILE A 315 ? 0.9322 0.3362 0.3199 0.039   0.2812 0.0356  315 ILE A CG2   
2601  C  CD1   . ILE A 315 ? 0.9747 0.357  0.3396 0.0201  0.2773 0.0222  315 ILE A CD1   
2602  N  N     . ARG A 316 ? 0.9231 0.3547 0.342  0.0364  0.2744 0.0359  316 ARG A N     
2603  C  CA    . ARG A 316 ? 0.9264 0.3715 0.3597 0.0424  0.2746 0.0411  316 ARG A CA    
2604  C  C     . ARG A 316 ? 0.9327 0.38   0.3672 0.0513  0.2785 0.0477  316 ARG A C     
2605  O  O     . ARG A 316 ? 0.944  0.3773 0.3639 0.0544  0.2835 0.0488  316 ARG A O     
2606  C  CB    . ARG A 316 ? 0.9525 0.3912 0.3817 0.0443  0.2781 0.0421  316 ARG A CB    
2607  C  CG    . ARG A 316 ? 0.997  0.4351 0.4261 0.0359  0.2741 0.0361  316 ARG A CG    
2608  C  CD    . ARG A 316 ? 1.038  0.4756 0.4687 0.0381  0.2761 0.0376  316 ARG A CD    
2609  N  NE    . ARG A 316 ? 1.0912 0.5101 0.5046 0.0431  0.2836 0.04    316 ARG A NE    
2610  C  CZ    . ARG A 316 ? 1.1364 0.5434 0.5391 0.0408  0.2856 0.0376  316 ARG A CZ    
2611  N  NH1   . ARG A 316 ? 1.1263 0.5387 0.5341 0.0335  0.2806 0.0329  316 ARG A NH1   
2612  N  NH2   . ARG A 316 ? 1.1572 0.5466 0.5434 0.0458  0.2927 0.0401  316 ARG A NH2   
2613  N  N     . LYS A 317 ? 0.9246 0.3894 0.3761 0.0552  0.2765 0.0523  317 LYS A N     
2614  C  CA    . LYS A 317 ? 0.9329 0.4022 0.3873 0.0636  0.2797 0.0591  317 LYS A CA    
2615  C  C     . LYS A 317 ? 0.9497 0.4039 0.3899 0.0719  0.2886 0.0639  317 LYS A C     
2616  O  O     . LYS A 317 ? 0.9538 0.4037 0.388  0.0781  0.2927 0.068   317 LYS A O     
2617  C  CB    . LYS A 317 ? 0.9449 0.436  0.4203 0.0658  0.2758 0.0634  317 LYS A CB    
2618  C  CG    . LYS A 317 ? 0.9988 0.4955 0.482  0.0671  0.2765 0.0652  317 LYS A CG    
2619  C  CD    . LYS A 317 ? 1.0499 0.5683 0.5537 0.0682  0.2721 0.0692  317 LYS A CD    
2620  C  CE    . LYS A 317 ? 1.0995 0.6239 0.6117 0.0677  0.2717 0.0698  317 LYS A CE    
2621  N  NZ    . LYS A 317 ? 1.1323 0.6535 0.6431 0.0591  0.2675 0.0623  317 LYS A NZ    
2622  N  N     . GLU A 318 ? 0.958  0.4029 0.3914 0.0721  0.2918 0.0632  318 GLU A N     
2623  C  CA    . GLU A 318 ? 0.9783 0.407  0.3967 0.0795  0.3005 0.0672  318 GLU A CA    
2624  C  C     . GLU A 318 ? 1.0021 0.4089 0.3983 0.079   0.305  0.0647  318 GLU A C     
2625  O  O     . GLU A 318 ? 1.014  0.4073 0.3969 0.0865  0.3126 0.0691  318 GLU A O     
2626  C  CB    . GLU A 318 ? 1.0044 0.4287 0.4212 0.0784  0.3018 0.0662  318 GLU A CB    
2627  C  CG    . GLU A 318 ? 1.0395 0.4829 0.4761 0.0809  0.2994 0.07    318 GLU A CG    
2628  C  CD    . GLU A 318 ? 1.0855 0.5459 0.5389 0.0727  0.2906 0.0655  318 GLU A CD    
2629  O  OE1   . GLU A 318 ? 1.1017 0.5578 0.5505 0.0644  0.2864 0.0587  318 GLU A OE1   
2630  O  OE2   . GLU A 318 ? 1.0888 0.5667 0.5596 0.0745  0.2879 0.069   318 GLU A OE2   
2631  N  N     . SER A 319 ? 1.0067 0.4097 0.3984 0.0702  0.3004 0.0579  319 SER A N     
2632  C  CA    . SER A 319 ? 1.0276 0.4107 0.3988 0.0684  0.3038 0.055   319 SER A CA    
2633  C  C     . SER A 319 ? 1.031  0.4189 0.4046 0.0671  0.3011 0.0542  319 SER A C     
2634  O  O     . SER A 319 ? 1.0453 0.4173 0.4025 0.0658  0.304  0.052   319 SER A O     
2635  C  CB    . SER A 319 ? 1.0527 0.425  0.4141 0.0588  0.3014 0.0477  319 SER A CB    
2636  O  OG    . SER A 319 ? 1.0905 0.4554 0.4467 0.0596  0.3043 0.048   319 SER A OG    
2637  N  N     . ARG A 320 ? 1.0165 0.4255 0.4098 0.0669  0.2954 0.0555  320 ARG A N     
2638  C  CA    . ARG A 320 ? 1.0177 0.433  0.4148 0.0655  0.2921 0.0547  320 ARG A CA    
2639  C  C     . ARG A 320 ? 1.0302 0.4356 0.416  0.0734  0.2984 0.0594  320 ARG A C     
2640  O  O     . ARG A 320 ? 1.0374 0.4344 0.4137 0.0708  0.2984 0.0566  320 ARG A O     
2641  C  CB    . ARG A 320 ? 1.0164 0.4558 0.4364 0.0646  0.2852 0.0562  320 ARG A CB    
2642  C  CG    . ARG A 320 ? 1.0418 0.4888 0.4666 0.0641  0.2818 0.0562  320 ARG A CG    
2643  C  CD    . ARG A 320 ? 1.072  0.5227 0.5003 0.0543  0.2749 0.0492  320 ARG A CD    
2644  N  NE    . ARG A 320 ? 1.0918 0.5622 0.5396 0.0512  0.2682 0.0489  320 ARG A NE    
2645  C  CZ    . ARG A 320 ? 1.1093 0.5946 0.57   0.0507  0.2631 0.0499  320 ARG A CZ    
2646  N  NH1   . ARG A 320 ? 1.0935 0.5951 0.5705 0.0477  0.2575 0.0497  320 ARG A NH1   
2647  N  NH2   . ARG A 320 ? 1.1083 0.5916 0.5647 0.0524  0.2635 0.0507  320 ARG A NH2   
2648  N  N     . ASN A 321 ? 1.0312 0.437  0.4172 0.0832  0.3042 0.0667  321 ASN A N     
2649  C  CA    . ASN A 321 ? 1.0436 0.4403 0.4189 0.0918  0.3109 0.0719  321 ASN A CA    
2650  C  C     . ASN A 321 ? 1.0647 0.4356 0.4152 0.0904  0.3164 0.0685  321 ASN A C     
2651  O  O     . ASN A 321 ? 1.0715 0.4356 0.4135 0.0911  0.3178 0.0682  321 ASN A O     
2652  C  CB    . ASN A 321 ? 1.0519 0.4527 0.431  0.1025  0.3166 0.0804  321 ASN A CB    
2653  C  CG    . ASN A 321 ? 1.0798 0.4948 0.4697 0.11    0.3168 0.0873  321 ASN A CG    
2654  O  OD1   . ASN A 321 ? 1.0809 0.5175 0.4908 0.1091  0.3109 0.0891  321 ASN A OD1   
2655  N  ND2   . ASN A 321 ? 1.0942 0.4974 0.4706 0.1174  0.3236 0.0913  321 ASN A ND2   
2656  N  N     . ASP A 322 ? 1.0727 0.4293 0.4115 0.0876  0.3191 0.0658  322 ASP A N     
2657  C  CA    . ASP A 322 ? 1.0947 0.4259 0.4091 0.0854  0.3242 0.0624  322 ASP A CA    
2658  C  C     . ASP A 322 ? 1.094  0.4219 0.4044 0.0749  0.3189 0.0549  322 ASP A C     
2659  O  O     . ASP A 322 ? 1.1073 0.4186 0.4007 0.0743  0.3225 0.0534  322 ASP A O     
2660  C  CB    . ASP A 322 ? 1.1282 0.4459 0.4317 0.0847  0.3279 0.0615  322 ASP A CB    
2661  C  CG    . ASP A 322 ? 1.1943 0.5073 0.4939 0.096   0.3358 0.0692  322 ASP A CG    
2662  O  OD1   . ASP A 322 ? 1.2056 0.5163 0.5013 0.1046  0.3409 0.0748  322 ASP A OD1   
2663  O  OD2   . ASP A 322 ? 1.2262 0.5379 0.5265 0.0965  0.3369 0.0697  322 ASP A OD2   
2664  N  N     . PHE A 323 ? 1.075  0.4186 0.4011 0.0668  0.3106 0.0504  323 PHE A N     
2665  C  CA    . PHE A 323 ? 1.0759 0.4187 0.4005 0.057   0.3052 0.0436  323 PHE A CA    
2666  C  C     . PHE A 323 ? 1.0737 0.4205 0.4    0.0594  0.3047 0.045   323 PHE A C     
2667  O  O     . PHE A 323 ? 1.0844 0.4173 0.3963 0.0563  0.3063 0.042   323 PHE A O     
2668  C  CB    . PHE A 323 ? 1.0624 0.4227 0.4047 0.0492  0.2968 0.0395  323 PHE A CB    
2669  C  CG    . PHE A 323 ? 1.0679 0.4334 0.4141 0.0405  0.2905 0.0339  323 PHE A CG    
2670  C  CD1   . PHE A 323 ? 1.0865 0.4385 0.4191 0.0325  0.2901 0.0282  323 PHE A CD1   
2671  C  CD2   . PHE A 323 ? 1.0651 0.4493 0.4284 0.0403  0.2849 0.0344  323 PHE A CD2   
2672  C  CE1   . PHE A 323 ? 1.0909 0.4481 0.4274 0.0247  0.2846 0.0233  323 PHE A CE1   
2673  C  CE2   . PHE A 323 ? 1.0697 0.458  0.4361 0.0326  0.2795 0.0294  323 PHE A CE2   
2674  C  CZ    . PHE A 323 ? 1.0754 0.4505 0.4286 0.0251  0.2795 0.024   323 PHE A CZ    
2675  N  N     . ILE A 324 ? 1.0578 0.4224 0.4005 0.0653  0.3028 0.0499  324 ILE A N     
2676  C  CA    . ILE A 324 ? 1.055  0.4251 0.4008 0.0684  0.3021 0.0518  324 ILE A CA    
2677  C  C     . ILE A 324 ? 1.0701 0.421  0.3962 0.075   0.3104 0.0549  324 ILE A C     
2678  O  O     . ILE A 324 ? 1.0797 0.4242 0.3982 0.073   0.3104 0.0526  324 ILE A O     
2679  C  CB    . ILE A 324 ? 1.0436 0.437  0.4109 0.0733  0.2983 0.057   324 ILE A CB    
2680  C  CG1   . ILE A 324 ? 1.0413 0.4526 0.4269 0.0656  0.2896 0.0531  324 ILE A CG1   
2681  C  CG2   . ILE A 324 ? 1.0466 0.4445 0.4155 0.0778  0.2985 0.06    324 ILE A CG2   
2682  C  CD1   . ILE A 324 ? 1.0564 0.4675 0.4416 0.0561  0.284  0.0461  324 ILE A CD1   
2683  N  N     . ASN A 325 ? 1.0724 0.4129 0.389  0.0826  0.3178 0.0596  325 ASN A N     
2684  C  CA    . ASN A 325 ? 1.0894 0.4097 0.3854 0.0894  0.3265 0.0628  325 ASN A CA    
2685  C  C     . ASN A 325 ? 1.1016 0.4006 0.3774 0.0819  0.3279 0.0563  325 ASN A C     
2686  O  O     . ASN A 325 ? 1.109  0.3969 0.3726 0.0837  0.3313 0.0564  325 ASN A O     
2687  C  CB    . ASN A 325 ? 1.1112 0.4228 0.3998 0.0979  0.3341 0.0684  325 ASN A CB    
2688  C  CG    . ASN A 325 ? 1.141  0.4686 0.4437 0.1084  0.3358 0.0768  325 ASN A CG    
2689  O  OD1   . ASN A 325 ? 1.1449 0.4884 0.4609 0.1106  0.3324 0.0793  325 ASN A OD1   
2690  N  ND2   . ASN A 325 ? 1.1508 0.4743 0.4507 0.115   0.3414 0.0816  325 ASN A ND2   
2691  N  N     . ASP A 326 ? 1.1012 0.3952 0.3739 0.0731  0.3251 0.0507  326 ASP A N     
2692  C  CA    . ASP A 326 ? 1.1175 0.3926 0.372  0.0647  0.3257 0.0445  326 ASP A CA    
2693  C  C     . ASP A 326 ? 1.1158 0.3972 0.3751 0.0578  0.32   0.0399  326 ASP A C     
2694  O  O     . ASP A 326 ? 1.1298 0.3951 0.3727 0.0552  0.3228 0.0375  326 ASP A O     
2695  C  CB    . ASP A 326 ? 1.1387 0.4091 0.3903 0.0573  0.3236 0.0401  326 ASP A CB    
2696  C  CG    . ASP A 326 ? 1.2014 0.4533 0.4363 0.0622  0.3313 0.0429  326 ASP A CG    
2697  O  OD1   . ASP A 326 ? 1.2217 0.4604 0.4432 0.0706  0.339  0.0475  326 ASP A OD1   
2698  O  OD2   . ASP A 326 ? 1.2205 0.4701 0.4545 0.0575  0.3298 0.0403  326 ASP A OD2   
2699  N  N     . VAL A 327 ? 1.0972 0.4014 0.3784 0.0549  0.3123 0.0389  327 VAL A N     
2700  C  CA    . VAL A 327 ? 1.0966 0.4078 0.3834 0.0489  0.3068 0.035   327 VAL A CA    
2701  C  C     . VAL A 327 ? 1.1018 0.4097 0.3836 0.0559  0.3105 0.0387  327 VAL A C     
2702  O  O     . VAL A 327 ? 1.1118 0.4103 0.3836 0.0521  0.3108 0.0355  327 VAL A O     
2703  C  CB    . VAL A 327 ? 1.089  0.4244 0.3995 0.0446  0.298  0.0334  327 VAL A CB    
2704  C  CG1   . VAL A 327 ? 1.0927 0.435  0.4086 0.0396  0.293  0.03    327 VAL A CG1   
2705  C  CG2   . VAL A 327 ? 1.0923 0.4296 0.4061 0.0371  0.2945 0.0292  327 VAL A CG2   
2706  N  N     . CYS A 328 ? 1.0934 0.4081 0.3811 0.0664  0.3139 0.0457  328 CYS A N     
2707  C  CA    . CYS A 328 ? 1.0979 0.4107 0.3816 0.0744  0.3178 0.0502  328 CYS A CA    
2708  C  C     . CYS A 328 ? 1.1198 0.4066 0.378  0.0765  0.3259 0.05    328 CYS A C     
2709  O  O     . CYS A 328 ? 1.1247 0.4059 0.3759 0.0776  0.3274 0.0499  328 CYS A O     
2710  C  CB    . CYS A 328 ? 1.0935 0.4197 0.3891 0.085   0.3197 0.0582  328 CYS A CB    
2711  S  SG    . CYS A 328 ? 1.1068 0.4645 0.4324 0.0831  0.3099 0.0591  328 CYS A SG    
2712  N  N     . LYS A 329 ? 1.1328 0.4032 0.3766 0.0768  0.3312 0.05    329 LYS A N     
2713  C  CA    . LYS A 329 ? 1.1568 0.4003 0.3744 0.0783  0.3392 0.0496  329 LYS A CA    
2714  C  C     . LYS A 329 ? 1.1699 0.4031 0.3775 0.0673  0.3363 0.0422  329 LYS A C     
2715  O  O     . LYS A 329 ? 1.1827 0.4014 0.3752 0.0684  0.3405 0.0419  329 LYS A O     
2716  C  CB    . LYS A 329 ? 1.1812 0.4098 0.3861 0.0801  0.3447 0.0508  329 LYS A CB    
2717  C  CG    . LYS A 329 ? 1.2359 0.4445 0.4208 0.0904  0.3553 0.0563  329 LYS A CG    
2718  C  CD    . LYS A 329 ? 1.2748 0.4977 0.4723 0.1029  0.3581 0.0648  329 LYS A CD    
2719  C  CE    . LYS A 329 ? 1.3303 0.5342 0.5084 0.1139  0.3689 0.0708  329 LYS A CE    
2720  N  NZ    . LYS A 329 ? 1.3464 0.5655 0.5378 0.1261  0.3715 0.0796  329 LYS A NZ    
2721  N  N     . LEU A 330 ? 1.1638 0.4051 0.3803 0.057   0.3292 0.0366  330 LEU A N     
2722  C  CA    . LEU A 330 ? 1.1733 0.407  0.3822 0.046   0.326  0.0297  330 LEU A CA    
2723  C  C     . LEU A 330 ? 1.1691 0.4104 0.3838 0.0451  0.3229 0.0287  330 LEU A C     
2724  O  O     . LEU A 330 ? 1.178  0.4046 0.3779 0.0412  0.325  0.0258  330 LEU A O     
2725  C  CB    . LEU A 330 ? 1.1707 0.4148 0.3906 0.0361  0.3188 0.0248  330 LEU A CB    
2726  C  CG    . LEU A 330 ? 1.1944 0.4332 0.4086 0.0241  0.3148 0.018   330 LEU A CG    
2727  C  CD1   . LEU A 330 ? 1.2217 0.4335 0.4094 0.021   0.3209 0.016   330 LEU A CD1   
2728  C  CD2   . LEU A 330 ? 1.1917 0.4442 0.4196 0.0158  0.3075 0.014   330 LEU A CD2   
2729  N  N     . TYR A 331 ? 1.1562 0.42   0.3922 0.0483  0.3179 0.031   331 TYR A N     
2730  C  CA    . TYR A 331 ? 1.1601 0.4329 0.4035 0.0472  0.3141 0.0299  331 TYR A CA    
2731  C  C     . TYR A 331 ? 1.1747 0.449  0.4178 0.0579  0.3181 0.0358  331 TYR A C     
2732  O  O     . TYR A 331 ? 1.1703 0.4544 0.4216 0.0578  0.3146 0.0355  331 TYR A O     
2733  C  CB    . TYR A 331 ? 1.1404 0.4367 0.4069 0.0417  0.3048 0.0275  331 TYR A CB    
2734  C  CG    . TYR A 331 ? 1.1454 0.4403 0.4115 0.0302  0.3003 0.021   331 TYR A CG    
2735  C  CD1   . TYR A 331 ? 1.1623 0.4461 0.4171 0.0226  0.3    0.0162  331 TYR A CD1   
2736  C  CD2   . TYR A 331 ? 1.1488 0.4542 0.4262 0.027   0.2964 0.02    331 TYR A CD2   
2737  C  CE1   . TYR A 331 ? 1.1728 0.4567 0.428  0.012   0.2958 0.0107  331 TYR A CE1   
2738  C  CE2   . TYR A 331 ? 1.1595 0.4646 0.437  0.0166  0.2922 0.0144  331 TYR A CE2   
2739  C  CZ    . TYR A 331 ? 1.1765 0.4712 0.4432 0.0092  0.2919 0.0099  331 TYR A CZ    
2740  O  OH    . TYR A 331 ? 1.1939 0.4891 0.4609 -0.001  0.2878 0.0048  331 TYR A OH    
2741  N  N     . ASN A 332 ? 1.1898 0.454  0.4229 0.0671  0.3257 0.0413  332 ASN A N     
2742  C  CA    . ASN A 332 ? 1.2051 0.4699 0.4366 0.0782  0.3305 0.0477  332 ASN A CA    
2743  C  C     . ASN A 332 ? 1.1992 0.49   0.4543 0.0822  0.3246 0.0513  332 ASN A C     
2744  O  O     . ASN A 332 ? 1.1955 0.4914 0.4534 0.0859  0.3242 0.0533  332 ASN A O     
2745  C  CB    . ASN A 332 ? 1.2327 0.4809 0.4469 0.0782  0.3345 0.0462  332 ASN A CB    
2746  C  CG    . ASN A 332 ? 1.2832 0.5208 0.4853 0.0901  0.3432 0.0528  332 ASN A CG    
2747  O  OD1   . ASN A 332 ? 1.3045 0.5359 0.5009 0.0973  0.349  0.0575  332 ASN A OD1   
2748  N  ND2   . ASN A 332 ? 1.2933 0.5286 0.4912 0.0929  0.3444 0.0536  332 ASN A ND2   
2749  N  N     . ILE A 333 ? 1.1969 0.5039 0.4688 0.0812  0.3202 0.0522  333 ILE A N     
2750  C  CA    . ILE A 333 ? 1.1984 0.5299 0.4925 0.0846  0.3146 0.0558  333 ILE A CA    
2751  C  C     . ILE A 333 ? 1.2139 0.548  0.5087 0.0969  0.3205 0.0644  333 ILE A C     
2752  O  O     . ILE A 333 ? 1.219  0.5486 0.5108 0.1002  0.3244 0.067   333 ILE A O     
2753  C  CB    . ILE A 333 ? 1.1949 0.5426 0.5066 0.0775  0.307  0.0527  333 ILE A CB    
2754  C  CG1   . ILE A 333 ? 1.2094 0.5536 0.5191 0.0657  0.3019 0.0445  333 ILE A CG1   
2755  C  CG2   . ILE A 333 ? 1.1865 0.5589 0.5204 0.0805  0.3012 0.0565  333 ILE A CG2   
2756  C  CD1   . ILE A 333 ? 1.2184 0.575  0.5419 0.0587  0.2956 0.0412  333 ILE A CD1   
2757  N  N     . ASN A 334 ? 1.2203 0.5609 0.5183 0.1038  0.3214 0.0691  334 ASN A N     
2758  C  CA    . ASN A 334 ? 1.2349 0.5785 0.5335 0.116   0.3272 0.078   334 ASN A CA    
2759  C  C     . ASN A 334 ? 1.2258 0.5954 0.5466 0.1203  0.3219 0.0833  334 ASN A C     
2760  O  O     . ASN A 334 ? 1.2252 0.6006 0.5493 0.1302  0.326  0.0911  334 ASN A O     
2761  C  CB    . ASN A 334 ? 1.2711 0.5959 0.5496 0.123   0.3356 0.0806  334 ASN A CB    
2762  C  CG    . ASN A 334 ? 1.3386 0.6367 0.5935 0.1223  0.3433 0.0783  334 ASN A CG    
2763  O  OD1   . ASN A 334 ? 1.3704 0.6511 0.6092 0.1176  0.3452 0.0734  334 ASN A OD1   
2764  N  ND2   . ASN A 334 ? 1.347  0.6408 0.5989 0.1269  0.3479 0.0818  334 ASN A ND2   
2765  N  N     . ASP A 335 ? 1.2164 0.6014 0.5521 0.1129  0.3128 0.0793  335 ASP A N     
2766  C  CA    . ASP A 335 ? 1.2084 0.6176 0.5645 0.1157  0.3071 0.0838  335 ASP A CA    
2767  C  C     . ASP A 335 ? 1.2051 0.6289 0.5761 0.1175  0.3054 0.0876  335 ASP A C     
2768  O  O     . ASP A 335 ? 1.2041 0.6306 0.5809 0.11    0.3014 0.083   335 ASP A O     
2769  C  CB    . ASP A 335 ? 1.2187 0.6386 0.5851 0.107   0.2981 0.0782  335 ASP A CB    
2770  C  CG    . ASP A 335 ? 1.2532 0.6948 0.6368 0.1104  0.2929 0.083   335 ASP A CG    
2771  O  OD1   . ASP A 335 ? 1.2624 0.7034 0.6418 0.1173  0.2958 0.0875  335 ASP A OD1   
2772  O  OD2   . ASP A 335 ? 1.264  0.723  0.6648 0.106   0.2859 0.0825  335 ASP A OD2   
2773  N  N     . MET A 336 ? 1.2015 0.6348 0.5786 0.1274  0.3086 0.0963  336 MET A N     
2774  C  CA    . MET A 336 ? 1.1997 0.6476 0.591  0.1304  0.3077 0.1013  336 MET A CA    
2775  C  C     . MET A 336 ? 1.1796 0.6479 0.5915 0.1223  0.2977 0.0983  336 MET A C     
2776  O  O     . MET A 336 ? 1.1774 0.65   0.5962 0.1193  0.2962 0.0973  336 MET A O     
2777  C  CB    . MET A 336 ? 1.2153 0.6724 0.611  0.1424  0.3122 0.1117  336 MET A CB    
2778  C  CG    . MET A 336 ? 1.2535 0.7241 0.6624 0.1464  0.3126 0.1175  336 MET A CG    
2779  S  SD    . MET A 336 ? 1.3431 0.8286 0.7602 0.16    0.3168 0.1304  336 MET A SD    
2780  C  CE    . MET A 336 ? 1.3142 0.8117 0.7447 0.1622  0.3173 0.1351  336 MET A CE    
2781  N  N     . LYS A 337 ? 1.1633 0.6434 0.5843 0.1189  0.291  0.0969  337 LYS A N     
2782  C  CA    . LYS A 337 ? 1.1487 0.6473 0.5881 0.1113  0.2815 0.0941  337 LYS A CA    
2783  C  C     . LYS A 337 ? 1.146  0.6375 0.5832 0.101   0.2783 0.0854  337 LYS A C     
2784  O  O     . LYS A 337 ? 1.1394 0.6415 0.5888 0.0969  0.274  0.0843  337 LYS A O     
2785  C  CB    . LYS A 337 ? 1.1656 0.6747 0.6117 0.1095  0.2755 0.0938  337 LYS A CB    
2786  C  CG    . LYS A 337 ? 1.2106 0.7286 0.6599 0.1192  0.2779 0.1025  337 LYS A CG    
2787  C  CD    . LYS A 337 ? 1.2566 0.7897 0.717  0.1163  0.2701 0.1025  337 LYS A CD    
2788  C  CE    . LYS A 337 ? 1.3121 0.8335 0.7618 0.1114  0.2687 0.0959  337 LYS A CE    
2789  N  NZ    . LYS A 337 ? 1.3511 0.8603 0.7863 0.1193  0.2755 0.0992  337 LYS A NZ    
2790  N  N     . ILE A 338 ? 1.1494 0.6229 0.571  0.0971  0.2805 0.0795  338 ILE A N     
2791  C  CA    . ILE A 338 ? 1.1515 0.6171 0.5693 0.0875  0.2779 0.0714  338 ILE A CA    
2792  C  C     . ILE A 338 ? 1.1513 0.6107 0.5661 0.0878  0.2815 0.0715  338 ILE A C     
2793  O  O     . ILE A 338 ? 1.1472 0.6126 0.5703 0.0812  0.277  0.0677  338 ILE A O     
2794  C  CB    . ILE A 338 ? 1.1689 0.6163 0.5695 0.0842  0.2803 0.0662  338 ILE A CB    
2795  C  CG1   . ILE A 338 ? 1.1768 0.632  0.5827 0.0818  0.2749 0.0646  338 ILE A CG1   
2796  C  CG2   . ILE A 338 ? 1.1803 0.6163 0.5736 0.0755  0.2796 0.0588  338 ILE A CG2   
2797  C  CD1   . ILE A 338 ? 1.2037 0.642  0.5934 0.079   0.2773 0.06    338 ILE A CD1   
2798  N  N     . ILE A 339 ? 1.1537 0.6008 0.5563 0.0957  0.2899 0.076   339 ILE A N     
2799  C  CA    . ILE A 339 ? 1.1586 0.5977 0.5562 0.0971  0.2944 0.0768  339 ILE A CA    
2800  C  C     . ILE A 339 ? 1.1436 0.6018 0.56   0.0982  0.2909 0.0805  339 ILE A C     
2801  O  O     . ILE A 339 ? 1.1434 0.6009 0.5621 0.0939  0.2898 0.0776  339 ILE A O     
2802  C  CB    . ILE A 339 ? 1.1771 0.5992 0.5573 0.1065  0.3045 0.0817  339 ILE A CB    
2803  C  CG1   . ILE A 339 ? 1.2038 0.6048 0.5637 0.104   0.308  0.0771  339 ILE A CG1   
2804  C  CG2   . ILE A 339 ? 1.1869 0.6018 0.5625 0.1093  0.3095 0.0837  339 ILE A CG2   
2805  C  CD1   . ILE A 339 ? 1.2324 0.6163 0.5744 0.1135  0.3179 0.0821  339 ILE A CD1   
2806  N  N     . LYS A 340 ? 1.1289 0.6045 0.5589 0.1035  0.2888 0.0867  340 LYS A N     
2807  C  CA    . LYS A 340 ? 1.1174 0.6123 0.5659 0.1044  0.2852 0.0907  340 LYS A CA    
2808  C  C     . LYS A 340 ? 1.1072 0.6126 0.568  0.094   0.2765 0.0844  340 LYS A C     
2809  O  O     . LYS A 340 ? 1.1032 0.6158 0.5731 0.0921  0.2748 0.0844  340 LYS A O     
2810  C  CB    . LYS A 340 ? 1.1303 0.6418 0.5904 0.1115  0.2843 0.0987  340 LYS A CB    
2811  C  CG    . LYS A 340 ? 1.1683 0.6952 0.6427 0.1161  0.2844 0.1055  340 LYS A CG    
2812  C  CD    . LYS A 340 ? 1.2112 0.754  0.6957 0.1236  0.2842 0.1141  340 LYS A CD    
2813  C  CE    . LYS A 340 ? 1.2451 0.8004 0.741  0.1298  0.2864 0.122   340 LYS A CE    
2814  N  NZ    . LYS A 340 ? 1.2802 0.8201 0.7624 0.1382  0.2965 0.1259  340 LYS A NZ    
2815  N  N     . GLU A 341 ? 1.1014 0.6069 0.5619 0.0875  0.2713 0.079   341 GLU A N     
2816  C  CA    . GLU A 341 ? 1.0966 0.6105 0.5671 0.0779  0.2635 0.0728  341 GLU A CA    
2817  C  C     . GLU A 341 ? 1.098  0.5998 0.5606 0.0722  0.2647 0.0669  341 GLU A C     
2818  O  O     . GLU A 341 ? 1.0942 0.6043 0.5668 0.0673  0.2606 0.0646  341 GLU A O     
2819  C  CB    . GLU A 341 ? 1.1313 0.646  0.601  0.0731  0.2588 0.0687  341 GLU A CB    
2820  C  CG    . GLU A 341 ? 1.1933 0.7231 0.6736 0.0769  0.2555 0.0738  341 GLU A CG    
2821  C  CD    . GLU A 341 ? 1.2673 0.8175 0.7667 0.0754  0.2495 0.0766  341 GLU A CD    
2822  O  OE1   . GLU A 341 ? 1.2799 0.8375 0.7874 0.0677  0.2426 0.072   341 GLU A OE1   
2823  O  OE2   . GLU A 341 ? 1.2896 0.8482 0.7956 0.082   0.252  0.0836  341 GLU A OE2   
2824  N  N     . LEU A 342 ? 1.1031 0.5852 0.5476 0.0729  0.2705 0.0646  342 LEU A N     
2825  C  CA    . LEU A 342 ? 1.1108 0.5798 0.5457 0.0676  0.2722 0.0593  342 LEU A CA    
2826  C  C     . LEU A 342 ? 1.1063 0.5758 0.5436 0.071   0.2754 0.0625  342 LEU A C     
2827  O  O     . LEU A 342 ? 1.1094 0.5763 0.5466 0.0655  0.2739 0.0583  342 LEU A O     
2828  C  CB    . LEU A 342 ? 1.1295 0.5766 0.5431 0.0683  0.2782 0.0572  342 LEU A CB    
2829  C  CG    . LEU A 342 ? 1.1539 0.5964 0.562  0.0631  0.2755 0.0524  342 LEU A CG    
2830  C  CD1   . LEU A 342 ? 1.1758 0.5966 0.5627 0.0651  0.2824 0.0516  342 LEU A CD1   
2831  C  CD2   . LEU A 342 ? 1.1603 0.6061 0.5733 0.0527  0.2692 0.0453  342 LEU A CD2   
2832  N  N     . LYS A 343 ? 1.0961 0.569  0.5352 0.0804  0.2801 0.0701  343 LYS A N     
2833  C  CA    . LYS A 343 ? 1.0927 0.5653 0.5333 0.0847  0.284  0.0738  343 LYS A CA    
2834  C  C     . LYS A 343 ? 1.0728 0.5666 0.5342 0.0845  0.2791 0.0768  343 LYS A C     
2835  O  O     . LYS A 343 ? 1.0724 0.5703 0.5379 0.091   0.2828 0.0828  343 LYS A O     
2836  C  CB    . LYS A 343 ? 1.1199 0.5828 0.5497 0.0954  0.2928 0.0808  343 LYS A CB    
2837  C  CG    . LYS A 343 ? 1.1842 0.6226 0.5909 0.0958  0.2991 0.0779  343 LYS A CG    
2838  C  CD    . LYS A 343 ? 1.2448 0.6735 0.6407 0.1069  0.3082 0.0852  343 LYS A CD    
2839  C  CE    . LYS A 343 ? 1.3073 0.7106 0.6791 0.1075  0.3148 0.0827  343 LYS A CE    
2840  N  NZ    . LYS A 343 ? 1.3445 0.736  0.7045 0.1179  0.3244 0.0893  343 LYS A NZ    
2841  N  N     . GLU A 344 ? 1.0547 0.5612 0.5285 0.0769  0.271  0.0726  344 GLU A N     
2842  C  CA    . GLU A 344 ? 1.0386 0.564  0.5311 0.0755  0.266  0.0747  344 GLU A CA    
2843  C  C     . GLU A 344 ? 1.0269 0.5486 0.5192 0.0744  0.268  0.0736  344 GLU A C     
2844  O  O     . GLU A 344 ? 1.0369 0.5449 0.518  0.0699  0.2692 0.068   344 GLU A O     
2845  C  CB    . GLU A 344 ? 1.0652 0.6018 0.5682 0.0671  0.2573 0.0697  344 GLU A CB    
2846  C  CG    . GLU A 344 ? 1.1237 0.6799 0.6457 0.0656  0.2519 0.072   344 GLU A CG    
2847  C  CD    . GLU A 344 ? 1.2183 0.7864 0.7504 0.0593  0.2439 0.0691  344 GLU A CD    
2848  O  OE1   . GLU A 344 ? 1.2323 0.7983 0.76   0.0595  0.243  0.0686  344 GLU A OE1   
2849  O  OE2   . GLU A 344 ? 1.253  0.8321 0.797  0.0544  0.2387 0.0674  344 GLU A OE2   
2850  N  N     . ASP A 345 ? 1.0041 0.5374 0.5079 0.0787  0.2686 0.0792  345 ASP A N     
2851  C  CA    . ASP A 345 ? 0.9957 0.5256 0.4994 0.0785  0.2709 0.0787  345 ASP A CA    
2852  C  C     . ASP A 345 ? 0.9714 0.5082 0.484  0.0695  0.2643 0.0727  345 ASP A C     
2853  O  O     . ASP A 345 ? 0.9629 0.5143 0.4902 0.0689  0.2611 0.0748  345 ASP A O     
2854  C  CB    . ASP A 345 ? 1.0156 0.5548 0.5279 0.0868  0.2745 0.0872  345 ASP A CB    
2855  C  CG    . ASP A 345 ? 1.0786 0.6097 0.5863 0.0885  0.2791 0.0875  345 ASP A CG    
2856  O  OD1   . ASP A 345 ? 1.102  0.6142 0.593  0.0879  0.2834 0.0839  345 ASP A OD1   
2857  O  OD2   . ASP A 345 ? 1.0945 0.638  0.6151 0.0904  0.2784 0.0913  345 ASP A OD2   
2858  N  N     . ALA A 346 ? 0.959  0.4849 0.4621 0.0627  0.2627 0.0654  346 ALA A N     
2859  C  CA    . ALA A 346 ? 0.944  0.4744 0.4533 0.0542  0.257  0.0593  346 ALA A CA    
2860  C  C     . ALA A 346 ? 0.9392 0.4527 0.4333 0.0491  0.2584 0.0528  346 ALA A C     
2861  O  O     . ALA A 346 ? 0.9482 0.4482 0.4282 0.0506  0.2622 0.0522  346 ALA A O     
2862  C  CB    . ALA A 346 ? 0.9371 0.4815 0.4585 0.0492  0.2496 0.0573  346 ALA A CB    
2863  N  N     . ASP A 347 ? 0.9236 0.4377 0.4201 0.0429  0.2555 0.0481  347 ASP A N     
2864  C  CA    . ASP A 347 ? 0.9238 0.4236 0.4069 0.0371  0.256  0.042   347 ASP A CA    
2865  C  C     . ASP A 347 ? 0.9104 0.4093 0.3908 0.032   0.2524 0.0378  347 ASP A C     
2866  O  O     . ASP A 347 ? 0.9004 0.4124 0.3925 0.0302  0.2473 0.0377  347 ASP A O     
2867  C  CB    . ASP A 347 ? 0.942  0.4453 0.4303 0.0316  0.253  0.0381  347 ASP A CB    
2868  C  CG    . ASP A 347 ? 0.9944 0.4961 0.4832 0.0359  0.2569 0.0413  347 ASP A CG    
2869  O  OD1   . ASP A 347 ? 1.0091 0.5023 0.4899 0.0428  0.263  0.0458  347 ASP A OD1   
2870  O  OD2   . ASP A 347 ? 1.0179 0.5264 0.5148 0.0326  0.254  0.0395  347 ASP A OD2   
2871  N  N     . LEU A 348 ? 0.91   0.3931 0.3745 0.0298  0.2552 0.0346  348 LEU A N     
2872  C  CA    . LEU A 348 ? 0.9063 0.3868 0.3666 0.0253  0.2525 0.0309  348 LEU A CA    
2873  C  C     . LEU A 348 ? 0.9012 0.3745 0.3546 0.0171  0.2505 0.0244  348 LEU A C     
2874  O  O     . LEU A 348 ? 0.9152 0.3752 0.3563 0.0164  0.2543 0.0232  348 LEU A O     
2875  C  CB    . LEU A 348 ? 0.9175 0.385  0.364  0.0304  0.2581 0.0333  348 LEU A CB    
2876  C  CG    . LEU A 348 ? 0.9388 0.4024 0.3797 0.0267  0.2562 0.0301  348 LEU A CG    
2877  C  CD1   . LEU A 348 ? 0.9364 0.416  0.3916 0.0273  0.2513 0.0316  348 LEU A CD1   
2878  C  CD2   . LEU A 348 ? 0.9574 0.4044 0.3814 0.0312  0.2627 0.0319  348 LEU A CD2   
2879  N  N     . ILE A 349 ? 0.8801 0.3618 0.3409 0.0108  0.2447 0.0205  349 ILE A N     
2880  C  CA    . ILE A 349 ? 0.8762 0.3523 0.331  0.003   0.2426 0.0148  349 ILE A CA    
2881  C  C     . ILE A 349 ? 0.8743 0.3398 0.3172 0.0009  0.2439 0.0127  349 ILE A C     
2882  O  O     . ILE A 349 ? 0.8769 0.3476 0.3239 0.002   0.2421 0.0134  349 ILE A O     
2883  C  CB    . ILE A 349 ? 0.8738 0.3643 0.3426 -0.0025 0.2361 0.0119  349 ILE A CB    
2884  C  CG1   . ILE A 349 ? 0.8832 0.3821 0.362  -0.0008 0.2355 0.0137  349 ILE A CG1   
2885  C  CG2   . ILE A 349 ? 0.8814 0.3669 0.3441 -0.0104 0.234  0.0063  349 ILE A CG2   
2886  C  CD1   . ILE A 349 ? 0.8907 0.4033 0.383  -0.0052 0.2297 0.0114  349 ILE A CD1   
2887  N  N     . VAL A 350 ? 0.8686 0.3185 0.296  -0.0018 0.2473 0.0103  350 VAL A N     
2888  C  CA    . VAL A 350 ? 0.8674 0.3061 0.2823 -0.0043 0.2488 0.0082  350 VAL A CA    
2889  C  C     . VAL A 350 ? 0.8555 0.2951 0.2699 -0.0134 0.2447 0.0028  350 VAL A C     
2890  O  O     . VAL A 350 ? 0.8607 0.2975 0.2724 -0.0175 0.2442 0.0005  350 VAL A O     
2891  C  CB    . VAL A 350 ? 0.8868 0.3063 0.2832 -0.0013 0.2556 0.0095  350 VAL A CB    
2892  C  CG1   . VAL A 350 ? 0.9026 0.3096 0.2852 -0.0051 0.257  0.0067  350 VAL A CG1   
2893  C  CG2   . VAL A 350 ? 0.8911 0.31   0.2878 0.0085  0.2601 0.0155  350 VAL A CG2   
2894  N  N     . CYS A 351 ? 0.8365 0.2803 0.2538 -0.0163 0.2416 0.0009  351 CYS A N     
2895  C  CA    . CYS A 351 ? 0.8268 0.2721 0.244  -0.0246 0.2379 -0.0038 351 CYS A CA    
2896  C  C     . CYS A 351 ? 0.8203 0.2526 0.2234 -0.0271 0.2403 -0.0056 351 CYS A C     
2897  O  O     . CYS A 351 ? 0.8206 0.2516 0.2224 -0.0234 0.2415 -0.0039 351 CYS A O     
2898  C  CB    . CYS A 351 ? 0.8257 0.2874 0.2586 -0.0263 0.2322 -0.0047 351 CYS A CB    
2899  S  SG    . CYS A 351 ? 0.8675 0.334  0.3031 -0.0358 0.2275 -0.0098 351 CYS A SG    
2900  N  N     . MET A 352 ? 0.8129 0.2352 0.2049 -0.0334 0.2411 -0.0087 352 MET A N     
2901  C  CA    . MET A 352 ? 0.8141 0.2234 0.192  -0.0365 0.2434 -0.0105 352 MET A CA    
2902  C  C     . MET A 352 ? 0.8048 0.2196 0.186  -0.0448 0.239  -0.0144 352 MET A C     
2903  O  O     . MET A 352 ? 0.805  0.2235 0.1887 -0.05   0.2366 -0.0165 352 MET A O     
2904  C  CB    . MET A 352 ? 0.8301 0.2213 0.1902 -0.0372 0.2485 -0.0106 352 MET A CB    
2905  C  CG    . MET A 352 ? 0.855  0.2391 0.2102 -0.0284 0.2538 -0.0063 352 MET A CG    
2906  S  SD    . MET A 352 ? 0.9003 0.2611 0.2328 -0.0282 0.2605 -0.006  352 MET A SD    
2907  C  CE    . MET A 352 ? 0.8859 0.2327 0.2027 -0.0348 0.2617 -0.0093 352 MET A CE    
2908  N  N     . LEU A 353 ? 0.793  0.2095 0.1751 -0.0456 0.2379 -0.0152 353 LEU A N     
2909  C  CA    . LEU A 353 ? 0.7855 0.2079 0.1713 -0.0528 0.2339 -0.0184 353 LEU A CA    
2910  C  C     . LEU A 353 ? 0.7911 0.2034 0.1659 -0.0551 0.2359 -0.0196 353 LEU A C     
2911  O  O     . LEU A 353 ? 0.7956 0.2031 0.1668 -0.0496 0.2385 -0.0177 353 LEU A O     
2912  C  CB    . LEU A 353 ? 0.773  0.2125 0.1759 -0.0513 0.2292 -0.0181 353 LEU A CB    
2913  C  CG    . LEU A 353 ? 0.7768 0.2284 0.1926 -0.0497 0.2265 -0.0171 353 LEU A CG    
2914  C  CD1   . LEU A 353 ? 0.7728 0.2381 0.2027 -0.0468 0.2229 -0.0161 353 LEU A CD1   
2915  C  CD2   . LEU A 353 ? 0.7816 0.2365 0.1987 -0.0565 0.2242 -0.0198 353 LEU A CD2   
2916  N  N     . LYS A 354 ? 0.7892 0.1991 0.1593 -0.063  0.2345 -0.0227 354 LYS A N     
2917  C  CA    . LYS A 354 ? 0.799  0.2    0.1593 -0.0657 0.2361 -0.0239 354 LYS A CA    
2918  C  C     . LYS A 354 ? 0.8006 0.2117 0.1713 -0.0632 0.2336 -0.0235 354 LYS A C     
2919  O  O     . LYS A 354 ? 0.806  0.2106 0.1709 -0.0599 0.2359 -0.0226 354 LYS A O     
2920  C  CB    . LYS A 354 ? 0.8188 0.2164 0.1728 -0.0752 0.235  -0.027  354 LYS A CB    
2921  C  CG    . LYS A 354 ? 0.8651 0.2517 0.2072 -0.0783 0.2372 -0.0281 354 LYS A CG    
2922  C  CD    . LYS A 354 ? 0.9139 0.2948 0.2473 -0.0879 0.2368 -0.0307 354 LYS A CD    
2923  C  CE    . LYS A 354 ? 0.9622 0.33   0.282  -0.0911 0.2397 -0.0317 354 LYS A CE    
2924  N  NZ    . LYS A 354 ? 0.9833 0.3601 0.3105 -0.0945 0.2368 -0.0329 354 LYS A NZ    
2925  N  N     . GLY A 355 ? 0.7944 0.221  0.1798 -0.0643 0.2289 -0.024  355 GLY A N     
2926  C  CA    . GLY A 355 ? 0.7941 0.2308 0.1899 -0.062  0.226  -0.0236 355 GLY A CA    
2927  C  C     . GLY A 355 ? 0.8014 0.2379 0.1952 -0.067  0.2249 -0.0257 355 GLY A C     
2928  O  O     . GLY A 355 ? 0.7965 0.2444 0.2009 -0.0681 0.2212 -0.0263 355 GLY A O     
2929  N  N     . PHE A 356 ? 0.8105 0.2336 0.1903 -0.0699 0.2282 -0.0267 356 PHE A N     
2930  C  CA    . PHE A 356 ? 0.8156 0.2377 0.1929 -0.0741 0.2276 -0.0283 356 PHE A CA    
2931  C  C     . PHE A 356 ? 0.8325 0.2458 0.1988 -0.0821 0.2289 -0.0304 356 PHE A C     
2932  O  O     . PHE A 356 ? 0.844  0.245  0.1982 -0.0831 0.2322 -0.0305 356 PHE A O     
2933  C  CB    . PHE A 356 ? 0.8123 0.2275 0.1843 -0.0688 0.2301 -0.0271 356 PHE A CB    
2934  C  CG    . PHE A 356 ? 0.8057 0.2301 0.1886 -0.0613 0.2284 -0.0248 356 PHE A CG    
2935  C  CD1   . PHE A 356 ? 0.8066 0.2422 0.2003 -0.0609 0.2246 -0.025  356 PHE A CD1   
2936  C  CD2   . PHE A 356 ? 0.811  0.2337 0.1937 -0.0552 0.2303 -0.0223 356 PHE A CD2   
2937  C  CE1   . PHE A 356 ? 0.8052 0.2495 0.2087 -0.0549 0.2226 -0.0229 356 PHE A CE1   
2938  C  CE2   . PHE A 356 ? 0.8098 0.2424 0.2035 -0.0491 0.2282 -0.02   356 PHE A CE2   
2939  C  CZ    . PHE A 356 ? 0.799  0.2422 0.2028 -0.0493 0.2243 -0.0204 356 PHE A CZ    
2940  N  N     . LYS A 357 ? 0.8315 0.2511 0.2017 -0.0878 0.2265 -0.032  357 LYS A N     
2941  C  CA    . LYS A 357 ? 0.8454 0.259  0.2068 -0.0962 0.2271 -0.0338 357 LYS A CA    
2942  C  C     . LYS A 357 ? 0.8652 0.2637 0.2122 -0.0968 0.2311 -0.0342 357 LYS A C     
2943  O  O     . LYS A 357 ? 0.8727 0.2673 0.2182 -0.0904 0.2329 -0.033  357 LYS A O     
2944  C  CB    . LYS A 357 ? 0.8532 0.2806 0.2255 -0.1011 0.223  -0.0347 357 LYS A CB    
2945  C  CG    . LYS A 357 ? 0.8845 0.3225 0.2654 -0.1037 0.22   -0.0348 357 LYS A CG    
2946  C  CD    . LYS A 357 ? 0.9215 0.3748 0.3156 -0.1058 0.2162 -0.0349 357 LYS A CD    
2947  C  CE    . LYS A 357 ? 0.9587 0.421  0.3643 -0.0987 0.2144 -0.0338 357 LYS A CE    
2948  N  NZ    . LYS A 357 ? 0.9713 0.4469 0.3884 -0.1001 0.2112 -0.0339 357 LYS A NZ    
2949  N  N     . PRO A 358 ? 0.8712 0.2609 0.207  -0.1044 0.2325 -0.0357 358 PRO A N     
2950  C  CA    . PRO A 358 ? 0.8789 0.2532 0.2001 -0.1049 0.2366 -0.036  358 PRO A CA    
2951  C  C     . PRO A 358 ? 0.88   0.2564 0.2046 -0.1011 0.2368 -0.0356 358 PRO A C     
2952  O  O     . PRO A 358 ? 0.8911 0.2559 0.2061 -0.0969 0.2405 -0.035  358 PRO A O     
2953  C  CB    . PRO A 358 ? 0.8924 0.2617 0.2051 -0.1152 0.2366 -0.0378 358 PRO A CB    
2954  C  CG    . PRO A 358 ? 0.8965 0.2726 0.214  -0.1187 0.234  -0.038  358 PRO A CG    
2955  C  CD    . PRO A 358 ? 0.8656 0.2582 0.2007 -0.113  0.2305 -0.0369 358 PRO A CD    
2956  N  N     . ARG A 359 ? 0.8695 0.2604 0.2074 -0.102  0.233  -0.0358 359 ARG A N     
2957  C  CA    . ARG A 359 ? 0.8704 0.2634 0.2116 -0.0984 0.233  -0.0355 359 ARG A CA    
2958  C  C     . ARG A 359 ? 0.8625 0.2611 0.212  -0.0891 0.2321 -0.0337 359 ARG A C     
2959  O  O     . ARG A 359 ? 0.8615 0.2628 0.2145 -0.0858 0.2316 -0.0333 359 ARG A O     
2960  C  CB    . ARG A 359 ? 0.8806 0.2853 0.231  -0.1034 0.2297 -0.0362 359 ARG A CB    
2961  C  CG    . ARG A 359 ? 0.9237 0.3243 0.2667 -0.1128 0.2303 -0.0375 359 ARG A CG    
2962  C  CD    . ARG A 359 ? 0.9564 0.3721 0.3112 -0.1179 0.2263 -0.0376 359 ARG A CD    
2963  N  NE    . ARG A 359 ? 0.9887 0.4137 0.3519 -0.1179 0.2246 -0.0374 359 ARG A NE    
2964  C  CZ    . ARG A 359 ? 1.0144 0.4512 0.3859 -0.1229 0.2219 -0.0372 359 ARG A CZ    
2965  N  NH1   . ARG A 359 ? 1.0066 0.4478 0.3793 -0.1286 0.2204 -0.0374 359 ARG A NH1   
2966  N  NH2   . ARG A 359 ? 1.016  0.4599 0.3942 -0.1222 0.2209 -0.0368 359 ARG A NH2   
2967  N  N     . GLY A 360 ? 0.8546 0.255  0.2071 -0.0853 0.2319 -0.0326 360 GLY A N     
2968  C  CA    . GLY A 360 ? 0.8515 0.258  0.2122 -0.077  0.2309 -0.0307 360 GLY A CA    
2969  C  C     . GLY A 360 ? 0.8404 0.2637 0.2175 -0.0764 0.226  -0.0305 360 GLY A C     
2970  O  O     . GLY A 360 ? 0.8404 0.2699 0.2252 -0.0703 0.2246 -0.0289 360 GLY A O     
2971  N  N     . ASP A 361 ? 0.8268 0.2577 0.2092 -0.0828 0.2235 -0.0319 361 ASP A N     
2972  C  CA    . ASP A 361 ? 0.8117 0.2579 0.2088 -0.0824 0.2192 -0.0317 361 ASP A CA    
2973  C  C     . ASP A 361 ? 0.8115 0.2619 0.2134 -0.0807 0.2183 -0.031  361 ASP A C     
2974  O  O     . ASP A 361 ? 0.8162 0.2607 0.2114 -0.0838 0.2199 -0.0315 361 ASP A O     
2975  C  CB    . ASP A 361 ? 0.8155 0.2686 0.2166 -0.0891 0.2171 -0.0331 361 ASP A CB    
2976  C  CG    . ASP A 361 ? 0.8513 0.2994 0.2446 -0.0967 0.2183 -0.0343 361 ASP A CG    
2977  O  OD1   . ASP A 361 ? 0.8635 0.2985 0.244  -0.0982 0.2217 -0.0347 361 ASP A OD1   
2978  O  OD2   . ASP A 361 ? 0.8645 0.3218 0.2642 -0.1013 0.2159 -0.0347 361 ASP A OD2   
2979  N  N     . ASP A 362 ? 0.8045 0.2643 0.2171 -0.0757 0.2158 -0.0297 362 ASP A N     
2980  C  CA    . ASP A 362 ? 0.8052 0.2692 0.223  -0.0733 0.2151 -0.0287 362 ASP A CA    
2981  C  C     . ASP A 362 ? 0.7975 0.2679 0.2196 -0.0785 0.2132 -0.0298 362 ASP A C     
2982  O  O     . ASP A 362 ? 0.7969 0.2745 0.224  -0.0827 0.211  -0.0309 362 ASP A O     
2983  C  CB    . ASP A 362 ? 0.8233 0.2963 0.2518 -0.0673 0.2127 -0.0271 362 ASP A CB    
2984  C  CG    . ASP A 362 ? 0.8739 0.358  0.3125 -0.0687 0.2089 -0.0277 362 ASP A CG    
2985  O  OD1   . ASP A 362 ? 0.8796 0.3623 0.3165 -0.0689 0.2088 -0.0282 362 ASP A OD1   
2986  O  OD2   . ASP A 362 ? 0.8984 0.3919 0.3461 -0.0694 0.2063 -0.0278 362 ASP A OD2   
2987  N  N     . ASN A 363 ? 0.7895 0.2573 0.2095 -0.0779 0.2143 -0.0293 363 ASN A N     
2988  C  CA    . ASN A 363 ? 0.789  0.2621 0.2124 -0.0822 0.2128 -0.0301 363 ASN A CA    
2989  C  C     . ASN A 363 ? 0.7775 0.2642 0.215  -0.0797 0.2094 -0.0294 363 ASN A C     
2990  O  O     . ASN A 363 ? 0.7815 0.27   0.2232 -0.0742 0.2093 -0.0279 363 ASN A O     
2991  C  CB    . ASN A 363 ? 0.813  0.2775 0.2288 -0.0814 0.2154 -0.0296 363 ASN A CB    
2992  C  CG    . ASN A 363 ? 0.8682 0.3172 0.2682 -0.0837 0.2193 -0.0302 363 ASN A CG    
2993  O  OD1   . ASN A 363 ? 0.8963 0.3406 0.2903 -0.0872 0.22   -0.0312 363 ASN A OD1   
2994  N  ND2   . ASN A 363 ? 0.8788 0.3188 0.271  -0.0819 0.2221 -0.0294 363 ASN A ND2   
2995  N  N     . ARG A 364 ? 0.7598 0.256  0.2044 -0.0836 0.2066 -0.0304 364 ARG A N     
2996  C  CA    . ARG A 364 ? 0.7427 0.2512 0.1999 -0.0815 0.2035 -0.0298 364 ARG A CA    
2997  C  C     . ARG A 364 ? 0.732  0.243  0.1927 -0.0797 0.2033 -0.0291 364 ARG A C     
2998  O  O     . ARG A 364 ? 0.7288 0.2452 0.1971 -0.075  0.2021 -0.0279 364 ARG A O     
2999  C  CB    . ARG A 364 ? 0.7494 0.2669 0.2123 -0.086  0.2012 -0.0307 364 ARG A CB    
3000  C  CG    . ARG A 364 ? 0.7721 0.2997 0.246  -0.0829 0.1985 -0.0301 364 ARG A CG    
3001  C  CD    . ARG A 364 ? 0.8076 0.3328 0.2807 -0.0799 0.1985 -0.0298 364 ARG A CD    
3002  N  NE    . ARG A 364 ? 0.8402 0.3619 0.3077 -0.0837 0.1995 -0.0307 364 ARG A NE    
3003  C  CZ    . ARG A 364 ? 0.8702 0.3818 0.3282 -0.084  0.202  -0.031  364 ARG A CZ    
3004  N  NH1   . ARG A 364 ? 0.8707 0.3745 0.3235 -0.0804 0.2038 -0.0303 364 ARG A NH1   
3005  N  NH2   . ARG A 364 ? 0.871  0.3801 0.3245 -0.0878 0.2028 -0.0317 364 ARG A NH2   
3006  N  N     . PRO A 365 ? 0.7238 0.2305 0.1787 -0.0831 0.2046 -0.0297 365 PRO A N     
3007  C  CA    . PRO A 365 ? 0.7193 0.228  0.1774 -0.0809 0.2045 -0.0289 365 PRO A CA    
3008  C  C     . PRO A 365 ? 0.7245 0.2282 0.1813 -0.0745 0.2065 -0.0271 365 PRO A C     
3009  O  O     . PRO A 365 ? 0.7243 0.2337 0.1884 -0.0711 0.2056 -0.026  365 PRO A O     
3010  C  CB    . PRO A 365 ? 0.7297 0.2319 0.1789 -0.0861 0.2059 -0.0299 365 PRO A CB    
3011  C  CG    . PRO A 365 ? 0.7364 0.2389 0.1824 -0.0921 0.2053 -0.0312 365 PRO A CG    
3012  C  CD    . PRO A 365 ? 0.7198 0.2199 0.1651 -0.0894 0.2058 -0.031  365 PRO A CD    
3013  N  N     . ASP A 366 ? 0.7296 0.2231 0.1774 -0.0726 0.2092 -0.0267 366 ASP A N     
3014  C  CA    . ASP A 366 ? 0.7349 0.2238 0.1811 -0.0661 0.2114 -0.0245 366 ASP A CA    
3015  C  C     . ASP A 366 ? 0.7262 0.2247 0.1838 -0.0611 0.2091 -0.0228 366 ASP A C     
3016  O  O     . ASP A 366 ? 0.7229 0.2218 0.1829 -0.056  0.2101 -0.0206 366 ASP A O     
3017  C  CB    . ASP A 366 ? 0.7641 0.24   0.1978 -0.0651 0.215  -0.0242 366 ASP A CB    
3018  C  CG    . ASP A 366 ? 0.8366 0.3004 0.257  -0.0694 0.2179 -0.0254 366 ASP A CG    
3019  O  OD1   . ASP A 366 ? 0.8463 0.3124 0.2673 -0.074  0.2168 -0.0266 366 ASP A OD1   
3020  O  OD2   . ASP A 366 ? 0.8756 0.3275 0.2847 -0.0684 0.2213 -0.0251 366 ASP A OD2   
3021  N  N     . ARG A 367 ? 0.7183 0.2248 0.1829 -0.0627 0.2061 -0.0237 367 ARG A N     
3022  C  CA    . ARG A 367 ? 0.7142 0.2296 0.189  -0.0588 0.2034 -0.0224 367 ARG A CA    
3023  C  C     . ARG A 367 ? 0.7065 0.23   0.1904 -0.0572 0.2019 -0.0214 367 ARG A C     
3024  O  O     . ARG A 367 ? 0.7103 0.2395 0.2015 -0.0532 0.2004 -0.0196 367 ARG A O     
3025  C  CB    . ARG A 367 ? 0.7296 0.2509 0.2089 -0.0614 0.2007 -0.0238 367 ARG A CB    
3026  C  CG    . ARG A 367 ? 0.7709 0.285  0.2421 -0.063  0.2021 -0.0247 367 ARG A CG    
3027  C  CD    . ARG A 367 ? 0.8013 0.3218 0.2774 -0.0656 0.1994 -0.0259 367 ARG A CD    
3028  N  NE    . ARG A 367 ? 0.8345 0.3492 0.3044 -0.066  0.2004 -0.0264 367 ARG A NE    
3029  C  CZ    . ARG A 367 ? 0.8684 0.3869 0.342  -0.0652 0.1985 -0.0265 367 ARG A CZ    
3030  N  NH1   . ARG A 367 ? 0.8694 0.3969 0.3523 -0.064  0.1955 -0.0262 367 ARG A NH1   
3031  N  NH2   . ARG A 367 ? 0.8743 0.3868 0.3417 -0.0655 0.1997 -0.027  367 ARG A NH2   
3032  N  N     . GLY A 368 ? 0.6921 0.2161 0.1755 -0.0603 0.2022 -0.0224 368 GLY A N     
3033  C  CA    . GLY A 368 ? 0.6808 0.2118 0.1721 -0.0589 0.201  -0.0216 368 GLY A CA    
3034  C  C     . GLY A 368 ? 0.6783 0.2034 0.1654 -0.0561 0.2039 -0.0201 368 GLY A C     
3035  O  O     . GLY A 368 ? 0.6816 0.212  0.175  -0.0546 0.2032 -0.0192 368 GLY A O     
3036  N  N     . ALA A 369 ? 0.6692 0.1829 0.1452 -0.0552 0.2074 -0.0196 369 ALA A N     
3037  C  CA    . ALA A 369 ? 0.6636 0.1704 0.1342 -0.0522 0.2107 -0.018  369 ALA A CA    
3038  C  C     . ALA A 369 ? 0.6505 0.1615 0.1278 -0.0456 0.2111 -0.0147 369 ALA A C     
3039  O  O     . ALA A 369 ? 0.6481 0.1617 0.1291 -0.0438 0.2115 -0.0136 369 ALA A O     
3040  C  CB    . ALA A 369 ? 0.6732 0.1656 0.1291 -0.0529 0.2146 -0.0183 369 ALA A CB    
3041  N  N     . LEU A 370 ? 0.6411 0.1536 0.1205 -0.0422 0.2107 -0.0132 370 LEU A N     
3042  C  CA    . LEU A 370 ? 0.6386 0.157  0.1256 -0.0363 0.2105 -0.0097 370 LEU A CA    
3043  C  C     . LEU A 370 ? 0.6351 0.1664 0.1354 -0.037  0.2066 -0.0097 370 LEU A C     
3044  O  O     . LEU A 370 ? 0.6341 0.1689 0.1392 -0.0342 0.2072 -0.0077 370 LEU A O     
3045  C  CB    . LEU A 370 ? 0.6391 0.1566 0.1252 -0.0326 0.2108 -0.0078 370 LEU A CB    
3046  C  CG    . LEU A 370 ? 0.6658 0.1703 0.1388 -0.0305 0.2153 -0.007  370 LEU A CG    
3047  C  CD1   . LEU A 370 ? 0.6716 0.177  0.1453 -0.0262 0.2154 -0.0046 370 LEU A CD1   
3048  C  CD2   . LEU A 370 ? 0.6797 0.1773 0.1471 -0.027  0.2196 -0.0049 370 LEU A CD2   
3049  N  N     . PRO A 371 ? 0.6296 0.1673 0.135  -0.0409 0.203  -0.012  371 PRO A N     
3050  C  CA    . PRO A 371 ? 0.6235 0.172  0.1401 -0.0418 0.1997 -0.0122 371 PRO A CA    
3051  C  C     . PRO A 371 ? 0.6261 0.1751 0.1437 -0.0427 0.2007 -0.0125 371 PRO A C     
3052  O  O     . PRO A 371 ? 0.6236 0.1798 0.1496 -0.0409 0.1995 -0.0111 371 PRO A O     
3053  C  CB    . PRO A 371 ? 0.6313 0.1829 0.1492 -0.0463 0.1969 -0.015  371 PRO A CB    
3054  C  CG    . PRO A 371 ? 0.64   0.1856 0.1512 -0.0459 0.1977 -0.0151 371 PRO A CG    
3055  C  CD    . PRO A 371 ? 0.6258 0.1611 0.1272 -0.0444 0.2019 -0.0143 371 PRO A CD    
3056  N  N     . LEU A 372 ? 0.6302 0.1713 0.1388 -0.0454 0.203  -0.0142 372 LEU A N     
3057  C  CA    . LEU A 372 ? 0.6348 0.1752 0.1429 -0.0463 0.2041 -0.0145 372 LEU A CA    
3058  C  C     . LEU A 372 ? 0.6384 0.1767 0.1469 -0.0409 0.2068 -0.0113 372 LEU A C     
3059  O  O     . LEU A 372 ? 0.6334 0.1773 0.1486 -0.0396 0.2063 -0.0103 372 LEU A O     
3060  C  CB    . LEU A 372 ? 0.6441 0.1754 0.1411 -0.0507 0.2059 -0.0168 372 LEU A CB    
3061  C  CG    . LEU A 372 ? 0.666  0.194  0.1596 -0.0517 0.2076 -0.017  372 LEU A CG    
3062  C  CD1   . LEU A 372 ? 0.6706 0.2087 0.1735 -0.0538 0.2047 -0.018  372 LEU A CD1   
3063  C  CD2   . LEU A 372 ? 0.6803 0.1984 0.1617 -0.0563 0.2092 -0.019  372 LEU A CD2   
3064  N  N     . VAL A 373 ? 0.6438 0.1743 0.1453 -0.0374 0.2098 -0.0094 373 VAL A N     
3065  C  CA    . VAL A 373 ? 0.6502 0.1784 0.1515 -0.0315 0.2129 -0.0058 373 VAL A CA    
3066  C  C     . VAL A 373 ? 0.6496 0.19   0.1643 -0.0283 0.2103 -0.0032 373 VAL A C     
3067  O  O     . VAL A 373 ? 0.6472 0.1908 0.1666 -0.0256 0.2112 -0.0011 373 VAL A O     
3068  C  CB    . VAL A 373 ? 0.6634 0.1817 0.1548 -0.0283 0.2163 -0.0041 373 VAL A CB    
3069  C  CG1   . VAL A 373 ? 0.6696 0.1874 0.1623 -0.0213 0.2194 0.0004  373 VAL A CG1   
3070  C  CG2   . VAL A 373 ? 0.678  0.183  0.1552 -0.0315 0.2193 -0.0064 373 VAL A CG2   
3071  N  N     . ALA A 374 ? 0.6482 0.195  0.1686 -0.0289 0.2071 -0.0034 374 ALA A N     
3072  C  CA    . ALA A 374 ? 0.6471 0.2052 0.1794 -0.0268 0.2041 -0.0012 374 ALA A CA    
3073  C  C     . ALA A 374 ? 0.6478 0.214  0.1887 -0.0293 0.2016 -0.0024 374 ALA A C     
3074  O  O     . ALA A 374 ? 0.6426 0.2161 0.1921 -0.0269 0.2006 0.0001  374 ALA A O     
3075  C  CB    . ALA A 374 ? 0.6458 0.2072 0.1802 -0.0279 0.2011 -0.0017 374 ALA A CB    
3076  N  N     . MET A 375 ? 0.6522 0.217  0.1907 -0.034  0.2006 -0.0059 375 MET A N     
3077  C  CA    . MET A 375 ? 0.6576 0.2293 0.2031 -0.0363 0.1985 -0.0072 375 MET A CA    
3078  C  C     . MET A 375 ? 0.6679 0.2377 0.213  -0.0343 0.2012 -0.0059 375 MET A C     
3079  O  O     . MET A 375 ? 0.6662 0.2428 0.2191 -0.0339 0.2    -0.0053 375 MET A O     
3080  C  CB    . MET A 375 ? 0.6672 0.2385 0.21   -0.0416 0.1969 -0.0109 375 MET A CB    
3081  C  CG    . MET A 375 ? 0.6961 0.2713 0.2418 -0.0435 0.1938 -0.0121 375 MET A CG    
3082  S  SD    . MET A 375 ? 0.7627 0.337  0.3044 -0.0492 0.1927 -0.0158 375 MET A SD    
3083  C  CE    . MET A 375 ? 0.7572 0.3389 0.3063 -0.0506 0.1913 -0.0165 375 MET A CE    
3084  N  N     . LEU A 376 ? 0.674  0.2338 0.2093 -0.033  0.205  -0.0055 376 LEU A N     
3085  C  CA    . LEU A 376 ? 0.6798 0.2361 0.213  -0.0309 0.2079 -0.0042 376 LEU A CA    
3086  C  C     . LEU A 376 ? 0.6864 0.245  0.2241 -0.0249 0.2099 0.0002  376 LEU A C     
3087  O  O     . LEU A 376 ? 0.6828 0.2458 0.2264 -0.0232 0.2102 0.0016  376 LEU A O     
3088  C  CB    . LEU A 376 ? 0.6878 0.2313 0.2073 -0.0321 0.2113 -0.0055 376 LEU A CB    
3089  C  CG    . LEU A 376 ? 0.7046 0.246  0.2194 -0.0383 0.2099 -0.0094 376 LEU A CG    
3090  C  CD1   . LEU A 376 ? 0.7202 0.2485 0.2208 -0.0399 0.2129 -0.0105 376 LEU A CD1   
3091  C  CD2   . LEU A 376 ? 0.7087 0.2545 0.2279 -0.0397 0.2091 -0.0103 376 LEU A CD2   
3092  N  N     . ALA A 377 ? 0.6941 0.2499 0.2291 -0.0214 0.2113 0.0026  377 ALA A N     
3093  C  CA    . ALA A 377 ? 0.7021 0.26   0.2408 -0.0153 0.2136 0.0074  377 ALA A CA    
3094  C  C     . ALA A 377 ? 0.701  0.269  0.2495 -0.0134 0.2108 0.01    377 ALA A C     
3095  O  O     . ALA A 377 ? 0.6995 0.2696 0.2508 -0.0082 0.2127 0.0145  377 ALA A O     
3096  C  CB    . ALA A 377 ? 0.713  0.2588 0.2397 -0.0117 0.2186 0.0091  377 ALA A CB    
3097  N  N     . GLY A 378 ? 0.7005 0.2747 0.2541 -0.0174 0.2064 0.0076  378 GLY A N     
3098  C  CA    . GLY A 378 ? 0.7052 0.2886 0.2674 -0.0163 0.2032 0.0098  378 GLY A CA    
3099  C  C     . GLY A 378 ? 0.7183 0.2974 0.2748 -0.0149 0.2036 0.0105  378 GLY A C     
3100  O  O     . GLY A 378 ? 0.7281 0.2984 0.2757 -0.0119 0.2077 0.0117  378 GLY A O     
3101  N  N     . GLU A 379 ? 0.7177 0.3024 0.2784 -0.017  0.1996 0.0096  379 GLU A N     
3102  C  CA    . GLU A 379 ? 0.7286 0.3097 0.2842 -0.0158 0.1997 0.0101  379 GLU A CA    
3103  C  C     . GLU A 379 ? 0.7317 0.3134 0.2875 -0.0096 0.2022 0.0153  379 GLU A C     
3104  O  O     . GLU A 379 ? 0.7374 0.3129 0.2859 -0.0075 0.2041 0.016   379 GLU A O     
3105  C  CB    . GLU A 379 ? 0.7549 0.3423 0.3155 -0.0192 0.1947 0.0084  379 GLU A CB    
3106  C  CG    . GLU A 379 ? 0.807  0.4059 0.3792 -0.0187 0.1912 0.0111  379 GLU A CG    
3107  C  CD    . GLU A 379 ? 0.8827 0.4864 0.4583 -0.0222 0.1864 0.0093  379 GLU A CD    
3108  O  OE1   . GLU A 379 ? 0.8957 0.4961 0.468  -0.0263 0.1852 0.0052  379 GLU A OE1   
3109  O  OE2   . GLU A 379 ? 0.9092 0.5196 0.4905 -0.0209 0.1838 0.0122  379 GLU A OE2   
3110  N  N     . ASN A 380 ? 0.7245 0.3138 0.2887 -0.0067 0.2023 0.0191  380 ASN A N     
3111  C  CA    . ASN A 380 ? 0.7262 0.3182 0.2925 -0.0004 0.2047 0.0249  380 ASN A CA    
3112  C  C     . ASN A 380 ? 0.7314 0.3123 0.2874 0.0041  0.211  0.0266  380 ASN A C     
3113  O  O     . ASN A 380 ? 0.7325 0.3138 0.2879 0.0099  0.2137 0.0313  380 ASN A O     
3114  C  CB    . ASN A 380 ? 0.7352 0.3392 0.314  0.0008  0.2029 0.0284  380 ASN A CB    
3115  C  CG    . ASN A 380 ? 0.776  0.3806 0.3578 -0.0019 0.2029 0.0261  380 ASN A CG    
3116  O  OD1   . ASN A 380 ? 0.7958 0.392  0.3706 -0.0011 0.2068 0.0249  380 ASN A OD1   
3117  N  ND2   . ASN A 380 ? 0.7754 0.3897 0.3672 -0.0052 0.1985 0.0255  380 ASN A ND2   
3118  N  N     . ALA A 381 ? 0.7333 0.3045 0.2809 0.0017  0.2134 0.0229  381 ALA A N     
3119  C  CA    . ALA A 381 ? 0.7435 0.3025 0.2798 0.0054  0.2194 0.0241  381 ALA A CA    
3120  C  C     . ALA A 381 ? 0.748  0.2984 0.2742 0.0077  0.2218 0.0246  381 ALA A C     
3121  O  O     . ALA A 381 ? 0.7504 0.3011 0.2756 0.0043  0.2189 0.0219  381 ALA A O     
3122  C  CB    . ALA A 381 ? 0.7513 0.3019 0.2805 0.0012  0.2205 0.0196  381 ALA A CB    
3123  N  N     . GLN A 382 ? 0.7478 0.2903 0.2663 0.0136  0.2274 0.0283  382 GLN A N     
3124  C  CA    . GLN A 382 ? 0.7552 0.2886 0.2632 0.0163  0.2303 0.0291  382 GLN A CA    
3125  C  C     . GLN A 382 ? 0.7624 0.2812 0.2563 0.0121  0.2323 0.0241  382 GLN A C     
3126  O  O     . GLN A 382 ? 0.7698 0.2796 0.2562 0.0118  0.2357 0.0232  382 GLN A O     
3127  C  CB    . GLN A 382 ? 0.7774 0.3077 0.2821 0.0247  0.2358 0.0352  382 GLN A CB    
3128  C  CG    . GLN A 382 ? 0.8202 0.3658 0.3389 0.0288  0.2336 0.0407  382 GLN A CG    
3129  C  CD    . GLN A 382 ? 0.8987 0.4419 0.4139 0.0374  0.2389 0.0471  382 GLN A CD    
3130  O  OE1   . GLN A 382 ? 0.9296 0.4606 0.432  0.0404  0.2433 0.0475  382 GLN A OE1   
3131  N  NE2   . GLN A 382 ? 0.9097 0.4647 0.4362 0.0417  0.2388 0.0526  382 GLN A NE2   
3132  N  N     . ILE A 383 ? 0.7587 0.2753 0.2491 0.0083  0.23   0.021   383 ILE A N     
3133  C  CA    . ILE A 383 ? 0.7694 0.2734 0.2473 0.0035  0.2313 0.0162  383 ILE A CA    
3134  C  C     . ILE A 383 ? 0.7802 0.2728 0.2457 0.0059  0.2349 0.0168  383 ILE A C     
3135  O  O     . ILE A 383 ? 0.7824 0.2794 0.2509 0.0078  0.2334 0.0182  383 ILE A O     
3136  C  CB    . ILE A 383 ? 0.771  0.2816 0.2549 -0.004  0.2257 0.0114  383 ILE A CB    
3137  C  CG1   . ILE A 383 ? 0.7761 0.2967 0.2711 -0.0062 0.2227 0.0108  383 ILE A CG1   
3138  C  CG2   . ILE A 383 ? 0.7842 0.2832 0.2561 -0.0095 0.2268 0.0068  383 ILE A CG2   
3139  C  CD1   . ILE A 383 ? 0.7866 0.316  0.2897 -0.0121 0.2171 0.0072  383 ILE A CD1   
3140  N  N     . PHE A 384 ? 0.7838 0.261  0.2345 0.0058  0.2399 0.0158  384 PHE A N     
3141  C  CA    . PHE A 384 ? 0.7908 0.2542 0.2271 0.0077  0.2442 0.016   384 PHE A CA    
3142  C  C     . PHE A 384 ? 0.7901 0.2458 0.2183 -0.0003 0.2427 0.0103  384 PHE A C     
3143  O  O     . PHE A 384 ? 0.7973 0.2462 0.2195 -0.004  0.2439 0.0079  384 PHE A O     
3144  C  CB    . PHE A 384 ? 0.7969 0.2475 0.2215 0.0129  0.2509 0.0189  384 PHE A CB    
3145  C  CG    . PHE A 384 ? 0.8145 0.2492 0.2227 0.0163  0.2566 0.0201  384 PHE A CG    
3146  C  CD1   . PHE A 384 ? 0.8338 0.254  0.2275 0.0109  0.2582 0.0159  384 PHE A CD1   
3147  C  CD2   . PHE A 384 ? 0.8245 0.258  0.2311 0.025   0.2609 0.0258  384 PHE A CD2   
3148  C  CE1   . PHE A 384 ? 0.8536 0.2581 0.2313 0.0141  0.2639 0.017   384 PHE A CE1   
3149  C  CE2   . PHE A 384 ? 0.8442 0.2621 0.2348 0.0286  0.2666 0.027   384 PHE A CE2   
3150  C  CZ    . PHE A 384 ? 0.8524 0.2555 0.2284 0.023   0.2681 0.0225  384 PHE A CZ    
3151  N  N     . THR A 385 ? 0.7781 0.2355 0.2067 -0.003  0.2402 0.0082  385 THR A N     
3152  C  CA    . THR A 385 ? 0.7804 0.2325 0.203  -0.0107 0.2385 0.0032  385 THR A CA    
3153  C  C     . THR A 385 ? 0.7842 0.2201 0.1901 -0.0108 0.2429 0.0024  385 THR A C     
3154  O  O     . THR A 385 ? 0.7872 0.2221 0.1915 -0.0073 0.2438 0.004   385 THR A O     
3155  C  CB    . THR A 385 ? 0.7901 0.2548 0.2242 -0.0141 0.2326 0.0013  385 THR A CB    
3156  O  OG1   . THR A 385 ? 0.7935 0.2721 0.2421 -0.0142 0.2288 0.0019  385 THR A OG1   
3157  C  CG2   . THR A 385 ? 0.7984 0.2593 0.2277 -0.0218 0.2308 -0.0035 385 THR A CG2   
3158  N  N     . PHE A 386 ? 0.7807 0.2038 0.1741 -0.015  0.2456 -0.0001 386 PHE A N     
3159  C  CA    . PHE A 386 ? 0.7865 0.1927 0.1626 -0.016  0.25   -0.0012 386 PHE A CA    
3160  C  C     . PHE A 386 ? 0.7902 0.1946 0.1632 -0.0247 0.2472 -0.006  386 PHE A C     
3161  O  O     . PHE A 386 ? 0.7922 0.1984 0.1664 -0.0309 0.2449 -0.0088 386 PHE A O     
3162  C  CB    . PHE A 386 ? 0.7855 0.1768 0.1477 -0.0145 0.2555 -0.0002 386 PHE A CB    
3163  C  CG    . PHE A 386 ? 0.7955 0.1675 0.1381 -0.0156 0.2605 -0.0013 386 PHE A CG    
3164  C  CD1   . PHE A 386 ? 0.807  0.17   0.141  -0.0084 0.2656 0.0022  386 PHE A CD1   
3165  C  CD2   . PHE A 386 ? 0.8067 0.1693 0.1391 -0.024  0.2602 -0.0054 386 PHE A CD2   
3166  C  CE1   . PHE A 386 ? 0.826  0.1702 0.1411 -0.0094 0.2705 0.0013  386 PHE A CE1   
3167  C  CE2   . PHE A 386 ? 0.8244 0.1687 0.1382 -0.0255 0.2648 -0.0064 386 PHE A CE2   
3168  C  CZ    . PHE A 386 ? 0.8286 0.1632 0.1334 -0.0182 0.2701 -0.0031 386 PHE A CZ    
3169  N  N     . ILE A 387 ? 0.788  0.1892 0.1569 -0.025  0.2474 -0.0067 387 ILE A N     
3170  C  CA    . ILE A 387 ? 0.793  0.193  0.1593 -0.0325 0.245  -0.0107 387 ILE A CA    
3171  C  C     . ILE A 387 ? 0.8052 0.1868 0.1528 -0.0344 0.2498 -0.0118 387 ILE A C     
3172  O  O     . ILE A 387 ? 0.8128 0.1856 0.1523 -0.0284 0.2541 -0.0092 387 ILE A O     
3173  C  CB    . ILE A 387 ? 0.7955 0.2081 0.1738 -0.0316 0.2408 -0.0106 387 ILE A CB    
3174  C  CG1   . ILE A 387 ? 0.7992 0.229  0.195  -0.0297 0.2363 -0.0093 387 ILE A CG1   
3175  C  CG2   . ILE A 387 ? 0.8026 0.2149 0.1792 -0.0389 0.2384 -0.0144 387 ILE A CG2   
3176  C  CD1   . ILE A 387 ? 0.8142 0.2503 0.2161 -0.0353 0.2333 -0.0117 387 ILE A CD1   
3177  N  N     . TYR A 388 ? 0.8065 0.1822 0.147  -0.0427 0.2491 -0.0154 388 TYR A N     
3178  C  CA    . TYR A 388 ? 0.8225 0.1799 0.1443 -0.0455 0.2536 -0.0166 388 TYR A CA    
3179  C  C     . TYR A 388 ? 0.8249 0.1811 0.1437 -0.0536 0.2515 -0.0201 388 TYR A C     
3180  O  O     . TYR A 388 ? 0.8334 0.1745 0.1366 -0.0574 0.2548 -0.0215 388 TYR A O     
3181  C  CB    . TYR A 388 ? 0.8328 0.1776 0.1423 -0.0473 0.257  -0.0168 388 TYR A CB    
3182  C  CG    . TYR A 388 ? 0.8357 0.1883 0.1519 -0.0537 0.2531 -0.019  388 TYR A CG    
3183  C  CD1   . TYR A 388 ? 0.8386 0.2021 0.1666 -0.0502 0.2512 -0.0173 388 TYR A CD1   
3184  C  CD2   . TYR A 388 ? 0.8486 0.1977 0.1591 -0.0631 0.2514 -0.0224 388 TYR A CD2   
3185  C  CE1   . TYR A 388 ? 0.8447 0.2153 0.1786 -0.0558 0.2477 -0.0193 388 TYR A CE1   
3186  C  CE2   . TYR A 388 ? 0.8538 0.2108 0.1705 -0.0688 0.2477 -0.0241 388 TYR A CE2   
3187  C  CZ    . TYR A 388 ? 0.8573 0.2249 0.1858 -0.0649 0.2459 -0.0226 388 TYR A CZ    
3188  O  OH    . TYR A 388 ? 0.8696 0.2452 0.2043 -0.0703 0.2424 -0.0242 388 TYR A OH    
3189  N  N     . GLY A 389 ? 0.8179 0.1894 0.151  -0.0562 0.2463 -0.0213 389 GLY A N     
3190  C  CA    . GLY A 389 ? 0.8285 0.201  0.1607 -0.0635 0.2441 -0.0243 389 GLY A CA    
3191  C  C     . GLY A 389 ? 0.8384 0.2067 0.1667 -0.0612 0.2456 -0.024  389 GLY A C     
3192  O  O     . GLY A 389 ? 0.8414 0.2098 0.1713 -0.0535 0.2472 -0.0214 389 GLY A O     
3193  N  N     . PRO A 390 ? 0.8399 0.205  0.1635 -0.0677 0.2451 -0.0264 390 PRO A N     
3194  C  CA    . PRO A 390 ? 0.8444 0.2042 0.163  -0.0656 0.2468 -0.0262 390 PRO A CA    
3195  C  C     . PRO A 390 ? 0.8356 0.209  0.1682 -0.0612 0.2434 -0.0253 390 PRO A C     
3196  O  O     . PRO A 390 ? 0.8341 0.2211 0.1794 -0.0641 0.2388 -0.0263 390 PRO A O     
3197  C  CB    . PRO A 390 ? 0.8587 0.2122 0.1692 -0.0746 0.2469 -0.0291 390 PRO A CB    
3198  C  CG    . PRO A 390 ? 0.865  0.2183 0.1737 -0.0812 0.2458 -0.0305 390 PRO A CG    
3199  C  CD    . PRO A 390 ? 0.8352 0.2005 0.1566 -0.0773 0.2432 -0.0292 390 PRO A CD    
3200  N  N     . LEU A 391 ? 0.8302 0.1994 0.1597 -0.0544 0.2458 -0.0232 391 LEU A N     
3201  C  CA    . LEU A 391 ? 0.8227 0.2033 0.1638 -0.0501 0.2427 -0.0221 391 LEU A CA    
3202  C  C     . LEU A 391 ? 0.8268 0.2027 0.1627 -0.0514 0.2434 -0.0232 391 LEU A C     
3203  O  O     . LEU A 391 ? 0.8374 0.1987 0.1591 -0.0512 0.248  -0.0233 391 LEU A O     
3204  C  CB    . LEU A 391 ? 0.8225 0.2039 0.1655 -0.0407 0.2443 -0.0184 391 LEU A CB    
3205  C  CG    . LEU A 391 ? 0.834  0.2204 0.1827 -0.0378 0.244  -0.0165 391 LEU A CG    
3206  C  CD1   . LEU A 391 ? 0.8357 0.2234 0.1864 -0.0285 0.2458 -0.0124 391 LEU A CD1   
3207  C  CD2   . LEU A 391 ? 0.8334 0.2359 0.1978 -0.041  0.2383 -0.0176 391 LEU A CD2   
3208  N  N     . ILE A 392 ? 0.8176 0.205  0.1645 -0.0525 0.2392 -0.024  392 ILE A N     
3209  C  CA    . ILE A 392 ? 0.8223 0.2063 0.1655 -0.0529 0.2397 -0.0248 392 ILE A CA    
3210  C  C     . ILE A 392 ? 0.8258 0.2062 0.1663 -0.0443 0.2418 -0.022  392 ILE A C     
3211  O  O     . ILE A 392 ? 0.8207 0.2079 0.1683 -0.0387 0.2407 -0.0195 392 ILE A O     
3212  C  CB    . ILE A 392 ? 0.8185 0.2159 0.1742 -0.0562 0.2347 -0.0262 392 ILE A CB    
3213  C  CG1   . ILE A 392 ? 0.8237 0.2351 0.1938 -0.0517 0.2305 -0.0245 392 ILE A CG1   
3214  C  CG2   . ILE A 392 ? 0.8218 0.2215 0.1784 -0.0647 0.2333 -0.0286 392 ILE A CG2   
3215  C  CD1   . ILE A 392 ? 0.8381 0.2615 0.2195 -0.0538 0.2259 -0.0255 392 ILE A CD1   
3216  N  N     . LYS A 393 ? 0.834  0.2039 0.1641 -0.0432 0.245  -0.0222 393 LYS A N     
3217  C  CA    . LYS A 393 ? 0.8433 0.2093 0.1698 -0.035  0.2474 -0.0193 393 LYS A CA    
3218  C  C     . LYS A 393 ? 0.8388 0.2194 0.1794 -0.03   0.2428 -0.0174 393 LYS A C     
3219  O  O     . LYS A 393 ? 0.8416 0.2239 0.1838 -0.023  0.2436 -0.0142 393 LYS A O     
3220  C  CB    . LYS A 393 ? 0.8744 0.2274 0.1879 -0.0352 0.2512 -0.0201 393 LYS A CB    
3221  C  CG    . LYS A 393 ? 0.9277 0.2751 0.2355 -0.0265 0.2543 -0.017  393 LYS A CG    
3222  C  CD    . LYS A 393 ? 0.9826 0.3221 0.2829 -0.0214 0.2587 -0.0143 393 LYS A CD    
3223  C  CE    . LYS A 393 ? 1.0387 0.3591 0.3203 -0.0201 0.2654 -0.0142 393 LYS A CE    
3224  N  NZ    . LYS A 393 ? 1.072  0.3894 0.3501 -0.0141 0.267  -0.0124 393 LYS A NZ    
3225  N  N     . GLY A 394 ? 0.8288 0.22   0.1797 -0.0338 0.238  -0.0192 394 GLY A N     
3226  C  CA    . GLY A 394 ? 0.8251 0.2297 0.1888 -0.0301 0.2334 -0.0177 394 GLY A CA    
3227  C  C     . GLY A 394 ? 0.8246 0.2389 0.1981 -0.0274 0.2312 -0.0157 394 GLY A C     
3228  O  O     . GLY A 394 ? 0.8208 0.2426 0.2013 -0.0221 0.229  -0.013  394 GLY A O     
3229  N  N     . ALA A 395 ? 0.826  0.2401 0.1999 -0.0312 0.2317 -0.0167 395 ALA A N     
3230  C  CA    . ALA A 395 ? 0.8257 0.2483 0.2084 -0.0291 0.2299 -0.0149 395 ALA A CA    
3231  C  C     . ALA A 395 ? 0.8307 0.2482 0.2085 -0.022  0.2336 -0.0113 395 ALA A C     
3232  O  O     . ALA A 395 ? 0.8247 0.2516 0.2116 -0.0173 0.2315 -0.0085 395 ALA A O     
3233  C  CB    . ALA A 395 ? 0.8281 0.2511 0.2115 -0.0351 0.2297 -0.0171 395 ALA A CB    
3234  N  N     . ILE A 396 ? 0.842  0.2448 0.2053 -0.0211 0.2391 -0.0112 396 ILE A N     
3235  C  CA    . ILE A 396 ? 0.8547 0.2514 0.2121 -0.0138 0.2434 -0.0074 396 ILE A CA    
3236  C  C     . ILE A 396 ? 0.8624 0.263  0.2224 -0.0068 0.2429 -0.0043 396 ILE A C     
3237  O  O     . ILE A 396 ? 0.864  0.2687 0.2274 -0.0003 0.2437 -0.0003 396 ILE A O     
3238  C  CB    . ILE A 396 ? 0.8696 0.2483 0.2096 -0.0146 0.2498 -0.008  396 ILE A CB    
3239  C  CG1   . ILE A 396 ? 0.8825 0.2563 0.2179 -0.0076 0.2541 -0.0041 396 ILE A CG1   
3240  C  CG2   . ILE A 396 ? 0.8809 0.248  0.209  -0.0152 0.2527 -0.0092 396 ILE A CG2   
3241  C  CD1   . ILE A 396 ? 0.8872 0.2706 0.2327 -0.0073 0.2519 -0.0029 396 ILE A CD1   
3242  N  N     . ASN A 397 ? 0.8632 0.2637 0.2225 -0.0084 0.2413 -0.0059 397 ASN A N     
3243  C  CA    . ASN A 397 ? 0.8662 0.2709 0.2283 -0.0024 0.2402 -0.0032 397 ASN A CA    
3244  C  C     . ASN A 397 ? 0.8605 0.2822 0.2386 -0.0006 0.2344 -0.0013 397 ASN A C     
3245  O  O     . ASN A 397 ? 0.8586 0.2853 0.2402 0.0059  0.2342 0.0027  397 ASN A O     
3246  C  CB    . ASN A 397 ? 0.8811 0.2815 0.2386 -0.005  0.2396 -0.0057 397 ASN A CB    
3247  C  CG    . ASN A 397 ? 0.93   0.3132 0.2709 -0.005  0.2457 -0.0065 397 ASN A CG    
3248  O  OD1   . ASN A 397 ? 0.9504 0.3242 0.282  -0.0013 0.2507 -0.0045 397 ASN A OD1   
3249  N  ND2   . ASN A 397 ? 0.9434 0.3217 0.2796 -0.0093 0.2455 -0.0095 397 ASN A ND2   
3250  N  N     . LEU A 398 ? 0.8573 0.2878 0.245  -0.0063 0.23   -0.0039 398 LEU A N     
3251  C  CA    . LEU A 398 ? 0.8564 0.3023 0.2588 -0.0055 0.2246 -0.0024 398 LEU A CA    
3252  C  C     . LEU A 398 ? 0.8597 0.3099 0.2664 -0.0017 0.2256 0.0009  398 LEU A C     
3253  O  O     . LEU A 398 ? 0.8549 0.3158 0.2711 0.002   0.2227 0.004   398 LEU A O     
3254  C  CB    . LEU A 398 ? 0.8551 0.308  0.2653 -0.0124 0.2202 -0.006  398 LEU A CB    
3255  C  CG    . LEU A 398 ? 0.8745 0.3303 0.287  -0.0146 0.2168 -0.0079 398 LEU A CG    
3256  C  CD1   . LEU A 398 ? 0.8805 0.3432 0.3005 -0.0209 0.213  -0.011  398 LEU A CD1   
3257  C  CD2   . LEU A 398 ? 0.8761 0.3398 0.2948 -0.0097 0.2135 -0.0048 398 LEU A CD2   
3258  N  N     . ILE A 399 ? 0.8652 0.3069 0.2647 -0.0026 0.2299 0.0004  399 ILE A N     
3259  C  CA    . ILE A 399 ? 0.8709 0.3147 0.2728 0.0014  0.2318 0.0036  399 ILE A CA    
3260  C  C     . ILE A 399 ? 0.8763 0.3191 0.2755 0.01    0.2347 0.0087  399 ILE A C     
3261  O  O     . ILE A 399 ? 0.8735 0.3254 0.2809 0.0144  0.2336 0.0126  399 ILE A O     
3262  C  CB    . ILE A 399 ? 0.8861 0.3183 0.2781 -0.0017 0.2362 0.0017  399 ILE A CB    
3263  C  CG1   . ILE A 399 ? 0.8956 0.3333 0.2941 -0.0093 0.2325 -0.0021 399 ILE A CG1   
3264  C  CG2   . ILE A 399 ? 0.8941 0.323  0.2831 0.004   0.2404 0.0055  399 ILE A CG2   
3265  C  CD1   . ILE A 399 ? 0.9207 0.347  0.3088 -0.0141 0.2358 -0.0049 399 ILE A CD1   
3266  N  N     . ASP A 400 ? 0.882  0.3144 0.2701 0.0123  0.238  0.0089  400 ASP A N     
3267  C  CA    . ASP A 400 ? 0.8897 0.3205 0.2742 0.0207  0.2411 0.0138  400 ASP A CA    
3268  C  C     . ASP A 400 ? 0.8845 0.3279 0.2791 0.0236  0.2362 0.0161  400 ASP A C     
3269  O  O     . ASP A 400 ? 0.8871 0.3328 0.2816 0.0308  0.2378 0.021   400 ASP A O     
3270  C  CB    . ASP A 400 ? 0.9229 0.3363 0.2903 0.0224  0.2473 0.0132  400 ASP A CB    
3271  C  CG    . ASP A 400 ? 0.9847 0.3844 0.3404 0.0207  0.2528 0.0119  400 ASP A CG    
3272  O  OD1   . ASP A 400 ? 0.9928 0.3962 0.353  0.0214  0.2531 0.0133  400 ASP A OD1   
3273  O  OD2   . ASP A 400 ? 1.0206 0.4054 0.3623 0.0186  0.2568 0.0095  400 ASP A OD2   
3274  N  N     . GLN A 401 ? 0.8763 0.3277 0.279  0.0183  0.2304 0.013   401 GLN A N     
3275  C  CA    . GLN A 401 ? 0.8738 0.3363 0.2851 0.0203  0.2254 0.015   401 GLN A CA    
3276  C  C     . GLN A 401 ? 0.8622 0.3405 0.2889 0.0182  0.2194 0.0157  401 GLN A C     
3277  O  O     . GLN A 401 ? 0.8581 0.3466 0.2925 0.0226  0.2172 0.02    401 GLN A O     
3278  C  CB    . GLN A 401 ? 0.8997 0.3577 0.3065 0.0169  0.2237 0.0115  401 GLN A CB    
3279  C  CG    . GLN A 401 ? 0.944  0.4133 0.3596 0.0178  0.2178 0.0128  401 GLN A CG    
3280  C  CD    . GLN A 401 ? 1.0043 0.4717 0.4189 0.0124  0.2148 0.0084  401 GLN A CD    
3281  O  OE1   . GLN A 401 ? 1.0355 0.4919 0.4409 0.0093  0.2179 0.005   401 GLN A OE1   
3282  N  NE2   . GLN A 401 ? 0.9974 0.4753 0.4212 0.0111  0.2088 0.0085  401 GLN A NE2   
3283  N  N     . ASP A 402 ? 0.8544 0.3348 0.2854 0.0114  0.2167 0.0115  402 ASP A N     
3284  C  CA    . ASP A 402 ? 0.8443 0.3382 0.2888 0.0087  0.2112 0.0116  402 ASP A CA    
3285  C  C     . ASP A 402 ? 0.8341 0.3262 0.2795 0.0027  0.2113 0.0076  402 ASP A C     
3286  O  O     . ASP A 402 ? 0.8335 0.3225 0.2768 -0.0026 0.2099 0.0035  402 ASP A O     
3287  C  CB    . ASP A 402 ? 0.8696 0.3701 0.3194 0.0065  0.2055 0.0104  402 ASP A CB    
3288  C  CG    . ASP A 402 ? 0.9281 0.4428 0.3913 0.0049  0.1996 0.0115  402 ASP A CG    
3289  O  OD1   . ASP A 402 ? 0.9367 0.4566 0.406  0.0048  0.1997 0.0127  402 ASP A OD1   
3290  O  OD2   . ASP A 402 ? 0.9538 0.4738 0.4208 0.0037  0.195  0.0112  402 ASP A OD2   
3291  N  N     . ILE A 403 ? 0.826  0.3197 0.274  0.0037  0.213  0.0091  403 ILE A N     
3292  C  CA    . ILE A 403 ? 0.826  0.3185 0.2751 -0.0016 0.2131 0.0058  403 ILE A CA    
3293  C  C     . ILE A 403 ? 0.8186 0.3217 0.2786 -0.0067 0.2072 0.0034  403 ILE A C     
3294  O  O     . ILE A 403 ? 0.8218 0.3231 0.2812 -0.0122 0.2067 -0.0003 403 ILE A O     
3295  C  CB    . ILE A 403 ? 0.8336 0.325  0.2824 0.0012  0.2166 0.0082  403 ILE A CB    
3296  C  CG1   . ILE A 403 ? 0.8478 0.3351 0.2946 -0.0043 0.2176 0.0046  403 ILE A CG1   
3297  C  CG2   . ILE A 403 ? 0.8322 0.3366 0.293  0.0048  0.2138 0.0124  403 ILE A CG2   
3298  C  CD1   . ILE A 403 ? 0.8723 0.3475 0.3077 -0.0084 0.2202 0.0009  403 ILE A CD1   
3299  N  N     . ASN A 404 ? 0.8064 0.3205 0.2758 -0.0049 0.2028 0.0058  404 ASN A N     
3300  C  CA    . ASN A 404 ? 0.7998 0.3232 0.2788 -0.0093 0.1972 0.0039  404 ASN A CA    
3301  C  C     . ASN A 404 ? 0.8013 0.3209 0.2766 -0.0136 0.1956 0       404 ASN A C     
3302  O  O     . ASN A 404 ? 0.8035 0.327  0.2835 -0.0182 0.1927 -0.0027 404 ASN A O     
3303  C  CB    . ASN A 404 ? 0.8069 0.3416 0.2952 -0.0065 0.1931 0.0076  404 ASN A CB    
3304  C  CG    . ASN A 404 ? 0.8508 0.3901 0.3432 -0.0019 0.1949 0.012   404 ASN A CG    
3305  O  OD1   . ASN A 404 ? 0.8656 0.4071 0.3618 -0.003  0.1958 0.0118  404 ASN A OD1   
3306  N  ND2   . ASN A 404 ? 0.8622 0.4028 0.3535 0.0038  0.196  0.0163  404 ASN A ND2   
3307  N  N     . LYS A 405 ? 0.7976 0.3093 0.2642 -0.0118 0.1976 -0.0002 405 LYS A N     
3308  C  CA    . LYS A 405 ? 0.7967 0.3036 0.2587 -0.0155 0.1968 -0.0036 405 LYS A CA    
3309  C  C     . LYS A 405 ? 0.795  0.2957 0.2525 -0.0204 0.1992 -0.0073 405 LYS A C     
3310  O  O     . LYS A 405 ? 0.7971 0.2989 0.2561 -0.0249 0.1972 -0.0102 405 LYS A O     
3311  C  CB    . LYS A 405 ? 0.8215 0.3202 0.2741 -0.012  0.1993 -0.0027 405 LYS A CB    
3312  C  CG    . LYS A 405 ? 0.8632 0.3675 0.3192 -0.0087 0.1958 -0.0002 405 LYS A CG    
3313  C  CD    . LYS A 405 ? 0.9141 0.4093 0.3599 -0.0055 0.1988 0.0003  405 LYS A CD    
3314  C  CE    . LYS A 405 ? 0.95   0.4503 0.3982 -0.0017 0.1957 0.0033  405 LYS A CE    
3315  N  NZ    . LYS A 405 ? 0.9841 0.4753 0.4221 0.0024  0.1993 0.0044  405 LYS A NZ    
3316  N  N     . LEU A 406 ? 0.7891 0.2833 0.2409 -0.0195 0.2037 -0.0069 406 LEU A N     
3317  C  CA    . LEU A 406 ? 0.7897 0.2781 0.2368 -0.0243 0.206  -0.0099 406 LEU A CA    
3318  C  C     . LEU A 406 ? 0.7822 0.2795 0.2388 -0.0279 0.203  -0.0111 406 LEU A C     
3319  O  O     . LEU A 406 ? 0.7825 0.2801 0.2396 -0.0329 0.2021 -0.014  406 LEU A O     
3320  C  CB    . LEU A 406 ? 0.7966 0.2753 0.2345 -0.022  0.2114 -0.0087 406 LEU A CB    
3321  C  CG    . LEU A 406 ? 0.8201 0.2907 0.2507 -0.0269 0.2143 -0.0116 406 LEU A CG    
3322  C  CD1   . LEU A 406 ? 0.8305 0.2959 0.2556 -0.0314 0.2144 -0.0146 406 LEU A CD1   
3323  C  CD2   . LEU A 406 ? 0.8375 0.2971 0.2575 -0.0239 0.2197 -0.01   406 LEU A CD2   
3324  N  N     . ALA A 407 ? 0.7737 0.2788 0.2382 -0.0251 0.2014 -0.0085 407 ALA A N     
3325  C  CA    . ALA A 407 ? 0.7709 0.2846 0.2447 -0.0278 0.1987 -0.0092 407 ALA A CA    
3326  C  C     . ALA A 407 ? 0.7682 0.2885 0.2483 -0.0311 0.1941 -0.0111 407 ALA A C     
3327  O  O     . ALA A 407 ? 0.7662 0.2903 0.2505 -0.035  0.1928 -0.0131 407 ALA A O     
3328  C  CB    . ALA A 407 ? 0.7695 0.2901 0.2503 -0.0236 0.1979 -0.0056 407 ALA A CB    
3329  N  N     . LYS A 408 ? 0.7672 0.2885 0.2472 -0.0294 0.192  -0.0104 408 LYS A N     
3330  C  CA    . LYS A 408 ? 0.7696 0.2957 0.2541 -0.0321 0.188  -0.0119 408 LYS A CA    
3331  C  C     . LYS A 408 ? 0.7746 0.2961 0.2546 -0.0366 0.1889 -0.0154 408 LYS A C     
3332  O  O     . LYS A 408 ? 0.7733 0.2995 0.2581 -0.0398 0.1865 -0.017  408 LYS A O     
3333  C  CB    . LYS A 408 ? 0.7931 0.3193 0.2764 -0.029  0.186  -0.0103 408 LYS A CB    
3334  C  CG    . LYS A 408 ? 0.8416 0.3725 0.3291 -0.0313 0.1815 -0.0115 408 LYS A CG    
3335  C  CD    . LYS A 408 ? 0.8969 0.4262 0.3814 -0.0288 0.1798 -0.0103 408 LYS A CD    
3336  C  CE    . LYS A 408 ? 0.9457 0.4663 0.4215 -0.03   0.182  -0.0126 408 LYS A CE    
3337  N  NZ    . LYS A 408 ? 0.9655 0.4864 0.4423 -0.0344 0.1806 -0.0155 408 LYS A NZ    
3338  N  N     . ARG A 409 ? 0.7779 0.2902 0.2487 -0.0369 0.1927 -0.0163 409 ARG A N     
3339  C  CA    . ARG A 409 ? 0.7833 0.2916 0.2499 -0.0412 0.1937 -0.0192 409 ARG A CA    
3340  C  C     . ARG A 409 ? 0.7796 0.2868 0.2453 -0.0451 0.1958 -0.0207 409 ARG A C     
3341  O  O     . ARG A 409 ? 0.7832 0.2911 0.249  -0.0493 0.1954 -0.0228 409 ARG A O     
3342  C  CB    . ARG A 409 ? 0.8118 0.3108 0.2687 -0.0403 0.1963 -0.0195 409 ARG A CB    
3343  C  CG    . ARG A 409 ? 0.8639 0.3547 0.3129 -0.0376 0.2005 -0.0183 409 ARG A CG    
3344  C  CD    . ARG A 409 ? 0.9186 0.3996 0.3576 -0.037  0.2032 -0.0188 409 ARG A CD    
3345  N  NE    . ARG A 409 ? 0.9646 0.4419 0.3997 -0.0421 0.2042 -0.0216 409 ARG A NE    
3346  C  CZ    . ARG A 409 ? 1.0067 0.4754 0.4331 -0.0448 0.208  -0.0228 409 ARG A CZ    
3347  N  NH1   . ARG A 409 ? 1.0099 0.4716 0.4297 -0.0426 0.2115 -0.0217 409 ARG A NH1   
3348  N  NH2   . ARG A 409 ? 1.0102 0.4769 0.4341 -0.0496 0.2085 -0.025  409 ARG A NH2   
3349  N  N     . ASN A 410 ? 0.7683 0.2738 0.2329 -0.0438 0.1979 -0.0196 410 ASN A N     
3350  C  CA    . ASN A 410 ? 0.7678 0.2714 0.2304 -0.0476 0.1998 -0.021  410 ASN A CA    
3351  C  C     . ASN A 410 ? 0.7614 0.2722 0.2318 -0.0472 0.1984 -0.0202 410 ASN A C     
3352  O  O     . ASN A 410 ? 0.7629 0.2756 0.236  -0.0431 0.1984 -0.0179 410 ASN A O     
3353  C  CB    . ASN A 410 ? 0.7881 0.2804 0.2395 -0.0471 0.2043 -0.0209 410 ASN A CB    
3354  C  CG    . ASN A 410 ? 0.8274 0.316  0.2746 -0.0519 0.2063 -0.0227 410 ASN A CG    
3355  O  OD1   . ASN A 410 ? 0.8396 0.3291 0.2882 -0.0516 0.207  -0.0221 410 ASN A OD1   
3356  N  ND2   . ASN A 410 ? 0.8386 0.3231 0.2806 -0.0564 0.2072 -0.0247 410 ASN A ND2   
3357  N  N     . GLY A 411 ? 0.7502 0.265  0.224  -0.0515 0.1975 -0.0219 411 GLY A N     
3358  C  CA    . GLY A 411 ? 0.7435 0.265  0.2245 -0.0517 0.1962 -0.0214 411 GLY A CA    
3359  C  C     . GLY A 411 ? 0.7416 0.2585 0.2187 -0.0504 0.1992 -0.0205 411 GLY A C     
3360  O  O     . GLY A 411 ? 0.737  0.2589 0.22   -0.0483 0.1984 -0.019  411 GLY A O     
3361  N  N     . LEU A 412 ? 0.741  0.2478 0.2076 -0.0518 0.2027 -0.0212 412 LEU A N     
3362  C  CA    . LEU A 412 ? 0.7441 0.2448 0.2053 -0.0504 0.2059 -0.0202 412 LEU A CA    
3363  C  C     . LEU A 412 ? 0.743  0.2416 0.2034 -0.044  0.2073 -0.0172 412 LEU A C     
3364  O  O     . LEU A 412 ? 0.7458 0.246  0.2089 -0.0411 0.2081 -0.0153 412 LEU A O     
3365  C  CB    . LEU A 412 ? 0.7502 0.2398 0.1995 -0.0542 0.2093 -0.0218 412 LEU A CB    
3366  C  CG    . LEU A 412 ? 0.7632 0.2451 0.2056 -0.0529 0.2127 -0.0209 412 LEU A CG    
3367  C  CD1   . LEU A 412 ? 0.7615 0.2499 0.2105 -0.0541 0.2113 -0.0209 412 LEU A CD1   
3368  C  CD2   . LEU A 412 ? 0.7772 0.2471 0.2066 -0.0566 0.216  -0.0224 412 LEU A CD2   
3369  N  N     . TRP A 413 ? 0.7354 0.231  0.1927 -0.0416 0.2076 -0.0165 413 TRP A N     
3370  C  CA    . TRP A 413 ? 0.7345 0.2296 0.1918 -0.0352 0.2087 -0.0132 413 TRP A CA    
3371  C  C     . TRP A 413 ? 0.7246 0.2318 0.1943 -0.0327 0.2049 -0.0112 413 TRP A C     
3372  O  O     . TRP A 413 ? 0.7235 0.2323 0.1952 -0.028  0.206  -0.0081 413 TRP A O     
3373  C  CB    . TRP A 413 ? 0.7396 0.2289 0.1905 -0.0333 0.2097 -0.0129 413 TRP A CB    
3374  C  CG    . TRP A 413 ? 0.7546 0.2304 0.1919 -0.0341 0.2144 -0.0138 413 TRP A CG    
3375  C  CD1   . TRP A 413 ? 0.7707 0.2399 0.2009 -0.0385 0.2153 -0.0164 413 TRP A CD1   
3376  C  CD2   . TRP A 413 ? 0.7599 0.2265 0.1887 -0.0307 0.219  -0.0119 413 TRP A CD2   
3377  N  NE1   . TRP A 413 ? 0.7817 0.238  0.1991 -0.0384 0.2201 -0.0165 413 TRP A NE1   
3378  C  CE2   . TRP A 413 ? 0.7771 0.2311 0.193  -0.0335 0.2226 -0.0137 413 TRP A CE2   
3379  C  CE3   . TRP A 413 ? 0.766  0.2336 0.1965 -0.0255 0.2207 -0.0086 413 TRP A CE3   
3380  C  CZ2   . TRP A 413 ? 0.7913 0.2329 0.1953 -0.0313 0.2277 -0.0126 413 TRP A CZ2   
3381  C  CZ3   . TRP A 413 ? 0.7836 0.2392 0.2025 -0.023  0.226  -0.0074 413 TRP A CZ3   
3382  C  CH2   . TRP A 413 ? 0.7924 0.2347 0.1979 -0.0259 0.2295 -0.0095 413 TRP A CH2   
3383  N  N     . LYS A 414 ? 0.7166 0.2322 0.1944 -0.0359 0.2009 -0.0128 414 LYS A N     
3384  C  CA    . LYS A 414 ? 0.7087 0.2354 0.1979 -0.0346 0.1971 -0.0113 414 LYS A CA    
3385  C  C     . LYS A 414 ? 0.7038 0.2336 0.1971 -0.0341 0.1979 -0.0103 414 LYS A C     
3386  O  O     . LYS A 414 ? 0.6967 0.2326 0.1966 -0.0307 0.1969 -0.0075 414 LYS A O     
3387  C  CB    . LYS A 414 ? 0.7214 0.2539 0.2159 -0.0387 0.1933 -0.0138 414 LYS A CB    
3388  C  CG    . LYS A 414 ? 0.7548 0.2967 0.2586 -0.0373 0.1891 -0.0123 414 LYS A CG    
3389  C  CD    . LYS A 414 ? 0.8    0.3467 0.3083 -0.0413 0.186  -0.0147 414 LYS A CD    
3390  C  CE    . LYS A 414 ? 0.843  0.3846 0.3453 -0.0436 0.1863 -0.0169 414 LYS A CE    
3391  N  NZ    . LYS A 414 ? 0.86   0.4059 0.3661 -0.0469 0.1836 -0.0188 414 LYS A NZ    
3392  N  N     . SER A 415 ? 0.7061 0.2318 0.1954 -0.0375 0.1998 -0.0124 415 SER A N     
3393  C  CA    . SER A 415 ? 0.7114 0.2386 0.2032 -0.0372 0.201  -0.0117 415 SER A CA    
3394  C  C     . SER A 415 ? 0.7199 0.2415 0.2069 -0.0321 0.2047 -0.0086 415 SER A C     
3395  O  O     . SER A 415 ? 0.7168 0.2432 0.2096 -0.0292 0.2047 -0.0063 415 SER A O     
3396  C  CB    . SER A 415 ? 0.7286 0.2514 0.2154 -0.0423 0.2022 -0.0147 415 SER A CB    
3397  O  OG    . SER A 415 ? 0.7527 0.2751 0.2399 -0.042  0.2038 -0.014  415 SER A OG    
3398  N  N     . PHE A 416 ? 0.7285 0.2397 0.2048 -0.0308 0.2081 -0.0085 416 PHE A N     
3399  C  CA    . PHE A 416 ? 0.7408 0.245  0.2107 -0.0255 0.2124 -0.0054 416 PHE A CA    
3400  C  C     . PHE A 416 ? 0.7443 0.2551 0.2206 -0.0196 0.2114 -0.0014 416 PHE A C     
3401  O  O     . PHE A 416 ? 0.7473 0.2592 0.2253 -0.0152 0.2134 0.0019  416 PHE A O     
3402  C  CB    . PHE A 416 ? 0.7474 0.2381 0.2033 -0.026  0.2163 -0.0065 416 PHE A CB    
3403  C  CG    . PHE A 416 ? 0.7608 0.2434 0.2084 -0.0316 0.2179 -0.0098 416 PHE A CG    
3404  C  CD1   . PHE A 416 ? 0.7709 0.2557 0.2212 -0.0344 0.2175 -0.0109 416 PHE A CD1   
3405  C  CD2   . PHE A 416 ? 0.7786 0.2507 0.215  -0.0341 0.2202 -0.0117 416 PHE A CD2   
3406  C  CE1   . PHE A 416 ? 0.7863 0.264  0.2287 -0.0399 0.2188 -0.0137 416 PHE A CE1   
3407  C  CE2   . PHE A 416 ? 0.7945 0.2592 0.2229 -0.0398 0.2216 -0.0145 416 PHE A CE2   
3408  C  CZ    . PHE A 416 ? 0.7915 0.2592 0.223  -0.0427 0.2208 -0.0154 416 PHE A CZ    
3409  N  N     . VAL A 417 ? 0.7422 0.2572 0.2216 -0.0194 0.2086 -0.0014 417 VAL A N     
3410  C  CA    . VAL A 417 ? 0.7461 0.2678 0.2313 -0.0144 0.2071 0.0024  417 VAL A CA    
3411  C  C     . VAL A 417 ? 0.748  0.2825 0.2463 -0.014  0.2034 0.0042  417 VAL A C     
3412  O  O     . VAL A 417 ? 0.7457 0.2855 0.2488 -0.0093 0.2035 0.0084  417 VAL A O     
3413  C  CB    . VAL A 417 ? 0.7536 0.275  0.2371 -0.015  0.2049 0.0015  417 VAL A CB    
3414  C  CG1   . VAL A 417 ? 0.7529 0.2832 0.2439 -0.0109 0.2021 0.0052  417 VAL A CG1   
3415  C  CG2   . VAL A 417 ? 0.7684 0.2769 0.2387 -0.0141 0.2093 0.0007  417 VAL A CG2   
3416  N  N     . SER A 418 ? 0.7509 0.2902 0.2547 -0.019  0.2004 0.0013  418 SER A N     
3417  C  CA    . SER A 418 ? 0.7537 0.3044 0.2693 -0.0192 0.197  0.0025  418 SER A CA    
3418  C  C     . SER A 418 ? 0.7631 0.3149 0.2811 -0.0171 0.1994 0.0045  418 SER A C     
3419  O  O     . SER A 418 ? 0.7612 0.3222 0.2886 -0.0152 0.1975 0.0073  418 SER A O     
3420  C  CB    . SER A 418 ? 0.7645 0.3191 0.2842 -0.0249 0.1935 -0.0012 418 SER A CB    
3421  O  OG    . SER A 418 ? 0.7929 0.3465 0.3105 -0.0269 0.1913 -0.0031 418 SER A OG    
3422  N  N     . LEU A 419 ? 0.7701 0.3129 0.28   -0.0178 0.2033 0.0031  419 LEU A N     
3423  C  CA    . LEU A 419 ? 0.7763 0.3195 0.2881 -0.0162 0.2056 0.0046  419 LEU A CA    
3424  C  C     . LEU A 419 ? 0.785  0.3194 0.2884 -0.0113 0.2111 0.0074  419 LEU A C     
3425  O  O     . LEU A 419 ? 0.7872 0.3221 0.2923 -0.0093 0.213  0.0092  419 LEU A O     
3426  C  CB    . LEU A 419 ? 0.7819 0.3233 0.2926 -0.0216 0.2051 0.0007  419 LEU A CB    
3427  C  CG    . LEU A 419 ? 0.7973 0.3486 0.3177 -0.0255 0.2002 -0.0013 419 LEU A CG    
3428  C  CD1   . LEU A 419 ? 0.8089 0.3578 0.3268 -0.0308 0.2    -0.0052 419 LEU A CD1   
3429  C  CD2   . LEU A 419 ? 0.7989 0.3603 0.3303 -0.0232 0.1983 0.0015  419 LEU A CD2   
3430  N  N     . SER A 420 ? 0.787  0.3127 0.2809 -0.009  0.2138 0.008   420 SER A N     
3431  C  CA    . SER A 420 ? 0.7952 0.3114 0.2799 -0.004  0.2195 0.0108  420 SER A CA    
3432  C  C     . SER A 420 ? 0.7968 0.3184 0.286  0.003   0.2204 0.0164  420 SER A C     
3433  O  O     . SER A 420 ? 0.7957 0.3221 0.2881 0.0041  0.218  0.0174  420 SER A O     
3434  C  CB    . SER A 420 ? 0.8126 0.3149 0.283  -0.0051 0.2228 0.0087  420 SER A CB    
3435  O  OG    . SER A 420 ? 0.8337 0.332  0.3002 -0.012  0.2214 0.0038  420 SER A OG    
3436  N  N     . ASP A 421 ? 0.7983 0.3187 0.2871 0.0078  0.2241 0.0201  421 ASP A N     
3437  C  CA    . ASP A 421 ? 0.8043 0.329  0.2961 0.0152  0.226  0.026   421 ASP A CA    
3438  C  C     . ASP A 421 ? 0.8175 0.3289 0.2952 0.0192  0.2313 0.0273  421 ASP A C     
3439  O  O     . ASP A 421 ? 0.8169 0.3312 0.2955 0.0243  0.2319 0.0311  421 ASP A O     
3440  C  CB    . ASP A 421 ? 0.8253 0.3539 0.3222 0.0192  0.2283 0.0299  421 ASP A CB    
3441  C  CG    . ASP A 421 ? 0.8818 0.4244 0.3933 0.016   0.2232 0.0295  421 ASP A CG    
3442  O  OD1   . ASP A 421 ? 0.8963 0.4378 0.4082 0.0107  0.2216 0.0253  421 ASP A OD1   
3443  O  OD2   . ASP A 421 ? 0.9021 0.457  0.4244 0.0188  0.2207 0.0336  421 ASP A OD2   
3444  N  N     . PHE A 422 ? 0.8261 0.3227 0.2903 0.0168  0.235  0.024   422 PHE A N     
3445  C  CA    . PHE A 422 ? 0.8385 0.3207 0.2878 0.0197  0.2402 0.0245  422 PHE A CA    
3446  C  C     . PHE A 422 ? 0.8509 0.3231 0.2907 0.0126  0.2397 0.0185  422 PHE A C     
3447  O  O     . PHE A 422 ? 0.8532 0.3238 0.2927 0.0072  0.2387 0.015   422 PHE A O     
3448  C  CB    . PHE A 422 ? 0.8406 0.3125 0.2807 0.025   0.2469 0.0276  422 PHE A CB    
3449  C  CG    . PHE A 422 ? 0.8387 0.3208 0.2888 0.0315  0.2477 0.0335  422 PHE A CG    
3450  C  CD1   . PHE A 422 ? 0.8456 0.333  0.2989 0.0386  0.249  0.0391  422 PHE A CD1   
3451  C  CD2   . PHE A 422 ? 0.8411 0.3283 0.298  0.0303  0.2469 0.0335  422 PHE A CD2   
3452  C  CE1   . PHE A 422 ? 0.8461 0.344  0.3093 0.0444  0.2497 0.0449  422 PHE A CE1   
3453  C  CE2   . PHE A 422 ? 0.8426 0.3395 0.309  0.0361  0.2477 0.0391  422 PHE A CE2   
3454  C  CZ    . PHE A 422 ? 0.8378 0.3402 0.3075 0.043   0.2491 0.0448  422 PHE A CZ    
3455  N  N     . ILE A 423 ? 0.8579 0.3241 0.2905 0.0124  0.2403 0.0175  423 ILE A N     
3456  C  CA    . ILE A 423 ? 0.8726 0.3293 0.296  0.0058  0.2401 0.0122  423 ILE A CA    
3457  C  C     . ILE A 423 ? 0.896  0.3353 0.302  0.0084  0.2465 0.0128  423 ILE A C     
3458  O  O     . ILE A 423 ? 0.903  0.3399 0.3055 0.0137  0.2487 0.0157  423 ILE A O     
3459  C  CB    . ILE A 423 ? 0.8723 0.3362 0.3017 0.0021  0.2351 0.0098  423 ILE A CB    
3460  C  CG1   . ILE A 423 ? 0.8726 0.3526 0.3181 -0.0008 0.2289 0.009   423 ILE A CG1   
3461  C  CG2   . ILE A 423 ? 0.8846 0.338  0.3036 -0.0043 0.2356 0.0049  423 ILE A CG2   
3462  C  CD1   . ILE A 423 ? 0.8816 0.3695 0.3337 -0.0031 0.224  0.0076  423 ILE A CD1   
3463  N  N     . VAL A 424 ? 0.9067 0.3333 0.3013 0.0048  0.2496 0.0102  424 VAL A N     
3464  C  CA    . VAL A 424 ? 0.9271 0.3354 0.3035 0.0065  0.2559 0.0105  424 VAL A CA    
3465  C  C     . VAL A 424 ? 0.9393 0.3385 0.3064 -0.0014 0.2553 0.0053  424 VAL A C     
3466  O  O     . VAL A 424 ? 0.9384 0.3397 0.3079 -0.0083 0.2524 0.0017  424 VAL A O     
3467  C  CB    . VAL A 424 ? 0.9444 0.3433 0.3128 0.0096  0.2609 0.0125  424 VAL A CB    
3468  C  CG1   . VAL A 424 ? 0.9679 0.346  0.3157 0.0111  0.2677 0.0126  424 VAL A CG1   
3469  C  CG2   . VAL A 424 ? 0.9441 0.3528 0.3223 0.0178  0.2618 0.0182  424 VAL A CG2   
3470  N  N     . LEU A 425 ? 0.9486 0.3383 0.3055 -0.0005 0.2579 0.005   425 LEU A N     
3471  C  CA    . LEU A 425 ? 0.9636 0.3441 0.3111 -0.008  0.2576 0.0004  425 LEU A CA    
3472  C  C     . LEU A 425 ? 0.9822 0.342  0.3094 -0.0071 0.2644 0.0005  425 LEU A C     
3473  O  O     . LEU A 425 ? 0.9879 0.3409 0.3083 0.0003  0.269  0.0042  425 LEU A O     
3474  C  CB    . LEU A 425 ? 0.9652 0.3514 0.3172 -0.0086 0.2547 -0.0005 425 LEU A CB    
3475  C  CG    . LEU A 425 ? 0.9741 0.3795 0.3447 -0.0079 0.2485 0.0002  425 LEU A CG    
3476  C  CD1   . LEU A 425 ? 0.9792 0.3872 0.3512 -0.0073 0.2467 -0.0002 425 LEU A CD1   
3477  C  CD2   . LEU A 425 ? 0.9782 0.3926 0.358  -0.015  0.2437 -0.0032 425 LEU A CD2   
3478  N  N     . ASP A 426 ? 0.9895 0.3392 0.3066 -0.0146 0.2651 -0.0033 426 ASP A N     
3479  C  CA    . ASP A 426 ? 1.01   0.3386 0.3063 -0.0156 0.2711 -0.004  426 ASP A CA    
3480  C  C     . ASP A 426 ? 1.0107 0.338  0.3046 -0.0255 0.268  -0.0089 426 ASP A C     
3481  O  O     . ASP A 426 ? 1.0157 0.3392 0.3056 -0.0326 0.2671 -0.0117 426 ASP A O     
3482  C  CB    . ASP A 426 ? 1.0438 0.3614 0.3301 -0.0152 0.275  -0.0033 426 ASP A CB    
3483  C  CG    . ASP A 426 ? 1.127  0.4211 0.3901 -0.0154 0.2819 -0.0035 426 ASP A CG    
3484  O  OD1   . ASP A 426 ? 1.14   0.4261 0.3946 -0.0166 0.2835 -0.0046 426 ASP A OD1   
3485  O  OD2   . ASP A 426 ? 1.169  0.4521 0.422  -0.0142 0.2858 -0.0025 426 ASP A OD2   
3486  N  N     . CYS A 427 ? 1.0027 0.3347 0.3006 -0.0259 0.266  -0.0096 427 CYS A N     
3487  C  CA    . CYS A 427 ? 1.0031 0.3377 0.3025 -0.0345 0.2624 -0.0137 427 CYS A CA    
3488  C  C     . CYS A 427 ? 1.0129 0.3334 0.2978 -0.0369 0.2657 -0.0152 427 CYS A C     
3489  O  O     . CYS A 427 ? 1.0179 0.3352 0.2998 -0.031  0.2681 -0.0132 427 CYS A O     
3490  C  CB    . CYS A 427 ? 0.9946 0.3488 0.313  -0.0343 0.2563 -0.0139 427 CYS A CB    
3491  S  SG    . CYS A 427 ? 1.0038 0.3755 0.3402 -0.0327 0.2518 -0.0125 427 CYS A SG    
3492  N  N     . PRO A 428 ? 1.0107 0.3255 0.2889 -0.0462 0.2649 -0.0189 428 PRO A N     
3493  C  CA    . PRO A 428 ? 1.0153 0.3192 0.282  -0.0496 0.2671 -0.0206 428 PRO A CA    
3494  C  C     . PRO A 428 ? 1.0048 0.3215 0.2839 -0.0485 0.2633 -0.0208 428 PRO A C     
3495  O  O     . PRO A 428 ? 0.9966 0.3303 0.2923 -0.0489 0.258  -0.021  428 PRO A O     
3496  C  CB    . PRO A 428 ? 1.0278 0.3274 0.2888 -0.0605 0.2657 -0.0242 428 PRO A CB    
3497  C  CG    . PRO A 428 ? 1.0305 0.3349 0.2961 -0.0619 0.264  -0.0241 428 PRO A CG    
3498  C  CD    . PRO A 428 ? 1.0007 0.3203 0.2826 -0.0542 0.2616 -0.0214 428 PRO A CD    
3499  N  N     . ILE A 429 ? 1.0058 0.3138 0.2763 -0.047  0.266  -0.0208 429 ILE A N     
3500  C  CA    . ILE A 429 ? 1.001  0.3195 0.2815 -0.046  0.2627 -0.0211 429 ILE A CA    
3501  C  C     . ILE A 429 ? 1.0051 0.3181 0.2791 -0.0542 0.2625 -0.0243 429 ILE A C     
3502  O  O     . ILE A 429 ? 1.0188 0.3151 0.2763 -0.0562 0.2672 -0.025  429 ILE A O     
3503  C  CB    . ILE A 429 ? 1.0074 0.323  0.2856 -0.0365 0.2656 -0.0179 429 ILE A CB    
3504  C  CG1   . ILE A 429 ? 1.015  0.3356 0.2988 -0.0283 0.2664 -0.0141 429 ILE A CG1   
3505  C  CG2   . ILE A 429 ? 1.0049 0.3312 0.2933 -0.0356 0.2619 -0.0182 429 ILE A CG2   
3506  C  CD1   . ILE A 429 ? 1.0178 0.3578 0.3207 -0.0281 0.2604 -0.0136 429 ILE A CD1   
3507  N  N     . ILE A 430 ? 0.9909 0.3175 0.2775 -0.0589 0.2573 -0.0261 430 ILE A N     
3508  C  CA    . ILE A 430 ? 0.9928 0.3167 0.2755 -0.0667 0.2567 -0.0288 430 ILE A CA    
3509  C  C     . ILE A 430 ? 1.0036 0.3161 0.2756 -0.0638 0.2606 -0.0285 430 ILE A C     
3510  O  O     . ILE A 430 ? 1.0029 0.3207 0.2808 -0.0573 0.2599 -0.0269 430 ILE A O     
3511  C  CB    . ILE A 430 ? 0.9815 0.3234 0.2811 -0.0699 0.2507 -0.0299 430 ILE A CB    
3512  C  CG1   . ILE A 430 ? 0.9803 0.3337 0.2907 -0.0723 0.247  -0.0301 430 ILE A CG1   
3513  C  CG2   . ILE A 430 ? 0.9884 0.3285 0.2847 -0.0776 0.2503 -0.0322 430 ILE A CG2   
3514  C  CD1   . ILE A 430 ? 0.9978 0.3444 0.3001 -0.0797 0.248  -0.0317 430 ILE A CD1   
3515  N  N     . GLY A 431 ? 1.0119 0.3083 0.2675 -0.0685 0.2647 -0.0299 431 GLY A N     
3516  C  CA    . GLY A 431 ? 1.0246 0.308  0.2679 -0.0662 0.2691 -0.0297 431 GLY A CA    
3517  C  C     . GLY A 431 ? 1.0351 0.3026 0.2638 -0.0594 0.2752 -0.0275 431 GLY A C     
3518  O  O     . GLY A 431 ? 1.0447 0.2999 0.2617 -0.057  0.2794 -0.0272 431 GLY A O     
3519  N  N     . GLU A 432 ? 1.0308 0.2983 0.26   -0.0559 0.2759 -0.0259 432 GLU A N     
3520  C  CA    . GLU A 432 ? 1.0447 0.2976 0.2604 -0.0489 0.282  -0.0233 432 GLU A CA    
3521  C  C     . GLU A 432 ? 1.0588 0.2987 0.2616 -0.0534 0.285  -0.0242 432 GLU A C     
3522  O  O     . GLU A 432 ? 1.0574 0.304  0.266  -0.0604 0.2813 -0.0261 432 GLU A O     
3523  C  CB    . GLU A 432 ? 1.0636 0.3272 0.2906 -0.0386 0.2811 -0.0196 432 GLU A CB    
3524  C  CG    . GLU A 432 ? 1.1203 0.3946 0.3576 -0.0339 0.2785 -0.0185 432 GLU A CG    
3525  C  CD    . GLU A 432 ? 1.205  0.4851 0.4482 -0.023  0.2793 -0.0143 432 GLU A CD    
3526  O  OE1   . GLU A 432 ? 1.2209 0.5076 0.4707 -0.0201 0.2784 -0.0124 432 GLU A OE1   
3527  O  OE2   . GLU A 432 ? 1.2319 0.5102 0.4729 -0.0174 0.2809 -0.0126 432 GLU A OE2   
3528  N  N     . SER A 433 ? 1.0714 0.2922 0.256  -0.0495 0.2917 -0.0228 433 SER A N     
3529  C  CA    . SER A 433 ? 1.0896 0.2948 0.2587 -0.0539 0.2952 -0.0237 433 SER A CA    
3530  C  C     . SER A 433 ? 1.0911 0.3    0.2645 -0.0497 0.2952 -0.0216 433 SER A C     
3531  O  O     . SER A 433 ? 1.0963 0.2992 0.2633 -0.0559 0.2952 -0.0232 433 SER A O     
3532  C  CB    . SER A 433 ? 1.1229 0.304  0.2688 -0.0517 0.303  -0.0231 433 SER A CB    
3533  O  OG    . SER A 433 ? 1.1565 0.3331 0.2977 -0.0537 0.3039 -0.0244 433 SER A OG    
3534  N  N     . TYR A 434 ? 1.0841 0.3015 0.2667 -0.0394 0.2955 -0.0179 434 TYR A N     
3535  C  CA    . TYR A 434 ? 1.087  0.3073 0.2731 -0.0347 0.2961 -0.0155 434 TYR A CA    
3536  C  C     . TYR A 434 ? 1.0751 0.3189 0.2846 -0.0302 0.2904 -0.0137 434 TYR A C     
3537  O  O     . TYR A 434 ? 1.0685 0.3255 0.2906 -0.0293 0.2865 -0.0138 434 TYR A O     
3538  C  CB    . TYR A 434 ? 1.0994 0.3021 0.269  -0.026  0.304  -0.0119 434 TYR A CB    
3539  C  CG    . TYR A 434 ? 1.1274 0.3056 0.2727 -0.0312 0.3097 -0.0139 434 TYR A CG    
3540  C  CD1   . TYR A 434 ? 1.1458 0.3141 0.2813 -0.0376 0.3105 -0.0157 434 TYR A CD1   
3541  C  CD2   . TYR A 434 ? 1.1481 0.3133 0.2804 -0.0309 0.3136 -0.0144 434 TYR A CD2   
3542  C  CE1   . TYR A 434 ? 1.1729 0.3185 0.2857 -0.0435 0.3152 -0.0178 434 TYR A CE1   
3543  C  CE2   . TYR A 434 ? 1.1741 0.3165 0.2839 -0.0367 0.3185 -0.0165 434 TYR A CE2   
3544  C  CZ    . TYR A 434 ? 1.1928 0.3253 0.2926 -0.0431 0.3193 -0.0182 434 TYR A CZ    
3545  O  OH    . TYR A 434 ? 1.2286 0.3379 0.3053 -0.0494 0.324  -0.0203 434 TYR A OH    
3546  N  N     . ASN A 435 ? 1.0683 0.3167 0.2829 -0.028  0.2899 -0.0121 435 ASN A N     
3547  C  CA    . ASN A 435 ? 1.0553 0.3248 0.2909 -0.0245 0.2847 -0.0104 435 ASN A CA    
3548  C  C     . ASN A 435 ? 1.0484 0.3255 0.2916 -0.0137 0.2857 -0.0059 435 ASN A C     
3549  O  O     . ASN A 435 ? 1.0553 0.3203 0.2867 -0.0069 0.2915 -0.0031 435 ASN A O     
3550  C  CB    . ASN A 435 ? 1.0697 0.3399 0.3065 -0.0255 0.2845 -0.0101 435 ASN A CB    
3551  C  CG    . ASN A 435 ? 1.111  0.3824 0.3482 -0.0364 0.2808 -0.0143 435 ASN A CG    
3552  O  OD1   . ASN A 435 ? 1.1269 0.3924 0.3573 -0.0439 0.2803 -0.0175 435 ASN A OD1   
3553  N  ND2   . ASN A 435 ? 1.1184 0.3977 0.3637 -0.0374 0.2784 -0.0142 435 ASN A ND2   
3554  N  N     . GLU A 436 ? 1.0324 0.3299 0.2957 -0.0122 0.2798 -0.0051 436 GLU A N     
3555  C  CA    . GLU A 436 ? 1.0249 0.3335 0.2988 -0.003  0.2792 -0.0008 436 GLU A CA    
3556  C  C     . GLU A 436 ? 1.0103 0.3288 0.2946 0.0001  0.2779 0.0017  436 GLU A C     
3557  O  O     . GLU A 436 ? 1.0032 0.3305 0.2966 -0.0057 0.2734 -0.0008 436 GLU A O     
3558  C  CB    . GLU A 436 ? 1.0418 0.3665 0.3309 -0.0046 0.273  -0.0019 436 GLU A CB    
3559  C  CG    . GLU A 436 ? 1.1095 0.4266 0.3904 -0.005  0.2746 -0.0031 436 GLU A CG    
3560  C  CD    . GLU A 436 ? 1.2013 0.5121 0.4753 0.0046  0.2794 0.0012  436 GLU A CD    
3561  O  OE1   . GLU A 436 ? 1.2316 0.5253 0.4889 0.0074  0.2861 0.0025  436 GLU A OE1   
3562  O  OE2   . GLU A 436 ? 1.2264 0.5493 0.5113 0.0094  0.2766 0.0035  436 GLU A OE2   
3563  N  N     . PHE A 437 ? 1.0039 0.3211 0.2868 0.0095  0.2818 0.0067  437 PHE A N     
3564  C  CA    . PHE A 437 ? 0.9979 0.3254 0.2916 0.0133  0.2807 0.0096  437 PHE A CA    
3565  C  C     . PHE A 437 ? 0.9825 0.3286 0.2935 0.0193  0.2769 0.0132  437 PHE A C     
3566  O  O     . PHE A 437 ? 0.9852 0.3302 0.2937 0.0258  0.2792 0.0164  437 PHE A O     
3567  C  CB    . PHE A 437 ? 1.0074 0.3206 0.2876 0.0192  0.2879 0.013   437 PHE A CB    
3568  C  CG    . PHE A 437 ? 1.008  0.3332 0.3004 0.0252  0.2873 0.0172  437 PHE A CG    
3569  C  CD1   . PHE A 437 ? 1.0117 0.3453 0.3135 0.0205  0.2835 0.0154  437 PHE A CD1   
3570  C  CD2   . PHE A 437 ? 1.017  0.3468 0.3129 0.0354  0.29   0.0232  437 PHE A CD2   
3571  C  CE1   . PHE A 437 ? 1.0136 0.359  0.3274 0.0258  0.2826 0.0193  437 PHE A CE1   
3572  C  CE2   . PHE A 437 ? 1.0186 0.3609 0.3269 0.0405  0.2891 0.0273  437 PHE A CE2   
3573  C  CZ    . PHE A 437 ? 1.0097 0.3594 0.3267 0.0356  0.2854 0.0252  437 PHE A CZ    
3574  N  N     . ARG A 438 ? 0.9642 0.3272 0.2921 0.0171  0.2711 0.0128  438 ARG A N     
3575  C  CA    . ARG A 438 ? 0.9525 0.3336 0.2972 0.0218  0.2669 0.0162  438 ARG A CA    
3576  C  C     . ARG A 438 ? 0.9477 0.3395 0.3038 0.0236  0.2654 0.0185  438 ARG A C     
3577  O  O     . ARG A 438 ? 0.9519 0.3433 0.3089 0.0181  0.264  0.0156  438 ARG A O     
3578  C  CB    . ARG A 438 ? 0.9562 0.3491 0.3121 0.0159  0.26   0.0127  438 ARG A CB    
3579  C  CG    . ARG A 438 ? 0.9906 0.3746 0.337  0.0137  0.261  0.0103  438 ARG A CG    
3580  C  CD    . ARG A 438 ? 1.0184 0.4054 0.3658 0.0211  0.2619 0.0142  438 ARG A CD    
3581  N  NE    . ARG A 438 ? 1.0559 0.4259 0.3861 0.0246  0.2683 0.0151  438 ARG A NE    
3582  C  CZ    . ARG A 438 ? 1.0786 0.4396 0.3997 0.021   0.269  0.0119  438 ARG A CZ    
3583  N  NH1   . ARG A 438 ? 1.0817 0.4264 0.3865 0.0245  0.2754 0.013   438 ARG A NH1   
3584  N  NH2   . ARG A 438 ? 1.0687 0.4358 0.3962 0.0137  0.2638 0.0076  438 ARG A NH2   
3585  N  N     . LEU A 439 ? 0.9349 0.337  0.2999 0.0313  0.2654 0.0239  439 LEU A N     
3586  C  CA    . LEU A 439 ? 0.9231 0.3373 0.3007 0.0333  0.2635 0.0266  439 LEU A CA    
3587  C  C     . LEU A 439 ? 0.9075 0.3407 0.3022 0.035   0.2576 0.0288  439 LEU A C     
3588  O  O     . LEU A 439 ? 0.9058 0.3423 0.3016 0.0415  0.2588 0.0331  439 LEU A O     
3589  C  CB    . LEU A 439 ? 0.9276 0.3349 0.2984 0.0415  0.2701 0.032   439 LEU A CB    
3590  C  CG    . LEU A 439 ? 0.932  0.3534 0.317  0.0455  0.2686 0.0362  439 LEU A CG    
3591  C  CD1   . LEU A 439 ? 0.9337 0.3612 0.3267 0.0385  0.2644 0.0323  439 LEU A CD1   
3592  C  CD2   . LEU A 439 ? 0.9446 0.3569 0.3207 0.0536  0.276  0.0413  439 LEU A CD2   
3593  N  N     . ILE A 440 ? 0.8953 0.3406 0.3026 0.029   0.2513 0.0258  440 ILE A N     
3594  C  CA    . ILE A 440 ? 0.887  0.3496 0.31   0.0293  0.2452 0.0273  440 ILE A CA    
3595  C  C     . ILE A 440 ? 0.8776 0.3536 0.3141 0.0311  0.243  0.0304  440 ILE A C     
3596  O  O     . ILE A 440 ? 0.8768 0.3546 0.317  0.0264  0.2413 0.0276  440 ILE A O     
3597  C  CB    . ILE A 440 ? 0.8937 0.3598 0.3205 0.0211  0.2396 0.0216  440 ILE A CB    
3598  C  CG1   . ILE A 440 ? 0.9166 0.369  0.3296 0.0188  0.2421 0.0184  440 ILE A CG1   
3599  C  CG2   . ILE A 440 ? 0.8907 0.3734 0.3323 0.0211  0.2333 0.023   440 ILE A CG2   
3600  C  CD1   . ILE A 440 ? 0.9298 0.385  0.3457 0.0112  0.2372 0.0133  440 ILE A CD1   
3601  N  N     . ILE A 441 ? 0.8697 0.3556 0.3139 0.0377  0.2428 0.0362  441 ILE A N     
3602  C  CA    . ILE A 441 ? 0.8663 0.3663 0.3244 0.0394  0.2404 0.0396  441 ILE A CA    
3603  C  C     . ILE A 441 ? 0.8617 0.376  0.3334 0.0339  0.2324 0.0373  441 ILE A C     
3604  O  O     . ILE A 441 ? 0.8579 0.3812 0.336  0.0358  0.2292 0.0397  441 ILE A O     
3605  C  CB    . ILE A 441 ? 0.8706 0.3754 0.3311 0.0487  0.2437 0.0472  441 ILE A CB    
3606  C  CG1   . ILE A 441 ? 0.8946 0.3828 0.3392 0.0544  0.2521 0.0493  441 ILE A CG1   
3607  C  CG2   . ILE A 441 ? 0.8659 0.3856 0.3411 0.0502  0.2413 0.051   441 ILE A CG2   
3608  C  CD1   . ILE A 441 ? 0.9168 0.3961 0.3557 0.0529  0.2557 0.0477  441 ILE A CD1   
3609  N  N     . ASN A 442 ? 0.8602 0.3756 0.3353 0.0271  0.2294 0.0325  442 ASN A N     
3610  C  CA    . ASN A 442 ? 0.8592 0.3854 0.3448 0.0212  0.2225 0.0295  442 ASN A CA    
3611  C  C     . ASN A 442 ? 0.8554 0.3965 0.3559 0.0209  0.2186 0.0317  442 ASN A C     
3612  O  O     . ASN A 442 ? 0.8535 0.4025 0.3622 0.0156  0.2131 0.029   442 ASN A O     
3613  C  CB    . ASN A 442 ? 0.8757 0.3939 0.3555 0.0139  0.2218 0.023   442 ASN A CB    
3614  C  CG    . ASN A 442 ? 0.9076 0.4323 0.3933 0.0081  0.2159 0.0192  442 ASN A CG    
3615  O  OD1   . ASN A 442 ? 0.9238 0.4497 0.4091 0.0087  0.214  0.0194  442 ASN A OD1   
3616  N  ND2   . ASN A 442 ? 0.9097 0.4381 0.4007 0.0027  0.2131 0.0159  442 ASN A ND2   
3617  N  N     . LYS A 443 ? 0.8516 0.3962 0.3554 0.0265  0.2216 0.0369  443 LYS A N     
3618  C  CA    . LYS A 443 ? 0.8467 0.4049 0.3642 0.0265  0.2185 0.0395  443 LYS A CA    
3619  C  C     . LYS A 443 ? 0.8423 0.415  0.3722 0.024   0.2116 0.0402  443 LYS A C     
3620  O  O     . LYS A 443 ? 0.8395 0.4189 0.3774 0.0189  0.2074 0.0376  443 LYS A O     
3621  C  CB    . LYS A 443 ? 0.8674 0.4275 0.3862 0.0342  0.2232 0.0461  443 LYS A CB    
3622  C  CG    . LYS A 443 ? 0.9214 0.4721 0.4338 0.0351  0.2283 0.0453  443 LYS A CG    
3623  C  CD    . LYS A 443 ? 0.9739 0.5294 0.4905 0.0422  0.232  0.0521  443 LYS A CD    
3624  C  CE    . LYS A 443 ? 1.0262 0.5746 0.5389 0.0423  0.2358 0.0512  443 LYS A CE    
3625  N  NZ    . LYS A 443 ? 1.0481 0.6048 0.5709 0.0362  0.2311 0.0479  443 LYS A NZ    
3626  N  N     . ASN A 444 ? 0.8422 0.4192 0.3732 0.0275  0.2105 0.0437  444 ASN A N     
3627  C  CA    . ASN A 444 ? 0.8427 0.4329 0.3845 0.0249  0.2039 0.0446  444 ASN A CA    
3628  C  C     . ASN A 444 ? 0.8483 0.436  0.3885 0.0179  0.1994 0.0383  444 ASN A C     
3629  O  O     . ASN A 444 ? 0.8439 0.441  0.393  0.0136  0.1938 0.0373  444 ASN A O     
3630  C  CB    . ASN A 444 ? 0.857  0.4528 0.4001 0.0305  0.2037 0.0502  444 ASN A CB    
3631  C  CG    . ASN A 444 ? 0.8906 0.5022 0.4466 0.0287  0.1971 0.0529  444 ASN A CG    
3632  O  OD1   . ASN A 444 ? 0.905  0.5206 0.4615 0.0297  0.1944 0.0547  444 ASN A OD1   
3633  N  ND2   . ASN A 444 ? 0.8935 0.5143 0.4598 0.0258  0.1942 0.0533  444 ASN A ND2   
3634  N  N     . ASN A 445 ? 0.8564 0.4312 0.3849 0.0165  0.2021 0.0343  445 ASN A N     
3635  C  CA    . ASN A 445 ? 0.8662 0.4379 0.3924 0.0102  0.1986 0.0286  445 ASN A CA    
3636  C  C     . ASN A 445 ? 0.8697 0.4434 0.4006 0.0046  0.1966 0.0247  445 ASN A C     
3637  O  O     . ASN A 445 ? 0.8678 0.447  0.4041 -0.0001 0.1917 0.0222  445 ASN A O     
3638  C  CB    . ASN A 445 ? 0.8884 0.446  0.4011 0.0103  0.2025 0.0257  445 ASN A CB    
3639  C  CG    . ASN A 445 ? 0.9288 0.4839 0.4392 0.0049  0.1991 0.0209  445 ASN A CG    
3640  O  OD1   . ASN A 445 ? 0.9374 0.5009 0.4549 0.0026  0.1938 0.0206  445 ASN A OD1   
3641  N  ND2   . ASN A 445 ? 0.9451 0.4884 0.445  0.0028  0.2021 0.0171  445 ASN A ND2   
3642  N  N     . LYS A 446 ? 0.8736 0.4428 0.4021 0.0054  0.2005 0.0245  446 LYS A N     
3643  C  CA    . LYS A 446 ? 0.8809 0.4518 0.4135 0.0006  0.1991 0.0213  446 LYS A CA    
3644  C  C     . LYS A 446 ? 0.8849 0.4695 0.4308 -0.0005 0.1945 0.0232  446 LYS A C     
3645  O  O     . LYS A 446 ? 0.8852 0.4734 0.4355 -0.0057 0.1907 0.0199  446 LYS A O     
3646  C  CB    . LYS A 446 ? 0.9025 0.466  0.4297 0.0025  0.2044 0.0215  446 LYS A CB    
3647  C  CG    . LYS A 446 ? 0.9413 0.5083 0.4741 -0.0012 0.2032 0.0193  446 LYS A CG    
3648  C  CD    . LYS A 446 ? 0.9922 0.5511 0.5186 0.0005  0.2083 0.0195  446 LYS A CD    
3649  C  CE    . LYS A 446 ? 1.0225 0.586  0.5554 -0.0027 0.2068 0.0179  446 LYS A CE    
3650  N  NZ    . LYS A 446 ? 1.0455 0.6    0.5711 -0.0016 0.2116 0.0175  446 LYS A NZ    
3651  N  N     . GLU A 447 ? 0.8861 0.4783 0.438  0.0043  0.1947 0.0289  447 GLU A N     
3652  C  CA    . GLU A 447 ? 0.8895 0.4952 0.4542 0.0032  0.1903 0.0314  447 GLU A CA    
3653  C  C     . GLU A 447 ? 0.8939 0.505  0.4625 -0.0013 0.1842 0.0293  447 GLU A C     
3654  O  O     . GLU A 447 ? 0.8926 0.5096 0.468  -0.0056 0.1804 0.0276  447 GLU A O     
3655  C  CB    . GLU A 447 ? 0.9178 0.5309 0.4878 0.0094  0.1918 0.0383  447 GLU A CB    
3656  C  CG    . GLU A 447 ? 0.9921 0.6028 0.5614 0.0136  0.1971 0.0409  447 GLU A CG    
3657  C  CD    . GLU A 447 ? 1.0782 0.6959 0.6522 0.0204  0.1992 0.0483  447 GLU A CD    
3658  O  OE1   . GLU A 447 ? 1.0941 0.7195 0.6723 0.022   0.1964 0.0517  447 GLU A OE1   
3659  O  OE2   . GLU A 447 ? 1.1077 0.7234 0.6811 0.0243  0.2038 0.0509  447 GLU A OE2   
3660  N  N     . SER A 448 ? 0.8966 0.5046 0.4599 -0.0002 0.1836 0.0294  448 SER A N     
3661  C  CA    . SER A 448 ? 0.9002 0.5118 0.4656 -0.0041 0.1781 0.0276  448 SER A CA    
3662  C  C     . SER A 448 ? 0.9096 0.5158 0.4718 -0.01   0.1767 0.0214  448 SER A C     
3663  O  O     . SER A 448 ? 0.909  0.5203 0.4762 -0.0141 0.172  0.0199  448 SER A O     
3664  C  CB    . SER A 448 ? 0.9175 0.5258 0.4769 -0.0011 0.1784 0.029   448 SER A CB    
3665  O  OG    . SER A 448 ? 0.9428 0.5573 0.5057 0.0046  0.1797 0.0352  448 SER A OG    
3666  N  N     . ILE A 449 ? 0.9183 0.5141 0.4721 -0.0104 0.1807 0.0182  449 ILE A N     
3667  C  CA    . ILE A 449 ? 0.932  0.5231 0.4828 -0.0157 0.1797 0.0128  449 ILE A CA    
3668  C  C     . ILE A 449 ? 0.9413 0.538  0.4995 -0.0189 0.178  0.0115  449 ILE A C     
3669  O  O     . ILE A 449 ? 0.9433 0.5416 0.5034 -0.0233 0.1747 0.0085  449 ILE A O     
3670  C  CB    . ILE A 449 ? 0.9455 0.5248 0.4856 -0.0157 0.1844 0.0099  449 ILE A CB    
3671  C  CG1   . ILE A 449 ? 0.9609 0.5343 0.4934 -0.0133 0.1855 0.0105  449 ILE A CG1   
3672  C  CG2   . ILE A 449 ? 0.9535 0.5294 0.4916 -0.0212 0.1835 0.0049  449 ILE A CG2   
3673  C  CD1   . ILE A 449 ? 0.9831 0.5449 0.5048 -0.0122 0.1907 0.0091  449 ILE A CD1   
3674  N  N     . LEU A 450 ? 0.9458 0.5456 0.508  -0.0165 0.1802 0.0141  450 LEU A N     
3675  C  CA    . LEU A 450 ? 0.9541 0.5592 0.5233 -0.0191 0.1788 0.0132  450 LEU A CA    
3676  C  C     . LEU A 450 ? 0.962  0.5772 0.5404 -0.0214 0.1735 0.0144  450 LEU A C     
3677  O  O     . LEU A 450 ? 0.9614 0.58   0.5446 -0.0245 0.1718 0.0128  450 LEU A O     
3678  C  CB    . LEU A 450 ? 0.9548 0.5602 0.5257 -0.0157 0.1827 0.0158  450 LEU A CB    
3679  C  CG    . LEU A 450 ? 0.9795 0.5741 0.5407 -0.0143 0.188  0.0143  450 LEU A CG    
3680  C  CD1   . LEU A 450 ? 0.9859 0.5808 0.5488 -0.0109 0.1916 0.0171  450 LEU A CD1   
3681  C  CD2   . LEU A 450 ? 0.9909 0.5798 0.5475 -0.0193 0.1878 0.009   450 LEU A CD2   
3682  N  N     . ARG A 451 ? 0.9678 0.5873 0.5481 -0.02   0.1708 0.0172  451 ARG A N     
3683  C  CA    . ARG A 451 ? 0.9766 0.605  0.5645 -0.0228 0.1654 0.0184  451 ARG A CA    
3684  C  C     . ARG A 451 ? 0.9913 0.6169 0.5751 -0.0261 0.1618 0.0156  451 ARG A C     
3685  O  O     . ARG A 451 ? 0.9897 0.6213 0.5778 -0.0279 0.1573 0.017   451 ARG A O     
3686  C  CB    . ARG A 451 ? 0.991  0.6285 0.5857 -0.0193 0.1644 0.0243  451 ARG A CB    
3687  C  CG    . ARG A 451 ? 1.0353 0.6743 0.6324 -0.0147 0.1688 0.0278  451 ARG A CG    
3688  C  CD    . ARG A 451 ? 1.0761 0.7265 0.6824 -0.0121 0.1672 0.0339  451 ARG A CD    
3689  N  NE    . ARG A 451 ? 1.1204 0.7704 0.7241 -0.006  0.1703 0.0383  451 ARG A NE    
3690  C  CZ    . ARG A 451 ? 1.1523 0.8047 0.7549 -0.0046 0.1682 0.0405  451 ARG A CZ    
3691  N  NH1   . ARG A 451 ? 1.1507 0.8023 0.7504 0.0015  0.1717 0.0447  451 ARG A NH1   
3692  N  NH2   . ARG A 451 ? 1.1506 0.8055 0.7541 -0.009  0.1628 0.0387  451 ARG A NH2   
3693  N  N     . LYS A 452 ? 1.0044 0.6208 0.5799 -0.027  0.1638 0.0117  452 LYS A N     
3694  C  CA    . LYS A 452 ? 1.0213 0.6341 0.5921 -0.0296 0.161  0.0092  452 LYS A CA    
3695  C  C     . LYS A 452 ? 1.0319 0.6438 0.6032 -0.0345 0.1589 0.0052  452 LYS A C     
3696  O  O     . LYS A 452 ? 1.0356 0.6444 0.6057 -0.0358 0.1614 0.0027  452 LYS A O     
3697  C  CB    . LYS A 452 ? 1.0522 0.6557 0.6135 -0.0278 0.1644 0.0075  452 LYS A CB    
3698  C  CG    . LYS A 452 ? 1.1069 0.7073 0.6634 -0.0289 0.1619 0.0063  452 LYS A CG    
3699  C  CD    . LYS A 452 ? 1.1632 0.7549 0.7107 -0.0264 0.1655 0.0055  452 LYS A CD    
3700  C  CE    . LYS A 452 ? 1.2073 0.7963 0.7503 -0.0271 0.1629 0.0048  452 LYS A CE    
3701  N  NZ    . LYS A 452 ? 1.2383 0.8185 0.7722 -0.0248 0.1666 0.0039  452 LYS A NZ    
3702  N  N     . THR A 453 ? 1.0334 0.6479 0.6061 -0.0373 0.1543 0.0049  453 THR A N     
3703  C  CA    . THR A 453 ? 1.0417 0.6545 0.6137 -0.0417 0.1522 0.0015  453 THR A CA    
3704  C  C     . THR A 453 ? 1.0483 0.6572 0.6149 -0.0432 0.1493 0.0002  453 THR A C     
3705  O  O     . THR A 453 ? 1.0481 0.6599 0.6154 -0.0422 0.1466 0.0029  453 THR A O     
3706  C  CB    . THR A 453 ? 1.0529 0.6729 0.6326 -0.044  0.1492 0.0027  453 THR A CB    
3707  O  OG1   . THR A 453 ? 1.0607 0.6864 0.6438 -0.0441 0.1451 0.0059  453 THR A OG1   
3708  C  CG2   . THR A 453 ? 1.0558 0.6796 0.641  -0.0426 0.152  0.0039  453 THR A CG2   
3709  N  N     . SER A 454 ? 1.0524 0.6552 0.6137 -0.0455 0.1499 -0.0035 454 SER A N     
3710  C  CA    . SER A 454 ? 1.0627 0.6609 0.6182 -0.0469 0.1474 -0.0048 454 SER A CA    
3711  C  C     . SER A 454 ? 1.0634 0.6649 0.6214 -0.05   0.1425 -0.0042 454 SER A C     
3712  O  O     . SER A 454 ? 1.0628 0.6695 0.6268 -0.0515 0.1413 -0.0035 454 SER A O     
3713  C  CB    . SER A 454 ? 1.0853 0.676  0.6343 -0.0481 0.1499 -0.0085 454 SER A CB    
3714  O  OG    . SER A 454 ? 1.1136 0.7047 0.6644 -0.0507 0.1501 -0.0106 454 SER A OG    
3715  N  N     . LYS A 455 ? 1.063  0.6612 0.6161 -0.0509 0.1395 -0.0045 455 LYS A N     
3716  C  CA    . LYS A 455 ? 1.0653 0.665  0.6187 -0.0542 0.1346 -0.004  455 LYS A CA    
3717  C  C     . LYS A 455 ? 1.0629 0.6622 0.6178 -0.0575 0.1342 -0.006  455 LYS A C     
3718  O  O     . LYS A 455 ? 1.071  0.665  0.6221 -0.0579 0.1369 -0.009  455 LYS A O     
3719  C  CB    . LYS A 455 ? 1.0944 0.6874 0.6397 -0.0548 0.1326 -0.0052 455 LYS A CB    
3720  C  CG    . LYS A 455 ? 1.1464 0.739  0.6899 -0.0585 0.1275 -0.005  455 LYS A CG    
3721  C  CD    . LYS A 455 ? 1.2054 0.7899 0.7397 -0.0589 0.1261 -0.0065 455 LYS A CD    
3722  C  CE    . LYS A 455 ? 1.2488 0.8321 0.7803 -0.0628 0.1208 -0.0062 455 LYS A CE    
3723  N  NZ    . LYS A 455 ? 1.2798 0.854  0.8013 -0.0631 0.1198 -0.0078 455 LYS A NZ    
3724  N  N     . GLN A 456 ? 1.0484 0.6537 0.6089 -0.0597 0.131  -0.0042 456 GLN A N     
3725  C  CA    . GLN A 456 ? 1.044  0.6487 0.6057 -0.0628 0.1306 -0.0059 456 GLN A CA    
3726  C  C     . GLN A 456 ? 1.0381 0.6352 0.5918 -0.0657 0.1284 -0.0082 456 GLN A C     
3727  O  O     . GLN A 456 ? 1.0424 0.639  0.5938 -0.0677 0.1242 -0.007  456 GLN A O     
3728  C  CB    . GLN A 456 ? 1.0614 0.6743 0.6309 -0.0646 0.1277 -0.0031 456 GLN A CB    
3729  C  CG    . GLN A 456 ? 1.107  0.7276 0.6843 -0.0614 0.1299 -0.0003 456 GLN A CG    
3730  C  CD    . GLN A 456 ? 1.1668 0.7863 0.7456 -0.0599 0.1346 -0.0022 456 GLN A CD    
3731  O  OE1   . GLN A 456 ? 1.1867 0.8041 0.7652 -0.062  0.1353 -0.0044 456 GLN A OE1   
3732  N  NE2   . GLN A 456 ? 1.1729 0.7934 0.7531 -0.0562 0.1381 -0.0013 456 GLN A NE2   
3733  N  N     . GLN A 457 ? 1.0252 0.6163 0.5746 -0.066  0.1313 -0.0112 457 GLN A N     
3734  C  CA    . GLN A 457 ? 1.0198 0.6027 0.5609 -0.0682 0.1301 -0.0133 457 GLN A CA    
3735  C  C     . GLN A 457 ? 1.0052 0.5845 0.5446 -0.0684 0.1335 -0.0158 457 GLN A C     
3736  O  O     . GLN A 457 ? 1.0046 0.5858 0.5468 -0.0664 0.1374 -0.0165 457 GLN A O     
3737  C  CB    . GLN A 457 ? 1.044  0.6208 0.5777 -0.0669 0.1299 -0.014  457 GLN A CB    
3738  C  CG    . GLN A 457 ? 1.0855 0.6605 0.6181 -0.0637 0.1346 -0.0152 457 GLN A CG    
3739  C  CD    . GLN A 457 ? 1.1417 0.7102 0.6667 -0.0624 0.1345 -0.0158 457 GLN A CD    
3740  O  OE1   . GLN A 457 ? 1.1573 0.7264 0.6824 -0.0599 0.1363 -0.0152 457 GLN A OE1   
3741  N  NE2   . GLN A 457 ? 1.1564 0.718  0.6741 -0.0642 0.1327 -0.017  457 GLN A NE2   
3742  N  N     . ASN A 458 ? 0.993  0.5668 0.5272 -0.0709 0.1321 -0.017  458 ASN A N     
3743  C  CA    . ASN A 458 ? 0.985  0.5553 0.5169 -0.071  0.1354 -0.019  458 ASN A CA    
3744  C  C     . ASN A 458 ? 0.9718 0.5364 0.4979 -0.0688 0.1388 -0.0206 458 ASN A C     
3745  O  O     . ASN A 458 ? 0.9775 0.5377 0.4982 -0.0682 0.1378 -0.0207 458 ASN A O     
3746  C  CB    . ASN A 458 ? 1.004  0.5688 0.5307 -0.0741 0.1331 -0.0195 458 ASN A CB    
3747  C  CG    . ASN A 458 ? 1.0431 0.6129 0.5748 -0.077  0.1294 -0.0178 458 ASN A CG    
3748  O  OD1   . ASN A 458 ? 1.0625 0.6279 0.5892 -0.0802 0.1259 -0.0176 458 ASN A OD1   
3749  N  ND2   . ASN A 458 ? 1.0468 0.6254 0.5879 -0.0762 0.13   -0.0164 458 ASN A ND2   
3750  N  N     . ILE A 459 ? 0.952  0.5172 0.4794 -0.0675 0.1428 -0.0218 459 ILE A N     
3751  C  CA    . ILE A 459 ? 0.9426 0.5036 0.4653 -0.0657 0.1462 -0.0231 459 ILE A CA    
3752  C  C     . ILE A 459 ? 0.9286 0.4858 0.4477 -0.0658 0.1488 -0.0242 459 ILE A C     
3753  O  O     . ILE A 459 ? 0.9273 0.4879 0.4504 -0.0663 0.1497 -0.0242 459 ILE A O     
3754  C  CB    . ILE A 459 ? 0.9453 0.5113 0.4728 -0.0637 0.1491 -0.023  459 ILE A CB    
3755  C  CG1   . ILE A 459 ? 0.9562 0.5239 0.485  -0.0629 0.1472 -0.0217 459 ILE A CG1   
3756  C  CG2   . ILE A 459 ? 0.953  0.5159 0.4767 -0.0624 0.153  -0.0242 459 ILE A CG2   
3757  C  CD1   . ILE A 459 ? 0.9691 0.5412 0.5024 -0.0612 0.1497 -0.0214 459 ILE A CD1   
3758  N  N     . LEU A 460 ? 0.9175 0.4676 0.4288 -0.0651 0.1501 -0.025  460 LEU A N     
3759  C  CA    . LEU A 460 ? 0.9117 0.4577 0.4186 -0.0644 0.1531 -0.0257 460 LEU A CA    
3760  C  C     . LEU A 460 ? 0.9023 0.4452 0.4051 -0.0625 0.1559 -0.0261 460 LEU A C     
3761  O  O     . LEU A 460 ? 0.9082 0.4446 0.4042 -0.0623 0.1547 -0.0262 460 LEU A O     
3762  C  CB    . LEU A 460 ? 0.9196 0.4577 0.419  -0.066  0.1511 -0.0259 460 LEU A CB    
3763  C  CG    . LEU A 460 ? 0.9404 0.4733 0.4343 -0.0648 0.1545 -0.0263 460 LEU A CG    
3764  C  CD1   . LEU A 460 ? 0.9435 0.4827 0.4439 -0.0645 0.1567 -0.0261 460 LEU A CD1   
3765  C  CD2   . LEU A 460 ? 0.9542 0.4772 0.4387 -0.0664 0.1525 -0.0265 460 LEU A CD2   
3766  N  N     . VAL A 461 ? 0.8856 0.4334 0.3925 -0.0612 0.1594 -0.0261 461 VAL A N     
3767  C  CA    . VAL A 461 ? 0.8794 0.4253 0.3831 -0.0597 0.1622 -0.0263 461 VAL A CA    
3768  C  C     . VAL A 461 ? 0.8741 0.4132 0.3702 -0.0585 0.1644 -0.0262 461 VAL A C     
3769  O  O     . VAL A 461 ? 0.8757 0.4154 0.3718 -0.058  0.1664 -0.026  461 VAL A O     
3770  C  CB    . VAL A 461 ? 0.8814 0.4348 0.3915 -0.0593 0.1651 -0.0261 461 VAL A CB    
3771  C  CG1   . VAL A 461 ? 0.8907 0.4424 0.3977 -0.0583 0.1678 -0.0262 461 VAL A CG1   
3772  C  CG2   . VAL A 461 ? 0.8804 0.4394 0.3971 -0.06   0.1633 -0.026  461 VAL A CG2   
3773  N  N     . ASP A 462 ? 0.8658 0.3981 0.3549 -0.0578 0.1643 -0.0264 462 ASP A N     
3774  C  CA    . ASP A 462 ? 0.8668 0.3918 0.3479 -0.0563 0.1668 -0.0261 462 ASP A CA    
3775  C  C     . ASP A 462 ? 0.856  0.3858 0.3399 -0.0547 0.1713 -0.0254 462 ASP A C     
3776  O  O     . ASP A 462 ? 0.8562 0.3906 0.344  -0.0548 0.1724 -0.0254 462 ASP A O     
3777  C  CB    . ASP A 462 ? 0.8939 0.411  0.3673 -0.0558 0.1656 -0.0264 462 ASP A CB    
3778  C  CG    . ASP A 462 ? 0.951  0.4592 0.415  -0.054  0.168  -0.026  462 ASP A CG    
3779  O  OD1   . ASP A 462 ? 0.9606 0.4639 0.42   -0.054  0.1681 -0.0259 462 ASP A OD1   
3780  O  OD2   . ASP A 462 ? 0.976  0.4816 0.4367 -0.0525 0.1701 -0.0258 462 ASP A OD2   
3781  N  N     . PRO A 463 ? 0.8451 0.3737 0.3268 -0.0534 0.1742 -0.0247 463 PRO A N     
3782  C  CA    . PRO A 463 ? 0.8374 0.372  0.3226 -0.0519 0.1784 -0.0235 463 PRO A CA    
3783  C  C     . PRO A 463 ? 0.8389 0.3717 0.3208 -0.0506 0.181  -0.0228 463 PRO A C     
3784  O  O     . PRO A 463 ? 0.8345 0.3732 0.3198 -0.0499 0.1843 -0.0216 463 PRO A O     
3785  C  CB    . PRO A 463 ? 0.8457 0.3784 0.3282 -0.0504 0.1806 -0.0226 463 PRO A CB    
3786  C  CG    . PRO A 463 ? 0.855  0.3828 0.3349 -0.0518 0.1772 -0.0236 463 PRO A CG    
3787  C  CD    . PRO A 463 ? 0.8395 0.3619 0.3158 -0.0532 0.1737 -0.0246 463 PRO A CD    
3788  N  N     . THR A 464 ? 0.8436 0.3686 0.319  -0.0504 0.1796 -0.0234 464 THR A N     
3789  C  CA    . THR A 464 ? 0.8516 0.3741 0.3234 -0.0492 0.1821 -0.0228 464 THR A CA    
3790  C  C     . THR A 464 ? 0.8543 0.3787 0.3287 -0.0507 0.1802 -0.0238 464 THR A C     
3791  O  O     . THR A 464 ? 0.8556 0.3763 0.3282 -0.0515 0.1767 -0.0248 464 THR A O     
3792  C  CB    . THR A 464 ? 0.8753 0.3867 0.3365 -0.0472 0.1828 -0.0224 464 THR A CB    
3793  O  OG1   . THR A 464 ? 0.8904 0.4011 0.3496 -0.0452 0.1859 -0.021  464 THR A OG1   
3794  C  CG2   . THR A 464 ? 0.8818 0.3895 0.3388 -0.0459 0.1849 -0.0219 464 THR A CG2   
3795  N  N     . PRO A 465 ? 0.8528 0.3834 0.3317 -0.0511 0.1826 -0.0233 465 PRO A N     
3796  C  CA    . PRO A 465 ? 0.8577 0.3895 0.3385 -0.0525 0.1813 -0.0242 465 PRO A CA    
3797  C  C     . PRO A 465 ? 0.8718 0.3958 0.3454 -0.0514 0.1817 -0.0243 465 PRO A C     
3798  O  O     . PRO A 465 ? 0.8779 0.3958 0.3452 -0.0496 0.1833 -0.0236 465 PRO A O     
3799  C  CB    . PRO A 465 ? 0.8585 0.3989 0.3455 -0.0537 0.1839 -0.0235 465 PRO A CB    
3800  C  CG    . PRO A 465 ? 0.8613 0.4027 0.347  -0.0522 0.1874 -0.0218 465 PRO A CG    
3801  C  CD    . PRO A 465 ? 0.843  0.3798 0.3252 -0.0505 0.1865 -0.0217 465 PRO A CD    
3802  N  N     . ASN A 466 ? 0.875  0.3987 0.3491 -0.0523 0.1804 -0.0251 466 ASN A N     
3803  C  CA    . ASN A 466 ? 0.89   0.407  0.358  -0.0514 0.1807 -0.0254 466 ASN A CA    
3804  C  C     . ASN A 466 ? 0.892  0.4087 0.3578 -0.0506 0.185  -0.0242 466 ASN A C     
3805  O  O     . ASN A 466 ? 0.8971 0.4065 0.356  -0.0488 0.1861 -0.0238 466 ASN A O     
3806  C  CB    . ASN A 466 ? 0.9133 0.4321 0.3838 -0.0526 0.1794 -0.0262 466 ASN A CB    
3807  C  CG    . ASN A 466 ? 0.9737 0.4853 0.4384 -0.0516 0.1771 -0.0267 466 ASN A CG    
3808  O  OD1   . ASN A 466 ? 0.9952 0.5069 0.4611 -0.0518 0.1737 -0.0271 466 ASN A OD1   
3809  N  ND2   . ASN A 466 ? 0.9876 0.4931 0.446  -0.0504 0.1788 -0.0266 466 ASN A ND2   
3810  N  N     . HIS A 467 ? 0.8867 0.4113 0.3584 -0.052  0.1874 -0.0235 467 HIS A N     
3811  C  CA    . HIS A 467 ? 0.8925 0.419  0.3637 -0.0517 0.1914 -0.0219 467 HIS A CA    
3812  C  C     . HIS A 467 ? 0.881  0.4177 0.3596 -0.0534 0.1932 -0.0208 467 HIS A C     
3813  O  O     . HIS A 467 ? 0.8762 0.418  0.3602 -0.0551 0.1913 -0.0217 467 HIS A O     
3814  C  CB    . HIS A 467 ? 0.9131 0.4361 0.3809 -0.0522 0.1927 -0.0221 467 HIS A CB    
3815  C  CG    . HIS A 467 ? 0.9488 0.4763 0.4208 -0.055  0.1924 -0.023  467 HIS A CG    
3816  N  ND1   . HIS A 467 ? 0.9757 0.5026 0.4491 -0.0556 0.1893 -0.0245 467 HIS A ND1   
3817  C  CD2   . HIS A 467 ? 0.9651 0.4971 0.4395 -0.0572 0.195  -0.0223 467 HIS A CD2   
3818  C  CE1   . HIS A 467 ? 0.9836 0.5139 0.4596 -0.058  0.1903 -0.0248 467 HIS A CE1   
3819  N  NE2   . HIS A 467 ? 0.9818 0.515  0.4582 -0.0593 0.1935 -0.0236 467 HIS A NE2   
3820  N  N     . TYR A 468 ? 0.8746 0.4146 0.3536 -0.0527 0.1967 -0.0187 468 TYR A N     
3821  C  CA    . TYR A 468 ? 0.8684 0.4187 0.3544 -0.0541 0.1984 -0.0173 468 TYR A CA    
3822  C  C     . TYR A 468 ? 0.8617 0.4172 0.3506 -0.0573 0.1997 -0.017  468 TYR A C     
3823  O  O     . TYR A 468 ? 0.8666 0.4193 0.3522 -0.0572 0.2018 -0.0162 468 TYR A O     
3824  C  CB    . TYR A 468 ? 0.8691 0.4211 0.3542 -0.0514 0.2014 -0.0147 468 TYR A CB    
3825  C  CG    . TYR A 468 ? 0.8837 0.4292 0.3646 -0.0486 0.2002 -0.0151 468 TYR A CG    
3826  C  CD1   . TYR A 468 ? 0.8927 0.4418 0.3774 -0.0488 0.1986 -0.0156 468 TYR A CD1   
3827  C  CD2   . TYR A 468 ? 0.9023 0.4372 0.3748 -0.0462 0.2003 -0.0153 468 TYR A CD2   
3828  C  CE1   . TYR A 468 ? 0.9089 0.4514 0.3891 -0.0468 0.1973 -0.0161 468 TYR A CE1   
3829  C  CE2   . TYR A 468 ? 0.9184 0.4464 0.386  -0.0443 0.1988 -0.0159 468 TYR A CE2   
3830  C  CZ    . TYR A 468 ? 0.9287 0.4605 0.4002 -0.0447 0.1973 -0.0163 468 TYR A CZ    
3831  O  OH    . TYR A 468 ? 0.9554 0.4799 0.4215 -0.0432 0.1959 -0.0169 468 TYR A OH    
3832  N  N     . GLN A 469 ? 0.8491 0.4111 0.3437 -0.0602 0.1985 -0.0177 469 GLN A N     
3833  C  CA    . GLN A 469 ? 0.8459 0.4119 0.3425 -0.0638 0.1994 -0.0177 469 GLN A CA    
3834  C  C     . GLN A 469 ? 0.8341 0.4113 0.3372 -0.0661 0.2008 -0.0158 469 GLN A C     
3835  O  O     . GLN A 469 ? 0.8326 0.4144 0.3382 -0.0643 0.2019 -0.014  469 GLN A O     
3836  C  CB    . GLN A 469 ? 0.8679 0.4307 0.3642 -0.0655 0.1967 -0.0202 469 GLN A CB    
3837  C  CG    . GLN A 469 ? 0.9157 0.4695 0.4071 -0.0632 0.1946 -0.0218 469 GLN A CG    
3838  C  CD    . GLN A 469 ? 0.9712 0.5255 0.4654 -0.063  0.1915 -0.0232 469 GLN A CD    
3839  O  OE1   . GLN A 469 ? 0.9911 0.5434 0.485  -0.0609 0.1897 -0.0235 469 GLN A OE1   
3840  N  NE2   . GLN A 469 ? 0.976  0.5326 0.4725 -0.0654 0.1909 -0.0241 469 GLN A NE2   
3841  N  N     . GLU A 470 ? 0.8238 0.4049 0.329  -0.0703 0.2008 -0.0162 470 GLU A N     
3842  C  CA    . GLU A 470 ? 0.8135 0.405  0.3244 -0.0734 0.2016 -0.0146 470 GLU A CA    
3843  C  C     . GLU A 470 ? 0.7971 0.3938 0.3128 -0.0724 0.2001 -0.0147 470 GLU A C     
3844  O  O     . GLU A 470 ? 0.7938 0.3995 0.3141 -0.0729 0.2013 -0.0125 470 GLU A O     
3845  C  CB    . GLU A 470 ? 0.8426 0.4341 0.3528 -0.0781 0.2011 -0.0158 470 GLU A CB    
3846  C  CG    . GLU A 470 ? 0.9023 0.5039 0.4172 -0.0823 0.2019 -0.0141 470 GLU A CG    
3847  C  CD    . GLU A 470 ? 0.9932 0.5933 0.506  -0.0873 0.2015 -0.0154 470 GLU A CD    
3848  O  OE1   . GLU A 470 ? 1.0071 0.6126 0.5229 -0.0906 0.2006 -0.0154 470 GLU A OE1   
3849  O  OE2   . GLU A 470 ? 1.027  0.6199 0.5345 -0.0881 0.2024 -0.0162 470 GLU A OE2   
3850  N  N     . ASN A 471 ? 0.785  0.3768 0.3    -0.0708 0.1977 -0.0169 471 ASN A N     
3851  C  CA    . ASN A 471 ? 0.7759 0.3721 0.2953 -0.0698 0.1963 -0.017  471 ASN A CA    
3852  C  C     . ASN A 471 ? 0.7707 0.3686 0.2906 -0.0662 0.1978 -0.0151 471 ASN A C     
3853  O  O     . ASN A 471 ? 0.7721 0.3771 0.2964 -0.0659 0.1982 -0.0138 471 ASN A O     
3854  C  CB    . ASN A 471 ? 0.7828 0.3736 0.3014 -0.0691 0.1935 -0.0194 471 ASN A CB    
3855  C  CG    . ASN A 471 ? 0.804  0.4005 0.3277 -0.0704 0.1922 -0.0199 471 ASN A CG    
3856  O  OD1   . ASN A 471 ? 0.8165 0.4113 0.3404 -0.0719 0.1907 -0.0214 471 ASN A OD1   
3857  N  ND2   . ASN A 471 ? 0.8041 0.4073 0.3318 -0.0695 0.193  -0.0183 471 ASN A ND2   
3858  N  N     . ASP A 472 ? 0.7618 0.3529 0.2766 -0.0635 0.1987 -0.0147 472 ASP A N     
3859  C  CA    . ASP A 472 ? 0.758  0.349  0.2716 -0.0598 0.2006 -0.0128 472 ASP A CA    
3860  C  C     . ASP A 472 ? 0.7462 0.3455 0.2626 -0.0599 0.2039 -0.0095 472 ASP A C     
3861  O  O     . ASP A 472 ? 0.7414 0.3452 0.2598 -0.0576 0.2054 -0.0074 472 ASP A O     
3862  C  CB    . ASP A 472 ? 0.789  0.3693 0.2954 -0.057  0.2005 -0.0135 472 ASP A CB    
3863  C  CG    . ASP A 472 ? 0.856  0.4297 0.3605 -0.0569 0.1969 -0.0163 472 ASP A CG    
3864  O  OD1   . ASP A 472 ? 0.8629 0.438  0.3697 -0.0562 0.1955 -0.0168 472 ASP A OD1   
3865  O  OD2   . ASP A 472 ? 0.895  0.4627 0.3961 -0.0576 0.1956 -0.0178 472 ASP A OD2   
3866  N  N     . VAL A 473 ? 0.7411 0.343  0.2578 -0.0628 0.205  -0.0087 473 VAL A N     
3867  C  CA    . VAL A 473 ? 0.7398 0.3511 0.26   -0.0636 0.2079 -0.0052 473 VAL A CA    
3868  C  C     . VAL A 473 ? 0.7355 0.3576 0.2626 -0.0654 0.2073 -0.0043 473 VAL A C     
3869  O  O     . VAL A 473 ? 0.7357 0.365  0.2659 -0.0634 0.2094 -0.0012 473 VAL A O     
3870  C  CB    . VAL A 473 ? 0.7491 0.3611 0.2684 -0.0673 0.2088 -0.0049 473 VAL A CB    
3871  C  CG1   . VAL A 473 ? 0.7511 0.3746 0.2751 -0.0689 0.2114 -0.001  473 VAL A CG1   
3872  C  CG2   . VAL A 473 ? 0.7604 0.3619 0.2728 -0.0652 0.2096 -0.0057 473 VAL A CG2   
3873  N  N     . ASP A 474 ? 0.7297 0.3519 0.2586 -0.0687 0.2045 -0.0068 474 ASP A N     
3874  C  CA    . ASP A 474 ? 0.7258 0.3567 0.2604 -0.0706 0.2035 -0.0065 474 ASP A CA    
3875  C  C     . ASP A 474 ? 0.7257 0.358  0.2621 -0.0667 0.2035 -0.006  474 ASP A C     
3876  O  O     . ASP A 474 ? 0.7226 0.3642 0.2637 -0.0666 0.2045 -0.0037 474 ASP A O     
3877  C  CB    . ASP A 474 ? 0.7441 0.3723 0.2786 -0.0743 0.2007 -0.0096 474 ASP A CB    
3878  C  CG    . ASP A 474 ? 0.7904 0.4214 0.3248 -0.0794 0.2009 -0.0094 474 ASP A CG    
3879  O  OD1   . ASP A 474 ? 0.7902 0.4309 0.3285 -0.0818 0.2019 -0.0069 474 ASP A OD1   
3880  O  OD2   . ASP A 474 ? 0.8212 0.4444 0.3511 -0.0809 0.2001 -0.0115 474 ASP A OD2   
3881  N  N     . THR A 475 ? 0.7266 0.3497 0.2591 -0.0636 0.2025 -0.0079 475 THR A N     
3882  C  CA    . THR A 475 ? 0.7269 0.3493 0.2598 -0.06   0.2026 -0.0076 475 THR A CA    
3883  C  C     . THR A 475 ? 0.7276 0.3541 0.2603 -0.0566 0.2062 -0.004  475 THR A C     
3884  O  O     . THR A 475 ? 0.7228 0.3556 0.259  -0.055  0.2072 -0.0023 475 THR A O     
3885  C  CB    . THR A 475 ? 0.744  0.355  0.2716 -0.058  0.2007 -0.0102 475 THR A CB    
3886  O  OG1   . THR A 475 ? 0.7537 0.3624 0.2823 -0.0606 0.1976 -0.0131 475 THR A OG1   
3887  C  CG2   . THR A 475 ? 0.7504 0.359  0.2768 -0.0544 0.2011 -0.0098 475 THR A CG2   
3888  N  N     . VAL A 476 ? 0.733  0.356  0.2618 -0.0553 0.2083 -0.0025 476 VAL A N     
3889  C  CA    . VAL A 476 ? 0.7414 0.3676 0.2695 -0.0516 0.2122 0.0014  476 VAL A CA    
3890  C  C     . VAL A 476 ? 0.7437 0.384  0.2787 -0.0533 0.2139 0.0048  476 VAL A C     
3891  O  O     . VAL A 476 ? 0.7448 0.391  0.2821 -0.0504 0.2161 0.0076  476 VAL A O     
3892  C  CB    . VAL A 476 ? 0.7544 0.3728 0.2762 -0.0499 0.2141 0.002   476 VAL A CB    
3893  C  CG1   . VAL A 476 ? 0.7588 0.382  0.2806 -0.0464 0.2186 0.0066  476 VAL A CG1   
3894  C  CG2   . VAL A 476 ? 0.7674 0.3722 0.2819 -0.0474 0.2126 -0.0007 476 VAL A CG2   
3895  N  N     . ILE A 477 ? 0.7438 0.3893 0.2819 -0.0582 0.2128 0.0045  477 ILE A N     
3896  C  CA    . ILE A 477 ? 0.7482 0.4075 0.2928 -0.0609 0.2138 0.0077  477 ILE A CA    
3897  C  C     . ILE A 477 ? 0.7536 0.4199 0.3031 -0.061  0.2125 0.0077  477 ILE A C     
3898  O  O     . ILE A 477 ? 0.7514 0.4278 0.3052 -0.0596 0.2145 0.0114  477 ILE A O     
3899  C  CB    . ILE A 477 ? 0.7566 0.418  0.3022 -0.0668 0.2124 0.0068  477 ILE A CB    
3900  C  CG1   . ILE A 477 ? 0.7766 0.4338 0.3183 -0.0664 0.2146 0.0081  477 ILE A CG1   
3901  C  CG2   . ILE A 477 ? 0.7558 0.4309 0.308  -0.071  0.2121 0.0092  477 ILE A CG2   
3902  C  CD1   . ILE A 477 ? 0.7915 0.4566 0.3353 -0.0635 0.2186 0.0132  477 ILE A CD1   
3903  N  N     . TYR A 478 ? 0.7582 0.4191 0.3071 -0.0624 0.2094 0.0038  478 TYR A N     
3904  C  CA    . TYR A 478 ? 0.7656 0.4317 0.3186 -0.0625 0.208  0.0034  478 TYR A CA    
3905  C  C     . TYR A 478 ? 0.7776 0.444  0.3302 -0.057  0.2103 0.0054  478 TYR A C     
3906  O  O     . TYR A 478 ? 0.775  0.4509 0.3321 -0.0562 0.2113 0.0078  478 TYR A O     
3907  C  CB    . TYR A 478 ? 0.7686 0.4271 0.3201 -0.0645 0.2046 -0.0011 478 TYR A CB    
3908  C  CG    . TYR A 478 ? 0.775  0.4384 0.3306 -0.065  0.2031 -0.0017 478 TYR A CG    
3909  C  CD1   . TYR A 478 ? 0.7821 0.4543 0.3421 -0.0691 0.2021 -0.0012 478 TYR A CD1   
3910  C  CD2   . TYR A 478 ? 0.7874 0.4464 0.3422 -0.0615 0.2027 -0.0029 478 TYR A CD2   
3911  C  CE1   . TYR A 478 ? 0.7908 0.4673 0.3543 -0.0694 0.2008 -0.0017 478 TYR A CE1   
3912  C  CE2   . TYR A 478 ? 0.7969 0.4603 0.3554 -0.0618 0.2016 -0.0034 478 TYR A CE2   
3913  C  CZ    . TYR A 478 ? 0.8051 0.4771 0.3679 -0.0656 0.2007 -0.0028 478 TYR A CZ    
3914  O  OH    . TYR A 478 ? 0.8235 0.4996 0.3897 -0.0658 0.1996 -0.0033 478 TYR A OH    
3915  N  N     . SER A 479 ? 0.7881 0.444  0.3349 -0.0532 0.2112 0.0045  479 SER A N     
3916  C  CA    . SER A 479 ? 0.8028 0.4568 0.3475 -0.0479 0.2135 0.0061  479 SER A CA    
3917  C  C     . SER A 479 ? 0.8113 0.4742 0.358  -0.045  0.2177 0.0112  479 SER A C     
3918  O  O     . SER A 479 ? 0.8109 0.4795 0.3599 -0.0423 0.2193 0.0135  479 SER A O     
3919  C  CB    . SER A 479 ? 0.8303 0.4702 0.3672 -0.0451 0.2135 0.0041  479 SER A CB    
3920  O  OG    . SER A 479 ? 0.8627 0.4955 0.3983 -0.0477 0.2096 -0.0002 479 SER A OG    
3921  N  N     . ILE A 480 ? 0.8166 0.4809 0.3625 -0.0455 0.2194 0.0133  480 ILE A N     
3922  C  CA    . ILE A 480 ? 0.8237 0.4969 0.3716 -0.0426 0.2236 0.0187  480 ILE A CA    
3923  C  C     . ILE A 480 ? 0.826  0.5151 0.3823 -0.0449 0.2236 0.0216  480 ILE A C     
3924  O  O     . ILE A 480 ? 0.8265 0.5225 0.3849 -0.0411 0.2264 0.0254  480 ILE A O     
3925  C  CB    . ILE A 480 ? 0.8328 0.5037 0.3782 -0.0433 0.2252 0.02    480 ILE A CB    
3926  C  CG1   . ILE A 480 ? 0.8532 0.5089 0.3895 -0.0394 0.2263 0.0184  480 ILE A CG1   
3927  C  CG2   . ILE A 480 ? 0.8345 0.5178 0.3841 -0.0419 0.229  0.0259  480 ILE A CG2   
3928  C  CD1   . ILE A 480 ? 0.8718 0.5231 0.4048 -0.0403 0.2272 0.0187  480 ILE A CD1   
3929  N  N     . PHE A 481 ? 0.8252 0.5196 0.3856 -0.0511 0.2205 0.02    481 PHE A N     
3930  C  CA    . PHE A 481 ? 0.8257 0.535  0.3934 -0.0541 0.22   0.0228  481 PHE A CA    
3931  C  C     . PHE A 481 ? 0.8357 0.5481 0.4065 -0.0545 0.2179 0.0212  481 PHE A C     
3932  O  O     . PHE A 481 ? 0.8349 0.5599 0.4114 -0.0558 0.218  0.0241  481 PHE A O     
3933  C  CB    . PHE A 481 ? 0.8197 0.5332 0.3896 -0.0609 0.2179 0.0222  481 PHE A CB    
3934  C  CG    . PHE A 481 ? 0.8225 0.5377 0.3915 -0.0606 0.2207 0.0253  481 PHE A CG    
3935  C  CD1   . PHE A 481 ? 0.8244 0.5521 0.3978 -0.0588 0.2238 0.0312  481 PHE A CD1   
3936  C  CD2   . PHE A 481 ? 0.835  0.5395 0.3988 -0.0619 0.2202 0.0227  481 PHE A CD2   
3937  C  CE1   . PHE A 481 ? 0.8315 0.561  0.4044 -0.0584 0.2266 0.0344  481 PHE A CE1   
3938  C  CE2   . PHE A 481 ? 0.8431 0.5489 0.4059 -0.0615 0.2229 0.0257  481 PHE A CE2   
3939  C  CZ    . PHE A 481 ? 0.8347 0.5531 0.4022 -0.0598 0.2261 0.0315  481 PHE A CZ    
3940  N  N     . LYS A 482 ? 0.842  0.5435 0.4091 -0.0534 0.2161 0.017   482 LYS A N     
3941  C  CA    . LYS A 482 ? 0.8454 0.5494 0.4152 -0.0536 0.2143 0.0155  482 LYS A CA    
3942  C  C     . LYS A 482 ? 0.8525 0.5535 0.4203 -0.0475 0.2167 0.0166  482 LYS A C     
3943  O  O     . LYS A 482 ? 0.8541 0.5614 0.4253 -0.0465 0.2167 0.0175  482 LYS A O     
3944  C  CB    . LYS A 482 ? 0.868  0.5639 0.4363 -0.0575 0.2102 0.0102  482 LYS A CB    
3945  C  CG    . LYS A 482 ? 0.9112 0.6112 0.4831 -0.0591 0.2081 0.0088  482 LYS A CG    
3946  C  CD    . LYS A 482 ? 0.9555 0.6693 0.5332 -0.0625 0.2078 0.0115  482 LYS A CD    
3947  C  CE    . LYS A 482 ? 0.9961 0.7127 0.5766 -0.0648 0.2053 0.0096  482 LYS A CE    
3948  N  NZ    . LYS A 482 ? 1.0164 0.7466 0.602  -0.0681 0.2049 0.0126  482 LYS A NZ    
3949  N  N     . TYR A 483 ? 0.8557 0.5465 0.4172 -0.0433 0.2188 0.0165  483 TYR A N     
3950  C  CA    . TYR A 483 ? 0.862  0.5477 0.42   -0.0377 0.2212 0.0172  483 TYR A CA    
3951  C  C     . TYR A 483 ? 0.8701 0.5569 0.4253 -0.0321 0.2262 0.0219  483 TYR A C     
3952  O  O     . TYR A 483 ? 0.87   0.5586 0.4245 -0.0276 0.2289 0.0243  483 TYR A O     
3953  C  CB    . TYR A 483 ? 0.8666 0.5374 0.4185 -0.0374 0.2191 0.0126  483 TYR A CB    
3954  C  CG    . TYR A 483 ? 0.8725 0.5427 0.4274 -0.0419 0.2146 0.0085  483 TYR A CG    
3955  C  CD1   . TYR A 483 ? 0.88   0.5569 0.4396 -0.0425 0.2137 0.0085  483 TYR A CD1   
3956  C  CD2   . TYR A 483 ? 0.8851 0.5483 0.4381 -0.0455 0.2116 0.005   483 TYR A CD2   
3957  C  CE1   . TYR A 483 ? 0.8908 0.5671 0.453  -0.0465 0.21   0.005   483 TYR A CE1   
3958  C  CE2   . TYR A 483 ? 0.8956 0.5582 0.4511 -0.0493 0.208  0.0017  483 TYR A CE2   
3959  C  CZ    . TYR A 483 ? 0.9054 0.5745 0.4655 -0.0498 0.2072 0.0017  483 TYR A CZ    
3960  O  OH    . TYR A 483 ? 0.9272 0.5955 0.4895 -0.0532 0.204  -0.0014 483 TYR A OH    
3961  N  N     . ILE A 484 ? 0.8767 0.5621 0.4297 -0.032  0.2277 0.0235  484 ILE A N     
3962  C  CA    . ILE A 484 ? 0.8912 0.5767 0.4409 -0.0263 0.2329 0.0282  484 ILE A CA    
3963  C  C     . ILE A 484 ? 0.895  0.5973 0.4517 -0.0257 0.2355 0.034   484 ILE A C     
3964  O  O     . ILE A 484 ? 0.895  0.6023 0.4523 -0.0207 0.239  0.0378  484 ILE A O     
3965  C  CB    . ILE A 484 ? 0.9057 0.5799 0.4484 -0.0255 0.2338 0.0273  484 ILE A CB    
3966  C  CG1   . ILE A 484 ? 0.9272 0.5852 0.4625 -0.0255 0.2313 0.0221  484 ILE A CG1   
3967  C  CG2   . ILE A 484 ? 0.9129 0.5873 0.4519 -0.0194 0.2395 0.0325  484 ILE A CG2   
3968  C  CD1   . ILE A 484 ? 0.9506 0.5977 0.4795 -0.0258 0.2311 0.0204  484 ILE A CD1   
3969  N  N     . VAL A 485 ? 0.8967 0.6077 0.4587 -0.0306 0.234  0.0349  485 VAL A N     
3970  C  CA    . VAL A 485 ? 0.9006 0.6283 0.4697 -0.0309 0.2361 0.0406  485 VAL A CA    
3971  C  C     . VAL A 485 ? 0.9097 0.6498 0.4857 -0.0324 0.2346 0.0418  485 VAL A C     
3972  O  O     . VAL A 485 ? 0.9108 0.6519 0.4895 -0.0377 0.2303 0.0381  485 VAL A O     
3973  C  CB    . VAL A 485 ? 0.9031 0.6356 0.475  -0.0364 0.2347 0.041   485 VAL A CB    
3974  C  CG1   . VAL A 485 ? 0.9001 0.6508 0.4798 -0.0374 0.2366 0.0472  485 VAL A CG1   
3975  C  CG2   . VAL A 485 ? 0.9138 0.6343 0.4787 -0.0343 0.2367 0.0403  485 VAL A CG2   
3976  N  N     . PRO A 486 ? 0.9145 0.6641 0.493  -0.0273 0.2385 0.0472  486 PRO A N     
3977  C  CA    . PRO A 486 ? 0.9187 0.68   0.5034 -0.028  0.2374 0.0486  486 PRO A CA    
3978  C  C     . PRO A 486 ? 0.9254 0.7024 0.5184 -0.0345 0.2345 0.0504  486 PRO A C     
3979  O  O     . PRO A 486 ? 0.9234 0.706  0.5188 -0.0376 0.2346 0.0525  486 PRO A O     
3980  C  CB    . PRO A 486 ? 0.9243 0.6903 0.5083 -0.02   0.2429 0.0544  486 PRO A CB    
3981  C  CG    . PRO A 486 ? 0.9279 0.6926 0.5093 -0.0172 0.2467 0.058   486 PRO A CG    
3982  C  CD    . PRO A 486 ? 0.9117 0.6607 0.4868 -0.0201 0.2443 0.0523  486 PRO A CD    
3983  N  N     . ASN A 487 ? 0.9314 0.7154 0.5287 -0.0366 0.232  0.0497  487 ASN A N     
3984  C  CA    . ASN A 487 ? 0.9388 0.7371 0.5433 -0.0431 0.2288 0.0509  487 ASN A CA    
3985  C  C     . ASN A 487 ? 0.9515 0.7465 0.5557 -0.0507 0.2251 0.0475  487 ASN A C     
3986  O  O     . ASN A 487 ? 0.9472 0.753  0.5557 -0.0552 0.2245 0.0505  487 ASN A O     
3987  C  CB    . ASN A 487 ? 0.9459 0.7622 0.5568 -0.0411 0.2317 0.0585  487 ASN A CB    
3988  C  CG    . ASN A 487 ? 0.9848 0.8054 0.5963 -0.0338 0.2351 0.062   487 ASN A CG    
3989  O  OD1   . ASN A 487 ? 0.9985 0.8264 0.6137 -0.0347 0.2334 0.0621  487 ASN A OD1   
3990  N  ND2   . ASN A 487 ? 0.9928 0.8081 0.6001 -0.0262 0.2403 0.0648  487 ASN A ND2   
3991  N  N     . CYS A 488 ? 0.9655 0.7452 0.5642 -0.0522 0.2228 0.0413  488 CYS A N     
3992  C  CA    . CYS A 488 ? 0.9814 0.7547 0.5781 -0.0586 0.2195 0.0372  488 CYS A CA    
3993  C  C     . CYS A 488 ? 0.9921 0.7615 0.5887 -0.0633 0.2151 0.0323  488 CYS A C     
3994  O  O     . CYS A 488 ? 0.9948 0.7618 0.5911 -0.0605 0.2148 0.0307  488 CYS A O     
3995  C  CB    . CYS A 488 ? 1.0011 0.7595 0.5911 -0.056  0.2209 0.0346  488 CYS A CB    
3996  S  SG    . CYS A 488 ? 1.0562 0.8179 0.6458 -0.0549 0.2244 0.0391  488 CYS A SG    
3997  N  N     . PHE A 489 ? 0.9974 0.7654 0.5935 -0.0702 0.2121 0.0297  489 PHE A N     
3998  C  CA    . PHE A 489 ? 1.0105 0.7742 0.6058 -0.0747 0.2082 0.0252  489 PHE A CA    
3999  C  C     . PHE A 489 ? 1.0274 0.7803 0.6181 -0.0794 0.206  0.021   489 PHE A C     
4000  O  O     . PHE A 489 ? 1.0297 0.7852 0.6203 -0.0831 0.2061 0.0223  489 PHE A O     
4001  C  CB    . PHE A 489 ? 1.0037 0.7811 0.6042 -0.0791 0.2063 0.0276  489 PHE A CB    
4002  C  CG    . PHE A 489 ? 1.014  0.7867 0.6131 -0.0833 0.2027 0.0232  489 PHE A CG    
4003  C  CD1   . PHE A 489 ? 1.0257 0.7932 0.6241 -0.0797 0.2023 0.0208  489 PHE A CD1   
4004  C  CD2   . PHE A 489 ? 1.0236 0.7965 0.6216 -0.0909 0.1998 0.0216  489 PHE A CD2   
4005  C  CE1   . PHE A 489 ? 1.0361 0.799  0.633  -0.0833 0.1992 0.017   489 PHE A CE1   
4006  C  CE2   . PHE A 489 ? 1.0353 0.8029 0.6311 -0.0943 0.1968 0.0178  489 PHE A CE2   
4007  C  CZ    . PHE A 489 ? 1.0343 0.7972 0.6299 -0.0904 0.1966 0.0156  489 PHE A CZ    
4008  N  N     . SER A 490 ? 1.0363 0.7772 0.6231 -0.0791 0.2041 0.016   490 SER A N     
4009  C  CA    . SER A 490 ? 1.0503 0.7804 0.6324 -0.0829 0.2022 0.012   490 SER A CA    
4010  C  C     . SER A 490 ? 1.0557 0.7866 0.6377 -0.0892 0.199  0.0098  490 SER A C     
4011  O  O     . SER A 490 ? 1.0604 0.7846 0.6407 -0.089  0.1973 0.0063  490 SER A O     
4012  C  CB    . SER A 490 ? 1.0738 0.7903 0.6515 -0.0788 0.2021 0.0083  490 SER A CB    
4013  O  OG    . SER A 490 ? 1.1078 0.8141 0.6811 -0.082  0.2003 0.0045  490 SER A OG    
4014  N  N     . GLY A 491 ? 1.0539 0.7929 0.6374 -0.0947 0.1984 0.0119  491 GLY A N     
4015  C  CA    . GLY A 491 ? 1.0632 0.8023 0.6454 -0.1013 0.1955 0.01    491 GLY A CA    
4016  C  C     . GLY A 491 ? 1.0769 0.8022 0.6527 -0.1039 0.1942 0.0055  491 GLY A C     
4017  O  O     . GLY A 491 ? 1.0838 0.8033 0.6569 -0.1061 0.1922 0.0024  491 GLY A O     
4018  N  N     . MET A 492 ? 1.0799 0.7995 0.6529 -0.1032 0.1956 0.0053  492 MET A N     
4019  C  CA    . MET A 492 ? 1.0927 0.7992 0.6593 -0.1052 0.1947 0.0014  492 MET A CA    
4020  C  C     . MET A 492 ? 1.0972 0.7943 0.6614 -0.0996 0.1962 0       492 MET A C     
4021  O  O     . MET A 492 ? 1.0955 0.796  0.6614 -0.0961 0.1984 0.0026  492 MET A O     
4022  C  CB    . MET A 492 ? 1.105  0.8124 0.669  -0.1116 0.1946 0.0022  492 MET A CB    
4023  C  CG    . MET A 492 ? 1.1373 0.8426 0.698  -0.1181 0.1923 0.0003  492 MET A CG    
4024  S  SD    . MET A 492 ? 1.2049 0.8982 0.7572 -0.1232 0.1922 -0.0024 492 MET A SD    
4025  C  CE    . MET A 492 ? 1.189  0.8678 0.7375 -0.1168 0.1926 -0.0062 492 MET A CE    
4026  N  N     . CYS A 493 ? 1.1018 0.7871 0.6615 -0.0988 0.195  -0.0039 493 CYS A N     
4027  C  CA    . CYS A 493 ? 1.1123 0.7879 0.6689 -0.0943 0.1959 -0.0055 493 CYS A CA    
4028  C  C     . CYS A 493 ? 1.1222 0.786  0.6734 -0.0958 0.1944 -0.0093 493 CYS A C     
4029  O  O     . CYS A 493 ? 1.1255 0.7856 0.6765 -0.0949 0.193  -0.0114 493 CYS A O     
4030  C  CB    . CYS A 493 ? 1.1205 0.7964 0.6797 -0.0883 0.1964 -0.0052 493 CYS A CB    
4031  S  SG    . CYS A 493 ? 1.1645 0.8324 0.7205 -0.0828 0.1982 -0.0052 493 CYS A SG    
4032  N  N     . ASN A 494 ? 1.1253 0.7835 0.6721 -0.0979 0.195  -0.0099 494 ASN A N     
4033  C  CA    . ASN A 494 ? 1.137  0.7839 0.6779 -0.0991 0.1941 -0.013  494 ASN A CA    
4034  C  C     . ASN A 494 ? 1.1444 0.7828 0.6816 -0.0958 0.1951 -0.0139 494 ASN A C     
4035  O  O     . ASN A 494 ? 1.1488 0.7835 0.6822 -0.098  0.196  -0.0139 494 ASN A O     
4036  C  CB    . ASN A 494 ? 1.1519 0.7983 0.6893 -0.1056 0.1939 -0.0133 494 ASN A CB    
4037  C  CG    . ASN A 494 ? 1.1942 0.8377 0.7297 -0.1082 0.1922 -0.0153 494 ASN A CG    
4038  O  OD1   . ASN A 494 ? 1.2043 0.8553 0.7434 -0.1098 0.1914 -0.0144 494 ASN A OD1   
4039  N  ND2   . ASN A 494 ? 1.2082 0.8408 0.7379 -0.1083 0.192  -0.0179 494 ASN A ND2   
4040  N  N     . PRO A 495 ? 1.1442 0.7789 0.6822 -0.0906 0.1947 -0.0148 495 PRO A N     
4041  C  CA    . PRO A 495 ? 1.1502 0.7764 0.6841 -0.0875 0.1952 -0.0157 495 PRO A CA    
4042  C  C     . PRO A 495 ? 1.1594 0.7754 0.688  -0.0885 0.1942 -0.0184 495 PRO A C     
4043  O  O     . PRO A 495 ? 1.1603 0.7755 0.6881 -0.0913 0.1933 -0.0196 495 PRO A O     
4044  C  CB    . PRO A 495 ? 1.1568 0.7829 0.6931 -0.0824 0.1949 -0.0156 495 PRO A CB    
4045  C  CG    . PRO A 495 ? 1.1557 0.7909 0.6975 -0.0827 0.1946 -0.0143 495 PRO A CG    
4046  C  CD    . PRO A 495 ? 1.135  0.7726 0.6769 -0.0876 0.1938 -0.0149 495 PRO A CD    
4047  N  N     . PRO A 496 ? 1.1652 0.773  0.6894 -0.0861 0.1945 -0.0193 496 PRO A N     
4048  C  CA    . PRO A 496 ? 1.1729 0.7716 0.6921 -0.0866 0.1937 -0.0216 496 PRO A CA    
4049  C  C     . PRO A 496 ? 1.1765 0.7732 0.6971 -0.0851 0.1919 -0.0231 496 PRO A C     
4050  O  O     . PRO A 496 ? 1.1772 0.7745 0.7005 -0.0816 0.1908 -0.0232 496 PRO A O     
4051  C  CB    . PRO A 496 ? 1.1846 0.7764 0.7    -0.0835 0.1942 -0.0218 496 PRO A CB    
4052  C  CG    . PRO A 496 ? 1.1859 0.7828 0.7031 -0.0827 0.1958 -0.0196 496 PRO A CG    
4053  C  CD    . PRO A 496 ? 1.1598 0.7661 0.6831 -0.0827 0.1956 -0.0182 496 PRO A CD    
4054  N  N     . GLY A 497 ? 1.177  0.7713 0.6954 -0.0879 0.1916 -0.0242 497 GLY A N     
4055  C  CA    . GLY A 497 ? 1.1829 0.7751 0.7022 -0.0866 0.1903 -0.0254 497 GLY A CA    
4056  C  C     . GLY A 497 ? 1.1818 0.7819 0.7067 -0.0872 0.1895 -0.0248 497 GLY A C     
4057  O  O     . GLY A 497 ? 1.1828 0.783  0.7105 -0.0847 0.1883 -0.0253 497 GLY A O     
4058  N  N     . GLY A 498 ? 1.1784 0.7853 0.705  -0.0905 0.1903 -0.0235 498 GLY A N     
4059  C  CA    . GLY A 498 ? 1.1806 0.7957 0.7124 -0.0911 0.1898 -0.0226 498 GLY A CA    
4060  C  C     . GLY A 498 ? 1.1851 0.8009 0.7153 -0.0953 0.1895 -0.0231 498 GLY A C     
4061  O  O     . GLY A 498 ? 1.1889 0.7997 0.7137 -0.0987 0.19   -0.0238 498 GLY A O     
4062  N  N     . ASP A 499 ? 1.1825 0.8041 0.7171 -0.095  0.1887 -0.0227 499 ASP A N     
4063  C  CA    . ASP A 499 ? 1.1879 0.8107 0.7214 -0.0986 0.1882 -0.023  499 ASP A CA    
4064  C  C     . ASP A 499 ? 1.1908 0.8196 0.7237 -0.104  0.1886 -0.0216 499 ASP A C     
4065  O  O     . ASP A 499 ? 1.1933 0.827  0.728  -0.1044 0.1893 -0.02   499 ASP A O     
4066  C  CB    . ASP A 499 ? 1.2021 0.8301 0.741  -0.0962 0.1874 -0.0228 499 ASP A CB    
4067  C  CG    . ASP A 499 ? 1.2556 0.8781 0.7951 -0.092  0.1868 -0.0241 499 ASP A CG    
4068  O  OD1   . ASP A 499 ? 1.2647 0.8817 0.8027 -0.0893 0.1868 -0.0247 499 ASP A OD1   
4069  O  OD2   . ASP A 499 ? 1.2813 0.9052 0.8229 -0.0913 0.1862 -0.0244 499 ASP A OD2   
4070  N  N     . TRP A 500 ? 1.1888 0.8173 0.719  -0.1082 0.1881 -0.022  500 TRP A N     
4071  C  CA    . TRP A 500 ? 1.1909 0.8257 0.7204 -0.114  0.188  -0.0206 500 TRP A CA    
4072  C  C     . TRP A 500 ? 1.1909 0.837  0.7276 -0.1129 0.1872 -0.0188 500 TRP A C     
4073  O  O     . TRP A 500 ? 1.1928 0.8396 0.7297 -0.1136 0.1863 -0.0193 500 TRP A O     
4074  C  CB    . TRP A 500 ? 1.1931 0.8208 0.7152 -0.1188 0.1877 -0.022  500 TRP A CB    
4075  C  CG    . TRP A 500 ? 1.2006 0.822  0.7156 -0.1235 0.1885 -0.0224 500 TRP A CG    
4076  C  CD1   . TRP A 500 ? 1.2127 0.834  0.7227 -0.1304 0.1882 -0.0222 500 TRP A CD1   
4077  C  CD2   . TRP A 500 ? 1.2044 0.8179 0.7156 -0.1217 0.1898 -0.0233 500 TRP A CD2   
4078  N  NE1   . TRP A 500 ? 1.2206 0.8344 0.724  -0.133  0.1894 -0.0228 500 TRP A NE1   
4079  C  CE2   . TRP A 500 ? 1.2177 0.8266 0.7218 -0.1276 0.1905 -0.0235 500 TRP A CE2   
4080  C  CE3   . TRP A 500 ? 1.2102 0.82   0.723  -0.1158 0.1904 -0.0239 500 TRP A CE3   
4081  C  CZ2   . TRP A 500 ? 1.2286 0.8293 0.7273 -0.1275 0.1919 -0.0243 500 TRP A CZ2   
4082  C  CZ3   . TRP A 500 ? 1.2243 0.8264 0.7319 -0.1157 0.1916 -0.0246 500 TRP A CZ3   
4083  C  CH2   . TRP A 500 ? 1.2291 0.8266 0.7298 -0.1213 0.1925 -0.0248 500 TRP A CH2   
4084  N  N     . SER A 501 ? 1.1876 0.8419 0.7298 -0.1106 0.1878 -0.0166 501 SER A N     
4085  C  CA    . SER A 501 ? 1.1888 0.8537 0.7379 -0.1086 0.1876 -0.0146 501 SER A CA    
4086  C  C     . SER A 501 ? 1.1881 0.8626 0.7387 -0.1137 0.1867 -0.0127 501 SER A C     
4087  O  O     . SER A 501 ? 1.188  0.8658 0.7405 -0.1137 0.1858 -0.0127 501 SER A O     
4088  C  CB    . SER A 501 ? 1.2032 0.8728 0.7565 -0.1043 0.1889 -0.0127 501 SER A CB    
4089  O  OG    . SER A 501 ? 1.2252 0.905  0.7846 -0.102  0.1892 -0.0104 501 SER A OG    
4090  N  N     . GLY A 502 ? 1.1855 0.8644 0.7353 -0.1182 0.187  -0.0109 502 GLY A N     
4091  C  CA    . GLY A 502 ? 1.1863 0.8756 0.738  -0.1235 0.1861 -0.0085 502 GLY A CA    
4092  C  C     . GLY A 502 ? 1.1822 0.8843 0.7406 -0.1221 0.1871 -0.0045 502 GLY A C     
4093  O  O     . GLY A 502 ? 1.1834 0.8857 0.7447 -0.1164 0.1887 -0.0038 502 GLY A O     
4094  N  N     . LEU A 503 ? 1.176  0.8887 0.7364 -0.1273 0.1863 -0.0017 503 LEU A N     
4095  C  CA    . LEU A 503 ? 1.1735 0.8995 0.7405 -0.1261 0.1876 0.0028  503 LEU A CA    
4096  C  C     . LEU A 503 ? 1.1694 0.9083 0.7425 -0.1253 0.1869 0.0056  503 LEU A C     
4097  O  O     . LEU A 503 ? 1.1688 0.9114 0.741  -0.1306 0.1848 0.0058  503 LEU A O     
4098  C  CB    . LEU A 503 ? 1.1754 0.9053 0.7409 -0.1325 0.1876 0.0048  503 LEU A CB    
4099  C  CG    . LEU A 503 ? 1.1854 0.9305 0.7579 -0.1321 0.1889 0.0101  503 LEU A CG    
4100  C  CD1   . LEU A 503 ? 1.1901 0.9341 0.7652 -0.1246 0.1918 0.0112  503 LEU A CD1   
4101  C  CD2   . LEU A 503 ? 1.1934 0.9432 0.7645 -0.1398 0.1884 0.0121  503 LEU A CD2   
4102  N  N     . SER A 504 ? 1.1648 0.9104 0.7436 -0.119  0.1887 0.0081  504 SER A N     
4103  C  CA    . SER A 504 ? 1.1642 0.9227 0.7491 -0.1174 0.1886 0.0113  504 SER A CA    
4104  C  C     . SER A 504 ? 1.1611 0.9335 0.7516 -0.117  0.1903 0.0167  504 SER A C     
4105  O  O     . SER A 504 ? 1.1632 0.9342 0.7543 -0.1134 0.1927 0.0179  504 SER A O     
4106  C  CB    . SER A 504 ? 1.182  0.9371 0.7686 -0.1099 0.1897 0.0101  504 SER A CB    
4107  O  OG    . SER A 504 ? 1.2175 0.9622 0.8002 -0.1102 0.1881 0.0058  504 SER A OG    
4108  N  N     . ILE A 505 ? 1.1547 0.9408 0.7493 -0.1207 0.189  0.0203  505 ILE A N     
4109  C  CA    . ILE A 505 ? 1.1538 0.9555 0.7546 -0.1205 0.1905 0.0262  505 ILE A CA    
4110  C  C     . ILE A 505 ? 1.1533 0.9668 0.7597 -0.1174 0.1905 0.0292  505 ILE A C     
4111  O  O     . ILE A 505 ? 1.1566 0.9717 0.7623 -0.1209 0.1879 0.0281  505 ILE A O     
4112  C  CB    . ILE A 505 ? 1.1591 0.9678 0.7595 -0.1297 0.1885 0.0281  505 ILE A CB    
4113  C  CG1   . ILE A 505 ? 1.1785 0.9743 0.7722 -0.1338 0.1883 0.0247  505 ILE A CG1   
4114  C  CG2   . ILE A 505 ? 1.157  0.9834 0.7647 -0.1296 0.19   0.0349  505 ILE A CG2   
4115  C  CD1   . ILE A 505 ? 1.1962 0.9881 0.7901 -0.1291 0.1915 0.0255  505 ILE A CD1   
4116  N  N     . ILE A 506 ? 1.1478 0.9693 0.7593 -0.1106 0.1936 0.0333  506 ILE A N     
4117  C  CA    . ILE A 506 ? 1.1485 0.9818 0.7653 -0.107  0.1941 0.0367  506 ILE A CA    
4118  C  C     . ILE A 506 ? 1.1464 0.9985 0.7695 -0.1097 0.1943 0.0433  506 ILE A C     
4119  O  O     . ILE A 506 ? 1.1457 1.0025 0.7711 -0.1081 0.1969 0.0468  506 ILE A O     
4120  C  CB    . ILE A 506 ? 1.1557 0.9843 0.7731 -0.0973 0.1975 0.0367  506 ILE A CB    
4121  C  CG1   . ILE A 506 ? 1.1756 0.9868 0.7872 -0.0953 0.1967 0.0303  506 ILE A CG1   
4122  C  CG2   . ILE A 506 ? 1.1556 0.997  0.7783 -0.0931 0.1987 0.0409  506 ILE A CG2   
4123  C  CD1   . ILE A 506 ? 1.1939 0.9982 0.8047 -0.0868 0.1999 0.0297  506 ILE A CD1   
4124  N  N     . ARG A 507 ? 1.1438 1.0068 0.7696 -0.1141 0.1916 0.0452  507 ARG A N     
4125  C  CA    . ARG A 507 ? 1.1423 1.0244 0.7745 -0.1175 0.1913 0.0517  507 ARG A CA    
4126  C  C     . ARG A 507 ? 1.1372 1.0314 0.7734 -0.1171 0.1897 0.0543  507 ARG A C     
4127  O  O     . ARG A 507 ? 1.1416 1.0307 0.7743 -0.1212 0.1865 0.0507  507 ARG A O     
4128  C  CB    . ARG A 507 ? 1.1633 1.0463 0.7931 -0.1279 0.1882 0.0513  507 ARG A CB    
4129  C  CG    . ARG A 507 ? 1.1956 1.0989 0.832  -0.1326 0.1873 0.0582  507 ARG A CG    
4130  C  CD    . ARG A 507 ? 1.2306 1.1432 0.8728 -0.1271 0.1916 0.0638  507 ARG A CD    
4131  N  NE    . ARG A 507 ? 1.2558 1.1891 0.905  -0.1317 0.1907 0.0709  507 ARG A NE    
4132  C  CZ    . ARG A 507 ? 1.2751 1.2222 0.9312 -0.1267 0.1943 0.0777  507 ARG A CZ    
4133  N  NH1   . ARG A 507 ? 1.2722 1.2135 0.9283 -0.1169 0.1991 0.0782  507 ARG A NH1   
4134  N  NH2   . ARG A 507 ? 1.2665 1.2331 0.9293 -0.1315 0.1931 0.0843  507 ARG A NH2   
4135  N  N     . ASN A 508 ? 1.1257 1.0355 0.7689 -0.112  0.1923 0.0608  508 ASN A N     
4136  C  CA    . ASN A 508 ? 1.1216 1.0451 0.7695 -0.1105 0.1915 0.0645  508 ASN A CA    
4137  C  C     . ASN A 508 ? 1.1214 1.0353 0.7663 -0.1055 0.1915 0.0604  508 ASN A C     
4138  O  O     . ASN A 508 ? 1.1205 1.04   0.7663 -0.1079 0.1889 0.0605  508 ASN A O     
4139  C  CB    . ASN A 508 ? 1.1344 1.07   0.7841 -0.1206 0.1869 0.0667  508 ASN A CB    
4140  C  CG    . ASN A 508 ? 1.1698 1.1169 0.8232 -0.1261 0.1867 0.0714  508 ASN A CG    
4141  O  OD1   . ASN A 508 ? 1.1794 1.1331 0.8371 -0.121  0.1905 0.0759  508 ASN A OD1   
4142  N  ND2   . ASN A 508 ? 1.1785 1.1277 0.8298 -0.1367 0.1823 0.0706  508 ASN A ND2   
4143  N  N     . GLY A 509 ? 1.1203 1.02   0.7618 -0.0988 0.1944 0.0569  509 GLY A N     
4144  C  CA    . GLY A 509 ? 1.1247 1.0145 0.7634 -0.0938 0.1948 0.0529  509 GLY A CA    
4145  C  C     . GLY A 509 ? 1.1291 1.0042 0.7615 -0.0988 0.1913 0.046   509 GLY A C     
4146  O  O     . GLY A 509 ? 1.1348 1.0023 0.765  -0.0956 0.1912 0.0427  509 GLY A O     
4147  N  N     . HIS A 510 ? 1.1243 0.995  0.7535 -0.1066 0.1888 0.0438  510 HIS A N     
4148  C  CA    . HIS A 510 ? 1.1307 0.9868 0.7531 -0.1115 0.1858 0.0375  510 HIS A CA    
4149  C  C     . HIS A 510 ? 1.1298 0.9716 0.7474 -0.1118 0.1867 0.0338  510 HIS A C     
4150  O  O     . HIS A 510 ? 1.1281 0.9733 0.7474 -0.1117 0.1884 0.0363  510 HIS A O     
4151  C  CB    . HIS A 510 ? 1.1422 1.0044 0.7633 -0.1212 0.1816 0.038   510 HIS A CB    
4152  C  CG    . HIS A 510 ? 1.1662 1.0404 0.7906 -0.1218 0.18   0.0408  510 HIS A CG    
4153  N  ND1   . HIS A 510 ? 1.1815 1.0747 0.8122 -0.1234 0.1797 0.0472  510 HIS A ND1   
4154  C  CD2   . HIS A 510 ? 1.1824 1.0519 0.8045 -0.1208 0.1786 0.0381  510 HIS A CD2   
4155  C  CE1   . HIS A 510 ? 1.1851 1.0847 0.8171 -0.1233 0.178  0.0481  510 HIS A CE1   
4156  N  NE2   . HIS A 510 ? 1.1896 1.0751 0.8163 -0.1218 0.1773 0.0427  510 HIS A NE2   
4157  N  N     . GLU A 511 ? 1.1287 0.9548 0.7405 -0.1122 0.1857 0.028   511 GLU A N     
4158  C  CA    . GLU A 511 ? 1.1332 0.9454 0.74   -0.1128 0.1862 0.0243  511 GLU A CA    
4159  C  C     . GLU A 511 ? 1.1324 0.9375 0.7333 -0.1211 0.183  0.021   511 GLU A C     
4160  O  O     . GLU A 511 ? 1.1362 0.9364 0.7341 -0.1227 0.1811 0.0182  511 GLU A O     
4161  C  CB    . GLU A 511 ? 1.1643 0.9635 0.7689 -0.1059 0.1879 0.0205  511 GLU A CB    
4162  C  CG    . GLU A 511 ? 1.2231 1.0081 0.8225 -0.1063 0.1883 0.0167  511 GLU A CG    
4163  C  CD    . GLU A 511 ? 1.2922 1.0644 0.8891 -0.1005 0.1894 0.0129  511 GLU A CD    
4164  O  OE1   . GLU A 511 ? 1.3057 1.0661 0.8983 -0.1009 0.1894 0.0097  511 GLU A OE1   
4165  O  OE2   . GLU A 511 ? 1.3139 1.0877 0.9131 -0.0957 0.1902 0.0132  511 GLU A OE2   
4166  N  N     . PHE A 512 ? 1.127  0.9315 0.7258 -0.1263 0.1826 0.0214  512 PHE A N     
4167  C  CA    . PHE A 512 ? 1.132  0.9289 0.7241 -0.1345 0.1799 0.0185  512 PHE A CA    
4168  C  C     . PHE A 512 ? 1.1333 0.9135 0.7195 -0.1331 0.181  0.014   512 PHE A C     
4169  O  O     . PHE A 512 ? 1.1343 0.9132 0.7223 -0.1289 0.1834 0.0148  512 PHE A O     
4170  C  CB    . PHE A 512 ? 1.1298 0.9376 0.7233 -0.1419 0.1787 0.0223  512 PHE A CB    
4171  C  CG    . PHE A 512 ? 1.1319 0.9584 0.7323 -0.143  0.1778 0.0276  512 PHE A CG    
4172  C  CD1   . PHE A 512 ? 1.1423 0.9728 0.7411 -0.1483 0.1746 0.0276  512 PHE A CD1   
4173  C  CD2   . PHE A 512 ? 1.1352 0.975  0.7433 -0.1384 0.1802 0.0328  512 PHE A CD2   
4174  C  CE1   . PHE A 512 ? 1.1433 0.9915 0.7486 -0.1491 0.1736 0.0327  512 PHE A CE1   
4175  C  CE2   . PHE A 512 ? 1.1361 0.9936 0.7507 -0.1389 0.1796 0.0381  512 PHE A CE2   
4176  C  CZ    . PHE A 512 ? 1.1328 0.9948 0.7462 -0.1443 0.1761 0.038   512 PHE A CZ    
4177  N  N     . ARG A 513 ? 1.1315 0.899  0.7106 -0.1362 0.1794 0.0096  513 ARG A N     
4178  C  CA    . ARG A 513 ? 1.1377 0.8896 0.7113 -0.1344 0.1804 0.0056  513 ARG A CA    
4179  C  C     . ARG A 513 ? 1.1438 0.885  0.7087 -0.1414 0.1788 0.0027  513 ARG A C     
4180  O  O     . ARG A 513 ? 1.1461 0.8854 0.7072 -0.1456 0.1768 0.0015  513 ARG A O     
4181  C  CB    . ARG A 513 ? 1.1533 0.8974 0.7273 -0.1272 0.1813 0.0029  513 ARG A CB    
4182  C  CG    . ARG A 513 ? 1.1908 0.9205 0.7604 -0.1242 0.1825 -0.0007 513 ARG A CG    
4183  C  CD    . ARG A 513 ? 1.223  0.9492 0.7953 -0.1165 0.1837 -0.0019 513 ARG A CD    
4184  N  NE    . ARG A 513 ? 1.2583 0.9712 0.8267 -0.1137 0.1845 -0.0052 513 ARG A NE    
4185  C  CZ    . ARG A 513 ? 1.2834 0.9935 0.8521 -0.1107 0.1861 -0.005  513 ARG A CZ    
4186  N  NH1   . ARG A 513 ? 1.2736 0.9929 0.8463 -0.11   0.1873 -0.0016 513 ARG A NH1   
4187  N  NH2   . ARG A 513 ? 1.2868 0.9851 0.8519 -0.1082 0.1865 -0.0079 513 ARG A NH2   
4188  N  N     . TRP A 514 ? 1.1461 0.8798 0.7073 -0.1426 0.1799 0.0015  514 TRP A N     
4189  C  CA    . TRP A 514 ? 1.1578 0.8795 0.7098 -0.1486 0.1791 -0.0014 514 TRP A CA    
4190  C  C     . TRP A 514 ? 1.169  0.8756 0.7166 -0.1437 0.1803 -0.0054 514 TRP A C     
4191  O  O     . TRP A 514 ? 1.1704 0.8745 0.7204 -0.1382 0.1821 -0.0056 514 TRP A O     
4192  C  CB    . TRP A 514 ? 1.1561 0.8793 0.7068 -0.1528 0.1798 0.0002  514 TRP A CB    
4193  C  CG    . TRP A 514 ? 1.1565 0.8928 0.7096 -0.1599 0.1783 0.004   514 TRP A CG    
4194  C  CD1   . TRP A 514 ? 1.1714 0.9054 0.718  -0.169  0.1764 0.0037  514 TRP A CD1   
4195  C  CD2   . TRP A 514 ? 1.1485 0.9022 0.7109 -0.1587 0.1786 0.0089  514 TRP A CD2   
4196  N  NE1   . TRP A 514 ? 1.1679 0.9177 0.7197 -0.1739 0.1752 0.0081  514 TRP A NE1   
4197  C  CE2   . TRP A 514 ? 1.1563 0.9187 0.7181 -0.1675 0.1766 0.0116  514 TRP A CE2   
4198  C  CE3   . TRP A 514 ? 1.1484 0.9109 0.7191 -0.151  0.1805 0.0115  514 TRP A CE3   
4199  C  CZ2   . TRP A 514 ? 1.1545 0.9352 0.7246 -0.1685 0.1764 0.017   514 TRP A CZ2   
4200  C  CZ3   . TRP A 514 ? 1.15   0.9297 0.7283 -0.1517 0.1807 0.0168  514 TRP A CZ3   
4201  C  CH2   . TRP A 514 ? 1.149  0.9382 0.7274 -0.1602 0.1786 0.0197  514 TRP A CH2   
4202  N  N     . LEU A 515 ? 1.1749 0.8713 0.7158 -0.1455 0.1793 -0.0084 515 LEU A N     
4203  C  CA    . LEU A 515 ? 1.1877 0.87   0.7242 -0.1411 0.1804 -0.0119 515 LEU A CA    
4204  C  C     . LEU A 515 ? 1.1997 0.8691 0.7261 -0.1459 0.1806 -0.0142 515 LEU A C     
4205  O  O     . LEU A 515 ? 1.2002 0.8713 0.7226 -0.1531 0.1797 -0.0132 515 LEU A O     
4206  C  CB    . LEU A 515 ? 1.1919 0.8716 0.7283 -0.1384 0.1796 -0.0134 515 LEU A CB    
4207  C  CG    . LEU A 515 ? 1.2028 0.8945 0.748  -0.1342 0.1794 -0.0112 515 LEU A CG    
4208  C  CD1   . LEU A 515 ? 1.2116 0.9011 0.7554 -0.1337 0.1784 -0.0125 515 LEU A CD1   
4209  C  CD2   . LEU A 515 ? 1.2077 0.9003 0.7587 -0.1266 0.1811 -0.011  515 LEU A CD2   
4210  N  N     . SER A 516 ? 1.2081 0.8647 0.7301 -0.1419 0.182  -0.0169 516 SER A N     
4211  C  CA    . SER A 516 ? 1.2254 0.8685 0.7374 -0.1452 0.1828 -0.0191 516 SER A CA    
4212  C  C     . SER A 516 ? 1.2332 0.8785 0.7436 -0.1501 0.1832 -0.0178 516 SER A C     
4213  O  O     . SER A 516 ? 1.2378 0.8797 0.7411 -0.1572 0.1826 -0.0179 516 SER A O     
4214  C  CB    . SER A 516 ? 1.2489 0.8847 0.7525 -0.15   0.1818 -0.0206 516 SER A CB    
4215  O  OG    . SER A 516 ? 1.2779 0.9125 0.7833 -0.1459 0.1815 -0.0215 516 SER A OG    
4216  N  N     . LEU A 517 ? 1.2334 0.8845 0.7501 -0.1463 0.1842 -0.0163 517 LEU A N     
4217  C  CA    . LEU A 517 ? 1.2431 0.8971 0.7592 -0.15   0.1849 -0.0147 517 LEU A CA    
4218  C  C     . LEU A 517 ? 1.2642 0.9037 0.771  -0.1514 0.1863 -0.0171 517 LEU A C     
4219  O  O     . LEU A 517 ? 1.2696 0.9015 0.7758 -0.1456 0.1876 -0.0187 517 LEU A O     
4220  C  CB    . LEU A 517 ? 1.2385 0.9011 0.7632 -0.1445 0.1861 -0.0125 517 LEU A CB    
4221  C  CG    . LEU A 517 ? 1.2483 0.9251 0.7825 -0.1416 0.1854 -0.0098 517 LEU A CG    
4222  C  CD1   . LEU A 517 ? 1.2503 0.933  0.7909 -0.1362 0.1871 -0.0077 517 LEU A CD1   
4223  C  CD2   . LEU A 517 ? 1.2529 0.9409 0.7889 -0.1483 0.1839 -0.0071 517 LEU A CD2   
4224  N  N     . PRO A 518 ? 1.2736 0.9091 0.7729 -0.1591 0.1861 -0.0172 518 PRO A N     
4225  C  CA    . PRO A 518 ? 1.2845 0.9054 0.7742 -0.1602 0.1878 -0.0194 518 PRO A CA    
4226  C  C     . PRO A 518 ? 1.2848 0.9075 0.7774 -0.158  0.1894 -0.0183 518 PRO A C     
4227  O  O     . PRO A 518 ? 1.2795 0.9145 0.7789 -0.1594 0.1892 -0.0154 518 PRO A O     
4228  C  CB    . PRO A 518 ? 1.2985 0.9155 0.7793 -0.1696 0.187  -0.0196 518 PRO A CB    
4229  C  CG    . PRO A 518 ? 1.2962 0.9295 0.7844 -0.1741 0.185  -0.0164 518 PRO A CG    
4230  C  CD    . PRO A 518 ? 1.2677 0.9113 0.7664 -0.1672 0.1843 -0.0153 518 PRO A CD    
4231  N  N     . ARG A 519 ? 1.2895 0.9003 0.7771 -0.1541 0.1912 -0.0204 519 ARG A N     
4232  C  CA    . ARG A 519 ? 1.2945 0.9052 0.7835 -0.1519 0.1928 -0.0196 519 ARG A CA    
4233  C  C     . ARG A 519 ? 1.3007 0.9108 0.7845 -0.1597 0.1934 -0.0186 519 ARG A C     
4234  O  O     . ARG A 519 ? 1.2986 0.9164 0.787  -0.1603 0.1941 -0.0163 519 ARG A O     
4235  C  CB    . ARG A 519 ? 1.3144 0.9122 0.7988 -0.146  0.1944 -0.0221 519 ARG A CB    
4236  C  CG    . ARG A 519 ? 1.344  0.9427 0.8313 -0.142  0.1958 -0.0213 519 ARG A CG    
4237  C  CD    . ARG A 519 ? 1.3836 0.968  0.863  -0.1393 0.1975 -0.0235 519 ARG A CD    
4238  N  NE    . ARG A 519 ? 1.4155 0.9907 0.8847 -0.1456 0.1986 -0.0244 519 ARG A NE    
4239  C  CZ    . ARG A 519 ? 1.4357 1.0102 0.9021 -0.1493 0.1999 -0.0235 519 ARG A CZ    
4240  N  NH1   . ARG A 519 ? 1.4254 1.0078 0.8984 -0.147  0.2004 -0.0216 519 ARG A NH1   
4241  N  NH2   . ARG A 519 ? 1.4375 1.0026 0.8937 -0.1552 0.201  -0.0245 519 ARG A NH2   
4242  N  N     . VAL A 520 ? 1.3052 0.9059 0.779  -0.1658 0.1933 -0.0202 520 VAL A N     
4243  C  CA    . VAL A 520 ? 1.3104 0.9088 0.7777 -0.1739 0.1938 -0.0196 520 VAL A CA    
4244  C  C     . VAL A 520 ? 1.3016 0.9151 0.7746 -0.1807 0.1918 -0.0164 520 VAL A C     
4245  O  O     . VAL A 520 ? 1.302  0.9193 0.7749 -0.1844 0.1897 -0.0161 520 VAL A O     
4246  C  CB    . VAL A 520 ? 1.33   0.9114 0.7831 -0.1781 0.1946 -0.0224 520 VAL A CB    
4247  C  CG1   . VAL A 520 ? 1.3435 0.9111 0.7906 -0.1727 0.1972 -0.0246 520 VAL A CG1   
4248  C  CG2   . VAL A 520 ? 1.3376 0.9158 0.7879 -0.1783 0.1932 -0.0238 520 VAL A CG2   
4249  N  N     . SER A 521 ? 1.2898 0.9122 0.7681 -0.1821 0.1925 -0.0136 521 SER A N     
4250  C  CA    . SER A 521 ? 1.2812 0.9188 0.7654 -0.1885 0.191  -0.0099 521 SER A CA    
4251  C  C     . SER A 521 ? 1.2806 0.9152 0.7596 -0.1946 0.1924 -0.009  521 SER A C     
4252  O  O     . SER A 521 ? 1.288  0.917  0.7661 -0.1905 0.1948 -0.0095 521 SER A O     
4253  C  CB    . SER A 521 ? 1.2847 0.9384 0.7822 -0.1827 0.1909 -0.0066 521 SER A CB    
4254  O  OG    . SER A 521 ? 1.3019 0.9709 0.8054 -0.1883 0.19   -0.0024 521 SER A OG    
4255  N  N     . GLU A 522 ? 1.2695 0.9071 0.7446 -0.2046 0.1909 -0.0077 522 GLU A N     
4256  C  CA    . GLU A 522 ? 1.2672 0.9017 0.7365 -0.2118 0.192  -0.0068 522 GLU A CA    
4257  C  C     . GLU A 522 ? 1.2529 0.8977 0.7309 -0.2091 0.1938 -0.0035 522 GLU A C     
4258  O  O     . GLU A 522 ? 1.259  0.8952 0.732  -0.209  0.1962 -0.0043 522 GLU A O     
4259  C  CB    . GLU A 522 ? 1.2934 0.9323 0.7587 -0.2233 0.1895 -0.0054 522 GLU A CB    
4260  C  CG    . GLU A 522 ? 1.3557 0.9822 0.8105 -0.2262 0.188  -0.0088 522 GLU A CG    
4261  C  CD    . GLU A 522 ? 1.4201 1.0562 0.8813 -0.2244 0.1853 -0.0082 522 GLU A CD    
4262  O  OE1   . GLU A 522 ? 1.4283 1.0629 0.8937 -0.2153 0.1859 -0.0096 522 GLU A OE1   
4263  O  OE2   . GLU A 522 ? 1.4431 1.0879 0.9048 -0.2324 0.1825 -0.0062 522 GLU A OE2   
4264  N  N     . ASN A 523 ? 1.2326 0.8952 0.7231 -0.2063 0.1929 0.0003  523 ASN A N     
4265  C  CA    . ASN A 523 ? 1.2214 0.8944 0.7204 -0.2031 0.1949 0.004   523 ASN A CA    
4266  C  C     . ASN A 523 ? 1.2077 0.8853 0.7153 -0.1918 0.1961 0.0045  523 ASN A C     
4267  O  O     . ASN A 523 ? 1.2058 0.8895 0.7191 -0.188  0.1982 0.0072  523 ASN A O     
4268  C  CB    . ASN A 523 ? 1.2266 0.918  0.7329 -0.21   0.1934 0.0092  523 ASN A CB    
4269  C  CG    . ASN A 523 ? 1.2702 0.9589 0.7686 -0.222  0.1918 0.0092  523 ASN A CG    
4270  O  OD1   . ASN A 523 ? 1.2862 0.9796 0.7837 -0.2281 0.1888 0.0095  523 ASN A OD1   
4271  N  ND2   . ASN A 523 ? 1.2816 0.9621 0.7735 -0.2258 0.1938 0.0087  523 ASN A ND2   
4272  N  N     . GLY A 524 ? 1.1962 0.8707 0.7045 -0.1868 0.1949 0.0022  524 GLY A N     
4273  C  CA    . GLY A 524 ? 1.1859 0.8646 0.7019 -0.1768 0.1958 0.0027  524 GLY A CA    
4274  C  C     . GLY A 524 ? 1.1823 0.8466 0.6938 -0.1694 0.1967 -0.0015 524 GLY A C     
4275  O  O     . GLY A 524 ? 1.191  0.8413 0.6932 -0.1713 0.1966 -0.0052 524 GLY A O     
4276  N  N     . LYS A 525 ? 1.1678 0.8357 0.6858 -0.1609 0.1977 -0.0008 525 LYS A N     
4277  C  CA    . LYS A 525 ? 1.1677 0.8246 0.6834 -0.1532 0.1983 -0.0041 525 LYS A CA    
4278  C  C     . LYS A 525 ? 1.1529 0.8183 0.6766 -0.1474 0.1974 -0.0031 525 LYS A C     
4279  O  O     . LYS A 525 ? 1.1474 0.8257 0.6788 -0.1458 0.1979 0.0007  525 LYS A O     
4280  C  CB    . LYS A 525 ? 1.1937 0.8439 0.7076 -0.1486 0.2008 -0.0044 525 LYS A CB    
4281  C  CG    . LYS A 525 ? 1.2472 0.8843 0.7568 -0.1421 0.201  -0.0081 525 LYS A CG    
4282  C  CD    . LYS A 525 ? 1.2997 0.9273 0.8046 -0.1393 0.2032 -0.009  525 LYS A CD    
4283  C  CE    . LYS A 525 ? 1.3477 0.9623 0.8476 -0.134  0.203  -0.0126 525 LYS A CE    
4284  N  NZ    . LYS A 525 ? 1.3791 0.9845 0.8716 -0.138  0.2021 -0.0154 525 LYS A NZ    
4285  N  N     . ARG A 526 ? 1.144  0.8025 0.6658 -0.144  0.1962 -0.0061 526 ARG A N     
4286  C  CA    . ARG A 526 ? 1.134  0.7992 0.6626 -0.1388 0.1954 -0.0055 526 ARG A CA    
4287  C  C     . ARG A 526 ? 1.1193 0.787  0.6527 -0.1313 0.1971 -0.0041 526 ARG A C     
4288  O  O     . ARG A 526 ? 1.1251 0.7827 0.6548 -0.1273 0.1981 -0.0061 526 ARG A O     
4289  C  CB    . ARG A 526 ? 1.1583 0.8142 0.6832 -0.1368 0.194  -0.0092 526 ARG A CB    
4290  C  CG    . ARG A 526 ? 1.1936 0.8563 0.7251 -0.132  0.193  -0.0086 526 ARG A CG    
4291  C  CD    . ARG A 526 ? 1.2372 0.8918 0.7653 -0.1311 0.1916 -0.0118 526 ARG A CD    
4292  N  NE    . ARG A 526 ? 1.279  0.9205 0.802  -0.1273 0.1924 -0.0148 526 ARG A NE    
4293  C  CZ    . ARG A 526 ? 1.313  0.9464 0.8329 -0.1252 0.1916 -0.0174 526 ARG A CZ    
4294  N  NH1   . ARG A 526 ? 1.3081 0.9445 0.8293 -0.1265 0.1902 -0.0176 526 ARG A NH1   
4295  N  NH2   . ARG A 526 ? 1.3198 0.9423 0.8354 -0.1217 0.1923 -0.0195 526 ARG A NH2   
4296  N  N     . PRO A 527 ? 1.0994 0.7802 0.6406 -0.1292 0.1975 -0.0006 527 PRO A N     
4297  C  CA    . PRO A 527 ? 1.0909 0.7732 0.6357 -0.122  0.1994 0.001   527 PRO A CA    
4298  C  C     . PRO A 527 ? 1.0867 0.7618 0.6311 -0.1156 0.1989 -0.0017 527 PRO A C     
4299  O  O     . PRO A 527 ? 1.0894 0.7632 0.6338 -0.116  0.1971 -0.0036 527 PRO A O     
4300  C  CB    . PRO A 527 ? 1.0918 0.7902 0.6446 -0.1218 0.2001 0.0057  527 PRO A CB    
4301  C  CG    . PRO A 527 ? 1.0961 0.8019 0.6494 -0.1299 0.1984 0.007   527 PRO A CG    
4302  C  CD    . PRO A 527 ? 1.0844 0.779  0.631  -0.1332 0.1963 0.0025  527 PRO A CD    
4303  N  N     . ASP A 528 ? 1.0792 0.7493 0.6228 -0.1098 0.2005 -0.0018 528 ASP A N     
4304  C  CA    . ASP A 528 ? 1.0788 0.7423 0.622  -0.1038 0.2    -0.0041 528 ASP A CA    
4305  C  C     . ASP A 528 ? 1.068  0.7408 0.6175 -0.1001 0.2002 -0.0019 528 ASP A C     
4306  O  O     . ASP A 528 ? 1.0677 0.7367 0.6175 -0.0966 0.1992 -0.0037 528 ASP A O     
4307  C  CB    . ASP A 528 ? 1.101  0.7555 0.6404 -0.0995 0.2014 -0.0049 528 ASP A CB    
4308  C  CG    . ASP A 528 ? 1.1524 0.7967 0.6852 -0.1023 0.2014 -0.0072 528 ASP A CG    
4309  O  OD1   . ASP A 528 ? 1.1591 0.8    0.6891 -0.1065 0.1999 -0.0093 528 ASP A OD1   
4310  O  OD2   . ASP A 528 ? 1.1791 0.8183 0.7089 -0.1002 0.203  -0.007  528 ASP A OD2   
4311  N  N     . HIS A 529 ? 1.0575 0.7421 0.6119 -0.1006 0.2016 0.0022  529 HIS A N     
4312  C  CA    . HIS A 529 ? 1.0545 0.7485 0.6146 -0.097  0.2022 0.0049  529 HIS A CA    
4313  C  C     . HIS A 529 ? 1.054  0.7624 0.6192 -0.1009 0.2027 0.0091  529 HIS A C     
4314  O  O     . HIS A 529 ? 1.053  0.7646 0.6181 -0.1036 0.204  0.0112  529 HIS A O     
4315  C  CB    . HIS A 529 ? 1.0598 0.7522 0.62   -0.0902 0.2049 0.0066  529 HIS A CB    
4316  C  CG    . HIS A 529 ? 1.0864 0.765  0.6412 -0.0865 0.2046 0.0032  529 HIS A CG    
4317  N  ND1   . HIS A 529 ? 1.1098 0.7831 0.664  -0.0836 0.2031 0.0005  529 HIS A ND1   
4318  C  CD2   . HIS A 529 ? 1.104  0.7739 0.654  -0.0852 0.2057 0.0023  529 HIS A CD2   
4319  C  CE1   . HIS A 529 ? 1.1207 0.7828 0.6701 -0.081  0.2031 -0.0018 529 HIS A CE1   
4320  N  NE2   . HIS A 529 ? 1.1217 0.7811 0.6682 -0.0817 0.2046 -0.0009 529 HIS A NE2   
4321  N  N     . VAL A 530 ? 1.0543 0.772  0.6242 -0.1013 0.2017 0.0105  530 VAL A N     
4322  C  CA    . VAL A 530 ? 1.0581 0.7911 0.6336 -0.1043 0.2022 0.0151  530 VAL A CA    
4323  C  C     . VAL A 530 ? 1.0677 0.8086 0.6482 -0.0982 0.2037 0.018   530 VAL A C     
4324  O  O     . VAL A 530 ? 1.0687 0.8086 0.65   -0.0965 0.2024 0.0163  530 VAL A O     
4325  C  CB    . VAL A 530 ? 1.0614 0.7996 0.6373 -0.1121 0.1993 0.0147  530 VAL A CB    
4326  C  CG1   . VAL A 530 ? 1.0591 0.8144 0.6414 -0.1149 0.1998 0.0202  530 VAL A CG1   
4327  C  CG2   . VAL A 530 ? 1.0711 0.8    0.6408 -0.1179 0.1982 0.0118  530 VAL A CG2   
4328  N  N     . ILE A 531 ? 1.0732 0.8208 0.6565 -0.0945 0.2068 0.0224  531 ILE A N     
4329  C  CA    . ILE A 531 ? 1.0853 0.8392 0.6723 -0.088  0.209  0.0255  531 ILE A CA    
4330  C  C     . ILE A 531 ? 1.0904 0.8619 0.6844 -0.0898 0.2095 0.0309  531 ILE A C     
4331  O  O     . ILE A 531 ? 1.0909 0.87   0.6869 -0.0932 0.2103 0.0342  531 ILE A O     
4332  C  CB    . ILE A 531 ? 1.0961 0.8439 0.6805 -0.0813 0.2126 0.0268  531 ILE A CB    
4333  C  CG1   . ILE A 531 ? 1.1181 0.8487 0.6954 -0.0803 0.2117 0.0216  531 ILE A CG1   
4334  C  CG2   . ILE A 531 ? 1.099  0.8509 0.6857 -0.0742 0.2152 0.0296  531 ILE A CG2   
4335  C  CD1   . ILE A 531 ? 1.1388 0.8611 0.7141 -0.079  0.2094 0.0171  531 ILE A CD1   
4336  N  N     . GLN A 532 ? 1.0924 0.8709 0.69   -0.0875 0.2092 0.0322  532 GLN A N     
4337  C  CA    . GLN A 532 ? 1.0982 0.8943 0.7026 -0.0888 0.2097 0.0377  532 GLN A CA    
4338  C  C     . GLN A 532 ? 1.1097 0.9121 0.7171 -0.0808 0.2137 0.0424  532 GLN A C     
4339  O  O     . GLN A 532 ? 1.1158 0.9119 0.7213 -0.0751 0.2146 0.0407  532 GLN A O     
4340  C  CB    . GLN A 532 ? 1.1142 0.9155 0.7207 -0.0932 0.2062 0.0364  532 GLN A CB    
4341  C  CG    . GLN A 532 ? 1.141  0.9614 0.7545 -0.0954 0.2062 0.0423  532 GLN A CG    
4342  C  CD    . GLN A 532 ? 1.1841 1.0092 0.7987 -0.1016 0.2022 0.0409  532 GLN A CD    
4343  O  OE1   . GLN A 532 ? 1.2085 1.0229 0.8189 -0.1029 0.1999 0.0357  532 GLN A OE1   
4344  N  NE2   . GLN A 532 ? 1.1786 1.0201 0.7988 -0.1055 0.2014 0.0457  532 GLN A NE2   
4345  N  N     . ILE A 533 ? 1.1116 0.9261 0.7232 -0.0801 0.2163 0.0484  533 ILE A N     
4346  C  CA    . ILE A 533 ? 1.1221 0.9435 0.7364 -0.0721 0.2208 0.0536  533 ILE A CA    
4347  C  C     . ILE A 533 ? 1.1233 0.9648 0.7456 -0.0739 0.2208 0.0598  533 ILE A C     
4348  O  O     . ILE A 533 ? 1.1192 0.971  0.7453 -0.0795 0.22   0.0629  533 ILE A O     
4349  C  CB    . ILE A 533 ? 1.1338 0.9501 0.7453 -0.0679 0.2248 0.0558  533 ILE A CB    
4350  C  CG1   . ILE A 533 ? 1.1558 0.952  0.7591 -0.0667 0.2242 0.0495  533 ILE A CG1   
4351  C  CG2   . ILE A 533 ? 1.1378 0.9604 0.7511 -0.0593 0.2298 0.0615  533 ILE A CG2   
4352  C  CD1   . ILE A 533 ? 1.1745 0.964  0.774  -0.0641 0.2271 0.0504  533 ILE A CD1   
4353  N  N     . LEU A 534 ? 1.1268 0.9744 0.7518 -0.0695 0.2215 0.0616  534 LEU A N     
4354  C  CA    . LEU A 534 ? 1.1311 0.9981 0.7637 -0.0713 0.2211 0.0673  534 LEU A CA    
4355  C  C     . LEU A 534 ? 1.1351 1.0142 0.772  -0.0638 0.2261 0.0749  534 LEU A C     
4356  O  O     . LEU A 534 ? 1.129  1.0261 0.7729 -0.0655 0.2258 0.0805  534 LEU A O     
4357  C  CB    . LEU A 534 ? 1.1361 1.0039 0.7693 -0.0729 0.2178 0.0644  534 LEU A CB    
4358  C  CG    . LEU A 534 ? 1.1626 1.0211 0.7922 -0.0809 0.2127 0.0579  534 LEU A CG    
4359  C  CD1   . LEU A 534 ? 1.1779 1.0196 0.8017 -0.0776 0.2121 0.0515  534 LEU A CD1   
4360  C  CD2   . LEU A 534 ? 1.1665 1.0377 0.8004 -0.0877 0.2089 0.0591  534 LEU A CD2   
4361  N  N     . ASP A 535 ? 1.1438 1.0134 0.7763 -0.0556 0.2307 0.0754  535 ASP A N     
4362  C  CA    . ASP A 535 ? 1.1508 1.0306 0.7864 -0.0477 0.2361 0.0827  535 ASP A CA    
4363  C  C     . ASP A 535 ? 1.1529 1.0341 0.7884 -0.0455 0.24   0.087   535 ASP A C     
4364  O  O     . ASP A 535 ? 1.1553 1.0374 0.7897 -0.0371 0.2454 0.0917  535 ASP A O     
4365  C  CB    . ASP A 535 ? 1.1861 1.0559 0.8168 -0.0389 0.2392 0.0815  535 ASP A CB    
4366  C  CG    . ASP A 535 ? 1.2672 1.1159 0.8887 -0.0354 0.2407 0.0764  535 ASP A CG    
4367  O  OD1   . ASP A 535 ? 1.2828 1.1221 0.9013 -0.0409 0.2377 0.0716  535 ASP A OD1   
4368  O  OD2   . ASP A 535 ? 1.3027 1.144  0.9195 -0.0272 0.2448 0.0774  535 ASP A OD2   
4369  N  N     . LEU A 536 ? 1.1496 1.0309 0.7858 -0.0528 0.2375 0.0856  536 LEU A N     
4370  C  CA    . LEU A 536 ? 1.152  1.0345 0.7881 -0.0513 0.2411 0.0895  536 LEU A CA    
4371  C  C     . LEU A 536 ? 1.1424 1.046  0.7875 -0.0566 0.2405 0.0962  536 LEU A C     
4372  O  O     . LEU A 536 ? 1.1387 1.0539 0.788  -0.0516 0.245  0.1037  536 LEU A O     
4373  C  CB    . LEU A 536 ? 1.1641 1.0286 0.793  -0.0547 0.2394 0.083   536 LEU A CB    
4374  C  CG    . LEU A 536 ? 1.1852 1.0484 0.8129 -0.0539 0.2427 0.0859  536 LEU A CG    
4375  C  CD1   . LEU A 536 ? 1.1929 1.0554 0.8188 -0.0435 0.2492 0.0911  536 LEU A CD1   
4376  C  CD2   . LEU A 536 ? 1.2034 1.0479 0.8235 -0.0569 0.2407 0.0788  536 LEU A CD2   
4377  N  N     . PHE A 537 ? 1.137  1.0458 0.7849 -0.0666 0.2351 0.0938  537 PHE A N     
4378  C  CA    . PHE A 537 ? 1.1321 1.061  0.7883 -0.0731 0.2337 0.0997  537 PHE A CA    
4379  C  C     . PHE A 537 ? 1.1254 1.0675 0.7869 -0.0771 0.2299 0.1008  537 PHE A C     
4380  O  O     . PHE A 537 ? 1.1313 1.0649 0.7894 -0.0758 0.2279 0.0959  537 PHE A O     
4381  C  CB    . PHE A 537 ? 1.1362 1.0603 0.7904 -0.0826 0.2305 0.0964  537 PHE A CB    
4382  C  CG    . PHE A 537 ? 1.1535 1.0628 0.8016 -0.0797 0.2336 0.0943  537 PHE A CG    
4383  C  CD1   . PHE A 537 ? 1.1613 1.0768 0.8118 -0.0745 0.2388 0.1007  537 PHE A CD1   
4384  C  CD2   . PHE A 537 ? 1.1739 1.0635 0.8138 -0.0822 0.2312 0.0862  537 PHE A CD2   
4385  C  CE1   . PHE A 537 ? 1.1776 1.079  0.8219 -0.0719 0.2415 0.0987  537 PHE A CE1   
4386  C  CE2   . PHE A 537 ? 1.19   1.0663 0.8242 -0.0797 0.2338 0.0843  537 PHE A CE2   
4387  C  CZ    . PHE A 537 ? 1.1848 1.0669 0.8211 -0.0746 0.2389 0.0904  537 PHE A CZ    
4388  N  N     . GLU A 538 ? 1.1106 1.0736 0.7805 -0.0822 0.2287 0.1073  538 GLU A N     
4389  C  CA    . GLU A 538 ? 1.1048 1.081  0.7796 -0.0868 0.2246 0.1086  538 GLU A CA    
4390  C  C     . GLU A 538 ? 1.1051 1.0697 0.7746 -0.0957 0.2185 0.1003  538 GLU A C     
4391  O  O     . GLU A 538 ? 1.1082 1.0714 0.7768 -0.096  0.2159 0.0974  538 GLU A O     
4392  C  CB    . GLU A 538 ? 1.1225 1.1236 0.8071 -0.0913 0.2241 0.1173  538 GLU A CB    
4393  C  CG    . GLU A 538 ? 1.1794 1.1837 0.8652 -0.0991 0.2232 0.1187  538 GLU A CG    
4394  C  CD    . GLU A 538 ? 1.2508 1.2585 0.9388 -0.0929 0.2291 0.1244  538 GLU A CD    
4395  O  OE1   . GLU A 538 ? 1.2639 1.2709 0.9517 -0.0986 0.2287 0.1247  538 GLU A OE1   
4396  O  OE2   . GLU A 538 ? 1.2755 1.2857 0.9648 -0.0823 0.2343 0.1287  538 GLU A OE2   
4397  N  N     . LYS A 539 ? 1.101  1.0563 0.7664 -0.1023 0.2168 0.0965  539 LYS A N     
4398  C  CA    . LYS A 539 ? 1.1059 1.0479 0.765  -0.1101 0.2118 0.0887  539 LYS A CA    
4399  C  C     . LYS A 539 ? 1.1092 1.0287 0.7601 -0.1043 0.2133 0.0817  539 LYS A C     
4400  O  O     . LYS A 539 ? 1.1126 1.0253 0.7615 -0.0979 0.2175 0.0825  539 LYS A O     
4401  C  CB    . LYS A 539 ? 1.1299 1.0723 0.7881 -0.1199 0.2096 0.0883  539 LYS A CB    
4402  C  CG    . LYS A 539 ? 1.1708 1.1346 0.8364 -0.1277 0.2072 0.0947  539 LYS A CG    
4403  C  CD    . LYS A 539 ? 1.2231 1.1844 0.8862 -0.1377 0.205  0.0934  539 LYS A CD    
4404  C  CE    . LYS A 539 ? 1.257  1.2386 0.9267 -0.1469 0.2018 0.0992  539 LYS A CE    
4405  N  NZ    . LYS A 539 ? 1.2839 1.2624 0.9505 -0.1569 0.1999 0.098   539 LYS A NZ    
4406  N  N     . PRO A 540 ? 1.1062 1.0137 0.7519 -0.1065 0.21   0.075   540 PRO A N     
4407  C  CA    . PRO A 540 ? 1.1096 0.9965 0.7478 -0.1015 0.2111 0.0686  540 PRO A CA    
4408  C  C     . PRO A 540 ? 1.1065 0.9812 0.7395 -0.1046 0.2113 0.0654  540 PRO A C     
4409  O  O     . PRO A 540 ? 1.1066 0.9844 0.7395 -0.1131 0.2089 0.0654  540 PRO A O     
4410  C  CB    . PRO A 540 ? 1.1244 1.004  0.7593 -0.1047 0.2069 0.0629  540 PRO A CB    
4411  C  CG    . PRO A 540 ? 1.1237 1.0208 0.7647 -0.1094 0.2044 0.0669  540 PRO A CG    
4412  C  CD    . PRO A 540 ? 1.0978 1.0098 0.744  -0.1137 0.205  0.0731  540 PRO A CD    
4413  N  N     . LEU A 541 ? 1.1021 0.9628 0.7302 -0.0979 0.2143 0.0628  541 LEU A N     
4414  C  CA    . LEU A 541 ? 1.1046 0.9528 0.7272 -0.1    0.2147 0.0597  541 LEU A CA    
4415  C  C     . LEU A 541 ? 1.105  0.9354 0.7202 -0.1024 0.2117 0.0517  541 LEU A C     
4416  O  O     . LEU A 541 ? 1.1115 0.9341 0.7245 -0.0975 0.2116 0.0486  541 LEU A O     
4417  C  CB    . LEU A 541 ? 1.1096 0.9525 0.7306 -0.0913 0.2198 0.0618  541 LEU A CB    
4418  C  CG    . LEU A 541 ? 1.1349 0.9609 0.7486 -0.0912 0.2205 0.0574  541 LEU A CG    
4419  C  CD1   . LEU A 541 ? 1.1393 0.9696 0.7539 -0.0981 0.2201 0.0591  541 LEU A CD1   
4420  C  CD2   . LEU A 541 ? 1.1468 0.9649 0.7574 -0.0819 0.225  0.0584  541 LEU A CD2   
4421  N  N     . LEU A 542 ? 1.0954 0.9193 0.7067 -0.1095 0.2094 0.0486  542 LEU A N     
4422  C  CA    . LEU A 542 ? 1.0961 0.9027 0.7    -0.1114 0.2071 0.0414  542 LEU A CA    
4423  C  C     . LEU A 542 ? 1.0907 0.8861 0.6897 -0.1103 0.2091 0.0399  542 LEU A C     
4424  O  O     . LEU A 542 ? 1.0926 0.8913 0.6916 -0.1154 0.2093 0.0417  542 LEU A O     
4425  C  CB    . LEU A 542 ? 1.0992 0.9064 0.7014 -0.1208 0.2029 0.039   542 LEU A CB    
4426  C  CG    . LEU A 542 ? 1.1154 0.9319 0.7213 -0.1224 0.2005 0.0399  542 LEU A CG    
4427  C  CD1   . LEU A 542 ? 1.1241 0.9411 0.7275 -0.1323 0.1965 0.038   542 LEU A CD1   
4428  C  CD2   . LEU A 542 ? 1.1283 0.9359 0.7323 -0.1161 0.2004 0.0362  542 LEU A CD2   
4429  N  N     . LEU A 543 ? 1.0816 0.8644 0.6765 -0.1035 0.2108 0.037   543 LEU A N     
4430  C  CA    . LEU A 543 ? 1.0798 0.8511 0.6695 -0.1016 0.2127 0.0353  543 LEU A CA    
4431  C  C     . LEU A 543 ? 1.0794 0.8347 0.662  -0.1042 0.2101 0.0287  543 LEU A C     
4432  O  O     . LEU A 543 ? 1.0857 0.8329 0.666  -0.1007 0.2091 0.0252  543 LEU A O     
4433  C  CB    . LEU A 543 ? 1.0821 0.8496 0.6712 -0.0922 0.2163 0.0368  543 LEU A CB    
4434  C  CG    . LEU A 543 ? 1.1045 0.8594 0.6877 -0.0892 0.2184 0.0352  543 LEU A CG    
4435  C  CD1   . LEU A 543 ? 1.1094 0.8708 0.6942 -0.0922 0.2204 0.0391  543 LEU A CD1   
4436  C  CD2   . LEU A 543 ? 1.114  0.8633 0.6952 -0.0802 0.2215 0.036   543 LEU A CD2   
4437  N  N     . SER A 544 ? 1.0699 0.821  0.649  -0.1104 0.209  0.0271  544 SER A N     
4438  C  CA    . SER A 544 ? 1.0706 0.8065 0.6425 -0.1129 0.2069 0.0213  544 SER A CA    
4439  C  C     . SER A 544 ? 1.0675 0.7912 0.6343 -0.1086 0.2091 0.0195  544 SER A C     
4440  O  O     . SER A 544 ? 1.0685 0.794  0.6352 -0.1092 0.2112 0.022   544 SER A O     
4441  C  CB    . SER A 544 ? 1.0844 0.8213 0.6542 -0.1221 0.2048 0.0204  544 SER A CB    
4442  O  OG    . SER A 544 ? 1.1055 0.8521 0.6789 -0.1263 0.2024 0.0214  544 SER A OG    
4443  N  N     . ILE A 545 ? 1.0625 0.774  0.6251 -0.1042 0.2084 0.0154  545 ILE A N     
4444  C  CA    . ILE A 545 ? 1.0646 0.7642 0.6221 -0.0997 0.2101 0.0137  545 ILE A CA    
4445  C  C     . ILE A 545 ? 1.0641 0.7496 0.6147 -0.102  0.2082 0.0086  545 ILE A C     
4446  O  O     . ILE A 545 ? 1.0661 0.7478 0.6156 -0.1032 0.2057 0.0054  545 ILE A O     
4447  C  CB    . ILE A 545 ? 1.0721 0.7692 0.6303 -0.0917 0.2113 0.0139  545 ILE A CB    
4448  C  CG1   . ILE A 545 ? 1.0776 0.7884 0.6423 -0.0888 0.2134 0.019   545 ILE A CG1   
4449  C  CG2   . ILE A 545 ? 1.0838 0.7692 0.6364 -0.087  0.2131 0.0126  545 ILE A CG2   
4450  C  CD1   . ILE A 545 ? 1.0958 0.804  0.6605 -0.0818 0.2144 0.019   545 ILE A CD1   
4451  N  N     . GLU A 546 ? 1.0593 0.7371 0.6052 -0.1021 0.2096 0.0079  546 GLU A N     
4452  C  CA    . GLU A 546 ? 1.0646 0.7286 0.6035 -0.1032 0.2083 0.0034  546 GLU A CA    
4453  C  C     . GLU A 546 ? 1.0598 0.7145 0.5952 -0.0966 0.2097 0.0025  546 GLU A C     
4454  O  O     . GLU A 546 ? 1.0591 0.7154 0.5947 -0.0942 0.2123 0.0052  546 GLU A O     
4455  C  CB    . GLU A 546 ? 1.0995 0.7614 0.6348 -0.1094 0.2087 0.0033  546 GLU A CB    
4456  C  CG    . GLU A 546 ? 1.1782 0.826  0.7058 -0.1108 0.2075 -0.0011 546 GLU A CG    
4457  C  CD    . GLU A 546 ? 1.2723 0.9185 0.798  -0.1161 0.2051 -0.0035 546 GLU A CD    
4458  O  OE1   . GLU A 546 ? 1.2825 0.9362 0.8128 -0.1168 0.2036 -0.003  546 GLU A OE1   
4459  O  OE2   . GLU A 546 ? 1.31   0.9468 0.8291 -0.1194 0.2049 -0.0059 546 GLU A OE2   
4460  N  N     . SER A 547 ? 1.0549 0.7004 0.5873 -0.0937 0.208  -0.001  547 SER A N     
4461  C  CA    . SER A 547 ? 1.0548 0.6913 0.5836 -0.0878 0.2088 -0.0021 547 SER A CA    
4462  C  C     . SER A 547 ? 1.0492 0.6732 0.5711 -0.0883 0.2081 -0.0053 547 SER A C     
4463  O  O     . SER A 547 ? 1.0536 0.6738 0.5735 -0.0916 0.2063 -0.0079 547 SER A O     
4464  C  CB    . SER A 547 ? 1.0738 0.7093 0.6043 -0.0837 0.2073 -0.0033 547 SER A CB    
4465  O  OG    . SER A 547 ? 1.1038 0.7368 0.6341 -0.0862 0.2045 -0.0063 547 SER A OG    
4466  N  N     . LYS A 548 ? 1.0379 0.6554 0.5558 -0.085  0.2098 -0.0049 548 LYS A N     
4467  C  CA    . LYS A 548 ? 1.0361 0.6416 0.5471 -0.0847 0.2095 -0.0076 548 LYS A CA    
4468  C  C     . LYS A 548 ? 1.0312 0.6289 0.5386 -0.0786 0.2099 -0.0081 548 LYS A C     
4469  O  O     . LYS A 548 ? 1.0297 0.631  0.5392 -0.0751 0.2112 -0.0059 548 LYS A O     
4470  C  CB    . LYS A 548 ? 1.0569 0.6622 0.5654 -0.0883 0.2116 -0.0064 548 LYS A CB    
4471  C  CG    . LYS A 548 ? 1.1041 0.7148 0.6143 -0.0952 0.2109 -0.0063 548 LYS A CG    
4472  C  CD    . LYS A 548 ? 1.1606 0.7636 0.6669 -0.0973 0.2086 -0.0101 548 LYS A CD    
4473  C  CE    . LYS A 548 ? 1.1936 0.8025 0.702  -0.1033 0.2074 -0.0102 548 LYS A CE    
4474  N  NZ    . LYS A 548 ? 1.214  0.8226 0.7192 -0.1092 0.2087 -0.0095 548 LYS A NZ    
4475  N  N     . GLU A 549 ? 1.0271 0.6137 0.5285 -0.0774 0.2089 -0.0108 549 GLU A N     
4476  C  CA    . GLU A 549 ? 1.0269 0.6054 0.5239 -0.0723 0.209  -0.0113 549 GLU A CA    
4477  C  C     . GLU A 549 ? 1.0259 0.6033 0.5203 -0.0706 0.2123 -0.0088 549 GLU A C     
4478  O  O     . GLU A 549 ? 1.0276 0.6042 0.5212 -0.0665 0.2136 -0.0072 549 GLU A O     
4479  C  CB    . GLU A 549 ? 1.0482 0.6161 0.5399 -0.0716 0.2068 -0.0145 549 GLU A CB    
4480  C  CG    . GLU A 549 ? 1.0801 0.6393 0.5667 -0.0668 0.2065 -0.0151 549 GLU A CG    
4481  C  CD    . GLU A 549 ? 1.1251 0.6758 0.6078 -0.0657 0.2036 -0.018  549 GLU A CD    
4482  O  OE1   . GLU A 549 ? 1.1309 0.6833 0.6159 -0.0679 0.2017 -0.0195 549 GLU A OE1   
4483  O  OE2   . GLU A 549 ? 1.1464 0.6891 0.6238 -0.0626 0.2033 -0.0185 549 GLU A OE2   
4484  N  N     . LYS A 550 ? 1.0222 0.5995 0.5151 -0.074  0.2139 -0.0083 550 LYS A N     
4485  C  CA    . LYS A 550 ? 1.026  0.6022 0.5164 -0.0728 0.2172 -0.0058 550 LYS A CA    
4486  C  C     . LYS A 550 ? 1.0235 0.6104 0.5187 -0.077  0.2194 -0.0027 550 LYS A C     
4487  O  O     . LYS A 550 ? 1.0196 0.6115 0.5176 -0.0821 0.2181 -0.0034 550 LYS A O     
4488  C  CB    . LYS A 550 ? 1.0525 0.6169 0.5353 -0.0725 0.2172 -0.008  550 LYS A CB    
4489  C  CG    . LYS A 550 ? 1.1063 0.6606 0.5842 -0.0682 0.215  -0.0106 550 LYS A CG    
4490  C  CD    . LYS A 550 ? 1.166  0.7092 0.6362 -0.0668 0.2157 -0.0119 550 LYS A CD    
4491  C  CE    . LYS A 550 ? 1.2173 0.7512 0.6827 -0.0629 0.2132 -0.0142 550 LYS A CE    
4492  N  NZ    . LYS A 550 ? 1.2473 0.7801 0.7118 -0.0585 0.2136 -0.0128 550 LYS A NZ    
4493  N  N     . PRO A 551 ? 1.0254 0.6157 0.5211 -0.0752 0.2227 0.0009  551 PRO A N     
4494  C  CA    . PRO A 551 ? 1.0239 0.6254 0.5247 -0.0795 0.2248 0.0043  551 PRO A CA    
4495  C  C     . PRO A 551 ? 1.031  0.6301 0.5292 -0.0854 0.2247 0.0031  551 PRO A C     
4496  O  O     . PRO A 551 ? 1.027  0.6353 0.5296 -0.0909 0.2247 0.0047  551 PRO A O     
4497  C  CB    . PRO A 551 ? 1.0306 0.6342 0.5314 -0.0752 0.2286 0.0084  551 PRO A CB    
4498  C  CG    . PRO A 551 ? 1.0417 0.6318 0.535  -0.0698 0.2288 0.0064  551 PRO A CG    
4499  C  CD    . PRO A 551 ? 1.0234 0.6076 0.5151 -0.0692 0.2249 0.0022  551 PRO A CD    
4500  N  N     . ASN A 552 ? 1.0398 0.6263 0.5306 -0.0844 0.2246 0.0003  552 ASN A N     
4501  C  CA    . ASN A 552 ? 1.0496 0.6316 0.5364 -0.0895 0.2247 -0.0013 552 ASN A CA    
4502  C  C     . ASN A 552 ? 1.0516 0.6338 0.5389 -0.0942 0.2218 -0.0041 552 ASN A C     
4503  O  O     . ASN A 552 ? 1.054  0.6346 0.5387 -0.0996 0.222  -0.0048 552 ASN A O     
4504  C  CB    . ASN A 552 ? 1.0751 0.6434 0.5536 -0.0865 0.2256 -0.0033 552 ASN A CB    
4505  C  CG    . ASN A 552 ? 1.1266 0.694  0.6036 -0.0829 0.2291 -0.0004 552 ASN A CG    
4506  O  OD1   . ASN A 552 ? 1.1414 0.7183 0.623  -0.0845 0.2315 0.0034  552 ASN A OD1   
4507  N  ND2   . ASN A 552 ? 1.1423 0.6984 0.6128 -0.078  0.2294 -0.0019 552 ASN A ND2   
4508  N  N     . ASP A 553 ? 1.0496 0.6329 0.5394 -0.0922 0.2191 -0.0057 553 ASP A N     
4509  C  CA    . ASP A 553 ? 1.0541 0.6378 0.5445 -0.0959 0.2164 -0.0081 553 ASP A CA    
4510  C  C     . ASP A 553 ? 1.045  0.641  0.5414 -0.1016 0.2162 -0.0059 553 ASP A C     
4511  O  O     . ASP A 553 ? 1.0466 0.6424 0.5423 -0.1059 0.2145 -0.0077 553 ASP A O     
4512  C  CB    . ASP A 553 ? 1.0815 0.6627 0.573  -0.0917 0.2138 -0.0102 553 ASP A CB    
4513  C  CG    . ASP A 553 ? 1.1562 0.7257 0.6418 -0.0867 0.2134 -0.0123 553 ASP A CG    
4514  O  OD1   . ASP A 553 ? 1.1734 0.7348 0.653  -0.0872 0.2145 -0.0133 553 ASP A OD1   
4515  O  OD2   . ASP A 553 ? 1.1856 0.7542 0.6725 -0.0824 0.2119 -0.013  553 ASP A OD2   
4516  N  N     . LEU A 554 ? 1.0336 0.6403 0.5356 -0.1014 0.218  -0.0019 554 LEU A N     
4517  C  CA    . LEU A 554 ? 1.0269 0.6467 0.5351 -0.1068 0.2178 0.0007  554 LEU A CA    
4518  C  C     . LEU A 554 ? 1.0326 0.6508 0.5372 -0.1137 0.2185 0.0007  554 LEU A C     
4519  O  O     . LEU A 554 ? 1.0351 0.6513 0.5374 -0.114  0.221  0.0022  554 LEU A O     
4520  C  CB    . LEU A 554 ? 1.0188 0.6503 0.5336 -0.1042 0.2199 0.0055  554 LEU A CB    
4521  C  CG    . LEU A 554 ? 1.0291 0.6633 0.5475 -0.0979 0.2195 0.006   554 LEU A CG    
4522  C  CD1   . LEU A 554 ? 1.0289 0.6728 0.5522 -0.0947 0.2224 0.011   554 LEU A CD1   
4523  C  CD2   . LEU A 554 ? 1.033  0.6727 0.5553 -0.1    0.2166 0.0048  554 LEU A CD2   
4524  N  N     . GLU A 555 ? 1.0334 0.6515 0.5368 -0.1193 0.2163 -0.0012 555 GLU A N     
4525  C  CA    . GLU A 555 ? 1.0438 0.6586 0.5423 -0.1266 0.2167 -0.0018 555 GLU A CA    
4526  C  C     . GLU A 555 ? 1.0378 0.6645 0.5409 -0.1319 0.2181 0.0025  555 GLU A C     
4527  O  O     . GLU A 555 ? 1.034  0.674  0.545  -0.1314 0.2179 0.0058  555 GLU A O     
4528  C  CB    . GLU A 555 ? 1.0787 0.6907 0.5747 -0.131  0.214  -0.0047 555 GLU A CB    
4529  C  CG    . GLU A 555 ? 1.1502 0.7501 0.6412 -0.1264 0.2128 -0.0087 555 GLU A CG    
4530  C  CD    . GLU A 555 ? 1.2344 0.8388 0.7307 -0.1227 0.2105 -0.0094 555 GLU A CD    
4531  O  OE1   . GLU A 555 ? 1.2433 0.86   0.7471 -0.1227 0.2101 -0.0067 555 GLU A OE1   
4532  O  OE2   . GLU A 555 ? 1.2712 0.8668 0.7639 -0.1197 0.2093 -0.0125 555 GLU A OE2   
4533  N  N     . PRO A 556 ? 1.0343 0.6568 0.5323 -0.1371 0.2195 0.0026  556 PRO A N     
4534  C  CA    . PRO A 556 ? 1.026  0.6604 0.5284 -0.1429 0.2207 0.0069  556 PRO A CA    
4535  C  C     . PRO A 556 ? 1.0175 0.6636 0.525  -0.149  0.2182 0.0083  556 PRO A C     
4536  O  O     . PRO A 556 ? 1.0194 0.6601 0.5227 -0.1525 0.2158 0.0052  556 PRO A O     
4537  C  CB    . PRO A 556 ? 1.0423 0.6668 0.5364 -0.148  0.2223 0.0056  556 PRO A CB    
4538  C  CG    . PRO A 556 ? 1.0563 0.6645 0.5427 -0.1422 0.2229 0.0015  556 PRO A CG    
4539  C  CD    . PRO A 556 ? 1.0362 0.6429 0.5241 -0.1381 0.2203 -0.001  556 PRO A CD    
4540  N  N     . LYS A 557 ? 1.0053 0.6676 0.5219 -0.1495 0.2186 0.0133  557 LYS A N     
4541  C  CA    . LYS A 557 ? 1.0004 0.6765 0.5231 -0.1548 0.2163 0.0156  557 LYS A CA    
4542  C  C     . LYS A 557 ? 0.9959 0.6729 0.5211 -0.1511 0.2138 0.0136  557 LYS A C     
4543  O  O     . LYS A 557 ? 0.9943 0.6792 0.5223 -0.1561 0.2114 0.0143  557 LYS A O     
4544  C  CB    . LYS A 557 ? 1.0276 0.7031 0.5458 -0.1654 0.2148 0.0151  557 LYS A CB    
4545  C  CG    . LYS A 557 ? 1.0856 0.7623 0.6024 -0.1701 0.2172 0.0177  557 LYS A CG    
4546  C  CD    . LYS A 557 ? 1.1452 0.8184 0.6555 -0.1809 0.2158 0.0166  557 LYS A CD    
4547  C  CE    . LYS A 557 ? 1.1868 0.8752 0.7031 -0.1879 0.213  0.0196  557 LYS A CE    
4548  N  NZ    . LYS A 557 ? 1.2208 0.907  0.7308 -0.1992 0.2119 0.0193  557 LYS A NZ    
4549  N  N     . ILE A 558 ? 0.9922 0.6617 0.5165 -0.1427 0.2143 0.0114  558 ILE A N     
4550  C  CA    . ILE A 558 ? 0.9912 0.6613 0.5179 -0.139  0.2121 0.0095  558 ILE A CA    
4551  C  C     . ILE A 558 ? 0.9827 0.6698 0.519  -0.1385 0.2117 0.0138  558 ILE A C     
4552  O  O     . ILE A 558 ? 0.9826 0.674  0.521  -0.1406 0.2092 0.013   558 ILE A O     
4553  C  CB    . ILE A 558 ? 1.0007 0.6594 0.5244 -0.1305 0.2126 0.0064  558 ILE A CB    
4554  C  CG1   . ILE A 558 ? 1.0116 0.6691 0.5365 -0.128  0.2101 0.0039  558 ILE A CG1   
4555  C  CG2   . ILE A 558 ? 1.0037 0.666  0.5311 -0.1237 0.2153 0.0095  558 ILE A CG2   
4556  C  CD1   . ILE A 558 ? 1.0311 0.6832 0.5515 -0.1335 0.2077 0.0007  558 ILE A CD1   
4557  N  N     . GLY A 559 ? 0.9735 0.6703 0.5153 -0.1361 0.2142 0.0185  559 GLY A N     
4558  C  CA    . GLY A 559 ? 0.9675 0.6812 0.5184 -0.1352 0.2144 0.0234  559 GLY A CA    
4559  C  C     . GLY A 559 ? 0.9638 0.6885 0.5178 -0.1439 0.2119 0.0251  559 GLY A C     
4560  O  O     . GLY A 559 ? 0.9609 0.6939 0.5195 -0.144  0.21   0.0259  559 GLY A O     
4561  N  N     . VAL A 560 ? 0.963  0.6869 0.5138 -0.1516 0.2118 0.0255  560 VAL A N     
4562  C  CA    . VAL A 560 ? 0.9628 0.6957 0.5149 -0.1611 0.2093 0.027   560 VAL A CA    
4563  C  C     . VAL A 560 ? 0.9694 0.6943 0.5164 -0.1642 0.2059 0.0222  560 VAL A C     
4564  O  O     . VAL A 560 ? 0.9643 0.699  0.5151 -0.1678 0.2034 0.0235  560 VAL A O     
4565  C  CB    . VAL A 560 ? 0.9726 0.7049 0.5214 -0.1687 0.2102 0.0283  560 VAL A CB    
4566  C  CG1   . VAL A 560 ? 0.9773 0.7181 0.5265 -0.1794 0.2073 0.0297  560 VAL A CG1   
4567  C  CG2   . VAL A 560 ? 0.9727 0.7141 0.5273 -0.1653 0.2138 0.0336  560 VAL A CG2   
4568  N  N     . GLN A 561 ? 0.979  0.6864 0.5175 -0.162  0.2059 0.0168  561 GLN A N     
4569  C  CA    . GLN A 561 ? 0.9914 0.6895 0.5243 -0.1639 0.2033 0.0122  561 GLN A CA    
4570  C  C     . GLN A 561 ? 0.9965 0.7001 0.5348 -0.1588 0.2018 0.0121  561 GLN A C     
4571  O  O     . GLN A 561 ? 0.9994 0.7029 0.5362 -0.1624 0.1992 0.0104  561 GLN A O     
4572  C  CB    . GLN A 561 ? 1.0155 0.6944 0.5388 -0.1614 0.2042 0.0072  561 GLN A CB    
4573  C  CG    . GLN A 561 ? 1.0523 0.7231 0.568  -0.1676 0.2053 0.0065  561 GLN A CG    
4574  C  CD    . GLN A 561 ? 1.1052 0.7579 0.612  -0.1638 0.2065 0.002   561 GLN A CD    
4575  O  OE1   . GLN A 561 ? 1.1223 0.7704 0.6285 -0.1587 0.2088 0.0021  561 GLN A OE1   
4576  N  NE2   . GLN A 561 ? 1.116  0.7581 0.6156 -0.166  0.2049 -0.0019 561 GLN A NE2   
4577  N  N     . LEU A 562 ? 0.9965 0.7044 0.5406 -0.1506 0.2035 0.0139  562 LEU A N     
4578  C  CA    . LEU A 562 ? 1.0034 0.7166 0.5526 -0.1455 0.2024 0.0139  562 LEU A CA    
4579  C  C     . LEU A 562 ? 1.0046 0.7345 0.5606 -0.1499 0.2008 0.0179  562 LEU A C     
4580  O  O     . LEU A 562 ? 1.0056 0.7372 0.5625 -0.1507 0.1985 0.0166  562 LEU A O     
4581  C  CB    . LEU A 562 ? 1.0045 0.7184 0.5575 -0.1361 0.2049 0.0153  562 LEU A CB    
4582  C  CG    . LEU A 562 ? 1.0294 0.7274 0.5761 -0.1308 0.2061 0.0115  562 LEU A CG    
4583  C  CD1   . LEU A 562 ? 1.0339 0.7333 0.584  -0.1222 0.2084 0.0133  562 LEU A CD1   
4584  C  CD2   . LEU A 562 ? 1.0448 0.731  0.5861 -0.1307 0.2038 0.0064  562 LEU A CD2   
4585  N  N     . ILE A 563 ? 1.0021 0.7443 0.5629 -0.1531 0.202  0.0228  563 ILE A N     
4586  C  CA    . ILE A 563 ? 1.0032 0.7629 0.571  -0.1577 0.2005 0.0274  563 ILE A CA    
4587  C  C     . ILE A 563 ? 1.0163 0.7738 0.5792 -0.1672 0.1971 0.0252  563 ILE A C     
4588  O  O     . ILE A 563 ? 1.0153 0.7803 0.5811 -0.1692 0.1947 0.0258  563 ILE A O     
4589  C  CB    . ILE A 563 ? 1.0014 0.774  0.575  -0.1589 0.2029 0.0334  563 ILE A CB    
4590  C  CG1   . ILE A 563 ? 1.0099 0.7834 0.5873 -0.1489 0.2066 0.0356  563 ILE A CG1   
4591  C  CG2   . ILE A 563 ? 0.9987 0.7905 0.5797 -0.1643 0.2011 0.0385  563 ILE A CG2   
4592  C  CD1   . ILE A 563 ? 1.0213 0.8014 0.6043 -0.1417 0.2069 0.037   563 ILE A CD1   
4593  N  N     . LYS A 564 ? 1.0264 0.7725 0.5811 -0.1728 0.197  0.0225  564 LYS A N     
4594  C  CA    . LYS A 564 ? 1.0402 0.7815 0.5881 -0.1821 0.1941 0.0201  564 LYS A CA    
4595  C  C     . LYS A 564 ? 1.0533 0.785  0.5967 -0.1804 0.1921 0.0156  564 LYS A C     
4596  O  O     . LYS A 564 ? 1.0565 0.7893 0.5971 -0.187  0.1894 0.0149  564 LYS A O     
4597  C  CB    . LYS A 564 ? 1.0716 0.8009 0.6106 -0.1877 0.1951 0.0181  564 LYS A CB    
4598  C  CG    . LYS A 564 ? 1.1224 0.8614 0.6653 -0.1911 0.1969 0.0228  564 LYS A CG    
4599  C  CD    . LYS A 564 ? 1.1719 0.9289 0.721  -0.1989 0.1947 0.0277  564 LYS A CD    
4600  C  CE    . LYS A 564 ? 1.2169 0.9832 0.7696 -0.2028 0.1966 0.0325  564 LYS A CE    
4601  N  NZ    . LYS A 564 ? 1.2416 1.0169 0.8031 -0.1938 0.1999 0.0364  564 LYS A NZ    
4602  N  N     . TYR A 565 ? 1.0598 0.7824 0.6026 -0.1716 0.1934 0.0126  565 TYR A N     
4603  C  CA    . TYR A 565 ? 1.074  0.7883 0.6133 -0.1693 0.1917 0.0087  565 TYR A CA    
4604  C  C     . TYR A 565 ? 1.0737 0.8016 0.6206 -0.1684 0.19   0.0111  565 TYR A C     
4605  O  O     . TYR A 565 ? 1.0772 0.8029 0.6211 -0.1716 0.1876 0.0093  565 TYR A O     
4606  C  CB    . TYR A 565 ? 1.0808 0.7833 0.6183 -0.1604 0.1934 0.0054  565 TYR A CB    
4607  C  CG    . TYR A 565 ? 1.0963 0.7882 0.629  -0.1587 0.1919 0.0011  565 TYR A CG    
4608  C  CD1   . TYR A 565 ? 1.1152 0.7922 0.6379 -0.162  0.1916 -0.0027 565 TYR A CD1   
4609  C  CD2   . TYR A 565 ? 1.1048 0.8013 0.6427 -0.1537 0.191  0.0011  565 TYR A CD2   
4610  C  CE1   . TYR A 565 ? 1.131  0.7983 0.6493 -0.16   0.1906 -0.0062 565 TYR A CE1   
4611  C  CE2   . TYR A 565 ? 1.1204 0.8076 0.6542 -0.152  0.1898 -0.0025 565 TYR A CE2   
4612  C  CZ    . TYR A 565 ? 1.1395 0.8123 0.6637 -0.1551 0.1896 -0.0061 565 TYR A CZ    
4613  O  OH    . TYR A 565 ? 1.1634 0.8271 0.6836 -0.1531 0.1888 -0.0093 565 TYR A OH    
4614  N  N     . ILE A 566 ? 1.0685 0.8098 0.6246 -0.1637 0.1913 0.0154  566 ILE A N     
4615  C  CA    . ILE A 566 ? 1.0706 0.8259 0.6343 -0.1622 0.1901 0.0183  566 ILE A CA    
4616  C  C     . ILE A 566 ? 1.0778 0.8436 0.6421 -0.1718 0.1874 0.0209  566 ILE A C     
4617  O  O     . ILE A 566 ? 1.0757 0.8451 0.6405 -0.1738 0.185  0.0205  566 ILE A O     
4618  C  CB    . ILE A 566 ? 1.0688 0.8355 0.6413 -0.1549 0.1928 0.0228  566 ILE A CB    
4619  C  CG1   . ILE A 566 ? 1.0848 0.8399 0.6554 -0.146  0.1952 0.0201  566 ILE A CG1   
4620  C  CG2   . ILE A 566 ? 1.0659 0.8471 0.6461 -0.1527 0.1918 0.0261  566 ILE A CG2   
4621  C  CD1   . ILE A 566 ? 1.1042 0.8498 0.6722 -0.1416 0.1941 0.0158  566 ILE A CD1   
4622  N  N     . GLU A 567 ? 1.0846 0.8543 0.6481 -0.1782 0.1877 0.0233  567 GLU A N     
4623  C  CA    . GLU A 567 ? 1.095  0.874  0.6584 -0.1885 0.185  0.0258  567 GLU A CA    
4624  C  C     . GLU A 567 ? 1.1112 0.8778 0.6645 -0.195  0.1822 0.0211  567 GLU A C     
4625  O  O     . GLU A 567 ? 1.1095 0.8834 0.663  -0.2012 0.1793 0.0224  567 GLU A O     
4626  C  CB    . GLU A 567 ? 1.1236 0.9068 0.6872 -0.1938 0.1863 0.0288  567 GLU A CB    
4627  C  CG    . GLU A 567 ? 1.1733 0.9712 0.7472 -0.1881 0.1891 0.0345  567 GLU A CG    
4628  C  CD    . GLU A 567 ? 1.2501 1.0546 0.8255 -0.1932 0.1904 0.0383  567 GLU A CD    
4629  O  OE1   . GLU A 567 ? 1.2721 1.069  0.8401 -0.2017 0.1892 0.0364  567 GLU A OE1   
4630  O  OE2   . GLU A 567 ? 1.2691 1.0861 0.853  -0.1887 0.1929 0.0435  567 GLU A OE2   
4631  N  N     . TYR A 568 ? 1.1248 0.8723 0.6691 -0.1931 0.1833 0.0159  568 TYR A N     
4632  C  CA    . TYR A 568 ? 1.1426 0.8755 0.6761 -0.1977 0.1815 0.0112  568 TYR A CA    
4633  C  C     . TYR A 568 ? 1.142  0.8765 0.6773 -0.1947 0.1796 0.01    568 TYR A C     
4634  O  O     . TYR A 568 ? 1.1429 0.8765 0.6734 -0.2013 0.177  0.0092  568 TYR A O     
4635  C  CB    . TYR A 568 ? 1.1575 0.8711 0.6826 -0.1941 0.1837 0.0066  568 TYR A CB    
4636  C  CG    . TYR A 568 ? 1.1824 0.8796 0.6972 -0.1951 0.1828 0.0017  568 TYR A CG    
4637  C  CD1   . TYR A 568 ? 1.2023 0.8919 0.7072 -0.2044 0.1812 0.0002  568 TYR A CD1   
4638  C  CD2   . TYR A 568 ? 1.1996 0.8878 0.7139 -0.1868 0.1837 -0.0015 568 TYR A CD2   
4639  C  CE1   . TYR A 568 ? 1.2242 0.8978 0.7188 -0.2048 0.1809 -0.0041 568 TYR A CE1   
4640  C  CE2   . TYR A 568 ? 1.2205 0.8939 0.7256 -0.1872 0.1832 -0.0056 568 TYR A CE2   
4641  C  CZ    . TYR A 568 ? 1.2385 0.9044 0.7335 -0.196  0.182  -0.0069 568 TYR A CZ    
4642  O  OH    . TYR A 568 ? 1.2662 0.9167 0.7514 -0.196  0.1819 -0.0107 568 TYR A OH    
4643  N  N     . LEU A 569 ? 1.1391 0.876  0.6809 -0.1851 0.1809 0.01    569 LEU A N     
4644  C  CA    . LEU A 569 ? 1.1438 0.8827 0.6877 -0.1817 0.1794 0.009   569 LEU A CA    
4645  C  C     . LEU A 569 ? 1.144  0.9007 0.6947 -0.1857 0.1772 0.0134  569 LEU A C     
4646  O  O     . LEU A 569 ? 1.1469 0.9036 0.6953 -0.1883 0.1749 0.0124  569 LEU A O     
4647  C  CB    . LEU A 569 ? 1.142  0.8793 0.6912 -0.1708 0.1815 0.0082  569 LEU A CB    
4648  C  CG    . LEU A 569 ? 1.1649 0.8851 0.7079 -0.1663 0.1833 0.0039  569 LEU A CG    
4649  C  CD1   . LEU A 569 ? 1.17   0.8904 0.7186 -0.1564 0.1851 0.0037  569 LEU A CD1   
4650  C  CD2   . LEU A 569 ? 1.1801 0.8859 0.7136 -0.169  0.182  -0.0005 569 LEU A CD2   
4651  N  N     . PHE A 570 ? 1.1391 0.911  0.6978 -0.1862 0.178  0.0184  570 PHE A N     
4652  C  CA    . PHE A 570 ? 1.1392 0.9298 0.7049 -0.19   0.176  0.0234  570 PHE A CA    
4653  C  C     . PHE A 570 ? 1.148  0.9389 0.7074 -0.2017 0.1725 0.0233  570 PHE A C     
4654  O  O     . PHE A 570 ? 1.1435 0.9469 0.7067 -0.2052 0.17   0.0261  570 PHE A O     
4655  C  CB    . PHE A 570 ? 1.1309 0.9373 0.7062 -0.1878 0.178  0.0292  570 PHE A CB    
4656  C  CG    . PHE A 570 ? 1.1352 0.9469 0.7183 -0.1766 0.1808 0.0309  570 PHE A CG    
4657  C  CD1   . PHE A 570 ? 1.1438 0.9553 0.7287 -0.1711 0.1803 0.0296  570 PHE A CD1   
4658  C  CD2   . PHE A 570 ? 1.1421 0.9584 0.7301 -0.1718 0.1841 0.0339  570 PHE A CD2   
4659  C  CE1   . PHE A 570 ? 1.1481 0.9638 0.7394 -0.1612 0.183  0.0312  570 PHE A CE1   
4660  C  CE2   . PHE A 570 ? 1.1463 0.9667 0.7404 -0.1617 0.1868 0.0356  570 PHE A CE2   
4661  C  CZ    . PHE A 570 ? 1.1423 0.9619 0.7377 -0.1566 0.1862 0.0341  570 PHE A CZ    
4662  N  N     . ASP A 571 ? 1.1596 0.9361 0.7087 -0.2077 0.1724 0.02    571 ASP A N     
4663  C  CA    . ASP A 571 ? 1.1739 0.9472 0.7146 -0.219  0.1692 0.0192  571 ASP A CA    
4664  C  C     . ASP A 571 ? 1.1819 0.9462 0.7159 -0.2198 0.1671 0.0156  571 ASP A C     
4665  O  O     . ASP A 571 ? 1.1893 0.9512 0.716  -0.229  0.1642 0.015   571 ASP A O     
4666  C  CB    . ASP A 571 ? 1.2098 0.9684 0.7403 -0.2245 0.1703 0.0165  571 ASP A CB    
4667  C  CG    . ASP A 571 ? 1.2699 1.0382 0.8051 -0.2279 0.1715 0.0206  571 ASP A CG    
4668  O  OD1   . ASP A 571 ? 1.2711 1.0589 0.817  -0.2279 0.171  0.0261  571 ASP A OD1   
4669  O  OD2   . ASP A 571 ? 1.304  1.0603 0.832  -0.2305 0.1732 0.0185  571 ASP A OD2   
4670  N  N     . PHE A 572 ? 1.1787 0.9374 0.7146 -0.2104 0.1684 0.0131  572 PHE A N     
4671  C  CA    . PHE A 572 ? 1.1851 0.9354 0.7154 -0.2099 0.1668 0.0098  572 PHE A CA    
4672  C  C     . PHE A 572 ? 1.1757 0.9377 0.7157 -0.2028 0.1666 0.0117  572 PHE A C     
4673  O  O     . PHE A 572 ? 1.1721 0.9425 0.7213 -0.1954 0.1688 0.014   572 PHE A O     
4674  C  CB    . PHE A 572 ? 1.1965 0.9256 0.7179 -0.2056 0.1689 0.0043  572 PHE A CB    
4675  C  CG    . PHE A 572 ? 1.2165 0.9325 0.7275 -0.2119 0.1696 0.0022  572 PHE A CG    
4676  C  CD1   . PHE A 572 ? 1.2355 0.9431 0.7353 -0.2213 0.1676 0.0007  572 PHE A CD1   
4677  C  CD2   . PHE A 572 ? 1.2292 0.9409 0.7409 -0.2085 0.1724 0.0019  572 PHE A CD2   
4678  C  CE1   . PHE A 572 ? 1.2538 0.9486 0.7432 -0.2271 0.1685 -0.0012 572 PHE A CE1   
4679  C  CE2   . PHE A 572 ? 1.2466 0.9463 0.7486 -0.2143 0.1732 0.0001  572 PHE A CE2   
4680  C  CZ    . PHE A 572 ? 1.2517 0.943  0.7426 -0.2235 0.1713 -0.0014 572 PHE A CZ    
4681  N  N     . THR A 573 ? 1.1703 0.9319 0.7074 -0.2049 0.1642 0.0108  573 THR A N     
4682  C  CA    . THR A 573 ? 1.1637 0.9349 0.7086 -0.1984 0.1639 0.0123  573 THR A CA    
4683  C  C     . THR A 573 ? 1.1645 0.9259 0.7109 -0.1878 0.1669 0.0092  573 THR A C     
4684  O  O     . THR A 573 ? 1.1728 0.9171 0.7109 -0.1871 0.1678 0.0047  573 THR A O     
4685  C  CB    . THR A 573 ? 1.182  0.9507 0.7209 -0.2036 0.1608 0.011   573 THR A CB    
4686  O  OG1   . THR A 573 ? 1.1902 0.9687 0.7278 -0.2139 0.1578 0.0141  573 THR A OG1   
4687  C  CG2   . THR A 573 ? 1.1835 0.9596 0.729  -0.1968 0.1607 0.0118  573 THR A CG2   
4688  N  N     . PRO A 574 ? 1.1557 0.9272 0.7122 -0.1796 0.1686 0.0115  574 PRO A N     
4689  C  CA    . PRO A 574 ? 1.1594 0.9213 0.7169 -0.1701 0.1711 0.0085  574 PRO A CA    
4690  C  C     . PRO A 574 ? 1.169  0.9188 0.7202 -0.1689 0.1703 0.0045  574 PRO A C     
4691  O  O     . PRO A 574 ? 1.1709 0.9247 0.7207 -0.1726 0.168  0.005   574 PRO A O     
4692  C  CB    . PRO A 574 ? 1.1587 0.9352 0.7272 -0.163  0.1724 0.0123  574 PRO A CB    
4693  C  CG    . PRO A 574 ? 1.1563 0.9497 0.7302 -0.1678 0.1715 0.0175  574 PRO A CG    
4694  C  CD    . PRO A 574 ? 1.1393 0.9311 0.7062 -0.1785 0.1683 0.0171  574 PRO A CD    
4695  N  N     . SER A 575 ? 1.1734 0.9088 0.7208 -0.1637 0.1721 0.0007  575 SER A N     
4696  C  CA    . SER A 575 ? 1.1849 0.9085 0.7265 -0.1621 0.1717 -0.003  575 SER A CA    
4697  C  C     . SER A 575 ? 1.1821 0.9142 0.7298 -0.1578 0.1711 -0.0017 575 SER A C     
4698  O  O     . SER A 575 ? 1.1839 0.914  0.7275 -0.1608 0.1693 -0.0026 575 SER A O     
4699  C  CB    . SER A 575 ? 1.2075 0.9168 0.746  -0.1563 0.1739 -0.0064 575 SER A CB    
4700  O  OG    . SER A 575 ? 1.2406 0.9418 0.7733 -0.1598 0.1747 -0.0075 575 SER A OG    
4701  N  N     . VAL A 576 ? 1.176  0.9175 0.7328 -0.1511 0.1726 0.0005  576 VAL A N     
4702  C  CA    . VAL A 576 ? 1.1791 0.9285 0.7418 -0.1462 0.1725 0.0018  576 VAL A CA    
4703  C  C     . VAL A 576 ? 1.1764 0.9428 0.7488 -0.1434 0.1733 0.0066  576 VAL A C     
4704  O  O     . VAL A 576 ? 1.1771 0.9479 0.752  -0.1438 0.1744 0.0086  576 VAL A O     
4705  C  CB    . VAL A 576 ? 1.193  0.9318 0.7555 -0.1386 0.1742 -0.0014 576 VAL A CB    
4706  C  CG1   . VAL A 576 ? 1.2082 0.9331 0.7622 -0.1407 0.1733 -0.0052 576 VAL A CG1   
4707  C  CG2   . VAL A 576 ? 1.2015 0.9349 0.7655 -0.1339 0.1765 -0.0023 576 VAL A CG2   
4708  N  N     . GLN A 577 ? 1.1721 0.9478 0.7496 -0.1402 0.1731 0.0085  577 GLN A N     
4709  C  CA    . GLN A 577 ? 1.1709 0.9625 0.7573 -0.1363 0.1743 0.0133  577 GLN A CA    
4710  C  C     . GLN A 577 ? 1.1742 0.9688 0.7646 -0.1296 0.1751 0.0136  577 GLN A C     
4711  O  O     . GLN A 577 ? 1.1807 0.9689 0.7673 -0.1302 0.1738 0.011   577 GLN A O     
4712  C  CB    . GLN A 577 ? 1.1832 0.9895 0.772  -0.1433 0.1722 0.0177  577 GLN A CB    
4713  C  CG    . GLN A 577 ? 1.2187 1.0297 0.8057 -0.1478 0.1692 0.0181  577 GLN A CG    
4714  C  CD    . GLN A 577 ? 1.2556 1.0832 0.8507 -0.1441 0.1694 0.0227  577 GLN A CD    
4715  O  OE1   . GLN A 577 ? 1.2657 1.1046 0.868  -0.1402 0.1715 0.0268  577 GLN A OE1   
4716  N  NE2   . GLN A 577 ? 1.2574 1.0867 0.8513 -0.1449 0.1676 0.0223  577 GLN A NE2   
4717  N  N     . ARG A 578 ? 1.1689 0.9727 0.7663 -0.1232 0.1775 0.0168  578 ARG A N     
4718  C  CA    . ARG A 578 ? 1.1744 0.9813 0.7753 -0.1167 0.1787 0.0174  578 ARG A CA    
4719  C  C     . ARG A 578 ? 1.1747 0.9962 0.7831 -0.1117 0.181  0.0227  578 ARG A C     
4720  O  O     . ARG A 578 ? 1.1751 1.0008 0.7858 -0.1113 0.1825 0.0251  578 ARG A O     
4721  C  CB    . ARG A 578 ? 1.1938 0.9862 0.7922 -0.1108 0.1803 0.0131  578 ARG A CB    
4722  C  CG    . ARG A 578 ? 1.2258 1.0139 0.8255 -0.106  0.1831 0.0131  578 ARG A CG    
4723  C  CD    . ARG A 578 ? 1.2612 1.0401 0.8606 -0.099  0.1849 0.0105  578 ARG A CD    
4724  N  NE    . ARG A 578 ? 1.2912 1.066  0.8913 -0.0945 0.1874 0.0106  578 ARG A NE    
4725  C  CZ    . ARG A 578 ? 1.3183 1.0863 0.9185 -0.0882 0.1893 0.0091  578 ARG A CZ    
4726  N  NH1   . ARG A 578 ? 1.3121 1.0772 0.9124 -0.0855 0.1891 0.0075  578 ARG A NH1   
4727  N  NH2   . ARG A 578 ? 1.3213 1.0852 0.9212 -0.0847 0.1913 0.0092  578 ARG A NH2   
4728  N  N     . LYS A 579 ? 1.1729 1.0016 0.7847 -0.1077 0.1814 0.0246  579 LYS A N     
4729  C  CA    . LYS A 579 ? 1.1744 1.0161 0.7928 -0.102  0.1841 0.0297  579 LYS A CA    
4730  C  C     . LYS A 579 ? 1.1837 1.0167 0.8021 -0.0937 0.1878 0.0282  579 LYS A C     
4731  O  O     . LYS A 579 ? 1.1922 1.0127 0.8072 -0.0915 0.1878 0.0239  579 LYS A O     
4732  C  CB    . LYS A 579 ? 1.191  1.0442 0.8127 -0.1011 0.1833 0.0326  579 LYS A CB    
4733  C  CG    . LYS A 579 ? 1.232  1.0993 0.8602 -0.095  0.1863 0.0384  579 LYS A CG    
4734  C  CD    . LYS A 579 ? 1.2791 1.1592 0.9106 -0.0946 0.1852 0.0418  579 LYS A CD    
4735  C  CE    . LYS A 579 ? 1.3204 1.2142 0.954  -0.1026 0.1819 0.0453  579 LYS A CE    
4736  N  NZ    . LYS A 579 ? 1.3446 1.2489 0.9825 -0.1032 0.1833 0.0501  579 LYS A NZ    
4737  N  N     . ILE A 580 ? 1.1796 1.0187 0.8015 -0.0891 0.1909 0.032   580 ILE A N     
4738  C  CA    . ILE A 580 ? 1.1883 1.0188 0.8093 -0.0815 0.1944 0.0309  580 ILE A CA    
4739  C  C     . ILE A 580 ? 1.1899 1.0195 0.8117 -0.0752 0.196  0.0307  580 ILE A C     
4740  O  O     . ILE A 580 ? 1.1953 1.0139 0.8146 -0.0702 0.198  0.0281  580 ILE A O     
4741  C  CB    . ILE A 580 ? 1.1947 1.0318 0.8184 -0.0783 0.1976 0.0353  580 ILE A CB    
4742  C  CG1   . ILE A 580 ? 1.2141 1.0379 0.8344 -0.0729 0.2003 0.0328  580 ILE A CG1   
4743  C  CG2   . ILE A 580 ? 1.1949 1.0476 0.824  -0.074  0.1998 0.0415  580 ILE A CG2   
4744  C  CD1   . ILE A 580 ? 1.2375 1.0467 0.8527 -0.0767 0.1983 0.0273  580 ILE A CD1   
4745  N  N     . ALA A 581 ? 1.1842 1.0245 0.8088 -0.0758 0.195  0.0332  581 ALA A N     
4746  C  CA    . ALA A 581 ? 1.1899 1.0295 0.8151 -0.0701 0.1965 0.033   581 ALA A CA    
4747  C  C     . ALA A 581 ? 1.1962 1.0263 0.818  -0.0729 0.1937 0.0281  581 ALA A C     
4748  O  O     . ALA A 581 ? 1.2017 1.0226 0.8217 -0.0684 0.1951 0.0254  581 ALA A O     
4749  C  CB    . ALA A 581 ? 1.1855 1.0421 0.8156 -0.0683 0.1973 0.0388  581 ALA A CB    
4750  N  N     . GLY A 582 ? 1.1931 1.025  0.8136 -0.0804 0.19   0.027   582 GLY A N     
4751  C  CA    . GLY A 582 ? 1.2007 1.0234 0.8172 -0.0834 0.1875 0.0226  582 GLY A CA    
4752  C  C     . GLY A 582 ? 1.2084 1.0145 0.8204 -0.0833 0.1876 0.0174  582 GLY A C     
4753  O  O     . GLY A 582 ? 1.2132 1.0103 0.8236 -0.0799 0.1883 0.0145  582 GLY A O     
4754  N  N     . GLY A 583 ? 1.2074 1.0099 0.8176 -0.0871 0.1869 0.0166  583 GLY A N     
4755  C  CA    . GLY A 583 ? 1.2171 1.0047 0.8231 -0.0871 0.1869 0.0122  583 GLY A CA    
4756  C  C     . GLY A 583 ? 1.222  1.0004 0.8229 -0.0925 0.1842 0.0083  583 GLY A C     
4757  O  O     . GLY A 583 ? 1.2291 0.9957 0.8264 -0.093  0.1841 0.005   583 GLY A O     
4758  N  N     . ASN A 584 ? 1.2162 0.9993 0.8162 -0.0965 0.182  0.0088  584 ASN A N     
4759  C  CA    . ASN A 584 ? 1.2236 0.9973 0.8176 -0.1015 0.1797 0.0053  584 ASN A CA    
4760  C  C     . ASN A 584 ? 1.2235 0.9972 0.8141 -0.1089 0.1778 0.0054  584 ASN A C     
4761  O  O     . ASN A 584 ? 1.2213 1.0065 0.8138 -0.113  0.1765 0.0087  584 ASN A O     
4762  C  CB    . ASN A 584 ? 1.2374 1.0147 0.8309 -0.1025 0.1783 0.0057  584 ASN A CB    
4763  C  CG    . ASN A 584 ? 1.2767 1.0548 0.8737 -0.0954 0.1803 0.0059  584 ASN A CG    
4764  O  OD1   . ASN A 584 ? 1.2937 1.0651 0.8917 -0.0901 0.1824 0.0044  584 ASN A OD1   
4765  N  ND2   . ASN A 584 ? 1.2819 1.0681 0.8804 -0.0952 0.1796 0.0078  584 ASN A ND2   
4766  N  N     . TRP A 585 ? 1.2237 0.9847 0.8092 -0.1107 0.1777 0.002   585 TRP A N     
4767  C  CA    . TRP A 585 ? 1.2264 0.9854 0.8075 -0.1176 0.1762 0.0018  585 TRP A CA    
4768  C  C     . TRP A 585 ? 1.2314 0.9898 0.8072 -0.1247 0.1734 0.0012  585 TRP A C     
4769  O  O     . TRP A 585 ? 1.2375 0.9885 0.8095 -0.1243 0.1729 -0.0011 585 TRP A O     
4770  C  CB    . TRP A 585 ? 1.2287 0.9735 0.8053 -0.1171 0.1771 -0.0017 585 TRP A CB    
4771  C  CG    . TRP A 585 ? 1.2289 0.9733 0.8092 -0.112  0.1793 -0.0012 585 TRP A CG    
4772  C  CD1   . TRP A 585 ? 1.2406 0.9784 0.8223 -0.1056 0.181  -0.0029 585 TRP A CD1   
4773  C  CD2   . TRP A 585 ? 1.2264 0.9762 0.8087 -0.1132 0.1801 0.001   585 TRP A CD2   
4774  N  NE1   . TRP A 585 ? 1.2434 0.9819 0.8274 -0.1027 0.1827 -0.0019 585 TRP A NE1   
4775  C  CE2   . TRP A 585 ? 1.2368 0.9825 0.8212 -0.107  0.1823 0.0005  585 TRP A CE2   
4776  C  CE3   . TRP A 585 ? 1.2299 0.9877 0.8123 -0.119  0.1791 0.0036  585 TRP A CE3   
4777  C  CZ2   . TRP A 585 ? 1.2424 0.9913 0.8287 -0.1062 0.1837 0.0024  585 TRP A CZ2   
4778  C  CZ3   . TRP A 585 ? 1.2381 0.9997 0.823  -0.1181 0.1806 0.0056  585 TRP A CZ3   
4779  C  CH2   . TRP A 585 ? 1.2406 0.9975 0.8272 -0.1115 0.183  0.005   585 TRP A CH2   
4780  N  N     . GLU A 586 ? 1.2278 0.9933 0.8027 -0.1313 0.1718 0.0034  586 GLU A N     
4781  C  CA    . GLU A 586 ? 1.2347 0.9996 0.8034 -0.1394 0.1689 0.0032  586 GLU A CA    
4782  C  C     . GLU A 586 ? 1.2395 0.9991 0.8027 -0.1461 0.1681 0.0024  586 GLU A C     
4783  O  O     . GLU A 586 ? 1.2396 0.9998 0.8055 -0.1444 0.1697 0.003   586 GLU A O     
4784  C  CB    . GLU A 586 ? 1.256  1.038  0.8297 -0.142  0.1671 0.0076  586 GLU A CB    
4785  C  CG    . GLU A 586 ? 1.3139 1.1001 0.8907 -0.1371 0.1673 0.0082  586 GLU A CG    
4786  C  CD    . GLU A 586 ? 1.3833 1.1819 0.961  -0.1418 0.1646 0.0113  586 GLU A CD    
4787  O  OE1   . GLU A 586 ? 1.3967 1.201  0.9724 -0.1495 0.1622 0.0131  586 GLU A OE1   
4788  O  OE2   . GLU A 586 ? 1.4039 1.2064 0.984  -0.1378 0.1647 0.0119  586 GLU A OE2   
4789  N  N     . PHE A 587 ? 1.2418 0.9956 0.7966 -0.1538 0.1658 0.0011  587 PHE A N     
4790  C  CA    . PHE A 587 ? 1.2488 0.9975 0.7976 -0.1609 0.165  0.0005  587 PHE A CA    
4791  C  C     . PHE A 587 ? 1.2452 1.0103 0.8002 -0.1647 0.1641 0.0051  587 PHE A C     
4792  O  O     . PHE A 587 ? 1.2384 1.018  0.7994 -0.1647 0.1629 0.0086  587 PHE A O     
4793  C  CB    . PHE A 587 ? 1.2531 0.9918 0.7906 -0.1685 0.1628 -0.0017 587 PHE A CB    
4794  C  CG    . PHE A 587 ? 1.2667 0.9867 0.796  -0.1659 0.1641 -0.0062 587 PHE A CG    
4795  C  CD1   . PHE A 587 ? 1.2786 0.9882 0.8066 -0.1622 0.1666 -0.0084 587 PHE A CD1   
4796  C  CD2   . PHE A 587 ? 1.2798 0.9925 0.8024 -0.1675 0.163  -0.0079 587 PHE A CD2   
4797  C  CE1   . PHE A 587 ? 1.2939 0.9872 0.8146 -0.1596 0.1679 -0.0121 587 PHE A CE1   
4798  C  CE2   . PHE A 587 ? 1.2957 0.9914 0.8107 -0.1649 0.1646 -0.0116 587 PHE A CE2   
4799  C  CZ    . PHE A 587 ? 1.2955 0.9819 0.8098 -0.1609 0.1671 -0.0135 587 PHE A CZ    
4800  N  N     . GLY A 588 ? 1.2475 1.0104 0.8011 -0.1675 0.1648 0.0052  588 GLY A N     
4801  C  CA    . GLY A 588 ? 1.248  1.0257 0.8073 -0.1712 0.1642 0.0097  588 GLY A CA    
4802  C  C     . GLY A 588 ? 1.2509 1.0367 0.8074 -0.1808 0.1607 0.0119  588 GLY A C     
4803  O  O     . GLY A 588 ? 1.259  1.0337 0.8053 -0.1875 0.1589 0.0092  588 GLY A O     
4804  N  N     . ASN A 589 ? 1.2424 1.0471 0.8074 -0.1815 0.1596 0.017   589 ASN A N     
4805  C  CA    . ASN A 589 ? 1.2463 1.0612 0.8098 -0.1906 0.1559 0.0198  589 ASN A CA    
4806  C  C     . ASN A 589 ? 1.2433 1.0713 0.8112 -0.1963 0.1553 0.0243  589 ASN A C     
4807  O  O     . ASN A 589 ? 1.2465 1.0746 0.8085 -0.2064 0.1524 0.0248  589 ASN A O     
4808  C  CB    . ASN A 589 ? 1.2552 1.0827 0.8247 -0.1873 0.1548 0.0225  589 ASN A CB    
4809  C  CG    . ASN A 589 ? 1.2896 1.1303 0.859  -0.1961 0.1507 0.0262  589 ASN A CG    
4810  O  OD1   . ASN A 589 ? 1.308  1.1419 0.8683 -0.2055 0.1479 0.0247  589 ASN A OD1   
4811  N  ND2   . ASN A 589 ? 1.2881 1.1479 0.8675 -0.1932 0.1505 0.0314  589 ASN A ND2   
4812  N  N     . LYS A 590 ? 1.2353 1.0742 0.813  -0.19   0.1579 0.0278  590 LYS A N     
4813  C  CA    . LYS A 590 ? 1.2343 1.087  0.8174 -0.1944 0.1578 0.0327  590 LYS A CA    
4814  C  C     . LYS A 590 ? 1.2396 1.0831 0.8209 -0.1933 0.1605 0.031   590 LYS A C     
4815  O  O     . LYS A 590 ? 1.2452 1.078  0.8261 -0.1853 0.1635 0.0279  590 LYS A O     
4816  C  CB    . LYS A 590 ? 1.2478 1.1209 0.8433 -0.1884 0.1591 0.0387  590 LYS A CB    
4817  C  CG    . LYS A 590 ? 1.2964 1.1808 0.8947 -0.1891 0.1565 0.0411  590 LYS A CG    
4818  C  CD    . LYS A 590 ? 1.3427 1.2451 0.9528 -0.1811 0.1587 0.0468  590 LYS A CD    
4819  C  CE    . LYS A 590 ? 1.3869 1.3001 0.9997 -0.1807 0.1565 0.0491  590 LYS A CE    
4820  N  NZ    . LYS A 590 ? 1.407  1.336  1.0305 -0.1718 0.1594 0.0545  590 LYS A NZ    
4821  N  N     . SER A 591 ? 1.2355 1.0834 0.8156 -0.2012 0.1594 0.0332  591 SER A N     
4822  C  CA    . SER A 591 ? 1.2409 1.081  0.8192 -0.2009 0.162  0.032   591 SER A CA    
4823  C  C     . SER A 591 ? 1.229  1.0826 0.8182 -0.1942 0.1651 0.0369  591 SER A C     
4824  O  O     . SER A 591 ? 1.2209 1.093  0.8189 -0.1932 0.1647 0.0424  591 SER A O     
4825  C  CB    . SER A 591 ? 1.2634 1.1014 0.835  -0.2126 0.1596 0.0322  591 SER A CB    
4826  O  OG    . SER A 591 ? 1.3058 1.1222 0.8651 -0.2155 0.1596 0.0262  591 SER A OG    
4827  N  N     . LEU A 592 ? 1.226  1.0701 0.8142 -0.1896 0.1683 0.035   592 LEU A N     
4828  C  CA    . LEU A 592 ? 1.2179 1.0723 0.8149 -0.1832 0.1717 0.0393  592 LEU A CA    
4829  C  C     . LEU A 592 ? 1.2118 1.0682 0.8079 -0.1893 0.1722 0.0413  592 LEU A C     
4830  O  O     . LEU A 592 ? 1.2213 1.0639 0.8086 -0.1951 0.1713 0.0374  592 LEU A O     
4831  C  CB    . LEU A 592 ? 1.2255 1.0684 0.8224 -0.1725 0.1752 0.0361  592 LEU A CB    
4832  C  CG    . LEU A 592 ? 1.2426 1.0905 0.845  -0.1636 0.1764 0.037   592 LEU A CG    
4833  C  CD1   . LEU A 592 ? 1.2531 1.0955 0.8513 -0.1654 0.1736 0.0337  592 LEU A CD1   
4834  C  CD2   . LEU A 592 ? 1.2555 1.093  0.8579 -0.154  0.1801 0.0347  592 LEU A CD2   
4835  N  N     . VAL A 593 ? 1.1943 1.0679 0.7995 -0.1881 0.1737 0.0477  593 VAL A N     
4836  C  CA    . VAL A 593 ? 1.1905 1.0685 0.7963 -0.1939 0.1743 0.0505  593 VAL A CA    
4837  C  C     . VAL A 593 ? 1.1837 1.0609 0.7936 -0.1854 0.179  0.0521  593 VAL A C     
4838  O  O     . VAL A 593 ? 1.1791 1.0644 0.7962 -0.1766 0.1816 0.0551  593 VAL A O     
4839  C  CB    . VAL A 593 ? 1.1905 1.0901 0.8029 -0.2014 0.1717 0.0571  593 VAL A CB    
4840  C  CG1   . VAL A 593 ? 1.1957 1.1021 0.8103 -0.2067 0.1727 0.061   593 VAL A CG1   
4841  C  CG2   . VAL A 593 ? 1.1986 1.0965 0.8049 -0.2109 0.1668 0.0551  593 VAL A CG2   
4842  N  N     . PRO A 594 ? 1.1821 1.0484 0.7868 -0.1879 0.1804 0.0499  594 PRO A N     
4843  C  CA    . PRO A 594 ? 1.1788 1.0428 0.7863 -0.18   0.1849 0.0511  594 PRO A CA    
4844  C  C     . PRO A 594 ? 1.1652 1.0489 0.7834 -0.1765 0.1873 0.0589  594 PRO A C     
4845  O  O     . PRO A 594 ? 1.167  1.05   0.7883 -0.1671 0.1912 0.0601  594 PRO A O     
4846  C  CB    . PRO A 594 ? 1.1952 1.046  0.7948 -0.1856 0.1852 0.048   594 PRO A CB    
4847  C  CG    . PRO A 594 ? 1.2077 1.0487 0.7986 -0.1942 0.1814 0.0435  594 PRO A CG    
4848  C  CD    . PRO A 594 ? 1.1824 1.037  0.7774 -0.1978 0.1781 0.0462  594 PRO A CD    
4849  N  N     . ASN A 595 ? 1.1496 1.0508 0.7729 -0.184  0.1852 0.0643  595 ASN A N     
4850  C  CA    . ASN A 595 ? 1.1366 1.0581 0.7707 -0.1807 0.1877 0.0725  595 ASN A CA    
4851  C  C     . ASN A 595 ? 1.1201 1.0521 0.7614 -0.1715 0.1892 0.0757  595 ASN A C     
4852  O  O     . ASN A 595 ? 1.1123 1.059  0.7618 -0.1664 0.1923 0.0824  595 ASN A O     
4853  C  CB    . ASN A 595 ? 1.1471 1.0852 0.7852 -0.1915 0.185  0.0778  595 ASN A CB    
4854  C  CG    . ASN A 595 ? 1.1833 1.1322 0.8275 -0.1908 0.1883 0.0839  595 ASN A CG    
4855  O  OD1   . ASN A 595 ? 1.1967 1.1518 0.8471 -0.1811 0.1926 0.0878  595 ASN A OD1   
4856  N  ND2   . ASN A 595 ? 1.1896 1.1407 0.832  -0.201  0.1866 0.085   595 ASN A ND2   
4857  N  N     . ASP A 596 ? 1.1131 1.037  0.7509 -0.1689 0.1875 0.0713  596 ASP A N     
4858  C  CA    . ASP A 596 ? 1.1042 1.0354 0.7476 -0.1596 0.1893 0.0736  596 ASP A CA    
4859  C  C     . ASP A 596 ? 1.095  1.015  0.7372 -0.1482 0.1941 0.0718  596 ASP A C     
4860  O  O     . ASP A 596 ? 1.0917 1.016  0.7377 -0.1397 0.1963 0.0738  596 ASP A O     
4861  C  CB    . ASP A 596 ? 1.1326 1.0588 0.7723 -0.1614 0.1856 0.0694  596 ASP A CB    
4862  C  CG    . ASP A 596 ? 1.1871 1.1289 0.8341 -0.1569 0.1856 0.0739  596 ASP A CG    
4863  O  OD1   . ASP A 596 ? 1.1897 1.1449 0.8443 -0.1506 0.189  0.0802  596 ASP A OD1   
4864  O  OD2   . ASP A 596 ? 1.2173 1.1576 0.862  -0.1594 0.1824 0.0714  596 ASP A OD2   
4865  N  N     . PHE A 597 ? 1.0886 0.9936 0.7249 -0.1481 0.1956 0.0681  597 PHE A N     
4866  C  CA    . PHE A 597 ? 1.0861 0.9783 0.7196 -0.1386 0.1996 0.0657  597 PHE A CA    
4867  C  C     . PHE A 597 ? 1.0752 0.966  0.7086 -0.1382 0.2027 0.0678  597 PHE A C     
4868  O  O     . PHE A 597 ? 1.0751 0.9694 0.7081 -0.1464 0.2013 0.069   597 PHE A O     
4869  C  CB    . PHE A 597 ? 1.0953 0.9663 0.7198 -0.1384 0.1979 0.0573  597 PHE A CB    
4870  C  CG    . PHE A 597 ? 1.1033 0.9736 0.7269 -0.1393 0.1948 0.0546  597 PHE A CG    
4871  C  CD1   . PHE A 597 ? 1.1098 0.983  0.7367 -0.1313 0.1963 0.0555  597 PHE A CD1   
4872  C  CD2   . PHE A 597 ? 1.116  0.9822 0.7349 -0.1482 0.1906 0.0512  597 PHE A CD2   
4873  C  CE1   . PHE A 597 ? 1.1188 0.9915 0.7449 -0.1321 0.1936 0.0531  597 PHE A CE1   
4874  C  CE2   . PHE A 597 ? 1.1248 0.9901 0.7427 -0.1489 0.1879 0.0488  597 PHE A CE2   
4875  C  CZ    . PHE A 597 ? 1.1194 0.9883 0.7412 -0.1408 0.1894 0.0498  597 PHE A CZ    
4876  N  N     . ILE A 598 ? 1.0649 0.9496 0.6979 -0.1288 0.207  0.0683  598 ILE A N     
4877  C  CA    . ILE A 598 ? 1.0615 0.942  0.6931 -0.1273 0.2103 0.0696  598 ILE A CA    
4878  C  C     . ILE A 598 ? 1.0636 0.9218 0.6857 -0.1271 0.2096 0.0618  598 ILE A C     
4879  O  O     . ILE A 598 ? 1.0703 0.9177 0.689  -0.1208 0.2101 0.058   598 ILE A O     
4880  C  CB    . ILE A 598 ? 1.0651 0.9508 0.7007 -0.1167 0.2156 0.0746  598 ILE A CB    
4881  C  CG1   . ILE A 598 ? 1.0666 0.9749 0.7118 -0.1155 0.2165 0.0826  598 ILE A CG1   
4882  C  CG2   . ILE A 598 ? 1.0736 0.9536 0.707  -0.1148 0.2192 0.0758  598 ILE A CG2   
4883  C  CD1   . ILE A 598 ? 1.0752 0.9997 0.7262 -0.1238 0.2152 0.088   598 ILE A CD1   
4884  N  N     . LEU A 599 ? 1.0559 0.9072 0.6734 -0.1342 0.2083 0.0593  599 LEU A N     
4885  C  CA    . LEU A 599 ? 1.0603 0.8908 0.6687 -0.1342 0.2076 0.0522  599 LEU A CA    
4886  C  C     . LEU A 599 ? 1.0556 0.8779 0.6612 -0.1298 0.2114 0.0524  599 LEU A C     
4887  O  O     . LEU A 599 ? 1.0554 0.8838 0.6627 -0.1333 0.2127 0.0559  599 LEU A O     
4888  C  CB    . LEU A 599 ? 1.0667 0.8916 0.6697 -0.1446 0.2037 0.0484  599 LEU A CB    
4889  C  CG    . LEU A 599 ? 1.085  0.9156 0.6889 -0.1501 0.1997 0.0475  599 LEU A CG    
4890  C  CD1   . LEU A 599 ? 1.0972 0.92   0.6942 -0.1602 0.1964 0.0439  599 LEU A CD1   
4891  C  CD2   . LEU A 599 ? 1.0984 0.921  0.7006 -0.1439 0.199  0.0436  599 LEU A CD2   
4892  N  N     . LEU A 600 ? 1.0495 0.8581 0.6506 -0.1221 0.213  0.0489  600 LEU A N     
4893  C  CA    . LEU A 600 ? 1.0484 0.8472 0.6456 -0.1176 0.2164 0.0485  600 LEU A CA    
4894  C  C     . LEU A 600 ? 1.0506 0.8294 0.639  -0.1171 0.215  0.0412  600 LEU A C     
4895  O  O     . LEU A 600 ? 1.0546 0.8272 0.6409 -0.1163 0.2127 0.0372  600 LEU A O     
4896  C  CB    . LEU A 600 ? 1.0486 0.8504 0.6487 -0.1076 0.2205 0.0522  600 LEU A CB    
4897  C  CG    . LEU A 600 ? 1.0577 0.8788 0.6663 -0.106  0.2231 0.0602  600 LEU A CG    
4898  C  CD1   . LEU A 600 ? 1.0637 0.8839 0.6728 -0.0954 0.2276 0.0631  600 LEU A CD1   
4899  C  CD2   . LEU A 600 ? 1.0647 0.8928 0.6753 -0.1112 0.2243 0.064   600 LEU A CD2   
4900  N  N     . SER A 601 ? 1.0468 0.8157 0.6302 -0.1173 0.2166 0.0398  601 SER A N     
4901  C  CA    . SER A 601 ? 1.0539 0.8041 0.6289 -0.1162 0.2156 0.0334  601 SER A CA    
4902  C  C     . SER A 601 ? 1.0513 0.7923 0.6232 -0.1079 0.2189 0.0333  601 SER A C     
4903  O  O     . SER A 601 ? 1.0499 0.7969 0.6243 -0.1051 0.2223 0.0379  601 SER A O     
4904  C  CB    . SER A 601 ? 1.074  0.8177 0.6439 -0.124  0.2142 0.0309  601 SER A CB    
4905  O  OG    . SER A 601 ? 1.0999 0.8478 0.6708 -0.1255 0.2168 0.0346  601 SER A OG    
4906  N  N     . ALA A 602 ? 1.0473 0.7741 0.6136 -0.1041 0.218  0.0283  602 ALA A N     
4907  C  CA    . ALA A 602 ? 1.0451 0.7619 0.6073 -0.0967 0.2206 0.0277  602 ALA A CA    
4908  C  C     . ALA A 602 ? 1.045  0.7447 0.5993 -0.0966 0.219  0.0218  602 ALA A C     
4909  O  O     . ALA A 602 ? 1.0492 0.7441 0.6016 -0.0997 0.2159 0.0178  602 ALA A O     
4910  C  CB    . ALA A 602 ? 1.0436 0.763  0.6084 -0.0897 0.2215 0.029   602 ALA A CB    
4911  N  N     . GLY A 603 ? 1.0388 0.7293 0.5883 -0.0928 0.2212 0.0215  603 GLY A N     
4912  C  CA    . GLY A 603 ? 1.0437 0.7183 0.5856 -0.0919 0.22   0.0164  603 GLY A CA    
4913  C  C     . GLY A 603 ? 1.0417 0.7083 0.5807 -0.0841 0.2212 0.0156  603 GLY A C     
4914  O  O     . GLY A 603 ? 1.0406 0.7089 0.5797 -0.0796 0.2244 0.019   603 GLY A O     
4915  N  N     . ALA A 604 ? 1.0406 0.6988 0.5767 -0.0824 0.2186 0.0115  604 ALA A N     
4916  C  CA    . ALA A 604 ? 1.0457 0.6956 0.5784 -0.0756 0.2193 0.0105  604 ALA A CA    
4917  C  C     . ALA A 604 ? 1.0513 0.6864 0.5766 -0.0749 0.2179 0.0063  604 ALA A C     
4918  O  O     . ALA A 604 ? 1.0565 0.6877 0.5802 -0.0788 0.2154 0.0031  604 ALA A O     
4919  C  CB    . ALA A 604 ? 1.0463 0.6992 0.5821 -0.0739 0.2174 0.0096  604 ALA A CB    
4920  N  N     . PHE A 605 ? 1.0488 0.6756 0.5691 -0.0698 0.2197 0.0065  605 PHE A N     
4921  C  CA    . PHE A 605 ? 1.0587 0.6718 0.5717 -0.0688 0.2185 0.003   605 PHE A CA    
4922  C  C     . PHE A 605 ? 1.0695 0.6738 0.5772 -0.0626 0.2198 0.0031  605 PHE A C     
4923  O  O     . PHE A 605 ? 1.0678 0.6761 0.5768 -0.0589 0.2223 0.0062  605 PHE A O     
4924  C  CB    . PHE A 605 ? 1.057  0.668  0.5674 -0.0721 0.22   0.0034  605 PHE A CB    
4925  C  CG    . PHE A 605 ? 1.0612 0.6787 0.5734 -0.0709 0.2239 0.008   605 PHE A CG    
4926  C  CD1   . PHE A 605 ? 1.0752 0.6864 0.5828 -0.0655 0.2266 0.0095  605 PHE A CD1   
4927  C  CD2   . PHE A 605 ? 1.0637 0.694  0.5822 -0.0752 0.225  0.0112  605 PHE A CD2   
4928  C  CE1   . PHE A 605 ? 1.0803 0.6977 0.5897 -0.064  0.2306 0.0142  605 PHE A CE1   
4929  C  CE2   . PHE A 605 ? 1.0685 0.7059 0.5893 -0.0739 0.2287 0.016   605 PHE A CE2   
4930  C  CZ    . PHE A 605 ? 1.0703 0.7012 0.5866 -0.0681 0.2317 0.0176  605 PHE A CZ    
4931  N  N     . ILE A 606 ? 1.0776 0.6697 0.5788 -0.0613 0.2181 -0.0002 606 ILE A N     
4932  C  CA    . ILE A 606 ? 1.0916 0.674  0.5866 -0.056  0.219  -0.0003 606 ILE A CA    
4933  C  C     . ILE A 606 ? 1.104  0.6807 0.5937 -0.0546 0.2218 0.001   606 ILE A C     
4934  O  O     . ILE A 606 ? 1.1063 0.6792 0.5938 -0.0574 0.2212 -0.0007 606 ILE A O     
4935  C  CB    . ILE A 606 ? 1.1037 0.6767 0.5947 -0.0551 0.2152 -0.0043 606 ILE A CB    
4936  C  CG1   . ILE A 606 ? 1.1141 0.6924 0.61   -0.0552 0.2132 -0.0049 606 ILE A CG1   
4937  C  CG2   . ILE A 606 ? 1.116  0.6772 0.5989 -0.0505 0.2158 -0.0048 606 ILE A CG2   
4938  C  CD1   . ILE A 606 ? 1.1335 0.7058 0.628  -0.0558 0.2092 -0.0087 606 ILE A CD1   
4939  N  N     . ASP A 607 ? 1.1109 0.6866 0.5982 -0.0502 0.2252 0.0041  607 ASP A N     
4940  C  CA    . ASP A 607 ? 1.125  0.6949 0.607  -0.0482 0.2283 0.0057  607 ASP A CA    
4941  C  C     . ASP A 607 ? 1.1365 0.6971 0.6114 -0.0422 0.2301 0.0066  607 ASP A C     
4942  O  O     . ASP A 607 ? 1.1348 0.6997 0.6113 -0.0391 0.2322 0.0093  607 ASP A O     
4943  C  CB    . ASP A 607 ? 1.1437 0.7248 0.6311 -0.0498 0.232  0.0101  607 ASP A CB    
4944  C  CG    . ASP A 607 ? 1.2131 0.7886 0.6952 -0.0474 0.2356 0.0122  607 ASP A CG    
4945  O  OD1   . ASP A 607 ? 1.2289 0.7966 0.7065 -0.0491 0.2347 0.0098  607 ASP A OD1   
4946  O  OD2   . ASP A 607 ? 1.2432 0.8216 0.7253 -0.0435 0.2396 0.0164  607 ASP A OD2   
4947  N  N     . TYR A 608 ? 1.1471 0.6949 0.6135 -0.0403 0.2297 0.0046  608 TYR A N     
4948  C  CA    . TYR A 608 ? 1.1632 0.7004 0.6213 -0.0349 0.2312 0.0052  608 TYR A CA    
4949  C  C     . TYR A 608 ? 1.1706 0.7063 0.6252 -0.0316 0.2364 0.0091  608 TYR A C     
4950  O  O     . TYR A 608 ? 1.1789 0.7032 0.6252 -0.0294 0.2372 0.0084  608 TYR A O     
4951  C  CB    . TYR A 608 ? 1.1734 0.6972 0.6237 -0.0346 0.2275 0.0011  608 TYR A CB    
4952  C  CG    . TYR A 608 ? 1.1845 0.7099 0.6382 -0.0372 0.2227 -0.0022 608 TYR A CG    
4953  C  CD1   . TYR A 608 ? 1.1982 0.7229 0.6515 -0.0353 0.2216 -0.0024 608 TYR A CD1   
4954  C  CD2   . TYR A 608 ? 1.196  0.7233 0.6529 -0.0414 0.2195 -0.005  608 TYR A CD2   
4955  C  CE1   . TYR A 608 ? 1.211  0.7374 0.6678 -0.0377 0.2173 -0.0052 608 TYR A CE1   
4956  C  CE2   . TYR A 608 ? 1.2077 0.7366 0.6678 -0.0435 0.2154 -0.0077 608 TYR A CE2   
4957  C  CZ    . TYR A 608 ? 1.222  0.7508 0.6824 -0.0417 0.2143 -0.0078 608 TYR A CZ    
4958  O  OH    . TYR A 608 ? 1.2423 0.7731 0.7062 -0.0437 0.2104 -0.0102 608 TYR A OH    
4959  N  N     . ASP A 609 ? 1.1661 0.7136 0.6272 -0.0312 0.2399 0.0135  609 ASP A N     
4960  C  CA    . ASP A 609 ? 1.1733 0.7232 0.6336 -0.0282 0.2453 0.0183  609 ASP A CA    
4961  C  C     . ASP A 609 ? 1.1772 0.723  0.6347 -0.0298 0.2465 0.018   609 ASP A C     
4962  O  O     . ASP A 609 ? 1.1812 0.721  0.633  -0.0259 0.2504 0.0205  609 ASP A O     
4963  C  CB    . ASP A 609 ? 1.2015 0.7435 0.6543 -0.0213 0.249  0.0209  609 ASP A CB    
4964  C  CG    . ASP A 609 ? 1.2674 0.7936 0.7097 -0.0183 0.2468 0.0175  609 ASP A CG    
4965  O  OD1   . ASP A 609 ? 1.2738 0.8001 0.7171 -0.0187 0.244  0.0156  609 ASP A OD1   
4966  O  OD2   . ASP A 609 ? 1.304  0.8177 0.7369 -0.0155 0.2481 0.0171  609 ASP A OD2   
4967  N  N     . ASN A 610 ? 1.1739 0.7229 0.6352 -0.0355 0.2435 0.0153  610 ASN A N     
4968  C  CA    . ASN A 610 ? 1.1823 0.7279 0.6412 -0.0376 0.2446 0.015   610 ASN A CA    
4969  C  C     . ASN A 610 ? 1.178  0.7373 0.6449 -0.0413 0.2472 0.0188  610 ASN A C     
4970  O  O     . ASN A 610 ? 1.1803 0.7376 0.6457 -0.0435 0.2485 0.0189  610 ASN A O     
4971  C  CB    . ASN A 610 ? 1.1992 0.7382 0.6557 -0.0414 0.2402 0.0099  610 ASN A CB    
4972  C  CG    . ASN A 610 ? 1.2456 0.7728 0.6954 -0.039  0.2367 0.0061  610 ASN A CG    
4973  O  OD1   . ASN A 610 ? 1.2661 0.7809 0.7073 -0.0365 0.2365 0.0045  610 ASN A OD1   
4974  N  ND2   . ASN A 610 ? 1.2526 0.7838 0.7063 -0.0399 0.2336 0.0046  610 ASN A ND2   
4975  N  N     . LEU A 611 ? 1.1694 0.7425 0.6448 -0.0422 0.248  0.0219  611 LEU A N     
4976  C  CA    . LEU A 611 ? 1.169  0.756  0.6523 -0.0463 0.2501 0.0257  611 LEU A CA    
4977  C  C     . LEU A 611 ? 1.173  0.766  0.6579 -0.0419 0.2556 0.0319  611 LEU A C     
4978  O  O     . LEU A 611 ? 1.173  0.7684 0.6585 -0.0371 0.2573 0.0344  611 LEU A O     
4979  C  CB    . LEU A 611 ? 1.1645 0.7643 0.6568 -0.0511 0.2471 0.0254  611 LEU A CB    
4980  C  CG    . LEU A 611 ? 1.1856 0.7812 0.6773 -0.056  0.242  0.0198  611 LEU A CG    
4981  C  CD1   . LEU A 611 ? 1.1861 0.7932 0.6856 -0.0595 0.2395 0.0198  611 LEU A CD1   
4982  C  CD2   . LEU A 611 ? 1.1952 0.7885 0.6854 -0.0611 0.2418 0.0184  611 LEU A CD2   
4983  N  N     . THR A 612 ? 1.1743 0.7698 0.6598 -0.0434 0.2586 0.0346  612 THR A N     
4984  C  CA    . THR A 612 ? 1.1793 0.7818 0.667  -0.0397 0.2642 0.0411  612 THR A CA    
4985  C  C     . THR A 612 ? 1.1786 0.8011 0.6782 -0.0442 0.2646 0.0455  612 THR A C     
4986  O  O     . THR A 612 ? 1.1761 0.8048 0.6807 -0.0505 0.2606 0.0429  612 THR A O     
4987  C  CB    . THR A 612 ? 1.1958 0.7905 0.678  -0.0394 0.2671 0.0418  612 THR A CB    
4988  O  OG1   . THR A 612 ? 1.2013 0.802  0.6879 -0.047  0.2654 0.0409  612 THR A OG1   
4989  C  CG2   . THR A 612 ? 1.2112 0.7865 0.6817 -0.0357 0.266  0.0372  612 THR A CG2   
4990  N  N     . GLU A 613 ? 1.179  0.8117 0.683  -0.0412 0.2695 0.0522  613 GLU A N     
4991  C  CA    . GLU A 613 ? 1.1808 0.8334 0.6961 -0.0454 0.2701 0.0571  613 GLU A CA    
4992  C  C     . GLU A 613 ? 1.188  0.8461 0.7072 -0.0545 0.2676 0.0557  613 GLU A C     
4993  O  O     . GLU A 613 ? 1.1824 0.8525 0.709  -0.0606 0.2647 0.0558  613 GLU A O     
4994  C  CB    . GLU A 613 ? 1.2046 0.8656 0.7228 -0.0399 0.2764 0.065   613 GLU A CB    
4995  C  CG    . GLU A 613 ? 1.2489 0.9317 0.7792 -0.0441 0.2774 0.071   613 GLU A CG    
4996  C  CD    . GLU A 613 ? 1.312  1.0033 0.8452 -0.039  0.2839 0.0792  613 GLU A CD    
4997  O  OE1   . GLU A 613 ? 1.3152 1.0232 0.8576 -0.0435 0.285  0.0843  613 GLU A OE1   
4998  O  OE2   . GLU A 613 ? 1.3397 1.0209 0.8659 -0.0306 0.288  0.0807  613 GLU A OE2   
4999  N  N     . ASN A 614 ? 1.1986 0.8467 0.7118 -0.0555 0.2688 0.0542  614 ASN A N     
5000  C  CA    . ASN A 614 ? 1.2084 0.8586 0.7231 -0.0638 0.2671 0.0526  614 ASN A CA    
5001  C  C     . ASN A 614 ? 1.2153 0.8592 0.7277 -0.0691 0.2614 0.0457  614 ASN A C     
5002  O  O     . ASN A 614 ? 1.2121 0.8629 0.7285 -0.0769 0.259  0.045   614 ASN A O     
5003  C  CB    . ASN A 614 ? 1.2337 0.8736 0.7417 -0.0624 0.2703 0.0528  614 ASN A CB    
5004  C  CG    . ASN A 614 ? 1.2746 0.9239 0.7866 -0.0597 0.276  0.0602  614 ASN A CG    
5005  O  OD1   . ASN A 614 ? 1.2829 0.9496 0.8045 -0.0616 0.2771 0.0656  614 ASN A OD1   
5006  N  ND2   . ASN A 614 ? 1.2888 0.9271 0.7937 -0.0551 0.2797 0.061   614 ASN A ND2   
5007  N  N     . ASP A 615 ? 1.223  0.8538 0.7288 -0.0649 0.2592 0.041   615 ASP A N     
5008  C  CA    . ASP A 615 ? 1.2332 0.858  0.737  -0.0689 0.254  0.0348  615 ASP A CA    
5009  C  C     . ASP A 615 ? 1.2277 0.8661 0.7399 -0.0728 0.2513 0.0355  615 ASP A C     
5010  O  O     . ASP A 615 ? 1.2267 0.8674 0.7406 -0.0797 0.2481 0.0329  615 ASP A O     
5011  C  CB    . ASP A 615 ? 1.2673 0.877  0.7631 -0.0632 0.2524 0.0304  615 ASP A CB    
5012  C  CG    . ASP A 615 ? 1.3429 0.9367 0.8291 -0.0611 0.2532 0.0276  615 ASP A CG    
5013  O  OD1   . ASP A 615 ? 1.3545 0.9476 0.8397 -0.065  0.2543 0.0278  615 ASP A OD1   
5014  O  OD2   . ASP A 615 ? 1.38   0.962  0.8595 -0.0557 0.2526 0.0252  615 ASP A OD2   
5015  N  N     . TYR A 616 ? 1.2229 0.8702 0.74   -0.0685 0.2528 0.0394  616 TYR A N     
5016  C  CA    . TYR A 616 ? 1.2213 0.8825 0.7467 -0.0715 0.2506 0.0408  616 TYR A CA    
5017  C  C     . TYR A 616 ? 1.2146 0.89   0.747  -0.0791 0.2507 0.044   616 TYR A C     
5018  O  O     . TYR A 616 ? 1.2119 0.8931 0.7479 -0.0853 0.247  0.0422  616 TYR A O     
5019  C  CB    . TYR A 616 ? 1.2214 0.8893 0.7502 -0.0648 0.2532 0.045   616 TYR A CB    
5020  C  CG    . TYR A 616 ? 1.2397 0.8963 0.763  -0.0594 0.2516 0.0411  616 TYR A CG    
5021  C  CD1   . TYR A 616 ? 1.2518 0.9075 0.7761 -0.0622 0.247  0.0367  616 TYR A CD1   
5022  C  CD2   . TYR A 616 ? 1.2586 0.9051 0.7753 -0.0516 0.2546 0.0419  616 TYR A CD2   
5023  C  CE1   . TYR A 616 ? 1.2692 0.9149 0.7888 -0.0577 0.2453 0.0333  616 TYR A CE1   
5024  C  CE2   . TYR A 616 ? 1.2766 0.9123 0.7877 -0.0473 0.2529 0.0384  616 TYR A CE2   
5025  C  CZ    . TYR A 616 ? 1.2881 0.9238 0.8011 -0.0505 0.2482 0.0341  616 TYR A CZ    
5026  O  OH    . TYR A 616 ? 1.3148 0.9404 0.8226 -0.0465 0.2465 0.0308  616 TYR A OH    
5027  N  N     . GLU A 617 ? 1.2105 0.8907 0.7444 -0.079  0.2546 0.0488  617 GLU A N     
5028  C  CA    . GLU A 617 ? 1.2077 0.901  0.7479 -0.0866 0.2549 0.0523  617 GLU A CA    
5029  C  C     . GLU A 617 ? 1.2087 0.8951 0.7449 -0.0948 0.2513 0.0471  617 GLU A C     
5030  O  O     . GLU A 617 ? 1.2046 0.901  0.7457 -0.1024 0.2489 0.0477  617 GLU A O     
5031  C  CB    . GLU A 617 ? 1.2372 0.9344 0.7783 -0.0839 0.2602 0.0581  617 GLU A CB    
5032  C  CG    . GLU A 617 ? 1.2961 1.0003 0.8401 -0.0919 0.2608 0.0604  617 GLU A CG    
5033  C  CD    . GLU A 617 ? 1.3806 1.0775 0.9199 -0.0891 0.2652 0.0623  617 GLU A CD    
5034  O  OE1   . GLU A 617 ? 1.3896 1.0955 0.9332 -0.0851 0.2697 0.0688  617 GLU A OE1   
5035  O  OE2   . GLU A 617 ? 1.4177 1.1    0.9489 -0.0909 0.2643 0.0574  617 GLU A OE2   
5036  N  N     . LYS A 618 ? 1.2126 0.8815 0.7396 -0.0931 0.2509 0.0421  618 LYS A N     
5037  C  CA    . LYS A 618 ? 1.2181 0.8785 0.74   -0.0998 0.248  0.037   618 LYS A CA    
5038  C  C     . LYS A 618 ? 1.214  0.8743 0.7367 -0.1028 0.2433 0.0329  618 LYS A C     
5039  O  O     . LYS A 618 ? 1.2139 0.8756 0.7365 -0.1104 0.2409 0.031   618 LYS A O     
5040  C  CB    . LYS A 618 ? 1.2515 0.8938 0.7634 -0.0963 0.2492 0.0333  618 LYS A CB    
5041  C  CG    . LYS A 618 ? 1.3074 0.9394 0.813  -0.1022 0.2467 0.0282  618 LYS A CG    
5042  C  CD    . LYS A 618 ? 1.3674 0.9866 0.8671 -0.099  0.2436 0.0224  618 LYS A CD    
5043  C  CE    . LYS A 618 ? 1.4185 1.028  0.9119 -0.1045 0.2415 0.0177  618 LYS A CE    
5044  N  NZ    . LYS A 618 ? 1.4506 1.0494 0.9393 -0.1015 0.2383 0.0126  618 LYS A NZ    
5045  N  N     . ILE A 619 ? 1.2095 0.8676 0.7325 -0.0969 0.2421 0.0315  619 ILE A N     
5046  C  CA    . ILE A 619 ? 1.21   0.8683 0.7341 -0.0991 0.2379 0.0278  619 ILE A CA    
5047  C  C     . ILE A 619 ? 1.1959 0.8711 0.7285 -0.105  0.2366 0.0311  619 ILE A C     
5048  O  O     . ILE A 619 ? 1.197  0.8727 0.7295 -0.1112 0.2333 0.0284  619 ILE A O     
5049  C  CB    . ILE A 619 ? 1.2214 0.8738 0.7439 -0.0915 0.2371 0.0259  619 ILE A CB    
5050  C  CG1   . ILE A 619 ? 1.2431 0.8787 0.7568 -0.0864 0.2379 0.0226  619 ILE A CG1   
5051  C  CG2   . ILE A 619 ? 1.2266 0.8798 0.7508 -0.094  0.2329 0.0223  619 ILE A CG2   
5052  C  CD1   . ILE A 619 ? 1.2612 0.891  0.7728 -0.0789 0.2376 0.0215  619 ILE A CD1   
5053  N  N     . PHE A 620 ? 1.1805 0.8695 0.7202 -0.103  0.2393 0.0372  620 PHE A N     
5054  C  CA    . PHE A 620 ? 1.1697 0.8764 0.7181 -0.1084 0.2382 0.0412  620 PHE A CA    
5055  C  C     . PHE A 620 ? 1.1608 0.8705 0.7089 -0.1182 0.2371 0.0412  620 PHE A C     
5056  O  O     . PHE A 620 ? 1.1568 0.8746 0.7083 -0.1248 0.2341 0.0412  620 PHE A O     
5057  C  CB    . PHE A 620 ? 1.1649 0.8855 0.7205 -0.104  0.242  0.0484  620 PHE A CB    
5058  C  CG    . PHE A 620 ? 1.1762 0.8983 0.7337 -0.0957 0.2429 0.0495  620 PHE A CG    
5059  C  CD1   . PHE A 620 ? 1.1862 0.9109 0.746  -0.0961 0.2396 0.0472  620 PHE A CD1   
5060  C  CD2   . PHE A 620 ? 1.1878 0.9092 0.7449 -0.0877 0.2474 0.0533  620 PHE A CD2   
5061  C  CE1   . PHE A 620 ? 1.1946 0.9206 0.7559 -0.0887 0.2407 0.0484  620 PHE A CE1   
5062  C  CE2   . PHE A 620 ? 1.1967 0.9186 0.7546 -0.0802 0.2485 0.0544  620 PHE A CE2   
5063  C  CZ    . PHE A 620 ? 1.1932 0.9174 0.7533 -0.0809 0.2451 0.0519  620 PHE A CZ    
5064  N  N     . GLU A 621 ? 1.156  0.8587 0.6995 -0.1191 0.2395 0.0414  621 GLU A N     
5065  C  CA    . GLU A 621 ? 1.154  0.8579 0.6961 -0.1283 0.2389 0.0414  621 GLU A CA    
5066  C  C     . GLU A 621 ? 1.1543 0.8462 0.6893 -0.1334 0.2352 0.0349  621 GLU A C     
5067  O  O     . GLU A 621 ? 1.1545 0.8514 0.6902 -0.1419 0.2329 0.0347  621 GLU A O     
5068  C  CB    . GLU A 621 ? 1.1856 0.8836 0.7239 -0.127  0.2428 0.043   621 GLU A CB    
5069  C  CG    . GLU A 621 ? 1.2419 0.9474 0.7819 -0.136  0.2434 0.0459  621 GLU A CG    
5070  C  CD    . GLU A 621 ? 1.3208 1.022  0.858  -0.1346 0.2477 0.0483  621 GLU A CD    
5071  O  OE1   . GLU A 621 ? 1.3362 1.028  0.8697 -0.1262 0.2503 0.0476  621 GLU A OE1   
5072  O  OE2   . GLU A 621 ? 1.3462 1.0534 0.8848 -0.1421 0.2483 0.0508  621 GLU A OE2   
5073  N  N     . VAL A 622 ? 1.1519 0.8282 0.6798 -0.128  0.2346 0.0298  622 VAL A N     
5074  C  CA    . VAL A 622 ? 1.1552 0.8193 0.676  -0.1315 0.2316 0.0238  622 VAL A CA    
5075  C  C     . VAL A 622 ? 1.1447 0.8152 0.6692 -0.1344 0.2278 0.0225  622 VAL A C     
5076  O  O     . VAL A 622 ? 1.1466 0.8165 0.6687 -0.1419 0.2255 0.0207  622 VAL A O     
5077  C  CB    . VAL A 622 ? 1.1722 0.8193 0.6854 -0.1245 0.232  0.0194  622 VAL A CB    
5078  C  CG1   . VAL A 622 ? 1.1869 0.8229 0.694  -0.1265 0.2287 0.0137  622 VAL A CG1   
5079  C  CG2   . VAL A 622 ? 1.1817 0.8201 0.6893 -0.1232 0.2352 0.0197  622 VAL A CG2   
5080  N  N     . THR A 623 ? 1.1304 0.8064 0.66   -0.1283 0.2273 0.0235  623 THR A N     
5081  C  CA    . THR A 623 ? 1.1224 0.8034 0.6553 -0.1296 0.224  0.0221  623 THR A CA    
5082  C  C     . THR A 623 ? 1.1066 0.8055 0.6478 -0.1347 0.223  0.0265  623 THR A C     
5083  O  O     . THR A 623 ? 1.1058 0.8072 0.6475 -0.1394 0.2199 0.0249  623 THR A O     
5084  C  CB    . THR A 623 ? 1.1376 0.8154 0.6715 -0.1208 0.224  0.021   623 THR A CB    
5085  O  OG1   . THR A 623 ? 1.1445 0.8325 0.6845 -0.1158 0.2268 0.0261  623 THR A OG1   
5086  C  CG2   . THR A 623 ? 1.1501 0.8106 0.6759 -0.1159 0.2244 0.0166  623 THR A CG2   
5087  N  N     . GLY A 624 ? 1.0932 0.8045 0.6409 -0.133  0.2257 0.0323  624 GLY A N     
5088  C  CA    . GLY A 624 ? 1.0829 0.8128 0.6395 -0.1368 0.2249 0.0373  624 GLY A CA    
5089  C  C     . GLY A 624 ? 1.0736 0.8105 0.6356 -0.1309 0.2242 0.0383  624 GLY A C     
5090  O  O     . GLY A 624 ? 1.0681 0.8194 0.6369 -0.1339 0.2227 0.0415  624 GLY A O     
5091  N  N     . CYS A 625 ? 1.0706 0.7972 0.6295 -0.1226 0.2251 0.0357  625 CYS A N     
5092  C  CA    . CYS A 625 ? 1.0677 0.7983 0.6304 -0.1164 0.2248 0.0362  625 CYS A CA    
5093  C  C     . CYS A 625 ? 1.0573 0.8029 0.6277 -0.1123 0.2279 0.043   625 CYS A C     
5094  O  O     . CYS A 625 ? 1.0577 0.805  0.6285 -0.1105 0.2313 0.0466  625 CYS A O     
5095  C  CB    . CYS A 625 ? 1.0835 0.7984 0.64   -0.1092 0.2251 0.0318  625 CYS A CB    
5096  S  SG    . CYS A 625 ? 1.1306 0.8301 0.6796 -0.1125 0.2211 0.0241  625 CYS A SG    
5097  N  N     . ASP A 626 ? 1.0473 0.8033 0.6235 -0.1105 0.227  0.0451  626 ASP A N     
5098  C  CA    . ASP A 626 ? 1.0422 0.8123 0.6255 -0.1056 0.2302 0.0518  626 ASP A CA    
5099  C  C     . ASP A 626 ? 1.041  0.8026 0.6213 -0.0952 0.2334 0.0517  626 ASP A C     
5100  O  O     . ASP A 626 ? 1.0401 0.809  0.6237 -0.0899 0.2373 0.0571  626 ASP A O     
5101  C  CB    . ASP A 626 ? 1.0597 0.845  0.6504 -0.1079 0.2281 0.0544  626 ASP A CB    
5102  C  CG    . ASP A 626 ? 1.12   0.9153 0.7139 -0.1183 0.225  0.0554  626 ASP A CG    
5103  O  OD1   . ASP A 626 ? 1.1246 0.9321 0.7233 -0.1215 0.2267 0.0609  626 ASP A OD1   
5104  O  OD2   . ASP A 626 ? 1.1525 0.9435 0.7439 -0.1235 0.2211 0.0509  626 ASP A OD2   
5105  N  N     . LEU A 627 ? 1.0391 0.7852 0.6128 -0.0924 0.2317 0.0457  627 LEU A N     
5106  C  CA    . LEU A 627 ? 1.0408 0.7774 0.6104 -0.0833 0.2341 0.045   627 LEU A CA    
5107  C  C     . LEU A 627 ? 1.0444 0.762  0.6052 -0.0825 0.2326 0.0386  627 LEU A C     
5108  O  O     . LEU A 627 ? 1.0469 0.759  0.6054 -0.0875 0.229  0.034   627 LEU A O     
5109  C  CB    . LEU A 627 ? 1.0409 0.7826 0.6139 -0.08   0.233  0.0452  627 LEU A CB    
5110  C  CG    . LEU A 627 ? 1.0639 0.7957 0.6324 -0.0712 0.2351 0.0442  627 LEU A CG    
5111  C  CD1   . LEU A 627 ? 1.0685 0.8038 0.6374 -0.0649 0.2403 0.0499  627 LEU A CD1   
5112  C  CD2   . LEU A 627 ? 1.0709 0.8065 0.6422 -0.0693 0.2334 0.0434  627 LEU A CD2   
5113  N  N     . LEU A 628 ? 1.0425 0.7498 0.5978 -0.0759 0.2355 0.0385  628 LEU A N     
5114  C  CA    . LEU A 628 ? 1.0494 0.7391 0.5963 -0.0744 0.234  0.0329  628 LEU A CA    
5115  C  C     . LEU A 628 ? 1.0521 0.7346 0.5957 -0.0668 0.2349 0.032   628 LEU A C     
5116  O  O     . LEU A 628 ? 1.0526 0.7382 0.5968 -0.0612 0.2386 0.0362  628 LEU A O     
5117  C  CB    . LEU A 628 ? 1.0538 0.7355 0.5955 -0.0744 0.2362 0.0329  628 LEU A CB    
5118  C  CG    . LEU A 628 ? 1.0681 0.754  0.6113 -0.0823 0.2353 0.033   628 LEU A CG    
5119  C  CD1   . LEU A 628 ? 1.0783 0.7574 0.6169 -0.0814 0.2382 0.0339  628 LEU A CD1   
5120  C  CD2   . LEU A 628 ? 1.0801 0.7595 0.6207 -0.0877 0.2309 0.0274  628 LEU A CD2   
5121  N  N     . ILE A 629 ? 1.0514 0.7248 0.5918 -0.0668 0.2315 0.0269  629 ILE A N     
5122  C  CA    . ILE A 629 ? 1.0559 0.7218 0.5927 -0.0605 0.2318 0.0257  629 ILE A CA    
5123  C  C     . ILE A 629 ? 1.0626 0.7117 0.5908 -0.0587 0.2308 0.0212  629 ILE A C     
5124  O  O     . ILE A 629 ? 1.068  0.7108 0.5943 -0.0619 0.2271 0.0166  629 ILE A O     
5125  C  CB    . ILE A 629 ? 1.0594 0.7302 0.6003 -0.0614 0.229  0.024   629 ILE A CB    
5126  C  CG1   . ILE A 629 ? 1.0619 0.7502 0.6115 -0.0639 0.2297 0.0285  629 ILE A CG1   
5127  C  CG2   . ILE A 629 ? 1.0695 0.7328 0.6065 -0.055  0.2297 0.0232  629 ILE A CG2   
5128  C  CD1   . ILE A 629 ? 1.0739 0.7674 0.6276 -0.0656 0.2267 0.0269  629 ILE A CD1   
5129  N  N     . ALA A 630 ? 1.0594 0.7012 0.5821 -0.0535 0.234  0.0229  630 ALA A N     
5130  C  CA    . ALA A 630 ? 1.0668 0.6926 0.5808 -0.0514 0.2332 0.0192  630 ALA A CA    
5131  C  C     . ALA A 630 ? 1.0658 0.6836 0.5755 -0.0465 0.2326 0.0176  630 ALA A C     
5132  O  O     . ALA A 630 ? 1.0666 0.6852 0.5751 -0.0414 0.2358 0.0208  630 ALA A O     
5133  C  CB    . ALA A 630 ? 1.0729 0.6945 0.5825 -0.0489 0.237  0.0218  630 ALA A CB    
5134  N  N     . ILE A 631 ? 1.062  0.6718 0.569  -0.048  0.2286 0.0128  631 ILE A N     
5135  C  CA    . ILE A 631 ? 1.0644 0.6666 0.5675 -0.0446 0.2271 0.0107  631 ILE A CA    
5136  C  C     . ILE A 631 ? 1.0699 0.6566 0.5638 -0.0425 0.2261 0.0077  631 ILE A C     
5137  O  O     . ILE A 631 ? 1.0723 0.6546 0.5642 -0.0453 0.2245 0.0054  631 ILE A O     
5138  C  CB    . ILE A 631 ? 1.0661 0.673  0.5745 -0.0485 0.223  0.0078  631 ILE A CB    
5139  C  CG1   . ILE A 631 ? 1.069  0.6908 0.5859 -0.0498 0.2241 0.0109  631 ILE A CG1   
5140  C  CG2   . ILE A 631 ? 1.0754 0.6735 0.58   -0.0464 0.2204 0.0046  631 ILE A CG2   
5141  C  CD1   . ILE A 631 ? 1.0818 0.7094 0.604  -0.0549 0.2205 0.0085  631 ILE A CD1   
5142  N  N     . LYS A 632 ? 1.0702 0.6483 0.5578 -0.0378 0.2271 0.0079  632 LYS A N     
5143  C  CA    . LYS A 632 ? 1.0801 0.6434 0.5584 -0.036  0.2257 0.0051  632 LYS A CA    
5144  C  C     . LYS A 632 ? 1.083  0.6389 0.5567 -0.0333 0.2244 0.0037  632 LYS A C     
5145  O  O     . LYS A 632 ? 1.0825 0.6415 0.5568 -0.0302 0.2268 0.0062  632 LYS A O     
5146  C  CB    . LYS A 632 ? 1.1081 0.6654 0.5802 -0.0328 0.2297 0.0076  632 LYS A CB    
5147  C  CG    . LYS A 632 ? 1.1621 0.721  0.6324 -0.0276 0.2345 0.012   632 LYS A CG    
5148  C  CD    . LYS A 632 ? 1.2237 0.781  0.6907 -0.0251 0.239  0.0155  632 LYS A CD    
5149  C  CE    . LYS A 632 ? 1.2643 0.8359 0.7404 -0.0285 0.2406 0.0183  632 LYS A CE    
5150  N  NZ    . LYS A 632 ? 1.2842 0.87   0.7693 -0.0294 0.241  0.0207  632 LYS A NZ    
5151  N  N     . ASN A 633 ? 1.0853 0.632  0.5547 -0.0345 0.2204 -0.0002 633 ASN A N     
5152  C  CA    . ASN A 633 ? 1.0956 0.6348 0.5603 -0.0325 0.2186 -0.0017 633 ASN A CA    
5153  C  C     . ASN A 633 ? 1.1128 0.6386 0.5663 -0.0286 0.2204 -0.0012 633 ASN A C     
5154  O  O     . ASN A 633 ? 1.1202 0.6394 0.5686 -0.0284 0.2207 -0.0017 633 ASN A O     
5155  C  CB    . ASN A 633 ? 1.1039 0.6409 0.57   -0.0359 0.2133 -0.0057 633 ASN A CB    
5156  C  CG    . ASN A 633 ? 1.1334 0.664  0.596  -0.0376 0.2111 -0.008  633 ASN A CG    
5157  O  OD1   . ASN A 633 ? 1.139  0.6746 0.6055 -0.04   0.2114 -0.008  633 ASN A OD1   
5158  N  ND2   . ASN A 633 ? 1.1454 0.6645 0.6003 -0.0367 0.2087 -0.01   633 ASN A ND2   
5159  N  N     . GLN A 634 ? 1.1165 0.6378 0.5654 -0.0254 0.2218 -0.0002 634 GLN A N     
5160  C  CA    . GLN A 634 ? 1.1311 0.6382 0.5679 -0.0216 0.2234 0.0002  634 GLN A CA    
5161  C  C     . GLN A 634 ? 1.1403 0.64   0.5736 -0.0233 0.2188 -0.0032 634 GLN A C     
5162  O  O     . GLN A 634 ? 1.1398 0.6452 0.5781 -0.0244 0.2175 -0.0037 634 GLN A O     
5163  C  CB    . GLN A 634 ? 1.1473 0.6555 0.5819 -0.0169 0.2289 0.0043  634 GLN A CB    
5164  C  CG    . GLN A 634 ? 1.1906 0.683  0.6115 -0.0126 0.2311 0.0049  634 GLN A CG    
5165  C  CD    . GLN A 634 ? 1.2435 0.7382 0.6629 -0.0076 0.237  0.0095  634 GLN A CD    
5166  O  OE1   . GLN A 634 ? 1.2593 0.7586 0.6801 -0.0049 0.2416 0.0132  634 GLN A OE1   
5167  N  NE2   . GLN A 634 ? 1.256  0.7477 0.6726 -0.0062 0.2372 0.0094  634 GLN A NE2   
5168  N  N     . ASN A 635 ? 1.1466 0.6346 0.5718 -0.0239 0.2159 -0.0057 635 ASN A N     
5169  C  CA    . ASN A 635 ? 1.1555 0.6372 0.5776 -0.0261 0.211  -0.0088 635 ASN A CA    
5170  C  C     . ASN A 635 ? 1.165  0.6353 0.5767 -0.0235 0.2121 -0.0083 635 ASN A C     
5171  O  O     . ASN A 635 ? 1.1687 0.6372 0.5802 -0.0253 0.2089 -0.0101 635 ASN A O     
5172  C  CB    . ASN A 635 ? 1.1737 0.6493 0.5927 -0.0285 0.2069 -0.0115 635 ASN A CB    
5173  C  CG    . ASN A 635 ? 1.2066 0.6924 0.6352 -0.0315 0.2054 -0.0124 635 ASN A CG    
5174  O  OD1   . ASN A 635 ? 1.2149 0.712  0.6532 -0.0333 0.205  -0.0123 635 ASN A OD1   
5175  N  ND2   . ASN A 635 ? 1.2173 0.6985 0.6426 -0.0319 0.2045 -0.0133 635 ASN A ND2   
5176  N  N     . ASN A 636 ? 1.1666 0.6285 0.5692 -0.0193 0.2167 -0.0059 636 ASN A N     
5177  C  CA    . ASN A 636 ? 1.1775 0.6265 0.5682 -0.0167 0.218  -0.0055 636 ASN A CA    
5178  C  C     . ASN A 636 ? 1.1767 0.6257 0.5643 -0.0114 0.2249 -0.0013 636 ASN A C     
5179  O  O     . ASN A 636 ? 1.183  0.6261 0.5641 -0.008  0.2288 0.0008  636 ASN A O     
5180  C  CB    . ASN A 636 ? 1.2008 0.6339 0.5786 -0.0164 0.2163 -0.007  636 ASN A CB    
5181  C  CG    . ASN A 636 ? 1.2336 0.6668 0.6139 -0.0208 0.2103 -0.0103 636 ASN A CG    
5182  O  OD1   . ASN A 636 ? 1.2485 0.6795 0.6284 -0.0241 0.2054 -0.0128 636 ASN A OD1   
5183  N  ND2   . ASN A 636 ? 1.2359 0.6717 0.6186 -0.0209 0.2106 -0.0103 636 ASN A ND2   
5184  N  N     . PRO A 637 ? 1.167  0.6213 0.5581 -0.0103 0.2266 0       637 PRO A N     
5185  C  CA    . PRO A 637 ? 1.1582 0.62   0.5573 -0.0138 0.2228 -0.0021 637 PRO A CA    
5186  C  C     . PRO A 637 ? 1.1435 0.6231 0.558  -0.0164 0.2218 -0.0019 637 PRO A C     
5187  O  O     . PRO A 637 ? 1.1425 0.6299 0.5617 -0.0148 0.2252 0.0007  637 PRO A O     
5188  C  CB    . PRO A 637 ? 1.1706 0.6294 0.5651 -0.0102 0.2269 0.0002  637 PRO A CB    
5189  C  CG    . PRO A 637 ? 1.1771 0.6377 0.5698 -0.0049 0.2336 0.0047  637 PRO A CG    
5190  C  CD    . PRO A 637 ? 1.1617 0.6159 0.5494 -0.0047 0.2335 0.0044  637 PRO A CD    
5191  N  N     . GLN A 638 ? 1.1304 0.6163 0.5525 -0.0206 0.2171 -0.0046 638 GLN A N     
5192  C  CA    . GLN A 638 ? 1.1189 0.6201 0.5544 -0.0234 0.2158 -0.0048 638 GLN A CA    
5193  C  C     . GLN A 638 ? 1.103  0.6162 0.5456 -0.021  0.2204 -0.0011 638 GLN A C     
5194  O  O     . GLN A 638 ? 1.1036 0.6184 0.5463 -0.0191 0.2223 0.0002  638 GLN A O     
5195  C  CB    . GLN A 638 ? 1.1386 0.6436 0.5801 -0.0276 0.2105 -0.0079 638 GLN A CB    
5196  C  CG    . GLN A 638 ? 1.1856 0.685  0.625  -0.0308 0.2057 -0.011  638 GLN A CG    
5197  C  CD    . GLN A 638 ? 1.242  0.7452 0.6873 -0.0345 0.2008 -0.0136 638 GLN A CD    
5198  O  OE1   . GLN A 638 ? 1.2648 0.7635 0.7069 -0.0348 0.1994 -0.0144 638 GLN A OE1   
5199  N  NE2   . GLN A 638 ? 1.2455 0.7569 0.699  -0.0373 0.1984 -0.0148 638 GLN A NE2   
5200  N  N     . LYS A 639 ? 1.0865 0.608  0.5347 -0.0213 0.2223 0.0006  639 LYS A N     
5201  C  CA    . LYS A 639 ? 1.0745 0.6089 0.5301 -0.0196 0.2263 0.0044  639 LYS A CA    
5202  C  C     . LYS A 639 ? 1.0635 0.6083 0.5276 -0.0228 0.2256 0.0047  639 LYS A C     
5203  O  O     . LYS A 639 ? 1.0656 0.6052 0.5267 -0.0242 0.2243 0.0032  639 LYS A O     
5204  C  CB    . LYS A 639 ? 1.0948 0.6242 0.5431 -0.014  0.2323 0.0085  639 LYS A CB    
5205  C  CG    . LYS A 639 ? 1.1356 0.6621 0.5797 -0.01   0.2353 0.0105  639 LYS A CG    
5206  C  CD    . LYS A 639 ? 1.1841 0.7035 0.6192 -0.004  0.2413 0.0145  639 LYS A CD    
5207  C  CE    . LYS A 639 ? 1.2186 0.7497 0.6593 -0.0003 0.2465 0.0196  639 LYS A CE    
5208  N  NZ    . LYS A 639 ? 1.2467 0.7739 0.6833 0.0027  0.2482 0.0203  639 LYS A NZ    
5209  N  N     . TRP A 640 ? 1.0497 0.6089 0.5236 -0.0241 0.2266 0.0066  640 TRP A N     
5210  C  CA    . TRP A 640 ? 1.0432 0.6124 0.5246 -0.0274 0.2263 0.0073  640 TRP A CA    
5211  C  C     . TRP A 640 ? 1.0377 0.6128 0.5198 -0.0241 0.2317 0.0123  640 TRP A C     
5212  O  O     . TRP A 640 ? 1.0354 0.6177 0.5205 -0.0215 0.2347 0.0156  640 TRP A O     
5213  C  CB    . TRP A 640 ? 1.0348 0.6163 0.5264 -0.0314 0.2237 0.0063  640 TRP A CB    
5214  C  CG    . TRP A 640 ? 1.0391 0.6172 0.5318 -0.0354 0.2185 0.0017  640 TRP A CG    
5215  C  CD1   . TRP A 640 ? 1.0494 0.6275 0.5441 -0.0365 0.2156 -0.0005 640 TRP A CD1   
5216  C  CD2   . TRP A 640 ? 1.0397 0.6147 0.532  -0.0388 0.2158 -0.0009 640 TRP A CD2   
5217  N  NE1   . TRP A 640 ? 1.0531 0.6285 0.5488 -0.0401 0.2113 -0.0041 640 TRP A NE1   
5218  C  CE2   . TRP A 640 ? 1.0498 0.623  0.5438 -0.0415 0.2114 -0.0044 640 TRP A CE2   
5219  C  CE3   . TRP A 640 ? 1.0454 0.6184 0.5356 -0.0396 0.2168 -0.0004 640 TRP A CE3   
5220  C  CZ2   . TRP A 640 ? 1.0567 0.6266 0.5504 -0.0447 0.2082 -0.0073 640 TRP A CZ2   
5221  C  CZ3   . TRP A 640 ? 1.055  0.6244 0.5448 -0.0429 0.2136 -0.0035 640 TRP A CZ3   
5222  C  CH2   . TRP A 640 ? 1.0571 0.6249 0.5484 -0.0452 0.2095 -0.0068 640 TRP A CH2   
5223  N  N     . VAL A 641 ? 1.0357 0.6076 0.5149 -0.024  0.2332 0.0131  641 VAL A N     
5224  C  CA    . VAL A 641 ? 1.0381 0.6157 0.5181 -0.021  0.2384 0.0182  641 VAL A CA    
5225  C  C     . VAL A 641 ? 1.0348 0.6272 0.5252 -0.0255 0.2379 0.0196  641 VAL A C     
5226  O  O     . VAL A 641 ? 1.0375 0.6293 0.5293 -0.0299 0.2351 0.0168  641 VAL A O     
5227  C  CB    . VAL A 641 ? 1.0526 0.6179 0.523  -0.0181 0.2407 0.0186  641 VAL A CB    
5228  C  CG1   . VAL A 641 ? 1.0561 0.6273 0.5274 -0.0144 0.2466 0.0243  641 VAL A CG1   
5229  C  CG2   . VAL A 641 ? 1.0675 0.6169 0.5267 -0.0146 0.2404 0.0167  641 VAL A CG2   
5230  N  N     . ILE A 642 ? 1.0267 0.6325 0.524  -0.0246 0.2407 0.0238  642 ILE A N     
5231  C  CA    . ILE A 642 ? 1.0235 0.6443 0.5308 -0.0293 0.24   0.0255  642 ILE A CA    
5232  C  C     . ILE A 642 ? 1.0236 0.6517 0.5328 -0.0274 0.2448 0.031   642 ILE A C     
5233  O  O     . ILE A 642 ? 1.0242 0.6544 0.5322 -0.022  0.2492 0.0354  642 ILE A O     
5234  C  CB    . ILE A 642 ? 1.0236 0.6562 0.5388 -0.0309 0.2386 0.0261  642 ILE A CB    
5235  C  CG1   . ILE A 642 ? 1.039  0.664  0.5517 -0.0311 0.2349 0.0216  642 ILE A CG1   
5236  C  CG2   . ILE A 642 ? 1.0216 0.6676 0.5459 -0.0371 0.2366 0.0265  642 ILE A CG2   
5237  C  CD1   . ILE A 642 ? 1.0571 0.6759 0.569  -0.036  0.23   0.0162  642 ILE A CD1   
5238  N  N     . LYS A 643 ? 1.0205 0.6528 0.5328 -0.0319 0.2441 0.031   643 LYS A N     
5239  C  CA    . LYS A 643 ? 1.0246 0.6653 0.5398 -0.031  0.2483 0.0363  643 LYS A CA    
5240  C  C     . LYS A 643 ? 1.0235 0.6805 0.5491 -0.0373 0.2467 0.0379  643 LYS A C     
5241  O  O     . LYS A 643 ? 1.0261 0.6822 0.5529 -0.0433 0.2431 0.0342  643 LYS A O     
5242  C  CB    . LYS A 643 ? 1.054  0.6836 0.5623 -0.0306 0.2495 0.0353  643 LYS A CB    
5243  C  CG    . LYS A 643 ? 1.1048 0.7413 0.6149 -0.0287 0.2545 0.0412  643 LYS A CG    
5244  C  CD    . LYS A 643 ? 1.1655 0.7904 0.6684 -0.0282 0.2557 0.0399  643 LYS A CD    
5245  C  CE    . LYS A 643 ? 1.2086 0.8387 0.7122 -0.025  0.2613 0.0461  643 LYS A CE    
5246  N  NZ    . LYS A 643 ? 1.2426 0.8599 0.7381 -0.0237 0.2628 0.0449  643 LYS A NZ    
5247  N  N     . PHE A 644 ? 1.0188 0.6905 0.5514 -0.036  0.2494 0.0434  644 PHE A N     
5248  C  CA    . PHE A 644 ? 1.0188 0.7069 0.5611 -0.0422 0.2478 0.0454  644 PHE A CA    
5249  C  C     . PHE A 644 ? 1.0213 0.7172 0.5665 -0.0434 0.251  0.0502  644 PHE A C     
5250  O  O     . PHE A 644 ? 1.0211 0.7206 0.5663 -0.0379 0.2559 0.0556  644 PHE A O     
5251  C  CB    . PHE A 644 ? 1.0128 0.7139 0.5617 -0.0404 0.2485 0.0489  644 PHE A CB    
5252  C  CG    . PHE A 644 ? 1.0241 0.7203 0.5718 -0.04   0.2452 0.0446  644 PHE A CG    
5253  C  CD1   . PHE A 644 ? 1.0322 0.7324 0.5842 -0.0464 0.2404 0.041   644 PHE A CD1   
5254  C  CD2   . PHE A 644 ? 1.0382 0.7258 0.5804 -0.0333 0.2472 0.0444  644 PHE A CD2   
5255  C  CE1   . PHE A 644 ? 1.0427 0.7388 0.5939 -0.0459 0.2377 0.0374  644 PHE A CE1   
5256  C  CE2   . PHE A 644 ? 1.0486 0.7321 0.5899 -0.0332 0.2443 0.0407  644 PHE A CE2   
5257  C  CZ    . PHE A 644 ? 1.0435 0.7316 0.5897 -0.0394 0.2395 0.0373  644 PHE A CZ    
5258  N  N     . LYS A 645 ? 1.0216 0.7204 0.5693 -0.0506 0.2485 0.0485  645 LYS A N     
5259  C  CA    . LYS A 645 ? 1.0273 0.7338 0.5781 -0.0528 0.2512 0.0529  645 LYS A CA    
5260  C  C     . LYS A 645 ? 1.0271 0.751  0.5874 -0.0601 0.2492 0.0554  645 LYS A C     
5261  O  O     . LYS A 645 ? 1.0282 0.7511 0.5888 -0.0672 0.2452 0.0514  645 LYS A O     
5262  C  CB    . LYS A 645 ? 1.0561 0.7494 0.6    -0.0551 0.2506 0.0491  645 LYS A CB    
5263  C  CG    . LYS A 645 ? 1.1057 0.8044 0.6511 -0.0558 0.2544 0.0539  645 LYS A CG    
5264  C  CD    . LYS A 645 ? 1.1622 0.8547 0.7026 -0.0472 0.2598 0.0575  645 LYS A CD    
5265  C  CE    . LYS A 645 ? 1.2029 0.8997 0.7445 -0.0479 0.2636 0.062   645 LYS A CE    
5266  N  NZ    . LYS A 645 ? 1.2345 0.9214 0.769  -0.0397 0.2686 0.0644  645 LYS A NZ    
5267  N  N     . PRO A 646 ? 1.0248 0.7647 0.5924 -0.0584 0.2521 0.0621  646 PRO A N     
5268  C  CA    . PRO A 646 ? 1.022  0.7795 0.5987 -0.0656 0.25   0.0649  646 PRO A CA    
5269  C  C     . PRO A 646 ? 1.0293 0.7927 0.6084 -0.0712 0.2509 0.0677  646 PRO A C     
5270  O  O     . PRO A 646 ? 1.0335 0.7943 0.6104 -0.0673 0.2551 0.0708  646 PRO A O     
5271  C  CB    . PRO A 646 ? 1.0221 0.7942 0.6054 -0.0606 0.2529 0.0714  646 PRO A CB    
5272  C  CG    . PRO A 646 ? 1.0298 0.7942 0.608  -0.0513 0.2583 0.0742  646 PRO A CG    
5273  C  CD    . PRO A 646 ? 1.0188 0.7617 0.5864 -0.0496 0.2574 0.0677  646 PRO A CD    
5274  N  N     . LYS A 647 ? 1.0284 0.7995 0.6116 -0.0804 0.2472 0.0666  647 LYS A N     
5275  C  CA    . LYS A 647 ? 1.0353 0.8127 0.6208 -0.0868 0.2478 0.0692  647 LYS A CA    
5276  C  C     . LYS A 647 ? 1.034  0.8329 0.6295 -0.0875 0.2501 0.0776  647 LYS A C     
5277  O  O     . LYS A 647 ? 1.0353 0.8399 0.633  -0.088  0.2533 0.0823  647 LYS A O     
5278  C  CB    . LYS A 647 ? 1.0574 0.832  0.6415 -0.0968 0.2427 0.0642  647 LYS A CB    
5279  C  CG    . LYS A 647 ? 1.1023 0.8813 0.6874 -0.1041 0.2432 0.0663  647 LYS A CG    
5280  C  CD    . LYS A 647 ? 1.1575 0.934  0.7405 -0.1143 0.2384 0.0617  647 LYS A CD    
5281  C  CE    . LYS A 647 ? 1.1963 0.9864 0.7858 -0.1192 0.2349 0.0629  647 LYS A CE    
5282  N  NZ    . LYS A 647 ? 1.2239 1.0124 0.811  -0.1298 0.2308 0.0595  647 LYS A NZ    
5283  N  N     . ASN A 648 ? 1.0303 0.8416 0.6321 -0.0876 0.2485 0.0797  648 ASN A N     
5284  C  CA    . ASN A 648 ? 1.0304 0.8637 0.6424 -0.0887 0.2501 0.0879  648 ASN A CA    
5285  C  C     . ASN A 648 ? 1.0367 0.8778 0.6525 -0.0803 0.2526 0.0919  648 ASN A C     
5286  O  O     . ASN A 648 ? 1.0462 0.8749 0.6564 -0.0743 0.2526 0.0879  648 ASN A O     
5287  C  CB    . ASN A 648 ? 1.0389 0.8834 0.6559 -0.0998 0.2451 0.0873  648 ASN A CB    
5288  C  CG    . ASN A 648 ? 1.0803 0.9171 0.694  -0.1027 0.2401 0.0806  648 ASN A CG    
5289  O  OD1   . ASN A 648 ? 1.0949 0.9299 0.7084 -0.0968 0.2401 0.0795  648 ASN A OD1   
5290  N  ND2   . ASN A 648 ? 1.0909 0.9222 0.7014 -0.1117 0.236  0.0758  648 ASN A ND2   
5291  N  N     . THR A 649 ? 1.0294 0.891  0.6545 -0.0799 0.2546 0.1001  649 THR A N     
5292  C  CA    . THR A 649 ? 1.0323 0.9035 0.6617 -0.072  0.2575 0.1051  649 THR A CA    
5293  C  C     . THR A 649 ? 1.0327 0.9042 0.6627 -0.0727 0.2535 0.1014  649 THR A C     
5294  O  O     . THR A 649 ? 1.034  0.904  0.663  -0.0645 0.2559 0.1025  649 THR A O     
5295  C  CB    . THR A 649 ? 1.0418 0.9362 0.6816 -0.0724 0.2603 0.115   649 THR A CB    
5296  O  OG1   . THR A 649 ? 1.0527 0.9606 0.699  -0.0834 0.2554 0.1154  649 THR A OG1   
5297  C  CG2   . THR A 649 ? 1.0462 0.9401 0.6853 -0.0695 0.2654 0.1195  649 THR A CG2   
5298  N  N     . ILE A 650 ? 1.0293 0.9018 0.6602 -0.0821 0.2477 0.0969  650 ILE A N     
5299  C  CA    . ILE A 650 ? 1.034  0.9056 0.6648 -0.083  0.2438 0.093   650 ILE A CA    
5300  C  C     . ILE A 650 ? 1.044  0.8939 0.6653 -0.0776 0.2437 0.0857  650 ILE A C     
5301  O  O     . ILE A 650 ? 1.0444 0.892  0.6648 -0.0716 0.2444 0.0852  650 ILE A O     
5302  C  CB    . ILE A 650 ? 1.0406 0.9177 0.6738 -0.0946 0.2378 0.0901  650 ILE A CB    
5303  C  CG1   . ILE A 650 ? 1.0443 0.9452 0.6876 -0.0998 0.2374 0.0978  650 ILE A CG1   
5304  C  CG2   . ILE A 650 ? 1.0496 0.9202 0.6801 -0.0955 0.2337 0.0843  650 ILE A CG2   
5305  C  CD1   . ILE A 650 ? 1.0546 0.9714 0.7052 -0.0947 0.2387 0.1035  650 ILE A CD1   
5306  N  N     . ALA A 651 ? 1.0507 0.8847 0.6647 -0.0797 0.2431 0.0806  651 ALA A N     
5307  C  CA    . ALA A 651 ? 1.0664 0.8799 0.6713 -0.075  0.2428 0.074   651 ALA A CA    
5308  C  C     . ALA A 651 ? 1.0755 0.8839 0.6774 -0.0642 0.2481 0.0769  651 ALA A C     
5309  O  O     . ALA A 651 ? 1.084  0.8808 0.6806 -0.0593 0.2479 0.0731  651 ALA A O     
5310  C  CB    . ALA A 651 ? 1.0743 0.8735 0.6726 -0.0793 0.2414 0.0689  651 ALA A CB    
5311  N  N     . GLU A 652 ? 1.0725 0.8895 0.6775 -0.0606 0.2529 0.0838  652 GLU A N     
5312  C  CA    . GLU A 652 ? 1.0828 0.8954 0.6844 -0.0502 0.2586 0.0874  652 GLU A CA    
5313  C  C     . GLU A 652 ? 1.0842 0.904  0.6888 -0.0449 0.2596 0.0899  652 GLU A C     
5314  O  O     . GLU A 652 ? 1.0917 0.9001 0.6899 -0.0372 0.2621 0.0887  652 GLU A O     
5315  C  CB    . GLU A 652 ? 1.1075 0.9297 0.7125 -0.048  0.2636 0.0949  652 GLU A CB    
5316  C  CG    . GLU A 652 ? 1.1745 0.9892 0.7741 -0.0371 0.27   0.0984  652 GLU A CG    
5317  C  CD    . GLU A 652 ? 1.2532 1.075  0.8551 -0.0346 0.2752 0.1054  652 GLU A CD    
5318  O  OE1   . GLU A 652 ? 1.2655 1.0912 0.8702 -0.0416 0.2737 0.1054  652 GLU A OE1   
5319  O  OE2   . GLU A 652 ? 1.282  1.1049 0.8826 -0.0256 0.2811 0.111   652 GLU A OE2   
5320  N  N     . LYS A 653 ? 1.0757 0.9135 0.6893 -0.0491 0.2574 0.0932  653 LYS A N     
5321  C  CA    . LYS A 653 ? 1.0776 0.9231 0.6944 -0.0446 0.258  0.0955  653 LYS A CA    
5322  C  C     . LYS A 653 ? 1.0846 0.9152 0.6953 -0.0444 0.2545 0.0876  653 LYS A C     
5323  O  O     . LYS A 653 ? 1.0876 0.9143 0.6956 -0.0374 0.2566 0.088   653 LYS A O     
5324  C  CB    . LYS A 653 ? 1.0927 0.9608 0.7204 -0.0502 0.2557 0.1003  653 LYS A CB    
5325  C  CG    . LYS A 653 ? 1.1392 1.0247 0.7741 -0.0486 0.26   0.1097  653 LYS A CG    
5326  C  CD    . LYS A 653 ? 1.1863 1.095  0.832  -0.0531 0.2579 0.1151  653 LYS A CD    
5327  C  CE    . LYS A 653 ? 1.2268 1.1537 0.8803 -0.0532 0.2614 0.1242  653 LYS A CE    
5328  N  NZ    . LYS A 653 ? 1.2464 1.1964 0.9105 -0.0592 0.2585 0.1293  653 LYS A NZ    
5329  N  N     . LEU A 654 ? 1.0858 0.9077 0.6938 -0.0518 0.2494 0.0808  654 LEU A N     
5330  C  CA    . LEU A 654 ? 1.0954 0.903  0.6977 -0.0521 0.2459 0.0733  654 LEU A CA    
5331  C  C     . LEU A 654 ? 1.1066 0.8956 0.6994 -0.0449 0.2487 0.0706  654 LEU A C     
5332  O  O     . LEU A 654 ? 1.1116 0.8931 0.7007 -0.0402 0.2489 0.0683  654 LEU A O     
5333  C  CB    . LEU A 654 ? 1.099  0.9018 0.7004 -0.0615 0.2404 0.0674  654 LEU A CB    
5334  C  CG    . LEU A 654 ? 1.1229 0.9092 0.7177 -0.0621 0.2369 0.0595  654 LEU A CG    
5335  C  CD1   . LEU A 654 ? 1.127  0.9168 0.724  -0.06   0.2356 0.0588  654 LEU A CD1   
5336  C  CD2   . LEU A 654 ? 1.1331 0.9152 0.7268 -0.0709 0.2324 0.0546  654 LEU A CD2   
5337  N  N     . VAL A 655 ? 1.1088 0.8905 0.6974 -0.0439 0.2511 0.071   655 VAL A N     
5338  C  CA    . VAL A 655 ? 1.1237 0.8875 0.7026 -0.0374 0.2538 0.0686  655 VAL A CA    
5339  C  C     . VAL A 655 ? 1.1322 0.8966 0.7093 -0.0281 0.2588 0.0732  655 VAL A C     
5340  O  O     . VAL A 655 ? 1.1412 0.8921 0.7111 -0.0236 0.2591 0.0698  655 VAL A O     
5341  C  CB    . VAL A 655 ? 1.133  0.8904 0.7082 -0.0383 0.2555 0.0689  655 VAL A CB    
5342  C  CG1   . VAL A 655 ? 1.1487 0.8893 0.7139 -0.0307 0.2592 0.0681  655 VAL A CG1   
5343  C  CG2   . VAL A 655 ? 1.14   0.8915 0.7141 -0.0466 0.2505 0.063   655 VAL A CG2   
5344  N  N     . ASN A 656 ? 1.1265 0.9067 0.71   -0.0253 0.2627 0.0809  656 ASN A N     
5345  C  CA    . ASN A 656 ? 1.1332 0.9149 0.7149 -0.0161 0.2681 0.086   656 ASN A CA    
5346  C  C     . ASN A 656 ? 1.1336 0.9158 0.7159 -0.0145 0.2663 0.084   656 ASN A C     
5347  O  O     . ASN A 656 ? 1.1405 0.9134 0.7163 -0.0072 0.2695 0.0842  656 ASN A O     
5348  C  CB    . ASN A 656 ? 1.1414 0.9421 0.7311 -0.0139 0.2725 0.0952  656 ASN A CB    
5349  C  CG    . ASN A 656 ? 1.1877 0.986  0.7754 -0.013  0.2759 0.0981  656 ASN A CG    
5350  O  OD1   . ASN A 656 ? 1.2133 0.9939 0.7918 -0.0112 0.2766 0.0941  656 ASN A OD1   
5351  N  ND2   . ASN A 656 ? 1.1886 1.0051 0.785  -0.0142 0.2781 0.1053  656 ASN A ND2   
5352  N  N     . TYR A 657 ? 1.1245 0.9165 0.7137 -0.0215 0.2613 0.0818  657 TYR A N     
5353  C  CA    . TYR A 657 ? 1.1277 0.9207 0.718  -0.0211 0.2589 0.0795  657 TYR A CA    
5354  C  C     . TYR A 657 ? 1.1353 0.9078 0.7164 -0.0202 0.2567 0.0719  657 TYR A C     
5355  O  O     . TYR A 657 ? 1.1409 0.9076 0.7182 -0.015  0.2581 0.0713  657 TYR A O     
5356  C  CB    . TYR A 657 ? 1.1229 0.9301 0.7221 -0.0297 0.2537 0.0787  657 TYR A CB    
5357  C  CG    . TYR A 657 ? 1.1339 0.9407 0.734  -0.0308 0.2503 0.075   657 TYR A CG    
5358  C  CD1   . TYR A 657 ? 1.1418 0.9585 0.7455 -0.0261 0.2525 0.0793  657 TYR A CD1   
5359  C  CD2   . TYR A 657 ? 1.1501 0.9478 0.7481 -0.0369 0.2449 0.0677  657 TYR A CD2   
5360  C  CE1   . TYR A 657 ? 1.1541 0.9707 0.7588 -0.0272 0.2494 0.076   657 TYR A CE1   
5361  C  CE2   . TYR A 657 ? 1.1621 0.9599 0.7612 -0.038  0.2419 0.0646  657 TYR A CE2   
5362  C  CZ    . TYR A 657 ? 1.1696 0.9769 0.7721 -0.0333 0.2441 0.0686  657 TYR A CZ    
5363  O  OH    . TYR A 657 ? 1.1881 0.995  0.7915 -0.0343 0.2412 0.0655  657 TYR A OH    
5364  N  N     . ILE A 658 ? 1.133  0.8945 0.7103 -0.0251 0.2534 0.0664  658 ILE A N     
5365  C  CA    . ILE A 658 ? 1.1408 0.8834 0.7096 -0.0248 0.251  0.0594  658 ILE A CA    
5366  C  C     . ILE A 658 ? 1.1503 0.8796 0.7099 -0.0166 0.2557 0.0604  658 ILE A C     
5367  O  O     . ILE A 658 ? 1.1572 0.8761 0.7112 -0.0134 0.2554 0.0575  658 ILE A O     
5368  C  CB    . ILE A 658 ? 1.1457 0.8806 0.7126 -0.0315 0.247  0.0542  658 ILE A CB    
5369  C  CG1   . ILE A 658 ? 1.1501 0.8954 0.7243 -0.0399 0.2422 0.0524  658 ILE A CG1   
5370  C  CG2   . ILE A 658 ? 1.1591 0.8747 0.7171 -0.0304 0.2451 0.0479  658 ILE A CG2   
5371  C  CD1   . ILE A 658 ? 1.1661 0.9061 0.7389 -0.0464 0.2392 0.0487  658 ILE A CD1   
5372  N  N     . LYS A 659 ? 1.1486 0.8783 0.7062 -0.0131 0.2602 0.0649  659 LYS A N     
5373  C  CA    . LYS A 659 ? 1.1614 0.878  0.7094 -0.0052 0.2651 0.0664  659 LYS A CA    
5374  C  C     . LYS A 659 ? 1.1634 0.8818 0.7099 0.0018  0.2688 0.0699  659 LYS A C     
5375  O  O     . LYS A 659 ? 1.1735 0.8768 0.7107 0.0061  0.27   0.0673  659 LYS A O     
5376  C  CB    . LYS A 659 ? 1.1858 0.905  0.7332 -0.0027 0.2696 0.0715  659 LYS A CB    
5377  C  CG    . LYS A 659 ? 1.2447 0.9537 0.788  -0.0069 0.2673 0.0675  659 LYS A CG    
5378  C  CD    . LYS A 659 ? 1.3013 1.0104 0.8425 -0.0032 0.2725 0.0725  659 LYS A CD    
5379  C  CE    . LYS A 659 ? 1.3578 1.0544 0.8887 0.006   0.2781 0.0749  659 LYS A CE    
5380  N  NZ    . LYS A 659 ? 1.3867 1.0816 0.9145 0.0098  0.2832 0.0795  659 LYS A NZ    
5381  N  N     . LEU A 660 ? 1.1521 0.8888 0.7074 0.0027  0.2707 0.0757  660 LEU A N     
5382  C  CA    . LEU A 660 ? 1.155  0.8952 0.7096 0.0096  0.2747 0.0798  660 LEU A CA    
5383  C  C     . LEU A 660 ? 1.1574 0.8928 0.7109 0.0082  0.2711 0.0747  660 LEU A C     
5384  O  O     . LEU A 660 ? 1.1645 0.8917 0.7115 0.0143  0.274  0.0751  660 LEU A O     
5385  C  CB    . LEU A 660 ? 1.1479 0.9109 0.7134 0.0103  0.2771 0.0875  660 LEU A CB    
5386  C  CG    . LEU A 660 ? 1.1682 0.9352 0.7319 0.0185  0.2847 0.0956  660 LEU A CG    
5387  C  CD1   . LEU A 660 ? 1.1794 0.9393 0.7392 0.0182  0.2864 0.0959  660 LEU A CD1   
5388  C  CD2   . LEU A 660 ? 1.1658 0.9569 0.7414 0.0187  0.2864 0.1032  660 LEU A CD2   
5389  N  N     . ASN A 661 ? 1.1504 0.8903 0.7099 0.0003  0.2649 0.0701  661 ASN A N     
5390  C  CA    . ASN A 661 ? 1.1556 0.8921 0.715  -0.0014 0.2613 0.0655  661 ASN A CA    
5391  C  C     . ASN A 661 ? 1.164  0.8824 0.7161 -0.0043 0.2573 0.0578  661 ASN A C     
5392  O  O     . ASN A 661 ? 1.1661 0.8836 0.7203 -0.0083 0.2528 0.0532  661 ASN A O     
5393  C  CB    . ASN A 661 ? 1.162  0.9155 0.7324 -0.0075 0.2573 0.0659  661 ASN A CB    
5394  C  CG    . ASN A 661 ? 1.1928 0.9645 0.7703 -0.0042 0.261  0.0736  661 ASN A CG    
5395  O  OD1   . ASN A 661 ? 1.1998 0.9853 0.7843 -0.0068 0.2614 0.0779  661 ASN A OD1   
5396  N  ND2   . ASN A 661 ? 1.2009 0.9732 0.7769 0.0017  0.2638 0.0757  661 ASN A ND2   
5397  N  N     . PHE A 662 ? 1.1662 0.8703 0.7096 -0.002  0.259  0.0565  662 PHE A N     
5398  C  CA    . PHE A 662 ? 1.1768 0.8638 0.7128 -0.0043 0.2554 0.0497  662 PHE A CA    
5399  C  C     . PHE A 662 ? 1.1879 0.8627 0.7155 0.0011  0.2574 0.0486  662 PHE A C     
5400  O  O     . PHE A 662 ? 1.198  0.8582 0.7155 0.005   0.2599 0.0481  662 PHE A O     
5401  C  CB    . PHE A 662 ? 1.1788 0.8559 0.7091 -0.0049 0.2558 0.0485  662 PHE A CB    
5402  C  CG    . PHE A 662 ? 1.1899 0.8561 0.7174 -0.0104 0.2503 0.0415  662 PHE A CG    
5403  C  CD1   . PHE A 662 ? 1.1944 0.8672 0.7284 -0.0173 0.2461 0.0391  662 PHE A CD1   
5404  C  CD2   . PHE A 662 ? 1.2079 0.857  0.7258 -0.0085 0.2494 0.0375  662 PHE A CD2   
5405  C  CE1   . PHE A 662 ? 1.2069 0.8697 0.738  -0.0218 0.2414 0.0331  662 PHE A CE1   
5406  C  CE2   . PHE A 662 ? 1.2201 0.8603 0.7359 -0.0133 0.2443 0.0315  662 PHE A CE2   
5407  C  CZ    . PHE A 662 ? 1.2126 0.8597 0.7351 -0.0196 0.2405 0.0295  662 PHE A CZ    
5408  N  N     . LYS A 663 ? 1.1844 0.8652 0.7159 0.0012  0.2565 0.0484  663 LYS A N     
5409  C  CA    . LYS A 663 ? 1.1946 0.8654 0.7191 0.0058  0.2582 0.0474  663 LYS A CA    
5410  C  C     . LYS A 663 ? 1.1913 0.8668 0.7215 0.0018  0.2537 0.0439  663 LYS A C     
5411  O  O     . LYS A 663 ? 1.1827 0.8733 0.7228 -0.0017 0.2518 0.0451  663 LYS A O     
5412  C  CB    . LYS A 663 ? 1.2178 0.8932 0.7403 0.0136  0.265  0.0541  663 LYS A CB    
5413  C  CG    . LYS A 663 ? 1.2782 0.9401 0.7908 0.019   0.2677 0.0534  663 LYS A CG    
5414  C  CD    . LYS A 663 ? 1.3312 1.0009 0.844  0.0263  0.274  0.0601  663 LYS A CD    
5415  C  CE    . LYS A 663 ? 1.3813 1.0407 0.8865 0.0303  0.2757 0.0588  663 LYS A CE    
5416  N  NZ    . LYS A 663 ? 1.4026 1.0674 0.9145 0.0255  0.2707 0.0549  663 LYS A NZ    
5417  N  N     . SER A 664 ? 1.1962 0.8585 0.7199 0.002   0.2521 0.0395  664 SER A N     
5418  C  CA    . SER A 664 ? 1.1987 0.8641 0.7272 -0.0015 0.2481 0.0361  664 SER A CA    
5419  C  C     . SER A 664 ? 1.2077 0.8615 0.7287 0.002   0.2492 0.0344  664 SER A C     
5420  O  O     . SER A 664 ? 1.2191 0.8577 0.7297 0.0045  0.2507 0.0332  664 SER A O     
5421  C  CB    . SER A 664 ? 1.2153 0.8781 0.7465 -0.0086 0.242  0.0306  664 SER A CB    
5422  O  OG    . SER A 664 ? 1.2426 0.9076 0.7781 -0.0118 0.2383 0.0273  664 SER A OG    
5423  N  N     . ASN A 665 ? 1.201  0.8614 0.7266 0.0018  0.2484 0.0342  665 ASN A N     
5424  C  CA    . ASN A 665 ? 1.2099 0.8599 0.7292 0.0043  0.2491 0.0323  665 ASN A CA    
5425  C  C     . ASN A 665 ? 1.21   0.8518 0.7289 -0.0013 0.2433 0.0259  665 ASN A C     
5426  O  O     . ASN A 665 ? 1.2188 0.8493 0.7311 -0.0001 0.2433 0.0236  665 ASN A O     
5427  C  CB    . ASN A 665 ? 1.222  0.8828 0.7461 0.0074  0.2515 0.0355  665 ASN A CB    
5428  C  CG    . ASN A 665 ? 1.263  0.9306 0.7862 0.0139  0.2578 0.0422  665 ASN A CG    
5429  O  OD1   . ASN A 665 ? 1.2813 0.9436 0.7988 0.0171  0.2611 0.0446  665 ASN A OD1   
5430  N  ND2   . ASN A 665 ? 1.2664 0.9461 0.7952 0.0164  0.2597 0.0457  665 ASN A ND2   
5431  N  N     . ILE A 666 ? 1.1989 0.846  0.7245 -0.0072 0.2386 0.0232  666 ILE A N     
5432  C  CA    . ILE A 666 ? 1.2009 0.8418 0.727  -0.0123 0.2333 0.0177  666 ILE A CA    
5433  C  C     . ILE A 666 ? 1.2032 0.8342 0.7246 -0.0148 0.2311 0.015   666 ILE A C     
5434  O  O     . ILE A 666 ? 1.2103 0.8288 0.7254 -0.0156 0.2291 0.0117  666 ILE A O     
5435  C  CB    . ILE A 666 ? 1.2004 0.8542 0.7371 -0.0169 0.2298 0.0166  666 ILE A CB    
5436  C  CG1   . ILE A 666 ? 1.2102 0.8733 0.751  -0.0143 0.2318 0.0192  666 ILE A CG1   
5437  C  CG2   . ILE A 666 ? 1.2075 0.8553 0.745  -0.0218 0.2246 0.0113  666 ILE A CG2   
5438  C  CD1   . ILE A 666 ? 1.2202 0.8972 0.771  -0.0184 0.229  0.0191  666 ILE A CD1   
5439  N  N     . PHE A 667 ? 1.1958 0.8326 0.7201 -0.0161 0.2313 0.0166  667 PHE A N     
5440  C  CA    . PHE A 667 ? 1.202  0.8305 0.7223 -0.0185 0.2293 0.0143  667 PHE A CA    
5441  C  C     . PHE A 667 ? 1.2083 0.8256 0.7185 -0.014  0.233  0.016   667 PHE A C     
5442  O  O     . PHE A 667 ? 1.209  0.8302 0.7181 -0.0096 0.2378 0.0205  667 PHE A O     
5443  C  CB    . PHE A 667 ? 1.1957 0.8346 0.7232 -0.0224 0.2278 0.0149  667 PHE A CB    
5444  C  CG    . PHE A 667 ? 1.2064 0.8388 0.7328 -0.0269 0.2236 0.0108  667 PHE A CG    
5445  C  CD1   . PHE A 667 ? 1.2156 0.8484 0.7458 -0.0313 0.2191 0.007   667 PHE A CD1   
5446  C  CD2   . PHE A 667 ? 1.2194 0.8457 0.7411 -0.0266 0.2244 0.011   667 PHE A CD2   
5447  C  CE1   . PHE A 667 ? 1.2267 0.8535 0.7556 -0.0349 0.2156 0.0035  667 PHE A CE1   
5448  C  CE2   . PHE A 667 ? 1.2302 0.8509 0.7509 -0.0306 0.2207 0.0075  667 PHE A CE2   
5449  C  CZ    . PHE A 667 ? 1.2267 0.8477 0.751  -0.0346 0.2164 0.0038  667 PHE A CZ    
5450  N  N     . ASP A 668 ? 1.2115 0.8149 0.7142 -0.0151 0.2309 0.0126  668 ASP A N     
5451  C  CA    . ASP A 668 ? 1.2226 0.8132 0.7144 -0.0115 0.2338 0.0136  668 ASP A CA    
5452  C  C     . ASP A 668 ? 1.2227 0.8168 0.7156 -0.0116 0.2351 0.0156  668 ASP A C     
5453  O  O     . ASP A 668 ? 1.2246 0.8151 0.7173 -0.0152 0.2318 0.0127  668 ASP A O     
5454  C  CB    . ASP A 668 ? 1.2497 0.8254 0.7338 -0.0137 0.2302 0.0091  668 ASP A CB    
5455  C  CG    . ASP A 668 ? 1.3172 0.8774 0.7881 -0.0099 0.233  0.0098  668 ASP A CG    
5456  O  OD1   . ASP A 668 ? 1.329  0.889  0.7965 -0.006  0.2375 0.0134  668 ASP A OD1   
5457  O  OD2   . ASP A 668 ? 1.3501 0.8981 0.8137 -0.0109 0.2309 0.0069  668 ASP A OD2   
5458  N  N     . THR A 669 ? 1.219  0.8201 0.7129 -0.0074 0.2401 0.0206  669 THR A N     
5459  C  CA    . THR A 669 ? 1.2231 0.8281 0.7182 -0.0072 0.242  0.0232  669 THR A CA    
5460  C  C     . THR A 669 ? 1.2346 0.8244 0.7183 -0.0047 0.2437 0.0228  669 THR A C     
5461  O  O     . THR A 669 ? 1.2361 0.8276 0.7201 -0.0046 0.2451 0.0246  669 THR A O     
5462  C  CB    . THR A 669 ? 1.2338 0.8525 0.7345 -0.0036 0.2467 0.0291  669 THR A CB    
5463  O  OG1   . THR A 669 ? 1.2515 0.8638 0.7445 0.0029  0.2517 0.0321  669 THR A OG1   
5464  C  CG2   . THR A 669 ? 1.2301 0.8646 0.7422 -0.0068 0.2446 0.0295  669 THR A CG2   
5465  N  N     . GLY A 670 ? 1.241  0.816  0.7147 -0.0029 0.2435 0.0206  670 GLY A N     
5466  C  CA    . GLY A 670 ? 1.2559 0.8147 0.7174 -0.0008 0.2447 0.0199  670 GLY A CA    
5467  C  C     . GLY A 670 ? 1.2606 0.8147 0.7218 -0.0055 0.2401 0.016   670 GLY A C     
5468  O  O     . GLY A 670 ? 1.268  0.8113 0.7206 -0.004  0.2412 0.016   670 GLY A O     
5469  N  N     . PHE A 671 ? 1.2543 0.8162 0.7244 -0.011  0.235  0.0129  671 PHE A N     
5470  C  CA    . PHE A 671 ? 1.2607 0.8196 0.7316 -0.0155 0.2307 0.0094  671 PHE A CA    
5471  C  C     . PHE A 671 ? 1.2585 0.8258 0.7344 -0.0163 0.2321 0.0116  671 PHE A C     
5472  O  O     . PHE A 671 ? 1.2606 0.8252 0.7366 -0.0196 0.2293 0.0092  671 PHE A O     
5473  C  CB    . PHE A 671 ? 1.2582 0.8217 0.7361 -0.0206 0.2252 0.0056  671 PHE A CB    
5474  C  CG    . PHE A 671 ? 1.2752 0.8294 0.7495 -0.024  0.2205 0.0013  671 PHE A CG    
5475  C  CD1   . PHE A 671 ? 1.2934 0.835  0.7594 -0.0238 0.2186 -0.0009 671 PHE A CD1   
5476  C  CD2   . PHE A 671 ? 1.2858 0.8441 0.7648 -0.0277 0.2179 -0.0002 671 PHE A CD2   
5477  C  CE1   . PHE A 671 ? 1.3075 0.8416 0.7706 -0.0269 0.2141 -0.0044 671 PHE A CE1   
5478  C  CE2   . PHE A 671 ? 1.3    0.8501 0.7755 -0.0304 0.2138 -0.0037 671 PHE A CE2   
5479  C  CZ    . PHE A 671 ? 1.3037 0.8424 0.7718 -0.03   0.2118 -0.0057 671 PHE A CZ    
5480  N  N     . PHE A 672 ? 1.2522 0.8294 0.7321 -0.0134 0.2367 0.0163  672 PHE A N     
5481  C  CA    . PHE A 672 ? 1.251  0.8371 0.7361 -0.0145 0.2382 0.0188  672 PHE A CA    
5482  C  C     . PHE A 672 ? 1.2562 0.8397 0.7357 -0.0089 0.2441 0.0236  672 PHE A C     
5483  O  O     . PHE A 672 ? 1.2584 0.8396 0.7337 -0.0038 0.248  0.0264  672 PHE A O     
5484  C  CB    . PHE A 672 ? 1.2405 0.8443 0.7376 -0.017  0.2379 0.0208  672 PHE A CB    
5485  C  CG    . PHE A 672 ? 1.2454 0.8535 0.7489 -0.0227 0.2325 0.0167  672 PHE A CG    
5486  C  CD1   . PHE A 672 ? 1.2554 0.8636 0.7603 -0.023  0.2306 0.0149  672 PHE A CD1   
5487  C  CD2   . PHE A 672 ? 1.2529 0.8647 0.7606 -0.0277 0.2296 0.0148  672 PHE A CD2   
5488  C  CE1   . PHE A 672 ? 1.2611 0.8731 0.7718 -0.0279 0.2259 0.0113  672 PHE A CE1   
5489  C  CE2   . PHE A 672 ? 1.2593 0.8744 0.7722 -0.0326 0.2251 0.0112  672 PHE A CE2   
5490  C  CZ    . PHE A 672 ? 1.2562 0.8716 0.7708 -0.0326 0.2233 0.0096  672 PHE A CZ    
5491  N  N     . HIS A 673 ? 1.2568 0.8415 0.7367 -0.0097 0.2452 0.0248  673 HIS A N     
5492  C  CA    . HIS A 673 ? 1.2655 0.8495 0.7415 -0.0046 0.251  0.0297  673 HIS A CA    
5493  C  C     . HIS A 673 ? 1.2609 0.8595 0.7464 -0.0074 0.2516 0.0325  673 HIS A C     
5494  O  O     . HIS A 673 ? 1.2625 0.86   0.7493 -0.0117 0.2488 0.0299  673 HIS A O     
5495  C  CB    . HIS A 673 ? 1.2877 0.8546 0.7516 -0.0024 0.2517 0.0282  673 HIS A CB    
5496  C  CG    . HIS A 673 ? 1.3241 0.8901 0.784  0.0028  0.2579 0.0334  673 HIS A CG    
5497  N  ND1   . HIS A 673 ? 1.3478 0.9157 0.8091 0.0014  0.2586 0.0344  673 HIS A ND1   
5498  C  CD2   . HIS A 673 ? 1.3424 0.9067 0.7974 0.0094  0.2637 0.0381  673 HIS A CD2   
5499  C  CE1   . HIS A 673 ? 1.3562 0.9233 0.8134 0.0072  0.2647 0.0396  673 HIS A CE1   
5500  N  NE2   . HIS A 673 ? 1.3572 0.9221 0.8105 0.0123  0.2681 0.0421  673 HIS A NE2   
5501  N  N     . ILE A 674 ? 1.2536 0.8663 0.7461 -0.0053 0.2552 0.0377  674 ILE A N     
5502  C  CA    . ILE A 674 ? 1.2521 0.8795 0.7538 -0.0084 0.2558 0.0408  674 ILE A CA    
5503  C  C     . ILE A 674 ? 1.2603 0.8863 0.7582 -0.0039 0.2614 0.0457  674 ILE A C     
5504  O  O     . ILE A 674 ? 1.2606 0.8892 0.7569 0.0021  0.2666 0.0509  674 ILE A O     
5505  C  CB    . ILE A 674 ? 1.2478 0.8933 0.7608 -0.0105 0.2553 0.0434  674 ILE A CB    
5506  C  CG1   . ILE A 674 ? 1.2591 0.9074 0.7709 -0.0039 0.2598 0.0477  674 ILE A CG1   
5507  C  CG2   . ILE A 674 ? 1.2516 0.898  0.7686 -0.0164 0.2492 0.0379  674 ILE A CG2   
5508  C  CD1   . ILE A 674 ? 1.2658 0.9323 0.7882 -0.0052 0.2599 0.0511  674 ILE A CD1   
5509  N  N     . GLU A 675 ? 1.2654 0.8859 0.7608 -0.0064 0.2604 0.044   675 GLU A N     
5510  C  CA    . GLU A 675 ? 1.2755 0.8931 0.7668 -0.0028 0.2652 0.0479  675 GLU A CA    
5511  C  C     . GLU A 675 ? 1.2722 0.9078 0.7727 -0.0019 0.2692 0.0548  675 GLU A C     
5512  O  O     . GLU A 675 ? 1.2749 0.9103 0.7722 0.0041  0.275  0.0602  675 GLU A O     
5513  C  CB    . GLU A 675 ? 1.3051 0.9155 0.7938 -0.0072 0.2624 0.0441  675 GLU A CB    
5514  C  CG    . GLU A 675 ? 1.3629 0.9688 0.8467 -0.0038 0.267  0.0476  675 GLU A CG    
5515  C  CD    . GLU A 675 ? 1.4287 1.0304 0.9118 -0.0085 0.2644 0.0444  675 GLU A CD    
5516  O  OE1   . GLU A 675 ? 1.4421 1.0395 0.9253 -0.0135 0.259  0.0388  675 GLU A OE1   
5517  O  OE2   . GLU A 675 ? 1.4484 1.051  0.9307 -0.0071 0.2681 0.0478  675 GLU A OE2   
5518  N  N     . GLY A 676 ? 1.2642 0.9152 0.7758 -0.0077 0.2662 0.0549  676 GLY A N     
5519  C  CA    . GLY A 676 ? 1.2615 0.9315 0.7831 -0.0082 0.2689 0.0612  676 GLY A CA    
5520  C  C     . GLY A 676 ? 1.2572 0.9411 0.7893 -0.0161 0.2641 0.0597  676 GLY A C     
5521  O  O     . GLY A 676 ? 1.2613 0.9395 0.7927 -0.0217 0.2591 0.0538  676 GLY A O     
5522  O  "O5'" . DG  B 1   ? 0.9802 0.4235 0.3719 -0.0855 0.2208 -0.0339 1   DG  E "O5'" 
5523  C  "C5'" . DG  B 1   ? 0.9854 0.4211 0.372  -0.0796 0.2216 -0.0337 1   DG  E "C5'" 
5524  C  "C4'" . DG  B 1   ? 0.9819 0.4243 0.3762 -0.0749 0.2186 -0.0329 1   DG  E "C4'" 
5525  O  "O4'" . DG  B 1   ? 0.9739 0.4268 0.3783 -0.0739 0.2152 -0.0326 1   DG  E "O4'" 
5526  C  "C3'" . DG  B 1   ? 0.9828 0.4282 0.3794 -0.0771 0.2181 -0.033  1   DG  E "C3'" 
5527  O  "O3'" . DG  B 1   ? 0.9865 0.4311 0.384  -0.0718 0.2175 -0.0321 1   DG  E "O3'" 
5528  C  "C2'" . DG  B 1   ? 0.9725 0.4305 0.3801 -0.0797 0.215  -0.033  1   DG  E "C2'" 
5529  C  "C1'" . DG  B 1   ? 0.9658 0.4277 0.3783 -0.0755 0.2129 -0.0325 1   DG  E "C1'" 
5530  N  N9    . DG  B 1   ? 0.9573 0.4279 0.3767 -0.0782 0.2113 -0.0324 1   DG  E N9    
5531  C  C8    . DG  B 1   ? 0.9552 0.4268 0.3734 -0.0834 0.2128 -0.0326 1   DG  E C8    
5532  N  N7    . DG  B 1   ? 0.9489 0.4297 0.3748 -0.0845 0.211  -0.0321 1   DG  E N7    
5533  C  C5    . DG  B 1   ? 0.9469 0.4325 0.379  -0.08   0.2081 -0.0318 1   DG  E C5    
5534  C  C6    . DG  B 1   ? 0.9425 0.4372 0.3832 -0.0787 0.2056 -0.0312 1   DG  E C6    
5535  O  O6    . DG  B 1   ? 0.9394 0.4402 0.3841 -0.0809 0.2055 -0.0306 1   DG  E O6    
5536  N  N1    . DG  B 1   ? 0.9417 0.4381 0.386  -0.0743 0.2031 -0.031  1   DG  E N1    
5537  C  C2    . DG  B 1   ? 0.9424 0.4335 0.3833 -0.0712 0.2031 -0.0311 1   DG  E C2    
5538  N  N2    . DG  B 1   ? 0.9394 0.4342 0.3853 -0.0675 0.2003 -0.0306 1   DG  E N2    
5539  N  N3    . DG  B 1   ? 0.948  0.4306 0.3809 -0.0718 0.2057 -0.0314 1   DG  E N3    
5540  C  C4    . DG  B 1   ? 0.9504 0.4304 0.3791 -0.0764 0.2082 -0.0319 1   DG  E C4    
5541  P  P     . DT  B 2   ? 0.9887 0.4322 0.3851 -0.0727 0.2183 -0.0319 2   DT  E P     
5542  O  OP1   . DT  B 2   ? 0.9969 0.4311 0.3857 -0.0678 0.2207 -0.031  2   DT  E OP1   
5543  O  OP2   . DT  B 2   ? 0.9881 0.4304 0.3813 -0.0799 0.2195 -0.0331 2   DT  E OP2   
5544  O  "O5'" . DT  B 2   ? 0.9774 0.4333 0.3863 -0.0707 0.2142 -0.0312 2   DT  E "O5'" 
5545  C  "C5'" . DT  B 2   ? 0.9725 0.4321 0.3865 -0.0647 0.2121 -0.03   2   DT  E "C5'" 
5546  C  "C4'" . DT  B 2   ? 0.964  0.4356 0.3897 -0.0647 0.2082 -0.0297 2   DT  E "C4'" 
5547  O  "O4'" . DT  B 2   ? 0.9606 0.4374 0.3901 -0.0682 0.2069 -0.0306 2   DT  E "O4'" 
5548  C  "C3'" . DT  B 2   ? 0.9631 0.4385 0.3922 -0.0668 0.2079 -0.0298 2   DT  E "C3'" 
5549  O  "O3'" . DT  B 2   ? 0.9586 0.4409 0.3956 -0.063  0.2053 -0.0286 2   DT  E "O3'" 
5550  C  "C2'" . DT  B 2   ? 0.9602 0.4419 0.3934 -0.0724 0.2069 -0.0309 2   DT  E "C2'" 
5551  C  "C1'" . DT  B 2   ? 0.9566 0.4419 0.3933 -0.0712 0.2052 -0.0309 2   DT  E "C1'" 
5552  N  N1    . DT  B 2   ? 0.9564 0.4448 0.394  -0.0762 0.2055 -0.0316 2   DT  E N1    
5553  C  C2    . DT  B 2   ? 0.9533 0.4506 0.3991 -0.0762 0.203  -0.0314 2   DT  E C2    
5554  O  O2    . DT  B 2   ? 0.9521 0.4541 0.4037 -0.0727 0.2005 -0.0308 2   DT  E O2    
5555  N  N3    . DT  B 2   ? 0.9512 0.4517 0.3977 -0.0806 0.2037 -0.0316 2   DT  E N3    
5556  C  C4    . DT  B 2   ? 0.9533 0.4495 0.3936 -0.0855 0.2062 -0.032  2   DT  E C4    
5557  O  O4    . DT  B 2   ? 0.9505 0.4514 0.393  -0.0892 0.2064 -0.0318 2   DT  E O4    
5558  C  C5    . DT  B 2   ? 0.9578 0.444  0.3893 -0.0857 0.2085 -0.0326 2   DT  E C5    
5559  C  C7    . DT  B 2   ? 0.9614 0.4413 0.3848 -0.0912 0.2113 -0.0332 2   DT  E C7    
5560  C  C6    . DT  B 2   ? 0.9597 0.4423 0.3901 -0.0808 0.2082 -0.0323 2   DT  E C6    
5561  P  P     . DC  B 3   ? 0.9574 0.4423 0.3973 -0.0631 0.2054 -0.0281 3   DC  E P     
5562  O  OP1   . DC  B 3   ? 0.96   0.441  0.3975 -0.0578 0.2065 -0.0263 3   DC  E OP1   
5563  O  OP2   . DC  B 3   ? 0.959  0.4409 0.3943 -0.0687 0.2073 -0.0294 3   DC  E OP2   
5564  O  "O5'" . DC  B 3   ? 0.9461 0.4431 0.3979 -0.0629 0.2014 -0.0278 3   DC  E "O5'" 
5565  C  "C5'" . DC  B 3   ? 0.9382 0.4394 0.3949 -0.0595 0.1988 -0.0271 3   DC  E "C5'" 
5566  C  "C4'" . DC  B 3   ? 0.9281 0.4379 0.3925 -0.0617 0.196  -0.0278 3   DC  E "C4'" 
5567  O  "O4'" . DC  B 3   ? 0.9334 0.4415 0.3945 -0.0656 0.1972 -0.029  3   DC  E "O4'" 
5568  C  "C3'" . DC  B 3   ? 0.9173 0.434  0.3881 -0.0635 0.1949 -0.0278 3   DC  E "C3'" 
5569  O  "O3'" . DC  B 3   ? 0.8988 0.4207 0.3762 -0.06   0.1926 -0.0266 3   DC  E "O3'" 
5570  C  "C2'" . DC  B 3   ? 0.9203 0.4426 0.395  -0.0669 0.1937 -0.0288 3   DC  E "C2'" 
5571  C  "C1'" . DC  B 3   ? 0.9298 0.4461 0.3978 -0.0682 0.1955 -0.0294 3   DC  E "C1'" 
5572  N  N1    . DC  B 3   ? 0.9373 0.4527 0.4021 -0.0733 0.1975 -0.0303 3   DC  E N1    
5573  C  C2    . DC  B 3   ? 0.9361 0.4583 0.4056 -0.0761 0.1965 -0.0305 3   DC  E C2    
5574  O  O2    . DC  B 3   ? 0.9345 0.4625 0.4102 -0.0741 0.1943 -0.03   3   DC  E O2    
5575  N  N3    . DC  B 3   ? 0.9366 0.4588 0.4034 -0.0809 0.1982 -0.0309 3   DC  E N3    
5576  C  C4    . DC  B 3   ? 0.9407 0.4555 0.3999 -0.0833 0.2006 -0.0314 3   DC  E C4    
5577  N  N4    . DC  B 3   ? 0.9398 0.4551 0.3966 -0.0886 0.2019 -0.0317 3   DC  E N4    
5578  C  C5    . DC  B 3   ? 0.9456 0.4521 0.3989 -0.0804 0.2018 -0.0314 3   DC  E C5    
5579  C  C6    . DC  B 3   ? 0.9438 0.4514 0.4006 -0.0753 0.2002 -0.0307 3   DC  E C6    
5580  P  P     . DT  B 4   ? 0.8791 0.4024 0.3587 -0.0588 0.1931 -0.0256 4   DT  E P     
5581  O  OP1   . DT  B 4   ? 0.8748 0.4019 0.3596 -0.0544 0.191  -0.0238 4   DT  E OP1   
5582  O  OP2   . DT  B 4   ? 0.8839 0.3986 0.3548 -0.0597 0.1967 -0.0258 4   DT  E OP2   
5583  O  "O5'" . DT  B 4   ? 0.8607 0.3912 0.3465 -0.0623 0.1919 -0.0265 4   DT  E "O5'" 
5584  C  "C5'" . DT  B 4   ? 0.8426 0.3804 0.3352 -0.0626 0.1891 -0.0267 4   DT  E "C5'" 
5585  C  "C4'" . DT  B 4   ? 0.8269 0.369  0.3218 -0.0667 0.1892 -0.0278 4   DT  E "C4'" 
5586  O  "O4'" . DT  B 4   ? 0.8243 0.3619 0.3129 -0.0698 0.1912 -0.0287 4   DT  E "O4'" 
5587  C  "C3'" . DT  B 4   ? 0.8188 0.3634 0.3157 -0.0683 0.1899 -0.0278 4   DT  E "C3'" 
5588  O  "O3'" . DT  B 4   ? 0.8086 0.3613 0.3125 -0.0695 0.1882 -0.028  4   DT  E "O3'" 
5589  C  "C2'" . DT  B 4   ? 0.8222 0.3614 0.3119 -0.0721 0.1925 -0.0287 4   DT  E "C2'" 
5590  C  "C1'" . DT  B 4   ? 0.8235 0.362  0.3111 -0.0736 0.1925 -0.0293 4   DT  E "C1'" 
5591  N  N1    . DT  B 4   ? 0.8313 0.3622 0.3102 -0.0763 0.1951 -0.0299 4   DT  E N1    
5592  C  C2    . DT  B 4   ? 0.8316 0.3641 0.3092 -0.081  0.1959 -0.0305 4   DT  E C2    
5593  O  O2    . DT  B 4   ? 0.825  0.3654 0.3085 -0.0826 0.1946 -0.0304 4   DT  E O2    
5594  N  N3    . DT  B 4   ? 0.8381 0.3628 0.3071 -0.0838 0.1983 -0.0311 4   DT  E N3    
5595  C  C4    . DT  B 4   ? 0.843  0.3579 0.3041 -0.0821 0.2003 -0.0311 4   DT  E C4    
5596  O  O4    . DT  B 4   ? 0.849  0.3568 0.302  -0.0851 0.2026 -0.0317 4   DT  E O4    
5597  C  C5    . DT  B 4   ? 0.8413 0.3552 0.3044 -0.0766 0.1996 -0.0303 4   DT  E C5    
5598  C  C7    . DT  B 4   ? 0.8471 0.3511 0.3022 -0.0736 0.202  -0.0298 4   DT  E C7    
5599  C  C6    . DT  B 4   ? 0.8366 0.3588 0.3087 -0.0742 0.197  -0.0297 4   DT  E C6    
5600  P  P     . DG  B 5   ? 0.799  0.3563 0.3078 -0.0695 0.1877 -0.0276 5   DG  E P     
5601  O  OP1   . DG  B 5   ? 0.7957 0.3582 0.3115 -0.0665 0.1853 -0.0268 5   DG  E OP1   
5602  O  OP2   . DG  B 5   ? 0.8023 0.3535 0.3057 -0.0693 0.1899 -0.0274 5   DG  E OP2   
5603  O  "O5'" . DG  B 5   ? 0.787  0.3493 0.2976 -0.0736 0.1879 -0.0283 5   DG  E "O5'" 
5604  C  "C5'" . DG  B 5   ? 0.7726 0.3414 0.2884 -0.0738 0.1864 -0.0283 5   DG  E "C5'" 
5605  C  "C4'" . DG  B 5   ? 0.7622 0.3326 0.2761 -0.0776 0.1874 -0.0287 5   DG  E "C4'" 
5606  O  "O4'" . DG  B 5   ? 0.7601 0.3239 0.2672 -0.0785 0.1888 -0.029  5   DG  E "O4'" 
5607  C  "C3'" . DG  B 5   ? 0.7587 0.3314 0.2719 -0.0813 0.1884 -0.0288 5   DG  E "C3'" 
5608  O  "O3'" . DG  B 5   ? 0.7577 0.3384 0.2775 -0.0814 0.1873 -0.0284 5   DG  E "O3'" 
5609  C  "C2'" . DG  B 5   ? 0.7541 0.3262 0.2636 -0.0848 0.1896 -0.0289 5   DG  E "C2'" 
5610  C  "C1'" . DG  B 5   ? 0.7553 0.3195 0.2594 -0.083  0.1902 -0.0293 5   DG  E "C1'" 
5611  N  N9    . DG  B 5   ? 0.7512 0.3074 0.2477 -0.0846 0.192  -0.0298 5   DG  E N9    
5612  C  C8    . DG  B 5   ? 0.7502 0.3002 0.2435 -0.0823 0.1926 -0.0299 5   DG  E C8    
5613  N  N7    . DG  B 5   ? 0.7521 0.2946 0.2374 -0.0846 0.1947 -0.0304 5   DG  E N7    
5614  C  C5    . DG  B 5   ? 0.751  0.2955 0.2347 -0.0893 0.1952 -0.0307 5   DG  E C5    
5615  C  C6    . DG  B 5   ? 0.7538 0.2927 0.2297 -0.094  0.197  -0.0313 5   DG  E C6    
5616  O  O6    . DG  B 5   ? 0.7607 0.2904 0.2285 -0.0948 0.1989 -0.0318 5   DG  E O6    
5617  N  N1    . DG  B 5   ? 0.7498 0.2946 0.2277 -0.0981 0.1967 -0.031  5   DG  E N1    
5618  C  C2    . DG  B 5   ? 0.7433 0.2979 0.2295 -0.0972 0.1952 -0.0302 5   DG  E C2    
5619  N  N2    . DG  B 5   ? 0.7399 0.2996 0.227  -0.1012 0.1954 -0.0296 5   DG  E N2    
5620  N  N3    . DG  B 5   ? 0.7426 0.3011 0.235  -0.0927 0.1937 -0.0299 5   DG  E N3    
5621  C  C4    . DG  B 5   ? 0.7481 0.3015 0.2391 -0.0892 0.1936 -0.0302 5   DG  E C4    
5622  P  P     . DC  B 6   ? 0.7573 0.3406 0.2777 -0.0839 0.1877 -0.0285 6   DC  E P     
5623  O  OP1   . DC  B 6   ? 0.7503 0.342  0.278  -0.0829 0.1865 -0.0279 6   DC  E OP1   
5624  O  OP2   . DC  B 6   ? 0.7602 0.3367 0.2767 -0.0828 0.1885 -0.0288 6   DC  E OP2   
5625  O  "O5'" . DC  B 6   ? 0.7609 0.3443 0.2769 -0.0891 0.1889 -0.0286 6   DC  E "O5'" 
5626  C  "C5'" . DC  B 6   ? 0.7566 0.3464 0.2754 -0.0907 0.1887 -0.0278 6   DC  E "C5'" 
5627  C  "C4'" . DC  B 6   ? 0.7537 0.3429 0.2678 -0.096  0.1898 -0.0277 6   DC  E "C4'" 
5628  O  "O4'" . DC  B 6   ? 0.7556 0.3357 0.2626 -0.0964 0.191  -0.0285 6   DC  E "O4'" 
5629  C  "C3'" . DC  B 6   ? 0.7528 0.3417 0.2643 -0.0998 0.19   -0.028  6   DC  E "C3'" 
5630  O  "O3'" . DC  B 6   ? 0.7509 0.3496 0.2683 -0.101  0.1891 -0.027  6   DC  E "O3'" 
5631  C  "C2'" . DC  B 6   ? 0.7534 0.338  0.2579 -0.1047 0.1912 -0.0282 6   DC  E "C2'" 
5632  C  "C1'" . DC  B 6   ? 0.7573 0.334  0.2581 -0.1016 0.1921 -0.0288 6   DC  E "C1'" 
5633  N  N1    . DC  B 6   ? 0.7634 0.3292 0.2568 -0.1009 0.1932 -0.0299 6   DC  E N1    
5634  C  C2    . DC  B 6   ? 0.7697 0.3281 0.2542 -0.1053 0.1947 -0.0305 6   DC  E C2    
5635  O  O2    . DC  B 6   ? 0.7715 0.3329 0.2549 -0.11   0.1949 -0.0301 6   DC  E O2    
5636  N  N3    . DC  B 6   ? 0.773  0.3209 0.2501 -0.1042 0.1962 -0.0314 6   DC  E N3    
5637  C  C4    . DC  B 6   ? 0.7719 0.3177 0.2509 -0.099  0.196  -0.0313 6   DC  E C4    
5638  N  N4    . DC  B 6   ? 0.7751 0.3107 0.2466 -0.0976 0.1978 -0.0317 6   DC  E N4    
5639  C  C5    . DC  B 6   ? 0.7674 0.3215 0.2561 -0.0949 0.1941 -0.0307 6   DC  E C5    
5640  C  C6    . DC  B 6   ? 0.7628 0.3261 0.2579 -0.0961 0.1928 -0.0301 6   DC  E C6    
5641  P  P     . DA  B 7   ? 0.7557 0.355  0.2723 -0.103  0.1886 -0.0273 7   DA  E P     
5642  O  OP1   . DA  B 7   ? 0.7496 0.3589 0.2741 -0.1017 0.1876 -0.0263 7   DA  E OP1   
5643  O  OP2   . DA  B 7   ? 0.7624 0.3521 0.2745 -0.1007 0.1893 -0.0285 7   DA  E OP2   
5644  O  "O5'" . DA  B 7   ? 0.7606 0.3594 0.2716 -0.1098 0.1891 -0.0271 7   DA  E "O5'" 
5645  C  "C5'" . DA  B 7   ? 0.7677 0.3595 0.2714 -0.1132 0.1895 -0.0281 7   DA  E "C5'" 
5646  C  "C4'" . DA  B 7   ? 0.7742 0.3603 0.2698 -0.1185 0.1905 -0.0284 7   DA  E "C4'" 
5647  O  "O4'" . DA  B 7   ? 0.7769 0.3531 0.2675 -0.1159 0.1919 -0.0294 7   DA  E "O4'" 
5648  C  "C3'" . DA  B 7   ? 0.782  0.3622 0.2696 -0.1237 0.1907 -0.0291 7   DA  E "C3'" 
5649  O  "O3'" . DA  B 7   ? 0.7867 0.3761 0.2768 -0.1289 0.1894 -0.0279 7   DA  E "O3'" 
5650  C  "C2'" . DA  B 7   ? 0.7856 0.3543 0.2632 -0.1261 0.1925 -0.0301 7   DA  E "C2'" 
5651  C  "C1'" . DA  B 7   ? 0.7817 0.3477 0.2617 -0.12   0.1933 -0.0303 7   DA  E "C1'" 
5652  N  N9    . DA  B 7   ? 0.7812 0.3365 0.2562 -0.1158 0.1946 -0.0313 7   DA  E N9    
5653  C  C8    . DA  B 7   ? 0.7787 0.3349 0.2589 -0.1095 0.1943 -0.0312 7   DA  E C8    
5654  N  N7    . DA  B 7   ? 0.7819 0.3279 0.2561 -0.1066 0.1959 -0.0318 7   DA  E N7    
5655  C  C5    . DA  B 7   ? 0.7833 0.3202 0.247  -0.1111 0.1976 -0.0324 7   DA  E C5    
5656  C  C6    . DA  B 7   ? 0.7866 0.3101 0.2396 -0.1106 0.2    -0.0331 7   DA  E C6    
5657  N  N6    . DA  B 7   ? 0.7871 0.3049 0.2389 -0.1048 0.2013 -0.0329 7   DA  E N6    
5658  N  N1    . DA  B 7   ? 0.7919 0.3083 0.2353 -0.1162 0.2014 -0.0337 7   DA  E N1    
5659  C  C2    . DA  B 7   ? 0.79   0.3132 0.2351 -0.1222 0.2    -0.0336 7   DA  E C2    
5660  N  N3    . DA  B 7   ? 0.7834 0.3201 0.2388 -0.123  0.1977 -0.0327 7   DA  E N3    
5661  C  C4    . DA  B 7   ? 0.7825 0.325  0.2466 -0.1171 0.1967 -0.0322 7   DA  E C4    
5662  P  P     . DT  B 8   ? 0.7956 0.3863 0.2836 -0.1324 0.1883 -0.0279 8   DT  E P     
5663  O  OP1   . DT  B 8   ? 0.7871 0.3925 0.2841 -0.1336 0.1866 -0.026  8   DT  E OP1   
5664  O  OP2   . DT  B 8   ? 0.7998 0.3825 0.2855 -0.1279 0.1891 -0.0292 8   DT  E OP2   
5665  O  "O5'" . DT  B 8   ? 0.8092 0.3919 0.286  -0.1401 0.1888 -0.0285 8   DT  E "O5'" 
5666  C  "C5'" . DT  B 8   ? 0.8148 0.3998 0.2905 -0.1444 0.189  -0.0277 8   DT  E "C5'" 
5667  C  "C4'" . DT  B 8   ? 0.8321 0.4031 0.2949 -0.1487 0.1906 -0.0291 8   DT  E "C4'" 
5668  O  "O4'" . DT  B 8   ? 0.8385 0.3975 0.2967 -0.143  0.1926 -0.0307 8   DT  E "O4'" 
5669  C  "C3'" . DT  B 8   ? 0.8451 0.4102 0.2985 -0.1555 0.1901 -0.0297 8   DT  E "C3'" 
5670  O  "O3'" . DT  B 8   ? 0.8607 0.4204 0.3056 -0.1625 0.1907 -0.0299 8   DT  E "O3'" 
5671  C  "C2'" . DT  B 8   ? 0.8482 0.3998 0.2944 -0.1512 0.1918 -0.0315 8   DT  E "C2'" 
5672  C  "C1'" . DT  B 8   ? 0.847  0.3931 0.2935 -0.1456 0.1938 -0.032  8   DT  E "C1'" 
5673  N  N1    . DT  B 8   ? 0.8473 0.3863 0.2933 -0.1383 0.1951 -0.0329 8   DT  E N1    
5674  C  C2    . DT  B 8   ? 0.8551 0.3798 0.2912 -0.1365 0.1977 -0.0339 8   DT  E C2    
5675  O  O2    . DT  B 8   ? 0.8618 0.3787 0.2893 -0.1403 0.1991 -0.0344 8   DT  E O2    
5676  N  N3    . DT  B 8   ? 0.8556 0.3757 0.2925 -0.1296 0.1989 -0.0341 8   DT  E N3    
5677  C  C4    . DT  B 8   ? 0.8488 0.3767 0.295  -0.1249 0.1976 -0.0335 8   DT  E C4    
5678  O  O4    . DT  B 8   ? 0.8497 0.3726 0.2958 -0.1191 0.1988 -0.0335 8   DT  E O4    
5679  C  C5    . DT  B 8   ? 0.8411 0.3831 0.2967 -0.1274 0.1949 -0.0327 8   DT  E C5    
5680  C  C7    . DT  B 8   ? 0.8359 0.3867 0.3015 -0.1228 0.1936 -0.0321 8   DT  E C7    
5681  C  C6    . DT  B 8   ? 0.8403 0.3872 0.2953 -0.1337 0.1939 -0.0323 8   DT  E C6    
5682  P  P     . DT  B 9   ? 0.8772 0.4314 0.3114 -0.1717 0.1898 -0.0302 9   DT  E P     
5683  O  OP1   . DT  B 9   ? 0.8786 0.4386 0.3123 -0.1792 0.1889 -0.0289 9   DT  E OP1   
5684  O  OP2   . DT  B 9   ? 0.8733 0.4329 0.3109 -0.1713 0.1879 -0.0299 9   DT  E OP2   
5685  O  "O5'" . DT  B 9   ? 0.8941 0.4278 0.3135 -0.1711 0.1927 -0.0325 9   DT  E "O5'" 
5686  C  "C5'" . DT  B 9   ? 0.9018 0.4266 0.315  -0.1714 0.1949 -0.0331 9   DT  E "C5'" 
5687  C  "C4'" . DT  B 9   ? 0.9159 0.4215 0.3154 -0.1694 0.198  -0.035  9   DT  E "C4'" 
5688  O  "O4'" . DT  B 9   ? 0.9129 0.4169 0.3168 -0.1604 0.1989 -0.0354 9   DT  E "O4'" 
5689  C  "C3'" . DT  B 9   ? 0.9318 0.4263 0.3176 -0.1762 0.1982 -0.036  9   DT  E "C3'" 
5690  O  "O3'" . DT  B 9   ? 0.9543 0.4319 0.3255 -0.1785 0.2012 -0.0372 9   DT  E "O3'" 
5691  C  "C2'" . DT  B 9   ? 0.928  0.4193 0.3144 -0.1701 0.1986 -0.0364 9   DT  E "C2'" 
5692  C  "C1'" . DT  B 9   ? 0.9213 0.412  0.3139 -0.1606 0.2004 -0.0364 9   DT  E "C1'" 
5693  N  N1    . DT  B 9   ? 0.9164 0.4102 0.3159 -0.153  0.2003 -0.0362 9   DT  E N1    
5694  C  C2    . DT  B 9   ? 0.9203 0.4025 0.3144 -0.1465 0.2032 -0.0367 9   DT  E C2    
5695  O  O2    . DT  B 9   ? 0.926  0.3953 0.3097 -0.1463 0.206  -0.0374 9   DT  E O2    
5696  N  N3    . DT  B 9   ? 0.9188 0.4053 0.3201 -0.1402 0.2028 -0.0363 9   DT  E N3    
5697  C  C4    . DT  B 9   ? 0.912  0.4122 0.3247 -0.1397 0.2    -0.0355 9   DT  E C4    
5698  O  O4    . DT  B 9   ? 0.9096 0.4117 0.3275 -0.1337 0.2002 -0.0352 9   DT  E O4    
5699  C  C5    . DT  B 9   ? 0.9071 0.4186 0.3245 -0.1464 0.1972 -0.0351 9   DT  E C5    
5700  C  C7    . DT  B 9   ? 0.8972 0.424  0.3265 -0.146  0.1943 -0.034  9   DT  E C7    
5701  C  C6    . DT  B 9   ? 0.9098 0.4179 0.3206 -0.1527 0.1974 -0.0353 9   DT  E C6    
5702  P  P     . DC  B 10  ? 0.9753 0.4374 0.3285 -0.1867 0.202  -0.0384 10  DC  E P     
5703  O  OP1   . DC  B 10  ? 0.9803 0.4384 0.3264 -0.1942 0.2026 -0.0385 10  DC  E OP1   
5704  O  OP2   . DC  B 10  ? 0.9713 0.4398 0.3263 -0.1904 0.1992 -0.038  10  DC  E OP2   
5705  O  "O5'" . DC  B 10  ? 0.9928 0.4365 0.3349 -0.18   0.2062 -0.0397 10  DC  E "O5'" 
5706  C  "C5'" . DC  B 10  ? 1.0014 0.4402 0.3443 -0.173  0.209  -0.0398 10  DC  E "C5'" 
5707  C  "C4'" . DC  B 10  ? 1.0158 0.4395 0.3497 -0.166  0.2126 -0.0404 10  DC  E "C4'" 
5708  O  "O4'" . DC  B 10  ? 1.0084 0.4408 0.3534 -0.1588 0.2114 -0.0397 10  DC  E "O4'" 
5709  C  "C3'" . DC  B 10  ? 1.0343 0.44   0.3496 -0.1707 0.2148 -0.0414 10  DC  E "C3'" 
5710  O  "O3'" . DC  B 10  ? 1.0538 0.4423 0.3574 -0.1654 0.2194 -0.0418 10  DC  E "O3'" 
5711  C  "C2'" . DC  B 10  ? 1.0267 0.4372 0.3463 -0.1689 0.2131 -0.0411 10  DC  E "C2'" 
5712  C  "C1'" . DC  B 10  ? 1.0127 0.4349 0.3483 -0.1589 0.2127 -0.04   10  DC  E "C1'" 
5713  N  N1    . DC  B 10  ? 0.9963 0.4323 0.344  -0.1574 0.2095 -0.0394 10  DC  E N1    
5714  C  C2    . DC  B 10  ? 0.9916 0.427  0.3431 -0.1493 0.2107 -0.0388 10  DC  E C2    
5715  O  O2    . DC  B 10  ? 0.9949 0.4184 0.3396 -0.1435 0.2143 -0.0387 10  DC  E O2    
5716  N  N3    . DC  B 10  ? 0.9853 0.4332 0.3479 -0.148  0.2079 -0.0382 10  DC  E N3    
5717  C  C4    . DC  B 10  ? 0.9797 0.4403 0.3491 -0.1541 0.2043 -0.038  10  DC  E C4    
5718  N  N4    . DC  B 10  ? 0.9726 0.445  0.3525 -0.1523 0.2019 -0.0374 10  DC  E N4    
5719  C  C5    . DC  B 10  ? 0.9801 0.4422 0.3459 -0.1624 0.203  -0.0383 10  DC  E C5    
5720  C  C6    . DC  B 10  ? 0.9878 0.4374 0.3429 -0.1638 0.2057 -0.039  10  DC  E C6    
5721  P  P     . DC  B 11  ? 1.079  0.4447 0.3597 -0.1702 0.2229 -0.0429 11  DC  E P     
5722  O  OP1   . DC  B 11  ? 1.0872 0.4396 0.3581 -0.1677 0.2271 -0.0432 11  DC  E OP1   
5723  O  OP2   . DC  B 11  ? 1.081  0.4482 0.3566 -0.1816 0.22   -0.0436 11  DC  E OP2   
5724  O  "O5'" . DC  B 11  ? 1.0904 0.4492 0.368  -0.1633 0.2249 -0.0425 11  DC  E "O5'" 
5725  C  "C5'" . DC  B 11  ? 1.0988 0.4554 0.3802 -0.1523 0.2278 -0.0414 11  DC  E "C5'" 
5726  C  "C4'" . DC  B 11  ? 1.1091 0.4626 0.3898 -0.1468 0.2289 -0.0407 11  DC  E "C4'" 
5727  O  "O4'" . DC  B 11  ? 1.097  0.4688 0.3936 -0.1473 0.2244 -0.0403 11  DC  E "O4'" 
5728  C  "C3'" . DC  B 11  ? 1.13   0.4647 0.391  -0.1513 0.2314 -0.0414 11  DC  E "C3'" 
5729  O  "O3'" . DC  B 11  ? 1.1494 0.4729 0.4042 -0.1425 0.2358 -0.0402 11  DC  E "O3'" 
5730  C  "C2'" . DC  B 11  ? 1.1189 0.465  0.3866 -0.157  0.2269 -0.0418 11  DC  E "C2'" 
5731  C  "C1'" . DC  B 11  ? 1.1004 0.4658 0.3895 -0.1495 0.2245 -0.0405 11  DC  E "C1'" 
5732  N  N1    . DC  B 11  ? 1.0843 0.4669 0.386  -0.1536 0.2194 -0.0406 11  DC  E N1    
5733  C  C2    . DC  B 11  ? 1.0752 0.4652 0.3859 -0.1483 0.2185 -0.0397 11  DC  E C2    
5734  O  O2    . DC  B 11  ? 1.076  0.4587 0.3845 -0.1403 0.2218 -0.0388 11  DC  E O2    
5735  N  N3    . DC  B 11  ? 1.0655 0.471  0.3874 -0.1518 0.2141 -0.0396 11  DC  E N3    
5736  C  C4    . DC  B 11  ? 1.062  0.4758 0.3863 -0.1602 0.2108 -0.0401 11  DC  E C4    
5737  N  N4    . DC  B 11  ? 1.0535 0.4828 0.3888 -0.163  0.2068 -0.0397 11  DC  E N4    
5738  C  C5    . DC  B 11  ? 1.068  0.4745 0.3832 -0.1661 0.2117 -0.0409 11  DC  E C5    
5739  C  C6    . DC  B 11  ? 1.0788 0.4695 0.3828 -0.1626 0.216  -0.0412 11  DC  E C6    
5740  P  P     . DT  B 12  ? 1.1814 0.4791 0.4117 -0.1437 0.241  -0.0406 12  DT  E P     
5741  O  OP1   . DT  B 12  ? 1.1896 0.4749 0.4106 -0.1399 0.2455 -0.0402 12  DT  E OP1   
5742  O  OP2   . DT  B 12  ? 1.185  0.4774 0.4048 -0.155  0.2387 -0.0423 12  DT  E OP2   
5743  O  "O5'" . DT  B 12  ? 1.1995 0.4956 0.432  -0.1347 0.2431 -0.0389 12  DT  E "O5'" 
5744  C  "C5'" . DT  B 12  ? 1.2076 0.5166 0.4568 -0.1247 0.243  -0.0369 12  DT  E "C5'" 
5745  C  "C4'" . DT  B 12  ? 1.2182 0.5346 0.4758 -0.1205 0.2419 -0.0359 12  DT  E "C4'" 
5746  O  "O4'" . DT  B 12  ? 1.213  0.5461 0.483  -0.1267 0.236  -0.037  12  DT  E "O4'" 
5747  C  "C3'" . DT  B 12  ? 1.2412 0.5393 0.4813 -0.1204 0.2456 -0.0356 12  DT  E "C3'" 
5748  O  "O3'" . DT  B 12  ? 1.252  0.5509 0.4972 -0.1103 0.2482 -0.0332 12  DT  E "O3'" 
5749  C  "C2'" . DT  B 12  ? 1.2388 0.5421 0.4792 -0.1295 0.2411 -0.0373 12  DT  E "C2'" 
5750  C  "C1'" . DT  B 12  ? 1.2216 0.5499 0.4854 -0.1293 0.2357 -0.0373 12  DT  E "C1'" 
5751  N  N1    . DT  B 12  ? 1.2206 0.5583 0.4876 -0.1395 0.2306 -0.039  12  DT  E N1    
5752  C  C2    . DT  B 12  ? 1.2129 0.5663 0.4937 -0.1395 0.2267 -0.0387 12  DT  E C2    
5753  O  O2    . DT  B 12  ? 1.2064 0.5672 0.498  -0.1317 0.227  -0.0373 12  DT  E O2    
5754  N  N3    . DT  B 12  ? 1.2115 0.5728 0.494  -0.149  0.2222 -0.0399 12  DT  E N3    
5755  C  C4    . DT  B 12  ? 1.2172 0.5722 0.4888 -0.1588 0.2213 -0.0413 12  DT  E C4    
5756  O  O4    . DT  B 12  ? 1.2152 0.5798 0.4904 -0.1668 0.217  -0.0419 12  DT  E O4    
5757  C  C5    . DT  B 12  ? 1.2242 0.5615 0.4807 -0.1586 0.2256 -0.0417 12  DT  E C5    
5758  C  C7    . DT  B 12  ? 1.2292 0.5578 0.4726 -0.1691 0.2251 -0.0431 12  DT  E C7    
5759  C  C6    . DT  B 12  ? 1.227  0.5563 0.4817 -0.149  0.2301 -0.0405 12  DT  E C6    
5760  P  P     . DC  B 13  ? 1.2795 0.5568 0.5057 -0.1063 0.2541 -0.0319 13  DC  E P     
5761  O  OP1   . DC  B 13  ? 1.2823 0.5578 0.5116 -0.0947 0.2586 -0.0289 13  DC  E OP1   
5762  O  OP2   . DC  B 13  ? 1.294  0.5515 0.4979 -0.1145 0.2562 -0.0339 13  DC  E OP2   
5763  O  "O5'" . DC  B 13  ? 1.2809 0.5651 0.5129 -0.107  0.2516 -0.0319 13  DC  E "O5'" 
5764  C  "C5'" . DC  B 13  ? 1.277  0.5747 0.5255 -0.0985 0.2511 -0.0297 13  DC  E "C5'" 
5765  C  "C4'" . DC  B 13  ? 1.2776 0.5852 0.5337 -0.1019 0.2471 -0.0305 13  DC  E "C4'" 
5766  O  "O4'" . DC  B 13  ? 1.2741 0.595  0.5387 -0.1107 0.2412 -0.0328 13  DC  E "O4'" 
5767  C  "C3'" . DC  B 13  ? 1.2919 0.5824 0.5298 -0.1056 0.2492 -0.0312 13  DC  E "C3'" 
5768  O  "O3'" . DC  B 13  ? 1.2957 0.5783 0.53   -0.0965 0.2539 -0.0286 13  DC  E "O3'" 
5769  C  "C2'" . DC  B 13  ? 1.2858 0.5904 0.5333 -0.1125 0.2432 -0.0328 13  DC  E "C2'" 
5770  C  "C1'" . DC  B 13  ? 1.2768 0.5994 0.5396 -0.1163 0.2385 -0.0339 13  DC  E "C1'" 
5771  N  N1    . DC  B 13  ? 1.2835 0.604  0.5385 -0.1279 0.2353 -0.0364 13  DC  E N1    
5772  C  C2    . DC  B 13  ? 1.2764 0.6107 0.54   -0.1347 0.2299 -0.0375 13  DC  E C2    
5773  O  O2    . DC  B 13  ? 1.2674 0.6145 0.5445 -0.1307 0.2279 -0.0366 13  DC  E O2    
5774  N  N3    . DC  B 13  ? 1.2791 0.6125 0.5361 -0.1453 0.227  -0.0393 13  DC  E N3    
5775  C  C4    . DC  B 13  ? 1.2884 0.6072 0.5305 -0.1495 0.2293 -0.0402 13  DC  E C4    
5776  N  N4    . DC  B 13  ? 1.2896 0.6086 0.5259 -0.1604 0.2262 -0.0417 13  DC  E N4    
5777  C  C5    . DC  B 13  ? 1.2967 0.6005 0.5291 -0.1426 0.2351 -0.0392 13  DC  E C5    
5778  C  C6    . DC  B 13  ? 1.2939 0.5994 0.5333 -0.1319 0.2379 -0.0373 13  DC  E C6    
5779  O  "O5'" . DG  C 1   ? 1.1113 0.5778 0.438  -0.2009 0.1819 -0.0378 1   DG  F "O5'" 
5780  C  "C5'" . DG  C 1   ? 1.1188 0.5688 0.4346 -0.1999 0.1857 -0.039  1   DG  F "C5'" 
5781  C  "C4'" . DG  C 1   ? 1.1176 0.5597 0.4352 -0.1885 0.1902 -0.0393 1   DG  F "C4'" 
5782  O  "O4'" . DG  C 1   ? 1.1283 0.5502 0.4307 -0.188  0.1945 -0.0404 1   DG  F "O4'" 
5783  C  "C3'" . DG  C 1   ? 1.1023 0.5601 0.4396 -0.1801 0.1905 -0.0383 1   DG  F "C3'" 
5784  O  "O3'" . DG  C 1   ? 1.0973 0.5539 0.4396 -0.1707 0.1927 -0.0379 1   DG  F "O3'" 
5785  C  "C2'" . DG  C 1   ? 1.1071 0.5561 0.4398 -0.1791 0.1933 -0.0389 1   DG  F "C2'" 
5786  C  "C1'" . DG  C 1   ? 1.1213 0.5466 0.4336 -0.1796 0.197  -0.04   1   DG  F "C1'" 
5787  N  N9    . DG  C 1   ? 1.1256 0.5371 0.4262 -0.1818 0.1998 -0.0408 1   DG  F N9    
5788  C  C8    . DG  C 1   ? 1.1253 0.5377 0.422  -0.1903 0.1981 -0.0412 1   DG  F C8    
5789  N  N7    . DG  C 1   ? 1.1332 0.5305 0.4185 -0.19   0.2016 -0.042  1   DG  F N7    
5790  C  C5    . DG  C 1   ? 1.1378 0.5237 0.4191 -0.1807 0.206  -0.0419 1   DG  F C5    
5791  C  C6    . DG  C 1   ? 1.1473 0.5153 0.4168 -0.1759 0.2112 -0.0422 1   DG  F C6    
5792  O  O6    . DG  C 1   ? 1.1534 0.511  0.413  -0.179  0.2132 -0.0429 1   DG  F O6    
5793  N  N1    . DG  C 1   ? 1.1479 0.5103 0.4179 -0.1663 0.2145 -0.0414 1   DG  F N1    
5794  C  C2    . DG  C 1   ? 1.1397 0.5124 0.4203 -0.1621 0.2129 -0.0406 1   DG  F C2    
5795  N  N2    . DG  C 1   ? 1.1422 0.508  0.422  -0.1529 0.2166 -0.0396 1   DG  F N2    
5796  N  N3    . DG  C 1   ? 1.1313 0.5201 0.4224 -0.1666 0.208  -0.0405 1   DG  F N3    
5797  C  C4    . DG  C 1   ? 1.1314 0.5262 0.4224 -0.1757 0.2048 -0.0411 1   DG  F C4    
5798  P  P     . DA  C 2   ? 1.0803 0.5557 0.4439 -0.1626 0.1918 -0.0367 2   DA  F P     
5799  O  OP1   . DA  C 2   ? 1.0816 0.5635 0.45   -0.1608 0.1903 -0.0361 2   DA  F OP1   
5800  O  OP2   . DA  C 2   ? 1.0714 0.5611 0.4457 -0.1656 0.1894 -0.0362 2   DA  F OP2   
5801  O  "O5'" . DA  C 2   ? 1.0681 0.5338 0.4315 -0.153  0.1964 -0.0367 2   DA  F "O5'" 
5802  C  "C5'" . DA  C 2   ? 1.0569 0.5111 0.414  -0.1472 0.1995 -0.0366 2   DA  F "C5'" 
5803  C  "C4'" . DA  C 2   ? 1.0429 0.4866 0.3973 -0.1397 0.204  -0.0363 2   DA  F "C4'" 
5804  O  "O4'" . DA  C 2   ? 1.0468 0.4786 0.3889 -0.144  0.2056 -0.0372 2   DA  F "O4'" 
5805  C  "C3'" . DA  C 2   ? 1.0191 0.4759 0.3908 -0.1322 0.204  -0.0353 2   DA  F "C3'" 
5806  O  "O3'" . DA  C 2   ? 1.0086 0.4572 0.3792 -0.1236 0.208  -0.0344 2   DA  F "O3'" 
5807  C  "C2'" . DA  C 2   ? 1.0205 0.4784 0.3919 -0.1357 0.2035 -0.0358 2   DA  F "C2'" 
5808  C  "C1'" . DA  C 2   ? 1.0368 0.4744 0.3879 -0.14   0.2062 -0.0368 2   DA  F "C1'" 
5809  N  N9    . DA  C 2   ? 1.0358 0.4721 0.3815 -0.1475 0.205  -0.0376 2   DA  F N9    
5810  C  C8    . DA  C 2   ? 1.0287 0.476  0.3785 -0.1555 0.2009 -0.0379 2   DA  F C8    
5811  N  N7    . DA  C 2   ? 1.0304 0.473  0.373  -0.1614 0.2009 -0.0386 2   DA  F N7    
5812  C  C5    . DA  C 2   ? 1.0391 0.4659 0.372  -0.1568 0.2054 -0.0389 2   DA  F C5    
5813  C  C6    . DA  C 2   ? 1.0454 0.4601 0.3673 -0.1592 0.2078 -0.0396 2   DA  F C6    
5814  N  N6    . DA  C 2   ? 1.0453 0.462  0.3643 -0.1675 0.2058 -0.0402 2   DA  F N6    
5815  N  N1    . DA  C 2   ? 1.0521 0.4527 0.3662 -0.1526 0.2124 -0.0394 2   DA  F N1    
5816  C  C2    . DA  C 2   ? 1.0533 0.4524 0.3706 -0.1444 0.2144 -0.0384 2   DA  F C2    
5817  N  N3    . DA  C 2   ? 1.0481 0.4578 0.3757 -0.1416 0.2125 -0.0378 2   DA  F N3    
5818  C  C4    . DA  C 2   ? 1.0417 0.4648 0.3765 -0.1482 0.2079 -0.0382 2   DA  F C4    
5819  P  P     . DG  C 3   ? 0.9881 0.4499 0.3764 -0.1148 0.2079 -0.0329 3   DG  F P     
5820  O  OP1   . DG  C 3   ? 0.9907 0.4436 0.3752 -0.1082 0.2113 -0.0318 3   DG  F OP1   
5821  O  OP2   . DG  C 3   ? 0.9793 0.4589 0.381  -0.1173 0.2036 -0.033  3   DG  F OP2   
5822  O  "O5'" . DG  C 3   ? 0.9742 0.4369 0.3666 -0.1118 0.209  -0.0326 3   DG  F "O5'" 
5823  C  "C5'" . DG  C 3   ? 0.9673 0.4154 0.3496 -0.1079 0.2132 -0.0321 3   DG  F "C5'" 
5824  C  "C4'" . DG  C 3   ? 0.9504 0.3986 0.3333 -0.1085 0.2134 -0.0324 3   DG  F "C4'" 
5825  O  "O4'" . DG  C 3   ? 0.9519 0.3959 0.3255 -0.1174 0.212  -0.034  3   DG  F "O4'" 
5826  C  "C3'" . DG  C 3   ? 0.9237 0.389  0.3242 -0.1059 0.2106 -0.0319 3   DG  F "C3'" 
5827  O  "O3'" . DG  C 3   ? 0.908  0.3701 0.3096 -0.1003 0.2129 -0.031  3   DG  F "O3'" 
5828  C  "C2'" . DG  C 3   ? 0.9243 0.3957 0.325  -0.114  0.2075 -0.0333 3   DG  F "C2'" 
5829  C  "C1'" . DG  C 3   ? 0.9395 0.3938 0.3221 -0.1187 0.2099 -0.0342 3   DG  F "C1'" 
5830  N  N9    . DG  C 3   ? 0.939  0.395  0.3171 -0.1279 0.2074 -0.0354 3   DG  F N9    
5831  C  C8    . DG  C 3   ? 0.9324 0.402  0.3186 -0.1329 0.2034 -0.0356 3   DG  F C8    
5832  N  N7    . DG  C 3   ? 0.9329 0.4029 0.3144 -0.1408 0.2018 -0.0364 3   DG  F N7    
5833  C  C5    . DG  C 3   ? 0.9399 0.3955 0.3097 -0.1409 0.2049 -0.0369 3   DG  F C5    
5834  C  C6    . DG  C 3   ? 0.9422 0.3913 0.3025 -0.1478 0.205  -0.0378 3   DG  F C6    
5835  O  O6    . DG  C 3   ? 0.9366 0.3923 0.2976 -0.1556 0.2022 -0.0381 3   DG  F O6    
5836  N  N1    . DG  C 3   ? 0.9514 0.3851 0.301  -0.1448 0.209  -0.038  3   DG  F N1    
5837  C  C2    . DG  C 3   ? 0.9555 0.3819 0.304  -0.136  0.2125 -0.0373 3   DG  F C2    
5838  N  N2    . DG  C 3   ? 0.9637 0.3755 0.301  -0.134  0.2163 -0.0373 3   DG  F N2    
5839  N  N3    . DG  C 3   ? 0.9518 0.3848 0.3096 -0.1298 0.2122 -0.0363 3   DG  F N3    
5840  C  C4    . DG  C 3   ? 0.9443 0.3914 0.3122 -0.1327 0.2084 -0.0363 3   DG  F C4    
5841  P  P     . DG  C 4   ? 0.8832 0.3594 0.3019 -0.0942 0.2114 -0.0298 4   DG  F P     
5842  O  OP1   . DG  C 4   ? 0.8795 0.3585 0.3041 -0.0883 0.2122 -0.0284 4   DG  F OP1   
5843  O  OP2   . DG  C 4   ? 0.8758 0.3653 0.3039 -0.0985 0.2075 -0.0308 4   DG  F OP2   
5844  O  "O5'" . DG  C 4   ? 0.8762 0.3449 0.2909 -0.0901 0.2141 -0.029  4   DG  F "O5'" 
5845  C  "C5'" . DG  C 4   ? 0.876  0.33   0.2791 -0.0863 0.2184 -0.0279 4   DG  F "C5'" 
5846  C  "C4'" . DG  C 4   ? 0.8746 0.3159 0.2642 -0.0895 0.2206 -0.0288 4   DG  F "C4'" 
5847  O  "O4'" . DG  C 4   ? 0.8745 0.3139 0.2573 -0.0984 0.2187 -0.0309 4   DG  F "O4'" 
5848  C  "C3'" . DG  C 4   ? 0.8638 0.309  0.2584 -0.0874 0.2203 -0.0285 4   DG  F "C3'" 
5849  O  "O3'" . DG  C 4   ? 0.8678 0.2979 0.2493 -0.0852 0.2245 -0.0279 4   DG  F "O3'" 
5850  C  "C2'" . DG  C 4   ? 0.8599 0.3114 0.2563 -0.0952 0.217  -0.0305 4   DG  F "C2'" 
5851  C  "C1'" . DG  C 4   ? 0.8699 0.3109 0.2527 -0.1016 0.2178 -0.0318 4   DG  F "C1'" 
5852  N  N9    . DG  C 4   ? 0.8641 0.3133 0.2498 -0.1095 0.2141 -0.0333 4   DG  F N9    
5853  C  C8    . DG  C 4   ? 0.8533 0.3167 0.2505 -0.1111 0.2106 -0.0334 4   DG  F C8    
5854  N  N7    . DG  C 4   ? 0.8505 0.3197 0.2483 -0.1184 0.2079 -0.0344 4   DG  F N7    
5855  C  C5    . DG  C 4   ? 0.8603 0.3185 0.2465 -0.122  0.2096 -0.0352 4   DG  F C5    
5856  C  C6    . DG  C 4   ? 0.8654 0.3237 0.2468 -0.1302 0.2082 -0.0362 4   DG  F C6    
5857  O  O6    . DG  C 4   ? 0.8608 0.3303 0.2484 -0.1357 0.2048 -0.0364 4   DG  F O6    
5858  N  N1    . DG  C 4   ? 0.8771 0.3213 0.2457 -0.1316 0.2111 -0.0367 4   DG  F N1    
5859  C  C2    . DG  C 4   ? 0.8849 0.3161 0.2457 -0.1255 0.2151 -0.0362 4   DG  F C2    
5860  N  N2    . DG  C 4   ? 0.8931 0.3111 0.2411 -0.1277 0.2178 -0.0368 4   DG  F N2    
5861  N  N3    . DG  C 4   ? 0.8827 0.3144 0.2483 -0.1176 0.2165 -0.035  4   DG  F N3    
5862  C  C4    . DG  C 4   ? 0.8693 0.3147 0.2476 -0.1166 0.2136 -0.0346 4   DG  F C4    
5863  P  P     . DA  C 5   ? 0.8617 0.2917 0.2447 -0.082  0.2253 -0.0273 5   DA  F P     
5864  O  OP1   . DA  C 5   ? 0.8671 0.2852 0.2418 -0.0753 0.2301 -0.0251 5   DA  F OP1   
5865  O  OP2   . DA  C 5   ? 0.8503 0.2974 0.2504 -0.0805 0.2214 -0.0271 5   DA  F OP2   
5866  O  "O5'" . DA  C 5   ? 0.8702 0.2928 0.2425 -0.0899 0.2252 -0.0295 5   DA  F "O5'" 
5867  C  "C5'" . DA  C 5   ? 0.8816 0.2868 0.2358 -0.0933 0.2286 -0.0302 5   DA  F "C5'" 
5868  C  "C4'" . DA  C 5   ? 0.8865 0.2858 0.2322 -0.0998 0.2286 -0.0319 5   DA  F "C4'" 
5869  O  "O4'" . DA  C 5   ? 0.8763 0.2873 0.2293 -0.1071 0.2241 -0.0335 5   DA  F "O4'" 
5870  C  "C3'" . DA  C 5   ? 0.8924 0.2922 0.2404 -0.096  0.2295 -0.0313 5   DA  F "C3'" 
5871  O  "O3'" . DA  C 5   ? 0.9141 0.299  0.2464 -0.1    0.2324 -0.0324 5   DA  F "O3'" 
5872  C  "C2'" . DA  C 5   ? 0.8757 0.2933 0.2394 -0.0987 0.2247 -0.0321 5   DA  F "C2'" 
5873  C  "C1'" . DA  C 5   ? 0.8695 0.29   0.2315 -0.1072 0.2221 -0.0337 5   DA  F "C1'" 
5874  N  N9    . DA  C 5   ? 0.8503 0.2888 0.2283 -0.1083 0.2177 -0.0338 5   DA  F N9    
5875  C  C8    . DA  C 5   ? 0.8372 0.2865 0.228  -0.1028 0.2161 -0.0327 5   DA  F C8    
5876  N  N7    . DA  C 5   ? 0.8261 0.2898 0.2284 -0.1056 0.2123 -0.0331 5   DA  F N7    
5877  C  C5    . DA  C 5   ? 0.8292 0.2921 0.2264 -0.1133 0.2112 -0.0344 5   DA  F C5    
5878  C  C6    . DA  C 5   ? 0.8227 0.2975 0.227  -0.1191 0.2078 -0.0349 5   DA  F C6    
5879  N  N6    . DA  C 5   ? 0.8131 0.3026 0.231  -0.1176 0.2049 -0.0344 5   DA  F N6    
5880  N  N1    . DA  C 5   ? 0.8282 0.2993 0.2249 -0.1264 0.2076 -0.0358 5   DA  F N1    
5881  C  C2    . DA  C 5   ? 0.84   0.2955 0.2223 -0.128  0.2107 -0.0364 5   DA  F C2    
5882  N  N3    . DA  C 5   ? 0.8482 0.2908 0.2221 -0.1227 0.2143 -0.0361 5   DA  F N3    
5883  C  C4    . DA  C 5   ? 0.8432 0.2908 0.2256 -0.1153 0.2144 -0.0349 5   DA  F C4    
5884  P  P     . DA  C 6   ? 0.9226 0.3028 0.2522 -0.0962 0.2347 -0.0317 6   DA  F P     
5885  O  OP1   . DA  C 6   ? 0.9352 0.2948 0.245  -0.0966 0.2398 -0.0318 6   DA  F OP1   
5886  O  OP2   . DA  C 6   ? 0.914  0.3048 0.2572 -0.0876 0.234  -0.0297 6   DA  F OP2   
5887  O  "O5'" . DA  C 6   ? 0.9253 0.314  0.2599 -0.1033 0.2312 -0.0336 6   DA  F "O5'" 
5888  C  "C5'" . DA  C 6   ? 0.9353 0.3191 0.2611 -0.1129 0.2304 -0.0355 6   DA  F "C5'" 
5889  C  "C4'" . DA  C 6   ? 0.9331 0.3308 0.2694 -0.1182 0.2263 -0.0365 6   DA  F "C4'" 
5890  O  "O4'" . DA  C 6   ? 0.9226 0.337  0.2743 -0.1177 0.2223 -0.0361 6   DA  F "O4'" 
5891  C  "C3'" . DA  C 6   ? 0.9348 0.337  0.2773 -0.1145 0.2263 -0.0361 6   DA  F "C3'" 
5892  O  "O3'" . DA  C 6   ? 0.949  0.3425 0.2811 -0.12   0.2277 -0.0372 6   DA  F "O3'" 
5893  C  "C2'" . DA  C 6   ? 0.9187 0.3408 0.2795 -0.1145 0.2216 -0.0359 6   DA  F "C2'" 
5894  C  "C1'" . DA  C 6   ? 0.9128 0.3403 0.276  -0.1191 0.2193 -0.0363 6   DA  F "C1'" 
5895  N  N9    . DA  C 6   ? 0.8954 0.3391 0.2749 -0.1157 0.216  -0.0355 6   DA  F N9    
5896  C  C8    . DA  C 6   ? 0.8882 0.3355 0.2752 -0.1078 0.2163 -0.0342 6   DA  F C8    
5897  N  N7    . DA  C 6   ? 0.8766 0.339  0.278  -0.1064 0.213  -0.0338 6   DA  F N7    
5898  C  C5    . DA  C 6   ? 0.8732 0.3425 0.277  -0.1134 0.2105 -0.0348 6   DA  F C5    
5899  C  C6    . DA  C 6   ? 0.86   0.3448 0.2763 -0.1154 0.207  -0.0346 6   DA  F C6    
5900  N  N6    . DA  C 6   ? 0.8483 0.3439 0.2769 -0.1106 0.2051 -0.0338 6   DA  F N6    
5901  N  N1    . DA  C 6   ? 0.8606 0.3492 0.2758 -0.1225 0.2055 -0.0352 6   DA  F N1    
5902  C  C2    . DA  C 6   ? 0.8714 0.349  0.2741 -0.1278 0.2073 -0.036  6   DA  F C2    
5903  N  N3    . DA  C 6   ? 0.883  0.3449 0.2726 -0.1269 0.2107 -0.0365 6   DA  F N3    
5904  C  C4    . DA  C 6   ? 0.8843 0.3428 0.2752 -0.1192 0.2123 -0.0357 6   DA  F C4    
5905  P  P     . DT  C 7   ? 0.955  0.3489 0.2892 -0.1167 0.2287 -0.0369 7   DT  F P     
5906  O  OP1   . DT  C 7   ? 0.9646 0.3419 0.2819 -0.1205 0.2323 -0.0378 7   DT  F OP1   
5907  O  OP2   . DT  C 7   ? 0.9524 0.3509 0.2951 -0.107  0.2291 -0.0353 7   DT  F OP2   
5908  O  "O5'" . DT  C 7   ? 0.9524 0.3627 0.2996 -0.1216 0.2243 -0.0375 7   DT  F "O5'" 
5909  C  "C5'" . DT  C 7   ? 0.9618 0.3724 0.3047 -0.1311 0.223  -0.0386 7   DT  F "C5'" 
5910  C  "C4'" . DT  C 7   ? 0.9586 0.3878 0.3166 -0.134  0.2186 -0.0383 7   DT  F "C4'" 
5911  O  "O4'" . DT  C 7   ? 0.9514 0.391  0.3201 -0.1308 0.2162 -0.0377 7   DT  F "O4'" 
5912  C  "C3'" . DT  C 7   ? 0.9611 0.3994 0.3293 -0.1304 0.2176 -0.0378 7   DT  F "C3'" 
5913  O  "O3'" . DT  C 7   ? 0.979  0.4124 0.3407 -0.1351 0.2188 -0.0383 7   DT  F "O3'" 
5914  C  "C2'" . DT  C 7   ? 0.9457 0.4019 0.3288 -0.1318 0.2135 -0.0372 7   DT  F "C2'" 
5915  C  "C1'" . DT  C 7   ? 0.94   0.3963 0.3232 -0.1312 0.2128 -0.0372 7   DT  F "C1'" 
5916  N  N1    . DT  C 7   ? 0.9286 0.3939 0.3237 -0.1238 0.2114 -0.0363 7   DT  F N1    
5917  C  C2    . DT  C 7   ? 0.9169 0.398  0.3256 -0.1239 0.2081 -0.0357 7   DT  F C2    
5918  O  O2    . DT  C 7   ? 0.913  0.4015 0.3246 -0.1299 0.2063 -0.0357 7   DT  F O2    
5919  N  N3    . DT  C 7   ? 0.9105 0.3983 0.3291 -0.117  0.2071 -0.0349 7   DT  F N3    
5920  C  C4    . DT  C 7   ? 0.9128 0.3944 0.3298 -0.1102 0.2088 -0.0345 7   DT  F C4    
5921  O  O4    . DT  C 7   ? 0.9048 0.3941 0.3316 -0.1049 0.2074 -0.0337 7   DT  F O4    
5922  C  C5    . DT  C 7   ? 0.9249 0.3908 0.328  -0.1099 0.2124 -0.0348 7   DT  F C5    
5923  C  C7    . DT  C 7   ? 0.9294 0.3881 0.3299 -0.1024 0.2147 -0.0338 7   DT  F C7    
5924  C  C6    . DT  C 7   ? 0.9308 0.389  0.3235 -0.1166 0.2136 -0.0358 7   DT  F C6    
5925  P  P     . DG  C 8   ? 0.9909 0.4269 0.3574 -0.1306 0.2192 -0.0379 8   DG  F P     
5926  O  OP1   . DG  C 8   ? 1.0015 0.4258 0.3557 -0.135  0.222  -0.0386 8   DG  F OP1   
5927  O  OP2   . DG  C 8   ? 0.9912 0.4272 0.3623 -0.1213 0.2198 -0.0372 8   DG  F OP2   
5928  O  "O5'" . DG  C 8   ? 0.9842 0.4383 0.3655 -0.1328 0.2155 -0.0373 8   DG  F "O5'" 
5929  C  "C5'" . DG  C 8   ? 0.9887 0.4488 0.3706 -0.1413 0.2138 -0.0372 8   DG  F "C5'" 
5930  C  "C4'" . DG  C 8   ? 0.9866 0.4648 0.384  -0.1409 0.2104 -0.0361 8   DG  F "C4'" 
5931  O  "O4'" . DG  C 8   ? 0.9826 0.467  0.3881 -0.1355 0.2088 -0.0358 8   DG  F "O4'" 
5932  C  "C3'" . DG  C 8   ? 0.9921 0.4761 0.3965 -0.1373 0.2103 -0.0354 8   DG  F "C3'" 
5933  O  "O3'" . DG  C 8   ? 0.999  0.4943 0.4098 -0.1425 0.2086 -0.0344 8   DG  F "O3'" 
5934  C  "C2'" . DG  C 8   ? 0.9819 0.4726 0.3964 -0.1292 0.2089 -0.035  8   DG  F "C2'" 
5935  C  "C1'" . DG  C 8   ? 0.9749 0.4705 0.3927 -0.1306 0.2071 -0.0349 8   DG  F "C1'" 
5936  N  N9    . DG  C 8   ? 0.9681 0.4649 0.391  -0.1234 0.2066 -0.0348 8   DG  F N9    
5937  C  C8    . DG  C 8   ? 0.9716 0.4581 0.3888 -0.1181 0.2086 -0.0351 8   DG  F C8    
5938  N  N7    . DG  C 8   ? 0.9665 0.458  0.3913 -0.1121 0.2075 -0.0345 8   DG  F N7    
5939  C  C5    . DG  C 8   ? 0.9579 0.4632 0.3938 -0.1134 0.2046 -0.034  8   DG  F C5    
5940  C  C6    . DG  C 8   ? 0.9469 0.4621 0.3938 -0.109  0.2025 -0.0333 8   DG  F C6    
5941  O  O6    . DG  C 8   ? 0.9435 0.4577 0.393  -0.1034 0.2024 -0.033  8   DG  F O6    
5942  N  N1    . DG  C 8   ? 0.939  0.4662 0.3942 -0.1119 0.2003 -0.0328 8   DG  F N1    
5943  C  C2    . DG  C 8   ? 0.9393 0.4696 0.393  -0.1181 0.2002 -0.0326 8   DG  F C2    
5944  N  N2    . DG  C 8   ? 0.9297 0.4726 0.3924 -0.1196 0.1982 -0.0316 8   DG  F N2    
5945  N  N3    . DG  C 8   ? 0.9493 0.4711 0.3933 -0.1226 0.2019 -0.0332 8   DG  F N3    
5946  C  C4    . DG  C 8   ? 0.9584 0.4673 0.3934 -0.12   0.2042 -0.034  8   DG  F C4    
5947  P  P     . DC  C 9   ? 1.0071 0.5076 0.4233 -0.1406 0.2089 -0.0335 9   DC  F P     
5948  O  OP1   . DC  C 9   ? 1.0066 0.5104 0.421  -0.1486 0.2089 -0.0327 9   DC  F OP1   
5949  O  OP2   . DC  C 9   ? 1.0107 0.5004 0.4215 -0.1347 0.2111 -0.0344 9   DC  F OP2   
5950  O  "O5'" . DC  C 9   ? 1.0123 0.5276 0.443  -0.136  0.2062 -0.0323 9   DC  F "O5'" 
5951  C  "C5'" . DC  C 9   ? 1.02   0.548  0.4582 -0.1399 0.204  -0.0311 9   DC  F "C5'" 
5952  C  "C4'" . DC  C 9   ? 1.026  0.5659 0.4767 -0.1343 0.2022 -0.03   9   DC  F "C4'" 
5953  O  "O4'" . DC  C 9   ? 1.0288 0.566  0.481  -0.1286 0.2017 -0.0309 9   DC  F "O4'" 
5954  C  "C3'" . DC  C 9   ? 1.0366 0.5784 0.491  -0.1303 0.2029 -0.0293 9   DC  F "C3'" 
5955  O  "O3'" . DC  C 9   ? 1.0461 0.6014 0.5106 -0.1299 0.2016 -0.0274 9   DC  F "O3'" 
5956  C  "C2'" . DC  C 9   ? 1.0345 0.5704 0.489  -0.1227 0.203  -0.0304 9   DC  F "C2'" 
5957  C  "C1'" . DC  C 9   ? 1.0293 0.5679 0.4866 -0.1219 0.2015 -0.0307 9   DC  F "C1'" 
5958  N  N1    . DC  C 9   ? 1.033  0.5629 0.4868 -0.1167 0.2021 -0.0318 9   DC  F N1    
5959  C  C2    . DC  C 9   ? 1.0276 0.5624 0.4888 -0.1111 0.2005 -0.0316 9   DC  F C2    
5960  O  O2    . DC  C 9   ? 1.0201 0.5656 0.4901 -0.1106 0.1988 -0.0307 9   DC  F O2    
5961  N  N3    . DC  C 9   ? 1.0316 0.5592 0.49   -0.1065 0.201  -0.0322 9   DC  F N3    
5962  C  C4    . DC  C 9   ? 1.0393 0.555  0.4876 -0.1068 0.2033 -0.033  9   DC  F C4    
5963  N  N4    . DC  C 9   ? 1.042  0.5517 0.4882 -0.1017 0.2039 -0.0331 9   DC  F N4    
5964  C  C5    . DC  C 9   ? 1.0446 0.554  0.4843 -0.1124 0.2051 -0.0334 9   DC  F C5    
5965  C  C6    . DC  C 9   ? 1.0413 0.5583 0.4843 -0.1174 0.2043 -0.0329 9   DC  F C6    
5966  P  P     . DA  C 10  ? 1.0614 0.6207 0.5289 -0.1289 0.2026 -0.0259 10  DA  F P     
5967  O  OP1   . DA  C 10  ? 1.0608 0.6274 0.5293 -0.1358 0.2027 -0.0241 10  DA  F OP1   
5968  O  OP2   . DA  C 10  ? 1.0694 0.6169 0.5299 -0.1257 0.2043 -0.0273 10  DA  F OP2   
5969  O  "O5'" . DA  C 10  ? 1.063  0.6318 0.5408 -0.1229 0.2012 -0.0248 10  DA  F "O5'" 
5970  C  "C5'" . DA  C 10  ? 1.0713 0.6395 0.5518 -0.1184 0.1998 -0.0259 10  DA  F "C5'" 
5971  C  "C4'" . DA  C 10  ? 1.0783 0.65   0.5649 -0.1119 0.1992 -0.0253 10  DA  F "C4'" 
5972  O  "O4'" . DA  C 10  ? 1.0802 0.6451 0.5653 -0.1071 0.1985 -0.0269 10  DA  F "O4'" 
5973  C  "C3'" . DA  C 10  ? 1.0923 0.6617 0.5775 -0.1101 0.2006 -0.0247 10  DA  F "C3'" 
5974  O  "O3'" . DA  C 10  ? 1.1077 0.683  0.5994 -0.1054 0.1999 -0.0236 10  DA  F "O3'" 
5975  C  "C2'" . DA  C 10  ? 1.0921 0.649  0.5699 -0.1075 0.2012 -0.0267 10  DA  F "C2'" 
5976  C  "C1'" . DA  C 10  ? 1.0847 0.6414 0.5651 -0.1041 0.1995 -0.0276 10  DA  F "C1'" 
5977  N  N9    . DA  C 10  ? 1.0858 0.6322 0.5592 -0.1037 0.2001 -0.0292 10  DA  F N9    
5978  C  C8    . DA  C 10  ? 1.0899 0.6279 0.5547 -0.1073 0.202  -0.0299 10  DA  F C8    
5979  N  N7    . DA  C 10  ? 1.0944 0.6238 0.5537 -0.1054 0.2025 -0.0311 10  DA  F N7    
5980  C  C5    . DA  C 10  ? 1.0908 0.6239 0.5562 -0.1004 0.2007 -0.031  10  DA  F C5    
5981  C  C6    . DA  C 10  ? 1.0912 0.6199 0.5558 -0.0963 0.2003 -0.0314 10  DA  F C6    
5982  N  N6    . DA  C 10  ? 1.0961 0.6148 0.5525 -0.0961 0.2021 -0.0321 10  DA  F N6    
5983  N  N1    . DA  C 10  ? 1.0863 0.6213 0.5586 -0.0923 0.1982 -0.031  10  DA  F N1    
5984  C  C2    . DA  C 10  ? 1.0807 0.6247 0.5602 -0.0923 0.1968 -0.0303 10  DA  F C2    
5985  N  N3    . DA  C 10  ? 1.0797 0.6284 0.5606 -0.0955 0.1973 -0.0296 10  DA  F N3    
5986  C  C4    . DA  C 10  ? 1.0851 0.6284 0.559  -0.0995 0.1992 -0.03   10  DA  F C4    
5987  P  P     . DG  C 11  ? 1.1248 0.7037 0.6182 -0.1045 0.2014 -0.0217 11  DG  F P     
5988  O  OP1   . DG  C 11  ? 1.1191 0.7104 0.6195 -0.1063 0.2012 -0.0193 11  DG  F OP1   
5989  O  OP2   . DG  C 11  ? 1.1282 0.6996 0.6145 -0.1071 0.2032 -0.0221 11  DG  F OP2   
5990  O  "O5'" . DG  C 11  ? 1.1425 0.718  0.637  -0.0977 0.2007 -0.0222 11  DG  F "O5'" 
5991  C  "C5'" . DG  C 11  ? 1.1542 0.7351 0.6546 -0.0944 0.1991 -0.0219 11  DG  F "C5'" 
5992  C  "C4'" . DG  C 11  ? 1.1723 0.7465 0.6712 -0.0891 0.1979 -0.0233 11  DG  F "C4'" 
5993  O  "O4'" . DG  C 11  ? 1.1791 0.7456 0.6735 -0.0893 0.1973 -0.0252 11  DG  F "O4'" 
5994  C  "C3'" . DG  C 11  ? 1.187  0.7561 0.6827 -0.0861 0.1989 -0.023  11  DG  F "C3'" 
5995  O  "O3'" . DG  C 11  ? 1.2022 0.7704 0.6997 -0.0814 0.1973 -0.0232 11  DG  F "O3'" 
5996  C  "C2'" . DG  C 11  ? 1.1885 0.7478 0.677  -0.0868 0.1994 -0.0245 11  DG  F "C2'" 
5997  C  "C1'" . DG  C 11  ? 1.1857 0.7435 0.6745 -0.0871 0.1979 -0.026  11  DG  F "C1'" 
5998  N  N9    . DG  C 11  ? 1.1899 0.7409 0.6725 -0.0899 0.199  -0.0271 11  DG  F N9    
5999  C  C8    . DG  C 11  ? 1.1912 0.7404 0.6695 -0.0942 0.201  -0.0268 11  DG  F C8    
6000  N  N7    . DG  C 11  ? 1.1958 0.7376 0.668  -0.096  0.2018 -0.028  11  DG  F N7    
6001  C  C5    . DG  C 11  ? 1.198  0.7371 0.6707 -0.0925 0.2003 -0.0289 11  DG  F C5    
6002  C  C6    . DG  C 11  ? 1.2043 0.7358 0.6718 -0.0919 0.2007 -0.03   11  DG  F C6    
6003  O  O6    . DG  C 11  ? 1.2103 0.7347 0.6706 -0.0947 0.2025 -0.0307 11  DG  F O6    
6004  N  N1    . DG  C 11  ? 1.2026 0.735  0.6737 -0.0877 0.1988 -0.0302 11  DG  F N1    
6005  C  C2    . DG  C 11  ? 1.1979 0.7372 0.6763 -0.0848 0.1968 -0.0297 11  DG  F C2    
6006  N  N2    . DG  C 11  ? 1.1971 0.7365 0.6781 -0.0814 0.1951 -0.0298 11  DG  F N2    
6007  N  N3    . DG  C 11  ? 1.1941 0.7394 0.6765 -0.0852 0.1965 -0.0288 11  DG  F N3    
6008  C  C4    . DG  C 11  ? 1.194  0.7392 0.6735 -0.0889 0.1984 -0.0284 11  DG  F C4    
6009  P  P     . DA  C 12  ? 1.2187 0.7836 0.7141 -0.0777 0.1981 -0.0224 12  DA  F P     
6010  O  OP1   . DA  C 12  ? 1.2163 0.788  0.7165 -0.0759 0.1982 -0.0208 12  DA  F OP1   
6011  O  OP2   . DA  C 12  ? 1.2222 0.7831 0.7127 -0.0792 0.2003 -0.022  12  DA  F OP2   
6012  O  "O5'" . DA  C 12  ? 1.2288 0.7861 0.7213 -0.0742 0.1959 -0.0241 12  DA  F "O5'" 
6013  C  "C5'" . DA  C 12  ? 1.2312 0.7896 0.7265 -0.0739 0.1937 -0.0252 12  DA  F "C5'" 
6014  C  "C4'" . DA  C 12  ? 1.2381 0.7888 0.7293 -0.0719 0.1923 -0.0266 12  DA  F "C4'" 
6015  O  "O4'" . DA  C 12  ? 1.2404 0.788  0.7285 -0.0744 0.1934 -0.0273 12  DA  F "O4'" 
6016  C  "C3'" . DA  C 12  ? 1.2451 0.7888 0.7311 -0.0693 0.1924 -0.0266 12  DA  F "C3'" 
6017  O  "O3'" . DA  C 12  ? 1.2507 0.7912 0.7363 -0.0662 0.1898 -0.0272 12  DA  F "O3'" 
6018  C  "C2'" . DA  C 12  ? 1.2479 0.7858 0.7283 -0.0709 0.1942 -0.0272 12  DA  F "C2'" 
6019  C  "C1'" . DA  C 12  ? 1.2465 0.7859 0.7284 -0.0729 0.1939 -0.0279 12  DA  F "C1'" 
6020  N  N9    . DA  C 12  ? 1.2501 0.7861 0.7275 -0.0762 0.1962 -0.0282 12  DA  F N9    
6021  C  C8    . DA  C 12  ? 1.2505 0.7873 0.7262 -0.0791 0.1984 -0.0275 12  DA  F C8    
6022  N  N7    . DA  C 12  ? 1.2537 0.7862 0.7246 -0.0821 0.2001 -0.0281 12  DA  F N7    
6023  C  C5    . DA  C 12  ? 1.2556 0.7837 0.7246 -0.0805 0.1991 -0.0291 12  DA  F C5    
6024  C  C6    . DA  C 12  ? 1.2592 0.7808 0.7225 -0.0818 0.2003 -0.03   12  DA  F C6    
6025  N  N6    . DA  C 12  ? 1.2621 0.7798 0.72   -0.0858 0.2027 -0.0302 12  DA  F N6    
6026  N  N1    . DA  C 12  ? 1.2607 0.7796 0.7238 -0.079  0.1992 -0.0304 12  DA  F N1    
6027  C  C2    . DA  C 12  ? 1.2579 0.7812 0.7267 -0.0756 0.1966 -0.0301 12  DA  F C2    
6028  N  N3    . DA  C 12  ? 1.2542 0.783  0.728  -0.0744 0.1951 -0.0295 12  DA  F N3    
6029  C  C4    . DA  C 12  ? 1.2533 0.7841 0.7268 -0.0768 0.1966 -0.0291 12  DA  F C4    
6030  P  P     . DC  C 13  ? 1.2576 0.7924 0.739  -0.0631 0.189  -0.0271 13  DC  F P     
6031  O  OP1   . DC  C 13  ? 1.2587 0.7944 0.7426 -0.0611 0.1859 -0.0272 13  DC  F OP1   
6032  O  OP2   . DC  C 13  ? 1.2567 0.7922 0.7368 -0.0634 0.1914 -0.026  13  DC  F OP2   
6033  O  "O5'" . DC  C 13  ? 1.2609 0.788  0.7362 -0.0623 0.1893 -0.0278 13  DC  F "O5'" 
6034  C  "C5'" . DC  C 13  ? 1.2588 0.7828 0.7332 -0.0603 0.1868 -0.0283 13  DC  F "C5'" 
6035  C  "C4'" . DC  C 13  ? 1.2517 0.7788 0.7294 -0.0615 0.1866 -0.0285 13  DC  F "C4'" 
6036  O  "O4'" . DC  C 13  ? 1.2502 0.7773 0.7264 -0.0644 0.1895 -0.0287 13  DC  F "O4'" 
6037  C  "C3'" . DC  C 13  ? 1.2506 0.7737 0.7261 -0.0593 0.1852 -0.0286 13  DC  F "C3'" 
6038  O  "O3'" . DC  C 13  ? 1.2454 0.773  0.7258 -0.0595 0.184  -0.0284 13  DC  F "O3'" 
6039  C  "C2'" . DC  C 13  ? 1.2537 0.7711 0.7232 -0.0602 0.1881 -0.0289 13  DC  F "C2'" 
6040  C  "C1'" . DC  C 13  ? 1.2511 0.7723 0.7225 -0.064  0.1904 -0.0291 13  DC  F "C1'" 
6041  N  N1    . DC  C 13  ? 1.2493 0.7662 0.7153 -0.0661 0.1934 -0.0293 13  DC  F N1    
6042  C  C2    . DC  C 13  ? 1.2505 0.7628 0.7119 -0.0676 0.1955 -0.0298 13  DC  F C2    
6043  O  O2    . DC  C 13  ? 1.2515 0.763  0.7132 -0.0666 0.1949 -0.0299 13  DC  F O2    
6044  N  N3    . DC  C 13  ? 1.2509 0.7592 0.7073 -0.0699 0.1982 -0.0299 13  DC  F N3    
6045  C  C4    . DC  C 13  ? 1.249  0.7587 0.7055 -0.0706 0.199  -0.0295 13  DC  F C4    
6046  N  N4    . DC  C 13  ? 1.2516 0.7576 0.7034 -0.0731 0.2018 -0.0295 13  DC  F N4    
6047  C  C5    . DC  C 13  ? 1.247  0.7614 0.7081 -0.0687 0.1972 -0.0289 13  DC  F C5    
6048  C  C6    . DC  C 13  ? 1.2467 0.7643 0.7121 -0.0666 0.1944 -0.0289 13  DC  F C6    
6049  O  "O5'" . DG  D 1   ? 0.9699 0.4834 0.3728 0.0765  0.3217 0.0316  1   DG  U "O5'" 
6050  C  "C5'" . DG  D 1   ? 0.9744 0.4764 0.37   0.0768  0.3244 0.03    1   DG  U "C5'" 
6051  C  "C4'" . DG  D 1   ? 0.974  0.4674 0.3708 0.0669  0.3181 0.024   1   DG  U "C4'" 
6052  O  "O4'" . DG  D 1   ? 0.9788 0.4554 0.3637 0.067   0.3218 0.0225  1   DG  U "O4'" 
6053  C  "C3'" . DG  D 1   ? 0.9619 0.4719 0.3768 0.0613  0.311  0.0213  1   DG  U "C3'" 
6054  O  "O3'" . DG  D 1   ? 0.9655 0.4713 0.3834 0.0524  0.3042 0.0169  1   DG  U "O3'" 
6055  C  "C2'" . DG  D 1   ? 0.9592 0.4653 0.3724 0.0625  0.3134 0.0205  1   DG  U "C2'" 
6056  C  "C1'" . DG  D 1   ? 0.969  0.4514 0.3641 0.0616  0.3171 0.0191  1   DG  U "C1'" 
6057  N  N9    . DG  D 1   ? 0.9675 0.4403 0.3542 0.065   0.3224 0.0195  1   DG  U N9    
6058  C  C8    . DG  D 1   ? 0.9653 0.4425 0.3498 0.0738  0.3289 0.0235  1   DG  U C8    
6059  N  N7    . DG  D 1   ? 0.9718 0.4373 0.3478 0.0749  0.3328 0.0227  1   DG  U N7    
6060  C  C5    . DG  D 1   ? 0.9763 0.429  0.3487 0.066   0.3284 0.018   1   DG  U C5    
6061  C  C6    . DG  D 1   ? 0.9837 0.4208 0.3473 0.0625  0.3296 0.0152  1   DG  U C6    
6062  O  O6    . DG  D 1   ? 0.9861 0.4164 0.3425 0.0668  0.3352 0.0163  1   DG  U O6    
6063  N  N1    . DG  D 1   ? 0.9868 0.4159 0.3502 0.0527  0.3236 0.011   1   DG  U N1    
6064  C  C2    . DG  D 1   ? 0.9809 0.4163 0.3516 0.0475  0.3172 0.0095  1   DG  U C2    
6065  N  N2    . DG  D 1   ? 0.9839 0.4107 0.3535 0.0384  0.3119 0.0055  1   DG  U N2    
6066  N  N3    . DG  D 1   ? 0.9728 0.4221 0.3514 0.0509  0.3163 0.0118  1   DG  U N3    
6067  C  C4    . DG  D 1   ? 0.9717 0.4292 0.3509 0.0599  0.322  0.016   1   DG  U C4    
6068  P  P     . DA  D 2   ? 0.956  0.4792 0.3922 0.0463  0.2961 0.0145  2   DA  U P     
6069  O  OP1   . DA  D 2   ? 0.9548 0.4794 0.3926 0.043   0.2924 0.014   2   DA  U OP1   
6070  O  OP2   . DA  D 2   ? 0.951  0.4914 0.3979 0.0507  0.297  0.017   2   DA  U OP2   
6071  O  "O5'" . DA  D 2   ? 0.9486 0.4636 0.3857 0.0388  0.292  0.0098  2   DA  U "O5'" 
6072  C  "C5'" . DA  D 2   ? 0.9405 0.4416 0.3707 0.0322  0.2888 0.0066  2   DA  U "C5'" 
6073  C  "C4'" . DA  D 2   ? 0.9254 0.4183 0.3549 0.0265  0.2866 0.0032  2   DA  U "C4'" 
6074  O  "O4'" . DA  D 2   ? 0.9222 0.4071 0.3431 0.0313  0.2928 0.0046  2   DA  U "O4'" 
6075  C  "C3'" . DA  D 2   ? 0.9049 0.4116 0.3506 0.0219  0.2807 0.0011  2   DA  U "C3'" 
6076  O  "O3'" . DA  D 2   ? 0.9015 0.3998 0.3466 0.014   0.2763 -0.0024 2   DA  U "O3'" 
6077  C  "C2'" . DA  D 2   ? 0.8987 0.4106 0.3467 0.0271  0.2848 0.0027  2   DA  U "C2'" 
6078  C  "C1'" . DA  D 2   ? 0.9067 0.4003 0.3378 0.0302  0.2912 0.0035  2   DA  U "C1'" 
6079  N  N9    . DA  D 2   ? 0.896  0.3918 0.3239 0.0383  0.2977 0.0066  2   DA  U N9    
6080  C  C8    . DA  D 2   ? 0.8869 0.3945 0.3181 0.0455  0.3009 0.0104  2   DA  U C8    
6081  N  N7    . DA  D 2   ? 0.8872 0.3938 0.3138 0.0522  0.3069 0.0129  2   DA  U N7    
6082  C  C5    . DA  D 2   ? 0.8938 0.3864 0.3133 0.0491  0.3079 0.0104  2   DA  U C5    
6083  C  C6    . DA  D 2   ? 0.8977 0.3822 0.3096 0.053   0.3134 0.0111  2   DA  U C6    
6084  N  N6    . DA  D 2   ? 0.8952 0.385  0.3053 0.0616  0.3193 0.0149  2   DA  U N6    
6085  N  N1    . DA  D 2   ? 0.904  0.3751 0.3103 0.0476  0.3126 0.008   2   DA  U N1    
6086  C  C2    . DA  D 2   ? 0.905  0.3716 0.3132 0.0389  0.3066 0.0046  2   DA  U C2    
6087  N  N3    . DA  D 2   ? 0.9011 0.3746 0.3163 0.0348  0.3011 0.0036  2   DA  U N3    
6088  C  C4    . DA  D 2   ? 0.8971 0.3833 0.3175 0.0403  0.3021 0.0066  2   DA  U C4    
6089  P  P     . DG  D 3   ? 0.8867 0.3965 0.347  0.0072  0.2685 -0.005  3   DG  U P     
6090  O  OP1   . DG  D 3   ? 0.8938 0.3929 0.3495 -0.0001 0.2645 -0.0076 3   DG  U OP1   
6091  O  OP2   . DG  D 3   ? 0.8783 0.4043 0.3492 0.0096  0.2667 -0.0036 3   DG  U OP2   
6092  O  "O5'" . DG  D 3   ? 0.8712 0.385  0.3379 0.0069  0.2689 -0.0057 3   DG  U "O5'" 
6093  C  "C5'" . DG  D 3   ? 0.8641 0.3647 0.3235 0.0039  0.2701 -0.0073 3   DG  U "C5'" 
6094  C  "C4'" . DG  D 3   ? 0.849  0.3533 0.3119 0.007   0.2731 -0.0067 3   DG  U "C4'" 
6095  O  "O4'" . DG  D 3   ? 0.8479 0.3505 0.3032 0.0153  0.28   -0.0038 3   DG  U "O4'" 
6096  C  "C3'" . DG  D 3   ? 0.8306 0.3522 0.3098 0.0068  0.2696 -0.0069 3   DG  U "C3'" 
6097  O  "O3'" . DG  D 3   ? 0.8211 0.3412 0.3041 0.0039  0.2689 -0.0083 3   DG  U "O3'" 
6098  C  "C2'" . DG  D 3   ? 0.8288 0.3589 0.3087 0.0149  0.2742 -0.0039 3   DG  U "C2'" 
6099  C  "C1'" . DG  D 3   ? 0.8391 0.3544 0.3041 0.0189  0.2808 -0.0028 3   DG  U "C1'" 
6100  N  N9    . DG  D 3   ? 0.8375 0.3566 0.2986 0.0274  0.2864 0.0007  3   DG  U N9    
6101  C  C8    . DG  D 3   ? 0.8318 0.3637 0.2986 0.0312  0.2861 0.003   3   DG  U C8    
6102  N  N7    . DG  D 3   ? 0.8324 0.3673 0.2956 0.0388  0.2917 0.0063  3   DG  U N7    
6103  C  C5    . DG  D 3   ? 0.8378 0.3615 0.2929 0.0405  0.296  0.0059  3   DG  U C5    
6104  C  C6    . DG  D 3   ? 0.8406 0.3617 0.2887 0.0481  0.303  0.0088  3   DG  U C6    
6105  O  O6    . DG  D 3   ? 0.8361 0.3655 0.2844 0.0553  0.3067 0.0124  3   DG  U O6    
6106  N  N1    . DG  D 3   ? 0.8488 0.3568 0.2894 0.0469  0.3055 0.0072  3   DG  U N1    
6107  C  C2    . DG  D 3   ? 0.8526 0.3517 0.293  0.039   0.3017 0.0035  3   DG  U C2    
6108  N  N2    . DG  D 3   ? 0.8579 0.3449 0.2906 0.0387  0.3051 0.0026  3   DG  U N2    
6109  N  N3    . DG  D 3   ? 0.8495 0.3516 0.2967 0.0319  0.2951 0.0011  3   DG  U N3    
6110  C  C4    . DG  D 3   ? 0.8416 0.3557 0.2955 0.0333  0.2927 0.0024  3   DG  U C4    
6111  P  P     . DG  D 4   ? 0.806  0.3395 0.3047 0.0002  0.2635 -0.0096 4   DG  U P     
6112  O  OP1   . DG  D 4   ? 0.8095 0.3424 0.3117 -0.0067 0.2576 -0.0114 4   DG  U OP1   
6113  O  OP2   . DG  D 4   ? 0.7988 0.3465 0.3056 0.0054  0.2642 -0.0079 4   DG  U OP2   
6114  O  "O5'" . DG  D 4   ? 0.8007 0.3289 0.2993 -0.0011 0.2651 -0.0104 4   DG  U "O5'" 
6115  C  "C5'" . DG  D 4   ? 0.8013 0.3148 0.2904 -0.0052 0.2659 -0.0115 4   DG  U "C5'" 
6116  C  "C4'" . DG  D 4   ? 0.7996 0.304  0.2794 -0.0008 0.2724 -0.0106 4   DG  U "C4'" 
6117  O  "O4'" . DG  D 4   ? 0.7974 0.3015 0.2702 0.0068  0.2775 -0.0084 4   DG  U "O4'" 
6118  C  "C3'" . DG  D 4   ? 0.7927 0.3034 0.2802 0.0009  0.2735 -0.0105 4   DG  U "C3'" 
6119  O  "O3'" . DG  D 4   ? 0.8066 0.3043 0.2852 -0.0001 0.2771 -0.0109 4   DG  U "O3'" 
6120  C  "C2'" . DG  D 4   ? 0.7842 0.3037 0.2731 0.0091  0.2773 -0.0083 4   DG  U "C2'" 
6121  C  "C1'" . DG  D 4   ? 0.7905 0.2997 0.2656 0.0125  0.2815 -0.007  4   DG  U "C1'" 
6122  N  N9    . DG  D 4   ? 0.7829 0.3013 0.2591 0.0194  0.2839 -0.0045 4   DG  U N9    
6123  C  C8    . DG  D 4   ? 0.7739 0.3042 0.2579 0.0195  0.2804 -0.0039 4   DG  U C8    
6124  N  N7    . DG  D 4   ? 0.7703 0.3083 0.2544 0.0262  0.2836 -0.0013 4   DG  U N7    
6125  C  C5    . DG  D 4   ? 0.7768 0.3076 0.2528 0.0313  0.2897 0.0001  4   DG  U C5    
6126  C  C6    . DG  D 4   ? 0.7788 0.3132 0.2509 0.0396  0.2953 0.0033  4   DG  U C6    
6127  O  O6    . DG  D 4   ? 0.7726 0.3186 0.2488 0.044   0.2958 0.0058  4   DG  U O6    
6128  N  N1    . DG  D 4   ? 0.7895 0.3132 0.2527 0.0427  0.3008 0.0037  4   DG  U N1    
6129  C  C2    . DG  D 4   ? 0.7957 0.3062 0.2537 0.0379  0.3008 0.0012  4   DG  U C2    
6130  N  N2    . DG  D 4   ? 0.8006 0.3015 0.2495 0.0419  0.3068 0.0021  4   DG  U N2    
6131  N  N3    . DG  D 4   ? 0.7946 0.3023 0.2565 0.0298  0.2953 -0.0017 4   DG  U N3    
6132  C  C4    . DG  D 4   ? 0.7849 0.3032 0.2556 0.0271  0.29   -0.002  4   DG  U C4    
6133  P  P     . DA  D 5   ? 0.8106 0.3108 0.2946 0.001   0.279  -0.0109 5   DA  U P     
6134  O  OP1   . DA  D 5   ? 0.8181 0.3061 0.2966 -0.0051 0.2788 -0.0123 5   DA  U OP1   
6135  O  OP2   . DA  D 5   ? 0.7998 0.3164 0.2991 0.0013  0.2752 -0.0109 5   DA  U OP2   
6136  O  "O5'" . DA  D 5   ? 0.8174 0.3143 0.2927 0.0097  0.2864 -0.0089 5   DA  U "O5'" 
6137  C  "C5'" . DA  D 5   ? 0.8296 0.3104 0.2888 0.0115  0.2916 -0.0084 5   DA  U "C5'" 
6138  C  "C4'" . DA  D 5   ? 0.8345 0.3137 0.2877 0.0199  0.2987 -0.0064 5   DA  U "C4'" 
6139  O  "O4'" . DA  D 5   ? 0.8272 0.3191 0.2852 0.0264  0.2995 -0.0042 5   DA  U "O4'" 
6140  C  "C3'" . DA  D 5   ? 0.8366 0.3188 0.2956 0.0207  0.3    -0.0066 5   DA  U "C3'" 
6141  O  "O3'" . DA  D 5   ? 0.8518 0.3228 0.2985 0.026   0.3073 -0.0054 5   DA  U "O3'" 
6142  C  "C2'" . DA  D 5   ? 0.8224 0.3231 0.2947 0.0248  0.298  -0.0055 5   DA  U "C2'" 
6143  C  "C1'" . DA  D 5   ? 0.8198 0.3236 0.2876 0.03    0.2998 -0.0035 5   DA  U "C1'" 
6144  N  N9    . DA  D 5   ? 0.8083 0.3286 0.2882 0.0303  0.2953 -0.003  5   DA  U N9    
6145  C  C8    . DA  D 5   ? 0.8002 0.3276 0.2903 0.0241  0.2886 -0.0047 5   DA  U C8    
6146  N  N7    . DA  D 5   ? 0.7922 0.3332 0.2905 0.0259  0.2859 -0.0038 5   DA  U N7    
6147  C  C5    . DA  D 5   ? 0.7943 0.3381 0.288  0.0337  0.291  -0.0011 5   DA  U C5    
6148  C  C6    . DA  D 5   ? 0.7869 0.3437 0.2851 0.0386  0.2912 0.0013  5   DA  U C6    
6149  N  N6    . DA  D 5   ? 0.7771 0.3461 0.2854 0.0362  0.286  0.001   5   DA  U N6    
6150  N  N1    . DA  D 5   ? 0.7911 0.3479 0.283  0.0462  0.297  0.0041  5   DA  U N1    
6151  C  C2    . DA  D 5   ? 0.8009 0.3446 0.2819 0.0489  0.3026 0.0045  5   DA  U C2    
6152  N  N3    . DA  D 5   ? 0.8078 0.3378 0.2831 0.0446  0.3031 0.0022  5   DA  U N3    
6153  C  C4    . DA  D 5   ? 0.8042 0.3354 0.2867 0.0368  0.2969 -0.0005 5   DA  U C4    
6154  P  P     . DA  D 6   ? 0.8562 0.3254 0.3046 0.0271  0.3103 -0.0056 6   DA  U P     
6155  O  OP1   . DA  D 6   ? 0.8651 0.3155 0.2973 0.0276  0.3161 -0.0057 6   DA  U OP1   
6156  O  OP2   . DA  D 6   ? 0.8471 0.3246 0.3092 0.0207  0.3043 -0.0074 6   DA  U OP2   
6157  O  "O5'" . DA  D 6   ? 0.8587 0.34   0.3115 0.0364  0.3136 -0.0032 6   DA  U "O5'" 
6158  C  "C5'" . DA  D 6   ? 0.8708 0.3494 0.3138 0.044   0.319  -0.0006 6   DA  U "C5'" 
6159  C  "C4'" . DA  D 6   ? 0.8697 0.365  0.3215 0.051   0.3195 0.0017  6   DA  U "C4'" 
6160  O  "O4'" . DA  D 6   ? 0.865  0.374  0.328  0.0482  0.3133 0.0014  6   DA  U "O4'" 
6161  C  "C3'" . DA  D 6   ? 0.867  0.3691 0.3268 0.0526  0.3198 0.0015  6   DA  U "C3'" 
6162  O  "O3'" . DA  D 6   ? 0.87   0.3684 0.3217 0.0607  0.327  0.0039  6   DA  U "O3'" 
6163  C  "C2'" . DA  D 6   ? 0.858  0.3793 0.3327 0.0526  0.3144 0.0019  6   DA  U "C2'" 
6164  C  "C1'" . DA  D 6   ? 0.8587 0.3831 0.3322 0.0521  0.3123 0.0027  6   DA  U "C1'" 
6165  N  N9    . DA  D 6   ? 0.8525 0.3897 0.3389 0.0474  0.3052 0.0015  6   DA  U N9    
6166  C  C8    . DA  D 6   ? 0.8514 0.3885 0.3449 0.0397  0.2997 -0.0012 6   DA  U C8    
6167  N  N7    . DA  D 6   ? 0.8418 0.3919 0.3464 0.0374  0.2943 -0.0016 6   DA  U N7    
6168  C  C5    . DA  D 6   ? 0.8363 0.3959 0.3415 0.0438  0.2962 0.001   6   DA  U C5    
6169  C  C6    . DA  D 6   ? 0.8251 0.3997 0.3392 0.0447  0.2927 0.002   6   DA  U C6    
6170  N  N6    . DA  D 6   ? 0.8152 0.3971 0.339  0.0392  0.2866 0.0003  6   DA  U N6    
6171  N  N1    . DA  D 6   ? 0.8254 0.4072 0.3376 0.0514  0.2958 0.005   6   DA  U N1    
6172  C  C2    . DA  D 6   ? 0.8321 0.4064 0.3342 0.0573  0.3023 0.007   6   DA  U C2    
6173  N  N3    . DA  D 6   ? 0.8408 0.4002 0.3332 0.0575  0.3064 0.0062  6   DA  U N3    
6174  C  C4    . DA  D 6   ? 0.8433 0.3959 0.3379 0.0502  0.3029 0.0031  6   DA  U C4    
6175  P  P     . DT  D 7   ? 0.8671 0.3689 0.3235 0.0635  0.329  0.0039  7   DT  U P     
6176  O  OP1   . DT  D 7   ? 0.8748 0.3639 0.3175 0.0694  0.337  0.0054  7   DT  U OP1   
6177  O  OP2   . DT  D 7   ? 0.8655 0.3682 0.3311 0.0557  0.3239 0.001   7   DT  U OP2   
6178  O  "O5'" . DT  D 7   ? 0.8589 0.3798 0.3255 0.0689  0.3274 0.0061  7   DT  U "O5'" 
6179  C  "C5'" . DT  D 7   ? 0.8597 0.3846 0.3209 0.0768  0.3316 0.0096  7   DT  U "C5'" 
6180  C  "C4'" . DT  D 7   ? 0.8491 0.3933 0.3217 0.0789  0.3277 0.0112  7   DT  U "C4'" 
6181  O  "O4'" . DT  D 7   ? 0.8425 0.392  0.3226 0.0721  0.321  0.0094  7   DT  U "O4'" 
6182  C  "C3'" . DT  D 7   ? 0.8447 0.4001 0.3276 0.0797  0.3255 0.011   7   DT  U "C3'" 
6183  O  "O3'" . DT  D 7   ? 0.8529 0.4092 0.331  0.0878  0.3313 0.0137  7   DT  U "O3'" 
6184  C  "C2'" . DT  D 7   ? 0.8336 0.4054 0.3269 0.0783  0.3199 0.0117  7   DT  U "C2'" 
6185  C  "C1'" . DT  D 7   ? 0.833  0.3999 0.3247 0.0729  0.3169 0.0103  7   DT  U "C1'" 
6186  N  N1    . DT  D 7   ? 0.828  0.3993 0.3299 0.0649  0.3098 0.0073  7   DT  U N1    
6187  C  C2    . DT  D 7   ? 0.8193 0.4054 0.3312 0.0638  0.3049 0.0078  7   DT  U C2    
6188  O  O2    . DT  D 7   ? 0.8159 0.4117 0.3285 0.0684  0.3057 0.0106  7   DT  U O2    
6189  N  N3    . DT  D 7   ? 0.814  0.4026 0.3344 0.0567  0.2989 0.005   7   DT  U N3    
6190  C  C4    . DT  D 7   ? 0.8145 0.3939 0.3355 0.0511  0.2974 0.0022  7   DT  U C4    
6191  O  O4    . DT  D 7   ? 0.8086 0.3923 0.3381 0.0455  0.2921 0.0004  7   DT  U O4    
6192  C  C5    . DT  D 7   ? 0.8232 0.3883 0.3343 0.0524  0.3026 0.002   7   DT  U C5    
6193  C  C7    . DT  D 7   ? 0.8251 0.3801 0.3361 0.0461  0.3012 -0.0006 7   DT  U C7    
6194  C  C6    . DT  D 7   ? 0.8303 0.3916 0.3321 0.0592  0.3085 0.0044  7   DT  U C6    
6195  P  P     . DG  D 8   ? 0.8563 0.4181 0.3408 0.0893  0.3312 0.0132  8   DG  U P     
6196  O  OP1   . DG  D 8   ? 0.864  0.4195 0.339  0.0972  0.3387 0.0155  8   DG  U OP1   
6197  O  OP2   . DG  D 8   ? 0.8593 0.4166 0.3497 0.0815  0.3271 0.0095  8   DG  U OP2   
6198  O  "O5'" . DG  D 8   ? 0.8449 0.4262 0.3403 0.0908  0.3267 0.0149  8   DG  U "O5'" 
6199  C  "C5'" . DG  D 8   ? 0.8404 0.4306 0.3339 0.0965  0.3284 0.0186  8   DG  U "C5'" 
6200  C  "C4'" . DG  D 8   ? 0.8303 0.4382 0.3353 0.0946  0.3223 0.0193  8   DG  U "C4'" 
6201  O  "O4'" . DG  D 8   ? 0.8225 0.4306 0.3338 0.0864  0.3161 0.0162  8   DG  U "O4'" 
6202  C  "C3'" . DG  D 8   ? 0.8322 0.4488 0.3442 0.0957  0.3206 0.0191  8   DG  U "C3'" 
6203  O  "O3'" . DG  D 8   ? 0.8386 0.4703 0.354  0.1002  0.3199 0.0226  8   DG  U "O3'" 
6204  C  "C2'" . DG  D 8   ? 0.8222 0.4404 0.3432 0.0874  0.3139 0.0155  8   DG  U "C2'" 
6205  C  "C1'" . DG  D 8   ? 0.8149 0.4335 0.3366 0.0832  0.3108 0.015   8   DG  U "C1'" 
6206  N  N9    . DG  D 8   ? 0.8077 0.4218 0.3344 0.0751  0.306  0.0113  8   DG  U N9    
6207  C  C8    . DG  D 8   ? 0.8117 0.413  0.3359 0.0715  0.3069 0.0087  8   DG  U C8    
6208  N  N7    . DG  D 8   ? 0.8056 0.4073 0.3366 0.0646  0.3016 0.006   8   DG  U N7    
6209  C  C5    . DG  D 8   ? 0.7954 0.4101 0.3334 0.0636  0.2971 0.0067  8   DG  U C5    
6210  C  C6    . DG  D 8   ? 0.7858 0.406  0.332  0.0574  0.2909 0.0048  8   DG  U C6    
6211  O  O6    . DG  D 8   ? 0.7859 0.4012 0.3355 0.0517  0.288  0.0023  8   DG  U O6    
6212  N  N1    . DG  D 8   ? 0.7766 0.4097 0.3273 0.0582  0.288  0.0064  8   DG  U N1    
6213  C  C2    . DG  D 8   ? 0.7737 0.4144 0.3218 0.0642  0.2906 0.0096  8   DG  U C2    
6214  N  N2    . DG  D 8   ? 0.7649 0.4181 0.3182 0.0635  0.2869 0.0109  8   DG  U N2    
6215  N  N3    . DG  D 8   ? 0.7829 0.4192 0.3237 0.0703  0.2964 0.0116  8   DG  U N3    
6216  C  C4    . DG  D 8   ? 0.7951 0.4178 0.3308 0.0697  0.2995 0.0099  8   DG  U C4    
6217  P  P     . DC  D 9   ? 0.845  0.4864 0.3653 0.1031  0.3192 0.0236  9   DC  U P     
6218  O  OP1   . DC  D 9   ? 0.8437 0.4943 0.3609 0.111   0.3228 0.0284  9   DC  U OP1   
6219  O  OP2   . DC  D 9   ? 0.8503 0.4807 0.3689 0.1022  0.3211 0.0209  9   DC  U OP2   
6220  O  "O5'" . DC  D 9   ? 0.8444 0.4974 0.3755 0.0966  0.3112 0.022   9   DC  U "O5'" 
6221  C  "C5'" . DC  D 9   ? 0.8483 0.5136 0.3831 0.096   0.3081 0.0242  9   DC  U "C5'" 
6222  C  "C4'" . DC  D 9   ? 0.8522 0.5264 0.3963 0.0897  0.3009 0.0223  9   DC  U "C4'" 
6223  O  "O4'" . DC  D 9   ? 0.8556 0.521  0.402  0.0828  0.2978 0.0183  9   DC  U "O4'" 
6224  C  "C3'" . DC  D 9   ? 0.8596 0.5385 0.4073 0.0903  0.2994 0.0219  9   DC  U "C3'" 
6225  O  "O3'" . DC  D 9   ? 0.8654 0.5586 0.4191 0.0884  0.2944 0.0232  9   DC  U "O3'" 
6226  C  "C2'" . DC  D 9   ? 0.859  0.5278 0.4091 0.0848  0.2974 0.0175  9   DC  U "C2'" 
6227  C  "C1'" . DC  D 9   ? 0.8561 0.5219 0.4079 0.0791  0.2944 0.0158  9   DC  U "C1'" 
6228  N  N1    . DC  D 9   ? 0.861  0.5138 0.4121 0.075   0.2946 0.0124  9   DC  U N1    
6229  C  C2    . DC  D 9   ? 0.8577 0.5103 0.4151 0.0681  0.2894 0.0096  9   DC  U C2    
6230  O  O2    . DC  D 9   ? 0.852  0.5144 0.4146 0.0656  0.2848 0.0098  9   DC  U O2    
6231  N  N3    . DC  D 9   ? 0.8623 0.5041 0.4196 0.0644  0.2895 0.0069  9   DC  U N3    
6232  C  C4    . DC  D 9   ? 0.8702 0.5012 0.4212 0.0668  0.2945 0.0068  9   DC  U C4    
6233  N  N4    . DC  D 9   ? 0.8742 0.4954 0.4257 0.0625  0.2941 0.0043  9   DC  U N4    
6234  C  C5    . DC  D 9   ? 0.8738 0.5036 0.4176 0.0738  0.3001 0.0094  9   DC  U C5    
6235  C  C6    . DC  D 9   ? 0.8693 0.5104 0.4136 0.0779  0.3    0.0122  9   DC  U C6    
6236  P  P     . DA  D 10  ? 0.8722 0.5746 0.4277 0.0914  0.2937 0.0248  10  DA  U P     
6237  O  OP1   . DA  D 10  ? 0.8696 0.5841 0.4238 0.0967  0.2953 0.0296  10  DA  U OP1   
6238  O  OP2   . DA  D 10  ? 0.8744 0.5666 0.427  0.0937  0.2971 0.0231  10  DA  U OP2   
6239  O  "O5'" . DA  D 10  ? 0.8763 0.585  0.439  0.0842  0.2865 0.0226  10  DA  U "O5'" 
6240  C  "C5'" . DA  D 10  ? 0.8857 0.5875 0.4513 0.0776  0.2832 0.019   10  DA  U "C5'" 
6241  C  "C4'" . DA  D 10  ? 0.8906 0.5942 0.461  0.0724  0.2782 0.0166  10  DA  U "C4'" 
6242  O  "O4'" . DA  D 10  ? 0.8924 0.5844 0.464  0.0685  0.2778 0.0129  10  DA  U "O4'" 
6243  C  "C3'" . DA  D 10  ? 0.8993 0.6056 0.4691 0.0754  0.2787 0.0173  10  DA  U "C3'" 
6244  O  "O3'" . DA  D 10  ? 0.9101 0.6209 0.4838 0.0704  0.2733 0.0159  10  DA  U "O3'" 
6245  C  "C2'" . DA  D 10  ? 0.8997 0.5926 0.467  0.077   0.2827 0.0151  10  DA  U "C2'" 
6246  C  "C1'" . DA  D 10  ? 0.895  0.5807 0.4652 0.0708  0.2802 0.012   10  DA  U "C1'" 
6247  N  N9    . DA  D 10  ? 0.8934 0.5669 0.4607 0.0716  0.2843 0.0106  10  DA  U N9    
6248  C  C8    . DA  D 10  ? 0.8949 0.5632 0.4564 0.077   0.29   0.012   10  DA  U C8    
6249  N  N7    . DA  D 10  ? 0.8979 0.5545 0.4573 0.0757  0.2924 0.0102  10  DA  U N7    
6250  C  C5    . DA  D 10  ? 0.8958 0.5507 0.4607 0.0692  0.2879 0.0075  10  DA  U C5    
6251  C  C6    . DA  D 10  ? 0.8967 0.5421 0.4629 0.0647  0.2874 0.005   10  DA  U C6    
6252  N  N6    . DA  D 10  ? 0.9012 0.5361 0.4628 0.0657  0.2915 0.0045  10  DA  U N6    
6253  N  N1    . DA  D 10  ? 0.8933 0.5404 0.4655 0.059   0.2825 0.0031  10  DA  U N1    
6254  C  C2    . DA  D 10  ? 0.8892 0.5457 0.465  0.0577  0.2785 0.0035  10  DA  U C2    
6255  N  N3    . DA  D 10  ? 0.8882 0.5539 0.4629 0.061   0.2782 0.0057  10  DA  U N3    
6256  C  C4    . DA  D 10  ? 0.8921 0.5569 0.4616 0.0668  0.283  0.0077  10  DA  U C4    
6257  P  P     . DG  D 11  ? 0.9185 0.6385 0.4918 0.0722  0.2716 0.0178  11  DG  U P     
6258  O  OP1   . DG  D 11  ? 0.9127 0.6455 0.4883 0.0697  0.2675 0.0199  11  DG  U OP1   
6259  O  OP2   . DG  D 11  ? 0.9179 0.6362 0.487  0.0794  0.2769 0.0197  11  DG  U OP2   
6260  O  "O5'" . DG  D 11  ? 0.9317 0.6454 0.5067 0.0679  0.2686 0.0145  11  DG  U "O5'" 
6261  C  "C5'" . DG  D 11  ? 0.9408 0.6544 0.5193 0.0611  0.2637 0.0123  11  DG  U "C5'" 
6262  C  "C4'" . DG  D 11  ? 0.9539 0.6572 0.5334 0.0585  0.2632 0.0091  11  DG  U "C4'" 
6263  O  "O4'" . DG  D 11  ? 0.9578 0.651  0.537  0.0601  0.2673 0.0078  11  DG  U "O4'" 
6264  C  "C3'" . DG  D 11  ? 0.9651 0.667  0.5424 0.0605  0.2636 0.0091  11  DG  U "C3'" 
6265  O  "O3'" . DG  D 11  ? 0.9808 0.6776 0.5595 0.0559  0.2605 0.0066  11  DG  U "O3'" 
6266  C  "C2'" . DG  D 11  ? 0.9638 0.6576 0.539  0.0658  0.2694 0.009   11  DG  U "C2'" 
6267  C  "C1'" . DG  D 11  ? 0.9611 0.6478 0.5384 0.0636  0.2705 0.0074  11  DG  U "C1'" 
6268  N  N9    . DG  D 11  ? 0.9612 0.6427 0.5357 0.0682  0.2759 0.0081  11  DG  U N9    
6269  C  C8    . DG  D 11  ? 0.9607 0.6461 0.5315 0.074   0.2794 0.0108  11  DG  U C8    
6270  N  N7    . DG  D 11  ? 0.9639 0.6419 0.5319 0.077   0.2842 0.0109  11  DG  U N7    
6271  C  C5    . DG  D 11  ? 0.9651 0.6344 0.5356 0.0725  0.2834 0.0081  11  DG  U C5    
6272  C  C6    . DG  D 11  ? 0.9682 0.6269 0.5371 0.0725  0.2869 0.0069  11  DG  U C6    
6273  O  O6    . DG  D 11  ? 0.9696 0.6236 0.5338 0.0766  0.2917 0.0079  11  DG  U O6    
6274  N  N1    . DG  D 11  ? 0.9675 0.6211 0.5407 0.0668  0.2842 0.0044  11  DG  U N1    
6275  C  C2    . DG  D 11  ? 0.9634 0.6208 0.5412 0.0623  0.2793 0.0032  11  DG  U C2    
6276  N  N2    . DG  D 11  ? 0.9625 0.6141 0.5439 0.0577  0.2776 0.0012  11  DG  U N2    
6277  N  N3    . DG  D 11  ? 0.9615 0.6274 0.5399 0.0623  0.2762 0.0041  11  DG  U N3    
6278  C  C4    . DG  D 11  ? 0.9626 0.6343 0.5375 0.0673  0.2784 0.0065  11  DG  U C4    
6279  P  P     . DA  D 12  ? 0.9954 0.6916 0.5714 0.056   0.259  0.0064  12  DA  U P     
6280  O  OP1   . DA  D 12  ? 0.9941 0.6958 0.5703 0.0505  0.2536 0.0061  12  DA  U OP1   
6281  O  OP2   . DA  D 12  ? 0.9964 0.6954 0.569  0.062   0.2622 0.0085  12  DA  U OP2   
6282  O  "O5'" . DA  D 12  ? 1.0044 0.6883 0.5815 0.0554  0.2608 0.0039  12  DA  U "O5'" 
6283  C  "C5'" . DA  D 12  ? 1.0067 0.6855 0.5876 0.052   0.2605 0.0022  12  DA  U "C5'" 
6284  C  "C4'" . DA  D 12  ? 1.0099 0.6783 0.5918 0.0539  0.2643 0.001   12  DA  U "C4'" 
6285  O  "O4'" . DA  D 12  ? 1.0088 0.6755 0.5904 0.0573  0.2685 0.0018  12  DA  U "O4'" 
6286  C  "C3'" . DA  D 12  ? 1.0128 0.6768 0.592  0.057   0.2663 0.0011  12  DA  U "C3'" 
6287  O  "O3'" . DA  D 12  ? 1.017  0.6727 0.5983 0.0551  0.2666 -0.0004 12  DA  U "O3'" 
6288  C  "C2'" . DA  D 12  ? 1.0123 0.6748 0.5895 0.0628  0.2713 0.0023  12  DA  U "C2'" 
6289  C  "C1'" . DA  D 12  ? 1.0114 0.672  0.5912 0.0616  0.2727 0.0019  12  DA  U "C1'" 
6290  N  N9    . DA  D 12  ? 1.0122 0.6738 0.5892 0.0663  0.2767 0.0034  12  DA  U N9    
6291  C  C8    . DA  D 12  ? 1.0113 0.6799 0.5848 0.0704  0.2776 0.0056  12  DA  U C8    
6292  N  N7    . DA  D 12  ? 1.0124 0.6793 0.5834 0.0747  0.282  0.0068  12  DA  U N7    
6293  C  C5    . DA  D 12  ? 1.0149 0.6727 0.5875 0.0729  0.284  0.0051  12  DA  U C5    
6294  C  C6    . DA  D 12  ? 1.0194 0.6704 0.5898 0.0752  0.2885 0.0052  12  DA  U C6    
6295  N  N6    . DA  D 12  ? 1.0219 0.674  0.5875 0.0805  0.2925 0.0071  12  DA  U N6    
6296  N  N1    . DA  D 12  ? 1.0212 0.664  0.594  0.0718  0.289  0.0033  12  DA  U N1    
6297  C  C2    . DA  D 12  ? 1.0187 0.6609 0.5963 0.0669  0.2852 0.0018  12  DA  U C2    
6298  N  N3    . DA  D 12  ? 1.0152 0.6626 0.5948 0.0648  0.2812 0.0015  12  DA  U N3    
6299  C  C4    . DA  D 12  ? 1.014  0.6689 0.5907 0.0678  0.2807 0.0031  12  DA  U C4    
6300  P  P     . DC  D 13  ? 1.0205 0.6714 0.5989 0.0564  0.2669 -0.0007 13  DC  U P     
6301  O  OP1   . DC  D 13  ? 1.0223 0.668  0.6033 0.0525  0.2651 -0.002  13  DC  U OP1   
6302  O  OP2   . DC  D 13  ? 1.0195 0.6769 0.5932 0.0574  0.2649 0.0004  13  DC  U OP2   
6303  O  "O5'" . DC  D 13  ? 1.0212 0.6658 0.5991 0.0617  0.2726 -0.0002 13  DC  U "O5'" 
6304  C  "C5'" . DC  D 13  ? 1.0201 0.6565 0.6015 0.0615  0.2752 -0.001  13  DC  U "C5'" 
6305  C  "C4'" . DC  D 13  ? 1.0164 0.6523 0.602  0.0593  0.2757 -0.0014 13  DC  U "C4'" 
6306  O  "O4'" . DC  D 13  ? 1.0145 0.6546 0.5979 0.0616  0.2772 -0.0006 13  DC  U "O4'" 
6307  C  "C3'" . DC  D 13  ? 1.0162 0.6443 0.6048 0.0599  0.2794 -0.0017 13  DC  U "C3'" 
6308  O  "O3'" . DC  D 13  ? 1.0147 0.6422 0.6078 0.0556  0.2778 -0.0024 13  DC  U "O3'" 
6309  C  "C2'" . DC  D 13  ? 1.017  0.6438 0.6024 0.0646  0.2838 -0.0009 13  DC  U "C2'" 
6310  C  "C1'" . DC  D 13  ? 1.015  0.6494 0.5983 0.0644  0.2819 -0.0004 13  DC  U "C1'" 
6311  N  N1    . DC  D 13  ? 1.0139 0.6507 0.5923 0.0698  0.285  0.001   13  DC  U N1    
6312  C  C2    . DC  D 13  ? 1.0129 0.6465 0.5895 0.0725  0.2891 0.0015  13  DC  U C2    
6313  O  O2    . DC  D 13  ? 1.0127 0.6411 0.5916 0.07    0.2901 0.0007  13  DC  U O2    
6314  N  N3    . DC  D 13  ? 1.0122 0.648  0.5839 0.0779  0.2921 0.0031  13  DC  U N3    
6315  C  C4    . DC  D 13  ? 1.0101 0.6522 0.5794 0.0802  0.2906 0.0041  13  DC  U C4    
6316  N  N4    . DC  D 13  ? 1.0095 0.6543 0.5743 0.0857  0.2937 0.0059  13  DC  U N4    
6317  C  C5    . DC  D 13  ? 1.0106 0.6559 0.5815 0.0769  0.2861 0.0035  13  DC  U C5    
6318  C  C6    . DC  D 13  ? 1.0121 0.6544 0.5873 0.072   0.2835 0.0019  13  DC  U C6    
6319  O  "O5'" . DG  E 1   ? 0.8683 0.4603 0.3973 0.1097  0.3336 0.0099  1   DG  V "O5'" 
6320  C  "C5'" . DG  E 1   ? 0.874  0.4547 0.4031 0.1075  0.3362 0.0082  1   DG  V "C5'" 
6321  C  "C4'" . DG  E 1   ? 0.8731 0.453  0.4097 0.0994  0.3313 0.0059  1   DG  V "C4'" 
6322  O  "O4'" . DG  E 1   ? 0.8684 0.4579 0.412  0.0977  0.326  0.0057  1   DG  V "O4'" 
6323  C  "C3'" . DG  E 1   ? 0.8733 0.4529 0.4102 0.0946  0.3288 0.0053  1   DG  V "C3'" 
6324  O  "O3'" . DG  E 1   ? 0.8742 0.4468 0.4146 0.0882  0.3276 0.0034  1   DG  V "O3'" 
6325  C  "C2'" . DG  E 1   ? 0.8673 0.4593 0.4097 0.0928  0.3229 0.0055  1   DG  V "C2'" 
6326  C  "C1'" . DG  E 1   ? 0.8649 0.4603 0.4127 0.0926  0.3208 0.005   1   DG  V "C1'" 
6327  N  N9    . DG  E 1   ? 0.861  0.4679 0.4111 0.0939  0.3169 0.006   1   DG  V N9    
6328  C  C8    . DG  E 1   ? 0.8598 0.4738 0.4059 0.0991  0.318  0.0082  1   DG  V C8    
6329  N  N7    . DG  E 1   ? 0.8559 0.4801 0.4054 0.0981  0.3133 0.0087  1   DG  V N7    
6330  C  C5    . DG  E 1   ? 0.8543 0.4775 0.41   0.092   0.3091 0.0066  1   DG  V C5    
6331  C  C6    . DG  E 1   ? 0.8506 0.4811 0.4111 0.0884  0.3035 0.006   1   DG  V C6    
6332  O  O6    . DG  E 1   ? 0.846  0.4858 0.4065 0.0893  0.3006 0.0072  1   DG  V O6    
6333  N  N1    . DG  E 1   ? 0.8523 0.4783 0.4179 0.083   0.3011 0.004   1   DG  V N1    
6334  C  C2    . DG  E 1   ? 0.8546 0.4712 0.4212 0.0812  0.3037 0.0029  1   DG  V C2    
6335  N  N2    . DG  E 1   ? 0.8547 0.4693 0.427  0.0761  0.3008 0.0014  1   DG  V N2    
6336  N  N3    . DG  E 1   ? 0.8566 0.4664 0.4187 0.084   0.3087 0.0033  1   DG  V N3    
6337  C  C4    . DG  E 1   ? 0.8572 0.4703 0.4137 0.0895  0.3113 0.0051  1   DG  V C4    
6338  P  P     . DT  E 2   ? 0.8755 0.4433 0.4139 0.0832  0.3265 0.0025  2   DT  V P     
6339  O  OP1   . DT  E 2   ? 0.8822 0.4378 0.4178 0.0805  0.3298 0.0015  2   DT  V OP1   
6340  O  OP2   . DT  E 2   ? 0.8767 0.4476 0.4088 0.0872  0.3279 0.0041  2   DT  V OP2   
6341  O  "O5'" . DT  E 2   ? 0.8632 0.4382 0.4109 0.0766  0.3195 0.0013  2   DT  V "O5'" 
6342  C  "C5'" . DT  E 2   ? 0.8534 0.4275 0.4083 0.0725  0.3173 0.0001  2   DT  V "C5'" 
6343  C  "C4'" . DT  E 2   ? 0.8425 0.4254 0.4051 0.0682  0.3109 -0.0005 2   DT  V "C4'" 
6344  O  "O4'" . DT  E 2   ? 0.8361 0.4282 0.399  0.0722  0.3094 0.0005  2   DT  V "O4'" 
6345  C  "C3'" . DT  E 2   ? 0.8416 0.4257 0.4042 0.0638  0.3077 -0.0011 2   DT  V "C3'" 
6346  O  "O3'" . DT  E 2   ? 0.8412 0.4264 0.4111 0.0574  0.3032 -0.0023 2   DT  V "O3'" 
6347  C  "C2'" . DT  E 2   ? 0.8352 0.4291 0.3971 0.0667  0.3055 -0.0001 2   DT  V "C2'" 
6348  C  "C1'" . DT  E 2   ? 0.8291 0.4285 0.3944 0.0694  0.3048 0.0003  2   DT  V "C1'" 
6349  N  N1    . DT  E 2   ? 0.8212 0.4292 0.384  0.0741  0.3045 0.0019  2   DT  V N1    
6350  C  C2    . DT  E 2   ? 0.8142 0.431  0.3815 0.073   0.3    0.0019  2   DT  V C2    
6351  O  O2    . DT  E 2   ? 0.8105 0.4278 0.3834 0.0688  0.2967 0.0007  2   DT  V O2    
6352  N  N3    . DT  E 2   ? 0.8113 0.4363 0.376  0.0768  0.2997 0.0036  2   DT  V N3    
6353  C  C4    . DT  E 2   ? 0.8114 0.4372 0.37   0.082   0.3035 0.0055  2   DT  V C4    
6354  O  O4    . DT  E 2   ? 0.8068 0.4415 0.3644 0.085   0.3026 0.0073  2   DT  V O4    
6355  C  C5    . DT  E 2   ? 0.8178 0.4333 0.3714 0.0834  0.3085 0.0053  2   DT  V C5    
6356  C  C7    . DT  E 2   ? 0.8222 0.4367 0.3681 0.0895  0.3134 0.0075  2   DT  V C7    
6357  C  C6    . DT  E 2   ? 0.8214 0.4284 0.3771 0.0792  0.3086 0.0034  2   DT  V C6    
6358  P  P     . DC  E 3   ? 0.8436 0.4274 0.4141 0.0515  0.3    -0.0032 3   DC  V P     
6359  O  OP1   . DC  E 3   ? 0.8489 0.4247 0.4206 0.047   0.3008 -0.0039 3   DC  V OP1   
6360  O  OP2   . DC  E 3   ? 0.8466 0.4307 0.4101 0.0542  0.3013 -0.0026 3   DC  V OP2   
6361  O  "O5'" . DC  E 3   ? 0.8318 0.4247 0.4104 0.0481  0.294  -0.0037 3   DC  V "O5'" 
6362  C  "C5'" . DC  E 3   ? 0.822  0.4172 0.4068 0.0476  0.2928 -0.0037 3   DC  V "C5'" 
6363  C  "C4'" . DC  E 3   ? 0.81   0.4142 0.3982 0.0479  0.2889 -0.0036 3   DC  V "C4'" 
6364  O  "O4'" . DC  E 3   ? 0.8056 0.4137 0.3891 0.0533  0.2906 -0.0027 3   DC  V "O4'" 
6365  C  "C3'" . DC  E 3   ? 0.8038 0.4125 0.394  0.0438  0.2843 -0.0042 3   DC  V "C3'" 
6366  O  "O3'" . DC  E 3   ? 0.7992 0.4077 0.3959 0.0387  0.2811 -0.0049 3   DC  V "O3'" 
6367  C  "C2'" . DC  E 3   ? 0.7984 0.4157 0.3884 0.0462  0.2822 -0.0037 3   DC  V "C2'" 
6368  C  "C1'" . DC  E 3   ? 0.797  0.4136 0.3824 0.0524  0.2864 -0.0027 3   DC  V "C1'" 
6369  N  N1    . DC  E 3   ? 0.7892 0.4098 0.3691 0.0562  0.2878 -0.0015 3   DC  V N1    
6370  C  C2    . DC  E 3   ? 0.7821 0.412  0.3626 0.0573  0.2849 -0.0008 3   DC  V C2    
6371  O  O2    . DC  E 3   ? 0.7793 0.4129 0.3641 0.0547  0.2812 -0.0014 3   DC  V O2    
6372  N  N3    . DC  E 3   ? 0.7786 0.413  0.3546 0.0612  0.2864 0.0008  3   DC  V N3    
6373  C  C4    . DC  E 3   ? 0.7793 0.4086 0.3499 0.0643  0.2909 0.0016  3   DC  V C4    
6374  N  N4    . DC  E 3   ? 0.7752 0.4095 0.3415 0.0686  0.2925 0.0036  3   DC  V N4    
6375  C  C5    . DC  E 3   ? 0.7859 0.4045 0.3549 0.0633  0.294  0.0006  3   DC  V C5    
6376  C  C6    . DC  E 3   ? 0.7889 0.404  0.363  0.0589  0.292  -0.0009 3   DC  V C6    
6377  P  P     . DT  E 4   ? 0.7953 0.4011 0.3933 0.033   0.2788 -0.0057 4   DT  V P     
6378  O  OP1   . DT  E 4   ? 0.7896 0.3944 0.3944 0.029   0.2769 -0.0057 4   DT  V OP1   
6379  O  OP2   . DT  E 4   ? 0.8007 0.3999 0.3919 0.0341  0.2823 -0.0056 4   DT  V OP2   
6380  O  "O5'" . DT  E 4   ? 0.7858 0.3986 0.3842 0.0316  0.2745 -0.006  4   DT  V "O5'" 
6381  C  "C5'" . DT  E 4   ? 0.7737 0.3931 0.3763 0.0313  0.2714 -0.006  4   DT  V "C5'" 
6382  C  "C4'" . DT  E 4   ? 0.7631 0.3891 0.3633 0.0323  0.2693 -0.0059 4   DT  V "C4'" 
6383  O  "O4'" . DT  E 4   ? 0.7607 0.3875 0.3554 0.0375  0.2727 -0.0049 4   DT  V "O4'" 
6384  C  "C3'" . DT  E 4   ? 0.7596 0.386  0.3589 0.029   0.2671 -0.0064 4   DT  V "C3'" 
6385  O  "O3'" . DT  E 4   ? 0.7556 0.3888 0.3573 0.0271  0.2629 -0.0066 4   DT  V "O3'" 
6386  C  "C2'" . DT  E 4   ? 0.7609 0.386  0.3534 0.0328  0.2705 -0.0056 4   DT  V "C2'" 
6387  C  "C1'" . DT  E 4   ? 0.7607 0.3897 0.3517 0.0379  0.2724 -0.0046 4   DT  V "C1'" 
6388  N  N1    . DT  E 4   ? 0.7665 0.3923 0.3512 0.0428  0.2773 -0.0035 4   DT  V N1    
6389  C  C2    . DT  E 4   ? 0.7668 0.3985 0.3479 0.0468  0.2782 -0.002  4   DT  V C2    
6390  O  O2    . DT  E 4   ? 0.7637 0.4036 0.3469 0.0462  0.275  -0.0016 4   DT  V O2    
6391  N  N3    . DT  E 4   ? 0.7687 0.3964 0.3436 0.0515  0.2831 -0.0009 4   DT  V N3    
6392  C  C4    . DT  E 4   ? 0.7723 0.3901 0.3435 0.0522  0.2872 -0.0012 4   DT  V C4    
6393  O  O4    . DT  E 4   ? 0.7768 0.3913 0.3417 0.0569  0.2917 0       4   DT  V O4    
6394  C  C5    . DT  E 4   ? 0.7711 0.3832 0.3465 0.0474  0.2857 -0.0029 4   DT  V C5    
6395  C  C7    . DT  E 4   ? 0.7742 0.3757 0.3463 0.0471  0.2896 -0.0033 4   DT  V C7    
6396  C  C6    . DT  E 4   ? 0.7689 0.3856 0.351  0.043   0.2809 -0.0038 4   DT  V C6    
6397  P  P     . DG  E 5   ? 0.7498 0.3836 0.353  0.0222  0.2593 -0.0074 5   DG  V P     
6398  O  OP1   . DG  E 5   ? 0.7465 0.3816 0.3556 0.0186  0.256  -0.008  5   DG  V OP1   
6399  O  OP2   . DG  E 5   ? 0.7507 0.3779 0.3506 0.0214  0.2614 -0.0076 5   DG  V OP2   
6400  O  "O5'" . DG  E 5   ? 0.7436 0.3846 0.3444 0.0235  0.2578 -0.0069 5   DG  V "O5'" 
6401  C  "C5'" . DG  E 5   ? 0.7363 0.384  0.3393 0.0232  0.255  -0.0067 5   DG  V "C5'" 
6402  C  "C4'" . DG  E 5   ? 0.7311 0.3851 0.3306 0.0269  0.256  -0.0054 5   DG  V "C4'" 
6403  O  "O4'" . DG  E 5   ? 0.7314 0.3828 0.3277 0.0317  0.2603 -0.0045 5   DG  V "O4'" 
6404  C  "C3'" . DG  E 5   ? 0.7287 0.3854 0.3252 0.0272  0.256  -0.0046 5   DG  V "C3'" 
6405  O  "O3'" . DG  E 5   ? 0.7242 0.3861 0.323  0.0236  0.2518 -0.005  5   DG  V "O3'" 
6406  C  "C2'" . DG  E 5   ? 0.7272 0.3887 0.3202 0.0323  0.2586 -0.0027 5   DG  V "C2'" 
6407  C  "C1'" . DG  E 5   ? 0.7299 0.3856 0.322  0.0352  0.2621 -0.0029 5   DG  V "C1'" 
6408  N  N9    . DG  E 5   ? 0.7335 0.3827 0.3212 0.0379  0.2664 -0.0024 5   DG  V N9    
6409  C  C8    . DG  E 5   ? 0.7358 0.3761 0.3231 0.0359  0.2678 -0.0036 5   DG  V C8    
6410  N  N7    . DG  E 5   ? 0.7401 0.3752 0.3219 0.0389  0.2719 -0.0029 5   DG  V N7    
6411  C  C5    . DG  E 5   ? 0.7414 0.3828 0.32   0.0435  0.2734 -0.0009 5   DG  V C5    
6412  C  C6    . DG  E 5   ? 0.748  0.3878 0.3201 0.0486  0.278  0.0009  5   DG  V C6    
6413  O  O6    . DG  E 5   ? 0.7562 0.3871 0.323  0.0499  0.2818 0.0008  5   DG  V O6    
6414  N  N1    . DG  E 5   ? 0.7449 0.3944 0.3165 0.0522  0.2779 0.003   5   DG  V N1    
6415  C  C2    . DG  E 5   ? 0.7392 0.3983 0.3156 0.0505  0.2737 0.0032  5   DG  V C2    
6416  N  N2    . DG  E 5   ? 0.7374 0.4057 0.3126 0.0542  0.2741 0.0056  5   DG  V N2    
6417  N  N3    . DG  E 5   ? 0.7358 0.3953 0.3175 0.0457  0.2697 0.0013  5   DG  V N3    
6418  C  C4    . DG  E 5   ? 0.7363 0.3869 0.3189 0.0427  0.2699 -0.0006 5   DG  V C4    
6419  P  P     . DC  E 6   ? 0.721  0.3834 0.3181 0.022   0.251  -0.0048 6   DC  V P     
6420  O  OP1   . DC  E 6   ? 0.7208 0.3886 0.3209 0.0181  0.2465 -0.0053 6   DC  V OP1   
6421  O  OP2   . DC  E 6   ? 0.7217 0.3752 0.3174 0.0209  0.2527 -0.0057 6   DC  V OP2   
6422  O  "O5'" . DC  E 6   ? 0.7197 0.3868 0.3124 0.0269  0.2539 -0.0025 6   DC  V "O5'" 
6423  C  "C5'" . DC  E 6   ? 0.7196 0.3961 0.3128 0.0285  0.2528 -0.001  6   DC  V "C5'" 
6424  C  "C4'" . DC  E 6   ? 0.7231 0.4036 0.3121 0.0338  0.2563 0.0016  6   DC  V "C4'" 
6425  O  "O4'" . DC  E 6   ? 0.7262 0.4008 0.3121 0.0381  0.2608 0.0019  6   DC  V "O4'" 
6426  C  "C3'" . DC  E 6   ? 0.7278 0.4068 0.3137 0.0344  0.2578 0.0025  6   DC  V "C3'" 
6427  O  "O3'" . DC  E 6   ? 0.7313 0.4181 0.3191 0.0321  0.2546 0.0033  6   DC  V "O3'" 
6428  C  "C2'" . DC  E 6   ? 0.7261 0.4057 0.3071 0.0409  0.2628 0.005   6   DC  V "C2'" 
6429  C  "C1'" . DC  E 6   ? 0.727  0.4009 0.3078 0.0425  0.2648 0.0039  6   DC  V "C1'" 
6430  N  N1    . DC  E 6   ? 0.7303 0.3922 0.3075 0.0429  0.2682 0.0027  6   DC  V N1    
6431  C  C2    . DC  E 6   ? 0.7325 0.3903 0.3032 0.048   0.2734 0.0045  6   DC  V C2    
6432  O  O2    . DC  E 6   ? 0.7304 0.3952 0.2991 0.0526  0.2753 0.0071  6   DC  V O2    
6433  N  N3    . DC  E 6   ? 0.7371 0.3832 0.3037 0.0478  0.2763 0.0033  6   DC  V N3    
6434  C  C4    . DC  E 6   ? 0.7376 0.3775 0.3071 0.0425  0.2739 0.0007  6   DC  V C4    
6435  N  N4    . DC  E 6   ? 0.7415 0.3702 0.3067 0.0419  0.2766 -0.0002 6   DC  V N4    
6436  C  C5    . DC  E 6   ? 0.7348 0.3795 0.3113 0.0377  0.2687 -0.0007 6   DC  V C5    
6437  C  C6    . DC  E 6   ? 0.7314 0.3865 0.3112 0.0381  0.2661 0.0002  6   DC  V C6    
6438  P  P     . DA  E 7   ? 0.7375 0.4215 0.3234 0.0305  0.2544 0.0033  7   DA  V P     
6439  O  OP1   . DA  E 7   ? 0.7353 0.4264 0.325  0.0263  0.2499 0.0031  7   DA  V OP1   
6440  O  OP2   . DA  E 7   ? 0.7414 0.4135 0.3255 0.0289  0.2557 0.0012  7   DA  V OP2   
6441  O  "O5'" . DA  E 7   ? 0.7436 0.4308 0.3246 0.0365  0.2588 0.0067  7   DA  V "O5'" 
6442  C  "C5'" . DA  E 7   ? 0.7566 0.436  0.3321 0.0384  0.2622 0.0071  7   DA  V "C5'" 
6443  C  "C4'" . DA  E 7   ? 0.7672 0.4456 0.3371 0.0452  0.2678 0.0097  7   DA  V "C4'" 
6444  O  "O4'" . DA  E 7   ? 0.7722 0.4426 0.3406 0.0463  0.2701 0.0082  7   DA  V "O4'" 
6445  C  "C3'" . DA  E 7   ? 0.7782 0.4502 0.3412 0.048   0.2717 0.0111  7   DA  V "C3'" 
6446  O  "O3'" . DA  E 7   ? 0.7846 0.4667 0.3478 0.0506  0.272  0.0144  7   DA  V "O3'" 
6447  C  "C2'" . DA  E 7   ? 0.7806 0.4451 0.3375 0.0532  0.2773 0.0119  7   DA  V "C2'" 
6448  C  "C1'" . DA  E 7   ? 0.7776 0.4401 0.3386 0.051   0.2756 0.0094  7   DA  V "C1'" 
6449  N  N9    . DA  E 7   ? 0.7816 0.4312 0.3403 0.0481  0.2763 0.0066  7   DA  V N9    
6450  C  C8    . DA  E 7   ? 0.7816 0.4281 0.3451 0.042   0.2722 0.0036  7   DA  V C8    
6451  N  N7    . DA  E 7   ? 0.7861 0.4212 0.3466 0.0404  0.2738 0.0019  7   DA  V N7    
6452  C  C5    . DA  E 7   ? 0.7872 0.4168 0.3399 0.0457  0.2794 0.0036  7   DA  V C5    
6453  C  C6    . DA  E 7   ? 0.789  0.406  0.3348 0.0468  0.2836 0.0029  7   DA  V C6    
6454  N  N6    . DA  E 7   ? 0.7892 0.3976 0.3357 0.0419  0.2822 0.0004  7   DA  V N6    
6455  N  N1    . DA  E 7   ? 0.7924 0.406  0.3303 0.0529  0.2892 0.0052  7   DA  V N1    
6456  C  C2    . DA  E 7   ? 0.7909 0.4142 0.3286 0.0579  0.2905 0.0081  7   DA  V C2    
6457  N  N3    . DA  E 7   ? 0.7872 0.4236 0.3316 0.0572  0.2867 0.0092  7   DA  V N3    
6458  C  C4    . DA  E 7   ? 0.7858 0.4242 0.3373 0.0509  0.2812 0.0066  7   DA  V C4    
6459  P  P     . DT  E 8   ? 0.7971 0.4768 0.3568 0.0502  0.2725 0.0153  8   DT  V P     
6460  O  OP1   . DT  E 8   ? 0.7909 0.484  0.3557 0.0491  0.2694 0.0174  8   DT  V OP1   
6461  O  OP2   . DT  E 8   ? 0.8009 0.4683 0.3589 0.0453  0.271  0.0117  8   DT  V OP2   
6462  O  "O5'" . DT  E 8   ? 0.8103 0.4856 0.3613 0.0578  0.2795 0.0186  8   DT  V "O5'" 
6463  C  "C5'" . DT  E 8   ? 0.8142 0.4974 0.3651 0.0638  0.2826 0.0218  8   DT  V "C5'" 
6464  C  "C4'" . DT  E 8   ? 0.8294 0.5021 0.3713 0.0697  0.2892 0.0229  8   DT  V "C4'" 
6465  O  "O4'" . DT  E 8   ? 0.838  0.4974 0.3778 0.0664  0.2892 0.019   8   DT  V "O4'" 
6466  C  "C3'" . DT  E 8   ? 0.8401 0.5062 0.3734 0.0737  0.294  0.0253  8   DT  V "C3'" 
6467  O  "O3'" . DT  E 8   ? 0.8486 0.5141 0.3756 0.0817  0.3003 0.0288  8   DT  V "O3'" 
6468  C  "C2'" . DT  E 8   ? 0.847  0.4962 0.375  0.0695  0.2941 0.0214  8   DT  V "C2'" 
6469  C  "C1'" . DT  E 8   ? 0.8476 0.4932 0.3781 0.0678  0.2934 0.0187  8   DT  V "C1'" 
6470  N  N1    . DT  E 8   ? 0.8529 0.4873 0.3836 0.0612  0.2905 0.0143  8   DT  V N1    
6471  C  C2    . DT  E 8   ? 0.8607 0.4818 0.3851 0.0615  0.2938 0.0128  8   DT  V C2    
6472  O  O2    . DT  E 8   ? 0.8655 0.4827 0.3838 0.0672  0.2992 0.0145  8   DT  V O2    
6473  N  N3    . DT  E 8   ? 0.8617 0.4744 0.3873 0.0549  0.2906 0.0091  8   DT  V N3    
6474  C  C4    . DT  E 8   ? 0.8565 0.4725 0.3887 0.0485  0.2847 0.007   8   DT  V C4    
6475  O  O4    . DT  E 8   ? 0.8577 0.4657 0.3903 0.0432  0.2824 0.0042  8   DT  V O4    
6476  C  C5    . DT  E 8   ? 0.8501 0.4792 0.3879 0.0487  0.2818 0.0087  8   DT  V C5    
6477  C  C7    . DT  E 8   ? 0.846  0.4792 0.3906 0.0422  0.2756 0.0066  8   DT  V C7    
6478  C  C6    . DT  E 8   ? 0.8486 0.4863 0.3855 0.0548  0.2847 0.0122  8   DT  V C6    
6479  P  P     . DT  E 9   ? 0.8629 0.5238 0.3804 0.088   0.3064 0.0326  9   DT  V P     
6480  O  OP1   . DT  E 9   ? 0.8618 0.5336 0.379  0.0958  0.3104 0.0377  9   DT  V OP1   
6481  O  OP2   . DT  E 9   ? 0.8632 0.5247 0.3818 0.0841  0.3035 0.0323  9   DT  V OP2   
6482  O  "O5'" . DT  E 9   ? 0.8726 0.5133 0.3792 0.0888  0.3111 0.0303  9   DT  V "O5'" 
6483  C  "C5'" . DT  E 9   ? 0.8736 0.5096 0.3766 0.0927  0.315  0.0304  9   DT  V "C5'" 
6484  C  "C4'" . DT  E 9   ? 0.8821 0.4981 0.3747 0.0917  0.3185 0.0277  9   DT  V "C4'" 
6485  O  "O4'" . DT  E 9   ? 0.8812 0.4912 0.3779 0.0829  0.313  0.0229  9   DT  V "O4'" 
6486  C  "C3'" . DT  E 9   ? 0.891  0.4953 0.3712 0.0955  0.324  0.0297  9   DT  V "C3'" 
6487  O  "O3'" . DT  E 9   ? 0.9052 0.4959 0.3746 0.0999  0.3304 0.03    9   DT  V "O3'" 
6488  C  "C2'" . DT  E 9   ? 0.8916 0.4871 0.3717 0.0874  0.3196 0.0258  9   DT  V "C2'" 
6489  C  "C1'" . DT  E 9   ? 0.8904 0.4845 0.3772 0.0813  0.3152 0.0215  9   DT  V "C1'" 
6490  N  N1    . DT  E 9   ? 0.893  0.4849 0.3849 0.0725  0.3089 0.0177  9   DT  V N1    
6491  C  C2    . DT  E 9   ? 0.9004 0.4788 0.389  0.0674  0.3081 0.0141  9   DT  V C2    
6492  O  O2    . DT  E 9   ? 0.9081 0.4758 0.3894 0.0693  0.3123 0.0137  9   DT  V O2    
6493  N  N3    . DT  E 9   ? 0.8998 0.4777 0.3936 0.0597  0.3021 0.0111  9   DT  V N3    
6494  C  C4    . DT  E 9   ? 0.8948 0.4834 0.3963 0.0569  0.2972 0.0111  9   DT  V C4    
6495  O  O4    . DT  E 9   ? 0.8947 0.4811 0.3999 0.0501  0.2923 0.0083  9   DT  V O4    
6496  C  C5    . DT  E 9   ? 0.8887 0.4907 0.3931 0.0623  0.2984 0.0149  9   DT  V C5    
6497  C  C7    . DT  E 9   ? 0.8808 0.495  0.3933 0.0595  0.2934 0.0153  9   DT  V C7    
6498  C  C6    . DT  E 9   ? 0.889  0.4924 0.3888 0.0698  0.304  0.0181  9   DT  V C6    
6499  P  P     . DC  E 10  ? 0.9214 0.4977 0.3749 0.1058  0.3381 0.0326  10  DC  V P     
6500  O  OP1   . DC  E 10  ? 0.9241 0.5022 0.3724 0.1151  0.345  0.0367  10  DC  V OP1   
6501  O  OP2   . DC  E 10  ? 0.9231 0.5022 0.3763 0.1051  0.3368 0.0341  10  DC  V OP2   
6502  O  "O5'" . DC  E 10  ? 0.9302 0.4857 0.3752 0.1002  0.3386 0.0281  10  DC  V "O5'" 
6503  C  "C5'" . DC  E 10  ? 0.9295 0.4814 0.3772 0.0975  0.3377 0.0252  10  DC  V "C5'" 
6504  C  "C4'" . DC  E 10  ? 0.938  0.4717 0.3788 0.0907  0.337  0.021   10  DC  V "C4'" 
6505  O  "O4'" . DC  E 10  ? 0.9308 0.4682 0.3803 0.0821  0.3294 0.0178  10  DC  V "O4'" 
6506  C  "C3'" . DC  E 10  ? 0.9536 0.4689 0.3776 0.093   0.3428 0.0218  10  DC  V "C3'" 
6507  O  "O3'" . DC  E 10  ? 0.9671 0.4655 0.3826 0.0899  0.3451 0.0191  10  DC  V "O3'" 
6508  C  "C2'" . DC  E 10  ? 0.9497 0.4647 0.3753 0.0872  0.338  0.0204  10  DC  V "C2'" 
6509  C  "C1'" . DC  E 10  ? 0.9381 0.4621 0.3781 0.0789  0.3298 0.0167  10  DC  V "C1'" 
6510  N  N1    . DC  E 10  ? 0.9289 0.4625 0.3773 0.0746  0.3238 0.0161  10  DC  V N1    
6511  C  C2    . DC  E 10  ? 0.9283 0.4568 0.3795 0.0658  0.3181 0.0123  10  DC  V C2    
6512  O  O2    . DC  E 10  ? 0.9337 0.4498 0.3804 0.0616  0.3182 0.0096  10  DC  V O2    
6513  N  N3    . DC  E 10  ? 0.9222 0.4596 0.381  0.0621  0.3127 0.0118  10  DC  V N3    
6514  C  C4    . DC  E 10  ? 0.9148 0.4656 0.3782 0.0666  0.3129 0.0149  10  DC  V C4    
6515  N  N4    . DC  E 10  ? 0.9073 0.4659 0.3778 0.0626  0.3076 0.0143  10  DC  V N4    
6516  C  C5    . DC  E 10  ? 0.9151 0.4717 0.3759 0.0754  0.3184 0.019   10  DC  V C5    
6517  C  C6    . DC  E 10  ? 0.9216 0.4695 0.375  0.0793  0.3237 0.0195  10  DC  V C6    
6518  P  P     . DC  E 11  ? 0.9868 0.4634 0.3823 0.0932  0.3527 0.02    11  DC  V P     
6519  O  OP1   . DC  E 11  ? 0.9947 0.4612 0.384  0.0948  0.3571 0.0192  11  DC  V OP1   
6520  O  OP2   . DC  E 11  ? 0.9881 0.4676 0.3774 0.1013  0.3574 0.0246  11  DC  V OP2   
6521  O  "O5'" . DC  E 11  ? 1.0008 0.465  0.3925 0.0837  0.3482 0.0162  11  DC  V "O5'" 
6522  C  "C5'" . DC  E 11  ? 1.0115 0.4714 0.408  0.0749  0.3434 0.012   11  DC  V "C5'" 
6523  C  "C4'" . DC  E 11  ? 1.0267 0.4788 0.4212 0.0664  0.3385 0.0092  11  DC  V "C4'" 
6524  O  "O4'" . DC  E 11  ? 1.0187 0.4862 0.4251 0.0647  0.3327 0.0095  11  DC  V "O4'" 
6525  C  "C3'" . DC  E 11  ? 1.0507 0.4833 0.4265 0.0674  0.3433 0.0098  11  DC  V "C3'" 
6526  O  "O3'" . DC  E 11  ? 1.0724 0.491  0.4432 0.0581  0.3401 0.0062  11  DC  V "O3'" 
6527  C  "C2'" . DC  E 11  ? 1.0418 0.4831 0.4206 0.0693  0.3413 0.0117  11  DC  V "C2'" 
6528  C  "C1'" . DC  E 11  ? 1.0253 0.4834 0.4227 0.0629  0.3326 0.0094  11  DC  V "C1'" 
6529  N  N1    . DC  E 11  ? 1.0126 0.4861 0.4189 0.0647  0.3295 0.0113  11  DC  V N1    
6530  C  C2    . DC  E 11  ? 1.0053 0.4818 0.4178 0.0575  0.3227 0.009   11  DC  V C2    
6531  O  O2    . DC  E 11  ? 1.009  0.4762 0.4201 0.0498  0.3193 0.0056  11  DC  V O2    
6532  N  N3    . DC  E 11  ? 0.9944 0.4845 0.4148 0.059   0.32   0.0106  11  DC  V N3    
6533  C  C4    . DC  E 11  ? 0.9899 0.4907 0.4121 0.0671  0.3237 0.0145  11  DC  V C4    
6534  N  N4    . DC  E 11  ? 0.9809 0.4952 0.4111 0.0678  0.3207 0.0161  11  DC  V N4    
6535  C  C5    . DC  E 11  ? 0.9963 0.4946 0.4123 0.0747  0.3306 0.0171  11  DC  V C5    
6536  C  C6    . DC  E 11  ? 1.0065 0.4908 0.4144 0.0734  0.3334 0.0153  11  DC  V C6    
6537  P  P     . DT  E 12  ? 1.1023 0.4952 0.4512 0.0572  0.3456 0.0057  12  DT  V P     
6538  O  OP1   . DT  E 12  ? 1.1084 0.4917 0.4519 0.0569  0.3493 0.0048  12  DT  V OP1   
6539  O  OP2   . DT  E 12  ? 1.1057 0.4937 0.4429 0.065   0.3513 0.0091  12  DT  V OP2   
6540  O  "O5'" . DT  E 12  ? 1.1201 0.507  0.4698 0.046   0.3384 0.0022  12  DT  V "O5'" 
6541  C  "C5'" . DT  E 12  ? 1.1264 0.5245 0.4922 0.0381  0.3306 -0.0006 12  DT  V "C5'" 
6542  C  "C4'" . DT  E 12  ? 1.1374 0.5387 0.5083 0.031   0.3235 -0.0023 12  DT  V "C4'" 
6543  O  "O4'" . DT  E 12  ? 1.1318 0.5487 0.5115 0.0358  0.3221 -0.0003 12  DT  V "O4'" 
6544  C  "C3'" . DT  E 12  ? 1.1616 0.5429 0.5152 0.0272  0.3247 -0.0032 12  DT  V "C3'" 
6545  O  "O3'" . DT  E 12  ? 1.1747 0.5541 0.5326 0.0167  0.3175 -0.0063 12  DT  V "O3'" 
6546  C  "C2'" . DT  E 12  ? 1.1589 0.5441 0.5097 0.033   0.3262 -0.0008 12  DT  V "C2'" 
6547  C  "C1'" . DT  E 12  ? 1.1414 0.5507 0.5127 0.0344  0.3213 -0.0002 12  DT  V "C1'" 
6548  N  N1    . DT  E 12  ? 1.1395 0.5585 0.5119 0.0428  0.3243 0.0032  12  DT  V N1    
6549  C  C2    . DT  E 12  ? 1.1332 0.5646 0.5156 0.0412  0.3191 0.0033  12  DT  V C2    
6550  O  O2    . DT  E 12  ? 1.1285 0.5646 0.5198 0.0335  0.3121 0.0006  12  DT  V O2    
6551  N  N3    . DT  E 12  ? 1.1304 0.5701 0.5129 0.0491  0.3225 0.0068  12  DT  V N3    
6552  C  C4    . DT  E 12  ? 1.1328 0.5693 0.5062 0.0586  0.3305 0.0105  12  DT  V C4    
6553  O  O4    . DT  E 12  ? 1.1282 0.5741 0.5035 0.0649  0.3326 0.0139  12  DT  V O4    
6554  C  C5    . DT  E 12  ? 1.1401 0.5622 0.5022 0.0601  0.3359 0.0102  12  DT  V C5    
6555  C  C7    . DT  E 12  ? 1.1443 0.5614 0.4954 0.0705  0.345  0.0142  12  DT  V C7    
6556  C  C6    . DT  E 12  ? 1.1437 0.5574 0.5056 0.0521  0.3326 0.0065  12  DT  V C6    
6557  P  P     . DC  E 13  ? 1.2025 0.5591 0.5427 0.0098  0.3176 -0.008  13  DC  V P     
6558  O  OP1   . DC  E 13  ? 1.2018 0.5567 0.5473 0.0003  0.3127 -0.0107 13  DC  V OP1   
6559  O  OP2   . DC  E 13  ? 1.2161 0.5551 0.5362 0.0165  0.3265 -0.0062 13  DC  V OP2   
6560  O  "O5'" . DC  E 13  ? 1.2094 0.569  0.5508 0.0072  0.3128 -0.0083 13  DC  V "O5'" 
6561  C  "C5'" . DC  E 13  ? 1.2085 0.5785 0.5636 -0.001  0.3041 -0.0105 13  DC  V "C5'" 
6562  C  "C4'" . DC  E 13  ? 1.2114 0.5881 0.5696 -0.0002 0.3009 -0.0099 13  DC  V "C4'" 
6563  O  "O4'" . DC  E 13  ? 1.2071 0.5978 0.5725 0.0089  0.3039 -0.0073 13  DC  V "O4'" 
6564  C  "C3'" . DC  E 13  ? 1.2282 0.5867 0.5675 -0.0002 0.3037 -0.0096 13  DC  V "C3'" 
6565  O  "O3'" . DC  E 13  ? 1.2349 0.5836 0.5699 -0.0104 0.2982 -0.0122 13  DC  V "O3'" 
6566  C  "C2'" . DC  E 13  ? 1.2243 0.5945 0.5694 0.0051  0.3031 -0.0078 13  DC  V "C2'" 
6567  C  "C1'" . DC  E 13  ? 1.214  0.6039 0.5746 0.0115  0.3042 -0.0061 13  DC  V "C1'" 
6568  N  N1    . DC  E 13  ? 1.2229 0.6128 0.5768 0.0222  0.3119 -0.0025 13  DC  V N1    
6569  C  C2    . DC  E 13  ? 1.2221 0.624  0.5817 0.0274  0.3119 -0.0002 13  DC  V C2    
6570  O  O2    . DC  E 13  ? 1.2185 0.6302 0.5883 0.0231  0.3056 -0.0014 13  DC  V O2    
6571  N  N3    . DC  E 13  ? 1.2242 0.627  0.578  0.0372  0.3189 0.0034  13  DC  V N3    
6572  C  C4    . DC  E 13  ? 1.231  0.6229 0.5735 0.0421  0.3259 0.0047  13  DC  V C4    
6573  N  N4    . DC  E 13  ? 1.2323 0.6263 0.5697 0.0521  0.3328 0.0088  13  DC  V N4    
6574  C  C5    . DC  E 13  ? 1.2363 0.6149 0.5721 0.0368  0.3262 0.0022  13  DC  V C5    
6575  C  C6    . DC  E 13  ? 1.2326 0.6109 0.5746 0.0268  0.319  -0.0014 13  DC  V C6    
6576  N  N     . MET F 1   ? 0.6568 0.2039 0.1502 -0.0393 0.2171 -0.0174 1   MET Z N     
6577  C  CA    . MET F 1   ? 0.6531 0.2141 0.1566 -0.0396 0.2148 -0.0177 1   MET Z CA    
6578  C  C     . MET F 1   ? 0.6499 0.217  0.1659 -0.0338 0.217  -0.0163 1   MET Z C     
6579  O  O     . MET F 1   ? 0.6539 0.2144 0.1697 -0.029  0.2205 -0.015  1   MET Z O     
6580  C  CB    . MET F 1   ? 0.6618 0.2225 0.159  -0.0412 0.2136 -0.0182 1   MET Z CB    
6581  C  CG    . MET F 1   ? 0.6737 0.2485 0.1804 -0.0412 0.2115 -0.0182 1   MET Z CG    
6582  S  SD    . MET F 1   ? 0.6844 0.2603 0.1838 -0.0435 0.2097 -0.0185 1   MET Z SD    
6583  C  CE    . MET F 1   ? 0.6452 0.2094 0.1397 -0.0375 0.2142 -0.0176 1   MET Z CE    
6584  N  N     . ASN F 2   ? 0.6413 0.2209 0.168  -0.0341 0.2151 -0.0166 2   ASN Z N     
6585  C  CA    . ASN F 2   ? 0.6422 0.228  0.1803 -0.0294 0.2168 -0.0155 2   ASN Z CA    
6586  C  C     . ASN F 2   ? 0.6437 0.2379 0.1857 -0.029  0.2158 -0.0157 2   ASN Z C     
6587  O  O     . ASN F 2   ? 0.6459 0.2466 0.1871 -0.0329 0.2128 -0.0166 2   ASN Z O     
6588  C  CB    . ASN F 2   ? 0.6476 0.2396 0.1945 -0.0297 0.2159 -0.0154 2   ASN Z CB    
6589  C  CG    . ASN F 2   ? 0.6857 0.2705 0.2321 -0.0274 0.2181 -0.0142 2   ASN Z CG    
6590  O  OD1   . ASN F 2   ? 0.7043 0.2814 0.2477 -0.0238 0.2213 -0.0129 2   ASN Z OD1   
6591  N  ND2   . ASN F 2   ? 0.69   0.2772 0.2395 -0.0293 0.2167 -0.0145 2   ASN Z ND2   
6592  N  N     . VAL F 3   ? 0.639  0.2331 0.1848 -0.0244 0.2184 -0.0147 3   VAL Z N     
6593  C  CA    . VAL F 3   ? 0.6403 0.2416 0.1893 -0.0234 0.2179 -0.0148 3   VAL Z CA    
6594  C  C     . VAL F 3   ? 0.6355 0.2445 0.1962 -0.0202 0.2189 -0.0141 3   VAL Z C     
6595  O  O     . VAL F 3   ? 0.6343 0.2405 0.1996 -0.0168 0.2214 -0.0131 3   VAL Z O     
6596  C  CB    . VAL F 3   ? 0.6558 0.2504 0.1979 -0.021  0.2199 -0.0144 3   VAL Z CB    
6597  C  CG1   . VAL F 3   ? 0.6593 0.2617 0.2049 -0.0197 0.2195 -0.0144 3   VAL Z CG1   
6598  C  CG2   . VAL F 3   ? 0.6697 0.2561 0.199  -0.0249 0.2185 -0.0152 3   VAL Z CG2   
6599  N  N     . PHE F 4   ? 0.6317 0.2502 0.1968 -0.0214 0.2171 -0.0146 4   PHE Z N     
6600  C  CA    . PHE F 4   ? 0.6344 0.2598 0.2092 -0.0188 0.218  -0.0141 4   PHE Z CA    
6601  C  C     . PHE F 4   ? 0.637  0.2672 0.2125 -0.0169 0.2185 -0.0139 4   PHE Z C     
6602  O  O     . PHE F 4   ? 0.6402 0.2719 0.21   -0.0188 0.2169 -0.0142 4   PHE Z O     
6603  C  CB    . PHE F 4   ? 0.6323 0.2645 0.2116 -0.0216 0.2155 -0.0146 4   PHE Z CB    
6604  C  CG    . PHE F 4   ? 0.6443 0.2724 0.2226 -0.0238 0.2147 -0.0149 4   PHE Z CG    
6605  C  CD1   . PHE F 4   ? 0.6546 0.2802 0.238  -0.0217 0.2162 -0.0141 4   PHE Z CD1   
6606  C  CD2   . PHE F 4   ? 0.6571 0.2838 0.2291 -0.0281 0.2123 -0.0158 4   PHE Z CD2   
6607  C  CE1   . PHE F 4   ? 0.6656 0.2876 0.2478 -0.0234 0.2155 -0.0142 4   PHE Z CE1   
6608  C  CE2   . PHE F 4   ? 0.6681 0.2905 0.2386 -0.0299 0.2118 -0.016  4   PHE Z CE2   
6609  C  CZ    . PHE F 4   ? 0.6652 0.2853 0.2408 -0.0273 0.2134 -0.0152 4   PHE Z CZ    
6610  N  N     . ARG F 5   ? 0.6339 0.2667 0.2161 -0.0132 0.2206 -0.0132 5   ARG Z N     
6611  C  CA    . ARG F 5   ? 0.6389 0.2763 0.222  -0.011  0.2215 -0.0129 5   ARG Z CA    
6612  C  C     . ARG F 5   ? 0.6421 0.2872 0.2319 -0.0105 0.2212 -0.0128 5   ARG Z C     
6613  O  O     . ARG F 5   ? 0.6449 0.2899 0.2403 -0.01   0.2219 -0.0127 5   ARG Z O     
6614  C  CB    . ARG F 5   ? 0.6568 0.2888 0.2397 -0.0066 0.2249 -0.0121 5   ARG Z CB    
6615  C  CG    . ARG F 5   ? 0.701  0.3257 0.2751 -0.0068 0.2252 -0.0121 5   ARG Z CG    
6616  C  CD    . ARG F 5   ? 0.7457 0.3639 0.3198 -0.0022 0.2289 -0.0111 5   ARG Z CD    
6617  N  NE    . ARG F 5   ? 0.7901 0.401  0.3548 -0.0021 0.2294 -0.0112 5   ARG Z NE    
6618  C  CZ    . ARG F 5   ? 0.8144 0.4198 0.3768 0.0018  0.2324 -0.0104 5   ARG Z CZ    
6619  N  NH1   . ARG F 5   ? 0.8044 0.4113 0.3737 0.0058  0.2353 -0.0095 5   ARG Z NH1   
6620  N  NH2   . ARG F 5   ? 0.8181 0.4161 0.3708 0.0016  0.2326 -0.0105 5   ARG Z NH2   
6621  N  N     . ILE F 6   ? 0.6399 0.2917 0.2288 -0.0107 0.2203 -0.0126 6   ILE Z N     
6622  C  CA    . ILE F 6   ? 0.6416 0.3003 0.2357 -0.0098 0.2205 -0.0123 6   ILE Z CA    
6623  C  C     . ILE F 6   ? 0.6463 0.3063 0.2411 -0.0056 0.2231 -0.0116 6   ILE Z C     
6624  O  O     . ILE F 6   ? 0.6471 0.3104 0.2383 -0.0051 0.2227 -0.0111 6   ILE Z O     
6625  C  CB    . ILE F 6   ? 0.6457 0.3119 0.2386 -0.013  0.2176 -0.0123 6   ILE Z CB    
6626  C  CG1   . ILE F 6   ? 0.6558 0.3201 0.2469 -0.0174 0.215  -0.0131 6   ILE Z CG1   
6627  C  CG2   . ILE F 6   ? 0.6493 0.3216 0.2471 -0.0115 0.2183 -0.0118 6   ILE Z CG2   
6628  C  CD1   . ILE F 6   ? 0.6694 0.3306 0.2647 -0.0177 0.2153 -0.0136 6   ILE Z CD1   
6629  N  N     . HIS F 7   ? 0.6483 0.3057 0.2476 -0.0027 0.2257 -0.0113 7   HIS Z N     
6630  C  CA    . HIS F 7   ? 0.6566 0.3144 0.2566 0.0014  0.2286 -0.0106 7   HIS Z CA    
6631  C  C     . HIS F 7   ? 0.6596 0.3234 0.2625 0.0021  0.2289 -0.0103 7   HIS Z C     
6632  O  O     . HIS F 7   ? 0.6624 0.326  0.2689 0.0009  0.2287 -0.0106 7   HIS Z O     
6633  C  CB    . HIS F 7   ? 0.6678 0.3192 0.271  0.0039  0.2315 -0.0104 7   HIS Z CB    
6634  C  CG    . HIS F 7   ? 0.6995 0.3443 0.2998 0.0038  0.2318 -0.0104 7   HIS Z CG    
6635  N  ND1   . HIS F 7   ? 0.7244 0.3655 0.321  0.0065  0.2337 -0.0099 7   HIS Z ND1   
6636  C  CD2   . HIS F 7   ? 0.7132 0.3542 0.3134 0.0015  0.2306 -0.0106 7   HIS Z CD2   
6637  C  CE1   . HIS F 7   ? 0.7314 0.3662 0.3256 0.0059  0.2338 -0.0099 7   HIS Z CE1   
6638  N  NE2   . HIS F 7   ? 0.7283 0.3629 0.3245 0.003   0.232  -0.0102 7   HIS Z NE2   
6639  N  N     . GLY F 8   ? 0.6549 0.324  0.2557 0.0039  0.2294 -0.0095 8   GLY Z N     
6640  C  CA    . GLY F 8   ? 0.654  0.3285 0.2566 0.0051  0.2301 -0.0088 8   GLY Z CA    
6641  C  C     . GLY F 8   ? 0.6552 0.3311 0.2568 0.0097  0.2332 -0.0077 8   GLY Z C     
6642  O  O     . GLY F 8   ? 0.6617 0.335  0.2614 0.0119  0.2346 -0.0076 8   GLY Z O     
6643  N  N     . ASP F 9   ? 0.6483 0.3279 0.2509 0.0115  0.2346 -0.0069 9   ASP Z N     
6644  C  CA    . ASP F 9   ? 0.6479 0.3289 0.249  0.0163  0.238  -0.0057 9   ASP Z CA    
6645  C  C     . ASP F 9   ? 0.638  0.3256 0.2358 0.0172  0.2369 -0.0045 9   ASP Z C     
6646  O  O     . ASP F 9   ? 0.6403 0.3272 0.2361 0.0206  0.2389 -0.0038 9   ASP Z O     
6647  C  CB    . ASP F 9   ? 0.6733 0.3566 0.275  0.018   0.2397 -0.0049 9   ASP Z CB    
6648  C  CG    . ASP F 9   ? 0.7425 0.4195 0.3466 0.017   0.2408 -0.0059 9   ASP Z CG    
6649  O  OD1   . ASP F 9   ? 0.7548 0.4254 0.3603 0.0177  0.2425 -0.0066 9   ASP Z OD1   
6650  O  OD2   . ASP F 9   ? 0.773  0.4516 0.3775 0.0156  0.2401 -0.0058 9   ASP Z OD2   
6651  N  N     . ASN F 10  ? 0.6238 0.3179 0.221  0.0139  0.2335 -0.004  10  ASN Z N     
6652  C  CA    . ASN F 10  ? 0.6178 0.3194 0.2121 0.0136  0.2316 -0.0026 10  ASN Z CA    
6653  C  C     . ASN F 10  ? 0.6103 0.3153 0.204  0.0079  0.2272 -0.0031 10  ASN Z C     
6654  O  O     . ASN F 10  ? 0.6178 0.319  0.2133 0.0049  0.226  -0.0045 10  ASN Z O     
6655  C  CB    . ASN F 10  ? 0.6284 0.3379 0.2225 0.0174  0.2335 -0.0002 10  ASN Z CB    
6656  C  CG    . ASN F 10  ? 0.6681 0.3794 0.2645 0.0178  0.2346 0.0003  10  ASN Z CG    
6657  O  OD1   . ASN F 10  ? 0.6837 0.3909 0.2806 0.0212  0.2381 0.0003  10  ASN Z OD1   
6658  N  ND2   . ASN F 10  ? 0.6808 0.3979 0.2781 0.0143  0.2316 0.0007  10  ASN Z ND2   
6659  N  N     . ILE F 11  ? 0.594  0.306  0.185  0.0063  0.2248 -0.0018 11  ILE Z N     
6660  C  CA    . ILE F 11  ? 0.5852 0.3001 0.1749 0.0006  0.2206 -0.0022 11  ILE Z CA    
6661  C  C     . ILE F 11  ? 0.5742 0.2936 0.1671 -0.0014 0.2196 -0.0018 11  ILE Z C     
6662  O  O     . ILE F 11  ? 0.5778 0.295  0.1707 -0.0059 0.217  -0.0031 11  ILE Z O     
6663  C  CB    . ILE F 11  ? 0.587  0.3092 0.1729 -0.0011 0.218  -0.0006 11  ILE Z CB    
6664  C  CG1   . ILE F 11  ? 0.5986 0.321  0.1818 -0.0077 0.2137 -0.0015 11  ILE Z CG1   
6665  C  CG2   . ILE F 11  ? 0.586  0.3201 0.1736 0.0015  0.2186 0.0024  11  ILE Z CG2   
6666  C  CD1   . ILE F 11  ? 0.6202 0.3307 0.2011 -0.0099 0.2134 -0.0041 11  ILE Z CD1   
6667  N  N     . ILE F 12  ? 0.5599 0.2847 0.1552 0.0021  0.2218 -0.0001 12  ILE Z N     
6668  C  CA    . ILE F 12  ? 0.5527 0.2815 0.1505 0.0008  0.2213 0.0005  12  ILE Z CA    
6669  C  C     . ILE F 12  ? 0.5578 0.2777 0.1574 -0.0007 0.2215 -0.0019 12  ILE Z C     
6670  O  O     . ILE F 12  ? 0.5604 0.2811 0.1609 -0.0046 0.2192 -0.0025 12  ILE Z O     
6671  C  CB    . ILE F 12  ? 0.5499 0.2856 0.1487 0.0057  0.2242 0.0032  12  ILE Z CB    
6672  C  CG1   . ILE F 12  ? 0.5565 0.3047 0.1549 0.0049  0.2223 0.0062  12  ILE Z CG1   
6673  C  CG2   . ILE F 12  ? 0.5558 0.2889 0.1565 0.0072  0.2263 0.0031  12  ILE Z CG2   
6674  C  CD1   . ILE F 12  ? 0.5736 0.3274 0.1734 0.0004  0.2193 0.0067  12  ILE Z CD1   
6675  N  N     . GLU F 13  ? 0.5572 0.2689 0.1575 0.0019  0.2242 -0.0031 13  GLU Z N     
6676  C  CA    . GLU F 13  ? 0.5605 0.2644 0.1629 0.0004  0.2244 -0.0051 13  GLU Z CA    
6677  C  C     . GLU F 13  ? 0.5577 0.258  0.1594 -0.0042 0.2213 -0.0067 13  GLU Z C     
6678  O  O     . GLU F 13  ? 0.5544 0.2529 0.1576 -0.007  0.2198 -0.0076 13  GLU Z O     
6679  C  CB    . GLU F 13  ? 0.5902 0.2867 0.1935 0.0039  0.2277 -0.0057 13  GLU Z CB    
6680  C  CG    . GLU F 13  ? 0.652  0.3506 0.2545 0.009   0.2313 -0.0042 13  GLU Z CG    
6681  C  CD    . GLU F 13  ? 0.737  0.4371 0.34   0.0105  0.233  -0.0033 13  GLU Z CD    
6682  O  OE1   . GLU F 13  ? 0.769  0.4649 0.3736 0.0083  0.2324 -0.0045 13  GLU Z OE1   
6683  O  OE2   . GLU F 13  ? 0.7538 0.459  0.3553 0.0141  0.2351 -0.0013 13  GLU Z OE2   
6684  N  N     . CYS F 14  ? 0.5588 0.2577 0.1577 -0.0047 0.2205 -0.0069 14  CYS Z N     
6685  C  CA    . CYS F 14  ? 0.567  0.2613 0.1638 -0.0087 0.218  -0.0083 14  CYS Z CA    
6686  C  C     . CYS F 14  ? 0.5703 0.2698 0.1662 -0.0133 0.2146 -0.0081 14  CYS Z C     
6687  O  O     . CYS F 14  ? 0.5739 0.2696 0.1701 -0.0165 0.2131 -0.0093 14  CYS Z O     
6688  C  CB    . CYS F 14  ? 0.5765 0.2682 0.1691 -0.0081 0.218  -0.0083 14  CYS Z CB    
6689  S  SG    . CYS F 14  ? 0.609  0.2944 0.2025 -0.0026 0.2222 -0.0083 14  CYS Z SG    
6690  N  N     . GLU F 15  ? 0.5668 0.2755 0.1619 -0.0135 0.2136 -0.0063 15  GLU Z N     
6691  C  CA    . GLU F 15  ? 0.5698 0.2847 0.1641 -0.0179 0.2105 -0.0057 15  GLU Z CA    
6692  C  C     . GLU F 15  ? 0.5723 0.2881 0.17   -0.0188 0.2104 -0.0059 15  GLU Z C     
6693  O  O     . GLU F 15  ? 0.5766 0.2934 0.1736 -0.0231 0.2079 -0.0064 15  GLU Z O     
6694  C  CB    . GLU F 15  ? 0.5954 0.3211 0.1887 -0.0177 0.2096 -0.0033 15  GLU Z CB    
6695  C  CG    . GLU F 15  ? 0.6674 0.3926 0.2561 -0.019  0.2082 -0.0032 15  GLU Z CG    
6696  C  CD    . GLU F 15  ? 0.7734 0.4947 0.3577 -0.025  0.2048 -0.0046 15  GLU Z CD    
6697  O  OE1   . GLU F 15  ? 0.7975 0.5193 0.3827 -0.0286 0.2031 -0.0051 15  GLU Z OE1   
6698  O  OE2   . GLU F 15  ? 0.8057 0.5228 0.385  -0.026  0.204  -0.0051 15  GLU Z OE2   
6699  N  N     . ARG F 16  ? 0.5683 0.2829 0.169  -0.0149 0.2133 -0.0057 16  ARG Z N     
6700  C  CA    . ARG F 16  ? 0.5681 0.2825 0.1713 -0.0156 0.2133 -0.0059 16  ARG Z CA    
6701  C  C     . ARG F 16  ? 0.5673 0.274  0.1707 -0.0189 0.2118 -0.0081 16  ARG Z C     
6702  O  O     . ARG F 16  ? 0.571  0.2788 0.1751 -0.0216 0.2102 -0.0084 16  ARG Z O     
6703  C  CB    . ARG F 16  ? 0.5886 0.3019 0.1937 -0.0109 0.2168 -0.0053 16  ARG Z CB    
6704  C  CG    . ARG F 16  ? 0.6381 0.3601 0.2428 -0.0077 0.2183 -0.0026 16  ARG Z CG    
6705  C  CD    . ARG F 16  ? 0.697  0.4192 0.3027 -0.0047 0.2208 -0.0016 16  ARG Z CD    
6706  N  NE    . ARG F 16  ? 0.751  0.4664 0.3564 -0.0008 0.2242 -0.0022 16  ARG Z NE    
6707  C  CZ    . ARG F 16  ? 0.7843 0.5018 0.3886 0.004   0.2275 -0.0005 16  ARG Z CZ    
6708  N  NH1   . ARG F 16  ? 0.7803 0.5072 0.3839 0.0058  0.2279 0.0023  16  ARG Z NH1   
6709  N  NH2   . ARG F 16  ? 0.7863 0.4966 0.39   0.007   0.2306 -0.0012 16  ARG Z NH2   
6710  N  N     . VAL F 17  ? 0.5626 0.2619 0.1653 -0.0185 0.2123 -0.0095 17  VAL Z N     
6711  C  CA    . VAL F 17  ? 0.5675 0.2598 0.1703 -0.0212 0.2111 -0.0112 17  VAL Z CA    
6712  C  C     . VAL F 17  ? 0.5743 0.2676 0.1737 -0.0258 0.2081 -0.0116 17  VAL Z C     
6713  O  O     . VAL F 17  ? 0.5742 0.2655 0.1737 -0.0287 0.2065 -0.0124 17  VAL Z O     
6714  C  CB    . VAL F 17  ? 0.5747 0.2594 0.1777 -0.019  0.2129 -0.012  17  VAL Z CB    
6715  C  CG1   . VAL F 17  ? 0.583  0.2609 0.1851 -0.0216 0.2117 -0.0132 17  VAL Z CG1   
6716  C  CG2   . VAL F 17  ? 0.5784 0.2612 0.185  -0.0155 0.2156 -0.0118 17  VAL Z CG2   
6717  N  N     . ILE F 18  ? 0.5768 0.2732 0.1726 -0.0267 0.2071 -0.0109 18  ILE Z N     
6718  C  CA    . ILE F 18  ? 0.5834 0.2808 0.175  -0.0316 0.2042 -0.0111 18  ILE Z CA    
6719  C  C     . ILE F 18  ? 0.5824 0.2869 0.1755 -0.0343 0.2024 -0.0103 18  ILE Z C     
6720  O  O     . ILE F 18  ? 0.5812 0.2834 0.1725 -0.0382 0.2005 -0.0112 18  ILE Z O     
6721  C  CB    . ILE F 18  ? 0.5907 0.2908 0.1782 -0.032  0.2035 -0.0103 18  ILE Z CB    
6722  C  CG1   . ILE F 18  ? 0.6067 0.2987 0.1922 -0.0291 0.2055 -0.0111 18  ILE Z CG1   
6723  C  CG2   . ILE F 18  ? 0.5981 0.299  0.1803 -0.0377 0.2002 -0.0104 18  ILE Z CG2   
6724  C  CD1   . ILE F 18  ? 0.6252 0.3068 0.2083 -0.0305 0.2055 -0.0127 18  ILE Z CD1   
6725  N  N     . ASP F 19  ? 0.5837 0.2962 0.1799 -0.0318 0.2034 -0.0086 19  ASP Z N     
6726  C  CA    . ASP F 19  ? 0.5923 0.3121 0.1902 -0.0336 0.2023 -0.0073 19  ASP Z CA    
6727  C  C     . ASP F 19  ? 0.5957 0.3107 0.1955 -0.0346 0.2022 -0.0087 19  ASP Z C     
6728  O  O     . ASP F 19  ? 0.5954 0.3131 0.1948 -0.0381 0.2003 -0.0085 19  ASP Z O     
6729  C  CB    . ASP F 19  ? 0.6147 0.3433 0.2152 -0.0298 0.2041 -0.0048 19  ASP Z CB    
6730  C  CG    . ASP F 19  ? 0.6758 0.4113 0.2746 -0.0292 0.2037 -0.0031 19  ASP Z CG    
6731  O  OD1   . ASP F 19  ? 0.6911 0.4255 0.2863 -0.0329 0.2013 -0.0036 19  ASP Z OD1   
6732  O  OD2   . ASP F 19  ? 0.7022 0.4436 0.3027 -0.0251 0.2058 -0.001  19  ASP Z OD2   
6733  N  N     . LEU F 20  ? 0.5957 0.3036 0.1973 -0.0319 0.2041 -0.0099 20  LEU Z N     
6734  C  CA    . LEU F 20  ? 0.6014 0.3042 0.2046 -0.0328 0.2039 -0.0112 20  LEU Z CA    
6735  C  C     . LEU F 20  ? 0.6077 0.3054 0.2081 -0.037  0.2016 -0.0126 20  LEU Z C     
6736  O  O     . LEU F 20  ? 0.613  0.3109 0.2133 -0.0397 0.2002 -0.013  20  LEU Z O     
6737  C  CB    . LEU F 20  ? 0.6092 0.3057 0.2148 -0.0294 0.2061 -0.012  20  LEU Z CB    
6738  C  CG    . LEU F 20  ? 0.6354 0.3344 0.2432 -0.0256 0.2085 -0.0109 20  LEU Z CG    
6739  C  CD1   . LEU F 20  ? 0.6431 0.3356 0.2526 -0.0228 0.2106 -0.0117 20  LEU Z CD1   
6740  C  CD2   . LEU F 20  ? 0.6477 0.3488 0.2563 -0.0265 0.208  -0.0105 20  LEU Z CD2   
6741  N  N     . ILE F 21  ? 0.604  0.2969 0.2017 -0.0374 0.2016 -0.0133 21  ILE Z N     
6742  C  CA    . ILE F 21  ? 0.6065 0.2932 0.2002 -0.0409 0.2    -0.0146 21  ILE Z CA    
6743  C  C     . ILE F 21  ? 0.6059 0.2973 0.1963 -0.0455 0.1975 -0.0142 21  ILE Z C     
6744  O  O     . ILE F 21  ? 0.6063 0.2952 0.1955 -0.0485 0.1962 -0.0149 21  ILE Z O     
6745  C  CB    . ILE F 21  ? 0.6157 0.2963 0.2062 -0.0397 0.201  -0.015  21  ILE Z CB    
6746  C  CG1   . ILE F 21  ? 0.6266 0.3019 0.2207 -0.0357 0.2035 -0.0154 21  ILE Z CG1   
6747  C  CG2   . ILE F 21  ? 0.6256 0.3    0.2101 -0.0434 0.1995 -0.016  21  ILE Z CG2   
6748  C  CD1   . ILE F 21  ? 0.643  0.3139 0.2351 -0.0334 0.205  -0.0153 21  ILE Z CD1   
6749  N  N     . LEU F 22  ? 0.6051 0.3036 0.1943 -0.0461 0.1968 -0.0128 22  LEU Z N     
6750  C  CA    . LEU F 22  ? 0.6159 0.3204 0.2022 -0.0508 0.1943 -0.012  22  LEU Z CA    
6751  C  C     . LEU F 22  ? 0.6307 0.3409 0.22   -0.0521 0.1935 -0.0112 22  LEU Z C     
6752  O  O     . LEU F 22  ? 0.6313 0.3443 0.2183 -0.0567 0.1913 -0.0109 22  LEU Z O     
6753  C  CB    . LEU F 22  ? 0.6136 0.326  0.1993 -0.0501 0.194  -0.0102 22  LEU Z CB    
6754  C  CG    . LEU F 22  ? 0.6318 0.3408 0.2113 -0.0526 0.1927 -0.0106 22  LEU Z CG    
6755  C  CD1   . LEU F 22  ? 0.6405 0.3504 0.215  -0.0592 0.1896 -0.0106 22  LEU Z CD1   
6756  C  CD2   . LEU F 22  ? 0.643  0.3403 0.22   -0.0506 0.1943 -0.0124 22  LEU Z CD2   
6757  N  N     . SER F 23  ? 0.6401 0.3517 0.2343 -0.0483 0.1954 -0.0108 23  SER Z N     
6758  C  CA    . SER F 23  ? 0.6541 0.3701 0.2508 -0.0491 0.1951 -0.0101 23  SER Z CA    
6759  C  C     . SER F 23  ? 0.6698 0.3791 0.2649 -0.0522 0.1938 -0.0118 23  SER Z C     
6760  O  O     . SER F 23  ? 0.6738 0.3866 0.2693 -0.0545 0.1928 -0.0113 23  SER Z O     
6761  C  CB    . SER F 23  ? 0.6721 0.3895 0.2729 -0.0441 0.1976 -0.0093 23  SER Z CB    
6762  O  OG    . SER F 23  ? 0.705  0.4139 0.307  -0.0424 0.1986 -0.0111 23  SER Z OG    
6763  N  N     . LYS F 24  ? 0.6787 0.3785 0.272  -0.052  0.1941 -0.0137 24  LYS Z N     
6764  C  CA    . LYS F 24  ? 0.6956 0.3888 0.2872 -0.0544 0.1932 -0.0151 24  LYS Z CA    
6765  C  C     . LYS F 24  ? 0.7142 0.402  0.2997 -0.0583 0.1918 -0.0161 24  LYS Z C     
6766  O  O     . LYS F 24  ? 0.7179 0.4031 0.3004 -0.0619 0.1905 -0.0167 24  LYS Z O     
6767  C  CB    . LYS F 24  ? 0.7171 0.4038 0.3117 -0.0511 0.1948 -0.0161 24  LYS Z CB    
6768  C  CG    . LYS F 24  ? 0.7646 0.4505 0.3611 -0.0515 0.1944 -0.0165 24  LYS Z CG    
6769  C  CD    . LYS F 24  ? 0.8251 0.5064 0.4179 -0.0554 0.1928 -0.0175 24  LYS Z CD    
6770  C  CE    . LYS F 24  ? 0.8743 0.5536 0.4688 -0.0555 0.1925 -0.018  24  LYS Z CE    
6771  N  NZ    . LYS F 24  ? 0.904  0.5769 0.4947 -0.0583 0.1915 -0.0191 24  LYS Z NZ    
6772  N  N     . ILE F 25  ? 0.7251 0.4106 0.308  -0.0575 0.1923 -0.0162 25  ILE Z N     
6773  C  CA    . ILE F 25  ? 0.7462 0.4257 0.322  -0.061  0.1913 -0.017  25  ILE Z CA    
6774  C  C     . ILE F 25  ? 0.753  0.4397 0.3259 -0.0654 0.189  -0.0159 25  ILE Z C     
6775  O  O     . ILE F 25  ? 0.7513 0.4463 0.3268 -0.0641 0.189  -0.0144 25  ILE Z O     
6776  C  CB    . ILE F 25  ? 0.7642 0.4385 0.3382 -0.0582 0.1928 -0.0172 25  ILE Z CB    
6777  C  CG1   . ILE F 25  ? 0.7833 0.4507 0.3603 -0.0541 0.195  -0.0179 25  ILE Z CG1   
6778  C  CG2   . ILE F 25  ? 0.7768 0.4449 0.3421 -0.0618 0.1918 -0.0178 25  ILE Z CG2   
6779  C  CD1   . ILE F 25  ? 0.8064 0.4653 0.3804 -0.0555 0.195  -0.019  25  ILE Z CD1   
6780  N  N     . ASN F 26  ? 0.7597 0.4433 0.3272 -0.0706 0.1873 -0.0165 26  ASN Z N     
6781  C  CA    . ASN F 26  ? 0.7675 0.4576 0.3316 -0.0756 0.1848 -0.0154 26  ASN Z CA    
6782  C  C     . ASN F 26  ? 0.7684 0.4497 0.3236 -0.0785 0.1842 -0.0165 26  ASN Z C     
6783  O  O     . ASN F 26  ? 0.7744 0.4467 0.3236 -0.0815 0.1839 -0.0178 26  ASN Z O     
6784  C  CB    . ASN F 26  ? 0.7931 0.4854 0.3568 -0.0799 0.1833 -0.0153 26  ASN Z CB    
6785  C  CG    . ASN F 26  ? 0.842  0.546  0.4066 -0.0837 0.1812 -0.0132 26  ASN Z CG    
6786  O  OD1   . ASN F 26  ? 0.8631 0.5715 0.4254 -0.0855 0.18   -0.0122 26  ASN Z OD1   
6787  N  ND2   . ASN F 26  ? 0.845  0.5546 0.413  -0.085  0.1807 -0.0124 26  ASN Z ND2   
6788  N  N     . PRO F 27  ? 0.7615 0.4441 0.3155 -0.077  0.1844 -0.0159 27  PRO Z N     
6789  C  CA    . PRO F 27  ? 0.7641 0.4368 0.3088 -0.0792 0.1842 -0.017  27  PRO Z CA    
6790  C  C     . PRO F 27  ? 0.7616 0.4345 0.2984 -0.0865 0.1812 -0.0168 27  PRO Z C     
6791  O  O     . PRO F 27  ? 0.7594 0.4434 0.2985 -0.0896 0.179  -0.0152 27  PRO Z O     
6792  C  CB    . PRO F 27  ? 0.7727 0.4472 0.3192 -0.0749 0.1855 -0.0163 27  PRO Z CB    
6793  C  CG    . PRO F 27  ? 0.773  0.4578 0.3296 -0.0702 0.1866 -0.015  27  PRO Z CG    
6794  C  CD    . PRO F 27  ? 0.75   0.4421 0.3102 -0.0729 0.1852 -0.0143 27  PRO Z CD    
6795  N  N     . GLN F 28  ? 0.7605 0.4207 0.2875 -0.0893 0.1813 -0.0183 28  GLN Z N     
6796  C  CA    . GLN F 28  ? 0.7645 0.4217 0.2818 -0.0967 0.1786 -0.0185 28  GLN Z CA    
6797  C  C     . GLN F 28  ? 0.7606 0.4207 0.274  -0.098  0.1772 -0.0176 28  GLN Z C     
6798  O  O     . GLN F 28  ? 0.7586 0.4267 0.2703 -0.1033 0.1742 -0.0164 28  GLN Z O     
6799  C  CB    . GLN F 28  ? 0.7957 0.4364 0.3028 -0.0984 0.1798 -0.0205 28  GLN Z CB    
6800  C  CG    . GLN F 28  ? 0.8414 0.478  0.3523 -0.0959 0.1817 -0.0213 28  GLN Z CG    
6801  C  CD    . GLN F 28  ? 0.8959 0.5405 0.4101 -0.1    0.1797 -0.0208 28  GLN Z CD    
6802  O  OE1   . GLN F 28  ? 0.9191 0.5611 0.4259 -0.1066 0.1777 -0.0211 28  GLN Z OE1   
6803  N  NE2   . GLN F 28  ? 0.894  0.5482 0.4191 -0.0963 0.1802 -0.02   28  GLN Z NE2   
6804  N  N     . LYS F 29  ? 0.7581 0.4121 0.2704 -0.093  0.1794 -0.0181 29  LYS Z N     
6805  C  CA    . LYS F 29  ? 0.7607 0.4161 0.2689 -0.0934 0.1784 -0.0174 29  LYS Z CA    
6806  C  C     . LYS F 29  ? 0.7555 0.4159 0.272  -0.0859 0.1808 -0.0166 29  LYS Z C     
6807  O  O     . LYS F 29  ? 0.7581 0.4121 0.2777 -0.0805 0.1839 -0.0175 29  LYS Z O     
6808  C  CB    . LYS F 29  ? 0.7919 0.431  0.2867 -0.0956 0.179  -0.0189 29  LYS Z CB    
6809  C  CG    . LYS F 29  ? 0.8471 0.48   0.3315 -0.1038 0.1765 -0.0197 29  LYS Z CG    
6810  C  CD    . LYS F 29  ? 0.9128 0.5265 0.3844 -0.1043 0.1785 -0.0215 29  LYS Z CD    
6811  C  CE    . LYS F 29  ? 0.9684 0.5744 0.429  -0.1062 0.1779 -0.0217 29  LYS Z CE    
6812  N  NZ    . LYS F 29  ? 1.0101 0.5964 0.4577 -0.1063 0.1803 -0.0233 29  LYS Z NZ    
6813  N  N     . VAL F 30  ? 0.7458 0.4178 0.266  -0.0856 0.1794 -0.0148 30  VAL Z N     
6814  C  CA    . VAL F 30  ? 0.7436 0.4203 0.2708 -0.0786 0.1817 -0.014  30  VAL Z CA    
6815  C  C     . VAL F 30  ? 0.7468 0.4243 0.2687 -0.0792 0.1807 -0.0132 30  VAL Z C     
6816  O  O     . VAL F 30  ? 0.7476 0.4323 0.2664 -0.0843 0.1774 -0.0119 30  VAL Z O     
6817  C  CB    . VAL F 30  ? 0.7427 0.4338 0.2814 -0.0757 0.182  -0.0122 30  VAL Z CB    
6818  C  CG1   . VAL F 30  ? 0.7457 0.4416 0.2902 -0.069  0.1843 -0.0111 30  VAL Z CG1   
6819  C  CG2   . VAL F 30  ? 0.7477 0.4368 0.2916 -0.0743 0.1834 -0.0131 30  VAL Z CG2   
6820  N  N     . LYS F 31  ? 0.7463 0.4163 0.2668 -0.074  0.1834 -0.0138 31  LYS Z N     
6821  C  CA    . LYS F 31  ? 0.7505 0.4204 0.2661 -0.0735 0.1829 -0.0132 31  LYS Z CA    
6822  C  C     . LYS F 31  ? 0.7486 0.4232 0.2725 -0.0658 0.1859 -0.0123 31  LYS Z C     
6823  O  O     . LYS F 31  ? 0.7508 0.4208 0.2796 -0.0609 0.1891 -0.0132 31  LYS Z O     
6824  C  CB    . LYS F 31  ? 0.7804 0.4338 0.2839 -0.075  0.1836 -0.0149 31  LYS Z CB    
6825  C  CG    . LYS F 31  ? 0.8307 0.4825 0.3281 -0.0744 0.1831 -0.0143 31  LYS Z CG    
6826  C  CD    . LYS F 31  ? 0.8933 0.5273 0.3781 -0.075  0.1845 -0.0159 31  LYS Z CD    
6827  C  CE    . LYS F 31  ? 0.9435 0.5725 0.4157 -0.0833 0.1808 -0.0163 31  LYS Z CE    
6828  N  NZ    . LYS F 31  ? 0.9771 0.5873 0.4358 -0.0838 0.1825 -0.0179 31  LYS Z NZ    
6829  N  N     . ARG F 32  ? 0.742  0.426  0.2673 -0.0648 0.1849 -0.0106 32  ARG Z N     
6830  C  CA    . ARG F 32  ? 0.7408 0.4286 0.2726 -0.0576 0.1879 -0.0097 32  ARG Z CA    
6831  C  C     . ARG F 32  ? 0.7425 0.4272 0.2678 -0.0566 0.1878 -0.0093 32  ARG Z C     
6832  O  O     . ARG F 32  ? 0.7467 0.4303 0.2636 -0.062  0.1847 -0.0092 32  ARG Z O     
6833  C  CB    . ARG F 32  ? 0.7486 0.4522 0.2899 -0.0558 0.1876 -0.0074 32  ARG Z CB    
6834  C  CG    . ARG F 32  ? 0.7813 0.4872 0.3306 -0.0538 0.1892 -0.0077 32  ARG Z CG    
6835  C  CD    . ARG F 32  ? 0.812  0.5331 0.3691 -0.0518 0.1891 -0.0051 32  ARG Z CD    
6836  N  NE    . ARG F 32  ? 0.844  0.5672 0.4083 -0.0496 0.1907 -0.0053 32  ARG Z NE    
6837  C  CZ    . ARG F 32  ? 0.8722 0.5931 0.4418 -0.0437 0.1942 -0.0057 32  ARG Z CZ    
6838  N  NH1   . ARG F 32  ? 0.8718 0.5881 0.4406 -0.0392 0.1966 -0.006  32  ARG Z NH1   
6839  N  NH2   . ARG F 32  ? 0.8709 0.5935 0.446  -0.0424 0.1953 -0.0058 32  ARG Z NH2   
6840  N  N     . GLY F 33  ? 0.7373 0.4202 0.2659 -0.0499 0.1912 -0.0092 33  GLY Z N     
6841  C  CA    . GLY F 33  ? 0.743  0.4229 0.2659 -0.0481 0.1916 -0.0088 33  GLY Z CA    
6842  C  C     . GLY F 33  ? 0.7429 0.4185 0.2701 -0.0404 0.1961 -0.0091 33  GLY Z C     
6843  O  O     . GLY F 33  ? 0.7418 0.4221 0.278  -0.0363 0.1983 -0.0087 33  GLY Z O     
6844  N  N     . PHE F 34  ? 0.7431 0.4093 0.2635 -0.0384 0.1974 -0.0096 34  PHE Z N     
6845  C  CA    . PHE F 34  ? 0.7449 0.4063 0.2686 -0.0313 0.2018 -0.0098 34  PHE Z CA    
6846  C  C     . PHE F 34  ? 0.7517 0.3969 0.2679 -0.0305 0.2039 -0.0113 34  PHE Z C     
6847  O  O     . PHE F 34  ? 0.7575 0.3955 0.2631 -0.0344 0.202  -0.0119 34  PHE Z O     
6848  C  CB    . PHE F 34  ? 0.7432 0.4108 0.2662 -0.0283 0.202  -0.0082 34  PHE Z CB    
6849  C  CG    . PHE F 34  ? 0.7457 0.4281 0.2775 -0.0256 0.2021 -0.0062 34  PHE Z CG    
6850  C  CD1   . PHE F 34  ? 0.754  0.4381 0.2939 -0.0194 0.206  -0.006  34  PHE Z CD1   
6851  C  CD2   . PHE F 34  ? 0.7522 0.4467 0.2835 -0.0292 0.1985 -0.0044 34  PHE Z CD2   
6852  C  CE1   . PHE F 34  ? 0.7567 0.4532 0.3033 -0.0166 0.2065 -0.004  34  PHE Z CE1   
6853  C  CE2   . PHE F 34  ? 0.7547 0.4628 0.2937 -0.0261 0.199  -0.0021 34  PHE Z CE2   
6854  C  CZ    . PHE F 34  ? 0.75   0.4585 0.2963 -0.0196 0.2032 -0.002  34  PHE Z CZ    
6855  N  N     . ILE F 35  ? 0.748  0.3871 0.2691 -0.0255 0.2079 -0.0119 35  ILE Z N     
6856  C  CA    . ILE F 35  ? 0.756  0.3802 0.2707 -0.0235 0.2106 -0.0128 35  ILE Z CA    
6857  C  C     . ILE F 35  ? 0.7571 0.378  0.2695 -0.0184 0.2133 -0.0121 35  ILE Z C     
6858  O  O     . ILE F 35  ? 0.7673 0.3762 0.2717 -0.0172 0.215  -0.0125 35  ILE Z O     
6859  C  CB    . ILE F 35  ? 0.7609 0.3797 0.2814 -0.0212 0.2134 -0.0133 35  ILE Z CB    
6860  C  CG1   . ILE F 35  ? 0.7638 0.389  0.2956 -0.0157 0.2163 -0.0126 35  ILE Z CG1   
6861  C  CG2   . ILE F 35  ? 0.7671 0.3869 0.2878 -0.0262 0.2109 -0.0141 35  ILE Z CG2   
6862  C  CD1   . ILE F 35  ? 0.7793 0.3967 0.3149 -0.0121 0.2199 -0.0127 35  ILE Z CD1   
6863  N  N     . SER F 36  ? 0.7441 0.3752 0.2633 -0.0151 0.2139 -0.011  36  SER Z N     
6864  C  CA    . SER F 36  ? 0.7437 0.3744 0.2621 -0.0102 0.2162 -0.0102 36  SER Z CA    
6865  C  C     . SER F 36  ? 0.7333 0.3787 0.2567 -0.0099 0.2145 -0.0088 36  SER Z C     
6866  O  O     . SER F 36  ? 0.7296 0.3843 0.2579 -0.0128 0.2122 -0.0085 36  SER Z O     
6867  C  CB    . SER F 36  ? 0.7599 0.3856 0.2846 -0.004  0.2211 -0.0102 36  SER Z CB    
6868  O  OG    . SER F 36  ? 0.782  0.4168 0.3174 -0.002  0.2221 -0.0098 36  SER Z OG    
6869  N  N     . LEU F 37  ? 0.728  0.3755 0.2502 -0.006  0.2158 -0.0078 37  LEU Z N     
6870  C  CA    . LEU F 37  ? 0.7258 0.387  0.2524 -0.0049 0.2147 -0.0061 37  LEU Z CA    
6871  C  C     . LEU F 37  ? 0.7185 0.388  0.2561 -0.0023 0.2164 -0.0055 37  LEU Z C     
6872  O  O     . LEU F 37  ? 0.7153 0.3967 0.2564 -0.0038 0.2143 -0.0042 37  LEU Z O     
6873  C  CB    . LEU F 37  ? 0.7337 0.3939 0.257  -0.0002 0.2167 -0.0051 37  LEU Z CB    
6874  C  CG    . LEU F 37  ? 0.7627 0.417  0.2745 -0.0033 0.2142 -0.0053 37  LEU Z CG    
6875  C  CD1   . LEU F 37  ? 0.774  0.4208 0.2817 0.0021  0.2175 -0.0052 37  LEU Z CD1   
6876  C  CD2   . LEU F 37  ? 0.7688 0.435  0.2784 -0.0079 0.2094 -0.0038 37  LEU Z CD2   
6877  N  N     . SER F 38  ? 0.7128 0.3759 0.2552 0.0012  0.2201 -0.0064 38  SER Z N     
6878  C  CA    . SER F 38  ? 0.706  0.3752 0.2578 0.0035  0.2218 -0.006  38  SER Z CA    
6879  C  C     . SER F 38  ? 0.6953 0.365  0.2505 -0.0004 0.2201 -0.0069 38  SER Z C     
6880  O  O     . SER F 38  ? 0.6903 0.3666 0.2522 0.0004  0.2206 -0.0065 38  SER Z O     
6881  C  CB    . SER F 38  ? 0.7279 0.3902 0.2834 0.009   0.2266 -0.0064 38  SER Z CB    
6882  O  OG    . SER F 38  ? 0.7637 0.4291 0.3192 0.0138  0.2289 -0.0052 38  SER Z OG    
6883  N  N     . CYS F 39  ? 0.6915 0.3534 0.2421 -0.0043 0.2186 -0.0082 39  CYS Z N     
6884  C  CA    . CYS F 39  ? 0.6887 0.3494 0.2423 -0.0075 0.2174 -0.0092 39  CYS Z CA    
6885  C  C     . CYS F 39  ? 0.6774 0.342  0.2274 -0.0138 0.2131 -0.0093 39  CYS Z C     
6886  O  O     . CYS F 39  ? 0.6844 0.3416 0.2268 -0.0173 0.2115 -0.0102 39  CYS Z O     
6887  C  CB    . CYS F 39  ? 0.7084 0.357  0.2609 -0.0064 0.2197 -0.0103 39  CYS Z CB    
6888  S  SG    . CYS F 39  ? 0.7729 0.4171 0.3309 0.0007  0.225  -0.0099 39  CYS Z SG    
6889  N  N     . PRO F 40  ? 0.6555 0.3305 0.2107 -0.0155 0.2114 -0.0086 40  PRO Z N     
6890  C  CA    . PRO F 40  ? 0.6431 0.3218 0.1956 -0.0218 0.2074 -0.0087 40  PRO Z CA    
6891  C  C     . PRO F 40  ? 0.6335 0.3046 0.1861 -0.0243 0.2073 -0.0103 40  PRO Z C     
6892  O  O     . PRO F 40  ? 0.6309 0.2967 0.1878 -0.021  0.2101 -0.011  40  PRO Z O     
6893  C  CB    . PRO F 40  ? 0.6461 0.3384 0.205  -0.0216 0.2064 -0.007  40  PRO Z CB    
6894  C  CG    . PRO F 40  ? 0.6513 0.3462 0.2154 -0.0151 0.2101 -0.0061 40  PRO Z CG    
6895  C  CD    . PRO F 40  ? 0.6398 0.3231 0.2031 -0.0117 0.2133 -0.0075 40  PRO Z CD    
6896  N  N     . PHE F 41  ? 0.6275 0.2983 0.1755 -0.0302 0.204  -0.0108 41  PHE Z N     
6897  C  CA    . PHE F 41  ? 0.6302 0.2941 0.1777 -0.0327 0.2037 -0.0122 41  PHE Z CA    
6898  C  C     . PHE F 41  ? 0.6292 0.2997 0.1769 -0.0383 0.2003 -0.0121 41  PHE Z C     
6899  O  O     . PHE F 41  ? 0.6296 0.3079 0.1751 -0.0416 0.1975 -0.011  41  PHE Z O     
6900  C  CB    . PHE F 41  ? 0.6363 0.2863 0.1749 -0.0338 0.2044 -0.0134 41  PHE Z CB    
6901  C  CG    . PHE F 41  ? 0.6469 0.294  0.1752 -0.0397 0.2011 -0.0137 41  PHE Z CG    
6902  C  CD1   . PHE F 41  ? 0.6563 0.3024 0.1815 -0.0453 0.1986 -0.0144 41  PHE Z CD1   
6903  C  CD2   . PHE F 41  ? 0.656  0.3006 0.1771 -0.0398 0.2007 -0.0133 41  PHE Z CD2   
6904  C  CE1   . PHE F 41  ? 0.6669 0.3101 0.1821 -0.0513 0.1955 -0.0146 41  PHE Z CE1   
6905  C  CE2   . PHE F 41  ? 0.6671 0.3085 0.1779 -0.0457 0.1974 -0.0136 41  PHE Z CE2   
6906  C  CZ    . PHE F 41  ? 0.666  0.3067 0.174  -0.0516 0.1949 -0.0143 41  PHE Z CZ    
6907  N  N     . ILE F 42  ? 0.6267 0.294  0.1769 -0.0395 0.2005 -0.013  42  ILE Z N     
6908  C  CA    . ILE F 42  ? 0.6301 0.3013 0.1796 -0.0449 0.1975 -0.0131 42  ILE Z CA    
6909  C  C     . ILE F 42  ? 0.6384 0.2975 0.1829 -0.0471 0.1978 -0.0148 42  ILE Z C     
6910  O  O     . ILE F 42  ? 0.6414 0.2947 0.1892 -0.0437 0.2004 -0.0154 42  ILE Z O     
6911  C  CB    . ILE F 42  ? 0.6307 0.3126 0.1888 -0.0443 0.1972 -0.0122 42  ILE Z CB    
6912  C  CG1   . ILE F 42  ? 0.6413 0.326  0.1977 -0.0503 0.1942 -0.0124 42  ILE Z CG1   
6913  C  CG2   . ILE F 42  ? 0.6365 0.3155 0.2015 -0.0396 0.2002 -0.0128 42  ILE Z CG2   
6914  C  CD1   . ILE F 42  ? 0.6511 0.3468 0.2146 -0.0502 0.1936 -0.0111 42  ILE Z CD1   
6915  N  N     . GLU F 43  ? 0.6394 0.2943 0.1752 -0.0526 0.1954 -0.0153 43  GLU Z N     
6916  C  CA    . GLU F 43  ? 0.6494 0.2922 0.1786 -0.0548 0.1957 -0.0167 43  GLU Z CA    
6917  C  C     . GLU F 43  ? 0.6532 0.3    0.1828 -0.06   0.1932 -0.0169 43  GLU Z C     
6918  O  O     . GLU F 43  ? 0.6551 0.3093 0.1828 -0.0646 0.1901 -0.0163 43  GLU Z O     
6919  C  CB    . GLU F 43  ? 0.6829 0.3162 0.2    -0.0575 0.1951 -0.0172 43  GLU Z CB    
6920  C  CG    . GLU F 43  ? 0.7449 0.3633 0.2541 -0.0582 0.1966 -0.0184 43  GLU Z CG    
6921  C  CD    . GLU F 43  ? 0.8147 0.4212 0.3114 -0.0594 0.197  -0.0188 43  GLU Z CD    
6922  O  OE1   . GLU F 43  ? 0.8276 0.4372 0.3222 -0.0589 0.1963 -0.0182 43  GLU Z OE1   
6923  O  OE2   . GLU F 43  ? 0.8381 0.4318 0.3266 -0.0605 0.1982 -0.0197 43  GLU Z OE2   
6924  N  N     . ILE F 44  ? 0.6519 0.2948 0.1846 -0.0591 0.1944 -0.0177 44  ILE Z N     
6925  C  CA    . ILE F 44  ? 0.6545 0.3004 0.1876 -0.0637 0.1922 -0.018  44  ILE Z CA    
6926  C  C     . ILE F 44  ? 0.6693 0.3028 0.1954 -0.0658 0.1928 -0.0193 44  ILE Z C     
6927  O  O     . ILE F 44  ? 0.6744 0.2989 0.1999 -0.0619 0.1956 -0.0197 44  ILE Z O     
6928  C  CB    . ILE F 44  ? 0.65   0.3057 0.1941 -0.0612 0.1925 -0.0174 44  ILE Z CB    
6929  C  CG1   . ILE F 44  ? 0.6595 0.3098 0.2088 -0.0562 0.1955 -0.0179 44  ILE Z CG1   
6930  C  CG2   . ILE F 44  ? 0.6497 0.3177 0.1997 -0.0594 0.1921 -0.0158 44  ILE Z CG2   
6931  C  CD1   . ILE F 44  ? 0.6694 0.3265 0.2272 -0.055  0.1955 -0.0176 44  ILE Z CD1   
6932  N  N     . ILE F 45  ? 0.6739 0.307  0.1945 -0.0719 0.1903 -0.0197 45  ILE Z N     
6933  C  CA    . ILE F 45  ? 0.6885 0.3105 0.202  -0.0745 0.1907 -0.0209 45  ILE Z CA    
6934  C  C     . ILE F 45  ? 0.6892 0.3183 0.2085 -0.0766 0.1893 -0.0208 45  ILE Z C     
6935  O  O     . ILE F 45  ? 0.6878 0.326  0.2082 -0.0809 0.1865 -0.0202 45  ILE Z O     
6936  C  CB    . ILE F 45  ? 0.7049 0.3189 0.205  -0.0805 0.1889 -0.0215 45  ILE Z CB    
6937  C  CG1   . ILE F 45  ? 0.7242 0.3307 0.2177 -0.0784 0.1903 -0.0214 45  ILE Z CG1   
6938  C  CG2   . ILE F 45  ? 0.7186 0.321  0.211  -0.0832 0.1895 -0.0226 45  ILE Z CG2   
6939  C  CD1   . ILE F 45  ? 0.7506 0.3496 0.2305 -0.0845 0.1883 -0.0219 45  ILE Z CD1   
6940  N  N     . PHE F 46  ? 0.6888 0.3147 0.2127 -0.0735 0.1911 -0.0212 46  PHE Z N     
6941  C  CA    . PHE F 46  ? 0.6893 0.3212 0.2186 -0.075  0.19   -0.0212 46  PHE Z CA    
6942  C  C     . PHE F 46  ? 0.7024 0.324  0.2278 -0.0753 0.1913 -0.0222 46  PHE Z C     
6943  O  O     . PHE F 46  ? 0.7075 0.3179 0.2269 -0.0734 0.1933 -0.0226 46  PHE Z O     
6944  C  CB    . PHE F 46  ? 0.6768 0.3189 0.2181 -0.0704 0.1908 -0.0204 46  PHE Z CB    
6945  C  CG    . PHE F 46  ? 0.6799 0.3173 0.2259 -0.0645 0.1936 -0.0205 46  PHE Z CG    
6946  C  CD1   . PHE F 46  ? 0.687  0.3221 0.2337 -0.0605 0.1955 -0.0201 46  PHE Z CD1   
6947  C  CD2   . PHE F 46  ? 0.6881 0.3239 0.2382 -0.0632 0.1943 -0.0208 46  PHE Z CD2   
6948  C  CE1   . PHE F 46  ? 0.6945 0.326  0.2459 -0.0554 0.1981 -0.0199 46  PHE Z CE1   
6949  C  CE2   . PHE F 46  ? 0.6949 0.3273 0.2496 -0.0582 0.1967 -0.0206 46  PHE Z CE2   
6950  C  CZ    . PHE F 46  ? 0.6911 0.3216 0.2467 -0.0544 0.1985 -0.0201 46  PHE Z CZ    
6951  N  N     . LYS F 47  ? 0.7093 0.3344 0.2378 -0.0772 0.1902 -0.0224 47  LYS Z N     
6952  C  CA    . LYS F 47  ? 0.7307 0.3467 0.2558 -0.0772 0.1914 -0.0231 47  LYS Z CA    
6953  C  C     . LYS F 47  ? 0.7362 0.3576 0.2701 -0.075  0.1915 -0.0229 47  LYS Z C     
6954  O  O     . LYS F 47  ? 0.7342 0.3663 0.2752 -0.0753 0.1902 -0.0224 47  LYS Z O     
6955  C  CB    . LYS F 47  ? 0.7658 0.3752 0.28   -0.0836 0.19   -0.0239 47  LYS Z CB    
6956  C  CG    . LYS F 47  ? 0.8172 0.4366 0.3336 -0.0887 0.187  -0.0236 47  LYS Z CG    
6957  C  CD    . LYS F 47  ? 0.887  0.4996 0.3924 -0.0955 0.1856 -0.0244 47  LYS Z CD    
6958  C  CE    . LYS F 47  ? 0.9306 0.5541 0.4383 -0.1009 0.1826 -0.0237 47  LYS Z CE    
6959  N  NZ    . LYS F 47  ? 0.963  0.5792 0.4604 -0.1076 0.1814 -0.0245 47  LYS Z NZ    
6960  N  N     . GLU F 48  ? 0.7419 0.3556 0.2751 -0.0727 0.1933 -0.0232 48  GLU Z N     
6961  C  CA    . GLU F 48  ? 0.7488 0.3657 0.2887 -0.071  0.1933 -0.0231 48  GLU Z CA    
6962  C  C     . GLU F 48  ? 0.7565 0.3649 0.2886 -0.0741 0.1934 -0.0238 48  GLU Z C     
6963  O  O     . GLU F 48  ? 0.7641 0.3635 0.293  -0.0716 0.1954 -0.0238 48  GLU Z O     
6964  C  CB    . GLU F 48  ? 0.7794 0.3947 0.3255 -0.065  0.1955 -0.0225 48  GLU Z CB    
6965  C  CG    . GLU F 48  ? 0.8393 0.4623 0.3927 -0.0619 0.1958 -0.0218 48  GLU Z CG    
6966  C  CD    . GLU F 48  ? 0.9226 0.5448 0.4826 -0.0566 0.1977 -0.0211 48  GLU Z CD    
6967  O  OE1   . GLU F 48  ? 0.948  0.5633 0.5064 -0.0549 0.1991 -0.0208 48  GLU Z OE1   
6968  O  OE2   . GLU F 48  ? 0.9372 0.5657 0.5038 -0.0541 0.198  -0.0206 48  GLU Z OE2   
6969  N  N     . GLY F 49  ? 0.7516 0.3625 0.28   -0.0795 0.1913 -0.0243 49  GLY Z N     
6970  C  CA    . GLY F 49  ? 0.7582 0.3607 0.2779 -0.0833 0.1912 -0.0251 49  GLY Z CA    
6971  C  C     . GLY F 49  ? 0.763  0.3541 0.2709 -0.0852 0.1922 -0.0255 49  GLY Z C     
6972  O  O     . GLY F 49  ? 0.7676 0.3599 0.2709 -0.0888 0.1908 -0.0257 49  GLY Z O     
6973  N  N     . HIS F 50  ? 0.7613 0.3409 0.2638 -0.0826 0.1948 -0.0256 50  HIS Z N     
6974  C  CA    . HIS F 50  ? 0.7691 0.3358 0.2591 -0.0837 0.1964 -0.0259 50  HIS Z CA    
6975  C  C     . HIS F 50  ? 0.7678 0.3324 0.2592 -0.0788 0.1984 -0.0251 50  HIS Z C     
6976  O  O     . HIS F 50  ? 0.7764 0.3308 0.2574 -0.0795 0.1997 -0.0253 50  HIS Z O     
6977  C  CB    . HIS F 50  ? 0.783  0.3371 0.2653 -0.0828 0.1989 -0.026  50  HIS Z CB    
6978  C  CG    . HIS F 50  ? 0.8096 0.3616 0.2865 -0.0881 0.1975 -0.0269 50  HIS Z CG    
6979  N  ND1   . HIS F 50  ? 0.8382 0.3799 0.3012 -0.0937 0.1974 -0.0278 50  HIS Z ND1   
6980  C  CD2   . HIS F 50  ? 0.8169 0.3747 0.2998 -0.0886 0.1965 -0.0271 50  HIS Z CD2   
6981  C  CE1   . HIS F 50  ? 0.8427 0.3849 0.3043 -0.0973 0.1963 -0.0284 50  HIS Z CE1   
6982  N  NE2   . HIS F 50  ? 0.8342 0.386  0.3077 -0.0943 0.1958 -0.028  50  HIS Z NE2   
6983  N  N     . ASP F 51  ? 0.7562 0.3295 0.2595 -0.0739 0.1988 -0.0243 51  ASP Z N     
6984  C  CA    . ASP F 51  ? 0.7551 0.327  0.2607 -0.0689 0.2008 -0.0234 51  ASP Z CA    
6985  C  C     . ASP F 51  ? 0.7473 0.3264 0.2551 -0.07   0.1993 -0.0234 51  ASP Z C     
6986  O  O     . ASP F 51  ? 0.7378 0.3286 0.2551 -0.0696 0.1976 -0.0232 51  ASP Z O     
6987  C  CB    . ASP F 51  ? 0.7668 0.3434 0.2836 -0.0631 0.2022 -0.0223 51  ASP Z CB    
6988  C  CG    . ASP F 51  ? 0.8204 0.387  0.334  -0.0587 0.2056 -0.0211 51  ASP Z CG    
6989  O  OD1   . ASP F 51  ? 0.8334 0.3914 0.34   -0.057  0.2078 -0.0206 51  ASP Z OD1   
6990  O  OD2   . ASP F 51  ? 0.8384 0.4058 0.3564 -0.0568 0.206  -0.0206 51  ASP Z OD2   
6991  N  N     . TYR F 52  ? 0.7507 0.3222 0.2492 -0.071  0.2    -0.0236 52  TYR Z N     
6992  C  CA    . TYR F 52  ? 0.7526 0.3303 0.2524 -0.0717 0.1987 -0.0235 52  TYR Z CA    
6993  C  C     . TYR F 52  ? 0.7367 0.3159 0.2432 -0.0653 0.201  -0.0225 52  TYR Z C     
6994  O  O     . TYR F 52  ? 0.7366 0.308  0.2422 -0.0609 0.204  -0.0218 52  TYR Z O     
6995  C  CB    . TYR F 52  ? 0.7715 0.3405 0.2577 -0.0763 0.198  -0.0241 52  TYR Z CB    
6996  C  CG    . TYR F 52  ? 0.7985 0.371  0.2802 -0.0839 0.1945 -0.0249 52  TYR Z CG    
6997  C  CD1   . TYR F 52  ? 0.8122 0.3968 0.2982 -0.087  0.1915 -0.0246 52  TYR Z CD1   
6998  C  CD2   . TYR F 52  ? 0.8252 0.3891 0.2981 -0.0879 0.1945 -0.0257 52  TYR Z CD2   
6999  C  CE1   . TYR F 52  ? 0.8308 0.4198 0.3133 -0.094  0.1883 -0.0249 52  TYR Z CE1   
7000  C  CE2   . TYR F 52  ? 0.8436 0.4109 0.3125 -0.0951 0.1913 -0.0263 52  TYR Z CE2   
7001  C  CZ    . TYR F 52  ? 0.854  0.4343 0.3281 -0.0983 0.1882 -0.0258 52  TYR Z CZ    
7002  O  OH    . TYR F 52  ? 0.8802 0.4649 0.351  -0.1055 0.185  -0.0259 52  TYR Z OH    
7003  N  N     . PHE F 53  ? 0.7218 0.3113 0.2351 -0.0646 0.1997 -0.0222 53  PHE Z N     
7004  C  CA    . PHE F 53  ? 0.716  0.3078 0.2357 -0.059  0.2017 -0.0213 53  PHE Z CA    
7005  C  C     . PHE F 53  ? 0.7036 0.299  0.221  -0.0601 0.2006 -0.0212 53  PHE Z C     
7006  O  O     . PHE F 53  ? 0.6996 0.3024 0.2167 -0.0644 0.1977 -0.0215 53  PHE Z O     
7007  C  CB    . PHE F 53  ? 0.712  0.3139 0.2447 -0.0558 0.2017 -0.0207 53  PHE Z CB    
7008  C  CG    . PHE F 53  ? 0.7249 0.324  0.2607 -0.0542 0.2027 -0.0205 53  PHE Z CG    
7009  C  CD1   . PHE F 53  ? 0.7384 0.3312 0.2755 -0.0495 0.2056 -0.0196 53  PHE Z CD1   
7010  C  CD2   . PHE F 53  ? 0.736  0.3387 0.2733 -0.0574 0.2007 -0.0211 53  PHE Z CD2   
7011  C  CE1   . PHE F 53  ? 0.7479 0.3386 0.2877 -0.0481 0.2064 -0.0191 53  PHE Z CE1   
7012  C  CE2   . PHE F 53  ? 0.7471 0.3471 0.2868 -0.056  0.2016 -0.0209 53  PHE Z CE2   
7013  C  CZ    . PHE F 53  ? 0.7458 0.34   0.2868 -0.0514 0.2043 -0.0198 53  PHE Z CZ    
7014  N  N     . HIS F 54  ? 0.6959 0.2862 0.2116 -0.0561 0.203  -0.0207 54  HIS Z N     
7015  C  CA    . HIS F 54  ? 0.6942 0.2868 0.2071 -0.0566 0.2022 -0.0206 54  HIS Z CA    
7016  C  C     . HIS F 54  ? 0.6858 0.2836 0.208  -0.0507 0.2043 -0.0196 54  HIS Z C     
7017  O  O     . HIS F 54  ? 0.6928 0.2835 0.2148 -0.0462 0.2074 -0.019  54  HIS Z O     
7018  C  CB    . HIS F 54  ? 0.714  0.2929 0.2134 -0.0577 0.2034 -0.0209 54  HIS Z CB    
7019  C  CG    . HIS F 54  ? 0.744  0.324  0.2379 -0.0596 0.2021 -0.0209 54  HIS Z CG    
7020  N  ND1   . HIS F 54  ? 0.7734 0.3414 0.2536 -0.062  0.2023 -0.0214 54  HIS Z ND1   
7021  C  CD2   . HIS F 54  ? 0.7544 0.3457 0.2544 -0.0592 0.2005 -0.0204 54  HIS Z CD2   
7022  C  CE1   . HIS F 54  ? 0.781  0.3537 0.2597 -0.0633 0.2006 -0.0212 54  HIS Z CE1   
7023  N  NE2   . HIS F 54  ? 0.7725 0.3595 0.2631 -0.0615 0.1995 -0.0206 54  HIS Z NE2   
7024  N  N     . TRP F 55  ? 0.668  0.2779 0.198  -0.0505 0.2027 -0.0193 55  TRP Z N     
7025  C  CA    . TRP F 55  ? 0.6573 0.2723 0.1959 -0.0452 0.2046 -0.0185 55  TRP Z CA    
7026  C  C     . TRP F 55  ? 0.6584 0.2783 0.1958 -0.045  0.204  -0.0181 55  TRP Z C     
7027  O  O     . TRP F 55  ? 0.6598 0.285  0.1941 -0.0492 0.2011 -0.0183 55  TRP Z O     
7028  C  CB    . TRP F 55  ? 0.6438 0.2687 0.1931 -0.0442 0.204  -0.0183 55  TRP Z CB    
7029  C  CG    . TRP F 55  ? 0.6431 0.2649 0.1962 -0.043  0.205  -0.0183 55  TRP Z CG    
7030  C  CD1   . TRP F 55  ? 0.6575 0.2694 0.2069 -0.0417 0.2069 -0.0182 55  TRP Z CD1   
7031  C  CD2   . TRP F 55  ? 0.6357 0.2647 0.1973 -0.0427 0.2042 -0.0183 55  TRP Z CD2   
7032  N  NE1   . TRP F 55  ? 0.6575 0.2706 0.2128 -0.0408 0.2071 -0.018  55  TRP Z NE1   
7033  C  CE2   . TRP F 55  ? 0.6466 0.2698 0.2092 -0.0416 0.2054 -0.0182 55  TRP Z CE2   
7034  C  CE3   . TRP F 55  ? 0.6344 0.2737 0.2022 -0.0432 0.2028 -0.0181 55  TRP Z CE3   
7035  C  CZ2   . TRP F 55  ? 0.648  0.2755 0.2176 -0.0412 0.2049 -0.0181 55  TRP Z CZ2   
7036  C  CZ3   . TRP F 55  ? 0.6405 0.2831 0.2145 -0.0428 0.2025 -0.0181 55  TRP Z CZ3   
7037  C  CH2   . TRP F 55  ? 0.6432 0.28   0.2181 -0.042  0.2034 -0.0182 55  TRP Z CH2   
7038  N  N     . ARG F 56  ? 0.6541 0.2731 0.1946 -0.04   0.2065 -0.0175 56  ARG Z N     
7039  C  CA    . ARG F 56  ? 0.6516 0.276  0.1921 -0.0389 0.2062 -0.017  56  ARG Z CA    
7040  C  C     . ARG F 56  ? 0.6492 0.2794 0.1996 -0.0336 0.2084 -0.0162 56  ARG Z C     
7041  O  O     . ARG F 56  ? 0.6492 0.2745 0.2031 -0.0299 0.2111 -0.016  56  ARG Z O     
7042  C  CB    . ARG F 56  ? 0.6666 0.2819 0.1974 -0.0386 0.2071 -0.017  56  ARG Z CB    
7043  C  CG    . ARG F 56  ? 0.6929 0.3151 0.2224 -0.0391 0.2056 -0.0165 56  ARG Z CG    
7044  C  CD    . ARG F 56  ? 0.7282 0.3416 0.2485 -0.0381 0.2068 -0.0165 56  ARG Z CD    
7045  N  NE    . ARG F 56  ? 0.7465 0.3544 0.2698 -0.0318 0.2108 -0.016  56  ARG Z NE    
7046  C  CZ    . ARG F 56  ? 0.7634 0.3592 0.279  -0.0299 0.2132 -0.016  56  ARG Z CZ    
7047  N  NH1   . ARG F 56  ? 0.7574 0.3444 0.261  -0.0338 0.2119 -0.0166 56  ARG Z NH1   
7048  N  NH2   . ARG F 56  ? 0.7624 0.3546 0.2821 -0.0241 0.217  -0.0152 56  ARG Z NH2   
7049  N  N     . PHE F 57  ? 0.6459 0.2866 0.201  -0.0334 0.2073 -0.0157 57  PHE Z N     
7050  C  CA    . PHE F 57  ? 0.6496 0.2956 0.2131 -0.0287 0.2094 -0.015  57  PHE Z CA    
7051  C  C     . PHE F 57  ? 0.6561 0.3042 0.2176 -0.0263 0.2102 -0.0143 57  PHE Z C     
7052  O  O     . PHE F 57  ? 0.6549 0.3097 0.2142 -0.0285 0.2081 -0.0138 57  PHE Z O     
7053  C  CB    . PHE F 57  ? 0.6442 0.3003 0.2143 -0.0297 0.208  -0.0147 57  PHE Z CB    
7054  C  CG    . PHE F 57  ? 0.6536 0.3082 0.2264 -0.0316 0.2073 -0.0153 57  PHE Z CG    
7055  C  CD1   . PHE F 57  ? 0.6659 0.3203 0.2345 -0.0365 0.2046 -0.0159 57  PHE Z CD1   
7056  C  CD2   . PHE F 57  ? 0.6609 0.3141 0.2401 -0.0287 0.2092 -0.0153 57  PHE Z CD2   
7057  C  CE1   . PHE F 57  ? 0.6741 0.3268 0.2449 -0.0381 0.2041 -0.0164 57  PHE Z CE1   
7058  C  CE2   . PHE F 57  ? 0.6701 0.322  0.2515 -0.0304 0.2083 -0.0158 57  PHE Z CE2   
7059  C  CZ    . PHE F 57  ? 0.6696 0.3212 0.2468 -0.0349 0.2059 -0.0164 57  PHE Z CZ    
7060  N  N     . ASP F 58  ? 0.6612 0.3037 0.2234 -0.0218 0.2134 -0.014  58  ASP Z N     
7061  C  CA    . ASP F 58  ? 0.6686 0.3122 0.2291 -0.0188 0.2147 -0.0133 58  ASP Z CA    
7062  C  C     . ASP F 58  ? 0.6693 0.3197 0.238  -0.0148 0.2166 -0.0126 58  ASP Z C     
7063  O  O     . ASP F 58  ? 0.6724 0.3205 0.2467 -0.0123 0.2187 -0.0126 58  ASP Z O     
7064  C  CB    . ASP F 58  ? 0.6903 0.3228 0.2458 -0.0162 0.2173 -0.0134 58  ASP Z CB    
7065  C  CG    . ASP F 58  ? 0.7532 0.3771 0.2989 -0.0199 0.2159 -0.0141 58  ASP Z CG    
7066  O  OD1   . ASP F 58  ? 0.7637 0.391  0.3054 -0.0249 0.2125 -0.0145 58  ASP Z OD1   
7067  O  OD2   . ASP F 58  ? 0.7849 0.3986 0.3267 -0.0177 0.2183 -0.014  58  ASP Z OD2   
7068  N  N     . MET F 59  ? 0.6615 0.3204 0.2309 -0.0145 0.2157 -0.0118 59  MET Z N     
7069  C  CA    . MET F 59  ? 0.6548 0.3201 0.2308 -0.0108 0.2176 -0.011  59  MET Z CA    
7070  C  C     . MET F 59  ? 0.6534 0.3166 0.2291 -0.0059 0.2206 -0.0103 59  MET Z C     
7071  O  O     . MET F 59  ? 0.6545 0.3171 0.2248 -0.0057 0.2202 -0.01   59  MET Z O     
7072  C  CB    . MET F 59  ? 0.6527 0.3289 0.2301 -0.0127 0.2153 -0.01   59  MET Z CB    
7073  C  CG    . MET F 59  ? 0.6654 0.3436 0.2441 -0.017  0.2128 -0.0106 59  MET Z CG    
7074  S  SD    . MET F 59  ? 0.6954 0.3862 0.2739 -0.0202 0.2097 -0.0092 59  MET Z SD    
7075  C  CE    . MET F 59  ? 0.6861 0.3733 0.2569 -0.0264 0.2061 -0.01   59  MET Z CE    
7076  N  N     . PHE F 60  ? 0.6488 0.3107 0.2301 -0.0021 0.2237 -0.0102 60  PHE Z N     
7077  C  CA    . PHE F 60  ? 0.6526 0.312  0.2343 0.0027  0.227  -0.0096 60  PHE Z CA    
7078  C  C     . PHE F 60  ? 0.6557 0.3219 0.2418 0.0056  0.2286 -0.0087 60  PHE Z C     
7079  O  O     . PHE F 60  ? 0.6567 0.3216 0.2478 0.0072  0.2305 -0.0088 60  PHE Z O     
7080  C  CB    . PHE F 60  ? 0.651  0.3016 0.2349 0.0047  0.2297 -0.01   60  PHE Z CB    
7081  C  CG    . PHE F 60  ? 0.662  0.3044 0.2401 0.0036  0.2294 -0.0103 60  PHE Z CG    
7082  C  CD1   . PHE F 60  ? 0.6719 0.312  0.247  -0.0006 0.2268 -0.0111 60  PHE Z CD1   
7083  C  CD2   . PHE F 60  ? 0.6749 0.3112 0.25   0.007   0.2321 -0.0099 60  PHE Z CD2   
7084  C  CE1   . PHE F 60  ? 0.683  0.3145 0.2516 -0.0013 0.227  -0.0113 60  PHE Z CE1   
7085  C  CE2   . PHE F 60  ? 0.6863 0.3141 0.2552 0.0064  0.2322 -0.0101 60  PHE Z CE2   
7086  C  CZ    . PHE F 60  ? 0.6834 0.3086 0.2488 0.0022  0.2297 -0.0108 60  PHE Z CZ    
7087  N  N     . PRO F 61  ? 0.6538 0.3273 0.2377 0.0062  0.2277 -0.0077 61  PRO Z N     
7088  C  CA    . PRO F 61  ? 0.6516 0.3315 0.2389 0.0093  0.2295 -0.0065 61  PRO Z CA    
7089  C  C     . PRO F 61  ? 0.6561 0.3323 0.2442 0.0146  0.2337 -0.0061 61  PRO Z C     
7090  O  O     . PRO F 61  ? 0.6609 0.3348 0.2454 0.0166  0.2346 -0.0058 61  PRO Z O     
7091  C  CB    . PRO F 61  ? 0.6575 0.3467 0.2419 0.0082  0.2272 -0.0051 61  PRO Z CB    
7092  C  CG    . PRO F 61  ? 0.6634 0.3509 0.2429 0.0035  0.2237 -0.0058 61  PRO Z CG    
7093  C  CD    . PRO F 61  ? 0.6479 0.3242 0.2258 0.0039  0.225  -0.0073 61  PRO Z CD    
7094  N  N     . GLY F 62  ? 0.6564 0.3318 0.2486 0.0166  0.2361 -0.0061 62  GLY Z N     
7095  C  CA    . GLY F 62  ? 0.6661 0.338  0.2592 0.0214  0.2402 -0.0057 62  GLY Z CA    
7096  C  C     . GLY F 62  ? 0.6757 0.339  0.2712 0.0218  0.2422 -0.0066 62  GLY Z C     
7097  O  O     . GLY F 62  ? 0.6819 0.3403 0.2755 0.0218  0.2423 -0.0069 62  GLY Z O     
7098  N  N     . PHE F 63  ? 0.6769 0.3381 0.2765 0.0222  0.2439 -0.0068 63  PHE Z N     
7099  C  CA    . PHE F 63  ? 0.6861 0.3401 0.2888 0.0226  0.2459 -0.0072 63  PHE Z CA    
7100  C  C     . PHE F 63  ? 0.698  0.3482 0.2996 0.0271  0.2499 -0.0066 63  PHE Z C     
7101  O  O     . PHE F 63  ? 0.7001 0.3532 0.2994 0.0302  0.2515 -0.0059 63  PHE Z O     
7102  C  CB    . PHE F 63  ? 0.6813 0.3346 0.2883 0.021   0.2461 -0.0075 63  PHE Z CB    
7103  C  CG    . PHE F 63  ? 0.6844 0.3397 0.2931 0.0165  0.2426 -0.0082 63  PHE Z CG    
7104  C  CD1   . PHE F 63  ? 0.6929 0.3448 0.3034 0.0141  0.241  -0.0087 63  PHE Z CD1   
7105  C  CD2   . PHE F 63  ? 0.6921 0.3524 0.3005 0.0152  0.2411 -0.0083 63  PHE Z CD2   
7106  C  CE1   . PHE F 63  ? 0.6982 0.3516 0.31   0.0102  0.238  -0.0093 63  PHE Z CE1   
7107  C  CE2   . PHE F 63  ? 0.6977 0.3594 0.3076 0.0112  0.238  -0.0089 63  PHE Z CE2   
7108  C  CZ    . PHE F 63  ? 0.6931 0.3513 0.3047 0.0087  0.2364 -0.0095 63  PHE Z CZ    
7109  N  N     . ASN F 64  ? 0.7037 0.3476 0.3074 0.0278  0.2516 -0.0066 64  ASN Z N     
7110  C  CA    . ASN F 64  ? 0.7155 0.3553 0.3188 0.032   0.2557 -0.0059 64  ASN Z CA    
7111  C  C     . ASN F 64  ? 0.7369 0.3757 0.3429 0.0331  0.2583 -0.0057 64  ASN Z C     
7112  O  O     . ASN F 64  ? 0.7403 0.3794 0.3497 0.0302  0.2572 -0.0061 64  ASN Z O     
7113  C  CB    . ASN F 64  ? 0.7133 0.3468 0.3182 0.0323  0.2569 -0.0057 64  ASN Z CB    
7114  C  CG    . ASN F 64  ? 0.7214 0.353  0.3215 0.033   0.2561 -0.0056 64  ASN Z CG    
7115  O  OD1   . ASN F 64  ? 0.7251 0.3604 0.3206 0.0326  0.2541 -0.0059 64  ASN Z OD1   
7116  N  ND2   . ASN F 64  ? 0.7226 0.3482 0.3233 0.0339  0.2576 -0.0051 64  ASN Z ND2   
7117  N  N     . LYS F 65  ? 0.7493 0.3865 0.3532 0.0372  0.2619 -0.0051 65  LYS Z N     
7118  C  CA    . LYS F 65  ? 0.7679 0.4029 0.3731 0.0385  0.2649 -0.0049 65  LYS Z CA    
7119  C  C     . LYS F 65  ? 0.7882 0.4167 0.3961 0.0398  0.2681 -0.0045 65  LYS Z C     
7120  O  O     . LYS F 65  ? 0.7903 0.416  0.4011 0.0383  0.2693 -0.0045 65  LYS Z O     
7121  C  CB    . LYS F 65  ? 0.7916 0.4293 0.3922 0.0424  0.267  -0.0043 65  LYS Z CB    
7122  C  CG    . LYS F 65  ? 0.8444 0.4891 0.4433 0.0409  0.2642 -0.0043 65  LYS Z CG    
7123  C  CD    . LYS F 65  ? 0.9029 0.5527 0.4973 0.0443  0.2645 -0.0033 65  LYS Z CD    
7124  C  CE    . LYS F 65  ? 0.9498 0.6073 0.5431 0.0431  0.262  -0.0027 65  LYS Z CE    
7125  N  NZ    . LYS F 65  ? 0.9809 0.6439 0.5702 0.0473  0.2634 -0.0011 65  LYS Z NZ    
7126  N  N     . ASN F 66  ? 0.8008 0.4267 0.4074 0.0423  0.2695 -0.0041 66  ASN Z N     
7127  C  CA    . ASN F 66  ? 0.8172 0.4373 0.4266 0.0438  0.2727 -0.0033 66  ASN Z CA    
7128  C  C     . ASN F 66  ? 0.8303 0.449  0.4435 0.0411  0.2707 -0.0031 66  ASN Z C     
7129  O  O     . ASN F 66  ? 0.83   0.4495 0.4477 0.0375  0.2691 -0.0031 66  ASN Z O     
7130  C  CB    . ASN F 66  ? 0.8311 0.4486 0.4363 0.0489  0.2762 -0.0027 66  ASN Z CB    
7131  C  CG    . ASN F 66  ? 0.8645 0.4759 0.4722 0.051   0.2801 -0.0018 66  ASN Z CG    
7132  O  OD1   . ASN F 66  ? 0.8729 0.4823 0.4859 0.0486  0.2802 -0.0013 66  ASN Z OD1   
7133  N  ND2   . ASN F 66  ? 0.8752 0.4839 0.4791 0.0555  0.2834 -0.0013 66  ASN Z ND2   
7134  N  N     . THR F 67  ? 0.8394 0.4561 0.4503 0.0428  0.2708 -0.0027 67  THR Z N     
7135  C  CA    . THR F 67  ? 0.8558 0.4704 0.4691 0.0409  0.2694 -0.0022 67  THR Z CA    
7136  C  C     . THR F 67  ? 0.8618 0.476  0.4694 0.0413  0.2675 -0.0026 67  THR Z C     
7137  O  O     . THR F 67  ? 0.8636 0.4786 0.4714 0.0382  0.2645 -0.0029 67  THR Z O     
7138  C  CB    . THR F 67  ? 0.8834 0.4933 0.5012 0.0426  0.273  -0.0006 67  THR Z CB    
7139  O  OG1   . THR F 67  ? 0.9017 0.5096 0.521  0.0416  0.272  0.0003  67  THR Z OG1   
7140  C  CG2   . THR F 67  ? 0.8921 0.498  0.5068 0.0474  0.2771 0       67  THR Z CG2   
7141  N  N     . ASN F 68  ? 0.8603 0.4728 0.4625 0.0448  0.2692 -0.0025 68  ASN Z N     
7142  C  CA    . ASN F 68  ? 0.8629 0.4745 0.4584 0.0449  0.2673 -0.0029 68  ASN Z CA    
7143  C  C     . ASN F 68  ? 0.8522 0.4675 0.4424 0.0468  0.2669 -0.0033 68  ASN Z C     
7144  O  O     . ASN F 68  ? 0.8584 0.4714 0.4426 0.0486  0.267  -0.0032 68  ASN Z O     
7145  C  CB    . ASN F 68  ? 0.8928 0.4968 0.486  0.0477  0.2699 -0.0019 68  ASN Z CB    
7146  C  CG    . ASN F 68  ? 0.9487 0.5492 0.5479 0.0473  0.2716 -0.0007 68  ASN Z CG    
7147  O  OD1   . ASN F 68  ? 0.9706 0.5666 0.5715 0.0506  0.2755 0.0007  68  ASN Z OD1   
7148  N  ND2   . ASN F 68  ? 0.9586 0.5611 0.5611 0.0435  0.2689 -0.0008 68  ASN Z ND2   
7149  N  N     . ASP F 69  ? 0.8346 0.4554 0.4266 0.0465  0.2667 -0.0036 69  ASP Z N     
7150  C  CA    . ASP F 69  ? 0.824  0.4493 0.4114 0.0488  0.2667 -0.0035 69  ASP Z CA    
7151  C  C     . ASP F 69  ? 0.8096 0.4403 0.3929 0.0461  0.2623 -0.0039 69  ASP Z C     
7152  O  O     . ASP F 69  ? 0.8119 0.4441 0.3898 0.0479  0.262  -0.0035 69  ASP Z O     
7153  C  CB    . ASP F 69  ? 0.8397 0.4684 0.4297 0.0501  0.2685 -0.0033 69  ASP Z CB    
7154  C  CG    . ASP F 69  ? 0.8875 0.52   0.4813 0.046   0.2659 -0.0039 69  ASP Z CG    
7155  O  OD1   . ASP F 69  ? 0.8925 0.5223 0.4906 0.0433  0.2652 -0.0042 69  ASP Z OD1   
7156  O  OD2   . ASP F 69  ? 0.9139 0.5523 0.5066 0.0459  0.2648 -0.0038 69  ASP Z OD2   
7157  N  N     . ARG F 70  ? 0.7923 0.4258 0.3778 0.0415  0.2588 -0.0046 70  ARG Z N     
7158  C  CA    . ARG F 70  ? 0.7794 0.4177 0.361  0.0383  0.2545 -0.0049 70  ARG Z CA    
7159  C  C     . ARG F 70  ? 0.7711 0.4039 0.3502 0.0356  0.2527 -0.0055 70  ARG Z C     
7160  O  O     . ARG F 70  ? 0.7746 0.4045 0.3476 0.0361  0.2522 -0.0054 70  ARG Z O     
7161  C  CB    . ARG F 70  ? 0.7811 0.4272 0.3656 0.0355  0.252  -0.0051 70  ARG Z CB    
7162  C  CG    . ARG F 70  ? 0.7983 0.4492 0.3797 0.0313  0.2474 -0.0054 70  ARG Z CG    
7163  C  CD    . ARG F 70  ? 0.8145 0.4746 0.3974 0.0303  0.2458 -0.0048 70  ARG Z CD    
7164  N  NE    . ARG F 70  ? 0.8273 0.4922 0.4079 0.0257  0.2413 -0.005  70  ARG Z NE    
7165  C  CZ    . ARG F 70  ? 0.8391 0.5083 0.4148 0.0249  0.2391 -0.0044 70  ARG Z CZ    
7166  N  NH1   . ARG F 70  ? 0.8352 0.5044 0.4076 0.0286  0.2408 -0.0035 70  ARG Z NH1   
7167  N  NH2   . ARG F 70  ? 0.8283 0.5017 0.4022 0.0201  0.2349 -0.0045 70  ARG Z NH2   
7168  N  N     . TRP F 71  ? 0.7577 0.3884 0.3409 0.0329  0.2519 -0.0059 71  TRP Z N     
7169  C  CA    . TRP F 71  ? 0.754  0.379  0.3349 0.0306  0.2506 -0.0062 71  TRP Z CA    
7170  C  C     . TRP F 71  ? 0.7521 0.369  0.3342 0.0339  0.2545 -0.0055 71  TRP Z C     
7171  O  O     . TRP F 71  ? 0.7499 0.3664 0.3366 0.0367  0.2576 -0.0049 71  TRP Z O     
7172  C  CB    . TRP F 71  ? 0.7475 0.3748 0.3324 0.0264  0.2479 -0.0068 71  TRP Z CB    
7173  C  CG    . TRP F 71  ? 0.7443 0.3798 0.3291 0.0233  0.2446 -0.0074 71  TRP Z CG    
7174  C  CD1   . TRP F 71  ? 0.7484 0.3898 0.338  0.023   0.2444 -0.0074 71  TRP Z CD1   
7175  C  CD2   . TRP F 71  ? 0.745  0.3837 0.3241 0.0204  0.241  -0.0078 71  TRP Z CD2   
7176  N  NE1   . TRP F 71  ? 0.7498 0.3981 0.3374 0.0204  0.2412 -0.0076 71  TRP Z NE1   
7177  C  CE2   . TRP F 71  ? 0.7494 0.3967 0.331  0.0185  0.2389 -0.0078 71  TRP Z CE2   
7178  C  CE3   . TRP F 71  ? 0.7566 0.3913 0.3283 0.0189  0.2394 -0.008  71  TRP Z CE3   
7179  C  CZ2   . TRP F 71  ? 0.7561 0.4092 0.334  0.0152  0.2353 -0.0078 71  TRP Z CZ2   
7180  C  CZ3   . TRP F 71  ? 0.766  0.4059 0.3336 0.0152  0.2356 -0.0083 71  TRP Z CZ3   
7181  C  CH2   . TRP F 71  ? 0.7613 0.4108 0.3324 0.0133  0.2335 -0.0081 71  TRP Z CH2   
7182  N  N     . ASN F 72  ? 0.7534 0.3635 0.3311 0.0335  0.2544 -0.0053 72  ASN Z N     
7183  C  CA    . ASN F 72  ? 0.761  0.3632 0.3395 0.0368  0.2582 -0.0042 72  ASN Z CA    
7184  C  C     . ASN F 72  ? 0.7539 0.3564 0.3412 0.0366  0.2598 -0.0034 72  ASN Z C     
7185  O  O     . ASN F 72  ? 0.7545 0.353  0.3449 0.0397  0.2634 -0.002  72  ASN Z O     
7186  C  CB    . ASN F 72  ? 0.7867 0.381  0.3574 0.0365  0.2579 -0.0041 72  ASN Z CB    
7187  C  CG    . ASN F 72  ? 0.8315 0.4238 0.4026 0.033   0.2559 -0.0042 72  ASN Z CG    
7188  O  OD1   . ASN F 72  ? 0.8369 0.4351 0.4114 0.0293  0.2529 -0.005  72  ASN Z OD1   
7189  N  ND2   . ASN F 72  ? 0.8538 0.4374 0.4209 0.0344  0.2578 -0.0033 72  ASN Z ND2   
7190  N  N     . SER F 73  ? 0.7458 0.353  0.3369 0.0327  0.2568 -0.004  73  SER Z N     
7191  C  CA    . SER F 73  ? 0.7446 0.3529 0.3438 0.0317  0.2574 -0.0033 73  SER Z CA    
7192  C  C     . SER F 73  ? 0.7336 0.3493 0.3365 0.0283  0.2545 -0.0044 73  SER Z C     
7193  O  O     . SER F 73  ? 0.7318 0.3512 0.3309 0.0261  0.2515 -0.0055 73  SER Z O     
7194  C  CB    . SER F 73  ? 0.7695 0.3733 0.3687 0.0306  0.2571 -0.0025 73  SER Z CB    
7195  O  OG    . SER F 73  ? 0.804  0.4076 0.3974 0.0274  0.2537 -0.0036 73  SER Z OG    
7196  N  N     . ASN F 74  ? 0.7256 0.3432 0.3356 0.028   0.2555 -0.0039 74  ASN Z N     
7197  C  CA    . ASN F 74  ? 0.7245 0.3479 0.3377 0.0252  0.2533 -0.0048 74  ASN Z CA    
7198  C  C     . ASN F 74  ? 0.7144 0.339  0.3308 0.0213  0.2505 -0.0049 74  ASN Z C     
7199  O  O     . ASN F 74  ? 0.7169 0.3398 0.3384 0.0211  0.2515 -0.0037 74  ASN Z O     
7200  C  CB    . ASN F 74  ? 0.7419 0.3657 0.3596 0.0267  0.256  -0.0043 74  ASN Z CB    
7201  C  CG    . ASN F 74  ? 0.7851 0.4136 0.4038 0.025   0.2546 -0.0052 74  ASN Z CG    
7202  O  OD1   . ASN F 74  ? 0.8024 0.4348 0.4194 0.0224  0.2515 -0.0061 74  ASN Z OD1   
7203  N  ND2   . ASN F 74  ? 0.7928 0.4206 0.4139 0.0263  0.2572 -0.0048 74  ASN Z ND2   
7204  N  N     . ILE F 75  ? 0.701  0.3293 0.315  0.0183  0.247  -0.0061 75  ILE Z N     
7205  C  CA    . ILE F 75  ? 0.6952 0.3248 0.312  0.0147  0.2443 -0.0064 75  ILE Z CA    
7206  C  C     . ILE F 75  ? 0.6822 0.3142 0.3055 0.0133  0.2444 -0.0061 75  ILE Z C     
7207  O  O     . ILE F 75  ? 0.6821 0.3139 0.3093 0.0112  0.2432 -0.0056 75  ILE Z O     
7208  C  CB    . ILE F 75  ? 0.7032 0.3361 0.3156 0.0117  0.2408 -0.0077 75  ILE Z CB    
7209  C  CG1   . ILE F 75  ? 0.7136 0.3457 0.3272 0.0084  0.2384 -0.0078 75  ILE Z CG1   
7210  C  CG2   . ILE F 75  ? 0.708  0.3467 0.3209 0.0109  0.2397 -0.0084 75  ILE Z CG2   
7211  C  CD1   . ILE F 75  ? 0.7309 0.357  0.3426 0.0094  0.2395 -0.0069 75  ILE Z CD1   
7212  N  N     . LEU F 76  ? 0.6672 0.3009 0.2914 0.0146  0.2459 -0.0063 76  LEU Z N     
7213  C  CA    . LEU F 76  ? 0.6575 0.2921 0.2865 0.0133  0.2462 -0.0061 76  LEU Z CA    
7214  C  C     . LEU F 76  ? 0.6525 0.2843 0.287  0.0138  0.2482 -0.0045 76  LEU Z C     
7215  O  O     . LEU F 76  ? 0.6486 0.2812 0.2876 0.0116  0.2476 -0.0041 76  LEU Z O     
7216  C  CB    . LEU F 76  ? 0.6579 0.2936 0.285  0.0151  0.248  -0.0065 76  LEU Z CB    
7217  C  CG    . LEU F 76  ? 0.6734 0.3133 0.2963 0.0145  0.2462 -0.0076 76  LEU Z CG    
7218  C  CD1   . LEU F 76  ? 0.6812 0.3216 0.3013 0.0176  0.2488 -0.0075 76  LEU Z CD1   
7219  C  CD2   . LEU F 76  ? 0.679  0.3213 0.3036 0.0109  0.2435 -0.0082 76  LEU Z CD2   
7220  N  N     . ASP F 77  ? 0.6522 0.2806 0.2862 0.0166  0.2505 -0.0033 77  ASP Z N     
7221  C  CA    . ASP F 77  ? 0.6545 0.2807 0.294  0.0174  0.2526 -0.0013 77  ASP Z CA    
7222  C  C     . ASP F 77  ? 0.6517 0.2793 0.2953 0.0145  0.2502 -0.0004 77  ASP Z C     
7223  O  O     . ASP F 77  ? 0.654  0.2822 0.3037 0.0136  0.2508 0.0012  77  ASP Z O     
7224  C  CB    . ASP F 77  ? 0.6767 0.2987 0.3142 0.0214  0.2558 -0.0001 77  ASP Z CB    
7225  C  CG    . ASP F 77  ? 0.7302 0.3506 0.374  0.0225  0.2583 0.0025  77  ASP Z CG    
7226  O  OD1   . ASP F 77  ? 0.7461 0.3668 0.3934 0.0227  0.2602 0.003   77  ASP Z OD1   
7227  O  OD2   . ASP F 77  ? 0.7475 0.3664 0.3926 0.0231  0.2585 0.0041  77  ASP Z OD2   
7228  N  N     . LEU F 78  ? 0.6436 0.2719 0.2839 0.0128  0.2474 -0.0014 78  LEU Z N     
7229  C  CA    . LEU F 78  ? 0.6394 0.269  0.283  0.0102  0.2452 -0.0007 78  LEU Z CA    
7230  C  C     . LEU F 78  ? 0.6368 0.27   0.2852 0.0068  0.2431 -0.0009 78  LEU Z C     
7231  O  O     . LEU F 78  ? 0.6371 0.2716 0.2904 0.0051  0.2421 0.0005  78  LEU Z O     
7232  C  CB    . LEU F 78  ? 0.6407 0.2698 0.2787 0.009   0.2427 -0.002  78  LEU Z CB    
7233  C  CG    . LEU F 78  ? 0.6589 0.2833 0.2914 0.0116  0.2442 -0.0016 78  LEU Z CG    
7234  C  CD1   . LEU F 78  ? 0.6681 0.2918 0.2948 0.0094  0.2415 -0.003  78  LEU Z CD1   
7235  C  CD2   . LEU F 78  ? 0.6654 0.2864 0.3011 0.014   0.2469 0.0011  78  LEU Z CD2   
7236  N  N     . LEU F 79  ? 0.6315 0.2662 0.2782 0.006   0.2427 -0.0025 79  LEU Z N     
7237  C  CA    . LEU F 79  ? 0.6269 0.2637 0.2766 0.0029  0.2412 -0.0029 79  LEU Z CA    
7238  C  C     . LEU F 79  ? 0.6233 0.2591 0.278  0.0032  0.2435 -0.0012 79  LEU Z C     
7239  O  O     . LEU F 79  ? 0.6177 0.2549 0.2772 0.0003  0.2421 -0.0002 79  LEU Z O     
7240  C  CB    . LEU F 79  ? 0.6302 0.2679 0.2752 0.0025  0.2406 -0.0049 79  LEU Z CB    
7241  C  CG    . LEU F 79  ? 0.6515 0.2912 0.2921 0.0017  0.2381 -0.0063 79  LEU Z CG    
7242  C  CD1   . LEU F 79  ? 0.6608 0.3019 0.297  0.0023  0.2383 -0.0077 79  LEU Z CD1   
7243  C  CD2   . LEU F 79  ? 0.6588 0.3002 0.3015 -0.0019 0.2348 -0.0065 79  LEU Z CD2   
7244  N  N     . SER F 80  ? 0.6256 0.259  0.2793 0.0065  0.2469 -0.0007 80  SER Z N     
7245  C  CA    . SER F 80  ? 0.6306 0.2628 0.2888 0.0068  0.2494 0.001   80  SER Z CA    
7246  C  C     . SER F 80  ? 0.6318 0.2649 0.2964 0.0067  0.2498 0.0037  80  SER Z C     
7247  O  O     . SER F 80  ? 0.6356 0.2696 0.3057 0.005   0.2504 0.0055  80  SER Z O     
7248  C  CB    . SER F 80  ? 0.6447 0.2739 0.2999 0.0106  0.2532 0.0008  80  SER Z CB    
7249  O  OG    . SER F 80  ? 0.6685 0.296  0.3219 0.0141  0.2548 0.0015  80  SER Z OG    
7250  N  N     . GLN F 81  ? 0.6257 0.2587 0.2896 0.0082  0.2494 0.0044  81  GLN Z N     
7251  C  CA    . GLN F 81  ? 0.6243 0.2583 0.2937 0.0086  0.2498 0.0074  81  GLN Z CA    
7252  C  C     . GLN F 81  ? 0.6183 0.2564 0.2926 0.0044  0.2465 0.0081  81  GLN Z C     
7253  O  O     . GLN F 81  ? 0.6188 0.2591 0.2995 0.004   0.2468 0.0111  81  GLN Z O     
7254  C  CB    . GLN F 81  ? 0.6471 0.2786 0.3126 0.0115  0.2505 0.0077  81  GLN Z CB    
7255  C  CG    . GLN F 81  ? 0.7006 0.3277 0.362  0.0159  0.2541 0.0078  81  GLN Z CG    
7256  C  CD    . GLN F 81  ? 0.7647 0.3882 0.4204 0.0181  0.2544 0.0078  81  GLN Z CD    
7257  O  OE1   . GLN F 81  ? 0.7864 0.41   0.4434 0.0177  0.2535 0.0092  81  GLN Z OE1   
7258  N  NE2   . GLN F 81  ? 0.7735 0.3933 0.4226 0.0207  0.2559 0.0064  81  GLN Z NE2   
7259  N  N     . LYS F 82  ? 0.6101 0.2494 0.2815 0.0013  0.2433 0.0057  82  LYS Z N     
7260  C  CA    . LYS F 82  ? 0.6068 0.2494 0.2819 -0.0028 0.2399 0.0061  82  LYS Z CA    
7261  C  C     . LYS F 82  ? 0.6057 0.2491 0.282  -0.0064 0.2386 0.0053  82  LYS Z C     
7262  O  O     . LYS F 82  ? 0.6085 0.254  0.2862 -0.0101 0.2354 0.005   82  LYS Z O     
7263  C  CB    . LYS F 82  ? 0.6269 0.2699 0.2977 -0.0037 0.237  0.0043  82  LYS Z CB    
7264  C  CG    . LYS F 82  ? 0.6647 0.3062 0.334  -0.0009 0.2379 0.0054  82  LYS Z CG    
7265  C  CD    . LYS F 82  ? 0.7092 0.3532 0.3845 -0.0015 0.2373 0.0085  82  LYS Z CD    
7266  C  CE    . LYS F 82  ? 0.7515 0.3981 0.4272 -0.0051 0.2334 0.0077  82  LYS Z CE    
7267  N  NZ    . LYS F 82  ? 0.775  0.4252 0.4575 -0.006  0.2326 0.011   82  LYS Z NZ    
7268  N  N     . GLY F 83  ? 0.5988 0.2398 0.274  -0.0053 0.2412 0.0049  83  GLY Z N     
7269  C  CA    . GLY F 83  ? 0.5984 0.2387 0.2737 -0.0087 0.2406 0.0043  83  GLY Z CA    
7270  C  C     . GLY F 83  ? 0.5967 0.2339 0.2649 -0.0085 0.241  0.0014  83  GLY Z C     
7271  O  O     . GLY F 83  ? 0.5992 0.2347 0.2662 -0.0114 0.2404 0.0008  83  GLY Z O     
7272  N  N     . SER F 84  ? 0.5897 0.2259 0.2526 -0.0052 0.2419 -0.0002 84  SER Z N     
7273  C  CA    . SER F 84  ? 0.5903 0.2243 0.2467 -0.0045 0.2426 -0.0024 84  SER Z CA    
7274  C  C     . SER F 84  ? 0.5917 0.2225 0.2468 -0.0017 0.2467 -0.0021 84  SER Z C     
7275  O  O     . SER F 84  ? 0.5921 0.2221 0.2446 0.0022  0.2489 -0.0023 84  SER Z O     
7276  C  CB    . SER F 84  ? 0.6019 0.2373 0.2537 -0.0025 0.2417 -0.0039 84  SER Z CB    
7277  O  OG    . SER F 84  ? 0.6266 0.2611 0.2727 -0.002  0.2421 -0.0056 84  SER Z OG    
7278  N  N     . PHE F 85  ? 0.5897 0.2182 0.2461 -0.004  0.2476 -0.0015 85  PHE Z N     
7279  C  CA    . PHE F 85  ? 0.5911 0.2157 0.2462 -0.0019 0.2515 -0.0011 85  PHE Z CA    
7280  C  C     . PHE F 85  ? 0.5974 0.2185 0.2448 0       0.2534 -0.003  85  PHE Z C     
7281  O  O     . PHE F 85  ? 0.6032 0.2206 0.2486 0.0021  0.257  -0.0027 85  PHE Z O     
7282  C  CB    . PHE F 85  ? 0.587  0.2105 0.2468 -0.0055 0.2518 0.0005  85  PHE Z CB    
7283  C  CG    . PHE F 85  ? 0.5943 0.2168 0.2529 -0.0107 0.2489 -0.0002 85  PHE Z CG    
7284  C  CD1   . PHE F 85  ? 0.6093 0.2269 0.2607 -0.0113 0.2499 -0.0019 85  PHE Z CD1   
7285  C  CD2   . PHE F 85  ? 0.6008 0.2269 0.2649 -0.0148 0.2454 0.0011  85  PHE Z CD2   
7286  C  CE1   . PHE F 85  ? 0.6202 0.236  0.2695 -0.016  0.2473 -0.0026 85  PHE Z CE1   
7287  C  CE2   . PHE F 85  ? 0.612  0.2369 0.2745 -0.0197 0.2426 0.0004  85  PHE Z CE2   
7288  C  CZ    . PHE F 85  ? 0.6146 0.2338 0.2694 -0.0204 0.2436 -0.0015 85  PHE Z CZ    
7289  N  N     . LEU F 86  ? 0.5969 0.219  0.24   -0.0007 0.2514 -0.0046 86  LEU Z N     
7290  C  CA    . LEU F 86  ? 0.6086 0.228  0.2444 0.0017  0.2534 -0.0059 86  LEU Z CA    
7291  C  C     . LEU F 86  ? 0.6178 0.2404 0.2513 0.0059  0.2539 -0.0063 86  LEU Z C     
7292  O  O     . LEU F 86  ? 0.6171 0.2437 0.2526 0.0053  0.2511 -0.0064 86  LEU Z O     
7293  C  CB    . LEU F 86  ? 0.6124 0.2307 0.2442 -0.0012 0.2513 -0.007  86  LEU Z CB    
7294  C  CG    . LEU F 86  ? 0.6293 0.2437 0.2617 -0.0059 0.2505 -0.0068 86  LEU Z CG    
7295  C  CD1   . LEU F 86  ? 0.6382 0.2508 0.2655 -0.0082 0.2485 -0.0081 86  LEU Z CD1   
7296  C  CD2   . LEU F 86  ? 0.6384 0.2469 0.2685 -0.0051 0.2544 -0.0064 86  LEU Z CD2   
7297  N  N     . TYR F 87  ? 0.6257 0.2465 0.2549 0.0101  0.2574 -0.0064 87  TYR Z N     
7298  C  CA    . TYR F 87  ? 0.6359 0.2599 0.2626 0.0138  0.2577 -0.0066 87  TYR Z CA    
7299  C  C     . TYR F 87  ? 0.6282 0.2549 0.2501 0.0142  0.2564 -0.0075 87  TYR Z C     
7300  O  O     . TYR F 87  ? 0.6287 0.2564 0.2462 0.018   0.2584 -0.0075 87  TYR Z O     
7301  C  CB    . TYR F 87  ? 0.6515 0.2733 0.2764 0.0184  0.2617 -0.006  87  TYR Z CB    
7302  C  CG    . TYR F 87  ? 0.674  0.2991 0.2982 0.0213  0.2613 -0.0059 87  TYR Z CG    
7303  C  CD1   . TYR F 87  ? 0.6898 0.3179 0.3168 0.0194  0.2581 -0.0059 87  TYR Z CD1   
7304  C  CD2   . TYR F 87  ? 0.6914 0.3159 0.3115 0.0259  0.2643 -0.0057 87  TYR Z CD2   
7305  C  CE1   . TYR F 87  ? 0.7051 0.3351 0.3303 0.0216  0.2577 -0.0059 87  TYR Z CE1   
7306  C  CE2   . TYR F 87  ? 0.7065 0.3335 0.3253 0.0281  0.2637 -0.0056 87  TYR Z CE2   
7307  C  CZ    . TYR F 87  ? 0.7207 0.3502 0.3418 0.0258  0.2604 -0.0057 87  TYR Z CZ    
7308  O  OH    . TYR F 87  ? 0.7463 0.3773 0.365  0.0276  0.2598 -0.0057 87  TYR Z OH    
7309  N  N     . GLU F 88  ? 0.6179 0.246  0.2407 0.0105  0.2532 -0.0081 88  GLU Z N     
7310  C  CA    . GLU F 88  ? 0.614  0.2451 0.233  0.0104  0.2516 -0.0087 88  GLU Z CA    
7311  C  C     . GLU F 88  ? 0.6025 0.239  0.2233 0.0101  0.2487 -0.0089 88  GLU Z C     
7312  O  O     . GLU F 88  ? 0.5976 0.2348 0.2226 0.0077  0.2465 -0.0088 88  GLU Z O     
7313  C  CB    . GLU F 88  ? 0.6455 0.2745 0.2643 0.0064  0.2497 -0.0092 88  GLU Z CB    
7314  C  CG    . GLU F 88  ? 0.7031 0.3256 0.3188 0.0062  0.2525 -0.0092 88  GLU Z CG    
7315  C  CD    . GLU F 88  ? 0.7776 0.398  0.3868 0.0065  0.2532 -0.0096 88  GLU Z CD    
7316  O  OE1   . GLU F 88  ? 0.7845 0.409  0.3928 0.0061  0.2509 -0.0099 88  GLU Z OE1   
7317  O  OE2   . GLU F 88  ? 0.8095 0.4236 0.4142 0.0072  0.2562 -0.0095 88  GLU Z OE2   
7318  N  N     . THR F 89  ? 0.597  0.2374 0.2142 0.0126  0.249  -0.0088 89  THR Z N     
7319  C  CA    . THR F 89  ? 0.5971 0.2422 0.2148 0.0123  0.2465 -0.0089 89  THR Z CA    
7320  C  C     . THR F 89  ? 0.6011 0.2506 0.2175 0.0101  0.2434 -0.0093 89  THR Z C     
7321  O  O     . THR F 89  ? 0.6033 0.255  0.2163 0.0116  0.2443 -0.009  89  THR Z O     
7322  C  CB    . THR F 89  ? 0.6076 0.2544 0.2224 0.0164  0.2486 -0.0083 89  THR Z CB    
7323  O  OG1   . THR F 89  ? 0.6211 0.2634 0.2373 0.0184  0.2514 -0.0079 89  THR Z OG1   
7324  C  CG2   . THR F 89  ? 0.6088 0.2599 0.2229 0.0159  0.246  -0.0084 89  THR Z CG2   
7325  N  N     . PRO F 90  ? 0.5979 0.2488 0.2169 0.0067  0.2401 -0.0098 90  PRO Z N     
7326  C  CA    . PRO F 90  ? 0.5965 0.2516 0.2142 0.0045  0.2372 -0.0102 90  PRO Z CA    
7327  C  C     . PRO F 90  ? 0.5995 0.2601 0.2143 0.0061  0.2368 -0.0098 90  PRO Z C     
7328  O  O     . PRO F 90  ? 0.5971 0.2578 0.211  0.0085  0.2381 -0.0094 90  PRO Z O     
7329  C  CB    . PRO F 90  ? 0.602  0.2563 0.2231 0.0009  0.2343 -0.0108 90  PRO Z CB    
7330  C  CG    . PRO F 90  ? 0.6079 0.2596 0.231  0.0021  0.2354 -0.0104 90  PRO Z CG    
7331  C  CD    . PRO F 90  ? 0.5891 0.2378 0.2119 0.0051  0.2391 -0.0099 90  PRO Z CD    
7332  N  N     . ASP F 91  ? 0.6032 0.2685 0.2165 0.0047  0.2348 -0.0097 91  ASP Z N     
7333  C  CA    . ASP F 91  ? 0.6125 0.2841 0.2234 0.0057  0.234  -0.009  91  ASP Z CA    
7334  C  C     . ASP F 91  ? 0.6245 0.2966 0.2354 0.0036  0.2316 -0.0095 91  ASP Z C     
7335  O  O     . ASP F 91  ? 0.6274 0.3019 0.2361 0.0051  0.2318 -0.0089 91  ASP Z O     
7336  C  CB    . ASP F 91  ? 0.6242 0.3011 0.2337 0.0049  0.2328 -0.0084 91  ASP Z CB    
7337  C  CG    . ASP F 91  ? 0.6655 0.342  0.273  0.0081  0.2359 -0.0074 91  ASP Z CG    
7338  O  OD1   . ASP F 91  ? 0.6736 0.3468 0.2801 0.0113  0.2391 -0.0071 91  ASP Z OD1   
7339  O  OD2   . ASP F 91  ? 0.6849 0.364  0.2913 0.0075  0.2354 -0.0069 91  ASP Z OD2   
7340  N  N     . VAL F 92  ? 0.6278 0.2971 0.2408 0.0003  0.2294 -0.0104 92  VAL Z N     
7341  C  CA    . VAL F 92  ? 0.6365 0.3048 0.2488 -0.0018 0.2274 -0.0109 92  VAL Z CA    
7342  C  C     . VAL F 92  ? 0.6427 0.3051 0.258  -0.0029 0.2274 -0.0114 92  VAL Z C     
7343  O  O     . VAL F 92  ? 0.6453 0.306  0.2636 -0.0038 0.2274 -0.0116 92  VAL Z O     
7344  C  CB    . VAL F 92  ? 0.6472 0.3201 0.2579 -0.0052 0.2241 -0.0111 92  VAL Z CB    
7345  C  CG1   . VAL F 92  ? 0.6579 0.328  0.2673 -0.008  0.222  -0.0118 92  VAL Z CG1   
7346  C  CG2   . VAL F 92  ? 0.6519 0.3318 0.2599 -0.0042 0.2239 -0.0101 92  VAL Z CG2   
7347  N  N     . ILE F 93  ? 0.6447 0.3039 0.2589 -0.0028 0.2274 -0.0114 93  ILE Z N     
7348  C  CA    . ILE F 93  ? 0.6525 0.3067 0.2691 -0.0036 0.2274 -0.0114 93  ILE Z CA    
7349  C  C     . ILE F 93  ? 0.6561 0.3093 0.269  -0.0058 0.2253 -0.0118 93  ILE Z C     
7350  O  O     . ILE F 93  ? 0.6574 0.3104 0.2659 -0.005  0.2254 -0.0118 93  ILE Z O     
7351  C  CB    . ILE F 93  ? 0.6607 0.3106 0.2786 -0.0004 0.2305 -0.0106 93  ILE Z CB    
7352  C  CG1   . ILE F 93  ? 0.6718 0.3217 0.2929 0.0015  0.2328 -0.0103 93  ILE Z CG1   
7353  C  CG2   . ILE F 93  ? 0.6675 0.3129 0.2876 -0.001  0.2305 -0.0102 93  ILE Z CG2   
7354  C  CD1   . ILE F 93  ? 0.6875 0.3337 0.3096 0.0047  0.236  -0.0094 93  ILE Z CD1   
7355  N  N     . ILE F 94  ? 0.6546 0.3069 0.2684 -0.0087 0.2232 -0.0122 94  ILE Z N     
7356  C  CA    . ILE F 94  ? 0.6626 0.3128 0.2723 -0.0109 0.2214 -0.0126 94  ILE Z CA    
7357  C  C     . ILE F 94  ? 0.6665 0.3105 0.277  -0.0099 0.2228 -0.012  94  ILE Z C     
7358  O  O     . ILE F 94  ? 0.6617 0.3048 0.2771 -0.0097 0.2233 -0.0114 94  ILE Z O     
7359  C  CB    . ILE F 94  ? 0.6716 0.3245 0.2811 -0.0146 0.2185 -0.0133 94  ILE Z CB    
7360  C  CG1   . ILE F 94  ? 0.682  0.3416 0.2915 -0.0153 0.2175 -0.0135 94  ILE Z CG1   
7361  C  CG2   . ILE F 94  ? 0.6795 0.3293 0.2839 -0.0172 0.2169 -0.0138 94  ILE Z CG2   
7362  C  CD1   . ILE F 94  ? 0.6954 0.3578 0.305  -0.0186 0.215  -0.0141 94  ILE Z CD1   
7363  N  N     . THR F 95  ? 0.6744 0.314  0.2799 -0.009  0.2236 -0.0118 95  THR Z N     
7364  C  CA    . THR F 95  ? 0.6845 0.3176 0.2899 -0.0075 0.2254 -0.0108 95  THR Z CA    
7365  C  C     . THR F 95  ? 0.6986 0.3271 0.2975 -0.0097 0.2241 -0.0112 95  THR Z C     
7366  O  O     . THR F 95  ? 0.6998 0.3295 0.2933 -0.0122 0.222  -0.0122 95  THR Z O     
7367  C  CB    . THR F 95  ? 0.6961 0.3261 0.3011 -0.0036 0.2285 -0.0099 95  THR Z CB    
7368  O  OG1   . THR F 95  ? 0.7112 0.3394 0.3088 -0.0037 0.2282 -0.0105 95  THR Z OG1   
7369  C  CG2   . THR F 95  ? 0.6965 0.3303 0.3068 -0.0015 0.2301 -0.0096 95  THR Z CG2   
7370  N  N     . SER F 96  ? 0.7074 0.3305 0.3066 -0.0086 0.2254 -0.0101 96  SER Z N     
7371  C  CA    . SER F 96  ? 0.7235 0.3402 0.3156 -0.01   0.225  -0.0103 96  SER Z CA    
7372  C  C     . SER F 96  ? 0.7326 0.3418 0.3205 -0.0066 0.2281 -0.0091 96  SER Z C     
7373  O  O     . SER F 96  ? 0.7298 0.3385 0.3228 -0.0031 0.2308 -0.0075 96  SER Z O     
7374  C  CB    . SER F 96  ? 0.7425 0.3584 0.3377 -0.011  0.2243 -0.0096 96  SER Z CB    
7375  O  OG    . SER F 96  ? 0.7805 0.3891 0.3683 -0.0118 0.2246 -0.0095 96  SER Z OG    
7376  N  N     . LEU F 97  ? 0.7425 0.3456 0.3208 -0.0077 0.2279 -0.0097 97  LEU Z N     
7377  C  CA    . LEU F 97  ? 0.7593 0.354  0.332  -0.0045 0.231  -0.0086 97  LEU Z CA    
7378  C  C     . LEU F 97  ? 0.7738 0.3605 0.3431 -0.0036 0.2326 -0.0073 97  LEU Z C     
7379  O  O     . LEU F 97  ? 0.7786 0.3612 0.3407 -0.0066 0.2311 -0.0082 97  LEU Z O     
7380  C  CB    . LEU F 97  ? 0.7677 0.3588 0.3304 -0.006  0.2301 -0.0098 97  LEU Z CB    
7381  C  CG    . LEU F 97  ? 0.7845 0.3808 0.3486 -0.005  0.2299 -0.0103 97  LEU Z CG    
7382  C  CD1   . LEU F 97  ? 0.796  0.3874 0.3494 -0.0063 0.2292 -0.0111 97  LEU Z CD1   
7383  C  CD2   . LEU F 97  ? 0.7917 0.3877 0.3616 0       0.2335 -0.0088 97  LEU Z CD2   
7384  N  N     . ASN F 98  ? 0.7778 0.3629 0.3524 0.0005  0.2358 -0.005  98  ASN Z N     
7385  C  CA    . ASN F 98  ? 0.7929 0.3708 0.3648 0.0021  0.2378 -0.0032 98  ASN Z CA    
7386  C  C     . ASN F 98  ? 0.8014 0.3738 0.3731 0.0074  0.2423 -0.0007 98  ASN Z C     
7387  O  O     . ASN F 98  ? 0.8009 0.3781 0.3804 0.0098  0.2437 0.0003  98  ASN Z O     
7388  C  CB    . ASN F 98  ? 0.8079 0.3916 0.3887 0.0016  0.2369 -0.0021 98  ASN Z CB    
7389  C  CG    . ASN F 98  ? 0.8483 0.439  0.4318 -0.0031 0.2327 -0.0042 98  ASN Z CG    
7390  O  OD1   . ASN F 98  ? 0.8663 0.4548 0.4456 -0.0057 0.2311 -0.0049 98  ASN Z OD1   
7391  N  ND2   . ASN F 98  ? 0.8478 0.4469 0.4386 -0.0039 0.2312 -0.005  98  ASN Z ND2   
7392  N  N     . ASN F 99  ? 0.8076 0.3693 0.3702 0.0093  0.2448 0.0005  99  ASN Z N     
7393  C  CA    . ASN F 99  ? 0.814  0.3683 0.3743 0.0147  0.2496 0.0032  99  ASN Z CA    
7394  C  C     . ASN F 99  ? 0.8061 0.3616 0.3678 0.017   0.2511 0.003   99  ASN Z C     
7395  O  O     . ASN F 99  ? 0.8094 0.3656 0.3771 0.0213  0.2543 0.0055  99  ASN Z O     
7396  C  CB    . ASN F 99  ? 0.8317 0.3879 0.4005 0.0183  0.2523 0.0067  99  ASN Z CB    
7397  C  CG    . ASN F 99  ? 0.8712 0.4396 0.4541 0.0174  0.2505 0.0073  99  ASN Z CG    
7398  O  OD1   . ASN F 99  ? 0.8842 0.458  0.4743 0.0187  0.2511 0.0077  99  ASN Z OD1   
7399  N  ND2   . ASN F 99  ? 0.877  0.4495 0.4637 0.015   0.2482 0.0073  99  ASN Z ND2   
7400  N  N     . GLY F 100 ? 0.7931 0.3485 0.3487 0.0142  0.2487 0.0003  100 GLY Z N     
7401  C  CA    . GLY F 100 ? 0.7842 0.3402 0.3396 0.0163  0.2499 0       100 GLY Z CA    
7402  C  C     . GLY F 100 ? 0.7633 0.3299 0.3305 0.017   0.2495 0       100 GLY Z C     
7403  O  O     . GLY F 100 ? 0.7641 0.3305 0.3323 0.0199  0.2515 0.0004  100 GLY Z O     
7404  N  N     . LYS F 101 ? 0.743  0.3181 0.3186 0.0144  0.2469 -0.0005 101 LYS Z N     
7405  C  CA    . LYS F 101 ? 0.7265 0.311  0.3126 0.0146  0.2464 -0.0005 101 LYS Z CA    
7406  C  C     . LYS F 101 ? 0.7084 0.301  0.2981 0.01    0.2422 -0.0026 101 LYS Z C     
7407  O  O     . LYS F 101 ? 0.7084 0.3003 0.2947 0.0069  0.2398 -0.0035 101 LYS Z O     
7408  C  CB    . LYS F 101 ? 0.7461 0.3322 0.3414 0.0178  0.2493 0.0024  101 LYS Z CB    
7409  C  CG    . LYS F 101 ? 0.7978 0.3865 0.3978 0.0161  0.2479 0.0034  101 LYS Z CG    
7410  C  CD    . LYS F 101 ? 0.8522 0.4436 0.4617 0.0189  0.2504 0.0067  101 LYS Z CD    
7411  C  CE    . LYS F 101 ? 0.8986 0.4955 0.5146 0.0164  0.2481 0.0073  101 LYS Z CE    
7412  N  NZ    . LYS F 101 ? 0.9252 0.5269 0.5517 0.0183  0.2498 0.0104  101 LYS Z NZ    
7413  N  N     . GLU F 102 ? 0.691  0.291  0.2873 0.0098  0.2415 -0.0032 102 GLU Z N     
7414  C  CA    . GLU F 102 ? 0.6797 0.2872 0.2794 0.006   0.2379 -0.0049 102 GLU Z CA    
7415  C  C     . GLU F 102 ? 0.667  0.2789 0.2759 0.0056  0.2377 -0.0038 102 GLU Z C     
7416  O  O     . GLU F 102 ? 0.6695 0.2815 0.2843 0.0082  0.2401 -0.0019 102 GLU Z O     
7417  C  CB    . GLU F 102 ? 0.6976 0.31   0.2978 0.006   0.2374 -0.0061 102 GLU Z CB    
7418  C  CG    . GLU F 102 ? 0.7465 0.3556 0.3381 0.0065  0.2375 -0.007  102 GLU Z CG    
7419  C  CD    . GLU F 102 ? 0.8119 0.4272 0.4035 0.006   0.2362 -0.0082 102 GLU Z CD    
7420  O  OE1   . GLU F 102 ? 0.8134 0.4351 0.4079 0.0032  0.2337 -0.0091 102 GLU Z OE1   
7421  O  OE2   . GLU F 102 ? 0.8438 0.4576 0.4325 0.0085  0.2379 -0.008  102 GLU Z OE2   
7422  N  N     . GLU F 103 ? 0.6513 0.2669 0.2615 0.002   0.2345 -0.0048 103 GLU Z N     
7423  C  CA    . GLU F 103 ? 0.6406 0.2605 0.2589 0.001   0.2337 -0.004  103 GLU Z CA    
7424  C  C     . GLU F 103 ? 0.631  0.2571 0.2509 -0.0022 0.2307 -0.0059 103 GLU Z C     
7425  O  O     . GLU F 103 ? 0.636  0.2626 0.2511 -0.0048 0.2284 -0.0074 103 GLU Z O     
7426  C  CB    . GLU F 103 ? 0.6645 0.2818 0.2822 0.0001  0.2331 -0.0029 103 GLU Z CB    
7427  C  CG    . GLU F 103 ? 0.7168 0.3283 0.334  0.0038  0.2366 -0.0003 103 GLU Z CG    
7428  C  CD    . GLU F 103 ? 0.7713 0.3774 0.3833 0.0037  0.2366 0.0004  103 GLU Z CD    
7429  O  OE1   . GLU F 103 ? 0.7874 0.3863 0.3938 0.0066  0.2394 0.0017  103 GLU Z OE1   
7430  O  OE2   . GLU F 103 ? 0.777  0.3853 0.3898 0.0009  0.2341 -0.0002 103 GLU Z OE2   
7431  N  N     . ILE F 104 ? 0.6162 0.2465 0.2422 -0.002  0.231  -0.0057 104 ILE Z N     
7432  C  CA    . ILE F 104 ? 0.6083 0.2436 0.2352 -0.0046 0.2286 -0.0073 104 ILE Z CA    
7433  C  C     . ILE F 104 ? 0.6012 0.2382 0.229  -0.0079 0.2257 -0.0078 104 ILE Z C     
7434  O  O     . ILE F 104 ? 0.5994 0.2361 0.2313 -0.0082 0.2256 -0.0066 104 ILE Z O     
7435  C  CB    . ILE F 104 ? 0.6081 0.246  0.2402 -0.0036 0.2299 -0.007  104 ILE Z CB    
7436  C  CG1   . ILE F 104 ? 0.6177 0.2542 0.2476 -0.0004 0.2327 -0.0069 104 ILE Z CG1   
7437  C  CG2   . ILE F 104 ? 0.6101 0.2522 0.2429 -0.0062 0.2277 -0.0083 104 ILE Z CG2   
7438  C  CD1   . ILE F 104 ? 0.6296 0.2675 0.2634 0.0008  0.2344 -0.0065 104 ILE Z CD1   
7439  N  N     . LEU F 105 ? 0.5968 0.2362 0.2209 -0.0103 0.2234 -0.0095 105 LEU Z N     
7440  C  CA    . LEU F 105 ? 0.5988 0.2401 0.2232 -0.0135 0.2206 -0.0102 105 LEU Z CA    
7441  C  C     . LEU F 105 ? 0.5981 0.2436 0.2259 -0.0147 0.2195 -0.0108 105 LEU Z C     
7442  O  O     . LEU F 105 ? 0.5971 0.2436 0.2279 -0.0166 0.2179 -0.0107 105 LEU Z O     
7443  C  CB    . LEU F 105 ? 0.6023 0.2434 0.2202 -0.0156 0.2188 -0.0115 105 LEU Z CB    
7444  C  CG    . LEU F 105 ? 0.6207 0.2562 0.2332 -0.0152 0.2195 -0.0112 105 LEU Z CG    
7445  C  CD1   . LEU F 105 ? 0.629  0.2647 0.235  -0.018  0.2174 -0.0126 105 LEU Z CD1   
7446  C  CD2   . LEU F 105 ? 0.6276 0.2597 0.2421 -0.015  0.2198 -0.01   105 LEU Z CD2   
7447  N  N     . MET F 106 ? 0.598  0.2458 0.2247 -0.0136 0.2204 -0.0114 106 MET Z N     
7448  C  CA    . MET F 106 ? 0.6022 0.253  0.2308 -0.0143 0.22   -0.0118 106 MET Z CA    
7449  C  C     . MET F 106 ? 0.6032 0.2555 0.2302 -0.0118 0.2221 -0.0119 106 MET Z C     
7450  O  O     . MET F 106 ? 0.6048 0.2568 0.2287 -0.0102 0.223  -0.0119 106 MET Z O     
7451  C  CB    . MET F 106 ? 0.6101 0.2636 0.2369 -0.0172 0.2173 -0.0128 106 MET Z CB    
7452  C  CG    . MET F 106 ? 0.637  0.2934 0.2591 -0.0174 0.2167 -0.0135 106 MET Z CG    
7453  S  SD    . MET F 106 ? 0.6769 0.3361 0.2971 -0.021  0.2135 -0.0144 106 MET Z SD    
7454  C  CE    . MET F 106 ? 0.6546 0.3096 0.2735 -0.0226 0.2124 -0.0144 106 MET Z CE    
7455  N  N     . ALA F 107 ? 0.5975 0.2508 0.2261 -0.0116 0.2227 -0.012  107 ALA Z N     
7456  C  CA    . ALA F 107 ? 0.5977 0.2521 0.2245 -0.0092 0.2248 -0.012  107 ALA Z CA    
7457  C  C     . ALA F 107 ? 0.5971 0.2548 0.2217 -0.0103 0.2236 -0.0125 107 ALA Z C     
7458  O  O     . ALA F 107 ? 0.5974 0.2546 0.2233 -0.0126 0.2221 -0.0128 107 ALA Z O     
7459  C  CB    . ALA F 107 ? 0.5984 0.25   0.2281 -0.0078 0.2271 -0.0113 107 ALA Z CB    
7460  N  N     . ILE F 108 ? 0.5937 0.2549 0.2151 -0.0087 0.2243 -0.0124 108 ILE Z N     
7461  C  CA    . ILE F 108 ? 0.5961 0.2609 0.2153 -0.0093 0.2235 -0.0124 108 ILE Z CA    
7462  C  C     . ILE F 108 ? 0.5948 0.2611 0.2119 -0.006  0.2263 -0.0117 108 ILE Z C     
7463  O  O     . ILE F 108 ? 0.5966 0.2637 0.2127 -0.0034 0.228  -0.0112 108 ILE Z O     
7464  C  CB    . ILE F 108 ? 0.605  0.2742 0.2221 -0.0111 0.2211 -0.0126 108 ILE Z CB    
7465  C  CG1   . ILE F 108 ? 0.615  0.2822 0.2333 -0.0144 0.2186 -0.0133 108 ILE Z CG1   
7466  C  CG2   . ILE F 108 ? 0.6135 0.2875 0.2288 -0.0115 0.2205 -0.0122 108 ILE Z CG2   
7467  C  CD1   . ILE F 108 ? 0.6303 0.3002 0.2457 -0.0162 0.2167 -0.0134 108 ILE Z CD1   
7468  N  N     . GLU F 109 ? 0.5896 0.2557 0.2056 -0.0059 0.2269 -0.0115 109 GLU Z N     
7469  C  CA    . GLU F 109 ? 0.591  0.2578 0.2041 -0.0024 0.2299 -0.0106 109 GLU Z CA    
7470  C  C     . GLU F 109 ? 0.6003 0.2717 0.211  -0.0025 0.2293 -0.0099 109 GLU Z C     
7471  O  O     . GLU F 109 ? 0.6011 0.2715 0.212  -0.0051 0.2275 -0.0105 109 GLU Z O     
7472  C  CB    . GLU F 109 ? 0.6062 0.2666 0.2192 -0.0017 0.2321 -0.0108 109 GLU Z CB    
7473  C  CG    . GLU F 109 ? 0.6581 0.3177 0.2671 0.0019  0.2356 -0.0099 109 GLU Z CG    
7474  C  CD    . GLU F 109 ? 0.7318 0.3922 0.34   0.0058  0.2384 -0.0091 109 GLU Z CD    
7475  O  OE1   . GLU F 109 ? 0.7495 0.4086 0.3603 0.0056  0.2382 -0.0095 109 GLU Z OE1   
7476  O  OE2   . GLU F 109 ? 0.7549 0.4168 0.3595 0.0093  0.2411 -0.008  109 GLU Z OE2   
7477  N  N     . PHE F 110 ? 0.6043 0.281  0.2128 0.0004  0.2306 -0.0086 110 PHE Z N     
7478  C  CA    . PHE F 110 ? 0.6117 0.294  0.2182 0.0009  0.2305 -0.0073 110 PHE Z CA    
7479  C  C     . PHE F 110 ? 0.623  0.3036 0.2261 0.005   0.2344 -0.006  110 PHE Z C     
7480  O  O     . PHE F 110 ? 0.626  0.3068 0.228  0.0085  0.237  -0.0052 110 PHE Z O     
7481  C  CB    . PHE F 110 ? 0.606  0.2967 0.2125 0.0012  0.2292 -0.0061 110 PHE Z CB    
7482  C  CG    . PHE F 110 ? 0.6077 0.2992 0.216  -0.0022 0.2261 -0.0072 110 PHE Z CG    
7483  C  CD1   . PHE F 110 ? 0.6176 0.3078 0.2271 -0.0063 0.2231 -0.0084 110 PHE Z CD1   
7484  C  CD2   . PHE F 110 ? 0.6096 0.3027 0.2175 -0.0012 0.2262 -0.007  110 PHE Z CD2   
7485  C  CE1   . PHE F 110 ? 0.6222 0.3124 0.2324 -0.0093 0.2206 -0.0093 110 PHE Z CE1   
7486  C  CE2   . PHE F 110 ? 0.616  0.3088 0.2243 -0.0044 0.2235 -0.008  110 PHE Z CE2   
7487  C  CZ    . PHE F 110 ? 0.6149 0.3061 0.2243 -0.0083 0.2208 -0.0091 110 PHE Z CZ    
7488  N  N     . CYS F 111 ? 0.6304 0.3089 0.2313 0.0049  0.235  -0.0057 111 CYS Z N     
7489  C  CA    . CYS F 111 ? 0.6465 0.322  0.2429 0.0089  0.239  -0.0044 111 CYS Z CA    
7490  C  C     . CYS F 111 ? 0.6479 0.3278 0.2415 0.0104  0.2398 -0.0025 111 CYS Z C     
7491  O  O     . CYS F 111 ? 0.6477 0.325  0.2404 0.0081  0.2385 -0.003  111 CYS Z O     
7492  C  CB    . CYS F 111 ? 0.6693 0.3344 0.2638 0.0081  0.2404 -0.0058 111 CYS Z CB    
7493  S  SG    . CYS F 111 ? 0.7379 0.3969 0.3259 0.0133  0.2461 -0.0044 111 CYS Z SG    
7494  N  N     . SER F 112 ? 0.6472 0.3338 0.2395 0.0145  0.242  0       112 SER Z N     
7495  C  CA    . SER F 112 ? 0.6525 0.3441 0.2422 0.0169  0.2435 0.0025  112 SER Z CA    
7496  C  C     . SER F 112 ? 0.6569 0.3413 0.2405 0.0211  0.2482 0.0036  112 SER Z C     
7497  O  O     . SER F 112 ? 0.6629 0.3471 0.2433 0.0222  0.2495 0.005   112 SER Z O     
7498  C  CB    . SER F 112 ? 0.6716 0.3748 0.263  0.0193  0.2436 0.0051  112 SER Z CB    
7499  O  OG    . SER F 112 ? 0.7017 0.4124 0.2967 0.0153  0.2395 0.0051  112 SER Z OG    
7500  N  N     . ALA F 113 ? 0.6524 0.3305 0.2338 0.0234  0.2511 0.003   113 ALA Z N     
7501  C  CA    . ALA F 113 ? 0.6567 0.3263 0.2314 0.0274  0.256  0.0038  113 ALA Z CA    
7502  C  C     . ALA F 113 ? 0.6545 0.3159 0.2242 0.0263  0.2568 0.0034  113 ALA Z C     
7503  O  O     . ALA F 113 ? 0.6572 0.316  0.229  0.0214  0.2532 0.0013  113 ALA Z O     
7504  C  CB    . ALA F 113 ? 0.6628 0.3249 0.2372 0.0274  0.2573 0.002   113 ALA Z CB    
7505  N  N     . LEU F 114 ? 0.6482 0.3047 0.2105 0.0311  0.2617 0.0053  114 LEU Z N     
7506  C  CA    . LEU F 114 ? 0.6482 0.2953 0.2039 0.0305  0.2631 0.0051  114 LEU Z CA    
7507  C  C     . LEU F 114 ? 0.6528 0.2883 0.2071 0.0261  0.2618 0.0019  114 LEU Z C     
7508  O  O     . LEU F 114 ? 0.6598 0.2907 0.2135 0.0268  0.2635 0.0011  114 LEU Z O     
7509  C  CB    . LEU F 114 ? 0.6482 0.2905 0.195  0.0369  0.2693 0.0079  114 LEU Z CB    
7510  C  CG    . LEU F 114 ? 0.6563 0.3097 0.2033 0.0423  0.2716 0.0119  114 LEU Z CG    
7511  C  CD1   . LEU F 114 ? 0.6663 0.3133 0.2038 0.049   0.2783 0.0146  114 LEU Z CD1   
7512  C  CD2   . LEU F 114 ? 0.6599 0.3195 0.2093 0.0402  0.2689 0.0128  114 LEU Z CD2   
7513  N  N     . GLN F 115 ? 0.6483 0.2797 0.2026 0.0215  0.2587 0.0002  115 GLN Z N     
7514  C  CA    . GLN F 115 ? 0.6518 0.2729 0.2049 0.0169  0.2571 -0.0025 115 GLN Z CA    
7515  C  C     . GLN F 115 ? 0.6511 0.2599 0.1933 0.0192  0.2617 -0.0019 115 GLN Z C     
7516  O  O     . GLN F 115 ? 0.661  0.2632 0.1983 0.0172  0.2611 -0.0023 115 GLN Z O     
7517  C  CB    . GLN F 115 ? 0.6746 0.2967 0.2317 0.0112  0.252  -0.0042 115 GLN Z CB    
7518  C  CG    . GLN F 115 ? 0.7138 0.3479 0.2801 0.0094  0.248  -0.0044 115 GLN Z CG    
7519  C  CD    . GLN F 115 ? 0.7744 0.4092 0.3471 0.0063  0.2454 -0.0062 115 GLN Z CD    
7520  O  OE1   . GLN F 115 ? 0.7957 0.4268 0.3708 0.0017  0.2422 -0.0081 115 GLN Z OE1   
7521  N  NE2   . GLN F 115 ? 0.7824 0.4223 0.358  0.009   0.2467 -0.0056 115 GLN Z NE2   
7522  N  N     . ALA F 116 ? 0.6389 0.2444 0.1767 0.0238  0.2664 -0.0007 116 ALA Z N     
7523  C  CA    . ALA F 116 ? 0.6425 0.2354 0.1687 0.0266  0.2714 0       116 ALA Z CA    
7524  C  C     . ALA F 116 ? 0.6398 0.2209 0.1658 0.0234  0.2704 -0.0019 116 ALA Z C     
7525  O  O     . ALA F 116 ? 0.636  0.2169 0.1656 0.0253  0.2711 -0.0015 116 ALA Z O     
7526  C  CB    . ALA F 116 ? 0.6421 0.2374 0.1676 0.0341  0.2749 0.0035  116 ALA Z CB    
7527  N  N     . GLY F 117 ? 0.639  0.2098 0.1635 0.0183  0.2671 -0.0034 117 GLY Z N     
7528  C  CA    . GLY F 117 ? 0.6445 0.2049 0.1631 0.0146  0.2687 -0.0056 117 GLY Z CA    
7529  C  C     . GLY F 117 ? 0.6349 0.2009 0.1629 0.0115  0.266  -0.007  117 GLY Z C     
7530  O  O     . GLY F 117 ? 0.6307 0.203  0.1649 0.007   0.2619 -0.0085 117 GLY Z O     
7531  N  N     . ASN F 118 ? 0.6302 0.1925 0.1625 0.0139  0.2663 -0.0061 118 ASN Z N     
7532  C  CA    . ASN F 118 ? 0.6311 0.1995 0.1646 0.0118  0.2684 -0.008  118 ASN Z CA    
7533  C  C     . ASN F 118 ? 0.6216 0.2042 0.1653 0.0138  0.2663 -0.0074 118 ASN Z C     
7534  O  O     . ASN F 118 ? 0.6194 0.206  0.1709 0.0113  0.2638 -0.0083 118 ASN Z O     
7535  C  CB    . ASN F 118 ? 0.6554 0.2153 0.1839 0.0134  0.2727 -0.008  118 ASN Z CB    
7536  C  CG    . ASN F 118 ? 0.7062 0.2664 0.2293 0.0209  0.2785 -0.006  118 ASN Z CG    
7537  O  OD1   . ASN F 118 ? 0.7192 0.288  0.2437 0.0253  0.2791 -0.0043 118 ASN Z OD1   
7538  N  ND2   . ASN F 118 ? 0.7217 0.2727 0.2385 0.0225  0.2828 -0.0059 118 ASN Z ND2   
7539  N  N     . GLN F 119 ? 0.6136 0.2021 0.1633 0.0177  0.2635 -0.005  119 GLN Z N     
7540  C  CA    . GLN F 119 ? 0.6091 0.2116 0.165  0.019   0.2626 -0.0047 119 GLN Z CA    
7541  C  C     . GLN F 119 ? 0.6051 0.2135 0.1653 0.0135  0.2588 -0.0067 119 GLN Z C     
7542  O  O     . GLN F 119 ? 0.6021 0.2185 0.17   0.0128  0.2563 -0.007  119 GLN Z O     
7543  C  CB    . GLN F 119 ? 0.6294 0.2398 0.1794 0.0246  0.2669 -0.0026 119 GLN Z CB    
7544  C  CG    . GLN F 119 ? 0.6791 0.2979 0.2324 0.0291  0.2687 -0.0011 119 GLN Z CG    
7545  C  CD    . GLN F 119 ? 0.7424 0.3727 0.3051 0.0269  0.2641 -0.0015 119 GLN Z CD    
7546  O  OE1   . GLN F 119 ? 0.7737 0.408  0.3398 0.0234  0.2602 -0.0021 119 GLN Z OE1   
7547  N  NE2   . GLN F 119 ? 0.737  0.3723 0.3034 0.029   0.2646 -0.0012 119 GLN Z NE2   
7548  N  N     . ALA F 120 ? 0.604  0.207  0.162  0.0095  0.2564 -0.0076 120 ALA Z N     
7549  C  CA    . ALA F 120 ? 0.6013 0.2077 0.1653 0.0041  0.2512 -0.0091 120 ALA Z CA    
7550  C  C     . ALA F 120 ? 0.5978 0.2038 0.1684 0.0005  0.2489 -0.0104 120 ALA Z C     
7551  O  O     . ALA F 120 ? 0.5982 0.2108 0.1763 -0.002  0.2451 -0.011  120 ALA Z O     
7552  C  CB    . ALA F 120 ? 0.6093 0.2081 0.1677 0.0011  0.2501 -0.0097 120 ALA Z CB    
7553  N  N     . TRP F 121 ? 0.5934 0.1915 0.1608 0.0002  0.2513 -0.0108 121 TRP Z N     
7554  C  CA    . TRP F 121 ? 0.5882 0.1861 0.1618 -0.003  0.2496 -0.0116 121 TRP Z CA    
7555  C  C     . TRP F 121 ? 0.5867 0.1872 0.1628 0.0007  0.2524 -0.011  121 TRP Z C     
7556  O  O     . TRP F 121 ? 0.5863 0.1862 0.1672 -0.0014 0.2516 -0.0114 121 TRP Z O     
7557  C  CB    . TRP F 121 ? 0.5895 0.1775 0.1596 -0.0076 0.2492 -0.0124 121 TRP Z CB    
7558  C  CG    . TRP F 121 ? 0.5997 0.1773 0.1603 -0.0056 0.2539 -0.0122 121 TRP Z CG    
7559  C  CD1   . TRP F 121 ? 0.6123 0.1864 0.1718 -0.0037 0.2574 -0.0119 121 TRP Z CD1   
7560  C  CD2   . TRP F 121 ? 0.6064 0.1739 0.1581 -0.0061 0.2547 -0.0121 121 TRP Z CD2   
7561  N  NE1   . TRP F 121 ? 0.6223 0.1851 0.171  -0.0028 0.2613 -0.0117 121 TRP Z NE1   
7562  C  CE2   . TRP F 121 ? 0.6213 0.1799 0.1639 -0.0043 0.2603 -0.012  121 TRP Z CE2   
7563  C  CE3   . TRP F 121 ? 0.6131 0.1789 0.1589 -0.0076 0.2539 -0.0125 121 TRP Z CE3   
7564  C  CZ2   . TRP F 121 ? 0.6348 0.1815 0.1652 -0.004  0.2632 -0.0119 121 TRP Z CZ2   
7565  C  CZ3   . TRP F 121 ? 0.629  0.1833 0.1631 -0.0073 0.2568 -0.0124 121 TRP Z CZ3   
7566  C  CH2   . TRP F 121 ? 0.6366 0.1813 0.1628 -0.0054 0.2615 -0.0121 121 TRP Z CH2   
7567  N  N     . GLN F 122 ? 0.584  0.1869 0.1619 0.006   0.2529 -0.0093 122 GLN Z N     
7568  C  CA    . GLN F 122 ? 0.5927 0.1994 0.168  0.01    0.2583 -0.0091 122 GLN Z CA    
7569  C  C     . GLN F 122 ? 0.6006 0.2141 0.185  0.0082  0.255  -0.0096 122 GLN Z C     
7570  O  O     . GLN F 122 ? 0.6096 0.2216 0.1967 0.0086  0.2563 -0.0097 122 GLN Z O     
7571  C  CB    . GLN F 122 ? 0.608  0.2195 0.1797 0.016   0.2612 -0.0074 122 GLN Z CB    
7572  C  CG    . GLN F 122 ? 0.6426 0.2575 0.2161 0.0201  0.2638 -0.0067 122 GLN Z CG    
7573  C  CD    . GLN F 122 ? 0.7024 0.3215 0.2717 0.0261  0.2671 -0.0047 122 GLN Z CD    
7574  O  OE1   . GLN F 122 ? 0.739  0.3521 0.3012 0.0298  0.2717 -0.0037 122 GLN Z OE1   
7575  N  NE2   . GLN F 122 ? 0.6973 0.3269 0.2707 0.0273  0.2649 -0.0038 122 GLN Z NE2   
7576  N  N     . ARG F 123 ? 0.5951 0.2155 0.184  0.0062  0.2511 -0.0099 123 ARG Z N     
7577  C  CA    . ARG F 123 ? 0.5939 0.2199 0.1904 0.0045  0.2481 -0.0102 123 ARG Z CA    
7578  C  C     . ARG F 123 ? 0.5969 0.2214 0.1977 -0.0009 0.2443 -0.0112 123 ARG Z C     
7579  O  O     . ARG F 123 ? 0.594  0.2238 0.2    -0.0027 0.2412 -0.0115 123 ARG Z O     
7580  C  CB    . ARG F 123 ? 0.601  0.236  0.1995 0.0064  0.2467 -0.0097 123 ARG Z CB    
7581  C  CG    . ARG F 123 ? 0.6328 0.2711 0.2278 0.0073  0.2463 -0.0091 123 ARG Z CG    
7582  C  CD    . ARG F 123 ? 0.6621 0.309  0.258  0.0105  0.2465 -0.008  123 ARG Z CD    
7583  N  NE    . ARG F 123 ? 0.6942 0.3405 0.2842 0.0149  0.2503 -0.0065 123 ARG Z NE    
7584  C  CZ    . ARG F 123 ? 0.7201 0.373  0.3086 0.0188  0.2517 -0.0047 123 ARG Z CZ    
7585  N  NH1   . ARG F 123 ? 0.7139 0.365  0.2966 0.0229  0.2557 -0.0031 123 ARG Z NH1   
7586  N  NH2   . ARG F 123 ? 0.7196 0.3809 0.3118 0.0185  0.2494 -0.0043 123 ARG Z NH2   
7587  N  N     . SER F 124 ? 0.5996 0.2168 0.198  -0.0037 0.2447 -0.0116 124 SER Z N     
7588  C  CA    . SER F 124 ? 0.6059 0.222  0.2088 -0.0088 0.2411 -0.0122 124 SER Z CA    
7589  C  C     . SER F 124 ? 0.6083 0.2253 0.2176 -0.0096 0.2411 -0.0118 124 SER Z C     
7590  O  O     . SER F 124 ? 0.6098 0.2289 0.2248 -0.013  0.2379 -0.0118 124 SER Z O     
7591  C  CB    . SER F 124 ? 0.6296 0.2378 0.2272 -0.012  0.241  -0.0126 124 SER Z CB    
7592  O  OG    . SER F 124 ? 0.669  0.2774 0.2628 -0.0125 0.2396 -0.013  124 SER Z OG    
7593  N  N     . GLY F 125 ? 0.605  0.2206 0.2135 -0.0063 0.2446 -0.0113 125 GLY Z N     
7594  C  CA    . GLY F 125 ? 0.6088 0.2251 0.223  -0.0064 0.2452 -0.0107 125 GLY Z CA    
7595  C  C     . GLY F 125 ? 0.6084 0.2316 0.2287 -0.0061 0.2428 -0.0104 125 GLY Z C     
7596  O  O     . GLY F 125 ? 0.6072 0.2313 0.2334 -0.0082 0.2413 -0.0099 125 GLY Z O     
7597  N  N     . ARG F 126 ? 0.6073 0.235  0.226  -0.0036 0.2424 -0.0107 126 ARG Z N     
7598  C  CA    . ARG F 126 ? 0.6106 0.2438 0.2338 -0.0036 0.2401 -0.0106 126 ARG Z CA    
7599  C  C     . ARG F 126 ? 0.6158 0.2505 0.2422 -0.0078 0.2362 -0.0109 126 ARG Z C     
7600  O  O     . ARG F 126 ? 0.6148 0.2513 0.2461 -0.0089 0.2347 -0.0104 126 ARG Z O     
7601  C  CB    . ARG F 126 ? 0.6215 0.2594 0.2421 -0.0004 0.2405 -0.0106 126 ARG Z CB    
7602  C  CG    . ARG F 126 ? 0.6446 0.2836 0.2601 0.0005  0.2407 -0.0108 126 ARG Z CG    
7603  C  CD    . ARG F 126 ? 0.6608 0.3045 0.2739 0.0043  0.242  -0.0103 126 ARG Z CD    
7604  N  NE    . ARG F 126 ? 0.674  0.315  0.2845 0.0082  0.2461 -0.0097 126 ARG Z NE    
7605  C  CZ    . ARG F 126 ? 0.6831 0.3253 0.289  0.0119  0.2487 -0.0089 126 ARG Z CZ    
7606  N  NH1   . ARG F 126 ? 0.6737 0.3204 0.2773 0.0123  0.2476 -0.0085 126 ARG Z NH1   
7607  N  NH2   . ARG F 126 ? 0.6804 0.3193 0.2839 0.0153  0.2525 -0.0084 126 ARG Z NH2   
7608  N  N     . ALA F 127 ? 0.6219 0.2553 0.2453 -0.0099 0.2347 -0.0115 127 ALA Z N     
7609  C  CA    . ALA F 127 ? 0.6322 0.2666 0.2582 -0.0139 0.231  -0.0118 127 ALA Z CA    
7610  C  C     . ALA F 127 ? 0.6369 0.2692 0.2677 -0.0169 0.2301 -0.0111 127 ALA Z C     
7611  O  O     . ALA F 127 ? 0.6365 0.2715 0.2721 -0.0188 0.2275 -0.0106 127 ALA Z O     
7612  C  CB    . ALA F 127 ? 0.6374 0.2697 0.2584 -0.0154 0.2301 -0.0125 127 ALA Z CB    
7613  N  N     . TYR F 128 ? 0.6369 0.2644 0.2663 -0.0171 0.2323 -0.0108 128 TYR Z N     
7614  C  CA    . TYR F 128 ? 0.638  0.2641 0.272  -0.0203 0.2315 -0.0098 128 TYR Z CA    
7615  C  C     . TYR F 128 ? 0.6379 0.2673 0.2784 -0.0186 0.2323 -0.0084 128 TYR Z C     
7616  O  O     . TYR F 128 ? 0.6394 0.2716 0.2856 -0.0208 0.23   -0.0074 128 TYR Z O     
7617  C  CB    . TYR F 128 ? 0.639  0.2585 0.269  -0.0212 0.2339 -0.0098 128 TYR Z CB    
7618  C  CG    . TYR F 128 ? 0.6436 0.2623 0.2789 -0.0238 0.2339 -0.0084 128 TYR Z CG    
7619  C  CD1   . TYR F 128 ? 0.6517 0.2716 0.2911 -0.0286 0.2304 -0.0076 128 TYR Z CD1   
7620  C  CD2   . TYR F 128 ? 0.6552 0.273  0.2923 -0.0213 0.2372 -0.0075 128 TYR Z CD2   
7621  C  CE1   . TYR F 128 ? 0.6602 0.2808 0.3055 -0.0311 0.2302 -0.0059 128 TYR Z CE1   
7622  C  CE2   . TYR F 128 ? 0.6643 0.2823 0.3071 -0.0237 0.2372 -0.0059 128 TYR Z CE2   
7623  C  CZ    . TYR F 128 ? 0.6729 0.2926 0.3199 -0.0286 0.2337 -0.0049 128 TYR Z CZ    
7624  O  OH    . TYR F 128 ? 0.69   0.3108 0.3431 -0.031  0.2337 -0.0028 128 TYR Z OH    
7625  N  N     . SER F 129 ? 0.6337 0.2627 0.2729 -0.0145 0.2356 -0.0083 129 SER Z N     
7626  C  CA    . SER F 129 ? 0.6329 0.2638 0.2771 -0.0124 0.237  -0.007  129 SER Z CA    
7627  C  C     . SER F 129 ? 0.6246 0.2599 0.2716 -0.0119 0.2349 -0.0068 129 SER Z C     
7628  O  O     . SER F 129 ? 0.6224 0.2593 0.2748 -0.0125 0.2343 -0.0053 129 SER Z O     
7629  C  CB    . SER F 129 ? 0.6549 0.2839 0.296  -0.0081 0.241  -0.0071 129 SER Z CB    
7630  O  OG    . SER F 129 ? 0.6893 0.3197 0.3254 -0.0053 0.2414 -0.0082 129 SER Z OG    
7631  N  N     . VAL F 130 ? 0.6182 0.2554 0.2614 -0.0108 0.2339 -0.008  130 VAL Z N     
7632  C  CA    . VAL F 130 ? 0.6143 0.2547 0.2589 -0.0107 0.2318 -0.008  130 VAL Z CA    
7633  C  C     . VAL F 130 ? 0.6108 0.2526 0.2586 -0.0145 0.2284 -0.0077 130 VAL Z C     
7634  O  O     . VAL F 130 ? 0.6118 0.2552 0.2632 -0.0146 0.2274 -0.0066 130 VAL Z O     
7635  C  CB    . VAL F 130 ? 0.6223 0.2647 0.2619 -0.0089 0.2316 -0.0093 130 VAL Z CB    
7636  C  CG1   . VAL F 130 ? 0.6294 0.2743 0.2696 -0.0096 0.2292 -0.0094 130 VAL Z CG1   
7637  C  CG2   . VAL F 130 ? 0.6298 0.2716 0.2666 -0.005  0.2348 -0.0092 130 VAL Z CG2   
7638  N  N     . GLY F 131 ? 0.6055 0.2461 0.2518 -0.0173 0.2269 -0.0084 131 GLY Z N     
7639  C  CA    . GLY F 131 ? 0.6044 0.2461 0.2533 -0.021  0.2236 -0.0081 131 GLY Z CA    
7640  C  C     . GLY F 131 ? 0.6    0.2426 0.2555 -0.0226 0.2231 -0.006  131 GLY Z C     
7641  O  O     . GLY F 131 ? 0.5977 0.2427 0.2564 -0.0243 0.2206 -0.0052 131 GLY Z O     
7642  N  N     . ARG F 132 ? 0.5962 0.2373 0.2539 -0.0219 0.2255 -0.0049 132 ARG Z N     
7643  C  CA    . ARG F 132 ? 0.5924 0.2353 0.257  -0.0234 0.2252 -0.0024 132 ARG Z CA    
7644  C  C     . ARG F 132 ? 0.591  0.2364 0.2596 -0.0202 0.2265 -0.0007 132 ARG Z C     
7645  O  O     . ARG F 132 ? 0.5901 0.2375 0.2648 -0.0207 0.2266 0.0018  132 ARG Z O     
7646  C  CB    . ARG F 132 ? 0.6    0.2402 0.2655 -0.0246 0.2271 -0.0017 132 ARG Z CB    
7647  C  CG    . ARG F 132 ? 0.626  0.2643 0.2906 -0.0206 0.2312 -0.0015 132 ARG Z CG    
7648  C  CD    . ARG F 132 ? 0.6574 0.2917 0.3207 -0.0218 0.2333 -0.0014 132 ARG Z CD    
7649  N  NE    . ARG F 132 ? 0.6755 0.311  0.3445 -0.0258 0.232  0.0008  132 ARG Z NE    
7650  C  CZ    . ARG F 132 ? 0.6823 0.3202 0.3578 -0.025  0.2335 0.0033  132 ARG Z CZ    
7651  N  NH1   . ARG F 132 ? 0.6698 0.3096 0.3507 -0.0291 0.2321 0.0055  132 ARG Z NH1   
7652  N  NH2   . ARG F 132 ? 0.6748 0.3133 0.3514 -0.0203 0.2365 0.0039  132 ARG Z NH2   
7653  N  N     . THR F 133 ? 0.5894 0.2344 0.2543 -0.017  0.2275 -0.0019 133 THR Z N     
7654  C  CA    . THR F 133 ? 0.5925 0.2383 0.2593 -0.0139 0.229  -0.0005 133 THR Z CA    
7655  C  C     . THR F 133 ? 0.5992 0.247  0.2672 -0.0147 0.2266 0.0001  133 THR Z C     
7656  O  O     . THR F 133 ? 0.6054 0.2534 0.2754 -0.0124 0.2278 0.0018  133 THR Z O     
7657  C  CB    . THR F 133 ? 0.6063 0.2501 0.2676 -0.0104 0.2311 -0.002  133 THR Z CB    
7658  O  OG1   . THR F 133 ? 0.6196 0.264  0.2759 -0.0113 0.229  -0.0041 133 THR Z OG1   
7659  C  CG2   . THR F 133 ? 0.6108 0.2525 0.2704 -0.0088 0.2339 -0.0025 133 THR Z CG2   
7660  N  N     . GLY F 134 ? 0.5952 0.2439 0.2612 -0.0175 0.2235 -0.0013 134 GLY Z N     
7661  C  CA    . GLY F 134 ? 0.5986 0.2486 0.2646 -0.0182 0.2214 -0.0011 134 GLY Z CA    
7662  C  C     . GLY F 134 ? 0.6049 0.2536 0.2646 -0.0169 0.2212 -0.0031 134 GLY Z C     
7663  O  O     . GLY F 134 ? 0.6079 0.2572 0.2663 -0.0179 0.2193 -0.0035 134 GLY Z O     
7664  N  N     . TYR F 135 ? 0.6053 0.2526 0.2611 -0.0149 0.2231 -0.0045 135 TYR Z N     
7665  C  CA    . TYR F 135 ? 0.6141 0.261  0.264  -0.0142 0.2227 -0.0063 135 TYR Z CA    
7666  C  C     . TYR F 135 ? 0.6146 0.2627 0.2616 -0.0164 0.2209 -0.0081 135 TYR Z C     
7667  O  O     . TYR F 135 ? 0.6165 0.2643 0.2638 -0.0167 0.2216 -0.0084 135 TYR Z O     
7668  C  CB    . TYR F 135 ? 0.62   0.2653 0.267  -0.0109 0.2256 -0.0064 135 TYR Z CB    
7669  C  CG    . TYR F 135 ? 0.6356 0.2788 0.2844 -0.0083 0.2278 -0.0046 135 TYR Z CG    
7670  C  CD1   . TYR F 135 ? 0.6502 0.2921 0.2977 -0.0081 0.2272 -0.004  135 TYR Z CD1   
7671  C  CD2   . TYR F 135 ? 0.6496 0.2915 0.3006 -0.0058 0.2308 -0.0035 135 TYR Z CD2   
7672  C  CE1   . TYR F 135 ? 0.6646 0.3038 0.3129 -0.0053 0.2296 -0.0021 135 TYR Z CE1   
7673  C  CE2   . TYR F 135 ? 0.6631 0.303  0.3155 -0.0031 0.2331 -0.0016 135 TYR Z CE2   
7674  C  CZ    . TYR F 135 ? 0.6784 0.3168 0.3293 -0.0028 0.2325 -0.0009 135 TYR Z CZ    
7675  O  OH    . TYR F 135 ? 0.7017 0.3371 0.3531 0.0003  0.2352 0.0012  135 TYR Z OH    
7676  N  N     . PRO F 136 ? 0.6102 0.2593 0.2541 -0.0178 0.2187 -0.0092 136 PRO Z N     
7677  C  CA    . PRO F 136 ? 0.6088 0.2591 0.25   -0.0197 0.2171 -0.0106 136 PRO Z CA    
7678  C  C     . PRO F 136 ? 0.6052 0.2559 0.243  -0.018  0.2188 -0.0115 136 PRO Z C     
7679  O  O     . PRO F 136 ? 0.6012 0.2522 0.2371 -0.0157 0.2205 -0.0115 136 PRO Z O     
7680  C  CB    . PRO F 136 ? 0.621  0.2723 0.2596 -0.0212 0.2149 -0.0114 136 PRO Z CB    
7681  C  CG    . PRO F 136 ? 0.6262 0.2762 0.2669 -0.0207 0.215  -0.0102 136 PRO Z CG    
7682  C  CD    . PRO F 136 ? 0.6044 0.253  0.2468 -0.0179 0.2178 -0.0091 136 PRO Z CD    
7683  N  N     . TYR F 137 ? 0.6062 0.2568 0.2428 -0.0192 0.2184 -0.012  137 TYR Z N     
7684  C  CA    . TYR F 137 ? 0.6146 0.2655 0.2477 -0.0173 0.2203 -0.0125 137 TYR Z CA    
7685  C  C     . TYR F 137 ? 0.6227 0.2752 0.2522 -0.0186 0.2188 -0.0134 137 TYR Z C     
7686  O  O     . TYR F 137 ? 0.6263 0.2774 0.2559 -0.0209 0.2173 -0.0136 137 TYR Z O     
7687  C  CB    . TYR F 137 ? 0.6133 0.261  0.2473 -0.0168 0.2223 -0.0121 137 TYR Z CB    
7688  C  CG    . TYR F 137 ? 0.6221 0.2694 0.2521 -0.0141 0.225  -0.0123 137 TYR Z CG    
7689  C  CD1   . TYR F 137 ? 0.6323 0.2799 0.2617 -0.0109 0.2276 -0.0119 137 TYR Z CD1   
7690  C  CD2   . TYR F 137 ? 0.6352 0.2815 0.2613 -0.0146 0.225  -0.0128 137 TYR Z CD2   
7691  C  CE1   . TYR F 137 ? 0.6446 0.2921 0.2701 -0.0081 0.2301 -0.0119 137 TYR Z CE1   
7692  C  CE2   . TYR F 137 ? 0.6478 0.2938 0.2698 -0.0117 0.2278 -0.0127 137 TYR Z CE2   
7693  C  CZ    . TYR F 137 ? 0.6583 0.3051 0.2802 -0.0084 0.2303 -0.0122 137 TYR Z CZ    
7694  O  OH    . TYR F 137 ? 0.6813 0.3281 0.299  -0.0051 0.2331 -0.0118 137 TYR Z OH    
7695  N  N     . ILE F 138 ? 0.624  0.2796 0.2503 -0.0171 0.2193 -0.0136 138 ILE Z N     
7696  C  CA    . ILE F 138 ? 0.6311 0.2892 0.2543 -0.0179 0.2182 -0.0139 138 ILE Z CA    
7697  C  C     . ILE F 138 ? 0.6402 0.2995 0.2601 -0.0151 0.2207 -0.0135 138 ILE Z C     
7698  O  O     . ILE F 138 ? 0.6388 0.3006 0.2577 -0.0127 0.2222 -0.013  138 ILE Z O     
7699  C  CB    . ILE F 138 ? 0.6364 0.2982 0.2589 -0.0191 0.2162 -0.0142 138 ILE Z CB    
7700  C  CG1   . ILE F 138 ? 0.6488 0.3088 0.2737 -0.0211 0.2144 -0.0144 138 ILE Z CG1   
7701  C  CG2   . ILE F 138 ? 0.6415 0.306  0.2614 -0.0204 0.2148 -0.0144 138 ILE Z CG2   
7702  C  CD1   . ILE F 138 ? 0.6648 0.3225 0.2919 -0.0234 0.2127 -0.0146 138 ILE Z CD1   
7703  N  N     . TYR F 139 ? 0.6489 0.3061 0.2664 -0.0153 0.2213 -0.0135 139 TYR Z N     
7704  C  CA    . TYR F 139 ? 0.6617 0.3193 0.2754 -0.0122 0.2241 -0.0128 139 TYR Z CA    
7705  C  C     . TYR F 139 ? 0.667  0.3285 0.2781 -0.0123 0.2233 -0.0124 139 TYR Z C     
7706  O  O     . TYR F 139 ? 0.6694 0.3284 0.279  -0.0141 0.2222 -0.0128 139 TYR Z O     
7707  C  CB    . TYR F 139 ? 0.669  0.32   0.2809 -0.0121 0.2259 -0.0129 139 TYR Z CB    
7708  C  CG    . TYR F 139 ? 0.6856 0.3352 0.2927 -0.0085 0.2295 -0.0121 139 TYR Z CG    
7709  C  CD1   . TYR F 139 ? 0.6967 0.3499 0.3031 -0.0048 0.2318 -0.0112 139 TYR Z CD1   
7710  C  CD2   . TYR F 139 ? 0.7026 0.3465 0.3053 -0.0087 0.2307 -0.0121 139 TYR Z CD2   
7711  C  CE1   . TYR F 139 ? 0.7108 0.3627 0.3126 -0.0011 0.2354 -0.0102 139 TYR Z CE1   
7712  C  CE2   . TYR F 139 ? 0.7188 0.3604 0.3163 -0.0051 0.2345 -0.0112 139 TYR Z CE2   
7713  C  CZ    . TYR F 139 ? 0.7295 0.3753 0.3266 -0.0011 0.2369 -0.0102 139 TYR Z CZ    
7714  O  OH    . TYR F 139 ? 0.7548 0.3982 0.3464 0.0029  0.2409 -0.009  139 TYR Z OH    
7715  N  N     . ILE F 140 ? 0.6671 0.3347 0.2774 -0.0106 0.2236 -0.0116 140 ILE Z N     
7716  C  CA    . ILE F 140 ? 0.6725 0.3453 0.2809 -0.0107 0.2229 -0.0107 140 ILE Z CA    
7717  C  C     . ILE F 140 ? 0.6816 0.3553 0.2862 -0.0068 0.2263 -0.0092 140 ILE Z C     
7718  O  O     . ILE F 140 ? 0.6834 0.3594 0.2875 -0.0036 0.2285 -0.0082 140 ILE Z O     
7719  C  CB    . ILE F 140 ? 0.6735 0.3531 0.2834 -0.0116 0.221  -0.0104 140 ILE Z CB    
7720  C  CG1   . ILE F 140 ? 0.6793 0.3566 0.2919 -0.015  0.2183 -0.0119 140 ILE Z CG1   
7721  C  CG2   . ILE F 140 ? 0.679  0.3648 0.2876 -0.0122 0.2201 -0.0093 140 ILE Z CG2   
7722  C  CD1   . ILE F 140 ? 0.6882 0.3697 0.3011 -0.0157 0.217  -0.0117 140 ILE Z CD1   
7723  N  N     . VAL F 141 ? 0.6857 0.3574 0.2874 -0.0067 0.2268 -0.0088 141 VAL Z N     
7724  C  CA    . VAL F 141 ? 0.6953 0.3665 0.2924 -0.0027 0.2305 -0.0071 141 VAL Z CA    
7725  C  C     . VAL F 141 ? 0.7018 0.3781 0.297  -0.0022 0.2304 -0.0055 141 VAL Z C     
7726  O  O     . VAL F 141 ? 0.7059 0.3808 0.3013 -0.0051 0.2281 -0.0063 141 VAL Z O     
7727  C  CB    . VAL F 141 ? 0.7087 0.37   0.3022 -0.0021 0.2327 -0.0078 141 VAL Z CB    
7728  C  CG1   . VAL F 141 ? 0.7163 0.3718 0.3103 -0.0065 0.2299 -0.0095 141 VAL Z CG1   
7729  C  CG2   . VAL F 141 ? 0.72   0.3792 0.3073 0.0019  0.2366 -0.006  141 VAL Z CG2   
7730  N  N     . ASP F 142 ? 0.7036 0.3861 0.2973 0.0018  0.2329 -0.0031 142 ASP Z N     
7731  C  CA    . ASP F 142 ? 0.7155 0.4042 0.3078 0.0031  0.2335 -0.0008 142 ASP Z CA    
7732  C  C     . ASP F 142 ? 0.7331 0.4147 0.32   0.0045  0.2357 -0.0004 142 ASP Z C     
7733  O  O     . ASP F 142 ? 0.7412 0.4164 0.3236 0.0077  0.2393 0       142 ASP Z O     
7734  C  CB    . ASP F 142 ? 0.7321 0.4287 0.3239 0.0077  0.2362 0.0021  142 ASP Z CB    
7735  C  CG    . ASP F 142 ? 0.7813 0.4898 0.3758 0.0071  0.2344 0.0042  142 ASP Z CG    
7736  O  OD1   . ASP F 142 ? 0.7877 0.4998 0.3859 0.0028  0.2306 0.0029  142 ASP Z OD1   
7737  O  OD2   . ASP F 142 ? 0.8021 0.5163 0.3948 0.0109  0.2371 0.0074  142 ASP Z OD2   
7738  N  N     . PHE F 143 ? 0.739  0.4212 0.3256 0.0022  0.2339 -0.0004 143 PHE Z N     
7739  C  CA    . PHE F 143 ? 0.7573 0.4325 0.3382 0.0034  0.2359 0.0001  143 PHE Z CA    
7740  C  C     . PHE F 143 ? 0.7708 0.4541 0.3512 0.0054  0.2369 0.0031  143 PHE Z C     
7741  O  O     . PHE F 143 ? 0.7688 0.4578 0.3529 0.002   0.2336 0.0028  143 PHE Z O     
7742  C  CB    . PHE F 143 ? 0.7581 0.4261 0.3393 -0.0015 0.2326 -0.0027 143 PHE Z CB    
7743  C  CG    . PHE F 143 ? 0.7726 0.4316 0.3472 -0.0011 0.2342 -0.0027 143 PHE Z CG    
7744  C  CD1   . PHE F 143 ? 0.7826 0.4438 0.3553 -0.0009 0.2341 -0.0014 143 PHE Z CD1   
7745  C  CD2   . PHE F 143 ? 0.7871 0.4351 0.3568 -0.001  0.2358 -0.0039 143 PHE Z CD2   
7746  C  CE1   . PHE F 143 ? 0.7952 0.4473 0.3608 -0.0001 0.2359 -0.0012 143 PHE Z CE1   
7747  C  CE2   . PHE F 143 ? 0.8003 0.4391 0.3628 -0.0008 0.2372 -0.0039 143 PHE Z CE2   
7748  C  CZ    . PHE F 143 ? 0.7975 0.4382 0.3578 -0.0002 0.2373 -0.0026 143 PHE Z CZ    
7749  N  N     . VAL F 144 ? 0.7806 0.4652 0.3567 0.0107  0.2413 0.0061  144 VAL Z N     
7750  C  CA    . VAL F 144 ? 0.7997 0.4775 0.3702 0.0153  0.2459 0.0069  144 VAL Z CA    
7751  C  C     . VAL F 144 ? 0.809  0.4964 0.3803 0.0206  0.249  0.0105  144 VAL Z C     
7752  O  O     . VAL F 144 ? 0.8025 0.5016 0.3778 0.0207  0.2478 0.0127  144 VAL Z O     
7753  C  CB    . VAL F 144 ? 0.8199 0.4879 0.3821 0.0175  0.2491 0.0077  144 VAL Z CB    
7754  C  CG1   . VAL F 144 ? 0.8345 0.491  0.3944 0.013   0.2468 0.0043  144 VAL Z CG1   
7755  C  CG2   . VAL F 144 ? 0.8247 0.4996 0.3863 0.0195  0.2501 0.0108  144 VAL Z CG2   
7756  N  N     . LYS F 145 ? 0.8234 0.5056 0.3902 0.0249  0.2532 0.0112  145 LYS Z N     
7757  C  CA    . LYS F 145 ? 0.8387 0.5284 0.4049 0.0308  0.2569 0.0148  145 LYS Z CA    
7758  C  C     . LYS F 145 ? 0.8598 0.54   0.4167 0.0364  0.2629 0.0165  145 LYS Z C     
7759  O  O     . LYS F 145 ? 0.8667 0.5337 0.4184 0.0352  0.2639 0.0141  145 LYS Z O     
7760  C  CB    . LYS F 145 ? 0.8624 0.5554 0.4326 0.0306  0.2559 0.0137  145 LYS Z CB    
7761  C  CG    . LYS F 145 ? 0.9134 0.6162 0.484  0.0362  0.2589 0.0175  145 LYS Z CG    
7762  C  CD    . LYS F 145 ? 0.965  0.6733 0.5407 0.0349  0.2567 0.0164  145 LYS Z CD    
7763  C  CE    . LYS F 145 ? 1.0125 0.7104 0.5856 0.0357  0.2586 0.0141  145 LYS Z CE    
7764  N  NZ    . LYS F 145 ? 1.0487 0.7411 0.6146 0.0421  0.2646 0.0163  145 LYS Z NZ    
7765  N  N     . TYR F 146 ? 0.8693 0.5558 0.4237 0.0422  0.2669 0.021   146 TYR Z N     
7766  C  CA    . TYR F 146 ? 0.8925 0.5697 0.4371 0.0481  0.2731 0.0231  146 TYR Z CA    
7767  C  C     . TYR F 146 ? 0.9087 0.584  0.4504 0.0529  0.2771 0.024   146 TYR Z C     
7768  O  O     . TYR F 146 ? 0.9057 0.5915 0.4533 0.0538  0.276  0.025   146 TYR Z O     
7769  C  CB    . TYR F 146 ? 0.8934 0.5786 0.4363 0.053   0.2763 0.0281  146 TYR Z CB    
7770  C  CG    . TYR F 146 ? 0.9081 0.5906 0.4497 0.0503  0.2747 0.0277  146 TYR Z CG    
7771  C  CD1   . TYR F 146 ? 0.9151 0.607  0.4648 0.045   0.2693 0.0269  146 TYR Z CD1   
7772  C  CD2   . TYR F 146 ? 0.9272 0.5975 0.4589 0.0532  0.2789 0.0286  146 TYR Z CD2   
7773  C  CE1   . TYR F 146 ? 0.9281 0.6175 0.4764 0.0427  0.2679 0.0266  146 TYR Z CE1   
7774  C  CE2   . TYR F 146 ? 0.9398 0.6073 0.4699 0.0509  0.2775 0.0284  146 TYR Z CE2   
7775  C  CZ    . TYR F 146 ? 0.9455 0.6229 0.4842 0.0457  0.272  0.0274  146 TYR Z CZ    
7776  O  OH    . TYR F 146 ? 0.9645 0.6391 0.5016 0.0435  0.2708 0.0272  146 TYR Z OH    
7777  N  N     . GLU F 147 ? 0.924  0.5853 0.4558 0.0562  0.282  0.0239  147 GLU Z N     
7778  C  CA    . GLU F 147 ? 0.9389 0.5968 0.4663 0.0615  0.2868 0.0252  147 GLU Z CA    
7779  C  C     . GLU F 147 ? 0.9422 0.6074 0.4662 0.0695  0.2921 0.0309  147 GLU Z C     
7780  O  O     . GLU F 147 ? 0.9464 0.6106 0.4664 0.0713  0.294  0.0332  147 GLU Z O     
7781  C  CB    . GLU F 147 ? 0.9818 0.6208 0.499  0.0615  0.29   0.0229  147 GLU Z CB    
7782  C  CG    . GLU F 147 ? 1.0455 0.68   0.5584 0.0661  0.2946 0.0235  147 GLU Z CG    
7783  C  CD    . GLU F 147 ? 1.1254 0.7428 0.6248 0.0698  0.3007 0.0238  147 GLU Z CD    
7784  O  OE1   . GLU F 147 ? 1.1392 0.7533 0.6341 0.0746  0.3053 0.0251  147 GLU Z OE1   
7785  O  OE2   . GLU F 147 ? 1.1559 0.763  0.6488 0.0677  0.301  0.0229  147 GLU Z OE2   
7786  N  N     . LEU F 148 ? 0.9379 0.6107 0.4634 0.0743  0.2946 0.0335  148 LEU Z N     
7787  C  CA    . LEU F 148 ? 0.9419 0.6223 0.4644 0.0824  0.2999 0.0393  148 LEU Z CA    
7788  C  C     . LEU F 148 ? 0.9569 0.6254 0.4686 0.0891  0.3071 0.0407  148 LEU Z C     
7789  O  O     . LEU F 148 ? 0.966  0.6245 0.4752 0.0874  0.3073 0.0373  148 LEU Z O     
7790  C  CB    . LEU F 148 ? 0.934  0.6341 0.4665 0.0832  0.2973 0.0421  148 LEU Z CB    
7791  C  CG    . LEU F 148 ? 0.9456 0.6569 0.4882 0.0762  0.2901 0.0406  148 LEU Z CG    
7792  C  CD1   . LEU F 148 ? 0.9461 0.6747 0.4974 0.0762  0.2873 0.0427  148 LEU Z CD1   
7793  C  CD2   . LEU F 148 ? 0.9522 0.6658 0.4939 0.076   0.2902 0.0428  148 LEU Z CD2   
7794  N  N     . ASN F 149 ? 0.9601 0.6291 0.465  0.0968  0.3133 0.0457  149 ASN Z N     
7795  C  CA    . ASN F 149 ? 0.9785 0.6349 0.4716 0.1036  0.3208 0.0472  149 ASN Z CA    
7796  C  C     . ASN F 149 ? 0.9824 0.6459 0.4772 0.1088  0.3234 0.0494  149 ASN Z C     
7797  O  O     . ASN F 149 ? 0.9907 0.6426 0.4759 0.1137  0.3292 0.0499  149 ASN Z O     
7798  C  CB    . ASN F 149 ? 1.0007 0.6525 0.4843 0.1102  0.327  0.0518  149 ASN Z CB    
7799  C  CG    . ASN F 149 ? 1.0367 0.7073 0.5258 0.1159  0.3285 0.0582  149 ASN Z CG    
7800  O  OD1   . ASN F 149 ? 1.0413 0.7296 0.5422 0.1138  0.3239 0.0591  149 ASN Z OD1   
7801  N  ND2   . ASN F 149 ? 1.0499 0.7172 0.5304 0.1232  0.3351 0.063   149 ASN Z ND2   
7802  N  N     . ASN F 150 ? 0.9741 0.6562 0.4804 0.1077  0.3192 0.0509  150 ASN Z N     
7803  C  CA    . ASN F 150 ? 0.9758 0.668  0.4858 0.1119  0.3203 0.0531  150 ASN Z CA    
7804  C  C     . ASN F 150 ? 0.9745 0.6727 0.4793 0.1222  0.3275 0.06    150 ASN Z C     
7805  O  O     . ASN F 150 ? 0.9711 0.6851 0.4821 0.1253  0.3269 0.0635  150 ASN Z O     
7806  C  CB    . ASN F 150 ? 0.9991 0.6803 0.5068 0.1101  0.3204 0.0488  150 ASN Z CB    
7807  C  CG    . ASN F 150 ? 1.0571 0.7191 0.5517 0.1142  0.3271 0.048   150 ASN Z CG    
7808  O  OD1   . ASN F 150 ? 1.0777 0.7382 0.5649 0.1226  0.3339 0.0523  150 ASN Z OD1   
7809  N  ND2   . ASN F 150 ? 1.0728 0.7195 0.5641 0.1083  0.3254 0.0428  150 ASN Z ND2   
7810  N  N     . SER F 151 ? 0.9742 0.6603 0.4675 0.1276  0.334  0.0622  151 SER Z N     
7811  C  CA    . SER F 151 ? 0.9742 0.6654 0.462  0.1379  0.3414 0.0691  151 SER Z CA    
7812  C  C     . SER F 151 ? 0.96   0.6723 0.4569 0.1393  0.3392 0.0744  151 SER Z C     
7813  O  O     . SER F 151 ? 0.9557 0.6827 0.4561 0.1452  0.3413 0.0797  151 SER Z O     
7814  C  CB    . SER F 151 ? 1.0049 0.6771 0.4776 0.1428  0.3487 0.07    151 SER Z CB    
7815  O  OG    . SER F 151 ? 1.0377 0.7062 0.5093 0.1393  0.3469 0.0694  151 SER Z OG    
7816  N  N     . ASP F 152 ? 0.9511 0.6655 0.4521 0.1334  0.3348 0.0729  152 ASP Z N     
7817  C  CA    . ASP F 152 ? 0.9431 0.6773 0.4532 0.1336  0.3322 0.0776  152 ASP Z CA    
7818  C  C     . ASP F 152 ? 0.9355 0.6767 0.4562 0.1232  0.3233 0.0734  152 ASP Z C     
7819  O  O     . ASP F 152 ? 0.9288 0.6832 0.4559 0.122   0.321  0.0765  152 ASP Z O     
7820  C  CB    . ASP F 152 ? 0.9697 0.7022 0.4727 0.1404  0.3385 0.0831  152 ASP Z CB    
7821  C  CG    . ASP F 152 ? 1.0337 0.7501 0.53   0.1366  0.3384 0.0796  152 ASP Z CG    
7822  O  OD1   . ASP F 152 ? 1.0519 0.7476 0.5369 0.1372  0.3419 0.0763  152 ASP Z OD1   
7823  O  OD2   . ASP F 152 ? 1.055  0.779  0.5569 0.1329  0.3349 0.0804  152 ASP Z OD2   
7824  N  N     . ARG F 153 ? 0.9354 0.6677 0.4579 0.1159  0.3185 0.0667  153 ARG Z N     
7825  C  CA    . ARG F 153 ? 0.9338 0.6704 0.4654 0.1061  0.3103 0.0621  153 ARG Z CA    
7826  C  C     . ARG F 153 ? 0.933  0.6662 0.4641 0.1024  0.3086 0.0614  153 ARG Z C     
7827  O  O     . ARG F 153 ? 0.9294 0.672  0.469  0.0961  0.3025 0.0601  153 ARG Z O     
7828  C  CB    . ARG F 153 ? 0.9406 0.6979 0.4837 0.1039  0.3053 0.0641  153 ARG Z CB    
7829  C  CG    . ARG F 153 ? 0.9743 0.7307 0.5234 0.0962  0.2989 0.0583  153 ARG Z CG    
7830  C  CD    . ARG F 153 ? 1.0031 0.7787 0.5622 0.0937  0.294  0.0603  153 ARG Z CD    
7831  N  NE    . ARG F 153 ? 1.0393 0.8131 0.6034 0.0864  0.288  0.0549  153 ARG Z NE    
7832  C  CZ    . ARG F 153 ? 1.0655 0.8411 0.6353 0.0784  0.2818 0.0515  153 ARG Z CZ    
7833  N  NH1   . ARG F 153 ? 1.0613 0.8407 0.6328 0.0762  0.2804 0.0528  153 ARG Z NH1   
7834  N  NH2   . ARG F 153 ? 1.0659 0.8392 0.6393 0.0726  0.2771 0.047   153 ARG Z NH2   
7835  N  N     . SER F 154 ? 0.9359 0.6547 0.4563 0.1062  0.3139 0.062   154 SER Z N     
7836  C  CA    . SER F 154 ? 0.9389 0.6522 0.4574 0.1029  0.3126 0.061   154 SER Z CA    
7837  C  C     . SER F 154 ? 0.9418 0.6393 0.4581 0.0951  0.3086 0.0538  154 SER Z C     
7838  O  O     . SER F 154 ? 0.9505 0.6379 0.4635 0.0942  0.309  0.0503  154 SER Z O     
7839  C  CB    . SER F 154 ? 0.9599 0.6652 0.4673 0.1108  0.3204 0.0655  154 SER Z CB    
7840  O  OG    . SER F 154 ? 0.9961 0.6818 0.4913 0.1137  0.3254 0.0634  154 SER Z OG    
7841  N  N     . ARG F 155 ? 0.9321 0.6278 0.4504 0.0896  0.3048 0.0517  155 ARG Z N     
7842  C  CA    . ARG F 155 ? 0.9325 0.6149 0.4496 0.0821  0.3005 0.0453  155 ARG Z CA    
7843  C  C     . ARG F 155 ? 0.9365 0.5976 0.4405 0.0832  0.3046 0.0432  155 ARG Z C     
7844  O  O     . ARG F 155 ? 0.9426 0.5975 0.438  0.0879  0.3095 0.0463  155 ARG Z O     
7845  C  CB    . ARG F 155 ? 0.9428 0.6313 0.467  0.0754  0.2945 0.0436  155 ARG Z CB    
7846  C  CG    . ARG F 155 ? 0.9659 0.6716 0.5026 0.0713  0.2888 0.0434  155 ARG Z CG    
7847  C  CD    . ARG F 155 ? 0.9946 0.7057 0.537  0.0655  0.2838 0.0423  155 ARG Z CD    
7848  N  NE    . ARG F 155 ? 1.0165 0.7442 0.5698 0.0618  0.2788 0.0428  155 ARG Z NE    
7849  C  CZ    . ARG F 155 ? 1.0307 0.7747 0.5891 0.0643  0.2792 0.0478  155 ARG Z CZ    
7850  N  NH1   . ARG F 155 ? 1.025  0.7715 0.579  0.0711  0.2847 0.0531  155 ARG Z NH1   
7851  N  NH2   . ARG F 155 ? 1.0183 0.7761 0.5859 0.0601  0.2742 0.0478  155 ARG Z NH2   
7852  N  N     . LYS F 156 ? 0.9297 0.5796 0.4323 0.0783  0.3022 0.0381  156 LYS Z N     
7853  C  CA    . LYS F 156 ? 0.9347 0.564  0.4258 0.0771  0.3044 0.0351  156 LYS Z CA    
7854  C  C     . LYS F 156 ? 0.9216 0.5462 0.4164 0.0681  0.2978 0.0302  156 LYS Z C     
7855  O  O     . LYS F 156 ? 0.9167 0.5537 0.4225 0.0636  0.2922 0.0292  156 LYS Z O     
7856  C  CB    . LYS F 156 ? 0.9666 0.5869 0.4532 0.0784  0.307  0.0333  156 LYS Z CB    
7857  C  CG    . LYS F 156 ? 1.0241 0.6464 0.5051 0.0878  0.3143 0.0382  156 LYS Z CG    
7858  C  CD    . LYS F 156 ? 1.0853 0.7065 0.5673 0.0887  0.3152 0.0368  156 LYS Z CD    
7859  C  CE    . LYS F 156 ? 1.1465 0.7471 0.6166 0.0883  0.3187 0.0341  156 LYS Z CE    
7860  N  NZ    . LYS F 156 ? 1.1762 0.7768 0.6479 0.0895  0.3197 0.033   156 LYS Z NZ    
7861  N  N     . ASN F 157 ? 0.9137 0.5207 0.3989 0.0655  0.2986 0.0273  157 ASN Z N     
7862  C  CA    . ASN F 157 ? 0.9047 0.5069 0.3926 0.0574  0.2926 0.0231  157 ASN Z CA    
7863  C  C     . ASN F 157 ? 0.8779 0.4882 0.3779 0.0508  0.2859 0.0195  157 ASN Z C     
7864  O  O     . ASN F 157 ? 0.8796 0.4916 0.3824 0.0513  0.2862 0.0187  157 ASN Z O     
7865  C  CB    . ASN F 157 ? 0.936  0.5176 0.4114 0.0555  0.2944 0.0206  157 ASN Z CB    
7866  C  CG    . ASN F 157 ? 0.996  0.5679 0.4585 0.0612  0.3006 0.0238  157 ASN Z CG    
7867  O  OD1   . ASN F 157 ? 1.0218 0.5837 0.4736 0.0665  0.3068 0.0255  157 ASN Z OD1   
7868  N  ND2   . ASN F 157 ? 1.0075 0.5813 0.4699 0.0605  0.2993 0.0248  157 ASN Z ND2   
7869  N  N     . LEU F 158 ? 0.8519 0.4669 0.3586 0.0451  0.2802 0.0175  158 LEU Z N     
7870  C  CA    . LEU F 158 ? 0.8319 0.4536 0.3493 0.0388  0.2739 0.0141  158 LEU Z CA    
7871  C  C     . LEU F 158 ? 0.8229 0.4325 0.3375 0.0349  0.2729 0.0104  158 LEU Z C     
7872  O  O     . LEU F 158 ? 0.8353 0.4305 0.3404 0.0342  0.2747 0.0093  158 LEU Z O     
7873  C  CB    . LEU F 158 ? 0.8319 0.4573 0.3541 0.0335  0.2688 0.0127  158 LEU Z CB    
7874  C  CG    . LEU F 158 ? 0.8419 0.4834 0.372  0.0344  0.2672 0.0153  158 LEU Z CG    
7875  C  CD1   . LEU F 158 ? 0.8452 0.4878 0.3789 0.0289  0.2623 0.0135  158 LEU Z CD1   
7876  C  CD2   . LEU F 158 ? 0.8444 0.4985 0.3838 0.0341  0.2651 0.0155  158 LEU Z CD2   
7877  N  N     . ARG F 159 ? 0.8011 0.4165 0.3239 0.0321  0.2698 0.0085  159 ARG Z N     
7878  C  CA    . ARG F 159 ? 0.794  0.3996 0.3157 0.0283  0.2685 0.0052  159 ARG Z CA    
7879  C  C     . ARG F 159 ? 0.7843 0.3927 0.3142 0.0212  0.262  0.0021  159 ARG Z C     
7880  O  O     . ARG F 159 ? 0.7793 0.3997 0.3186 0.0198  0.2587 0.002   159 ARG Z O     
7881  C  CB    . ARG F 159 ? 0.797  0.4045 0.3201 0.0315  0.2712 0.0057  159 ARG Z CB    
7882  C  CG    . ARG F 159 ? 0.8203 0.423  0.334  0.0387  0.2781 0.0088  159 ARG Z CG    
7883  C  CD    . ARG F 159 ? 0.853  0.438  0.3539 0.0388  0.2815 0.008   159 ARG Z CD    
7884  N  NE    . ARG F 159 ? 0.8713 0.4461 0.3694 0.0364  0.2821 0.0056  159 ARG Z NE    
7885  C  CZ    . ARG F 159 ? 0.8904 0.458  0.3893 0.0296  0.2782 0.0023  159 ARG Z CZ    
7886  N  NH1   . ARG F 159 ? 0.8909 0.4605 0.3937 0.0246  0.2733 0.0008  159 ARG Z NH1   
7887  N  NH2   . ARG F 159 ? 0.8819 0.4409 0.3783 0.0277  0.2791 0.0005  159 ARG Z NH2   
7888  N  N     . PHE F 160 ? 0.78   0.3772 0.3061 0.0166  0.2602 -0.0004 160 PHE Z N     
7889  C  CA    . PHE F 160 ? 0.775  0.3741 0.3083 0.01    0.2543 -0.0032 160 PHE Z CA    
7890  C  C     . PHE F 160 ? 0.772  0.3638 0.3056 0.0066  0.2533 -0.0055 160 PHE Z C     
7891  O  O     . PHE F 160 ? 0.7822 0.3629 0.3073 0.0076  0.2567 -0.0055 160 PHE Z O     
7892  C  CB    . PHE F 160 ? 0.7751 0.3687 0.3046 0.0068  0.2521 -0.004  160 PHE Z CB    
7893  C  CG    . PHE F 160 ? 0.7782 0.3787 0.3076 0.0095  0.2527 -0.0018 160 PHE Z CG    
7894  C  CD1   . PHE F 160 ? 0.7779 0.3916 0.3166 0.0087  0.2496 -0.0014 160 PHE Z CD1   
7895  C  CD2   . PHE F 160 ? 0.7926 0.3857 0.3121 0.0128  0.2565 0       160 PHE Z CD2   
7896  C  CE1   . PHE F 160 ? 0.7833 0.4038 0.3223 0.0109  0.2502 0.0009  160 PHE Z CE1   
7897  C  CE2   . PHE F 160 ? 0.7976 0.3974 0.3174 0.0155  0.2573 0.0024  160 PHE Z CE2   
7898  C  CZ    . PHE F 160 ? 0.7863 0.4002 0.3161 0.0144  0.254  0.0028  160 PHE Z CZ    
7899  N  N     . PRO F 161 ? 0.7563 0.3536 0.2992 0.0023  0.2488 -0.0072 161 PRO Z N     
7900  C  CA    . PRO F 161 ? 0.7523 0.3433 0.2961 -0.0012 0.2478 -0.0091 161 PRO Z CA    
7901  C  C     . PRO F 161 ? 0.7529 0.3326 0.2909 -0.0059 0.2461 -0.0105 161 PRO Z C     
7902  O  O     . PRO F 161 ? 0.7589 0.3374 0.2945 -0.0074 0.2444 -0.0107 161 PRO Z O     
7903  C  CB    . PRO F 161 ? 0.7539 0.3546 0.3091 -0.0042 0.2434 -0.0101 161 PRO Z CB    
7904  C  CG    . PRO F 161 ? 0.7557 0.3636 0.314  -0.0049 0.2407 -0.0098 161 PRO Z CG    
7905  C  CD    . PRO F 161 ? 0.7391 0.3481 0.2915 0.0003  0.2446 -0.0075 161 PRO Z CD    
7906  N  N     . ASN F 162 ? 0.7454 0.3171 0.2812 -0.0086 0.2464 -0.0117 162 ASN Z N     
7907  C  CA    . ASN F 162 ? 0.7495 0.3111 0.2804 -0.014  0.2441 -0.0131 162 ASN Z CA    
7908  C  C     . ASN F 162 ? 0.742  0.3104 0.2821 -0.019  0.2381 -0.0142 162 ASN Z C     
7909  O  O     . ASN F 162 ? 0.7399 0.3176 0.2898 -0.0193 0.2362 -0.0143 162 ASN Z O     
7910  C  CB    . ASN F 162 ? 0.7713 0.325  0.2997 -0.0161 0.2455 -0.0138 162 ASN Z CB    
7911  C  CG    . ASN F 162 ? 0.8261 0.3688 0.3484 -0.022  0.2433 -0.015  162 ASN Z CG    
7912  O  OD1   . ASN F 162 ? 0.8366 0.382  0.3648 -0.0273 0.2383 -0.016  162 ASN Z OD1   
7913  N  ND2   . ASN F 162 ? 0.8509 0.3807 0.361  -0.0213 0.247  -0.0149 162 ASN Z ND2   
7914  N  N     . PRO F 163 ? 0.7364 0.3003 0.2732 -0.0227 0.2353 -0.015  163 PRO Z N     
7915  C  CA    . PRO F 163 ? 0.7264 0.2969 0.2718 -0.0271 0.2297 -0.0159 163 PRO Z CA    
7916  C  C     . PRO F 163 ? 0.7186 0.2929 0.2727 -0.0305 0.227  -0.0165 163 PRO Z C     
7917  O  O     . PRO F 163 ? 0.7118 0.2945 0.2748 -0.0321 0.2236 -0.0167 163 PRO Z O     
7918  C  CB    . PRO F 163 ? 0.7414 0.3032 0.2795 -0.0308 0.2277 -0.0166 163 PRO Z CB    
7919  C  CG    . PRO F 163 ? 0.7543 0.3072 0.2805 -0.027  0.2324 -0.0158 163 PRO Z CG    
7920  C  CD    . PRO F 163 ? 0.7365 0.2886 0.261  -0.0228 0.2371 -0.0149 163 PRO Z CD    
7921  N  N     . ALA F 164 ? 0.7185 0.2864 0.2699 -0.0315 0.2289 -0.0166 164 ALA Z N     
7922  C  CA    . ALA F 164 ? 0.7151 0.2861 0.2743 -0.0346 0.2269 -0.0168 164 ALA Z CA    
7923  C  C     . ALA F 164 ? 0.7059 0.2873 0.2742 -0.0312 0.2277 -0.0162 164 ALA Z C     
7924  O  O     . ALA F 164 ? 0.7038 0.2902 0.2804 -0.0335 0.2252 -0.0162 164 ALA Z O     
7925  C  CB    . ALA F 164 ? 0.7226 0.2837 0.2757 -0.0363 0.2292 -0.0169 164 ALA Z CB    
7926  N  N     . ILE F 165 ? 0.6994 0.2838 0.2658 -0.0257 0.2311 -0.0155 165 ILE Z N     
7927  C  CA    . ILE F 165 ? 0.6947 0.2886 0.2689 -0.0226 0.2318 -0.015  165 ILE Z CA    
7928  C  C     . ILE F 165 ? 0.6929 0.2956 0.2749 -0.0241 0.2277 -0.0152 165 ILE Z C     
7929  O  O     . ILE F 165 ? 0.6902 0.2969 0.2795 -0.026  0.2257 -0.0153 165 ILE Z O     
7930  C  CB    . ILE F 165 ? 0.6986 0.2943 0.269  -0.0165 0.2362 -0.0139 165 ILE Z CB    
7931  C  CG1   . ILE F 165 ? 0.7197 0.3051 0.2802 -0.0146 0.2407 -0.0136 165 ILE Z CG1   
7932  C  CG2   . ILE F 165 ? 0.6963 0.3001 0.2739 -0.014  0.2368 -0.0135 165 ILE Z CG2   
7933  C  CD1   . ILE F 165 ? 0.7406 0.3197 0.3008 -0.017  0.2414 -0.0141 165 ILE Z CD1   
7934  N  N     . PRO F 166 ? 0.6923 0.2974 0.2725 -0.0237 0.2265 -0.0152 166 PRO Z N     
7935  C  CA    . PRO F 166 ? 0.685  0.2976 0.2722 -0.0256 0.2226 -0.0155 166 PRO Z CA    
7936  C  C     . PRO F 166 ? 0.6796 0.2909 0.2711 -0.0306 0.2189 -0.0161 166 PRO Z C     
7937  O  O     . PRO F 166 ? 0.6723 0.2896 0.2711 -0.0315 0.2167 -0.0161 166 PRO Z O     
7938  C  CB    . PRO F 166 ? 0.6984 0.3108 0.2809 -0.0252 0.2222 -0.0155 166 PRO Z CB    
7939  C  CG    . PRO F 166 ? 0.7088 0.3173 0.2838 -0.0211 0.2265 -0.0146 166 PRO Z CG    
7940  C  CD    . PRO F 166 ? 0.6914 0.2926 0.2633 -0.0214 0.2288 -0.0148 166 PRO Z CD    
7941  N  N     . TYR F 167 ? 0.6817 0.2848 0.2683 -0.0336 0.2183 -0.0165 167 TYR Z N     
7942  C  CA    . TYR F 167 ? 0.6812 0.2836 0.2718 -0.0385 0.2146 -0.0167 167 TYR Z CA    
7943  C  C     . TYR F 167 ? 0.6734 0.2787 0.271  -0.0391 0.2147 -0.0161 167 TYR Z C     
7944  O  O     . TYR F 167 ? 0.671  0.2808 0.2755 -0.0416 0.2116 -0.0157 167 TYR Z O     
7945  C  CB    . TYR F 167 ? 0.6869 0.2799 0.2702 -0.0422 0.2137 -0.0172 167 TYR Z CB    
7946  C  CG    . TYR F 167 ? 0.6945 0.2889 0.2827 -0.0473 0.2091 -0.0171 167 TYR Z CG    
7947  C  CD1   . TYR F 167 ? 0.7037 0.3024 0.2947 -0.0485 0.2058 -0.0173 167 TYR Z CD1   
7948  C  CD2   . TYR F 167 ? 0.7051 0.2981 0.2964 -0.0507 0.208  -0.0166 167 TYR Z CD2   
7949  C  CE1   . TYR F 167 ? 0.7125 0.3135 0.3086 -0.0526 0.2017 -0.017  167 TYR Z CE1   
7950  C  CE2   . TYR F 167 ? 0.7139 0.3099 0.3108 -0.0551 0.2037 -0.016  167 TYR Z CE2   
7951  C  CZ    . TYR F 167 ? 0.7233 0.3233 0.3225 -0.0559 0.2006 -0.0162 167 TYR Z CZ    
7952  O  OH    . TYR F 167 ? 0.7401 0.3433 0.3448 -0.0598 0.1965 -0.0154 167 TYR Z OH    
7953  N  N     . SER F 168 ? 0.6705 0.2737 0.2664 -0.0366 0.2183 -0.0158 168 SER Z N     
7954  C  CA    . SER F 168 ? 0.6749 0.2806 0.2772 -0.0368 0.2189 -0.0151 168 SER Z CA    
7955  C  C     . SER F 168 ? 0.6647 0.2793 0.2757 -0.0356 0.2174 -0.0146 168 SER Z C     
7956  O  O     . SER F 168 ? 0.661  0.2782 0.2785 -0.0372 0.2162 -0.0137 168 SER Z O     
7957  C  CB    . SER F 168 ? 0.7033 0.3054 0.3018 -0.0334 0.2234 -0.0149 168 SER Z CB    
7958  O  OG    . SER F 168 ? 0.74   0.3465 0.3382 -0.0284 0.2259 -0.0148 168 SER Z OG    
7959  N  N     . TYR F 169 ? 0.6577 0.2768 0.2686 -0.0329 0.2174 -0.0149 169 TYR Z N     
7960  C  CA    . TYR F 169 ? 0.6552 0.2815 0.2726 -0.0318 0.2161 -0.0146 169 TYR Z CA    
7961  C  C     . TYR F 169 ? 0.6556 0.2839 0.2772 -0.0355 0.2121 -0.0144 169 TYR Z C     
7962  O  O     . TYR F 169 ? 0.6548 0.287  0.2828 -0.0358 0.2111 -0.0136 169 TYR Z O     
7963  C  CB    . TYR F 169 ? 0.6551 0.2851 0.27   -0.0286 0.2171 -0.0149 169 TYR Z CB    
7964  C  CG    . TYR F 169 ? 0.6662 0.2963 0.2787 -0.0244 0.221  -0.0146 169 TYR Z CG    
7965  C  CD1   . TYR F 169 ? 0.6799 0.3046 0.2861 -0.023  0.2239 -0.0146 169 TYR Z CD1   
7966  C  CD2   . TYR F 169 ? 0.673  0.308  0.289  -0.0219 0.222  -0.0142 169 TYR Z CD2   
7967  C  CE1   . TYR F 169 ? 0.6894 0.3142 0.2933 -0.0189 0.2276 -0.0141 169 TYR Z CE1   
7968  C  CE2   . TYR F 169 ? 0.6821 0.3175 0.296  -0.018  0.2254 -0.0138 169 TYR Z CE2   
7969  C  CZ    . TYR F 169 ? 0.6951 0.3257 0.3032 -0.0164 0.2283 -0.0137 169 TYR Z CZ    
7970  O  OH    . TYR F 169 ? 0.7133 0.3443 0.3191 -0.0123 0.2318 -0.0131 169 TYR Z OH    
7971  N  N     . ILE F 170 ? 0.6569 0.2823 0.2748 -0.0381 0.21   -0.015  170 ILE Z N     
7972  C  CA    . ILE F 170 ? 0.6593 0.2862 0.2806 -0.0416 0.2061 -0.0147 170 ILE Z CA    
7973  C  C     . ILE F 170 ? 0.6634 0.2894 0.2889 -0.0447 0.2049 -0.0136 170 ILE Z C     
7974  O  O     . ILE F 170 ? 0.6636 0.2941 0.2956 -0.0458 0.2028 -0.0126 170 ILE Z O     
7975  C  CB    . ILE F 170 ? 0.6662 0.2895 0.2817 -0.0435 0.2044 -0.0156 170 ILE Z CB    
7976  C  CG1   . ILE F 170 ? 0.6776 0.3029 0.2897 -0.0406 0.2055 -0.0163 170 ILE Z CG1   
7977  C  CG2   . ILE F 170 ? 0.6693 0.294  0.2881 -0.0472 0.2003 -0.0153 170 ILE Z CG2   
7978  C  CD1   . ILE F 170 ? 0.6989 0.3197 0.3043 -0.0416 0.2049 -0.017  170 ILE Z CD1   
7979  N  N     . SER F 171 ? 0.664  0.2844 0.2859 -0.046  0.2062 -0.0137 171 SER Z N     
7980  C  CA    . SER F 171 ? 0.6668 0.2865 0.2925 -0.0494 0.205  -0.0124 171 SER Z CA    
7981  C  C     . SER F 171 ? 0.6633 0.2878 0.2964 -0.0474 0.2066 -0.0111 171 SER Z C     
7982  O  O     . SER F 171 ? 0.6604 0.2883 0.3    -0.0497 0.2047 -0.0094 171 SER Z O     
7983  C  CB    . SER F 171 ? 0.6904 0.3018 0.3092 -0.0517 0.2062 -0.0129 171 SER Z CB    
7984  O  OG    . SER F 171 ? 0.7225 0.3308 0.3369 -0.0479 0.2105 -0.0135 171 SER Z OG    
7985  N  N     . HIS F 172 ? 0.6631 0.2882 0.2953 -0.043  0.2101 -0.0115 172 HIS Z N     
7986  C  CA    . HIS F 172 ? 0.6656 0.2947 0.3041 -0.0407 0.2119 -0.0102 172 HIS Z CA    
7987  C  C     . HIS F 172 ? 0.6666 0.3019 0.3112 -0.0402 0.2098 -0.0093 172 HIS Z C     
7988  O  O     . HIS F 172 ? 0.6646 0.3032 0.3157 -0.0402 0.2097 -0.0075 172 HIS Z O     
7989  C  CB    . HIS F 172 ? 0.6757 0.3041 0.3112 -0.036  0.2158 -0.0109 172 HIS Z CB    
7990  C  CG    . HIS F 172 ? 0.7055 0.3354 0.3457 -0.034  0.2182 -0.0096 172 HIS Z CG    
7991  N  ND1   . HIS F 172 ? 0.7293 0.3588 0.3738 -0.0366 0.2179 -0.0081 172 HIS Z ND1   
7992  C  CD2   . HIS F 172 ? 0.7215 0.3532 0.3621 -0.0297 0.221  -0.0096 172 HIS Z CD2   
7993  C  CE1   . HIS F 172 ? 0.7348 0.3657 0.3825 -0.0335 0.2207 -0.0072 172 HIS Z CE1   
7994  N  NE2   . HIS F 172 ? 0.734  0.3659 0.3792 -0.0293 0.2227 -0.0082 172 HIS Z NE2   
7995  N  N     . SER F 173 ? 0.6653 0.302  0.3076 -0.0397 0.2083 -0.0104 173 SER Z N     
7996  C  CA    . SER F 173 ? 0.6648 0.3061 0.3112 -0.0394 0.2064 -0.0098 173 SER Z CA    
7997  C  C     . SER F 173 ? 0.6679 0.3109 0.3191 -0.0429 0.2034 -0.0082 173 SER Z C     
7998  O  O     . SER F 173 ? 0.6688 0.3157 0.3259 -0.0422 0.2031 -0.0064 173 SER Z O     
7999  C  CB    . SER F 173 ? 0.6775 0.319  0.3195 -0.0389 0.2053 -0.0113 173 SER Z CB    
8000  O  OG    . SER F 173 ? 0.6996 0.3412 0.3382 -0.0356 0.2078 -0.0123 173 SER Z OG    
8001  N  N     . LYS F 174 ? 0.6687 0.3088 0.3173 -0.0466 0.2012 -0.0085 174 LYS Z N     
8002  C  CA    . LYS F 174 ? 0.6734 0.3156 0.3265 -0.0504 0.1979 -0.0068 174 LYS Z CA    
8003  C  C     . LYS F 174 ? 0.6708 0.3152 0.3302 -0.0511 0.1988 -0.0045 174 LYS Z C     
8004  O  O     . LYS F 174 ? 0.6706 0.3201 0.3367 -0.0514 0.1975 -0.0021 174 LYS Z O     
8005  C  CB    . LYS F 174 ? 0.7083 0.3458 0.356  -0.0545 0.1955 -0.0078 174 LYS Z CB    
8006  C  CG    . LYS F 174 ? 0.7754 0.4108 0.4172 -0.054  0.1945 -0.0097 174 LYS Z CG    
8007  C  CD    . LYS F 174 ? 0.849  0.4797 0.4859 -0.0583 0.1918 -0.0103 174 LYS Z CD    
8008  C  CE    . LYS F 174 ? 0.9204 0.5471 0.5497 -0.0574 0.192  -0.0123 174 LYS Z CE    
8009  N  NZ    . LYS F 174 ? 0.9613 0.5908 0.5915 -0.058  0.1891 -0.0124 174 LYS Z NZ    
8010  N  N     . ASN F 175 ? 0.6668 0.3075 0.3239 -0.0511 0.2012 -0.0048 175 ASN Z N     
8011  C  CA    . ASN F 175 ? 0.6649 0.3071 0.3274 -0.0519 0.2024 -0.0027 175 ASN Z CA    
8012  C  C     . ASN F 175 ? 0.6582 0.3056 0.3274 -0.048  0.2045 -0.0009 175 ASN Z C     
8013  O  O     . ASN F 175 ? 0.6557 0.3071 0.3318 -0.0489 0.2041 0.0019  175 ASN Z O     
8014  C  CB    . ASN F 175 ? 0.6801 0.3162 0.3374 -0.0521 0.2051 -0.0038 175 ASN Z CB    
8015  C  CG    . ASN F 175 ? 0.7164 0.3463 0.367  -0.0565 0.2034 -0.005  175 ASN Z CG    
8016  O  OD1   . ASN F 175 ? 0.7291 0.3599 0.3807 -0.0608 0.1996 -0.0043 175 ASN Z OD1   
8017  N  ND2   . ASN F 175 ? 0.7282 0.3513 0.3712 -0.0555 0.2061 -0.0067 175 ASN Z ND2   
8018  N  N     . THR F 176 ? 0.6533 0.3004 0.32   -0.0436 0.2067 -0.0023 176 THR Z N     
8019  C  CA    . THR F 176 ? 0.6529 0.3033 0.3242 -0.0397 0.209  -0.0008 176 THR Z CA    
8020  C  C     . THR F 176 ? 0.6509 0.3052 0.3251 -0.0385 0.2075 0.0001  176 THR Z C     
8021  O  O     . THR F 176 ? 0.6537 0.3106 0.3324 -0.0359 0.2091 0.0021  176 THR Z O     
8022  C  CB    . THR F 176 ? 0.67   0.3176 0.3365 -0.0357 0.2124 -0.0027 176 THR Z CB    
8023  O  OG1   . THR F 176 ? 0.6849 0.3313 0.3457 -0.0353 0.2113 -0.005  176 THR Z OG1   
8024  C  CG2   . THR F 176 ? 0.6757 0.3193 0.3394 -0.0358 0.2148 -0.0033 176 THR Z CG2   
8025  N  N     . GLY F 177 ? 0.6446 0.2985 0.3155 -0.0399 0.205  -0.0013 177 GLY Z N     
8026  C  CA    . GLY F 177 ? 0.6415 0.298  0.3136 -0.0386 0.2038 -0.0007 177 GLY Z CA    
8027  C  C     . GLY F 177 ? 0.6373 0.2924 0.3052 -0.0351 0.2059 -0.0024 177 GLY Z C     
8028  O  O     . GLY F 177 ? 0.6387 0.295  0.3065 -0.0338 0.2054 -0.0022 177 GLY Z O     
8029  N  N     . ASN F 178 ? 0.6316 0.2841 0.2956 -0.0335 0.2081 -0.0041 178 ASN Z N     
8030  C  CA    . ASN F 178 ? 0.6352 0.2867 0.295  -0.0304 0.21   -0.0056 178 ASN Z CA    
8031  C  C     . ASN F 178 ? 0.6369 0.2871 0.2907 -0.0314 0.2088 -0.008  178 ASN Z C     
8032  O  O     . ASN F 178 ? 0.6405 0.2894 0.2927 -0.0341 0.2071 -0.0086 178 ASN Z O     
8033  C  CB    . ASN F 178 ? 0.6503 0.3005 0.3101 -0.0279 0.2134 -0.0055 178 ASN Z CB    
8034  C  CG    . ASN F 178 ? 0.6896 0.3392 0.3459 -0.0245 0.2156 -0.0064 178 ASN Z CG    
8035  O  OD1   . ASN F 178 ? 0.7073 0.3576 0.362  -0.0238 0.2148 -0.0067 178 ASN Z OD1   
8036  N  ND2   . ASN F 178 ? 0.6946 0.3428 0.3494 -0.0224 0.2182 -0.0067 178 ASN Z ND2   
8037  N  N     . PHE F 179 ? 0.6319 0.2822 0.282  -0.0293 0.2098 -0.0092 179 PHE Z N     
8038  C  CA    . PHE F 179 ? 0.6326 0.2826 0.2775 -0.0299 0.2089 -0.011  179 PHE Z CA    
8039  C  C     . PHE F 179 ? 0.6356 0.2846 0.2771 -0.0279 0.2114 -0.0118 179 PHE Z C     
8040  O  O     . PHE F 179 ? 0.6389 0.2887 0.2792 -0.0254 0.2133 -0.0119 179 PHE Z O     
8041  C  CB    . PHE F 179 ? 0.6295 0.2809 0.2723 -0.0293 0.2082 -0.0116 179 PHE Z CB    
8042  C  CG    . PHE F 179 ? 0.6385 0.2904 0.2766 -0.0302 0.2072 -0.0131 179 PHE Z CG    
8043  C  CD1   . PHE F 179 ? 0.6496 0.3006 0.2865 -0.0326 0.2052 -0.0137 179 PHE Z CD1   
8044  C  CD2   . PHE F 179 ? 0.6502 0.3036 0.2849 -0.0288 0.208  -0.0139 179 PHE Z CD2   
8045  C  CE1   . PHE F 179 ? 0.659  0.3106 0.2916 -0.0331 0.2046 -0.0148 179 PHE Z CE1   
8046  C  CE2   . PHE F 179 ? 0.6612 0.3159 0.2921 -0.0296 0.2071 -0.0148 179 PHE Z CE2   
8047  C  CZ    . PHE F 179 ? 0.6579 0.3117 0.2879 -0.0316 0.2055 -0.0153 179 PHE Z CZ    
8048  N  N     . ILE F 180 ? 0.6307 0.2774 0.2701 -0.0291 0.2116 -0.0123 180 ILE Z N     
8049  C  CA    . ILE F 180 ? 0.6286 0.2737 0.264  -0.027  0.2141 -0.0129 180 ILE Z CA    
8050  C  C     . ILE F 180 ? 0.6304 0.2745 0.2609 -0.0281 0.2131 -0.0139 180 ILE Z C     
8051  O  O     . ILE F 180 ? 0.6337 0.2755 0.2637 -0.0309 0.2114 -0.014  180 ILE Z O     
8052  C  CB    . ILE F 180 ? 0.6302 0.2721 0.2668 -0.0273 0.2158 -0.0122 180 ILE Z CB    
8053  C  CG1   . ILE F 180 ? 0.6316 0.2748 0.2739 -0.0264 0.2167 -0.0108 180 ILE Z CG1   
8054  C  CG2   . ILE F 180 ? 0.6401 0.2797 0.272  -0.0248 0.2188 -0.0127 180 ILE Z CG2   
8055  C  CD1   . ILE F 180 ? 0.6416 0.2843 0.2885 -0.0294 0.2151 -0.0095 180 ILE Z CD1   
8056  N  N     . VAL F 181 ? 0.6283 0.2746 0.2554 -0.0262 0.214  -0.0144 181 VAL Z N     
8057  C  CA    . VAL F 181 ? 0.6364 0.2823 0.2591 -0.0269 0.2132 -0.015  181 VAL Z CA    
8058  C  C     . VAL F 181 ? 0.6409 0.2879 0.2592 -0.0238 0.2159 -0.0149 181 VAL Z C     
8059  O  O     . VAL F 181 ? 0.6415 0.2907 0.2602 -0.0212 0.2179 -0.0145 181 VAL Z O     
8060  C  CB    . VAL F 181 ? 0.6432 0.2922 0.2669 -0.0286 0.2105 -0.0154 181 VAL Z CB    
8061  C  CG1   . VAL F 181 ? 0.6514 0.3048 0.2747 -0.0268 0.2111 -0.0154 181 VAL Z CG1   
8062  C  CG2   . VAL F 181 ? 0.6493 0.297  0.2696 -0.0303 0.209  -0.0159 181 VAL Z CG2   
8063  N  N     . GLN F 182 ? 0.6402 0.2854 0.2541 -0.024  0.216  -0.0151 182 GLN Z N     
8064  C  CA    . GLN F 182 ? 0.6434 0.2901 0.2529 -0.021  0.2185 -0.0146 182 GLN Z CA    
8065  C  C     . GLN F 182 ? 0.6422 0.2932 0.2509 -0.0219 0.2166 -0.0146 182 GLN Z C     
8066  O  O     . GLN F 182 ? 0.6449 0.2939 0.253  -0.0244 0.2145 -0.0151 182 GLN Z O     
8067  C  CB    . GLN F 182 ? 0.6656 0.306  0.2697 -0.0202 0.2207 -0.0144 182 GLN Z CB    
8068  C  CG    . GLN F 182 ? 0.7021 0.3434 0.3021 -0.0159 0.2244 -0.0134 182 GLN Z CG    
8069  C  CD    . GLN F 182 ? 0.755  0.3883 0.3491 -0.0152 0.227  -0.0133 182 GLN Z CD    
8070  O  OE1   . GLN F 182 ? 0.7827 0.4115 0.3726 -0.0167 0.2264 -0.0136 182 GLN Z OE1   
8071  N  NE2   . GLN F 182 ? 0.7546 0.3853 0.3476 -0.0129 0.23   -0.013  182 GLN Z NE2   
8072  N  N     . ALA F 183 ? 0.6337 0.2906 0.2427 -0.02   0.2172 -0.014  183 ALA Z N     
8073  C  CA    . ALA F 183 ? 0.6308 0.2928 0.2394 -0.0209 0.2156 -0.0137 183 ALA Z CA    
8074  C  C     . ALA F 183 ? 0.6276 0.2929 0.2326 -0.0178 0.2181 -0.0123 183 ALA Z C     
8075  O  O     . ALA F 183 ? 0.6313 0.2977 0.2354 -0.0147 0.2207 -0.0114 183 ALA Z O     
8076  C  CB    . ALA F 183 ? 0.629  0.2956 0.2407 -0.0218 0.2141 -0.0139 183 ALA Z CB    
8077  N  N     . TYR F 184 ? 0.6194 0.2864 0.2222 -0.0184 0.2175 -0.0118 184 TYR Z N     
8078  C  CA    . TYR F 184 ? 0.6181 0.2884 0.2175 -0.0151 0.2201 -0.0099 184 TYR Z CA    
8079  C  C     . TYR F 184 ? 0.6129 0.2919 0.2137 -0.0155 0.2189 -0.0088 184 TYR Z C     
8080  O  O     . TYR F 184 ? 0.6089 0.2891 0.2108 -0.0186 0.2162 -0.0095 184 TYR Z O     
8081  C  CB    . TYR F 184 ? 0.622  0.2863 0.2165 -0.0146 0.2214 -0.0097 184 TYR Z CB    
8082  C  CG    . TYR F 184 ? 0.6311 0.2863 0.2241 -0.0155 0.2217 -0.0111 184 TYR Z CG    
8083  C  CD1   . TYR F 184 ? 0.6409 0.2921 0.2312 -0.0127 0.225  -0.0106 184 TYR Z CD1   
8084  C  CD2   . TYR F 184 ? 0.6417 0.2926 0.2363 -0.0195 0.2187 -0.0127 184 TYR Z CD2   
8085  C  CE1   . TYR F 184 ? 0.6528 0.2959 0.2419 -0.0141 0.2251 -0.0117 184 TYR Z CE1   
8086  C  CE2   . TYR F 184 ? 0.6529 0.2966 0.2469 -0.0208 0.2186 -0.0137 184 TYR Z CE2   
8087  C  CZ    . TYR F 184 ? 0.6643 0.3041 0.2555 -0.0184 0.2218 -0.0132 184 TYR Z CZ    
8088  O  OH    . TYR F 184 ? 0.6862 0.3187 0.2764 -0.0202 0.2217 -0.0141 184 TYR Z OH    
8089  N  N     . PHE F 185 ? 0.6111 0.2964 0.2117 -0.0126 0.2208 -0.007  185 PHE Z N     
8090  C  CA    . PHE F 185 ? 0.6159 0.3105 0.2178 -0.0131 0.2197 -0.0054 185 PHE Z CA    
8091  C  C     . PHE F 185 ? 0.6302 0.3281 0.2291 -0.0098 0.2225 -0.0028 185 PHE Z C     
8092  O  O     . PHE F 185 ? 0.6301 0.3245 0.2259 -0.006  0.2258 -0.0019 185 PHE Z O     
8093  C  CB    . PHE F 185 ? 0.6071 0.3074 0.2111 -0.0124 0.2196 -0.0049 185 PHE Z CB    
8094  C  CG    . PHE F 185 ? 0.6075 0.3064 0.2141 -0.0159 0.2167 -0.0069 185 PHE Z CG    
8095  C  CD1   . PHE F 185 ? 0.6174 0.3095 0.2249 -0.0187 0.2149 -0.009  185 PHE Z CD1   
8096  C  CD2   . PHE F 185 ? 0.6125 0.3167 0.2203 -0.0163 0.2158 -0.0064 185 PHE Z CD2   
8097  C  CE1   . PHE F 185 ? 0.6239 0.3144 0.2333 -0.0213 0.2128 -0.0105 185 PHE Z CE1   
8098  C  CE2   . PHE F 185 ? 0.6209 0.3227 0.23   -0.0192 0.2136 -0.0082 185 PHE Z CE2   
8099  C  CZ    . PHE F 185 ? 0.6191 0.314  0.229  -0.0215 0.2122 -0.0101 185 PHE Z CZ    
8100  N  N     . ARG F 186 ? 0.6397 0.3443 0.2394 -0.0112 0.2212 -0.0015 186 ARG Z N     
8101  C  CA    . ARG F 186 ? 0.6571 0.3659 0.2544 -0.008  0.2237 0.0014  186 ARG Z CA    
8102  C  C     . ARG F 186 ? 0.6658 0.3823 0.2632 -0.0038 0.2264 0.0044  186 ARG Z C     
8103  O  O     . ARG F 186 ? 0.6619 0.3876 0.2624 -0.0049 0.2248 0.0055  186 ARG Z O     
8104  C  CB    . ARG F 186 ? 0.6783 0.3927 0.2769 -0.0109 0.2215 0.0022  186 ARG Z CB    
8105  C  CG    . ARG F 186 ? 0.7236 0.4418 0.3197 -0.0075 0.2244 0.0055  186 ARG Z CG    
8106  C  CD    . ARG F 186 ? 0.7637 0.4922 0.3624 -0.0096 0.2227 0.0076  186 ARG Z CD    
8107  N  NE    . ARG F 186 ? 0.8069 0.5329 0.4067 -0.0147 0.2192 0.0054  186 ARG Z NE    
8108  C  CZ    . ARG F 186 ? 0.8408 0.5628 0.4384 -0.0152 0.2194 0.0053  186 ARG Z CZ    
8109  N  NH1   . ARG F 186 ? 0.8359 0.5554 0.4297 -0.011  0.2229 0.0073  186 ARG Z NH1   
8110  N  NH2   . ARG F 186 ? 0.8471 0.5669 0.4457 -0.0198 0.2162 0.0033  186 ARG Z NH2   
8111  N  N     . GLY F 187 ? 0.6767 0.3892 0.2703 0.001   0.2304 0.0056  187 GLY Z N     
8112  C  CA    . GLY F 187 ? 0.6891 0.4083 0.2822 0.0058  0.2336 0.0088  187 GLY Z CA    
8113  C  C     . GLY F 187 ? 0.6966 0.4259 0.29   0.0078  0.2348 0.0127  187 GLY Z C     
8114  O  O     . GLY F 187 ? 0.6989 0.4272 0.2912 0.0066  0.2344 0.013   187 GLY Z O     
8115  N  N     . GLU F 188 ? 0.6976 0.4369 0.2925 0.0109  0.2362 0.0158  188 GLU Z N     
8116  C  CA    . GLU F 188 ? 0.7041 0.4547 0.2999 0.0131  0.2375 0.0202  188 GLU Z CA    
8117  C  C     . GLU F 188 ? 0.7163 0.4622 0.307  0.0182  0.2421 0.0225  188 GLU Z C     
8118  O  O     . GLU F 188 ? 0.7178 0.4695 0.3088 0.0187  0.2427 0.0253  188 GLU Z O     
8119  C  CB    . GLU F 188 ? 0.7276 0.4898 0.3259 0.0158  0.2383 0.0233  188 GLU Z CB    
8120  C  CG    . GLU F 188 ? 0.783  0.5493 0.3852 0.0111  0.2339 0.0213  188 GLU Z CG    
8121  C  CD    . GLU F 188 ? 0.8571 0.6168 0.4583 0.0124  0.2346 0.019   188 GLU Z CD    
8122  O  OE1   . GLU F 188 ? 0.867  0.6152 0.4648 0.0144  0.237  0.017   188 GLU Z OE1   
8123  O  OE2   . GLU F 188 ? 0.8851 0.6509 0.4886 0.0113  0.2328 0.0192  188 GLU Z OE2   
8124  N  N     . GLU F 189 ? 0.7248 0.4597 0.3102 0.0217  0.2456 0.0215  189 GLU Z N     
8125  C  CA    . GLU F 189 ? 0.7392 0.4677 0.3181 0.0266  0.2504 0.0235  189 GLU Z CA    
8126  C  C     . GLU F 189 ? 0.7495 0.466  0.3247 0.0235  0.2494 0.0206  189 GLU Z C     
8127  O  O     . GLU F 189 ? 0.7552 0.4632 0.3235 0.0271  0.2533 0.0216  189 GLU Z O     
8128  C  CB    . GLU F 189 ? 0.7745 0.4971 0.3482 0.0323  0.2552 0.0245  189 GLU Z CB    
8129  C  CG    . GLU F 189 ? 0.8377 0.5726 0.4127 0.0379  0.2583 0.0294  189 GLU Z CG    
8130  C  CD    . GLU F 189 ? 0.9274 0.6569 0.4969 0.0442  0.2635 0.0308  189 GLU Z CD    
8131  O  OE1   . GLU F 189 ? 0.9411 0.6597 0.5082 0.043   0.2636 0.0272  189 GLU Z OE1   
8132  O  OE2   . GLU F 189 ? 0.9595 0.6958 0.5272 0.0503  0.2677 0.0356  189 GLU Z OE2   
8133  N  N     . TYR F 190 ? 0.7482 0.464  0.3274 0.0171  0.2443 0.0173  190 TYR Z N     
8134  C  CA    . TYR F 190 ? 0.7577 0.4638 0.334  0.0141  0.243  0.0149  190 TYR Z CA    
8135  C  C     . TYR F 190 ? 0.7609 0.4735 0.337  0.0152  0.2438 0.0181  190 TYR Z C     
8136  O  O     . TYR F 190 ? 0.7588 0.4813 0.3404 0.0119  0.2406 0.0187  190 TYR Z O     
8137  C  CB    . TYR F 190 ? 0.7562 0.4603 0.337  0.0074  0.2375 0.0107  190 TYR Z CB    
8138  C  CG    . TYR F 190 ? 0.7677 0.4638 0.346  0.0042  0.2358 0.0087  190 TYR Z CG    
8139  C  CD1   . TYR F 190 ? 0.7846 0.4675 0.3567 0.0048  0.2373 0.007   190 TYR Z CD1   
8140  C  CD2   . TYR F 190 ? 0.7761 0.4775 0.3579 0.0004  0.2325 0.0085  190 TYR Z CD2   
8141  C  CE1   . TYR F 190 ? 0.7988 0.4745 0.3684 0.0019  0.2356 0.0053  190 TYR Z CE1   
8142  C  CE2   . TYR F 190 ? 0.7899 0.4839 0.3692 -0.0023 0.231  0.0068  190 TYR Z CE2   
8143  C  CZ    . TYR F 190 ? 0.8071 0.4884 0.3803 -0.0014 0.2325 0.0052  190 TYR Z CZ    
8144  O  OH    . TYR F 190 ? 0.8294 0.5034 0.3998 -0.004  0.2309 0.0036  190 TYR Z OH    
8145  N  N     . GLN F 191 ? 0.7625 0.4699 0.3321 0.02    0.2483 0.0205  191 GLN Z N     
8146  C  CA    . GLN F 191 ? 0.7638 0.4771 0.3327 0.0218  0.2499 0.024   191 GLN Z CA    
8147  C  C     . GLN F 191 ? 0.7697 0.4694 0.3309 0.0223  0.2516 0.0228  191 GLN Z C     
8148  O  O     . GLN F 191 ? 0.7774 0.4704 0.3311 0.0276  0.2566 0.025   191 GLN Z O     
8149  C  CB    . GLN F 191 ? 0.7823 0.5041 0.3502 0.0287  0.2548 0.0294  191 GLN Z CB    
8150  C  CG    . GLN F 191 ? 0.818  0.5562 0.392  0.0288  0.2541 0.0335  191 GLN Z CG    
8151  C  CD    . GLN F 191 ? 0.8684 0.617  0.4508 0.0232  0.2487 0.032   191 GLN Z CD    
8152  O  OE1   . GLN F 191 ? 0.8848 0.6352 0.4693 0.0229  0.2477 0.0308  191 GLN Z OE1   
8153  N  NE2   . GLN F 191 ? 0.8731 0.628  0.4597 0.0187  0.2452 0.032   191 GLN Z NE2   
8154  N  N     . PRO F 192 ? 0.7654 0.4599 0.3276 0.0167  0.2474 0.0194  192 PRO Z N     
8155  C  CA    . PRO F 192 ? 0.7706 0.4512 0.325  0.0165  0.2485 0.0178  192 PRO Z CA    
8156  C  C     . PRO F 192 ? 0.7708 0.4515 0.3204 0.0204  0.2521 0.0215  192 PRO Z C     
8157  O  O     . PRO F 192 ? 0.777  0.445  0.3179 0.0222  0.2547 0.0212  192 PRO Z O     
8158  C  CB    . PRO F 192 ? 0.779  0.457  0.3373 0.0096  0.2428 0.0137  192 PRO Z CB    
8159  C  CG    . PRO F 192 ? 0.7768 0.4689 0.3441 0.0068  0.2395 0.0143  192 PRO Z CG    
8160  C  CD    . PRO F 192 ? 0.7538 0.4539 0.3235 0.0103  0.2417 0.0166  192 PRO Z CD    
8161  N  N     . LYS F 193 ? 0.7611 0.4558 0.3161 0.0217  0.2524 0.0253  193 LYS Z N     
8162  C  CA    . LYS F 193 ? 0.762  0.4585 0.3133 0.0259  0.2562 0.0295  193 LYS Z CA    
8163  C  C     . LYS F 193 ? 0.7666 0.4594 0.3106 0.0337  0.263  0.0332  193 LYS Z C     
8164  O  O     . LYS F 193 ? 0.7734 0.4626 0.3113 0.0379  0.267  0.0363  193 LYS Z O     
8165  C  CB    . LYS F 193 ? 0.7717 0.4859 0.3317 0.0248  0.2547 0.0328  193 LYS Z CB    
8166  C  CG    . LYS F 193 ? 0.812  0.5302 0.3787 0.0172  0.2483 0.0294  193 LYS Z CG    
8167  C  CD    . LYS F 193 ? 0.8528 0.5886 0.4277 0.0158  0.2468 0.0328  193 LYS Z CD    
8168  C  CE    . LYS F 193 ? 0.8893 0.628  0.4698 0.0082  0.2409 0.0295  193 LYS Z CE    
8169  N  NZ    . LYS F 193 ? 0.9024 0.6579 0.4906 0.006   0.2389 0.0324  193 LYS Z NZ    
8170  N  N     . TYR F 194 ? 0.7627 0.4557 0.3066 0.0361  0.2645 0.0332  194 TYR Z N     
8171  C  CA    . TYR F 194 ? 0.7675 0.4571 0.3042 0.0438  0.2711 0.0369  194 TYR Z CA    
8172  C  C     . TYR F 194 ? 0.7727 0.4448 0.3    0.0449  0.2733 0.0339  194 TYR Z C     
8173  O  O     . TYR F 194 ? 0.7814 0.4462 0.2997 0.0511  0.2793 0.0367  194 TYR Z O     
8174  C  CB    . TYR F 194 ? 0.7623 0.4675 0.3058 0.0468  0.2721 0.0404  194 TYR Z CB    
8175  C  CG    . TYR F 194 ? 0.7676 0.4902 0.319  0.0467  0.2709 0.0445  194 TYR Z CG    
8176  C  CD1   . TYR F 194 ? 0.7832 0.5106 0.3318 0.0527  0.2759 0.0502  194 TYR Z CD1   
8177  C  CD2   . TYR F 194 ? 0.7723 0.506  0.3335 0.0403  0.2649 0.0427  194 TYR Z CD2   
8178  C  CE1   . TYR F 194 ? 0.7884 0.5322 0.3446 0.0521  0.2747 0.0542  194 TYR Z CE1   
8179  C  CE2   . TYR F 194 ? 0.7785 0.5278 0.3465 0.0394  0.2637 0.0465  194 TYR Z CE2   
8180  C  CZ    . TYR F 194 ? 0.7914 0.5461 0.3573 0.0452  0.2685 0.0523  194 TYR Z CZ    
8181  O  OH    . TYR F 194 ? 0.8027 0.5735 0.3757 0.0442  0.2672 0.0563  194 TYR Z OH    
8182  N  N     . ASP F 195 ? 0.7664 0.4314 0.2951 0.0389  0.2688 0.0286  195 ASP Z N     
8183  C  CA    . ASP F 195 ? 0.7739 0.4228 0.2942 0.0392  0.2705 0.0257  195 ASP Z CA    
8184  C  C     . ASP F 195 ? 0.7738 0.4086 0.2887 0.0343  0.2679 0.0218  195 ASP Z C     
8185  O  O     . ASP F 195 ? 0.7681 0.405  0.2894 0.028   0.2622 0.0184  195 ASP Z O     
8186  C  CB    . ASP F 195 ? 0.7978 0.4493 0.3231 0.0373  0.2686 0.0234  195 ASP Z CB    
8187  C  CG    . ASP F 195 ? 0.8689 0.507  0.3852 0.0402  0.2725 0.0226  195 ASP Z CG    
8188  O  OD1   . ASP F 195 ? 0.8863 0.509  0.3932 0.0394  0.2738 0.0209  195 ASP Z OD1   
8189  O  OD2   . ASP F 195 ? 0.8965 0.5392 0.4148 0.0431  0.2744 0.0236  195 ASP Z OD2   
8190  N  N     . LYS F 196 ? 0.7804 0.4004 0.2831 0.0372  0.2721 0.0223  196 LYS Z N     
8191  C  CA    . LYS F 196 ? 0.7914 0.3967 0.2872 0.033   0.27   0.0189  196 LYS Z CA    
8192  C  C     . LYS F 196 ? 0.7916 0.3899 0.2888 0.027   0.2657 0.014   196 LYS Z C     
8193  O  O     . LYS F 196 ? 0.7976 0.3888 0.2936 0.0217  0.2618 0.0109  196 LYS Z O     
8194  C  CB    . LYS F 196 ? 0.8273 0.4177 0.3084 0.0379  0.276  0.0209  196 LYS Z CB    
8195  C  CG    . LYS F 196 ? 0.8812 0.4777 0.3601 0.0444  0.2807 0.0261  196 LYS Z CG    
8196  C  CD    . LYS F 196 ? 0.9247 0.5299 0.4102 0.0415  0.2772 0.0265  196 LYS Z CD    
8197  C  CE    . LYS F 196 ? 0.9678 0.5723 0.4468 0.0474  0.2824 0.0312  196 LYS Z CE    
8198  N  NZ    . LYS F 196 ? 0.9904 0.6039 0.4698 0.0552  0.2882 0.0367  196 LYS Z NZ    
8199  N  N     . LYS F 197 ? 0.7829 0.3835 0.2829 0.0278  0.2664 0.0135  197 LYS Z N     
8200  C  CA    . LYS F 197 ? 0.7865 0.3815 0.2887 0.0224  0.2626 0.0093  197 LYS Z CA    
8201  C  C     . LYS F 197 ? 0.7803 0.3845 0.2939 0.0162  0.2559 0.0067  197 LYS Z C     
8202  O  O     . LYS F 197 ? 0.7847 0.3831 0.2995 0.0108  0.2521 0.0033  197 LYS Z O     
8203  C  CB    . LYS F 197 ? 0.8104 0.4073 0.3138 0.0251  0.2651 0.0098  197 LYS Z CB    
8204  C  CG    . LYS F 197 ? 0.8702 0.4549 0.3612 0.0304  0.2715 0.0115  197 LYS Z CG    
8205  C  CD    . LYS F 197 ? 0.9208 0.5073 0.4133 0.0328  0.2737 0.0117  197 LYS Z CD    
8206  C  CE    . LYS F 197 ? 0.9765 0.5488 0.4555 0.0376  0.2802 0.013   197 LYS Z CE    
8207  N  NZ    . LYS F 197 ? 1.0105 0.565  0.4797 0.0332  0.2793 0.01    197 LYS Z NZ    
8208  N  N     . LEU F 198 ? 0.7673 0.3859 0.2892 0.0168  0.2545 0.0086  198 LEU Z N     
8209  C  CA    . LEU F 198 ? 0.7586 0.386  0.2906 0.0113  0.2487 0.0064  198 LEU Z CA    
8210  C  C     . LEU F 198 ? 0.7557 0.3821 0.2872 0.0085  0.2462 0.006   198 LEU Z C     
8211  O  O     . LEU F 198 ? 0.756  0.3897 0.2953 0.0043  0.2417 0.0045  198 LEU Z O     
8212  C  CB    . LEU F 198 ? 0.7519 0.3954 0.2929 0.0129  0.2483 0.0086  198 LEU Z CB    
8213  C  CG    . LEU F 198 ? 0.7725 0.419  0.3147 0.0161  0.2508 0.0095  198 LEU Z CG    
8214  C  CD1   . LEU F 198 ? 0.7721 0.4344 0.3214 0.0183  0.251  0.0125  198 LEU Z CD1   
8215  C  CD2   . LEU F 198 ? 0.7839 0.4261 0.3291 0.012   0.2477 0.0058  198 LEU Z CD2   
8216  N  N     . LYS F 199 ? 0.7497 0.3668 0.2718 0.0109  0.2492 0.0072  199 LYS Z N     
8217  C  CA    . LYS F 199 ? 0.7459 0.3613 0.2666 0.0088  0.2473 0.007   199 LYS Z CA    
8218  C  C     . LYS F 199 ? 0.7393 0.3517 0.2638 0.002   0.2414 0.003   199 LYS Z C     
8219  O  O     . LYS F 199 ? 0.7389 0.3568 0.2679 -0.0006 0.2384 0.0026  199 LYS Z O     
8220  C  CB    . LYS F 199 ? 0.7737 0.3764 0.2819 0.0123  0.2516 0.0085  199 LYS Z CB    
8221  C  CG    . LYS F 199 ? 0.8199 0.4285 0.3258 0.019   0.257  0.0134  199 LYS Z CG    
8222  C  CD    . LYS F 199 ? 0.8792 0.4812 0.3777 0.0204  0.2587 0.0148  199 LYS Z CD    
8223  C  CE    . LYS F 199 ? 0.9363 0.5191 0.4206 0.0214  0.2614 0.0137  199 LYS Z CE    
8224  N  NZ    . LYS F 199 ? 0.9655 0.5433 0.4411 0.0285  0.2685 0.0172  199 LYS Z NZ    
8225  N  N     . PHE F 200 ? 0.7324 0.3365 0.2551 -0.0009 0.2398 0.0001  200 PHE Z N     
8226  C  CA    . PHE F 200 ? 0.7292 0.3305 0.2553 -0.0071 0.2343 -0.0033 200 PHE Z CA    
8227  C  C     . PHE F 200 ? 0.7196 0.3286 0.2555 -0.01   0.231  -0.005  200 PHE Z C     
8228  O  O     . PHE F 200 ? 0.7236 0.3277 0.2607 -0.0142 0.2278 -0.0076 200 PHE Z O     
8229  C  CB    . PHE F 200 ? 0.7364 0.322  0.2529 -0.0091 0.2342 -0.0051 200 PHE Z CB    
8230  C  CG    . PHE F 200 ? 0.7482 0.3252 0.2544 -0.0065 0.2373 -0.0035 200 PHE Z CG    
8231  C  CD1   . PHE F 200 ? 0.7568 0.3358 0.2636 -0.0076 0.2355 -0.0033 200 PHE Z CD1   
8232  C  CD2   . PHE F 200 ? 0.7638 0.3307 0.2591 -0.0024 0.2424 -0.002  200 PHE Z CD2   
8233  C  CE1   . PHE F 200 ? 0.7704 0.3415 0.2674 -0.0048 0.2386 -0.0017 200 PHE Z CE1   
8234  C  CE2   . PHE F 200 ? 0.7789 0.3374 0.264  0.0005  0.2456 -0.0003 200 PHE Z CE2   
8235  C  CZ    . PHE F 200 ? 0.7748 0.3356 0.261  -0.0006 0.2437 -0.0001 200 PHE Z CZ    
8236  N  N     . PHE F 201 ? 0.7054 0.3265 0.2482 -0.008  0.2317 -0.0034 201 PHE Z N     
8237  C  CA    . PHE F 201 ? 0.6976 0.3259 0.2493 -0.0105 0.2287 -0.0049 201 PHE Z CA    
8238  C  C     . PHE F 201 ? 0.6958 0.3312 0.2541 -0.0143 0.2245 -0.0058 201 PHE Z C     
8239  O  O     . PHE F 201 ? 0.6977 0.3388 0.2565 -0.0132 0.225  -0.0041 201 PHE Z O     
8240  C  CB    . PHE F 201 ? 0.6867 0.3237 0.2416 -0.0066 0.2315 -0.0028 201 PHE Z CB    
8241  C  CG    . PHE F 201 ? 0.6856 0.3287 0.2485 -0.0091 0.2288 -0.0043 201 PHE Z CG    
8242  C  CD1   . PHE F 201 ? 0.6968 0.3335 0.2597 -0.0109 0.2279 -0.0064 201 PHE Z CD1   
8243  C  CD2   . PHE F 201 ? 0.6885 0.3431 0.2583 -0.0097 0.2271 -0.0035 201 PHE Z CD2   
8244  C  CE1   . PHE F 201 ? 0.7018 0.3438 0.2718 -0.0127 0.2257 -0.0075 201 PHE Z CE1   
8245  C  CE2   . PHE F 201 ? 0.6937 0.3528 0.2698 -0.0119 0.2247 -0.005  201 PHE Z CE2   
8246  C  CZ    . PHE F 201 ? 0.6933 0.346  0.2695 -0.0131 0.2242 -0.0069 201 PHE Z CZ    
8247  N  N     . ASP F 202 ? 0.6896 0.3245 0.2526 -0.0186 0.2205 -0.0083 202 ASP Z N     
8248  C  CA    . ASP F 202 ? 0.6867 0.3274 0.2554 -0.022  0.2167 -0.0093 202 ASP Z CA    
8249  C  C     . ASP F 202 ? 0.6779 0.329  0.2536 -0.0219 0.2161 -0.0088 202 ASP Z C     
8250  O  O     . ASP F 202 ? 0.6824 0.3337 0.2612 -0.0225 0.2155 -0.0098 202 ASP Z O     
8251  C  CB    . ASP F 202 ? 0.7107 0.3453 0.2804 -0.0264 0.2129 -0.0119 202 ASP Z CB    
8252  C  CG    . ASP F 202 ? 0.7639 0.4017 0.337  -0.0297 0.2094 -0.0128 202 ASP Z CG    
8253  O  OD1   . ASP F 202 ? 0.7718 0.4156 0.3458 -0.0289 0.2099 -0.0115 202 ASP Z OD1   
8254  O  OD2   . ASP F 202 ? 0.7867 0.4212 0.3617 -0.033  0.2063 -0.0146 202 ASP Z OD2   
8255  N  N     . GLU F 203 ? 0.6622 0.322  0.2402 -0.0214 0.2163 -0.0071 203 GLU Z N     
8256  C  CA    . GLU F 203 ? 0.6514 0.3211 0.2352 -0.0216 0.2155 -0.0065 203 GLU Z CA    
8257  C  C     . GLU F 203 ? 0.6462 0.3166 0.2349 -0.0257 0.2118 -0.0088 203 GLU Z C     
8258  O  O     . GLU F 203 ? 0.6451 0.3218 0.2377 -0.0261 0.2112 -0.0086 203 GLU Z O     
8259  C  CB    . GLU F 203 ? 0.6716 0.3504 0.2565 -0.0206 0.2164 -0.004  203 GLU Z CB    
8260  C  CG    . GLU F 203 ? 0.7301 0.4107 0.3114 -0.0156 0.2208 -0.0009 203 GLU Z CG    
8261  C  CD    . GLU F 203 ? 0.8065 0.4976 0.3894 -0.0142 0.2218 0.0023  203 GLU Z CD    
8262  O  OE1   . GLU F 203 ? 0.8232 0.521  0.4104 -0.0176 0.219  0.002   203 GLU Z OE1   
8263  O  OE2   . GLU F 203 ? 0.8316 0.524  0.4112 -0.0098 0.2256 0.0052  203 GLU Z OE2   
8264  N  N     . THR F 204 ? 0.646  0.3097 0.234  -0.0286 0.2094 -0.0109 204 THR Z N     
8265  C  CA    . THR F 204 ? 0.6528 0.3164 0.245  -0.0318 0.2063 -0.0128 204 THR Z CA    
8266  C  C     . THR F 204 ? 0.6578 0.3193 0.2519 -0.0311 0.2068 -0.0135 204 THR Z C     
8267  O  O     . THR F 204 ? 0.6629 0.3255 0.2608 -0.033  0.2049 -0.0145 204 THR Z O     
8268  C  CB    . THR F 204 ? 0.6767 0.3347 0.268  -0.0348 0.2036 -0.0143 204 THR Z CB    
8269  O  OG1   . THR F 204 ? 0.6974 0.3475 0.2861 -0.0348 0.2037 -0.0151 204 THR Z OG1   
8270  C  CG2   . THR F 204 ? 0.6831 0.342  0.2718 -0.0353 0.2035 -0.0136 204 THR Z CG2   
8271  N  N     . ILE F 205 ? 0.6521 0.3102 0.2432 -0.0282 0.2096 -0.0128 205 ILE Z N     
8272  C  CA    . ILE F 205 ? 0.6492 0.3051 0.2415 -0.0272 0.2107 -0.0132 205 ILE Z CA    
8273  C  C     . ILE F 205 ? 0.6417 0.3051 0.2379 -0.026  0.2112 -0.0125 205 ILE Z C     
8274  O  O     . ILE F 205 ? 0.6423 0.3051 0.2415 -0.0264 0.2108 -0.0133 205 ILE Z O     
8275  C  CB    . ILE F 205 ? 0.6612 0.3111 0.2481 -0.0244 0.2139 -0.0125 205 ILE Z CB    
8276  C  CG1   . ILE F 205 ? 0.6792 0.32   0.2621 -0.0265 0.2127 -0.0136 205 ILE Z CG1   
8277  C  CG2   . ILE F 205 ? 0.6686 0.3176 0.2565 -0.0225 0.2158 -0.0124 205 ILE Z CG2   
8278  C  CD1   . ILE F 205 ? 0.7011 0.3344 0.2768 -0.0242 0.2158 -0.0129 205 ILE Z CD1   
8279  N  N     . PHE F 206 ? 0.6358 0.3065 0.2321 -0.0246 0.2121 -0.0109 206 PHE Z N     
8280  C  CA    . PHE F 206 ? 0.6409 0.319  0.2403 -0.0239 0.2123 -0.0101 206 PHE Z CA    
8281  C  C     . PHE F 206 ? 0.6494 0.3281 0.2526 -0.0272 0.2093 -0.0117 206 PHE Z C     
8282  O  O     . PHE F 206 ? 0.6507 0.3281 0.2543 -0.0302 0.2069 -0.0127 206 PHE Z O     
8283  C  CB    . PHE F 206 ? 0.6362 0.3227 0.2352 -0.0227 0.2132 -0.0079 206 PHE Z CB    
8284  C  CG    . PHE F 206 ? 0.6454 0.3322 0.2408 -0.0185 0.2168 -0.0057 206 PHE Z CG    
8285  C  CD1   . PHE F 206 ? 0.6571 0.3415 0.2509 -0.015  0.2197 -0.0051 206 PHE Z CD1   
8286  C  CD2   . PHE F 206 ? 0.6547 0.3441 0.2479 -0.0177 0.2176 -0.0039 206 PHE Z CD2   
8287  C  CE1   . PHE F 206 ? 0.6662 0.35   0.2557 -0.0107 0.2235 -0.0029 206 PHE Z CE1   
8288  C  CE2   . PHE F 206 ? 0.6636 0.3528 0.253  -0.0134 0.2214 -0.0016 206 PHE Z CE2   
8289  C  CZ    . PHE F 206 ? 0.6624 0.3489 0.2498 -0.0098 0.2243 -0.001  206 PHE Z CZ    
8290  N  N     . ALA F 207 ? 0.6508 0.3304 0.2561 -0.0264 0.2098 -0.012  207 ALA Z N     
8291  C  CA    . ALA F 207 ? 0.6549 0.3335 0.2629 -0.0288 0.2076 -0.0133 207 ALA Z CA    
8292  C  C     . ALA F 207 ? 0.6555 0.34   0.2646 -0.0292 0.2071 -0.0129 207 ALA Z C     
8293  O  O     . ALA F 207 ? 0.6564 0.339  0.267  -0.0299 0.2064 -0.0137 207 ALA Z O     
8294  C  CB    . ALA F 207 ? 0.6564 0.3292 0.2658 -0.0282 0.2082 -0.0142 207 ALA Z CB    
8295  N  N     . GLU F 208 ? 0.6534 0.3447 0.2616 -0.0289 0.2074 -0.0114 208 GLU Z N     
8296  C  CA    . GLU F 208 ? 0.6588 0.3558 0.2675 -0.0298 0.2066 -0.0108 208 GLU Z CA    
8297  C  C     . GLU F 208 ? 0.6672 0.3619 0.2761 -0.0337 0.2039 -0.0123 208 GLU Z C     
8298  O  O     . GLU F 208 ? 0.6703 0.364  0.2794 -0.034  0.2036 -0.0129 208 GLU Z O     
8299  C  CB    . GLU F 208 ? 0.6793 0.3849 0.2873 -0.0295 0.2069 -0.0086 208 GLU Z CB    
8300  C  CG    . GLU F 208 ? 0.7277 0.4372 0.3353 -0.0251 0.2099 -0.0066 208 GLU Z CG    
8301  C  CD    . GLU F 208 ? 0.8007 0.5095 0.4067 -0.0228 0.2119 -0.0054 208 GLU Z CD    
8302  O  OE1   . GLU F 208 ? 0.8119 0.515  0.4171 -0.0243 0.211  -0.0067 208 GLU Z OE1   
8303  O  OE2   . GLU F 208 ? 0.8323 0.546  0.4375 -0.0193 0.2143 -0.003  208 GLU Z OE2   
8304  N  N     . ASP F 209 ? 0.6692 0.3626 0.2776 -0.0363 0.2022 -0.013  209 ASP Z N     
8305  C  CA    . ASP F 209 ? 0.678  0.3685 0.2857 -0.0397 0.2    -0.0143 209 ASP Z CA    
8306  C  C     . ASP F 209 ? 0.6757 0.359  0.2845 -0.0394 0.1999 -0.0157 209 ASP Z C     
8307  O  O     . ASP F 209 ? 0.6772 0.3583 0.2854 -0.0407 0.1991 -0.0163 209 ASP Z O     
8308  C  CB    . ASP F 209 ? 0.7106 0.4012 0.3172 -0.0424 0.1984 -0.0145 209 ASP Z CB    
8309  C  CG    . ASP F 209 ? 0.7768 0.4749 0.3822 -0.0442 0.1978 -0.0131 209 ASP Z CG    
8310  O  OD1   . ASP F 209 ? 0.7862 0.4904 0.3921 -0.0425 0.1989 -0.0115 209 ASP Z OD1   
8311  O  OD2   . ASP F 209 ? 0.8041 0.5022 0.4083 -0.0473 0.1962 -0.0134 209 ASP Z OD2   
8312  N  N     . ASP F 210 ? 0.6704 0.35   0.2807 -0.0378 0.2007 -0.0159 210 ASP Z N     
8313  C  CA    . ASP F 210 ? 0.67   0.3439 0.2821 -0.0376 0.2005 -0.0168 210 ASP Z CA    
8314  C  C     . ASP F 210 ? 0.658  0.3311 0.2714 -0.0356 0.202  -0.0166 210 ASP Z C     
8315  O  O     . ASP F 210 ? 0.66   0.3294 0.2746 -0.0359 0.2017 -0.017  210 ASP Z O     
8316  C  CB    . ASP F 210 ? 0.7003 0.3706 0.3132 -0.0371 0.2006 -0.017  210 ASP Z CB    
8317  C  CG    . ASP F 210 ? 0.7678 0.437  0.3794 -0.0394 0.1988 -0.0174 210 ASP Z CG    
8318  O  OD1   . ASP F 210 ? 0.7769 0.4471 0.3876 -0.0415 0.1974 -0.0178 210 ASP Z OD1   
8319  O  OD2   . ASP F 210 ? 0.7998 0.4667 0.4108 -0.0391 0.1989 -0.0175 210 ASP Z OD2   
8320  N  N     . ILE F 211 ? 0.6446 0.3212 0.2577 -0.0333 0.2037 -0.0158 211 ILE Z N     
8321  C  CA    . ILE F 211 ? 0.638  0.3139 0.2519 -0.0312 0.2053 -0.0155 211 ILE Z CA    
8322  C  C     . ILE F 211 ? 0.624  0.3007 0.2363 -0.0327 0.2043 -0.0157 211 ILE Z C     
8323  O  O     . ILE F 211 ? 0.6247 0.2977 0.2375 -0.0321 0.2047 -0.0161 211 ILE Z O     
8324  C  CB    . ILE F 211 ? 0.6478 0.327  0.2613 -0.0281 0.2076 -0.0145 211 ILE Z CB    
8325  C  CG1   . ILE F 211 ? 0.6645 0.3402 0.2788 -0.0265 0.209  -0.0145 211 ILE Z CG1   
8326  C  CG2   . ILE F 211 ? 0.6542 0.334  0.2678 -0.026  0.209  -0.0142 211 ILE Z CG2   
8327  C  CD1   . ILE F 211 ? 0.6848 0.3548 0.3014 -0.0264 0.2092 -0.0152 211 ILE Z CD1   
8328  N  N     . ALA F 212 ? 0.611  0.2921 0.221  -0.0347 0.203  -0.0155 212 ALA Z N     
8329  C  CA    . ALA F 212 ? 0.6083 0.2894 0.2155 -0.0369 0.2018 -0.0157 212 ALA Z CA    
8330  C  C     . ALA F 212 ? 0.6041 0.2788 0.2106 -0.0387 0.2008 -0.0168 212 ALA Z C     
8331  O  O     . ALA F 212 ? 0.6071 0.2781 0.2119 -0.0387 0.2011 -0.017  212 ALA Z O     
8332  C  CB    . ALA F 212 ? 0.6092 0.2964 0.2143 -0.0394 0.2004 -0.0151 212 ALA Z CB    
8333  N  N     . ASP F 213 ? 0.5973 0.2702 0.2048 -0.0399 0.1998 -0.0172 213 ASP Z N     
8334  C  CA    . ASP F 213 ? 0.5967 0.264  0.2039 -0.0413 0.1989 -0.0179 213 ASP Z CA    
8335  C  C     . ASP F 213 ? 0.5918 0.2547 0.2015 -0.0389 0.2003 -0.0178 213 ASP Z C     
8336  O  O     . ASP F 213 ? 0.5958 0.2544 0.2041 -0.0392 0.2004 -0.0179 213 ASP Z O     
8337  C  CB    . ASP F 213 ? 0.6139 0.2808 0.222  -0.0426 0.1977 -0.0183 213 ASP Z CB    
8338  C  CG    . ASP F 213 ? 0.6661 0.336  0.2715 -0.0455 0.1963 -0.0184 213 ASP Z CG    
8339  O  OD1   . ASP F 213 ? 0.6741 0.3461 0.2765 -0.0471 0.1959 -0.0183 213 ASP Z OD1   
8340  O  OD2   . ASP F 213 ? 0.6958 0.3659 0.3017 -0.0462 0.1955 -0.0185 213 ASP Z OD2   
8341  N  N     . TYR F 214 ? 0.5815 0.2454 0.1946 -0.0366 0.2015 -0.0174 214 TYR Z N     
8342  C  CA    . TYR F 214 ? 0.5797 0.2403 0.1959 -0.0344 0.2029 -0.0169 214 TYR Z CA    
8343  C  C     . TYR F 214 ? 0.5713 0.2305 0.1858 -0.033  0.2043 -0.0166 214 TYR Z C     
8344  O  O     . TYR F 214 ? 0.5738 0.229  0.1888 -0.0323 0.2049 -0.0163 214 TYR Z O     
8345  C  CB    . TYR F 214 ? 0.583  0.2448 0.2022 -0.0326 0.204  -0.0166 214 TYR Z CB    
8346  C  CG    . TYR F 214 ? 0.597  0.256  0.2195 -0.0306 0.2055 -0.016  214 TYR Z CG    
8347  C  CD1   . TYR F 214 ? 0.611  0.2673 0.2365 -0.0312 0.2048 -0.0156 214 TYR Z CD1   
8348  C  CD2   . TYR F 214 ? 0.6105 0.2699 0.2333 -0.0282 0.2077 -0.0155 214 TYR Z CD2   
8349  C  CE1   . TYR F 214 ? 0.624  0.2785 0.253  -0.0296 0.2062 -0.0146 214 TYR Z CE1   
8350  C  CE2   . TYR F 214 ? 0.6235 0.2803 0.2494 -0.0264 0.2092 -0.0148 214 TYR Z CE2   
8351  C  CZ    . TYR F 214 ? 0.6353 0.2899 0.2645 -0.0272 0.2085 -0.0142 214 TYR Z CZ    
8352  O  OH    . TYR F 214 ? 0.6504 0.3034 0.2833 -0.0256 0.21   -0.0131 214 TYR Z OH    
8353  N  N     . ILE F 215 ? 0.5613 0.2239 0.1738 -0.0324 0.2049 -0.0166 215 ILE Z N     
8354  C  CA    . ILE F 215 ? 0.558  0.2194 0.1683 -0.0311 0.2061 -0.0163 215 ILE Z CA    
8355  C  C     . ILE F 215 ? 0.5591 0.2165 0.1651 -0.0331 0.2052 -0.0167 215 ILE Z C     
8356  O  O     . ILE F 215 ? 0.5699 0.2225 0.1752 -0.0317 0.2065 -0.0164 215 ILE Z O     
8357  C  CB    . ILE F 215 ? 0.5597 0.2265 0.1686 -0.0303 0.2066 -0.016  215 ILE Z CB    
8358  C  CG1   . ILE F 215 ? 0.5667 0.2358 0.179  -0.0275 0.2082 -0.0155 215 ILE Z CG1   
8359  C  CG2   . ILE F 215 ? 0.5668 0.2321 0.1724 -0.0294 0.2074 -0.0158 215 ILE Z CG2   
8360  C  CD1   . ILE F 215 ? 0.5791 0.2543 0.1901 -0.0265 0.2088 -0.0148 215 ILE Z CD1   
8361  N  N     . ILE F 216 ? 0.5487 0.2075 0.1516 -0.0363 0.2033 -0.0172 216 ILE Z N     
8362  C  CA    . ILE F 216 ? 0.5494 0.2035 0.147  -0.0386 0.2025 -0.0177 216 ILE Z CA    
8363  C  C     . ILE F 216 ? 0.5588 0.2065 0.1572 -0.0377 0.2031 -0.0175 216 ILE Z C     
8364  O  O     . ILE F 216 ? 0.5629 0.2049 0.1575 -0.0373 0.2041 -0.0173 216 ILE Z O     
8365  C  CB    . ILE F 216 ? 0.5475 0.2045 0.1419 -0.0425 0.2003 -0.0182 216 ILE Z CB    
8366  C  CG1   . ILE F 216 ? 0.5487 0.2124 0.1419 -0.0431 0.1998 -0.0178 216 ILE Z CG1   
8367  C  CG2   . ILE F 216 ? 0.5578 0.2086 0.1459 -0.0451 0.1996 -0.0187 216 ILE Z CG2   
8368  C  CD1   . ILE F 216 ? 0.5583 0.2271 0.1505 -0.0462 0.1979 -0.0178 216 ILE Z CD1   
8369  N  N     . ALA F 217 ? 0.5627 0.2114 0.1659 -0.0373 0.2028 -0.0173 217 ALA Z N     
8370  C  CA    . ALA F 217 ? 0.5761 0.2201 0.1808 -0.0363 0.2033 -0.0167 217 ALA Z CA    
8371  C  C     . ALA F 217 ? 0.5896 0.231  0.1968 -0.033  0.2056 -0.0156 217 ALA Z C     
8372  O  O     . ALA F 217 ? 0.5977 0.2341 0.2036 -0.0319 0.2067 -0.0147 217 ALA Z O     
8373  C  CB    . ALA F 217 ? 0.5754 0.2216 0.1846 -0.0369 0.202  -0.0167 217 ALA Z CB    
8374  N  N     . LYS F 218 ? 0.5891 0.2337 0.1995 -0.0311 0.2066 -0.0153 218 LYS Z N     
8375  C  CA    . LYS F 218 ? 0.6002 0.2426 0.213  -0.0279 0.209  -0.0142 218 LYS Z CA    
8376  C  C     . LYS F 218 ? 0.6132 0.2512 0.2202 -0.0272 0.2103 -0.0141 218 LYS Z C     
8377  O  O     . LYS F 218 ? 0.6166 0.2499 0.2234 -0.0251 0.2121 -0.013  218 LYS Z O     
8378  C  CB    . LYS F 218 ? 0.6213 0.2677 0.2379 -0.0263 0.2099 -0.0141 218 LYS Z CB    
8379  C  CG    . LYS F 218 ? 0.6702 0.3179 0.2931 -0.0256 0.21   -0.0134 218 LYS Z CG    
8380  C  CD    . LYS F 218 ? 0.7233 0.3678 0.3493 -0.0233 0.2118 -0.0117 218 LYS Z CD    
8381  C  CE    . LYS F 218 ? 0.7661 0.4125 0.3983 -0.0225 0.2124 -0.0108 218 LYS Z CE    
8382  N  NZ    . LYS F 218 ? 0.795  0.4436 0.4295 -0.0249 0.2102 -0.0112 218 LYS Z NZ    
8383  N  N     . LEU F 219 ? 0.6184 0.2577 0.2204 -0.029  0.2093 -0.0152 219 LEU Z N     
8384  C  CA    . LEU F 219 ? 0.6324 0.2671 0.2274 -0.029  0.2101 -0.0153 219 LEU Z CA    
8385  C  C     . LEU F 219 ? 0.6521 0.2797 0.242  -0.0301 0.2102 -0.0152 219 LEU Z C     
8386  O  O     . LEU F 219 ? 0.6594 0.2806 0.2447 -0.0286 0.212  -0.0146 219 LEU Z O     
8387  C  CB    . LEU F 219 ? 0.6314 0.2703 0.2225 -0.0316 0.2084 -0.0163 219 LEU Z CB    
8388  C  CG    . LEU F 219 ? 0.6433 0.2887 0.2379 -0.0301 0.2087 -0.0161 219 LEU Z CG    
8389  C  CD1   . LEU F 219 ? 0.6483 0.2991 0.2396 -0.0328 0.2068 -0.0166 219 LEU Z CD1   
8390  C  CD2   . LEU F 219 ? 0.6538 0.2967 0.2483 -0.0267 0.2112 -0.0154 219 LEU Z CD2   
8391  N  N     . GLN F 220 ? 0.6584 0.2865 0.2487 -0.0324 0.2085 -0.0156 220 GLN Z N     
8392  C  CA    . GLN F 220 ? 0.6767 0.2981 0.262  -0.0333 0.2087 -0.0154 220 GLN Z CA    
8393  C  C     . GLN F 220 ? 0.6808 0.2992 0.2704 -0.0301 0.2106 -0.0137 220 GLN Z C     
8394  O  O     . GLN F 220 ? 0.6821 0.2947 0.2677 -0.0301 0.2112 -0.0131 220 GLN Z O     
8395  C  CB    . GLN F 220 ? 0.7117 0.3354 0.296  -0.0371 0.2062 -0.0165 220 GLN Z CB    
8396  C  CG    . GLN F 220 ? 0.783  0.4085 0.3616 -0.0408 0.2044 -0.0178 220 GLN Z CG    
8397  C  CD    . GLN F 220 ? 0.8683 0.4858 0.437  -0.0432 0.2045 -0.0182 220 GLN Z CD    
8398  O  OE1   . GLN F 220 ? 0.8948 0.5127 0.4579 -0.0465 0.2031 -0.0191 220 GLN Z OE1   
8399  N  NE2   . GLN F 220 ? 0.8854 0.4952 0.4514 -0.0416 0.2062 -0.0175 220 GLN Z NE2   
8400  N  N     . HIS F 221 ? 0.6828 0.3054 0.2803 -0.0276 0.2114 -0.0127 221 HIS Z N     
8401  C  CA    . HIS F 221 ? 0.6945 0.3165 0.2977 -0.0249 0.2128 -0.0107 221 HIS Z CA    
8402  C  C     . HIS F 221 ? 0.6936 0.3161 0.2981 -0.0264 0.2112 -0.0105 221 HIS Z C     
8403  O  O     . HIS F 221 ? 0.7016 0.3194 0.3041 -0.0252 0.2123 -0.0091 221 HIS Z O     
8404  C  CB    . HIS F 221 ? 0.7213 0.337  0.322  -0.0214 0.2159 -0.0088 221 HIS Z CB    
8405  C  CG    . HIS F 221 ? 0.7689 0.3863 0.3772 -0.0184 0.2174 -0.0063 221 HIS Z CG    
8406  N  ND1   . HIS F 221 ? 0.7947 0.4172 0.4104 -0.0171 0.2178 -0.0057 221 HIS Z ND1   
8407  C  CD2   . HIS F 221 ? 0.7881 0.4031 0.3977 -0.0166 0.2185 -0.0041 221 HIS Z CD2   
8408  C  CE1   . HIS F 221 ? 0.8007 0.4241 0.4221 -0.015  0.2189 -0.0031 221 HIS Z CE1   
8409  N  NE2   . HIS F 221 ? 0.8014 0.4208 0.4197 -0.0145 0.2194 -0.002  221 HIS Z NE2   
8410  N  N     . ARG F 222 ? 0.6797 0.3074 0.2868 -0.029  0.2086 -0.0118 222 ARG Z N     
8411  C  CA    . ARG F 222 ? 0.6709 0.2994 0.2792 -0.0307 0.2068 -0.0118 222 ARG Z CA    
8412  C  C     . ARG F 222 ? 0.6597 0.2937 0.2761 -0.0304 0.2058 -0.0112 222 ARG Z C     
8413  O  O     . ARG F 222 ? 0.6604 0.2974 0.2805 -0.0295 0.2063 -0.0111 222 ARG Z O     
8414  C  CB    . ARG F 222 ? 0.6825 0.3116 0.2859 -0.0343 0.2047 -0.0138 222 ARG Z CB    
8415  C  CG    . ARG F 222 ? 0.7166 0.3397 0.3113 -0.0354 0.2054 -0.0144 222 ARG Z CG    
8416  C  CD    . ARG F 222 ? 0.7581 0.3827 0.3484 -0.0394 0.2033 -0.0162 222 ARG Z CD    
8417  N  NE    . ARG F 222 ? 0.8018 0.4194 0.383  -0.041  0.2038 -0.0167 222 ARG Z NE    
8418  C  CZ    . ARG F 222 ? 0.8283 0.446  0.4038 -0.0446 0.2025 -0.0181 222 ARG Z CZ    
8419  N  NH1   . ARG F 222 ? 0.8125 0.4376 0.3909 -0.0464 0.2007 -0.0189 222 ARG Z NH1   
8420  N  NH2   . ARG F 222 ? 0.8377 0.448  0.4043 -0.0463 0.203  -0.0184 222 ARG Z NH2   
8421  N  N     . ASP F 223 ? 0.6495 0.2843 0.2682 -0.0313 0.2043 -0.0107 223 ASP Z N     
8422  C  CA    . ASP F 223 ? 0.6433 0.2827 0.2687 -0.0317 0.2029 -0.0101 223 ASP Z CA    
8423  C  C     . ASP F 223 ? 0.6414 0.2841 0.2666 -0.0338 0.2014 -0.0121 223 ASP Z C     
8424  O  O     . ASP F 223 ? 0.6435 0.2862 0.265  -0.036  0.1999 -0.0135 223 ASP Z O     
8425  C  CB    . ASP F 223 ? 0.6568 0.2962 0.284  -0.0323 0.2015 -0.009  223 ASP Z CB    
8426  C  CG    . ASP F 223 ? 0.7031 0.3468 0.3366 -0.0332 0.1997 -0.0084 223 ASP Z CG    
8427  O  OD1   . ASP F 223 ? 0.7095 0.3553 0.3474 -0.0322 0.2005 -0.0076 223 ASP Z OD1   
8428  O  OD2   . ASP F 223 ? 0.7313 0.3758 0.3648 -0.0351 0.1975 -0.0089 223 ASP Z OD2   
8429  N  N     . THR F 224 ? 0.6358 0.2812 0.2646 -0.033  0.2019 -0.012  224 THR Z N     
8430  C  CA    . THR F 224 ? 0.6367 0.2849 0.2651 -0.0343 0.201  -0.0134 224 THR Z CA    
8431  C  C     . THR F 224 ? 0.6357 0.2857 0.2677 -0.0356 0.1994 -0.0133 224 THR Z C     
8432  O  O     . THR F 224 ? 0.6335 0.2851 0.2649 -0.0363 0.1991 -0.0142 224 THR Z O     
8433  C  CB    . THR F 224 ? 0.6487 0.2979 0.2773 -0.0326 0.203  -0.0135 224 THR Z CB    
8434  O  OG1   . THR F 224 ? 0.6593 0.308  0.2924 -0.0305 0.2045 -0.012  224 THR Z OG1   
8435  C  CG2   . THR F 224 ? 0.6526 0.3005 0.2763 -0.0321 0.204  -0.0141 224 THR Z CG2   
8436  N  N     . SER F 225 ? 0.6355 0.2851 0.2706 -0.0359 0.1984 -0.012  225 SER Z N     
8437  C  CA    . SER F 225 ? 0.6414 0.2924 0.2796 -0.0375 0.1965 -0.0117 225 SER Z CA    
8438  C  C     . SER F 225 ? 0.6494 0.3004 0.2842 -0.0397 0.1948 -0.0134 225 SER Z C     
8439  O  O     . SER F 225 ? 0.6467 0.2981 0.2819 -0.0406 0.1942 -0.0138 225 SER Z O     
8440  C  CB    . SER F 225 ? 0.6579 0.309  0.2995 -0.0377 0.1954 -0.0098 225 SER Z CB    
8441  O  OG    . SER F 225 ? 0.6868 0.3384 0.3325 -0.0355 0.1972 -0.0077 225 SER Z OG    
8442  N  N     . ASN F 226 ? 0.6597 0.3098 0.2904 -0.0404 0.1942 -0.0143 226 ASN Z N     
8443  C  CA    . ASN F 226 ? 0.6751 0.3255 0.3026 -0.0423 0.1928 -0.0157 226 ASN Z CA    
8444  C  C     . ASN F 226 ? 0.6775 0.3294 0.3029 -0.0419 0.1939 -0.0167 226 ASN Z C     
8445  O  O     . ASN F 226 ? 0.6779 0.33   0.3024 -0.0427 0.1933 -0.0172 226 ASN Z O     
8446  C  CB    . ASN F 226 ? 0.7018 0.3509 0.3255 -0.0433 0.1921 -0.0163 226 ASN Z CB    
8447  C  CG    . ASN F 226 ? 0.7535 0.4009 0.3784 -0.0436 0.1909 -0.0153 226 ASN Z CG    
8448  O  OD1   . ASN F 226 ? 0.7738 0.4217 0.4024 -0.0436 0.1899 -0.0142 226 ASN Z OD1   
8449  N  ND2   . ASN F 226 ? 0.7613 0.4066 0.3828 -0.0439 0.1911 -0.0155 226 ASN Z ND2   
8450  N  N     . ILE F 227 ? 0.6762 0.329  0.3006 -0.0406 0.1956 -0.0168 227 ILE Z N     
8451  C  CA    . ILE F 227 ? 0.6791 0.3341 0.3017 -0.0398 0.1968 -0.0173 227 ILE Z CA    
8452  C  C     . ILE F 227 ? 0.6782 0.3331 0.3033 -0.0386 0.1978 -0.0169 227 ILE Z C     
8453  O  O     . ILE F 227 ? 0.6846 0.3403 0.308  -0.0384 0.1983 -0.0173 227 ILE Z O     
8454  C  CB    . ILE F 227 ? 0.6876 0.3436 0.3085 -0.0388 0.1982 -0.0173 227 ILE Z CB    
8455  C  CG1   . ILE F 227 ? 0.7046 0.3593 0.3224 -0.0403 0.1973 -0.0177 227 ILE Z CG1   
8456  C  CG2   . ILE F 227 ? 0.6915 0.3509 0.3105 -0.0381 0.1992 -0.0176 227 ILE Z CG2   
8457  C  CD1   . ILE F 227 ? 0.7249 0.3791 0.3402 -0.0397 0.1985 -0.0176 227 ILE Z CD1   
8458  N  N     . GLU F 228 ? 0.6695 0.3232 0.2983 -0.0378 0.1983 -0.016  228 GLU Z N     
8459  C  CA    . GLU F 228 ? 0.6684 0.3214 0.2994 -0.0371 0.1992 -0.0155 228 GLU Z CA    
8460  C  C     . GLU F 228 ? 0.6672 0.3189 0.2974 -0.039  0.1976 -0.0159 228 GLU Z C     
8461  O  O     . GLU F 228 ? 0.6708 0.3215 0.2991 -0.0387 0.1985 -0.0162 228 GLU Z O     
8462  C  CB    . GLU F 228 ? 0.6921 0.3445 0.3278 -0.0363 0.1997 -0.0141 228 GLU Z CB    
8463  C  CG    . GLU F 228 ? 0.7365 0.3894 0.3726 -0.0339 0.202  -0.0137 228 GLU Z CG    
8464  C  CD    . GLU F 228 ? 0.7942 0.4465 0.4347 -0.0328 0.2029 -0.0119 228 GLU Z CD    
8465  O  OE1   . GLU F 228 ? 0.8086 0.461  0.4528 -0.0334 0.2025 -0.011  228 GLU Z OE1   
8466  O  OE2   . GLU F 228 ? 0.8128 0.4644 0.4529 -0.0312 0.204  -0.0114 228 GLU Z OE2   
8467  N  N     . GLN F 229 ? 0.6612 0.3122 0.2916 -0.041  0.1953 -0.0158 229 GLN Z N     
8468  C  CA    . GLN F 229 ? 0.6609 0.3099 0.2896 -0.0429 0.1935 -0.0162 229 GLN Z CA    
8469  C  C     . GLN F 229 ? 0.653  0.3018 0.2768 -0.0428 0.194  -0.0173 229 GLN Z C     
8470  O  O     . GLN F 229 ? 0.6512 0.2975 0.2725 -0.0434 0.194  -0.0176 229 GLN Z O     
8471  C  CB    . GLN F 229 ? 0.6831 0.3318 0.3131 -0.0448 0.191  -0.0158 229 GLN Z CB    
8472  C  CG    . GLN F 229 ? 0.7276 0.3756 0.3612 -0.0462 0.1895 -0.0146 229 GLN Z CG    
8473  C  CD    . GLN F 229 ? 0.7803 0.4302 0.418  -0.0459 0.1887 -0.0131 229 GLN Z CD    
8474  O  OE1   . GLN F 229 ? 0.7965 0.4465 0.4328 -0.0458 0.1881 -0.0134 229 GLN Z OE1   
8475  N  NE2   . GLN F 229 ? 0.7862 0.4373 0.4288 -0.0457 0.1889 -0.0114 229 GLN Z NE2   
8476  N  N     . LEU F 230 ? 0.6476 0.2986 0.2695 -0.0421 0.1946 -0.0177 230 LEU Z N     
8477  C  CA    . LEU F 230 ? 0.6509 0.303  0.2688 -0.0418 0.1953 -0.0183 230 LEU Z CA    
8478  C  C     . LEU F 230 ? 0.6489 0.3012 0.2657 -0.0397 0.1977 -0.018  230 LEU Z C     
8479  O  O     . LEU F 230 ? 0.6524 0.3032 0.2659 -0.0393 0.1984 -0.0181 230 LEU Z O     
8480  C  CB    . LEU F 230 ? 0.6559 0.3111 0.2726 -0.0419 0.1952 -0.0185 230 LEU Z CB    
8481  C  CG    . LEU F 230 ? 0.6784 0.3329 0.2945 -0.044  0.1931 -0.0189 230 LEU Z CG    
8482  C  CD1   . LEU F 230 ? 0.6851 0.3422 0.2993 -0.0445 0.1933 -0.0191 230 LEU Z CD1   
8483  C  CD2   . LEU F 230 ? 0.6903 0.3428 0.304  -0.0453 0.1918 -0.0192 230 LEU Z CD2   
8484  N  N     . LEU F 231 ? 0.6413 0.2949 0.2605 -0.0381 0.1992 -0.0176 231 LEU Z N     
8485  C  CA    . LEU F 231 ? 0.6451 0.2988 0.2633 -0.0358 0.2018 -0.0173 231 LEU Z CA    
8486  C  C     . LEU F 231 ? 0.6432 0.2925 0.261  -0.036  0.2023 -0.0172 231 LEU Z C     
8487  O  O     . LEU F 231 ? 0.6471 0.2949 0.2616 -0.0345 0.2042 -0.017  231 LEU Z O     
8488  C  CB    . LEU F 231 ? 0.6483 0.3043 0.2689 -0.034  0.2032 -0.0169 231 LEU Z CB    
8489  C  CG    . LEU F 231 ? 0.6659 0.3259 0.2853 -0.0337 0.2032 -0.0169 231 LEU Z CG    
8490  C  CD1   . LEU F 231 ? 0.6691 0.3298 0.2904 -0.0326 0.204  -0.0166 231 LEU Z CD1   
8491  C  CD2   . LEU F 231 ? 0.6769 0.3401 0.2934 -0.0322 0.2046 -0.0166 231 LEU Z CD2   
8492  N  N     . ILE F 232 ? 0.6341 0.2812 0.2548 -0.038  0.2005 -0.017  232 ILE Z N     
8493  C  CA    . ILE F 232 ? 0.6321 0.2749 0.2522 -0.0392 0.2004 -0.0169 232 ILE Z CA    
8494  C  C     . ILE F 232 ? 0.6329 0.2723 0.2477 -0.0405 0.1995 -0.0175 232 ILE Z C     
8495  O  O     . ILE F 232 ? 0.6364 0.2717 0.2474 -0.0402 0.201  -0.0176 232 ILE Z O     
8496  C  CB    . ILE F 232 ? 0.6352 0.2777 0.2602 -0.0414 0.1983 -0.0162 232 ILE Z CB    
8497  C  CG1   . ILE F 232 ? 0.6474 0.2925 0.2772 -0.0397 0.1996 -0.0154 232 ILE Z CG1   
8498  C  CG2   . ILE F 232 ? 0.6412 0.2794 0.2651 -0.0438 0.1973 -0.0161 232 ILE Z CG2   
8499  C  CD1   . ILE F 232 ? 0.6678 0.3116 0.297  -0.0378 0.2025 -0.0152 232 ILE Z CD1   
8500  N  N     . ASN F 233 ? 0.6271 0.2678 0.2413 -0.0417 0.1976 -0.0179 233 ASN Z N     
8501  C  CA    . ASN F 233 ? 0.628  0.2655 0.237  -0.0426 0.1969 -0.0183 233 ASN Z CA    
8502  C  C     . ASN F 233 ? 0.6192 0.2564 0.2234 -0.04   0.1997 -0.0182 233 ASN Z C     
8503  O  O     . ASN F 233 ? 0.6245 0.2568 0.2235 -0.0401 0.2004 -0.0183 233 ASN Z O     
8504  C  CB    . ASN F 233 ? 0.6455 0.2846 0.2549 -0.0442 0.1945 -0.0187 233 ASN Z CB    
8505  C  CG    . ASN F 233 ? 0.692  0.3299 0.3044 -0.0468 0.1915 -0.0186 233 ASN Z CG    
8506  O  OD1   . ASN F 233 ? 0.7047 0.3402 0.3185 -0.0481 0.1909 -0.0182 233 ASN Z OD1   
8507  N  ND2   . ASN F 233 ? 0.7058 0.3454 0.3191 -0.0478 0.1897 -0.0187 233 ASN Z ND2   
8508  N  N     . LYS F 234 ? 0.604  0.2463 0.2097 -0.0377 0.2015 -0.0178 234 LYS Z N     
8509  C  CA    . LYS F 234 ? 0.5991 0.2424 0.2009 -0.0348 0.2044 -0.0172 234 LYS Z CA    
8510  C  C     . LYS F 234 ? 0.6015 0.2408 0.201  -0.033  0.207  -0.0169 234 LYS Z C     
8511  O  O     . LYS F 234 ? 0.6079 0.2442 0.202  -0.0312 0.2093 -0.0164 234 LYS Z O     
8512  C  CB    . LYS F 234 ? 0.6069 0.2573 0.2109 -0.0332 0.2052 -0.0167 234 LYS Z CB    
8513  C  CG    . LYS F 234 ? 0.6352 0.2888 0.2399 -0.035  0.203  -0.0169 234 LYS Z CG    
8514  C  CD    . LYS F 234 ? 0.6698 0.33   0.276  -0.0341 0.2035 -0.0163 234 LYS Z CD    
8515  C  CE    . LYS F 234 ? 0.7079 0.3706 0.3142 -0.0363 0.2014 -0.0166 234 LYS Z CE    
8516  N  NZ    . LYS F 234 ? 0.7321 0.4014 0.3386 -0.0358 0.202  -0.0158 234 LYS Z NZ    
8517  N  N     . ASN F 235 ? 0.5955 0.2341 0.1987 -0.0335 0.2069 -0.017  235 ASN Z N     
8518  C  CA    . ASN F 235 ? 0.5984 0.2326 0.1996 -0.0324 0.2093 -0.0168 235 ASN Z CA    
8519  C  C     . ASN F 235 ? 0.6008 0.2272 0.197  -0.0346 0.2086 -0.0172 235 ASN Z C     
8520  O  O     . ASN F 235 ? 0.606  0.2274 0.1967 -0.0331 0.2112 -0.0169 235 ASN Z O     
8521  C  CB    . ASN F 235 ? 0.6063 0.2417 0.2132 -0.0329 0.2089 -0.0167 235 ASN Z CB    
8522  C  CG    . ASN F 235 ? 0.6346 0.267  0.2403 -0.0311 0.2118 -0.0163 235 ASN Z CG    
8523  O  OD1   . ASN F 235 ? 0.6471 0.2742 0.2471 -0.0304 0.2138 -0.0163 235 ASN Z OD1   
8524  N  ND2   . ASN F 235 ? 0.6413 0.2764 0.2517 -0.0303 0.2124 -0.016  235 ASN Z ND2   
8525  N  N     . LEU F 236 ? 0.5958 0.221  0.1935 -0.038  0.2052 -0.0177 236 LEU Z N     
8526  C  CA    . LEU F 236 ? 0.6011 0.2191 0.1939 -0.0408 0.2038 -0.0181 236 LEU Z CA    
8527  C  C     . LEU F 236 ? 0.6113 0.2258 0.1966 -0.0393 0.2052 -0.0181 236 LEU Z C     
8528  O  O     . LEU F 236 ? 0.6208 0.2276 0.1992 -0.0397 0.2064 -0.0182 236 LEU Z O     
8529  C  CB    . LEU F 236 ? 0.5973 0.2163 0.1941 -0.0445 0.1997 -0.0184 236 LEU Z CB    
8530  C  CG    . LEU F 236 ? 0.616  0.2279 0.2086 -0.048  0.1977 -0.0187 236 LEU Z CG    
8531  C  CD1   . LEU F 236 ? 0.6255 0.2336 0.2181 -0.0493 0.1985 -0.0184 236 LEU Z CD1   
8532  C  CD2   . LEU F 236 ? 0.6197 0.2336 0.216  -0.0512 0.1936 -0.0187 236 LEU Z CD2   
8533  N  N     . LYS F 237 ? 0.6057 0.2258 0.1922 -0.0377 0.2053 -0.0179 237 LYS Z N     
8534  C  CA    . LYS F 237 ? 0.6105 0.2288 0.1908 -0.0358 0.2069 -0.0175 237 LYS Z CA    
8535  C  C     . LYS F 237 ? 0.6092 0.2253 0.1846 -0.032  0.2113 -0.0165 237 LYS Z C     
8536  O  O     . LYS F 237 ? 0.6183 0.2286 0.1862 -0.0307 0.2132 -0.016  237 LYS Z O     
8537  C  CB    . LYS F 237 ? 0.6347 0.2606 0.2183 -0.0351 0.206  -0.0171 237 LYS Z CB    
8538  C  CG    . LYS F 237 ? 0.693  0.3182 0.2772 -0.0383 0.2026 -0.0179 237 LYS Z CG    
8539  C  CD    . LYS F 237 ? 0.7402 0.3725 0.3272 -0.0378 0.2019 -0.0176 237 LYS Z CD    
8540  C  CE    . LYS F 237 ? 0.7767 0.416  0.37   -0.0375 0.2016 -0.0175 237 LYS Z CE    
8541  N  NZ    . LYS F 237 ? 0.7975 0.4415 0.3934 -0.0389 0.1996 -0.0178 237 LYS Z NZ    
8542  N  N     . MET F 238 ? 0.596  0.2159 0.1748 -0.03   0.2131 -0.016  238 MET Z N     
8543  C  CA    . MET F 238 ? 0.5984 0.2159 0.1725 -0.0261 0.2174 -0.015  238 MET Z CA    
8544  C  C     . MET F 238 ? 0.6097 0.2166 0.1775 -0.0272 0.2185 -0.0155 238 MET Z C     
8545  O  O     . MET F 238 ? 0.6175 0.2185 0.1775 -0.0247 0.2219 -0.0147 238 MET Z O     
8546  C  CB    . MET F 238 ? 0.5972 0.2213 0.1765 -0.0237 0.2189 -0.0145 238 MET Z CB    
8547  C  CG    . MET F 238 ? 0.6129 0.2347 0.1874 -0.0195 0.2235 -0.0133 238 MET Z CG    
8548  S  SD    . MET F 238 ? 0.6311 0.2551 0.1999 -0.0152 0.2266 -0.0112 238 MET Z SD    
8549  C  CE    . MET F 238 ? 0.6009 0.2382 0.1774 -0.014  0.2256 -0.0103 238 MET Z CE    
8550  N  N     . VAL F 239 ? 0.61   0.2142 0.1808 -0.0312 0.2158 -0.0166 239 VAL Z N     
8551  C  CA    . VAL F 239 ? 0.6247 0.2187 0.1896 -0.0335 0.2161 -0.0171 239 VAL Z CA    
8552  C  C     . VAL F 239 ? 0.6433 0.2295 0.1997 -0.0347 0.2158 -0.0173 239 VAL Z C     
8553  O  O     . VAL F 239 ? 0.6519 0.2288 0.1993 -0.0339 0.2184 -0.0172 239 VAL Z O     
8554  C  CB    . VAL F 239 ? 0.6303 0.2249 0.2014 -0.038  0.2126 -0.0178 239 VAL Z CB    
8555  C  CG1   . VAL F 239 ? 0.6423 0.2267 0.2072 -0.0414 0.2122 -0.0183 239 VAL Z CG1   
8556  C  CG2   . VAL F 239 ? 0.6332 0.234  0.2116 -0.0364 0.2136 -0.0174 239 VAL Z CG2   
8557  N  N     . GLU F 240 ? 0.6461 0.2358 0.2046 -0.0361 0.2129 -0.0176 240 GLU Z N     
8558  C  CA    . GLU F 240 ? 0.6597 0.2429 0.2106 -0.0369 0.2124 -0.0178 240 GLU Z CA    
8559  C  C     . GLU F 240 ? 0.6652 0.2458 0.2087 -0.032  0.2171 -0.0165 240 GLU Z C     
8560  O  O     . GLU F 240 ? 0.6734 0.2438 0.2071 -0.0316 0.2191 -0.0164 240 GLU Z O     
8561  C  CB    . GLU F 240 ? 0.6915 0.2804 0.2473 -0.0388 0.2087 -0.0182 240 GLU Z CB    
8562  C  CG    . GLU F 240 ? 0.7736 0.3549 0.3222 -0.041  0.2071 -0.0186 240 GLU Z CG    
8563  C  CD    . GLU F 240 ? 0.878  0.4612 0.4238 -0.0382 0.2084 -0.0179 240 GLU Z CD    
8564  O  OE1   . GLU F 240 ? 0.8973 0.4827 0.4411 -0.0338 0.2124 -0.0166 240 GLU Z OE1   
8565  O  OE2   . GLU F 240 ? 0.9162 0.4989 0.4617 -0.0404 0.2056 -0.0184 240 GLU Z OE2   
8566  N  N     . PHE F 241 ? 0.6604 0.2503 0.2084 -0.0281 0.219  -0.0153 241 PHE Z N     
8567  C  CA    . PHE F 241 ? 0.6707 0.2603 0.213  -0.023  0.2236 -0.0135 241 PHE Z CA    
8568  C  C     . PHE F 241 ? 0.6856 0.2665 0.22   -0.0205 0.2278 -0.0129 241 PHE Z C     
8569  O  O     . PHE F 241 ? 0.6942 0.2674 0.219  -0.018  0.231  -0.0119 241 PHE Z O     
8570  C  CB    . PHE F 241 ? 0.6626 0.2649 0.2123 -0.0199 0.2245 -0.0121 241 PHE Z CB    
8571  C  CG    . PHE F 241 ? 0.6712 0.2748 0.216  -0.0142 0.2294 -0.0097 241 PHE Z CG    
8572  C  CD1   . PHE F 241 ? 0.6844 0.2859 0.2234 -0.0121 0.2311 -0.0083 241 PHE Z CD1   
8573  C  CD2   . PHE F 241 ? 0.6784 0.285  0.2242 -0.0107 0.2325 -0.0086 241 PHE Z CD2   
8574  C  CE1   . PHE F 241 ? 0.6939 0.2971 0.2287 -0.0065 0.236  -0.0056 241 PHE Z CE1   
8575  C  CE2   . PHE F 241 ? 0.6893 0.2973 0.2306 -0.0052 0.2373 -0.006  241 PHE Z CE2   
8576  C  CZ    . PHE F 241 ? 0.6894 0.2959 0.2253 -0.0031 0.239  -0.0044 241 PHE Z CZ    
8577  N  N     . LEU F 242 ? 0.6896 0.2713 0.2276 -0.0209 0.2281 -0.0134 242 LEU Z N     
8578  C  CA    . LEU F 242 ? 0.7059 0.2797 0.2368 -0.0186 0.2323 -0.0129 242 LEU Z CA    
8579  C  C     . LEU F 242 ? 0.7272 0.2868 0.2486 -0.0219 0.2321 -0.014  242 LEU Z C     
8580  O  O     . LEU F 242 ? 0.7354 0.2855 0.2462 -0.0192 0.2363 -0.0132 242 LEU Z O     
8581  C  CB    . LEU F 242 ? 0.702  0.281  0.2399 -0.0182 0.2326 -0.0131 242 LEU Z CB    
8582  C  CG    . LEU F 242 ? 0.7082 0.3    0.254  -0.0148 0.2333 -0.0119 242 LEU Z CG    
8583  C  CD1   . LEU F 242 ? 0.7131 0.309  0.2657 -0.0153 0.2328 -0.0125 242 LEU Z CD1   
8584  C  CD2   . LEU F 242 ? 0.715  0.3079 0.2555 -0.0087 0.2382 -0.0097 242 LEU Z CD2   
8585  N  N     . SER F 243 ? 0.7342 0.2921 0.2587 -0.0278 0.2273 -0.0157 243 SER Z N     
8586  C  CA    . SER F 243 ? 0.7549 0.2998 0.2707 -0.0319 0.2264 -0.0167 243 SER Z CA    
8587  C  C     . SER F 243 ? 0.773  0.3095 0.2785 -0.0315 0.2271 -0.0165 243 SER Z C     
8588  O  O     . SER F 243 ? 0.788  0.3113 0.2818 -0.0321 0.2293 -0.0166 243 SER Z O     
8589  C  CB    . SER F 243 ? 0.7696 0.3164 0.2923 -0.0382 0.221  -0.0181 243 SER Z CB    
8590  O  OG    . SER F 243 ? 0.7908 0.3454 0.3205 -0.04   0.2169 -0.0184 243 SER Z OG    
8591  N  N     . LYS F 244 ? 0.7715 0.3148 0.2806 -0.0304 0.2257 -0.0161 244 LYS Z N     
8592  C  CA    . LYS F 244 ? 0.7874 0.3233 0.287  -0.0295 0.2266 -0.0156 244 LYS Z CA    
8593  C  C     . LYS F 244 ? 0.802  0.3336 0.2928 -0.023  0.233  -0.0136 244 LYS Z C     
8594  O  O     . LYS F 244 ? 0.8126 0.3354 0.2933 -0.0216 0.2349 -0.0129 244 LYS Z O     
8595  C  CB    . LYS F 244 ? 0.8081 0.3522 0.3142 -0.0305 0.2231 -0.0158 244 LYS Z CB    
8596  C  CG    . LYS F 244 ? 0.8609 0.4062 0.3726 -0.0368 0.2171 -0.0176 244 LYS Z CG    
8597  C  CD    . LYS F 244 ? 0.92   0.473  0.4376 -0.0376 0.214  -0.0177 244 LYS Z CD    
8598  C  CE    . LYS F 244 ? 0.9818 0.5259 0.4906 -0.0392 0.2128 -0.0181 244 LYS Z CE    
8599  N  NZ    . LYS F 244 ? 1.0087 0.5601 0.5218 -0.0383 0.2113 -0.0177 244 LYS Z NZ    
8600  N  N     . ASN F 245 ? 0.8035 0.3409 0.2977 -0.0187 0.2365 -0.0123 245 ASN Z N     
8601  C  CA    . ASN F 245 ? 0.8166 0.3508 0.303  -0.0121 0.2428 -0.01   245 ASN Z CA    
8602  C  C     . ASN F 245 ? 0.8306 0.3518 0.3065 -0.0113 0.2468 -0.01   245 ASN Z C     
8603  O  O     . ASN F 245 ? 0.8381 0.3544 0.3056 -0.0056 0.2525 -0.0079 245 ASN Z O     
8604  C  CB    . ASN F 245 ? 0.8214 0.3703 0.3171 -0.0075 0.2445 -0.0081 245 ASN Z CB    
8605  C  CG    . ASN F 245 ? 0.8596 0.4162 0.3573 -0.0047 0.2449 -0.0063 245 ASN Z CG    
8606  O  OD1   . ASN F 245 ? 0.8831 0.4324 0.3725 -0.0038 0.2462 -0.0056 245 ASN Z OD1   
8607  N  ND2   . ASN F 245 ? 0.8584 0.4296 0.3667 -0.0032 0.2439 -0.0054 245 ASN Z ND2   
8608  N  N     . THR F 246 ? 0.8321 0.3479 0.3085 -0.0166 0.244  -0.0121 246 THR Z N     
8609  C  CA    . THR F 246 ? 0.8456 0.3486 0.3119 -0.0165 0.2475 -0.0123 246 THR Z CA    
8610  C  C     . THR F 246 ? 0.856  0.3425 0.3094 -0.0209 0.2466 -0.0136 246 THR Z C     
8611  O  O     . THR F 246 ? 0.858  0.3447 0.3134 -0.0257 0.2417 -0.0148 246 THR Z O     
8612  C  CB    . THR F 246 ? 0.8601 0.3675 0.3347 -0.0195 0.2456 -0.0135 246 THR Z CB    
8613  O  OG1   . THR F 246 ? 0.8692 0.3795 0.3509 -0.0265 0.2392 -0.0154 246 THR Z OG1   
8614  C  CG2   . THR F 246 ? 0.8593 0.3811 0.3448 -0.015  0.247  -0.0123 246 THR Z CG2   
8615  N  N     . LYS F 247 ? 0.8608 0.3326 0.3005 -0.0195 0.2512 -0.0132 247 LYS Z N     
8616  C  CA    . LYS F 247 ? 0.8754 0.3296 0.3009 -0.024  0.2507 -0.0144 247 LYS Z CA    
8617  C  C     . LYS F 247 ? 0.8771 0.3315 0.3084 -0.0325 0.2445 -0.0167 247 LYS Z C     
8618  O  O     . LYS F 247 ? 0.8758 0.3333 0.3126 -0.0339 0.2444 -0.0172 247 LYS Z O     
8619  C  CB    . LYS F 247 ? 0.9049 0.3433 0.3146 -0.0208 0.2573 -0.0136 247 LYS Z CB    
8620  C  CG    . LYS F 247 ? 0.9468 0.3878 0.3534 -0.0113 0.2643 -0.0107 247 LYS Z CG    
8621  C  CD    . LYS F 247 ? 0.9959 0.4323 0.3981 -0.0078 0.2697 -0.0099 247 LYS Z CD    
8622  C  CE    . LYS F 247 ? 1.0366 0.4654 0.4372 -0.0141 0.2677 -0.0121 247 LYS Z CE    
8623  N  NZ    . LYS F 247 ? 1.0439 0.4881 0.4616 -0.0162 0.264  -0.0129 247 LYS Z NZ    
8624  N  N     . ASN F 248 ? 0.8786 0.3303 0.309  -0.038  0.2395 -0.018  248 ASN Z N     
8625  C  CA    . ASN F 248 ? 0.8819 0.3353 0.3185 -0.0462 0.2331 -0.0197 248 ASN Z CA    
8626  C  C     . ASN F 248 ? 0.8957 0.3353 0.3228 -0.0511 0.2335 -0.0206 248 ASN Z C     
8627  O  O     . ASN F 248 ? 0.8915 0.3354 0.3263 -0.057  0.2291 -0.0215 248 ASN Z O     
8628  C  CB    . ASN F 248 ? 0.8931 0.3467 0.3301 -0.0503 0.2278 -0.0205 248 ASN Z CB    
8629  C  CG    . ASN F 248 ? 0.9312 0.3723 0.3594 -0.0583 0.2237 -0.022  248 ASN Z CG    
8630  O  OD1   . ASN F 248 ? 0.95   0.3746 0.3619 -0.0589 0.2261 -0.0222 248 ASN Z OD1   
8631  N  ND2   . ASN F 248 ? 0.933  0.3818 0.3716 -0.0645 0.2177 -0.0228 248 ASN Z ND2   
8632  N  N     . ASP F 249 ? 0.9101 0.3334 0.3204 -0.049  0.2387 -0.0203 249 ASP Z N     
8633  C  CA    . ASP F 249 ? 0.9276 0.3362 0.3271 -0.0542 0.2392 -0.0212 249 ASP Z CA    
8634  C  C     . ASP F 249 ? 0.9227 0.3361 0.3291 -0.0541 0.2408 -0.0211 249 ASP Z C     
8635  O  O     . ASP F 249 ? 0.9244 0.3304 0.3273 -0.0604 0.239  -0.0221 249 ASP Z O     
8636  C  CB    . ASP F 249 ? 0.9719 0.3601 0.35   -0.0518 0.2447 -0.0209 249 ASP Z CB    
8637  C  CG    . ASP F 249 ? 1.0372 0.4257 0.4111 -0.0417 0.2521 -0.0188 249 ASP Z CG    
8638  O  OD1   . ASP F 249 ? 1.0435 0.4394 0.4238 -0.0372 0.2555 -0.0178 249 ASP Z OD1   
8639  O  OD2   . ASP F 249 ? 1.067  0.4483 0.4309 -0.0382 0.2545 -0.0179 249 ASP Z OD2   
8640  N  N     . ASN F 250 ? 0.9167 0.3422 0.3326 -0.0472 0.244  -0.0199 250 ASN Z N     
8641  C  CA    . ASN F 250 ? 0.9198 0.3505 0.3427 -0.0463 0.2459 -0.0197 250 ASN Z CA    
8642  C  C     . ASN F 250 ? 0.9046 0.3555 0.3475 -0.0458 0.2423 -0.0195 250 ASN Z C     
8643  O  O     . ASN F 250 ? 0.9054 0.3616 0.355  -0.0449 0.2436 -0.0193 250 ASN Z O     
8644  C  CB    . ASN F 250 ? 0.9468 0.3724 0.3616 -0.0382 0.2538 -0.0182 250 ASN Z CB    
8645  C  CG    . ASN F 250 ? 1.0157 0.421  0.412  -0.039  0.2583 -0.0184 250 ASN Z CG    
8646  O  OD1   . ASN F 250 ? 1.038  0.4395 0.4316 -0.0371 0.2624 -0.018  250 ASN Z OD1   
8647  N  ND2   . ASN F 250 ? 1.0377 0.4287 0.42   -0.0419 0.258  -0.0189 250 ASN Z ND2   
8648  N  N     . ASN F 251 ? 0.8892 0.3508 0.3408 -0.046  0.2383 -0.0195 251 ASN Z N     
8649  C  CA    . ASN F 251 ? 0.8748 0.3544 0.3441 -0.0454 0.2351 -0.0193 251 ASN Z CA    
8650  C  C     . ASN F 251 ? 0.8708 0.3562 0.3476 -0.0514 0.2281 -0.0202 251 ASN Z C     
8651  O  O     . ASN F 251 ? 0.8795 0.3567 0.3481 -0.0544 0.2262 -0.0208 251 ASN Z O     
8652  C  CB    . ASN F 251 ? 0.8776 0.3669 0.3512 -0.0377 0.2381 -0.018  251 ASN Z CB    
8653  C  CG    . ASN F 251 ? 0.9121 0.3969 0.3782 -0.0308 0.2451 -0.0167 251 ASN Z CG    
8654  O  OD1   . ASN F 251 ? 0.9333 0.4079 0.3867 -0.0276 0.2491 -0.0159 251 ASN Z OD1   
8655  N  ND2   . ASN F 251 ? 0.9139 0.4063 0.3875 -0.0281 0.2469 -0.0162 251 ASN Z ND2   
8656  N  N     . PHE F 252 ? 0.8563 0.3556 0.3482 -0.0527 0.2246 -0.0202 252 PHE Z N     
8657  C  CA    . PHE F 252 ? 0.852  0.3581 0.3518 -0.0576 0.2184 -0.0207 252 PHE Z CA    
8658  C  C     . PHE F 252 ? 0.8505 0.3599 0.3497 -0.0547 0.2178 -0.0206 252 PHE Z C     
8659  O  O     . PHE F 252 ? 0.8482 0.3626 0.3487 -0.0486 0.2212 -0.0198 252 PHE Z O     
8660  C  CB    . PHE F 252 ? 0.8396 0.3602 0.3554 -0.0582 0.2157 -0.0203 252 PHE Z CB    
8661  C  CG    . PHE F 252 ? 0.8429 0.3634 0.3632 -0.0636 0.2134 -0.0202 252 PHE Z CG    
8662  C  CD1   . PHE F 252 ? 0.8591 0.3669 0.3692 -0.068  0.2138 -0.0206 252 PHE Z CD1   
8663  C  CD2   . PHE F 252 ? 0.8411 0.3739 0.3754 -0.0643 0.211  -0.0196 252 PHE Z CD2   
8664  C  CE1   . PHE F 252 ? 0.8647 0.3732 0.3795 -0.0733 0.2116 -0.0203 252 PHE Z CE1   
8665  C  CE2   . PHE F 252 ? 0.8475 0.3809 0.3863 -0.069  0.2091 -0.0191 252 PHE Z CE2   
8666  C  CZ    . PHE F 252 ? 0.8519 0.3736 0.3813 -0.0735 0.2094 -0.0194 252 PHE Z CZ    
8667  N  N     . THR F 253 ? 0.8509 0.3576 0.3481 -0.0591 0.2135 -0.0212 253 THR Z N     
8668  C  CA    . THR F 253 ? 0.8568 0.3669 0.3541 -0.0568 0.2126 -0.0211 253 THR Z CA    
8669  C  C     . THR F 253 ? 0.8481 0.3737 0.3606 -0.0571 0.2088 -0.021  253 THR Z C     
8670  O  O     . THR F 253 ? 0.8479 0.3794 0.3692 -0.06   0.2064 -0.021  253 THR Z O     
8671  C  CB    . THR F 253 ? 0.8857 0.385  0.3728 -0.0611 0.2099 -0.0219 253 THR Z CB    
8672  O  OG1   . THR F 253 ? 0.9091 0.3929 0.3821 -0.0626 0.2126 -0.0222 253 THR Z OG1   
8673  C  CG2   . THR F 253 ? 0.8943 0.3941 0.3781 -0.0576 0.2106 -0.0216 253 THR Z CG2   
8674  N  N     . TYR F 254 ? 0.8406 0.3725 0.3561 -0.0542 0.2085 -0.0208 254 TYR Z N     
8675  C  CA    . TYR F 254 ? 0.8341 0.3794 0.3627 -0.0545 0.2051 -0.0207 254 TYR Z CA    
8676  C  C     . TYR F 254 ? 0.8355 0.3817 0.3683 -0.0607 0.1995 -0.0211 254 TYR Z C     
8677  O  O     . TYR F 254 ? 0.8312 0.3868 0.3749 -0.0619 0.1971 -0.0208 254 TYR Z O     
8678  C  CB    . TYR F 254 ? 0.8305 0.3818 0.3608 -0.0508 0.2057 -0.0203 254 TYR Z CB    
8679  C  CG    . TYR F 254 ? 0.831  0.395  0.374  -0.0512 0.2027 -0.0203 254 TYR Z CG    
8680  C  CD1   . TYR F 254 ? 0.8387 0.4108 0.3904 -0.0496 0.2036 -0.0199 254 TYR Z CD1   
8681  C  CD2   . TYR F 254 ? 0.8402 0.4071 0.3861 -0.0537 0.1987 -0.0207 254 TYR Z CD2   
8682  C  CE1   . TYR F 254 ? 0.8432 0.4256 0.4055 -0.0502 0.201  -0.0198 254 TYR Z CE1   
8683  C  CE2   . TYR F 254 ? 0.8461 0.4235 0.4028 -0.0542 0.1961 -0.0205 254 TYR Z CE2   
8684  C  CZ    . TYR F 254 ? 0.8536 0.4384 0.4182 -0.0524 0.1973 -0.0201 254 TYR Z CZ    
8685  O  OH    . TYR F 254 ? 0.8676 0.4616 0.4416 -0.0527 0.1951 -0.0199 254 TYR Z OH    
8686  N  N     . SER F 255 ? 0.8407 0.3769 0.3646 -0.0647 0.1974 -0.0217 255 SER Z N     
8687  C  CA    . SER F 255 ? 0.8444 0.3816 0.3718 -0.0709 0.1918 -0.0218 255 SER Z CA    
8688  C  C     . SER F 255 ? 0.8441 0.3841 0.3778 -0.0741 0.1906 -0.0213 255 SER Z C     
8689  O  O     . SER F 255 ? 0.8416 0.3895 0.3847 -0.0772 0.1867 -0.0207 255 SER Z O     
8690  C  CB    . SER F 255 ? 0.869  0.3937 0.3841 -0.0747 0.1901 -0.0225 255 SER Z CB    
8691  O  OG    . SER F 255 ? 0.9013 0.4237 0.4112 -0.0719 0.1908 -0.0228 255 SER Z OG    
8692  N  N     . GLU F 256 ? 0.8456 0.3794 0.3742 -0.0732 0.1944 -0.0213 256 GLU Z N     
8693  C  CA    . GLU F 256 ? 0.8473 0.3833 0.3813 -0.0759 0.1939 -0.0207 256 GLU Z CA    
8694  C  C     . GLU F 256 ? 0.8384 0.3879 0.386  -0.0725 0.1946 -0.0199 256 GLU Z C     
8695  O  O     . GLU F 256 ? 0.8344 0.3905 0.391  -0.0755 0.1917 -0.0191 256 GLU Z O     
8696  C  CB    . GLU F 256 ? 0.8816 0.4064 0.4053 -0.0754 0.1982 -0.0211 256 GLU Z CB    
8697  C  CG    . GLU F 256 ? 0.9495 0.4603 0.4603 -0.0806 0.1967 -0.0217 256 GLU Z CG    
8698  C  CD    . GLU F 256 ? 1.035  0.532  0.5322 -0.0793 0.2017 -0.0222 256 GLU Z CD    
8699  O  OE1   . GLU F 256 ? 1.056  0.5409 0.5427 -0.0845 0.2005 -0.0226 256 GLU Z OE1   
8700  O  OE2   . GLU F 256 ? 1.0625 0.5606 0.5592 -0.0731 0.2068 -0.0219 256 GLU Z OE2   
8701  N  N     . TRP F 257 ? 0.8334 0.3869 0.3822 -0.0664 0.1982 -0.02   257 TRP Z N     
8702  C  CA    . TRP F 257 ? 0.8285 0.3938 0.3888 -0.0632 0.1988 -0.0194 257 TRP Z CA    
8703  C  C     . TRP F 257 ? 0.8193 0.3937 0.3887 -0.0648 0.1945 -0.019  257 TRP Z C     
8704  O  O     . TRP F 257 ? 0.8158 0.3984 0.3951 -0.0649 0.1934 -0.0182 257 TRP Z O     
8705  C  CB    . TRP F 257 ? 0.8303 0.3978 0.389  -0.0568 0.2031 -0.0195 257 TRP Z CB    
8706  C  CG    . TRP F 257 ? 0.8427 0.4042 0.395  -0.0538 0.2081 -0.0194 257 TRP Z CG    
8707  C  CD1   . TRP F 257 ? 0.859  0.4137 0.4014 -0.0502 0.2119 -0.0194 257 TRP Z CD1   
8708  C  CD2   . TRP F 257 ? 0.8443 0.4065 0.3998 -0.0533 0.2101 -0.0189 257 TRP Z CD2   
8709  N  NE1   . TRP F 257 ? 0.8653 0.4162 0.4043 -0.0476 0.2162 -0.0191 257 TRP Z NE1   
8710  C  CE2   . TRP F 257 ? 0.8585 0.4137 0.4054 -0.0496 0.2151 -0.0189 257 TRP Z CE2   
8711  C  CE3   . TRP F 257 ? 0.8475 0.4153 0.4121 -0.0556 0.2083 -0.0184 257 TRP Z CE3   
8712  C  CZ2   . TRP F 257 ? 0.8671 0.4207 0.4141 -0.0482 0.2183 -0.0185 257 TRP Z CZ2   
8713  C  CZ3   . TRP F 257 ? 0.8579 0.424  0.4228 -0.0544 0.2114 -0.018  257 TRP Z CZ3   
8714  C  CH2   . TRP F 257 ? 0.8635 0.4226 0.4196 -0.0507 0.2163 -0.0182 257 TRP Z CH2   
8715  N  N     . GLU F 258 ? 0.8149 0.3873 0.3805 -0.0658 0.1923 -0.0195 258 GLU Z N     
8716  C  CA    . GLU F 258 ? 0.8115 0.3911 0.384  -0.0673 0.1883 -0.0192 258 GLU Z CA    
8717  C  C     . GLU F 258 ? 0.8094 0.391  0.387  -0.0725 0.1842 -0.0183 258 GLU Z C     
8718  O  O     . GLU F 258 ? 0.8044 0.3949 0.3917 -0.0726 0.1822 -0.0173 258 GLU Z O     
8719  C  CB    . GLU F 258 ? 0.8394 0.4147 0.4051 -0.0673 0.1872 -0.02   258 GLU Z CB    
8720  C  CG    . GLU F 258 ? 0.8876 0.47   0.4596 -0.068  0.1837 -0.0198 258 GLU Z CG    
8721  C  CD    . GLU F 258 ? 0.9654 0.543  0.5302 -0.0681 0.1827 -0.0206 258 GLU Z CD    
8722  O  OE1   . GLU F 258 ? 0.9849 0.553  0.5408 -0.0709 0.1819 -0.021  258 GLU Z OE1   
8723  O  OE2   . GLU F 258 ? 0.9873 0.5701 0.555  -0.0656 0.1829 -0.0207 258 GLU Z OE2   
8724  N  N     . SER F 259 ? 0.8122 0.3855 0.3833 -0.0768 0.1831 -0.0184 259 SER Z N     
8725  C  CA    . SER F 259 ? 0.8149 0.3902 0.3906 -0.0824 0.1791 -0.0172 259 SER Z CA    
8726  C  C     . SER F 259 ? 0.8131 0.3957 0.3986 -0.0819 0.18   -0.0157 259 SER Z C     
8727  O  O     . SER F 259 ? 0.8108 0.4001 0.4045 -0.0849 0.1768 -0.0141 259 SER Z O     
8728  C  CB    . SER F 259 ? 0.8366 0.4005 0.4018 -0.0875 0.1777 -0.0176 259 SER Z CB    
8729  O  OG    . SER F 259 ? 0.8661 0.4229 0.4256 -0.0872 0.1814 -0.018  259 SER Z OG    
8730  N  N     . ILE F 260 ? 0.8113 0.393  0.3961 -0.078  0.1846 -0.0162 260 ILE Z N     
8731  C  CA    . ILE F 260 ? 0.8078 0.3959 0.4013 -0.0767 0.1862 -0.0149 260 ILE Z CA    
8732  C  C     . ILE F 260 ? 0.8036 0.4022 0.4066 -0.0728 0.1861 -0.0143 260 ILE Z C     
8733  O  O     . ILE F 260 ? 0.803  0.4091 0.4153 -0.0736 0.1846 -0.0126 260 ILE Z O     
8734  C  CB    . ILE F 260 ? 0.8169 0.3993 0.4051 -0.0737 0.1912 -0.0156 260 ILE Z CB    
8735  C  CG1   . ILE F 260 ? 0.8316 0.4023 0.4093 -0.0776 0.1916 -0.0162 260 ILE Z CG1   
8736  C  CG2   . ILE F 260 ? 0.8199 0.4091 0.4171 -0.0717 0.1931 -0.0144 260 ILE Z CG2   
8737  C  CD1   . ILE F 260 ? 0.8497 0.4132 0.4197 -0.0739 0.1969 -0.0171 260 ILE Z CD1   
8738  N  N     . TYR F 261 ? 0.8008 0.3998 0.401  -0.0688 0.1876 -0.0155 261 TYR Z N     
8739  C  CA    . TYR F 261 ? 0.8004 0.4079 0.4077 -0.0654 0.1877 -0.0152 261 TYR Z CA    
8740  C  C     . TYR F 261 ? 0.8021 0.4154 0.4159 -0.0679 0.1835 -0.014  261 TYR Z C     
8741  O  O     . TYR F 261 ? 0.7978 0.4185 0.42   -0.0665 0.1834 -0.0127 261 TYR Z O     
8742  C  CB    . TYR F 261 ? 0.8018 0.4079 0.4037 -0.0618 0.1896 -0.0166 261 TYR Z CB    
8743  C  CG    . TYR F 261 ? 0.8047 0.4187 0.4127 -0.0589 0.1894 -0.0164 261 TYR Z CG    
8744  C  CD1   . TYR F 261 ? 0.8095 0.4284 0.4221 -0.0554 0.192  -0.0161 261 TYR Z CD1   
8745  C  CD2   . TYR F 261 ? 0.8137 0.4295 0.422  -0.0599 0.1867 -0.0166 261 TYR Z CD2   
8746  C  CE1   . TYR F 261 ? 0.8157 0.4408 0.4328 -0.0532 0.1918 -0.0159 261 TYR Z CE1   
8747  C  CE2   . TYR F 261 ? 0.8196 0.4417 0.4327 -0.0576 0.1866 -0.0164 261 TYR Z CE2   
8748  C  CZ    . TYR F 261 ? 0.8254 0.4519 0.4426 -0.0544 0.1891 -0.0161 261 TYR Z CZ    
8749  O  OH    . TYR F 261 ? 0.8376 0.4692 0.4582 -0.0524 0.1891 -0.0161 261 TYR Z OH    
8750  N  N     . ASN F 262 ? 0.8067 0.4166 0.4163 -0.0713 0.1803 -0.0143 262 ASN Z N     
8751  C  CA    . ASN F 262 ? 0.8123 0.4277 0.4276 -0.0734 0.1763 -0.013  262 ASN Z CA    
8752  C  C     . ASN F 262 ? 0.8152 0.4341 0.4367 -0.0774 0.1737 -0.0108 262 ASN Z C     
8753  O  O     . ASN F 262 ? 0.8176 0.441  0.4435 -0.0795 0.1702 -0.0093 262 ASN Z O     
8754  C  CB    . ASN F 262 ? 0.8311 0.4424 0.4401 -0.0751 0.1738 -0.014  262 ASN Z CB    
8755  C  CG    . ASN F 262 ? 0.8811 0.4831 0.4811 -0.0793 0.1724 -0.0147 262 ASN Z CG    
8756  O  OD1   . ASN F 262 ? 0.8996 0.4992 0.4993 -0.0825 0.1719 -0.014  262 ASN Z OD1   
8757  N  ND2   . ASN F 262 ? 0.8938 0.49   0.4858 -0.0793 0.1719 -0.0161 262 ASN Z ND2   
8758  N  N     . GLY F 263 ? 0.8124 0.4295 0.4343 -0.0783 0.1755 -0.0103 263 GLY Z N     
8759  C  CA    . GLY F 263 ? 0.8137 0.4347 0.442  -0.082  0.1734 -0.0079 263 GLY Z CA    
8760  C  C     . GLY F 263 ? 0.8209 0.4377 0.4451 -0.0884 0.1695 -0.0074 263 GLY Z C     
8761  O  O     . GLY F 263 ? 0.8174 0.4394 0.4482 -0.0919 0.1668 -0.0049 263 GLY Z O     
8762  N  N     . THR F 264 ? 0.8307 0.4381 0.4441 -0.09   0.169  -0.0095 264 THR Z N     
8763  C  CA    . THR F 264 ? 0.8447 0.4465 0.4525 -0.0965 0.1652 -0.0092 264 THR Z CA    
8764  C  C     . THR F 264 ? 0.8559 0.4535 0.4619 -0.1    0.1662 -0.0087 264 THR Z C     
8765  O  O     . THR F 264 ? 0.8568 0.4563 0.4655 -0.1056 0.1627 -0.0068 264 THR Z O     
8766  C  CB    . THR F 264 ? 0.8679 0.4597 0.4635 -0.097  0.1649 -0.0116 264 THR Z CB    
8767  O  OG1   . THR F 264 ? 0.8798 0.4757 0.4774 -0.0934 0.1645 -0.0121 264 THR Z OG1   
8768  C  CG2   . THR F 264 ? 0.8773 0.4632 0.4667 -0.1038 0.1605 -0.0113 264 THR Z CG2   
8769  N  N     . TYR F 265 ? 0.8612 0.4536 0.463  -0.0967 0.171  -0.0101 265 TYR Z N     
8770  C  CA    . TYR F 265 ? 0.8716 0.4592 0.471  -0.0994 0.1727 -0.0098 265 TYR Z CA    
8771  C  C     . TYR F 265 ? 0.8754 0.4662 0.4796 -0.094  0.1776 -0.0097 265 TYR Z C     
8772  O  O     . TYR F 265 ? 0.8742 0.4676 0.4795 -0.0882 0.1803 -0.0107 265 TYR Z O     
8773  C  CB    . TYR F 265 ? 0.8814 0.4543 0.4657 -0.1015 0.174  -0.0119 265 TYR Z CB    
8774  C  CG    . TYR F 265 ? 0.8936 0.4606 0.4702 -0.1061 0.1698 -0.0126 265 TYR Z CG    
8775  C  CD1   . TYR F 265 ? 0.904  0.4711 0.4812 -0.1134 0.165  -0.0111 265 TYR Z CD1   
8776  C  CD2   . TYR F 265 ? 0.9085 0.4691 0.4763 -0.1033 0.1709 -0.0146 265 TYR Z CD2   
8777  C  CE1   . TYR F 265 ? 0.9198 0.4809 0.4891 -0.1178 0.161  -0.0117 265 TYR Z CE1   
8778  C  CE2   . TYR F 265 ? 0.9248 0.479  0.4847 -0.1073 0.1673 -0.0152 265 TYR Z CE2   
8779  C  CZ    . TYR F 265 ? 0.9369 0.4912 0.4974 -0.1146 0.1622 -0.0138 265 TYR Z CZ    
8780  O  OH    . TYR F 265 ? 0.9629 0.5107 0.5151 -0.1187 0.1585 -0.0144 265 TYR Z OH    
8781  N  N     . ARG F 266 ? 0.8792 0.4694 0.4854 -0.0962 0.1789 -0.0086 266 ARG Z N     
8782  C  CA    . ARG F 266 ? 0.8897 0.4808 0.4983 -0.0914 0.1838 -0.0088 266 ARG Z CA    
8783  C  C     . ARG F 266 ? 0.8988 0.4769 0.4941 -0.0905 0.1875 -0.0111 266 ARG Z C     
8784  O  O     . ARG F 266 ? 0.9084 0.4771 0.4939 -0.0949 0.1859 -0.012  266 ARG Z O     
8785  C  CB    . ARG F 266 ? 0.9119 0.5091 0.5297 -0.0936 0.1837 -0.0062 266 ARG Z CB    
8786  C  CG    . ARG F 266 ? 0.9736 0.563  0.5857 -0.0996 0.1833 -0.0059 266 ARG Z CG    
8787  C  CD    . ARG F 266 ? 1.0229 0.6197 0.6451 -0.1025 0.1826 -0.0029 266 ARG Z CD    
8788  N  NE    . ARG F 266 ? 1.0736 0.6619 0.6894 -0.1077 0.1833 -0.003  266 ARG Z NE    
8789  C  CZ    . ARG F 266 ? 1.1056 0.6926 0.7204 -0.1156 0.1791 -0.0015 266 ARG Z CZ    
8790  N  NH1   . ARG F 266 ? 1.0961 0.6908 0.7169 -0.119  0.1739 0.0003  266 ARG Z NH1   
8791  N  NH2   . ARG F 266 ? 1.1115 0.6897 0.7193 -0.1202 0.1801 -0.0018 266 ARG Z NH2   
8792  N  N     . ILE F 267 ? 0.8925 0.4696 0.4868 -0.0848 0.1925 -0.0119 267 ILE Z N     
8793  C  CA    . ILE F 267 ? 0.9004 0.4658 0.4822 -0.083  0.1966 -0.0138 267 ILE Z CA    
8794  C  C     . ILE F 267 ? 0.9065 0.4619 0.4808 -0.0883 0.197  -0.0137 267 ILE Z C     
8795  O  O     . ILE F 267 ? 0.9164 0.4599 0.4779 -0.0885 0.1991 -0.0152 267 ILE Z O     
8796  C  CB    . ILE F 267 ? 0.905  0.4729 0.4883 -0.0756 0.2017 -0.0142 267 ILE Z CB    
8797  C  CG1   . ILE F 267 ? 0.9251 0.4831 0.4959 -0.0722 0.2056 -0.0159 267 ILE Z CG1   
8798  C  CG2   . ILE F 267 ? 0.9085 0.479  0.4975 -0.0752 0.204  -0.0131 267 ILE Z CG2   
8799  C  CD1   . ILE F 267 ? 0.9406 0.5028 0.5132 -0.0649 0.2096 -0.0162 267 ILE Z CD1   
8800  N  N     . THR F 268 ? 0.8997 0.4595 0.4813 -0.0928 0.1948 -0.0119 268 THR Z N     
8801  C  CA    . THR F 268 ? 0.9075 0.4581 0.4822 -0.0986 0.1949 -0.0117 268 THR Z CA    
8802  C  C     . THR F 268 ? 0.907  0.4543 0.4782 -0.1068 0.1893 -0.0112 268 THR Z C     
8803  O  O     . THR F 268 ? 0.9135 0.4512 0.4765 -0.1124 0.1891 -0.0114 268 THR Z O     
8804  C  CB    . THR F 268 ? 0.9203 0.4764 0.5037 -0.0989 0.1966 -0.0099 268 THR Z CB    
8805  O  OG1   . THR F 268 ? 0.9271 0.4972 0.525  -0.0992 0.1934 -0.0076 268 THR Z OG1   
8806  C  CG2   . THR F 268 ? 0.9235 0.4781 0.5058 -0.0918 0.2027 -0.0107 268 THR Z CG2   
8807  N  N     . ASN F 269 ? 0.8981 0.4529 0.4748 -0.1077 0.1849 -0.0106 269 ASN Z N     
8808  C  CA    . ASN F 269 ? 0.9017 0.4538 0.475  -0.1153 0.1794 -0.0101 269 ASN Z CA    
8809  C  C     . ASN F 269 ? 0.8979 0.4436 0.4618 -0.1145 0.178  -0.012  269 ASN Z C     
8810  O  O     . ASN F 269 ? 0.8985 0.4458 0.4626 -0.1191 0.1729 -0.0114 269 ASN Z O     
8811  C  CB    . ASN F 269 ? 0.914  0.48   0.5015 -0.1189 0.1745 -0.007  269 ASN Z CB    
8812  C  CG    . ASN F 269 ? 0.9563 0.5336 0.553  -0.1153 0.1722 -0.0063 269 ASN Z CG    
8813  O  OD1   . ASN F 269 ? 0.974  0.5492 0.5666 -0.1109 0.1733 -0.0082 269 ASN Z OD1   
8814  N  ND2   . ASN F 269 ? 0.9582 0.5479 0.5678 -0.117  0.1692 -0.0033 269 ASN Z ND2   
8815  N  N     . LEU F 270 ? 0.8917 0.4304 0.4474 -0.1086 0.1826 -0.0141 270 LEU Z N     
8816  C  CA    . LEU F 270 ? 0.8908 0.4227 0.4369 -0.107  0.1824 -0.0159 270 LEU Z CA    
8817  C  C     . LEU F 270 ? 0.8932 0.4115 0.4259 -0.114  0.18   -0.0166 270 LEU Z C     
8818  O  O     . LEU F 270 ? 0.8997 0.4084 0.4246 -0.1167 0.1822 -0.0169 270 LEU Z O     
8819  C  CB    . LEU F 270 ? 0.8945 0.4213 0.4342 -0.0994 0.1885 -0.0174 270 LEU Z CB    
8820  C  CG    . LEU F 270 ? 0.9084 0.4365 0.4462 -0.0944 0.1891 -0.0184 270 LEU Z CG    
8821  C  CD1   . LEU F 270 ? 0.9073 0.4504 0.4593 -0.0924 0.1864 -0.0174 270 LEU Z CD1   
8822  C  CD2   . LEU F 270 ? 0.9174 0.4411 0.4493 -0.0874 0.1952 -0.0194 270 LEU Z CD2   
8823  N  N     . PRO F 271 ? 0.8842 0.4014 0.4139 -0.1175 0.1754 -0.0167 271 PRO Z N     
8824  C  CA    . PRO F 271 ? 0.8869 0.3908 0.4032 -0.1247 0.1728 -0.0174 271 PRO Z CA    
8825  C  C     . PRO F 271 ? 0.892  0.3784 0.3908 -0.1228 0.1778 -0.0194 271 PRO Z C     
8826  O  O     . PRO F 271 ? 0.9016 0.3753 0.3887 -0.1286 0.1773 -0.0198 271 PRO Z O     
8827  C  CB    . PRO F 271 ? 0.8954 0.4023 0.4124 -0.1268 0.1677 -0.0173 271 PRO Z CB    
8828  C  CG    . PRO F 271 ? 0.8959 0.4132 0.4217 -0.1192 0.1694 -0.0174 271 PRO Z CG    
8829  C  CD    . PRO F 271 ? 0.8701 0.3974 0.4077 -0.1151 0.1725 -0.0164 271 PRO Z CD    
8830  N  N     . SER F 272 ? 0.8854 0.3711 0.3822 -0.1147 0.1827 -0.0204 272 SER Z N     
8831  C  CA    . SER F 272 ? 0.897  0.3674 0.3779 -0.1114 0.1881 -0.0219 272 SER Z CA    
8832  C  C     . SER F 272 ? 0.9    0.3667 0.3791 -0.1087 0.1936 -0.0218 272 SER Z C     
8833  O  O     . SER F 272 ? 0.9117 0.3657 0.3775 -0.1053 0.1987 -0.0227 272 SER Z O     
8834  C  CB    . SER F 272 ? 0.9115 0.3835 0.391  -0.1039 0.1908 -0.0225 272 SER Z CB    
8835  O  OG    . SER F 272 ? 0.9299 0.4173 0.4243 -0.0984 0.1919 -0.0218 272 SER Z OG    
8836  N  N     . LEU F 273 ? 0.8866 0.364  0.3785 -0.1096 0.193  -0.0206 273 LEU Z N     
8837  C  CA    . LEU F 273 ? 0.8855 0.3601 0.3766 -0.1069 0.1982 -0.0204 273 LEU Z CA    
8838  C  C     . LEU F 273 ? 0.8889 0.3456 0.3637 -0.1119 0.1999 -0.0212 273 LEU Z C     
8839  O  O     . LEU F 273 ? 0.8947 0.3471 0.3663 -0.1203 0.1954 -0.0209 273 LEU Z O     
8840  C  CB    . LEU F 273 ? 0.8797 0.3684 0.3872 -0.1081 0.1965 -0.0188 273 LEU Z CB    
8841  C  CG    . LEU F 273 ? 0.8989 0.3924 0.4119 -0.1012 0.2021 -0.0185 273 LEU Z CG    
8842  C  CD1   . LEU F 273 ? 0.903  0.4037 0.4201 -0.093  0.2043 -0.0189 273 LEU Z CD1   
8843  C  CD2   . LEU F 273 ? 0.9001 0.4057 0.4279 -0.1031 0.2004 -0.0167 273 LEU Z CD2   
8844  N  N     . GLY F 274 ? 0.8829 0.3289 0.3466 -0.1067 0.2063 -0.022  274 GLY Z N     
8845  C  CA    . GLY F 274 ? 0.887  0.3141 0.3332 -0.1104 0.2089 -0.0228 274 GLY Z CA    
8846  C  C     . GLY F 274 ? 0.8848 0.297  0.3136 -0.1071 0.2123 -0.024  274 GLY Z C     
8847  O  O     . GLY F 274 ? 0.8966 0.2923 0.3097 -0.1074 0.2165 -0.0246 274 GLY Z O     
8848  N  N     . ARG F 275 ? 0.8685 0.2858 0.2995 -0.1036 0.2108 -0.0241 275 ARG Z N     
8849  C  CA    . ARG F 275 ? 0.8717 0.2755 0.2867 -0.0997 0.2143 -0.0249 275 ARG Z CA    
8850  C  C     . ARG F 275 ? 0.8719 0.2695 0.2796 -0.0913 0.2226 -0.0247 275 ARG Z C     
8851  O  O     . ARG F 275 ? 0.8864 0.2678 0.2769 -0.0892 0.2268 -0.0251 275 ARG Z O     
8852  C  CB    . ARG F 275 ? 0.8759 0.2874 0.2958 -0.0973 0.2114 -0.0249 275 ARG Z CB    
8853  C  CG    . ARG F 275 ? 0.8862 0.3166 0.3234 -0.0909 0.2117 -0.0242 275 ARG Z CG    
8854  C  CD    . ARG F 275 ? 0.9002 0.3378 0.3421 -0.0901 0.208  -0.0242 275 ARG Z CD    
8855  N  NE    . ARG F 275 ? 0.9066 0.359  0.361  -0.0829 0.2097 -0.0236 275 ARG Z NE    
8856  C  CZ    . ARG F 275 ? 0.9238 0.3749 0.3739 -0.0752 0.2151 -0.0233 275 ARG Z CZ    
8857  N  NH1   . ARG F 275 ? 0.9297 0.3653 0.3634 -0.073  0.2197 -0.0234 275 ARG Z NH1   
8858  N  NH2   . ARG F 275 ? 0.9085 0.3739 0.3706 -0.0696 0.2159 -0.0226 275 ARG Z NH2   
8859  N  N     . PHE F 276 ? 0.8546 0.2643 0.2748 -0.0867 0.2249 -0.0239 276 PHE Z N     
8860  C  CA    . PHE F 276 ? 0.8561 0.2613 0.2708 -0.0794 0.2324 -0.0234 276 PHE Z CA    
8861  C  C     . PHE F 276 ? 0.8518 0.2615 0.2743 -0.0813 0.2331 -0.0231 276 PHE Z C     
8862  O  O     . PHE F 276 ? 0.8442 0.2659 0.2807 -0.0858 0.2281 -0.0228 276 PHE Z O     
8863  C  CB    . PHE F 276 ? 0.8457 0.2609 0.2663 -0.0698 0.2357 -0.0226 276 PHE Z CB    
8864  C  CG    . PHE F 276 ? 0.8364 0.2723 0.277  -0.0682 0.2322 -0.0221 276 PHE Z CG    
8865  C  CD1   . PHE F 276 ? 0.8377 0.2838 0.2891 -0.065  0.2342 -0.0215 276 PHE Z CD1   
8866  C  CD2   . PHE F 276 ? 0.8412 0.2858 0.289  -0.0695 0.2273 -0.0223 276 PHE Z CD2   
8867  C  CE1   . PHE F 276 ? 0.8346 0.2984 0.3032 -0.0635 0.2312 -0.021  276 PHE Z CE1   
8868  C  CE2   . PHE F 276 ? 0.8387 0.3012 0.3037 -0.0679 0.2245 -0.0218 276 PHE Z CE2   
8869  C  CZ    . PHE F 276 ? 0.8298 0.3015 0.3048 -0.0649 0.2264 -0.0212 276 PHE Z CZ    
8870  N  N     . LYS F 277 ? 0.8542 0.2535 0.2669 -0.0781 0.2393 -0.023  277 LYS Z N     
8871  C  CA    . LYS F 277 ? 0.8527 0.2542 0.2708 -0.0796 0.2407 -0.0227 277 LYS Z CA    
8872  C  C     . LYS F 277 ? 0.8407 0.2536 0.2686 -0.0709 0.2451 -0.0217 277 LYS Z C     
8873  O  O     . LYS F 277 ? 0.8386 0.255  0.266  -0.0634 0.248  -0.0212 277 LYS Z O     
8874  C  CB    . LYS F 277 ? 0.8911 0.2718 0.2906 -0.0826 0.2447 -0.0232 277 LYS Z CB    
8875  C  CG    . LYS F 277 ? 0.9498 0.3201 0.3416 -0.0935 0.2397 -0.024  277 LYS Z CG    
8876  C  CD    . LYS F 277 ? 1.0156 0.3669 0.3909 -0.0969 0.2438 -0.0245 277 LYS Z CD    
8877  C  CE    . LYS F 277 ? 1.0667 0.4106 0.4375 -0.1089 0.2382 -0.0251 277 LYS Z CE    
8878  N  NZ    . LYS F 277 ? 1.0879 0.4442 0.4743 -0.1139 0.2348 -0.0243 277 LYS Z NZ    
8879  N  N     . PHE F 278 ? 0.8303 0.2491 0.267  -0.072  0.2454 -0.0213 278 PHE Z N     
8880  C  CA    . PHE F 278 ? 0.8233 0.2518 0.2683 -0.0641 0.2497 -0.0204 278 PHE Z CA    
8881  C  C     . PHE F 278 ? 0.8223 0.2358 0.2519 -0.0599 0.2571 -0.0203 278 PHE Z C     
8882  O  O     . PHE F 278 ? 0.8267 0.2289 0.2486 -0.0645 0.2584 -0.0207 278 PHE Z O     
8883  C  CB    . PHE F 278 ? 0.8191 0.2604 0.2801 -0.0669 0.2468 -0.0199 278 PHE Z CB    
8884  C  CG    . PHE F 278 ? 0.8323 0.279  0.2987 -0.0604 0.2518 -0.0191 278 PHE Z CG    
8885  C  CD1   . PHE F 278 ? 0.8431 0.2953 0.3107 -0.0514 0.2556 -0.0186 278 PHE Z CD1   
8886  C  CD2   . PHE F 278 ? 0.8438 0.2908 0.3146 -0.0634 0.2523 -0.0188 278 PHE Z CD2   
8887  C  CE1   . PHE F 278 ? 0.8504 0.3071 0.3221 -0.0456 0.2601 -0.0178 278 PHE Z CE1   
8888  C  CE2   . PHE F 278 ? 0.8514 0.303  0.3268 -0.0573 0.2568 -0.0181 278 PHE Z CE2   
8889  C  CZ    . PHE F 278 ? 0.848  0.3044 0.3237 -0.0485 0.2606 -0.0177 278 PHE Z CZ    
8890  N  N     . ARG F 279 ? 0.8151 0.2281 0.2398 -0.0512 0.2621 -0.0196 279 ARG Z N     
8891  C  CA    . ARG F 279 ? 0.8236 0.2233 0.2337 -0.0457 0.2698 -0.0191 279 ARG Z CA    
8892  C  C     . ARG F 279 ? 0.8117 0.2228 0.2296 -0.0363 0.2741 -0.0177 279 ARG Z C     
8893  O  O     . ARG F 279 ? 0.8102 0.2255 0.2273 -0.0296 0.2763 -0.0167 279 ARG Z O     
8894  C  CB    . ARG F 279 ? 0.8531 0.2381 0.2458 -0.0441 0.2724 -0.0191 279 ARG Z CB    
8895  C  CG    . ARG F 279 ? 0.8951 0.269  0.2797 -0.0536 0.2676 -0.0205 279 ARG Z CG    
8896  C  CD    . ARG F 279 ? 0.9325 0.2883 0.2971 -0.0521 0.2711 -0.0206 279 ARG Z CD    
8897  N  NE    . ARG F 279 ? 0.9535 0.2991 0.3105 -0.0616 0.2659 -0.022  279 ARG Z NE    
8898  C  CZ    . ARG F 279 ? 0.9801 0.3097 0.3248 -0.0687 0.266  -0.0229 279 ARG Z CZ    
8899  N  NH1   . ARG F 279 ? 0.9859 0.3074 0.3243 -0.0672 0.2713 -0.0227 279 ARG Z NH1   
8900  N  NH2   . ARG F 279 ? 0.9772 0.2987 0.3156 -0.0774 0.2608 -0.0241 279 ARG Z NH2   
8901  N  N     . LYS F 280 ? 0.8028 0.219  0.2284 -0.036  0.2752 -0.0176 280 LYS Z N     
8902  C  CA    . LYS F 280 ? 0.8006 0.2275 0.2339 -0.0278 0.279  -0.0163 280 LYS Z CA    
8903  C  C     . LYS F 280 ? 0.811  0.2283 0.2305 -0.0197 0.2867 -0.0151 280 LYS Z C     
8904  O  O     . LYS F 280 ? 0.8255 0.2258 0.2299 -0.0206 0.2908 -0.0153 280 LYS Z O     
8905  C  CB    . LYS F 280 ? 0.8194 0.25   0.2607 -0.03   0.279  -0.0164 280 LYS Z CB    
8906  C  CG    . LYS F 280 ? 0.8664 0.3043 0.3126 -0.0218 0.2838 -0.0152 280 LYS Z CG    
8907  C  CD    . LYS F 280 ? 0.9081 0.3652 0.3701 -0.0181 0.2808 -0.0146 280 LYS Z CD    
8908  C  CE    . LYS F 280 ? 0.9453 0.4094 0.4115 -0.0104 0.2852 -0.0134 280 LYS Z CE    
8909  N  NZ    . LYS F 280 ? 0.9844 0.4376 0.4363 -0.0039 0.2924 -0.0123 280 LYS Z NZ    
8910  N  N     . LYS F 281 ? 0.8032 0.2311 0.2275 -0.0117 0.2887 -0.0136 281 LYS Z N     
8911  C  CA    . LYS F 281 ? 0.8136 0.2348 0.2263 -0.003  0.2962 -0.0118 281 LYS Z CA    
8912  C  C     . LYS F 281 ? 0.8091 0.2345 0.2254 0.0025  0.3007 -0.0108 281 LYS Z C     
8913  O  O     . LYS F 281 ? 0.7987 0.2403 0.2291 0.0052  0.2988 -0.0102 281 LYS Z O     
8914  C  CB    . LYS F 281 ? 0.8359 0.2667 0.2515 0.0027  0.2961 -0.0103 281 LYS Z CB    
8915  C  CG    . LYS F 281 ? 0.9011 0.3227 0.3071 -0.0002 0.2946 -0.0107 281 LYS Z CG    
8916  C  CD    . LYS F 281 ? 0.9678 0.3923 0.3694 0.008   0.2984 -0.0083 281 LYS Z CD    
8917  C  CE    . LYS F 281 ? 1.0145 0.4585 0.4316 0.0096  0.2941 -0.0077 281 LYS Z CE    
8918  N  NZ    . LYS F 281 ? 1.048  0.4937 0.4691 0.0026  0.2874 -0.0093 281 LYS Z NZ    
8919  N  N     . ILE F 282 ? 0.8141 0.2246 0.217  0.0043  0.3067 -0.0105 282 ILE Z N     
8920  C  CA    . ILE F 282 ? 0.8135 0.2264 0.2182 0.0097  0.3115 -0.0095 282 ILE Z CA    
8921  C  C     . ILE F 282 ? 0.8233 0.2286 0.2147 0.0192  0.3195 -0.0072 282 ILE Z C     
8922  O  O     . ILE F 282 ? 0.8369 0.2251 0.2116 0.0191  0.3234 -0.0071 282 ILE Z O     
8923  C  CB    . ILE F 282 ? 0.8219 0.2245 0.2234 0.0036  0.3118 -0.011  282 ILE Z CB    
8924  C  CG1   . ILE F 282 ? 0.8264 0.2372 0.2415 -0.0056 0.3039 -0.0128 282 ILE Z CG1   
8925  C  CG2   . ILE F 282 ? 0.8257 0.2301 0.2286 0.0095  0.317  -0.01   282 ILE Z CG2   
8926  C  CD1   . ILE F 282 ? 0.8468 0.2474 0.2586 -0.0128 0.3035 -0.014  282 ILE Z CD1   
8927  N  N     . ALA F 283 ? 0.8163 0.2343 0.2147 0.0273  0.3222 -0.0051 283 ALA Z N     
8928  C  CA    . ALA F 283 ? 0.827  0.2398 0.214  0.037   0.33   -0.0023 283 ALA Z CA    
8929  C  C     . ALA F 283 ? 0.8411 0.2371 0.2148 0.0381  0.3363 -0.0025 283 ALA Z C     
8930  O  O     . ALA F 283 ? 0.8371 0.2329 0.2159 0.034   0.335  -0.004  283 ALA Z O     
8931  C  CB    . ALA F 283 ? 0.8184 0.2497 0.2173 0.0445  0.3307 -0.0001 283 ALA Z CB    
8932  N  N     . GLU F 284 ? 0.8553 0.2368 0.2115 0.0437  0.3435 -0.0007 284 GLU Z N     
8933  C  CA    . GLU F 284 ? 0.8741 0.2376 0.2153 0.0451  0.3502 -0.0007 284 GLU Z CA    
8934  C  C     . GLU F 284 ? 0.8674 0.2386 0.2157 0.0498  0.353  0.0001  284 GLU Z C     
8935  O  O     . GLU F 284 ? 0.8711 0.2324 0.2151 0.0465  0.3548 -0.0013 284 GLU Z O     
8936  C  CB    . GLU F 284 ? 0.9213 0.2694 0.2427 0.052   0.358  0.0016  284 GLU Z CB    
8937  C  CG    . GLU F 284 ? 1.0085 0.3368 0.3145 0.0454  0.3576 -0.0001 284 GLU Z CG    
8938  C  CD    . GLU F 284 ? 1.1287 0.4399 0.4137 0.0524  0.3659 0.0024  284 GLU Z CD    
8939  O  OE1   . GLU F 284 ? 1.1598 0.467  0.4387 0.0523  0.3651 0.0029  284 GLU Z OE1   
8940  O  OE2   . GLU F 284 ? 1.163  0.4646 0.4374 0.0585  0.3735 0.0039  284 GLU Z OE2   
8941  N  N     . LYS F 285 ? 0.8553 0.2445 0.2148 0.0568  0.353  0.0023  285 LYS Z N     
8942  C  CA    . LYS F 285 ? 0.8546 0.2527 0.2216 0.0617  0.3552 0.0032  285 LYS Z CA    
8943  C  C     . LYS F 285 ? 0.8558 0.2606 0.2364 0.0542  0.3495 0.0005  285 LYS Z C     
8944  O  O     . LYS F 285 ? 0.8612 0.2667 0.244  0.0565  0.3521 0.0006  285 LYS Z O     
8945  C  CB    . LYS F 285 ? 0.8629 0.2796 0.2392 0.0702  0.3557 0.0062  285 LYS Z CB    
8946  C  CG    . LYS F 285 ? 0.8952 0.33   0.288  0.0663  0.3475 0.0055  285 LYS Z CG    
8947  C  CD    . LYS F 285 ? 0.928  0.3809 0.3294 0.0741  0.3479 0.0086  285 LYS Z CD    
8948  C  CE    . LYS F 285 ? 0.9512 0.4211 0.3682 0.0699  0.3399 0.0077  285 LYS Z CE    
8949  N  NZ    . LYS F 285 ? 0.9631 0.4511 0.389  0.0767  0.3399 0.0107  285 LYS Z NZ    
8950  N  N     . SER F 286 ? 0.8511 0.2603 0.2403 0.0455  0.342  -0.0018 286 SER Z N     
8951  C  CA    . SER F 286 ? 0.8517 0.2675 0.254  0.0382  0.3364 -0.004  286 SER Z CA    
8952  C  C     . SER F 286 ? 0.8704 0.2697 0.2644 0.0306  0.3368 -0.0061 286 SER Z C     
8953  O  O     . SER F 286 ? 0.8688 0.2725 0.2727 0.0253  0.3333 -0.0074 286 SER Z O     
8954  C  CB    . SER F 286 ? 0.856  0.2849 0.2716 0.0328  0.3281 -0.0051 286 SER Z CB    
8955  O  OG    . SER F 286 ? 0.877  0.3209 0.2999 0.0389  0.3273 -0.0033 286 SER Z OG    
8956  N  N     . LEU F 287 ? 0.8847 0.2653 0.2609 0.0297  0.3408 -0.0062 287 LEU Z N     
8957  C  CA    . LEU F 287 ? 0.9008 0.2648 0.268  0.0216  0.3409 -0.0081 287 LEU Z CA    
8958  C  C     . LEU F 287 ? 0.9179 0.275  0.2812 0.0234  0.3461 -0.008  287 LEU Z C     
8959  O  O     . LEU F 287 ? 0.924  0.2799 0.2819 0.0325  0.3526 -0.0061 287 LEU Z O     
8960  C  CB    . LEU F 287 ? 0.9126 0.2574 0.2605 0.0198  0.3436 -0.0083 287 LEU Z CB    
8961  C  CG    . LEU F 287 ? 0.927  0.2748 0.2774 0.0146  0.3374 -0.0092 287 LEU Z CG    
8962  C  CD1   . LEU F 287 ? 0.9473 0.2751 0.2771 0.0141  0.3411 -0.0091 287 LEU Z CD1   
8963  C  CD2   . LEU F 287 ? 0.9288 0.2817 0.2904 0.0037  0.3294 -0.0114 287 LEU Z CD2   
8964  N  N     . SER F 288 ? 0.9242 0.2767 0.2903 0.0147  0.3432 -0.0098 288 SER Z N     
8965  C  CA    . SER F 288 ? 0.9383 0.2833 0.3014 0.0142  0.3472 -0.01   288 SER Z CA    
8966  C  C     . SER F 288 ? 0.9448 0.282  0.308  0.0022  0.3429 -0.012  288 SER Z C     
8967  O  O     . SER F 288 ? 0.9411 0.2817 0.3092 -0.0051 0.3364 -0.0131 288 SER Z O     
8968  C  CB    . SER F 288 ? 0.9496 0.3119 0.3288 0.0192  0.3468 -0.0092 288 SER Z CB    
8969  O  OG    . SER F 288 ? 0.9834 0.3517 0.3612 0.0303  0.3515 -0.0071 288 SER Z OG    
8970  N  N     . GLY F 289 ? 0.9544 0.281  0.3118 0.0001  0.3467 -0.0124 289 GLY Z N     
8971  C  CA    . GLY F 289 ? 0.9687 0.2883 0.3263 -0.0113 0.3431 -0.0138 289 GLY Z CA    
8972  C  C     . GLY F 289 ? 0.9841 0.2941 0.3337 -0.0203 0.3387 -0.0151 289 GLY Z C     
8973  O  O     . GLY F 289 ? 0.9988 0.2933 0.3308 -0.0189 0.3424 -0.0152 289 GLY Z O     
8974  N  N     . LYS F 290 ? 0.9795 0.299  0.3421 -0.0295 0.3308 -0.0159 290 LYS Z N     
8975  C  CA    . LYS F 290 ? 0.9942 0.3064 0.3509 -0.0388 0.3256 -0.017  290 LYS Z CA    
8976  C  C     . LYS F 290 ? 0.9947 0.322  0.363  -0.0385 0.3192 -0.017  290 LYS Z C     
8977  O  O     . LYS F 290 ? 0.9961 0.324  0.3668 -0.0471 0.3129 -0.0178 290 LYS Z O     
8978  C  CB    . LYS F 290 ? 1.0153 0.3253 0.3763 -0.0504 0.3213 -0.0177 290 LYS Z CB    
8979  C  CG    . LYS F 290 ? 1.076  0.3695 0.4244 -0.0521 0.3273 -0.0178 290 LYS Z CG    
8980  C  CD    . LYS F 290 ? 1.1321 0.4286 0.4895 -0.0625 0.323  -0.0179 290 LYS Z CD    
8981  C  CE    . LYS F 290 ? 1.1961 0.4777 0.5424 -0.0636 0.3292 -0.0179 290 LYS Z CE    
8982  N  NZ    . LYS F 290 ? 1.2218 0.511  0.5812 -0.0714 0.3257 -0.0173 290 LYS Z NZ    
8983  N  N     . VAL F 291 ? 0.9908 0.3305 0.3662 -0.0287 0.3208 -0.016  291 VAL Z N     
8984  C  CA    . VAL F 291 ? 0.9885 0.3435 0.3754 -0.0274 0.3154 -0.0159 291 VAL Z CA    
8985  C  C     . VAL F 291 ? 1.0006 0.3458 0.3758 -0.0304 0.3136 -0.0165 291 VAL Z C     
8986  O  O     . VAL F 291 ? 0.9945 0.3469 0.3776 -0.0365 0.3067 -0.0172 291 VAL Z O     
8987  C  CB    . VAL F 291 ? 0.9907 0.3591 0.3854 -0.0163 0.3183 -0.0145 291 VAL Z CB    
8988  C  CG1   . VAL F 291 ? 0.9917 0.3741 0.396  -0.0148 0.3133 -0.0143 291 VAL Z CG1   
8989  C  CG2   . VAL F 291 ? 0.9862 0.366  0.3946 -0.0144 0.3186 -0.0139 291 VAL Z CG2   
8990  N  N     . LYS F 292 ? 1.0183 0.3462 0.374  -0.0263 0.32   -0.0163 292 LYS Z N     
8991  C  CA    . LYS F 292 ? 1.0367 0.3528 0.3789 -0.0286 0.3193 -0.0168 292 LYS Z CA    
8992  C  C     . LYS F 292 ? 1.0496 0.3566 0.3879 -0.0413 0.3138 -0.0184 292 LYS Z C     
8993  O  O     . LYS F 292 ? 1.0522 0.3605 0.3912 -0.046  0.3084 -0.0191 292 LYS Z O     
8994  C  CB    . LYS F 292 ? 1.0713 0.3689 0.3921 -0.0217 0.328  -0.0159 292 LYS Z CB    
8995  C  CG    . LYS F 292 ? 1.1321 0.4199 0.4404 -0.0221 0.3276 -0.016  292 LYS Z CG    
8996  C  CD    . LYS F 292 ? 1.2034 0.4701 0.4884 -0.0164 0.3363 -0.0151 292 LYS Z CD    
8997  C  CE    . LYS F 292 ? 1.258  0.5153 0.5305 -0.0157 0.3363 -0.0149 292 LYS Z CE    
8998  N  NZ    . LYS F 292 ? 1.2879 0.5404 0.5595 -0.0276 0.3287 -0.017  292 LYS Z NZ    
8999  N  N     . GLU F 293 ? 1.0547 0.3537 0.3901 -0.0469 0.3148 -0.019  293 GLU Z N     
9000  C  CA    . GLU F 293 ? 1.066  0.357  0.3983 -0.0594 0.3098 -0.0202 293 GLU Z CA    
9001  C  C     . GLU F 293 ? 1.0503 0.3609 0.4035 -0.0657 0.3006 -0.0203 293 GLU Z C     
9002  O  O     . GLU F 293 ? 1.0502 0.3582 0.4019 -0.0742 0.2948 -0.0211 293 GLU Z O     
9003  C  CB    . GLU F 293 ? 1.1105 0.391  0.437  -0.0629 0.3136 -0.0203 293 GLU Z CB    
9004  C  CG    . GLU F 293 ? 1.205  0.4636 0.5088 -0.0579 0.3226 -0.0203 293 GLU Z CG    
9005  C  CD    . GLU F 293 ? 1.3041 0.5663 0.6091 -0.046  0.3301 -0.019  293 GLU Z CD    
9006  O  OE1   . GLU F 293 ? 1.3346 0.5869 0.6325 -0.0457 0.3353 -0.0189 293 GLU Z OE1   
9007  O  OE2   . GLU F 293 ? 1.3279 0.6029 0.6406 -0.0371 0.3308 -0.0179 293 GLU Z OE2   
9008  N  N     . PHE F 294 ? 1.0345 0.3643 0.4066 -0.0613 0.2996 -0.0194 294 PHE Z N     
9009  C  CA    . PHE F 294 ? 1.0239 0.3728 0.4162 -0.0658 0.2917 -0.0191 294 PHE Z CA    
9010  C  C     . PHE F 294 ? 1.019  0.3744 0.4137 -0.0646 0.2876 -0.0194 294 PHE Z C     
9011  O  O     . PHE F 294 ? 1.0177 0.3789 0.4193 -0.072  0.2806 -0.0197 294 PHE Z O     
9012  C  CB    . PHE F 294 ? 1.0131 0.3794 0.4229 -0.06   0.2925 -0.018  294 PHE Z CB    
9013  C  CG    . PHE F 294 ? 1.0102 0.3959 0.4401 -0.0636 0.285  -0.0176 294 PHE Z CG    
9014  C  CD1   . PHE F 294 ? 1.016  0.4056 0.4544 -0.0726 0.2803 -0.0172 294 PHE Z CD1   
9015  C  CD2   . PHE F 294 ? 1.0137 0.4134 0.4535 -0.058  0.2827 -0.0173 294 PHE Z CD2   
9016  C  CE1   . PHE F 294 ? 1.0137 0.4208 0.4699 -0.0754 0.2738 -0.0165 294 PHE Z CE1   
9017  C  CE2   . PHE F 294 ? 1.0113 0.4275 0.4682 -0.0613 0.2761 -0.0169 294 PHE Z CE2   
9018  C  CZ    . PHE F 294 ? 1.0047 0.4245 0.4697 -0.0696 0.2718 -0.0164 294 PHE Z CZ    
9019  N  N     . ASN F 295 ? 1.0131 0.3676 0.4021 -0.0553 0.2919 -0.0191 295 ASN Z N     
9020  C  CA    . ASN F 295 ? 1.0095 0.3699 0.4002 -0.0536 0.2886 -0.0192 295 ASN Z CA    
9021  C  C     . ASN F 295 ? 1.0194 0.3652 0.3965 -0.0613 0.2857 -0.0203 295 ASN Z C     
9022  O  O     . ASN F 295 ? 1.0169 0.3698 0.4004 -0.0653 0.2796 -0.0207 295 ASN Z O     
9023  C  CB    . ASN F 295 ? 1.0202 0.3816 0.4063 -0.0422 0.2943 -0.0182 295 ASN Z CB    
9024  C  CG    . ASN F 295 ? 1.0439 0.4186 0.4389 -0.0392 0.2905 -0.0179 295 ASN Z CG    
9025  O  OD1   . ASN F 295 ? 1.0467 0.4316 0.4532 -0.0449 0.2835 -0.0185 295 ASN Z OD1   
9026  N  ND2   . ASN F 295 ? 1.0518 0.4268 0.4418 -0.0301 0.2951 -0.0168 295 ASN Z ND2   
9027  N  N     . ASN F 296 ? 1.0303 0.3553 0.3885 -0.064  0.2901 -0.0208 296 ASN Z N     
9028  C  CA    . ASN F 296 ? 1.0452 0.3541 0.3885 -0.072  0.2876 -0.0219 296 ASN Z CA    
9029  C  C     . ASN F 296 ? 1.0364 0.3515 0.3897 -0.0836 0.2793 -0.0225 296 ASN Z C     
9030  O  O     . ASN F 296 ? 1.0397 0.3529 0.3904 -0.0894 0.2742 -0.0231 296 ASN Z O     
9031  C  CB    . ASN F 296 ? 1.0826 0.3674 0.4033 -0.0726 0.2943 -0.0224 296 ASN Z CB    
9032  C  CG    . ASN F 296 ? 1.1427 0.4191 0.451  -0.0612 0.3028 -0.0215 296 ASN Z CG    
9033  O  OD1   . ASN F 296 ? 1.1735 0.4367 0.4696 -0.058  0.3097 -0.0212 296 ASN Z OD1   
9034  N  ND2   . ASN F 296 ? 1.1488 0.433  0.4602 -0.0546 0.3026 -0.0208 296 ASN Z ND2   
9035  N  N     . ILE F 297 ? 1.0231 0.3464 0.388  -0.0869 0.2782 -0.022  297 ILE Z N     
9036  C  CA    . ILE F 297 ? 1.0157 0.3471 0.3919 -0.0974 0.2706 -0.0218 297 ILE Z CA    
9037  C  C     . ILE F 297 ? 1.0045 0.3552 0.3979 -0.097  0.2641 -0.0214 297 ILE Z C     
9038  O  O     . ILE F 297 ? 1.0048 0.3571 0.4002 -0.105  0.2576 -0.0216 297 ILE Z O     
9039  C  CB    . ILE F 297 ? 1.0134 0.3501 0.399  -0.0995 0.2717 -0.021  297 ILE Z CB    
9040  C  CG1   . ILE F 297 ? 1.0331 0.3487 0.4002 -0.1023 0.2773 -0.0215 297 ILE Z CG1   
9041  C  CG2   . ILE F 297 ? 1.0098 0.3604 0.4118 -0.1086 0.2638 -0.0201 297 ILE Z CG2   
9042  C  CD1   . ILE F 297 ? 1.0437 0.3632 0.4182 -0.1021 0.28   -0.0207 297 ILE Z CD1   
9043  N  N     . VAL F 298 ? 0.9934 0.3585 0.3986 -0.0876 0.2659 -0.0208 298 VAL Z N     
9044  C  CA    . VAL F 298 ? 0.9843 0.3673 0.4052 -0.0864 0.2603 -0.0204 298 VAL Z CA    
9045  C  C     . VAL F 298 ? 0.994  0.3708 0.4057 -0.0879 0.2577 -0.0213 298 VAL Z C     
9046  O  O     . VAL F 298 ? 0.9913 0.3749 0.4101 -0.094  0.2509 -0.0213 298 VAL Z O     
9047  C  CB    . VAL F 298 ? 0.9806 0.3778 0.413  -0.076  0.2634 -0.0196 298 VAL Z CB    
9048  C  CG1   . VAL F 298 ? 0.9759 0.3893 0.4218 -0.0746 0.2581 -0.0194 298 VAL Z CG1   
9049  C  CG2   . VAL F 298 ? 0.9793 0.3842 0.4225 -0.0752 0.265  -0.0187 298 VAL Z CG2   
9050  N  N     . GLN F 299 ? 1.002  0.3646 0.3969 -0.0826 0.2632 -0.0218 299 GLN Z N     
9051  C  CA    . GLN F 299 ? 1.0086 0.3632 0.3928 -0.0831 0.2618 -0.0225 299 GLN Z CA    
9052  C  C     . GLN F 299 ? 1.0237 0.3651 0.397  -0.0942 0.2573 -0.0234 299 GLN Z C     
9053  O  O     . GLN F 299 ? 1.0298 0.3672 0.3972 -0.0963 0.2543 -0.024  299 GLN Z O     
9054  C  CB    . GLN F 299 ? 1.0267 0.3694 0.3955 -0.0741 0.2695 -0.0223 299 GLN Z CB    
9055  C  CG    . GLN F 299 ? 1.0487 0.4061 0.4289 -0.0635 0.273  -0.0212 299 GLN Z CG    
9056  C  CD    . GLN F 299 ? 1.0993 0.4488 0.4671 -0.0542 0.2797 -0.0205 299 GLN Z CD    
9057  O  OE1   . GLN F 299 ? 1.1254 0.4618 0.4786 -0.0546 0.2807 -0.0208 299 GLN Z OE1   
9058  N  NE2   . GLN F 299 ? 1.0991 0.4569 0.4727 -0.0453 0.2844 -0.0192 299 GLN Z NE2   
9059  N  N     . ARG F 300 ? 1.0284 0.3638 0.3997 -0.1015 0.2567 -0.0235 300 ARG Z N     
9060  C  CA    . ARG F 300 ? 1.0427 0.3667 0.4046 -0.1129 0.252  -0.0242 300 ARG Z CA    
9061  C  C     . ARG F 300 ? 1.0312 0.3712 0.4095 -0.1199 0.2431 -0.0236 300 ARG Z C     
9062  O  O     . ARG F 300 ? 1.0409 0.3745 0.4124 -0.1274 0.2382 -0.0242 300 ARG Z O     
9063  C  CB    . ARG F 300 ? 1.0709 0.3837 0.4255 -0.1184 0.2546 -0.0242 300 ARG Z CB    
9064  C  CG    . ARG F 300 ? 1.1338 0.427  0.4684 -0.1129 0.263  -0.0248 300 ARG Z CG    
9065  C  CD    . ARG F 300 ? 1.1993 0.471  0.5146 -0.1224 0.2626 -0.0258 300 ARG Z CD    
9066  N  NE    . ARG F 300 ? 1.2479 0.5164 0.564  -0.1273 0.2641 -0.0254 300 ARG Z NE    
9067  C  CZ    . ARG F 300 ? 1.2882 0.5475 0.5978 -0.1392 0.2604 -0.0257 300 ARG Z CZ    
9068  N  NH1   . ARG F 300 ? 1.2865 0.5379 0.5873 -0.1474 0.255  -0.0264 300 ARG Z NH1   
9069  N  NH2   . ARG F 300 ? 1.2926 0.5502 0.6041 -0.1431 0.262  -0.0252 300 ARG Z NH2   
9070  N  N     . TYR F 301 ? 1.0066 0.3673 0.4061 -0.1174 0.241  -0.0224 301 TYR Z N     
9071  C  CA    . TYR F 301 ? 0.9919 0.3687 0.4079 -0.1236 0.233  -0.0215 301 TYR Z CA    
9072  C  C     . TYR F 301 ? 0.9737 0.369  0.4056 -0.1173 0.2306 -0.0209 301 TYR Z C     
9073  O  O     . TYR F 301 ? 0.966  0.3737 0.4101 -0.122  0.2241 -0.0201 301 TYR Z O     
9074  C  CB    . TYR F 301 ? 0.9855 0.3707 0.4135 -0.1283 0.2316 -0.02   301 TYR Z CB    
9075  C  CG    . TYR F 301 ? 1.0055 0.3739 0.4196 -0.1357 0.2333 -0.0203 301 TYR Z CG    
9076  C  CD1   . TYR F 301 ? 1.0252 0.3815 0.4285 -0.1311 0.2409 -0.0209 301 TYR Z CD1   
9077  C  CD2   . TYR F 301 ? 1.0179 0.383  0.4298 -0.1474 0.2273 -0.0199 301 TYR Z CD2   
9078  C  CE1   . TYR F 301 ? 1.0458 0.3857 0.4354 -0.138  0.2427 -0.0212 301 TYR Z CE1   
9079  C  CE2   . TYR F 301 ? 1.0393 0.3884 0.4378 -0.1549 0.2288 -0.0202 301 TYR Z CE2   
9080  C  CZ    . TYR F 301 ? 1.0575 0.3943 0.4453 -0.1502 0.2366 -0.0209 301 TYR Z CZ    
9081  O  OH    . TYR F 301 ? 1.0843 0.4051 0.4588 -0.1577 0.2382 -0.0211 301 TYR Z OH    
9082  N  N     . SER F 302 ? 0.9636 0.3619 0.3963 -0.107  0.2358 -0.0211 302 SER Z N     
9083  C  CA    . SER F 302 ? 0.9506 0.3664 0.3983 -0.1009 0.234  -0.0206 302 SER Z CA    
9084  C  C     . SER F 302 ? 0.9505 0.3672 0.3961 -0.1013 0.2303 -0.0212 302 SER Z C     
9085  O  O     . SER F 302 ? 0.9637 0.3655 0.3933 -0.1033 0.2309 -0.0222 302 SER Z O     
9086  C  CB    . SER F 302 ? 0.9591 0.378  0.4081 -0.0902 0.2406 -0.0205 302 SER Z CB    
9087  O  OG    . SER F 302 ? 0.9912 0.3968 0.4241 -0.0852 0.2454 -0.0213 302 SER Z OG    
9088  N  N     . VAL F 303 ? 0.9316 0.3655 0.3931 -0.0994 0.2264 -0.0205 303 VAL Z N     
9089  C  CA    . VAL F 303 ? 0.9293 0.3678 0.3922 -0.098  0.2231 -0.0209 303 VAL Z CA    
9090  C  C     . VAL F 303 ? 0.9205 0.3713 0.3932 -0.0884 0.2261 -0.0206 303 VAL Z C     
9091  O  O     . VAL F 303 ? 0.92   0.381  0.404  -0.0855 0.2274 -0.0197 303 VAL Z O     
9092  C  CB    . VAL F 303 ? 0.9332 0.3804 0.4054 -0.1057 0.2152 -0.0203 303 VAL Z CB    
9093  C  CG1   . VAL F 303 ? 0.9503 0.3847 0.4115 -0.1154 0.2123 -0.0206 303 VAL Z CG1   
9094  C  CG2   . VAL F 303 ? 0.9264 0.3913 0.418  -0.1059 0.2127 -0.0187 303 VAL Z CG2   
9095  N  N     . GLY F 304 ? 0.9136 0.3623 0.3805 -0.0835 0.2276 -0.0211 304 GLY Z N     
9096  C  CA    . GLY F 304 ? 0.9043 0.3636 0.3786 -0.0747 0.2304 -0.0207 304 GLY Z CA    
9097  C  C     . GLY F 304 ? 0.8864 0.3638 0.3785 -0.0745 0.2258 -0.0201 304 GLY Z C     
9098  O  O     . GLY F 304 ? 0.8845 0.3657 0.3808 -0.0796 0.2202 -0.0201 304 GLY Z O     
9099  N  N     . LEU F 305 ? 0.8728 0.3609 0.3748 -0.0686 0.2282 -0.0194 305 LEU Z N     
9100  C  CA    . LEU F 305 ? 0.8614 0.3659 0.3793 -0.0676 0.2247 -0.0188 305 LEU Z CA    
9101  C  C     . LEU F 305 ? 0.8534 0.3635 0.3723 -0.0602 0.227  -0.0188 305 LEU Z C     
9102  O  O     . LEU F 305 ? 0.8551 0.3668 0.3739 -0.0542 0.2317 -0.0184 305 LEU Z O     
9103  C  CB    . LEU F 305 ? 0.8593 0.3717 0.388  -0.0673 0.2254 -0.0178 305 LEU Z CB    
9104  C  CG    . LEU F 305 ? 0.8736 0.4015 0.4183 -0.0676 0.2214 -0.0169 305 LEU Z CG    
9105  C  CD1   . LEU F 305 ? 0.8816 0.4115 0.43   -0.0751 0.2153 -0.0165 305 LEU Z CD1   
9106  C  CD2   . LEU F 305 ? 0.8785 0.4132 0.4324 -0.0656 0.2234 -0.0159 305 LEU Z CD2   
9107  N  N     . ALA F 306 ? 0.8416 0.3546 0.3609 -0.0607 0.2239 -0.0192 306 ALA Z N     
9108  C  CA    . ALA F 306 ? 0.8364 0.355  0.3567 -0.0547 0.2253 -0.0191 306 ALA Z CA    
9109  C  C     . ALA F 306 ? 0.8374 0.3453 0.3438 -0.0502 0.2303 -0.0191 306 ALA Z C     
9110  O  O     . ALA F 306 ? 0.8414 0.3484 0.3437 -0.0486 0.23   -0.0192 306 ALA Z O     
9111  C  CB    . ALA F 306 ? 0.8318 0.3636 0.3639 -0.0498 0.2264 -0.0184 306 ALA Z CB    
9112  N  N     . SER F 307 ? 0.8335 0.3336 0.3327 -0.0479 0.2352 -0.0189 307 SER Z N     
9113  C  CA    . SER F 307 ? 0.8402 0.3293 0.3254 -0.0432 0.2407 -0.0186 307 SER Z CA    
9114  C  C     . SER F 307 ? 0.8441 0.3199 0.319  -0.0447 0.2443 -0.0188 307 SER Z C     
9115  O  O     . SER F 307 ? 0.8445 0.3234 0.3254 -0.0458 0.2447 -0.0187 307 SER Z O     
9116  C  CB    . SER F 307 ? 0.852  0.3497 0.341  -0.0349 0.2447 -0.0174 307 SER Z CB    
9117  O  OG    . SER F 307 ? 0.8763 0.3837 0.3713 -0.0333 0.2421 -0.0172 307 SER Z OG    
9118  N  N     . SER F 308 ? 0.8441 0.3046 0.303  -0.0444 0.2474 -0.0189 308 SER Z N     
9119  C  CA    . SER F 308 ? 0.8478 0.2935 0.2945 -0.0459 0.2513 -0.0192 308 SER Z CA    
9120  C  C     . SER F 308 ? 0.8362 0.2841 0.284  -0.0392 0.2572 -0.0182 308 SER Z C     
9121  O  O     . SER F 308 ? 0.8396 0.2818 0.2851 -0.0414 0.2589 -0.0184 308 SER Z O     
9122  C  CB    . SER F 308 ? 0.8783 0.3065 0.3064 -0.0458 0.2541 -0.0194 308 SER Z CB    
9123  O  OG    . SER F 308 ? 0.9121 0.3397 0.3345 -0.0372 0.2596 -0.018  308 SER Z OG    
9124  N  N     . ASP F 309 ? 0.8201 0.2768 0.2717 -0.0314 0.2601 -0.0169 309 ASP Z N     
9125  C  CA    . ASP F 309 ? 0.8141 0.273  0.2659 -0.0246 0.2657 -0.0157 309 ASP Z CA    
9126  C  C     . ASP F 309 ? 0.7958 0.2717 0.2643 -0.0228 0.2639 -0.0154 309 ASP Z C     
9127  O  O     . ASP F 309 ? 0.798  0.2778 0.2677 -0.0164 0.2683 -0.0142 309 ASP Z O     
9128  C  CB    . ASP F 309 ? 0.8382 0.2937 0.2806 -0.0165 0.2715 -0.0141 309 ASP Z CB    
9129  C  CG    . ASP F 309 ? 0.8882 0.3558 0.3376 -0.013  0.2696 -0.0132 309 ASP Z CG    
9130  O  OD1   . ASP F 309 ? 0.8948 0.3693 0.3524 -0.0178 0.2636 -0.0142 309 ASP Z OD1   
9131  O  OD2   . ASP F 309 ? 0.9138 0.384  0.3603 -0.0055 0.2742 -0.0113 309 ASP Z OD2   
9132  N  N     . LEU F 310 ? 0.7768 0.2621 0.2576 -0.0282 0.2577 -0.0162 310 LEU Z N     
9133  C  CA    . LEU F 310 ? 0.7626 0.262  0.258  -0.0269 0.2563 -0.0159 310 LEU Z CA    
9134  C  C     . LEU F 310 ? 0.7646 0.2583 0.2588 -0.0285 0.2586 -0.016  310 LEU Z C     
9135  O  O     . LEU F 310 ? 0.7705 0.2514 0.2553 -0.0331 0.2591 -0.0167 310 LEU Z O     
9136  C  CB    . LEU F 310 ? 0.7534 0.2635 0.2613 -0.0319 0.2495 -0.0165 310 LEU Z CB    
9137  C  CG    . LEU F 310 ? 0.7637 0.284  0.2771 -0.0289 0.2475 -0.0162 310 LEU Z CG    
9138  C  CD1   . LEU F 310 ? 0.7657 0.2946 0.2898 -0.0341 0.2412 -0.0168 310 LEU Z CD1   
9139  C  CD2   . LEU F 310 ? 0.7659 0.2962 0.2849 -0.022  0.2505 -0.0151 310 LEU Z CD2   
9140  N  N     . PRO F 311 ? 0.7574 0.2595 0.2601 -0.025  0.2603 -0.0154 311 PRO Z N     
9141  C  CA    . PRO F 311 ? 0.7602 0.2559 0.2608 -0.0261 0.2631 -0.0154 311 PRO Z CA    
9142  C  C     . PRO F 311 ? 0.7593 0.255  0.2659 -0.0341 0.2589 -0.016  311 PRO Z C     
9143  O  O     . PRO F 311 ? 0.76   0.2539 0.2683 -0.0349 0.2607 -0.0158 311 PRO Z O     
9144  C  CB    . PRO F 311 ? 0.7627 0.2685 0.271  -0.0196 0.2659 -0.0145 311 PRO Z CB    
9145  C  CG    . PRO F 311 ? 0.7586 0.2786 0.2782 -0.0187 0.2617 -0.0143 311 PRO Z CG    
9146  C  CD    . PRO F 311 ? 0.7414 0.2579 0.2545 -0.0197 0.2601 -0.0146 311 PRO Z CD    
9147  N  N     . PHE F 312 ? 0.7552 0.2529 0.2651 -0.0399 0.2533 -0.0166 312 PHE Z N     
9148  C  CA    . PHE F 312 ? 0.7557 0.2546 0.2718 -0.0476 0.2488 -0.0167 312 PHE Z CA    
9149  C  C     . PHE F 312 ? 0.7717 0.2643 0.2823 -0.0543 0.2446 -0.0174 312 PHE Z C     
9150  O  O     . PHE F 312 ? 0.7755 0.2669 0.2815 -0.0529 0.2437 -0.0178 312 PHE Z O     
9151  C  CB    . PHE F 312 ? 0.7355 0.2504 0.2685 -0.0474 0.2454 -0.0159 312 PHE Z CB    
9152  C  CG    . PHE F 312 ? 0.7318 0.2568 0.2707 -0.0441 0.2431 -0.016  312 PHE Z CG    
9153  C  CD1   . PHE F 312 ? 0.7365 0.2672 0.2769 -0.0367 0.2463 -0.0156 312 PHE Z CD1   
9154  C  CD2   . PHE F 312 ? 0.7375 0.2662 0.28   -0.0485 0.2377 -0.0163 312 PHE Z CD2   
9155  C  CE1   . PHE F 312 ? 0.74   0.2797 0.2854 -0.0342 0.2441 -0.0156 312 PHE Z CE1   
9156  C  CE2   . PHE F 312 ? 0.7387 0.276  0.286  -0.0456 0.2358 -0.0163 312 PHE Z CE2   
9157  C  CZ    . PHE F 312 ? 0.7337 0.2764 0.2824 -0.0387 0.239  -0.016  312 PHE Z CZ    
9158  N  N     . GLY F 313 ? 0.78   0.2686 0.2909 -0.0618 0.2418 -0.0174 313 GLY Z N     
9159  C  CA    . GLY F 313 ? 0.7991 0.282  0.3052 -0.0692 0.2372 -0.0179 313 GLY Z CA    
9160  C  C     . GLY F 313 ? 0.809  0.2964 0.3238 -0.0769 0.2326 -0.0171 313 GLY Z C     
9161  O  O     . GLY F 313 ? 0.8056 0.3016 0.3312 -0.0759 0.233  -0.016  313 GLY Z O     
9162  N  N     . VAL F 314 ? 0.8183 0.3005 0.3288 -0.0845 0.2281 -0.0173 314 VAL Z N     
9163  C  CA    . VAL F 314 ? 0.8269 0.3145 0.346  -0.0922 0.2232 -0.0161 314 VAL Z CA    
9164  C  C     . VAL F 314 ? 0.8431 0.3166 0.3505 -0.0998 0.223  -0.0164 314 VAL Z C     
9165  O  O     . VAL F 314 ? 0.8545 0.3143 0.3469 -0.1012 0.2239 -0.0177 314 VAL Z O     
9166  C  CB    . VAL F 314 ? 0.8329 0.3313 0.3615 -0.0953 0.2167 -0.0155 314 VAL Z CB    
9167  C  CG1   . VAL F 314 ? 0.8358 0.3416 0.3747 -0.1027 0.2119 -0.0137 314 VAL Z CG1   
9168  C  CG2   . VAL F 314 ? 0.8319 0.3432 0.3709 -0.088  0.217  -0.0154 314 VAL Z CG2   
9169  N  N     . ILE F 315 ? 0.8427 0.3191 0.3564 -0.1048 0.2219 -0.0151 315 ILE Z N     
9170  C  CA    . ILE F 315 ? 0.857  0.3224 0.3622 -0.1136 0.2205 -0.0149 315 ILE Z CA    
9171  C  C     . ILE F 315 ? 0.8623 0.3399 0.3803 -0.1206 0.2133 -0.0131 315 ILE Z C     
9172  O  O     . ILE F 315 ? 0.8554 0.3463 0.3883 -0.12   0.2124 -0.0111 315 ILE Z O     
9173  C  CB    . ILE F 315 ? 0.8605 0.321  0.3642 -0.1135 0.2252 -0.0144 315 ILE Z CB    
9174  C  CG1   . ILE F 315 ? 0.8757 0.3267 0.3689 -0.105  0.2328 -0.0158 315 ILE Z CG1   
9175  C  CG2   . ILE F 315 ? 0.8729 0.3227 0.3683 -0.1239 0.223  -0.0141 315 ILE Z CG2   
9176  C  CD1   . ILE F 315 ? 0.9067 0.339  0.3798 -0.1056 0.2355 -0.0176 315 ILE Z CD1   
9177  N  N     . ARG F 316 ? 0.8726 0.3464 0.3851 -0.1265 0.2083 -0.0135 316 ARG Z N     
9178  C  CA    . ARG F 316 ? 0.8773 0.3628 0.4013 -0.1331 0.2013 -0.0115 316 ARG Z CA    
9179  C  C     . ARG F 316 ? 0.8815 0.3687 0.4102 -0.1408 0.1996 -0.0094 316 ARG Z C     
9180  O  O     . ARG F 316 ? 0.8895 0.3639 0.4073 -0.1436 0.2028 -0.0101 316 ARG Z O     
9181  C  CB    . ARG F 316 ? 0.9064 0.3854 0.4213 -0.1382 0.1965 -0.0125 316 ARG Z CB    
9182  C  CG    . ARG F 316 ? 0.9514 0.4298 0.4627 -0.1309 0.1979 -0.0142 316 ARG Z CG    
9183  C  CD    . ARG F 316 ? 0.9908 0.4676 0.4979 -0.1357 0.1922 -0.0146 316 ARG Z CD    
9184  N  NE    . ARG F 316 ? 1.0379 0.4971 0.5275 -0.1427 0.1913 -0.0158 316 ARG Z NE    
9185  C  CZ    . ARG F 316 ? 1.0754 0.5229 0.5511 -0.1426 0.1912 -0.0176 316 ARG Z CZ    
9186  N  NH1   . ARG F 316 ? 1.0657 0.5177 0.5435 -0.1358 0.1919 -0.0184 316 ARG Z NH1   
9187  N  NH2   . ARG F 316 ? 1.0902 0.5209 0.5494 -0.1494 0.1904 -0.0185 316 ARG Z NH2   
9188  N  N     . LYS F 317 ? 0.8745 0.3775 0.4192 -0.1441 0.1948 -0.0066 317 LYS Z N     
9189  C  CA    . LYS F 317 ? 0.8815 0.3881 0.4323 -0.1514 0.193  -0.004  317 LYS Z CA    
9190  C  C     . LYS F 317 ? 0.9009 0.3934 0.4378 -0.1618 0.1905 -0.0045 317 LYS Z C     
9191  O  O     . LYS F 317 ? 0.9056 0.3939 0.4409 -0.1668 0.1917 -0.0034 317 LYS Z O     
9192  C  CB    . LYS F 317 ? 0.888  0.4143 0.4581 -0.1531 0.188  -0.0004 317 LYS Z CB    
9193  C  CG    . LYS F 317 ? 0.9325 0.4638 0.5042 -0.1568 0.1815 0       317 LYS Z CG    
9194  C  CD    . LYS F 317 ? 0.9733 0.5243 0.564  -0.1572 0.1775 0.0039  317 LYS Z CD    
9195  C  CE    . LYS F 317 ? 1.0164 0.573  0.6092 -0.1588 0.1718 0.0042  317 LYS Z CE    
9196  N  NZ    . LYS F 317 ? 1.0462 0.6    0.6345 -0.1506 0.1742 0.0012  317 LYS Z NZ    
9197  N  N     . GLU F 318 ? 0.9087 0.3926 0.4343 -0.1647 0.1874 -0.0062 318 GLU Z N     
9198  C  CA    . GLU F 318 ? 0.9263 0.395  0.4364 -0.1745 0.1847 -0.007  318 GLU Z CA    
9199  C  C     . GLU F 318 ? 0.9431 0.3918 0.4352 -0.1738 0.1911 -0.0094 318 GLU Z C     
9200  O  O     . GLU F 318 ? 0.9555 0.3914 0.4356 -0.1825 0.1898 -0.0096 318 GLU Z O     
9201  C  CB    . GLU F 318 ? 0.9615 0.4262 0.4641 -0.1763 0.1803 -0.0083 318 GLU Z CB    
9202  C  CG    . GLU F 318 ? 1.0113 0.4936 0.5291 -0.1791 0.1733 -0.0058 318 GLU Z CG    
9203  C  CD    . GLU F 318 ? 1.0747 0.5726 0.6072 -0.1696 0.1742 -0.0053 318 GLU Z CD    
9204  O  OE1   . GLU F 318 ? 1.0914 0.5854 0.6203 -0.1606 0.1797 -0.0074 318 GLU Z OE1   
9205  O  OE2   . GLU F 318 ? 1.0901 0.6042 0.6375 -0.1712 0.1694 -0.0025 318 GLU Z OE2   
9206  N  N     . SER F 319 ? 0.9411 0.3867 0.4309 -0.1635 0.1979 -0.011  319 SER Z N     
9207  C  CA    . SER F 319 ? 0.9536 0.3812 0.4271 -0.1612 0.2047 -0.013  319 SER Z CA    
9208  C  C     . SER F 319 ? 0.9493 0.3817 0.4306 -0.1563 0.2101 -0.0121 319 SER Z C     
9209  O  O     . SER F 319 ? 0.9592 0.3773 0.4277 -0.1542 0.216  -0.0135 319 SER Z O     
9210  C  CB    . SER F 319 ? 0.9759 0.3938 0.4374 -0.1529 0.2089 -0.0156 319 SER Z CB    
9211  O  OG    . SER F 319 ? 1.0093 0.42   0.461  -0.157  0.2048 -0.0166 319 SER Z OG    
9212  N  N     . ARG F 320 ? 0.9336 0.3854 0.4351 -0.1538 0.2085 -0.0098 320 ARG Z N     
9213  C  CA    . ARG F 320 ? 0.9312 0.389  0.4415 -0.1487 0.2133 -0.0087 320 ARG Z CA    
9214  C  C     . ARG F 320 ? 0.9433 0.3915 0.4473 -0.1553 0.2153 -0.008  320 ARG Z C     
9215  O  O     . ARG F 320 ? 0.9507 0.3916 0.4493 -0.1504 0.2217 -0.0089 320 ARG Z O     
9216  C  CB    . ARG F 320 ? 0.9279 0.4078 0.4604 -0.1462 0.2104 -0.006  320 ARG Z CB    
9217  C  CG    . ARG F 320 ? 0.9491 0.4361 0.4918 -0.1416 0.2148 -0.0044 320 ARG Z CG    
9218  C  CD    . ARG F 320 ? 0.9708 0.4619 0.5168 -0.1299 0.2197 -0.0056 320 ARG Z CD    
9219  N  NE    . ARG F 320 ? 0.9829 0.4885 0.5453 -0.1254 0.221  -0.0034 320 ARG Z NE    
9220  C  CZ    . ARG F 320 ? 0.9954 0.5172 0.5729 -0.1232 0.2177 -0.0016 320 ARG Z CZ    
9221  N  NH1   . ARG F 320 ? 0.9913 0.5177 0.5707 -0.1259 0.2124 -0.0015 320 ARG Z NH1   
9222  N  NH2   . ARG F 320 ? 0.9816 0.5146 0.5723 -0.1189 0.2196 0.0005  320 ARG Z NH2   
9223  N  N     . ASN F 321 ? 0.9441 0.3919 0.448  -0.1665 0.2098 -0.0065 321 ASN Z N     
9224  C  CA    . ASN F 321 ? 0.9555 0.3943 0.4534 -0.174  0.2112 -0.0057 321 ASN Z CA    
9225  C  C     . ASN F 321 ? 0.9782 0.3936 0.4536 -0.1731 0.2171 -0.0087 321 ASN Z C     
9226  O  O     . ASN F 321 ? 0.9821 0.3911 0.454  -0.1712 0.2227 -0.0088 321 ASN Z O     
9227  C  CB    . ASN F 321 ? 0.9648 0.4067 0.4651 -0.1867 0.2037 -0.0035 321 ASN Z CB    
9228  C  CG    . ASN F 321 ? 0.9915 0.4456 0.5064 -0.1917 0.2023 0.0001  321 ASN Z CG    
9229  O  OD1   . ASN F 321 ? 0.9886 0.4622 0.5227 -0.1898 0.1994 0.0029  321 ASN Z OD1   
9230  N  ND2   . ASN F 321 ? 1.009  0.4513 0.5147 -0.1982 0.2044 0.0002  321 ASN Z ND2   
9231  N  N     . ASP F 322 ? 0.9917 0.3943 0.4518 -0.1736 0.2163 -0.011  322 ASP Z N     
9232  C  CA    . ASP F 322 ? 1.0174 0.397  0.4549 -0.1724 0.2221 -0.0137 322 ASP Z CA    
9233  C  C     . ASP F 322 ? 1.0191 0.3965 0.4546 -0.1596 0.2301 -0.0149 322 ASP Z C     
9234  O  O     . ASP F 322 ? 1.0309 0.3935 0.4534 -0.1579 0.2363 -0.016  322 ASP Z O     
9235  C  CB    . ASP F 322 ? 1.0558 0.4228 0.4778 -0.176  0.2191 -0.0155 322 ASP Z CB    
9236  C  CG    . ASP F 322 ? 1.1297 0.4914 0.5462 -0.1897 0.2124 -0.0147 322 ASP Z CG    
9237  O  OD1   . ASP F 322 ? 1.1396 0.4984 0.5558 -0.1971 0.2123 -0.0135 322 ASP Z OD1   
9238  O  OD2   . ASP F 322 ? 1.1685 0.5289 0.5809 -0.1933 0.2073 -0.0153 322 ASP Z OD2   
9239  N  N     . PHE F 323 ? 1.0042 0.3966 0.4527 -0.1508 0.2299 -0.0147 323 PHE Z N     
9240  C  CA    . PHE F 323 ? 1.0061 0.3992 0.4548 -0.1388 0.2368 -0.0156 323 PHE Z CA    
9241  C  C     . PHE F 323 ? 1.0075 0.4044 0.4635 -0.1369 0.241  -0.0143 323 PHE Z C     
9242  O  O     . PHE F 323 ? 1.0194 0.4044 0.4645 -0.1321 0.2478 -0.0153 323 PHE Z O     
9243  C  CB    . PHE F 323 ? 0.9925 0.4023 0.455  -0.1312 0.2348 -0.0153 323 PHE Z CB    
9244  C  CG    . PHE F 323 ? 0.995  0.411  0.4631 -0.1196 0.2407 -0.0155 323 PHE Z CG    
9245  C  CD1   . PHE F 323 ? 1.0115 0.4162 0.4662 -0.112  0.2468 -0.0171 323 PHE Z CD1   
9246  C  CD2   . PHE F 323 ? 0.9917 0.4251 0.4784 -0.1163 0.2402 -0.0137 323 PHE Z CD2   
9247  C  CE1   . PHE F 323 ? 1.0148 0.426  0.4749 -0.1016 0.2519 -0.017  323 PHE Z CE1   
9248  C  CE2   . PHE F 323 ? 0.9956 0.4343 0.4868 -0.106  0.2453 -0.0139 323 PHE Z CE2   
9249  C  CZ    . PHE F 323 ? 1.0002 0.4281 0.4783 -0.0989 0.251  -0.0155 323 PHE Z CZ    
9250  N  N     . ILE F 324 ? 0.993  0.4055 0.4666 -0.141  0.2369 -0.0119 324 ILE Z N     
9251  C  CA    . ILE F 324 ? 0.9891 0.4065 0.471  -0.1398 0.2404 -0.0104 324 ILE Z CA    
9252  C  C     . ILE F 324 ? 1.0006 0.3999 0.4673 -0.1457 0.2439 -0.0109 324 ILE Z C     
9253  O  O     . ILE F 324 ? 1.0049 0.3989 0.4683 -0.1403 0.2504 -0.0112 324 ILE Z O     
9254  C  CB    . ILE F 324 ? 0.9811 0.4189 0.4847 -0.1434 0.235  -0.0073 324 ILE Z CB    
9255  C  CG1   . ILE F 324 ? 0.9828 0.4376 0.5008 -0.1358 0.233  -0.0068 324 ILE Z CG1   
9256  C  CG2   . ILE F 324 ? 0.9832 0.4244 0.4941 -0.1436 0.2384 -0.0054 324 ILE Z CG2   
9257  C  CD1   . ILE F 324 ? 0.9982 0.4544 0.517  -0.1239 0.2392 -0.008  324 ILE Z CD1   
9258  N  N     . ASN F 325 ? 1.0044 0.3931 0.4604 -0.1563 0.24   -0.0112 325 ASN Z N     
9259  C  CA    . ASN F 325 ? 1.0173 0.3869 0.4567 -0.163  0.243  -0.0119 325 ASN Z CA    
9260  C  C     . ASN F 325 ? 1.0267 0.3778 0.4472 -0.1551 0.2512 -0.0144 325 ASN Z C     
9261  O  O     . ASN F 325 ? 1.0316 0.3726 0.4447 -0.1542 0.2569 -0.0146 325 ASN Z O     
9262  C  CB    . ASN F 325 ? 1.0375 0.398  0.4668 -0.1755 0.2369 -0.0121 325 ASN Z CB    
9263  C  CG    . ASN F 325 ? 1.0645 0.4384 0.5082 -0.1858 0.23   -0.0091 325 ASN Z CG    
9264  O  OD1   . ASN F 325 ? 1.0659 0.4538 0.5259 -0.1847 0.2304 -0.0068 325 ASN Z OD1   
9265  N  ND2   . ASN F 325 ? 1.0754 0.4454 0.5135 -0.1961 0.2235 -0.009  325 ASN Z ND2   
9266  N  N     . ASP F 326 ? 1.027  0.3745 0.4404 -0.149  0.2518 -0.0161 326 ASP Z N     
9267  C  CA    . ASP F 326 ? 1.0408 0.3722 0.4369 -0.1407 0.2594 -0.0181 326 ASP Z CA    
9268  C  C     . ASP F 326 ? 1.0379 0.3767 0.4419 -0.1295 0.2658 -0.0176 326 ASP Z C     
9269  O  O     . ASP F 326 ? 1.0481 0.373  0.439  -0.1252 0.273  -0.0184 326 ASP Z O     
9270  C  CB    . ASP F 326 ? 1.0618 0.3893 0.4499 -0.1373 0.2581 -0.0195 326 ASP Z CB    
9271  C  CG    . ASP F 326 ? 1.1177 0.4271 0.4871 -0.1463 0.2555 -0.0207 326 ASP Z CG    
9272  O  OD1   . ASP F 326 ? 1.1334 0.43   0.4928 -0.1549 0.2558 -0.0207 326 ASP Z OD1   
9273  O  OD2   . ASP F 326 ? 1.1385 0.4459 0.5028 -0.1449 0.2534 -0.0216 326 ASP Z OD2   
9274  N  N     . VAL F 327 ? 1.0223 0.3824 0.4469 -0.1248 0.2633 -0.0163 327 VAL Z N     
9275  C  CA    . VAL F 327 ? 1.0216 0.3898 0.4545 -0.1145 0.2687 -0.0158 327 VAL Z CA    
9276  C  C     . VAL F 327 ? 1.0273 0.3918 0.461  -0.1175 0.272  -0.0148 327 VAL Z C     
9277  O  O     . VAL F 327 ? 1.0347 0.392  0.4618 -0.1106 0.2791 -0.0152 327 VAL Z O     
9278  C  CB    . VAL F 327 ? 1.0157 0.4064 0.4695 -0.1094 0.265  -0.0146 327 VAL Z CB    
9279  C  CG1   . VAL F 327 ? 1.0179 0.4166 0.4801 -0.0998 0.2703 -0.014  327 VAL Z CG1   
9280  C  CG2   . VAL F 327 ? 1.0221 0.4152 0.4737 -0.1057 0.2627 -0.0157 327 VAL Z CG2   
9281  N  N     . CYS F 328 ? 1.0236 0.3923 0.4644 -0.1279 0.267  -0.0134 328 CYS Z N     
9282  C  CA    . CYS F 328 ? 1.03   0.3959 0.4724 -0.1322 0.2694 -0.0121 328 CYS Z CA    
9283  C  C     . CYS F 328 ? 1.0468 0.3888 0.4667 -0.1342 0.2752 -0.0137 328 CYS Z C     
9284  O  O     . CYS F 328 ? 1.0488 0.3858 0.4663 -0.1314 0.281  -0.0134 328 CYS Z O     
9285  C  CB    . CYS F 328 ? 1.033  0.4089 0.4874 -0.1435 0.2622 -0.0099 328 CYS Z CB    
9286  S  SG    . CYS F 328 ? 1.0574 0.462  0.5398 -0.1403 0.2569 -0.0072 328 CYS Z SG    
9287  N  N     . LYS F 329 ? 1.0579 0.3847 0.4608 -0.1389 0.274  -0.0153 329 LYS Z N     
9288  C  CA    . LYS F 329 ? 1.0828 0.3848 0.4621 -0.1408 0.2797 -0.0169 329 LYS Z CA    
9289  C  C     . LYS F 329 ? 1.0978 0.3928 0.4686 -0.1277 0.2884 -0.0179 329 LYS Z C     
9290  O  O     . LYS F 329 ? 1.1096 0.3916 0.4695 -0.126  0.295  -0.0182 329 LYS Z O     
9291  C  CB    . LYS F 329 ? 1.1096 0.3972 0.4724 -0.148  0.2762 -0.0183 329 LYS Z CB    
9292  C  CG    . LYS F 329 ? 1.1569 0.4243 0.5022 -0.1592 0.2766 -0.0189 329 LYS Z CG    
9293  C  CD    . LYS F 329 ? 1.1916 0.4697 0.5497 -0.1715 0.2692 -0.017  329 LYS Z CD    
9294  C  CE    . LYS F 329 ? 1.2399 0.4987 0.5815 -0.1829 0.2699 -0.0173 329 LYS Z CE    
9295  N  NZ    . LYS F 329 ? 1.2534 0.5246 0.6094 -0.1944 0.2633 -0.0148 329 LYS Z NZ    
9296  N  N     . LEU F 330 ? 1.0943 0.3985 0.4702 -0.1186 0.2884 -0.0182 330 LEU Z N     
9297  C  CA    . LEU F 330 ? 1.105  0.4046 0.4738 -0.106  0.296  -0.0188 330 LEU Z CA    
9298  C  C     . LEU F 330 ? 1.1075 0.4153 0.4864 -0.0993 0.3007 -0.0177 330 LEU Z C     
9299  O  O     . LEU F 330 ? 1.1145 0.4103 0.4815 -0.0931 0.3084 -0.0181 330 LEU Z O     
9300  C  CB    . LEU F 330 ? 1.0989 0.4094 0.4737 -0.0988 0.2939 -0.0191 330 LEU Z CB    
9301  C  CG    . LEU F 330 ? 1.1166 0.4251 0.4857 -0.0856 0.3011 -0.0192 330 LEU Z CG    
9302  C  CD1   . LEU F 330 ? 1.1394 0.4236 0.4835 -0.0839 0.3079 -0.0202 330 LEU Z CD1   
9303  C  CD2   . LEU F 330 ? 1.1155 0.4375 0.4934 -0.0797 0.2981 -0.0191 330 LEU Z CD2   
9304  N  N     . TYR F 331 ? 1.1    0.4278 0.5004 -0.1003 0.2963 -0.0163 331 TYR Z N     
9305  C  CA    . TYR F 331 ? 1.1063 0.4435 0.5177 -0.0936 0.3003 -0.0152 331 TYR Z CA    
9306  C  C     . TYR F 331 ? 1.1238 0.4603 0.5399 -0.1007 0.3004 -0.014  331 TYR Z C     
9307  O  O     . TYR F 331 ? 1.1186 0.4646 0.5459 -0.0958 0.303  -0.0128 331 TYR Z O     
9308  C  CB    . TYR F 331 ? 1.0892 0.4488 0.5207 -0.0876 0.2967 -0.0142 331 TYR Z CB    
9309  C  CG    . TYR F 331 ? 1.0959 0.4568 0.5232 -0.0782 0.2986 -0.0151 331 TYR Z CG    
9310  C  CD1   . TYR F 331 ? 1.1122 0.4654 0.5296 -0.0685 0.3061 -0.0155 331 TYR Z CD1   
9311  C  CD2   . TYR F 331 ? 1.0998 0.47   0.5332 -0.079  0.2928 -0.0154 331 TYR Z CD2   
9312  C  CE1   . TYR F 331 ? 1.1229 0.4786 0.5373 -0.0598 0.3078 -0.0159 331 TYR Z CE1   
9313  C  CE2   . TYR F 331 ? 1.1106 0.4826 0.5407 -0.0706 0.2945 -0.016  331 TYR Z CE2   
9314  C  CZ    . TYR F 331 ? 1.1274 0.4925 0.5483 -0.0611 0.302  -0.0161 331 TYR Z CZ    
9315  O  OH    . TYR F 331 ? 1.1457 0.5135 0.5637 -0.0528 0.3036 -0.0163 331 TYR Z OH    
9316  N  N     . ASN F 332 ? 1.1425 0.4675 0.5496 -0.1121 0.2979 -0.0142 332 ASN Z N     
9317  C  CA    . ASN F 332 ? 1.1588 0.4821 0.5691 -0.1202 0.2977 -0.0128 332 ASN Z CA    
9318  C  C     . ASN F 332 ? 1.1563 0.5022 0.591  -0.1218 0.2929 -0.0104 332 ASN Z C     
9319  O  O     . ASN F 332 ? 1.1537 0.5037 0.5958 -0.1206 0.2959 -0.009  332 ASN Z O     
9320  C  CB    . ASN F 332 ? 1.1842 0.493  0.5824 -0.1157 0.3065 -0.0133 332 ASN Z CB    
9321  C  CG    . ASN F 332 ? 1.2344 0.531  0.6248 -0.1266 0.307  -0.0128 332 ASN Z CG    
9322  O  OD1   . ASN F 332 ? 1.2535 0.5427 0.6369 -0.1376 0.3023 -0.0131 332 ASN Z OD1   
9323  N  ND2   . ASN F 332 ? 1.2448 0.5389 0.6361 -0.1239 0.3125 -0.0121 332 ASN Z ND2   
9324  N  N     . ILE F 333 ? 1.1554 0.5158 0.6023 -0.1242 0.2858 -0.0097 333 ILE Z N     
9325  C  CA    . ILE F 333 ? 1.1552 0.5368 0.6247 -0.1258 0.281  -0.0072 333 ILE Z CA    
9326  C  C     . ILE F 333 ? 1.1717 0.5529 0.6435 -0.1393 0.276  -0.0054 333 ILE Z C     
9327  O  O     . ILE F 333 ? 1.1769 0.5534 0.6423 -0.1472 0.2709 -0.006  333 ILE Z O     
9328  C  CB    . ILE F 333 ? 1.1509 0.5481 0.6322 -0.1216 0.276  -0.0071 333 ILE Z CB    
9329  C  CG1   . ILE F 333 ? 1.1615 0.5582 0.6391 -0.1089 0.2809 -0.0088 333 ILE Z CG1   
9330  C  CG2   . ILE F 333 ? 1.1433 0.5617 0.6472 -0.1229 0.2715 -0.0042 333 ILE Z CG2   
9331  C  CD1   . ILE F 333 ? 1.1697 0.5787 0.6555 -0.1051 0.2764 -0.0091 333 ILE Z CD1   
9332  N  N     . ASN F 334 ? 1.1785 0.5641 0.6586 -0.142  0.2775 -0.0033 334 ASN Z N     
9333  C  CA    . ASN F 334 ? 1.1949 0.5808 0.6778 -0.1551 0.273  -0.0012 334 ASN Z CA    
9334  C  C     . ASN F 334 ? 1.1934 0.6014 0.6998 -0.1573 0.2687 0.0027  334 ASN Z C     
9335  O  O     . ASN F 334 ? 1.1943 0.6056 0.7053 -0.1682 0.2643 0.005   334 ASN Z O     
9336  C  CB    . ASN F 334 ? 1.2222 0.5901 0.6906 -0.1593 0.2785 -0.0017 334 ASN Z CB    
9337  C  CG    . ASN F 334 ? 1.2831 0.6274 0.7266 -0.1618 0.281  -0.0048 334 ASN Z CG    
9338  O  OD1   . ASN F 334 ? 1.3086 0.6383 0.738  -0.155  0.2884 -0.0068 334 ASN Z OD1   
9339  N  ND2   . ASN F 334 ? 1.2957 0.6354 0.7327 -0.1715 0.2749 -0.0052 334 ASN Z ND2   
9340  N  N     . ASP F 335 ? 1.1892 0.612  0.7101 -0.1473 0.2701 0.0036  335 ASP Z N     
9341  C  CA    . ASP F 335 ? 1.1868 0.63   0.7295 -0.1483 0.2668 0.0074  335 ASP Z CA    
9342  C  C     . ASP F 335 ? 1.1894 0.6453 0.742  -0.1548 0.2583 0.0091  335 ASP Z C     
9343  O  O     . ASP F 335 ? 1.1898 0.6497 0.743  -0.1504 0.2558 0.0076  335 ASP Z O     
9344  C  CB    . ASP F 335 ? 1.1983 0.6522 0.752  -0.1357 0.2708 0.0077  335 ASP Z CB    
9345  C  CG    . ASP F 335 ? 1.2355 0.7071 0.8094 -0.136  0.2694 0.0119  335 ASP Z CG    
9346  O  OD1   . ASP F 335 ? 1.2408 0.71   0.8162 -0.1391 0.2724 0.0137  335 ASP Z OD1   
9347  O  OD2   . ASP F 335 ? 1.2535 0.7409 0.8413 -0.1331 0.2655 0.0135  335 ASP Z OD2   
9348  N  N     . MET F 336 ? 1.1885 0.651  0.749  -0.1652 0.2538 0.0124  336 MET Z N     
9349  C  CA    . MET F 336 ? 1.1901 0.6654 0.7607 -0.1725 0.2455 0.0148  336 MET Z CA    
9350  C  C     . MET F 336 ? 1.1704 0.6648 0.7581 -0.1646 0.2432 0.0163  336 MET Z C     
9351  O  O     . MET F 336 ? 1.1697 0.6689 0.7586 -0.1658 0.238  0.0158  336 MET Z O     
9352  C  CB    . MET F 336 ? 1.2076 0.6892 0.7864 -0.1839 0.2422 0.0189  336 MET Z CB    
9353  C  CG    . MET F 336 ? 1.2488 0.7434 0.8373 -0.1923 0.2335 0.0218  336 MET Z CG    
9354  S  SD    . MET F 336 ? 1.3406 0.849  0.9445 -0.2036 0.2297 0.0281  336 MET Z SD    
9355  C  CE    . MET F 336 ? 1.3193 0.8379 0.9281 -0.213  0.2194 0.03    336 MET Z CE    
9356  N  N     . LYS F 337 ? 1.153  0.6576 0.7532 -0.1567 0.2471 0.0181  337 LYS Z N     
9357  C  CA    . LYS F 337 ? 1.1396 0.6612 0.7553 -0.149  0.2455 0.0197  337 LYS Z CA    
9358  C  C     . LYS F 337 ? 1.138  0.6556 0.7464 -0.1409 0.2461 0.0159  337 LYS Z C     
9359  O  O     . LYS F 337 ? 1.1316 0.6594 0.7472 -0.1397 0.2416 0.0163  337 LYS Z O     
9360  C  CB    . LYS F 337 ? 1.1553 0.6853 0.7828 -0.1417 0.2506 0.0221  337 LYS Z CB    
9361  C  CG    . LYS F 337 ? 1.2007 0.7361 0.8371 -0.1488 0.2504 0.0264  337 LYS Z CG    
9362  C  CD    . LYS F 337 ? 1.2455 0.793  0.8968 -0.1412 0.2542 0.0295  337 LYS Z CD    
9363  C  CE    . LYS F 337 ? 1.2988 0.8364 0.9425 -0.1318 0.262  0.0268  337 LYS Z CE    
9364  N  NZ    . LYS F 337 ? 1.3346 0.86   0.9698 -0.1364 0.2662 0.0267  337 LYS Z NZ    
9365  N  N     . ILE F 338 ? 1.1424 0.6452 0.7364 -0.1355 0.2518 0.0123  338 ILE Z N     
9366  C  CA    . ILE F 338 ? 1.1477 0.6457 0.7336 -0.1276 0.2531 0.0088  338 ILE Z CA    
9367  C  C     . ILE F 338 ? 1.152  0.6451 0.7295 -0.1335 0.2478 0.0071  338 ILE Z C     
9368  O  O     . ILE F 338 ? 1.1507 0.6504 0.7315 -0.1293 0.2451 0.0062  338 ILE Z O     
9369  C  CB    . ILE F 338 ? 1.1646 0.6475 0.7365 -0.1213 0.2608 0.0059  338 ILE Z CB    
9370  C  CG1   . ILE F 338 ? 1.1723 0.6619 0.7536 -0.1132 0.2659 0.0073  338 ILE Z CG1   
9371  C  CG2   . ILE F 338 ? 1.1763 0.6513 0.7364 -0.1151 0.262  0.0024  338 ILE Z CG2   
9372  C  CD1   . ILE F 338 ? 1.1974 0.6732 0.766  -0.1067 0.2737 0.005   338 ILE Z CD1   
9373  N  N     . ILE F 339 ? 1.1564 0.6376 0.7226 -0.1432 0.2463 0.0066  339 ILE Z N     
9374  C  CA    . ILE F 339 ? 1.1641 0.6384 0.7204 -0.1498 0.2413 0.0051  339 ILE Z CA    
9375  C  C     . ILE F 339 ? 1.1522 0.6433 0.723  -0.1538 0.2337 0.0076  339 ILE Z C     
9376  O  O     . ILE F 339 ? 1.1529 0.6444 0.7206 -0.1529 0.2303 0.0061  339 ILE Z O     
9377  C  CB    . ILE F 339 ? 1.1825 0.6404 0.724  -0.1601 0.2414 0.0045  339 ILE Z CB    
9378  C  CG1   . ILE F 339 ? 1.2079 0.6474 0.7327 -0.1552 0.2493 0.0017  339 ILE Z CG1   
9379  C  CG2   . ILE F 339 ? 1.1948 0.6462 0.7266 -0.1681 0.2355 0.0033  339 ILE Z CG2   
9380  C  CD1   . ILE F 339 ? 1.2365 0.6592 0.7468 -0.1648 0.2505 0.0013  339 ILE Z CD1   
9381  N  N     . LYS F 340 ? 1.1397 0.645  0.7264 -0.1573 0.2313 0.0117  340 LYS Z N     
9382  C  CA    . LYS F 340 ? 1.1326 0.655  0.7342 -0.1606 0.2245 0.0148  340 LYS Z CA    
9383  C  C     . LYS F 340 ? 1.1237 0.6568 0.7338 -0.1504 0.2246 0.0142  340 LYS Z C     
9384  O  O     . LYS F 340 ? 1.1224 0.6625 0.7364 -0.1518 0.2194 0.0145  340 LYS Z O     
9385  C  CB    . LYS F 340 ? 1.15   0.6855 0.7671 -0.1655 0.2231 0.0197  340 LYS Z CB    
9386  C  CG    . LYS F 340 ? 1.1967 0.7459 0.8246 -0.1734 0.2152 0.0233  340 LYS Z CG    
9387  C  CD    . LYS F 340 ? 1.2459 0.8077 0.8885 -0.1785 0.2142 0.0287  340 LYS Z CD    
9388  C  CE    . LYS F 340 ? 1.2902 0.8627 0.9405 -0.1888 0.2063 0.0324  340 LYS Z CE    
9389  N  NZ    . LYS F 340 ? 1.3295 0.8879 0.9643 -0.2    0.2029 0.0306  340 LYS Z NZ    
9390  N  N     . GLU F 341 ? 1.1155 0.6492 0.7279 -0.1404 0.2306 0.0133  341 GLU Z N     
9391  C  CA    . GLU F 341 ? 1.1077 0.6501 0.7269 -0.1307 0.2312 0.0125  341 GLU Z CA    
9392  C  C     . GLU F 341 ? 1.1073 0.6406 0.7138 -0.1282 0.2305 0.0086  341 GLU Z C     
9393  O  O     . GLU F 341 ? 1.1046 0.6459 0.7162 -0.1256 0.2271 0.0085  341 GLU Z O     
9394  C  CB    . GLU F 341 ? 1.135  0.6784 0.7576 -0.1212 0.2378 0.0124  341 GLU Z CB    
9395  C  CG    . GLU F 341 ? 1.1885 0.7435 0.8259 -0.1217 0.2386 0.0166  341 GLU Z CG    
9396  C  CD    . GLU F 341 ? 1.256  0.8287 0.9098 -0.1218 0.2339 0.0201  341 GLU Z CD    
9397  O  OE1   . GLU F 341 ? 1.268  0.848  0.9282 -0.1134 0.2351 0.02    341 GLU Z OE1   
9398  O  OE2   . GLU F 341 ? 1.2777 0.8567 0.9376 -0.1302 0.229  0.0231  341 GLU Z OE2   
9399  N  N     . LEU F 342 ? 1.1084 0.6246 0.698  -0.1291 0.2338 0.0056  342 LEU Z N     
9400  C  CA    . LEU F 342 ? 1.1125 0.6182 0.6883 -0.1269 0.2339 0.0021  342 LEU Z CA    
9401  C  C     . LEU F 342 ? 1.1072 0.6128 0.6804 -0.1349 0.2271 0.0022  342 LEU Z C     
9402  O  O     . LEU F 342 ? 1.1126 0.6168 0.6811 -0.132  0.2256 0.0002  342 LEU Z O     
9403  C  CB    . LEU F 342 ? 1.1274 0.6138 0.685  -0.1267 0.2394 -0.0004 342 LEU Z CB    
9404  C  CG    . LEU F 342 ? 1.1466 0.6299 0.7026 -0.1174 0.2468 -0.0013 342 LEU Z CG    
9405  C  CD1   . LEU F 342 ? 1.1674 0.6313 0.7052 -0.1186 0.2518 -0.0033 342 LEU Z CD1   
9406  C  CD2   . LEU F 342 ? 1.1515 0.6397 0.7091 -0.1074 0.2483 -0.0029 342 LEU Z CD2   
9407  N  N     . LYS F 343 ? 1.0946 0.6019 0.6707 -0.1451 0.2229 0.0045  343 LYS Z N     
9408  C  CA    . LYS F 343 ? 1.0896 0.5966 0.6627 -0.1535 0.2162 0.0047  343 LYS Z CA    
9409  C  C     . LYS F 343 ? 1.0651 0.591  0.6552 -0.1545 0.2101 0.0077  343 LYS Z C     
9410  O  O     . LYS F 343 ? 1.065  0.5943 0.6571 -0.1635 0.2042 0.0096  343 LYS Z O     
9411  C  CB    . LYS F 343 ? 1.1192 0.6163 0.684  -0.165  0.2144 0.0055  343 LYS Z CB    
9412  C  CG    . LYS F 343 ? 1.1837 0.659  0.7277 -0.1653 0.2194 0.0022  343 LYS Z CG    
9413  C  CD    . LYS F 343 ? 1.245  0.7103 0.7802 -0.1776 0.217  0.0029  343 LYS Z CD    
9414  C  CE    . LYS F 343 ? 1.307  0.7494 0.8208 -0.1783 0.2224 -0.0001 343 LYS Z CE    
9415  N  NZ    . LYS F 343 ? 1.346  0.776  0.8448 -0.1731 0.2244 -0.0037 343 LYS Z NZ    
9416  N  N     . GLU F 344 ? 1.0424 0.5802 0.6439 -0.1454 0.2116 0.0082  344 GLU Z N     
9417  C  CA    . GLU F 344 ? 1.0243 0.5791 0.6409 -0.1454 0.2065 0.011   344 GLU Z CA    
9418  C  C     . GLU F 344 ? 1.0155 0.5675 0.6254 -0.1484 0.2014 0.0093  344 GLU Z C     
9419  O  O     . GLU F 344 ? 1.0266 0.567  0.6235 -0.1451 0.2035 0.0057  344 GLU Z O     
9420  C  CB    . GLU F 344 ? 1.0438 0.609  0.6712 -0.1347 0.2099 0.0114  344 GLU Z CB    
9421  C  CG    . GLU F 344 ? 1.091  0.6735 0.7341 -0.1339 0.2055 0.0147  344 GLU Z CG    
9422  C  CD    . GLU F 344 ? 1.1592 0.7521 0.814  -0.1248 0.209  0.0161  344 GLU Z CD    
9423  O  OE1   . GLU F 344 ? 1.171  0.7616 0.8267 -0.1217 0.2141 0.0164  344 GLU Z OE1   
9424  O  OE2   . GLU F 344 ? 1.1811 0.7841 0.8439 -0.1209 0.2069 0.0169  344 GLU Z OE2   
9425  N  N     . ASP F 345 ? 0.9925 0.555  0.6109 -0.1547 0.1949 0.0122  345 ASP Z N     
9426  C  CA    . ASP F 345 ? 0.9843 0.5443 0.5965 -0.158  0.1899 0.0108  345 ASP Z CA    
9427  C  C     . ASP F 345 ? 0.9632 0.5298 0.5798 -0.1496 0.1898 0.0095  345 ASP Z C     
9428  O  O     . ASP F 345 ? 0.9571 0.5369 0.5849 -0.1498 0.1856 0.0119  345 ASP Z O     
9429  C  CB    . ASP F 345 ? 1.0023 0.5703 0.6208 -0.1682 0.1827 0.0142  345 ASP Z CB    
9430  C  CG    . ASP F 345 ? 1.0643 0.6255 0.6724 -0.1734 0.1776 0.0124  345 ASP Z CG    
9431  O  OD1   . ASP F 345 ? 1.0851 0.6294 0.6762 -0.1738 0.1796 0.0086  345 ASP Z OD1   
9432  O  OD2   . ASP F 345 ? 1.0826 0.6553 0.6995 -0.1767 0.1718 0.0149  345 ASP Z OD2   
9433  N  N     . ALA F 346 ? 0.9503 0.5076 0.5574 -0.1424 0.1945 0.0059  346 ALA Z N     
9434  C  CA    . ALA F 346 ? 0.9354 0.4972 0.5447 -0.1344 0.1949 0.0044  346 ALA Z CA    
9435  C  C     . ALA F 346 ? 0.9286 0.4758 0.5223 -0.13   0.199  0.0002  346 ALA Z C     
9436  O  O     . ALA F 346 ? 0.9353 0.4703 0.5186 -0.1307 0.2029 -0.0011 346 ALA Z O     
9437  C  CB    . ALA F 346 ? 0.9281 0.5022 0.5511 -0.1266 0.1979 0.0061  346 ALA Z CB    
9438  N  N     . ASP F 347 ? 0.914  0.4621 0.5057 -0.1252 0.1983 -0.0015 347 ASP Z N     
9439  C  CA    . ASP F 347 ? 0.9122 0.448  0.4901 -0.1201 0.2023 -0.0049 347 ASP Z CA    
9440  C  C     . ASP F 347 ? 0.8909 0.4265 0.4702 -0.1122 0.2088 -0.0055 347 ASP Z C     
9441  O  O     . ASP F 347 ? 0.8825 0.4299 0.4747 -0.1083 0.2096 -0.0037 347 ASP Z O     
9442  C  CB    . ASP F 347 ? 0.9362 0.4753 0.5139 -0.1165 0.2001 -0.0062 347 ASP Z CB    
9443  C  CG    . ASP F 347 ? 0.9998 0.5368 0.5735 -0.1236 0.1942 -0.0061 347 ASP Z CG    
9444  O  OD1   . ASP F 347 ? 1.0146 0.5435 0.5812 -0.1315 0.1922 -0.0059 347 ASP Z OD1   
9445  O  OD2   . ASP F 347 ? 1.0267 0.5697 0.6038 -0.1215 0.1914 -0.0064 347 ASP Z OD2   
9446  N  N     . LEU F 348 ? 0.8807 0.4027 0.4464 -0.1098 0.2136 -0.0077 348 LEU Z N     
9447  C  CA    . LEU F 348 ? 0.8699 0.3906 0.4353 -0.1024 0.2199 -0.0082 348 LEU Z CA    
9448  C  C     . LEU F 348 ? 0.8573 0.3727 0.4141 -0.095  0.2234 -0.0105 348 LEU Z C     
9449  O  O     . LEU F 348 ? 0.8672 0.3704 0.4103 -0.0966 0.2239 -0.0122 348 LEU Z O     
9450  C  CB    . LEU F 348 ? 0.8804 0.3893 0.4371 -0.1061 0.2232 -0.0083 348 LEU Z CB    
9451  C  CG    . LEU F 348 ? 0.9019 0.4084 0.4575 -0.0992 0.2298 -0.0087 348 LEU Z CG    
9452  C  CD1   . LEU F 348 ? 0.9015 0.4223 0.4735 -0.0966 0.2299 -0.0064 348 LEU Z CD1   
9453  C  CD2   . LEU F 348 ? 0.9192 0.4105 0.462  -0.1027 0.2335 -0.0093 348 LEU Z CD2   
9454  N  N     . ILE F 349 ? 0.8326 0.3565 0.3968 -0.0871 0.2258 -0.0105 349 ILE Z N     
9455  C  CA    . ILE F 349 ? 0.8235 0.3436 0.3802 -0.0799 0.2293 -0.0122 349 ILE Z CA    
9456  C  C     . ILE F 349 ? 0.8145 0.3264 0.3639 -0.0755 0.2358 -0.0128 349 ILE Z C     
9457  O  O     . ILE F 349 ? 0.8136 0.3307 0.3704 -0.0735 0.2379 -0.0117 349 ILE Z O     
9458  C  CB    . ILE F 349 ? 0.8198 0.3533 0.3874 -0.0742 0.2281 -0.0119 349 ILE Z CB    
9459  C  CG1   . ILE F 349 ? 0.8289 0.3686 0.4014 -0.0784 0.222  -0.0116 349 ILE Z CG1   
9460  C  CG2   . ILE F 349 ? 0.8272 0.3578 0.388  -0.0665 0.2323 -0.0133 349 ILE Z CG2   
9461  C  CD1   . ILE F 349 ? 0.8375 0.3899 0.4205 -0.0738 0.2203 -0.0112 349 ILE Z CD1   
9462  N  N     . VAL F 350 ? 0.8058 0.3042 0.34   -0.0741 0.2392 -0.0142 350 VAL Z N     
9463  C  CA    . VAL F 350 ? 0.7999 0.2896 0.3258 -0.0695 0.2458 -0.0146 350 VAL Z CA    
9464  C  C     . VAL F 350 ? 0.788  0.2803 0.312  -0.0603 0.2494 -0.0152 350 VAL Z C     
9465  O  O     . VAL F 350 ? 0.7937 0.2834 0.3116 -0.059  0.2486 -0.016  350 VAL Z O     
9466  C  CB    . VAL F 350 ? 0.8163 0.2881 0.3256 -0.0739 0.2479 -0.0155 350 VAL Z CB    
9467  C  CG1   . VAL F 350 ? 0.8277 0.29   0.3272 -0.0679 0.2553 -0.0159 350 VAL Z CG1   
9468  C  CG2   . VAL F 350 ? 0.8217 0.2913 0.333  -0.0835 0.2443 -0.0148 350 VAL Z CG2   
9469  N  N     . CYS F 351 ? 0.7689 0.2669 0.2983 -0.0541 0.2531 -0.0146 351 CYS Z N     
9470  C  CA    . CYS F 351 ? 0.7608 0.2624 0.2891 -0.0455 0.2565 -0.0148 351 CYS Z CA    
9471  C  C     . CYS F 351 ? 0.7571 0.2488 0.2752 -0.0409 0.2633 -0.0148 351 CYS Z C     
9472  O  O     . CYS F 351 ? 0.7619 0.2528 0.2827 -0.0413 0.2654 -0.0143 351 CYS Z O     
9473  C  CB    . CYS F 351 ? 0.7594 0.2766 0.3025 -0.042  0.2548 -0.014  351 CYS Z CB    
9474  S  SG    . CYS F 351 ? 0.7921 0.3162 0.3352 -0.0328 0.2572 -0.014  351 CYS Z SG    
9475  N  N     . MET F 352 ? 0.7482 0.2322 0.2545 -0.0364 0.267  -0.0152 352 MET Z N     
9476  C  CA    . MET F 352 ? 0.7461 0.2204 0.2419 -0.0312 0.2738 -0.015  352 MET Z CA    
9477  C  C     . MET F 352 ? 0.7328 0.215  0.2309 -0.0221 0.2769 -0.0142 352 MET Z C     
9478  O  O     . MET F 352 ? 0.7345 0.2203 0.2315 -0.0195 0.2758 -0.0142 352 MET Z O     
9479  C  CB    . MET F 352 ? 0.7643 0.2213 0.2426 -0.0333 0.2763 -0.0157 352 MET Z CB    
9480  C  CG    . MET F 352 ? 0.7825 0.2304 0.2571 -0.0429 0.2734 -0.0163 352 MET Z CG    
9481  S  SD    . MET F 352 ? 0.7638 0.1892 0.2161 -0.0464 0.2762 -0.0173 352 MET Z SD    
9482  C  CE    . MET F 352 ? 0.7199 0.1357 0.1605 -0.0375 0.2854 -0.0167 352 MET Z CE    
9483  N  N     . LEU F 353 ? 0.7177 0.2036 0.2196 -0.0173 0.2805 -0.0135 353 LEU Z N     
9484  C  CA    . LEU F 353 ? 0.7098 0.2042 0.2145 -0.0088 0.2832 -0.0126 353 LEU Z CA    
9485  C  C     . LEU F 353 ? 0.7066 0.1947 0.2044 -0.0031 0.29   -0.0119 353 LEU Z C     
9486  O  O     . LEU F 353 ? 0.7075 0.1906 0.2053 -0.0056 0.2914 -0.0121 353 LEU Z O     
9487  C  CB    . LEU F 353 ? 0.7025 0.2126 0.2231 -0.0085 0.2794 -0.0123 353 LEU Z CB    
9488  C  CG    . LEU F 353 ? 0.7175 0.2363 0.2468 -0.0129 0.2729 -0.0128 353 LEU Z CG    
9489  C  CD1   . LEU F 353 ? 0.7143 0.2452 0.2578 -0.0135 0.2699 -0.0124 353 LEU Z CD1   
9490  C  CD2   . LEU F 353 ? 0.7286 0.2512 0.2553 -0.0093 0.2724 -0.0126 353 LEU Z CD2   
9491  N  N     . LYS F 354 ? 0.7009 0.1899 0.1932 0.0047  0.2941 -0.0108 354 LYS Z N     
9492  C  CA    . LYS F 354 ? 0.7035 0.1875 0.1895 0.011   0.3007 -0.0099 354 LYS Z CA    
9493  C  C     . LYS F 354 ? 0.6944 0.1891 0.1923 0.0129  0.3001 -0.0095 354 LYS Z C     
9494  O  O     . LYS F 354 ? 0.6932 0.1826 0.1895 0.0134  0.3034 -0.0095 354 LYS Z O     
9495  C  CB    . LYS F 354 ? 0.724  0.208  0.2022 0.0191  0.305  -0.0084 354 LYS Z CB    
9496  C  CG    . LYS F 354 ? 0.7662 0.2437 0.2362 0.0258  0.3123 -0.0072 354 LYS Z CG    
9497  C  CD    . LYS F 354 ? 0.8118 0.2869 0.2719 0.0334  0.317  -0.0053 354 LYS Z CD    
9498  C  CE    . LYS F 354 ? 0.8557 0.3221 0.3057 0.0398  0.3246 -0.004  354 LYS Z CE    
9499  N  NZ    . LYS F 354 ? 0.8724 0.3514 0.3298 0.0469  0.3263 -0.0024 354 LYS Z NZ    
9500  N  N     . GLY F 355 ? 0.6879 0.1968 0.1975 0.0136  0.2959 -0.0094 355 GLY Z N     
9501  C  CA    . GLY F 355 ? 0.6898 0.209  0.2107 0.0151  0.2948 -0.0091 355 GLY Z CA    
9502  C  C     . GLY F 355 ? 0.6976 0.2209 0.2174 0.0234  0.2992 -0.0077 355 GLY Z C     
9503  O  O     . GLY F 355 ? 0.6928 0.2279 0.2217 0.0258  0.2972 -0.0073 355 GLY Z O     
9504  N  N     . PHE F 356 ? 0.7082 0.2216 0.2167 0.0277  0.3053 -0.007  356 PHE Z N     
9505  C  CA    . PHE F 356 ? 0.7155 0.2324 0.2228 0.0357  0.3099 -0.0056 356 PHE Z CA    
9506  C  C     . PHE F 356 ? 0.7373 0.2493 0.2329 0.0422  0.3151 -0.0041 356 PHE Z C     
9507  O  O     . PHE F 356 ? 0.7474 0.2471 0.2319 0.0411  0.3177 -0.0042 356 PHE Z O     
9508  C  CB    . PHE F 356 ? 0.7093 0.22   0.2162 0.0356  0.3132 -0.0058 356 PHE Z CB    
9509  C  CG    . PHE F 356 ? 0.7046 0.2206 0.2233 0.0298  0.3087 -0.0068 356 PHE Z CG    
9510  C  CD1   . PHE F 356 ? 0.713  0.2231 0.2325 0.0219  0.3057 -0.008  356 PHE Z CD1   
9511  C  CD2   . PHE F 356 ? 0.7077 0.2349 0.2366 0.0322  0.307  -0.0064 356 PHE Z CD2   
9512  C  CE1   . PHE F 356 ? 0.7172 0.2335 0.2481 0.0168  0.3015 -0.0084 356 PHE Z CE1   
9513  C  CE2   . PHE F 356 ? 0.7117 0.2436 0.2511 0.0273  0.3031 -0.007  356 PHE Z CE2   
9514  C  CZ    . PHE F 356 ? 0.7091 0.2361 0.2498 0.0198  0.3003 -0.0078 356 PHE Z CZ    
9515  N  N     . LYS F 357 ? 0.742  0.2639 0.24   0.0491  0.3165 -0.0023 357 LYS Z N     
9516  C  CA    . LYS F 357 ? 0.7618 0.282  0.2503 0.0566  0.3216 -0.0001 357 LYS Z CA    
9517  C  C     . LYS F 357 ? 0.7834 0.2924 0.2618 0.0613  0.3288 0.0007  357 LYS Z C     
9518  O  O     . LYS F 357 ? 0.7889 0.2932 0.2693 0.0587  0.3294 -0.0005 357 LYS Z O     
9519  C  CB    . LYS F 357 ? 0.7786 0.315  0.2748 0.0614  0.3197 0.0016  357 LYS Z CB    
9520  C  CG    . LYS F 357 ? 0.8229 0.367  0.3231 0.0588  0.3149 0.0016  357 LYS Z CG    
9521  C  CD    . LYS F 357 ? 0.8665 0.4272 0.3766 0.0611  0.3115 0.0027  357 LYS Z CD    
9522  C  CE    . LYS F 357 ? 0.9096 0.4761 0.431  0.0557  0.3061 0.0007  357 LYS Z CE    
9523  N  NZ    . LYS F 357 ? 0.932  0.5133 0.462  0.0577  0.303  0.0017  357 LYS Z NZ    
9524  N  N     . PRO F 358 ? 0.7948 0.2989 0.2622 0.0683  0.3347 0.0029  358 PRO Z N     
9525  C  CA    . PRO F 358 ? 0.8055 0.2978 0.2625 0.0728  0.3418 0.0036  358 PRO Z CA    
9526  C  C     . PRO F 358 ? 0.8091 0.3058 0.2721 0.0752  0.343  0.0036  358 PRO Z C     
9527  O  O     . PRO F 358 ? 0.8213 0.3067 0.2786 0.0746  0.3468 0.0028  358 PRO Z O     
9528  C  CB    . PRO F 358 ? 0.818  0.3096 0.2653 0.0813  0.3472 0.0066  358 PRO Z CB    
9529  C  CG    . PRO F 358 ? 0.8223 0.3181 0.2706 0.0788  0.3435 0.0068  358 PRO Z CG    
9530  C  CD    . PRO F 358 ? 0.7915 0.2998 0.2549 0.0724  0.3354 0.0049  358 PRO Z CD    
9531  N  N     . ARG F 359 ? 0.7971 0.3095 0.2711 0.0776  0.3398 0.0043  359 ARG Z N     
9532  C  CA    . ARG F 359 ? 0.7952 0.3118 0.2747 0.08    0.3407 0.0043  359 ARG Z CA    
9533  C  C     . ARG F 359 ? 0.7848 0.3024 0.2742 0.0727  0.3361 0.0019  359 ARG Z C     
9534  O  O     . ARG F 359 ? 0.785  0.3063 0.2797 0.0743  0.3365 0.0019  359 ARG Z O     
9535  C  CB    . ARG F 359 ? 0.8102 0.3423 0.2958 0.0861  0.3397 0.0065  359 ARG Z CB    
9536  C  CG    . ARG F 359 ? 0.8617 0.3946 0.3385 0.094   0.3446 0.0096  359 ARG Z CG    
9537  C  CD    . ARG F 359 ? 0.9041 0.4524 0.3875 0.0954  0.3404 0.0112  359 ARG Z CD    
9538  N  NE    . ARG F 359 ? 0.938  0.4994 0.4285 0.0995  0.3393 0.0126  359 ARG Z NE    
9539  C  CZ    . ARG F 359 ? 0.9633 0.5391 0.4588 0.1019  0.3365 0.0146  359 ARG Z CZ    
9540  N  NH1   . ARG F 359 ? 0.9564 0.5359 0.4515 0.1009  0.3347 0.0156  359 ARG Z NH1   
9541  N  NH2   . ARG F 359 ? 0.9612 0.5477 0.4623 0.1052  0.3354 0.0158  359 ARG Z NH2   
9542  N  N     . GLY F 360 ? 0.7741 0.2884 0.2657 0.065   0.3319 0.0001  360 GLY Z N     
9543  C  CA    . GLY F 360 ? 0.7701 0.2858 0.2712 0.0579  0.3275 -0.0018 360 GLY Z CA    
9544  C  C     . GLY F 360 ? 0.759  0.2892 0.2728 0.0557  0.3209 -0.0021 360 GLY Z C     
9545  O  O     . GLY F 360 ? 0.7574 0.29   0.2797 0.0503  0.3172 -0.0033 360 GLY Z O     
9546  N  N     . ASP F 361 ? 0.7495 0.2897 0.2647 0.0597  0.3197 -0.0009 361 ASP Z N     
9547  C  CA    . ASP F 361 ? 0.7409 0.2943 0.267  0.0575  0.3136 -0.0012 361 ASP Z CA    
9548  C  C     . ASP F 361 ? 0.733  0.2858 0.2616 0.0505  0.3088 -0.0025 361 ASP Z C     
9549  O  O     . ASP F 361 ? 0.7363 0.2831 0.2574 0.0501  0.31   -0.0023 361 ASP Z O     
9550  C  CB    . ASP F 361 ? 0.7634 0.328  0.2902 0.0636  0.3137 0.0008  361 ASP Z CB    
9551  C  CG    . ASP F 361 ? 0.8399 0.4025 0.3575 0.0683  0.3172 0.0027  361 ASP Z CG    
9552  O  OD1   . ASP F 361 ? 0.8599 0.4113 0.3676 0.071   0.3228 0.0032  361 ASP Z OD1   
9553  O  OD2   . ASP F 361 ? 0.8702 0.4426 0.3903 0.0696  0.3147 0.0039  361 ASP Z OD2   
9554  N  N     . ASP F 362 ? 0.7206 0.2786 0.259  0.0452  0.3036 -0.0038 362 ASP Z N     
9555  C  CA    . ASP F 362 ? 0.7158 0.2733 0.2572 0.0384  0.2989 -0.005  362 ASP Z CA    
9556  C  C     . ASP F 362 ? 0.6977 0.2614 0.2388 0.0386  0.2961 -0.0046 362 ASP Z C     
9557  O  O     . ASP F 362 ? 0.6953 0.2686 0.2389 0.0427  0.2956 -0.0035 362 ASP Z O     
9558  C  CB    . ASP F 362 ? 0.7395 0.3021 0.2919 0.0334  0.2944 -0.006  362 ASP Z CB    
9559  C  CG    . ASP F 362 ? 0.7964 0.3709 0.3566 0.036   0.2919 -0.0055 362 ASP Z CG    
9560  O  OD1   . ASP F 362 ? 0.8045 0.3805 0.3649 0.0405  0.2948 -0.0048 362 ASP Z OD1   
9561  O  OD2   . ASP F 362 ? 0.8206 0.4023 0.386  0.0333  0.2873 -0.0059 362 ASP Z OD2   
9562  N  N     . ASN F 363 ? 0.6846 0.2429 0.2225 0.034   0.2943 -0.0055 363 ASN Z N     
9563  C  CA    . ASN F 363 ? 0.676  0.2385 0.213  0.0336  0.2918 -0.0052 363 ASN Z CA    
9564  C  C     . ASN F 363 ? 0.6533 0.2261 0.2012 0.0297  0.2857 -0.006  363 ASN Z C     
9565  O  O     . ASN F 363 ? 0.6541 0.2251 0.2067 0.0239  0.2824 -0.0073 363 ASN Z O     
9566  C  CB    . ASN F 363 ? 0.7057 0.2574 0.2352 0.0294  0.2918 -0.006  363 ASN Z CB    
9567  C  CG    . ASN F 363 ? 0.7739 0.3128 0.2907 0.0324  0.2979 -0.0054 363 ASN Z CG    
9568  O  OD1   . ASN F 363 ? 0.7981 0.3364 0.3108 0.0387  0.3027 -0.0041 363 ASN Z OD1   
9569  N  ND2   . ASN F 363 ? 0.7929 0.3206 0.3024 0.0281  0.2979 -0.0063 363 ASN Z ND2   
9570  N  N     . ARG F 364 ? 0.6333 0.217  0.1851 0.0327  0.2841 -0.005  364 ARG Z N     
9571  C  CA    . ARG F 364 ? 0.6159 0.2082 0.1801 0.029   0.2766 -0.0053 364 ARG Z CA    
9572  C  C     . ARG F 364 ? 0.6156 0.2066 0.1785 0.0232  0.274  -0.0068 364 ARG Z C     
9573  O  O     . ARG F 364 ? 0.615  0.2082 0.1843 0.0187  0.2706 -0.008  364 ARG Z O     
9574  C  CB    . ARG F 364 ? 0.6106 0.2136 0.179  0.0328  0.2746 -0.0037 364 ARG Z CB    
9575  C  CG    . ARG F 364 ? 0.6188 0.2316 0.1915 0.031   0.2734 -0.005  364 ARG Z CG    
9576  C  CD    . ARG F 364 ? 0.636  0.2481 0.2113 0.0329  0.2752 -0.005  364 ARG Z CD    
9577  N  NE    . ARG F 364 ? 0.6388 0.2525 0.2097 0.0393  0.2794 -0.0034 364 ARG Z NE    
9578  C  CZ    . ARG F 364 ? 0.646  0.2523 0.2111 0.0426  0.2844 -0.003  364 ARG Z CZ    
9579  N  NH1   . ARG F 364 ? 0.6404 0.2368 0.2034 0.0397  0.2857 -0.004  364 ARG Z NH1   
9580  N  NH2   . ARG F 364 ? 0.6383 0.247  0.1996 0.0487  0.288  -0.0013 364 ARG Z NH2   
9581  N  N     . PRO F 365 ? 0.611  0.1955 0.174  0.0228  0.2704 -0.0055 365 PRO Z N     
9582  C  CA    . PRO F 365 ? 0.6092 0.1922 0.1711 0.0172  0.2678 -0.0071 365 PRO Z CA    
9583  C  C     . PRO F 365 ? 0.6164 0.1933 0.1736 0.0118  0.2699 -0.0092 365 PRO Z C     
9584  O  O     . PRO F 365 ? 0.6167 0.1956 0.179  0.0067  0.2653 -0.0101 365 PRO Z O     
9585  C  CB    . PRO F 365 ? 0.62   0.1975 0.1712 0.0194  0.2709 -0.0064 365 PRO Z CB    
9586  C  CG    . PRO F 365 ? 0.625  0.2069 0.1736 0.0265  0.2747 -0.0043 365 PRO Z CG    
9587  C  CD    . PRO F 365 ? 0.6044 0.1824 0.1698 0.0275  0.2679 -0.0023 365 PRO Z CD    
9588  N  N     . ASP F 366 ? 0.6214 0.1898 0.1739 0.0126  0.2737 -0.0091 366 ASP Z N     
9589  C  CA    . ASP F 366 ? 0.6296 0.1908 0.1827 0.007   0.2727 -0.0102 366 ASP Z CA    
9590  C  C     . ASP F 366 ? 0.6249 0.1932 0.1894 0.0037  0.2689 -0.0105 366 ASP Z C     
9591  O  O     . ASP F 366 ? 0.6206 0.1863 0.188  -0.0021 0.2661 -0.0111 366 ASP Z O     
9592  C  CB    . ASP F 366 ? 0.658  0.2087 0.2032 0.0088  0.278  -0.0099 366 ASP Z CB    
9593  C  CG    . ASP F 366 ? 0.729  0.2698 0.2614 0.011   0.2819 -0.0096 366 ASP Z CG    
9594  O  OD1   . ASP F 366 ? 0.7424 0.2852 0.272  0.012   0.2808 -0.0093 366 ASP Z OD1   
9595  O  OD2   . ASP F 366 ? 0.7682 0.2986 0.2927 0.0118  0.2862 -0.0095 366 ASP Z OD2   
9596  N  N     . ARG F 367 ? 0.6246 0.2019 0.1954 0.0073  0.2687 -0.0099 367 ARG Z N     
9597  C  CA    . ARG F 367 ? 0.6302 0.214  0.2112 0.0049  0.2655 -0.01   367 ARG Z CA    
9598  C  C     . ARG F 367 ? 0.6336 0.2217 0.22   -0.0002 0.26   -0.0106 367 ARG Z C     
9599  O  O     . ARG F 367 ? 0.6358 0.2269 0.2297 -0.0034 0.2574 -0.0105 367 ARG Z O     
9600  C  CB    . ARG F 367 ? 0.6437 0.2356 0.2286 0.0099  0.2664 -0.0094 367 ARG Z CB    
9601  C  CG    . ARG F 367 ? 0.6788 0.2676 0.2592 0.0153  0.2716 -0.0086 367 ARG Z CG    
9602  C  CD    . ARG F 367 ? 0.7095 0.3069 0.2933 0.0198  0.2717 -0.008  367 ARG Z CD    
9603  N  NE    . ARG F 367 ? 0.7427 0.338  0.3239 0.0247  0.2762 -0.0072 367 ARG Z NE    
9604  C  CZ    . ARG F 367 ? 0.7826 0.3827 0.3682 0.0272  0.2764 -0.0068 367 ARG Z CZ    
9605  N  NH1   . ARG F 367 ? 0.7792 0.386  0.3718 0.0251  0.2724 -0.0071 367 ARG Z NH1   
9606  N  NH2   . ARG F 367 ? 0.7901 0.3877 0.3727 0.0318  0.2807 -0.0061 367 ARG Z NH2   
9607  N  N     . GLY F 368 ? 0.6287 0.2169 0.2112 -0.0007 0.2586 -0.011  368 GLY Z N     
9608  C  CA    . GLY F 368 ? 0.6278 0.2194 0.2143 -0.0052 0.2536 -0.0115 368 GLY Z CA    
9609  C  C     . GLY F 368 ? 0.6341 0.2179 0.2163 -0.0103 0.2522 -0.0121 368 GLY Z C     
9610  O  O     . GLY F 368 ? 0.6396 0.2258 0.225  -0.0143 0.248  -0.0126 368 GLY Z O     
9611  N  N     . ALA F 369 ? 0.6338 0.2078 0.2084 -0.0105 0.2556 -0.0122 369 ALA Z N     
9612  C  CA    . ALA F 369 ? 0.6405 0.2058 0.2094 -0.0157 0.2543 -0.0128 369 ALA Z CA    
9613  C  C     . ALA F 369 ? 0.6374 0.2039 0.2135 -0.0221 0.2503 -0.0128 369 ALA Z C     
9614  O  O     . ALA F 369 ? 0.6383 0.2049 0.2151 -0.0265 0.2464 -0.0133 369 ALA Z O     
9615  C  CB    . ALA F 369 ? 0.6502 0.2038 0.2079 -0.0144 0.2591 -0.0129 369 ALA Z CB    
9616  N  N     . LEU F 370 ? 0.6339 0.2019 0.2155 -0.0223 0.2514 -0.0122 370 LEU Z N     
9617  C  CA    . LEU F 370 ? 0.6368 0.2076 0.2265 -0.0278 0.2478 -0.0116 370 LEU Z CA    
9618  C  C     . LEU F 370 ? 0.6358 0.2169 0.2347 -0.0284 0.2434 -0.0113 370 LEU Z C     
9619  O  O     . LEU F 370 ? 0.6372 0.2192 0.2385 -0.0334 0.2394 -0.0113 370 LEU Z O     
9620  C  CB    . LEU F 370 ? 0.638  0.2081 0.2316 -0.0276 0.2503 -0.0106 370 LEU Z CB    
9621  C  CG    . LEU F 370 ? 0.6639 0.2228 0.2484 -0.0284 0.2542 -0.0108 370 LEU Z CG    
9622  C  CD1   . LEU F 370 ? 0.6721 0.2314 0.2618 -0.0289 0.2561 -0.0097 370 LEU Z CD1   
9623  C  CD2   . LEU F 370 ? 0.6782 0.229  0.2563 -0.0349 0.2519 -0.0114 370 LEU Z CD2   
9624  N  N     . PRO F 371 ? 0.631  0.2193 0.2338 -0.0236 0.2441 -0.0112 371 PRO Z N     
9625  C  CA    . PRO F 371 ? 0.6258 0.2226 0.2356 -0.0242 0.2401 -0.0111 371 PRO Z CA    
9626  C  C     . PRO F 371 ? 0.6267 0.2227 0.2332 -0.0271 0.2369 -0.0119 371 PRO Z C     
9627  O  O     . PRO F 371 ? 0.6258 0.2262 0.2379 -0.0302 0.233  -0.0117 371 PRO Z O     
9628  C  CB    . PRO F 371 ? 0.6334 0.2354 0.2441 -0.0184 0.2422 -0.0111 371 PRO Z CB    
9629  C  CG    . PRO F 371 ? 0.6407 0.2392 0.2494 -0.0152 0.2466 -0.0106 371 PRO Z CG    
9630  C  CD    . PRO F 371 ? 0.6254 0.2144 0.2262 -0.0174 0.2483 -0.0111 371 PRO Z CD    
9631  N  N     . LEU F 372 ? 0.6273 0.2171 0.2244 -0.026  0.2387 -0.0127 372 LEU Z N     
9632  C  CA    . LEU F 372 ? 0.631  0.2188 0.2239 -0.0284 0.236  -0.0135 372 LEU Z CA    
9633  C  C     . LEU F 372 ? 0.6319 0.2154 0.225  -0.035  0.2329 -0.0135 372 LEU Z C     
9634  O  O     . LEU F 372 ? 0.6338 0.2205 0.23   -0.0382 0.2288 -0.0136 372 LEU Z O     
9635  C  CB    . LEU F 372 ? 0.6386 0.2197 0.2207 -0.0252 0.2395 -0.014  372 LEU Z CB    
9636  C  CG    . LEU F 372 ? 0.6577 0.2342 0.2332 -0.0276 0.2377 -0.0146 372 LEU Z CG    
9637  C  CD1   . LEU F 372 ? 0.6612 0.2459 0.2415 -0.0272 0.2345 -0.0148 372 LEU Z CD1   
9638  C  CD2   . LEU F 372 ? 0.6686 0.2376 0.2331 -0.024  0.242  -0.0146 372 LEU Z CD2   
9639  N  N     . VAL F 373 ? 0.6278 0.2043 0.2177 -0.0372 0.2347 -0.0132 373 VAL Z N     
9640  C  CA    . VAL F 373 ? 0.6293 0.2018 0.2194 -0.0439 0.2318 -0.013  373 VAL Z CA    
9641  C  C     . VAL F 373 ? 0.6242 0.2061 0.2262 -0.0467 0.2278 -0.0118 373 VAL Z C     
9642  O  O     . VAL F 373 ? 0.6254 0.2086 0.2293 -0.0513 0.2236 -0.0116 373 VAL Z O     
9643  C  CB    . VAL F 373 ? 0.6423 0.2064 0.2274 -0.0453 0.2351 -0.0128 373 VAL Z CB    
9644  C  CG1   . VAL F 373 ? 0.6493 0.2111 0.2364 -0.0527 0.2318 -0.0121 373 VAL Z CG1   
9645  C  CG2   . VAL F 373 ? 0.6571 0.2105 0.229  -0.0429 0.239  -0.0138 373 VAL Z CG2   
9646  N  N     . ALA F 374 ? 0.6174 0.2059 0.2272 -0.0434 0.2293 -0.0108 374 ALA Z N     
9647  C  CA    . ALA F 374 ? 0.6137 0.211  0.2347 -0.0448 0.2265 -0.0092 374 ALA Z CA    
9648  C  C     . ALA F 374 ? 0.61   0.2136 0.2343 -0.0444 0.2231 -0.0095 374 ALA Z C     
9649  O  O     . ALA F 374 ? 0.6059 0.2145 0.2369 -0.0475 0.2196 -0.0084 374 ALA Z O     
9650  C  CB    . ALA F 374 ? 0.6115 0.2128 0.2379 -0.0405 0.2297 -0.0083 374 ALA Z CB    
9651  N  N     . MET F 375 ? 0.6089 0.2125 0.2286 -0.0406 0.2242 -0.0109 375 MET Z N     
9652  C  CA    . MET F 375 ? 0.6136 0.2224 0.2355 -0.0403 0.2213 -0.0113 375 MET Z CA    
9653  C  C     . MET F 375 ? 0.622  0.2275 0.2402 -0.0449 0.2178 -0.0118 375 MET Z C     
9654  O  O     . MET F 375 ? 0.6219 0.2321 0.2442 -0.0465 0.2143 -0.0116 375 MET Z O     
9655  C  CB    . MET F 375 ? 0.6233 0.2334 0.2414 -0.0351 0.2236 -0.0122 375 MET Z CB    
9656  C  CG    . MET F 375 ? 0.6483 0.2633 0.2711 -0.0308 0.2259 -0.0116 375 MET Z CG    
9657  S  SD    . MET F 375 ? 0.7066 0.3233 0.3244 -0.0252 0.2285 -0.0125 375 MET Z SD    
9658  C  CE    . MET F 375 ? 0.6968 0.3184 0.316  -0.0267 0.2245 -0.013  375 MET Z CE    
9659  N  N     . LEU F 376 ? 0.6254 0.2222 0.2353 -0.0471 0.2188 -0.0125 376 LEU Z N     
9660  C  CA    . LEU F 376 ? 0.6306 0.2228 0.2355 -0.0516 0.2156 -0.0131 376 LEU Z CA    
9661  C  C     . LEU F 376 ? 0.6344 0.2272 0.2439 -0.0577 0.212  -0.0119 376 LEU Z C     
9662  O  O     . LEU F 376 ? 0.6351 0.2305 0.2468 -0.0609 0.208  -0.0117 376 LEU Z O     
9663  C  CB    . LEU F 376 ? 0.6376 0.219  0.2304 -0.0513 0.2184 -0.0143 376 LEU Z CB    
9664  C  CG    . LEU F 376 ? 0.6548 0.2352 0.2417 -0.0461 0.2212 -0.0152 376 LEU Z CG    
9665  C  CD1   . LEU F 376 ? 0.6657 0.2353 0.241  -0.0449 0.225  -0.0158 376 LEU Z CD1   
9666  C  CD2   . LEU F 376 ? 0.6643 0.2473 0.2509 -0.0468 0.2181 -0.0157 376 LEU Z CD2   
9667  N  N     . ALA F 377 ? 0.6354 0.2262 0.2464 -0.0595 0.2135 -0.011  377 ALA Z N     
9668  C  CA    . ALA F 377 ? 0.6413 0.2327 0.2563 -0.0657 0.2102 -0.0095 377 ALA Z CA    
9669  C  C     . ALA F 377 ? 0.6423 0.2426 0.2692 -0.0657 0.2097 -0.0071 377 ALA Z C     
9670  O  O     . ALA F 377 ? 0.6429 0.2444 0.2737 -0.0707 0.2076 -0.0054 377 ALA Z O     
9671  C  CB    . ALA F 377 ? 0.648  0.2288 0.2542 -0.0695 0.2115 -0.0099 377 ALA Z CB    
9672  N  N     . GLY F 378 ? 0.6418 0.2482 0.2742 -0.0602 0.2118 -0.0068 378 GLY Z N     
9673  C  CA    . GLY F 378 ? 0.6454 0.2595 0.2883 -0.0593 0.2121 -0.0045 378 GLY Z CA    
9674  C  C     . GLY F 378 ? 0.6538 0.2649 0.2965 -0.058  0.216  -0.0039 378 GLY Z C     
9675  O  O     . GLY F 378 ? 0.6611 0.2646 0.2974 -0.0609 0.2171 -0.0045 378 GLY Z O     
9676  N  N     . GLU F 379 ? 0.6504 0.2667 0.2995 -0.0536 0.2185 -0.0028 379 GLU Z N     
9677  C  CA    . GLU F 379 ? 0.6578 0.2716 0.3072 -0.0517 0.2226 -0.0022 379 GLU Z CA    
9678  C  C     . GLU F 379 ? 0.6644 0.2777 0.3174 -0.0571 0.2218 -0.0001 379 GLU Z C     
9679  O  O     . GLU F 379 ? 0.6699 0.278  0.3199 -0.0571 0.2249 -0.0001 379 GLU Z O     
9680  C  CB    . GLU F 379 ? 0.6743 0.2938 0.3297 -0.046  0.225  -0.0013 379 GLU Z CB    
9681  C  CG    . GLU F 379 ? 0.713  0.3412 0.3788 -0.0467 0.2226 0.0013  379 GLU Z CG    
9682  C  CD    . GLU F 379 ? 0.7776 0.4101 0.448  -0.041  0.2252 0.0022  379 GLU Z CD    
9683  O  OE1   . GLU F 379 ? 0.7911 0.4221 0.457  -0.0367 0.2269 0.0003  379 GLU Z OE1   
9684  O  OE2   . GLU F 379 ? 0.7998 0.437  0.4781 -0.0408 0.2257 0.005   379 GLU Z OE2   
9685  N  N     . ASN F 380 ? 0.6618 0.2803 0.3207 -0.0617 0.2175 0.0018  380 ASN Z N     
9686  C  CA    . ASN F 380 ? 0.6639 0.2837 0.3273 -0.0677 0.2157 0.0042  380 ASN Z CA    
9687  C  C     . ASN F 380 ? 0.6625 0.2728 0.3165 -0.0734 0.2149 0.0028  380 ASN Z C     
9688  O  O     . ASN F 380 ? 0.6627 0.2725 0.3188 -0.0786 0.2141 0.0047  380 ASN Z O     
9689  C  CB    . ASN F 380 ? 0.6792 0.3086 0.3518 -0.0705 0.2111 0.0069  380 ASN Z CB    
9690  C  CG    . ASN F 380 ? 0.7273 0.3574 0.397  -0.0706 0.2077 0.0053  380 ASN Z CG    
9691  O  OD1   . ASN F 380 ? 0.7526 0.3756 0.4133 -0.0732 0.2064 0.003   380 ASN Z OD1   
9692  N  ND2   . ASN F 380 ? 0.7261 0.3642 0.4027 -0.0677 0.2065 0.0066  380 ASN Z ND2   
9693  N  N     . ALA F 381 ? 0.6607 0.2631 0.304  -0.0727 0.2152 -0.0002 381 ALA Z N     
9694  C  CA    . ALA F 381 ? 0.6699 0.2616 0.3025 -0.0777 0.2148 -0.0016 381 ALA Z CA    
9695  C  C     . ALA F 381 ? 0.6749 0.2594 0.303  -0.0775 0.2193 -0.0018 381 ALA Z C     
9696  O  O     . ALA F 381 ? 0.6764 0.262  0.3062 -0.0715 0.2235 -0.0019 381 ALA Z O     
9697  C  CB    . ALA F 381 ? 0.6782 0.2632 0.3003 -0.0756 0.215  -0.0045 381 ALA Z CB    
9698  N  N     . GLN F 382 ? 0.6746 0.2514 0.2967 -0.084  0.2184 -0.0017 382 GLN Z N     
9699  C  CA    . GLN F 382 ? 0.679  0.2479 0.296  -0.0844 0.2228 -0.0018 382 GLN Z CA    
9700  C  C     . GLN F 382 ? 0.6854 0.2426 0.2888 -0.0802 0.227  -0.0047 382 GLN Z C     
9701  O  O     . GLN F 382 ? 0.6943 0.2435 0.2876 -0.0827 0.2257 -0.0064 382 GLN Z O     
9702  C  CB    . GLN F 382 ? 0.6997 0.2647 0.3152 -0.0933 0.2203 -0.0004 382 GLN Z CB    
9703  C  CG    . GLN F 382 ? 0.7329 0.3105 0.3629 -0.0969 0.2168 0.0032  382 GLN Z CG    
9704  C  CD    . GLN F 382 ? 0.7947 0.3691 0.424  -0.1054 0.2152 0.005   382 GLN Z CD    
9705  O  OE1   . GLN F 382 ? 0.8263 0.3898 0.4466 -0.1072 0.2184 0.0039  382 GLN Z OE1   
9706  N  NE2   . GLN F 382 ? 0.7922 0.3761 0.431  -0.1109 0.2101 0.0079  382 GLN Z NE2   
9707  N  N     . ILE F 383 ? 0.6806 0.2371 0.2837 -0.0736 0.2322 -0.0051 383 ILE Z N     
9708  C  CA    . ILE F 383 ? 0.6907 0.2377 0.2819 -0.0686 0.2367 -0.0074 383 ILE Z CA    
9709  C  C     . ILE F 383 ? 0.6975 0.2346 0.2814 -0.0684 0.2417 -0.0076 383 ILE Z C     
9710  O  O     . ILE F 383 ? 0.6986 0.2397 0.2894 -0.0669 0.2439 -0.0062 383 ILE Z O     
9711  C  CB    . ILE F 383 ? 0.6939 0.2481 0.289  -0.0604 0.2384 -0.008  383 ILE Z CB    
9712  C  CG1   . ILE F 383 ? 0.7044 0.267  0.3053 -0.061  0.2335 -0.0079 383 ILE Z CG1   
9713  C  CG2   . ILE F 383 ? 0.7059 0.2519 0.2896 -0.0548 0.243  -0.0098 383 ILE Z CG2   
9714  C  CD1   . ILE F 383 ? 0.7182 0.2897 0.3254 -0.0543 0.2343 -0.008  383 ILE Z CD1   
9715  N  N     . PHE F 384 ? 0.7004 0.2243 0.2701 -0.0697 0.2438 -0.0092 384 PHE Z N     
9716  C  CA    . PHE F 384 ? 0.708  0.22   0.2679 -0.0695 0.2489 -0.0097 384 PHE Z CA    
9717  C  C     . PHE F 384 ? 0.7097 0.2171 0.2612 -0.0611 0.2539 -0.0111 384 PHE Z C     
9718  O  O     . PHE F 384 ? 0.7175 0.2191 0.26   -0.0603 0.2537 -0.0124 384 PHE Z O     
9719  C  CB    . PHE F 384 ? 0.7144 0.2136 0.2625 -0.0773 0.2473 -0.0104 384 PHE Z CB    
9720  C  CG    . PHE F 384 ? 0.7283 0.2133 0.2646 -0.0791 0.252  -0.0109 384 PHE Z CG    
9721  C  CD1   . PHE F 384 ? 0.7376 0.2221 0.2779 -0.0847 0.2518 -0.0094 384 PHE Z CD1   
9722  C  CD2   . PHE F 384 ? 0.7477 0.219  0.2682 -0.0758 0.2564 -0.0126 384 PHE Z CD2   
9723  C  CE1   . PHE F 384 ? 0.756  0.2267 0.2849 -0.0866 0.2561 -0.0099 384 PHE Z CE1   
9724  C  CE2   . PHE F 384 ? 0.7671 0.2241 0.2757 -0.0774 0.2609 -0.013  384 PHE Z CE2   
9725  C  CZ    . PHE F 384 ? 0.7639 0.2203 0.2763 -0.0832 0.2606 -0.0118 384 PHE Z CZ    
9726  N  N     . THR F 385 ? 0.699  0.2095 0.2539 -0.0547 0.2582 -0.0107 385 THR Z N     
9727  C  CA    . THR F 385 ? 0.7032 0.2114 0.2515 -0.0463 0.2629 -0.0116 385 THR Z CA    
9728  C  C     . THR F 385 ? 0.7051 0.1999 0.2409 -0.0442 0.269  -0.012  385 THR Z C     
9729  O  O     . THR F 385 ? 0.711  0.2051 0.2494 -0.0439 0.2717 -0.0113 385 THR Z O     
9730  C  CB    . THR F 385 ? 0.7201 0.2411 0.2801 -0.0402 0.2634 -0.0107 385 THR Z CB    
9731  O  OG1   . THR F 385 ? 0.7268 0.259  0.2973 -0.042  0.258  -0.0103 385 THR Z OG1   
9732  C  CG2   . THR F 385 ? 0.7314 0.2519 0.286  -0.0316 0.2678 -0.0113 385 THR Z CG2   
9733  N  N     . PHE F 386 ? 0.7004 0.1847 0.2225 -0.0424 0.2716 -0.0131 386 PHE Z N     
9734  C  CA    . PHE F 386 ? 0.704  0.1742 0.2123 -0.0398 0.2779 -0.0135 386 PHE Z CA    
9735  C  C     . PHE F 386 ? 0.711  0.1829 0.2159 -0.0297 0.2829 -0.0133 386 PHE Z C     
9736  O  O     . PHE F 386 ? 0.7106 0.1849 0.213  -0.0263 0.2823 -0.0136 386 PHE Z O     
9737  C  CB    . PHE F 386 ? 0.7018 0.1571 0.1953 -0.0449 0.2778 -0.0145 386 PHE Z CB    
9738  C  CG    . PHE F 386 ? 0.7091 0.1481 0.1867 -0.0426 0.2845 -0.0148 386 PHE Z CG    
9739  C  CD1   . PHE F 386 ? 0.7192 0.1488 0.1923 -0.0478 0.2861 -0.0148 386 PHE Z CD1   
9740  C  CD2   . PHE F 386 ? 0.7192 0.1518 0.1855 -0.0355 0.2891 -0.015  386 PHE Z CD2   
9741  C  CE1   . PHE F 386 ? 0.7353 0.1488 0.1926 -0.0457 0.2925 -0.0151 386 PHE Z CE1   
9742  C  CE2   . PHE F 386 ? 0.734  0.151  0.1849 -0.0329 0.2957 -0.0151 386 PHE Z CE2   
9743  C  CZ    . PHE F 386 ? 0.7363 0.1433 0.1823 -0.0381 0.2974 -0.0153 386 PHE Z CZ    
9744  N  N     . ILE F 387 ? 0.7145 0.1853 0.2193 -0.0251 0.2878 -0.0127 387 ILE Z N     
9745  C  CA    . ILE F 387 ? 0.7268 0.2001 0.2292 -0.0155 0.2927 -0.0123 387 ILE Z CA    
9746  C  C     . ILE F 387 ? 0.7527 0.2108 0.2395 -0.0122 0.2996 -0.0123 387 ILE Z C     
9747  O  O     . ILE F 387 ? 0.7599 0.2088 0.2425 -0.0161 0.3016 -0.0124 387 ILE Z O     
9748  C  CB    . ILE F 387 ? 0.7251 0.2108 0.2408 -0.0121 0.2925 -0.0114 387 ILE Z CB    
9749  C  CG1   . ILE F 387 ? 0.7298 0.2293 0.2601 -0.0156 0.2859 -0.0113 387 ILE Z CG1   
9750  C  CG2   . ILE F 387 ? 0.7292 0.2187 0.2432 -0.0025 0.297  -0.0107 387 ILE Z CG2   
9751  C  CD1   . ILE F 387 ? 0.7444 0.25   0.2754 -0.0142 0.2826 -0.0117 387 ILE Z CD1   
9752  N  N     . TYR F 388 ? 0.7632 0.2187 0.2415 -0.0051 0.3035 -0.0119 388 TYR Z N     
9753  C  CA    . TYR F 388 ? 0.7832 0.2236 0.2456 -0.0013 0.3105 -0.0116 388 TYR Z CA    
9754  C  C     . TYR F 388 ? 0.7861 0.2299 0.2459 0.0093  0.3161 -0.0103 388 TYR Z C     
9755  O  O     . TYR F 388 ? 0.7949 0.2266 0.2409 0.0135  0.3223 -0.0098 388 TYR Z O     
9756  C  CB    . TYR F 388 ? 0.7985 0.2259 0.2469 -0.0043 0.3108 -0.0123 388 TYR Z CB    
9757  C  CG    . TYR F 388 ? 0.8105 0.2452 0.2607 -0.0022 0.3078 -0.0121 388 TYR Z CG    
9758  C  CD1   . TYR F 388 ? 0.8174 0.2593 0.2761 -0.0085 0.3008 -0.0129 388 TYR Z CD1   
9759  C  CD2   . TYR F 388 ? 0.8263 0.2607 0.2694 0.0063  0.3122 -0.0109 388 TYR Z CD2   
9760  C  CE1   . TYR F 388 ? 0.8259 0.2742 0.2861 -0.0066 0.2982 -0.0127 388 TYR Z CE1   
9761  C  CE2   . TYR F 388 ? 0.8339 0.2753 0.279  0.0082  0.3096 -0.0105 388 TYR Z CE2   
9762  C  CZ    . TYR F 388 ? 0.8414 0.2896 0.295  0.0017  0.3026 -0.0115 388 TYR Z CZ    
9763  O  OH    . TYR F 388 ? 0.8646 0.3198 0.3202 0.0036  0.3002 -0.0111 388 TYR Z OH    
9764  N  N     . GLY F 389 ? 0.7778 0.2372 0.2501 0.0134  0.3141 -0.0096 389 GLY Z N     
9765  C  CA    . GLY F 389 ? 0.7811 0.2458 0.2524 0.023   0.3185 -0.0081 389 GLY Z CA    
9766  C  C     . GLY F 389 ? 0.7799 0.2428 0.2515 0.0266  0.323  -0.0076 389 GLY Z C     
9767  O  O     . GLY F 389 ? 0.7808 0.2415 0.2568 0.0215  0.3219 -0.0083 389 GLY Z O     
9768  N  N     . PRO F 390 ? 0.7762 0.2405 0.2435 0.0354  0.3282 -0.0061 390 PRO Z N     
9769  C  CA    . PRO F 390 ? 0.7794 0.2409 0.2458 0.0393  0.333  -0.0056 390 PRO Z CA    
9770  C  C     . PRO F 390 ? 0.776  0.25   0.2572 0.0389  0.3299 -0.0057 390 PRO Z C     
9771  O  O     . PRO F 390 ? 0.7752 0.2629 0.2658 0.0411  0.3264 -0.0052 390 PRO Z O     
9772  C  CB    . PRO F 390 ? 0.7896 0.2503 0.2474 0.0492  0.339  -0.0036 390 PRO Z CB    
9773  C  CG    . PRO F 390 ? 0.7952 0.2557 0.2475 0.05    0.338  -0.0031 390 PRO Z CG    
9774  C  CD    . PRO F 390 ? 0.7694 0.2371 0.2315 0.0424  0.3304 -0.0045 390 PRO Z CD    
9775  N  N     . LEU F 391 ? 0.7726 0.2412 0.255  0.0362  0.3315 -0.0061 391 LEU Z N     
9776  C  CA    . LEU F 391 ? 0.7674 0.246  0.2627 0.036   0.3292 -0.006  391 LEU Z CA    
9777  C  C     . LEU F 391 ? 0.7692 0.2471 0.2621 0.0434  0.3349 -0.005  391 LEU Z C     
9778  O  O     . LEU F 391 ? 0.7766 0.2422 0.2585 0.0455  0.3407 -0.0047 391 LEU Z O     
9779  C  CB    . LEU F 391 ? 0.7717 0.2463 0.2718 0.0275  0.3267 -0.0069 391 LEU Z CB    
9780  C  CG    . LEU F 391 ? 0.7945 0.2699 0.2979 0.0192  0.3208 -0.0079 391 LEU Z CG    
9781  C  CD1   . LEU F 391 ? 0.8037 0.2761 0.3123 0.0113  0.3187 -0.0082 391 LEU Z CD1   
9782  C  CD2   . LEU F 391 ? 0.7962 0.2864 0.3106 0.0196  0.3151 -0.0078 391 LEU Z CD2   
9783  N  N     . ILE F 392 ? 0.7591 0.2494 0.262  0.0471  0.3332 -0.0044 392 ILE Z N     
9784  C  CA    . ILE F 392 ? 0.7594 0.2499 0.2613 0.0538  0.338  -0.0034 392 ILE Z CA    
9785  C  C     . ILE F 392 ? 0.7649 0.2488 0.2693 0.0495  0.3393 -0.0039 392 ILE Z C     
9786  O  O     . ILE F 392 ? 0.7612 0.2469 0.2731 0.0421  0.3348 -0.0047 392 ILE Z O     
9787  C  CB    . ILE F 392 ? 0.7533 0.2588 0.2648 0.0582  0.3352 -0.0026 392 ILE Z CB    
9788  C  CG1   . ILE F 392 ? 0.7545 0.2691 0.2792 0.0522  0.3286 -0.0034 392 ILE Z CG1   
9789  C  CG2   . ILE F 392 ? 0.7572 0.2687 0.2651 0.0631  0.3349 -0.0016 392 ILE Z CG2   
9790  C  CD1   . ILE F 392 ? 0.7615 0.289  0.2949 0.0556  0.3258 -0.0029 392 ILE Z CD1   
9791  N  N     . LYS F 393 ? 0.7727 0.2489 0.2705 0.054   0.3454 -0.0033 393 LYS Z N     
9792  C  CA    . LYS F 393 ? 0.7816 0.2509 0.281  0.0501  0.3473 -0.0036 393 LYS Z CA    
9793  C  C     . LYS F 393 ? 0.7845 0.2644 0.2988 0.0469  0.3428 -0.0035 393 LYS Z C     
9794  O  O     . LYS F 393 ? 0.7893 0.2664 0.3081 0.0402  0.3412 -0.0038 393 LYS Z O     
9795  C  CB    . LYS F 393 ? 0.801  0.2616 0.2913 0.0567  0.3549 -0.0029 393 LYS Z CB    
9796  C  CG    . LYS F 393 ? 0.8441 0.2961 0.3345 0.0527  0.3576 -0.0031 393 LYS Z CG    
9797  C  CD    . LYS F 393 ? 0.8928 0.3334 0.3774 0.0442  0.3569 -0.004  393 LYS Z CD    
9798  C  CE    . LYS F 393 ? 0.9387 0.3627 0.4083 0.0459  0.3642 -0.004  393 LYS Z CE    
9799  N  NZ    . LYS F 393 ? 0.9611 0.3815 0.4324 0.0471  0.3682 -0.0035 393 LYS Z NZ    
9800  N  N     . GLY F 394 ? 0.7777 0.2697 0.2995 0.0514  0.3405 -0.003  394 GLY Z N     
9801  C  CA    . GLY F 394 ? 0.78   0.2815 0.3148 0.0491  0.3365 -0.0028 394 GLY Z CA    
9802  C  C     . GLY F 394 ? 0.7875 0.2934 0.33   0.041   0.3302 -0.0034 394 GLY Z C     
9803  O  O     . GLY F 394 ? 0.7869 0.296  0.3386 0.037   0.328  -0.003  394 GLY Z O     
9804  N  N     . ALA F 395 ? 0.7908 0.297  0.3298 0.0388  0.3274 -0.0041 395 ALA Z N     
9805  C  CA    . ALA F 395 ? 0.7936 0.3036 0.3389 0.0313  0.3214 -0.0047 395 ALA Z CA    
9806  C  C     . ALA F 395 ? 0.8042 0.3055 0.348  0.0238  0.3214 -0.0049 395 ALA Z C     
9807  O  O     . ALA F 395 ? 0.8004 0.3065 0.3537 0.0181  0.3174 -0.0046 395 ALA Z O     
9808  C  CB    . ALA F 395 ? 0.7945 0.3065 0.3354 0.0315  0.319  -0.0053 395 ALA Z CB    
9809  N  N     . ILE F 396 ? 0.8168 0.3052 0.3486 0.0238  0.3261 -0.0053 396 ILE Z N     
9810  C  CA    . ILE F 396 ? 0.8335 0.3125 0.3627 0.0162  0.3262 -0.0055 396 ILE Z CA    
9811  C  C     . ILE F 396 ? 0.8434 0.3234 0.3802 0.0146  0.3276 -0.0044 396 ILE Z C     
9812  O  O     . ILE F 396 ? 0.8461 0.3258 0.3881 0.0071  0.3248 -0.0041 396 ILE Z O     
9813  C  CB    . ILE F 396 ? 0.8503 0.3139 0.3634 0.0161  0.3309 -0.0062 396 ILE Z CB    
9814  C  CG1   . ILE F 396 ? 0.8646 0.3196 0.3747 0.0063  0.3288 -0.0067 396 ILE Z CG1   
9815  C  CG2   . ILE F 396 ? 0.8613 0.3172 0.3665 0.0227  0.3383 -0.0057 396 ILE Z CG2   
9816  C  CD1   . ILE F 396 ? 0.8738 0.3354 0.3898 0.0002  0.3218 -0.0072 396 ILE Z CD1   
9817  N  N     . ASN F 397 ? 0.8452 0.3276 0.3835 0.0217  0.3314 -0.0038 397 ASN Z N     
9818  C  CA    . ASN F 397 ? 0.8498 0.3338 0.3956 0.0212  0.3329 -0.0026 397 ASN Z CA    
9819  C  C     . ASN F 397 ? 0.8458 0.3422 0.4062 0.0177  0.3272 -0.0017 397 ASN Z C     
9820  O  O     . ASN F 397 ? 0.8457 0.3428 0.413  0.0127  0.3263 -0.0006 397 ASN Z O     
9821  C  CB    . ASN F 397 ? 0.8668 0.3503 0.4099 0.0301  0.3382 -0.0021 397 ASN Z CB    
9822  C  CG    . ASN F 397 ? 0.9198 0.3898 0.449  0.0331  0.3448 -0.0025 397 ASN Z CG    
9823  O  OD1   . ASN F 397 ? 0.9404 0.3998 0.4621 0.0278  0.3461 -0.003  397 ASN Z OD1   
9824  N  ND2   . ASN F 397 ? 0.9315 0.4013 0.4563 0.0417  0.3493 -0.0021 397 ASN Z ND2   
9825  N  N     . LEU F 398 ? 0.8415 0.3476 0.4065 0.02    0.3233 -0.0021 398 LEU Z N     
9826  C  CA    . LEU F 398 ? 0.841  0.3583 0.4188 0.0171  0.3179 -0.0013 398 LEU Z CA    
9827  C  C     . LEU F 398 ? 0.841  0.3585 0.422  0.0082  0.3132 -0.0013 398 LEU Z C     
9828  O  O     . LEU F 398 ? 0.8384 0.3623 0.4298 0.0042  0.3101 0.0001  398 LEU Z O     
9829  C  CB    . LEU F 398 ? 0.8433 0.3699 0.4238 0.0218  0.3151 -0.0018 398 LEU Z CB    
9830  C  CG    . LEU F 398 ? 0.8645 0.3959 0.4481 0.0289  0.3174 -0.0011 398 LEU Z CG    
9831  C  CD1   . LEU F 398 ? 0.87   0.4103 0.4557 0.0322  0.314  -0.0016 398 LEU Z CD1   
9832  C  CD2   . LEU F 398 ? 0.8689 0.4039 0.4625 0.0273  0.3172 0.0005  398 LEU Z CD2   
9833  N  N     . ILE F 399 ? 0.8408 0.3511 0.4126 0.0052  0.3127 -0.0026 399 ILE Z N     
9834  C  CA    . ILE F 399 ? 0.8401 0.3492 0.4132 -0.0035 0.3084 -0.0027 399 ILE Z CA    
9835  C  C     . ILE F 399 ? 0.835  0.3395 0.4106 -0.0094 0.3096 -0.0014 399 ILE Z C     
9836  O  O     . ILE F 399 ? 0.8329 0.3424 0.4167 -0.016  0.3053 -0.0002 399 ILE Z O     
9837  C  CB    . ILE F 399 ? 0.8567 0.357  0.4171 -0.0045 0.3087 -0.0044 399 ILE Z CB    
9838  C  CG1   . ILE F 399 ? 0.8659 0.3736 0.427  -0.0008 0.3058 -0.0052 399 ILE Z CG1   
9839  C  CG2   . ILE F 399 ? 0.8674 0.3615 0.425  -0.0138 0.3059 -0.0046 399 ILE Z CG2   
9840  C  CD1   . ILE F 399 ? 0.8891 0.3889 0.4375 0.0013  0.3077 -0.0064 399 ILE Z CD1   
9841  N  N     . ASP F 400 ? 0.8322 0.3282 0.4015 -0.0067 0.3154 -0.0012 400 ASP Z N     
9842  C  CA    . ASP F 400 ? 0.8349 0.3262 0.4061 -0.012  0.3171 0.0001  400 ASP Z CA    
9843  C  C     . ASP F 400 ? 0.8256 0.3261 0.4101 -0.0107 0.3171 0.0024  400 ASP Z C     
9844  O  O     . ASP F 400 ? 0.8286 0.328  0.4175 -0.016  0.3175 0.0041  400 ASP Z O     
9845  C  CB    . ASP F 400 ? 0.8627 0.3396 0.4205 -0.0101 0.3236 -0.0007 400 ASP Z CB    
9846  C  CG    . ASP F 400 ? 0.9186 0.3843 0.4624 -0.0126 0.3239 -0.0025 400 ASP Z CG    
9847  O  OD1   . ASP F 400 ? 0.9255 0.3932 0.4705 -0.0188 0.3187 -0.0029 400 ASP Z OD1   
9848  O  OD2   . ASP F 400 ? 0.9495 0.4043 0.4809 -0.0083 0.3295 -0.0034 400 ASP Z OD2   
9849  N  N     . GLN F 401 ? 0.8101 0.3195 0.4008 -0.0039 0.3169 0.0027  401 GLN Z N     
9850  C  CA    . GLN F 401 ? 0.8002 0.3174 0.4025 -0.0021 0.3173 0.0049  401 GLN Z CA    
9851  C  C     . GLN F 401 ? 0.781  0.3108 0.395  -0.0037 0.3115 0.006   401 GLN Z C     
9852  O  O     . GLN F 401 ? 0.7763 0.3116 0.4003 -0.0079 0.3096 0.0083  401 GLN Z O     
9853  C  CB    . GLN F 401 ? 0.8264 0.3426 0.4261 0.0072  0.3223 0.0047  401 GLN Z CB    
9854  C  CG    . GLN F 401 ? 0.8661 0.3904 0.477  0.0101  0.3227 0.0069  401 GLN Z CG    
9855  C  CD    . GLN F 401 ? 0.9171 0.4433 0.5261 0.0192  0.3253 0.0063  401 GLN Z CD    
9856  O  OE1   . GLN F 401 ? 0.9461 0.4664 0.5451 0.024   0.3285 0.0047  401 GLN Z OE1   
9857  N  NE2   . GLN F 401 ? 0.9074 0.4419 0.5256 0.0219  0.324  0.0078  401 GLN Z NE2   
9858  N  N     . ASP F 402 ? 0.768  0.3024 0.381  -0.0002 0.309  0.0045  402 ASP Z N     
9859  C  CA    . ASP F 402 ? 0.7565 0.3018 0.3792 -0.0011 0.3039 0.0053  402 ASP Z CA    
9860  C  C     . ASP F 402 ? 0.7444 0.2909 0.3618 0       0.3009 0.0031  402 ASP Z C     
9861  O  O     . ASP F 402 ? 0.7476 0.2948 0.3611 0.0065  0.3026 0.002   402 ASP Z O     
9862  C  CB    . ASP F 402 ? 0.7794 0.3308 0.4087 0.0052  0.3056 0.0067  402 ASP Z CB    
9863  C  CG    . ASP F 402 ? 0.8384 0.4003 0.4787 0.004   0.3012 0.0083  402 ASP Z CG    
9864  O  OD1   . ASP F 402 ? 0.8515 0.417  0.4944 -0.0012 0.2964 0.0081  402 ASP Z OD1   
9865  O  OD2   . ASP F 402 ? 0.8618 0.4278 0.5075 0.0085  0.3027 0.0097  402 ASP Z OD2   
9866  N  N     . ILE F 403 ? 0.7287 0.2755 0.3459 -0.0063 0.2966 0.0026  403 ILE Z N     
9867  C  CA    . ILE F 403 ? 0.7198 0.2678 0.3322 -0.0057 0.2936 0.0007  403 ILE Z CA    
9868  C  C     . ILE F 403 ? 0.701  0.2593 0.3205 -0.0021 0.2906 0.0009  403 ILE Z C     
9869  O  O     . ILE F 403 ? 0.7041 0.2635 0.319  0.0014  0.29   -0.0006 403 ILE Z O     
9870  C  CB    . ILE F 403 ? 0.7248 0.2699 0.3349 -0.0136 0.2898 0.0002  403 ILE Z CB    
9871  C  CG1   . ILE F 403 ? 0.7361 0.2799 0.3389 -0.0127 0.2878 -0.0019 403 ILE Z CG1   
9872  C  CG2   . ILE F 403 ? 0.7235 0.2768 0.3452 -0.0193 0.285  0.0022  403 ILE Z CG2   
9873  C  CD1   . ILE F 403 ? 0.757  0.2935 0.3486 -0.007  0.2923 -0.0033 403 ILE Z CD1   
9874  N  N     . ASN F 404 ? 0.6798 0.2452 0.3098 -0.0027 0.2892 0.0029  404 ASN Z N     
9875  C  CA    . ASN F 404 ? 0.6692 0.2433 0.3055 0.0005  0.2867 0.0033  404 ASN Z CA    
9876  C  C     . ASN F 404 ? 0.6722 0.2462 0.3047 0.0082  0.29   0.0025  404 ASN Z C     
9877  O  O     . ASN F 404 ? 0.6721 0.2511 0.3053 0.011   0.2878 0.0018  404 ASN Z O     
9878  C  CB    . ASN F 404 ? 0.6685 0.249  0.316  -0.0016 0.2853 0.006   404 ASN Z CB    
9879  C  CG    . ASN F 404 ? 0.6973 0.2789 0.349  -0.0094 0.282  0.0072  404 ASN Z CG    
9880  O  OD1   . ASN F 404 ? 0.7093 0.2929 0.3605 -0.0131 0.2777 0.0063  404 ASN Z OD1   
9881  N  ND2   . ASN F 404 ? 0.7041 0.2842 0.3596 -0.0124 0.2838 0.0093  404 ASN Z ND2   
9882  N  N     . LYS F 405 ? 0.674  0.242  0.3022 0.0117  0.2951 0.0027  405 LYS Z N     
9883  C  CA    . LYS F 405 ? 0.6773 0.2445 0.3011 0.0191  0.2984 0.002   405 LYS Z CA    
9884  C  C     . LYS F 405 ? 0.6787 0.2446 0.294  0.0213  0.298  0       405 LYS Z C     
9885  O  O     . LYS F 405 ? 0.6806 0.2503 0.2945 0.026   0.2977 -0.0005 405 LYS Z O     
9886  C  CB    . LYS F 405 ? 0.7047 0.2649 0.3251 0.0217  0.3041 0.0027  405 LYS Z CB    
9887  C  CG    . LYS F 405 ? 0.7559 0.3183 0.384  0.0228  0.3059 0.0049  405 LYS Z CG    
9888  C  CD    . LYS F 405 ? 0.8106 0.3654 0.4341 0.0259  0.3118 0.0053  405 LYS Z CD    
9889  C  CE    . LYS F 405 ? 0.8487 0.4049 0.4796 0.0267  0.3141 0.0077  405 LYS Z CE    
9890  N  NZ    . LYS F 405 ? 0.8816 0.4297 0.5078 0.0285  0.3197 0.008   405 LYS Z NZ    
9891  N  N     . LEU F 406 ? 0.6763 0.2365 0.2855 0.0179  0.298  -0.001  406 LEU Z N     
9892  C  CA    . LEU F 406 ? 0.6835 0.2418 0.2843 0.0197  0.2979 -0.0025 406 LEU Z CA    
9893  C  C     . LEU F 406 ? 0.6854 0.2514 0.29   0.018   0.2925 -0.0031 406 LEU Z C     
9894  O  O     . LEU F 406 ? 0.6881 0.2575 0.2896 0.0219  0.2921 -0.0038 406 LEU Z O     
9895  C  CB    . LEU F 406 ? 0.6899 0.2388 0.2829 0.0159  0.2995 -0.0032 406 LEU Z CB    
9896  C  CG    . LEU F 406 ? 0.7094 0.2542 0.2922 0.0181  0.3005 -0.0044 406 LEU Z CG    
9897  C  CD1   . LEU F 406 ? 0.7155 0.2602 0.293  0.0261  0.3047 -0.0044 406 LEU Z CD1   
9898  C  CD2   . LEU F 406 ? 0.7264 0.2603 0.3009 0.0141  0.3025 -0.0049 406 LEU Z CD2   
9899  N  N     . ALA F 407 ? 0.6807 0.25   0.2923 0.0121  0.2884 -0.0026 407 ALA Z N     
9900  C  CA    . ALA F 407 ? 0.6817 0.258  0.2973 0.0101  0.2833 -0.003  407 ALA Z CA    
9901  C  C     . ALA F 407 ? 0.6838 0.2673 0.3036 0.0144  0.2825 -0.0027 407 ALA Z C     
9902  O  O     . ALA F 407 ? 0.6868 0.2749 0.3061 0.015   0.2796 -0.0035 407 ALA Z O     
9903  C  CB    . ALA F 407 ? 0.6791 0.2575 0.3018 0.0034  0.2797 -0.002  407 ALA Z CB    
9904  N  N     . LYS F 408 ? 0.6831 0.267  0.3065 0.0174  0.285  -0.0015 408 LYS Z N     
9905  C  CA    . LYS F 408 ? 0.6892 0.2784 0.3156 0.0216  0.2847 -0.0011 408 LYS Z CA    
9906  C  C     . LYS F 408 ? 0.698  0.2878 0.3176 0.0268  0.286  -0.0022 408 LYS Z C     
9907  O  O     . LYS F 408 ? 0.6973 0.2925 0.3178 0.0282  0.2835 -0.0025 408 LYS Z O     
9908  C  CB    . LYS F 408 ? 0.7125 0.3003 0.3429 0.0239  0.288  0.0006  408 LYS Z CB    
9909  C  CG    . LYS F 408 ? 0.7668 0.3588 0.4    0.0279  0.2877 0.0012  408 LYS Z CG    
9910  C  CD    . LYS F 408 ? 0.828  0.4175 0.4634 0.0312  0.2918 0.0028  408 LYS Z CD    
9911  C  CE    . LYS F 408 ? 0.8761 0.4665 0.5198 0.0277  0.2915 0.005   408 LYS Z CE    
9912  N  NZ    . LYS F 408 ? 0.9084 0.4937 0.5523 0.0288  0.2962 0.0062  408 LYS Z NZ    
9913  N  N     . ARG F 409 ? 0.7051 0.2894 0.3175 0.0294  0.2898 -0.0026 409 ARG Z N     
9914  C  CA    . ARG F 409 ? 0.7167 0.3021 0.3227 0.0347  0.2914 -0.0032 409 ARG Z CA    
9915  C  C     . ARG F 409 ? 0.7113 0.2977 0.3122 0.0339  0.2896 -0.0041 409 ARG Z C     
9916  O  O     . ARG F 409 ? 0.7115 0.3022 0.3095 0.0374  0.2892 -0.0043 409 ARG Z O     
9917  C  CB    . ARG F 409 ? 0.7541 0.3337 0.3549 0.0395  0.297  -0.0027 409 ARG Z CB    
9918  C  CG    . ARG F 409 ? 0.8249 0.3962 0.4212 0.0374  0.3    -0.0029 409 ARG Z CG    
9919  C  CD    . ARG F 409 ? 0.8943 0.4597 0.4853 0.0424  0.3057 -0.0024 409 ARG Z CD    
9920  N  NE    . ARG F 409 ? 0.9572 0.5242 0.5416 0.0483  0.3075 -0.0025 409 ARG Z NE    
9921  C  CZ    . ARG F 409 ? 1.0062 0.5693 0.5851 0.0538  0.3125 -0.002  409 ARG Z CZ    
9922  N  NH1   . ARG F 409 ? 1.0068 0.5634 0.5856 0.0542  0.3162 -0.0015 409 ARG Z NH1   
9923  N  NH2   . ARG F 409 ? 1.0155 0.5813 0.5888 0.059   0.3137 -0.0018 409 ARG Z NH2   
9924  N  N     . ASN F 410 ? 0.7043 0.287  0.3041 0.0293  0.2886 -0.0046 410 ASN Z N     
9925  C  CA    . ASN F 410 ? 0.7056 0.2881 0.2997 0.0287  0.2874 -0.0054 410 ASN Z CA    
9926  C  C     . ASN F 410 ? 0.7056 0.2915 0.3039 0.023   0.2822 -0.006  410 ASN Z C     
9927  O  O     . ASN F 410 ? 0.7093 0.2934 0.3119 0.0181  0.2805 -0.0059 410 ASN Z O     
9928  C  CB    . ASN F 410 ? 0.7221 0.2953 0.3079 0.0291  0.2915 -0.0055 410 ASN Z CB    
9929  C  CG    . ASN F 410 ? 0.7607 0.3327 0.3393 0.0301  0.2915 -0.006  410 ASN Z CG    
9930  O  OD1   . ASN F 410 ? 0.7761 0.3466 0.354  0.0255  0.2889 -0.0066 410 ASN Z OD1   
9931  N  ND2   . ASN F 410 ? 0.7686 0.3412 0.3414 0.0361  0.2947 -0.0054 410 ASN Z ND2   
9932  N  N     . GLY F 411 ? 0.699  0.2901 0.2961 0.0238  0.2797 -0.0064 411 GLY Z N     
9933  C  CA    . GLY F 411 ? 0.6977 0.2922 0.2981 0.019   0.2748 -0.007  411 GLY Z CA    
9934  C  C     . GLY F 411 ? 0.6991 0.2876 0.2956 0.0147  0.2743 -0.0075 411 GLY Z C     
9935  O  O     . GLY F 411 ? 0.7017 0.2916 0.3025 0.0097  0.2704 -0.0078 411 GLY Z O     
9936  N  N     . LEU F 412 ? 0.6961 0.2774 0.2841 0.0167  0.2781 -0.0076 412 LEU Z N     
9937  C  CA    . LEU F 412 ? 0.698  0.2718 0.2808 0.0125  0.2779 -0.0082 412 LEU Z CA    
9938  C  C     . LEU F 412 ? 0.6975 0.2663 0.2832 0.0077  0.2779 -0.0081 412 LEU Z C     
9939  O  O     . LEU F 412 ? 0.7009 0.2682 0.2882 0.0019  0.2746 -0.0084 412 LEU Z O     
9940  C  CB    . LEU F 412 ? 0.7022 0.2688 0.2738 0.0161  0.2823 -0.0082 412 LEU Z CB    
9941  C  CG    . LEU F 412 ? 0.72   0.2776 0.2849 0.0116  0.2821 -0.0089 412 LEU Z CG    
9942  C  CD1   . LEU F 412 ? 0.7253 0.2869 0.2922 0.008   0.2772 -0.0094 412 LEU Z CD1   
9943  C  CD2   . LEU F 412 ? 0.7329 0.2821 0.2861 0.0156  0.2871 -0.0086 412 LEU Z CD2   
9944  N  N     . TRP F 413 ? 0.6899 0.2566 0.2768 0.01    0.2813 -0.0074 413 TRP Z N     
9945  C  CA    . TRP F 413 ? 0.6878 0.2509 0.2786 0.0056  0.2814 -0.0069 413 TRP Z CA    
9946  C  C     . TRP F 413 ? 0.6809 0.252  0.2827 0.0018  0.2767 -0.0062 413 TRP Z C     
9947  O  O     . TRP F 413 ? 0.6812 0.2506 0.2862 -0.0039 0.2747 -0.0058 413 TRP Z O     
9948  C  CB    . TRP F 413 ? 0.6879 0.2471 0.2773 0.0093  0.2864 -0.0062 413 TRP Z CB    
9949  C  CG    . TRP F 413 ? 0.7013 0.2503 0.2795 0.0114  0.2912 -0.0066 413 TRP Z CG    
9950  C  CD1   . TRP F 413 ? 0.715  0.262  0.2864 0.0181  0.2956 -0.0065 413 TRP Z CD1   
9951  C  CD2   . TRP F 413 ? 0.7075 0.2464 0.279  0.0066  0.2922 -0.007  413 TRP Z CD2   
9952  N  NE1   . TRP F 413 ? 0.7248 0.2609 0.2857 0.0183  0.2996 -0.0068 413 TRP Z NE1   
9953  C  CE2   . TRP F 413 ? 0.723  0.2534 0.2833 0.0111  0.2976 -0.0072 413 TRP Z CE2   
9954  C  CE3   . TRP F 413 ? 0.7136 0.2497 0.287  -0.0011 0.289  -0.0071 413 TRP Z CE3   
9955  C  CZ2   . TRP F 413 ? 0.7372 0.2555 0.2876 0.008   0.3    -0.0077 413 TRP Z CZ2   
9956  C  CZ3   . TRP F 413 ? 0.73   0.2546 0.2938 -0.0045 0.291  -0.0076 413 TRP Z CZ3   
9957  C  CH2   . TRP F 413 ? 0.7375 0.2528 0.2896 0       0.2966 -0.008  413 TRP Z CH2   
9958  N  N     . LYS F 414 ? 0.6713 0.2507 0.2782 0.0046  0.2747 -0.0061 414 LYS Z N     
9959  C  CA    . LYS F 414 ? 0.6663 0.253  0.2826 0.0018  0.2705 -0.0054 414 LYS Z CA    
9960  C  C     . LYS F 414 ? 0.6679 0.2554 0.2846 -0.0037 0.266  -0.006  414 LYS Z C     
9961  O  O     . LYS F 414 ? 0.6641 0.2541 0.2874 -0.0082 0.2631 -0.0051 414 LYS Z O     
9962  C  CB    . LYS F 414 ? 0.6809 0.2746 0.2997 0.0063  0.2697 -0.0055 414 LYS Z CB    
9963  C  CG    . LYS F 414 ? 0.7223 0.322  0.3502 0.0054  0.2674 -0.0043 414 LYS Z CG    
9964  C  CD    . LYS F 414 ? 0.7708 0.3764 0.3995 0.0088  0.266  -0.0047 414 LYS Z CD    
9965  C  CE    . LYS F 414 ? 0.8141 0.4188 0.4383 0.0147  0.2696 -0.0048 414 LYS Z CE    
9966  N  NZ    . LYS F 414 ? 0.8368 0.4386 0.463  0.0169  0.2732 -0.0037 414 LYS Z NZ    
9967  N  N     . SER F 415 ? 0.6715 0.2569 0.2813 -0.0033 0.2656 -0.0072 415 SER Z N     
9968  C  CA    . SER F 415 ? 0.6785 0.2635 0.2872 -0.0081 0.2617 -0.0079 415 SER Z CA    
9969  C  C     . SER F 415 ? 0.6922 0.27   0.2987 -0.0137 0.2615 -0.0077 415 SER Z C     
9970  O  O     . SER F 415 ? 0.6927 0.2723 0.3032 -0.0191 0.2576 -0.0075 415 SER Z O     
9971  C  CB    . SER F 415 ? 0.6908 0.2742 0.2915 -0.0056 0.2622 -0.009  415 SER Z CB    
9972  O  OG    . SER F 415 ? 0.7125 0.2936 0.3106 -0.0101 0.2591 -0.0097 415 SER Z OG    
9973  N  N     . PHE F 416 ? 0.7001 0.2697 0.2999 -0.0126 0.2659 -0.0078 416 PHE Z N     
9974  C  CA    . PHE F 416 ? 0.7092 0.2706 0.3053 -0.018  0.2663 -0.0077 416 PHE Z CA    
9975  C  C     . PHE F 416 ? 0.7095 0.2742 0.3149 -0.0221 0.2648 -0.0062 416 PHE Z C     
9976  O  O     . PHE F 416 ? 0.7104 0.2737 0.3173 -0.0286 0.2618 -0.0057 416 PHE Z O     
9977  C  CB    . PHE F 416 ? 0.7153 0.2666 0.3011 -0.0151 0.2719 -0.0082 416 PHE Z CB    
9978  C  CG    . PHE F 416 ? 0.7298 0.2762 0.3051 -0.0115 0.2739 -0.0093 416 PHE Z CG    
9979  C  CD1   . PHE F 416 ? 0.7428 0.2908 0.3162 -0.0132 0.2705 -0.01   416 PHE Z CD1   
9980  C  CD2   . PHE F 416 ? 0.7464 0.2861 0.3131 -0.0064 0.2795 -0.0094 416 PHE Z CD2   
9981  C  CE1   . PHE F 416 ? 0.7595 0.303  0.3232 -0.0097 0.2727 -0.0106 416 PHE Z CE1   
9982  C  CE2   . PHE F 416 ? 0.7623 0.2976 0.3192 -0.0028 0.2817 -0.0099 416 PHE Z CE2   
9983  C  CZ    . PHE F 416 ? 0.7624 0.2997 0.318  -0.0045 0.2784 -0.0105 416 PHE Z CZ    
9984  N  N     . VAL F 417 ? 0.7056 0.2744 0.3169 -0.0183 0.2671 -0.0051 417 VAL Z N     
9985  C  CA    . VAL F 417 ? 0.7073 0.2797 0.3277 -0.0211 0.2665 -0.0031 417 VAL Z CA    
9986  C  C     . VAL F 417 ? 0.7067 0.2883 0.3369 -0.024  0.2614 -0.002  417 VAL Z C     
9987  O  O     . VAL F 417 ? 0.7057 0.2895 0.3422 -0.029  0.2594 -0.0002 417 VAL Z O     
9988  C  CB    . VAL F 417 ? 0.7151 0.2883 0.3377 -0.0153 0.2709 -0.0023 417 VAL Z CB    
9989  C  CG1   . VAL F 417 ? 0.715  0.2934 0.3481 -0.017  0.2705 0.0001  417 VAL Z CG1   
9990  C  CG2   . VAL F 417 ? 0.7294 0.2926 0.3424 -0.0133 0.2761 -0.003  417 VAL Z CG2   
9991  N  N     . SER F 418 ? 0.7058 0.2926 0.3369 -0.0214 0.2592 -0.0028 418 SER Z N     
9992  C  CA    . SER F 418 ? 0.7079 0.3029 0.3473 -0.0236 0.2548 -0.0018 418 SER Z CA    
9993  C  C     . SER F 418 ? 0.7135 0.3081 0.3523 -0.0299 0.2504 -0.0021 418 SER Z C     
9994  O  O     . SER F 418 ? 0.7111 0.3117 0.3578 -0.0331 0.2469 -0.0005 418 SER Z O     
9995  C  CB    . SER F 418 ? 0.7233 0.3234 0.363  -0.0188 0.254  -0.0027 418 SER Z CB    
9996  O  OG    . SER F 418 ? 0.7527 0.3535 0.3927 -0.013  0.2577 -0.0025 418 SER Z OG    
9997  N  N     . LEU F 419 ? 0.7174 0.305  0.3467 -0.0313 0.2505 -0.0039 419 LEU Z N     
9998  C  CA    . LEU F 419 ? 0.72   0.3066 0.3476 -0.0369 0.2462 -0.0044 419 LEU Z CA    
9999  C  C     . LEU F 419 ? 0.7242 0.3021 0.3454 -0.0426 0.2462 -0.0046 419 LEU Z C     
10000 O  O     . LEU F 419 ? 0.7276 0.3049 0.3478 -0.0478 0.2422 -0.0048 419 LEU Z O     
10001 C  CB    . LEU F 419 ? 0.7243 0.3109 0.3463 -0.0344 0.2451 -0.0063 419 LEU Z CB    
10002 C  CG    . LEU F 419 ? 0.7381 0.3337 0.3665 -0.0308 0.2435 -0.0061 419 LEU Z CG    
10003 C  CD1   . LEU F 419 ? 0.7477 0.343  0.37   -0.0277 0.2434 -0.0078 419 LEU Z CD1   
10004 C  CD2   . LEU F 419 ? 0.7424 0.3446 0.3793 -0.0349 0.2389 -0.0047 419 LEU Z CD2   
10005 N  N     . SER F 420 ? 0.7223 0.2933 0.3388 -0.0419 0.2504 -0.0046 420 SER Z N     
10006 C  CA    . SER F 420 ? 0.7318 0.2932 0.3411 -0.0478 0.2505 -0.0049 420 SER Z CA    
10007 C  C     . SER F 420 ? 0.733  0.297  0.3498 -0.0534 0.249  -0.0026 420 SER Z C     
10008 O  O     . SER F 420 ? 0.7321 0.3002 0.3557 -0.0511 0.2513 -0.0011 420 SER Z O     
10009 C  CB    . SER F 420 ? 0.7532 0.304  0.3515 -0.0445 0.2561 -0.0061 420 SER Z CB    
10010 O  OG    . SER F 420 ? 0.7782 0.3279 0.3705 -0.038  0.2585 -0.0076 420 SER Z OG    
10011 N  N     . ASP F 421 ? 0.7337 0.2952 0.349  -0.061  0.2453 -0.0023 421 ASP Z N     
10012 C  CA    . ASP F 421 ? 0.7373 0.3005 0.3586 -0.0673 0.2438 0.0001  421 ASP Z CA    
10013 C  C     . ASP F 421 ? 0.7419 0.2933 0.3541 -0.069  0.2481 -0.0005 421 ASP Z C     
10014 O  O     . ASP F 421 ? 0.7396 0.2924 0.357  -0.0714 0.2493 0.0015  421 ASP Z O     
10015 C  CB    . ASP F 421 ? 0.7644 0.3298 0.3874 -0.0751 0.2377 0.0008  421 ASP Z CB    
10016 C  CG    . ASP F 421 ? 0.8291 0.4066 0.4623 -0.0738 0.2337 0.0019  421 ASP Z CG    
10017 O  OD1   . ASP F 421 ? 0.846  0.4234 0.4755 -0.0704 0.2329 0       421 ASP Z OD1   
10018 O  OD2   . ASP F 421 ? 0.8522 0.4391 0.4969 -0.0759 0.2315 0.0048  421 ASP Z OD2   
10019 N  N     . PHE F 422 ? 0.7462 0.286  0.3446 -0.0676 0.2507 -0.003  422 PHE Z N     
10020 C  CA    . PHE F 422 ? 0.7568 0.2839 0.3445 -0.0685 0.2553 -0.0037 422 PHE Z CA    
10021 C  C     . PHE F 422 ? 0.7617 0.2825 0.3398 -0.0604 0.2603 -0.0058 422 PHE Z C     
10022 O  O     . PHE F 422 ? 0.7665 0.2869 0.3401 -0.0579 0.2592 -0.0072 422 PHE Z O     
10023 C  CB    . PHE F 422 ? 0.7635 0.2802 0.3412 -0.0769 0.2529 -0.0044 422 PHE Z CB    
10024 C  CG    . PHE F 422 ? 0.7648 0.2887 0.3513 -0.0854 0.2467 -0.0025 422 PHE Z CG    
10025 C  CD1   . PHE F 422 ? 0.7722 0.2991 0.3658 -0.0904 0.2463 0       422 PHE Z CD1   
10026 C  CD2   . PHE F 422 ? 0.7688 0.2968 0.3567 -0.0881 0.2414 -0.0028 422 PHE Z CD2   
10027 C  CE1   . PHE F 422 ? 0.7741 0.3088 0.3762 -0.0981 0.2406 0.0023  422 PHE Z CE1   
10028 C  CE2   . PHE F 422 ? 0.7712 0.3063 0.3671 -0.0956 0.2357 -0.0007 422 PHE Z CE2   
10029 C  CZ    . PHE F 422 ? 0.7665 0.3051 0.3696 -0.1006 0.2353 0.0019  422 PHE Z CZ    
10030 N  N     . ILE F 423 ? 0.7592 0.2755 0.3345 -0.0561 0.2659 -0.0057 423 ILE Z N     
10031 C  CA    . ILE F 423 ? 0.7685 0.2791 0.3346 -0.0482 0.271  -0.0072 423 ILE Z CA    
10032 C  C     . ILE F 423 ? 0.7881 0.2832 0.3404 -0.0497 0.2756 -0.008  423 ILE Z C     
10033 O  O     . ILE F 423 ? 0.7946 0.2867 0.348  -0.0515 0.278  -0.007  423 ILE Z O     
10034 C  CB    . ILE F 423 ? 0.765  0.2837 0.3389 -0.0404 0.274  -0.0064 423 ILE Z CB    
10035 C  CG1   . ILE F 423 ? 0.7675 0.3003 0.3538 -0.0388 0.2697 -0.0057 423 ILE Z CG1   
10036 C  CG2   . ILE F 423 ? 0.7739 0.2865 0.3377 -0.0326 0.2794 -0.0077 423 ILE Z CG2   
10037 C  CD1   . ILE F 423 ? 0.7767 0.3175 0.3713 -0.0325 0.2719 -0.0047 423 ILE Z CD1   
10038 N  N     . VAL F 424 ? 0.7951 0.28   0.334  -0.0488 0.277  -0.0096 424 VAL Z N     
10039 C  CA    . VAL F 424 ? 0.8091 0.2777 0.3329 -0.0499 0.2817 -0.0104 424 VAL Z CA    
10040 C  C     . VAL F 424 ? 0.8181 0.2818 0.3328 -0.0407 0.2876 -0.0112 424 VAL Z C     
10041 O  O     . VAL F 424 ? 0.8172 0.2843 0.3305 -0.0364 0.2868 -0.0118 424 VAL Z O     
10042 C  CB    . VAL F 424 ? 0.8244 0.2829 0.3381 -0.0575 0.2787 -0.0114 424 VAL Z CB    
10043 C  CG1   . VAL F 424 ? 0.8443 0.2843 0.3406 -0.0586 0.284  -0.0123 424 VAL Z CG1   
10044 C  CG2   . VAL F 424 ? 0.8252 0.2897 0.3484 -0.0669 0.2726 -0.0103 424 VAL Z CG2   
10045 N  N     . LEU F 425 ? 0.8262 0.2822 0.335  -0.0376 0.2934 -0.011  425 LEU Z N     
10046 C  CA    . LEU F 425 ? 0.8397 0.2908 0.3395 -0.0285 0.2995 -0.0113 425 LEU Z CA    
10047 C  C     . LEU F 425 ? 0.8586 0.2911 0.3407 -0.0296 0.3046 -0.012  425 LEU Z C     
10048 O  O     . LEU F 425 ? 0.8642 0.2886 0.3432 -0.0354 0.3054 -0.0119 425 LEU Z O     
10049 C  CB    . LEU F 425 ? 0.8369 0.2949 0.3445 -0.0222 0.303  -0.0103 425 LEU Z CB    
10050 C  CG    . LEU F 425 ? 0.8419 0.3165 0.3667 -0.0217 0.2988 -0.0094 425 LEU Z CG    
10051 C  CD1   . LEU F 425 ? 0.8473 0.3255 0.3773 -0.0164 0.3027 -0.0085 425 LEU Z CD1   
10052 C  CD2   . LEU F 425 ? 0.8437 0.3281 0.3726 -0.0177 0.2958 -0.0097 425 LEU Z CD2   
10053 N  N     . ASP F 426 ? 0.8678 0.2933 0.338  -0.0239 0.3082 -0.0125 426 ASP Z N     
10054 C  CA    . ASP F 426 ? 0.8893 0.2963 0.3411 -0.0228 0.3142 -0.0129 426 ASP Z CA    
10055 C  C     . ASP F 426 ? 0.8956 0.3055 0.3442 -0.0117 0.3192 -0.0123 426 ASP Z C     
10056 O  O     . ASP F 426 ? 0.9026 0.3103 0.344  -0.0081 0.3199 -0.0123 426 ASP Z O     
10057 C  CB    . ASP F 426 ? 0.9173 0.3125 0.3568 -0.0286 0.3124 -0.014  426 ASP Z CB    
10058 C  CG    . ASP F 426 ? 0.9906 0.3647 0.4098 -0.0286 0.3186 -0.0144 426 ASP Z CG    
10059 O  OD1   . ASP F 426 ? 1.0025 0.3713 0.4168 -0.0232 0.3249 -0.0139 426 ASP Z OD1   
10060 O  OD2   . ASP F 426 ? 1.0287 0.3911 0.4365 -0.0339 0.3174 -0.0153 426 ASP Z OD2   
10061 N  N     . CYS F 427 ? 0.8895 0.3057 0.3447 -0.0062 0.3222 -0.0114 427 CYS Z N     
10062 C  CA    . CYS F 427 ? 0.8917 0.3144 0.3472 0.0042  0.3259 -0.0105 427 CYS Z CA    
10063 C  C     . CYS F 427 ? 0.8932 0.3059 0.3379 0.0109  0.334  -0.0098 427 CYS Z C     
10064 O  O     . CYS F 427 ? 0.8957 0.3047 0.3416 0.0095  0.3362 -0.0098 427 CYS Z O     
10065 C  CB    . CYS F 427 ? 0.8951 0.3362 0.3684 0.0062  0.322  -0.0099 427 CYS Z CB    
10066 S  SG    . CYS F 427 ? 0.9467 0.4009 0.4331 -0.0001 0.3129 -0.0105 427 CYS Z SG    
10067 N  N     . PRO F 428 ? 0.8872 0.2983 0.3236 0.0193  0.3383 -0.0089 428 PRO Z N     
10068 C  CA    . PRO F 428 ? 0.8873 0.2918 0.3153 0.0272  0.346  -0.0078 428 PRO Z CA    
10069 C  C     . PRO F 428 ? 0.876  0.2941 0.3173 0.0315  0.3457 -0.0071 428 PRO Z C     
10070 O  O     . PRO F 428 ? 0.8683 0.3019 0.3235 0.0311  0.3403 -0.0071 428 PRO Z O     
10071 C  CB    . PRO F 428 ? 0.8993 0.3031 0.3183 0.0352  0.3494 -0.0066 428 PRO Z CB    
10072 C  CG    . PRO F 428 ? 0.9063 0.3123 0.3262 0.0304  0.344  -0.0073 428 PRO Z CG    
10073 C  CD    . PRO F 428 ? 0.8783 0.2949 0.3136 0.0225  0.3364 -0.0085 428 PRO Z CD    
10074 N  N     . ILE F 429 ? 0.8737 0.2858 0.3106 0.0355  0.3514 -0.0065 429 ILE Z N     
10075 C  CA    . ILE F 429 ? 0.8644 0.288  0.3126 0.04    0.3517 -0.0058 429 ILE Z CA    
10076 C  C     . ILE F 429 ? 0.8635 0.2875 0.305  0.0508  0.3577 -0.0042 429 ILE Z C     
10077 O  O     . ILE F 429 ? 0.875  0.2852 0.3022 0.0542  0.3642 -0.0037 429 ILE Z O     
10078 C  CB    . ILE F 429 ? 0.8712 0.2893 0.3221 0.0355  0.3529 -0.0063 429 ILE Z CB    
10079 C  CG1   . ILE F 429 ? 0.8807 0.2981 0.3374 0.0243  0.3471 -0.0075 429 ILE Z CG1   
10080 C  CG2   . ILE F 429 ? 0.8693 0.2991 0.3317 0.0403  0.3531 -0.0055 429 ILE Z CG2   
10081 C  CD1   . ILE F 429 ? 0.8844 0.3182 0.3568 0.0213  0.3395 -0.0076 429 ILE Z CD1   
10082 N  N     . ILE F 430 ? 0.8492 0.2887 0.3003 0.0563  0.3556 -0.0032 430 ILE Z N     
10083 C  CA    . ILE F 430 ? 0.8499 0.2925 0.2964 0.0667  0.3606 -0.0013 430 ILE Z CA    
10084 C  C     . ILE F 430 ? 0.8565 0.2905 0.2971 0.0707  0.3672 -0.0008 430 ILE Z C     
10085 O  O     . ILE F 430 ? 0.8507 0.2882 0.2999 0.0687  0.366  -0.0013 430 ILE Z O     
10086 C  CB    . ILE F 430 ? 0.8416 0.3032 0.3013 0.0702  0.3562 -0.0004 430 ILE Z CB    
10087 C  CG1   . ILE F 430 ? 0.8455 0.3156 0.3113 0.0659  0.3497 -0.001  430 ILE Z CG1   
10088 C  CG2   . ILE F 430 ? 0.8464 0.3124 0.3018 0.0806  0.361  0.0018  430 ILE Z CG2   
10089 C  CD1   . ILE F 430 ? 0.8662 0.3315 0.3215 0.0686  0.3518 -0.0001 430 ILE Z CD1   
10090 N  N     . GLY F 431 ? 0.8659 0.2876 0.2915 0.076   0.3742 0.0003  431 GLY Z N     
10091 C  CA    . GLY F 431 ? 0.8769 0.2884 0.2947 0.0801  0.3811 0.0008  431 GLY Z CA    
10092 C  C     . GLY F 431 ? 0.8861 0.2792 0.2936 0.0738  0.384  -0.0006 431 GLY Z C     
10093 O  O     . GLY F 431 ? 0.8882 0.271  0.2881 0.0765  0.3901 -0.0003 431 GLY Z O     
10094 N  N     . GLU F 432 ? 0.8906 0.2791 0.2976 0.0649  0.3797 -0.0022 432 GLU Z N     
10095 C  CA    . GLU F 432 ? 0.9098 0.281  0.3069 0.0576  0.3816 -0.0035 432 GLU Z CA    
10096 C  C     . GLU F 432 ? 0.9249 0.2835 0.3072 0.056   0.383  -0.0037 432 GLU Z C     
10097 O  O     . GLU F 432 ? 0.9221 0.2881 0.306  0.0581  0.3803 -0.0032 432 GLU Z O     
10098 C  CB    . GLU F 432 ? 0.9375 0.3134 0.3471 0.0471  0.375  -0.005  432 GLU Z CB    
10099 C  CG    . GLU F 432 ? 1.0018 0.3878 0.4243 0.0487  0.3745 -0.0047 432 GLU Z CG    
10100 C  CD    . GLU F 432 ? 1.0873 0.4733 0.5185 0.039   0.3705 -0.0057 432 GLU Z CD    
10101 O  OE1   . GLU F 432 ? 1.0951 0.4838 0.5312 0.031   0.3645 -0.0065 432 GLU Z OE1   
10102 O  OE2   . GLU F 432 ? 1.1196 0.5031 0.5529 0.0393  0.3736 -0.0054 432 GLU Z OE2   
10103 N  N     . SER F 433 ? 0.9399 0.279  0.3073 0.0525  0.3875 -0.0044 433 SER Z N     
10104 C  CA    . SER F 433 ? 0.9584 0.2826 0.3092 0.0515  0.39   -0.0046 433 SER Z CA    
10105 C  C     . SER F 433 ? 0.96   0.2828 0.3126 0.041   0.3831 -0.0062 433 SER Z C     
10106 O  O     . SER F 433 ? 0.969  0.2861 0.3123 0.0418  0.3834 -0.006  433 SER Z O     
10107 C  CB    . SER F 433 ? 0.9936 0.2956 0.3252 0.0523  0.3981 -0.0046 433 SER Z CB    
10108 O  OG    . SER F 433 ? 1.0282 0.3302 0.3579 0.0612  0.4046 -0.0031 433 SER Z OG    
10109 N  N     . TYR F 434 ? 0.9515 0.2783 0.315  0.0314  0.3774 -0.0077 434 TYR Z N     
10110 C  CA    . TYR F 434 ? 0.954  0.2791 0.3189 0.0211  0.3709 -0.0091 434 TYR Z CA    
10111 C  C     . TYR F 434 ? 0.937  0.2816 0.3231 0.016   0.3622 -0.0096 434 TYR Z C     
10112 O  O     . TYR F 434 ? 0.9259 0.2838 0.3254 0.0193  0.3613 -0.0089 434 TYR Z O     
10113 C  CB    . TYR F 434 ? 0.9664 0.2719 0.3184 0.0122  0.3726 -0.0104 434 TYR Z CB    
10114 C  CG    . TYR F 434 ? 0.991  0.2756 0.3201 0.0168  0.3809 -0.01   434 TYR Z CG    
10115 C  CD1   . TYR F 434 ? 1.0086 0.2846 0.3295 0.0231  0.3888 -0.0092 434 TYR Z CD1   
10116 C  CD2   . TYR F 434 ? 1.01   0.2837 0.3255 0.0157  0.3812 -0.0103 434 TYR Z CD2   
10117 C  CE1   . TYR F 434 ? 1.0332 0.2901 0.3327 0.0284  0.3969 -0.0086 434 TYR Z CE1   
10118 C  CE2   . TYR F 434 ? 1.0352 0.2895 0.3291 0.0208  0.3894 -0.0097 434 TYR Z CE2   
10119 C  CZ    . TYR F 434 ? 1.0524 0.2984 0.3383 0.0273  0.3973 -0.0088 434 TYR Z CZ    
10120 O  OH    . TYR F 434 ? 1.0868 0.313  0.3507 0.0327  0.4057 -0.008  434 TYR Z OH    
10121 N  N     . ASN F 435 ? 0.9315 0.2774 0.3198 0.0083  0.3559 -0.0106 435 ASN Z N     
10122 C  CA    . ASN F 435 ? 0.9196 0.2826 0.3263 0.0032  0.3476 -0.0109 435 ASN Z CA    
10123 C  C     . ASN F 435 ? 0.9085 0.2752 0.326  -0.0046 0.3443 -0.0112 435 ASN Z C     
10124 O  O     . ASN F 435 ? 0.9157 0.2695 0.3253 -0.0093 0.3471 -0.0115 435 ASN Z O     
10125 C  CB    . ASN F 435 ? 0.9378 0.2993 0.3416 -0.0025 0.3424 -0.0118 435 ASN Z CB    
10126 C  CG    . ASN F 435 ? 0.9822 0.3476 0.3825 0.005   0.3434 -0.0111 435 ASN Z CG    
10127 O  OD1   . ASN F 435 ? 0.9984 0.3621 0.3922 0.0144  0.3494 -0.01   435 ASN Z OD1   
10128 N  ND2   . ASN F 435 ? 0.9913 0.3622 0.3955 0.001   0.3375 -0.0117 435 ASN Z ND2   
10129 N  N     . GLU F 436 ? 0.8877 0.2722 0.3233 -0.006  0.3382 -0.0109 436 GLU Z N     
10130 C  CA    . GLU F 436 ? 0.8774 0.269  0.3261 -0.0129 0.3342 -0.0106 436 GLU Z CA    
10131 C  C     . GLU F 436 ? 0.865  0.2628 0.3209 -0.0213 0.3264 -0.0111 436 GLU Z C     
10132 O  O     . GLU F 436 ? 0.8607 0.2677 0.3213 -0.0189 0.3229 -0.0113 436 GLU Z O     
10133 C  CB    . GLU F 436 ? 0.8936 0.3012 0.3575 -0.0069 0.3338 -0.0096 436 GLU Z CB    
10134 C  CG    . GLU F 436 ? 0.9508 0.3534 0.4104 -0.0002 0.3409 -0.009  436 GLU Z CG    
10135 C  CD    . GLU F 436 ? 1.0265 0.4206 0.4847 -0.0061 0.343  -0.0088 436 GLU Z CD    
10136 O  OE1   . GLU F 436 ? 1.0473 0.4249 0.491  -0.0096 0.3463 -0.0094 436 GLU Z OE1   
10137 O  OE2   . GLU F 436 ? 1.0522 0.4559 0.5237 -0.0071 0.3413 -0.0079 436 GLU Z OE2   
10138 N  N     . PHE F 437 ? 0.8591 0.2521 0.3156 -0.0312 0.3236 -0.0112 437 PHE Z N     
10139 C  CA    . PHE F 437 ? 0.8562 0.2559 0.3204 -0.0396 0.3159 -0.0114 437 PHE Z CA    
10140 C  C     . PHE F 437 ? 0.8443 0.2589 0.3271 -0.0431 0.3116 -0.01   437 PHE Z C     
10141 O  O     . PHE F 437 ? 0.8477 0.2598 0.3328 -0.0456 0.3138 -0.0092 437 PHE Z O     
10142 C  CB    . PHE F 437 ? 0.8669 0.2511 0.318  -0.049  0.3148 -0.0123 437 PHE Z CB    
10143 C  CG    . PHE F 437 ? 0.8731 0.2652 0.3338 -0.0587 0.3066 -0.012  437 PHE Z CG    
10144 C  CD1   . PHE F 437 ? 0.8791 0.2791 0.344  -0.0585 0.3016 -0.0125 437 PHE Z CD1   
10145 C  CD2   . PHE F 437 ? 0.8837 0.2772 0.351  -0.0674 0.3039 -0.011  437 PHE Z CD2   
10146 C  CE1   . PHE F 437 ? 0.8827 0.2911 0.3573 -0.0667 0.2942 -0.012  437 PHE Z CE1   
10147 C  CE2   . PHE F 437 ? 0.887  0.2895 0.3643 -0.0758 0.2963 -0.0103 437 PHE Z CE2   
10148 C  CZ    . PHE F 437 ? 0.8794 0.2891 0.3601 -0.0752 0.2916 -0.0109 437 PHE Z CZ    
10149 N  N     . ARG F 438 ? 0.8301 0.2595 0.3259 -0.0434 0.3058 -0.0097 438 ARG Z N     
10150 C  CA    . ARG F 438 ? 0.8212 0.2651 0.3346 -0.0465 0.3015 -0.0081 438 ARG Z CA    
10151 C  C     . ARG F 438 ? 0.8195 0.2711 0.3401 -0.0534 0.2939 -0.008  438 ARG Z C     
10152 O  O     . ARG F 438 ? 0.8251 0.2774 0.3421 -0.0518 0.2918 -0.009  438 ARG Z O     
10153 C  CB    . ARG F 438 ? 0.8235 0.2803 0.3475 -0.0374 0.3027 -0.0074 438 ARG Z CB    
10154 C  CG    . ARG F 438 ? 0.8537 0.3049 0.3722 -0.0299 0.3099 -0.0074 438 ARG Z CG    
10155 C  CD    . ARG F 438 ? 0.8818 0.333  0.4061 -0.0323 0.3119 -0.006  438 ARG Z CD    
10156 N  NE    . ARG F 438 ? 0.9047 0.3519 0.4242 -0.0239 0.3186 -0.006  438 ARG Z NE    
10157 C  CZ    . ARG F 438 ? 0.9242 0.357  0.4306 -0.0228 0.3245 -0.0065 438 ARG Z CZ    
10158 N  NH1   . ARG F 438 ? 0.9173 0.3375 0.4137 -0.0303 0.3246 -0.007  438 ARG Z NH1   
10159 N  NH2   . ARG F 438 ? 0.9235 0.3543 0.4265 -0.0144 0.3304 -0.0063 438 ARG Z NH2   
10160 N  N     . LEU F 439 ? 0.8104 0.2684 0.3415 -0.0607 0.29   -0.0064 439 LEU Z N     
10161 C  CA    . LEU F 439 ? 0.806  0.2734 0.3459 -0.0669 0.2827 -0.0057 439 LEU Z CA    
10162 C  C     . LEU F 439 ? 0.7922 0.2755 0.3503 -0.0661 0.2804 -0.0034 439 LEU Z C     
10163 O  O     . LEU F 439 ? 0.7952 0.2797 0.3588 -0.0694 0.2813 -0.0016 439 LEU Z O     
10164 C  CB    . LEU F 439 ? 0.8154 0.2741 0.349  -0.0779 0.2796 -0.0057 439 LEU Z CB    
10165 C  CG    . LEU F 439 ? 0.8264 0.2958 0.3708 -0.0854 0.2718 -0.0043 439 LEU Z CG    
10166 C  CD1   . LEU F 439 ? 0.8295 0.3056 0.3759 -0.0821 0.2683 -0.0054 439 LEU Z CD1   
10167 C  CD2   . LEU F 439 ? 0.8422 0.3015 0.3781 -0.096  0.2691 -0.0044 439 LEU Z CD2   
10168 N  N     . ILE F 440 ? 0.7767 0.2719 0.3436 -0.0613 0.2778 -0.0034 440 ILE Z N     
10169 C  CA    . ILE F 440 ? 0.7663 0.2761 0.3494 -0.0594 0.276  -0.0012 440 ILE Z CA    
10170 C  C     . ILE F 440 ? 0.762  0.2822 0.3551 -0.0651 0.2691 0.0001  440 ILE Z C     
10171 O  O     . ILE F 440 ? 0.7649 0.2875 0.3566 -0.0641 0.2661 -0.0012 440 ILE Z O     
10172 C  CB    . ILE F 440 ? 0.7666 0.2821 0.3523 -0.0492 0.2788 -0.0018 440 ILE Z CB    
10173 C  CG1   . ILE F 440 ? 0.781  0.2863 0.3562 -0.043  0.2858 -0.003  440 ILE Z CG1   
10174 C  CG2   . ILE F 440 ? 0.7631 0.2923 0.3643 -0.047  0.2773 0.0004  440 ILE Z CG2   
10175 C  CD1   . ILE F 440 ? 0.7908 0.3014 0.3676 -0.0331 0.2886 -0.0035 440 ILE Z CD1   
10176 N  N     . ILE F 441 ? 0.7563 0.2828 0.3594 -0.0708 0.2667 0.0028  441 ILE Z N     
10177 C  CA    . ILE F 441 ? 0.7567 0.2942 0.3704 -0.0758 0.2603 0.0046  441 ILE Z CA    
10178 C  C     . ILE F 441 ? 0.7575 0.3082 0.3835 -0.069  0.2601 0.0059  441 ILE Z C     
10179 O  O     . ILE F 441 ? 0.7551 0.3126 0.391  -0.0676 0.2615 0.0084  441 ILE Z O     
10180 C  CB    . ILE F 441 ? 0.7605 0.2998 0.3797 -0.0849 0.2579 0.0073  441 ILE Z CB    
10181 C  CG1   . ILE F 441 ? 0.7847 0.3088 0.3896 -0.0916 0.2589 0.0058  441 ILE Z CG1   
10182 C  CG2   . ILE F 441 ? 0.7584 0.3097 0.3885 -0.09   0.2513 0.0096  441 ILE Z CG2   
10183 C  CD1   . ILE F 441 ? 0.8089 0.3259 0.4031 -0.095  0.2556 0.0034  441 ILE Z CD1   
10184 N  N     . ASN F 442 ? 0.7606 0.3139 0.3852 -0.0645 0.2587 0.0041  442 ASN Z N     
10185 C  CA    . ASN F 442 ? 0.7657 0.3293 0.3991 -0.0577 0.2586 0.0047  442 ASN Z CA    
10186 C  C     . ASN F 442 ? 0.7701 0.3456 0.4146 -0.0604 0.253  0.0066  442 ASN Z C     
10187 O  O     . ASN F 442 ? 0.7677 0.3509 0.4182 -0.055  0.2527 0.0069  442 ASN Z O     
10188 C  CB    . ASN F 442 ? 0.7833 0.3426 0.4079 -0.0512 0.2607 0.0017  442 ASN Z CB    
10189 C  CG    . ASN F 442 ? 0.8231 0.3895 0.4531 -0.0432 0.2626 0.0019  442 ASN Z CG    
10190 O  OD1   . ASN F 442 ? 0.8385 0.4059 0.4721 -0.0395 0.2662 0.003   442 ASN Z OD1   
10191 N  ND2   . ASN F 442 ? 0.8307 0.4016 0.4611 -0.0405 0.2601 0.0007  442 ASN Z ND2   
10192 N  N     . LYS F 443 ? 0.7734 0.3502 0.4203 -0.0686 0.2488 0.008   443 LYS Z N     
10193 C  CA    . LYS F 443 ? 0.777  0.3648 0.4339 -0.0716 0.2433 0.0101  443 LYS Z CA    
10194 C  C     . LYS F 443 ? 0.777  0.3768 0.4472 -0.067  0.2438 0.013   443 LYS Z C     
10195 O  O     . LYS F 443 ? 0.7767 0.3828 0.4507 -0.0636 0.2418 0.0128  443 LYS Z O     
10196 C  CB    . LYS F 443 ? 0.8    0.388  0.4583 -0.0814 0.2392 0.0119  443 LYS Z CB    
10197 C  CG    . LYS F 443 ? 0.8609 0.4412 0.5087 -0.0862 0.2359 0.0094  443 LYS Z CG    
10198 C  CD    . LYS F 443 ? 0.922  0.5052 0.5731 -0.0959 0.2306 0.0116  443 LYS Z CD    
10199 C  CE    . LYS F 443 ? 0.9803 0.5579 0.6225 -0.1001 0.2265 0.0094  443 LYS Z CE    
10200 N  NZ    . LYS F 443 ? 1.0045 0.5901 0.6514 -0.0962 0.2236 0.0089  443 LYS Z NZ    
10201 N  N     . ASN F 444 ? 0.7754 0.3776 0.452  -0.0669 0.2466 0.0157  444 ASN Z N     
10202 C  CA    . ASN F 444 ? 0.7754 0.3881 0.464  -0.0625 0.2475 0.0188  444 ASN Z CA    
10203 C  C     . ASN F 444 ? 0.7772 0.3892 0.4638 -0.0533 0.251  0.017   444 ASN Z C     
10204 O  O     . ASN F 444 ? 0.7741 0.394  0.4679 -0.0493 0.2504 0.0185  444 ASN Z O     
10205 C  CB    . ASN F 444 ? 0.7886 0.4042 0.4846 -0.0648 0.2496 0.0225  444 ASN Z CB    
10206 C  CG    . ASN F 444 ? 0.8295 0.4572 0.5391 -0.0621 0.2493 0.0268  444 ASN Z CG    
10207 O  OD1   . ASN F 444 ? 0.8465 0.4764 0.5617 -0.0592 0.2531 0.0293  444 ASN Z OD1   
10208 N  ND2   . ASN F 444 ? 0.8352 0.4709 0.5502 -0.0627 0.245  0.0279  444 ASN Z ND2   
10209 N  N     . ASN F 445 ? 0.7791 0.3816 0.4554 -0.0501 0.2548 0.014   445 ASN Z N     
10210 C  CA    . ASN F 445 ? 0.783  0.3846 0.4564 -0.0418 0.258  0.0122  445 ASN Z CA    
10211 C  C     . ASN F 445 ? 0.7847 0.3894 0.4565 -0.0399 0.2547 0.0103  445 ASN Z C     
10212 O  O     . ASN F 445 ? 0.7824 0.3922 0.4581 -0.0347 0.2551 0.0106  445 ASN Z O     
10213 C  CB    . ASN F 445 ? 0.8032 0.3942 0.4657 -0.0393 0.2625 0.0097  445 ASN Z CB    
10214 C  CG    . ASN F 445 ? 0.8474 0.4382 0.5081 -0.0308 0.2663 0.0086  445 ASN Z CG    
10215 O  OD1   . ASN F 445 ? 0.8638 0.4612 0.5319 -0.0269 0.2667 0.0102  445 ASN Z OD1   
10216 N  ND2   . ASN F 445 ? 0.858  0.4407 0.5082 -0.0278 0.2692 0.0059  445 ASN Z ND2   
10217 N  N     . LYS F 446 ? 0.7873 0.3886 0.4532 -0.0445 0.2514 0.0085  446 LYS Z N     
10218 C  CA    . LYS F 446 ? 0.7927 0.3964 0.4566 -0.0434 0.2481 0.0068  446 LYS Z CA    
10219 C  C     . LYS F 446 ? 0.7937 0.4078 0.4683 -0.0438 0.2447 0.0092  446 LYS Z C     
10220 O  O     . LYS F 446 ? 0.7933 0.4113 0.4691 -0.0394 0.2442 0.0086  446 LYS Z O     
10221 C  CB    . LYS F 446 ? 0.812  0.4095 0.4677 -0.0489 0.2453 0.0049  446 LYS Z CB    
10222 C  CG    . LYS F 446 ? 0.844  0.4451 0.4992 -0.0491 0.2412 0.0036  446 LYS Z CG    
10223 C  CD    . LYS F 446 ? 0.8858 0.48   0.5322 -0.0542 0.2388 0.0018  446 LYS Z CD    
10224 C  CE    . LYS F 446 ? 0.913  0.5113 0.56   -0.0546 0.2346 0.0009  446 LYS Z CE    
10225 N  NZ    . LYS F 446 ? 0.9355 0.5261 0.5727 -0.0587 0.2327 -0.0011 446 LYS Z NZ    
10226 N  N     . GLU F 447 ? 0.7936 0.4125 0.4759 -0.049  0.2426 0.0123  447 GLU Z N     
10227 C  CA    . GLU F 447 ? 0.7975 0.4266 0.4902 -0.0495 0.2395 0.0153  447 GLU Z CA    
10228 C  C     . GLU F 447 ? 0.7953 0.4289 0.4934 -0.0424 0.2426 0.0166  447 GLU Z C     
10229 O  O     . GLU F 447 ? 0.7954 0.4341 0.4966 -0.0397 0.2409 0.017   447 GLU Z O     
10230 C  CB    . GLU F 447 ? 0.8307 0.4644 0.531  -0.0559 0.2374 0.0189  447 GLU Z CB    
10231 C  CG    . GLU F 447 ? 0.9061 0.5377 0.6026 -0.0636 0.2328 0.0181  447 GLU Z CG    
10232 C  CD    . GLU F 447 ? 0.9979 0.634  0.7013 -0.0708 0.2304 0.0218  447 GLU Z CD    
10233 O  OE1   . GLU F 447 ? 1.0153 0.6567 0.7271 -0.0697 0.2326 0.0252  447 GLU Z OE1   
10234 O  OE2   . GLU F 447 ? 1.0319 0.6663 0.732  -0.0776 0.2262 0.0213  447 GLU Z OE2   
10235 N  N     . SER F 448 ? 0.7914 0.4221 0.4894 -0.0393 0.2472 0.0173  448 SER Z N     
10236 C  CA    . SER F 448 ? 0.7901 0.4236 0.4921 -0.0325 0.2506 0.0186  448 SER Z CA    
10237 C  C     . SER F 448 ? 0.7898 0.4207 0.4853 -0.027  0.2513 0.0154  448 SER Z C     
10238 O  O     . SER F 448 ? 0.7885 0.4235 0.4873 -0.023  0.2515 0.0162  448 SER Z O     
10239 C  CB    . SER F 448 ? 0.8101 0.4402 0.5126 -0.0308 0.2554 0.0197  448 SER Z CB    
10240 O  OG    . SER F 448 ? 0.8389 0.4723 0.5482 -0.0362 0.2545 0.023   448 SER Z OG    
10241 N  N     . ILE F 449 ? 0.7895 0.4136 0.4754 -0.027  0.2518 0.0119  449 ILE Z N     
10242 C  CA    . ILE F 449 ? 0.7939 0.4162 0.4736 -0.0222 0.2524 0.0091  449 ILE Z CA    
10243 C  C     . ILE F 449 ? 0.7952 0.4222 0.4762 -0.0231 0.2482 0.0086  449 ILE Z C     
10244 O  O     . ILE F 449 ? 0.7976 0.4265 0.4783 -0.0188 0.2485 0.008   449 ILE Z O     
10245 C  CB    . ILE F 449 ? 0.8045 0.4188 0.4738 -0.0217 0.2543 0.0061  449 ILE Z CB    
10246 C  CG1   . ILE F 449 ? 0.8168 0.4263 0.4843 -0.0194 0.2592 0.0066  449 ILE Z CG1   
10247 C  CG2   . ILE F 449 ? 0.8125 0.4263 0.4759 -0.0174 0.2543 0.0036  449 ILE Z CG2   
10248 C  CD1   . ILE F 449 ? 0.8381 0.4393 0.496  -0.0201 0.2612 0.0044  449 ILE Z CD1   
10249 N  N     . LEU F 450 ? 0.7929 0.4215 0.4754 -0.0289 0.2442 0.009   450 LEU Z N     
10250 C  CA    . LEU F 450 ? 0.7955 0.4283 0.4793 -0.0299 0.2401 0.0086  450 LEU Z CA    
10251 C  C     . LEU F 450 ? 0.8007 0.4407 0.4928 -0.0277 0.2396 0.0113  450 LEU Z C     
10252 O  O     . LEU F 450 ? 0.8037 0.4465 0.4959 -0.0271 0.2371 0.0108  450 LEU Z O     
10253 C  CB    . LEU F 450 ? 0.7927 0.4253 0.4758 -0.0366 0.236  0.0084  450 LEU Z CB    
10254 C  CG    . LEU F 450 ? 0.8108 0.4355 0.4841 -0.0388 0.2363 0.0055  450 LEU Z CG    
10255 C  CD1   . LEU F 450 ? 0.8186 0.4428 0.491  -0.0455 0.232  0.0055  450 LEU Z CD1   
10256 C  CD2   . LEU F 450 ? 0.8182 0.44   0.4841 -0.0346 0.2372 0.0025  450 LEU Z CD2   
10257 N  N     . ARG F 451 ? 0.7992 0.4415 0.4976 -0.0262 0.2421 0.0143  451 ARG Z N     
10258 C  CA    . ARG F 451 ? 0.8031 0.4514 0.5087 -0.0234 0.2423 0.0173  451 ARG Z CA    
10259 C  C     . ARG F 451 ? 0.8098 0.456  0.514  -0.0168 0.2466 0.0173  451 ARG Z C     
10260 O  O     . ARG F 451 ? 0.8107 0.4604 0.5205 -0.014  0.248  0.0203  451 ARG Z O     
10261 C  CB    . ARG F 451 ? 0.8191 0.4731 0.5342 -0.0268 0.2415 0.0216  451 ARG Z CB    
10262 C  CG    . ARG F 451 ? 0.8669 0.5221 0.5827 -0.034  0.2375 0.0217  451 ARG Z CG    
10263 C  CD    . ARG F 451 ? 0.912  0.5753 0.6379 -0.0374 0.2354 0.0263  451 ARG Z CD    
10264 N  NE    . ARG F 451 ? 0.9588 0.627  0.6868 -0.0387 0.2312 0.0269  451 ARG Z NE    
10265 C  CZ    . ARG F 451 ? 0.9972 0.6656 0.7231 -0.0442 0.2269 0.0257  451 ARG Z CZ    
10266 N  NH1   . ARG F 451 ? 0.9942 0.667  0.722  -0.0448 0.2235 0.0263  451 ARG Z NH1   
10267 N  NH2   . ARG F 451 ? 1.0015 0.665  0.7228 -0.0492 0.226  0.024   451 ARG Z NH2   
10268 N  N     . LYS F 452 ? 0.8138 0.4542 0.5102 -0.0142 0.2488 0.0142  452 LYS Z N     
10269 C  CA    . LYS F 452 ? 0.8206 0.4586 0.5149 -0.0082 0.2527 0.0141  452 LYS Z CA    
10270 C  C     . LYS F 452 ? 0.8252 0.4633 0.5154 -0.0048 0.2518 0.0124  452 LYS Z C     
10271 O  O     . LYS F 452 ? 0.8286 0.4657 0.5135 -0.0061 0.2495 0.0096  452 LYS Z O     
10272 C  CB    . LYS F 452 ? 0.8463 0.4784 0.5346 -0.0069 0.2558 0.012   452 LYS Z CB    
10273 C  CG    . LYS F 452 ? 0.8934 0.5231 0.5808 -0.0012 0.2604 0.0127  452 LYS Z CG    
10274 C  CD    . LYS F 452 ? 0.9483 0.5723 0.6306 -0.0002 0.2637 0.0113  452 LYS Z CD    
10275 C  CE    . LYS F 452 ? 0.9944 0.6161 0.6764 0.0053  0.2682 0.0123  452 LYS Z CE    
10276 N  NZ    . LYS F 452 ? 1.0225 0.6388 0.7004 0.0062  0.2718 0.0115  452 LYS Z NZ    
10277 N  N     . THR F 453 ? 0.8232 0.4622 0.5156 -0.0007 0.2538 0.0142  453 THR Z N     
10278 C  CA    . THR F 453 ? 0.8288 0.4669 0.5167 0.0026  0.2534 0.0129  453 THR Z CA    
10279 C  C     . THR F 453 ? 0.8338 0.4686 0.5197 0.008   0.2576 0.0136  453 THR Z C     
10280 O  O     . THR F 453 ? 0.8322 0.4675 0.5232 0.0096  0.2603 0.0166  453 THR Z O     
10281 C  CB    . THR F 453 ? 0.8402 0.4823 0.5322 0.0017  0.2509 0.0147  453 THR Z CB    
10282 O  OG1   . THR F 453 ? 0.8463 0.4907 0.5451 0.0033  0.253  0.0188  453 THR Z OG1   
10283 C  CG2   . THR F 453 ? 0.8453 0.4907 0.539  -0.0036 0.2465 0.0141  453 THR Z CG2   
10284 N  N     . SER F 454 ? 0.8387 0.4704 0.5173 0.0109  0.258  0.0112  454 SER Z N     
10285 C  CA    . SER F 454 ? 0.8494 0.4775 0.5251 0.016   0.2618 0.0117  454 SER Z CA    
10286 C  C     . SER F 454 ? 0.8545 0.4825 0.5319 0.0184  0.2625 0.0141  454 SER Z C     
10287 O  O     . SER F 454 ? 0.8556 0.4865 0.5354 0.0163  0.2598 0.0149  454 SER Z O     
10288 C  CB    . SER F 454 ? 0.8699 0.495  0.537  0.0179  0.2618 0.0085  454 SER Z CB    
10289 O  OG    . SER F 454 ? 0.9005 0.5266 0.5638 0.0168  0.2587 0.0069  454 SER Z OG    
10290 N  N     . LYS F 455 ? 0.8561 0.4805 0.532  0.023   0.2663 0.0155  455 LYS Z N     
10291 C  CA    . LYS F 455 ? 0.8625 0.4852 0.5387 0.0262  0.268  0.018   455 LYS Z CA    
10292 C  C     . LYS F 455 ? 0.8628 0.4851 0.5345 0.0254  0.265  0.0167  455 LYS Z C     
10293 O  O     . LYS F 455 ? 0.87   0.4903 0.5347 0.025   0.2634 0.0136  455 LYS Z O     
10294 C  CB    . LYS F 455 ? 0.8928 0.5097 0.5644 0.0314  0.2723 0.0184  455 LYS Z CB    
10295 C  CG    . LYS F 455 ? 0.9528 0.5663 0.6231 0.0353  0.2746 0.021   455 LYS Z CG    
10296 C  CD    . LYS F 455 ? 1.0195 0.6264 0.6838 0.0403  0.2786 0.021   455 LYS Z CD    
10297 C  CE    . LYS F 455 ? 1.0738 0.6762 0.736  0.0444  0.2814 0.0238  455 LYS Z CE    
10298 N  NZ    . LYS F 455 ? 1.1085 0.7036 0.7637 0.0491  0.2852 0.0236  455 LYS Z NZ    
10299 N  N     . GLN F 456 ? 0.8524 0.4767 0.5283 0.0252  0.2644 0.0194  456 GLN Z N     
10300 C  CA    . GLN F 456 ? 0.8539 0.4772 0.5254 0.0245  0.262  0.0185  456 GLN Z CA    
10301 C  C     . GLN F 456 ? 0.8507 0.467  0.5138 0.0286  0.2643 0.0182  456 GLN Z C     
10302 O  O     . GLN F 456 ? 0.8551 0.4683 0.519  0.0325  0.268  0.0212  456 GLN Z O     
10303 C  CB    . GLN F 456 ? 0.8755 0.5028 0.5536 0.0235  0.2611 0.0218  456 GLN Z CB    
10304 C  CG    . GLN F 456 ? 0.9205 0.5547 0.6068 0.0191  0.2586 0.0224  456 GLN Z CG    
10305 C  CD    . GLN F 456 ? 0.9784 0.6142 0.6616 0.0147  0.2543 0.0187  456 GLN Z CD    
10306 O  OE1   . GLN F 456 ? 0.9978 0.6321 0.6758 0.0141  0.2522 0.0169  456 GLN Z OE1   
10307 N  NE2   . GLN F 456 ? 0.9829 0.6213 0.6689 0.0115  0.253  0.0175  456 GLN Z NE2   
10308 N  N     . GLN F 457 ? 0.8399 0.4534 0.4948 0.0276  0.2622 0.0148  457 GLN Z N     
10309 C  CA    . GLN F 457 ? 0.8368 0.4432 0.4825 0.0306  0.2638 0.0141  457 GLN Z CA    
10310 C  C     . GLN F 457 ? 0.8249 0.4303 0.463  0.0278  0.2602 0.0108  457 GLN Z C     
10311 O  O     . GLN F 457 ? 0.8213 0.4311 0.4601 0.0245  0.2573 0.0084  457 GLN Z O     
10312 C  CB    . GLN F 457 ? 0.8607 0.4632 0.5033 0.0341  0.2672 0.014   457 GLN Z CB    
10313 C  CG    . GLN F 457 ? 0.902  0.5072 0.5436 0.0324  0.2658 0.0111  457 GLN Z CG    
10314 C  CD    . GLN F 457 ? 0.9528 0.554  0.5911 0.0362  0.2693 0.011   457 GLN Z CD    
10315 O  OE1   . GLN F 457 ? 0.9716 0.5751 0.6133 0.0364  0.2704 0.0107  457 GLN Z OE1   
10316 N  NE2   . GLN F 457 ? 0.9596 0.5541 0.5906 0.0394  0.2712 0.0113  457 GLN Z NE2   
10317 N  N     . ASN F 458 ? 0.8187 0.418  0.4491 0.0291  0.2606 0.0108  458 ASN Z N     
10318 C  CA    . ASN F 458 ? 0.8162 0.4141 0.4388 0.0262  0.2574 0.0078  458 ASN Z CA    
10319 C  C     . ASN F 458 ? 0.8054 0.4025 0.4222 0.0262  0.2568 0.0052  458 ASN Z C     
10320 O  O     . ASN F 458 ? 0.8114 0.4055 0.4267 0.0295  0.2598 0.0059  458 ASN Z O     
10321 C  CB    . ASN F 458 ? 0.8389 0.4292 0.4538 0.0276  0.2584 0.0088  458 ASN Z CB    
10322 C  CG    . ASN F 458 ? 0.8818 0.4723 0.5016 0.0285  0.2595 0.0118  458 ASN Z CG    
10323 O  OD1   . ASN F 458 ? 0.9027 0.4864 0.5181 0.0317  0.2624 0.014   458 ASN Z OD1   
10324 N  ND2   . ASN F 458 ? 0.8853 0.4833 0.5136 0.0258  0.2572 0.0122  458 ASN Z ND2   
10325 N  N     . ILE F 459 ? 0.7869 0.3872 0.4006 0.0226  0.2531 0.0025  459 ILE Z N     
10326 C  CA    . ILE F 459 ? 0.7771 0.378  0.3855 0.0224  0.2523 0.0004  459 ILE Z CA    
10327 C  C     . ILE F 459 ? 0.7663 0.3651 0.3659 0.0197  0.2494 -0.0015 459 ILE Z C     
10328 O  O     . ILE F 459 ? 0.7662 0.3667 0.3658 0.0165  0.2467 -0.0022 459 ILE Z O     
10329 C  CB    . ILE F 459 ? 0.778  0.3863 0.3923 0.0209  0.251  -0.0007 459 ILE Z CB    
10330 C  CG1   . ILE F 459 ? 0.7878 0.3969 0.409  0.0235  0.2542 0.001   459 ILE Z CG1   
10331 C  CG2   . ILE F 459 ? 0.7847 0.3951 0.3935 0.0203  0.2496 -0.0028 459 ILE Z CG2   
10332 C  CD1   . ILE F 459 ? 0.7996 0.4145 0.4263 0.0218  0.2532 0.0003  459 ILE Z CD1   
10333 N  N     . LEU F 460 ? 0.7561 0.3509 0.3479 0.021   0.25   -0.0023 460 LEU Z N     
10334 C  CA    . LEU F 460 ? 0.7543 0.3474 0.3371 0.0181  0.2472 -0.004  460 LEU Z CA    
10335 C  C     . LEU F 460 ? 0.7507 0.346  0.3303 0.0191  0.2471 -0.005  460 LEU Z C     
10336 O  O     . LEU F 460 ? 0.7554 0.3456 0.3312 0.0225  0.2498 -0.0043 460 LEU Z O     
10337 C  CB    . LEU F 460 ? 0.7618 0.3449 0.3362 0.0191  0.2486 -0.0033 460 LEU Z CB    
10338 C  CG    . LEU F 460 ? 0.7813 0.3613 0.3452 0.0155  0.2456 -0.005  460 LEU Z CG    
10339 C  CD1   . LEU F 460 ? 0.7859 0.3708 0.3517 0.0108  0.2419 -0.0062 460 LEU Z CD1   
10340 C  CD2   . LEU F 460 ? 0.7952 0.3635 0.3494 0.017   0.2477 -0.0042 460 LEU Z CD2   
10341 N  N     . VAL F 461 ? 0.7423 0.3454 0.3237 0.0165  0.2442 -0.0064 461 VAL Z N     
10342 C  CA    . VAL F 461 ? 0.743  0.3496 0.3221 0.0176  0.2441 -0.007  461 VAL Z CA    
10343 C  C     . VAL F 461 ? 0.7477 0.3506 0.3164 0.0165  0.2427 -0.0077 461 VAL Z C     
10344 O  O     . VAL F 461 ? 0.7521 0.3555 0.3164 0.0125  0.2395 -0.0086 461 VAL Z O     
10345 C  CB    . VAL F 461 ? 0.746  0.3622 0.33   0.0156  0.2419 -0.0078 461 VAL Z CB    
10346 C  CG1   . VAL F 461 ? 0.7515 0.3716 0.3332 0.0174  0.2422 -0.008  461 VAL Z CG1   
10347 C  CG2   . VAL F 461 ? 0.7478 0.3667 0.341  0.0162  0.2432 -0.0072 461 VAL Z CG2   
10348 N  N     . ASP F 462 ? 0.7458 0.3448 0.3104 0.02    0.245  -0.0072 462 ASP Z N     
10349 C  CA    . ASP F 462 ? 0.7519 0.3471 0.306  0.0189  0.2436 -0.0077 462 ASP Z CA    
10350 C  C     . ASP F 462 ? 0.7448 0.3494 0.2984 0.0159  0.24   -0.0086 462 ASP Z C     
10351 O  O     . ASP F 462 ? 0.7421 0.354  0.3012 0.0177  0.2405 -0.0084 462 ASP Z O     
10352 C  CB    . ASP F 462 ? 0.7779 0.3672 0.3284 0.0237  0.2472 -0.0069 462 ASP Z CB    
10353 C  CG    . ASP F 462 ? 0.8436 0.4276 0.3825 0.0229  0.2459 -0.0073 462 ASP Z CG    
10354 O  OD1   . ASP F 462 ? 0.8583 0.4356 0.3897 0.0201  0.2445 -0.0078 462 ASP Z OD1   
10355 O  OD2   . ASP F 462 ? 0.8718 0.4581 0.4086 0.025   0.2464 -0.0072 462 ASP Z OD2   
10356 N  N     . PRO F 463 ? 0.7397 0.3443 0.2864 0.0114  0.2363 -0.0094 463 PRO Z N     
10357 C  CA    . PRO F 463 ? 0.7347 0.3493 0.2813 0.0083  0.2327 -0.0099 463 PRO Z CA    
10358 C  C     . PRO F 463 ? 0.7381 0.357  0.2823 0.0105  0.2329 -0.0093 463 PRO Z C     
10359 O  O     . PRO F 463 ? 0.7367 0.3651 0.2817 0.0085  0.2302 -0.0091 463 PRO Z O     
10360 C  CB    . PRO F 463 ? 0.7443 0.3562 0.2832 0.0027  0.2291 -0.0107 463 PRO Z CB    
10361 C  CG    . PRO F 463 ? 0.7534 0.3549 0.2905 0.003   0.2309 -0.0108 463 PRO Z CG    
10362 C  CD    . PRO F 463 ? 0.7369 0.3324 0.2755 0.0087  0.2354 -0.0099 463 PRO Z CD    
10363 N  N     . THR F 464 ? 0.7401 0.3524 0.2812 0.0148  0.2361 -0.0088 464 THR Z N     
10364 C  CA    . THR F 464 ? 0.7447 0.3606 0.2833 0.0174  0.2366 -0.0082 464 THR Z CA    
10365 C  C     . THR F 464 ? 0.7473 0.3656 0.2934 0.0228  0.2405 -0.0074 464 THR Z C     
10366 O  O     . THR F 464 ? 0.7482 0.3595 0.2965 0.0261  0.2442 -0.0071 464 THR Z O     
10367 C  CB    . THR F 464 ? 0.7641 0.3709 0.2918 0.0176  0.2367 -0.0082 464 THR Z CB    
10368 O  OG1   . THR F 464 ? 0.7775 0.3844 0.298  0.0118  0.2323 -0.0089 464 THR Z OG1   
10369 C  CG2   . THR F 464 ? 0.7683 0.3774 0.2935 0.0214  0.2379 -0.0074 464 THR Z CG2   
10370 N  N     . PRO F 465 ? 0.7457 0.374  0.296  0.0236  0.24   -0.0069 465 PRO Z N     
10371 C  CA    . PRO F 465 ? 0.7487 0.3787 0.3053 0.0286  0.2438 -0.0062 465 PRO Z CA    
10372 C  C     . PRO F 465 ? 0.761  0.3872 0.3137 0.0334  0.2469 -0.0055 465 PRO Z C     
10373 O  O     . PRO F 465 ? 0.7664 0.3893 0.3111 0.0329  0.2456 -0.0055 465 PRO Z O     
10374 C  CB    . PRO F 465 ? 0.75   0.3914 0.3108 0.0276  0.2421 -0.0058 465 PRO Z CB    
10375 C  CG    . PRO F 465 ? 0.7539 0.4003 0.3087 0.0242  0.2381 -0.0056 465 PRO Z CG    
10376 C  CD    . PRO F 465 ? 0.7367 0.3751 0.2858 0.0203  0.236  -0.0066 465 PRO Z CD    
10377 N  N     . ASN F 466 ? 0.7625 0.3886 0.3203 0.0379  0.2509 -0.005  466 ASN Z N     
10378 C  CA    . ASN F 466 ? 0.7719 0.3945 0.3273 0.0431  0.2545 -0.0042 466 ASN Z CA    
10379 C  C     . ASN F 466 ? 0.7725 0.4018 0.323  0.0437  0.2526 -0.0036 466 ASN Z C     
10380 O  O     . ASN F 466 ? 0.7787 0.4039 0.3225 0.0456  0.2531 -0.0033 466 ASN Z O     
10381 C  CB    . ASN F 466 ? 0.7876 0.4109 0.3502 0.0467  0.2584 -0.0038 466 ASN Z CB    
10382 C  CG    . ASN F 466 ? 0.8394 0.4545 0.4018 0.0513  0.2631 -0.0032 466 ASN Z CG    
10383 O  OD1   . ASN F 466 ? 0.8592 0.4686 0.4255 0.0515  0.2652 -0.0032 466 ASN Z OD1   
10384 N  ND2   . ASN F 466 ? 0.8505 0.4657 0.4091 0.0554  0.2651 -0.0026 466 ASN Z ND2   
10385 N  N     . HIS F 467 ? 0.7654 0.4049 0.3188 0.042   0.2503 -0.0032 467 HIS Z N     
10386 C  CA    . HIS F 467 ? 0.7674 0.4154 0.317  0.0422  0.2482 -0.0021 467 HIS Z CA    
10387 C  C     . HIS F 467 ? 0.7587 0.4174 0.3119 0.0385  0.2448 -0.0017 467 HIS Z C     
10388 O  O     . HIS F 467 ? 0.7569 0.4163 0.3158 0.037   0.2449 -0.0023 467 HIS Z O     
10389 C  CB    . HIS F 467 ? 0.7817 0.4311 0.3313 0.0484  0.252  -0.0008 467 HIS Z CB    
10390 C  CG    . HIS F 467 ? 0.8133 0.4668 0.3695 0.0511  0.2549 -0.0003 467 HIS Z CG    
10391 N  ND1   . HIS F 467 ? 0.84   0.4874 0.4014 0.0519  0.2579 -0.0012 467 HIS Z ND1   
10392 C  CD2   . HIS F 467 ? 0.8264 0.4886 0.384  0.0534  0.2555 0.0011  467 HIS Z CD2   
10393 C  CE1   . HIS F 467 ? 0.845  0.4971 0.4103 0.0541  0.26   -0.0005 467 HIS Z CE1   
10394 N  NE2   . HIS F 467 ? 0.8415 0.5021 0.4045 0.0554  0.2589 0.001   467 HIS Z NE2   
10395 N  N     . TYR F 468 ? 0.7507 0.4177 0.3003 0.0369  0.2415 -0.0005 468 TYR Z N     
10396 C  CA    . TYR F 468 ? 0.745  0.4228 0.2976 0.0334  0.2382 0.0003  468 TYR Z CA    
10397 C  C     . TYR F 468 ? 0.7361 0.4227 0.2926 0.0377  0.2405 0.0022  468 TYR Z C     
10398 O  O     . TYR F 468 ? 0.7395 0.429  0.2932 0.0416  0.2418 0.0036  468 TYR Z O     
10399 C  CB    . TYR F 468 ? 0.7475 0.4297 0.2943 0.0284  0.2331 0.0007  468 TYR Z CB    
10400 C  CG    . TYR F 468 ? 0.7652 0.437  0.3069 0.0243  0.2314 -0.0012 468 TYR Z CG    
10401 C  CD1   . TYR F 468 ? 0.7767 0.4464 0.3205 0.0197  0.2294 -0.0025 468 TYR Z CD1   
10402 C  CD2   . TYR F 468 ? 0.7844 0.4473 0.3189 0.0256  0.2322 -0.0017 468 TYR Z CD2   
10403 C  CE1   . TYR F 468 ? 0.7947 0.454  0.3334 0.0165  0.2284 -0.0041 468 TYR Z CE1   
10404 C  CE2   . TYR F 468 ? 0.8029 0.4548 0.3321 0.0225  0.2313 -0.0032 468 TYR Z CE2   
10405 C  CZ    . TYR F 468 ? 0.8151 0.4654 0.3464 0.018   0.2295 -0.0044 468 TYR Z CZ    
10406 O  OH    . TYR F 468 ? 0.8452 0.4843 0.3705 0.0153  0.2289 -0.0057 468 TYR Z OH    
10407 N  N     . GLN F 469 ? 0.7238 0.4139 0.2862 0.0374  0.2412 0.0022  469 GLN Z N     
10408 C  CA    . GLN F 469 ? 0.7201 0.4169 0.2857 0.0417  0.244  0.004   469 GLN Z CA    
10409 C  C     . GLN F 469 ? 0.7067 0.4154 0.2747 0.0392  0.2411 0.0056  469 GLN Z C     
10410 O  O     . GLN F 469 ? 0.7081 0.4211 0.2746 0.0341  0.2366 0.0056  469 GLN Z O     
10411 C  CB    . GLN F 469 ? 0.7488 0.4382 0.3187 0.0444  0.2483 0.0028  469 GLN Z CB    
10412 C  CG    . GLN F 469 ? 0.8104 0.4882 0.3795 0.0458  0.2508 0.0012  469 GLN Z CG    
10413 C  CD    . GLN F 469 ? 0.8762 0.5477 0.4496 0.0431  0.2511 -0.0006 469 GLN Z CD    
10414 O  OE1   . GLN F 469 ? 0.8942 0.56   0.4668 0.0399  0.2494 -0.0019 469 GLN Z OE1   
10415 N  NE2   . GLN F 469 ? 0.8873 0.5592 0.4648 0.0443  0.2533 -0.0005 469 GLN Z NE2   
10416 N  N     . GLU F 470 ? 0.6922 0.4056 0.2635 0.0428  0.244  0.007   470 GLU Z N     
10417 C  CA    . GLU F 470 ? 0.6811 0.4051 0.255  0.0416  0.2424 0.0089  470 GLU Z CA    
10418 C  C     . GLU F 470 ? 0.6679 0.3914 0.2444 0.0354  0.2389 0.0074  470 GLU Z C     
10419 O  O     . GLU F 470 ? 0.6672 0.4001 0.2444 0.0323  0.2357 0.0088  470 GLU Z O     
10420 C  CB    . GLU F 470 ? 0.7068 0.4314 0.2828 0.047   0.2472 0.0102  470 GLU Z CB    
10421 C  CG    . GLU F 470 ? 0.7565 0.4922 0.3344 0.0474  0.2465 0.0129  470 GLU Z CG    
10422 C  CD    . GLU F 470 ? 0.8291 0.564  0.4075 0.0532  0.2517 0.0143  470 GLU Z CD    
10423 O  OE1   . GLU F 470 ? 0.8414 0.579  0.422  0.0525  0.252  0.0149  470 GLU Z OE1   
10424 O  OE2   . GLU F 470 ? 0.8566 0.5878 0.4327 0.0584  0.2556 0.0148  470 GLU Z OE2   
10425 N  N     . ASN F 471 ? 0.6559 0.369  0.2337 0.0336  0.2396 0.0047  471 ASN Z N     
10426 C  CA    . ASN F 471 ? 0.6489 0.361  0.2288 0.028   0.2364 0.0032  471 ASN Z CA    
10427 C  C     . ASN F 471 ? 0.6432 0.3575 0.2197 0.0228  0.2317 0.0029  471 ASN Z C     
10428 O  O     . ASN F 471 ? 0.646  0.3654 0.2237 0.0182  0.2284 0.003   471 ASN Z O     
10429 C  CB    . ASN F 471 ? 0.6598 0.361  0.2421 0.0275  0.2381 0.0008  471 ASN Z CB    
10430 C  CG    . ASN F 471 ? 0.6877 0.3898 0.2738 0.0243  0.2369 0.0001  471 ASN Z CG    
10431 O  OD1   . ASN F 471 ? 0.6985 0.3962 0.2875 0.0258  0.2394 -0.0006 471 ASN Z OD1   
10432 N  ND2   . ASN F 471 ? 0.6888 0.3966 0.2747 0.0196  0.2328 0.0002  471 ASN Z ND2   
10433 N  N     . ASP F 472 ? 0.6334 0.3438 0.2054 0.0233  0.2314 0.0026  472 ASP Z N     
10434 C  CA    . ASP F 472 ? 0.6305 0.3417 0.1977 0.0183  0.2271 0.0023  472 ASP Z CA    
10435 C  C     . ASP F 472 ? 0.626  0.3503 0.1922 0.0169  0.2241 0.0049  472 ASP Z C     
10436 O  O     . ASP F 472 ? 0.6277 0.3557 0.1921 0.0112  0.2199 0.0049  472 ASP Z O     
10437 C  CB    . ASP F 472 ? 0.6463 0.3481 0.2081 0.0194  0.2279 0.0012  472 ASP Z CB    
10438 C  CG    . ASP F 472 ? 0.6924 0.3822 0.2557 0.0203  0.2306 -0.001  472 ASP Z CG    
10439 O  OD1   . ASP F 472 ? 0.6879 0.3741 0.2522 0.0162  0.2288 -0.0025 472 ASP Z OD1   
10440 O  OD2   . ASP F 472 ? 0.7312 0.4158 0.2952 0.0252  0.2345 -0.0011 472 ASP Z OD2   
10441 N  N     . VAL F 473 ? 0.6181 0.3498 0.1856 0.022   0.2265 0.0074  473 VAL Z N     
10442 C  CA    . VAL F 473 ? 0.6159 0.3618 0.1835 0.0214  0.2241 0.0106  473 VAL Z CA    
10443 C  C     . VAL F 473 ? 0.6142 0.3671 0.1863 0.0179  0.2222 0.0112  473 VAL Z C     
10444 O  O     . VAL F 473 ? 0.6134 0.3743 0.1847 0.013   0.218  0.0124  473 VAL Z O     
10445 C  CB    . VAL F 473 ? 0.6232 0.3752 0.1918 0.0285  0.2279 0.0133  473 VAL Z CB    
10446 C  CG1   . VAL F 473 ? 0.6254 0.3932 0.195  0.0282  0.2256 0.0172  473 VAL Z CG1   
10447 C  CG2   . VAL F 473 ? 0.6344 0.3797 0.1983 0.032   0.2297 0.0128  473 VAL Z CG2   
10448 N  N     . ASP F 474 ? 0.613  0.3618 0.1893 0.0201  0.2252 0.0103  474 ASP Z N     
10449 C  CA    . ASP F 474 ? 0.6142 0.3675 0.1945 0.0174  0.2241 0.0106  474 ASP Z CA    
10450 C  C     . ASP F 474 ? 0.6152 0.3654 0.1945 0.0101  0.2198 0.0085  474 ASP Z C     
10451 O  O     . ASP F 474 ? 0.614  0.3725 0.1949 0.0064  0.217  0.0098  474 ASP Z O     
10452 C  CB    . ASP F 474 ? 0.637  0.3841 0.2207 0.0212  0.2284 0.0096  474 ASP Z CB    
10453 C  CG    . ASP F 474 ? 0.6922 0.4456 0.2773 0.0275  0.2322 0.0124  474 ASP Z CG    
10454 O  OD1   . ASP F 474 ? 0.7004 0.4651 0.2868 0.0276  0.2312 0.0154  474 ASP Z OD1   
10455 O  OD2   . ASP F 474 ? 0.718  0.4647 0.3024 0.0325  0.2364 0.0119  474 ASP Z OD2   
10456 N  N     . THR F 475 ? 0.6152 0.3537 0.1918 0.0083  0.2196 0.0056  475 THR Z N     
10457 C  CA    . THR F 475 ? 0.6174 0.3511 0.1919 0.0018  0.216  0.0035  475 THR Z CA    
10458 C  C     . THR F 475 ? 0.6144 0.3554 0.1847 -0.0031 0.2115 0.0049  475 THR Z C     
10459 O  O     . THR F 475 ? 0.6086 0.3534 0.1791 -0.0084 0.2082 0.0049  475 THR Z O     
10460 C  CB    . THR F 475 ? 0.6374 0.357  0.209  0.0021  0.2174 0.0008  475 THR Z CB    
10461 O  OG1   . THR F 475 ? 0.6494 0.363  0.2255 0.0053  0.2209 -0.0004 475 THR Z OG1   
10462 C  CG2   . THR F 475 ? 0.6464 0.3602 0.214  -0.0041 0.214  -0.0011 475 THR Z CG2   
10463 N  N     . VAL F 476 ? 0.6169 0.3602 0.1834 -0.0014 0.2113 0.0061  476 VAL Z N     
10464 C  CA    . VAL F 476 ? 0.6219 0.3722 0.1838 -0.006  0.2069 0.0077  476 VAL Z CA    
10465 C  C     . VAL F 476 ? 0.6166 0.3828 0.1827 -0.0072 0.205  0.011   476 VAL Z C     
10466 O  O     . VAL F 476 ? 0.6186 0.39   0.1835 -0.0135 0.2009 0.0115  476 VAL Z O     
10467 C  CB    . VAL F 476 ? 0.6349 0.3833 0.1915 -0.0033 0.2074 0.0083  476 VAL Z CB    
10468 C  CG1   . VAL F 476 ? 0.642  0.4004 0.1945 -0.0077 0.2028 0.0106  476 VAL Z CG1   
10469 C  CG2   . VAL F 476 ? 0.647  0.3796 0.1982 -0.0035 0.2085 0.0051  476 VAL Z CG2   
10470 N  N     . ILE F 477 ? 0.6079 0.3815 0.179  -0.0011 0.2083 0.0134  477 ILE Z N     
10471 C  CA    . ILE F 477 ? 0.604  0.3927 0.1793 -0.0011 0.2074 0.0171  477 ILE Z CA    
10472 C  C     . ILE F 477 ? 0.6012 0.3908 0.1799 -0.0055 0.2058 0.0163  477 ILE Z C     
10473 O  O     . ILE F 477 ? 0.5966 0.3965 0.1762 -0.01   0.2024 0.0184  477 ILE Z O     
10474 C  CB    . ILE F 477 ? 0.6111 0.4049 0.19   0.0072  0.2122 0.0196  477 ILE Z CB    
10475 C  CG1   . ILE F 477 ? 0.6243 0.421  0.1999 0.0111  0.213  0.0213  477 ILE Z CG1   
10476 C  CG2   . ILE F 477 ? 0.6127 0.42   0.1967 0.0082  0.2125 0.0232  477 ILE Z CG2   
10477 C  CD1   . ILE F 477 ? 0.6367 0.4463 0.2104 0.0074  0.2086 0.0245  477 ILE Z CD1   
10478 N  N     . TYR F 478 ? 0.6027 0.3815 0.183  -0.0044 0.2082 0.0134  478 TYR Z N     
10479 C  CA    . TYR F 478 ? 0.6068 0.3848 0.1899 -0.0081 0.2071 0.0123  478 TYR Z CA    
10480 C  C     . TYR F 478 ? 0.6136 0.3901 0.193  -0.0162 0.2022 0.011   478 TYR Z C     
10481 O  O     . TYR F 478 ? 0.6154 0.3993 0.1966 -0.0203 0.1997 0.0122  478 TYR Z O     
10482 C  CB    . TYR F 478 ? 0.6108 0.3765 0.1958 -0.0056 0.2104 0.0093  478 TYR Z CB    
10483 C  CG    . TYR F 478 ? 0.6212 0.3859 0.2091 -0.0087 0.2095 0.0083  478 TYR Z CG    
10484 C  CD1   . TYR F 478 ? 0.6295 0.4018 0.2216 -0.0066 0.2109 0.0104  478 TYR Z CD1   
10485 C  CD2   . TYR F 478 ? 0.6366 0.3923 0.2225 -0.0136 0.2074 0.0053  478 TYR Z CD2   
10486 C  CE1   . TYR F 478 ? 0.6408 0.4119 0.2353 -0.0094 0.2101 0.0095  478 TYR Z CE1   
10487 C  CE2   . TYR F 478 ? 0.6477 0.4024 0.2361 -0.0164 0.2066 0.0044  478 TYR Z CE2   
10488 C  CZ    . TYR F 478 ? 0.6557 0.4182 0.2485 -0.0144 0.2079 0.0064  478 TYR Z CZ    
10489 O  OH    . TYR F 478 ? 0.6753 0.4364 0.2703 -0.017  0.2071 0.0055  478 TYR Z OH    
10490 N  N     . SER F 479 ? 0.6172 0.3838 0.1908 -0.0183 0.2011 0.0086  479 SER Z N     
10491 C  CA    . SER F 479 ? 0.6232 0.3861 0.1917 -0.0258 0.1969 0.0071  479 SER Z CA    
10492 C  C     . SER F 479 ? 0.6219 0.3975 0.1888 -0.0305 0.1927 0.01    479 SER Z C     
10493 O  O     . SER F 479 ? 0.6192 0.398  0.1856 -0.0366 0.1895 0.0101  479 SER Z O     
10494 C  CB    . SER F 479 ? 0.645  0.3942 0.2068 -0.0261 0.1972 0.0044  479 SER Z CB    
10495 O  OG    . SER F 479 ? 0.6754 0.4137 0.2394 -0.022  0.201  0.0021  479 SER Z OG    
10496 N  N     . ILE F 480 ? 0.6226 0.4061 0.1889 -0.0276 0.1928 0.0126  480 ILE Z N     
10497 C  CA    . ILE F 480 ? 0.6287 0.4256 0.1937 -0.0317 0.1888 0.0159  480 ILE Z CA    
10498 C  C     . ILE F 480 ? 0.6316 0.4429 0.2033 -0.0328 0.1879 0.0191  480 ILE Z C     
10499 O  O     . ILE F 480 ? 0.631  0.4485 0.2016 -0.0396 0.1838 0.0201  480 ILE Z O     
10500 C  CB    . ILE F 480 ? 0.6339 0.4357 0.1971 -0.0273 0.1896 0.0181  480 ILE Z CB    
10501 C  CG1   . ILE F 480 ? 0.6527 0.441  0.2076 -0.0284 0.1891 0.0152  480 ILE Z CG1   
10502 C  CG2   . ILE F 480 ? 0.6336 0.4531 0.198  -0.0298 0.1861 0.0227  480 ILE Z CG2   
10503 C  CD1   . ILE F 480 ? 0.6667 0.4571 0.2197 -0.023  0.1908 0.0167  480 ILE Z CD1   
10504 N  N     . PHE F 481 ? 0.6332 0.4492 0.2112 -0.026  0.192  0.0208  481 PHE Z N     
10505 C  CA    . PHE F 481 ? 0.6356 0.4654 0.2198 -0.0258 0.1919 0.0243  481 PHE Z CA    
10506 C  C     . PHE F 481 ? 0.6517 0.4773 0.2385 -0.0286 0.192  0.0225  481 PHE Z C     
10507 O  O     . PHE F 481 ? 0.6527 0.4895 0.2437 -0.0299 0.1911 0.0254  481 PHE Z O     
10508 C  CB    . PHE F 481 ? 0.6272 0.4643 0.2158 -0.0171 0.1964 0.0275  481 PHE Z CB    
10509 C  CG    . PHE F 481 ? 0.6269 0.4731 0.2138 -0.0149 0.1957 0.0307  481 PHE Z CG    
10510 C  CD1   . PHE F 481 ? 0.6284 0.4906 0.2166 -0.0185 0.1921 0.0349  481 PHE Z CD1   
10511 C  CD2   . PHE F 481 ? 0.6387 0.4781 0.223  -0.0094 0.1986 0.0296  481 PHE Z CD2   
10512 C  CE1   . PHE F 481 ? 0.634  0.5053 0.2207 -0.0165 0.1912 0.0381  481 PHE Z CE1   
10513 C  CE2   . PHE F 481 ? 0.6463 0.4941 0.2288 -0.0072 0.198  0.0326  481 PHE Z CE2   
10514 C  CZ    . PHE F 481 ? 0.6371 0.5009 0.2208 -0.0108 0.1942 0.0368  481 PHE Z CZ    
10515 N  N     . LYS F 482 ? 0.6635 0.4738 0.2479 -0.0294 0.1929 0.0181  482 LYS Z N     
10516 C  CA    . LYS F 482 ? 0.6763 0.4824 0.2631 -0.032  0.1929 0.0164  482 LYS Z CA    
10517 C  C     . LYS F 482 ? 0.6929 0.493  0.2749 -0.0402 0.1888 0.014   482 LYS Z C     
10518 O  O     . LYS F 482 ? 0.6902 0.4922 0.2739 -0.044  0.1874 0.0139  482 LYS Z O     
10519 C  CB    . LYS F 482 ? 0.7006 0.4951 0.2893 -0.0268 0.1972 0.0136  482 LYS Z CB    
10520 C  CG    . LYS F 482 ? 0.7488 0.5413 0.341  -0.0277 0.1979 0.0127  482 LYS Z CG    
10521 C  CD    . LYS F 482 ? 0.7934 0.5999 0.3905 -0.0262 0.1984 0.0167  482 LYS Z CD    
10522 C  CE    . LYS F 482 ? 0.8379 0.6415 0.4382 -0.0257 0.1999 0.0159  482 LYS Z CE    
10523 N  NZ    . LYS F 482 ? 0.8584 0.6754 0.4628 -0.0246 0.2004 0.0201  482 LYS Z NZ    
10524 N  N     . TYR F 483 ? 0.7091 0.5015 0.2844 -0.0429 0.187  0.0121  483 TYR Z N     
10525 C  CA    . TYR F 483 ? 0.7272 0.5117 0.2964 -0.0505 0.1835 0.0097  483 TYR Z CA    
10526 C  C     . TYR F 483 ? 0.737  0.5269 0.3003 -0.0568 0.179  0.0111  483 TYR Z C     
10527 O  O     . TYR F 483 ? 0.7358 0.5249 0.2957 -0.0641 0.1756 0.0105  483 TYR Z O     
10528 C  CB    . TYR F 483 ? 0.7369 0.5039 0.3018 -0.0491 0.1855 0.0056  483 TYR Z CB    
10529 C  CG    . TYR F 483 ? 0.7502 0.5118 0.3206 -0.0443 0.1893 0.0041  483 TYR Z CG    
10530 C  CD1   . TYR F 483 ? 0.7609 0.5241 0.3348 -0.0465 0.1888 0.0039  483 TYR Z CD1   
10531 C  CD2   . TYR F 483 ? 0.7643 0.5199 0.3365 -0.0377 0.1932 0.0032  483 TYR Z CD2   
10532 C  CE1   . TYR F 483 ? 0.7733 0.5318 0.352  -0.0424 0.192  0.0026  483 TYR Z CE1   
10533 C  CE2   . TYR F 483 ? 0.7765 0.5276 0.3536 -0.0338 0.1963 0.002   483 TYR Z CE2   
10534 C  CZ    . TYR F 483 ? 0.7872 0.5396 0.3673 -0.0362 0.1957 0.0017  483 TYR Z CZ    
10535 O  OH    . TYR F 483 ? 0.809  0.5568 0.3934 -0.0327 0.1985 0.0006  483 TYR Z OH    
10536 N  N     . ILE F 484 ? 0.7478 0.5426 0.3094 -0.0545 0.1788 0.0129  484 ILE Z N     
10537 C  CA    . ILE F 484 ? 0.7669 0.5664 0.3223 -0.0607 0.1743 0.0143  484 ILE Z CA    
10538 C  C     . ILE F 484 ? 0.7784 0.5976 0.3387 -0.0633 0.1715 0.0191  484 ILE Z C     
10539 O  O     . ILE F 484 ? 0.7803 0.6035 0.3382 -0.0712 0.1674 0.0198  484 ILE Z O     
10540 C  CB    . ILE F 484 ? 0.7757 0.5694 0.3255 -0.0577 0.1749 0.0137  484 ILE Z CB    
10541 C  CG1   . ILE F 484 ? 0.7963 0.5703 0.3407 -0.0562 0.1774 0.0093  484 ILE Z CG1   
10542 C  CG2   . ILE F 484 ? 0.7815 0.5806 0.3244 -0.0644 0.1699 0.0154  484 ILE Z CG2   
10543 C  CD1   . ILE F 484 ? 0.8162 0.5836 0.3563 -0.0517 0.1792 0.0086  484 ILE Z CD1   
10544 N  N     . VAL F 485 ? 0.7836 0.615  0.3504 -0.0568 0.1738 0.0226  485 VAL Z N     
10545 C  CA    . VAL F 485 ? 0.7932 0.6442 0.3651 -0.0581 0.1717 0.0279  485 VAL Z CA    
10546 C  C     . VAL F 485 ? 0.8087 0.6667 0.3868 -0.0601 0.1717 0.0292  485 VAL Z C     
10547 O  O     . VAL F 485 ? 0.8097 0.6645 0.3927 -0.0547 0.1757 0.0284  485 VAL Z O     
10548 C  CB    . VAL F 485 ? 0.796  0.6571 0.3723 -0.0499 0.1747 0.0314  485 VAL Z CB    
10549 C  CG1   . VAL F 485 ? 0.7932 0.6756 0.3752 -0.0508 0.1728 0.0374  485 VAL Z CG1   
10550 C  CG2   . VAL F 485 ? 0.8051 0.6599 0.3749 -0.0485 0.1743 0.0303  485 VAL Z CG2   
10551 N  N     . PRO F 486 ? 0.8185 0.6859 0.396  -0.0681 0.1671 0.0313  486 PRO Z N     
10552 C  CA    . PRO F 486 ? 0.8247 0.6983 0.4075 -0.0705 0.1669 0.0326  486 PRO Z CA    
10553 C  C     . PRO F 486 ? 0.8303 0.7199 0.4225 -0.0644 0.1697 0.0375  486 PRO Z C     
10554 O  O     . PRO F 486 ? 0.8275 0.728  0.4223 -0.0599 0.1706 0.0413  486 PRO Z O     
10555 C  CB    . PRO F 486 ? 0.8314 0.7105 0.4101 -0.0811 0.161  0.0337  486 PRO Z CB    
10556 C  CG    . PRO F 486 ? 0.8339 0.719  0.4087 -0.0824 0.1584 0.0357  486 PRO Z CG    
10557 C  CD    . PRO F 486 ? 0.8162 0.6876 0.3873 -0.0758 0.1617 0.0324  486 PRO Z CD    
10558 N  N     . ASN F 487 ? 0.8354 0.726  0.4321 -0.0645 0.1711 0.0377  487 ASN Z N     
10559 C  CA    . ASN F 487 ? 0.8403 0.7437 0.4452 -0.0589 0.1742 0.0421  487 ASN Z CA    
10560 C  C     . ASN F 487 ? 0.8518 0.7547 0.4592 -0.0487 0.1793 0.043   487 ASN Z C     
10561 O  O     . ASN F 487 ? 0.8457 0.763  0.4576 -0.044  0.1809 0.0481  487 ASN Z O     
10562 C  CB    . ASN F 487 ? 0.8456 0.7692 0.4544 -0.0631 0.171  0.048   487 ASN Z CB    
10563 C  CG    . ASN F 487 ? 0.8862 0.8103 0.4931 -0.0732 0.1664 0.0472  487 ASN Z CG    
10564 O  OD1   . ASN F 487 ? 0.8995 0.8253 0.51   -0.0742 0.1673 0.0477  487 ASN Z OD1   
10565 N  ND2   . ASN F 487 ? 0.8961 0.8181 0.4965 -0.0811 0.1615 0.046   487 ASN Z ND2   
10566 N  N     . CYS F 488 ? 0.8674 0.7535 0.4716 -0.0452 0.1821 0.0382  488 CYS Z N     
10567 C  CA    . CYS F 488 ? 0.8831 0.7648 0.4884 -0.036  0.1871 0.038   488 CYS Z CA    
10568 C  C     . CYS F 488 ? 0.8962 0.7683 0.5038 -0.0317 0.1913 0.0357  488 CYS Z C     
10569 O  O     . CYS F 488 ? 0.9013 0.7655 0.5081 -0.036  0.19   0.0326  488 CYS Z O     
10570 C  CB    . CYS F 488 ? 0.9011 0.7715 0.5006 -0.0356 0.1867 0.0346  488 CYS Z CB    
10571 S  SG    . CYS F 488 ? 0.9507 0.8334 0.5486 -0.0345 0.1849 0.0386  488 CYS Z SG    
10572 N  N     . PHE F 489 ? 0.9013 0.7733 0.5112 -0.0232 0.1962 0.037   489 PHE Z N     
10573 C  CA    . PHE F 489 ? 0.9171 0.7798 0.5285 -0.019  0.2002 0.0349  489 PHE Z CA    
10574 C  C     . PHE F 489 ? 0.9302 0.7845 0.5404 -0.0112 0.2049 0.0337  489 PHE Z C     
10575 O  O     . PHE F 489 ? 0.9281 0.7899 0.5389 -0.006  0.207  0.037   489 PHE Z O     
10576 C  CB    . PHE F 489 ? 0.9132 0.7868 0.5293 -0.0172 0.2018 0.0391  489 PHE Z CB    
10577 C  CG    . PHE F 489 ? 0.9264 0.7902 0.5433 -0.0135 0.2056 0.037   489 PHE Z CG    
10578 C  CD1   . PHE F 489 ? 0.942  0.795  0.5577 -0.0182 0.204  0.0329  489 PHE Z CD1   
10579 C  CD2   . PHE F 489 ? 0.9359 0.8006 0.554  -0.0054 0.2108 0.0394  489 PHE Z CD2   
10580 C  CE1   . PHE F 489 ? 0.9544 0.7985 0.5705 -0.015  0.2072 0.0311  489 PHE Z CE1   
10581 C  CE2   . PHE F 489 ? 0.9493 0.8041 0.5672 -0.0025 0.2141 0.0374  489 PHE Z CE2   
10582 C  CZ    . PHE F 489 ? 0.9514 0.7962 0.5684 -0.0074 0.2121 0.0333  489 PHE Z CZ    
10583 N  N     . SER F 490 ? 0.941  0.7797 0.5494 -0.0106 0.2065 0.0291  490 SER Z N     
10584 C  CA    . SER F 490 ? 0.9546 0.7841 0.5616 -0.004  0.2109 0.0275  490 SER Z CA    
10585 C  C     . SER F 490 ? 0.961  0.7884 0.5701 0.0014  0.2154 0.0284  490 SER Z C     
10586 O  O     . SER F 490 ? 0.9666 0.7826 0.5752 0.0008  0.2164 0.0251  490 SER Z O     
10587 C  CB    . SER F 490 ? 0.9785 0.7927 0.5824 -0.0064 0.2101 0.0223  490 SER Z CB    
10588 O  OG    . SER F 490 ? 1.0094 0.8143 0.6124 -0.0005 0.2144 0.0208  490 SER Z OG    
10589 N  N     . GLY F 491 ? 0.9591 0.7971 0.5699 0.0066  0.2182 0.0331  491 GLY Z N     
10590 C  CA    . GLY F 491 ? 0.9689 0.8047 0.5804 0.0123  0.2229 0.0345  491 GLY Z CA    
10591 C  C     . GLY F 491 ? 0.9817 0.8047 0.5904 0.0175  0.2271 0.0319  491 GLY Z C     
10592 O  O     . GLY F 491 ? 0.9877 0.8011 0.5954 0.0191  0.2297 0.03    491 GLY Z O     
10593 N  N     . MET F 492 ? 0.9844 0.8067 0.5913 0.02    0.2278 0.0318  492 MET Z N     
10594 C  CA    . MET F 492 ? 0.9969 0.8074 0.6011 0.0248  0.2318 0.0296  492 MET Z CA    
10595 C  C     . MET F 492 ? 1.0028 0.8058 0.6052 0.0222  0.2297 0.0261  492 MET Z C     
10596 O  O     . MET F 492 ? 1.0009 0.8106 0.6031 0.0196  0.2265 0.0269  492 MET Z O     
10597 C  CB    . MET F 492 ? 1.0059 0.8221 0.6089 0.0327  0.2365 0.0337  492 MET Z CB    
10598 C  CG    . MET F 492 ? 1.0361 0.8479 0.6379 0.038   0.2415 0.0349  492 MET Z CG    
10599 S  SD    . MET F 492 ? 1.0846 0.8887 0.6819 0.0466  0.248  0.0354  492 MET Z SD    
10600 C  CE    . MET F 492 ? 1.0678 0.856  0.6638 0.043   0.2466 0.0292  492 MET Z CE    
10601 N  N     . CYS F 493 ? 1.0076 0.7967 0.6085 0.023   0.2316 0.0223  493 CYS Z N     
10602 C  CA    . CYS F 493 ? 1.0171 0.7979 0.6162 0.0215  0.2305 0.0192  493 CYS Z CA    
10603 C  C     . CYS F 493 ? 1.0262 0.7942 0.6239 0.0252  0.2346 0.0167  493 CYS Z C     
10604 O  O     . CYS F 493 ? 1.0294 0.7888 0.6278 0.023   0.2345 0.0141  493 CYS Z O     
10605 C  CB    . CYS F 493 ? 1.0271 0.8049 0.6265 0.0141  0.2256 0.0163  493 CYS Z CB    
10606 S  SG    . CYS F 493 ? 1.0718 0.845  0.6681 0.0121  0.2235 0.0143  493 CYS Z SG    
10607 N  N     . ASN F 494 ? 1.0273 0.7942 0.6231 0.0307  0.238  0.0178  494 ASN Z N     
10608 C  CA    . ASN F 494 ? 1.0365 0.7918 0.6305 0.0345  0.2422 0.016   494 ASN Z CA    
10609 C  C     . ASN F 494 ? 1.0397 0.7897 0.6321 0.0355  0.2426 0.0144  494 ASN Z C     
10610 O  O     . ASN F 494 ? 1.041  0.7919 0.6313 0.0408  0.2459 0.0161  494 ASN Z O     
10611 C  CB    . ASN F 494 ? 1.0506 0.8075 0.6429 0.0411  0.2473 0.0188  494 ASN Z CB    
10612 C  CG    . ASN F 494 ? 1.0903 0.8398 0.6821 0.0413  0.2494 0.0178  494 ASN Z CG    
10613 O  OD1   . ASN F 494 ? 1.1004 0.8543 0.6935 0.0393  0.2481 0.0188  494 ASN Z OD1   
10614 N  ND2   . ASN F 494 ? 1.1036 0.8414 0.6932 0.0434  0.2527 0.0157  494 ASN Z ND2   
10615 N  N     . PRO F 495 ? 1.0395 0.7832 0.6324 0.0308  0.2397 0.0113  495 PRO Z N     
10616 C  CA    . PRO F 495 ? 1.0436 0.7812 0.6346 0.032   0.2403 0.0098  495 PRO Z CA    
10617 C  C     . PRO F 495 ? 1.0512 0.778  0.6415 0.0359  0.2449 0.0084  495 PRO Z C     
10618 O  O     . PRO F 495 ? 1.0541 0.7776 0.6451 0.0371  0.2471 0.0083  495 PRO Z O     
10619 C  CB    . PRO F 495 ? 1.0522 0.7864 0.6436 0.0257  0.2359 0.0073  495 PRO Z CB    
10620 C  CG    . PRO F 495 ? 1.0535 0.7933 0.647  0.0212  0.2328 0.0077  495 PRO Z CG    
10621 C  CD    . PRO F 495 ? 1.0325 0.7739 0.6273 0.0246  0.2359 0.0091  495 PRO Z CD    
10622 N  N     . PRO F 496 ? 1.0536 0.7743 0.6424 0.0378  0.2464 0.0073  496 PRO Z N     
10623 C  CA    . PRO F 496 ? 1.0596 0.7702 0.6479 0.041   0.2507 0.0061  496 PRO Z CA    
10624 C  C     . PRO F 496 ? 1.0657 0.7683 0.6565 0.0374  0.2501 0.0036  496 PRO Z C     
10625 O  O     . PRO F 496 ? 1.068  0.7679 0.6604 0.0331  0.247  0.0017  496 PRO Z O     
10626 C  CB    . PRO F 496 ? 1.0692 0.7756 0.6558 0.0426  0.2515 0.0053  496 PRO Z CB    
10627 C  CG    . PRO F 496 ? 1.0715 0.787  0.6565 0.042   0.2486 0.007   496 PRO Z CG    
10628 C  CD    . PRO F 496 ? 1.048  0.7701 0.6348 0.037   0.2444 0.0072  496 PRO Z CD    
10629 N  N     . GLY F 497 ? 1.0664 0.7652 0.6571 0.0392  0.2531 0.0037  497 GLY Z N     
10630 C  CA    . GLY F 497 ? 1.0734 0.7648 0.6661 0.036   0.2526 0.0016  497 GLY Z CA    
10631 C  C     . GLY F 497 ? 1.0744 0.7701 0.669  0.0318  0.2492 0.0014  497 GLY Z C     
10632 O  O     . GLY F 497 ? 1.0737 0.7651 0.6707 0.0276  0.247  -0.0005 497 GLY Z O     
10633 N  N     . GLY F 498 ? 1.0747 0.7793 0.6684 0.033   0.2488 0.0037  498 GLY Z N     
10634 C  CA    . GLY F 498 ? 1.0827 0.7923 0.6779 0.0293  0.2456 0.0039  498 GLY Z CA    
10635 C  C     . GLY F 498 ? 1.0924 0.801  0.6864 0.0308  0.2478 0.0049  498 GLY Z C     
10636 O  O     . GLY F 498 ? 1.0954 0.8014 0.6866 0.0355  0.2521 0.0061  498 GLY Z O     
10637 N  N     . ASP F 499 ? 1.0953 0.8058 0.6911 0.0269  0.245  0.0044  499 ASP Z N     
10638 C  CA    . ASP F 499 ? 1.105  0.8144 0.6994 0.0275  0.2464 0.0052  499 ASP Z CA    
10639 C  C     . ASP F 499 ? 1.1116 0.8298 0.7041 0.0318  0.2486 0.0089  499 ASP Z C     
10640 O  O     . ASP F 499 ? 1.1104 0.8373 0.7034 0.0333  0.2481 0.0108  499 ASP Z O     
10641 C  CB    . ASP F 499 ? 1.1213 0.8311 0.7182 0.0219  0.2424 0.0037  499 ASP Z CB    
10642 C  CG    . ASP F 499 ? 1.1706 0.8713 0.7692 0.0182  0.2408 0.0006  499 ASP Z CG    
10643 O  OD1   . ASP F 499 ? 1.1759 0.8722 0.7752 0.0184  0.2412 -0.0007 499 ASP Z OD1   
10644 O  OD2   . ASP F 499 ? 1.1978 0.8959 0.7971 0.015   0.2392 -0.0004 499 ASP Z OD2   
10645 N  N     . TRP F 500 ? 1.1162 0.8323 0.7062 0.0336  0.251  0.01    500 TRP Z N     
10646 C  CA    . TRP F 500 ? 1.1229 0.8471 0.711  0.0378  0.2533 0.0138  500 TRP Z CA    
10647 C  C     . TRP F 500 ? 1.1271 0.8595 0.7184 0.0336  0.2493 0.0145  500 TRP Z C     
10648 O  O     . TRP F 500 ? 1.1319 0.8609 0.7228 0.0317  0.2489 0.0138  500 TRP Z O     
10649 C  CB    . TRP F 500 ? 1.1274 0.8434 0.7104 0.0416  0.258  0.0145  500 TRP Z CB    
10650 C  CG    . TRP F 500 ? 1.1353 0.8497 0.7139 0.0484  0.2634 0.0167  500 TRP Z CG    
10651 C  CD1   . TRP F 500 ? 1.1478 0.8633 0.7218 0.0539  0.2679 0.02    500 TRP Z CD1   
10652 C  CD2   . TRP F 500 ? 1.1375 0.8476 0.715  0.0506  0.2653 0.0157  500 TRP Z CD2   
10653 N  NE1   . TRP F 500 ? 1.1535 0.866  0.7236 0.0595  0.2724 0.0212  500 TRP Z NE1   
10654 C  CE2   . TRP F 500 ? 1.1496 0.8588 0.7219 0.0575  0.2709 0.0185  500 TRP Z CE2   
10655 C  CE3   . TRP F 500 ? 1.1433 0.8503 0.7237 0.0478  0.263  0.013   500 TRP Z CE3   
10656 C  CZ2   . TRP F 500 ? 1.1586 0.8638 0.7286 0.0613  0.2741 0.0185  500 TRP Z CZ2   
10657 C  CZ3   . TRP F 500 ? 1.1559 0.8592 0.7341 0.0516  0.2662 0.0131  500 TRP Z CZ3   
10658 C  CH2   . TRP F 500 ? 1.1595 0.8618 0.7325 0.0582  0.2716 0.0157  500 TRP Z CH2   
10659 N  N     . SER F 501 ? 1.1232 0.8658 0.7176 0.0316  0.246  0.0155  501 SER Z N     
10660 C  CA    . SER F 501 ? 1.1264 0.8768 0.7239 0.0269  0.2418 0.0159  501 SER Z CA    
10661 C  C     . SER F 501 ? 1.1304 0.8895 0.7277 0.0291  0.2432 0.0198  501 SER Z C     
10662 O  O     . SER F 501 ? 1.133  0.891  0.7309 0.0265  0.242  0.0193  501 SER Z O     
10663 C  CB    . SER F 501 ? 1.1376 0.8952 0.7373 0.0237  0.238  0.0159  501 SER Z CB    
10664 O  OG    . SER F 501 ? 1.1592 0.9246 0.7614 0.0188  0.2339 0.0165  501 SER Z OG    
10665 N  N     . GLY F 502 ? 1.129  0.8967 0.7256 0.0341  0.2457 0.0237  502 GLY Z N     
10666 C  CA    . GLY F 502 ? 1.1333 0.911  0.7302 0.0368  0.2472 0.0281  502 GLY Z CA    
10667 C  C     . GLY F 502 ? 1.1328 0.9261 0.7333 0.0351  0.2441 0.0312  502 GLY Z C     
10668 O  O     . GLY F 502 ? 1.1334 0.9284 0.7358 0.0307  0.2401 0.0293  502 GLY Z O     
10669 N  N     . LEU F 503 ? 1.1299 0.9347 0.7313 0.0385  0.2458 0.0362  503 LEU Z N     
10670 C  CA    . LEU F 503 ? 1.131  0.9518 0.736  0.0368  0.2427 0.0397  503 LEU Z CA    
10671 C  C     . LEU F 503 ? 1.131  0.9606 0.7394 0.0326  0.2399 0.0416  503 LEU Z C     
10672 O  O     . LEU F 503 ? 1.1341 0.9646 0.7419 0.0357  0.2429 0.044   503 LEU Z O     
10673 C  CB    . LEU F 503 ? 1.1328 0.9629 0.737  0.0442  0.2468 0.0449  503 LEU Z CB    
10674 C  CG    . LEU F 503 ? 1.148  0.9966 0.7561 0.0431  0.244  0.0496  503 LEU Z CG    
10675 C  CD1   . LEU F 503 ? 1.1554 1.0061 0.7648 0.0377  0.2389 0.0473  503 LEU Z CD1   
10676 C  CD2   . LEU F 503 ? 1.1545 1.0122 0.7618 0.0513  0.2487 0.0554  503 LEU Z CD2   
10677 N  N     . SER F 504 ? 1.1268 0.9631 0.7383 0.0259  0.2344 0.0408  504 SER Z N     
10678 C  CA    . SER F 504 ? 1.1288 0.9743 0.7436 0.0213  0.2314 0.0427  504 SER Z CA    
10679 C  C     . SER F 504 ? 1.1262 0.9896 0.7442 0.0204  0.2292 0.0476  504 SER Z C     
10680 O  O     . SER F 504 ? 1.1279 0.9943 0.7458 0.0187  0.2267 0.0471  504 SER Z O     
10681 C  CB    . SER F 504 ? 1.1468 0.985  0.7619 0.0133  0.2267 0.0379  504 SER Z CB    
10682 O  OG    . SER F 504 ? 1.1803 1.0038 0.7931 0.0136  0.2283 0.034   504 SER Z OG    
10683 N  N     . ILE F 505 ? 1.1203 0.9956 0.7411 0.0216  0.23   0.0525  505 ILE Z N     
10684 C  CA    . ILE F 505 ? 1.1188 1.013  0.7435 0.0205  0.2278 0.0579  505 ILE Z CA    
10685 C  C     . ILE F 505 ? 1.1254 1.0266 0.7535 0.0144  0.2245 0.059   505 ILE Z C     
10686 O  O     . ILE F 505 ? 1.1288 1.0267 0.7569 0.0163  0.2271 0.0596  505 ILE Z O     
10687 C  CB    . ILE F 505 ? 1.118  1.022  0.7433 0.0295  0.2332 0.0643  505 ILE Z CB    
10688 C  CG1   . ILE F 505 ? 1.1322 1.0278 0.7533 0.0365  0.2375 0.0633  505 ILE Z CG1   
10689 C  CG2   . ILE F 505 ? 1.1147 1.0396 0.7447 0.0283  0.2307 0.0704  505 ILE Z CG2   
10690 C  CD1   . ILE F 505 ? 1.148  1.0454 0.7687 0.0346  0.2346 0.062   505 ILE Z CD1   
10691 N  N     . ILE F 506 ? 1.126  1.0364 0.7565 0.0072  0.2189 0.0595  506 ILE Z N     
10692 C  CA    . ILE F 506 ? 1.1344 1.052  0.7679 0.0009  0.2157 0.0607  506 ILE Z CA    
10693 C  C     . ILE F 506 ? 1.1373 1.076  0.7757 0.0021  0.2155 0.0683  506 ILE Z C     
10694 O  O     . ILE F 506 ? 1.1361 1.0851 0.7755 0.0013  0.2134 0.0708  506 ILE Z O     
10695 C  CB    . ILE F 506 ? 1.1432 1.0552 0.7753 -0.0087 0.2097 0.0559  506 ILE Z CB    
10696 C  CG1   . ILE F 506 ? 1.1639 1.0557 0.7919 -0.0093 0.2103 0.0491  506 ILE Z CG1   
10697 C  CG2   . ILE F 506 ? 1.1452 1.0659 0.7803 -0.0155 0.2061 0.0577  506 ILE Z CG2   
10698 C  CD1   . ILE F 506 ? 1.1849 1.0695 0.8104 -0.0173 0.2053 0.0444  506 ILE Z CD1   
10699 N  N     . ARG F 507 ? 1.1392 1.0843 0.7803 0.0042  0.2179 0.0721  507 ARG Z N     
10700 C  CA    . ARG F 507 ? 1.141  1.1068 0.7873 0.0059  0.2182 0.0799  507 ARG Z CA    
10701 C  C     . ARG F 507 ? 1.1401 1.1116 0.7897 0.0028  0.2178 0.0822  507 ARG Z C     
10702 O  O     . ARG F 507 ? 1.146  1.1074 0.7938 0.0062  0.2214 0.0807  507 ARG Z O     
10703 C  CB    . ARG F 507 ? 1.1643 1.1342 0.8102 0.0168  0.2246 0.0846  507 ARG Z CB    
10704 C  CG    . ARG F 507 ? 1.2082 1.2    0.8596 0.0199  0.2257 0.0934  507 ARG Z CG    
10705 C  CD    . ARG F 507 ? 1.2548 1.2619 0.9094 0.015   0.2206 0.0961  507 ARG Z CD    
10706 N  NE    . ARG F 507 ? 1.2928 1.3222 0.9533 0.0179  0.2216 0.105   507 ARG Z NE    
10707 C  CZ    . ARG F 507 ? 1.3188 1.3659 0.9837 0.0124  0.2166 0.109   507 ARG Z CZ    
10708 N  NH1   . ARG F 507 ? 1.3166 1.3607 0.9797 0.0037  0.2103 0.1046  507 ARG Z NH1   
10709 N  NH2   . ARG F 507 ? 1.3118 1.3797 0.9825 0.0156  0.2179 0.1175  507 ARG Z NH2   
10710 N  N     . ASN F 508 ? 1.1312 1.1185 0.7854 -0.0038 0.2132 0.0857  508 ASN Z N     
10711 C  CA    . ASN F 508 ? 1.1315 1.1269 0.7896 -0.0077 0.2122 0.0886  508 ASN Z CA    
10712 C  C     . ASN F 508 ? 1.1382 1.1177 0.7933 -0.013  0.2106 0.0822  508 ASN Z C     
10713 O  O     . ASN F 508 ? 1.1414 1.1209 0.7979 -0.0122 0.2127 0.0836  508 ASN Z O     
10714 C  CB    . ASN F 508 ? 1.1427 1.1479 0.8039 0.001   0.2181 0.0955  508 ASN Z CB    
10715 C  CG    . ASN F 508 ? 1.1772 1.1999 0.8419 0.0066  0.2199 0.1027  508 ASN Z CG    
10716 O  OD1   . ASN F 508 ? 1.1875 1.222  0.8545 0.002   0.2154 0.1045  508 ASN Z OD1   
10717 N  ND2   . ASN F 508 ? 1.1852 1.2094 0.8496 0.0169  0.2267 0.107   508 ASN Z ND2   
10718 N  N     . GLY F 509 ? 1.1383 1.1047 0.7893 -0.0183 0.2071 0.0755  509 GLY Z N     
10719 C  CA    . GLY F 509 ? 1.1455 1.0966 0.7935 -0.0234 0.2055 0.0694  509 GLY Z CA    
10720 C  C     . GLY F 509 ? 1.1487 1.0823 0.7928 -0.0174 0.21   0.0654  509 GLY Z C     
10721 O  O     . GLY F 509 ? 1.1561 1.0773 0.7979 -0.0207 0.2092 0.0608  509 GLY Z O     
10722 N  N     . HIS F 510 ? 1.141  1.0731 0.784  -0.0087 0.2148 0.0671  510 HIS Z N     
10723 C  CA    . HIS F 510 ? 1.1465 1.0621 0.7852 -0.0028 0.2193 0.0636  510 HIS Z CA    
10724 C  C     . HIS F 510 ? 1.1447 1.0511 0.7799 0       0.2201 0.0603  510 HIS Z C     
10725 O  O     . HIS F 510 ? 1.1426 1.0578 0.779  0.0008  0.2191 0.0626  510 HIS Z O     
10726 C  CB    . HIS F 510 ? 1.1557 1.0758 0.7949 0.0057  0.2253 0.0689  510 HIS Z CB    
10727 C  CG    . HIS F 510 ? 1.1805 1.1066 0.8223 0.0041  0.2256 0.0718  510 HIS Z CG    
10728 N  ND1   . HIS F 510 ? 1.195  1.1404 0.8422 0.0041  0.2254 0.0787  510 HIS Z ND1   
10729 C  CD2   . HIS F 510 ? 1.1988 1.1142 0.8386 0.0025  0.2262 0.0689  510 HIS Z CD2   
10730 C  CE1   . HIS F 510 ? 1.2009 1.1465 0.8492 0.0025  0.2259 0.0797  510 HIS Z CE1   
10731 N  NE2   . HIS F 510 ? 1.2079 1.1355 0.8516 0.0016  0.2264 0.0738  510 HIS Z NE2   
10732 N  N     . GLU F 511 ? 1.1431 1.0318 0.7741 0.0014  0.2217 0.055   511 GLU Z N     
10733 C  CA    . GLU F 511 ? 1.1447 1.0238 0.7724 0.0044  0.2229 0.0518  511 GLU Z CA    
10734 C  C     . GLU F 511 ? 1.1432 1.0148 0.7678 0.0129  0.2292 0.0527  511 GLU Z C     
10735 O  O     . GLU F 511 ? 1.1494 1.0112 0.7719 0.0137  0.231  0.0508  511 GLU Z O     
10736 C  CB    . GLU F 511 ? 1.1757 1.0402 0.8009 -0.0013 0.2196 0.0449  511 GLU Z CB    
10737 C  CG    . GLU F 511 ? 1.231  1.0853 0.853  0.0017  0.2211 0.0417  511 GLU Z CG    
10738 C  CD    . GLU F 511 ? 1.3031 1.1426 0.9227 -0.0029 0.2186 0.0354  511 GLU Z CD    
10739 O  OE1   . GLU F 511 ? 1.3184 1.1488 0.9356 -0.0003 0.22   0.0327  511 GLU Z OE1   
10740 O  OE2   . GLU F 511 ? 1.3272 1.1644 0.9474 -0.0088 0.2153 0.0332  511 GLU Z OE2   
10741 N  N     . PHE F 512 ? 1.1342 1.0103 0.7582 0.0193  0.2325 0.0558  512 PHE Z N     
10742 C  CA    . PHE F 512 ? 1.1372 1.0059 0.7571 0.0278  0.2388 0.057   512 PHE Z CA    
10743 C  C     . PHE F 512 ? 1.1391 0.9941 0.7552 0.029   0.2396 0.0522  512 PHE Z C     
10744 O  O     . PHE F 512 ? 1.1386 0.9965 0.7558 0.0267  0.2368 0.051   512 PHE Z O     
10745 C  CB    . PHE F 512 ? 1.1318 1.0152 0.7533 0.0347  0.2425 0.0641  512 PHE Z CB    
10746 C  CG    . PHE F 512 ? 1.134  1.0336 0.7604 0.0332  0.2414 0.0696  512 PHE Z CG    
10747 C  CD1   . PHE F 512 ? 1.1445 1.043  0.77   0.0364  0.2449 0.0721  512 PHE Z CD1   
10748 C  CD2   . PHE F 512 ? 1.1376 1.0532 0.7692 0.0284  0.2368 0.0723  512 PHE Z CD2   
10749 C  CE1   . PHE F 512 ? 1.147  1.0607 0.7774 0.035   0.2441 0.0773  512 PHE Z CE1   
10750 C  CE2   . PHE F 512 ? 1.1396 1.0705 0.7761 0.0266  0.2357 0.0775  512 PHE Z CE2   
10751 C  CZ    . PHE F 512 ? 1.1374 1.0675 0.7735 0.03    0.2394 0.08    512 PHE Z CZ    
10752 N  N     . ARG F 513 ? 1.1395 0.9797 0.7509 0.0324  0.2432 0.0495  513 ARG Z N     
10753 C  CA    . ARG F 513 ? 1.1454 0.9723 0.7534 0.0332  0.244  0.045   513 ARG Z CA    
10754 C  C     . ARG F 513 ? 1.148  0.9651 0.7503 0.0408  0.2503 0.0456  513 ARG Z C     
10755 O  O     . ARG F 513 ? 1.1519 0.9634 0.7513 0.0431  0.2533 0.0464  513 ARG Z O     
10756 C  CB    . ARG F 513 ? 1.1661 0.9814 0.7739 0.0263  0.24   0.039   513 ARG Z CB    
10757 C  CG    . ARG F 513 ? 1.2093 1.0124 0.8147 0.026   0.24   0.0344  513 ARG Z CG    
10758 C  CD    . ARG F 513 ? 1.2518 1.0483 0.8587 0.0186  0.2351 0.0295  513 ARG Z CD    
10759 N  NE    . ARG F 513 ? 1.2951 1.0798 0.9001 0.0183  0.2352 0.0253  513 ARG Z NE    
10760 C  CZ    . ARG F 513 ? 1.3243 1.1103 0.9298 0.0176  0.2337 0.0244  513 ARG Z CZ    
10761 N  NH1   . ARG F 513 ? 1.315  1.1136 0.9226 0.017   0.2319 0.0273  513 ARG Z NH1   
10762 N  NH2   . ARG F 513 ? 1.3293 1.1042 0.9333 0.0174  0.2341 0.0207  513 ARG Z NH2   
10763 N  N     . TRP F 514 ? 1.144  0.9586 0.7443 0.0445  0.2523 0.0454  514 TRP Z N     
10764 C  CA    . TRP F 514 ? 1.1493 0.9537 0.7436 0.0515  0.2583 0.0457  514 TRP Z CA    
10765 C  C     . TRP F 514 ? 1.1586 0.947  0.7504 0.0485  0.2574 0.0396  514 TRP Z C     
10766 O  O     . TRP F 514 ? 1.1584 0.9467 0.7524 0.0453  0.2542 0.037   514 TRP Z O     
10767 C  CB    . TRP F 514 ? 1.1436 0.9557 0.7374 0.0575  0.2613 0.0494  514 TRP Z CB    
10768 C  CG    . TRP F 514 ? 1.1412 0.9675 0.7361 0.0629  0.2642 0.0563  514 TRP Z CG    
10769 C  CD1   . TRP F 514 ? 1.1536 0.9782 0.7436 0.071   0.2708 0.0602  514 TRP Z CD1   
10770 C  CD2   . TRP F 514 ? 1.1338 0.9785 0.7349 0.0606  0.2608 0.0603  514 TRP Z CD2   
10771 N  NE1   . TRP F 514 ? 1.1507 0.9921 0.744  0.0743  0.2718 0.0667  514 TRP Z NE1   
10772 C  CE2   . TRP F 514 ? 1.1404 0.9949 0.7409 0.0677  0.2655 0.0669  514 TRP Z CE2   
10773 C  CE3   . TRP F 514 ? 1.1354 0.9891 0.7422 0.0529  0.2542 0.0591  514 TRP Z CE3   
10774 C  CZ2   . TRP F 514 ? 1.1399 1.0138 0.7461 0.0674  0.2637 0.0725  514 TRP Z CZ2   
10775 C  CZ3   . TRP F 514 ? 1.1379 1.01   0.7498 0.0521  0.2522 0.0643  514 TRP Z CZ3   
10776 C  CH2   . TRP F 514 ? 1.1363 1.0188 0.7482 0.0592  0.2568 0.071   514 TRP Z CH2   
10777 N  N     . LEU F 515 ? 1.1664 0.9414 0.7534 0.0495  0.26   0.0375  515 LEU Z N     
10778 C  CA    . LEU F 515 ? 1.1817 0.9417 0.7664 0.0468  0.2593 0.0322  515 LEU Z CA    
10779 C  C     . LEU F 515 ? 1.1978 0.9477 0.7758 0.0531  0.2652 0.0326  515 LEU Z C     
10780 O  O     . LEU F 515 ? 1.1997 0.9532 0.7743 0.0596  0.2699 0.0368  515 LEU Z O     
10781 C  CB    . LEU F 515 ? 1.1872 0.9388 0.7711 0.0422  0.2574 0.0293  515 LEU Z CB    
10782 C  CG    . LEU F 515 ? 1.2026 0.9629 0.792  0.0363  0.2522 0.0291  515 LEU Z CG    
10783 C  CD1   . LEU F 515 ? 1.2138 0.9663 0.8013 0.0336  0.2516 0.0274  515 LEU Z CD1   
10784 C  CD2   . LEU F 515 ? 1.21   0.9721 0.804  0.0304  0.247  0.0259  515 LEU Z CD2   
10785 N  N     . SER F 516 ? 1.2073 0.9448 0.7833 0.0513  0.265  0.0283  516 SER Z N     
10786 C  CA    . SER F 516 ? 1.2236 0.95   0.793  0.0562  0.2703 0.028   516 SER Z CA    
10787 C  C     . SER F 516 ? 1.229  0.9631 0.7974 0.0628  0.2739 0.0319  516 SER Z C     
10788 O  O     . SER F 516 ? 1.2327 0.9647 0.7953 0.0692  0.2795 0.035   516 SER Z O     
10789 C  CB    . SER F 516 ? 1.2482 0.9642 0.8104 0.0587  0.2743 0.0286  516 SER Z CB    
10790 O  OG    . SER F 516 ? 1.2802 0.9905 0.8433 0.0529  0.2708 0.0256  516 SER Z OG    
10791 N  N     . LEU F 517 ? 1.2288 0.972  0.8025 0.0612  0.2708 0.0318  517 LEU Z N     
10792 C  CA    . LEU F 517 ? 1.2368 0.9885 0.8101 0.0669  0.2735 0.0354  517 LEU Z CA    
10793 C  C     . LEU F 517 ? 1.2536 0.9939 0.8212 0.0713  0.2781 0.0343  517 LEU Z C     
10794 O  O     . LEU F 517 ? 1.2592 0.9925 0.8278 0.0681  0.2763 0.0304  517 LEU Z O     
10795 C  CB    . LEU F 517 ? 1.2327 0.9958 0.8124 0.0632  0.2684 0.0352  517 LEU Z CB    
10796 C  CG    . LEU F 517 ? 1.2463 1.0209 0.8318 0.0579  0.2631 0.0361  517 LEU Z CG    
10797 C  CD1   . LEU F 517 ? 1.2498 1.0337 0.8399 0.0544  0.2585 0.0357  517 LEU Z CD1   
10798 C  CD2   . LEU F 517 ? 1.2513 1.0369 0.8369 0.0618  0.2653 0.0415  517 LEU Z CD2   
10799 N  N     . PRO F 518 ? 1.2582 0.997  0.8198 0.0789  0.2843 0.0379  518 PRO Z N     
10800 C  CA    . PRO F 518 ? 1.2689 0.9965 0.8246 0.0831  0.289  0.0368  518 PRO Z CA    
10801 C  C     . PRO F 518 ? 1.2743 1.0092 0.8329 0.0849  0.2883 0.0375  518 PRO Z C     
10802 O  O     . PRO F 518 ? 1.271  1.0209 0.8338 0.0862  0.2867 0.041   518 PRO Z O     
10803 C  CB    . PRO F 518 ? 1.2792 1.0037 0.8272 0.0907  0.2959 0.0409  518 PRO Z CB    
10804 C  CG    . PRO F 518 ? 1.2766 1.0168 0.8284 0.0924  0.2949 0.0456  518 PRO Z CG    
10805 C  CD    . PRO F 518 ? 1.2503 0.9971 0.8099 0.0842  0.2877 0.0432  518 PRO Z CD    
10806 N  N     . ARG F 519 ? 1.2804 1.005  0.837  0.0845  0.2893 0.0343  519 ARG Z N     
10807 C  CA    . ARG F 519 ? 1.286  1.0159 0.8445 0.0865  0.2891 0.0347  519 ARG Z CA    
10808 C  C     . ARG F 519 ? 1.2925 1.0268 0.8462 0.0954  0.295  0.0396  519 ARG Z C     
10809 O  O     . ARG F 519 ? 1.29   1.0366 0.8466 0.0979  0.2941 0.0425  519 ARG Z O     
10810 C  CB    . ARG F 519 ? 1.3043 1.0213 0.8616 0.0843  0.2892 0.0302  519 ARG Z CB    
10811 C  CG    . ARG F 519 ? 1.3294 1.052  0.8899 0.0846  0.2874 0.03    519 ARG Z CG    
10812 C  CD    . ARG F 519 ? 1.3662 1.0761 0.923  0.0862  0.2906 0.0274  519 ARG Z CD    
10813 N  NE    . ARG F 519 ? 1.3966 1.1004 0.9458 0.0935  0.2977 0.0298  519 ARG Z NE    
10814 C  CZ    . ARG F 519 ? 1.4152 1.1242 0.9619 0.1002  0.3012 0.033   519 ARG Z CZ    
10815 N  NH1   . ARG F 519 ? 1.4038 1.1245 0.955  0.1002  0.2981 0.0343  519 ARG Z NH1   
10816 N  NH2   . ARG F 519 ? 1.4168 1.1187 0.9557 0.1068  0.3079 0.0351  519 ARG Z NH2   
10817 N  N     . VAL F 520 ? 1.2984 1.0226 0.8444 0.1003  0.301  0.0408  520 VAL Z N     
10818 C  CA    . VAL F 520 ? 1.305  1.0313 0.8451 0.1094  0.3075 0.0455  520 VAL Z CA    
10819 C  C     . VAL F 520 ? 1.3018 1.0439 0.8441 0.1131  0.3079 0.0513  520 VAL Z C     
10820 O  O     . VAL F 520 ? 1.3045 1.0464 0.8457 0.1128  0.3085 0.0526  520 VAL Z O     
10821 C  CB    . VAL F 520 ? 1.3232 1.0318 0.853  0.1134  0.3143 0.0447  520 VAL Z CB    
10822 C  CG1   . VAL F 520 ? 1.3351 1.0317 0.8624 0.1125  0.3154 0.0408  520 VAL Z CG1   
10823 C  CG2   . VAL F 520 ? 1.333  1.0323 0.8602 0.1094  0.3137 0.0427  520 VAL Z CG2   
10824 N  N     . SER F 521 ? 1.2917 1.0479 0.8374 0.1166  0.3075 0.0549  521 SER Z N     
10825 C  CA    . SER F 521 ? 1.2855 1.0588 0.8339 0.1207  0.308  0.0612  521 SER Z CA    
10826 C  C     . SER F 521 ? 1.2824 1.0592 0.8264 0.1298  0.3137 0.0655  521 SER Z C     
10827 O  O     . SER F 521 ? 1.2852 1.0605 0.8293 0.1302  0.3132 0.0638  521 SER Z O     
10828 C  CB    . SER F 521 ? 1.2924 1.0819 0.8504 0.1144  0.3004 0.0614  521 SER Z CB    
10829 O  OG    . SER F 521 ? 1.3129 1.1204 0.8739 0.1186  0.3009 0.068   521 SER Z OG    
10830 N  N     . GLU F 522 ? 1.2746 1.0551 0.8141 0.1375  0.3195 0.0711  522 GLU Z N     
10831 C  CA    . GLU F 522 ? 1.2728 1.0562 0.8072 0.1472  0.3258 0.0759  522 GLU Z CA    
10832 C  C     . GLU F 522 ? 1.2603 1.0603 0.801  0.1479  0.3225 0.0784  522 GLU Z C     
10833 O  O     . GLU F 522 ? 1.2637 1.0601 0.8009 0.1523  0.3254 0.0784  522 GLU Z O     
10834 C  CB    . GLU F 522 ? 1.2965 1.0834 0.8259 0.1554  0.3323 0.0823  522 GLU Z CB    
10835 C  CG    . GLU F 522 ? 1.3391 1.1309 0.8715 0.1522  0.3303 0.0837  522 GLU Z CG    
10836 C  CD    . GLU F 522 ? 1.4042 1.177  0.9309 0.1486  0.3314 0.079   522 GLU Z CD    
10837 O  OE1   . GLU F 522 ? 1.4112 1.1789 0.9421 0.1396  0.3254 0.0732  522 GLU Z OE1   
10838 O  OE2   . GLU F 522 ? 1.4311 1.1939 0.9486 0.1547  0.3383 0.0813  522 GLU Z OE2   
10839 N  N     . ASN F 523 ? 1.243  1.0603 0.7925 0.1432  0.3162 0.0803  523 ASN Z N     
10840 C  CA    . ASN F 523 ? 1.2301 1.0637 0.7854 0.1429  0.3123 0.0828  523 ASN Z CA    
10841 C  C     . ASN F 523 ? 1.2113 1.0482 0.7738 0.1326  0.3036 0.078   523 ASN Z C     
10842 O  O     . ASN F 523 ? 1.2094 1.0574 0.7756 0.1315  0.3    0.0792  523 ASN Z O     
10843 C  CB    . ASN F 523 ? 1.2394 1.0936 0.7985 0.1474  0.3129 0.0908  523 ASN Z CB    
10844 C  CG    . ASN F 523 ? 1.2826 1.135  0.8347 0.1581  0.3217 0.0963  523 ASN Z CG    
10845 O  OD1   . ASN F 523 ? 1.2975 1.1502 0.8485 0.1599  0.3243 0.099   523 ASN Z OD1   
10846 N  ND2   . ASN F 523 ? 1.2913 1.1414 0.8382 0.1658  0.3268 0.0984  523 ASN Z ND2   
10847 N  N     . GLY F 524 ? 1.1953 1.0229 0.7592 0.1252  0.3002 0.073   524 GLY Z N     
10848 C  CA    . GLY F 524 ? 1.1803 1.0104 0.7502 0.1157  0.2923 0.0687  524 GLY Z CA    
10849 C  C     . GLY F 524 ? 1.169  0.9821 0.7374 0.1105  0.2906 0.0615  524 GLY Z C     
10850 O  O     . GLY F 524 ? 1.177  0.9745 0.7396 0.1132  0.2953 0.0591  524 GLY Z O     
10851 N  N     . LYS F 525 ? 1.1479 0.9641 0.7213 0.1027  0.2838 0.0582  525 LYS Z N     
10852 C  CA    . LYS F 525 ? 1.1388 0.9412 0.7121 0.0969  0.2812 0.0517  525 LYS Z CA    
10853 C  C     . LYS F 525 ? 1.1166 0.9228 0.6953 0.0879  0.2744 0.0493  525 LYS Z C     
10854 O  O     . LYS F 525 ? 1.1119 0.9325 0.6948 0.0851  0.2701 0.0519  525 LYS Z O     
10855 C  CB    . LYS F 525 ? 1.1608 0.9614 0.7331 0.0976  0.2805 0.0502  525 LYS Z CB    
10856 C  CG    . LYS F 525 ? 1.2143 0.999  0.7856 0.0933  0.2795 0.044   525 LYS Z CG    
10857 C  CD    . LYS F 525 ? 1.2695 1.0495 0.8382 0.0962  0.2811 0.0429  525 LYS Z CD    
10858 C  CE    . LYS F 525 ? 1.3192 1.0829 0.8867 0.0931  0.2814 0.0374  525 LYS Z CE    
10859 N  NZ    . LYS F 525 ? 1.3513 1.1025 0.9149 0.0954  0.2863 0.0363  525 LYS Z NZ    
10860 N  N     . ARG F 526 ? 1.1013 0.8949 0.6798 0.0832  0.2734 0.0446  526 ARG Z N     
10861 C  CA    . ARG F 526 ? 1.0869 0.8825 0.67   0.075   0.2674 0.0421  526 ARG Z CA    
10862 C  C     . ARG F 526 ? 1.066  0.8659 0.6521 0.0695  0.2617 0.0402  526 ARG Z C     
10863 O  O     . ARG F 526 ? 1.071  0.8622 0.6556 0.0691  0.2618 0.037   526 ARG Z O     
10864 C  CB    . ARG F 526 ? 1.1098 0.8902 0.6915 0.0718  0.2679 0.0375  526 ARG Z CB    
10865 C  CG    . ARG F 526 ? 1.1452 0.9273 0.7312 0.0638  0.2622 0.0352  526 ARG Z CG    
10866 C  CD    . ARG F 526 ? 1.1895 0.9579 0.774  0.0613  0.263  0.0315  526 ARG Z CD    
10867 N  NE    . ARG F 526 ? 1.2295 0.9847 0.8121 0.0607  0.264  0.0274  526 ARG Z NE    
10868 C  CZ    . ARG F 526 ? 1.2614 1.0042 0.843  0.058   0.2643 0.0239  526 ARG Z CZ    
10869 N  NH1   . ARG F 526 ? 1.2566 0.9976 0.8384 0.0556  0.2635 0.0235  526 ARG Z NH1   
10870 N  NH2   . ARG F 526 ? 1.267  0.9992 0.8474 0.0576  0.2652 0.0207  526 ARG Z NH2   
10871 N  N     . PRO F 527 ? 1.0402 0.8532 0.6303 0.0651  0.2569 0.0421  527 PRO Z N     
10872 C  CA    . PRO F 527 ? 1.0246 0.841  0.6164 0.0595  0.2514 0.0403  527 PRO Z CA    
10873 C  C     . PRO F 527 ? 1.0112 0.8156 0.6034 0.0529  0.2482 0.0347  527 PRO Z C     
10874 O  O     . PRO F 527 ? 1.0132 0.811  0.6061 0.0507  0.2484 0.0327  527 PRO Z O     
10875 C  CB    . PRO F 527 ? 1.0284 0.8615 0.6239 0.0562  0.2473 0.0442  527 PRO Z CB    
10876 C  CG    . PRO F 527 ? 1.0349 0.8751 0.6308 0.0619  0.2514 0.0489  527 PRO Z CG    
10877 C  CD    . PRO F 527 ? 1.0256 0.8508 0.6184 0.065   0.2562 0.0462  527 PRO Z CD    
10878 N  N     . ASP F 528 ? 0.9949 0.7966 0.5864 0.05    0.2453 0.0324  528 ASP Z N     
10879 C  CA    . ASP F 528 ? 0.988  0.7788 0.5796 0.044   0.2423 0.0274  528 ASP Z CA    
10880 C  C     . ASP F 528 ? 0.9709 0.7676 0.5651 0.0365  0.2367 0.027   528 ASP Z C     
10881 O  O     . ASP F 528 ? 0.9745 0.7628 0.5692 0.0318  0.2347 0.0233  528 ASP Z O     
10882 C  CB    . ASP F 528 ? 1.0103 0.7953 0.5995 0.0441  0.2418 0.0254  528 ASP Z CB    
10883 C  CG    . ASP F 528 ? 1.0624 0.8401 0.6489 0.051   0.2474 0.0254  528 ASP Z CG    
10884 O  OD1   . ASP F 528 ? 1.0687 0.8408 0.6548 0.0544  0.2514 0.0253  528 ASP Z OD1   
10885 O  OD2   . ASP F 528 ? 1.0907 0.8677 0.675  0.0529  0.2477 0.0254  528 ASP Z OD2   
10886 N  N     . HIS F 529 ? 0.9501 0.7613 0.5458 0.0353  0.2342 0.0307  529 HIS Z N     
10887 C  CA    . HIS F 529 ? 0.9391 0.7568 0.537  0.0282  0.229  0.0308  529 HIS Z CA    
10888 C  C     . HIS F 529 ? 0.9249 0.759  0.5254 0.0297  0.2288 0.0362  529 HIS Z C     
10889 O  O     . HIS F 529 ? 0.9239 0.7667 0.524  0.0341  0.2303 0.0398  529 HIS Z O     
10890 C  CB    . HIS F 529 ? 0.9451 0.7635 0.5411 0.0227  0.2242 0.0293  529 HIS Z CB    
10891 C  CG    . HIS F 529 ? 0.971  0.7749 0.564  0.0219  0.2245 0.0248  529 HIS Z CG    
10892 N  ND1   . HIS F 529 ? 0.9956 0.7885 0.5886 0.0176  0.2232 0.0208  529 HIS Z ND1   
10893 C  CD2   . HIS F 529 ? 0.9853 0.7847 0.5751 0.0248  0.2258 0.0242  529 HIS Z CD2   
10894 C  CE1   . HIS F 529 ? 1.0048 0.7872 0.595  0.0183  0.224  0.018   529 HIS Z CE1   
10895 N  NE2   . HIS F 529 ? 1.0029 0.7885 0.5911 0.0225  0.2256 0.0198  529 HIS Z NE2   
10896 N  N     . VAL F 530 ? 0.9113 0.7502 0.5146 0.0261  0.227  0.037   530 VAL Z N     
10897 C  CA    . VAL F 530 ? 0.9015 0.7572 0.5079 0.0266  0.2263 0.0425  530 VAL Z CA    
10898 C  C     . VAL F 530 ? 0.8985 0.7594 0.5066 0.0178  0.2203 0.0418  530 VAL Z C     
10899 O  O     . VAL F 530 ? 0.9028 0.7569 0.5116 0.0139  0.2192 0.039   530 VAL Z O     
10900 C  CB    . VAL F 530 ? 0.9067 0.7651 0.5146 0.0323  0.231  0.0455  530 VAL Z CB    
10901 C  CG1   . VAL F 530 ? 0.907  0.784  0.5185 0.0326  0.23   0.0516  530 VAL Z CG1   
10902 C  CG2   . VAL F 530 ? 0.9131 0.7649 0.5181 0.0409  0.2372 0.0461  530 VAL Z CG2   
10903 N  N     . ILE F 531 ? 0.8911 0.7628 0.4993 0.0142  0.2163 0.044   531 ILE Z N     
10904 C  CA    . ILE F 531 ? 0.8923 0.7682 0.501  0.0052  0.2104 0.0433  531 ILE Z CA    
10905 C  C     . ILE F 531 ? 0.888  0.7818 0.501  0.0041  0.2089 0.0489  531 ILE Z C     
10906 O  O     . ILE F 531 ? 0.8864 0.7928 0.5009 0.0083  0.21   0.0537  531 ILE Z O     
10907 C  CB    . ILE F 531 ? 0.8984 0.7724 0.503  0.0007  0.2063 0.0415  531 ILE Z CB    
10908 C  CG1   . ILE F 531 ? 0.9159 0.7729 0.5164 0.0032  0.2085 0.0367  531 ILE Z CG1   
10909 C  CG2   . ILE F 531 ? 0.9032 0.7789 0.5068 -0.0091 0.2003 0.0402  531 ILE Z CG2   
10910 C  CD1   . ILE F 531 ? 0.9356 0.7778 0.5356 0.0009  0.2091 0.0318  531 ILE Z CD1   
10911 N  N     . GLN F 532 ? 0.8848 0.7803 0.4999 -0.0015 0.2064 0.0484  532 GLN Z N     
10912 C  CA    . GLN F 532 ? 0.8832 0.7961 0.5027 -0.0031 0.2049 0.0539  532 GLN Z CA    
10913 C  C     . GLN F 532 ? 0.8806 0.8003 0.4997 -0.0127 0.1984 0.054   532 GLN Z C     
10914 O  O     . GLN F 532 ? 0.8849 0.7945 0.5015 -0.0192 0.1955 0.0496  532 GLN Z O     
10915 C  CB    . GLN F 532 ? 0.9066 0.8184 0.5291 -0.0013 0.2077 0.0545  532 GLN Z CB    
10916 C  CG    . GLN F 532 ? 0.9488 0.8792 0.5763 -0.0019 0.207  0.0608  532 GLN Z CG    
10917 C  CD    . GLN F 532 ? 1.009  0.9388 0.6389 0.0023  0.2111 0.0624  532 GLN Z CD    
10918 O  OE1   . GLN F 532 ? 1.037  0.9519 0.6648 0.0039  0.2137 0.0582  532 GLN Z OE1   
10919 N  NE2   . GLN F 532 ? 1.009  0.9552 0.6433 0.0042  0.212  0.0687  532 GLN Z NE2   
10920 N  N     . ILE F 533 ? 0.8722 0.809  0.4933 -0.0138 0.196  0.0593  533 ILE Z N     
10921 C  CA    . ILE F 533 ? 0.8744 0.8192 0.4949 -0.0234 0.1895 0.0601  533 ILE Z CA    
10922 C  C     . ILE F 533 ? 0.8705 0.8346 0.4971 -0.0246 0.1886 0.0664  533 ILE Z C     
10923 O  O     . ILE F 533 ? 0.8651 0.8432 0.4955 -0.0188 0.1908 0.0722  533 ILE Z O     
10924 C  CB    . ILE F 533 ? 0.8795 0.8266 0.496  -0.0251 0.1865 0.0603  533 ILE Z CB    
10925 C  CG1   . ILE F 533 ? 0.8983 0.8256 0.5088 -0.0231 0.1882 0.0541  533 ILE Z CG1   
10926 C  CG2   . ILE F 533 ? 0.8839 0.8383 0.4986 -0.0358 0.1796 0.061   533 ILE Z CG2   
10927 C  CD1   . ILE F 533 ? 0.9145 0.8417 0.5208 -0.0227 0.1866 0.0541  533 ILE Z CD1   
10928 N  N     . LEU F 534 ? 0.8713 0.8361 0.4991 -0.0319 0.1856 0.0656  534 LEU Z N     
10929 C  CA    . LEU F 534 ? 0.8722 0.8545 0.5063 -0.033  0.1851 0.0715  534 LEU Z CA    
10930 C  C     . LEU F 534 ? 0.8722 0.8687 0.5072 -0.0424 0.1787 0.0747  534 LEU Z C     
10931 O  O     . LEU F 534 ? 0.8656 0.8792 0.5065 -0.043  0.1782 0.0806  534 LEU Z O     
10932 C  CB    . LEU F 534 ? 0.8784 0.8533 0.5142 -0.0332 0.1872 0.0695  534 LEU Z CB    
10933 C  CG    . LEU F 534 ? 0.9021 0.8651 0.5376 -0.024  0.1937 0.0675  534 LEU Z CG    
10934 C  CD1   . LEU F 534 ? 0.9181 0.8601 0.5489 -0.0266 0.1936 0.0599  534 LEU Z CD1   
10935 C  CD2   . LEU F 534 ? 0.9065 0.8782 0.5471 -0.0194 0.1975 0.072   534 LEU Z CD2   
10936 N  N     . ASP F 535 ? 0.8773 0.8669 0.5063 -0.0499 0.1738 0.071   535 ASP Z N     
10937 C  CA    . ASP F 535 ? 0.8816 0.8836 0.5103 -0.0597 0.1674 0.0737  535 ASP Z CA    
10938 C  C     . ASP F 535 ? 0.8781 0.8901 0.505  -0.0603 0.1645 0.0768  535 ASP Z C     
10939 O  O     . ASP F 535 ? 0.881  0.8967 0.5043 -0.0695 0.1585 0.0768  535 ASP Z O     
10940 C  CB    . ASP F 535 ? 0.9179 0.9058 0.5404 -0.0697 0.1632 0.0679  535 ASP Z CB    
10941 C  CG    . ASP F 535 ? 0.997  0.966  0.6108 -0.0707 0.1625 0.0616  535 ASP Z CG    
10942 O  OD1   . ASP F 535 ? 1.0126 0.9744 0.6257 -0.0624 0.1666 0.0601  535 ASP Z OD1   
10943 O  OD2   . ASP F 535 ? 1.0314 0.9924 0.6387 -0.0797 0.158  0.0583  535 ASP Z OD2   
10944 N  N     . LEU F 536 ? 0.869  0.8855 0.4981 -0.0506 0.1686 0.0795  536 LEU Z N     
10945 C  CA    . LEU F 536 ? 0.8657 0.8919 0.4932 -0.05   0.1664 0.0826  536 LEU Z CA    
10946 C  C     . LEU F 536 ? 0.8525 0.9031 0.4881 -0.0457 0.1673 0.0914  536 LEU Z C     
10947 O  O     . LEU F 536 ? 0.8484 0.915  0.4853 -0.0517 0.1623 0.0959  536 LEU Z O     
10948 C  CB    . LEU F 536 ? 0.8746 0.8859 0.4972 -0.0428 0.17   0.0786  536 LEU Z CB    
10949 C  CG    . LEU F 536 ? 0.891  0.9097 0.5113 -0.0407 0.1686 0.0812  536 LEU Z CG    
10950 C  CD1   . LEU F 536 ? 0.8997 0.9212 0.5148 -0.0517 0.1611 0.0807  536 LEU Z CD1   
10951 C  CD2   . LEU F 536 ? 0.9067 0.9085 0.5221 -0.0336 0.1727 0.0766  536 LEU Z CD2   
10952 N  N     . PHE F 537 ? 0.8441 0.8978 0.4848 -0.0355 0.1738 0.0942  537 PHE Z N     
10953 C  CA    . PHE F 537 ? 0.8361 0.9124 0.4845 -0.0301 0.1758 0.103   537 PHE Z CA    
10954 C  C     . PHE F 537 ? 0.8292 0.9113 0.4837 -0.0294 0.1783 0.1057  537 PHE Z C     
10955 O  O     . PHE F 537 ? 0.8364 0.9032 0.4888 -0.0314 0.1793 0.1003  537 PHE Z O     
10956 C  CB    . PHE F 537 ? 0.8377 0.9134 0.4861 -0.0176 0.1821 0.105   537 PHE Z CB    
10957 C  CG    . PHE F 537 ? 0.8539 0.9217 0.4961 -0.0167 0.1809 0.1019  537 PHE Z CG    
10958 C  CD1   . PHE F 537 ? 0.8609 0.9421 0.5025 -0.0212 0.1757 0.1054  537 PHE Z CD1   
10959 C  CD2   . PHE F 537 ? 0.8734 0.9208 0.5104 -0.0112 0.185  0.0959  537 PHE Z CD2   
10960 C  CE1   . PHE F 537 ? 0.8752 0.9486 0.5105 -0.0201 0.1747 0.1027  537 PHE Z CE1   
10961 C  CE2   . PHE F 537 ? 0.8871 0.9272 0.5184 -0.0101 0.1841 0.0933  537 PHE Z CE2   
10962 C  CZ    . PHE F 537 ? 0.8813 0.9341 0.5115 -0.0144 0.1791 0.0966  537 PHE Z CZ    
10963 N  N     . GLU F 538 ? 0.8127 0.9168 0.4746 -0.0261 0.1795 0.1142  538 GLU Z N     
10964 C  CA    . GLU F 538 ? 0.8085 0.9184 0.4762 -0.0244 0.1824 0.1173  538 GLU Z CA    
10965 C  C     . GLU F 538 ? 0.8085 0.9027 0.4746 -0.0145 0.19   0.1143  538 GLU Z C     
10966 O  O     . GLU F 538 ? 0.8156 0.901  0.482  -0.0156 0.1916 0.1116  538 GLU Z O     
10967 C  CB    . GLU F 538 ? 0.8264 0.9633 0.5025 -0.022  0.1827 0.1276  538 GLU Z CB    
10968 C  CG    . GLU F 538 ? 0.8815 1.0281 0.5629 -0.0283 0.1807 0.1305  538 GLU Z CG    
10969 C  CD    . GLU F 538 ? 0.9534 1.0994 0.6388 -0.0205 0.1874 0.1329  538 GLU Z CD    
10970 O  OE1   . GLU F 538 ? 0.9654 1.116  0.6543 -0.0258 0.186  0.1342  538 GLU Z OE1   
10971 O  OE2   . GLU F 538 ? 0.9783 1.1189 0.6627 -0.0092 0.1942 0.1337  538 GLU Z OE2   
10972 N  N     . LYS F 539 ? 0.7985 0.8883 0.4622 -0.0051 0.1946 0.1145  539 LYS Z N     
10973 C  CA    . LYS F 539 ? 0.7985 0.8715 0.4593 0.0039  0.2016 0.1111  539 LYS Z CA    
10974 C  C     . LYS F 539 ? 0.8012 0.8511 0.4547 0.0004  0.2001 0.1018  539 LYS Z C     
10975 O  O     . LYS F 539 ? 0.8048 0.8531 0.455  -0.0041 0.1958 0.0995  539 LYS Z O     
10976 C  CB    . LYS F 539 ? 0.814  0.8928 0.475  0.0156  0.2074 0.1158  539 LYS Z CB    
10977 C  CG    . LYS F 539 ? 0.8456 0.9461 0.5134 0.0213  0.2104 0.1255  539 LYS Z CG    
10978 C  CD    . LYS F 539 ? 0.89   0.9932 0.5566 0.0334  0.2168 0.1295  539 LYS Z CD    
10979 C  CE    . LYS F 539 ? 0.9191 1.0424 0.5919 0.0405  0.2209 0.1393  539 LYS Z CE    
10980 N  NZ    . LYS F 539 ? 0.9432 1.0687 0.6141 0.0526  0.2273 0.1434  539 LYS Z NZ    
10981 N  N     . PRO F 540 ? 0.7976 0.8296 0.4485 0.0025  0.2035 0.0965  540 PRO Z N     
10982 C  CA    . PRO F 540 ? 0.8012 0.8118 0.4457 -0.0004 0.2024 0.0881  540 PRO Z CA    
10983 C  C     . PRO F 540 ? 0.7988 0.8033 0.4395 0.0064  0.2052 0.087   540 PRO Z C     
10984 O  O     . PRO F 540 ? 0.7995 0.8094 0.4414 0.0156  0.2105 0.0913  540 PRO Z O     
10985 C  CB    . PRO F 540 ? 0.8161 0.812  0.4597 0.0018  0.2062 0.0843  540 PRO Z CB    
10986 C  CG    . PRO F 540 ? 0.818  0.8275 0.4671 0.0035  0.208  0.0902  540 PRO Z CG    
10987 C  CD    . PRO F 540 ? 0.7905 0.8206 0.4437 0.0077  0.2087 0.0982  540 PRO Z CD    
10988 N  N     . LEU F 541 ? 0.7938 0.7867 0.4295 0.002   0.202  0.0815  541 LEU Z N     
10989 C  CA    . LEU F 541 ? 0.7937 0.7795 0.4254 0.0079  0.2045 0.08    541 LEU Z CA    
10990 C  C     . LEU F 541 ? 0.7977 0.762  0.4254 0.0119  0.2089 0.0739  541 LEU Z C     
10991 O  O     . LEU F 541 ? 0.8032 0.7547 0.4289 0.0062  0.2068 0.0684  541 LEU Z O     
10992 C  CB    . LEU F 541 ? 0.7952 0.7808 0.4231 0.0011  0.1987 0.0779  541 LEU Z CB    
10993 C  CG    . LEU F 541 ? 0.8151 0.7884 0.4376 0.0053  0.2006 0.0744  541 LEU Z CG    
10994 C  CD1   . LEU F 541 ? 0.8147 0.7985 0.4386 0.0144  0.2045 0.0798  541 LEU Z CD1   
10995 C  CD2   . LEU F 541 ? 0.8284 0.7967 0.446  -0.0027 0.1947 0.0709  541 LEU Z CD2   
10996 N  N     . LEU F 542 ? 0.7925 0.7528 0.4189 0.0213  0.2148 0.0749  542 LEU Z N     
10997 C  CA    . LEU F 542 ? 0.7992 0.7396 0.4215 0.0251  0.2188 0.0694  542 LEU Z CA    
10998 C  C     . LEU F 542 ? 0.8    0.7355 0.4185 0.0283  0.2195 0.068   542 LEU Z C     
10999 O  O     . LEU F 542 ? 0.798  0.742  0.4167 0.0351  0.2225 0.0724  542 LEU Z O     
11000 C  CB    . LEU F 542 ? 0.8022 0.7403 0.4253 0.0336  0.2256 0.0716  542 LEU Z CB    
11001 C  CG    . LEU F 542 ? 0.8219 0.7627 0.4482 0.0313  0.2256 0.0727  542 LEU Z CG    
11002 C  CD1   . LEU F 542 ? 0.8302 0.7695 0.4561 0.0403  0.2326 0.0757  542 LEU Z CD1   
11003 C  CD2   . LEU F 542 ? 0.8369 0.7629 0.4616 0.0242  0.2227 0.066   542 LEU Z CD2   
11004 N  N     . LEU F 543 ? 0.8006 0.723  0.4153 0.0233  0.2166 0.0621  543 LEU Z N     
11005 C  CA    . LEU F 543 ? 0.8046 0.7208 0.4152 0.0256  0.217  0.0603  543 LEU Z CA    
11006 C  C     . LEU F 543 ? 0.8098 0.7077 0.4173 0.0305  0.222  0.0557  543 LEU Z C     
11007 O  O     . LEU F 543 ? 0.8166 0.7013 0.4228 0.0264  0.2209 0.0506  543 LEU Z O     
11008 C  CB    . LEU F 543 ? 0.8088 0.7223 0.4166 0.0167  0.2106 0.057   543 LEU Z CB    
11009 C  CG    . LEU F 543 ? 0.8308 0.737  0.4337 0.0182  0.2105 0.0548  543 LEU Z CG    
11010 C  CD1   . LEU F 543 ? 0.8319 0.7521 0.4353 0.0234  0.2114 0.0603  543 LEU Z CD1   
11011 C  CD2   . LEU F 543 ? 0.8427 0.743  0.4417 0.009   0.2045 0.051   543 LEU Z CD2   
11012 N  N     . SER F 544 ? 0.8054 0.7026 0.4117 0.0393  0.2274 0.0578  544 SER Z N     
11013 C  CA    . SER F 544 ? 0.8146 0.6948 0.4178 0.0442  0.2324 0.0539  544 SER Z CA    
11014 C  C     . SER F 544 ? 0.818  0.6901 0.4172 0.0444  0.2318 0.0509  544 SER Z C     
11015 O  O     . SER F 544 ? 0.8184 0.6986 0.4166 0.0477  0.2321 0.054   544 SER Z O     
11016 C  CB    . SER F 544 ? 0.8315 0.7138 0.4344 0.0535  0.2391 0.0576  544 SER Z CB    
11017 O  OG    . SER F 544 ? 0.857  0.7443 0.4628 0.0536  0.2402 0.06    544 SER Z OG    
11018 N  N     . ILE F 545 ? 0.8179 0.6744 0.4149 0.0411  0.2311 0.0452  545 ILE Z N     
11019 C  CA    . ILE F 545 ? 0.8211 0.6685 0.4142 0.0407  0.2305 0.0421  545 ILE Z CA    
11020 C  C     . ILE F 545 ? 0.8225 0.6547 0.4132 0.0461  0.2358 0.039   545 ILE Z C     
11021 O  O     . ILE F 545 ? 0.827  0.6498 0.4185 0.0456  0.2376 0.0363  545 ILE Z O     
11022 C  CB    . ILE F 545 ? 0.83   0.6723 0.422  0.0317  0.2247 0.0382  545 ILE Z CB    
11023 C  CG1   . ILE F 545 ? 0.8378 0.6941 0.4319 0.0253  0.2192 0.0409  545 ILE Z CG1   
11024 C  CG2   . ILE F 545 ? 0.8408 0.6746 0.4282 0.0313  0.2238 0.0355  545 ILE Z CG2   
11025 C  CD1   . ILE F 545 ? 0.8576 0.7074 0.4501 0.0163  0.214  0.037   545 ILE Z CD1   
11026 N  N     . GLU F 546 ? 0.8165 0.6461 0.4042 0.0509  0.2382 0.0393  546 GLU Z N     
11027 C  CA    . GLU F 546 ? 0.8218 0.6368 0.4069 0.0554  0.243  0.0363  546 GLU Z CA    
11028 C  C     . GLU F 546 ? 0.8223 0.6293 0.4045 0.0523  0.2405 0.033   546 GLU Z C     
11029 O  O     . GLU F 546 ? 0.8222 0.6361 0.4025 0.052   0.2382 0.0347  546 GLU Z O     
11030 C  CB    . GLU F 546 ? 0.8496 0.6674 0.4329 0.0644  0.2488 0.0398  546 GLU Z CB    
11031 C  CG    . GLU F 546 ? 0.9129 0.7153 0.4933 0.069   0.2542 0.0369  546 GLU Z CG    
11032 C  CD    . GLU F 546 ? 0.9825 0.7789 0.5632 0.0717  0.2584 0.0367  546 GLU Z CD    
11033 O  OE1   . GLU F 546 ? 0.9844 0.7838 0.5679 0.0679  0.2563 0.0367  546 GLU Z OE1   
11034 O  OE2   . GLU F 546 ? 1.0134 0.8015 0.591  0.0776  0.264  0.0365  546 GLU Z OE2   
11035 N  N     . SER F 547 ? 0.8216 0.6146 0.4032 0.0497  0.2408 0.0284  547 SER Z N     
11036 C  CA    . SER F 547 ? 0.8261 0.6104 0.4048 0.0468  0.2387 0.0252  547 SER Z CA    
11037 C  C     . SER F 547 ? 0.826  0.5988 0.4024 0.0523  0.2436 0.0235  547 SER Z C     
11038 O  O     . SER F 547 ? 0.8294 0.5956 0.4068 0.0554  0.2478 0.0226  547 SER Z O     
11039 C  CB    . SER F 547 ? 0.8468 0.6239 0.4266 0.0397  0.2353 0.0215  547 SER Z CB    
11040 O  OG    . SER F 547 ? 0.8786 0.6479 0.4608 0.0406  0.2381 0.0196  547 SER Z OG    
11041 N  N     . LYS F 548 ? 0.8208 0.5912 0.3937 0.0532  0.2432 0.0231  548 LYS Z N     
11042 C  CA    . LYS F 548 ? 0.8244 0.584  0.3947 0.0582  0.2477 0.0216  548 LYS Z CA    
11043 C  C     . LYS F 548 ? 0.825  0.5768 0.392  0.0549  0.2452 0.0189  548 LYS Z C     
11044 O  O     . LYS F 548 ? 0.8246 0.5805 0.3904 0.0494  0.2401 0.0187  548 LYS Z O     
11045 C  CB    . LYS F 548 ? 0.8457 0.6119 0.414  0.0655  0.2512 0.0251  548 LYS Z CB    
11046 C  CG    . LYS F 548 ? 0.8962 0.668  0.4665 0.0702  0.2551 0.028   548 LYS Z CG    
11047 C  CD    . LYS F 548 ? 0.9561 0.7154 0.5268 0.0724  0.2597 0.0255  548 LYS Z CD    
11048 C  CE    . LYS F 548 ? 1.0034 0.7667 0.576  0.0744  0.262  0.0275  548 LYS Z CE    
11049 N  NZ    . LYS F 548 ? 1.0346 0.8026 0.6047 0.0823  0.267  0.0313  548 LYS Z NZ    
11050 N  N     . GLU F 549 ? 0.8233 0.5634 0.3886 0.0582  0.2488 0.0168  549 GLU Z N     
11051 C  CA    . GLU F 549 ? 0.8252 0.557  0.3869 0.056   0.2473 0.0146  549 GLU Z CA    
11052 C  C     . GLU F 549 ? 0.8278 0.5657 0.3849 0.0579  0.246  0.0168  549 GLU Z C     
11053 O  O     . GLU F 549 ? 0.8277 0.5657 0.3814 0.0535  0.2418 0.0162  549 GLU Z O     
11054 C  CB    . GLU F 549 ? 0.8398 0.5579 0.4014 0.0591  0.2518 0.0122  549 GLU Z CB    
11055 C  CG    . GLU F 549 ? 0.8571 0.5661 0.4148 0.0577  0.2509 0.0102  549 GLU Z CG    
11056 C  CD    . GLU F 549 ? 0.8849 0.5808 0.4438 0.0592  0.2546 0.0078  549 GLU Z CD    
11057 O  OE1   . GLU F 549 ? 0.8872 0.5805 0.4504 0.0593  0.2566 0.007   549 GLU Z OE1   
11058 O  OE2   . GLU F 549 ? 0.9027 0.5909 0.4581 0.0602  0.2554 0.0068  549 GLU Z OE2   
11059 N  N     . LYS F 550 ? 0.83   0.5729 0.3865 0.0644  0.2496 0.0194  550 LYS Z N     
11060 C  CA    . LYS F 550 ? 0.8399 0.589  0.3922 0.0672  0.2489 0.0218  550 LYS Z CA    
11061 C  C     . LYS F 550 ? 0.8459 0.6108 0.3998 0.0698  0.2485 0.0263  550 LYS Z C     
11062 O  O     . LYS F 550 ? 0.8439 0.6122 0.4014 0.0724  0.2513 0.0276  550 LYS Z O     
11063 C  CB    . LYS F 550 ? 0.862  0.6014 0.4112 0.0736  0.2541 0.0211  550 LYS Z CB    
11064 C  CG    . LYS F 550 ? 0.9114 0.636  0.4589 0.0714  0.2546 0.0173  550 LYS Z CG    
11065 C  CD    . LYS F 550 ? 0.9626 0.679  0.5061 0.0771  0.2587 0.017   550 LYS Z CD    
11066 C  CE    . LYS F 550 ? 1.0065 0.7095 0.5479 0.0746  0.2586 0.0138  550 LYS Z CE    
11067 N  NZ    . LYS F 550 ? 1.0328 0.727  0.5788 0.0741  0.2615 0.0115  550 LYS Z NZ    
11068 N  N     . PRO F 551 ? 0.8518 0.6265 0.4028 0.0694  0.2454 0.0289  551 PRO Z N     
11069 C  CA    . PRO F 551 ? 0.8543 0.6452 0.4072 0.0722  0.2451 0.0338  551 PRO Z CA    
11070 C  C     . PRO F 551 ? 0.8672 0.6588 0.4203 0.0814  0.2517 0.0362  551 PRO Z C     
11071 O  O     . PRO F 551 ? 0.864  0.6662 0.4201 0.0843  0.2532 0.0397  551 PRO Z O     
11072 C  CB    . PRO F 551 ? 0.859  0.6584 0.408  0.0696  0.2402 0.0358  551 PRO Z CB    
11073 C  CG    . PRO F 551 ? 0.8684 0.6538 0.412  0.0685  0.2401 0.0322  551 PRO Z CG    
11074 C  CD    . PRO F 551 ? 0.8504 0.6218 0.3958 0.0662  0.2417 0.0278  551 PRO Z CD    
11075 N  N     . ASN F 552 ? 0.8793 0.6591 0.4291 0.0861  0.2561 0.0343  552 ASN Z N     
11076 C  CA    . ASN F 552 ? 0.8918 0.6698 0.4407 0.0948  0.2629 0.0361  552 ASN Z CA    
11077 C  C     . ASN F 552 ? 0.9043 0.6766 0.4564 0.0962  0.2669 0.0351  552 ASN Z C     
11078 O  O     . ASN F 552 ? 0.9068 0.6798 0.4582 0.1029  0.2723 0.0373  552 ASN Z O     
11079 C  CB    . ASN F 552 ? 0.9087 0.675  0.4529 0.0987  0.2662 0.0342  552 ASN Z CB    
11080 C  CG    . ASN F 552 ? 0.9456 0.7179 0.4856 0.0992  0.2632 0.036   552 ASN Z CG    
11081 O  OD1   . ASN F 552 ? 0.9536 0.7407 0.4939 0.0995  0.2606 0.04    552 ASN Z OD1   
11082 N  ND2   . ASN F 552 ? 0.9593 0.7206 0.4951 0.0991  0.2636 0.0333  552 ASN Z ND2   
11083 N  N     . ASP F 553 ? 0.9108 0.6774 0.466  0.0899  0.2645 0.0318  553 ASP Z N     
11084 C  CA    . ASP F 553 ? 0.9218 0.683  0.4798 0.0902  0.2674 0.0307  553 ASP Z CA    
11085 C  C     . ASP F 553 ? 0.9223 0.6962 0.4832 0.0906  0.2669 0.0343  553 ASP Z C     
11086 O  O     . ASP F 553 ? 0.926  0.6962 0.488  0.0925  0.2704 0.0342  553 ASP Z O     
11087 C  CB    . ASP F 553 ? 0.9495 0.701  0.5098 0.0833  0.2647 0.0263  553 ASP Z CB    
11088 C  CG    . ASP F 553 ? 1.0214 0.76   0.5794 0.083   0.2657 0.023   553 ASP Z CG    
11089 O  OD1   . ASP F 553 ? 1.0355 0.7692 0.5904 0.0889  0.2702 0.0234  553 ASP Z OD1   
11090 O  OD2   . ASP F 553 ? 1.0542 0.7874 0.6131 0.0772  0.2622 0.0201  553 ASP Z OD2   
11091 N  N     . LEU F 554 ? 0.9164 0.7049 0.4783 0.0887  0.2626 0.0375  554 LEU Z N     
11092 C  CA    . LEU F 554 ? 0.9155 0.7174 0.4804 0.0894  0.2621 0.0415  554 LEU Z CA    
11093 C  C     . LEU F 554 ? 0.9193 0.724  0.4821 0.0987  0.2685 0.0452  554 LEU Z C     
11094 O  O     . LEU F 554 ? 0.9181 0.7272 0.4781 0.1033  0.2698 0.0476  554 LEU Z O     
11095 C  CB    . LEU F 554 ? 0.9116 0.7287 0.478  0.0849  0.2558 0.0442  554 LEU Z CB    
11096 C  CG    . LEU F 554 ? 0.9271 0.7426 0.495  0.0753  0.2494 0.041   554 LEU Z CG    
11097 C  CD1   . LEU F 554 ? 0.9289 0.7586 0.497  0.0711  0.2435 0.0439  554 LEU Z CD1   
11098 C  CD2   . LEU F 554 ? 0.9329 0.747  0.5048 0.0719  0.249  0.0399  554 LEU Z CD2   
11099 N  N     . GLU F 555 ? 0.9219 0.7227 0.4853 0.1015  0.2727 0.0456  555 GLU Z N     
11100 C  CA    . GLU F 555 ? 0.9297 0.7304 0.4901 0.1103  0.2796 0.0488  555 GLU Z CA    
11101 C  C     . GLU F 555 ? 0.9276 0.746  0.4888 0.1147  0.2797 0.0552  555 GLU Z C     
11102 O  O     . GLU F 555 ? 0.9225 0.7538 0.4877 0.1103  0.2747 0.0573  555 GLU Z O     
11103 C  CB    . GLU F 555 ? 0.9601 0.752  0.5205 0.111   0.2834 0.0476  555 GLU Z CB    
11104 C  CG    . GLU F 555 ? 1.0227 0.7973 0.5823 0.1075  0.284  0.0418  555 GLU Z CG    
11105 C  CD    . GLU F 555 ? 1.0958 0.868  0.6596 0.0991  0.2792 0.0386  555 GLU Z CD    
11106 O  OE1   . GLU F 555 ? 1.1185 0.8772 0.682  0.0966  0.2801 0.0344  555 GLU Z OE1   
11107 O  OE2   . GLU F 555 ? 1.1097 0.8937 0.6771 0.0951  0.2745 0.0402  555 GLU Z OE2   
11108 N  N     . PRO F 556 ? 0.9289 0.7483 0.4861 0.1235  0.2854 0.0585  556 PRO Z N     
11109 C  CA    . PRO F 556 ? 0.9245 0.7616 0.4826 0.1284  0.2859 0.0652  556 PRO Z CA    
11110 C  C     . PRO F 556 ? 0.9248 0.7699 0.4863 0.1281  0.2863 0.0682  556 PRO Z C     
11111 O  O     . PRO F 556 ? 0.9293 0.7638 0.4894 0.1292  0.2901 0.0664  556 PRO Z O     
11112 C  CB    . PRO F 556 ? 0.9356 0.7679 0.488  0.1384  0.2934 0.0674  556 PRO Z CB    
11113 C  CG    . PRO F 556 ? 0.9473 0.762  0.4962 0.1374  0.2948 0.0618  556 PRO Z CG    
11114 C  CD    . PRO F 556 ? 0.9297 0.7347 0.4815 0.1295  0.2919 0.0567  556 PRO Z CD    
11115 N  N     . LYS F 557 ? 0.9181 0.7815 0.484  0.1257  0.2817 0.0725  557 LYS Z N     
11116 C  CA    . LYS F 557 ? 0.92   0.7941 0.49   0.1249  0.2812 0.0761  557 LYS Z CA    
11117 C  C     . LYS F 557 ? 0.9253 0.7919 0.4981 0.1168  0.2778 0.0715  557 LYS Z C     
11118 O  O     . LYS F 557 ? 0.9235 0.7941 0.4984 0.1171  0.2789 0.0736  557 LYS Z O     
11119 C  CB    . LYS F 557 ? 0.944  0.8181 0.5108 0.1348  0.2893 0.0806  557 LYS Z CB    
11120 C  CG    . LYS F 557 ? 0.9964 0.8803 0.5606 0.1434  0.2928 0.0861  557 LYS Z CG    
11121 C  CD    . LYS F 557 ? 1.0603 0.9412 0.6199 0.1536  0.3016 0.0901  557 LYS Z CD    
11122 C  CE    . LYS F 557 ? 1.1078 1.0004 0.6709 0.1546  0.3022 0.0951  557 LYS Z CE    
11123 N  NZ    . LYS F 557 ? 1.1417 1.0313 0.6992 0.1653  0.3112 0.0995  557 LYS Z NZ    
11124 N  N     . ILE F 558 ? 0.929  0.7855 0.502  0.1097  0.2736 0.0656  558 ILE Z N     
11125 C  CA    . ILE F 558 ? 0.9357 0.7852 0.5114 0.102   0.2702 0.0613  558 ILE Z CA    
11126 C  C     . ILE F 558 ? 0.9335 0.7984 0.5145 0.0966  0.2649 0.0642  558 ILE Z C     
11127 O  O     . ILE F 558 ? 0.9356 0.7991 0.5187 0.0944  0.265  0.0637  558 ILE Z O     
11128 C  CB    . ILE F 558 ? 0.9462 0.782  0.5208 0.096   0.2671 0.0548  558 ILE Z CB    
11129 C  CG1   . ILE F 558 ? 0.96   0.7865 0.5368 0.0896  0.2651 0.0505  558 ILE Z CG1   
11130 C  CG2   . ILE F 558 ? 0.9492 0.7925 0.5246 0.0912  0.261  0.0547  558 ILE Z CG2   
11131 C  CD1   . ILE F 558 ? 0.9801 0.797  0.5553 0.0933  0.2706 0.0498  558 ILE Z CD1   
11132 N  N     . GLY F 559 ? 0.9287 0.8087 0.5116 0.095   0.2607 0.0676  559 GLY Z N     
11133 C  CA    . GLY F 559 ? 0.9297 0.8258 0.5177 0.0897  0.2555 0.0708  559 GLY Z CA    
11134 C  C     . GLY F 559 ? 0.9314 0.8368 0.5218 0.0945  0.2592 0.076   559 GLY Z C     
11135 O  O     . GLY F 559 ? 0.9307 0.839  0.5247 0.09    0.2571 0.076   559 GLY Z O     
11136 N  N     . VAL F 560 ? 0.9331 0.8419 0.5212 0.1041  0.2653 0.0804  560 VAL Z N     
11137 C  CA    . VAL F 560 ? 0.9386 0.8552 0.5278 0.1102  0.27   0.0859  560 VAL Z CA    
11138 C  C     . VAL F 560 ? 0.9484 0.8494 0.5355 0.1106  0.2739 0.0824  560 VAL Z C     
11139 O  O     . VAL F 560 ? 0.9467 0.8531 0.5366 0.1097  0.2741 0.0846  560 VAL Z O     
11140 C  CB    . VAL F 560 ? 0.9488 0.8715 0.5349 0.1209  0.276  0.0915  560 VAL Z CB    
11141 C  CG1   . VAL F 560 ? 0.954  0.8838 0.5404 0.128   0.2816 0.0974  560 VAL Z CG1   
11142 C  CG2   . VAL F 560 ? 0.9492 0.8885 0.5376 0.1201  0.2717 0.0953  560 VAL Z CG2   
11143 N  N     . GLN F 561 ? 0.9567 0.8386 0.5391 0.1112  0.2766 0.0768  561 GLN Z N     
11144 C  CA    . GLN F 561 ? 0.9698 0.8358 0.5496 0.111   0.2799 0.073   561 GLN Z CA    
11145 C  C     . GLN F 561 ? 0.9761 0.8409 0.5602 0.1019  0.2744 0.0696  561 GLN Z C     
11146 O  O     . GLN F 561 ? 0.982  0.8413 0.5656 0.102   0.2766 0.0692  561 GLN Z O     
11147 C  CB    . GLN F 561 ? 0.9941 0.841  0.5686 0.1126  0.2831 0.0678  561 GLN Z CB    
11148 C  CG    . GLN F 561 ? 1.029  0.8732 0.5978 0.1225  0.2901 0.0707  561 GLN Z CG    
11149 C  CD    . GLN F 561 ? 1.0836 0.9097 0.6477 0.123   0.2925 0.0654  561 GLN Z CD    
11150 O  OE1   . GLN F 561 ? 1.1033 0.9288 0.6671 0.1224  0.2908 0.0639  561 GLN Z OE1   
11151 N  NE2   . GLN F 561 ? 1.0928 0.9036 0.6531 0.1239  0.2966 0.0626  561 GLN Z NE2   
11152 N  N     . LEU F 562 ? 0.9735 0.8431 0.5612 0.094   0.2674 0.0674  562 LEU Z N     
11153 C  CA    . LEU F 562 ? 0.9798 0.8486 0.5711 0.0853  0.2622 0.0643  562 LEU Z CA    
11154 C  C     . LEU F 562 ? 0.9797 0.8632 0.5751 0.0851  0.2614 0.0694  562 LEU Z C     
11155 O  O     . LEU F 562 ? 0.9821 0.8611 0.5786 0.0824  0.2613 0.068   562 LEU Z O     
11156 C  CB    . LEU F 562 ? 0.9806 0.8515 0.5738 0.0773  0.2552 0.0613  562 LEU Z CB    
11157 C  CG    . LEU F 562 ? 1.0043 0.8602 0.5939 0.0764  0.2552 0.056   562 LEU Z CG    
11158 C  CD1   . LEU F 562 ? 1.0095 0.8679 0.6002 0.0686  0.2484 0.0536  562 LEU Z CD1   
11159 C  CD2   . LEU F 562 ? 1.0194 0.8575 0.6071 0.0757  0.2579 0.051   562 LEU Z CD2   
11160 N  N     . ILE F 563 ? 0.9751 0.8761 0.5727 0.0883  0.2612 0.0757  563 ILE Z N     
11161 C  CA    . ILE F 563 ? 0.9766 0.8938 0.5786 0.0888  0.2607 0.0815  563 ILE Z CA    
11162 C  C     . ILE F 563 ? 0.9861 0.8979 0.5854 0.0963  0.2679 0.0838  563 ILE Z C     
11163 O  O     . ILE F 563 ? 0.9849 0.8987 0.5865 0.0943  0.2677 0.0847  563 ILE Z O     
11164 C  CB    . ILE F 563 ? 0.9754 0.9127 0.5802 0.0912  0.2591 0.088   563 ILE Z CB    
11165 C  CG1   . ILE F 563 ? 0.9847 0.9261 0.5909 0.0831  0.2517 0.0855  563 ILE Z CG1   
11166 C  CG2   . ILE F 563 ? 0.9746 0.9299 0.5844 0.0924  0.2592 0.0949  563 ILE Z CG2   
11167 C  CD1   . ILE F 563 ? 0.9989 0.9421 0.6088 0.0727  0.2451 0.0828  563 ILE Z CD1   
11168 N  N     . LYS F 564 ? 0.9942 0.8975 0.5879 0.1047  0.2744 0.0844  564 LYS Z N     
11169 C  CA    . LYS F 564 ? 1.0082 0.9042 0.5975 0.1122  0.2819 0.0864  564 LYS Z CA    
11170 C  C     . LYS F 564 ? 1.0204 0.8994 0.6075 0.1083  0.2823 0.0808  564 LYS Z C     
11171 O  O     . LYS F 564 ? 1.0237 0.8998 0.6086 0.1118  0.2864 0.0829  564 LYS Z O     
11172 C  CB    . LYS F 564 ? 1.038  0.927  0.6209 0.1215  0.2887 0.0877  564 LYS Z CB    
11173 C  CG    . LYS F 564 ? 1.0888 0.9951 0.6733 0.127   0.2893 0.0942  564 LYS Z CG    
11174 C  CD    . LYS F 564 ? 1.1417 1.0659 0.7297 0.1312  0.291  0.1022  564 LYS Z CD    
11175 C  CE    . LYS F 564 ? 1.1871 1.1285 0.7765 0.1373  0.2922 0.109   564 LYS Z CE    
11176 N  NZ    . LYS F 564 ? 1.2118 1.1661 0.8069 0.13    0.2841 0.1086  564 LYS Z NZ    
11177 N  N     . TYR F 565 ? 1.0247 0.8925 0.6121 0.1011  0.278  0.074   565 TYR Z N     
11178 C  CA    . TYR F 565 ? 1.0365 0.8891 0.6223 0.0968  0.2778 0.0688  565 TYR Z CA    
11179 C  C     . TYR F 565 ? 1.033  0.8941 0.6238 0.0914  0.2739 0.07    565 TYR Z C     
11180 O  O     . TYR F 565 ? 1.0347 0.8884 0.6236 0.0918  0.2763 0.0693  565 TYR Z O     
11181 C  CB    . TYR F 565 ? 1.0429 0.8828 0.6283 0.0907  0.2742 0.0619  565 TYR Z CB    
11182 C  CG    . TYR F 565 ? 1.0594 0.8825 0.6424 0.0875  0.2749 0.0568  565 TYR Z CG    
11183 C  CD1   . TYR F 565 ? 1.0773 0.8851 0.654  0.0922  0.2806 0.0549  565 TYR Z CD1   
11184 C  CD2   . TYR F 565 ? 1.0689 0.8914 0.6556 0.0797  0.2698 0.0538  565 TYR Z CD2   
11185 C  CE1   . TYR F 565 ? 1.0934 0.8862 0.6679 0.0889  0.2808 0.0504  565 TYR Z CE1   
11186 C  CE2   . TYR F 565 ? 1.0849 0.8926 0.6696 0.0768  0.2703 0.0494  565 TYR Z CE2   
11187 C  CZ    . TYR F 565 ? 1.1026 0.8957 0.6813 0.0813  0.2756 0.0477  565 TYR Z CZ    
11188 O  OH    . TYR F 565 ? 1.126  0.9049 0.7025 0.078   0.2758 0.0434  565 TYR Z OH    
11189 N  N     . ILE F 566 ? 1.0274 0.9034 0.6241 0.0861  0.268  0.0717  566 ILE Z N     
11190 C  CA    . ILE F 566 ? 1.0301 0.9158 0.6318 0.0806  0.2641 0.0731  566 ILE Z CA    
11191 C  C     . ILE F 566 ? 1.0364 0.9316 0.6383 0.0874  0.2689 0.0799  566 ILE Z C     
11192 O  O     . ILE F 566 ? 1.0378 0.9308 0.6401 0.0861  0.2695 0.08    566 ILE Z O     
11193 C  CB    . ILE F 566 ? 1.0274 0.927  0.6344 0.0736  0.2568 0.0738  566 ILE Z CB    
11194 C  CG1   . ILE F 566 ? 1.0414 0.9302 0.6471 0.0677  0.2528 0.0674  566 ILE Z CG1   
11195 C  CG2   . ILE F 566 ? 1.027  0.9367 0.6392 0.0674  0.2527 0.0754  566 ILE Z CG2   
11196 C  CD1   . ILE F 566 ? 1.0618 0.9348 0.6664 0.0623  0.2513 0.0611  566 ILE Z CD1   
11197 N  N     . GLU F 567 ? 1.0386 0.9433 0.6395 0.0951  0.2728 0.0855  567 GLU Z N     
11198 C  CA    . GLU F 567 ? 1.0471 0.9609 0.6475 0.1029  0.2783 0.0925  567 GLU Z CA    
11199 C  C     . GLU F 567 ? 1.0661 0.9629 0.6596 0.1081  0.2849 0.0911  567 GLU Z C     
11200 O  O     . GLU F 567 ? 1.0662 0.9667 0.6597 0.111   0.2878 0.0949  567 GLU Z O     
11201 C  CB    . GLU F 567 ? 1.0681 0.9938 0.6681 0.1106  0.2814 0.0984  567 GLU Z CB    
11202 C  CG    . GLU F 567 ? 1.1096 1.0544 0.7164 0.1057  0.2749 0.1011  567 GLU Z CG    
11203 C  CD    . GLU F 567 ? 1.1679 1.1268 0.775  0.113   0.2774 0.1076  567 GLU Z CD    
11204 O  OE1   . GLU F 567 ? 1.1841 1.1376 0.7859 0.1226  0.2848 0.1101  567 GLU Z OE1   
11205 O  OE2   . GLU F 567 ? 1.1809 1.1564 0.7934 0.1089  0.272  0.1103  567 GLU Z OE2   
11206 N  N     . TYR F 568 ? 1.0807 0.9589 0.6683 0.1087  0.287  0.0855  568 TYR Z N     
11207 C  CA    . TYR F 568 ? 1.1022 0.9619 0.6822 0.1124  0.2927 0.0831  568 TYR Z CA    
11208 C  C     . TYR F 568 ? 1.104  0.9579 0.6854 0.1061  0.2899 0.08    568 TYR Z C     
11209 O  O     . TYR F 568 ? 1.1072 0.9563 0.6847 0.1099  0.2944 0.0821  568 TYR Z O     
11210 C  CB    . TYR F 568 ? 1.1191 0.9616 0.6936 0.1127  0.2942 0.0775  568 TYR Z CB    
11211 C  CG    . TYR F 568 ? 1.1485 0.9701 0.7159 0.1129  0.2978 0.0731  568 TYR Z CG    
11212 C  CD1   . TYR F 568 ? 1.1687 0.9824 0.7283 0.1209  0.3054 0.076   568 TYR Z CD1   
11213 C  CD2   . TYR F 568 ? 1.1684 0.9777 0.7365 0.1053  0.2936 0.0662  568 TYR Z CD2   
11214 C  CE1   . TYR F 568 ? 1.1919 0.9857 0.7441 0.1206  0.3085 0.072   568 TYR Z CE1   
11215 C  CE2   . TYR F 568 ? 1.1907 0.9814 0.7524 0.105   0.2966 0.0623  568 TYR Z CE2   
11216 C  CZ    . TYR F 568 ? 1.2083 0.9911 0.7619 0.1125  0.3039 0.0651  568 TYR Z CZ    
11217 O  OH    . TYR F 568 ? 1.2372 1.001  0.7836 0.1118  0.3066 0.0613  568 TYR Z OH    
11218 N  N     . LEU F 569 ? 1.1006 0.9548 0.6872 0.0966  0.2828 0.0753  569 LEU Z N     
11219 C  CA    . LEU F 569 ? 1.1066 0.9558 0.6947 0.0904  0.2798 0.0724  569 LEU Z CA    
11220 C  C     . LEU F 569 ? 1.1009 0.9654 0.6934 0.0908  0.2794 0.078   569 LEU Z C     
11221 O  O     . LEU F 569 ? 1.104  0.9632 0.6947 0.0907  0.281  0.078   569 LEU Z O     
11222 C  CB    . LEU F 569 ? 1.1109 0.9573 0.7032 0.0807  0.2725 0.0665  569 LEU Z CB    
11223 C  CG    . LEU F 569 ? 1.1389 0.9696 0.7276 0.0794  0.2726 0.0606  569 LEU Z CG    
11224 C  CD1   . LEU F 569 ? 1.1474 0.9773 0.7404 0.0704  0.2656 0.0557  569 LEU Z CD1   
11225 C  CD2   . LEU F 569 ? 1.1546 0.9671 0.7367 0.0815  0.2769 0.0576  569 LEU Z CD2   
11226 N  N     . PHE F 570 ? 1.0911 0.9748 0.6891 0.0914  0.2774 0.0832  570 PHE Z N     
11227 C  CA    . PHE F 570 ? 1.0887 0.9892 0.6916 0.092   0.2771 0.0894  570 PHE Z CA    
11228 C  C     . PHE F 570 ? 1.0937 0.993  0.6917 0.1017  0.285  0.0948  570 PHE Z C     
11229 O  O     . PHE F 570 ? 1.0923 1.0003 0.6931 0.1021  0.2856 0.0989  570 PHE Z O     
11230 C  CB    . PHE F 570 ? 1.0791 1.0006 0.6886 0.0906  0.2732 0.094   570 PHE Z CB    
11231 C  CG    . PHE F 570 ? 1.084  1.0103 0.699  0.0798  0.2647 0.0902  570 PHE Z CG    
11232 C  CD1   . PHE F 570 ? 1.0956 1.0156 0.7121 0.0724  0.261  0.086   570 PHE Z CD1   
11233 C  CD2   . PHE F 570 ? 1.0884 1.0252 0.7065 0.0772  0.2605 0.0909  570 PHE Z CD2   
11234 C  CE1   . PHE F 570 ? 1.1011 1.0248 0.7217 0.0628  0.2536 0.0827  570 PHE Z CE1   
11235 C  CE2   . PHE F 570 ? 1.0938 1.0342 0.7158 0.0672  0.2529 0.0876  570 PHE Z CE2   
11236 C  CZ    . PHE F 570 ? 1.0932 1.0265 0.7162 0.0602  0.2497 0.0835  570 PHE Z CZ    
11237 N  N     . ASP F 571 ? 1.0981 0.9858 0.6885 0.1093  0.2914 0.0947  571 ASP Z N     
11238 C  CA    . ASP F 571 ? 1.1065 0.9894 0.6902 0.1188  0.2996 0.0992  571 ASP Z CA    
11239 C  C     . ASP F 571 ? 1.1079 0.9748 0.6866 0.117   0.3013 0.0958  571 ASP Z C     
11240 O  O     . ASP F 571 ? 1.1135 0.9757 0.6861 0.124   0.3078 0.0995  571 ASP Z O     
11241 C  CB    . ASP F 571 ? 1.1415 1.0149 0.7174 0.1269  0.3058 0.0996  571 ASP Z CB    
11242 C  CG    . ASP F 571 ? 1.2055 1.0955 0.7845 0.1322  0.3069 0.1054  571 ASP Z CG    
11243 O  OD1   . ASP F 571 ? 1.2109 1.1214 0.7978 0.1309  0.3037 0.1105  571 ASP Z OD1   
11244 O  OD2   . ASP F 571 ? 1.2387 1.1214 0.8122 0.1376  0.3108 0.105   571 ASP Z OD2   
11245 N  N     . PHE F 572 ? 1.1011 0.959  0.6816 0.108   0.2956 0.0889  572 PHE Z N     
11246 C  CA    . PHE F 572 ? 1.1047 0.9477 0.6808 0.1054  0.2963 0.0852  572 PHE Z CA    
11247 C  C     . PHE F 572 ? 1.0957 0.9458 0.6791 0.0966  0.2896 0.0835  572 PHE Z C     
11248 O  O     . PHE F 572 ? 1.0898 0.9503 0.6804 0.0904  0.2834 0.0822  572 PHE Z O     
11249 C  CB    . PHE F 572 ? 1.113  0.935  0.6828 0.1032  0.2966 0.0781  572 PHE Z CB    
11250 C  CG    . PHE F 572 ? 1.1273 0.9407 0.6892 0.1113  0.3032 0.0793  572 PHE Z CG    
11251 C  CD1   . PHE F 572 ? 1.1442 0.9478 0.6969 0.1189  0.3107 0.0821  572 PHE Z CD1   
11252 C  CD2   . PHE F 572 ? 1.1371 0.9517 0.7002 0.1115  0.3021 0.0777  572 PHE Z CD2   
11253 C  CE1   . PHE F 572 ? 1.1594 0.9542 0.704  0.1264  0.317  0.0832  572 PHE Z CE1   
11254 C  CE2   . PHE F 572 ? 1.1516 0.9582 0.7073 0.1191  0.3083 0.079   572 PHE Z CE2   
11255 C  CZ    . PHE F 572 ? 1.1559 0.9524 0.7022 0.1264  0.3158 0.0816  572 PHE Z CZ    
11256 N  N     . THR F 573 ? 1.094  0.9375 0.6749 0.096   0.291  0.0833  573 THR Z N     
11257 C  CA    . THR F 573 ? 1.0922 0.9403 0.6788 0.0881  0.2853 0.0815  573 THR Z CA    
11258 C  C     . THR F 573 ? 1.096  0.9339 0.684  0.0795  0.2793 0.0736  573 THR Z C     
11259 O  O     . THR F 573 ? 1.1058 0.9267 0.6876 0.08    0.2811 0.069   573 THR Z O     
11260 C  CB    . THR F 573 ? 1.1103 0.9497 0.6917 0.0905  0.2891 0.0825  573 THR Z CB    
11261 O  OG1   . THR F 573 ? 1.1174 0.9667 0.6976 0.099   0.295  0.0904  573 THR Z OG1   
11262 C  CG2   . THR F 573 ? 1.1144 0.9556 0.7006 0.0825  0.2837 0.08    573 THR Z CG2   
11263 N  N     . PRO F 574 ? 1.0867 0.9345 0.6824 0.0715  0.2724 0.0719  574 PRO Z N     
11264 C  CA    . PRO F 574 ? 1.0909 0.9285 0.6874 0.0637  0.2671 0.0646  574 PRO Z CA    
11265 C  C     . PRO F 574 ? 1.102  0.9223 0.6936 0.0616  0.2677 0.06    574 PRO Z C     
11266 O  O     . PRO F 574 ? 1.105  0.9249 0.6951 0.063   0.2697 0.0622  574 PRO Z O     
11267 C  CB    . PRO F 574 ? 1.0916 0.9428 0.696  0.0561  0.2605 0.0648  574 PRO Z CB    
11268 C  CG    . PRO F 574 ? 1.0886 0.9588 0.697  0.0598  0.2618 0.0721  574 PRO Z CG    
11269 C  CD    . PRO F 574 ? 1.0704 0.9383 0.6737 0.0691  0.2693 0.0767  574 PRO Z CD    
11270 N  N     . SER F 575 ? 1.1068 0.913  0.6959 0.0584  0.2661 0.054   575 SER Z N     
11271 C  CA    . SER F 575 ? 1.1194 0.9094 0.704  0.056   0.2663 0.0496  575 SER Z CA    
11272 C  C     . SER F 575 ? 1.1205 0.9136 0.7088 0.0499  0.2621 0.0486  575 SER Z C     
11273 O  O     . SER F 575 ? 1.1233 0.9101 0.7079 0.051   0.2642 0.0491  575 SER Z O     
11274 C  CB    . SER F 575 ? 1.1403 0.9174 0.7232 0.0527  0.2645 0.0437  575 SER Z CB    
11275 O  OG    . SER F 575 ? 1.1698 0.9437 0.7491 0.0583  0.2684 0.0445  575 SER Z OG    
11276 N  N     . VAL F 576 ? 1.1161 0.9188 0.7111 0.0436  0.2564 0.0476  576 VAL Z N     
11277 C  CA    . VAL F 576 ? 1.1217 0.9274 0.7204 0.0373  0.2522 0.0464  576 VAL Z CA    
11278 C  C     . VAL F 576 ? 1.1208 0.9446 0.7264 0.034   0.2484 0.0497  576 VAL Z C     
11279 O  O     . VAL F 576 ? 1.1181 0.9513 0.726  0.0356  0.2482 0.0519  576 VAL Z O     
11280 C  CB    . VAL F 576 ? 1.1352 0.9283 0.7335 0.0308  0.2481 0.0397  576 VAL Z CB    
11281 C  CG1   . VAL F 576 ? 1.1498 0.9262 0.7416 0.0326  0.251  0.037   576 VAL Z CG1   
11282 C  CG2   . VAL F 576 ? 1.1411 0.9331 0.741  0.0287  0.2457 0.0368  576 VAL Z CG2   
11283 N  N     . GLN F 577 ? 1.1217 0.9503 0.7304 0.0292  0.2455 0.05    577 GLN Z N     
11284 C  CA    . GLN F 577 ? 1.1252 0.9699 0.7401 0.0247  0.2414 0.0527  577 GLN Z CA    
11285 C  C     . GLN F 577 ? 1.1359 0.9784 0.7528 0.0171  0.237  0.0497  577 GLN Z C     
11286 O  O     . GLN F 577 ? 1.1431 0.9748 0.7568 0.0172  0.2382 0.0475  577 GLN Z O     
11287 C  CB    . GLN F 577 ? 1.1365 0.9966 0.7537 0.0299  0.2447 0.0602  577 GLN Z CB    
11288 C  CG    . GLN F 577 ? 1.1745 1.0336 0.7903 0.0324  0.2478 0.0628  577 GLN Z CG    
11289 C  CD    . GLN F 577 ? 1.2158 1.0881 0.8373 0.0272  0.2443 0.0655  577 GLN Z CD    
11290 O  OE1   . GLN F 577 ? 1.2249 1.111  0.8517 0.0233  0.2406 0.0674  577 GLN Z OE1   
11291 N  NE2   . GLN F 577 ? 1.2234 1.0914 0.8436 0.0267  0.2454 0.0656  577 GLN Z NE2   
11292 N  N     . ARG F 578 ? 1.1352 0.9874 0.7565 0.0107  0.232  0.0497  578 ARG Z N     
11293 C  CA    . ARG F 578 ? 1.1454 0.996  0.7683 0.0034  0.2279 0.0472  578 ARG Z CA    
11294 C  C     . ARG F 578 ? 1.1481 1.014  0.7759 -0.0023 0.2236 0.0498  578 ARG Z C     
11295 O  O     . ARG F 578 ? 1.1467 1.022  0.7764 -0.0022 0.2224 0.0519  578 ARG Z O     
11296 C  CB    . ARG F 578 ? 1.1678 1.0031 0.788  -0.001  0.2251 0.0403  578 ARG Z CB    
11297 C  CG    . ARG F 578 ? 1.2032 1.039  0.8241 -0.0042 0.2219 0.0379  578 ARG Z CG    
11298 C  CD    . ARG F 578 ? 1.2413 1.0658 0.8609 -0.0104 0.2181 0.0321  578 ARG Z CD    
11299 N  NE    . ARG F 578 ? 1.2691 1.0936 0.8887 -0.0134 0.2152 0.03    578 ARG Z NE    
11300 C  CZ    . ARG F 578 ? 1.2962 1.1129 0.9148 -0.019  0.2117 0.0256  578 ARG Z CZ    
11301 N  NH1   . ARG F 578 ? 1.2941 1.1029 0.9118 -0.0223 0.2105 0.0228  578 ARG Z NH1   
11302 N  NH2   . ARG F 578 ? 1.296  1.1125 0.914  -0.0212 0.2095 0.0241  578 ARG Z NH2   
11303 N  N     . LYS F 579 ? 1.151  1.0193 0.7805 -0.0075 0.2211 0.0497  579 LYS Z N     
11304 C  CA    . LYS F 579 ? 1.1573 1.039  0.7909 -0.014  0.2167 0.0519  579 LYS Z CA    
11305 C  C     . LYS F 579 ? 1.1695 1.0438 0.8015 -0.0213 0.2117 0.0464  579 LYS Z C     
11306 O  O     . LYS F 579 ? 1.1777 1.0372 0.8065 -0.0226 0.2113 0.0412  579 LYS Z O     
11307 C  CB    . LYS F 579 ? 1.18   1.0674 0.8159 -0.0166 0.2164 0.0543  579 LYS Z CB    
11308 C  CG    . LYS F 579 ? 1.2256 1.1274 0.8656 -0.0237 0.2119 0.057   579 LYS Z CG    
11309 C  CD    . LYS F 579 ? 1.2777 1.1864 0.9203 -0.0255 0.2123 0.0602  579 LYS Z CD    
11310 C  CE    . LYS F 579 ? 1.3175 1.2399 0.9636 -0.0188 0.2165 0.0675  579 LYS Z CE    
11311 N  NZ    . LYS F 579 ? 1.3371 1.2758 0.987  -0.0187 0.2153 0.0721  579 LYS Z NZ    
11312 N  N     . ILE F 580 ? 1.1684 1.0527 0.8023 -0.0259 0.208  0.0477  580 ILE Z N     
11313 C  CA    . ILE F 580 ? 1.18   1.0572 0.8116 -0.0326 0.2035 0.0429  580 ILE Z CA    
11314 C  C     . ILE F 580 ? 1.1881 1.0588 0.8184 -0.0396 0.2005 0.0397  580 ILE Z C     
11315 O  O     . ILE F 580 ? 1.1961 1.0558 0.8231 -0.0438 0.198  0.0347  580 ILE Z O     
11316 C  CB    . ILE F 580 ? 1.1835 1.0728 0.8164 -0.0359 0.2003 0.0453  580 ILE Z CB    
11317 C  CG1   . ILE F 580 ? 1.2007 1.0798 0.8296 -0.0397 0.1974 0.0403  580 ILE Z CG1   
11318 C  CG2   . ILE F 580 ? 1.1844 1.088  0.8205 -0.042  0.1971 0.0491  580 ILE Z CG2   
11319 C  CD1   . ILE F 580 ? 1.2228 1.089  0.849  -0.0338 0.2005 0.037   580 ILE Z CD1   
11320 N  N     . ALA F 581 ? 1.1841 1.0611 0.8168 -0.0404 0.2011 0.0425  581 ALA Z N     
11321 C  CA    . ALA F 581 ? 1.1926 1.0636 0.8241 -0.0465 0.1987 0.0397  581 ALA Z CA    
11322 C  C     . ALA F 581 ? 1.1995 1.0565 0.8286 -0.043  0.2015 0.0365  581 ALA Z C     
11323 O  O     . ALA F 581 ? 1.2064 1.0517 0.8326 -0.0469 0.1996 0.0318  581 ALA Z O     
11324 C  CB    . ALA F 581 ? 1.1907 1.076  0.8259 -0.05   0.1976 0.0445  581 ALA Z CB    
11325 N  N     . GLY F 582 ? 1.1962 1.0542 0.8261 -0.0357 0.206  0.0392  582 GLY Z N     
11326 C  CA    . GLY F 582 ? 1.2053 1.0503 0.8324 -0.0321 0.2088 0.0366  582 GLY Z CA    
11327 C  C     . GLY F 582 ? 1.2126 1.0431 0.8362 -0.0307 0.209  0.0315  582 GLY Z C     
11328 O  O     . GLY F 582 ? 1.2189 1.0376 0.8401 -0.0335 0.2077 0.0271  582 GLY Z O     
11329 N  N     . GLY F 583 ? 1.2096 1.0414 0.8331 -0.0263 0.2108 0.0323  583 GLY Z N     
11330 C  CA    . GLY F 583 ? 1.2172 1.0366 0.8378 -0.0247 0.2112 0.0281  583 GLY Z CA    
11331 C  C     . GLY F 583 ? 1.22   1.0288 0.8378 -0.0188 0.2153 0.027   583 GLY Z C     
11332 O  O     . GLY F 583 ? 1.2251 1.0244 0.8407 -0.017  0.216  0.024   583 GLY Z O     
11333 N  N     . ASN F 584 ? 1.2144 1.0243 0.8318 -0.016  0.2179 0.0295  584 ASN Z N     
11334 C  CA    . ASN F 584 ? 1.2188 1.0178 0.8323 -0.0107 0.2218 0.0286  584 ASN Z CA    
11335 C  C     . ASN F 584 ? 1.2097 1.0126 0.8222 -0.0035 0.2263 0.0322  584 ASN Z C     
11336 O  O     . ASN F 584 ? 1.2061 1.0208 0.8206 -0.0007 0.2282 0.0373  584 ASN Z O     
11337 C  CB    . ASN F 584 ? 1.2384 1.0354 0.8507 -0.0107 0.2229 0.0296  584 ASN Z CB    
11338 C  CG    . ASN F 584 ? 1.2837 1.0776 0.8968 -0.0176 0.2188 0.0265  584 ASN Z CG    
11339 O  OD1   . ASN F 584 ? 1.3022 1.0903 0.9153 -0.0218 0.2156 0.0224  584 ASN Z OD1   
11340 N  ND2   . ASN F 584 ? 1.2904 1.0878 0.904  -0.0186 0.219  0.0285  584 ASN Z ND2   
11341 N  N     . TRP F 585 ? 1.2038 0.9969 0.8133 -0.0005 0.228  0.0297  585 TRP Z N     
11342 C  CA    . TRP F 585 ? 1.1993 0.9943 0.807  0.0065  0.2325 0.0327  585 TRP Z CA    
11343 C  C     . TRP F 585 ? 1.1937 0.9855 0.7975 0.0122  0.2374 0.0356  585 TRP Z C     
11344 O  O     . TRP F 585 ? 1.201  0.9818 0.8013 0.0116  0.2379 0.0331  585 TRP Z O     
11345 C  CB    . TRP F 585 ? 1.2032 0.9874 0.8082 0.0079  0.2332 0.0291  585 TRP Z CB    
11346 C  CG    . TRP F 585 ? 1.2071 0.9947 0.8151 0.0042  0.2296 0.0272  585 TRP Z CG    
11347 C  CD1   . TRP F 585 ? 1.2208 1.0012 0.8293 -0.001  0.2259 0.0226  585 TRP Z CD1   
11348 C  CD2   . TRP F 585 ? 1.2045 1.0026 0.8146 0.0061  0.2298 0.03    585 TRP Z CD2   
11349 N  NE1   . TRP F 585 ? 1.2223 1.0076 0.8328 -0.0026 0.2239 0.0222  585 TRP Z NE1   
11350 C  CE2   . TRP F 585 ? 1.2151 1.0112 0.8265 0.0015  0.2261 0.0266  585 TRP Z CE2   
11351 C  CE3   . TRP F 585 ? 1.2078 1.0169 0.8187 0.0114  0.2329 0.0352  585 TRP Z CE3   
11352 C  CZ2   . TRP F 585 ? 1.2205 1.0248 0.8336 0.0018  0.2251 0.0281  585 TRP Z CZ2   
11353 C  CZ3   . TRP F 585 ? 1.216  1.034  0.8291 0.0116  0.2318 0.0367  585 TRP Z CZ3   
11354 C  CH2   . TRP F 585 ? 1.2184 1.0337 0.8324 0.0067  0.2279 0.0331  585 TRP Z CH2   
11355 N  N     . GLU F 586 ? 1.1796 0.9806 0.7835 0.018   0.2412 0.0408  586 GLU Z N     
11356 C  CA    . GLU F 586 ? 1.1778 0.9764 0.7773 0.0246  0.2468 0.0444  586 GLU Z CA    
11357 C  C     . GLU F 586 ? 1.1705 0.9686 0.7669 0.0317  0.2515 0.0468  586 GLU Z C     
11358 O  O     . GLU F 586 ? 1.1683 0.9717 0.7674 0.0314  0.2501 0.0466  586 GLU Z O     
11359 C  CB    . GLU F 586 ? 1.1982 1.011  0.8014 0.0253  0.2474 0.0499  586 GLU Z CB    
11360 C  CG    . GLU F 586 ? 1.251  1.0622 0.8554 0.0199  0.2445 0.0483  586 GLU Z CG    
11361 C  CD    . GLU F 586 ? 1.3094 1.1289 0.9146 0.0228  0.2472 0.0537  586 GLU Z CD    
11362 O  OE1   . GLU F 586 ? 1.3157 1.143  0.9205 0.0293  0.2517 0.0592  586 GLU Z OE1   
11363 O  OE2   . GLU F 586 ? 1.3301 1.1482 0.936  0.0187  0.2451 0.0526  586 GLU Z OE2   
11364 N  N     . PHE F 587 ? 1.1653 0.9569 0.7554 0.0383  0.2572 0.0492  587 PHE Z N     
11365 C  CA    . PHE F 587 ? 1.1632 0.954  0.7495 0.0457  0.2623 0.0519  587 PHE Z CA    
11366 C  C     . PHE F 587 ? 1.1542 0.9642 0.7458 0.049   0.2633 0.0582  587 PHE Z C     
11367 O  O     . PHE F 587 ? 1.1502 0.972  0.7463 0.0476  0.2622 0.0617  587 PHE Z O     
11368 C  CB    . PHE F 587 ? 1.1652 0.9439 0.7426 0.0519  0.2684 0.0533  587 PHE Z CB    
11369 C  CG    . PHE F 587 ? 1.1776 0.9366 0.7482 0.0501  0.2684 0.0476  587 PHE Z CG    
11370 C  CD1   . PHE F 587 ? 1.1892 0.9417 0.7595 0.0484  0.2669 0.0437  587 PHE Z CD1   
11371 C  CD2   . PHE F 587 ? 1.1908 0.938  0.7553 0.0501  0.27   0.0465  587 PHE Z CD2   
11372 C  CE1   . PHE F 587 ? 1.2043 0.9397 0.7689 0.0465  0.2668 0.0388  587 PHE Z CE1   
11373 C  CE2   . PHE F 587 ? 1.2062 0.936  0.7645 0.0481  0.2697 0.0416  587 PHE Z CE2   
11374 C  CZ    . PHE F 587 ? 1.2056 0.93   0.7643 0.0462  0.2681 0.0378  587 PHE Z CZ    
11375 N  N     . GLY F 588 ? 1.1493 0.9624 0.7406 0.0531  0.2653 0.0597  588 GLY Z N     
11376 C  CA    . GLY F 588 ? 1.1439 0.9752 0.7399 0.0565  0.2663 0.0658  588 GLY Z CA    
11377 C  C     . GLY F 588 ? 1.1427 0.9798 0.7364 0.0638  0.2721 0.0724  588 GLY Z C     
11378 O  O     . GLY F 588 ? 1.1499 0.9748 0.7356 0.0698  0.2777 0.0729  588 GLY Z O     
11379 N  N     . ASN F 589 ? 1.1321 0.9874 0.7325 0.0633  0.2709 0.0778  589 ASN Z N     
11380 C  CA    . ASN F 589 ? 1.1329 0.9956 0.7321 0.0703  0.2764 0.0849  589 ASN Z CA    
11381 C  C     . ASN F 589 ? 1.1204 1.001  0.7236 0.0759  0.2788 0.0919  589 ASN Z C     
11382 O  O     . ASN F 589 ? 1.1216 1.0026 0.7203 0.0849  0.2855 0.0971  589 ASN Z O     
11383 C  CB    . ASN F 589 ? 1.1473 1.0166 0.7509 0.0656  0.2737 0.0861  589 ASN Z CB    
11384 C  CG    . ASN F 589 ? 1.1875 1.0668 0.7913 0.0722  0.2789 0.0939  589 ASN Z CG    
11385 O  OD1   . ASN F 589 ? 1.2066 1.0783 0.8031 0.0806  0.2858 0.0967  589 ASN Z OD1   
11386 N  ND2   . ASN F 589 ? 1.1891 1.0854 0.8009 0.0685  0.2759 0.0978  589 ASN Z ND2   
11387 N  N     . LYS F 590 ? 1.106  1.0013 0.717  0.0707  0.2733 0.0924  590 LYS Z N     
11388 C  CA    . LYS F 590 ? 1.0967 1.0106 0.7122 0.0751  0.2746 0.0992  590 LYS Z CA    
11389 C  C     . LYS F 590 ? 1.0926 1.0042 0.7068 0.0764  0.2741 0.097   590 LYS Z C     
11390 O  O     . LYS F 590 ? 1.098  1.0003 0.7118 0.0703  0.2697 0.0903  590 LYS Z O     
11391 C  CB    . LYS F 590 ? 1.11   1.044  0.7353 0.0684  0.2688 0.1022  590 LYS Z CB    
11392 C  CG    . LYS F 590 ? 1.1585 1.0968 0.786  0.067   0.2693 0.1051  590 LYS Z CG    
11393 C  CD    . LYS F 590 ? 1.2013 1.1577 0.8379 0.0589  0.2629 0.1071  590 LYS Z CD    
11394 C  CE    . LYS F 590 ? 1.2413 1.202  0.8804 0.0571  0.2632 0.1098  590 LYS Z CE    
11395 N  NZ    . LYS F 590 ? 1.2593 1.2375 0.907  0.0487  0.2569 0.1118  590 LYS Z NZ    
11396 N  N     . SER F 591 ? 1.0806 1.0011 0.6942 0.0844  0.2787 0.1029  591 SER Z N     
11397 C  CA    . SER F 591 ? 1.0776 0.9971 0.6898 0.0867  0.2788 0.1017  591 SER Z CA    
11398 C  C     . SER F 591 ? 1.0607 0.9981 0.681  0.0811  0.2726 0.1031  591 SER Z C     
11399 O  O     . SER F 591 ? 1.0532 1.0081 0.6804 0.0784  0.27   0.1078  591 SER Z O     
11400 C  CB    . SER F 591 ? 1.0955 1.016  0.7026 0.0983  0.2869 0.1075  591 SER Z CB    
11401 O  OG    . SER F 591 ? 1.1331 1.0322 0.7306 0.1023  0.2914 0.1031  591 SER Z OG    
11402 N  N     . LEU F 592 ? 1.0533 0.9865 0.6727 0.0793  0.2702 0.0993  592 LEU Z N     
11403 C  CA    . LEU F 592 ? 1.0434 0.9918 0.6691 0.0742  0.2644 0.1003  592 LEU Z CA    
11404 C  C     . LEU F 592 ? 1.0332 0.9905 0.6582 0.082   0.2679 0.1054  592 LEU Z C     
11405 O  O     . LEU F 592 ? 1.0385 0.984  0.657  0.0891  0.2735 0.1045  592 LEU Z O     
11406 C  CB    . LEU F 592 ? 1.0508 0.9883 0.6761 0.0656  0.2584 0.0922  592 LEU Z CB    
11407 C  CG    . LEU F 592 ? 1.0697 1.0076 0.6988 0.0554  0.252  0.0887  592 LEU Z CG    
11408 C  CD1   . LEU F 592 ? 1.083  1.0084 0.7092 0.0554  0.2543 0.0863  592 LEU Z CD1   
11409 C  CD2   . LEU F 592 ? 1.081  1.0104 0.7095 0.048   0.2465 0.0819  592 LEU Z CD2   
11410 N  N     . VAL F 593 ? 1.0158 0.9942 0.6474 0.0806  0.2648 0.1109  593 VAL Z N     
11411 C  CA    . VAL F 593 ? 1.0094 0.9991 0.6412 0.0879  0.2678 0.1164  593 VAL Z CA    
11412 C  C     . VAL F 593 ? 1.0011 0.9961 0.6353 0.0822  0.2617 0.114   593 VAL Z C     
11413 O  O     . VAL F 593 ? 1      1.0026 0.639  0.0729  0.2547 0.1125  593 VAL Z O     
11414 C  CB    . VAL F 593 ? 1.0103 1.0213 0.6473 0.0929  0.2704 0.1263  593 VAL Z CB    
11415 C  CG1   . VAL F 593 ? 1.0125 1.0376 0.6505 0.0999  0.2728 0.1326  593 VAL Z CG1   
11416 C  CG2   . VAL F 593 ? 1.0209 1.0243 0.6539 0.0999  0.2775 0.1288  593 VAL Z CG2   
11417 N  N     . PRO F 594 ? 0.9934 0.9834 0.6233 0.0878  0.2645 0.1135  594 PRO Z N     
11418 C  CA    . PRO F 594 ? 0.9844 0.978  0.6156 0.0828  0.259  0.111   594 PRO Z CA    
11419 C  C     . PRO F 594 ? 0.965  0.9822 0.6034 0.0786  0.2537 0.1166  594 PRO Z C     
11420 O  O     . PRO F 594 ? 0.9671 0.986  0.6069 0.0705  0.2471 0.1132  594 PRO Z O     
11421 C  CB    . PRO F 594 ? 0.9995 0.9855 0.625  0.0917  0.2646 0.1111  594 PRO Z CB    
11422 C  CG    . PRO F 594 ? 1.0131 0.9852 0.6328 0.0991  0.2721 0.111   594 PRO Z CG    
11423 C  CD    . PRO F 594 ? 0.9909 0.9707 0.6141 0.0987  0.2729 0.1149  594 PRO Z CD    
11424 N  N     . ASN F 595 ? 0.9445 0.9799 0.587  0.0839  0.2565 0.1252  595 ASN Z N     
11425 C  CA    . ASN F 595 ? 0.9272 0.9865 0.5769 0.0799  0.2513 0.1313  595 ASN Z CA    
11426 C  C     . ASN F 595 ? 0.9123 0.9777 0.5672 0.0682  0.2441 0.1296  595 ASN Z C     
11427 O  O     . ASN F 595 ? 0.9051 0.9883 0.5653 0.0626  0.2386 0.1333  595 ASN Z O     
11428 C  CB    . ASN F 595 ? 0.9336 1.0115 0.5867 0.0891  0.2565 0.1414  595 ASN Z CB    
11429 C  CG    . ASN F 595 ? 0.9647 1.0617 0.6214 0.0899  0.2538 0.147   595 ASN Z CG    
11430 O  OD1   . ASN F 595 ? 0.9753 1.0816 0.6357 0.0807  0.2461 0.146   595 ASN Z OD1   
11431 N  ND2   . ASN F 595 ? 0.9706 1.0737 0.6258 0.101   0.2602 0.153   595 ASN Z ND2   
11432 N  N     . ASP F 596 ? 0.9073 0.9575 0.5602 0.0643  0.244  0.1239  596 ASP Z N     
11433 C  CA    . ASP F 596 ? 0.904  0.9571 0.5606 0.0531  0.2373 0.1215  596 ASP Z CA    
11434 C  C     . ASP F 596 ? 0.9015 0.9459 0.5559 0.0437  0.2305 0.1143  596 ASP Z C     
11435 O  O     . ASP F 596 ? 0.903  0.9491 0.5594 0.0339  0.2245 0.1119  596 ASP Z O     
11436 C  CB    . ASP F 596 ? 0.9306 0.9702 0.5856 0.0528  0.2399 0.1182  596 ASP Z CB    
11437 C  CG    . ASP F 596 ? 0.9762 1.0262 0.6367 0.0454  0.236  0.1202  596 ASP Z CG    
11438 O  OD1   . ASP F 596 ? 0.977  1.0432 0.6425 0.0386  0.2302 0.123   596 ASP Z OD1   
11439 O  OD2   . ASP F 596 ? 1.0037 1.0455 0.6634 0.0461  0.2386 0.1189  596 ASP Z OD2   
11440 N  N     . PHE F 597 ? 0.896  0.9305 0.5455 0.047   0.2317 0.1109  597 PHE Z N     
11441 C  CA    . PHE F 597 ? 0.8945 0.9189 0.5407 0.0399  0.2264 0.1043  597 PHE Z CA    
11442 C  C     . PHE F 597 ? 0.8816 0.9131 0.5267 0.0425  0.2256 0.1064  597 PHE Z C     
11443 O  O     . PHE F 597 ? 0.8793 0.9181 0.5246 0.0517  0.2305 0.1116  597 PHE Z O     
11444 C  CB    . PHE F 597 ? 0.9047 0.9042 0.5449 0.0412  0.2292 0.0964  597 PHE Z CB    
11445 C  CG    . PHE F 597 ? 0.9175 0.9081 0.558  0.0395  0.2306 0.094   597 PHE Z CG    
11446 C  CD1   . PHE F 597 ? 0.9287 0.9179 0.5709 0.0297  0.2251 0.0907  597 PHE Z CD1   
11447 C  CD2   . PHE F 597 ? 0.9302 0.9136 0.5686 0.0477  0.2375 0.0951  597 PHE Z CD2   
11448 C  CE1   . PHE F 597 ? 0.9403 0.9216 0.5826 0.0284  0.2263 0.0887  597 PHE Z CE1   
11449 C  CE2   . PHE F 597 ? 0.9422 0.9174 0.5804 0.0461  0.2386 0.093   597 PHE Z CE2   
11450 C  CZ    . PHE F 597 ? 0.9401 0.9146 0.5805 0.0365  0.233  0.0899  597 PHE Z CZ    
11451 N  N     . ILE F 598 ? 0.8728 0.9012 0.516  0.0347  0.2195 0.1023  598 ILE Z N     
11452 C  CA    . ILE F 598 ? 0.8689 0.9012 0.5099 0.0366  0.2183 0.1032  598 ILE Z CA    
11453 C  C     . ILE F 598 ? 0.8721 0.8819 0.5066 0.0398  0.2214 0.0962  598 ILE Z C     
11454 O  O     . ILE F 598 ? 0.8803 0.8753 0.5122 0.0335  0.2188 0.0895  598 ILE Z O     
11455 C  CB    . ILE F 598 ? 0.8725 0.9132 0.5141 0.0259  0.2099 0.1027  598 ILE Z CB    
11456 C  CG1   . ILE F 598 ? 0.8742 0.9365 0.5226 0.0211  0.2063 0.1092  598 ILE Z CG1   
11457 C  CG2   . ILE F 598 ? 0.8794 0.9227 0.5179 0.0278  0.2087 0.1033  598 ILE Z CG2   
11458 C  CD1   . ILE F 598 ? 0.8818 0.9645 0.5351 0.0289  0.2097 0.1184  598 ILE Z CD1   
11459 N  N     . LEU F 599 ? 0.8632 0.87   0.4952 0.0497  0.2273 0.0978  599 LEU Z N     
11460 C  CA    . LEU F 599 ? 0.8668 0.8526 0.4928 0.0529  0.2306 0.0915  599 LEU Z CA    
11461 C  C     . LEU F 599 ? 0.8601 0.8448 0.4828 0.0528  0.2285 0.0902  599 LEU Z C     
11462 O  O     . LEU F 599 ? 0.8563 0.8533 0.4796 0.0581  0.2299 0.0955  599 LEU Z O     
11463 C  CB    . LEU F 599 ? 0.8714 0.8505 0.4953 0.0637  0.2391 0.0932  599 LEU Z CB    
11464 C  CG    . LEU F 599 ? 0.8876 0.8651 0.5133 0.0652  0.2423 0.0944  599 LEU Z CG    
11465 C  CD1   . LEU F 599 ? 0.898  0.8674 0.5198 0.076   0.2507 0.096   599 LEU Z CD1   
11466 C  CD2   . LEU F 599 ? 0.9008 0.8635 0.5255 0.0577  0.2393 0.0875  599 LEU Z CD2   
11467 N  N     . LEU F 600 ? 0.8571 0.8271 0.4761 0.0469  0.2253 0.0833  600 LEU Z N     
11468 C  CA    . LEU F 600 ? 0.8573 0.8236 0.4722 0.0466  0.2235 0.0814  600 LEU Z CA    
11469 C  C     . LEU F 600 ? 0.8616 0.8058 0.4714 0.0491  0.2269 0.0748  600 LEU Z C     
11470 O  O     . LEU F 600 ? 0.8671 0.7987 0.4766 0.0466  0.2275 0.0703  600 LEU Z O     
11471 C  CB    . LEU F 600 ? 0.8583 0.829  0.4729 0.036   0.2154 0.0798  600 LEU Z CB    
11472 C  CG    . LEU F 600 ? 0.8684 0.8615 0.4874 0.032   0.2108 0.0862  600 LEU Z CG    
11473 C  CD1   . LEU F 600 ? 0.8755 0.8688 0.4922 0.021   0.203  0.0835  600 LEU Z CD1   
11474 C  CD2   . LEU F 600 ? 0.872  0.8798 0.4922 0.0394  0.2131 0.0927  600 LEU Z CD2   
11475 N  N     . SER F 601 ? 0.8566 0.7965 0.4626 0.054   0.229  0.0743  601 SER Z N     
11476 C  CA    . SER F 601 ? 0.8614 0.7811 0.4628 0.0562  0.2321 0.0684  601 SER Z CA    
11477 C  C     . SER F 601 ? 0.8567 0.7705 0.4542 0.0512  0.2277 0.0648  601 SER Z C     
11478 O  O     . SER F 601 ? 0.8523 0.7778 0.4496 0.0495  0.2241 0.0678  601 SER Z O     
11479 C  CB    . SER F 601 ? 0.8786 0.7947 0.4777 0.0669  0.2395 0.0704  601 SER Z CB    
11480 O  OG    . SER F 601 ? 0.8974 0.8256 0.4959 0.0713  0.2398 0.0751  601 SER Z OG    
11481 N  N     . ALA F 602 ? 0.8562 0.7521 0.4507 0.0488  0.2279 0.0585  602 ALA Z N     
11482 C  CA    . ALA F 602 ? 0.8584 0.7464 0.4486 0.0444  0.2243 0.0548  602 ALA Z CA    
11483 C  C     . ALA F 602 ? 0.8602 0.7296 0.4467 0.048   0.2284 0.05    602 ALA Z C     
11484 O  O     . ALA F 602 ? 0.8664 0.7259 0.4538 0.0502  0.2321 0.0476  602 ALA Z O     
11485 C  CB    . ALA F 602 ? 0.8602 0.747  0.4506 0.0341  0.2181 0.052   602 ALA Z CB    
11486 N  N     . GLY F 603 ? 0.8531 0.7179 0.4354 0.0486  0.2277 0.0486  603 GLY Z N     
11487 C  CA    . GLY F 603 ? 0.8571 0.7047 0.4358 0.0516  0.2313 0.0442  603 GLY Z CA    
11488 C  C     . GLY F 603 ? 0.8554 0.6935 0.4306 0.0446  0.2268 0.0399  603 GLY Z C     
11489 O  O     . GLY F 603 ? 0.8542 0.6983 0.4267 0.0411  0.2226 0.041   603 GLY Z O     
11490 N  N     . ALA F 604 ? 0.8545 0.6781 0.4295 0.0423  0.2276 0.0351  604 ALA Z N     
11491 C  CA    . ALA F 604 ? 0.8613 0.6745 0.4325 0.0361  0.224  0.0311  604 ALA Z CA    
11492 C  C     . ALA F 604 ? 0.8677 0.6658 0.4358 0.0402  0.228  0.0278  604 ALA Z C     
11493 O  O     . ALA F 604 ? 0.8738 0.6655 0.4438 0.0451  0.2329 0.027   604 ALA Z O     
11494 C  CB    . ALA F 604 ? 0.8639 0.6729 0.4373 0.0296  0.2214 0.0284  604 ALA Z CB    
11495 N  N     . PHE F 605 ? 0.8647 0.6569 0.4275 0.0382  0.2259 0.0262  605 PHE Z N     
11496 C  CA    . PHE F 605 ? 0.8728 0.6512 0.4325 0.0422  0.2297 0.0236  605 PHE Z CA    
11497 C  C     . PHE F 605 ? 0.8838 0.6536 0.4375 0.0377  0.2264 0.021   605 PHE Z C     
11498 O  O     . PHE F 605 ? 0.884  0.6594 0.4352 0.0318  0.2212 0.0216  605 PHE Z O     
11499 C  CB    . PHE F 605 ? 0.8678 0.6506 0.4265 0.0503  0.2338 0.0264  605 PHE Z CB    
11500 C  CG    . PHE F 605 ? 0.8673 0.6638 0.4238 0.0499  0.2305 0.0303  605 PHE Z CG    
11501 C  CD1   . PHE F 605 ? 0.8776 0.6715 0.4282 0.0476  0.2275 0.0296  605 PHE Z CD1   
11502 C  CD2   . PHE F 605 ? 0.8673 0.6794 0.4276 0.0517  0.2303 0.0347  605 PHE Z CD2   
11503 C  CE1   . PHE F 605 ? 0.8811 0.688  0.4296 0.0465  0.2239 0.0332  605 PHE Z CE1   
11504 C  CE2   . PHE F 605 ? 0.8706 0.6965 0.4294 0.051   0.2269 0.0386  605 PHE Z CE2   
11505 C  CZ    . PHE F 605 ? 0.8709 0.6942 0.4239 0.0483  0.2236 0.0378  605 PHE Z CZ    
11506 N  N     . ILE F 606 ? 0.8918 0.6478 0.4428 0.0405  0.2296 0.0183  606 ILE Z N     
11507 C  CA    . ILE F 606 ? 0.9058 0.6523 0.4503 0.0373  0.2273 0.0161  606 ILE Z CA    
11508 C  C     . ILE F 606 ? 0.9172 0.6651 0.4566 0.0415  0.2283 0.0178  606 ILE Z C     
11509 O  O     . ILE F 606 ? 0.9203 0.6664 0.4608 0.0485  0.2331 0.0185  606 ILE Z O     
11510 C  CB    . ILE F 606 ? 0.9164 0.647  0.4609 0.037   0.2298 0.0123  606 ILE Z CB    
11511 C  CG1   . ILE F 606 ? 0.926  0.6554 0.4739 0.0313  0.2275 0.0106  606 ILE Z CG1   
11512 C  CG2   . ILE F 606 ? 0.9294 0.649  0.4663 0.0359  0.2291 0.0105  606 ILE Z CG2   
11513 C  CD1   . ILE F 606 ? 0.9439 0.6606 0.4941 0.0321  0.2306 0.0077  606 ILE Z CD1   
11514 N  N     . ASP F 607 ? 0.9224 0.6735 0.456  0.0372  0.2236 0.0185  607 ASP Z N     
11515 C  CA    . ASP F 607 ? 0.9361 0.6884 0.4641 0.0405  0.2237 0.02    607 ASP Z CA    
11516 C  C     . ASP F 607 ? 0.9528 0.6964 0.472  0.0352  0.2199 0.0181  607 ASP Z C     
11517 O  O     . ASP F 607 ? 0.9536 0.7012 0.4705 0.0279  0.2146 0.0182  607 ASP Z O     
11518 C  CB    . ASP F 607 ? 0.9494 0.7198 0.4791 0.0415  0.2216 0.0246  607 ASP Z CB    
11519 C  CG    . ASP F 607 ? 1.0034 0.7759 0.527  0.0446  0.2213 0.0265  607 ASP Z CG    
11520 O  OD1   . ASP F 607 ? 1.014  0.7804 0.5367 0.0518  0.2263 0.0262  607 ASP Z OD1   
11521 O  OD2   . ASP F 607 ? 1.0284 0.8082 0.5477 0.0396  0.2159 0.0281  607 ASP Z OD2   
11522 N  N     . TYR F 608 ? 0.9635 0.6952 0.4772 0.0388  0.2227 0.0166  608 TYR Z N     
11523 C  CA    . TYR F 608 ? 0.9799 0.7014 0.484  0.0344  0.2197 0.0148  608 TYR Z CA    
11524 C  C     . TYR F 608 ? 0.9901 0.7186 0.4875 0.0342  0.2165 0.0173  608 TYR Z C     
11525 O  O     . TYR F 608 ? 0.9975 0.7174 0.4882 0.0373  0.2182 0.0167  608 TYR Z O     
11526 C  CB    . TYR F 608 ? 0.9866 0.6905 0.4879 0.0381  0.2243 0.0119  608 TYR Z CB    
11527 C  CG    . TYR F 608 ? 0.9963 0.6935 0.5038 0.0375  0.2268 0.0096  608 TYR Z CG    
11528 C  CD1   . TYR F 608 ? 1.0111 0.7025 0.5166 0.0309  0.2237 0.0075  608 TYR Z CD1   
11529 C  CD2   . TYR F 608 ? 1.0062 0.7027 0.5211 0.0434  0.2321 0.0095  608 TYR Z CD2   
11530 C  CE1   . TYR F 608 ? 1.0237 0.7093 0.5348 0.0304  0.2258 0.0056  608 TYR Z CE1   
11531 C  CE2   . TYR F 608 ? 1.0185 0.7093 0.539  0.0425  0.234  0.0076  608 TYR Z CE2   
11532 C  CZ    . TYR F 608 ? 1.0323 0.718  0.5512 0.0361  0.2308 0.0057  608 TYR Z CZ    
11533 O  OH    . TYR F 608 ? 1.0502 0.7308 0.5747 0.0353  0.2325 0.004   608 TYR Z OH    
11534 N  N     . ASP F 609 ? 0.9888 0.7333 0.4882 0.0303  0.2119 0.0202  609 ASP Z N     
11535 C  CA    . ASP F 609 ? 0.9968 0.7521 0.4914 0.029   0.2079 0.0234  609 ASP Z CA    
11536 C  C     . ASP F 609 ? 1.0037 0.7612 0.4974 0.0374  0.2118 0.0254  609 ASP Z C     
11537 O  O     . ASP F 609 ? 1.01   0.7674 0.4961 0.0371  0.2095 0.0264  609 ASP Z O     
11538 C  CB    . ASP F 609 ? 1.0231 0.7713 0.5068 0.0211  0.2024 0.0219  609 ASP Z CB    
11539 C  CG    . ASP F 609 ? 1.0712 0.8337 0.5549 0.0131  0.1956 0.0243  609 ASP Z CG    
11540 O  OD1   . ASP F 609 ? 1.0754 0.8391 0.5628 0.0077  0.1938 0.0233  609 ASP Z OD1   
11541 O  OD2   . ASP F 609 ? 1.096  0.8687 0.576  0.012   0.1921 0.0274  609 ASP Z OD2   
11542 N  N     . ASN F 610 ? 1.0004 0.7597 0.5015 0.045   0.2176 0.0261  610 ASN Z N     
11543 C  CA    . ASN F 610 ? 1.0069 0.7686 0.5075 0.0535  0.2218 0.0282  610 ASN Z CA    
11544 C  C     . ASN F 610 ? 1.0052 0.7866 0.511  0.0564  0.2212 0.0331  610 ASN Z C     
11545 O  O     . ASN F 610 ? 1.0092 0.7938 0.5146 0.0638  0.2248 0.0354  610 ASN Z O     
11546 C  CB    . ASN F 610 ? 1.021  0.7716 0.5251 0.0606  0.2291 0.0262  610 ASN Z CB    
11547 C  CG    . ASN F 610 ? 1.0629 0.795  0.5638 0.059   0.2308 0.0218  610 ASN Z CG    
11548 O  OD1   . ASN F 610 ? 1.0765 0.802  0.5827 0.0615  0.235  0.0201  610 ASN Z OD1   
11549 N  ND2   . ASN F 610 ? 1.0744 0.7975 0.5665 0.0552  0.2279 0.0202  610 ASN Z ND2   
11550 N  N     . LEU F 611 ? 0.9975 0.7917 0.5079 0.0511  0.2171 0.0351  611 LEU Z N     
11551 C  CA    . LEU F 611 ? 0.9946 0.8082 0.5104 0.054   0.2167 0.0402  611 LEU Z CA    
11552 C  C     . LEU F 611 ? 0.9952 0.8221 0.5071 0.049   0.2101 0.0436  611 LEU Z C     
11553 O  O     . LEU F 611 ? 0.9967 0.8244 0.5061 0.0401  0.2043 0.0427  611 LEU Z O     
11554 C  CB    . LEU F 611 ? 0.9921 0.8131 0.5166 0.0527  0.2174 0.041   611 LEU Z CB    
11555 C  CG    . LEU F 611 ? 1.0124 0.8227 0.5415 0.0579  0.2239 0.0384  611 LEU Z CG    
11556 C  CD1   . LEU F 611 ? 1.0139 0.8302 0.5502 0.055   0.2234 0.0387  611 LEU Z CD1   
11557 C  CD2   . LEU F 611 ? 1.0208 0.8325 0.551  0.068   0.2302 0.0406  611 LEU Z CD2   
11558 N  N     . THR F 612 ? 0.9926 0.8299 0.5039 0.0547  0.2112 0.0477  612 THR Z N     
11559 C  CA    . THR F 612 ? 0.9953 0.8476 0.5036 0.0509  0.2052 0.0518  612 THR Z CA    
11560 C  C     . THR F 612 ? 0.9901 0.8637 0.5071 0.0504  0.2036 0.057   612 THR Z C     
11561 O  O     . THR F 612 ? 0.9877 0.8626 0.5119 0.0541  0.2079 0.0571  612 THR Z O     
11562 C  CB    . THR F 612 ? 1.0124 0.865  0.5156 0.0581  0.2075 0.0538  612 THR Z CB    
11563 O  OG1   . THR F 612 ? 1.0199 0.8805 0.5293 0.0678  0.2135 0.0571  612 THR Z OG1   
11564 C  CG2   . THR F 612 ? 1.027  0.8582 0.5222 0.0597  0.2101 0.0489  612 THR Z CG2   
11565 N  N     . GLU F 613 ? 0.9865 0.8769 0.5029 0.046   0.1976 0.0614  613 GLU Z N     
11566 C  CA    . GLU F 613 ? 0.9841 0.8961 0.5088 0.0456  0.196  0.067   613 GLU Z CA    
11567 C  C     . GLU F 613 ? 0.9832 0.9026 0.5139 0.0572  0.2032 0.0707  613 GLU Z C     
11568 O  O     . GLU F 613 ? 0.9786 0.9067 0.5171 0.0592  0.2055 0.073   613 GLU Z O     
11569 C  CB    . GLU F 613 ? 1.008  0.9365 0.53   0.0396  0.1886 0.0715  613 GLU Z CB    
11570 C  CG    . GLU F 613 ? 1.0521 1.0052 0.5827 0.0399  0.1869 0.0783  613 GLU Z CG    
11571 C  CD    . GLU F 613 ? 1.1194 1.0899 0.6476 0.0349  0.1799 0.0834  613 GLU Z CD    
11572 O  OE1   . GLU F 613 ? 1.1222 1.1138 0.6569 0.0385  0.18   0.0901  613 GLU Z OE1   
11573 O  OE2   . GLU F 613 ? 1.1521 1.1149 0.6715 0.0274  0.1745 0.0808  613 GLU Z OE2   
11574 N  N     . ASN F 614 ? 0.9863 0.901  0.5127 0.065   0.2071 0.0711  614 ASN Z N     
11575 C  CA    . ASN F 614 ? 0.9889 0.9083 0.5191 0.0765  0.2144 0.0744  614 ASN Z CA    
11576 C  C     . ASN F 614 ? 0.9904 0.8954 0.5237 0.0811  0.2213 0.0705  614 ASN Z C     
11577 O  O     . ASN F 614 ? 0.9857 0.8968 0.5241 0.088   0.2265 0.0735  614 ASN Z O     
11578 C  CB    . ASN F 614 ? 1.0109 0.9279 0.5347 0.0829  0.2164 0.0756  614 ASN Z CB    
11579 C  CG    . ASN F 614 ? 1.0497 0.9857 0.5722 0.0811  0.2109 0.0813  614 ASN Z CG    
11580 O  OD1   . ASN F 614 ? 1.0549 1.01   0.5833 0.0784  0.2076 0.0862  614 ASN Z OD1   
11581 N  ND2   . ASN F 614 ? 1.0661 0.9974 0.5808 0.0825  0.2097 0.0809  614 ASN Z ND2   
11582 N  N     . ASP F 615 ? 0.9956 0.8811 0.5253 0.0772  0.2214 0.0642  615 ASP Z N     
11583 C  CA    . ASP F 615 ? 1.0035 0.8749 0.536  0.0804  0.2273 0.0603  615 ASP Z CA    
11584 C  C     . ASP F 615 ? 0.997  0.8764 0.5369 0.0771  0.2264 0.0613  615 ASP Z C     
11585 O  O     . ASP F 615 ? 0.9978 0.8764 0.542  0.0829  0.232  0.062   615 ASP Z O     
11586 C  CB    . ASP F 615 ? 1.0369 0.8878 0.5644 0.076   0.2267 0.0537  615 ASP Z CB    
11587 C  CG    . ASP F 615 ? 1.1095 0.9475 0.6304 0.0815  0.2304 0.0518  615 ASP Z CG    
11588 O  OD1   . ASP F 615 ? 1.1212 0.9638 0.6419 0.0899  0.2347 0.0548  615 ASP Z OD1   
11589 O  OD2   . ASP F 615 ? 1.1462 0.9692 0.662  0.0777  0.2291 0.0473  615 ASP Z OD2   
11590 N  N     . TYR F 616 ? 0.9887 0.8761 0.5297 0.0678  0.2194 0.0618  616 TYR Z N     
11591 C  CA    . TYR F 616 ? 0.9841 0.8802 0.532  0.064   0.2181 0.0631  616 TYR Z CA    
11592 C  C     . TYR F 616 ? 0.9757 0.8898 0.5292 0.0706  0.2209 0.0696  616 TYR Z C     
11593 O  O     . TYR F 616 ? 0.974  0.889  0.5327 0.0737  0.2247 0.0703  616 TYR Z O     
11594 C  CB    . TYR F 616 ? 0.9824 0.8845 0.5294 0.0527  0.2098 0.0628  616 TYR Z CB    
11595 C  CG    . TYR F 616 ? 0.9981 0.8821 0.5414 0.046   0.208  0.0563  616 TYR Z CG    
11596 C  CD1   . TYR F 616 ? 1.0101 0.8847 0.5572 0.0456  0.2108 0.053   616 TYR Z CD1   
11597 C  CD2   . TYR F 616 ? 1.0141 0.89   0.5495 0.0402  0.2035 0.0537  616 TYR Z CD2   
11598 C  CE1   . TYR F 616 ? 1.0272 0.8856 0.571  0.0399  0.2093 0.0474  616 TYR Z CE1   
11599 C  CE2   . TYR F 616 ? 1.0313 0.8902 0.5627 0.0346  0.2023 0.048   616 TYR Z CE2   
11600 C  CZ    . TYR F 616 ? 1.0431 0.8937 0.5791 0.0346  0.2052 0.045   616 TYR Z CZ    
11601 O  OH    . TYR F 616 ? 1.0673 0.9017 0.5995 0.0294  0.2042 0.0399  616 TYR Z OH    
11602 N  N     . GLU F 617 ? 0.97   0.8976 0.5221 0.0735  0.2194 0.0746  617 GLU Z N     
11603 C  CA    . GLU F 617 ? 0.9679 0.9132 0.5247 0.0807  0.2224 0.0815  617 GLU Z CA    
11604 C  C     . GLU F 617 ? 0.9705 0.9072 0.5279 0.0915  0.2315 0.0812  617 GLU Z C     
11605 O  O     . GLU F 617 ? 0.9663 0.9114 0.5287 0.0961  0.2352 0.0849  617 GLU Z O     
11606 C  CB    . GLU F 617 ? 0.9968 0.9564 0.5509 0.0819  0.2191 0.0864  617 GLU Z CB    
11607 C  CG    . GLU F 617 ? 1.0519 1.032  0.6095 0.0743  0.2116 0.0912  617 GLU Z CG    
11608 C  CD    . GLU F 617 ? 1.1208 1.124  0.6834 0.0803  0.2127 0.0997  617 GLU Z CD    
11609 O  OE1   . GLU F 617 ? 1.1363 1.1463 0.6955 0.0842  0.2122 0.1029  617 GLU Z OE1   
11610 O  OE2   . GLU F 617 ? 1.1375 1.1522 0.7071 0.0811  0.2139 0.1033  617 GLU Z OE2   
11611 N  N     . LYS F 618 ? 0.9758 0.8948 0.5278 0.0952  0.2353 0.0768  618 LYS Z N     
11612 C  CA    . LYS F 618 ? 0.9818 0.8904 0.5333 0.1046  0.2439 0.076   618 LYS Z CA    
11613 C  C     . LYS F 618 ? 0.9834 0.8822 0.5384 0.1029  0.2465 0.0726  618 LYS Z C     
11614 O  O     . LYS F 618 ? 0.9845 0.8836 0.5416 0.1095  0.2524 0.0745  618 LYS Z O     
11615 C  CB    . LYS F 618 ? 1.0124 0.9048 0.5571 0.1083  0.2469 0.0722  618 LYS Z CB    
11616 C  CG    . LYS F 618 ? 1.0657 0.945  0.6091 0.1171  0.2556 0.0706  618 LYS Z CG    
11617 C  CD    . LYS F 618 ? 1.1146 1.0044 0.6586 0.1272  0.2613 0.0766  618 LYS Z CD    
11618 C  CE    . LYS F 618 ? 1.1644 1.0395 0.7062 0.135   0.2699 0.0747  618 LYS Z CE    
11619 N  NZ    . LYS F 618 ? 1.1869 1.0718 0.7293 0.1444  0.2757 0.0806  618 LYS Z NZ    
11620 N  N     . ILE F 619 ? 0.9818 0.8726 0.5373 0.0939  0.2419 0.0678  619 ILE Z N     
11621 C  CA    . ILE F 619 ? 0.9841 0.8664 0.5431 0.0915  0.2436 0.0646  619 ILE Z CA    
11622 C  C     . ILE F 619 ? 0.9762 0.8743 0.5412 0.0916  0.2432 0.0694  619 ILE Z C     
11623 O  O     . ILE F 619 ? 0.9777 0.8721 0.545  0.0958  0.2483 0.0695  619 ILE Z O     
11624 C  CB    . ILE F 619 ? 0.9942 0.865  0.5521 0.082   0.2387 0.0588  619 ILE Z CB    
11625 C  CG1   . ILE F 619 ? 1.0128 0.8676 0.5646 0.0826  0.2396 0.0544  619 ILE Z CG1   
11626 C  CG2   . ILE F 619 ? 1.0007 0.8635 0.5623 0.0798  0.2404 0.0558  619 ILE Z CG2   
11627 C  CD1   . ILE F 619 ? 1.0307 0.8753 0.5801 0.0737  0.2346 0.0495  619 ILE Z CD1   
11628 N  N     . PHE F 620 ? 0.9667 0.8825 0.534  0.0874  0.2376 0.0736  620 PHE Z N     
11629 C  CA    . PHE F 620 ? 0.9624 0.8952 0.5358 0.0875  0.2371 0.079   620 PHE Z CA    
11630 C  C     . PHE F 620 ? 0.9583 0.8975 0.5326 0.0987  0.2443 0.0841  620 PHE Z C     
11631 O  O     . PHE F 620 ? 0.9561 0.8999 0.5343 0.1014  0.2473 0.0865  620 PHE Z O     
11632 C  CB    . PHE F 620 ? 0.9562 0.9077 0.5314 0.0811  0.2296 0.0831  620 PHE Z CB    
11633 C  CG    . PHE F 620 ? 0.967  0.9159 0.5423 0.0693  0.2223 0.0794  620 PHE Z CG    
11634 C  CD1   . PHE F 620 ? 0.9787 0.922  0.5573 0.0648  0.222  0.0766  620 PHE Z CD1   
11635 C  CD2   . PHE F 620 ? 0.9763 0.9291 0.548  0.0627  0.2158 0.0792  620 PHE Z CD2   
11636 C  CE1   . PHE F 620 ? 0.9878 0.9287 0.566  0.0542  0.2155 0.0734  620 PHE Z CE1   
11637 C  CE2   . PHE F 620 ? 0.9865 0.936  0.5572 0.0518  0.2093 0.0759  620 PHE Z CE2   
11638 C  CZ    . PHE F 620 ? 0.9855 0.9292 0.5596 0.0478  0.2094 0.0731  620 PHE Z CZ    
11639 N  N     . GLU F 621 ? 0.9558 0.8948 0.5259 0.1055  0.2471 0.0858  621 GLU Z N     
11640 C  CA    . GLU F 621 ? 0.9568 0.9008 0.5265 0.1167  0.2543 0.0907  621 GLU Z CA    
11641 C  C     . GLU F 621 ? 0.9599 0.8861 0.5276 0.122   0.2618 0.0871  621 GLU Z C     
11642 O  O     . GLU F 621 ? 0.9635 0.8935 0.5327 0.1281  0.267  0.0907  621 GLU Z O     
11643 C  CB    . GLU F 621 ? 0.9899 0.9368 0.5551 0.122   0.2552 0.0928  621 GLU Z CB    
11644 C  CG    . GLU F 621 ? 1.0548 1.0151 0.6206 0.1324  0.2605 0.1002  621 GLU Z CG    
11645 C  CD    . GLU F 621 ? 1.1444 1.1085 0.7057 0.1378  0.2612 0.1027  621 GLU Z CD    
11646 O  OE1   . GLU F 621 ? 1.1595 1.1165 0.7171 0.133   0.2571 0.0988  621 GLU Z OE1   
11647 O  OE2   . GLU F 621 ? 1.1742 1.1482 0.7353 0.1471  0.2661 0.1088  621 GLU Z OE2   
11648 N  N     . VAL F 622 ? 0.9564 0.8634 0.5206 0.1193  0.2622 0.0803  622 VAL Z N     
11649 C  CA    . VAL F 622 ? 0.9608 0.8502 0.5229 0.1231  0.2686 0.0765  622 VAL Z CA    
11650 C  C     . VAL F 622 ? 0.9577 0.8456 0.5239 0.1194  0.2685 0.0755  622 VAL Z C     
11651 O  O     . VAL F 622 ? 0.9589 0.8441 0.5248 0.1254  0.2745 0.0772  622 VAL Z O     
11652 C  CB    . VAL F 622 ? 0.9767 0.8473 0.5346 0.1206  0.2685 0.0699  622 VAL Z CB    
11653 C  CG1   . VAL F 622 ? 0.9902 0.8429 0.547  0.1219  0.2736 0.0655  622 VAL Z CG1   
11654 C  CG2   . VAL F 622 ? 0.9857 0.855  0.5387 0.1265  0.2708 0.071   622 VAL Z CG2   
11655 N  N     . THR F 623 ? 0.9509 0.8401 0.5204 0.1098  0.2619 0.0727  623 THR Z N     
11656 C  CA    . THR F 623 ? 0.9498 0.8362 0.5229 0.1052  0.2611 0.0709  623 THR Z CA    
11657 C  C     . THR F 623 ? 0.9396 0.8435 0.5177 0.105   0.2598 0.0765  623 THR Z C     
11658 O  O     . THR F 623 ? 0.9424 0.8434 0.5222 0.1059  0.2626 0.0766  623 THR Z O     
11659 C  CB    . THR F 623 ? 0.9655 0.8441 0.5393 0.0951  0.2549 0.0653  623 THR Z CB    
11660 O  OG1   . THR F 623 ? 0.9714 0.8638 0.5469 0.0891  0.248  0.0675  623 THR Z OG1   
11661 C  CG2   . THR F 623 ? 0.9773 0.8381 0.5466 0.0951  0.2563 0.0598  623 THR Z CG2   
11662 N  N     . GLY F 624 ? 0.9263 0.8478 0.5068 0.103   0.2553 0.081   624 GLY Z N     
11663 C  CA    . GLY F 624 ? 0.9182 0.858  0.5042 0.1017  0.2532 0.0866  624 GLY Z CA    
11664 C  C     . GLY F 624 ? 0.9128 0.8537 0.5025 0.0911  0.2468 0.0838  624 GLY Z C     
11665 O  O     . GLY F 624 ? 0.9118 0.8646 0.5063 0.0894  0.2456 0.0874  624 GLY Z O     
11666 N  N     . CYS F 625 ? 0.9078 0.8359 0.495  0.084   0.2428 0.0775  625 CYS Z N     
11667 C  CA    . CYS F 625 ? 0.9047 0.8313 0.4943 0.0738  0.2369 0.0742  625 CYS Z CA    
11668 C  C     . CYS F 625 ? 0.8923 0.8373 0.4848 0.0676  0.2301 0.0782  625 CYS Z C     
11669 O  O     . CYS F 625 ? 0.8919 0.8459 0.4828 0.0687  0.2282 0.0812  625 CYS Z O     
11670 C  CB    . CYS F 625 ? 0.9195 0.8276 0.505  0.069   0.2351 0.067   625 CYS Z CB    
11671 S  SG    . CYS F 625 ? 0.9642 0.8506 0.5478 0.0731  0.2416 0.0616  625 CYS Z SG    
11672 N  N     . ASP F 626 ? 0.8801 0.8307 0.4765 0.0607  0.2263 0.0783  626 ASP Z N     
11673 C  CA    . ASP F 626 ? 0.8706 0.8378 0.4697 0.0532  0.2193 0.0817  626 ASP Z CA    
11674 C  C     . ASP F 626 ? 0.8627 0.8213 0.4575 0.0437  0.2129 0.0766  626 ASP Z C     
11675 O  O     . ASP F 626 ? 0.8587 0.8288 0.4532 0.0378  0.2071 0.079   626 ASP Z O     
11676 C  CB    . ASP F 626 ? 0.891  0.868  0.4961 0.0499  0.2182 0.0843  626 ASP Z CB    
11677 C  CG    . ASP F 626 ? 0.9506 0.9377 0.5595 0.0589  0.2241 0.0903  626 ASP Z CG    
11678 O  OD1   . ASP F 626 ? 0.9538 0.959  0.5652 0.0623  0.224  0.097   626 ASP Z OD1   
11679 O  OD2   . ASP F 626 ? 0.9847 0.9617 0.5939 0.0627  0.2291 0.0883  626 ASP Z OD2   
11680 N  N     . LEU F 627 ? 0.8581 0.7965 0.4492 0.042   0.214  0.0698  627 LEU Z N     
11681 C  CA    . LEU F 627 ? 0.8565 0.7848 0.4428 0.0337  0.2088 0.0649  627 LEU Z CA    
11682 C  C     . LEU F 627 ? 0.8544 0.7622 0.4357 0.037   0.2124 0.0592  627 LEU Z C     
11683 O  O     . LEU F 627 ? 0.8574 0.756  0.44   0.0425  0.2179 0.0575  627 LEU Z O     
11684 C  CB    . LEU F 627 ? 0.86   0.7862 0.4485 0.0252  0.2052 0.0624  627 LEU Z CB    
11685 C  CG    . LEU F 627 ? 0.886  0.8002 0.4692 0.0162  0.2001 0.0571  627 LEU Z CG    
11686 C  CD1   . LEU F 627 ? 0.8914 0.8152 0.4712 0.0105  0.1941 0.0594  627 LEU Z CD1   
11687 C  CD2   . LEU F 627 ? 0.8955 0.8057 0.4809 0.0096  0.198  0.0546  627 LEU Z CD2   
11688 N  N     . LEU F 628 ? 0.8488 0.7493 0.4242 0.0335  0.2094 0.0565  628 LEU Z N     
11689 C  CA    . LEU F 628 ? 0.8549 0.736  0.4256 0.0359  0.2124 0.0512  628 LEU Z CA    
11690 C  C     . LEU F 628 ? 0.8578 0.7278 0.4244 0.0269  0.2076 0.0464  628 LEU Z C     
11691 O  O     . LEU F 628 ? 0.8582 0.7342 0.4217 0.0203  0.2019 0.0474  628 LEU Z O     
11692 C  CB    . LEU F 628 ? 0.8584 0.7387 0.4248 0.0419  0.2145 0.0525  628 LEU Z CB    
11693 C  CG    . LEU F 628 ? 0.8714 0.7596 0.4407 0.0519  0.2203 0.0568  628 LEU Z CG    
11694 C  CD1   . LEU F 628 ? 0.8789 0.768  0.4436 0.057   0.2215 0.0583  628 LEU Z CD1   
11695 C  CD2   . LEU F 628 ? 0.8828 0.759  0.4539 0.0574  0.2268 0.0542  628 LEU Z CD2   
11696 N  N     . ILE F 629 ? 0.8584 0.7128 0.4248 0.0263  0.2098 0.0416  629 ILE Z N     
11697 C  CA    . ILE F 629 ? 0.8667 0.7095 0.429  0.0185  0.2061 0.0371  629 ILE Z CA    
11698 C  C     . ILE F 629 ? 0.8757 0.7012 0.4327 0.0213  0.2088 0.0331  629 ILE Z C     
11699 O  O     . ILE F 629 ? 0.8778 0.6929 0.4367 0.0256  0.2135 0.0306  629 ILE Z O     
11700 C  CB    . ILE F 629 ? 0.872  0.7118 0.4384 0.0145  0.2056 0.0351  629 ILE Z CB    
11701 C  CG1   . ILE F 629 ? 0.8738 0.7313 0.4459 0.0127  0.2036 0.0396  629 ILE Z CG1   
11702 C  CG2   . ILE F 629 ? 0.8841 0.7124 0.4456 0.0063  0.2016 0.0309  629 ILE Z CG2   
11703 C  CD1   . ILE F 629 ? 0.8891 0.7444 0.4655 0.0098  0.2038 0.0382  629 ILE Z CD1   
11704 N  N     . ALA F 630 ? 0.8782 0.7011 0.4285 0.0191  0.206  0.0326  630 ALA Z N     
11705 C  CA    . ALA F 630 ? 0.8906 0.6974 0.4352 0.0217  0.2084 0.0292  630 ALA Z CA    
11706 C  C     . ALA F 630 ? 0.8997 0.6932 0.4397 0.0147  0.2056 0.0249  630 ALA Z C     
11707 O  O     . ALA F 630 ? 0.9016 0.6972 0.437  0.0074  0.2003 0.025   630 ALA Z O     
11708 C  CB    . ALA F 630 ? 0.8942 0.7047 0.4333 0.0238  0.2073 0.0313  630 ALA Z CB    
11709 N  N     . ILE F 631 ? 0.9034 0.6831 0.4445 0.0168  0.2093 0.0214  631 ILE Z N     
11710 C  CA    . ILE F 631 ? 0.9152 0.6814 0.4527 0.0114  0.2078 0.0175  631 ILE Z CA    
11711 C  C     . ILE F 631 ? 0.9276 0.6784 0.459  0.0141  0.2103 0.0148  631 ILE Z C     
11712 O  O     . ILE F 631 ? 0.9316 0.6793 0.4645 0.0212  0.215  0.015   631 ILE Z O     
11713 C  CB    . ILE F 631 ? 0.9192 0.6831 0.4638 0.012   0.2102 0.0161  631 ILE Z CB    
11714 C  CG1   . ILE F 631 ? 0.925  0.7031 0.4746 0.0082  0.2073 0.0185  631 ILE Z CG1   
11715 C  CG2   . ILE F 631 ? 0.9302 0.6789 0.4725 0.0088  0.2104 0.012   631 ILE Z CG2   
11716 C  CD1   . ILE F 631 ? 0.9391 0.7183 0.4962 0.0112  0.2106 0.0184  631 ILE Z CD1   
11717 N  N     . LYS F 632 ? 0.9317 0.6725 0.4555 0.0087  0.2074 0.0125  632 LYS Z N     
11718 C  CA    . LYS F 632 ? 0.9451 0.6706 0.4626 0.0113  0.2099 0.0102  632 LYS Z CA    
11719 C  C     . LYS F 632 ? 0.955  0.6673 0.4675 0.0059  0.2084 0.0071  632 LYS Z C     
11720 O  O     . LYS F 632 ? 0.9566 0.6714 0.4658 -0.0013 0.2037 0.007   632 LYS Z O     
11721 C  CB    . LYS F 632 ? 0.971  0.6979 0.481  0.0123  0.2085 0.0117  632 LYS Z CB    
11722 C  CG    . LYS F 632 ? 1.0237 0.7554 0.5268 0.0043  0.202  0.0126  632 LYS Z CG    
11723 C  CD    . LYS F 632 ? 1.076  0.8148 0.574  0.0056  0.2001 0.0152  632 LYS Z CD    
11724 C  CE    . LYS F 632 ? 1.1132 0.8709 0.6189 0.0088  0.2001 0.0193  632 LYS Z CE    
11725 N  NZ    . LYS F 632 ? 1.1351 0.9046 0.647  0.0036  0.1969 0.0206  632 LYS Z NZ    
11726 N  N     . ASN F 633 ? 0.9593 0.6578 0.4715 0.0093  0.2125 0.0047  633 ASN Z N     
11727 C  CA    . ASN F 633 ? 0.9713 0.6566 0.4786 0.005   0.2117 0.002   633 ASN Z CA    
11728 C  C     . ASN F 633 ? 0.9855 0.6599 0.4812 0.0038  0.2108 0.0012  633 ASN Z C     
11729 O  O     . ASN F 633 ? 0.99   0.6615 0.483  0.0088  0.2132 0.0017  633 ASN Z O     
11730 C  CB    . ASN F 633 ? 0.9815 0.658  0.4945 0.0087  0.2164 0.0002  633 ASN Z CB    
11731 C  CG    . ASN F 633 ? 1.0095 0.6807 0.5239 0.0163  0.2216 0.0003  633 ASN Z CG    
11732 O  OD1   . ASN F 633 ? 1.0142 0.6936 0.5339 0.021   0.2237 0.0019  633 ASN Z OD1   
11733 N  ND2   . ASN F 633 ? 1.0209 0.6779 0.5302 0.0178  0.2239 -0.0013 633 ASN Z ND2   
11734 N  N     . GLN F 634 ? 0.9907 0.6584 0.479  -0.003  0.2073 -0.0002 634 GLN Z N     
11735 C  CA    . GLN F 634 ? 1.0048 0.6594 0.4803 -0.0053 0.2062 -0.0013 634 GLN Z CA    
11736 C  C     . GLN F 634 ? 1.0158 0.6554 0.4901 -0.0049 0.2092 -0.0037 634 GLN Z C     
11737 O  O     . GLN F 634 ? 1.0166 0.6571 0.4946 -0.0085 0.2082 -0.0045 634 GLN Z O     
11738 C  CB    . GLN F 634 ? 1.0239 0.6827 0.4918 -0.014  0.1999 -0.0009 634 GLN Z CB    
11739 C  CG    . GLN F 634 ? 1.0741 0.7183 0.5271 -0.0176 0.1983 -0.0022 634 GLN Z CG    
11740 C  CD    . GLN F 634 ? 1.1289 0.7785 0.5749 -0.0266 0.1918 -0.0015 634 GLN Z CD    
11741 O  OE1   . GLN F 634 ? 1.1431 0.804  0.588  -0.0283 0.1884 0.0007  634 GLN Z OE1   
11742 N  NE2   . GLN F 634 ? 1.1432 0.7852 0.5844 -0.0328 0.1899 -0.0032 634 GLN Z NE2   
11743 N  N     . ASN F 635 ? 1.0235 0.6501 0.4933 -0.0001 0.2133 -0.0045 635 ASN Z N     
11744 C  CA    . ASN F 635 ? 1.0372 0.6502 0.5066 0.0012  0.2167 -0.0062 635 ASN Z CA    
11745 C  C     . ASN F 635 ? 1.0537 0.6533 0.5104 -0.0041 0.2147 -0.0076 635 ASN Z C     
11746 O  O     . ASN F 635 ? 1.0579 0.6493 0.5146 -0.0052 0.2161 -0.0088 635 ASN Z O     
11747 C  CB    . ASN F 635 ? 1.0518 0.6574 0.5235 0.0092  0.2226 -0.0061 635 ASN Z CB    
11748 C  CG    . ASN F 635 ? 1.0791 0.6957 0.5633 0.0144  0.2252 -0.0051 635 ASN Z CG    
11749 O  OD1   . ASN F 635 ? 1.0892 0.7156 0.5823 0.0129  0.2242 -0.0049 635 ASN Z OD1   
11750 N  ND2   . ASN F 635 ? 1.0833 0.6979 0.5679 0.0207  0.2289 -0.0044 635 ASN Z ND2   
11751 N  N     . ASN F 636 ? 1.0607 0.6572 0.5057 -0.0074 0.2117 -0.0073 636 ASN Z N     
11752 C  CA    . ASN F 636 ? 1.0767 0.6584 0.5074 -0.0124 0.21   -0.0087 636 ASN Z CA    
11753 C  C     . ASN F 636 ? 1.0815 0.6683 0.5037 -0.0209 0.2035 -0.0084 636 ASN Z C     
11754 O  O     . ASN F 636 ? 1.0855 0.6725 0.5    -0.0216 0.2015 -0.0076 636 ASN Z O     
11755 C  CB    . ASN F 636 ? 1.0987 0.6652 0.5196 -0.0078 0.2136 -0.0089 636 ASN Z CB    
11756 C  CG    . ASN F 636 ? 1.1322 0.6953 0.5612 0.001   0.22   -0.0086 636 ASN Z CG    
11757 O  OD1   . ASN F 636 ? 1.1494 0.7036 0.5805 0.0032  0.2236 -0.0093 636 ASN Z OD1   
11758 N  ND2   . ASN F 636 ? 1.1325 0.7027 0.5663 0.0062  0.2216 -0.0075 636 ASN Z ND2   
11759 N  N     . PRO F 637 ? 1.0819 0.6713 0.5041 -0.0277 0.2001 -0.009  637 PRO Z N     
11760 C  CA    . PRO F 637 ? 1.0828 0.6729 0.5135 -0.0279 0.2016 -0.0098 637 PRO Z CA    
11761 C  C     . PRO F 637 ? 1.0771 0.6854 0.524  -0.0256 0.2016 -0.0086 637 PRO Z C     
11762 O  O     . PRO F 637 ? 1.0751 0.6969 0.5253 -0.0261 0.199  -0.0069 637 PRO Z O     
11763 C  CB    . PRO F 637 ? 1.0951 0.6811 0.5166 -0.037  0.1971 -0.0108 637 PRO Z CB    
11764 C  CG    . PRO F 637 ? 1.0977 0.6931 0.5138 -0.0423 0.1917 -0.0095 637 PRO Z CG    
11765 C  CD    . PRO F 637 ? 1.0782 0.6721 0.4918 -0.0365 0.1937 -0.0086 637 PRO Z CD    
11766 N  N     . GLN F 638 ? 1.0724 0.6809 0.529  -0.0228 0.2046 -0.0092 638 GLN Z N     
11767 C  CA    . GLN F 638 ? 1.0674 0.6912 0.5383 -0.0202 0.2051 -0.0081 638 GLN Z CA    
11768 C  C     . GLN F 638 ? 1.053  0.692  0.5268 -0.026  0.1999 -0.0069 638 GLN Z C     
11769 O  O     . GLN F 638 ? 1.0555 0.6937 0.5262 -0.0325 0.1968 -0.0076 638 GLN Z O     
11770 C  CB    . GLN F 638 ? 1.0953 0.7157 0.5747 -0.0173 0.2086 -0.009  638 GLN Z CB    
11771 C  CG    . GLN F 638 ? 1.1518 0.7649 0.6345 -0.0096 0.2142 -0.0091 638 GLN Z CG    
11772 C  CD    . GLN F 638 ? 1.2185 0.8286 0.7093 -0.0073 0.2173 -0.0098 638 GLN Z CD    
11773 O  OE1   . GLN F 638 ? 1.2481 0.8488 0.7349 -0.0098 0.2174 -0.0109 638 GLN Z OE1   
11774 N  NE2   . GLN F 638 ? 1.2198 0.8375 0.7218 -0.0026 0.2198 -0.0091 638 GLN Z NE2   
11775 N  N     . LYS F 639 ? 1.0353 0.6881 0.5147 -0.0236 0.1993 -0.0048 639 LYS Z N     
11776 C  CA    . LYS F 639 ? 1.0238 0.693  0.507  -0.028  0.1948 -0.0029 639 LYS Z CA    
11777 C  C     . LYS F 639 ? 1.0105 0.6937 0.5039 -0.022  0.1967 -0.0006 639 LYS Z C     
11778 O  O     . LYS F 639 ? 1.0134 0.6941 0.507  -0.0158 0.2    -0.0002 639 LYS Z O     
11779 C  CB    . LYS F 639 ? 1.0468 0.7167 0.5189 -0.0339 0.19   -0.0021 639 LYS Z CB    
11780 C  CG    . LYS F 639 ? 1.099  0.7637 0.5632 -0.0429 0.1859 -0.0033 639 LYS Z CG    
11781 C  CD    . LYS F 639 ? 1.1563 0.8198 0.6082 -0.0487 0.1813 -0.0026 639 LYS Z CD    
11782 C  CE    . LYS F 639 ? 1.1937 0.8715 0.6467 -0.0565 0.1755 -0.0007 639 LYS Z CE    
11783 N  NZ    . LYS F 639 ? 1.2242 0.8937 0.6704 -0.0644 0.173  -0.0025 639 LYS Z NZ    
11784 N  N     . TRP F 640 ? 0.9931 0.6909 0.4945 -0.0238 0.1948 0.0011  640 TRP Z N     
11785 C  CA    . TRP F 640 ? 0.981  0.6926 0.4911 -0.0184 0.1965 0.0037  640 TRP Z CA    
11786 C  C     . TRP F 640 ? 0.9731 0.6976 0.4803 -0.0219 0.192  0.0065  640 TRP Z C     
11787 O  O     . TRP F 640 ? 0.9707 0.7023 0.4772 -0.0287 0.1876 0.0073  640 TRP Z O     
11788 C  CB    . TRP F 640 ? 0.9713 0.691  0.4921 -0.0174 0.1977 0.0041  640 TRP Z CB    
11789 C  CG    . TRP F 640 ? 0.9754 0.6863 0.5015 -0.0121 0.2027 0.0022  640 TRP Z CG    
11790 C  CD1   . TRP F 640 ? 0.9873 0.6915 0.5159 -0.014  0.2034 0.0002  640 TRP Z CD1   
11791 C  CD2   . TRP F 640 ? 0.9748 0.6838 0.5048 -0.0042 0.2076 0.0025  640 TRP Z CD2   
11792 N  NE1   . TRP F 640 ? 0.9909 0.6894 0.5247 -0.008  0.2082 -0.0007 640 TRP Z NE1   
11793 C  CE2   . TRP F 640 ? 0.9857 0.6866 0.5204 -0.0021 0.2109 0.0006  640 TRP Z CE2   
11794 C  CE3   . TRP F 640 ? 0.9789 0.6916 0.5085 0.0012  0.2096 0.0042  640 TRP Z CE3   
11795 C  CZ2   . TRP F 640 ? 0.9918 0.6887 0.5308 0.0047  0.2159 0.0003  640 TRP Z CZ2   
11796 C  CZ3   . TRP F 640 ? 0.9878 0.6961 0.5215 0.0083  0.2148 0.0038  640 TRP Z CZ3   
11797 C  CH2   . TRP F 640 ? 0.9905 0.6908 0.5287 0.0097  0.2178 0.0019  640 TRP Z CH2   
11798 N  N     . VAL F 641 ? 0.9684 0.6958 0.4736 -0.0175 0.193  0.0081  641 VAL Z N     
11799 C  CA    . VAL F 641 ? 0.9677 0.708  0.4703 -0.0203 0.1888 0.0112  641 VAL Z CA    
11800 C  C     . VAL F 641 ? 0.9625 0.7202 0.4756 -0.0157 0.1901 0.0146  641 VAL Z C     
11801 O  O     . VAL F 641 ? 0.9615 0.719  0.4795 -0.0078 0.195  0.015   641 VAL Z O     
11802 C  CB    . VAL F 641 ? 0.9802 0.7137 0.4736 -0.0183 0.1889 0.0111  641 VAL Z CB    
11803 C  CG1   . VAL F 641 ? 0.9832 0.7304 0.4734 -0.0219 0.1839 0.0145  641 VAL Z CG1   
11804 C  CG2   . VAL F 641 ? 0.9959 0.7102 0.4785 -0.0218 0.1885 0.0077  641 VAL Z CG2   
11805 N  N     . ILE F 642 ? 0.9569 0.7291 0.4733 -0.0206 0.1861 0.0172  642 ILE Z N     
11806 C  CA    . ILE F 642 ? 0.9527 0.7418 0.4789 -0.0165 0.1874 0.0209  642 ILE Z CA    
11807 C  C     . ILE F 642 ? 0.9521 0.7567 0.4771 -0.0172 0.1841 0.0252  642 ILE Z C     
11808 O  O     . ILE F 642 ? 0.9549 0.764  0.475  -0.0249 0.1786 0.0262  642 ILE Z O     
11809 C  CB    . ILE F 642 ? 0.9532 0.7486 0.486  -0.0204 0.1862 0.0212  642 ILE Z CB    
11810 C  CG1   . ILE F 642 ? 0.9698 0.7496 0.502  -0.022  0.188  0.0168  642 ILE Z CG1   
11811 C  CG2   . ILE F 642 ? 0.9513 0.7606 0.4941 -0.0144 0.1892 0.0246  642 ILE Z CG2   
11812 C  CD1   . ILE F 642 ? 0.988  0.7584 0.5241 -0.0142 0.194  0.0149  642 ILE Z CD1   
11813 N  N     . LYS F 643 ? 0.9468 0.7599 0.4765 -0.0094 0.1875 0.0281  643 LYS Z N     
11814 C  CA    . LYS F 643 ? 0.9496 0.7788 0.4792 -0.009  0.1849 0.0328  643 LYS Z CA    
11815 C  C     . LYS F 643 ? 0.947  0.793  0.487  -0.0044 0.187  0.037   643 LYS Z C     
11816 O  O     . LYS F 643 ? 0.9487 0.7927 0.4934 0.0037  0.1928 0.037   643 LYS Z O     
11817 C  CB    . LYS F 643 ? 0.9785 0.8025 0.5028 -0.0032 0.1871 0.0328  643 LYS Z CB    
11818 C  CG    . LYS F 643 ? 1.0299 0.8696 0.5526 -0.0035 0.1837 0.0375  643 LYS Z CG    
11819 C  CD    . LYS F 643 ? 1.0937 0.9273 0.6108 0.0026  0.1861 0.0375  643 LYS Z CD    
11820 C  CE    . LYS F 643 ? 1.1388 0.9866 0.6528 0.0011  0.1819 0.0418  643 LYS Z CE    
11821 N  NZ    . LYS F 643 ? 1.1697 1.0099 0.677  0.0065  0.184  0.0413  643 LYS Z NZ    
11822 N  N     . PHE F 644 ? 0.9406 0.8026 0.4838 -0.0097 0.1826 0.0406  644 PHE Z N     
11823 C  CA    . PHE F 644 ? 0.9369 0.8155 0.4895 -0.0056 0.1846 0.0451  644 PHE Z CA    
11824 C  C     . PHE F 644 ? 0.9319 0.8269 0.4855 -0.0019 0.1839 0.0506  644 PHE Z C     
11825 O  O     . PHE F 644 ? 0.9323 0.8357 0.4822 -0.0079 0.1783 0.0528  644 PHE Z O     
11826 C  CB    . PHE F 644 ? 0.9342 0.8218 0.4906 -0.0133 0.1805 0.0464  644 PHE Z CB    
11827 C  CG    . PHE F 644 ? 0.95   0.8242 0.5068 -0.0167 0.1813 0.0417  644 PHE Z CG    
11828 C  CD1   . PHE F 644 ? 0.9595 0.8324 0.5231 -0.0116 0.186  0.0413  644 PHE Z CD1   
11829 C  CD2   . PHE F 644 ? 0.9674 0.8302 0.5172 -0.025  0.1773 0.0379  644 PHE Z CD2   
11830 C  CE1   . PHE F 644 ? 0.9728 0.8341 0.5369 -0.0148 0.1865 0.0372  644 PHE Z CE1   
11831 C  CE2   . PHE F 644 ? 0.9809 0.832  0.5311 -0.0278 0.1782 0.0339  644 PHE Z CE2   
11832 C  CZ    . PHE F 644 ? 0.9762 0.827  0.5339 -0.0227 0.1827 0.0336  644 PHE Z CZ    
11833 N  N     . LYS F 645 ? 0.9263 0.8261 0.4847 0.0078  0.1895 0.0531  645 LYS Z N     
11834 C  CA    . LYS F 645 ? 0.9263 0.8419 0.486  0.0126  0.1896 0.0588  645 LYS Z CA    
11835 C  C     . LYS F 645 ? 0.9208 0.8535 0.4895 0.017   0.192  0.0641  645 LYS Z C     
11836 O  O     . LYS F 645 ? 0.9226 0.8519 0.4948 0.0251  0.1983 0.0642  645 LYS Z O     
11837 C  CB    . LYS F 645 ? 0.9523 0.8586 0.5082 0.0212  0.1945 0.0576  645 LYS Z CB    
11838 C  CG    . LYS F 645 ? 0.9962 0.9172 0.5514 0.0253  0.1938 0.063   645 LYS Z CG    
11839 C  CD    . LYS F 645 ? 1.053  0.9732 0.6002 0.0186  0.1876 0.0625  645 LYS Z CD    
11840 C  CE    . LYS F 645 ? 1.0963 1.0304 0.6426 0.0231  0.1871 0.0677  645 LYS Z CE    
11841 N  NZ    . LYS F 645 ? 1.1302 1.0595 0.667  0.0176  0.1819 0.0664  645 LYS Z NZ    
11842 N  N     . PRO F 646 ? 0.912  0.8631 0.484  0.0118  0.1871 0.0689  646 PRO Z N     
11843 C  CA    . PRO F 646 ? 0.9048 0.8729 0.4854 0.0163  0.1896 0.0746  646 PRO Z CA    
11844 C  C     . PRO F 646 ? 0.9033 0.885  0.4858 0.0252  0.1927 0.0806  646 PRO Z C     
11845 O  O     . PRO F 646 ? 0.9052 0.8913 0.4834 0.0246  0.1898 0.0821  646 PRO Z O     
11846 C  CB    . PRO F 646 ? 0.9071 0.889  0.4902 0.0063  0.1828 0.0773  646 PRO Z CB    
11847 C  CG    . PRO F 646 ? 0.915  0.8937 0.4903 -0.0015 0.1765 0.0755  646 PRO Z CG    
11848 C  CD    . PRO F 646 ? 0.905  0.8617 0.4728 0.0013  0.1792 0.0694  646 PRO Z CD    
11849 N  N     . LYS F 647 ? 0.8975 0.8856 0.4858 0.0337  0.1986 0.084   647 LYS Z N     
11850 C  CA    . LYS F 647 ? 0.8974 0.8985 0.4875 0.0429  0.2022 0.0901  647 LYS Z CA    
11851 C  C     . LYS F 647 ? 0.8891 0.9155 0.4849 0.0404  0.1983 0.0978  647 LYS Z C     
11852 O  O     . LYS F 647 ? 0.8861 0.9261 0.4817 0.0433  0.1972 0.1029  647 LYS Z O     
11853 C  CB    . LYS F 647 ? 0.9221 0.9175 0.5147 0.0536  0.2109 0.0906  647 LYS Z CB    
11854 C  CG    . LYS F 647 ? 0.9697 0.9766 0.5631 0.0641  0.2156 0.0967  647 LYS Z CG    
11855 C  CD    . LYS F 647 ? 1.0257 1.0268 0.6208 0.0744  0.2243 0.0976  647 LYS Z CD    
11856 C  CE    . LYS F 647 ? 1.0683 1.0771 0.6695 0.0735  0.2253 0.1001  647 LYS Z CE    
11857 N  NZ    . LYS F 647 ? 1.0982 1.1032 0.7001 0.0841  0.2339 0.1021  647 LYS Z NZ    
11858 N  N     . ASN F 648 ? 0.8837 0.917  0.4848 0.0351  0.1962 0.0989  648 ASN Z N     
11859 C  CA    . ASN F 648 ? 0.8778 0.9354 0.4854 0.0326  0.1929 0.1065  648 ASN Z CA    
11860 C  C     . ASN F 648 ? 0.8772 0.939  0.4858 0.0196  0.1852 0.1053  648 ASN Z C     
11861 O  O     . ASN F 648 ? 0.8852 0.9299 0.4893 0.013   0.1831 0.0984  648 ASN Z O     
11862 C  CB    . ASN F 648 ? 0.8857 0.9515 0.5    0.0414  0.1995 0.1112  648 ASN Z CB    
11863 C  CG    . ASN F 648 ? 0.9255 0.9744 0.5401 0.0422  0.2036 0.1059  648 ASN Z CG    
11864 O  OD1   . ASN F 648 ? 0.9393 0.9807 0.5535 0.0334  0.1997 0.1015  648 ASN Z OD1   
11865 N  ND2   . ASN F 648 ? 0.9351 0.9772 0.5498 0.0526  0.2115 0.1062  648 ASN Z ND2   
11866 N  N     . THR F 649 ? 0.866  0.9506 0.4805 0.0159  0.1814 0.1122  649 THR Z N     
11867 C  CA    . THR F 649 ? 0.8684 0.9599 0.4843 0.0036  0.1741 0.1123  649 THR Z CA    
11868 C  C     . THR F 649 ? 0.8712 0.953  0.4896 0.0002  0.1754 0.1084  649 THR Z C     
11869 O  O     . THR F 649 ? 0.874  0.951  0.49   -0.0104 0.1699 0.105   649 THR Z O     
11870 C  CB    . THR F 649 ? 0.8752 0.9948 0.4976 0.0018  0.1705 0.1214  649 THR Z CB    
11871 O  OG1   . THR F 649 ? 0.8842 1.0155 0.5145 0.0112  0.1767 0.1272  649 THR Z OG1   
11872 C  CG2   . THR F 649 ? 0.8768 1.0059 0.4959 0.0028  0.1676 0.1248  649 THR Z CG2   
11873 N  N     . ILE F 650 ? 0.8686 0.9468 0.491  0.0091  0.1826 0.1089  650 ILE Z N     
11874 C  CA    . ILE F 650 ? 0.8751 0.9432 0.4995 0.0065  0.1842 0.1052  650 ILE Z CA    
11875 C  C     . ILE F 650 ? 0.8885 0.9311 0.5054 0.0029  0.1838 0.0959  650 ILE Z C     
11876 O  O     . ILE F 650 ? 0.8935 0.9287 0.5091 -0.0058 0.18   0.0919  650 ILE Z O     
11877 C  CB    . ILE F 650 ? 0.8795 0.9496 0.5091 0.0172  0.1921 0.1082  650 ILE Z CB    
11878 C  CG1   . ILE F 650 ? 0.8814 0.9773 0.5189 0.0197  0.1923 0.1177  650 ILE Z CG1   
11879 C  CG2   . ILE F 650 ? 0.8901 0.9443 0.5197 0.0158  0.1945 0.1027  650 ILE Z CG2   
11880 C  CD1   . ILE F 650 ? 0.892  0.9997 0.5343 0.0098  0.1868 0.1198  650 ILE Z CD1   
11881 N  N     . ALA F 651 ? 0.8916 0.9213 0.5036 0.0095  0.1875 0.0928  651 ALA Z N     
11882 C  CA    . ALA F 651 ? 0.9048 0.9111 0.5099 0.0069  0.1875 0.0846  651 ALA Z CA    
11883 C  C     . ALA F 651 ? 0.9099 0.9132 0.5091 -0.0039 0.18   0.0819  651 ALA Z C     
11884 O  O     . ALA F 651 ? 0.9176 0.9045 0.5124 -0.0095 0.1784 0.0758  651 ALA Z O     
11885 C  CB    . ALA F 651 ? 0.9117 0.9071 0.5132 0.0164  0.1931 0.0828  651 ALA Z CB    
11886 N  N     . GLU F 652 ? 0.9045 0.9236 0.5034 -0.0069 0.1754 0.0867  652 GLU Z N     
11887 C  CA    . GLU F 652 ? 0.9135 0.9309 0.5059 -0.0176 0.168  0.0847  652 GLU Z CA    
11888 C  C     . GLU F 652 ? 0.9141 0.9326 0.5077 -0.0281 0.1634 0.0836  652 GLU Z C     
11889 O  O     . GLU F 652 ? 0.9226 0.9277 0.5092 -0.0362 0.1595 0.0784  652 GLU Z O     
11890 C  CB    . GLU F 652 ? 0.9391 0.9753 0.5315 -0.0183 0.1642 0.0909  652 GLU Z CB    
11891 C  CG    . GLU F 652 ? 1.0117 1.0444 0.5957 -0.0288 0.1567 0.0888  652 GLU Z CG    
11892 C  CD    . GLU F 652 ? 1.098  1.1476 0.681  -0.0291 0.153  0.0945  652 GLU Z CD    
11893 O  OE1   . GLU F 652 ? 1.1129 1.1705 0.6993 -0.019  0.1574 0.0984  652 GLU Z OE1   
11894 O  OE2   . GLU F 652 ? 1.1282 1.1827 0.7067 -0.0394 0.1456 0.0951  652 GLU Z OE2   
11895 N  N     . LYS F 653 ? 0.9036 0.937  0.5057 -0.0275 0.1642 0.0882  653 LYS Z N     
11896 C  CA    . LYS F 653 ? 0.9064 0.9413 0.5103 -0.0368 0.1605 0.0873  653 LYS Z CA    
11897 C  C     . LYS F 653 ? 0.9096 0.9217 0.5103 -0.0376 0.163  0.0798  653 LYS Z C     
11898 O  O     . LYS F 653 ? 0.9141 0.9185 0.5109 -0.047  0.1589 0.0762  653 LYS Z O     
11899 C  CB    . LYS F 653 ? 0.9263 0.9819 0.5404 -0.0346 0.1618 0.0943  653 LYS Z CB    
11900 C  CG    . LYS F 653 ? 0.9754 1.0557 0.5932 -0.0368 0.1576 0.1021  653 LYS Z CG    
11901 C  CD    . LYS F 653 ? 1.0235 1.1241 0.6513 -0.036  0.1584 0.109   653 LYS Z CD    
11902 C  CE    . LYS F 653 ? 1.0617 1.1881 0.6943 -0.0361 0.1553 0.1177  653 LYS Z CE    
11903 N  NZ    . LYS F 653 ? 1.0811 1.2276 0.7239 -0.0335 0.1572 0.125   653 LYS Z NZ    
11904 N  N     . LEU F 654 ? 0.9049 0.906  0.5066 -0.0279 0.1698 0.0774  654 LEU Z N     
11905 C  CA    . LEU F 654 ? 0.9108 0.8907 0.5098 -0.0276 0.1727 0.0706  654 LEU Z CA    
11906 C  C     . LEU F 654 ? 0.9178 0.8803 0.5072 -0.0325 0.1699 0.0647  654 LEU Z C     
11907 O  O     . LEU F 654 ? 0.9244 0.8741 0.51   -0.039  0.1679 0.06    654 LEU Z O     
11908 C  CB    . LEU F 654 ? 0.913  0.8865 0.515  -0.016  0.1804 0.0701  654 LEU Z CB    
11909 C  CG    . LEU F 654 ? 0.9368 0.8878 0.5356 -0.0145 0.1838 0.0631  654 LEU Z CG    
11910 C  CD1   . LEU F 654 ? 0.9414 0.888  0.5418 -0.0206 0.1822 0.0607  654 LEU Z CD1   
11911 C  CD2   . LEU F 654 ? 0.9465 0.8927 0.5477 -0.0033 0.1912 0.0633  654 LEU Z CD2   
11912 N  N     . VAL F 655 ? 0.9138 0.8758 0.4988 -0.0295 0.1697 0.0653  655 VAL Z N     
11913 C  CA    . VAL F 655 ? 0.9215 0.8674 0.4969 -0.0334 0.1674 0.0602  655 VAL Z CA    
11914 C  C     . VAL F 655 ? 0.9226 0.8687 0.4925 -0.0457 0.1602 0.0592  655 VAL Z C     
11915 O  O     . VAL F 655 ? 0.9326 0.8613 0.4959 -0.0507 0.159  0.0537  655 VAL Z O     
11916 C  CB    . VAL F 655 ? 0.9296 0.877  0.5016 -0.0275 0.1686 0.0618  655 VAL Z CB    
11917 C  CG1   . VAL F 655 ? 0.9463 0.8795 0.5076 -0.0328 0.1652 0.0576  655 VAL Z CG1   
11918 C  CG2   . VAL F 655 ? 0.9356 0.8764 0.5106 -0.0159 0.1762 0.061   655 VAL Z CG2   
11919 N  N     . ASN F 656 ? 0.9104 0.8761 0.4833 -0.0508 0.1555 0.0647  656 ASN Z N     
11920 C  CA    . ASN F 656 ? 0.9125 0.8797 0.4801 -0.0631 0.1485 0.0643  656 ASN Z CA    
11921 C  C     . ASN F 656 ? 0.9133 0.8723 0.4817 -0.0687 0.1481 0.061   656 ASN Z C     
11922 O  O     . ASN F 656 ? 0.9205 0.8683 0.481  -0.0776 0.1441 0.0573  656 ASN Z O     
11923 C  CB    . ASN F 656 ? 0.9164 0.908  0.4883 -0.067  0.1438 0.0715  656 ASN Z CB    
11924 C  CG    . ASN F 656 ? 0.9526 0.9511 0.5213 -0.064  0.1425 0.0744  656 ASN Z CG    
11925 O  OD1   . ASN F 656 ? 0.972  0.9552 0.5326 -0.062  0.1434 0.0704  656 ASN Z OD1   
11926 N  ND2   . ASN F 656 ? 0.951  0.9729 0.5259 -0.0634 0.1405 0.0816  656 ASN Z ND2   
11927 N  N     . TYR F 657 ? 0.9054 0.869  0.4827 -0.0633 0.1524 0.0623  657 TYR Z N     
11928 C  CA    . TYR F 657 ? 0.9102 0.8667 0.4894 -0.0671 0.1529 0.0594  657 TYR Z CA    
11929 C  C     . TYR F 657 ? 0.9228 0.8543 0.495  -0.0665 0.1552 0.052   657 TYR Z C     
11930 O  O     . TYR F 657 ? 0.9295 0.8508 0.497  -0.0741 0.1526 0.0485  657 TYR Z O     
11931 C  CB    . TYR F 657 ? 0.9024 0.8695 0.4922 -0.0599 0.1576 0.0628  657 TYR Z CB    
11932 C  CG    . TYR F 657 ? 0.9117 0.8696 0.5038 -0.0614 0.1595 0.0596  657 TYR Z CG    
11933 C  CD1   . TYR F 657 ? 0.9189 0.8832 0.5124 -0.07   0.1555 0.0607  657 TYR Z CD1   
11934 C  CD2   . TYR F 657 ? 0.9256 0.8702 0.5191 -0.0539 0.1653 0.056   657 TYR Z CD2   
11935 C  CE1   . TYR F 657 ? 0.9314 0.8877 0.527  -0.0711 0.1573 0.0579  657 TYR Z CE1   
11936 C  CE2   . TYR F 657 ? 0.9379 0.8748 0.5334 -0.0551 0.1669 0.0533  657 TYR Z CE2   
11937 C  CZ    . TYR F 657 ? 0.9457 0.8885 0.5423 -0.0635 0.163  0.0543  657 TYR Z CZ    
11938 O  OH    . TYR F 657 ? 0.9636 0.8986 0.5621 -0.0645 0.1646 0.0516  657 TYR Z OH    
11939 N  N     . ILE F 658 ? 0.9239 0.846  0.4954 -0.0577 0.16   0.05    658 ILE Z N     
11940 C  CA    . ILE F 658 ? 0.9371 0.8365 0.5027 -0.0562 0.1626 0.0436  658 ILE Z CA    
11941 C  C     . ILE F 658 ? 0.9447 0.833  0.4992 -0.064  0.1581 0.0405  658 ILE Z C     
11942 O  O     . ILE F 658 ? 0.9534 0.8263 0.5025 -0.0685 0.1575 0.0359  658 ILE Z O     
11943 C  CB    . ILE F 658 ? 0.9464 0.84   0.5138 -0.0452 0.1687 0.0429  658 ILE Z CB    
11944 C  CG1   . ILE F 658 ? 0.9548 0.8558 0.5317 -0.0376 0.1737 0.0452  658 ILE Z CG1   
11945 C  CG2   . ILE F 658 ? 0.9616 0.8328 0.5225 -0.0441 0.1709 0.0367  658 ILE Z CG2   
11946 C  CD1   . ILE F 658 ? 0.9729 0.8716 0.5517 -0.027  0.1794 0.0457  658 ILE Z CD1   
11947 N  N     . LYS F 659 ? 0.9403 0.8363 0.4908 -0.0657 0.1549 0.0432  659 LYS Z N     
11948 C  CA    . LYS F 659 ? 0.9509 0.8367 0.4897 -0.0732 0.1504 0.0407  659 LYS Z CA    
11949 C  C     . LYS F 659 ? 0.9542 0.8384 0.4886 -0.0846 0.1453 0.0396  659 LYS Z C     
11950 O  O     . LYS F 659 ? 0.9644 0.8308 0.4894 -0.0893 0.1442 0.035   659 LYS Z O     
11951 C  CB    . LYS F 659 ? 0.9709 0.8683 0.5071 -0.0732 0.1474 0.0446  659 LYS Z CB    
11952 C  CG    . LYS F 659 ? 1.0248 0.916  0.5597 -0.0636 0.1519 0.0438  659 LYS Z CG    
11953 C  CD    . LYS F 659 ? 1.0796 0.9799 0.6099 -0.0647 0.1483 0.0471  659 LYS Z CD    
11954 C  CE    . LYS F 659 ? 1.1341 1.0238 0.6515 -0.0745 0.1427 0.0446  659 LYS Z CE    
11955 N  NZ    . LYS F 659 ? 1.1577 1.0548 0.6698 -0.0752 0.1394 0.0475  659 LYS Z NZ    
11956 N  N     . LEU F 660 ? 0.9445 0.8469 0.4854 -0.0888 0.1423 0.044   660 LEU Z N     
11957 C  CA    . LEU F 660 ? 0.951  0.8538 0.4883 -0.1    0.1373 0.0436  660 LEU Z CA    
11958 C  C     . LEU F 660 ? 0.9579 0.8472 0.4957 -0.1008 0.1399 0.0393  660 LEU Z C     
11959 O  O     . LEU F 660 ? 0.9655 0.8438 0.4953 -0.1091 0.1369 0.0363  660 LEU Z O     
11960 C  CB    . LEU F 660 ? 0.9436 0.8712 0.4892 -0.1034 0.1341 0.0501  660 LEU Z CB    
11961 C  CG    . LEU F 660 ? 0.9607 0.8988 0.5006 -0.1124 0.1272 0.0534  660 LEU Z CG    
11962 C  CD1   . LEU F 660 ? 0.9669 0.906  0.5029 -0.1079 0.1271 0.0545  660 LEU Z CD1   
11963 C  CD2   . LEU F 660 ? 0.9587 0.9215 0.508  -0.1159 0.1243 0.06    660 LEU Z CD2   
11964 N  N     . ASN F 661 ? 0.953  0.8428 0.4997 -0.0922 0.1454 0.0392  661 ASN Z N     
11965 C  CA    . ASN F 661 ? 0.9603 0.8387 0.5085 -0.0923 0.1479 0.0355  661 ASN Z CA    
11966 C  C     . ASN F 661 ? 0.9707 0.8282 0.5145 -0.0869 0.1522 0.0301  661 ASN Z C     
11967 O  O     . ASN F 661 ? 0.972  0.8225 0.52   -0.0835 0.1558 0.0278  661 ASN Z O     
11968 C  CB    . ASN F 661 ? 0.9673 0.8592 0.5274 -0.0877 0.1507 0.0387  661 ASN Z CB    
11969 C  CG    . ASN F 661 ? 1.0034 0.9147 0.5678 -0.0941 0.1464 0.0438  661 ASN Z CG    
11970 O  OD1   . ASN F 661 ? 1.0102 0.9397 0.5808 -0.091  0.1462 0.0492  661 ASN Z OD1   
11971 N  ND2   . ASN F 661 ? 1.016  0.9239 0.5769 -0.1032 0.143  0.0424  661 ASN Z ND2   
11972 N  N     . PHE F 662 ? 0.9766 0.8239 0.512  -0.0863 0.1519 0.0282  662 PHE Z N     
11973 C  CA    . PHE F 662 ? 0.9893 0.8169 0.5203 -0.0815 0.1559 0.0234  662 PHE Z CA    
11974 C  C     . PHE F 662 ? 1      0.8111 0.5212 -0.0891 0.1538 0.0193  662 PHE Z C     
11975 O  O     . PHE F 662 ? 1.0086 0.8073 0.5191 -0.0919 0.1524 0.017   662 PHE Z O     
11976 C  CB    . PHE F 662 ? 0.9914 0.8151 0.5181 -0.0765 0.1572 0.0233  662 PHE Z CB    
11977 C  CG    . PHE F 662 ? 1.0043 0.8142 0.5321 -0.0679 0.163  0.0201  662 PHE Z CG    
11978 C  CD1   . PHE F 662 ? 1.0084 0.8253 0.5455 -0.0588 0.1676 0.0218  662 PHE Z CD1   
11979 C  CD2   . PHE F 662 ? 1.0245 0.8145 0.5439 -0.0689 0.1641 0.0157  662 PHE Z CD2   
11980 C  CE1   . PHE F 662 ? 1.0211 0.8255 0.5593 -0.0515 0.1728 0.019   662 PHE Z CE1   
11981 C  CE2   . PHE F 662 ? 1.0368 0.8153 0.558  -0.0612 0.1694 0.0131  662 PHE Z CE2   
11982 C  CZ    . PHE F 662 ? 1.0282 0.814  0.5587 -0.0528 0.1736 0.0147  662 PHE Z CZ    
11983 N  N     . LYS F 663 ? 0.9972 0.8082 0.5216 -0.0925 0.1536 0.0185  663 LYS Z N     
11984 C  CA    . LYS F 663 ? 1.0078 0.8039 0.5238 -0.0995 0.152  0.0149  663 LYS Z CA    
11985 C  C     . LYS F 663 ? 1.0037 0.797  0.5266 -0.0971 0.155  0.0133  663 LYS Z C     
11986 O  O     . LYS F 663 ? 0.9954 0.8025 0.5286 -0.0945 0.1559 0.0161  663 LYS Z O     
11987 C  CB    . LYS F 663 ? 1.0319 0.8348 0.5421 -0.1105 0.1458 0.0167  663 LYS Z CB    
11988 C  CG    . LYS F 663 ? 1.094  0.8794 0.5924 -0.1182 0.144  0.0128  663 LYS Z CG    
11989 C  CD    . LYS F 663 ? 1.1473 0.9407 0.6421 -0.1292 0.1384 0.0147  663 LYS Z CD    
11990 C  CE    . LYS F 663 ? 1.1992 0.9768 0.6853 -0.1358 0.1377 0.0111  663 LYS Z CE    
11991 N  NZ    . LYS F 663 ? 1.2211 0.997  0.7153 -0.1319 0.1414 0.0098  663 LYS Z NZ    
11992 N  N     . SER F 664 ? 1.0088 0.7839 0.5259 -0.0976 0.1568 0.0091  664 SER Z N     
11993 C  CA    . SER F 664 ? 1.0132 0.7843 0.5361 -0.0955 0.1596 0.0074  664 SER Z CA    
11994 C  C     . SER F 664 ? 1.0264 0.7809 0.5403 -0.1009 0.159  0.0038  664 SER Z C     
11995 O  O     . SER F 664 ? 1.0353 0.7759 0.5387 -0.1026 0.1587 0.0015  664 SER Z O     
11996 C  CB    . SER F 664 ? 1.0264 0.7937 0.556  -0.0854 0.1649 0.0064  664 SER Z CB    
11997 O  OG    . SER F 664 ? 1.0504 0.813  0.5849 -0.0835 0.1675 0.0047  664 SER Z OG    
11998 N  N     . ASN F 665 ? 1.0265 0.7817 0.5441 -0.1031 0.1591 0.0033  665 ASN Z N     
11999 C  CA    . ASN F 665 ? 1.0415 0.7811 0.5513 -0.1075 0.1591 0       665 ASN Z CA    
12000 C  C     . ASN F 665 ? 1.0447 0.7713 0.5566 -0.1003 0.1639 -0.0029 665 ASN Z C     
12001 O  O     . ASN F 665 ? 1.0529 0.7644 0.5574 -0.1024 0.1647 -0.0058 665 ASN Z O     
12002 C  CB    . ASN F 665 ? 1.0585 0.8047 0.5706 -0.1137 0.1567 0.0009  665 ASN Z CB    
12003 C  CG    . ASN F 665 ? 1.1046 0.8621 0.6135 -0.1221 0.1516 0.0036  665 ASN Z CG    
12004 O  OD1   . ASN F 665 ? 1.1249 0.8831 0.6277 -0.1245 0.1492 0.0045  665 ASN Z OD1   
12005 N  ND2   . ASN F 665 ? 1.1096 0.8761 0.6224 -0.127  0.1497 0.0052  665 ASN Z ND2   
12006 N  N     . ILE F 666 ? 1.0359 0.7684 0.5576 -0.0921 0.1673 -0.0021 666 ILE Z N     
12007 C  CA    . ILE F 666 ? 1.0391 0.7614 0.564  -0.0854 0.1717 -0.0043 666 ILE Z CA    
12008 C  C     . ILE F 666 ? 1.0391 0.7555 0.5624 -0.0793 0.1743 -0.0049 666 ILE Z C     
12009 O  O     . ILE F 666 ? 1.047  0.7486 0.5651 -0.0775 0.1765 -0.0074 666 ILE Z O     
12010 C  CB    . ILE F 666 ? 1.0387 0.7709 0.5755 -0.0811 0.1737 -0.0031 666 ILE Z CB    
12011 C  CG1   . ILE F 666 ? 1.0499 0.7872 0.588  -0.0869 0.1713 -0.0026 666 ILE Z CG1   
12012 C  CG2   . ILE F 666 ? 1.0465 0.7692 0.5869 -0.0744 0.178  -0.0052 666 ILE Z CG2   
12013 C  CD1   . ILE F 666 ? 1.0606 0.8096 0.6096 -0.0832 0.1728 -0.0007 666 ILE Z CD1   
12014 N  N     . PHE F 667 ? 1.0288 0.7565 0.5563 -0.0761 0.1742 -0.0024 667 PHE Z N     
12015 C  CA    . PHE F 667 ? 1.0317 0.7549 0.5582 -0.07   0.1769 -0.0027 667 PHE Z CA    
12016 C  C     . PHE F 667 ? 1.0397 0.756  0.5549 -0.0736 0.1747 -0.0032 667 PHE Z C     
12017 O  O     . PHE F 667 ? 1.0404 0.7643 0.5519 -0.0794 0.1706 -0.0015 667 PHE Z O     
12018 C  CB    . PHE F 667 ? 1.0207 0.7582 0.5564 -0.0642 0.1783 0.0001  667 PHE Z CB    
12019 C  CG    . PHE F 667 ? 1.0271 0.759  0.5658 -0.0559 0.1828 -0.0007 667 PHE Z CG    
12020 C  CD1   . PHE F 667 ? 1.0366 0.7652 0.5706 -0.0534 0.1834 -0.0005 667 PHE Z CD1   
12021 C  CD2   . PHE F 667 ? 1.0348 0.765  0.581  -0.0508 0.1864 -0.0015 667 PHE Z CD2   
12022 C  CE1   . PHE F 667 ? 1.0443 0.7679 0.5812 -0.0459 0.1877 -0.0011 667 PHE Z CE1   
12023 C  CE2   . PHE F 667 ? 1.0424 0.7673 0.5911 -0.0438 0.1905 -0.0021 667 PHE Z CE2   
12024 C  CZ    . PHE F 667 ? 1.04   0.7617 0.5842 -0.0413 0.1912 -0.0019 667 PHE Z CZ    
12025 N  N     . ASP F 668 ? 1.0436 0.7456 0.5535 -0.0702 0.1774 -0.0053 668 ASP Z N     
12026 C  CA    . ASP F 668 ? 1.054  0.7469 0.5522 -0.0727 0.176  -0.006  668 ASP Z CA    
12027 C  C     . ASP F 668 ? 1.0513 0.7545 0.5514 -0.0697 0.1754 -0.0036 668 ASP Z C     
12028 O  O     . ASP F 668 ? 1.0514 0.7524 0.5547 -0.0626 0.179  -0.0037 668 ASP Z O     
12029 C  CB    . ASP F 668 ? 1.0818 0.7568 0.5748 -0.0685 0.1799 -0.0085 668 ASP Z CB    
12030 C  CG    . ASP F 668 ? 1.1517 0.8134 0.6304 -0.0719 0.1787 -0.0097 668 ASP Z CG    
12031 O  OD1   . ASP F 668 ? 1.1631 0.8302 0.6367 -0.0755 0.1754 -0.0083 668 ASP Z OD1   
12032 O  OD2   . ASP F 668 ? 1.1874 0.8333 0.6598 -0.071  0.1812 -0.0117 668 ASP Z OD2   
12033 N  N     . THR F 669 ? 1.0471 0.7617 0.5454 -0.0753 0.171  -0.0013 669 THR Z N     
12034 C  CA    . THR F 669 ? 1.0486 0.7742 0.5483 -0.073  0.17   0.0014  669 THR Z CA    
12035 C  C     . THR F 669 ? 1.0596 0.7743 0.5484 -0.0726 0.1699 0.0004  669 THR Z C     
12036 O  O     . THR F 669 ? 1.0585 0.7808 0.548  -0.0699 0.1695 0.0024  669 THR Z O     
12037 C  CB    . THR F 669 ? 1.059  0.8017 0.5609 -0.079  0.1652 0.0046  669 THR Z CB    
12038 O  OG1   . THR F 669 ? 1.0794 0.8156 0.5704 -0.0884 0.1609 0.0036  669 THR Z OG1   
12039 C  CG2   . THR F 669 ? 1.0549 0.8096 0.5682 -0.0782 0.1658 0.0061  669 THR Z CG2   
12040 N  N     . GLY F 670 ? 1.069  0.7656 0.5477 -0.0748 0.1706 -0.0026 670 GLY Z N     
12041 C  CA    . GLY F 670 ? 1.0835 0.767  0.5508 -0.0743 0.1711 -0.0038 670 GLY Z CA    
12042 C  C     . GLY F 670 ? 1.088  0.7677 0.5592 -0.0647 0.176  -0.004  670 GLY Z C     
12043 O  O     . GLY F 670 ? 1.0964 0.7692 0.5598 -0.0632 0.1764 -0.0042 670 GLY Z O     
12044 N  N     . PHE F 671 ? 1.0813 0.7653 0.5643 -0.0584 0.1798 -0.004  671 PHE Z N     
12045 C  CA    . PHE F 671 ? 1.0863 0.7681 0.5745 -0.0495 0.1846 -0.004  671 PHE Z CA    
12046 C  C     . PHE F 671 ? 1.0799 0.7766 0.5736 -0.0458 0.1843 -0.0011 671 PHE Z C     
12047 O  O     . PHE F 671 ? 1.081  0.7765 0.5782 -0.0385 0.1882 -0.0009 671 PHE Z O     
12048 C  CB    . PHE F 671 ? 1.0865 0.7666 0.5844 -0.0449 0.1886 -0.005  671 PHE Z CB    
12049 C  CG    . PHE F 671 ? 1.104  0.7728 0.6026 -0.0377 0.1937 -0.0064 671 PHE Z CG    
12050 C  CD1   . PHE F 671 ? 1.1248 0.777  0.616  -0.0381 0.1954 -0.0085 671 PHE Z CD1   
12051 C  CD2   . PHE F 671 ? 1.1127 0.7874 0.6194 -0.0305 0.1971 -0.0053 671 PHE Z CD2   
12052 C  CE1   . PHE F 671 ? 1.1384 0.7812 0.6309 -0.0315 0.2002 -0.0093 671 PHE Z CE1   
12053 C  CE2   . PHE F 671 ? 1.1264 0.7911 0.634  -0.0243 0.2018 -0.0063 671 PHE Z CE2   
12054 C  CZ    . PHE F 671 ? 1.1318 0.781  0.6326 -0.0248 0.2033 -0.0082 671 PHE Z CZ    
12055 N  N     . PHE F 672 ? 1.0716 0.7823 0.5659 -0.0506 0.1799 0.0013  672 PHE Z N     
12056 C  CA    . PHE F 672 ? 1.0689 0.7947 0.5684 -0.0472 0.1794 0.0045  672 PHE Z CA    
12057 C  C     . PHE F 672 ? 1.0768 0.8067 0.5676 -0.0524 0.1748 0.0062  672 PHE Z C     
12058 O  O     . PHE F 672 ? 1.0826 0.8099 0.5659 -0.0607 0.1705 0.0056  672 PHE Z O     
12059 C  CB    . PHE F 672 ? 1.0572 0.7999 0.5676 -0.0475 0.1786 0.007   672 PHE Z CB    
12060 C  CG    . PHE F 672 ? 1.0611 0.8025 0.581  -0.0419 0.1831 0.006   672 PHE Z CG    
12061 C  CD1   . PHE F 672 ? 1.0715 0.8063 0.5924 -0.045  0.1832 0.0039  672 PHE Z CD1   
12062 C  CD2   . PHE F 672 ? 1.0665 0.8134 0.5937 -0.0338 0.1871 0.0074  672 PHE Z CD2   
12063 C  CE1   . PHE F 672 ? 1.0772 0.811  0.6065 -0.0402 0.187  0.0031  672 PHE Z CE1   
12064 C  CE2   . PHE F 672 ? 1.0726 0.8179 0.6078 -0.0292 0.191  0.0065  672 PHE Z CE2   
12065 C  CZ    . PHE F 672 ? 1.0709 0.81   0.6071 -0.0326 0.1908 0.0044  672 PHE Z CZ    
12066 N  N     . HIS F 673 ? 1.0765 0.8139 0.5686 -0.0478 0.1754 0.0084  673 HIS Z N     
12067 C  CA    . HIS F 673 ? 1.0875 0.8313 0.5725 -0.0522 0.1708 0.0105  673 HIS Z CA    
12068 C  C     . HIS F 673 ? 1.0831 0.8465 0.5773 -0.0479 0.1709 0.0147  673 HIS Z C     
12069 O  O     . HIS F 673 ? 1.0831 0.847  0.5816 -0.0396 0.1752 0.0152  673 HIS Z O     
12070 C  CB    . HIS F 673 ? 1.1124 0.842  0.5865 -0.0502 0.1719 0.0089  673 HIS Z CB    
12071 C  CG    . HIS F 673 ? 1.1527 0.8894 0.6196 -0.0542 0.1672 0.0112  673 HIS Z CG    
12072 N  ND1   . HIS F 673 ? 1.1762 0.921  0.6453 -0.0482 0.1684 0.0137  673 HIS Z ND1   
12073 C  CD2   . HIS F 673 ? 1.1736 0.911  0.6314 -0.0637 0.1613 0.0117  673 HIS Z CD2   
12074 C  CE1   . HIS F 673 ? 1.1853 0.9357 0.6469 -0.0541 0.1631 0.0156  673 HIS Z CE1   
12075 N  NE2   . HIS F 673 ? 1.1882 0.9342 0.6426 -0.0638 0.1586 0.0144  673 HIS Z NE2   
12076 N  N     . ILE F 674 ? 1.0786 0.8581 0.5762 -0.0534 0.1665 0.0178  674 ILE Z N     
12077 C  CA    . ILE F 674 ? 1.0785 0.8776 0.5848 -0.0492 0.1667 0.0223  674 ILE Z CA    
12078 C  C     . ILE F 674 ? 1.0889 0.8951 0.5888 -0.0515 0.1628 0.025   674 ILE Z C     
12079 O  O     . ILE F 674 ? 1.0903 0.9016 0.5849 -0.0602 0.157  0.0262  674 ILE Z O     
12080 C  CB    . ILE F 674 ? 1.0763 0.8906 0.5923 -0.0516 0.1654 0.0249  674 ILE Z CB    
12081 C  CG1   . ILE F 674 ? 1.0904 0.906  0.6012 -0.0629 0.1594 0.0247  674 ILE Z CG1   
12082 C  CG2   . ILE F 674 ? 1.0815 0.8897 0.605  -0.0464 0.1705 0.0227  674 ILE Z CG2   
12083 C  CD1   . ILE F 674 ? 1.0991 0.9307 0.6187 -0.0658 0.1577 0.0277  674 ILE Z CD1   
12084 N  N     . GLU F 675 ? 1.0956 0.9007 0.5952 -0.0438 0.166  0.0256  675 GLU Z N     
12085 C  CA    . GLU F 675 ? 1.1057 0.9163 0.5992 -0.0441 0.1632 0.0281  675 GLU Z CA    
12086 C  C     . GLU F 675 ? 1.1026 0.9365 0.6017 -0.0471 0.159  0.0336  675 GLU Z C     
12087 O  O     . GLU F 675 ? 1.1043 0.9437 0.5966 -0.0532 0.1536 0.0354  675 GLU Z O     
12088 C  CB    . GLU F 675 ? 1.1358 0.9419 0.6305 -0.0336 0.1687 0.0279  675 GLU Z CB    
12089 C  CG    . GLU F 675 ? 1.1979 1.0081 0.686  -0.0328 0.1665 0.0302  675 GLU Z CG    
12090 C  CD    . GLU F 675 ? 1.2769 1.0858 0.7676 -0.022  0.1721 0.0309  675 GLU Z CD    
12091 O  OE1   . GLU F 675 ? 1.2959 1.0955 0.791  -0.0156 0.1779 0.0284  675 GLU Z OE1   
12092 O  OE2   . GLU F 675 ? 1.2992 1.1166 0.7874 -0.02   0.1707 0.0339  675 GLU Z OE2   
12093 N  N     . GLY F 676 ? 1.0959 0.9431 0.6068 -0.0429 0.1614 0.0362  676 GLY Z N     
12094 C  CA    . GLY F 676 ? 1.0923 0.9627 0.6102 -0.0446 0.1583 0.0419  676 GLY Z CA    
12095 C  C     . GLY F 676 ? 1.0871 0.9679 0.6174 -0.0381 0.1627 0.0442  676 GLY Z C     
12096 O  O     . GLY F 676 ? 1.0899 0.9615 0.6234 -0.0304 0.1687 0.0419  676 GLY Z O     
12097 CA CA    . CA  G .   ? 0.5961 0.1898 0.1275 -0.0784 0.1852 -0.0272 701 CA  A CA    
12098 CA CA    . CA  H .   ? 0.7317 0.3384 0.268  -0.0857 0.1859 -0.0268 702 CA  A CA    
12099 CA CA    . CA  I .   ? 0.9227 0.5453 0.4454 -0.0983 0.2008 -0.0124 703 CA  A CA    
12100 CA CA    . CA  J .   ? 0.4904 0.1505 0.1512 0.0106  0.2047 -0.0007 701 CA  Z CA    
12101 CA CA    . CA  K .   ? 0.6418 0.3145 0.2455 0.018   0.2441 -0.0057 702 CA  Z CA    
12102 CA CA    . CA  L .   ? 1.085  0.8399 0.6666 0.0557  0.2525 0.0203  703 CA  Z CA    
12103 O  O1    . MES M .   ? 1.0741 0.7346 0.5517 0.0432  0.2299 0.007   704 MES Z O1    
12104 C  C2    . MES M .   ? 1.0795 0.7316 0.5528 0.0367  0.2271 0.005   704 MES Z C2    
12105 C  C3    . MES M .   ? 1.0764 0.7349 0.5588 0.0333  0.2261 0.0045  704 MES Z C3    
12106 N  N4    . MES M .   ? 1.0746 0.7317 0.5666 0.0392  0.2318 0.0041  704 MES Z N4    
12107 C  C5    . MES M .   ? 1.0706 0.7337 0.5657 0.0464  0.2353 0.006   704 MES Z C5    
12108 C  C6    . MES M .   ? 1.0737 0.7308 0.5594 0.049   0.2357 0.0064  704 MES Z C6    
12109 C  C7    . MES M .   ? 1.0801 0.722  0.5717 0.0402  0.2353 0.0019  704 MES Z C7    
12110 C  C8    . MES M .   ? 1.0766 0.7195 0.5789 0.0428  0.2389 0.0014  704 MES Z C8    
12111 S  S     . MES M .   ? 1.0802 0.7144 0.5841 0.038   0.2383 -0.0008 704 MES Z S     
12112 O  O1S   . MES M .   ? 1.0774 0.7199 0.5813 0.0314  0.2329 -0.0007 704 MES Z O1S   
12113 O  O2S   . MES M .   ? 1.0873 0.7074 0.5823 0.0379  0.2392 -0.0018 704 MES Z O2S   
12114 O  O3S   . MES M .   ? 1.0769 0.7108 0.5904 0.0415  0.2424 -0.0011 704 MES Z O3S   
12128 CL CL    . CL  N .   ? 1.2956 0.5306 0.5867 -0.1729 0.2492 -0.026  705 CL  Z CL    
12129 O  O     . HOH O .   ? 0.5098 0.0796 0.0975 -0.0786 0.1646 -0.027  801 HOH A O     
12130 O  O     . HOH O .   ? 0.677  0.3107 0.1806 -0.1512 0.1949 -0.0128 802 HOH A O     
12131 O  O     . HOH O .   ? 0.5055 0.0667 0.0963 -0.0814 0.1623 -0.0283 803 HOH A O     
12132 O  O     . HOH O .   ? 0.6526 0.2627 0.1129 -0.1957 0.1871 -0.0177 804 HOH A O     
12133 O  O     . HOH O .   ? 0.7907 0.3849 0.2745 -0.0289 0.2582 0.036   805 HOH A O     
12134 O  O     . HOH O .   ? 0.7324 0.1533 0.1259 -0.0383 0.2425 -0.0094 806 HOH A O     
12135 O  O     . HOH O .   ? 0.5622 0.1262 0.1021 -0.086  0.1795 -0.0291 807 HOH A O     
12136 O  O     . HOH O .   ? 0.9959 0.1958 0.1675 0.0701  0.3457 0.041   808 HOH A O     
12137 O  O     . HOH O .   ? 0.4955 0.2053 0.1112 -0.0902 0.1736 -0.0078 809 HOH A O     
12138 O  O     . HOH O .   ? 0.3882 0.0455 0.0976 -0.0462 0.1425 -0.0189 810 HOH A O     
12139 O  O     . HOH O .   ? 0.5206 0.5645 0.2239 -0.1068 0.2302 0.1399  811 HOH A O     
12140 O  O     . HOH O .   ? 0.5136 0.1557 0.1248 -0.0452 0.1927 -0.0173 812 HOH A O     
12141 O  O     . HOH O .   ? 0.8689 0.3758 0.3279 -0.0514 0.1826 -0.0267 813 HOH A O     
12142 O  O     . HOH O .   ? 0.5057 0.0542 0.0918 -0.0647 0.1557 -0.0219 814 HOH A O     
12143 O  O     . HOH O .   ? 0.385  0.0441 0.1    -0.0403 0.1448 -0.0169 815 HOH A O     
12144 O  O     . HOH O .   ? 0.6402 0.1759 0.1253 -0.0088 0.2252 -0.0013 816 HOH A O     
12145 O  O     . HOH O .   ? 0.8946 0.4244 0.3409 -0.0361 0.2515 0.0171  817 HOH A O     
12146 O  O     . HOH O .   ? 0.5551 0.1374 0.1454 0.0155  0.226  0.0307  818 HOH A O     
12147 O  O     . HOH O .   ? 0.419  0.0939 0.0919 -0.082  0.1405 -0.0265 819 HOH A O     
12148 O  O     . HOH O .   ? 0.5318 0.1128 0.1207 -0.0589 0.162  -0.0217 820 HOH A O     
12149 O  O     . HOH O .   ? 0.6417 0.1641 0.1133 0.014   0.2066 0.0205  821 HOH A O     
12150 O  O     . HOH O .   ? 0.5677 0.0764 0.0883 -0.0543 0.1588 -0.0202 822 HOH A O     
12151 O  O     . HOH O .   ? 0.9201 0.1725 0.1419 -0.0031 0.2981 0.0012  823 HOH A O     
12152 O  O     . HOH O .   ? 0.7259 0.2527 0.2089 -0.0558 0.148  -0.0241 824 HOH A O     
12153 O  O     . HOH O .   ? 0.5994 0.2293 0.116  -0.1235 0.1974 -0.0137 825 HOH A O     
12154 O  O     . HOH O .   ? 0.6805 0.1964 0.1531 -0.0547 0.1564 -0.0266 826 HOH A O     
12155 O  O     . HOH O .   ? 0.5556 0.1987 0.1078 -0.0963 0.1843 -0.0216 827 HOH A O     
12156 O  O     . HOH O .   ? 0.8846 0.1787 0.1431 0.0242  0.2937 0.013   828 HOH A O     
12157 O  O     . HOH O .   ? 0.9264 0.2145 0.1709 -0.0861 0.2641 -0.0337 829 HOH A O     
12158 O  O     . HOH O .   ? 0.7409 0.1656 0.1176 0.0101  0.2323 0.0033  830 HOH A O     
12159 O  O     . HOH O .   ? 0.5546 0.0907 0.1003 -0.05   0.176  -0.018  831 HOH A O     
12160 O  O     . HOH O .   ? 0.4797 0.0737 0.1027 -0.0532 0.1661 -0.0204 832 HOH A O     
12161 O  O     . HOH O .   ? 0.4686 0.1275 0.1001 -0.0801 0.1594 -0.0216 833 HOH A O     
12162 O  O     . HOH O .   ? 0.6144 0.1591 0.1408 0.0227  0.2332 0.0353  834 HOH A O     
12163 O  O     . HOH O .   ? 0.56   0.0744 0.0805 -0.0628 0.1445 -0.0208 835 HOH A O     
12164 O  O     . HOH O .   ? 0.6182 0.2189 0.1461 -0.0794 0.1923 -0.0252 836 HOH A O     
12165 O  O     . HOH O .   ? 0.5801 0.1241 0.0978 -0.0207 0.176  -0.0023 837 HOH A O     
12166 O  O     . HOH O .   ? 0.7614 0.1568 0.1563 0.0326  0.2851 0.0311  838 HOH A O     
12167 O  O     . HOH O .   ? 0.4794 0.0486 0.0878 -0.0625 0.1455 -0.0207 839 HOH A O     
12168 O  O     . HOH O .   ? 0.6805 0.1858 0.1    -0.1334 0.1943 -0.0346 840 HOH A O     
12169 O  O     . HOH O .   ? 0.717  0.5028 0.2673 -0.2223 0.1782 0.0289  841 HOH A O     
12170 O  O     . HOH O .   ? 1.0604 0.1677 0.1373 -0.0604 0.3135 -0.0166 842 HOH A O     
12171 O  O     . HOH O .   ? 0.4325 0.0418 0.1097 -0.0231 0.166  -0.0096 843 HOH A O     
12172 O  O     . HOH O .   ? 0.6279 0.2756 0.1953 -0.0654 0.1914 -0.0214 844 HOH A O     
12173 O  O     . HOH O .   ? 0.8079 0.1627 0.1214 -0.059  0.2475 -0.0281 845 HOH A O     
12174 O  O     . HOH O .   ? 0.9228 0.2246 0.1966 0.1386  0.3595 0.0959  846 HOH A O     
12175 O  O     . HOH O .   ? 0.4001 0.043  0.1034 -0.0357 0.1519 -0.015  847 HOH A O     
12176 O  O     . HOH O .   ? 0.6803 0.1669 0.1597 0.0457  0.2686 0.0474  848 HOH A O     
12177 O  O     . HOH O .   ? 0.5579 0.0735 0.0836 -0.0604 0.1497 -0.0204 849 HOH A O     
12178 O  O     . HOH O .   ? 0.5192 0.0647 0.0925 -0.0666 0.1589 -0.0228 850 HOH A O     
12179 O  O     . HOH O .   ? 0.737  0.2141 0.1349 0.007   0.2534 0.0203  851 HOH A O     
12180 O  O     . HOH O .   ? 1.0202 0.1845 0.1603 0.0373  0.341  0.023   852 HOH A O     
12181 O  O     . HOH O .   ? 0.8966 0.1569 0.1393 -0.0195 0.2897 0.0008  853 HOH A O     
12182 O  O     . HOH O .   ? 0.6999 0.176  0.1142 -0.0214 0.2199 -0.0043 854 HOH A O     
12183 O  O     . HOH O .   ? 0.6031 0.336  0.1058 -0.226  0.1553 0.0031  855 HOH A O     
12184 O  O     . HOH O .   ? 0.7504 0.1788 0.1147 -0.1228 0.2264 -0.0371 856 HOH A O     
12185 O  O     . HOH O .   ? 0.6862 0.3113 0.1732 0.0233  0.2729 0.0529  857 HOH A O     
12186 O  O     . HOH O .   ? 0.4407 0.0733 0.1008 -0.0559 0.1501 -0.0188 858 HOH A O     
12187 O  O     . HOH O .   ? 0.4245 0.0477 0.0832 -0.0562 0.1297 -0.0189 859 HOH A O     
12188 O  O     . HOH O .   ? 0.856  0.1681 0.1205 -0.098  0.2545 -0.0352 860 HOH A O     
12189 O  O     . HOH O .   ? 0.9595 0.1621 0.1373 -0.0373 0.2973 -0.0074 861 HOH A O     
12190 O  O     . HOH O .   ? 0.788  0.1771 0.1751 0.0744  0.309  0.0604  862 HOH A O     
12191 O  O     . HOH O .   ? 0.5852 0.3451 0.1044 -0.2181 0.1521 0.0077  863 HOH A O     
12192 O  O     . HOH O .   ? 0.6378 0.1987 0.1546 -0.0166 0.1819 0.0052  864 HOH A O     
12193 O  O     . HOH O .   ? 0.5164 0.2757 0.1189 -0.0728 0.1877 0.0014  865 HOH A O     
12194 O  O     . HOH O .   ? 0.4223 0.0418 0.1053 -0.0299 0.1586 -0.0124 866 HOH A O     
12195 O  O     . HOH O .   ? 1.0386 0.237  0.2048 0.0589  0.339  0.0317  867 HOH A O     
12196 O  O     . HOH O .   ? 0.7696 0.1599 0.1177 -0.0575 0.2355 -0.0282 868 HOH A O     
12197 O  O     . HOH O .   ? 0.6399 0.4732 0.2404 -0.1172 0.1695 0.0203  869 HOH A O     
12198 O  O     . HOH O .   ? 0.6887 0.2143 0.1371 0.007   0.2494 0.0066  870 HOH A O     
12199 O  O     . HOH O .   ? 0.5543 0.1432 0.0884 -0.0188 0.1526 0.0123  871 HOH A O     
12200 O  O     . HOH P .   ? 0.7757 0.1779 0.1073 -0.1339 0.2211 -0.0383 101 HOH E O     
12201 O  O     . HOH P .   ? 0.584  0.0826 0.0973 -0.0634 0.1761 -0.0236 102 HOH E O     
12202 O  O     . HOH Q .   ? 0.609  0.1169 0.1004 -0.1024 0.1851 -0.0323 101 HOH F O     
12203 O  O     . HOH Q .   ? 0.8258 0.2785 0.1646 -0.1804 0.195  -0.039  102 HOH F O     
12204 O  O     . HOH Q .   ? 0.7796 0.182  0.111  -0.1434 0.2276 -0.0399 103 HOH F O     
12205 O  O     . HOH Q .   ? 0.7003 0.2026 0.0976 -0.1549 0.1926 -0.0356 104 HOH F O     
12206 O  O     . HOH Q .   ? 0.6318 0.1759 0.11   -0.119  0.2005 -0.0275 105 HOH F O     
12207 O  O     . HOH Q .   ? 0.6377 0.1328 0.1032 -0.0983 0.1937 -0.0307 106 HOH F O     
12208 O  O     . HOH R .   ? 0.7011 0.1669 0.1594 -0.0106 0.279  -0.0133 101 HOH U O     
12209 O  O     . HOH R .   ? 0.87   0.2624 0.1894 0.0748  0.3494 0.0189  102 HOH U O     
12210 O  O     . HOH R .   ? 0.8435 0.3698 0.3001 0.0995  0.3492 0.0141  103 HOH U O     
12211 O  O     . HOH R .   ? 0.7582 0.2804 0.1829 0.0701  0.3182 0.0222  104 HOH U O     
12212 O  O     . HOH R .   ? 0.6984 0.256  0.1701 0.0445  0.2906 0.0114  105 HOH U O     
12213 O  O     . HOH R .   ? 0.51   0.1186 0.162  0.0477  0.2372 0.0116  106 HOH U O     
12214 O  O     . HOH R .   ? 0.7577 0.3073 0.2203 0.1135  0.3524 0.0198  107 HOH U O     
12215 O  O     . HOH R .   ? 0.5484 0.2274 0.1627 0.0632  0.2481 0.0184  108 HOH U O     
12216 O  O     . HOH S .   ? 0.5014 0.1621 0.1487 0.0385  0.2228 0.0089  101 HOH V O     
12217 O  O     . HOH S .   ? 0.8632 0.1664 0.1552 -0.0127 0.306  -0.0126 102 HOH V O     
12218 O  O     . HOH S .   ? 0.7092 0.2475 0.2234 0.0885  0.3402 0.0039  103 HOH V O     
12219 O  O     . HOH S .   ? 0.6652 0.2183 0.2194 0.0856  0.3248 0.0059  104 HOH V O     
12220 O  O     . HOH S .   ? 0.8748 0.2405 0.1801 0.0568  0.3395 0.0121  105 HOH V O     
12221 O  O     . HOH S .   ? 0.6057 0.1843 0.199  0.074   0.2928 0.0094  106 HOH V O     
12222 O  O     . HOH S .   ? 1.0158 0.3289 0.3056 0.0149  0.3256 -0.0053 107 HOH V O     
12223 O  O     . HOH T .   ? 0.6354 0.2218 0.1228 -0.0105 0.2202 -0.0122 801 HOH Z O     
12224 O  O     . HOH T .   ? 0.5223 0.1586 0.1433 0.0383  0.2211 0.0045  802 HOH Z O     
12225 O  O     . HOH T .   ? 0.6634 0.1341 0.1844 -0.182  0.1913 -0.0026 803 HOH Z O     
12226 O  O     . HOH T .   ? 0.4866 0.0657 0.1116 -0.0267 0.1792 -0.0113 804 HOH Z O     
12227 O  O     . HOH T .   ? 0.5222 0.2236 0.125  -0.05   0.1952 -0.0124 805 HOH Z O     
12228 O  O     . HOH T .   ? 0.8439 0.0967 0.1621 -0.1591 0.2656 -0.023  806 HOH Z O     
12229 O  O     . HOH T .   ? 0.6114 0.4476 0.0837 -0.0644 0.1442 0.0363  807 HOH Z O     
12230 O  O     . HOH T .   ? 0.5798 0.2005 0.1385 0.0316  0.2281 -0.0014 808 HOH Z O     
12231 O  O     . HOH T .   ? 0.4317 0.0656 0.1306 0.0142  0.1887 0.0044  809 HOH Z O     
12232 O  O     . HOH T .   ? 0.3912 0.0428 0.1037 -0.0347 0.1504 -0.0148 810 HOH Z O     
12233 O  O     . HOH T .   ? 0.7221 0.1265 0.1476 -0.0533 0.2701 -0.0192 811 HOH Z O     
12234 O  O     . HOH T .   ? 0.7512 0.263  0.1958 0.071   0.3285 0.0104  812 HOH Z O     
12235 O  O     . HOH T .   ? 0.6175 0.173  0.1488 0.0126  0.2493 -0.0012 813 HOH Z O     
12236 O  O     . HOH T .   ? 0.3845 0.0713 0.0957 -0.0504 0.1393 -0.019  814 HOH Z O     
12237 O  O     . HOH T .   ? 0.8223 0.1046 0.1677 -0.1793 0.2439 -0.0208 815 HOH Z O     
12238 O  O     . HOH T .   ? 0.4386 0.1895 0.1133 -0.0132 0.1706 0.0024  816 HOH Z O     
12239 O  O     . HOH T .   ? 0.9    0.2241 0.2445 0.078   0.4093 -0.0002 817 HOH Z O     
12240 O  O     . HOH T .   ? 1.0285 0.8036 0.5792 -0.0806 0.17   0.0062  818 HOH Z O     
12241 O  O     . HOH T .   ? 0.6292 0.2347 0.1144 -0.0232 0.208  -0.0119 819 HOH Z O     
12242 O  O     . HOH T .   ? 0.6541 0.1428 0.1252 -0.0328 0.2277 -0.016  820 HOH Z O     
12243 O  O     . HOH T .   ? 0.4203 0.1263 0.1173 -0.0015 0.1719 0.0014  821 HOH Z O     
12244 O  O     . HOH T .   ? 0.6812 0.243  0.1638 0.036   0.2799 0.0092  822 HOH Z O     
12245 O  O     . HOH T .   ? 0.4256 0.0617 0.1045 -0.0296 0.1584 -0.0118 823 HOH Z O     
12246 O  O     . HOH T .   ? 0.4343 0.0639 0.1319 -0.0486 0.1877 -0.0156 824 HOH Z O     
12247 O  O     . HOH T .   ? 0.6523 0.3774 0.2347 0.0401  0.257  0.0184  825 HOH Z O     
12248 O  O     . HOH T .   ? 0.7904 0.3116 0.3412 -0.1268 0.1877 -0.0103 826 HOH Z O     
12249 O  O     . HOH T .   ? 0.732  0.3183 0.2149 0.1131  0.3416 0.0229  827 HOH Z O     
12250 O  O     . HOH T .   ? 0.5434 0.2945 0.1577 0.0635  0.2424 0.0277  828 HOH Z O     
12251 O  O     . HOH T .   ? 0.3861 0.0415 0.1152 -0.0267 0.162  -0.0125 829 HOH Z O     
12252 O  O     . HOH T .   ? 0.7212 0.3395 0.1979 0.1013  0.3257 0.0385  830 HOH Z O     
12253 O  O     . HOH T .   ? 0.8301 0.2444 0.2333 0.0873  0.381  0.0036  831 HOH Z O     
12254 O  O     . HOH T .   ? 0.5512 0.1245 0.1059 -0.0668 0.1801 -0.0218 832 HOH Z O     
12255 O  O     . HOH T .   ? 0.536  0.1434 0.1238 -0.0227 0.2032 -0.0111 833 HOH Z O     
12256 O  O     . HOH T .   ? 0.8743 0.2107 0.1863 0.037   0.3458 -0.0013 834 HOH Z O     
12257 O  O     . HOH T .   ? 0.7516 0.4125 0.3213 0.018   0.2502 0.0022  835 HOH Z O     
12258 O  O     . HOH T .   ? 0.4415 0.1726 0.1229 0.0097  0.1826 0.0071  836 HOH Z O     
12259 O  O     . HOH T .   ? 0.8976 0.1482 0.1907 -0.0181 0.3578 -0.0154 837 HOH Z O     
12260 O  O     . HOH T .   ? 0.6719 0.0954 0.1178 -0.1468 0.1859 -0.0208 838 HOH Z O     
12261 O  O     . HOH T .   ? 0.5198 0.0943 0.1663 0.0433  0.2444 0.0134  839 HOH Z O     
12262 O  O     . HOH T .   ? 0.6549 0.1489 0.2259 0.0219  0.3362 0.0018  840 HOH Z O     
12263 O  O     . HOH T .   ? 0.6267 0.1588 0.1886 -0.1456 0.1749 -0.0054 841 HOH Z O     
12264 O  O     . HOH T .   ? 0.4084 0.047  0.1024 -0.0527 0.1523 -0.0218 842 HOH Z O     
12265 O  O     . HOH T .   ? 0.7323 0.1523 0.2174 0.011   0.3482 -0.0059 843 HOH Z O     
12266 O  O     . HOH T .   ? 0.7554 0.3031 0.1872 0.0821  0.3225 0.0312  844 HOH Z O     
12267 O  O     . HOH T .   ? 0.7062 0.1276 0.1783 -0.1966 0.1935 -0.0075 845 HOH Z O     
12268 O  O     . HOH T .   ? 0.4192 0.0421 0.108  -0.0311 0.1612 -0.0132 846 HOH Z O     
12269 O  O     . HOH T .   ? 0.6787 0.2848 0.1288 -0.0418 0.1963 -0.0116 847 HOH Z O     
12270 O  O     . HOH T .   ? 0.614  0.503  0.2042 0.1078  0.2997 0.1084  848 HOH Z O     
12271 O  O     . HOH T .   ? 0.8635 0.1634 0.1863 -0.0036 0.3446 -0.0131 849 HOH Z O     
12272 O  O     . HOH T .   ? 0.4728 0.1169 0.1513 -0.0101 0.2184 0.002   850 HOH Z O     
12273 O  O     . HOH T .   ? 0.7162 0.2313 0.2423 0.0377  0.3176 -0.0055 851 HOH Z O     
12274 O  O     . HOH T .   ? 0.5977 0.1514 0.1196 -0.0241 0.2097 -0.0138 852 HOH Z O     
12275 O  O     . HOH T .   ? 0.5607 0.4569 0.1939 -0.019  0.2079 0.0505  853 HOH Z O     
12276 O  O     . HOH T .   ? 0.6286 0.1179 0.2169 -0.0391 0.3132 0.0063  854 HOH Z O     
12277 O  O     . HOH T .   ? 0.4826 0.6175 0.1528 0.0006  0.1916 0.1305  855 HOH Z O     
12278 O  O     . HOH T .   ? 0.6991 0.3004 0.2232 0.0827  0.315  0.0099  856 HOH Z O     
12279 O  O     . HOH T .   ? 0.6882 0.1791 0.1368 -0.0098 0.249  -0.0086 857 HOH Z O     
12280 O  O     . HOH T .   ? 0.7865 0.1546 0.1552 -0.0238 0.2917 -0.0158 858 HOH Z O     
12281 O  O     . HOH T .   ? 0.488  0.1454 0.1787 -0.0166 0.226  0.0106  859 HOH Z O     
12282 O  O     . HOH T .   ? 0.64   0.3218 0.1873 0.089   0.2949 0.0301  860 HOH Z O     
12283 O  O     . HOH T .   ? 0.612  0.4441 0.1548 0.1026  0.2547 0.0531  861 HOH Z O     
12284 O  O     . HOH T .   ? 0.5243 0.3729 0.1082 -0.0743 0.1698 0.0246  862 HOH Z O     
12285 O  O     . HOH T .   ? 0.7774 0.421  0.379  0.0159  0.2411 -0.0084 863 HOH Z O     
12286 O  O     . HOH T .   ? 0.4187 0.0801 0.1319 -0.0421 0.1812 -0.006  864 HOH Z O     
12287 O  O     . HOH T .   ? 0.5366 0.1171 0.1776 0.0443  0.2586 0.0094  865 HOH Z O     
12288 O  O     . HOH T .   ? 0.4316 0.1151 0.1217 0.0021  0.1791 0.0001  866 HOH Z O     
12289 O  O     . HOH T .   ? 0.5473 0.1811 0.2323 0.0216  0.2574 0.0271  867 HOH Z O     
12290 O  O     . HOH T .   ? 0.554  0.2513 0.1592 -0.0381 0.2017 -0.011  868 HOH Z O     
12291 O  O     . HOH T .   ? 0.4613 0.0469 0.1384 0.0096  0.2039 0.005   869 HOH Z O     
12292 O  O     . HOH T .   ? 0.5199 0.1663 0.173  -0.0863 0.1631 0.0005  870 HOH Z O     
12293 O  O     . HOH T .   ? 0.3884 0.041  0.1143 -0.0233 0.1617 -0.0108 871 HOH Z O     
12294 O  O     . HOH T .   ? 0.4853 0.0651 0.1638 0.0365  0.2344 0.016   872 HOH Z O     
12295 O  O     . HOH T .   ? 0.7357 0.3131 0.1829 -0.03   0.207  -0.0133 873 HOH Z O     
12296 O  O     . HOH T .   ? 0.6533 0.206  0.2021 0.0648  0.3087 0.0037  874 HOH Z O     
12297 O  O     . HOH T .   ? 0.5803 0.1226 0.2254 -0.0312 0.304  0.0159  875 HOH Z O     
12298 O  O     . HOH T .   ? 0.7104 0.2063 0.2353 0.0705  0.3519 -0.0004 876 HOH Z O     
12299 O  O     . HOH T .   ? 0.5602 0.1202 0.204  -0.0431 0.2786 0.01    877 HOH Z O     
12300 O  O     . HOH T .   ? 0.6817 0.1493 0.1212 -0.0404 0.227  -0.0183 878 HOH Z O     
12301 O  O     . HOH T .   ? 0.9143 0.102  0.1528 -0.0962 0.3116 -0.0254 879 HOH Z O     
12302 O  O     . HOH T .   ? 0.4992 0.1074 0.2107 0.0204  0.2785 0.0223  880 HOH Z O     
# 
