data_9EZ5
# 
_entry.id   9EZ5 
# 
_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   9EZ5         pdb_00009ez5 10.2210/pdb9ez5/pdb 
WWPDB D_1292137842 ?            ?                   
# 
_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                        9EZ5 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-10 
_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 
# 
_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 
'Rondelez, Y.' 6  0000-0002-2565-476X 
'Haouz, A.'    7  0000-0003-1196-1635 
'Legrand, P.'  8  0000-0003-2431-2255 
'Sauguet, L.'  9  0000-0002-1259-6601 
'Delarue, M.'  10 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                                   77974.078 1   ? 'E109V, R507D, G509V, E546V' ? ? 
2 polymer     syn 'DNA (Bottom strand)'                  3893.534  1   ? ?                            ? ? 
3 polymer     syn 'DNA (Top strand)'                     4049.661  1   ? ?                            ? ? 
4 non-polymer syn 'CHLORIDE ION'                         35.453    1   ? ?                            ? ? 
5 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' 195.237   1   ? ?                            ? ? 
6 water       nat water                                  18.015    439 ? ?                            ? ? 
# 
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
QKGSFLYETPDVIITSLNNGKEEILMAIVFCSALQAGNQAWQRSGRAYSVGRTGYPYIYIVDFVKYELNNSDRSRKNLRF
PNPAIPYSYISHSKNTGNFIVQAYFRGEEYQPKYDKKLKFFDETIFADDIADYIIAKLQHRDTSNIEQLLINKNLKMVEF
LSKNTKNDNNFTYSEWESIYNGTYRITNLPSLGRFKFRKKIAEKSLSGKVKEFNNIVQRYSVGLASSDLPFGVIRKESRN
DFINDVCKLYNINDMKIIKELKEDADLIVCMLKGFKPRGDDNRPDRGALPLVAMLAGENAQIFTFIYGPLIKGAINLIDQ
DINKLAKRNGLWKSFVSLSDFIVLDCPIIGESYNEFRLIINKNNKESILRKTSKQQNILVDPTPNHYQENDVDTVIYSIF
KYIVPNCFSGMCNPPGGDWSGLSIIDNVHEFRWLSLPRVSENGKRPDHVIQILDLFEKPLLLSIVSKEKPNDLEPKIGVQ
LIKYIEYLFDFTPSVQRKIAGNWEFGNKSLVPNDFILLSAGAFIDYDNLTENDYEKIFEVTGCDLLIAIKNQNNPQKWVI
KFKPKNTIAEKLVNYIKLNFKSNIFDTGFFHIEG
;
;MNVFRIHGDNIIECERVIDLILSKINPQKVKRGFISLSCPFIEIIFKEGHDYFHWRFDMFPGFNKNTNDRWNSNILDLLS
QKGSFLYETPDVIITSLNNGKEEILMAIVFCSALQAGNQAWQRSGRAYSVGRTGYPYIYIVDFVKYELNNSDRSRKNLRF
PNPAIPYSYISHSKNTGNFIVQAYFRGEEYQPKYDKKLKFFDETIFADDIADYIIAKLQHRDTSNIEQLLINKNLKMVEF
LSKNTKNDNNFTYSEWESIYNGTYRITNLPSLGRFKFRKKIAEKSLSGKVKEFNNIVQRYSVGLASSDLPFGVIRKESRN
DFINDVCKLYNINDMKIIKELKEDADLIVCMLKGFKPRGDDNRPDRGALPLVAMLAGENAQIFTFIYGPLIKGAINLIDQ
DINKLAKRNGLWKSFVSLSDFIVLDCPIIGESYNEFRLIINKNNKESILRKTSKQQNILVDPTPNHYQENDVDTVIYSIF
KYIVPNCFSGMCNPPGGDWSGLSIIDNVHEFRWLSLPRVSENGKRPDHVIQILDLFEKPLLLSIVSKEKPNDLEPKIGVQ
LIKYIEYLFDFTPSVQRKIAGNWEFGNKSLVPNDFILLSAGAFIDYDNLTENDYEKIFEVTGCDLLIAIKNQNNPQKWVI
KFKPKNTIAEKLVNYIKLNFKSNIFDTGFFHIEG
;
A ? 
2 polydeoxyribonucleotide no no '(DG)(DT)(DC)(DT)(DG)(DC)(DA)(DT)(DT)(DC)(DC)(DT)(DC)' GTCTGCATTCCTC E ? 
3 polydeoxyribonucleotide no no '(DG)(DA)(DG)(DG)(DA)(DA)(DT)(DG)(DC)(DA)(DG)(DA)(DC)' GAGGAATGCAGAC F ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 'CHLORIDE ION'                         CL  
5 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' MES 
6 water                                  HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   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 VAL 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 ASP n 
1 209 ASP n 
1 210 ILE n 
1 211 ALA n 
1 212 ASP n 
1 213 TYR n 
1 214 ILE n 
1 215 ILE n 
1 216 ALA n 
1 217 LYS n 
1 218 LEU n 
1 219 GLN n 
1 220 HIS n 
1 221 ARG n 
1 222 ASP n 
1 223 THR n 
1 224 SER n 
1 225 ASN n 
1 226 ILE n 
1 227 GLU n 
1 228 GLN n 
1 229 LEU n 
1 230 LEU n 
1 231 ILE n 
1 232 ASN n 
1 233 LYS n 
1 234 ASN n 
1 235 LEU n 
1 236 LYS n 
1 237 MET n 
1 238 VAL n 
1 239 GLU n 
1 240 PHE n 
1 241 LEU n 
1 242 SER n 
1 243 LYS n 
1 244 ASN n 
1 245 THR n 
1 246 LYS n 
1 247 ASN n 
1 248 ASP n 
1 249 ASN n 
1 250 ASN n 
1 251 PHE n 
1 252 THR n 
1 253 TYR n 
1 254 SER n 
1 255 GLU n 
1 256 TRP n 
1 257 GLU n 
1 258 SER n 
1 259 ILE n 
1 260 TYR n 
1 261 ASN n 
1 262 GLY n 
1 263 THR n 
1 264 TYR n 
1 265 ARG n 
1 266 ILE n 
1 267 THR n 
1 268 ASN n 
1 269 LEU n 
1 270 PRO n 
1 271 SER n 
1 272 LEU n 
1 273 GLY n 
1 274 ARG n 
1 275 PHE n 
1 276 LYS n 
1 277 PHE n 
1 278 ARG n 
1 279 LYS n 
1 280 LYS n 
1 281 ILE n 
1 282 ALA n 
1 283 GLU n 
1 284 LYS n 
1 285 SER n 
1 286 LEU n 
1 287 SER n 
1 288 GLY n 
1 289 LYS n 
1 290 VAL n 
1 291 LYS n 
1 292 GLU n 
1 293 PHE n 
1 294 ASN n 
1 295 ASN n 
1 296 ILE n 
1 297 VAL n 
1 298 GLN n 
1 299 ARG n 
1 300 TYR n 
1 301 SER n 
1 302 VAL n 
1 303 GLY n 
1 304 LEU n 
1 305 ALA n 
1 306 SER n 
1 307 SER n 
1 308 ASP n 
1 309 LEU n 
1 310 PRO n 
1 311 PHE n 
1 312 GLY n 
1 313 VAL n 
1 314 ILE n 
1 315 ARG n 
1 316 LYS n 
1 317 GLU n 
1 318 SER n 
1 319 ARG n 
1 320 ASN n 
1 321 ASP n 
1 322 PHE n 
1 323 ILE n 
1 324 ASN n 
1 325 ASP n 
1 326 VAL n 
1 327 CYS n 
1 328 LYS n 
1 329 LEU n 
1 330 TYR n 
1 331 ASN n 
1 332 ILE n 
1 333 ASN n 
1 334 ASP n 
1 335 MET n 
1 336 LYS n 
1 337 ILE n 
1 338 ILE n 
1 339 LYS n 
1 340 GLU n 
1 341 LEU n 
1 342 LYS n 
1 343 GLU n 
1 344 ASP n 
1 345 ALA n 
1 346 ASP n 
1 347 LEU n 
1 348 ILE n 
1 349 VAL n 
1 350 CYS n 
1 351 MET n 
1 352 LEU n 
1 353 LYS n 
1 354 GLY n 
1 355 PHE n 
1 356 LYS n 
1 357 PRO n 
1 358 ARG n 
1 359 GLY n 
1 360 ASP n 
1 361 ASP n 
1 362 ASN n 
1 363 ARG n 
1 364 PRO n 
1 365 ASP n 
1 366 ARG n 
1 367 GLY n 
1 368 ALA n 
1 369 LEU n 
1 370 PRO n 
1 371 LEU n 
1 372 VAL n 
1 373 ALA n 
1 374 MET n 
1 375 LEU n 
1 376 ALA n 
1 377 GLY n 
1 378 GLU n 
1 379 ASN n 
1 380 ALA n 
1 381 GLN n 
1 382 ILE n 
1 383 PHE n 
1 384 THR n 
1 385 PHE n 
1 386 ILE n 
1 387 TYR n 
1 388 GLY n 
1 389 PRO n 
1 390 LEU n 
1 391 ILE n 
1 392 LYS n 
1 393 GLY n 
1 394 ALA n 
1 395 ILE n 
1 396 ASN n 
1 397 LEU n 
1 398 ILE n 
1 399 ASP n 
1 400 GLN n 
1 401 ASP n 
1 402 ILE n 
1 403 ASN n 
1 404 LYS n 
1 405 LEU n 
1 406 ALA n 
1 407 LYS n 
1 408 ARG n 
1 409 ASN n 
1 410 GLY n 
1 411 LEU n 
1 412 TRP n 
1 413 LYS n 
1 414 SER n 
1 415 PHE n 
1 416 VAL n 
1 417 SER n 
1 418 LEU n 
1 419 SER n 
1 420 ASP n 
1 421 PHE n 
1 422 ILE n 
1 423 VAL n 
1 424 LEU n 
1 425 ASP n 
1 426 CYS n 
1 427 PRO n 
1 428 ILE n 
1 429 ILE n 
1 430 GLY n 
1 431 GLU n 
1 432 SER n 
1 433 TYR n 
1 434 ASN n 
1 435 GLU n 
1 436 PHE n 
1 437 ARG n 
1 438 LEU n 
1 439 ILE n 
1 440 ILE n 
1 441 ASN n 
1 442 LYS n 
1 443 ASN n 
1 444 ASN n 
1 445 LYS n 
1 446 GLU n 
1 447 SER n 
1 448 ILE n 
1 449 LEU n 
1 450 ARG n 
1 451 LYS n 
1 452 THR n 
1 453 SER n 
1 454 LYS n 
1 455 GLN n 
1 456 GLN n 
1 457 ASN n 
1 458 ILE n 
1 459 LEU n 
1 460 VAL n 
1 461 ASP n 
1 462 PRO n 
1 463 THR n 
1 464 PRO n 
1 465 ASN n 
1 466 HIS n 
1 467 TYR n 
1 468 GLN n 
1 469 GLU n 
1 470 ASN n 
1 471 ASP n 
1 472 VAL n 
1 473 ASP n 
1 474 THR n 
1 475 VAL n 
1 476 ILE n 
1 477 TYR n 
1 478 SER n 
1 479 ILE n 
1 480 PHE n 
1 481 LYS n 
1 482 TYR n 
1 483 ILE n 
1 484 VAL n 
1 485 PRO n 
1 486 ASN n 
1 487 CYS n 
1 488 PHE n 
1 489 SER n 
1 490 GLY n 
1 491 MET n 
1 492 CYS n 
1 493 ASN n 
1 494 PRO n 
1 495 PRO n 
1 496 GLY n 
1 497 GLY n 
1 498 ASP n 
1 499 TRP n 
1 500 SER n 
1 501 GLY n 
1 502 LEU n 
1 503 SER n 
1 504 ILE n 
1 505 ILE n 
1 506 ASP n 
1 507 ASN n 
1 508 VAL n 
1 509 HIS n 
1 510 GLU n 
1 511 PHE n 
1 512 ARG n 
1 513 TRP n 
1 514 LEU n 
1 515 SER n 
1 516 LEU n 
1 517 PRO n 
1 518 ARG n 
1 519 VAL n 
1 520 SER n 
1 521 GLU n 
1 522 ASN n 
1 523 GLY n 
1 524 LYS n 
1 525 ARG n 
1 526 PRO n 
1 527 ASP n 
1 528 HIS n 
1 529 VAL n 
1 530 ILE n 
1 531 GLN n 
1 532 ILE n 
1 533 LEU n 
1 534 ASP n 
1 535 LEU n 
1 536 PHE n 
1 537 GLU n 
1 538 LYS n 
1 539 PRO n 
1 540 LEU n 
1 541 LEU n 
1 542 LEU n 
1 543 SER n 
1 544 ILE n 
1 545 VAL n 
1 546 SER n 
1 547 LYS n 
1 548 GLU n 
1 549 LYS n 
1 550 PRO n 
1 551 ASN n 
1 552 ASP n 
1 553 LEU n 
1 554 GLU n 
1 555 PRO n 
1 556 LYS n 
1 557 ILE n 
1 558 GLY n 
1 559 VAL n 
1 560 GLN n 
1 561 LEU n 
1 562 ILE n 
1 563 LYS n 
1 564 TYR n 
1 565 ILE n 
1 566 GLU n 
1 567 TYR n 
1 568 LEU n 
1 569 PHE n 
1 570 ASP n 
1 571 PHE n 
1 572 THR n 
1 573 PRO n 
1 574 SER n 
1 575 VAL n 
1 576 GLN n 
1 577 ARG n 
1 578 LYS n 
1 579 ILE n 
1 580 ALA n 
1 581 GLY n 
1 582 ASN n 
1 583 TRP n 
1 584 GLU n 
1 585 PHE n 
1 586 GLY n 
1 587 ASN n 
1 588 LYS n 
1 589 SER n 
1 590 LEU n 
1 591 VAL n 
1 592 PRO n 
1 593 ASN n 
1 594 ASP n 
1 595 PHE n 
1 596 ILE n 
1 597 LEU n 
1 598 LEU n 
1 599 SER n 
1 600 ALA n 
1 601 GLY n 
1 602 ALA n 
1 603 PHE n 
1 604 ILE n 
1 605 ASP n 
1 606 TYR n 
1 607 ASP n 
1 608 ASN n 
1 609 LEU n 
1 610 THR n 
1 611 GLU n 
1 612 ASN n 
1 613 ASP n 
1 614 TYR n 
1 615 GLU n 
1 616 LYS n 
1 617 ILE n 
1 618 PHE n 
1 619 GLU n 
1 620 VAL n 
1 621 THR n 
1 622 GLY n 
1 623 CYS n 
1 624 ASP n 
1 625 LEU n 
1 626 LEU n 
1 627 ILE n 
1 628 ALA n 
1 629 ILE n 
1 630 LYS n 
1 631 ASN n 
1 632 GLN n 
1 633 ASN n 
1 634 ASN n 
1 635 PRO n 
1 636 GLN n 
1 637 LYS n 
1 638 TRP n 
1 639 VAL n 
1 640 ILE n 
1 641 LYS n 
1 642 PHE n 
1 643 LYS n 
1 644 PRO n 
1 645 LYS n 
1 646 ASN n 
1 647 THR n 
1 648 ILE n 
1 649 ALA n 
1 650 GLU n 
1 651 LYS n 
1 652 LEU n 
1 653 VAL n 
1 654 ASN n 
1 655 TYR n 
1 656 ILE n 
1 657 LYS n 
1 658 LEU n 
1 659 ASN n 
1 660 PHE n 
1 661 LYS n 
1 662 SER n 
1 663 ASN n 
1 664 ILE n 
1 665 PHE n 
1 666 ASP n 
1 667 THR n 
1 668 GLY n 
1 669 PHE n 
1 670 PHE n 
1 671 HIS n 
1 672 ILE n 
1 673 GLU n 
1 674 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                   674 
_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 
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 VAL 109 109 109 VAL VAL 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 ASP 208 209 209 ASP ASP A . n 
A 1 209 ASP 209 210 210 ASP ASP A . n 
A 1 210 ILE 210 211 211 ILE ILE A . n 
A 1 211 ALA 211 212 212 ALA ALA A . n 
A 1 212 ASP 212 213 213 ASP ASP A . n 
A 1 213 TYR 213 214 214 TYR TYR A . n 
A 1 214 ILE 214 215 215 ILE ILE A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 ALA 216 217 217 ALA ALA A . n 
A 1 217 LYS 217 218 218 LYS LYS A . n 
A 1 218 LEU 218 219 219 LEU LEU A . n 
A 1 219 GLN 219 220 220 GLN GLN A . n 
A 1 220 HIS 220 221 221 HIS HIS A . n 
A 1 221 ARG 221 222 222 ARG ARG A . n 
A 1 222 ASP 222 223 223 ASP ASP A . n 
A 1 223 THR 223 224 224 THR THR A . n 
A 1 224 SER 224 225 225 SER SER A . n 
A 1 225 ASN 225 226 226 ASN ASN A . n 
A 1 226 ILE 226 227 227 ILE ILE A . n 
A 1 227 GLU 227 228 228 GLU GLU A . n 
A 1 228 GLN 228 229 229 GLN GLN A . n 
A 1 229 LEU 229 230 230 LEU LEU A . n 
A 1 230 LEU 230 231 231 LEU LEU A . n 
A 1 231 ILE 231 232 232 ILE ILE A . n 
A 1 232 ASN 232 233 233 ASN ASN A . n 
A 1 233 LYS 233 234 234 LYS LYS A . n 
A 1 234 ASN 234 235 235 ASN ASN A . n 
A 1 235 LEU 235 236 236 LEU LEU A . n 
A 1 236 LYS 236 237 237 LYS LYS A . n 
A 1 237 MET 237 238 238 MET MET A . n 
A 1 238 VAL 238 239 239 VAL VAL A . n 
A 1 239 GLU 239 240 240 GLU GLU A . n 
A 1 240 PHE 240 241 241 PHE PHE A . n 
A 1 241 LEU 241 242 242 LEU LEU A . n 
A 1 242 SER 242 243 243 SER SER A . n 
A 1 243 LYS 243 244 244 LYS LYS A . n 
A 1 244 ASN 244 245 245 ASN ASN A . n 
A 1 245 THR 245 246 246 THR THR A . n 
A 1 246 LYS 246 247 247 LYS LYS A . n 
A 1 247 ASN 247 248 248 ASN ASN A . n 
A 1 248 ASP 248 249 249 ASP ASP A . n 
A 1 249 ASN 249 250 250 ASN ASN A . n 
A 1 250 ASN 250 251 251 ASN ASN A . n 
A 1 251 PHE 251 252 252 PHE PHE A . n 
A 1 252 THR 252 253 253 THR THR A . n 
A 1 253 TYR 253 254 254 TYR TYR A . n 
A 1 254 SER 254 255 255 SER SER A . n 
A 1 255 GLU 255 256 256 GLU GLU A . n 
A 1 256 TRP 256 257 257 TRP TRP A . n 
A 1 257 GLU 257 258 258 GLU GLU A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 ILE 259 260 260 ILE ILE A . n 
A 1 260 TYR 260 261 261 TYR TYR A . n 
A 1 261 ASN 261 262 262 ASN ASN A . n 
A 1 262 GLY 262 263 263 GLY GLY A . n 
A 1 263 THR 263 264 264 THR THR A . n 
A 1 264 TYR 264 265 265 TYR TYR A . n 
A 1 265 ARG 265 266 266 ARG ARG A . n 
A 1 266 ILE 266 267 267 ILE ILE A . n 
A 1 267 THR 267 268 268 THR THR A . n 
A 1 268 ASN 268 269 269 ASN ASN A . n 
A 1 269 LEU 269 270 270 LEU LEU A . n 
A 1 270 PRO 270 271 271 PRO PRO A . n 
A 1 271 SER 271 272 272 SER SER A . n 
A 1 272 LEU 272 273 273 LEU LEU A . n 
A 1 273 GLY 273 274 274 GLY GLY A . n 
A 1 274 ARG 274 275 275 ARG ARG A . n 
A 1 275 PHE 275 276 276 PHE PHE A . n 
A 1 276 LYS 276 277 277 LYS LYS A . n 
A 1 277 PHE 277 278 278 PHE PHE A . n 
A 1 278 ARG 278 279 279 ARG ARG A . n 
A 1 279 LYS 279 280 280 LYS LYS A . n 
A 1 280 LYS 280 281 281 LYS LYS A . n 
A 1 281 ILE 281 282 282 ILE ILE A . n 
A 1 282 ALA 282 283 283 ALA ALA A . n 
A 1 283 GLU 283 284 284 GLU GLU A . n 
A 1 284 LYS 284 285 285 LYS LYS A . n 
A 1 285 SER 285 286 286 SER SER A . n 
A 1 286 LEU 286 287 287 LEU LEU A . n 
A 1 287 SER 287 288 288 SER SER A . n 
A 1 288 GLY 288 289 289 GLY GLY A . n 
A 1 289 LYS 289 290 290 LYS LYS A . n 
A 1 290 VAL 290 291 291 VAL VAL A . n 
A 1 291 LYS 291 292 292 LYS LYS A . n 
A 1 292 GLU 292 293 293 GLU GLU A . n 
A 1 293 PHE 293 294 294 PHE PHE A . n 
A 1 294 ASN 294 295 295 ASN ASN A . n 
A 1 295 ASN 295 296 296 ASN ASN A . n 
A 1 296 ILE 296 297 297 ILE ILE A . n 
A 1 297 VAL 297 298 298 VAL VAL A . n 
A 1 298 GLN 298 299 299 GLN GLN A . n 
A 1 299 ARG 299 300 300 ARG ARG A . n 
A 1 300 TYR 300 301 301 TYR TYR A . n 
A 1 301 SER 301 302 302 SER SER A . n 
A 1 302 VAL 302 303 303 VAL VAL A . n 
A 1 303 GLY 303 304 304 GLY GLY A . n 
A 1 304 LEU 304 305 305 LEU LEU A . n 
A 1 305 ALA 305 306 306 ALA ALA A . n 
A 1 306 SER 306 307 307 SER SER A . n 
A 1 307 SER 307 308 308 SER SER A . n 
A 1 308 ASP 308 309 309 ASP ASP A . n 
A 1 309 LEU 309 310 310 LEU LEU A . n 
A 1 310 PRO 310 311 311 PRO PRO A . n 
A 1 311 PHE 311 312 312 PHE PHE A . n 
A 1 312 GLY 312 313 313 GLY GLY A . n 
A 1 313 VAL 313 314 314 VAL VAL A . n 
A 1 314 ILE 314 315 315 ILE ILE A . n 
A 1 315 ARG 315 316 316 ARG ARG A . n 
A 1 316 LYS 316 317 317 LYS LYS A . n 
A 1 317 GLU 317 318 318 GLU GLU A . n 
A 1 318 SER 318 319 319 SER SER A . n 
A 1 319 ARG 319 320 320 ARG ARG A . n 
A 1 320 ASN 320 321 321 ASN ASN A . n 
A 1 321 ASP 321 322 322 ASP ASP A . n 
A 1 322 PHE 322 323 323 PHE PHE A . n 
A 1 323 ILE 323 324 324 ILE ILE A . n 
A 1 324 ASN 324 325 325 ASN ASN A . n 
A 1 325 ASP 325 326 326 ASP ASP A . n 
A 1 326 VAL 326 327 327 VAL VAL A . n 
A 1 327 CYS 327 328 328 CYS CYS A . n 
A 1 328 LYS 328 329 329 LYS LYS A . n 
A 1 329 LEU 329 330 330 LEU LEU A . n 
A 1 330 TYR 330 331 331 TYR TYR A . n 
A 1 331 ASN 331 332 332 ASN ASN A . n 
A 1 332 ILE 332 333 333 ILE ILE A . n 
A 1 333 ASN 333 334 334 ASN ASN A . n 
A 1 334 ASP 334 335 335 ASP ASP A . n 
A 1 335 MET 335 336 336 MET MET A . n 
A 1 336 LYS 336 337 337 LYS LYS A . n 
A 1 337 ILE 337 338 338 ILE ILE A . n 
A 1 338 ILE 338 339 339 ILE ILE A . n 
A 1 339 LYS 339 340 340 LYS LYS A . n 
A 1 340 GLU 340 341 341 GLU GLU A . n 
A 1 341 LEU 341 342 342 LEU LEU A . n 
A 1 342 LYS 342 343 343 LYS LYS A . n 
A 1 343 GLU 343 344 344 GLU GLU A . n 
A 1 344 ASP 344 345 345 ASP ASP A . n 
A 1 345 ALA 345 346 346 ALA ALA A . n 
A 1 346 ASP 346 347 347 ASP ASP A . n 
A 1 347 LEU 347 348 348 LEU LEU A . n 
A 1 348 ILE 348 349 349 ILE ILE A . n 
A 1 349 VAL 349 350 350 VAL VAL A . n 
A 1 350 CYS 350 351 351 CYS CYS A . n 
A 1 351 MET 351 352 352 MET MET A . n 
A 1 352 LEU 352 353 353 LEU LEU A . n 
A 1 353 LYS 353 354 354 LYS LYS A . n 
A 1 354 GLY 354 355 355 GLY GLY A . n 
A 1 355 PHE 355 356 356 PHE PHE A . n 
A 1 356 LYS 356 357 357 LYS LYS A . n 
A 1 357 PRO 357 358 358 PRO PRO A . n 
A 1 358 ARG 358 359 359 ARG ARG A . n 
A 1 359 GLY 359 360 360 GLY GLY A . n 
A 1 360 ASP 360 361 361 ASP ASP A . n 
A 1 361 ASP 361 362 362 ASP ASP A . n 
A 1 362 ASN 362 363 363 ASN ASN A . n 
A 1 363 ARG 363 364 364 ARG ARG A . n 
A 1 364 PRO 364 365 365 PRO PRO A . n 
A 1 365 ASP 365 366 366 ASP ASP A . n 
A 1 366 ARG 366 367 367 ARG ARG A . n 
A 1 367 GLY 367 368 368 GLY GLY A . n 
A 1 368 ALA 368 369 369 ALA ALA A . n 
A 1 369 LEU 369 370 370 LEU LEU A . n 
A 1 370 PRO 370 371 371 PRO PRO A . n 
A 1 371 LEU 371 372 372 LEU LEU A . n 
A 1 372 VAL 372 373 373 VAL VAL A . n 
A 1 373 ALA 373 374 374 ALA ALA A . n 
A 1 374 MET 374 375 375 MET MET A . n 
A 1 375 LEU 375 376 376 LEU LEU A . n 
A 1 376 ALA 376 377 377 ALA ALA A . n 
A 1 377 GLY 377 378 378 GLY GLY A . n 
A 1 378 GLU 378 379 379 GLU GLU A . n 
A 1 379 ASN 379 380 380 ASN ASN A . n 
A 1 380 ALA 380 381 381 ALA ALA A . n 
A 1 381 GLN 381 382 382 GLN GLN A . n 
A 1 382 ILE 382 383 383 ILE ILE A . n 
A 1 383 PHE 383 384 384 PHE PHE A . n 
A 1 384 THR 384 385 385 THR THR A . n 
A 1 385 PHE 385 386 386 PHE PHE A . n 
A 1 386 ILE 386 387 387 ILE ILE A . n 
A 1 387 TYR 387 388 388 TYR TYR A . n 
A 1 388 GLY 388 389 389 GLY GLY A . n 
A 1 389 PRO 389 390 390 PRO PRO A . n 
A 1 390 LEU 390 391 391 LEU LEU A . n 
A 1 391 ILE 391 392 392 ILE ILE A . n 
A 1 392 LYS 392 393 393 LYS LYS A . n 
A 1 393 GLY 393 394 394 GLY GLY A . n 
A 1 394 ALA 394 395 395 ALA ALA A . n 
A 1 395 ILE 395 396 396 ILE ILE A . n 
A 1 396 ASN 396 397 397 ASN ASN A . n 
A 1 397 LEU 397 398 398 LEU LEU A . n 
A 1 398 ILE 398 399 399 ILE ILE A . n 
A 1 399 ASP 399 400 400 ASP ASP A . n 
A 1 400 GLN 400 401 401 GLN GLN A . n 
A 1 401 ASP 401 402 402 ASP ASP A . n 
A 1 402 ILE 402 403 403 ILE ILE A . n 
A 1 403 ASN 403 404 404 ASN ASN A . n 
A 1 404 LYS 404 405 405 LYS LYS A . n 
A 1 405 LEU 405 406 406 LEU LEU A . n 
A 1 406 ALA 406 407 407 ALA ALA A . n 
A 1 407 LYS 407 408 408 LYS LYS A . n 
A 1 408 ARG 408 409 409 ARG ARG A . n 
A 1 409 ASN 409 410 410 ASN ASN A . n 
A 1 410 GLY 410 411 411 GLY GLY A . n 
A 1 411 LEU 411 412 412 LEU LEU A . n 
A 1 412 TRP 412 413 413 TRP TRP A . n 
A 1 413 LYS 413 414 414 LYS LYS A . n 
A 1 414 SER 414 415 415 SER SER A . n 
A 1 415 PHE 415 416 416 PHE PHE A . n 
A 1 416 VAL 416 417 417 VAL VAL A . n 
A 1 417 SER 417 418 418 SER SER A . n 
A 1 418 LEU 418 419 419 LEU LEU A . n 
A 1 419 SER 419 420 420 SER SER A . n 
A 1 420 ASP 420 421 421 ASP ASP A . n 
A 1 421 PHE 421 422 422 PHE PHE A . n 
A 1 422 ILE 422 423 423 ILE ILE A . n 
A 1 423 VAL 423 424 424 VAL VAL A . n 
A 1 424 LEU 424 425 425 LEU LEU A . n 
A 1 425 ASP 425 426 426 ASP ASP A . n 
A 1 426 CYS 426 427 427 CYS CYS A . n 
A 1 427 PRO 427 428 428 PRO PRO A . n 
A 1 428 ILE 428 429 429 ILE ILE A . n 
A 1 429 ILE 429 430 430 ILE ILE A . n 
A 1 430 GLY 430 431 431 GLY GLY A . n 
A 1 431 GLU 431 432 432 GLU GLU A . n 
A 1 432 SER 432 433 433 SER SER A . n 
A 1 433 TYR 433 434 434 TYR TYR A . n 
A 1 434 ASN 434 435 435 ASN ASN A . n 
A 1 435 GLU 435 436 436 GLU GLU A . n 
A 1 436 PHE 436 437 437 PHE PHE A . n 
A 1 437 ARG 437 438 438 ARG ARG A . n 
A 1 438 LEU 438 439 439 LEU LEU A . n 
A 1 439 ILE 439 440 440 ILE ILE A . n 
A 1 440 ILE 440 441 441 ILE ILE A . n 
A 1 441 ASN 441 442 442 ASN ASN A . n 
A 1 442 LYS 442 443 443 LYS LYS A . n 
A 1 443 ASN 443 444 444 ASN ASN A . n 
A 1 444 ASN 444 445 445 ASN ASN A . n 
A 1 445 LYS 445 446 446 LYS LYS A . n 
A 1 446 GLU 446 447 447 GLU GLU A . n 
A 1 447 SER 447 448 448 SER SER A . n 
A 1 448 ILE 448 449 449 ILE ILE A . n 
A 1 449 LEU 449 450 450 LEU LEU A . n 
A 1 450 ARG 450 451 451 ARG ARG A . n 
A 1 451 LYS 451 452 452 LYS LYS A . n 
A 1 452 THR 452 453 453 THR THR A . n 
A 1 453 SER 453 454 454 SER SER A . n 
A 1 454 LYS 454 455 455 LYS LYS A . n 
A 1 455 GLN 455 456 456 GLN GLN A . n 
A 1 456 GLN 456 457 457 GLN GLN A . n 
A 1 457 ASN 457 458 458 ASN ASN A . n 
A 1 458 ILE 458 459 459 ILE ILE A . n 
A 1 459 LEU 459 460 460 LEU LEU A . n 
A 1 460 VAL 460 461 461 VAL VAL A . n 
A 1 461 ASP 461 462 462 ASP ASP A . n 
A 1 462 PRO 462 463 463 PRO PRO A . n 
A 1 463 THR 463 464 464 THR THR A . n 
A 1 464 PRO 464 465 465 PRO PRO A . n 
A 1 465 ASN 465 466 466 ASN ASN A . n 
A 1 466 HIS 466 467 467 HIS HIS A . n 
A 1 467 TYR 467 468 468 TYR TYR A . n 
A 1 468 GLN 468 469 469 GLN GLN A . n 
A 1 469 GLU 469 470 470 GLU GLU A . n 
A 1 470 ASN 470 471 471 ASN ASN A . n 
A 1 471 ASP 471 472 472 ASP ASP A . n 
A 1 472 VAL 472 473 473 VAL VAL A . n 
A 1 473 ASP 473 474 474 ASP ASP A . n 
A 1 474 THR 474 475 475 THR THR A . n 
A 1 475 VAL 475 476 476 VAL VAL A . n 
A 1 476 ILE 476 477 477 ILE ILE A . n 
A 1 477 TYR 477 478 478 TYR TYR A . n 
A 1 478 SER 478 479 479 SER SER A . n 
A 1 479 ILE 479 480 480 ILE ILE A . n 
A 1 480 PHE 480 481 481 PHE PHE A . n 
A 1 481 LYS 481 482 482 LYS LYS A . n 
A 1 482 TYR 482 483 483 TYR TYR A . n 
A 1 483 ILE 483 484 484 ILE ILE A . n 
A 1 484 VAL 484 485 485 VAL VAL A . n 
A 1 485 PRO 485 486 486 PRO PRO A . n 
A 1 486 ASN 486 487 487 ASN ASN A . n 
A 1 487 CYS 487 488 488 CYS CYS A . n 
A 1 488 PHE 488 489 489 PHE PHE A . n 
A 1 489 SER 489 490 490 SER SER A . n 
A 1 490 GLY 490 491 491 GLY GLY A . n 
A 1 491 MET 491 492 492 MET MET A . n 
A 1 492 CYS 492 493 493 CYS CYS A . n 
A 1 493 ASN 493 494 494 ASN ASN A . n 
A 1 494 PRO 494 495 495 PRO PRO A . n 
A 1 495 PRO 495 496 496 PRO PRO A . n 
A 1 496 GLY 496 497 497 GLY GLY A . n 
A 1 497 GLY 497 498 498 GLY GLY A . n 
A 1 498 ASP 498 499 499 ASP ASP A . n 
A 1 499 TRP 499 500 500 TRP TRP A . n 
A 1 500 SER 500 501 501 SER SER A . n 
A 1 501 GLY 501 502 502 GLY GLY A . n 
A 1 502 LEU 502 503 503 LEU LEU A . n 
A 1 503 SER 503 504 504 SER SER A . n 
A 1 504 ILE 504 505 505 ILE ILE A . n 
A 1 505 ILE 505 506 506 ILE ILE A . n 
A 1 506 ASP 506 507 507 ASP ASP A . n 
A 1 507 ASN 507 508 508 ASN ASN A . n 
A 1 508 VAL 508 509 509 VAL VAL A . n 
A 1 509 HIS 509 510 510 HIS HIS A . n 
A 1 510 GLU 510 511 511 GLU GLU A . n 
A 1 511 PHE 511 512 512 PHE PHE A . n 
A 1 512 ARG 512 513 513 ARG ARG A . n 
A 1 513 TRP 513 514 514 TRP TRP A . n 
A 1 514 LEU 514 515 515 LEU LEU A . n 
A 1 515 SER 515 516 516 SER SER A . n 
A 1 516 LEU 516 517 517 LEU LEU A . n 
A 1 517 PRO 517 518 518 PRO PRO A . n 
A 1 518 ARG 518 519 519 ARG ARG A . n 
A 1 519 VAL 519 520 520 VAL VAL A . n 
A 1 520 SER 520 521 521 SER SER A . n 
A 1 521 GLU 521 522 522 GLU GLU A . n 
A 1 522 ASN 522 523 523 ASN ASN A . n 
A 1 523 GLY 523 524 524 GLY GLY A . n 
A 1 524 LYS 524 525 525 LYS LYS A . n 
A 1 525 ARG 525 526 526 ARG ARG A . n 
A 1 526 PRO 526 527 527 PRO PRO A . n 
A 1 527 ASP 527 528 528 ASP ASP A . n 
A 1 528 HIS 528 529 529 HIS HIS A . n 
A 1 529 VAL 529 530 530 VAL VAL A . n 
A 1 530 ILE 530 531 531 ILE ILE A . n 
A 1 531 GLN 531 532 532 GLN GLN A . n 
A 1 532 ILE 532 533 533 ILE ILE A . n 
A 1 533 LEU 533 534 534 LEU LEU A . n 
A 1 534 ASP 534 535 535 ASP ASP A . n 
A 1 535 LEU 535 536 536 LEU LEU A . n 
A 1 536 PHE 536 537 537 PHE PHE A . n 
A 1 537 GLU 537 538 538 GLU GLU A . n 
A 1 538 LYS 538 539 539 LYS LYS A . n 
A 1 539 PRO 539 540 540 PRO PRO A . n 
A 1 540 LEU 540 541 541 LEU LEU A . n 
A 1 541 LEU 541 542 542 LEU LEU A . n 
A 1 542 LEU 542 543 543 LEU LEU A . n 
A 1 543 SER 543 544 544 SER SER A . n 
A 1 544 ILE 544 545 545 ILE ILE A . n 
A 1 545 VAL 545 546 546 VAL VAL A . n 
A 1 546 SER 546 547 547 SER SER A . n 
A 1 547 LYS 547 548 548 LYS LYS A . n 
A 1 548 GLU 548 549 549 GLU GLU A . n 
A 1 549 LYS 549 550 550 LYS LYS A . n 
A 1 550 PRO 550 551 551 PRO PRO A . n 
A 1 551 ASN 551 552 552 ASN ASN A . n 
A 1 552 ASP 552 553 553 ASP ASP A . n 
A 1 553 LEU 553 554 554 LEU LEU A . n 
A 1 554 GLU 554 555 555 GLU GLU A . n 
A 1 555 PRO 555 556 556 PRO PRO A . n 
A 1 556 LYS 556 557 557 LYS LYS A . n 
A 1 557 ILE 557 558 558 ILE ILE A . n 
A 1 558 GLY 558 559 559 GLY GLY A . n 
A 1 559 VAL 559 560 560 VAL VAL A . n 
A 1 560 GLN 560 561 561 GLN GLN A . n 
A 1 561 LEU 561 562 562 LEU LEU A . n 
A 1 562 ILE 562 563 563 ILE ILE A . n 
A 1 563 LYS 563 564 564 LYS LYS A . n 
A 1 564 TYR 564 565 565 TYR TYR A . n 
A 1 565 ILE 565 566 566 ILE ILE A . n 
A 1 566 GLU 566 567 567 GLU GLU A . n 
A 1 567 TYR 567 568 568 TYR TYR A . n 
A 1 568 LEU 568 569 569 LEU LEU A . n 
A 1 569 PHE 569 570 570 PHE PHE A . n 
A 1 570 ASP 570 571 571 ASP ASP A . n 
A 1 571 PHE 571 572 572 PHE PHE A . n 
A 1 572 THR 572 573 573 THR THR A . n 
A 1 573 PRO 573 574 574 PRO PRO A . n 
A 1 574 SER 574 575 575 SER SER A . n 
A 1 575 VAL 575 576 576 VAL VAL A . n 
A 1 576 GLN 576 577 577 GLN GLN A . n 
A 1 577 ARG 577 578 578 ARG ARG A . n 
A 1 578 LYS 578 579 579 LYS LYS A . n 
A 1 579 ILE 579 580 580 ILE ILE A . n 
A 1 580 ALA 580 581 581 ALA ALA A . n 
A 1 581 GLY 581 582 582 GLY GLY A . n 
A 1 582 ASN 582 584 584 ASN ASN A . n 
A 1 583 TRP 583 585 585 TRP TRP A . n 
A 1 584 GLU 584 586 586 GLU GLU A . n 
A 1 585 PHE 585 587 587 PHE PHE A . n 
A 1 586 GLY 586 588 588 GLY GLY A . n 
A 1 587 ASN 587 589 589 ASN ASN A . n 
A 1 588 LYS 588 590 590 LYS LYS A . n 
A 1 589 SER 589 591 591 SER SER A . n 
A 1 590 LEU 590 592 592 LEU LEU A . n 
A 1 591 VAL 591 593 593 VAL VAL A . n 
A 1 592 PRO 592 594 594 PRO PRO A . n 
A 1 593 ASN 593 595 595 ASN ASN A . n 
A 1 594 ASP 594 596 596 ASP ASP A . n 
A 1 595 PHE 595 597 597 PHE PHE A . n 
A 1 596 ILE 596 598 598 ILE ILE A . n 
A 1 597 LEU 597 599 599 LEU LEU A . n 
A 1 598 LEU 598 600 600 LEU LEU A . n 
A 1 599 SER 599 601 601 SER SER A . n 
A 1 600 ALA 600 602 602 ALA ALA A . n 
A 1 601 GLY 601 603 603 GLY GLY A . n 
A 1 602 ALA 602 604 604 ALA ALA A . n 
A 1 603 PHE 603 605 605 PHE PHE A . n 
A 1 604 ILE 604 606 606 ILE ILE A . n 
A 1 605 ASP 605 607 607 ASP ASP A . n 
A 1 606 TYR 606 608 608 TYR TYR A . n 
A 1 607 ASP 607 609 609 ASP ASP A . n 
A 1 608 ASN 608 610 610 ASN ASN A . n 
A 1 609 LEU 609 611 611 LEU LEU A . n 
A 1 610 THR 610 612 612 THR THR A . n 
A 1 611 GLU 611 613 613 GLU GLU A . n 
A 1 612 ASN 612 614 614 ASN ASN A . n 
A 1 613 ASP 613 615 615 ASP ASP A . n 
A 1 614 TYR 614 616 616 TYR TYR A . n 
A 1 615 GLU 615 617 617 GLU GLU A . n 
A 1 616 LYS 616 618 618 LYS LYS A . n 
A 1 617 ILE 617 619 619 ILE ILE A . n 
A 1 618 PHE 618 620 620 PHE PHE A . n 
A 1 619 GLU 619 621 621 GLU GLU A . n 
A 1 620 VAL 620 622 622 VAL VAL A . n 
A 1 621 THR 621 623 623 THR THR A . n 
A 1 622 GLY 622 624 624 GLY GLY A . n 
A 1 623 CYS 623 625 625 CYS CYS A . n 
A 1 624 ASP 624 626 626 ASP ASP A . n 
A 1 625 LEU 625 627 627 LEU LEU A . n 
A 1 626 LEU 626 628 628 LEU LEU A . n 
A 1 627 ILE 627 629 629 ILE ILE A . n 
A 1 628 ALA 628 630 630 ALA ALA A . n 
A 1 629 ILE 629 631 631 ILE ILE A . n 
A 1 630 LYS 630 632 632 LYS LYS A . n 
A 1 631 ASN 631 633 633 ASN ASN A . n 
A 1 632 GLN 632 634 634 GLN GLN A . n 
A 1 633 ASN 633 635 635 ASN ASN A . n 
A 1 634 ASN 634 636 636 ASN ASN A . n 
A 1 635 PRO 635 637 637 PRO PRO A . n 
A 1 636 GLN 636 638 638 GLN GLN A . n 
A 1 637 LYS 637 639 639 LYS LYS A . n 
A 1 638 TRP 638 640 640 TRP TRP A . n 
A 1 639 VAL 639 641 641 VAL VAL A . n 
A 1 640 ILE 640 642 642 ILE ILE A . n 
A 1 641 LYS 641 643 643 LYS LYS A . n 
A 1 642 PHE 642 644 644 PHE PHE A . n 
A 1 643 LYS 643 645 645 LYS LYS A . n 
A 1 644 PRO 644 646 646 PRO PRO A . n 
A 1 645 LYS 645 647 647 LYS LYS A . n 
A 1 646 ASN 646 648 648 ASN ASN A . n 
A 1 647 THR 647 649 649 THR THR A . n 
A 1 648 ILE 648 650 650 ILE ILE A . n 
A 1 649 ALA 649 651 651 ALA ALA A . n 
A 1 650 GLU 650 652 652 GLU GLU A . n 
A 1 651 LYS 651 653 653 LYS LYS A . n 
A 1 652 LEU 652 654 654 LEU LEU A . n 
A 1 653 VAL 653 655 655 VAL VAL A . n 
A 1 654 ASN 654 656 656 ASN ASN A . n 
A 1 655 TYR 655 657 657 TYR TYR A . n 
A 1 656 ILE 656 658 658 ILE ILE A . n 
A 1 657 LYS 657 659 659 LYS LYS A . n 
A 1 658 LEU 658 660 660 LEU LEU A . n 
A 1 659 ASN 659 661 661 ASN ASN A . n 
A 1 660 PHE 660 662 662 PHE PHE A . n 
A 1 661 LYS 661 663 663 LYS LYS A . n 
A 1 662 SER 662 664 664 SER SER A . n 
A 1 663 ASN 663 665 665 ASN ASN A . n 
A 1 664 ILE 664 666 666 ILE ILE A . n 
A 1 665 PHE 665 667 667 PHE PHE A . n 
A 1 666 ASP 666 668 668 ASP ASP A . n 
A 1 667 THR 667 669 669 THR THR A . n 
A 1 668 GLY 668 670 670 GLY GLY A . n 
A 1 669 PHE 669 671 671 PHE PHE A . n 
A 1 670 PHE 670 672 672 PHE PHE A . n 
A 1 671 HIS 671 673 673 HIS HIS A . n 
A 1 672 ILE 672 674 674 ILE ILE A . n 
A 1 673 GLU 673 675 675 GLU GLU A . n 
A 1 674 GLY 674 676 676 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 
# 
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 
D 4 CL  1   701  1   CL  CL  A . 
E 5 MES 1   702  1   MES MES A . 
F 6 HOH 1   801  426 HOH HOH A . 
F 6 HOH 2   802  422 HOH HOH A . 
F 6 HOH 3   803  254 HOH HOH A . 
F 6 HOH 4   804  361 HOH HOH A . 
F 6 HOH 5   805  428 HOH HOH A . 
F 6 HOH 6   806  267 HOH HOH A . 
F 6 HOH 7   807  429 HOH HOH A . 
F 6 HOH 8   808  376 HOH HOH A . 
F 6 HOH 9   809  430 HOH HOH A . 
F 6 HOH 10  810  266 HOH HOH A . 
F 6 HOH 11  811  423 HOH HOH A . 
F 6 HOH 12  812  68  HOH HOH A . 
F 6 HOH 13  813  365 HOH HOH A . 
F 6 HOH 14  814  6   HOH HOH A . 
F 6 HOH 15  815  150 HOH HOH A . 
F 6 HOH 16  816  273 HOH HOH A . 
F 6 HOH 17  817  112 HOH HOH A . 
F 6 HOH 18  818  122 HOH HOH A . 
F 6 HOH 19  819  413 HOH HOH A . 
F 6 HOH 20  820  3   HOH HOH A . 
F 6 HOH 21  821  435 HOH HOH A . 
F 6 HOH 22  822  69  HOH HOH A . 
F 6 HOH 23  823  427 HOH HOH A . 
F 6 HOH 24  824  285 HOH HOH A . 
F 6 HOH 25  825  189 HOH HOH A . 
F 6 HOH 26  826  344 HOH HOH A . 
F 6 HOH 27  827  221 HOH HOH A . 
F 6 HOH 28  828  433 HOH HOH A . 
F 6 HOH 29  829  26  HOH HOH A . 
F 6 HOH 30  830  138 HOH HOH A . 
F 6 HOH 31  831  264 HOH HOH A . 
F 6 HOH 32  832  312 HOH HOH A . 
F 6 HOH 33  833  64  HOH HOH A . 
F 6 HOH 34  834  119 HOH HOH A . 
F 6 HOH 35  835  196 HOH HOH A . 
F 6 HOH 36  836  80  HOH HOH A . 
F 6 HOH 37  837  95  HOH HOH A . 
F 6 HOH 38  838  178 HOH HOH A . 
F 6 HOH 39  839  159 HOH HOH A . 
F 6 HOH 40  840  335 HOH HOH A . 
F 6 HOH 41  841  215 HOH HOH A . 
F 6 HOH 42  842  83  HOH HOH A . 
F 6 HOH 43  843  13  HOH HOH A . 
F 6 HOH 44  844  142 HOH HOH A . 
F 6 HOH 45  845  118 HOH HOH A . 
F 6 HOH 46  846  10  HOH HOH A . 
F 6 HOH 47  847  40  HOH HOH A . 
F 6 HOH 48  848  393 HOH HOH A . 
F 6 HOH 49  849  71  HOH HOH A . 
F 6 HOH 50  850  60  HOH HOH A . 
F 6 HOH 51  851  78  HOH HOH A . 
F 6 HOH 52  852  32  HOH HOH A . 
F 6 HOH 53  853  327 HOH HOH A . 
F 6 HOH 54  854  103 HOH HOH A . 
F 6 HOH 55  855  397 HOH HOH A . 
F 6 HOH 56  856  48  HOH HOH A . 
F 6 HOH 57  857  352 HOH HOH A . 
F 6 HOH 58  858  25  HOH HOH A . 
F 6 HOH 59  859  117 HOH HOH A . 
F 6 HOH 60  860  439 HOH HOH A . 
F 6 HOH 61  861  232 HOH HOH A . 
F 6 HOH 62  862  31  HOH HOH A . 
F 6 HOH 63  863  193 HOH HOH A . 
F 6 HOH 64  864  396 HOH HOH A . 
F 6 HOH 65  865  286 HOH HOH A . 
F 6 HOH 66  866  268 HOH HOH A . 
F 6 HOH 67  867  51  HOH HOH A . 
F 6 HOH 68  868  27  HOH HOH A . 
F 6 HOH 69  869  76  HOH HOH A . 
F 6 HOH 70  870  155 HOH HOH A . 
F 6 HOH 71  871  271 HOH HOH A . 
F 6 HOH 72  872  39  HOH HOH A . 
F 6 HOH 73  873  392 HOH HOH A . 
F 6 HOH 74  874  333 HOH HOH A . 
F 6 HOH 75  875  46  HOH HOH A . 
F 6 HOH 76  876  218 HOH HOH A . 
F 6 HOH 77  877  328 HOH HOH A . 
F 6 HOH 78  878  381 HOH HOH A . 
F 6 HOH 79  879  23  HOH HOH A . 
F 6 HOH 80  880  30  HOH HOH A . 
F 6 HOH 81  881  380 HOH HOH A . 
F 6 HOH 82  882  360 HOH HOH A . 
F 6 HOH 83  883  121 HOH HOH A . 
F 6 HOH 84  884  43  HOH HOH A . 
F 6 HOH 85  885  388 HOH HOH A . 
F 6 HOH 86  886  52  HOH HOH A . 
F 6 HOH 87  887  257 HOH HOH A . 
F 6 HOH 88  888  37  HOH HOH A . 
F 6 HOH 89  889  323 HOH HOH A . 
F 6 HOH 90  890  419 HOH HOH A . 
F 6 HOH 91  891  195 HOH HOH A . 
F 6 HOH 92  892  141 HOH HOH A . 
F 6 HOH 93  893  210 HOH HOH A . 
F 6 HOH 94  894  310 HOH HOH A . 
F 6 HOH 95  895  70  HOH HOH A . 
F 6 HOH 96  896  115 HOH HOH A . 
F 6 HOH 97  897  366 HOH HOH A . 
F 6 HOH 98  898  407 HOH HOH A . 
F 6 HOH 99  899  38  HOH HOH A . 
F 6 HOH 100 900  75  HOH HOH A . 
F 6 HOH 101 901  179 HOH HOH A . 
F 6 HOH 102 902  2   HOH HOH A . 
F 6 HOH 103 903  53  HOH HOH A . 
F 6 HOH 104 904  403 HOH HOH A . 
F 6 HOH 105 905  61  HOH HOH A . 
F 6 HOH 106 906  144 HOH HOH A . 
F 6 HOH 107 907  414 HOH HOH A . 
F 6 HOH 108 908  227 HOH HOH A . 
F 6 HOH 109 909  97  HOH HOH A . 
F 6 HOH 110 910  385 HOH HOH A . 
F 6 HOH 111 911  313 HOH HOH A . 
F 6 HOH 112 912  151 HOH HOH A . 
F 6 HOH 113 913  255 HOH HOH A . 
F 6 HOH 114 914  187 HOH HOH A . 
F 6 HOH 115 915  66  HOH HOH A . 
F 6 HOH 116 916  275 HOH HOH A . 
F 6 HOH 117 917  342 HOH HOH A . 
F 6 HOH 118 918  11  HOH HOH A . 
F 6 HOH 119 919  315 HOH HOH A . 
F 6 HOH 120 920  389 HOH HOH A . 
F 6 HOH 121 921  94  HOH HOH A . 
F 6 HOH 122 922  278 HOH HOH A . 
F 6 HOH 123 923  350 HOH HOH A . 
F 6 HOH 124 924  57  HOH HOH A . 
F 6 HOH 125 925  136 HOH HOH A . 
F 6 HOH 126 926  173 HOH HOH A . 
F 6 HOH 127 927  321 HOH HOH A . 
F 6 HOH 128 928  230 HOH HOH A . 
F 6 HOH 129 929  93  HOH HOH A . 
F 6 HOH 130 930  188 HOH HOH A . 
F 6 HOH 131 931  8   HOH HOH A . 
F 6 HOH 132 932  182 HOH HOH A . 
F 6 HOH 133 933  153 HOH HOH A . 
F 6 HOH 134 934  50  HOH HOH A . 
F 6 HOH 135 935  234 HOH HOH A . 
F 6 HOH 136 936  79  HOH HOH A . 
F 6 HOH 137 937  47  HOH HOH A . 
F 6 HOH 138 938  318 HOH HOH A . 
F 6 HOH 139 939  183 HOH HOH A . 
F 6 HOH 140 940  106 HOH HOH A . 
F 6 HOH 141 941  437 HOH HOH A . 
F 6 HOH 142 942  235 HOH HOH A . 
F 6 HOH 143 943  74  HOH HOH A . 
F 6 HOH 144 944  135 HOH HOH A . 
F 6 HOH 145 945  170 HOH HOH A . 
F 6 HOH 146 946  263 HOH HOH A . 
F 6 HOH 147 947  304 HOH HOH A . 
F 6 HOH 148 948  45  HOH HOH A . 
F 6 HOH 149 949  357 HOH HOH A . 
F 6 HOH 150 950  114 HOH HOH A . 
F 6 HOH 151 951  206 HOH HOH A . 
F 6 HOH 152 952  362 HOH HOH A . 
F 6 HOH 153 953  145 HOH HOH A . 
F 6 HOH 154 954  212 HOH HOH A . 
F 6 HOH 155 955  104 HOH HOH A . 
F 6 HOH 156 956  351 HOH HOH A . 
F 6 HOH 157 957  370 HOH HOH A . 
F 6 HOH 158 958  90  HOH HOH A . 
F 6 HOH 159 959  42  HOH HOH A . 
F 6 HOH 160 960  220 HOH HOH A . 
F 6 HOH 161 961  274 HOH HOH A . 
F 6 HOH 162 962  174 HOH HOH A . 
F 6 HOH 163 963  110 HOH HOH A . 
F 6 HOH 164 964  216 HOH HOH A . 
F 6 HOH 165 965  137 HOH HOH A . 
F 6 HOH 166 966  190 HOH HOH A . 
F 6 HOH 167 967  133 HOH HOH A . 
F 6 HOH 168 968  49  HOH HOH A . 
F 6 HOH 169 969  33  HOH HOH A . 
F 6 HOH 170 970  404 HOH HOH A . 
F 6 HOH 171 971  420 HOH HOH A . 
F 6 HOH 172 972  17  HOH HOH A . 
F 6 HOH 173 973  63  HOH HOH A . 
F 6 HOH 174 974  282 HOH HOH A . 
F 6 HOH 175 975  29  HOH HOH A . 
F 6 HOH 176 976  277 HOH HOH A . 
F 6 HOH 177 977  172 HOH HOH A . 
F 6 HOH 178 978  41  HOH HOH A . 
F 6 HOH 179 979  152 HOH HOH A . 
F 6 HOH 180 980  316 HOH HOH A . 
F 6 HOH 181 981  201 HOH HOH A . 
F 6 HOH 182 982  55  HOH HOH A . 
F 6 HOH 183 983  208 HOH HOH A . 
F 6 HOH 184 984  276 HOH HOH A . 
F 6 HOH 185 985  298 HOH HOH A . 
F 6 HOH 186 986  34  HOH HOH A . 
F 6 HOH 187 987  107 HOH HOH A . 
F 6 HOH 188 988  14  HOH HOH A . 
F 6 HOH 189 989  65  HOH HOH A . 
F 6 HOH 190 990  100 HOH HOH A . 
F 6 HOH 191 991  129 HOH HOH A . 
F 6 HOH 192 992  343 HOH HOH A . 
F 6 HOH 193 993  356 HOH HOH A . 
F 6 HOH 194 994  256 HOH HOH A . 
F 6 HOH 195 995  108 HOH HOH A . 
F 6 HOH 196 996  89  HOH HOH A . 
F 6 HOH 197 997  143 HOH HOH A . 
F 6 HOH 198 998  236 HOH HOH A . 
F 6 HOH 199 999  219 HOH HOH A . 
F 6 HOH 200 1000 81  HOH HOH A . 
F 6 HOH 201 1001 154 HOH HOH A . 
F 6 HOH 202 1002 394 HOH HOH A . 
F 6 HOH 203 1003 120 HOH HOH A . 
F 6 HOH 204 1004 303 HOH HOH A . 
F 6 HOH 205 1005 262 HOH HOH A . 
F 6 HOH 206 1006 309 HOH HOH A . 
F 6 HOH 207 1007 384 HOH HOH A . 
F 6 HOH 208 1008 111 HOH HOH A . 
F 6 HOH 209 1009 54  HOH HOH A . 
F 6 HOH 210 1010 28  HOH HOH A . 
F 6 HOH 211 1011 22  HOH HOH A . 
F 6 HOH 212 1012 253 HOH HOH A . 
F 6 HOH 213 1013 306 HOH HOH A . 
F 6 HOH 214 1014 367 HOH HOH A . 
F 6 HOH 215 1015 233 HOH HOH A . 
F 6 HOH 216 1016 295 HOH HOH A . 
F 6 HOH 217 1017 167 HOH HOH A . 
F 6 HOH 218 1018 84  HOH HOH A . 
F 6 HOH 219 1019 177 HOH HOH A . 
F 6 HOH 220 1020 132 HOH HOH A . 
F 6 HOH 221 1021 330 HOH HOH A . 
F 6 HOH 222 1022 59  HOH HOH A . 
F 6 HOH 223 1023 35  HOH HOH A . 
F 6 HOH 224 1024 249 HOH HOH A . 
F 6 HOH 225 1025 284 HOH HOH A . 
F 6 HOH 226 1026 168 HOH HOH A . 
F 6 HOH 227 1027 164 HOH HOH A . 
F 6 HOH 228 1028 109 HOH HOH A . 
F 6 HOH 229 1029 130 HOH HOH A . 
F 6 HOH 230 1030 438 HOH HOH A . 
F 6 HOH 231 1031 96  HOH HOH A . 
F 6 HOH 232 1032 283 HOH HOH A . 
F 6 HOH 233 1033 228 HOH HOH A . 
F 6 HOH 234 1034 251 HOH HOH A . 
F 6 HOH 235 1035 175 HOH HOH A . 
F 6 HOH 236 1036 113 HOH HOH A . 
F 6 HOH 237 1037 307 HOH HOH A . 
F 6 HOH 238 1038 209 HOH HOH A . 
F 6 HOH 239 1039 72  HOH HOH A . 
F 6 HOH 240 1040 127 HOH HOH A . 
F 6 HOH 241 1041 317 HOH HOH A . 
F 6 HOH 242 1042 252 HOH HOH A . 
F 6 HOH 243 1043 308 HOH HOH A . 
F 6 HOH 244 1044 243 HOH HOH A . 
F 6 HOH 245 1045 261 HOH HOH A . 
F 6 HOH 246 1046 5   HOH HOH A . 
F 6 HOH 247 1047 244 HOH HOH A . 
F 6 HOH 248 1048 36  HOH HOH A . 
F 6 HOH 249 1049 368 HOH HOH A . 
F 6 HOH 250 1050 334 HOH HOH A . 
F 6 HOH 251 1051 280 HOH HOH A . 
F 6 HOH 252 1052 398 HOH HOH A . 
F 6 HOH 253 1053 359 HOH HOH A . 
F 6 HOH 254 1054 229 HOH HOH A . 
F 6 HOH 255 1055 311 HOH HOH A . 
F 6 HOH 256 1056 77  HOH HOH A . 
F 6 HOH 257 1057 217 HOH HOH A . 
F 6 HOH 258 1058 160 HOH HOH A . 
F 6 HOH 259 1059 87  HOH HOH A . 
F 6 HOH 260 1060 176 HOH HOH A . 
F 6 HOH 261 1061 62  HOH HOH A . 
F 6 HOH 262 1062 24  HOH HOH A . 
F 6 HOH 263 1063 339 HOH HOH A . 
F 6 HOH 264 1064 181 HOH HOH A . 
F 6 HOH 265 1065 358 HOH HOH A . 
F 6 HOH 266 1066 341 HOH HOH A . 
F 6 HOH 267 1067 374 HOH HOH A . 
F 6 HOH 268 1068 246 HOH HOH A . 
F 6 HOH 269 1069 331 HOH HOH A . 
F 6 HOH 270 1070 248 HOH HOH A . 
F 6 HOH 271 1071 88  HOH HOH A . 
F 6 HOH 272 1072 199 HOH HOH A . 
F 6 HOH 273 1073 346 HOH HOH A . 
F 6 HOH 274 1074 383 HOH HOH A . 
F 6 HOH 275 1075 148 HOH HOH A . 
F 6 HOH 276 1076 131 HOH HOH A . 
F 6 HOH 277 1077 191 HOH HOH A . 
F 6 HOH 278 1078 214 HOH HOH A . 
F 6 HOH 279 1079 147 HOH HOH A . 
F 6 HOH 280 1080 102 HOH HOH A . 
F 6 HOH 281 1081 166 HOH HOH A . 
F 6 HOH 282 1082 369 HOH HOH A . 
F 6 HOH 283 1083 250 HOH HOH A . 
F 6 HOH 284 1084 242 HOH HOH A . 
F 6 HOH 285 1085 239 HOH HOH A . 
F 6 HOH 286 1086 222 HOH HOH A . 
F 6 HOH 287 1087 281 HOH HOH A . 
F 6 HOH 288 1088 125 HOH HOH A . 
F 6 HOH 289 1089 157 HOH HOH A . 
F 6 HOH 290 1090 294 HOH HOH A . 
F 6 HOH 291 1091 391 HOH HOH A . 
F 6 HOH 292 1092 197 HOH HOH A . 
F 6 HOH 293 1093 207 HOH HOH A . 
F 6 HOH 294 1094 19  HOH HOH A . 
F 6 HOH 295 1095 432 HOH HOH A . 
F 6 HOH 296 1096 124 HOH HOH A . 
F 6 HOH 297 1097 355 HOH HOH A . 
F 6 HOH 298 1098 198 HOH HOH A . 
F 6 HOH 299 1099 140 HOH HOH A . 
F 6 HOH 300 1100 205 HOH HOH A . 
F 6 HOH 301 1101 279 HOH HOH A . 
F 6 HOH 302 1102 301 HOH HOH A . 
F 6 HOH 303 1103 16  HOH HOH A . 
F 6 HOH 304 1104 21  HOH HOH A . 
F 6 HOH 305 1105 340 HOH HOH A . 
F 6 HOH 306 1106 116 HOH HOH A . 
F 6 HOH 307 1107 421 HOH HOH A . 
F 6 HOH 308 1108 185 HOH HOH A . 
F 6 HOH 309 1109 226 HOH HOH A . 
F 6 HOH 310 1110 337 HOH HOH A . 
F 6 HOH 311 1111 409 HOH HOH A . 
F 6 HOH 312 1112 291 HOH HOH A . 
F 6 HOH 313 1113 326 HOH HOH A . 
F 6 HOH 314 1114 82  HOH HOH A . 
F 6 HOH 315 1115 213 HOH HOH A . 
F 6 HOH 316 1116 290 HOH HOH A . 
F 6 HOH 317 1117 293 HOH HOH A . 
F 6 HOH 318 1118 165 HOH HOH A . 
F 6 HOH 319 1119 1   HOH HOH A . 
F 6 HOH 320 1120 204 HOH HOH A . 
F 6 HOH 321 1121 399 HOH HOH A . 
F 6 HOH 322 1122 225 HOH HOH A . 
F 6 HOH 323 1123 237 HOH HOH A . 
F 6 HOH 324 1124 387 HOH HOH A . 
F 6 HOH 325 1125 325 HOH HOH A . 
F 6 HOH 326 1126 288 HOH HOH A . 
F 6 HOH 327 1127 105 HOH HOH A . 
F 6 HOH 328 1128 139 HOH HOH A . 
F 6 HOH 329 1129 411 HOH HOH A . 
F 6 HOH 330 1130 336 HOH HOH A . 
F 6 HOH 331 1131 86  HOH HOH A . 
F 6 HOH 332 1132 56  HOH HOH A . 
F 6 HOH 333 1133 332 HOH HOH A . 
F 6 HOH 334 1134 379 HOH HOH A . 
F 6 HOH 335 1135 162 HOH HOH A . 
F 6 HOH 336 1136 156 HOH HOH A . 
F 6 HOH 337 1137 194 HOH HOH A . 
F 6 HOH 338 1138 134 HOH HOH A . 
F 6 HOH 339 1139 322 HOH HOH A . 
F 6 HOH 340 1140 180 HOH HOH A . 
F 6 HOH 341 1141 12  HOH HOH A . 
F 6 HOH 342 1142 146 HOH HOH A . 
F 6 HOH 343 1143 238 HOH HOH A . 
F 6 HOH 344 1144 353 HOH HOH A . 
F 6 HOH 345 1145 224 HOH HOH A . 
F 6 HOH 346 1146 324 HOH HOH A . 
F 6 HOH 347 1147 163 HOH HOH A . 
F 6 HOH 348 1148 386 HOH HOH A . 
F 6 HOH 349 1149 149 HOH HOH A . 
F 6 HOH 350 1150 408 HOH HOH A . 
F 6 HOH 351 1151 412 HOH HOH A . 
F 6 HOH 352 1152 329 HOH HOH A . 
F 6 HOH 353 1153 202 HOH HOH A . 
F 6 HOH 354 1154 349 HOH HOH A . 
F 6 HOH 355 1155 211 HOH HOH A . 
F 6 HOH 356 1156 390 HOH HOH A . 
F 6 HOH 357 1157 126 HOH HOH A . 
F 6 HOH 358 1158 401 HOH HOH A . 
F 6 HOH 359 1159 98  HOH HOH A . 
F 6 HOH 360 1160 231 HOH HOH A . 
F 6 HOH 361 1161 128 HOH HOH A . 
F 6 HOH 362 1162 416 HOH HOH A . 
F 6 HOH 363 1163 406 HOH HOH A . 
F 6 HOH 364 1164 101 HOH HOH A . 
F 6 HOH 365 1165 300 HOH HOH A . 
F 6 HOH 366 1166 373 HOH HOH A . 
F 6 HOH 367 1167 402 HOH HOH A . 
F 6 HOH 368 1168 123 HOH HOH A . 
F 6 HOH 369 1169 241 HOH HOH A . 
F 6 HOH 370 1170 270 HOH HOH A . 
F 6 HOH 371 1171 186 HOH HOH A . 
F 6 HOH 372 1172 415 HOH HOH A . 
F 6 HOH 373 1173 169 HOH HOH A . 
F 6 HOH 374 1174 44  HOH HOH A . 
F 6 HOH 375 1175 364 HOH HOH A . 
F 6 HOH 376 1176 296 HOH HOH A . 
F 6 HOH 377 1177 371 HOH HOH A . 
F 6 HOH 378 1178 319 HOH HOH A . 
F 6 HOH 379 1179 425 HOH HOH A . 
F 6 HOH 380 1180 223 HOH HOH A . 
F 6 HOH 381 1181 424 HOH HOH A . 
F 6 HOH 382 1182 258 HOH HOH A . 
F 6 HOH 383 1183 305 HOH HOH A . 
F 6 HOH 384 1184 410 HOH HOH A . 
F 6 HOH 385 1185 431 HOH HOH A . 
F 6 HOH 386 1186 269 HOH HOH A . 
F 6 HOH 387 1187 240 HOH HOH A . 
F 6 HOH 388 1188 363 HOH HOH A . 
F 6 HOH 389 1189 260 HOH HOH A . 
F 6 HOH 390 1190 184 HOH HOH A . 
F 6 HOH 391 1191 289 HOH HOH A . 
F 6 HOH 392 1192 292 HOH HOH A . 
F 6 HOH 393 1193 299 HOH HOH A . 
F 6 HOH 394 1194 158 HOH HOH A . 
F 6 HOH 395 1195 320 HOH HOH A . 
G 6 HOH 1   101  417 HOH HOH E . 
G 6 HOH 2   102  375 HOH HOH E . 
G 6 HOH 3   103  4   HOH HOH E . 
G 6 HOH 4   104  245 HOH HOH E . 
G 6 HOH 5   105  161 HOH HOH E . 
G 6 HOH 6   106  348 HOH HOH E . 
G 6 HOH 7   107  377 HOH HOH E . 
G 6 HOH 8   108  400 HOH HOH E . 
G 6 HOH 9   109  67  HOH HOH E . 
G 6 HOH 10  110  345 HOH HOH E . 
G 6 HOH 11  111  91  HOH HOH E . 
G 6 HOH 12  112  192 HOH HOH E . 
G 6 HOH 13  113  382 HOH HOH E . 
G 6 HOH 14  114  272 HOH HOH E . 
G 6 HOH 15  115  338 HOH HOH E . 
G 6 HOH 16  116  418 HOH HOH E . 
G 6 HOH 17  117  372 HOH HOH E . 
G 6 HOH 18  118  247 HOH HOH E . 
G 6 HOH 19  119  395 HOH HOH E . 
G 6 HOH 20  120  436 HOH HOH E . 
H 6 HOH 1   101  434 HOH HOH F . 
H 6 HOH 2   102  297 HOH HOH F . 
H 6 HOH 3   103  171 HOH HOH F . 
H 6 HOH 4   104  347 HOH HOH F . 
H 6 HOH 5   105  9   HOH HOH F . 
H 6 HOH 6   106  354 HOH HOH F . 
H 6 HOH 7   107  92  HOH HOH F . 
H 6 HOH 8   108  378 HOH HOH F . 
H 6 HOH 9   109  287 HOH HOH F . 
H 6 HOH 10  110  20  HOH HOH F . 
H 6 HOH 11  111  203 HOH HOH F . 
H 6 HOH 12  112  99  HOH HOH F . 
H 6 HOH 13  113  85  HOH HOH F . 
H 6 HOH 14  114  73  HOH HOH F . 
H 6 HOH 15  115  18  HOH HOH F . 
H 6 HOH 16  116  15  HOH HOH F . 
H 6 HOH 17  117  58  HOH HOH F . 
H 6 HOH 18  118  7   HOH HOH F . 
H 6 HOH 19  119  405 HOH HOH F . 
H 6 HOH 20  120  314 HOH HOH F . 
H 6 HOH 21  121  302 HOH HOH F . 
H 6 HOH 22  122  259 HOH HOH F . 
H 6 HOH 23  123  200 HOH HOH F . 
H 6 HOH 24  124  265 HOH HOH F . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A THR 67  ? OG1 ? A THR 67  OG1 
2  1 Y 1 A THR 67  ? CG2 ? A THR 67  CG2 
3  1 Y 1 A ASN 68  ? CG  ? A ASN 68  CG  
4  1 Y 1 A ASN 68  ? OD1 ? A ASN 68  OD1 
5  1 Y 1 A ASN 68  ? ND2 ? A ASN 68  ND2 
6  1 Y 1 A ASN 98  ? CG  ? A ASN 98  CG  
7  1 Y 1 A ASN 98  ? OD1 ? A ASN 98  OD1 
8  1 Y 1 A ASN 98  ? ND2 ? A ASN 98  ND2 
9  1 Y 1 A GLU 103 ? CG  ? A GLU 103 CG  
10 1 Y 1 A GLU 103 ? CD  ? A GLU 103 CD  
11 1 Y 1 A GLU 103 ? OE1 ? A GLU 103 OE1 
12 1 Y 1 A GLU 103 ? OE2 ? A GLU 103 OE2 
13 1 Y 1 A LYS 174 ? CG  ? A LYS 174 CG  
14 1 Y 1 A LYS 174 ? CD  ? A LYS 174 CD  
15 1 Y 1 A LYS 174 ? CE  ? A LYS 174 CE  
16 1 Y 1 A LYS 174 ? NZ  ? A LYS 174 NZ  
17 1 Y 1 A ASP 209 ? CG  ? A ASP 208 CG  
18 1 Y 1 A ASP 209 ? OD1 ? A ASP 208 OD1 
19 1 Y 1 A ASP 209 ? OD2 ? A ASP 208 OD2 
20 1 Y 1 A ASN 269 ? CG  ? A ASN 268 CG  
21 1 Y 1 A ASN 269 ? OD1 ? A ASN 268 OD1 
22 1 Y 1 A ASN 269 ? ND2 ? A ASN 268 ND2 
23 1 Y 1 A ARG 316 ? CG  ? A ARG 315 CG  
24 1 Y 1 A ARG 316 ? CD  ? A ARG 315 CD  
25 1 Y 1 A ARG 316 ? NE  ? A ARG 315 NE  
26 1 Y 1 A ARG 316 ? CZ  ? A ARG 315 CZ  
27 1 Y 1 A ARG 316 ? NH1 ? A ARG 315 NH1 
28 1 Y 1 A ARG 316 ? NH2 ? A ARG 315 NH2 
29 1 Y 1 A MET 336 ? CG  ? A MET 335 CG  
30 1 Y 1 A MET 336 ? SD  ? A MET 335 SD  
31 1 Y 1 A MET 336 ? CE  ? A MET 335 CE  
32 1 Y 1 A ASN 380 ? CG  ? A ASN 379 CG  
33 1 Y 1 A ASN 380 ? OD1 ? A ASN 379 OD1 
34 1 Y 1 A ASN 380 ? ND2 ? A ASN 379 ND2 
35 1 Y 1 A GLN 401 ? CG  ? A GLN 400 CG  
36 1 Y 1 A GLN 401 ? CD  ? A GLN 400 CD  
37 1 Y 1 A GLN 401 ? OE1 ? A GLN 400 OE1 
38 1 Y 1 A GLN 401 ? NE2 ? A GLN 400 NE2 
39 1 Y 1 A CYS 493 ? SG  ? A CYS 492 SG  
40 1 Y 1 A ASP 535 ? CG  ? A ASP 534 CG  
41 1 Y 1 A ASP 535 ? OD1 ? A ASP 534 OD1 
42 1 Y 1 A ASP 535 ? OD2 ? A ASP 534 OD2 
43 1 Y 1 A GLU 621 ? CG  ? A GLU 619 CG  
44 1 Y 1 A GLU 621 ? CD  ? A GLU 619 CD  
45 1 Y 1 A GLU 621 ? OE1 ? A GLU 619 OE1 
46 1 Y 1 A GLU 621 ? OE2 ? A GLU 619 OE2 
# 
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' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? 1.0.5  2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? 1.0.5  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP   ? ? ? .      4 
# 
_cell.angle_alpha                  90 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EZ5 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     98.481 
_cell.length_a_esd                 ? 
_cell.length_b                     132.584 
_cell.length_b_esd                 ? 
_cell.length_c                     63.745 
_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                         9EZ5 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9EZ5 
_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             2.42 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.21 
_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    
;100mM MES, pH6.5
200mM MgCl2
30% PEG400
25% 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   0.97857 
_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        0.97857 
_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                                       9EZ5 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.846 
_reflns.d_resolution_low                               79.058 
_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                                     38714 
_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                           92.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                14.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.6 
_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                                0.193 
_reflns.pdbx_Rpim_I_all                                0.05 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.186 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.846 
_reflns_shell.d_res_low                                     2.023 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.5 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1936 
_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                               13.7 
_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                               2.138 
_reflns_shell.pdbx_Rpim_I_all                               0.559 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.626 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          51.1 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  2.061 
_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]                            -10.8406 
_refine.aniso_B[1][2]                            0 
_refine.aniso_B[1][3]                            0 
_refine.aniso_B[2][2]                            -8.145 
_refine.aniso_B[2][3]                            0 
_refine.aniso_B[3][3]                            18.9856 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               30.25 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.911 
_refine.correlation_coeff_Fo_to_Fc_free          0.882 
_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                                 9EZ5 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.846 
_refine.ls_d_res_low                             34.08 
_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                     38701 
_refine.ls_number_reflns_R_free                  1871 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    53.4 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2085 
_refine.ls_R_factor_R_free                       0.2462 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2065 
_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   0.228 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.231 
_refine.pdbx_overall_SU_R_Blow_DPI               0.36 
_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             0.331 
_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                        9EZ5 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.3 
_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                       1.846 
_refine_hist.d_res_low                        34.08 
_refine_hist.number_atoms_solvent             439 
_refine_hist.number_atoms_total               6437 
_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        5458 
_refine_hist.pdbx_number_atoms_nucleic_acid   527 
_refine_hist.pdbx_number_atoms_ligand         13 
_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' ? 0.009 ? 6194 ? t_bond_d                  2  HARMONIC     
'X-RAY DIFFRACTION' ? 0.95  ? 8482 ? t_angle_deg               2  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 2103 ? t_dihedral_angle_d        2  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? 971  ? t_gen_planes              5  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 6194 ? t_it                      10 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 806  ? t_chiral_improper_torsion 5  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? 5077 ? t_ideal_dist_contact      4  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? 3.53  ? ?    ? t_omega_torsion           ?  ?            
'X-RAY DIFFRACTION' ? 17.63 ? ?    ? t_other_torsion           ?  ?            
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.85 
_refine_ls_shell.d_res_low                        1.97 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                775 
_refine_ls_shell.number_reflns_R_free             27 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.percent_reflns_obs               6.07 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     0.2704 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2708 
_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                  0.2613 
# 
_struct.entry_id                     9EZ5 
_struct.title                        'BsmI (Inactive) crystallized with Mg2+ 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        9EZ5 
_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 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 6 ? 
H N N 6 ? 
# 
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 9EZ5         9EZ5   ? 2 ? 1 
3 PDB 9EZ5         9EZ5   ? 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 9EZ5 A 1 ? 674 ? Q8RLN4 1 ? 676 ? 1 676 
2 2 9EZ5 E 1 ? 13  ? 9EZ5   1 ? 13  ? 1 13  
3 3 9EZ5 F 1 ? 13  ? 9EZ5   1 ? 13  ? 1 13  
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9EZ5 VAL A 109 ? UNP Q8RLN4 GLU 109 'engineered mutation' 109 1 
1 9EZ5 ?   A ?   ? UNP Q8RLN4 GLU 208 deletion              ?   2 
1 9EZ5 ASP A 506 ? UNP Q8RLN4 ARG 507 'engineered mutation' 507 3 
1 9EZ5 VAL A 508 ? UNP Q8RLN4 GLY 509 'engineered mutation' 509 4 
1 9EZ5 VAL A 545 ? UNP Q8RLN4 GLU 546 'engineered mutation' 546 5 
1 9EZ5 ?   A ?   ? UNP Q8RLN4 GLY 582 deletion              ?   6 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     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)' 4980  ? 
1 MORE         -30   ? 
1 'SSA (A^2)'  30460 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'equilibrium centrifugation' 
_pdbx_struct_assembly_auth_evidence.details                'Analytical Ultra-Centrifugation' 
# 
_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  ? SER A 23  ? ASN A 10  SER A 23  1 ? 14 
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 GLN A 191 ? LYS A 199 ? GLN A 191 LYS A 199 5 ? 9  
HELX_P HELX_P7  AA7 ASP A 202 ? PHE A 206 ? ASP A 202 PHE A 206 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 209 ? GLN A 219 ? ASP A 210 GLN A 220 1 ? 11 
HELX_P HELX_P9  AA9 THR A 223 ? LYS A 243 ? THR A 224 LYS A 244 1 ? 21 
HELX_P HELX_P10 AB1 THR A 252 ? ASN A 261 ? THR A 253 ASN A 262 1 ? 10 
HELX_P HELX_P11 AB2 ALA A 282 ? LEU A 286 ? ALA A 283 LEU A 287 5 ? 5  
HELX_P HELX_P12 AB3 LYS A 289 ? SER A 301 ? LYS A 290 SER A 302 1 ? 13 
HELX_P HELX_P13 AB4 ARG A 315 ? ASN A 331 ? ARG A 316 ASN A 332 1 ? 17 
HELX_P HELX_P14 AB5 ASP A 334 ? LYS A 342 ? ASP A 335 LYS A 343 1 ? 9  
HELX_P HELX_P15 AB6 ARG A 363 ? ARG A 366 ? ARG A 364 ARG A 367 5 ? 4  
HELX_P HELX_P16 AB7 GLY A 367 ? GLY A 377 ? GLY A 368 GLY A 378 1 ? 11 
HELX_P HELX_P17 AB8 ILE A 391 ? ASP A 401 ? ILE A 392 ASP A 402 1 ? 11 
HELX_P HELX_P18 AB9 ASP A 401 ? ASN A 409 ? ASP A 402 ASN A 410 1 ? 9  
HELX_P HELX_P19 AC1 ASN A 409 ? SER A 419 ? ASN A 410 SER A 420 1 ? 11 
HELX_P HELX_P20 AC2 ASN A 441 ? LYS A 451 ? ASN A 442 LYS A 452 1 ? 11 
HELX_P HELX_P21 AC3 GLN A 468 ? TYR A 482 ? GLN A 469 TYR A 483 1 ? 15 
HELX_P HELX_P22 AC4 LYS A 549 ? LEU A 553 ? LYS A 550 LEU A 554 5 ? 5  
HELX_P HELX_P23 AC5 LYS A 556 ? ASP A 570 ? LYS A 557 ASP A 571 1 ? 15 
HELX_P HELX_P24 AC6 VAL A 591 ? PHE A 595 ? VAL A 593 PHE A 597 5 ? 5  
HELX_P HELX_P25 AC7 THR A 610 ? GLY A 622 ? THR A 612 GLY A 624 1 ? 13 
HELX_P HELX_P26 AC8 ASN A 646 ? ASN A 659 ? ASN A 648 ASN A 661 1 ? 14 
HELX_P HELX_P27 AC9 ASP A 666 ? GLY A 668 ? ASP A 668 GLY A 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 
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 ? ? ? 
# 
_struct_conn_type.id          hydrog 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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 -1.22 
2 ASN 634 A . ? ASN 636 A PRO 635 A ? PRO 637 A 1 -4.38 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 6 ? 
AA3 ? 5 ? 
AA4 ? 6 ? 
# 
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 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? anti-parallel 
AA4 5 6 ? 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 302 ? GLY A 303 ? VAL A 303 GLY A 304 
AA2 2 PHE A 311 ? ILE A 314 ? PHE A 312 ILE A 315 
AA2 3 LEU A 347 ? LEU A 352 ? LEU A 348 LEU A 353 
AA2 4 ILE A 382 ? ILE A 386 ? ILE A 383 ILE A 387 
AA2 5 PHE A 421 ? CYS A 426 ? PHE A 422 CYS A 427 
AA2 6 GLU A 435 ? ILE A 440 ? GLU A 436 ILE A 441 
AA3 1 GLY A 497 ? ASP A 498 ? GLY A 498 ASP A 499 
AA3 2 GLY A 501 ? ILE A 505 ? GLY A 502 ILE A 506 
AA3 3 HIS A 509 ? LEU A 514 ? HIS A 510 LEU A 515 
AA3 4 VAL A 575 ? LYS A 578 ? VAL A 576 LYS A 579 
AA3 5 GLU A 584 ? PHE A 585 ? GLU A 586 PHE A 587 
AA4 1 HIS A 528 ? ILE A 532 ? HIS A 529 ILE A 533 
AA4 2 LEU A 540 ? SER A 546 ? LEU A 541 SER A 547 
AA4 3 ILE A 596 ? ILE A 604 ? ILE A 598 ILE A 606 
AA4 4 LEU A 625 ? GLN A 632 ? LEU A 627 GLN A 634 
AA4 5 LYS A 637 ? PRO A 644 ? LYS A 639 PRO A 646 
AA4 6 PHE A 670 ? ILE A 672 ? PHE A 672 ILE A 674 
# 
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 PHE A 60  ? O PHE A 60  N ILE A 6   ? N ILE A 6   
AA1 4 5 N ARG A 5   ? N ARG A 5   O THR A 95  ? O THR A 95  
AA1 5 6 N ILE A 94  ? N ILE A 94  O LEU A 105 ? O LEU A 105 
AA1 6 7 N VAL A 109 ? N VAL A 109 O ILE A 140 ? O ILE A 140 
AA1 7 8 N TYR A 139 ? N TYR A 139 O ALA A 183 ? O ALA A 183 
AA2 1 2 N VAL A 302 ? N VAL A 303 O VAL A 313 ? O VAL A 314 
AA2 2 3 N ILE A 314 ? N ILE A 315 O LEU A 347 ? O LEU A 348 
AA2 3 4 N ILE A 348 ? N ILE A 349 O PHE A 383 ? O PHE A 384 
AA2 4 5 N THR A 384 ? N THR A 385 O VAL A 423 ? O VAL A 424 
AA2 5 6 N ILE A 422 ? N ILE A 423 O ILE A 439 ? O ILE A 440 
AA3 1 2 N ASP A 498 ? N ASP A 499 O GLY A 501 ? O GLY A 502 
AA3 2 3 N ILE A 504 ? N ILE A 505 O PHE A 511 ? O PHE A 512 
AA3 3 4 N ARG A 512 ? N ARG A 513 O VAL A 575 ? O VAL A 576 
AA3 4 5 N GLN A 576 ? N GLN A 577 O GLU A 584 ? O GLU A 586 
AA4 1 2 N HIS A 528 ? N HIS A 529 O ILE A 544 ? O ILE A 545 
AA4 2 3 N LEU A 541 ? N LEU A 542 O ILE A 596 ? O ILE A 598 
AA4 3 4 N GLY A 601 ? N GLY A 603 O ILE A 627 ? O ILE A 629 
AA4 4 5 N LYS A 630 ? N LYS A 632 O VAL A 639 ? O VAL A 641 
AA4 5 6 N ILE A 640 ? N ILE A 642 O HIS A 671 ? O HIS A 673 
# 
_pdbx_entry_details.entry_id                   9EZ5 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            "O3'" 
_pdbx_validate_rmsd_bond.auth_asym_id_1            E 
_pdbx_validate_rmsd_bond.auth_comp_id_1            DC 
_pdbx_validate_rmsd_bond.auth_seq_id_1             3 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            "C3'" 
_pdbx_validate_rmsd_bond.auth_asym_id_2            E 
_pdbx_validate_rmsd_bond.auth_comp_id_2            DC 
_pdbx_validate_rmsd_bond.auth_seq_id_2             3 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.381 
_pdbx_validate_rmsd_bond.bond_target_value         1.419 
_pdbx_validate_rmsd_bond.bond_deviation            -0.038 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.006 
_pdbx_validate_rmsd_bond.linker_flag               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'" E DA 7 ? ? "C1'" E DA 7 ? ? N9 E DA 7 ? ? 111.09 108.30 2.79 0.30 N 
2 1 "O4'" F DG 3 ? ? "C1'" F DG 3 ? ? N9 F DG 3 ? ? 110.19 108.30 1.89 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  ? ? -161.82 -163.17 
2  1 ASN A 68  ? ? -146.42 29.45   
3  1 ALA A 306 ? ? 72.42   -46.25  
4  1 PRO A 311 ? ? -76.26  24.27   
5  1 ASP A 402 ? ? -166.49 97.63   
6  1 ASN A 487 ? ? 60.70   62.79   
7  1 ASN A 494 ? ? 21.36   -157.16 
8  1 ASP A 507 ? ? -133.35 -152.01 
9  1 VAL A 509 ? ? -131.82 -33.42  
10 1 LEU A 536 ? ? -121.78 -59.90  
# 
loop_
_pdbx_validate_polymer_linkage.id 
_pdbx_validate_polymer_linkage.PDB_model_num 
_pdbx_validate_polymer_linkage.auth_atom_id_1 
_pdbx_validate_polymer_linkage.auth_asym_id_1 
_pdbx_validate_polymer_linkage.auth_comp_id_1 
_pdbx_validate_polymer_linkage.auth_seq_id_1 
_pdbx_validate_polymer_linkage.PDB_ins_code_1 
_pdbx_validate_polymer_linkage.label_alt_id_1 
_pdbx_validate_polymer_linkage.auth_atom_id_2 
_pdbx_validate_polymer_linkage.auth_asym_id_2 
_pdbx_validate_polymer_linkage.auth_comp_id_2 
_pdbx_validate_polymer_linkage.auth_seq_id_2 
_pdbx_validate_polymer_linkage.PDB_ins_code_2 
_pdbx_validate_polymer_linkage.label_alt_id_2 
_pdbx_validate_polymer_linkage.dist 
1 1 C A ALA 207 ? ? N A ASP 209 ? ? 3.74 
2 1 C A GLY 582 ? ? N A ASN 584 ? ? 3.93 
# 
_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         16.5217 
_pdbx_refine_tls.origin_y         22.6365 
_pdbx_refine_tls.origin_z         10.5178 
_pdbx_refine_tls.T[1][1]          -0.1873 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0054 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0002 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          -0.1402 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0593 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.2561 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.1994 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.1597 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.0398 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.1701 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.1716 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.1439 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0054 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0234 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0354 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0234 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0141 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.004 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0354 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.004 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0195 
_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 ? ? C 1 ? ? ? C 1   ? ? '{ *|* }' 
3 'X-RAY DIFFRACTION' 1 ? ? E 1 ? ? ? E 13  ? ? '{ *|* }' 
4 'X-RAY DIFFRACTION' 1 ? ? F 1 ? ? ? F 13  ? ? '{ *|* }' 
5 'X-RAY DIFFRACTION' 1 ? ? L 1 ? ? ? L 1   ? ? '{ *|* }' 
6 'X-RAY DIFFRACTION' 1 ? ? W 1 ? ? ? W 439 ? ? '{ *|* }' 
# 
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  
CL  CL     CL N N 74  
CYS N      N  N N 75  
CYS CA     C  N R 76  
CYS C      C  N N 77  
CYS O      O  N N 78  
CYS CB     C  N N 79  
CYS SG     S  N N 80  
CYS OXT    O  N N 81  
CYS H      H  N N 82  
CYS H2     H  N N 83  
CYS HA     H  N N 84  
CYS HB2    H  N N 85  
CYS HB3    H  N N 86  
CYS HG     H  N N 87  
CYS HXT    H  N N 88  
DA  OP3    O  N N 89  
DA  P      P  N N 90  
DA  OP1    O  N N 91  
DA  OP2    O  N N 92  
DA  "O5'"  O  N N 93  
DA  "C5'"  C  N N 94  
DA  "C4'"  C  N R 95  
DA  "O4'"  O  N N 96  
DA  "C3'"  C  N S 97  
DA  "O3'"  O  N N 98  
DA  "C2'"  C  N N 99  
DA  "C1'"  C  N R 100 
DA  N9     N  Y N 101 
DA  C8     C  Y N 102 
DA  N7     N  Y N 103 
DA  C5     C  Y N 104 
DA  C6     C  Y N 105 
DA  N6     N  N N 106 
DA  N1     N  Y N 107 
DA  C2     C  Y N 108 
DA  N3     N  Y N 109 
DA  C4     C  Y N 110 
DA  HOP3   H  N N 111 
DA  HOP2   H  N N 112 
DA  "H5'"  H  N N 113 
DA  "H5''" H  N N 114 
DA  "H4'"  H  N N 115 
DA  "H3'"  H  N N 116 
DA  "HO3'" H  N N 117 
DA  "H2'"  H  N N 118 
DA  "H2''" H  N N 119 
DA  "H1'"  H  N N 120 
DA  H8     H  N N 121 
DA  H61    H  N N 122 
DA  H62    H  N N 123 
DA  H2     H  N N 124 
DC  OP3    O  N N 125 
DC  P      P  N N 126 
DC  OP1    O  N N 127 
DC  OP2    O  N N 128 
DC  "O5'"  O  N N 129 
DC  "C5'"  C  N N 130 
DC  "C4'"  C  N R 131 
DC  "O4'"  O  N N 132 
DC  "C3'"  C  N S 133 
DC  "O3'"  O  N N 134 
DC  "C2'"  C  N N 135 
DC  "C1'"  C  N R 136 
DC  N1     N  N N 137 
DC  C2     C  N N 138 
DC  O2     O  N N 139 
DC  N3     N  N N 140 
DC  C4     C  N N 141 
DC  N4     N  N N 142 
DC  C5     C  N N 143 
DC  C6     C  N N 144 
DC  HOP3   H  N N 145 
DC  HOP2   H  N N 146 
DC  "H5'"  H  N N 147 
DC  "H5''" H  N N 148 
DC  "H4'"  H  N N 149 
DC  "H3'"  H  N N 150 
DC  "HO3'" H  N N 151 
DC  "H2'"  H  N N 152 
DC  "H2''" H  N N 153 
DC  "H1'"  H  N N 154 
DC  H41    H  N N 155 
DC  H42    H  N N 156 
DC  H5     H  N N 157 
DC  H6     H  N N 158 
DG  OP3    O  N N 159 
DG  P      P  N N 160 
DG  OP1    O  N N 161 
DG  OP2    O  N N 162 
DG  "O5'"  O  N N 163 
DG  "C5'"  C  N N 164 
DG  "C4'"  C  N R 165 
DG  "O4'"  O  N N 166 
DG  "C3'"  C  N S 167 
DG  "O3'"  O  N N 168 
DG  "C2'"  C  N N 169 
DG  "C1'"  C  N R 170 
DG  N9     N  Y N 171 
DG  C8     C  Y N 172 
DG  N7     N  Y N 173 
DG  C5     C  Y N 174 
DG  C6     C  N N 175 
DG  O6     O  N N 176 
DG  N1     N  N N 177 
DG  C2     C  N N 178 
DG  N2     N  N N 179 
DG  N3     N  N N 180 
DG  C4     C  Y N 181 
DG  HOP3   H  N N 182 
DG  HOP2   H  N N 183 
DG  "H5'"  H  N N 184 
DG  "H5''" H  N N 185 
DG  "H4'"  H  N N 186 
DG  "H3'"  H  N N 187 
DG  "HO3'" H  N N 188 
DG  "H2'"  H  N N 189 
DG  "H2''" H  N N 190 
DG  "H1'"  H  N N 191 
DG  H8     H  N N 192 
DG  H1     H  N N 193 
DG  H21    H  N N 194 
DG  H22    H  N N 195 
DT  OP3    O  N N 196 
DT  P      P  N N 197 
DT  OP1    O  N N 198 
DT  OP2    O  N N 199 
DT  "O5'"  O  N N 200 
DT  "C5'"  C  N N 201 
DT  "C4'"  C  N R 202 
DT  "O4'"  O  N N 203 
DT  "C3'"  C  N S 204 
DT  "O3'"  O  N N 205 
DT  "C2'"  C  N N 206 
DT  "C1'"  C  N R 207 
DT  N1     N  N N 208 
DT  C2     C  N N 209 
DT  O2     O  N N 210 
DT  N3     N  N N 211 
DT  C4     C  N N 212 
DT  O4     O  N N 213 
DT  C5     C  N N 214 
DT  C7     C  N N 215 
DT  C6     C  N N 216 
DT  HOP3   H  N N 217 
DT  HOP2   H  N N 218 
DT  "H5'"  H  N N 219 
DT  "H5''" H  N N 220 
DT  "H4'"  H  N N 221 
DT  "H3'"  H  N N 222 
DT  "HO3'" H  N N 223 
DT  "H2'"  H  N N 224 
DT  "H2''" H  N N 225 
DT  "H1'"  H  N N 226 
DT  H3     H  N N 227 
DT  H71    H  N N 228 
DT  H72    H  N N 229 
DT  H73    H  N N 230 
DT  H6     H  N N 231 
GLN N      N  N N 232 
GLN CA     C  N S 233 
GLN C      C  N N 234 
GLN O      O  N N 235 
GLN CB     C  N N 236 
GLN CG     C  N N 237 
GLN CD     C  N N 238 
GLN OE1    O  N N 239 
GLN NE2    N  N N 240 
GLN OXT    O  N N 241 
GLN H      H  N N 242 
GLN H2     H  N N 243 
GLN HA     H  N N 244 
GLN HB2    H  N N 245 
GLN HB3    H  N N 246 
GLN HG2    H  N N 247 
GLN HG3    H  N N 248 
GLN HE21   H  N N 249 
GLN HE22   H  N N 250 
GLN HXT    H  N N 251 
GLU N      N  N N 252 
GLU CA     C  N S 253 
GLU C      C  N N 254 
GLU O      O  N N 255 
GLU CB     C  N N 256 
GLU CG     C  N N 257 
GLU CD     C  N N 258 
GLU OE1    O  N N 259 
GLU OE2    O  N N 260 
GLU OXT    O  N N 261 
GLU H      H  N N 262 
GLU H2     H  N N 263 
GLU HA     H  N N 264 
GLU HB2    H  N N 265 
GLU HB3    H  N N 266 
GLU HG2    H  N N 267 
GLU HG3    H  N N 268 
GLU HE2    H  N N 269 
GLU HXT    H  N N 270 
GLY N      N  N N 271 
GLY CA     C  N N 272 
GLY C      C  N N 273 
GLY O      O  N N 274 
GLY OXT    O  N N 275 
GLY H      H  N N 276 
GLY H2     H  N N 277 
GLY HA2    H  N N 278 
GLY HA3    H  N N 279 
GLY HXT    H  N N 280 
HIS N      N  N N 281 
HIS CA     C  N S 282 
HIS C      C  N N 283 
HIS O      O  N N 284 
HIS CB     C  N N 285 
HIS CG     C  Y N 286 
HIS ND1    N  Y N 287 
HIS CD2    C  Y N 288 
HIS CE1    C  Y N 289 
HIS NE2    N  Y N 290 
HIS OXT    O  N N 291 
HIS H      H  N N 292 
HIS H2     H  N N 293 
HIS HA     H  N N 294 
HIS HB2    H  N N 295 
HIS HB3    H  N N 296 
HIS HD1    H  N N 297 
HIS HD2    H  N N 298 
HIS HE1    H  N N 299 
HIS HE2    H  N N 300 
HIS HXT    H  N N 301 
HOH O      O  N N 302 
HOH H1     H  N N 303 
HOH H2     H  N N 304 
ILE N      N  N N 305 
ILE CA     C  N S 306 
ILE C      C  N N 307 
ILE O      O  N N 308 
ILE CB     C  N S 309 
ILE CG1    C  N N 310 
ILE CG2    C  N N 311 
ILE CD1    C  N N 312 
ILE OXT    O  N N 313 
ILE H      H  N N 314 
ILE H2     H  N N 315 
ILE HA     H  N N 316 
ILE HB     H  N N 317 
ILE HG12   H  N N 318 
ILE HG13   H  N N 319 
ILE HG21   H  N N 320 
ILE HG22   H  N N 321 
ILE HG23   H  N N 322 
ILE HD11   H  N N 323 
ILE HD12   H  N N 324 
ILE HD13   H  N N 325 
ILE HXT    H  N N 326 
LEU N      N  N N 327 
LEU CA     C  N S 328 
LEU C      C  N N 329 
LEU O      O  N N 330 
LEU CB     C  N N 331 
LEU CG     C  N N 332 
LEU CD1    C  N N 333 
LEU CD2    C  N N 334 
LEU OXT    O  N N 335 
LEU H      H  N N 336 
LEU H2     H  N N 337 
LEU HA     H  N N 338 
LEU HB2    H  N N 339 
LEU HB3    H  N N 340 
LEU HG     H  N N 341 
LEU HD11   H  N N 342 
LEU HD12   H  N N 343 
LEU HD13   H  N N 344 
LEU HD21   H  N N 345 
LEU HD22   H  N N 346 
LEU HD23   H  N N 347 
LEU HXT    H  N N 348 
LYS N      N  N N 349 
LYS CA     C  N S 350 
LYS C      C  N N 351 
LYS O      O  N N 352 
LYS CB     C  N N 353 
LYS CG     C  N N 354 
LYS CD     C  N N 355 
LYS CE     C  N N 356 
LYS NZ     N  N N 357 
LYS OXT    O  N N 358 
LYS H      H  N N 359 
LYS H2     H  N N 360 
LYS HA     H  N N 361 
LYS HB2    H  N N 362 
LYS HB3    H  N N 363 
LYS HG2    H  N N 364 
LYS HG3    H  N N 365 
LYS HD2    H  N N 366 
LYS HD3    H  N N 367 
LYS HE2    H  N N 368 
LYS HE3    H  N N 369 
LYS HZ1    H  N N 370 
LYS HZ2    H  N N 371 
LYS HZ3    H  N N 372 
LYS HXT    H  N N 373 
MES O1     O  N N 374 
MES C2     C  N N 375 
MES C3     C  N N 376 
MES N4     N  N N 377 
MES C5     C  N N 378 
MES C6     C  N N 379 
MES C7     C  N N 380 
MES C8     C  N N 381 
MES S      S  N N 382 
MES O1S    O  N N 383 
MES O2S    O  N N 384 
MES O3S    O  N N 385 
MES H21    H  N N 386 
MES H22    H  N N 387 
MES H31    H  N N 388 
MES H32    H  N N 389 
MES HN4    H  N N 390 
MES H51    H  N N 391 
MES H52    H  N N 392 
MES H61    H  N N 393 
MES H62    H  N N 394 
MES H71    H  N N 395 
MES H72    H  N N 396 
MES H81    H  N N 397 
MES H82    H  N N 398 
MET N      N  N N 399 
MET CA     C  N S 400 
MET C      C  N N 401 
MET O      O  N N 402 
MET CB     C  N N 403 
MET CG     C  N N 404 
MET SD     S  N N 405 
MET CE     C  N N 406 
MET OXT    O  N N 407 
MET H      H  N N 408 
MET H2     H  N N 409 
MET HA     H  N N 410 
MET HB2    H  N N 411 
MET HB3    H  N N 412 
MET HG2    H  N N 413 
MET HG3    H  N N 414 
MET HE1    H  N N 415 
MET HE2    H  N N 416 
MET HE3    H  N N 417 
MET HXT    H  N N 418 
PHE N      N  N N 419 
PHE CA     C  N S 420 
PHE C      C  N N 421 
PHE O      O  N N 422 
PHE CB     C  N N 423 
PHE CG     C  Y N 424 
PHE CD1    C  Y N 425 
PHE CD2    C  Y N 426 
PHE CE1    C  Y N 427 
PHE CE2    C  Y N 428 
PHE CZ     C  Y N 429 
PHE OXT    O  N N 430 
PHE H      H  N N 431 
PHE H2     H  N N 432 
PHE HA     H  N N 433 
PHE HB2    H  N N 434 
PHE HB3    H  N N 435 
PHE HD1    H  N N 436 
PHE HD2    H  N N 437 
PHE HE1    H  N N 438 
PHE HE2    H  N N 439 
PHE HZ     H  N N 440 
PHE HXT    H  N N 441 
PRO N      N  N N 442 
PRO CA     C  N S 443 
PRO C      C  N N 444 
PRO O      O  N N 445 
PRO CB     C  N N 446 
PRO CG     C  N N 447 
PRO CD     C  N N 448 
PRO OXT    O  N N 449 
PRO H      H  N N 450 
PRO HA     H  N N 451 
PRO HB2    H  N N 452 
PRO HB3    H  N N 453 
PRO HG2    H  N N 454 
PRO HG3    H  N N 455 
PRO HD2    H  N N 456 
PRO HD3    H  N N 457 
PRO HXT    H  N N 458 
SER N      N  N N 459 
SER CA     C  N S 460 
SER C      C  N N 461 
SER O      O  N N 462 
SER CB     C  N N 463 
SER OG     O  N N 464 
SER OXT    O  N N 465 
SER H      H  N N 466 
SER H2     H  N N 467 
SER HA     H  N N 468 
SER HB2    H  N N 469 
SER HB3    H  N N 470 
SER HG     H  N N 471 
SER HXT    H  N N 472 
THR N      N  N N 473 
THR CA     C  N S 474 
THR C      C  N N 475 
THR O      O  N N 476 
THR CB     C  N R 477 
THR OG1    O  N N 478 
THR CG2    C  N N 479 
THR OXT    O  N N 480 
THR H      H  N N 481 
THR H2     H  N N 482 
THR HA     H  N N 483 
THR HB     H  N N 484 
THR HG1    H  N N 485 
THR HG21   H  N N 486 
THR HG22   H  N N 487 
THR HG23   H  N N 488 
THR HXT    H  N N 489 
TRP N      N  N N 490 
TRP CA     C  N S 491 
TRP C      C  N N 492 
TRP O      O  N N 493 
TRP CB     C  N N 494 
TRP CG     C  Y N 495 
TRP CD1    C  Y N 496 
TRP CD2    C  Y N 497 
TRP NE1    N  Y N 498 
TRP CE2    C  Y N 499 
TRP CE3    C  Y N 500 
TRP CZ2    C  Y N 501 
TRP CZ3    C  Y N 502 
TRP CH2    C  Y N 503 
TRP OXT    O  N N 504 
TRP H      H  N N 505 
TRP H2     H  N N 506 
TRP HA     H  N N 507 
TRP HB2    H  N N 508 
TRP HB3    H  N N 509 
TRP HD1    H  N N 510 
TRP HE1    H  N N 511 
TRP HE3    H  N N 512 
TRP HZ2    H  N N 513 
TRP HZ3    H  N N 514 
TRP HH2    H  N N 515 
TRP HXT    H  N N 516 
TYR N      N  N N 517 
TYR CA     C  N S 518 
TYR C      C  N N 519 
TYR O      O  N N 520 
TYR CB     C  N N 521 
TYR CG     C  Y N 522 
TYR CD1    C  Y N 523 
TYR CD2    C  Y N 524 
TYR CE1    C  Y N 525 
TYR CE2    C  Y N 526 
TYR CZ     C  Y N 527 
TYR OH     O  N N 528 
TYR OXT    O  N N 529 
TYR H      H  N N 530 
TYR H2     H  N N 531 
TYR HA     H  N N 532 
TYR HB2    H  N N 533 
TYR HB3    H  N N 534 
TYR HD1    H  N N 535 
TYR HD2    H  N N 536 
TYR HE1    H  N N 537 
TYR HE2    H  N N 538 
TYR HH     H  N N 539 
TYR HXT    H  N N 540 
VAL N      N  N N 541 
VAL CA     C  N S 542 
VAL C      C  N N 543 
VAL O      O  N N 544 
VAL CB     C  N N 545 
VAL CG1    C  N N 546 
VAL CG2    C  N N 547 
VAL OXT    O  N N 548 
VAL H      H  N N 549 
VAL H2     H  N N 550 
VAL HA     H  N N 551 
VAL HB     H  N N 552 
VAL HG11   H  N N 553 
VAL HG12   H  N N 554 
VAL HG13   H  N N 555 
VAL HG21   H  N N 556 
VAL HG22   H  N N 557 
VAL HG23   H  N N 558 
VAL HXT    H  N N 559 
# 
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 
9EZ5 'double helix'        
9EZ5 '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 -0.263 -0.234 0.264  -10.006 -12.627 -3.436 1  E_DG1:DC13_F E 1  ? F 13 ? 19 1 
1 B DT 2  1_555 C DA 12 1_555 -0.275 -0.070 0.169  -6.695  -10.476 0.556  2  E_DT2:DA12_F E 2  ? F 12 ? 20 1 
1 B DC 3  1_555 C DG 11 1_555 0.247  -0.140 0.041  -4.710  -9.645  1.426  3  E_DC3:DG11_F E 3  ? F 11 ? 19 1 
1 B DT 4  1_555 C DA 10 1_555 -0.134 -0.165 0.225  -0.842  -2.795  5.887  4  E_DT4:DA10_F E 4  ? F 10 ? 20 1 
1 B DG 5  1_555 C DC 9  1_555 -0.397 -0.265 -0.023 -4.083  -12.333 -1.950 5  E_DG5:DC9_F  E 5  ? F 9  ? 19 1 
1 B DC 6  1_555 C DG 8  1_555 0.143  -0.127 0.137  -5.784  -6.812  0.172  6  E_DC6:DG8_F  E 6  ? F 8  ? 19 1 
1 B DA 7  1_555 C DT 7  1_555 0.254  -0.121 0.171  2.072   1.761   2.314  7  E_DA7:DT7_F  E 7  ? F 7  ? 20 1 
1 B DT 8  1_555 C DA 6  1_555 -0.196 -0.107 -0.041 8.524   -11.893 -1.967 8  E_DT8:DA6_F  E 8  ? F 6  ? 20 1 
1 B DT 9  1_555 C DA 5  1_555 -0.076 -0.153 -0.395 10.926  -16.613 1.392  9  E_DT9:DA5_F  E 9  ? F 5  ? 20 1 
1 B DC 10 1_555 C DG 4  1_555 0.083  -0.128 0.465  -13.152 -7.817  -1.746 10 E_DC10:DG4_F E 10 ? F 4  ? 19 1 
1 B DC 11 1_555 C DG 3  1_555 0.111  -0.087 0.314  -12.120 -0.187  -0.205 11 E_DC11:DG3_F E 11 ? F 3  ? 19 1 
1 B DT 12 1_555 C DA 2  1_555 -0.081 -0.130 0.087  -2.438  -12.546 -0.704 12 E_DT12:DA2_F E 12 ? F 2  ? 20 1 
1 B DC 13 1_555 C DG 1  1_555 0.266  -0.181 -0.280 4.149   -14.056 -2.997 13 E_DC13:DG1_F E 13 ? F 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 -0.667 -0.890 3.246 1.962  2.525  33.145 -1.964 1.483  3.128 4.414   
-3.430 33.295 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 -0.173 -0.067 3.237 1.396  2.456  36.388 -0.443 0.467  3.217 3.925   
-2.231 36.494 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 0.428  0.231  3.341 -0.750 4.310  31.705 -0.379 -0.916 3.332 7.842   
1.365  31.997 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 -0.895 0.016  3.402 0.693  1.151  35.942 -0.144 1.553  3.384 1.864   
-1.122 35.966 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 0.931  -0.352 3.422 0.722  -1.773 37.986 -0.303 -1.333 3.450 -2.722  
-1.109 38.033 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 0.754  -0.761 3.477 -2.442 7.849  24.210 -3.995 -2.414 2.997 18.060  
5.620  25.547 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 -0.793 -0.745 3.427 4.092  -8.979 32.379 0.265  2.068  3.385 -15.655 
-7.134 33.811 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 -0.547 -0.501 3.255 2.866  -4.277 33.670 -0.176 1.390  3.236 -7.331  
-4.912 34.050 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 0.050  -0.635 3.958 -6.072 -2.966 44.549 -0.504 -0.729 3.951 -3.886  
7.955  45.033 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 0.195  0.231  3.350 0.421  -3.741 37.700 0.845  -0.245 3.315 -5.771  
-0.649 37.881 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 -1.138 0.273  3.109 0.281  -1.646 30.730 0.818  2.196  3.080 -3.104  
-0.530 30.774 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 0.466  0.254  3.085 4.031  0.055  37.185 0.388  -0.223 3.117 0.086   
-6.298 37.395 12 EE_DT12DC13:DG1DA2_FF E 12 ? F 2  ? E 13 ? F 1  ? 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                France 
_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 from experimental phasing' 
# 
_atom_sites.entry_id                    9EZ5 
_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]   0.010154 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007542 
_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]   0.015688 
_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  
CL 
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_site.pdbx_tls_group_id 
ATOM   1    N  N     . MET A 1 1   ? 26.963  -9.964  5.132   1   17.09  ? 1    MET A N     1 1 
ATOM   2    C  CA    . MET A 1 1   ? 26.676  -8.786  5.949   1   17.5   ? 1    MET A CA    1 1 
ATOM   3    C  C     . MET A 1 1   ? 26.461  -7.582  5.061   1   17.73  ? 1    MET A C     1 1 
ATOM   4    O  O     . MET A 1 1   ? 27.083  -7.494  3.997   1   19.03  ? 1    MET A O     1 1 
ATOM   5    C  CB    . MET A 1 1   ? 27.826  -8.519  6.95    1   18.38  ? 1    MET A CB    1 1 
ATOM   6    C  CG    . MET A 1 1   ? 27.585  -7.281  7.818   1   22.35  ? 1    MET A CG    1 1 
ATOM   7    S  SD    . MET A 1 1   ? 28.812  -7.012  9.106   1   30.26  ? 1    MET A SD    1 1 
ATOM   8    C  CE    . MET A 1 1   ? 30.145  -6.576  8.126   1   27.23  ? 1    MET A CE    1 1 
ATOM   9    N  N     . ASN A 1 2   ? 25.607  -6.648  5.486   1   16.19  ? 2    ASN A N     1 1 
ATOM   10   C  CA    . ASN A 1 2   ? 25.452  -5.392  4.776   1   16.16  ? 2    ASN A CA    1 1 
ATOM   11   C  C     . ASN A 1 2   ? 25.848  -4.244  5.681   1   15.78  ? 2    ASN A C     1 1 
ATOM   12   O  O     . ASN A 1 2   ? 25.577  -4.271  6.884   1   15.77  ? 2    ASN A O     1 1 
ATOM   13   C  CB    . ASN A 1 2   ? 24.062  -5.207  4.191   1   17.98  ? 2    ASN A CB    1 1 
ATOM   14   C  CG    . ASN A 1 2   ? 23.923  -5.964  2.898   1   23.17  ? 2    ASN A CG    1 1 
ATOM   15   O  OD1   . ASN A 1 2   ? 24.901  -6.101  2.128   1   26.43  ? 2    ASN A OD1   1 1 
ATOM   16   N  ND2   . ASN A 1 2   ? 22.738  -6.489  2.642   1   21.38  ? 2    ASN A ND2   1 1 
ATOM   17   N  N     . VAL A 1 3   ? 26.541  -3.253  5.116   1   15.22  ? 3    VAL A N     1 1 
ATOM   18   C  CA    . VAL A 1 3   ? 26.987  -2.103  5.892   1   15.04  ? 3    VAL A CA    1 1 
ATOM   19   C  C     . VAL A 1 3   ? 26.352  -0.834  5.345   1   15.31  ? 3    VAL A C     1 1 
ATOM   20   O  O     . VAL A 1 3   ? 26.291  -0.63   4.131   1   15.59  ? 3    VAL A O     1 1 
ATOM   21   C  CB    . VAL A 1 3   ? 28.538  -2.014  5.947   1   15.35  ? 3    VAL A CB    1 1 
ATOM   22   C  CG1   . VAL A 1 3   ? 29      -0.76   6.678   1   15.84  ? 3    VAL A CG1   1 1 
ATOM   23   C  CG2   . VAL A 1 3   ? 29.126  -3.255  6.602   1   15.6   ? 3    VAL A CG2   1 1 
ATOM   24   N  N     . PHE A 1 4   ? 25.858  0.004   6.263   1   14.86  ? 4    PHE A N     1 1 
ATOM   25   C  CA    . PHE A 1 4   ? 25.236  1.289   5.995   1   14.85  ? 4    PHE A CA    1 1 
ATOM   26   C  C     . PHE A 1 4   ? 25.942  2.356   6.796   1   15.44  ? 4    PHE A C     1 1 
ATOM   27   O  O     . PHE A 1 4   ? 26.428  2.086   7.897   1   16.32  ? 4    PHE A O     1 1 
ATOM   28   C  CB    . PHE A 1 4   ? 23.767  1.275   6.416   1   13.99  ? 4    PHE A CB    1 1 
ATOM   29   C  CG    . PHE A 1 4   ? 22.985  0.184   5.739   1   13.69  ? 4    PHE A CG    1 1 
ATOM   30   C  CD1   . PHE A 1 4   ? 22.502  0.354   4.455   1   13.88  ? 4    PHE A CD1   1 1 
ATOM   31   C  CD2   . PHE A 1 4   ? 22.769  -1.035  6.373   1   14.29  ? 4    PHE A CD2   1 1 
ATOM   32   C  CE1   . PHE A 1 4   ? 21.748  -0.646  3.846   1   13.99  ? 4    PHE A CE1   1 1 
ATOM   33   C  CE2   . PHE A 1 4   ? 22.062  -2.047  5.743   1   14.76  ? 4    PHE A CE2   1 1 
ATOM   34   C  CZ    . PHE A 1 4   ? 21.548  -1.838  4.488   1   14.2   ? 4    PHE A CZ    1 1 
ATOM   35   N  N     . ARG A 1 5   ? 26.03   3.549   6.242   1   15.11  ? 5    ARG A N     1 1 
ATOM   36   C  CA    . ARG A 1 5   ? 26.606  4.659   6.981   1   16.22  ? 5    ARG A CA    1 1 
ATOM   37   C  C     . ARG A 1 5   ? 25.53   5.683   7.272   1   16.54  ? 5    ARG A C     1 1 
ATOM   38   O  O     . ARG A 1 5   ? 24.652  5.907   6.456   1   16.61  ? 5    ARG A O     1 1 
ATOM   39   C  CB    . ARG A 1 5   ? 27.832  5.276   6.276   1   17.25  ? 5    ARG A CB    1 1 
ATOM   40   C  CG    . ARG A 1 5   ? 29.049  4.345   6.318   1   17.98  ? 5    ARG A CG    1 1 
ATOM   41   C  CD    . ARG A 1 5   ? 30.169  4.855   5.434   1   19.03  ? 5    ARG A CD    1 1 
ATOM   42   N  NE    . ARG A 1 5   ? 31.423  4.121   5.658   1   18.93  ? 5    ARG A NE    1 1 
ATOM   43   C  CZ    . ARG A 1 5   ? 32.619  4.54    5.258   1   19.82  ? 5    ARG A CZ    1 1 
ATOM   44   N  NH1   . ARG A 1 5   ? 32.742  5.677   4.59    1   18.37  ? 5    ARG A NH1   1 1 
ATOM   45   N  NH2   . ARG A 1 5   ? 33.705  3.821   5.524   1   19.33  ? 5    ARG A NH2   1 1 
ATOM   46   N  N     . ILE A 1 6   ? 25.595  6.286   8.446   1   16.12  ? 6    ILE A N     1 1 
ATOM   47   C  CA    . ILE A 1 6   ? 24.68   7.331   8.852   1   15.07  ? 6    ILE A CA    1 1 
ATOM   48   C  C     . ILE A 1 6   ? 25.574  8.524   9.11    1   14.69  ? 6    ILE A C     1 1 
ATOM   49   O  O     . ILE A 1 6   ? 26.306  8.542   10.091  1   13.28  ? 6    ILE A O     1 1 
ATOM   50   C  CB    . ILE A 1 6   ? 23.891  6.94    10.118  1   15.52  ? 6    ILE A CB    1 1 
ATOM   51   C  CG1   . ILE A 1 6   ? 23.141  5.6     9.89    1   16.84  ? 6    ILE A CG1   1 1 
ATOM   52   C  CG2   . ILE A 1 6   ? 22.926  8.069   10.535  1   16.53  ? 6    ILE A CG2   1 1 
ATOM   53   C  CD1   . ILE A 1 6   ? 22.242  5.18    10.975  1   17.75  ? 6    ILE A CD1   1 1 
ATOM   54   N  N     . HIS A 1 7   ? 25.539  9.498   8.198   1   14.88  ? 7    HIS A N     1 1 
ATOM   55   C  CA    . HIS A 1 7   ? 26.302  10.73   8.286   1   14.97  ? 7    HIS A CA    1 1 
ATOM   56   C  C     . HIS A 1 7   ? 25.327  11.728  8.886   1   17.21  ? 7    HIS A C     1 1 
ATOM   57   O  O     . HIS A 1 7   ? 24.247  11.929  8.337   1   16.74  ? 7    HIS A O     1 1 
ATOM   58   C  CB    . HIS A 1 7   ? 26.72   11.171  6.888   1   13.92  ? 7    HIS A CB    1 1 
ATOM   59   C  CG    . HIS A 1 7   ? 27.592  10.181  6.188   1   14.81  ? 7    HIS A CG    1 1 
ATOM   60   N  ND1   . HIS A 1 7   ? 28.979  10.24   6.288   1   16.44  ? 7    HIS A ND1   1 1 
ATOM   61   C  CD2   . HIS A 1 7   ? 27.256  9.142   5.387   1   14.58  ? 7    HIS A CD2   1 1 
ATOM   62   C  CE1   . HIS A 1 7   ? 29.428  9.23    5.554   1   16.24  ? 7    HIS A CE1   1 1 
ATOM   63   N  NE2   . HIS A 1 7   ? 28.424  8.56    4.976   1   15.1   ? 7    HIS A NE2   1 1 
ATOM   64   N  N     . GLY A 1 8   ? 25.662  12.269  10.048  1   18.26  ? 8    GLY A N     1 1 
ATOM   65   C  CA    . GLY A 1 8   ? 24.766  13.185  10.727  1   19.72  ? 8    GLY A CA    1 1 
ATOM   66   C  C     . GLY A 1 8   ? 25.452  14.45   11.191  1   21.65  ? 8    GLY A C     1 1 
ATOM   67   O  O     . GLY A 1 8   ? 26.673  14.559  11.163  1   21.93  ? 8    GLY A O     1 1 
ATOM   68   N  N     . ASP A 1 9   ? 24.652  15.407  11.61   1   22.79  ? 9    ASP A N     1 1 
ATOM   69   C  CA    . ASP A 1 9   ? 25.146  16.679  12.116  1   24.42  ? 9    ASP A CA    1 1 
ATOM   70   C  C     . ASP A 1 9   ? 25.838  16.479  13.484  1   22.99  ? 9    ASP A C     1 1 
ATOM   71   O  O     . ASP A 1 9   ? 26.775  17.197  13.798  1   22.76  ? 9    ASP A O     1 1 
ATOM   72   C  CB    . ASP A 1 9   ? 23.968  17.665  12.199  1   29.49  ? 9    ASP A CB    1 1 
ATOM   73   C  CG    . ASP A 1 9   ? 24.297  18.998  12.816  1   39.19  ? 9    ASP A CG    1 1 
ATOM   74   O  OD1   . ASP A 1 9   ? 25.383  19.549  12.495  1   41.32  ? 9    ASP A OD1   1 1 
ATOM   75   O  OD2   . ASP A 1 9   ? 23.46   19.506  13.615  1   42.86  ? 9    ASP A OD2   1 1 
ATOM   76   N  N     . ASN A 1 10  ? 25.42   15.453  14.246  1   21.96  ? 10   ASN A N     1 1 
ATOM   77   C  CA    . ASN A 1 10  ? 25.98   15.065  15.536  1   21.68  ? 10   ASN A CA    1 1 
ATOM   78   C  C     . ASN A 1 10  ? 25.534  13.612  15.888  1   21.77  ? 10   ASN A C     1 1 
ATOM   79   O  O     . ASN A 1 10  ? 24.716  13.032  15.173  1   21.75  ? 10   ASN A O     1 1 
ATOM   80   C  CB    . ASN A 1 10  ? 25.61   16.081  16.62   1   22.48  ? 10   ASN A CB    1 1 
ATOM   81   C  CG    . ASN A 1 10  ? 24.137  16.28   16.762  1   25.54  ? 10   ASN A CG    1 1 
ATOM   82   O  OD1   . ASN A 1 10  ? 23.399  15.35   17.095  1   26.23  ? 10   ASN A OD1   1 1 
ATOM   83   N  ND2   . ASN A 1 10  ? 23.682  17.518  16.531  1   26.45  ? 10   ASN A ND2   1 1 
ATOM   84   N  N     . ILE A 1 11  ? 26.072  13.024  16.97   1   21.77  ? 11   ILE A N     1 1 
ATOM   85   C  CA    . ILE A 1 11  ? 25.731  11.657  17.344  1   22.25  ? 11   ILE A CA    1 1 
ATOM   86   C  C     . ILE A 1 11  ? 24.241  11.483  17.666  1   22.89  ? 11   ILE A C     1 1 
ATOM   87   O  O     . ILE A 1 11  ? 23.69   10.454  17.293  1   23.31  ? 11   ILE A O     1 1 
ATOM   88   C  CB    . ILE A 1 11  ? 26.654  11.118  18.466  1   22.54  ? 11   ILE A CB    1 1 
ATOM   89   C  CG1   . ILE A 1 11  ? 26.53   9.594   18.639  1   23.06  ? 11   ILE A CG1   1 1 
ATOM   90   C  CG2   . ILE A 1 11  ? 26.439  11.867  19.772  1   23.28  ? 11   ILE A CG2   1 1 
ATOM   91   C  CD1   . ILE A 1 11  ? 26.827  8.789   17.363  1   23.61  ? 11   ILE A CD1   1 1 
ATOM   92   N  N     . ILE A 1 12  ? 23.558  12.496  18.27   1   22.81  ? 12   ILE A N     1 1 
ATOM   93   C  CA    . ILE A 1 12  ? 22.136  12.387  18.596  1   22.77  ? 12   ILE A CA    1 1 
ATOM   94   C  C     . ILE A 1 12  ? 21.281  12.215  17.331  1   21.56  ? 12   ILE A C     1 1 
ATOM   95   O  O     . ILE A 1 12  ? 20.392  11.383  17.325  1   20.8   ? 12   ILE A O     1 1 
ATOM   96   C  CB    . ILE A 1 12  ? 21.649  13.556  19.518  1   24.37  ? 12   ILE A CB    1 1 
ATOM   97   C  CG1   . ILE A 1 12  ? 22.171  13.339  20.955  1   26.28  ? 12   ILE A CG1   1 1 
ATOM   98   C  CG2   . ILE A 1 12  ? 20.106  13.693  19.532  1   24.58  ? 12   ILE A CG2   1 1 
ATOM   99   C  CD1   . ILE A 1 12  ? 22.048  14.563  21.88   1   28.11  ? 12   ILE A CD1   1 1 
ATOM   100  N  N     . GLU A 1 13  ? 21.58   12.959  16.258  1   21.58  ? 13   GLU A N     1 1 
ATOM   101  C  CA    . GLU A 1 13  ? 20.834  12.834  15.009  1   22.11  ? 13   GLU A CA    1 1 
ATOM   102  C  C     . GLU A 1 13  ? 21.053  11.435  14.4    1   22.43  ? 13   GLU A C     1 1 
ATOM   103  O  O     . GLU A 1 13  ? 20.083  10.798  13.955  1   22.7   ? 13   GLU A O     1 1 
ATOM   104  C  CB    . GLU A 1 13  ? 21.256  13.903  14.006  1   25.35  ? 13   GLU A CB    1 1 
ATOM   105  C  CG    . GLU A 1 13  ? 21.146  15.322  14.533  1   35.31  ? 13   GLU A CG    1 1 
ATOM   106  C  CD    . GLU A 1 13  ? 19.757  15.912  14.46   1   47.95  ? 13   GLU A CD    1 1 
ATOM   107  O  OE1   . GLU A 1 13  ? 18.776  15.143  14.334  1   51.26  ? 13   GLU A OE1   1 1 
ATOM   108  O  OE2   . GLU A 1 13  ? 19.65   17.157  14.526  1   53     ? 13   GLU A OE2   1 1 
ATOM   109  N  N     . CYS A 1 14  ? 22.31   10.937  14.425  1   21.05  ? 14   CYS A N     1 1 
ATOM   110  C  CA    . CYS A 1 14  ? 22.636  9.584   13.931  1   20.79  ? 14   CYS A CA    1 1 
ATOM   111  C  C     . CYS A 1 14  ? 21.834  8.553   14.687  1   20.98  ? 14   CYS A C     1 1 
ATOM   112  O  O     . CYS A 1 14  ? 21.151  7.723   14.07   1   21.27  ? 14   CYS A O     1 1 
ATOM   113  C  CB    . CYS A 1 14  ? 24.135  9.299   14.023  1   21.22  ? 14   CYS A CB    1 1 
ATOM   114  S  SG    . CYS A 1 14  ? 25.173  10.417  13.041  1   23.93  ? 14   CYS A SG    1 1 
ATOM   115  N  N     . GLU A 1 15  ? 21.813  8.674   16.018  1   20.66  ? 15   GLU A N     1 1 
ATOM   116  C  CA    . GLU A 1 15  ? 21.097  7.725   16.863  1   20.72  ? 15   GLU A CA    1 1 
ATOM   117  C  C     . GLU A 1 15  ? 19.588  7.772   16.709  1   21.89  ? 15   GLU A C     1 1 
ATOM   118  O  O     . GLU A 1 15  ? 18.956  6.731   16.878  1   22.28  ? 15   GLU A O     1 1 
ATOM   119  C  CB    . GLU A 1 15  ? 21.526  7.84    18.324  1   21.66  ? 15   GLU A CB    1 1 
ATOM   120  C  CG    . GLU A 1 15  ? 22.993  7.445   18.5    1   24.03  ? 15   GLU A CG    1 1 
ATOM   121  C  CD    . GLU A 1 15  ? 23.303  5.959   18.4    1   31.29  ? 15   GLU A CD    1 1 
ATOM   122  O  OE1   . GLU A 1 15  ? 22.365  5.154   18.204  1   30.6   ? 15   GLU A OE1   1 1 
ATOM   123  O  OE2   . GLU A 1 15  ? 24.487  5.593   18.557  1   37.98  ? 15   GLU A OE2   1 1 
ATOM   124  N  N     . ARG A 1 16  ? 19.015  8.91    16.274  1   22.57  ? 16   ARG A N     1 1 
ATOM   125  C  CA    . ARG A 1 16  ? 17.58   8.995   15.998  1   23.2   ? 16   ARG A CA    1 1 
ATOM   126  C  C     . ARG A 1 16  ? 17.183  8.064   14.87   1   21.55  ? 16   ARG A C     1 1 
ATOM   127  O  O     . ARG A 1 16  ? 16.118  7.473   14.935  1   21.13  ? 16   ARG A O     1 1 
ATOM   128  C  CB    . ARG A 1 16  ? 17.135  10.429  15.69   1   27.38  ? 16   ARG A CB    1 1 
ATOM   129  C  CG    . ARG A 1 16  ? 17.195  11.307  16.918  1   35.15  ? 16   ARG A CG    1 1 
ATOM   130  C  CD    . ARG A 1 16  ? 16.032  12.262  17.05   1   41.78  ? 16   ARG A CD    1 1 
ATOM   131  N  NE    . ARG A 1 16  ? 16.234  13.502  16.302  1   48.41  ? 16   ARG A NE    1 1 
ATOM   132  C  CZ    . ARG A 1 16  ? 16.542  14.676  16.851  1   52.77  ? 16   ARG A CZ    1 1 
ATOM   133  N  NH1   . ARG A 1 16  ? 16.731  14.775  18.162  1   53.37  ? 16   ARG A NH1   1 1 
ATOM   134  N  NH2   . ARG A 1 16  ? 16.682  15.753  16.09   1   53.01  ? 16   ARG A NH2   1 1 
ATOM   135  N  N     . VAL A 1 17  ? 18.035  7.905   13.853  1   20.6   ? 17   VAL A N     1 1 
ATOM   136  C  CA    . VAL A 1 17  ? 17.75   6.983   12.759  1   20.81  ? 17   VAL A CA    1 1 
ATOM   137  C  C     . VAL A 1 17  ? 17.772  5.525   13.26   1   20.97  ? 17   VAL A C     1 1 
ATOM   138  O  O     . VAL A 1 17  ? 16.89   4.754   12.906  1   21.48  ? 17   VAL A O     1 1 
ATOM   139  C  CB    . VAL A 1 17  ? 18.705  7.201   11.582  1   21.57  ? 17   VAL A CB    1 1 
ATOM   140  C  CG1   . VAL A 1 17  ? 18.475  6.155   10.503  1   22.59  ? 17   VAL A CG1   1 1 
ATOM   141  C  CG2   . VAL A 1 17  ? 18.54   8.593   11.02   1   22.18  ? 17   VAL A CG2   1 1 
ATOM   142  N  N     . ILE A 1 18  ? 18.751  5.171   14.122  1   20.9   ? 18   ILE A N     1 1 
ATOM   143  C  CA    . ILE A 1 18  ? 18.869  3.838   14.723  1   21.36  ? 18   ILE A CA    1 1 
ATOM   144  C  C     . ILE A 1 18  ? 17.632  3.534   15.549  1   22.23  ? 18   ILE A C     1 1 
ATOM   145  O  O     . ILE A 1 18  ? 17.079  2.462   15.407  1   22.6   ? 18   ILE A O     1 1 
ATOM   146  C  CB    . ILE A 1 18  ? 20.174  3.722   15.574  1   21.35  ? 18   ILE A CB    1 1 
ATOM   147  C  CG1   . ILE A 1 18  ? 21.443  3.96    14.73   1   20.69  ? 18   ILE A CG1   1 1 
ATOM   148  C  CG2   . ILE A 1 18  ? 20.247  2.4     16.337  1   21.96  ? 18   ILE A CG2   1 1 
ATOM   149  C  CD1   . ILE A 1 18  ? 21.575  3.037   13.622  1   21.27  ? 18   ILE A CD1   1 1 
ATOM   150  N  N     . ASP A 1 19  ? 17.137  4.497   16.35   1   22.59  ? 19   ASP A N     1 1 
ATOM   151  C  CA    . ASP A 1 19  ? 15.908  4.308   17.146  1   22.69  ? 19   ASP A CA    1 1 
ATOM   152  C  C     . ASP A 1 19  ? 14.711  4.043   16.267  1   21.99  ? 19   ASP A C     1 1 
ATOM   153  O  O     . ASP A 1 19  ? 13.867  3.223   16.636  1   22.85  ? 19   ASP A O     1 1 
ATOM   154  C  CB    . ASP A 1 19  ? 15.621  5.529   18.04   1   26.24  ? 19   ASP A CB    1 1 
ATOM   155  C  CG    . ASP A 1 19  ? 16.64   5.756   19.139  1   34.48  ? 19   ASP A CG    1 1 
ATOM   156  O  OD1   . ASP A 1 19  ? 17.424  4.826   19.426  1   37.07  ? 19   ASP A OD1   1 1 
ATOM   157  O  OD2   . ASP A 1 19  ? 16.65   6.857   19.72   1   38.66  ? 19   ASP A OD2   1 1 
ATOM   158  N  N     . LEU A 1 20  ? 14.611  4.709   15.107  1   20.83  ? 20   LEU A N     1 1 
ATOM   159  C  CA    . LEU A 1 20  ? 13.488  4.453   14.184  1   20.94  ? 20   LEU A CA    1 1 
ATOM   160  C  C     . LEU A 1 20  ? 13.562  3.013   13.663  1   22.12  ? 20   LEU A C     1 1 
ATOM   161  O  O     . LEU A 1 20  ? 12.556  2.318   13.624  1   22.99  ? 20   LEU A O     1 1 
ATOM   162  C  CB    . LEU A 1 20  ? 13.519  5.439   13.005  1   20.48  ? 20   LEU A CB    1 1 
ATOM   163  C  CG    . LEU A 1 20  ? 13.017  6.848   13.312  1   20.33  ? 20   LEU A CG    1 1 
ATOM   164  C  CD1   . LEU A 1 20  ? 13.401  7.824   12.208  1   19.77  ? 20   LEU A CD1   1 1 
ATOM   165  C  CD2   . LEU A 1 20  ? 11.519  6.826   13.557  1   20.71  ? 20   LEU A CD2   1 1 
ATOM   166  N  N     . ILE A 1 21  ? 14.766  2.544   13.313  1   22.09  ? 21   ILE A N     1 1 
ATOM   167  C  CA    . ILE A 1 21  ? 14.96   1.185   12.832  1   22.71  ? 21   ILE A CA    1 1 
ATOM   168  C  C     . ILE A 1 21  ? 14.608  0.19    13.942  1   23.49  ? 21   ILE A C     1 1 
ATOM   169  O  O     . ILE A 1 21  ? 13.792  -0.702  13.723  1   24.05  ? 21   ILE A O     1 1 
ATOM   170  C  CB    . ILE A 1 21  ? 16.408  1.006   12.317  1   23.19  ? 21   ILE A CB    1 1 
ATOM   171  C  CG1   . ILE A 1 21  ? 16.613  1.779   11.014  1   24.1   ? 21   ILE A CG1   1 1 
ATOM   172  C  CG2   . ILE A 1 21  ? 16.783  -0.472  12.151  1   24.23  ? 21   ILE A CG2   1 1 
ATOM   173  C  CD1   . ILE A 1 21  ? 18.069  2.106   10.717  1   25.8   ? 21   ILE A CD1   1 1 
ATOM   174  N  N     . LEU A 1 22  ? 15.142  0.411   15.147  1   23.78  ? 22   LEU A N     1 1 
ATOM   175  C  CA    . LEU A 1 22  ? 14.921  -0.465  16.291  1   24.88  ? 22   LEU A CA    1 1 
ATOM   176  C  C     . LEU A 1 22  ? 13.48   -0.495  16.797  1   27.22  ? 22   LEU A C     1 1 
ATOM   177  O  O     . LEU A 1 22  ? 13.128  -1.429  17.52   1   27.95  ? 22   LEU A O     1 1 
ATOM   178  C  CB    . LEU A 1 22  ? 15.902  -0.162  17.439  1   24.13  ? 22   LEU A CB    1 1 
ATOM   179  C  CG    . LEU A 1 22  ? 17.363  -0.437  17.108  1   24.62  ? 22   LEU A CG    1 1 
ATOM   180  C  CD1   . LEU A 1 22  ? 18.276  -0.048  18.253  1   24.61  ? 22   LEU A CD1   1 1 
ATOM   181  C  CD2   . LEU A 1 22  ? 17.585  -1.898  16.738  1   24.87  ? 22   LEU A CD2   1 1 
ATOM   182  N  N     . SER A 1 23  ? 12.633  0.462   16.366  1   28.24  ? 23   SER A N     1 1 
ATOM   183  C  CA    . SER A 1 23  ? 11.209  0.504   16.697  1   29.25  ? 23   SER A CA    1 1 
ATOM   184  C  C     . SER A 1 23  ? 10.42   -0.586  15.929  1   30.61  ? 23   SER A C     1 1 
ATOM   185  O  O     . SER A 1 23  ? 9.326   -0.959  16.351  1   31.4   ? 23   SER A O     1 1 
ATOM   186  C  CB    . SER A 1 23  ? 10.627  1.884   16.391  1   30.18  ? 23   SER A CB    1 1 
ATOM   187  O  OG    . SER A 1 23  ? 10.367  2.093   15.01   1   31.06  ? 23   SER A OG    1 1 
ATOM   188  N  N     . LYS A 1 24  ? 10.942  -1.052  14.782  1   30.36  ? 24   LYS A N     1 1 
ATOM   189  C  CA    . LYS A 1 24  ? 10.277  -2.074  13.984  1   30.97  ? 24   LYS A CA    1 1 
ATOM   190  C  C     . LYS A 1 24  ? 11.083  -3.392  13.976  1   31.18  ? 24   LYS A C     1 1 
ATOM   191  O  O     . LYS A 1 24  ? 10.507  -4.471  13.901  1   31.01  ? 24   LYS A O     1 1 
ATOM   192  C  CB    . LYS A 1 24  ? 10.013  -1.567  12.56   1   33.88  ? 24   LYS A CB    1 1 
ATOM   193  C  CG    . LYS A 1 24  ? 9.215   -2.557  11.717  1   41.05  ? 24   LYS A CG    1 1 
ATOM   194  C  CD    . LYS A 1 24  ? 9.171   -2.187  10.247  1   47.45  ? 24   LYS A CD    1 1 
ATOM   195  C  CE    . LYS A 1 24  ? 8.875   -3.366  9.342   1   51.35  ? 24   LYS A CE    1 1 
ATOM   196  N  NZ    . LYS A 1 24  ? 8.955   -2.976  7.909   1   53.3   ? 24   LYS A NZ    1 1 
ATOM   197  N  N     . ILE A 1 25  ? 12.406  -3.298  14.067  1   31.68  ? 25   ILE A N     1 1 
ATOM   198  C  CA    . ILE A 1 25  ? 13.261  -4.469  14.128  1   32.91  ? 25   ILE A CA    1 1 
ATOM   199  C  C     . ILE A 1 25  ? 13.426  -4.839  15.592  1   33.95  ? 25   ILE A C     1 1 
ATOM   200  O  O     . ILE A 1 25  ? 13.852  -3.987  16.381  1   34.71  ? 25   ILE A O     1 1 
ATOM   201  C  CB    . ILE A 1 25  ? 14.674  -4.151  13.562  1   33.38  ? 25   ILE A CB    1 1 
ATOM   202  C  CG1   . ILE A 1 25  ? 14.65   -3.666  12.1    1   34.34  ? 25   ILE A CG1   1 1 
ATOM   203  C  CG2   . ILE A 1 25  ? 15.594  -5.328  13.748  1   33.58  ? 25   ILE A CG2   1 1 
ATOM   204  C  CD1   . ILE A 1 25  ? 14.136  -4.625  11.112  1   35.55  ? 25   ILE A CD1   1 1 
ATOM   205  N  N     . ASN A 1 26  ? 13.155  -6.095  15.951  1   33.88  ? 26   ASN A N     1 1 
ATOM   206  C  CA    . ASN A 1 26  ? 13.461  -6.565  17.291  1   34.71  ? 26   ASN A CA    1 1 
ATOM   207  C  C     . ASN A 1 26  ? 14.651  -7.529  17.083  1   33.93  ? 26   ASN A C     1 1 
ATOM   208  O  O     . ASN A 1 26  ? 14.483  -8.638  16.561  1   34.19  ? 26   ASN A O     1 1 
ATOM   209  C  CB    . ASN A 1 26  ? 12.269  -7.247  17.952  1   37.8   ? 26   ASN A CB    1 1 
ATOM   210  C  CG    . ASN A 1 26  ? 12.641  -7.831  19.297  1   43.84  ? 26   ASN A CG    1 1 
ATOM   211  O  OD1   . ASN A 1 26  ? 13.49   -7.288  20.033  1   46.13  ? 26   ASN A OD1   1 1 
ATOM   212  N  ND2   . ASN A 1 26  ? 12.054  -8.972  19.625  1   45.02  ? 26   ASN A ND2   1 1 
ATOM   213  N  N     . PRO A 1 27  ? 15.873  -7.081  17.4    1   32.78  ? 27   PRO A N     1 1 
ATOM   214  C  CA    . PRO A 1 27  ? 17.047  -7.906  17.102  1   32.45  ? 27   PRO A CA    1 1 
ATOM   215  C  C     . PRO A 1 27  ? 17.29   -9.08   18.052  1   32.23  ? 27   PRO A C     1 1 
ATOM   216  O  O     . PRO A 1 27  ? 16.968  -9.02   19.233  1   33.17  ? 27   PRO A O     1 1 
ATOM   217  C  CB    . PRO A 1 27  ? 18.209  -6.894  17.121  1   33.06  ? 27   PRO A CB    1 1 
ATOM   218  C  CG    . PRO A 1 27  ? 17.57   -5.523  17.28   1   33.37  ? 27   PRO A CG    1 1 
ATOM   219  C  CD    . PRO A 1 27  ? 16.263  -5.773  17.954  1   32.01  ? 27   PRO A CD    1 1 
ATOM   220  N  N     . GLN A 1 28  ? 17.872  -10.141 17.527  1   30.9   ? 28   GLN A N     1 1 
ATOM   221  C  CA    . GLN A 1 28  ? 18.254  -11.32  18.297  1   30.8   ? 28   GLN A CA    1 1 
ATOM   222  C  C     . GLN A 1 28  ? 19.568  -11.007 19.05   1   30.27  ? 28   GLN A C     1 1 
ATOM   223  O  O     . GLN A 1 28  ? 19.747  -11.437 20.198  1   30.06  ? 28   GLN A O     1 1 
ATOM   224  C  CB    . GLN A 1 28  ? 18.486  -12.515 17.35   1   32.94  ? 28   GLN A CB    1 1 
ATOM   225  C  CG    . GLN A 1 28  ? 17.369  -12.726 16.331  1   39.48  ? 28   GLN A CG    1 1 
ATOM   226  C  CD    . GLN A 1 28  ? 16.092  -13.123 17.017  1   46.25  ? 28   GLN A CD    1 1 
ATOM   227  O  OE1   . GLN A 1 28  ? 15.992  -14.21  17.592  1   49.04  ? 28   GLN A OE1   1 1 
ATOM   228  N  NE2   . GLN A 1 28  ? 15.094  -12.251 16.985  1   46.97  ? 28   GLN A NE2   1 1 
ATOM   229  N  N     . LYS A 1 29  ? 20.51   -10.287 18.367  1   29.13  ? 29   LYS A N     1 1 
ATOM   230  C  CA    . LYS A 1 29  ? 21.807  -9.889  18.897  1   28.69  ? 29   LYS A CA    1 1 
ATOM   231  C  C     . LYS A 1 29  ? 22.106  -8.448  18.484  1   26.86  ? 29   LYS A C     1 1 
ATOM   232  O  O     . LYS A 1 29  ? 21.822  -8.05   17.351  1   26.03  ? 29   LYS A O     1 1 
ATOM   233  C  CB    . LYS A 1 29  ? 22.922  -10.826 18.38   1   31.27  ? 29   LYS A CB    1 1 
ATOM   234  C  CG    . LYS A 1 29  ? 22.651  -12.316 18.66   1   37.3   ? 29   LYS A CG    1 1 
ATOM   235  C  CD    . LYS A 1 29  ? 23.418  -13.244 17.727  1   41.96  ? 29   LYS A CD    1 1 
ATOM   236  C  CE    . LYS A 1 29  ? 23.056  -14.694 17.914  1   44.94  ? 29   LYS A CE    1 1 
ATOM   237  N  NZ    . LYS A 1 29  ? 24.184  -15.569 17.493  1   47.16  ? 29   LYS A NZ    1 1 
ATOM   238  N  N     . VAL A 1 30  ? 22.653  -7.662  19.423  1   25.94  ? 30   VAL A N     1 1 
ATOM   239  C  CA    . VAL A 1 30  ? 23.033  -6.259  19.2    1   25.71  ? 30   VAL A CA    1 1 
ATOM   240  C  C     . VAL A 1 30  ? 24.418  -6.072  19.795  1   24.55  ? 30   VAL A C     1 1 
ATOM   241  O  O     . VAL A 1 30  ? 24.619  -6.425  20.962  1   23.62  ? 30   VAL A O     1 1 
ATOM   242  C  CB    . VAL A 1 30  ? 22.071  -5.215  19.843  1   26.57  ? 30   VAL A CB    1 1 
ATOM   243  C  CG1   . VAL A 1 30  ? 22.571  -3.794  19.6    1   26.66  ? 30   VAL A CG1   1 1 
ATOM   244  C  CG2   . VAL A 1 30  ? 20.643  -5.359  19.341  1   27.86  ? 30   VAL A CG2   1 1 
ATOM   245  N  N     . LYS A 1 31  ? 25.352  -5.474  19.011  1   24.18  ? 31   LYS A N     1 1 
ATOM   246  C  CA    . LYS A 1 31  ? 26.699  -5.157  19.441  1   24.26  ? 31   LYS A CA    1 1 
ATOM   247  C  C     . LYS A 1 31  ? 27.012  -3.678  19.119  1   23.11  ? 31   LYS A C     1 1 
ATOM   248  O  O     . LYS A 1 31  ? 26.66   -3.172  18.051  1   22.36  ? 31   LYS A O     1 1 
ATOM   249  C  CB    . LYS A 1 31  ? 27.721  -6.08   18.775  1   28.73  ? 31   LYS A CB    1 1 
ATOM   250  C  CG    . LYS A 1 31  ? 29.169  -5.768  19.163  1   36.92  ? 31   LYS A CG    1 1 
ATOM   251  C  CD    . LYS A 1 31  ? 30.201  -6.751  18.582  1   44.62  ? 31   LYS A CD    1 1 
ATOM   252  C  CE    . LYS A 1 31  ? 31.609  -6.355  18.976  1   50.69  ? 31   LYS A CE    1 1 
ATOM   253  N  NZ    . LYS A 1 31  ? 32.444  -7.542  19.35   1   54.62  ? 31   LYS A NZ    1 1 
ATOM   254  N  N     . ARG A 1 32  ? 27.641  -2.981  20.057  1   22.4   ? 32   ARG A N     1 1 
ATOM   255  C  CA    . ARG A 1 32  ? 28.021  -1.591  19.849  1   22.38  ? 32   ARG A CA    1 1 
ATOM   256  C  C     . ARG A 1 32  ? 29.505  -1.399  20.096  1   22.54  ? 32   ARG A C     1 1 
ATOM   257  O  O     . ARG A 1 32  ? 30.117  -2.151  20.844  1   22.09  ? 32   ARG A O     1 1 
ATOM   258  C  CB    . ARG A 1 32  ? 27.177  -0.66   20.722  1   22.85  ? 32   ARG A CB    1 1 
ATOM   259  C  CG    . ARG A 1 32  ? 25.768  -0.408  20.191  1   22.33  ? 32   ARG A CG    1 1 
ATOM   260  C  CD    . ARG A 1 32  ? 25.098  0.59    21.102  1   24.51  ? 32   ARG A CD    1 1 
ATOM   261  N  NE    . ARG A 1 32  ? 23.757  0.979   20.661  1   27.39  ? 32   ARG A NE    1 1 
ATOM   262  C  CZ    . ARG A 1 32  ? 23.499  1.976   19.815  1   30.01  ? 32   ARG A CZ    1 1 
ATOM   263  N  NH1   . ARG A 1 32  ? 24.495  2.652   19.248  1   28.84  ? 32   ARG A NH1   1 1 
ATOM   264  N  NH2   . ARG A 1 32  ? 22.245  2.283   19.506  1   31.04  ? 32   ARG A NH2   1 1 
ATOM   265  N  N     . GLY A 1 33  ? 30.074  -0.392  19.463  1   22.19  ? 33   GLY A N     1 1 
ATOM   266  C  CA    . GLY A 1 33  ? 31.487  -0.081  19.627  1   21.57  ? 33   GLY A CA    1 1 
ATOM   267  C  C     . GLY A 1 33  ? 31.923  1.029   18.695  1   20.26  ? 33   GLY A C     1 1 
ATOM   268  O  O     . GLY A 1 33  ? 31.104  1.863   18.302  1   19.45  ? 33   GLY A O     1 1 
ATOM   269  N  N     . PHE A 1 34  ? 33.186  1.007   18.268  1   18.99  ? 34   PHE A N     1 1 
ATOM   270  C  CA    . PHE A 1 34  ? 33.704  2.031   17.359  1   18.87  ? 34   PHE A CA    1 1 
ATOM   271  C  C     . PHE A 1 34  ? 34.462  1.354   16.219  1   18.77  ? 34   PHE A C     1 1 
ATOM   272  O  O     . PHE A 1 34  ? 35.23   0.44    16.478  1   18.89  ? 34   PHE A O     1 1 
ATOM   273  C  CB    . PHE A 1 34  ? 34.716  2.952   18.134  1   18.7   ? 34   PHE A CB    1 1 
ATOM   274  C  CG    . PHE A 1 34  ? 34.109  4.033   19.005  1   20.13  ? 34   PHE A CG    1 1 
ATOM   275  C  CD1   . PHE A 1 34  ? 33.651  3.747   20.28   1   21.82  ? 34   PHE A CD1   1 1 
ATOM   276  C  CD2   . PHE A 1 34  ? 33.995  5.334   18.545  1   20.63  ? 34   PHE A CD2   1 1 
ATOM   277  C  CE1   . PHE A 1 34  ? 33.052  4.742   21.062  1   22.95  ? 34   PHE A CE1   1 1 
ATOM   278  C  CE2   . PHE A 1 34  ? 33.411  6.328   19.334  1   21.96  ? 34   PHE A CE2   1 1 
ATOM   279  C  CZ    . PHE A 1 34  ? 32.956  6.032   20.59   1   22.36  ? 34   PHE A CZ    1 1 
ATOM   280  N  N     . ILE A 1 35  ? 34.295  1.81    14.984  1   18.45  ? 35   ILE A N     1 1 
ATOM   281  C  CA    . ILE A 1 35  ? 35.127  1.317   13.864  1   18.82  ? 35   ILE A CA    1 1 
ATOM   282  C  C     . ILE A 1 35  ? 36.405  2.195   13.716  1   18.14  ? 35   ILE A C     1 1 
ATOM   283  O  O     . ILE A 1 35  ? 37.371  1.803   13.044  1   18.02  ? 35   ILE A O     1 1 
ATOM   284  C  CB    . ILE A 1 35  ? 34.353  1.254   12.525  1   20.81  ? 35   ILE A CB    1 1 
ATOM   285  C  CG1   . ILE A 1 35  ? 33.939  2.675   12.05   1   22.75  ? 35   ILE A CG1   1 1 
ATOM   286  C  CG2   . ILE A 1 35  ? 33.156  0.313   12.609  1   20.91  ? 35   ILE A CG2   1 1 
ATOM   287  C  CD1   . ILE A 1 35  ? 33.751  2.781   10.568  1   24.7   ? 35   ILE A CD1   1 1 
ATOM   288  N  N     . SER A 1 36  ? 36.383  3.407   14.314  1   17.23  ? 36   SER A N     1 1 
ATOM   289  C  CA    . SER A 1 36  ? 37.453  4.387   14.37   1   17.04  ? 36   SER A CA    1 1 
ATOM   290  C  C     . SER A 1 36  ? 37.183  5.246   15.627  1   16.58  ? 36   SER A C     1 1 
ATOM   291  O  O     . SER A 1 36  ? 36.175  5.044   16.297  1   15.83  ? 36   SER A O     1 1 
ATOM   292  C  CB    . SER A 1 36  ? 37.461  5.249   13.108  1   18.44  ? 36   SER A CB    1 1 
ATOM   293  O  OG    . SER A 1 36  ? 36.472  6.28    13.135  1   19.35  ? 36   SER A OG    1 1 
ATOM   294  N  N     . LEU A 1 37  ? 38.063  6.196   15.939  1   16.38  ? 37   LEU A N     1 1 
ATOM   295  C  CA    . LEU A 1 37  ? 37.902  7.05    17.111  1   16.74  ? 37   LEU A CA    1 1 
ATOM   296  C  C     . LEU A 1 37  ? 36.673  7.944   17.026  1   16.91  ? 37   LEU A C     1 1 
ATOM   297  O  O     . LEU A 1 37  ? 36.036  8.207   18.031  1   17.58  ? 37   LEU A O     1 1 
ATOM   298  C  CB    . LEU A 1 37  ? 39.173  7.88    17.317  1   16.94  ? 37   LEU A CB    1 1 
ATOM   299  C  CG    . LEU A 1 37  ? 40.39   7.1     17.829  1   18.93  ? 37   LEU A CG    1 1 
ATOM   300  C  CD1   . LEU A 1 37  ? 41.714  7.824   17.457  1   19.25  ? 37   LEU A CD1   1 1 
ATOM   301  C  CD2   . LEU A 1 37  ? 40.276  6.845   19.316  1   19.53  ? 37   LEU A CD2   1 1 
ATOM   302  N  N     . SER A 1 38  ? 36.318  8.385   15.82   1   16.72  ? 38   SER A N     1 1 
ATOM   303  C  CA    . SER A 1 38  ? 35.192  9.291   15.552  1   16.43  ? 38   SER A CA    1 1 
ATOM   304  C  C     . SER A 1 38  ? 33.908  8.594   15.188  1   16.34  ? 38   SER A C     1 1 
ATOM   305  O  O     . SER A 1 38  ? 32.877  9.241   15.177  1   15.76  ? 38   SER A O     1 1 
ATOM   306  C  CB    . SER A 1 38  ? 35.52   10.163  14.342  1   18.07  ? 38   SER A CB    1 1 
ATOM   307  O  OG    . SER A 1 38  ? 36.61   11.046  14.576  1   20.14  ? 38   SER A OG    1 1 
ATOM   308  N  N     . CYS A 1 39  ? 33.978  7.327   14.751  1   16.23  ? 39   CYS A N     1 1 
ATOM   309  C  CA    . CYS A 1 39  ? 32.83   6.639   14.196  1   16.48  ? 39   CYS A CA    1 1 
ATOM   310  C  C     . CYS A 1 39  ? 32.327  5.472   14.997  1   15.68  ? 39   CYS A C     1 1 
ATOM   311  O  O     . CYS A 1 39  ? 32.802  4.368   14.807  1   15.05  ? 39   CYS A O     1 1 
ATOM   312  C  CB    . CYS A 1 39  ? 33.151  6.203   12.77   1   17.61  ? 39   CYS A CB    1 1 
ATOM   313  S  SG    . CYS A 1 39  ? 33.694  7.561   11.698  1   20.66  ? 39   CYS A SG    1 1 
ATOM   314  N  N     . PRO A 1 40  ? 31.307  5.677   15.834  1   15.52  ? 40   PRO A N     1 1 
ATOM   315  C  CA    . PRO A 1 40  ? 30.706  4.532   16.528  1   15.1   ? 40   PRO A CA    1 1 
ATOM   316  C  C     . PRO A 1 40  ? 29.913  3.658   15.548  1   15.11  ? 40   PRO A C     1 1 
ATOM   317  O  O     . PRO A 1 40  ? 29.552  4.096   14.443  1   14.77  ? 40   PRO A O     1 1 
ATOM   318  C  CB    . PRO A 1 40  ? 29.754  5.172   17.553  1   15.6   ? 40   PRO A CB    1 1 
ATOM   319  C  CG    . PRO A 1 40  ? 29.886  6.607   17.388  1   16.68  ? 40   PRO A CG    1 1 
ATOM   320  C  CD    . PRO A 1 40  ? 30.593  6.929   16.124  1   15.22  ? 40   PRO A CD    1 1 
ATOM   321  N  N     . PHE A 1 41  ? 29.632  2.432   15.962  1   14.89  ? 41   PHE A N     1 1 
ATOM   322  C  CA    . PHE A 1 41  ? 28.824  1.545   15.164  1   15.57  ? 41   PHE A CA    1 1 
ATOM   323  C  C     . PHE A 1 41  ? 27.792  0.844   16.034  1   15.41  ? 41   PHE A C     1 1 
ATOM   324  O  O     . PHE A 1 41  ? 27.97   0.726   17.254  1   15.65  ? 41   PHE A O     1 1 
ATOM   325  C  CB    . PHE A 1 41  ? 29.696  0.5     14.393  1   15.69  ? 41   PHE A CB    1 1 
ATOM   326  C  CG    . PHE A 1 41  ? 30.229  -0.668  15.21   1   16.92  ? 41   PHE A CG    1 1 
ATOM   327  C  CD1   . PHE A 1 41  ? 29.438  -1.777  15.473  1   18.07  ? 41   PHE A CD1   1 1 
ATOM   328  C  CD2   . PHE A 1 41  ? 31.53   -0.671  15.678  1   17.61  ? 41   PHE A CD2   1 1 
ATOM   329  C  CE1   . PHE A 1 41  ? 29.918  -2.835  16.246  1   18.55  ? 41   PHE A CE1   1 1 
ATOM   330  C  CE2   . PHE A 1 41  ? 32.017  -1.742  16.426  1   18.73  ? 41   PHE A CE2   1 1 
ATOM   331  C  CZ    . PHE A 1 41  ? 31.208  -2.819  16.704  1   18.51  ? 41   PHE A CZ    1 1 
ATOM   332  N  N     . ILE A 1 42  ? 26.743  0.329   15.373  1   14.47  ? 42   ILE A N     1 1 
ATOM   333  C  CA    . ILE A 1 42  ? 25.774  -0.593  15.942  1   14.51  ? 42   ILE A CA    1 1 
ATOM   334  C  C     . ILE A 1 42  ? 25.63   -1.73   14.946  1   15.4   ? 42   ILE A C     1 1 
ATOM   335  O  O     . ILE A 1 42  ? 25.436  -1.492  13.752  1   15.44  ? 42   ILE A O     1 1 
ATOM   336  C  CB    . ILE A 1 42  ? 24.424  0.004   16.383  1   13.95  ? 42   ILE A CB    1 1 
ATOM   337  C  CG1   . ILE A 1 42  ? 23.466  -1.12   16.889  1   14.5   ? 42   ILE A CG1   1 1 
ATOM   338  C  CG2   . ILE A 1 42  ? 23.819  0.835   15.266  1   13.79  ? 42   ILE A CG2   1 1 
ATOM   339  C  CD1   . ILE A 1 42  ? 22.215  -0.647  17.631  1   15.82  ? 42   ILE A CD1   1 1 
ATOM   340  N  N     . GLU A 1 43  ? 25.788  -2.959  15.436  1   16.01  ? 43   GLU A N     1 1 
ATOM   341  C  CA    . GLU A 1 43  ? 25.707  -4.186  14.662  1   17.48  ? 43   GLU A CA    1 1 
ATOM   342  C  C     . GLU A 1 43  ? 24.492  -4.983  15.15   1   18.88  ? 43   GLU A C     1 1 
ATOM   343  O  O     . GLU A 1 43  ? 24.327  -5.205  16.35   1   18.76  ? 43   GLU A O     1 1 
ATOM   344  C  CB    . GLU A 1 43  ? 26.995  -4.998  14.855  1   20.37  ? 43   GLU A CB    1 1 
ATOM   345  C  CG    . GLU A 1 43  ? 27.128  -6.176  13.908  1   25.57  ? 43   GLU A CG    1 1 
ATOM   346  C  CD    . GLU A 1 43  ? 28.472  -6.873  13.913  1   33.87  ? 43   GLU A CD    1 1 
ATOM   347  O  OE1   . GLU A 1 43  ? 29.475  -6.252  14.336  1   36.36  ? 43   GLU A OE1   1 1 
ATOM   348  O  OE2   . GLU A 1 43  ? 28.529  -8.038  13.454  1   35.98  ? 43   GLU A OE2   1 1 
ATOM   349  N  N     . ILE A 1 44  ? 23.616  -5.37   14.227  1   19.66  ? 44   ILE A N     1 1 
ATOM   350  C  CA    . ILE A 1 44  ? 22.407  -6.119  14.581  1   20.63  ? 44   ILE A CA    1 1 
ATOM   351  C  C     . ILE A 1 44  ? 22.229  -7.387  13.75   1   21.66  ? 44   ILE A C     1 1 
ATOM   352  O  O     . ILE A 1 44  ? 22.523  -7.42   12.54   1   21.34  ? 44   ILE A O     1 1 
ATOM   353  C  CB    . ILE A 1 44  ? 21.115  -5.259  14.522  1   20.85  ? 44   ILE A CB    1 1 
ATOM   354  C  CG1   . ILE A 1 44  ? 20.794  -4.838  13.099  1   21.88  ? 44   ILE A CG1   1 1 
ATOM   355  C  CG2   . ILE A 1 44  ? 21.149  -4.064  15.48   1   21.47  ? 44   ILE A CG2   1 1 
ATOM   356  C  CD1   . ILE A 1 44  ? 19.417  -4.279  12.958  1   24.2   ? 44   ILE A CD1   1 1 
ATOM   357  N  N     . ILE A 1 45  ? 21.761  -8.445  14.442  1   21.93  ? 45   ILE A N     1 1 
ATOM   358  C  CA    . ILE A 1 45  ? 21.384  -9.709  13.844  1   22.75  ? 45   ILE A CA    1 1 
ATOM   359  C  C     . ILE A 1 45  ? 19.899  -9.766  14.098  1   21.64  ? 45   ILE A C     1 1 
ATOM   360  O  O     . ILE A 1 45  ? 19.459  -9.631  15.244  1   21.41  ? 45   ILE A O     1 1 
ATOM   361  C  CB    . ILE A 1 45  ? 22.058  -10.97  14.444  1   24.49  ? 45   ILE A CB    1 1 
ATOM   362  C  CG1   . ILE A 1 45  ? 23.603  -10.899 14.456  1   26.97  ? 45   ILE A CG1   1 1 
ATOM   363  C  CG2   . ILE A 1 45  ? 21.581  -12.198 13.7    1   25.05  ? 45   ILE A CG2   1 1 
ATOM   364  C  CD1   . ILE A 1 45  ? 24.229  -10.647 13.136  1   29.04  ? 45   ILE A CD1   1 1 
ATOM   365  N  N     . PHE A 1 46  ? 19.121  -9.894  13.036  1   20.52  ? 46   PHE A N     1 1 
ATOM   366  C  CA    . PHE A 1 46  ? 17.673  -9.982  13.157  1   19.74  ? 46   PHE A CA    1 1 
ATOM   367  C  C     . PHE A 1 46  ? 17.108  -10.947 12.109  1   18.92  ? 46   PHE A C     1 1 
ATOM   368  O  O     . PHE A 1 46  ? 17.817  -11.328 11.184  1   18.39  ? 46   PHE A O     1 1 
ATOM   369  C  CB    . PHE A 1 46  ? 17.026  -8.583  13.085  1   19.3   ? 46   PHE A CB    1 1 
ATOM   370  C  CG    . PHE A 1 46  ? 17.019  -7.926  11.726  1   20.2   ? 46   PHE A CG    1 1 
ATOM   371  C  CD1   . PHE A 1 46  ? 18.105  -7.182  11.292  1   22.06  ? 46   PHE A CD1   1 1 
ATOM   372  C  CD2   . PHE A 1 46  ? 15.913  -8.017  10.899  1   20.91  ? 46   PHE A CD2   1 1 
ATOM   373  C  CE1   . PHE A 1 46  ? 18.073  -6.527  10.062  1   22.77  ? 46   PHE A CE1   1 1 
ATOM   374  C  CE2   . PHE A 1 46  ? 15.908  -7.409  9.65    1   21.98  ? 46   PHE A CE2   1 1 
ATOM   375  C  CZ    . PHE A 1 46  ? 16.973  -6.644  9.251   1   22.04  ? 46   PHE A CZ    1 1 
ATOM   376  N  N     . LYS A 1 47  ? 15.84   -11.334 12.245  1   18.96  ? 47   LYS A N     1 1 
ATOM   377  C  CA    . LYS A 1 47  ? 15.219  -12.222 11.275  1   19.56  ? 47   LYS A CA    1 1 
ATOM   378  C  C     . LYS A 1 47  ? 13.832  -11.783 10.897  1   19.84  ? 47   LYS A C     1 1 
ATOM   379  O  O     . LYS A 1 47  ? 13.159  -11.095 11.66   1   20.77  ? 47   LYS A O     1 1 
ATOM   380  C  CB    . LYS A 1 47  ? 15.214  -13.681 11.763  1   21.41  ? 47   LYS A CB    1 1 
ATOM   381  C  CG    . LYS A 1 47  ? 14.445  -13.872 13.056  1   25.77  ? 47   LYS A CG    1 1 
ATOM   382  C  CD    . LYS A 1 47  ? 14.598  -15.303 13.59   1   29.65  ? 47   LYS A CD    1 1 
ATOM   383  C  CE    . LYS A 1 47  ? 13.995  -15.413 14.963  1   33.67  ? 47   LYS A CE    1 1 
ATOM   384  N  NZ    . LYS A 1 47  ? 14.792  -16.329 15.819  1   37.89  ? 47   LYS A NZ    1 1 
ATOM   385  N  N     . GLU A 1 48  ? 13.413  -12.162 9.7     1   18.99  ? 48   GLU A N     1 1 
ATOM   386  C  CA    . GLU A 1 48  ? 12.081  -11.948 9.186   1   18.94  ? 48   GLU A CA    1 1 
ATOM   387  C  C     . GLU A 1 48  ? 11.655  -13.365 8.945   1   19.17  ? 48   GLU A C     1 1 
ATOM   388  O  O     . GLU A 1 48  ? 12.003  -13.965 7.917   1   18.9   ? 48   GLU A O     1 1 
ATOM   389  C  CB    . GLU A 1 48  ? 12.126  -11.181 7.868   1   21.14  ? 48   GLU A CB    1 1 
ATOM   390  C  CG    . GLU A 1 48  ? 12.606  -9.754  8.024   1   26.09  ? 48   GLU A CG    1 1 
ATOM   391  C  CD    . GLU A 1 48  ? 12.669  -8.971  6.728   1   35.75  ? 48   GLU A CD    1 1 
ATOM   392  O  OE1   . GLU A 1 48  ? 12.532  -9.585  5.644   1   36.55  ? 48   GLU A OE1   1 1 
ATOM   393  O  OE2   . GLU A 1 48  ? 12.869  -7.736  6.796   1   42.31  ? 48   GLU A OE2   1 1 
ATOM   394  N  N     . GLY A 1 49  ? 11.039  -13.947 9.965   1   19.1   ? 49   GLY A N     1 1 
ATOM   395  C  CA    . GLY A 1 49  ? 10.633  -15.344 9.917   1   19.01  ? 49   GLY A CA    1 1 
ATOM   396  C  C     . GLY A 1 49  ? 11.838  -16.241 10.041  1   18.99  ? 49   GLY A C     1 1 
ATOM   397  O  O     . GLY A 1 49  ? 12.515  -16.215 11.067  1   19.63  ? 49   GLY A O     1 1 
ATOM   398  N  N     . HIS A 1 50  ? 12.107  -17.051 8.991   1   18.19  ? 50   HIS A N     1 1 
ATOM   399  C  CA    . HIS A 1 50  ? 13.276  -17.921 8.89    1   18.15  ? 50   HIS A CA    1 1 
ATOM   400  C  C     . HIS A 1 50  ? 14.515  -17.162 8.276   1   18.42  ? 50   HIS A C     1 1 
ATOM   401  O  O     . HIS A 1 50  ? 15.627  -17.679 8.355   1   19.12  ? 50   HIS A O     1 1 
ATOM   402  C  CB    . HIS A 1 50  ? 12.974  -19.138 7.992   1   17.81  ? 50   HIS A CB    1 1 
ATOM   403  C  CG    . HIS A 1 50  ? 11.952  -20.082 8.539   1   18.86  ? 50   HIS A CG    1 1 
ATOM   404  N  ND1   . HIS A 1 50  ? 12.317  -21.312 9.092   1   19.86  ? 50   HIS A ND1   1 1 
ATOM   405  C  CD2   . HIS A 1 50  ? 10.602  -19.975 8.565   1   18.87  ? 50   HIS A CD2   1 1 
ATOM   406  C  CE1   . HIS A 1 50  ? 11.184  -21.889 9.447   1   20.27  ? 50   HIS A CE1   1 1 
ATOM   407  N  NE2   . HIS A 1 50  ? 10.127  -21.112 9.169   1   20.37  ? 50   HIS A NE2   1 1 
ATOM   408  N  N     . ASP A 1 51  ? 14.298  -16.032 7.577   1   17.86  ? 51   ASP A N     1 1 
ATOM   409  C  CA    . ASP A 1 51  ? 15.344  -15.242 6.897   1   18.79  ? 51   ASP A CA    1 1 
ATOM   410  C  C     . ASP A 1 51  ? 16.164  -14.315 7.824   1   18.9   ? 51   ASP A C     1 1 
ATOM   411  O  O     . ASP A 1 51  ? 15.667  -13.277 8.264   1   18.39  ? 51   ASP A O     1 1 
ATOM   412  C  CB    . ASP A 1 51  ? 14.726  -14.431 5.727   1   20.98  ? 51   ASP A CB    1 1 
ATOM   413  C  CG    . ASP A 1 51  ? 15.716  -13.95  4.662   1   28.95  ? 51   ASP A CG    1 1 
ATOM   414  O  OD1   . ASP A 1 51  ? 16.918  -14.245 4.789   1   30.86  ? 51   ASP A OD1   1 1 
ATOM   415  O  OD2   . ASP A 1 51  ? 15.28   -13.277 3.7     1   32.02  ? 51   ASP A OD2   1 1 
ATOM   416  N  N     . TYR A 1 52  ? 17.452  -14.64  8.036   1   18.63  ? 52   TYR A N     1 1 
ATOM   417  C  CA    . TYR A 1 52  ? 18.31   -13.824 8.89    1   18.99  ? 52   TYR A CA    1 1 
ATOM   418  C  C     . TYR A 1 52  ? 19.003  -12.697 8.127   1   18.51  ? 52   TYR A C     1 1 
ATOM   419  O  O     . TYR A 1 52  ? 19.284  -12.823 6.934   1   18.44  ? 52   TYR A O     1 1 
ATOM   420  C  CB    . TYR A 1 52  ? 19.372  -14.679 9.583   1   19.31  ? 52   TYR A CB    1 1 
ATOM   421  C  CG    . TYR A 1 52  ? 18.9    -15.448 10.788  1   21.37  ? 52   TYR A CG    1 1 
ATOM   422  C  CD1   . TYR A 1 52  ? 18.906  -14.872 12.05   1   23.23  ? 52   TYR A CD1   1 1 
ATOM   423  C  CD2   . TYR A 1 52  ? 18.472  -16.761 10.674  1   23.16  ? 52   TYR A CD2   1 1 
ATOM   424  C  CE1   . TYR A 1 52  ? 18.531  -15.6   13.175  1   24.85  ? 52   TYR A CE1   1 1 
ATOM   425  C  CE2   . TYR A 1 52  ? 18.065  -17.488 11.785  1   24.74  ? 52   TYR A CE2   1 1 
ATOM   426  C  CZ    . TYR A 1 52  ? 18.117  -16.912 13.039  1   26.25  ? 52   TYR A CZ    1 1 
ATOM   427  O  OH    . TYR A 1 52  ? 17.724  -17.649 14.132  1   28.63  ? 52   TYR A OH    1 1 
ATOM   428  N  N     . PHE A 1 53  ? 19.281  -11.607 8.83    1   17.95  ? 53   PHE A N     1 1 
ATOM   429  C  CA    . PHE A 1 53  ? 19.974  -10.44  8.298   1   19.06  ? 53   PHE A CA    1 1 
ATOM   430  C  C     . PHE A 1 53  ? 21.021  -9.983  9.286   1   18.86  ? 53   PHE A C     1 1 
ATOM   431  O  O     . PHE A 1 53  ? 20.826  -10.062 10.5    1   20     ? 53   PHE A O     1 1 
ATOM   432  C  CB    . PHE A 1 53  ? 19.014  -9.279  7.983   1   19.85  ? 53   PHE A CB    1 1 
ATOM   433  C  CG    . PHE A 1 53  ? 18.021  -9.64   6.91    1   22.02  ? 53   PHE A CG    1 1 
ATOM   434  C  CD1   . PHE A 1 53  ? 18.377  -9.598  5.574   1   23.22  ? 53   PHE A CD1   1 1 
ATOM   435  C  CD2   . PHE A 1 53  ? 16.765  -10.126 7.239   1   23.44  ? 53   PHE A CD2   1 1 
ATOM   436  C  CE1   . PHE A 1 53  ? 17.499  -10.033 4.591   1   24.16  ? 53   PHE A CE1   1 1 
ATOM   437  C  CE2   . PHE A 1 53  ? 15.893  -10.558 6.253   1   24.03  ? 53   PHE A CE2   1 1 
ATOM   438  C  CZ    . PHE A 1 53  ? 16.255  -10.477 4.937   1   23.82  ? 53   PHE A CZ    1 1 
ATOM   439  N  N     . HIS A 1 54  ? 22.143  -9.515  8.765   1   16.92  ? 54   HIS A N     1 1 
ATOM   440  C  CA    . HIS A 1 54  ? 23.238  -9.05   9.582   1   16.01  ? 54   HIS A CA    1 1 
ATOM   441  C  C     . HIS A 1 54  ? 23.595  -7.691  9.032   1   15     ? 54   HIS A C     1 1 
ATOM   442  O  O     . HIS A 1 54  ? 24.068  -7.601  7.901   1   14.92  ? 54   HIS A O     1 1 
ATOM   443  C  CB    . HIS A 1 54  ? 24.428  -10.025 9.45    1   17.01  ? 54   HIS A CB    1 1 
ATOM   444  C  CG    . HIS A 1 54  ? 25.591  -9.724  10.337  1   18.99  ? 54   HIS A CG    1 1 
ATOM   445  N  ND1   . HIS A 1 54  ? 26.778  -10.414 10.207  1   20.72  ? 54   HIS A ND1   1 1 
ATOM   446  C  CD2   . HIS A 1 54  ? 25.725  -8.805  11.327  1   20.24  ? 54   HIS A CD2   1 1 
ATOM   447  C  CE1   . HIS A 1 54  ? 27.591  -9.897  11.111  1   21.38  ? 54   HIS A CE1   1 1 
ATOM   448  N  NE2   . HIS A 1 54  ? 27.004  -8.935  11.812  1   20.93  ? 54   HIS A NE2   1 1 
ATOM   449  N  N     . TRP A 1 55  ? 23.278  -6.626  9.797   1   13.59  ? 55   TRP A N     1 1 
ATOM   450  C  CA    . TRP A 1 55  ? 23.544  -5.273  9.383   1   14.39  ? 55   TRP A CA    1 1 
ATOM   451  C  C     . TRP A 1 55  ? 24.476  -4.567  10.332  1   14.73  ? 55   TRP A C     1 1 
ATOM   452  O  O     . TRP A 1 55  ? 24.397  -4.762  11.546  1   15.45  ? 55   TRP A O     1 1 
ATOM   453  C  CB    . TRP A 1 55  ? 22.233  -4.437  9.347   1   13.49  ? 55   TRP A CB    1 1 
ATOM   454  C  CG    . TRP A 1 55  ? 21.303  -4.723  8.209   1   13.82  ? 55   TRP A CG    1 1 
ATOM   455  C  CD1   . TRP A 1 55  ? 21.52   -5.545  7.137   1   14.42  ? 55   TRP A CD1   1 1 
ATOM   456  C  CD2   . TRP A 1 55  ? 19.971  -4.21   8.058   1   13.69  ? 55   TRP A CD2   1 1 
ATOM   457  N  NE1   . TRP A 1 55  ? 20.415  -5.548  6.315   1   14.54  ? 55   TRP A NE1   1 1 
ATOM   458  C  CE2   . TRP A 1 55  ? 19.435  -4.771  6.879   1   14.24  ? 55   TRP A CE2   1 1 
ATOM   459  C  CE3   . TRP A 1 55  ? 19.161  -3.376  8.837   1   13.52  ? 55   TRP A CE3   1 1 
ATOM   460  C  CZ2   . TRP A 1 55  ? 18.168  -4.44   6.41    1   14.5   ? 55   TRP A CZ2   1 1 
ATOM   461  C  CZ3   . TRP A 1 55  ? 17.904  -3.053  8.373   1   14.52  ? 55   TRP A CZ3   1 1 
ATOM   462  C  CH2   . TRP A 1 55  ? 17.402  -3.619  7.196   1   14.86  ? 55   TRP A CH2   1 1 
ATOM   463  N  N     . ARG A 1 56  ? 25.287  -3.671  9.786   1   13.92  ? 56   ARG A N     1 1 
ATOM   464  C  CA    . ARG A 1 56  ? 26.14   -2.826  10.61   1   13.35  ? 56   ARG A CA    1 1 
ATOM   465  C  C     . ARG A 1 56  ? 25.959  -1.376  10.119  1   14.15  ? 56   ARG A C     1 1 
ATOM   466  O  O     . ARG A 1 56  ? 25.902  -1.121  8.911   1   14.33  ? 56   ARG A O     1 1 
ATOM   467  C  CB    . ARG A 1 56  ? 27.619  -3.28   10.657  1   13.22  ? 56   ARG A CB    1 1 
ATOM   468  C  CG    . ARG A 1 56  ? 28.384  -2.578  11.808  1   13.68  ? 56   ARG A CG    1 1 
ATOM   469  C  CD    . ARG A 1 56  ? 29.859  -2.847  11.8    1   13.68  ? 56   ARG A CD    1 1 
ATOM   470  N  NE    . ARG A 1 56  ? 30.542  -2.079  10.766  1   15.21  ? 56   ARG A NE    1 1 
ATOM   471  C  CZ    . ARG A 1 56  ? 31.597  -2.51   10.076  1   19.13  ? 56   ARG A CZ    1 1 
ATOM   472  N  NH1   . ARG A 1 56  ? 32.083  -3.739  10.28   1   16.19  ? 56   ARG A NH1   1 1 
ATOM   473  N  NH2   . ARG A 1 56  ? 32.178  -1.719  9.177   1   19.31  ? 56   ARG A NH2   1 1 
ATOM   474  N  N     . PHE A 1 57  ? 25.762  -0.463  11.072  1   13.74  ? 57   PHE A N     1 1 
ATOM   475  C  CA    . PHE A 1 57  ? 25.554  0.947   10.83   1   14.3   ? 57   PHE A CA    1 1 
ATOM   476  C  C     . PHE A 1 57  ? 26.76   1.68    11.417  1   15.35  ? 57   PHE A C     1 1 
ATOM   477  O  O     . PHE A 1 57  ? 27.005  1.608   12.626  1   15.84  ? 57   PHE A O     1 1 
ATOM   478  C  CB    . PHE A 1 57  ? 24.246  1.441   11.492  1   13.38  ? 57   PHE A CB    1 1 
ATOM   479  C  CG    . PHE A 1 57  ? 22.99   0.843   10.877  1   13.31  ? 57   PHE A CG    1 1 
ATOM   480  C  CD1   . PHE A 1 57  ? 22.388  1.435   9.776   1   13.3   ? 57   PHE A CD1   1 1 
ATOM   481  C  CD2   . PHE A 1 57  ? 22.434  -0.322  11.386  1   13.84  ? 57   PHE A CD2   1 1 
ATOM   482  C  CE1   . PHE A 1 57  ? 21.271  0.863   9.179   1   13.57  ? 57   PHE A CE1   1 1 
ATOM   483  C  CE2   . PHE A 1 57  ? 21.316  -0.905  10.779  1   14.5   ? 57   PHE A CE2   1 1 
ATOM   484  C  CZ    . PHE A 1 57  ? 20.734  -0.298  9.688   1   13.86  ? 57   PHE A CZ    1 1 
ATOM   485  N  N     . ASP A 1 58  ? 27.537  2.342   10.547  1   14.98  ? 58   ASP A N     1 1 
ATOM   486  C  CA    . ASP A 1 58  ? 28.718  3.089   10.947  1   14.46  ? 58   ASP A CA    1 1 
ATOM   487  C  C     . ASP A 1 58  ? 28.302  4.559   10.922  1   15.33  ? 58   ASP A C     1 1 
ATOM   488  O  O     . ASP A 1 58  ? 27.747  5.04    9.935   1   15.64  ? 58   ASP A O     1 1 
ATOM   489  C  CB    . ASP A 1 58  ? 29.898  2.787   9.995   1   13.72  ? 58   ASP A CB    1 1 
ATOM   490  C  CG    . ASP A 1 58  ? 30.362  1.335   10.031  1   17.53  ? 58   ASP A CG    1 1 
ATOM   491  O  OD1   . ASP A 1 58  ? 29.992  0.613   10.986  1   17.61  ? 58   ASP A OD1   1 1 
ATOM   492  O  OD2   . ASP A 1 58  ? 31.101  0.92    9.11    1   18.79  ? 58   ASP A OD2   1 1 
ATOM   493  N  N     . MET A 1 59  ? 28.479  5.238   12.044  1   15.28  ? 59   MET A N     1 1 
ATOM   494  C  CA    . MET A 1 59  ? 28.016  6.605   12.208  1   16.04  ? 59   MET A CA    1 1 
ATOM   495  C  C     . MET A 1 59  ? 29.11   7.625   12.022  1   16.88  ? 59   MET A C     1 1 
ATOM   496  O  O     . MET A 1 59  ? 30.183  7.451   12.563  1   18.32  ? 59   MET A O     1 1 
ATOM   497  C  CB    . MET A 1 59  ? 27.34   6.735   13.566  1   16.13  ? 59   MET A CB    1 1 
ATOM   498  C  CG    . MET A 1 59  ? 26.066  5.949   13.617  1   19.74  ? 59   MET A CG    1 1 
ATOM   499  S  SD    . MET A 1 59  ? 25.443  5.842   15.278  1   27.01  ? 59   MET A SD    1 1 
ATOM   500  C  CE    . MET A 1 59  ? 25.963  4.19    15.694  1   29.28  ? 59   MET A CE    1 1 
ATOM   501  N  N     . PHE A 1 60  ? 28.85   8.682   11.25   1   16.74  ? 60   PHE A N     1 1 
ATOM   502  C  CA    . PHE A 1 60  ? 29.817  9.758   10.97   1   16.32  ? 60   PHE A CA    1 1 
ATOM   503  C  C     . PHE A 1 60  ? 29.269  11.096  11.501  1   16.8   ? 60   PHE A C     1 1 
ATOM   504  O  O     . PHE A 1 60  ? 28.558  11.822  10.807  1   15.7   ? 60   PHE A O     1 1 
ATOM   505  C  CB    . PHE A 1 60  ? 30.11   9.854   9.465   1   15.39  ? 60   PHE A CB    1 1 
ATOM   506  C  CG    . PHE A 1 60  ? 31.007  8.773   8.926   1   16.06  ? 60   PHE A CG    1 1 
ATOM   507  C  CD1   . PHE A 1 60  ? 30.589  7.447   8.89    1   16.5   ? 60   PHE A CD1   1 1 
ATOM   508  C  CD2   . PHE A 1 60  ? 32.291  9.065   8.493   1   16.72  ? 60   PHE A CD2   1 1 
ATOM   509  C  CE1   . PHE A 1 60  ? 31.432  6.447   8.429   1   16.5   ? 60   PHE A CE1   1 1 
ATOM   510  C  CE2   . PHE A 1 60  ? 33.112  8.062   7.993   1   16.89  ? 60   PHE A CE2   1 1 
ATOM   511  C  CZ    . PHE A 1 60  ? 32.675  6.759   7.961   1   16.31  ? 60   PHE A CZ    1 1 
ATOM   512  N  N     . PRO A 1 61  ? 29.631  11.452  12.739  1   18.18  ? 61   PRO A N     1 1 
ATOM   513  C  CA    . PRO A 1 61  ? 29.091  12.68   13.342  1   18.43  ? 61   PRO A CA    1 1 
ATOM   514  C  C     . PRO A 1 61  ? 29.842  13.962  12.982  1   18.58  ? 61   PRO A C     1 1 
ATOM   515  O  O     . PRO A 1 61  ? 31.045  14.035  13.139  1   18.79  ? 61   PRO A O     1 1 
ATOM   516  C  CB    . PRO A 1 61  ? 29.194  12.404  14.854  1   19.48  ? 61   PRO A CB    1 1 
ATOM   517  C  CG    . PRO A 1 61  ? 29.566  10.881  14.966  1   20.28  ? 61   PRO A CG    1 1 
ATOM   518  C  CD    . PRO A 1 61  ? 30.397  10.679  13.727  1   18.16  ? 61   PRO A CD    1 1 
ATOM   519  N  N     . GLY A 1 62  ? 29.091  14.987  12.577  1   18.18  ? 62   GLY A N     1 1 
ATOM   520  C  CA    . GLY A 1 62  ? 29.631  16.286  12.234  1   17.67  ? 62   GLY A CA    1 1 
ATOM   521  C  C     . GLY A 1 62  ? 29.954  16.393  10.768  1   18.46  ? 62   GLY A C     1 1 
ATOM   522  O  O     . GLY A 1 62  ? 30.929  15.792  10.313  1   20.64  ? 62   GLY A O     1 1 
ATOM   523  N  N     . PHE A 1 63  ? 29.175  17.178  10.023  1   17.76  ? 63   PHE A N     1 1 
ATOM   524  C  CA    . PHE A 1 63  ? 29.428  17.354  8.603   1   18.28  ? 63   PHE A CA    1 1 
ATOM   525  C  C     . PHE A 1 63  ? 30.582  18.32   8.344   1   20.24  ? 63   PHE A C     1 1 
ATOM   526  O  O     . PHE A 1 63  ? 30.865  19.205  9.164   1   19.82  ? 63   PHE A O     1 1 
ATOM   527  C  CB    . PHE A 1 63  ? 28.171  17.882  7.902   1   17.54  ? 63   PHE A CB    1 1 
ATOM   528  C  CG    . PHE A 1 63  ? 27.039  16.899  7.718   1   18.25  ? 63   PHE A CG    1 1 
ATOM   529  C  CD1   . PHE A 1 63  ? 27.171  15.818  6.863   1   18.58  ? 63   PHE A CD1   1 1 
ATOM   530  C  CD2   . PHE A 1 63  ? 25.838  17.067  8.386   1   18.8   ? 63   PHE A CD2   1 1 
ATOM   531  C  CE1   . PHE A 1 63  ? 26.112  14.927  6.675   1   19.35  ? 63   PHE A CE1   1 1 
ATOM   532  C  CE2   . PHE A 1 63  ? 24.785  16.177  8.196   1   18.94  ? 63   PHE A CE2   1 1 
ATOM   533  C  CZ    . PHE A 1 63  ? 24.921  15.121  7.335   1   18.94  ? 63   PHE A CZ    1 1 
ATOM   534  N  N     . ASN A 1 64  ? 31.21   18.194  7.17    1   21.59  ? 64   ASN A N     1 1 
ATOM   535  C  CA    . ASN A 1 64  ? 32.227  19.161  6.742   1   23.17  ? 64   ASN A CA    1 1 
ATOM   536  C  C     . ASN A 1 64  ? 31.533  20.456  6.334   1   27.27  ? 64   ASN A C     1 1 
ATOM   537  O  O     . ASN A 1 64  ? 30.436  20.425  5.752   1   26.88  ? 64   ASN A O     1 1 
ATOM   538  C  CB    . ASN A 1 64  ? 32.897  18.676  5.458   1   20.88  ? 64   ASN A CB    1 1 
ATOM   539  C  CG    . ASN A 1 64  ? 33.997  17.701  5.644   1   19.49  ? 64   ASN A CG    1 1 
ATOM   540  O  OD1   . ASN A 1 64  ? 34.191  17.168  6.722   1   19.17  ? 64   ASN A OD1   1 1 
ATOM   541  N  ND2   . ASN A 1 64  ? 34.753  17.458  4.596   1   19.31  ? 64   ASN A ND2   1 1 
ATOM   542  N  N     . LYS A 1 65  ? 32.212  21.575  6.541   1   30.72  ? 65   LYS A N     1 1 
ATOM   543  C  CA    . LYS A 1 65  ? 31.761  22.865  6.015   1   34.95  ? 65   LYS A CA    1 1 
ATOM   544  C  C     . LYS A 1 65  ? 32.464  23.147  4.621   1   38.79  ? 65   LYS A C     1 1 
ATOM   545  O  O     . LYS A 1 65  ? 32.222  24.197  4.035   1   39.36  ? 65   LYS A O     1 1 
ATOM   546  C  CB    . LYS A 1 65  ? 32.03   24.009  7.02    1   37.16  ? 65   LYS A CB    1 1 
ATOM   547  C  CG    . LYS A 1 65  ? 31.509  23.734  8.437   1   41.19  ? 65   LYS A CG    1 1 
ATOM   548  C  CD    . LYS A 1 65  ? 29.998  23.589  8.479   1   45.95  ? 65   LYS A CD    1 1 
ATOM   549  C  CE    . LYS A 1 65  ? 29.478  22.968  9.759   1   49.29  ? 65   LYS A CE    1 1 
ATOM   550  N  NZ    . LYS A 1 65  ? 28.949  21.581  9.539   1   50.14  ? 65   LYS A NZ    1 1 
ATOM   551  N  N     . ASN A 1 66  ? 33.303  22.195  4.096   1   40.86  ? 66   ASN A N     1 1 
ATOM   552  C  CA    . ASN A 1 66  ? 34.004  22.255  2.797   1   42.85  ? 66   ASN A CA    1 1 
ATOM   553  C  C     . ASN A 1 66  ? 34.487  20.821  2.344   1   42.96  ? 66   ASN A C     1 1 
ATOM   554  O  O     . ASN A 1 66  ? 33.956  19.837  2.848   1   43.48  ? 66   ASN A O     1 1 
ATOM   555  C  CB    . ASN A 1 66  ? 35.118  23.332  2.774   1   45.35  ? 66   ASN A CB    1 1 
ATOM   556  C  CG    . ASN A 1 66  ? 36.209  23.139  3.793   1   50.6   ? 66   ASN A CG    1 1 
ATOM   557  O  OD1   . ASN A 1 66  ? 37.072  22.246  3.673   1   53.09  ? 66   ASN A OD1   1 1 
ATOM   558  N  ND2   . ASN A 1 66  ? 36.211  24      4.805   1   51.12  ? 66   ASN A ND2   1 1 
ATOM   559  N  N     . THR A 1 67  ? 35.426  20.686  1.379   1   42.34  ? 67   THR A N     1 1 
ATOM   560  C  CA    . THR A 1 67  ? 35.82   19.36   0.876   1   41.95  ? 67   THR A CA    1 1 
ATOM   561  C  C     . THR A 1 67  ? 36.716  18.525  1.82    1   40.73  ? 67   THR A C     1 1 
ATOM   562  O  O     . THR A 1 67  ? 36.671  17.302  1.732   1   40.44  ? 67   THR A O     1 1 
ATOM   563  C  CB    . THR A 1 67  ? 36.462  19.484  -0.502  1   43.77  ? 67   THR A CB    1 1 
ATOM   564  N  N     . ASN A 1 68  ? 37.519  19.16   2.709   1   39.4   ? 68   ASN A N     1 1 
ATOM   565  C  CA    . ASN A 1 68  ? 38.384  18.393  3.614   1   38.07  ? 68   ASN A CA    1 1 
ATOM   566  C  C     . ASN A 1 68  ? 38.582  19.04   4.989   1   36.33  ? 68   ASN A C     1 1 
ATOM   567  O  O     . ASN A 1 68  ? 39.599  18.812  5.626   1   37.06  ? 68   ASN A O     1 1 
ATOM   568  C  CB    . ASN A 1 68  ? 39.717  18.075  2.967   1   39.27  ? 68   ASN A CB    1 1 
ATOM   569  N  N     . ASP A 1 69  ? 37.587  19.794  5.449   1   34.35  ? 69   ASP A N     1 1 
ATOM   570  C  CA    . ASP A 1 69  ? 37.482  20.475  6.743   1   33.16  ? 69   ASP A CA    1 1 
ATOM   571  C  C     . ASP A 1 69  ? 37.613  19.491  7.958   1   30.68  ? 69   ASP A C     1 1 
ATOM   572  O  O     . ASP A 1 69  ? 38.436  19.682  8.847   1   30.83  ? 69   ASP A O     1 1 
ATOM   573  C  CB    . ASP A 1 69  ? 36.093  21.176  6.761   1   36.43  ? 69   ASP A CB    1 1 
ATOM   574  C  CG    . ASP A 1 69  ? 35.69   21.783  8.077   1   43.75  ? 69   ASP A CG    1 1 
ATOM   575  O  OD1   . ASP A 1 69  ? 36.542  22.462  8.706   1   47.19  ? 69   ASP A OD1   1 1 
ATOM   576  O  OD2   . ASP A 1 69  ? 34.526  21.596  8.479   1   44.77  ? 69   ASP A OD2   1 1 
ATOM   577  N  N     . ARG A 1 70  ? 36.765  18.469  8.009   1   28.17  ? 70   ARG A N     1 1 
ATOM   578  C  CA    . ARG A 1 70  ? 36.768  17.479  9.079   1   26.04  ? 70   ARG A CA    1 1 
ATOM   579  C  C     . ARG A 1 70  ? 37.13   16.13   8.448   1   24.52  ? 70   ARG A C     1 1 
ATOM   580  O  O     . ARG A 1 70  ? 38.234  15.644  8.622   1   24.2   ? 70   ARG A O     1 1 
ATOM   581  C  CB    . ARG A 1 70  ? 35.392  17.483  9.799   1   25.31  ? 70   ARG A CB    1 1 
ATOM   582  C  CG    . ARG A 1 70  ? 35.031  16.222  10.581  1   24.14  ? 70   ARG A CG    1 1 
ATOM   583  C  CD    . ARG A 1 70  ? 34.078  16.607  11.699  1   22.91  ? 70   ARG A CD    1 1 
ATOM   584  N  NE    . ARG A 1 70  ? 33.612  15.479  12.504  1   21.04  ? 70   ARG A NE    1 1 
ATOM   585  C  CZ    . ARG A 1 70  ? 34.295  14.933  13.505  1   19.98  ? 70   ARG A CZ    1 1 
ATOM   586  N  NH1   . ARG A 1 70  ? 35.523  15.353  13.792  1   18.25  ? 70   ARG A NH1   1 1 
ATOM   587  N  NH2   . ARG A 1 70  ? 33.763  13.957  14.217  1   18.58  ? 70   ARG A NH2   1 1 
ATOM   588  N  N     . TRP A 1 71  ? 36.236  15.577  7.641   1   23.19  ? 71   TRP A N     1 1 
ATOM   589  C  CA    . TRP A 1 71  ? 36.436  14.333  6.925   1   21.66  ? 71   TRP A CA    1 1 
ATOM   590  C  C     . TRP A 1 71  ? 37.27   14.603  5.655   1   22.05  ? 71   TRP A C     1 1 
ATOM   591  O  O     . TRP A 1 71  ? 37.211  15.696  5.1     1   21.74  ? 71   TRP A O     1 1 
ATOM   592  C  CB    . TRP A 1 71  ? 35.069  13.707  6.589   1   19.94  ? 71   TRP A CB    1 1 
ATOM   593  C  CG    . TRP A 1 71  ? 34.14   13.588  7.769   1   18.92  ? 71   TRP A CG    1 1 
ATOM   594  C  CD1   . TRP A 1 71  ? 33.045  14.356  8.031   1   19.97  ? 71   TRP A CD1   1 1 
ATOM   595  C  CD2   . TRP A 1 71  ? 34.243  12.649  8.856   1   18.41  ? 71   TRP A CD2   1 1 
ATOM   596  N  NE1   . TRP A 1 71  ? 32.453  13.956  9.211   1   20.17  ? 71   TRP A NE1   1 1 
ATOM   597  C  CE2   . TRP A 1 71  ? 33.159  12.892  9.725   1   18.93  ? 71   TRP A CE2   1 1 
ATOM   598  C  CE3   . TRP A 1 71  ? 35.135  11.607  9.163   1   18.6   ? 71   TRP A CE3   1 1 
ATOM   599  C  CZ2   . TRP A 1 71  ? 32.979  12.175  10.906  1   18.59  ? 71   TRP A CZ2   1 1 
ATOM   600  C  CZ3   . TRP A 1 71  ? 34.935  10.873  10.316  1   18.78  ? 71   TRP A CZ3   1 1 
ATOM   601  C  CH2   . TRP A 1 71  ? 33.877  11.166  11.18   1   18.82  ? 71   TRP A CH2   1 1 
ATOM   602  N  N     . ASN A 1 72  ? 38.047  13.597  5.205   1   22.84  ? 72   ASN A N     1 1 
ATOM   603  C  CA    . ASN A 1 72  ? 38.947  13.649  4.047   1   23.82  ? 72   ASN A CA    1 1 
ATOM   604  C  C     . ASN A 1 72  ? 38.196  13.86   2.74    1   23.85  ? 72   ASN A C     1 1 
ATOM   605  O  O     . ASN A 1 72  ? 38.744  14.445  1.814   1   24.69  ? 72   ASN A O     1 1 
ATOM   606  C  CB    . ASN A 1 72  ? 39.892  12.441  4.008   1   26.58  ? 72   ASN A CB    1 1 
ATOM   607  C  CG    . ASN A 1 72  ? 41.062  12.59   4.988   1   33.03  ? 72   ASN A CG    1 1 
ATOM   608  O  OD1   . ASN A 1 72  ? 41.354  13.697  5.489   1   36.03  ? 72   ASN A OD1   1 1 
ATOM   609  N  ND2   . ASN A 1 72  ? 41.766  11.49   5.298   1   34.16  ? 72   ASN A ND2   1 1 
ATOM   610  N  N     . SER A 1 73  ? 36.918  13.462  2.685   1   22.96  ? 73   SER A N     1 1 
ATOM   611  C  CA    . SER A 1 73  ? 36.026  13.756  1.575   1   22.06  ? 73   SER A CA    1 1 
ATOM   612  C  C     . SER A 1 73  ? 34.634  14.109  2.122   1   20.92  ? 73   SER A C     1 1 
ATOM   613  O  O     . SER A 1 73  ? 34.307  13.768  3.257   1   20.69  ? 73   SER A O     1 1 
ATOM   614  C  CB    . SER A 1 73  ? 36.002  12.644  0.543   1   23.41  ? 73   SER A CB    1 1 
ATOM   615  O  OG    . SER A 1 73  ? 35.739  11.406  1.17    1   27.78  ? 73   SER A OG    1 1 
ATOM   616  N  N     . ASN A 1 74  ? 33.86   14.877  1.35    1   20.16  ? 74   ASN A N     1 1 
ATOM   617  C  CA    . ASN A 1 74  ? 32.573  15.369  1.766   1   19.53  ? 74   ASN A CA    1 1 
ATOM   618  C  C     . ASN A 1 74  ? 31.458  14.52   1.181   1   19.76  ? 74   ASN A C     1 1 
ATOM   619  O  O     . ASN A 1 74  ? 31.227  14.575  -0.031  1   19.63  ? 74   ASN A O     1 1 
ATOM   620  C  CB    . ASN A 1 74  ? 32.413  16.799  1.288   1   20.46  ? 74   ASN A CB    1 1 
ATOM   621  C  CG    . ASN A 1 74  ? 31.282  17.56   1.971   1   21.41  ? 74   ASN A CG    1 1 
ATOM   622  O  OD1   . ASN A 1 74  ? 30.536  17.01   2.79    1   21.7   ? 74   ASN A OD1   1 1 
ATOM   623  N  ND2   . ASN A 1 74  ? 31.158  18.843  1.667   1   21.68  ? 74   ASN A ND2   1 1 
ATOM   624  N  N     . ILE A 1 75  ? 30.708  13.784  2.045   1   19.26  ? 75   ILE A N     1 1 
ATOM   625  C  CA    . ILE A 1 75  ? 29.56   13.007  1.594   1   19.07  ? 75   ILE A CA    1 1 
ATOM   626  C  C     . ILE A 1 75  ? 28.527  13.904  0.862   1   19.05  ? 75   ILE A C     1 1 
ATOM   627  O  O     . ILE A 1 75  ? 27.873  13.448  -0.084  1   19.7   ? 75   ILE A O     1 1 
ATOM   628  C  CB    . ILE A 1 75  ? 28.9    12.185  2.739   1   19.86  ? 75   ILE A CB    1 1 
ATOM   629  C  CG1   . ILE A 1 75  ? 27.989  11.096  2.165   1   20.03  ? 75   ILE A CG1   1 1 
ATOM   630  C  CG2   . ILE A 1 75  ? 28.139  13.061  3.744   1   21.39  ? 75   ILE A CG2   1 1 
ATOM   631  C  CD1   . ILE A 1 75  ? 28.785  10.074  1.205   1   20.9   ? 75   ILE A CD1   1 1 
ATOM   632  N  N     . LEU A 1 76  ? 28.421  15.176  1.273   1   18.33  ? 76   LEU A N     1 1 
ATOM   633  C  CA    . LEU A 1 76  ? 27.486  16.139  0.687   1   18.31  ? 76   LEU A CA    1 1 
ATOM   634  C  C     . LEU A 1 76  ? 27.752  16.393  -0.786  1   18.97  ? 76   LEU A C     1 1 
ATOM   635  O  O     . LEU A 1 76  ? 26.842  16.827  -1.478  1   18.89  ? 76   LEU A O     1 1 
ATOM   636  C  CB    . LEU A 1 76  ? 27.492  17.453  1.48    1   18.89  ? 76   LEU A CB    1 1 
ATOM   637  C  CG    . LEU A 1 76  ? 27.052  17.322  2.947   1   21.05  ? 76   LEU A CG    1 1 
ATOM   638  C  CD1   . LEU A 1 76  ? 27.213  18.638  3.699   1   21.93  ? 76   LEU A CD1   1 1 
ATOM   639  C  CD2   . LEU A 1 76  ? 25.617  16.811  3.058   1   20.93  ? 76   LEU A CD2   1 1 
ATOM   640  N  N     . ASP A 1 77  ? 29      16.146  -1.275  1   19.6   ? 77   ASP A N     1 1 
ATOM   641  C  CA    . ASP A 1 77  ? 29.372  16.277  -2.693  1   20.26  ? 77   ASP A CA    1 1 
ATOM   642  C  C     . ASP A 1 77  ? 28.513  15.347  -3.566  1   19.46  ? 77   ASP A C     1 1 
ATOM   643  O  O     . ASP A 1 77  ? 28.298  15.645  -4.739  1   18.87  ? 77   ASP A O     1 1 
ATOM   644  C  CB    . ASP A 1 77  ? 30.861  15.917  -2.915  1   23.86  ? 77   ASP A CB    1 1 
ATOM   645  C  CG    . ASP A 1 77  ? 31.846  16.982  -2.461  1   33.15  ? 77   ASP A CG    1 1 
ATOM   646  O  OD1   . ASP A 1 77  ? 31.393  18.043  -1.969  1   35.03  ? 77   ASP A OD1   1 1 
ATOM   647  O  OD2   . ASP A 1 77  ? 33.083  16.752  -2.596  1   36.68  ? 77   ASP A OD2   1 1 
ATOM   648  N  N     . LEU A 1 78  ? 28.014  14.231  -3.004  1   19.02  ? 78   LEU A N     1 1 
ATOM   649  C  CA    . LEU A 1 78  ? 27.127  13.35   -3.762  1   19.31  ? 78   LEU A CA    1 1 
ATOM   650  C  C     . LEU A 1 78  ? 25.811  14.059  -4.119  1   19.27  ? 78   LEU A C     1 1 
ATOM   651  O  O     . LEU A 1 78  ? 25.23   13.752  -5.162  1   19.89  ? 78   LEU A O     1 1 
ATOM   652  C  CB    . LEU A 1 78  ? 26.878  12.013  -3.049  1   19.19  ? 78   LEU A CB    1 1 
ATOM   653  C  CG    . LEU A 1 78  ? 28.05   11.04   -2.996  1   20.82  ? 78   LEU A CG    1 1 
ATOM   654  C  CD1   . LEU A 1 78  ? 27.658  9.747   -2.309  1   20.94  ? 78   LEU A CD1   1 1 
ATOM   655  C  CD2   . LEU A 1 78  ? 28.634  10.769  -4.386  1   21.45  ? 78   LEU A CD2   1 1 
ATOM   656  N  N     . LEU A 1 79  ? 25.368  15.033  -3.287  1   18.38  ? 79   LEU A N     1 1 
ATOM   657  C  CA    . LEU A 1 79  ? 24.163  15.799  -3.555  1   18.56  ? 79   LEU A CA    1 1 
ATOM   658  C  C     . LEU A 1 79  ? 24.487  16.895  -4.604  1   19.4   ? 79   LEU A C     1 1 
ATOM   659  O  O     . LEU A 1 79  ? 23.767  17.043  -5.593  1   18.9   ? 79   LEU A O     1 1 
ATOM   660  C  CB    . LEU A 1 79  ? 23.616  16.429  -2.259  1   18.28  ? 79   LEU A CB    1 1 
ATOM   661  C  CG    . LEU A 1 79  ? 23.267  15.462  -1.133  1   19.16  ? 79   LEU A CG    1 1 
ATOM   662  C  CD1   . LEU A 1 79  ? 22.83   16.213  0.123   1   19.42  ? 79   LEU A CD1   1 1 
ATOM   663  C  CD2   . LEU A 1 79  ? 22.188  14.462  -1.565  1   19.57  ? 79   LEU A CD2   1 1 
ATOM   664  N  N     . SER A 1 80  ? 25.595  17.618  -4.428  1   19.87  ? 80   SER A N     1 1 
ATOM   665  C  CA    . SER A 1 80  ? 26.002  18.662  -5.385  1   21.16  ? 80   SER A CA    1 1 
ATOM   666  C  C     . SER A 1 80  ? 26.189  18.076  -6.807  1   21.23  ? 80   SER A C     1 1 
ATOM   667  O  O     . SER A 1 80  ? 25.894  18.767  -7.793  1   21.8   ? 80   SER A O     1 1 
ATOM   668  C  CB    . SER A 1 80  ? 27.315  19.308  -4.95   1   23.42  ? 80   SER A CB    1 1 
ATOM   669  O  OG    . SER A 1 80  ? 27.433  19.428  -3.544  1   27.04  ? 80   SER A OG    1 1 
ATOM   670  N  N     . GLN A 1 81  ? 26.683  16.827  -6.898  1   19.88  ? 81   GLN A N     1 1 
ATOM   671  C  CA    . GLN A 1 81  ? 26.899  16.115  -8.161  1   20.91  ? 81   GLN A CA    1 1 
ATOM   672  C  C     . GLN A 1 81  ? 25.605  15.825  -8.898  1   21.87  ? 81   GLN A C     1 1 
ATOM   673  O  O     . GLN A 1 81  ? 25.644  15.584  -10.103 1   22.43  ? 81   GLN A O     1 1 
ATOM   674  C  CB    . GLN A 1 81  ? 27.606  14.761  -7.934  1   21.97  ? 81   GLN A CB    1 1 
ATOM   675  C  CG    . GLN A 1 81  ? 29.066  14.882  -7.603  1   24.5   ? 81   GLN A CG    1 1 
ATOM   676  C  CD    . GLN A 1 81  ? 29.696  13.545  -7.277  1   26.81  ? 81   GLN A CD    1 1 
ATOM   677  O  OE1   . GLN A 1 81  ? 29.434  12.527  -7.929  1   26.22  ? 81   GLN A OE1   1 1 
ATOM   678  N  NE2   . GLN A 1 81  ? 30.582  13.533  -6.284  1   26.72  ? 81   GLN A NE2   1 1 
ATOM   679  N  N     . LYS A 1 82  ? 24.483  15.734  -8.169  1   21.65  ? 82   LYS A N     1 1 
ATOM   680  C  CA    . LYS A 1 82  ? 23.184  15.472  -8.764  1   21.75  ? 82   LYS A CA    1 1 
ATOM   681  C  C     . LYS A 1 82  ? 22.289  16.729  -8.873  1   21.51  ? 82   LYS A C     1 1 
ATOM   682  O  O     . LYS A 1 82  ? 21.1    16.606  -9.159  1   22.75  ? 82   LYS A O     1 1 
ATOM   683  C  CB    . LYS A 1 82  ? 22.481  14.326  -8.019  1   24.29  ? 82   LYS A CB    1 1 
ATOM   684  C  CG    . LYS A 1 82  ? 23.145  12.962  -8.216  1   27.84  ? 82   LYS A CG    1 1 
ATOM   685  C  CD    . LYS A 1 82  ? 23.126  12.527  -9.678  1   33.13  ? 82   LYS A CD    1 1 
ATOM   686  C  CE    . LYS A 1 82  ? 23.656  11.124  -9.86   1   38.85  ? 82   LYS A CE    1 1 
ATOM   687  N  NZ    . LYS A 1 82  ? 22.698  10.122  -9.325  1   42.77  ? 82   LYS A NZ    1 1 
ATOM   688  N  N     . GLY A 1 83  ? 22.86   17.923  -8.688  1   19.97  ? 83   GLY A N     1 1 
ATOM   689  C  CA    . GLY A 1 83  ? 22.096  19.15   -8.829  1   19.27  ? 83   GLY A CA    1 1 
ATOM   690  C  C     . GLY A 1 83  ? 21.715  19.903  -7.571  1   18.88  ? 83   GLY A C     1 1 
ATOM   691  O  O     . GLY A 1 83  ? 20.98   20.892  -7.668  1   18.24  ? 83   GLY A O     1 1 
ATOM   692  N  N     . SER A 1 84  ? 22.205  19.478  -6.384  1   18.87  ? 84   SER A N     1 1 
ATOM   693  C  CA    . SER A 1 84  ? 21.909  20.256  -5.171  1   19.49  ? 84   SER A CA    1 1 
ATOM   694  C  C     . SER A 1 84  ? 22.882  21.464  -5.115  1   21.01  ? 84   SER A C     1 1 
ATOM   695  O  O     . SER A 1 84  ? 23.897  21.42   -4.416  1   21.32  ? 84   SER A O     1 1 
ATOM   696  C  CB    . SER A 1 84  ? 22.001  19.401  -3.914  1   18.67  ? 84   SER A CB    1 1 
ATOM   697  O  OG    . SER A 1 84  ? 21.549  20.15   -2.797  1   17.98  ? 84   SER A OG    1 1 
ATOM   698  N  N     . PHE A 1 85  ? 22.575  22.536  -5.868  1   21.74  ? 85   PHE A N     1 1 
ATOM   699  C  CA    . PHE A 1 85  ? 23.465  23.697  -5.966  1   22.6   ? 85   PHE A CA    1 1 
ATOM   700  C  C     . PHE A 1 85  ? 23.353  24.697  -4.809  1   23.76  ? 85   PHE A C     1 1 
ATOM   701  O  O     . PHE A 1 85  ? 24.168  25.612  -4.748  1   23.65  ? 85   PHE A O     1 1 
ATOM   702  C  CB    . PHE A 1 85  ? 23.296  24.416  -7.314  1   22.45  ? 85   PHE A CB    1 1 
ATOM   703  C  CG    . PHE A 1 85  ? 21.872  24.833  -7.639  1   22.25  ? 85   PHE A CG    1 1 
ATOM   704  C  CD1   . PHE A 1 85  ? 21.272  25.892  -6.977  1   22.19  ? 85   PHE A CD1   1 1 
ATOM   705  C  CD2   . PHE A 1 85  ? 21.142  24.17   -8.616  1   22.54  ? 85   PHE A CD2   1 1 
ATOM   706  C  CE1   . PHE A 1 85  ? 19.954  26.237  -7.236  1   22.56  ? 85   PHE A CE1   1 1 
ATOM   707  C  CE2   . PHE A 1 85  ? 19.844  24.554  -8.911  1   23.09  ? 85   PHE A CE2   1 1 
ATOM   708  C  CZ    . PHE A 1 85  ? 19.264  25.6    -8.229  1   22.77  ? 85   PHE A CZ    1 1 
ATOM   709  N  N     . LEU A 1 86  ? 22.34   24.577  -3.934  1   24.7   ? 86   LEU A N     1 1 
ATOM   710  C  CA    . LEU A 1 86  ? 22.262  25.479  -2.784  1   26.62  ? 86   LEU A CA    1 1 
ATOM   711  C  C     . LEU A 1 86  ? 23.142  24.922  -1.684  1   30.35  ? 86   LEU A C     1 1 
ATOM   712  O  O     . LEU A 1 86  ? 23.425  23.717  -1.659  1   30.23  ? 86   LEU A O     1 1 
ATOM   713  C  CB    . LEU A 1 86  ? 20.826  25.754  -2.304  1   25.91  ? 86   LEU A CB    1 1 
ATOM   714  C  CG    . LEU A 1 86  ? 19.884  26.431  -3.307  1   26.15  ? 86   LEU A CG    1 1 
ATOM   715  C  CD1   . LEU A 1 86  ? 18.497  26.682  -2.685  1   25.67  ? 86   LEU A CD1   1 1 
ATOM   716  C  CD2   . LEU A 1 86  ? 20.499  27.72   -3.889  1   26.41  ? 86   LEU A CD2   1 1 
ATOM   717  N  N     . TYR A 1 87  ? 23.663  25.791  -0.822  1   33.57  ? 87   TYR A N     1 1 
ATOM   718  C  CA    . TYR A 1 87  ? 24.567  25.336  0.25    1   37.39  ? 87   TYR A CA    1 1 
ATOM   719  C  C     . TYR A 1 87  ? 23.612  24.857  1.312   1   38.45  ? 87   TYR A C     1 1 
ATOM   720  O  O     . TYR A 1 87  ? 23.179  25.662  2.149   1   39.01  ? 87   TYR A O     1 1 
ATOM   721  C  CB    . TYR A 1 87  ? 25.457  26.514  0.733   1   39.08  ? 87   TYR A CB    1 1 
ATOM   722  C  CG    . TYR A 1 87  ? 26.551  26.145  1.71    1   42.07  ? 87   TYR A CG    1 1 
ATOM   723  C  CD1   . TYR A 1 87  ? 27.469  25.148  1.412   1   44.03  ? 87   TYR A CD1   1 1 
ATOM   724  C  CD2   . TYR A 1 87  ? 26.739  26.871  2.878   1   43.94  ? 87   TYR A CD2   1 1 
ATOM   725  C  CE1   . TYR A 1 87  ? 28.511  24.839  2.285   1   45.43  ? 87   TYR A CE1   1 1 
ATOM   726  C  CE2   . TYR A 1 87  ? 27.77   26.567  3.762   1   45.27  ? 87   TYR A CE2   1 1 
ATOM   727  C  CZ    . TYR A 1 87  ? 28.652  25.544  3.466   1   46.6   ? 87   TYR A CZ    1 1 
ATOM   728  O  OH    . TYR A 1 87  ? 29.679  25.25   4.334   1   48.6   ? 87   TYR A OH    1 1 
ATOM   729  N  N     . GLU A 1 88  ? 23.158  23.575  1.191   1   37.92  ? 88   GLU A N     1 1 
ATOM   730  C  CA    . GLU A 1 88  ? 22.121  23.034  2.083   1   36.56  ? 88   GLU A CA    1 1 
ATOM   731  C  C     . GLU A 1 88  ? 22.477  21.718  2.634   1   35     ? 88   GLU A C     1 1 
ATOM   732  O  O     . GLU A 1 88  ? 22.912  20.821  1.907   1   36.21  ? 88   GLU A O     1 1 
ATOM   733  C  CB    . GLU A 1 88  ? 20.74   22.975  1.424   1   37.44  ? 88   GLU A CB    1 1 
ATOM   734  C  CG    . GLU A 1 88  ? 20.229  24.311  0.929   1   40.18  ? 88   GLU A CG    1 1 
ATOM   735  C  CD    . GLU A 1 88  ? 19.919  25.359  1.982   1   46.54  ? 88   GLU A CD    1 1 
ATOM   736  O  OE1   . GLU A 1 88  ? 20.15   25.096  3.185   1   48     ? 88   GLU A OE1   1 1 
ATOM   737  O  OE2   . GLU A 1 88  ? 19.432  26.448  1.602   1   48.83  ? 88   GLU A OE2   1 1 
ATOM   738  N  N     . THR A 1 89  ? 22.305  21.586  3.939   1   32.72  ? 89   THR A N     1 1 
ATOM   739  C  CA    . THR A 1 89  ? 22.682  20.362  4.625   1   30.97  ? 89   THR A CA    1 1 
ATOM   740  C  C     . THR A 1 89  ? 21.496  19.76   5.359   1   27.65  ? 89   THR A C     1 1 
ATOM   741  O  O     . THR A 1 89  ? 20.894  20.414  6.215   1   27.32  ? 89   THR A O     1 1 
ATOM   742  C  CB    . THR A 1 89  ? 23.83   20.667  5.6     1   32.99  ? 89   THR A CB    1 1 
ATOM   743  O  OG1   . THR A 1 89  ? 24.877  21.335  4.901   1   34.95  ? 89   THR A OG1   1 1 
ATOM   744  C  CG2   . THR A 1 89  ? 24.395  19.426  6.238   1   33.27  ? 89   THR A CG2   1 1 
ATOM   745  N  N     . PRO A 1 90  ? 21.165  18.492  5.077   1   25.03  ? 90   PRO A N     1 1 
ATOM   746  C  CA    . PRO A 1 90  ? 20.114  17.834  5.875   1   23.27  ? 90   PRO A CA    1 1 
ATOM   747  C  C     . PRO A 1 90  ? 20.626  17.485  7.288   1   21.31  ? 90   PRO A C     1 1 
ATOM   748  O  O     . PRO A 1 90  ? 21.797  17.73   7.596   1   21.29  ? 90   PRO A O     1 1 
ATOM   749  C  CB    . PRO A 1 90  ? 19.769  16.58   5.047   1   24.06  ? 90   PRO A CB    1 1 
ATOM   750  C  CG    . PRO A 1 90  ? 20.962  16.312  4.242   1   25.07  ? 90   PRO A CG    1 1 
ATOM   751  C  CD    . PRO A 1 90  ? 21.803  17.564  4.122   1   24.19  ? 90   PRO A CD    1 1 
ATOM   752  N  N     . ASP A 1 91  ? 19.783  16.887  8.14    1   19.79  ? 91   ASP A N     1 1 
ATOM   753  C  CA    . ASP A 1 91  ? 20.24   16.451  9.458   1   18.91  ? 91   ASP A CA    1 1 
ATOM   754  C  C     . ASP A 1 91  ? 21      15.128  9.366   1   19.07  ? 91   ASP A C     1 1 
ATOM   755  O  O     . ASP A 1 91  ? 22.039  14.976  10.004  1   19.59  ? 91   ASP A O     1 1 
ATOM   756  C  CB    . ASP A 1 91  ? 19.097  16.405  10.461  1   18.56  ? 91   ASP A CB    1 1 
ATOM   757  C  CG    . ASP A 1 91  ? 18.524  17.79   10.766  1   21.8   ? 91   ASP A CG    1 1 
ATOM   758  O  OD1   . ASP A 1 91  ? 19.229  18.806  10.505  1   19.97  ? 91   ASP A OD1   1 1 
ATOM   759  O  OD2   . ASP A 1 91  ? 17.385  17.86   11.271  1   22.68  ? 91   ASP A OD2   1 1 
ATOM   760  N  N     . VAL A 1 92  ? 20.488  14.17   8.559   1   18     ? 92   VAL A N     1 1 
ATOM   761  C  CA    . VAL A 1 92  ? 21.125  12.86   8.362   1   17.24  ? 92   VAL A CA    1 1 
ATOM   762  C  C     . VAL A 1 92  ? 21.125  12.493  6.879   1   16.44  ? 92   VAL A C     1 1 
ATOM   763  O  O     . VAL A 1 92  ? 20.173  12.8    6.175   1   16.88  ? 92   VAL A O     1 1 
ATOM   764  C  CB    . VAL A 1 92  ? 20.354  11.764  9.168   1   18.7   ? 92   VAL A CB    1 1 
ATOM   765  C  CG1   . VAL A 1 92  ? 20.733  10.355  8.734   1   20.57  ? 92   VAL A CG1   1 1 
ATOM   766  C  CG2   . VAL A 1 92  ? 20.538  11.916  10.671  1   19.24  ? 92   VAL A CG2   1 1 
ATOM   767  N  N     . ILE A 1 93  ? 22.157  11.786  6.422   1   15.7   ? 93   ILE A N     1 1 
ATOM   768  C  CA    . ILE A 1 93  ? 22.227  11.146  5.115   1   15.57  ? 93   ILE A CA    1 1 
ATOM   769  C  C     . ILE A 1 93  ? 22.485  9.658   5.408   1   14.66  ? 93   ILE A C     1 1 
ATOM   770  O  O     . ILE A 1 93  ? 23.481  9.351   6.059   1   14.87  ? 93   ILE A O     1 1 
ATOM   771  C  CB    . ILE A 1 93  ? 23.392  11.65   4.259   1   16.41  ? 93   ILE A CB    1 1 
ATOM   772  C  CG1   . ILE A 1 93  ? 23.312  13.171  3.976   1   18.74  ? 93   ILE A CG1   1 1 
ATOM   773  C  CG2   . ILE A 1 93  ? 23.524  10.8    2.964   1   15.99  ? 93   ILE A CG2   1 1 
ATOM   774  C  CD1   . ILE A 1 93  ? 22.236  13.547  3.055   1   21.42  ? 93   ILE A CD1   1 1 
ATOM   775  N  N     . ILE A 1 94  ? 21.672  8.746   4.881   1   14.13  ? 94   ILE A N     1 1 
ATOM   776  C  CA    . ILE A 1 94  ? 21.9    7.312   5.048   1   14.3   ? 94   ILE A CA    1 1 
ATOM   777  C  C     . ILE A 1 94  ? 22.429  6.747   3.755   1   15.42  ? 94   ILE A C     1 1 
ATOM   778  O  O     . ILE A 1 94  ? 21.84   7       2.715   1   15.49  ? 94   ILE A O     1 1 
ATOM   779  C  CB    . ILE A 1 94  ? 20.633  6.552   5.448   1   13.74  ? 94   ILE A CB    1 1 
ATOM   780  C  CG1   . ILE A 1 94  ? 19.952  7.156   6.696   1   14.25  ? 94   ILE A CG1   1 1 
ATOM   781  C  CG2   . ILE A 1 94  ? 20.928  5.062   5.605   1   14.61  ? 94   ILE A CG2   1 1 
ATOM   782  C  CD1   . ILE A 1 94  ? 18.548  6.48    6.979   1   15.94  ? 94   ILE A CD1   1 1 
ATOM   783  N  N     . THR A 1 95  ? 23.558  5.998   3.802   1   15.35  ? 95   THR A N     1 1 
ATOM   784  C  CA    . THR A 1 95  ? 24.153  5.427   2.601   1   15.91  ? 95   THR A CA    1 1 
ATOM   785  C  C     . THR A 1 95  ? 24.275  3.894   2.675   1   17.06  ? 95   THR A C     1 1 
ATOM   786  O  O     . THR A 1 95  ? 24.256  3.303   3.746   1   16.83  ? 95   THR A O     1 1 
ATOM   787  C  CB    . THR A 1 95  ? 25.526  6.08    2.294   1   16.47  ? 95   THR A CB    1 1 
ATOM   788  O  OG1   . THR A 1 95  ? 26.485  5.626   3.251   1   15.89  ? 95   THR A OG1   1 1 
ATOM   789  C  CG2   . THR A 1 95  ? 25.472  7.618   2.267   1   16.87  ? 95   THR A CG2   1 1 
ATOM   790  N  N     . SER A 1 96  ? 24.39   3.265   1.524   1   18.08  ? 96   SER A N     1 1 
ATOM   791  C  CA    . SER A 1 96  ? 24.652  1.854   1.395   1   19.49  ? 96   SER A CA    1 1 
ATOM   792  C  C     . SER A 1 96  ? 26.105  1.728   0.917   1   20.9   ? 96   SER A C     1 1 
ATOM   793  O  O     . SER A 1 96  ? 26.5    2.425   -0.021  1   20.99  ? 96   SER A O     1 1 
ATOM   794  C  CB    . SER A 1 96  ? 23.719  1.252   0.352   1   21.81  ? 96   SER A CB    1 1 
ATOM   795  O  OG    . SER A 1 96  ? 24.079  -0.091  0.074   1   27.29  ? 96   SER A OG    1 1 
ATOM   796  N  N     . LEU A 1 97  ? 26.903  0.858   1.544   1   21.96  ? 97   LEU A N     1 1 
ATOM   797  C  CA    . LEU A 1 97  ? 28.279  0.616   1.108   1   24.1   ? 97   LEU A CA    1 1 
ATOM   798  C  C     . LEU A 1 97  ? 28.31   -0.563  0.114   1   25.37  ? 97   LEU A C     1 1 
ATOM   799  O  O     . LEU A 1 97  ? 27.941  -1.678  0.472   1   24.92  ? 97   LEU A O     1 1 
ATOM   800  C  CB    . LEU A 1 97  ? 29.148  0.222   2.311   1   25.26  ? 97   LEU A CB    1 1 
ATOM   801  C  CG    . LEU A 1 97  ? 30.076  1.236   2.95    1   27.64  ? 97   LEU A CG    1 1 
ATOM   802  C  CD1   . LEU A 1 97  ? 31.109  0.519   3.838   1   27.34  ? 97   LEU A CD1   1 1 
ATOM   803  C  CD2   . LEU A 1 97  ? 30.896  1.964   1.898   1   29.61  ? 97   LEU A CD2   1 1 
ATOM   804  N  N     . ASN A 1 98  ? 28.764  -0.328  -1.106  1   26.94  ? 98   ASN A N     1 1 
ATOM   805  C  CA    . ASN A 1 98  ? 28.918  -1.379  -2.115  1   29.33  ? 98   ASN A CA    1 1 
ATOM   806  C  C     . ASN A 1 98  ? 30.062  -1.037  -3.076  1   30.79  ? 98   ASN A C     1 1 
ATOM   807  O  O     . ASN A 1 98  ? 30.187  0.103   -3.526  1   31.04  ? 98   ASN A O     1 1 
ATOM   808  C  CB    . ASN A 1 98  ? 27.636  -1.648  -2.872  1   31.39  ? 98   ASN A CB    1 1 
ATOM   809  N  N     . ASN A 1 99  ? 30.876  -2.044  -3.396  1   31.45  ? 99   ASN A N     1 1 
ATOM   810  C  CA    . ASN A 1 99  ? 32.059  -1.985  -4.26   1   32.08  ? 99   ASN A CA    1 1 
ATOM   811  C  C     . ASN A 1 99  ? 32.985  -0.813  -3.932  1   29.99  ? 99   ASN A C     1 1 
ATOM   812  O  O     . ASN A 1 99  ? 33.442  -0.108  -4.83   1   30.11  ? 99   ASN A O     1 1 
ATOM   813  C  CB    . ASN A 1 99  ? 31.757  -2.052  -5.781  1   35.65  ? 99   ASN A CB    1 1 
ATOM   814  C  CG    . ASN A 1 99  ? 30.329  -1.841  -6.219  1   41.37  ? 99   ASN A CG    1 1 
ATOM   815  O  OD1   . ASN A 1 99  ? 29.865  -0.705  -6.391  1   43.8   ? 99   ASN A OD1   1 1 
ATOM   816  N  ND2   . ASN A 1 99  ? 29.608  -2.94   -6.414  1   42.73  ? 99   ASN A ND2   1 1 
ATOM   817  N  N     . GLY A 1 100 ? 33.305  -0.663  -2.655  1   28.43  ? 100  GLY A N     1 1 
ATOM   818  C  CA    . GLY A 1 100 ? 34.244  0.352   -2.192  1   28.06  ? 100  GLY A CA    1 1 
ATOM   819  C  C     . GLY A 1 100 ? 33.761  1.783   -2.21   1   27.14  ? 100  GLY A C     1 1 
ATOM   820  O  O     . GLY A 1 100 ? 34.566  2.706   -2.035  1   28.21  ? 100  GLY A O     1 1 
ATOM   821  N  N     . LYS A 1 101 ? 32.45   1.994   -2.4    1   25.43  ? 101  LYS A N     1 1 
ATOM   822  C  CA    . LYS A 1 101 ? 31.905  3.344   -2.421  1   23.93  ? 101  LYS A CA    1 1 
ATOM   823  C  C     . LYS A 1 101 ? 30.527  3.425   -1.711  1   21.65  ? 101  LYS A C     1 1 
ATOM   824  O  O     . LYS A 1 101 ? 29.884  2.4     -1.429  1   20.36  ? 101  LYS A O     1 1 
ATOM   825  C  CB    . LYS A 1 101 ? 31.843  3.859   -3.866  1   26.86  ? 101  LYS A CB    1 1 
ATOM   826  C  CG    . LYS A 1 101 ? 30.716  3.228   -4.67   1   34.67  ? 101  LYS A CG    1 1 
ATOM   827  C  CD    . LYS A 1 101 ? 30.722  3.703   -6.102  1   42.42  ? 101  LYS A CD    1 1 
ATOM   828  C  CE    . LYS A 1 101 ? 29.404  3.459   -6.796  1   48.15  ? 101  LYS A CE    1 1 
ATOM   829  N  NZ    . LYS A 1 101 ? 28.317  4.306   -6.242  1   51.21  ? 101  LYS A NZ    1 1 
ATOM   830  N  N     . GLU A 1 102 ? 30.084  4.656   -1.419  1   20.01  ? 102  GLU A N     1 1 
ATOM   831  C  CA    . GLU A 1 102 ? 28.815  4.905   -0.764  1   18.92  ? 102  GLU A CA    1 1 
ATOM   832  C  C     . GLU A 1 102 ? 27.773  5.347   -1.766  1   19.21  ? 102  GLU A C     1 1 
ATOM   833  O  O     . GLU A 1 102 ? 28.081  6.104   -2.693  1   19.28  ? 102  GLU A O     1 1 
ATOM   834  C  CB    . GLU A 1 102 ? 28.961  5.984   0.297   1   18.88  ? 102  GLU A CB    1 1 
ATOM   835  C  CG    . GLU A 1 102 ? 30.075  5.723   1.281   1   21.01  ? 102  GLU A CG    1 1 
ATOM   836  C  CD    . GLU A 1 102 ? 30.009  6.711   2.423   1   23.26  ? 102  GLU A CD    1 1 
ATOM   837  O  OE1   . GLU A 1 102 ? 28.913  6.893   2.992   1   24.54  ? 102  GLU A OE1   1 1 
ATOM   838  O  OE2   . GLU A 1 102 ? 31.051  7.311   2.745   1   23.88  ? 102  GLU A OE2   1 1 
ATOM   839  N  N     . GLU A 1 103 ? 26.532  4.88    -1.574  1   18.37  ? 103  GLU A N     1 1 
ATOM   840  C  CA    . GLU A 1 103 ? 25.417  5.266   -2.413  1   18.71  ? 103  GLU A CA    1 1 
ATOM   841  C  C     . GLU A 1 103 ? 24.341  5.833   -1.48   1   18.93  ? 103  GLU A C     1 1 
ATOM   842  O  O     . GLU A 1 103 ? 23.898  5.123   -0.578  1   19.64  ? 103  GLU A O     1 1 
ATOM   843  C  CB    . GLU A 1 103 ? 24.835  4.046   -3.154  1   20.44  ? 103  GLU A CB    1 1 
ATOM   844  N  N     . ILE A 1 104 ? 23.91   7.079   -1.692  1   17.74  ? 104  ILE A N     1 1 
ATOM   845  C  CA    . ILE A 1 104 ? 22.868  7.673   -0.855  1   16.91  ? 104  ILE A CA    1 1 
ATOM   846  C  C     . ILE A 1 104 ? 21.51   6.95    -1.006  1   16.5   ? 104  ILE A C     1 1 
ATOM   847  O  O     . ILE A 1 104 ? 21.077  6.674   -2.121  1   17.26  ? 104  ILE A O     1 1 
ATOM   848  C  CB    . ILE A 1 104 ? 22.772  9.191   -1.107  1   16.91  ? 104  ILE A CB    1 1 
ATOM   849  C  CG1   . ILE A 1 104 ? 24.081  9.891   -0.66   1   17.45  ? 104  ILE A CG1   1 1 
ATOM   850  C  CG2   . ILE A 1 104 ? 21.51   9.797   -0.435  1   16.88  ? 104  ILE A CG2   1 1 
ATOM   851  C  CD1   . ILE A 1 104 ? 24.118  11.378  -0.896  1   18.15  ? 104  ILE A CD1   1 1 
ATOM   852  N  N     . LEU A 1 105 ? 20.891  6.582   0.122   1   15.34  ? 105  LEU A N     1 1 
ATOM   853  C  CA    . LEU A 1 105 ? 19.563  5.976   0.164   1   15.59  ? 105  LEU A CA    1 1 
ATOM   854  C  C     . LEU A 1 105 ? 18.506  7.075   0.4     1   14.75  ? 105  LEU A C     1 1 
ATOM   855  O  O     . LEU A 1 105 ? 17.434  7.048   -0.215  1   14.72  ? 105  LEU A O     1 1 
ATOM   856  C  CB    . LEU A 1 105 ? 19.495  4.904   1.269   1   16.54  ? 105  LEU A CB    1 1 
ATOM   857  C  CG    . LEU A 1 105 ? 20.423  3.703   1.052   1   18.16  ? 105  LEU A CG    1 1 
ATOM   858  C  CD1   . LEU A 1 105 ? 20.366  2.745   2.22    1   18.94  ? 105  LEU A CD1   1 1 
ATOM   859  C  CD2   . LEU A 1 105 ? 20.079  2.982   -0.216  1   18.93  ? 105  LEU A CD2   1 1 
ATOM   860  N  N     . MET A 1 106 ? 18.808  8.025   1.3     1   13.4   ? 106  MET A N     1 1 
ATOM   861  C  CA    . MET A 1 106 ? 17.902  9.133   1.612   1   13.25  ? 106  MET A CA    1 1 
ATOM   862  C  C     . MET A 1 106 ? 18.591  10.238  2.427   1   12.9   ? 106  MET A C     1 1 
ATOM   863  O  O     . MET A 1 106 ? 19.615  10.014  3.066   1   12.55  ? 106  MET A O     1 1 
ATOM   864  C  CB    . MET A 1 106 ? 16.67   8.623   2.395   1   13.24  ? 106  MET A CB    1 1 
ATOM   865  C  CG    . MET A 1 106 ? 16.999  8.193   3.812   1   14.53  ? 106  MET A CG    1 1 
ATOM   866  S  SD    . MET A 1 106 ? 15.647  7.269   4.561   1   16.72  ? 106  MET A SD    1 1 
ATOM   867  C  CE    . MET A 1 106 ? 15.814  5.726   3.658   1   12.51  ? 106  MET A CE    1 1 
ATOM   868  N  N     . ALA A 1 107 ? 17.984  11.429  2.422   1   12.67  ? 107  ALA A N     1 1 
ATOM   869  C  CA    . ALA A 1 107 ? 18.383  12.545  3.248   1   13.33  ? 107  ALA A CA    1 1 
ATOM   870  C  C     . ALA A 1 107 ? 17.179  12.755  4.201   1   14.39  ? 107  ALA A C     1 1 
ATOM   871  O  O     . ALA A 1 107 ? 16.029  12.702  3.771   1   13.96  ? 107  ALA A O     1 1 
ATOM   872  C  CB    . ALA A 1 107 ? 18.595  13.795  2.387   1   12.79  ? 107  ALA A CB    1 1 
ATOM   873  N  N     . ILE A 1 108 ? 17.444  12.966  5.481   1   14.71  ? 108  ILE A N     1 1 
ATOM   874  C  CA    . ILE A 1 108 ? 16.41   13.174  6.476   1   15.14  ? 108  ILE A CA    1 1 
ATOM   875  C  C     . ILE A 1 108 ? 16.67   14.457  7.256   1   14.91  ? 108  ILE A C     1 1 
ATOM   876  O  O     . ILE A 1 108 ? 17.813  14.768  7.615   1   14.1   ? 108  ILE A O     1 1 
ATOM   877  C  CB    . ILE A 1 108 ? 16.333  11.944  7.451   1   16.03  ? 108  ILE A CB    1 1 
ATOM   878  C  CG1   . ILE A 1 108 ? 16.039  10.639  6.713   1   16.47  ? 108  ILE A CG1   1 1 
ATOM   879  C  CG2   . ILE A 1 108 ? 15.284  12.192  8.553   1   16.74  ? 108  ILE A CG2   1 1 
ATOM   880  C  CD1   . ILE A 1 108 ? 16.113  9.357   7.629   1   17.43  ? 108  ILE A CD1   1 1 
ATOM   881  N  N     . VAL A 1 109 ? 15.599  15.222  7.5     1   15.42  ? 109  VAL A N     1 1 
ATOM   882  C  CA    . VAL A 1 109 ? 15.655  16.4    8.323   1   16.46  ? 109  VAL A CA    1 1 
ATOM   883  C  C     . VAL A 1 109 ? 14.635  16.206  9.461   1   18.04  ? 109  VAL A C     1 1 
ATOM   884  O  O     . VAL A 1 109 ? 13.518  15.752  9.223   1   17.92  ? 109  VAL A O     1 1 
ATOM   885  C  CB    . VAL A 1 109 ? 15.382  17.691  7.503   1   17.97  ? 109  VAL A CB    1 1 
ATOM   886  C  CG1   . VAL A 1 109 ? 15.155  18.87   8.43    1   18.88  ? 109  VAL A CG1   1 1 
ATOM   887  C  CG2   . VAL A 1 109 ? 16.53   17.992  6.541   1   17.62  ? 109  VAL A CG2   1 1 
ATOM   888  N  N     . PHE A 1 110 ? 15.037  16.479  10.696  1   19.62  ? 110  PHE A N     1 1 
ATOM   889  C  CA    . PHE A 1 110 ? 14.173  16.383  11.86   1   22.21  ? 110  PHE A CA    1 1 
ATOM   890  C  C     . PHE A 1 110 ? 13.879  17.795  12.366  1   25.2   ? 110  PHE A C     1 1 
ATOM   891  O  O     . PHE A 1 110 ? 14.81   18.58   12.552  1   26.5   ? 110  PHE A O     1 1 
ATOM   892  C  CB    . PHE A 1 110 ? 14.866  15.593  12.982  1   22.69  ? 110  PHE A CB    1 1 
ATOM   893  C  CG    . PHE A 1 110 ? 15.136  14.14   12.693  1   24.45  ? 110  PHE A CG    1 1 
ATOM   894  C  CD1   . PHE A 1 110 ? 14.123  13.196  12.791  1   25.48  ? 110  PHE A CD1   1 1 
ATOM   895  C  CD2   . PHE A 1 110 ? 16.417  13.703  12.396  1   26.02  ? 110  PHE A CD2   1 1 
ATOM   896  C  CE1   . PHE A 1 110 ? 14.378  11.852  12.554  1   26.73  ? 110  PHE A CE1   1 1 
ATOM   897  C  CE2   . PHE A 1 110 ? 16.678  12.357  12.182  1   27.12  ? 110  PHE A CE2   1 1 
ATOM   898  C  CZ    . PHE A 1 110 ? 15.651  11.437  12.238  1   26.88  ? 110  PHE A CZ    1 1 
ATOM   899  N  N     . CYS A 1 111 ? 12.618  18.1    12.664  1   26.65  ? 111  CYS A N     1 1 
ATOM   900  C  CA    . CYS A 1 111 ? 12.214  19.396  13.185  1   29.23  ? 111  CYS A CA    1 1 
ATOM   901  C  C     . CYS A 1 111 ? 11.323  19.187  14.423  1   32.63  ? 111  CYS A C     1 1 
ATOM   902  O  O     . CYS A 1 111 ? 10.397  18.365  14.4    1   32.64  ? 111  CYS A O     1 1 
ATOM   903  C  CB    . CYS A 1 111 ? 11.5    20.181  12.092  1   30.79  ? 111  CYS A CB    1 1 
ATOM   904  S  SG    . CYS A 1 111 ? 11.26   21.938  12.461  1   37.92  ? 111  CYS A SG    1 1 
ATOM   905  N  N     . SER A 1 112 ? 11.594  19.917  15.515  1   35.23  ? 112  SER A N     1 1 
ATOM   906  C  CA    . SER A 1 112 ? 10.816  19.741  16.758  1   37.98  ? 112  SER A CA    1 1 
ATOM   907  C  C     . SER A 1 112 ? 9.363   20.236  16.728  1   39.5   ? 112  SER A C     1 1 
ATOM   908  O  O     . SER A 1 112 ? 8.542   19.836  17.573  1   39.96  ? 112  SER A O     1 1 
ATOM   909  C  CB    . SER A 1 112 ? 11.539  20.403  17.92   1   40.76  ? 112  SER A CB    1 1 
ATOM   910  O  OG    . SER A 1 112 ? 11.581  21.796  17.68   1   45.22  ? 112  SER A OG    1 1 
ATOM   911  N  N     . ALA A 1 113 ? 9.052   21.14   15.791  1   39.45  ? 113  ALA A N     1 1 
ATOM   912  C  CA    . ALA A 1 113 ? 7.716   21.73   15.717  1   39.01  ? 113  ALA A CA    1 1 
ATOM   913  C  C     . ALA A 1 113 ? 7.381   22.162  14.327  1   38.01  ? 113  ALA A C     1 1 
ATOM   914  O  O     . ALA A 1 113 ? 8.264   22.605  13.587  1   38.51  ? 113  ALA A O     1 1 
ATOM   915  C  CB    . ALA A 1 113 ? 7.65    22.957  16.615  1   38.92  ? 113  ALA A CB    1 1 
ATOM   916  N  N     . LEU A 1 114 ? 6.091   22.104  13.989  1   36.38  ? 114  LEU A N     1 1 
ATOM   917  C  CA    . LEU A 1 114 ? 5.608   22.589  12.711  1   35.47  ? 114  LEU A CA    1 1 
ATOM   918  C  C     . LEU A 1 114 ? 5.703   24.136  12.78   1   34.05  ? 114  LEU A C     1 1 
ATOM   919  O  O     . LEU A 1 114 ? 4.917   24.783  13.473  1   34.54  ? 114  LEU A O     1 1 
ATOM   920  C  CB    . LEU A 1 114 ? 4.159   22.145  12.539  1   35.97  ? 114  LEU A CB    1 1 
ATOM   921  C  CG    . LEU A 1 114 ? 3.563   22.209  11.14   1   37.44  ? 114  LEU A CG    1 1 
ATOM   922  C  CD1   . LEU A 1 114 ? 4.416   21.416  10.129  1   37.31  ? 114  LEU A CD1   1 1 
ATOM   923  C  CD2   . LEU A 1 114 ? 2.099   21.723  11.161  1   37.86  ? 114  LEU A CD2   1 1 
ATOM   924  N  N     . GLN A 1 115 ? 6.721   24.696  12.138  1   31.99  ? 115  GLN A N     1 1 
ATOM   925  C  CA    . GLN A 1 115 ? 6.988   26.123  12.12   1   30.52  ? 115  GLN A CA    1 1 
ATOM   926  C  C     . GLN A 1 115 ? 5.962   26.92   11.322  1   28.39  ? 115  GLN A C     1 1 
ATOM   927  O  O     . GLN A 1 115 ? 5.366   26.416  10.368  1   28.38  ? 115  GLN A O     1 1 
ATOM   928  C  CB    . GLN A 1 115 ? 8.392   26.36   11.604  1   33.13  ? 115  GLN A CB    1 1 
ATOM   929  C  CG    . GLN A 1 115 ? 9.425   25.75   12.533  1   39.06  ? 115  GLN A CG    1 1 
ATOM   930  C  CD    . GLN A 1 115 ? 10.769  25.595  11.891  1   44.74  ? 115  GLN A CD    1 1 
ATOM   931  O  OE1   . GLN A 1 115 ? 10.905  25.541  10.663  1   47.12  ? 115  GLN A OE1   1 1 
ATOM   932  N  NE2   . GLN A 1 115 ? 11.791  25.492  12.719  1   46.33  ? 115  GLN A NE2   1 1 
ATOM   933  N  N     . ALA A 1 116 ? 5.718   28.152  11.744  1   26.79  ? 116  ALA A N     1 1 
ATOM   934  C  CA    . ALA A 1 116 ? 4.711   28.985  11.105  1   25.62  ? 116  ALA A CA    1 1 
ATOM   935  C  C     . ALA A 1 116 ? 5.292   30.322  10.573  1   23.92  ? 116  ALA A C     1 1 
ATOM   936  O  O     . ALA A 1 116 ? 6.47    30.616  10.812  1   23.48  ? 116  ALA A O     1 1 
ATOM   937  C  CB    . ALA A 1 116 ? 3.533   29.179  12.066  1   25.69  ? 116  ALA A CB    1 1 
ATOM   938  N  N     . GLY A 1 117 ? 4.498   31.073  9.79    1   22.98  ? 117  GLY A N     1 1 
ATOM   939  C  CA    . GLY A 1 117 ? 4.923   32.325  9.188   1   22.21  ? 117  GLY A CA    1 1 
ATOM   940  C  C     . GLY A 1 117 ? 6.051   32.097  8.202   1   21.39  ? 117  GLY A C     1 1 
ATOM   941  O  O     . GLY A 1 117 ? 6.092   31.064  7.531   1   21.78  ? 117  GLY A O     1 1 
ATOM   942  N  N     . ASN A 1 118 ? 6.972   33.043  8.104   1   20.24  ? 118  ASN A N     1 1 
ATOM   943  C  CA    . ASN A 1 118 ? 8.119   32.898  7.196   1   19.5   ? 118  ASN A CA    1 1 
ATOM   944  C  C     . ASN A 1 118 ? 9.172   31.93   7.733   1   19.44  ? 118  ASN A C     1 1 
ATOM   945  O  O     . ASN A 1 118 ? 10.066  31.537  6.981   1   19.78  ? 118  ASN A O     1 1 
ATOM   946  C  CB    . ASN A 1 118 ? 8.735   34.263  6.775   1   18.57  ? 118  ASN A CB    1 1 
ATOM   947  C  CG    . ASN A 1 118 ? 9.285   35.158  7.852   1   19.79  ? 118  ASN A CG    1 1 
ATOM   948  O  OD1   . ASN A 1 118 ? 9.515   34.756  8.995   1   20.46  ? 118  ASN A OD1   1 1 
ATOM   949  N  ND2   . ASN A 1 118 ? 9.538   36.415  7.48    1   20.31  ? 118  ASN A ND2   1 1 
ATOM   950  N  N     . GLN A 1 119 ? 9.084   31.544  9.022   1   19     ? 119  GLN A N     1 1 
ATOM   951  C  CA    . GLN A 1 119 ? 9.954   30.533  9.578   1   19.8   ? 119  GLN A CA    1 1 
ATOM   952  C  C     . GLN A 1 119 ? 9.636   29.182  8.894   1   19.39  ? 119  GLN A C     1 1 
ATOM   953  O  O     . GLN A 1 119 ? 10.532  28.344  8.79    1   20.02  ? 119  GLN A O     1 1 
ATOM   954  C  CB    . GLN A 1 119 ? 9.774   30.428  11.097  1   23.4   ? 119  GLN A CB    1 1 
ATOM   955  C  CG    . GLN A 1 119 ? 10.721  29.433  11.739  1   32.11  ? 119  GLN A CG    1 1 
ATOM   956  C  CD    . GLN A 1 119 ? 10.449  29.19   13.202  1   42     ? 119  GLN A CD    1 1 
ATOM   957  O  OE1   . GLN A 1 119 ? 9.3     29.243  13.662  1   44.68  ? 119  GLN A OE1   1 1 
ATOM   958  N  NE2   . GLN A 1 119 ? 11.516  28.881  13.962  1   44.42  ? 119  GLN A NE2   1 1 
ATOM   959  N  N     . ALA A 1 120 ? 8.39    28.987  8.366   1   18.05  ? 120  ALA A N     1 1 
ATOM   960  C  CA    . ALA A 1 120 ? 8.034   27.753  7.672   1   18.38  ? 120  ALA A CA    1 1 
ATOM   961  C  C     . ALA A 1 120 ? 8.814   27.571  6.386   1   18.82  ? 120  ALA A C     1 1 
ATOM   962  O  O     . ALA A 1 120 ? 9.026   26.436  5.993   1   19.82  ? 120  ALA A O     1 1 
ATOM   963  C  CB    . ALA A 1 120 ? 6.546   27.709  7.376   1   17.39  ? 120  ALA A CB    1 1 
ATOM   964  N  N     . TRP A 1 121 ? 9.157   28.661  5.684   1   18.1   ? 121  TRP A N     1 1 
ATOM   965  C  CA    . TRP A 1 121 ? 9.935   28.525  4.448   1   17.03  ? 121  TRP A CA    1 1 
ATOM   966  C  C     . TRP A 1 121 ? 11.395  28.93   4.603   1   16.12  ? 121  TRP A C     1 1 
ATOM   967  O  O     . TRP A 1 121 ? 12.164  28.755  3.657   1   16.07  ? 121  TRP A O     1 1 
ATOM   968  C  CB    . TRP A 1 121 ? 9.279   29.249  3.258   1   16.7   ? 121  TRP A CB    1 1 
ATOM   969  C  CG    . TRP A 1 121 ? 9.11    30.726  3.404   1   17.62  ? 121  TRP A CG    1 1 
ATOM   970  C  CD1   . TRP A 1 121 ? 10.053  31.681  3.165   1   18.82  ? 121  TRP A CD1   1 1 
ATOM   971  C  CD2   . TRP A 1 121 ? 7.881   31.431  3.64    1   18.11  ? 121  TRP A CD2   1 1 
ATOM   972  N  NE1   . TRP A 1 121 ? 9.505   32.934  3.302   1   18.86  ? 121  TRP A NE1   1 1 
ATOM   973  C  CE2   . TRP A 1 121 ? 8.179   32.812  3.607   1   18.9   ? 121  TRP A CE2   1 1 
ATOM   974  C  CE3   . TRP A 1 121 ? 6.576   31.032  3.967   1   18.5   ? 121  TRP A CE3   1 1 
ATOM   975  C  CZ2   . TRP A 1 121 ? 7.204   33.796  3.82    1   18.92  ? 121  TRP A CZ2   1 1 
ATOM   976  C  CZ3   . TRP A 1 121 ? 5.615   32.009  4.184   1   18.93  ? 121  TRP A CZ3   1 1 
ATOM   977  C  CH2   . TRP A 1 121 ? 5.94    33.37   4.135   1   18.85  ? 121  TRP A CH2   1 1 
ATOM   978  N  N     . GLN A 1 122 ? 11.812  29.419  5.79    1   15.55  ? 122  GLN A N     1 1 
ATOM   979  C  CA    . GLN A 1 122 ? 13.186  29.851  6.056   1   15.56  ? 122  GLN A CA    1 1 
ATOM   980  C  C     . GLN A 1 122 ? 14.267  28.875  5.518   1   16.51  ? 122  GLN A C     1 1 
ATOM   981  O  O     . GLN A 1 122 ? 15.235  29.302  4.861   1   15.49  ? 122  GLN A O     1 1 
ATOM   982  C  CB    . GLN A 1 122 ? 13.376  30.137  7.554   1   15.98  ? 122  GLN A CB    1 1 
ATOM   983  C  CG    . GLN A 1 122 ? 14.793  30.585  7.927   1   20.87  ? 122  GLN A CG    1 1 
ATOM   984  C  CD    . GLN A 1 122 ? 14.73   31.265  9.267   1   28.46  ? 122  GLN A CD    1 1 
ATOM   985  O  OE1   . GLN A 1 122 ? 14.797  32.48   9.37    1   30.38  ? 122  GLN A OE1   1 1 
ATOM   986  N  NE2   . GLN A 1 122 ? 14.502  30.506  10.321  1   30.71  ? 122  GLN A NE2   1 1 
ATOM   987  N  N     . ARG A 1 123 ? 14.035  27.547  5.716   1   17.06  ? 123  ARG A N     1 1 
ATOM   988  C  CA    . ARG A 1 123 ? 14.935  26.489  5.261   1   17.87  ? 123  ARG A CA    1 1 
ATOM   989  C  C     . ARG A 1 123 ? 14.393  25.657  4.08    1   17.96  ? 123  ARG A C     1 1 
ATOM   990  O  O     . ARG A 1 123 ? 14.898  24.571  3.822   1   17.15  ? 123  ARG A O     1 1 
ATOM   991  C  CB    . ARG A 1 123 ? 15.328  25.564  6.418   1   19.76  ? 123  ARG A CB    1 1 
ATOM   992  C  CG    . ARG A 1 123 ? 15.916  26.305  7.591   1   23.9   ? 123  ARG A CG    1 1 
ATOM   993  C  CD    . ARG A 1 123 ? 17.401  26.084  7.61    1   30.35  ? 123  ARG A CD    1 1 
ATOM   994  N  NE    . ARG A 1 123 ? 17.806  25.264  8.747   1   34.43  ? 123  ARG A NE    1 1 
ATOM   995  C  CZ    . ARG A 1 123 ? 18.849  24.451  8.754   1   37.74  ? 123  ARG A CZ    1 1 
ATOM   996  N  NH1   . ARG A 1 123 ? 19.597  24.305  7.663   1   37.65  ? 123  ARG A NH1   1 1 
ATOM   997  N  NH2   . ARG A 1 123 ? 19.136  23.747  9.838   1   39.23  ? 123  ARG A NH2   1 1 
ATOM   998  N  N     . SER A 1 124 ? 13.461  26.209  3.312   1   19.17  ? 124  SER A N     1 1 
ATOM   999  C  CA    . SER A 1 124 ? 12.894  25.535  2.143   1   20.47  ? 124  SER A CA    1 1 
ATOM   1000 C  C     . SER A 1 124 ? 13.899  25.223  1.049   1   20.62  ? 124  SER A C     1 1 
ATOM   1001 O  O     . SER A 1 124 ? 13.635  24.358  0.214   1   20.57  ? 124  SER A O     1 1 
ATOM   1002 C  CB    . SER A 1 124 ? 11.737  26.33   1.56    1   23.06  ? 124  SER A CB    1 1 
ATOM   1003 O  OG    . SER A 1 124 ? 10.567  26.076  2.318   1   26.92  ? 124  SER A OG    1 1 
ATOM   1004 N  N     . GLY A 1 125 ? 15.027  25.941  1.04    1   20.66  ? 125  GLY A N     1 1 
ATOM   1005 C  CA    . GLY A 1 125 ? 16.125  25.694  0.116   1   20.55  ? 125  GLY A CA    1 1 
ATOM   1006 C  C     . GLY A 1 125 ? 16.656  24.283  0.247   1   19.27  ? 125  GLY A C     1 1 
ATOM   1007 O  O     . GLY A 1 125 ? 17.052  23.689  -0.753  1   18.94  ? 125  GLY A O     1 1 
ATOM   1008 N  N     . ARG A 1 126 ? 16.629  23.715  1.473   1   18.95  ? 126  ARG A N     1 1 
ATOM   1009 C  CA    . ARG A 1 126 ? 17.058  22.32   1.692   1   18.78  ? 126  ARG A CA    1 1 
ATOM   1010 C  C     . ARG A 1 126 ? 16.167  21.356  0.881   1   17.62  ? 126  ARG A C     1 1 
ATOM   1011 O  O     . ARG A 1 126 ? 16.695  20.539  0.117   1   17.36  ? 126  ARG A O     1 1 
ATOM   1012 C  CB    . ARG A 1 126 ? 16.955  21.883  3.165   1   20.67  ? 126  ARG A CB    1 1 
ATOM   1013 C  CG    . ARG A 1 126 ? 17.993  22.341  4.156   1   24.47  ? 126  ARG A CG    1 1 
ATOM   1014 C  CD    . ARG A 1 126 ? 17.702  21.708  5.528   1   27.65  ? 126  ARG A CD    1 1 
ATOM   1015 N  NE    . ARG A 1 126 ? 16.344  22.034  5.974   1   31.45  ? 126  ARG A NE    1 1 
ATOM   1016 C  CZ    . ARG A 1 126 ? 15.948  22.105  7.239   1   33.1   ? 126  ARG A CZ    1 1 
ATOM   1017 N  NH1   . ARG A 1 126 ? 16.809  21.891  8.221   1   31.84  ? 126  ARG A NH1   1 1 
ATOM   1018 N  NH2   . ARG A 1 126 ? 14.682  22.397  7.53    1   32.96  ? 126  ARG A NH2   1 1 
ATOM   1019 N  N     . ALA A 1 127 ? 14.83   21.425  1.074   1   16.75  ? 127  ALA A N     1 1 
ATOM   1020 C  CA    . ALA A 1 127 ? 13.903  20.529  0.385   1   16.63  ? 127  ALA A CA    1 1 
ATOM   1021 C  C     . ALA A 1 127 ? 13.961  20.726  -1.108  1   16.02  ? 127  ALA A C     1 1 
ATOM   1022 O  O     . ALA A 1 127 ? 13.893  19.746  -1.843  1   14.85  ? 127  ALA A O     1 1 
ATOM   1023 C  CB    . ALA A 1 127 ? 12.493  20.726  0.888   1   16.92  ? 127  ALA A CB    1 1 
ATOM   1024 N  N     . TYR A 1 128 ? 14.1    21.99   -1.566  1   16.15  ? 128  TYR A N     1 1 
ATOM   1025 C  CA    . TYR A 1 128 ? 14.18   22.246  -2.991  1   16.99  ? 128  TYR A CA    1 1 
ATOM   1026 C  C     . TYR A 1 128 ? 15.456  21.66   -3.6    1   17.14  ? 128  TYR A C     1 1 
ATOM   1027 O  O     . TYR A 1 128 ? 15.379  20.942  -4.595  1   17.01  ? 128  TYR A O     1 1 
ATOM   1028 C  CB    . TYR A 1 128 ? 14.024  23.742  -3.329  1   17.78  ? 128  TYR A CB    1 1 
ATOM   1029 C  CG    . TYR A 1 128 ? 14.498  24.057  -4.732  1   18.92  ? 128  TYR A CG    1 1 
ATOM   1030 C  CD1   . TYR A 1 128 ? 13.742  23.689  -5.841  1   19.34  ? 128  TYR A CD1   1 1 
ATOM   1031 C  CD2   . TYR A 1 128 ? 15.756  24.618  -4.954  1   19.81  ? 128  TYR A CD2   1 1 
ATOM   1032 C  CE1   . TYR A 1 128 ? 14.209  23.908  -7.135  1   20.4   ? 128  TYR A CE1   1 1 
ATOM   1033 C  CE2   . TYR A 1 128 ? 16.241  24.825  -6.241  1   20.34  ? 128  TYR A CE2   1 1 
ATOM   1034 C  CZ    . TYR A 1 128 ? 15.467  24.47   -7.331  1   21     ? 128  TYR A CZ    1 1 
ATOM   1035 O  OH    . TYR A 1 128 ? 15.961  24.691  -8.598  1   20.86  ? 128  TYR A OH    1 1 
ATOM   1036 N  N     . SER A 1 129 ? 16.625  22.015  -3.033  1   16.89  ? 129  SER A N     1 1 
ATOM   1037 C  CA    . SER A 1 129 ? 17.934  21.674  -3.542  1   16.28  ? 129  SER A CA    1 1 
ATOM   1038 C  C     . SER A 1 129 ? 18.183  20.184  -3.462  1   16.5   ? 129  SER A C     1 1 
ATOM   1039 O  O     . SER A 1 129 ? 18.577  19.579  -4.462  1   17.16  ? 129  SER A O     1 1 
ATOM   1040 C  CB    . SER A 1 129 ? 19.005  22.468  -2.795  1   17.06  ? 129  SER A CB    1 1 
ATOM   1041 O  OG    . SER A 1 129 ? 20.252  22.44   -3.465  1   17.67  ? 129  SER A OG    1 1 
ATOM   1042 N  N     . VAL A 1 130 ? 17.933  19.569  -2.302  1   16.49  ? 130  VAL A N     1 1 
ATOM   1043 C  CA    . VAL A 1 130 ? 18.093  18.102  -2.186  1   16.74  ? 130  VAL A CA    1 1 
ATOM   1044 C  C     . VAL A 1 130 ? 17.024  17.367  -3.004  1   16.89  ? 130  VAL A C     1 1 
ATOM   1045 O  O     . VAL A 1 130 ? 17.292  16.317  -3.581  1   17.77  ? 130  VAL A O     1 1 
ATOM   1046 C  CB    . VAL A 1 130 ? 18.146  17.618  -0.723  1   17.08  ? 130  VAL A CB    1 1 
ATOM   1047 C  CG1   . VAL A 1 130 ? 18.264  16.085  -0.65   1   18.03  ? 130  VAL A CG1   1 1 
ATOM   1048 C  CG2   . VAL A 1 130 ? 19.308  18.29   0.012   1   16.84  ? 130  VAL A CG2   1 1 
ATOM   1049 N  N     . GLY A 1 131 ? 15.839  17.949  -3.105  1   16.67  ? 131  GLY A N     1 1 
ATOM   1050 C  CA    . GLY A 1 131 ? 14.74   17.341  -3.844  1   16.4   ? 131  GLY A CA    1 1 
ATOM   1051 C  C     . GLY A 1 131 ? 15.025  17.162  -5.316  1   16.79  ? 131  GLY A C     1 1 
ATOM   1052 O  O     . GLY A 1 131 ? 14.615  16.159  -5.896  1   17.13  ? 131  GLY A O     1 1 
ATOM   1053 N  N     . ARG A 1 132 ? 15.775  18.091  -5.922  1   17.21  ? 132  ARG A N     1 1 
ATOM   1054 C  CA    . ARG A 1 132 ? 16.072  17.98   -7.349  1   18.26  ? 132  ARG A CA    1 1 
ATOM   1055 C  C     . ARG A 1 132 ? 17.198  16.985  -7.697  1   19.61  ? 132  ARG A C     1 1 
ATOM   1056 O  O     . ARG A 1 132 ? 17.477  16.81   -8.88   1   21.1   ? 132  ARG A O     1 1 
ATOM   1057 C  CB    . ARG A 1 132 ? 16.32   19.357  -7.985  1   18.46  ? 132  ARG A CB    1 1 
ATOM   1058 C  CG    . ARG A 1 132 ? 17.631  20.003  -7.626  1   18.41  ? 132  ARG A CG    1 1 
ATOM   1059 C  CD    . ARG A 1 132 ? 17.675  21.476  -8.025  1   19.98  ? 132  ARG A CD    1 1 
ATOM   1060 N  NE    . ARG A 1 132 ? 17.428  21.719  -9.453  1   20.12  ? 132  ARG A NE    1 1 
ATOM   1061 C  CZ    . ARG A 1 132 ? 18.352  21.627  -10.405 1   21     ? 132  ARG A CZ    1 1 
ATOM   1062 N  NH1   . ARG A 1 132 ? 18.039  21.878  -11.667 1   21.42  ? 132  ARG A NH1   1 1 
ATOM   1063 N  NH2   . ARG A 1 132 ? 19.587  21.255  -10.107 1   18.97  ? 132  ARG A NH2   1 1 
ATOM   1064 N  N     . THR A 1 133 ? 17.77   16.253  -6.711  1   18.73  ? 133  THR A N     1 1 
ATOM   1065 C  CA    . THR A 1 133 ? 18.829  15.292  -6.972  1   18.63  ? 133  THR A CA    1 1 
ATOM   1066 C  C     . THR A 1 133 ? 18.365  13.876  -7.332  1   18.63  ? 133  THR A C     1 1 
ATOM   1067 O  O     . THR A 1 133 ? 19.159  13.072  -7.844  1   18.77  ? 133  THR A O     1 1 
ATOM   1068 C  CB    . THR A 1 133 ? 19.735  15.165  -5.746  1   19.34  ? 133  THR A CB    1 1 
ATOM   1069 O  OG1   . THR A 1 133 ? 18.996  14.605  -4.659  1   19.69  ? 133  THR A OG1   1 1 
ATOM   1070 C  CG2   . THR A 1 133 ? 20.329  16.473  -5.338  1   19.78  ? 133  THR A CG2   1 1 
ATOM   1071 N  N     . GLY A 1 134 ? 17.138  13.546  -6.978  1   18.06  ? 134  GLY A N     1 1 
ATOM   1072 C  CA    . GLY A 1 134 ? 16.65   12.185  -7.153  1   18.05  ? 134  GLY A CA    1 1 
ATOM   1073 C  C     . GLY A 1 134 ? 16.866  11.333  -5.914  1   18.32  ? 134  GLY A C     1 1 
ATOM   1074 O  O     . GLY A 1 134 ? 16.503  10.155  -5.909  1   19.67  ? 134  GLY A O     1 1 
ATOM   1075 N  N     . TYR A 1 135 ? 17.487  11.894  -4.858  1   16.81  ? 135  TYR A N     1 1 
ATOM   1076 C  CA    . TYR A 1 135 ? 17.666  11.175  -3.608  1   16.43  ? 135  TYR A CA    1 1 
ATOM   1077 C  C     . TYR A 1 135 ? 16.506  11.58   -2.695  1   15.47  ? 135  TYR A C     1 1 
ATOM   1078 O  O     . TYR A 1 135 ? 16.26   12.77   -2.482  1   15.08  ? 135  TYR A O     1 1 
ATOM   1079 C  CB    . TYR A 1 135 ? 18.999  11.52   -2.93   1   16.49  ? 135  TYR A CB    1 1 
ATOM   1080 C  CG    . TYR A 1 135 ? 20.196  11.057  -3.717  1   17.77  ? 135  TYR A CG    1 1 
ATOM   1081 C  CD1   . TYR A 1 135 ? 20.38   9.711   -4.011  1   19.29  ? 135  TYR A CD1   1 1 
ATOM   1082 C  CD2   . TYR A 1 135 ? 21.138  11.963  -4.186  1   18.69  ? 135  TYR A CD2   1 1 
ATOM   1083 C  CE1   . TYR A 1 135 ? 21.484  9.277   -4.734  1   20.51  ? 135  TYR A CE1   1 1 
ATOM   1084 C  CE2   . TYR A 1 135 ? 22.255  11.538  -4.898  1   19.7   ? 135  TYR A CE2   1 1 
ATOM   1085 C  CZ    . TYR A 1 135 ? 22.41   10.198  -5.194  1   21.32  ? 135  TYR A CZ    1 1 
ATOM   1086 O  OH    . TYR A 1 135 ? 23.51   9.755   -5.904  1   23.05  ? 135  TYR A OH    1 1 
ATOM   1087 N  N     . PRO A 1 136 ? 15.81   10.598  -2.114  1   14.56  ? 136  PRO A N     1 1 
ATOM   1088 C  CA    . PRO A 1 136 ? 14.668  10.925  -1.251  1   14.97  ? 136  PRO A CA    1 1 
ATOM   1089 C  C     . PRO A 1 136 ? 14.952  11.918  -0.146  1   14.83  ? 136  PRO A C     1 1 
ATOM   1090 O  O     . PRO A 1 136 ? 16.003  11.858  0.473   1   14.57  ? 136  PRO A O     1 1 
ATOM   1091 C  CB    . PRO A 1 136 ? 14.232  9.567   -0.7    1   14.77  ? 136  PRO A CB    1 1 
ATOM   1092 C  CG    . PRO A 1 136 ? 14.705  8.609   -1.709  1   14.87  ? 136  PRO A CG    1 1 
ATOM   1093 C  CD    . PRO A 1 136 ? 15.944  9.146   -2.309  1   13.38  ? 136  PRO A CD    1 1 
ATOM   1094 N  N     . TYR A 1 137 ? 14.009  12.836  0.085   1   14.98  ? 137  TYR A N     1 1 
ATOM   1095 C  CA    . TYR A 1 137 ? 14.154  13.867  1.105   1   15.65  ? 137  TYR A CA    1 1 
ATOM   1096 C  C     . TYR A 1 137 ? 12.978  13.721  2.038   1   16.38  ? 137  TYR A C     1 1 
ATOM   1097 O  O     . TYR A 1 137 ? 11.839  13.909  1.633   1   16.28  ? 137  TYR A O     1 1 
ATOM   1098 C  CB    . TYR A 1 137 ? 14.177  15.265  0.465   1   15.74  ? 137  TYR A CB    1 1 
ATOM   1099 C  CG    . TYR A 1 137 ? 14.355  16.396  1.465   1   15.83  ? 137  TYR A CG    1 1 
ATOM   1100 C  CD1   . TYR A 1 137 ? 15.621  16.803  1.868   1   16.89  ? 137  TYR A CD1   1 1 
ATOM   1101 C  CD2   . TYR A 1 137 ? 13.258  17      2.063   1   16.38  ? 137  TYR A CD2   1 1 
ATOM   1102 C  CE1   . TYR A 1 137 ? 15.786  17.825  2.798   1   18.41  ? 137  TYR A CE1   1 1 
ATOM   1103 C  CE2   . TYR A 1 137 ? 13.41   18      3.011   1   17.74  ? 137  TYR A CE2   1 1 
ATOM   1104 C  CZ    . TYR A 1 137 ? 14.675  18.424  3.364   1   19.54  ? 137  TYR A CZ    1 1 
ATOM   1105 O  OH    . TYR A 1 137 ? 14.816  19.429  4.288   1   21.89  ? 137  TYR A OH    1 1 
ATOM   1106 N  N     . ILE A 1 138 ? 13.25   13.354  3.276   1   17.07  ? 138  ILE A N     1 1 
ATOM   1107 C  CA    . ILE A 1 138 ? 12.219  13.093  4.27    1   18.31  ? 138  ILE A CA    1 1 
ATOM   1108 C  C     . ILE A 1 138 ? 12.287  14.145  5.365   1   19.12  ? 138  ILE A C     1 1 
ATOM   1109 O  O     . ILE A 1 138 ? 13.287  14.239  6.081   1   18.48  ? 138  ILE A O     1 1 
ATOM   1110 C  CB    . ILE A 1 138 ? 12.408  11.678  4.895   1   19.8   ? 138  ILE A CB    1 1 
ATOM   1111 C  CG1   . ILE A 1 138 ? 12.766  10.586  3.839   1   21.18  ? 138  ILE A CG1   1 1 
ATOM   1112 C  CG2   . ILE A 1 138 ? 11.177  11.29   5.73    1   20.67  ? 138  ILE A CG2   1 1 
ATOM   1113 C  CD1   . ILE A 1 138 ? 11.667  10.345  2.829   1   22.05  ? 138  ILE A CD1   1 1 
ATOM   1114 N  N     . TYR A 1 139 ? 11.22   14.92   5.516   1   19.99  ? 139  TYR A N     1 1 
ATOM   1115 C  CA    . TYR A 1 139 ? 11.146  15.948  6.538   1   21.51  ? 139  TYR A CA    1 1 
ATOM   1116 C  C     . TYR A 1 139 ? 10.232  15.429  7.646   1   20.89  ? 139  TYR A C     1 1 
ATOM   1117 O  O     . TYR A 1 139 ? 9.07    15.173  7.397   1   21.43  ? 139  TYR A O     1 1 
ATOM   1118 C  CB    . TYR A 1 139 ? 10.592  17.227  5.903   1   23.07  ? 139  TYR A CB    1 1 
ATOM   1119 C  CG    . TYR A 1 139 ? 10.634  18.442  6.795   1   26.2   ? 139  TYR A CG    1 1 
ATOM   1120 C  CD1   . TYR A 1 139 ? 11.619  18.589  7.759   1   28.41  ? 139  TYR A CD1   1 1 
ATOM   1121 C  CD2   . TYR A 1 139 ? 9.75    19.485  6.613   1   28.77  ? 139  TYR A CD2   1 1 
ATOM   1122 C  CE1   . TYR A 1 139 ? 11.694  19.73   8.547   1   30.21  ? 139  TYR A CE1   1 1 
ATOM   1123 C  CE2   . TYR A 1 139 ? 9.823   20.64   7.382   1   30.55  ? 139  TYR A CE2   1 1 
ATOM   1124 C  CZ    . TYR A 1 139 ? 10.781  20.748  8.366   1   31.95  ? 139  TYR A CZ    1 1 
ATOM   1125 O  OH    . TYR A 1 139 ? 10.819  21.87   9.158   1   34.76  ? 139  TYR A OH    1 1 
ATOM   1126 N  N     . ILE A 1 140 ? 10.761  15.209  8.841   1   20.02  ? 140  ILE A N     1 1 
ATOM   1127 C  CA    . ILE A 1 140 ? 9.999   14.633  9.947   1   19.78  ? 140  ILE A CA    1 1 
ATOM   1128 C  C     . ILE A 1 140 ? 9.821   15.675  11.023  1   20.29  ? 140  ILE A C     1 1 
ATOM   1129 O  O     . ILE A 1 140 ? 10.8    16.234  11.517  1   19.51  ? 140  ILE A O     1 1 
ATOM   1130 C  CB    . ILE A 1 140 ? 10.733  13.398  10.5    1   20.34  ? 140  ILE A CB    1 1 
ATOM   1131 C  CG1   . ILE A 1 140 ? 10.894  12.307  9.413   1   20.95  ? 140  ILE A CG1   1 1 
ATOM   1132 C  CG2   . ILE A 1 140 ? 10.035  12.856  11.746  1   21.42  ? 140  ILE A CG2   1 1 
ATOM   1133 C  CD1   . ILE A 1 140 ? 11.878  11.209  9.784   1   21.86  ? 140  ILE A CD1   1 1 
ATOM   1134 N  N     . VAL A 1 141 ? 8.565   15.95   11.384  1   20.62  ? 141  VAL A N     1 1 
ATOM   1135 C  CA    . VAL A 1 141 ? 8.273   16.963  12.37   1   21.63  ? 141  VAL A CA    1 1 
ATOM   1136 C  C     . VAL A 1 141 ? 7.239   16.522  13.417  1   22.47  ? 141  VAL A C     1 1 
ATOM   1137 O  O     . VAL A 1 141 ? 6.343   15.735  13.115  1   21.64  ? 141  VAL A O     1 1 
ATOM   1138 C  CB    . VAL A 1 141 ? 7.857   18.247  11.636  1   22.49  ? 141  VAL A CB    1 1 
ATOM   1139 C  CG1   . VAL A 1 141 ? 6.508   18.091  10.952  1   21.97  ? 141  VAL A CG1   1 1 
ATOM   1140 C  CG2   . VAL A 1 141 ? 7.834   19.41   12.584  1   24.31  ? 141  VAL A CG2   1 1 
ATOM   1141 N  N     . ASP A 1 142 ? 7.375   17.011  14.658  1   23.23  ? 142  ASP A N     1 1 
ATOM   1142 C  CA    . ASP A 1 142 ? 6.42    16.66   15.711  1   24.04  ? 142  ASP A CA    1 1 
ATOM   1143 C  C     . ASP A 1 142 ? 5.217   17.571  15.627  1   23.35  ? 142  ASP A C     1 1 
ATOM   1144 O  O     . ASP A 1 142 ? 5.363   18.783  15.471  1   22.83  ? 142  ASP A O     1 1 
ATOM   1145 C  CB    . ASP A 1 142 ? 7.052   16.773  17.106  1   27.27  ? 142  ASP A CB    1 1 
ATOM   1146 C  CG    . ASP A 1 142 ? 7.838   15.55   17.533  1   34.93  ? 142  ASP A CG    1 1 
ATOM   1147 O  OD1   . ASP A 1 142 ? 8.148   14.71   16.663  1   35.62  ? 142  ASP A OD1   1 1 
ATOM   1148 O  OD2   . ASP A 1 142 ? 8.149   15.436  18.744  1   38.9   ? 142  ASP A OD2   1 1 
ATOM   1149 N  N     . PHE A 1 143 ? 4.027   16.982  15.693  1   23.06  ? 143  PHE A N     1 1 
ATOM   1150 C  CA    . PHE A 1 143 ? 2.78    17.729  15.676  1   23.46  ? 143  PHE A CA    1 1 
ATOM   1151 C  C     . PHE A 1 143 ? 2.071   17.361  16.97   1   23.36  ? 143  PHE A C     1 1 
ATOM   1152 O  O     . PHE A 1 143 ? 1.699   16.197  17.121  1   23.9   ? 143  PHE A O     1 1 
ATOM   1153 C  CB    . PHE A 1 143 ? 1.927   17.296  14.463  1   23.14  ? 143  PHE A CB    1 1 
ATOM   1154 C  CG    . PHE A 1 143 ? 0.641   18.067  14.317  1   23.1   ? 143  PHE A CG    1 1 
ATOM   1155 C  CD1   . PHE A 1 143 ? -0.507  17.666  14.98   1   23.18  ? 143  PHE A CD1   1 1 
ATOM   1156 C  CD2   . PHE A 1 143 ? 0.577   19.191  13.507  1   24.07  ? 143  PHE A CD2   1 1 
ATOM   1157 C  CE1   . PHE A 1 143 ? -1.684  18.398  14.867  1   24.02  ? 143  PHE A CE1   1 1 
ATOM   1158 C  CE2   . PHE A 1 143 ? -0.613  19.919  13.383  1   24.37  ? 143  PHE A CE2   1 1 
ATOM   1159 C  CZ    . PHE A 1 143 ? -1.73   19.515  14.061  1   23.98  ? 143  PHE A CZ    1 1 
ATOM   1160 N  N     . VAL A 1 144 ? 1.892   18.287  17.918  1   22.57  ? 144  VAL A N     1 1 
ATOM   1161 C  CA    . VAL A 1 144 ? 2.321   19.683  17.91   1   22.74  ? 144  VAL A CA    1 1 
ATOM   1162 C  C     . VAL A 1 144 ? 3.258   19.891  19.122  1   23.51  ? 144  VAL A C     1 1 
ATOM   1163 O  O     . VAL A 1 144 ? 3.295   19.074  20.042  1   23.21  ? 144  VAL A O     1 1 
ATOM   1164 C  CB    . VAL A 1 144 ? 1.095   20.668  18.057  1   23.05  ? 144  VAL A CB    1 1 
ATOM   1165 C  CG1   . VAL A 1 144 ? 0.309   20.837  16.763  1   23.72  ? 144  VAL A CG1   1 1 
ATOM   1166 C  CG2   . VAL A 1 144 ? 0.175   20.252  19.208  1   22.74  ? 144  VAL A CG2   1 1 
ATOM   1167 N  N     . LYS A 1 145 ? 3.969   21.028  19.145  1   24.57  ? 145  LYS A N     1 1 
ATOM   1168 C  CA    . LYS A 1 145 ? 4.784   21.445  20.277  1   26.14  ? 145  LYS A CA    1 1 
ATOM   1169 C  C     . LYS A 1 145 ? 4.429   22.919  20.501  1   27.56  ? 145  LYS A C     1 1 
ATOM   1170 O  O     . LYS A 1 145 ? 4.38    23.69   19.536  1   28.72  ? 145  LYS A O     1 1 
ATOM   1171 C  CB    . LYS A 1 145 ? 6.284   21.257  19.984  1   28.64  ? 145  LYS A CB    1 1 
ATOM   1172 C  CG    . LYS A 1 145 ? 7.157   21.534  21.208  1   33.54  ? 145  LYS A CG    1 1 
ATOM   1173 C  CD    . LYS A 1 145 ? 8.661   21.372  20.933  1   38.68  ? 145  LYS A CD    1 1 
ATOM   1174 C  CE    . LYS A 1 145 ? 9.246   22.449  20.03   1   42.74  ? 145  LYS A CE    1 1 
ATOM   1175 N  NZ    . LYS A 1 145 ? 8.993   23.846  20.51   1   44.29  ? 145  LYS A NZ    1 1 
ATOM   1176 N  N     . TYR A 1 146 ? 4.094   23.304  21.735  1   27.55  ? 146  TYR A N     1 1 
ATOM   1177 C  CA    . TYR A 1 146 ? 3.709   24.702  21.993  1   28.15  ? 146  TYR A CA    1 1 
ATOM   1178 C  C     . TYR A 1 146 ? 4.905   25.609  22.126  1   29.78  ? 146  TYR A C     1 1 
ATOM   1179 O  O     . TYR A 1 146 ? 5.853   25.271  22.831  1   29.44  ? 146  TYR A O     1 1 
ATOM   1180 C  CB    . TYR A 1 146 ? 2.871   24.816  23.263  1   27.74  ? 146  TYR A CB    1 1 
ATOM   1181 C  CG    . TYR A 1 146 ? 1.468   24.273  23.104  1   28.28  ? 146  TYR A CG    1 1 
ATOM   1182 C  CD1   . TYR A 1 146 ? 1.185   22.939  23.356  1   29.06  ? 146  TYR A CD1   1 1 
ATOM   1183 C  CD2   . TYR A 1 146 ? 0.432   25.084  22.659  1   28.71  ? 146  TYR A CD2   1 1 
ATOM   1184 C  CE1   . TYR A 1 146 ? -0.107  22.438  23.23   1   29.96  ? 146  TYR A CE1   1 1 
ATOM   1185 C  CE2   . TYR A 1 146 ? -0.861  24.592  22.524  1   29.2   ? 146  TYR A CE2   1 1 
ATOM   1186 C  CZ    . TYR A 1 146 ? -1.124  23.263  22.796  1   30.02  ? 146  TYR A CZ    1 1 
ATOM   1187 O  OH    . TYR A 1 146 ? -2.389  22.741  22.653  1   31.15  ? 146  TYR A OH    1 1 
ATOM   1188 N  N     . GLU A 1 147 ? 4.857   26.778  21.478  1   31.09  ? 147  GLU A N     1 1 
ATOM   1189 C  CA    . GLU A 1 147 ? 5.879   27.805  21.672  1   32.37  ? 147  GLU A CA    1 1 
ATOM   1190 C  C     . GLU A 1 147 ? 5.603   28.395  23.064  1   34.06  ? 147  GLU A C     1 1 
ATOM   1191 O  O     . GLU A 1 147 ? 4.447   28.466  23.5    1   34.12  ? 147  GLU A O     1 1 
ATOM   1192 C  CB    . GLU A 1 147 ? 5.764   28.923  20.632  1   32.89  ? 147  GLU A CB    1 1 
ATOM   1193 C  CG    . GLU A 1 147 ? 6.009   28.445  19.223  1   35.67  ? 147  GLU A CG    1 1 
ATOM   1194 C  CD    . GLU A 1 147 ? 5.766   29.519  18.187  1   40.85  ? 147  GLU A CD    1 1 
ATOM   1195 O  OE1   . GLU A 1 147 ? 6.754   30.154  17.751  1   43.32  ? 147  GLU A OE1   1 1 
ATOM   1196 O  OE2   . GLU A 1 147 ? 4.591   29.735  17.813  1   40.9   ? 147  GLU A OE2   1 1 
ATOM   1197 N  N     . LEU A 1 148 ? 6.661   28.777  23.768  1   35.01  ? 148  LEU A N     1 1 
ATOM   1198 C  CA    . LEU A 1 148 ? 6.524   29.275  25.127  1   35.9   ? 148  LEU A CA    1 1 
ATOM   1199 C  C     . LEU A 1 148 ? 7.039   30.679  25.311  1   36.64  ? 148  LEU A C     1 1 
ATOM   1200 O  O     . LEU A 1 148 ? 7.888   31.158  24.557  1   36.91  ? 148  LEU A O     1 1 
ATOM   1201 C  CB    . LEU A 1 148 ? 7.33    28.367  26.073  1   35.82  ? 148  LEU A CB    1 1 
ATOM   1202 C  CG    . LEU A 1 148 ? 7.053   26.894  26.027  1   35.67  ? 148  LEU A CG    1 1 
ATOM   1203 C  CD1   . LEU A 1 148 ? 8.013   26.153  26.918  1   35.52  ? 148  LEU A CD1   1 1 
ATOM   1204 C  CD2   . LEU A 1 148 ? 5.63    26.614  26.421  1   35.92  ? 148  LEU A CD2   1 1 
ATOM   1205 N  N     . ASN A 1 149 ? 6.536   31.331  26.355  1   36.84  ? 149  ASN A N     1 1 
ATOM   1206 C  CA    . ASN A 1 149 ? 7.067   32.605  26.795  1   37.05  ? 149  ASN A CA    1 1 
ATOM   1207 C  C     . ASN A 1 149 ? 8.14    32.095  27.755  1   38     ? 149  ASN A C     1 1 
ATOM   1208 O  O     . ASN A 1 149 ? 7.813   31.45   28.752  1   38.16  ? 149  ASN A O     1 1 
ATOM   1209 C  CB    . ASN A 1 149 ? 6.01    33.401  27.555  1   36.7   ? 149  ASN A CB    1 1 
ATOM   1210 C  CG    . ASN A 1 149 ? 4.799   33.732  26.725  1   37.83  ? 149  ASN A CG    1 1 
ATOM   1211 O  OD1   . ASN A 1 149 ? 3.703   33.23   26.973  1   37.81  ? 149  ASN A OD1   1 1 
ATOM   1212 N  ND2   . ASN A 1 149 ? 4.965   34.59   25.73   1   37.95  ? 149  ASN A ND2   1 1 
ATOM   1213 N  N     . ASN A 1 150 ? 9.411   32.28   27.411  1   38.53  ? 150  ASN A N     1 1 
ATOM   1214 C  CA    . ASN A 1 150 ? 10.507  31.745  28.214  1   39.59  ? 150  ASN A CA    1 1 
ATOM   1215 C  C     . ASN A 1 150 ? 10.557  32.308  29.648  1   41.32  ? 150  ASN A C     1 1 
ATOM   1216 O  O     . ASN A 1 150 ? 11.036  31.63   30.549  1   41.96  ? 150  ASN A O     1 1 
ATOM   1217 C  CB    . ASN A 1 150 ? 11.825  31.894  27.479  1   39.66  ? 150  ASN A CB    1 1 
ATOM   1218 C  CG    . ASN A 1 150 ? 11.848  31.071  26.207  1   41.52  ? 150  ASN A CG    1 1 
ATOM   1219 O  OD1   . ASN A 1 150 ? 11.492  29.878  26.197  1   41.64  ? 150  ASN A OD1   1 1 
ATOM   1220 N  ND2   . ASN A 1 150 ? 12.237  31.694  25.094  1   42.31  ? 150  ASN A ND2   1 1 
ATOM   1221 N  N     . SER A 1 151 ? 9.984   33.483  29.872  1   42.1   ? 151  SER A N     1 1 
ATOM   1222 C  CA    . SER A 1 151 ? 9.912   34.11   31.182  1   43.19  ? 151  SER A CA    1 1 
ATOM   1223 C  C     . SER A 1 151 ? 9.169   33.213  32.201  1   43.08  ? 151  SER A C     1 1 
ATOM   1224 O  O     . SER A 1 151 ? 9.665   33.028  33.308  1   44.05  ? 151  SER A O     1 1 
ATOM   1225 C  CB    . SER A 1 151 ? 9.204   35.462  31.068  1   46.12  ? 151  SER A CB    1 1 
ATOM   1226 O  OG    . SER A 1 151 ? 9.705   36.241  29.988  1   49.53  ? 151  SER A OG    1 1 
ATOM   1227 N  N     . ASP A 1 152 ? 8.014   32.636  31.829  1   41.7   ? 152  ASP A N     1 1 
ATOM   1228 C  CA    . ASP A 1 152 ? 7.251   31.79   32.761  1   41.26  ? 152  ASP A CA    1 1 
ATOM   1229 C  C     . ASP A 1 152 ? 6.871   30.379  32.242  1   39.56  ? 152  ASP A C     1 1 
ATOM   1230 O  O     . ASP A 1 152 ? 6.073   29.692  32.882  1   39.68  ? 152  ASP A O     1 1 
ATOM   1231 C  CB    . ASP A 1 152 ? 5.979   32.516  33.243  1   43.85  ? 152  ASP A CB    1 1 
ATOM   1232 C  CG    . ASP A 1 152 ? 5.021   32.951  32.139  1   49.89  ? 152  ASP A CG    1 1 
ATOM   1233 O  OD1   . ASP A 1 152 ? 5.363   32.775  30.945  1   50.66  ? 152  ASP A OD1   1 1 
ATOM   1234 O  OD2   . ASP A 1 152 ? 3.936   33.49   32.47   1   52.72  ? 152  ASP A OD2   1 1 
ATOM   1235 N  N     . ARG A 1 153 ? 7.408   29.963  31.092  1   37.92  ? 153  ARG A N     1 1 
ATOM   1236 C  CA    . ARG A 1 153 ? 7.095   28.671  30.463  1   36.98  ? 153  ARG A CA    1 1 
ATOM   1237 C  C     . ARG A 1 153 ? 5.601   28.489  30.143  1   36.2   ? 153  ARG A C     1 1 
ATOM   1238 O  O     . ARG A 1 153 ? 5.119   27.362  30.052  1   36.49  ? 153  ARG A O     1 1 
ATOM   1239 C  CB    . ARG A 1 153 ? 7.632   27.48   31.272  1   37.34  ? 153  ARG A CB    1 1 
ATOM   1240 C  CG    . ARG A 1 153 ? 9.124   27.547  31.5    1   39.59  ? 153  ARG A CG    1 1 
ATOM   1241 C  CD    . ARG A 1 153 ? 9.736   26.172  31.54   1   41.31  ? 153  ARG A CD    1 1 
ATOM   1242 N  NE    . ARG A 1 153 ? 10.42   25.916  30.282  1   42.55  ? 153  ARG A NE    1 1 
ATOM   1243 C  CZ    . ARG A 1 153 ? 10.22   24.858  29.511  1   42.29  ? 153  ARG A CZ    1 1 
ATOM   1244 N  NH1   . ARG A 1 153 ? 9.366   23.91   29.877  1   40.7   ? 153  ARG A NH1   1 1 
ATOM   1245 N  NH2   . ARG A 1 153 ? 10.882  24.73   28.373  1   42.04  ? 153  ARG A NH2   1 1 
ATOM   1246 N  N     . SER A 1 154 ? 4.867   29.597  29.994  1   35.23  ? 154  SER A N     1 1 
ATOM   1247 C  CA    . SER A 1 154 ? 3.447   29.534  29.663  1   34.35  ? 154  SER A CA    1 1 
ATOM   1248 C  C     . SER A 1 154 ? 3.321   29.338  28.154  1   33.62  ? 154  SER A C     1 1 
ATOM   1249 O  O     . SER A 1 154 ? 4.112   29.893  27.378  1   33.71  ? 154  SER A O     1 1 
ATOM   1250 C  CB    . SER A 1 154 ? 2.726   30.811  30.093  1   34.38  ? 154  SER A CB    1 1 
ATOM   1251 O  OG    . SER A 1 154 ? 3.19    31.926  29.347  1   35.35  ? 154  SER A OG    1 1 
ATOM   1252 N  N     . ARG A 1 155 ? 2.336   28.54   27.741  1   32.75  ? 155  ARG A N     1 1 
ATOM   1253 C  CA    . ARG A 1 155 ? 2.143   28.264  26.331  1   32.21  ? 155  ARG A CA    1 1 
ATOM   1254 C  C     . ARG A 1 155 ? 1.452   29.373  25.573  1   31.36  ? 155  ARG A C     1 1 
ATOM   1255 O  O     . ARG A 1 155 ? 0.486   29.967  26.042  1   31.99  ? 155  ARG A O     1 1 
ATOM   1256 C  CB    . ARG A 1 155 ? 1.389   26.948  26.127  1   33.24  ? 155  ARG A CB    1 1 
ATOM   1257 C  CG    . ARG A 1 155 ? 2.088   25.754  26.737  1   35.7   ? 155  ARG A CG    1 1 
ATOM   1258 C  CD    . ARG A 1 155 ? 1.156   24.581  26.809  1   39.24  ? 155  ARG A CD    1 1 
ATOM   1259 N  NE    . ARG A 1 155 ? 1.848   23.38   27.268  1   42.15  ? 155  ARG A NE    1 1 
ATOM   1260 C  CZ    . ARG A 1 155 ? 1.885   22.969  28.532  1   43.7   ? 155  ARG A CZ    1 1 
ATOM   1261 N  NH1   . ARG A 1 155 ? 1.274   23.665  29.484  1   43.21  ? 155  ARG A NH1   1 1 
ATOM   1262 N  NH2   . ARG A 1 155 ? 2.535   21.858  28.855  1   42.77  ? 155  ARG A NH2   1 1 
ATOM   1263 N  N     . LYS A 1 156 ? 1.959   29.63   24.384  1   29.78  ? 156  LYS A N     1 1 
ATOM   1264 C  CA    A LYS A 1 156 ? 1.401   30.581  23.438  0.5 29.58  ? 156  LYS A CA    1 1 
ATOM   1265 C  CA    B LYS A 1 156 ? 1.38    30.584  23.45   0.5 29.29  ? 156  LYS A CA    1 1 
ATOM   1266 C  C     . LYS A 1 156 ? 0.401   29.805  22.557  1   29.32  ? 156  LYS A C     1 1 
ATOM   1267 O  O     . LYS A 1 156 ? 0.528   28.584  22.417  1   29.13  ? 156  LYS A O     1 1 
ATOM   1268 C  CB    A LYS A 1 156 ? 2.543   31.149  22.574  0.5 31.41  ? 156  LYS A CB    1 1 
ATOM   1269 C  CB    B LYS A 1 156 ? 2.475   31.2    22.565  0.5 30.24  ? 156  LYS A CB    1 1 
ATOM   1270 C  CG    A LYS A 1 156 ? 2.091   32.001  21.396  0.5 35.07  ? 156  LYS A CG    1 1 
ATOM   1271 C  CG    B LYS A 1 156 ? 3.528   32.024  23.293  0.5 32.15  ? 156  LYS A CG    1 1 
ATOM   1272 C  CD    A LYS A 1 156 ? 2.793   31.613  20.111  0.5 38.15  ? 156  LYS A CD    1 1 
ATOM   1273 C  CD    B LYS A 1 156 ? 4.335   32.813  22.281  0.5 35.34  ? 156  LYS A CD    1 1 
ATOM   1274 C  CE    A LYS A 1 156 ? 2.271   32.45   18.979  0.5 40.51  ? 156  LYS A CE    1 1 
ATOM   1275 C  CE    B LYS A 1 156 ? 5.74    33.081  22.744  0.5 39.53  ? 156  LYS A CE    1 1 
ATOM   1276 N  NZ    A LYS A 1 156 ? 0.789   32.383  18.9    0.5 41.59  ? 156  LYS A NZ    1 1 
ATOM   1277 N  NZ    B LYS A 1 156 ? 6.452   34.027  21.842  0.5 42.17  ? 156  LYS A NZ    1 1 
ATOM   1278 N  N     . ASN A 1 157 ? -0.587  30.49   21.949  1   28.86  ? 157  ASN A N     1 1 
ATOM   1279 C  CA    . ASN A 1 157 ? -1.537  29.808  21.073  1   28.74  ? 157  ASN A CA    1 1 
ATOM   1280 C  C     . ASN A 1 157 ? -0.845  29.177  19.847  1   27.48  ? 157  ASN A C     1 1 
ATOM   1281 O  O     . ASN A 1 157 ? 0.172   29.678  19.388  1   27.62  ? 157  ASN A O     1 1 
ATOM   1282 C  CB    . ASN A 1 157 ? -2.707  30.712  20.704  1   31.15  ? 157  ASN A CB    1 1 
ATOM   1283 C  CG    . ASN A 1 157 ? -3.746  30.673  21.803  1   36.54  ? 157  ASN A CG    1 1 
ATOM   1284 O  OD1   . ASN A 1 157 ? -4.463  29.661  21.982  1   39.68  ? 157  ASN A OD1   1 1 
ATOM   1285 N  ND2   . ASN A 1 157 ? -3.814  31.727  22.602  1   36.62  ? 157  ASN A ND2   1 1 
ATOM   1286 N  N     . LEU A 1 158 ? -1.338  28.02   19.386  1   26.43  ? 158  LEU A N     1 1 
ATOM   1287 C  CA    . LEU A 1 158 ? -0.728  27.317  18.266  1   25.08  ? 158  LEU A CA    1 1 
ATOM   1288 C  C     . LEU A 1 158 ? -0.827  28.154  17.008  1   24.21  ? 158  LEU A C     1 1 
ATOM   1289 O  O     . LEU A 1 158 ? -1.872  28.695  16.719  1   24.08  ? 158  LEU A O     1 1 
ATOM   1290 C  CB    . LEU A 1 158 ? -1.431  25.982  17.98   1   24.37  ? 158  LEU A CB    1 1 
ATOM   1291 C  CG    . LEU A 1 158 ? -1.255  24.836  18.956  1   24.64  ? 158  LEU A CG    1 1 
ATOM   1292 C  CD1   . LEU A 1 158 ? -2.253  23.712  18.635  1   23.69  ? 158  LEU A CD1   1 1 
ATOM   1293 C  CD2   . LEU A 1 158 ? 0.218   24.342  18.995  1   24.49  ? 158  LEU A CD2   1 1 
ATOM   1294 N  N     . ARG A 1 159 ? 0.236   28.166  16.233  1   23.72  ? 159  ARG A N     1 1 
ATOM   1295 C  CA    . ARG A 1 159 ? 0.306   28.781  14.931  1   23.88  ? 159  ARG A CA    1 1 
ATOM   1296 C  C     . ARG A 1 159 ? 0.611   27.644  13.935  1   22.43  ? 159  ARG A C     1 1 
ATOM   1297 O  O     . ARG A 1 159 ? 1.4     26.739  14.224  1   22.82  ? 159  ARG A O     1 1 
ATOM   1298 C  CB    . ARG A 1 159 ? 1.46    29.792  14.893  1   26.71  ? 159  ARG A CB    1 1 
ATOM   1299 C  CG    . ARG A 1 159 ? 1.25    31.085  15.667  1   32.59  ? 159  ARG A CG    1 1 
ATOM   1300 C  CD    . ARG A 1 159 ? 2.399   32.076  15.353  1   38.85  ? 159  ARG A CD    1 1 
ATOM   1301 N  NE    . ARG A 1 159 ? 3.723   31.525  15.689  1   44.57  ? 159  ARG A NE    1 1 
ATOM   1302 C  CZ    . ARG A 1 159 ? 4.815   31.643  14.931  1   48.39  ? 159  ARG A CZ    1 1 
ATOM   1303 N  NH1   . ARG A 1 159 ? 4.764   32.292  13.774  1   49.72  ? 159  ARG A NH1   1 1 
ATOM   1304 N  NH2   . ARG A 1 159 ? 5.964   31.118  15.328  1   47.71  ? 159  ARG A NH2   1 1 
ATOM   1305 N  N     . PHE A 1 160 ? -0.002  27.693  12.773  1   21.27  ? 160  PHE A N     1 1 
ATOM   1306 C  CA    . PHE A 1 160 ? 0.226   26.695  11.741  1   21.24  ? 160  PHE A CA    1 1 
ATOM   1307 C  C     . PHE A 1 160 ? 0.825   27.353  10.521  1   20.02  ? 160  PHE A C     1 1 
ATOM   1308 O  O     . PHE A 1 160 ? 0.522   28.51   10.22   1   20.42  ? 160  PHE A O     1 1 
ATOM   1309 C  CB    . PHE A 1 160 ? -1.081  25.972  11.368  1   21.47  ? 160  PHE A CB    1 1 
ATOM   1310 C  CG    . PHE A 1 160 ? -1.751  25.285  12.532  1   22.73  ? 160  PHE A CG    1 1 
ATOM   1311 C  CD1   . PHE A 1 160 ? -1.236  24.114  13.057  1   23.47  ? 160  PHE A CD1   1 1 
ATOM   1312 C  CD2   . PHE A 1 160 ? -2.847  25.856  13.155  1   23.57  ? 160  PHE A CD2   1 1 
ATOM   1313 C  CE1   . PHE A 1 160 ? -1.832  23.507  14.157  1   24.3   ? 160  PHE A CE1   1 1 
ATOM   1314 C  CE2   . PHE A 1 160 ? -3.442  25.242  14.25   1   24.25  ? 160  PHE A CE2   1 1 
ATOM   1315 C  CZ    . PHE A 1 160 ? -2.944  24.06   14.734  1   23.6   ? 160  PHE A CZ    1 1 
ATOM   1316 N  N     . PRO A 1 161 ? 1.669   26.62   9.784   1   18.5   ? 161  PRO A N     1 1 
ATOM   1317 C  CA    . PRO A 1 161 ? 2.221   27.195  8.549   1   17.75  ? 161  PRO A CA    1 1 
ATOM   1318 C  C     . PRO A 1 161 ? 1.128   27.396  7.505   1   16.67  ? 161  PRO A C     1 1 
ATOM   1319 O  O     . PRO A 1 161 ? 0.081   26.749  7.572   1   17.38  ? 161  PRO A O     1 1 
ATOM   1320 C  CB    . PRO A 1 161 ? 3.207   26.106  8.075   1   18.24  ? 161  PRO A CB    1 1 
ATOM   1321 C  CG    . PRO A 1 161 ? 2.618   24.811  8.646   1   18.79  ? 161  PRO A CG    1 1 
ATOM   1322 C  CD    . PRO A 1 161 ? 2.129   25.23   10      1   17.58  ? 161  PRO A CD    1 1 
ATOM   1323 N  N     . ASN A 1 162 ? 1.378   28.226  6.489   1   15.19  ? 162  ASN A N     1 1 
ATOM   1324 C  CA    . ASN A 1 162 ? 0.444   28.388  5.377   1   15.19  ? 162  ASN A CA    1 1 
ATOM   1325 C  C     . ASN A 1 162 ? 0.278   27.018  4.676   1   16.05  ? 162  ASN A C     1 1 
ATOM   1326 O  O     . ASN A 1 162 ? 1.268   26.313  4.506   1   16.19  ? 162  ASN A O     1 1 
ATOM   1327 C  CB    . ASN A 1 162 ? 0.994   29.398  4.384   1   15.07  ? 162  ASN A CB    1 1 
ATOM   1328 C  CG    . ASN A 1 162 ? 0.028   29.782  3.296   1   15.68  ? 162  ASN A CG    1 1 
ATOM   1329 O  OD1   . ASN A 1 162 ? -0.378  28.955  2.466   1   15.55  ? 162  ASN A OD1   1 1 
ATOM   1330 N  ND2   . ASN A 1 162 ? -0.334  31.066  3.253   1   16.21  ? 162  ASN A ND2   1 1 
ATOM   1331 N  N     . PRO A 1 163 ? -0.95   26.583  4.368   1   16.8   ? 163  PRO A N     1 1 
ATOM   1332 C  CA    . PRO A 1 163 ? -1.131  25.257  3.722   1   16.79  ? 163  PRO A CA    1 1 
ATOM   1333 C  C     . PRO A 1 163 ? -0.221  25.001  2.507   1   17.54  ? 163  PRO A C     1 1 
ATOM   1334 O  O     . PRO A 1 163 ? 0.062   23.845  2.187   1   18.41  ? 163  PRO A O     1 1 
ATOM   1335 C  CB    . PRO A 1 163 ? -2.6    25.283  3.296   1   17.4   ? 163  PRO A CB    1 1 
ATOM   1336 C  CG    . PRO A 1 163 ? -3.254  26.249  4.229   1   17.38  ? 163  PRO A CG    1 1 
ATOM   1337 C  CD    . PRO A 1 163 ? -2.24   27.288  4.56    1   15.98  ? 163  PRO A CD    1 1 
ATOM   1338 N  N     . ALA A 1 164 ? 0.246   26.078  1.836   1   16.81  ? 164  ALA A N     1 1 
ATOM   1339 C  CA    . ALA A 1 164 ? 1.146   25.984  0.679   1   17.1   ? 164  ALA A CA    1 1 
ATOM   1340 C  C     . ALA A 1 164 ? 2.513   25.364  1.043   1   16.75  ? 164  ALA A C     1 1 
ATOM   1341 O  O     . ALA A 1 164 ? 3.137   24.735  0.182   1   16.16  ? 164  ALA A O     1 1 
ATOM   1342 C  CB    . ALA A 1 164 ? 1.365   27.373  0.07    1   16.84  ? 164  ALA A CB    1 1 
ATOM   1343 N  N     . ILE A 1 165 ? 2.986   25.558  2.29    1   16.27  ? 165  ILE A N     1 1 
ATOM   1344 C  CA    . ILE A 1 165 ? 4.275   24.997  2.691   1   17.16  ? 165  ILE A CA    1 1 
ATOM   1345 C  C     . ILE A 1 165 ? 4.223   23.459  2.672   1   16.47  ? 165  ILE A C     1 1 
ATOM   1346 O  O     . ILE A 1 165 ? 4.935   22.848  1.841   1   15.86  ? 165  ILE A O     1 1 
ATOM   1347 C  CB    . ILE A 1 165 ? 4.888   25.569  4.003   1   19.44  ? 165  ILE A CB    1 1 
ATOM   1348 C  CG1   . ILE A 1 165 ? 4.648   27.086  4.184   1   21.99  ? 165  ILE A CG1   1 1 
ATOM   1349 C  CG2   . ILE A 1 165 ? 6.351   25.238  4.065   1   20.58  ? 165  ILE A CG2   1 1 
ATOM   1350 C  CD1   . ILE A 1 165 ? 4.98    27.957  3.043   1   23.5   ? 165  ILE A CD1   1 1 
ATOM   1351 N  N     . PRO A 1 166 ? 3.375   22.784  3.488   1   16.07  ? 166  PRO A N     1 1 
ATOM   1352 C  CA    . PRO A 1 166 ? 3.303   21.301  3.383   1   16.3   ? 166  PRO A CA    1 1 
ATOM   1353 C  C     . PRO A 1 166 ? 2.966   20.851  1.957   1   16.61  ? 166  PRO A C     1 1 
ATOM   1354 O  O     . PRO A 1 166 ? 3.471   19.82   1.523   1   16.36  ? 166  PRO A O     1 1 
ATOM   1355 C  CB    . PRO A 1 166 ? 2.158   20.927  4.342   1   16.59  ? 166  PRO A CB    1 1 
ATOM   1356 C  CG    . PRO A 1 166 ? 2.165   22.011  5.355   1   17.36  ? 166  PRO A CG    1 1 
ATOM   1357 C  CD    . PRO A 1 166 ? 2.475   23.279  4.548   1   15.88  ? 166  PRO A CD    1 1 
ATOM   1358 N  N     . TYR A 1 167 ? 2.173   21.667  1.198   1   16.39  ? 167  TYR A N     1 1 
ATOM   1359 C  CA    . TYR A 1 167 ? 1.824   21.272  -0.171  1   17.18  ? 167  TYR A CA    1 1 
ATOM   1360 C  C     . TYR A 1 167 ? 3.014   21.245  -1.099  1   17.58  ? 167  TYR A C     1 1 
ATOM   1361 O  O     . TYR A 1 167 ? 3.038   20.408  -2.024  1   17.71  ? 167  TYR A O     1 1 
ATOM   1362 C  CB    . TYR A 1 167 ? 0.703   22.125  -0.801  1   17.38  ? 167  TYR A CB    1 1 
ATOM   1363 C  CG    . TYR A 1 167 ? 0.234   21.506  -2.099  1   18.31  ? 167  TYR A CG    1 1 
ATOM   1364 C  CD1   . TYR A 1 167 ? -0.608  20.401  -2.1    1   19.76  ? 167  TYR A CD1   1 1 
ATOM   1365 C  CD2   . TYR A 1 167 ? 0.724   21.949  -3.32   1   19.27  ? 167  TYR A CD2   1 1 
ATOM   1366 C  CE1   . TYR A 1 167 ? -0.96   19.761  -3.282  1   21.15  ? 167  TYR A CE1   1 1 
ATOM   1367 C  CE2   . TYR A 1 167 ? 0.404   21.3    -4.504  1   20.58  ? 167  TYR A CE2   1 1 
ATOM   1368 C  CZ    . TYR A 1 167 ? -0.45   20.216  -4.483  1   22.5   ? 167  TYR A CZ    1 1 
ATOM   1369 O  OH    . TYR A 1 167 ? -0.765  19.583  -5.656  1   25.1   ? 167  TYR A OH    1 1 
ATOM   1370 N  N     . SER A 1 168 ? 3.997   22.155  -0.858  1   16.16  ? 168  SER A N     1 1 
ATOM   1371 C  CA    . SER A 1 168 ? 5.187   22.334  -1.689  1   15.5   ? 168  SER A CA    1 1 
ATOM   1372 C  C     . SER A 1 168 ? 6.014   21.079  -1.824  1   14.83  ? 168  SER A C     1 1 
ATOM   1373 O  O     . SER A 1 168 ? 6.652   20.888  -2.856  1   14.01  ? 168  SER A O     1 1 
ATOM   1374 C  CB    . SER A 1 168 ? 6.039   23.519  -1.217  1   14.96  ? 168  SER A CB    1 1 
ATOM   1375 O  OG    . SER A 1 168 ? 6.637   23.248  0.039   1   16.3   ? 168  SER A OG    1 1 
ATOM   1376 N  N     . TYR A 1 169 ? 6.007   20.226  -0.792  1   15.01  ? 169  TYR A N     1 1 
ATOM   1377 C  CA    . TYR A 1 169 ? 6.718   18.963  -0.799  1   15.62  ? 169  TYR A CA    1 1 
ATOM   1378 C  C     . TYR A 1 169 ? 6.042   18.035  -1.838  1   14.55  ? 169  TYR A C     1 1 
ATOM   1379 O  O     . TYR A 1 169 ? 6.73    17.441  -2.673  1   13.47  ? 169  TYR A O     1 1 
ATOM   1380 C  CB    . TYR A 1 169 ? 6.702   18.349  0.609   1   17.08  ? 169  TYR A CB    1 1 
ATOM   1381 C  CG    . TYR A 1 169 ? 7.599   19.1    1.562   1   20.27  ? 169  TYR A CG    1 1 
ATOM   1382 C  CD1   . TYR A 1 169 ? 7.225   20.333  2.074   1   22.29  ? 169  TYR A CD1   1 1 
ATOM   1383 C  CD2   . TYR A 1 169 ? 8.841   18.595  1.926   1   22.56  ? 169  TYR A CD2   1 1 
ATOM   1384 C  CE1   . TYR A 1 169 ? 8.066   21.057  2.907   1   24.28  ? 169  TYR A CE1   1 1 
ATOM   1385 C  CE2   . TYR A 1 169 ? 9.693   19.309  2.767   1   24.15  ? 169  TYR A CE2   1 1 
ATOM   1386 C  CZ    . TYR A 1 169 ? 9.298   20.539  3.259   1   26.12  ? 169  TYR A CZ    1 1 
ATOM   1387 O  OH    . TYR A 1 169 ? 10.132  21.294  4.062   1   29.83  ? 169  TYR A OH    1 1 
ATOM   1388 N  N     . ILE A 1 170 ? 4.687   18.032  -1.864  1   14.61  ? 170  ILE A N     1 1 
ATOM   1389 C  CA    . ILE A 1 170 ? 3.915   17.224  -2.809  1   16.01  ? 170  ILE A CA    1 1 
ATOM   1390 C  C     . ILE A 1 170 ? 4.161   17.679  -4.227  1   15.82  ? 170  ILE A C     1 1 
ATOM   1391 O  O     . ILE A 1 170 ? 4.471   16.831  -5.068  1   15.66  ? 170  ILE A O     1 1 
ATOM   1392 C  CB    . ILE A 1 170 ? 2.405   17.192  -2.463  1   17.09  ? 170  ILE A CB    1 1 
ATOM   1393 C  CG1   . ILE A 1 170 ? 2.155   16.615  -1.056  1   18.21  ? 170  ILE A CG1   1 1 
ATOM   1394 C  CG2   . ILE A 1 170 ? 1.609   16.411  -3.501  1   17.72  ? 170  ILE A CG2   1 1 
ATOM   1395 C  CD1   . ILE A 1 170 ? 0.765   16.952  -0.534  1   18.79  ? 170  ILE A CD1   1 1 
ATOM   1396 N  N     . SER A 1 171 ? 4.082   19.012  -4.49   1   15.16  ? 171  SER A N     1 1 
ATOM   1397 C  CA    . SER A 1 171 ? 4.315   19.534  -5.835  1   15.19  ? 171  SER A CA    1 1 
ATOM   1398 C  C     . SER A 1 171 ? 5.749   19.344  -6.287  1   14.72  ? 171  SER A C     1 1 
ATOM   1399 O  O     . SER A 1 171 ? 5.968   19.036  -7.465  1   14.79  ? 171  SER A O     1 1 
ATOM   1400 C  CB    . SER A 1 171 ? 3.889   20.996  -5.968  1   16.5   ? 171  SER A CB    1 1 
ATOM   1401 O  OG    . SER A 1 171 ? 4.415   21.79   -4.925  1   19.81  ? 171  SER A OG    1 1 
ATOM   1402 N  N     . HIS A 1 172 ? 6.726   19.466  -5.346  1   14.06  ? 172  HIS A N     1 1 
ATOM   1403 C  CA    . HIS A 1 172 ? 8.122   19.247  -5.672  1   14.83  ? 172  HIS A CA    1 1 
ATOM   1404 C  C     . HIS A 1 172 ? 8.347   17.801  -6.063  1   15.48  ? 172  HIS A C     1 1 
ATOM   1405 O  O     . HIS A 1 172 ? 9.089   17.571  -7.006  1   15.45  ? 172  HIS A O     1 1 
ATOM   1406 C  CB    . HIS A 1 172 ? 9.088   19.678  -4.552  1   14.69  ? 172  HIS A CB    1 1 
ATOM   1407 C  CG    . HIS A 1 172 ? 10.483  19.951  -5.05   1   15.44  ? 172  HIS A CG    1 1 
ATOM   1408 N  ND1   . HIS A 1 172 ? 10.71   20.52   -6.303  1   16.58  ? 172  HIS A ND1   1 1 
ATOM   1409 C  CD2   . HIS A 1 172 ? 11.672  19.793  -4.425  1   15.49  ? 172  HIS A CD2   1 1 
ATOM   1410 C  CE1   . HIS A 1 172 ? 12.02   20.643  -6.409  1   16.74  ? 172  HIS A CE1   1 1 
ATOM   1411 N  NE2   . HIS A 1 172 ? 12.641  20.215  -5.307  1   16.64  ? 172  HIS A NE2   1 1 
ATOM   1412 N  N     . SER A 1 173 ? 7.686   16.833  -5.37   1   16.59  ? 173  SER A N     1 1 
ATOM   1413 C  CA    . SER A 1 173 ? 7.751   15.422  -5.729  1   18.49  ? 173  SER A CA    1 1 
ATOM   1414 C  C     . SER A 1 173 ? 7.224   15.207  -7.149  1   19.73  ? 173  SER A C     1 1 
ATOM   1415 O  O     . SER A 1 173 ? 7.86    14.495  -7.923  1   20.26  ? 173  SER A O     1 1 
ATOM   1416 C  CB    . SER A 1 173 ? 6.91    14.556  -4.784  1   20.6   ? 173  SER A CB    1 1 
ATOM   1417 O  OG    . SER A 1 173 ? 7.451   14.47   -3.48   1   24.24  ? 173  SER A OG    1 1 
ATOM   1418 N  N     . LYS A 1 174 ? 6.05    15.773  -7.477  1   19.68  ? 174  LYS A N     1 1 
ATOM   1419 C  CA    . LYS A 1 174 ? 5.463   15.578  -8.794  1   20.78  ? 174  LYS A CA    1 1 
ATOM   1420 C  C     . LYS A 1 174 ? 6.344   16.133  -9.91   1   22.22  ? 174  LYS A C     1 1 
ATOM   1421 O  O     . LYS A 1 174 ? 6.579   15.435  -10.901 1   22.23  ? 174  LYS A O     1 1 
ATOM   1422 C  CB    . LYS A 1 174 ? 4.02    16.126  -8.859  1   22.04  ? 174  LYS A CB    1 1 
ATOM   1423 N  N     . ASN A 1 175 ? 6.891   17.35   -9.713  1   22.41  ? 175  ASN A N     1 1 
ATOM   1424 C  CA    . ASN A 1 175 ? 7.739   18.036  -10.694 1   23.55  ? 175  ASN A CA    1 1 
ATOM   1425 C  C     . ASN A 1 175 ? 9.052   17.349  -11.005 1   24.77  ? 175  ASN A C     1 1 
ATOM   1426 O  O     . ASN A 1 175 ? 9.493   17.351  -12.154 1   25.75  ? 175  ASN A O     1 1 
ATOM   1427 C  CB    . ASN A 1 175 ? 8.029   19.464  -10.224 1   24.37  ? 175  ASN A CB    1 1 
ATOM   1428 C  CG    . ASN A 1 175 ? 6.799   20.334  -10.233 1   26.92  ? 175  ASN A CG    1 1 
ATOM   1429 O  OD1   . ASN A 1 175 ? 5.871   20.1    -11.014 1   29.12  ? 175  ASN A OD1   1 1 
ATOM   1430 N  ND2   . ASN A 1 175 ? 6.742   21.322  -9.346  1   25.61  ? 175  ASN A ND2   1 1 
ATOM   1431 N  N     . THR A 1 176 ? 9.711   16.809  -9.967  1   23.9   ? 176  THR A N     1 1 
ATOM   1432 C  CA    . THR A 1 176 ? 10.999  16.166  -10.089 1   22.66  ? 176  THR A CA    1 1 
ATOM   1433 C  C     . THR A 1 176 ? 10.896  14.675  -10.415 1   22.75  ? 176  THR A C     1 1 
ATOM   1434 O  O     . THR A 1 176 ? 11.772  14.133  -11.077 1   23.38  ? 176  THR A O     1 1 
ATOM   1435 C  CB    . THR A 1 176 ? 11.75   16.334  -8.773  1   21.86  ? 176  THR A CB    1 1 
ATOM   1436 O  OG1   . THR A 1 176 ? 10.975  15.767  -7.716  1   21.07  ? 176  THR A OG1   1 1 
ATOM   1437 C  CG2   . THR A 1 176 ? 12.095  17.775  -8.472  1   21.87  ? 176  THR A CG2   1 1 
ATOM   1438 N  N     . GLY A 1 177 ? 9.85    14.018  -9.927  1   21.61  ? 177  GLY A N     1 1 
ATOM   1439 C  CA    . GLY A 1 177 ? 9.741   12.57   -10.036 1   21.1   ? 177  GLY A CA    1 1 
ATOM   1440 C  C     . GLY A 1 177 ? 10.437  11.888  -8.862  1   20.12  ? 177  GLY A C     1 1 
ATOM   1441 O  O     . GLY A 1 177 ? 10.591  10.668  -8.855  1   20.44  ? 177  GLY A O     1 1 
ATOM   1442 N  N     . ASN A 1 178 ? 10.895  12.664  -7.859  1   18.3   ? 178  ASN A N     1 1 
ATOM   1443 C  CA    . ASN A 1 178 ? 11.575  12.131  -6.682  1   17.82  ? 178  ASN A CA    1 1 
ATOM   1444 C  C     . ASN A 1 178 ? 10.595  12.07   -5.476  1   17.17  ? 178  ASN A C     1 1 
ATOM   1445 O  O     . ASN A 1 178 ? 9.515   12.647  -5.531  1   17.81  ? 178  ASN A O     1 1 
ATOM   1446 C  CB    . ASN A 1 178 ? 12.818  13.02   -6.374  1   18.63  ? 178  ASN A CB    1 1 
ATOM   1447 C  CG    . ASN A 1 178 ? 13.675  12.601  -5.187  1   22.79  ? 178  ASN A CG    1 1 
ATOM   1448 O  OD1   . ASN A 1 178 ? 13.669  11.393  -4.751  1   24.65  ? 178  ASN A OD1   1 1 
ATOM   1449 N  ND2   . ASN A 1 178 ? 14.471  13.574  -4.662  1   20.74  ? 178  ASN A ND2   1 1 
ATOM   1450 N  N     . PHE A 1 179 ? 10.955  11.342  -4.407  1   15.94  ? 179  PHE A N     1 1 
ATOM   1451 C  CA    . PHE A 1 179 ? 10.157  11.258  -3.184  1   15.28  ? 179  PHE A CA    1 1 
ATOM   1452 C  C     . PHE A 1 179 ? 10.605  12.364  -2.182  1   14.75  ? 179  PHE A C     1 1 
ATOM   1453 O  O     . PHE A 1 179 ? 11.66   12.253  -1.552  1   13.54  ? 179  PHE A O     1 1 
ATOM   1454 C  CB    . PHE A 1 179 ? 10.316  9.881   -2.533  1   14.58  ? 179  PHE A CB    1 1 
ATOM   1455 C  CG    . PHE A 1 179 ? 9.432   9.681   -1.325  1   15.25  ? 179  PHE A CG    1 1 
ATOM   1456 C  CD1   . PHE A 1 179 ? 8.065   9.906   -1.4    1   16.39  ? 179  PHE A CD1   1 1 
ATOM   1457 C  CD2   . PHE A 1 179 ? 9.949   9.172   -0.147  1   15.84  ? 179  PHE A CD2   1 1 
ATOM   1458 C  CE1   . PHE A 1 179 ? 7.235   9.655   -0.305  1   16.75  ? 179  PHE A CE1   1 1 
ATOM   1459 C  CE2   . PHE A 1 179 ? 9.123   8.926   0.943   1   16.69  ? 179  PHE A CE2   1 1 
ATOM   1460 C  CZ    . PHE A 1 179 ? 7.769   9.153   0.855   1   16.5   ? 179  PHE A CZ    1 1 
ATOM   1461 N  N     . ILE A 1 180 ? 9.802   13.432  -2.067  1   14.51  ? 180  ILE A N     1 1 
ATOM   1462 C  CA    . ILE A 1 180 ? 10.071  14.539  -1.147  1   15.73  ? 180  ILE A CA    1 1 
ATOM   1463 C  C     . ILE A 1 180 ? 8.787   14.638  -0.334  1   16.95  ? 180  ILE A C     1 1 
ATOM   1464 O  O     . ILE A 1 180 ? 7.713   14.87   -0.916  1   17.96  ? 180  ILE A O     1 1 
ATOM   1465 C  CB    . ILE A 1 180 ? 10.319  15.866  -1.916  1   15.91  ? 180  ILE A CB    1 1 
ATOM   1466 C  CG1   . ILE A 1 180 ? 11.533  15.741  -2.848  1   16.6   ? 180  ILE A CG1   1 1 
ATOM   1467 C  CG2   . ILE A 1 180 ? 10.501  17.04   -0.931  1   16.38  ? 180  ILE A CG2   1 1 
ATOM   1468 C  CD1   . ILE A 1 180 ? 11.282  16.104  -4.241  1   17.76  ? 180  ILE A CD1   1 1 
ATOM   1469 N  N     . VAL A 1 181 ? 8.873   14.438  0.981   1   16.22  ? 181  VAL A N     1 1 
ATOM   1470 C  CA    . VAL A 1 181 ? 7.67    14.394  1.793   1   16.39  ? 181  VAL A CA    1 1 
ATOM   1471 C  C     . VAL A 1 181 ? 7.871   15.037  3.144   1   16.76  ? 181  VAL A C     1 1 
ATOM   1472 O  O     . VAL A 1 181 ? 8.991   15.074  3.674   1   16.65  ? 181  VAL A O     1 1 
ATOM   1473 C  CB    . VAL A 1 181 ? 7.246   12.91   1.948   1   16.61  ? 181  VAL A CB    1 1 
ATOM   1474 C  CG1   . VAL A 1 181 ? 8.219   12.136  2.841   1   16.34  ? 181  VAL A CG1   1 1 
ATOM   1475 C  CG2   . VAL A 1 181 ? 5.788   12.759  2.427   1   17.23  ? 181  VAL A CG2   1 1 
ATOM   1476 N  N     . GLN A 1 182 ? 6.769   15.502  3.716   1   16.33  ? 182  GLN A N     1 1 
ATOM   1477 C  CA    . GLN A 1 182 ? 6.73    15.965  5.081   1   17.43  ? 182  GLN A CA    1 1 
ATOM   1478 C  C     . GLN A 1 182 ? 5.937   14.876  5.873   1   18.27  ? 182  GLN A C     1 1 
ATOM   1479 O  O     . GLN A 1 182 ? 4.886   14.44   5.427   1   19.04  ? 182  GLN A O     1 1 
ATOM   1480 C  CB    . GLN A 1 182 ? 6.034   17.318  5.144   1   18.87  ? 182  GLN A CB    1 1 
ATOM   1481 C  CG    . GLN A 1 182 ? 6.347   18.094  6.383   1   23.29  ? 182  GLN A CG    1 1 
ATOM   1482 C  CD    . GLN A 1 182 ? 5.767   19.48   6.26    1   28.81  ? 182  GLN A CD    1 1 
ATOM   1483 O  OE1   . GLN A 1 182 ? 4.559   19.649  6.149   1   31.78  ? 182  GLN A OE1   1 1 
ATOM   1484 N  NE2   . GLN A 1 182 ? 6.601   20.494  6.253   1   29.96  ? 182  GLN A NE2   1 1 
ATOM   1485 N  N     . ALA A 1 183 ? 6.497   14.36   6.966   1   18.36  ? 183  ALA A N     1 1 
ATOM   1486 C  CA    . ALA A 1 183 ? 5.867   13.328  7.811   1   18.95  ? 183  ALA A CA    1 1 
ATOM   1487 C  C     . ALA A 1 183 ? 5.733   13.885  9.228   1   19.52  ? 183  ALA A C     1 1 
ATOM   1488 O  O     . ALA A 1 183 ? 6.59    14.65   9.696   1   19.97  ? 183  ALA A O     1 1 
ATOM   1489 C  CB    . ALA A 1 183 ? 6.693   12.04   7.815   1   19.35  ? 183  ALA A CB    1 1 
ATOM   1490 N  N     . TYR A 1 184 ? 4.637   13.552  9.889   1   19.06  ? 184  TYR A N     1 1 
ATOM   1491 C  CA    . TYR A 1 184 ? 4.313   14.112  11.197  1   18.95  ? 184  TYR A CA    1 1 
ATOM   1492 C  C     . TYR A 1 184 ? 4.256   13.031  12.242  1   19.3   ? 184  TYR A C     1 1 
ATOM   1493 O  O     . TYR A 1 184 ? 3.588   12.039  12.055  1   18.66  ? 184  TYR A O     1 1 
ATOM   1494 C  CB    . TYR A 1 184 ? 2.966   14.884  11.148  1   18.98  ? 184  TYR A CB    1 1 
ATOM   1495 C  CG    . TYR A 1 184 ? 2.842   15.735  9.905   1   19.39  ? 184  TYR A CG    1 1 
ATOM   1496 C  CD1   . TYR A 1 184 ? 3.429   16.991  9.839   1   19.95  ? 184  TYR A CD1   1 1 
ATOM   1497 C  CD2   . TYR A 1 184 ? 2.303   15.212  8.738   1   20.15  ? 184  TYR A CD2   1 1 
ATOM   1498 C  CE1   . TYR A 1 184 ? 3.413   17.732  8.67    1   20.8   ? 184  TYR A CE1   1 1 
ATOM   1499 C  CE2   . TYR A 1 184 ? 2.302   15.934  7.558   1   21.01  ? 184  TYR A CE2   1 1 
ATOM   1500 C  CZ    . TYR A 1 184 ? 2.837   17.196  7.533   1   22.04  ? 184  TYR A CZ    1 1 
ATOM   1501 O  OH    . TYR A 1 184 ? 2.787   17.895  6.355   1   25.39  ? 184  TYR A OH    1 1 
ATOM   1502 N  N     . PHE A 1 185 ? 4.981   13.211  13.325  1   19.89  ? 185  PHE A N     1 1 
ATOM   1503 C  CA    . PHE A 1 185 ? 4.965   12.285  14.438  1   21.59  ? 185  PHE A CA    1 1 
ATOM   1504 C  C     . PHE A 1 185 ? 4.141   12.89   15.551  1   23.4   ? 185  PHE A C     1 1 
ATOM   1505 O  O     . PHE A 1 185 ? 4.14    14.116  15.717  1   24.42  ? 185  PHE A O     1 1 
ATOM   1506 C  CB    . PHE A 1 185 ? 6.401   12.021  14.914  1   22     ? 185  PHE A CB    1 1 
ATOM   1507 C  CG    . PHE A 1 185 ? 7.226   11.079  14.061  1   22.88  ? 185  PHE A CG    1 1 
ATOM   1508 C  CD1   . PHE A 1 185 ? 6.715   10.542  12.887  1   24.13  ? 185  PHE A CD1   1 1 
ATOM   1509 C  CD2   . PHE A 1 185 ? 8.507   10.72   14.44   1   23.88  ? 185  PHE A CD2   1 1 
ATOM   1510 C  CE1   . PHE A 1 185 ? 7.473   9.663   12.121  1   25.19  ? 185  PHE A CE1   1 1 
ATOM   1511 C  CE2   . PHE A 1 185 ? 9.254   9.833   13.676  1   24.74  ? 185  PHE A CE2   1 1 
ATOM   1512 C  CZ    . PHE A 1 185 ? 8.728   9.308   12.529  1   24.74  ? 185  PHE A CZ    1 1 
ATOM   1513 N  N     . ARG A 1 186 ? 3.415   12.065  16.298  1   23.74  ? 186  ARG A N     1 1 
ATOM   1514 C  CA    . ARG A 1 186 ? 2.604   12.576  17.394  1   25     ? 186  ARG A CA    1 1 
ATOM   1515 C  C     . ARG A 1 186 ? 3.507   13.157  18.495  1   26.41  ? 186  ARG A C     1 1 
ATOM   1516 O  O     . ARG A 1 186 ? 4.293   12.437  19.108  1   26.92  ? 186  ARG A O     1 1 
ATOM   1517 C  CB    . ARG A 1 186 ? 1.663   11.492  17.939  1   26.01  ? 186  ARG A CB    1 1 
ATOM   1518 C  CG    . ARG A 1 186 ? 0.853   11.965  19.137  1   29.54  ? 186  ARG A CG    1 1 
ATOM   1519 C  CD    . ARG A 1 186 ? 0.229   10.819  19.905  1   33.52  ? 186  ARG A CD    1 1 
ATOM   1520 N  NE    . ARG A 1 186 ? -0.963  10.308  19.245  1   37.45  ? 186  ARG A NE    1 1 
ATOM   1521 C  CZ    . ARG A 1 186 ? -2.203  10.442  19.715  1   40.58  ? 186  ARG A CZ    1 1 
ATOM   1522 N  NH1   . ARG A 1 186 ? -2.421  11.066  20.87   1   40.55  ? 186  ARG A NH1   1 1 
ATOM   1523 N  NH2   . ARG A 1 186 ? -3.231  9.953   19.037  1   40.07  ? 186  ARG A NH2   1 1 
ATOM   1524 N  N     . GLY A 1 187 ? 3.41    14.463  18.708  1   27.19  ? 187  GLY A N     1 1 
ATOM   1525 C  CA    . GLY A 1 187 ? 4.173   15.106  19.768  1   27.5   ? 187  GLY A CA    1 1 
ATOM   1526 C  C     . GLY A 1 187 ? 3.586   14.737  21.119  1   27.51  ? 187  GLY A C     1 1 
ATOM   1527 O  O     . GLY A 1 187 ? 2.404   14.387  21.215  1   26.42  ? 187  GLY A O     1 1 
ATOM   1528 N  N     . GLU A 1 188 ? 4.393   14.824  22.185  1   27.83  ? 188  GLU A N     1 1 
ATOM   1529 C  CA    . GLU A 1 188 ? 3.887   14.594  23.542  1   28.53  ? 188  GLU A CA    1 1 
ATOM   1530 C  C     . GLU A 1 188 ? 2.793   15.672  23.884  1   29.06  ? 188  GLU A C     1 1 
ATOM   1531 O  O     . GLU A 1 188 ? 1.851   15.388  24.608  1   29.35  ? 188  GLU A O     1 1 
ATOM   1532 C  CB    . GLU A 1 188 ? 5.04    14.691  24.557  1   29.91  ? 188  GLU A CB    1 1 
ATOM   1533 C  CG    . GLU A 1 188 ? 6.193   13.747  24.283  1   31.7   ? 188  GLU A CG    1 1 
ATOM   1534 C  CD    . GLU A 1 188 ? 7.397   14.381  23.611  1   35.84  ? 188  GLU A CD    1 1 
ATOM   1535 O  OE1   . GLU A 1 188 ? 7.222   15.186  22.665  1   35.39  ? 188  GLU A OE1   1 1 
ATOM   1536 O  OE2   . GLU A 1 188 ? 8.53    14.067  24.041  1   39.1   ? 188  GLU A OE2   1 1 
ATOM   1537 N  N     . GLU A 1 189 ? 2.913   16.884  23.327  1   29.37  ? 189  GLU A N     1 1 
ATOM   1538 C  CA    . GLU A 1 189 ? 1.952   17.962  23.555  1   30.13  ? 189  GLU A CA    1 1 
ATOM   1539 C  C     . GLU A 1 189 ? 0.759   17.957  22.592  1   31.1   ? 189  GLU A C     1 1 
ATOM   1540 O  O     . GLU A 1 189 ? 0.012   18.937  22.564  1   32.05  ? 189  GLU A O     1 1 
ATOM   1541 C  CB    . GLU A 1 189 ? 2.633   19.34   23.566  1   31.45  ? 189  GLU A CB    1 1 
ATOM   1542 C  CG    . GLU A 1 189 ? 3.311   19.629  24.886  1   33.1   ? 189  GLU A CG    1 1 
ATOM   1543 C  CD    . GLU A 1 189 ? 3.919   21.003  25.036  1   36.69  ? 189  GLU A CD    1 1 
ATOM   1544 O  OE1   . GLU A 1 189 ? 4.397   21.584  24.031  1   36.58  ? 189  GLU A OE1   1 1 
ATOM   1545 O  OE2   . GLU A 1 189 ? 3.927   21.495  26.186  1   38.6   ? 189  GLU A OE2   1 1 
ATOM   1546 N  N     . TYR A 1 190 ? 0.552   16.87   21.827  1   30.76  ? 190  TYR A N     1 1 
ATOM   1547 C  CA    . TYR A 1 190 ? -0.649  16.758  21.006  1   31.13  ? 190  TYR A CA    1 1 
ATOM   1548 C  C     . TYR A 1 190 ? -1.707  16.302  22.011  1   32.48  ? 190  TYR A C     1 1 
ATOM   1549 O  O     . TYR A 1 190 ? -1.717  15.14   22.402  1   32.73  ? 190  TYR A O     1 1 
ATOM   1550 C  CB    . TYR A 1 190 ? -0.492  15.722  19.886  1   30.47  ? 190  TYR A CB    1 1 
ATOM   1551 C  CG    . TYR A 1 190 ? -1.798  15.45   19.171  1   30.73  ? 190  TYR A CG    1 1 
ATOM   1552 C  CD1   . TYR A 1 190 ? -2.401  16.427  18.385  1   31.09  ? 190  TYR A CD1   1 1 
ATOM   1553 C  CD2   . TYR A 1 190 ? -2.465  14.244  19.334  1   30.84  ? 190  TYR A CD2   1 1 
ATOM   1554 C  CE1   . TYR A 1 190 ? -3.607  16.191  17.739  1   30.91  ? 190  TYR A CE1   1 1 
ATOM   1555 C  CE2   . TYR A 1 190 ? -3.682  14.003  18.707  1   31.42  ? 190  TYR A CE2   1 1 
ATOM   1556 C  CZ    . TYR A 1 190 ? -4.246  14.979  17.905  1   31.87  ? 190  TYR A CZ    1 1 
ATOM   1557 O  OH    . TYR A 1 190 ? -5.443  14.758  17.27   1   32.63  ? 190  TYR A OH    1 1 
ATOM   1558 N  N     . GLN A 1 191 ? -2.536  17.234  22.488  1   33.35  ? 191  GLN A N     1 1 
ATOM   1559 C  CA    . GLN A 1 191 ? -3.559  16.972  23.492  1   34.59  ? 191  GLN A CA    1 1 
ATOM   1560 C  C     . GLN A 1 191 ? -4.866  17.608  22.991  1   34.89  ? 191  GLN A C     1 1 
ATOM   1561 O  O     . GLN A 1 191 ? -5.209  18.733  23.376  1   34.57  ? 191  GLN A O     1 1 
ATOM   1562 C  CB    . GLN A 1 191 ? -3.112  17.637  24.797  1   37.48  ? 191  GLN A CB    1 1 
ATOM   1563 C  CG    . GLN A 1 191 ? -3.295  16.771  26.025  1   43.2   ? 191  GLN A CG    1 1 
ATOM   1564 C  CD    . GLN A 1 191 ? -2.484  15.511  25.968  1   49.35  ? 191  GLN A CD    1 1 
ATOM   1565 O  OE1   . GLN A 1 191 ? -1.273  15.521  25.691  1   51.3   ? 191  GLN A OE1   1 1 
ATOM   1566 N  NE2   . GLN A 1 191 ? -3.142  14.39   26.239  1   50.64  ? 191  GLN A NE2   1 1 
ATOM   1567 N  N     . PRO A 1 192 ? -5.572  16.918  22.074  1   34.92  ? 192  PRO A N     1 1 
ATOM   1568 C  CA    . PRO A 1 192 ? -6.751  17.527  21.441  1   35.21  ? 192  PRO A CA    1 1 
ATOM   1569 C  C     . PRO A 1 192 ? -7.951  17.793  22.358  1   36.62  ? 192  PRO A C     1 1 
ATOM   1570 O  O     . PRO A 1 192 ? -8.781  18.633  22.018  1   36.74  ? 192  PRO A O     1 1 
ATOM   1571 C  CB    . PRO A 1 192 ? -7.079  16.567  20.303  1   35.38  ? 192  PRO A CB    1 1 
ATOM   1572 C  CG    . PRO A 1 192 ? -6.488  15.27   20.719  1   35.72  ? 192  PRO A CG    1 1 
ATOM   1573 C  CD    . PRO A 1 192 ? -5.249  15.612  21.474  1   34.31  ? 192  PRO A CD    1 1 
ATOM   1574 N  N     . LYS A 1 193 ? -8.024  17.146  23.527  1   37.3   ? 193  LYS A N     1 1 
ATOM   1575 C  CA    . LYS A 1 193 ? -9.105  17.403  24.478  1   38.16  ? 193  LYS A CA    1 1 
ATOM   1576 C  C     . LYS A 1 193 ? -8.977  18.796  25.137  1   38.59  ? 193  LYS A C     1 1 
ATOM   1577 O  O     . LYS A 1 193 ? -9.966  19.302  25.663  1   39.09  ? 193  LYS A O     1 1 
ATOM   1578 C  CB    . LYS A 1 193 ? -9.121  16.318  25.567  1   40.68  ? 193  LYS A CB    1 1 
ATOM   1579 C  CG    . LYS A 1 193 ? -9.733  14.995  25.091  1   46.01  ? 193  LYS A CG    1 1 
ATOM   1580 C  CD    . LYS A 1 193 ? -8.828  13.784  25.396  1   51.62  ? 193  LYS A CD    1 1 
ATOM   1581 C  CE    . LYS A 1 193 ? -9.168  13.076  26.693  1   55.77  ? 193  LYS A CE    1 1 
ATOM   1582 N  NZ    . LYS A 1 193 ? -8.075  12.159  27.123  1   57.89  ? 193  LYS A NZ    1 1 
ATOM   1583 N  N     . TYR A 1 194 ? -7.785  19.418  25.098  1   38.01  ? 194  TYR A N     1 1 
ATOM   1584 C  CA    . TYR A 1 194 ? -7.538  20.71   25.736  1   38.64  ? 194  TYR A CA    1 1 
ATOM   1585 C  C     . TYR A 1 194 ? -7.33   21.885  24.768  1   37.5   ? 194  TYR A C     1 1 
ATOM   1586 O  O     . TYR A 1 194 ? -7.076  23.002  25.223  1   38.33  ? 194  TYR A O     1 1 
ATOM   1587 C  CB    . TYR A 1 194 ? -6.322  20.608  26.676  1   39.99  ? 194  TYR A CB    1 1 
ATOM   1588 C  CG    . TYR A 1 194 ? -6.528  19.618  27.796  1   42.76  ? 194  TYR A CG    1 1 
ATOM   1589 C  CD1   . TYR A 1 194 ? -7.22   19.973  28.944  1   44.88  ? 194  TYR A CD1   1 1 
ATOM   1590 C  CD2   . TYR A 1 194 ? -6.099  18.305  27.677  1   44.2   ? 194  TYR A CD2   1 1 
ATOM   1591 C  CE1   . TYR A 1 194 ? -7.458  19.052  29.959  1   46.47  ? 194  TYR A CE1   1 1 
ATOM   1592 C  CE2   . TYR A 1 194 ? -6.322  17.377  28.685  1   45.8   ? 194  TYR A CE2   1 1 
ATOM   1593 C  CZ    . TYR A 1 194 ? -6.987  17.758  29.835  1   47.59  ? 194  TYR A CZ    1 1 
ATOM   1594 O  OH    . TYR A 1 194 ? -7.211  16.843  30.841  1   49.81  ? 194  TYR A OH    1 1 
ATOM   1595 N  N     . ASP A 1 195 ? -7.389  21.644  23.455  1   35.31  ? 195  ASP A N     1 1 
ATOM   1596 C  CA    . ASP A 1 195 ? -7.168  22.706  22.479  1   33.25  ? 195  ASP A CA    1 1 
ATOM   1597 C  C     . ASP A 1 195 ? -8.127  22.559  21.321  1   31.39  ? 195  ASP A C     1 1 
ATOM   1598 O  O     . ASP A 1 195 ? -8.054  21.593  20.563  1   31.01  ? 195  ASP A O     1 1 
ATOM   1599 C  CB    . ASP A 1 195 ? -5.708  22.701  21.984  1   33.87  ? 195  ASP A CB    1 1 
ATOM   1600 C  CG    . ASP A 1 195 ? -5.262  24.012  21.346  1   34.91  ? 195  ASP A CG    1 1 
ATOM   1601 O  OD1   . ASP A 1 195 ? -6.08   24.643  20.641  1   34.04  ? 195  ASP A OD1   1 1 
ATOM   1602 O  OD2   . ASP A 1 195 ? -4.092  24.397  21.539  1   36.06  ? 195  ASP A OD2   1 1 
ATOM   1603 N  N     . LYS A 1 196 ? -9.01   23.549  21.169  1   30.22  ? 196  LYS A N     1 1 
ATOM   1604 C  CA    . LYS A 1 196 ? -10.022 23.595  20.126  1   29.06  ? 196  LYS A CA    1 1 
ATOM   1605 C  C     . LYS A 1 196 ? -9.439  23.687  18.721  1   26.63  ? 196  LYS A C     1 1 
ATOM   1606 O  O     . LYS A 1 196 ? -10.091 23.255  17.776  1   26.36  ? 196  LYS A O     1 1 
ATOM   1607 C  CB    . LYS A 1 196 ? -11.001 24.741  20.4    1   32.51  ? 196  LYS A CB    1 1 
ATOM   1608 C  CG    . LYS A 1 196 ? -11.822 24.496  21.659  1   39     ? 196  LYS A CG    1 1 
ATOM   1609 C  CD    . LYS A 1 196 ? -12.731 25.681  22.012  1   44.54  ? 196  LYS A CD    1 1 
ATOM   1610 C  CE    . LYS A 1 196 ? -13.678 25.331  23.141  1   48.35  ? 196  LYS A CE    1 1 
ATOM   1611 N  NZ    . LYS A 1 196 ? -14.285 23.982  22.956  1   50.58  ? 196  LYS A NZ    1 1 
ATOM   1612 N  N     . LYS A 1 197 ? -8.216  24.199  18.575  1   24.98  ? 197  LYS A N     1 1 
ATOM   1613 C  CA    . LYS A 1 197 ? -7.567  24.276  17.264  1   24.64  ? 197  LYS A CA    1 1 
ATOM   1614 C  C     . LYS A 1 197 ? -7.316  22.896  16.64   1   23.6   ? 197  LYS A C     1 1 
ATOM   1615 O  O     . LYS A 1 197 ? -7.205  22.771  15.417  1   23.38  ? 197  LYS A O     1 1 
ATOM   1616 C  CB    . LYS A 1 197 ? -6.252  25.056  17.346  1   26.22  ? 197  LYS A CB    1 1 
ATOM   1617 C  CG    . LYS A 1 197 ? -6.462  26.519  17.683  1   30.6   ? 197  LYS A CG    1 1 
ATOM   1618 C  CD    . LYS A 1 197 ? -5.179  27.309  17.538  1   35.37  ? 197  LYS A CD    1 1 
ATOM   1619 C  CE    . LYS A 1 197 ? -5.371  28.737  18.022  1   39.69  ? 197  LYS A CE    1 1 
ATOM   1620 N  NZ    . LYS A 1 197 ? -4.638  29.693  17.161  1   43.52  ? 197  LYS A NZ    1 1 
ATOM   1621 N  N     . LEU A 1 198 ? -7.244  21.861  17.475  1   22.79  ? 198  LEU A N     1 1 
ATOM   1622 C  CA    . LEU A 1 198 ? -7.022  20.507  16.998  1   22.37  ? 198  LEU A CA    1 1 
ATOM   1623 C  C     . LEU A 1 198 ? -8.303  19.702  16.797  1   22.33  ? 198  LEU A C     1 1 
ATOM   1624 O  O     . LEU A 1 198 ? -8.212  18.513  16.495  1   22.15  ? 198  LEU A O     1 1 
ATOM   1625 C  CB    . LEU A 1 198 ? -6.084  19.777  17.972  1   22.3   ? 198  LEU A CB    1 1 
ATOM   1626 C  CG    . LEU A 1 198 ? -4.747  20.455  18.258  1   21.88  ? 198  LEU A CG    1 1 
ATOM   1627 C  CD1   . LEU A 1 198 ? -3.982  19.702  19.333  1   22.04  ? 198  LEU A CD1   1 1 
ATOM   1628 C  CD2   . LEU A 1 198 ? -3.915  20.577  17.006  1   21.89  ? 198  LEU A CD2   1 1 
ATOM   1629 N  N     . LYS A 1 199 ? -9.49   20.335  16.943  1   22.03  ? 199  LYS A N     1 1 
ATOM   1630 C  CA    . LYS A 1 199 ? -10.795 19.673  16.82   1   22.49  ? 199  LYS A CA    1 1 
ATOM   1631 C  C     . LYS A 1 199 ? -10.962 18.834  15.562  1   21.23  ? 199  LYS A C     1 1 
ATOM   1632 O  O     . LYS A 1 199 ? -11.475 17.717  15.63   1   21.3   ? 199  LYS A O     1 1 
ATOM   1633 C  CB    . LYS A 1 199 ? -11.948 20.689  16.94   1   24.67  ? 199  LYS A CB    1 1 
ATOM   1634 C  CG    . LYS A 1 199 ? -13.287 20.019  17.156  1   30.36  ? 199  LYS A CG    1 1 
ATOM   1635 C  CD    . LYS A 1 199 ? -14.445 21.001  17.123  1   36.38  ? 199  LYS A CD    1 1 
ATOM   1636 C  CE    . LYS A 1 199 ? -15.766 20.267  17.174  1   41.64  ? 199  LYS A CE    1 1 
ATOM   1637 N  NZ    . LYS A 1 199 ? -16.9   21.174  16.833  1   45.5   ? 199  LYS A NZ    1 1 
ATOM   1638 N  N     . PHE A 1 200 ? -10.503 19.363  14.428  1   20.11  ? 200  PHE A N     1 1 
ATOM   1639 C  CA    . PHE A 1 200 ? -10.664 18.666  13.165  1   20.26  ? 200  PHE A CA    1 1 
ATOM   1640 C  C     . PHE A 1 200 ? -9.413  18.005  12.655  1   19.9   ? 200  PHE A C     1 1 
ATOM   1641 O  O     . PHE A 1 200 ? -9.314  17.768  11.45   1   19.9   ? 200  PHE A O     1 1 
ATOM   1642 C  CB    . PHE A 1 200 ? -11.264 19.603  12.11   1   20.56  ? 200  PHE A CB    1 1 
ATOM   1643 C  CG    . PHE A 1 200 ? -12.61  20.106  12.571  1   21.42  ? 200  PHE A CG    1 1 
ATOM   1644 C  CD1   . PHE A 1 200 ? -13.662 19.23   12.768  1   22.82  ? 200  PHE A CD1   1 1 
ATOM   1645 C  CD2   . PHE A 1 200 ? -12.795 21.438  12.893  1   22.58  ? 200  PHE A CD2   1 1 
ATOM   1646 C  CE1   . PHE A 1 200 ? -14.89  19.683  13.244  1   23.74  ? 200  PHE A CE1   1 1 
ATOM   1647 C  CE2   . PHE A 1 200 ? -14.014 21.887  13.392  1   23.36  ? 200  PHE A CE2   1 1 
ATOM   1648 C  CZ    . PHE A 1 200 ? -15.062 21.01   13.537  1   23.27  ? 200  PHE A CZ    1 1 
ATOM   1649 N  N     . PHE A 1 201 ? -8.453  17.706  13.546  1   19.44  ? 201  PHE A N     1 1 
ATOM   1650 C  CA    . PHE A 1 201 ? -7.239  17.032  13.113  1   20.11  ? 201  PHE A CA    1 1 
ATOM   1651 C  C     . PHE A 1 201 ? -7.515  15.549  12.866  1   21.34  ? 201  PHE A C     1 1 
ATOM   1652 O  O     . PHE A 1 201 ? -8.138  14.887  13.701  1   22.9   ? 201  PHE A O     1 1 
ATOM   1653 C  CB    . PHE A 1 201 ? -6.085  17.2    14.117  1   18.97  ? 201  PHE A CB    1 1 
ATOM   1654 C  CG    . PHE A 1 201 ? -4.799  16.641  13.561  1   18.22  ? 201  PHE A CG    1 1 
ATOM   1655 C  CD1   . PHE A 1 201 ? -4.162  17.253  12.49   1   18.6   ? 201  PHE A CD1   1 1 
ATOM   1656 C  CD2   . PHE A 1 201 ? -4.231  15.498  14.1    1   18.24  ? 201  PHE A CD2   1 1 
ATOM   1657 C  CE1   . PHE A 1 201 ? -2.958  16.75   11.997  1   19.13  ? 201  PHE A CE1   1 1 
ATOM   1658 C  CE2   . PHE A 1 201 ? -3.038  14.979  13.586  1   18.61  ? 201  PHE A CE2   1 1 
ATOM   1659 C  CZ    . PHE A 1 201 ? -2.41   15.603  12.537  1   18.58  ? 201  PHE A CZ    1 1 
ATOM   1660 N  N     . ASP A 1 202 ? -7.047  15.021  11.731  1   20.19  ? 202  ASP A N     1 1 
ATOM   1661 C  CA    . ASP A 1 202 ? -7.263  13.611  11.411  1   19.68  ? 202  ASP A CA    1 1 
ATOM   1662 C  C     . ASP A 1 202 ? -6.037  12.863  11.946  1   18.87  ? 202  ASP A C     1 1 
ATOM   1663 O  O     . ASP A 1 202 ? -4.954  13.025  11.405  1   17.44  ? 202  ASP A O     1 1 
ATOM   1664 C  CB    . ASP A 1 202 ? -7.408  13.466  9.887   1   20.84  ? 202  ASP A CB    1 1 
ATOM   1665 C  CG    . ASP A 1 202 ? -7.824  12.1    9.414   1   25.41  ? 202  ASP A CG    1 1 
ATOM   1666 O  OD1   . ASP A 1 202 ? -7.579  11.124  10.145  1   26.62  ? 202  ASP A OD1   1 1 
ATOM   1667 O  OD2   . ASP A 1 202 ? -8.358  12.001  8.288   1   26.63  ? 202  ASP A OD2   1 1 
ATOM   1668 N  N     . GLU A 1 203 ? -6.194  12.062  13.016  1   19.29  ? 203  GLU A N     1 1 
ATOM   1669 C  CA    . GLU A 1 203 ? -5.059  11.345  13.6    1   20     ? 203  GLU A CA    1 1 
ATOM   1670 C  C     . GLU A 1 203 ? -4.444  10.32   12.66   1   19.8   ? 203  GLU A C     1 1 
ATOM   1671 O  O     . GLU A 1 203 ? -3.338  9.898   12.929  1   21.56  ? 203  GLU A O     1 1 
ATOM   1672 C  CB    . GLU A 1 203 ? -5.407  10.725  14.953  1   23.46  ? 203  GLU A CB    1 1 
ATOM   1673 C  CG    . GLU A 1 203 ? -5.633  11.801  15.989  1   29.57  ? 203  GLU A CG    1 1 
ATOM   1674 C  CD    . GLU A 1 203 ? -6.144  11.339  17.338  1   35.78  ? 203  GLU A CD    1 1 
ATOM   1675 O  OE1   . GLU A 1 203 ? -6.043  10.127  17.626  1   34.8   ? 203  GLU A OE1   1 1 
ATOM   1676 O  OE2   . GLU A 1 203 ? -6.614  12.199  18.12   1   38.73  ? 203  GLU A OE2   1 1 
ATOM   1677 N  N     . THR A 1 204 ? -5.097  9.97    11.533  1   18.27  ? 204  THR A N     1 1 
ATOM   1678 C  CA    . THR A 1 204 ? -4.446  9.105   10.541  1   17.61  ? 204  THR A CA    1 1 
ATOM   1679 C  C     . THR A 1 204 ? -3.328  9.857   9.757   1   17.93  ? 204  THR A C     1 1 
ATOM   1680 O  O     . THR A 1 204 ? -2.646  9.252   8.946   1   18.44  ? 204  THR A O     1 1 
ATOM   1681 C  CB    . THR A 1 204 ? -5.427  8.405   9.634   1   17.6   ? 204  THR A CB    1 1 
ATOM   1682 O  OG1   . THR A 1 204 ? -6.058  9.392   8.82    1   19.36  ? 204  THR A OG1   1 1 
ATOM   1683 C  CG2   . THR A 1 204 ? -6.415  7.59    10.409  1   17.02  ? 204  THR A CG2   1 1 
ATOM   1684 N  N     . ILE A 1 205 ? -3.135  11.151  10.009  1   17.35  ? 205  ILE A N     1 1 
ATOM   1685 C  CA    . ILE A 1 205 ? -2.032  11.922  9.425   1   17.45  ? 205  ILE A CA    1 1 
ATOM   1686 C  C     . ILE A 1 205 ? -0.695  11.498  10.089  1   18.12  ? 205  ILE A C     1 1 
ATOM   1687 O  O     . ILE A 1 205 ? 0.362   11.529  9.431   1   18.82  ? 205  ILE A O     1 1 
ATOM   1688 C  CB    . ILE A 1 205 ? -2.313  13.436  9.584   1   17.17  ? 205  ILE A CB    1 1 
ATOM   1689 C  CG1   . ILE A 1 205 ? -3.495  13.894  8.691   1   17     ? 205  ILE A CG1   1 1 
ATOM   1690 C  CG2   . ILE A 1 205 ? -1.072  14.279  9.336   1   17.48  ? 205  ILE A CG2   1 1 
ATOM   1691 C  CD1   . ILE A 1 205 ? -4.001  15.263  8.964   1   17.82  ? 205  ILE A CD1   1 1 
ATOM   1692 N  N     . PHE A 1 206 ? -0.726  11.094  11.382  1   17.68  ? 206  PHE A N     1 1 
ATOM   1693 C  CA    . PHE A 1 206 ? 0.489   10.661  12.074  1   18.41  ? 206  PHE A CA    1 1 
ATOM   1694 C  C     . PHE A 1 206 ? 1.153   9.488   11.351  1   19.06  ? 206  PHE A C     1 1 
ATOM   1695 O  O     . PHE A 1 206 ? 0.489   8.497   10.998  1   17.38  ? 206  PHE A O     1 1 
ATOM   1696 C  CB    . PHE A 1 206 ? 0.19    10.284  13.51   1   18.35  ? 206  PHE A CB    1 1 
ATOM   1697 C  CG    . PHE A 1 206 ? -0.272  11.435  14.354  1   18.98  ? 206  PHE A CG    1 1 
ATOM   1698 C  CD1   . PHE A 1 206 ? 0.417   12.63   14.353  1   19.88  ? 206  PHE A CD1   1 1 
ATOM   1699 C  CD2   . PHE A 1 206 ? -1.343  11.292  15.218  1   19.15  ? 206  PHE A CD2   1 1 
ATOM   1700 C  CE1   . PHE A 1 206 ? 0.015   13.668  15.171  1   20.4   ? 206  PHE A CE1   1 1 
ATOM   1701 C  CE2   . PHE A 1 206 ? -1.731  12.325  16.044  1   19.27  ? 206  PHE A CE2   1 1 
ATOM   1702 C  CZ    . PHE A 1 206 ? -1.057  13.505  16.015  1   19.52  ? 206  PHE A CZ    1 1 
ATOM   1703 N  N     . ALA A 1 207 ? 2.449   9.649   11.057  1   20.52  ? 207  ALA A N     1 1 
ATOM   1704 C  CA    . ALA A 1 207 ? 3.187   8.668   10.286  1   23     ? 207  ALA A CA    1 1 
ATOM   1705 C  C     . ALA A 1 207 ? 3.735   7.512   11.139  1   26.22  ? 207  ALA A C     1 1 
ATOM   1706 O  O     . ALA A 1 207 ? 4.943   7.186   11.038  1   28.97  ? 207  ALA A O     1 1 
ATOM   1707 C  CB    . ALA A 1 207 ? 4.302   9.356   9.509   1   22.9   ? 207  ALA A CB    1 1 
ATOM   1708 N  N     . ASP A 1 208 ? 4.198   3.952   12.186  1   20.9   ? 209  ASP A N     1 1 
ATOM   1709 C  CA    . ASP A 1 208 ? 5.221   3.03    11.72   1   20.98  ? 209  ASP A CA    1 1 
ATOM   1710 C  C     . ASP A 1 208 ? 5.572   3.224   10.241  1   20.14  ? 209  ASP A C     1 1 
ATOM   1711 O  O     . ASP A 1 208 ? 6.481   2.557   9.791   1   20.38  ? 209  ASP A O     1 1 
ATOM   1712 C  CB    . ASP A 1 208 ? 4.838   1.565   12.038  1   22.15  ? 209  ASP A CB    1 1 
ATOM   1713 N  N     . ASP A 1 209 ? 4.914   4.147   9.501   1   19.23  ? 210  ASP A N     1 1 
ATOM   1714 C  CA    . ASP A 1 209 ? 5.21    4.324   8.077   1   18.99  ? 210  ASP A CA    1 1 
ATOM   1715 C  C     . ASP A 1 209 ? 6.641   4.792   7.756   1   18.74  ? 210  ASP A C     1 1 
ATOM   1716 O  O     . ASP A 1 209 ? 7.197   4.364   6.74    1   18.88  ? 210  ASP A O     1 1 
ATOM   1717 C  CB    . ASP A 1 209 ? 4.193   5.246   7.415   1   20.91  ? 210  ASP A CB    1 1 
ATOM   1718 C  CG    . ASP A 1 209 ? 2.834   4.61    7.162   1   24.7   ? 210  ASP A CG    1 1 
ATOM   1719 O  OD1   . ASP A 1 209 ? 2.746   3.37    7.166   1   25.23  ? 210  ASP A OD1   1 1 
ATOM   1720 O  OD2   . ASP A 1 209 ? 1.868   5.354   6.953   1   26.11  ? 210  ASP A OD2   1 1 
ATOM   1721 N  N     . ILE A 1 210 ? 7.252   5.645   8.618   1   17.87  ? 211  ILE A N     1 1 
ATOM   1722 C  CA    . ILE A 1 210 ? 8.618   6.129   8.405   1   17.48  ? 211  ILE A CA    1 1 
ATOM   1723 C  C     . ILE A 1 210 ? 9.623   5.004   8.664   1   18.13  ? 211  ILE A C     1 1 
ATOM   1724 O  O     . ILE A 1 210 ? 10.537  4.777   7.856   1   18.16  ? 211  ILE A O     1 1 
ATOM   1725 C  CB    . ILE A 1 210 ? 8.915   7.405   9.237   1   17.95  ? 211  ILE A CB    1 1 
ATOM   1726 C  CG1   . ILE A 1 210 ? 8.174   8.634   8.632   1   18.6   ? 211  ILE A CG1   1 1 
ATOM   1727 C  CG2   . ILE A 1 210 ? 10.445  7.68    9.359   1   18.38  ? 211  ILE A CG2   1 1 
ATOM   1728 C  CD1   . ILE A 1 210 ? 8.649   8.997   7.219   1   19.36  ? 211  ILE A CD1   1 1 
ATOM   1729 N  N     . ALA A 1 211 ? 9.408   4.231   9.746   1   17.29  ? 212  ALA A N     1 1 
ATOM   1730 C  CA    . ALA A 1 211 ? 10.287  3.111   10.04   1   16.16  ? 212  ALA A CA    1 1 
ATOM   1731 C  C     . ALA A 1 211 ? 10.137  2.046   8.937   1   15.24  ? 212  ALA A C     1 1 
ATOM   1732 O  O     . ALA A 1 211 ? 11.132  1.533   8.462   1   14.12  ? 212  ALA A O     1 1 
ATOM   1733 C  CB    . ALA A 1 211 ? 9.965   2.537   11.398  1   15.92  ? 212  ALA A CB    1 1 
ATOM   1734 N  N     . ASP A 1 212 ? 8.915   1.823   8.439   1   15.95  ? 213  ASP A N     1 1 
ATOM   1735 C  CA    . ASP A 1 212 ? 8.674   0.867   7.357   1   16.69  ? 213  ASP A CA    1 1 
ATOM   1736 C  C     . ASP A 1 212 ? 9.402   1.303   6.098   1   15.48  ? 213  ASP A C     1 1 
ATOM   1737 O  O     . ASP A 1 212 ? 10.02   0.469   5.439   1   14.9   ? 213  ASP A O     1 1 
ATOM   1738 C  CB    . ASP A 1 212 ? 7.184   0.744   7.039   1   20.38  ? 213  ASP A CB    1 1 
ATOM   1739 C  CG    . ASP A 1 212 ? 6.364   -0.028  8.045   1   27.45  ? 213  ASP A CG    1 1 
ATOM   1740 O  OD1   . ASP A 1 212 ? 6.954   -0.586  8.995   1   28.4   ? 213  ASP A OD1   1 1 
ATOM   1741 O  OD2   . ASP A 1 212 ? 5.139   -0.043  7.905   1   31.98  ? 213  ASP A OD2   1 1 
ATOM   1742 N  N     . TYR A 1 213 ? 9.345   2.601   5.779   1   14.35  ? 214  TYR A N     1 1 
ATOM   1743 C  CA    . TYR A 1 213 ? 10.009  3.139   4.602   1   15.08  ? 214  TYR A CA    1 1 
ATOM   1744 C  C     . TYR A 1 213 ? 11.525  2.966   4.697   1   14.54  ? 214  TYR A C     1 1 
ATOM   1745 O  O     . TYR A 1 213 ? 12.151  2.461   3.753   1   13.69  ? 214  TYR A O     1 1 
ATOM   1746 C  CB    . TYR A 1 213 ? 9.641   4.636   4.416   1   15.98  ? 214  TYR A CB    1 1 
ATOM   1747 C  CG    . TYR A 1 213 ? 10.412  5.291   3.302   1   16.71  ? 214  TYR A CG    1 1 
ATOM   1748 C  CD1   . TYR A 1 213 ? 10.092  5.045   1.974   1   17.56  ? 214  TYR A CD1   1 1 
ATOM   1749 C  CD2   . TYR A 1 213 ? 11.526  6.082   3.57    1   17.61  ? 214  TYR A CD2   1 1 
ATOM   1750 C  CE1   . TYR A 1 213 ? 10.787  5.661   0.942   1   18.64  ? 214  TYR A CE1   1 1 
ATOM   1751 C  CE2   . TYR A 1 213 ? 12.239  6.689   2.549   1   18.09  ? 214  TYR A CE2   1 1 
ATOM   1752 C  CZ    . TYR A 1 213 ? 11.878  6.462   1.235   1   19.48  ? 214  TYR A CZ    1 1 
ATOM   1753 O  OH    . TYR A 1 213 ? 12.599  7.032   0.224   1   21.2   ? 214  TYR A OH    1 1 
ATOM   1754 N  N     . ILE A 1 214 ? 12.116  3.342   5.847   1   15.19  ? 215  ILE A N     1 1 
ATOM   1755 C  CA    . ILE A 1 214 ? 13.566  3.214   6.067   1   15.73  ? 215  ILE A CA    1 1 
ATOM   1756 C  C     . ILE A 1 214 ? 14.017  1.772   5.911   1   17.54  ? 215  ILE A C     1 1 
ATOM   1757 O  O     . ILE A 1 214 ? 14.971  1.516   5.169   1   17.9   ? 215  ILE A O     1 1 
ATOM   1758 C  CB    . ILE A 1 214 ? 13.967  3.785   7.434   1   15.71  ? 215  ILE A CB    1 1 
ATOM   1759 C  CG1   . ILE A 1 214 ? 13.806  5.325   7.448   1   17.06  ? 215  ILE A CG1   1 1 
ATOM   1760 C  CG2   . ILE A 1 214 ? 15.384  3.327   7.877   1   15.9   ? 215  ILE A CG2   1 1 
ATOM   1761 C  CD1   . ILE A 1 214 ? 14.055  5.977   8.776   1   17.78  ? 215  ILE A CD1   1 1 
ATOM   1762 N  N     . ILE A 1 215 ? 13.31   0.822   6.572   1   17.73  ? 216  ILE A N     1 1 
ATOM   1763 C  CA    . ILE A 1 215 ? 13.664  -0.587  6.512   1   18.1   ? 216  ILE A CA    1 1 
ATOM   1764 C  C     . ILE A 1 215 ? 13.513  -1.139  5.097   1   17.72  ? 216  ILE A C     1 1 
ATOM   1765 O  O     . ILE A 1 215 ? 14.36   -1.914  4.667   1   17.07  ? 216  ILE A O     1 1 
ATOM   1766 C  CB    . ILE A 1 215 ? 12.84   -1.385  7.557   1   19.06  ? 216  ILE A CB    1 1 
ATOM   1767 C  CG1   . ILE A 1 215 ? 13.328  -1.005  8.967   1   21.02  ? 216  ILE A CG1   1 1 
ATOM   1768 C  CG2   . ILE A 1 215 ? 12.941  -2.917  7.313   1   18.3   ? 216  ILE A CG2   1 1 
ATOM   1769 C  CD1   . ILE A 1 215 ? 12.499  -1.445  10.016  1   22.35  ? 216  ILE A CD1   1 1 
ATOM   1770 N  N     . ALA A 1 216 ? 12.456  -0.72   4.356   1   17.27  ? 217  ALA A N     1 1 
ATOM   1771 C  CA    . ALA A 1 216 ? 12.287  -1.209  2.987   1   17.41  ? 217  ALA A CA    1 1 
ATOM   1772 C  C     . ALA A 1 216 ? 13.419  -0.681  2.072   1   18.09  ? 217  ALA A C     1 1 
ATOM   1773 O  O     . ALA A 1 216 ? 13.919  -1.438  1.222   1   18.18  ? 217  ALA A O     1 1 
ATOM   1774 C  CB    . ALA A 1 216 ? 10.914  -0.844  2.442   1   16.75  ? 217  ALA A CB    1 1 
ATOM   1775 N  N     . LYS A 1 217 ? 13.895  0.563   2.326   1   17.69  ? 218  LYS A N     1 1 
ATOM   1776 C  CA    . LYS A 1 217 ? 15.019  1.146   1.578   1   18.01  ? 218  LYS A CA    1 1 
ATOM   1777 C  C     . LYS A 1 217 ? 16.3    0.416   1.904   1   18.7   ? 218  LYS A C     1 1 
ATOM   1778 O  O     . LYS A 1 217 ? 17.017  0.046   0.977   1   19.85  ? 218  LYS A O     1 1 
ATOM   1779 C  CB    . LYS A 1 217 ? 15.192  2.664   1.832   1   18.19  ? 218  LYS A CB    1 1 
ATOM   1780 C  CG    . LYS A 1 217 ? 14.041  3.501   1.306   1   21.91  ? 218  LYS A CG    1 1 
ATOM   1781 C  CD    . LYS A 1 217 ? 13.932  3.455   -0.19   1   24.83  ? 218  LYS A CD    1 1 
ATOM   1782 C  CE    . LYS A 1 217 ? 14.843  4.411   -0.878  1   26.89  ? 218  LYS A CE    1 1 
ATOM   1783 N  NZ    . LYS A 1 217 ? 14.249  4.815   -2.176  1   28.84  ? 218  LYS A NZ    1 1 
ATOM   1784 N  N     . LEU A 1 218 ? 16.539  0.113   3.2     1   17.87  ? 219  LEU A N     1 1 
ATOM   1785 C  CA    . LEU A 1 218 ? 17.7    -0.659  3.654   1   17.14  ? 219  LEU A CA    1 1 
ATOM   1786 C  C     . LEU A 1 218 ? 17.728  -2.04   3.028   1   18.07  ? 219  LEU A C     1 1 
ATOM   1787 O  O     . LEU A 1 218 ? 18.799  -2.532  2.68    1   18.58  ? 219  LEU A O     1 1 
ATOM   1788 C  CB    . LEU A 1 218 ? 17.741  -0.758  5.187   1   16.47  ? 219  LEU A CB    1 1 
ATOM   1789 C  CG    . LEU A 1 218 ? 17.953  0.584   5.94    1   17.87  ? 219  LEU A CG    1 1 
ATOM   1790 C  CD1   . LEU A 1 218 ? 17.903  0.4     7.446   1   18.31  ? 219  LEU A CD1   1 1 
ATOM   1791 C  CD2   . LEU A 1 218 ? 19.227  1.262   5.529   1   17.39  ? 219  LEU A CD2   1 1 
ATOM   1792 N  N     . GLN A 1 219 ? 16.546  -2.67   2.872   1   17.69  ? 220  GLN A N     1 1 
ATOM   1793 C  CA    . GLN A 1 219 ? 16.411  -3.975  2.25    1   17.77  ? 220  GLN A CA    1 1 
ATOM   1794 C  C     . GLN A 1 219 ? 16.429  -3.953  0.721   1   19.64  ? 220  GLN A C     1 1 
ATOM   1795 O  O     . GLN A 1 219 ? 16.327  -5.015  0.121   1   20.41  ? 220  GLN A O     1 1 
ATOM   1796 C  CB    . GLN A 1 219 ? 15.116  -4.665  2.716   1   17.61  ? 220  GLN A CB    1 1 
ATOM   1797 C  CG    . GLN A 1 219 ? 15.07   -5.001  4.192   1   19.7   ? 220  GLN A CG    1 1 
ATOM   1798 C  CD    . GLN A 1 219 ? 15.814  -6.274  4.506   1   24.82  ? 220  GLN A CD    1 1 
ATOM   1799 O  OE1   . GLN A 1 219 ? 16.772  -6.661  3.812   1   28.11  ? 220  GLN A OE1   1 1 
ATOM   1800 N  NE2   . GLN A 1 219 ? 15.381  -6.963  5.557   1   23.47  ? 220  GLN A NE2   1 1 
ATOM   1801 N  N     . HIS A 1 220 ? 16.506  -2.777  0.085   1   20.97  ? 221  HIS A N     1 1 
ATOM   1802 C  CA    . HIS A 1 220 ? 16.461  -2.635  -1.372  1   22.53  ? 221  HIS A CA    1 1 
ATOM   1803 C  C     . HIS A 1 220 ? 15.147  -3.221  -1.923  1   20.82  ? 221  HIS A C     1 1 
ATOM   1804 O  O     . HIS A 1 220 ? 15.139  -3.902  -2.948  1   20.13  ? 221  HIS A O     1 1 
ATOM   1805 C  CB    . HIS A 1 220 ? 17.72   -3.23   -2.061  1   26.95  ? 221  HIS A CB    1 1 
ATOM   1806 C  CG    . HIS A 1 220 ? 17.859  -2.827  -3.5    1   34.55  ? 221  HIS A CG    1 1 
ATOM   1807 N  ND1   . HIS A 1 220 ? 17.963  -1.499  -3.865  1   37.75  ? 221  HIS A ND1   1 1 
ATOM   1808 C  CD2   . HIS A 1 220 ? 17.84   -3.589  -4.623  1   37.16  ? 221  HIS A CD2   1 1 
ATOM   1809 C  CE1   . HIS A 1 220 ? 18.015  -1.489  -5.19   1   38.89  ? 221  HIS A CE1   1 1 
ATOM   1810 N  NE2   . HIS A 1 220 ? 17.948  -2.72   -5.694  1   38.88  ? 221  HIS A NE2   1 1 
ATOM   1811 N  N     . ARG A 1 221 ? 14.036  -2.967  -1.208  1   19.98  ? 222  ARG A N     1 1 
ATOM   1812 C  CA    . ARG A 1 221 ? 12.709  -3.415  -1.61   1   20.43  ? 222  ARG A CA    1 1 
ATOM   1813 C  C     . ARG A 1 221 ? 11.909  -2.271  -2.258  1   21.48  ? 222  ARG A C     1 1 
ATOM   1814 O  O     . ARG A 1 221 ? 12.302  -1.103  -2.182  1   21.98  ? 222  ARG A O     1 1 
ATOM   1815 C  CB    . ARG A 1 221 ? 11.949  -4.025  -0.413  1   20.08  ? 222  ARG A CB    1 1 
ATOM   1816 C  CG    . ARG A 1 221 ? 12.538  -5.35   0.01    1   20.85  ? 222  ARG A CG    1 1 
ATOM   1817 C  CD    . ARG A 1 221 ? 11.958  -5.899  1.285   1   21.74  ? 222  ARG A CD    1 1 
ATOM   1818 N  NE    . ARG A 1 221 ? 12.656  -7.131  1.65    1   24.49  ? 222  ARG A NE    1 1 
ATOM   1819 C  CZ    . ARG A 1 221 ? 12.604  -7.703  2.847   1   25.23  ? 222  ARG A CZ    1 1 
ATOM   1820 N  NH1   . ARG A 1 221 ? 11.871  -7.166  3.815   1   26.23  ? 222  ARG A NH1   1 1 
ATOM   1821 N  NH2   . ARG A 1 221 ? 13.269  -8.823  3.08    1   23.75  ? 222  ARG A NH2   1 1 
ATOM   1822 N  N     . ASP A 1 222 ? 10.809  -2.62   -2.921  1   22.07  ? 223  ASP A N     1 1 
ATOM   1823 C  CA    . ASP A 1 222 ? 9.921   -1.662  -3.56   1   22.51  ? 223  ASP A CA    1 1 
ATOM   1824 C  C     . ASP A 1 222 ? 9.202   -0.834  -2.469  1   22.32  ? 223  ASP A C     1 1 
ATOM   1825 O  O     . ASP A 1 222 ? 8.501   -1.381  -1.61   1   22.67  ? 223  ASP A O     1 1 
ATOM   1826 C  CB    . ASP A 1 222 ? 8.926   -2.423  -4.461  1   24.59  ? 223  ASP A CB    1 1 
ATOM   1827 C  CG    . ASP A 1 222 ? 7.892   -1.586  -5.213  1   31.69  ? 223  ASP A CG    1 1 
ATOM   1828 O  OD1   . ASP A 1 222 ? 6.933   -2.179  -5.753  1   35.46  ? 223  ASP A OD1   1 1 
ATOM   1829 O  OD2   . ASP A 1 222 ? 8.032   -0.349  -5.251  1   31.8   ? 223  ASP A OD2   1 1 
ATOM   1830 N  N     . THR A 1 223 ? 9.392   0.476   -2.502  1   21.36  ? 224  THR A N     1 1 
ATOM   1831 C  CA    . THR A 1 223 ? 8.779   1.374   -1.531  1   22     ? 224  THR A CA    1 1 
ATOM   1832 C  C     . THR A 1 223 ? 7.643   2.217   -2.109  1   22.39  ? 224  THR A C     1 1 
ATOM   1833 O  O     . THR A 1 223 ? 7.158   3.081   -1.393  1   22.02  ? 224  THR A O     1 1 
ATOM   1834 C  CB    . THR A 1 223 ? 9.845   2.313   -0.912  1   23.21  ? 224  THR A CB    1 1 
ATOM   1835 O  OG1   . THR A 1 223 ? 10.547  3.019   -1.948  1   23.34  ? 224  THR A OG1   1 1 
ATOM   1836 C  CG2   . THR A 1 223 ? 10.847  1.562   -0.06   1   23.89  ? 224  THR A CG2   1 1 
ATOM   1837 N  N     . SER A 1 224 ? 7.241   2.015   -3.384  1   23.04  ? 225  SER A N     1 1 
ATOM   1838 C  CA    . SER A 1 224 ? 6.17    2.804   -4.042  1   23.89  ? 225  SER A CA    1 1 
ATOM   1839 C  C     . SER A 1 224 ? 4.895   2.904   -3.222  1   22.87  ? 225  SER A C     1 1 
ATOM   1840 O  O     . SER A 1 224 ? 4.311   3.973   -3.119  1   23.36  ? 225  SER A O     1 1 
ATOM   1841 C  CB    . SER A 1 224 ? 5.801   2.195   -5.395  1   27.98  ? 225  SER A CB    1 1 
ATOM   1842 O  OG    . SER A 1 224 ? 6.924   1.984   -6.234  1   34.18  ? 225  SER A OG    1 1 
ATOM   1843 N  N     . ASN A 1 225 ? 4.451   1.788   -2.652  1   22.28  ? 226  ASN A N     1 1 
ATOM   1844 C  CA    . ASN A 1 225 ? 3.209   1.753   -1.91   1   21.73  ? 226  ASN A CA    1 1 
ATOM   1845 C  C     . ASN A 1 225 ? 3.33    2.477   -0.57   1   19.64  ? 226  ASN A C     1 1 
ATOM   1846 O  O     . ASN A 1 225 ? 2.415   3.213   -0.219  1   19.48  ? 226  ASN A O     1 1 
ATOM   1847 C  CB    . ASN A 1 225 ? 2.703   0.302   -1.796  1   24.05  ? 226  ASN A CB    1 1 
ATOM   1848 C  CG    . ASN A 1 225 ? 2.355   -0.262  -3.16   1   29.79  ? 226  ASN A CG    1 1 
ATOM   1849 O  OD1   . ASN A 1 225 ? 1.894   0.447   -4.063  1   31.34  ? 226  ASN A OD1   1 1 
ATOM   1850 N  ND2   . ASN A 1 225 ? 2.556   -1.552  -3.353  1   33.18  ? 226  ASN A ND2   1 1 
ATOM   1851 N  N     . ILE A 1 226 ? 4.442   2.302   0.164   1   17.97  ? 227  ILE A N     1 1 
ATOM   1852 C  CA    . ILE A 1 226 ? 4.689   3.032   1.423   1   17.65  ? 227  ILE A CA    1 1 
ATOM   1853 C  C     . ILE A 1 226 ? 4.815   4.546   1.114   1   16.99  ? 227  ILE A C     1 1 
ATOM   1854 O  O     . ILE A 1 226 ? 4.327   5.376   1.878   1   17.23  ? 227  ILE A O     1 1 
ATOM   1855 C  CB    . ILE A 1 226 ? 5.957   2.499   2.17    1   18.13  ? 227  ILE A CB    1 1 
ATOM   1856 C  CG1   . ILE A 1 226 ? 5.812   0.994   2.482   1   19.76  ? 227  ILE A CG1   1 1 
ATOM   1857 C  CG2   . ILE A 1 226 ? 6.172   3.268   3.461   1   18.24  ? 227  ILE A CG2   1 1 
ATOM   1858 C  CD1   . ILE A 1 226 ? 7.149   0.248   2.858   1   20.74  ? 227  ILE A CD1   1 1 
ATOM   1859 N  N     . GLU A 1 227 ? 5.428   4.908   -0.033  1   16.6   ? 228  GLU A N     1 1 
ATOM   1860 C  CA    . GLU A 1 227 ? 5.567   6.317   -0.456  1   16.77  ? 228  GLU A CA    1 1 
ATOM   1861 C  C     . GLU A 1 227 ? 4.189   6.923   -0.635  1   18.27  ? 228  GLU A C     1 1 
ATOM   1862 O  O     . GLU A 1 227 ? 3.956   8.018   -0.137  1   19.53  ? 228  GLU A O     1 1 
ATOM   1863 C  CB    . GLU A 1 227 ? 6.356   6.43    -1.772  1   17.22  ? 228  GLU A CB    1 1 
ATOM   1864 C  CG    . GLU A 1 227 ? 7.849   6.155   -1.609  1   21.96  ? 228  GLU A CG    1 1 
ATOM   1865 C  CD    . GLU A 1 227 ? 8.628   5.986   -2.902  1   25.54  ? 228  GLU A CD    1 1 
ATOM   1866 O  OE1   . GLU A 1 227 ? 8.199   6.521   -3.949  1   27.66  ? 228  GLU A OE1   1 1 
ATOM   1867 O  OE2   . GLU A 1 227 ? 9.681   5.314   -2.867  1   25.65  ? 228  GLU A OE2   1 1 
ATOM   1868 N  N     . GLN A 1 228 ? 3.258   6.199   -1.304  1   18.12  ? 229  GLN A N     1 1 
ATOM   1869 C  CA    . GLN A 1 228 ? 1.906   6.7     -1.498  1   18.89  ? 229  GLN A CA    1 1 
ATOM   1870 C  C     . GLN A 1 228 ? 1.168   6.937   -0.194  1   19.1   ? 229  GLN A C     1 1 
ATOM   1871 O  O     . GLN A 1 228 ? 0.479   7.945   -0.076  1   19.79  ? 229  GLN A O     1 1 
ATOM   1872 C  CB    . GLN A 1 228 ? 1.059   5.809   -2.436  1   20.88  ? 229  GLN A CB    1 1 
ATOM   1873 C  CG    . GLN A 1 228 ? -0.218  6.529   -2.926  1   25.68  ? 229  GLN A CG    1 1 
ATOM   1874 C  CD    . GLN A 1 228 ? 0.107   7.814   -3.662  1   31.7   ? 229  GLN A CD    1 1 
ATOM   1875 O  OE1   . GLN A 1 228 ? 0.732   7.794   -4.73   1   35.09  ? 229  GLN A OE1   1 1 
ATOM   1876 N  NE2   . GLN A 1 228 ? -0.271  8.969   -3.1    1   30.9   ? 229  GLN A NE2   1 1 
ATOM   1877 N  N     . LEU A 1 229 ? 1.334   6.06    0.797   1   18.2   ? 230  LEU A N     1 1 
ATOM   1878 C  CA    . LEU A 1 229 ? 0.675   6.25    2.09    1   17.96  ? 230  LEU A CA    1 1 
ATOM   1879 C  C     . LEU A 1 229 ? 1.199   7.503   2.77    1   17.61  ? 230  LEU A C     1 1 
ATOM   1880 O  O     . LEU A 1 229 ? 0.414   8.248   3.336   1   18.07  ? 230  LEU A O     1 1 
ATOM   1881 C  CB    . LEU A 1 229 ? 0.854   5.033   3.01    1   17.89  ? 230  LEU A CB    1 1 
ATOM   1882 C  CG    . LEU A 1 229 ? 0.34    3.682   2.481   1   18.34  ? 230  LEU A CG    1 1 
ATOM   1883 C  CD1   . LEU A 1 229 ? 0.609   2.564   3.492   1   18.61  ? 230  LEU A CD1   1 1 
ATOM   1884 C  CD2   . LEU A 1 229 ? -1.131  3.741   2.164   1   19.03  ? 230  LEU A CD2   1 1 
ATOM   1885 N  N     . LEU A 1 230 ? 2.501   7.776   2.66    1   17     ? 231  LEU A N     1 1 
ATOM   1886 C  CA    . LEU A 1 230 ? 3.11    8.967   3.251   1   17.27  ? 231  LEU A CA    1 1 
ATOM   1887 C  C     . LEU A 1 230 ? 2.686   10.231  2.522   1   17.93  ? 231  LEU A C     1 1 
ATOM   1888 O  O     . LEU A 1 230 ? 2.412   11.226  3.178   1   18.02  ? 231  LEU A O     1 1 
ATOM   1889 C  CB    . LEU A 1 230 ? 4.641   8.849   3.301   1   17.02  ? 231  LEU A CB    1 1 
ATOM   1890 C  CG    . LEU A 1 230 ? 5.14    7.893   4.375   1   18.67  ? 231  LEU A CG    1 1 
ATOM   1891 C  CD1   . LEU A 1 230 ? 6.604   7.51    4.136   1   19.93  ? 231  LEU A CD1   1 1 
ATOM   1892 C  CD2   . LEU A 1 230 ? 4.938   8.484   5.759   1   18.51  ? 231  LEU A CD2   1 1 
ATOM   1893 N  N     . ILE A 1 231 ? 2.581   10.186  1.179   1   18.64  ? 232  ILE A N     1 1 
ATOM   1894 C  CA    . ILE A 1 231 ? 2.116   11.337  0.374   1   19.82  ? 232  ILE A CA    1 1 
ATOM   1895 C  C     . ILE A 1 231 ? 0.655   11.667  0.743   1   18.43  ? 232  ILE A C     1 1 
ATOM   1896 O  O     . ILE A 1 231 ? 0.294   12.844  0.884   1   17.32  ? 232  ILE A O     1 1 
ATOM   1897 C  CB    . ILE A 1 231 ? 2.228   11.035  -1.152  1   21.88  ? 232  ILE A CB    1 1 
ATOM   1898 C  CG1   . ILE A 1 231 ? 3.685   10.748  -1.583  1   23.74  ? 232  ILE A CG1   1 1 
ATOM   1899 C  CG2   . ILE A 1 231 ? 1.607   12.153  -1.992  1   22.49  ? 232  ILE A CG2   1 1 
ATOM   1900 C  CD1   . ILE A 1 231 ? 4.598   11.833  -1.292  1   26.4   ? 232  ILE A CD1   1 1 
ATOM   1901 N  N     . ASN A 1 232 ? -0.166  10.604  0.934   1   17.81  ? 233  ASN A N     1 1 
ATOM   1902 C  CA    . ASN A 1 232 ? -1.562  10.735  1.333   1   17.43  ? 233  ASN A CA    1 1 
ATOM   1903 C  C     . ASN A 1 232 ? -1.688  11.466  2.677   1   16.63  ? 233  ASN A C     1 1 
ATOM   1904 O  O     . ASN A 1 232 ? -2.505  12.36   2.795   1   17     ? 233  ASN A O     1 1 
ATOM   1905 C  CB    . ASN A 1 232 ? -2.238  9.374   1.344   1   19.77  ? 233  ASN A CB    1 1 
ATOM   1906 C  CG    . ASN A 1 232 ? -2.513  8.844   -0.053  1   24.06  ? 233  ASN A CG    1 1 
ATOM   1907 O  OD1   . ASN A 1 232 ? -2.312  9.534   -1.07   1   26.79  ? 233  ASN A OD1   1 1 
ATOM   1908 N  ND2   . ASN A 1 232 ? -2.976  7.616   -0.134  1   23.83  ? 233  ASN A ND2   1 1 
ATOM   1909 N  N     . LYS A 1 233 ? -0.808  11.175  3.637   1   16.01  ? 234  LYS A N     1 1 
ATOM   1910 C  CA    . LYS A 1 233 ? -0.814  11.851  4.93    1   15.78  ? 234  LYS A CA    1 1 
ATOM   1911 C  C     . LYS A 1 233 ? -0.377  13.322  4.817   1   16.26  ? 234  LYS A C     1 1 
ATOM   1912 O  O     . LYS A 1 233 ? -0.944  14.205  5.48    1   15.83  ? 234  LYS A O     1 1 
ATOM   1913 C  CB    . LYS A 1 233 ? 0.078   11.077  5.898   1   16.36  ? 234  LYS A CB    1 1 
ATOM   1914 C  CG    . LYS A 1 233 ? -0.574  9.759   6.274   1   17.37  ? 234  LYS A CG    1 1 
ATOM   1915 C  CD    . LYS A 1 233 ? 0.297   8.928   7.184   1   18.29  ? 234  LYS A CD    1 1 
ATOM   1916 C  CE    . LYS A 1 233 ? -0.379  7.604   7.472   1   18.64  ? 234  LYS A CE    1 1 
ATOM   1917 N  NZ    . LYS A 1 233 ? 0.199   6.973   8.685   1   19.21  ? 234  LYS A NZ    1 1 
ATOM   1918 N  N     . ASN A 1 234 ? 0.637   13.59   3.956   1   15.98  ? 235  ASN A N     1 1 
ATOM   1919 C  CA    . ASN A 1 234 ? 1.129   14.939  3.666   1   15.23  ? 235  ASN A CA    1 1 
ATOM   1920 C  C     . ASN A 1 234 ? -0.061  15.769  3.081   1   15.27  ? 235  ASN A C     1 1 
ATOM   1921 O  O     . ASN A 1 234 ? -0.3    16.9    3.515   1   14.96  ? 235  ASN A O     1 1 
ATOM   1922 C  CB    . ASN A 1 234 ? 2.294   14.861  2.653   1   14.98  ? 235  ASN A CB    1 1 
ATOM   1923 C  CG    . ASN A 1 234 ? 3.124   16.124  2.531   1   17.59  ? 235  ASN A CG    1 1 
ATOM   1924 O  OD1   . ASN A 1 234 ? 2.726   17.228  2.972   1   21.23  ? 235  ASN A OD1   1 1 
ATOM   1925 N  ND2   . ASN A 1 234 ? 4.294   16.01   1.928   1   14.23  ? 235  ASN A ND2   1 1 
ATOM   1926 N  N     . LEU A 1 235 ? -0.848  15.159  2.165   1   15.28  ? 236  LEU A N     1 1 
ATOM   1927 C  CA    . LEU A 1 235 ? -2.015  15.804  1.552   1   16.11  ? 236  LEU A CA    1 1 
ATOM   1928 C  C     . LEU A 1 235 ? -3.113  16.028  2.576   1   16.76  ? 236  LEU A C     1 1 
ATOM   1929 O  O     . LEU A 1 235 ? -3.747  17.081  2.559   1   17.86  ? 236  LEU A O     1 1 
ATOM   1930 C  CB    . LEU A 1 235 ? -2.544  14.948  0.396   1   16.54  ? 236  LEU A CB    1 1 
ATOM   1931 C  CG    . LEU A 1 235 ? -3.625  15.592  -0.445  1   17.71  ? 236  LEU A CG    1 1 
ATOM   1932 C  CD1   . LEU A 1 235 ? -3.077  16.798  -1.203  1   18.31  ? 236  LEU A CD1   1 1 
ATOM   1933 C  CD2   . LEU A 1 235 ? -4.283  14.565  -1.351  1   18.44  ? 236  LEU A CD2   1 1 
ATOM   1934 N  N     . LYS A 1 236 ? -3.34   15.067  3.478   1   16.69  ? 237  LYS A N     1 1 
ATOM   1935 C  CA    . LYS A 1 236 ? -4.338  15.246  4.532   1   17.77  ? 237  LYS A CA    1 1 
ATOM   1936 C  C     . LYS A 1 236 ? -3.957  16.375  5.505   1   18.17  ? 237  LYS A C     1 1 
ATOM   1937 O  O     . LYS A 1 236 ? -4.837  16.969  6.107   1   18.8   ? 237  LYS A O     1 1 
ATOM   1938 C  CB    . LYS A 1 236 ? -4.629  13.943  5.27    1   19.79  ? 237  LYS A CB    1 1 
ATOM   1939 C  CG    . LYS A 1 236 ? -5.087  12.844  4.326   1   24.62  ? 237  LYS A CG    1 1 
ATOM   1940 C  CD    . LYS A 1 236 ? -6.013  11.865  4.966   1   28.98  ? 237  LYS A CD    1 1 
ATOM   1941 C  CE    . LYS A 1 236 ? -5.343  11.029  5.986   1   31.73  ? 237  LYS A CE    1 1 
ATOM   1942 N  NZ    . LYS A 1 236 ? -6.06   9.718   6.122   1   32.26  ? 237  LYS A NZ    1 1 
ATOM   1943 N  N     . MET A 1 237 ? -2.667  16.679  5.65    1   18.4   ? 238  MET A N     1 1 
ATOM   1944 C  CA    . MET A 1 237 ? -2.224  17.807  6.473   1   17.6   ? 238  MET A CA    1 1 
ATOM   1945 C  C     . MET A 1 237 ? -2.623  19.112  5.766   1   17.55  ? 238  MET A C     1 1 
ATOM   1946 O  O     . MET A 1 237 ? -3.123  20.04   6.409   1   18.06  ? 238  MET A O     1 1 
ATOM   1947 C  CB    . MET A 1 237 ? -0.707  17.77   6.734   1   16.14  ? 238  MET A CB    1 1 
ATOM   1948 C  CG    . MET A 1 237 ? -0.187  19.047  7.439   1   17.33  ? 238  MET A CG    1 1 
ATOM   1949 S  SD    . MET A 1 237 ? -0.986  19.321  9.039   1   17.13  ? 238  MET A SD    1 1 
ATOM   1950 C  CE    . MET A 1 237 ? -0.067  18.162  10.049  1   16.89  ? 238  MET A CE    1 1 
ATOM   1951 N  N     . VAL A 1 238 ? -2.425  19.174  4.436   1   16.95  ? 239  VAL A N     1 1 
ATOM   1952 C  CA    . VAL A 1 238 ? -2.837  20.343  3.636   1   17.09  ? 239  VAL A CA    1 1 
ATOM   1953 C  C     . VAL A 1 238 ? -4.348  20.524  3.738   1   17.1   ? 239  VAL A C     1 1 
ATOM   1954 O  O     . VAL A 1 238 ? -4.815  21.643  3.84    1   17.72  ? 239  VAL A O     1 1 
ATOM   1955 C  CB    . VAL A 1 238 ? -2.385  20.165  2.168   1   17.11  ? 239  VAL A CB    1 1 
ATOM   1956 C  CG1   . VAL A 1 238 ? -2.97   21.244  1.256   1   16.85  ? 239  VAL A CG1   1 1 
ATOM   1957 C  CG2   . VAL A 1 238 ? -0.866  20.139  2.083   1   16.93  ? 239  VAL A CG2   1 1 
ATOM   1958 N  N     . GLU A 1 239 ? -5.106  19.413  3.766   1   16.64  ? 240  GLU A N     1 1 
ATOM   1959 C  CA    . GLU A 1 239 ? -6.541  19.42   3.913   1   16.86  ? 240  GLU A CA    1 1 
ATOM   1960 C  C     . GLU A 1 239 ? -6.95   20.011  5.265   1   17.71  ? 240  GLU A C     1 1 
ATOM   1961 O  O     . GLU A 1 239 ? -7.778  20.927  5.313   1   17.15  ? 240  GLU A O     1 1 
ATOM   1962 C  CB    . GLU A 1 239 ? -7.093  18.007  3.747   1   16.86  ? 240  GLU A CB    1 1 
ATOM   1963 C  CG    . GLU A 1 239 ? -8.6    17.978  3.596   1   17.36  ? 240  GLU A CG    1 1 
ATOM   1964 C  CD    . GLU A 1 239 ? -9.19   16.579  3.531   1   23.16  ? 240  GLU A CD    1 1 
ATOM   1965 O  OE1   . GLU A 1 239 ? -8.426  15.607  3.33    1   22.24  ? 240  GLU A OE1   1 1 
ATOM   1966 O  OE2   . GLU A 1 239 ? -10.421 16.453  3.702   1   26.7   ? 240  GLU A OE2   1 1 
ATOM   1967 N  N     . PHE A 1 240 ? -6.308  19.545  6.354   1   17.88  ? 241  PHE A N     1 1 
ATOM   1968 C  CA    . PHE A 1 240 ? -6.587  20.039  7.703   1   18.7   ? 241  PHE A CA    1 1 
ATOM   1969 C  C     . PHE A 1 240 ? -6.345  21.537  7.79    1   18.74  ? 241  PHE A C     1 1 
ATOM   1970 O  O     . PHE A 1 240 ? -7.164  22.266  8.352   1   19.32  ? 241  PHE A O     1 1 
ATOM   1971 C  CB    . PHE A 1 240 ? -5.703  19.31   8.736   1   19.16  ? 241  PHE A CB    1 1 
ATOM   1972 C  CG    . PHE A 1 240 ? -5.627  20      10.086  1   19.87  ? 241  PHE A CG    1 1 
ATOM   1973 C  CD1   . PHE A 1 240 ? -6.726  20.029  10.928  1   20.16  ? 241  PHE A CD1   1 1 
ATOM   1974 C  CD2   . PHE A 1 240 ? -4.441  20.596  10.519  1   20.78  ? 241  PHE A CD2   1 1 
ATOM   1975 C  CE1   . PHE A 1 240 ? -6.645  20.627  12.178  1   20.96  ? 241  PHE A CE1   1 1 
ATOM   1976 C  CE2   . PHE A 1 240 ? -4.371  21.219  11.766  1   20.9   ? 241  PHE A CE2   1 1 
ATOM   1977 C  CZ    . PHE A 1 240 ? -5.487  21.258  12.576  1   20.24  ? 241  PHE A CZ    1 1 
ATOM   1978 N  N     . LEU A 1 241 ? -5.219  21.987  7.228   1   18.19  ? 242  LEU A N     1 1 
ATOM   1979 C  CA    . LEU A 1 241 ? -4.826  23.384  7.266   1   17.87  ? 242  LEU A CA    1 1 
ATOM   1980 C  C     . LEU A 1 241 ? -5.69   24.284  6.423   1   17.53  ? 242  LEU A C     1 1 
ATOM   1981 O  O     . LEU A 1 241 ? -6.112  25.325  6.923   1   17.57  ? 242  LEU A O     1 1 
ATOM   1982 C  CB    . LEU A 1 241 ? -3.343  23.562  6.885   1   17.5   ? 242  LEU A CB    1 1 
ATOM   1983 C  CG    . LEU A 1 241 ? -2.321  22.916  7.806   1   16.96  ? 242  LEU A CG    1 1 
ATOM   1984 C  CD1   . LEU A 1 241 ? -0.911  23.113  7.259   1   16.55  ? 242  LEU A CD1   1 1 
ATOM   1985 C  CD2   . LEU A 1 241 ? -2.433  23.454  9.213   1   16.46  ? 242  LEU A CD2   1 1 
ATOM   1986 N  N     . SER A 1 242 ? -5.952  23.911  5.157   1   16.93  ? 243  SER A N     1 1 
ATOM   1987 C  CA    . SER A 1 242 ? -6.739  24.77   4.288   1   17.94  ? 243  SER A CA    1 1 
ATOM   1988 C  C     . SER A 1 242 ? -8.182  24.872  4.719   1   19.04  ? 243  SER A C     1 1 
ATOM   1989 O  O     . SER A 1 242 ? -8.762  25.939  4.592   1   20.53  ? 243  SER A O     1 1 
ATOM   1990 C  CB    . SER A 1 242 ? -6.609  24.373  2.824   1   18.7   ? 243  SER A CB    1 1 
ATOM   1991 O  OG    . SER A 1 242 ? -6.854  22.995  2.624   1   19.27  ? 243  SER A OG    1 1 
ATOM   1992 N  N     . LYS A 1 243 ? -8.741  23.814  5.304   1   18.38  ? 244  LYS A N     1 1 
ATOM   1993 C  CA    . LYS A 1 243 ? -10.104 23.852  5.811   1   18.48  ? 244  LYS A CA    1 1 
ATOM   1994 C  C     . LYS A 1 243 ? -10.245 24.67   7.118   1   19.64  ? 244  LYS A C     1 1 
ATOM   1995 O  O     . LYS A 1 243 ? -11.358 25.007  7.51    1   19.6   ? 244  LYS A O     1 1 
ATOM   1996 C  CB    . LYS A 1 243 ? -10.676 22.431  5.938   1   18.86  ? 244  LYS A CB    1 1 
ATOM   1997 C  CG    . LYS A 1 243 ? -10.971 21.824  4.574   1   22.55  ? 244  LYS A CG    1 1 
ATOM   1998 C  CD    . LYS A 1 243 ? -11.556 20.414  4.682   1   26.77  ? 244  LYS A CD    1 1 
ATOM   1999 C  CE    . LYS A 1 243 ? -11.921 19.853  3.341   1   28.56  ? 244  LYS A CE    1 1 
ATOM   2000 N  NZ    . LYS A 1 243 ? -12.382 18.441  3.477   1   30.9   ? 244  LYS A NZ    1 1 
ATOM   2001 N  N     . ASN A 1 244 ? -9.13   25.04   7.755   1   20.97  ? 245  ASN A N     1 1 
ATOM   2002 C  CA    . ASN A 1 244 ? -9.169  25.887  8.938   1   23.16  ? 245  ASN A CA    1 1 
ATOM   2003 C  C     . ASN A 1 244 ? -8.854  27.361  8.624   1   25.38  ? 245  ASN A C     1 1 
ATOM   2004 O  O     . ASN A 1 244 ? -9.059  28.2    9.491   1   26.55  ? 245  ASN A O     1 1 
ATOM   2005 C  CB    . ASN A 1 244 ? -8.306  25.34   10.054  1   24.73  ? 245  ASN A CB    1 1 
ATOM   2006 C  CG    . ASN A 1 244 ? -8.977  24.195  10.788  1   28.19  ? 245  ASN A CG    1 1 
ATOM   2007 O  OD1   . ASN A 1 244 ? -10.203 24.078  10.827  1   31.63  ? 245  ASN A OD1   1 1 
ATOM   2008 N  ND2   . ASN A 1 244 ? -8.21   23.341  11.396  1   26.53  ? 245  ASN A ND2   1 1 
ATOM   2009 N  N     . THR A 1 245 ? -8.454  27.695  7.385   1   26.27  ? 246  THR A N     1 1 
ATOM   2010 C  CA    . THR A 1 245 ? -8.202  29.079  6.977   1   28.29  ? 246  THR A CA    1 1 
ATOM   2011 C  C     . THR A 1 245 ? -9.408  29.674  6.219   1   30.31  ? 246  THR A C     1 1 
ATOM   2012 O  O     . THR A 1 245 ? -10.253 28.936  5.717   1   30.59  ? 246  THR A O     1 1 
ATOM   2013 C  CB    . THR A 1 245 ? -6.927  29.167  6.115   1   30.17  ? 246  THR A CB    1 1 
ATOM   2014 O  OG1   . THR A 1 245 ? -7.088  28.389  4.918   1   31.28  ? 246  THR A OG1   1 1 
ATOM   2015 C  CG2   . THR A 1 245 ? -5.683  28.735  6.867   1   30.63  ? 246  THR A CG2   1 1 
ATOM   2016 N  N     . LYS A 1 246 ? -9.476  31.012  6.106   1   31.64  ? 247  LYS A N     1 1 
ATOM   2017 C  CA    . LYS A 1 246 ? -10.571 31.663  5.384   1   33.11  ? 247  LYS A CA    1 1 
ATOM   2018 C  C     . LYS A 1 246 ? -10.38  31.49   3.881   1   33.34  ? 247  LYS A C     1 1 
ATOM   2019 O  O     . LYS A 1 246 ? -9.274  31.629  3.377   1   33.59  ? 247  LYS A O     1 1 
ATOM   2020 C  CB    . LYS A 1 246 ? -10.7   33.144  5.789   1   36.68  ? 247  LYS A CB    1 1 
ATOM   2021 C  CG    . LYS A 1 246 ? -11.847 33.385  6.777   1   43.41  ? 247  LYS A CG    1 1 
ATOM   2022 C  CD    . LYS A 1 246 ? -11.431 33.275  8.244   1   49.34  ? 247  LYS A CD    1 1 
ATOM   2023 C  CE    . LYS A 1 246 ? -12.226 32.217  8.984   1   54.05  ? 247  LYS A CE    1 1 
ATOM   2024 N  NZ    . LYS A 1 246 ? -11.699 30.835  8.755   1   57.08  ? 247  LYS A NZ    1 1 
ATOM   2025 N  N     . ASN A 1 247 ? -11.445 31.117  3.185   1   33.39  ? 248  ASN A N     1 1 
ATOM   2026 C  CA    . ASN A 1 247 ? -11.42  30.873  1.751   1   34.16  ? 248  ASN A CA    1 1 
ATOM   2027 C  C     . ASN A 1 247 ? -11.368 32.146  0.912   1   34.37  ? 248  ASN A C     1 1 
ATOM   2028 O  O     . ASN A 1 247 ? -11.033 32.047  -0.264  1   34.73  ? 248  ASN A O     1 1 
ATOM   2029 C  CB    . ASN A 1 247 ? -12.653 30.055  1.333   1   36.55  ? 248  ASN A CB    1 1 
ATOM   2030 C  CG    . ASN A 1 247 ? -12.737 28.657  1.934   1   41.29  ? 248  ASN A CG    1 1 
ATOM   2031 O  OD1   . ASN A 1 247 ? -13.815 28.061  2       1   42.62  ? 248  ASN A OD1   1 1 
ATOM   2032 N  ND2   . ASN A 1 247 ? -11.61  28.086  2.362   1   42.49  ? 248  ASN A ND2   1 1 
ATOM   2033 N  N     . ASP A 1 248 ? -11.719 33.323  1.474   1   33.64  ? 249  ASP A N     1 1 
ATOM   2034 C  CA    . ASP A 1 248 ? -11.746 34.546  0.68    1   34.37  ? 249  ASP A CA    1 1 
ATOM   2035 C  C     . ASP A 1 248 ? -10.379 34.924  0.084   1   33.49  ? 249  ASP A C     1 1 
ATOM   2036 O  O     . ASP A 1 248 ? -10.311 35.357  -1.066  1   34.15  ? 249  ASP A O     1 1 
ATOM   2037 C  CB    . ASP A 1 248 ? -12.366 35.734  1.466   1   38.15  ? 249  ASP A CB    1 1 
ATOM   2038 C  CG    . ASP A 1 248 ? -11.541 36.223  2.648   1   46.97  ? 249  ASP A CG    1 1 
ATOM   2039 O  OD1   . ASP A 1 248 ? -10.761 35.414  3.208   1   50.12  ? 249  ASP A OD1   1 1 
ATOM   2040 O  OD2   . ASP A 1 248 ? -11.665 37.419  3.009   1   49.64  ? 249  ASP A OD2   1 1 
ATOM   2041 N  N     . ASN A 1 249 ? -9.297  34.758  0.853   1   31.67  ? 250  ASN A N     1 1 
ATOM   2042 C  CA    . ASN A 1 249 ? -7.966  35.152  0.395   1   30.7   ? 250  ASN A CA    1 1 
ATOM   2043 C  C     . ASN A 1 249 ? -6.978  33.993  0.256   1   28.18  ? 250  ASN A C     1 1 
ATOM   2044 O  O     . ASN A 1 249 ? -5.798  34.243  0.04    1   28.04  ? 250  ASN A O     1 1 
ATOM   2045 C  CB    . ASN A 1 249 ? -7.391  36.194  1.345   1   32.86  ? 250  ASN A CB    1 1 
ATOM   2046 C  CG    . ASN A 1 249 ? -8.058  37.537  1.233   1   39.99  ? 250  ASN A CG    1 1 
ATOM   2047 O  OD1   . ASN A 1 249 ? -8.419  38.162  2.241   1   42.13  ? 250  ASN A OD1   1 1 
ATOM   2048 N  ND2   . ASN A 1 249 ? -8.257  38.015  0.001   1   42.18  ? 250  ASN A ND2   1 1 
ATOM   2049 N  N     . ASN A 1 250 ? -7.43   32.74   0.431   1   26.24  ? 251  ASN A N     1 1 
ATOM   2050 C  CA    . ASN A 1 250 ? -6.537  31.565  0.34    1   24.48  ? 251  ASN A CA    1 1 
ATOM   2051 C  C     . ASN A 1 250 ? -7.187  30.506  -0.5    1   22.91  ? 251  ASN A C     1 1 
ATOM   2052 O  O     . ASN A 1 250 ? -8.411  30.484  -0.593  1   23.44  ? 251  ASN A O     1 1 
ATOM   2053 C  CB    . ASN A 1 250 ? -6.278  30.985  1.729   1   24.76  ? 251  ASN A CB    1 1 
ATOM   2054 C  CG    . ASN A 1 250 ? -5.826  32.007  2.733   1   28.33  ? 251  ASN A CG    1 1 
ATOM   2055 O  OD1   . ASN A 1 250 ? -6.612  32.495  3.559   1   30.53  ? 251  ASN A OD1   1 1 
ATOM   2056 N  ND2   . ASN A 1 250 ? -4.565  32.38   2.669   1   27.72  ? 251  ASN A ND2   1 1 
ATOM   2057 N  N     . PHE A 1 251 ? -6.393  29.58   -1.068  1   21.18  ? 252  PHE A N     1 1 
ATOM   2058 C  CA    . PHE A 1 251 ? -6.904  28.445  -1.821  1   20.12  ? 252  PHE A CA    1 1 
ATOM   2059 C  C     . PHE A 1 251 ? -7.682  27.557  -0.885  1   20.32  ? 252  PHE A C     1 1 
ATOM   2060 O  O     . PHE A 1 251 ? -7.275  27.335  0.25    1   20.28  ? 252  PHE A O     1 1 
ATOM   2061 C  CB    . PHE A 1 251 ? -5.765  27.559  -2.36   1   19.75  ? 252  PHE A CB    1 1 
ATOM   2062 C  CG    . PHE A 1 251 ? -5.108  27.959  -3.652  1   19.69  ? 252  PHE A CG    1 1 
ATOM   2063 C  CD1   . PHE A 1 251 ? -5.535  29.082  -4.349  1   20.42  ? 252  PHE A CD1   1 1 
ATOM   2064 C  CD2   . PHE A 1 251 ? -4.04   27.229  -4.159  1   19.73  ? 252  PHE A CD2   1 1 
ATOM   2065 C  CE1   . PHE A 1 251 ? -4.89   29.478  -5.518  1   20.85  ? 252  PHE A CE1   1 1 
ATOM   2066 C  CE2   . PHE A 1 251 ? -3.419  27.606  -5.336  1   20.15  ? 252  PHE A CE2   1 1 
ATOM   2067 C  CZ    . PHE A 1 251 ? -3.825  28.749  -5.994  1   20.15  ? 252  PHE A CZ    1 1 
ATOM   2068 N  N     . THR A 1 252 ? -8.786  27.017  -1.372  1   20.71  ? 253  THR A N     1 1 
ATOM   2069 C  CA    . THR A 1 252 ? -9.606  26.085  -0.631  1   21.04  ? 253  THR A CA    1 1 
ATOM   2070 C  C     . THR A 1 252 ? -8.986  24.684  -0.815  1   21.34  ? 253  THR A C     1 1 
ATOM   2071 O  O     . THR A 1 252 ? -8.198  24.475  -1.757  1   21.09  ? 253  THR A O     1 1 
ATOM   2072 C  CB    . THR A 1 252 ? -11.014 26.053  -1.266  1   22.77  ? 253  THR A CB    1 1 
ATOM   2073 O  OG1   . THR A 1 252 ? -10.925 25.554  -2.614  1   24.31  ? 253  THR A OG1   1 1 
ATOM   2074 C  CG2   . THR A 1 252 ? -11.738 27.37   -1.196  1   22.12  ? 253  THR A CG2   1 1 
ATOM   2075 N  N     . TYR A 1 253 ? -9.423  23.688  -0.002  1   21.73  ? 254  TYR A N     1 1 
ATOM   2076 C  CA    . TYR A 1 253 ? -8.947  22.324  -0.205  1   22.13  ? 254  TYR A CA    1 1 
ATOM   2077 C  C     . TYR A 1 253 ? -9.336  21.808  -1.6    1   21.98  ? 254  TYR A C     1 1 
ATOM   2078 O  O     . TYR A 1 253 ? -8.483  21.224  -2.252  1   21.5   ? 254  TYR A O     1 1 
ATOM   2079 C  CB    . TYR A 1 253 ? -9.399  21.339  0.885   1   22.21  ? 254  TYR A CB    1 1 
ATOM   2080 C  CG    . TYR A 1 253 ? -8.81   19.978  0.605   1   23.99  ? 254  TYR A CG    1 1 
ATOM   2081 C  CD1   . TYR A 1 253 ? -7.434  19.802  0.527   1   25.09  ? 254  TYR A CD1   1 1 
ATOM   2082 C  CD2   . TYR A 1 253 ? -9.622  18.909  0.244   1   25.56  ? 254  TYR A CD2   1 1 
ATOM   2083 C  CE1   . TYR A 1 253 ? -6.881  18.582  0.172   1   26.42  ? 254  TYR A CE1   1 1 
ATOM   2084 C  CE2   . TYR A 1 253 ? -9.079  17.68   -0.114  1   26.67  ? 254  TYR A CE2   1 1 
ATOM   2085 C  CZ    . TYR A 1 253 ? -7.705  17.526  -0.153  1   27.5   ? 254  TYR A CZ    1 1 
ATOM   2086 O  OH    . TYR A 1 253 ? -7.132  16.324  -0.457  1   28.88  ? 254  TYR A OH    1 1 
ATOM   2087 N  N     . SER A 1 254 ? -10.556 22.106  -2.095  1   22.24  ? 255  SER A N     1 1 
ATOM   2088 C  CA    . SER A 1 254 ? -10.941 21.61   -3.431  1   23.47  ? 255  SER A CA    1 1 
ATOM   2089 C  C     . SER A 1 254 ? -10.034 22.178  -4.542  1   23.35  ? 255  SER A C     1 1 
ATOM   2090 O  O     . SER A 1 254 ? -9.758  21.471  -5.52   1   24.13  ? 255  SER A O     1 1 
ATOM   2091 C  CB    . SER A 1 254 ? -12.423 21.808  -3.726  1   24.94  ? 255  SER A CB    1 1 
ATOM   2092 O  OG    . SER A 1 254 ? -12.772 23.15   -3.441  1   30.57  ? 255  SER A OG    1 1 
ATOM   2093 N  N     . GLU A 1 255 ? -9.517  23.393  -4.362  1   22.09  ? 256  GLU A N     1 1 
ATOM   2094 C  CA    . GLU A 1 255 ? -8.552  23.959  -5.313  1   21.79  ? 256  GLU A CA    1 1 
ATOM   2095 C  C     . GLU A 1 255 ? -7.219  23.194  -5.227  1   20.57  ? 256  GLU A C     1 1 
ATOM   2096 O  O     . GLU A 1 255 ? -6.73   22.709  -6.247  1   20.93  ? 256  GLU A O     1 1 
ATOM   2097 C  CB    . GLU A 1 255 ? -8.364  25.473  -5.086  1   23.29  ? 256  GLU A CB    1 1 
ATOM   2098 C  CG    . GLU A 1 255 ? -9.592  26.272  -5.506  1   25.1   ? 256  GLU A CG    1 1 
ATOM   2099 C  CD    . GLU A 1 255 ? -9.566  27.724  -5.075  1   29.19  ? 256  GLU A CD    1 1 
ATOM   2100 O  OE1   . GLU A 1 255 ? -9.147  28.005  -3.934  1   27.03  ? 256  GLU A OE1   1 1 
ATOM   2101 O  OE2   . GLU A 1 255 ? -9.962  28.591  -5.88   1   34.2   ? 256  GLU A OE2   1 1 
ATOM   2102 N  N     . TRP A 1 256 ? -6.682  22.985  -4.011  1   19.19  ? 257  TRP A N     1 1 
ATOM   2103 C  CA    . TRP A 1 256 ? -5.467  22.167  -3.839  1   18.64  ? 257  TRP A CA    1 1 
ATOM   2104 C  C     . TRP A 1 256 ? -5.647  20.766  -4.435  1   19.69  ? 257  TRP A C     1 1 
ATOM   2105 O  O     . TRP A 1 256 ? -4.77   20.286  -5.139  1   20.05  ? 257  TRP A O     1 1 
ATOM   2106 C  CB    . TRP A 1 256 ? -5.079  22.022  -2.351  1   17.34  ? 257  TRP A CB    1 1 
ATOM   2107 C  CG    . TRP A 1 256 ? -4.513  23.262  -1.703  1   16.47  ? 257  TRP A CG    1 1 
ATOM   2108 C  CD1   . TRP A 1 256 ? -4.978  23.884  -0.577  1   16.76  ? 257  TRP A CD1   1 1 
ATOM   2109 C  CD2   . TRP A 1 256 ? -3.334  23.984  -2.104  1   15.58  ? 257  TRP A CD2   1 1 
ATOM   2110 N  NE1   . TRP A 1 256 ? -4.167  24.952  -0.259  1   16.91  ? 257  TRP A NE1   1 1 
ATOM   2111 C  CE2   . TRP A 1 256 ? -3.151  25.035  -1.18   1   16.27  ? 257  TRP A CE2   1 1 
ATOM   2112 C  CE3   . TRP A 1 256 ? -2.408  23.836  -3.149  1   15.92  ? 257  TRP A CE3   1 1 
ATOM   2113 C  CZ2   . TRP A 1 256 ? -2.104  25.949  -1.289  1   16.54  ? 257  TRP A CZ2   1 1 
ATOM   2114 C  CZ3   . TRP A 1 256 ? -1.361  24.741  -3.247  1   16.68  ? 257  TRP A CZ3   1 1 
ATOM   2115 C  CH2   . TRP A 1 256 ? -1.21   25.771  -2.316  1   16.81  ? 257  TRP A CH2   1 1 
ATOM   2116 N  N     . GLU A 1 257 ? -6.812  20.139  -4.188  1   19.98  ? 258  GLU A N     1 1 
ATOM   2117 C  CA    . GLU A 1 257 ? -7.145  18.803  -4.688  1   21.5   ? 258  GLU A CA    1 1 
ATOM   2118 C  C     . GLU A 1 257 ? -7.149  18.765  -6.213  1   22.78  ? 258  GLU A C     1 1 
ATOM   2119 O  O     . GLU A 1 257 ? -6.602  17.846  -6.791  1   23.11  ? 258  GLU A O     1 1 
ATOM   2120 C  CB    . GLU A 1 257 ? -8.512  18.365  -4.146  1   22.75  ? 258  GLU A CB    1 1 
ATOM   2121 C  CG    . GLU A 1 257 ? -8.875  16.926  -4.453  1   28.06  ? 258  GLU A CG    1 1 
ATOM   2122 C  CD    . GLU A 1 257 ? -10.239 16.578  -3.893  1   33.37  ? 258  GLU A CD    1 1 
ATOM   2123 O  OE1   . GLU A 1 257 ? -11.207 17.336  -4.143  1   33.21  ? 258  GLU A OE1   1 1 
ATOM   2124 O  OE2   . GLU A 1 257 ? -10.331 15.558  -3.176  1   35.86  ? 258  GLU A OE2   1 1 
ATOM   2125 N  N     . SER A 1 258 ? -7.73   19.777  -6.866  1   23.49  ? 259  SER A N     1 1 
ATOM   2126 C  CA    . SER A 1 258 ? -7.747  19.837  -8.328  1   24.43  ? 259  SER A CA    1 1 
ATOM   2127 C  C     . SER A 1 258 ? -6.332  20.002  -8.935  1   25.65  ? 259  SER A C     1 1 
ATOM   2128 O  O     . SER A 1 258 ? -6.126  19.602  -10.082 1   26.49  ? 259  SER A O     1 1 
ATOM   2129 C  CB    . SER A 1 258 ? -8.693  20.93   -8.811  1   25.12  ? 259  SER A CB    1 1 
ATOM   2130 O  OG    . SER A 1 258 ? -8.116  22.189  -8.524  1   27.84  ? 259  SER A OG    1 1 
ATOM   2131 N  N     . ILE A 1 259 ? -5.36   20.57   -8.166  1   25.18  ? 260  ILE A N     1 1 
ATOM   2132 C  CA    . ILE A 1 259 ? -3.957  20.688  -8.588  1   25.43  ? 260  ILE A CA    1 1 
ATOM   2133 C  C     . ILE A 1 259 ? -3.274  19.334  -8.361  1   25.95  ? 260  ILE A C     1 1 
ATOM   2134 O  O     . ILE A 1 259 ? -2.624  18.804  -9.266  1   26.3   ? 260  ILE A O     1 1 
ATOM   2135 C  CB    . ILE A 1 259 ? -3.224  21.816  -7.806  1   25.67  ? 260  ILE A CB    1 1 
ATOM   2136 C  CG1   . ILE A 1 259 ? -3.851  23.205  -8.081  1   26.3   ? 260  ILE A CG1   1 1 
ATOM   2137 C  CG2   . ILE A 1 259 ? -1.723  21.808  -8.125  1   26.35  ? 260  ILE A CG2   1 1 
ATOM   2138 C  CD1   . ILE A 1 259 ? -3.466  24.258  -7.094  1   26.24  ? 260  ILE A CD1   1 1 
ATOM   2139 N  N     . TYR A 1 260 ? -3.469  18.747  -7.161  1   26.11  ? 261  TYR A N     1 1 
ATOM   2140 C  CA    . TYR A 1 260 ? -2.925  17.444  -6.778  1   26.44  ? 261  TYR A CA    1 1 
ATOM   2141 C  C     . TYR A 1 260 ? -3.317  16.335  -7.756  1   28.01  ? 261  TYR A C     1 1 
ATOM   2142 O  O     . TYR A 1 260 ? -2.466  15.509  -8.092  1   27.79  ? 261  TYR A O     1 1 
ATOM   2143 C  CB    . TYR A 1 260 ? -3.365  17.051  -5.347  1   25.82  ? 261  TYR A CB    1 1 
ATOM   2144 C  CG    . TYR A 1 260 ? -2.912  15.659  -4.934  1   26.31  ? 261  TYR A CG    1 1 
ATOM   2145 C  CD1   . TYR A 1 260 ? -1.621  15.431  -4.493  1   27.26  ? 261  TYR A CD1   1 1 
ATOM   2146 C  CD2   . TYR A 1 260 ? -3.769  14.569  -5.022  1   26.92  ? 261  TYR A CD2   1 1 
ATOM   2147 C  CE1   . TYR A 1 260 ? -1.199  14.164  -4.109  1   28.46  ? 261  TYR A CE1   1 1 
ATOM   2148 C  CE2   . TYR A 1 260 ? -3.364  13.298  -4.634  1   27.83  ? 261  TYR A CE2   1 1 
ATOM   2149 C  CZ    . TYR A 1 260 ? -2.069  13.094  -4.185  1   29.25  ? 261  TYR A CZ    1 1 
ATOM   2150 O  OH    . TYR A 1 260 ? -1.612  11.835  -3.815  1   29.8   ? 261  TYR A OH    1 1 
ATOM   2151 N  N     . ASN A 1 261 ? -4.603  16.267  -8.163  1   28.73  ? 262  ASN A N     1 1 
ATOM   2152 C  CA    . ASN A 1 261 ? -5.001  15.178  -9.075  1   30.34  ? 262  ASN A CA    1 1 
ATOM   2153 C  C     . ASN A 1 261 ? -4.717  15.493  -10.572 1   31.99  ? 262  ASN A C     1 1 
ATOM   2154 O  O     . ASN A 1 261 ? -5.094  14.715  -11.447 1   32.64  ? 262  ASN A O     1 1 
ATOM   2155 C  CB    . ASN A 1 261 ? -6.443  14.711  -8.841  1   30.24  ? 262  ASN A CB    1 1 
ATOM   2156 C  CG    . ASN A 1 261 ? -7.475  15.771  -9.07   1   33.38  ? 262  ASN A CG    1 1 
ATOM   2157 O  OD1   . ASN A 1 261 ? -7.289  16.698  -9.87   1   34.42  ? 262  ASN A OD1   1 1 
ATOM   2158 N  ND2   . ASN A 1 261 ? -8.595  15.66   -8.363  1   34.26  ? 262  ASN A ND2   1 1 
ATOM   2159 N  N     . GLY A 1 262 ? -4.05   16.604  -10.84  1   32.51  ? 263  GLY A N     1 1 
ATOM   2160 C  CA    . GLY A 1 262 ? -3.649  16.972  -12.184 1   34.17  ? 263  GLY A CA    1 1 
ATOM   2161 C  C     . GLY A 1 262 ? -4.72   17.589  -13.05  1   35.89  ? 263  GLY A C     1 1 
ATOM   2162 O  O     . GLY A 1 262 ? -4.502  17.752  -14.255 1   36.92  ? 263  GLY A O     1 1 
ATOM   2163 N  N     . THR A 1 263 ? -5.871  17.968  -12.461 1   35.77  ? 264  THR A N     1 1 
ATOM   2164 C  CA    . THR A 1 263 ? -6.943  18.574  -13.258 1   36.22  ? 264  THR A CA    1 1 
ATOM   2165 C  C     . THR A 1 263 ? -6.472  19.923  -13.784 1   36.54  ? 264  THR A C     1 1 
ATOM   2166 O  O     . THR A 1 263 ? -6.624  20.215  -14.97  1   37.36  ? 264  THR A O     1 1 
ATOM   2167 C  CB    . THR A 1 263 ? -8.266  18.689  -12.476 1   36.8   ? 264  THR A CB    1 1 
ATOM   2168 O  OG1   . THR A 1 263 ? -8.643  17.419  -11.961 1   37.79  ? 264  THR A OG1   1 1 
ATOM   2169 C  CG2   . THR A 1 263 ? -9.387  19.213  -13.335 1   36.94  ? 264  THR A CG2   1 1 
ATOM   2170 N  N     . TYR A 1 264 ? -5.857  20.721  -12.902 1   35.68  ? 265  TYR A N     1 1 
ATOM   2171 C  CA    . TYR A 1 264 ? -5.331  22.026  -13.254 1   35.17  ? 265  TYR A CA    1 1 
ATOM   2172 C  C     . TYR A 1 264 ? -3.915  22.208  -12.69  1   34.67  ? 265  TYR A C     1 1 
ATOM   2173 O  O     . TYR A 1 264 ? -3.52   21.537  -11.724 1   34.11  ? 265  TYR A O     1 1 
ATOM   2174 C  CB    . TYR A 1 264 ? -6.227  23.143  -12.678 1   35.69  ? 265  TYR A CB    1 1 
ATOM   2175 C  CG    . TYR A 1 264 ? -7.696  23.025  -13.016 1   36.51  ? 265  TYR A CG    1 1 
ATOM   2176 C  CD1   . TYR A 1 264 ? -8.162  23.313  -14.291 1   37.37  ? 265  TYR A CD1   1 1 
ATOM   2177 C  CD2   . TYR A 1 264 ? -8.626  22.668  -12.049 1   37.36  ? 265  TYR A CD2   1 1 
ATOM   2178 C  CE1   . TYR A 1 264 ? -9.517  23.23   -14.601 1   38.04  ? 265  TYR A CE1   1 1 
ATOM   2179 C  CE2   . TYR A 1 264 ? -9.985  22.591  -12.343 1   37.85  ? 265  TYR A CE2   1 1 
ATOM   2180 C  CZ    . TYR A 1 264 ? -10.427 22.859  -13.624 1   38.68  ? 265  TYR A CZ    1 1 
ATOM   2181 O  OH    . TYR A 1 264 ? -11.776 22.772  -13.914 1   39.9   ? 265  TYR A OH    1 1 
ATOM   2182 N  N     . ARG A 1 265 ? -3.158  23.135  -13.286 1   34.27  ? 266  ARG A N     1 1 
ATOM   2183 C  CA    . ARG A 1 265 ? -1.858  23.494  -12.746 1   34.74  ? 266  ARG A CA    1 1 
ATOM   2184 C  C     . ARG A 1 265 ? -2.092  24.706  -11.824 1   34.05  ? 266  ARG A C     1 1 
ATOM   2185 O  O     . ARG A 1 265 ? -3.12   25.374  -11.931 1   34.38  ? 266  ARG A O     1 1 
ATOM   2186 C  CB    . ARG A 1 265 ? -0.828  23.741  -13.857 1   37.33  ? 266  ARG A CB    1 1 
ATOM   2187 C  CG    . ARG A 1 265 ? -1.121  24.976  -14.68  1   43.13  ? 266  ARG A CG    1 1 
ATOM   2188 C  CD    . ARG A 1 265 ? -0.184  25.12   -15.868 1   49.08  ? 266  ARG A CD    1 1 
ATOM   2189 N  NE    . ARG A 1 265 ? -0.181  26.495  -16.374 1   54.04  ? 266  ARG A NE    1 1 
ATOM   2190 C  CZ    . ARG A 1 265 ? -0.866  26.912  -17.434 1   57.43  ? 266  ARG A CZ    1 1 
ATOM   2191 N  NH1   . ARG A 1 265 ? -1.599  26.057  -18.138 1   56.7   ? 266  ARG A NH1   1 1 
ATOM   2192 N  NH2   . ARG A 1 265 ? -0.812  28.184  -17.807 1   58.89  ? 266  ARG A NH2   1 1 
ATOM   2193 N  N     . ILE A 1 266 ? -1.196  24.96   -10.884 1   33.27  ? 267  ILE A N     1 1 
ATOM   2194 C  CA    . ILE A 1 266 ? -1.353  26.03   -9.9    1   33.27  ? 267  ILE A CA    1 1 
ATOM   2195 C  C     . ILE A 1 266 ? -1.52   27.449  -10.539 1   34.15  ? 267  ILE A C     1 1 
ATOM   2196 O  O     . ILE A 1 266 ? -2.043  28.365  -9.899  1   33.52  ? 267  ILE A O     1 1 
ATOM   2197 C  CB    . ILE A 1 266 ? -0.182  25.945  -8.881  1   33.31  ? 267  ILE A CB    1 1 
ATOM   2198 C  CG1   . ILE A 1 266 ? -0.495  26.691  -7.575  1   34.1   ? 267  ILE A CG1   1 1 
ATOM   2199 C  CG2   . ILE A 1 266 ? 1.138   26.386  -9.492  1   33.72  ? 267  ILE A CG2   1 1 
ATOM   2200 C  CD1   . ILE A 1 266 ? 0.405   26.29   -6.447  1   35.08  ? 267  ILE A CD1   1 1 
ATOM   2201 N  N     . THR A 1 267 ? -1.121  27.611  -11.812 1   34.82  ? 268  THR A N     1 1 
ATOM   2202 C  CA    . THR A 1 267 ? -1.254  28.896  -12.513 1   35.09  ? 268  THR A CA    1 1 
ATOM   2203 C  C     . THR A 1 267 ? -2.473  28.943  -13.468 1   35.79  ? 268  THR A C     1 1 
ATOM   2204 O  O     . THR A 1 267 ? -2.739  30.003  -14.03  1   36.84  ? 268  THR A O     1 1 
ATOM   2205 C  CB    . THR A 1 267 ? 0.031   29.198  -13.298 1   35.53  ? 268  THR A CB    1 1 
ATOM   2206 O  OG1   . THR A 1 267 ? 0.328   28.086  -14.148 1   35.86  ? 268  THR A OG1   1 1 
ATOM   2207 C  CG2   . THR A 1 267 ? 1.22    29.503  -12.387 1   35.47  ? 268  THR A CG2   1 1 
ATOM   2208 N  N     . ASN A 1 268 ? -3.164  27.81   -13.701 1   34.91  ? 269  ASN A N     1 1 
ATOM   2209 C  CA    . ASN A 1 268 ? -4.334  27.768  -14.596 1   35.06  ? 269  ASN A CA    1 1 
ATOM   2210 C  C     . ASN A 1 268 ? -5.63   27.341  -13.881 1   35.02  ? 269  ASN A C     1 1 
ATOM   2211 O  O     . ASN A 1 268 ? -6.566  26.818  -14.509 1   35.2   ? 269  ASN A O     1 1 
ATOM   2212 C  CB    . ASN A 1 268 ? -4.086  26.872  -15.813 1   35.56  ? 269  ASN A CB    1 1 
ATOM   2213 N  N     . LEU A 1 269 ? -5.706  27.59   -12.571 1   34.7   ? 270  LEU A N     1 1 
ATOM   2214 C  CA    . LEU A 1 269 ? -6.895  27.286  -11.774 1   35.19  ? 270  LEU A CA    1 1 
ATOM   2215 C  C     . LEU A 1 269 ? -8.072  28.14   -12.32  1   34.83  ? 270  LEU A C     1 1 
ATOM   2216 O  O     . LEU A 1 269 ? -7.875  29.33   -12.599 1   34.94  ? 270  LEU A O     1 1 
ATOM   2217 C  CB    . LEU A 1 269 ? -6.577  27.673  -10.323 1   35.78  ? 270  LEU A CB    1 1 
ATOM   2218 C  CG    . LEU A 1 269 ? -7.068  26.75   -9.223  1   37.65  ? 270  LEU A CG    1 1 
ATOM   2219 C  CD1   . LEU A 1 269 ? -6.585  25.325  -9.432  1   38.68  ? 270  LEU A CD1   1 1 
ATOM   2220 C  CD2   . LEU A 1 269 ? -6.579  27.231  -7.89   1   38.43  ? 270  LEU A CD2   1 1 
ATOM   2221 N  N     . PRO A 1 270 ? -9.256  27.555  -12.602 1   34.27  ? 271  PRO A N     1 1 
ATOM   2222 C  CA    . PRO A 1 270 ? -10.353 28.365  -13.176 1   33.27  ? 271  PRO A CA    1 1 
ATOM   2223 C  C     . PRO A 1 270 ? -10.822 29.506  -12.276 1   32.62  ? 271  PRO A C     1 1 
ATOM   2224 O  O     . PRO A 1 270 ? -11.281 30.534  -12.761 1   32.8   ? 271  PRO A O     1 1 
ATOM   2225 C  CB    . PRO A 1 270 ? -11.441 27.341  -13.461 1   33.89  ? 271  PRO A CB    1 1 
ATOM   2226 C  CG    . PRO A 1 270 ? -11.161 26.226  -12.52  1   34.78  ? 271  PRO A CG    1 1 
ATOM   2227 C  CD    . PRO A 1 270 ? -9.674  26.158  -12.383 1   33.76  ? 271  PRO A CD    1 1 
ATOM   2228 N  N     . SER A 1 271 ? -10.645 29.345  -10.972 1   32     ? 272  SER A N     1 1 
ATOM   2229 C  CA    . SER A 1 271 ? -10.981 30.343  -9.963  1   32.36  ? 272  SER A CA    1 1 
ATOM   2230 C  C     . SER A 1 271 ? -9.829  31.307  -9.658  1   33.4   ? 272  SER A C     1 1 
ATOM   2231 O  O     . SER A 1 271 ? -9.974  32.154  -8.777  1   33.62  ? 272  SER A O     1 1 
ATOM   2232 C  CB    . SER A 1 271 ? -11.395 29.652  -8.672  1   32.93  ? 272  SER A CB    1 1 
ATOM   2233 O  OG    . SER A 1 271 ? -10.476 28.614  -8.369  1   34.53  ? 272  SER A OG    1 1 
ATOM   2234 N  N     . LEU A 1 272 ? -8.677  31.202  -10.363 1   33.96  ? 273  LEU A N     1 1 
ATOM   2235 C  CA    . LEU A 1 272 ? -7.542  32.107  -10.145 1   34.15  ? 273  LEU A CA    1 1 
ATOM   2236 C  C     . LEU A 1 272 ? -7.987  33.518  -10.502 1   33.16  ? 273  LEU A C     1 1 
ATOM   2237 O  O     . LEU A 1 272 ? -8.603  33.728  -11.542 1   33.69  ? 273  LEU A O     1 1 
ATOM   2238 C  CB    . LEU A 1 272 ? -6.32   31.698  -10.983 1   34.93  ? 273  LEU A CB    1 1 
ATOM   2239 C  CG    . LEU A 1 272 ? -4.968  31.949  -10.317 1   37.01  ? 273  LEU A CG    1 1 
ATOM   2240 C  CD1   . LEU A 1 272 ? -4.772  31.029  -9.129  1   37.35  ? 273  LEU A CD1   1 1 
ATOM   2241 C  CD2   . LEU A 1 272 ? -3.83   31.742  -11.296 1   38.25  ? 273  LEU A CD2   1 1 
ATOM   2242 N  N     . GLY A 1 273 ? -7.778  34.439  -9.583  1   31.83  ? 274  GLY A N     1 1 
ATOM   2243 C  CA    . GLY A 1 273 ? -8.253  35.801  -9.743  1   30.79  ? 274  GLY A CA    1 1 
ATOM   2244 C  C     . GLY A 1 273 ? -9.312  36.179  -8.721  1   29.38  ? 274  GLY A C     1 1 
ATOM   2245 O  O     . GLY A 1 273 ? -9.614  37.368  -8.568  1   30.22  ? 274  GLY A O     1 1 
ATOM   2246 N  N     . ARG A 1 274 ? -9.884  35.198  -7.993  1   27.57  ? 275  ARG A N     1 1 
ATOM   2247 C  CA    . ARG A 1 274 ? -10.87  35.523  -6.954  1   26.76  ? 275  ARG A CA    1 1 
ATOM   2248 C  C     . ARG A 1 274 ? -10.237 36.331  -5.805  1   26.18  ? 275  ARG A C     1 1 
ATOM   2249 O  O     . ARG A 1 274 ? -10.931 37.053  -5.095  1   26.01  ? 275  ARG A O     1 1 
ATOM   2250 C  CB    . ARG A 1 274 ? -11.654 34.296  -6.472  1   26.86  ? 275  ARG A CB    1 1 
ATOM   2251 C  CG    . ARG A 1 274 ? -10.824 33.167  -5.956  1   27.43  ? 275  ARG A CG    1 1 
ATOM   2252 C  CD    . ARG A 1 274 ? -11.753 32.021  -5.549  1   28.08  ? 275  ARG A CD    1 1 
ATOM   2253 N  NE    . ARG A 1 274 ? -11.076 31.051  -4.685  1   27.11  ? 275  ARG A NE    1 1 
ATOM   2254 C  CZ    . ARG A 1 274 ? -10.885 31.223  -3.381  1   26.72  ? 275  ARG A CZ    1 1 
ATOM   2255 N  NH1   . ARG A 1 274 ? -11.337 32.313  -2.774  1   25.57  ? 275  ARG A NH1   1 1 
ATOM   2256 N  NH2   . ARG A 1 274 ? -10.246 30.306  -2.673  1   25.61  ? 275  ARG A NH2   1 1 
ATOM   2257 N  N     . PHE A 1 275 ? -8.917  36.223  -5.642  1   25.37  ? 276  PHE A N     1 1 
ATOM   2258 C  CA    . PHE A 1 275 ? -8.105  37.057  -4.762  1   24.83  ? 276  PHE A CA    1 1 
ATOM   2259 C  C     . PHE A 1 275 ? -6.824  37.428  -5.539  1   23.74  ? 276  PHE A C     1 1 
ATOM   2260 O  O     . PHE A 1 275 ? -6.365  36.669  -6.405  1   23.51  ? 276  PHE A O     1 1 
ATOM   2261 C  CB    . PHE A 1 275 ? -7.835  36.427  -3.379  1   24.75  ? 276  PHE A CB    1 1 
ATOM   2262 C  CG    . PHE A 1 275 ? -7.073  35.125  -3.39   1   25.6   ? 276  PHE A CG    1 1 
ATOM   2263 C  CD1   . PHE A 1 275 ? -5.683  35.113  -3.43   1   26.71  ? 276  PHE A CD1   1 1 
ATOM   2264 C  CD2   . PHE A 1 275 ? -7.738  33.916  -3.324  1   26.04  ? 276  PHE A CD2   1 1 
ATOM   2265 C  CE1   . PHE A 1 275 ? -4.98   33.911  -3.451  1   27.33  ? 276  PHE A CE1   1 1 
ATOM   2266 C  CE2   . PHE A 1 275 ? -7.034  32.714  -3.337  1   27.09  ? 276  PHE A CE2   1 1 
ATOM   2267 C  CZ    . PHE A 1 275 ? -5.658  32.718  -3.372  1   26.96  ? 276  PHE A CZ    1 1 
ATOM   2268 N  N     . LYS A 1 276 ? -6.299  38.624  -5.295  1   23.43  ? 277  LYS A N     1 1 
ATOM   2269 C  CA    . LYS A 1 276 ? -5.094  39.095  -5.982  1   23.53  ? 277  LYS A CA    1 1 
ATOM   2270 C  C     . LYS A 1 276 ? -3.831  38.841  -5.149  1   22.9   ? 277  LYS A C     1 1 
ATOM   2271 O  O     . LYS A 1 276 ? -3.92   38.352  -4.026  1   23.11  ? 277  LYS A O     1 1 
ATOM   2272 C  CB    . LYS A 1 276 ? -5.226  40.601  -6.276  1   26.14  ? 277  LYS A CB    1 1 
ATOM   2273 C  CG    . LYS A 1 276 ? -6.257  40.913  -7.341  1   33.15  ? 277  LYS A CG    1 1 
ATOM   2274 C  CD    . LYS A 1 276 ? -6.087  42.349  -7.816  1   40.03  ? 277  LYS A CD    1 1 
ATOM   2275 C  CE    . LYS A 1 276 ? -6.234  42.486  -9.315  1   46     ? 277  LYS A CE    1 1 
ATOM   2276 N  NZ    . LYS A 1 276 ? -6.755  43.835  -9.708  1   49.57  ? 277  LYS A NZ    1 1 
ATOM   2277 N  N     . PHE A 1 277 ? -2.643  39.125  -5.723  1   22.14  ? 278  PHE A N     1 1 
ATOM   2278 C  CA    . PHE A 1 277 ? -1.414  39.043  -4.966  1   22.06  ? 278  PHE A CA    1 1 
ATOM   2279 C  C     . PHE A 1 277 ? -1.235  40.45   -4.393  1   22.68  ? 278  PHE A C     1 1 
ATOM   2280 O  O     . PHE A 1 277 ? -1.089  41.427  -5.143  1   23.66  ? 278  PHE A O     1 1 
ATOM   2281 C  CB    . PHE A 1 277 ? -0.222  38.61   -5.849  1   21.07  ? 278  PHE A CB    1 1 
ATOM   2282 C  CG    . PHE A 1 277 ? 1.16    38.967  -5.332  1   20.89  ? 278  PHE A CG    1 1 
ATOM   2283 C  CD1   . PHE A 1 277 ? 1.506   38.737  -4.015  1   21.27  ? 278  PHE A CD1   1 1 
ATOM   2284 C  CD2   . PHE A 1 277 ? 2.14    39.433  -6.191  1   20.68  ? 278  PHE A CD2   1 1 
ATOM   2285 C  CE1   . PHE A 1 277 ? 2.775   39.04   -3.554  1   21.36  ? 278  PHE A CE1   1 1 
ATOM   2286 C  CE2   . PHE A 1 277 ? 3.418   39.711  -5.728  1   21.08  ? 278  PHE A CE2   1 1 
ATOM   2287 C  CZ    . PHE A 1 277 ? 3.727   39.513  -4.412  1   20.98  ? 278  PHE A CZ    1 1 
ATOM   2288 N  N     . ARG A 1 278 ? -1.297  40.565  -3.067  1   22.05  ? 279  ARG A N     1 1 
ATOM   2289 C  CA    . ARG A 1 278 ? -1.124  41.857  -2.395  1   21.79  ? 279  ARG A CA    1 1 
ATOM   2290 C  C     . ARG A 1 278 ? -0.011  41.778  -1.355  1   20.72  ? 279  ARG A C     1 1 
ATOM   2291 O  O     . ARG A 1 278 ? -0.262  41.488  -0.19   1   20.16  ? 279  ARG A O     1 1 
ATOM   2292 C  CB    . ARG A 1 278 ? -2.431  42.308  -1.742  1   23     ? 279  ARG A CB    1 1 
ATOM   2293 C  CG    . ARG A 1 278 ? -3.612  42.323  -2.713  1   27.13  ? 279  ARG A CG    1 1 
ATOM   2294 C  CD    . ARG A 1 278 ? -4.777  43.088  -2.151  1   30.11  ? 279  ARG A CD    1 1 
ATOM   2295 N  NE    . ARG A 1 278 ? -5.891  43.14   -3.098  1   33.74  ? 279  ARG A NE    1 1 
ATOM   2296 C  CZ    . ARG A 1 278 ? -6.137  44.153  -3.924  1   34.54  ? 279  ARG A CZ    1 1 
ATOM   2297 N  NH1   . ARG A 1 278 ? -5.349  45.225  -3.927  1   32.42  ? 279  ARG A NH1   1 1 
ATOM   2298 N  NH2   . ARG A 1 278 ? -7.182  44.112  -4.739  1   34.69  ? 279  ARG A NH2   1 1 
ATOM   2299 N  N     . LYS A 1 279 ? 1.221   42.044  -1.778  1   20.45  ? 280  LYS A N     1 1 
ATOM   2300 C  CA    . LYS A 1 279 ? 2.375   42.046  -0.893  1   19.81  ? 280  LYS A CA    1 1 
ATOM   2301 C  C     . LYS A 1 279 ? 2.228   43.109  0.236   1   20.24  ? 280  LYS A C     1 1 
ATOM   2302 O  O     . LYS A 1 279 ? 1.921   44.265  -0.044  1   20.3   ? 280  LYS A O     1 1 
ATOM   2303 C  CB    . LYS A 1 279 ? 3.646   42.316  -1.73   1   19.64  ? 280  LYS A CB    1 1 
ATOM   2304 C  CG    . LYS A 1 279 ? 4.896   42.568  -0.918  1   19.84  ? 280  LYS A CG    1 1 
ATOM   2305 C  CD    . LYS A 1 279 ? 5.441   41.33   -0.256  1   20.54  ? 280  LYS A CD    1 1 
ATOM   2306 C  CE    . LYS A 1 279 ? 6.587   41.716  0.661   1   20.48  ? 280  LYS A CE    1 1 
ATOM   2307 N  NZ    . LYS A 1 279 ? 7.291   40.521  1.188   1   19.9   ? 280  LYS A NZ    1 1 
ATOM   2308 N  N     . LYS A 1 280 ? 2.432   42.709  1.497   1   20.45  ? 281  LYS A N     1 1 
ATOM   2309 C  CA    . LYS A 1 280 ? 2.39    43.632  2.621   1   21.61  ? 281  LYS A CA    1 1 
ATOM   2310 C  C     . LYS A 1 280 ? 3.796   44.127  2.834   1   22.05  ? 281  LYS A C     1 1 
ATOM   2311 O  O     . LYS A 1 280 ? 4.736   43.325  2.984   1   22.68  ? 281  LYS A O     1 1 
ATOM   2312 C  CB    . LYS A 1 280 ? 1.911   42.946  3.91    1   24.69  ? 281  LYS A CB    1 1 
ATOM   2313 C  CG    . LYS A 1 280 ? 0.419   42.607  3.969   1   30.01  ? 281  LYS A CG    1 1 
ATOM   2314 C  CD    . LYS A 1 280 ? 0.099   41.689  5.164   1   34.18  ? 281  LYS A CD    1 1 
ATOM   2315 C  CE    . LYS A 1 280 ? -1.388  41.443  5.342   1   39.5   ? 281  LYS A CE    1 1 
ATOM   2316 N  NZ    . LYS A 1 280 ? -1.714  40.75   6.626   1   41.87  ? 281  LYS A NZ    1 1 
ATOM   2317 N  N     . ILE A 1 281 ? 3.973   45.439  2.81    1   21.52  ? 282  ILE A N     1 1 
ATOM   2318 C  CA    . ILE A 1 281 ? 5.267   46.069  3.028   1   21.49  ? 282  ILE A CA    1 1 
ATOM   2319 C  C     . ILE A 1 281 ? 5.093   47.049  4.163   1   22.2   ? 282  ILE A C     1 1 
ATOM   2320 O  O     . ILE A 1 281 ? 4.17    47.855  4.12    1   23.1   ? 282  ILE A O     1 1 
ATOM   2321 C  CB    . ILE A 1 281 ? 5.784   46.785  1.749   1   21.65  ? 282  ILE A CB    1 1 
ATOM   2322 C  CG1   . ILE A 1 281 ? 5.882   45.8    0.56    1   22.9   ? 282  ILE A CG1   1 1 
ATOM   2323 C  CG2   . ILE A 1 281 ? 7.137   47.498  2.01    1   21.31  ? 282  ILE A CG2   1 1 
ATOM   2324 C  CD1   . ILE A 1 281 ? 6.421   46.429  -0.776  1   24.29  ? 282  ILE A CD1   1 1 
ATOM   2325 N  N     . ALA A 1 282 ? 5.949   46.982  5.198   1   21.91  ? 283  ALA A N     1 1 
ATOM   2326 C  CA    . ALA A 1 282 ? 5.869   47.925  6.311   1   22.18  ? 283  ALA A CA    1 1 
ATOM   2327 C  C     . ALA A 1 282 ? 6.198   49.327  5.798   1   23.4   ? 283  ALA A C     1 1 
ATOM   2328 O  O     . ALA A 1 282 ? 7.036   49.471  4.907   1   23.69  ? 283  ALA A O     1 1 
ATOM   2329 C  CB    . ALA A 1 282 ? 6.857   47.532  7.398   1   21.62  ? 283  ALA A CB    1 1 
ATOM   2330 N  N     . GLU A 1 283 ? 5.549   50.358  6.35    1   23.61  ? 284  GLU A N     1 1 
ATOM   2331 C  CA    . GLU A 1 283 ? 5.797   51.73   5.916   1   24.76  ? 284  GLU A CA    1 1 
ATOM   2332 C  C     . GLU A 1 283 ? 7.251   52.136  6.154   1   24     ? 284  GLU A C     1 1 
ATOM   2333 O  O     . GLU A 1 283 ? 7.847   52.802  5.311   1   24.27  ? 284  GLU A O     1 1 
ATOM   2334 C  CB    . GLU A 1 283 ? 4.781   52.708  6.562   1   28.27  ? 284  GLU A CB    1 1 
ATOM   2335 C  CG    . GLU A 1 283 ? 4.799   54.098  5.952   1   36.58  ? 284  GLU A CG    1 1 
ATOM   2336 C  CD    . GLU A 1 283 ? 3.689   54.993  6.463   1   49.85  ? 284  GLU A CD    1 1 
ATOM   2337 O  OE1   . GLU A 1 283 ? 2.518   54.547  6.456   1   54.06  ? 284  GLU A OE1   1 1 
ATOM   2338 O  OE2   . GLU A 1 283 ? 3.986   56.14   6.872   1   53.11  ? 284  GLU A OE2   1 1 
ATOM   2339 N  N     . LYS A 1 284 ? 7.866   51.643  7.238   1   23.21  ? 285  LYS A N     1 1 
ATOM   2340 C  CA    . LYS A 1 284 ? 9.273   51.943  7.528   1   22.79  ? 285  LYS A CA    1 1 
ATOM   2341 C  C     . LYS A 1 284 ? 10.238  51.317  6.49    1   21.92  ? 285  LYS A C     1 1 
ATOM   2342 O  O     . LYS A 1 284 ? 11.369  51.754  6.383   1   22.16  ? 285  LYS A O     1 1 
ATOM   2343 C  CB    . LYS A 1 284 ? 9.643   51.457  8.933   1   24.47  ? 285  LYS A CB    1 1 
ATOM   2344 C  CG    . LYS A 1 284 ? 9.556   49.935  9.079   1   27.04  ? 285  LYS A CG    1 1 
ATOM   2345 C  CD    . LYS A 1 284 ? 9.961   49.477  10.467  1   29.93  ? 285  LYS A CD    1 1 
ATOM   2346 C  CE    . LYS A 1 284 ? 9.876   47.971  10.623  1   30.93  ? 285  LYS A CE    1 1 
ATOM   2347 N  NZ    . LYS A 1 284 ? 9.991   47.564  12.043  1   30.64  ? 285  LYS A NZ    1 1 
ATOM   2348 N  N     . SER A 1 285 ? 9.789   50.319  5.715   1   20.21  ? 286  SER A N     1 1 
ATOM   2349 C  CA    . SER A 1 285 ? 10.638  49.702  4.691   1   19.63  ? 286  SER A CA    1 1 
ATOM   2350 C  C     . SER A 1 285 ? 10.588  50.446  3.37    1   19.69  ? 286  SER A C     1 1 
ATOM   2351 O  O     . SER A 1 285 ? 11.392  50.138  2.497   1   19.55  ? 286  SER A O     1 1 
ATOM   2352 C  CB    . SER A 1 285 ? 10.181  48.266  4.432   1   19.18  ? 286  SER A CB    1 1 
ATOM   2353 O  OG    . SER A 1 285 ? 10.091  47.539  5.642   1   19.84  ? 286  SER A OG    1 1 
ATOM   2354 N  N     . LEU A 1 286 ? 9.602   51.351  3.168   1   20.22  ? 287  LEU A N     1 1 
ATOM   2355 C  CA    . LEU A 1 286 ? 9.45    52.036  1.898   1   21.43  ? 287  LEU A CA    1 1 
ATOM   2356 C  C     . LEU A 1 286 ? 10.535  53.038  1.597   1   23.61  ? 287  LEU A C     1 1 
ATOM   2357 O  O     . LEU A 1 286 ? 11.057  53.727  2.485   1   24.09  ? 287  LEU A O     1 1 
ATOM   2358 C  CB    . LEU A 1 286 ? 8.074   52.695  1.766   1   21.58  ? 287  LEU A CB    1 1 
ATOM   2359 C  CG    . LEU A 1 286 ? 6.85    51.743  1.798   1   21.36  ? 287  LEU A CG    1 1 
ATOM   2360 C  CD1   . LEU A 1 286 ? 5.579   52.545  1.867   1   21.82  ? 287  LEU A CD1   1 1 
ATOM   2361 C  CD2   . LEU A 1 286 ? 6.803   50.86   0.581   1   20.48  ? 287  LEU A CD2   1 1 
ATOM   2362 N  N     . SER A 1 287 ? 10.88   53.1    0.313   1   24.26  ? 288  SER A N     1 1 
ATOM   2363 C  CA    . SER A 1 287 ? 11.861  54.02   -0.263  1   24.67  ? 288  SER A CA    1 1 
ATOM   2364 C  C     . SER A 1 287 ? 11.687  54.003  -1.798  1   24.67  ? 288  SER A C     1 1 
ATOM   2365 O  O     . SER A 1 287 ? 10.95   53.15   -2.329  1   25.51  ? 288  SER A O     1 1 
ATOM   2366 C  CB    . SER A 1 287 ? 13.277  53.595  0.117   1   25.95  ? 288  SER A CB    1 1 
ATOM   2367 O  OG    . SER A 1 287 ? 13.592  52.384  -0.542  1   29.95  ? 288  SER A OG    1 1 
ATOM   2368 N  N     . GLY A 1 288 ? 12.34   54.938  -2.485  1   23.29  ? 289  GLY A N     1 1 
ATOM   2369 C  CA    . GLY A 1 288 ? 12.322  55.042  -3.938  1   23.22  ? 289  GLY A CA    1 1 
ATOM   2370 C  C     . GLY A 1 288 ? 10.946  54.982  -4.555  1   22.73  ? 289  GLY A C     1 1 
ATOM   2371 O  O     . GLY A 1 288 ? 10.04   55.667  -4.083  1   23.4   ? 289  GLY A O     1 1 
ATOM   2372 N  N     . LYS A 1 289 ? 10.749  54.091  -5.551  1   21.52  ? 290  LYS A N     1 1 
ATOM   2373 C  CA    . LYS A 1 289 ? 9.441   53.913  -6.183  1   20.87  ? 290  LYS A CA    1 1 
ATOM   2374 C  C     . LYS A 1 289 ? 8.756   52.601  -5.784  1   21.47  ? 290  LYS A C     1 1 
ATOM   2375 O  O     . LYS A 1 289 ? 7.895   52.108  -6.517  1   21.74  ? 290  LYS A O     1 1 
ATOM   2376 C  CB    . LYS A 1 289 ? 9.576   53.993  -7.698  1   22.38  ? 290  LYS A CB    1 1 
ATOM   2377 C  CG    . LYS A 1 289 ? 10.017  55.372  -8.192  1   27.34  ? 290  LYS A CG    1 1 
ATOM   2378 C  CD    . LYS A 1 289 ? 10.8    55.277  -9.499  1   31.75  ? 290  LYS A CD    1 1 
ATOM   2379 C  CE    . LYS A 1 289 ? 10.973  56.646  -10.124 1   36.93  ? 290  LYS A CE    1 1 
ATOM   2380 N  NZ    . LYS A 1 289 ? 11.789  56.583  -11.368 1   38.76  ? 290  LYS A NZ    1 1 
ATOM   2381 N  N     . VAL A 1 290 ? 9.137   52.036  -4.63   1   21.22  ? 291  VAL A N     1 1 
ATOM   2382 C  CA    . VAL A 1 290 ? 8.615   50.765  -4.151  1   20.94  ? 291  VAL A CA    1 1 
ATOM   2383 C  C     . VAL A 1 290 ? 7.11    50.754  -4.036  1   21.44  ? 291  VAL A C     1 1 
ATOM   2384 O  O     . VAL A 1 290 ? 6.484   49.822  -4.556  1   21.69  ? 291  VAL A O     1 1 
ATOM   2385 C  CB    . VAL A 1 290 ? 9.314   50.341  -2.844  1   21.69  ? 291  VAL A CB    1 1 
ATOM   2386 C  CG1   . VAL A 1 290 ? 8.659   49.092  -2.233  1   22.28  ? 291  VAL A CG1   1 1 
ATOM   2387 C  CG2   . VAL A 1 290 ? 10.805  50.096  -3.114  1   22.3   ? 291  VAL A CG2   1 1 
ATOM   2388 N  N     . LYS A 1 291 ? 6.509   51.802  -3.42   1   20.88  ? 292  LYS A N     1 1 
ATOM   2389 C  CA    . LYS A 1 291 ? 5.047   51.866  -3.264  1   21.07  ? 292  LYS A CA    1 1 
ATOM   2390 C  C     . LYS A 1 291 ? 4.321   51.851  -4.6    1   21.34  ? 292  LYS A C     1 1 
ATOM   2391 O  O     . LYS A 1 291 ? 3.363   51.11   -4.749  1   22.46  ? 292  LYS A O     1 1 
ATOM   2392 C  CB    . LYS A 1 291 ? 4.619   53.074  -2.414  1   22.41  ? 292  LYS A CB    1 1 
ATOM   2393 C  CG    . LYS A 1 291 ? 3.132   53.119  -2.113  1   27.06  ? 292  LYS A CG    1 1 
ATOM   2394 C  CD    . LYS A 1 291 ? 2.835   54.159  -1.042  1   33.73  ? 292  LYS A CD    1 1 
ATOM   2395 C  CE    . LYS A 1 291 ? 1.356   54.401  -0.836  1   40     ? 292  LYS A CE    1 1 
ATOM   2396 N  NZ    . LYS A 1 291 ? 0.595   53.121  -0.705  1   45.4   ? 292  LYS A NZ    1 1 
ATOM   2397 N  N     . GLU A 1 292 ? 4.825   52.58   -5.591  1   20.88  ? 293  GLU A N     1 1 
ATOM   2398 C  CA    . GLU A 1 292 ? 4.216   52.61   -6.915  1   21.33  ? 293  GLU A CA    1 1 
ATOM   2399 C  C     . GLU A 1 292 ? 4.406   51.284  -7.659  1   20.7   ? 293  GLU A C     1 1 
ATOM   2400 O  O     . GLU A 1 292 ? 3.509   50.877  -8.397  1   20.66  ? 293  GLU A O     1 1 
ATOM   2401 C  CB    . GLU A 1 292 ? 4.725   53.821  -7.724  1   24.94  ? 293  GLU A CB    1 1 
ATOM   2402 C  CG    . GLU A 1 292 ? 3.888   54.183  -8.953  1   35.62  ? 293  GLU A CG    1 1 
ATOM   2403 C  CD    . GLU A 1 292 ? 2.393   53.898  -8.976  1   47.24  ? 293  GLU A CD    1 1 
ATOM   2404 O  OE1   . GLU A 1 292 ? 1.974   53.066  -9.816  1   49.22  ? 293  GLU A OE1   1 1 
ATOM   2405 O  OE2   . GLU A 1 292 ? 1.642   54.504  -8.171  1   50.66  ? 293  GLU A OE2   1 1 
ATOM   2406 N  N     . PHE A 1 293 ? 5.529   50.574  -7.426  1   19.79  ? 294  PHE A N     1 1 
ATOM   2407 C  CA    . PHE A 1 293 ? 5.72    49.249  -8.035  1   19.58  ? 294  PHE A CA    1 1 
ATOM   2408 C  C     . PHE A 1 293 ? 4.711   48.283  -7.444  1   19.65  ? 294  PHE A C     1 1 
ATOM   2409 O  O     . PHE A 1 293 ? 4.088   47.498  -8.175  1   19.82  ? 294  PHE A O     1 1 
ATOM   2410 C  CB    . PHE A 1 293 ? 7.153   48.704  -7.799  1   19.53  ? 294  PHE A CB    1 1 
ATOM   2411 C  CG    . PHE A 1 293 ? 7.325   47.312  -8.357  1   19.73  ? 294  PHE A CG    1 1 
ATOM   2412 C  CD1   . PHE A 1 293 ? 7.494   47.112  -9.712  1   20.43  ? 294  PHE A CD1   1 1 
ATOM   2413 C  CD2   . PHE A 1 293 ? 7.213   46.198  -7.537  1   20.4   ? 294  PHE A CD2   1 1 
ATOM   2414 C  CE1   . PHE A 1 293 ? 7.594   45.822  -10.231 1   21.43  ? 294  PHE A CE1   1 1 
ATOM   2415 C  CE2   . PHE A 1 293 ? 7.343   44.912  -8.056  1   21.16  ? 294  PHE A CE2   1 1 
ATOM   2416 C  CZ    . PHE A 1 293 ? 7.525   44.731  -9.397  1   21.02  ? 294  PHE A CZ    1 1 
ATOM   2417 N  N     . ASN A 1 294 ? 4.527   48.325  -6.112  1   19.43  ? 295  ASN A N     1 1 
ATOM   2418 C  CA    . ASN A 1 294 ? 3.545   47.461  -5.461  1   19.23  ? 295  ASN A CA    1 1 
ATOM   2419 C  C     . ASN A 1 294 ? 2.129   47.72   -6.01   1   20.78  ? 295  ASN A C     1 1 
ATOM   2420 O  O     . ASN A 1 294 ? 1.39    46.758  -6.239  1   21.03  ? 295  ASN A O     1 1 
ATOM   2421 C  CB    . ASN A 1 294 ? 3.599   47.607  -3.939  1   19.11  ? 295  ASN A CB    1 1 
ATOM   2422 C  CG    . ASN A 1 294 ? 3.106   46.381  -3.197  1   19.43  ? 295  ASN A CG    1 1 
ATOM   2423 O  OD1   . ASN A 1 294 ? 2.847   45.33   -3.784  1   19.27  ? 295  ASN A OD1   1 1 
ATOM   2424 N  ND2   . ASN A 1 294 ? 2.962   46.482  -1.893  1   18.89  ? 295  ASN A ND2   1 1 
ATOM   2425 N  N     . ASN A 1 295 ? 1.789   49.005  -6.312  1   21.14  ? 296  ASN A N     1 1 
ATOM   2426 C  CA    . ASN A 1 295 ? 0.505   49.379  -6.918  1   21.78  ? 296  ASN A CA    1 1 
ATOM   2427 C  C     . ASN A 1 295 ? 0.353   48.736  -8.302  1   20.69  ? 296  ASN A C     1 1 
ATOM   2428 O  O     . ASN A 1 295 ? -0.712  48.22   -8.619  1   20.52  ? 296  ASN A O     1 1 
ATOM   2429 C  CB    . ASN A 1 295 ? 0.393   50.903  -7.054  1   26.38  ? 296  ASN A CB    1 1 
ATOM   2430 C  CG    . ASN A 1 295 ? 0.246   51.68   -5.756  1   35.38  ? 296  ASN A CG    1 1 
ATOM   2431 O  OD1   . ASN A 1 295 ? 0.602   52.871  -5.665  1   38.7   ? 296  ASN A OD1   1 1 
ATOM   2432 N  ND2   . ASN A 1 295 ? -0.281  51.047  -4.721  1   37.17  ? 296  ASN A ND2   1 1 
ATOM   2433 N  N     . ILE A 1 296 ? 1.418   48.739  -9.116  1   20.28  ? 297  ILE A N     1 1 
ATOM   2434 C  CA    . ILE A 1 296 ? 1.409   48.135  -10.448 1   20.54  ? 297  ILE A CA    1 1 
ATOM   2435 C  C     . ILE A 1 296 ? 1.221   46.621  -10.375 1   21.98  ? 297  ILE A C     1 1 
ATOM   2436 O  O     . ILE A 1 296 ? 0.413   46.045  -11.133 1   21.89  ? 297  ILE A O     1 1 
ATOM   2437 C  CB    . ILE A 1 296 ? 2.672   48.537  -11.226 1   20.59  ? 297  ILE A CB    1 1 
ATOM   2438 C  CG1   . ILE A 1 296 ? 2.672   50.045  -11.512 1   21.44  ? 297  ILE A CG1   1 1 
ATOM   2439 C  CG2   . ILE A 1 296 ? 2.833   47.708  -12.507 1   20.67  ? 297  ILE A CG2   1 1 
ATOM   2440 C  CD1   . ILE A 1 296 ? 4.075   50.553  -11.919 1   23.08  ? 297  ILE A CD1   1 1 
ATOM   2441 N  N     . VAL A 1 297 ? 1.905   45.959  -9.41   1   21.79  ? 298  VAL A N     1 1 
ATOM   2442 C  CA    . VAL A 1 297 ? 1.688   44.522  -9.207  1   21.46  ? 298  VAL A CA    1 1 
ATOM   2443 C  C     . VAL A 1 297 ? 0.237   44.235  -8.835  1   22.06  ? 298  VAL A C     1 1 
ATOM   2444 O  O     . VAL A 1 297 ? -0.398  43.371  -9.446  1   23.09  ? 298  VAL A O     1 1 
ATOM   2445 C  CB    . VAL A 1 297 ? 2.671   43.923  -8.159  1   21.09  ? 298  VAL A CB    1 1 
ATOM   2446 C  CG1   . VAL A 1 297 ? 2.365   42.463  -7.884  1   20.1   ? 298  VAL A CG1   1 1 
ATOM   2447 C  CG2   . VAL A 1 297 ? 4.102   44.071  -8.627  1   20.96  ? 298  VAL A CG2   1 1 
ATOM   2448 N  N     . GLN A 1 298 ? -0.314  44.993  -7.878  1   21.36  ? 299  GLN A N     1 1 
ATOM   2449 C  CA    . GLN A 1 298 ? -1.691  44.774  -7.44   1   21.88  ? 299  GLN A CA    1 1 
ATOM   2450 C  C     . GLN A 1 298 ? -2.754  45.165  -8.52   1   22.17  ? 299  GLN A C     1 1 
ATOM   2451 O  O     . GLN A 1 298 ? -3.89   44.735  -8.43   1   22.67  ? 299  GLN A O     1 1 
ATOM   2452 C  CB    . GLN A 1 298 ? -1.943  45.47   -6.095  1   23.36  ? 299  GLN A CB    1 1 
ATOM   2453 C  CG    . GLN A 1 298 ? -0.99   44.992  -5.018  1   24.46  ? 299  GLN A CG    1 1 
ATOM   2454 C  CD    . GLN A 1 298 ? -1.371  45.431  -3.629  1   26.25  ? 299  GLN A CD    1 1 
ATOM   2455 O  OE1   . GLN A 1 298 ? -2.532  45.688  -3.345  1   29.54  ? 299  GLN A OE1   1 1 
ATOM   2456 N  NE2   . GLN A 1 298 ? -0.407  45.502  -2.715  1   24.89  ? 299  GLN A NE2   1 1 
ATOM   2457 N  N     . ARG A 1 299 ? -2.364  45.915  -9.552  1   21.17  ? 300  ARG A N     1 1 
ATOM   2458 C  CA    . ARG A 1 299 ? -3.222  46.273  -10.677 1   21.36  ? 300  ARG A CA    1 1 
ATOM   2459 C  C     . ARG A 1 299 ? -3.442  45.078  -11.634 1   21.94  ? 300  ARG A C     1 1 
ATOM   2460 O  O     . ARG A 1 299 ? -4.452  45.028  -12.325 1   23.02  ? 300  ARG A O     1 1 
ATOM   2461 C  CB    . ARG A 1 299 ? -2.543  47.422  -11.467 1   22.33  ? 300  ARG A CB    1 1 
ATOM   2462 C  CG    . ARG A 1 299 ? -3.349  47.981  -12.647 1   25.01  ? 300  ARG A CG    1 1 
ATOM   2463 C  CD    . ARG A 1 299 ? -2.702  49.206  -13.258 1   27.7   ? 300  ARG A CD    1 1 
ATOM   2464 N  NE    . ARG A 1 299 ? -2.541  50.283  -12.275 1   31.19  ? 300  ARG A NE    1 1 
ATOM   2465 C  CZ    . ARG A 1 299 ? -1.509  51.121  -12.238 1   34.89  ? 300  ARG A CZ    1 1 
ATOM   2466 N  NH1   . ARG A 1 299 ? -0.547  51.043  -13.149 1   33.62  ? 300  ARG A NH1   1 1 
ATOM   2467 N  NH2   . ARG A 1 299 ? -1.439  52.057  -11.301 1   36.68  ? 300  ARG A NH2   1 1 
ATOM   2468 N  N     . TYR A 1 300 ? -2.478  44.166  -11.729 1   21.53  ? 301  TYR A N     1 1 
ATOM   2469 C  CA    . TYR A 1 300 ? -2.529  43.073  -12.693 1   21.6   ? 301  TYR A CA    1 1 
ATOM   2470 C  C     . TYR A 1 300 ? -2.495  41.683  -12.11  1   21.03  ? 301  TYR A C     1 1 
ATOM   2471 O  O     . TYR A 1 300 ? -2.869  40.746  -12.799 1   21.21  ? 301  TYR A O     1 1 
ATOM   2472 C  CB    . TYR A 1 300 ? -1.341  43.189  -13.678 1   21.33  ? 301  TYR A CB    1 1 
ATOM   2473 C  CG    . TYR A 1 300 ? -1.35   44.475  -14.468 1   22.33  ? 301  TYR A CG    1 1 
ATOM   2474 C  CD1   . TYR A 1 300 ? -2.275  44.682  -15.483 1   24.1   ? 301  TYR A CD1   1 1 
ATOM   2475 C  CD2   . TYR A 1 300 ? -0.496  45.517  -14.147 1   22.62  ? 301  TYR A CD2   1 1 
ATOM   2476 C  CE1   . TYR A 1 300 ? -2.333  45.886  -16.175 1   24.63  ? 301  TYR A CE1   1 1 
ATOM   2477 C  CE2   . TYR A 1 300 ? -0.52   46.71   -14.855 1   24.01  ? 301  TYR A CE2   1 1 
ATOM   2478 C  CZ    . TYR A 1 300 ? -1.441  46.892  -15.874 1   25.51  ? 301  TYR A CZ    1 1 
ATOM   2479 O  OH    . TYR A 1 300 ? -1.504  48.079  -16.577 1   27.24  ? 301  TYR A OH    1 1 
ATOM   2480 N  N     . SER A 1 301 ? -2.01   41.527  -10.895 1   20.98  ? 302  SER A N     1 1 
ATOM   2481 C  CA    . SER A 1 301 ? -1.762  40.197  -10.319 1   21.52  ? 302  SER A CA    1 1 
ATOM   2482 C  C     . SER A 1 301 ? -2.981  39.359  -9.963  1   22.07  ? 302  SER A C     1 1 
ATOM   2483 O  O     . SER A 1 301 ? -4.072  39.879  -9.716  1   22.16  ? 302  SER A O     1 1 
ATOM   2484 C  CB    . SER A 1 301 ? -0.873  40.309  -9.081  1   22.96  ? 302  SER A CB    1 1 
ATOM   2485 O  OG    . SER A 1 301 ? -1.642  40.815  -7.998  1   26.69  ? 302  SER A OG    1 1 
ATOM   2486 N  N     . VAL A 1 302 ? -2.765  38.03   -9.941  1   21.85  ? 303  VAL A N     1 1 
ATOM   2487 C  CA    . VAL A 1 302 ? -3.694  37.027  -9.47   1   22.04  ? 303  VAL A CA    1 1 
ATOM   2488 C  C     . VAL A 1 302 ? -2.928  36.304  -8.345  1   22.14  ? 303  VAL A C     1 1 
ATOM   2489 O  O     . VAL A 1 302 ? -1.712  36.157  -8.412  1   23.13  ? 303  VAL A O     1 1 
ATOM   2490 C  CB    . VAL A 1 302 ? -4.22   36.095  -10.586 1   22.84  ? 303  VAL A CB    1 1 
ATOM   2491 C  CG1   . VAL A 1 302 ? -5.069  36.877  -11.571 1   23.57  ? 303  VAL A CG1   1 1 
ATOM   2492 C  CG2   . VAL A 1 302 ? -3.09   35.389  -11.312 1   23.04  ? 303  VAL A CG2   1 1 
ATOM   2493 N  N     . GLY A 1 303 ? -3.619  35.964  -7.282  1   21.52  ? 304  GLY A N     1 1 
ATOM   2494 C  CA    . GLY A 1 303 ? -2.991  35.346  -6.123  1   21.42  ? 304  GLY A CA    1 1 
ATOM   2495 C  C     . GLY A 1 303 ? -2.531  33.926  -6.346  1   21.02  ? 304  GLY A C     1 1 
ATOM   2496 O  O     . GLY A 1 303 ? -3.186  33.174  -7.069  1   21.95  ? 304  GLY A O     1 1 
ATOM   2497 N  N     . LEU A 1 304 ? -1.405  33.547  -5.729  1   19.49  ? 305  LEU A N     1 1 
ATOM   2498 C  CA    . LEU A 1 304 ? -0.897  32.173  -5.816  1   20.22  ? 305  LEU A CA    1 1 
ATOM   2499 C  C     . LEU A 1 304 ? -0.952  31.653  -4.4    1   19.19  ? 305  LEU A C     1 1 
ATOM   2500 O  O     . LEU A 1 304 ? -0.181  32.112  -3.568  1   19.54  ? 305  LEU A O     1 1 
ATOM   2501 C  CB    . LEU A 1 304 ? 0.559   32.163  -6.314  1   21.28  ? 305  LEU A CB    1 1 
ATOM   2502 C  CG    . LEU A 1 304 ? 1.18    30.844  -6.683  1   25     ? 305  LEU A CG    1 1 
ATOM   2503 C  CD1   . LEU A 1 304 ? 0.52    30.277  -7.885  1   27     ? 305  LEU A CD1   1 1 
ATOM   2504 C  CD2   . LEU A 1 304 ? 2.62    31.03   -7.023  1   26.29  ? 305  LEU A CD2   1 1 
ATOM   2505 N  N     . ALA A 1 305 ? -1.911  30.756  -4.106  1   18.17  ? 306  ALA A N     1 1 
ATOM   2506 C  CA    . ALA A 1 305 ? -2.166  30.106  -2.808  1   18.01  ? 306  ALA A CA    1 1 
ATOM   2507 C  C     . ALA A 1 305 ? -2.776  31.008  -1.731  1   17.79  ? 306  ALA A C     1 1 
ATOM   2508 O  O     . ALA A 1 305 ? -3.658  30.562  -1.015  1   17.15  ? 306  ALA A O     1 1 
ATOM   2509 C  CB    . ALA A 1 305 ? -0.923  29.424  -2.268  1   18.68  ? 306  ALA A CB    1 1 
ATOM   2510 N  N     . SER A 1 306 ? -2.242  32.222  -1.55   1   18.03  ? 307  SER A N     1 1 
ATOM   2511 C  CA    . SER A 1 306 ? -2.695  33.217  -0.576  1   18.61  ? 307  SER A CA    1 1 
ATOM   2512 C  C     . SER A 1 306 ? -2.423  34.599  -1.127  1   19.16  ? 307  SER A C     1 1 
ATOM   2513 O  O     . SER A 1 306 ? -1.421  34.819  -1.812  1   18.38  ? 307  SER A O     1 1 
ATOM   2514 C  CB    . SER A 1 306 ? -1.941  33.08   0.738   1   20.06  ? 307  SER A CB    1 1 
ATOM   2515 O  OG    . SER A 1 306 ? -2.279  31.852  1.353   1   22.25  ? 307  SER A OG    1 1 
ATOM   2516 N  N     . SER A 1 307 ? -3.318  35.541  -0.826  1   20.22  ? 308  SER A N     1 1 
ATOM   2517 C  CA    . SER A 1 307 ? -3.163  36.894  -1.302  1   20.6   ? 308  SER A CA    1 1 
ATOM   2518 C  C     . SER A 1 307 ? -1.926  37.552  -0.665  1   21.04  ? 308  SER A C     1 1 
ATOM   2519 O  O     . SER A 1 307 ? -1.272  38.352  -1.33   1   21.5   ? 308  SER A O     1 1 
ATOM   2520 C  CB    . SER A 1 307 ? -4.423  37.694  -0.998  1   23.07  ? 308  SER A CB    1 1 
ATOM   2521 O  OG    . SER A 1 307 ? -4.6    37.782  0.404   1   27.19  ? 308  SER A OG    1 1 
ATOM   2522 N  N     . ASP A 1 308 ? -1.58   37.199  0.599   1   19.9   ? 309  ASP A N     1 1 
ATOM   2523 C  CA    . ASP A 1 308 ? -0.47   37.869  1.257   1   19.67  ? 309  ASP A CA    1 1 
ATOM   2524 C  C     . ASP A 1 308 ? 0.791   37.019  1.389   1   19.55  ? 309  ASP A C     1 1 
ATOM   2525 O  O     . ASP A 1 308 ? 1.718   37.427  2.101   1   20.02  ? 309  ASP A O     1 1 
ATOM   2526 C  CB    . ASP A 1 308 ? -0.859  38.492  2.601   1   21.65  ? 309  ASP A CB    1 1 
ATOM   2527 C  CG    . ASP A 1 308 ? -1.3    37.502  3.652   1   28.63  ? 309  ASP A CG    1 1 
ATOM   2528 O  OD1   . ASP A 1 308 ? -1.641  36.354  3.282   1   30.45  ? 309  ASP A OD1   1 1 
ATOM   2529 O  OD2   . ASP A 1 308 ? -1.313  37.872  4.849   1   30.63  ? 309  ASP A OD2   1 1 
ATOM   2530 N  N     . LEU A 1 309 ? 0.916   35.945  0.595   1   18.78  ? 310  LEU A N     1 1 
ATOM   2531 C  CA    . LEU A 1 309 ? 2.204   35.236  0.51    1   19.25  ? 310  LEU A CA    1 1 
ATOM   2532 C  C     . LEU A 1 309 ? 3.135   36.226  -0.298  1   18.95  ? 310  LEU A C     1 1 
ATOM   2533 O  O     . LEU A 1 309 ? 2.6     37.09   -1.008  1   18.69  ? 310  LEU A O     1 1 
ATOM   2534 C  CB    . LEU A 1 309 ? 2.046   33.878  -0.219  1   18.9   ? 310  LEU A CB    1 1 
ATOM   2535 C  CG    . LEU A 1 309 ? 1.672   32.687  0.679   1   19.31  ? 310  LEU A CG    1 1 
ATOM   2536 C  CD1   . LEU A 1 309 ? 1.445   31.421  -0.145  1   19.28  ? 310  LEU A CD1   1 1 
ATOM   2537 C  CD2   . LEU A 1 309 ? 2.754   32.432  1.75    1   20.01  ? 310  LEU A CD2   1 1 
ATOM   2538 N  N     . PRO A 1 310 ? 4.478   36.178  -0.18   1   18.95  ? 311  PRO A N     1 1 
ATOM   2539 C  CA    . PRO A 1 310 ? 5.304   37.185  -0.9    1   18.59  ? 311  PRO A CA    1 1 
ATOM   2540 C  C     . PRO A 1 310 ? 5.459   36.95   -2.403  1   18.65  ? 311  PRO A C     1 1 
ATOM   2541 O  O     . PRO A 1 310 ? 6.45    37.399  -2.968  1   20.25  ? 311  PRO A O     1 1 
ATOM   2542 C  CB    . PRO A 1 310 ? 6.658   37.113  -0.182  1   18.97  ? 311  PRO A CB    1 1 
ATOM   2543 C  CG    . PRO A 1 310 ? 6.733   35.675  0.293   1   18.76  ? 311  PRO A CG    1 1 
ATOM   2544 C  CD    . PRO A 1 310 ? 5.31    35.276  0.655   1   17.28  ? 311  PRO A CD    1 1 
ATOM   2545 N  N     . PHE A 1 311 ? 4.534   36.244  -3.04   1   17.72  ? 312  PHE A N     1 1 
ATOM   2546 C  CA    . PHE A 1 311 ? 4.608   35.981  -4.474  1   18.27  ? 312  PHE A CA    1 1 
ATOM   2547 C  C     . PHE A 1 311 ? 3.225   35.82   -5.082  1   19.37  ? 312  PHE A C     1 1 
ATOM   2548 O  O     . PHE A 1 311 ? 2.276   35.446  -4.401  1   20.51  ? 312  PHE A O     1 1 
ATOM   2549 C  CB    . PHE A 1 311 ? 5.496   34.751  -4.813  1   17.81  ? 312  PHE A CB    1 1 
ATOM   2550 C  CG    . PHE A 1 311 ? 5.235   33.565  -3.923  1   18.24  ? 312  PHE A CG    1 1 
ATOM   2551 C  CD1   . PHE A 1 311 ? 4.138   32.747  -4.135  1   18.84  ? 312  PHE A CD1   1 1 
ATOM   2552 C  CD2   . PHE A 1 311 ? 6.076   33.279  -2.858  1   18.64  ? 312  PHE A CD2   1 1 
ATOM   2553 C  CE1   . PHE A 1 311 ? 3.885   31.674  -3.299  1   19.52  ? 312  PHE A CE1   1 1 
ATOM   2554 C  CE2   . PHE A 1 311 ? 5.814   32.205  -2.021  1   19.48  ? 312  PHE A CE2   1 1 
ATOM   2555 C  CZ    . PHE A 1 311 ? 4.723   31.413  -2.244  1   19.18  ? 312  PHE A CZ    1 1 
ATOM   2556 N  N     . GLY A 1 312 ? 3.127   36.098  -6.366  1   19.78  ? 313  GLY A N     1 1 
ATOM   2557 C  CA    . GLY A 1 312 ? 1.891   35.982  -7.122  1   20.93  ? 313  GLY A CA    1 1 
ATOM   2558 C  C     . GLY A 1 312 ? 2.145   35.82   -8.6    1   21.7   ? 313  GLY A C     1 1 
ATOM   2559 O  O     . GLY A 1 312 ? 3.297   35.632  -9.014  1   22.99  ? 313  GLY A O     1 1 
ATOM   2560 N  N     . VAL A 1 313 ? 1.088   35.864  -9.407  1   21.02  ? 314  VAL A N     1 1 
ATOM   2561 C  CA    . VAL A 1 313 ? 1.236   35.669  -10.838 1   22.13  ? 314  VAL A CA    1 1 
ATOM   2562 C  C     . VAL A 1 313 ? 0.735   36.856  -11.637 1   22.58  ? 314  VAL A C     1 1 
ATOM   2563 O  O     . VAL A 1 313 ? -0.256  37.465  -11.26  1   23.01  ? 314  VAL A O     1 1 
ATOM   2564 C  CB    . VAL A 1 313 ? 0.511   34.363  -11.289 1   23.81  ? 314  VAL A CB    1 1 
ATOM   2565 C  CG1   . VAL A 1 313 ? 0.71    34.1    -12.782 1   24.52  ? 314  VAL A CG1   1 1 
ATOM   2566 C  CG2   . VAL A 1 313 ? 0.956   33.162  -10.448 1   24.27  ? 314  VAL A CG2   1 1 
ATOM   2567 N  N     . ILE A 1 314 ? 1.424   37.182  -12.735 1   22.24  ? 315  ILE A N     1 1 
ATOM   2568 C  CA    . ILE A 1 314 ? 0.982   38.12   -13.744 1   23.47  ? 315  ILE A CA    1 1 
ATOM   2569 C  C     . ILE A 1 314 ? 0.722   37.209  -14.96  1   24.11  ? 315  ILE A C     1 1 
ATOM   2570 O  O     . ILE A 1 314 ? 1.684   36.729  -15.564 1   24.69  ? 315  ILE A O     1 1 
ATOM   2571 C  CB    . ILE A 1 314 ? 2.004   39.223  -14.09  1   24.52  ? 315  ILE A CB    1 1 
ATOM   2572 C  CG1   . ILE A 1 314 ? 2.435   40.045  -12.844 1   24.64  ? 315  ILE A CG1   1 1 
ATOM   2573 C  CG2   . ILE A 1 314 ? 1.447   40.118  -15.207 1   25.89  ? 315  ILE A CG2   1 1 
ATOM   2574 C  CD1   . ILE A 1 314 ? 1.392   40.939  -12.238 1   25.2   ? 315  ILE A CD1   1 1 
ATOM   2575 N  N     . ARG A 1 315 ? -0.56   36.904  -15.276 1   23.74  ? 316  ARG A N     1 1 
ATOM   2576 C  CA    . ARG A 1 315 ? -0.9    36.043  -16.42  1   24.32  ? 316  ARG A CA    1 1 
ATOM   2577 C  C     . ARG A 1 315 ? -0.362  36.62   -17.731 1   24.83  ? 316  ARG A C     1 1 
ATOM   2578 O  O     . ARG A 1 315 ? -0.184  37.84   -17.816 1   24.36  ? 316  ARG A O     1 1 
ATOM   2579 C  CB    . ARG A 1 315 ? -2.41   35.788  -16.505 1   25.06  ? 316  ARG A CB    1 1 
ATOM   2580 N  N     . LYS A 1 316 ? -0.049  35.762  -18.743 1   25.34  ? 317  LYS A N     1 1 
ATOM   2581 C  CA    . LYS A 1 316 ? 0.515   36.285  -20.01  1   26.37  ? 317  LYS A CA    1 1 
ATOM   2582 C  C     . LYS A 1 316 ? -0.404  37.337  -20.668 1   27.16  ? 317  LYS A C     1 1 
ATOM   2583 O  O     . LYS A 1 316 ? 0.082   38.276  -21.311 1   27.98  ? 317  LYS A O     1 1 
ATOM   2584 C  CB    . LYS A 1 316 ? 0.859   35.15   -20.998 1   27.6   ? 317  LYS A CB    1 1 
ATOM   2585 C  CG    . LYS A 1 316 ? -0.315  34.3    -21.412 1   30.24  ? 317  LYS A CG    1 1 
ATOM   2586 C  CD    . LYS A 1 316 ? 0.06    33.305  -22.504 1   35.17  ? 317  LYS A CD    1 1 
ATOM   2587 C  CE    . LYS A 1 316 ? -1.152  32.521  -22.949 1   39.72  ? 317  LYS A CE    1 1 
ATOM   2588 N  NZ    . LYS A 1 316 ? -0.873  31.655  -24.122 1   43.53  ? 317  LYS A NZ    1 1 
ATOM   2589 N  N     . GLU A 1 317 ? -1.729  37.207  -20.446 1   26.44  ? 318  GLU A N     1 1 
ATOM   2590 C  CA    . GLU A 1 317 ? -2.734  38.129  -20.96  1   26.21  ? 318  GLU A CA    1 1 
ATOM   2591 C  C     . GLU A 1 317 ? -2.61   39.541  -20.356 1   25.33  ? 318  GLU A C     1 1 
ATOM   2592 O  O     . GLU A 1 317 ? -3.2    40.477  -20.894 1   26.21  ? 318  GLU A O     1 1 
ATOM   2593 C  CB    . GLU A 1 317 ? -4.149  37.568  -20.716 1   28.02  ? 318  GLU A CB    1 1 
ATOM   2594 C  CG    . GLU A 1 317 ? -4.468  36.339  -21.557 1   33.55  ? 318  GLU A CG    1 1 
ATOM   2595 C  CD    . GLU A 1 317 ? -3.952  35.017  -21.018 1   38.91  ? 318  GLU A CD    1 1 
ATOM   2596 O  OE1   . GLU A 1 317 ? -3.454  34.997  -19.868 1   39.08  ? 318  GLU A OE1   1 1 
ATOM   2597 O  OE2   . GLU A 1 317 ? -4.05   33.997  -21.741 1   41.59  ? 318  GLU A OE2   1 1 
ATOM   2598 N  N     . SER A 1 318 ? -1.905  39.689  -19.233 1   23.38  ? 319  SER A N     1 1 
ATOM   2599 C  CA    . SER A 1 318 ? -1.706  40.984  -18.596 1   23.58  ? 319  SER A CA    1 1 
ATOM   2600 C  C     . SER A 1 318 ? -0.234  41.425  -18.568 1   23.43  ? 319  SER A C     1 1 
ATOM   2601 O  O     . SER A 1 318 ? 0.047   42.53   -18.144 1   23.13  ? 319  SER A O     1 1 
ATOM   2602 C  CB    . SER A 1 318 ? -2.256  40.971  -17.176 1   25.48  ? 319  SER A CB    1 1 
ATOM   2603 O  OG    . SER A 1 318 ? -3.674  40.955  -17.172 1   28.59  ? 319  SER A OG    1 1 
ATOM   2604 N  N     . ARG A 1 319 ? 0.697   40.566  -19.012 1   23.89  ? 320  ARG A N     1 1 
ATOM   2605 C  CA    . ARG A 1 319 ? 2.132   40.792  -18.984 1   24.04  ? 320  ARG A CA    1 1 
ATOM   2606 C  C     . ARG A 1 319 ? 2.577   42.007  -19.764 1   25.19  ? 320  ARG A C     1 1 
ATOM   2607 O  O     . ARG A 1 319 ? 3.367   42.781  -19.239 1   25.44  ? 320  ARG A O     1 1 
ATOM   2608 C  CB    . ARG A 1 319 ? 2.877   39.54   -19.441 1   24.88  ? 320  ARG A CB    1 1 
ATOM   2609 C  CG    . ARG A 1 319 ? 4.386   39.676  -19.305 1   26.9   ? 320  ARG A CG    1 1 
ATOM   2610 C  CD    . ARG A 1 319 ? 5.043   38.324  -19.351 1   27.49  ? 320  ARG A CD    1 1 
ATOM   2611 N  NE    . ARG A 1 319 ? 6.502   38.448  -19.286 1   29.33  ? 320  ARG A NE    1 1 
ATOM   2612 C  CZ    . ARG A 1 319 ? 7.328   37.43   -19.063 1   30.3   ? 320  ARG A CZ    1 1 
ATOM   2613 N  NH1   . ARG A 1 319 ? 6.85    36.206  -18.868 1   29.68  ? 320  ARG A NH1   1 1 
ATOM   2614 N  NH2   . ARG A 1 319 ? 8.638   37.629  -19.029 1   28.39  ? 320  ARG A NH2   1 1 
ATOM   2615 N  N     . ASN A 1 320 ? 2.055   42.225  -20.984 1   25.85  ? 321  ASN A N     1 1 
ATOM   2616 C  CA    . ASN A 1 320 ? 2.397   43.416  -21.779 1   26.32  ? 321  ASN A CA    1 1 
ATOM   2617 C  C     . ASN A 1 320 ? 2.103   44.708  -21.01  1   26.5   ? 321  ASN A C     1 1 
ATOM   2618 O  O     . ASN A 1 320 ? 2.932   45.615  -20.981 1   26.82  ? 321  ASN A O     1 1 
ATOM   2619 C  CB    . ASN A 1 320 ? 1.621   43.429  -23.112 1   28.29  ? 321  ASN A CB    1 1 
ATOM   2620 C  CG    . ASN A 1 320 ? 1.949   44.63   -23.981 1   34.28  ? 321  ASN A CG    1 1 
ATOM   2621 O  OD1   . ASN A 1 320 ? 2.943   44.624  -24.726 1   36.52  ? 321  ASN A OD1   1 1 
ATOM   2622 N  ND2   . ASN A 1 320 ? 1.143   45.702  -23.899 1   35.02  ? 321  ASN A ND2   1 1 
ATOM   2623 N  N     . ASP A 1 321 ? 0.916   44.799  -20.406 1   26.17  ? 322  ASP A N     1 1 
ATOM   2624 C  CA    . ASP A 1 321 ? 0.508   46.012  -19.697 1   26.3   ? 322  ASP A CA    1 1 
ATOM   2625 C  C     . ASP A 1 321 ? 1.3     46.226  -18.41  1   25.17  ? 322  ASP A C     1 1 
ATOM   2626 O  O     . ASP A 1 321 ? 1.71    47.346  -18.11  1   24.62  ? 322  ASP A O     1 1 
ATOM   2627 C  CB    . ASP A 1 321 ? -1      46.001  -19.454 1   28.39  ? 322  ASP A CB    1 1 
ATOM   2628 C  CG    . ASP A 1 321 ? -1.821  46.051  -20.735 1   33.83  ? 322  ASP A CG    1 1 
ATOM   2629 O  OD1   . ASP A 1 321 ? -1.274  46.485  -21.778 1   35.59  ? 322  ASP A OD1   1 1 
ATOM   2630 O  OD2   . ASP A 1 321 ? -3.004  45.642  -20.7   1   34.81  ? 322  ASP A OD2   1 1 
ATOM   2631 N  N     . PHE A 1 322 ? 1.573   45.128  -17.684 1   24.29  ? 323  PHE A N     1 1 
ATOM   2632 C  CA    . PHE A 1 322 ? 2.37    45.164  -16.463 1   23.7   ? 323  PHE A CA    1 1 
ATOM   2633 C  C     . PHE A 1 322 ? 3.77    45.652  -16.808 1   23.75  ? 323  PHE A C     1 1 
ATOM   2634 O  O     . PHE A 1 322 ? 4.269   46.564  -16.155 1   24.12  ? 323  PHE A O     1 1 
ATOM   2635 C  CB    . PHE A 1 322 ? 2.42    43.765  -15.806 1   23.01  ? 323  PHE A CB    1 1 
ATOM   2636 C  CG    . PHE A 1 322 ? 3.501   43.598  -14.759 1   22.9   ? 323  PHE A CG    1 1 
ATOM   2637 C  CD1   . PHE A 1 322 ? 3.373   44.176  -13.509 1   23.62  ? 323  PHE A CD1   1 1 
ATOM   2638 C  CD2   . PHE A 1 322 ? 4.648   42.88   -15.032 1   22.79  ? 323  PHE A CD2   1 1 
ATOM   2639 C  CE1   . PHE A 1 322 ? 4.37    44.037  -12.554 1   24.01  ? 323  PHE A CE1   1 1 
ATOM   2640 C  CE2   . PHE A 1 322 ? 5.626   42.713  -14.063 1   23.4   ? 323  PHE A CE2   1 1 
ATOM   2641 C  CZ    . PHE A 1 322 ? 5.48    43.283  -12.828 1   23.33  ? 323  PHE A CZ    1 1 
ATOM   2642 N  N     . ILE A 1 323 ? 4.364   45.098  -17.877 1   23.21  ? 324  ILE A N     1 1 
ATOM   2643 C  CA    . ILE A 1 323 ? 5.692   45.497  -18.312 1   23.59  ? 324  ILE A CA    1 1 
ATOM   2644 C  C     . ILE A 1 323 ? 5.718   46.979  -18.709 1   23.71  ? 324  ILE A C     1 1 
ATOM   2645 O  O     . ILE A 1 323 ? 6.623   47.664  -18.266 1   24.27  ? 324  ILE A O     1 1 
ATOM   2646 C  CB    . ILE A 1 323 ? 6.284   44.55   -19.396 1   24.28  ? 324  ILE A CB    1 1 
ATOM   2647 C  CG1   . ILE A 1 323 ? 6.558   43.133  -18.807 1   25.03  ? 324  ILE A CG1   1 1 
ATOM   2648 C  CG2   . ILE A 1 323 ? 7.573   45.119  -20.014 1   24.56  ? 324  ILE A CG2   1 1 
ATOM   2649 C  CD1   . ILE A 1 323 ? 7.459   43.109  -17.519 1   25.43  ? 324  ILE A CD1   1 1 
ATOM   2650 N  N     . ASN A 1 324 ? 4.727   47.478  -19.476 1   23.12  ? 325  ASN A N     1 1 
ATOM   2651 C  CA    . ASN A 1 324 ? 4.666   48.888  -19.872 1   24.76  ? 325  ASN A CA    1 1 
ATOM   2652 C  C     . ASN A 1 324 ? 4.644   49.806  -18.651 1   25.57  ? 325  ASN A C     1 1 
ATOM   2653 O  O     . ASN A 1 324 ? 5.32    50.824  -18.648 1   26.48  ? 325  ASN A O     1 1 
ATOM   2654 C  CB    . ASN A 1 324 ? 3.419   49.193  -20.713 1   26.18  ? 325  ASN A CB    1 1 
ATOM   2655 C  CG    . ASN A 1 324 ? 3.447   48.676  -22.121 1   28.97  ? 325  ASN A CG    1 1 
ATOM   2656 O  OD1   . ASN A 1 324 ? 4.494   48.294  -22.642 1   29.17  ? 325  ASN A OD1   1 1 
ATOM   2657 N  ND2   . ASN A 1 324 ? 2.28    48.634  -22.76  1   29.73  ? 325  ASN A ND2   1 1 
ATOM   2658 N  N     . ASP A 1 325 ? 3.9     49.432  -17.611 1   25.37  ? 326  ASP A N     1 1 
ATOM   2659 C  CA    . ASP A 1 325 ? 3.832   50.228  -16.393 1   25.56  ? 326  ASP A CA    1 1 
ATOM   2660 C  C     . ASP A 1 325 ? 5.152   50.22   -15.605 1   25.39  ? 326  ASP A C     1 1 
ATOM   2661 O  O     . ASP A 1 325 ? 5.539   51.243  -15.048 1   25.27  ? 326  ASP A O     1 1 
ATOM   2662 C  CB    . ASP A 1 325 ? 2.636   49.775  -15.527 1   26.17  ? 326  ASP A CB    1 1 
ATOM   2663 C  CG    . ASP A 1 325 ? 1.292   50.247  -16.039 1   28.98  ? 326  ASP A CG    1 1 
ATOM   2664 O  OD1   . ASP A 1 325 ? 1.269   51.028  -17.011 1   30.23  ? 326  ASP A OD1   1 1 
ATOM   2665 O  OD2   . ASP A 1 325 ? 0.263   49.859  -15.448 1   29.11  ? 326  ASP A OD2   1 1 
ATOM   2666 N  N     . VAL A 1 326 ? 5.843   49.073  -15.566 1   25.05  ? 327  VAL A N     1 1 
ATOM   2667 C  CA    . VAL A 1 326 ? 7.136   48.993  -14.877 1   24.78  ? 327  VAL A CA    1 1 
ATOM   2668 C  C     . VAL A 1 326 ? 8.171   49.814  -15.628 1   24.4   ? 327  VAL A C     1 1 
ATOM   2669 O  O     . VAL A 1 326 ? 8.915   50.601  -15.022 1   23.05  ? 327  VAL A O     1 1 
ATOM   2670 C  CB    . VAL A 1 326 ? 7.585   47.528  -14.672 1   25.4   ? 327  VAL A CB    1 1 
ATOM   2671 C  CG1   . VAL A 1 326 ? 8.978   47.457  -14.057 1   25.86  ? 327  VAL A CG1   1 1 
ATOM   2672 C  CG2   . VAL A 1 326 ? 6.577   46.782  -13.806 1   25.98  ? 327  VAL A CG2   1 1 
ATOM   2673 N  N     . CYS A 1 327 ? 8.191   49.668  -16.954 1   25.19  ? 328  CYS A N     1 1 
ATOM   2674 C  CA    . CYS A 1 327 ? 9.123   50.409  -17.795 1   26.82  ? 328  CYS A CA    1 1 
ATOM   2675 C  C     . CYS A 1 327 ? 8.922   51.921  -17.69  1   27.62  ? 328  CYS A C     1 1 
ATOM   2676 O  O     . CYS A 1 327 ? 9.901   52.652  -17.62  1   27.53  ? 328  CYS A O     1 1 
ATOM   2677 C  CB    . CYS A 1 327 ? 9.054   49.923  -19.239 1   28.19  ? 328  CYS A CB    1 1 
ATOM   2678 S  SG    . CYS A 1 327 ? 9.697   48.248  -19.478 1   32.39  ? 328  CYS A SG    1 1 
ATOM   2679 N  N     . LYS A 1 328 ? 7.666   52.383  -17.64  1   28.09  ? 329  LYS A N     1 1 
ATOM   2680 C  CA    . LYS A 1 328 ? 7.35    53.803  -17.488 1   29.09  ? 329  LYS A CA    1 1 
ATOM   2681 C  C     . LYS A 1 328 ? 7.787   54.304  -16.1   1   28.75  ? 329  LYS A C     1 1 
ATOM   2682 O  O     . LYS A 1 328 ? 8.294   55.419  -15.986 1   29.89  ? 329  LYS A O     1 1 
ATOM   2683 C  CB    . LYS A 1 328 ? 5.841   54.03   -17.7   1   31.72  ? 329  LYS A CB    1 1 
ATOM   2684 C  CG    . LYS A 1 328 ? 5.374   55.483  -17.625 1   39.82  ? 329  LYS A CG    1 1 
ATOM   2685 C  CD    . LYS A 1 328 ? 6.071   56.373  -18.666 1   47.49  ? 329  LYS A CD    1 1 
ATOM   2686 C  CE    . LYS A 1 328 ? 5.441   57.747  -18.77  1   52.73  ? 329  LYS A CE    1 1 
ATOM   2687 N  NZ    . LYS A 1 328 ? 6.252   58.659  -19.628 1   56.17  ? 329  LYS A NZ    1 1 
ATOM   2688 N  N     . LEU A 1 329 ? 7.632   53.469  -15.062 1   26.97  ? 330  LEU A N     1 1 
ATOM   2689 C  CA    . LEU A 1 329 ? 7.987   53.822  -13.695 1   26.3   ? 330  LEU A CA    1 1 
ATOM   2690 C  C     . LEU A 1 329 ? 9.483   53.987  -13.492 1   25.95  ? 330  LEU A C     1 1 
ATOM   2691 O  O     . LEU A 1 329 ? 9.91    54.919  -12.832 1   25.45  ? 330  LEU A O     1 1 
ATOM   2692 C  CB    . LEU A 1 329 ? 7.413   52.802  -12.696 1   26.55  ? 330  LEU A CB    1 1 
ATOM   2693 C  CG    . LEU A 1 329 ? 7.698   53.069  -11.221 1   28.14  ? 330  LEU A CG    1 1 
ATOM   2694 C  CD1   . LEU A 1 329 ? 7.019   54.354  -10.75  1   28.5   ? 330  LEU A CD1   1 1 
ATOM   2695 C  CD2   . LEU A 1 329 ? 7.315   51.905  -10.349 1   28.42  ? 330  LEU A CD2   1 1 
ATOM   2696 N  N     . TYR A 1 330 ? 10.277  53.08   -14.053 1   25.68  ? 331  TYR A N     1 1 
ATOM   2697 C  CA    . TYR A 1 330 ? 11.711  53.092  -13.881 1   25.79  ? 331  TYR A CA    1 1 
ATOM   2698 C  C     . TYR A 1 330 ? 12.482  53.599  -15.084 1   27.77  ? 331  TYR A C     1 1 
ATOM   2699 O  O     . TYR A 1 330 ? 13.688  53.435  -15.107 1   28.36  ? 331  TYR A O     1 1 
ATOM   2700 C  CB    . TYR A 1 330 ? 12.195  51.698  -13.473 1   24.56  ? 331  TYR A CB    1 1 
ATOM   2701 C  CG    . TYR A 1 330 ? 11.753  51.321  -12.082 1   23.68  ? 331  TYR A CG    1 1 
ATOM   2702 C  CD1   . TYR A 1 330 ? 12.195  52.031  -10.979 1   23.68  ? 331  TYR A CD1   1 1 
ATOM   2703 C  CD2   . TYR A 1 330 ? 10.928  50.22   -11.864 1   24.01  ? 331  TYR A CD2   1 1 
ATOM   2704 C  CE1   . TYR A 1 330 ? 11.816  51.674  -9.694  1   24.18  ? 331  TYR A CE1   1 1 
ATOM   2705 C  CE2   . TYR A 1 330 ? 10.521  49.868  -10.581 1   24.19  ? 331  TYR A CE2   1 1 
ATOM   2706 C  CZ    . TYR A 1 330 ? 10.976  50.597  -9.497  1   24.41  ? 331  TYR A CZ    1 1 
ATOM   2707 O  OH    . TYR A 1 330 ? 10.594  50.283  -8.219  1   24.97  ? 331  TYR A OH    1 1 
ATOM   2708 N  N     . ASN A 1 331 ? 11.808  54.196  -16.076 1   29.23  ? 332  ASN A N     1 1 
ATOM   2709 C  CA    . ASN A 1 331 ? 12.452  54.745  -17.261 1   31.63  ? 332  ASN A CA    1 1 
ATOM   2710 C  C     . ASN A 1 331 ? 13.266  53.715  -18.065 1   32.86  ? 332  ASN A C     1 1 
ATOM   2711 O  O     . ASN A 1 331 ? 14.384  54.004  -18.483 1   33     ? 332  ASN A O     1 1 
ATOM   2712 C  CB    . ASN A 1 331 ? 13.31   55.97   -16.901 1   33.48  ? 332  ASN A CB    1 1 
ATOM   2713 C  CG    . ASN A 1 331 ? 13.484  56.921  -18.048 1   38.02  ? 332  ASN A CG    1 1 
ATOM   2714 O  OD1   . ASN A 1 331 ? 12.587  57.064  -18.888 1   39.24  ? 332  ASN A OD1   1 1 
ATOM   2715 N  ND2   . ASN A 1 331 ? 14.656  57.59   -18.113 1   39.3   ? 332  ASN A ND2   1 1 
ATOM   2716 N  N     . ILE A 1 332 ? 12.708  52.529  -18.297 1   33.47  ? 333  ILE A N     1 1 
ATOM   2717 C  CA    . ILE A 1 332 ? 13.397  51.498  -19.081 1   34.34  ? 333  ILE A CA    1 1 
ATOM   2718 C  C     . ILE A 1 332 ? 12.982  51.709  -20.522 1   35.8   ? 333  ILE A C     1 1 
ATOM   2719 O  O     . ILE A 1 332 ? 11.816  51.539  -20.857 1   36.09  ? 333  ILE A O     1 1 
ATOM   2720 C  CB    . ILE A 1 332 ? 13.034  50.09   -18.577 1   34.24  ? 333  ILE A CB    1 1 
ATOM   2721 C  CG1   . ILE A 1 332 ? 13.349  49.934  -17.078 1   34.57  ? 333  ILE A CG1   1 1 
ATOM   2722 C  CG2   . ILE A 1 332 ? 13.704  49.005  -19.425 1   34.4   ? 333  ILE A CG2   1 1 
ATOM   2723 C  CD1   . ILE A 1 332 ? 12.679  48.684  -16.427 1   35.26  ? 333  ILE A CD1   1 1 
ATOM   2724 N  N     . ASN A 1 333 ? 13.911  52.151  -21.357 1   36.87  ? 334  ASN A N     1 1 
ATOM   2725 C  CA    . ASN A 1 333 ? 13.615  52.473  -22.748 1   38.46  ? 334  ASN A CA    1 1 
ATOM   2726 C  C     . ASN A 1 333 ? 14.288  51.537  -23.763 1   39.37  ? 334  ASN A C     1 1 
ATOM   2727 O  O     . ASN A 1 333 ? 13.889  51.546  -24.928 1   40.06  ? 334  ASN A O     1 1 
ATOM   2728 C  CB    . ASN A 1 333 ? 13.977  53.942  -23.04  1   40.22  ? 334  ASN A CB    1 1 
ATOM   2729 C  CG    . ASN A 1 333 ? 13.017  54.939  -22.417 1   43.82  ? 334  ASN A CG    1 1 
ATOM   2730 O  OD1   . ASN A 1 333 ? 13.363  55.679  -21.483 1   44.92  ? 334  ASN A OD1   1 1 
ATOM   2731 N  ND2   . ASN A 1 333 ? 11.785  54.991  -22.925 1   43.92  ? 334  ASN A ND2   1 1 
ATOM   2732 N  N     . ASP A 1 334 ? 15.294  50.743  -23.341 1   38.98  ? 335  ASP A N     1 1 
ATOM   2733 C  CA    . ASP A 1 334 ? 15.995  49.829  -24.235 1   39.69  ? 335  ASP A CA    1 1 
ATOM   2734 C  C     . ASP A 1 334 ? 15.077  48.8    -24.899 1   41.08  ? 335  ASP A C     1 1 
ATOM   2735 O  O     . ASP A 1 334 ? 14.586  47.89   -24.227 1   41.08  ? 335  ASP A O     1 1 
ATOM   2736 C  CB    . ASP A 1 334 ? 17.127  49.108  -23.499 1   40.99  ? 335  ASP A CB    1 1 
ATOM   2737 C  CG    . ASP A 1 334 ? 18.038  48.367  -24.452 1   46.27  ? 335  ASP A CG    1 1 
ATOM   2738 O  OD1   . ASP A 1 334 ? 18.944  49.009  -25.028 1   48.18  ? 335  ASP A OD1   1 1 
ATOM   2739 O  OD2   . ASP A 1 334 ? 17.836  47.156  -24.639 1   47.89  ? 335  ASP A OD2   1 1 
ATOM   2740 N  N     . MET A 1 335 ? 14.896  48.92   -26.228 1   41.84  ? 336  MET A N     1 1 
ATOM   2741 C  CA    . MET A 1 335 ? 14.066  48.032  -27.049 1   42.74  ? 336  MET A CA    1 1 
ATOM   2742 C  C     . MET A 1 335 ? 14.3    46.547  -26.781 1   43.19  ? 336  MET A C     1 1 
ATOM   2743 O  O     . MET A 1 335 ? 13.33   45.804  -26.611 1   43.59  ? 336  MET A O     1 1 
ATOM   2744 C  CB    . MET A 1 335 ? 14.253  48.341  -28.546 1   43.51  ? 336  MET A CB    1 1 
ATOM   2745 N  N     . LYS A 1 336 ? 15.575  46.116  -26.723 1   42.94  ? 337  LYS A N     1 1 
ATOM   2746 C  CA    . LYS A 1 336 ? 15.917  44.715  -26.487 1   43.2   ? 337  LYS A CA    1 1 
ATOM   2747 C  C     . LYS A 1 336 ? 15.551  44.232  -25.071 1   42.05  ? 337  LYS A C     1 1 
ATOM   2748 O  O     . LYS A 1 336 ? 15.062  43.115  -24.92  1   42.15  ? 337  LYS A O     1 1 
ATOM   2749 C  CB    . LYS A 1 336 ? 17.395  44.442  -26.822 1   46.46  ? 337  LYS A CB    1 1 
ATOM   2750 C  CG    . LYS A 1 336 ? 17.756  44.758  -28.278 1   51.66  ? 337  LYS A CG    1 1 
ATOM   2751 C  CD    . LYS A 1 336 ? 18.419  43.572  -28.997 1   56.72  ? 337  LYS A CD    1 1 
ATOM   2752 C  CE    . LYS A 1 336 ? 19.923  43.542  -28.867 1   61.49  ? 337  LYS A CE    1 1 
ATOM   2753 N  NZ    . LYS A 1 336 ? 20.58   44.621  -29.666 1   64.72  ? 337  LYS A NZ    1 1 
ATOM   2754 N  N     . ILE A 1 337 ? 15.742  45.08   -24.045 1   40.76  ? 338  ILE A N     1 1 
ATOM   2755 C  CA    . ILE A 1 337 ? 15.389  44.723  -22.665 1   39.82  ? 338  ILE A CA    1 1 
ATOM   2756 C  C     . ILE A 1 337 ? 13.867  44.55   -22.523 1   38.09  ? 338  ILE A C     1 1 
ATOM   2757 O  O     . ILE A 1 337 ? 13.404  43.602  -21.878 1   37.84  ? 338  ILE A O     1 1 
ATOM   2758 C  CB    . ILE A 1 337 ? 15.946  45.771  -21.666 1   40.3   ? 338  ILE A CB    1 1 
ATOM   2759 C  CG1   . ILE A 1 337 ? 17.471  45.661  -21.542 1   41.67  ? 338  ILE A CG1   1 1 
ATOM   2760 C  CG2   . ILE A 1 337 ? 15.287  45.647  -20.292 1   40.49  ? 338  ILE A CG2   1 1 
ATOM   2761 C  CD1   . ILE A 1 337 ? 18.104  46.775  -20.618 1   43.43  ? 338  ILE A CD1   1 1 
ATOM   2762 N  N     . ILE A 1 338 ? 13.103  45.458  -23.144 1   36.83  ? 339  ILE A N     1 1 
ATOM   2763 C  CA    . ILE A 1 338 ? 11.645  45.411  -23.123 1   36.65  ? 339  ILE A CA    1 1 
ATOM   2764 C  C     . ILE A 1 338 ? 11.123  44.127  -23.792 1   37.04  ? 339  ILE A C     1 1 
ATOM   2765 O  O     . ILE A 1 338 ? 10.233  43.482  -23.241 1   36.79  ? 339  ILE A O     1 1 
ATOM   2766 C  CB    . ILE A 1 338 ? 11.043  46.698  -23.714 1   36.04  ? 339  ILE A CB    1 1 
ATOM   2767 C  CG1   . ILE A 1 338 ? 11.567  47.932  -22.953 1   36.6   ? 339  ILE A CG1   1 1 
ATOM   2768 C  CG2   . ILE A 1 338 ? 9.535   46.639  -23.684 1   36.01  ? 339  ILE A CG2   1 1 
ATOM   2769 C  CD1   . ILE A 1 338 ? 11.128  49.289  -23.551 1   37.41  ? 339  ILE A CD1   1 1 
ATOM   2770 N  N     . LYS A 1 339 ? 11.751  43.699  -24.907 1   37.51  ? 340  LYS A N     1 1 
ATOM   2771 C  CA    . LYS A 1 339 ? 11.386  42.455  -25.595 1   38.28  ? 340  LYS A CA    1 1 
ATOM   2772 C  C     . LYS A 1 339 ? 11.603  41.254  -24.697 1   38.09  ? 340  LYS A C     1 1 
ATOM   2773 O  O     . LYS A 1 339 ? 10.769  40.348  -24.683 1   38.69  ? 340  LYS A O     1 1 
ATOM   2774 C  CB    . LYS A 1 339 ? 12.16   42.289  -26.912 1   41.2   ? 340  LYS A CB    1 1 
ATOM   2775 C  CG    . LYS A 1 339 ? 11.473  42.996  -28.072 1   48.45  ? 340  LYS A CG    1 1 
ATOM   2776 C  CD    . LYS A 1 339 ? 12.385  43.228  -29.28  1   54.91  ? 340  LYS A CD    1 1 
ATOM   2777 C  CE    . LYS A 1 339 ? 11.68   44      -30.385 1   59.12  ? 340  LYS A CE    1 1 
ATOM   2778 N  NZ    . LYS A 1 339 ? 11.195  45.33   -29.927 1   60.85  ? 340  LYS A NZ    1 1 
ATOM   2779 N  N     . GLU A 1 340 ? 12.699  41.258  -23.92  1   36.89  ? 341  GLU A N     1 1 
ATOM   2780 C  CA    . GLU A 1 340 ? 12.996  40.177  -22.981 1   35.83  ? 341  GLU A CA    1 1 
ATOM   2781 C  C     . GLU A 1 340 ? 11.918  40.117  -21.905 1   33.23  ? 341  GLU A C     1 1 
ATOM   2782 O  O     . GLU A 1 340 ? 11.42   39.048  -21.588 1   32.83  ? 341  GLU A O     1 1 
ATOM   2783 C  CB    . GLU A 1 340 ? 14.379  40.39   -22.331 1   39.38  ? 341  GLU A CB    1 1 
ATOM   2784 C  CG    . GLU A 1 340 ? 15.552  40.166  -23.268 1   47.88  ? 341  GLU A CG    1 1 
ATOM   2785 C  CD    . GLU A 1 340 ? 15.568  38.766  -23.847 1   59.48  ? 341  GLU A CD    1 1 
ATOM   2786 O  OE1   . GLU A 1 340 ? 15.957  37.824  -23.117 1   61     ? 341  GLU A OE1   1 1 
ATOM   2787 O  OE2   . GLU A 1 340 ? 15.156  38.607  -25.021 1   63.83  ? 341  GLU A OE2   1 1 
ATOM   2788 N  N     . LEU A 1 341 ? 11.529  41.283  -21.371 1   31.64  ? 342  LEU A N     1 1 
ATOM   2789 C  CA    . LEU A 1 341 ? 10.503  41.38   -20.334 1   30.48  ? 342  LEU A CA    1 1 
ATOM   2790 C  C     . LEU A 1 341 ? 9.125   40.974  -20.835 1   29.44  ? 342  LEU A C     1 1 
ATOM   2791 O  O     . LEU A 1 341 ? 8.33    40.471  -20.059 1   29.39  ? 342  LEU A O     1 1 
ATOM   2792 C  CB    . LEU A 1 341 ? 10.437  42.812  -19.811 1   29.95  ? 342  LEU A CB    1 1 
ATOM   2793 C  CG    . LEU A 1 341 ? 11.62   43.278  -19.003 1   30.75  ? 342  LEU A CG    1 1 
ATOM   2794 C  CD1   . LEU A 1 341 ? 11.545  44.743  -18.788 1   30.36  ? 342  LEU A CD1   1 1 
ATOM   2795 C  CD2   . LEU A 1 341 ? 11.7    42.521  -17.677 1   31.58  ? 342  LEU A CD2   1 1 
ATOM   2796 N  N     . LYS A 1 342 ? 8.838   41.215  -22.123 1   28.87  ? 343  LYS A N     1 1 
ATOM   2797 C  CA    . LYS A 1 342 ? 7.55    40.917  -22.736 1   29.15  ? 343  LYS A CA    1 1 
ATOM   2798 C  C     . LYS A 1 342 ? 7.416   39.534  -23.356 1   30.6   ? 343  LYS A C     1 1 
ATOM   2799 O  O     . LYS A 1 342 ? 6.569   39.344  -24.233 1   31.26  ? 343  LYS A O     1 1 
ATOM   2800 C  CB    . LYS A 1 342 ? 7.194   41.975  -23.777 1   29.07  ? 343  LYS A CB    1 1 
ATOM   2801 C  CG    . LYS A 1 342 ? 6.859   43.299  -23.156 1   30.69  ? 343  LYS A CG    1 1 
ATOM   2802 C  CD    . LYS A 1 342 ? 6.307   44.246  -24.173 1   32.82  ? 343  LYS A CD    1 1 
ATOM   2803 C  CE    . LYS A 1 342 ? 5.891   45.543  -23.536 1   34.35  ? 343  LYS A CE    1 1 
ATOM   2804 N  NZ    . LYS A 1 342 ? 5.16    46.382  -24.518 1   36.56  ? 343  LYS A NZ    1 1 
ATOM   2805 N  N     . GLU A 1 343 ? 8.173   38.542  -22.881 1   31.27  ? 344  GLU A N     1 1 
ATOM   2806 C  CA    . GLU A 1 343 ? 8.04    37.158  -23.381 1   32.53  ? 344  GLU A CA    1 1 
ATOM   2807 C  C     . GLU A 1 343 ? 6.613   36.667  -23.118 1   33.53  ? 344  GLU A C     1 1 
ATOM   2808 O  O     . GLU A 1 343 ? 6.076   36.961  -22.057 1   33.99  ? 344  GLU A O     1 1 
ATOM   2809 C  CB    . GLU A 1 343 ? 9.062   36.229  -22.7   1   34.77  ? 344  GLU A CB    1 1 
ATOM   2810 C  CG    . GLU A 1 343 ? 9.03    34.803  -23.224 1   38.65  ? 344  GLU A CG    1 1 
ATOM   2811 C  CD    . GLU A 1 343 ? 10.227  33.951  -22.85  1   43.78  ? 344  GLU A CD    1 1 
ATOM   2812 O  OE1   . GLU A 1 343 ? 11.198  34.493  -22.281 1   43.81  ? 344  GLU A OE1   1 1 
ATOM   2813 O  OE2   . GLU A 1 343 ? 10.181  32.726  -23.101 1   47.69  ? 344  GLU A OE2   1 1 
ATOM   2814 N  N     . ASP A 1 344 ? 5.961   36.037  -24.114 1   33.29  ? 345  ASP A N     1 1 
ATOM   2815 C  CA    . ASP A 1 344 ? 4.573   35.627  -23.986 1   32.71  ? 345  ASP A CA    1 1 
ATOM   2816 C  C     . ASP A 1 344 ? 4.384   34.376  -23.137 1   31.72  ? 345  ASP A C     1 1 
ATOM   2817 O  O     . ASP A 1 344 ? 4.118   33.291  -23.655 1   32.72  ? 345  ASP A O     1 1 
ATOM   2818 C  CB    . ASP A 1 344 ? 3.933   35.483  -25.369 1   35.37  ? 345  ASP A CB    1 1 
ATOM   2819 C  CG    . ASP A 1 344 ? 2.442   35.215  -25.347 1   41.86  ? 345  ASP A CG    1 1 
ATOM   2820 O  OD1   . ASP A 1 344 ? 1.733   35.855  -24.534 1   43.74  ? 345  ASP A OD1   1 1 
ATOM   2821 O  OD2   . ASP A 1 344 ? 1.983   34.359  -26.138 1   44.32  ? 345  ASP A OD2   1 1 
ATOM   2822 N  N     . ALA A 1 345 ? 4.454   34.543  -21.823 1   29.9   ? 346  ALA A N     1 1 
ATOM   2823 C  CA    . ALA A 1 345 ? 4.26    33.464  -20.854 1   28.65  ? 346  ALA A CA    1 1 
ATOM   2824 C  C     . ALA A 1 345 ? 3.838   34.057  -19.5   1   27.08  ? 346  ALA A C     1 1 
ATOM   2825 O  O     . ALA A 1 345 ? 4.066   35.241  -19.26  1   27.25  ? 346  ALA A O     1 1 
ATOM   2826 C  CB    . ALA A 1 345 ? 5.561   32.682  -20.689 1   28.72  ? 346  ALA A CB    1 1 
ATOM   2827 N  N     . ASP A 1 346 ? 3.256   33.247  -18.602 1   25.5   ? 347  ASP A N     1 1 
ATOM   2828 C  CA    . ASP A 1 346 ? 2.893   33.72   -17.264 1   24.54  ? 347  ASP A CA    1 1 
ATOM   2829 C  C     . ASP A 1 346 ? 4.185   34.113  -16.504 1   23.46  ? 347  ASP A C     1 1 
ATOM   2830 O  O     . ASP A 1 346 ? 5.253   33.54   -16.729 1   22.76  ? 347  ASP A O     1 1 
ATOM   2831 C  CB    . ASP A 1 346 ? 2.155   32.639  -16.459 1   26.07  ? 347  ASP A CB    1 1 
ATOM   2832 C  CG    . ASP A 1 346 ? 0.79    32.245  -16.981 1   30.32  ? 347  ASP A CG    1 1 
ATOM   2833 O  OD1   . ASP A 1 346 ? 0.215   33.009  -17.781 1   30.84  ? 347  ASP A OD1   1 1 
ATOM   2834 O  OD2   . ASP A 1 346 ? 0.297   31.181  -16.583 1   33.25  ? 347  ASP A OD2   1 1 
ATOM   2835 N  N     . LEU A 1 347 ? 4.063   35.066  -15.585 1   23.03  ? 348  LEU A N     1 1 
ATOM   2836 C  CA    . LEU A 1 347 ? 5.212   35.568  -14.862 1   23.26  ? 348  LEU A CA    1 1 
ATOM   2837 C  C     . LEU A 1 347 ? 4.953   35.533  -13.383 1   23.21  ? 348  LEU A C     1 1 
ATOM   2838 O  O     . LEU A 1 347 ? 4.044   36.214  -12.924 1   24.62  ? 348  LEU A O     1 1 
ATOM   2839 C  CB    . LEU A 1 347 ? 5.468   37.012  -15.312 1   23.41  ? 348  LEU A CB    1 1 
ATOM   2840 C  CG    . LEU A 1 347 ? 6.717   37.691  -14.771 1   25.66  ? 348  LEU A CG    1 1 
ATOM   2841 C  CD1   . LEU A 1 347 ? 7.973   37.02   -15.299 1   26.06  ? 348  LEU A CD1   1 1 
ATOM   2842 C  CD2   . LEU A 1 347 ? 6.731   39.174  -15.157 1   26.99  ? 348  LEU A CD2   1 1 
ATOM   2843 N  N     . ILE A 1 348 ? 5.756   34.779  -12.622 1   21.4   ? 349  ILE A N     1 1 
ATOM   2844 C  CA    . ILE A 1 348 ? 5.619   34.774  -11.175 1   20.8   ? 349  ILE A CA    1 1 
ATOM   2845 C  C     . ILE A 1 348 ? 6.395   35.97   -10.639 1   20.07  ? 349  ILE A C     1 1 
ATOM   2846 O  O     . ILE A 1 348 ? 7.515   36.172  -11.046 1   19.75  ? 349  ILE A O     1 1 
ATOM   2847 C  CB    . ILE A 1 348 ? 6.065   33.445  -10.566 1   22.05  ? 349  ILE A CB    1 1 
ATOM   2848 C  CG1   . ILE A 1 348 ? 5.033   32.365  -10.934 1   24.12  ? 349  ILE A CG1   1 1 
ATOM   2849 C  CG2   . ILE A 1 348 ? 6.222   33.57   -9.05   1   22.79  ? 349  ILE A CG2   1 1 
ATOM   2850 C  CD1   . ILE A 1 348 ? 5.388   31.042  -10.562 1   26.77  ? 349  ILE A CD1   1 1 
ATOM   2851 N  N     . VAL A 1 349 ? 5.774   36.809  -9.816  1   19.08  ? 350  VAL A N     1 1 
ATOM   2852 C  CA    . VAL A 1 349 ? 6.442   37.973  -9.251  1   18.69  ? 350  VAL A CA    1 1 
ATOM   2853 C  C     . VAL A 1 349 ? 6.621   37.718  -7.778  1   19     ? 350  VAL A C     1 1 
ATOM   2854 O  O     . VAL A 1 349 ? 5.643   37.462  -7.074  1   20.14  ? 350  VAL A O     1 1 
ATOM   2855 C  CB    . VAL A 1 349 ? 5.677   39.302  -9.51   1   17.98  ? 350  VAL A CB    1 1 
ATOM   2856 C  CG1   . VAL A 1 349 ? 6.318   40.458  -8.742  1   18.6   ? 350  VAL A CG1   1 1 
ATOM   2857 C  CG2   . VAL A 1 349 ? 5.615   39.622  -11.003 1   17.34  ? 350  VAL A CG2   1 1 
ATOM   2858 N  N     . CYS A 1 350 ? 7.847   37.778  -7.316  1   18.12  ? 351  CYS A N     1 1 
ATOM   2859 C  CA    . CYS A 1 350 ? 8.156   37.577  -5.922  1   17.9   ? 351  CYS A CA    1 1 
ATOM   2860 C  C     . CYS A 1 350 ? 8.718   38.866  -5.355  1   17.07  ? 351  CYS A C     1 1 
ATOM   2861 O  O     . CYS A 1 350 ? 9.675   39.424  -5.917  1   16.91  ? 351  CYS A O     1 1 
ATOM   2862 C  CB    . CYS A 1 350 ? 9.142   36.429  -5.763  1   17.89  ? 351  CYS A CB    1 1 
ATOM   2863 S  SG    . CYS A 1 350 ? 9.537   36.055  -4.046  1   21.38  ? 351  CYS A SG    1 1 
ATOM   2864 N  N     . MET A 1 351 ? 8.141   39.354  -4.253  1   16.66  ? 352  MET A N     1 1 
ATOM   2865 C  CA    . MET A 1 351 ? 8.599   40.638  -3.685  1   17.6   ? 352  MET A CA    1 1 
ATOM   2866 C  C     . MET A 1 351 ? 9.181   40.424  -2.302  1   18.35  ? 352  MET A C     1 1 
ATOM   2867 O  O     . MET A 1 351 ? 8.503   39.86   -1.444  1   19.21  ? 352  MET A O     1 1 
ATOM   2868 C  CB    . MET A 1 351 ? 7.472   41.675  -3.675  1   17.44  ? 352  MET A CB    1 1 
ATOM   2869 C  CG    . MET A 1 351 ? 6.9     41.961  -5.048  1   19     ? 352  MET A CG    1 1 
ATOM   2870 S  SD    . MET A 1 351 ? 5.485   43.114  -5.021  1   21.37  ? 352  MET A SD    1 1 
ATOM   2871 C  CE    . MET A 1 351 ? 6.223   44.578  -4.285  1   18     ? 352  MET A CE    1 1 
ATOM   2872 N  N     . LEU A 1 352 ? 10.455  40.773  -2.107  1   17.25  ? 353  LEU A N     1 1 
ATOM   2873 C  CA    . LEU A 1 352 ? 11.136  40.53   -0.827  1   17.25  ? 353  LEU A CA    1 1 
ATOM   2874 C  C     . LEU A 1 352 ? 11.972  41.706  -0.416  1   17.84  ? 353  LEU A C     1 1 
ATOM   2875 O  O     . LEU A 1 352 ? 12.712  42.23   -1.24   1   18.21  ? 353  LEU A O     1 1 
ATOM   2876 C  CB    . LEU A 1 352 ? 12.084  39.29   -0.926  1   16.72  ? 353  LEU A CB    1 1 
ATOM   2877 C  CG    . LEU A 1 352 ? 11.437  37.949  -1.262  1   16.32  ? 353  LEU A CG    1 1 
ATOM   2878 C  CD1   . LEU A 1 352 ? 12.484  36.962  -1.828  1   16.15  ? 353  LEU A CD1   1 1 
ATOM   2879 C  CD2   . LEU A 1 352 ? 10.75   37.358  -0.047  1   16.07  ? 353  LEU A CD2   1 1 
ATOM   2880 N  N     . LYS A 1 353 ? 11.945  42.082  0.868   1   18.05  ? 354  LYS A N     1 1 
ATOM   2881 C  CA    . LYS A 1 353 ? 12.824  43.151  1.359   1   18.63  ? 354  LYS A CA    1 1 
ATOM   2882 C  C     . LYS A 1 353 ? 14.282  42.75   1.195   1   19.73  ? 354  LYS A C     1 1 
ATOM   2883 O  O     . LYS A 1 353 ? 15.124  43.555  0.804   1   19.75  ? 354  LYS A O     1 1 
ATOM   2884 C  CB    . LYS A 1 353 ? 12.536  43.506  2.817   1   18.81  ? 354  LYS A CB    1 1 
ATOM   2885 C  CG    . LYS A 1 353 ? 13.225  44.807  3.234   1   18.86  ? 354  LYS A CG    1 1 
ATOM   2886 C  CD    . LYS A 1 353 ? 12.67   45.393  4.498   1   18.89  ? 354  LYS A CD    1 1 
ATOM   2887 C  CE    . LYS A 1 353 ? 13.332  46.741  4.846   1   20.32  ? 354  LYS A CE    1 1 
ATOM   2888 N  NZ    . LYS A 1 353 ? 14.583  46.608  5.639   1   19.11  ? 354  LYS A NZ    1 1 
ATOM   2889 N  N     . GLY A 1 354 ? 14.575  41.478  1.432   1   19.47  ? 355  GLY A N     1 1 
ATOM   2890 C  CA    . GLY A 1 354 ? 15.906  40.939  1.255   1   18.72  ? 355  GLY A CA    1 1 
ATOM   2891 C  C     . GLY A 1 354 ? 16.852  41.22   2.392   1   19.17  ? 355  GLY A C     1 1 
ATOM   2892 O  O     . GLY A 1 354 ? 17.614  40.327  2.81    1   19.28  ? 355  GLY A O     1 1 
ATOM   2893 N  N     . PHE A 1 355 ? 16.885  42.489  2.836   1   18.73  ? 356  PHE A N     1 1 
ATOM   2894 C  CA    . PHE A 1 355 ? 17.906  42.959  3.77    1   19.33  ? 356  PHE A CA    1 1 
ATOM   2895 C  C     . PHE A 1 355 ? 17.365  43.847  4.86    1   20.52  ? 356  PHE A C     1 1 
ATOM   2896 O  O     . PHE A 1 355 ? 16.453  44.653  4.648   1   21.44  ? 356  PHE A O     1 1 
ATOM   2897 C  CB    . PHE A 1 355 ? 19.044  43.712  3.004   1   19.12  ? 356  PHE A CB    1 1 
ATOM   2898 C  CG    . PHE A 1 355 ? 19.551  42.915  1.83    1   19.25  ? 356  PHE A CG    1 1 
ATOM   2899 C  CD1   . PHE A 1 355 ? 18.892  42.952  0.612   1   19     ? 356  PHE A CD1   1 1 
ATOM   2900 C  CD2   . PHE A 1 355 ? 20.563  41.985  1.992   1   20.14  ? 356  PHE A CD2   1 1 
ATOM   2901 C  CE1   . PHE A 1 355 ? 19.239  42.082  -0.41   1   19.47  ? 356  PHE A CE1   1 1 
ATOM   2902 C  CE2   . PHE A 1 355 ? 20.909  41.13   0.961   1   20.29  ? 356  PHE A CE2   1 1 
ATOM   2903 C  CZ    . PHE A 1 355 ? 20.259  41.199  -0.236  1   19.44  ? 356  PHE A CZ    1 1 
ATOM   2904 N  N     . LYS A 1 356 ? 17.969  43.716  6.032   1   20.52  ? 357  LYS A N     1 1 
ATOM   2905 C  CA    . LYS A 1 356 ? 17.65   44.483  7.229   1   20.79  ? 357  LYS A CA    1 1 
ATOM   2906 C  C     . LYS A 1 356 ? 18.301  45.91   7.153   1   21.6   ? 357  LYS A C     1 1 
ATOM   2907 O  O     . LYS A 1 356 ? 19.01   46.201  6.181   1   20.5   ? 357  LYS A O     1 1 
ATOM   2908 C  CB    . LYS A 1 356 ? 18.117  43.645  8.441   1   20.76  ? 357  LYS A CB    1 1 
ATOM   2909 C  CG    . LYS A 1 356 ? 17.068  42.644  8.907   1   19.77  ? 357  LYS A CG    1 1 
ATOM   2910 C  CD    . LYS A 1 356 ? 17.677  41.61   9.808   1   23.35  ? 357  LYS A CD    1 1 
ATOM   2911 C  CE    . LYS A 1 356 ? 18.355  40.526  8.99    1   25.58  ? 357  LYS A CE    1 1 
ATOM   2912 N  NZ    . LYS A 1 356 ? 19.299  39.724  9.803   1   26.1   ? 357  LYS A NZ    1 1 
ATOM   2913 N  N     . PRO A 1 357 ? 18.037  46.843  8.108   1   22.93  ? 358  PRO A N     1 1 
ATOM   2914 C  CA    . PRO A 1 357 ? 18.571  48.218  7.963   1   23.6   ? 358  PRO A CA    1 1 
ATOM   2915 C  C     . PRO A 1 357 ? 20.08   48.368  7.753   1   24.85  ? 358  PRO A C     1 1 
ATOM   2916 O  O     . PRO A 1 357 ? 20.493  49.302  7.056   1   26.1   ? 358  PRO A O     1 1 
ATOM   2917 C  CB    . PRO A 1 357 ? 18.11   48.908  9.243   1   24.3   ? 358  PRO A CB    1 1 
ATOM   2918 C  CG    . PRO A 1 357 ? 16.792  48.155  9.58    1   24.36  ? 358  PRO A CG    1 1 
ATOM   2919 C  CD    . PRO A 1 357 ? 17.171  46.73   9.301   1   22.2   ? 358  PRO A CD    1 1 
ATOM   2920 N  N     . ARG A 1 358 ? 20.906  47.469  8.306   1   23.88  ? 359  ARG A N     1 1 
ATOM   2921 C  CA    . ARG A 1 358 ? 22.351  47.563  8.091   1   23.07  ? 359  ARG A CA    1 1 
ATOM   2922 C  C     . ARG A 1 358 ? 22.85   46.71   6.89    1   21.64  ? 359  ARG A C     1 1 
ATOM   2923 O  O     . ARG A 1 358 ? 24.056  46.556  6.707   1   20.92  ? 359  ARG A O     1 1 
ATOM   2924 C  CB    . ARG A 1 358 ? 23.137  47.255  9.375   1   24.92  ? 359  ARG A CB    1 1 
ATOM   2925 C  CG    . ARG A 1 358 ? 22.667  48.082  10.567  1   27.25  ? 359  ARG A CG    1 1 
ATOM   2926 C  CD    . ARG A 1 358 ? 23.293  47.57   11.847  1   31.01  ? 359  ARG A CD    1 1 
ATOM   2927 N  NE    . ARG A 1 358 ? 22.664  46.332  12.31   1   35.06  ? 359  ARG A NE    1 1 
ATOM   2928 C  CZ    . ARG A 1 358 ? 23.152  45.556  13.274  1   37.48  ? 359  ARG A CZ    1 1 
ATOM   2929 N  NH1   . ARG A 1 358 ? 24.302  45.865  13.867  1   38.29  ? 359  ARG A NH1   1 1 
ATOM   2930 N  NH2   . ARG A 1 358 ? 22.513  44.45   13.631  1   36.49  ? 359  ARG A NH2   1 1 
ATOM   2931 N  N     . GLY A 1 359 ? 21.93   46.227  6.049   1   20.61  ? 360  GLY A N     1 1 
ATOM   2932 C  CA    . GLY A 1 359 ? 22.303  45.486  4.855   1   20.15  ? 360  GLY A CA    1 1 
ATOM   2933 C  C     . GLY A 1 359 ? 22.587  44.011  5.074   1   19.7   ? 360  GLY A C     1 1 
ATOM   2934 O  O     . GLY A 1 359 ? 23.007  43.321  4.144   1   19.3   ? 360  GLY A O     1 1 
ATOM   2935 N  N     . ASP A 1 360 ? 22.381  43.523  6.305   1   19.86  ? 361  ASP A N     1 1 
ATOM   2936 C  CA    . ASP A 1 360 ? 22.531  42.11   6.617   1   21.07  ? 361  ASP A CA    1 1 
ATOM   2937 C  C     . ASP A 1 360 ? 21.283  41.377  6.051   1   21.41  ? 361  ASP A C     1 1 
ATOM   2938 O  O     . ASP A 1 360 ? 20.169  41.896  6.105   1   21.63  ? 361  ASP A O     1 1 
ATOM   2939 C  CB    . ASP A 1 360 ? 22.764  41.875  8.122   1   23.08  ? 361  ASP A CB    1 1 
ATOM   2940 C  CG    . ASP A 1 360 ? 21.766  42.547  9.041   1   28.72  ? 361  ASP A CG    1 1 
ATOM   2941 O  OD1   . ASP A 1 360 ? 21.481  43.734  8.836   1   29.46  ? 361  ASP A OD1   1 1 
ATOM   2942 O  OD2   . ASP A 1 360 ? 21.286  41.886  9.983   1   31.96  ? 361  ASP A OD2   1 1 
ATOM   2943 N  N     . ASP A 1 361 ? 21.491  40.211  5.445   1   21.14  ? 362  ASP A N     1 1 
ATOM   2944 C  CA    . ASP A 1 361 ? 20.445  39.516  4.744   1   20.72  ? 362  ASP A CA    1 1 
ATOM   2945 C  C     . ASP A 1 361 ? 19.419  38.854  5.662   1   20.37  ? 362  ASP A C     1 1 
ATOM   2946 O  O     . ASP A 1 361 ? 19.719  38.4    6.77    1   20.67  ? 362  ASP A O     1 1 
ATOM   2947 C  CB    . ASP A 1 361 ? 21.02   38.533  3.7     1   22.98  ? 362  ASP A CB    1 1 
ATOM   2948 C  CG    . ASP A 1 361 ? 21.401  37.157  4.204   1   30.09  ? 362  ASP A CG    1 1 
ATOM   2949 O  OD1   . ASP A 1 361 ? 20.486  36.292  4.347   1   33.46  ? 362  ASP A OD1   1 1 
ATOM   2950 O  OD2   . ASP A 1 361 ? 22.596  36.928  4.431   1   31.41  ? 362  ASP A OD2   1 1 
ATOM   2951 N  N     . ASN A 1 362 ? 18.188  38.827  5.164   1   19.44  ? 363  ASN A N     1 1 
ATOM   2952 C  CA    . ASN A 1 362 ? 17.061  38.239  5.83    1   19.42  ? 363  ASN A CA    1 1 
ATOM   2953 C  C     . ASN A 1 362 ? 17.18   36.713  5.629   1   20.01  ? 363  ASN A C     1 1 
ATOM   2954 O  O     . ASN A 1 362 ? 17.178  36.241  4.489   1   20.81  ? 363  ASN A O     1 1 
ATOM   2955 C  CB    . ASN A 1 362 ? 15.772  38.71   5.165   1   19.27  ? 363  ASN A CB    1 1 
ATOM   2956 C  CG    . ASN A 1 362 ? 15.426  40.184  5.316   1   21.13  ? 363  ASN A CG    1 1 
ATOM   2957 O  OD1   . ASN A 1 362 ? 16.021  40.933  6.102   1   21.06  ? 363  ASN A OD1   1 1 
ATOM   2958 N  ND2   . ASN A 1 362 ? 14.415  40.639  4.567   1   22     ? 363  ASN A ND2   1 1 
ATOM   2959 N  N     . ARG A 1 363 ? 17.26   35.954  6.722   1   18.87  ? 364  ARG A N     1 1 
ATOM   2960 C  CA    . ARG A 1 363 ? 17.274  34.5    6.633   1   18.15  ? 364  ARG A CA    1 1 
ATOM   2961 C  C     . ARG A 1 363 ? 15.984  33.931  6.028   1   18.2   ? 364  ARG A C     1 1 
ATOM   2962 O  O     . ARG A 1 363 ? 16.093  33.075  5.145   1   18.56  ? 364  ARG A O     1 1 
ATOM   2963 C  CB    . ARG A 1 363 ? 17.554  33.84   7.981   1   18.36  ? 364  ARG A CB    1 1 
ATOM   2964 C  CG    . ARG A 1 363 ? 18.32   32.52   7.826   1   19.17  ? 364  ARG A CG    1 1 
ATOM   2965 C  CD    . ARG A 1 363 ? 19.792  32.725  7.516   1   20.55  ? 364  ARG A CD    1 1 
ATOM   2966 N  NE    . ARG A 1 363 ? 20.398  33.57   8.543   1   20.61  ? 364  ARG A NE    1 1 
ATOM   2967 C  CZ    . ARG A 1 363 ? 20.651  34.869  8.396   1   20.12  ? 364  ARG A CZ    1 1 
ATOM   2968 N  NH1   . ARG A 1 363 ? 20.464  35.46   7.224   1   18.2   ? 364  ARG A NH1   1 1 
ATOM   2969 N  NH2   . ARG A 1 363 ? 21.115  35.578  9.415   1   19.71  ? 364  ARG A NH2   1 1 
ATOM   2970 N  N     . PRO A 1 364 ? 14.761  34.337  6.467   1   17.81  ? 365  PRO A N     1 1 
ATOM   2971 C  CA    . PRO A 1 364 ? 13.553  33.727  5.878   1   17.67  ? 365  PRO A CA    1 1 
ATOM   2972 C  C     . PRO A 1 364 ? 13.448  33.9    4.37    1   18.02  ? 365  PRO A C     1 1 
ATOM   2973 O  O     . PRO A 1 364 ? 12.922  33.017  3.697   1   18.02  ? 365  PRO A O     1 1 
ATOM   2974 C  CB    . PRO A 1 364 ? 12.395  34.43   6.589   1   18.28  ? 365  PRO A CB    1 1 
ATOM   2975 C  CG    . PRO A 1 364 ? 12.985  34.985  7.857   1   18.78  ? 365  PRO A CG    1 1 
ATOM   2976 C  CD    . PRO A 1 364 ? 14.417  35.315  7.52    1   17.25  ? 365  PRO A CD    1 1 
ATOM   2977 N  N     . ASP A 1 365 ? 13.977  35.027  3.832   1   17.71  ? 366  ASP A N     1 1 
ATOM   2978 C  CA    . ASP A 1 365 ? 13.938  35.295  2.388   1   17.48  ? 366  ASP A CA    1 1 
ATOM   2979 C  C     . ASP A 1 365 ? 14.715  34.278  1.549   1   16.72  ? 366  ASP A C     1 1 
ATOM   2980 O  O     . ASP A 1 365 ? 14.471  34.163  0.344   1   16.16  ? 366  ASP A O     1 1 
ATOM   2981 C  CB    . ASP A 1 365 ? 14.439  36.705  2.072   1   18.36  ? 366  ASP A CB    1 1 
ATOM   2982 C  CG    . ASP A 1 365 ? 13.615  37.823  2.664   1   20.38  ? 366  ASP A CG    1 1 
ATOM   2983 O  OD1   . ASP A 1 365 ? 12.706  37.535  3.499   1   20.19  ? 366  ASP A OD1   1 1 
ATOM   2984 O  OD2   . ASP A 1 365 ? 13.871  38.978  2.318   1   20.81  ? 366  ASP A OD2   1 1 
ATOM   2985 N  N     . ARG A 1 366 ? 15.655  33.555  2.174   1   16.29  ? 367  ARG A N     1 1 
ATOM   2986 C  CA    . ARG A 1 366 ? 16.427  32.546  1.46    1   17.14  ? 367  ARG A CA    1 1 
ATOM   2987 C  C     . ARG A 1 366 ? 15.552  31.423  0.94    1   17.12  ? 367  ARG A C     1 1 
ATOM   2988 O  O     . ARG A 1 366 ? 15.916  30.814  -0.06   1   18.48  ? 367  ARG A O     1 1 
ATOM   2989 C  CB    . ARG A 1 366 ? 17.563  31.981  2.333   1   18.67  ? 367  ARG A CB    1 1 
ATOM   2990 C  CG    . ARG A 1 366 ? 18.546  33.027  2.783   1   23.26  ? 367  ARG A CG    1 1 
ATOM   2991 C  CD    . ARG A 1 366 ? 19.563  32.457  3.753   1   26.97  ? 367  ARG A CD    1 1 
ATOM   2992 N  NE    . ARG A 1 366 ? 20.698  33.368  3.959   1   28.36  ? 367  ARG A NE    1 1 
ATOM   2993 C  CZ    . ARG A 1 366 ? 21.955  32.969  4.145   1   29.51  ? 367  ARG A CZ    1 1 
ATOM   2994 N  NH1   . ARG A 1 366 ? 22.254  31.674  4.143   1   28.92  ? 367  ARG A NH1   1 1 
ATOM   2995 N  NH2   . ARG A 1 366 ? 22.929  33.867  4.303   1   27.67  ? 367  ARG A NH2   1 1 
ATOM   2996 N  N     . GLY A 1 367 ? 14.435  31.135  1.619   1   16.62  ? 368  GLY A N     1 1 
ATOM   2997 C  CA    . GLY A 1 367 ? 13.526  30.064  1.225   1   16.57  ? 368  GLY A CA    1 1 
ATOM   2998 C  C     . GLY A 1 367 ? 12.366  30.485  0.357   1   17.48  ? 368  GLY A C     1 1 
ATOM   2999 O  O     . GLY A 1 367 ? 11.597  29.629  -0.074  1   19.04  ? 368  GLY A O     1 1 
ATOM   3000 N  N     . ALA A 1 368 ? 12.196  31.797  0.096   1   16.92  ? 369  ALA A N     1 1 
ATOM   3001 C  CA    . ALA A 1 368 ? 11.059  32.259  -0.702  1   15.99  ? 369  ALA A CA    1 1 
ATOM   3002 C  C     . ALA A 1 368 ? 11.096  31.745  -2.159  1   15.32  ? 369  ALA A C     1 1 
ATOM   3003 O  O     . ALA A 1 368 ? 10.126  31.136  -2.595  1   14.92  ? 369  ALA A O     1 1 
ATOM   3004 C  CB    . ALA A 1 368 ? 10.916  33.771  -0.626  1   15.76  ? 369  ALA A CB    1 1 
ATOM   3005 N  N     . LEU A 1 369 ? 12.175  31.974  -2.896  1   15.47  ? 370  LEU A N     1 1 
ATOM   3006 C  CA    . LEU A 1 369 ? 12.303  31.446  -4.271  1   16.62  ? 370  LEU A CA    1 1 
ATOM   3007 C  C     . LEU A 1 369 ? 12.324  29.908  -4.305  1   16.76  ? 370  LEU A C     1 1 
ATOM   3008 O  O     . LEU A 1 369 ? 11.587  29.356  -5.106  1   17.58  ? 370  LEU A O     1 1 
ATOM   3009 C  CB    . LEU A 1 369 ? 13.488  32.072  -5.049  1   16.65  ? 370  LEU A CB    1 1 
ATOM   3010 C  CG    . LEU A 1 369 ? 13.329  33.583  -5.295  1   18.66  ? 370  LEU A CG    1 1 
ATOM   3011 C  CD1   . LEU A 1 369 ? 14.469  34.138  -6.112  1   19.55  ? 370  LEU A CD1   1 1 
ATOM   3012 C  CD2   . LEU A 1 369 ? 12.015  33.91   -5.982  1   20.19  ? 370  LEU A CD2   1 1 
ATOM   3013 N  N     . PRO A 1 370 ? 13.017  29.182  -3.398  1   15.85  ? 371  PRO A N     1 1 
ATOM   3014 C  CA    . PRO A 1 370 ? 12.857  27.713  -3.361  1   15.72  ? 371  PRO A CA    1 1 
ATOM   3015 C  C     . PRO A 1 370 ? 11.389  27.301  -3.165  1   16.85  ? 371  PRO A C     1 1 
ATOM   3016 O  O     . PRO A 1 370 ? 10.957  26.406  -3.864  1   17.72  ? 371  PRO A O     1 1 
ATOM   3017 C  CB    . PRO A 1 370 ? 13.712  27.299  -2.163  1   15.34  ? 371  PRO A CB    1 1 
ATOM   3018 C  CG    . PRO A 1 370 ? 14.799  28.339  -2.12   1   15.32  ? 371  PRO A CG    1 1 
ATOM   3019 C  CD    . PRO A 1 370 ? 14.035  29.62   -2.415  1   14.44  ? 371  PRO A CD    1 1 
ATOM   3020 N  N     . LEU A 1 371 ? 10.619  27.973  -2.279  1   16.25  ? 372  LEU A N     1 1 
ATOM   3021 C  CA    . LEU A 1 371 ? 9.208   27.669  -2.078  1   16.89  ? 372  LEU A CA    1 1 
ATOM   3022 C  C     . LEU A 1 371 ? 8.407   27.859  -3.391  1   18.27  ? 372  LEU A C     1 1 
ATOM   3023 O  O     . LEU A 1 371 ? 7.631   26.964  -3.769  1   18.53  ? 372  LEU A O     1 1 
ATOM   3024 C  CB    . LEU A 1 371 ? 8.63    28.578  -0.988  1   16.34  ? 372  LEU A CB    1 1 
ATOM   3025 C  CG    . LEU A 1 371 ? 7.14    28.423  -0.705  1   15.08  ? 372  LEU A CG    1 1 
ATOM   3026 C  CD1   . LEU A 1 371 ? 6.816   27.004  -0.209  1   14.03  ? 372  LEU A CD1   1 1 
ATOM   3027 C  CD2   . LEU A 1 371 ? 6.716   29.45   0.314   1   14.95  ? 372  LEU A CD2   1 1 
ATOM   3028 N  N     . VAL A 1 372 ? 8.638   28.996  -4.111  1   17.83  ? 373  VAL A N     1 1 
ATOM   3029 C  CA    . VAL A 1 372 ? 7.992   29.267  -5.408  1   17.56  ? 373  VAL A CA    1 1 
ATOM   3030 C  C     . VAL A 1 372 ? 8.349   28.151  -6.397  1   16.95  ? 373  VAL A C     1 1 
ATOM   3031 O  O     . VAL A 1 372 ? 7.485   27.718  -7.131  1   16.9   ? 373  VAL A O     1 1 
ATOM   3032 C  CB    . VAL A 1 372 ? 8.481   30.623  -6.001  1   18.58  ? 373  VAL A CB    1 1 
ATOM   3033 C  CG1   . VAL A 1 372 ? 8.039   30.795  -7.45   1   19.14  ? 373  VAL A CG1   1 1 
ATOM   3034 C  CG2   . VAL A 1 372 ? 8.024   31.802  -5.156  1   19.13  ? 373  VAL A CG2   1 1 
ATOM   3035 N  N     . ALA A 1 373 ? 9.638   27.727  -6.446  1   16.46  ? 374  ALA A N     1 1 
ATOM   3036 C  CA    . ALA A 1 373 ? 10.113  26.708  -7.382  1   17.65  ? 374  ALA A CA    1 1 
ATOM   3037 C  C     . ALA A 1 373 ? 9.549   25.333  -7.03   1   17.7   ? 374  ALA A C     1 1 
ATOM   3038 O  O     . ALA A 1 373 ? 9.282   24.537  -7.927  1   19.7   ? 374  ALA A O     1 1 
ATOM   3039 C  CB    . ALA A 1 373 ? 11.651  26.673  -7.392  1   18.48  ? 374  ALA A CB    1 1 
ATOM   3040 N  N     . MET A 1 374 ? 9.329   25.05   -5.743  1   15.97  ? 375  MET A N     1 1 
ATOM   3041 C  CA    . MET A 1 374 ? 8.723   23.787  -5.326  1   15.05  ? 375  MET A CA    1 1 
ATOM   3042 C  C     . MET A 1 374 ? 7.237   23.745  -5.736  1   16.2   ? 375  MET A C     1 1 
ATOM   3043 O  O     . MET A 1 374 ? 6.745   22.69   -6.143  1   16.36  ? 375  MET A O     1 1 
ATOM   3044 C  CB    . MET A 1 374 ? 8.875   23.601  -3.824  1   13.76  ? 375  MET A CB    1 1 
ATOM   3045 C  CG    . MET A 1 374 ? 10.277  23.248  -3.415  1   15.46  ? 375  MET A CG    1 1 
ATOM   3046 S  SD    . MET A 1 374 ? 10.429  23.141  -1.626  1   18.62  ? 375  MET A SD    1 1 
ATOM   3047 C  CE    . MET A 1 374 ? 9.65    21.568  -1.315  1   13.58  ? 375  MET A CE    1 1 
ATOM   3048 N  N     . LEU A 1 375 ? 6.535   24.889  -5.639  1   15.93  ? 376  LEU A N     1 1 
ATOM   3049 C  CA    . LEU A 1 375 ? 5.119   25.014  -5.986  1   16.04  ? 376  LEU A CA    1 1 
ATOM   3050 C  C     . LEU A 1 375 ? 4.861   25.074  -7.482  1   17.13  ? 376  LEU A C     1 1 
ATOM   3051 O  O     . LEU A 1 375 ? 3.982   24.381  -7.976  1   17.16  ? 376  LEU A O     1 1 
ATOM   3052 C  CB    . LEU A 1 375 ? 4.499   26.277  -5.33   1   15     ? 376  LEU A CB    1 1 
ATOM   3053 C  CG    . LEU A 1 375 ? 4.254   26.204  -3.832  1   15.25  ? 376  LEU A CG    1 1 
ATOM   3054 C  CD1   . LEU A 1 375 ? 3.918   27.578  -3.261  1   14.95  ? 376  LEU A CD1   1 1 
ATOM   3055 C  CD2   . LEU A 1 375 ? 3.186   25.138  -3.491  1   15.55  ? 376  LEU A CD2   1 1 
ATOM   3056 N  N     . ALA A 1 376 ? 5.604   25.91   -8.196  1   17.92  ? 377  ALA A N     1 1 
ATOM   3057 C  CA    . ALA A 1 376 ? 5.38    26.182  -9.601  1   19.02  ? 377  ALA A CA    1 1 
ATOM   3058 C  C     . ALA A 1 376 ? 6.351   25.56   -10.585 1   20.41  ? 377  ALA A C     1 1 
ATOM   3059 O  O     . ALA A 1 376 ? 6.103   25.641  -11.788 1   21.52  ? 377  ALA A O     1 1 
ATOM   3060 C  CB    . ALA A 1 376 ? 5.351   27.675  -9.812  1   18.78  ? 377  ALA A CB    1 1 
ATOM   3061 N  N     . GLY A 1 377 ? 7.447   24.981  -10.104 1   19.89  ? 378  GLY A N     1 1 
ATOM   3062 C  CA    . GLY A 1 377 ? 8.473   24.436  -10.983 1   19.36  ? 378  GLY A CA    1 1 
ATOM   3063 C  C     . GLY A 1 377 ? 9.609   25.448  -11.142 1   18.97  ? 378  GLY A C     1 1 
ATOM   3064 O  O     . GLY A 1 377 ? 9.368   26.658  -11.187 1   17.98  ? 378  GLY A O     1 1 
ATOM   3065 N  N     . GLU A 1 378 ? 10.869  24.965  -11.166 1   18.45  ? 379  GLU A N     1 1 
ATOM   3066 C  CA    . GLU A 1 378 ? 12.022  25.846  -11.302 1   18.59  ? 379  GLU A CA    1 1 
ATOM   3067 C  C     . GLU A 1 378 ? 12.096  26.517  -12.677 1   19.83  ? 379  GLU A C     1 1 
ATOM   3068 O  O     . GLU A 1 378 ? 12.753  27.535  -12.799 1   20.17  ? 379  GLU A O     1 1 
ATOM   3069 C  CB    . GLU A 1 378 ? 13.335  25.111  -10.988 1   18.72  ? 379  GLU A CB    1 1 
ATOM   3070 C  CG    . GLU A 1 378 ? 13.731  24.107  -12.056 1   20.61  ? 379  GLU A CG    1 1 
ATOM   3071 C  CD    . GLU A 1 378 ? 14.874  23.191  -11.655 1   22.85  ? 379  GLU A CD    1 1 
ATOM   3072 O  OE1   . GLU A 1 378 ? 15.008  22.931  -10.438 1   24.27  ? 379  GLU A OE1   1 1 
ATOM   3073 O  OE2   . GLU A 1 378 ? 15.613  22.713  -12.549 1   19.69  ? 379  GLU A OE2   1 1 
ATOM   3074 N  N     . ASN A 1 379 ? 11.438  25.963  -13.696 1   20.86  ? 380  ASN A N     1 1 
ATOM   3075 C  CA    . ASN A 1 379 ? 11.454  26.553  -15.031 1   22.44  ? 380  ASN A CA    1 1 
ATOM   3076 C  C     . ASN A 1 379 ? 10.36   27.591  -15.247 1   23.51  ? 380  ASN A C     1 1 
ATOM   3077 O  O     . ASN A 1 379 ? 10.304  28.175  -16.329 1   24.89  ? 380  ASN A O     1 1 
ATOM   3078 C  CB    . ASN A 1 379 ? 11.429  25.474  -16.123 1   24.87  ? 380  ASN A CB    1 1 
ATOM   3079 N  N     . ALA A 1 380 ? 9.535   27.894  -14.214 1   22.82  ? 381  ALA A N     1 1 
ATOM   3080 C  CA    . ALA A 1 380 ? 8.561   28.983  -14.292 1   23.14  ? 381  ALA A CA    1 1 
ATOM   3081 C  C     . ALA A 1 380 ? 9.336   30.277  -14.348 1   24.12  ? 381  ALA A C     1 1 
ATOM   3082 O  O     . ALA A 1 380 ? 10.402  30.367  -13.737 1   24.58  ? 381  ALA A O     1 1 
ATOM   3083 C  CB    . ALA A 1 380 ? 7.688   28.994  -13.052 1   23.27  ? 381  ALA A CB    1 1 
ATOM   3084 N  N     . GLN A 1 381 ? 8.838   31.267  -15.093 1   24.23  ? 382  GLN A N     1 1 
ATOM   3085 C  CA    . GLN A 1 381 ? 9.517   32.544  -15.189 1   24.38  ? 382  GLN A CA    1 1 
ATOM   3086 C  C     . GLN A 1 381 ? 9.305   33.331  -13.924 1   23.42  ? 382  GLN A C     1 1 
ATOM   3087 O  O     . GLN A 1 381 ? 8.168   33.621  -13.569 1   23     ? 382  GLN A O     1 1 
ATOM   3088 C  CB    . GLN A 1 381 ? 9.055   33.312  -16.407 1   27.81  ? 382  GLN A CB    1 1 
ATOM   3089 C  CG    . GLN A 1 381 ? 9.569   32.683  -17.674 1   35.84  ? 382  GLN A CG    1 1 
ATOM   3090 C  CD    . GLN A 1 381 ? 9.322   33.596  -18.844 1   45.92  ? 382  GLN A CD    1 1 
ATOM   3091 O  OE1   . GLN A 1 381 ? 9.599   34.81   -18.814 1   46.4   ? 382  GLN A OE1   1 1 
ATOM   3092 N  NE2   . GLN A 1 381 ? 8.788   33.015  -19.903 1   49.37  ? 382  GLN A NE2   1 1 
ATOM   3093 N  N     . ILE A 1 382 ? 10.401  33.651  -13.211 1   22.2   ? 383  ILE A N     1 1 
ATOM   3094 C  CA    . ILE A 1 382 ? 10.304  34.38   -11.949 1   21.06  ? 383  ILE A CA    1 1 
ATOM   3095 C  C     . ILE A 1 382 ? 10.935  35.768  -12.031 1   20.1   ? 383  ILE A C     1 1 
ATOM   3096 O  O     . ILE A 1 382 ? 12.083  35.909  -12.455 1   19.9   ? 383  ILE A O     1 1 
ATOM   3097 C  CB    . ILE A 1 382 ? 10.91   33.517  -10.817 1   21.01  ? 383  ILE A CB    1 1 
ATOM   3098 C  CG1   . ILE A 1 382 ? 10.144  32.179  -10.679 1   20.81  ? 383  ILE A CG1   1 1 
ATOM   3099 C  CG2   . ILE A 1 382 ? 10.956  34.266  -9.498  1   21.39  ? 383  ILE A CG2   1 1 
ATOM   3100 C  CD1   . ILE A 1 382 ? 10.856  31.12   -9.822  1   21.9   ? 383  ILE A CD1   1 1 
ATOM   3101 N  N     . PHE A 1 383 ? 10.165  36.787  -11.651 1   18.37  ? 384  PHE A N     1 1 
ATOM   3102 C  CA    . PHE A 1 383 ? 10.561  38.178  -11.604 1   19.23  ? 384  PHE A CA    1 1 
ATOM   3103 C  C     . PHE A 1 383 ? 10.678  38.471  -10.12  1   18.63  ? 384  PHE A C     1 1 
ATOM   3104 O  O     . PHE A 1 383 ? 9.657   38.469  -9.429  1   18.79  ? 384  PHE A O     1 1 
ATOM   3105 C  CB    . PHE A 1 383 ? 9.443   39.058  -12.215 1   19.92  ? 384  PHE A CB    1 1 
ATOM   3106 C  CG    . PHE A 1 383 ? 9.709   40.545  -12.355 1   21.16  ? 384  PHE A CG    1 1 
ATOM   3107 C  CD1   . PHE A 1 383 ? 9.531   41.403  -11.277 1   22.12  ? 384  PHE A CD1   1 1 
ATOM   3108 C  CD2   . PHE A 1 383 ? 9.964   41.103  -13.595 1   22.23  ? 384  PHE A CD2   1 1 
ATOM   3109 C  CE1   . PHE A 1 383 ? 9.7     42.779  -11.418 1   23.04  ? 384  PHE A CE1   1 1 
ATOM   3110 C  CE2   . PHE A 1 383 ? 10.126  42.483  -13.738 1   23.19  ? 384  PHE A CE2   1 1 
ATOM   3111 C  CZ    . PHE A 1 383 ? 9.941   43.318  -12.657 1   22.91  ? 384  PHE A CZ    1 1 
ATOM   3112 N  N     . THR A 1 384 ? 11.891  38.701  -9.624  1   17.3   ? 385  THR A N     1 1 
ATOM   3113 C  CA    . THR A 1 384 ? 12.124  38.936  -8.211  1   17.88  ? 385  THR A CA    1 1 
ATOM   3114 C  C     . THR A 1 384 ? 12.44   40.39   -7.992  1   18.4   ? 385  THR A C     1 1 
ATOM   3115 O  O     . THR A 1 384 ? 13.408  40.896  -8.542  1   18.39  ? 385  THR A O     1 1 
ATOM   3116 C  CB    . THR A 1 384 ? 13.296  38.06   -7.716  1   20.27  ? 385  THR A CB    1 1 
ATOM   3117 O  OG1   . THR A 1 384 ? 12.982  36.683  -7.935  1   21.8   ? 385  THR A OG1   1 1 
ATOM   3118 C  CG2   . THR A 1 384 ? 13.63   38.289  -6.252  1   20.47  ? 385  THR A CG2   1 1 
ATOM   3119 N  N     . PHE A 1 385 ? 11.632  41.053  -7.168  1   18.23  ? 386  PHE A N     1 1 
ATOM   3120 C  CA    . PHE A 1 385 ? 11.769  42.457  -6.829  1   18.47  ? 386  PHE A CA    1 1 
ATOM   3121 C  C     . PHE A 1 385 ? 12.274  42.582  -5.394  1   19     ? 386  PHE A C     1 1 
ATOM   3122 O  O     . PHE A 1 385 ? 11.605  42.117  -4.461  1   18.97  ? 386  PHE A O     1 1 
ATOM   3123 C  CB    . PHE A 1 385 ? 10.402  43.155  -6.977  1   18.22  ? 386  PHE A CB    1 1 
ATOM   3124 C  CG    . PHE A 1 385 ? 10.423  44.631  -6.662  1   18.66  ? 386  PHE A CG    1 1 
ATOM   3125 C  CD1   . PHE A 1 385 ? 10.869  45.548  -7.597  1   19.14  ? 386  PHE A CD1   1 1 
ATOM   3126 C  CD2   . PHE A 1 385 ? 9.976   45.102  -5.44   1   19.61  ? 386  PHE A CD2   1 1 
ATOM   3127 C  CE1   . PHE A 1 385 ? 10.919  46.906  -7.298  1   20.1   ? 386  PHE A CE1   1 1 
ATOM   3128 C  CE2   . PHE A 1 385 ? 9.987   46.47   -5.154  1   19.98  ? 386  PHE A CE2   1 1 
ATOM   3129 C  CZ    . PHE A 1 385 ? 10.454  47.362  -6.086  1   19.93  ? 386  PHE A CZ    1 1 
ATOM   3130 N  N     . ILE A 1 386 ? 13.435  43.243  -5.225  1   19.29  ? 387  ILE A N     1 1 
ATOM   3131 C  CA    . ILE A 1 386 ? 14.124  43.467  -3.947  1   19.7   ? 387  ILE A CA    1 1 
ATOM   3132 C  C     . ILE A 1 386 ? 14.153  44.957  -3.571  1   19.35  ? 387  ILE A C     1 1 
ATOM   3133 O  O     . ILE A 1 386 ? 14.513  45.797  -4.406  1   19.33  ? 387  ILE A O     1 1 
ATOM   3134 C  CB    . ILE A 1 386 ? 15.539  42.835  -3.963  1   19.7   ? 387  ILE A CB    1 1 
ATOM   3135 C  CG1   . ILE A 1 386 ? 15.511  41.375  -4.45   1   21.11  ? 387  ILE A CG1   1 1 
ATOM   3136 C  CG2   . ILE A 1 386 ? 16.244  42.942  -2.61   1   20.03  ? 387  ILE A CG2   1 1 
ATOM   3137 C  CD1   . ILE A 1 386 ? 14.633  40.487  -3.613  1   22.3   ? 387  ILE A CD1   1 1 
ATOM   3138 N  N     . TYR A 1 387 ? 13.808  45.29   -2.318  1   19.11  ? 388  TYR A N     1 1 
ATOM   3139 C  CA    . TYR A 1 387 ? 13.721  46.712  -1.932  1   19.34  ? 388  TYR A CA    1 1 
ATOM   3140 C  C     . TYR A 1 387 ? 14.42   47.093  -0.614  1   19.39  ? 388  TYR A C     1 1 
ATOM   3141 O  O     . TYR A 1 387 ? 14.318  48.236  -0.183  1   19.55  ? 388  TYR A O     1 1 
ATOM   3142 C  CB    . TYR A 1 387 ? 12.249  47.148  -1.904  1   19.32  ? 388  TYR A CB    1 1 
ATOM   3143 C  CG    . TYR A 1 387 ? 11.369  46.276  -1.03   1   19.1   ? 388  TYR A CG    1 1 
ATOM   3144 C  CD1   . TYR A 1 387 ? 10.716  45.168  -1.551  1   18.85  ? 388  TYR A CD1   1 1 
ATOM   3145 C  CD2   . TYR A 1 387 ? 11.119  46.611  0.294   1   19.11  ? 388  TYR A CD2   1 1 
ATOM   3146 C  CE1   . TYR A 1 387 ? 9.878   44.388  -0.764  1   18.72  ? 388  TYR A CE1   1 1 
ATOM   3147 C  CE2   . TYR A 1 387 ? 10.314  45.822  1.098   1   19.26  ? 388  TYR A CE2   1 1 
ATOM   3148 C  CZ    . TYR A 1 387 ? 9.712   44.698  0.569   1   19.49  ? 388  TYR A CZ    1 1 
ATOM   3149 O  OH    . TYR A 1 387 ? 8.935   43.906  1.369   1   21.15  ? 388  TYR A OH    1 1 
ATOM   3150 N  N     . GLY A 1 388 ? 15.172  46.174  -0.027  1   19.27  ? 389  GLY A N     1 1 
ATOM   3151 C  CA    . GLY A 1 388 ? 15.913  46.421  1.206   1   20.29  ? 389  GLY A CA    1 1 
ATOM   3152 C  C     . GLY A 1 388 ? 17.265  47.097  0.995   1   21.8   ? 389  GLY A C     1 1 
ATOM   3153 O  O     . GLY A 1 388 ? 17.833  47.063  -0.106  1   22.72  ? 389  GLY A O     1 1 
ATOM   3154 N  N     . PRO A 1 389 ? 17.835  47.694  2.058   1   21.42  ? 390  PRO A N     1 1 
ATOM   3155 C  CA    . PRO A 1 389 ? 19.132  48.386  1.9     1   21.25  ? 390  PRO A CA    1 1 
ATOM   3156 C  C     . PRO A 1 389 ? 20.313  47.499  1.546   1   21.44  ? 390  PRO A C     1 1 
ATOM   3157 O  O     . PRO A 1 389 ? 20.478  46.434  2.141   1   22.63  ? 390  PRO A O     1 1 
ATOM   3158 C  CB    . PRO A 1 389 ? 19.363  49.096  3.241   1   21.8   ? 390  PRO A CB    1 1 
ATOM   3159 C  CG    . PRO A 1 389 ? 18.169  48.863  4.056   1   22.97  ? 390  PRO A CG    1 1 
ATOM   3160 C  CD    . PRO A 1 389 ? 17.292  47.816  3.422   1   21.17  ? 390  PRO A CD    1 1 
ATOM   3161 N  N     . LEU A 1 390 ? 21.108  47.916  0.559   1   20     ? 391  LEU A N     1 1 
ATOM   3162 C  CA    . LEU A 1 390 ? 22.291  47.183  0.142   1   20.19  ? 391  LEU A CA    1 1 
ATOM   3163 C  C     . LEU A 1 390 ? 23.552  47.897  0.597   1   20.74  ? 391  LEU A C     1 1 
ATOM   3164 O  O     . LEU A 1 390 ? 23.644  49.103  0.449   1   20.46  ? 391  LEU A O     1 1 
ATOM   3165 C  CB    . LEU A 1 390 ? 22.353  47.039  -1.385  1   20.09  ? 391  LEU A CB    1 1 
ATOM   3166 C  CG    . LEU A 1 390 ? 21.187  46.351  -2.065  1   21.5   ? 391  LEU A CG    1 1 
ATOM   3167 C  CD1   . LEU A 1 390 ? 21.395  46.294  -3.557  1   22.31  ? 391  LEU A CD1   1 1 
ATOM   3168 C  CD2   . LEU A 1 390 ? 20.99   44.961  -1.531  1   21.66  ? 391  LEU A CD2   1 1 
ATOM   3169 N  N     . ILE A 1 391 ? 24.546  47.149  1.09    1   21.08  ? 392  ILE A N     1 1 
ATOM   3170 C  CA    . ILE A 1 391 ? 25.833  47.734  1.43    1   22.67  ? 392  ILE A CA    1 1 
ATOM   3171 C  C     . ILE A 1 391 ? 26.551  48.074  0.085   1   22.64  ? 392  ILE A C     1 1 
ATOM   3172 O  O     . ILE A 1 391 ? 26.288  47.414  -0.936  1   23.34  ? 392  ILE A O     1 1 
ATOM   3173 C  CB    . ILE A 1 391 ? 26.672  46.76   2.299   1   24.48  ? 392  ILE A CB    1 1 
ATOM   3174 C  CG1   . ILE A 1 391 ? 26.772  45.375  1.627   1   26.52  ? 392  ILE A CG1   1 1 
ATOM   3175 C  CG2   . ILE A 1 391 ? 26.077  46.64   3.698   1   24.57  ? 392  ILE A CG2   1 1 
ATOM   3176 C  CD1   . ILE A 1 391 ? 27.958  44.484  2.133   1   28.48  ? 392  ILE A CD1   1 1 
ATOM   3177 N  N     . LYS A 1 392 ? 27.456  49.08   0.074   1   21.21  ? 393  LYS A N     1 1 
ATOM   3178 C  CA    . LYS A 1 392 ? 28.137  49.46   -1.152  1   21.35  ? 393  LYS A CA    1 1 
ATOM   3179 C  C     . LYS A 1 392 ? 28.796  48.317  -1.912  1   21.84  ? 393  LYS A C     1 1 
ATOM   3180 O  O     . LYS A 1 392 ? 28.598  48.205  -3.121  1   21.86  ? 393  LYS A O     1 1 
ATOM   3181 C  CB    . LYS A 1 392 ? 29.156  50.574  -0.911  1   23.92  ? 393  LYS A CB    1 1 
ATOM   3182 C  CG    . LYS A 1 392 ? 29.631  51.212  -2.208  1   27.03  ? 393  LYS A CG    1 1 
ATOM   3183 C  CD    . LYS A 1 392 ? 28.476  51.795  -3.035  1   29.32  ? 393  LYS A CD    1 1 
ATOM   3184 C  CE    . LYS A 1 392 ? 29.027  52.559  -4.203  1   36.57  ? 393  LYS A CE    1 1 
ATOM   3185 N  NZ    . LYS A 1 392 ? 27.955  53.196  -5.011  1   41.28  ? 393  LYS A NZ    1 1 
ATOM   3186 N  N     . GLY A 1 393 ? 29.517  47.445  -1.199  1   22     ? 394  GLY A N     1 1 
ATOM   3187 C  CA    . GLY A 1 393 ? 30.151  46.287  -1.797  1   23     ? 394  GLY A CA    1 1 
ATOM   3188 C  C     . GLY A 1 393 ? 29.189  45.366  -2.53   1   24.06  ? 394  GLY A C     1 1 
ATOM   3189 O  O     . GLY A 1 393 ? 29.587  44.731  -3.513  1   25.04  ? 394  GLY A O     1 1 
ATOM   3190 N  N     . ALA A 1 394 ? 27.918  45.27   -2.072  1   23.53  ? 395  ALA A N     1 1 
ATOM   3191 C  CA    . ALA A 1 394 ? 26.953  44.38   -2.73   1   23.85  ? 395  ALA A CA    1 1 
ATOM   3192 C  C     . ALA A 1 394 ? 26.501  44.949  -4.07   1   24.68  ? 395  ALA A C     1 1 
ATOM   3193 O  O     . ALA A 1 394 ? 26.588  44.245  -5.067  1   25.81  ? 395  ALA A O     1 1 
ATOM   3194 C  CB    . ALA A 1 394 ? 25.761  44.088  -1.826  1   23.03  ? 395  ALA A CB    1 1 
ATOM   3195 N  N     . ILE A 1 395 ? 26.125  46.234  -4.125  1   23.86  ? 396  ILE A N     1 1 
ATOM   3196 C  CA    . ILE A 1 395 ? 25.753  46.86   -5.398  1   23.2   ? 396  ILE A CA    1 1 
ATOM   3197 C  C     . ILE A 1 395 ? 26.988  46.904  -6.358  1   22.06  ? 396  ILE A C     1 1 
ATOM   3198 O  O     . ILE A 1 395 ? 26.835  46.701  -7.565  1   21.61  ? 396  ILE A O     1 1 
ATOM   3199 C  CB    . ILE A 1 395 ? 25.021  48.233  -5.223  1   22.89  ? 396  ILE A CB    1 1 
ATOM   3200 C  CG1   . ILE A 1 395 ? 24.36   48.695  -6.533  1   23.77  ? 396  ILE A CG1   1 1 
ATOM   3201 C  CG2   . ILE A 1 395 ? 25.877  49.327  -4.611  1   22.84  ? 396  ILE A CG2   1 1 
ATOM   3202 C  CD1   . ILE A 1 395 ? 23.235  47.755  -7.025  1   24.63  ? 396  ILE A CD1   1 1 
ATOM   3203 N  N     . ASN A 1 396 ? 28.195  47.049  -5.818  1   21.91  ? 397  ASN A N     1 1 
ATOM   3204 C  CA    . ASN A 1 396 ? 29.416  47.014  -6.65   1   22.18  ? 397  ASN A CA    1 1 
ATOM   3205 C  C     . ASN A 1 396 ? 29.588  45.651  -7.342  1   23.2   ? 397  ASN A C     1 1 
ATOM   3206 O  O     . ASN A 1 396 ? 29.903  45.594  -8.534  1   22.55  ? 397  ASN A O     1 1 
ATOM   3207 C  CB    . ASN A 1 396 ? 30.648  47.391  -5.842  1   21.78  ? 397  ASN A CB    1 1 
ATOM   3208 C  CG    . ASN A 1 396 ? 30.828  48.892  -5.73   1   23.53  ? 397  ASN A CG    1 1 
ATOM   3209 O  OD1   . ASN A 1 396 ? 30.237  49.682  -6.485  1   22.68  ? 397  ASN A OD1   1 1 
ATOM   3210 N  ND2   . ASN A 1 396 ? 31.638  49.311  -4.78   1   23.37  ? 397  ASN A ND2   1 1 
ATOM   3211 N  N     . LEU A 1 397 ? 29.331  44.555  -6.605  1   24.68  ? 398  LEU A N     1 1 
ATOM   3212 C  CA    . LEU A 1 397 ? 29.436  43.205  -7.153  1   25.65  ? 398  LEU A CA    1 1 
ATOM   3213 C  C     . LEU A 1 397 ? 28.316  42.925  -8.139  1   26.96  ? 398  LEU A C     1 1 
ATOM   3214 O  O     . LEU A 1 397 ? 28.554  42.275  -9.139  1   28.17  ? 398  LEU A O     1 1 
ATOM   3215 C  CB    . LEU A 1 397 ? 29.451  42.148  -6.051  1   25.91  ? 398  LEU A CB    1 1 
ATOM   3216 C  CG    . LEU A 1 397 ? 30.771  41.941  -5.336  1   26.95  ? 398  LEU A CG    1 1 
ATOM   3217 C  CD1   . LEU A 1 397 ? 30.624  40.914  -4.249  1   27     ? 398  LEU A CD1   1 1 
ATOM   3218 C  CD2   . LEU A 1 397 ? 31.845  41.49   -6.308  1   27.91  ? 398  LEU A CD2   1 1 
ATOM   3219 N  N     . ILE A 1 398 ? 27.114  43.438  -7.895  1   26.99  ? 399  ILE A N     1 1 
ATOM   3220 C  CA    . ILE A 1 398 ? 25.973  43.33   -8.814  1   28.15  ? 399  ILE A CA    1 1 
ATOM   3221 C  C     . ILE A 1 398 ? 26.364  43.971  -10.177 1   28.99  ? 399  ILE A C     1 1 
ATOM   3222 O  O     . ILE A 1 398 ? 26.111  43.389  -11.228 1   29.77  ? 399  ILE A O     1 1 
ATOM   3223 C  CB    . ILE A 1 398 ? 24.734  44.03   -8.155  1   28.98  ? 399  ILE A CB    1 1 
ATOM   3224 C  CG1   . ILE A 1 398 ? 24.052  43.087  -7.142  1   30.07  ? 399  ILE A CG1   1 1 
ATOM   3225 C  CG2   . ILE A 1 398 ? 23.706  44.533  -9.186  1   29.27  ? 399  ILE A CG2   1 1 
ATOM   3226 C  CD1   . ILE A 1 398 ? 23.325  43.752  -6.149  1   31.08  ? 399  ILE A CD1   1 1 
ATOM   3227 N  N     . ASP A 1 399 ? 27.056  45.111  -10.142 1   28.57  ? 400  ASP A N     1 1 
ATOM   3228 C  CA    . ASP A 1 399 ? 27.504  45.79   -11.356 1   29.62  ? 400  ASP A CA    1 1 
ATOM   3229 C  C     . ASP A 1 399 ? 28.747  45.184  -12.027 1   30.78  ? 400  ASP A C     1 1 
ATOM   3230 O  O     . ASP A 1 399 ? 29.047  45.543  -13.163 1   32.31  ? 400  ASP A O     1 1 
ATOM   3231 C  CB    . ASP A 1 399 ? 27.737  47.282  -11.083 1   30.51  ? 400  ASP A CB    1 1 
ATOM   3232 C  CG    . ASP A 1 399 ? 26.48   48.023  -10.675 1   32.48  ? 400  ASP A CG    1 1 
ATOM   3233 O  OD1   . ASP A 1 399 ? 25.378  47.561  -11.027 1   32.65  ? 400  ASP A OD1   1 1 
ATOM   3234 O  OD2   . ASP A 1 399 ? 26.6    49.064  -10.008 1   34.22  ? 400  ASP A OD2   1 1 
ATOM   3235 N  N     . GLN A 1 400 ? 29.483  44.311  -11.336 1   29.52  ? 401  GLN A N     1 1 
ATOM   3236 C  CA    . GLN A 1 400 ? 30.679  43.689  -11.899 1   29.11  ? 401  GLN A CA    1 1 
ATOM   3237 C  C     . GLN A 1 400 ? 30.445  42.216  -12.299 1   28.72  ? 401  GLN A C     1 1 
ATOM   3238 O  O     . GLN A 1 400 ? 30.697  41.847  -13.44  1   28.82  ? 401  GLN A O     1 1 
ATOM   3239 C  CB    . GLN A 1 400 ? 31.836  43.786  -10.903 1   30.12  ? 401  GLN A CB    1 1 
ATOM   3240 N  N     . ASP A 1 401 ? 29.925  41.395  -11.372 1   28.15  ? 402  ASP A N     1 1 
ATOM   3241 C  CA    . ASP A 1 401 ? 29.739  39.957  -11.54  1   28.42  ? 402  ASP A CA    1 1 
ATOM   3242 C  C     . ASP A 1 401 ? 28.83   39.46   -10.423 1   27.44  ? 402  ASP A C     1 1 
ATOM   3243 O  O     . ASP A 1 401 ? 29.279  39.21   -9.301  1   26.71  ? 402  ASP A O     1 1 
ATOM   3244 C  CB    . ASP A 1 401 ? 31.105  39.261  -11.453 1   31.06  ? 402  ASP A CB    1 1 
ATOM   3245 C  CG    . ASP A 1 401 ? 31.069  37.753  -11.551 1   38.79  ? 402  ASP A CG    1 1 
ATOM   3246 O  OD1   . ASP A 1 401 ? 30.043  37.203  -12.045 1   40.25  ? 402  ASP A OD1   1 1 
ATOM   3247 O  OD2   . ASP A 1 401 ? 32.051  37.119  -11.142 1   43.21  ? 402  ASP A OD2   1 1 
ATOM   3248 N  N     . ILE A 1 402 ? 27.543  39.324  -10.734 1   26.93  ? 403  ILE A N     1 1 
ATOM   3249 C  CA    . ILE A 1 402 ? 26.559  38.902  -9.754  1   26.92  ? 403  ILE A CA    1 1 
ATOM   3250 C  C     . ILE A 1 402 ? 26.86   37.511  -9.174  1   26.02  ? 403  ILE A C     1 1 
ATOM   3251 O  O     . ILE A 1 402 ? 26.583  37.277  -7.997  1   26.18  ? 403  ILE A O     1 1 
ATOM   3252 C  CB    . ILE A 1 402 ? 25.146  39.02   -10.365 1   27.79  ? 403  ILE A CB    1 1 
ATOM   3253 C  CG1   . ILE A 1 402 ? 24.029  38.902  -9.316  1   29.91  ? 403  ILE A CG1   1 1 
ATOM   3254 C  CG2   . ILE A 1 402 ? 24.95   38.02   -11.502 1   27.99  ? 403  ILE A CG2   1 1 
ATOM   3255 C  CD1   . ILE A 1 402 ? 24.184  39.706  -8.09   1   32.01  ? 403  ILE A CD1   1 1 
ATOM   3256 N  N     . ASN A 1 403 ? 27.495  36.62   -9.957  1   25.14  ? 404  ASN A N     1 1 
ATOM   3257 C  CA    . ASN A 1 403 ? 27.818  35.272  -9.494  1   24.53  ? 404  ASN A CA    1 1 
ATOM   3258 C  C     . ASN A 1 403 ? 28.867  35.243  -8.385  1   23.56  ? 404  ASN A C     1 1 
ATOM   3259 O  O     . ASN A 1 403 ? 28.88   34.316  -7.579  1   23.27  ? 404  ASN A O     1 1 
ATOM   3260 C  CB    . ASN A 1 403 ? 28.198  34.361  -10.662 1   25.78  ? 404  ASN A CB    1 1 
ATOM   3261 C  CG    . ASN A 1 403 ? 27.004  34.099  -11.544 1   27.9   ? 404  ASN A CG    1 1 
ATOM   3262 O  OD1   . ASN A 1 403 ? 25.877  34.004  -11.068 1   27.59  ? 404  ASN A OD1   1 1 
ATOM   3263 N  ND2   . ASN A 1 403 ? 27.21   34.005  -12.846 1   29.07  ? 404  ASN A ND2   1 1 
ATOM   3264 N  N     . LYS A 1 404 ? 29.708  36.263  -8.309  1   22.84  ? 405  LYS A N     1 1 
ATOM   3265 C  CA    . LYS A 1 404 ? 30.676  36.404  -7.239  1   23.51  ? 405  LYS A CA    1 1 
ATOM   3266 C  C     . LYS A 1 404 ? 29.933  36.612  -5.908  1   23.11  ? 405  LYS A C     1 1 
ATOM   3267 O  O     . LYS A 1 404 ? 30.281  36.006  -4.898  1   23.31  ? 405  LYS A O     1 1 
ATOM   3268 C  CB    . LYS A 1 404 ? 31.617  37.6    -7.528  1   26.36  ? 405  LYS A CB    1 1 
ATOM   3269 C  CG    . LYS A 1 404 ? 32.95   37.465  -6.825  1   31.8   ? 405  LYS A CG    1 1 
ATOM   3270 C  CD    . LYS A 1 404 ? 34.006  38.464  -7.335  1   37.37  ? 405  LYS A CD    1 1 
ATOM   3271 C  CE    . LYS A 1 404 ? 35.379  37.963  -6.949  1   41.98  ? 405  LYS A CE    1 1 
ATOM   3272 N  NZ    . LYS A 1 404 ? 36.485  38.789  -7.517  1   43.34  ? 405  LYS A NZ    1 1 
ATOM   3273 N  N     . LEU A 1 405 ? 28.884  37.419  -5.929  1   23.43  ? 406  LEU A N     1 1 
ATOM   3274 C  CA    . LEU A 1 405 ? 28.021  37.702  -4.786  1   24.06  ? 406  LEU A CA    1 1 
ATOM   3275 C  C     . LEU A 1 405 ? 27.234  36.42   -4.385  1   24.75  ? 406  LEU A C     1 1 
ATOM   3276 O  O     . LEU A 1 405 ? 27.239  36.035  -3.217  1   25.1   ? 406  LEU A O     1 1 
ATOM   3277 C  CB    . LEU A 1 405 ? 27.086  38.84   -5.193  1   24.29  ? 406  LEU A CB    1 1 
ATOM   3278 C  CG    . LEU A 1 405 ? 26.311  39.557  -4.107  1   26.04  ? 406  LEU A CG    1 1 
ATOM   3279 C  CD1   . LEU A 1 405 ? 27.234  40.126  -3.053  1   26.19  ? 406  LEU A CD1   1 1 
ATOM   3280 C  CD2   . LEU A 1 405 ? 25.541  40.697  -4.697  1   26.99  ? 406  LEU A CD2   1 1 
ATOM   3281 N  N     . ALA A 1 406 ? 26.644  35.724  -5.376  1   24.46  ? 407  ALA A N     1 1 
ATOM   3282 C  CA    . ALA A 1 406 ? 25.915  34.471  -5.199  1   24.74  ? 407  ALA A CA    1 1 
ATOM   3283 C  C     . ALA A 1 406 ? 26.813  33.38   -4.608  1   26.14  ? 407  ALA A C     1 1 
ATOM   3284 O  O     . ALA A 1 406 ? 26.351  32.559  -3.815  1   26.04  ? 407  ALA A O     1 1 
ATOM   3285 C  CB    . ALA A 1 406 ? 25.375  34.007  -6.541  1   24.25  ? 407  ALA A CB    1 1 
ATOM   3286 N  N     . LYS A 1 407 ? 28.118  33.391  -4.96   1   26.75  ? 408  LYS A N     1 1 
ATOM   3287 C  CA    . LYS A 1 407 ? 29.039  32.394  -4.457  1   27.97  ? 408  LYS A CA    1 1 
ATOM   3288 C  C     . LYS A 1 407 ? 29.272  32.498  -2.949  1   29.05  ? 408  LYS A C     1 1 
ATOM   3289 O  O     . LYS A 1 407 ? 29.379  31.474  -2.278  1   29.74  ? 408  LYS A O     1 1 
ATOM   3290 C  CB    . LYS A 1 407 ? 30.354  32.428  -5.251  1   30.59  ? 408  LYS A CB    1 1 
ATOM   3291 C  CG    . LYS A 1 407 ? 31.374  31.42   -4.797  1   36.22  ? 408  LYS A CG    1 1 
ATOM   3292 C  CD    . LYS A 1 407 ? 32.576  31.43   -5.702  1   43.78  ? 408  LYS A CD    1 1 
ATOM   3293 C  CE    . LYS A 1 407 ? 32.519  30.282  -6.68   1   49.6   ? 408  LYS A CE    1 1 
ATOM   3294 N  NZ    . LYS A 1 407 ? 33.886  29.746  -6.954  1   52.61  ? 408  LYS A NZ    1 1 
ATOM   3295 N  N     . ARG A 1 408 ? 29.315  33.705  -2.408  1   29.85  ? 409  ARG A N     1 1 
ATOM   3296 C  CA    . ARG A 1 408 ? 29.608  33.883  -0.991  1   31.41  ? 409  ARG A CA    1 1 
ATOM   3297 C  C     . ARG A 1 408 ? 28.396  34.04   -0.102  1   31.1   ? 409  ARG A C     1 1 
ATOM   3298 O  O     . ARG A 1 408 ? 28.502  33.77   1.097   1   32.24  ? 409  ARG A O     1 1 
ATOM   3299 C  CB    . ARG A 1 408 ? 30.57   35.049  -0.779  1   35.04  ? 409  ARG A CB    1 1 
ATOM   3300 C  CG    . ARG A 1 408 ? 30.118  36.322  -1.438  1   41.24  ? 409  ARG A CG    1 1 
ATOM   3301 C  CD    . ARG A 1 408 ? 31.285  37.279  -1.578  1   46.23  ? 409  ARG A CD    1 1 
ATOM   3302 N  NE    . ARG A 1 408 ? 31.499  38.086  -0.378  1   51.01  ? 409  ARG A NE    1 1 
ATOM   3303 C  CZ    . ARG A 1 408 ? 30.869  39.232  -0.125  1   54.18  ? 409  ARG A CZ    1 1 
ATOM   3304 N  NH1   . ARG A 1 408 ? 31.142  39.917  0.982   1   54.21  ? 409  ARG A NH1   1 1 
ATOM   3305 N  NH2   . ARG A 1 408 ? 29.969  39.706  -0.976  1   53.99  ? 409  ARG A NH2   1 1 
ATOM   3306 N  N     . ASN A 1 409 ? 27.243  34.429  -0.66   1   28.96  ? 410  ASN A N     1 1 
ATOM   3307 C  CA    . ASN A 1 409 ? 26.067  34.645  0.159   1   27.58  ? 410  ASN A CA    1 1 
ATOM   3308 C  C     . ASN A 1 409 ? 24.868  33.745  -0.239  1   25.94  ? 410  ASN A C     1 1 
ATOM   3309 O  O     . ASN A 1 409 ? 24.45   33.772  -1.395  1   26.49  ? 410  ASN A O     1 1 
ATOM   3310 C  CB    . ASN A 1 409 ? 25.722  36.126  0.104   1   28.91  ? 410  ASN A CB    1 1 
ATOM   3311 C  CG    . ASN A 1 409 ? 24.619  36.518  1.03    1   32.31  ? 410  ASN A CG    1 1 
ATOM   3312 O  OD1   . ASN A 1 409 ? 23.449  36.269  0.763   1   33.42  ? 410  ASN A OD1   1 1 
ATOM   3313 N  ND2   . ASN A 1 409 ? 24.974  37.158  2.132   1   33.45  ? 410  ASN A ND2   1 1 
ATOM   3314 N  N     . GLY A 1 410 ? 24.325  32.988  0.726   1   23.47  ? 411  GLY A N     1 1 
ATOM   3315 C  CA    . GLY A 1 410 ? 23.174  32.105  0.524   1   22.36  ? 411  GLY A CA    1 1 
ATOM   3316 C  C     . GLY A 1 410 ? 21.916  32.778  0.005   1   21.36  ? 411  GLY A C     1 1 
ATOM   3317 O  O     . GLY A 1 410 ? 21.184  32.196  -0.806  1   21.61  ? 411  GLY A O     1 1 
ATOM   3318 N  N     . LEU A 1 411 ? 21.637  34.011  0.471   1   20.54  ? 412  LEU A N     1 1 
ATOM   3319 C  CA    . LEU A 1 411 ? 20.477  34.732  -0.034  1   20.39  ? 412  LEU A CA    1 1 
ATOM   3320 C  C     . LEU A 1 411 ? 20.669  35.087  -1.513  1   20.07  ? 412  LEU A C     1 1 
ATOM   3321 O  O     . LEU A 1 411 ? 19.777  34.832  -2.33   1   19.67  ? 412  LEU A O     1 1 
ATOM   3322 C  CB    . LEU A 1 411 ? 20.147  35.987  0.783   1   20.41  ? 412  LEU A CB    1 1 
ATOM   3323 C  CG    . LEU A 1 411 ? 18.924  36.697  0.291   1   22.17  ? 412  LEU A CG    1 1 
ATOM   3324 C  CD1   . LEU A 1 411 ? 17.706  35.77   0.322   1   23.54  ? 412  LEU A CD1   1 1 
ATOM   3325 C  CD2   . LEU A 1 411 ? 18.69   37.944  1.059   1   22.98  ? 412  LEU A CD2   1 1 
ATOM   3326 N  N     . TRP A 1 412 ? 21.834  35.668  -1.852  1   19.41  ? 413  TRP A N     1 1 
ATOM   3327 C  CA    . TRP A 1 412 ? 22.137  35.993  -3.229  1   19.07  ? 413  TRP A CA    1 1 
ATOM   3328 C  C     . TRP A 1 412 ? 22.201  34.736  -4.11   1   18.75  ? 413  TRP A C     1 1 
ATOM   3329 O  O     . TRP A 1 412 ? 21.741  34.791  -5.241  1   19.36  ? 413  TRP A O     1 1 
ATOM   3330 C  CB    . TRP A 1 412 ? 23.413  36.846  -3.333  1   18.48  ? 413  TRP A CB    1 1 
ATOM   3331 C  CG    . TRP A 1 412 ? 23.172  38.283  -2.948  1   18.7   ? 413  TRP A CG    1 1 
ATOM   3332 C  CD1   . TRP A 1 412 ? 23.617  38.923  -1.829  1   18.82  ? 413  TRP A CD1   1 1 
ATOM   3333 C  CD2   . TRP A 1 412 ? 22.386  39.232  -3.67   1   18.82  ? 413  TRP A CD2   1 1 
ATOM   3334 N  NE1   . TRP A 1 412 ? 23.188  40.224  -1.83   1   19.21  ? 413  TRP A NE1   1 1 
ATOM   3335 C  CE2   . TRP A 1 412 ? 22.419  40.439  -2.945  1   19.31  ? 413  TRP A CE2   1 1 
ATOM   3336 C  CE3   . TRP A 1 412 ? 21.654  39.178  -4.864  1   19.14  ? 413  TRP A CE3   1 1 
ATOM   3337 C  CZ2   . TRP A 1 412 ? 21.767  41.583  -3.384  1   20.21  ? 413  TRP A CZ2   1 1 
ATOM   3338 C  CZ3   . TRP A 1 412 ? 20.969  40.299  -5.273  1   19.74  ? 413  TRP A CZ3   1 1 
ATOM   3339 C  CH2   . TRP A 1 412 ? 20.987  41.473  -4.513  1   20.41  ? 413  TRP A CH2   1 1 
ATOM   3340 N  N     . LYS A 1 413 ? 22.672  33.608  -3.586  1   17.64  ? 414  LYS A N     1 1 
ATOM   3341 C  CA    . LYS A 1 413 ? 22.7    32.358  -4.338  1   18.47  ? 414  LYS A CA    1 1 
ATOM   3342 C  C     . LYS A 1 413 ? 21.247  31.913  -4.709  1   19.25  ? 414  LYS A C     1 1 
ATOM   3343 O  O     . LYS A 1 413 ? 21.007  31.47   -5.829  1   19.19  ? 414  LYS A O     1 1 
ATOM   3344 C  CB    . LYS A 1 413 ? 23.361  31.262  -3.479  1   21.44  ? 414  LYS A CB    1 1 
ATOM   3345 C  CG    . LYS A 1 413 ? 23.88   30.064  -4.268  1   25.66  ? 414  LYS A CG    1 1 
ATOM   3346 C  CD    . LYS A 1 413 ? 24.295  28.941  -3.32   1   33.07  ? 414  LYS A CD    1 1 
ATOM   3347 C  CE    . LYS A 1 413 ? 25.296  29.303  -2.22   1   37.9   ? 414  LYS A CE    1 1 
ATOM   3348 N  NZ    . LYS A 1 413 ? 26.491  29.998  -2.741  1   40.02  ? 414  LYS A NZ    1 1 
ATOM   3349 N  N     . SER A 1 414 ? 20.295  32.056  -3.761  1   18.89  ? 415  SER A N     1 1 
ATOM   3350 C  CA    . SER A 1 414 ? 18.888  31.719  -3.954  1   19.67  ? 415  SER A CA    1 1 
ATOM   3351 C  C     . SER A 1 414 ? 18.295  32.648  -5.047  1   18.76  ? 415  SER A C     1 1 
ATOM   3352 O  O     . SER A 1 414 ? 17.678  32.177  -6.004  1   17.91  ? 415  SER A O     1 1 
ATOM   3353 C  CB    . SER A 1 414 ? 18.145  31.922  -2.636  1   22.92  ? 415  SER A CB    1 1 
ATOM   3354 O  OG    . SER A 1 414 ? 16.861  31.333  -2.659  1   27.84  ? 415  SER A OG    1 1 
ATOM   3355 N  N     . PHE A 1 415 ? 18.586  33.946  -4.957  1   18.46  ? 416  PHE A N     1 1 
ATOM   3356 C  CA    . PHE A 1 415 ? 18.109  34.915  -5.943  1   19.39  ? 416  PHE A CA    1 1 
ATOM   3357 C  C     . PHE A 1 415 ? 18.642  34.654  -7.339  1   19.38  ? 416  PHE A C     1 1 
ATOM   3358 O  O     . PHE A 1 415 ? 17.874  34.66   -8.286  1   20.63  ? 416  PHE A O     1 1 
ATOM   3359 C  CB    . PHE A 1 415 ? 18.447  36.357  -5.534  1   19.41  ? 416  PHE A CB    1 1 
ATOM   3360 C  CG    . PHE A 1 415 ? 17.735  36.896  -4.319  1   20.54  ? 416  PHE A CG    1 1 
ATOM   3361 C  CD1   . PHE A 1 415 ? 16.577  36.299  -3.85   1   21.02  ? 416  PHE A CD1   1 1 
ATOM   3362 C  CD2   . PHE A 1 415 ? 18.216  38.018  -3.654  1   21.78  ? 416  PHE A CD2   1 1 
ATOM   3363 C  CE1   . PHE A 1 415 ? 15.931  36.792  -2.727  1   22.12  ? 416  PHE A CE1   1 1 
ATOM   3364 C  CE2   . PHE A 1 415 ? 17.543  38.533  -2.55   1   22.73  ? 416  PHE A CE2   1 1 
ATOM   3365 C  CZ    . PHE A 1 415 ? 16.395  37.923  -2.1    1   22.29  ? 416  PHE A CZ    1 1 
ATOM   3366 N  N     . VAL A 1 416 ? 19.925  34.451  -7.468  1   18.45  ? 417  VAL A N     1 1 
ATOM   3367 C  CA    . VAL A 1 416 ? 20.56   34.276  -8.764  1   18.85  ? 417  VAL A CA    1 1 
ATOM   3368 C  C     . VAL A 1 416 ? 20.239  32.914  -9.402  1   18.77  ? 417  VAL A C     1 1 
ATOM   3369 O  O     . VAL A 1 416 ? 20.135  32.826  -10.628 1   18.99  ? 417  VAL A O     1 1 
ATOM   3370 C  CB    . VAL A 1 416 ? 22.085  34.55   -8.674  1   18.98  ? 417  VAL A CB    1 1 
ATOM   3371 C  CG1   . VAL A 1 416 ? 22.753  34.265  -9.99   1   19.87  ? 417  VAL A CG1   1 1 
ATOM   3372 C  CG2   . VAL A 1 416 ? 22.37   35.986  -8.235  1   18.46  ? 417  VAL A CG2   1 1 
ATOM   3373 N  N     . SER A 1 417 ? 20.034  31.871  -8.59   1   18.28  ? 418  SER A N     1 1 
ATOM   3374 C  CA    . SER A 1 417 ? 19.77   30.54   -9.15   1   18.02  ? 418  SER A CA    1 1 
ATOM   3375 C  C     . SER A 1 417 ? 18.363  30.38   -9.682  1   18.63  ? 418  SER A C     1 1 
ATOM   3376 O  O     . SER A 1 417 ? 18.135  29.586  -10.613 1   18.89  ? 418  SER A O     1 1 
ATOM   3377 C  CB    . SER A 1 417 ? 20.025  29.465  -8.106  1   18.94  ? 418  SER A CB    1 1 
ATOM   3378 O  OG    . SER A 1 417 ? 21.358  29.54   -7.621  1   20.51  ? 418  SER A OG    1 1 
ATOM   3379 N  N     . LEU A 1 418 ? 17.4    31.06   -9.046  1   17.8   ? 419  LEU A N     1 1 
ATOM   3380 C  CA    . LEU A 1 418 ? 16.001  30.873  -9.402  1   17.64  ? 419  LEU A CA    1 1 
ATOM   3381 C  C     . LEU A 1 418 ? 15.291  32.035  -10.091 1   17.95  ? 419  LEU A C     1 1 
ATOM   3382 O  O     . LEU A 1 418 ? 14.148  31.832  -10.51  1   18.03  ? 419  LEU A O     1 1 
ATOM   3383 C  CB    . LEU A 1 418 ? 15.225  30.477  -8.142  1   17.36  ? 419  LEU A CB    1 1 
ATOM   3384 C  CG    . LEU A 1 418 ? 15.682  29.124  -7.584  1   18     ? 419  LEU A CG    1 1 
ATOM   3385 C  CD1   . LEU A 1 418 ? 15.14   28.883  -6.193  1   17.83  ? 419  LEU A CD1   1 1 
ATOM   3386 C  CD2   . LEU A 1 418 ? 15.305  27.994  -8.54   1   18.24  ? 419  LEU A CD2   1 1 
ATOM   3387 N  N     . SER A 1 419 ? 15.922  33.227  -10.225 1   17.61  ? 420  SER A N     1 1 
ATOM   3388 C  CA    . SER A 1 419 ? 15.212  34.342  -10.871 1   18.58  ? 420  SER A CA    1 1 
ATOM   3389 C  C     . SER A 1 419 ? 15.524  34.471  -12.332 1   19.17  ? 420  SER A C     1 1 
ATOM   3390 O  O     . SER A 1 419 ? 16.686  34.482  -12.693 1   18.35  ? 420  SER A O     1 1 
ATOM   3391 C  CB    . SER A 1 419 ? 15.554  35.676  -10.211 1   19.48  ? 420  SER A CB    1 1 
ATOM   3392 O  OG    . SER A 1 419 ? 15.396  35.673  -8.804  1   21.35  ? 420  SER A OG    1 1 
ATOM   3393 N  N     . ASP A 1 420 ? 14.506  34.69   -13.161 1   20.16  ? 421  ASP A N     1 1 
ATOM   3394 C  CA    . ASP A 1 420 ? 14.732  34.994  -14.574 1   21.6   ? 421  ASP A CA    1 1 
ATOM   3395 C  C     . ASP A 1 420 ? 15.067  36.488  -14.72  1   23.11  ? 421  ASP A C     1 1 
ATOM   3396 O  O     . ASP A 1 420 ? 15.854  36.845  -15.59  1   24.03  ? 421  ASP A O     1 1 
ATOM   3397 C  CB    . ASP A 1 420 ? 13.514  34.621  -15.416 1   22.12  ? 421  ASP A CB    1 1 
ATOM   3398 C  CG    . ASP A 1 420 ? 13.332  33.124  -15.481 1   25.53  ? 421  ASP A CG    1 1 
ATOM   3399 O  OD1   . ASP A 1 420 ? 12.75   32.557  -14.535 1   26.11  ? 421  ASP A OD1   1 1 
ATOM   3400 O  OD2   . ASP A 1 420 ? 13.797  32.512  -16.459 1   27.24  ? 421  ASP A OD2   1 1 
ATOM   3401 N  N     . PHE A 1 421 ? 14.459  37.359  -13.876 1   23.48  ? 422  PHE A N     1 1 
ATOM   3402 C  CA    . PHE A 1 421 ? 14.688  38.813  -13.844 1   23.83  ? 422  PHE A CA    1 1 
ATOM   3403 C  C     . PHE A 1 421 ? 14.829  39.237  -12.411 1   23.85  ? 422  PHE A C     1 1 
ATOM   3404 O  O     . PHE A 1 421 ? 14.024  38.848  -11.586 1   23.81  ? 422  PHE A O     1 1 
ATOM   3405 C  CB    . PHE A 1 421 ? 13.508  39.599  -14.447 1   24.08  ? 422  PHE A CB    1 1 
ATOM   3406 C  CG    . PHE A 1 421 ? 13.017  39.04   -15.755 1   24.95  ? 422  PHE A CG    1 1 
ATOM   3407 C  CD1   . PHE A 1 421 ? 13.664  39.343  -16.941 1   26     ? 422  PHE A CD1   1 1 
ATOM   3408 C  CD2   . PHE A 1 421 ? 11.936  38.18   -15.795 1   25.55  ? 422  PHE A CD2   1 1 
ATOM   3409 C  CE1   . PHE A 1 421 ? 13.222  38.813  -18.143 1   26.72  ? 422  PHE A CE1   1 1 
ATOM   3410 C  CE2   . PHE A 1 421 ? 11.499  37.651  -16.996 1   26.37  ? 422  PHE A CE2   1 1 
ATOM   3411 C  CZ    . PHE A 1 421 ? 12.15   37.964  -18.162 1   26.26  ? 422  PHE A CZ    1 1 
ATOM   3412 N  N     . ILE A 1 422 ? 15.848  40.016  -12.101 1   24.48  ? 423  ILE A N     1 1 
ATOM   3413 C  CA    . ILE A 1 422 ? 16.045  40.537  -10.752 1   24.89  ? 423  ILE A CA    1 1 
ATOM   3414 C  C     . ILE A 1 422 ? 15.955  42.06   -10.836 1   24.65  ? 423  ILE A C     1 1 
ATOM   3415 O  O     . ILE A 1 422 ? 16.737  42.693  -11.545 1   25.23  ? 423  ILE A O     1 1 
ATOM   3416 C  CB    . ILE A 1 422 ? 17.394  40.091  -10.139 1   25.62  ? 423  ILE A CB    1 1 
ATOM   3417 C  CG1   . ILE A 1 422 ? 17.504  38.565  -10.044 1   26.11  ? 423  ILE A CG1   1 1 
ATOM   3418 C  CG2   . ILE A 1 422 ? 17.626  40.764  -8.776  1   26.43  ? 423  ILE A CG2   1 1 
ATOM   3419 C  CD1   . ILE A 1 422 ? 18.905  38.083  -9.678  1   26.95  ? 423  ILE A CD1   1 1 
ATOM   3420 N  N     . VAL A 1 423 ? 15.011  42.636  -10.117 1   23.51  ? 424  VAL A N     1 1 
ATOM   3421 C  CA    . VAL A 1 423 ? 14.811  44.057  -10.094 1   23.77  ? 424  VAL A CA    1 1 
ATOM   3422 C  C     . VAL A 1 423 ? 15.108  44.568  -8.727  1   22.5   ? 424  VAL A C     1 1 
ATOM   3423 O  O     . VAL A 1 423 ? 14.577  44.052  -7.749  1   21.49  ? 424  VAL A O     1 1 
ATOM   3424 C  CB    . VAL A 1 423 ? 13.382  44.406  -10.516 1   25.7   ? 424  VAL A CB    1 1 
ATOM   3425 C  CG1   . VAL A 1 423 ? 13.154  45.898  -10.438 1   26.59  ? 424  VAL A CG1   1 1 
ATOM   3426 C  CG2   . VAL A 1 423 ? 13.113  43.899  -11.915 1   26.94  ? 424  VAL A CG2   1 1 
ATOM   3427 N  N     . LEU A 1 424 ? 16.01   45.554  -8.643  1   22.21  ? 425  LEU A N     1 1 
ATOM   3428 C  CA    . LEU A 1 424 ? 16.34   46.135  -7.36   1   21.98  ? 425  LEU A CA    1 1 
ATOM   3429 C  C     . LEU A 1 424 ? 15.891  47.574  -7.348  1   21.17  ? 425  LEU A C     1 1 
ATOM   3430 O  O     . LEU A 1 424 ? 16.181  48.302  -8.29   1   21.78  ? 425  LEU A O     1 1 
ATOM   3431 C  CB    . LEU A 1 424 ? 17.844  46.114  -7.093  1   22.21  ? 425  LEU A CB    1 1 
ATOM   3432 C  CG    . LEU A 1 424 ? 18.615  44.864  -7.4    1   24.51  ? 425  LEU A CG    1 1 
ATOM   3433 C  CD1   . LEU A 1 424 ? 20.109  45.129  -7.252  1   24.64  ? 425  LEU A CD1   1 1 
ATOM   3434 C  CD2   . LEU A 1 424 ? 18.135  43.694  -6.533  1   25.57  ? 425  LEU A CD2   1 1 
ATOM   3435 N  N     . ASP A 1 425 ? 15.27   48.002  -6.264  1   19.89  ? 426  ASP A N     1 1 
ATOM   3436 C  CA    . ASP A 1 425 ? 14.965  49.408  -6.036  1   20.11  ? 426  ASP A CA    1 1 
ATOM   3437 C  C     . ASP A 1 425 ? 15.356  49.575  -4.597  1   20.61  ? 426  ASP A C     1 1 
ATOM   3438 O  O     . ASP A 1 425 ? 14.516  49.489  -3.704  1   21.45  ? 426  ASP A O     1 1 
ATOM   3439 C  CB    . ASP A 1 425 ? 13.481  49.742  -6.24   1   20.06  ? 426  ASP A CB    1 1 
ATOM   3440 C  CG    . ASP A 1 425 ? 13.167  51.227  -6.104  1   20.75  ? 426  ASP A CG    1 1 
ATOM   3441 O  OD1   . ASP A 1 425 ? 14.083  52.005  -5.723  1   21.53  ? 426  ASP A OD1   1 1 
ATOM   3442 O  OD2   . ASP A 1 425 ? 12.028  51.61   -6.371  1   20.31  ? 426  ASP A OD2   1 1 
ATOM   3443 N  N     . CYS A 1 426 ? 16.63   49.758  -4.373  1   20.21  ? 427  CYS A N     1 1 
ATOM   3444 C  CA    . CYS A 1 426 ? 17.228  49.725  -3.049  1   20.34  ? 427  CYS A CA    1 1 
ATOM   3445 C  C     . CYS A 1 426 ? 17.911  50.971  -2.579  1   20.67  ? 427  CYS A C     1 1 
ATOM   3446 O  O     . CYS A 1 426 ? 18.837  51.45   -3.234  1   20.62  ? 427  CYS A O     1 1 
ATOM   3447 C  CB    . CYS A 1 426 ? 18.21   48.556  -2.972  1   20.05  ? 427  CYS A CB    1 1 
ATOM   3448 S  SG    . CYS A 1 426 ? 17.456  46.939  -3.279  1   25.27  ? 427  CYS A SG    1 1 
ATOM   3449 N  N     . PRO A 1 427 ? 17.685  51.306  -1.296  1   20.65  ? 428  PRO A N     1 1 
ATOM   3450 C  CA    . PRO A 1 427 ? 18.559  52.288  -0.657  1   21.26  ? 428  PRO A CA    1 1 
ATOM   3451 C  C     . PRO A 1 427 ? 19.979  51.675  -0.564  1   22.51  ? 428  PRO A C     1 1 
ATOM   3452 O  O     . PRO A 1 427 ? 20.127  50.44   -0.43   1   21.99  ? 428  PRO A O     1 1 
ATOM   3453 C  CB    . PRO A 1 427 ? 17.959  52.43   0.75    1   21.55  ? 428  PRO A CB    1 1 
ATOM   3454 C  CG    . PRO A 1 427 ? 16.591  51.823  0.686   1   21.6   ? 428  PRO A CG    1 1 
ATOM   3455 C  CD    . PRO A 1 427 ? 16.716  50.736  -0.332  1   20.12  ? 428  PRO A CD    1 1 
ATOM   3456 N  N     . ILE A 1 428 ? 21.014  52.505  -0.74   1   22.86  ? 429  ILE A N     1 1 
ATOM   3457 C  CA    . ILE A 1 428 ? 22.394  52.056  -0.616  1   24.16  ? 429  ILE A CA    1 1 
ATOM   3458 C  C     . ILE A 1 428 ? 22.893  52.714  0.648   1   24.53  ? 429  ILE A C     1 1 
ATOM   3459 O  O     . ILE A 1 428 ? 22.801  53.944  0.779   1   24.35  ? 429  ILE A O     1 1 
ATOM   3460 C  CB    . ILE A 1 428 ? 23.264  52.502  -1.812  1   25.18  ? 429  ILE A CB    1 1 
ATOM   3461 C  CG1   . ILE A 1 428 ? 22.649  52.059  -3.153  1   26.05  ? 429  ILE A CG1   1 1 
ATOM   3462 C  CG2   . ILE A 1 428 ? 24.713  52.042  -1.626  1   26     ? 429  ILE A CG2   1 1 
ATOM   3463 C  CD1   . ILE A 1 428 ? 22.449  50.603  -3.302  1   26.66  ? 429  ILE A CD1   1 1 
ATOM   3464 N  N     . ILE A 1 429 ? 23.387  51.915  1.592   1   24.09  ? 430  ILE A N     1 1 
ATOM   3465 C  CA    . ILE A 1 429 ? 23.904  52.453  2.852   1   24.41  ? 430  ILE A CA    1 1 
ATOM   3466 C  C     . ILE A 1 429 ? 25.078  53.424  2.595   1   24.76  ? 430  ILE A C     1 1 
ATOM   3467 O  O     . ILE A 1 429 ? 26.05   53.065  1.927   1   24.96  ? 430  ILE A O     1 1 
ATOM   3468 C  CB    . ILE A 1 429 ? 24.274  51.266  3.775   1   24.15  ? 430  ILE A CB    1 1 
ATOM   3469 C  CG1   . ILE A 1 429 ? 22.996  50.441  4.05    1   24.02  ? 430  ILE A CG1   1 1 
ATOM   3470 C  CG2   . ILE A 1 429 ? 24.933  51.749  5.077   1   23.89  ? 430  ILE A CG2   1 1 
ATOM   3471 C  CD1   . ILE A 1 429 ? 23.238  49.18   4.582   1   24.95  ? 430  ILE A CD1   1 1 
ATOM   3472 N  N     . GLY A 1 430 ? 24.923  54.665  3.044   1   24.5   ? 431  GLY A N     1 1 
ATOM   3473 C  CA    . GLY A 1 430 ? 25.936  55.682  2.811   1   25.69  ? 431  GLY A CA    1 1 
ATOM   3474 C  C     . GLY A 1 430 ? 25.577  56.668  1.709   1   26.64  ? 431  GLY A C     1 1 
ATOM   3475 O  O     . GLY A 1 430 ? 26.311  57.625  1.482   1   27.49  ? 431  GLY A O     1 1 
ATOM   3476 N  N     . GLU A 1 431 ? 24.471  56.433  0.988   1   25.83  ? 432  GLU A N     1 1 
ATOM   3477 C  CA    . GLU A 1 431 ? 24.012  57.303  -0.081  1   25.95  ? 432  GLU A CA    1 1 
ATOM   3478 C  C     . GLU A 1 431 ? 22.577  57.764  0.212   1   26.78  ? 432  GLU A C     1 1 
ATOM   3479 O  O     . GLU A 1 431 ? 21.801  57.046  0.867   1   27.57  ? 432  GLU A O     1 1 
ATOM   3480 C  CB    . GLU A 1 431 ? 24.092  56.588  -1.428  1   27.48  ? 432  GLU A CB    1 1 
ATOM   3481 C  CG    . GLU A 1 431 ? 25.491  56.092  -1.759  1   31.55  ? 432  GLU A CG    1 1 
ATOM   3482 C  CD    . GLU A 1 431 ? 25.69   55.641  -3.19   1   38.14  ? 432  GLU A CD    1 1 
ATOM   3483 O  OE1   . GLU A 1 431 ? 24.696  55.62   -3.948  1   41.37  ? 432  GLU A OE1   1 1 
ATOM   3484 O  OE2   . GLU A 1 431 ? 26.843  55.329  -3.564  1   41.35  ? 432  GLU A OE2   1 1 
ATOM   3485 N  N     . SER A 1 432 ? 22.208  58.954  -0.278  1   26.23  ? 433  SER A N     1 1 
ATOM   3486 C  CA    . SER A 1 432 ? 20.883  59.508  0.002   1   25.36  ? 433  SER A CA    1 1 
ATOM   3487 C  C     . SER A 1 432 ? 19.733  58.929  -0.808  1   23.78  ? 433  SER A C     1 1 
ATOM   3488 O  O     . SER A 1 432 ? 18.607  58.96   -0.308  1   24.08  ? 433  SER A O     1 1 
ATOM   3489 C  CB    . SER A 1 432 ? 20.884  61.029  -0.138  1   27.99  ? 433  SER A CB    1 1 
ATOM   3490 O  OG    . SER A 1 432 ? 21.912  61.623  0.646   1   31.35  ? 433  SER A OG    1 1 
ATOM   3491 N  N     . TYR A 1 433 ? 19.961  58.442  -2.038  1   22.22  ? 434  TYR A N     1 1 
ATOM   3492 C  CA    . TYR A 1 433 ? 18.833  57.962  -2.862  1   21.94  ? 434  TYR A CA    1 1 
ATOM   3493 C  C     . TYR A 1 433 ? 18.987  56.545  -3.346  1   21.83  ? 434  TYR A C     1 1 
ATOM   3494 O  O     . TYR A 1 433 ? 20.095  56.027  -3.342  1   21.53  ? 434  TYR A O     1 1 
ATOM   3495 C  CB    . TYR A 1 433 ? 18.577  58.917  -4.036  1   21.93  ? 434  TYR A CB    1 1 
ATOM   3496 C  CG    . TYR A 1 433 ? 18.242  60.292  -3.531  1   22.56  ? 434  TYR A CG    1 1 
ATOM   3497 C  CD1   . TYR A 1 433 ? 17.061  60.528  -2.848  1   23.9   ? 434  TYR A CD1   1 1 
ATOM   3498 C  CD2   . TYR A 1 433 ? 19.182  61.308  -3.562  1   23.84  ? 434  TYR A CD2   1 1 
ATOM   3499 C  CE1   . TYR A 1 433 ? 16.776  61.776  -2.308  1   24.84  ? 434  TYR A CE1   1 1 
ATOM   3500 C  CE2   . TYR A 1 433 ? 18.916  62.551  -3.018  1   24.86  ? 434  TYR A CE2   1 1 
ATOM   3501 C  CZ    . TYR A 1 433 ? 17.701  62.787  -2.417  1   25.83  ? 434  TYR A CZ    1 1 
ATOM   3502 O  OH    . TYR A 1 433 ? 17.453  64.006  -1.864  1   28.94  ? 434  TYR A OH    1 1 
ATOM   3503 N  N     . ASN A 1 434 ? 17.883  55.898  -3.747  1   22     ? 435  ASN A N     1 1 
ATOM   3504 C  CA    . ASN A 1 434 ? 17.95   54.502  -4.189  1   21.55  ? 435  ASN A CA    1 1 
ATOM   3505 C  C     . ASN A 1 434 ? 18.697  54.301  -5.513  1   22.43  ? 435  ASN A C     1 1 
ATOM   3506 O  O     . ASN A 1 434 ? 18.883  55.246  -6.297  1   22.74  ? 435  ASN A O     1 1 
ATOM   3507 C  CB    . ASN A 1 434 ? 16.562  53.919  -4.325  1   21.45  ? 435  ASN A CB    1 1 
ATOM   3508 C  CG    . ASN A 1 434 ? 15.904  53.596  -3.024  1   23.56  ? 435  ASN A CG    1 1 
ATOM   3509 O  OD1   . ASN A 1 434 ? 16.239  54.156  -1.984  1   24.78  ? 435  ASN A OD1   1 1 
ATOM   3510 N  ND2   . ASN A 1 434 ? 14.935  52.701  -3.066  1   23.39  ? 435  ASN A ND2   1 1 
ATOM   3511 N  N     . GLU A 1 435 ? 19.107  53.054  -5.752  1   22.25  ? 436  GLU A N     1 1 
ATOM   3512 C  CA    . GLU A 1 435 ? 19.679  52.575  -6.997  1   22.46  ? 436  GLU A CA    1 1 
ATOM   3513 C  C     . GLU A 1 435 ? 18.612  51.685  -7.642  1   22.78  ? 436  GLU A C     1 1 
ATOM   3514 O  O     . GLU A 1 435 ? 17.925  50.933  -6.951  1   23.76  ? 436  GLU A O     1 1 
ATOM   3515 C  CB    . GLU A 1 435 ? 20.92   51.724  -6.75   1   24.09  ? 436  GLU A CB    1 1 
ATOM   3516 C  CG    . GLU A 1 435 ? 22.249  52.473  -6.705  1   28.74  ? 436  GLU A CG    1 1 
ATOM   3517 C  CD    . GLU A 1 435 ? 22.479  53.577  -7.719  1   31.24  ? 436  GLU A CD    1 1 
ATOM   3518 O  OE1   . GLU A 1 435 ? 22.345  53.337  -8.937  1   33.68  ? 436  GLU A OE1   1 1 
ATOM   3519 O  OE2   . GLU A 1 435 ? 22.812  54.694  -7.282  1   30.43  ? 436  GLU A OE2   1 1 
ATOM   3520 N  N     . PHE A 1 436 ? 18.471  51.765  -8.952  1   21.87  ? 437  PHE A N     1 1 
ATOM   3521 C  CA    . PHE A 1 436 ? 17.56   50.899  -9.68   1   21.5   ? 437  PHE A CA    1 1 
ATOM   3522 C  C     . PHE A 1 436 ? 18.411  49.991  -10.552 1   21.38  ? 437  PHE A C     1 1 
ATOM   3523 O  O     . PHE A 1 436 ? 19.317  50.457  -11.249 1   21.17  ? 437  PHE A O     1 1 
ATOM   3524 C  CB    . PHE A 1 436 ? 16.545  51.682  -10.548 1   21.04  ? 437  PHE A CB    1 1 
ATOM   3525 C  CG    . PHE A 1 436 ? 15.81   50.776  -11.519 1   21.24  ? 437  PHE A CG    1 1 
ATOM   3526 C  CD1   . PHE A 1 436 ? 14.888  49.845  -11.061 1   21.92  ? 437  PHE A CD1   1 1 
ATOM   3527 C  CD2   . PHE A 1 436 ? 16.14   50.762  -12.863 1   21.76  ? 437  PHE A CD2   1 1 
ATOM   3528 C  CE1   . PHE A 1 436 ? 14.294  48.936  -11.931 1   22.58  ? 437  PHE A CE1   1 1 
ATOM   3529 C  CE2   . PHE A 1 436 ? 15.526  49.881  -13.733 1   23.08  ? 437  PHE A CE2   1 1 
ATOM   3530 C  CZ    . PHE A 1 436 ? 14.596  48.972  -13.265 1   22.8   ? 437  PHE A CZ    1 1 
ATOM   3531 N  N     . ARG A 1 437 ? 18.09   48.692  -10.55  1   21.21  ? 438  ARG A N     1 1 
ATOM   3532 C  CA    . ARG A 1 437 ? 18.744  47.744  -11.423 1   21.11  ? 438  ARG A CA    1 1 
ATOM   3533 C  C     . ARG A 1 437 ? 17.709  46.829  -12.017 1   22.36  ? 438  ARG A C     1 1 
ATOM   3534 O  O     . ARG A 1 437 ? 16.759  46.434  -11.334 1   22.31  ? 438  ARG A O     1 1 
ATOM   3535 C  CB    . ARG A 1 437 ? 19.781  46.894  -10.665 1   21.72  ? 438  ARG A CB    1 1 
ATOM   3536 C  CG    . ARG A 1 437 ? 21.029  47.639  -10.206 1   23.35  ? 438  ARG A CG    1 1 
ATOM   3537 C  CD    . ARG A 1 437 ? 21.79   48.331  -11.331 1   24.93  ? 438  ARG A CD    1 1 
ATOM   3538 N  NE    . ARG A 1 437 ? 23.015  48.937  -10.82  1   27.96  ? 438  ARG A NE    1 1 
ATOM   3539 C  CZ    . ARG A 1 437 ? 23.102  50.165  -10.312 1   28.75  ? 438  ARG A CZ    1 1 
ATOM   3540 N  NH1   . ARG A 1 437 ? 22.04   50.954  -10.283 1   25.89  ? 438  ARG A NH1   1 1 
ATOM   3541 N  NH2   . ARG A 1 437 ? 24.257  50.616  -9.849  1   29.03  ? 438  ARG A NH2   1 1 
ATOM   3542 N  N     . LEU A 1 438 ? 17.886  46.484  -13.285 1   22.88  ? 439  LEU A N     1 1 
ATOM   3543 C  CA    . LEU A 1 438 ? 17.063  45.496  -13.955 1   23.75  ? 439  LEU A CA    1 1 
ATOM   3544 C  C     . LEU A 1 438 ? 18.061  44.512  -14.542 1   24.69  ? 439  LEU A C     1 1 
ATOM   3545 O  O     . LEU A 1 438 ? 18.783  44.836  -15.498 1   24.45  ? 439  LEU A O     1 1 
ATOM   3546 C  CB    . LEU A 1 438 ? 16.15   46.065  -15.044 1   24.12  ? 439  LEU A CB    1 1 
ATOM   3547 C  CG    . LEU A 1 438 ? 15.481  45.002  -15.966 1   27.29  ? 439  LEU A CG    1 1 
ATOM   3548 C  CD1   . LEU A 1 438 ? 14.752  43.921  -15.178 1   27.98  ? 439  LEU A CD1   1 1 
ATOM   3549 C  CD2   . LEU A 1 438 ? 14.483  45.632  -16.856 1   28.76  ? 439  LEU A CD2   1 1 
ATOM   3550 N  N     . ILE A 1 439 ? 18.146  43.332  -13.914 1   24.65  ? 440  ILE A N     1 1 
ATOM   3551 C  CA    . ILE A 1 439 ? 19.076  42.29   -14.305 1   24.82  ? 440  ILE A CA    1 1 
ATOM   3552 C  C     . ILE A 1 439 ? 18.329  41.23   -15.106 1   24.27  ? 440  ILE A C     1 1 
ATOM   3553 O  O     . ILE A 1 439 ? 17.389  40.628  -14.595 1   23.33  ? 440  ILE A O     1 1 
ATOM   3554 C  CB    . ILE A 1 439 ? 19.7    41.648  -13.043 1   25.79  ? 440  ILE A CB    1 1 
ATOM   3555 C  CG1   . ILE A 1 439 ? 20.242  42.709  -12.04  1   27.3   ? 440  ILE A CG1   1 1 
ATOM   3556 C  CG2   . ILE A 1 439 ? 20.756  40.604  -13.418 1   26.02  ? 440  ILE A CG2   1 1 
ATOM   3557 C  CD1   . ILE A 1 439 ? 21.409  43.461  -12.5   1   30.15  ? 440  ILE A CD1   1 1 
ATOM   3558 N  N     . ILE A 1 440 ? 18.755  40.982  -16.349 1   24.53  ? 441  ILE A N     1 1 
ATOM   3559 C  CA    . ILE A 1 440 ? 18.18   39.92   -17.171 1   24.6   ? 441  ILE A CA    1 1 
ATOM   3560 C  C     . ILE A 1 440 ? 19.024  38.696  -16.855 1   24.46  ? 441  ILE A C     1 1 
ATOM   3561 O  O     . ILE A 1 440 ? 20.114  38.534  -17.384 1   25.2   ? 441  ILE A O     1 1 
ATOM   3562 C  CB    . ILE A 1 440 ? 18.179  40.264  -18.68  1   25.02  ? 441  ILE A CB    1 1 
ATOM   3563 C  CG1   . ILE A 1 440 ? 17.471  41.636  -18.936 1   25.97  ? 441  ILE A CG1   1 1 
ATOM   3564 C  CG2   . ILE A 1 440 ? 17.502  39.141  -19.486 1   25.13  ? 441  ILE A CG2   1 1 
ATOM   3565 C  CD1   . ILE A 1 440 ? 16.051  41.684  -18.571 1   27.41  ? 441  ILE A CD1   1 1 
ATOM   3566 N  N     . ASN A 1 441 ? 18.552  37.875  -15.939 1   23.54  ? 442  ASN A N     1 1 
ATOM   3567 C  CA    . ASN A 1 441 ? 19.292  36.74   -15.438 1   23.42  ? 442  ASN A CA    1 1 
ATOM   3568 C  C     . ASN A 1 441 ? 18.925  35.402  -16.081 1   24.28  ? 442  ASN A C     1 1 
ATOM   3569 O  O     . ASN A 1 441 ? 19.352  34.377  -15.577 1   24.14  ? 442  ASN A O     1 1 
ATOM   3570 C  CB    . ASN A 1 441 ? 19.072  36.692  -13.925 1   23.1   ? 442  ASN A CB    1 1 
ATOM   3571 C  CG    . ASN A 1 441 ? 20.06   35.849  -13.158 1   24.02  ? 442  ASN A CG    1 1 
ATOM   3572 O  OD1   . ASN A 1 441 ? 21.268  36.083  -13.16  1   23.57  ? 442  ASN A OD1   1 1 
ATOM   3573 N  ND2   . ASN A 1 441 ? 19.549  34.829  -12.494 1   24.64  ? 442  ASN A ND2   1 1 
ATOM   3574 N  N     . LYS A 1 442 ? 18.12   35.396  -17.158 1   25.49  ? 443  LYS A N     1 1 
ATOM   3575 C  CA    . LYS A 1 442 ? 17.627  34.161  -17.79  1   26.87  ? 443  LYS A CA    1 1 
ATOM   3576 C  C     . LYS A 1 442 ? 18.698  33.149  -18.136 1   27.07  ? 443  LYS A C     1 1 
ATOM   3577 O  O     . LYS A 1 442 ? 18.585  31.992  -17.734 1   27.33  ? 443  LYS A O     1 1 
ATOM   3578 C  CB    . LYS A 1 442 ? 16.77   34.456  -19.038 1   30.71  ? 443  LYS A CB    1 1 
ATOM   3579 C  CG    . LYS A 1 442 ? 15.311  34.774  -18.748 1   38.32  ? 443  LYS A CG    1 1 
ATOM   3580 C  CD    . LYS A 1 442 ? 14.438  34.392  -19.936 1   45.9   ? 443  LYS A CD    1 1 
ATOM   3581 C  CE    . LYS A 1 442 ? 13.095  33.808  -19.528 1   52.13  ? 443  LYS A CE    1 1 
ATOM   3582 N  NZ    . LYS A 1 442 ? 13.199  32.365  -19.13  1   55.86  ? 443  LYS A NZ    1 1 
ATOM   3583 N  N     . ASN A 1 443 ? 19.713  33.558  -18.905 1   27     ? 444  ASN A N     1 1 
ATOM   3584 C  CA    . ASN A 1 443 ? 20.779  32.661  -19.324 1   28     ? 444  ASN A CA    1 1 
ATOM   3585 C  C     . ASN A 1 443 ? 21.571  32.11   -18.134 1   27.52  ? 444  ASN A C     1 1 
ATOM   3586 O  O     . ASN A 1 443 ? 21.902  30.92   -18.11  1   28.76  ? 444  ASN A O     1 1 
ATOM   3587 C  CB    . ASN A 1 443 ? 21.694  33.369  -20.322 1   30.54  ? 444  ASN A CB    1 1 
ATOM   3588 C  CG    . ASN A 1 443 ? 21.113  33.44   -21.709 1   35.64  ? 444  ASN A CG    1 1 
ATOM   3589 O  OD1   . ASN A 1 443 ? 20.279  32.625  -22.082 1   38.2   ? 444  ASN A OD1   1 1 
ATOM   3590 N  ND2   . ASN A 1 443 ? 21.546  34.406  -22.515 1   36.66  ? 444  ASN A ND2   1 1 
ATOM   3591 N  N     . ASN A 1 444 ? 21.84   32.969  -17.14  1   25.34  ? 445  ASN A N     1 1 
ATOM   3592 C  CA    . ASN A 1 444 ? 22.582  32.615  -15.941 1   23.65  ? 445  ASN A CA    1 1 
ATOM   3593 C  C     . ASN A 1 444 ? 21.81   31.594  -15.112 1   23.5   ? 445  ASN A C     1 1 
ATOM   3594 O  O     . ASN A 1 444 ? 22.374  30.566  -14.716 1   24.05  ? 445  ASN A O     1 1 
ATOM   3595 C  CB    . ASN A 1 444 ? 22.862  33.856  -15.137 1   23.46  ? 445  ASN A CB    1 1 
ATOM   3596 C  CG    . ASN A 1 444 ? 23.828  33.627  -14.031 1   26.18  ? 445  ASN A CG    1 1 
ATOM   3597 O  OD1   . ASN A 1 444 ? 24.687  32.753  -14.095 1   28.22  ? 445  ASN A OD1   1 1 
ATOM   3598 N  ND2   . ASN A 1 444 ? 23.756  34.445  -13.009 1   26.07  ? 445  ASN A ND2   1 1 
ATOM   3599 N  N     . LYS A 1 445 ? 20.486  31.817  -14.928 1   22.54  ? 446  LYS A N     1 1 
ATOM   3600 C  CA    . LYS A 1 445 ? 19.61   30.888  -14.212 1   22.09  ? 446  LYS A CA    1 1 
ATOM   3601 C  C     . LYS A 1 445 ? 19.65   29.524  -14.923 1   22.44  ? 446  LYS A C     1 1 
ATOM   3602 O  O     . LYS A 1 445 ? 19.904  28.509  -14.277 1   21.26  ? 446  LYS A O     1 1 
ATOM   3603 C  CB    . LYS A 1 445 ? 18.164  31.434  -14.121 1   21.79  ? 446  LYS A CB    1 1 
ATOM   3604 C  CG    . LYS A 1 445 ? 17.117  30.382  -13.724 1   22.14  ? 446  LYS A CG    1 1 
ATOM   3605 C  CD    . LYS A 1 445 ? 15.726  30.973  -13.531 1   23.93  ? 446  LYS A CD    1 1 
ATOM   3606 C  CE    . LYS A 1 445 ? 14.719  29.941  -13.098 1   22.22  ? 446  LYS A CE    1 1 
ATOM   3607 N  NZ    . LYS A 1 445 ? 13.374  30.535  -12.853 1   20.44  ? 446  LYS A NZ    1 1 
ATOM   3608 N  N     . GLU A 1 446 ? 19.482  29.523  -16.255 1   24.22  ? 447  GLU A N     1 1 
ATOM   3609 C  CA    . GLU A 1 446 ? 19.494  28.279  -17.021 1   26.99  ? 447  GLU A CA    1 1 
ATOM   3610 C  C     . GLU A 1 446 ? 20.807  27.511  -16.859 1   27.48  ? 447  GLU A C     1 1 
ATOM   3611 O  O     . GLU A 1 446 ? 20.769  26.299  -16.702 1   28.13  ? 447  GLU A O     1 1 
ATOM   3612 C  CB    . GLU A 1 446 ? 19.204  28.536  -18.496 1   31.6   ? 447  GLU A CB    1 1 
ATOM   3613 C  CG    . GLU A 1 446 ? 17.74   28.746  -18.805 1   39.95  ? 447  GLU A CG    1 1 
ATOM   3614 C  CD    . GLU A 1 446 ? 17.45   29.162  -20.237 1   53.28  ? 447  GLU A CD    1 1 
ATOM   3615 O  OE1   . GLU A 1 446 ? 18.408  29.302  -21.035 1   56.6   ? 447  GLU A OE1   1 1 
ATOM   3616 O  OE2   . GLU A 1 446 ? 16.255  29.361  -20.558 1   57.45  ? 447  GLU A OE2   1 1 
ATOM   3617 N  N     . SER A 1 447 ? 21.952  28.218  -16.83  1   27.09  ? 448  SER A N     1 1 
ATOM   3618 C  CA    . SER A 1 447 ? 23.245  27.585  -16.619 1   27.33  ? 448  SER A CA    1 1 
ATOM   3619 C  C     . SER A 1 447 ? 23.329  26.94   -15.239 1   25.37  ? 448  SER A C     1 1 
ATOM   3620 O  O     . SER A 1 447 ? 23.87   25.854  -15.109 1   24.93  ? 448  SER A O     1 1 
ATOM   3621 C  CB    . SER A 1 447 ? 24.371  28.6    -16.773 1   30.8   ? 448  SER A CB    1 1 
ATOM   3622 O  OG    . SER A 1 447 ? 24.653  28.831  -18.141 1   35.99  ? 448  SER A OG    1 1 
ATOM   3623 N  N     . ILE A 1 448 ? 22.81   27.612  -14.217 1   23.96  ? 449  ILE A N     1 1 
ATOM   3624 C  CA    . ILE A 1 448 ? 22.862  27.106  -12.853 1   23.23  ? 449  ILE A CA    1 1 
ATOM   3625 C  C     . ILE A 1 448 ? 21.996  25.87   -12.697 1   23.39  ? 449  ILE A C     1 1 
ATOM   3626 O  O     . ILE A 1 448 ? 22.408  24.898  -12.043 1   23.09  ? 449  ILE A O     1 1 
ATOM   3627 C  CB    . ILE A 1 448 ? 22.505  28.232  -11.842 1   23.03  ? 449  ILE A CB    1 1 
ATOM   3628 C  CG1   . ILE A 1 448 ? 23.592  29.341  -11.846 1   22.87  ? 449  ILE A CG1   1 1 
ATOM   3629 C  CG2   . ILE A 1 448 ? 22.285  27.661  -10.438 1   23.44  ? 449  ILE A CG2   1 1 
ATOM   3630 C  CD1   . ILE A 1 448 ? 23.12   30.674  -11.28  1   23.61  ? 449  ILE A CD1   1 1 
ATOM   3631 N  N     . LEU A 1 449 ? 20.844  25.844  -13.378 1   23.61  ? 450  LEU A N     1 1 
ATOM   3632 C  CA    . LEU A 1 449 ? 19.941  24.705  -13.289 1   24.04  ? 450  LEU A CA    1 1 
ATOM   3633 C  C     . LEU A 1 449 ? 20.488  23.45   -13.995 1   25.27  ? 450  LEU A C     1 1 
ATOM   3634 O  O     . LEU A 1 449 ? 20.047  22.357  -13.655 1   23.8   ? 450  LEU A O     1 1 
ATOM   3635 C  CB    . LEU A 1 449 ? 18.512  25.076  -13.741 1   23.44  ? 450  LEU A CB    1 1 
ATOM   3636 C  CG    . LEU A 1 449 ? 17.856  26.223  -12.947 1   23.21  ? 450  LEU A CG    1 1 
ATOM   3637 C  CD1   . LEU A 1 449 ? 16.505  26.547  -13.488 1   23.92  ? 450  LEU A CD1   1 1 
ATOM   3638 C  CD2   . LEU A 1 449 ? 17.729  25.907  -11.495 1   22.54  ? 450  LEU A CD2   1 1 
ATOM   3639 N  N     . ARG A 1 450 ? 21.522  23.584  -14.872 1   27.81  ? 451  ARG A N     1 1 
ATOM   3640 C  CA    . ARG A 1 450 ? 22.216  22.415  -15.494 1   30.46  ? 451  ARG A CA    1 1 
ATOM   3641 C  C     . ARG A 1 450 ? 23.518  22.036  -14.756 1   32.25  ? 451  ARG A C     1 1 
ATOM   3642 O  O     . ARG A 1 450 ? 24.046  20.946  -14.973 1   32.83  ? 451  ARG A O     1 1 
ATOM   3643 C  CB    . ARG A 1 450 ? 22.603  22.668  -16.952 1   32.92  ? 451  ARG A CB    1 1 
ATOM   3644 C  CG    . ARG A 1 450 ? 21.487  23.156  -17.845 1   39.96  ? 451  ARG A CG    1 1 
ATOM   3645 C  CD    . ARG A 1 450 ? 21.938  23.308  -19.294 1   46.14  ? 451  ARG A CD    1 1 
ATOM   3646 N  NE    . ARG A 1 450 ? 23.177  24.08   -19.456 1   50     ? 451  ARG A NE    1 1 
ATOM   3647 C  CZ    . ARG A 1 450 ? 23.224  25.364  -19.798 1   52.79  ? 451  ARG A CZ    1 1 
ATOM   3648 N  NH1   . ARG A 1 450 ? 22.099  26.048  -20.003 1   51.21  ? 451  ARG A NH1   1 1 
ATOM   3649 N  NH2   . ARG A 1 450 ? 24.395  25.979  -19.932 1   52.86  ? 451  ARG A NH2   1 1 
ATOM   3650 N  N     . LYS A 1 451 ? 24.059  22.937  -13.933 1   33.23  ? 452  LYS A N     1 1 
ATOM   3651 C  CA    . LYS A 1 451 ? 25.312  22.727  -13.212 1   35.23  ? 452  LYS A CA    1 1 
ATOM   3652 C  C     . LYS A 1 451 ? 25.306  21.629  -12.142 1   36.31  ? 452  LYS A C     1 1 
ATOM   3653 O  O     . LYS A 1 451 ? 24.399  21.541  -11.297 1   36.93  ? 452  LYS A O     1 1 
ATOM   3654 C  CB    . LYS A 1 451 ? 25.788  24.034  -12.578 1   38.35  ? 452  LYS A CB    1 1 
ATOM   3655 C  CG    . LYS A 1 451 ? 27.079  24.554  -13.178 1   44.06  ? 452  LYS A CG    1 1 
ATOM   3656 C  CD    . LYS A 1 451 ? 26.977  26.06   -13.394 1   49.98  ? 452  LYS A CD    1 1 
ATOM   3657 C  CE    . LYS A 1 451 ? 28.113  26.633  -14.215 1   55.45  ? 452  LYS A CE    1 1 
ATOM   3658 N  NZ    . LYS A 1 451 ? 27.827  28.039  -14.633 1   58.39  ? 452  LYS A NZ    1 1 
ATOM   3659 N  N     . THR A 1 452 ? 26.357  20.808  -12.175 1   36.04  ? 453  THR A N     1 1 
ATOM   3660 C  CA    . THR A 1 452 ? 26.601  19.737  -11.215 1   36.56  ? 453  THR A CA    1 1 
ATOM   3661 C  C     . THR A 1 452 ? 28.096  19.74   -10.894 1   36.18  ? 453  THR A C     1 1 
ATOM   3662 O  O     . THR A 1 452 ? 28.91   20.016  -11.786 1   36.38  ? 453  THR A O     1 1 
ATOM   3663 C  CB    . THR A 1 452 ? 26.222  18.353  -11.805 1   38.23  ? 453  THR A CB    1 1 
ATOM   3664 O  OG1   . THR A 1 452 ? 26.998  18.082  -12.981 1   38.92  ? 453  THR A OG1   1 1 
ATOM   3665 C  CG2   . THR A 1 452 ? 24.726  18.209  -12.091 1   38.9   ? 453  THR A CG2   1 1 
ATOM   3666 N  N     . SER A 1 453 ? 28.47   19.424  -9.644  1   35.46  ? 454  SER A N     1 1 
ATOM   3667 C  CA    . SER A 1 453 ? 29.894  19.323  -9.305  1   35.48  ? 454  SER A CA    1 1 
ATOM   3668 C  C     . SER A 1 453 ? 30.484  18.028  -9.942  1   36.18  ? 454  SER A C     1 1 
ATOM   3669 O  O     . SER A 1 453 ? 29.73   17.15   -10.392 1   36.12  ? 454  SER A O     1 1 
ATOM   3670 C  CB    . SER A 1 453 ? 30.104  19.342  -7.795  1   35.66  ? 454  SER A CB    1 1 
ATOM   3671 O  OG    . SER A 1 453 ? 29.541  18.2    -7.171  1   37     ? 454  SER A OG    1 1 
ATOM   3672 N  N     . LYS A 1 454 ? 31.831  17.949  -10.01  1   36.03  ? 455  LYS A N     1 1 
ATOM   3673 C  CA    . LYS A 1 454 ? 32.623  16.848  -10.569 1   36.15  ? 455  LYS A CA    1 1 
ATOM   3674 C  C     . LYS A 1 454 ? 32.087  15.479  -10.168 1   35.65  ? 455  LYS A C     1 1 
ATOM   3675 O  O     . LYS A 1 454 ? 31.882  15.238  -8.98   1   35.2   ? 455  LYS A O     1 1 
ATOM   3676 C  CB    . LYS A 1 454 ? 34.087  16.994  -10.089 1   38.99  ? 455  LYS A CB    1 1 
ATOM   3677 C  CG    . LYS A 1 454 ? 35.036  15.909  -10.564 1   45.32  ? 455  LYS A CG    1 1 
ATOM   3678 C  CD    . LYS A 1 454 ? 36.436  16.044  -9.933  1   51.58  ? 455  LYS A CD    1 1 
ATOM   3679 C  CE    . LYS A 1 454 ? 37.332  14.877  -10.311 1   56.25  ? 455  LYS A CE    1 1 
ATOM   3680 N  NZ    . LYS A 1 454 ? 38.693  14.984  -9.712  1   58.81  ? 455  LYS A NZ    1 1 
ATOM   3681 N  N     . GLN A 1 455 ? 31.847  14.594  -11.15  1   35.43  ? 456  GLN A N     1 1 
ATOM   3682 C  CA    . GLN A 1 455 ? 31.369  13.256  -10.844 1   36.23  ? 456  GLN A CA    1 1 
ATOM   3683 C  C     . GLN A 1 455 ? 32.527  12.477  -10.24  1   35.73  ? 456  GLN A C     1 1 
ATOM   3684 O  O     . GLN A 1 455 ? 33.626  12.455  -10.805 1   35.64  ? 456  GLN A O     1 1 
ATOM   3685 C  CB    . GLN A 1 455 ? 30.853  12.534  -12.095 1   38.96  ? 456  GLN A CB    1 1 
ATOM   3686 C  CG    . GLN A 1 455 ? 29.682  13.223  -12.76  1   45     ? 456  GLN A CG    1 1 
ATOM   3687 C  CD    . GLN A 1 455 ? 28.462  13.306  -11.875 1   51.99  ? 456  GLN A CD    1 1 
ATOM   3688 O  OE1   . GLN A 1 455 ? 28.016  12.313  -11.275 1   54.42  ? 456  GLN A OE1   1 1 
ATOM   3689 N  NE2   . GLN A 1 455 ? 27.883  14.497  -11.79  1   52.87  ? 456  GLN A NE2   1 1 
ATOM   3690 N  N     . GLN A 1 456 ? 32.287  11.863  -9.084  1   34.62  ? 457  GLN A N     1 1 
ATOM   3691 C  CA    . GLN A 1 456 ? 33.317  11.086  -8.416  1   34.08  ? 457  GLN A CA    1 1 
ATOM   3692 C  C     . GLN A 1 456 ? 32.716  10.26   -7.296  1   31.89  ? 457  GLN A C     1 1 
ATOM   3693 O  O     . GLN A 1 456 ? 31.751  10.67   -6.643  1   31.49  ? 457  GLN A O     1 1 
ATOM   3694 C  CB    . GLN A 1 456 ? 34.478  11.97   -7.908  1   36.26  ? 457  GLN A CB    1 1 
ATOM   3695 C  CG    . GLN A 1 456 ? 34.099  12.94   -6.804  1   41.65  ? 457  GLN A CG    1 1 
ATOM   3696 C  CD    . GLN A 1 456 ? 35.302  13.651  -6.227  1   49.14  ? 457  GLN A CD    1 1 
ATOM   3697 O  OE1   . GLN A 1 456 ? 35.268  14.859  -5.965  1   51.39  ? 457  GLN A OE1   1 1 
ATOM   3698 N  NE2   . GLN A 1 456 ? 36.396  12.918  -6.018  1   50.67  ? 457  GLN A NE2   1 1 
ATOM   3699 N  N     . ASN A 1 457 ? 33.275  9.087   -7.106  1   30.32  ? 458  ASN A N     1 1 
ATOM   3700 C  CA    . ASN A 1 457 ? 32.85   8.18    -6.059  1   29.37  ? 458  ASN A CA    1 1 
ATOM   3701 C  C     . ASN A 1 457 ? 33.331  8.672   -4.711  1   27.99  ? 458  ASN A C     1 1 
ATOM   3702 O  O     . ASN A 1 457 ? 34.413  9.278   -4.607  1   28.13  ? 458  ASN A O     1 1 
ATOM   3703 C  CB    . ASN A 1 457 ? 33.36   6.766   -6.33   1   29.47  ? 458  ASN A CB    1 1 
ATOM   3704 C  CG    . ASN A 1 457 ? 32.806  6.137   -7.595  1   31.5   ? 458  ASN A CG    1 1 
ATOM   3705 O  OD1   . ASN A 1 457 ? 33.471  5.314   -8.254  1   33.22  ? 458  ASN A OD1   1 1 
ATOM   3706 N  ND2   . ASN A 1 457 ? 31.575  6.475   -7.954  1   30.12  ? 458  ASN A ND2   1 1 
ATOM   3707 N  N     . ILE A 1 458 ? 32.516  8.439   -3.677  1   26.11  ? 459  ILE A N     1 1 
ATOM   3708 C  CA    . ILE A 1 458 ? 32.89   8.852   -2.341  1   25.68  ? 459  ILE A CA    1 1 
ATOM   3709 C  C     . ILE A 1 458 ? 32.859  7.669   -1.359  1   24.67  ? 459  ILE A C     1 1 
ATOM   3710 O  O     . ILE A 1 458 ? 31.997  6.791   -1.429  1   24.5   ? 459  ILE A O     1 1 
ATOM   3711 C  CB    . ILE A 1 458 ? 32.079  10.086  -1.874  1   26.8   ? 459  ILE A CB    1 1 
ATOM   3712 C  CG1   . ILE A 1 458 ? 32.496  11.325  -2.704  1   28.41  ? 459  ILE A CG1   1 1 
ATOM   3713 C  CG2   . ILE A 1 458 ? 32.273  10.356  -0.384  1   27.24  ? 459  ILE A CG2   1 1 
ATOM   3714 C  CD1   . ILE A 1 458 ? 31.569  12.333  -2.708  1   30.13  ? 459  ILE A CD1   1 1 
ATOM   3715 N  N     . LEU A 1 459 ? 33.882  7.611   -0.514  1   23.39  ? 460  LEU A N     1 1 
ATOM   3716 C  CA    . LEU A 1 459 ? 34.033  6.67    0.563   1   23.45  ? 460  LEU A CA    1 1 
ATOM   3717 C  C     . LEU A 1 459 ? 34.701  7.505   1.604   1   23.02  ? 460  LEU A C     1 1 
ATOM   3718 O  O     . LEU A 1 459 ? 35.891  7.808   1.468   1   24.99  ? 460  LEU A O     1 1 
ATOM   3719 C  CB    . LEU A 1 459 ? 34.959  5.513   0.165   1   24.55  ? 460  LEU A CB    1 1 
ATOM   3720 C  CG    . LEU A 1 459 ? 35.18   4.477   1.273   1   26.67  ? 460  LEU A CG    1 1 
ATOM   3721 C  CD1   . LEU A 1 459 ? 33.885  3.77    1.629   1   27.23  ? 460  LEU A CD1   1 1 
ATOM   3722 C  CD2   . LEU A 1 459 ? 36.255  3.509   0.896   1   27.76  ? 460  LEU A CD2   1 1 
ATOM   3723 N  N     . VAL A 1 460 ? 33.946  7.998   2.57    1   20.93  ? 461  VAL A N     1 1 
ATOM   3724 C  CA    . VAL A 1 460 ? 34.514  8.863   3.603   1   19.38  ? 461  VAL A CA    1 1 
ATOM   3725 C  C     . VAL A 1 460 ? 35.422  8.033   4.482   1   18.76  ? 461  VAL A C     1 1 
ATOM   3726 O  O     . VAL A 1 460 ? 35.03   6.952   4.909   1   18.39  ? 461  VAL A O     1 1 
ATOM   3727 C  CB    . VAL A 1 460 ? 33.414  9.538   4.446   1   19.03  ? 461  VAL A CB    1 1 
ATOM   3728 C  CG1   . VAL A 1 460 ? 34.042  10.471  5.479   1   18.63  ? 461  VAL A CG1   1 1 
ATOM   3729 C  CG2   . VAL A 1 460 ? 32.4    10.269  3.558   1   18.86  ? 461  VAL A CG2   1 1 
ATOM   3730 N  N     . ASP A 1 461 ? 36.634  8.493   4.708   1   18.2   ? 462  ASP A N     1 1 
ATOM   3731 C  CA    . ASP A 1 461 ? 37.569  7.773   5.554   1   18.76  ? 462  ASP A CA    1 1 
ATOM   3732 C  C     . ASP A 1 461 ? 37.161  7.998   7.016   1   18.58  ? 462  ASP A C     1 1 
ATOM   3733 O  O     . ASP A 1 461 ? 36.881  9.125   7.407   1   17.83  ? 462  ASP A O     1 1 
ATOM   3734 C  CB    . ASP A 1 461 ? 39.01   8.238   5.279   1   21.6   ? 462  ASP A CB    1 1 
ATOM   3735 C  CG    . ASP A 1 461 ? 39.988  7.416   6.061   1   29.55  ? 462  ASP A CG    1 1 
ATOM   3736 O  OD1   . ASP A 1 461 ? 40.3    6.294   5.62    1   32.49  ? 462  ASP A OD1   1 1 
ATOM   3737 O  OD2   . ASP A 1 461 ? 40.396  7.864   7.139   1   32.37  ? 462  ASP A OD2   1 1 
ATOM   3738 N  N     . PRO A 1 462 ? 37.133  6.943   7.845   1   19.37  ? 463  PRO A N     1 1 
ATOM   3739 C  CA    . PRO A 1 462 ? 36.658  7.117   9.228   1   20.23  ? 463  PRO A CA    1 1 
ATOM   3740 C  C     . PRO A 1 462 ? 37.62   7.85    10.167  1   20.9   ? 463  PRO A C     1 1 
ATOM   3741 O  O     . PRO A 1 462 ? 37.317  7.988   11.346  1   21.44  ? 463  PRO A O     1 1 
ATOM   3742 C  CB    . PRO A 1 462 ? 36.345  5.683   9.691   1   20.82  ? 463  PRO A CB    1 1 
ATOM   3743 C  CG    . PRO A 1 462 ? 36.376  4.843   8.439   1   21.15  ? 463  PRO A CG    1 1 
ATOM   3744 C  CD    . PRO A 1 462 ? 37.354  5.526   7.534   1   19.23  ? 463  PRO A CD    1 1 
ATOM   3745 N  N     . THR A 1 463 ? 38.748  8.366   9.657   1   20.87  ? 464  THR A N     1 1 
ATOM   3746 C  CA    . THR A 1 463 ? 39.682  9.131   10.471  1   20.63  ? 464  THR A CA    1 1 
ATOM   3747 C  C     . THR A 1 463 ? 39.637  10.561  9.973   1   21.63  ? 464  THR A C     1 1 
ATOM   3748 O  O     . THR A 1 463 ? 39.958  10.834  8.815   1   21.88  ? 464  THR A O     1 1 
ATOM   3749 C  CB    . THR A 1 463 ? 41.104  8.518   10.434  1   20.88  ? 464  THR A CB    1 1 
ATOM   3750 O  OG1   . THR A 1 463 ? 41.076  7.191   10.993  1   21.26  ? 464  THR A OG1   1 1 
ATOM   3751 C  CG2   . THR A 1 463 ? 42.135  9.377   11.168  1   20.82  ? 464  THR A CG2   1 1 
ATOM   3752 N  N     . PRO A 1 464 ? 39.174  11.491  10.819  1   22.05  ? 465  PRO A N     1 1 
ATOM   3753 C  CA    . PRO A 1 464 ? 39.082  12.89   10.386  1   22.23  ? 465  PRO A CA    1 1 
ATOM   3754 C  C     . PRO A 1 464 ? 40.438  13.619  10.464  1   22.66  ? 465  PRO A C     1 1 
ATOM   3755 O  O     . PRO A 1 464 ? 41.416  13.051  10.946  1   22.98  ? 465  PRO A O     1 1 
ATOM   3756 C  CB    . PRO A 1 464 ? 38.059  13.476  11.365  1   22.58  ? 465  PRO A CB    1 1 
ATOM   3757 C  CG    . PRO A 1 464 ? 38.326  12.761  12.622  1   23.28  ? 465  PRO A CG    1 1 
ATOM   3758 C  CD    . PRO A 1 464 ? 38.728  11.33   12.217  1   21.96  ? 465  PRO A CD    1 1 
ATOM   3759 N  N     . ASN A 1 465 ? 40.493  14.864  9.992   1   22.8   ? 466  ASN A N     1 1 
ATOM   3760 C  CA    . ASN A 1 465 ? 41.704  15.716  9.979   1   23.48  ? 466  ASN A CA    1 1 
ATOM   3761 C  C     . ASN A 1 465 ? 42.296  15.82   11.389  1   23.76  ? 466  ASN A C     1 1 
ATOM   3762 O  O     . ASN A 1 465 ? 43.511  15.74   11.562  1   24.17  ? 466  ASN A O     1 1 
ATOM   3763 C  CB    . ASN A 1 465 ? 41.356  17.139  9.451   1   24.13  ? 466  ASN A CB    1 1 
ATOM   3764 C  CG    . ASN A 1 465 ? 42.521  18.132  9.465   1   27.49  ? 466  ASN A CG    1 1 
ATOM   3765 O  OD1   . ASN A 1 465 ? 42.575  19.084  10.269  1   27.18  ? 466  ASN A OD1   1 1 
ATOM   3766 N  ND2   . ASN A 1 465 ? 43.476  17.931  8.571   1   28.8   ? 466  ASN A ND2   1 1 
ATOM   3767 N  N     . HIS A 1 466 ? 41.417  16.01   12.381  1   23.32  ? 467  HIS A N     1 1 
ATOM   3768 C  CA    . HIS A 1 466 ? 41.748  16.111  13.796  1   23.22  ? 467  HIS A CA    1 1 
ATOM   3769 C  C     . HIS A 1 466 ? 40.466  15.878  14.653  1   22.84  ? 467  HIS A C     1 1 
ATOM   3770 O  O     . HIS A 1 466 ? 39.342  15.936  14.148  1   23.02  ? 467  HIS A O     1 1 
ATOM   3771 C  CB    . HIS A 1 466 ? 42.418  17.474  14.12   1   23.4   ? 467  HIS A CB    1 1 
ATOM   3772 C  CG    . HIS A 1 466 ? 41.507  18.656  13.984  1   26.12  ? 467  HIS A CG    1 1 
ATOM   3773 N  ND1   . HIS A 1 466 ? 41.298  19.267  12.761  1   28.05  ? 467  HIS A ND1   1 1 
ATOM   3774 C  CD2   . HIS A 1 466 ? 40.757  19.291  14.922  1   27.73  ? 467  HIS A CD2   1 1 
ATOM   3775 C  CE1   . HIS A 1 466 ? 40.424  20.241  12.989  1   29.15  ? 467  HIS A CE1   1 1 
ATOM   3776 N  NE2   . HIS A 1 466 ? 40.078  20.303  14.274  1   28.95  ? 467  HIS A NE2   1 1 
ATOM   3777 N  N     . TYR A 1 467 ? 40.64   15.616  15.943  1   21.64  ? 468  TYR A N     1 1 
ATOM   3778 C  CA    . TYR A 1 467 ? 39.518  15.397  16.844  1   20.62  ? 468  TYR A CA    1 1 
ATOM   3779 C  C     . TYR A 1 467 ? 39.096  16.711  17.523  1   20.79  ? 468  TYR A C     1 1 
ATOM   3780 O  O     . TYR A 1 467 ? 39.946  17.479  17.99   1   20.83  ? 468  TYR A O     1 1 
ATOM   3781 C  CB    . TYR A 1 467 ? 39.828  14.255  17.828  1   19.89  ? 468  TYR A CB    1 1 
ATOM   3782 C  CG    . TYR A 1 467 ? 40.192  13      17.066  1   19.41  ? 468  TYR A CG    1 1 
ATOM   3783 C  CD1   . TYR A 1 467 ? 39.211  12.205  16.501  1   19.18  ? 468  TYR A CD1   1 1 
ATOM   3784 C  CD2   . TYR A 1 467 ? 41.51   12.732  16.724  1   19.45  ? 468  TYR A CD2   1 1 
ATOM   3785 C  CE1   . TYR A 1 467 ? 39.532  11.118  15.706  1   19.73  ? 468  TYR A CE1   1 1 
ATOM   3786 C  CE2   . TYR A 1 467 ? 41.841  11.669  15.898  1   19.76  ? 468  TYR A CE2   1 1 
ATOM   3787 C  CZ    . TYR A 1 467 ? 40.847  10.852  15.405  1   20.38  ? 468  TYR A CZ    1 1 
ATOM   3788 O  OH    . TYR A 1 467 ? 41.161  9.787   14.605  1   21.1   ? 468  TYR A OH    1 1 
ATOM   3789 N  N     . GLN A 1 468 ? 37.783  16.98   17.545  1   20.16  ? 469  GLN A N     1 1 
ATOM   3790 C  CA    . GLN A 1 468 ? 37.28   18.217  18.102  1   20.56  ? 469  GLN A CA    1 1 
ATOM   3791 C  C     . GLN A 1 468 ? 35.937  18.013  18.883  1   20.92  ? 469  GLN A C     1 1 
ATOM   3792 O  O     . GLN A 1 468 ? 35.657  16.898  19.301  1   21     ? 469  GLN A O     1 1 
ATOM   3793 C  CB    . GLN A 1 468 ? 37.218  19.315  16.988  1   22.5   ? 469  GLN A CB    1 1 
ATOM   3794 C  CG    . GLN A 1 468 ? 36.846  18.824  15.575  1   26.32  ? 469  GLN A CG    1 1 
ATOM   3795 C  CD    . GLN A 1 468 ? 35.402  18.397  15.489  1   31.29  ? 469  GLN A CD    1 1 
ATOM   3796 O  OE1   . GLN A 1 468 ? 34.938  17.582  16.276  1   33.66  ? 469  GLN A OE1   1 1 
ATOM   3797 N  NE2   . GLN A 1 468 ? 34.644  18.935  14.543  1   31.21  ? 469  GLN A NE2   1 1 
ATOM   3798 N  N     . GLU A 1 469 ? 35.141  19.089  19.129  1   21.37  ? 470  GLU A N     1 1 
ATOM   3799 C  CA    . GLU A 1 469 ? 33.908  19.062  19.9    1   22.13  ? 470  GLU A CA    1 1 
ATOM   3800 C  C     . GLU A 1 469 ? 32.907  17.966  19.48   1   21.23  ? 470  GLU A C     1 1 
ATOM   3801 O  O     . GLU A 1 469 ? 32.257  17.388  20.356  1   21.49  ? 470  GLU A O     1 1 
ATOM   3802 C  CB    . GLU A 1 469 ? 33.237  20.447  19.909  1   26.44  ? 470  GLU A CB    1 1 
ATOM   3803 C  CG    . GLU A 1 469 ? 32.562  20.871  18.607  1   34     ? 470  GLU A CG    1 1 
ATOM   3804 C  CD    . GLU A 1 469 ? 33.417  21.666  17.634  1   40.84  ? 470  GLU A CD    1 1 
ATOM   3805 O  OE1   . GLU A 1 469 ? 34.631  21.373  17.527  1   38.73  ? 470  GLU A OE1   1 1 
ATOM   3806 O  OE2   . GLU A 1 469 ? 32.865  22.579  16.972  1   45.37  ? 470  GLU A OE2   1 1 
ATOM   3807 N  N     . ASN A 1 470 ? 32.79   17.648  18.178  1   20.72  ? 471  ASN A N     1 1 
ATOM   3808 C  CA    . ASN A 1 470 ? 31.889  16.554  17.737  1   20.78  ? 471  ASN A CA    1 1 
ATOM   3809 C  C     . ASN A 1 470 ? 32.338  15.223  18.344  1   19.79  ? 471  ASN A C     1 1 
ATOM   3810 O  O     . ASN A 1 470 ? 31.496  14.414  18.76   1   20.16  ? 471  ASN A O     1 1 
ATOM   3811 C  CB    . ASN A 1 470 ? 31.892  16.4    16.212  1   22.72  ? 471  ASN A CB    1 1 
ATOM   3812 C  CG    . ASN A 1 470 ? 31.114  17.458  15.481  1   28.6   ? 471  ASN A CG    1 1 
ATOM   3813 O  OD1   . ASN A 1 470 ? 31.656  18.186  14.646  1   30.72  ? 471  ASN A OD1   1 1 
ATOM   3814 N  ND2   . ASN A 1 470 ? 29.827  17.542  15.753  1   30.11  ? 471  ASN A ND2   1 1 
ATOM   3815 N  N     . ASP A 1 471 ? 33.66   15.005  18.397  1   18.41  ? 472  ASP A N     1 1 
ATOM   3816 C  CA    . ASP A 1 471 ? 34.254  13.78   18.929  1   18.97  ? 472  ASP A CA    1 1 
ATOM   3817 C  C     . ASP A 1 471 ? 34.096  13.704  20.439  1   20.16  ? 472  ASP A C     1 1 
ATOM   3818 O  O     . ASP A 1 471 ? 33.781  12.636  20.96   1   20.1   ? 472  ASP A O     1 1 
ATOM   3819 C  CB    . ASP A 1 471 ? 35.713  13.654  18.481  1   19.4   ? 472  ASP A CB    1 1 
ATOM   3820 C  CG    . ASP A 1 471 ? 35.809  13.634  16.973  1   21.54  ? 472  ASP A CG    1 1 
ATOM   3821 O  OD1   . ASP A 1 471 ? 35.225  12.716  16.356  1   22.12  ? 472  ASP A OD1   1 1 
ATOM   3822 O  OD2   . ASP A 1 471 ? 36.41   14.571  16.402  1   21.16  ? 472  ASP A OD2   1 1 
ATOM   3823 N  N     . VAL A 1 472 ? 34.237  14.844  21.136  1   21.1   ? 473  VAL A N     1 1 
ATOM   3824 C  CA    . VAL A 1 472 ? 34.012  14.91   22.587  1   22.51  ? 473  VAL A CA    1 1 
ATOM   3825 C  C     . VAL A 1 472 ? 32.555  14.536  22.907  1   23.6   ? 473  VAL A C     1 1 
ATOM   3826 O  O     . VAL A 1 472 ? 32.287  13.754  23.822  1   24.56  ? 473  VAL A O     1 1 
ATOM   3827 C  CB    . VAL A 1 472 ? 34.343  16.313  23.145  1   22.98  ? 473  VAL A CB    1 1 
ATOM   3828 C  CG1   . VAL A 1 472 ? 34.005  16.399  24.629  1   23.61  ? 473  VAL A CG1   1 1 
ATOM   3829 C  CG2   . VAL A 1 472 ? 35.808  16.638  22.919  1   22.97  ? 473  VAL A CG2   1 1 
ATOM   3830 N  N     . ASP A 1 473 ? 31.625  15.064  22.104  1   22.72  ? 474  ASP A N     1 1 
ATOM   3831 C  CA    . ASP A 1 473 ? 30.213  14.807  22.232  1   22.54  ? 474  ASP A CA    1 1 
ATOM   3832 C  C     . ASP A 1 473 ? 29.894  13.319  21.988  1   21.27  ? 474  ASP A C     1 1 
ATOM   3833 O  O     . ASP A 1 473 ? 29.116  12.728  22.746  1   21.62  ? 474  ASP A O     1 1 
ATOM   3834 C  CB    . ASP A 1 473 ? 29.465  15.671  21.228  1   25.49  ? 474  ASP A CB    1 1 
ATOM   3835 C  CG    . ASP A 1 473 ? 27.992  15.584  21.433  1   35.22  ? 474  ASP A CG    1 1 
ATOM   3836 O  OD1   . ASP A 1 473 ? 27.531  15.941  22.535  1   38.03  ? 474  ASP A OD1   1 1 
ATOM   3837 O  OD2   . ASP A 1 473 ? 27.291  15.142  20.5    1   38.9   ? 474  ASP A OD2   1 1 
ATOM   3838 N  N     . THR A 1 474 ? 30.485  12.719  20.937  1   19.11  ? 475  THR A N     1 1 
ATOM   3839 C  CA    . THR A 1 474 ? 30.278  11.309  20.637  1   18.33  ? 475  THR A CA    1 1 
ATOM   3840 C  C     . THR A 1 474 ? 30.775  10.44   21.795  1   18.67  ? 475  THR A C     1 1 
ATOM   3841 O  O     . THR A 1 474 ? 30.073  9.518   22.213  1   18.37  ? 475  THR A O     1 1 
ATOM   3842 C  CB    . THR A 1 474 ? 30.987  10.945  19.338  1   18.56  ? 475  THR A CB    1 1 
ATOM   3843 O  OG1   . THR A 1 474 ? 30.389  11.658  18.261  1   19.47  ? 475  THR A OG1   1 1 
ATOM   3844 C  CG2   . THR A 1 474 ? 30.97   9.439   19.047  1   18.27  ? 475  THR A CG2   1 1 
ATOM   3845 N  N     . VAL A 1 475 ? 31.955  10.759  22.333  1   19.02  ? 476  VAL A N     1 1 
ATOM   3846 C  CA    . VAL A 1 475 ? 32.533  10.022  23.446  1   20.45  ? 476  VAL A CA    1 1 
ATOM   3847 C  C     . VAL A 1 475 ? 31.668  10.158  24.694  1   21.81  ? 476  VAL A C     1 1 
ATOM   3848 O  O     . VAL A 1 475 ? 31.384  9.15    25.326  1   22.16  ? 476  VAL A O     1 1 
ATOM   3849 C  CB    . VAL A 1 475 ? 34.007  10.425  23.706  1   21.49  ? 476  VAL A CB    1 1 
ATOM   3850 C  CG1   . VAL A 1 475 ? 34.516  9.827   25.009  1   22.53  ? 476  VAL A CG1   1 1 
ATOM   3851 C  CG2   . VAL A 1 475 ? 34.906  10.01   22.546  1   21.94  ? 476  VAL A CG2   1 1 
ATOM   3852 N  N     . ILE A 1 476 ? 31.229  11.386  25.041  1   22.23  ? 477  ILE A N     1 1 
ATOM   3853 C  CA    . ILE A 1 476 ? 30.406  11.61   26.237  1   23.17  ? 477  ILE A CA    1 1 
ATOM   3854 C  C     . ILE A 1 476 ? 29.095  10.877  26.127  1   23.87  ? 477  ILE A C     1 1 
ATOM   3855 O  O     . ILE A 1 476 ? 28.673  10.178  27.061  1   23.75  ? 477  ILE A O     1 1 
ATOM   3856 C  CB    . ILE A 1 476 ? 30.212  13.127  26.499  1   23.95  ? 477  ILE A CB    1 1 
ATOM   3857 C  CG1   . ILE A 1 476 ? 31.504  13.763  27.004  1   24.4   ? 477  ILE A CG1   1 1 
ATOM   3858 C  CG2   . ILE A 1 476 ? 29.031  13.425  27.454  1   24.76  ? 477  ILE A CG2   1 1 
ATOM   3859 C  CD1   . ILE A 1 476 ? 32.017  13.172  28.3    1   25.43  ? 477  ILE A CD1   1 1 
ATOM   3860 N  N     . TYR A 1 477 ? 28.453  11.016  24.964  1   24.12  ? 478  TYR A N     1 1 
ATOM   3861 C  CA    . TYR A 1 477 ? 27.196  10.349  24.695  1   24.94  ? 478  TYR A CA    1 1 
ATOM   3862 C  C     . TYR A 1 477 ? 27.325  8.84    24.788  1   24.06  ? 478  TYR A C     1 1 
ATOM   3863 O  O     . TYR A 1 477 ? 26.487  8.226   25.415  1   23.85  ? 478  TYR A O     1 1 
ATOM   3864 C  CB    . TYR A 1 477 ? 26.661  10.755  23.323  1   26.31  ? 478  TYR A CB    1 1 
ATOM   3865 C  CG    . TYR A 1 477 ? 25.276  10.231  23.025  1   28.52  ? 478  TYR A CG    1 1 
ATOM   3866 C  CD1   . TYR A 1 477 ? 24.147  10.854  23.547  1   30.66  ? 478  TYR A CD1   1 1 
ATOM   3867 C  CD2   . TYR A 1 477 ? 25.089  9.159   22.17   1   29.91  ? 478  TYR A CD2   1 1 
ATOM   3868 C  CE1   . TYR A 1 477 ? 22.868  10.384  23.259  1   31.79  ? 478  TYR A CE1   1 1 
ATOM   3869 C  CE2   . TYR A 1 477 ? 23.822  8.677   21.882  1   31.51  ? 478  TYR A CE2   1 1 
ATOM   3870 C  CZ    . TYR A 1 477 ? 22.714  9.292   22.423  1   33.03  ? 478  TYR A CZ    1 1 
ATOM   3871 O  OH    . TYR A 1 477 ? 21.472  8.79    22.118  1   35.84  ? 478  TYR A OH    1 1 
ATOM   3872 N  N     . SER A 1 478 ? 28.38   8.246   24.217  1   23.93  ? 479  SER A N     1 1 
ATOM   3873 C  CA    . SER A 1 478 ? 28.562  6.795   24.26   1   24.3   ? 479  SER A CA    1 1 
ATOM   3874 C  C     . SER A 1 478 ? 28.762  6.271   25.676  1   25.1   ? 479  SER A C     1 1 
ATOM   3875 O  O     . SER A 1 478 ? 28.185  5.252   26.043  1   25.98  ? 479  SER A O     1 1 
ATOM   3876 C  CB    . SER A 1 478 ? 29.726  6.368   23.375  1   25.16  ? 479  SER A CB    1 1 
ATOM   3877 O  OG    . SER A 1 478 ? 29.546  6.856   22.057  1   27.2   ? 479  SER A OG    1 1 
ATOM   3878 N  N     . ILE A 1 479 ? 29.534  6.975   26.476  1   24.75  ? 480  ILE A N     1 1 
ATOM   3879 C  CA    . ILE A 1 479 ? 29.818  6.584   27.848  1   26.07  ? 480  ILE A CA    1 1 
ATOM   3880 C  C     . ILE A 1 479 ? 28.572  6.658   28.741  1   27.76  ? 480  ILE A C     1 1 
ATOM   3881 O  O     . ILE A 1 479 ? 28.264  5.698   29.441  1   28.18  ? 480  ILE A O     1 1 
ATOM   3882 C  CB    . ILE A 1 479 ? 30.982  7.468   28.378  1   26.84  ? 480  ILE A CB    1 1 
ATOM   3883 C  CG1   . ILE A 1 479 ? 32.325  7.034   27.744  1   27.68  ? 480  ILE A CG1   1 1 
ATOM   3884 C  CG2   . ILE A 1 479 ? 31.054  7.501   29.907  1   27.66  ? 480  ILE A CG2   1 1 
ATOM   3885 C  CD1   . ILE A 1 479 ? 33.487  7.975   28.006  1   29.19  ? 480  ILE A CD1   1 1 
ATOM   3886 N  N     . PHE A 1 480 ? 27.864  7.79    28.72   1   28.23  ? 481  PHE A N     1 1 
ATOM   3887 C  CA    . PHE A 1 480 ? 26.726  7.992   29.597  1   29.21  ? 481  PHE A CA    1 1 
ATOM   3888 C  C     . PHE A 1 480 ? 25.427  7.465   29.079  1   31.84  ? 481  PHE A C     1 1 
ATOM   3889 O  O     . PHE A 1 480 ? 24.478  7.416   29.858  1   32.44  ? 481  PHE A O     1 1 
ATOM   3890 C  CB    . PHE A 1 480 ? 26.581  9.471   29.967  1   28.19  ? 481  PHE A CB    1 1 
ATOM   3891 C  CG    . PHE A 1 480 ? 27.659  9.93    30.91   1   27.79  ? 481  PHE A CG    1 1 
ATOM   3892 C  CD1   . PHE A 1 480 ? 27.68   9.501   32.223  1   27.82  ? 481  PHE A CD1   1 1 
ATOM   3893 C  CD2   . PHE A 1 480 ? 28.677  10.755  30.472  1   28.61  ? 481  PHE A CD2   1 1 
ATOM   3894 C  CE1   . PHE A 1 480 ? 28.689  9.897   33.084  1   28.6   ? 481  PHE A CE1   1 1 
ATOM   3895 C  CE2   . PHE A 1 480 ? 29.691  11.142  31.334  1   29.35  ? 481  PHE A CE2   1 1 
ATOM   3896 C  CZ    . PHE A 1 480 ? 29.687  10.716  32.637  1   28.79  ? 481  PHE A CZ    1 1 
ATOM   3897 N  N     . LYS A 1 481 ? 25.338  7.104   27.789  1   33.62  ? 482  LYS A N     1 1 
ATOM   3898 C  CA    . LYS A 1 481 ? 24.089  6.572   27.242  1   36.28  ? 482  LYS A CA    1 1 
ATOM   3899 C  C     . LYS A 1 481 ? 24.119  5.071   27.028  1   38.26  ? 482  LYS A C     1 1 
ATOM   3900 O  O     . LYS A 1 481 ? 23.063  4.453   27.055  1   38.49  ? 482  LYS A O     1 1 
ATOM   3901 C  CB    . LYS A 1 481 ? 23.674  7.271   25.941  1   39.12  ? 482  LYS A CB    1 1 
ATOM   3902 C  CG    . LYS A 1 481 ? 22.337  8.015   26.039  1   43.79  ? 482  LYS A CG    1 1 
ATOM   3903 C  CD    . LYS A 1 481 ? 22.37   9.178   27.046  1   47.09  ? 482  LYS A CD    1 1 
ATOM   3904 C  CE    . LYS A 1 481 ? 20.971  9.578   27.485  1   49.46  ? 482  LYS A CE    1 1 
ATOM   3905 N  NZ    . LYS A 1 481 ? 20.981  10.651  28.521  1   50.55  ? 482  LYS A NZ    1 1 
ATOM   3906 N  N     . TYR A 1 482 ? 25.312  4.474   26.821  1   39.14  ? 483  TYR A N     1 1 
ATOM   3907 C  CA    . TYR A 1 482 ? 25.404  3.042   26.553  1   40.03  ? 483  TYR A CA    1 1 
ATOM   3908 C  C     . TYR A 1 482 ? 26.253  2.266   27.536  1   41.07  ? 483  TYR A C     1 1 
ATOM   3909 O  O     . TYR A 1 482 ? 25.867  1.165   27.92   1   41.64  ? 483  TYR A O     1 1 
ATOM   3910 C  CB    . TYR A 1 482 ? 25.894  2.785   25.117  1   40.15  ? 483  TYR A CB    1 1 
ATOM   3911 C  CG    . TYR A 1 482 ? 24.992  3.403   24.075  1   41.61  ? 483  TYR A CG    1 1 
ATOM   3912 C  CD1   . TYR A 1 482 ? 23.66   3.032   23.975  1   42.56  ? 483  TYR A CD1   1 1 
ATOM   3913 C  CD2   . TYR A 1 482 ? 25.458  4.39    23.22   1   42.99  ? 483  TYR A CD2   1 1 
ATOM   3914 C  CE1   . TYR A 1 482 ? 22.817  3.616   23.042  1   43.79  ? 483  TYR A CE1   1 1 
ATOM   3915 C  CE2   . TYR A 1 482 ? 24.619  4.994   22.291  1   44.29  ? 483  TYR A CE2   1 1 
ATOM   3916 C  CZ    . TYR A 1 482 ? 23.299  4.595   22.197  1   45.36  ? 483  TYR A CZ    1 1 
ATOM   3917 O  OH    . TYR A 1 482 ? 22.445  5.201   21.305  1   47.72  ? 483  TYR A OH    1 1 
ATOM   3918 N  N     . ILE A 1 483 ? 27.418  2.795   27.917  1   41.34  ? 484  ILE A N     1 1 
ATOM   3919 C  CA    . ILE A 1 483 ? 28.328  2.054   28.791  1   41.99  ? 484  ILE A CA    1 1 
ATOM   3920 C  C     . ILE A 1 483 ? 27.884  2.08    30.266  1   42.63  ? 484  ILE A C     1 1 
ATOM   3921 O  O     . ILE A 1 483 ? 27.573  1.026   30.814  1   42.55  ? 484  ILE A O     1 1 
ATOM   3922 C  CB    . ILE A 1 483 ? 29.81   2.489   28.595  1   42.11  ? 484  ILE A CB    1 1 
ATOM   3923 C  CG1   . ILE A 1 483 ? 30.263  2.285   27.131  1   42.35  ? 484  ILE A CG1   1 1 
ATOM   3924 C  CG2   . ILE A 1 483 ? 30.726  1.747   29.563  1   42.55  ? 484  ILE A CG2   1 1 
ATOM   3925 C  CD1   . ILE A 1 483 ? 31.585  2.88    26.813  1   42.94  ? 484  ILE A CD1   1 1 
ATOM   3926 N  N     . VAL A 1 484 ? 27.836  3.257   30.898  1   43.13  ? 485  VAL A N     1 1 
ATOM   3927 C  CA    . VAL A 1 484 ? 27.456  3.377   32.308  1   44.36  ? 485  VAL A CA    1 1 
ATOM   3928 C  C     . VAL A 1 484 ? 25.994  2.918   32.624  1   46.27  ? 485  VAL A C     1 1 
ATOM   3929 O  O     . VAL A 1 484 ? 25.828  2.18    33.603  1   46.43  ? 485  VAL A O     1 1 
ATOM   3930 C  CB    . VAL A 1 484 ? 27.752  4.784   32.849  1   44.37  ? 485  VAL A CB    1 1 
ATOM   3931 C  CG1   . VAL A 1 484 ? 27.384  4.878   34.318  1   44.92  ? 485  VAL A CG1   1 1 
ATOM   3932 C  CG2   . VAL A 1 484 ? 29.221  5.128   32.649  1   44.54  ? 485  VAL A CG2   1 1 
ATOM   3933 N  N     . PRO A 1 485 ? 24.941  3.233   31.819  1   47.65  ? 486  PRO A N     1 1 
ATOM   3934 C  CA    . PRO A 1 485 ? 23.603  2.709   32.152  1   49.36  ? 486  PRO A CA    1 1 
ATOM   3935 C  C     . PRO A 1 485 ? 23.288  1.303   31.609  1   51.47  ? 486  PRO A C     1 1 
ATOM   3936 O  O     . PRO A 1 485 ? 22.251  0.742   31.959  1   51.99  ? 486  PRO A O     1 1 
ATOM   3937 C  CB    . PRO A 1 485 ? 22.672  3.748   31.536  1   49.76  ? 486  PRO A CB    1 1 
ATOM   3938 C  CG    . PRO A 1 485 ? 23.401  4.205   30.338  1   49.7   ? 486  PRO A CG    1 1 
ATOM   3939 C  CD    . PRO A 1 485 ? 24.883  4.088   30.614  1   47.38  ? 486  PRO A CD    1 1 
ATOM   3940 N  N     . ASN A 1 486 ? 24.167  0.757   30.746  1   52.66  ? 487  ASN A N     1 1 
ATOM   3941 C  CA    . ASN A 1 486 ? 24.035  -0.537  30.065  1   54.55  ? 487  ASN A CA    1 1 
ATOM   3942 C  C     . ASN A 1 486 ? 22.788  -0.583  29.172  1   55.67  ? 487  ASN A C     1 1 
ATOM   3943 O  O     . ASN A 1 486 ? 21.876  -1.378  29.395  1   55.48  ? 487  ASN A O     1 1 
ATOM   3944 C  CB    . ASN A 1 486 ? 24.128  -1.735  31.018  1   56.23  ? 487  ASN A CB    1 1 
ATOM   3945 C  CG    . ASN A 1 486 ? 25.556  -2.122  31.338  1   59.33  ? 487  ASN A CG    1 1 
ATOM   3946 O  OD1   . ASN A 1 486 ? 26.405  -1.273  31.673  1   60.03  ? 487  ASN A OD1   1 1 
ATOM   3947 N  ND2   . ASN A 1 486 ? 25.852  -3.419  31.237  1   60.2   ? 487  ASN A ND2   1 1 
ATOM   3948 N  N     . CYS A 1 487 ? 22.772  0.295   28.157  1   56.57  ? 488  CYS A N     1 1 
ATOM   3949 C  CA    . CYS A 1 487 ? 21.691  0.438   27.184  1   57.92  ? 488  CYS A CA    1 1 
ATOM   3950 C  C     . CYS A 1 487 ? 22.179  0.178   25.746  1   58.31  ? 488  CYS A C     1 1 
ATOM   3951 O  O     . CYS A 1 487 ? 23.384  0.186   25.482  1   58.64  ? 488  CYS A O     1 1 
ATOM   3952 C  CB    . CYS A 1 487 ? 21.058  1.822   27.303  1   59.68  ? 488  CYS A CB    1 1 
ATOM   3953 S  SG    . CYS A 1 487 ? 20.472  2.234   28.967  1   66.83  ? 488  CYS A SG    1 1 
ATOM   3954 N  N     . PHE A 1 488 ? 21.241  -0.045  24.816  1   58.19  ? 489  PHE A N     1 1 
ATOM   3955 C  CA    . PHE A 1 488 ? 21.578  -0.236  23.403  1   58.64  ? 489  PHE A CA    1 1 
ATOM   3956 C  C     . PHE A 1 488 ? 20.768  0.67    22.453  1   58.82  ? 489  PHE A C     1 1 
ATOM   3957 O  O     . PHE A 1 488 ? 21.003  0.656   21.252  1   58.75  ? 489  PHE A O     1 1 
ATOM   3958 C  CB    . PHE A 1 488 ? 21.499  -1.716  22.971  1   58.6   ? 489  PHE A CB    1 1 
ATOM   3959 C  CG    . PHE A 1 488 ? 20.137  -2.366  22.847  1   59.2   ? 489  PHE A CG    1 1 
ATOM   3960 C  CD1   . PHE A 1 488 ? 19.374  -2.203  21.701  1   59.81  ? 489  PHE A CD1   1 1 
ATOM   3961 C  CD2   . PHE A 1 488 ? 19.692  -3.263  23.802  1   60.06  ? 489  PHE A CD2   1 1 
ATOM   3962 C  CE1   . PHE A 1 488 ? 18.153  -2.849  21.559  1   60.47  ? 489  PHE A CE1   1 1 
ATOM   3963 C  CE2   . PHE A 1 488 ? 18.472  -3.913  23.653  1   60.73  ? 489  PHE A CE2   1 1 
ATOM   3964 C  CZ    . PHE A 1 488 ? 17.714  -3.705  22.531  1   60.42  ? 489  PHE A CZ    1 1 
ATOM   3965 N  N     . SER A 1 489 ? 19.814  1.436   22.979  1   59.06  ? 490  SER A N     1 1 
ATOM   3966 C  CA    . SER A 1 489 ? 18.974  2.313   22.174  1   60.07  ? 490  SER A CA    1 1 
ATOM   3967 C  C     . SER A 1 489 ? 18.496  3.521   22.999  1   61.04  ? 490  SER A C     1 1 
ATOM   3968 O  O     . SER A 1 489 ? 18.684  3.56    24.218  1   61.03  ? 490  SER A O     1 1 
ATOM   3969 C  CB    . SER A 1 489 ? 17.779  1.533   21.611  1   61.05  ? 490  SER A CB    1 1 
ATOM   3970 O  OG    . SER A 1 489 ? 16.912  1.035   22.62   1   62.82  ? 490  SER A OG    1 1 
ATOM   3971 N  N     . GLY A 1 490 ? 17.883  4.49    22.323  1   61.68  ? 491  GLY A N     1 1 
ATOM   3972 C  CA    . GLY A 1 490 ? 17.321  5.679   22.95   1   62.84  ? 491  GLY A CA    1 1 
ATOM   3973 C  C     . GLY A 1 490 ? 16.152  5.363   23.866  1   63.85  ? 491  GLY A C     1 1 
ATOM   3974 O  O     . GLY A 1 490 ? 15.909  6.084   24.838  1   64.08  ? 491  GLY A O     1 1 
ATOM   3975 N  N     . MET A 1 491 ? 15.426  4.271   23.569  1   64.16  ? 492  MET A N     1 1 
ATOM   3976 C  CA    . MET A 1 491 ? 14.295  3.831   24.387  1   65.06  ? 492  MET A CA    1 1 
ATOM   3977 C  C     . MET A 1 491 ? 14.823  2.874   25.452  1   64.77  ? 492  MET A C     1 1 
ATOM   3978 O  O     . MET A 1 491 ? 14.699  1.656   25.306  1   64.76  ? 492  MET A O     1 1 
ATOM   3979 C  CB    . MET A 1 491 ? 13.192  3.141   23.549  1   66.68  ? 492  MET A CB    1 1 
ATOM   3980 C  CG    . MET A 1 491 ? 13.298  3.359   22.046  1   70.8   ? 492  MET A CG    1 1 
ATOM   3981 S  SD    . MET A 1 491 ? 13.149  5.092   21.498  1   79.87  ? 492  MET A SD    1 1 
ATOM   3982 C  CE    . MET A 1 491 ? 11.375  5.177   21.187  1   78.9   ? 492  MET A CE    1 1 
ATOM   3983 N  N     . CYS A 1 492 ? 15.438  3.435   26.51   1   64.31  ? 493  CYS A N     1 1 
ATOM   3984 C  CA    . CYS A 1 492 ? 16.029  2.665   27.607  1   64.21  ? 493  CYS A CA    1 1 
ATOM   3985 C  C     . CYS A 1 492 ? 16.246  3.518   28.878  1   63.56  ? 493  CYS A C     1 1 
ATOM   3986 O  O     . CYS A 1 492 ? 16.239  4.753   28.798  1   63.77  ? 493  CYS A O     1 1 
ATOM   3987 C  CB    . CYS A 1 492 ? 17.336  2.019   27.152  1   64.96  ? 493  CYS A CB    1 1 
ATOM   3988 N  N     . ASN A 1 493 ? 16.44   2.833   30.051  1   62.29  ? 494  ASN A N     1 1 
ATOM   3989 C  CA    . ASN A 1 493 ? 16.741  3.351   31.408  1   60.95  ? 494  ASN A CA    1 1 
ATOM   3990 C  C     . ASN A 1 493 ? 16.323  4.861   31.586  1   58.66  ? 494  ASN A C     1 1 
ATOM   3991 O  O     . ASN A 1 493 ? 15.405  5.243   30.854  1   59.02  ? 494  ASN A O     1 1 
ATOM   3992 C  CB    . ASN A 1 493 ? 18.231  3.051   31.725  1   62.49  ? 494  ASN A CB    1 1 
ATOM   3993 C  CG    . ASN A 1 493 ? 18.476  2.018   32.814  1   66.1   ? 494  ASN A CG    1 1 
ATOM   3994 O  OD1   . ASN A 1 493 ? 19.629  1.762   33.198  1   67.04  ? 494  ASN A OD1   1 1 
ATOM   3995 N  ND2   . ASN A 1 493 ? 17.413  1.402   33.341  1   66.69  ? 494  ASN A ND2   1 1 
ATOM   3996 N  N     . PRO A 1 494 ? 16.845  5.729   32.514  1   56.16  ? 495  PRO A N     1 1 
ATOM   3997 C  CA    . PRO A 1 494 ? 16.374  7.13    32.529  1   54.44  ? 495  PRO A CA    1 1 
ATOM   3998 C  C     . PRO A 1 494 ? 16.801  7.844   31.242  1   52.09  ? 495  PRO A C     1 1 
ATOM   3999 O  O     . PRO A 1 494 ? 17.958  7.751   30.831  1   51.9   ? 495  PRO A O     1 1 
ATOM   4000 C  CB    . PRO A 1 494 ? 17.034  7.72    33.776  1   55.4   ? 495  PRO A CB    1 1 
ATOM   4001 C  CG    . PRO A 1 494 ? 18.235  6.897   33.999  1   56.08  ? 495  PRO A CG    1 1 
ATOM   4002 C  CD    . PRO A 1 494 ? 17.905  5.513   33.523  1   55.11  ? 495  PRO A CD    1 1 
ATOM   4003 N  N     . PRO A 1 495 ? 15.852  8.479   30.534  1   50.02  ? 496  PRO A N     1 1 
ATOM   4004 C  CA    . PRO A 1 495 ? 16.199  9.117   29.251  1   48.52  ? 496  PRO A CA    1 1 
ATOM   4005 C  C     . PRO A 1 495 ? 17.136  10.32   29.353  1   46.8   ? 496  PRO A C     1 1 
ATOM   4006 O  O     . PRO A 1 495 ? 17.846  10.632  28.393  1   46.78  ? 496  PRO A O     1 1 
ATOM   4007 C  CB    . PRO A 1 495 ? 14.836  9.509   28.662  1   49.49  ? 496  PRO A CB    1 1 
ATOM   4008 C  CG    . PRO A 1 495 ? 13.795  8.828   29.527  1   50.17  ? 496  PRO A CG    1 1 
ATOM   4009 C  CD    . PRO A 1 495 ? 14.424  8.645   30.862  1   49.05  ? 496  PRO A CD    1 1 
ATOM   4010 N  N     . GLY A 1 496 ? 17.119  10.986  30.506  1   44.89  ? 497  GLY A N     1 1 
ATOM   4011 C  CA    . GLY A 1 496 ? 17.925  12.17   30.746  1   43.38  ? 497  GLY A CA    1 1 
ATOM   4012 C  C     . GLY A 1 496 ? 17.493  13.306  29.856  1   41.39  ? 497  GLY A C     1 1 
ATOM   4013 O  O     . GLY A 1 496 ? 16.323  13.399  29.504  1   41.49  ? 497  GLY A O     1 1 
ATOM   4014 N  N     . GLY A 1 497 ? 18.441  14.122  29.432  1   39.64  ? 498  GLY A N     1 1 
ATOM   4015 C  CA    . GLY A 1 497 ? 18.132  15.237  28.561  1   38.71  ? 498  GLY A CA    1 1 
ATOM   4016 C  C     . GLY A 1 497 ? 19.22   15.609  27.588  1   37.5   ? 498  GLY A C     1 1 
ATOM   4017 O  O     . GLY A 1 497 ? 20.363  15.162  27.697  1   36.49  ? 498  GLY A O     1 1 
ATOM   4018 N  N     . ASP A 1 498 ? 18.848  16.452  26.641  1   37.28  ? 499  ASP A N     1 1 
ATOM   4019 C  CA    . ASP A 1 498 ? 19.708  17.027  25.618  1   37.81  ? 499  ASP A CA    1 1 
ATOM   4020 C  C     . ASP A 1 498 ? 19.093  18.389  25.212  1   38.76  ? 499  ASP A C     1 1 
ATOM   4021 O  O     . ASP A 1 498 ? 18.218  18.895  25.921  1   38.81  ? 499  ASP A O     1 1 
ATOM   4022 C  CB    . ASP A 1 498 ? 19.896  16.05   24.434  1   39     ? 499  ASP A CB    1 1 
ATOM   4023 C  CG    . ASP A 1 498 ? 18.631  15.661  23.67   1   42.64  ? 499  ASP A CG    1 1 
ATOM   4024 O  OD1   . ASP A 1 498 ? 17.584  16.319  23.868  1   42.91  ? 499  ASP A OD1   1 1 
ATOM   4025 O  OD2   . ASP A 1 498 ? 18.691  14.701  22.872  1   43.93  ? 499  ASP A OD2   1 1 
ATOM   4026 N  N     . TRP A 1 499 ? 19.508  18.965  24.082  1   39.34  ? 500  TRP A N     1 1 
ATOM   4027 C  CA    . TRP A 1 499 ? 18.978  20.236  23.619  1   40.53  ? 500  TRP A CA    1 1 
ATOM   4028 C  C     . TRP A 1 499 ? 17.475  20.205  23.296  1   40.32  ? 500  TRP A C     1 1 
ATOM   4029 O  O     . TRP A 1 499 ? 16.849  21.263  23.285  1   41.16  ? 500  TRP A O     1 1 
ATOM   4030 C  CB    . TRP A 1 499 ? 19.782  20.721  22.398  1   41.59  ? 500  TRP A CB    1 1 
ATOM   4031 C  CG    . TRP A 1 499 ? 19.52   19.944  21.143  1   43.54  ? 500  TRP A CG    1 1 
ATOM   4032 C  CD1   . TRP A 1 499 ? 20.145  18.802  20.739  1   45     ? 500  TRP A CD1   1 1 
ATOM   4033 C  CD2   . TRP A 1 499 ? 18.553  20.255  20.129  1   44.36  ? 500  TRP A CD2   1 1 
ATOM   4034 N  NE1   . TRP A 1 499 ? 19.619  18.374  19.539  1   45.81  ? 500  TRP A NE1   1 1 
ATOM   4035 C  CE2   . TRP A 1 499 ? 18.637  19.25   19.145  1   45.54  ? 500  TRP A CE2   1 1 
ATOM   4036 C  CE3   . TRP A 1 499 ? 17.635  21.299  19.95   1   45.42  ? 500  TRP A CE3   1 1 
ATOM   4037 C  CZ2   . TRP A 1 499 ? 17.84   19.26   18      1   46.47  ? 500  TRP A CZ2   1 1 
ATOM   4038 C  CZ3   . TRP A 1 499 ? 16.83   21.294  18.827  1   46.54  ? 500  TRP A CZ3   1 1 
ATOM   4039 C  CH2   . TRP A 1 499 ? 16.945  20.29   17.862  1   46.7   ? 500  TRP A CH2   1 1 
ATOM   4040 N  N     . SER A 1 500 ? 16.898  19.022  23.032  1   39.01  ? 501  SER A N     1 1 
ATOM   4041 C  CA    . SER A 1 500 ? 15.487  18.882  22.643  1   38.5   ? 501  SER A CA    1 1 
ATOM   4042 C  C     . SER A 1 500 ? 14.466  18.671  23.792  1   37.67  ? 501  SER A C     1 1 
ATOM   4043 O  O     . SER A 1 500 ? 13.249  18.648  23.545  1   37.83  ? 501  SER A O     1 1 
ATOM   4044 C  CB    . SER A 1 500 ? 15.336  17.75   21.629  1   39.04  ? 501  SER A CB    1 1 
ATOM   4045 O  OG    . SER A 1 500 ? 15.373  16.484  22.268  1   41.26  ? 501  SER A OG    1 1 
ATOM   4046 N  N     . GLY A 1 501 ? 14.956  18.468  25.002  1   36.46  ? 502  GLY A N     1 1 
ATOM   4047 C  CA    . GLY A 1 501 ? 14.086  18.22   26.137  1   35.73  ? 502  GLY A CA    1 1 
ATOM   4048 C  C     . GLY A 1 501 ? 14.755  17.491  27.276  1   35.06  ? 502  GLY A C     1 1 
ATOM   4049 O  O     . GLY A 1 501 ? 15.777  16.825  27.096  1   35.26  ? 502  GLY A O     1 1 
ATOM   4050 N  N     . LEU A 1 502 ? 14.193  17.635  28.468  1   34.11  ? 503  LEU A N     1 1 
ATOM   4051 C  CA    . LEU A 1 502 ? 14.74   17.006  29.658  1   33.32  ? 503  LEU A CA    1 1 
ATOM   4052 C  C     . LEU A 1 502 ? 13.695  16.101  30.278  1   33.72  ? 503  LEU A C     1 1 
ATOM   4053 O  O     . LEU A 1 502 ? 12.609  16.553  30.629  1   33.71  ? 503  LEU A O     1 1 
ATOM   4054 C  CB    . LEU A 1 502 ? 15.204  18.075  30.678  1   32.3   ? 503  LEU A CB    1 1 
ATOM   4055 C  CG    . LEU A 1 502 ? 15.561  17.569  32.074  1   32.33  ? 503  LEU A CG    1 1 
ATOM   4056 C  CD1   . LEU A 1 502 ? 16.749  16.636  32.028  1   32.42  ? 503  LEU A CD1   1 1 
ATOM   4057 C  CD2   . LEU A 1 502 ? 15.84   18.707  33.015  1   32.47  ? 503  LEU A CD2   1 1 
ATOM   4058 N  N     . SER A 1 503 ? 14.048  14.83   30.454  1   33.47  ? 504  SER A N     1 1 
ATOM   4059 C  CA    . SER A 1 503 ? 13.196  13.871  31.117  1   34.22  ? 504  SER A CA    1 1 
ATOM   4060 C  C     . SER A 1 503 ? 13.783  13.507  32.479  1   35.34  ? 504  SER A C     1 1 
ATOM   4061 O  O     . SER A 1 503 ? 14.981  13.278  32.605  1   35.82  ? 504  SER A O     1 1 
ATOM   4062 C  CB    . SER A 1 503 ? 13.042  12.612  30.27   1   35.11  ? 504  SER A CB    1 1 
ATOM   4063 O  OG    . SER A 1 503 ? 12.19   12.865  29.167  1   36.46  ? 504  SER A OG    1 1 
ATOM   4064 N  N     . ILE A 1 504 ? 12.937  13.454  33.497  1   35.86  ? 505  ILE A N     1 1 
ATOM   4065 C  CA    . ILE A 1 504 ? 13.294  13.054  34.855  1   36.85  ? 505  ILE A CA    1 1 
ATOM   4066 C  C     . ILE A 1 504 ? 12.345  11.908  35.204  1   37.89  ? 505  ILE A C     1 1 
ATOM   4067 O  O     . ILE A 1 504 ? 11.13   12.074  35.05   1   37.78  ? 505  ILE A O     1 1 
ATOM   4068 C  CB    . ILE A 1 504 ? 13.08   14.21   35.872  1   37.32  ? 505  ILE A CB    1 1 
ATOM   4069 C  CG1   . ILE A 1 504 ? 13.788  15.503  35.458  1   38.39  ? 505  ILE A CG1   1 1 
ATOM   4070 C  CG2   . ILE A 1 504 ? 13.467  13.773  37.275  1   37.83  ? 505  ILE A CG2   1 1 
ATOM   4071 C  CD1   . ILE A 1 504 ? 15.198  15.433  35.375  1   39.82  ? 505  ILE A CD1   1 1 
ATOM   4072 N  N     . ILE A 1 505 ? 12.867  10.769  35.676  1   38.48  ? 506  ILE A N     1 1 
ATOM   4073 C  CA    . ILE A 1 505 ? 11.992  9.667   36.065  1   40.06  ? 506  ILE A CA    1 1 
ATOM   4074 C  C     . ILE A 1 505 ? 11.991  9.459   37.579  1   41.9   ? 506  ILE A C     1 1 
ATOM   4075 O  O     . ILE A 1 505 ? 12.905  9.9     38.275  1   41.7   ? 506  ILE A O     1 1 
ATOM   4076 C  CB    . ILE A 1 505 ? 12.306  8.353   35.309  1   40.66  ? 506  ILE A CB    1 1 
ATOM   4077 C  CG1   . ILE A 1 505 ? 13.68   7.811   35.696  1   41.77  ? 506  ILE A CG1   1 1 
ATOM   4078 C  CG2   . ILE A 1 505 ? 12.141  8.502   33.809  1   40.93  ? 506  ILE A CG2   1 1 
ATOM   4079 C  CD1   . ILE A 1 505 ? 13.817  6.331   35.516  1   43.48  ? 506  ILE A CD1   1 1 
ATOM   4080 N  N     . ASP A 1 506 ? 10.938  8.819   38.091  1   43.51  ? 507  ASP A N     1 1 
ATOM   4081 C  CA    . ASP A 1 506 ? 10.848  8.431   39.49   1   45.83  ? 507  ASP A CA    1 1 
ATOM   4082 C  C     . ASP A 1 506 ? 10.365  6.959   39.541  1   47.55  ? 507  ASP A C     1 1 
ATOM   4083 O  O     . ASP A 1 506 ? 10.667  6.211   38.604  1   48.08  ? 507  ASP A O     1 1 
ATOM   4084 C  CB    . ASP A 1 506 ? 10.065  9.453   40.364  1   48.64  ? 507  ASP A CB    1 1 
ATOM   4085 C  CG    . ASP A 1 506 ? 8.576   9.569   40.11   1   54.99  ? 507  ASP A CG    1 1 
ATOM   4086 O  OD1   . ASP A 1 506 ? 8.052   8.785   39.303  1   55.82  ? 507  ASP A OD1   1 1 
ATOM   4087 O  OD2   . ASP A 1 506 ? 7.932   10.446  40.735  1   58.04  ? 507  ASP A OD2   1 1 
ATOM   4088 N  N     . ASN A 1 507 ? 9.673   6.519   40.605  1   48.31  ? 508  ASN A N     1 1 
ATOM   4089 C  CA    . ASN A 1 507 ? 9.202   5.139   40.679  1   49.43  ? 508  ASN A CA    1 1 
ATOM   4090 C  C     . ASN A 1 507 ? 7.949   4.864   39.821  1   49.26  ? 508  ASN A C     1 1 
ATOM   4091 O  O     . ASN A 1 507 ? 7.631   3.702   39.562  1   49.51  ? 508  ASN A O     1 1 
ATOM   4092 C  CB    . ASN A 1 507 ? 8.945   4.752   42.136  1   51.74  ? 508  ASN A CB    1 1 
ATOM   4093 C  CG    . ASN A 1 507 ? 9.956   3.783   42.697  1   56.47  ? 508  ASN A CG    1 1 
ATOM   4094 O  OD1   . ASN A 1 507 ? 9.605   2.858   43.442  1   58.31  ? 508  ASN A OD1   1 1 
ATOM   4095 N  ND2   . ASN A 1 507 ? 11.23   3.966   42.353  1   57.32  ? 508  ASN A ND2   1 1 
ATOM   4096 N  N     . VAL A 1 508 ? 7.24    5.914   39.389  1   48.65  ? 509  VAL A N     1 1 
ATOM   4097 C  CA    . VAL A 1 508 ? 5.989   5.735   38.656  1   48.22  ? 509  VAL A CA    1 1 
ATOM   4098 C  C     . VAL A 1 508 ? 5.882   6.578   37.36   1   47.19  ? 509  VAL A C     1 1 
ATOM   4099 O  O     . VAL A 1 508 ? 5.287   6.115   36.388  1   47.18  ? 509  VAL A O     1 1 
ATOM   4100 C  CB    . VAL A 1 508 ? 4.797   5.992   39.623  1   49.02  ? 509  VAL A CB    1 1 
ATOM   4101 C  CG1   . VAL A 1 508 ? 4.914   7.357   40.308  1   49.77  ? 509  VAL A CG1   1 1 
ATOM   4102 C  CG2   . VAL A 1 508 ? 3.452   5.851   38.918  1   49.46  ? 509  VAL A CG2   1 1 
ATOM   4103 N  N     . HIS A 1 509 ? 6.463   7.787   37.328  1   46.1   ? 510  HIS A N     1 1 
ATOM   4104 C  CA    . HIS A 1 509 ? 6.335   8.667   36.166  1   45.64  ? 510  HIS A CA    1 1 
ATOM   4105 C  C     . HIS A 1 509 ? 7.626   9.113   35.482  1   43.23  ? 510  HIS A C     1 1 
ATOM   4106 O  O     . HIS A 1 509 ? 8.703   9.079   36.066  1   43.17  ? 510  HIS A O     1 1 
ATOM   4107 C  CB    . HIS A 1 509 ? 5.564   9.947   36.553  1   47.97  ? 510  HIS A CB    1 1 
ATOM   4108 C  CG    . HIS A 1 509 ? 4.175   9.726   37.049  1   52.97  ? 510  HIS A CG    1 1 
ATOM   4109 N  ND1   . HIS A 1 509 ? 3.872   9.812   38.396  1   55.45  ? 510  HIS A ND1   1 1 
ATOM   4110 C  CD2   . HIS A 1 509 ? 3.036   9.487   36.355  1   54.92  ? 510  HIS A CD2   1 1 
ATOM   4111 C  CE1   . HIS A 1 509 ? 2.568   9.604   38.481  1   56.49  ? 510  HIS A CE1   1 1 
ATOM   4112 N  NE2   . HIS A 1 509 ? 2.022   9.402   37.277  1   56.44  ? 510  HIS A NE2   1 1 
ATOM   4113 N  N     . GLU A 1 510 ? 7.479   9.597   34.243  1   41.1   ? 511  GLU A N     1 1 
ATOM   4114 C  CA    . GLU A 1 510 ? 8.521   10.248  33.486  1   39.66  ? 511  GLU A CA    1 1 
ATOM   4115 C  C     . GLU A 1 510 ? 7.977   11.635  33.233  1   38.54  ? 511  GLU A C     1 1 
ATOM   4116 O  O     . GLU A 1 510 ? 6.944   11.78   32.592  1   38.67  ? 511  GLU A O     1 1 
ATOM   4117 C  CB    . GLU A 1 510 ? 8.782   9.568   32.143  1   41.05  ? 511  GLU A CB    1 1 
ATOM   4118 C  CG    . GLU A 1 510 ? 9.826   10.316  31.324  1   42.69  ? 511  GLU A CG    1 1 
ATOM   4119 C  CD    . GLU A 1 510 ? 10.029  9.803   29.915  1   45.59  ? 511  GLU A CD    1 1 
ATOM   4120 O  OE1   . GLU A 1 510 ? 9.562   8.678   29.625  1   46.69  ? 511  GLU A OE1   1 1 
ATOM   4121 O  OE2   . GLU A 1 510 ? 10.66   10.516  29.1    1   45.22  ? 511  GLU A OE2   1 1 
ATOM   4122 N  N     . PHE A 1 511 ? 8.641   12.649  33.773  1   37.36  ? 512  PHE A N     1 1 
ATOM   4123 C  CA    . PHE A 1 511 ? 8.28    14.051  33.618  1   36.64  ? 512  PHE A CA    1 1 
ATOM   4124 C  C     . PHE A 1 511 ? 9.185   14.63   32.551  1   35.21  ? 512  PHE A C     1 1 
ATOM   4125 O  O     . PHE A 1 511 ? 10.382  14.345  32.555  1   35.05  ? 512  PHE A O     1 1 
ATOM   4126 C  CB    . PHE A 1 511 ? 8.496   14.798  34.937  1   36.99  ? 512  PHE A CB    1 1 
ATOM   4127 C  CG    . PHE A 1 511 ? 7.762   14.177  36.097  1   38.22  ? 512  PHE A CG    1 1 
ATOM   4128 C  CD1   . PHE A 1 511 ? 6.447   14.508  36.361  1   39.44  ? 512  PHE A CD1   1 1 
ATOM   4129 C  CD2   . PHE A 1 511 ? 8.391   13.27   36.93   1   39.35  ? 512  PHE A CD2   1 1 
ATOM   4130 C  CE1   . PHE A 1 511 ? 5.768   13.931  37.428  1   40.24  ? 512  PHE A CE1   1 1 
ATOM   4131 C  CE2   . PHE A 1 511 ? 7.7     12.67   37.978  1   40.33  ? 512  PHE A CE2   1 1 
ATOM   4132 C  CZ    . PHE A 1 511 ? 6.401   13.017  38.229  1   40.15  ? 512  PHE A CZ    1 1 
ATOM   4133 N  N     . ARG A 1 512 ? 8.638   15.448  31.648  1   33.8   ? 513  ARG A N     1 1 
ATOM   4134 C  CA    . ARG A 1 512 ? 9.434   15.995  30.558  1   32.99  ? 513  ARG A CA    1 1 
ATOM   4135 C  C     . ARG A 1 512 ? 9.187   17.467  30.29   1   32.26  ? 513  ARG A C     1 1 
ATOM   4136 O  O     . ARG A 1 512 ? 8.036   17.895  30.179  1   32.03  ? 513  ARG A O     1 1 
ATOM   4137 C  CB    . ARG A 1 512 ? 9.232   15.152  29.284  1   33.51  ? 513  ARG A CB    1 1 
ATOM   4138 C  CG    . ARG A 1 512 ? 10.123  15.542  28.117  1   35.04  ? 513  ARG A CG    1 1 
ATOM   4139 C  CD    . ARG A 1 512 ? 10.226  14.39   27.129  1   37.09  ? 513  ARG A CD    1 1 
ATOM   4140 N  NE    . ARG A 1 512 ? 10.997  14.767  25.944  1   38.58  ? 513  ARG A NE    1 1 
ATOM   4141 C  CZ    . ARG A 1 512 ? 12.32   14.675  25.843  1   39.44  ? 513  ARG A CZ    1 1 
ATOM   4142 N  NH1   . ARG A 1 512 ? 13.04   14.213  26.859  1   39.28  ? 513  ARG A NH1   1 1 
ATOM   4143 N  NH2   . ARG A 1 512 ? 12.934  15.049  24.728  1   38.31  ? 513  ARG A NH2   1 1 
ATOM   4144 N  N     . TRP A 1 513 ? 10.28   18.242  30.191  1   31.48  ? 514  TRP A N     1 1 
ATOM   4145 C  CA    . TRP A 1 513 ? 10.231  19.656  29.842  1   31.5   ? 514  TRP A CA    1 1 
ATOM   4146 C  C     . TRP A 1 513 ? 10.613  19.715  28.374  1   30.84  ? 514  TRP A C     1 1 
ATOM   4147 O  O     . TRP A 1 513 ? 11.684  19.249  28.001  1   31.52  ? 514  TRP A O     1 1 
ATOM   4148 C  CB    . TRP A 1 513 ? 11.256  20.499  30.657  1   32.01  ? 514  TRP A CB    1 1 
ATOM   4149 C  CG    . TRP A 1 513 ? 10.854  20.81   32.069  1   33.12  ? 514  TRP A CG    1 1 
ATOM   4150 C  CD1   . TRP A 1 513 ? 10.264  21.952  32.527  1   33.98  ? 514  TRP A CD1   1 1 
ATOM   4151 C  CD2   . TRP A 1 513 ? 11.037  19.967  33.211  1   33.62  ? 514  TRP A CD2   1 1 
ATOM   4152 N  NE1   . TRP A 1 513 ? 10.059  21.867  33.884  1   34.38  ? 514  TRP A NE1   1 1 
ATOM   4153 C  CE2   . TRP A 1 513 ? 10.514  20.652  34.328  1   34.48  ? 514  TRP A CE2   1 1 
ATOM   4154 C  CE3   . TRP A 1 513 ? 11.564  18.688  33.393  1   34.78  ? 514  TRP A CE3   1 1 
ATOM   4155 C  CZ2   . TRP A 1 513 ? 10.515  20.1    35.609  1   35.52  ? 514  TRP A CZ2   1 1 
ATOM   4156 C  CZ3   . TRP A 1 513 ? 11.562  18.144  34.66   1   36.11  ? 514  TRP A CZ3   1 1 
ATOM   4157 C  CH2   . TRP A 1 513 ? 11.037  18.844  35.75   1   36.15  ? 514  TRP A CH2   1 1 
ATOM   4158 N  N     . LEU A 1 514 ? 9.767   20.281  27.549  1   29.94  ? 515  LEU A N     1 1 
ATOM   4159 C  CA    . LEU A 1 514 ? 10.025  20.453  26.123  1   29.89  ? 515  LEU A CA    1 1 
ATOM   4160 C  C     . LEU A 1 514 ? 10.386  21.917  25.846  1   29.63  ? 515  LEU A C     1 1 
ATOM   4161 O  O     . LEU A 1 514 ? 10.22   22.765  26.733  1   30     ? 515  LEU A O     1 1 
ATOM   4162 C  CB    . LEU A 1 514 ? 8.737   20.09   25.34   1   30.18  ? 515  LEU A CB    1 1 
ATOM   4163 C  CG    . LEU A 1 514 ? 8.188   18.696  25.583  1   31.22  ? 515  LEU A CG    1 1 
ATOM   4164 C  CD1   . LEU A 1 514 ? 6.796   18.542  24.973  1   31.7   ? 515  LEU A CD1   1 1 
ATOM   4165 C  CD2   . LEU A 1 514 ? 9.127   17.641  25.071  1   31.4   ? 515  LEU A CD2   1 1 
ATOM   4166 N  N     . SER A 1 515 ? 10.787  22.241  24.601  1   29.01  ? 516  SER A N     1 1 
ATOM   4167 C  CA    . SER A 1 515 ? 11.076  23.613  24.177  1   29.34  ? 516  SER A CA    1 1 
ATOM   4168 C  C     . SER A 1 515 ? 12.065  24.322  25.105  1   30.26  ? 516  SER A C     1 1 
ATOM   4169 O  O     . SER A 1 515 ? 11.768  25.386  25.668  1   30.31  ? 516  SER A O     1 1 
ATOM   4170 C  CB    . SER A 1 515 ? 9.79    24.428  24.028  1   30.17  ? 516  SER A CB    1 1 
ATOM   4171 O  OG    . SER A 1 515 ? 8.825   23.799  23.201  1   31.34  ? 516  SER A OG    1 1 
ATOM   4172 N  N     . LEU A 1 516 ? 13.236  23.711  25.285  1   30.7   ? 517  LEU A N     1 1 
ATOM   4173 C  CA    . LEU A 1 516 ? 14.277  24.27   26.129  1   31.35  ? 517  LEU A CA    1 1 
ATOM   4174 C  C     . LEU A 1 516 ? 14.988  25.394  25.387  1   32.3   ? 517  LEU A C     1 1 
ATOM   4175 O  O     . LEU A 1 516 ? 15.551  25.167  24.314  1   32.59  ? 517  LEU A O     1 1 
ATOM   4176 C  CB    . LEU A 1 516 ? 15.317  23.19   26.498  1   31.69  ? 517  LEU A CB    1 1 
ATOM   4177 C  CG    . LEU A 1 516 ? 14.821  21.899  27.161  1   33.36  ? 517  LEU A CG    1 1 
ATOM   4178 C  CD1   . LEU A 1 516 ? 16.013  21.025  27.587  1   33.09  ? 517  LEU A CD1   1 1 
ATOM   4179 C  CD2   . LEU A 1 516 ? 13.891  22.198  28.366  1   34.1   ? 517  LEU A CD2   1 1 
ATOM   4180 N  N     . PRO A 1 517 ? 15.02   26.606  25.961  1   32.54  ? 518  PRO A N     1 1 
ATOM   4181 C  CA    . PRO A 1 517 ? 15.753  27.699  25.302  1   32.71  ? 518  PRO A CA    1 1 
ATOM   4182 C  C     . PRO A 1 517 ? 17.269  27.52   25.421  1   33.37  ? 518  PRO A C     1 1 
ATOM   4183 O  O     . PRO A 1 517 ? 17.737  26.821  26.326  1   33.32  ? 518  PRO A O     1 1 
ATOM   4184 C  CB    . PRO A 1 517 ? 15.274  28.947  26.056  1   33.04  ? 518  PRO A CB    1 1 
ATOM   4185 C  CG    . PRO A 1 517 ? 14.871  28.452  27.403  1   33.07  ? 518  PRO A CG    1 1 
ATOM   4186 C  CD    . PRO A 1 517 ? 14.391  27.039  27.227  1   31.84  ? 518  PRO A CD    1 1 
ATOM   4187 N  N     . ARG A 1 518 ? 18.046  28.158  24.524  1   33.76  ? 519  ARG A N     1 1 
ATOM   4188 C  CA    . ARG A 1 518 ? 19.515  28.084  24.553  1   34.57  ? 519  ARG A CA    1 1 
ATOM   4189 C  C     . ARG A 1 518 ? 20.053  28.643  25.886  1   34.88  ? 519  ARG A C     1 1 
ATOM   4190 O  O     . ARG A 1 518 ? 20.991  28.094  26.452  1   34.36  ? 519  ARG A O     1 1 
ATOM   4191 C  CB    . ARG A 1 518 ? 20.119  28.831  23.351  1   36.47  ? 519  ARG A CB    1 1 
ATOM   4192 C  CG    . ARG A 1 518 ? 21.61   28.614  23.149  1   41.26  ? 519  ARG A CG    1 1 
ATOM   4193 C  CD    . ARG A 1 518 ? 22.239  29.647  22.204  1   46.49  ? 519  ARG A CD    1 1 
ATOM   4194 N  NE    . ARG A 1 518 ? 21.963  31.019  22.636  1   50.66  ? 519  ARG A NE    1 1 
ATOM   4195 C  CZ    . ARG A 1 518 ? 22.76   31.735  23.424  1   53.09  ? 519  ARG A CZ    1 1 
ATOM   4196 N  NH1   . ARG A 1 518 ? 23.914  31.232  23.848  1   51.81  ? 519  ARG A NH1   1 1 
ATOM   4197 N  NH2   . ARG A 1 518 ? 22.406  32.958  23.798  1   53.69  ? 519  ARG A NH2   1 1 
ATOM   4198 N  N     . VAL A 1 519 ? 19.409  29.686  26.425  1   35.51  ? 520  VAL A N     1 1 
ATOM   4199 C  CA    . VAL A 1 519 ? 19.802  30.264  27.713  1   37.12  ? 520  VAL A CA    1 1 
ATOM   4200 C  C     . VAL A 1 519 ? 18.572  30.652  28.545  1   39.1   ? 520  VAL A C     1 1 
ATOM   4201 O  O     . VAL A 1 519 ? 17.486  30.845  28.005  1   39.72  ? 520  VAL A O     1 1 
ATOM   4202 C  CB    . VAL A 1 519 ? 20.72   31.516  27.541  1   37.43  ? 520  VAL A CB    1 1 
ATOM   4203 C  CG1   . VAL A 1 519 ? 22.074  31.159  26.968  1   38.15  ? 520  VAL A CG1   1 1 
ATOM   4204 C  CG2   . VAL A 1 519 ? 20.042  32.593  26.707  1   37.78  ? 520  VAL A CG2   1 1 
ATOM   4205 N  N     . SER A 1 520 ? 18.76   30.794  29.859  1   39.98  ? 521  SER A N     1 1 
ATOM   4206 C  CA    . SER A 1 520 ? 17.77   31.335  30.79   1   41.33  ? 521  SER A CA    1 1 
ATOM   4207 C  C     . SER A 1 520 ? 18.442  32.592  31.469  1   42.22  ? 521  SER A C     1 1 
ATOM   4208 O  O     . SER A 1 520 ? 19.544  32.981  31.057  1   41.94  ? 521  SER A O     1 1 
ATOM   4209 C  CB    . SER A 1 520 ? 17.302  30.273  31.791  1   42.88  ? 521  SER A CB    1 1 
ATOM   4210 O  OG    . SER A 1 520 ? 18.259  30.028  32.812  1   45.09  ? 521  SER A OG    1 1 
ATOM   4211 N  N     . GLU A 1 521 ? 17.787  33.251  32.45   1   43     ? 522  GLU A N     1 1 
ATOM   4212 C  CA    . GLU A 1 521 ? 18.363  34.464  33.07   1   44.05  ? 522  GLU A CA    1 1 
ATOM   4213 C  C     . GLU A 1 521 ? 19.756  34.238  33.653  1   43.71  ? 522  GLU A C     1 1 
ATOM   4214 O  O     . GLU A 1 521 ? 20.678  35.007  33.382  1   44.15  ? 522  GLU A O     1 1 
ATOM   4215 C  CB    . GLU A 1 521 ? 17.408  35.071  34.115  1   47.72  ? 522  GLU A CB    1 1 
ATOM   4216 C  CG    . GLU A 1 521 ? 17.921  36.349  34.761  1   55.35  ? 522  GLU A CG    1 1 
ATOM   4217 C  CD    . GLU A 1 521 ? 17.751  37.616  33.941  1   64.43  ? 522  GLU A CD    1 1 
ATOM   4218 O  OE1   . GLU A 1 521 ? 17.165  37.538  32.837  1   66.21  ? 522  GLU A OE1   1 1 
ATOM   4219 O  OE2   . GLU A 1 521 ? 18.206  38.689  34.405  1   67.37  ? 522  GLU A OE2   1 1 
ATOM   4220 N  N     . ASN A 1 522 ? 19.924  33.159  34.403  1   43.07  ? 523  ASN A N     1 1 
ATOM   4221 C  CA    . ASN A 1 522 ? 21.222  32.813  34.986  1   42.6   ? 523  ASN A CA    1 1 
ATOM   4222 C  C     . ASN A 1 522 ? 21.775  31.453  34.528  1   40.43  ? 523  ASN A C     1 1 
ATOM   4223 O  O     . ASN A 1 522 ? 22.798  31.015  35.046  1   40.21  ? 523  ASN A O     1 1 
ATOM   4224 C  CB    . ASN A 1 522 ? 21.136  32.833  36.511  1   45     ? 523  ASN A CB    1 1 
ATOM   4225 C  CG    . ASN A 1 522 ? 20.975  34.215  37.078  1   50.24  ? 523  ASN A CG    1 1 
ATOM   4226 O  OD1   . ASN A 1 522 ? 19.853  34.706  37.276  1   51.57  ? 523  ASN A OD1   1 1 
ATOM   4227 N  ND2   . ASN A 1 522 ? 22.109  34.872  37.347  1   51.49  ? 523  ASN A ND2   1 1 
ATOM   4228 N  N     . GLY A 1 523 ? 21.1    30.788  33.595  1   38.8   ? 524  GLY A N     1 1 
ATOM   4229 C  CA    . GLY A 1 523 ? 21.531  29.47   33.147  1   37.11  ? 524  GLY A CA    1 1 
ATOM   4230 C  C     . GLY A 1 523 ? 21.817  29.294  31.67   1   34.62  ? 524  GLY A C     1 1 
ATOM   4231 O  O     . GLY A 1 523 ? 21.405  30.096  30.827  1   35     ? 524  GLY A O     1 1 
ATOM   4232 N  N     . LYS A 1 524 ? 22.528  28.222  31.359  1   31.8   ? 525  LYS A N     1 1 
ATOM   4233 C  CA    . LYS A 1 524 ? 22.82   27.833  29.991  1   30.37  ? 525  LYS A CA    1 1 
ATOM   4234 C  C     . LYS A 1 524 ? 22.363  26.382  29.789  1   27.6   ? 525  LYS A C     1 1 
ATOM   4235 O  O     . LYS A 1 524 ? 22.563  25.536  30.665  1   27.06  ? 525  LYS A O     1 1 
ATOM   4236 C  CB    . LYS A 1 524 ? 24.305  28      29.668  1   33.15  ? 525  LYS A CB    1 1 
ATOM   4237 C  CG    . LYS A 1 524 ? 24.669  29.452  29.429  1   39.9   ? 525  LYS A CG    1 1 
ATOM   4238 C  CD    . LYS A 1 524 ? 25.841  29.572  28.482  1   46.92  ? 525  LYS A CD    1 1 
ATOM   4239 C  CE    . LYS A 1 524 ? 25.937  30.956  27.91   1   51.65  ? 525  LYS A CE    1 1 
ATOM   4240 N  NZ    . LYS A 1 524 ? 26.076  31.97   28.982  1   54.78  ? 525  LYS A NZ    1 1 
ATOM   4241 N  N     . ARG A 1 525 ? 21.732  26.105  28.653  1   25.85  ? 526  ARG A N     1 1 
ATOM   4242 C  CA    . ARG A 1 525 ? 21.232  24.763  28.361  1   25.06  ? 526  ARG A CA    1 1 
ATOM   4243 C  C     . ARG A 1 525 ? 22.375  23.775  28.247  1   24.85  ? 526  ARG A C     1 1 
ATOM   4244 O  O     . ARG A 1 525 ? 23.262  23.963  27.416  1   25.06  ? 526  ARG A O     1 1 
ATOM   4245 C  CB    . ARG A 1 525 ? 20.418  24.781  27.069  1   24.82  ? 526  ARG A CB    1 1 
ATOM   4246 C  CG    . ARG A 1 525 ? 19.754  23.466  26.758  1   24.94  ? 526  ARG A CG    1 1 
ATOM   4247 C  CD    . ARG A 1 525 ? 18.97   23.542  25.47   1   26.74  ? 526  ARG A CD    1 1 
ATOM   4248 N  NE    . ARG A 1 525 ? 19.832  23.852  24.33   1   29.09  ? 526  ARG A NE    1 1 
ATOM   4249 C  CZ    . ARG A 1 525 ? 19.426  24.468  23.225  1   31.15  ? 526  ARG A CZ    1 1 
ATOM   4250 N  NH1   . ARG A 1 525 ? 18.159  24.832  23.087  1   29.99  ? 526  ARG A NH1   1 1 
ATOM   4251 N  NH2   . ARG A 1 525 ? 20.284  24.707  22.237  1   31.42  ? 526  ARG A NH2   1 1 
ATOM   4252 N  N     . PRO A 1 526 ? 22.406  22.731  29.102  1   24.75  ? 527  PRO A N     1 1 
ATOM   4253 C  CA    . PRO A 1 526 ? 23.493  21.734  28.986  1   24.81  ? 527  PRO A CA    1 1 
ATOM   4254 C  C     . PRO A 1 526 ? 23.405  20.928  27.687  1   24.7   ? 527  PRO A C     1 1 
ATOM   4255 O  O     . PRO A 1 526 ? 22.317  20.801  27.11   1   24.59  ? 527  PRO A O     1 1 
ATOM   4256 C  CB    . PRO A 1 526 ? 23.283  20.822  30.214  1   25.41  ? 527  PRO A CB    1 1 
ATOM   4257 C  CG    . PRO A 1 526 ? 22.184  21.471  31.057  1   25.39  ? 527  PRO A CG    1 1 
ATOM   4258 C  CD    . PRO A 1 526 ? 21.413  22.353  30.132  1   24.05  ? 527  PRO A CD    1 1 
ATOM   4259 N  N     . ASP A 1 527 ? 24.538  20.392  27.218  1   24.72  ? 528  ASP A N     1 1 
ATOM   4260 C  CA    . ASP A 1 527 ? 24.53   19.554  26.019  1   25.46  ? 528  ASP A CA    1 1 
ATOM   4261 C  C     . ASP A 1 527 ? 23.868  18.218  26.356  1   25.94  ? 528  ASP A C     1 1 
ATOM   4262 O  O     . ASP A 1 527 ? 23.148  17.658  25.528  1   25.95  ? 528  ASP A O     1 1 
ATOM   4263 C  CB    . ASP A 1 527 ? 25.95   19.318  25.498  1   28.78  ? 528  ASP A CB    1 1 
ATOM   4264 C  CG    . ASP A 1 527 ? 26.669  20.545  24.981  1   34.41  ? 528  ASP A CG    1 1 
ATOM   4265 O  OD1   . ASP A 1 527 ? 26.01   21.538  24.714  1   35.05  ? 528  ASP A OD1   1 1 
ATOM   4266 O  OD2   . ASP A 1 527 ? 27.893  20.483  24.815  1   39.98  ? 528  ASP A OD2   1 1 
ATOM   4267 N  N     . HIS A 1 528 ? 24.095  17.701  27.576  1   26.08  ? 529  HIS A N     1 1 
ATOM   4268 C  CA    . HIS A 1 528 ? 23.503  16.445  28.028  1   26.12  ? 529  HIS A CA    1 1 
ATOM   4269 C  C     . HIS A 1 528 ? 23.191  16.52   29.504  1   25.65  ? 529  HIS A C     1 1 
ATOM   4270 O  O     . HIS A 1 528 ? 23.945  17.114  30.266  1   25.95  ? 529  HIS A O     1 1 
ATOM   4271 C  CB    . HIS A 1 528 ? 24.482  15.28   27.828  1   27.07  ? 529  HIS A CB    1 1 
ATOM   4272 C  CG    . HIS A 1 528 ? 24.906  15.068  26.411  1   29.24  ? 529  HIS A CG    1 1 
ATOM   4273 N  ND1   . HIS A 1 528 ? 24.047  14.513  25.477  1   30.64  ? 529  HIS A ND1   1 1 
ATOM   4274 C  CD2   . HIS A 1 528 ? 26.079  15.372  25.807  1   29.8   ? 529  HIS A CD2   1 1 
ATOM   4275 C  CE1   . HIS A 1 528 ? 24.722  14.503  24.338  1   31.33  ? 529  HIS A CE1   1 1 
ATOM   4276 N  NE2   . HIS A 1 528 ? 25.953  15.003  24.49   1   30.78  ? 529  HIS A NE2   1 1 
ATOM   4277 N  N     . VAL A 1 529 ? 22.096  15.911  29.916  1   24.62  ? 530  VAL A N     1 1 
ATOM   4278 C  CA    . VAL A 1 529 ? 21.753  15.787  31.323  1   24.99  ? 530  VAL A CA    1 1 
ATOM   4279 C  C     . VAL A 1 529 ? 21.621  14.275  31.578  1   25.26  ? 530  VAL A C     1 1 
ATOM   4280 O  O     . VAL A 1 529 ? 20.914  13.581  30.844  1   24.54  ? 530  VAL A O     1 1 
ATOM   4281 C  CB    . VAL A 1 529 ? 20.49   16.572  31.752  1   25.89  ? 530  VAL A CB    1 1 
ATOM   4282 C  CG1   . VAL A 1 529 ? 20.233  16.42   33.251  1   26.85  ? 530  VAL A CG1   1 1 
ATOM   4283 C  CG2   . VAL A 1 529 ? 20.599  18.045  31.373  1   25.51  ? 530  VAL A CG2   1 1 
ATOM   4284 N  N     . ILE A 1 530 ? 22.38   13.755  32.543  1   25.31  ? 531  ILE A N     1 1 
ATOM   4285 C  CA    . ILE A 1 530 ? 22.369  12.331  32.84   1   26.29  ? 531  ILE A CA    1 1 
ATOM   4286 C  C     . ILE A 1 530 ? 21.747  12.091  34.205  1   27.67  ? 531  ILE A C     1 1 
ATOM   4287 O  O     . ILE A 1 530 ? 22.176  12.715  35.167  1   28.01  ? 531  ILE A O     1 1 
ATOM   4288 C  CB    . ILE A 1 530 ? 23.808  11.746  32.784  1   26.05  ? 531  ILE A CB    1 1 
ATOM   4289 C  CG1   . ILE A 1 530 ? 24.578  12.192  31.52   1   26.83  ? 531  ILE A CG1   1 1 
ATOM   4290 C  CG2   . ILE A 1 530 ? 23.786  10.249  32.926  1   25.79  ? 531  ILE A CG2   1 1 
ATOM   4291 C  CD1   . ILE A 1 530 ? 23.906  11.781  30.215  1   28.02  ? 531  ILE A CD1   1 1 
ATOM   4292 N  N     . GLN A 1 531 ? 20.759  11.197  34.303  1   28.18  ? 532  GLN A N     1 1 
ATOM   4293 C  CA    . GLN A 1 531 ? 20.166  10.882  35.596  1   29.52  ? 532  GLN A CA    1 1 
ATOM   4294 C  C     . GLN A 1 531 ? 20.715  9.567   36.119  1   30.97  ? 532  GLN A C     1 1 
ATOM   4295 O  O     . GLN A 1 531 ? 20.637  8.554   35.426  1   31.37  ? 532  GLN A O     1 1 
ATOM   4296 C  CB    . GLN A 1 531 ? 18.619  10.846  35.556  1   29.87  ? 532  GLN A CB    1 1 
ATOM   4297 C  CG    . GLN A 1 531 ? 18.006  10.55   36.929  1   31.84  ? 532  GLN A CG    1 1 
ATOM   4298 C  CD    . GLN A 1 531 ? 16.482  10.631  36.98   1   35.63  ? 532  GLN A CD    1 1 
ATOM   4299 O  OE1   . GLN A 1 531 ? 15.798  10.736  35.954  1   37.99  ? 532  GLN A OE1   1 1 
ATOM   4300 N  NE2   . GLN A 1 531 ? 15.921  10.564  38.185  1   34.14  ? 532  GLN A NE2   1 1 
ATOM   4301 N  N     . ILE A 1 532 ? 21.246  9.563   37.345  1   31.91  ? 533  ILE A N     1 1 
ATOM   4302 C  CA    . ILE A 1 532 ? 21.742  8.328   37.954  1   33.8   ? 533  ILE A CA    1 1 
ATOM   4303 C  C     . ILE A 1 532 ? 20.98   8.076   39.264  1   36.46  ? 533  ILE A C     1 1 
ATOM   4304 O  O     . ILE A 1 532 ? 21.017  8.913   40.16   1   36.55  ? 533  ILE A O     1 1 
ATOM   4305 C  CB    . ILE A 1 532 ? 23.278  8.359   38.128  1   33.32  ? 533  ILE A CB    1 1 
ATOM   4306 C  CG1   . ILE A 1 532 ? 23.975  8.44    36.758  1   34.25  ? 533  ILE A CG1   1 1 
ATOM   4307 C  CG2   . ILE A 1 532 ? 23.762  7.153   38.893  1   32.91  ? 533  ILE A CG2   1 1 
ATOM   4308 C  CD1   . ILE A 1 532 ? 25.38   8.917   36.8    1   35.16  ? 533  ILE A CD1   1 1 
ATOM   4309 N  N     . LEU A 1 533 ? 20.264  6.95    39.363  1   38.4   ? 534  LEU A N     1 1 
ATOM   4310 C  CA    . LEU A 1 533 ? 19.442  6.669   40.542  1   40.82  ? 534  LEU A CA    1 1 
ATOM   4311 C  C     . LEU A 1 533 ? 20.035  5.672   41.546  1   42.85  ? 534  LEU A C     1 1 
ATOM   4312 O  O     . LEU A 1 533 ? 19.506  5.548   42.655  1   43.18  ? 534  LEU A O     1 1 
ATOM   4313 C  CB    . LEU A 1 533 ? 18.066  6.163   40.096  1   41.45  ? 534  LEU A CB    1 1 
ATOM   4314 C  CG    . LEU A 1 533 ? 17.24   7.144   39.3    1   43.9   ? 534  LEU A CG    1 1 
ATOM   4315 C  CD1   . LEU A 1 533 ? 17.045  6.662   37.897  1   44.53  ? 534  LEU A CD1   1 1 
ATOM   4316 C  CD2   . LEU A 1 533 ? 15.902  7.382   39.96   1   45.27  ? 534  LEU A CD2   1 1 
ATOM   4317 N  N     . ASP A 1 534 ? 21.089  4.936   41.164  1   43.78  ? 535  ASP A N     1 1 
ATOM   4318 C  CA    . ASP A 1 534 ? 21.645  3.907   42.04   1   44.97  ? 535  ASP A CA    1 1 
ATOM   4319 C  C     . ASP A 1 534 ? 22.991  4.285   42.649  1   45.91  ? 535  ASP A C     1 1 
ATOM   4320 O  O     . ASP A 1 534 ? 23.854  3.409   42.841  1   46.32  ? 535  ASP A O     1 1 
ATOM   4321 C  CB    . ASP A 1 534 ? 21.756  2.577   41.277  1   46.99  ? 535  ASP A CB    1 1 
ATOM   4322 N  N     . LEU A 1 535 ? 23.175  5.569   42.973  1   45.73  ? 536  LEU A N     1 1 
ATOM   4323 C  CA    . LEU A 1 535 ? 24.448  6.025   43.529  1   45.96  ? 536  LEU A CA    1 1 
ATOM   4324 C  C     . LEU A 1 535 ? 24.244  6.672   44.899  1   46.92  ? 536  LEU A C     1 1 
ATOM   4325 O  O     . LEU A 1 535 ? 24.771  6.173   45.892  1   47.28  ? 536  LEU A O     1 1 
ATOM   4326 C  CB    . LEU A 1 535 ? 25.16   6.962   42.528  1   45.41  ? 536  LEU A CB    1 1 
ATOM   4327 C  CG    . LEU A 1 535 ? 26.419  7.657   42.99   1   46.12  ? 536  LEU A CG    1 1 
ATOM   4328 C  CD1   . LEU A 1 535 ? 27.46   6.655   43.484  1   46.19  ? 536  LEU A CD1   1 1 
ATOM   4329 C  CD2   . LEU A 1 535 ? 26.99   8.5     41.87   1   46.77  ? 536  LEU A CD2   1 1 
ATOM   4330 N  N     . PHE A 1 536 ? 23.448  7.742   44.963  1   47.1   ? 537  PHE A N     1 1 
ATOM   4331 C  CA    . PHE A 1 536 ? 23.15   8.42    46.217  1   47.82  ? 537  PHE A CA    1 1 
ATOM   4332 C  C     . PHE A 1 536 ? 21.716  8.076   46.686  1   48.85  ? 537  PHE A C     1 1 
ATOM   4333 O  O     . PHE A 1 536 ? 20.95   7.453   45.948  1   49.39  ? 537  PHE A O     1 1 
ATOM   4334 C  CB    . PHE A 1 536 ? 23.301  9.939   46.029  1   47.46  ? 537  PHE A CB    1 1 
ATOM   4335 C  CG    . PHE A 1 536 ? 24.663  10.38   45.55   1   48.04  ? 537  PHE A CG    1 1 
ATOM   4336 C  CD1   . PHE A 1 536 ? 25.783  10.212  46.346  1   48.83  ? 537  PHE A CD1   1 1 
ATOM   4337 C  CD2   . PHE A 1 536 ? 24.816  10.998  44.322  1   48.66  ? 537  PHE A CD2   1 1 
ATOM   4338 C  CE1   . PHE A 1 536 ? 27.034  10.631  45.913  1   49.41  ? 537  PHE A CE1   1 1 
ATOM   4339 C  CE2   . PHE A 1 536 ? 26.069  11.423  43.894  1   49.22  ? 537  PHE A CE2   1 1 
ATOM   4340 C  CZ    . PHE A 1 536 ? 27.168  11.236  44.691  1   49.14  ? 537  PHE A CZ    1 1 
ATOM   4341 N  N     . GLU A 1 537 ? 21.347  8.487   47.909  1   48.83  ? 538  GLU A N     1 1 
ATOM   4342 C  CA    . GLU A 1 537 ? 19.992  8.293   48.423  1   49.28  ? 538  GLU A CA    1 1 
ATOM   4343 C  C     . GLU A 1 537 ? 19.002  9.082   47.531  1   48.63  ? 538  GLU A C     1 1 
ATOM   4344 O  O     . GLU A 1 537 ? 17.95   8.564   47.178  1   49     ? 538  GLU A O     1 1 
ATOM   4345 C  CB    . GLU A 1 537 ? 19.905  8.74    49.896  1   52.74  ? 538  GLU A CB    1 1 
ATOM   4346 C  CG    . GLU A 1 537 ? 20.598  10.066  50.179  1   59.95  ? 538  GLU A CG    1 1 
ATOM   4347 C  CD    . GLU A 1 537 ? 20.447  10.562  51.602  1   69.23  ? 538  GLU A CD    1 1 
ATOM   4348 O  OE1   . GLU A 1 537 ? 20.723  9.772   52.534  1   71.8   ? 538  GLU A OE1   1 1 
ATOM   4349 O  OE2   . GLU A 1 537 ? 20.063  11.74   51.789  1   71.75  ? 538  GLU A OE2   1 1 
ATOM   4350 N  N     . LYS A 1 538 ? 19.395  10.296  47.099  1   47.1   ? 539  LYS A N     1 1 
ATOM   4351 C  CA    . LYS A 1 538 ? 18.636  11.131  46.184  1   45.84  ? 539  LYS A CA    1 1 
ATOM   4352 C  C     . LYS A 1 538 ? 19.159  10.929  44.745  1   44.7   ? 539  LYS A C     1 1 
ATOM   4353 O  O     . LYS A 1 538 ? 20.363  10.754  44.54   1   44.99  ? 539  LYS A O     1 1 
ATOM   4354 C  CB    . LYS A 1 538 ? 18.825  12.603  46.556  1   46.84  ? 539  LYS A CB    1 1 
ATOM   4355 C  CG    . LYS A 1 538 ? 18.411  12.943  47.965  1   49.82  ? 539  LYS A CG    1 1 
ATOM   4356 C  CD    . LYS A 1 538 ? 18.664  14.421  48.253  1   52.81  ? 539  LYS A CD    1 1 
ATOM   4357 C  CE    . LYS A 1 538 ? 18.192  14.8    49.635  1   55.24  ? 539  LYS A CE    1 1 
ATOM   4358 N  NZ    . LYS A 1 538 ? 18.296  16.257  49.881  1   56.35  ? 539  LYS A NZ    1 1 
ATOM   4359 N  N     . PRO A 1 539 ? 18.276  11.007  43.729  1   42.68  ? 540  PRO A N     1 1 
ATOM   4360 C  CA    . PRO A 1 539 ? 18.751  10.877  42.336  1   41.01  ? 540  PRO A CA    1 1 
ATOM   4361 C  C     . PRO A 1 539 ? 19.728  11.977  41.936  1   38.44  ? 540  PRO A C     1 1 
ATOM   4362 O  O     . PRO A 1 539 ? 19.62   13.096  42.405  1   37.8   ? 540  PRO A O     1 1 
ATOM   4363 C  CB    . PRO A 1 539 ? 17.474  10.999  41.502  1   41.99  ? 540  PRO A CB    1 1 
ATOM   4364 C  CG    . PRO A 1 539 ? 16.364  10.849  42.452  1   42.85  ? 540  PRO A CG    1 1 
ATOM   4365 C  CD    . PRO A 1 539 ? 16.821  11.212  43.801  1   41.57  ? 540  PRO A CD    1 1 
ATOM   4366 N  N     . LEU A 1 540 ? 20.684  11.652  41.065  1   36.93  ? 541  LEU A N     1 1 
ATOM   4367 C  CA    . LEU A 1 540 ? 21.669  12.62   40.598  1   35.35  ? 541  LEU A CA    1 1 
ATOM   4368 C  C     . LEU A 1 540 ? 21.309  13.097  39.195  1   33.9   ? 541  LEU A C     1 1 
ATOM   4369 O  O     . LEU A 1 540 ? 20.955  12.297  38.344  1   33.88  ? 541  LEU A O     1 1 
ATOM   4370 C  CB    . LEU A 1 540 ? 23.075  11.985  40.597  1   35.21  ? 541  LEU A CB    1 1 
ATOM   4371 C  CG    . LEU A 1 540 ? 24.168  12.705  39.786  1   36.27  ? 541  LEU A CG    1 1 
ATOM   4372 C  CD1   . LEU A 1 540 ? 24.602  13.975  40.459  1   36.67  ? 541  LEU A CD1   1 1 
ATOM   4373 C  CD2   . LEU A 1 540 ? 25.322  11.798  39.468  1   36.5   ? 541  LEU A CD2   1 1 
ATOM   4374 N  N     . LEU A 1 541 ? 21.446  14.391  38.944  1   32.52  ? 542  LEU A N     1 1 
ATOM   4375 C  CA    . LEU A 1 541 ? 21.269  14.947  37.618  1   31.61  ? 542  LEU A CA    1 1 
ATOM   4376 C  C     . LEU A 1 541 ? 22.606  15.589  37.293  1   30.79  ? 542  LEU A C     1 1 
ATOM   4377 O  O     . LEU A 1 541 ? 23.01   16.553  37.946  1   31.29  ? 542  LEU A O     1 1 
ATOM   4378 C  CB    . LEU A 1 541 ? 20.132  15.971  37.572  1   31.42  ? 542  LEU A CB    1 1 
ATOM   4379 C  CG    . LEU A 1 541 ? 18.731  15.417  37.835  1   32.41  ? 542  LEU A CG    1 1 
ATOM   4380 C  CD1   . LEU A 1 541 ? 17.699  16.551  37.959  1   33.05  ? 542  LEU A CD1   1 1 
ATOM   4381 C  CD2   . LEU A 1 541 ? 18.326  14.435  36.77   1   32.29  ? 542  LEU A CD2   1 1 
ATOM   4382 N  N     . LEU A 1 542 ? 23.337  14.991  36.356  1   29.58  ? 543  LEU A N     1 1 
ATOM   4383 C  CA    . LEU A 1 542 ? 24.651  15.45   35.937  1   28.67  ? 543  LEU A CA    1 1 
ATOM   4384 C  C     . LEU A 1 542 ? 24.527  16.221  34.629  1   27.49  ? 543  LEU A C     1 1 
ATOM   4385 O  O     . LEU A 1 542 ? 24.181  15.64   33.606  1   27.18  ? 543  LEU A O     1 1 
ATOM   4386 C  CB    . LEU A 1 542 ? 25.586  14.249  35.76   1   28.28  ? 543  LEU A CB    1 1 
ATOM   4387 C  CG    . LEU A 1 542 ? 26.987  14.587  35.239  1   28.91  ? 543  LEU A CG    1 1 
ATOM   4388 C  CD1   . LEU A 1 542 ? 27.797  15.36   36.274  1   29     ? 543  LEU A CD1   1 1 
ATOM   4389 C  CD2   . LEU A 1 542 ? 27.715  13.324  34.785  1   29.15  ? 543  LEU A CD2   1 1 
ATOM   4390 N  N     . SER A 1 543 ? 24.807  17.518  34.658  1   26.48  ? 544  SER A N     1 1 
ATOM   4391 C  CA    . SER A 1 543 ? 24.687  18.368  33.475  1   26.47  ? 544  SER A CA    1 1 
ATOM   4392 C  C     . SER A 1 543 ? 26.059  18.519  32.832  1   26.77  ? 544  SER A C     1 1 
ATOM   4393 O  O     . SER A 1 543 ? 27.01   18.83   33.529  1   27.62  ? 544  SER A O     1 1 
ATOM   4394 C  CB    . SER A 1 543 ? 24.113  19.727  33.87   1   27.14  ? 544  SER A CB    1 1 
ATOM   4395 O  OG    . SER A 1 543 ? 22.883  19.574  34.571  1   29.18  ? 544  SER A OG    1 1 
ATOM   4396 N  N     . ILE A 1 544 ? 26.19   18.255  31.53   1   26.22  ? 545  ILE A N     1 1 
ATOM   4397 C  CA    . ILE A 1 544 ? 27.498  18.289  30.865  1   26.33  ? 545  ILE A CA    1 1 
ATOM   4398 C  C     . ILE A 1 544 ? 27.543  19.235  29.681  1   27.03  ? 545  ILE A C     1 1 
ATOM   4399 O  O     . ILE A 1 544 ? 26.598  19.304  28.91   1   28.12  ? 545  ILE A O     1 1 
ATOM   4400 C  CB    . ILE A 1 544 ? 27.889  16.863  30.385  1   26.25  ? 545  ILE A CB    1 1 
ATOM   4401 C  CG1   . ILE A 1 544 ? 27.7    15.785  31.479  1   26.61  ? 545  ILE A CG1   1 1 
ATOM   4402 C  CG2   . ILE A 1 544 ? 29.303  16.823  29.801  1   26.35  ? 545  ILE A CG2   1 1 
ATOM   4403 C  CD1   . ILE A 1 544 ? 27.802  14.38   30.955  1   27.55  ? 545  ILE A CD1   1 1 
ATOM   4404 N  N     . VAL A 1 545 ? 28.65   19.937  29.522  1   26.84  ? 546  VAL A N     1 1 
ATOM   4405 C  CA    . VAL A 1 545 ? 28.938  20.781  28.372  1   27.52  ? 546  VAL A CA    1 1 
ATOM   4406 C  C     . VAL A 1 545 ? 30.207  20.202  27.711  1   27.33  ? 546  VAL A C     1 1 
ATOM   4407 O  O     . VAL A 1 545 ? 31.101  19.701  28.413  1   27.45  ? 546  VAL A O     1 1 
ATOM   4408 C  CB    . VAL A 1 545 ? 29.1    22.269  28.777  1   29.07  ? 546  VAL A CB    1 1 
ATOM   4409 C  CG1   . VAL A 1 545 ? 30.127  22.421  29.894  1   29.81  ? 546  VAL A CG1   1 1 
ATOM   4410 C  CG2   . VAL A 1 545 ? 29.473  23.136  27.577  1   29.78  ? 546  VAL A CG2   1 1 
ATOM   4411 N  N     . SER A 1 546 ? 30.249  20.161  26.38   1   27.17  ? 547  SER A N     1 1 
ATOM   4412 C  CA    . SER A 1 546 ? 31.428  19.63   25.7    1   28.17  ? 547  SER A CA    1 1 
ATOM   4413 C  C     . SER A 1 546 ? 32.064  20.684  24.818  1   27.17  ? 547  SER A C     1 1 
ATOM   4414 O  O     . SER A 1 546 ? 31.374  21.412  24.111  1   27.39  ? 547  SER A O     1 1 
ATOM   4415 C  CB    . SER A 1 546 ? 31.114  18.352  24.927  1   31.94  ? 547  SER A CB    1 1 
ATOM   4416 O  OG    . SER A 1 546 ? 30.101  18.611  23.97   1   38.64  ? 547  SER A OG    1 1 
ATOM   4417 N  N     . LYS A 1 547 ? 33.382  20.813  24.914  1   25.74  ? 548  LYS A N     1 1 
ATOM   4418 C  CA    . LYS A 1 547 ? 34.126  21.778  24.132  1   25.44  ? 548  LYS A CA    1 1 
ATOM   4419 C  C     . LYS A 1 547 ? 35.323  21.105  23.487  1   24.75  ? 548  LYS A C     1 1 
ATOM   4420 O  O     . LYS A 1 547 ? 35.769  20.061  23.969  1   25.04  ? 548  LYS A O     1 1 
ATOM   4421 C  CB    . LYS A 1 547 ? 34.595  22.935  25.034  1   27.02  ? 548  LYS A CB    1 1 
ATOM   4422 C  CG    . LYS A 1 547 ? 33.467  23.795  25.589  1   29.98  ? 548  LYS A CG    1 1 
ATOM   4423 C  CD    . LYS A 1 547 ? 32.744  24.549  24.482  1   34.7   ? 548  LYS A CD    1 1 
ATOM   4424 C  CE    . LYS A 1 547 ? 31.506  25.223  25.003  1   39.98  ? 548  LYS A CE    1 1 
ATOM   4425 N  NZ    . LYS A 1 547 ? 31.095  26.35   24.127  1   43.17  ? 548  LYS A NZ    1 1 
ATOM   4426 N  N     . GLU A 1 548 ? 35.889  21.715  22.432  1   24.09  ? 549  GLU A N     1 1 
ATOM   4427 C  CA    . GLU A 1 548 ? 37.084  21.144  21.792  1   23.84  ? 549  GLU A CA    1 1 
ATOM   4428 C  C     . GLU A 1 548 ? 38.281  21.237  22.736  1   23.85  ? 549  GLU A C     1 1 
ATOM   4429 O  O     . GLU A 1 548 ? 39.008  20.252  22.896  1   22.89  ? 549  GLU A O     1 1 
ATOM   4430 C  CB    . GLU A 1 548 ? 37.388  21.876  20.477  1   25.42  ? 549  GLU A CB    1 1 
ATOM   4431 C  CG    . GLU A 1 548 ? 38.641  21.41   19.748  1   28.15  ? 549  GLU A CG    1 1 
ATOM   4432 C  CD    . GLU A 1 548 ? 38.946  22.146  18.448  1   33.94  ? 549  GLU A CD    1 1 
ATOM   4433 O  OE1   . GLU A 1 548 ? 38.24   23.14   18.152  1   37.67  ? 549  GLU A OE1   1 1 
ATOM   4434 O  OE2   . GLU A 1 548 ? 39.886  21.738  17.726  1   32.56  ? 549  GLU A OE2   1 1 
ATOM   4435 N  N     . LYS A 1 549 ? 38.452  22.409  23.407  1   24.13  ? 550  LYS A N     1 1 
ATOM   4436 C  CA    . LYS A 1 549 ? 39.599  22.677  24.291  1   24.92  ? 550  LYS A CA    1 1 
ATOM   4437 C  C     . LYS A 1 549 ? 39.162  23.139  25.683  1   25.87  ? 550  LYS A C     1 1 
ATOM   4438 O  O     . LYS A 1 549 ? 38.132  23.773  25.806  1   24.94  ? 550  LYS A O     1 1 
ATOM   4439 C  CB    . LYS A 1 549 ? 40.51   23.763  23.654  1   25.72  ? 550  LYS A CB    1 1 
ATOM   4440 C  CG    . LYS A 1 549 ? 41.076  23.347  22.316  1   27.43  ? 550  LYS A CG    1 1 
ATOM   4441 C  CD    . LYS A 1 549 ? 42.015  24.346  21.672  1   28.94  ? 550  LYS A CD    1 1 
ATOM   4442 C  CE    . LYS A 1 549 ? 42.586  23.655  20.456  1   31.08  ? 550  LYS A CE    1 1 
ATOM   4443 N  NZ    . LYS A 1 549 ? 43.729  24.361  19.841  1   31.81  ? 550  LYS A NZ    1 1 
ATOM   4444 N  N     . PRO A 1 550 ? 39.974  22.907  26.737  1   27.45  ? 551  PRO A N     1 1 
ATOM   4445 C  CA    . PRO A 1 550 ? 39.576  23.359  28.084  1   28.26  ? 551  PRO A CA    1 1 
ATOM   4446 C  C     . PRO A 1 550 ? 39.352  24.856  28.21   1   30.33  ? 551  PRO A C     1 1 
ATOM   4447 O  O     . PRO A 1 550 ? 38.436  25.25   28.934  1   31.03  ? 551  PRO A O     1 1 
ATOM   4448 C  CB    . PRO A 1 550 ? 40.712  22.867  28.992  1   28.76  ? 551  PRO A CB    1 1 
ATOM   4449 C  CG    . PRO A 1 550 ? 41.855  22.568  28.081  1   28.54  ? 551  PRO A CG    1 1 
ATOM   4450 C  CD    . PRO A 1 550 ? 41.26   22.179  26.763  1   27.07  ? 551  PRO A CD    1 1 
ATOM   4451 N  N     . ASN A 1 551 ? 40.136  25.704  27.503  1   30.93  ? 552  ASN A N     1 1 
ATOM   4452 C  CA    . ASN A 1 551 ? 39.912  27.16   27.59   1   32.09  ? 552  ASN A CA    1 1 
ATOM   4453 C  C     . ASN A 1 551 ? 38.655  27.631  26.844  1   32.25  ? 552  ASN A C     1 1 
ATOM   4454 O  O     . ASN A 1 551 ? 38.24   28.778  27.018  1   31.74  ? 552  ASN A O     1 1 
ATOM   4455 C  CB    . ASN A 1 551 ? 41.127  27.984  27.198  1   34.67  ? 552  ASN A CB    1 1 
ATOM   4456 C  CG    . ASN A 1 551 ? 42.246  27.87   28.214  1   40.08  ? 552  ASN A CG    1 1 
ATOM   4457 O  OD1   . ASN A 1 551 ? 42.017  27.562  29.394  1   41.35  ? 552  ASN A OD1   1 1 
ATOM   4458 N  ND2   . ASN A 1 551 ? 43.49   28.083  27.77   1   41.9   ? 552  ASN A ND2   1 1 
ATOM   4459 N  N     . ASP A 1 552 ? 37.992  26.728  26.087  1   31.94  ? 553  ASP A N     1 1 
ATOM   4460 C  CA    . ASP A 1 552 ? 36.709  27.051  25.481  1   31.91  ? 553  ASP A CA    1 1 
ATOM   4461 C  C     . ASP A 1 552 ? 35.579  26.991  26.537  1   31.7   ? 553  ASP A C     1 1 
ATOM   4462 O  O     . ASP A 1 552 ? 34.48   27.441  26.247  1   32.26  ? 553  ASP A O     1 1 
ATOM   4463 C  CB    . ASP A 1 552 ? 36.403  26.105  24.309  1   33.8   ? 553  ASP A CB    1 1 
ATOM   4464 C  CG    . ASP A 1 552 ? 37.429  26.176  23.2    1   38.2   ? 553  ASP A CG    1 1 
ATOM   4465 O  OD1   . ASP A 1 552 ? 38.071  27.236  23.054  1   38.72  ? 553  ASP A OD1   1 1 
ATOM   4466 O  OD2   . ASP A 1 552 ? 37.591  25.169  22.476  1   39.84  ? 553  ASP A OD2   1 1 
ATOM   4467 N  N     . LEU A 1 553 ? 35.817  26.4    27.728  1   31.2   ? 554  LEU A N     1 1 
ATOM   4468 C  CA    . LEU A 1 553 ? 34.816  26.346  28.784  1   31.89  ? 554  LEU A CA    1 1 
ATOM   4469 C  C     . LEU A 1 553 ? 34.738  27.762  29.365  1   33.24  ? 554  LEU A C     1 1 
ATOM   4470 O  O     . LEU A 1 553 ? 35.715  28.252  29.919  1   33.14  ? 554  LEU A O     1 1 
ATOM   4471 C  CB    . LEU A 1 553 ? 35.22   25.343  29.872  1   31.31  ? 554  LEU A CB    1 1 
ATOM   4472 C  CG    . LEU A 1 553 ? 35.137  23.878  29.495  1   31.69  ? 554  LEU A CG    1 1 
ATOM   4473 C  CD1   . LEU A 1 553 ? 35.74   23.018  30.573  1   31.76  ? 554  LEU A CD1   1 1 
ATOM   4474 C  CD2   . LEU A 1 553 ? 33.703  23.47   29.221  1   31.83  ? 554  LEU A CD2   1 1 
ATOM   4475 N  N     . GLU A 1 554 ? 33.604  28.432  29.16   1   34.33  ? 555  GLU A N     1 1 
ATOM   4476 C  CA    . GLU A 1 554 ? 33.376  29.823  29.541  1   36.13  ? 555  GLU A CA    1 1 
ATOM   4477 C  C     . GLU A 1 554 ? 33.301  30.045  31.04   1   36.8   ? 555  GLU A C     1 1 
ATOM   4478 O  O     . GLU A 1 554 ? 32.935  29.13   31.772  1   36.97  ? 555  GLU A O     1 1 
ATOM   4479 C  CB    . GLU A 1 554 ? 32.093  30.337  28.856  1   40.3   ? 555  GLU A CB    1 1 
ATOM   4480 C  CG    . GLU A 1 554 ? 32.306  30.671  27.39   1   49.03  ? 555  GLU A CG    1 1 
ATOM   4481 C  CD    . GLU A 1 554 ? 31.043  30.829  26.568  1   60.21  ? 555  GLU A CD    1 1 
ATOM   4482 O  OE1   . GLU A 1 554 ? 30.195  29.906  26.586  1   63.3   ? 555  GLU A OE1   1 1 
ATOM   4483 O  OE2   . GLU A 1 554 ? 30.909  31.874  25.888  1   63.95  ? 555  GLU A OE2   1 1 
ATOM   4484 N  N     . PRO A 1 555 ? 33.613  31.272  31.522  1   37.07  ? 556  PRO A N     1 1 
ATOM   4485 C  CA    . PRO A 1 555 ? 33.496  31.545  32.964  1   36.7   ? 556  PRO A CA    1 1 
ATOM   4486 C  C     . PRO A 1 555 ? 32.088  31.264  33.502  1   36.19  ? 556  PRO A C     1 1 
ATOM   4487 O  O     . PRO A 1 555 ? 31.094  31.578  32.853  1   35.99  ? 556  PRO A O     1 1 
ATOM   4488 C  CB    . PRO A 1 555 ? 33.858  33.034  33.077  1   37.66  ? 556  PRO A CB    1 1 
ATOM   4489 C  CG    . PRO A 1 555 ? 34.675  33.324  31.855  1   38.28  ? 556  PRO A CG    1 1 
ATOM   4490 C  CD    . PRO A 1 555 ? 34.07   32.465  30.782  1   36.82  ? 556  PRO A CD    1 1 
ATOM   4491 N  N     . LYS A 1 556 ? 32.028  30.592  34.659  1   35.98  ? 557  LYS A N     1 1 
ATOM   4492 C  CA    . LYS A 1 556 ? 30.827  30.182  35.377  1   36.4   ? 557  LYS A CA    1 1 
ATOM   4493 C  C     . LYS A 1 556 ? 29.929  29.193  34.606  1   36.13  ? 557  LYS A C     1 1 
ATOM   4494 O  O     . LYS A 1 556 ? 28.784  29.018  35.006  1   36.6   ? 557  LYS A O     1 1 
ATOM   4495 C  CB    . LYS A 1 556 ? 30.012  31.401  35.857  1   38.98  ? 557  LYS A CB    1 1 
ATOM   4496 C  CG    . LYS A 1 556 ? 30.842  32.394  36.672  1   43.47  ? 557  LYS A CG    1 1 
ATOM   4497 C  CD    . LYS A 1 556 ? 30.168  33.758  36.751  1   48.89  ? 557  LYS A CD    1 1 
ATOM   4498 C  CE    . LYS A 1 556 ? 28.884  33.775  37.556  1   52.94  ? 557  LYS A CE    1 1 
ATOM   4499 N  NZ    . LYS A 1 556 ? 28.464  35.174  37.893  1   54.46  ? 557  LYS A NZ    1 1 
ATOM   4500 N  N     . ILE A 1 557 ? 30.438  28.515  33.552  1   35.28  ? 558  ILE A N     1 1 
ATOM   4501 C  CA    . ILE A 1 557 ? 29.618  27.563  32.783  1   34.89  ? 558  ILE A CA    1 1 
ATOM   4502 C  C     . ILE A 1 557 ? 29.046  26.455  33.677  1   34.35  ? 558  ILE A C     1 1 
ATOM   4503 O  O     . ILE A 1 557 ? 27.878  26.126  33.535  1   34.55  ? 558  ILE A O     1 1 
ATOM   4504 C  CB    . ILE A 1 557 ? 30.345  27.001  31.521  1   35.34  ? 558  ILE A CB    1 1 
ATOM   4505 C  CG1   . ILE A 1 557 ? 29.373  26.252  30.587  1   36.14  ? 558  ILE A CG1   1 1 
ATOM   4506 C  CG2   . ILE A 1 557 ? 31.535  26.126  31.883  1   35.54  ? 558  ILE A CG2   1 1 
ATOM   4507 C  CD1   . ILE A 1 557 ? 28.185  27.079  30.101  1   37     ? 558  ILE A CD1   1 1 
ATOM   4508 N  N     . GLY A 1 558 ? 29.838  25.953  34.626  1   33.76  ? 559  GLY A N     1 1 
ATOM   4509 C  CA    . GLY A 1 558 ? 29.397  24.927  35.565  1   33.21  ? 559  GLY A CA    1 1 
ATOM   4510 C  C     . GLY A 1 558 ? 28.227  25.383  36.412  1   32.74  ? 559  GLY A C     1 1 
ATOM   4511 O  O     . GLY A 1 558 ? 27.231  24.667  36.529  1   32.71  ? 559  GLY A O     1 1 
ATOM   4512 N  N     . VAL A 1 559 ? 28.307  26.614  36.951  1   32.39  ? 560  VAL A N     1 1 
ATOM   4513 C  CA    . VAL A 1 559 ? 27.236  27.207  37.759  1   32.53  ? 560  VAL A CA    1 1 
ATOM   4514 C  C     . VAL A 1 559 ? 25.98   27.478  36.901  1   32.35  ? 560  VAL A C     1 1 
ATOM   4515 O  O     . VAL A 1 559 ? 24.856  27.224  37.341  1   32.76  ? 560  VAL A O     1 1 
ATOM   4516 C  CB    . VAL A 1 559 ? 27.739  28.489  38.482  1   33.57  ? 560  VAL A CB    1 1 
ATOM   4517 C  CG1   . VAL A 1 559 ? 26.601  29.194  39.222  1   34.59  ? 560  VAL A CG1   1 1 
ATOM   4518 C  CG2   . VAL A 1 559 ? 28.889  28.167  39.434  1   33.79  ? 560  VAL A CG2   1 1 
ATOM   4519 N  N     . GLN A 1 560 ? 26.174  27.952  35.663  1   31.8   ? 561  GLN A N     1 1 
ATOM   4520 C  CA    . GLN A 1 560 ? 25.083  28.237  34.73   1   31.62  ? 561  GLN A CA    1 1 
ATOM   4521 C  C     . GLN A 1 560 ? 24.319  26.959  34.346  1   31.6   ? 561  GLN A C     1 1 
ATOM   4522 O  O     . GLN A 1 560 ? 23.116  27.029  34.12   1   31.81  ? 561  GLN A O     1 1 
ATOM   4523 C  CB    . GLN A 1 560 ? 25.614  28.934  33.47   1   33.28  ? 561  GLN A CB    1 1 
ATOM   4524 C  CG    . GLN A 1 560 ? 26.153  30.321  33.753  1   38.74  ? 561  GLN A CG    1 1 
ATOM   4525 C  CD    . GLN A 1 560 ? 26.74   30.957  32.525  1   45.56  ? 561  GLN A CD    1 1 
ATOM   4526 O  OE1   . GLN A 1 560 ? 27.923  30.799  32.215  1   47.82  ? 561  GLN A OE1   1 1 
ATOM   4527 N  NE2   . GLN A 1 560 ? 25.922  31.697  31.8    1   47.58  ? 561  GLN A NE2   1 1 
ATOM   4528 N  N     . LEU A 1 561 ? 25.009  25.808  34.258  1   30.86  ? 562  LEU A N     1 1 
ATOM   4529 C  CA    . LEU A 1 561 ? 24.361  24.546  33.932  1   31.17  ? 562  LEU A CA    1 1 
ATOM   4530 C  C     . LEU A 1 561 ? 23.416  24.159  35.053  1   32.14  ? 562  LEU A C     1 1 
ATOM   4531 O  O     . LEU A 1 561 ? 22.291  23.751  34.772  1   32.71  ? 562  LEU A O     1 1 
ATOM   4532 C  CB    . LEU A 1 561 ? 25.387  23.413  33.672  1   30.81  ? 562  LEU A CB    1 1 
ATOM   4533 C  CG    . LEU A 1 561 ? 26.315  23.607  32.47   1   32.17  ? 562  LEU A CG    1 1 
ATOM   4534 C  CD1   . LEU A 1 561 ? 27.346  22.474  32.338  1   33.23  ? 562  LEU A CD1   1 1 
ATOM   4535 C  CD2   . LEU A 1 561 ? 25.549  23.82   31.192  1   32.58  ? 562  LEU A CD2   1 1 
ATOM   4536 N  N     . ILE A 1 562 ? 23.853  24.307  36.318  1   32.14  ? 563  ILE A N     1 1 
ATOM   4537 C  CA    . ILE A 1 562 ? 23.019  23.999  37.483  1   32.5   ? 563  ILE A CA    1 1 
ATOM   4538 C  C     . ILE A 1 562 ? 21.826  24.934  37.542  1   33.13  ? 563  ILE A C     1 1 
ATOM   4539 O  O     . ILE A 1 562 ? 20.693  24.474  37.721  1   33.1   ? 563  ILE A O     1 1 
ATOM   4540 C  CB    . ILE A 1 562 ? 23.835  24.07   38.787  1   32.83  ? 563  ILE A CB    1 1 
ATOM   4541 C  CG1   . ILE A 1 562 ? 25.009  23.082  38.762  1   33.39  ? 563  ILE A CG1   1 1 
ATOM   4542 C  CG2   . ILE A 1 562 ? 22.94   23.888  40.02   1   33.15  ? 563  ILE A CG2   1 1 
ATOM   4543 C  CD1   . ILE A 1 562 ? 24.633  21.676  38.702  1   34.54  ? 563  ILE A CD1   1 1 
ATOM   4544 N  N     . LYS A 1 563 ? 22.066  26.232  37.326  1   33.52  ? 564  LYS A N     1 1 
ATOM   4545 C  CA    . LYS A 1 563 ? 21.022  27.256  37.341  1   34.31  ? 564  LYS A CA    1 1 
ATOM   4546 C  C     . LYS A 1 563 ? 19.975  27.043  36.254  1   34.4   ? 564  LYS A C     1 1 
ATOM   4547 O  O     . LYS A 1 563 ? 18.811  27.41   36.451  1   34.88  ? 564  LYS A O     1 1 
ATOM   4548 C  CB    . LYS A 1 563 ? 21.613  28.669  37.279  1   37.59  ? 564  LYS A CB    1 1 
ATOM   4549 C  CG    . LYS A 1 563 ? 22.532  29.027  38.456  1   44.33  ? 564  LYS A CG    1 1 
ATOM   4550 C  CD    . LYS A 1 563 ? 21.904  28.857  39.866  1   51.16  ? 564  LYS A CD    1 1 
ATOM   4551 C  CE    . LYS A 1 563 ? 22.715  29.601  40.927  1   56.25  ? 564  LYS A CE    1 1 
ATOM   4552 N  NZ    . LYS A 1 563 ? 22.389  29.191  42.331  1   58.41  ? 564  LYS A NZ    1 1 
ATOM   4553 N  N     . TYR A 1 564 ? 20.352  26.38   35.143  1   33.56  ? 565  TYR A N     1 1 
ATOM   4554 C  CA    . TYR A 1 564 ? 19.404  26.032  34.087  1   32.64  ? 565  TYR A CA    1 1 
ATOM   4555 C  C     . TYR A 1 564 ? 18.45   24.946  34.581  1   33.21  ? 565  TYR A C     1 1 
ATOM   4556 O  O     . TYR A 1 564 ? 17.245  25.01   34.315  1   33.89  ? 565  TYR A O     1 1 
ATOM   4557 C  CB    . TYR A 1 564 ? 20.134  25.553  32.848  1   31.41  ? 565  TYR A CB    1 1 
ATOM   4558 C  CG    . TYR A 1 564 ? 19.239  25.492  31.641  1   30.54  ? 565  TYR A CG    1 1 
ATOM   4559 C  CD1   . TYR A 1 564 ? 19.026  26.614  30.854  1   30.61  ? 565  TYR A CD1   1 1 
ATOM   4560 C  CD2   . TYR A 1 564 ? 18.606  24.307  31.277  1   30.79  ? 565  TYR A CD2   1 1 
ATOM   4561 C  CE1   . TYR A 1 564 ? 18.225  26.556  29.725  1   31.03  ? 565  TYR A CE1   1 1 
ATOM   4562 C  CE2   . TYR A 1 564 ? 17.788  24.242  30.161  1   30.83  ? 565  TYR A CE2   1 1 
ATOM   4563 C  CZ    . TYR A 1 564 ? 17.598  25.372  29.391  1   31.34  ? 565  TYR A CZ    1 1 
ATOM   4564 O  OH    . TYR A 1 564 ? 16.801  25.317  28.286  1   31.9   ? 565  TYR A OH    1 1 
ATOM   4565 N  N     . ILE A 1 565 ? 18.969  23.955  35.307  1   32.9   ? 566  ILE A N     1 1 
ATOM   4566 C  CA    . ILE A 1 565 ? 18.124  22.905  35.873  1   33.14  ? 566  ILE A CA    1 1 
ATOM   4567 C  C     . ILE A 1 565 ? 17.201  23.515  36.943  1   34.06  ? 566  ILE A C     1 1 
ATOM   4568 O  O     . ILE A 1 565 ? 16.019  23.183  37      1   34.25  ? 566  ILE A O     1 1 
ATOM   4569 C  CB    . ILE A 1 565 ? 18.986  21.738  36.42   1   33.1   ? 566  ILE A CB    1 1 
ATOM   4570 C  CG1   . ILE A 1 565 ? 19.942  21.195  35.336  1   33.64  ? 566  ILE A CG1   1 1 
ATOM   4571 C  CG2   . ILE A 1 565 ? 18.121  20.633  37.02   1   33.06  ? 566  ILE A CG2   1 1 
ATOM   4572 C  CD1   . ILE A 1 565 ? 19.287  20.665  34.115  1   34.43  ? 566  ILE A CD1   1 1 
ATOM   4573 N  N     . GLU A 1 566 ? 17.728  24.455  37.744  1   34.48  ? 567  GLU A N     1 1 
ATOM   4574 C  CA    . GLU A 1 566 ? 16.97   25.17   38.771  1   34.94  ? 567  GLU A CA    1 1 
ATOM   4575 C  C     . GLU A 1 566 ? 15.839  25.972  38.14   1   35.19  ? 567  GLU A C     1 1 
ATOM   4576 O  O     . GLU A 1 566 ? 14.755  26.042  38.714  1   35.75  ? 567  GLU A O     1 1 
ATOM   4577 C  CB    . GLU A 1 566 ? 17.891  26.087  39.604  1   37.51  ? 567  GLU A CB    1 1 
ATOM   4578 C  CG    . GLU A 1 566 ? 18.995  25.374  40.378  1   43.24  ? 567  GLU A CG    1 1 
ATOM   4579 C  CD    . GLU A 1 566 ? 18.624  24.725  41.702  1   51.69  ? 567  GLU A CD    1 1 
ATOM   4580 O  OE1   . GLU A 1 566 ? 17.51   24.162  41.816  1   53.22  ? 567  GLU A OE1   1 1 
ATOM   4581 O  OE2   . GLU A 1 566 ? 19.47   24.762  42.626  1   54.55  ? 567  GLU A OE2   1 1 
ATOM   4582 N  N     . TYR A 1 567 ? 16.079  26.561  36.953  1   34.76  ? 568  TYR A N     1 1 
ATOM   4583 C  CA    . TYR A 1 567 ? 15.075  27.298  36.184  1   34.92  ? 568  TYR A CA    1 1 
ATOM   4584 C  C     . TYR A 1 567 ? 13.933  26.357  35.796  1   35.06  ? 568  TYR A C     1 1 
ATOM   4585 O  O     . TYR A 1 567 ? 12.788  26.695  36.038  1   35.35  ? 568  TYR A O     1 1 
ATOM   4586 C  CB    . TYR A 1 567 ? 15.727  27.929  34.944  1   35.38  ? 568  TYR A CB    1 1 
ATOM   4587 C  CG    . TYR A 1 567 ? 14.805  28.305  33.806  1   37.35  ? 568  TYR A CG    1 1 
ATOM   4588 C  CD1   . TYR A 1 567 ? 14.008  29.436  33.877  1   38.95  ? 568  TYR A CD1   1 1 
ATOM   4589 C  CD2   . TYR A 1 567 ? 14.82   27.599  32.612  1   38.92  ? 568  TYR A CD2   1 1 
ATOM   4590 C  CE1   . TYR A 1 567 ? 13.199  29.819  32.812  1   40.37  ? 568  TYR A CE1   1 1 
ATOM   4591 C  CE2   . TYR A 1 567 ? 14.03   27.983  31.533  1   40.03  ? 568  TYR A CE2   1 1 
ATOM   4592 C  CZ    . TYR A 1 567 ? 13.214  29.09   31.638  1   41.22  ? 568  TYR A CZ    1 1 
ATOM   4593 O  OH    . TYR A 1 567 ? 12.434  29.479  30.573  1   42.75  ? 568  TYR A OH    1 1 
ATOM   4594 N  N     . LEU A 1 568 ? 14.236  25.165  35.251  1   34.54  ? 569  LEU A N     1 1 
ATOM   4595 C  CA    . LEU A 1 568 ? 13.206  24.213  34.864  1   34.59  ? 569  LEU A CA    1 1 
ATOM   4596 C  C     . LEU A 1 568 ? 12.398  23.756  36.058  1   35.91  ? 569  LEU A C     1 1 
ATOM   4597 O  O     . LEU A 1 568 ? 11.172  23.714  35.959  1   36.46  ? 569  LEU A O     1 1 
ATOM   4598 C  CB    . LEU A 1 568 ? 13.802  23.022  34.097  1   33.97  ? 569  LEU A CB    1 1 
ATOM   4599 C  CG    . LEU A 1 568 ? 14.577  23.401  32.833  1   34.67  ? 569  LEU A CG    1 1 
ATOM   4600 C  CD1   . LEU A 1 568 ? 15.168  22.185  32.177  1   35.06  ? 569  LEU A CD1   1 1 
ATOM   4601 C  CD2   . LEU A 1 568 ? 13.694  24.153  31.834  1   34.98  ? 569  LEU A CD2   1 1 
ATOM   4602 N  N     . PHE A 1 569 ? 13.058  23.478  37.205  1   36.31  ? 570  PHE A N     1 1 
ATOM   4603 C  CA    . PHE A 1 569 ? 12.368  23.074  38.437  1   37.27  ? 570  PHE A CA    1 1 
ATOM   4604 C  C     . PHE A 1 569 ? 11.391  24.148  38.96   1   38.11  ? 570  PHE A C     1 1 
ATOM   4605 O  O     . PHE A 1 569 ? 10.44   23.813  39.672  1   38.6   ? 570  PHE A O     1 1 
ATOM   4606 C  CB    . PHE A 1 569 ? 13.352  22.671  39.537  1   37.54  ? 570  PHE A CB    1 1 
ATOM   4607 C  CG    . PHE A 1 569 ? 13.758  21.217  39.52   1   38.59  ? 570  PHE A CG    1 1 
ATOM   4608 C  CD1   . PHE A 1 569 ? 14.804  20.783  38.727  1   39.43  ? 570  PHE A CD1   1 1 
ATOM   4609 C  CD2   . PHE A 1 569 ? 13.116  20.291  40.321  1   39.51  ? 570  PHE A CD2   1 1 
ATOM   4610 C  CE1   . PHE A 1 569 ? 15.183  19.451  38.714  1   40.21  ? 570  PHE A CE1   1 1 
ATOM   4611 C  CE2   . PHE A 1 569 ? 13.497  18.956  40.304  1   40.54  ? 570  PHE A CE2   1 1 
ATOM   4612 C  CZ    . PHE A 1 569 ? 14.54   18.547  39.512  1   40.28  ? 570  PHE A CZ    1 1 
ATOM   4613 N  N     . ASP A 1 570 ? 11.587  25.423  38.583  1   38.14  ? 571  ASP A N     1 1 
ATOM   4614 C  CA    . ASP A 1 570 ? 10.656  26.489  38.986  1   38.74  ? 571  ASP A CA    1 1 
ATOM   4615 C  C     . ASP A 1 570 ? 9.289   26.392  38.267  1   39.66  ? 571  ASP A C     1 1 
ATOM   4616 O  O     . ASP A 1 570 ? 8.403   27.205  38.552  1   40.13  ? 571  ASP A O     1 1 
ATOM   4617 C  CB    . ASP A 1 570 ? 11.238  27.873  38.683  1   39.77  ? 571  ASP A CB    1 1 
ATOM   4618 C  CG    . ASP A 1 570 ? 12.335  28.333  39.615  1   44.37  ? 571  ASP A CG    1 1 
ATOM   4619 O  OD1   . ASP A 1 570 ? 12.534  27.681  40.669  1   45.06  ? 571  ASP A OD1   1 1 
ATOM   4620 O  OD2   . ASP A 1 570 ? 13      29.341  39.29   1   46.54  ? 571  ASP A OD2   1 1 
ATOM   4621 N  N     . PHE A 1 571 ? 9.143   25.458  37.304  1   39.25  ? 572  PHE A N     1 1 
ATOM   4622 C  CA    . PHE A 1 571 ? 7.941   25.314  36.509  1   39.26  ? 572  PHE A CA    1 1 
ATOM   4623 C  C     . PHE A 1 571 ? 7.485   23.87   36.409  1   38.93  ? 572  PHE A C     1 1 
ATOM   4624 O  O     . PHE A 1 571 ? 8.29    22.945  36.547  1   38.51  ? 572  PHE A O     1 1 
ATOM   4625 C  CB    . PHE A 1 571 ? 8.159   25.894  35.107  1   39.32  ? 572  PHE A CB    1 1 
ATOM   4626 C  CG    . PHE A 1 571 ? 8.636   27.322  35.124  1   40.53  ? 572  PHE A CG    1 1 
ATOM   4627 C  CD1   . PHE A 1 571 ? 7.773   28.354  35.442  1   41.6   ? 572  PHE A CD1   1 1 
ATOM   4628 C  CD2   . PHE A 1 571 ? 9.958   27.63   34.869  1   41.75  ? 572  PHE A CD2   1 1 
ATOM   4629 C  CE1   . PHE A 1 571 ? 8.22    29.665  35.486  1   42.43  ? 572  PHE A CE1   1 1 
ATOM   4630 C  CE2   . PHE A 1 571 ? 10.396  28.948  34.883  1   42.67  ? 572  PHE A CE2   1 1 
ATOM   4631 C  CZ    . PHE A 1 571 ? 9.521   29.958  35.181  1   42.42  ? 572  PHE A CZ    1 1 
ATOM   4632 N  N     . THR A 1 572 ? 6.172   23.683  36.175  1   38.52  ? 573  THR A N     1 1 
ATOM   4633 C  CA    . THR A 1 572 ? 5.565   22.361  36.014  1   38.62  ? 573  THR A CA    1 1 
ATOM   4634 C  C     . THR A 1 572 ? 6.124   21.732  34.734  1   37.97  ? 573  THR A C     1 1 
ATOM   4635 O  O     . THR A 1 572 ? 6.186   22.406  33.709  1   37.91  ? 573  THR A O     1 1 
ATOM   4636 C  CB    . THR A 1 572 ? 4.04    22.528  35.881  1   40.51  ? 573  THR A CB    1 1 
ATOM   4637 O  OG1   . THR A 1 572 ? 3.498   23.097  37.078  1   42.23  ? 573  THR A OG1   1 1 
ATOM   4638 C  CG2   . THR A 1 572 ? 3.336   21.237  35.56   1   40.51  ? 573  THR A CG2   1 1 
ATOM   4639 N  N     . PRO A 1 573 ? 6.526   20.446  34.742  1   37.73  ? 574  PRO A N     1 1 
ATOM   4640 C  CA    . PRO A 1 573 ? 7.011   19.819  33.494  1   37.72  ? 574  PRO A CA    1 1 
ATOM   4641 C  C     . PRO A 1 573 ? 5.999   19.955  32.359  1   37.32  ? 574  PRO A C     1 1 
ATOM   4642 O  O     . PRO A 1 573 ? 4.797   19.896  32.619  1   37.88  ? 574  PRO A O     1 1 
ATOM   4643 C  CB    . PRO A 1 573 ? 7.171   18.342  33.871  1   38.58  ? 574  PRO A CB    1 1 
ATOM   4644 C  CG    . PRO A 1 573 ? 7.302   18.333  35.348  1   39.02  ? 574  PRO A CG    1 1 
ATOM   4645 C  CD    . PRO A 1 573 ? 6.502   19.489  35.862  1   37.13  ? 574  PRO A CD    1 1 
ATOM   4646 N  N     . SER A 1 574 ? 6.456   20.165  31.112  1   35.98  ? 575  SER A N     1 1 
ATOM   4647 C  CA    . SER A 1 574 ? 5.543   20.294  29.974  1   35.27  ? 575  SER A CA    1 1 
ATOM   4648 C  C     . SER A 1 574 ? 4.551   19.095  29.886  1   35.45  ? 575  SER A C     1 1 
ATOM   4649 O  O     . SER A 1 574 ? 3.336   19.289  29.842  1   35.36  ? 575  SER A O     1 1 
ATOM   4650 C  CB    . SER A 1 574 ? 6.329   20.401  28.672  1   34.75  ? 575  SER A CB    1 1 
ATOM   4651 O  OG    . SER A 1 574 ? 7.242   21.484  28.674  1   34.17  ? 575  SER A OG    1 1 
ATOM   4652 N  N     . VAL A 1 575 ? 5.08    17.872  29.966  1   35.16  ? 576  VAL A N     1 1 
ATOM   4653 C  CA    . VAL A 1 575 ? 4.292   16.647  29.881  1   35.44  ? 576  VAL A CA    1 1 
ATOM   4654 C  C     . VAL A 1 575 ? 4.744   15.59   30.902  1   35.91  ? 576  VAL A C     1 1 
ATOM   4655 O  O     . VAL A 1 575 ? 5.817   15.694  31.49   1   35.64  ? 576  VAL A O     1 1 
ATOM   4656 C  CB    . VAL A 1 575 ? 4.332   16.08   28.435  1   35.72  ? 576  VAL A CB    1 1 
ATOM   4657 C  CG1   . VAL A 1 575 ? 3.473   16.909  27.48   1   36.07  ? 576  VAL A CG1   1 1 
ATOM   4658 C  CG2   . VAL A 1 575 ? 5.775   15.952  27.932  1   35.79  ? 576  VAL A CG2   1 1 
ATOM   4659 N  N     . GLN A 1 576 ? 3.911   14.583  31.125  1   36.53  ? 577  GLN A N     1 1 
ATOM   4660 C  CA    . GLN A 1 576 ? 4.24    13.461  31.985  1   37.77  ? 577  GLN A CA    1 1 
ATOM   4661 C  C     . GLN A 1 576 ? 3.471   12.206  31.533  1   39.17  ? 577  GLN A C     1 1 
ATOM   4662 O  O     . GLN A 1 576 ? 2.466   12.305  30.835  1   38.71  ? 577  GLN A O     1 1 
ATOM   4663 C  CB    . GLN A 1 576 ? 3.97    13.778  33.452  1   39.39  ? 577  GLN A CB    1 1 
ATOM   4664 C  CG    . GLN A 1 576 ? 2.496   13.88   33.772  1   44.32  ? 577  GLN A CG    1 1 
ATOM   4665 C  CD    . GLN A 1 576 ? 2.313   14.014  35.248  1   50.12  ? 577  GLN A CD    1 1 
ATOM   4666 O  OE1   . GLN A 1 576 ? 2.765   14.988  35.858  1   52.9   ? 577  GLN A OE1   1 1 
ATOM   4667 N  NE2   . GLN A 1 576 ? 1.657   13.038  35.853  1   50.34  ? 577  GLN A NE2   1 1 
ATOM   4668 N  N     . ARG A 1 577 ? 3.97    11.035  31.912  1   40.69  ? 578  ARG A N     1 1 
ATOM   4669 C  CA    . ARG A 1 577 ? 3.351   9.758   31.611  1   42.91  ? 578  ARG A CA    1 1 
ATOM   4670 C  C     . ARG A 1 577 ? 3.729   8.739   32.672  1   46.15  ? 578  ARG A C     1 1 
ATOM   4671 O  O     . ARG A 1 577 ? 4.751   8.881   33.344  1   46.42  ? 578  ARG A O     1 1 
ATOM   4672 C  CB    . ARG A 1 577 ? 3.731   9.25    30.205  1   43.71  ? 578  ARG A CB    1 1 
ATOM   4673 C  CG    . ARG A 1 577 ? 5.173   8.749   30.067  1   46.02  ? 578  ARG A CG    1 1 
ATOM   4674 C  CD    . ARG A 1 577 ? 5.418   8.116   28.718  1   47.56  ? 578  ARG A CD    1 1 
ATOM   4675 N  NE    . ARG A 1 577 ? 6.847   7.98    28.438  1   49.29  ? 578  ARG A NE    1 1 
ATOM   4676 C  CZ    . ARG A 1 577 ? 7.345   7.47    27.315  1   50.43  ? 578  ARG A CZ    1 1 
ATOM   4677 N  NH1   . ARG A 1 577 ? 6.532   7.031   26.358  1   50.07  ? 578  ARG A NH1   1 1 
ATOM   4678 N  NH2   . ARG A 1 577 ? 8.661   7.384   27.144  1   48.48  ? 578  ARG A NH2   1 1 
ATOM   4679 N  N     . LYS A 1 578 ? 2.9     7.705   32.83   1   48.46  ? 579  LYS A N     1 1 
ATOM   4680 C  CA    . LYS A 1 578 ? 3.192   6.629   33.768  1   50.78  ? 579  LYS A CA    1 1 
ATOM   4681 C  C     . LYS A 1 578 ? 4.133   5.679   33.031  1   53.08  ? 579  LYS A C     1 1 
ATOM   4682 O  O     . LYS A 1 578 ? 3.853   5.309   31.893  1   53.25  ? 579  LYS A O     1 1 
ATOM   4683 C  CB    . LYS A 1 578 ? 1.895   5.905   34.169  1   52.81  ? 579  LYS A CB    1 1 
ATOM   4684 C  CG    . LYS A 1 578 ? 0.807   6.836   34.682  1   57.88  ? 579  LYS A CG    1 1 
ATOM   4685 C  CD    . LYS A 1 578 ? -0.554  6.144   34.746  1   63.89  ? 579  LYS A CD    1 1 
ATOM   4686 C  CE    . LYS A 1 578 ? -1.104  5.79    33.377  1   68.48  ? 579  LYS A CE    1 1 
ATOM   4687 N  NZ    . LYS A 1 578 ? -2.409  5.074   33.466  1   70.6   ? 579  LYS A NZ    1 1 
ATOM   4688 N  N     . ILE A 1 579 ? 5.251   5.302   33.651  1   54.88  ? 580  ILE A N     1 1 
ATOM   4689 C  CA    . ILE A 1 579 ? 6.221   4.404   33.016  1   57.38  ? 580  ILE A CA    1 1 
ATOM   4690 C  C     . ILE A 1 579 ? 5.606   3.012   32.71   1   59.14  ? 580  ILE A C     1 1 
ATOM   4691 O  O     . ILE A 1 579 ? 6.04    2.344   31.774  1   59.17  ? 580  ILE A O     1 1 
ATOM   4692 C  CB    . ILE A 1 579 ? 7.54    4.337   33.837  1   58.56  ? 580  ILE A CB    1 1 
ATOM   4693 C  CG1   . ILE A 1 579 ? 8.722   3.844   32.991  1   59.99  ? 580  ILE A CG1   1 1 
ATOM   4694 C  CG2   . ILE A 1 579 ? 7.392   3.536   35.123  1   59.35  ? 580  ILE A CG2   1 1 
ATOM   4695 C  CD1   . ILE A 1 579 ? 9.277   4.892   32.041  1   61.54  ? 580  ILE A CD1   1 1 
ATOM   4696 N  N     . ALA A 1 580 ? 4.545   2.621   33.442  1   60.45  ? 581  ALA A N     1 1 
ATOM   4697 C  CA    . ALA A 1 580 ? 3.844   1.357   33.225  1   62.08  ? 581  ALA A CA    1 1 
ATOM   4698 C  C     . ALA A 1 580 ? 2.771   1.492   32.124  1   63.37  ? 581  ALA A C     1 1 
ATOM   4699 O  O     . ALA A 1 580 ? 2.594   0.58    31.315  1   63.8   ? 581  ALA A O     1 1 
ATOM   4700 C  CB    . ALA A 1 580 ? 3.199   0.892   34.522  1   62.3   ? 581  ALA A CB    1 1 
ATOM   4701 N  N     . GLY A 1 581 ? 2.067   2.62    32.115  1   63.67  ? 582  GLY A N     1 1 
ATOM   4702 C  CA    . GLY A 1 581 ? 1.026   2.891   31.132  1   64.37  ? 582  GLY A CA    1 1 
ATOM   4703 C  C     . GLY A 1 581 ? 1.584   3.27    29.777  1   64.89  ? 582  GLY A C     1 1 
ATOM   4704 O  O     . GLY A 1 581 ? 2.107   4.371   29.6    1   65.14  ? 582  GLY A O     1 1 
ATOM   4705 N  N     . ASN A 1 582 ? 0.422   6.677   28.208  1   41.26  ? 584  ASN A N     1 1 
ATOM   4706 C  CA    . ASN A 1 582 ? 0.084   7.796   27.324  1   41.48  ? 584  ASN A CA    1 1 
ATOM   4707 C  C     . ASN A 1 582 ? 0.521   9.129   27.924  1   40.97  ? 584  ASN A C     1 1 
ATOM   4708 O  O     . ASN A 1 582 ? 0.349   9.349   29.121  1   40.86  ? 584  ASN A O     1 1 
ATOM   4709 C  CB    . ASN A 1 582 ? -1.417  7.838   27.049  1   43.31  ? 584  ASN A CB    1 1 
ATOM   4710 C  CG    . ASN A 1 582 ? -1.928  6.756   26.138  1   47.56  ? 584  ASN A CG    1 1 
ATOM   4711 O  OD1   . ASN A 1 582 ? -1.166  6.071   25.435  1   49.02  ? 584  ASN A OD1   1 1 
ATOM   4712 N  ND2   . ASN A 1 582 ? -3.242  6.591   26.126  1   48.19  ? 584  ASN A ND2   1 1 
ATOM   4713 N  N     . TRP A 1 583 ? 1.057   10.029  27.088  1   40.5   ? 585  TRP A N     1 1 
ATOM   4714 C  CA    . TRP A 1 583 ? 1.496   11.345  27.55   1   40.69  ? 585  TRP A CA    1 1 
ATOM   4715 C  C     . TRP A 1 583 ? 0.307   12.262  27.842  1   41.18  ? 585  TRP A C     1 1 
ATOM   4716 O  O     . TRP A 1 583 ? -0.652  12.308  27.077  1   41.66  ? 585  TRP A O     1 1 
ATOM   4717 C  CB    . TRP A 1 583 ? 2.395   12.035  26.506  1   40.05  ? 585  TRP A CB    1 1 
ATOM   4718 C  CG    . TRP A 1 583 ? 3.765   11.45   26.343  1   39.89  ? 585  TRP A CG    1 1 
ATOM   4719 C  CD1   . TRP A 1 583 ? 4.219   10.722  25.286  1   40.58  ? 585  TRP A CD1   1 1 
ATOM   4720 C  CD2   . TRP A 1 583 ? 4.897   11.667  27.198  1   39.67  ? 585  TRP A CD2   1 1 
ATOM   4721 N  NE1   . TRP A 1 583 ? 5.554   10.439  25.444  1   40.92  ? 585  TRP A NE1   1 1 
ATOM   4722 C  CE2   . TRP A 1 583 ? 5.999   11.017  26.605  1   40.56  ? 585  TRP A CE2   1 1 
ATOM   4723 C  CE3   . TRP A 1 583 ? 5.085   12.34   28.41   1   39.93  ? 585  TRP A CE3   1 1 
ATOM   4724 C  CZ2   . TRP A 1 583 ? 7.269   11.017  27.187  1   40.8   ? 585  TRP A CZ2   1 1 
ATOM   4725 C  CZ3   . TRP A 1 583 ? 6.346   12.352  28.977  1   40.81  ? 585  TRP A CZ3   1 1 
ATOM   4726 C  CH2   . TRP A 1 583 ? 7.42    11.69   28.371  1   40.81  ? 585  TRP A CH2   1 1 
ATOM   4727 N  N     . GLU A 1 584 ? 0.394   13      28.936  1   40.79  ? 586  GLU A N     1 1 
ATOM   4728 C  CA    . GLU A 1 584 ? -0.58   13.99   29.376  1   40.98  ? 586  GLU A CA    1 1 
ATOM   4729 C  C     . GLU A 1 584 ? 0.184   15.289  29.663  1   41.37  ? 586  GLU A C     1 1 
ATOM   4730 O  O     . GLU A 1 584 ? 1.413   15.261  29.814  1   41.82  ? 586  GLU A O     1 1 
ATOM   4731 C  CB    . GLU A 1 584 ? -1.202  13.55   30.711  1   43.73  ? 586  GLU A CB    1 1 
ATOM   4732 C  CG    . GLU A 1 584 ? -1.906  12.215  30.705  1   51.93  ? 586  GLU A CG    1 1 
ATOM   4733 C  CD    . GLU A 1 584 ? -2.394  11.797  32.079  1   61.52  ? 586  GLU A CD    1 1 
ATOM   4734 O  OE1   . GLU A 1 584 ? -1.789  12.236  33.088  1   63.41  ? 586  GLU A OE1   1 1 
ATOM   4735 O  OE2   . GLU A 1 584 ? -3.375  11.018  32.147  1   63.87  ? 586  GLU A OE2   1 1 
ATOM   4736 N  N     . PHE A 1 585 ? -0.53   16.417  29.838  1   40.75  ? 587  PHE A N     1 1 
ATOM   4737 C  CA    . PHE A 1 585 ? 0.112   17.653  30.26   1   40.89  ? 587  PHE A CA    1 1 
ATOM   4738 C  C     . PHE A 1 585 ? 0.593   17.468  31.701  1   42.46  ? 587  PHE A C     1 1 
ATOM   4739 O  O     . PHE A 1 585 ? -0.02   16.721  32.471  1   42.18  ? 587  PHE A O     1 1 
ATOM   4740 C  CB    . PHE A 1 585 ? -0.861  18.815  30.217  1   39.94  ? 587  PHE A CB    1 1 
ATOM   4741 C  CG    . PHE A 1 585 ? -1.073  19.394  28.846  1   39.53  ? 587  PHE A CG    1 1 
ATOM   4742 C  CD1   . PHE A 1 585 ? 0.002   19.772  28.063  1   39.7   ? 587  PHE A CD1   1 1 
ATOM   4743 C  CD2   . PHE A 1 585 ? -2.349  19.629  28.368  1   39.15  ? 587  PHE A CD2   1 1 
ATOM   4744 C  CE1   . PHE A 1 585 ? -0.2    20.345  26.812  1   40.16  ? 587  PHE A CE1   1 1 
ATOM   4745 C  CE2   . PHE A 1 585 ? -2.545  20.212  27.128  1   39.53  ? 587  PHE A CE2   1 1 
ATOM   4746 C  CZ    . PHE A 1 585 ? -1.473  20.556  26.351  1   39.59  ? 587  PHE A CZ    1 1 
ATOM   4747 N  N     . GLY A 1 586 ? 1.702   18.122  32.044  1   43.54  ? 588  GLY A N     1 1 
ATOM   4748 C  CA    . GLY A 1 586 ? 2.27    18.056  33.381  1   45.14  ? 588  GLY A CA    1 1 
ATOM   4749 C  C     . GLY A 1 586 ? 1.298   18.562  34.422  1   47.01  ? 588  GLY A C     1 1 
ATOM   4750 O  O     . GLY A 1 586 ? 0.625   19.575  34.211  1   46.86  ? 588  GLY A O     1 1 
ATOM   4751 N  N     . ASN A 1 587 ? 1.188   17.832  35.518  1   48.76  ? 589  ASN A N     1 1 
ATOM   4752 C  CA    . ASN A 1 587 ? 0.236   18.124  36.571  1   51.12  ? 589  ASN A CA    1 1 
ATOM   4753 C  C     . ASN A 1 587 ? 0.919   18.597  37.862  1   52.58  ? 589  ASN A C     1 1 
ATOM   4754 O  O     . ASN A 1 587 ? 0.501   19.59   38.453  1   52.31  ? 589  ASN A O     1 1 
ATOM   4755 C  CB    . ASN A 1 587 ? -0.608  16.854  36.802  1   53.12  ? 589  ASN A CB    1 1 
ATOM   4756 C  CG    . ASN A 1 587 ? -1.642  16.931  37.889  1   57.82  ? 589  ASN A CG    1 1 
ATOM   4757 O  OD1   . ASN A 1 587 ? -2.362  17.93   38.04   1   59.83  ? 589  ASN A OD1   1 1 
ATOM   4758 N  ND2   . ASN A 1 587 ? -1.751  15.855  38.662  1   58.5   ? 589  ASN A ND2   1 1 
ATOM   4759 N  N     . LYS A 1 588 ? 1.963   17.879  38.299  1   53.9   ? 590  LYS A N     1 1 
ATOM   4760 C  CA    . LYS A 1 588 ? 2.676   18.181  39.539  1   55.23  ? 590  LYS A CA    1 1 
ATOM   4761 C  C     . LYS A 1 588 ? 4.073   18.74   39.294  1   55.83  ? 590  LYS A C     1 1 
ATOM   4762 O  O     . LYS A 1 588 ? 4.768   18.305  38.377  1   55.6   ? 590  LYS A O     1 1 
ATOM   4763 C  CB    . LYS A 1 588 ? 2.78    16.916  40.417  1   57.77  ? 590  LYS A CB    1 1 
ATOM   4764 C  CG    . LYS A 1 588 ? 1.438   16.374  40.903  1   63.14  ? 590  LYS A CG    1 1 
ATOM   4765 C  CD    . LYS A 1 588 ? 1.613   15.079  41.709  1   68.51  ? 590  LYS A CD    1 1 
ATOM   4766 C  CE    . LYS A 1 588 ? 0.302   14.36   41.971  1   72.09  ? 590  LYS A CE    1 1 
ATOM   4767 N  NZ    . LYS A 1 588 ? 0.512   13.024  42.601  1   73.75  ? 590  LYS A NZ    1 1 
ATOM   4768 N  N     . SER A 1 589 ? 4.492   19.69   40.138  1   56.26  ? 591  SER A N     1 1 
ATOM   4769 C  CA    . SER A 1 589 ? 5.824   20.287  40.072  1   56.73  ? 591  SER A CA    1 1 
ATOM   4770 C  C     . SER A 1 589 ? 6.811   19.425  40.841  1   57.37  ? 591  SER A C     1 1 
ATOM   4771 O  O     . SER A 1 589 ? 6.453   18.79   41.835  1   57.41  ? 591  SER A O     1 1 
ATOM   4772 C  CB    . SER A 1 589 ? 5.815   21.689  40.67   1   57.97  ? 591  SER A CB    1 1 
ATOM   4773 O  OG    . SER A 1 589 ? 5.921   22.69   39.671  1   59.94  ? 591  SER A OG    1 1 
ATOM   4774 N  N     . LEU A 1 590 ? 8.061   19.401  40.386  1   57.71  ? 592  LEU A N     1 1 
ATOM   4775 C  CA    . LEU A 1 590 ? 9.1     18.612  41.038  1   58.14  ? 592  LEU A CA    1 1 
ATOM   4776 C  C     . LEU A 1 590 ? 9.855   19.467  42.059  1   58.47  ? 592  LEU A C     1 1 
ATOM   4777 O  O     . LEU A 1 590 ? 9.859   20.697  41.965  1   58.65  ? 592  LEU A O     1 1 
ATOM   4778 C  CB    . LEU A 1 590 ? 10.061  18.037  39.991  1   58.4   ? 592  LEU A CB    1 1 
ATOM   4779 C  CG    . LEU A 1 590 ? 9.704   16.681  39.389  1   59.87  ? 592  LEU A CG    1 1 
ATOM   4780 C  CD1   . LEU A 1 590 ? 8.344   16.714  38.703  1   60.39  ? 592  LEU A CD1   1 1 
ATOM   4781 C  CD2   . LEU A 1 590 ? 10.794  16.214  38.422  1   60.2   ? 592  LEU A CD2   1 1 
ATOM   4782 N  N     . VAL A 1 591 ? 10.502  18.817  43.031  1   58.41  ? 593  VAL A N     1 1 
ATOM   4783 C  CA    . VAL A 1 591 ? 11.236  19.517  44.086  1   58.64  ? 593  VAL A CA    1 1 
ATOM   4784 C  C     . VAL A 1 591 ? 12.764  19.349  43.947  1   57.83  ? 593  VAL A C     1 1 
ATOM   4785 O  O     . VAL A 1 591 ? 13.27   18.223  44.005  1   57.85  ? 593  VAL A O     1 1 
ATOM   4786 C  CB    . VAL A 1 591 ? 10.689  19.063  45.464  1   60     ? 593  VAL A CB    1 1 
ATOM   4787 C  CG1   . VAL A 1 591 ? 11.639  19.416  46.603  1   61.05  ? 593  VAL A CG1   1 1 
ATOM   4788 C  CG2   . VAL A 1 591 ? 9.308   19.652  45.709  1   60.59  ? 593  VAL A CG2   1 1 
ATOM   4789 N  N     . PRO A 1 592 ? 13.51   20.465  43.778  1   56.74  ? 594  PRO A N     1 1 
ATOM   4790 C  CA    . PRO A 1 592 ? 14.971  20.362  43.602  1   55.99  ? 594  PRO A CA    1 1 
ATOM   4791 C  C     . PRO A 1 592 ? 15.753  19.712  44.762  1   54.84  ? 594  PRO A C     1 1 
ATOM   4792 O  O     . PRO A 1 592 ? 16.751  19.044  44.503  1   54.79  ? 594  PRO A O     1 1 
ATOM   4793 C  CB    . PRO A 1 592 ? 15.407  21.81   43.352  1   57     ? 594  PRO A CB    1 1 
ATOM   4794 C  CG    . PRO A 1 592 ? 14.296  22.65   43.893  1   57.54  ? 594  PRO A CG    1 1 
ATOM   4795 C  CD    . PRO A 1 592 ? 13.047  21.86   43.672  1   56.11  ? 594  PRO A CD    1 1 
ATOM   4796 N  N     . ASN A 1 593 ? 15.3    19.868  46.023  1   53.64  ? 595  ASN A N     1 1 
ATOM   4797 C  CA    . ASN A 1 593 ? 15.955  19.237  47.182  1   52.57  ? 595  ASN A CA    1 1 
ATOM   4798 C  C     . ASN A 1 593 ? 15.851  17.711  47.143  1   51.36  ? 595  ASN A C     1 1 
ATOM   4799 O  O     . ASN A 1 593 ? 16.605  17.044  47.841  1   51.91  ? 595  ASN A O     1 1 
ATOM   4800 C  CB    . ASN A 1 593 ? 15.425  19.81   48.515  1   53.52  ? 595  ASN A CB    1 1 
ATOM   4801 C  CG    . ASN A 1 593 ? 16.107  19.307  49.784  1   55.24  ? 595  ASN A CG    1 1 
ATOM   4802 O  OD1   . ASN A 1 593 ? 17.331  19.086  49.839  1   55.65  ? 595  ASN A OD1   1 1 
ATOM   4803 N  ND2   . ASN A 1 593 ? 15.313  19.128  50.842  1   55.12  ? 595  ASN A ND2   1 1 
ATOM   4804 N  N     . ASP A 1 594 ? 14.953  17.142  46.313  1   49.76  ? 596  ASP A N     1 1 
ATOM   4805 C  CA    . ASP A 1 594 ? 14.888  15.691  46.141  1   48.5   ? 596  ASP A CA    1 1 
ATOM   4806 C  C     . ASP A 1 594 ? 16.02   15.178  45.206  1   46.85  ? 596  ASP A C     1 1 
ATOM   4807 O  O     . ASP A 1 594 ? 16.087  13.976  44.969  1   47.39  ? 596  ASP A O     1 1 
ATOM   4808 C  CB    . ASP A 1 594 ? 13.522  15.269  45.562  1   49.99  ? 596  ASP A CB    1 1 
ATOM   4809 C  CG    . ASP A 1 594 ? 12.402  15.15   46.584  1   54.23  ? 596  ASP A CG    1 1 
ATOM   4810 O  OD1   . ASP A 1 594 ? 12.593  15.612  47.734  1   54.76  ? 596  ASP A OD1   1 1 
ATOM   4811 O  OD2   . ASP A 1 594 ? 11.331  14.592  46.233  1   55.99  ? 596  ASP A OD2   1 1 
ATOM   4812 N  N     . PHE A 1 595 ? 16.883  16.07   44.662  1   44.8   ? 597  PHE A N     1 1 
ATOM   4813 C  CA    . PHE A 1 595 ? 17.928  15.714  43.712  1   43.7   ? 597  PHE A CA    1 1 
ATOM   4814 C  C     . PHE A 1 595 ? 19.288  16.302  44.042  1   42.36  ? 597  PHE A C     1 1 
ATOM   4815 O  O     . PHE A 1 595 ? 19.382  17.39   44.61   1   42.42  ? 597  PHE A O     1 1 
ATOM   4816 C  CB    . PHE A 1 595 ? 17.54   16.207  42.305  1   43.6   ? 597  PHE A CB    1 1 
ATOM   4817 C  CG    . PHE A 1 595 ? 16.273  15.591  41.762  1   44.8   ? 597  PHE A CG    1 1 
ATOM   4818 C  CD1   . PHE A 1 595 ? 15.038  16.161  42.023  1   45.77  ? 597  PHE A CD1   1 1 
ATOM   4819 C  CD2   . PHE A 1 595 ? 16.317  14.447  40.989  1   45.6   ? 597  PHE A CD2   1 1 
ATOM   4820 C  CE1   . PHE A 1 595 ? 13.874  15.582  41.548  1   46.54  ? 597  PHE A CE1   1 1 
ATOM   4821 C  CE2   . PHE A 1 595 ? 15.152  13.88   40.502  1   46.42  ? 597  PHE A CE2   1 1 
ATOM   4822 C  CZ    . PHE A 1 595 ? 13.937  14.443  40.794  1   46.21  ? 597  PHE A CZ    1 1 
ATOM   4823 N  N     . ILE A 1 596 ? 20.347  15.602  43.617  1   40.87  ? 598  ILE A N     1 1 
ATOM   4824 C  CA    . ILE A 1 596 ? 21.719  16.09   43.715  1   39.81  ? 598  ILE A CA    1 1 
ATOM   4825 C  C     . ILE A 1 596 ? 22.041  16.64   42.319  1   38.53  ? 598  ILE A C     1 1 
ATOM   4826 O  O     . ILE A 1 596 ? 21.836  15.925  41.332  1   38.64  ? 598  ILE A O     1 1 
ATOM   4827 C  CB    . ILE A 1 596 ? 22.737  14.982  44.094  1   39.7   ? 598  ILE A CB    1 1 
ATOM   4828 C  CG1   . ILE A 1 596 ? 22.344  14.238  45.382  1   40.92  ? 598  ILE A CG1   1 1 
ATOM   4829 C  CG2   . ILE A 1 596 ? 24.135  15.562  44.183  1   39.74  ? 598  ILE A CG2   1 1 
ATOM   4830 C  CD1   . ILE A 1 596 ? 22.213  15.106  46.575  1   42.68  ? 598  ILE A CD1   1 1 
ATOM   4831 N  N     . LEU A 1 597 ? 22.493  17.898  42.223  1   36.67  ? 599  LEU A N     1 1 
ATOM   4832 C  CA    . LEU A 1 597 ? 22.833  18.462  40.925  1   35.68  ? 599  LEU A CA    1 1 
ATOM   4833 C  C     . LEU A 1 597 ? 24.34   18.682  40.806  1   34.92  ? 599  LEU A C     1 1 
ATOM   4834 O  O     . LEU A 1 597 ? 24.943  19.374  41.632  1   34.66  ? 599  LEU A O     1 1 
ATOM   4835 C  CB    . LEU A 1 597 ? 22.098  19.78   40.674  1   35.54  ? 599  LEU A CB    1 1 
ATOM   4836 C  CG    . LEU A 1 597 ? 20.581  19.781  40.793  1   37.12  ? 599  LEU A CG    1 1 
ATOM   4837 C  CD1   . LEU A 1 597 ? 20.031  21.152  40.483  1   37.46  ? 599  LEU A CD1   1 1 
ATOM   4838 C  CD2   . LEU A 1 597 ? 19.948  18.791  39.86   1   38.09  ? 599  LEU A CD2   1 1 
ATOM   4839 N  N     . LEU A 1 598 ? 24.947  18.099  39.773  1   34.15  ? 600  LEU A N     1 1 
ATOM   4840 C  CA    . LEU A 1 598 ? 26.366  18.286  39.509  1   33.59  ? 600  LEU A CA    1 1 
ATOM   4841 C  C     . LEU A 1 598 ? 26.561  18.77   38.084  1   32.31  ? 600  LEU A C     1 1 
ATOM   4842 O  O     . LEU A 1 598 ? 25.701  18.554  37.231  1   32.22  ? 600  LEU A O     1 1 
ATOM   4843 C  CB    . LEU A 1 598 ? 27.151  16.988  39.713  1   34.22  ? 600  LEU A CB    1 1 
ATOM   4844 C  CG    . LEU A 1 598 ? 27.248  16.434  41.128  1   36.01  ? 600  LEU A CG    1 1 
ATOM   4845 C  CD1   . LEU A 1 598 ? 28.065  15.166  41.128  1   36.63  ? 600  LEU A CD1   1 1 
ATOM   4846 C  CD2   . LEU A 1 598 ? 27.862  17.441  42.085  1   36.55  ? 600  LEU A CD2   1 1 
ATOM   4847 N  N     . SER A 1 599 ? 27.7    19.412  37.814  1   31.1   ? 601  SER A N     1 1 
ATOM   4848 C  CA    . SER A 1 599 ? 28.014  19.877  36.468  1   30.57  ? 601  SER A CA    1 1 
ATOM   4849 C  C     . SER A 1 599 ? 29.347  19.304  36.036  1   30.1   ? 601  SER A C     1 1 
ATOM   4850 O  O     . SER A 1 599 ? 30.179  18.933  36.872  1   30.99  ? 601  SER A O     1 1 
ATOM   4851 C  CB    . SER A 1 599 ? 28.048  21.398  36.407  1   31.68  ? 601  SER A CB    1 1 
ATOM   4852 O  OG    . SER A 1 599 ? 29.084  21.871  37.253  1   33.5   ? 601  SER A OG    1 1 
ATOM   4853 N  N     . ALA A 1 600 ? 29.564  19.225  34.726  1   28.81  ? 602  ALA A N     1 1 
ATOM   4854 C  CA    . ALA A 1 600 ? 30.807  18.678  34.186  1   27.34  ? 602  ALA A CA    1 1 
ATOM   4855 C  C     . ALA A 1 600 ? 31.17   19.341  32.88   1   26.09  ? 602  ALA A C     1 1 
ATOM   4856 O  O     . ALA A 1 600 ? 30.292  19.662  32.081  1   26.79  ? 602  ALA A O     1 1 
ATOM   4857 C  CB    . ALA A 1 600 ? 30.667  17.188  33.973  1   27.09  ? 602  ALA A CB    1 1 
ATOM   4858 N  N     . GLY A 1 601 ? 32.458  19.562  32.674  1   24.11  ? 603  GLY A N     1 1 
ATOM   4859 C  CA    . GLY A 1 601 ? 32.957  20.129  31.435  1   23.43  ? 603  GLY A CA    1 1 
ATOM   4860 C  C     . GLY A 1 601 ? 33.843  19.099  30.774  1   23.65  ? 603  GLY A C     1 1 
ATOM   4861 O  O     . GLY A 1 601 ? 34.729  18.542  31.427  1   23.73  ? 603  GLY A O     1 1 
ATOM   4862 N  N     . ALA A 1 602 ? 33.591  18.78   29.504  1   23.54  ? 604  ALA A N     1 1 
ATOM   4863 C  CA    . ALA A 1 602 ? 34.394  17.778  28.799  1   23.77  ? 604  ALA A CA    1 1 
ATOM   4864 C  C     . ALA A 1 602 ? 35.15   18.424  27.654  1   23.63  ? 604  ALA A C     1 1 
ATOM   4865 O  O     . ALA A 1 602 ? 34.644  19.348  27.02   1   23.51  ? 604  ALA A O     1 1 
ATOM   4866 C  CB    . ALA A 1 602 ? 33.496  16.666  28.277  1   24.18  ? 604  ALA A CB    1 1 
ATOM   4867 N  N     . PHE A 1 603 ? 36.352  17.936  27.375  1   23.79  ? 605  PHE A N     1 1 
ATOM   4868 C  CA    . PHE A 1 603 ? 37.197  18.53   26.335  1   24.07  ? 605  PHE A CA    1 1 
ATOM   4869 C  C     . PHE A 1 603 ? 38.303  17.589  25.915  1   24.4   ? 605  PHE A C     1 1 
ATOM   4870 O  O     . PHE A 1 603 ? 38.51   16.545  26.554  1   24.32  ? 605  PHE A O     1 1 
ATOM   4871 C  CB    . PHE A 1 603 ? 37.799  19.875  26.847  1   23.94  ? 605  PHE A CB    1 1 
ATOM   4872 C  CG    . PHE A 1 603 ? 38.485  19.732  28.191  1   24.29  ? 605  PHE A CG    1 1 
ATOM   4873 C  CD1   . PHE A 1 603 ? 39.756  19.189  28.287  1   24.52  ? 605  PHE A CD1   1 1 
ATOM   4874 C  CD2   . PHE A 1 603 ? 37.834  20.088  29.358  1   25.02  ? 605  PHE A CD2   1 1 
ATOM   4875 C  CE1   . PHE A 1 603 ? 40.365  19.022  29.519  1   25.15  ? 605  PHE A CE1   1 1 
ATOM   4876 C  CE2   . PHE A 1 603 ? 38.441  19.904  30.59   1   25.61  ? 605  PHE A CE2   1 1 
ATOM   4877 C  CZ    . PHE A 1 603 ? 39.71   19.389  30.661  1   25.34  ? 605  PHE A CZ    1 1 
ATOM   4878 N  N     . ILE A 1 604 ? 39.043  17.962  24.851  1   24.63  ? 606  ILE A N     1 1 
ATOM   4879 C  CA    . ILE A 1 604 ? 40.208  17.2    24.431  1   25.21  ? 606  ILE A CA    1 1 
ATOM   4880 C  C     . ILE A 1 604 ? 41.464  17.922  24.913  1   26.12  ? 606  ILE A C     1 1 
ATOM   4881 O  O     . ILE A 1 604 ? 41.655  19.113  24.626  1   25.65  ? 606  ILE A O     1 1 
ATOM   4882 C  CB    . ILE A 1 604 ? 40.247  16.924  22.911  1   25.61  ? 606  ILE A CB    1 1 
ATOM   4883 C  CG1   . ILE A 1 604 ? 39.184  15.887  22.521  1   27.51  ? 606  ILE A CG1   1 1 
ATOM   4884 C  CG2   . ILE A 1 604 ? 41.622  16.434  22.473  1   25.1   ? 606  ILE A CG2   1 1 
ATOM   4885 C  CD1   . ILE A 1 604 ? 38.905  15.841  21.057  1   29.21  ? 606  ILE A CD1   1 1 
ATOM   4886 N  N     . ASP A 1 605 ? 42.328  17.188  25.631  1   26.71  ? 607  ASP A N     1 1 
ATOM   4887 C  CA    . ASP A 1 605 ? 43.584  17.714  26.099  1   27.47  ? 607  ASP A CA    1 1 
ATOM   4888 C  C     . ASP A 1 605 ? 44.681  16.689  25.85   1   28.39  ? 607  ASP A C     1 1 
ATOM   4889 O  O     . ASP A 1 605 ? 44.584  15.553  26.32   1   28.87  ? 607  ASP A O     1 1 
ATOM   4890 C  CB    . ASP A 1 605 ? 43.531  18.075  27.583  1   29.34  ? 607  ASP A CB    1 1 
ATOM   4891 C  CG    . ASP A 1 605 ? 44.862  18.658  28.035  1   33.8   ? 607  ASP A CG    1 1 
ATOM   4892 O  OD1   . ASP A 1 605 ? 45.252  19.725  27.502  1   34.63  ? 607  ASP A OD1   1 1 
ATOM   4893 O  OD2   . ASP A 1 605 ? 45.54   18.018  28.887  1   35.05  ? 607  ASP A OD2   1 1 
ATOM   4894 N  N     . TYR A 1 606 ? 45.74   17.096  25.144  1   28.25  ? 608  TYR A N     1 1 
ATOM   4895 C  CA    . TYR A 1 606 ? 46.846  16.197  24.87   1   29.11  ? 608  TYR A CA    1 1 
ATOM   4896 C  C     . TYR A 1 606 ? 47.952  16.324  25.929  1   31.5   ? 608  TYR A C     1 1 
ATOM   4897 O  O     . TYR A 1 606 ? 49.081  16.678  25.607  1   32.08  ? 608  TYR A O     1 1 
ATOM   4898 C  CB    . TYR A 1 606 ? 47.354  16.419  23.452  1   27.78  ? 608  TYR A CB    1 1 
ATOM   4899 C  CG    . TYR A 1 606 ? 46.347  15.977  22.417  1   26.95  ? 608  TYR A CG    1 1 
ATOM   4900 C  CD1   . TYR A 1 606 ? 46.152  14.632  22.139  1   27.15  ? 608  TYR A CD1   1 1 
ATOM   4901 C  CD2   . TYR A 1 606 ? 45.591  16.903  21.711  1   26.71  ? 608  TYR A CD2   1 1 
ATOM   4902 C  CE1   . TYR A 1 606 ? 45.237  14.218  21.181  1   27.06  ? 608  TYR A CE1   1 1 
ATOM   4903 C  CE2   . TYR A 1 606 ? 44.716  16.504  20.706  1   26.83  ? 608  TYR A CE2   1 1 
ATOM   4904 C  CZ    . TYR A 1 606 ? 44.533  15.157  20.452  1   27.16  ? 608  TYR A CZ    1 1 
ATOM   4905 O  OH    . TYR A 1 606 ? 43.64   14.732  19.499  1   27.08  ? 608  TYR A OH    1 1 
ATOM   4906 N  N     . ASP A 1 607 ? 47.603  16.044  27.194  1   32.98  ? 609  ASP A N     1 1 
ATOM   4907 C  CA    . ASP A 1 607 ? 48.467  16.096  28.377  1   35.51  ? 609  ASP A CA    1 1 
ATOM   4908 C  C     . ASP A 1 607 ? 49.194  17.432  28.554  1   37.27  ? 609  ASP A C     1 1 
ATOM   4909 O  O     . ASP A 1 607 ? 50.321  17.464  29.038  1   37.96  ? 609  ASP A O     1 1 
ATOM   4910 C  CB    . ASP A 1 607 ? 49.443  14.912  28.417  1   38.51  ? 609  ASP A CB    1 1 
ATOM   4911 C  CG    . ASP A 1 607 ? 48.731  13.566  28.46   1   45.07  ? 609  ASP A CG    1 1 
ATOM   4912 O  OD1   . ASP A 1 607 ? 47.599  13.509  29.003  1   46.31  ? 609  ASP A OD1   1 1 
ATOM   4913 O  OD2   . ASP A 1 607 ? 49.302  12.571  27.948  1   48.25  ? 609  ASP A OD2   1 1 
ATOM   4914 N  N     . ASN A 1 608 ? 48.529  18.532  28.201  1   38.06  ? 610  ASN A N     1 1 
ATOM   4915 C  CA    . ASN A 1 608 ? 49.041  19.897  28.345  1   39.41  ? 610  ASN A CA    1 1 
ATOM   4916 C  C     . ASN A 1 608 ? 48.432  20.62   29.59   1   40.61  ? 610  ASN A C     1 1 
ATOM   4917 O  O     . ASN A 1 608 ? 48.422  21.847  29.65   1   40.73  ? 610  ASN A O     1 1 
ATOM   4918 C  CB    . ASN A 1 608 ? 48.747  20.692  27.072  1   40.16  ? 610  ASN A CB    1 1 
ATOM   4919 C  CG    . ASN A 1 608 ? 49.53   21.968  26.971  1   43.88  ? 610  ASN A CG    1 1 
ATOM   4920 O  OD1   . ASN A 1 608 ? 50.676  22.05   27.44   1   44.54  ? 610  ASN A OD1   1 1 
ATOM   4921 N  ND2   . ASN A 1 608 ? 48.926  22.993  26.364  1   44.94  ? 610  ASN A ND2   1 1 
ATOM   4922 N  N     . LEU A 1 609 ? 47.914  19.861  30.571  1   41.23  ? 611  LEU A N     1 1 
ATOM   4923 C  CA    . LEU A 1 609 ? 47.345  20.452  31.781  1   42.18  ? 611  LEU A CA    1 1 
ATOM   4924 C  C     . LEU A 1 609 ? 48.082  20.016  33.058  1   44.27  ? 611  LEU A C     1 1 
ATOM   4925 O  O     . LEU A 1 609 ? 48.161  18.827  33.369  1   44.62  ? 611  LEU A O     1 1 
ATOM   4926 C  CB    . LEU A 1 609 ? 45.833  20.166  31.904  1   41.54  ? 611  LEU A CB    1 1 
ATOM   4927 C  CG    . LEU A 1 609 ? 44.947  20.81   30.853  1   42.16  ? 611  LEU A CG    1 1 
ATOM   4928 C  CD1   . LEU A 1 609 ? 43.515  20.322  30.965  1   42.47  ? 611  LEU A CD1   1 1 
ATOM   4929 C  CD2   . LEU A 1 609 ? 45.018  22.336  30.899  1   42.68  ? 611  LEU A CD2   1 1 
ATOM   4930 N  N     . THR A 1 610 ? 48.615  20.981  33.795  1   45.54  ? 612  THR A N     1 1 
ATOM   4931 C  CA    . THR A 1 610 ? 49.284  20.734  35.071  1   47.54  ? 612  THR A CA    1 1 
ATOM   4932 C  C     . THR A 1 610 ? 48.225  20.748  36.22   1   49.25  ? 612  THR A C     1 1 
ATOM   4933 O  O     . THR A 1 610 ? 47.056  21.052  35.961  1   50.03  ? 612  THR A O     1 1 
ATOM   4934 C  CB    . THR A 1 610 ? 50.358  21.826  35.284  1   49.06  ? 612  THR A CB    1 1 
ATOM   4935 O  OG1   . THR A 1 610 ? 49.692  23.074  35.471  1   50.11  ? 612  THR A OG1   1 1 
ATOM   4936 C  CG2   . THR A 1 610 ? 51.348  21.918  34.126  1   49.14  ? 612  THR A CG2   1 1 
ATOM   4937 N  N     . GLU A 1 611 ? 48.626  20.471  37.489  1   49.57  ? 613  GLU A N     1 1 
ATOM   4938 C  CA    . GLU A 1 611 ? 47.699  20.531  38.63   1   50.19  ? 613  GLU A CA    1 1 
ATOM   4939 C  C     . GLU A 1 611 ? 47.132  21.959  38.762  1   49.68  ? 613  GLU A C     1 1 
ATOM   4940 O  O     . GLU A 1 611 ? 45.951  22.118  39.062  1   49.57  ? 613  GLU A O     1 1 
ATOM   4941 C  CB    . GLU A 1 611 ? 48.413  20.17   39.948  1   54.01  ? 613  GLU A CB    1 1 
ATOM   4942 C  CG    . GLU A 1 611 ? 49.121  18.825  39.969  1   61.79  ? 613  GLU A CG    1 1 
ATOM   4943 C  CD    . GLU A 1 611 ? 50.514  18.879  40.576  1   71.2   ? 613  GLU A CD    1 1 
ATOM   4944 O  OE1   . GLU A 1 611 ? 50.761  19.768  41.426  1   73.47  ? 613  GLU A OE1   1 1 
ATOM   4945 O  OE2   . GLU A 1 611 ? 51.366  18.049  40.183  1   73.53  ? 613  GLU A OE2   1 1 
ATOM   4946 N  N     . ASN A 1 612 ? 47.98   22.987  38.521  1   49.21  ? 614  ASN A N     1 1 
ATOM   4947 C  CA    . ASN A 1 612 ? 47.608  24.406  38.599  1   49.36  ? 614  ASN A CA    1 1 
ATOM   4948 C  C     . ASN A 1 612 ? 46.655  24.811  37.491  1   47.55  ? 614  ASN A C     1 1 
ATOM   4949 O  O     . ASN A 1 612 ? 45.778  25.643  37.711  1   47.63  ? 614  ASN A O     1 1 
ATOM   4950 C  CB    . ASN A 1 612 ? 48.845  25.31   38.577  1   52.5   ? 614  ASN A CB    1 1 
ATOM   4951 C  CG    . ASN A 1 612 ? 49.549  25.392  39.907  1   58.77  ? 614  ASN A CG    1 1 
ATOM   4952 O  OD1   . ASN A 1 612 ? 48.937  25.218  40.969  1   61.11  ? 614  ASN A OD1   1 1 
ATOM   4953 N  ND2   . ASN A 1 612 ? 50.858  25.64   39.878  1   59.92  ? 614  ASN A ND2   1 1 
ATOM   4954 N  N     . ASP A 1 613 ? 46.82   24.229  36.3    1   46.19  ? 615  ASP A N     1 1 
ATOM   4955 C  CA    . ASP A 1 613 ? 45.932  24.492  35.171  1   45.44  ? 615  ASP A CA    1 1 
ATOM   4956 C  C     . ASP A 1 613 ? 44.526  23.974  35.516  1   44     ? 615  ASP A C     1 1 
ATOM   4957 O  O     . ASP A 1 613 ? 43.558  24.71   35.379  1   43.18  ? 615  ASP A O     1 1 
ATOM   4958 C  CB    . ASP A 1 613 ? 46.461  23.823  33.889  1   47.04  ? 615  ASP A CB    1 1 
ATOM   4959 C  CG    . ASP A 1 613 ? 47.67   24.505  33.255  1   51.34  ? 615  ASP A CG    1 1 
ATOM   4960 O  OD1   . ASP A 1 613 ? 47.929  25.692  33.581  1   52.73  ? 615  ASP A OD1   1 1 
ATOM   4961 O  OD2   . ASP A 1 613 ? 48.358  23.851  32.433  1   51.96  ? 615  ASP A OD2   1 1 
ATOM   4962 N  N     . TYR A 1 614 ? 44.44   22.75   36.065  1   43.61  ? 616  TYR A N     1 1 
ATOM   4963 C  CA    . TYR A 1 614 ? 43.174  22.16   36.488  1   43.74  ? 616  TYR A CA    1 1 
ATOM   4964 C  C     . TYR A 1 614 ? 42.52   22.973  37.588  1   43.78  ? 616  TYR A C     1 1 
ATOM   4965 O  O     . TYR A 1 614 ? 41.308  23.183  37.546  1   43.87  ? 616  TYR A O     1 1 
ATOM   4966 C  CB    . TYR A 1 614 ? 43.37   20.725  36.961  1   43.68  ? 616  TYR A CB    1 1 
ATOM   4967 C  CG    . TYR A 1 614 ? 43.315  19.735  35.829  1   44.39  ? 616  TYR A CG    1 1 
ATOM   4968 C  CD1   . TYR A 1 614 ? 42.149  19.549  35.099  1   45.33  ? 616  TYR A CD1   1 1 
ATOM   4969 C  CD2   . TYR A 1 614 ? 44.427  18.988  35.482  1   45.13  ? 616  TYR A CD2   1 1 
ATOM   4970 C  CE1   . TYR A 1 614 ? 42.087  18.621  34.065  1   46.31  ? 616  TYR A CE1   1 1 
ATOM   4971 C  CE2   . TYR A 1 614 ? 44.378  18.059  34.453  1   46.21  ? 616  TYR A CE2   1 1 
ATOM   4972 C  CZ    . TYR A 1 614 ? 43.205  17.878  33.745  1   47.34  ? 616  TYR A CZ    1 1 
ATOM   4973 O  OH    . TYR A 1 614 ? 43.163  16.984  32.704  1   49.27  ? 616  TYR A OH    1 1 
ATOM   4974 N  N     . GLU A 1 615 ? 43.324  23.464  38.548  1   43.36  ? 617  GLU A N     1 1 
ATOM   4975 C  CA    . GLU A 1 615 ? 42.848  24.304  39.642  1   43.87  ? 617  GLU A CA    1 1 
ATOM   4976 C  C     . GLU A 1 615 ? 42.225  25.581  39.075  1   43.06  ? 617  GLU A C     1 1 
ATOM   4977 O  O     . GLU A 1 615 ? 41.147  25.968  39.505  1   42.95  ? 617  GLU A O     1 1 
ATOM   4978 C  CB    . GLU A 1 615 ? 44.006  24.641  40.599  1   47.65  ? 617  GLU A CB    1 1 
ATOM   4979 C  CG    . GLU A 1 615 ? 43.626  25.543  41.765  1   55.34  ? 617  GLU A CG    1 1 
ATOM   4980 C  CD    . GLU A 1 615 ? 44.742  25.801  42.765  1   64.93  ? 617  GLU A CD    1 1 
ATOM   4981 O  OE1   . GLU A 1 615 ? 44.582  26.716  43.607  1   67.07  ? 617  GLU A OE1   1 1 
ATOM   4982 O  OE2   . GLU A 1 615 ? 45.773  25.089  42.712  1   67.5   ? 617  GLU A OE2   1 1 
ATOM   4983 N  N     . LYS A 1 616 ? 42.866  26.18   38.06   1   42.59  ? 618  LYS A N     1 1 
ATOM   4984 C  CA    . LYS A 1 616 ? 42.39   27.394  37.397  1   42.88  ? 618  LYS A CA    1 1 
ATOM   4985 C  C     . LYS A 1 616 ? 41.098  27.141  36.624  1   41.91  ? 618  LYS A C     1 1 
ATOM   4986 O  O     . LYS A 1 616 ? 40.195  27.957  36.702  1   42.79  ? 618  LYS A O     1 1 
ATOM   4987 C  CB    . LYS A 1 616 ? 43.496  27.987  36.496  1   46.23  ? 618  LYS A CB    1 1 
ATOM   4988 C  CG    . LYS A 1 616 ? 43.082  29.192  35.643  1   51.99  ? 618  LYS A CG    1 1 
ATOM   4989 C  CD    . LYS A 1 616 ? 42.671  30.421  36.468  1   57.05  ? 618  LYS A CD    1 1 
ATOM   4990 C  CE    . LYS A 1 616 ? 42.543  31.655  35.597  1   60.81  ? 618  LYS A CE    1 1 
ATOM   4991 N  NZ    . LYS A 1 616 ? 41.742  32.73   36.25   1   63.06  ? 618  LYS A NZ    1 1 
ATOM   4992 N  N     . ILE A 1 617 ? 40.973  25.999  35.935  1   40.26  ? 619  ILE A N     1 1 
ATOM   4993 C  CA    . ILE A 1 617 ? 39.753  25.67   35.199  1   38.85  ? 619  ILE A CA    1 1 
ATOM   4994 C  C     . ILE A 1 617 ? 38.577  25.509  36.162  1   37.69  ? 619  ILE A C     1 1 
ATOM   4995 O  O     . ILE A 1 617 ? 37.498  26.011  35.878  1   38.41  ? 619  ILE A O     1 1 
ATOM   4996 C  CB    . ILE A 1 617 ? 39.945  24.438  34.276  1   39.22  ? 619  ILE A CB    1 1 
ATOM   4997 C  CG1   . ILE A 1 617 ? 41.085  24.673  33.274  1   40.2   ? 619  ILE A CG1   1 1 
ATOM   4998 C  CG2   . ILE A 1 617 ? 38.659  24.095  33.536  1   39.58  ? 619  ILE A CG2   1 1 
ATOM   4999 C  CD1   . ILE A 1 617 ? 41.537  23.435  32.55   1   41.7   ? 619  ILE A CD1   1 1 
ATOM   5000 N  N     . PHE A 1 618 ? 38.786  24.874  37.323  1   36.22  ? 620  PHE A N     1 1 
ATOM   5001 C  CA    . PHE A 1 618 ? 37.728  24.728  38.327  1   35.65  ? 620  PHE A CA    1 1 
ATOM   5002 C  C     . PHE A 1 618 ? 37.287  26.091  38.854  1   35.28  ? 620  PHE A C     1 1 
ATOM   5003 O  O     . PHE A 1 618 ? 36.089  26.328  39.024  1   35.15  ? 620  PHE A O     1 1 
ATOM   5004 C  CB    . PHE A 1 618 ? 38.195  23.864  39.502  1   35.72  ? 620  PHE A CB    1 1 
ATOM   5005 C  CG    . PHE A 1 618 ? 38.165  22.383  39.227  1   37.13  ? 620  PHE A CG    1 1 
ATOM   5006 C  CD1   . PHE A 1 618 ? 37.036  21.783  38.704  1   38.28  ? 620  PHE A CD1   1 1 
ATOM   5007 C  CD2   . PHE A 1 618 ? 39.252  21.587  39.518  1   38.25  ? 620  PHE A CD2   1 1 
ATOM   5008 C  CE1   . PHE A 1 618 ? 36.998  20.416  38.474  1   39.18  ? 620  PHE A CE1   1 1 
ATOM   5009 C  CE2   . PHE A 1 618 ? 39.22   20.221  39.26   1   39.28  ? 620  PHE A CE2   1 1 
ATOM   5010 C  CZ    . PHE A 1 618 ? 38.095  19.646  38.74   1   38.97  ? 620  PHE A CZ    1 1 
ATOM   5011 N  N     . GLU A 1 619 ? 38.258  26.996  39.102  1   34.25  ? 621  GLU A N     1 1 
ATOM   5012 C  CA    . GLU A 1 619 ? 37.952  28.32   39.596  1   33.78  ? 621  GLU A CA    1 1 
ATOM   5013 C  C     . GLU A 1 619 ? 37.177  29.113  38.557  1   33.77  ? 621  GLU A C     1 1 
ATOM   5014 O  O     . GLU A 1 619 ? 36.203  29.779  38.903  1   34.21  ? 621  GLU A O     1 1 
ATOM   5015 C  CB    . GLU A 1 619 ? 39.24   29.062  40.004  1   35.3   ? 621  GLU A CB    1 1 
ATOM   5016 N  N     . VAL A 1 620 ? 37.586  29.039  37.289  1   33.37  ? 622  VAL A N     1 1 
ATOM   5017 C  CA    . VAL A 1 620 ? 36.928  29.79   36.214  1   33.56  ? 622  VAL A CA    1 1 
ATOM   5018 C  C     . VAL A 1 620 ? 35.501  29.279  35.932  1   33.42  ? 622  VAL A C     1 1 
ATOM   5019 O  O     . VAL A 1 620 ? 34.55   30.07   35.895  1   33.37  ? 622  VAL A O     1 1 
ATOM   5020 C  CB    . VAL A 1 620 ? 37.802  29.772  34.922  1   34.59  ? 622  VAL A CB    1 1 
ATOM   5021 C  CG1   . VAL A 1 620 ? 37.027  30.275  33.704  1   35.7   ? 622  VAL A CG1   1 1 
ATOM   5022 C  CG2   . VAL A 1 620 ? 39.088  30.564  35.105  1   34.51  ? 622  VAL A CG2   1 1 
ATOM   5023 N  N     . THR A 1 621 ? 35.347  27.963  35.761  1   32.52  ? 623  THR A N     1 1 
ATOM   5024 C  CA    . THR A 1 621 ? 34.048  27.394  35.395  1   32.47  ? 623  THR A CA    1 1 
ATOM   5025 C  C     . THR A 1 621 ? 33.079  27.092  36.538  1   32.77  ? 623  THR A C     1 1 
ATOM   5026 O  O     . THR A 1 621 ? 31.863  27.199  36.367  1   33.21  ? 623  THR A O     1 1 
ATOM   5027 C  CB    . THR A 1 621 ? 34.279  26.12   34.58   1   32.7   ? 623  THR A CB    1 1 
ATOM   5028 O  OG1   . THR A 1 621 ? 34.883  25.134  35.423  1   33.36  ? 623  THR A OG1   1 1 
ATOM   5029 C  CG2   . THR A 1 621 ? 35.152  26.368  33.361  1   32.41  ? 623  THR A CG2   1 1 
ATOM   5030 N  N     . GLY A 1 622 ? 33.606  26.635  37.657  1   32.63  ? 624  GLY A N     1 1 
ATOM   5031 C  CA    . GLY A 1 622 ? 32.769  26.201  38.768  1   33.47  ? 624  GLY A CA    1 1 
ATOM   5032 C  C     . GLY A 1 622 ? 32.218  24.798  38.571  1   34.19  ? 624  GLY A C     1 1 
ATOM   5033 O  O     . GLY A 1 622 ? 31.309  24.383  39.295  1   34.46  ? 624  GLY A O     1 1 
ATOM   5034 N  N     . CYS A 1 623 ? 32.781  24.035  37.603  1   34.2   ? 625  CYS A N     1 1 
ATOM   5035 C  CA    . CYS A 1 623 ? 32.365  22.668  37.296  1   34.19  ? 625  CYS A CA    1 1 
ATOM   5036 C  C     . CYS A 1 623 ? 32.705  21.751  38.439  1   33.54  ? 625  CYS A C     1 1 
ATOM   5037 O  O     . CYS A 1 623 ? 33.773  21.895  39.018  1   34.22  ? 625  CYS A O     1 1 
ATOM   5038 C  CB    . CYS A 1 623 ? 33.026  22.183  36.009  1   35.47  ? 625  CYS A CB    1 1 
ATOM   5039 S  SG    . CYS A 1 623 ? 32.375  22.94   34.5    1   41.07  ? 625  CYS A SG    1 1 
ATOM   5040 N  N     . ASP A 1 624 ? 31.835  20.794  38.751  1   32.38  ? 626  ASP A N     1 1 
ATOM   5041 C  CA    . ASP A 1 624 ? 32.139  19.813  39.785  1   32.47  ? 626  ASP A CA    1 1 
ATOM   5042 C  C     . ASP A 1 624 ? 33.065  18.714  39.244  1   31.8   ? 626  ASP A C     1 1 
ATOM   5043 O  O     . ASP A 1 624 ? 33.737  18.047  40.025  1   32.01  ? 626  ASP A O     1 1 
ATOM   5044 C  CB    . ASP A 1 624 ? 30.862  19.161  40.316  1   35.39  ? 626  ASP A CB    1 1 
ATOM   5045 C  CG    . ASP A 1 624 ? 29.925  20.163  40.935  1   40.61  ? 626  ASP A CG    1 1 
ATOM   5046 O  OD1   . ASP A 1 624 ? 30.206  20.615  42.067  1   42.49  ? 626  ASP A OD1   1 1 
ATOM   5047 O  OD2   . ASP A 1 624 ? 28.929  20.52   40.279  1   41.68  ? 626  ASP A OD2   1 1 
ATOM   5048 N  N     . LEU A 1 625 ? 33.09   18.508  37.92   1   30.63  ? 627  LEU A N     1 1 
ATOM   5049 C  CA    . LEU A 1 625 ? 33.862  17.444  37.298  1   29.56  ? 627  LEU A CA    1 1 
ATOM   5050 C  C     . LEU A 1 625 ? 34.425  17.919  35.967  1   28.97  ? 627  LEU A C     1 1 
ATOM   5051 O  O     . LEU A 1 625 ? 33.733  18.597  35.228  1   29.85  ? 627  LEU A O     1 1 
ATOM   5052 C  CB    . LEU A 1 625 ? 32.908  16.245  37.051  1   28.71  ? 627  LEU A CB    1 1 
ATOM   5053 C  CG    . LEU A 1 625 ? 33.502  15.028  36.344  1   29.78  ? 627  LEU A CG    1 1 
ATOM   5054 C  CD1   . LEU A 1 625 ? 34.561  14.375  37.191  1   30.68  ? 627  LEU A CD1   1 1 
ATOM   5055 C  CD2   . LEU A 1 625 ? 32.455  14.018  36.025  1   30.63  ? 627  LEU A CD2   1 1 
ATOM   5056 N  N     . LEU A 1 626 ? 35.666  17.573  35.659  1   27.52  ? 628  LEU A N     1 1 
ATOM   5057 C  CA    . LEU A 1 626 ? 36.24   17.861  34.352  1   26.98  ? 628  LEU A CA    1 1 
ATOM   5058 C  C     . LEU A 1 626 ? 36.537  16.518  33.715  1   26.46  ? 628  LEU A C     1 1 
ATOM   5059 O  O     . LEU A 1 626 ? 36.998  15.601  34.393  1   26.83  ? 628  LEU A O     1 1 
ATOM   5060 C  CB    . LEU A 1 626 ? 37.506  18.728  34.446  1   26.95  ? 628  LEU A CB    1 1 
ATOM   5061 C  CG    . LEU A 1 626 ? 37.277  20.122  34.962  1   28.78  ? 628  LEU A CG    1 1 
ATOM   5062 C  CD1   . LEU A 1 626 ? 38.614  20.836  35.265  1   29.15  ? 628  LEU A CD1   1 1 
ATOM   5063 C  CD2   . LEU A 1 626 ? 36.387  20.927  34.008  1   29.6   ? 628  LEU A CD2   1 1 
ATOM   5064 N  N     . ILE A 1 627 ? 36.216  16.364  32.437  1   25.93  ? 629  ILE A N     1 1 
ATOM   5065 C  CA    . ILE A 1 627 ? 36.461  15.103  31.736  1   26     ? 629  ILE A CA    1 1 
ATOM   5066 C  C     . ILE A 1 627 ? 37.45   15.392  30.633  1   26.08  ? 629  ILE A C     1 1 
ATOM   5067 O  O     . ILE A 1 627 ? 37.097  16.021  29.632  1   26.24  ? 629  ILE A O     1 1 
ATOM   5068 C  CB    . ILE A 1 627 ? 35.165  14.465  31.206  1   26.46  ? 629  ILE A CB    1 1 
ATOM   5069 C  CG1   . ILE A 1 627 ? 34.086  14.383  32.32   1   27.95  ? 629  ILE A CG1   1 1 
ATOM   5070 C  CG2   . ILE A 1 627 ? 35.45   13.094  30.58   1   26.15  ? 629  ILE A CG2   1 1 
ATOM   5071 C  CD1   . ILE A 1 627 ? 32.694  13.898  31.853  1   29.59  ? 629  ILE A CD1   1 1 
ATOM   5072 N  N     . ALA A 1 628 ? 38.713  15.031  30.86   1   25.5   ? 630  ALA A N     1 1 
ATOM   5073 C  CA    . ALA A 1 628 ? 39.751  15.284  29.875  1   25.87  ? 630  ALA A CA    1 1 
ATOM   5074 C  C     . ALA A 1 628 ? 39.922  14.04   29.028  1   26.35  ? 630  ALA A C     1 1 
ATOM   5075 O  O     . ALA A 1 628 ? 40.177  12.962  29.542  1   26.94  ? 630  ALA A O     1 1 
ATOM   5076 C  CB    . ALA A 1 628 ? 41.047  15.667  30.557  1   25.5   ? 630  ALA A CB    1 1 
ATOM   5077 N  N     . ILE A 1 629 ? 39.758  14.192  27.733  1   26.58  ? 631  ILE A N     1 1 
ATOM   5078 C  CA    . ILE A 1 629 ? 39.79   13.098  26.781  1   27.93  ? 631  ILE A CA    1 1 
ATOM   5079 C  C     . ILE A 1 629 ? 40.96   13.284  25.804  1   28.17  ? 631  ILE A C     1 1 
ATOM   5080 O  O     . ILE A 1 629 ? 41.307  14.404  25.458  1   28.06  ? 631  ILE A O     1 1 
ATOM   5081 C  CB    . ILE A 1 629 ? 38.397  13.168  26.058  1   29.5   ? 631  ILE A CB    1 1 
ATOM   5082 C  CG1   . ILE A 1 629 ? 37.269  12.78   26.986  1   31.29  ? 631  ILE A CG1   1 1 
ATOM   5083 C  CG2   . ILE A 1 629 ? 38.317  12.414  24.757  1   30.17  ? 631  ILE A CG2   1 1 
ATOM   5084 C  CD1   . ILE A 1 629 ? 35.939  13.299  26.516  1   33.88  ? 631  ILE A CD1   1 1 
ATOM   5085 N  N     . LYS A 1 630 ? 41.577  12.192  25.379  1   28.13  ? 632  LYS A N     1 1 
ATOM   5086 C  CA    . LYS A 1 630 ? 42.604  12.219  24.352  1   28.04  ? 632  LYS A CA    1 1 
ATOM   5087 C  C     . LYS A 1 630 ? 42.62   10.897  23.627  1   27.26  ? 632  LYS A C     1 1 
ATOM   5088 O  O     . LYS A 1 630 ? 42.443  9.849   24.243  1   27     ? 632  LYS A O     1 1 
ATOM   5089 C  CB    . LYS A 1 630 ? 43.998  12.581  24.878  1   30.34  ? 632  LYS A CB    1 1 
ATOM   5090 C  CG    . LYS A 1 630 ? 44.556  11.633  25.904  1   35.77  ? 632  LYS A CG    1 1 
ATOM   5091 C  CD    . LYS A 1 630 ? 46.053  11.826  26.037  1   42.72  ? 632  LYS A CD    1 1 
ATOM   5092 C  CE    . LYS A 1 630 ? 46.583  10.904  27.101  1   48.74  ? 632  LYS A CE    1 1 
ATOM   5093 N  NZ    . LYS A 1 630 ? 45.856  11.122  28.389  1   52.31  ? 632  LYS A NZ    1 1 
ATOM   5094 N  N     . ASN A 1 631 ? 42.782  10.942  22.309  1   27.03  ? 633  ASN A N     1 1 
ATOM   5095 C  CA    . ASN A 1 631 ? 42.886  9.722   21.522  1   27.25  ? 633  ASN A CA    1 1 
ATOM   5096 C  C     . ASN A 1 631 ? 44.323  9.259   21.49   1   29.6   ? 633  ASN A C     1 1 
ATOM   5097 O  O     . ASN A 1 631 ? 45.258  10.064  21.471  1   30     ? 633  ASN A O     1 1 
ATOM   5098 C  CB    . ASN A 1 631 ? 42.425  9.938   20.092  1   26.17  ? 633  ASN A CB    1 1 
ATOM   5099 C  CG    . ASN A 1 631 ? 43.14   11.079  19.418  1   24.96  ? 633  ASN A CG    1 1 
ATOM   5100 O  OD1   . ASN A 1 631 ? 42.99   12.221  19.821  1   25.02  ? 633  ASN A OD1   1 1 
ATOM   5101 N  ND2   . ASN A 1 631 ? 43.924  10.781  18.397  1   22.61  ? 633  ASN A ND2   1 1 
ATOM   5102 N  N     . GLN A 1 632 ? 44.483  7.952   21.457  1   30.98  ? 634  GLN A N     1 1 
ATOM   5103 C  CA    . GLN A 1 632 ? 45.744  7.247   21.306  1   33     ? 634  GLN A CA    1 1 
ATOM   5104 C  C     . GLN A 1 632 ? 45.58   6.61    19.912  1   34.44  ? 634  GLN A C     1 1 
ATOM   5105 O  O     . GLN A 1 632 ? 44.516  6.033   19.646  1   35.27  ? 634  GLN A O     1 1 
ATOM   5106 C  CB    . GLN A 1 632 ? 45.832  6.175   22.408  1   35.05  ? 634  GLN A CB    1 1 
ATOM   5107 C  CG    . GLN A 1 632 ? 46.953  5.177   22.254  1   38.64  ? 634  GLN A CG    1 1 
ATOM   5108 C  CD    . GLN A 1 632 ? 46.831  4.118   23.317  1   42.61  ? 634  GLN A CD    1 1 
ATOM   5109 O  OE1   . GLN A 1 632 ? 47.143  4.349   24.489  1   44.75  ? 634  GLN A OE1   1 1 
ATOM   5110 N  NE2   . GLN A 1 632 ? 46.348  2.944   22.936  1   41.91  ? 634  GLN A NE2   1 1 
ATOM   5111 N  N     . ASN A 1 633 ? 46.573  6.74    19.006  1   34.41  ? 635  ASN A N     1 1 
ATOM   5112 C  CA    . ASN A 1 633 ? 46.399  6.216   17.643  1   35.25  ? 635  ASN A CA    1 1 
ATOM   5113 C  C     . ASN A 1 633 ? 46.836  4.759   17.413  1   37.6   ? 635  ASN A C     1 1 
ATOM   5114 O  O     . ASN A 1 633 ? 46.264  4.096   16.532  1   38.24  ? 635  ASN A O     1 1 
ATOM   5115 C  CB    . ASN A 1 633 ? 47.038  7.13    16.623  1   34.86  ? 635  ASN A CB    1 1 
ATOM   5116 C  CG    . ASN A 1 633 ? 46.242  8.419   16.47   1   35.84  ? 635  ASN A CG    1 1 
ATOM   5117 O  OD1   . ASN A 1 633 ? 45.017  8.462   16.689  1   35.75  ? 635  ASN A OD1   1 1 
ATOM   5118 N  ND2   . ASN A 1 633 ? 46.91   9.495   16.091  1   35.51  ? 635  ASN A ND2   1 1 
ATOM   5119 N  N     . ASN A 1 634 ? 47.803  4.236   18.183  1   38.74  ? 636  ASN A N     1 1 
ATOM   5120 C  CA    . ASN A 1 634 ? 48.245  2.835   17.979  1   40.09  ? 636  ASN A CA    1 1 
ATOM   5121 C  C     . ASN A 1 634 ? 48.346  2.045   19.294  1   39.98  ? 636  ASN A C     1 1 
ATOM   5122 O  O     . ASN A 1 634 ? 49.34   2.175   20.003  1   40.24  ? 636  ASN A O     1 1 
ATOM   5123 C  CB    . ASN A 1 634 ? 49.601  2.783   17.249  1   42.56  ? 636  ASN A CB    1 1 
ATOM   5124 C  CG    . ASN A 1 634 ? 49.714  3.706   16.051  1   48.27  ? 636  ASN A CG    1 1 
ATOM   5125 O  OD1   . ASN A 1 634 ? 49.21   3.417   14.956  1   50.31  ? 636  ASN A OD1   1 1 
ATOM   5126 N  ND2   . ASN A 1 634 ? 50.369  4.853   16.237  1   49.38  ? 636  ASN A ND2   1 1 
ATOM   5127 N  N     . PRO A 1 635 ? 47.361  1.196   19.631  1   39.6   ? 637  PRO A N     1 1 
ATOM   5128 C  CA    . PRO A 1 635 ? 46.094  0.972   18.915  1   39.26  ? 637  PRO A CA    1 1 
ATOM   5129 C  C     . PRO A 1 635 ? 45.07   2.082   19.234  1   38.82  ? 637  PRO A C     1 1 
ATOM   5130 O  O     . PRO A 1 635 ? 45.178  2.732   20.284  1   38.55  ? 637  PRO A O     1 1 
ATOM   5131 C  CB    . PRO A 1 635 ? 45.656  -0.396  19.446  1   40.02  ? 637  PRO A CB    1 1 
ATOM   5132 C  CG    . PRO A 1 635 ? 46.142  -0.402  20.878  1   40.46  ? 637  PRO A CG    1 1 
ATOM   5133 C  CD    . PRO A 1 635 ? 47.414  0.426   20.895  1   39.07  ? 637  PRO A CD    1 1 
ATOM   5134 N  N     . GLN A 1 636 ? 44.108  2.331   18.327  1   38.17  ? 638  GLN A N     1 1 
ATOM   5135 C  CA    . GLN A 1 636 ? 43.105  3.378   18.534  1   37.96  ? 638  GLN A CA    1 1 
ATOM   5136 C  C     . GLN A 1 636 ? 42.343  3.19    19.853  1   36.57  ? 638  GLN A C     1 1 
ATOM   5137 O  O     . GLN A 1 636 ? 41.714  2.157   20.067  1   36.88  ? 638  GLN A O     1 1 
ATOM   5138 C  CB    . GLN A 1 636 ? 42.115  3.433   17.356  1   40.34  ? 638  GLN A CB    1 1 
ATOM   5139 C  CG    . GLN A 1 636 ? 42.564  4.236   16.136  1   44.53  ? 638  GLN A CG    1 1 
ATOM   5140 C  CD    . GLN A 1 636 ? 41.476  4.162   15.083  1   50.99  ? 638  GLN A CD    1 1 
ATOM   5141 O  OE1   . GLN A 1 636 ? 41.039  3.075   14.667  1   52.86  ? 638  GLN A OE1   1 1 
ATOM   5142 N  NE2   . GLN A 1 636 ? 40.982  5.313   14.655  1   52.17  ? 638  GLN A NE2   1 1 
ATOM   5143 N  N     . LYS A 1 637 ? 42.466  4.152   20.755  1   35     ? 639  LYS A N     1 1 
ATOM   5144 C  CA    . LYS A 1 637 ? 41.759  4.106   22.036  1   34.1   ? 639  LYS A CA    1 1 
ATOM   5145 C  C     . LYS A 1 637 ? 41.454  5.534   22.506  1   31.54  ? 639  LYS A C     1 1 
ATOM   5146 O  O     . LYS A 1 637 ? 42.192  6.459   22.192  1   31.21  ? 639  LYS A O     1 1 
ATOM   5147 C  CB    . LYS A 1 637 ? 42.617  3.416   23.113  1   36.8   ? 639  LYS A CB    1 1 
ATOM   5148 C  CG    . LYS A 1 637 ? 42.374  1.921   23.276  1   42.29  ? 639  LYS A CG    1 1 
ATOM   5149 C  CD    . LYS A 1 637 ? 43.422  1.294   24.198  1   48.15  ? 639  LYS A CD    1 1 
ATOM   5150 C  CE    . LYS A 1 637 ? 42.858  0.87    25.535  1   52.79  ? 639  LYS A CE    1 1 
ATOM   5151 N  NZ    . LYS A 1 637 ? 42.306  -0.508  25.491  1   55.7   ? 639  LYS A NZ    1 1 
ATOM   5152 N  N     . TRP A 1 638 ? 40.399  5.699   23.293  1   29.36  ? 640  TRP A N     1 1 
ATOM   5153 C  CA    . TRP A 1 638 ? 40.076  6.982   23.876  1   27.44  ? 640  TRP A CA    1 1 
ATOM   5154 C  C     . TRP A 1 638 ? 40.503  6.873   25.317  1   26.63  ? 640  TRP A C     1 1 
ATOM   5155 O  O     . TRP A 1 638 ? 39.999  6.009   26.037  1   27     ? 640  TRP A O     1 1 
ATOM   5156 C  CB    . TRP A 1 638 ? 38.567  7.278   23.793  1   26.3   ? 640  TRP A CB    1 1 
ATOM   5157 C  CG    . TRP A 1 638 ? 38.098  7.823   22.474  1   25.54  ? 640  TRP A CG    1 1 
ATOM   5158 C  CD1   . TRP A 1 638 ? 37.241  7.226   21.596  1   25.89  ? 640  TRP A CD1   1 1 
ATOM   5159 C  CD2   . TRP A 1 638 ? 38.433  9.096   21.903  1   24.91  ? 640  TRP A CD2   1 1 
ATOM   5160 N  NE1   . TRP A 1 638 ? 37.045  8.039   20.502  1   25.67  ? 640  TRP A NE1   1 1 
ATOM   5161 C  CE2   . TRP A 1 638 ? 37.751  9.198   20.674  1   25.25  ? 640  TRP A CE2   1 1 
ATOM   5162 C  CE3   . TRP A 1 638 ? 39.269  10.15   22.296  1   25.25  ? 640  TRP A CE3   1 1 
ATOM   5163 C  CZ2   . TRP A 1 638 ? 37.875  10.314  19.842  1   25.51  ? 640  TRP A CZ2   1 1 
ATOM   5164 C  CZ3   . TRP A 1 638 ? 39.354  11.271  21.493  1   25.58  ? 640  TRP A CZ3   1 1 
ATOM   5165 C  CH2   . TRP A 1 638 ? 38.668  11.341  20.277  1   25.48  ? 640  TRP A CH2   1 1 
ATOM   5166 N  N     . VAL A 1 639 ? 41.447  7.7     25.731  1   25.82  ? 641  VAL A N     1 1 
ATOM   5167 C  CA    . VAL A 1 639 ? 41.931  7.723   27.1    1   26.26  ? 641  VAL A CA    1 1 
ATOM   5168 C  C     . VAL A 1 639 ? 41.166  8.818   27.842  1   26.65  ? 641  VAL A C     1 1 
ATOM   5169 O  O     . VAL A 1 639 ? 41.176  9.983   27.441  1   26.12  ? 641  VAL A O     1 1 
ATOM   5170 C  CB    . VAL A 1 639 ? 43.466  7.902   27.169  1   27.13  ? 641  VAL A CB    1 1 
ATOM   5171 C  CG1   . VAL A 1 639 ? 43.951  7.991   28.617  1   27.51  ? 641  VAL A CG1   1 1 
ATOM   5172 C  CG2   . VAL A 1 639 ? 44.178  6.77    26.418  1   27.34  ? 641  VAL A CG2   1 1 
ATOM   5173 N  N     . ILE A 1 640 ? 40.449  8.418   28.894  1   27.07  ? 642  ILE A N     1 1 
ATOM   5174 C  CA    . ILE A 1 640 ? 39.595  9.312   29.655  1   27.94  ? 642  ILE A CA    1 1 
ATOM   5175 C  C     . ILE A 1 640 ? 40.133  9.566   31.047  1   30.01  ? 642  ILE A C     1 1 
ATOM   5176 O  O     . ILE A 1 640 ? 40.39   8.612   31.782  1   31.1   ? 642  ILE A O     1 1 
ATOM   5177 C  CB    . ILE A 1 640 ? 38.137  8.785   29.743  1   27.36  ? 642  ILE A CB    1 1 
ATOM   5178 C  CG1   . ILE A 1 640 ? 37.643  8.153   28.421  1   27.89  ? 642  ILE A CG1   1 1 
ATOM   5179 C  CG2   . ILE A 1 640 ? 37.201  9.887   30.24   1   27.26  ? 642  ILE A CG2   1 1 
ATOM   5180 C  CD1   . ILE A 1 640 ? 37.455  9.075   27.292  1   29.05  ? 642  ILE A CD1   1 1 
ATOM   5181 N  N     . LYS A 1 641 ? 40.23   10.845  31.432  1   30.62  ? 643  LYS A N     1 1 
ATOM   5182 C  CA    . LYS A 1 641 ? 40.691  11.264  32.746  1   32.46  ? 643  LYS A CA    1 1 
ATOM   5183 C  C     . LYS A 1 641 ? 39.578  12.037  33.437  1   33.19  ? 643  LYS A C     1 1 
ATOM   5184 O  O     . LYS A 1 641 ? 39.145  13.067  32.93   1   33.58  ? 643  LYS A O     1 1 
ATOM   5185 C  CB    . LYS A 1 641 ? 41.941  12.147  32.606  1   35.41  ? 643  LYS A CB    1 1 
ATOM   5186 C  CG    . LYS A 1 641 ? 42.604  12.516  33.931  1   41.15  ? 643  LYS A CG    1 1 
ATOM   5187 C  CD    . LYS A 1 641 ? 43.895  13.301  33.705  1   46.27  ? 643  LYS A CD    1 1 
ATOM   5188 C  CE    . LYS A 1 641 ? 44.638  13.548  34.997  1   51.15  ? 643  LYS A CE    1 1 
ATOM   5189 N  NZ    . LYS A 1 641 ? 45.9    14.331  34.791  1   53.39  ? 643  LYS A NZ    1 1 
ATOM   5190 N  N     . PHE A 1 642 ? 39.064  11.521  34.557  1   33.54  ? 644  PHE A N     1 1 
ATOM   5191 C  CA    . PHE A 1 642 ? 37.978  12.182  35.28   1   34.21  ? 644  PHE A CA    1 1 
ATOM   5192 C  C     . PHE A 1 642 ? 38.576  12.959  36.436  1   34.83  ? 644  PHE A C     1 1 
ATOM   5193 O  O     . PHE A 1 642 ? 39.203  12.365  37.301  1   35.27  ? 644  PHE A O     1 1 
ATOM   5194 C  CB    . PHE A 1 642 ? 36.975  11.147  35.807  1   34.46  ? 644  PHE A CB    1 1 
ATOM   5195 C  CG    . PHE A 1 642 ? 36.159  10.449  34.743  1   35.4   ? 644  PHE A CG    1 1 
ATOM   5196 C  CD1   . PHE A 1 642 ? 35.063  11.067  34.171  1   36.23  ? 644  PHE A CD1   1 1 
ATOM   5197 C  CD2   . PHE A 1 642 ? 36.483  9.169   34.324  1   36.15  ? 644  PHE A CD2   1 1 
ATOM   5198 C  CE1   . PHE A 1 642 ? 34.317  10.428  33.192  1   36.92  ? 644  PHE A CE1   1 1 
ATOM   5199 C  CE2   . PHE A 1 642 ? 35.737  8.535   33.341  1   36.82  ? 644  PHE A CE2   1 1 
ATOM   5200 C  CZ    . PHE A 1 642 ? 34.659  9.17    32.782  1   36.66  ? 644  PHE A CZ    1 1 
ATOM   5201 N  N     . LYS A 1 643 ? 38.431  14.277  36.44   1   34.83  ? 645  LYS A N     1 1 
ATOM   5202 C  CA    . LYS A 1 643 ? 38.992  15.123  37.486  1   35.54  ? 645  LYS A CA    1 1 
ATOM   5203 C  C     . LYS A 1 643 ? 37.899  15.708  38.361  1   35.78  ? 645  LYS A C     1 1 
ATOM   5204 O  O     . LYS A 1 643 ? 37.226  16.668  37.962  1   35.83  ? 645  LYS A O     1 1 
ATOM   5205 C  CB    . LYS A 1 643 ? 39.819  16.25   36.861  1   38.25  ? 645  LYS A CB    1 1 
ATOM   5206 C  CG    . LYS A 1 643 ? 41.265  15.871  36.589  1   44.95  ? 645  LYS A CG    1 1 
ATOM   5207 C  CD    . LYS A 1 643 ? 42.12   16.042  37.846  1   51     ? 645  LYS A CD    1 1 
ATOM   5208 C  CE    . LYS A 1 643 ? 43.596  16.103  37.567  1   55.74  ? 645  LYS A CE    1 1 
ATOM   5209 N  NZ    . LYS A 1 643 ? 44.378  16.188  38.828  1   58.83  ? 645  LYS A NZ    1 1 
ATOM   5210 N  N     . PRO A 1 644 ? 37.679  15.141  39.557  1   35.4   ? 646  PRO A N     1 1 
ATOM   5211 C  CA    . PRO A 1 644 ? 36.637  15.696  40.435  1   35.62  ? 646  PRO A CA    1 1 
ATOM   5212 C  C     . PRO A 1 644 ? 37.094  16.946  41.204  1   36.64  ? 646  PRO A C     1 1 
ATOM   5213 O  O     . PRO A 1 644 ? 38.273  17.078  41.566  1   36.71  ? 646  PRO A O     1 1 
ATOM   5214 C  CB    . PRO A 1 644 ? 36.314  14.534  41.375  1   35.94  ? 646  PRO A CB    1 1 
ATOM   5215 C  CG    . PRO A 1 644 ? 37.546  13.708  41.414  1   36.1   ? 646  PRO A CG    1 1 
ATOM   5216 C  CD    . PRO A 1 644 ? 38.362  13.987  40.169  1   34.59  ? 646  PRO A CD    1 1 
ATOM   5217 N  N     . LYS A 1 645 ? 36.17   17.863  41.437  1   37.13  ? 647  LYS A N     1 1 
ATOM   5218 C  CA    . LYS A 1 645 ? 36.463  19.069  42.196  1   38.82  ? 647  LYS A CA    1 1 
ATOM   5219 C  C     . LYS A 1 645 ? 36.313  18.795  43.686  1   40.59  ? 647  LYS A C     1 1 
ATOM   5220 O  O     . LYS A 1 645 ? 37.072  19.343  44.495  1   40.72  ? 647  LYS A O     1 1 
ATOM   5221 C  CB    . LYS A 1 645 ? 35.518  20.23   41.799  1   40.21  ? 647  LYS A CB    1 1 
ATOM   5222 C  CG    . LYS A 1 645 ? 35.886  21.555  42.458  1   43.73  ? 647  LYS A CG    1 1 
ATOM   5223 C  CD    . LYS A 1 645 ? 34.957  22.7    42.095  1   49.21  ? 647  LYS A CD    1 1 
ATOM   5224 C  CE    . LYS A 1 645 ? 33.55   22.449  42.582  1   54.9   ? 647  LYS A CE    1 1 
ATOM   5225 N  NZ    . LYS A 1 645 ? 32.674  23.632  42.372  1   58.75  ? 647  LYS A NZ    1 1 
ATOM   5226 N  N     . ASN A 1 646 ? 35.322  17.961  44.049  1   41.38  ? 648  ASN A N     1 1 
ATOM   5227 C  CA    . ASN A 1 646 ? 34.948  17.692  45.427  1   42.62  ? 648  ASN A CA    1 1 
ATOM   5228 C  C     . ASN A 1 646 ? 34.677  16.206  45.693  1   43.82  ? 648  ASN A C     1 1 
ATOM   5229 O  O     . ASN A 1 646 ? 34.796  15.387  44.778  1   44.45  ? 648  ASN A O     1 1 
ATOM   5230 C  CB    . ASN A 1 646 ? 33.725  18.573  45.787  1   43.57  ? 648  ASN A CB    1 1 
ATOM   5231 C  CG    . ASN A 1 646 ? 32.601  18.508  44.769  1   46.88  ? 648  ASN A CG    1 1 
ATOM   5232 O  OD1   . ASN A 1 646 ? 32.233  17.441  44.281  1   48.47  ? 648  ASN A OD1   1 1 
ATOM   5233 N  ND2   . ASN A 1 646 ? 32.039  19.654  44.411  1   47.12  ? 648  ASN A ND2   1 1 
ATOM   5234 N  N     . THR A 1 647 ? 34.312  15.858  46.951  1   43.9   ? 649  THR A N     1 1 
ATOM   5235 C  CA    . THR A 1 647 ? 34.026  14.486  47.376  1   44.27  ? 649  THR A CA    1 1 
ATOM   5236 C  C     . THR A 1 647 ? 32.791  13.88   46.721  1   43.66  ? 649  THR A C     1 1 
ATOM   5237 O  O     . THR A 1 647 ? 32.764  12.671  46.511  1   43.77  ? 649  THR A O     1 1 
ATOM   5238 C  CB    . THR A 1 647 ? 33.941  14.405  48.903  1   46.21  ? 649  THR A CB    1 1 
ATOM   5239 O  OG1   . THR A 1 647 ? 32.95   15.329  49.368  1   47.64  ? 649  THR A OG1   1 1 
ATOM   5240 C  CG2   . THR A 1 647 ? 35.283  14.676  49.575  1   46.38  ? 649  THR A CG2   1 1 
ATOM   5241 N  N     . ILE A 1 648 ? 31.774  14.694  46.396  1   43.03  ? 650  ILE A N     1 1 
ATOM   5242 C  CA    . ILE A 1 648 ? 30.576  14.179  45.736  1   42.76  ? 650  ILE A CA    1 1 
ATOM   5243 C  C     . ILE A 1 648 ? 30.917  13.743  44.317  1   40.97  ? 650  ILE A C     1 1 
ATOM   5244 O  O     . ILE A 1 648 ? 30.592  12.624  43.927  1   40.76  ? 650  ILE A O     1 1 
ATOM   5245 C  CB    . ILE A 1 648 ? 29.408  15.189  45.802  1   44.33  ? 650  ILE A CB    1 1 
ATOM   5246 C  CG1   . ILE A 1 648 ? 28.87   15.288  47.244  1   46.08  ? 650  ILE A CG1   1 1 
ATOM   5247 C  CG2   . ILE A 1 648 ? 28.277  14.812  44.831  1   44.92  ? 650  ILE A CG2   1 1 
ATOM   5248 C  CD1   . ILE A 1 648 ? 28.222  13.984  47.789  1   47.75  ? 650  ILE A CD1   1 1 
ATOM   5249 N  N     . ALA A 1 649 ? 31.632  14.591  43.572  1   39.75  ? 651  ALA A N     1 1 
ATOM   5250 C  CA    . ALA A 1 649 ? 32.061  14.242  42.222  1   39.12  ? 651  ALA A CA    1 1 
ATOM   5251 C  C     . ALA A 1 649 ? 33.017  13.041  42.22   1   38.82  ? 651  ALA A C     1 1 
ATOM   5252 O  O     . ALA A 1 649 ? 32.987  12.252  41.283  1   38.21  ? 651  ALA A O     1 1 
ATOM   5253 C  CB    . ALA A 1 649 ? 32.71   15.428  41.552  1   38.88  ? 651  ALA A CB    1 1 
ATOM   5254 N  N     . GLU A 1 650 ? 33.804  12.859  43.293  1   38.9   ? 652  GLU A N     1 1 
ATOM   5255 C  CA    . GLU A 1 650 ? 34.7    11.719  43.424  1   39.48  ? 652  GLU A CA    1 1 
ATOM   5256 C  C     . GLU A 1 650 ? 33.896  10.419  43.532  1   39.02  ? 652  GLU A C     1 1 
ATOM   5257 O  O     . GLU A 1 650 ? 34.272  9.416   42.921  1   39.1   ? 652  GLU A O     1 1 
ATOM   5258 C  CB    . GLU A 1 650 ? 35.62   11.897  44.635  1   42.87  ? 652  GLU A CB    1 1 
ATOM   5259 C  CG    . GLU A 1 650 ? 36.655  10.792  44.772  1   49.57  ? 652  GLU A CG    1 1 
ATOM   5260 C  CD    . GLU A 1 650 ? 37.795  11.097  45.725  1   58.2   ? 652  GLU A CD    1 1 
ATOM   5261 O  OE1   . GLU A 1 650 ? 37.734  12.136  46.426  1   59.02  ? 652  GLU A OE1   1 1 
ATOM   5262 O  OE2   . GLU A 1 650 ? 38.762  10.299  45.755  1   60.93  ? 652  GLU A OE2   1 1 
ATOM   5263 N  N     . LYS A 1 651 ? 32.762  10.45   44.258  1   38.17  ? 653  LYS A N     1 1 
ATOM   5264 C  CA    . LYS A 1 651 ? 31.878  9.285   44.377  1   38.16  ? 653  LYS A CA    1 1 
ATOM   5265 C  C     . LYS A 1 651 ? 31.295  8.93    43.002  1   37.35  ? 653  LYS A C     1 1 
ATOM   5266 O  O     . LYS A 1 651 ? 31.194  7.745   42.674  1   37.74  ? 653  LYS A O     1 1 
ATOM   5267 C  CB    . LYS A 1 651 ? 30.765  9.532   45.412  1   40.42  ? 653  LYS A CB    1 1 
ATOM   5268 C  CG    . LYS A 1 651 ? 31.284  9.577   46.839  1   45.07  ? 653  LYS A CG    1 1 
ATOM   5269 C  CD    . LYS A 1 651 ? 30.185  9.391   47.866  1   50.47  ? 653  LYS A CD    1 1 
ATOM   5270 C  CE    . LYS A 1 651 ? 30.688  8.648   49.088  1   55.14  ? 653  LYS A CE    1 1 
ATOM   5271 N  NZ    . LYS A 1 651 ? 29.726  8.729   50.225  1   57.82  ? 653  LYS A NZ    1 1 
ATOM   5272 N  N     . LEU A 1 652 ? 30.959  9.96    42.183  1   35.93  ? 654  LEU A N     1 1 
ATOM   5273 C  CA    . LEU A 1 652 ? 30.469  9.765   40.822  1   35.01  ? 654  LEU A CA    1 1 
ATOM   5274 C  C     . LEU A 1 652 ? 31.554  9.099   39.961  1   35.07  ? 654  LEU A C     1 1 
ATOM   5275 O  O     . LEU A 1 652 ? 31.248  8.153   39.238  1   35.46  ? 654  LEU A O     1 1 
ATOM   5276 C  CB    . LEU A 1 652 ? 30.039  11.097  40.195  1   34.39  ? 654  LEU A CB    1 1 
ATOM   5277 C  CG    . LEU A 1 652 ? 29.653  11.067  38.715  1   35.27  ? 654  LEU A CG    1 1 
ATOM   5278 C  CD1   . LEU A 1 652 ? 28.511  10.101  38.458  1   35.6   ? 654  LEU A CD1   1 1 
ATOM   5279 C  CD2   . LEU A 1 652 ? 29.237  12.443  38.241  1   36.11  ? 654  LEU A CD2   1 1 
ATOM   5280 N  N     . VAL A 1 653 ? 32.807  9.567   40.054  1   34.32  ? 655  VAL A N     1 1 
ATOM   5281 C  CA    . VAL A 1 653 ? 33.931  9.005   39.313  1   34.9   ? 655  VAL A CA    1 1 
ATOM   5282 C  C     . VAL A 1 653 ? 34.12   7.526   39.648  1   35.42  ? 655  VAL A C     1 1 
ATOM   5283 O  O     . VAL A 1 653 ? 34.179  6.701   38.736  1   35.46  ? 655  VAL A O     1 1 
ATOM   5284 C  CB    . VAL A 1 653 ? 35.22   9.819   39.547  1   35.33  ? 655  VAL A CB    1 1 
ATOM   5285 C  CG1   . VAL A 1 653 ? 36.439  9.102   38.973  1   35.65  ? 655  VAL A CG1   1 1 
ATOM   5286 C  CG2   . VAL A 1 653 ? 35.084  11.216  38.95   1   35.62  ? 655  VAL A CG2   1 1 
ATOM   5287 N  N     . ASN A 1 654 ? 34.136  7.182   40.947  1   35.52  ? 656  ASN A N     1 1 
ATOM   5288 C  CA    . ASN A 1 654 ? 34.256  5.786   41.367  1   35.98  ? 656  ASN A CA    1 1 
ATOM   5289 C  C     . ASN A 1 654 ? 33.091  4.946   40.853  1   36.03  ? 656  ASN A C     1 1 
ATOM   5290 O  O     . ASN A 1 654 ? 33.294  3.776   40.526  1   36.8   ? 656  ASN A O     1 1 
ATOM   5291 C  CB    . ASN A 1 654 ? 34.345  5.656   42.878  1   37.42  ? 656  ASN A CB    1 1 
ATOM   5292 C  CG    . ASN A 1 654 ? 35.561  6.281   43.468  1   41.31  ? 656  ASN A CG    1 1 
ATOM   5293 O  OD1   . ASN A 1 654 ? 36.566  6.494   42.788  1   43.69  ? 656  ASN A OD1   1 1 
ATOM   5294 N  ND2   . ASN A 1 654 ? 35.487  6.612   44.751  1   41.91  ? 656  ASN A ND2   1 1 
ATOM   5295 N  N     . TYR A 1 655 ? 31.883  5.531   40.771  1   35.05  ? 657  TYR A N     1 1 
ATOM   5296 C  CA    . TYR A 1 655 ? 30.695  4.84    40.263  1   34.75  ? 657  TYR A CA    1 1 
ATOM   5297 C  C     . TYR A 1 655 ? 30.845  4.529   38.766  1   35.68  ? 657  TYR A C     1 1 
ATOM   5298 O  O     . TYR A 1 655 ? 30.481  3.431   38.327  1   35.84  ? 657  TYR A O     1 1 
ATOM   5299 C  CB    . TYR A 1 655 ? 29.418  5.677   40.524  1   33.42  ? 657  TYR A CB    1 1 
ATOM   5300 C  CG    . TYR A 1 655 ? 28.176  5.159   39.834  1   32.79  ? 657  TYR A CG    1 1 
ATOM   5301 C  CD1   . TYR A 1 655 ? 27.358  4.216   40.442  1   33.11  ? 657  TYR A CD1   1 1 
ATOM   5302 C  CD2   . TYR A 1 655 ? 27.791  5.647   38.592  1   33.09  ? 657  TYR A CD2   1 1 
ATOM   5303 C  CE1   . TYR A 1 655 ? 26.217  3.736   39.812  1   33.34  ? 657  TYR A CE1   1 1 
ATOM   5304 C  CE2   . TYR A 1 655 ? 26.668  5.157   37.941  1   33.36  ? 657  TYR A CE2   1 1 
ATOM   5305 C  CZ    . TYR A 1 655 ? 25.888  4.193   38.55   1   33.82  ? 657  TYR A CZ    1 1 
ATOM   5306 O  OH    . TYR A 1 655 ? 24.772  3.722   37.903  1   34.21  ? 657  TYR A OH    1 1 
ATOM   5307 N  N     . ILE A 1 656 ? 31.324  5.515   37.983  1   35.97  ? 658  ILE A N     1 1 
ATOM   5308 C  CA    . ILE A 1 656 ? 31.532  5.374   36.54   1   36.76  ? 658  ILE A CA    1 1 
ATOM   5309 C  C     . ILE A 1 656 ? 32.548  4.259   36.289  1   38.01  ? 658  ILE A C     1 1 
ATOM   5310 O  O     . ILE A 1 656 ? 32.301  3.381   35.467  1   37.82  ? 658  ILE A O     1 1 
ATOM   5311 C  CB    . ILE A 1 656 ? 31.978  6.722   35.915  1   36.65  ? 658  ILE A CB    1 1 
ATOM   5312 C  CG1   . ILE A 1 656 ? 30.856  7.754   35.975  1   36.85  ? 658  ILE A CG1   1 1 
ATOM   5313 C  CG2   . ILE A 1 656 ? 32.481  6.545   34.482  1   37.02  ? 658  ILE A CG2   1 1 
ATOM   5314 C  CD1   . ILE A 1 656 ? 31.353  9.19    35.66   1   37.78  ? 658  ILE A CD1   1 1 
ATOM   5315 N  N     . LYS A 1 657 ? 33.653  4.27    37.054  1   39.11  ? 659  LYS A N     1 1 
ATOM   5316 C  CA    . LYS A 1 657 ? 34.712  3.264   37.007  1   40.71  ? 659  LYS A CA    1 1 
ATOM   5317 C  C     . LYS A 1 657 ? 34.178  1.864   37.303  1   42.52  ? 659  LYS A C     1 1 
ATOM   5318 O  O     . LYS A 1 657 ? 34.483  0.927   36.566  1   43.74  ? 659  LYS A O     1 1 
ATOM   5319 C  CB    . LYS A 1 657 ? 35.83   3.633   37.991  1   42.49  ? 659  LYS A CB    1 1 
ATOM   5320 C  CG    . LYS A 1 657 ? 36.904  4.505   37.362  1   46.48  ? 659  LYS A CG    1 1 
ATOM   5321 C  CD    . LYS A 1 657 ? 37.374  5.602   38.288  1   51.36  ? 659  LYS A CD    1 1 
ATOM   5322 C  CE    . LYS A 1 657 ? 38.611  5.256   39.07   1   55.28  ? 659  LYS A CE    1 1 
ATOM   5323 N  NZ    . LYS A 1 657 ? 39.433  6.475   39.341  1   57.49  ? 659  LYS A NZ    1 1 
ATOM   5324 N  N     . LEU A 1 658 ? 33.356  1.722   38.349  1   42.83  ? 660  LEU A N     1 1 
ATOM   5325 C  CA    . LEU A 1 658 ? 32.78   0.437   38.73   1   43.98  ? 660  LEU A CA    1 1 
ATOM   5326 C  C     . LEU A 1 658 ? 31.804  -0.096  37.691  1   43.86  ? 660  LEU A C     1 1 
ATOM   5327 O  O     . LEU A 1 658 ? 31.724  -1.3    37.485  1   43.95  ? 660  LEU A O     1 1 
ATOM   5328 C  CB    . LEU A 1 658 ? 32.08   0.558   40.093  1   45.15  ? 660  LEU A CB    1 1 
ATOM   5329 C  CG    . LEU A 1 658 ? 32.765  -0.151  41.262  1   47.87  ? 660  LEU A CG    1 1 
ATOM   5330 C  CD1   . LEU A 1 658 ? 34.194  0.372   41.476  1   48.91  ? 660  LEU A CD1   1 1 
ATOM   5331 C  CD2   . LEU A 1 658 ? 31.953  -0.01   42.538  1   48.75  ? 660  LEU A CD2   1 1 
ATOM   5332 N  N     . ASN A 1 659 ? 31.059  0.795   37.041  1   43.66  ? 661  ASN A N     1 1 
ATOM   5333 C  CA    . ASN A 1 659 ? 30.064  0.398   36.051  1   43.69  ? 661  ASN A CA    1 1 
ATOM   5334 C  C     . ASN A 1 659 ? 30.519  0.531   34.612  1   42.55  ? 661  ASN A C     1 1 
ATOM   5335 O  O     . ASN A 1 659 ? 29.668  0.509   33.721  1   42.33  ? 661  ASN A O     1 1 
ATOM   5336 C  CB    . ASN A 1 659 ? 28.782  1.173   36.265  1   46.04  ? 661  ASN A CB    1 1 
ATOM   5337 C  CG    . ASN A 1 659 ? 28.107  0.77    37.545  1   50.91  ? 661  ASN A CG    1 1 
ATOM   5338 O  OD1   . ASN A 1 659 ? 28.236  1.441   38.579  1   52.11  ? 661  ASN A OD1   1 1 
ATOM   5339 N  ND2   . ASN A 1 659 ? 27.409  -0.367  37.506  1   52.07  ? 661  ASN A ND2   1 1 
ATOM   5340 N  N     . PHE A 1 660 ? 31.848  0.681   34.371  1   41.43  ? 662  PHE A N     1 1 
ATOM   5341 C  CA    . PHE A 1 660 ? 32.392  0.785   33.015  1   40.89  ? 662  PHE A CA    1 1 
ATOM   5342 C  C     . PHE A 1 660 ? 32.554  -0.633  32.459  1   41.2   ? 662  PHE A C     1 1 
ATOM   5343 O  O     . PHE A 1 660 ? 33.666  -1.105  32.217  1   41.09  ? 662  PHE A O     1 1 
ATOM   5344 C  CB    . PHE A 1 660 ? 33.734  1.535   32.991  1   40.08  ? 662  PHE A CB    1 1 
ATOM   5345 C  CG    . PHE A 1 660 ? 33.971  2.258   31.685  1   39.68  ? 662  PHE A CG    1 1 
ATOM   5346 C  CD1   . PHE A 1 660 ? 33.493  3.542   31.488  1   39.67  ? 662  PHE A CD1   1 1 
ATOM   5347 C  CD2   . PHE A 1 660 ? 34.635  1.638   30.638  1   39.82  ? 662  PHE A CD2   1 1 
ATOM   5348 C  CE1   . PHE A 1 660 ? 33.682  4.195   30.276  1   40.04  ? 662  PHE A CE1   1 1 
ATOM   5349 C  CE2   . PHE A 1 660 ? 34.816  2.293   29.424  1   40.26  ? 662  PHE A CE2   1 1 
ATOM   5350 C  CZ    . PHE A 1 660 ? 34.328  3.565   29.248  1   39.91  ? 662  PHE A CZ    1 1 
ATOM   5351 N  N     . LYS A 1 661 ? 31.426  -1.311  32.308  1   41.06  ? 663  LYS A N     1 1 
ATOM   5352 C  CA    . LYS A 1 661 ? 31.317  -2.684  31.841  1   41.85  ? 663  LYS A CA    1 1 
ATOM   5353 C  C     . LYS A 1 661 ? 30.048  -2.78   30.976  1   41     ? 663  LYS A C     1 1 
ATOM   5354 O  O     . LYS A 1 661 ? 29.105  -2.021  31.196  1   41.13  ? 663  LYS A O     1 1 
ATOM   5355 C  CB    . LYS A 1 661 ? 31.204  -3.623  33.064  1   45.09  ? 663  LYS A CB    1 1 
ATOM   5356 C  CG    . LYS A 1 661 ? 31.377  -5.1    32.743  1   51.41  ? 663  LYS A CG    1 1 
ATOM   5357 C  CD    . LYS A 1 661 ? 30.444  -5.97   33.577  1   57.35  ? 663  LYS A CD    1 1 
ATOM   5358 C  CE    . LYS A 1 661 ? 30.588  -7.434  33.238  1   61.77  ? 663  LYS A CE    1 1 
ATOM   5359 N  NZ    . LYS A 1 661 ? 29.633  -8.27   34.017  1   64.54  ? 663  LYS A NZ    1 1 
ATOM   5360 N  N     . SER A 1 662 ? 30.027  -3.684  29.985  1   40.31  ? 664  SER A N     1 1 
ATOM   5361 C  CA    . SER A 1 662 ? 28.859  -3.836  29.124  1   40.35  ? 664  SER A CA    1 1 
ATOM   5362 C  C     . SER A 1 662 ? 28.855  -5.129  28.338  1   40.68  ? 664  SER A C     1 1 
ATOM   5363 O  O     . SER A 1 662 ? 29.883  -5.547  27.821  1   40.77  ? 664  SER A O     1 1 
ATOM   5364 C  CB    . SER A 1 662 ? 28.741  -2.666  28.152  1   41.08  ? 664  SER A CB    1 1 
ATOM   5365 O  OG    . SER A 1 662 ? 27.544  -2.731  27.393  1   42.7   ? 664  SER A OG    1 1 
ATOM   5366 N  N     . ASN A 1 663 ? 27.676  -5.725  28.19   1   40.75  ? 665  ASN A N     1 1 
ATOM   5367 C  CA    . ASN A 1 663 ? 27.49   -6.913  27.357  1   41.2   ? 665  ASN A CA    1 1 
ATOM   5368 C  C     . ASN A 1 663 ? 27.268  -6.528  25.881  1   39.98  ? 665  ASN A C     1 1 
ATOM   5369 O  O     . ASN A 1 663 ? 27.553  -7.329  24.99   1   40.75  ? 665  ASN A O     1 1 
ATOM   5370 C  CB    . ASN A 1 663 ? 26.307  -7.737  27.863  1   43.69  ? 665  ASN A CB    1 1 
ATOM   5371 C  CG    . ASN A 1 663 ? 26.621  -8.463  29.142  1   48.6   ? 665  ASN A CG    1 1 
ATOM   5372 O  OD1   . ASN A 1 663 ? 27.776  -8.867  29.394  1   50.11  ? 665  ASN A OD1   1 1 
ATOM   5373 N  ND2   . ASN A 1 663 ? 25.601  -8.635  29.98   1   49.62  ? 665  ASN A ND2   1 1 
ATOM   5374 N  N     . ILE A 1 664 ? 26.77   -5.309  25.631  1   38.09  ? 666  ILE A N     1 1 
ATOM   5375 C  CA    . ILE A 1 664 ? 26.505  -4.769  24.306  1   36.91  ? 666  ILE A CA    1 1 
ATOM   5376 C  C     . ILE A 1 664 ? 27.705  -3.941  23.755  1   34.89  ? 666  ILE A C     1 1 
ATOM   5377 O  O     . ILE A 1 664 ? 28.18   -4.205  22.645  1   34.29  ? 666  ILE A O     1 1 
ATOM   5378 C  CB    . ILE A 1 664 ? 25.218  -3.926  24.386  1   37.58  ? 666  ILE A CB    1 1 
ATOM   5379 C  CG1   . ILE A 1 664 ? 24.024  -4.778  24.886  1   39.13  ? 666  ILE A CG1   1 1 
ATOM   5380 C  CG2   . ILE A 1 664 ? 24.931  -3.246  23.06   1   38.19  ? 666  ILE A CG2   1 1 
ATOM   5381 C  CD1   . ILE A 1 664 ? 22.891  -3.946  25.598  1   40.71  ? 666  ILE A CD1   1 1 
ATOM   5382 N  N     . PHE A 1 665 ? 28.188  -2.952  24.538  1   33.34  ? 667  PHE A N     1 1 
ATOM   5383 C  CA    . PHE A 1 665 ? 29.252  -2.047  24.112  1   32.45  ? 667  PHE A CA    1 1 
ATOM   5384 C  C     . PHE A 1 665 ? 30.65   -2.608  24.335  1   32.41  ? 667  PHE A C     1 1 
ATOM   5385 O  O     . PHE A 1 665 ? 30.964  -3.134  25.407  1   32.72  ? 667  PHE A O     1 1 
ATOM   5386 C  CB    . PHE A 1 665 ? 29.118  -0.659  24.789  1   31.72  ? 667  PHE A CB    1 1 
ATOM   5387 C  CG    . PHE A 1 665 ? 29.589  0.485   23.919  1   31.85  ? 667  PHE A CG    1 1 
ATOM   5388 C  CD1   . PHE A 1 665 ? 30.937  0.765   23.781  1   32.83  ? 667  PHE A CD1   1 1 
ATOM   5389 C  CD2   . PHE A 1 665 ? 28.686  1.268   23.226  1   32.28  ? 667  PHE A CD2   1 1 
ATOM   5390 C  CE1   . PHE A 1 665 ? 31.371  1.786   22.943  1   33.4   ? 667  PHE A CE1   1 1 
ATOM   5391 C  CE2   . PHE A 1 665 ? 29.12   2.282   22.384  1   32.94  ? 667  PHE A CE2   1 1 
ATOM   5392 C  CZ    . PHE A 1 665 ? 30.457  2.542   22.255  1   33.03  ? 667  PHE A CZ    1 1 
ATOM   5393 N  N     . ASP A 1 666 ? 31.505  -2.464  23.325  1   31.78  ? 668  ASP A N     1 1 
ATOM   5394 C  CA    . ASP A 1 666 ? 32.887  -2.89   23.412  1   31.74  ? 668  ASP A CA    1 1 
ATOM   5395 C  C     . ASP A 1 666 ? 33.652  -1.809  24.16   1   32.06  ? 668  ASP A C     1 1 
ATOM   5396 O  O     . ASP A 1 666 ? 34.11   -0.842  23.54   1   32.11  ? 668  ASP A O     1 1 
ATOM   5397 C  CB    . ASP A 1 666 ? 33.452  -3.041  22      1   33.07  ? 668  ASP A CB    1 1 
ATOM   5398 C  CG    . ASP A 1 666 ? 34.827  -3.654  21.937  1   37.59  ? 668  ASP A CG    1 1 
ATOM   5399 O  OD1   . ASP A 1 666 ? 35.547  -3.61   22.956  1   36.82  ? 668  ASP A OD1   1 1 
ATOM   5400 O  OD2   . ASP A 1 666 ? 35.177  -4.196  20.876  1   41.71  ? 668  ASP A OD2   1 1 
ATOM   5401 N  N     . THR A 1 667 ? 33.794  -1.961  25.488  1   32.33  ? 669  THR A N     1 1 
ATOM   5402 C  CA    . THR A 1 667 ? 34.525  -0.985  26.308  1   33.32  ? 669  THR A CA    1 1 
ATOM   5403 C  C     . THR A 1 667 ? 36.042  -1.001  26.119  1   34.08  ? 669  THR A C     1 1 
ATOM   5404 O  O     . THR A 1 667 ? 36.729  -0.12   26.646  1   34.88  ? 669  THR A O     1 1 
ATOM   5405 C  CB    . THR A 1 667 ? 34.163  -1.147  27.784  1   34.97  ? 669  THR A CB    1 1 
ATOM   5406 O  OG1   . THR A 1 667 ? 34.692  -2.381  28.287  1   35.79  ? 669  THR A OG1   1 1 
ATOM   5407 C  CG2   . THR A 1 667 ? 32.668  -1.065  28.023  1   35.01  ? 669  THR A CG2   1 1 
ATOM   5408 N  N     . GLY A 1 668 ? 36.554  -1.967  25.36   1   33.93  ? 670  GLY A N     1 1 
ATOM   5409 C  CA    . GLY A 1 668 ? 37.974  -2.108  25.06   1   34.36  ? 670  GLY A CA    1 1 
ATOM   5410 C  C     . GLY A 1 668 ? 38.557  -0.968  24.246  1   34.76  ? 670  GLY A C     1 1 
ATOM   5411 O  O     . GLY A 1 668 ? 39.772  -0.797  24.193  1   35.08  ? 670  GLY A O     1 1 
ATOM   5412 N  N     . PHE A 1 669 ? 37.704  -0.178  23.606  1   34.77  ? 671  PHE A N     1 1 
ATOM   5413 C  CA    . PHE A 1 669 ? 38.14   0.986   22.846  1   35.73  ? 671  PHE A CA    1 1 
ATOM   5414 C  C     . PHE A 1 669 ? 38.429  2.211   23.776  1   35.99  ? 671  PHE A C     1 1 
ATOM   5415 O  O     . PHE A 1 669 ? 38.853  3.252   23.297  1   35.93  ? 671  PHE A O     1 1 
ATOM   5416 C  CB    . PHE A 1 669 ? 37.073  1.333   21.801  1   36.15  ? 671  PHE A CB    1 1 
ATOM   5417 C  CG    . PHE A 1 669 ? 37.612  1.952   20.536  1   36.98  ? 671  PHE A CG    1 1 
ATOM   5418 C  CD1   . PHE A 1 669 ? 38.019  1.159   19.477  1   37.82  ? 671  PHE A CD1   1 1 
ATOM   5419 C  CD2   . PHE A 1 669 ? 37.643  3.325   20.378  1   37.81  ? 671  PHE A CD2   1 1 
ATOM   5420 C  CE1   . PHE A 1 669 ? 38.494  1.735   18.302  1   38.57  ? 671  PHE A CE1   1 1 
ATOM   5421 C  CE2   . PHE A 1 669 ? 38.113  3.896   19.207  1   38.45  ? 671  PHE A CE2   1 1 
ATOM   5422 C  CZ    . PHE A 1 669 ? 38.542  3.101   18.178  1   38.15  ? 671  PHE A CZ    1 1 
ATOM   5423 N  N     . PHE A 1 670 ? 38.213  2.069   25.094  1   36     ? 672  PHE A N     1 1 
ATOM   5424 C  CA    . PHE A 1 670 ? 38.414  3.103   26.09   1   36.3   ? 672  PHE A CA    1 1 
ATOM   5425 C  C     . PHE A 1 670 ? 39.436  2.684   27.134  1   37.75  ? 672  PHE A C     1 1 
ATOM   5426 O  O     . PHE A 1 670 ? 39.592  1.504   27.422  1   37.68  ? 672  PHE A O     1 1 
ATOM   5427 C  CB    . PHE A 1 670 ? 37.089  3.361   26.816  1   35.61  ? 672  PHE A CB    1 1 
ATOM   5428 C  CG    . PHE A 1 670 ? 36.026  4.003   25.972  1   35.24  ? 672  PHE A CG    1 1 
ATOM   5429 C  CD1   . PHE A 1 670 ? 35.163  3.232   25.213  1   35.41  ? 672  PHE A CD1   1 1 
ATOM   5430 C  CD2   . PHE A 1 670 ? 35.903  5.379   25.917  1   35.65  ? 672  PHE A CD2   1 1 
ATOM   5431 C  CE1   . PHE A 1 670 ? 34.192  3.827   24.415  1   36     ? 672  PHE A CE1   1 1 
ATOM   5432 C  CE2   . PHE A 1 670 ? 34.92   5.972   25.133  1   36.19  ? 672  PHE A CE2   1 1 
ATOM   5433 C  CZ    . PHE A 1 670 ? 34.063  5.192   24.395  1   35.83  ? 672  PHE A CZ    1 1 
ATOM   5434 N  N     . HIS A 1 671 ? 40.093  3.658   27.737  1   39.03  ? 673  HIS A N     1 1 
ATOM   5435 C  CA    . HIS A 1 671 ? 41.003  3.42    28.841  1   41.24  ? 673  HIS A CA    1 1 
ATOM   5436 C  C     . HIS A 1 671 ? 40.7    4.505   29.838  1   44.06  ? 673  HIS A C     1 1 
ATOM   5437 O  O     . HIS A 1 671 ? 40.934  5.676   29.535  1   44.16  ? 673  HIS A O     1 1 
ATOM   5438 C  CB    . HIS A 1 671 ? 42.478  3.496   28.423  1   41.91  ? 673  HIS A CB    1 1 
ATOM   5439 C  CG    . HIS A 1 671 ? 43.419  3.343   29.581  1   45.14  ? 673  HIS A CG    1 1 
ATOM   5440 N  ND1   . HIS A 1 671 ? 44.059  4.44    30.149  1   47.49  ? 673  HIS A ND1   1 1 
ATOM   5441 C  CD2   . HIS A 1 671 ? 43.791  2.226   30.253  1   46.36  ? 673  HIS A CD2   1 1 
ATOM   5442 C  CE1   . HIS A 1 671 ? 44.808  3.953   31.13   1   47.79  ? 673  HIS A CE1   1 1 
ATOM   5443 N  NE2   . HIS A 1 671 ? 44.675  2.628   31.237  1   47.45  ? 673  HIS A NE2   1 1 
ATOM   5444 N  N     . ILE A 1 672 ? 40.134  4.145   30.99   1   46.31  ? 674  ILE A N     1 1 
ATOM   5445 C  CA    . ILE A 1 672 ? 39.833  5.147   31.992  1   49.62  ? 674  ILE A CA    1 1 
ATOM   5446 C  C     . ILE A 1 672 ? 40.967  5.169   33.004  1   52.86  ? 674  ILE A C     1 1 
ATOM   5447 O  O     . ILE A 1 672 ? 41.2    4.197   33.734  1   53.4   ? 674  ILE A O     1 1 
ATOM   5448 C  CB    . ILE A 1 672 ? 38.407  5.031   32.572  1   50.7   ? 674  ILE A CB    1 1 
ATOM   5449 C  CG1   . ILE A 1 672 ? 38.154  3.662   33.205  1   52.26  ? 674  ILE A CG1   1 1 
ATOM   5450 C  CG2   . ILE A 1 672 ? 37.383  5.313   31.456  1   51.28  ? 674  ILE A CG2   1 1 
ATOM   5451 C  CD1   . ILE A 1 672 ? 36.751  3.496   33.812  1   53.77  ? 674  ILE A CD1   1 1 
ATOM   5452 N  N     . GLU A 1 673 ? 41.775  6.241   32.926  1   54.69  ? 675  GLU A N     1 1 
ATOM   5453 C  CA    . GLU A 1 673 ? 42.939  6.457   33.788  1   56.72  ? 675  GLU A CA    1 1 
ATOM   5454 C  C     . GLU A 1 673 ? 42.512  6.456   35.265  1   57.91  ? 675  GLU A C     1 1 
ATOM   5455 O  O     . GLU A 1 673 ? 43.147  5.799   36.1    1   58.19  ? 675  GLU A O     1 1 
ATOM   5456 C  CB    . GLU A 1 673 ? 43.618  7.785   33.415  1   60     ? 675  GLU A CB    1 1 
ATOM   5457 C  CG    . GLU A 1 673 ? 44.764  8.184   34.327  1   67.22  ? 675  GLU A CG    1 1 
ATOM   5458 C  CD    . GLU A 1 673 ? 45.264  9.593   34.078  1   77.29  ? 675  GLU A CD    1 1 
ATOM   5459 O  OE1   . GLU A 1 673 ? 45.162  10.059  32.92   1   80.19  ? 675  GLU A OE1   1 1 
ATOM   5460 O  OE2   . GLU A 1 673 ? 45.752  10.232  35.039  1   80     ? 675  GLU A OE2   1 1 
ATOM   5461 N  N     . GLY A 1 674 ? 41.397  7.135   35.539  1   58.22  ? 676  GLY A N     1 1 
ATOM   5462 C  CA    . GLY A 1 674 ? 40.814  7.244   36.867  1   58.66  ? 676  GLY A CA    1 1 
ATOM   5463 C  C     . GLY A 1 674 ? 39.827  8.388   36.954  1   58.77  ? 676  GLY A C     1 1 
ATOM   5464 O  O     . GLY A 1 674 ? 40.054  9.35    37.687  1   58.74  ? 676  GLY A O     1 1 
ATOM   5465 O  "O5'" . DG  B 2 1   ? 31.792  44.556  10.895  1   43.54  ? 1    DG  E "O5'" 1 ? 
ATOM   5466 C  "C5'" . DG  B 2 1   ? 33.23   44.633  10.887  1   43.06  ? 1    DG  E "C5'" 1 ? 
ATOM   5467 C  "C4'" . DG  B 2 1   ? 33.845  43.721  9.823   1   42.73  ? 1    DG  E "C4'" 1 ? 
ATOM   5468 O  "O4'" . DG  B 2 1   ? 34.902  42.931  10.436  1   42.16  ? 1    DG  E "O4'" 1 ? 
ATOM   5469 C  "C3'" . DG  B 2 1   ? 32.89   42.717  9.176   1   42.92  ? 1    DG  E "C3'" 1 ? 
ATOM   5470 O  "O3'" . DG  B 2 1   ? 32.391  43.239  7.936   1   43.79  ? 1    DG  E "O3'" 1 ? 
ATOM   5471 C  "C2'" . DG  B 2 1   ? 33.755  41.479  8.944   1   42.25  ? 1    DG  E "C2'" 1 ? 
ATOM   5472 C  "C1'" . DG  B 2 1   ? 34.824  41.579  10.028  1   41.39  ? 1    DG  E "C1'" 1 ? 
ATOM   5473 N  N9    . DG  B 2 1   ? 34.579  40.741  11.209  1   39.29  ? 1    DG  E N9    1 1 
ATOM   5474 C  C8    . DG  B 2 1   ? 34.45   41.177  12.511  1   38.42  ? 1    DG  E C8    1 1 
ATOM   5475 N  N7    . DG  B 2 1   ? 34.339  40.206  13.37   1   37.48  ? 1    DG  E N7    1 1 
ATOM   5476 C  C5    . DG  B 2 1   ? 34.361  39.061  12.591  1   37.04  ? 1    DG  E C5    1 1 
ATOM   5477 C  C6    . DG  B 2 1   ? 34.32   37.709  12.981  1   36.98  ? 1    DG  E C6    1 1 
ATOM   5478 O  O6    . DG  B 2 1   ? 34.197  37.249  14.12   1   37.12  ? 1    DG  E O6    1 1 
ATOM   5479 N  N1    . DG  B 2 1   ? 34.378  36.851  11.886  1   36.83  ? 1    DG  E N1    1 1 
ATOM   5480 C  C2    . DG  B 2 1   ? 34.533  37.258  10.58   1   36.8   ? 1    DG  E C2    1 1 
ATOM   5481 N  N2    . DG  B 2 1   ? 34.595  36.28   9.656   1   36.87  ? 1    DG  E N2    1 1 
ATOM   5482 N  N3    . DG  B 2 1   ? 34.638  38.525  10.206  1   36.67  ? 1    DG  E N3    1 1 
ATOM   5483 C  C4    . DG  B 2 1   ? 34.538  39.369  11.262  1   37.39  ? 1    DG  E C4    1 1 
ATOM   5484 P  P     . DT  B 2 2   ? 30.954  42.769  7.378   1   44.19  ? 2    DT  E P     1 1 
ATOM   5485 O  OP1   . DT  B 2 2   ? 30.678  43.514  6.122   1   44.74  ? 2    DT  E OP1   1 1 
ATOM   5486 O  OP2   . DT  B 2 2   ? 29.987  42.832  8.505   1   44.49  ? 2    DT  E OP2   1 1 
ATOM   5487 O  "O5'" . DT  B 2 2   ? 31.188  41.226  7.017   1   42.54  ? 2    DT  E "O5'" 1 ? 
ATOM   5488 C  "C5'" . DT  B 2 2   ? 31.982  40.854  5.891   1   40.76  ? 2    DT  E "C5'" 1 ? 
ATOM   5489 C  "C4'" . DT  B 2 2   ? 31.796  39.386  5.583   1   38.95  ? 2    DT  E "C4'" 1 ? 
ATOM   5490 O  "O4'" . DT  B 2 2   ? 32.209  38.582  6.729   1   37.61  ? 2    DT  E "O4'" 1 ? 
ATOM   5491 C  "C3'" . DT  B 2 2   ? 30.362  38.977  5.269   1   38.41  ? 2    DT  E "C3'" 1 ? 
ATOM   5492 O  "O3'" . DT  B 2 2   ? 30.376  37.986  4.286   1   38.81  ? 2    DT  E "O3'" 1 ? 
ATOM   5493 C  "C2'" . DT  B 2 2   ? 29.859  38.444  6.601   1   37.34  ? 2    DT  E "C2'" 1 ? 
ATOM   5494 C  "C1'" . DT  B 2 2   ? 31.127  37.82   7.198   1   36.6   ? 2    DT  E "C1'" 1 ? 
ATOM   5495 N  N1    . DT  B 2 2   ? 31.145  37.836  8.702   1   34.93  ? 2    DT  E N1    1 1 
ATOM   5496 C  C2    . DT  B 2 2   ? 31.162  36.637  9.379   1   33.63  ? 2    DT  E C2    1 1 
ATOM   5497 O  O2    . DT  B 2 2   ? 31.213  35.569  8.819   1   33.42  ? 2    DT  E O2    1 1 
ATOM   5498 N  N3    . DT  B 2 2   ? 31.093  36.737  10.742  1   33.08  ? 2    DT  E N3    1 1 
ATOM   5499 C  C4    . DT  B 2 2   ? 30.99   37.896  11.487  1   33.53  ? 2    DT  E C4    1 1 
ATOM   5500 O  O4    . DT  B 2 2   ? 30.963  37.828  12.712  1   33.7   ? 2    DT  E O4    1 1 
ATOM   5501 C  C5    . DT  B 2 2   ? 30.927  39.127  10.721  1   33.74  ? 2    DT  E C5    1 1 
ATOM   5502 C  C7    . DT  B 2 2   ? 30.836  40.441  11.429  1   33.42  ? 2    DT  E C7    1 1 
ATOM   5503 C  C6    . DT  B 2 2   ? 30.968  39.038  9.376   1   34.31  ? 2    DT  E C6    1 1 
ATOM   5504 P  P     . DC  B 2 3   ? 29.059  37.632  3.466   1   39.25  ? 3    DC  E P     1 1 
ATOM   5505 O  OP1   . DC  B 2 3   ? 29.456  37.421  2.048   1   40.06  ? 3    DC  E OP1   1 1 
ATOM   5506 O  OP2   . DC  B 2 3   ? 27.996  38.617  3.814   1   39.54  ? 3    DC  E OP2   1 1 
ATOM   5507 O  "O5'" . DC  B 2 3   ? 28.639  36.22   4.081   1   36.98  ? 3    DC  E "O5'" 1 ? 
ATOM   5508 C  "C5'" . DC  B 2 3   ? 29.543  35.148  4.054   1   34.64  ? 3    DC  E "C5'" 1 ? 
ATOM   5509 C  "C4'" . DC  B 2 3   ? 29.001  34.009  4.871   1   32.71  ? 3    DC  E "C4'" 1 ? 
ATOM   5510 O  "O4'" . DC  B 2 3   ? 29.119  34.324  6.274   1   31.58  ? 3    DC  E "O4'" 1 ? 
ATOM   5511 C  "C3'" . DC  B 2 3   ? 27.523  33.709  4.63    1   31.72  ? 3    DC  E "C3'" 1 ? 
ATOM   5512 O  "O3'" . DC  B 2 3   ? 27.374  32.348  4.447   1   30.86  ? 3    DC  E "O3'" 1 ? 
ATOM   5513 C  "C2'" . DC  B 2 3   ? 26.824  34.209  5.903   1   31.07  ? 3    DC  E "C2'" 1 ? 
ATOM   5514 C  "C1'" . DC  B 2 3   ? 27.916  34.019  6.932   1   30.16  ? 3    DC  E "C1'" 1 ? 
ATOM   5515 N  N1    . DC  B 2 3   ? 27.802  34.894  8.115   1   28.18  ? 3    DC  E N1    1 1 
ATOM   5516 C  C2    . DC  B 2 3   ? 27.932  34.331  9.377   1   27.32  ? 3    DC  E C2    1 1 
ATOM   5517 O  O2    . DC  B 2 3   ? 28.046  33.12   9.462   1   26.85  ? 3    DC  E O2    1 1 
ATOM   5518 N  N3    . DC  B 2 3   ? 27.871  35.123  10.473  1   27.31  ? 3    DC  E N3    1 1 
ATOM   5519 C  C4    . DC  B 2 3   ? 27.715  36.433  10.331  1   27.6   ? 3    DC  E C4    1 1 
ATOM   5520 N  N4    . DC  B 2 3   ? 27.681  37.182  11.439  1   27.42  ? 3    DC  E N4    1 1 
ATOM   5521 C  C5    . DC  B 2 3   ? 27.604  37.039  9.04    1   27.82  ? 3    DC  E C5    1 1 
ATOM   5522 C  C6    . DC  B 2 3   ? 27.639  36.229  7.968   1   27.89  ? 3    DC  E C6    1 1 
ATOM   5523 P  P     . DT  B 2 4   ? 26.053  31.759  3.814   1   29.87  ? 4    DT  E P     1 1 
ATOM   5524 O  OP1   . DT  B 2 4   ? 26.446  30.649  2.911   1   30.9   ? 4    DT  E OP1   1 1 
ATOM   5525 O  OP2   . DT  B 2 4   ? 25.251  32.876  3.283   1   29.78  ? 4    DT  E OP2   1 1 
ATOM   5526 O  "O5'" . DT  B 2 4   ? 25.339  31.156  5.103   1   28.77  ? 4    DT  E "O5'" 1 ? 
ATOM   5527 C  "C5'" . DT  B 2 4   ? 25.908  30.004  5.749   1   28.42  ? 4    DT  E "C5'" 1 ? 
ATOM   5528 C  "C4'" . DT  B 2 4   ? 25.23   29.728  7.073   1   27.98  ? 4    DT  E "C4'" 1 ? 
ATOM   5529 O  "O4'" . DT  B 2 4   ? 25.411  30.857  7.967   1   27.52  ? 4    DT  E "O4'" 1 ? 
ATOM   5530 C  "C3'" . DT  B 2 4   ? 23.719  29.497  6.999   1   28.24  ? 4    DT  E "C3'" 1 ? 
ATOM   5531 O  "O3'" . DT  B 2 4   ? 23.39   28.402  7.827   1   29.53  ? 4    DT  E "O3'" 1 ? 
ATOM   5532 C  "C2'" . DT  B 2 4   ? 23.148  30.793  7.571   1   27.23  ? 4    DT  E "C2'" 1 ? 
ATOM   5533 C  "C1'" . DT  B 2 4   ? 24.195  31.111  8.612   1   26.35  ? 4    DT  E "C1'" 1 ? 
ATOM   5534 N  N1    . DT  B 2 4   ? 24.198  32.5    9.068   1   25.12  ? 4    DT  E N1    1 1 
ATOM   5535 C  C2    . DT  B 2 4   ? 24.318  32.749  10.407  1   24.81  ? 4    DT  E C2    1 1 
ATOM   5536 O  O2    . DT  B 2 4   ? 24.439  31.87   11.226  1   24.99  ? 4    DT  E O2    1 1 
ATOM   5537 N  N3    . DT  B 2 4   ? 24.365  34.082  10.749  1   24.2   ? 4    DT  E N3    1 1 
ATOM   5538 C  C4    . DT  B 2 4   ? 24.283  35.162  9.894   1   23.98  ? 4    DT  E C4    1 1 
ATOM   5539 O  O4    . DT  B 2 4   ? 24.296  36.305  10.358  1   24.34  ? 4    DT  E O4    1 1 
ATOM   5540 C  C5    . DT  B 2 4   ? 24.146  34.831  8.491   1   23.8   ? 4    DT  E C5    1 1 
ATOM   5541 C  C7    . DT  B 2 4   ? 24.052  35.92   7.466   1   23.21  ? 4    DT  E C7    1 1 
ATOM   5542 C  C6    . DT  B 2 4   ? 24.121  33.53   8.148   1   24.5   ? 4    DT  E C6    1 1 
ATOM   5543 P  P     . DG  B 2 5   ? 22.237  27.382  7.429   1   29.82  ? 5    DG  E P     1 1 
ATOM   5544 O  OP1   . DG  B 2 5   ? 22.876  26.256  6.747   1   30.59  ? 5    DG  E OP1   1 1 
ATOM   5545 O  OP2   . DG  B 2 5   ? 21.153  28.121  6.758   1   30.23  ? 5    DG  E OP2   1 1 
ATOM   5546 O  "O5'" . DG  B 2 5   ? 21.715  26.926  8.859   1   29.97  ? 5    DG  E "O5'" 1 ? 
ATOM   5547 C  "C5'" . DG  B 2 5   ? 22.655  26.499  9.818   1   30.84  ? 5    DG  E "C5'" 1 ? 
ATOM   5548 C  "C4'" . DG  B 2 5   ? 22.198  26.834  11.223  1   31.97  ? 5    DG  E "C4'" 1 ? 
ATOM   5549 O  "O4'" . DG  B 2 5   ? 22.415  28.243  11.485  1   31.14  ? 5    DG  E "O4'" 1 ? 
ATOM   5550 C  "C3'" . DG  B 2 5   ? 20.724  26.553  11.53   1   33.33  ? 5    DG  E "C3'" 1 ? 
ATOM   5551 O  "O3'" . DG  B 2 5   ? 20.625  25.762  12.708  1   35.7   ? 5    DG  E "O3'" 1 ? 
ATOM   5552 C  "C2'" . DG  B 2 5   ? 20.132  27.944  11.746  1   32.05  ? 5    DG  E "C2'" 1 ? 
ATOM   5553 C  "C1'" . DG  B 2 5   ? 21.331  28.753  12.206  1   30.65  ? 5    DG  E "C1'" 1 ? 
ATOM   5554 N  N9    . DG  B 2 5   ? 21.216  30.185  11.89   1   28.74  ? 5    DG  E N9    1 1 
ATOM   5555 C  C8    . DG  B 2 5   ? 20.995  30.733  10.652  1   28.21  ? 5    DG  E C8    1 1 
ATOM   5556 N  N7    . DG  B 2 5   ? 20.946  32.03   10.655  1   27.36  ? 5    DG  E N7    1 1 
ATOM   5557 C  C5    . DG  B 2 5   ? 21.129  32.366  11.986  1   27.11  ? 5    DG  E C5    1 1 
ATOM   5558 C  C6    . DG  B 2 5   ? 21.183  33.64   12.592  1   26.37  ? 5    DG  E C6    1 1 
ATOM   5559 O  O6    . DG  B 2 5   ? 21.05   34.729  12.047  1   25.95  ? 5    DG  E O6    1 1 
ATOM   5560 N  N1    . DG  B 2 5   ? 21.389  33.56   13.969  1   26.02  ? 5    DG  E N1    1 1 
ATOM   5561 C  C2    . DG  B 2 5   ? 21.532  32.38   14.665  1   26.27  ? 5    DG  E C2    1 1 
ATOM   5562 N  N2    . DG  B 2 5   ? 21.778  32.488  15.983  1   25.52  ? 5    DG  E N2    1 1 
ATOM   5563 N  N3    . DG  B 2 5   ? 21.531  31.172  14.092  1   27.07  ? 5    DG  E N3    1 1 
ATOM   5564 C  C4    . DG  B 2 5   ? 21.307  31.244  12.759  1   27.6   ? 5    DG  E C4    1 1 
ATOM   5565 P  P     . DC  B 2 6   ? 19.211  25.18   13.201  1   38.77  ? 6    DC  E P     1 1 
ATOM   5566 O  OP1   . DC  B 2 6   ? 19.522  23.951  13.981  1   39.76  ? 6    DC  E OP1   1 1 
ATOM   5567 O  OP2   . DC  B 2 6   ? 18.262  25.113  12.043  1   38.72  ? 6    DC  E OP2   1 1 
ATOM   5568 O  "O5'" . DC  B 2 6   ? 18.658  26.311  14.196  1   38.23  ? 6    DC  E "O5'" 1 ? 
ATOM   5569 C  "C5'" . DC  B 2 6   ? 19.36   26.612  15.382  1   38.2   ? 6    DC  E "C5'" 1 ? 
ATOM   5570 C  "C4'" . DC  B 2 6   ? 18.758  27.824  16.044  1   38.43  ? 6    DC  E "C4'" 1 ? 
ATOM   5571 O  "O4'" . DC  B 2 6   ? 19.073  28.991  15.252  1   37.77  ? 6    DC  E "O4'" 1 ? 
ATOM   5572 C  "C3'" . DC  B 2 6   ? 17.238  27.791  16.115  1   39.38  ? 6    DC  E "C3'" 1 ? 
ATOM   5573 O  "O3'" . DC  B 2 6   ? 16.789  27.505  17.441  1   40.84  ? 6    DC  E "O3'" 1 ? 
ATOM   5574 C  "C2'" . DC  B 2 6   ? 16.785  29.183  15.654  1   38.47  ? 6    DC  E "C2'" 1 ? 
ATOM   5575 C  "C1'" . DC  B 2 6   ? 18.084  29.949  15.476  1   37.38  ? 6    DC  E "C1'" 1 ? 
ATOM   5576 N  N1    . DC  B 2 6   ? 18.022  30.854  14.329  1   35.92  ? 6    DC  E N1    1 1 
ATOM   5577 C  C2    . DC  B 2 6   ? 18.016  32.213  14.558  1   35.23  ? 6    DC  E C2    1 1 
ATOM   5578 O  O2    . DC  B 2 6   ? 18.224  32.616  15.705  1   35.55  ? 6    DC  E O2    1 1 
ATOM   5579 N  N3    . DC  B 2 6   ? 17.837  33.056  13.515  1   34.6   ? 6    DC  E N3    1 1 
ATOM   5580 C  C4    . DC  B 2 6   ? 17.624  32.563  12.295  1   34.46  ? 6    DC  E C4    1 1 
ATOM   5581 N  N4    . DC  B 2 6   ? 17.464  33.423  11.292  1   34.14  ? 6    DC  E N4    1 1 
ATOM   5582 C  C5    . DC  B 2 6   ? 17.567  31.165  12.052  1   34.93  ? 6    DC  E C5    1 1 
ATOM   5583 C  C6    . DC  B 2 6   ? 17.735  30.356  13.095  1   35.48  ? 6    DC  E C6    1 1 
ATOM   5584 P  P     . DA  B 2 7   ? 15.245  27.111  17.681  1   41.47  ? 7    DA  E P     1 1 
ATOM   5585 O  OP1   . DA  B 2 7   ? 15.17   26.255  18.89   1   42.06  ? 7    DA  E OP1   1 1 
ATOM   5586 O  OP2   . DA  B 2 7   ? 14.679  26.622  16.391  1   41.1   ? 7    DA  E OP2   1 1 
ATOM   5587 O  "O5'" . DA  B 2 7   ? 14.578  28.519  18.01   1   41.54  ? 7    DA  E "O5'" 1 ? 
ATOM   5588 C  "C5'" . DA  B 2 7   ? 15.283  29.467  18.793  1   41.76  ? 7    DA  E "C5'" 1 ? 
ATOM   5589 C  "C4'" . DA  B 2 7   ? 14.644  30.833  18.667  1   41.72  ? 7    DA  E "C4'" 1 ? 
ATOM   5590 O  "O4'" . DA  B 2 7   ? 15.109  31.503  17.451  1   41.44  ? 7    DA  E "O4'" 1 ? 
ATOM   5591 C  "C3'" . DA  B 2 7   ? 13.109  30.831  18.585  1   42.04  ? 7    DA  E "C3'" 1 ? 
ATOM   5592 O  "O3'" . DA  B 2 7   ? 12.622  31.879  19.383  1   43.31  ? 7    DA  E "O3'" 1 ? 
ATOM   5593 C  "C2'" . DA  B 2 7   ? 12.87   31.14   17.109  1   41.31  ? 7    DA  E "C2'" 1 ? 
ATOM   5594 C  "C1'" . DA  B 2 7   ? 13.999  32.13   16.873  1   40.47  ? 7    DA  E "C1'" 1 ? 
ATOM   5595 N  N9    . DA  B 2 7   ? 14.24   32.431  15.463  1   38.58  ? 7    DA  E N9    1 1 
ATOM   5596 C  C8    . DA  B 2 7   ? 14.206  31.54   14.423  1   38.05  ? 7    DA  E C8    1 1 
ATOM   5597 N  N7    . DA  B 2 7   ? 14.261  32.1    13.236  1   37.32  ? 7    DA  E N7    1 1 
ATOM   5598 C  C5    . DA  B 2 7   ? 14.243  33.46   13.509  1   36.65  ? 7    DA  E C5    1 1 
ATOM   5599 C  C6    . DA  B 2 7   ? 14.249  34.604  12.674  1   35.33  ? 7    DA  E C6    1 1 
ATOM   5600 N  N6    . DA  B 2 7   ? 14.312  34.539  11.34   1   34.82  ? 7    DA  E N6    1 1 
ATOM   5601 N  N1    . DA  B 2 7   ? 14.25   35.816  13.268  1   34.73  ? 7    DA  E N1    1 1 
ATOM   5602 C  C2    . DA  B 2 7   ? 14.214  35.882  14.6    1   35.32  ? 7    DA  E C2    1 1 
ATOM   5603 N  N3    . DA  B 2 7   ? 14.173  34.888  15.492  1   36.48  ? 7    DA  E N3    1 1 
ATOM   5604 C  C4    . DA  B 2 7   ? 14.206  33.684  14.875  1   37.36  ? 7    DA  E C4    1 1 
ATOM   5605 P  P     . DT  B 2 8   ? 11.445  31.654  20.439  1   43.96  ? 8    DT  E P     1 1 
ATOM   5606 O  OP1   . DT  B 2 8   ? 12.033  30.964  21.617  1   44.39  ? 8    DT  E OP1   1 1 
ATOM   5607 O  OP2   . DT  B 2 8   ? 10.284  31.067  19.727  1   44.1   ? 8    DT  E OP2   1 1 
ATOM   5608 O  "O5'" . DT  B 2 8   ? 11.077  33.179  20.847  1   43.41  ? 8    DT  E "O5'" 1 ? 
ATOM   5609 C  "C5'" . DT  B 2 8   ? 12.145  34.096  21.198  1   42.69  ? 8    DT  E "C5'" 1 ? 
ATOM   5610 C  "C4'" . DT  B 2 8   ? 11.866  35.517  20.709  1   42.04  ? 8    DT  E "C4'" 1 ? 
ATOM   5611 O  "O4'" . DT  B 2 8   ? 12.139  35.615  19.281  1   41.44  ? 8    DT  E "O4'" 1 ? 
ATOM   5612 C  "C3'" . DT  B 2 8   ? 10.425  36.024  20.903  1   41.53  ? 8    DT  E "C3'" 1 ? 
ATOM   5613 O  "O3'" . DT  B 2 8   ? 10.44   37.32   21.417  1   41.78  ? 8    DT  E "O3'" 1 ? 
ATOM   5614 C  "C2'" . DT  B 2 8   ? 9.857   36.013  19.493  1   40.67  ? 8    DT  E "C2'" 1 ? 
ATOM   5615 C  "C1'" . DT  B 2 8   ? 11.088  36.325  18.667  1   40.17  ? 8    DT  E "C1'" 1 ? 
ATOM   5616 N  N1    . DT  B 2 8   ? 10.961  35.873  17.273  1   38.48  ? 8    DT  E N1    1 1 
ATOM   5617 C  C2    . DT  B 2 8   ? 11.1    36.788  16.266  1   37.77  ? 8    DT  E C2    1 1 
ATOM   5618 O  O2    . DT  B 2 8   ? 11.4    37.948  16.46   1   37.6   ? 8    DT  E O2    1 1 
ATOM   5619 N  N3    . DT  B 2 8   ? 10.888  36.289  15.012  1   37.61  ? 8    DT  E N3    1 1 
ATOM   5620 C  C4    . DT  B 2 8   ? 10.509  34.997  14.681  1   37.39  ? 8    DT  E C4    1 1 
ATOM   5621 O  O4    . DT  B 2 8   ? 10.353  34.699  13.512  1   37.19  ? 8    DT  E O4    1 1 
ATOM   5622 C  C5    . DT  B 2 8   ? 10.342  34.101  15.79   1   37.73  ? 8    DT  E C5    1 1 
ATOM   5623 C  C7    . DT  B 2 8   ? 9.933   32.679  15.558  1   38.08  ? 8    DT  E C7    1 1 
ATOM   5624 C  C6    . DT  B 2 8   ? 10.553  34.58   17.018  1   38.18  ? 8    DT  E C6    1 1 
ATOM   5625 P  P     . DT  B 2 9   ? 9.114   37.962  22.058  1   42.58  ? 9    DT  E P     1 1 
ATOM   5626 O  OP1   . DT  B 2 9   ? 9.408   38.257  23.483  1   43.36  ? 9    DT  E OP1   1 1 
ATOM   5627 O  OP2   . DT  B 2 9   ? 7.951   37.127  21.696  1   42.9   ? 9    DT  E OP2   1 1 
ATOM   5628 O  "O5'" . DT  B 2 9   ? 8.982   39.344  21.266  1   41.29  ? 9    DT  E "O5'" 1 ? 
ATOM   5629 C  "C5'" . DT  B 2 9   ? 10.098  40.209  21.196  1   39.38  ? 9    DT  E "C5'" 1 ? 
ATOM   5630 C  "C4'" . DT  B 2 9   ? 9.968   41.186  20.04   1   37.45  ? 9    DT  E "C4'" 1 ? 
ATOM   5631 O  "O4'" . DT  B 2 9   ? 9.927   40.469  18.781  1   36.15  ? 9    DT  E "O4'" 1 ? 
ATOM   5632 C  "C3'" . DT  B 2 9   ? 8.738   42.093  20.052  1   36.78  ? 9    DT  E "C3'" 1 ? 
ATOM   5633 O  "O3'" . DT  B 2 9   ? 9.159   43.397  19.639  1   37.1   ? 9    DT  E "O3'" 1 ? 
ATOM   5634 C  "C2'" . DT  B 2 9   ? 7.83    41.431  19.013  1   35.6   ? 9    DT  E "C2'" 1 ? 
ATOM   5635 C  "C1'" . DT  B 2 9   ? 8.854   40.952  18.009  1   34.29  ? 9    DT  E "C1'" 1 ? 
ATOM   5636 N  N1    . DT  B 2 9   ? 8.381   39.858  17.141  1   31.79  ? 9    DT  E N1    1 1 
ATOM   5637 C  C2    . DT  B 2 9   ? 8.521   39.983  15.782  1   30.82  ? 9    DT  E C2    1 1 
ATOM   5638 O  O2    . DT  B 2 9   ? 8.924   41.003  15.246  1   30.94  ? 9    DT  E O2    1 1 
ATOM   5639 N  N3    . DT  B 2 9   ? 8.106   38.895  15.063  1   29.69  ? 9    DT  E N3    1 1 
ATOM   5640 C  C4    . DT  B 2 9   ? 7.638   37.699  15.565  1   29.79  ? 9    DT  E C4    1 1 
ATOM   5641 O  O4    . DT  B 2 9   ? 7.325   36.797  14.793  1   29.71  ? 9    DT  E O4    1 1 
ATOM   5642 C  C5    . DT  B 2 9   ? 7.523   37.633  16.997  1   30.03  ? 9    DT  E C5    1 1 
ATOM   5643 C  C7    . DT  B 2 9   ? 6.975   36.401  17.645  1   29.87  ? 9    DT  E C7    1 1 
ATOM   5644 C  C6    . DT  B 2 9   ? 7.925   38.69   17.712  1   30.77  ? 9    DT  E C6    1 1 
ATOM   5645 P  P     . DC  B 2 10  ? 8.136   44.616  19.463  1   36.74  ? 10   DC  E P     1 1 
ATOM   5646 O  OP1   . DC  B 2 10  ? 8.868   45.837  19.851  1   37.34  ? 10   DC  E OP1   1 1 
ATOM   5647 O  OP2   . DC  B 2 10  ? 6.85    44.273  20.12   1   36.74  ? 10   DC  E OP2   1 1 
ATOM   5648 O  "O5'" . DC  B 2 10  ? 7.899   44.631  17.896  1   34.53  ? 10   DC  E "O5'" 1 ? 
ATOM   5649 C  "C5'" . DC  B 2 10  ? 8.993   44.902  17.032  1   32.18  ? 10   DC  E "C5'" 1 ? 
ATOM   5650 C  "C4'" . DC  B 2 10  ? 8.488   45.139  15.628  1   30.5   ? 10   DC  E "C4'" 1 ? 
ATOM   5651 O  "O4'" . DC  B 2 10  ? 7.91    43.91   15.099  1   29.53  ? 10   DC  E "O4'" 1 ? 
ATOM   5652 C  "C3'" . DC  B 2 10  ? 7.394   46.206  15.501  1   29.43  ? 10   DC  E "C3'" 1 ? 
ATOM   5653 O  "O3'" . DC  B 2 10  ? 7.661   46.952  14.336  1   29.11  ? 10   DC  E "O3'" 1 ? 
ATOM   5654 C  "C2'" . DC  B 2 10  ? 6.105   45.379  15.377  1   28.69  ? 10   DC  E "C2'" 1 ? 
ATOM   5655 C  "C1'" . DC  B 2 10  ? 6.602   44.162  14.616  1   28.23  ? 10   DC  E "C1'" 1 ? 
ATOM   5656 N  N1    . DC  B 2 10  ? 5.819   42.921  14.832  1   26.58  ? 10   DC  E N1    1 1 
ATOM   5657 C  C2    . DC  B 2 10  ? 5.33    42.224  13.727  1   25.2   ? 10   DC  E C2    1 1 
ATOM   5658 O  O2    . DC  B 2 10  ? 5.387   42.752  12.616  1   24.13  ? 10   DC  E O2    1 1 
ATOM   5659 N  N3    . DC  B 2 10  ? 4.776   41.003  13.915  1   25.3   ? 10   DC  E N3    1 1 
ATOM   5660 C  C4    . DC  B 2 10  ? 4.729   40.471  15.14   1   25.58  ? 10   DC  E C4    1 1 
ATOM   5661 N  N4    . DC  B 2 10  ? 4.191   39.254  15.277  1   25.71  ? 10   DC  E N4    1 1 
ATOM   5662 C  C5    . DC  B 2 10  ? 5.251   41.149  16.271  1   25.74  ? 10   DC  E C5    1 1 
ATOM   5663 C  C6    . DC  B 2 10  ? 5.826   42.336  16.065  1   26.38  ? 10   DC  E C6    1 1 
ATOM   5664 P  P     . DC  B 2 11  ? 6.911   48.311  14.014  1   28.4   ? 11   DC  E P     1 1 
ATOM   5665 O  OP1   . DC  B 2 11  ? 7.895   49.184  13.33   1   29.05  ? 11   DC  E OP1   1 1 
ATOM   5666 O  OP2   . DC  B 2 11  ? 6.209   48.782  15.241  1   28.5   ? 11   DC  E OP2   1 1 
ATOM   5667 O  "O5'" . DC  B 2 11  ? 5.825   47.861  12.961  1   25.87  ? 11   DC  E "O5'" 1 ? 
ATOM   5668 C  "C5'" . DC  B 2 11  ? 6.248   47.358  11.732  1   25.86  ? 11   DC  E "C5'" 1 ? 
ATOM   5669 C  "C4'" . DC  B 2 11  ? 5.077   46.907  10.909  1   26.62  ? 11   DC  E "C4'" 1 ? 
ATOM   5670 O  "O4'" . DC  B 2 11  ? 4.545   45.681  11.446  1   26.1   ? 11   DC  E "O4'" 1 ? 
ATOM   5671 C  "C3'" . DC  B 2 11  ? 3.914   47.9    10.812  1   27.79  ? 11   DC  E "C3'" 1 ? 
ATOM   5672 O  "O3'" . DC  B 2 11  ? 3.645   48.072  9.428   1   28.93  ? 11   DC  E "O3'" 1 ? 
ATOM   5673 C  "C2'" . DC  B 2 11  ? 2.768   47.173  11.569  1   26.91  ? 11   DC  E "C2'" 1 ? 
ATOM   5674 C  "C1'" . DC  B 2 11  ? 3.153   45.706  11.407  1   26.44  ? 11   DC  E "C1'" 1 ? 
ATOM   5675 N  N1    . DC  B 2 11  ? 2.668   44.778  12.491  1   26.04  ? 11   DC  E N1    1 1 
ATOM   5676 C  C2    . DC  B 2 11  ? 2.061   43.569  12.133  1   25.79  ? 11   DC  E C2    1 1 
ATOM   5677 O  O2    . DC  B 2 11  ? 1.845   43.341  10.939  1   25.54  ? 11   DC  E O2    1 1 
ATOM   5678 N  N3    . DC  B 2 11  ? 1.748   42.674  13.102  1   25.95  ? 11   DC  E N3    1 1 
ATOM   5679 C  C4    . DC  B 2 11  ? 1.974   42.97   14.383  1   25.91  ? 11   DC  E C4    1 1 
ATOM   5680 N  N4    . DC  B 2 11  ? 1.627   42.059  15.307  1   25.99  ? 11   DC  E N4    1 1 
ATOM   5681 C  C5    . DC  B 2 11  ? 2.591   44.194  14.77   1   25.8   ? 11   DC  E C5    1 1 
ATOM   5682 C  C6    . DC  B 2 11  ? 2.935   45.055  13.799  1   25.95  ? 11   DC  E C6    1 1 
ATOM   5683 P  P     . DT  B 2 12  ? 2.629   49.145  8.865   1   29.21  ? 12   DT  E P     1 1 
ATOM   5684 O  OP1   . DT  B 2 12  ? 3.392   50.064  8.008   1   29.2   ? 12   DT  E OP1   1 1 
ATOM   5685 O  OP2   . DT  B 2 12  ? 1.801   49.66   9.981   1   29.15  ? 12   DT  E OP2   1 1 
ATOM   5686 O  "O5'" . DT  B 2 12  ? 1.697   48.247  7.933   1   30.55  ? 12   DT  E "O5'" 1 ? 
ATOM   5687 C  "C5'" . DT  B 2 12  ? 2.291   47.181  7.162   1   31.75  ? 12   DT  E "C5'" 1 ? 
ATOM   5688 C  "C4'" . DT  B 2 12  ? 1.228   46.267  6.583   1   33.16  ? 12   DT  E "C4'" 1 ? 
ATOM   5689 O  "O4'" . DT  B 2 12  ? 0.83    45.302  7.581   1   32.67  ? 12   DT  E "O4'" 1 ? 
ATOM   5690 C  "C3'" . DT  B 2 12  ? -0.046  46.962  6.135   1   35.45  ? 12   DT  E "C3'" 1 ? 
ATOM   5691 O  "O3'" . DT  B 2 12  ? -0.449  46.414  4.9     1   39.23  ? 12   DT  E "O3'" 1 ? 
ATOM   5692 C  "C2'" . DT  B 2 12  ? -1.047  46.657  7.266   1   33.76  ? 12   DT  E "C2'" 1 ? 
ATOM   5693 C  "C1'" . DT  B 2 12  ? -0.568  45.309  7.754   1   32.37  ? 12   DT  E "C1'" 1 ? 
ATOM   5694 N  N1    . DT  B 2 12  ? -0.852  45.034  9.198   1   31.12  ? 12   DT  E N1    1 1 
ATOM   5695 C  C2    . DT  B 2 12  ? -1.275  43.767  9.572   1   30.45  ? 12   DT  E C2    1 1 
ATOM   5696 O  O2    . DT  B 2 12  ? -1.464  42.851  8.778   1   30.12  ? 12   DT  E O2    1 1 
ATOM   5697 N  N3    . DT  B 2 12  ? -1.421  43.588  10.923  1   30.25  ? 12   DT  E N3    1 1 
ATOM   5698 C  C4    . DT  B 2 12  ? -1.208  44.523  11.922  1   30.64  ? 12   DT  E C4    1 1 
ATOM   5699 O  O4    . DT  B 2 12  ? -1.35   44.194  13.1    1   30.89  ? 12   DT  E O4    1 1 
ATOM   5700 C  C5    . DT  B 2 12  ? -0.769  45.827  11.47   1   30.43  ? 12   DT  E C5    1 1 
ATOM   5701 C  C7    . DT  B 2 12  ? -0.549  46.927  12.466  1   30.31  ? 12   DT  E C7    1 1 
ATOM   5702 C  C6    . DT  B 2 12  ? -0.597  46.015  10.144  1   30.66  ? 12   DT  E C6    1 1 
ATOM   5703 P  P     . DC  B 2 13  ? -1.579  47.128  4.009   1   42.46  ? 13   DC  E P     1 1 
ATOM   5704 O  OP1   . DC  B 2 13  ? -1.188  46.988  2.584   1   43.28  ? 13   DC  E OP1   1 1 
ATOM   5705 O  OP2   . DC  B 2 13  ? -1.857  48.478  4.574   1   42.39  ? 13   DC  E OP2   1 1 
ATOM   5706 O  "O5'" . DC  B 2 13  ? -2.857  46.206  4.285   1   43.2   ? 13   DC  E "O5'" 1 ? 
ATOM   5707 C  "C5'" . DC  B 2 13  ? -2.832  44.837  3.932   1   43.9   ? 13   DC  E "C5'" 1 ? 
ATOM   5708 C  "C4'" . DC  B 2 13  ? -3.977  44.105  4.613   1   44.53  ? 13   DC  E "C4'" 1 ? 
ATOM   5709 O  "O4'" . DC  B 2 13  ? -3.713  44.021  6.03    1   44.32  ? 13   DC  E "O4'" 1 ? 
ATOM   5710 C  "C3'" . DC  B 2 13  ? -5.335  44.798  4.486   1   44.94  ? 13   DC  E "C3'" 1 ? 
ATOM   5711 O  "O3'" . DC  B 2 13  ? -6.161  44.093  3.557   1   45.41  ? 13   DC  E "O3'" 1 ? 
ATOM   5712 C  "C2'" . DC  B 2 13  ? -5.929  44.77   5.912   1   44.67  ? 13   DC  E "C2'" 1 ? 
ATOM   5713 C  "C1'" . DC  B 2 13  ? -4.933  43.919  6.71    1   43.75  ? 13   DC  E "C1'" 1 ? 
ATOM   5714 N  N1    . DC  B 2 13  ? -4.73   44.414  8.114   1   42.01  ? 13   DC  E N1    1 1 
ATOM   5715 C  C2    . DC  B 2 13  ? -4.824  43.519  9.191   1   40.75  ? 13   DC  E C2    1 1 
ATOM   5716 O  O2    . DC  B 2 13  ? -5.047  42.321  8.963   1   40.23  ? 13   DC  E O2    1 1 
ATOM   5717 N  N3    . DC  B 2 13  ? -4.673  43.996  10.458  1   40.35  ? 13   DC  E N3    1 1 
ATOM   5718 C  C4    . DC  B 2 13  ? -4.458  45.305  10.656  1   40.59  ? 13   DC  E C4    1 1 
ATOM   5719 N  N4    . DC  B 2 13  ? -4.286  45.732  11.91   1   40.51  ? 13   DC  E N4    1 1 
ATOM   5720 C  C5    . DC  B 2 13  ? -4.376  46.232  9.571   1   40.92  ? 13   DC  E C5    1 1 
ATOM   5721 C  C6    . DC  B 2 13  ? -4.538  45.752  8.334   1   41.47  ? 13   DC  E C6    1 1 
ATOM   5722 O  "O5'" . DG  C 3 1   ? -7.111  39.43   19.363  1   50.93  ? 1    DG  F "O5'" 1 ? 
ATOM   5723 C  "C5'" . DG  C 3 1   ? -8.078  38.376  19.121  1   50.42  ? 1    DG  F "C5'" 1 ? 
ATOM   5724 C  "C4'" . DG  C 3 1   ? -7.889  37.726  17.747  1   49.68  ? 1    DG  F "C4'" 1 ? 
ATOM   5725 O  "O4'" . DG  C 3 1   ? -7.745  38.735  16.699  1   49     ? 1    DG  F "O4'" 1 ? 
ATOM   5726 C  "C3'" . DG  C 3 1   ? -6.683  36.805  17.61   1   49.41  ? 1    DG  F "C3'" 1 ? 
ATOM   5727 O  "O3'" . DG  C 3 1   ? -7.045  35.682  16.798  1   50.01  ? 1    DG  F "O3'" 1 ? 
ATOM   5728 C  "C2'" . DG  C 3 1   ? -5.639  37.698  16.934  1   48.43  ? 1    DG  F "C2'" 1 ? 
ATOM   5729 C  "C1'" . DG  C 3 1   ? -6.497  38.569  16.033  1   47.64  ? 1    DG  F "C1'" 1 ? 
ATOM   5730 N  N9    . DG  C 3 1   ? -5.921  39.888  15.807  1   45.53  ? 1    DG  F N9    1 1 
ATOM   5731 C  C8    . DG  C 3 1   ? -5.423  40.742  16.763  1   44.91  ? 1    DG  F C8    1 1 
ATOM   5732 N  N7    . DG  C 3 1   ? -5.015  41.884  16.278  1   44.24  ? 1    DG  F N7    1 1 
ATOM   5733 C  C5    . DG  C 3 1   ? -5.241  41.775  14.91   1   43.57  ? 1    DG  F C5    1 1 
ATOM   5734 C  C6    . DG  C 3 1   ? -4.972  42.693  13.871  1   42.83  ? 1    DG  F C6    1 1 
ATOM   5735 O  O6    . DG  C 3 1   ? -4.446  43.818  13.961  1   42.95  ? 1    DG  F O6    1 1 
ATOM   5736 N  N1    . DG  C 3 1   ? -5.342  42.186  12.623  1   42.11  ? 1    DG  F N1    1 1 
ATOM   5737 C  C2    . DG  C 3 1   ? -5.896  40.938  12.413  1   42.11  ? 1    DG  F C2    1 1 
ATOM   5738 N  N2    . DG  C 3 1   ? -6.173  40.615  11.143  1   41.84  ? 1    DG  F N2    1 1 
ATOM   5739 N  N3    . DG  C 3 1   ? -6.153  40.065  13.38   1   42.65  ? 1    DG  F N3    1 1 
ATOM   5740 C  C4    . DG  C 3 1   ? -5.799  40.55   14.6    1   43.92  ? 1    DG  F C4    1 1 
ATOM   5741 P  P     . DA  C 3 2   ? -5.989  34.51   16.478  1   50.14  ? 2    DA  F P     1 1 
ATOM   5742 O  OP1   . DA  C 3 2   ? -6.725  33.215  16.524  1   50.72  ? 2    DA  F OP1   1 1 
ATOM   5743 O  OP2   . DA  C 3 2   ? -4.779  34.706  17.318  1   50.25  ? 2    DA  F OP2   1 1 
ATOM   5744 O  "O5'" . DA  C 3 2   ? -5.606  34.833  14.953  1   47.59  ? 2    DA  F "O5'" 1 ? 
ATOM   5745 C  "C5'" . DA  C 3 2   ? -6.649  34.825  13.944  1   44.26  ? 2    DA  F "C5'" 1 ? 
ATOM   5746 C  "C4'" . DA  C 3 2   ? -6.065  34.993  12.544  1   40.79  ? 2    DA  F "C4'" 1 ? 
ATOM   5747 O  "O4'" . DA  C 3 2   ? -5.524  36.333  12.39   1   38.9   ? 2    DA  F "O4'" 1 ? 
ATOM   5748 C  "C3'" . DA  C 3 2   ? -4.928  34.041  12.179  1   38.59  ? 2    DA  F "C3'" 1 ? 
ATOM   5749 O  "O3'" . DA  C 3 2   ? -5.03   33.684  10.802  1   37.17  ? 2    DA  F "O3'" 1 ? 
ATOM   5750 C  "C2'" . DA  C 3 2   ? -3.682  34.885  12.455  1   37.83  ? 2    DA  F "C2'" 1 ? 
ATOM   5751 C  "C1'" . DA  C 3 2   ? -4.161  36.27   12.055  1   37.28  ? 2    DA  F "C1'" 1 ? 
ATOM   5752 N  N9    . DA  C 3 2   ? -3.502  37.35   12.765  1   35.13  ? 2    DA  F N9    1 1 
ATOM   5753 C  C8    . DA  C 3 2   ? -3.266  37.431  14.11   1   34.38  ? 2    DA  F C8    1 1 
ATOM   5754 N  N7    . DA  C 3 2   ? -2.784  38.589  14.493  1   33.36  ? 2    DA  F N7    1 1 
ATOM   5755 C  C5    . DA  C 3 2   ? -2.723  39.32   13.322  1   32.96  ? 2    DA  F C5    1 1 
ATOM   5756 C  C6    . DA  C 3 2   ? -2.266  40.61   13.042  1   32.57  ? 2    DA  F C6    1 1 
ATOM   5757 N  N6    . DA  C 3 2   ? -1.802  41.446  13.98   1   32.4   ? 2    DA  F N6    1 1 
ATOM   5758 N  N1    . DA  C 3 2   ? -2.323  41.025  11.761  1   32.59  ? 2    DA  F N1    1 1 
ATOM   5759 C  C2    . DA  C 3 2   ? -2.768  40.187  10.823  1   32.44  ? 2    DA  F C2    1 1 
ATOM   5760 N  N3    . DA  C 3 2   ? -3.227  38.953  10.964  1   32.86  ? 2    DA  F N3    1 1 
ATOM   5761 C  C4    . DA  C 3 2   ? -3.16   38.57   12.249  1   33.58  ? 2    DA  F C4    1 1 
ATOM   5762 P  P     . DG  C 3 3   ? -4.188  32.449  10.218  1   36.23  ? 3    DG  F P     1 1 
ATOM   5763 O  OP1   . DG  C 3 3   ? -4.95   31.89   9.053   1   36.11  ? 3    DG  F OP1   1 1 
ATOM   5764 O  OP2   . DG  C 3 3   ? -3.803  31.577  11.356  1   36.72  ? 3    DG  F OP2   1 1 
ATOM   5765 O  "O5'" . DG  C 3 3   ? -2.844  33.129  9.687   1   32.13  ? 3    DG  F "O5'" 1 ? 
ATOM   5766 C  "C5'" . DG  C 3 3   ? -2.882  33.973  8.552   1   28.39  ? 3    DG  F "C5'" 1 ? 
ATOM   5767 C  "C4'" . DG  C 3 3   ? -1.568  34.712  8.399   1   24.73  ? 3    DG  F "C4'" 1 ? 
ATOM   5768 O  "O4'" . DG  C 3 3   ? -1.449  35.726  9.438   1   23.66  ? 3    DG  F "O4'" 1 ? 
ATOM   5769 C  "C3'" . DG  C 3 3   ? -0.304  33.844  8.497   1   22.61  ? 3    DG  F "C3'" 1 ? 
ATOM   5770 O  "O3'" . DG  C 3 3   ? 0.604   34.254  7.51    1   20.9   ? 3    DG  F "O3'" 1 ? 
ATOM   5771 C  "C2'" . DG  C 3 3   ? 0.236   34.219  9.872   1   23.12  ? 3    DG  F "C2'" 1 ? 
ATOM   5772 C  "C1'" . DG  C 3 3   ? -0.137  35.691  9.898   1   23.46  ? 3    DG  F "C1'" 1 ? 
ATOM   5773 N  N9    . DG  C 3 3   ? -0.044  36.332  11.189  1   23.31  ? 3    DG  F N9    1 1 
ATOM   5774 C  C8    . DG  C 3 3   ? -0.109  35.747  12.424  1   23.53  ? 3    DG  F C8    1 1 
ATOM   5775 N  N7    . DG  C 3 3   ? 0.129   36.583  13.402  1   24.03  ? 3    DG  F N7    1 1 
ATOM   5776 C  C5    . DG  C 3 3   ? 0.382   37.791  12.766  1   23.77  ? 3    DG  F C5    1 1 
ATOM   5777 C  C6    . DG  C 3 3   ? 0.705   39.057  13.303  1   23.75  ? 3    DG  F C6    1 1 
ATOM   5778 O  O6    . DG  C 3 3   ? 0.832   39.371  14.492  1   23.78  ? 3    DG  F O6    1 1 
ATOM   5779 N  N1    . DG  C 3 3   ? 0.881   40.011  12.298  1   23.78  ? 3    DG  F N1    1 1 
ATOM   5780 C  C2    . DG  C 3 3   ? 0.775   39.752  10.947  1   23.26  ? 3    DG  F C2    1 1 
ATOM   5781 N  N2    . DG  C 3 3   ? 0.975   40.778  10.119  1   22.66  ? 3    DG  F N2    1 1 
ATOM   5782 N  N3    . DG  C 3 3   ? 0.409   38.589  10.449  1   23.21  ? 3    DG  F N3    1 1 
ATOM   5783 C  C4    . DG  C 3 3   ? 0.275   37.65   11.407  1   23.51  ? 3    DG  F C4    1 1 
ATOM   5784 P  P     . DG  C 3 4   ? 1.189   33.263  6.406   1   19.5   ? 4    DG  F P     1 1 
ATOM   5785 O  OP1   . DG  C 3 4   ? 0.075   32.78   5.564   1   20.01  ? 4    DG  F OP1   1 1 
ATOM   5786 O  OP2   . DG  C 3 4   ? 2.092   32.302  7.069   1   18.76  ? 4    DG  F OP2   1 1 
ATOM   5787 O  "O5'" . DG  C 3 4   ? 2.095   34.264  5.537   1   20.48  ? 4    DG  F "O5'" 1 ? 
ATOM   5788 C  "C5'" . DG  C 3 4   ? 1.501   35.341  4.848   1   19.83  ? 4    DG  F "C5'" 1 ? 
ATOM   5789 C  "C4'" . DG  C 3 4   ? 2.23    36.651  5.117   1   19.74  ? 4    DG  F "C4'" 1 ? 
ATOM   5790 O  "O4'" . DG  C 3 4   ? 2.09    37.063  6.504   1   19.42  ? 4    DG  F "O4'" 1 ? 
ATOM   5791 C  "C3'" . DG  C 3 4   ? 3.733   36.68   4.809   1   19.58  ? 4    DG  F "C3'" 1 ? 
ATOM   5792 O  "O3'" . DG  C 3 4   ? 4.017   37.936  4.181   1   18.89  ? 4    DG  F "O3'" 1 ? 
ATOM   5793 C  "C2'" . DG  C 3 4   ? 4.346   36.614  6.204   1   19.6   ? 4    DG  F "C2'" 1 ? 
ATOM   5794 C  "C1'" . DG  C 3 4   ? 3.352   37.454  6.983   1   19.56  ? 4    DG  F "C1'" 1 ? 
ATOM   5795 N  N9    . DG  C 3 4   ? 3.4     37.189  8.403   1   19.76  ? 4    DG  F N9    1 1 
ATOM   5796 C  C8    . DG  C 3 4   ? 3.257   35.963  9.024   1   19.53  ? 4    DG  F C8    1 1 
ATOM   5797 N  N7    . DG  C 3 4   ? 3.405   36.024  10.317  1   19.63  ? 4    DG  F N7    1 1 
ATOM   5798 C  C5    . DG  C 3 4   ? 3.671   37.379  10.563  1   19.92  ? 4    DG  F C5    1 1 
ATOM   5799 C  C6    . DG  C 3 4   ? 3.881   38.07   11.788  1   20.35  ? 4    DG  F C6    1 1 
ATOM   5800 O  O6    . DG  C 3 4   ? 3.907   37.606  12.937  1   20.79  ? 4    DG  F O6    1 1 
ATOM   5801 N  N1    . DG  C 3 4   ? 4.164   39.422  11.578  1   20     ? 4    DG  F N1    1 1 
ATOM   5802 C  C2    . DG  C 3 4   ? 4.142   40.043  10.352  1   19.93  ? 4    DG  F C2    1 1 
ATOM   5803 N  N2    . DG  C 3 4   ? 4.397   41.374  10.341  1   19.62  ? 4    DG  F N2    1 1 
ATOM   5804 N  N3    . DG  C 3 4   ? 3.918   39.406  9.204   1   19.71  ? 4    DG  F N3    1 1 
ATOM   5805 C  C4    . DG  C 3 4   ? 3.698   38.089  9.388   1   19.6   ? 4    DG  F C4    1 1 
ATOM   5806 P  P     . DA  C 3 5   ? 5.5     38.41   3.833   1   19.31  ? 5    DA  F P     1 1 
ATOM   5807 O  OP1   . DA  C 3 5   ? 5.448   39.064  2.517   1   20.12  ? 5    DA  F OP1   1 1 
ATOM   5808 O  OP2   . DA  C 3 5   ? 6.434   37.302  4.062   1   19.74  ? 5    DA  F OP2   1 1 
ATOM   5809 O  "O5'" . DA  C 3 5   ? 5.77    39.501  4.951   1   18.77  ? 5    DA  F "O5'" 1 ? 
ATOM   5810 C  "C5'" . DA  C 3 5   ? 4.925   40.627  5.048   1   18.14  ? 5    DA  F "C5'" 1 ? 
ATOM   5811 C  "C4'" . DA  C 3 5   ? 5.616   41.758  5.802   1   18.89  ? 5    DA  F "C4'" 1 ? 
ATOM   5812 O  "O4'" . DA  C 3 5   ? 5.71    41.437  7.214   1   19.34  ? 5    DA  F "O4'" 1 ? 
ATOM   5813 C  "C3'" . DA  C 3 5   ? 7.039   42.06   5.356   1   19.09  ? 5    DA  F "C3'" 1 ? 
ATOM   5814 O  "O3'" . DA  C 3 5   ? 7.274   43.459  5.499   1   18.9   ? 5    DA  F "O3'" 1 ? 
ATOM   5815 C  "C2'" . DA  C 3 5   ? 7.894   41.219  6.315   1   19.14  ? 5    DA  F "C2'" 1 ? 
ATOM   5816 C  "C1'" . DA  C 3 5   ? 7.067   41.267  7.599   1   19.78  ? 5    DA  F "C1'" 1 ? 
ATOM   5817 N  N9    . DA  C 3 5   ? 7.158   40.048  8.413   1   20.62  ? 5    DA  F N9    1 1 
ATOM   5818 C  C8    . DA  C 3 5   ? 6.992   38.76   7.988   1   20.69  ? 5    DA  F C8    1 1 
ATOM   5819 N  N7    . DA  C 3 5   ? 7.117   37.864  8.943   1   20.94  ? 5    DA  F N7    1 1 
ATOM   5820 C  C5    . DA  C 3 5   ? 7.309   38.619  10.088  1   20.77  ? 5    DA  F C5    1 1 
ATOM   5821 C  C6    . DA  C 3 5   ? 7.474   38.256  11.441  1   20.31  ? 5    DA  F C6    1 1 
ATOM   5822 N  N6    . DA  C 3 5   ? 7.452   36.978  11.872  1   19.31  ? 5    DA  F N6    1 1 
ATOM   5823 N  N1    . DA  C 3 5   ? 7.664   39.249  12.335  1   20.82  ? 5    DA  F N1    1 1 
ATOM   5824 C  C2    . DA  C 3 5   ? 7.736   40.527  11.886  1   21.25  ? 5    DA  F C2    1 1 
ATOM   5825 N  N3    . DA  C 3 5   ? 7.583   40.991  10.64   1   21.02  ? 5    DA  F N3    1 1 
ATOM   5826 C  C4    . DA  C 3 5   ? 7.412   39.967  9.772   1   20.9   ? 5    DA  F C4    1 1 
ATOM   5827 P  P     . DA  C 3 6   ? 8.629   44.123  5.003   1   18.59  ? 6    DA  F P     1 1 
ATOM   5828 O  OP1   . DA  C 3 6   ? 8.374   45.564  4.788   1   18.77  ? 6    DA  F OP1   1 1 
ATOM   5829 O  OP2   . DA  C 3 6   ? 9.185   43.314  3.895   1   18.5   ? 6    DA  F OP2   1 1 
ATOM   5830 O  "O5'" . DA  C 3 6   ? 9.583   43.968  6.281   1   18.58  ? 6    DA  F "O5'" 1 ? 
ATOM   5831 C  "C5'" . DA  C 3 6   ? 9.139   44.514  7.505   1   19.36  ? 6    DA  F "C5'" 1 ? 
ATOM   5832 C  "C4'" . DA  C 3 6   ? 9.97    44.029  8.678   1   20.16  ? 6    DA  F "C4'" 1 ? 
ATOM   5833 O  "O4'" . DA  C 3 6   ? 9.705   42.644  8.966   1   19.83  ? 6    DA  F "O4'" 1 ? 
ATOM   5834 C  "C3'" . DA  C 3 6   ? 11.492  44.138  8.549   1   20.57  ? 6    DA  F "C3'" 1 ? 
ATOM   5835 O  "O3'" . DA  C 3 6   ? 11.936  45.302  9.25    1   21.72  ? 6    DA  F "O3'" 1 ? 
ATOM   5836 C  "C2'" . DA  C 3 6   ? 12.013  42.852  9.223   1   19.52  ? 6    DA  F "C2'" 1 ? 
ATOM   5837 C  "C1'" . DA  C 3 6   ? 10.745  42.227  9.805   1   19.33  ? 6    DA  F "C1'" 1 ? 
ATOM   5838 N  N9    . DA  C 3 6   ? 10.762  40.776  9.844   1   19.21  ? 6    DA  F N9    1 1 
ATOM   5839 C  C8    . DA  C 3 6   ? 10.672  39.911  8.784   1   18.76  ? 6    DA  F C8    1 1 
ATOM   5840 N  N7    . DA  C 3 6   ? 10.673  38.654  9.135   1   18.2   ? 6    DA  F N7    1 1 
ATOM   5841 C  C5    . DA  C 3 6   ? 10.802  38.692  10.511  1   18.15  ? 6    DA  F C5    1 1 
ATOM   5842 C  C6    . DA  C 3 6   ? 10.854  37.68   11.48   1   17.93  ? 6    DA  F C6    1 1 
ATOM   5843 N  N6    . DA  C 3 6   ? 10.842  36.371  11.179  1   17.02  ? 6    DA  F N6    1 1 
ATOM   5844 N  N1    . DA  C 3 6   ? 10.976  38.057  12.768  1   18.48  ? 6    DA  F N1    1 1 
ATOM   5845 C  C2    . DA  C 3 6   ? 10.98   39.356  13.061  1   19.37  ? 6    DA  F C2    1 1 
ATOM   5846 N  N3    . DA  C 3 6   ? 10.949  40.405  12.236  1   19.54  ? 6    DA  F N3    1 1 
ATOM   5847 C  C4    . DA  C 3 6   ? 10.868  39.992  10.962  1   19.13  ? 6    DA  F C4    1 1 
ATOM   5848 P  P     . DT  C 3 7   ? 13.454  45.786  9.187   1   22.17  ? 7    DT  F P     1 1 
ATOM   5849 O  OP1   . DT  C 3 7   ? 13.463  47.233  9.517   1   22     ? 7    DT  F OP1   1 1 
ATOM   5850 O  OP2   . DT  C 3 7   ? 14.065  45.302  7.933   1   21.52  ? 7    DT  F OP2   1 1 
ATOM   5851 O  "O5'" . DT  C 3 7   ? 14.123  44.994  10.384  1   24.09  ? 7    DT  F "O5'" 1 ? 
ATOM   5852 C  "C5'" . DT  C 3 7   ? 13.663  45.229  11.698  1   25.31  ? 7    DT  F "C5'" 1 ? 
ATOM   5853 C  "C4'" . DT  C 3 7   ? 14.161  44.154  12.646  1   25.62  ? 7    DT  F "C4'" 1 ? 
ATOM   5854 O  "O4'" . DT  C 3 7   ? 13.562  42.899  12.33   1   25.01  ? 7    DT  F "O4'" 1 ? 
ATOM   5855 C  "C3'" . DT  C 3 7   ? 15.652  43.862  12.606  1   26.31  ? 7    DT  F "C3'" 1 ? 
ATOM   5856 O  "O3'" . DT  C 3 7   ? 16.351  44.841  13.412  1   28.19  ? 7    DT  F "O3'" 1 ? 
ATOM   5857 C  "C2'" . DT  C 3 7   ? 15.707  42.459  13.241  1   25.28  ? 7    DT  F "C2'" 1 ? 
ATOM   5858 C  "C1'" . DT  C 3 7   ? 14.298  41.907  13.012  1   24.24  ? 7    DT  F "C1'" 1 ? 
ATOM   5859 N  N1    . DT  C 3 7   ? 14.278  40.663  12.234  1   22.9   ? 7    DT  F N1    1 1 
ATOM   5860 C  C2    . DT  C 3 7   ? 14.351  39.463  12.907  1   23.43  ? 7    DT  F C2    1 1 
ATOM   5861 O  O2    . DT  C 3 7   ? 14.375  39.386  14.125  1   24.44  ? 7    DT  F O2    1 1 
ATOM   5862 N  N3    . DT  C 3 7   ? 14.364  38.351  12.104  1   22.16  ? 7    DT  F N3    1 1 
ATOM   5863 C  C4    . DT  C 3 7   ? 14.311  38.334  10.733  1   21.3   ? 7    DT  F C4    1 1 
ATOM   5864 O  O4    . DT  C 3 7   ? 14.322  37.272  10.154  1   21.64  ? 7    DT  F O4    1 1 
ATOM   5865 C  C5    . DT  C 3 7   ? 14.282  39.631  10.088  1   20.31  ? 7    DT  F C5    1 1 
ATOM   5866 C  C7    . DT  C 3 7   ? 14.237  39.727  8.598   1   18.95  ? 7    DT  F C7    1 1 
ATOM   5867 C  C6    . DT  C 3 7   ? 14.283  40.718  10.863  1   21.21  ? 7    DT  F C6    1 1 
ATOM   5868 P  P     . DG  C 3 8   ? 17.933  44.96   13.406  1   30.62  ? 8    DG  F P     1 1 
ATOM   5869 O  OP1   . DG  C 3 8   ? 18.295  46.296  13.935  1   30.69  ? 8    DG  F OP1   1 1 
ATOM   5870 O  OP2   . DG  C 3 8   ? 18.46   44.508  12.092  1   31.02  ? 8    DG  F OP2   1 1 
ATOM   5871 O  "O5'" . DG  C 3 8   ? 18.362  43.871  14.485  1   31.51  ? 8    DG  F "O5'" 1 ? 
ATOM   5872 C  "C5'" . DG  C 3 8   ? 17.802  43.934  15.784  1   31.73  ? 8    DG  F "C5'" 1 ? 
ATOM   5873 C  "C4'" . DG  C 3 8   ? 18.238  42.742  16.601  1   31.83  ? 8    DG  F "C4'" 1 ? 
ATOM   5874 O  "O4'" . DG  C 3 8   ? 17.715  41.52   16.011  1   30.75  ? 8    DG  F "O4'" 1 ? 
ATOM   5875 C  "C3'" . DG  C 3 8   ? 19.747  42.556  16.728  1   32.42  ? 8    DG  F "C3'" 1 ? 
ATOM   5876 O  "O3'" . DG  C 3 8   ? 20.026  42.165  18.046  1   34.57  ? 8    DG  F "O3'" 1 ? 
ATOM   5877 C  "C2'" . DG  C 3 8   ? 20.025  41.428  15.739  1   31.29  ? 8    DG  F "C2'" 1 ? 
ATOM   5878 C  "C1'" . DG  C 3 8   ? 18.756  40.597  15.845  1   30.12  ? 8    DG  F "C1'" 1 ? 
ATOM   5879 N  N9    . DG  C 3 8   ? 18.49   39.786  14.659  1   28.94  ? 8    DG  F N9    1 1 
ATOM   5880 C  C8    . DG  C 3 8   ? 18.474  40.205  13.352  1   28.65  ? 8    DG  F C8    1 1 
ATOM   5881 N  N7    . DG  C 3 8   ? 18.26   39.235  12.493  1   28.62  ? 8    DG  F N7    1 1 
ATOM   5882 C  C5    . DG  C 3 8   ? 18.22   38.091  13.275  1   28.43  ? 8    DG  F C5    1 1 
ATOM   5883 C  C6    . DG  C 3 8   ? 18.069  36.744  12.905  1   28.59  ? 8    DG  F C6    1 1 
ATOM   5884 O  O6    . DG  C 3 8   ? 17.9    36.272  11.775  1   28.81  ? 8    DG  F O6    1 1 
ATOM   5885 N  N1    . DG  C 3 8   ? 18.042  35.906  14.013  1   28.92  ? 8    DG  F N1    1 1 
ATOM   5886 C  C2    . DG  C 3 8   ? 18.174  36.321  15.315  1   29.08  ? 8    DG  F C2    1 1 
ATOM   5887 N  N2    . DG  C 3 8   ? 18.121  35.367  16.255  1   29.62  ? 8    DG  F N2    1 1 
ATOM   5888 N  N3    . DG  C 3 8   ? 18.32   37.575  15.674  1   28.82  ? 8    DG  F N3    1 1 
ATOM   5889 C  C4    . DG  C 3 8   ? 18.36   38.406  14.607  1   28.89  ? 8    DG  F C4    1 1 
ATOM   5890 P  P     . DC  C 3 9   ? 21.484  42.281  18.693  1   36.78  ? 9    DC  F P     1 1 
ATOM   5891 O  OP1   . DC  C 3 9   ? 21.391  43.199  19.855  1   37.77  ? 9    DC  F OP1   1 1 
ATOM   5892 O  OP2   . DC  C 3 9   ? 22.5    42.537  17.629  1   36.33  ? 9    DC  F OP2   1 1 
ATOM   5893 O  "O5'" . DC  C 3 9   ? 21.696  40.807  19.237  1   37.75  ? 9    DC  F "O5'" 1 ? 
ATOM   5894 C  "C5'" . DC  C 3 9   ? 20.708  40.213  20.053  1   38.68  ? 9    DC  F "C5'" 1 ? 
ATOM   5895 C  "C4'" . DC  C 3 9   ? 21.055  38.761  20.311  1   39.74  ? 9    DC  F "C4'" 1 ? 
ATOM   5896 O  "O4'" . DC  C 3 9   ? 20.704  37.963  19.143  1   39.71  ? 9    DC  F "O4'" 1 ? 
ATOM   5897 C  "C3'" . DC  C 3 9   ? 22.534  38.489  20.585  1   40.79  ? 9    DC  F "C3'" 1 ? 
ATOM   5898 O  "O3'" . DC  C 3 9   ? 22.66   37.485  21.58   1   42.52  ? 9    DC  F "O3'" 1 ? 
ATOM   5899 C  "C2'" . DC  C 3 9   ? 23.056  38.002  19.237  1   40.15  ? 9    DC  F "C2'" 1 ? 
ATOM   5900 C  "C1'" . DC  C 3 9   ? 21.84   37.278  18.665  1   39.28  ? 9    DC  F "C1'" 1 ? 
ATOM   5901 N  N1    . DC  C 3 9   ? 21.79   37.299  17.177  1   37.94  ? 9    DC  F N1    1 1 
ATOM   5902 C  C2    . DC  C 3 9   ? 21.608  36.102  16.485  1   36.95  ? 9    DC  F C2    1 1 
ATOM   5903 O  O2    . DC  C 3 9   ? 21.448  35.061  17.133  1   36.65  ? 9    DC  F O2    1 1 
ATOM   5904 N  N3    . DC  C 3 9   ? 21.557  36.126  15.124  1   36.17  ? 9    DC  F N3    1 1 
ATOM   5905 C  C4    . DC  C 3 9   ? 21.699  37.283  14.47   1   35.64  ? 9    DC  F C4    1 1 
ATOM   5906 N  N4    . DC  C 3 9   ? 21.638  37.26   13.135  1   34.47  ? 9    DC  F N4    1 1 
ATOM   5907 C  C5    . DC  C 3 9   ? 21.928  38.518  15.163  1   36.47  ? 9    DC  F C5    1 1 
ATOM   5908 C  C6    . DC  C 3 9   ? 21.948  38.484  16.5    1   37.27  ? 9    DC  F C6    1 1 
ATOM   5909 P  P     . DA  C 3 10  ? 24.054  37.247  22.335  1   44.14  ? 10   DA  F P     1 1 
ATOM   5910 O  OP1   . DA  C 3 10  ? 23.749  37.062  23.775  1   44.44  ? 10   DA  F OP1   1 1 
ATOM   5911 O  OP2   . DA  C 3 10  ? 25.018  38.292  21.896  1   44.36  ? 10   DA  F OP2   1 1 
ATOM   5912 O  "O5'" . DA  C 3 10  ? 24.544  35.853  21.722  1   44.28  ? 10   DA  F "O5'" 1 ? 
ATOM   5913 C  "C5'" . DA  C 3 10  ? 23.576  34.884  21.335  1   43.85  ? 10   DA  F "C5'" 1 ? 
ATOM   5914 C  "C4'" . DA  C 3 10  ? 24.207  33.732  20.577  1   43.47  ? 10   DA  F "C4'" 1 ? 
ATOM   5915 O  "O4'" . DA  C 3 10  ? 24.003  33.909  19.155  1   42.42  ? 10   DA  F "O4'" 1 ? 
ATOM   5916 C  "C3'" . DA  C 3 10  ? 25.704  33.542  20.779  1   43.91  ? 10   DA  F "C3'" 1 ? 
ATOM   5917 O  "O3'" . DA  C 3 10  ? 25.977  32.171  20.86   1   45.37  ? 10   DA  F "O3'" 1 ? 
ATOM   5918 C  "C2'" . DA  C 3 10  ? 26.307  34.172  19.521  1   42.63  ? 10   DA  F "C2'" 1 ? 
ATOM   5919 C  "C1'" . DA  C 3 10  ? 25.236  33.867  18.475  1   40.96  ? 10   DA  F "C1'" 1 ? 
ATOM   5920 N  N9    . DA  C 3 10  ? 25.186  34.844  17.381  1   37.54  ? 10   DA  F N9    1 1 
ATOM   5921 C  C8    . DA  C 3 10  ? 25.308  36.197  17.486  1   36.59  ? 10   DA  F C8    1 1 
ATOM   5922 N  N7    . DA  C 3 10  ? 25.206  36.832  16.338  1   35.76  ? 10   DA  F N7    1 1 
ATOM   5923 C  C5    . DA  C 3 10  ? 25.055  35.815  15.408  1   34.75  ? 10   DA  F C5    1 1 
ATOM   5924 C  C6    . DA  C 3 10  ? 24.917  35.822  14.004  1   33.25  ? 10   DA  F C6    1 1 
ATOM   5925 N  N6    . DA  C 3 10  ? 24.912  36.939  13.268  1   32.43  ? 10   DA  F N6    1 1 
ATOM   5926 N  N1    . DA  C 3 10  ? 24.819  34.635  13.383  1   32.89  ? 10   DA  F N1    1 1 
ATOM   5927 C  C2    . DA  C 3 10  ? 24.831  33.523  14.123  1   33.57  ? 10   DA  F C2    1 1 
ATOM   5928 N  N3    . DA  C 3 10  ? 24.932  33.392  15.444  1   34.42  ? 10   DA  F N3    1 1 
ATOM   5929 C  C4    . DA  C 3 10  ? 25.043  34.584  16.033  1   35.32  ? 10   DA  F C4    1 1 
ATOM   5930 P  P     . DG  C 3 11  ? 27.292  31.629  21.609  1   46.66  ? 11   DG  F P     1 1 
ATOM   5931 O  OP1   . DG  C 3 11  ? 26.838  30.9    22.827  1   47.21  ? 11   DG  F OP1   1 1 
ATOM   5932 O  OP2   . DG  C 3 11  ? 28.29   32.726  21.714  1   46.38  ? 11   DG  F OP2   1 1 
ATOM   5933 O  "O5'" . DG  C 3 11  ? 27.824  30.547  20.565  1   46.29  ? 11   DG  F "O5'" 1 ? 
ATOM   5934 C  "C5'" . DG  C 3 11  ? 26.879  29.772  19.829  1   45.57  ? 11   DG  F "C5'" 1 ? 
ATOM   5935 C  "C4'" . DG  C 3 11  ? 27.458  29.347  18.499  1   44.87  ? 11   DG  F "C4'" 1 ? 
ATOM   5936 O  "O4'" . DG  C 3 11  ? 27.339  30.428  17.537  1   43.69  ? 11   DG  F "O4'" 1 ? 
ATOM   5937 C  "C3'" . DG  C 3 11  ? 28.94   28.983  18.527  1   45.29  ? 11   DG  F "C3'" 1 ? 
ATOM   5938 O  "O3'" . DG  C 3 11  ? 29.143  27.876  17.677  1   47.34  ? 11   DG  F "O3'" 1 ? 
ATOM   5939 C  "C2'" . DG  C 3 11  ? 29.614  30.244  17.98   1   43.59  ? 11   DG  F "C2'" 1 ? 
ATOM   5940 C  "C1'" . DG  C 3 11  ? 28.596  30.648  16.937  1   42.07  ? 11   DG  F "C1'" 1 ? 
ATOM   5941 N  N9    . DG  C 3 11  ? 28.667  32.038  16.505  1   38.9   ? 11   DG  F N9    1 1 
ATOM   5942 C  C8    . DG  C 3 11  ? 28.806  33.155  17.285  1   37.66  ? 11   DG  F C8    1 1 
ATOM   5943 N  N7    . DG  C 3 11  ? 28.701  34.27   16.611  1   36.78  ? 11   DG  F N7    1 1 
ATOM   5944 C  C5    . DG  C 3 11  ? 28.456  33.858  15.309  1   35.98  ? 11   DG  F C5    1 1 
ATOM   5945 C  C6    . DG  C 3 11  ? 28.295  34.611  14.114  1   34.73  ? 11   DG  F C6    1 1 
ATOM   5946 O  O6    . DG  C 3 11  ? 28.321  35.845  13.964  1   33.82  ? 11   DG  F O6    1 1 
ATOM   5947 N  N1    . DG  C 3 11  ? 28.101  33.775  13.011  1   34.62  ? 11   DG  F N1    1 1 
ATOM   5948 C  C2    . DG  C 3 11  ? 28.069  32.396  13.063  1   34.54  ? 11   DG  F C2    1 1 
ATOM   5949 N  N2    . DG  C 3 11  ? 27.853  31.755  11.917  1   33.91  ? 11   DG  F N2    1 1 
ATOM   5950 N  N3    . DG  C 3 11  ? 28.21   31.699  14.165  1   35.49  ? 11   DG  F N3    1 1 
ATOM   5951 C  C4    . DG  C 3 11  ? 28.432  32.488  15.237  1   36.79  ? 11   DG  F C4    1 1 
ATOM   5952 P  P     . DA  C 3 12  ? 30.305  26.824  17.982  1   49.08  ? 12   DA  F P     1 1 
ATOM   5953 O  OP1   . DA  C 3 12  ? 29.653  25.533  18.328  1   49.22  ? 12   DA  F OP1   1 1 
ATOM   5954 O  OP2   . DA  C 3 12  ? 31.291  27.457  18.916  1   48.96  ? 12   DA  F OP2   1 1 
ATOM   5955 O  "O5'" . DA  C 3 12  ? 31.01   26.693  16.556  1   48.87  ? 12   DA  F "O5'" 1 ? 
ATOM   5956 C  "C5'" . DA  C 3 12  ? 30.21   26.748  15.386  1   48     ? 12   DA  F "C5'" 1 ? 
ATOM   5957 C  "C4'" . DA  C 3 12  ? 30.972  27.374  14.234  1   47.14  ? 12   DA  F "C4'" 1 ? 
ATOM   5958 O  "O4'" . DA  C 3 12  ? 30.729  28.795  14.199  1   46.07  ? 12   DA  F "O4'" 1 ? 
ATOM   5959 C  "C3'" . DA  C 3 12  ? 32.492  27.185  14.26   1   47.08  ? 12   DA  F "C3'" 1 ? 
ATOM   5960 O  "O3'" . DA  C 3 12  ? 32.875  26.433  13.106  1   48.55  ? 12   DA  F "O3'" 1 ? 
ATOM   5961 C  "C2'" . DA  C 3 12  ? 33.052  28.621  14.239  1   45.73  ? 12   DA  F "C2'" 1 ? 
ATOM   5962 C  "C1'" . DA  C 3 12  ? 31.874  29.438  13.716  1   44.57  ? 12   DA  F "C1'" 1 ? 
ATOM   5963 N  N9    . DA  C 3 12  ? 31.85   30.838  14.171  1   41.94  ? 12   DA  F N9    1 1 
ATOM   5964 C  C8    . DA  C 3 12  ? 32.052  31.308  15.443  1   40.93  ? 12   DA  F C8    1 1 
ATOM   5965 N  N7    . DA  C 3 12  ? 31.993  32.623  15.543  1   39.87  ? 12   DA  F N7    1 1 
ATOM   5966 C  C5    . DA  C 3 12  ? 31.718  33.043  14.255  1   39.22  ? 12   DA  F C5    1 1 
ATOM   5967 C  C6    . DA  C 3 12  ? 31.543  34.326  13.687  1   38     ? 12   DA  F C6    1 1 
ATOM   5968 N  N6    . DA  C 3 12  ? 31.582  35.464  14.393  1   37.56  ? 12   DA  F N6    1 1 
ATOM   5969 N  N1    . DA  C 3 12  ? 31.344  34.397  12.362  1   38.07  ? 12   DA  F N1    1 1 
ATOM   5970 C  C2    . DA  C 3 12  ? 31.288  33.261  11.655  1   39.02  ? 12   DA  F C2    1 1 
ATOM   5971 N  N3    . DA  C 3 12  ? 31.416  31.996  12.073  1   39.88  ? 12   DA  F N3    1 1 
ATOM   5972 C  C4    . DA  C 3 12  ? 31.656  31.958  13.391  1   40.38  ? 12   DA  F C4    1 1 
ATOM   5973 P  P     . DC  C 3 13  ? 34.37   25.859  12.909  1   50.21  ? 13   DC  F P     1 1 
ATOM   5974 O  OP1   . DC  C 3 13  ? 34.235  24.521  12.283  1   50.46  ? 13   DC  F OP1   1 1 
ATOM   5975 O  OP2   . DC  C 3 13  ? 35.139  26.019  14.18   1   50.27  ? 13   DC  F OP2   1 1 
ATOM   5976 O  "O5'" . DC  C 3 13  ? 34.985  26.884  11.829  1   50.21  ? 13   DC  F "O5'" 1 ? 
ATOM   5977 C  "C5'" . DC  C 3 13  ? 34.123  27.404  10.808  1   50.07  ? 13   DC  F "C5'" 1 ? 
ATOM   5978 C  "C4'" . DC  C 3 13  ? 34.622  28.732  10.259  1   49.69  ? 13   DC  F "C4'" 1 ? 
ATOM   5979 O  "O4'" . DC  C 3 13  ? 34.234  29.827  11.119  1   49.28  ? 13   DC  F "O4'" 1 ? 
ATOM   5980 C  "C3'" . DC  C 3 13  ? 36.135  28.854  10.085  1   49.33  ? 13   DC  F "C3'" 1 ? 
ATOM   5981 O  "O3'" . DC  C 3 13  ? 36.459  28.731  8.703   1   49.55  ? 13   DC  F "O3'" 1 ? 
ATOM   5982 C  "C2'" . DC  C 3 13  ? 36.471  30.263  10.625  1   48.67  ? 13   DC  F "C2'" 1 ? 
ATOM   5983 C  "C1'" . DC  C 3 13  ? 35.092  30.894  10.828  1   48.29  ? 13   DC  F "C1'" 1 ? 
ATOM   5984 N  N1    . DC  C 3 13  ? 35.039  31.881  11.937  1   46.94  ? 13   DC  F N1    1 1 
ATOM   5985 C  C2    . DC  C 3 13  ? 34.842  33.231  11.636  1   46.17  ? 13   DC  F C2    1 1 
ATOM   5986 O  O2    . DC  C 3 13  ? 34.642  33.556  10.46   1   46.46  ? 13   DC  F O2    1 1 
ATOM   5987 N  N3    . DC  C 3 13  ? 34.831  34.137  12.642  1   45.22  ? 13   DC  F N3    1 1 
ATOM   5988 C  C4    . DC  C 3 13  ? 35.042  33.74   13.895  1   44.98  ? 13   DC  F C4    1 1 
ATOM   5989 N  N4    . DC  C 3 13  ? 35.009  34.668  14.855  1   44.81  ? 13   DC  F N4    1 1 
ATOM   5990 C  C5    . DC  C 3 13  ? 35.27   32.371  14.223  1   45.53  ? 13   DC  F C5    1 1 
ATOM   5991 C  C6    . DC  C 3 13  ? 35.263  31.482  13.221  1   46.2   ? 13   DC  F C6    1 1 
HETATM 5992 CL CL    . CL  D 4 .   ? -9.855  17.582  6.871   1   48.15  ? 701  CL  A CL    1 1 
HETATM 5993 O  O1    . MES E 5 .   ? 0.451   50.712  -21.01  1   30.02  ? 702  MES A O1    1 1 
HETATM 5994 C  C2    . MES E 5 .   ? 0.05    49.664  -20.125 1   30.13  ? 702  MES A C2    1 1 
HETATM 5995 C  C3    . MES E 5 .   ? -1.179  50.046  -19.338 1   30.7   ? 702  MES A C3    1 1 
HETATM 5996 N  N4    . MES E 5 .   ? -0.932  51.315  -18.579 1   31.12  ? 702  MES A N4    1 1 
HETATM 5997 C  C5    . MES E 5 .   ? -0.427  52.402  -19.49  1   30.5   ? 702  MES A C5    1 1 
HETATM 5998 C  C6    . MES E 5 .   ? 0.767   51.905  -20.275 1   30.25  ? 702  MES A C6    1 1 
HETATM 5999 C  C7    . MES E 5 .   ? -2.191  51.723  -17.87  1   31.96  ? 702  MES A C7    1 1 
HETATM 6000 C  C8    . MES E 5 .   ? -1.849  52.436  -16.579 1   33.32  ? 702  MES A C8    1 1 
HETATM 6001 S  S     . MES E 5 .   ? -3.328  53.035  -15.798 1   34.77  ? 702  MES A S     1 1 
HETATM 6002 O  O1S   . MES E 5 .   ? -3.826  51.949  -14.966 1   34.26  ? 702  MES A O1S   1 1 
HETATM 6003 O  O2S   . MES E 5 .   ? -4.244  53.376  -16.877 1   34.78  ? 702  MES A O2S   1 1 
HETATM 6004 O  O3S   . MES E 5 .   ? -2.919  54.205  -15.023 1   34.8   ? 702  MES A O3S   1 1 
HETATM 6005 O  O     . HOH F 6 .   ? 28.258  16.896  24.511  1   26.89  ? 801  HOH A O     1 1 
HETATM 6006 O  O     . HOH F 6 .   ? 30.452  16.157  4.954   1   17.33  ? 802  HOH A O     1 1 
HETATM 6007 O  O     . HOH F 6 .   ? 40.608  11.015  39.219  1   52.19  ? 803  HOH A O     1 1 
HETATM 6008 O  O     . HOH F 6 .   ? -15.777 27.323  3.156   1   35.5   ? 804  HOH A O     1 1 
HETATM 6009 O  O     . HOH F 6 .   ? 32.179  1.744   7.11    1   26.24  ? 805  HOH A O     1 1 
HETATM 6010 O  O     . HOH F 6 .   ? 0.04    40.371  -22.523 1   24.65  ? 806  HOH A O     1 1 
HETATM 6011 O  O     . HOH F 6 .   ? 31.76   16.387  -6.844  1   30.92  ? 807  HOH A O     1 1 
HETATM 6012 O  O     . HOH F 6 .   ? 20.171  19.505  45.517  1   44.66  ? 808  HOH A O     1 1 
HETATM 6013 O  O     . HOH F 6 .   ? 12.677  52.869  4.651   1   28.67  ? 809  HOH A O     1 1 
HETATM 6014 O  O     . HOH F 6 .   ? 6.508   23.506  24.395  1   24.07  ? 810  HOH A O     1 1 
HETATM 6015 O  O     . HOH F 6 .   ? 27.636  49.906  -7.956  1   23.75  ? 811  HOH A O     1 1 
HETATM 6016 O  O     . HOH F 6 .   ? 27.551  19.055  11.446  1   23.04  ? 812  HOH A O     1 1 
HETATM 6017 O  O     . HOH F 6 .   ? 34.799  15.569  -1.288  1   28.04  ? 813  HOH A O     1 1 
HETATM 6018 O  O     . HOH F 6 .   ? -0.363  35.624  -3.887  1   16.1   ? 814  HOH A O     1 1 
HETATM 6019 O  O     . HOH F 6 .   ? 27.455  59.096  -0.135  1   42.77  ? 815  HOH A O     1 1 
HETATM 6020 O  O     . HOH F 6 .   ? -11.55  27.033  4.823   1   46.13  ? 816  HOH A O     1 1 
HETATM 6021 O  O     . HOH F 6 .   ? 30.858  46.053  -14.764 1   36.22  ? 817  HOH A O     1 1 
HETATM 6022 O  O     . HOH F 6 .   ? 14.39   0.24    -2.101  1   20.91  ? 818  HOH A O     1 1 
HETATM 6023 O  O     . HOH F 6 .   ? 24.382  41.85   -12.192 1   51.17  ? 819  HOH A O     1 1 
HETATM 6024 O  O     . HOH F 6 .   ? 14.83   33.152  -1.925  1   15.23  ? 820  HOH A O     1 1 
HETATM 6025 O  O     . HOH F 6 .   ? -8.346  14.611  -1.961  1   37.01  ? 821  HOH A O     1 1 
HETATM 6026 O  O     . HOH F 6 .   ? 18.963  20.623  8.501   1   26.79  ? 822  HOH A O     1 1 
HETATM 6027 O  O     . HOH F 6 .   ? 15.754  10.961  33.23   1   35.21  ? 823  HOH A O     1 1 
HETATM 6028 O  O     . HOH F 6 .   ? 22.45   18.367  23.211  1   37.21  ? 824  HOH A O     1 1 
HETATM 6029 O  O     . HOH F 6 .   ? 13.601  10.54   40.613  1   36     ? 825  HOH A O     1 1 
HETATM 6030 O  O     . HOH F 6 .   ? 47.93   16.851  31.804  1   50.87  ? 826  HOH A O     1 1 
HETATM 6031 O  O     . HOH F 6 .   ? 6.927   23.35   31.48   1   40.22  ? 827  HOH A O     1 1 
HETATM 6032 O  O     . HOH F 6 .   ? 9.405   -2.086  5.582   1   24.25  ? 828  HOH A O     1 1 
HETATM 6033 O  O     . HOH F 6 .   ? 20.545  45.498  10.413  1   24.15  ? 829  HOH A O     1 1 
HETATM 6034 O  O     . HOH F 6 .   ? -10.27  19.634  20.203  1   36.71  ? 830  HOH A O     1 1 
HETATM 6035 O  O     . HOH F 6 .   ? 5.527   24.916  29.406  1   30.56  ? 831  HOH A O     1 1 
HETATM 6036 O  O     . HOH F 6 .   ? 32.455  35.228  -3.781  1   54.26  ? 832  HOH A O     1 1 
HETATM 6037 O  O     . HOH F 6 .   ? 13.928  49.336  2.103   1   22.25  ? 833  HOH A O     1 1 
HETATM 6038 O  O     . HOH F 6 .   ? 8.989   24.246  1.448   1   22.72  ? 834  HOH A O     1 1 
HETATM 6039 O  O     . HOH F 6 .   ? 39.734  7.806   13.8    1   42.68  ? 835  HOH A O     1 1 
HETATM 6040 O  O     . HOH F 6 .   ? 2.71    11.847  8.416   1   27.94  ? 836  HOH A O     1 1 
HETATM 6041 O  O     . HOH F 6 .   ? 4.238   22.881  -10.057 1   20.75  ? 837  HOH A O     1 1 
HETATM 6042 O  O     . HOH F 6 .   ? 11.385  20.209  22.681  1   25.77  ? 838  HOH A O     1 1 
HETATM 6043 O  O     . HOH F 6 .   ? 29.608  19.892  -1.719  1   34.12  ? 839  HOH A O     1 1 
HETATM 6044 O  O     . HOH F 6 .   ? 17.229  7.789   -5.17   1   40.8   ? 840  HOH A O     1 1 
HETATM 6045 O  O     . HOH F 6 .   ? 15.346  64.546  -0.466  1   34.3   ? 841  HOH A O     1 1 
HETATM 6046 O  O     . HOH F 6 .   ? 6.213   31.158  -16.383 1   27.57  ? 842  HOH A O     1 1 
HETATM 6047 O  O     . HOH F 6 .   ? 26.692  -3.09   2.251   1   19.12  ? 843  HOH A O     1 1 
HETATM 6048 O  O     . HOH F 6 .   ? -1.716  7.186   11.372  1   30.2   ? 844  HOH A O     1 1 
HETATM 6049 O  O     . HOH F 6 .   ? 18.694  26.529  4.788   1   35.46  ? 845  HOH A O     1 1 
HETATM 6050 O  O     . HOH F 6 .   ? 38.085  11.325  6.731   1   16.2   ? 846  HOH A O     1 1 
HETATM 6051 O  O     . HOH F 6 .   ? -6.601  14.823  1.655   1   22.53  ? 847  HOH A O     1 1 
HETATM 6052 O  O     . HOH F 6 .   ? 24.504  46.431  -13.202 1   40.26  ? 848  HOH A O     1 1 
HETATM 6053 O  O     . HOH F 6 .   ? -5.034  27.403  1.571   1   25.56  ? 849  HOH A O     1 1 
HETATM 6054 O  O     . HOH F 6 .   ? -2.153  34.074  4.428   1   24.41  ? 850  HOH A O     1 1 
HETATM 6055 O  O     . HOH F 6 .   ? 14.526  -10.454 14.688  1   35.71  ? 851  HOH A O     1 1 
HETATM 6056 O  O     . HOH F 6 .   ? -2.551  28.938  1.02    1   17.02  ? 852  HOH A O     1 1 
HETATM 6057 O  O     . HOH F 6 .   ? 3.996   3.864   36.095  1   50.58  ? 853  HOH A O     1 1 
HETATM 6058 O  O     . HOH F 6 .   ? 19.839  10.551  -7.714  1   27.42  ? 854  HOH A O     1 1 
HETATM 6059 O  O     . HOH F 6 .   ? -3.427  9.895   -3.414  1   42.25  ? 855  HOH A O     1 1 
HETATM 6060 O  O     . HOH F 6 .   ? 20.522  42.659  12.368  1   29.4   ? 856  HOH A O     1 1 
HETATM 6061 O  O     . HOH F 6 .   ? -3.98   40.44   -23.396 1   38.14  ? 857  HOH A O     1 1 
HETATM 6062 O  O     . HOH F 6 .   ? 9.366   21.942  -8.289  1   21.13  ? 858  HOH A O     1 1 
HETATM 6063 O  O     . HOH F 6 .   ? 20.297  4.674   19.743  1   31.68  ? 859  HOH A O     1 1 
HETATM 6064 O  O     . HOH F 6 .   ? -3.269  36.762  6.208   1   59.16  ? 860  HOH A O     1 1 
HETATM 6065 O  O     . HOH F 6 .   ? 24.867  23.862  4.18    1   40.91  ? 861  HOH A O     1 1 
HETATM 6066 O  O     . HOH F 6 .   ? 2.654   39.868  1.806   1   16.75  ? 862  HOH A O     1 1 
HETATM 6067 O  O     . HOH F 6 .   ? -5.739  44.451  -14.547 1   26.04  ? 863  HOH A O     1 1 
HETATM 6068 O  O     . HOH F 6 .   ? 47.903  6.629   25.564  1   40.15  ? 864  HOH A O     1 1 
HETATM 6069 O  O     . HOH F 6 .   ? 8.941   30.915  -21.644 1   44.06  ? 865  HOH A O     1 1 
HETATM 6070 O  O     . HOH F 6 .   ? 5.931   23.114  26.74   1   30.57  ? 866  HOH A O     1 1 
HETATM 6071 O  O     . HOH F 6 .   ? 13.676  2.161   19.041  1   19.75  ? 867  HOH A O     1 1 
HETATM 6072 O  O     . HOH F 6 .   ? 4.772   14.816  -0.374  1   21.99  ? 868  HOH A O     1 1 
HETATM 6073 O  O     . HOH F 6 .   ? 4.964   17.738  21.59   1   26.96  ? 869  HOH A O     1 1 
HETATM 6074 O  O     . HOH F 6 .   ? -3.452  26.878  20.888  1   24.94  ? 870  HOH A O     1 1 
HETATM 6075 O  O     . HOH F 6 .   ? 23.47   44.088  1.654   1   25.56  ? 871  HOH A O     1 1 
HETATM 6076 O  O     . HOH F 6 .   ? 25.601  11.412  -6.356  1   22.75  ? 872  HOH A O     1 1 
HETATM 6077 O  O     . HOH F 6 .   ? 28.984  31.182  29.809  1   51.45  ? 873  HOH A O     1 1 
HETATM 6078 O  O     . HOH F 6 .   ? 10.921  27.646  24.55   1   36.32  ? 874  HOH A O     1 1 
HETATM 6079 O  O     . HOH F 6 .   ? 21.493  38.408  9.058   1   21.25  ? 875  HOH A O     1 1 
HETATM 6080 O  O     . HOH F 6 .   ? 6.256   24.369  8.902   1   26.38  ? 876  HOH A O     1 1 
HETATM 6081 O  O     . HOH F 6 .   ? 24.79   14.764  19.643  1   29.8   ? 877  HOH A O     1 1 
HETATM 6082 O  O     . HOH F 6 .   ? 14.862  23.197  22.641  1   50.06  ? 878  HOH A O     1 1 
HETATM 6083 O  O     . HOH F 6 .   ? -9.308  22.046  13.931  1   21.93  ? 879  HOH A O     1 1 
HETATM 6084 O  O     . HOH F 6 .   ? 20.478  55.306  -0.793  1   21.21  ? 880  HOH A O     1 1 
HETATM 6085 O  O     . HOH F 6 .   ? -11.07  38.214  -2.687  1   56.56  ? 881  HOH A O     1 1 
HETATM 6086 O  O     . HOH F 6 .   ? 23.087  19.837  -0.58   1   23.68  ? 882  HOH A O     1 1 
HETATM 6087 O  O     . HOH F 6 .   ? 38.492  7.323   1.91    1   24.6   ? 883  HOH A O     1 1 
HETATM 6088 O  O     . HOH F 6 .   ? 37.58   17.12   12.508  1   20.12  ? 884  HOH A O     1 1 
HETATM 6089 O  O     . HOH F 6 .   ? 37.057  30.447  29.153  1   43.76  ? 885  HOH A O     1 1 
HETATM 6090 O  O     . HOH F 6 .   ? -7.308  16.269  6.888   1   17.04  ? 886  HOH A O     1 1 
HETATM 6091 O  O     . HOH F 6 .   ? 28.861  23.144  39.607  1   46.74  ? 887  HOH A O     1 1 
HETATM 6092 O  O     . HOH F 6 .   ? 12.008  6.557   -2.359  1   29.84  ? 888  HOH A O     1 1 
HETATM 6093 O  O     . HOH F 6 .   ? 23.675  53.264  -11.274 1   37.67  ? 889  HOH A O     1 1 
HETATM 6094 O  O     . HOH F 6 .   ? 30.256  31.977  2.075   1   50.75  ? 890  HOH A O     1 1 
HETATM 6095 O  O     . HOH F 6 .   ? -8.785  9.754   6.865   1   30.47  ? 891  HOH A O     1 1 
HETATM 6096 O  O     . HOH F 6 .   ? -2.159  41.82   1.694   1   22.54  ? 892  HOH A O     1 1 
HETATM 6097 O  O     . HOH F 6 .   ? 21.932  8.788   42.693  1   45.98  ? 893  HOH A O     1 1 
HETATM 6098 O  O     . HOH F 6 .   ? 43.746  9.105   14.235  1   35.73  ? 894  HOH A O     1 1 
HETATM 6099 O  O     . HOH F 6 .   ? 13.425  21.07   -9.288  1   20.96  ? 895  HOH A O     1 1 
HETATM 6100 O  O     . HOH F 6 .   ? 2.181   38.186  -23.246 1   30.11  ? 896  HOH A O     1 1 
HETATM 6101 O  O     . HOH F 6 .   ? 43.394  14.411  28.459  1   34.31  ? 897  HOH A O     1 1 
HETATM 6102 O  O     . HOH F 6 .   ? 2.781   27.754  17.5    1   37.22  ? 898  HOH A O     1 1 
HETATM 6103 O  O     . HOH F 6 .   ? 1.528   30.938  9.572   1   16.27  ? 899  HOH A O     1 1 
HETATM 6104 O  O     . HOH F 6 .   ? 43.299  15.921  17.091  1   22.17  ? 900  HOH A O     1 1 
HETATM 6105 O  O     . HOH F 6 .   ? 26.641  30.223  -13.557 1   43.19  ? 901  HOH A O     1 1 
HETATM 6106 O  O     . HOH F 6 .   ? 16.201  28.069  2.651   1   14.3   ? 902  HOH A O     1 1 
HETATM 6107 O  O     . HOH F 6 .   ? 30.058  7.135   -4.235  1   17.7   ? 903  HOH A O     1 1 
HETATM 6108 O  O     . HOH F 6 .   ? 40.5    16.338  6.272   1   55     ? 904  HOH A O     1 1 
HETATM 6109 O  O     . HOH F 6 .   ? -2.651  38.572  -14.405 1   26.31  ? 905  HOH A O     1 1 
HETATM 6110 O  O     . HOH F 6 .   ? 32.848  19.981  -0.752  1   37.05  ? 906  HOH A O     1 1 
HETATM 6111 O  O     . HOH F 6 .   ? 29.105  28.788  -1.999  1   51.59  ? 907  HOH A O     1 1 
HETATM 6112 O  O     . HOH F 6 .   ? 12.811  -12.15  3.795   1   32.2   ? 908  HOH A O     1 1 
HETATM 6113 O  O     . HOH F 6 .   ? 24.75   7.939   -4.306  1   25.02  ? 909  HOH A O     1 1 
HETATM 6114 O  O     . HOH F 6 .   ? 9.593   57.122  -17.661 1   43.15  ? 910  HOH A O     1 1 
HETATM 6115 O  O     . HOH F 6 .   ? 16.685  -12.251 1.61    1   32.19  ? 911  HOH A O     1 1 
HETATM 6116 O  O     . HOH F 6 .   ? 45.945  17.441  7.53    1   18.25  ? 912  HOH A O     1 1 
HETATM 6117 O  O     . HOH F 6 .   ? 12.877  36.584  -21.802 1   38.6   ? 913  HOH A O     1 1 
HETATM 6118 O  O     . HOH F 6 .   ? 25.084  21.354  -8.089  1   27.56  ? 914  HOH A O     1 1 
HETATM 6119 O  O     . HOH F 6 .   ? -4.993  26.277  9.223   1   17.18  ? 915  HOH A O     1 1 
HETATM 6120 O  O     . HOH F 6 .   ? 16.91   1.151   -1.519  1   32.8   ? 916  HOH A O     1 1 
HETATM 6121 O  O     . HOH F 6 .   ? 18.79   55.47   -9.019  1   45.14  ? 917  HOH A O     1 1 
HETATM 6122 O  O     . HOH F 6 .   ? -8.879  28.148  2.442   1   23.07  ? 918  HOH A O     1 1 
HETATM 6123 O  O     . HOH F 6 .   ? 4.191   1.549   5.722   1   31.95  ? 919  HOH A O     1 1 
HETATM 6124 O  O     . HOH F 6 .   ? 1.673   22.918  -7.838  1   32.91  ? 920  HOH A O     1 1 
HETATM 6125 O  O     . HOH F 6 .   ? -4.042  35.337  2.435   1   31.22  ? 921  HOH A O     1 1 
HETATM 6126 O  O     . HOH F 6 .   ? 27.166  21.772  7.463   1   33.57  ? 922  HOH A O     1 1 
HETATM 6127 O  O     . HOH F 6 .   ? 28.368  31.678  -8.133  1   34.25  ? 923  HOH A O     1 1 
HETATM 6128 O  O     . HOH F 6 .   ? 11.53   28.083  28.389  1   26.01  ? 924  HOH A O     1 1 
HETATM 6129 O  O     . HOH F 6 .   ? 6.43    51.826  -20.951 1   35.49  ? 925  HOH A O     1 1 
HETATM 6130 O  O     . HOH F 6 .   ? 42.55   26.464  18.523  1   35.91  ? 926  HOH A O     1 1 
HETATM 6131 O  O     . HOH F 6 .   ? 26.003  25.065  -16.651 1   28.17  ? 927  HOH A O     1 1 
HETATM 6132 O  O     . HOH F 6 .   ? 9.55    11.574  24.588  1   35.81  ? 928  HOH A O     1 1 
HETATM 6133 O  O     . HOH F 6 .   ? 30.583  12.366  6.969   1   15.75  ? 929  HOH A O     1 1 
HETATM 6134 O  O     . HOH F 6 .   ? 8.421   22.048  10.497  1   48.72  ? 930  HOH A O     1 1 
HETATM 6135 O  O     . HOH F 6 .   ? 32.563  11.612  16.54   1   19.91  ? 931  HOH A O     1 1 
HETATM 6136 O  O     . HOH F 6 .   ? -5.058  41.556  -14.864 1   42.84  ? 932  HOH A O     1 1 
HETATM 6137 O  O     . HOH F 6 .   ? 45.365  15.376  9.548   1   28.63  ? 933  HOH A O     1 1 
HETATM 6138 O  O     . HOH F 6 .   ? 31.574  -5.644  12.642  1   22.11  ? 934  HOH A O     1 1 
HETATM 6139 O  O     . HOH F 6 .   ? 22.971  19.504  9.364   1   40.42  ? 935  HOH A O     1 1 
HETATM 6140 O  O     . HOH F 6 .   ? 14.014  42.803  6.514   1   26.12  ? 936  HOH A O     1 1 
HETATM 6141 O  O     . HOH F 6 .   ? 15.353  49.236  6.084   1   28.43  ? 937  HOH A O     1 1 
HETATM 6142 O  O     . HOH F 6 .   ? 5.388   5.947   13.708  1   27.85  ? 938  HOH A O     1 1 
HETATM 6143 O  O     . HOH F 6 .   ? 17.668  31.482  35.104  1   37.42  ? 939  HOH A O     1 1 
HETATM 6144 O  O     . HOH F 6 .   ? 27.494  2.56    19.286  1   23.67  ? 940  HOH A O     1 1 
HETATM 6145 O  O     . HOH F 6 .   ? -9.535  13.053  3.416   1   43.98  ? 941  HOH A O     1 1 
HETATM 6146 O  O     . HOH F 6 .   ? 26.088  48.388  7.253   1   28.79  ? 942  HOH A O     1 1 
HETATM 6147 O  O     . HOH F 6 .   ? 45.028  22.381  18.362  1   24.32  ? 943  HOH A O     1 1 
HETATM 6148 O  O     . HOH F 6 .   ? 6.917   25.035  19.068  1   36.82  ? 944  HOH A O     1 1 
HETATM 6149 O  O     . HOH F 6 .   ? -11.277 19.269  -6.33   1   30.77  ? 945  HOH A O     1 1 
HETATM 6150 O  O     . HOH F 6 .   ? 15.81   23.427  -15.245 1   42.52  ? 946  HOH A O     1 1 
HETATM 6151 O  O     . HOH F 6 .   ? 19.785  20.214  28.145  1   35.88  ? 947  HOH A O     1 1 
HETATM 6152 O  O     . HOH F 6 .   ? 9.473   44.809  12.089  1   19.77  ? 948  HOH A O     1 1 
HETATM 6153 O  O     . HOH F 6 .   ? 17.927  -16.348 16.61   1   34.15  ? 949  HOH A O     1 1 
HETATM 6154 O  O     . HOH F 6 .   ? 36.219  9.589   -0.916  1   20.67  ? 950  HOH A O     1 1 
HETATM 6155 O  O     . HOH F 6 .   ? -10.582 17.642  -8.478  1   29.05  ? 951  HOH A O     1 1 
HETATM 6156 O  O     . HOH F 6 .   ? 24.089  39.028  5.556   1   31.4   ? 952  HOH A O     1 1 
HETATM 6157 O  O     . HOH F 6 .   ? 3.867   53.491  -14.79  1   34.14  ? 953  HOH A O     1 1 
HETATM 6158 O  O     . HOH F 6 .   ? 22.221  22.356  24.418  1   43.66  ? 954  HOH A O     1 1 
HETATM 6159 O  O     . HOH F 6 .   ? 12.055  26.395  7.43    1   18.99  ? 955  HOH A O     1 1 
HETATM 6160 O  O     . HOH F 6 .   ? -3.652  8.244   6.163   1   26.12  ? 956  HOH A O     1 1 
HETATM 6161 O  O     . HOH F 6 .   ? -8.048  30.484  -6.734  1   38.72  ? 957  HOH A O     1 1 
HETATM 6162 O  O     . HOH F 6 .   ? -2.498  27.271  8.601   1   22.08  ? 958  HOH A O     1 1 
HETATM 6163 O  O     . HOH F 6 .   ? 24.352  -1.836  2.464   1   25.1   ? 959  HOH A O     1 1 
HETATM 6164 O  O     . HOH F 6 .   ? 3.331   42.08   -25.9   1   28.67  ? 960  HOH A O     1 1 
HETATM 6165 O  O     . HOH F 6 .   ? 23.037  55.397  5.021   1   27.65  ? 961  HOH A O     1 1 
HETATM 6166 O  O     . HOH F 6 .   ? 21.473  24.104  5.481   1   48.59  ? 962  HOH A O     1 1 
HETATM 6167 O  O     . HOH F 6 .   ? 29.115  13.642  8.709   1   21.42  ? 963  HOH A O     1 1 
HETATM 6168 O  O     . HOH F 6 .   ? 2.221   29.103  -16.397 1   26.91  ? 964  HOH A O     1 1 
HETATM 6169 O  O     . HOH F 6 .   ? 10.559  35.677  3.462   1   16.07  ? 965  HOH A O     1 1 
HETATM 6170 O  O     . HOH F 6 .   ? 27.889  5.069   20.599  1   31.76  ? 966  HOH A O     1 1 
HETATM 6171 O  O     . HOH F 6 .   ? 12.516  29.979  -16.603 1   27.11  ? 967  HOH A O     1 1 
HETATM 6172 O  O     . HOH F 6 .   ? 8.03    5.277   12.001  1   21.93  ? 968  HOH A O     1 1 
HETATM 6173 O  O     . HOH F 6 .   ? 19.629  -6.72   3.845   1   15     ? 969  HOH A O     1 1 
HETATM 6174 O  O     . HOH F 6 .   ? 9.824   4.259   -5.505  1   35.8   ? 970  HOH A O     1 1 
HETATM 6175 O  O     . HOH F 6 .   ? 29.333  42.38   -0.237  1   50.79  ? 971  HOH A O     1 1 
HETATM 6176 O  O     . HOH F 6 .   ? 28.458  14.158  18.031  1   17.42  ? 972  HOH A O     1 1 
HETATM 6177 O  O     . HOH F 6 .   ? 21.11   42.364  -17.168 1   28.21  ? 973  HOH A O     1 1 
HETATM 6178 O  O     . HOH F 6 .   ? 0.27    12.987  22.489  1   53.74  ? 974  HOH A O     1 1 
HETATM 6179 O  O     . HOH F 6 .   ? 3.39    12.037  5.783   1   13.94  ? 975  HOH A O     1 1 
HETATM 6180 O  O     . HOH F 6 .   ? -7.406  16.868  9.529   1   26.99  ? 976  HOH A O     1 1 
HETATM 6181 O  O     . HOH F 6 .   ? 18.598  24.844  -17.847 1   30.49  ? 977  HOH A O     1 1 
HETATM 6182 O  O     . HOH F 6 .   ? 17.297  55.763  0.124   1   25.71  ? 978  HOH A O     1 1 
HETATM 6183 O  O     . HOH F 6 .   ? -0.813  49.163  -2.643  1   41.29  ? 979  HOH A O     1 1 
HETATM 6184 O  O     . HOH F 6 .   ? 18.93   10.358  19.554  1   32.97  ? 980  HOH A O     1 1 
HETATM 6185 O  O     . HOH F 6 .   ? -9.63   9.136   10.17   1   24.2   ? 981  HOH A O     1 1 
HETATM 6186 O  O     . HOH F 6 .   ? 9.324   21.368  38.701  1   29.38  ? 982  HOH A O     1 1 
HETATM 6187 O  O     . HOH F 6 .   ? 2.912   34.046  12.483  1   36.45  ? 983  HOH A O     1 1 
HETATM 6188 O  O     . HOH F 6 .   ? 29.383  16.52   -13.195 1   46.21  ? 984  HOH A O     1 1 
HETATM 6189 O  O     . HOH F 6 .   ? -7.508  45.711  -7.087  1   45.92  ? 985  HOH A O     1 1 
HETATM 6190 O  O     . HOH F 6 .   ? 1.614   42.861  -4.547  1   19.87  ? 986  HOH A O     1 1 
HETATM 6191 O  O     . HOH F 6 .   ? 17.009  5.87    -2.794  1   27.2   ? 987  HOH A O     1 1 
HETATM 6192 O  O     . HOH F 6 .   ? 27.65   50.546  2.533   1   22.14  ? 988  HOH A O     1 1 
HETATM 6193 O  O     . HOH F 6 .   ? -2.074  7.233   4.343   1   20.13  ? 989  HOH A O     1 1 
HETATM 6194 O  O     . HOH F 6 .   ? 6.255   50.753  9.44    1   27.66  ? 990  HOH A O     1 1 
HETATM 6195 O  O     . HOH F 6 .   ? 19.829  9.664   31.871  1   24.27  ? 991  HOH A O     1 1 
HETATM 6196 O  O     . HOH F 6 .   ? 34.127  29.182  23.99   1   43.07  ? 992  HOH A O     1 1 
HETATM 6197 O  O     . HOH F 6 .   ? 2.276   26.065  -13.537 1   37.2   ? 993  HOH A O     1 1 
HETATM 6198 O  O     . HOH F 6 .   ? 31.388  27.226  27.786  1   37.46  ? 994  HOH A O     1 1 
HETATM 6199 O  O     . HOH F 6 .   ? -8.483  13.943  6.171   1   27.72  ? 995  HOH A O     1 1 
HETATM 6200 O  O     . HOH F 6 .   ? 36.451  3.654   4.674   1   21.24  ? 996  HOH A O     1 1 
HETATM 6201 O  O     . HOH F 6 .   ? 15.732  14.517  25.154  1   33.08  ? 997  HOH A O     1 1 
HETATM 6202 O  O     . HOH F 6 .   ? 31.883  -2.226  -0.698  1   44.7   ? 998  HOH A O     1 1 
HETATM 6203 O  O     . HOH F 6 .   ? 10.706  15.512  22.826  1   42.09  ? 999  HOH A O     1 1 
HETATM 6204 O  O     . HOH F 6 .   ? 5.781   -0.196  -0.364  1   18.22  ? 1000 HOH A O     1 1 
HETATM 6205 O  O     . HOH F 6 .   ? 20.553  29.362  3.871   1   31.57  ? 1001 HOH A O     1 1 
HETATM 6206 O  O     . HOH F 6 .   ? 27.996  0.808   41.384  1   46.68  ? 1002 HOH A O     1 1 
HETATM 6207 O  O     . HOH F 6 .   ? 35.516  8.304   -8.749  1   28.18  ? 1003 HOH A O     1 1 
HETATM 6208 O  O     . HOH F 6 .   ? -3.761  6.345   2.341   1   30.94  ? 1004 HOH A O     1 1 
HETATM 6209 O  O     . HOH F 6 .   ? 42.562  12.139  8.003   1   53.17  ? 1005 HOH A O     1 1 
HETATM 6210 O  O     . HOH F 6 .   ? -3.115  12.815  23.41   1   33.98  ? 1006 HOH A O     1 1 
HETATM 6211 O  O     . HOH F 6 .   ? 25.647  54.459  -6.424  1   48.83  ? 1007 HOH A O     1 1 
HETATM 6212 O  O     . HOH F 6 .   ? 18.248  28.745  0.294   1   23.06  ? 1008 HOH A O     1 1 
HETATM 6213 O  O     . HOH F 6 .   ? -11.118 13.955  4.992   1   33.49  ? 1009 HOH A O     1 1 
HETATM 6214 O  O     . HOH F 6 .   ? 7.952   54.086  -2.373  1   31.01  ? 1010 HOH A O     1 1 
HETATM 6215 O  O     . HOH F 6 .   ? 12.984  21.801  4.15    1   19.79  ? 1011 HOH A O     1 1 
HETATM 6216 O  O     . HOH F 6 .   ? 5.623   23.188  6.685   1   29.67  ? 1012 HOH A O     1 1 
HETATM 6217 O  O     . HOH F 6 .   ? 8.465   23.799  7.063   1   33.23  ? 1013 HOH A O     1 1 
HETATM 6218 O  O     . HOH F 6 .   ? 22.729  28.437  -0.082  1   46.39  ? 1014 HOH A O     1 1 
HETATM 6219 O  O     . HOH F 6 .   ? 1.346   50.41   -2.399  1   43.8   ? 1015 HOH A O     1 1 
HETATM 6220 O  O     . HOH F 6 .   ? 13.9    57.101  -1.325  1   29.07  ? 1016 HOH A O     1 1 
HETATM 6221 O  O     . HOH F 6 .   ? 18.404  -0.452  25.31   1   42.52  ? 1017 HOH A O     1 1 
HETATM 6222 O  O     . HOH F 6 .   ? 45.947  19.683  23.831  1   30.94  ? 1018 HOH A O     1 1 
HETATM 6223 O  O     . HOH F 6 .   ? 39.567  2.839   11.44   1   29.06  ? 1019 HOH A O     1 1 
HETATM 6224 O  O     . HOH F 6 .   ? 21.719  22.507  9.326   1   33.4   ? 1020 HOH A O     1 1 
HETATM 6225 O  O     . HOH F 6 .   ? 34.918  -1.11   19.268  1   36.23  ? 1021 HOH A O     1 1 
HETATM 6226 O  O     . HOH F 6 .   ? 2.491   27.524  19.952  1   24.13  ? 1022 HOH A O     1 1 
HETATM 6227 O  O     . HOH F 6 .   ? 10.811  39.53   4.466   1   17.29  ? 1023 HOH A O     1 1 
HETATM 6228 O  O     . HOH F 6 .   ? -3.459  31.547  5.237   1   37.54  ? 1024 HOH A O     1 1 
HETATM 6229 O  O     . HOH F 6 .   ? 22.148  -9.045  5.883   1   28.67  ? 1025 HOH A O     1 1 
HETATM 6230 O  O     . HOH F 6 .   ? 30.358  -6.148  22.496  1   54.06  ? 1026 HOH A O     1 1 
HETATM 6231 O  O     . HOH F 6 .   ? 0.844   22.921  -10.394 1   22.85  ? 1027 HOH A O     1 1 
HETATM 6232 O  O     . HOH F 6 .   ? 19.662  53.642  -10.856 1   23.12  ? 1028 HOH A O     1 1 
HETATM 6233 O  O     . HOH F 6 .   ? 16.579  20.667  11.069  1   31.17  ? 1029 HOH A O     1 1 
HETATM 6234 O  O     . HOH F 6 .   ? 31.36   8.397   -10.153 1   46.87  ? 1030 HOH A O     1 1 
HETATM 6235 O  O     . HOH F 6 .   ? -11.138 24.585  2.197   1   29.4   ? 1031 HOH A O     1 1 
HETATM 6236 O  O     . HOH F 6 .   ? 32.725  46.263  -8.959  1   43.83  ? 1032 HOH A O     1 1 
HETATM 6237 O  O     . HOH F 6 .   ? 2.374   -3.349  -1.043  1   27.24  ? 1033 HOH A O     1 1 
HETATM 6238 O  O     . HOH F 6 .   ? 32.623  -4.51   27.954  1   47.56  ? 1034 HOH A O     1 1 
HETATM 6239 O  O     . HOH F 6 .   ? 10.39   1.646   -5.001  1   35.25  ? 1035 HOH A O     1 1 
HETATM 6240 O  O     . HOH F 6 .   ? 14.335  54.226  -7.627  1   29.13  ? 1036 HOH A O     1 1 
HETATM 6241 O  O     . HOH F 6 .   ? 9.308   28.37   22.561  1   26.93  ? 1037 HOH A O     1 1 
HETATM 6242 O  O     . HOH F 6 .   ? 3.695   46.118  -27.142 1   40.33  ? 1038 HOH A O     1 1 
HETATM 6243 O  O     . HOH F 6 .   ? 24.14   40.965  2.798   1   30.52  ? 1039 HOH A O     1 1 
HETATM 6244 O  O     . HOH F 6 .   ? 24.311  41.847  0.353   1   20.56  ? 1040 HOH A O     1 1 
HETATM 6245 O  O     . HOH F 6 .   ? 29.613  20.447  12.176  1   40.93  ? 1041 HOH A O     1 1 
HETATM 6246 O  O     . HOH F 6 .   ? 33.246  1.438   -7.331  1   34.84  ? 1042 HOH A O     1 1 
HETATM 6247 O  O     . HOH F 6 .   ? 5.782   -1.113  -2.724  1   31.07  ? 1043 HOH A O     1 1 
HETATM 6248 O  O     . HOH F 6 .   ? 42.959  11.74   29.003  1   30.65  ? 1044 HOH A O     1 1 
HETATM 6249 O  O     . HOH F 6 .   ? 40.597  4.995   9.075   1   38.96  ? 1045 HOH A O     1 1 
HETATM 6250 O  O     . HOH F 6 .   ? 31.719  13.496  4.81    1   14.03  ? 1046 HOH A O     1 1 
HETATM 6251 O  O     . HOH F 6 .   ? 12.85   57.781  -13.857 1   52.72  ? 1047 HOH A O     1 1 
HETATM 6252 O  O     . HOH F 6 .   ? 10.653  -12.461 12.498  1   16.56  ? 1048 HOH A O     1 1 
HETATM 6253 O  O     . HOH F 6 .   ? 8.236   3.992   14.216  1   38.92  ? 1049 HOH A O     1 1 
HETATM 6254 O  O     . HOH F 6 .   ? 15.482  12.496  26.809  1   42.58  ? 1050 HOH A O     1 1 
HETATM 6255 O  O     . HOH F 6 .   ? 13.941  28.154  12.42   1   41.44  ? 1051 HOH A O     1 1 
HETATM 6256 O  O     . HOH F 6 .   ? 48.026  11.136  21.482  1   41.58  ? 1052 HOH A O     1 1 
HETATM 6257 O  O     . HOH F 6 .   ? 4.934   9.704   18.113  1   33.9   ? 1053 HOH A O     1 1 
HETATM 6258 O  O     . HOH F 6 .   ? 22.181  7.133   33.311  1   39.19  ? 1054 HOH A O     1 1 
HETATM 6259 O  O     . HOH F 6 .   ? 31.036  -9.125  12.254  1   32.95  ? 1055 HOH A O     1 1 
HETATM 6260 O  O     . HOH F 6 .   ? 11.052  22.061  -10.465 1   20.6   ? 1056 HOH A O     1 1 
HETATM 6261 O  O     . HOH F 6 .   ? 22.108  35.864  -17.857 1   32.49  ? 1057 HOH A O     1 1 
HETATM 6262 O  O     . HOH F 6 .   ? 14.02   21.673  15.358  1   45.98  ? 1058 HOH A O     1 1 
HETATM 6263 O  O     . HOH F 6 .   ? -0.182  2.347   -1.448  1   19.55  ? 1059 HOH A O     1 1 
HETATM 6264 O  O     . HOH F 6 .   ? -1.362  8.286   17.054  1   38.69  ? 1060 HOH A O     1 1 
HETATM 6265 O  O     . HOH F 6 .   ? -7.76   40.473  -3.425  1   23.25  ? 1061 HOH A O     1 1 
HETATM 6266 O  O     . HOH F 6 .   ? 1.213   19.627  -7.926  1   17.51  ? 1062 HOH A O     1 1 
HETATM 6267 O  O     . HOH F 6 .   ? 10.877  -2.918  18.864  1   50.4   ? 1063 HOH A O     1 1 
HETATM 6268 O  O     . HOH F 6 .   ? 2.926   30.273  -19.026 1   33.76  ? 1064 HOH A O     1 1 
HETATM 6269 O  O     . HOH F 6 .   ? 9.913   7.947   -5.996  1   43.4   ? 1065 HOH A O     1 1 
HETATM 6270 O  O     . HOH F 6 .   ? -6.339  33.526  -7.076  1   30.21  ? 1066 HOH A O     1 1 
HETATM 6271 O  O     . HOH F 6 .   ? 37.234  19.97   11.631  1   39.13  ? 1067 HOH A O     1 1 
HETATM 6272 O  O     . HOH F 6 .   ? 3.943   40.64   -23.388 1   34.17  ? 1068 HOH A O     1 1 
HETATM 6273 O  O     . HOH F 6 .   ? 29.424  21.298  2.179   1   36.87  ? 1069 HOH A O     1 1 
HETATM 6274 O  O     . HOH F 6 .   ? 51.521  19.331  37.421  1   42.47  ? 1070 HOH A O     1 1 
HETATM 6275 O  O     . HOH F 6 .   ? 42.714  25.32   25.91   1   31.11  ? 1071 HOH A O     1 1 
HETATM 6276 O  O     . HOH F 6 .   ? 20.215  36.453  -19.758 1   33.29  ? 1072 HOH A O     1 1 
HETATM 6277 O  O     . HOH F 6 .   ? -2.723  17.146  33.842  1   53.06  ? 1073 HOH A O     1 1 
HETATM 6278 O  O     . HOH F 6 .   ? 18.674  21.58   11.96   1   45.71  ? 1074 HOH A O     1 1 
HETATM 6279 O  O     . HOH F 6 .   ? 9.798   33.753  24.745  1   32.78  ? 1075 HOH A O     1 1 
HETATM 6280 O  O     . HOH F 6 .   ? -1.254  42.889  -21.445 1   32.54  ? 1076 HOH A O     1 1 
HETATM 6281 O  O     . HOH F 6 .   ? -8.867  11.233  14.283  1   28.94  ? 1077 HOH A O     1 1 
HETATM 6282 O  O     . HOH F 6 .   ? 6.909   11.59   -7.602  1   31.64  ? 1078 HOH A O     1 1 
HETATM 6283 O  O     . HOH F 6 .   ? 19.834  48.265  -14.865 1   28.83  ? 1079 HOH A O     1 1 
HETATM 6284 O  O     . HOH F 6 .   ? 20.547  4.792   37.183  1   32.08  ? 1080 HOH A O     1 1 
HETATM 6285 O  O     . HOH F 6 .   ? 6.448   55.049  -4.709  1   29.99  ? 1081 HOH A O     1 1 
HETATM 6286 O  O     . HOH F 6 .   ? 14.269  -17.684 4.965   1   47.49  ? 1082 HOH A O     1 1 
HETATM 6287 O  O     . HOH F 6 .   ? 13.228  32.333  -23.56  1   54.53  ? 1083 HOH A O     1 1 
HETATM 6288 O  O     . HOH F 6 .   ? 10.025  15.034  49.384  1   50.97  ? 1084 HOH A O     1 1 
HETATM 6289 O  O     . HOH F 6 .   ? 51.022  22.617  39.174  1   43.88  ? 1085 HOH A O     1 1 
HETATM 6290 O  O     . HOH F 6 .   ? 14.297  25.347  41.721  1   40.19  ? 1086 HOH A O     1 1 
HETATM 6291 O  O     . HOH F 6 .   ? 13.479  22.888  10.406  1   47.88  ? 1087 HOH A O     1 1 
HETATM 6292 O  O     . HOH F 6 .   ? 14.863  54.481  -12.424 1   35.7   ? 1088 HOH A O     1 1 
HETATM 6293 O  O     . HOH F 6 .   ? 11.437  24.552  5.429   1   32.08  ? 1089 HOH A O     1 1 
HETATM 6294 O  O     . HOH F 6 .   ? -11.466 14.579  1.448   1   29.04  ? 1090 HOH A O     1 1 
HETATM 6295 O  O     . HOH F 6 .   ? 50.92   3.739   22.2    1   40.04  ? 1091 HOH A O     1 1 
HETATM 6296 O  O     . HOH F 6 .   ? 41.446  19.749  19.565  1   25.82  ? 1092 HOH A O     1 1 
HETATM 6297 O  O     . HOH F 6 .   ? 27.043  39.905  -13.766 1   44.1   ? 1093 HOH A O     1 1 
HETATM 6298 O  O     . HOH F 6 .   ? 15.164  57.45   -3.715  1   21.34  ? 1094 HOH A O     1 1 
HETATM 6299 O  O     . HOH F 6 .   ? -2.039  29.838  8.985   1   30.53  ? 1095 HOH A O     1 1 
HETATM 6300 O  O     . HOH F 6 .   ? 25.64   19.77   -0.984  1   28.3   ? 1096 HOH A O     1 1 
HETATM 6301 O  O     . HOH F 6 .   ? 40.35   3.208   6.231   1   59.08  ? 1097 HOH A O     1 1 
HETATM 6302 O  O     . HOH F 6 .   ? 21.821  51.502  8.873   1   32.8   ? 1098 HOH A O     1 1 
HETATM 6303 O  O     . HOH F 6 .   ? 19.254  17.888  52.408  1   35.79  ? 1099 HOH A O     1 1 
HETATM 6304 O  O     . HOH F 6 .   ? 28.185  54.186  -0.118  1   35.66  ? 1100 HOH A O     1 1 
HETATM 6305 O  O     . HOH F 6 .   ? 16.305  29.005  22.017  1   35.98  ? 1101 HOH A O     1 1 
HETATM 6306 O  O     . HOH F 6 .   ? -4.466  40.112  2.546   1   45.02  ? 1102 HOH A O     1 1 
HETATM 6307 O  O     . HOH F 6 .   ? 3.12    49.265  -0.388  1   19.29  ? 1103 HOH A O     1 1 
HETATM 6308 O  O     . HOH F 6 .   ? 11.745  41.566  6.006   1   18.33  ? 1104 HOH A O     1 1 
HETATM 6309 O  O     . HOH F 6 .   ? 24.991  59.719  3.467   1   57.56  ? 1105 HOH A O     1 1 
HETATM 6310 O  O     . HOH F 6 .   ? -5.14   38.27   -16.323 1   20.57  ? 1106 HOH A O     1 1 
HETATM 6311 O  O     . HOH F 6 .   ? 27.628  22.31   22.091  1   41.11  ? 1107 HOH A O     1 1 
HETATM 6312 O  O     . HOH F 6 .   ? -5.244  24.486  11.218  1   31.56  ? 1108 HOH A O     1 1 
HETATM 6313 O  O     . HOH F 6 .   ? 10.556  -5.534  -4.19   1   31.03  ? 1109 HOH A O     1 1 
HETATM 6314 O  O     . HOH F 6 .   ? 23.214  32.994  30.718  1   40.95  ? 1110 HOH A O     1 1 
HETATM 6315 O  O     . HOH F 6 .   ? 10.077  54.778  -20.224 1   56.83  ? 1111 HOH A O     1 1 
HETATM 6316 O  O     . HOH F 6 .   ? 14.595  32.953  32.225  1   35.03  ? 1112 HOH A O     1 1 
HETATM 6317 O  O     . HOH F 6 .   ? 20.104  5.988   -5.11   1   37.44  ? 1113 HOH A O     1 1 
HETATM 6318 O  O     . HOH F 6 .   ? -12.777 23.057  0.031   1   24.37  ? 1114 HOH A O     1 1 
HETATM 6319 O  O     . HOH F 6 .   ? 9.785   23.255  -14.284 1   43.77  ? 1115 HOH A O     1 1 
HETATM 6320 O  O     . HOH F 6 .   ? -0.149  3.676   8.84    1   30.09  ? 1116 HOH A O     1 1 
HETATM 6321 O  O     . HOH F 6 .   ? 38.277  5.26    3.296   1   34.75  ? 1117 HOH A O     1 1 
HETATM 6322 O  O     . HOH F 6 .   ? -14.33  31.086  4.683   1   38.27  ? 1118 HOH A O     1 1 
HETATM 6323 O  O     . HOH F 6 .   ? 3.327   8.943   15.39   1   14.78  ? 1119 HOH A O     1 1 
HETATM 6324 O  O     . HOH F 6 .   ? 49.747  10.532  17.299  1   35.52  ? 1120 HOH A O     1 1 
HETATM 6325 O  O     . HOH F 6 .   ? 34.604  17.978  50.31   1   50.72  ? 1121 HOH A O     1 1 
HETATM 6326 O  O     . HOH F 6 .   ? 8.584   40.151  -27.102 1   38.75  ? 1122 HOH A O     1 1 
HETATM 6327 O  O     . HOH F 6 .   ? 19.044  56.926  2.614   1   43.45  ? 1123 HOH A O     1 1 
HETATM 6328 O  O     . HOH F 6 .   ? 26.386  52.333  -7.743  1   36.53  ? 1124 HOH A O     1 1 
HETATM 6329 O  O     . HOH F 6 .   ? 12.982  13.187  16.181  1   52.07  ? 1125 HOH A O     1 1 
HETATM 6330 O  O     . HOH F 6 .   ? 26.655  50.931  -12.693 1   45.96  ? 1126 HOH A O     1 1 
HETATM 6331 O  O     . HOH F 6 .   ? 19.919  -5.107  0.999   1   24.12  ? 1127 HOH A O     1 1 
HETATM 6332 O  O     . HOH F 6 .   ? 33.005  48.399  -1.932  1   28.06  ? 1128 HOH A O     1 1 
HETATM 6333 O  O     . HOH F 6 .   ? 5.766   1.77    37.664  1   51.8   ? 1129 HOH A O     1 1 
HETATM 6334 O  O     . HOH F 6 .   ? 0.152   27.175  29.789  1   42.18  ? 1130 HOH A O     1 1 
HETATM 6335 O  O     . HOH F 6 .   ? 17.1    51.064  -20.602 1   34.88  ? 1131 HOH A O     1 1 
HETATM 6336 O  O     . HOH F 6 .   ? 10.473  -4.18   4.012   1   20.28  ? 1132 HOH A O     1 1 
HETATM 6337 O  O     . HOH F 6 .   ? 25.121  61.635  1.433   1   52.15  ? 1133 HOH A O     1 1 
HETATM 6338 O  O     . HOH F 6 .   ? 25.582  20.79   9.429   1   43.01  ? 1134 HOH A O     1 1 
HETATM 6339 O  O     . HOH F 6 .   ? 2.545   48.221  -26.038 1   41.08  ? 1135 HOH A O     1 1 
HETATM 6340 O  O     . HOH F 6 .   ? -2.43   28.507  25.428  1   50.59  ? 1136 HOH A O     1 1 
HETATM 6341 O  O     . HOH F 6 .   ? 14.224  15.879  -12.482 1   45.78  ? 1137 HOH A O     1 1 
HETATM 6342 O  O     . HOH F 6 .   ? 4.659   26.641  36.067  1   36.88  ? 1138 HOH A O     1 1 
HETATM 6343 O  O     . HOH F 6 .   ? 12.332  16.484  16.346  1   32.6   ? 1139 HOH A O     1 1 
HETATM 6344 O  O     . HOH F 6 .   ? 8.454   57.877  -12.293 1   43.38  ? 1140 HOH A O     1 1 
HETATM 6345 O  O     . HOH F 6 .   ? 43.065  20.081  21.754  1   21.66  ? 1141 HOH A O     1 1 
HETATM 6346 O  O     . HOH F 6 .   ? 34.582  23.886  20.248  1   24.74  ? 1142 HOH A O     1 1 
HETATM 6347 O  O     . HOH F 6 .   ? 19.204  21.22   43.836  1   43.14  ? 1143 HOH A O     1 1 
HETATM 6348 O  O     . HOH F 6 .   ? 27.487  42.785  -14.258 1   46.64  ? 1144 HOH A O     1 1 
HETATM 6349 O  O     . HOH F 6 .   ? -0.532  33.777  22.647  1   32.08  ? 1145 HOH A O     1 1 
HETATM 6350 O  O     . HOH F 6 .   ? 30.057  21.623  21.022  1   59.73  ? 1146 HOH A O     1 1 
HETATM 6351 O  O     . HOH F 6 .   ? 14.107  12.38   -9.388  1   32.94  ? 1147 HOH A O     1 1 
HETATM 6352 O  O     . HOH F 6 .   ? 28.925  8.012   -6.542  1   33.39  ? 1148 HOH A O     1 1 
HETATM 6353 O  O     . HOH F 6 .   ? 31.102  17.876  48.105  1   56.32  ? 1149 HOH A O     1 1 
HETATM 6354 O  O     . HOH F 6 .   ? -10.213 9.659   26.298  1   47.98  ? 1150 HOH A O     1 1 
HETATM 6355 O  O     . HOH F 6 .   ? 10.98   1.427   40.116  1   45.25  ? 1151 HOH A O     1 1 
HETATM 6356 O  O     . HOH F 6 .   ? 12.04   46.943  14.689  1   39.17  ? 1152 HOH A O     1 1 
HETATM 6357 O  O     . HOH F 6 .   ? 39.471  23.733  5.765   1   32.84  ? 1153 HOH A O     1 1 
HETATM 6358 O  O     . HOH F 6 .   ? 2.454   53.646  3.157   1   44.63  ? 1154 HOH A O     1 1 
HETATM 6359 O  O     . HOH F 6 .   ? 12.119  -12.084 15.296  1   33.43  ? 1155 HOH A O     1 1 
HETATM 6360 O  O     . HOH F 6 .   ? -4.826  34.834  5.318   1   44.67  ? 1156 HOH A O     1 1 
HETATM 6361 O  O     . HOH F 6 .   ? -11.209 24.217  14.679  1   23.94  ? 1157 HOH A O     1 1 
HETATM 6362 O  O     . HOH F 6 .   ? 26.059  44.195  8.188   1   30.31  ? 1158 HOH A O     1 1 
HETATM 6363 O  O     . HOH F 6 .   ? 26.618  53.1    -10.108 1   27.34  ? 1159 HOH A O     1 1 
HETATM 6364 O  O     . HOH F 6 .   ? -1.311  12.369  -8.897  1   41.56  ? 1160 HOH A O     1 1 
HETATM 6365 O  O     . HOH F 6 .   ? -13.096 26.522  -5.108  1   35.8   ? 1161 HOH A O     1 1 
HETATM 6366 O  O     . HOH F 6 .   ? 16.342  57.393  -15.103 1   43.52  ? 1162 HOH A O     1 1 
HETATM 6367 O  O     . HOH F 6 .   ? 23.209  24.979  24.071  1   37.39  ? 1163 HOH A O     1 1 
HETATM 6368 O  O     . HOH F 6 .   ? 12.144  -8.278  13.445  1   23.37  ? 1164 HOH A O     1 1 
HETATM 6369 O  O     . HOH F 6 .   ? 8.411   11.937  18.744  1   37.12  ? 1165 HOH A O     1 1 
HETATM 6370 O  O     . HOH F 6 .   ? 4.589   17.834  -13.329 1   40.93  ? 1166 HOH A O     1 1 
HETATM 6371 O  O     . HOH F 6 .   ? 51.555  19.001  31.921  1   40.05  ? 1167 HOH A O     1 1 
HETATM 6372 O  O     . HOH F 6 .   ? 44.738  12.085  11.429  1   32.39  ? 1168 HOH A O     1 1 
HETATM 6373 O  O     . HOH F 6 .   ? -13.353 25.037  4.594   1   31.56  ? 1169 HOH A O     1 1 
HETATM 6374 O  O     . HOH F 6 .   ? 20.104  54.406  3.029   1   41.6   ? 1170 HOH A O     1 1 
HETATM 6375 O  O     . HOH F 6 .   ? 30.344  47.597  2.247   1   29     ? 1171 HOH A O     1 1 
HETATM 6376 O  O     . HOH F 6 .   ? 34.814  -4.613  17.36   1   41.28  ? 1172 HOH A O     1 1 
HETATM 6377 O  O     . HOH F 6 .   ? 8.23    -4.299  16.914  1   45.24  ? 1173 HOH A O     1 1 
HETATM 6378 O  O     . HOH F 6 .   ? 33.621  -4.952  7.276   1   26.99  ? 1174 HOH A O     1 1 
HETATM 6379 O  O     . HOH F 6 .   ? -9.217  15.111  17.233  1   40.31  ? 1175 HOH A O     1 1 
HETATM 6380 O  O     . HOH F 6 .   ? 13.986  -1.184  -5.391  1   49.99  ? 1176 HOH A O     1 1 
HETATM 6381 O  O     . HOH F 6 .   ? 22.835  19.332  45.562  1   35.85  ? 1177 HOH A O     1 1 
HETATM 6382 O  O     . HOH F 6 .   ? 19.97   -8.934  2.109   1   34.13  ? 1178 HOH A O     1 1 
HETATM 6383 O  O     . HOH F 6 .   ? 33.167  -3.013  5.795   1   30.35  ? 1179 HOH A O     1 1 
HETATM 6384 O  O     . HOH F 6 .   ? 25.679  -15.053 14.086  1   54.26  ? 1180 HOH A O     1 1 
HETATM 6385 O  O     . HOH F 6 .   ? 14.822  50.882  3.959   1   26.06  ? 1181 HOH A O     1 1 
HETATM 6386 O  O     . HOH F 6 .   ? 19.326  52.474  5.312   1   40.67  ? 1182 HOH A O     1 1 
HETATM 6387 O  O     . HOH F 6 .   ? 27.412  29.427  -11.091 1   41.59  ? 1183 HOH A O     1 1 
HETATM 6388 O  O     . HOH F 6 .   ? 21.6    53.685  -12.979 1   44.72  ? 1184 HOH A O     1 1 
HETATM 6389 O  O     . HOH F 6 .   ? 10.378  21.088  -12.88  1   38.35  ? 1185 HOH A O     1 1 
HETATM 6390 O  O     . HOH F 6 .   ? 35.102  42.453  -7.193  1   31.16  ? 1186 HOH A O     1 1 
HETATM 6391 O  O     . HOH F 6 .   ? -3.186  31.003  -19.204 1   45.7   ? 1187 HOH A O     1 1 
HETATM 6392 O  O     . HOH F 6 .   ? 1.095   32.056  12.23   1   41.29  ? 1188 HOH A O     1 1 
HETATM 6393 O  O     . HOH F 6 .   ? 33.494  8.038   -11.295 1   38.47  ? 1189 HOH A O     1 1 
HETATM 6394 O  O     . HOH F 6 .   ? 33.668  44.836  -7.12   1   38.8   ? 1190 HOH A O     1 1 
HETATM 6395 O  O     . HOH F 6 .   ? 33.638  -4.368  14.03   1   43.75  ? 1191 HOH A O     1 1 
HETATM 6396 O  O     . HOH F 6 .   ? 44.85   17.812  17.003  1   30.21  ? 1192 HOH A O     1 1 
HETATM 6397 O  O     . HOH F 6 .   ? -9.676  10.232  4.07    1   39.04  ? 1193 HOH A O     1 1 
HETATM 6398 O  O     . HOH F 6 .   ? 12.7    21.897  48.986  1   135.23 ? 1194 HOH A O     1 1 
HETATM 6399 O  O     . HOH F 6 .   ? 17.585  22.243  -17.136 1   38.94  ? 1195 HOH A O     1 1 
HETATM 6400 O  O     . HOH G 6 .   ? 23.969  26.854  4.738   1   58.08  ? 101  HOH E O     1 1 
HETATM 6401 O  O     . HOH G 6 .   ? 1.961   50.684  12.27   1   38.52  ? 102  HOH E O     1 1 
HETATM 6402 O  O     . HOH G 6 .   ? 7.012   43.776  10.783  1   20.46  ? 103  HOH E O     1 1 
HETATM 6403 O  O     . HOH G 6 .   ? 27.727  30.714  0.57    1   53.41  ? 104  HOH E O     1 1 
HETATM 6404 O  O     . HOH G 6 .   ? 27.477  39.814  11.927  1   31.9   ? 105  HOH E O     1 1 
HETATM 6405 O  O     . HOH G 6 .   ? 27.498  41.015  2.546   1   26.57  ? 106  HOH E O     1 1 
HETATM 6406 O  O     . HOH G 6 .   ? 14.935  36.064  17.958  1   52.46  ? 107  HOH E O     1 1 
HETATM 6407 O  O     . HOH G 6 .   ? 32.056  33.24   7.382   1   50.11  ? 108  HOH E O     1 1 
HETATM 6408 O  O     . HOH G 6 .   ? 3.044   43.643  8.328   1   28.01  ? 109  HOH E O     1 1 
HETATM 6409 O  O     . HOH G 6 .   ? 29.172  29.768  3.577   1   40.54  ? 110  HOH E O     1 1 
HETATM 6410 O  O     . HOH G 6 .   ? 24.139  39.075  9.286   1   25.54  ? 111  HOH E O     1 1 
HETATM 6411 O  O     . HOH G 6 .   ? 6.872   51.614  11.941  1   36.08  ? 112  HOH E O     1 1 
HETATM 6412 O  O     . HOH G 6 .   ? 23.79   29.222  2.64    1   54.94  ? 113  HOH E O     1 1 
HETATM 6413 O  O     . HOH G 6 .   ? 1.763   47.417  1.617   1   29.49  ? 114  HOH E O     1 1 
HETATM 6414 O  O     . HOH G 6 .   ? 18.281  29.34   7.154   1   43.98  ? 115  HOH E O     1 1 
HETATM 6415 O  O     . HOH G 6 .   ? 10.127  50.932  14.991  1   41.91  ? 116  HOH E O     1 1 
HETATM 6416 O  O     . HOH G 6 .   ? 4.221   38.281  18.463  1   38.93  ? 117  HOH E O     1 1 
HETATM 6417 O  O     . HOH G 6 .   ? 25.197  29.463  13.774  1   39.2   ? 118  HOH E O     1 1 
HETATM 6418 O  O     . HOH G 6 .   ? 13.069  26.615  21.86   1   46.75  ? 119  HOH E O     1 1 
HETATM 6419 O  O     . HOH G 6 .   ? 25.994  39.693  7.448   1   43.09  ? 120  HOH E O     1 1 
HETATM 6420 O  O     . HOH H 6 .   ? -2.045  31.97   12.767  1   43.6   ? 101  HOH F O     1 1 
HETATM 6421 O  O     . HOH H 6 .   ? 32.748  28.651  17.6    1   55.12  ? 102  HOH F O     1 1 
HETATM 6422 O  O     . HOH H 6 .   ? 31.813  29.098  20.505  1   50.62  ? 103  HOH F O     1 1 
HETATM 6423 O  O     . HOH H 6 .   ? 27.581  33.772  23.87   1   47.77  ? 104  HOH F O     1 1 
HETATM 6424 O  O     . HOH H 6 .   ? 9.756   41.168  2.657   1   17.52  ? 105  HOH F O     1 1 
HETATM 6425 O  O     . HOH H 6 .   ? 31.05   30.276  10.151  1   44.43  ? 106  HOH F O     1 1 
HETATM 6426 O  O     . HOH H 6 .   ? 13.363  49.303  7.933   1   31.27  ? 107  HOH F O     1 1 
HETATM 6427 O  O     . HOH H 6 .   ? 23.567  41.77   15.374  1   37.23  ? 108  HOH F O     1 1 
HETATM 6428 O  O     . HOH H 6 .   ? -3.878  37.805  8.669   1   38.25  ? 109  HOH F O     1 1 
HETATM 6429 O  O     . HOH H 6 .   ? 8.969   37.421  4.833   1   16.51  ? 110  HOH F O     1 1 
HETATM 6430 O  O     . HOH H 6 .   ? 24.926  30.912  16.514  1   44.34  ? 111  HOH F O     1 1 
HETATM 6431 O  O     . HOH H 6 .   ? 6.48    35.35   9.756   1   24.88  ? 112  HOH F O     1 1 
HETATM 6432 O  O     . HOH H 6 .   ? -1.531  30.876  6.705   1   19.78  ? 113  HOH F O     1 1 
HETATM 6433 O  O     . HOH H 6 .   ? 2.182   40.784  7.583   1   24.6   ? 114  HOH F O     1 1 
HETATM 6434 O  O     . HOH H 6 .   ? 3.591   30.033  6.633   1   15.73  ? 115  HOH F O     1 1 
HETATM 6435 O  O     . HOH H 6 .   ? 10.264  42.8    13.424  1   22.25  ? 116  HOH F O     1 1 
HETATM 6436 O  O     . HOH H 6 .   ? -0.179  38.483  7.729   1   23.15  ? 117  HOH F O     1 1 
HETATM 6437 O  O     . HOH H 6 .   ? 17.115  37.256  9.255   1   17.91  ? 118  HOH F O     1 1 
HETATM 6438 O  O     . HOH H 6 .   ? 28.576  23.407  19.832  1   43.43  ? 119  HOH F O     1 1 
HETATM 6439 O  O     . HOH H 6 .   ? 21.955  39.864  11.979  1   35.45  ? 120  HOH F O     1 1 
HETATM 6440 O  O     . HOH H 6 .   ? 28.836  38.051  15.788  1   44.09  ? 121  HOH F O     1 1 
HETATM 6441 O  O     . HOH H 6 .   ? 29.158  36.519  18.412  1   42.9   ? 122  HOH F O     1 1 
HETATM 6442 O  O     . HOH H 6 .   ? 36.729  28.487  14.117  1   46.08  ? 123  HOH F O     1 1 
HETATM 6443 O  O     . HOH H 6 .   ? 5.48    44.47   8.275   1   26.25  ? 124  HOH F O     1 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   ? 0.1442 0.077  0.4283 0.0301  -0.0096 -0.0354 1    MET A N     
2    C  CA    . MET A 1   ? 0.143  0.0855 0.4366 0.0279  -0.0085 -0.036  1    MET A CA    
3    C  C     . MET A 1   ? 0.1452 0.0881 0.4404 0.028   -0.0086 -0.0367 1    MET A C     
4    O  O     . MET A 1   ? 0.165  0.1031 0.4548 0.0308  -0.0079 -0.0364 1    MET A O     
5    C  CB    . MET A 1   ? 0.1503 0.1006 0.4477 0.0292  -0.0048 -0.0357 1    MET A CB    
6    C  CG    . MET A 1   ? 0.1941 0.1542 0.501  0.0271  -0.0038 -0.0365 1    MET A CG    
7    S  SD    . MET A 1   ? 0.2896 0.2588 0.6013 0.0282  -0.0002 -0.0364 1    MET A SD    
8    C  CE    . MET A 1   ? 0.2531 0.2203 0.5611 0.0317  0.0022  -0.0358 1    MET A CE    
9    N  N     . ASN A 2   ? 0.1213 0.0699 0.424  0.0253  -0.0093 -0.0373 2    ASN A N     
10   C  CA    . ASN A 2   ? 0.1195 0.0696 0.4248 0.0253  -0.0091 -0.0379 2    ASN A CA    
11   C  C     . ASN A 2   ? 0.1087 0.0685 0.4224 0.0246  -0.0066 -0.0384 2    ASN A C     
12   O  O     . ASN A 2   ? 0.1049 0.0706 0.4237 0.0228  -0.0063 -0.0387 2    ASN A O     
13   C  CB    . ASN A 2   ? 0.1435 0.0903 0.4493 0.0229  -0.0124 -0.0383 2    ASN A CB    
14   C  CG    . ASN A 2   ? 0.2157 0.1522 0.5125 0.0245  -0.0146 -0.038  2    ASN A CG    
15   O  OD1   . ASN A 2   ? 0.2602 0.1928 0.5511 0.0279  -0.0131 -0.0377 2    ASN A OD1   
16   N  ND2   . ASN A 2   ? 0.195  0.127  0.4904 0.0223  -0.0181 -0.038  2    ASN A ND2   
17   N  N     . VAL A 3   ? 0.1005 0.0622 0.4155 0.0263  -0.0047 -0.0385 3    VAL A N     
18   C  CA    . VAL A 3   ? 0.0927 0.0632 0.4156 0.0257  -0.0025 -0.0391 3    VAL A CA    
19   C  C     . VAL A 3   ? 0.0941 0.0663 0.4214 0.0246  -0.0031 -0.0398 3    VAL A C     
20   O  O     . VAL A 3   ? 0.1005 0.0677 0.4241 0.0258  -0.0036 -0.0394 3    VAL A O     
21   C  CB    . VAL A 3   ? 0.0962 0.0687 0.4182 0.0286  0.0006  -0.0384 3    VAL A CB    
22   C  CG1   . VAL A 3   ? 0.0967 0.0779 0.4272 0.028   0.0025  -0.0391 3    VAL A CG1   
23   C  CG2   . VAL A 3   ? 0.101  0.0725 0.4192 0.0296  0.0013  -0.0377 3    VAL A CG2   
24   N  N     . PHE A 4   ? 0.0835 0.0627 0.4185 0.0223  -0.003  -0.0407 4    PHE A N     
25   C  CA    . PHE A 4   ? 0.0806 0.0627 0.421  0.021   -0.0033 -0.0415 4    PHE A CA    
26   C  C     . PHE A 4   ? 0.083  0.073  0.4305 0.021   -0.001  -0.0422 4    PHE A C     
27   O  O     . PHE A 4   ? 0.0921 0.0865 0.4417 0.0209  0       -0.0426 4    PHE A O     
28   C  CB    . PHE A 4   ? 0.0678 0.054  0.4097 0.0154  -0.0059 -0.0415 4    PHE A CB    
29   C  CG    . PHE A 4   ? 0.0674 0.0501 0.4026 0.0133  -0.0087 -0.0403 4    PHE A CG    
30   C  CD1   . PHE A 4   ? 0.0726 0.05   0.4048 0.0141  -0.0102 -0.04   4    PHE A CD1   
31   C  CD2   . PHE A 4   ? 0.078  0.0525 0.4123 0.0165  -0.0094 -0.0406 4    PHE A CD2   
32   C  CE1   . PHE A 4   ? 0.0781 0.0485 0.4049 0.0142  -0.013  -0.0395 4    PHE A CE1   
33   C  CE2   . PHE A 4   ? 0.0885 0.0551 0.4173 0.0163  -0.0121 -0.04   4    PHE A CE2   
34   C  CZ    . PHE A 4   ? 0.0829 0.0486 0.408  0.0147  -0.0141 -0.0394 4    PHE A CZ    
35   N  N     . ARG A 5   ? 0.077  0.0687 0.4282 0.0212  -0.0003 -0.0425 5    ARG A N     
36   C  CA    . ARG A 5   ? 0.0863 0.0852 0.4447 0.021   0.0014  -0.0434 5    ARG A CA    
37   C  C     . ARG A 5   ? 0.0871 0.0896 0.4516 0.0187  0.0004  -0.0446 5    ARG A C     
38   O  O     . ARG A 5   ? 0.0894 0.0886 0.4529 0.0179  -0.001  -0.0443 5    ARG A O     
39   C  CB    . ARG A 5   ? 0.0992 0.0983 0.458  0.0234  0.0034  -0.0425 5    ARG A CB    
40   C  CG    . ARG A 5   ? 0.1105 0.108  0.4647 0.0258  0.0049  -0.0413 5    ARG A CG    
41   C  CD    . ARG A 5   ? 0.1241 0.1209 0.4779 0.0284  0.0069  -0.0399 5    ARG A CD    
42   N  NE    . ARG A 5   ? 0.124  0.1207 0.4746 0.0307  0.0086  -0.0386 5    ARG A NE    
43   C  CZ    . ARG A 5   ? 0.1343 0.1325 0.4861 0.033   0.0107  -0.0371 5    ARG A CZ    
44   N  NH1   . ARG A 5   ? 0.1142 0.1138 0.4701 0.0333  0.0114  -0.0366 5    ARG A NH1   
45   N  NH2   . ARG A 5   ? 0.129  0.1274 0.478  0.0349  0.0123  -0.0358 5    ARG A NH2   
46   N  N     . ILE A 6   ? 0.0776 0.0867 0.4481 0.0176  0.001   -0.0459 6    ILE A N     
47   C  CA    . ILE A 6   ? 0.061  0.074  0.4375 0.0157  0.0003  -0.0471 6    ILE A CA    
48   C  C     . ILE A 6   ? 0.0529 0.0706 0.4347 0.016   0.0019  -0.0479 6    ILE A C     
49   O  O     . ILE A 6   ? 0.0426 0.0535 0.4085 0.0048  0.0013  -0.0477 6    ILE A O     
50   C  CB    . ILE A 6   ? 0.0648 0.0815 0.4432 0.0141  -0.0006 -0.0479 6    ILE A CB    
51   C  CG1   . ILE A 6   ? 0.0852 0.0968 0.4579 0.0135  -0.0023 -0.0466 6    ILE A CG1   
52   C  CG2   . ILE A 6   ? 0.0743 0.0951 0.4588 0.0124  -0.0012 -0.0491 6    ILE A CG2   
53   C  CD1   . ILE A 6   ? 0.095  0.1098 0.4696 0.0119  -0.0033 -0.0468 6    ILE A CD1   
54   N  N     . HIS A 7   ? 0.0547 0.0716 0.4392 0.0166  0.0022  -0.0477 7    HIS A N     
55   C  CA    . HIS A 7   ? 0.0536 0.0733 0.4418 0.0155  0.0034  -0.0482 7    HIS A CA    
56   C  C     . HIS A 7   ? 0.0776 0.1024 0.4739 0.0151  0.0028  -0.05   7    HIS A C     
57   O  O     . HIS A 7   ? 0.0724 0.0951 0.4684 0.0141  0.0017  -0.0498 7    HIS A O     
58   C  CB    . HIS A 7   ? 0.0474 0.0585 0.4231 0.0085  0.003   -0.0459 7    HIS A CB    
59   C  CG    . HIS A 7   ? 0.0568 0.0691 0.4369 0.0184  0.0049  -0.0447 7    HIS A CG    
60   N  ND1   . HIS A 7   ? 0.0751 0.0902 0.4591 0.0226  0.0069  -0.0442 7    HIS A ND1   
61   C  CD2   . HIS A 7   ? 0.0584 0.065  0.4305 0.0183  0.004   -0.0435 7    HIS A CD2   
62   C  CE1   . HIS A 7   ? 0.0767 0.0868 0.4537 0.0246  0.0074  -0.0425 7    HIS A CE1   
63   N  NE2   . HIS A 7   ? 0.0658 0.0707 0.4373 0.0241  0.0058  -0.0424 7    HIS A NE2   
64   N  N     . GLY A 8   ? 0.0874 0.1177 0.4886 0.0147  0.0032  -0.0516 8    GLY A N     
65   C  CA    . GLY A 8   ? 0.1029 0.137  0.5093 0.0132  0.0024  -0.0533 8    GLY A CA    
66   C  C     . GLY A 8   ? 0.1236 0.1621 0.5367 0.0133  0.0032  -0.0548 8    GLY A C     
67   O  O     . GLY A 8   ? 0.1266 0.166  0.5406 0.0144  0.0042  -0.0545 8    GLY A O     
68   N  N     . ASP A 9   ? 0.1358 0.1769 0.5533 0.0121  0.0026  -0.0563 9    ASP A N     
69   C  CA    . ASP A 9   ? 0.1529 0.198  0.577  0.0121  0.0029  -0.058  9    ASP A CA    
70   C  C     . ASP A 9   ? 0.133  0.1824 0.5583 0.0124  0.0029  -0.0596 9    ASP A C     
71   O  O     . ASP A 9   ? 0.1278 0.1797 0.5573 0.0128  0.0032  -0.0606 9    ASP A O     
72   C  CB    . ASP A 9   ? 0.2155 0.2618 0.6433 0.0109  0.0022  -0.0591 9    ASP A CB    
73   C  CG    . ASP A 9   ? 0.3348 0.3848 0.7692 0.0107  0.0023  -0.0612 9    ASP A CG    
74   O  OD1   . ASP A 9   ? 0.3607 0.4112 0.7982 0.0113  0.0029  -0.0611 9    ASP A OD1   
75   O  OD2   . ASP A 9   ? 0.3797 0.4323 0.8164 0.0101  0.0016  -0.0629 9    ASP A OD2   
76   N  N     . ASN A 10  ? 0.1209 0.1709 0.5425 0.0124  0.0025  -0.0597 10   ASN A N     
77   C  CA    . ASN A 10  ? 0.1161 0.17   0.5378 0.0129  0.0025  -0.061  10   ASN A CA    
78   C  C     . ASN A 10  ? 0.1195 0.1722 0.5356 0.013   0.0023  -0.0599 10   ASN A C     
79   O  O     . ASN A 10  ? 0.1216 0.1706 0.5342 0.0124  0.0019  -0.0584 10   ASN A O     
80   C  CB    . ASN A 10  ? 0.123  0.1815 0.5497 0.0125  0.0018  -0.0637 10   ASN A CB    
81   C  CG    . ASN A 10  ? 0.1617 0.2202 0.5885 0.0116  0.0011  -0.064  10   ASN A CG    
82   O  OD1   . ASN A 10  ? 0.1717 0.23   0.595  0.0115  0.0008  -0.0631 10   ASN A OD1   
83   N  ND2   . ASN A 10  ? 0.1716 0.2306 0.6027 0.0111  0.0009  -0.065  10   ASN A ND2   
84   N  N     . ILE A 11  ? 0.1187 0.1746 0.534  0.0137  0.0025  -0.0606 11   ILE A N     
85   C  CA    . ILE A 11  ? 0.1266 0.1818 0.537  0.0138  0.0024  -0.0594 11   ILE A CA    
86   C  C     . ILE A 11  ? 0.1347 0.1902 0.5448 0.0129  0.0015  -0.0593 11   ILE A C     
87   O  O     . ILE A 11  ? 0.1425 0.1948 0.5485 0.0125  0.0011  -0.0575 11   ILE A O     
88   C  CB    . ILE A 11  ? 0.1292 0.1882 0.5392 0.0149  0.0029  -0.0601 11   ILE A CB    
89   C  CG1   . ILE A 11  ? 0.1381 0.1954 0.5427 0.0153  0.0031  -0.0584 11   ILE A CG1   
90   C  CG2   . ILE A 11  ? 0.1353 0.2    0.5494 0.015   0.0025  -0.0626 11   ILE A CG2   
91   C  CD1   . ILE A 11  ? 0.1488 0.2    0.5485 0.0155  0.0035  -0.0561 11   ILE A CD1   
92   N  N     . ILE A 12  ? 0.1312 0.19   0.5455 0.0124  0.001   -0.061  12   ILE A N     
93   C  CA    . ILE A 12  ? 0.1304 0.1899 0.5447 0.0117  0.0002  -0.0606 12   ILE A CA    
94   C  C     . ILE A 12  ? 0.1174 0.1719 0.5298 0.0105  -0.0003 -0.0587 12   ILE A C     
95   O  O     . ILE A 12  ? 0.109  0.1622 0.519  0.0099  -0.001  -0.0571 12   ILE A O     
96   C  CB    . ILE A 12  ? 0.1475 0.2117 0.5665 0.0119  0       -0.0628 12   ILE A CB    
97   C  CG1   . ILE A 12  ? 0.17   0.2392 0.5894 0.0131  0.0003  -0.0644 12   ILE A CG1   
98   C  CG2   . ILE A 12  ? 0.15   0.2144 0.5696 0.011   -0.0006 -0.062  12   ILE A CG2   
99   C  CD1   . ILE A 12  ? 0.1903 0.2638 0.614  0.0138  0       -0.0671 12   ILE A CD1   
100  N  N     . GLU A 13  ? 0.1182 0.1699 0.5318 0.0103  -0.0002 -0.0587 13   GLU A N     
101  C  CA    . GLU A 13  ? 0.1271 0.1741 0.5388 0.0093  -0.0008 -0.057  13   GLU A CA    
102  C  C     . GLU A 13  ? 0.1347 0.1771 0.5404 0.0095  -0.0011 -0.055  13   GLU A C     
103  O  O     . GLU A 13  ? 0.14   0.1794 0.5432 0.0086  -0.0021 -0.0534 13   GLU A O     
104  C  CB    . GLU A 13  ? 0.1679 0.2132 0.5821 0.0094  -0.0003 -0.0573 13   GLU A CB    
105  C  CG    . GLU A 13  ? 0.2908 0.34   0.7109 0.0093  -0.0001 -0.0593 13   GLU A CG    
106  C  CD    . GLU A 13  ? 0.45   0.4997 0.8723 0.0082  -0.0008 -0.0592 13   GLU A CD    
107  O  OE1   . GLU A 13  ? 0.4933 0.5415 0.9127 0.0075  -0.0015 -0.0577 13   GLU A OE1   
108  O  OE2   . GLU A 13  ? 0.5118 0.5634 0.9386 0.0081  -0.0005 -0.0606 13   GLU A OE2   
109  N  N     . CYS A 14  ? 0.1181 0.16   0.5217 0.0107  -0.0002 -0.0549 14   CYS A N     
110  C  CA    . CYS A 14  ? 0.1183 0.1557 0.5159 0.0112  -0.0003 -0.0532 14   CYS A CA    
111  C  C     . CYS A 14  ? 0.1212 0.1592 0.5167 0.0106  -0.0012 -0.0524 14   CYS A C     
112  O  O     . CYS A 14  ? 0.1276 0.1613 0.5194 0.0099  -0.0023 -0.0508 14   CYS A O     
113  C  CB    . CYS A 14  ? 0.1241 0.1619 0.5204 0.0128  0.001   -0.0533 14   CYS A CB    
114  S  SG    . CYS A 14  ? 0.1579 0.1947 0.5567 0.0137  0.0021  -0.0534 14   CYS A SG    
115  N  N     . GLU A 15  ? 0.1143 0.1579 0.5126 0.0108  -0.0008 -0.0536 15   GLU A N     
116  C  CA    . GLU A 15  ? 0.115  0.1603 0.5121 0.0104  -0.0014 -0.0527 15   GLU A CA    
117  C  C     . GLU A 15  ? 0.1297 0.1743 0.5278 0.0089  -0.0027 -0.0516 15   GLU A C     
118  O  O     . GLU A 15  ? 0.1358 0.1792 0.5317 0.0084  -0.0036 -0.0499 15   GLU A O     
119  C  CB    . GLU A 15  ? 0.124  0.1755 0.5235 0.0114  -0.0005 -0.0541 15   GLU A CB    
120  C  CG    . GLU A 15  ? 0.1545 0.2064 0.5523 0.0128  0.0006  -0.0545 15   GLU A CG    
121  C  CD    . GLU A 15  ? 0.2492 0.298  0.6418 0.0132  0.0007  -0.0527 15   GLU A CD    
122  O  OE1   . GLU A 15  ? 0.242  0.2882 0.6324 0.0123  -0.0003 -0.051  15   GLU A OE1   
123  O  OE2   . GLU A 15  ? 0.3343 0.3835 0.7254 0.0144  0.0018  -0.0528 15   GLU A OE2   
124  N  N     . ARG A 16  ? 0.137  0.182  0.5384 0.0082  -0.003  -0.0523 16   ARG A N     
125  C  CA    . ARG A 16  ? 0.1449 0.1891 0.5473 0.0068  -0.0043 -0.051  16   ARG A CA    
126  C  C     . ARG A 16  ? 0.1277 0.1654 0.5256 0.0058  -0.0056 -0.049  16   ARG A C     
127  O  O     . ARG A 16  ? 0.1227 0.1598 0.5202 0.0047  -0.007  -0.0473 16   ARG A O     
128  C  CB    . ARG A 16  ? 0.196  0.2416 0.6026 0.0064  -0.0041 -0.0522 16   ARG A CB    
129  C  CG    . ARG A 16  ? 0.2909 0.3428 0.7019 0.0072  -0.0032 -0.0541 16   ARG A CG    
130  C  CD    . ARG A 16  ? 0.3728 0.4269 0.7876 0.0065  -0.0036 -0.0542 16   ARG A CD    
131  N  NE    . ARG A 16  ? 0.4563 0.5094 0.8737 0.0064  -0.0032 -0.0555 16   ARG A NE    
132  C  CZ    . ARG A 16  ? 0.5091 0.5656 0.9305 0.0071  -0.0025 -0.0577 16   ARG A CZ    
133  N  NH1   . ARG A 16  ? 0.5145 0.5758 0.9373 0.0082  -0.0021 -0.0592 16   ARG A NH1   
134  N  NH2   . ARG A 16  ? 0.5116 0.5669 0.9355 0.0069  -0.0022 -0.0585 16   ARG A NH2   
135  N  N     . VAL A 17  ? 0.1184 0.1515 0.513  0.0064  -0.0054 -0.049  17   VAL A N     
136  C  CA    . VAL A 17  ? 0.1249 0.1513 0.5144 0.0059  -0.0068 -0.0472 17   VAL A CA    
137  C  C     . VAL A 17  ? 0.1286 0.1536 0.5145 0.0059  -0.0074 -0.046  17   VAL A C     
138  O  O     . VAL A 17  ? 0.1368 0.1585 0.5207 0.0047  -0.0093 -0.0443 17   VAL A O     
139  C  CB    . VAL A 17  ? 0.137  0.1589 0.5236 0.007   -0.0062 -0.0475 17   VAL A CB    
140  C  CG1   . VAL A 17  ? 0.1544 0.169  0.5349 0.0068  -0.0078 -0.0459 17   VAL A CG1   
141  C  CG2   . VAL A 17  ? 0.1431 0.1661 0.5336 0.0068  -0.0058 -0.0484 17   VAL A CG2   
142  N  N     . ILE A 18  ? 0.1269 0.1548 0.5125 0.0072  -0.006  -0.0467 18   ILE A N     
143  C  CA    . ILE A 18  ? 0.1338 0.1612 0.5165 0.0075  -0.0063 -0.0455 18   ILE A CA    
144  C  C     . ILE A 18  ? 0.1429 0.1735 0.5282 0.0062  -0.0073 -0.0443 18   ILE A C     
145  O  O     . ILE A 18  ? 0.1495 0.1769 0.5323 0.0054  -0.0088 -0.0425 18   ILE A O     
146  C  CB    . ILE A 18  ? 0.1325 0.1636 0.5152 0.0092  -0.0043 -0.0466 18   ILE A CB    
147  C  CG1   . ILE A 18  ? 0.1261 0.154  0.5062 0.0106  -0.0032 -0.0473 18   ILE A CG1   
148  C  CG2   . ILE A 18  ? 0.1409 0.1724 0.5212 0.0095  -0.0044 -0.0454 18   ILE A CG2   
149  C  CD1   . ILE A 18  ? 0.1378 0.1584 0.512  0.0109  -0.004  -0.0459 18   ILE A CD1   
150  N  N     . ASP A 19  ? 0.1438 0.1804 0.5343 0.006   -0.0067 -0.0452 19   ASP A N     
151  C  CA    . ASP A 19  ? 0.1428 0.1831 0.5363 0.0051  -0.0075 -0.0438 19   ASP A CA    
152  C  C     . ASP A 19  ? 0.1356 0.1716 0.5285 0.0032  -0.0097 -0.0419 19   ASP A C     
153  O  O     . ASP A 19  ? 0.1463 0.1826 0.5395 0.0023  -0.0109 -0.0397 19   ASP A O     
154  C  CB    . ASP A 19  ? 0.1838 0.2308 0.5826 0.0056  -0.0065 -0.0453 19   ASP A CB    
155  C  CG    . ASP A 19  ? 0.2861 0.3381 0.6859 0.0075  -0.0047 -0.0472 19   ASP A CG    
156  O  OD1   . ASP A 19  ? 0.32   0.3714 0.717  0.0083  -0.0042 -0.0469 19   ASP A OD1   
157  O  OD2   . ASP A 19  ? 0.3363 0.3927 0.7397 0.0081  -0.0039 -0.049  19   ASP A OD2   
158  N  N     . LEU A 20  ? 0.1223 0.1545 0.5146 0.0026  -0.0103 -0.0424 20   LEU A N     
159  C  CA    . LEU A 20  ? 0.1255 0.1533 0.5169 0.0008  -0.0125 -0.0405 20   LEU A CA    
160  C  C     . LEU A 20  ? 0.1442 0.1659 0.5304 0.0003  -0.0142 -0.039  20   LEU A C     
161  O  O     . LEU A 20  ? 0.1557 0.1759 0.5419 -0.0012 -0.0162 -0.0368 20   LEU A O     
162  C  CB    . LEU A 20  ? 0.1207 0.1456 0.512  0.0006  -0.0127 -0.0415 20   LEU A CB    
163  C  CG    . LEU A 20  ? 0.1153 0.1451 0.512  0.0005  -0.0118 -0.0425 20   LEU A CG    
164  C  CD1   . LEU A 20  ? 0.1091 0.1363 0.5056 0.0007  -0.0113 -0.0437 20   LEU A CD1   
165  C  CD2   . LEU A 20  ? 0.1184 0.1502 0.5181 -0.0012 -0.0132 -0.0404 20   LEU A CD2   
166  N  N     . ILE A 21  ? 0.1464 0.1647 0.5281 0.0017  -0.0134 -0.0399 21   ILE A N     
167  C  CA    . ILE A 21  ? 0.1581 0.1702 0.5343 0.0016  -0.0148 -0.0387 21   ILE A CA    
168  C  C     . ILE A 21  ? 0.1668 0.1817 0.5441 0.0012  -0.0151 -0.0371 21   ILE A C     
169  O  O     . ILE A 21  ? 0.1754 0.1869 0.5515 -0.0002 -0.0174 -0.0351 21   ILE A O     
170  C  CB    . ILE A 21  ? 0.167  0.1756 0.5385 0.0037  -0.0134 -0.04   21   ILE A CB    
171  C  CG1   . ILE A 21  ? 0.1804 0.185  0.5501 0.004   -0.0136 -0.0408 21   ILE A CG1   
172  C  CG2   . ILE A 21  ? 0.1838 0.1871 0.5496 0.0041  -0.0143 -0.0389 21   ILE A CG2   
173  C  CD1   . ILE A 21  ? 0.2029 0.2069 0.5704 0.0063  -0.0114 -0.0422 21   ILE A CD1   
174  N  N     . LEU A 22  ? 0.1674 0.1887 0.5475 0.0025  -0.013  -0.0379 22   LEU A N     
175  C  CA    . LEU A 22  ? 0.1797 0.2046 0.5611 0.0025  -0.0128 -0.0364 22   LEU A CA    
176  C  C     . LEU A 22  ? 0.2068 0.2349 0.5926 0.0009  -0.0141 -0.0343 22   LEU A C     
177  O  O     . LEU A 22  ? 0.2152 0.2449 0.6017 0.0007  -0.0146 -0.0324 22   LEU A O     
178  C  CB    . LEU A 22  ? 0.1675 0.1987 0.5505 0.0045  -0.0101 -0.038  22   LEU A CB    
179  C  CG    . LEU A 22  ? 0.1761 0.2045 0.5548 0.0061  -0.0088 -0.0394 22   LEU A CG    
180  C  CD1   . LEU A 22  ? 0.173  0.208  0.554  0.0079  -0.0064 -0.0409 22   LEU A CD1   
181  C  CD2   . LEU A 22  ? 0.1829 0.2055 0.5565 0.0061  -0.0098 -0.0378 22   LEU A CD2   
182  N  N     . SER A 23  ? 0.2184 0.2474 0.6071 -0.0002 -0.0149 -0.0343 23   SER A N     
183  C  CA    . SER A 23  ? 0.2289 0.2606 0.6219 -0.0018 -0.0162 -0.032  23   SER A CA    
184  C  C     . SER A 23  ? 0.249  0.2744 0.6397 -0.0038 -0.0193 -0.0294 23   SER A C     
185  O  O     . SER A 23  ? 0.257  0.2847 0.6511 -0.0051 -0.0206 -0.0268 23   SER A O     
186  C  CB    . SER A 23  ? 0.2387 0.2728 0.6352 -0.0022 -0.016  -0.0329 23   SER A CB    
187  O  OG    . SER A 23  ? 0.2527 0.2806 0.6468 -0.0034 -0.0177 -0.033  23   SER A OG    
188  N  N     . LYS A 24  ? 0.2502 0.2679 0.6355 -0.004  -0.0206 -0.0302 24   LYS A N     
189  C  CA    . LYS A 24  ? 0.2611 0.2721 0.6436 -0.0058 -0.0238 -0.0281 24   LYS A CA    
190  C  C     . LYS A 24  ? 0.267  0.2732 0.6444 -0.005  -0.0241 -0.0279 24   LYS A C     
191  O  O     . LYS A 24  ? 0.2663 0.269  0.6428 -0.0064 -0.0265 -0.0258 24   LYS A O     
192  C  CB    . LYS A 24  ? 0.3007 0.3058 0.6807 -0.0066 -0.0255 -0.0289 24   LYS A CB    
193  C  CG    . LYS A 24  ? 0.3948 0.3928 0.7721 -0.0086 -0.0293 -0.0269 24   LYS A CG    
194  C  CD    . LYS A 24  ? 0.4795 0.4708 0.8527 -0.009  -0.031  -0.0279 24   LYS A CD    
195  C  CE    . LYS A 24  ? 0.5335 0.516  0.9015 -0.0101 -0.0346 -0.0269 24   LYS A CE    
196  N  NZ    . LYS A 24  ? 0.5619 0.538  0.9254 -0.0099 -0.036  -0.0282 24   LYS A NZ    
197  N  N     . ILE A 25  ? 0.2744 0.2805 0.6486 -0.0029 -0.0218 -0.0301 25   ILE A N     
198  C  CA    . ILE A 25  ? 0.2929 0.2952 0.6624 -0.0018 -0.0216 -0.03   25   ILE A CA    
199  C  C     . ILE A 25  ? 0.3025 0.3118 0.6754 -0.001  -0.0198 -0.0291 25   ILE A C     
200  O  O     . ILE A 25  ? 0.3089 0.3249 0.685  0.0002  -0.0172 -0.0305 25   ILE A O     
201  C  CB    . ILE A 25  ? 0.3014 0.301  0.6661 0.0004  -0.0197 -0.0325 25   ILE A CB    
202  C  CG1   . ILE A 25  ? 0.3167 0.31   0.6779 0.0002  -0.021  -0.0335 25   ILE A CG1   
203  C  CG2   . ILE A 25  ? 0.3065 0.3029 0.6666 0.0018  -0.0191 -0.0322 25   ILE A CG2   
204  C  CD1   . ILE A 25  ? 0.3366 0.3213 0.693  -0.0009 -0.0242 -0.0323 25   ILE A CD1   
205  N  N     . ASN A 26  ? 0.3025 0.31   0.6746 -0.0016 -0.021  -0.0269 26   ASN A N     
206  C  CA    . ASN A 26  ? 0.3102 0.3238 0.6848 -0.0005 -0.0191 -0.0261 26   ASN A CA    
207  C  C     . ASN A 26  ? 0.3039 0.3126 0.6725 0.001   -0.0184 -0.0267 26   ASN A C     
208  O  O     . ASN A 26  ? 0.3106 0.3127 0.6757 0.0002  -0.0205 -0.0254 26   ASN A O     
209  C  CB    . ASN A 26  ? 0.347  0.3632 0.726  -0.0021 -0.0206 -0.0227 26   ASN A CB    
210  C  CG    . ASN A 26  ? 0.4208 0.4431 0.8019 -0.0007 -0.0186 -0.0216 26   ASN A CG    
211  O  OD1   . ASN A 26  ? 0.4478 0.4754 0.8294 0.0013  -0.0157 -0.0235 26   ASN A OD1   
212  N  ND2   . ASN A 26  ? 0.4357 0.4569 0.8179 -0.0017 -0.0201 -0.0186 26   ASN A ND2   
213  N  N     . PRO A 27  ? 0.2889 0.3005 0.6562 0.0032  -0.0155 -0.0289 27   PRO A N     
214  C  CA    . PRO A 27  ? 0.2882 0.295  0.6496 0.0048  -0.0147 -0.0294 27   PRO A CA    
215  C  C     . PRO A 27  ? 0.2849 0.2935 0.6461 0.0054  -0.014  -0.0277 27   PRO A C     
216  O  O     . PRO A 27  ? 0.2927 0.3087 0.6588 0.0055  -0.0129 -0.0267 27   PRO A O     
217  C  CB    . PRO A 27  ? 0.2952 0.3051 0.656  0.0067  -0.012  -0.0321 27   PRO A CB    
218  C  CG    . PRO A 27  ? 0.2955 0.3106 0.6617 0.0059  -0.0118 -0.0331 27   PRO A CG    
219  C  CD    . PRO A 27  ? 0.2757 0.2942 0.6465 0.0043  -0.0131 -0.0309 27   PRO A CD    
220  N  N     . GLN A 28  ? 0.2722 0.274  0.6278 0.006   -0.0146 -0.0273 28   GLN A N     
221  C  CA    . GLN A 28  ? 0.271  0.2735 0.6256 0.0069  -0.0138 -0.0258 28   GLN A CA    
222  C  C     . GLN A 28  ? 0.2626 0.2706 0.6169 0.0094  -0.0102 -0.0273 28   GLN A C     
223  O  O     . GLN A 28  ? 0.2571 0.2709 0.614  0.0102  -0.0086 -0.0262 28   GLN A O     
224  C  CB    . GLN A 28  ? 0.3038 0.2961 0.6516 0.0069  -0.0157 -0.0251 28   GLN A CB    
225  C  CG    . GLN A 28  ? 0.3893 0.3746 0.7362 0.0045  -0.0195 -0.0242 28   GLN A CG    
226  C  CD    . GLN A 28  ? 0.472  0.4605 0.8246 0.0023  -0.0213 -0.0215 28   GLN A CD    
227  O  OE1   . GLN A 28  ? 0.5073 0.4956 0.8604 0.0022  -0.0217 -0.0195 28   GLN A OE1   
228  N  NE2   . GLN A 28  ? 0.4785 0.4703 0.8359 0.0006  -0.0224 -0.0213 28   GLN A NE2   
229  N  N     . LYS A 29  ? 0.2498 0.2561 0.6011 0.0107  -0.009  -0.0295 29   LYS A N     
230  C  CA    . LYS A 29  ? 0.2427 0.2536 0.5937 0.013   -0.0059 -0.031  29   LYS A CA    
231  C  C     . LYS A 29  ? 0.2184 0.2314 0.5709 0.0132  -0.0051 -0.0333 29   LYS A C     
232  O  O     . LYS A 29  ? 0.2104 0.2179 0.5609 0.0125  -0.0066 -0.0338 29   LYS A O     
233  C  CB    . LYS A 29  ? 0.2797 0.2845 0.6238 0.0148  -0.0051 -0.0308 29   LYS A CB    
234  C  CG    . LYS A 29  ? 0.358  0.3594 0.7    0.0145  -0.0061 -0.0286 29   LYS A CG    
235  C  CD    . LYS A 29  ? 0.4225 0.415  0.7568 0.0159  -0.0063 -0.0284 29   LYS A CD    
236  C  CE    . LYS A 29  ? 0.4624 0.4506 0.7946 0.0154  -0.0077 -0.0262 29   LYS A CE    
237  N  NZ    . LYS A 29  ? 0.4947 0.4772 0.8199 0.0177  -0.0065 -0.0261 29   LYS A NZ    
238  N  N     . VAL A 30  ? 0.2028 0.2237 0.5592 0.0143  -0.0029 -0.0345 30   VAL A N     
239  C  CA    . VAL A 30  ? 0.1981 0.2219 0.5568 0.0146  -0.002  -0.0367 30   VAL A CA    
240  C  C     . VAL A 30  ? 0.1821 0.2102 0.5407 0.0167  0.0006  -0.0378 30   VAL A C     
241  O  O     . VAL A 30  ? 0.1678 0.2015 0.5283 0.0175  0.0018  -0.0374 30   VAL A O     
242  C  CB    . VAL A 30  ? 0.2048 0.2349 0.5699 0.0134  -0.0024 -0.0374 30   VAL A CB    
243  C  CG1   . VAL A 30  ? 0.2043 0.2369 0.5716 0.0139  -0.0015 -0.0397 30   VAL A CG1   
244  C  CG2   . VAL A 30  ? 0.2219 0.2487 0.5879 0.0113  -0.0049 -0.036  30   VAL A CG2   
245  N  N     . LYS A 31  ? 0.1788 0.2046 0.5353 0.0177  0.0014  -0.039  31   LYS A N     
246  C  CA    . LYS A 31  ? 0.1784 0.208  0.5352 0.0196  0.0037  -0.0399 31   LYS A CA    
247  C  C     . LYS A 31  ? 0.162  0.1941 0.5221 0.0196  0.0041  -0.0419 31   LYS A C     
248  O  O     . LYS A 31  ? 0.1543 0.1819 0.5135 0.0189  0.0031  -0.0421 31   LYS A O     
249  C  CB    . LYS A 31  ? 0.239  0.263  0.5896 0.0212  0.0046  -0.0389 31   LYS A CB    
250  C  CG    . LYS A 31  ? 0.3412 0.3692 0.6922 0.0232  0.007   -0.0395 31   LYS A CG    
251  C  CD    . LYS A 31  ? 0.4426 0.4654 0.7873 0.0251  0.0082  -0.0381 31   LYS A CD    
252  C  CE    . LYS A 31  ? 0.5176 0.545  0.8634 0.027   0.0105  -0.0385 31   LYS A CE    
253  N  NZ    . LYS A 31  ? 0.5689 0.5958 0.9108 0.0287  0.012   -0.0369 31   LYS A NZ    
254  N  N     . ARG A 32  ? 0.1494 0.1885 0.5134 0.0203  0.0055  -0.0432 32   ARG A N     
255  C  CA    . ARG A 32  ? 0.147  0.1886 0.5146 0.0203  0.0059  -0.045  32   ARG A CA    
256  C  C     . ARG A 32  ? 0.1481 0.1925 0.5158 0.022   0.0077  -0.0455 32   ARG A C     
257  O  O     . ARG A 32  ? 0.142  0.1888 0.5085 0.0231  0.0088  -0.0449 32   ARG A O     
258  C  CB    . ARG A 32  ? 0.1491 0.1967 0.5224 0.0193  0.0052  -0.0465 32   ARG A CB    
259  C  CG    . ARG A 32  ? 0.1431 0.188  0.5174 0.0175  0.0034  -0.0462 32   ARG A CG    
260  C  CD    . ARG A 32  ? 0.1667 0.218  0.5466 0.0169  0.0032  -0.0477 32   ARG A CD    
261  N  NE    . ARG A 32  ? 0.2033 0.2528 0.5847 0.0152  0.0016  -0.0474 32   ARG A NE    
262  C  CZ    . ARG A 32  ? 0.2366 0.2841 0.6195 0.0145  0.001   -0.0482 32   ARG A CZ    
263  N  NH1   . ARG A 32  ? 0.2221 0.2686 0.605  0.0152  0.0018  -0.0494 32   ARG A NH1   
264  N  NH2   . ARG A 32  ? 0.2495 0.2959 0.6339 0.013   -0.0003 -0.0478 32   ARG A NH2   
265  N  N     . GLY A 33  ? 0.1432 0.1873 0.5126 0.0222  0.008   -0.0464 33   GLY A N     
266  C  CA    . GLY A 33  ? 0.1342 0.181  0.5044 0.0237  0.0096  -0.0466 33   GLY A CA    
267  C  C     . GLY A 33  ? 0.1174 0.1628 0.4896 0.0237  0.0097  -0.0472 33   GLY A C     
268  O  O     . GLY A 33  ? 0.1065 0.1512 0.4813 0.0225  0.0086  -0.0481 33   GLY A O     
269  N  N     . PHE A 34  ? 0.1019 0.1466 0.4729 0.0253  0.0111  -0.0462 34   PHE A N     
270  C  CA    . PHE A 34  ? 0.1001 0.1437 0.4733 0.0255  0.0114  -0.0463 34   PHE A CA    
271  C  C     . PHE A 34  ? 0.1026 0.1404 0.4703 0.0273  0.0125  -0.044  34   PHE A C     
272  O  O     . PHE A 34  ? 0.1052 0.1429 0.4696 0.0288  0.0137  -0.0427 34   PHE A O     
273  C  CB    . PHE A 34  ? 0.0938 0.1441 0.4727 0.0259  0.0121  -0.0474 34   PHE A CB    
274  C  CG    . PHE A 34  ? 0.1081 0.1637 0.4931 0.0244  0.0109  -0.05   34   PHE A CG    
275  C  CD1   . PHE A 34  ? 0.1276 0.1876 0.5137 0.024   0.0104  -0.0512 34   PHE A CD1   
276  C  CD2   . PHE A 34  ? 0.1128 0.1688 0.5023 0.0236  0.0103  -0.0511 34   PHE A CD2   
277  C  CE1   . PHE A 34  ? 0.1388 0.2033 0.5299 0.0229  0.0093  -0.0536 34   PHE A CE1   
278  C  CE2   . PHE A 34  ? 0.1263 0.1868 0.5211 0.0223  0.0091  -0.0535 34   PHE A CE2   
279  C  CZ    . PHE A 34  ? 0.1298 0.1944 0.5252 0.0221  0.0087  -0.0548 34   PHE A CZ    
280  N  N     . ILE A 35  ? 0.1003 0.1336 0.4669 0.0275  0.0122  -0.0434 35   ILE A N     
281  C  CA    . ILE A 35  ? 0.1085 0.1367 0.47   0.0297  0.0135  -0.0411 35   ILE A CA    
282  C  C     . ILE A 35  ? 0.0973 0.1291 0.463  0.0309  0.015   -0.0404 35   ILE A C     
283  O  O     . ILE A 35  ? 0.0977 0.127  0.46   0.0332  0.0166  -0.0383 35   ILE A O     
284  C  CB    . ILE A 35  ? 0.1375 0.1584 0.4949 0.0297  0.0125  -0.0405 35   ILE A CB    
285  C  CG1   . ILE A 35  ? 0.1598 0.1821 0.5226 0.0286  0.0119  -0.0416 35   ILE A CG1   
286  C  CG2   . ILE A 35  ? 0.1414 0.1584 0.4947 0.0285  0.0108  -0.0409 35   ILE A CG2   
287  C  CD1   . ILE A 35  ? 0.1877 0.2038 0.5468 0.0296  0.0117  -0.0404 35   ILE A CD1   
288  N  N     . SER A 36  ? 0.0814 0.1188 0.4544 0.0295  0.0145  -0.0422 36   SER A N     
289  C  CA    . SER A 36  ? 0.0757 0.1175 0.4543 0.03    0.0154  -0.0419 36   SER A CA    
290  C  C     . SER A 36  ? 0.0654 0.1138 0.4508 0.0281  0.0143  -0.0446 36   SER A C     
291  O  O     . SER A 36  ? 0.0557 0.1049 0.4409 0.0268  0.0131  -0.0463 36   SER A O     
292  C  CB    . SER A 36  ? 0.0939 0.1328 0.4739 0.0304  0.0156  -0.041  36   SER A CB    
293  O  OG    . SER A 36  ? 0.1036 0.1435 0.4881 0.0284  0.014   -0.043  36   SER A OG    
294  N  N     . LEU A 37  ? 0.0593 0.1124 0.4507 0.0281  0.0146  -0.0449 37   LEU A N     
295  C  CA    . LEU A 37  ? 0.0598 0.1189 0.4574 0.0266  0.0133  -0.0476 37   LEU A CA    
296  C  C     . LEU A 37  ? 0.0612 0.1197 0.4617 0.0248  0.0118  -0.0497 37   LEU A C     
297  O  O     . LEU A 37  ? 0.0678 0.1297 0.4705 0.0237  0.0106  -0.0521 37   LEU A O     
298  C  CB    . LEU A 37  ? 0.0589 0.1224 0.4623 0.027   0.0138  -0.0472 37   LEU A CB    
299  C  CG    . LEU A 37  ? 0.0838 0.1499 0.4857 0.0285  0.015   -0.0456 37   LEU A CG    
300  C  CD1   . LEU A 37  ? 0.0854 0.1539 0.4922 0.0293  0.0158  -0.0438 37   LEU A CD1   
301  C  CD2   . LEU A 37  ? 0.0894 0.1604 0.4923 0.0279  0.0142  -0.0478 37   LEU A CD2   
302  N  N     . SER A 38  ? 0.0603 0.1146 0.4605 0.0248  0.0118  -0.0488 38   SER A N     
303  C  CA    . SER A 38  ? 0.0559 0.1094 0.4589 0.0232  0.0105  -0.0504 38   SER A CA    
304  C  C     . SER A 38  ? 0.058  0.1071 0.456  0.0226  0.0099  -0.0504 38   SER A C     
305  O  O     . SER A 38  ? 0.0512 0.0984 0.4491 0.0202  0.0086  -0.0517 38   SER A O     
306  C  CB    . SER A 38  ? 0.0766 0.1279 0.4821 0.0236  0.011   -0.0491 38   SER A CB    
307  O  OG    . SER A 38  ? 0.0994 0.1548 0.511  0.0238  0.0114  -0.049  38   SER A OG    
308  N  N     . CYS A 39  ? 0.0601 0.1051 0.4514 0.0237  0.0105  -0.0486 39   CYS A N     
309  C  CA    . CYS A 39  ? 0.0666 0.1065 0.453  0.0231  0.0097  -0.0482 39   CYS A CA    
310  C  C     . CYS A 39  ? 0.0578 0.0976 0.4404 0.0229  0.0092  -0.0483 39   CYS A C     
311  O  O     . CYS A 39  ? 0.0541 0.0891 0.4286 0.0225  0.0097  -0.0466 39   CYS A O     
312  C  CB    . CYS A 39  ? 0.0847 0.1183 0.466  0.0247  0.0104  -0.0459 39   CYS A CB    
313  S  SG    . CYS A 39  ? 0.122  0.1555 0.5077 0.0253  0.0111  -0.0451 39   CYS A SG    
314  N  N     . PRO A 40  ? 0.054  0.0967 0.439  0.0213  0.008   -0.05   40   PRO A N     
315  C  CA    . PRO A 40  ? 0.0522 0.0915 0.4299 0.0192  0.0072  -0.0496 40   PRO A CA    
316  C  C     . PRO A 40  ? 0.055  0.0895 0.4296 0.0201  0.0066  -0.0482 40   PRO A C     
317  O  O     . PRO A 40  ? 0.0543 0.0823 0.4245 0.0176  0.0058  -0.0476 40   PRO A O     
318  C  CB    . PRO A 40  ? 0.0531 0.1004 0.4393 0.0196  0.0065  -0.0517 40   PRO A CB    
319  C  CG    . PRO A 40  ? 0.0642 0.1138 0.4558 0.0191  0.0063  -0.0532 40   PRO A CG    
320  C  CD    . PRO A 40  ? 0.05   0.0921 0.4363 0.0179  0.0067  -0.0518 40   PRO A CD    
321  N  N     . PHE A 41  ? 0.0546 0.0869 0.4241 0.0195  0.0063  -0.0472 41   PHE A N     
322  C  CA    . PHE A 41  ? 0.0657 0.0933 0.4326 0.0205  0.0053  -0.0461 41   PHE A CA    
323  C  C     . PHE A 41  ? 0.0631 0.0921 0.4301 0.0192  0.0042  -0.046  41   PHE A C     
324  O  O     . PHE A 41  ? 0.0635 0.0981 0.4329 0.0193  0.0048  -0.0466 41   PHE A O     
325  C  CB    . PHE A 41  ? 0.0713 0.0933 0.4316 0.0224  0.0062  -0.0443 41   PHE A CB    
326  C  CG    . PHE A 41  ? 0.0875 0.1105 0.445  0.0233  0.0071  -0.0434 41   PHE A CG    
327  C  CD1   . PHE A 41  ? 0.1039 0.1244 0.4583 0.0226  0.006   -0.0427 41   PHE A CD1   
328  C  CD2   . PHE A 41  ? 0.0948 0.1214 0.4529 0.0249  0.009   -0.0432 41   PHE A CD2   
329  C  CE1   . PHE A 41  ? 0.1103 0.132  0.4624 0.0235  0.0068  -0.0418 41   PHE A CE1   
330  C  CE2   . PHE A 41  ? 0.1094 0.1372 0.4651 0.0259  0.0099  -0.0424 41   PHE A CE2   
331  C  CZ    . PHE A 41  ? 0.1084 0.1337 0.461  0.0252  0.0089  -0.0417 41   PHE A CZ    
332  N  N     . ILE A 42  ? 0.054  0.0778 0.4181 0.0181  0.0025  -0.0451 42   ILE A N     
333  C  CA    . ILE A 42  ? 0.0548 0.0783 0.418  0.017   0.0013  -0.0443 42   ILE A CA    
334  C  C     . ILE A 42  ? 0.0711 0.0864 0.4277 0.0172  0.0002  -0.0427 42   ILE A C     
335  O  O     . ILE A 42  ? 0.0742 0.0841 0.4283 0.0172  -0.0006 -0.0425 42   ILE A O     
336  C  CB    . ILE A 42  ? 0.0486 0.071  0.4107 0.0121  -0.0004 -0.0446 42   ILE A CB    
337  C  CG1   . ILE A 42  ? 0.0529 0.0787 0.4195 0.014   -0.0014 -0.0433 42   ILE A CG1   
338  C  CG2   . ILE A 42  ? 0.0481 0.0664 0.4096 0.0103  -0.0016 -0.0449 42   ILE A CG2   
339  C  CD1   . ILE A 42  ? 0.0664 0.0968 0.438  0.0125  -0.0023 -0.0433 42   ILE A CD1   
340  N  N     . GLU A 43  ? 0.0801 0.0944 0.4336 0.0177  0.0004  -0.0415 43   GLU A N     
341  C  CA    . GLU A 43  ? 0.1036 0.11   0.4505 0.0181  -0.0007 -0.0401 43   GLU A CA    
342  C  C     . GLU A 43  ? 0.1213 0.1271 0.4689 0.0163  -0.0027 -0.039  43   GLU A C     
343  O  O     . GLU A 43  ? 0.1168 0.1283 0.4677 0.016   -0.0021 -0.0388 43   GLU A O     
344  C  CB    . GLU A 43  ? 0.1418 0.1474 0.4848 0.0204  0.0012  -0.0394 43   GLU A CB    
345  C  CG    . GLU A 43  ? 0.2132 0.2099 0.5486 0.0213  0.0003  -0.0381 43   GLU A CG    
346  C  CD    . GLU A 43  ? 0.3201 0.3156 0.6511 0.0239  0.0024  -0.0373 43   GLU A CD    
347  O  OE1   . GLU A 43  ? 0.349  0.3498 0.6826 0.0251  0.0046  -0.0378 43   GLU A OE1   
348  O  OE2   . GLU A 43  ? 0.3511 0.3399 0.676  0.0247  0.0017  -0.0361 43   GLU A OE2   
349  N  N     . ILE A 44  ? 0.1344 0.1336 0.4791 0.0151  -0.0051 -0.0383 44   ILE A N     
350  C  CA    . ILE A 44  ? 0.1466 0.1449 0.4922 0.0132  -0.0072 -0.0369 44   ILE A CA    
351  C  C     . ILE A 44  ? 0.1649 0.1542 0.504  0.0132  -0.0092 -0.0356 44   ILE A C     
352  O  O     . ILE A 44  ? 0.1648 0.1472 0.4988 0.014   -0.0099 -0.036  44   ILE A O     
353  C  CB    . ILE A 44  ? 0.147  0.1476 0.4976 0.011   -0.0089 -0.0371 44   ILE A CB    
354  C  CG1   . ILE A 44  ? 0.1632 0.1573 0.5109 0.0105  -0.0105 -0.0375 44   ILE A CG1   
355  C  CG2   . ILE A 44  ? 0.1497 0.1592 0.5068 0.0109  -0.0072 -0.0384 44   ILE A CG2   
356  C  CD1   . ILE A 44  ? 0.1909 0.186  0.5426 0.0082  -0.0125 -0.0372 44   ILE A CD1   
357  N  N     . ILE A 45  ? 0.1681 0.1575 0.5075 0.0124  -0.0101 -0.0341 45   ILE A N     
358  C  CA    . ILE A 45  ? 0.183  0.1642 0.5172 0.0119  -0.0124 -0.0328 45   ILE A CA    
359  C  C     . ILE A 45  ? 0.1671 0.1494 0.5057 0.0091  -0.015  -0.0315 45   ILE A C     
360  O  O     . ILE A 45  ? 0.1598 0.1494 0.5042 0.0083  -0.0143 -0.0308 45   ILE A O     
361  C  CB    . ILE A 45  ? 0.2063 0.1866 0.5375 0.0132  -0.0114 -0.0316 45   ILE A CB    
362  C  CG1   . ILE A 45  ? 0.2385 0.2196 0.5664 0.0161  -0.0083 -0.0325 45   ILE A CG1   
363  C  CG2   . ILE A 45  ? 0.2185 0.1893 0.5442 0.0126  -0.0143 -0.0304 45   ILE A CG2   
364  C  CD1   . ILE A 45  ? 0.269  0.2434 0.5911 0.0177  -0.0083 -0.0334 45   ILE A CD1   
365  N  N     . PHE A 46  ? 0.1561 0.1315 0.4921 0.0078  -0.018  -0.0313 46   PHE A N     
366  C  CA    . PHE A 46  ? 0.1446 0.1205 0.4848 0.005   -0.0208 -0.0298 46   PHE A CA    
367  C  C     . PHE A 46  ? 0.1394 0.1052 0.4743 0.0039  -0.0245 -0.0289 46   PHE A C     
368  O  O     . PHE A 46  ? 0.1374 0.0959 0.4653 0.0055  -0.0248 -0.0298 46   PHE A O     
369  C  CB    . PHE A 46  ? 0.1358 0.1165 0.4812 0.0039  -0.0207 -0.0306 46   PHE A CB    
370  C  CG    . PHE A 46  ? 0.1501 0.1254 0.4921 0.004   -0.0218 -0.0319 46   PHE A CG    
371  C  CD1   . PHE A 46  ? 0.1743 0.1498 0.514  0.0061  -0.0195 -0.0338 46   PHE A CD1   
372  C  CD2   . PHE A 46  ? 0.1609 0.1312 0.5023 0.002   -0.0252 -0.0312 46   PHE A CD2   
373  C  CE1   . PHE A 46  ? 0.1857 0.1568 0.5228 0.0064  -0.0203 -0.0348 46   PHE A CE1   
374  C  CE2   . PHE A 46  ? 0.1772 0.1427 0.5154 0.0023  -0.0262 -0.0324 46   PHE A CE2   
375  C  CZ    . PHE A 46  ? 0.1783 0.1444 0.5145 0.0046  -0.0236 -0.0341 46   PHE A CZ    
376  N  N     . LYS A 47  ? 0.139  0.1043 0.4772 0.0013  -0.0274 -0.027  47   LYS A N     
377  C  CA    . LYS A 47  ? 0.1512 0.107  0.485  0       -0.0314 -0.0262 47   LYS A CA    
378  C  C     . LYS A 47  ? 0.1534 0.1091 0.4912 -0.0028 -0.0344 -0.0252 47   LYS A C     
379  O  O     . LYS A 47  ? 0.1602 0.1238 0.5052 -0.0041 -0.0336 -0.0243 47   LYS A O     
380  C  CB    . LYS A 47  ? 0.1761 0.1288 0.5084 -0.0003 -0.0325 -0.0244 47   LYS A CB    
381  C  CG    . LYS A 47  ? 0.2261 0.1866 0.5663 -0.0019 -0.0322 -0.022  47   LYS A CG    
382  C  CD    . LYS A 47  ? 0.2766 0.2345 0.6155 -0.0018 -0.0328 -0.0201 47   LYS A CD    
383  C  CE    . LYS A 47  ? 0.3218 0.2887 0.6687 -0.0029 -0.0318 -0.0176 47   LYS A CE    
384  N  NZ    . LYS A 47  ? 0.375  0.3437 0.721  -0.0012 -0.0296 -0.0168 47   LYS A NZ    
385  N  N     . GLU A 48  ? 0.1473 0.094  0.4802 -0.0036 -0.0379 -0.0254 48   GLU A N     
386  C  CA    . GLU A 48  ? 0.1463 0.0913 0.4821 -0.0064 -0.0415 -0.0243 48   GLU A CA    
387  C  C     . GLU A 48  ? 0.1528 0.0902 0.4855 -0.0077 -0.0452 -0.0227 48   GLU A C     
388  O  O     . GLU A 48  ? 0.1552 0.0829 0.4801 -0.0067 -0.0473 -0.0238 48   GLU A O     
389  C  CB    . GLU A 48  ? 0.1772 0.1173 0.5087 -0.0058 -0.0425 -0.0262 48   GLU A CB    
390  C  CG    . GLU A 48  ? 0.2365 0.1837 0.5709 -0.0045 -0.0389 -0.0278 48   GLU A CG    
391  C  CD    . GLU A 48  ? 0.3617 0.3045 0.6923 -0.0037 -0.0396 -0.0295 48   GLU A CD    
392  O  OE1   . GLU A 48  ? 0.3769 0.3106 0.7012 -0.0037 -0.0426 -0.0297 48   GLU A OE1   
393  O  OE2   . GLU A 48  ? 0.4417 0.3902 0.7756 -0.0031 -0.0371 -0.0305 48   GLU A OE2   
394  N  N     . GLY A 49  ? 0.1485 0.0901 0.4869 -0.0094 -0.0457 -0.0201 49   GLY A N     
395  C  CA    . GLY A 49  ? 0.1501 0.0853 0.4868 -0.0107 -0.0491 -0.0182 49   GLY A CA    
396  C  C     . GLY A 49  ? 0.1532 0.0844 0.4838 -0.0082 -0.0474 -0.0191 49   GLY A C     
397  O  O     . GLY A 49  ? 0.1583 0.0962 0.4913 -0.0067 -0.0437 -0.0189 49   GLY A O     
398  N  N     . HIS A 50  ? 0.1495 0.0695 0.4719 -0.0075 -0.0502 -0.0201 50   HIS A N     
399  C  CA    . HIS A 50  ? 0.1533 0.0678 0.4684 -0.0048 -0.0488 -0.0212 50   HIS A CA    
400  C  C     . HIS A 50  ? 0.159  0.0728 0.4681 -0.0014 -0.0455 -0.0241 50   HIS A C     
401  O  O     . HIS A 50  ? 0.1704 0.0819 0.4743 0.0013  -0.0433 -0.0248 50   HIS A O     
402  C  CB    . HIS A 50  ? 0.1552 0.0575 0.4638 -0.0055 -0.0535 -0.021  50   HIS A CB    
403  C  CG    . HIS A 50  ? 0.1671 0.0688 0.4807 -0.0085 -0.0568 -0.018  50   HIS A CG    
404  N  ND1   . HIS A 50  ? 0.181  0.0801 0.4934 -0.0081 -0.0568 -0.0167 50   HIS A ND1   
405  C  CD2   . HIS A 50  ? 0.1646 0.0677 0.4845 -0.012  -0.0603 -0.016  50   HIS A CD2   
406  C  CE1   . HIS A 50  ? 0.1843 0.0835 0.5025 -0.0113 -0.0602 -0.0139 50   HIS A CE1   
407  N  NE2   . HIS A 50  ? 0.183  0.0849 0.5061 -0.0137 -0.0624 -0.0132 50   HIS A NE2   
408  N  N     . ASP A 51  ? 0.1516 0.0663 0.4609 -0.0015 -0.0455 -0.0255 51   ASP A N     
409  C  CA    . ASP A 51  ? 0.1653 0.0792 0.4695 0.0016  -0.0428 -0.0279 51   ASP A CA    
410  C  C     . ASP A 51  ? 0.1617 0.0859 0.4705 0.0031  -0.0377 -0.0284 51   ASP A C     
411  O  O     . ASP A 51  ? 0.1503 0.0823 0.466  0.0018  -0.0367 -0.0283 51   ASP A O     
412  C  CB    . ASP A 51  ? 0.1946 0.1051 0.4974 0.0009  -0.0451 -0.029  51   ASP A CB    
413  C  CG    . ASP A 51  ? 0.2996 0.2055 0.5949 0.0042  -0.0436 -0.0311 51   ASP A CG    
414  O  OD1   . ASP A 51  ? 0.3255 0.2306 0.6165 0.0071  -0.0407 -0.0318 51   ASP A OD1   
415  O  OD2   . ASP A 51  ? 0.3398 0.2431 0.6337 0.0039  -0.0452 -0.032  51   ASP A OD2   
416  N  N     . TYR A 52  ? 0.1597 0.0837 0.4643 0.006   -0.0346 -0.0292 52   TYR A N     
417  C  CA    . TYR A 52  ? 0.1598 0.0931 0.4685 0.0075  -0.0301 -0.0297 52   TYR A CA    
418  C  C     . TYR A 52  ? 0.1543 0.0881 0.4608 0.0095  -0.0281 -0.0316 52   TYR A C     
419  O  O     . TYR A 52  ? 0.1585 0.0843 0.458  0.011   -0.0293 -0.0325 52   TYR A O     
420  C  CB    . TYR A 52  ? 0.1646 0.0985 0.4707 0.0097  -0.0276 -0.0293 52   TYR A CB    
421  C  CG    . TYR A 52  ? 0.1876 0.1258 0.4987 0.008   -0.0278 -0.0273 52   TYR A CG    
422  C  CD1   . TYR A 52  ? 0.205  0.1539 0.5236 0.0076  -0.0251 -0.0268 52   TYR A CD1   
423  C  CD2   . TYR A 52  ? 0.2135 0.1448 0.5217 0.0071  -0.0307 -0.0259 52   TYR A CD2   
424  C  CE1   . TYR A 52  ? 0.2227 0.1757 0.5456 0.0065  -0.025  -0.0248 52   TYR A CE1   
425  C  CE2   . TYR A 52  ? 0.2305 0.1659 0.5436 0.0058  -0.0307 -0.0238 52   TYR A CE2   
426  C  CZ    . TYR A 52  ? 0.2435 0.19   0.5639 0.0056  -0.0277 -0.0232 52   TYR A CZ    
427  O  OH    . TYR A 52  ? 0.2707 0.2213 0.5957 0.0046  -0.0277 -0.0209 52   TYR A OH    
428  N  N     . PHE A 53  ? 0.1422 0.0852 0.4547 0.0097  -0.0251 -0.0321 53   PHE A N     
429  C  CA    . PHE A 53  ? 0.1556 0.1007 0.4677 0.0114  -0.0229 -0.0337 53   PHE A CA    
430  C  C     . PHE A 53  ? 0.1493 0.1024 0.4647 0.013   -0.0188 -0.0341 53   PHE A C     
431  O  O     . PHE A 53  ? 0.1597 0.1196 0.4806 0.0119  -0.0179 -0.0334 53   PHE A O     
432  C  CB    . PHE A 53  ? 0.1631 0.1111 0.4802 0.0094  -0.0241 -0.0341 53   PHE A CB    
433  C  CG    . PHE A 53  ? 0.1943 0.1344 0.5079 0.0079  -0.0282 -0.0338 53   PHE A CG    
434  C  CD1   . PHE A 53  ? 0.2144 0.1469 0.5211 0.0097  -0.029  -0.0347 53   PHE A CD1   
435  C  CD2   . PHE A 53  ? 0.2112 0.1511 0.5283 0.005   -0.0312 -0.0324 53   PHE A CD2   
436  C  CE1   . PHE A 53  ? 0.2302 0.1549 0.533  0.0085  -0.0331 -0.0345 53   PHE A CE1   
437  C  CE2   . PHE A 53  ? 0.2225 0.1546 0.5361 0.0036  -0.0353 -0.032  53   PHE A CE2   
438  C  CZ    . PHE A 53  ? 0.2246 0.1492 0.5311 0.0053  -0.0363 -0.0333 53   PHE A CZ    
439  N  N     . HIS A 54  ? 0.1261 0.0786 0.4383 0.0156  -0.0165 -0.035  54   HIS A N     
440  C  CA    . HIS A 54  ? 0.1112 0.0708 0.4263 0.0172  -0.0128 -0.0354 54   HIS A CA    
441  C  C     . HIS A 54  ? 0.0969 0.0591 0.4139 0.018   -0.0114 -0.0366 54   HIS A C     
442  O  O     . HIS A 54  ? 0.0995 0.0561 0.4113 0.0199  -0.0114 -0.0369 54   HIS A O     
443  C  CB    . HIS A 54  ? 0.1274 0.0828 0.4359 0.0201  -0.0113 -0.0349 54   HIS A CB    
444  C  CG    . HIS A 54  ? 0.1494 0.1119 0.4604 0.0217  -0.0077 -0.0351 54   HIS A CG    
445  N  ND1   . HIS A 54  ? 0.1739 0.1337 0.4796 0.0245  -0.0058 -0.0345 54   HIS A ND1   
446  C  CD2   . HIS A 54  ? 0.1596 0.1315 0.4779 0.021   -0.0058 -0.0357 54   HIS A CD2   
447  C  CE1   . HIS A 54  ? 0.1782 0.1459 0.4882 0.0253  -0.0029 -0.0347 54   HIS A CE1   
448  N  NE2   . HIS A 54  ? 0.1675 0.1426 0.4851 0.0232  -0.0029 -0.0355 54   HIS A NE2   
449  N  N     . TRP A 55  ? 0.0721 0.0486 0.3958 0.0138  -0.0107 -0.0366 55   TRP A N     
450  C  CA    . TRP A 55  ? 0.0819 0.0555 0.4096 0.0171  -0.0092 -0.0383 55   TRP A CA    
451  C  C     . TRP A 55  ? 0.0819 0.0636 0.4144 0.018   -0.0062 -0.039  55   TRP A C     
452  O  O     . TRP A 55  ? 0.0878 0.0751 0.424  0.0172  -0.0055 -0.0389 55   TRP A O     
453  C  CB    . TRP A 55  ? 0.0662 0.0484 0.398  0.0114  -0.0113 -0.038  55   TRP A CB    
454  C  CG    . TRP A 55  ? 0.0747 0.0468 0.4035 0.0121  -0.0142 -0.0379 55   TRP A CG    
455  C  CD1   . TRP A 55  ? 0.089  0.0486 0.4104 0.0148  -0.0155 -0.0379 55   TRP A CD1   
456  C  CD2   . TRP A 55  ? 0.071  0.0453 0.4037 0.0095  -0.0165 -0.0377 55   TRP A CD2   
457  N  NE1   . TRP A 55  ? 0.0925 0.0473 0.4126 0.0131  -0.0186 -0.0377 55   TRP A NE1   
458  C  CE2   . TRP A 55  ? 0.0843 0.0451 0.4117 0.0106  -0.0192 -0.0377 55   TRP A CE2   
459  C  CE3   . TRP A 55  ? 0.0642 0.045  0.4045 0.0077  -0.0164 -0.0378 55   TRP A CE3   
460  C  CZ2   . TRP A 55  ? 0.0874 0.0468 0.4167 0.0084  -0.0219 -0.0374 55   TRP A CZ2   
461  C  CZ3   . TRP A 55  ? 0.078  0.0531 0.4205 0.0067  -0.0187 -0.0378 55   TRP A CZ3   
462  C  CH2   . TRP A 55  ? 0.087  0.0538 0.4241 0.0063  -0.0216 -0.0373 55   TRP A CH2   
463  N  N     . ARG A 56  ? 0.0706 0.0563 0.4018 0.0168  -0.0048 -0.0391 56   ARG A N     
464  C  CA    . ARG A 56  ? 0.0596 0.0549 0.3928 0.0132  -0.0027 -0.0393 56   ARG A CA    
465  C  C     . ARG A 56  ? 0.0675 0.0606 0.4095 0.0191  -0.0018 -0.0413 56   ARG A C     
466  O  O     . ARG A 56  ? 0.0725 0.0602 0.4119 0.0204  -0.0023 -0.0411 56   ARG A O     
467  C  CB    . ARG A 56  ? 0.0595 0.0549 0.3881 0.0144  -0.0005 -0.0385 56   ARG A CB    
468  C  CG    . ARG A 56  ? 0.061  0.0611 0.3976 0.0184  0.0021  -0.0399 56   ARG A CG    
469  C  CD    . ARG A 56  ? 0.062  0.0625 0.3952 0.02    0.0043  -0.039  56   ARG A CD    
470  N  NE    . ARG A 56  ? 0.0808 0.0785 0.4186 0.0273  0.006   -0.0395 56   ARG A NE    
471  C  CZ    . ARG A 56  ? 0.1334 0.1274 0.4661 0.03    0.0075  -0.0382 56   ARG A CZ    
472  N  NH1   . ARG A 56  ? 0.0988 0.0901 0.4263 0.0314  0.0081  -0.0371 56   ARG A NH1   
473  N  NH2   . ARG A 56  ? 0.1359 0.1291 0.4689 0.0315  0.0085  -0.0377 56   ARG A NH2   
474  N  N     . PHE A 57  ? 0.0583 0.0597 0.404  0.0142  -0.0016 -0.0419 57   PHE A N     
475  C  CA    . PHE A 57  ? 0.0618 0.0652 0.4163 0.0179  -0.0008 -0.0435 57   PHE A CA    
476  C  C     . PHE A 57  ? 0.0718 0.081  0.4302 0.0191  0.0015  -0.0442 57   PHE A C     
477  O  O     . PHE A 57  ? 0.0753 0.0899 0.4366 0.0189  0.0022  -0.0448 57   PHE A O     
478  C  CB    . PHE A 57  ? 0.0494 0.0559 0.4032 0.0098  -0.0029 -0.0436 57   PHE A CB    
479  C  CG    . PHE A 57  ? 0.05   0.0531 0.4027 0.0091  -0.0053 -0.0427 57   PHE A CG    
480  C  CD1   . PHE A 57  ? 0.0506 0.0514 0.4035 0.0086  -0.0065 -0.0427 57   PHE A CD1   
481  C  CD2   . PHE A 57  ? 0.0569 0.0574 0.4117 0.013   -0.0061 -0.0423 57   PHE A CD2   
482  C  CE1   . PHE A 57  ? 0.056  0.051  0.4088 0.0103  -0.0087 -0.0421 57   PHE A CE1   
483  C  CE2   . PHE A 57  ? 0.0677 0.063  0.42   0.0116  -0.0087 -0.0413 57   PHE A CE2   
484  C  CZ    . PHE A 57  ? 0.061  0.0528 0.4128 0.0109  -0.01   -0.0414 57   PHE A CZ    
485  N  N     . ASP A 58  ? 0.0678 0.0756 0.426  0.0205  0.0026  -0.044  58   ASP A N     
486  C  CA    . ASP A 58  ? 0.0592 0.0713 0.4189 0.0197  0.0043  -0.0442 58   ASP A CA    
487  C  C     . ASP A 58  ? 0.0658 0.0824 0.4345 0.0205  0.0044  -0.0457 58   ASP A C     
488  O  O     . ASP A 58  ? 0.0709 0.0842 0.4392 0.0201  0.0036  -0.0455 58   ASP A O     
489  C  CB    . ASP A 58  ? 0.0552 0.0627 0.4032 0.0153  0.0049  -0.0418 58   ASP A CB    
490  C  CG    . ASP A 58  ? 0.1033 0.1085 0.4542 0.0258  0.0064  -0.0416 58   ASP A CG    
491  O  OD1   . ASP A 58  ? 0.1038 0.1106 0.4545 0.0248  0.0059  -0.042  58   ASP A OD1   
492  O  OD2   . ASP A 58  ? 0.1226 0.1231 0.4684 0.0281  0.0074  -0.0402 58   ASP A OD2   
493  N  N     . MET A 59  ? 0.061  0.0842 0.4355 0.0197  0.0049  -0.0472 59   MET A N     
494  C  CA    . MET A 59  ? 0.0671 0.0941 0.448  0.0185  0.0045  -0.0486 59   MET A CA    
495  C  C     . MET A 59  ? 0.0756 0.1053 0.4606 0.0195  0.0059  -0.0489 59   MET A C     
496  O  O     . MET A 59  ? 0.0927 0.1251 0.4784 0.0205  0.007   -0.0487 59   MET A O     
497  C  CB    . MET A 59  ? 0.0654 0.0976 0.45   0.0171  0.0038  -0.0502 59   MET A CB    
498  C  CG    . MET A 59  ? 0.1128 0.1426 0.4946 0.0159  0.0023  -0.0497 59   MET A CG    
499  S  SD    . MET A 59  ? 0.2016 0.2377 0.5868 0.0149  0.0019  -0.0509 59   MET A SD    
500  C  CE    . MET A 59  ? 0.2327 0.2672 0.6124 0.0159  0.0024  -0.0494 59   MET A CE    
501  N  N     . PHE A 60  ? 0.073  0.102  0.4611 0.0191  0.0057  -0.049  60   PHE A N     
502  C  CA    . PHE A 60  ? 0.0652 0.0967 0.4581 0.0199  0.0069  -0.049  60   PHE A CA    
503  C  C     . PHE A 60  ? 0.0675 0.1033 0.4675 0.0183  0.0062  -0.051  60   PHE A C     
504  O  O     . PHE A 60  ? 0.0535 0.0878 0.4552 0.0176  0.0057  -0.0511 60   PHE A O     
505  C  CB    . PHE A 60  ? 0.0565 0.0825 0.4458 0.0207  0.0075  -0.0469 60   PHE A CB    
506  C  CG    . PHE A 60  ? 0.0679 0.0907 0.4518 0.0235  0.0086  -0.0449 60   PHE A CG    
507  C  CD1   . PHE A 60  ? 0.0771 0.0958 0.4541 0.0238  0.008   -0.0444 60   PHE A CD1   
508  C  CD2   . PHE A 60  ? 0.0755 0.0992 0.4606 0.0255  0.0103  -0.0434 60   PHE A CD2   
509  C  CE1   . PHE A 60  ? 0.0803 0.0954 0.4513 0.026   0.009   -0.0426 60   PHE A CE1   
510  C  CE2   . PHE A 60  ? 0.0809 0.1011 0.4598 0.0278  0.0115  -0.0413 60   PHE A CE2   
511  C  CZ    . PHE A 60  ? 0.0774 0.0932 0.4491 0.0281  0.0108  -0.041  60   PHE A CZ    
512  N  N     . PRO A 61  ? 0.0818 0.123  0.4859 0.0179  0.0062  -0.0527 61   PRO A N     
513  C  CA    . PRO A 61  ? 0.0816 0.1267 0.492  0.0166  0.0055  -0.0549 61   PRO A CA    
514  C  C     . PRO A 61  ? 0.0809 0.1277 0.4972 0.0168  0.006   -0.0551 61   PRO A C     
515  O  O     . PRO A 61  ? 0.0824 0.1311 0.5003 0.0177  0.0068  -0.0546 61   PRO A O     
516  C  CB    . PRO A 61  ? 0.093  0.1428 0.5045 0.0163  0.0051  -0.0566 61   PRO A CB    
517  C  CG    . PRO A 61  ? 0.1058 0.1538 0.511  0.0173  0.0056  -0.0551 61   PRO A CG    
518  C  CD    . PRO A 61  ? 0.0811 0.1251 0.4839 0.0186  0.0067  -0.0529 61   PRO A CD    
519  N  N     . GLY A 62  ? 0.0747 0.1213 0.4946 0.0158  0.0055  -0.0558 62   GLY A N     
520  C  CA    . GLY A 62  ? 0.0656 0.1139 0.4918 0.0158  0.0058  -0.0561 62   GLY A CA    
521  C  C     . GLY A 62  ? 0.0773 0.1218 0.5023 0.0168  0.0068  -0.0536 62   GLY A C     
522  O  O     . GLY A 62  ? 0.1062 0.1493 0.5286 0.0183  0.0078  -0.0516 62   GLY A O     
523  N  N     . PHE A 63  ? 0.0683 0.1112 0.4953 0.0161  0.0065  -0.0535 63   PHE A N     
524  C  CA    . PHE A 63  ? 0.0763 0.1158 0.5024 0.0173  0.0075  -0.051  63   PHE A CA    
525  C  C     . PHE A 63  ? 0.0984 0.1402 0.5306 0.018   0.0085  -0.0502 63   PHE A C     
526  O  O     . PHE A 63  ? 0.0896 0.1355 0.5282 0.0171  0.008   -0.0519 63   PHE A O     
527  C  CB    . PHE A 63  ? 0.0676 0.1049 0.494  0.0164  0.0069  -0.0511 63   PHE A CB    
528  C  CG    . PHE A 63  ? 0.0799 0.1137 0.4998 0.0158  0.0059  -0.051  63   PHE A CG    
529  C  CD1   . PHE A 63  ? 0.088  0.1171 0.501  0.0171  0.0062  -0.049  63   PHE A CD1   
530  C  CD2   . PHE A 63  ? 0.0861 0.1212 0.507  0.0141  0.0047  -0.0527 63   PHE A CD2   
531  C  CE1   . PHE A 63  ? 0.1007 0.1263 0.5081 0.0164  0.005   -0.0489 63   PHE A CE1   
532  C  CE2   . PHE A 63  ? 0.0907 0.1227 0.5063 0.0135  0.0037  -0.0523 63   PHE A CE2   
533  C  CZ    . PHE A 63  ? 0.0944 0.1217 0.5035 0.0145  0.0037  -0.0504 63   PHE A CZ    
534  N  N     . ASN A 64  ? 0.1169 0.1561 0.5474 0.0198  0.0098  -0.0474 64   ASN A N     
535  C  CA    . ASN A 64  ? 0.134  0.1753 0.5709 0.0206  0.0108  -0.0459 64   ASN A CA    
536  C  C     . ASN A 64  ? 0.1839 0.2258 0.6265 0.0196  0.0105  -0.0466 64   ASN A C     
537  O  O     . ASN A 64  ? 0.1808 0.2199 0.6206 0.0192  0.0101  -0.0466 64   ASN A O     
538  C  CB    . ASN A 64  ? 0.1075 0.1455 0.5405 0.0231  0.0125  -0.0424 64   ASN A CB    
539  C  CG    . ASN A 64  ? 0.0911 0.1291 0.5204 0.0248  0.0134  -0.0409 64   ASN A CG    
540  O  OD1   . ASN A 64  ? 0.0866 0.1266 0.515  0.024   0.0128  -0.0424 64   ASN A OD1   
541  N  ND2   . ASN A 64  ? 0.0903 0.1262 0.5174 0.0273  0.015   -0.0377 64   ASN A ND2   
542  N  N     . LYS A 65  ? 0.2238 0.269  0.6744 0.0192  0.0106  -0.0467 65   LYS A N     
543  C  CA    . LYS A 65  ? 0.2752 0.3209 0.7318 0.0185  0.0106  -0.0467 65   LYS A CA    
544  C  C     . LYS A 65  ? 0.3239 0.3681 0.7818 0.0206  0.0124  -0.0429 65   LYS A C     
545  O  O     . LYS A 65  ? 0.3293 0.3739 0.7923 0.0204  0.0127  -0.0423 65   LYS A O     
546  C  CB    . LYS A 65  ? 0.299  0.349  0.7641 0.017   0.0096  -0.0491 65   LYS A CB    
547  C  CG    . LYS A 65  ? 0.3498 0.4016 0.8136 0.0155  0.008   -0.0526 65   LYS A CG    
548  C  CD    . LYS A 65  ? 0.4119 0.4618 0.8721 0.0145  0.0073  -0.0541 65   LYS A CD    
549  C  CE    . LYS A 65  ? 0.4548 0.5061 0.9119 0.0136  0.0061  -0.0568 65   LYS A CE    
550  N  NZ    . LYS A 65  ? 0.4693 0.5177 0.918  0.0141  0.0062  -0.0558 65   LYS A NZ    
551  N  N     . ASN A 66  ? 0.3523 0.3949 0.8052 0.0227  0.0137  -0.0403 66   ASN A N     
552  C  CA    . ASN A 66  ? 0.3781 0.4192 0.8308 0.0253  0.0156  -0.0364 66   ASN A CA    
553  C  C     . ASN A 66  ? 0.3837 0.4215 0.8273 0.0277  0.0165  -0.0344 66   ASN A C     
554  O  O     . ASN A 66  ? 0.393  0.4288 0.8302 0.027   0.0156  -0.0361 66   ASN A O     
555  C  CB    . ASN A 66  ? 0.4053 0.4503 0.8674 0.0256  0.0163  -0.0347 66   ASN A CB    
556  C  CG    . ASN A 66  ? 0.4697 0.5182 0.9346 0.0252  0.016   -0.0351 66   ASN A CG    
557  O  OD1   . ASN A 66  ? 0.5027 0.5508 0.9636 0.027   0.0171  -0.033  66   ASN A OD1   
558  N  ND2   . ASN A 66  ? 0.4728 0.5248 0.9447 0.023   0.0145  -0.0377 66   ASN A ND2   
559  N  N     . THR A 67  ? 0.3764 0.4133 0.8191 0.0305  0.0184  -0.0307 67   THR A N     
560  C  CA    . THR A 67  ? 0.3757 0.4089 0.8093 0.033   0.0194  -0.0287 67   THR A CA    
561  C  C     . THR A 67  ? 0.3603 0.3953 0.7921 0.0332  0.0195  -0.029  67   THR A C     
562  O  O     . THR A 67  ? 0.3606 0.3921 0.784  0.0344  0.0196  -0.0287 67   THR A O     
563  C  CB    . THR A 67  ? 0.3996 0.4312 0.8323 0.0364  0.0215  -0.0246 67   THR A CB    
564  N  N     . ASN A 68  ? 0.3391 0.3792 0.7787 0.032   0.0193  -0.0294 68   ASN A N     
565  C  CA    . ASN A 68  ? 0.3221 0.3642 0.7602 0.0322  0.0194  -0.0295 68   ASN A CA    
566  C  C     . ASN A 68  ? 0.296  0.3432 0.7414 0.0295  0.0178  -0.0323 68   ASN A C     
567  O  O     . ASN A 68  ? 0.3036 0.3537 0.7509 0.0298  0.0181  -0.0316 68   ASN A O     
568  C  CB    . ASN A 68  ? 0.3374 0.3799 0.775  0.0352  0.0215  -0.0253 68   ASN A CB    
569  N  N     . ASP A 69  ? 0.2695 0.3174 0.7183 0.0271  0.0162  -0.0354 69   ASP A N     
570  C  CA    . ASP A 69  ? 0.251  0.303  0.706  0.0245  0.0144  -0.0387 69   ASP A CA    
571  C  C     . ASP A 69  ? 0.2205 0.2738 0.6714 0.024   0.0136  -0.0408 69   ASP A C     
572  O  O     . ASP A 69  ? 0.2198 0.2769 0.6749 0.0234  0.0131  -0.0414 69   ASP A O     
573  C  CB    . ASP A 69  ? 0.2923 0.3432 0.7486 0.0227  0.0131  -0.0414 69   ASP A CB    
574  C  CG    . ASP A 69  ? 0.3825 0.4366 0.8433 0.0203  0.0112  -0.0453 69   ASP A CG    
575  O  OD1   . ASP A 69  ? 0.4225 0.4804 0.8901 0.0197  0.0106  -0.0457 69   ASP A OD1   
576  O  OD2   . ASP A 69  ? 0.3968 0.4497 0.8544 0.0191  0.0102  -0.0477 69   ASP A OD2   
577  N  N     . ARG A 70  ? 0.1925 0.2425 0.6354 0.024   0.0134  -0.0418 70   ARG A N     
578  C  CA    . ARG A 70  ? 0.1666 0.2175 0.6052 0.0236  0.0127  -0.0434 70   ARG A CA    
579  C  C     . ARG A 70  ? 0.1513 0.1986 0.5816 0.0258  0.0142  -0.0409 70   ARG A C     
580  O  O     . ARG A 70  ? 0.1471 0.1958 0.5768 0.0272  0.0152  -0.0392 70   ARG A O     
581  C  CB    . ARG A 70  ? 0.1579 0.2085 0.5951 0.0216  0.0111  -0.0469 70   ARG A CB    
582  C  CG    . ARG A 70  ? 0.1455 0.1955 0.5762 0.0215  0.0106  -0.048  70   ARG A CG    
583  C  CD    . ARG A 70  ? 0.1285 0.1809 0.5613 0.0195  0.009   -0.0515 70   ARG A CD    
584  N  NE    . ARG A 70  ? 0.1066 0.1589 0.5339 0.0194  0.0085  -0.0526 70   ARG A NE    
585  C  CZ    . ARG A 70  ? 0.0924 0.1477 0.5192 0.0197  0.0085  -0.0532 70   ARG A CZ    
586  N  NH1   . ARG A 70  ? 0.0679 0.1264 0.499  0.0202  0.0088  -0.0527 70   ARG A NH1   
587  N  NH2   . ARG A 70  ? 0.0762 0.1314 0.4983 0.0195  0.0081  -0.0541 70   ARG A NH2   
588  N  N     . TRP A 71  ? 0.1383 0.1806 0.5623 0.0263  0.0143  -0.0405 71   TRP A N     
589  C  CA    . TRP A 71  ? 0.1232 0.1611 0.5388 0.0285  0.0153  -0.0383 71   TRP A CA    
590  C  C     . TRP A 71  ? 0.1286 0.1649 0.5445 0.0311  0.0172  -0.0347 71   TRP A C     
591  O  O     . TRP A 71  ? 0.1224 0.1597 0.5438 0.0309  0.0174  -0.0341 71   TRP A O     
592  C  CB    . TRP A 71  ? 0.1051 0.1382 0.5143 0.0279  0.0143  -0.0395 71   TRP A CB    
593  C  CG    . TRP A 71  ? 0.0914 0.1264 0.5011 0.0254  0.0125  -0.0427 71   TRP A CG    
594  C  CD1   . TRP A 71  ? 0.1032 0.1392 0.5164 0.0233  0.0112  -0.0448 71   TRP A CD1   
595  C  CD2   . TRP A 71  ? 0.0854 0.1218 0.4922 0.025   0.0121  -0.0438 71   TRP A CD2   
596  N  NE1   . TRP A 71  ? 0.1053 0.1432 0.5178 0.0218  0.01    -0.0472 71   TRP A NE1   
597  C  CE2   . TRP A 71  ? 0.0908 0.129  0.4995 0.0228  0.0105  -0.0466 71   TRP A CE2   
598  C  CE3   . TRP A 71  ? 0.0892 0.1255 0.492  0.0265  0.0131  -0.0426 71   TRP A CE3   
599  C  CZ2   . TRP A 71  ? 0.0864 0.1266 0.4933 0.022   0.0099  -0.0481 71   TRP A CZ2   
600  C  CZ3   . TRP A 71  ? 0.0915 0.1297 0.4925 0.0256  0.0124  -0.0442 71   TRP A CZ3   
601  C  CH2   . TRP A 71  ? 0.0906 0.1308 0.4937 0.0235  0.0108  -0.0469 71   TRP A CH2   
602  N  N     . ASN A 72  ? 0.1414 0.1753 0.5513 0.0337  0.0186  -0.0321 72   ASN A N     
603  C  CA    . ASN A 72  ? 0.1545 0.1869 0.5635 0.0368  0.0207  -0.0283 72   ASN A CA    
604  C  C     . ASN A 72  ? 0.1575 0.1853 0.5634 0.0379  0.0209  -0.0273 72   ASN A C     
605  O  O     . ASN A 72  ? 0.1673 0.1952 0.5756 0.0399  0.0223  -0.0245 72   ASN A O     
606  C  CB    . ASN A 72  ? 0.1921 0.223  0.5948 0.0394  0.0222  -0.026  72   ASN A CB    
607  C  CG    . ASN A 72  ? 0.2701 0.3068 0.6783 0.039   0.0227  -0.0255 72   ASN A CG    
608  O  OD1   . ASN A 72  ? 0.3033 0.345  0.7206 0.0373  0.0221  -0.0262 72   ASN A OD1   
609  N  ND2   . ASN A 72  ? 0.2862 0.3224 0.6893 0.0406  0.0236  -0.0243 72   ASN A ND2   
610  N  N     . SER A 73  ? 0.149  0.1731 0.5501 0.0366  0.0193  -0.0295 73   SER A N     
611  C  CA    . SER A 73  ? 0.1398 0.1599 0.5385 0.037   0.0189  -0.0292 73   SER A CA    
612  C  C     . SER A 73  ? 0.1247 0.145  0.5251 0.0337  0.0168  -0.0326 73   SER A C     
613  O  O     . SER A 73  ? 0.1211 0.1432 0.5219 0.0317  0.0156  -0.035  73   SER A O     
614  C  CB    . SER A 73  ? 0.1624 0.176  0.551  0.04    0.0195  -0.0274 73   SER A CB    
615  O  OG    . SER A 73  ? 0.2209 0.232  0.6029 0.0394  0.0185  -0.0288 73   SER A OG    
616  N  N     . ASN A 74  ? 0.1149 0.1339 0.5171 0.0333  0.0164  -0.0326 74   ASN A N     
617  C  CA    . ASN A 74  ? 0.106  0.1256 0.5107 0.0304  0.0146  -0.0353 74   ASN A CA    
618  C  C     . ASN A 74  ? 0.1135 0.1274 0.5101 0.0304  0.0133  -0.0357 74   ASN A C     
619  O  O     . ASN A 74  ? 0.1141 0.1243 0.5076 0.0321  0.0136  -0.0341 74   ASN A O     
620  C  CB    . ASN A 74  ? 0.1144 0.1364 0.5267 0.0299  0.015   -0.0349 74   ASN A CB    
621  C  CG    . ASN A 74  ? 0.1241 0.1483 0.5411 0.0268  0.0134  -0.0378 74   ASN A CG    
622  O  OD1   . ASN A 74  ? 0.1287 0.1526 0.5432 0.025   0.0119  -0.04   74   ASN A OD1   
623  N  ND2   . ASN A 74  ? 0.1244 0.1509 0.5484 0.0262  0.0137  -0.0377 74   ASN A ND2   
624  N  N     . ILE A 75  ? 0.1083 0.1215 0.502  0.0284  0.0116  -0.0379 75   ILE A N     
625  C  CA    . ILE A 75  ? 0.1097 0.1179 0.4968 0.0279  0.01    -0.0384 75   ILE A CA    
626  C  C     . ILE A 75  ? 0.1089 0.1163 0.4985 0.0269  0.0092  -0.0386 75   ILE A C     
627  O  O     . ILE A 75  ? 0.1208 0.1231 0.5046 0.0277  0.0084  -0.038  75   ILE A O     
628  C  CB    . ILE A 75  ? 0.1203 0.1289 0.5054 0.0258  0.0084  -0.0405 75   ILE A CB    
629  C  CG1   . ILE A 75  ? 0.1272 0.1295 0.5042 0.0258  0.0067  -0.0403 75   ILE A CG1   
630  C  CG2   . ILE A 75  ? 0.1357 0.1492 0.5279 0.0229  0.0074  -0.0428 75   ILE A CG2   
631  C  CD1   . ILE A 75  ? 0.143  0.1397 0.5116 0.029   0.0075  -0.0382 75   ILE A CD1   
632  N  N     . LEU A 76  ? 0.0954 0.1077 0.4934 0.0255  0.0095  -0.0396 76   LEU A N     
633  C  CA    . LEU A 76  ? 0.0941 0.1063 0.4954 0.0244  0.009   -0.0398 76   LEU A CA    
634  C  C     . LEU A 76  ? 0.1042 0.1133 0.5034 0.027   0.0101  -0.0373 76   LEU A C     
635  O  O     . LEU A 76  ? 0.1036 0.1111 0.5029 0.0265  0.0095  -0.0372 76   LEU A O     
636  C  CB    . LEU A 76  ? 0.0963 0.1143 0.5072 0.0226  0.0093  -0.0412 76   LEU A CB    
637  C  CG    . LEU A 76  ? 0.1218 0.1431 0.5348 0.0203  0.0081  -0.0439 76   LEU A CG    
638  C  CD1   . LEU A 76  ? 0.1282 0.1548 0.5502 0.019   0.0084  -0.0454 76   LEU A CD1   
639  C  CD2   . LEU A 76  ? 0.1224 0.1414 0.5317 0.0186  0.0063  -0.0449 76   LEU A CD2   
640  N  N     . ASP A 77  ? 0.1129 0.1214 0.5105 0.0298  0.0119  -0.0351 77   ASP A N     
641  C  CA    . ASP A 77  ? 0.1231 0.1286 0.5179 0.0328  0.0132  -0.0324 77   ASP A CA    
642  C  C     . ASP A 77  ? 0.1183 0.1173 0.5039 0.0337  0.0118  -0.0323 77   ASP A C     
643  O  O     . ASP A 77  ? 0.1122 0.1087 0.4959 0.0355  0.0121  -0.0307 77   ASP A O     
644  C  CB    . ASP A 77  ? 0.1691 0.1749 0.5626 0.0359  0.0153  -0.03   77   ASP A CB    
645  C  CG    . ASP A 77  ? 0.2816 0.2934 0.6845 0.0358  0.0169  -0.0292 77   ASP A CG    
646  O  OD1   . ASP A 77  ? 0.3015 0.3171 0.7122 0.0334  0.0163  -0.0307 77   ASP A OD1   
647  O  OD2   . ASP A 77  ? 0.3261 0.3388 0.7288 0.0382  0.0186  -0.0269 77   ASP A OD2   
648  N  N     . LEU A 78  ? 0.1155 0.1117 0.4954 0.0325  0.01    -0.0338 78   LEU A N     
649  C  CA    . LEU A 78  ? 0.1241 0.114  0.4956 0.0329  0.0082  -0.0338 78   LEU A CA    
650  C  C     . LEU A 78  ? 0.1227 0.1125 0.4968 0.0309  0.0067  -0.0347 78   LEU A C     
651  O  O     . LEU A 78  ? 0.134  0.119  0.5026 0.032   0.0057  -0.034  78   LEU A O     
652  C  CB    . LEU A 78  ? 0.1255 0.1125 0.4911 0.0319  0.0065  -0.0351 78   LEU A CB    
653  C  CG    . LEU A 78  ? 0.1485 0.1336 0.5089 0.0345  0.0077  -0.034  78   LEU A CG    
654  C  CD1   . LEU A 78  ? 0.153  0.1351 0.5078 0.0332  0.006   -0.0353 78   LEU A CD1   
655  C  CD2   . LEU A 78  ? 0.1602 0.1404 0.5142 0.0385  0.0088  -0.0316 78   LEU A CD2   
656  N  N     . LEU A 79  ? 0.1069 0.1021 0.4893 0.0281  0.0067  -0.0361 79   LEU A N     
657  C  CA    . LEU A 79  ? 0.1079 0.1037 0.4935 0.0262  0.0056  -0.0368 79   LEU A CA    
658  C  C     . LEU A 79  ? 0.117  0.1139 0.5062 0.0281  0.0073  -0.035  79   LEU A C     
659  O  O     . LEU A 79  ? 0.1124 0.1064 0.4992 0.0286  0.0066  -0.0342 79   LEU A O     
660  C  CB    . LEU A 79  ? 0.1002 0.1014 0.493  0.023   0.005   -0.0389 79   LEU A CB    
661  C  CG    . LEU A 79  ? 0.1122 0.1133 0.5025 0.0211  0.0035  -0.0405 79   LEU A CG    
662  C  CD1   . LEU A 79  ? 0.1111 0.1179 0.5087 0.0185  0.0033  -0.0424 79   LEU A CD1   
663  C  CD2   . LEU A 79  ? 0.1215 0.1174 0.5048 0.0204  0.0012  -0.0405 79   LEU A CD2   
664  N  N     . SER A 80  ? 0.1197 0.1205 0.5147 0.0292  0.0095  -0.0341 80   SER A N     
665  C  CA    . SER A 80  ? 0.1343 0.1364 0.5334 0.0312  0.0113  -0.032  80   SER A CA    
666  C  C     . SER A 80  ? 0.1395 0.1364 0.5308 0.0347  0.0117  -0.0297 80   SER A C     
667  O  O     . SER A 80  ? 0.1465 0.1429 0.539  0.0359  0.0123  -0.0283 80   SER A O     
668  C  CB    . SER A 80  ? 0.1591 0.1658 0.5649 0.032   0.0134  -0.031  80   SER A CB    
669  O  OG    . SER A 80  ? 0.2021 0.2128 0.6126 0.0295  0.0129  -0.0332 80   SER A OG    
670  N  N     . GLN A 81  ? 0.1265 0.1193 0.5097 0.0364  0.0114  -0.0293 81   GLN A N     
671  C  CA    . GLN A 81  ? 0.1443 0.1314 0.5188 0.0401  0.0116  -0.0274 81   GLN A CA    
672  C  C     . GLN A 81  ? 0.1598 0.1422 0.5288 0.0395  0.0093  -0.0281 81   GLN A C     
673  O  O     . GLN A 81  ? 0.1703 0.1485 0.5334 0.0425  0.0094  -0.0265 81   GLN A O     
674  C  CB    . GLN A 81  ? 0.1616 0.145  0.5283 0.0417  0.0115  -0.0272 81   GLN A CB    
675  C  CG    . GLN A 81  ? 0.1915 0.1782 0.5613 0.0437  0.014   -0.0256 81   GLN A CG    
676  C  CD    . GLN A 81  ? 0.2243 0.2077 0.5867 0.0451  0.0139  -0.0256 81   GLN A CD    
677  O  OE1   . GLN A 81  ? 0.2222 0.1992 0.575  0.0469  0.0127  -0.0254 81   GLN A OE1   
678  N  NE2   . GLN A 81  ? 0.2204 0.208  0.5869 0.0445  0.015   -0.0256 81   GLN A NE2   
679  N  N     . LYS A 82  ? 0.1564 0.1393 0.5269 0.0357  0.007   -0.0304 82   LYS A N     
680  C  CA    . LYS A 82  ? 0.1605 0.1394 0.5267 0.0346  0.0046  -0.0311 82   LYS A CA    
681  C  C     . LYS A 82  ? 0.1536 0.1364 0.5272 0.0326  0.0045  -0.0313 82   LYS A C     
682  O  O     . LYS A 82  ? 0.1708 0.1513 0.5422 0.031   0.0023  -0.032  82   LYS A O     
683  C  CB    . LYS A 82  ? 0.195  0.1711 0.5566 0.0322  0.0018  -0.033  82   LYS A CB    
684  C  CG    . LYS A 82  ? 0.2449 0.2155 0.5973 0.0345  0.0014  -0.0326 82   LYS A CG    
685  C  CD    . LYS A 82  ? 0.3168 0.2811 0.6609 0.0379  0.0008  -0.0312 82   LYS A CD    
686  C  CE    . LYS A 82  ? 0.3945 0.3526 0.7288 0.0402  0       -0.0311 82   LYS A CE    
687  N  NZ    . LYS A 82  ? 0.4467 0.4013 0.7771 0.0373  -0.0033 -0.0329 82   LYS A NZ    
688  N  N     . GLY A 83  ? 0.1296 0.1177 0.5116 0.0328  0.0069  -0.0306 83   GLY A N     
689  C  CA    . GLY A 83  ? 0.1173 0.1088 0.5062 0.0312  0.0071  -0.0307 83   GLY A CA    
690  C  C     . GLY A 83  ? 0.1076 0.1046 0.505  0.0277  0.007   -0.0325 83   GLY A C     
691  O  O     . GLY A 83  ? 0.0969 0.0963 0.4997 0.0263  0.0071  -0.0327 83   GLY A O     
692  N  N     . SER A 84  ? 0.1065 0.1054 0.5051 0.0265  0.0069  -0.034  84   SER A N     
693  C  CA    . SER A 84  ? 0.11   0.114  0.5165 0.0236  0.0069  -0.0358 84   SER A CA    
694  C  C     . SER A 84  ? 0.125  0.1336 0.5397 0.0245  0.0093  -0.035  84   SER A C     
695  O  O     . SER A 84  ? 0.1273 0.1382 0.5444 0.0248  0.0102  -0.0353 84   SER A O     
696  C  CB    . SER A 84  ? 0.1    0.1047 0.5048 0.022   0.0059  -0.0377 84   SER A CB    
697  O  OG    . SER A 84  ? 0.0873 0.0967 0.4991 0.0194  0.0056  -0.0395 84   SER A OG    
698  N  N     . PHE A 85  ? 0.1323 0.1422 0.5515 0.0249  0.0102  -0.0339 85   PHE A N     
699  C  CA    . PHE A 85  ? 0.1392 0.153  0.5664 0.0259  0.0124  -0.0327 85   PHE A CA    
700  C  C     . PHE A 85  ? 0.1494 0.1681 0.5854 0.0233  0.0124  -0.0347 85   PHE A C     
701  O  O     . PHE A 85  ? 0.1446 0.1665 0.5876 0.0239  0.0139  -0.0339 85   PHE A O     
702  C  CB    . PHE A 85  ? 0.1372 0.1503 0.5656 0.0279  0.0136  -0.0303 85   PHE A CB    
703  C  CG    . PHE A 85  ? 0.1348 0.1472 0.5634 0.0262  0.0124  -0.0309 85   PHE A CG    
704  C  CD1   . PHE A 85  ? 0.1301 0.1464 0.5664 0.0238  0.0124  -0.0323 85   PHE A CD1   
705  C  CD2   . PHE A 85  ? 0.1424 0.1504 0.5635 0.0272  0.0113  -0.0301 85   PHE A CD2   
706  C  CE1   . PHE A 85  ? 0.1349 0.1509 0.5715 0.0223  0.0113  -0.0328 85   PHE A CE1   
707  C  CE2   . PHE A 85  ? 0.1493 0.1571 0.571  0.0256  0.0101  -0.0305 85   PHE A CE2   
708  C  CZ    . PHE A 85  ? 0.1412 0.1531 0.5707 0.0232  0.0103  -0.0317 85   PHE A CZ    
709  N  N     . LEU A 86  ? 0.161  0.1804 0.597  0.0206  0.0107  -0.0371 86   LEU A N     
710  C  CA    . LEU A 86  ? 0.1814 0.2052 0.6251 0.0185  0.0107  -0.0392 86   LEU A CA    
711  C  C     . LEU A 86  ? 0.2281 0.2534 0.6716 0.0183  0.0104  -0.0405 86   LEU A C     
712  O  O     . LEU A 86  ? 0.2297 0.2524 0.6664 0.019   0.0099  -0.0403 86   LEU A O     
713  C  CB    . LEU A 86  ? 0.1718 0.1963 0.6164 0.0161  0.0093  -0.0409 86   LEU A CB    
714  C  CG    . LEU A 86  ? 0.1748 0.1984 0.6205 0.0162  0.0094  -0.0397 86   LEU A CG    
715  C  CD1   . LEU A 86  ? 0.1678 0.1926 0.6148 0.0137  0.0081  -0.0413 86   LEU A CD1   
716  C  CD2   . LEU A 86  ? 0.1749 0.2008 0.6278 0.0173  0.0114  -0.0383 86   LEU A CD2   
717  N  N     . TYR A 87  ? 0.2651 0.2944 0.7159 0.0174  0.0109  -0.0418 87   TYR A N     
718  C  CA    . TYR A 87  ? 0.3128 0.3438 0.7639 0.0171  0.0106  -0.0431 87   TYR A CA    
719  C  C     . TYR A 87  ? 0.3269 0.3584 0.7757 0.0151  0.009   -0.0457 87   TYR A C     
720  O  O     . TYR A 87  ? 0.3313 0.3657 0.7852 0.0136  0.0085  -0.0477 87   TYR A O     
721  C  CB    . TYR A 87  ? 0.3299 0.365  0.7901 0.0169  0.0114  -0.0435 87   TYR A CB    
722  C  CG    . TYR A 87  ? 0.3667 0.4038 0.8278 0.017   0.0113  -0.0445 87   TYR A CG    
723  C  CD1   . TYR A 87  ? 0.3937 0.4293 0.85   0.0187  0.0119  -0.0427 87   TYR A CD1   
724  C  CD2   . TYR A 87  ? 0.3872 0.4279 0.8544 0.0155  0.0105  -0.0469 87   TYR A CD2   
725  C  CE1   . TYR A 87  ? 0.4103 0.448  0.8677 0.0188  0.0119  -0.0433 87   TYR A CE1   
726  C  CE2   . TYR A 87  ? 0.403  0.4458 0.8713 0.0155  0.0103  -0.0477 87   TYR A CE2   
727  C  CZ    . TYR A 87  ? 0.4218 0.4633 0.8854 0.0171  0.011   -0.0459 87   TYR A CZ    
728  O  OH    . TYR A 87  ? 0.446  0.4898 0.9108 0.0172  0.0108  -0.0465 87   TYR A OH    
729  N  N     . GLU A 88  ? 0.3239 0.3521 0.7647 0.0152  0.008   -0.0454 88   GLU A N     
730  C  CA    . GLU A 88  ? 0.3075 0.336  0.7458 0.0134  0.0064  -0.0473 88   GLU A CA    
731  C  C     . GLU A 88  ? 0.2901 0.3172 0.7225 0.0136  0.0058  -0.0476 88   GLU A C     
732  O  O     . GLU A 88  ? 0.3085 0.3321 0.7352 0.0151  0.006   -0.046  88   GLU A O     
733  C  CB    . GLU A 88  ? 0.3203 0.3464 0.756  0.0126  0.0055  -0.0467 88   GLU A CB    
734  C  CG    . GLU A 88  ? 0.3525 0.3801 0.7941 0.0122  0.0062  -0.0464 88   GLU A CG    
735  C  CD    . GLU A 88  ? 0.4293 0.4611 0.8778 0.0107  0.0061  -0.0486 88   GLU A CD    
736  O  OE1   . GLU A 88  ? 0.447  0.4809 0.8959 0.0101  0.0056  -0.0504 88   GLU A OE1   
737  O  OE2   . GLU A 88  ? 0.4565 0.4894 0.9097 0.0104  0.0066  -0.0484 88   GLU A OE2   
738  N  N     . THR A 89  ? 0.2598 0.2897 0.6936 0.0123  0.0051  -0.0497 89   THR A N     
739  C  CA    . THR A 89  ? 0.2395 0.2689 0.6684 0.0125  0.0045  -0.0501 89   THR A CA    
740  C  C     . THR A 89  ? 0.1982 0.2277 0.6246 0.0109  0.003   -0.0511 89   THR A C     
741  O  O     . THR A 89  ? 0.1916 0.2244 0.6222 0.0097  0.0026  -0.0528 89   THR A O     
742  C  CB    . THR A 89  ? 0.2625 0.2957 0.6955 0.0128  0.0052  -0.0513 89   THR A CB    
743  O  OG1   . THR A 89  ? 0.286  0.3194 0.7224 0.0142  0.0065  -0.05   89   THR A OG1   
744  C  CG2   . THR A 89  ? 0.2678 0.3005 0.6959 0.0133  0.005   -0.0515 89   THR A CG2   
745  N  N     . PRO A 90  ? 0.1685 0.1944 0.5881 0.011   0.0021  -0.0502 90   PRO A N     
746  C  CA    . PRO A 90  ? 0.1466 0.1731 0.5643 0.0095  0.0007  -0.0509 90   PRO A CA    
747  C  C     . PRO A 90  ? 0.1203 0.1503 0.5389 0.0094  0.0008  -0.0524 90   PRO A C     
748  O  O     . PRO A 90  ? 0.1188 0.1506 0.5394 0.0104  0.0018  -0.053  90   PRO A O     
749  C  CB    . PRO A 90  ? 0.161  0.182  0.5712 0.0098  -0.0004 -0.0492 90   PRO A CB    
750  C  CG    . PRO A 90  ? 0.1756 0.194  0.583  0.0118  0.0007  -0.0481 90   PRO A CG    
751  C  CD    . PRO A 90  ? 0.1615 0.1828 0.5749 0.0126  0.0024  -0.0484 90   PRO A CD    
752  N  N     . ASP A 91  ? 0.1012 0.1324 0.5185 0.0083  -0.0003 -0.0529 91   ASP A N     
753  C  CA    . ASP A 91  ? 0.0888 0.1234 0.5064 0.0084  -0.0002 -0.0543 91   ASP A CA    
754  C  C     . ASP A 91  ? 0.0936 0.1254 0.5055 0.0094  -0.0001 -0.0533 91   ASP A C     
755  O  O     . ASP A 91  ? 0.0993 0.1333 0.5117 0.0102  0.0007  -0.054  91   ASP A O     
756  C  CB    . ASP A 91  ? 0.083  0.1204 0.5019 0.0072  -0.0011 -0.055  91   ASP A CB    
757  C  CG    . ASP A 91  ? 0.1209 0.1617 0.5458 0.0067  -0.0008 -0.0563 91   ASP A CG    
758  O  OD1   . ASP A 91  ? 0.0961 0.1377 0.5248 0.0072  0       -0.0572 91   ASP A OD1   
759  O  OD2   . ASP A 91  ? 0.1312 0.1737 0.557  0.0058  -0.0015 -0.0564 91   ASP A OD2   
760  N  N     . VAL A 92  ? 0.0835 0.1105 0.4899 0.0092  -0.0011 -0.0516 92   VAL A N     
761  C  CA    . VAL A 92  ? 0.0771 0.1007 0.4774 0.0102  -0.0011 -0.0506 92   VAL A CA    
762  C  C     . VAL A 92  ? 0.0705 0.0881 0.466  0.011   -0.0015 -0.0489 92   VAL A C     
763  O  O     . VAL A 92  ? 0.0767 0.0923 0.4722 0.0101  -0.0025 -0.0483 92   VAL A O     
764  C  CB    . VAL A 92  ? 0.0964 0.1201 0.494  0.0091  -0.0024 -0.0504 92   VAL A CB    
765  C  CG1   . VAL A 92  ? 0.124  0.1428 0.5147 0.0099  -0.0029 -0.049  92   VAL A CG1   
766  C  CG2   . VAL A 92  ? 0.1002 0.1297 0.5013 0.009   -0.0019 -0.0519 92   VAL A CG2   
767  N  N     . ILE A 93  ? 0.0637 0.0782 0.4548 0.0127  -0.0008 -0.048  93   ILE A N     
768  C  CA    . ILE A 93  ? 0.0662 0.0744 0.4511 0.0139  -0.0012 -0.0464 93   ILE A CA    
769  C  C     . ILE A 93  ? 0.0577 0.0629 0.4364 0.0144  -0.0019 -0.0459 93   ILE A C     
770  O  O     . ILE A 93  ? 0.0597 0.067  0.4384 0.0154  -0.0006 -0.0461 93   ILE A O     
771  C  CB    . ILE A 93  ? 0.0771 0.0843 0.4619 0.0162  0.0006  -0.0456 93   ILE A CB    
772  C  CG1   . ILE A 93  ? 0.1033 0.1138 0.495  0.0159  0.0014  -0.0459 93   ILE A CG1   
773  C  CG2   . ILE A 93  ? 0.0768 0.0771 0.4539 0.018   0.0001  -0.0439 93   ILE A CG2   
774  C  CD1   . ILE A 93  ? 0.1382 0.1461 0.5294 0.0152  0.0004  -0.0454 93   ILE A CD1   
775  N  N     . ILE A 94  ? 0.0549 0.056  0.4261 0.0112  -0.0041 -0.0448 94   ILE A N     
776  C  CA    . ILE A 94  ? 0.0599 0.0567 0.4267 0.0139  -0.0046 -0.0444 94   ILE A CA    
777  C  C     . ILE A 94  ? 0.0787 0.0684 0.439  0.0166  -0.0046 -0.0433 94   ILE A C     
778  O  O     . ILE A 94  ? 0.0813 0.0674 0.4398 0.0167  -0.0056 -0.0428 94   ILE A O     
779  C  CB    . ILE A 94  ? 0.0534 0.0512 0.4173 0.009   -0.0072 -0.0438 94   ILE A CB    
780  C  CG1   . ILE A 94  ? 0.0556 0.0574 0.4283 0.0103  -0.0069 -0.0453 94   ILE A CG1   
781  C  CG2   . ILE A 94  ? 0.0681 0.0591 0.4279 0.0129  -0.0077 -0.0437 94   ILE A CG2   
782  C  CD1   . ILE A 94  ? 0.0776 0.0784 0.4498 0.0081  -0.0093 -0.0446 94   ILE A CD1   
783  N  N     . THR A 95  ? 0.0797 0.0677 0.4359 0.0187  -0.0033 -0.0428 95   THR A N     
784  C  CA    . THR A 95  ? 0.0913 0.0729 0.4404 0.0213  -0.0032 -0.0416 95   THR A CA    
785  C  C     . THR A 95  ? 0.1101 0.0865 0.4518 0.022   -0.0042 -0.0411 95   THR A C     
786  O  O     . THR A 95  ? 0.106  0.0848 0.4487 0.0209  -0.0044 -0.0415 95   THR A O     
787  C  CB    . THR A 95  ? 0.0972 0.0809 0.4478 0.0239  -0.0004 -0.0409 95   THR A CB    
788  O  OG1   . THR A 95  ? 0.0885 0.0753 0.4397 0.0245  0.0011  -0.041  95   THR A OG1   
789  C  CG2   . THR A 95  ? 0.0979 0.0869 0.4564 0.0232  0.0007  -0.0413 95   THR A CG2   
790  N  N     . SER A 96  ? 0.1278 0.097  0.462  0.024   -0.005  -0.0402 96   SER A N     
791  C  CA    . SER A 96  ? 0.1502 0.1135 0.4767 0.0252  -0.0059 -0.0397 96   SER A CA    
792  C  C     . SER A 96  ? 0.1698 0.1317 0.4926 0.0289  -0.0033 -0.0386 96   SER A C     
793  O  O     . SER A 96  ? 0.1714 0.1324 0.4938 0.0309  -0.0022 -0.0379 96   SER A O     
794  C  CB    . SER A 96  ? 0.1844 0.1398 0.5046 0.025   -0.0089 -0.0395 96   SER A CB    
795  O  OG    . SER A 96  ? 0.2588 0.2075 0.5707 0.0267  -0.0097 -0.039  96   SER A OG    
796  N  N     . LEU A 97  ? 0.1841 0.146  0.5043 0.03    -0.0023 -0.0382 97   LEU A N     
797  C  CA    . LEU A 97  ? 0.213  0.1734 0.5292 0.0336  0.0002  -0.0369 97   LEU A CA    
798  C  C     . LEU A 97  ? 0.2358 0.1868 0.5415 0.0361  -0.0011 -0.0362 97   LEU A C     
799  O  O     . LEU A 97  ? 0.2326 0.1799 0.5342 0.0353  -0.0028 -0.0365 97   LEU A O     
800  C  CB    . LEU A 97  ? 0.2254 0.1905 0.5439 0.0337  0.002   -0.0368 97   LEU A CB    
801  C  CG    . LEU A 97  ? 0.2504 0.2235 0.5763 0.0339  0.0046  -0.0367 97   LEU A CG    
802  C  CD1   . LEU A 97  ? 0.246  0.2216 0.5712 0.035   0.0064  -0.0361 97   LEU A CD1   
803  C  CD2   . LEU A 97  ? 0.2756 0.2481 0.6012 0.0368  0.0065  -0.0352 97   LEU A CD2   
804  N  N     . ASN A 98  ? 0.2583 0.2054 0.5597 0.0392  -0.0003 -0.0351 98   ASN A N     
805  C  CA    . ASN A 98  ? 0.2953 0.2332 0.5861 0.0421  -0.0013 -0.0344 98   ASN A CA    
806  C  C     . ASN A 98  ? 0.3153 0.2519 0.6028 0.0466  0.0014  -0.0326 98   ASN A C     
807  O  O     . ASN A 98  ? 0.3157 0.2558 0.6078 0.0471  0.0026  -0.032  98   ASN A O     
808  C  CB    . ASN A 98  ? 0.3248 0.2563 0.6116 0.0408  -0.0049 -0.0353 98   ASN A CB    
809  N  N     . ASN A 99  ? 0.328  0.2595 0.6075 0.05    0.0022  -0.0315 99   ASN A N     
810  C  CA    . ASN A 99  ? 0.3381 0.2677 0.6131 0.0548  0.0049  -0.0294 99   ASN A CA    
811  C  C     . ASN A 99  ? 0.3058 0.2441 0.5894 0.0554  0.0083  -0.028  99   ASN A C     
812  O  O     . ASN A 99  ? 0.3072 0.2458 0.5909 0.0581  0.0099  -0.0264 99   ASN A O     
813  C  CB    . ASN A 99  ? 0.3884 0.3104 0.6556 0.0579  0.0037  -0.0289 99   ASN A CB    
814  C  CG    . ASN A 99  ? 0.4619 0.3808 0.729  0.0552  0.0002  -0.0307 99   ASN A CG    
815  O  OD1   . ASN A 99  ? 0.4892 0.4124 0.7628 0.0535  0.0002  -0.0309 99   ASN A OD1   
816  N  ND2   . ASN A 99  ? 0.4842 0.3953 0.744  0.0546  -0.003  -0.0319 99   ASN A ND2   
817  N  N     . GLY A 100 ? 0.2815 0.2267 0.5719 0.053   0.0093  -0.0284 100  GLY A N     
818  C  CA    . GLY A 100 ? 0.2714 0.2247 0.57   0.0532  0.0122  -0.0272 100  GLY A CA    
819  C  C     . GLY A 100 ? 0.255  0.2138 0.5625 0.051   0.0121  -0.0278 100  GLY A C     
820  O  O     . GLY A 100 ? 0.2642 0.2291 0.5784 0.0515  0.0144  -0.0266 100  GLY A O     
821  N  N     . LYS A 101 ? 0.2338 0.1906 0.5418 0.0484  0.0094  -0.0296 101  LYS A N     
822  C  CA    . LYS A 101 ? 0.2104 0.1722 0.5266 0.0462  0.0092  -0.0303 101  LYS A CA    
823  C  C     . LYS A 101 ? 0.18   0.143  0.4997 0.0417  0.0065  -0.0327 101  LYS A C     
824  O  O     . LYS A 101 ? 0.1665 0.1255 0.4815 0.0405  0.0044  -0.0338 101  LYS A O     
825  C  CB    . LYS A 101 ? 0.2497 0.2079 0.563  0.0488  0.0095  -0.0289 101  LYS A CB    
826  C  CG    . LYS A 101 ? 0.3537 0.3042 0.6596 0.0486  0.0065  -0.03   101  LYS A CG    
827  C  CD    . LYS A 101 ? 0.4542 0.4011 0.7566 0.0517  0.0069  -0.0286 101  LYS A CD    
828  C  CE    . LYS A 101 ? 0.5301 0.4712 0.828  0.0505  0.0036  -0.0299 101  LYS A CE    
829  N  NZ    . LYS A 101 ? 0.5646 0.5104 0.8707 0.0461  0.0021  -0.0315 101  LYS A NZ    
830  N  N     . GLU A 102 ? 0.1545 0.1231 0.4827 0.0394  0.0065  -0.0335 102  GLU A N     
831  C  CA    . GLU A 102 ? 0.1386 0.1092 0.4709 0.0354  0.0043  -0.0355 102  GLU A CA    
832  C  C     . GLU A 102 ? 0.1438 0.111  0.475  0.0349  0.0025  -0.0357 102  GLU A C     
833  O  O     . GLU A 102 ? 0.1445 0.1116 0.4765 0.0369  0.0037  -0.0346 102  GLU A O     
834  C  CB    . GLU A 102 ? 0.132  0.1111 0.4744 0.0332  0.0054  -0.0365 102  GLU A CB    
835  C  CG    . GLU A 102 ? 0.1568 0.1401 0.5013 0.0338  0.0072  -0.0362 102  GLU A CG    
836  C  CD    . GLU A 102 ? 0.1795 0.1706 0.5334 0.0313  0.0076  -0.0376 102  GLU A CD    
837  O  OE1   . GLU A 102 ? 0.1944 0.187  0.551  0.0284  0.0058  -0.0393 102  GLU A OE1   
838  O  OE2   . GLU A 102 ? 0.1843 0.1801 0.5429 0.0322  0.0095  -0.037  102  GLU A OE2   
839  N  N     . GLU A 103 ? 0.1345 0.0993 0.4642 0.0323  -0.0003 -0.037  103  GLU A N     
840  C  CA    . GLU A 103 ? 0.14   0.1019 0.469  0.0314  -0.0023 -0.0373 103  GLU A CA    
841  C  C     . GLU A 103 ? 0.1387 0.1056 0.475  0.0273  -0.0036 -0.0387 103  GLU A C     
842  O  O     . GLU A 103 ? 0.1476 0.1149 0.4838 0.0253  -0.0049 -0.0395 103  GLU A O     
843  C  CB    . GLU A 103 ? 0.168  0.1212 0.4875 0.0321  -0.005  -0.0372 103  GLU A CB    
844  N  N     . ILE A 104 ? 0.1204 0.091  0.4628 0.0263  -0.0032 -0.0389 104  ILE A N     
845  C  CA    . ILE A 104 ? 0.106  0.0813 0.4551 0.0228  -0.0043 -0.0401 104  ILE A CA    
846  C  C     . ILE A 104 ? 0.1034 0.0745 0.449  0.0207  -0.0075 -0.0404 104  ILE A C     
847  O  O     . ILE A 104 ? 0.1167 0.0821 0.457  0.0216  -0.0091 -0.0398 104  ILE A O     
848  C  CB    . ILE A 104 ? 0.1021 0.0819 0.4584 0.0225  -0.003  -0.0401 104  ILE A CB    
849  C  CG1   . ILE A 104 ? 0.1056 0.0905 0.4668 0.0239  0       -0.0399 104  ILE A CG1   
850  C  CG2   . ILE A 104 ? 0.0985 0.0822 0.4607 0.0191  -0.0043 -0.0413 104  ILE A CG2   
851  C  CD1   . ILE A 104 ? 0.1106 0.0999 0.4791 0.0237  0.0013  -0.0398 104  ILE A CD1   
852  N  N     . LEU A 105 ? 0.0869 0.0607 0.4352 0.0181  -0.0086 -0.0412 105  LEU A N     
853  C  CA    . LEU A 105 ? 0.0915 0.0626 0.4382 0.0157  -0.0117 -0.0413 105  LEU A CA    
854  C  C     . LEU A 105 ? 0.077  0.0528 0.4308 0.0133  -0.0121 -0.0416 105  LEU A C     
855  O  O     . LEU A 105 ? 0.0778 0.0508 0.4305 0.012   -0.0144 -0.0412 105  LEU A O     
856  C  CB    . LEU A 105 ? 0.1036 0.0753 0.4494 0.0145  -0.0125 -0.0415 105  LEU A CB    
857  C  CG    . LEU A 105 ? 0.1284 0.0948 0.4667 0.0167  -0.0123 -0.0411 105  LEU A CG    
858  C  CD1   . LEU A 105 ? 0.1378 0.1057 0.4762 0.0155  -0.0128 -0.0412 105  LEU A CD1   
859  C  CD2   . LEU A 105 ? 0.1436 0.1016 0.4741 0.0178  -0.0146 -0.0405 105  LEU A CD2   
860  N  N     . MET A 106 ? 0.0519 0.047  0.4102 0.0061  -0.0107 -0.0409 106  MET A N     
861  C  CA    . MET A 106 ? 0.0461 0.0466 0.4108 0.0034  -0.0109 -0.0412 106  MET A CA    
862  C  C     . MET A 106 ? 0.0416 0.0462 0.4022 0.001   -0.0084 -0.0412 106  MET A C     
863  O  O     . MET A 106 ? 0.0394 0.044  0.3933 0.0008  -0.007  -0.0411 106  MET A O     
864  C  CB    . MET A 106 ? 0.0447 0.0462 0.4122 0.0026  -0.0129 -0.0413 106  MET A CB    
865  C  CG    . MET A 106 ? 0.0625 0.0555 0.434  0.0075  -0.0116 -0.0434 106  MET A CG    
866  S  SD    . MET A 106 ? 0.0902 0.0833 0.4617 0.0048  -0.0142 -0.0426 106  MET A SD    
867  C  CE    . MET A 106 ? 0.04   0.0434 0.3918 0.0018  -0.0163 -0.0385 106  MET A CE    
868  N  N     . ALA A 107 ? 0.0396 0.0441 0.3976 0.0009  -0.0078 -0.041  107  ALA A N     
869  C  CA    . ALA A 107 ? 0.0434 0.0483 0.4148 0.0007  -0.0062 -0.0435 107  ALA A CA    
870  C  C     . ALA A 107 ? 0.0507 0.0574 0.4387 0.0042  -0.0068 -0.0457 107  ALA A C     
871  O  O     . ALA A 107 ? 0.0469 0.0518 0.4318 0.001   -0.0086 -0.0447 107  ALA A O     
872  C  CB    . ALA A 107 ? 0.0393 0.0441 0.4027 0.0006  -0.0049 -0.042  107  ALA A CB    
873  N  N     . ILE A 108 ? 0.05   0.0632 0.4457 0.007   -0.0056 -0.0472 108  ILE A N     
874  C  CA    . ILE A 108 ? 0.0529 0.0701 0.4524 0.0052  -0.0064 -0.0476 108  ILE A CA    
875  C  C     . ILE A 108 ? 0.0458 0.0687 0.4519 0.0053  -0.0048 -0.0493 108  ILE A C     
876  O  O     . ILE A 108 ? 0.0455 0.0544 0.4358 0.0013  -0.0039 -0.0502 108  ILE A O     
877  C  CB    . ILE A 108 ? 0.0649 0.0824 0.4617 0.0048  -0.0072 -0.0475 108  ILE A CB    
878  C  CG1   . ILE A 108 ? 0.0746 0.0861 0.4649 0.0046  -0.009  -0.0459 108  ILE A CG1   
879  C  CG2   . ILE A 108 ? 0.0709 0.0933 0.4719 0.0033  -0.0077 -0.0477 108  ILE A CG2   
880  C  CD1   . ILE A 108 ? 0.0878 0.0993 0.4753 0.0043  -0.0096 -0.0456 108  ILE A CD1   
881  N  N     . VAL A 109 ? 0.0501 0.0756 0.4603 0.0041  -0.0052 -0.0494 109  VAL A N     
882  C  CA    . VAL A 109 ? 0.0595 0.0903 0.4758 0.0041  -0.004  -0.051  109  VAL A CA    
883  C  C     . VAL A 109 ? 0.0778 0.1121 0.4956 0.0031  -0.0048 -0.0512 109  VAL A C     
884  O  O     . VAL A 109 ? 0.0772 0.1101 0.4937 0.0019  -0.0061 -0.0496 109  VAL A O     
885  C  CB    . VAL A 109 ? 0.0773 0.108  0.4973 0.0041  -0.0034 -0.051  109  VAL A CB    
886  C  CG1   . VAL A 109 ? 0.0851 0.1209 0.5113 0.0039  -0.0026 -0.0527 109  VAL A CG1   
887  C  CG2   . VAL A 109 ? 0.0739 0.1023 0.4933 0.0054  -0.0024 -0.0509 109  VAL A CG2   
888  N  N     . PHE A 110 ? 0.0954 0.1341 0.5159 0.0037  -0.004  -0.0528 110  PHE A N     
889  C  CA    . PHE A 110 ? 0.1263 0.169  0.5486 0.0032  -0.0043 -0.053  110  PHE A CA    
890  C  C     . PHE A 110 ? 0.1611 0.2077 0.5888 0.0034  -0.0035 -0.0546 110  PHE A C     
891  O  O     . PHE A 110 ? 0.1762 0.2242 0.6065 0.0043  -0.0025 -0.0565 110  PHE A O     
892  C  CB    . PHE A 110 ? 0.1322 0.1771 0.5528 0.004   -0.004  -0.0538 110  PHE A CB    
893  C  CG    . PHE A 110 ? 0.1574 0.1988 0.5727 0.0039  -0.0048 -0.0523 110  PHE A CG    
894  C  CD1   . PHE A 110 ? 0.1715 0.212  0.5847 0.0029  -0.0061 -0.0504 110  PHE A CD1   
895  C  CD2   . PHE A 110 ? 0.1789 0.2181 0.5915 0.0049  -0.0042 -0.0528 110  PHE A CD2   
896  C  CE1   . PHE A 110 ? 0.1901 0.227  0.5984 0.0028  -0.007  -0.0491 110  PHE A CE1   
897  C  CE2   . PHE A 110 ? 0.1957 0.2316 0.6032 0.005   -0.0048 -0.0514 110  PHE A CE2   
898  C  CZ    . PHE A 110 ? 0.1938 0.2283 0.5991 0.0039  -0.0063 -0.0497 110  PHE A CZ    
899  N  N     . CYS A 111 ? 0.1781 0.2268 0.6078 0.0027  -0.0039 -0.0538 111  CYS A N     
900  C  CA    . CYS A 111 ? 0.2079 0.2602 0.6424 0.0031  -0.0032 -0.0552 111  CYS A CA    
901  C  C     . CYS A 111 ? 0.2493 0.3057 0.6847 0.0034  -0.0034 -0.055  111  CYS A C     
902  O  O     . CYS A 111 ? 0.2502 0.3062 0.6837 0.0025  -0.0043 -0.0527 111  CYS A O     
903  C  CB    . CYS A 111 ? 0.2278 0.2781 0.6641 0.0023  -0.0033 -0.0542 111  CYS A CB    
904  S  SG    . CYS A 111 ? 0.315  0.3686 0.7573 0.0029  -0.0021 -0.0561 111  CYS A SG    
905  N  N     . SER A 112 ? 0.2801 0.3405 0.7181 0.0046  -0.0026 -0.0573 112  SER A N     
906  C  CA    . SER A 112 ? 0.3133 0.378  0.7519 0.0054  -0.0026 -0.0571 112  SER A CA    
907  C  C     . SER A 112 ? 0.3312 0.3974 0.772  0.005   -0.0026 -0.0554 112  SER A C     
908  O  O     . SER A 112 ? 0.336  0.4054 0.7768 0.0055  -0.0027 -0.0541 112  SER A O     
909  C  CB    . SER A 112 ? 0.3467 0.4149 0.7871 0.0072  -0.0018 -0.0601 112  SER A CB    
910  O  OG    . SER A 112 ? 0.4019 0.4703 0.8459 0.0074  -0.0013 -0.0619 112  SER A OG    
911  N  N     . ALA A 113 ? 0.3305 0.3949 0.7735 0.0043  -0.0025 -0.0553 113  ALA A N     
912  C  CA    . ALA A 113 ? 0.3236 0.3896 0.7689 0.004   -0.0024 -0.0537 113  ALA A CA    
913  C  C     . ALA A 113 ? 0.3119 0.3744 0.7579 0.0026  -0.0026 -0.0524 113  ALA A C     
914  O  O     . ALA A 113 ? 0.319  0.3789 0.7653 0.0025  -0.0023 -0.0538 113  ALA A O     
915  C  CB    . ALA A 113 ? 0.3203 0.3897 0.7689 0.0056  -0.0013 -0.056  113  ALA A CB    
916  N  N     . LEU A 114 ? 0.2909 0.3537 0.7376 0.0016  -0.0031 -0.0498 114  LEU A N     
917  C  CA    . LEU A 114 ? 0.28   0.3401 0.7276 0.0004  -0.0034 -0.0484 114  LEU A CA    
918  C  C     . LEU A 114 ? 0.2601 0.3217 0.7118 0.0014  -0.002  -0.0504 114  LEU A C     
919  O  O     . LEU A 114 ? 0.2644 0.3294 0.7186 0.0022  -0.0013 -0.0503 114  LEU A O     
920  C  CB    . LEU A 114 ? 0.2861 0.347  0.7338 -0.0008 -0.0043 -0.045  114  LEU A CB    
921  C  CG    . LEU A 114 ? 0.3059 0.3635 0.7534 -0.0024 -0.0052 -0.0429 114  LEU A CG    
922  C  CD1   . LEU A 114 ? 0.3071 0.3596 0.7507 -0.0031 -0.0062 -0.043  114  LEU A CD1   
923  C  CD2   . LEU A 114 ? 0.3105 0.3695 0.7585 -0.0036 -0.0064 -0.0393 114  LEU A CD2   
924  N  N     . GLN A 115 ? 0.2346 0.2939 0.6871 0.0016  -0.0015 -0.0522 115  GLN A N     
925  C  CA    . GLN A 115 ? 0.2143 0.2745 0.6708 0.0024  -0.0003 -0.0542 115  GLN A CA    
926  C  C     . GLN A 115 ? 0.1866 0.2465 0.6456 0.0018  0.0001  -0.0525 115  GLN A C     
927  O  O     . GLN A 115 ? 0.1877 0.2455 0.6451 0.0005  -0.0007 -0.0499 115  GLN A O     
928  C  CB    . GLN A 115 ? 0.2481 0.3058 0.7048 0.0027  0       -0.056  115  GLN A CB    
929  C  CG    . GLN A 115 ? 0.3234 0.3821 0.7784 0.0035  -0.0002 -0.0579 115  GLN A CG    
930  C  CD    . GLN A 115 ? 0.3966 0.4526 0.8507 0.0035  -0.0001 -0.0587 115  GLN A CD    
931  O  OE1   . GLN A 115 ? 0.4281 0.4809 0.8815 0.0029  -0.0001 -0.0573 115  GLN A OE1   
932  N  NE2   . GLN A 115 ? 0.4164 0.4736 0.8704 0.0044  0       -0.0609 115  GLN A NE2   
933  N  N     . ALA A 116 ? 0.1643 0.2263 0.6271 0.0027  0.0011  -0.0539 116  ALA A N     
934  C  CA    . ALA A 116 ? 0.1485 0.2108 0.614  0.0023  0.0017  -0.0523 116  ALA A CA    
935  C  C     . ALA A 116 ? 0.126  0.1873 0.5955 0.0028  0.0028  -0.054  116  ALA A C     
936  O  O     . ALA A 116 ? 0.1204 0.181  0.5907 0.0035  0.003   -0.0565 116  ALA A O     
937  C  CB    . ALA A 116 ? 0.1478 0.2138 0.6144 0.0031  0.002   -0.0514 116  ALA A CB    
938  N  N     . GLY A 117 ? 0.1135 0.1744 0.5853 0.0024  0.0034  -0.0525 117  GLY A N     
939  C  CA    . GLY A 117 ? 0.1027 0.1627 0.5786 0.0027  0.0045  -0.0536 117  GLY A CA    
940  C  C     . GLY A 117 ? 0.0936 0.1504 0.5688 0.0023  0.0043  -0.0537 117  GLY A C     
941  O  O     . GLY A 117 ? 0.1004 0.1553 0.5719 0.0014  0.0034  -0.0519 117  GLY A O     
942  N  N     . ASN A 118 ? 0.078  0.1344 0.5568 0.003   0.0051  -0.0557 118  ASN A N     
943  C  CA    . ASN A 118 ? 0.0694 0.1232 0.5481 0.0028  0.0052  -0.0556 118  ASN A CA    
944  C  C     . ASN A 118 ? 0.0699 0.1232 0.5454 0.0031  0.0044  -0.0569 118  ASN A C     
945  O  O     . ASN A 118 ? 0.0754 0.1265 0.5496 0.003   0.0044  -0.0563 118  ASN A O     
946  C  CB    . ASN A 118 ? 0.0559 0.1095 0.5402 0.0034  0.0064  -0.0567 118  ASN A CB    
947  C  CG    . ASN A 118 ? 0.0695 0.1247 0.5576 0.0043  0.0066  -0.0598 118  ASN A CG    
948  O  OD1   . ASN A 118 ? 0.0781 0.1347 0.5645 0.0047  0.0059  -0.0617 118  ASN A OD1   
949  N  ND2   . ASN A 118 ? 0.0744 0.1294 0.5678 0.0046  0.0075  -0.0604 118  ASN A ND2   
950  N  N     . GLN A 119 ? 0.0642 0.1195 0.5382 0.0034  0.0039  -0.0584 119  GLN A N     
951  C  CA    . GLN A 119 ? 0.0755 0.1307 0.5463 0.0036  0.0031  -0.0594 119  GLN A CA    
952  C  C     . GLN A 119 ? 0.0727 0.1257 0.5383 0.0027  0.0023  -0.0568 119  GLN A C     
953  O  O     . GLN A 119 ? 0.0822 0.1337 0.5448 0.0028  0.0018  -0.0569 119  GLN A O     
954  C  CB    . GLN A 119 ? 0.1201 0.1783 0.5905 0.0044  0.0028  -0.0614 119  GLN A CB    
955  C  CG    . GLN A 119 ? 0.2316 0.2899 0.6988 0.0047  0.0021  -0.0624 119  GLN A CG    
956  C  CD    . GLN A 119 ? 0.3561 0.4175 0.8223 0.0057  0.0017  -0.064  119  GLN A CD    
957  O  OE1   . GLN A 119 ? 0.3895 0.4528 0.8554 0.0059  0.0018  -0.0632 119  GLN A OE1   
958  N  NE2   . GLN A 119 ? 0.3867 0.4488 0.8521 0.0064  0.0014  -0.0661 119  GLN A NE2   
959  N  N     . ALA A 120 ? 0.0563 0.109  0.5208 0.0019  0.002   -0.0544 120  ALA A N     
960  C  CA    . ALA A 120 ? 0.0628 0.113  0.5225 0.0009  0.0008  -0.052  120  ALA A CA    
961  C  C     . ALA A 120 ? 0.0701 0.1167 0.5282 0.0009  0.0009  -0.0512 120  ALA A C     
962  O  O     . ALA A 120 ? 0.0851 0.1292 0.5386 0.0006  -0.0001 -0.0501 120  ALA A O     
963  C  CB    . ALA A 120 ? 0.0501 0.101  0.5098 0       0.0003  -0.0496 120  ALA A CB    
964  N  N     . TRP A 121 ? 0.0599 0.1061 0.5218 0.0014  0.002   -0.0514 121  TRP A N     
965  C  CA    . TRP A 121 ? 0.0479 0.0909 0.5084 0.0018  0.0023  -0.0504 121  TRP A CA    
966  C  C     . TRP A 121 ? 0.0415 0.0758 0.4954 0.0021  0.0031  -0.0521 121  TRP A C     
967  O  O     . TRP A 121 ? 0.0414 0.0743 0.495  0.0026  0.0034  -0.0511 121  TRP A O     
968  C  CB    . TRP A 121 ? 0.0433 0.0854 0.5058 0.0016  0.0028  -0.0485 121  TRP A CB    
969  C  CG    . TRP A 121 ? 0.0521 0.0965 0.5209 0.0019  0.0042  -0.0494 121  TRP A CG    
970  C  CD1   . TRP A 121 ? 0.0658 0.1104 0.5389 0.0028  0.0055  -0.0503 121  TRP A CD1   
971  C  CD2   . TRP A 121 ? 0.0567 0.1032 0.5282 0.0014  0.0044  -0.0489 121  TRP A CD2   
972  N  NE1   . TRP A 121 ? 0.0639 0.1105 0.5423 0.0028  0.0064  -0.0508 121  TRP A NE1   
973  C  CE2   . TRP A 121 ? 0.0643 0.1121 0.5416 0.0021  0.0059  -0.05   121  TRP A CE2   
974  C  CE3   . TRP A 121 ? 0.0618 0.1095 0.5317 0.0005  0.0036  -0.0477 121  TRP A CE3   
975  C  CZ2   . TRP A 121 ? 0.0627 0.1125 0.5438 0.002   0.0066  -0.0499 121  TRP A CZ2   
976  C  CZ3   . TRP A 121 ? 0.0651 0.1152 0.5388 0.0004  0.0044  -0.0474 121  TRP A CZ3   
977  C  CH2   . TRP A 121 ? 0.062  0.1131 0.5411 0.0012  0.0059  -0.0486 121  TRP A CH2   
978  N  N     . GLN A 122 ? 0.0402 0.0655 0.4853 0.0013  0.0031  -0.0545 122  GLN A N     
979  C  CA    . GLN A 122 ? 0.0402 0.0646 0.4866 0.0015  0.0036  -0.0561 122  GLN A CA    
980  C  C     . GLN A 122 ? 0.0423 0.0821 0.5029 0.004   0.0039  -0.0553 122  GLN A C     
981  O  O     . GLN A 122 ? 0.0401 0.0625 0.4859 0.002   0.0042  -0.0548 122  GLN A O     
982  C  CB    . GLN A 122 ? 0.0409 0.0725 0.4936 0.0022  0.0034  -0.0589 122  GLN A CB    
983  C  CG    . GLN A 122 ? 0.0898 0.1397 0.5635 0.0049  0.0041  -0.0608 122  GLN A CG    
984  C  CD    . GLN A 122 ? 0.1839 0.2367 0.6607 0.0052  0.0037  -0.0637 122  GLN A CD    
985  O  OE1   . GLN A 122 ? 0.2062 0.2598 0.6882 0.0054  0.0041  -0.0649 122  GLN A OE1   
986  N  NE2   . GLN A 122 ? 0.213  0.2673 0.6865 0.0053  0.003   -0.0647 122  GLN A NE2   
987  N  N     . ARG A 123 ? 0.0489 0.0916 0.5078 0.0042  0.0029  -0.0546 123  ARG A N     
988  C  CA    . ARG A 123 ? 0.0615 0.1016 0.5158 0.0048  0.0027  -0.0537 123  ARG A CA    
989  C  C     . ARG A 123 ? 0.0657 0.102  0.5148 0.0046  0.0021  -0.0513 123  ARG A C     
990  O  O     . ARG A 123 ? 0.058  0.0918 0.502  0.0051  0.0016  -0.0506 123  ARG A O     
991  C  CB    . ARG A 123 ? 0.086  0.1273 0.5375 0.0048  0.002   -0.0551 123  ARG A CB    
992  C  CG    . ARG A 123 ? 0.1359 0.1806 0.5918 0.0051  0.0024  -0.0576 123  ARG A CG    
993  C  CD    . ARG A 123 ? 0.2176 0.262  0.6736 0.006   0.0028  -0.0581 123  ARG A CD    
994  N  NE    . ARG A 123 ? 0.2696 0.3155 0.7231 0.0062  0.0022  -0.0594 123  ARG A NE    
995  C  CZ    . ARG A 123 ? 0.3128 0.3578 0.7635 0.0068  0.0023  -0.0591 123  ARG A CZ    
996  N  NH1   . ARG A 123 ? 0.3128 0.3552 0.7625 0.0075  0.003   -0.0574 123  ARG A NH1   
997  N  NH2   . ARG A 123 ? 0.3317 0.3784 0.7804 0.0069  0.0018  -0.0603 123  ARG A NH2   
998  N  N     . SER A 124 ? 0.0807 0.1165 0.531  0.0042  0.0021  -0.05   124  SER A N     
999  C  CA    . SER A 124 ? 0.1001 0.1322 0.5456 0.0041  0.0013  -0.0478 124  SER A CA    
1000 C  C     . SER A 124 ? 0.104  0.1328 0.5467 0.0056  0.0019  -0.0466 124  SER A C     
1001 O  O     . SER A 124 ? 0.1064 0.1316 0.5436 0.0058  0.0009  -0.0451 124  SER A O     
1002 C  CB    . SER A 124 ? 0.1318 0.1644 0.5799 0.0034  0.0014  -0.0467 124  SER A CB    
1003 O  OG    . SER A 124 ? 0.1802 0.2145 0.6281 0.002   0.0003  -0.0468 124  SER A OG    
1004 N  N     . GLY A 125 ? 0.1027 0.1329 0.5493 0.0067  0.0034  -0.0472 125  GLY A N     
1005 C  CA    . GLY A 125 ? 0.1028 0.1306 0.5474 0.0085  0.0042  -0.0459 125  GLY A CA    
1006 C  C     . GLY A 125 ? 0.0897 0.1148 0.5276 0.009   0.0034  -0.0458 125  GLY A C     
1007 O  O     . GLY A 125 ? 0.0883 0.1099 0.5215 0.0104  0.0034  -0.0442 125  GLY A O     
1008 N  N     . ARG A 126 ? 0.0854 0.1121 0.5225 0.0081  0.0026  -0.0474 126  ARG A N     
1009 C  CA    . ARG A 126 ? 0.0862 0.1105 0.517  0.0084  0.0018  -0.0473 126  ARG A CA    
1010 C  C     . ARG A 126 ? 0.0751 0.095  0.4994 0.0081  0.0002  -0.0458 126  ARG A C     
1011 O  O     . ARG A 126 ? 0.075  0.091  0.4938 0.0094  0       -0.0446 126  ARG A O     
1012 C  CB    . ARG A 126 ? 0.1091 0.1361 0.5403 0.0074  0.0011  -0.0491 126  ARG A CB    
1013 C  CG    . ARG A 126 ? 0.1547 0.1852 0.5899 0.0078  0.0021  -0.0508 126  ARG A CG    
1014 C  CD    . ARG A 126 ? 0.1945 0.2273 0.6287 0.0069  0.0012  -0.0523 126  ARG A CD    
1015 N  NE    . ARG A 126 ? 0.2415 0.276  0.6774 0.0055  0.0004  -0.0527 126  ARG A NE    
1016 C  CZ    . ARG A 126 ? 0.2606 0.2985 0.6983 0.0049  0       -0.0542 126  ARG A CZ    
1017 N  NH1   . ARG A 126 ? 0.2438 0.2839 0.682  0.0055  0.0003  -0.0557 126  ARG A NH1   
1018 N  NH2   . ARG A 126 ? 0.2579 0.2973 0.697  0.0039  -0.0005 -0.054  126  ARG A NH2   
1019 N  N     . ALA A 127 ? 0.0636 0.0843 0.4886 0.0064  -0.0011 -0.0457 127  ALA A N     
1020 C  CA    . ALA A 127 ? 0.0653 0.082  0.4847 0.0057  -0.003  -0.0443 127  ALA A CA    
1021 C  C     . ALA A 127 ? 0.0595 0.0727 0.4766 0.007   -0.0028 -0.0427 127  ALA A C     
1022 O  O     . ALA A 127 ? 0.0488 0.057  0.4585 0.0069  -0.0042 -0.0416 127  ALA A O     
1023 C  CB    . ALA A 127 ? 0.0675 0.0864 0.4892 0.0037  -0.0041 -0.0442 127  ALA A CB    
1024 N  N     . TYR A 128 ? 0.0587 0.074  0.481  0.0076  -0.0012 -0.0425 128  TYR A N     
1025 C  CA    . TYR A 128 ? 0.0709 0.0833 0.4913 0.0091  -0.0008 -0.0408 128  TYR A CA    
1026 C  C     . TYR A 128 ? 0.0753 0.0847 0.4913 0.0116  0       -0.0401 128  TYR A C     
1027 O  O     . TYR A 128 ? 0.0772 0.082  0.487  0.0127  -0.001  -0.0389 128  TYR A O     
1028 C  CB    . TYR A 128 ? 0.0775 0.0931 0.505  0.0093  0.0009  -0.0405 128  TYR A CB    
1029 C  CG    . TYR A 128 ? 0.0932 0.1064 0.5193 0.0115  0.0019  -0.0387 128  TYR A CG    
1030 C  CD1   . TYR A 128 ? 0.1012 0.1109 0.5226 0.0118  0.0006  -0.0372 128  TYR A CD1   
1031 C  CD2   . TYR A 128 ? 0.103  0.1174 0.5321 0.0134  0.004   -0.0383 128  TYR A CD2   
1032 C  CE1   . TYR A 128 ? 0.116  0.1235 0.5355 0.0142  0.0016  -0.0355 128  TYR A CE1   
1033 C  CE2   . TYR A 128 ? 0.111  0.1234 0.5386 0.0158  0.0051  -0.0363 128  TYR A CE2   
1034 C  CZ    . TYR A 128 ? 0.1221 0.131  0.5447 0.0164  0.004   -0.035  128  TYR A CZ    
1035 O  OH    . TYR A 128 ? 0.1215 0.1286 0.5424 0.0191  0.0051  -0.033  128  TYR A OH    
1036 N  N     . SER A 129 ? 0.0701 0.082  0.4896 0.0125  0.0017  -0.0408 129  SER A N     
1037 C  CA    . SER A 129 ? 0.0639 0.074  0.4807 0.0149  0.0029  -0.0399 129  SER A CA    
1038 C  C     . SER A 129 ? 0.0706 0.0768 0.4795 0.0154  0.0016  -0.04   129  SER A C     
1039 O  O     . SER A 129 ? 0.0824 0.0843 0.4854 0.0175  0.0016  -0.0386 129  SER A O     
1040 C  CB    . SER A 129 ? 0.0701 0.0845 0.4936 0.0153  0.0048  -0.0407 129  SER A CB    
1041 O  OG    . SER A 129 ? 0.0784 0.0918 0.501  0.0179  0.0064  -0.0392 129  SER A OG    
1042 N  N     . VAL A 130 ? 0.0703 0.0776 0.4787 0.0137  0.0005  -0.0414 130  VAL A N     
1043 C  CA    . VAL A 130 ? 0.0772 0.0806 0.4781 0.014   -0.0008 -0.0414 130  VAL A CA    
1044 C  C     . VAL A 130 ? 0.0827 0.0813 0.4777 0.0135  -0.0031 -0.0406 130  VAL A C     
1045 O  O     . VAL A 130 ? 0.098  0.0916 0.4858 0.0148  -0.0041 -0.0399 130  VAL A O     
1046 C  CB    . VAL A 130 ? 0.0802 0.0864 0.4824 0.0125  -0.0013 -0.043  130  VAL A CB    
1047 C  CG1   . VAL A 130 ? 0.0961 0.0981 0.4907 0.0128  -0.0027 -0.0428 130  VAL A CG1   
1048 C  CG2   . VAL A 130 ? 0.074  0.0845 0.4815 0.0132  0.0008  -0.0439 130  VAL A CG2   
1049 N  N     . GLY A 131 ? 0.0785 0.0784 0.4765 0.0117  -0.0041 -0.0405 131  GLY A N     
1050 C  CA    . GLY A 131 ? 0.0781 0.0738 0.4712 0.0109  -0.0065 -0.0396 131  GLY A CA    
1051 C  C     . GLY A 131 ? 0.0865 0.0773 0.4743 0.0133  -0.0066 -0.0383 131  GLY A C     
1052 O  O     . GLY A 131 ? 0.0948 0.0804 0.4756 0.0135  -0.0088 -0.0378 131  GLY A O     
1053 N  N     . ARG A 132 ? 0.0903 0.0826 0.481  0.0154  -0.0043 -0.0376 132  ARG A N     
1054 C  CA    . ARG A 132 ? 0.1067 0.0948 0.4924 0.0181  -0.0041 -0.036  132  ARG A CA    
1055 C  C     . ARG A 132 ? 0.1275 0.1114 0.5061 0.0208  -0.0038 -0.0356 132  ARG A C     
1056 O  O     . ARG A 132 ? 0.1493 0.1293 0.5229 0.0235  -0.0036 -0.0343 132  ARG A O     
1057 C  CB    . ARG A 132 ? 0.1062 0.0974 0.4976 0.0194  -0.0018 -0.035  132  ARG A CB    
1058 C  CG    . ARG A 132 ? 0.1028 0.0976 0.4991 0.0209  0.0011  -0.0349 132  ARG A CG    
1059 C  CD    . ARG A 132 ? 0.1188 0.1175 0.5227 0.0214  0.0031  -0.034  132  ARG A CD    
1060 N  NE    . ARG A 132 ? 0.1224 0.1185 0.5235 0.0235  0.0033  -0.0321 132  ARG A NE    
1061 C  CZ    . ARG A 132 ? 0.1352 0.1293 0.5332 0.0269  0.0047  -0.0303 132  ARG A CZ    
1062 N  NH1   . ARG A 132 ? 0.1421 0.134  0.5376 0.0289  0.0049  -0.0287 132  ARG A NH1   
1063 N  NH2   . ARG A 132 ? 0.1099 0.104  0.5069 0.0286  0.0061  -0.0301 132  ARG A NH2   
1064 N  N     . THR A 133 ? 0.1166 0.1009 0.4942 0.0203  -0.0037 -0.0366 133  THR A N     
1065 C  CA    . THR A 133 ? 0.1188 0.0993 0.4899 0.0229  -0.0033 -0.0361 133  THR A CA    
1066 C  C     . THR A 133 ? 0.1241 0.0979 0.486  0.023   -0.0061 -0.0363 133  THR A C     
1067 O  O     . THR A 133 ? 0.1295 0.0989 0.4846 0.0257  -0.0059 -0.0357 133  THR A O     
1068 C  CB    . THR A 133 ? 0.1255 0.1097 0.4998 0.0225  -0.0019 -0.037  133  THR A CB    
1069 O  OG1   . THR A 133 ? 0.1294 0.1145 0.5043 0.0196  -0.0037 -0.0385 133  THR A OG1   
1070 C  CG2   . THR A 133 ? 0.1261 0.1164 0.5092 0.0225  0.0006  -0.037  133  THR A CG2   
1071 N  N     . GLY A 134 ? 0.1171 0.0903 0.4789 0.0201  -0.0087 -0.037  134  GLY A N     
1072 C  CA    . GLY A 134 ? 0.1216 0.0887 0.4756 0.0197  -0.0117 -0.0372 134  GLY A CA    
1073 C  C     . GLY A 134 ? 0.1247 0.0927 0.4786 0.0182  -0.0121 -0.0382 134  GLY A C     
1074 O  O     . GLY A 134 ? 0.1455 0.1087 0.4934 0.0176  -0.0146 -0.0384 134  GLY A O     
1075 N  N     . TYR A 135 ? 0.1015 0.0755 0.4617 0.0176  -0.0098 -0.0388 135  TYR A N     
1076 C  CA    . TYR A 135 ? 0.0959 0.0716 0.4566 0.0162  -0.0101 -0.0397 135  TYR A CA    
1077 C  C     . TYR A 135 ? 0.0803 0.0604 0.447  0.0128  -0.0112 -0.0404 135  TYR A C     
1078 O  O     . TYR A 135 ? 0.0715 0.0564 0.445  0.012   -0.0099 -0.0406 135  TYR A O     
1079 C  CB    . TYR A 135 ? 0.0942 0.074  0.4582 0.0177  -0.0072 -0.0401 135  TYR A CB    
1080 C  CG    . TYR A 135 ? 0.1136 0.0895 0.4719 0.0211  -0.0059 -0.0391 135  TYR A CG    
1081 C  CD1   . TYR A 135 ? 0.1378 0.1076 0.4876 0.0223  -0.0073 -0.0388 135  TYR A CD1   
1082 C  CD2   . TYR A 135 ? 0.1235 0.1017 0.4848 0.0234  -0.0032 -0.0383 135  TYR A CD2   
1083 C  CE1   . TYR A 135 ? 0.1563 0.1225 0.5006 0.0258  -0.0059 -0.0378 135  TYR A CE1   
1084 C  CE2   . TYR A 135 ? 0.1392 0.1142 0.4953 0.0269  -0.0018 -0.037  135  TYR A CE2   
1085 C  CZ    . TYR A 135 ? 0.1646 0.1335 0.5119 0.0282  -0.0032 -0.0368 135  TYR A CZ    
1086 O  OH    . TYR A 135 ? 0.1895 0.1551 0.5313 0.0319  -0.0017 -0.0354 135  TYR A OH    
1087 N  N     . PRO A 136 ? 0.0698 0.0492 0.4342 0.0106  -0.0135 -0.0405 136  PRO A N     
1088 C  CA    . PRO A 136 ? 0.072  0.0548 0.442  0.008   -0.0145 -0.0408 136  PRO A CA    
1089 C  C     . PRO A 136 ? 0.0653 0.0554 0.443  0.0074  -0.0122 -0.0418 136  PRO A C     
1090 O  O     . PRO A 136 ? 0.061  0.0532 0.4395 0.0085  -0.0104 -0.0425 136  PRO A O     
1091 C  CB    . PRO A 136 ? 0.0716 0.0517 0.4378 0.0066  -0.0168 -0.0406 136  PRO A CB    
1092 C  CG    . PRO A 136 ? 0.0782 0.0509 0.436  0.0085  -0.018  -0.0402 136  PRO A CG    
1093 C  CD    . PRO A 136 ? 0.0543 0.0446 0.4095 0.0058  -0.0159 -0.0385 136  PRO A CD    
1094 N  N     . TYR A 137 ? 0.064  0.058  0.4474 0.0056  -0.0123 -0.0418 137  TYR A N     
1095 C  CA    . TYR A 137 ? 0.0678 0.0684 0.4585 0.0051  -0.0103 -0.0429 137  TYR A CA    
1096 C  C     . TYR A 137 ? 0.075  0.0786 0.4686 0.0027  -0.0117 -0.0428 137  TYR A C     
1097 O  O     . TYR A 137 ? 0.0736 0.0767 0.4681 0.0013  -0.0131 -0.0418 137  TYR A O     
1098 C  CB    . TYR A 137 ? 0.0667 0.0693 0.4619 0.0057  -0.0088 -0.0428 137  TYR A CB    
1099 C  CG    . TYR A 137 ? 0.0633 0.0723 0.466  0.0053  -0.007  -0.0441 137  TYR A CG    
1100 C  CD1   . TYR A 137 ? 0.0752 0.0865 0.4802 0.0067  -0.0049 -0.0451 137  TYR A CD1   
1101 C  CD2   . TYR A 137 ? 0.0674 0.0801 0.4748 0.0035  -0.0074 -0.0443 137  TYR A CD2   
1102 C  CE1   . TYR A 137 ? 0.0904 0.1072 0.502  0.0063  -0.0036 -0.0465 137  TYR A CE1   
1103 C  CE2   . TYR A 137 ? 0.0808 0.0989 0.4945 0.0033  -0.0058 -0.0457 137  TYR A CE2   
1104 C  CZ    . TYR A 137 ? 0.1022 0.1222 0.518  0.0047  -0.0041 -0.0469 137  TYR A CZ    
1105 O  OH    . TYR A 137 ? 0.1283 0.1532 0.5502 0.0045  -0.0029 -0.0485 137  TYR A OH    
1106 N  N     . ILE A 138 ? 0.0822 0.0891 0.4773 0.0024  -0.0112 -0.0436 138  ILE A N     
1107 C  CA    . ILE A 138 ? 0.0961 0.106  0.4936 0.0005  -0.0123 -0.0432 138  ILE A CA    
1108 C  C     . ILE A 138 ? 0.1019 0.1185 0.5059 0.0005  -0.0104 -0.0446 138  ILE A C     
1109 O  O     . ILE A 138 ? 0.0927 0.1116 0.4977 0.0016  -0.0089 -0.046  138  ILE A O     
1110 C  CB    . ILE A 138 ? 0.1169 0.1251 0.5103 0.0003  -0.0134 -0.0429 138  ILE A CB    
1111 C  CG1   . ILE A 138 ? 0.1393 0.1403 0.5253 0.0011  -0.0149 -0.0421 138  ILE A CG1   
1112 C  CG2   . ILE A 138 ? 0.1263 0.1372 0.522  -0.0017 -0.0149 -0.0419 138  ILE A CG2   
1113 C  CD1   . ILE A 138 ? 0.1525 0.1492 0.5362 -0.0002 -0.0174 -0.0407 138  ILE A CD1   
1114 N  N     . TYR A 139 ? 0.1105 0.13   0.5189 -0.0007 -0.0107 -0.0442 139  TYR A N     
1115 C  CA    . TYR A 139 ? 0.1259 0.1513 0.5401 -0.0006 -0.0091 -0.0455 139  TYR A CA    
1116 C  C     . TYR A 139 ? 0.1166 0.1452 0.532  -0.0017 -0.01   -0.0448 139  TYR A C     
1117 O  O     . TYR A 139 ? 0.1237 0.1516 0.5391 -0.0031 -0.0115 -0.043  139  TYR A O     
1118 C  CB    . TYR A 139 ? 0.144  0.1705 0.5622 -0.0009 -0.0085 -0.0453 139  TYR A CB    
1119 C  CG    . TYR A 139 ? 0.1798 0.2116 0.6039 -0.0005 -0.0068 -0.0469 139  TYR A CG    
1120 C  CD1   . TYR A 139 ? 0.2065 0.241  0.632  0.0006  -0.0056 -0.0489 139  TYR A CD1   
1121 C  CD2   . TYR A 139 ? 0.2104 0.2442 0.6386 -0.001  -0.0065 -0.0466 139  TYR A CD2   
1122 C  CE1   . TYR A 139 ? 0.226  0.2649 0.6567 0.001   -0.0043 -0.0506 139  TYR A CE1   
1123 C  CE2   . TYR A 139 ? 0.2297 0.2679 0.6631 -0.0005 -0.005  -0.0482 139  TYR A CE2   
1124 C  CZ    . TYR A 139 ? 0.2462 0.2868 0.6808 0.0005  -0.0041 -0.0503 139  TYR A CZ    
1125 O  OH    . TYR A 139 ? 0.2789 0.3235 0.7184 0.0011  -0.0029 -0.0521 139  TYR A OH    
1126 N  N     . ILE A 140 ? 0.1041 0.136  0.5204 -0.0011 -0.0091 -0.046  140  ILE A N     
1127 C  CA    . ILE A 140 ? 0.0997 0.1348 0.5169 -0.0017 -0.0098 -0.0451 140  ILE A CA    
1128 C  C     . ILE A 140 ? 0.1025 0.1435 0.5248 -0.0011 -0.0083 -0.0465 140  ILE A C     
1129 O  O     . ILE A 140 ? 0.0915 0.1345 0.5153 0.0002  -0.0069 -0.0487 140  ILE A O     
1130 C  CB    . ILE A 140 ? 0.1085 0.1426 0.5219 -0.0012 -0.01   -0.0452 140  ILE A CB    
1131 C  CG1   . ILE A 140 ? 0.1201 0.1478 0.528  -0.0017 -0.0116 -0.0439 140  ILE A CG1   
1132 C  CG2   . ILE A 140 ? 0.1203 0.1585 0.5352 -0.0016 -0.0103 -0.0443 140  ILE A CG2   
1133 C  CD1   . ILE A 140 ? 0.1335 0.1595 0.5374 -0.0008 -0.0115 -0.0443 140  ILE A CD1   
1134 N  N     . VAL A 141 ? 0.1049 0.1487 0.53   -0.0019 -0.0087 -0.0452 141  VAL A N     
1135 C  CA    . VAL A 141 ? 0.1143 0.1635 0.5439 -0.001  -0.0074 -0.0464 141  VAL A CA    
1136 C  C     . VAL A 141 ? 0.1233 0.1764 0.5542 -0.0012 -0.0078 -0.0447 141  VAL A C     
1137 O  O     . VAL A 141 ? 0.1136 0.1654 0.5433 -0.0026 -0.0093 -0.042  141  VAL A O     
1138 C  CB    . VAL A 141 ? 0.1242 0.1732 0.5569 -0.0013 -0.0069 -0.0466 141  VAL A CB    
1139 C  CG1   . VAL A 141 ? 0.118  0.1659 0.551  -0.0028 -0.0082 -0.0438 141  VAL A CG1   
1140 C  CG2   . VAL A 141 ? 0.1443 0.198  0.5812 -0.0001 -0.0054 -0.0485 141  VAL A CG2   
1141 N  N     . ASP A 142 ? 0.1304 0.1884 0.5636 0.0002  -0.0066 -0.0463 142  ASP A N     
1142 C  CA    . ASP A 142 ? 0.1389 0.2011 0.5734 0.0005  -0.0066 -0.0445 142  ASP A CA    
1143 C  C     . ASP A 142 ? 0.1282 0.1927 0.5663 0.0003  -0.0064 -0.0433 142  ASP A C     
1144 O  O     . ASP A 142 ? 0.1206 0.1857 0.561  0.0009  -0.0054 -0.0451 142  ASP A O     
1145 C  CB    . ASP A 142 ? 0.1781 0.2447 0.6132 0.0026  -0.0054 -0.0467 142  ASP A CB    
1146 C  CG    . ASP A 142 ? 0.2764 0.3424 0.7083 0.0029  -0.0057 -0.0467 142  ASP A CG    
1147 O  OD1   . ASP A 142 ? 0.2877 0.3492 0.7166 0.0016  -0.0068 -0.0457 142  ASP A OD1   
1148 O  OD2   . ASP A 142 ? 0.3252 0.3953 0.7574 0.0045  -0.0049 -0.0477 142  ASP A OD2   
1149 N  N     . PHE A 143 ? 0.124  0.1896 0.5626 -0.0007 -0.0074 -0.04   143  PHE A N     
1150 C  CA    . PHE A 143 ? 0.1271 0.1953 0.5691 -0.0009 -0.0072 -0.0382 143  PHE A CA    
1151 C  C     . PHE A 143 ? 0.1235 0.197  0.567  0.0002  -0.0068 -0.0364 143  PHE A C     
1152 O  O     . PHE A 143 ? 0.1307 0.2041 0.5731 -0.0007 -0.008  -0.0338 143  PHE A O     
1153 C  CB    . PHE A 143 ? 0.1244 0.189  0.566  -0.0033 -0.0091 -0.0351 143  PHE A CB    
1154 C  CG    . PHE A 143 ? 0.1218 0.1889 0.567  -0.0037 -0.0089 -0.033  143  PHE A CG    
1155 C  CD1   . PHE A 143 ? 0.1209 0.1918 0.5681 -0.0039 -0.0093 -0.0297 143  PHE A CD1   
1156 C  CD2   . PHE A 143 ? 0.134  0.1998 0.5807 -0.0039 -0.0083 -0.034  143  PHE A CD2   
1157 C  CE1   . PHE A 143 ? 0.1295 0.203  0.5801 -0.0041 -0.009  -0.0275 143  PHE A CE1   
1158 C  CE2   . PHE A 143 ? 0.1359 0.2041 0.586  -0.0041 -0.008  -0.0319 143  PHE A CE2   
1159 C  CZ    . PHE A 143 ? 0.129  0.2011 0.5809 -0.0042 -0.0083 -0.0287 143  PHE A CZ    
1160 N  N     . VAL A 144 ? 0.1112 0.1892 0.5571 0.0023  -0.0051 -0.0377 144  VAL A N     
1161 C  CA    . VAL A 144 ? 0.1127 0.1911 0.5602 0.0036  -0.0038 -0.0408 144  VAL A CA    
1162 C  C     . VAL A 144 ? 0.1217 0.2029 0.5686 0.006   -0.0026 -0.0441 144  VAL A C     
1163 O  O     . VAL A 144 ? 0.1174 0.2012 0.5632 0.0069  -0.0026 -0.0433 144  VAL A O     
1164 C  CB    . VAL A 144 ? 0.1144 0.196  0.5655 0.0042  -0.003  -0.0393 144  VAL A CB    
1165 C  CG1   . VAL A 144 ? 0.1234 0.2022 0.5755 0.002   -0.0039 -0.0369 144  VAL A CG1   
1166 C  CG2   . VAL A 144 ? 0.1083 0.1951 0.5604 0.0056  -0.0025 -0.0367 144  VAL A CG2   
1167 N  N     . LYS A 145 ? 0.1349 0.2157 0.5829 0.007   -0.0017 -0.0476 145  LYS A N     
1168 C  CA    . LYS A 145 ? 0.154  0.2374 0.6019 0.0094  -0.0008 -0.0509 145  LYS A CA    
1169 C  C     . LYS A 145 ? 0.1705 0.2555 0.6212 0.0108  0.0002  -0.0526 145  LYS A C     
1170 O  O     . LYS A 145 ? 0.1855 0.2678 0.6379 0.0097  0.0002  -0.053  145  LYS A O     
1171 C  CB    . LYS A 145 ? 0.1872 0.2676 0.6333 0.009   -0.0011 -0.0537 145  LYS A CB    
1172 C  CG    . LYS A 145 ? 0.2485 0.3317 0.6942 0.0113  -0.0005 -0.057  145  LYS A CG    
1173 C  CD    . LYS A 145 ? 0.3148 0.3955 0.7593 0.011   -0.0008 -0.0595 145  LYS A CD    
1174 C  CE    . LYS A 145 ? 0.3666 0.4441 0.8131 0.0102  -0.0007 -0.0614 145  LYS A CE    
1175 N  NZ    . LYS A 145 ? 0.3846 0.464  0.8342 0.0117  -0.0001 -0.0637 145  LYS A NZ    
1176 N  N     . TYR A 146 ? 0.1687 0.258  0.62   0.0133  0.001   -0.0535 146  TYR A N     
1177 C  CA    . TYR A 146 ? 0.1751 0.2656 0.6288 0.0149  0.0019  -0.0552 146  TYR A CA    
1178 C  C     . TYR A 146 ? 0.1962 0.2851 0.6504 0.0157  0.002   -0.0597 146  TYR A C     
1179 O  O     . TYR A 146 ? 0.1921 0.2818 0.6447 0.0167  0.0018  -0.062  146  TYR A O     
1180 C  CB    . TYR A 146 ? 0.1683 0.2638 0.622  0.0177  0.0028  -0.0543 146  TYR A CB    
1181 C  CG    . TYR A 146 ? 0.1741 0.2717 0.6287 0.017   0.003   -0.0494 146  TYR A CG    
1182 C  CD1   . TYR A 146 ? 0.1839 0.283  0.6371 0.0164  0.0024  -0.0464 146  TYR A CD1   
1183 C  CD2   . TYR A 146 ? 0.1787 0.2766 0.6357 0.0169  0.0035  -0.0477 146  TYR A CD2   
1184 C  CE1   . TYR A 146 ? 0.1942 0.2954 0.6487 0.0158  0.0023  -0.0416 146  TYR A CE1   
1185 C  CE2   . TYR A 146 ? 0.1837 0.2838 0.6418 0.0163  0.0036  -0.043  146  TYR A CE2   
1186 C  CZ    . TYR A 146 ? 0.194  0.2956 0.6509 0.0156  0.0029  -0.0399 146  TYR A CZ    
1187 O  OH    . TYR A 146 ? 0.2071 0.3109 0.6656 0.0148  0.0026  -0.035  146  TYR A OH    
1188 N  N     . GLU A 147 ? 0.2126 0.2995 0.6693 0.0153  0.0023  -0.061  147  GLU A N     
1189 C  CA    . GLU A 147 ? 0.2287 0.3144 0.6868 0.0162  0.0023  -0.0652 147  GLU A CA    
1190 C  C     . GLU A 147 ? 0.2489 0.3382 0.7069 0.0194  0.0028  -0.0672 147  GLU A C     
1191 O  O     . GLU A 147 ? 0.2489 0.3409 0.7068 0.0207  0.0036  -0.0652 147  GLU A O     
1192 C  CB    . GLU A 147 ? 0.2351 0.318  0.6964 0.0151  0.0026  -0.0656 147  GLU A CB    
1193 C  CG    . GLU A 147 ? 0.2715 0.3508 0.7329 0.0124  0.0022  -0.0637 147  GLU A CG    
1194 C  CD    . GLU A 147 ? 0.3369 0.4139 0.8015 0.0114  0.0027  -0.0635 147  GLU A CD    
1195 O  OE1   . GLU A 147 ? 0.3683 0.4431 0.8347 0.0111  0.0026  -0.0658 147  GLU A OE1   
1196 O  OE2   . GLU A 147 ? 0.337  0.4147 0.8025 0.0111  0.0031  -0.061  147  GLU A OE2   
1197 N  N     . LEU A 148 ? 0.2611 0.3504 0.7187 0.0207  0.0024  -0.0711 148  LEU A N     
1198 C  CA    . LEU A 148 ? 0.2716 0.364  0.7284 0.024   0.0026  -0.0735 148  LEU A CA    
1199 C  C     . LEU A 148 ? 0.2809 0.3716 0.7397 0.0251  0.0023  -0.0775 148  LEU A C     
1200 O  O     . LEU A 148 ? 0.2846 0.3722 0.7457 0.0234  0.0017  -0.0792 148  LEU A O     
1201 C  CB    . LEU A 148 ? 0.271  0.3654 0.7248 0.0251  0.002   -0.0747 148  LEU A CB    
1202 C  CG    . LEU A 148 ? 0.2692 0.3651 0.7208 0.0241  0.0021  -0.0712 148  LEU A CG    
1203 C  CD1   . LEU A 148 ? 0.2676 0.3652 0.7167 0.0252  0.0016  -0.0729 148  LEU A CD1   
1204 C  CD2   . LEU A 148 ? 0.2715 0.3707 0.7227 0.0254  0.0031  -0.0677 148  LEU A CD2   
1205 N  N     . ASN A 149 ? 0.2829 0.3759 0.741  0.0282  0.0026  -0.0791 149  ASN A N     
1206 C  CA    . ASN A 149 ? 0.2855 0.3772 0.7451 0.0297  0.002   -0.0835 149  ASN A CA    
1207 C  C     . ASN A 149 ? 0.2979 0.3909 0.7551 0.0309  0.0009  -0.0863 149  ASN A C     
1208 O  O     . ASN A 149 ? 0.2997 0.3962 0.7538 0.0332  0.0012  -0.0857 149  ASN A O     
1209 C  CB    . ASN A 149 ? 0.2805 0.3742 0.7396 0.0329  0.0029  -0.0838 149  ASN A CB    
1210 C  CG    . ASN A 149 ? 0.2944 0.3877 0.7553 0.032   0.0042  -0.0803 149  ASN A CG    
1211 O  OD1   . ASN A 149 ? 0.2935 0.3899 0.7532 0.033   0.0053  -0.0769 149  ASN A OD1   
1212 N  ND2   . ASN A 149 ? 0.2959 0.3858 0.7603 0.0301  0.0041  -0.0809 149  ASN A ND2   
1213 N  N     . ASN A 150 ? 0.305  0.3954 0.7637 0.0294  -0.0003 -0.0888 150  ASN A N     
1214 C  CA    . ASN A 150 ? 0.3186 0.4102 0.7754 0.0301  -0.0014 -0.0912 150  ASN A CA    
1215 C  C     . ASN A 150 ? 0.3405 0.4342 0.7953 0.0338  -0.0021 -0.0948 150  ASN A C     
1216 O  O     . ASN A 150 ? 0.3487 0.4449 0.8007 0.0353  -0.0026 -0.0958 150  ASN A O     
1217 C  CB    . ASN A 150 ? 0.3196 0.4082 0.779  0.0277  -0.0025 -0.0928 150  ASN A CB    
1218 C  CG    . ASN A 150 ? 0.3436 0.4305 0.8035 0.0246  -0.0018 -0.0891 150  ASN A CG    
1219 O  OD1   . ASN A 150 ? 0.3454 0.4339 0.8027 0.0242  -0.0012 -0.0862 150  ASN A OD1   
1220 N  ND2   . ASN A 150 ? 0.3535 0.4371 0.817  0.0225  -0.002  -0.089  150  ASN A ND2   
1221 N  N     . SER A 151 ? 0.3503 0.4432 0.8062 0.0355  -0.002  -0.0965 151  SER A N     
1222 C  CA    . SER A 151 ? 0.3643 0.4586 0.818  0.0393  -0.0027 -0.1    151  SER A CA    
1223 C  C     . SER A 151 ? 0.3628 0.4619 0.8122 0.0423  -0.0017 -0.098  151  SER A C     
1224 O  O     . SER A 151 ? 0.3754 0.4765 0.8219 0.0448  -0.0025 -0.1006 151  SER A O     
1225 C  CB    . SER A 151 ? 0.4015 0.4939 0.857  0.0406  -0.0024 -0.1012 151  SER A CB    
1226 O  OG    . SER A 151 ? 0.4445 0.5328 0.9046 0.0377  -0.003  -0.1021 151  SER A OG    
1227 N  N     . ASP A 152 ? 0.3449 0.4458 0.7938 0.0419  0.0001  -0.0934 152  ASP A N     
1228 C  CA    . ASP A 152 ? 0.3389 0.4446 0.7844 0.0447  0.0012  -0.091  152  ASP A CA    
1229 C  C     . ASP A 152 ? 0.3168 0.4244 0.7621 0.0425  0.0022  -0.086  152  ASP A C     
1230 O  O     . ASP A 152 ? 0.3176 0.4292 0.7608 0.0445  0.0033  -0.0831 152  ASP A O     
1231 C  CB    . ASP A 152 ? 0.3714 0.4787 0.8161 0.0479  0.0025  -0.0901 152  ASP A CB    
1232 C  CG    . ASP A 152 ? 0.4474 0.553  0.8952 0.0459  0.0037  -0.087  152  ASP A CG    
1233 O  OD1   . ASP A 152 ? 0.4572 0.56   0.9078 0.042   0.0034  -0.0858 152  ASP A OD1   
1234 O  OD2   . ASP A 152 ? 0.4829 0.59   0.9302 0.0484  0.0049  -0.0857 152  ASP A OD2   
1235 N  N     . ARG A 153 ? 0.2963 0.401  0.7436 0.0385  0.0018  -0.0848 153  ARG A N     
1236 C  CA    . ARG A 153 ? 0.2842 0.3897 0.7312 0.0361  0.0024  -0.0803 153  ARG A CA    
1237 C  C     . ARG A 153 ? 0.2735 0.3807 0.7213 0.0361  0.0038  -0.0758 153  ARG A C     
1238 O  O     . ARG A 153 ? 0.2768 0.386  0.7238 0.0353  0.0043  -0.0719 153  ARG A O     
1239 C  CB    . ARG A 153 ? 0.2887 0.3972 0.7329 0.0371  0.0022  -0.08   153  ARG A CB    
1240 C  CG    . ARG A 153 ? 0.3178 0.4248 0.7616 0.0367  0.0008  -0.084  153  ARG A CG    
1241 C  CD    . ARG A 153 ? 0.3398 0.4479 0.7818 0.0355  0.0007  -0.0824 153  ARG A CD    
1242 N  NE    . ARG A 153 ? 0.3563 0.4604 0.8    0.0318  0.0002  -0.0817 153  ARG A NE    
1243 C  CZ    . ARG A 153 ? 0.3533 0.4566 0.7967 0.0294  0.0006  -0.0781 153  ARG A CZ    
1244 N  NH1   . ARG A 153 ? 0.3328 0.439  0.7746 0.0302  0.0014  -0.0746 153  ARG A NH1   
1245 N  NH2   . ARG A 153 ? 0.3511 0.4505 0.7957 0.0265  0.0001  -0.0779 153  ARG A NH2   
1246 N  N     . SER A 154 ? 0.2609 0.3674 0.7103 0.0371  0.0044  -0.0761 154  SER A N     
1247 C  CA    . SER A 154 ? 0.2489 0.357  0.6992 0.0372  0.0057  -0.0717 154  SER A CA    
1248 C  C     . SER A 154 ? 0.2399 0.3447 0.6928 0.033   0.0055  -0.0692 154  SER A C     
1249 O  O     . SER A 154 ? 0.2418 0.3426 0.6964 0.031   0.0047  -0.0716 154  SER A O     
1250 C  CB    . SER A 154 ? 0.2489 0.3575 0.6997 0.04    0.0065  -0.073  154  SER A CB    
1251 O  OG    . SER A 154 ? 0.2618 0.3661 0.7151 0.0386  0.0059  -0.0758 154  SER A OG    
1252 N  N     . ARG A 155 ? 0.2282 0.3346 0.6815 0.0317  0.0061  -0.0643 155  ARG A N     
1253 C  CA    . ARG A 155 ? 0.2218 0.325  0.677  0.028   0.0057  -0.0618 155  ARG A CA    
1254 C  C     . ARG A 155 ? 0.2106 0.3121 0.6686 0.0274  0.0063  -0.0613 155  ARG A C     
1255 O  O     . ARG A 155 ? 0.2177 0.3216 0.6762 0.0296  0.0074  -0.0602 155  ARG A O     
1256 C  CB    . ARG A 155 ? 0.2344 0.3396 0.6891 0.0266  0.0057  -0.0568 155  ARG A CB    
1257 C  CG    . ARG A 155 ? 0.2659 0.3724 0.7181 0.0268  0.0051  -0.0569 155  ARG A CG    
1258 C  CD    . ARG A 155 ? 0.3098 0.4191 0.7618 0.0262  0.0053  -0.0518 155  ARG A CD    
1259 N  NE    . ARG A 155 ? 0.3472 0.4574 0.797  0.026   0.0047  -0.0517 155  ARG A NE    
1260 C  CZ    . ARG A 155 ? 0.3659 0.4803 0.8141 0.0289  0.0053  -0.0518 155  ARG A CZ    
1261 N  NH1   . ARG A 155 ? 0.3586 0.4766 0.8067 0.0324  0.0064  -0.0521 155  ARG A NH1   
1262 N  NH2   . ARG A 155 ? 0.3546 0.4696 0.8009 0.0286  0.0048  -0.0515 155  ARG A NH2   
1263 N  N     . LYS A 156 ? 0.1915 0.2889 0.6512 0.0245  0.0057  -0.062  156  LYS A N     
1264 C  CA    A LYS A 156 ? 0.1887 0.284  0.6512 0.0234  0.0062  -0.0612 156  LYS A CA    
1265 C  CA    B LYS A 156 ? 0.185  0.2804 0.6475 0.0234  0.0062  -0.0612 156  LYS A CA    
1266 C  C     . LYS A 156 ? 0.1851 0.2807 0.6483 0.0211  0.0062  -0.0561 156  LYS A C     
1267 O  O     . LYS A 156 ? 0.1832 0.2789 0.6448 0.0196  0.0054  -0.0541 156  LYS A O     
1268 C  CB    A LYS A 156 ? 0.2128 0.3038 0.6769 0.0215  0.0055  -0.0642 156  LYS A CB    
1269 C  CB    B LYS A 156 ? 0.1979 0.2889 0.6621 0.0216  0.0055  -0.0641 156  LYS A CB    
1270 C  CG    A LYS A 156 ? 0.2589 0.3474 0.7261 0.0199  0.0059  -0.0632 156  LYS A CG    
1271 C  CG    B LYS A 156 ? 0.2224 0.3126 0.6867 0.0234  0.0051  -0.0692 156  LYS A CG    
1272 C  CD    A LYS A 156 ? 0.299  0.3838 0.7668 0.0168  0.0052  -0.0627 156  LYS A CD    
1273 C  CD    B LYS A 156 ? 0.2631 0.3492 0.7303 0.0214  0.0047  -0.0711 156  LYS A CD    
1274 C  CE    A LYS A 156 ? 0.3286 0.4113 0.7994 0.0155  0.0057  -0.0614 156  LYS A CE    
1275 C  CE    B LYS A 156 ? 0.3167 0.4015 0.7838 0.0219  0.0037  -0.0754 156  LYS A CE    
1276 N  NZ    A LYS A 156 ? 0.3413 0.4264 0.8126 0.0156  0.0065  -0.0576 156  LYS A NZ    
1277 N  NZ    B LYS A 156 ? 0.3501 0.4313 0.8208 0.0204  0.0034  -0.0772 156  LYS A NZ    
1278 N  N     . ASN A 157 ? 0.1785 0.2741 0.644  0.0206  0.007   -0.054  157  ASN A N     
1279 C  CA    . ASN A 157 ? 0.1766 0.2723 0.6429 0.0183  0.0067  -0.0492 157  ASN A CA    
1280 C  C     . ASN A 157 ? 0.1623 0.2538 0.6282 0.0149  0.0054  -0.049  157  ASN A C     
1281 O  O     . ASN A 157 ? 0.1649 0.2533 0.6312 0.0143  0.0051  -0.0521 157  ASN A O     
1282 C  CB    . ASN A 157 ? 0.206  0.3026 0.6749 0.0187  0.0078  -0.047  157  ASN A CB    
1283 C  CG    . ASN A 157 ? 0.2728 0.3743 0.7413 0.0215  0.0089  -0.0447 157  ASN A CG    
1284 O  OD1   . ASN A 157 ? 0.3118 0.416  0.78   0.0211  0.0086  -0.0407 157  ASN A OD1   
1285 N  ND2   . ASN A 157 ? 0.2732 0.3761 0.742  0.0247  0.0101  -0.0471 157  ASN A ND2   
1286 N  N     . LEU A 158 ? 0.1492 0.2407 0.6142 0.013   0.0045  -0.0453 158  LEU A N     
1287 C  CA    . LEU A 158 ? 0.1338 0.2213 0.5978 0.0101  0.0032  -0.0449 158  LEU A CA    
1288 C  C     . LEU A 158 ? 0.1231 0.2076 0.5892 0.0086  0.0033  -0.0449 158  LEU A C     
1289 O  O     . LEU A 158 ? 0.1204 0.2061 0.5885 0.0086  0.0039  -0.0427 158  LEU A O     
1290 C  CB    . LEU A 158 ? 0.125  0.213  0.5878 0.0083  0.0019  -0.0407 158  LEU A CB    
1291 C  CG    . LEU A 158 ? 0.1284 0.2186 0.589  0.0091  0.0015  -0.04   158  LEU A CG    
1292 C  CD1   . LEU A 158 ? 0.1162 0.2071 0.5767 0.0072  0.0003  -0.0351 158  LEU A CD1   
1293 C  CD2   . LEU A 158 ? 0.1283 0.2159 0.5863 0.0088  0.0009  -0.0433 158  LEU A CD2   
1294 N  N     . ARG A 159 ? 0.1185 0.1991 0.5839 0.0073  0.0027  -0.047  159  ARG A N     
1295 C  CA    . ARG A 159 ? 0.121  0.1983 0.588  0.0058  0.0027  -0.0468 159  ARG A CA    
1296 C  C     . ARG A 159 ? 0.1045 0.1786 0.569  0.0035  0.0012  -0.0451 159  ARG A C     
1297 O  O     . ARG A 159 ? 0.1107 0.1838 0.5725 0.0034  0.0005  -0.0461 159  ARG A O     
1298 C  CB    . ARG A 159 ? 0.1569 0.2326 0.6254 0.0067  0.0034  -0.0509 159  ARG A CB    
1299 C  CG    . ARG A 159 ? 0.2298 0.3076 0.7009 0.0089  0.0047  -0.053  159  ARG A CG    
1300 C  CD    . ARG A 159 ? 0.3093 0.3845 0.7824 0.0092  0.005   -0.0566 159  ARG A CD    
1301 N  NE    . ARG A 159 ? 0.3828 0.4568 0.8541 0.0091  0.0042  -0.059  159  ARG A NE    
1302 C  CZ    . ARG A 159 ? 0.4319 0.5029 0.9039 0.0082  0.0039  -0.0604 159  ARG A CZ    
1303 N  NH1   . ARG A 159 ? 0.4485 0.5174 0.9231 0.0072  0.0044  -0.0597 159  ARG A NH1   
1304 N  NH2   . ARG A 159 ? 0.4241 0.4944 0.8944 0.0083  0.0033  -0.0623 159  ARG A NH2   
1305 N  N     . PHE A 160 ? 0.0903 0.1625 0.5555 0.0019  0.0008  -0.0428 160  PHE A N     
1306 C  CA    . PHE A 160 ? 0.092  0.1605 0.5544 -0.0002 -0.0008 -0.0412 160  PHE A CA    
1307 C  C     . PHE A 160 ? 0.0775 0.1424 0.5406 -0.0007 -0.0005 -0.0423 160  PHE A C     
1308 O  O     . PHE A 160 ? 0.0813 0.1469 0.5476 -0.0003 0.0006  -0.0426 160  PHE A O     
1309 C  CB    . PHE A 160 ? 0.0949 0.164  0.557  -0.0017 -0.0021 -0.037  160  PHE A CB    
1310 C  CG    . PHE A 160 ? 0.1096 0.1825 0.5715 -0.0011 -0.0023 -0.0353 160  PHE A CG    
1311 C  CD1   . PHE A 160 ? 0.12   0.1926 0.579  -0.0012 -0.0033 -0.0355 160  PHE A CD1   
1312 C  CD2   . PHE A 160 ? 0.118  0.1951 0.5827 -0.0001 -0.0013 -0.0335 160  PHE A CD2   
1313 C  CE1   . PHE A 160 ? 0.1293 0.2057 0.5884 -0.0005 -0.0033 -0.0337 160  PHE A CE1   
1314 C  CE2   . PHE A 160 ? 0.1252 0.2061 0.5899 0.0008  -0.0013 -0.0317 160  PHE A CE2   
1315 C  CZ    . PHE A 160 ? 0.118  0.1986 0.58   0.0005  -0.0023 -0.0317 160  PHE A CZ    
1316 N  N     . PRO A 161 ? 0.0605 0.1217 0.5207 -0.0016 -0.0015 -0.0426 161  PRO A N     
1317 C  CA    . PRO A 161 ? 0.0519 0.1099 0.5127 -0.002  -0.0012 -0.0432 161  PRO A CA    
1318 C  C     . PRO A 161 ? 0.0413 0.0939 0.4983 -0.0029 -0.0016 -0.0403 161  PRO A C     
1319 O  O     . PRO A 161 ? 0.0471 0.1053 0.5079 -0.0042 -0.0028 -0.0376 161  PRO A O     
1320 C  CB    . PRO A 161 ? 0.0608 0.1151 0.5173 -0.0025 -0.0023 -0.0436 161  PRO A CB    
1321 C  CG    . PRO A 161 ? 0.0685 0.1235 0.5221 -0.0033 -0.0039 -0.0418 161  PRO A CG    
1322 C  CD    . PRO A 161 ? 0.0507 0.1105 0.5069 -0.0022 -0.0029 -0.0423 161  PRO A CD    
1323 N  N     . ASN A 162 ? 0.0397 0.0648 0.4726 -0.0013 -0.0007 -0.0405 162  ASN A N     
1324 C  CA    . ASN A 162 ? 0.0398 0.0641 0.4732 -0.0017 -0.0012 -0.0378 162  ASN A CA    
1325 C  C     . ASN A 162 ? 0.041  0.0806 0.4883 -0.0043 -0.0036 -0.0358 162  ASN A C     
1326 O  O     . ASN A 162 ? 0.0417 0.0831 0.4904 -0.0047 -0.0043 -0.0371 162  ASN A O     
1327 C  CB    . ASN A 162 ? 0.0397 0.06   0.473  -0.0013 0       -0.0386 162  ASN A CB    
1328 C  CG    . ASN A 162 ? 0.0401 0.0707 0.4852 -0.0025 -0.0003 -0.036  162  ASN A CG    
1329 O  OD1   . ASN A 162 ? 0.0402 0.0685 0.4821 -0.0031 -0.0019 -0.0339 162  ASN A OD1   
1330 N  ND2   . ASN A 162 ? 0.0404 0.0793 0.4963 -0.0028 0.0013  -0.0361 162  ASN A ND2   
1331 N  N     . PRO A 163 ? 0.0428 0.0942 0.5014 -0.0071 -0.0052 -0.0328 163  PRO A N     
1332 C  CA    . PRO A 163 ? 0.0453 0.0932 0.4994 -0.0086 -0.0078 -0.0311 163  PRO A CA    
1333 C  C     . PRO A 163 ? 0.0577 0.1006 0.5082 -0.0084 -0.0084 -0.0319 163  PRO A C     
1334 O  O     . PRO A 163 ? 0.0714 0.1108 0.5173 -0.009  -0.0103 -0.0315 163  PRO A O     
1335 C  CB    . PRO A 163 ? 0.0521 0.1012 0.5077 -0.01   -0.009  -0.0277 163  PRO A CB    
1336 C  CG    . PRO A 163 ? 0.0485 0.1028 0.5089 -0.0093 -0.0071 -0.0275 163  PRO A CG    
1337 C  CD    . PRO A 163 ? 0.0405 0.0798 0.4869 -0.0051 -0.0043 -0.0307 163  PRO A CD    
1338 N  N     . ALA A 164 ? 0.0478 0.0904 0.5005 -0.0074 -0.0067 -0.0329 164  ALA A N     
1339 C  CA    . ALA A 164 ? 0.0539 0.0923 0.5036 -0.0067 -0.0068 -0.0335 164  ALA A CA    
1340 C  C     . ALA A 164 ? 0.0511 0.0875 0.4979 -0.0057 -0.0066 -0.0357 164  ALA A C     
1341 O  O     . ALA A 164 ? 0.0464 0.0787 0.4889 -0.0054 -0.0075 -0.0357 164  ALA A O     
1342 C  CB    . ALA A 164 ? 0.049  0.0883 0.5027 -0.0057 -0.0046 -0.034  164  ALA A CB    
1343 N  N     . ILE A 165 ? 0.0433 0.0827 0.4922 -0.0051 -0.0054 -0.0376 165  ILE A N     
1344 C  CA    . ILE A 165 ? 0.0559 0.0938 0.5023 -0.0042 -0.0052 -0.0396 165  ILE A CA    
1345 C  C     . ILE A 165 ? 0.05   0.0849 0.4908 -0.005  -0.0074 -0.0387 165  ILE A C     
1346 O  O     . ILE A 165 ? 0.0451 0.0758 0.4817 -0.0046 -0.0081 -0.0387 165  ILE A O     
1347 C  CB    . ILE A 165 ? 0.0825 0.124  0.5322 -0.0032 -0.0036 -0.0421 165  ILE A CB    
1348 C  CG1   . ILE A 165 ? 0.1118 0.1564 0.5673 -0.0026 -0.0017 -0.0429 165  ILE A CG1   
1349 C  CG2   . ILE A 165 ? 0.0981 0.1378 0.5459 -0.0022 -0.0031 -0.044  165  ILE A CG2   
1350 C  CD1   . ILE A 165 ? 0.1308 0.1739 0.5882 -0.0021 -0.0007 -0.0427 165  ILE A CD1   
1351 N  N     . PRO A 166 ? 0.0444 0.0812 0.4849 -0.0062 -0.0087 -0.0376 166  PRO A N     
1352 C  CA    . PRO A 166 ? 0.0501 0.0836 0.4855 -0.0071 -0.011  -0.0365 166  PRO A CA    
1353 C  C     . PRO A 166 ? 0.0569 0.0857 0.4887 -0.0078 -0.0129 -0.0348 166  PRO A C     
1354 O  O     . PRO A 166 ? 0.0568 0.0813 0.4835 -0.0078 -0.0143 -0.0348 166  PRO A O     
1355 C  CB    . PRO A 166 ? 0.0521 0.089  0.4893 -0.0083 -0.0119 -0.0348 166  PRO A CB    
1356 C  CG    . PRO A 166 ? 0.0584 0.1005 0.5006 -0.0073 -0.0096 -0.0362 166  PRO A CG    
1357 C  CD    . PRO A 166 ? 0.0419 0.0793 0.4821 -0.0057 -0.0079 -0.0371 166  PRO A CD    
1358 N  N     . TYR A 167 ? 0.0531 0.0824 0.4872 -0.0082 -0.0128 -0.0335 167  TYR A N     
1359 C  CA    . TYR A 167 ? 0.0659 0.0907 0.4964 -0.0088 -0.0147 -0.0319 167  TYR A CA    
1360 C  C     . TYR A 167 ? 0.0735 0.0942 0.5004 -0.0071 -0.0141 -0.0332 167  TYR A C     
1361 O  O     . TYR A 167 ? 0.0785 0.0943 0.5001 -0.0072 -0.0161 -0.0324 167  TYR A O     
1362 C  CB    . TYR A 167 ? 0.0667 0.0932 0.5006 -0.0096 -0.0147 -0.0301 167  TYR A CB    
1363 C  CG    . TYR A 167 ? 0.0814 0.1032 0.5109 -0.0103 -0.0173 -0.0284 167  TYR A CG    
1364 C  CD1   . TYR A 167 ? 0.1014 0.1212 0.5282 -0.0122 -0.0205 -0.0266 167  TYR A CD1   
1365 C  CD2   . TYR A 167 ? 0.0953 0.1142 0.5229 -0.009  -0.0168 -0.0287 167  TYR A CD2   
1366 C  CE1   . TYR A 167 ? 0.1222 0.1371 0.5445 -0.0128 -0.0232 -0.0253 167  TYR A CE1   
1367 C  CE2   . TYR A 167 ? 0.115  0.1291 0.5378 -0.0093 -0.0193 -0.0274 167  TYR A CE2   
1368 C  CZ    . TYR A 167 ? 0.141  0.153  0.561  -0.0113 -0.0227 -0.0259 167  TYR A CZ    
1369 O  OH    . TYR A 167 ? 0.1773 0.1842 0.5923 -0.0116 -0.0255 -0.0248 167  TYR A OH    
1370 N  N     . SER A 168 ? 0.0538 0.0765 0.4836 -0.0055 -0.0113 -0.0351 168  SER A N     
1371 C  CA    . SER A 168 ? 0.0471 0.0669 0.4747 -0.0036 -0.0102 -0.036  168  SER A CA    
1372 C  C     . SER A 168 ? 0.0452 0.0563 0.4618 -0.0016 -0.0112 -0.0364 168  SER A C     
1373 O  O     . SER A 168 ? 0.0421 0.045  0.4454 0.001   -0.0108 -0.0358 168  SER A O     
1374 C  CB    . SER A 168 ? 0.0427 0.0583 0.4676 -0.0012 -0.0071 -0.0377 168  SER A CB    
1375 O  OG    . SER A 168 ? 0.0534 0.0789 0.4871 -0.0022 -0.0067 -0.0394 168  SER A OG    
1376 N  N     . TYR A 169 ? 0.0457 0.0604 0.4642 -0.0032 -0.0122 -0.0369 169  TYR A N     
1377 C  CA    . TYR A 169 ? 0.0556 0.0679 0.47   -0.0033 -0.0135 -0.0374 169  TYR A CA    
1378 C  C     . TYR A 169 ? 0.0468 0.0525 0.4534 -0.0025 -0.0162 -0.0356 169  TYR A C     
1379 O  O     . TYR A 169 ? 0.041  0.0433 0.4275 0.0014  -0.016  -0.0341 169  TYR A O     
1380 C  CB    . TYR A 169 ? 0.0729 0.0879 0.4882 -0.0041 -0.0137 -0.038  169  TYR A CB    
1381 C  CG    . TYR A 169 ? 0.1106 0.1298 0.5299 -0.003  -0.0111 -0.04   169  TYR A CG    
1382 C  CD1   . TYR A 169 ? 0.1325 0.1564 0.5579 -0.0031 -0.0095 -0.0405 169  TYR A CD1   
1383 C  CD2   . TYR A 169 ? 0.1407 0.1589 0.5576 -0.0018 -0.0103 -0.0414 169  TYR A CD2   
1384 C  CE1   . TYR A 169 ? 0.1553 0.1826 0.5845 -0.0021 -0.0074 -0.0425 169  TYR A CE1   
1385 C  CE2   . TYR A 169 ? 0.1583 0.1802 0.5791 -0.0008 -0.0082 -0.0432 169  TYR A CE2   
1386 C  CZ    . TYR A 169 ? 0.1797 0.2061 0.6066 -0.001  -0.0068 -0.0439 169  TYR A CZ    
1387 O  OH    . TYR A 169 ? 0.2243 0.2541 0.6551 0       -0.005  -0.0459 169  TYR A OH    
1388 N  N     . ILE A 170 ? 0.0465 0.0535 0.4552 -0.0048 -0.018  -0.0339 170  ILE A N     
1389 C  CA    . ILE A 170 ? 0.0664 0.0696 0.4723 -0.0071 -0.0214 -0.0324 170  ILE A CA    
1390 C  C     . ILE A 170 ? 0.0659 0.0658 0.4693 -0.0056 -0.0213 -0.0322 170  ILE A C     
1391 O  O     . ILE A 170 ? 0.068  0.0622 0.4649 -0.0048 -0.0231 -0.0321 170  ILE A O     
1392 C  CB    . ILE A 170 ? 0.0782 0.0839 0.4874 -0.0096 -0.0232 -0.0304 170  ILE A CB    
1393 C  CG1   . ILE A 170 ? 0.0905 0.0995 0.5018 -0.0108 -0.0235 -0.0303 170  ILE A CG1   
1394 C  CG2   . ILE A 170 ? 0.0892 0.09   0.494  -0.0108 -0.0268 -0.0287 170  ILE A CG2   
1395 C  CD1   . ILE A 170 ? 0.0948 0.1081 0.5112 -0.0128 -0.0242 -0.0282 170  ILE A CD1   
1396 N  N     . SER A 171 ? 0.0548 0.0582 0.4631 -0.005  -0.019  -0.0322 171  SER A N     
1397 C  CA    . SER A 171 ? 0.0566 0.0575 0.4631 -0.0033 -0.0185 -0.0317 171  SER A CA    
1398 C  C     . SER A 171 ? 0.0529 0.0508 0.4555 -0.0007 -0.0171 -0.0329 171  SER A C     
1399 O  O     . SER A 171 ? 0.0571 0.0504 0.4545 0.0008  -0.0181 -0.0324 171  SER A O     
1400 C  CB    . SER A 171 ? 0.0695 0.075  0.4825 -0.0033 -0.0164 -0.0312 171  SER A CB    
1401 O  OG    . SER A 171 ? 0.1079 0.1182 0.5265 -0.003  -0.0136 -0.0326 171  SER A OG    
1402 N  N     . HIS A 172 ? 0.0435 0.0458 0.445  0.0012  -0.0148 -0.0339 172  HIS A N     
1403 C  CA    . HIS A 172 ? 0.0547 0.0527 0.4562 0.0026  -0.0136 -0.0353 172  HIS A CA    
1404 C  C     . HIS A 172 ? 0.0676 0.0596 0.461  0.003   -0.016  -0.0352 172  HIS A C     
1405 O  O     . HIS A 172 ? 0.0702 0.0582 0.4588 0.0053  -0.0157 -0.035  172  HIS A O     
1406 C  CB    . HIS A 172 ? 0.0501 0.0522 0.456  0.0031  -0.011  -0.0369 172  HIS A CB    
1407 C  CG    . HIS A 172 ? 0.0602 0.0613 0.4651 0.0058  -0.0089 -0.0372 172  HIS A CG    
1408 N  ND1   . HIS A 172 ? 0.0755 0.0748 0.4796 0.0076  -0.008  -0.0362 172  HIS A ND1   
1409 C  CD2   . HIS A 172 ? 0.0604 0.0624 0.4656 0.0069  -0.0074 -0.0383 172  HIS A CD2   
1410 C  CE1   . HIS A 172 ? 0.0777 0.0769 0.4816 0.0099  -0.006  -0.0365 172  HIS A CE1   
1411 N  NE2   . HIS A 172 ? 0.0756 0.0764 0.4802 0.0094  -0.0056 -0.0378 172  HIS A NE2   
1412 N  N     . SER A 173 ? 0.0826 0.0737 0.4743 0.0009  -0.0184 -0.0351 173  SER A N     
1413 C  CA    . SER A 173 ? 0.1112 0.0961 0.4952 0.001   -0.0211 -0.0349 173  SER A CA    
1414 C  C     . SER A 173 ? 0.1303 0.1101 0.5093 0.0016  -0.0233 -0.0339 173  SER A C     
1415 O  O     . SER A 173 ? 0.1412 0.1154 0.5133 0.0036  -0.0241 -0.0341 173  SER A O     
1416 C  CB    . SER A 173 ? 0.1376 0.1232 0.5221 -0.0016 -0.0234 -0.0346 173  SER A CB    
1417 O  OG    . SER A 173 ? 0.1814 0.1707 0.5688 -0.0019 -0.0217 -0.0356 173  SER A OG    
1418 N  N     . LYS A 174 ? 0.128  0.1095 0.5102 0       -0.0244 -0.0327 174  LYS A N     
1419 C  CA    . LYS A 174 ? 0.145  0.1219 0.5226 0.0003  -0.0268 -0.0317 174  LYS A CA    
1420 C  C     . LYS A 174 ? 0.1648 0.1397 0.5397 0.0037  -0.0249 -0.0318 174  LYS A C     
1421 O  O     . LYS A 174 ? 0.1694 0.1382 0.5369 0.0054  -0.0266 -0.0317 174  LYS A O     
1422 C  CB    . LYS A 174 ? 0.1585 0.1383 0.5407 -0.0022 -0.0282 -0.0302 174  LYS A CB    
1423 N  N     . ASN A 175 ? 0.1636 0.1436 0.5445 0.0048  -0.0212 -0.032  175  ASN A N     
1424 C  CA    . ASN A 175 ? 0.1785 0.1578 0.5585 0.008   -0.0189 -0.0317 175  ASN A CA    
1425 C  C     . ASN A 175 ? 0.1973 0.1726 0.5712 0.0109  -0.0181 -0.0324 175  ASN A C     
1426 O  O     . ASN A 175 ? 0.2124 0.1843 0.5818 0.0137  -0.0179 -0.0317 175  ASN A O     
1427 C  CB    . ASN A 175 ? 0.1838 0.1697 0.5725 0.0081  -0.0153 -0.0318 175  ASN A CB    
1428 C  CG    . ASN A 175 ? 0.213  0.2026 0.6072 0.0061  -0.0156 -0.0309 175  ASN A CG    
1429 O  OD1   . ASN A 175 ? 0.2427 0.2298 0.6341 0.0054  -0.018  -0.0298 175  ASN A OD1   
1430 N  ND2   . ASN A 175 ? 0.1919 0.1874 0.5939 0.005   -0.0134 -0.0313 175  ASN A ND2   
1431 N  N     . THR A 176 ? 0.1859 0.162  0.5601 0.0105  -0.0175 -0.0335 176  THR A N     
1432 C  CA    . THR A 176 ? 0.173  0.146  0.5422 0.0131  -0.0165 -0.034  176  THR A CA    
1433 C  C     . THR A 176 ? 0.1794 0.1454 0.5395 0.0134  -0.0197 -0.0342 176  THR A C     
1434 O  O     . THR A 176 ? 0.191  0.1525 0.5447 0.0163  -0.0194 -0.0341 176  THR A O     
1435 C  CB    . THR A 176 ? 0.1597 0.1373 0.5338 0.0125  -0.0143 -0.035  176  THR A CB    
1436 O  OG1   . THR A 176 ? 0.1488 0.1276 0.5243 0.0094  -0.0162 -0.0356 176  THR A OG1   
1437 C  CG2   . THR A 176 ? 0.1549 0.1387 0.5374 0.0127  -0.0111 -0.035  176  THR A CG2   
1438 N  N     . GLY A 177 ? 0.1654 0.1304 0.5251 0.0104  -0.0227 -0.0343 177  GLY A N     
1439 C  CA    . GLY A 177 ? 0.1637 0.1223 0.5157 0.0102  -0.0259 -0.0346 177  GLY A CA    
1440 C  C     . GLY A 177 ? 0.1508 0.1105 0.5031 0.0097  -0.0251 -0.0355 177  GLY A C     
1441 O  O     . GLY A 177 ? 0.1588 0.1132 0.5047 0.0099  -0.0272 -0.0359 177  GLY A O     
1442 N  N     . ASN A 178 ? 0.1232 0.0894 0.4826 0.0092  -0.022  -0.036  178  ASN A N     
1443 C  CA    . ASN A 178 ? 0.1162 0.0843 0.4765 0.0088  -0.021  -0.0369 178  ASN A CA    
1444 C  C     . ASN A 178 ? 0.1048 0.0771 0.4705 0.0054  -0.0221 -0.037  178  ASN A C     
1445 O  O     . ASN A 178 ? 0.1108 0.0855 0.4805 0.0035  -0.023  -0.0363 178  ASN A O     
1446 C  CB    . ASN A 178 ? 0.1236 0.0961 0.4881 0.0109  -0.017  -0.0374 178  ASN A CB    
1447 C  CG    . ASN A 178 ? 0.1751 0.1501 0.5409 0.0109  -0.0156 -0.0384 178  ASN A CG    
1448 O  OD1   . ASN A 178 ? 0.2012 0.173  0.5625 0.0103  -0.0173 -0.0386 178  ASN A OD1   
1449 N  ND2   . ASN A 178 ? 0.1454 0.1257 0.5171 0.0116  -0.0125 -0.0388 178  ASN A ND2   
1450 N  N     . PHE A 179 ? 0.0889 0.0622 0.4546 0.0047  -0.022  -0.0376 179  PHE A N     
1451 C  CA    . PHE A 179 ? 0.0774 0.0551 0.4481 0.0019  -0.0227 -0.0376 179  PHE A CA    
1452 C  C     . PHE A 179 ? 0.0657 0.0509 0.4439 0.0019  -0.0194 -0.0385 179  PHE A C     
1453 O  O     . PHE A 179 ? 0.0451 0.0458 0.4235 0.002   -0.0176 -0.0381 179  PHE A O     
1454 C  CB    . PHE A 179 ? 0.0708 0.0458 0.4375 0.0013  -0.0243 -0.0377 179  PHE A CB    
1455 C  CG    . PHE A 179 ? 0.0762 0.0556 0.4477 -0.0014 -0.0252 -0.0372 179  PHE A CG    
1456 C  CD1   . PHE A 179 ? 0.0892 0.0698 0.4637 -0.0038 -0.0272 -0.0359 179  PHE A CD1   
1457 C  CD2   . PHE A 179 ? 0.0825 0.0644 0.455  -0.0015 -0.0241 -0.0378 179  PHE A CD2   
1458 C  CE1   . PHE A 179 ? 0.0911 0.0756 0.4698 -0.006  -0.028  -0.0351 179  PHE A CE1   
1459 C  CE2   . PHE A 179 ? 0.0905 0.0764 0.4671 -0.0037 -0.0249 -0.0371 179  PHE A CE2   
1460 C  CZ    . PHE A 179 ? 0.0867 0.0738 0.4663 -0.0059 -0.0268 -0.0356 179  PHE A CZ    
1461 N  N     . ILE A 180 ? 0.0592 0.0487 0.4434 0.0006  -0.0189 -0.0381 180  ILE A N     
1462 C  CA    . ILE A 180 ? 0.07   0.0662 0.4614 0.0006  -0.0162 -0.0391 180  ILE A CA    
1463 C  C     . ILE A 180 ? 0.0828 0.0827 0.4784 -0.0019 -0.0174 -0.0384 180  ILE A C     
1464 O  O     . ILE A 180 ? 0.0955 0.0948 0.4919 -0.0032 -0.0189 -0.0371 180  ILE A O     
1465 C  CB    . ILE A 180 ? 0.0707 0.0684 0.4653 0.0019  -0.0142 -0.0391 180  ILE A CB    
1466 C  CG1   . ILE A 180 ? 0.0822 0.0761 0.4724 0.0046  -0.0131 -0.0392 180  ILE A CG1   
1467 C  CG2   . ILE A 180 ? 0.0719 0.0762 0.4742 0.0016  -0.0118 -0.0402 180  ILE A CG2   
1468 C  CD1   . ILE A 180 ? 0.0986 0.0894 0.4867 0.0057  -0.0135 -0.0381 180  ILE A CD1   
1469 N  N     . VAL A 181 ? 0.0715 0.0752 0.4697 -0.0026 -0.0167 -0.039  181  VAL A N     
1470 C  CA    . VAL A 181 ? 0.0712 0.0784 0.4731 -0.0047 -0.0178 -0.0381 181  VAL A CA    
1471 C  C     . VAL A 181 ? 0.072  0.0856 0.4793 -0.0045 -0.0157 -0.0392 181  VAL A C     
1472 O  O     . VAL A 181 ? 0.0702 0.085  0.4775 -0.0031 -0.014  -0.0408 181  VAL A O     
1473 C  CB    . VAL A 181 ? 0.0766 0.0803 0.474  -0.0059 -0.0205 -0.0369 181  VAL A CB    
1474 C  CG1   . VAL A 181 ? 0.0737 0.0778 0.4692 -0.005  -0.0197 -0.038  181  VAL A CG1   
1475 C  CG2   . VAL A 181 ? 0.0825 0.0888 0.4832 -0.0082 -0.0223 -0.035  181  VAL A CG2   
1476 N  N     . GLN A 182 ? 0.0636 0.0813 0.4754 -0.0059 -0.0159 -0.0383 182  GLN A N     
1477 C  CA    . GLN A 182 ? 0.0741 0.0976 0.4905 -0.0057 -0.0143 -0.0392 182  GLN A CA    
1478 C  C     . GLN A 182 ? 0.0846 0.1091 0.5003 -0.0071 -0.0161 -0.0376 182  GLN A C     
1479 O  O     . GLN A 182 ? 0.0951 0.1179 0.5102 -0.0087 -0.0182 -0.0354 182  GLN A O     
1480 C  CB    . GLN A 182 ? 0.0891 0.1167 0.5111 -0.0059 -0.0131 -0.0391 182  GLN A CB    
1481 C  CG    . GLN A 182 ? 0.1419 0.1749 0.5682 -0.005  -0.011  -0.0409 182  GLN A CG    
1482 C  CD    . GLN A 182 ? 0.2091 0.2451 0.6404 -0.005  -0.0098 -0.041  182  GLN A CD    
1483 O  OE1   . GLN A 182 ? 0.2458 0.283  0.6789 -0.0061 -0.0106 -0.0391 182  GLN A OE1   
1484 N  NE2   . GLN A 182 ? 0.2225 0.2596 0.6563 -0.0037 -0.0079 -0.043  182  GLN A NE2   
1485 N  N     . ALA A 183 ? 0.0852 0.1118 0.5006 -0.0065 -0.0154 -0.0385 183  ALA A N     
1486 C  CA    . ALA A 183 ? 0.0922 0.1202 0.5074 -0.0075 -0.0167 -0.0369 183  ALA A CA    
1487 C  C     . ALA A 183 ? 0.0957 0.1304 0.5154 -0.0067 -0.0149 -0.0375 183  ALA A C     
1488 O  O     . ALA A 183 ? 0.1001 0.1372 0.5214 -0.0052 -0.0128 -0.0399 183  ALA A O     
1489 C  CB    . ALA A 183 ? 0.1003 0.1244 0.5104 -0.0071 -0.0176 -0.0371 183  ALA A CB    
1490 N  N     . TYR A 184 ? 0.0882 0.1259 0.5102 -0.0077 -0.0158 -0.0354 184  TYR A N     
1491 C  CA    . TYR A 184 ? 0.0831 0.1274 0.5094 -0.0068 -0.0142 -0.0356 184  TYR A CA    
1492 C  C     . TYR A 184 ? 0.0871 0.1334 0.5127 -0.0067 -0.0146 -0.0345 184  TYR A C     
1493 O  O     . TYR A 184 ? 0.08   0.1244 0.5044 -0.0082 -0.0166 -0.032  184  TYR A O     
1494 C  CB    . TYR A 184 ? 0.0812 0.1284 0.5116 -0.0076 -0.0143 -0.0337 184  TYR A CB    
1495 C  CG    . TYR A 184 ? 0.0873 0.1317 0.518  -0.0082 -0.0144 -0.034  184  TYR A CG    
1496 C  CD1   . TYR A 184 ? 0.0932 0.1389 0.5259 -0.0068 -0.0124 -0.0364 184  TYR A CD1   
1497 C  CD2   . TYR A 184 ? 0.0991 0.1389 0.5275 -0.0098 -0.0167 -0.0321 184  TYR A CD2   
1498 C  CE1   . TYR A 184 ? 0.1047 0.1478 0.5377 -0.0072 -0.0123 -0.0367 184  TYR A CE1   
1499 C  CE2   . TYR A 184 ? 0.1111 0.1481 0.5392 -0.01   -0.0167 -0.0325 184  TYR A CE2   
1500 C  CZ    . TYR A 184 ? 0.1227 0.1616 0.5533 -0.0087 -0.0144 -0.0346 184  TYR A CZ    
1501 O  OH    . TYR A 184 ? 0.1659 0.2022 0.5965 -0.0088 -0.0144 -0.0347 184  TYR A OH    
1502 N  N     . PHE A 185 ? 0.0932 0.1431 0.5195 -0.005  -0.0128 -0.0364 185  PHE A N     
1503 C  CA    . PHE A 185 ? 0.1139 0.1666 0.5399 -0.0045 -0.0128 -0.0355 185  PHE A CA    
1504 C  C     . PHE A 185 ? 0.1332 0.1924 0.5635 -0.0036 -0.0117 -0.0347 185  PHE A C     
1505 O  O     . PHE A 185 ? 0.1444 0.2062 0.5773 -0.0026 -0.0102 -0.0363 185  PHE A O     
1506 C  CB    . PHE A 185 ? 0.12   0.1725 0.5435 -0.003  -0.0116 -0.0382 185  PHE A CB    
1507 C  CG    . PHE A 185 ? 0.1347 0.1812 0.5534 -0.0035 -0.0127 -0.0384 185  PHE A CG    
1508 C  CD1   . PHE A 185 ? 0.1532 0.1942 0.5695 -0.0052 -0.0148 -0.0366 185  PHE A CD1   
1509 C  CD2   . PHE A 185 ? 0.1484 0.1944 0.5646 -0.0022 -0.0116 -0.0404 185  PHE A CD2   
1510 C  CE1   . PHE A 185 ? 0.1702 0.2054 0.5815 -0.0054 -0.0158 -0.0369 185  PHE A CE1   
1511 C  CE2   . PHE A 185 ? 0.1627 0.2032 0.5742 -0.0024 -0.0125 -0.0404 185  PHE A CE2   
1512 C  CZ    . PHE A 185 ? 0.1654 0.2004 0.5743 -0.0039 -0.0145 -0.0387 185  PHE A CZ    
1513 N  N     . ARG A 186 ? 0.1362 0.1983 0.5676 -0.0038 -0.0123 -0.0319 186  ARG A N     
1514 C  CA    . ARG A 186 ? 0.1487 0.2172 0.5839 -0.0026 -0.0111 -0.0308 186  ARG A CA    
1515 C  C     . ARG A 186 ? 0.1652 0.2376 0.6007 0.0001  -0.0089 -0.034  186  ARG A C     
1516 O  O     . ARG A 186 ? 0.1722 0.245  0.6056 0.001   -0.0086 -0.0349 186  ARG A O     
1517 C  CB    . ARG A 186 ? 0.1604 0.2311 0.5968 -0.0033 -0.0122 -0.0267 186  ARG A CB    
1518 C  CG    . ARG A 186 ? 0.2015 0.2793 0.6417 -0.0015 -0.0108 -0.0252 186  ARG A CG    
1519 C  CD    . ARG A 186 ? 0.2505 0.3313 0.6918 -0.0016 -0.0114 -0.0215 186  ARG A CD    
1520 N  NE    . ARG A 186 ? 0.3001 0.3795 0.7433 -0.004  -0.0136 -0.0173 186  ARG A NE    
1521 C  CZ    . ARG A 186 ? 0.3368 0.4208 0.7841 -0.0039 -0.0135 -0.0136 186  ARG A CZ    
1522 N  NH1   . ARG A 186 ? 0.3336 0.424  0.7831 -0.0012 -0.0112 -0.0136 186  ARG A NH1   
1523 N  NH2   . ARG A 186 ? 0.3303 0.4127 0.7795 -0.0064 -0.0157 -0.0097 186  ARG A NH2   
1524 N  N     . GLY A 187 ? 0.1734 0.2483 0.6112 0.0013  -0.0075 -0.0358 187  GLY A N     
1525 C  CA    . GLY A 187 ? 0.176  0.2546 0.6143 0.0038  -0.0057 -0.039  187  GLY A CA    
1526 C  C     . GLY A 187 ? 0.1738 0.2582 0.6133 0.0056  -0.005  -0.0373 187  GLY A C     
1527 O  O     . GLY A 187 ? 0.1587 0.245  0.6001 0.005   -0.0055 -0.0336 187  GLY A O     
1528 N  N     . GLU A 188 ? 0.1771 0.2645 0.6158 0.0079  -0.0038 -0.0398 188  GLU A N     
1529 C  CA    . GLU A 188 ? 0.1837 0.277  0.6235 0.0101  -0.0029 -0.0384 188  GLU A CA    
1530 C  C     . GLU A 188 ? 0.188  0.2851 0.631  0.0114  -0.002  -0.0375 188  GLU A C     
1531 O  O     . GLU A 188 ? 0.1898 0.2911 0.6344 0.0125  -0.0016 -0.0345 188  GLU A O     
1532 C  CB    . GLU A 188 ? 0.2008 0.2965 0.639  0.0125  -0.0018 -0.0419 188  GLU A CB    
1533 C  CG    . GLU A 188 ? 0.2256 0.3181 0.6608 0.0116  -0.0024 -0.0429 188  GLU A CG    
1534 C  CD    . GLU A 188 ? 0.2797 0.3683 0.7137 0.0111  -0.0024 -0.0467 188  GLU A CD    
1535 O  OE1   . GLU A 188 ? 0.2746 0.3602 0.7097 0.0099  -0.0027 -0.0473 188  GLU A OE1   
1536 O  OE2   . GLU A 188 ? 0.3217 0.4104 0.7537 0.012   -0.002  -0.0488 188  GLU A OE2   
1537 N  N     . GLU A 189 ? 0.1922 0.2874 0.6362 0.0113  -0.0016 -0.0399 189  GLU A N     
1538 C  CA    . GLU A 189 ? 0.2001 0.2981 0.6468 0.0125  -0.0007 -0.0394 189  GLU A CA    
1539 C  C     . GLU A 189 ? 0.212  0.3087 0.6608 0.0103  -0.0016 -0.0356 189  GLU A C     
1540 O  O     . GLU A 189 ? 0.2228 0.321  0.6738 0.011   -0.0008 -0.0352 189  GLU A O     
1541 C  CB    . GLU A 189 ? 0.2168 0.3141 0.6639 0.0138  0.0001  -0.0438 189  GLU A CB    
1542 C  CG    . GLU A 189 ? 0.2369 0.3377 0.683  0.0169  0.0011  -0.0468 189  GLU A CG    
1543 C  CD    . GLU A 189 ? 0.2824 0.3826 0.7292 0.0183  0.0017  -0.0512 189  GLU A CD    
1544 O  OE1   . GLU A 189 ? 0.2821 0.3781 0.7295 0.0166  0.0013  -0.0528 189  GLU A OE1   
1545 O  OE2   . GLU A 189 ? 0.3054 0.4093 0.752  0.0213  0.0025  -0.0529 189  GLU A OE2   
1546 N  N     . TYR A 190 ? 0.209  0.3027 0.6569 0.0077  -0.0032 -0.0329 190  TYR A N     
1547 C  CA    . TYR A 190 ? 0.2134 0.3061 0.6634 0.0055  -0.0043 -0.029  190  TYR A CA    
1548 C  C     . TYR A 190 ? 0.2278 0.3262 0.68   0.0068  -0.0038 -0.0251 190  TYR A C     
1549 O  O     . TYR A 190 ? 0.231  0.3302 0.6825 0.0065  -0.0045 -0.023  190  TYR A O     
1550 C  CB    . TYR A 190 ? 0.2074 0.2947 0.6555 0.0025  -0.0065 -0.0276 190  TYR A CB    
1551 C  CG    . TYR A 190 ? 0.2103 0.297  0.6605 0.0003  -0.008  -0.0232 190  TYR A CG    
1552 C  CD1   . TYR A 190 ? 0.2145 0.3003 0.6666 -0.0005 -0.0079 -0.0229 190  TYR A CD1   
1553 C  CD2   . TYR A 190 ? 0.2111 0.2986 0.6619 -0.001  -0.0094 -0.0192 190  TYR A CD2   
1554 C  CE1   . TYR A 190 ? 0.2115 0.297  0.6657 -0.0025 -0.0094 -0.0189 190  TYR A CE1   
1555 C  CE2   . TYR A 190 ? 0.2179 0.305  0.6711 -0.0031 -0.011  -0.015  190  TYR A CE2   
1556 C  CZ    . TYR A 190 ? 0.2233 0.3095 0.6781 -0.0039 -0.011  -0.0149 190  TYR A CZ    
1557 O  OH    . TYR A 190 ? 0.2322 0.3181 0.6894 -0.006  -0.0127 -0.0108 190  TYR A OH    
1558 N  N     . GLN A 191 ? 0.2367 0.3391 0.6914 0.0086  -0.0025 -0.0242 191  GLN A N     
1559 C  CA    . GLN A 191 ? 0.2496 0.358  0.7066 0.0105  -0.0017 -0.0204 191  GLN A CA    
1560 C  C     . GLN A 191 ? 0.2519 0.3615 0.7122 0.0097  -0.0016 -0.0171 191  GLN A C     
1561 O  O     . GLN A 191 ? 0.2466 0.3588 0.7081 0.0119  0       -0.0181 191  GLN A O     
1562 C  CB    . GLN A 191 ? 0.2851 0.3977 0.7413 0.0145  0.0004  -0.0233 191  GLN A CB    
1563 C  CG    . GLN A 191 ? 0.3559 0.4736 0.812  0.0166  0.0011  -0.021  191  GLN A CG    
1564 C  CD    . GLN A 191 ? 0.4353 0.5507 0.8893 0.0152  -0.0001 -0.0212 191  GLN A CD    
1565 O  OE1   . GLN A 191 ? 0.4621 0.5738 0.9133 0.0146  -0.0004 -0.0253 191  GLN A OE1   
1566 N  NE2   . GLN A 191 ? 0.4503 0.568  0.9057 0.0145  -0.0008 -0.0166 191  GLN A NE2   
1567 N  N     . PRO A 192 ? 0.2526 0.36   0.7143 0.0066  -0.0036 -0.0134 192  PRO A N     
1568 C  CA    . PRO A 192 ? 0.2549 0.363  0.7197 0.0055  -0.0038 -0.0104 192  PRO A CA    
1569 C  C     . PRO A 192 ? 0.2694 0.3842 0.7376 0.0078  -0.0023 -0.0063 192  PRO A C     
1570 O  O     . PRO A 192 ? 0.2698 0.3858 0.7404 0.0079  -0.0017 -0.0048 192  PRO A O     
1571 C  CB    . PRO A 192 ? 0.2586 0.3624 0.7235 0.0016  -0.0066 -0.0076 192  PRO A CB    
1572 C  CG    . PRO A 192 ? 0.2638 0.3668 0.7267 0.0012  -0.0076 -0.0073 192  PRO A CG    
1573 C  CD    . PRO A 192 ? 0.2467 0.3502 0.7068 0.0038  -0.0059 -0.0122 192  PRO A CD    
1574 N  N     . LYS A 193 ? 0.2765 0.3958 0.7449 0.0099  -0.0015 -0.0046 193  LYS A N     
1575 C  CA    . LYS A 193 ? 0.2841 0.4102 0.7555 0.0127  0.0001  -0.0007 193  LYS A CA    
1576 C  C     . LYS A 193 ? 0.2889 0.4175 0.7596 0.0165  0.0027  -0.004  193  LYS A C     
1577 O  O     . LYS A 193 ? 0.2929 0.4262 0.7659 0.0187  0.0042  -0.001  193  LYS A O     
1578 C  CB    . LYS A 193 ? 0.3146 0.445  0.7863 0.0143  0.0004  0.0019  193  LYS A CB    
1579 C  CG    . LYS A 193 ? 0.3814 0.5111 0.8555 0.011   -0.002  0.007   193  LYS A CG    
1580 C  CD    . LYS A 193 ? 0.4538 0.5818 0.9255 0.0104  -0.0029 0.006   193  LYS A CD    
1581 C  CE    . LYS A 193 ? 0.5038 0.6382 0.9771 0.0131  -0.0018 0.0095  193  LYS A CE    
1582 N  NZ    . LYS A 193 ? 0.5321 0.6651 1.0024 0.0133  -0.0021 0.0072  193  LYS A NZ    
1583 N  N     . TYR A 194 ? 0.2838 0.409  0.7513 0.0172  0.0031  -0.01   194  TYR A N     
1584 C  CA    . TYR A 194 ? 0.2916 0.4184 0.7581 0.0207  0.0052  -0.0136 194  TYR A CA    
1585 C  C     . TYR A 194 ? 0.2785 0.4011 0.7451 0.0195  0.0052  -0.0168 194  TYR A C     
1586 O  O     . TYR A 194 ? 0.2891 0.4124 0.755  0.0221  0.0067  -0.0201 194  TYR A O     
1587 C  CB    . TYR A 194 ? 0.3097 0.4369 0.7729 0.0231  0.0058  -0.0182 194  TYR A CB    
1588 C  CG    . TYR A 194 ? 0.3432 0.4754 0.8062 0.0252  0.0063  -0.0153 194  TYR A CG    
1589 C  CD1   . TYR A 194 ? 0.3678 0.5059 0.8315 0.0293  0.0082  -0.0134 194  TYR A CD1   
1590 C  CD2   . TYR A 194 ? 0.362  0.4929 0.8243 0.0231  0.0049  -0.0141 194  TYR A CD2   
1591 C  CE1   . TYR A 194 ? 0.3862 0.5293 0.8501 0.0314  0.0088  -0.0103 194  TYR A CE1   
1592 C  CE2   . TYR A 194 ? 0.3807 0.5163 0.8433 0.025   0.0054  -0.0111 194  TYR A CE2   
1593 C  CZ    . TYR A 194 ? 0.4009 0.5428 0.8644 0.0292  0.0074  -0.0092 194  TYR A CZ    
1594 O  OH    . TYR A 194 ? 0.4272 0.5741 0.8911 0.0312  0.0081  -0.006  194  TYR A OH    
1595 N  N     . ASP A 195 ? 0.2521 0.3702 0.7195 0.0156  0.0035  -0.0159 195  ASP A N     
1596 C  CA    . ASP A 195 ? 0.2272 0.3414 0.6948 0.0144  0.0035  -0.0186 195  ASP A CA    
1597 C  C     . ASP A 195 ? 0.2032 0.316  0.6733 0.0113  0.0022  -0.0146 195  ASP A C     
1598 O  O     . ASP A 195 ? 0.1996 0.3093 0.6693 0.0082  0.0002  -0.013  195  ASP A O     
1599 C  CB    . ASP A 195 ? 0.2377 0.3467 0.7025 0.0132  0.0027  -0.0237 195  ASP A CB    
1600 C  CG    . ASP A 195 ? 0.2518 0.3577 0.7169 0.0132  0.0033  -0.0274 195  ASP A CG    
1601 O  OD1   . ASP A 195 ? 0.2401 0.3457 0.7075 0.0123  0.0035  -0.0255 195  ASP A OD1   
1602 O  OD2   . ASP A 195 ? 0.2676 0.3715 0.7309 0.0141  0.0036  -0.032  195  ASP A OD2   
1603 N  N     . LYS A 196 ? 0.1871 0.3017 0.6596 0.0122  0.0034  -0.0131 196  LYS A N     
1604 C  CA    . LYS A 196 ? 0.1716 0.2855 0.6469 0.0095  0.0024  -0.0092 196  LYS A CA    
1605 C  C     . LYS A 196 ? 0.1433 0.251  0.6175 0.0064  0.0009  -0.0114 196  LYS A C     
1606 O  O     . LYS A 196 ? 0.1399 0.2461 0.6155 0.0035  -0.0008 -0.0081 196  LYS A O     
1607 C  CB    . LYS A 196 ? 0.2133 0.3309 0.6912 0.0118  0.0045  -0.0075 196  LYS A CB    
1608 C  CG    . LYS A 196 ? 0.2929 0.4169 0.7721 0.0148  0.0058  -0.0039 196  LYS A CG    
1609 C  CD    . LYS A 196 ? 0.3611 0.4887 0.8424 0.0176  0.0081  -0.0025 196  LYS A CD    
1610 C  CE    . LYS A 196 ? 0.4067 0.5409 0.8895 0.0205  0.0094  0.0021  196  LYS A CE    
1611 N  NZ    . LYS A 196 ? 0.4336 0.5695 0.9186 0.0179  0.0075  0.0075  196  LYS A NZ    
1612 N  N     . LYS A 197 ? 0.1243 0.2286 0.5963 0.0068  0.0013  -0.0166 197  LYS A N     
1613 C  CA    . LYS A 197 ? 0.1223 0.2208 0.5931 0.0042  0       -0.0186 197  LYS A CA    
1614 C  C     . LYS A 197 ? 0.1108 0.2061 0.5797 0.0013  -0.0025 -0.0172 197  LYS A C     
1615 O  O     . LYS A 197 ? 0.1097 0.2006 0.5779 -0.0011 -0.004  -0.0171 197  LYS A O     
1616 C  CB    . LYS A 197 ? 0.1437 0.2396 0.6127 0.0055  0.001   -0.0243 197  LYS A CB    
1617 C  CG    . LYS A 197 ? 0.198  0.2957 0.6689 0.0079  0.0031  -0.0261 197  LYS A CG    
1618 C  CD    . LYS A 197 ? 0.2598 0.3543 0.7297 0.0086  0.0037  -0.0314 197  LYS A CD    
1619 C  CE    . LYS A 197 ? 0.3134 0.4096 0.785  0.0111  0.0056  -0.0334 197  LYS A CE    
1620 N  NZ    . LYS A 197 ? 0.3629 0.4553 0.8354 0.0104  0.0058  -0.0366 197  LYS A NZ    
1621 N  N     . LEU A 198 ? 0.1002 0.1975 0.5681 0.0018  -0.003  -0.0159 198  LEU A N     
1622 C  CA    . LEU A 198 ? 0.0966 0.1908 0.5626 -0.0007 -0.0054 -0.0145 198  LEU A CA    
1623 C  C     . LEU A 198 ? 0.0946 0.1906 0.5631 -0.0026 -0.0071 -0.0088 198  LEU A C     
1624 O  O     . LEU A 198 ? 0.0936 0.1872 0.5607 -0.0046 -0.0092 -0.0073 198  LEU A O     
1625 C  CB    . LEU A 198 ? 0.0962 0.1912 0.5598 0.0007  -0.0051 -0.0166 198  LEU A CB    
1626 C  CG    . LEU A 198 ? 0.0922 0.1856 0.5535 0.0025  -0.0037 -0.0221 198  LEU A CG    
1627 C  CD1   . LEU A 198 ? 0.0944 0.1894 0.5536 0.0041  -0.0034 -0.0235 198  LEU A CD1   
1628 C  CD2   . LEU A 198 ? 0.095  0.1824 0.5544 0.0006  -0.0047 -0.0246 198  LEU A CD2   
1629 N  N     . LYS A 199 ? 0.0883 0.1883 0.5604 -0.002  -0.0062 -0.0055 199  LYS A N     
1630 C  CA    . LYS A 199 ? 0.0923 0.1947 0.5674 -0.0036 -0.0077 0.0004  199  LYS A CA    
1631 C  C     . LYS A 199 ? 0.0783 0.1757 0.5527 -0.0074 -0.0109 0.0021  199  LYS A C     
1632 O  O     . LYS A 199 ? 0.0787 0.1766 0.5541 -0.0091 -0.013  0.0057  199  LYS A O     
1633 C  CB    . LYS A 199 ? 0.1172 0.224  0.5961 -0.0024 -0.0061 0.0032  199  LYS A CB    
1634 C  CG    . LYS A 199 ? 0.1866 0.2976 0.6694 -0.0034 -0.0072 0.0096  199  LYS A CG    
1635 C  CD    . LYS A 199 ? 0.2603 0.3752 0.7467 -0.0024 -0.0057 0.0128  199  LYS A CD    
1636 C  CE    . LYS A 199 ? 0.3243 0.443  0.8149 -0.0039 -0.0072 0.0196  199  LYS A CE    
1637 N  NZ    . LYS A 199 ? 0.371  0.4927 0.8652 -0.0037 -0.0062 0.0229  199  LYS A NZ    
1638 N  N     . PHE A 200 ? 0.0663 0.1589 0.5389 -0.0087 -0.0115 -0.0006 200  PHE A N     
1639 C  CA    . PHE A 200 ? 0.0703 0.1578 0.5417 -0.0121 -0.0146 0.0007  200  PHE A CA    
1640 C  C     . PHE A 200 ? 0.0693 0.1509 0.536  -0.0129 -0.0159 -0.0029 200  PHE A C     
1641 O  O     . PHE A 200 ? 0.0716 0.148  0.5364 -0.0151 -0.018  -0.0032 200  PHE A O     
1642 C  CB    . PHE A 200 ? 0.0739 0.1603 0.5469 -0.0131 -0.0147 0.0014  200  PHE A CB    
1643 C  CG    . PHE A 200 ? 0.0813 0.1736 0.5591 -0.0125 -0.0137 0.0058  200  PHE A CG    
1644 C  CD1   . PHE A 200 ? 0.0972 0.1921 0.5778 -0.014  -0.0155 0.0111  200  PHE A CD1   
1645 C  CD2   . PHE A 200 ? 0.0942 0.1897 0.5739 -0.0101 -0.0107 0.0047  200  PHE A CD2   
1646 C  CE1   . PHE A 200 ? 0.1054 0.2061 0.5905 -0.0132 -0.0144 0.0154  200  PHE A CE1   
1647 C  CE2   . PHE A 200 ? 0.1008 0.202  0.5847 -0.0092 -0.0096 0.0088  200  PHE A CE2   
1648 C  CZ    . PHE A 200 ? 0.0979 0.2018 0.5845 -0.0107 -0.0114 0.0143  200  PHE A CZ    
1649 N  N     . PHE A 201 ? 0.064  0.1461 0.5286 -0.0111 -0.0147 -0.0056 201  PHE A N     
1650 C  CA    . PHE A 201 ? 0.0758 0.1525 0.5359 -0.0118 -0.0157 -0.0088 201  PHE A CA    
1651 C  C     . PHE A 201 ? 0.0927 0.1668 0.5515 -0.0141 -0.0188 -0.006  201  PHE A C     
1652 O  O     . PHE A 201 ? 0.1104 0.1883 0.5715 -0.014  -0.0191 -0.0028 201  PHE A O     
1653 C  CB    . PHE A 201 ? 0.0615 0.1396 0.5198 -0.0092 -0.0135 -0.0127 201  PHE A CB    
1654 C  CG    . PHE A 201 ? 0.0554 0.1279 0.5092 -0.0097 -0.0144 -0.016  201  PHE A CG    
1655 C  CD1   . PHE A 201 ? 0.0623 0.1304 0.5141 -0.0102 -0.0144 -0.0187 201  PHE A CD1   
1656 C  CD2   . PHE A 201 ? 0.0566 0.1283 0.508  -0.0097 -0.0152 -0.0161 201  PHE A CD2   
1657 C  CE1   . PHE A 201 ? 0.072  0.1352 0.5197 -0.0104 -0.015  -0.0215 201  PHE A CE1   
1658 C  CE2   . PHE A 201 ? 0.0645 0.1311 0.5116 -0.01   -0.0158 -0.019  201  PHE A CE2   
1659 C  CZ    . PHE A 201 ? 0.0662 0.1285 0.5114 -0.0103 -0.0158 -0.0216 201  PHE A CZ    
1660 N  N     . ASP A 202 ? 0.0813 0.149  0.5366 -0.016  -0.021  -0.0071 202  ASP A N     
1661 C  CA    . ASP A 202 ? 0.0766 0.1408 0.5303 -0.0182 -0.0243 -0.0048 202  ASP A CA    
1662 C  C     . ASP A 202 ? 0.0683 0.1306 0.5182 -0.0171 -0.0238 -0.0076 202  ASP A C     
1663 O  O     . ASP A 202 ? 0.0528 0.1109 0.4989 -0.0166 -0.0234 -0.0113 202  ASP A O     
1664 C  CB    . ASP A 202 ? 0.0942 0.1521 0.5454 -0.0205 -0.027  -0.0047 202  ASP A CB    
1665 C  CG    . ASP A 202 ? 0.154  0.2079 0.6037 -0.023  -0.0308 -0.002  202  ASP A CG    
1666 O  OD1   . ASP A 202 ? 0.1693 0.2235 0.6185 -0.023  -0.0313 -0.0014 202  ASP A OD1   
1667 O  OD2   . ASP A 202 ? 0.1709 0.2209 0.6199 -0.0251 -0.0335 -0.0008 202  ASP A OD2   
1668 N  N     . GLU A 203 ? 0.072  0.1376 0.5232 -0.0166 -0.0237 -0.0056 203  GLU A N     
1669 C  CA    . GLU A 203 ? 0.0826 0.1469 0.5305 -0.0155 -0.0231 -0.0081 203  GLU A CA    
1670 C  C     . GLU A 203 ? 0.084  0.1409 0.5272 -0.0172 -0.0257 -0.009  203  GLU A C     
1671 O  O     . GLU A 203 ? 0.1081 0.1631 0.5478 -0.0161 -0.025  -0.0117 203  GLU A O     
1672 C  CB    . GLU A 203 ? 0.1236 0.1935 0.5742 -0.0144 -0.0224 -0.0055 203  GLU A CB    
1673 C  CG    . GLU A 203 ? 0.1977 0.2745 0.6515 -0.0117 -0.0192 -0.006  203  GLU A CG    
1674 C  CD    . GLU A 203 ? 0.2731 0.3563 0.73   -0.0102 -0.0181 -0.003  203  GLU A CD    
1675 O  OE1   . GLU A 203 ? 0.2613 0.3437 0.7174 -0.011  -0.0195 -0.0013 203  GLU A OE1   
1676 O  OE2   . GLU A 203 ? 0.3076 0.3965 0.7674 -0.0081 -0.0159 -0.0024 203  GLU A OE2   
1677 N  N     . THR A 204 ? 0.0664 0.1188 0.5089 -0.0197 -0.0288 -0.0071 204  THR A N     
1678 C  CA    . THR A 204 ? 0.0624 0.1071 0.4995 -0.021  -0.0312 -0.0085 204  THR A CA    
1679 C  C     . THR A 204 ? 0.0691 0.11   0.5022 -0.0197 -0.0298 -0.0129 204  THR A C     
1680 O  O     . THR A 204 ? 0.0793 0.1139 0.5075 -0.0201 -0.0313 -0.0144 204  THR A O     
1681 C  CB    . THR A 204 ? 0.0636 0.1043 0.5009 -0.0238 -0.0352 -0.0052 204  THR A CB    
1682 O  OG1   . THR A 204 ? 0.0852 0.1262 0.5241 -0.0245 -0.0353 -0.0049 204  THR A OG1   
1683 C  CG2   . THR A 204 ? 0.0536 0.0979 0.495  -0.0251 -0.0367 -0.0008 204  THR A CG2   
1684 N  N     . ILE A 205 ? 0.0598 0.1044 0.4951 -0.018  -0.0269 -0.0147 205  ILE A N     
1685 C  CA    . ILE A 205 ? 0.0629 0.1049 0.4953 -0.0166 -0.0253 -0.0186 205  ILE A CA    
1686 C  C     . ILE A 205 ? 0.0725 0.114  0.502  -0.0148 -0.0237 -0.0215 205  ILE A C     
1687 O  O     . ILE A 205 ? 0.0842 0.1214 0.5097 -0.0142 -0.0234 -0.0242 205  ILE A O     
1688 C  CB    . ILE A 205 ? 0.0565 0.103  0.4929 -0.0154 -0.0227 -0.0195 205  ILE A CB    
1689 C  CG1   . ILE A 205 ? 0.0538 0.0999 0.4924 -0.0171 -0.0242 -0.0169 205  ILE A CG1   
1690 C  CG2   . ILE A 205 ? 0.0614 0.1066 0.496  -0.0136 -0.0205 -0.0235 205  ILE A CG2   
1691 C  CD1   . ILE A 205 ? 0.0611 0.1121 0.504  -0.0161 -0.0219 -0.0169 205  ILE A CD1   
1692 N  N     . PHE A 206 ? 0.0648 0.1109 0.4962 -0.014  -0.0227 -0.0207 206  PHE A N     
1693 C  CA    . PHE A 206 ? 0.0749 0.121  0.5036 -0.0124 -0.0213 -0.0232 206  PHE A CA    
1694 C  C     . PHE A 206 ? 0.0871 0.1265 0.5106 -0.0132 -0.0234 -0.0236 206  PHE A C     
1695 O  O     . PHE A 206 ? 0.0671 0.1036 0.4896 -0.0151 -0.0261 -0.0209 206  PHE A O     
1696 C  CB    . PHE A 206 ? 0.0712 0.1233 0.5028 -0.0114 -0.0203 -0.0217 206  PHE A CB    
1697 C  CG    . PHE A 206 ? 0.0756 0.1342 0.5115 -0.0099 -0.018  -0.0219 206  PHE A CG    
1698 C  CD1   . PHE A 206 ? 0.0865 0.1461 0.5227 -0.0083 -0.0159 -0.0253 206  PHE A CD1   
1699 C  CD2   . PHE A 206 ? 0.0746 0.1385 0.5145 -0.0098 -0.0179 -0.0186 206  PHE A CD2   
1700 C  CE1   . PHE A 206 ? 0.09   0.1553 0.5299 -0.0067 -0.0138 -0.0256 206  PHE A CE1   
1701 C  CE2   . PHE A 206 ? 0.073  0.1428 0.5164 -0.008  -0.0157 -0.0188 206  PHE A CE2   
1702 C  CZ    . PHE A 206 ? 0.0761 0.1464 0.5193 -0.0064 -0.0137 -0.0224 206  PHE A CZ    
1703 N  N     . ALA A 207 ? 0.1077 0.1444 0.5276 -0.0118 -0.0221 -0.0268 207  ALA A N     
1704 C  CA    . ALA A 207 ? 0.1432 0.1732 0.5576 -0.0122 -0.0237 -0.0275 207  ALA A CA    
1705 C  C     . ALA A 207 ? 0.1845 0.2147 0.597  -0.0116 -0.0237 -0.0273 207  ALA A C     
1706 O  O     . ALA A 207 ? 0.2216 0.249  0.6301 -0.0104 -0.0228 -0.0295 207  ALA A O     
1707 C  CB    . ALA A 207 ? 0.1439 0.1708 0.5554 -0.0108 -0.0223 -0.0306 207  ALA A CB    
1708 N  N     . ASP A 208 ? 0.1208 0.146  0.5273 -0.0125 -0.0268 -0.0241 209  ASP A N     
1709 C  CA    . ASP A 208 ? 0.1258 0.145  0.5264 -0.012  -0.0275 -0.0254 209  ASP A CA    
1710 C  C     . ASP A 208 ? 0.1191 0.1312 0.5151 -0.0122 -0.0287 -0.0268 209  ASP A C     
1711 O  O     . ASP A 208 ? 0.1256 0.1324 0.5162 -0.0114 -0.029  -0.028  209  ASP A O     
1712 C  CB    . ASP A 208 ? 0.1415 0.1586 0.5413 -0.0132 -0.0297 -0.0228 209  ASP A CB    
1713 N  N     . ASP A 209 ? 0.107  0.1189 0.5047 -0.013  -0.0293 -0.0267 210  ASP A N     
1714 C  CA    . ASP A 209 ? 0.1076 0.113  0.5008 -0.013  -0.0305 -0.0279 210  ASP A CA    
1715 C  C     . ASP A 209 ? 0.1062 0.11   0.4959 -0.0106 -0.028  -0.0309 210  ASP A C     
1716 O  O     . ASP A 209 ? 0.112  0.1093 0.4961 -0.01   -0.0291 -0.0317 210  ASP A O     
1717 C  CB    . ASP A 209 ? 0.1307 0.137  0.5269 -0.0142 -0.0314 -0.0269 210  ASP A CB    
1718 C  CG    . ASP A 209 ? 0.1787 0.1834 0.5764 -0.0168 -0.0349 -0.0238 210  ASP A CG    
1719 O  OD1   . ASP A 209 ? 0.1876 0.1884 0.5827 -0.0177 -0.0372 -0.0225 210  ASP A OD1   
1720 O  OD2   . ASP A 209 ? 0.1944 0.2016 0.5959 -0.0179 -0.0353 -0.0224 210  ASP A OD2   
1721 N  N     . ILE A 210 ? 0.0921 0.1019 0.4852 -0.0091 -0.0249 -0.0325 211  ILE A N     
1722 C  CA    . ILE A 210 ? 0.0881 0.0972 0.4789 -0.0069 -0.0225 -0.0352 211  ILE A CA    
1723 C  C     . ILE A 210 ? 0.0989 0.1051 0.485  -0.0058 -0.0224 -0.0357 211  ILE A C     
1724 O  O     . ILE A 210 ? 0.1025 0.1038 0.4837 -0.0046 -0.0222 -0.0367 211  ILE A O     
1725 C  CB    . ILE A 210 ? 0.09   0.1061 0.4859 -0.0059 -0.0196 -0.0367 211  ILE A CB    
1726 C  CG1   . ILE A 210 ? 0.0967 0.1141 0.496  -0.0065 -0.0196 -0.0367 211  ILE A CG1   
1727 C  CG2   . ILE A 210 ? 0.0959 0.1122 0.4901 -0.0037 -0.0173 -0.0392 211  ILE A CG2   
1728 C  CD1   . ILE A 210 ? 0.1091 0.1213 0.5052 -0.0059 -0.0198 -0.0375 211  ILE A CD1   
1729 N  N     . ALA A 211 ? 0.0867 0.0958 0.4742 -0.0062 -0.0225 -0.0346 212  ALA A N     
1730 C  CA    . ALA A 211 ? 0.0747 0.0812 0.458  -0.0053 -0.0223 -0.0348 212  ALA A CA    
1731 C  C     . ALA A 211 ? 0.0679 0.0659 0.4453 -0.006  -0.0252 -0.0338 212  ALA A C     
1732 O  O     . ALA A 211 ? 0.057  0.0505 0.4292 -0.0046 -0.0249 -0.0348 212  ALA A O     
1733 C  CB    . ALA A 211 ? 0.069  0.0806 0.4554 -0.0056 -0.0219 -0.0335 212  ALA A CB    
1734 N  N     . ASP A 212 ? 0.0774 0.0731 0.4556 -0.0081 -0.0281 -0.0319 213  ASP A N     
1735 C  CA    . ASP A 212 ? 0.0914 0.0787 0.464  -0.0089 -0.0313 -0.0311 213  ASP A CA    
1736 C  C     . ASP A 212 ? 0.0795 0.0616 0.4472 -0.0074 -0.031  -0.0329 213  ASP A C     
1737 O  O     . ASP A 212 ? 0.0765 0.0519 0.4377 -0.0064 -0.032  -0.0333 213  ASP A O     
1738 C  CB    . ASP A 212 ? 0.1376 0.1241 0.5128 -0.0116 -0.0345 -0.0288 213  ASP A CB    
1739 C  CG    . ASP A 212 ? 0.2247 0.2144 0.6038 -0.0133 -0.0357 -0.0262 213  ASP A CG    
1740 O  OD1   . ASP A 212 ? 0.2359 0.228  0.6151 -0.0124 -0.0342 -0.0263 213  ASP A OD1   
1741 O  OD2   . ASP A 212 ? 0.2809 0.2711 0.6632 -0.0155 -0.038  -0.024  213  ASP A OD2   
1742 N  N     . TYR A 213 ? 0.0631 0.0483 0.4337 -0.007  -0.0295 -0.0338 214  TYR A N     
1743 C  CA    . TYR A 213 ? 0.0751 0.0562 0.4418 -0.0054 -0.0289 -0.0352 214  TYR A CA    
1744 C  C     . TYR A 213 ? 0.0697 0.0498 0.4328 -0.0028 -0.0264 -0.0368 214  TYR A C     
1745 O  O     . TYR A 213 ? 0.0601 0.0432 0.4167 0       -0.0269 -0.0362 214  TYR A O     
1746 C  CB    . TYR A 213 ? 0.0832 0.0689 0.455  -0.0055 -0.0274 -0.0357 214  TYR A CB    
1747 C  CG    . TYR A 213 ? 0.0945 0.077  0.4632 -0.0036 -0.0263 -0.037  214  TYR A CG    
1748 C  CD1   . TYR A 213 ? 0.1092 0.0851 0.4731 -0.0036 -0.0286 -0.0365 214  TYR A CD1   
1749 C  CD2   . TYR A 213 ? 0.1043 0.0903 0.4746 -0.0016 -0.023  -0.0386 214  TYR A CD2   
1750 C  CE1   . TYR A 213 ? 0.1245 0.0979 0.4856 -0.0015 -0.0274 -0.0375 214  TYR A CE1   
1751 C  CE2   . TYR A 213 ? 0.1119 0.0954 0.4799 0.0003  -0.0219 -0.0394 214  TYR A CE2   
1752 C  CZ    . TYR A 213 ? 0.1332 0.1104 0.4965 0.0004  -0.0239 -0.0387 214  TYR A CZ    
1753 O  OH    . TYR A 213 ? 0.1566 0.1314 0.5174 0.0026  -0.0227 -0.0393 214  TYR A OH    
1754 N  N     . ILE A 214 ? 0.0745 0.0611 0.4417 -0.0021 -0.0237 -0.0376 215  ILE A N     
1755 C  CA    . ILE A 214 ? 0.0822 0.0688 0.4468 0.0003  -0.0212 -0.0389 215  ILE A CA    
1756 C  C     . ILE A 214 ? 0.1092 0.0899 0.4673 0.001   -0.0225 -0.0384 215  ILE A C     
1757 O  O     . ILE A 214 ? 0.1171 0.0932 0.4698 0.003   -0.0218 -0.0391 215  ILE A O     
1758 C  CB    . ILE A 214 ? 0.0773 0.072  0.4475 0.0007  -0.0186 -0.0398 215  ILE A CB    
1759 C  CG1   . ILE A 214 ? 0.091  0.0906 0.4667 0.0006  -0.0171 -0.0408 215  ILE A CG1   
1760 C  CG2   . ILE A 214 ? 0.0805 0.0755 0.448  0.0028  -0.0165 -0.0407 215  ILE A CG2   
1761 C  CD1   . ILE A 214 ? 0.0957 0.103  0.477  0.0009  -0.0149 -0.0418 215  ILE A CD1   
1762 N  N     . ILE A 215 ? 0.1114 0.0921 0.47   -0.0007 -0.0242 -0.0371 216  ILE A N     
1763 C  CA    . ILE A 215 ? 0.1199 0.0951 0.4729 -0.0002 -0.0256 -0.0365 216  ILE A CA    
1764 C  C     . ILE A 215 ? 0.1204 0.0865 0.4666 0       -0.0282 -0.0363 216  ILE A C     
1765 O  O     . ILE A 215 ? 0.116  0.0767 0.4559 0.0019  -0.0282 -0.0367 216  ILE A O     
1766 C  CB    . ILE A 215 ? 0.13   0.1079 0.4862 -0.0022 -0.0269 -0.0348 216  ILE A CB    
1767 C  CG1   . ILE A 215 ? 0.1503 0.1367 0.5115 -0.0015 -0.0239 -0.0353 216  ILE A CG1   
1768 C  CG2   . ILE A 215 ? 0.1248 0.0956 0.4751 -0.0022 -0.0291 -0.0338 216  ILE A CG2   
1769 C  CD1   . ILE A 215 ? 0.1643 0.1549 0.5298 -0.0031 -0.0246 -0.0336 216  ILE A CD1   
1770 N  N     . ALA A 216 ? 0.1148 0.0791 0.4621 -0.0016 -0.0305 -0.0357 217  ALA A N     
1771 C  CA    . ALA A 216 ? 0.1219 0.0773 0.4623 -0.0012 -0.0333 -0.0357 217  ALA A CA    
1772 C  C     . ALA A 216 ? 0.1329 0.0856 0.4688 0.0019  -0.0312 -0.0371 217  ALA A C     
1773 O  O     . ALA A 216 ? 0.139  0.0843 0.4674 0.0036  -0.0323 -0.0374 217  ALA A O     
1774 C  CB    . ALA A 216 ? 0.1129 0.0676 0.4558 -0.0036 -0.0362 -0.0346 217  ALA A CB    
1775 N  N     . LYS A 217 ? 0.1242 0.0832 0.4648 0.0028  -0.0281 -0.0379 218  LYS A N     
1776 C  CA    . LYS A 217 ? 0.1296 0.0873 0.4673 0.0057  -0.0257 -0.039  218  LYS A CA    
1777 C  C     . LYS A 217 ? 0.1403 0.0965 0.4738 0.008   -0.0239 -0.0393 218  LYS A C     
1778 O  O     . LYS A 217 ? 0.159  0.1093 0.4858 0.0104  -0.0238 -0.0395 218  LYS A O     
1779 C  CB    . LYS A 217 ? 0.1272 0.0921 0.4717 0.0059  -0.023  -0.0396 218  LYS A CB    
1780 C  CG    . LYS A 217 ? 0.1729 0.1388 0.5208 0.0041  -0.0244 -0.0392 218  LYS A CG    
1781 C  CD    . LYS A 217 ? 0.2141 0.1731 0.5562 0.0053  -0.026  -0.039  218  LYS A CD    
1782 C  CE    . LYS A 217 ? 0.2401 0.1998 0.582  0.0078  -0.0234 -0.0396 218  LYS A CE    
1783 N  NZ    . LYS A 217 ? 0.2668 0.2226 0.6064 0.0081  -0.025  -0.0393 218  LYS A NZ    
1784 N  N     . LEU A 218 ? 0.1268 0.0881 0.4639 0.0073  -0.0226 -0.0393 219  LEU A N     
1785 C  CA    . LEU A 218 ? 0.119  0.0795 0.4526 0.0093  -0.0209 -0.0395 219  LEU A CA    
1786 C  C     . LEU A 218 ? 0.1365 0.0883 0.462  0.01    -0.0232 -0.0389 219  LEU A C     
1787 O  O     . LEU A 218 ? 0.146  0.0942 0.4659 0.0127  -0.022  -0.0391 219  LEU A O     
1788 C  CB    . LEU A 218 ? 0.1063 0.0739 0.4454 0.0082  -0.0195 -0.0395 219  LEU A CB    
1789 C  CG    . LEU A 218 ? 0.1187 0.095  0.4653 0.008   -0.0169 -0.0404 219  LEU A CG    
1790 C  CD1   . LEU A 218 ? 0.1204 0.1033 0.4718 0.0071  -0.0159 -0.0403 219  LEU A CD1   
1791 C  CD2   . LEU A 218 ? 0.1126 0.0896 0.4584 0.0105  -0.0142 -0.0412 219  LEU A CD2   
1792 N  N     . GLN A 219 ? 0.1331 0.0813 0.4578 0.0077  -0.0268 -0.0381 220  GLN A N     
1793 C  CA    . GLN A 219 ? 0.1395 0.0788 0.4568 0.008   -0.0296 -0.0377 220  GLN A CA    
1794 C  C     . GLN A 219 ? 0.1681 0.0995 0.4785 0.0097  -0.0313 -0.0381 220  GLN A C     
1795 O  O     . GLN A 219 ? 0.1829 0.1062 0.4864 0.0101  -0.034  -0.0379 220  GLN A O     
1796 C  CB    . GLN A 219 ? 0.1369 0.0756 0.4567 0.0047  -0.033  -0.0365 220  GLN A CB    
1797 C  CG    . GLN A 219 ? 0.1594 0.1045 0.4846 0.0034  -0.0318 -0.0357 220  GLN A CG    
1798 C  CD    . GLN A 219 ? 0.2271 0.1684 0.5474 0.0047  -0.0316 -0.0355 220  GLN A CD    
1799 O  OE1   . GLN A 219 ? 0.2729 0.2087 0.5863 0.0074  -0.0309 -0.0362 220  GLN A OE1   
1800 N  NE2   . GLN A 219 ? 0.2079 0.1521 0.5317 0.003   -0.0322 -0.0342 220  GLN A NE2   
1801 N  N     . HIS A 220 ? 0.1837 0.1172 0.4958 0.0105  -0.03   -0.0386 221  HIS A N     
1802 C  CA    . HIS A 220 ? 0.2077 0.1346 0.5139 0.0122  -0.0315 -0.0389 221  HIS A CA    
1803 C  C     . HIS A 220 ? 0.1887 0.1098 0.4926 0.0098  -0.0362 -0.0384 221  HIS A C     
1804 O  O     . HIS A 220 ? 0.1854 0.098  0.4815 0.0112  -0.0386 -0.0387 221  HIS A O     
1805 C  CB    . HIS A 220 ? 0.2686 0.1894 0.5661 0.0162  -0.0302 -0.0392 221  HIS A CB    
1806 C  CG    . HIS A 220 ? 0.3683 0.2839 0.6604 0.0187  -0.0307 -0.0395 221  HIS A CG    
1807 N  ND1   . HIS A 220 ? 0.4059 0.3262 0.7023 0.0193  -0.0286 -0.0395 221  HIS A ND1   
1808 C  CD2   . HIS A 220 ? 0.4076 0.3137 0.6905 0.0206  -0.0332 -0.0397 221  HIS A CD2   
1809 C  CE1   . HIS A 220 ? 0.4247 0.3387 0.7145 0.0216  -0.0297 -0.0396 221  HIS A CE1   
1810 N  NE2   . HIS A 220 ? 0.4302 0.3355 0.7116 0.0226  -0.0325 -0.0397 221  HIS A NE2   
1811 N  N     . ARG A 221 ? 0.174  0.1    0.4851 0.0063  -0.0375 -0.0377 222  ARG A N     
1812 C  CA    . ARG A 221 ? 0.1811 0.1031 0.4919 0.0036  -0.042  -0.0369 222  ARG A CA    
1813 C  C     . ARG A 221 ? 0.1926 0.1169 0.5069 0.0025  -0.0426 -0.0368 222  ARG A C     
1814 O  O     . ARG A 221 ? 0.1956 0.1257 0.5139 0.0035  -0.0394 -0.0372 222  ARG A O     
1815 C  CB    . ARG A 221 ? 0.1737 0.0993 0.4899 0.0004  -0.0433 -0.0356 222  ARG A CB    
1816 C  CG    . ARG A 221 ? 0.1864 0.1077 0.498  0.0012  -0.0438 -0.0355 222  ARG A CG    
1817 C  CD    . ARG A 221 ? 0.1943 0.1202 0.5117 -0.0014 -0.0443 -0.0341 222  ARG A CD    
1818 N  NE    . ARG A 221 ? 0.2319 0.1538 0.5446 -0.0002 -0.0443 -0.034  222  ARG A NE    
1819 C  CZ    . ARG A 221 ? 0.2386 0.1646 0.5553 -0.0014 -0.0437 -0.0329 222  ARG A CZ    
1820 N  NH1   . ARG A 221 ? 0.2457 0.1799 0.5709 -0.0037 -0.043  -0.0318 222  ARG A NH1   
1821 N  NH2   . ARG A 221 ? 0.2228 0.1447 0.5348 -0.0002 -0.0436 -0.0329 222  ARG A NH2   
1822 N  N     . ASP A 222 ? 0.2021 0.1216 0.5147 0.0006  -0.0468 -0.0361 223  ASP A N     
1823 C  CA    . ASP A 222 ? 0.2061 0.1273 0.5219 -0.0006 -0.0479 -0.0358 223  ASP A CA    
1824 C  C     . ASP A 222 ? 0.197  0.128  0.5232 -0.0034 -0.0464 -0.0347 223  ASP A C     
1825 O  O     . ASP A 222 ? 0.1994 0.1325 0.5294 -0.0059 -0.0479 -0.0335 223  ASP A O     
1826 C  CB    . ASP A 222 ? 0.2367 0.15   0.5479 -0.0021 -0.0532 -0.0352 223  ASP A CB    
1827 C  CG    . ASP A 222 ? 0.3254 0.2395 0.6391 -0.0036 -0.055  -0.0347 223  ASP A CG    
1828 O  OD1   . ASP A 222 ? 0.3756 0.2845 0.6872 -0.0055 -0.0596 -0.034  223  ASP A OD1   
1829 O  OD2   . ASP A 222 ? 0.3233 0.2434 0.6414 -0.0029 -0.052  -0.0349 223  ASP A OD2   
1830 N  N     . THR A 223 ? 0.1814 0.1181 0.5119 -0.0026 -0.0434 -0.0352 224  THR A N     
1831 C  CA    . THR A 223 ? 0.1835 0.1292 0.5232 -0.0046 -0.0417 -0.0344 224  THR A CA    
1832 C  C     . THR A 223 ? 0.1867 0.134  0.5301 -0.0064 -0.0433 -0.0336 224  THR A C     
1833 O  O     . THR A 223 ? 0.1771 0.1317 0.5278 -0.0077 -0.0416 -0.033  224  THR A O     
1834 C  CB    . THR A 223 ? 0.1955 0.1477 0.5388 -0.0027 -0.037  -0.0356 224  THR A CB    
1835 O  OG1   . THR A 223 ? 0.1989 0.1489 0.539  -0.0001 -0.0354 -0.0366 224  THR A OG1   
1836 C  CG2   . THR A 223 ? 0.2045 0.1571 0.5461 -0.0014 -0.0352 -0.0362 224  THR A CG2   
1837 N  N     . SER A 224 ? 0.1989 0.1395 0.537  -0.0062 -0.0462 -0.0335 225  SER A N     
1838 C  CA    . SER A 224 ? 0.2083 0.1501 0.5494 -0.0077 -0.0478 -0.0326 225  SER A CA    
1839 C  C     . SER A 224 ? 0.1911 0.1381 0.5396 -0.0112 -0.0492 -0.0307 225  SER A C     
1840 O  O     . SER A 224 ? 0.1935 0.1462 0.548  -0.0121 -0.048  -0.03   225  SER A O     
1841 C  CB    . SER A 224 ? 0.2655 0.1984 0.5992 -0.0073 -0.0518 -0.0326 225  SER A CB    
1842 O  OG    . SER A 224 ? 0.3486 0.2758 0.6744 -0.0038 -0.0508 -0.0342 225  SER A OG    
1843 N  N     . ASN A 225 ? 0.1843 0.1295 0.5327 -0.0131 -0.0518 -0.0295 226  ASN A N     
1844 C  CA    . ASN A 225 ? 0.1736 0.1233 0.5288 -0.0164 -0.0534 -0.0272 226  ASN A CA    
1845 C  C     . ASN A 225 ? 0.1413 0.1006 0.5041 -0.0165 -0.0495 -0.0269 226  ASN A C     
1846 O  O     . ASN A 225 ? 0.1353 0.1002 0.5045 -0.0181 -0.0492 -0.0255 226  ASN A O     
1847 C  CB    . ASN A 225 ? 0.2056 0.15   0.5583 -0.0183 -0.0576 -0.0259 226  ASN A CB    
1848 C  CG    . ASN A 225 ? 0.2836 0.2189 0.6295 -0.0185 -0.062  -0.0261 226  ASN A CG    
1849 O  OD1   . ASN A 225 ? 0.3035 0.238  0.6491 -0.0185 -0.0629 -0.0261 226  ASN A OD1   
1850 N  ND2   . ASN A 225 ? 0.3309 0.2589 0.6711 -0.0185 -0.065  -0.0263 226  ASN A ND2   
1851 N  N     . ILE A 226 ? 0.12   0.0809 0.4818 -0.0146 -0.0466 -0.0283 227  ILE A N     
1852 C  CA    . ILE A 226 ? 0.1108 0.0805 0.4792 -0.0143 -0.0428 -0.0285 227  ILE A CA    
1853 C  C     . ILE A 226 ? 0.0999 0.0739 0.4716 -0.0132 -0.04   -0.0295 227  ILE A C     
1854 O  O     . ILE A 226 ? 0.0985 0.0795 0.4768 -0.014  -0.0383 -0.0289 227  ILE A O     
1855 C  CB    . ILE A 226 ? 0.1177 0.0877 0.4837 -0.0123 -0.0404 -0.0299 227  ILE A CB    
1856 C  CG1   . ILE A 226 ? 0.1407 0.1065 0.5038 -0.0134 -0.0431 -0.0288 227  ILE A CG1   
1857 C  CG2   . ILE A 226 ? 0.1139 0.0927 0.4864 -0.012  -0.0368 -0.0302 227  ILE A CG2   
1858 C  CD1   . ILE A 226 ? 0.1554 0.1189 0.5138 -0.0112 -0.0413 -0.0302 227  ILE A CD1   
1859 N  N     . GLU A 227 ? 0.0981 0.0677 0.465  -0.0114 -0.0397 -0.0309 228  GLU A N     
1860 C  CA    . GLU A 227 ? 0.0981 0.0711 0.468  -0.0103 -0.0372 -0.0317 228  GLU A CA    
1861 C  C     . GLU A 227 ? 0.1146 0.0904 0.4893 -0.0125 -0.0387 -0.03   228  GLU A C     
1862 O  O     . GLU A 227 ? 0.1264 0.1085 0.507  -0.0127 -0.0364 -0.0299 228  GLU A O     
1863 C  CB    . GLU A 227 ? 0.1079 0.075  0.4714 -0.0079 -0.0371 -0.033  228  GLU A CB    
1864 C  CG    . GLU A 227 ? 0.1696 0.1354 0.5293 -0.0052 -0.0346 -0.0347 228  GLU A CG    
1865 C  CD    . GLU A 227 ? 0.2196 0.1787 0.572  -0.0025 -0.0348 -0.0355 228  GLU A CD    
1866 O  OE1   . GLU A 227 ? 0.2475 0.2046 0.5988 -0.0023 -0.0357 -0.0352 228  GLU A OE1   
1867 O  OE2   . GLU A 227 ? 0.2237 0.1796 0.5712 -0.0006 -0.0339 -0.0363 228  GLU A OE2   
1868 N  N     . GLN A 228 ? 0.1151 0.0861 0.4873 -0.0144 -0.0428 -0.0284 229  GLN A N     
1869 C  CA    . GLN A 228 ? 0.1225 0.096  0.4992 -0.0166 -0.0445 -0.0264 229  GLN A CA    
1870 C  C     . GLN A 228 ? 0.1201 0.1011 0.5044 -0.0184 -0.0435 -0.0247 229  GLN A C     
1871 O  O     . GLN A 228 ? 0.1254 0.1115 0.5151 -0.019  -0.0424 -0.0238 229  GLN A O     
1872 C  CB    . GLN A 228 ? 0.1513 0.1181 0.524  -0.0184 -0.0495 -0.025  229  GLN A CB    
1873 C  CG    . GLN A 228 ? 0.21   0.179  0.5869 -0.0203 -0.051  -0.0231 229  GLN A CG    
1874 C  CD    . GLN A 228 ? 0.2856 0.2562 0.6629 -0.0185 -0.0484 -0.0243 229  GLN A CD    
1875 O  OE1   . GLN A 228 ? 0.3323 0.2975 0.7035 -0.0165 -0.0488 -0.0257 229  GLN A OE1   
1876 N  NE2   . GLN A 228 ? 0.2706 0.2487 0.6549 -0.0188 -0.0457 -0.0237 229  GLN A NE2   
1877 N  N     . LEU A 229 ? 0.1082 0.0902 0.493  -0.0188 -0.0437 -0.0243 230  LEU A N     
1878 C  CA    . LEU A 229 ? 0.1004 0.0898 0.4921 -0.0201 -0.0426 -0.0226 230  LEU A CA    
1879 C  C     . LEU A 229 ? 0.0924 0.0884 0.4883 -0.0184 -0.0382 -0.0241 230  LEU A C     
1880 O  O     . LEU A 229 ? 0.0942 0.0963 0.4961 -0.0191 -0.0372 -0.0228 230  LEU A O     
1881 C  CB    . LEU A 229 ? 0.0999 0.0889 0.4909 -0.0206 -0.0434 -0.0218 230  LEU A CB    
1882 C  CG    . LEU A 229 ? 0.1091 0.0914 0.4964 -0.0224 -0.048  -0.0202 230  LEU A CG    
1883 C  CD1   . LEU A 229 ? 0.1123 0.095  0.4996 -0.0227 -0.0482 -0.0194 230  LEU A CD1   
1884 C  CD2   . LEU A 229 ? 0.1163 0.0993 0.5074 -0.0252 -0.0511 -0.0172 230  LEU A CD2   
1885 N  N     . LEU A 230 ? 0.086  0.0809 0.4789 -0.016  -0.0357 -0.0268 231  LEU A N     
1886 C  CA    . LEU A 230 ? 0.0863 0.0869 0.4829 -0.0143 -0.0318 -0.0285 231  LEU A CA    
1887 C  C     . LEU A 230 ? 0.0933 0.0954 0.4925 -0.0142 -0.031  -0.0286 231  LEU A C     
1888 O  O     . LEU A 230 ? 0.0906 0.0988 0.4953 -0.0141 -0.0288 -0.0287 231  LEU A O     
1889 C  CB    . LEU A 230 ? 0.085  0.0838 0.4778 -0.0119 -0.0297 -0.0311 231  LEU A CB    
1890 C  CG    . LEU A 230 ? 0.1058 0.1057 0.4978 -0.0117 -0.0293 -0.0312 231  LEU A CG    
1891 C  CD1   . LEU A 230 ? 0.1248 0.121  0.5116 -0.0095 -0.028  -0.0333 231  LEU A CD1   
1892 C  CD2   . LEU A 230 ? 0.0991 0.1069 0.4973 -0.0116 -0.0271 -0.0312 231  LEU A CD2   
1893 N  N     . ILE A 231 ? 0.1055 0.1021 0.5007 -0.0143 -0.0328 -0.0285 232  ILE A N     
1894 C  CA    . ILE A 231 ? 0.1193 0.117  0.5169 -0.0142 -0.0322 -0.0283 232  ILE A CA    
1895 C  C     . ILE A 231 ? 0.0984 0.1004 0.5015 -0.0165 -0.0334 -0.0257 232  ILE A C     
1896 O  O     . ILE A 231 ? 0.0811 0.0879 0.4891 -0.0163 -0.0314 -0.0256 232  ILE A O     
1897 C  CB    . ILE A 231 ? 0.1497 0.1403 0.5412 -0.0138 -0.0344 -0.0284 232  ILE A CB    
1898 C  CG1   . ILE A 231 ? 0.1766 0.163  0.5625 -0.0112 -0.0331 -0.0306 232  ILE A CG1   
1899 C  CG2   . ILE A 231 ? 0.1562 0.148  0.5502 -0.0139 -0.0341 -0.0278 232  ILE A CG2   
1900 C  CD1   . ILE A 231 ? 0.2079 0.1983 0.5968 -0.0092 -0.0292 -0.0323 232  ILE A CD1   
1901 N  N     . ASN A 232 ? 0.0912 0.0917 0.4938 -0.0185 -0.0365 -0.0236 233  ASN A N     
1902 C  CA    . ASN A 232 ? 0.0833 0.0878 0.4912 -0.0207 -0.0378 -0.0206 233  ASN A CA    
1903 C  C     . ASN A 232 ? 0.0685 0.081  0.4826 -0.0202 -0.0347 -0.0205 233  ASN A C     
1904 O  O     . ASN A 232 ? 0.07   0.0869 0.4889 -0.0207 -0.0338 -0.0192 233  ASN A O     
1905 C  CB    . ASN A 232 ? 0.1147 0.1158 0.5209 -0.0229 -0.0418 -0.0184 233  ASN A CB    
1906 C  CG    . ASN A 232 ? 0.1731 0.1668 0.5742 -0.0238 -0.0455 -0.018  233  ASN A CG    
1907 O  OD1   . ASN A 232 ? 0.2091 0.2007 0.6081 -0.0228 -0.0451 -0.0191 233  ASN A OD1   
1908 N  ND2   . ASN A 232 ? 0.1723 0.1619 0.5711 -0.0256 -0.0492 -0.0165 233  ASN A ND2   
1909 N  N     . LYS A 233 ? 0.0601 0.0743 0.4738 -0.0189 -0.0328 -0.0221 234  LYS A N     
1910 C  CA    . LYS A 233 ? 0.053  0.0745 0.4719 -0.0179 -0.0298 -0.0223 234  LYS A CA    
1911 C  C     . LYS A 233 ? 0.0575 0.0818 0.4787 -0.0163 -0.0267 -0.0244 234  LYS A C     
1912 O  O     . LYS A 233 ? 0.0491 0.0781 0.4742 -0.0155 -0.0249 -0.0238 234  LYS A O     
1913 C  CB    . LYS A 233 ? 0.0609 0.0828 0.478  -0.0169 -0.0289 -0.0236 234  LYS A CB    
1914 C  CG    . LYS A 233 ? 0.0741 0.0949 0.4908 -0.0186 -0.0316 -0.0209 234  LYS A CG    
1915 C  CD    . LYS A 233 ? 0.0864 0.1074 0.5011 -0.0176 -0.0308 -0.022  234  LYS A CD    
1916 C  CE    . LYS A 233 ? 0.0914 0.111  0.5059 -0.0194 -0.0337 -0.0191 234  LYS A CE    
1917 N  NZ    . LYS A 233 ? 0.0975 0.12   0.5123 -0.0183 -0.0323 -0.0194 234  LYS A NZ    
1918 N  N     . ASN A 234 ? 0.0564 0.0767 0.4739 -0.015  -0.026  -0.0268 235  ASN A N     
1919 C  CA    . ASN A 234 ? 0.0483 0.067  0.4634 -0.0112 -0.0229 -0.0284 235  ASN A CA    
1920 C  C     . ASN A 234 ? 0.0479 0.0673 0.4651 -0.0116 -0.0233 -0.0264 235  ASN A C     
1921 O  O     . ASN A 234 ? 0.0449 0.0632 0.4601 -0.0084 -0.0206 -0.0266 235  ASN A O     
1922 C  CB    . ASN A 234 ? 0.0482 0.0622 0.4587 -0.0097 -0.0227 -0.0303 235  ASN A CB    
1923 C  CG    . ASN A 234 ? 0.0775 0.0963 0.4944 -0.0103 -0.02   -0.0327 235  ASN A CG    
1924 O  OD1   . ASN A 234 ? 0.1203 0.1438 0.5424 -0.0101 -0.0183 -0.0328 235  ASN A OD1   
1925 N  ND2   . ASN A 234 ? 0.043  0.0512 0.4463 -0.0033 -0.0184 -0.0338 235  ASN A ND2   
1926 N  N     . LEU A 235 ? 0.0497 0.0659 0.4649 -0.013  -0.0263 -0.0243 236  LEU A N     
1927 C  CA    . LEU A 235 ? 0.0556 0.0769 0.4794 -0.0175 -0.0277 -0.0225 236  LEU A CA    
1928 C  C     . LEU A 235 ? 0.06   0.0873 0.4894 -0.0186 -0.0274 -0.0202 236  LEU A C     
1929 O  O     . LEU A 235 ? 0.0713 0.1024 0.5049 -0.0185 -0.026  -0.0193 236  LEU A O     
1930 C  CB    . LEU A 235 ? 0.0645 0.0799 0.4841 -0.0191 -0.0315 -0.0209 236  LEU A CB    
1931 C  CG    . LEU A 235 ? 0.0783 0.0944 0.5002 -0.0202 -0.0326 -0.0188 236  LEU A CG    
1932 C  CD1   . LEU A 235 ? 0.0858 0.1019 0.508  -0.0184 -0.0302 -0.0206 236  LEU A CD1   
1933 C  CD2   . LEU A 235 ? 0.0907 0.1013 0.5088 -0.0221 -0.037  -0.017  236  LEU A CD2   
1934 N  N     . LYS A 236 ? 0.0586 0.0872 0.4883 -0.0193 -0.0285 -0.0189 237  LYS A N     
1935 C  CA    . LYS A 236 ? 0.0685 0.1032 0.5034 -0.0199 -0.0279 -0.0165 237  LYS A CA    
1936 C  C     . LYS A 236 ? 0.0704 0.1108 0.5091 -0.0179 -0.0241 -0.0183 237  LYS A C     
1937 O  O     . LYS A 236 ? 0.0752 0.1207 0.5185 -0.0179 -0.0231 -0.0165 237  LYS A O     
1938 C  CB    . LYS A 236 ? 0.0942 0.1289 0.5287 -0.0211 -0.0299 -0.0146 237  LYS A CB    
1939 C  CG    . LYS A 236 ? 0.1584 0.1874 0.5896 -0.0233 -0.034  -0.0127 237  LYS A CG    
1940 C  CD    . LYS A 236 ? 0.2123 0.243  0.6459 -0.0251 -0.0363 -0.0092 237  LYS A CD    
1941 C  CE    . LYS A 236 ? 0.2473 0.2787 0.6797 -0.0243 -0.0357 -0.0099 237  LYS A CE    
1942 N  NZ    . LYS A 236 ? 0.2544 0.2842 0.6871 -0.0265 -0.0392 -0.0066 237  LYS A NZ    
1943 N  N     . MET A 237 ? 0.0744 0.1137 0.511  -0.016  -0.0221 -0.0218 238  MET A N     
1944 C  CA    . MET A 237 ? 0.0616 0.1055 0.5015 -0.0141 -0.0188 -0.0239 238  MET A CA    
1945 C  C     . MET A 237 ? 0.0598 0.1047 0.5024 -0.0138 -0.0176 -0.0239 238  MET A C     
1946 O  O     . MET A 237 ? 0.0632 0.1129 0.5101 -0.0131 -0.0158 -0.0237 238  MET A O     
1947 C  CB    . MET A 237 ? 0.0457 0.0864 0.4811 -0.0118 -0.0172 -0.0274 238  MET A CB    
1948 C  CG    . MET A 237 ? 0.0572 0.1036 0.4977 -0.0104 -0.0142 -0.03   238  MET A CG    
1949 S  SD    . MET A 237 ? 0.0509 0.1044 0.4957 -0.0096 -0.0129 -0.0289 238  MET A SD    
1950 C  CE    . MET A 237 ? 0.0488 0.1022 0.4906 -0.0089 -0.0131 -0.0301 238  MET A CE    
1951 N  N     . VAL A 238 ? 0.0546 0.0948 0.4946 -0.0143 -0.0187 -0.0242 239  VAL A N     
1952 C  CA    . VAL A 238 ? 0.0553 0.0962 0.4979 -0.0142 -0.0177 -0.0239 239  VAL A CA    
1953 C  C     . VAL A 238 ? 0.0531 0.0973 0.4993 -0.0156 -0.0186 -0.0204 239  VAL A C     
1954 O  O     . VAL A 238 ? 0.0585 0.1062 0.5087 -0.015  -0.0167 -0.0201 239  VAL A O     
1955 C  CB    . VAL A 238 ? 0.0588 0.0939 0.4973 -0.0144 -0.019  -0.0243 239  VAL A CB    
1956 C  CG1   . VAL A 238 ? 0.0545 0.0901 0.4954 -0.0145 -0.0184 -0.0234 239  VAL A CG1   
1957 C  CG2   . VAL A 238 ? 0.0585 0.0909 0.4939 -0.0127 -0.0177 -0.0275 239  VAL A CG2   
1958 N  N     . GLU A 239 ? 0.048  0.0913 0.4931 -0.0174 -0.0214 -0.0177 240  GLU A N     
1959 C  CA    . GLU A 239 ? 0.0484 0.0949 0.4972 -0.0189 -0.0225 -0.0139 240  GLU A CA    
1960 C  C     . GLU A 239 ? 0.0555 0.1086 0.5089 -0.0177 -0.0201 -0.0133 240  GLU A C     
1961 O  O     . GLU A 239 ? 0.0458 0.1027 0.5032 -0.0176 -0.0188 -0.0118 240  GLU A O     
1962 C  CB    . GLU A 239 ? 0.0501 0.094  0.4967 -0.0211 -0.0262 -0.0113 240  GLU A CB    
1963 C  CG    . GLU A 239 ? 0.0543 0.1007 0.5046 -0.023  -0.028  -0.007  240  GLU A CG    
1964 C  CD    . GLU A 239 ? 0.129  0.1731 0.578  -0.0253 -0.0318 -0.0042 240  GLU A CD    
1965 O  OE1   . GLU A 239 ? 0.1205 0.1597 0.5649 -0.0256 -0.0334 -0.0058 240  GLU A OE1   
1966 O  OE2   . GLU A 239 ? 0.1715 0.2187 0.6244 -0.0269 -0.0332 -0.0003 240  GLU A OE2   
1967 N  N     . PHE A 240 ? 0.0574 0.112  0.51   -0.0166 -0.0192 -0.0148 241  PHE A N     
1968 C  CA    . PHE A 240 ? 0.0645 0.1252 0.5208 -0.0151 -0.0169 -0.0146 241  PHE A CA    
1969 C  C     . PHE A 240 ? 0.0634 0.1264 0.5221 -0.0132 -0.0139 -0.0168 241  PHE A C     
1970 O  O     . PHE A 240 ? 0.068  0.1356 0.5305 -0.0125 -0.0124 -0.0152 241  PHE A O     
1971 C  CB    . PHE A 240 ? 0.0709 0.132  0.5252 -0.014  -0.0164 -0.0164 241  PHE A CB    
1972 C  CG    . PHE A 240 ? 0.0771 0.1438 0.5341 -0.0116 -0.0136 -0.0175 241  PHE A CG    
1973 C  CD1   . PHE A 240 ? 0.0779 0.1498 0.5384 -0.0113 -0.0132 -0.0143 241  PHE A CD1   
1974 C  CD2   . PHE A 240 ? 0.0889 0.1555 0.5449 -0.0096 -0.0115 -0.0217 241  PHE A CD2   
1975 C  CE1   . PHE A 240 ? 0.0857 0.1625 0.5481 -0.0088 -0.0107 -0.0154 241  PHE A CE1   
1976 C  CE2   . PHE A 240 ? 0.0882 0.1596 0.5463 -0.0073 -0.0092 -0.0229 241  PHE A CE2   
1977 C  CZ    . PHE A 240 ? 0.0771 0.1535 0.5382 -0.0068 -0.0088 -0.0198 241  PHE A CZ    
1978 N  N     . LEU A 241 ? 0.0583 0.1179 0.5149 -0.0124 -0.013  -0.0202 242  LEU A N     
1979 C  CA    . LEU A 241 ? 0.0529 0.1141 0.5118 -0.0107 -0.0103 -0.0226 242  LEU A CA    
1980 C  C     . LEU A 241 ? 0.0476 0.1094 0.5093 -0.0113 -0.01   -0.0208 242  LEU A C     
1981 O  O     . LEU A 241 ? 0.0456 0.1111 0.5108 -0.01   -0.008  -0.0209 242  LEU A O     
1982 C  CB    . LEU A 241 ? 0.0503 0.1079 0.5067 -0.0097 -0.0096 -0.0264 242  LEU A CB    
1983 C  CG    . LEU A 241 ? 0.0442 0.1018 0.4984 -0.0088 -0.0093 -0.0287 242  LEU A CG    
1984 C  CD1   . LEU A 241 ? 0.043  0.094  0.4919 -0.0075 -0.0085 -0.0319 242  LEU A CD1   
1985 C  CD2   . LEU A 241 ? 0.0422 0.0946 0.4887 -0.0058 -0.0071 -0.0296 242  LEU A CD2   
1986 N  N     . SER A 242 ? 0.0432 0.0991 0.5008 -0.0125 -0.0119 -0.0193 243  SER A N     
1987 C  CA    . SER A 242 ? 0.0536 0.1122 0.5159 -0.0135 -0.0117 -0.0177 243  SER A CA    
1988 C  C     . SER A 242 ? 0.0648 0.1278 0.5307 -0.0142 -0.012  -0.0139 243  SER A C     
1989 O  O     . SER A 242 ? 0.0818 0.1474 0.5511 -0.0136 -0.0103 -0.0131 243  SER A O     
1990 C  CB    . SER A 242 ? 0.066  0.1195 0.5251 -0.0148 -0.0138 -0.0172 243  SER A CB    
1991 O  OG    . SER A 242 ? 0.0752 0.1259 0.531  -0.0165 -0.017  -0.0155 243  SER A OG    
1992 N  N     . LYS A 243 ? 0.0562 0.1204 0.5217 -0.0153 -0.0138 -0.0115 244  LYS A N     
1993 C  CA    . LYS A 243 ? 0.0546 0.1235 0.5239 -0.0158 -0.0139 -0.0075 244  LYS A CA    
1994 C  C     . LYS A 243 ? 0.0665 0.1409 0.539  -0.0134 -0.0109 -0.008  244  LYS A C     
1995 O  O     . LYS A 243 ? 0.0633 0.1421 0.5393 -0.0133 -0.0103 -0.0048 244  LYS A O     
1996 C  CB    . LYS A 243 ? 0.0601 0.1283 0.5283 -0.0179 -0.0171 -0.0043 244  LYS A CB    
1997 C  CG    . LYS A 243 ? 0.1092 0.1726 0.5752 -0.0203 -0.0203 -0.0028 244  LYS A CG    
1998 C  CD    . LYS A 243 ? 0.1632 0.2256 0.6284 -0.0225 -0.0238 0.0003  244  LYS A CD    
1999 C  CE    . LYS A 243 ? 0.1882 0.2458 0.6511 -0.0249 -0.0273 0.0017  244  LYS A CE    
2000 N  NZ    . LYS A 243 ? 0.2186 0.2746 0.6807 -0.027  -0.0309 0.0044  244  LYS A NZ    
2001 N  N     . ASN A 244 ? 0.0838 0.1579 0.5551 -0.0114 -0.009  -0.012  245  ASN A N     
2002 C  CA    . ASN A 244 ? 0.1092 0.1879 0.583  -0.0089 -0.0062 -0.0131 245  ASN A CA    
2003 C  C     . ASN A 244 ? 0.1367 0.2153 0.6123 -0.0075 -0.0039 -0.0156 245  ASN A C     
2004 O  O     . ASN A 244 ? 0.1496 0.2318 0.6275 -0.0054 -0.0017 -0.0163 245  ASN A O     
2005 C  CB    . ASN A 244 ? 0.1295 0.2088 0.6013 -0.0075 -0.0058 -0.0155 245  ASN A CB    
2006 C  CG    . ASN A 244 ? 0.1725 0.2543 0.6443 -0.0081 -0.0072 -0.0122 245  ASN A CG    
2007 O  OD1   . ASN A 244 ? 0.2142 0.299  0.6886 -0.0089 -0.0077 -0.008  245  ASN A OD1   
2008 N  ND2   . ASN A 244 ? 0.1526 0.2336 0.6219 -0.0078 -0.0077 -0.0138 245  ASN A ND2   
2009 N  N     . THR A 245 ? 0.1495 0.2243 0.6243 -0.0084 -0.0043 -0.0166 246  THR A N     
2010 C  CA    . THR A 245 ? 0.1744 0.2491 0.6515 -0.0073 -0.0021 -0.0186 246  THR A CA    
2011 C  C     . THR A 245 ? 0.1986 0.2748 0.6785 -0.0081 -0.002  -0.0152 246  THR A C     
2012 O  O     . THR A 245 ? 0.2022 0.2783 0.6818 -0.01   -0.0041 -0.0117 246  THR A O     
2013 C  CB    . THR A 245 ? 0.2006 0.2705 0.6753 -0.0074 -0.0023 -0.0217 246  THR A CB    
2014 O  OG1   . THR A 245 ? 0.2166 0.283  0.6889 -0.0095 -0.0047 -0.0199 246  THR A OG1   
2015 C  CG2   . THR A 245 ? 0.2076 0.2763 0.68   -0.0064 -0.0021 -0.0252 246  THR A CG2   
2016 N  N     . LYS A 246 ? 0.2139 0.2914 0.6967 -0.0067 0.0003  -0.0162 247  LYS A N     
2017 C  CA    . LYS A 246 ? 0.2311 0.3101 0.7168 -0.0073 0.0007  -0.013  247  LYS A CA    
2018 C  C     . LYS A 246 ? 0.2358 0.3109 0.7201 -0.0091 -0.0008 -0.0125 247  LYS A C     
2019 O  O     . LYS A 246 ? 0.2407 0.3124 0.7233 -0.0088 -0.0006 -0.0155 247  LYS A O     
2020 C  CB    . LYS A 246 ? 0.2742 0.3558 0.7634 -0.0051 0.0038  -0.0142 247  LYS A CB    
2021 C  CG    . LYS A 246 ? 0.3571 0.4437 0.8487 -0.004  0.0049  -0.0115 247  LYS A CG    
2022 C  CD    . LYS A 246 ? 0.4318 0.5204 0.9225 -0.0019 0.0058  -0.0136 247  LYS A CD    
2023 C  CE    . LYS A 246 ? 0.4907 0.5823 0.9808 -0.0023 0.0045  -0.0102 247  LYS A CE    
2024 N  NZ    . LYS A 246 ? 0.531  0.6199 1.0179 -0.0043 0.0019  -0.0103 247  LYS A NZ    
2025 N  N     . ASN A 247 ? 0.2361 0.3117 0.7209 -0.0109 -0.0025 -0.0087 248  ASN A N     
2026 C  CA    . ASN A 247 ? 0.2477 0.3197 0.7307 -0.0125 -0.0042 -0.0078 248  ASN A CA    
2027 C  C     . ASN A 247 ? 0.2495 0.3214 0.7349 -0.0116 -0.0022 -0.0084 248  ASN A C     
2028 O  O     . ASN A 247 ? 0.2559 0.3244 0.7395 -0.0124 -0.0033 -0.0086 248  ASN A O     
2029 C  CB    . ASN A 247 ? 0.2776 0.3504 0.7607 -0.0148 -0.007  -0.0033 248  ASN A CB    
2030 C  CG    . ASN A 247 ? 0.3387 0.4109 0.8193 -0.016  -0.0095 -0.0023 248  ASN A CG    
2031 O  OD1   . ASN A 247 ? 0.3544 0.4286 0.8363 -0.0176 -0.0114 0.0016  248  ASN A OD1   
2032 N  ND2   . ASN A 247 ? 0.3557 0.4254 0.8332 -0.0154 -0.0097 -0.0055 248  ASN A ND2   
2033 N  N     . ASP A 248 ? 0.2378 0.3132 0.7271 -0.01   0.0006  -0.0085 249  ASP A N     
2034 C  CA    . ASP A 248 ? 0.2461 0.3215 0.7382 -0.0092 0.0025  -0.0087 249  ASP A CA    
2035 C  C     . ASP A 248 ? 0.2367 0.3083 0.7275 -0.0084 0.0033  -0.0123 249  ASP A C     
2036 O  O     . ASP A 248 ? 0.2454 0.3155 0.7367 -0.0086 0.0035  -0.0118 249  ASP A O     
2037 C  CB    . ASP A 248 ? 0.2912 0.3709 0.7876 -0.0075 0.0054  -0.0082 249  ASP A CB    
2038 C  CG    . ASP A 248 ? 0.4026 0.4828 0.8994 -0.0053 0.0073  -0.012  249  ASP A CG    
2039 O  OD1   . ASP A 248 ? 0.444  0.5226 0.9379 -0.0054 0.0062  -0.0141 249  ASP A OD1   
2040 O  OD2   . ASP A 248 ? 0.4347 0.5167 0.9347 -0.0035 0.0098  -0.0128 249  ASP A OD2   
2041 N  N     . ASN A 249 ? 0.2145 0.2849 0.704  -0.0074 0.0038  -0.0158 250  ASN A N     
2042 C  CA    . ASN A 249 ? 0.2035 0.2708 0.6924 -0.0065 0.0046  -0.0191 250  ASN A CA    
2043 C  C     . ASN A 249 ? 0.1743 0.2379 0.6585 -0.0071 0.0027  -0.0207 250  ASN A C     
2044 O  O     . ASN A 249 ? 0.1734 0.2348 0.6572 -0.0062 0.0034  -0.0234 250  ASN A O     
2045 C  CB    . ASN A 249 ? 0.2293 0.2981 0.7213 -0.0045 0.0071  -0.022  250  ASN A CB    
2046 C  CG    . ASN A 249 ? 0.3172 0.3886 0.8138 -0.0035 0.0094  -0.0211 250  ASN A CG    
2047 O  OD1   . ASN A 249 ? 0.3427 0.4167 0.8415 -0.0023 0.0109  -0.0216 250  ASN A OD1   
2048 N  ND2   . ASN A 249 ? 0.3447 0.4151 0.8426 -0.004  0.0098  -0.0196 250  ASN A ND2   
2049 N  N     . ASN A 250 ? 0.1509 0.2141 0.632  -0.0086 0.0002  -0.0191 251  ASN A N     
2050 C  CA    . ASN A 250 ? 0.1314 0.1909 0.6077 -0.0091 -0.0017 -0.0205 251  ASN A CA    
2051 C  C     . ASN A 250 ? 0.1133 0.1706 0.5864 -0.011  -0.0047 -0.0178 251  ASN A C     
2052 O  O     . ASN A 250 ? 0.1188 0.1783 0.5935 -0.0121 -0.0055 -0.0146 251  ASN A O     
2053 C  CB    . ASN A 250 ? 0.1348 0.1958 0.6103 -0.0087 -0.0018 -0.0218 251  ASN A CB    
2054 C  CG    . ASN A 250 ? 0.1781 0.2417 0.6568 -0.0068 0.0008  -0.0244 251  ASN A CG    
2055 O  OD1   . ASN A 250 ? 0.2037 0.2711 0.6851 -0.0062 0.0019  -0.0235 251  ASN A OD1   
2056 N  ND2   . ASN A 250 ? 0.171  0.2326 0.6495 -0.0057 0.0018  -0.0276 251  ASN A ND2   
2057 N  N     . PHE A 251 ? 0.0946 0.1475 0.5629 -0.0114 -0.0065 -0.0188 252  PHE A N     
2058 C  CA    . PHE A 251 ? 0.0833 0.1333 0.5478 -0.0132 -0.0097 -0.0167 252  PHE A CA    
2059 C  C     . PHE A 251 ? 0.0852 0.1372 0.5497 -0.0145 -0.0114 -0.0148 252  PHE A C     
2060 O  O     . PHE A 251 ? 0.0841 0.1376 0.5488 -0.0139 -0.0106 -0.0163 252  PHE A O     
2061 C  CB    . PHE A 251 ? 0.0822 0.127  0.5413 -0.0129 -0.0111 -0.0186 252  PHE A CB    
2062 C  CG    . PHE A 251 ? 0.0832 0.1246 0.5404 -0.0119 -0.0107 -0.0194 252  PHE A CG    
2063 C  CD1   . PHE A 251 ? 0.0907 0.1338 0.5514 -0.0114 -0.0091 -0.0184 252  PHE A CD1   
2064 C  CD2   . PHE A 251 ? 0.0869 0.1237 0.5391 -0.0112 -0.0116 -0.021  252  PHE A CD2   
2065 C  CE1   . PHE A 251 ? 0.0975 0.1379 0.5567 -0.0102 -0.0085 -0.0189 252  PHE A CE1   
2066 C  CE2   . PHE A 251 ? 0.0937 0.1277 0.5443 -0.0099 -0.011  -0.0215 252  PHE A CE2   
2067 C  CZ    . PHE A 251 ? 0.0918 0.1278 0.546  -0.0093 -0.0094 -0.0205 252  PHE A CZ    
2068 N  N     . THR A 252 ? 0.0903 0.1421 0.5544 -0.0164 -0.0139 -0.0115 253  THR A N     
2069 C  CA    . THR A 252 ? 0.0939 0.1475 0.5582 -0.0179 -0.0159 -0.0091 253  THR A CA    
2070 C  C     . THR A 252 ? 0.101  0.1497 0.56   -0.0188 -0.0188 -0.01   253  THR A C     
2071 O  O     . THR A 252 ? 0.1007 0.1447 0.5557 -0.0184 -0.0195 -0.0118 253  THR A O     
2072 C  CB    . THR A 252 ? 0.1146 0.1695 0.5809 -0.0198 -0.0178 -0.005  253  THR A CB    
2073 O  OG1   . THR A 252 ? 0.1371 0.1871 0.5994 -0.0208 -0.0204 -0.0048 253  THR A OG1   
2074 C  CG2   . THR A 252 ? 0.1032 0.1627 0.5746 -0.019  -0.0152 -0.0037 253  THR A CG2   
2075 N  N     . TYR A 253 ? 0.1057 0.1554 0.5644 -0.02   -0.0205 -0.0085 254  TYR A N     
2076 C  CA    . TYR A 253 ? 0.1141 0.159  0.5679 -0.021  -0.0234 -0.009  254  TYR A CA    
2077 C  C     . TYR A 253 ? 0.1148 0.155  0.5653 -0.0226 -0.0267 -0.0076 254  TYR A C     
2078 O  O     . TYR A 253 ? 0.1123 0.1471 0.5576 -0.0222 -0.028  -0.0096 254  TYR A O     
2079 C  CB    . TYR A 253 ? 0.1142 0.1611 0.5687 -0.0221 -0.0248 -0.0072 254  TYR A CB    
2080 C  CG    . TYR A 253 ? 0.1403 0.1818 0.5895 -0.0229 -0.0277 -0.0081 254  TYR A CG    
2081 C  CD1   . TYR A 253 ? 0.1567 0.1946 0.6018 -0.0214 -0.0267 -0.0117 254  TYR A CD1   
2082 C  CD2   . TYR A 253 ? 0.1614 0.2006 0.6094 -0.0253 -0.0316 -0.0052 254  TYR A CD2   
2083 C  CE1   . TYR A 253 ? 0.1772 0.2097 0.617  -0.022  -0.0293 -0.0125 254  TYR A CE1   
2084 C  CE2   . TYR A 253 ? 0.179  0.2125 0.6217 -0.0261 -0.0344 -0.0061 254  TYR A CE2   
2085 C  CZ    . TYR A 253 ? 0.1921 0.2222 0.6305 -0.0243 -0.0331 -0.0098 254  TYR A CZ    
2086 O  OH    . TYR A 253 ? 0.2133 0.2378 0.6464 -0.0248 -0.0356 -0.0107 254  TYR A OH    
2087 N  N     . SER A 254 ? 0.1165 0.1586 0.5697 -0.024  -0.0279 -0.0044 255  SER A N     
2088 C  CA    . SER A 254 ? 0.1348 0.1722 0.5847 -0.0254 -0.0314 -0.0031 255  SER A CA    
2089 C  C     . SER A 254 ? 0.1357 0.1693 0.5821 -0.0237 -0.0302 -0.0057 255  SER A C     
2090 O  O     . SER A 254 ? 0.1492 0.1773 0.5905 -0.024  -0.0329 -0.0063 255  SER A O     
2091 C  CB    . SER A 254 ? 0.1512 0.1916 0.6049 -0.0273 -0.033  0.0011  255  SER A CB    
2092 O  OG    . SER A 254 ? 0.219  0.2648 0.6778 -0.0261 -0.0295 0.0016  255  SER A OG    
2093 N  N     . GLU A 255 ? 0.1179 0.1544 0.5671 -0.0217 -0.0263 -0.0075 256  GLU A N     
2094 C  CA    . GLU A 255 ? 0.1159 0.1494 0.5626 -0.0198 -0.0249 -0.0099 256  GLU A CA    
2095 C  C     . GLU A 255 ? 0.1037 0.1327 0.5452 -0.0187 -0.0251 -0.0129 256  GLU A C     
2096 O  O     . GLU A 255 ? 0.1117 0.1355 0.5481 -0.0182 -0.0267 -0.0136 256  GLU A O     
2097 C  CB    . GLU A 255 ? 0.1319 0.1696 0.5835 -0.0181 -0.0207 -0.0107 256  GLU A CB    
2098 C  CG    . GLU A 255 ? 0.1522 0.1935 0.6081 -0.0189 -0.0205 -0.0078 256  GLU A CG    
2099 C  CD    . GLU A 255 ? 0.2007 0.2466 0.662  -0.0173 -0.0165 -0.0084 256  GLU A CD    
2100 O  OE1   . GLU A 255 ? 0.1717 0.2201 0.6352 -0.0164 -0.0143 -0.01   256  GLU A OE1   
2101 O  OE2   . GLU A 255 ? 0.263  0.3099 0.7264 -0.017  -0.0155 -0.0073 256  GLU A OE2   
2102 N  N     . TRP A 256 ? 0.0852 0.1162 0.5278 -0.0182 -0.0237 -0.0143 257  TRP A N     
2103 C  CA    . TRP A 256 ? 0.0811 0.1081 0.5189 -0.0173 -0.024  -0.0169 257  TRP A CA    
2104 C  C     . TRP A 256 ? 0.0982 0.1197 0.5303 -0.0187 -0.0281 -0.016  257  TRP A C     
2105 O  O     . TRP A 256 ? 0.1061 0.1226 0.5329 -0.0176 -0.0289 -0.0176 257  TRP A O     
2106 C  CB    . TRP A 256 ? 0.0629 0.0932 0.5028 -0.0169 -0.0224 -0.0181 257  TRP A CB    
2107 C  CG    . TRP A 256 ? 0.049  0.0834 0.4932 -0.0151 -0.0185 -0.02   257  TRP A CG    
2108 C  CD1   . TRP A 256 ? 0.0493 0.0891 0.4985 -0.015  -0.0166 -0.0197 257  TRP A CD1   
2109 C  CD2   . TRP A 256 ? 0.0443 0.0692 0.4785 -0.0096 -0.0157 -0.0224 257  TRP A CD2   
2110 N  NE1   . TRP A 256 ? 0.0497 0.0913 0.5013 -0.0131 -0.0135 -0.0221 257  TRP A NE1   
2111 C  CE2   . TRP A 256 ? 0.0452 0.0811 0.4919 -0.0114 -0.0131 -0.0238 257  TRP A CE2   
2112 C  CE3   . TRP A 256 ? 0.0456 0.074  0.4851 -0.0119 -0.0163 -0.0238 257  TRP A CE3   
2113 C  CZ2   . TRP A 256 ? 0.0467 0.0846 0.4969 -0.0102 -0.0106 -0.0262 257  TRP A CZ2   
2114 C  CZ3   . TRP A 256 ? 0.0545 0.0836 0.4958 -0.01   -0.0135 -0.026  257  TRP A CZ3   
2115 C  CH2   . TRP A 256 ? 0.0528 0.0865 0.4994 -0.0092 -0.0108 -0.0271 257  TRP A CH2   
2116 N  N     . GLU A 257 ? 0.101  0.1235 0.5344 -0.021  -0.0309 -0.0132 258  GLU A N     
2117 C  CA    . GLU A 257 ? 0.1236 0.141  0.5523 -0.0227 -0.0352 -0.012  258  GLU A CA    
2118 C  C     . GLU A 257 ? 0.143  0.1552 0.5672 -0.0224 -0.0372 -0.0121 258  GLU A C     
2119 O  O     . GLU A 257 ? 0.1513 0.1575 0.5693 -0.0221 -0.0395 -0.0132 258  GLU A O     
2120 C  CB    . GLU A 257 ? 0.1372 0.1576 0.5697 -0.0253 -0.0375 -0.0085 258  GLU A CB    
2121 C  CG    . GLU A 257 ? 0.2074 0.2228 0.6358 -0.0273 -0.0422 -0.0072 258  GLU A CG    
2122 C  CD    . GLU A 257 ? 0.2719 0.2909 0.705  -0.0299 -0.0443 -0.0033 258  GLU A CD    
2123 O  OE1   . GLU A 257 ? 0.2672 0.2899 0.7046 -0.0306 -0.0441 -0.001  258  GLU A OE1   
2124 O  OE2   . GLU A 257 ? 0.3037 0.3223 0.7366 -0.031  -0.0461 -0.0025 258  GLU A OE2   
2125 N  N     . SER A 258 ? 0.1503 0.1648 0.5773 -0.0222 -0.0363 -0.0109 259  SER A N     
2126 C  CA    . SER A 258 ? 0.1651 0.1753 0.588  -0.0216 -0.038  -0.0108 259  SER A CA    
2127 C  C     . SER A 258 ? 0.1833 0.1897 0.6015 -0.0187 -0.0361 -0.0139 259  SER A C     
2128 O  O     . SER A 258 ? 0.1976 0.1986 0.6102 -0.018  -0.0382 -0.0142 259  SER A O     
2129 C  CB    . SER A 258 ? 0.1709 0.1851 0.5985 -0.022  -0.037  -0.0087 259  SER A CB    
2130 O  OG    . SER A 258 ? 0.2028 0.2209 0.6342 -0.02   -0.0324 -0.0101 259  SER A OG    
2131 N  N     . ILE A 259 ? 0.1758 0.1848 0.5962 -0.017  -0.0323 -0.0159 260  ILE A N     
2132 C  CA    . ILE A 259 ? 0.1812 0.1872 0.5979 -0.0143 -0.0303 -0.0185 260  ILE A CA    
2133 C  C     . ILE A 259 ? 0.1913 0.1924 0.6021 -0.0143 -0.0324 -0.0198 260  ILE A C     
2134 O  O     . ILE A 259 ? 0.1998 0.1953 0.6043 -0.0128 -0.0336 -0.0208 260  ILE A O     
2135 C  CB    . ILE A 259 ? 0.1808 0.1918 0.6028 -0.0128 -0.0258 -0.0201 260  ILE A CB    
2136 C  CG1   . ILE A 259 ? 0.1852 0.2008 0.6131 -0.0126 -0.0235 -0.0189 260  ILE A CG1   
2137 C  CG2   . ILE A 259 ? 0.1916 0.1996 0.61   -0.0101 -0.0239 -0.0225 260  ILE A CG2   
2138 C  CD1   . ILE A 259 ? 0.1808 0.2016 0.6146 -0.0118 -0.0198 -0.02   260  ILE A CD1   
2139 N  N     . TYR A 260 ? 0.1921 0.1952 0.6047 -0.0158 -0.0329 -0.0197 261  TYR A N     
2140 C  CA    . TYR A 260 ? 0.1992 0.1982 0.607  -0.016  -0.0348 -0.0206 261  TYR A CA    
2141 C  C     . TYR A 260 ? 0.2235 0.2158 0.625  -0.0169 -0.0393 -0.0198 261  TYR A C     
2142 O  O     . TYR A 260 ? 0.2247 0.2115 0.6198 -0.0156 -0.0403 -0.0213 261  TYR A O     
2143 C  CB    . TYR A 260 ? 0.1886 0.1917 0.6005 -0.0178 -0.0348 -0.0198 261  TYR A CB    
2144 C  CG    . TYR A 260 ? 0.1978 0.1969 0.6051 -0.0182 -0.0369 -0.0205 261  TYR A CG    
2145 C  CD1   . TYR A 260 ? 0.211  0.209  0.6158 -0.0163 -0.0349 -0.0229 261  TYR A CD1   
2146 C  CD2   . TYR A 260 ? 0.2071 0.2033 0.6125 -0.0205 -0.041  -0.0186 261  TYR A CD2   
2147 C  CE1   . TYR A 260 ? 0.2288 0.2232 0.6294 -0.0166 -0.0367 -0.0234 261  TYR A CE1   
2148 C  CE2   . TYR A 260 ? 0.2212 0.2137 0.6227 -0.0209 -0.0429 -0.0191 261  TYR A CE2   
2149 C  CZ    . TYR A 260 ? 0.2403 0.2318 0.6392 -0.0189 -0.0407 -0.0216 261  TYR A CZ    
2150 O  OH    . TYR A 260 ? 0.25   0.2377 0.6448 -0.0191 -0.0424 -0.0221 261  TYR A OH    
2151 N  N     . ASN A 261 ? 0.2321 0.2246 0.635  -0.0191 -0.0421 -0.0174 262  ASN A N     
2152 C  CA    . ASN A 261 ? 0.2567 0.2425 0.6535 -0.0201 -0.0469 -0.0167 262  ASN A CA    
2153 C  C     . ASN A 261 ? 0.2808 0.2622 0.6725 -0.0181 -0.0475 -0.0174 262  ASN A C     
2154 O  O     . ASN A 261 ? 0.2927 0.2683 0.6791 -0.0186 -0.0515 -0.017  262  ASN A O     
2155 C  CB    . ASN A 261 ? 0.2539 0.2411 0.6539 -0.0234 -0.0505 -0.0137 262  ASN A CB    
2156 C  CG    . ASN A 261 ? 0.2901 0.2824 0.6959 -0.0244 -0.0497 -0.0115 262  ASN A CG    
2157 O  OD1   . ASN A 261 ? 0.3032 0.296  0.7088 -0.0227 -0.0479 -0.012  262  ASN A OD1   
2158 N  ND2   . ASN A 261 ? 0.298  0.2945 0.7092 -0.027  -0.0509 -0.0087 262  ASN A ND2   
2159 N  N     . GLY A 262 ? 0.286  0.27   0.6794 -0.0157 -0.0435 -0.0185 263  GLY A N     
2160 C  CA    . GLY A 262 ? 0.3096 0.2901 0.6986 -0.0132 -0.0434 -0.0191 263  GLY A CA    
2161 C  C     . GLY A 262 ? 0.3304 0.3121 0.7212 -0.0141 -0.0447 -0.0171 263  GLY A C     
2162 O  O     . GLY A 262 ? 0.3461 0.3244 0.7325 -0.0121 -0.0453 -0.0174 263  GLY A O     
2163 N  N     . THR A 263 ? 0.3249 0.3118 0.7223 -0.0168 -0.0451 -0.0149 264  THR A N     
2164 C  CA    . THR A 263 ? 0.3294 0.3178 0.7289 -0.0177 -0.0463 -0.0127 264  THR A CA    
2165 C  C     . THR A 263 ? 0.3316 0.3232 0.7336 -0.0151 -0.0422 -0.0132 264  THR A C     
2166 O  O     . THR A 263 ? 0.3436 0.3331 0.7428 -0.0139 -0.043  -0.0128 264  THR A O     
2167 C  CB    . THR A 263 ? 0.3328 0.3265 0.7391 -0.021  -0.0474 -0.01   264  THR A CB    
2168 O  OG1   . THR A 263 ? 0.3469 0.3378 0.7513 -0.0233 -0.0512 -0.0093 264  THR A OG1   
2169 C  CG2   . THR A 263 ? 0.3334 0.3285 0.7416 -0.022  -0.049  -0.0076 264  THR A CG2   
2170 N  N     . TYR A 264 ? 0.3174 0.3138 0.7244 -0.0142 -0.0378 -0.0142 265  TYR A N     
2171 C  CA    . TYR A 264 ? 0.3088 0.3084 0.719  -0.0118 -0.0337 -0.0147 265  TYR A CA    
2172 C  C     . TYR A 264 ? 0.3025 0.3022 0.7126 -0.0097 -0.0303 -0.0172 265  TYR A C     
2173 O  O     . TYR A 264 ? 0.2957 0.2951 0.7052 -0.0104 -0.0305 -0.0183 265  TYR A O     
2174 C  CB    . TYR A 264 ? 0.3102 0.3169 0.7288 -0.0132 -0.0315 -0.013  265  TYR A CB    
2175 C  CG    . TYR A 264 ? 0.3198 0.3275 0.7399 -0.0157 -0.0345 -0.0101 265  TYR A CG    
2176 C  CD1   . TYR A 264 ? 0.3319 0.338  0.75   -0.0151 -0.0358 -0.0089 265  TYR A CD1   
2177 C  CD2   . TYR A 264 ? 0.3283 0.339  0.7521 -0.0184 -0.0359 -0.0085 265  TYR A CD2   
2178 C  CE1   . TYR A 264 ? 0.3394 0.3467 0.7593 -0.0175 -0.0387 -0.0061 265  TYR A CE1   
2179 C  CE2   . TYR A 264 ? 0.3334 0.3455 0.7592 -0.0208 -0.0387 -0.0055 265  TYR A CE2   
2180 C  CZ    . TYR A 264 ? 0.3451 0.3554 0.7689 -0.0204 -0.0402 -0.0044 265  TYR A CZ    
2181 O  OH    . TYR A 264 ? 0.3595 0.3713 0.7854 -0.0228 -0.043  -0.0013 265  TYR A OH    
2182 N  N     . ARG A 265 ? 0.2968 0.2974 0.7078 -0.007  -0.0272 -0.0179 266  ARG A N     
2183 C  CA    . ARG A 265 ? 0.3021 0.3038 0.7143 -0.005  -0.0238 -0.0199 266  ARG A CA    
2184 C  C     . ARG A 265 ? 0.2881 0.2966 0.709  -0.0057 -0.0204 -0.0197 266  ARG A C     
2185 O  O     . ARG A 265 ? 0.2898 0.3016 0.715  -0.0069 -0.0203 -0.018  266  ARG A O     
2186 C  CB    . ARG A 265 ? 0.3371 0.3358 0.7455 -0.0017 -0.0223 -0.0205 266  ARG A CB    
2187 C  CG    . ARG A 265 ? 0.4084 0.4099 0.8205 -0.0004 -0.0202 -0.0191 266  ARG A CG    
2188 C  CD    . ARG A 265 ? 0.4862 0.4846 0.8941 0.0031  -0.0191 -0.0193 266  ARG A CD    
2189 N  NE    . ARG A 265 ? 0.5458 0.5482 0.9592 0.0045  -0.0159 -0.0182 266  ARG A NE    
2190 C  CZ    . ARG A 265 ? 0.5889 0.5913 1.0018 0.0051  -0.0165 -0.0165 266  ARG A CZ    
2191 N  NH1   . ARG A 265 ? 0.583  0.5814 0.9899 0.0044  -0.0204 -0.0157 266  ARG A NH1   
2192 N  NH2   . ARG A 265 ? 0.6042 0.6106 1.0227 0.0064  -0.0133 -0.0155 266  ARG A NH2   
2193 N  N     . ILE A 266 ? 0.2767 0.2873 0.7003 -0.005  -0.0179 -0.0215 267  ILE A N     
2194 C  CA    . ILE A 266 ? 0.2722 0.2886 0.7034 -0.0055 -0.015  -0.0217 267  ILE A CA    
2195 C  C     . ILE A 266 ? 0.2806 0.3001 0.7167 -0.0043 -0.0124 -0.0208 267  ILE A C     
2196 O  O     . ILE A 266 ? 0.269  0.2932 0.7114 -0.0051 -0.0106 -0.0204 267  ILE A O     
2197 C  CB    . ILE A 266 ? 0.2722 0.2893 0.7042 -0.0046 -0.0131 -0.0241 267  ILE A CB    
2198 C  CG1   . ILE A 266 ? 0.278  0.3007 0.7168 -0.0056 -0.0112 -0.0246 267  ILE A CG1   
2199 C  CG2   . ILE A 266 ? 0.2781 0.2938 0.7093 -0.0019 -0.0108 -0.0252 267  ILE A CG2   
2200 C  CD1   . ILE A 266 ? 0.2904 0.3135 0.729  -0.0054 -0.0104 -0.0267 267  ILE A CD1   
2201 N  N     . THR A 267 ? 0.291  0.3078 0.7242 -0.0024 -0.0122 -0.0203 268  THR A N     
2202 C  CA    . THR A 267 ? 0.292  0.3116 0.7297 -0.0011 -0.0097 -0.0192 268  THR A CA    
2203 C  C     . THR A 267 ? 0.3013 0.3206 0.738  -0.002  -0.0116 -0.0168 268  THR A C     
2204 O  O     . THR A 267 ? 0.3124 0.3343 0.753  -0.0011 -0.0097 -0.0156 268  THR A O     
2205 C  CB    . THR A 267 ? 0.2988 0.3164 0.7349 0.0019  -0.0077 -0.0199 268  THR A CB    
2206 O  OG1   . THR A 267 ? 0.3076 0.3196 0.7354 0.003   -0.0102 -0.0198 268  THR A OG1   
2207 C  CG2   . THR A 267 ? 0.2965 0.3156 0.7356 0.0028  -0.0052 -0.0219 268  THR A CG2   
2208 N  N     . ASN A 268 ? 0.2931 0.3091 0.7245 -0.0035 -0.0155 -0.0161 269  ASN A N     
2209 C  CA    . ASN A 268 ? 0.2955 0.311  0.7257 -0.0045 -0.0179 -0.0138 269  ASN A CA    
2210 C  C     . ASN A 268 ? 0.2937 0.3111 0.7258 -0.0078 -0.0203 -0.0123 269  ASN A C     
2211 O  O     . ASN A 268 ? 0.2975 0.3131 0.7269 -0.0092 -0.0236 -0.0106 269  ASN A O     
2212 C  CB    . ASN A 268 ? 0.3066 0.316  0.7284 -0.0032 -0.0207 -0.0138 269  ASN A CB    
2213 N  N     . LEU A 269 ? 0.2867 0.308  0.7237 -0.009  -0.0188 -0.0129 270  LEU A N     
2214 C  CA    . LEU A 269 ? 0.2911 0.3151 0.7309 -0.0117 -0.0205 -0.0112 270  LEU A CA    
2215 C  C     . LEU A 269 ? 0.2841 0.3115 0.7279 -0.0125 -0.0202 -0.0085 270  LEU A C     
2216 O  O     . LEU A 269 ? 0.2832 0.3134 0.7309 -0.0109 -0.017  -0.0085 270  LEU A O     
2217 C  CB    . LEU A 269 ? 0.2956 0.3236 0.7401 -0.0119 -0.0179 -0.0125 270  LEU A CB    
2218 C  CG    . LEU A 269 ? 0.3191 0.3477 0.7635 -0.014  -0.0199 -0.0122 270  LEU A CG    
2219 C  CD1   . LEU A 269 ? 0.3365 0.3594 0.7739 -0.0144 -0.0231 -0.0131 270  LEU A CD1   
2220 C  CD2   . LEU A 269 ? 0.3265 0.3588 0.775  -0.0135 -0.017  -0.0138 270  LEU A CD2   
2221 N  N     . PRO A 270 ? 0.2775 0.3045 0.7203 -0.0147 -0.0237 -0.0061 271  PRO A N     
2222 C  CA    . PRO A 270 ? 0.2623 0.2927 0.7089 -0.0153 -0.0234 -0.0033 271  PRO A CA    
2223 C  C     . PRO A 270 ? 0.2494 0.2863 0.7037 -0.0155 -0.0199 -0.0025 271  PRO A C     
2224 O  O     . PRO A 270 ? 0.2494 0.2893 0.7074 -0.0148 -0.018  -0.001  271  PRO A O     
2225 C  CB    . PRO A 270 ? 0.2717 0.3003 0.7157 -0.0179 -0.0282 -0.0011 271  PRO A CB    
2226 C  CG    . PRO A 270 ? 0.2844 0.311  0.7261 -0.0191 -0.03   -0.0022 271  PRO A CG    
2227 C  CD    . PRO A 270 ? 0.2734 0.2971 0.712  -0.0168 -0.028  -0.0056 271  PRO A CD    
2228 N  N     . SER A 271 ? 0.2402 0.279  0.6967 -0.016  -0.0189 -0.0035 272  SER A N     
2229 C  CA    . SER A 271 ? 0.2406 0.2851 0.7037 -0.0158 -0.0157 -0.0031 272  SER A CA    
2230 C  C     . SER A 271 ? 0.2528 0.2981 0.7182 -0.0135 -0.0117 -0.0059 272  SER A C     
2231 O  O     . SER A 271 ? 0.2525 0.3019 0.723  -0.013  -0.009  -0.0061 272  SER A O     
2232 C  CB    . SER A 271 ? 0.2469 0.2932 0.711  -0.0174 -0.0168 -0.0027 272  SER A CB    
2233 O  OG    . SER A 271 ? 0.2701 0.3124 0.7295 -0.0174 -0.0183 -0.005  272  SER A OG    
2234 N  N     . LEU A 272 ? 0.2623 0.3038 0.7241 -0.0118 -0.0114 -0.008  273  LEU A N     
2235 C  CA    . LEU A 272 ? 0.2636 0.3058 0.7279 -0.0096 -0.0078 -0.0104 273  LEU A CA    
2236 C  C     . LEU A 272 ? 0.248  0.294  0.718  -0.0087 -0.0049 -0.0091 273  LEU A C     
2237 O  O     . LEU A 272 ? 0.2549 0.3007 0.7244 -0.0088 -0.0056 -0.007  273  LEU A O     
2238 C  CB    . LEU A 272 ? 0.2768 0.3144 0.7362 -0.0078 -0.0081 -0.0121 273  LEU A CB    
2239 C  CG    . LEU A 272 ? 0.3028 0.3401 0.7632 -0.0063 -0.0057 -0.015  273  LEU A CG    
2240 C  CD1   . LEU A 272 ? 0.3079 0.3447 0.7665 -0.0074 -0.007  -0.0164 273  LEU A CD1   
2241 C  CD2   . LEU A 272 ? 0.3213 0.3546 0.7775 -0.0042 -0.0055 -0.016  273  LEU A CD2   
2242 N  N     . GLY A 273 ? 0.2283 0.2776 0.7034 -0.008  -0.002  -0.0102 274  GLY A N     
2243 C  CA    . GLY A 273 ? 0.212  0.2649 0.6929 -0.0073 0.0008  -0.0091 274  GLY A CA    
2244 C  C     . GLY A 273 ? 0.1914 0.2486 0.6764 -0.0084 0.0015  -0.0078 274  GLY A C     
2245 O  O     . GLY A 273 ? 0.1992 0.2596 0.6893 -0.0075 0.0042  -0.0073 274  GLY A O     
2246 N  N     . ARG A 274 ? 0.169  0.2265 0.6519 -0.01   -0.0009 -0.0071 275  ARG A N     
2247 C  CA    . ARG A 274 ? 0.1561 0.2179 0.6429 -0.0107 -0.0001 -0.0057 275  ARG A CA    
2248 C  C     . ARG A 274 ? 0.1469 0.2106 0.6371 -0.0092 0.0028  -0.0083 275  ARG A C     
2249 O  O     . ARG A 274 ? 0.1422 0.2097 0.6364 -0.0089 0.0046  -0.0074 275  ARG A O     
2250 C  CB    . ARG A 274 ? 0.1581 0.22   0.6423 -0.0128 -0.0033 -0.0038 275  ARG A CB    
2251 C  CG    . ARG A 274 ? 0.1679 0.2266 0.6478 -0.0131 -0.0051 -0.0061 275  ARG A CG    
2252 C  CD    . ARG A 274 ? 0.1765 0.2357 0.6547 -0.0153 -0.0082 -0.0036 275  ARG A CD    
2253 N  NE    . ARG A 274 ? 0.1658 0.2232 0.641  -0.0155 -0.0093 -0.0056 275  ARG A NE    
2254 C  CZ    . ARG A 274 ? 0.1593 0.2194 0.6366 -0.0147 -0.0077 -0.0069 275  ARG A CZ    
2255 N  NH1   . ARG A 274 ? 0.1416 0.2061 0.6238 -0.0137 -0.0049 -0.0064 275  ARG A NH1   
2256 N  NH2   . ARG A 274 ? 0.1467 0.2052 0.6212 -0.0149 -0.0087 -0.0086 275  ARG A NH2   
2257 N  N     . PHE A 275 ? 0.138  0.1992 0.6266 -0.0081 0.0034  -0.0116 276  PHE A N     
2258 C  CA    . PHE A 275 ? 0.1298 0.192  0.6215 -0.0066 0.006   -0.0145 276  PHE A CA    
2259 C  C     . PHE A 275 ? 0.1171 0.1764 0.6085 -0.0052 0.0071  -0.0165 276  PHE A C     
2260 O  O     . PHE A 275 ? 0.1167 0.1727 0.6039 -0.0055 0.0054  -0.0163 276  PHE A O     
2261 C  CB    . PHE A 275 ? 0.1291 0.1919 0.6195 -0.0067 0.0054  -0.0163 276  PHE A CB    
2262 C  CG    . PHE A 275 ? 0.1427 0.202  0.6278 -0.0074 0.0031  -0.0176 276  PHE A CG    
2263 C  CD1   . PHE A 275 ? 0.1582 0.2148 0.642  -0.0063 0.0037  -0.0205 276  PHE A CD1   
2264 C  CD2   . PHE A 275 ? 0.1497 0.2084 0.6314 -0.0091 0.0003  -0.0157 276  PHE A CD2   
2265 C  CE1   . PHE A 275 ? 0.1688 0.2222 0.6476 -0.0067 0.0017  -0.0216 276  PHE A CE1   
2266 C  CE2   . PHE A 275 ? 0.1658 0.221  0.6425 -0.0096 -0.0019 -0.0169 276  PHE A CE2   
2267 C  CZ    . PHE A 275 ? 0.1655 0.2181 0.6407 -0.0083 -0.001  -0.0199 276  PHE A CZ    
2268 N  N     . LYS A 276 ? 0.1112 0.1718 0.6071 -0.0038 0.0098  -0.0181 277  LYS A N     
2269 C  CA    . LYS A 276 ? 0.1129 0.1713 0.6096 -0.0024 0.0111  -0.0196 277  LYS A CA    
2270 C  C     . LYS A 276 ? 0.1057 0.1627 0.6017 -0.0018 0.0112  -0.023  277  LYS A C     
2271 O  O     . LYS A 276 ? 0.1085 0.1663 0.6034 -0.0023 0.0104  -0.0242 277  LYS A O     
2272 C  CB    . LYS A 276 ? 0.1433 0.2038 0.6461 -0.0013 0.0139  -0.0192 277  LYS A CB    
2273 C  CG    . LYS A 276 ? 0.2314 0.2932 0.7351 -0.0016 0.0141  -0.0159 277  LYS A CG    
2274 C  CD    . LYS A 276 ? 0.3161 0.3793 0.8255 -0.0002 0.017   -0.0156 277  LYS A CD    
2275 C  CE    . LYS A 276 ? 0.3921 0.4546 0.901  0.0003  0.0172  -0.0132 277  LYS A CE    
2276 N  NZ    . LYS A 276 ? 0.4345 0.4997 0.9492 0.0011  0.0198  -0.0116 277  LYS A NZ    
2277 N  N     . PHE A 277 ? 0.0966 0.1516 0.5932 -0.0006 0.0121  -0.0242 278  PHE A N     
2278 C  CA    . PHE A 277 ? 0.0958 0.1498 0.5926 0.0001  0.0125  -0.0272 278  PHE A CA    
2279 C  C     . PHE A 277 ? 0.1008 0.1569 0.6041 0.001   0.0149  -0.0286 278  PHE A C     
2280 O  O     . PHE A 277 ? 0.1118 0.1683 0.6191 0.0019  0.0166  -0.0278 278  PHE A O     
2281 C  CB    . PHE A 277 ? 0.0852 0.1361 0.5794 0.0009  0.0122  -0.0275 278  PHE A CB    
2282 C  CG    . PHE A 277 ? 0.0823 0.1326 0.5789 0.002   0.0133  -0.0301 278  PHE A CG    
2283 C  CD1   . PHE A 277 ? 0.0868 0.1378 0.5834 0.0016  0.0129  -0.0326 278  PHE A CD1   
2284 C  CD2   . PHE A 277 ? 0.0794 0.1286 0.5779 0.0033  0.0146  -0.0299 278  PHE A CD2   
2285 C  CE1   . PHE A 277 ? 0.0874 0.1379 0.5862 0.0025  0.0136  -0.035  278  PHE A CE1   
2286 C  CE2   . PHE A 277 ? 0.0838 0.1326 0.5847 0.0042  0.0154  -0.032  278  PHE A CE2   
2287 C  CZ    . PHE A 277 ? 0.0822 0.1316 0.5832 0.0037  0.0148  -0.0346 278  PHE A CZ    
2288 N  N     . ARG A 278 ? 0.0919 0.1495 0.5963 0.0009  0.0149  -0.0306 279  ARG A N     
2289 C  CA    . ARG A 278 ? 0.0863 0.1454 0.5963 0.0019  0.0168  -0.0324 279  ARG A CA    
2290 C  C     . ARG A 278 ? 0.0728 0.1313 0.583  0.0024  0.0166  -0.0358 279  ARG A C     
2291 O  O     . ARG A 278 ? 0.0658 0.1253 0.5747 0.0023  0.0159  -0.0373 279  ARG A O     
2292 C  CB    . ARG A 278 ? 0.1001 0.1621 0.6117 0.0018  0.0174  -0.0314 279  ARG A CB    
2293 C  CG    . ARG A 278 ? 0.1522 0.2152 0.6635 0.0011  0.0174  -0.0278 279  ARG A CG    
2294 C  CD    . ARG A 278 ? 0.1879 0.2539 0.7022 0.0014  0.0187  -0.0268 279  ARG A CD    
2295 N  NE    . ARG A 278 ? 0.2335 0.3007 0.7478 0.0007  0.0187  -0.0231 279  ARG A NE    
2296 C  CZ    . ARG A 278 ? 0.242  0.31   0.7603 0.0013  0.0205  -0.0217 279  ARG A CZ    
2297 N  NH1   . ARG A 278 ? 0.2138 0.2813 0.7366 0.0026  0.0224  -0.0235 279  ARG A NH1   
2298 N  NH2   . ARG A 278 ? 0.2435 0.3129 0.7616 0.0007  0.0204  -0.0183 279  ARG A NH2   
2299 N  N     . LYS A 279 ? 0.0694 0.1263 0.5815 0.0031  0.0171  -0.0369 280  LYS A N     
2300 C  CA    . LYS A 279 ? 0.0612 0.1173 0.574  0.0035  0.0168  -0.04   280  LYS A CA    
2301 C  C     . LYS A 279 ? 0.0647 0.1224 0.5819 0.0042  0.0177  -0.0424 280  LYS A C     
2302 O  O     . LYS A 279 ? 0.0636 0.1221 0.5857 0.0047  0.0192  -0.042  280  LYS A O     
2303 C  CB    . LYS A 279 ? 0.0589 0.1133 0.574  0.0042  0.0175  -0.0401 280  LYS A CB    
2304 C  CG    . LYS A 279 ? 0.0608 0.1147 0.5782 0.0047  0.0174  -0.043  280  LYS A CG    
2305 C  CD    . LYS A 279 ? 0.0717 0.1248 0.5839 0.0042  0.0156  -0.0445 280  LYS A CD    
2306 C  CE    . LYS A 279 ? 0.0701 0.1231 0.5851 0.0047  0.0155  -0.0475 280  LYS A CE    
2307 N  NZ    . LYS A 279 ? 0.0646 0.1167 0.5748 0.0045  0.014   -0.0487 280  LYS A NZ    
2308 N  N     . LYS A 280 ? 0.0679 0.126  0.5832 0.0042  0.0167  -0.0449 281  LYS A N     
2309 C  CA    . LYS A 280 ? 0.0812 0.1403 0.5997 0.0051  0.0172  -0.0475 281  LYS A CA    
2310 C  C     . LYS A 280 ? 0.086  0.1438 0.6079 0.0056  0.0172  -0.0501 281  LYS A C     
2311 O  O     . LYS A 280 ? 0.0952 0.1519 0.6145 0.0053  0.0161  -0.0511 281  LYS A O     
2312 C  CB    . LYS A 280 ? 0.121  0.1815 0.6357 0.0052  0.0161  -0.0488 281  LYS A CB    
2313 C  CG    . LYS A 280 ? 0.1884 0.2509 0.7007 0.0049  0.0162  -0.0462 281  LYS A CG    
2314 C  CD    . LYS A 280 ? 0.2423 0.3061 0.7504 0.005   0.015   -0.0471 281  LYS A CD    
2315 C  CE    . LYS A 280 ? 0.3093 0.3755 0.8159 0.0049  0.0151  -0.0444 281  LYS A CE    
2316 N  NZ    . LYS A 280 ? 0.3399 0.4078 0.8433 0.0054  0.0143  -0.0452 281  LYS A NZ    
2317 N  N     . ILE A 281 ? 0.0774 0.1351 0.6051 0.0063  0.0184  -0.051  282  ILE A N     
2318 C  CA    . ILE A 281 ? 0.0761 0.1326 0.608  0.0067  0.0182  -0.0534 282  ILE A CA    
2319 C  C     . ILE A 281 ? 0.084  0.1408 0.6189 0.0076  0.0183  -0.0563 282  ILE A C     
2320 O  O     . ILE A 281 ? 0.0944 0.1519 0.6314 0.0081  0.0194  -0.0556 282  ILE A O     
2321 C  CB    . ILE A 281 ? 0.0766 0.1323 0.6136 0.0067  0.0196  -0.0514 282  ILE A CB    
2322 C  CG1   . ILE A 281 ? 0.0939 0.1491 0.6273 0.0062  0.0196  -0.0484 282  ILE A CG1   
2323 C  CG2   . ILE A 281 ? 0.0709 0.1256 0.6133 0.007   0.0193  -0.0536 282  ILE A CG2   
2324 C  CD1   . ILE A 281 ? 0.1101 0.1648 0.648  0.0066  0.021   -0.046  282  ILE A CD1   
2325 N  N     . ALA A 282 ? 0.0805 0.1368 0.6153 0.0079  0.0169  -0.0597 283  ALA A N     
2326 C  CA    . ALA A 282 ? 0.0831 0.1392 0.6203 0.009   0.0167  -0.0629 283  ALA A CA    
2327 C  C     . ALA A 282 ? 0.0966 0.1515 0.6411 0.0092  0.0177  -0.063  283  ALA A C     
2328 O  O     . ALA A 282 ? 0.0994 0.1535 0.6474 0.0086  0.018   -0.0618 283  ALA A O     
2329 C  CB    . ALA A 282 ? 0.0767 0.1323 0.6124 0.0092  0.0148  -0.0663 283  ALA A CB    
2330 N  N     . GLU A 283 ? 0.0985 0.1533 0.6454 0.0103  0.0182  -0.0644 284  GLU A N     
2331 C  CA    . GLU A 283 ? 0.111  0.1646 0.665  0.0106  0.0192  -0.0647 284  GLU A CA    
2332 C  C     . GLU A 283 ? 0.1005 0.1523 0.659  0.0103  0.0178  -0.0671 284  GLU A C     
2333 O  O     . GLU A 283 ? 0.1023 0.1534 0.6667 0.0099  0.0185  -0.0659 284  GLU A O     
2334 C  CB    . GLU A 283 ? 0.1552 0.2087 0.7102 0.012   0.0199  -0.0659 284  GLU A CB    
2335 C  CG    . GLU A 283 ? 0.2585 0.3109 0.8207 0.0123  0.0213  -0.0654 284  GLU A CG    
2336 C  CD    . GLU A 283 ? 0.4265 0.4788 0.989  0.0138  0.0223  -0.066  284  GLU A CD    
2337 O  OE1   . GLU A 283 ? 0.4805 0.5348 1.0388 0.0142  0.0233  -0.064  284  GLU A OE1   
2338 O  OE2   . GLU A 283 ? 0.4668 0.5171 1.034  0.0146  0.0221  -0.0685 284  GLU A OE2   
2339 N  N     . LYS A 284 ? 0.0917 0.1431 0.6473 0.0105  0.0159  -0.0703 285  LYS A N     
2340 C  CA    . LYS A 284 ? 0.0855 0.1354 0.6451 0.01    0.0143  -0.0726 285  LYS A CA    
2341 C  C     . LYS A 284 ? 0.0739 0.1241 0.6349 0.0089  0.0145  -0.07   285  LYS A C     
2342 O  O     . LYS A 284 ? 0.0755 0.1248 0.6416 0.0084  0.0137  -0.0707 285  LYS A O     
2343 C  CB    . LYS A 284 ? 0.1081 0.1579 0.6637 0.0106  0.0121  -0.0764 285  LYS A CB    
2344 C  CG    . LYS A 284 ? 0.1425 0.194  0.691  0.0102  0.0117  -0.0754 285  LYS A CG    
2345 C  CD    . LYS A 284 ? 0.1803 0.2318 0.725  0.0109  0.0097  -0.079  285  LYS A CD    
2346 C  CE    . LYS A 284 ? 0.1947 0.2478 0.7326 0.0105  0.0094  -0.0779 285  LYS A CE    
2347 N  NZ    . LYS A 284 ? 0.1922 0.2459 0.726  0.0115  0.0078  -0.0812 285  LYS A NZ    
2348 N  N     . SER A 285 ? 0.0533 0.1048 0.6098 0.0084  0.0155  -0.0668 286  SER A N     
2349 C  CA    . SER A 285 ? 0.0457 0.0973 0.6028 0.0077  0.0158  -0.0642 286  SER A CA    
2350 C  C     . SER A 285 ? 0.0447 0.0963 0.6071 0.0077  0.0177  -0.061  286  SER A C     
2351 O  O     . SER A 285 ? 0.0424 0.094  0.6064 0.0074  0.0181  -0.0588 286  SER A O     
2352 C  CB    . SER A 285 ? 0.0422 0.0948 0.5916 0.0073  0.0158  -0.0624 286  SER A CB    
2353 O  OG    . SER A 285 ? 0.0522 0.1051 0.5964 0.0075  0.0143  -0.065  286  SER A OG    
2354 N  N     . LEU A 286 ? 0.0506 0.1023 0.6155 0.0081  0.019   -0.0604 287  LEU A N     
2355 C  CA    . LEU A 286 ? 0.0641 0.1162 0.634  0.0082  0.021   -0.0571 287  LEU A CA    
2356 C  C     . LEU A 286 ? 0.0892 0.1404 0.6675 0.0082  0.0211  -0.0572 287  LEU A C     
2357 O  O     . LEU A 286 ? 0.0944 0.1444 0.6764 0.0082  0.0197  -0.0603 287  LEU A O     
2358 C  CB    . LEU A 286 ? 0.0658 0.1184 0.6359 0.0087  0.0224  -0.0562 287  LEU A CB    
2359 C  CG    . LEU A 286 ? 0.0651 0.119  0.6277 0.0087  0.0226  -0.0549 287  LEU A CG    
2360 C  CD1   . LEU A 286 ? 0.0702 0.1248 0.6339 0.0093  0.024   -0.0543 287  LEU A CD1   
2361 C  CD2   . LEU A 286 ? 0.0546 0.1093 0.6142 0.0082  0.0233  -0.0513 287  LEU A CD2   
2362 N  N     . SER A 287 ? 0.0962 0.148  0.6775 0.0083  0.0226  -0.0536 288  SER A N     
2363 C  CA    . SER A 287 ? 0.0986 0.1502 0.6886 0.0084  0.0231  -0.0524 288  SER A CA    
2364 C  C     . SER A 287 ? 0.0977 0.1505 0.689  0.0089  0.0254  -0.0477 288  SER A C     
2365 O  O     . SER A 287 ? 0.1103 0.1638 0.6952 0.0091  0.0261  -0.0458 288  SER A O     
2366 C  CB    . SER A 287 ? 0.1145 0.1656 0.7057 0.008   0.0214  -0.0536 288  SER A CB    
2367 O  OG    . SER A 287 ? 0.1668 0.2186 0.7526 0.0081  0.0218  -0.0512 288  SER A OG    
2368 N  N     . GLY A 288 ? 0.0774 0.1304 0.6769 0.0093  0.0265  -0.0458 289  GLY A N     
2369 C  CA    . GLY A 288 ? 0.0754 0.1298 0.6772 0.0101  0.0288  -0.0413 289  GLY A CA    
2370 C  C     . GLY A 288 ? 0.0701 0.1253 0.6681 0.0106  0.0304  -0.0394 289  GLY A C     
2371 O  O     . GLY A 288 ? 0.0784 0.1334 0.6773 0.0104  0.0306  -0.0408 289  GLY A O     
2372 N  N     . LYS A 289 ? 0.0562 0.1123 0.6491 0.0111  0.0312  -0.0363 290  LYS A N     
2373 C  CA    . LYS A 289 ? 0.0491 0.106  0.6378 0.0114  0.0324  -0.0344 290  LYS A CA    
2374 C  C     . LYS A 289 ? 0.0601 0.1167 0.639  0.0108  0.031   -0.0354 290  LYS A C     
2375 O  O     . LYS A 289 ? 0.0647 0.122  0.6392 0.011   0.0316  -0.0332 290  LYS A O     
2376 C  CB    . LYS A 289 ? 0.0672 0.1253 0.6577 0.0127  0.0344  -0.03   290  LYS A CB    
2377 C  CG    . LYS A 289 ? 0.1263 0.1853 0.7271 0.0134  0.0362  -0.0283 290  LYS A CG    
2378 C  CD    . LYS A 289 ? 0.181  0.2412 0.7842 0.0149  0.0378  -0.0243 290  LYS A CD    
2379 C  CE    . LYS A 289 ? 0.2429 0.3043 0.8561 0.0157  0.0399  -0.0219 290  LYS A CE    
2380 N  NZ    . LYS A 289 ? 0.2647 0.3275 0.8806 0.0174  0.0415  -0.0177 290  LYS A NZ    
2381 N  N     . VAL A 290 ? 0.0583 0.1139 0.6341 0.01    0.029   -0.0387 291  VAL A N     
2382 C  CA    . VAL A 290 ? 0.0579 0.1131 0.6248 0.0094  0.0275  -0.0398 291  VAL A CA    
2383 C  C     . VAL A 290 ? 0.0649 0.1209 0.6286 0.0091  0.0278  -0.0394 291  VAL A C     
2384 O  O     . VAL A 290 ? 0.0701 0.1263 0.6276 0.0089  0.0276  -0.0376 291  VAL A O     
2385 C  CB    . VAL A 290 ? 0.0682 0.1225 0.6335 0.0087  0.0255  -0.0435 291  VAL A CB    
2386 C  CG1   . VAL A 290 ? 0.0785 0.1327 0.6352 0.0081  0.024   -0.0446 291  VAL A CG1   
2387 C  CG2   . VAL A 290 ? 0.0753 0.1291 0.6429 0.009   0.0251  -0.0431 291  VAL A CG2   
2388 N  N     . LYS A 291 ? 0.0564 0.1128 0.6241 0.0091  0.0284  -0.0408 292  LYS A N     
2389 C  CA    . LYS A 291 ? 0.0595 0.1168 0.6244 0.009   0.0289  -0.0403 292  LYS A CA    
2390 C  C     . LYS A 291 ? 0.0626 0.1211 0.627  0.0093  0.0304  -0.0363 292  LYS A C     
2391 O  O     . LYS A 291 ? 0.0784 0.1376 0.6373 0.0089  0.03    -0.035  292  LYS A O     
2392 C  CB    . LYS A 291 ? 0.0748 0.1321 0.6444 0.0094  0.0294  -0.0424 292  LYS A CB    
2393 C  CG    . LYS A 291 ? 0.1343 0.1929 0.7009 0.0095  0.0299  -0.0418 292  LYS A CG    
2394 C  CD    . LYS A 291 ? 0.2178 0.2759 0.7877 0.0101  0.0301  -0.0446 292  LYS A CD    
2395 C  CE    . LYS A 291 ? 0.2975 0.357  0.8655 0.0105  0.0311  -0.0436 292  LYS A CE    
2396 N  NZ    . LYS A 291 ? 0.3678 0.4286 0.9284 0.0099  0.0301  -0.0424 292  LYS A NZ    
2397 N  N     . GLU A 292 ? 0.0549 0.1137 0.6249 0.0101  0.032   -0.0342 293  GLU A N     
2398 C  CA    . GLU A 292 ? 0.0602 0.1202 0.6299 0.0106  0.0335  -0.0303 293  GLU A CA    
2399 C  C     . GLU A 292 ? 0.0547 0.1142 0.6176 0.0106  0.0326  -0.0286 293  GLU A C     
2400 O  O     . GLU A 292 ? 0.0551 0.1154 0.6144 0.0106  0.0328  -0.0262 293  GLU A O     
2401 C  CB    . GLU A 292 ? 0.103  0.1637 0.6811 0.0117  0.0357  -0.0285 293  GLU A CB    
2402 C  CG    . GLU A 292 ? 0.2373 0.2996 0.8164 0.0124  0.0376  -0.0247 293  GLU A CG    
2403 C  CD    . GLU A 292 ? 0.3856 0.4491 0.9601 0.0119  0.0376  -0.0237 293  GLU A CD    
2404 O  OE1   . GLU A 292 ? 0.4124 0.4762 0.9816 0.012   0.0373  -0.0214 293  GLU A OE1   
2405 O  OE2   . GLU A 292 ? 0.4283 0.4922 1.0043 0.0116  0.0379  -0.0251 293  GLU A OE2   
2406 N  N     . PHE A 293 ? 0.0443 0.1025 0.6053 0.0106  0.0313  -0.0299 294  PHE A N     
2407 C  CA    . PHE A 293 ? 0.0442 0.1015 0.598  0.0106  0.0302  -0.0286 294  PHE A CA    
2408 C  C     . PHE A 293 ? 0.0476 0.1046 0.5943 0.0094  0.0285  -0.0295 294  PHE A C     
2409 O  O     . PHE A 293 ? 0.0517 0.1085 0.593  0.0094  0.028   -0.0275 294  PHE A O     
2410 C  CB    . PHE A 293 ? 0.0443 0.1002 0.5976 0.0109  0.0293  -0.0299 294  PHE A CB    
2411 C  CG    . PHE A 293 ? 0.0499 0.1045 0.5953 0.0111  0.0282  -0.0287 294  PHE A CG    
2412 C  CD1   . PHE A 293 ? 0.0592 0.1136 0.6033 0.0125  0.0291  -0.0256 294  PHE A CD1   
2413 C  CD2   . PHE A 293 ? 0.0609 0.1144 0.5998 0.0101  0.0261  -0.0308 294  PHE A CD2   
2414 C  CE1   . PHE A 293 ? 0.0751 0.1278 0.6114 0.0128  0.0279  -0.0247 294  PHE A CE1   
2415 C  CE2   . PHE A 293 ? 0.0735 0.1254 0.6051 0.0103  0.0249  -0.0298 294  PHE A CE2   
2416 C  CZ    . PHE A 293 ? 0.0723 0.1237 0.6025 0.0117  0.0258  -0.0268 294  PHE A CZ    
2417 N  N     . ASN A 294 ? 0.0449 0.102  0.5914 0.0086  0.0275  -0.0325 295  ASN A N     
2418 C  CA    . ASN A 294 ? 0.0443 0.1015 0.5847 0.0076  0.026   -0.0332 295  ASN A CA    
2419 C  C     . ASN A 294 ? 0.0636 0.1223 0.6035 0.0074  0.0268  -0.0307 295  ASN A C     
2420 O  O     . ASN A 294 ? 0.0687 0.1274 0.603  0.0067  0.0256  -0.0294 295  ASN A O     
2421 C  CB    . ASN A 294 ? 0.0426 0.0999 0.5835 0.0071  0.0252  -0.0367 295  ASN A CB    
2422 C  CG    . ASN A 294 ? 0.049  0.1062 0.583  0.0062  0.0233  -0.0376 295  ASN A CG    
2423 O  OD1   . ASN A 294 ? 0.049  0.1056 0.5777 0.0057  0.0223  -0.0359 295  ASN A OD1   
2424 N  ND2   . ASN A 294 ? 0.0421 0.0997 0.576  0.0061  0.0226  -0.0402 295  ASN A ND2   
2425 N  N     . ASN A 295 ? 0.0657 0.1257 0.6119 0.008   0.0288  -0.0298 296  ASN A N     
2426 C  CA    . ASN A 295 ? 0.0731 0.1348 0.6196 0.008   0.0299  -0.0271 296  ASN A CA    
2427 C  C     . ASN A 295 ? 0.0605 0.122  0.6036 0.0082  0.0297  -0.0239 296  ASN A C     
2428 O  O     . ASN A 295 ? 0.0594 0.1217 0.5987 0.0076  0.029   -0.0221 296  ASN A O     
2429 C  CB    . ASN A 295 ? 0.1284 0.1912 0.6826 0.0089  0.0322  -0.0267 296  ASN A CB    
2430 C  CG    . ASN A 295 ? 0.2412 0.3043 0.7987 0.0089  0.0324  -0.0296 296  ASN A CG    
2431 O  OD1   . ASN A 295 ? 0.2811 0.3441 0.8451 0.0096  0.0338  -0.0303 296  ASN A OD1   
2432 N  ND2   . ASN A 295 ? 0.2654 0.3286 0.8184 0.0083  0.031   -0.0312 296  ASN A ND2   
2433 N  N     . ILE A 296 ? 0.0553 0.1158 0.5996 0.0092  0.0303  -0.0232 297  ILE A N     
2434 C  CA    . ILE A 296 ? 0.0599 0.1199 0.6007 0.0099  0.0301  -0.0204 297  ILE A CA    
2435 C  C     . ILE A 296 ? 0.0815 0.1397 0.6137 0.009   0.0276  -0.0206 297  ILE A C     
2436 O  O     . ILE A 296 ? 0.0819 0.1401 0.6098 0.0087  0.0267  -0.0185 297  ILE A O     
2437 C  CB    . ILE A 296 ? 0.0595 0.1189 0.6039 0.0115  0.0315  -0.0195 297  ILE A CB    
2438 C  CG1   . ILE A 296 ? 0.0668 0.1281 0.6198 0.0124  0.0341  -0.0184 297  ILE A CG1   
2439 C  CG2   . ILE A 296 ? 0.0626 0.1209 0.6018 0.0125  0.0311  -0.017  297  ILE A CG2   
2440 C  CD1   . ILE A 296 ? 0.0859 0.1469 0.6442 0.0138  0.0354  -0.0181 297  ILE A CD1   
2441 N  N     . VAL A 297 ? 0.0804 0.1372 0.6102 0.0084  0.0261  -0.0233 298  VAL A N     
2442 C  CA    . VAL A 297 ? 0.0794 0.1346 0.6014 0.0074  0.0237  -0.0237 298  VAL A CA    
2443 C  C     . VAL A 297 ? 0.0874 0.1438 0.607  0.006   0.0226  -0.023  298  VAL A C     
2444 O  O     . VAL A 297 ? 0.1024 0.158  0.6168 0.0054  0.0211  -0.0213 298  VAL A O     
2445 C  CB    . VAL A 297 ? 0.0757 0.1295 0.596  0.007   0.0225  -0.0267 298  VAL A CB    
2446 C  CG1   . VAL A 297 ? 0.0663 0.1185 0.5789 0.006   0.02    -0.0271 298  VAL A CG1   
2447 C  CG2   . VAL A 297 ? 0.0738 0.1264 0.5961 0.0084  0.0233  -0.0269 298  VAL A CG2   
2448 N  N     . GLN A 298 ? 0.0766 0.1349 0.6    0.0055  0.0234  -0.0242 299  GLN A N     
2449 C  CA    . GLN A 298 ? 0.0832 0.1432 0.6048 0.0044  0.0226  -0.0233 299  GLN A CA    
2450 C  C     . GLN A 298 ? 0.0861 0.1475 0.6086 0.0044  0.0234  -0.0199 299  GLN A C     
2451 O  O     . GLN A 298 ? 0.0929 0.1555 0.613  0.0034  0.0223  -0.0184 299  GLN A O     
2452 C  CB    . GLN A 298 ? 0.1003 0.1619 0.6254 0.0043  0.0234  -0.0254 299  GLN A CB    
2453 C  CG    . GLN A 298 ? 0.1152 0.1754 0.6388 0.0042  0.0223  -0.0287 299  GLN A CG    
2454 C  CD    . GLN A 298 ? 0.1368 0.1985 0.6622 0.0042  0.0225  -0.0308 299  GLN A CD    
2455 O  OE1   . GLN A 298 ? 0.1777 0.2413 0.7035 0.004   0.0229  -0.0296 299  GLN A OE1   
2456 N  NE2   . GLN A 298 ? 0.1196 0.1804 0.6458 0.0046  0.0223  -0.034  299  GLN A NE2   
2457 N  N     . ARG A 299 ? 0.0722 0.1338 0.5982 0.0057  0.0252  -0.0185 300  ARG A N     
2458 C  CA    . ARG A 299 ? 0.074  0.1369 0.6007 0.006   0.0259  -0.0152 300  ARG A CA    
2459 C  C     . ARG A 299 ? 0.0842 0.1453 0.6041 0.0056  0.0238  -0.0134 300  ARG A C     
2460 O  O     . ARG A 299 ? 0.0978 0.1601 0.6166 0.0052  0.0234  -0.0109 300  ARG A O     
2461 C  CB    . ARG A 299 ? 0.0841 0.1476 0.6168 0.0077  0.0286  -0.0144 300  ARG A CB    
2462 C  CG    . ARG A 299 ? 0.1168 0.1821 0.6512 0.0084  0.0299  -0.011  300  ARG A CG    
2463 C  CD    . ARG A 299 ? 0.1483 0.2145 0.6895 0.0101  0.0327  -0.0102 300  ARG A CD    
2464 N  NE    . ARG A 299 ? 0.1901 0.2573 0.7376 0.0101  0.0343  -0.0121 300  ARG A NE    
2465 C  CZ    . ARG A 299 ? 0.2351 0.302  0.7884 0.0112  0.036   -0.013  300  ARG A CZ    
2466 N  NH1   . ARG A 299 ? 0.2191 0.2852 0.773  0.0125  0.0365  -0.0119 300  ARG A NH1   
2467 N  NH2   . ARG A 299 ? 0.2559 0.3233 0.8145 0.0111  0.037   -0.015  300  ARG A NH2   
2468 N  N     . TYR A 300 ? 0.0813 0.1397 0.5969 0.0059  0.0223  -0.0147 301  TYR A N     
2469 C  CA    . TYR A 300 ? 0.0852 0.1413 0.5941 0.0059  0.0203  -0.0133 301  TYR A CA    
2470 C  C     . TYR A 300 ? 0.081  0.1347 0.5834 0.0046  0.0174  -0.0146 301  TYR A C     
2471 O  O     . TYR A 300 ? 0.0857 0.1376 0.5825 0.0042  0.0152  -0.0134 301  TYR A O     
2472 C  CB    . TYR A 300 ? 0.0823 0.1367 0.5912 0.0081  0.0214  -0.0129 301  TYR A CB    
2473 C  CG    . TYR A 300 ? 0.0923 0.1489 0.6074 0.0096  0.0242  -0.011  301  TYR A CG    
2474 C  CD1   . TYR A 300 ? 0.1144 0.1722 0.629  0.0099  0.0244  -0.0081 301  TYR A CD1   
2475 C  CD2   . TYR A 300 ? 0.0933 0.1511 0.6151 0.0106  0.0267  -0.0119 301  TYR A CD2   
2476 C  CE1   . TYR A 300 ? 0.1183 0.1785 0.6388 0.0113  0.0271  -0.0062 301  TYR A CE1   
2477 C  CE2   . TYR A 300 ? 0.1081 0.168  0.6361 0.012   0.0293  -0.01   301  TYR A CE2   
2478 C  CZ    . TYR A 300 ? 0.1269 0.1881 0.6542 0.0124  0.0296  -0.0071 301  TYR A CZ    
2479 O  OH    . TYR A 300 ? 0.146  0.2095 0.6794 0.0138  0.0324  -0.0051 301  TYR A OH    
2480 N  N     . SER A 301 ? 0.0801 0.1338 0.5833 0.004   0.0172  -0.0172 302  SER A N     
2481 C  CA    . SER A 301 ? 0.0897 0.141  0.5868 0.003   0.0146  -0.0187 302  SER A CA    
2482 C  C     . SER A 301 ? 0.0978 0.1495 0.5914 0.0011  0.0122  -0.0177 302  SER A C     
2483 O  O     . SER A 301 ? 0.0971 0.1515 0.5935 0.0003  0.0127  -0.0163 302  SER A O     
2484 C  CB    . SER A 301 ? 0.1073 0.1587 0.6065 0.003   0.0152  -0.0217 302  SER A CB    
2485 O  OG    . SER A 301 ? 0.1525 0.2066 0.655  0.0021  0.0157  -0.0224 302  SER A OG    
2486 N  N     . VAL A 302 ? 0.0981 0.1469 0.5853 0.0004  0.0097  -0.0182 303  VAL A N     
2487 C  CA    . VAL A 302 ? 0.1018 0.1504 0.5853 -0.0016 0.007   -0.0175 303  VAL A CA    
2488 C  C     . VAL A 302 ? 0.1041 0.1515 0.5855 -0.0019 0.0062  -0.0201 303  VAL A C     
2489 O  O     . VAL A 302 ? 0.1178 0.1632 0.5981 -0.0007 0.0068  -0.0218 303  VAL A O     
2490 C  CB    . VAL A 302 ? 0.1146 0.1605 0.5925 -0.0021 0.0043  -0.0154 303  VAL A CB    
2491 C  CG1   . VAL A 302 ? 0.1226 0.1702 0.6029 -0.0019 0.0052  -0.0128 303  VAL A CG1   
2492 C  CG2   . VAL A 302 ? 0.1203 0.162  0.593  -0.0008 0.0035  -0.0164 303  VAL A CG2   
2493 N  N     . GLY A 303 ? 0.0956 0.1448 0.5773 -0.0033 0.0053  -0.0203 304  GLY A N     
2494 C  CA    . GLY A 303 ? 0.0951 0.1437 0.5752 -0.0035 0.0048  -0.0226 304  GLY A CA    
2495 C  C     . GLY A 303 ? 0.0934 0.1383 0.5669 -0.004  0.0022  -0.023  304  GLY A C     
2496 O  O     . GLY A 303 ? 0.107  0.1501 0.5767 -0.0049 0       -0.0211 304  GLY A O     
2497 N  N     . LEU A 304 ? 0.0749 0.1185 0.5471 -0.0034 0.0024  -0.0254 305  LEU A N     
2498 C  CA    . LEU A 304 ? 0.0874 0.1274 0.5533 -0.0037 0.0001  -0.0259 305  LEU A CA    
2499 C  C     . LEU A 304 ? 0.074  0.1155 0.5398 -0.0046 -0.0004 -0.0273 305  LEU A C     
2500 O  O     . LEU A 304 ? 0.077  0.1199 0.5455 -0.0037 0.0011  -0.0295 305  LEU A O     
2501 C  CB    . LEU A 304 ? 0.1023 0.1397 0.5667 -0.0019 0.0011  -0.0274 305  LEU A CB    
2502 C  CG    . LEU A 304 ? 0.1531 0.1862 0.6107 -0.0017 -0.0009 -0.0278 305  LEU A CG    
2503 C  CD1   . LEU A 304 ? 0.1809 0.2111 0.634  -0.002  -0.0029 -0.0256 305  LEU A CD1   
2504 C  CD2   . LEU A 304 ? 0.1701 0.2016 0.6273 0.0003  0.0006  -0.029  305  LEU A CD2   
2505 N  N     . ALA A 305 ? 0.0618 0.1033 0.5251 -0.0062 -0.0027 -0.0258 306  ALA A N     
2506 C  CA    . ALA A 305 ? 0.0594 0.1026 0.5224 -0.0071 -0.0036 -0.0264 306  ALA A CA    
2507 C  C     . ALA A 305 ? 0.0533 0.1012 0.5216 -0.007  -0.0018 -0.0266 306  ALA A C     
2508 O  O     . ALA A 305 ? 0.0444 0.0944 0.5128 -0.0081 -0.0028 -0.0253 306  ALA A O     
2509 C  CB    . ALA A 305 ? 0.0695 0.1107 0.5296 -0.0064 -0.0037 -0.0289 306  ALA A CB    
2510 N  N     . SER A 306 ? 0.0544 0.1039 0.5269 -0.0056 0.0007  -0.0282 307  SER A N     
2511 C  CA    . SER A 306 ? 0.0587 0.1122 0.5361 -0.0051 0.0026  -0.0288 307  SER A CA    
2512 C  C     . SER A 306 ? 0.064  0.1182 0.5459 -0.0039 0.0049  -0.0293 307  SER A C     
2513 O  O     . SER A 306 ? 0.0549 0.1068 0.5366 -0.0031 0.0055  -0.0303 307  SER A O     
2514 C  CB    . SER A 306 ? 0.0767 0.1313 0.5542 -0.0044 0.0031  -0.0316 307  SER A CB    
2515 O  OG    . SER A 306 ? 0.1056 0.1601 0.5796 -0.0053 0.0011  -0.0309 307  SER A OG    
2516 N  N     . SER A 307 ? 0.0749 0.1323 0.5609 -0.0038 0.0063  -0.0283 308  SER A N     
2517 C  CA    . SER A 307 ? 0.0779 0.1361 0.5686 -0.0027 0.0085  -0.0286 308  SER A CA    
2518 C  C     . SER A 307 ? 0.0828 0.1406 0.5759 -0.0013 0.01    -0.032  308  SER A C     
2519 O  O     . SER A 307 ? 0.088  0.1449 0.5839 -0.0005 0.0113  -0.0325 308  SER A O     
2520 C  CB    . SER A 307 ? 0.1069 0.1684 0.6011 -0.0027 0.0096  -0.0269 308  SER A CB    
2521 O  OG    . SER A 307 ? 0.1581 0.2219 0.6532 -0.0022 0.01    -0.0283 308  SER A OG    
2522 N  N     . ASP A 308 ? 0.0685 0.127  0.5606 -0.0011 0.0096  -0.0342 309  ASP A N     
2523 C  CA    . ASP A 308 ? 0.0647 0.1231 0.5594 0.0001  0.0107  -0.0374 309  ASP A CA    
2524 C  C     . ASP A 308 ? 0.065  0.1212 0.5566 0.0001  0.0097  -0.0393 309  ASP A C     
2525 O  O     . ASP A 308 ? 0.0703 0.1266 0.5638 0.001   0.0103  -0.042  309  ASP A O     
2526 C  CB    . ASP A 308 ? 0.0881 0.1493 0.5853 0.001   0.0115  -0.0391 309  ASP A CB    
2527 C  CG    . ASP A 308 ? 0.1772 0.2398 0.6709 0.0006  0.0102  -0.0391 309  ASP A CG    
2528 O  OD1   . ASP A 308 ? 0.2019 0.2636 0.6916 -0.0006 0.0086  -0.0371 309  ASP A OD1   
2529 O  OD2   . ASP A 308 ? 0.2015 0.2659 0.6963 0.0017  0.0108  -0.041  309  ASP A OD2   
2530 N  N     . LEU A 309 ? 0.0576 0.1114 0.5447 -0.0006 0.0082  -0.0378 310  LEU A N     
2531 C  CA    . LEU A 309 ? 0.0652 0.1166 0.5496 -0.0003 0.0076  -0.0393 310  LEU A CA    
2532 C  C     . LEU A 309 ? 0.0604 0.1108 0.5486 0.0007  0.0092  -0.0398 310  LEU A C     
2533 O  O     . LEU A 309 ? 0.0559 0.107  0.5472 0.0009  0.0103  -0.0383 310  LEU A O     
2534 C  CB    . LEU A 309 ? 0.0636 0.1123 0.542  -0.0013 0.0056  -0.0375 310  LEU A CB    
2535 C  CG    . LEU A 309 ? 0.0701 0.1191 0.5445 -0.0022 0.0038  -0.0376 310  LEU A CG    
2536 C  CD1   . LEU A 309 ? 0.0726 0.1185 0.5415 -0.0031 0.0017  -0.0357 310  LEU A CD1   
2537 C  CD2   . LEU A 309 ? 0.079  0.1282 0.553  -0.0015 0.004   -0.0404 310  LEU A CD2   
2538 N  N     . PRO A 310 ? 0.0609 0.11   0.5493 0.0015  0.0095  -0.0416 311  PRO A N     
2539 C  CA    . PRO A 310 ? 0.055  0.1037 0.5479 0.0025  0.0111  -0.0417 311  PRO A CA    
2540 C  C     . PRO A 310 ? 0.0569 0.1035 0.548  0.0029  0.0113  -0.0392 311  PRO A C     
2541 O  O     . PRO A 310 ? 0.0767 0.1225 0.5701 0.004   0.0123  -0.0392 311  PRO A O     
2542 C  CB    . PRO A 310 ? 0.0595 0.1079 0.5533 0.0031  0.0111  -0.0442 311  PRO A CB    
2543 C  CG    . PRO A 310 ? 0.0594 0.1067 0.5469 0.0025  0.0093  -0.0446 311  PRO A CG    
2544 C  CD    . PRO A 310 ? 0.0418 0.0891 0.5259 0.0014  0.0084  -0.0435 311  PRO A CD    
2545 N  N     . PHE A 311 ? 0.0469 0.0925 0.5338 0.0022  0.0101  -0.0371 312  PHE A N     
2546 C  CA    . PHE A 311 ? 0.0554 0.0988 0.5398 0.0028  0.0101  -0.0349 312  PHE A CA    
2547 C  C     . PHE A 311 ? 0.07   0.1136 0.5526 0.0019  0.0092  -0.0325 312  PHE A C     
2548 O  O     . PHE A 311 ? 0.0843 0.1291 0.5658 0.0006  0.0081  -0.0324 312  PHE A O     
2549 C  CB    . PHE A 311 ? 0.0527 0.0929 0.5311 0.0033  0.0088  -0.035  312  PHE A CB    
2550 C  CG    . PHE A 311 ? 0.06   0.0995 0.5336 0.0021  0.0068  -0.036  312  PHE A CG    
2551 C  CD1   . PHE A 311 ? 0.0693 0.1078 0.5387 0.0009  0.0049  -0.0345 312  PHE A CD1   
2552 C  CD2   . PHE A 311 ? 0.0649 0.1048 0.5385 0.0022  0.0067  -0.0383 312  PHE A CD2   
2553 C  CE1   . PHE A 311 ? 0.0793 0.1175 0.545  -0.0002 0.0031  -0.0351 312  PHE A CE1   
2554 C  CE2   . PHE A 311 ? 0.077  0.1165 0.5465 0.0012  0.005   -0.039  312  PHE A CE2   
2555 C  CZ    . PHE A 311 ? 0.0748 0.1135 0.5405 0       0.0033  -0.0374 312  PHE A CZ    
2556 N  N     . GLY A 312 ? 0.0755 0.118  0.558  0.0027  0.0097  -0.0305 313  GLY A N     
2557 C  CA    . GLY A 312 ? 0.0906 0.1332 0.5714 0.002   0.0089  -0.0281 313  GLY A CA    
2558 C  C     . GLY A 312 ? 0.1021 0.1423 0.5801 0.0032  0.0088  -0.0262 313  GLY A C     
2559 O  O     . GLY A 312 ? 0.1196 0.1578 0.5962 0.0047  0.0093  -0.0267 313  GLY A O     
2560 N  N     . VAL A 313 ? 0.0938 0.1341 0.5708 0.0027  0.0081  -0.024  314  VAL A N     
2561 C  CA    . VAL A 313 ? 0.1097 0.1476 0.5835 0.0041  0.0079  -0.0221 314  VAL A CA    
2562 C  C     . VAL A 313 ? 0.113  0.1533 0.5916 0.0049  0.0098  -0.0202 314  VAL A C     
2563 O  O     . VAL A 313 ? 0.1163 0.1594 0.5986 0.0037  0.0102  -0.0196 314  VAL A O     
2564 C  CB    . VAL A 313 ? 0.1345 0.1694 0.6009 0.003   0.0046  -0.0211 314  VAL A CB    
2565 C  CG1   . VAL A 313 ? 0.1459 0.1779 0.608  0.0047  0.0041  -0.0194 314  VAL A CG1   
2566 C  CG2   . VAL A 313 ? 0.1425 0.1752 0.6044 0.0022  0.0027  -0.0229 314  VAL A CG2   
2567 N  N     . ILE A 314 ? 0.1091 0.1483 0.5877 0.007   0.0111  -0.0191 315  ILE A N     
2568 C  CA    . ILE A 314 ? 0.123  0.1639 0.6049 0.0081  0.0127  -0.0169 315  ILE A CA    
2569 C  C     . ILE A 314 ? 0.1346 0.1723 0.6092 0.0089  0.0106  -0.0152 315  ILE A C     
2570 O  O     . ILE A 314 ? 0.1441 0.1791 0.6149 0.0108  0.0106  -0.0153 315  ILE A O     
2571 C  CB    . ILE A 314 ? 0.1338 0.1762 0.6216 0.0102  0.0158  -0.0167 315  ILE A CB    
2572 C  CG1   . ILE A 314 ? 0.1323 0.1771 0.6269 0.0095  0.0174  -0.0187 315  ILE A CG1   
2573 C  CG2   . ILE A 314 ? 0.1495 0.1937 0.6404 0.0114  0.0174  -0.014  315  ILE A CG2   
2574 C  CD1   . ILE A 314 ? 0.1366 0.1845 0.6363 0.0081  0.0183  -0.0187 315  ILE A CD1   
2575 N  N     . ARG A 315 ? 0.1306 0.1684 0.603  0.0075  0.0087  -0.0138 316  ARG A N     
2576 C  CA    . ARG A 315 ? 0.1415 0.176  0.6067 0.0081  0.0063  -0.0123 316  ARG A CA    
2577 C  C     . ARG A 315 ? 0.1479 0.1822 0.6134 0.0111  0.0082  -0.0107 316  ARG A C     
2578 O  O     . ARG A 315 ? 0.1386 0.1761 0.6108 0.0121  0.0112  -0.01   316  ARG A O     
2579 C  CB    . ARG A 315 ? 0.1509 0.1862 0.615  0.0059  0.004   -0.0108 316  ARG A CB    
2580 N  N     . LYS A 316 ? 0.1582 0.1885 0.6162 0.0128  0.0064  -0.0101 317  LYS A N     
2581 C  CA    . LYS A 316 ? 0.1714 0.2015 0.6293 0.0161  0.0083  -0.0084 317  LYS A CA    
2582 C  C     . LYS A 316 ? 0.1786 0.2122 0.6412 0.0163  0.0098  -0.006  317  LYS A C     
2583 O  O     . LYS A 316 ? 0.1869 0.2225 0.6537 0.0187  0.0127  -0.0046 317  LYS A O     
2584 C  CB    . LYS A 316 ? 0.1917 0.2167 0.6401 0.0181  0.006   -0.0081 317  LYS A CB    
2585 C  CG    . LYS A 316 ? 0.2282 0.2506 0.6704 0.0165  0.0021  -0.0076 317  LYS A CG    
2586 C  CD    . LYS A 316 ? 0.2954 0.3126 0.7282 0.019   -0.0001 -0.0074 317  LYS A CD    
2587 C  CE    . LYS A 316 ? 0.3559 0.3705 0.783  0.0173  -0.0042 -0.0068 317  LYS A CE    
2588 N  NZ    . LYS A 316 ? 0.4089 0.4182 0.8267 0.02    -0.0065 -0.0066 317  LYS A NZ    
2589 N  N     . GLU A 317 ? 0.1691 0.2037 0.6316 0.0137  0.0078  -0.0055 318  GLU A N     
2590 C  CA    . GLU A 317 ? 0.1636 0.2017 0.6304 0.0135  0.0089  -0.0032 318  GLU A CA    
2591 C  C     . GLU A 317 ? 0.1476 0.1905 0.6242 0.0134  0.0127  -0.0031 318  GLU A C     
2592 O  O     . GLU A 317 ? 0.1564 0.2022 0.6373 0.0139  0.0144  -0.001  318  GLU A O     
2593 C  CB    . GLU A 317 ? 0.1872 0.2254 0.6518 0.0105  0.0057  -0.0026 318  GLU A CB    
2594 C  CG    . GLU A 317 ? 0.2619 0.2955 0.7175 0.0106  0.0017  -0.0022 318  GLU A CG    
2595 C  CD    . GLU A 317 ? 0.3334 0.3625 0.7826 0.0098  -0.0011 -0.0044 318  GLU A CD    
2596 O  OE1   . GLU A 317 ? 0.3343 0.3642 0.7863 0.0087  -0.0001 -0.0062 318  GLU A OE1   
2597 O  OE2   . GLU A 317 ? 0.3714 0.3961 0.8128 0.0103  -0.0043 -0.0043 318  GLU A OE2   
2598 N  N     . SER A 318 ? 0.1218 0.1651 0.6017 0.0127  0.0138  -0.0052 319  SER A N     
2599 C  CA    . SER A 318 ? 0.12   0.1671 0.6088 0.0127  0.017   -0.0055 319  SER A CA    
2600 C  C     . SER A 318 ? 0.1172 0.164  0.609  0.0148  0.0194  -0.0064 319  SER A C     
2601 O  O     . SER A 318 ? 0.1099 0.1595 0.6093 0.015   0.0221  -0.0066 319  SER A O     
2602 C  CB    . SER A 318 ? 0.1428 0.1913 0.634  0.0099  0.0164  -0.0072 319  SER A CB    
2603 O  OG    . SER A 318 ? 0.1817 0.2319 0.6728 0.0081  0.0151  -0.0058 319  SER A OG    
2604 N  N     . ARG A 319 ? 0.1259 0.1695 0.6121 0.0164  0.0185  -0.0068 320  ARG A N     
2605 C  CA    . ARG A 319 ? 0.1273 0.1704 0.6157 0.0184  0.0204  -0.0075 320  ARG A CA    
2606 C  C     . ARG A 319 ? 0.1389 0.1846 0.6337 0.0208  0.0238  -0.0053 320  ARG A C     
2607 O  O     . ARG A 319 ? 0.1392 0.1867 0.6406 0.0211  0.0259  -0.0059 320  ARG A O     
2608 C  CB    . ARG A 319 ? 0.1422 0.181  0.6222 0.0199  0.0186  -0.0079 320  ARG A CB    
2609 C  CG    . ARG A 319 ? 0.1672 0.2057 0.6492 0.0218  0.0204  -0.0084 320  ARG A CG    
2610 C  CD    . ARG A 319 ? 0.1789 0.2131 0.6525 0.0226  0.0183  -0.0095 320  ARG A CD    
2611 N  NE    . ARG A 319 ? 0.2015 0.2356 0.6772 0.0246  0.0202  -0.0096 320  ARG A NE    
2612 C  CZ    . ARG A 319 ? 0.2167 0.2477 0.6868 0.0253  0.019   -0.0108 320  ARG A CZ    
2613 N  NH1   . ARG A 319 ? 0.2127 0.2402 0.6749 0.024   0.0159  -0.0121 320  ARG A NH1   
2614 N  NH2   . ARG A 319 ? 0.1916 0.223  0.6642 0.0272  0.0209  -0.0105 320  ARG A NH2   
2615 N  N     . ASN A 320 ? 0.1475 0.1938 0.641  0.0224  0.0242  -0.0027 321  ASN A N     
2616 C  CA    . ASN A 320 ? 0.1503 0.1994 0.6502 0.0248  0.0275  -0.0003 321  ASN A CA    
2617 C  C     . ASN A 320 ? 0.1481 0.201  0.6577 0.0233  0.0297  -0.0006 321  ASN A C     
2618 O  O     . ASN A 320 ? 0.1492 0.2039 0.6658 0.0246  0.0324  0       321  ASN A O     
2619 C  CB    . ASN A 320 ? 0.1763 0.2257 0.6729 0.0265  0.0273  0.0025  321  ASN A CB    
2620 C  CG    . ASN A 320 ? 0.2489 0.3015 0.7522 0.0292  0.0308  0.0053  321  ASN A CG    
2621 O  OD1   . ASN A 320 ? 0.2776 0.3297 0.7802 0.0323  0.0322  0.0067  321  ASN A OD1   
2622 N  ND2   . ASN A 320 ? 0.2547 0.311  0.7648 0.0282  0.0325  0.0064  321  ASN A ND2   
2623 N  N     . ASP A 321 ? 0.1433 0.1974 0.6536 0.0207  0.0286  -0.0012 322  ASP A N     
2624 C  CA    . ASP A 321 ? 0.1411 0.1984 0.6598 0.0195  0.0306  -0.0015 322  ASP A CA    
2625 C  C     . ASP A 321 ? 0.1255 0.1827 0.6482 0.0184  0.031   -0.0043 322  ASP A C     
2626 O  O     . ASP A 321 ? 0.1152 0.1745 0.6458 0.0188  0.0334  -0.0044 322  ASP A O     
2627 C  CB    . ASP A 321 ? 0.1674 0.2261 0.6852 0.0173  0.0294  -0.0011 322  ASP A CB    
2628 C  CG    . ASP A 321 ? 0.2368 0.2964 0.7523 0.0184  0.0293  0.0019  322  ASP A CG    
2629 O  OD1   . ASP A 321 ? 0.2583 0.3184 0.7753 0.0211  0.0312  0.0039  322  ASP A OD1   
2630 O  OD2   . ASP A 321 ? 0.2501 0.3099 0.7625 0.0167  0.0274  0.0025  322  ASP A OD2   
2631 N  N     . PHE A 322 ? 0.1171 0.1717 0.6342 0.0171  0.0286  -0.0067 323  PHE A N     
2632 C  CA    . PHE A 322 ? 0.1088 0.1631 0.6286 0.0162  0.0286  -0.0095 323  PHE A CA    
2633 C  C     . PHE A 322 ? 0.108  0.1623 0.632  0.0183  0.0306  -0.009  323  PHE A C     
2634 O  O     . PHE A 322 ? 0.1098 0.1656 0.6409 0.0181  0.0321  -0.01   323  PHE A O     
2635 C  CB    . PHE A 322 ? 0.1036 0.155  0.6157 0.0148  0.0256  -0.0116 323  PHE A CB    
2636 C  CG    . PHE A 322 ? 0.102  0.1525 0.6155 0.0144  0.0255  -0.0143 323  PHE A CG    
2637 C  CD1   . PHE A 322 ? 0.1091 0.1612 0.6273 0.0128  0.0258  -0.0165 323  PHE A CD1   
2638 C  CD2   . PHE A 322 ? 0.1025 0.1508 0.6124 0.0158  0.0251  -0.0146 323  PHE A CD2   
2639 C  CE1   . PHE A 322 ? 0.1139 0.1652 0.6333 0.0125  0.0256  -0.019  323  PHE A CE1   
2640 C  CE2   . PHE A 322 ? 0.1101 0.1577 0.6213 0.0153  0.0249  -0.0169 323  PHE A CE2   
2641 C  CZ    . PHE A 322 ? 0.1071 0.1564 0.6231 0.0137  0.0251  -0.0192 323  PHE A CZ    
2642 N  N     . ILE A 323 ? 0.1032 0.156  0.6229 0.0205  0.0306  -0.0073 324  ILE A N     
2643 C  CA    . ILE A 323 ? 0.1066 0.1597 0.6301 0.0229  0.0326  -0.0062 324  ILE A CA    
2644 C  C     . ILE A 323 ? 0.1039 0.1603 0.6368 0.0239  0.0356  -0.0042 324  ILE A C     
2645 O  O     . ILE A 323 ? 0.1084 0.1658 0.648  0.0242  0.037   -0.0047 324  ILE A O     
2646 C  CB    . ILE A 323 ? 0.1186 0.1692 0.6348 0.0255  0.032   -0.0045 324  ILE A CB    
2647 C  CG1   . ILE A 323 ? 0.132  0.1791 0.6399 0.0244  0.0292  -0.0069 324  ILE A CG1   
2648 C  CG2   . ILE A 323 ? 0.1201 0.1718 0.6412 0.0284  0.0346  -0.0025 324  ILE A CG2   
2649 C  CD1   . ILE A 323 ? 0.1361 0.1831 0.6472 0.0231  0.029   -0.0096 324  ILE A CD1   
2650 N  N     . ASN A 324 ? 0.0955 0.1535 0.6293 0.0244  0.0365  -0.002  325  ASN A N     
2651 C  CA    . ASN A 324 ? 0.1123 0.1735 0.655  0.0253  0.0394  0       325  ASN A CA    
2652 C  C     . ASN A 324 ? 0.1196 0.1821 0.67   0.0233  0.0401  -0.0022 325  ASN A C     
2653 O  O     . ASN A 324 ? 0.1278 0.192  0.6864 0.0242  0.0422  -0.0015 325  ASN A O     
2654 C  CB    . ASN A 324 ? 0.13   0.1928 0.6718 0.0257  0.0399  0.0023  325  ASN A CB    
2655 C  CG    . ASN A 324 ? 0.1673 0.2295 0.7037 0.0283  0.0399  0.0051  325  ASN A CG    
2656 O  OD1   . ASN A 324 ? 0.1709 0.2319 0.7054 0.0306  0.0403  0.006   325  ASN A OD1   
2657 N  ND2   . ASN A 324 ? 0.1777 0.2407 0.7112 0.0282  0.0394  0.0067  325  ASN A ND2   
2658 N  N     . ASP A 325 ? 0.1182 0.18   0.6658 0.0208  0.0382  -0.0048 326  ASP A N     
2659 C  CA    . ASP A 325 ? 0.1182 0.1809 0.672  0.0191  0.0386  -0.0072 326  ASP A CA    
2660 C  C     . ASP A 325 ? 0.1156 0.1771 0.6721 0.019   0.0383  -0.0095 326  ASP A C     
2661 O  O     . ASP A 325 ? 0.1112 0.1737 0.6754 0.0187  0.0396  -0.0104 326  ASP A O     
2662 C  CB    . ASP A 325 ? 0.1275 0.1899 0.6771 0.0168  0.0367  -0.0091 326  ASP A CB    
2663 C  CG    . ASP A 325 ? 0.1622 0.2266 0.7124 0.0166  0.0375  -0.007  326  ASP A CG    
2664 O  OD1   . ASP A 325 ? 0.1761 0.2422 0.7305 0.0182  0.0396  -0.0043 326  ASP A OD1   
2665 O  OD2   . ASP A 325 ? 0.1649 0.2294 0.7117 0.0149  0.036   -0.0079 326  ASP A OD2   
2666 N  N     . VAL A 326 ? 0.114  0.1734 0.6643 0.0192  0.0367  -0.0103 327  VAL A N     
2667 C  CA    . VAL A 326 ? 0.1102 0.1686 0.6628 0.0192  0.0364  -0.0121 327  VAL A CA    
2668 C  C     . VAL A 326 ? 0.1026 0.1624 0.6622 0.0213  0.0387  -0.0097 327  VAL A C     
2669 O  O     . VAL A 326 ? 0.0828 0.1433 0.6498 0.021   0.0394  -0.0107 327  VAL A O     
2670 C  CB    . VAL A 326 ? 0.1217 0.1776 0.6657 0.019   0.0341  -0.0134 327  VAL A CB    
2671 C  CG1   . VAL A 326 ? 0.1269 0.1821 0.6735 0.0192  0.034   -0.0149 327  VAL A CG1   
2672 C  CG2   . VAL A 326 ? 0.1314 0.1863 0.6696 0.0168  0.0318  -0.0158 327  VAL A CG2   
2673 N  N     . CYS A 327 ? 0.1131 0.1733 0.6707 0.0236  0.0399  -0.0063 328  CYS A N     
2674 C  CA    . CYS A 327 ? 0.131  0.1929 0.6952 0.026   0.0423  -0.0033 328  CYS A CA    
2675 C  C     . CYS A 327 ? 0.1369 0.2013 0.7115 0.0257  0.0444  -0.0026 328  CYS A C     
2676 O  O     . CYS A 327 ? 0.1328 0.1982 0.7151 0.0264  0.0457  -0.0018 328  CYS A O     
2677 C  CB    . CYS A 327 ? 0.1501 0.2119 0.7092 0.0287  0.0431  0.0001  328  CYS A CB    
2678 S  SG    . CYS A 327 ? 0.208  0.2666 0.7561 0.0298  0.0411  -0.0004 328  CYS A SG    
2679 N  N     . LYS A 328 ? 0.1424 0.2077 0.7173 0.0246  0.0446  -0.0027 329  LYS A N     
2680 C  CA    . LYS A 328 ? 0.1512 0.2186 0.7355 0.0243  0.0466  -0.0022 329  LYS A CA    
2681 C  C     . LYS A 328 ? 0.1455 0.2121 0.7348 0.0224  0.0457  -0.0057 329  LYS A C     
2682 O  O     . LYS A 328 ? 0.1565 0.2242 0.755  0.0226  0.0471  -0.0052 329  LYS A O     
2683 C  CB    . LYS A 328 ? 0.1848 0.2532 0.7671 0.0236  0.0468  -0.0016 329  LYS A CB    
2684 C  CG    . LYS A 328 ? 0.2838 0.3543 0.8751 0.0235  0.049   -0.0009 329  LYS A CG    
2685 C  CD    . LYS A 328 ? 0.3776 0.4502 0.9766 0.0259  0.0517  0.0028  329  LYS A CD    
2686 C  CE    . LYS A 328 ? 0.4406 0.5153 1.0477 0.0259  0.054   0.0041  329  LYS A CE    
2687 N  NZ    . LYS A 328 ? 0.4805 0.5573 1.0962 0.0281  0.0566  0.0075  329  LYS A NZ    
2688 N  N     . LEU A 329 ? 0.1255 0.1901 0.709  0.0206  0.0432  -0.0092 330  LEU A N     
2689 C  CA    . LEU A 329 ? 0.1161 0.1799 0.7031 0.0188  0.0421  -0.0128 330  LEU A CA    
2690 C  C     . LEU A 329 ? 0.1102 0.1736 0.7021 0.0193  0.0421  -0.0131 330  LEU A C     
2691 O  O     . LEU A 329 ? 0.1014 0.1649 0.7007 0.0187  0.0423  -0.0145 330  LEU A O     
2692 C  CB    . LEU A 329 ? 0.1226 0.1846 0.7015 0.0171  0.0395  -0.016  330  LEU A CB    
2693 C  CG    . LEU A 329 ? 0.1422 0.2033 0.7235 0.0155  0.0382  -0.02   330  LEU A CG    
2694 C  CD1   . LEU A 329 ? 0.1444 0.2064 0.7321 0.015   0.0392  -0.0209 330  LEU A CD1   
2695 C  CD2   . LEU A 329 ? 0.149  0.2087 0.7221 0.0141  0.0358  -0.0227 330  LEU A CD2   
2696 N  N     . TYR A 330 ? 0.1084 0.1712 0.6961 0.0205  0.0417  -0.0117 331  TYR A N     
2697 C  CA    . TYR A 330 ? 0.1085 0.1711 0.7002 0.0211  0.0417  -0.0116 331  TYR A CA    
2698 C  C     . TYR A 330 ? 0.1312 0.1956 0.7284 0.0235  0.044   -0.0073 331  TYR A C     
2699 O  O     . TYR A 330 ? 0.1378 0.2023 0.7374 0.0243  0.044   -0.0065 331  TYR A O     
2700 C  CB    . TYR A 330 ? 0.0964 0.1571 0.6796 0.0207  0.0396  -0.0133 331  TYR A CB    
2701 C  CG    . TYR A 330 ? 0.0869 0.1461 0.6666 0.0184  0.0373  -0.0177 331  TYR A CG    
2702 C  CD1   . TYR A 330 ? 0.085  0.1441 0.6708 0.017   0.0366  -0.0204 331  TYR A CD1   
2703 C  CD2   . TYR A 330 ? 0.0947 0.1526 0.6651 0.0176  0.0357  -0.019  331  TYR A CD2   
2704 C  CE1   . TYR A 330 ? 0.0928 0.1508 0.6752 0.0152  0.0345  -0.0244 331  TYR A CE1   
2705 C  CE2   . TYR A 330 ? 0.0983 0.1552 0.6656 0.0156  0.0337  -0.0227 331  TYR A CE2   
2706 C  CZ    . TYR A 330 ? 0.0991 0.1561 0.6723 0.0146  0.0332  -0.0254 331  TYR A CZ    
2707 O  OH    . TYR A 330 ? 0.1076 0.1637 0.6777 0.013   0.0314  -0.0291 331  TYR A OH    
2708 N  N     . ASN A 331 ? 0.1483 0.2144 0.7477 0.0248  0.0461  -0.0043 332  ASN A N     
2709 C  CA    . ASN A 331 ? 0.1762 0.2444 0.7812 0.0274  0.0486  0.0002  332  ASN A CA    
2710 C  C     . ASN A 331 ? 0.1939 0.2617 0.7931 0.0297  0.0487  0.0025  332  ASN A C     
2711 O  O     . ASN A 331 ? 0.1933 0.2624 0.7981 0.0314  0.05    0.0051  332  ASN A O     
2712 C  CB    . ASN A 331 ? 0.1952 0.2647 0.8123 0.0271  0.0496  0.0006  332  ASN A CB    
2713 C  CG    . ASN A 331 ? 0.2492 0.3215 0.874  0.0294  0.0525  0.0052  332  ASN A CG    
2714 O  OD1   . ASN A 331 ? 0.2649 0.3383 0.8877 0.0306  0.054   0.0073  332  ASN A OD1   
2715 N  ND2   . ASN A 331 ? 0.2619 0.3354 0.8959 0.0301  0.0535  0.0071  332  ASN A ND2   
2716 N  N     . ILE A 332 ? 0.2057 0.2718 0.7942 0.0299  0.0473  0.0018  333  ILE A N     
2717 C  CA    . ILE A 332 ? 0.2192 0.2844 0.8011 0.0324  0.0473  0.0038  333  ILE A CA    
2718 C  C     . ILE A 332 ? 0.2375 0.3043 0.8186 0.0352  0.0494  0.0079  333  ILE A C     
2719 O  O     . ILE A 332 ? 0.2428 0.3092 0.8191 0.0349  0.049   0.0077  333  ILE A O     
2720 C  CB    . ILE A 332 ? 0.2228 0.2849 0.7934 0.0311  0.0446  0.0008  333  ILE A CB    
2721 C  CG1   . ILE A 332 ? 0.227  0.2879 0.7986 0.0283  0.0426  -0.0033 333  ILE A CG1   
2722 C  CG2   . ILE A 332 ? 0.2276 0.2884 0.7908 0.0338  0.0445  0.0029  333  ILE A CG2   
2723 C  CD1   . ILE A 332 ? 0.2401 0.2983 0.8014 0.0265  0.0398  -0.0065 333  ILE A CD1   
2724 N  N     . ASN A 333 ? 0.2487 0.3174 0.835  0.038   0.0517  0.0117  334  ASN A N     
2725 C  CA    . ASN A 333 ? 0.2681 0.3388 0.8546 0.0412  0.054   0.016   334  ASN A CA    
2726 C  C     . ASN A 333 ? 0.2821 0.3521 0.8616 0.0448  0.0545  0.0187  334  ASN A C     
2727 O  O     . ASN A 333 ? 0.2915 0.3624 0.8683 0.0475  0.0559  0.0217  334  ASN A O     
2728 C  CB    . ASN A 333 ? 0.2848 0.359  0.8842 0.042   0.0568  0.0189  334  ASN A CB    
2729 C  CG    . ASN A 333 ? 0.3283 0.4033 0.9335 0.0393  0.0568  0.017   334  ASN A CG    
2730 O  OD1   . ASN A 333 ? 0.3396 0.4147 0.9526 0.0372  0.0565  0.0151  334  ASN A OD1   
2731 N  ND2   . ASN A 333 ? 0.3307 0.406  0.9321 0.0394  0.0571  0.0174  334  ASN A ND2   
2732 N  N     . ASP A 334 ? 0.2788 0.3471 0.8553 0.045   0.0534  0.0178  335  ASP A N     
2733 C  CA    . ASP A 334 ? 0.2904 0.3578 0.8599 0.0487  0.0539  0.0203  335  ASP A CA    
2734 C  C     . ASP A 334 ? 0.313  0.3777 0.8702 0.0497  0.0525  0.0198  335  ASP A C     
2735 O  O     . ASP A 334 ? 0.3166 0.3782 0.8661 0.0474  0.0497  0.0161  335  ASP A O     
2736 C  CB    . ASP A 334 ? 0.308  0.3737 0.8759 0.0482  0.0526  0.0189  335  ASP A CB    
2737 C  CG    . ASP A 334 ? 0.3767 0.442  0.9393 0.0525  0.0538  0.0222  335  ASP A CG    
2738 O  OD1   . ASP A 334 ? 0.3975 0.4657 0.9675 0.0551  0.0563  0.0263  335  ASP A OD1   
2739 O  OD2   . ASP A 334 ? 0.4021 0.4641 0.9534 0.0533  0.0521  0.0209  335  ASP A OD2   
2740 N  N     . MET A 335 ? 0.3228 0.3887 0.8781 0.0534  0.0543  0.0235  336  MET A N     
2741 C  CA    . MET A 335 ? 0.3388 0.4022 0.8827 0.055   0.053   0.0235  336  MET A CA    
2742 C  C     . MET A 335 ? 0.3498 0.4088 0.8823 0.0549  0.0503  0.0211  336  MET A C     
2743 O  O     . MET A 335 ? 0.3585 0.4146 0.8829 0.0531  0.0477  0.0185  336  MET A O     
2744 C  CB    . MET A 335 ? 0.3478 0.4134 0.8918 0.0599  0.0557  0.0284  336  MET A CB    
2745 N  N     . LYS A 336 ? 0.3469 0.4054 0.8791 0.0568  0.0509  0.0221  337  LYS A N     
2746 C  CA    . LYS A 336 ? 0.3552 0.4094 0.8768 0.0571  0.0485  0.02    337  LYS A CA    
2747 C  C     . LYS A 336 ? 0.3419 0.3939 0.8618 0.0523  0.0456  0.0151  337  LYS A C     
2748 O  O     . LYS A 336 ? 0.3478 0.396  0.8577 0.0514  0.043   0.0127  337  LYS A O     
2749 C  CB    . LYS A 336 ? 0.3962 0.4508 0.9183 0.0606  0.0502  0.0228  337  LYS A CB    
2750 C  CG    . LYS A 336 ? 0.4614 0.518  0.9836 0.0659  0.0531  0.0278  337  LYS A CG    
2751 C  CD    . LYS A 336 ? 0.5301 0.5835 1.0415 0.0702  0.0528  0.0292  337  LYS A CD    
2752 C  CE    . LYS A 336 ? 0.5887 0.6435 1.1041 0.0724  0.0546  0.0316  337  LYS A CE    
2753 N  NZ    . LYS A 336 ? 0.6247 0.6845 1.1497 0.0758  0.0584  0.0368  337  LYS A NZ    
2754 N  N     . ILE A 337 ? 0.3216 0.376  0.8512 0.0493  0.046   0.0137  338  ILE A N     
2755 C  CA    . ILE A 337 ? 0.3106 0.3632 0.8391 0.045   0.0435  0.0092  338  ILE A CA    
2756 C  C     . ILE A 337 ? 0.2905 0.342  0.8146 0.0426  0.0416  0.007   338  ILE A C     
2757 O  O     . ILE A 337 ? 0.2908 0.3393 0.8078 0.0404  0.0389  0.0039  338  ILE A O     
2758 C  CB    . ILE A 337 ? 0.3119 0.3674 0.8521 0.0427  0.0444  0.0083  338  ILE A CB    
2759 C  CG1   . ILE A 337 ? 0.328  0.3841 0.8714 0.0444  0.0454  0.0098  338  ILE A CG1   
2760 C  CG2   . ILE A 337 ? 0.3148 0.3691 0.8546 0.0384  0.042   0.0037  338  ILE A CG2   
2761 C  CD1   . ILE A 337 ? 0.3452 0.4041 0.9009 0.0423  0.0461  0.0092  338  ILE A CD1   
2762 N  N     . ILE A 338 ? 0.2724 0.3262 0.8007 0.043   0.043   0.0088  339  ILE A N     
2763 C  CA    . ILE A 338 ? 0.2715 0.3247 0.7965 0.0409  0.0415  0.0074  339  ILE A CA    
2764 C  C     . ILE A 338 ? 0.2817 0.3312 0.7944 0.0421  0.0393  0.0072  339  ILE A C     
2765 O  O     . ILE A 338 ? 0.2811 0.3285 0.7884 0.0394  0.0366  0.0045  339  ILE A O     
2766 C  CB    . ILE A 338 ? 0.26   0.3168 0.7927 0.0415  0.0438  0.0098  339  ILE A CB    
2767 C  CG1   . ILE A 338 ? 0.2621 0.3218 0.8068 0.0401  0.0456  0.0096  339  ILE A CG1   
2768 C  CG2   . ILE A 338 ? 0.2609 0.3173 0.7901 0.0394  0.0423  0.0086  339  ILE A CG2   
2769 C  CD1   . ILE A 338 ? 0.2683 0.3316 0.8217 0.0409  0.0483  0.0124  339  ILE A CD1   
2770 N  N     . LYS A 339 ? 0.2896 0.3381 0.7976 0.0461  0.0402  0.0099  340  LYS A N     
2771 C  CA    . LYS A 339 ? 0.3046 0.3491 0.8006 0.0477  0.038   0.0097  340  LYS A CA    
2772 C  C     . LYS A 339 ? 0.3058 0.3465 0.7949 0.0456  0.0351  0.0063  340  LYS A C     
2773 O  O     . LYS A 339 ? 0.3173 0.3548 0.7982 0.0443  0.0323  0.0046  340  LYS A O     
2774 C  CB    . LYS A 339 ? 0.3428 0.3871 0.8354 0.0528  0.0398  0.0132  340  LYS A CB    
2775 C  CG    . LYS A 339 ? 0.4334 0.4799 0.9275 0.0551  0.0413  0.0162  340  LYS A CG    
2776 C  CD    . LYS A 339 ? 0.5148 0.5626 1.009  0.0605  0.0441  0.0204  340  LYS A CD    
2777 C  CE    . LYS A 339 ? 0.5665 0.617  1.0628 0.0627  0.0458  0.0234  340  LYS A CE    
2778 N  NZ    . LYS A 339 ? 0.583  0.638  1.0909 0.06    0.0476  0.0238  340  LYS A NZ    
2779 N  N     . GLU A 340 ? 0.2892 0.3303 0.7821 0.0453  0.0359  0.0055  341  GLU A N     
2780 C  CA    . GLU A 340 ? 0.2787 0.3167 0.766  0.0434  0.0334  0.0024  341  GLU A CA    
2781 C  C     . GLU A 340 ? 0.2457 0.2835 0.7335 0.0388  0.0312  -0.0009 341  GLU A C     
2782 O  O     . GLU A 340 ? 0.2444 0.2788 0.7242 0.0374  0.0284  -0.003  341  GLU A O     
2783 C  CB    . GLU A 340 ? 0.3213 0.3607 0.8142 0.0437  0.0349  0.0025  341  GLU A CB    
2784 C  CG    . GLU A 340 ? 0.4297 0.4689 0.9208 0.0483  0.0368  0.0057  341  GLU A CG    
2785 C  CD    . GLU A 340 ? 0.5824 0.6167 1.0608 0.0504  0.035   0.0055  341  GLU A CD    
2786 O  OE1   . GLU A 340 ? 0.6042 0.6359 1.0778 0.0492  0.0332  0.0032  341  GLU A OE1   
2787 O  OE2   . GLU A 340 ? 0.6397 0.6728 1.1128 0.0532  0.0351  0.0074  341  GLU A OE2   
2788 N  N     . LEU A 341 ? 0.2212 0.2626 0.7183 0.0368  0.0324  -0.0012 342  LEU A N     
2789 C  CA    . LEU A 341 ? 0.206  0.2477 0.7044 0.0328  0.0307  -0.004  342  LEU A CA    
2790 C  C     . LEU A 341 ? 0.1953 0.2357 0.6877 0.032   0.0289  -0.0039 342  LEU A C     
2791 O  O     . LEU A 341 ? 0.1959 0.2352 0.6855 0.0291  0.0266  -0.0062 342  LEU A O     
2792 C  CB    . LEU A 341 ? 0.1942 0.2399 0.7038 0.0315  0.0328  -0.0039 342  LEU A CB    
2793 C  CG    . LEU A 341 ? 0.2016 0.2487 0.7181 0.0312  0.0339  -0.0047 342  LEU A CG    
2794 C  CD1   . LEU A 341 ? 0.1919 0.2425 0.7192 0.0305  0.036   -0.0041 342  LEU A CD1   
2795 C  CD2   . LEU A 341 ? 0.2137 0.259  0.7271 0.0285  0.0316  -0.0084 342  LEU A CD2   
2796 N  N     . LYS A 342 ? 0.1884 0.2291 0.6793 0.0346  0.0299  -0.0011 343  LYS A N     
2797 C  CA    . LYS A 342 ? 0.194  0.2338 0.6798 0.0341  0.0282  -0.0006 343  LYS A CA    
2798 C  C     . LYS A 342 ? 0.2178 0.2528 0.692  0.0353  0.0254  -0.0008 343  LYS A C     
2799 O  O     . LYS A 342 ? 0.2279 0.2621 0.6977 0.036   0.0243  0.0004  343  LYS A O     
2800 C  CB    . LYS A 342 ? 0.1904 0.2332 0.6809 0.0361  0.0306  0.0026  343  LYS A CB    
2801 C  CG    . LYS A 342 ? 0.206  0.253  0.7072 0.0342  0.0326  0.0025  343  LYS A CG    
2802 C  CD    . LYS A 342 ? 0.2307 0.2805 0.7358 0.0359  0.0347  0.0056  343  LYS A CD    
2803 C  CE    . LYS A 342 ? 0.2454 0.299  0.7606 0.034   0.0365  0.0055  343  LYS A CE    
2804 N  NZ    . LYS A 342 ? 0.2715 0.3278 0.7898 0.0354  0.0383  0.0084  343  LYS A NZ    
2805 N  N     . GLU A 343 ? 0.229  0.261  0.6981 0.0354  0.0241  -0.0025 344  GLU A N     
2806 C  CA    . GLU A 343 ? 0.2505 0.2774 0.7082 0.0363  0.0211  -0.0031 344  GLU A CA    
2807 C  C     . GLU A 343 ? 0.2649 0.2904 0.7188 0.0331  0.0179  -0.0044 344  GLU A C     
2808 O  O     . GLU A 343 ? 0.2685 0.296  0.727  0.0297  0.0175  -0.0061 344  GLU A O     
2809 C  CB    . GLU A 343 ? 0.2811 0.3052 0.7349 0.0364  0.0203  -0.0049 344  GLU A CB    
2810 C  CG    . GLU A 343 ? 0.336  0.3545 0.778  0.0377  0.0174  -0.0055 344  GLU A CG    
2811 C  CD    . GLU A 343 ? 0.4032 0.4191 0.8412 0.0389  0.0173  -0.0065 344  GLU A CD    
2812 O  OE1   . GLU A 343 ? 0.4006 0.4191 0.845  0.0392  0.0196  -0.0064 344  GLU A OE1   
2813 O  OE2   . GLU A 343 ? 0.4576 0.4685 0.8859 0.0396  0.0147  -0.0074 344  GLU A OE2   
2814 N  N     . ASP A 344 ? 0.2653 0.288  0.7115 0.0344  0.0158  -0.0035 345  ASP A N     
2815 C  CA    . ASP A 344 ? 0.2593 0.2809 0.7025 0.0314  0.0127  -0.0043 345  ASP A CA    
2816 C  C     . ASP A 344 ? 0.25   0.2679 0.6873 0.0288  0.0093  -0.0069 345  ASP A C     
2817 O  O     . ASP A 344 ? 0.2672 0.2805 0.6955 0.0293  0.0063  -0.0072 345  ASP A O     
2818 C  CB    . ASP A 344 ? 0.2954 0.3155 0.7331 0.0336  0.0116  -0.0023 345  ASP A CB    
2819 C  CG    . ASP A 344 ? 0.3783 0.398  0.8141 0.0306  0.0085  -0.0025 345  ASP A CG    
2820 O  OD1   . ASP A 344 ? 0.3987 0.422  0.8412 0.0275  0.009   -0.0029 345  ASP A OD1   
2821 O  OD2   . ASP A 344 ? 0.4136 0.4294 0.841  0.0314  0.0055  -0.0023 345  ASP A OD2   
2822 N  N     . ALA A 345 ? 0.2246 0.2445 0.667  0.026   0.0097  -0.0087 346  ALA A N     
2823 C  CA    . ALA A 345 ? 0.2111 0.2283 0.6493 0.0233  0.0068  -0.011  346  ALA A CA    
2824 C  C     . ALA A 345 ? 0.1874 0.2085 0.6331 0.0199  0.0075  -0.0123 346  ALA A C     
2825 O  O     . ALA A 345 ? 0.1854 0.2106 0.6392 0.0201  0.0104  -0.0119 346  ALA A O     
2826 C  CB    . ALA A 345 ? 0.2145 0.2286 0.6483 0.0251  0.0069  -0.0121 346  ALA A CB    
2827 N  N     . ASP A 346 ? 0.1686 0.1884 0.6118 0.017   0.0048  -0.014  347  ASP A N     
2828 C  CA    . ASP A 346 ? 0.1532 0.1765 0.6027 0.0142  0.0054  -0.0153 347  ASP A CA    
2829 C  C     . ASP A 346 ? 0.1376 0.1623 0.5914 0.015   0.0079  -0.0168 347  ASP A C     
2830 O  O     . ASP A 346 ? 0.1309 0.153  0.5809 0.0169  0.008   -0.0172 347  ASP A O     
2831 C  CB    . ASP A 346 ? 0.1746 0.196  0.62   0.0113  0.0021  -0.0166 347  ASP A CB    
2832 C  CG    . ASP A 346 ? 0.2298 0.2503 0.672  0.0098  -0.0007 -0.0152 347  ASP A CG    
2833 O  OD1   . ASP A 346 ? 0.235  0.2573 0.6795 0.0104  0.0002  -0.0133 347  ASP A OD1   
2834 O  OD2   . ASP A 346 ? 0.2693 0.2873 0.7068 0.0079  -0.0037 -0.0159 347  ASP A OD2   
2835 N  N     . LEU A 347 ? 0.1283 0.1569 0.5898 0.0136  0.0096  -0.0175 348  LEU A N     
2836 C  CA    . LEU A 347 ? 0.1291 0.1593 0.5955 0.0142  0.0118  -0.0189 348  LEU A CA    
2837 C  C     . LEU A 347 ? 0.1269 0.1588 0.596  0.0116  0.0112  -0.0211 348  LEU A C     
2838 O  O     . LEU A 347 ? 0.1425 0.1771 0.616  0.0101  0.0115  -0.0211 348  LEU A O     
2839 C  CB    . LEU A 347 ? 0.1273 0.1608 0.6015 0.0156  0.0149  -0.0174 348  LEU A CB    
2840 C  CG    . LEU A 347 ? 0.1531 0.1883 0.6334 0.0165  0.0172  -0.0183 348  LEU A CG    
2841 C  CD1   . LEU A 347 ? 0.1605 0.1931 0.6365 0.019   0.0174  -0.0179 348  LEU A CD1   
2842 C  CD2   . LEU A 347 ? 0.166  0.2047 0.6548 0.0175  0.0201  -0.0168 348  LEU A CD2   
2843 N  N     . ILE A 348 ? 0.1054 0.1357 0.5719 0.0114  0.0104  -0.023  349  ILE A N     
2844 C  CA    . ILE A 348 ? 0.0963 0.1284 0.5655 0.0093  0.01    -0.0252 349  ILE A CA    
2845 C  C     . ILE A 348 ? 0.0835 0.1185 0.5606 0.0099  0.0126  -0.0261 349  ILE A C     
2846 O  O     . ILE A 348 ? 0.0791 0.1138 0.5575 0.0118  0.014   -0.0258 349  ILE A O     
2847 C  CB    . ILE A 348 ? 0.1151 0.1445 0.5782 0.0088  0.008   -0.0267 349  ILE A CB    
2848 C  CG1   . ILE A 348 ? 0.1445 0.1712 0.6008 0.0076  0.0051  -0.0259 349  ILE A CG1   
2849 C  CG2   . ILE A 348 ? 0.1226 0.1542 0.5891 0.0072  0.0081  -0.0291 349  ILE A CG2   
2850 C  CD1   . ILE A 348 ? 0.1812 0.2047 0.6312 0.0072  0.003   -0.0269 349  ILE A CD1   
2851 N  N     . VAL A 349 ? 0.0681 0.1062 0.5508 0.0085  0.0133  -0.027  350  VAL A N     
2852 C  CA    . VAL A 349 ? 0.0597 0.1004 0.5501 0.0089  0.0154  -0.028  350  VAL A CA    
2853 C  C     . VAL A 349 ? 0.0632 0.1046 0.554  0.0076  0.0146  -0.0308 350  VAL A C     
2854 O  O     . VAL A 349 ? 0.0777 0.12   0.5674 0.006   0.0134  -0.0315 350  VAL A O     
2855 C  CB    . VAL A 349 ? 0.0476 0.091  0.5444 0.0088  0.0171  -0.0269 350  VAL A CB    
2856 C  CG1   . VAL A 349 ? 0.0521 0.0977 0.5567 0.009   0.0189  -0.0285 350  VAL A CG1   
2857 C  CG2   . VAL A 349 ? 0.0431 0.0811 0.5345 0.0092  0.0179  -0.024  350  VAL A CG2   
2858 N  N     . CYS A 350 ? 0.0515 0.0928 0.5442 0.0082  0.0152  -0.0323 351  CYS A N     
2859 C  CA    . CYS A 350 ? 0.0483 0.0904 0.5416 0.0072  0.0144  -0.035  351  CYS A CA    
2860 C  C     . CYS A 350 ? 0.0424 0.0748 0.5312 0.005   0.0155  -0.0362 351  CYS A C     
2861 O  O     . CYS A 350 ? 0.0418 0.0705 0.5303 0.0051  0.0166  -0.0354 351  CYS A O     
2862 C  CB    . CYS A 350 ? 0.0505 0.0905 0.5387 0.0077  0.0134  -0.0357 351  CYS A CB    
2863 S  SG    . CYS A 350 ? 0.0944 0.1354 0.5826 0.0065  0.0124  -0.039  351  CYS A SG    
2864 N  N     . MET A 351 ? 0.0409 0.0674 0.5246 0.003   0.0149  -0.0381 352  MET A N     
2865 C  CA    . MET A 351 ? 0.0421 0.0816 0.5449 0.0052  0.0167  -0.0397 352  MET A CA    
2866 C  C     . MET A 351 ? 0.0457 0.0941 0.5574 0.0062  0.0161  -0.0429 352  MET A C     
2867 O  O     . MET A 351 ? 0.0577 0.1065 0.5659 0.0053  0.0149  -0.0441 352  MET A O     
2868 C  CB    . MET A 351 ? 0.0414 0.0779 0.5434 0.0042  0.0174  -0.0392 352  MET A CB    
2869 C  CG    . MET A 351 ? 0.0521 0.1018 0.568  0.0069  0.0191  -0.0361 352  MET A CG    
2870 S  SD    . MET A 351 ? 0.0799 0.1317 0.6002 0.0065  0.0203  -0.0353 352  MET A SD    
2871 C  CE    . MET A 351 ? 0.0418 0.0832 0.5589 0.005   0.021   -0.0375 352  MET A CE    
2872 N  N     . LEU A 352 ? 0.0413 0.0739 0.5404 0.0039  0.0157  -0.0438 353  LEU A N     
2873 C  CA    . LEU A 352 ? 0.0412 0.0741 0.5401 0.0037  0.0146  -0.0468 353  LEU A CA    
2874 C  C     . LEU A 352 ? 0.0415 0.0818 0.5547 0.0051  0.0155  -0.0484 353  LEU A C     
2875 O  O     . LEU A 352 ? 0.042  0.0863 0.5635 0.0065  0.0168  -0.0468 353  LEU A O     
2876 C  CB    . LEU A 352 ? 0.0409 0.0662 0.5284 0.0027  0.0135  -0.0465 353  LEU A CB    
2877 C  CG    . LEU A 352 ? 0.0407 0.0619 0.5175 0.0019  0.0124  -0.0453 353  LEU A CG    
2878 C  CD1   . LEU A 352 ? 0.0407 0.0598 0.513  0.0021  0.0121  -0.0442 353  LEU A CD1   
2879 C  CD2   . LEU A 352 ? 0.0403 0.0594 0.5111 0.0011  0.011   -0.0473 353  LEU A CD2   
2880 N  N     . LYS A 353 ? 0.0415 0.0853 0.5591 0.0052  0.0149  -0.0515 354  LYS A N     
2881 C  CA    . LYS A 353 ? 0.0418 0.0927 0.5732 0.0065  0.0152  -0.0534 354  LYS A CA    
2882 C  C     . LYS A 353 ? 0.0557 0.1062 0.588  0.0068  0.0149  -0.0531 354  LYS A C     
2883 O  O     . LYS A 353 ? 0.0538 0.1044 0.5923 0.0072  0.0156  -0.0525 354  LYS A O     
2884 C  CB    . LYS A 353 ? 0.0437 0.0954 0.5758 0.0062  0.0141  -0.057  354  LYS A CB    
2885 C  CG    . LYS A 353 ? 0.0417 0.0935 0.5816 0.0064  0.0141  -0.0589 354  LYS A CG    
2886 C  CD    . LYS A 353 ? 0.0417 0.0939 0.5822 0.0064  0.0132  -0.0622 354  LYS A CD    
2887 C  CE    . LYS A 353 ? 0.0573 0.1091 0.6058 0.0066  0.0129  -0.0641 354  LYS A CE    
2888 N  NZ    . LYS A 353 ? 0.0416 0.0931 0.5914 0.0064  0.0112  -0.0666 354  LYS A NZ    
2889 N  N     . GLY A 354 ? 0.0547 0.1046 0.5807 0.0067  0.014   -0.0533 355  GLY A N     
2890 C  CA    . GLY A 354 ? 0.0453 0.0948 0.571  0.0072  0.0138  -0.0527 355  GLY A CA    
2891 C  C     . GLY A 354 ? 0.0497 0.1    0.5787 0.0069  0.0126  -0.0556 355  GLY A C     
2892 O  O     . GLY A 354 ? 0.0522 0.1024 0.5779 0.007   0.0118  -0.0562 355  GLY A O     
2893 N  N     . PHE A 355 ? 0.0417 0.0926 0.5775 0.0067  0.0125  -0.0572 356  PHE A N     
2894 C  CA    . PHE A 355 ? 0.0476 0.0991 0.5879 0.0064  0.0113  -0.0598 356  PHE A CA    
2895 C  C     . PHE A 355 ? 0.0617 0.1135 0.6047 0.0061  0.0103  -0.0632 356  PHE A C     
2896 O  O     . PHE A 355 ? 0.0726 0.1243 0.6178 0.0061  0.0111  -0.063  356  PHE A O     
2897 C  CB    . PHE A 355 ? 0.0423 0.094  0.5902 0.0068  0.0121  -0.0578 356  PHE A CB    
2898 C  CG    . PHE A 355 ? 0.045  0.0963 0.5901 0.0076  0.0133  -0.0541 356  PHE A CG    
2899 C  CD1   . PHE A 355 ? 0.0424 0.0932 0.5864 0.0082  0.015   -0.0511 356  PHE A CD1   
2900 C  CD2   . PHE A 355 ? 0.0572 0.1085 0.5994 0.0078  0.0127  -0.0538 356  PHE A CD2   
2901 C  CE1   . PHE A 355 ? 0.0499 0.1    0.5898 0.0092  0.0159  -0.048  356  PHE A CE1   
2902 C  CE2   . PHE A 355 ? 0.0607 0.1114 0.599  0.0089  0.0139  -0.0506 356  PHE A CE2   
2903 C  CZ    . PHE A 355 ? 0.0505 0.1005 0.5877 0.0096  0.0154  -0.0477 356  PHE A CZ    
2904 N  N     . LYS A 356 ? 0.0616 0.1138 0.6044 0.0059  0.0086  -0.0662 357  LYS A N     
2905 C  CA    . LYS A 356 ? 0.0643 0.1165 0.609  0.0059  0.0073  -0.07   357  LYS A CA    
2906 C  C     . LYS A 356 ? 0.0716 0.1233 0.6256 0.0057  0.0069  -0.0707 357  LYS A C     
2907 O  O     . LYS A 356 ? 0.0562 0.1079 0.6149 0.0056  0.0078  -0.068  357  LYS A O     
2908 C  CB    . LYS A 356 ? 0.0652 0.1181 0.6055 0.0059  0.0055  -0.0727 357  LYS A CB    
2909 C  CG    . LYS A 356 ? 0.0551 0.1086 0.5874 0.0062  0.0056  -0.073  357  LYS A CG    
2910 C  CD    . LYS A 356 ? 0.1018 0.156  0.6295 0.0063  0.0042  -0.0747 357  LYS A CD    
2911 C  CE    . LYS A 356 ? 0.1311 0.1851 0.6559 0.006   0.0048  -0.0718 357  LYS A CE    
2912 N  NZ    . LYS A 356 ? 0.1382 0.1931 0.6605 0.0061  0.0035  -0.0733 357  LYS A NZ    
2913 N  N     . PRO A 357 ? 0.0877 0.1389 0.6445 0.0058  0.0057  -0.0741 358  PRO A N     
2914 C  CA    . PRO A 357 ? 0.0935 0.1438 0.6592 0.0055  0.0053  -0.0747 358  PRO A CA    
2915 C  C     . PRO A 357 ? 0.1074 0.1579 0.6789 0.005   0.0044  -0.0739 358  PRO A C     
2916 O  O     . PRO A 357 ? 0.1208 0.1709 0.7    0.0047  0.005   -0.0723 358  PRO A O     
2917 C  CB    . PRO A 357 ? 0.1027 0.1521 0.6684 0.006   0.0036  -0.0791 358  PRO A CB    
2918 C  CG    . PRO A 357 ? 0.106  0.1561 0.6635 0.0066  0.0045  -0.0793 358  PRO A CG    
2919 C  CD    . PRO A 357 ? 0.08   0.1313 0.632  0.0063  0.0047  -0.0774 358  PRO A CD    
2920 N  N     . ARG A 358 ? 0.0959 0.1471 0.6643 0.0048  0.0031  -0.0748 359  ARG A N     
2921 C  CA    . ARG A 358 ? 0.0836 0.1354 0.6576 0.0043  0.0023  -0.0737 359  ARG A CA    
2922 C  C     . ARG A 358 ? 0.0657 0.1184 0.6382 0.0045  0.0042  -0.0691 359  ARG A C     
2923 O  O     . ARG A 358 ? 0.0551 0.1086 0.631  0.0043  0.0038  -0.0677 359  ARG A O     
2924 C  CB    . ARG A 358 ? 0.1073 0.1594 0.6801 0.004   -0.0003 -0.0771 359  ARG A CB    
2925 C  CG    . ARG A 358 ? 0.1369 0.1879 0.7106 0.0041  -0.0023 -0.0818 359  ARG A CG    
2926 C  CD    . ARG A 358 ? 0.1854 0.2369 0.7561 0.0041  -0.0048 -0.0852 359  ARG A CD    
2927 N  NE    . ARG A 358 ? 0.2395 0.292  0.8007 0.0048  -0.0043 -0.0857 359  ARG A NE    
2928 C  CZ    . ARG A 358 ? 0.2712 0.3248 0.8282 0.005   -0.0059 -0.0878 359  ARG A CZ    
2929 N  NH1   . ARG A 358 ? 0.28   0.3338 0.8413 0.0045  -0.0082 -0.0897 359  ARG A NH1   
2930 N  NH2   . ARG A 358 ? 0.2611 0.3156 0.8099 0.0057  -0.0052 -0.088  359  ARG A NH2   
2931 N  N     . GLY A 359 ? 0.0542 0.1068 0.622  0.0051  0.0063  -0.0667 360  GLY A N     
2932 C  CA    . GLY A 359 ? 0.0489 0.1019 0.6149 0.0056  0.0081  -0.0625 360  GLY A CA    
2933 C  C     . GLY A 359 ? 0.0457 0.0991 0.6037 0.0059  0.0078  -0.0623 360  GLY A C     
2934 O  O     . GLY A 359 ? 0.0413 0.0948 0.5972 0.0065  0.0092  -0.059  360  GLY A O     
2935 N  N     . ASP A 360 ? 0.0492 0.1027 0.6027 0.0055  0.0062  -0.0657 361  ASP A N     
2936 C  CA    . ASP A 360 ? 0.067  0.1208 0.6127 0.0058  0.0059  -0.0658 361  ASP A CA    
2937 C  C     . ASP A 360 ? 0.0739 0.127  0.6126 0.0061  0.0072  -0.0643 361  ASP A C     
2938 O  O     . ASP A 360 ? 0.0769 0.1296 0.6154 0.006   0.0075  -0.0651 361  ASP A O     
2939 C  CB    . ASP A 360 ? 0.0929 0.1474 0.6366 0.0055  0.0037  -0.0698 361  ASP A CB    
2940 C  CG    . ASP A 360 ? 0.1645 0.2188 0.7081 0.0054  0.0028  -0.0732 361  ASP A CG    
2941 O  OD1   . ASP A 360 ? 0.1721 0.2258 0.7215 0.0052  0.0029  -0.0735 361  ASP A OD1   
2942 O  OD2   . ASP A 360 ? 0.2073 0.262  0.7451 0.0056  0.0019  -0.0754 361  ASP A OD2   
2943 N  N     . ASP A 361 ? 0.0725 0.1252 0.6056 0.0066  0.008   -0.0619 362  ASP A N     
2944 C  CA    . ASP A 361 ? 0.0696 0.1213 0.5966 0.0068  0.009   -0.0601 362  ASP A CA    
2945 C  C     . ASP A 361 ? 0.0672 0.119  0.5879 0.0064  0.0081  -0.0623 362  ASP A C     
2946 O  O     . ASP A 361 ? 0.0714 0.124  0.59   0.0063  0.0068  -0.0648 362  ASP A O     
2947 C  CB    . ASP A 361 ? 0.0998 0.1505 0.6229 0.0076  0.01    -0.0568 362  ASP A CB    
2948 C  CG    . ASP A 361 ? 0.1922 0.2427 0.7084 0.0078  0.0093  -0.0573 362  ASP A CG    
2949 O  OD1   . ASP A 361 ? 0.2373 0.287  0.7468 0.0076  0.009   -0.0576 362  ASP A OD1   
2950 O  OD2   . ASP A 361 ? 0.2082 0.2593 0.7258 0.0081  0.009   -0.0572 362  ASP A OD2   
2951 N  N     . ASN A 362 ? 0.0564 0.1076 0.5746 0.0064  0.0088  -0.0612 363  ASN A N     
2952 C  CA    . ASN A 362 ? 0.0579 0.1093 0.5707 0.006   0.0082  -0.0624 363  ASN A CA    
2953 C  C     . ASN A 362 ? 0.0681 0.1186 0.5735 0.0061  0.008   -0.0611 363  ASN A C     
2954 O  O     . ASN A 362 ? 0.0796 0.1287 0.5826 0.0064  0.0088  -0.0583 363  ASN A O     
2955 C  CB    . ASN A 362 ? 0.0561 0.1071 0.569  0.0059  0.0092  -0.061  363  ASN A CB    
2956 C  CG    . ASN A 362 ? 0.0771 0.1288 0.5967 0.0059  0.0096  -0.0621 363  ASN A CG    
2957 O  OD1   . ASN A 362 ? 0.0746 0.1268 0.5986 0.0059  0.0089  -0.0646 363  ASN A OD1   
2958 N  ND2   . ASN A 362 ? 0.088  0.1394 0.6083 0.0059  0.0107  -0.0603 363  ASN A ND2   
2959 N  N     . ARG A 363 ? 0.0547 0.106  0.5563 0.006   0.0068  -0.063  364  ARG A N     
2960 C  CA    . ARG A 363 ? 0.0483 0.0987 0.5428 0.006   0.0065  -0.0619 364  ARG A CA    
2961 C  C     . ARG A 363 ? 0.0508 0.1001 0.5408 0.0057  0.0067  -0.06   364  ARG A C     
2962 O  O     . ARG A 363 ? 0.0573 0.1048 0.5432 0.0058  0.0069  -0.0578 364  ARG A O     
2963 C  CB    . ARG A 363 ? 0.0513 0.1032 0.5431 0.006   0.0053  -0.0643 364  ARG A CB    
2964 C  CG    . ARG A 363 ? 0.0636 0.1145 0.5503 0.0063  0.0051  -0.0632 364  ARG A CG    
2965 C  CD    . ARG A 363 ? 0.08   0.1308 0.5699 0.0068  0.0054  -0.0628 364  ARG A CD    
2966 N  NE    . ARG A 363 ? 0.0784 0.1312 0.5734 0.0067  0.0046  -0.0656 364  ARG A NE    
2967 C  CZ    . ARG A 363 ? 0.0698 0.1231 0.5717 0.0066  0.0048  -0.0662 364  ARG A CZ    
2968 N  NH1   . ARG A 363 ? 0.0449 0.0971 0.5497 0.0067  0.006   -0.0639 364  ARG A NH1   
2969 N  NH2   . ARG A 363 ? 0.0627 0.1175 0.5687 0.0065  0.0037  -0.069  364  ARG A NH2   
2970 N  N     . PRO A 364 ? 0.0453 0.0957 0.5356 0.0052  0.0065  -0.0607 365  PRO A N     
2971 C  CA    . PRO A 364 ? 0.0454 0.0948 0.5314 0.0048  0.0065  -0.0586 365  PRO A CA    
2972 C  C     . PRO A 364 ? 0.0502 0.0977 0.5366 0.0049  0.0074  -0.0558 365  PRO A C     
2973 O  O     . PRO A 364 ? 0.0524 0.0982 0.5339 0.0046  0.0071  -0.0538 365  PRO A O     
2974 C  CB    . PRO A 364 ? 0.0517 0.103  0.5397 0.0045  0.0065  -0.0597 365  PRO A CB    
2975 C  CG    . PRO A 364 ? 0.0566 0.1097 0.5475 0.005   0.0061  -0.0629 365  PRO A CG    
2976 C  CD    . PRO A 364 ? 0.0412 0.0862 0.5279 0.0043  0.0061  -0.0633 365  PRO A CD    
2977 N  N     . ASP A 365 ? 0.0448 0.0917 0.5363 0.0052  0.0085  -0.0556 366  ASP A N     
2978 C  CA    . ASP A 365 ? 0.0438 0.0868 0.5337 0.0052  0.0095  -0.0528 366  ASP A CA    
2979 C  C     . ASP A 365 ? 0.0425 0.0742 0.5185 0.0041  0.0091  -0.0508 366  ASP A C     
2980 O  O     . ASP A 365 ? 0.0417 0.0642 0.5081 0.0028  0.0093  -0.0483 366  ASP A O     
2981 C  CB    . ASP A 365 ? 0.0499 0.0969 0.5507 0.0062  0.0108  -0.0529 366  ASP A CB    
2982 C  CG    . ASP A 365 ? 0.0734 0.1221 0.5788 0.0057  0.0109  -0.0544 366  ASP A CG    
2983 O  OD1   . ASP A 365 ? 0.0717 0.1212 0.5744 0.0052  0.0102  -0.0556 366  ASP A OD1   
2984 O  OD2   . ASP A 365 ? 0.0767 0.1258 0.5882 0.006   0.0119  -0.0542 366  ASP A OD2   
2985 N  N     . ARG A 366 ? 0.0409 0.068  0.51   0.0033  0.0083  -0.0519 367  ARG A N     
2986 C  CA    . ARG A 366 ? 0.0437 0.0838 0.5238 0.0072  0.009   -0.0503 367  ARG A CA    
2987 C  C     . ARG A 366 ? 0.0455 0.0848 0.52   0.0073  0.0082  -0.0489 367  ARG A C     
2988 O  O     . ARG A 366 ? 0.0649 0.1017 0.5356 0.0082  0.0084  -0.0469 367  ARG A O     
2989 C  CB    . ARG A 366 ? 0.0621 0.1044 0.543  0.0078  0.0085  -0.0518 367  ARG A CB    
2990 C  CG    . ARG A 366 ? 0.1171 0.1614 0.6051 0.008   0.009   -0.0531 367  ARG A CG    
2991 C  CD    . ARG A 366 ? 0.1641 0.2094 0.6512 0.0081  0.0083  -0.0547 367  ARG A CD    
2992 N  NE    . ARG A 366 ? 0.1789 0.2258 0.6729 0.0084  0.0087  -0.0553 367  ARG A NE    
2993 C  CZ    . ARG A 366 ? 0.1933 0.2406 0.6874 0.009   0.0087  -0.0551 367  ARG A CZ    
2994 N  NH1   . ARG A 366 ? 0.1884 0.2345 0.676  0.0095  0.0084  -0.0544 367  ARG A NH1   
2995 N  NH2   . ARG A 366 ? 0.1671 0.216  0.6682 0.0091  0.0088  -0.0554 367  ARG A NH2   
2996 N  N     . GLY A 367 ? 0.043  0.0781 0.5104 0.0051  0.007   -0.0498 368  GLY A N     
2997 C  CA    . GLY A 367 ? 0.0434 0.0791 0.5073 0.0051  0.006   -0.0485 368  GLY A CA    
2998 C  C     . GLY A 367 ? 0.0534 0.0908 0.52   0.0051  0.0061  -0.0467 368  GLY A C     
2999 O  O     . GLY A 367 ? 0.0756 0.1109 0.5371 0.0046  0.005   -0.0454 368  GLY A O     
3000 N  N     . ALA A 368 ? 0.0438 0.0828 0.5164 0.0053  0.0074  -0.0467 369  ALA A N     
3001 C  CA    . ALA A 368 ? 0.0407 0.0664 0.5005 0.0028  0.0071  -0.0449 369  ALA A CA    
3002 C  C     . ALA A 368 ? 0.0402 0.0546 0.4873 0.0015  0.0068  -0.0423 369  ALA A C     
3003 O  O     . ALA A 368 ? 0.0399 0.0485 0.4785 0.0004  0.0056  -0.041  369  ALA A O     
3004 C  CB    . ALA A 368 ? 0.0402 0.0598 0.4987 0.0016  0.0083  -0.0453 369  ALA A CB    
3005 N  N     . LEU A 369 ? 0.0406 0.0565 0.4908 0.0024  0.0079  -0.0414 370  LEU A N     
3006 C  CA    . LEU A 369 ? 0.0447 0.0764 0.5104 0.0086  0.0087  -0.0392 370  LEU A CA    
3007 C  C     . LEU A 369 ? 0.0504 0.0788 0.5078 0.0085  0.0069  -0.0391 370  LEU A C     
3008 O  O     . LEU A 369 ? 0.063  0.089  0.5158 0.0085  0.0058  -0.0377 370  LEU A O     
3009 C  CB    . LEU A 369 ? 0.0455 0.0751 0.5121 0.0098  0.0104  -0.038  370  LEU A CB    
3010 C  CG    . LEU A 369 ? 0.0658 0.1002 0.5428 0.0107  0.0122  -0.0375 370  LEU A CG    
3011 C  CD1   . LEU A 369 ? 0.076  0.1104 0.5563 0.0128  0.0141  -0.0358 370  LEU A CD1   
3012 C  CD2   . LEU A 369 ? 0.0854 0.1197 0.562  0.0102  0.0121  -0.0362 370  LEU A CD2   
3013 N  N     . PRO A 370 ? 0.0443 0.0658 0.4921 0.0059  0.006   -0.0405 371  PRO A N     
3014 C  CA    . PRO A 370 ? 0.0453 0.0651 0.4868 0.0059  0.0042  -0.0405 371  PRO A CA    
3015 C  C     . PRO A 370 ? 0.0566 0.0815 0.502  0.0062  0.0027  -0.0403 371  PRO A C     
3016 O  O     . PRO A 370 ? 0.0708 0.0923 0.5103 0.0062  0.0012  -0.0391 371  PRO A O     
3017 C  CB    . PRO A 370 ? 0.0439 0.0594 0.4795 0.0038  0.004   -0.0423 371  PRO A CB    
3018 C  CG    . PRO A 370 ? 0.043  0.0578 0.4813 0.0036  0.0057  -0.0426 371  PRO A CG    
3019 C  CD    . PRO A 370 ? 0.0399 0.0438 0.4651 -0.0006 0.0059  -0.0416 371  PRO A CD    
3020 N  N     . LEU A 371 ? 0.0464 0.0748 0.4965 0.0047  0.0028  -0.0413 372  LEU A N     
3021 C  CA    . LEU A 371 ? 0.0548 0.0835 0.5036 0.003   0.0013  -0.0407 372  LEU A CA    
3022 C  C     . LEU A 371 ? 0.0732 0.1001 0.5207 0.0031  0.0008  -0.0384 372  LEU A C     
3023 O  O     . LEU A 371 ? 0.079  0.1035 0.5216 0.0022  -0.0012 -0.0373 372  LEU A O     
3024 C  CB    . LEU A 371 ? 0.0454 0.0769 0.4984 0.002   0.0019  -0.0419 372  LEU A CB    
3025 C  CG    . LEU A 371 ? 0.0425 0.0552 0.4753 0.0001  0.0007  -0.0409 372  LEU A CG    
3026 C  CD1   . LEU A 371 ? 0.0397 0.0436 0.4497 0.0001  -0.0012 -0.0397 372  LEU A CD1   
3027 C  CD2   . LEU A 371 ? 0.0424 0.052  0.4737 -0.0001 0.0017  -0.0422 372  LEU A CD2   
3028 N  N     . VAL A 372 ? 0.066  0.0939 0.5178 0.0042  0.0027  -0.0378 373  VAL A N     
3029 C  CA    . VAL A 372 ? 0.0633 0.0898 0.5142 0.0046  0.0025  -0.0357 373  VAL A CA    
3030 C  C     . VAL A 372 ? 0.0597 0.0814 0.5031 0.0057  0.0012  -0.0346 373  VAL A C     
3031 O  O     . VAL A 372 ? 0.061  0.0805 0.5007 0.0052  -0.0004 -0.0332 373  VAL A O     
3032 C  CB    . VAL A 372 ? 0.0737 0.102  0.5305 0.006   0.005   -0.0351 373  VAL A CB    
3033 C  CG1   . VAL A 372 ? 0.0819 0.1084 0.5369 0.007   0.0051  -0.0328 373  VAL A CG1   
3034 C  CG2   . VAL A 372 ? 0.0768 0.1092 0.5409 0.005   0.0062  -0.0361 373  VAL A CG2   
3035 N  N     . ALA A 373 ? 0.0548 0.0748 0.4959 0.0073  0.0019  -0.0351 374  ALA A N     
3036 C  CA    . ALA A 373 ? 0.0738 0.0892 0.5076 0.0088  0.0008  -0.0342 374  ALA A CA    
3037 C  C     . ALA A 373 ? 0.0775 0.0899 0.5049 0.0074  -0.0019 -0.0346 374  ALA A C     
3038 O  O     . ALA A 373 ? 0.1064 0.1146 0.5275 0.008   -0.0037 -0.0335 374  ALA A O     
3039 C  CB    . ALA A 373 ? 0.0845 0.0995 0.5183 0.011   0.0025  -0.0346 374  ALA A CB    
3040 N  N     . MET A 374 ? 0.0545 0.069  0.4834 0.0057  -0.0025 -0.036  375  MET A N     
3041 C  CA    . MET A 374 ? 0.0453 0.0575 0.4691 0.0042  -0.0051 -0.0361 375  MET A CA    
3042 C  C     . MET A 374 ? 0.0601 0.072  0.4835 0.0024  -0.007  -0.0346 375  MET A C     
3043 O  O     . MET A 374 ? 0.0653 0.0734 0.4829 0.0018  -0.0096 -0.0339 375  MET A O     
3044 C  CB    . MET A 374 ? 0.0398 0.0431 0.4401 0.0004  -0.0049 -0.0365 375  MET A CB    
3045 C  CG    . MET A 374 ? 0.0492 0.064  0.4742 0.0044  -0.0039 -0.039  375  MET A CG    
3046 S  SD    . MET A 374 ? 0.0868 0.1056 0.515  0.0032  -0.0036 -0.041  375  MET A SD    
3047 C  CE    . MET A 374 ? 0.0395 0.0432 0.4334 0.0006  -0.0062 -0.0389 375  MET A CE    
3048 N  N     . LEU A 375 ? 0.0533 0.0691 0.4827 0.0017  -0.0059 -0.0342 376  LEU A N     
3049 C  CA    . LEU A 375 ? 0.0544 0.0707 0.4845 0.0001  -0.0074 -0.0326 376  LEU A CA    
3050 C  C     . LEU A 375 ? 0.0702 0.0833 0.4972 0.0011  -0.0081 -0.031  376  LEU A C     
3051 O  O     . LEU A 375 ? 0.0728 0.0834 0.4959 0       -0.0107 -0.0298 376  LEU A O     
3052 C  CB    . LEU A 375 ? 0.0421 0.0559 0.472  -0.0003 -0.0055 -0.0327 376  LEU A CB    
3053 C  CG    . LEU A 375 ? 0.0407 0.0616 0.477  -0.0016 -0.0055 -0.0339 376  LEU A CG    
3054 C  CD1   . LEU A 375 ? 0.04   0.0551 0.4729 -0.0008 -0.0032 -0.0343 376  LEU A CD1   
3055 C  CD2   . LEU A 375 ? 0.0432 0.0673 0.4805 -0.004  -0.0083 -0.0328 376  LEU A CD2   
3056 N  N     . ALA A 376 ? 0.0795 0.0929 0.5084 0.0032  -0.0058 -0.0308 377  ALA A N     
3057 C  CA    . ALA A 376 ? 0.0948 0.1062 0.5217 0.0045  -0.006  -0.0292 377  ALA A CA    
3058 C  C     . ALA A 376 ? 0.1161 0.1228 0.5367 0.0071  -0.0061 -0.0289 377  ALA A C     
3059 O  O     . ALA A 376 ? 0.1318 0.1364 0.5496 0.0084  -0.0066 -0.0275 377  ALA A O     
3060 C  CB    . ALA A 376 ? 0.0881 0.1035 0.5221 0.0052  -0.0032 -0.0286 377  ALA A CB    
3061 N  N     . GLY A 377 ? 0.1107 0.1161 0.5291 0.0081  -0.0056 -0.0302 378  GLY A N     
3062 C  CA    . GLY A 377 ? 0.1072 0.1085 0.5197 0.0109  -0.0054 -0.0299 378  GLY A CA    
3063 C  C     . GLY A 377 ? 0.0998 0.1038 0.5172 0.0131  -0.002  -0.0297 378  GLY A C     
3064 O  O     . GLY A 377 ? 0.0837 0.0916 0.5079 0.013   -0.0002 -0.0292 378  GLY A O     
3065 N  N     . GLU A 378 ? 0.0948 0.0969 0.5093 0.0152  -0.0011 -0.03   379  GLU A N     
3066 C  CA    . GLU A 378 ? 0.0942 0.0989 0.5135 0.0173  0.002   -0.0295 379  GLU A CA    
3067 C  C     . GLU A 378 ? 0.1099 0.1141 0.5294 0.0199  0.0034  -0.0274 379  GLU A C     
3068 O  O     . GLU A 378 ? 0.1111 0.1185 0.5367 0.0211  0.006   -0.0266 379  GLU A O     
3069 C  CB    . GLU A 378 ? 0.0974 0.1003 0.5134 0.019   0.0026  -0.0301 379  GLU A CB    
3070 C  CG    . GLU A 378 ? 0.1262 0.1236 0.5332 0.0216  0.0017  -0.029  379  GLU A CG    
3071 C  CD    . GLU A 378 ? 0.1567 0.1521 0.5595 0.0229  0.0019  -0.0296 379  GLU A CD    
3072 O  OE1   . GLU A 378 ? 0.1733 0.1705 0.5783 0.0209  0.0016  -0.0313 379  GLU A OE1   
3073 O  OE2   . GLU A 378 ? 0.1196 0.1115 0.5168 0.0261  0.0024  -0.0284 379  GLU A OE2   
3074 N  N     . ASN A 379 ? 0.1264 0.1268 0.5395 0.0207  0.0015  -0.0264 380  ASN A N     
3075 C  CA    . ASN A 379 ? 0.1467 0.1466 0.5594 0.0233  0.0027  -0.0243 380  ASN A CA    
3076 C  C     . ASN A 379 ? 0.1572 0.1605 0.5756 0.0218  0.003   -0.0235 380  ASN A C     
3077 O  O     . ASN A 379 ? 0.1745 0.1779 0.5933 0.0239  0.0042  -0.0216 380  ASN A O     
3078 C  CB    . ASN A 379 ? 0.1829 0.1768 0.5854 0.0256  0.0007  -0.0235 380  ASN A CB    
3079 N  N     . ALA A 380 ? 0.1459 0.152  0.569  0.0184  0.0024  -0.0247 381  ALA A N     
3080 C  CA    . ALA A 380 ? 0.1467 0.1565 0.576  0.0171  0.0031  -0.024  381  ALA A CA    
3081 C  C     . ALA A 380 ? 0.1552 0.1689 0.5923 0.0185  0.0065  -0.0233 381  ALA A C     
3082 O  O     . ALA A 380 ? 0.1598 0.1746 0.5995 0.0191  0.0079  -0.0241 381  ALA A O     
3083 C  CB    . ALA A 380 ? 0.1463 0.1586 0.579  0.0136  0.0019  -0.0254 381  ALA A CB    
3084 N  N     . GLN A 381 ? 0.1545 0.1704 0.5957 0.0192  0.0078  -0.0216 382  GLN A N     
3085 C  CA    . GLN A 381 ? 0.1525 0.1722 0.6017 0.0205  0.0111  -0.0207 382  GLN A CA    
3086 C  C     . GLN A 381 ? 0.1365 0.16   0.5934 0.018   0.0118  -0.0223 382  GLN A C     
3087 O  O     . GLN A 381 ? 0.13   0.1551 0.5889 0.0159  0.011   -0.0227 382  GLN A O     
3088 C  CB    . GLN A 381 ? 0.1951 0.2157 0.6459 0.0222  0.0122  -0.0183 382  GLN A CB    
3089 C  CG    . GLN A 381 ? 0.3004 0.3174 0.7441 0.0256  0.0121  -0.0166 382  GLN A CG    
3090 C  CD    . GLN A 381 ? 0.4265 0.4452 0.873  0.0277  0.0139  -0.014  382  GLN A CD    
3091 O  OE1   . GLN A 381 ? 0.4285 0.4512 0.8834 0.0281  0.0166  -0.013  382  GLN A OE1   
3092 N  NE2   . GLN A 381 ? 0.4736 0.4891 0.9129 0.0291  0.0122  -0.0128 382  GLN A NE2   
3093 N  N     . ILE A 382 ? 0.1191 0.1442 0.5803 0.0184  0.0133  -0.0234 383  ILE A N     
3094 C  CA    . ILE A 382 ? 0.1011 0.1297 0.5693 0.0162  0.0139  -0.0253 383  ILE A CA    
3095 C  C     . ILE A 382 ? 0.0849 0.1168 0.562  0.0172  0.0167  -0.0245 383  ILE A C     
3096 O  O     . ILE A 382 ? 0.0819 0.1137 0.5604 0.0193  0.0181  -0.0235 383  ILE A O     
3097 C  CB    . ILE A 382 ? 0.1017 0.1293 0.5673 0.0152  0.0127  -0.0276 383  ILE A CB    
3098 C  CG1   . ILE A 382 ? 0.103  0.1274 0.5603 0.0139  0.0099  -0.0282 383  ILE A CG1   
3099 C  CG2   . ILE A 382 ? 0.1032 0.1341 0.5756 0.0134  0.0133  -0.0297 383  ILE A CG2   
3100 C  CD1   . ILE A 382 ? 0.1186 0.1414 0.572  0.0135  0.0087  -0.03   383  ILE A CD1   
3101 N  N     . PHE A 383 ? 0.06   0.0947 0.5432 0.0158  0.0174  -0.0249 384  PHE A N     
3102 C  CA    . PHE A 383 ? 0.0668 0.1046 0.5592 0.0162  0.0197  -0.0244 384  PHE A CA    
3103 C  C     . PHE A 383 ? 0.0574 0.0968 0.5537 0.0143  0.0193  -0.0273 384  PHE A C     
3104 O  O     . PHE A 383 ? 0.0592 0.0994 0.5552 0.0124  0.0182  -0.0286 384  PHE A O     
3105 C  CB    . PHE A 383 ? 0.074  0.1135 0.5695 0.016   0.0205  -0.0229 384  PHE A CB    
3106 C  CG    . PHE A 383 ? 0.0855 0.1281 0.5905 0.0166  0.023   -0.0219 384  PHE A CG    
3107 C  CD1   . PHE A 383 ? 0.0948 0.1395 0.6062 0.015   0.0234  -0.0239 384  PHE A CD1   
3108 C  CD2   . PHE A 383 ? 0.0981 0.1412 0.6053 0.0189  0.0249  -0.019  384  PHE A CD2   
3109 C  CE1   . PHE A 383 ? 0.1027 0.1499 0.6228 0.0155  0.0255  -0.0231 384  PHE A CE1   
3110 C  CE2   . PHE A 383 ? 0.1063 0.1522 0.6225 0.0194  0.0271  -0.018  384  PHE A CE2   
3111 C  CZ    . PHE A 383 ? 0.1    0.1478 0.6226 0.0176  0.0274  -0.0201 384  PHE A CZ    
3112 N  N     . THR A 384 ? 0.0451 0.0768 0.5355 0.0114  0.0195  -0.028  385  THR A N     
3113 C  CA    . THR A 384 ? 0.0455 0.086  0.5477 0.0128  0.0194  -0.0311 385  THR A CA    
3114 C  C     . THR A 384 ? 0.0475 0.0915 0.5603 0.0132  0.0211  -0.0313 385  THR A C     
3115 O  O     . THR A 384 ? 0.0461 0.0901 0.5625 0.0144  0.0225  -0.0298 385  THR A O     
3116 C  CB    . THR A 384 ? 0.0765 0.1168 0.5768 0.0136  0.0187  -0.0322 385  THR A CB    
3117 O  OG1   . THR A 384 ? 0.0998 0.1373 0.591  0.0136  0.0171  -0.0321 385  THR A OG1   
3118 C  CG2   . THR A 384 ? 0.0775 0.1192 0.5811 0.0121  0.018   -0.0353 385  THR A CG2   
3119 N  N     . PHE A 385 ? 0.0445 0.0889 0.5594 0.0113  0.0208  -0.033  386  PHE A N     
3120 C  CA    . PHE A 385 ? 0.0442 0.0902 0.5674 0.011   0.022   -0.0336 386  PHE A CA    
3121 C  C     . PHE A 385 ? 0.0488 0.097  0.5761 0.0104  0.0211  -0.037  386  PHE A C     
3122 O  O     . PHE A 385 ? 0.0496 0.0977 0.5733 0.0092  0.0197  -0.0392 386  PHE A O     
3123 C  CB    . PHE A 385 ? 0.0435 0.0857 0.5632 0.0091  0.0222  -0.0331 386  PHE A CB    
3124 C  CG    . PHE A 385 ? 0.0437 0.0903 0.575  0.0097  0.0237  -0.0337 386  PHE A CG    
3125 C  CD1   . PHE A 385 ? 0.0447 0.0961 0.5863 0.012   0.0259  -0.0315 386  PHE A CD1   
3126 C  CD2   . PHE A 385 ? 0.052  0.1034 0.5898 0.0095  0.0233  -0.0366 386  PHE A CD2   
3127 C  CE1   . PHE A 385 ? 0.0536 0.1064 0.6036 0.0118  0.027   -0.032  386  PHE A CE1   
3128 C  CE2   . PHE A 385 ? 0.0537 0.1062 0.5993 0.0095  0.0244  -0.0373 386  PHE A CE2   
3129 C  CZ    . PHE A 385 ? 0.0507 0.1039 0.6025 0.0106  0.0262  -0.0351 386  PHE A CZ    
3130 N  N     . ILE A 386 ? 0.0501 0.099  0.5836 0.0109  0.0217  -0.0374 387  ILE A N     
3131 C  CA    . ILE A 386 ? 0.0542 0.1036 0.5907 0.0101  0.0207  -0.0405 387  ILE A CA    
3132 C  C     . ILE A 386 ? 0.0464 0.0971 0.5917 0.0098  0.0214  -0.0415 387  ILE A C     
3133 O  O     . ILE A 386 ? 0.0439 0.0952 0.5952 0.0106  0.0229  -0.0393 387  ILE A O     
3134 C  CB    . ILE A 386 ? 0.0547 0.1036 0.5903 0.0108  0.0204  -0.0401 387  ILE A CB    
3135 C  CG1   . ILE A 386 ? 0.076  0.1232 0.6027 0.0113  0.0198  -0.0389 387  ILE A CG1   
3136 C  CG2   . ILE A 386 ? 0.0578 0.1073 0.5959 0.0098  0.019   -0.0434 387  ILE A CG2   
3137 C  CD1   . ILE A 386 ? 0.0936 0.1401 0.6136 0.0101  0.0181  -0.0411 387  ILE A CD1   
3138 N  N     . TYR A 387 ? 0.0429 0.094  0.5893 0.0087  0.0202  -0.0448 388  TYR A N     
3139 C  CA    . TYR A 387 ? 0.0429 0.0946 0.5972 0.0085  0.0207  -0.0461 388  TYR A CA    
3140 C  C     . TYR A 387 ? 0.0425 0.0943 0.6001 0.0079  0.0191  -0.0497 388  TYR A C     
3141 O  O     . TYR A 387 ? 0.0425 0.0944 0.606  0.0077  0.0192  -0.0512 388  TYR A O     
3142 C  CB    . TYR A 387 ? 0.0428 0.095  0.5962 0.0082  0.0212  -0.0461 388  TYR A CB    
3143 C  CG    . TYR A 387 ? 0.0425 0.0945 0.5888 0.0075  0.0199  -0.048  388  TYR A CG    
3144 C  CD1   . TYR A 387 ? 0.0424 0.0932 0.5807 0.0072  0.0197  -0.0463 388  TYR A CD1   
3145 C  CD2   . TYR A 387 ? 0.0423 0.0945 0.5891 0.0071  0.0188  -0.0514 388  TYR A CD2   
3146 C  CE1   . TYR A 387 ? 0.0421 0.0939 0.5754 0.0067  0.0185  -0.0476 388  TYR A CE1   
3147 C  CE2   . TYR A 387 ? 0.0462 0.0987 0.5868 0.0067  0.0178  -0.0528 388  TYR A CE2   
3148 C  CZ    . TYR A 387 ? 0.0513 0.1037 0.5854 0.0064  0.0176  -0.0508 388  TYR A CZ    
3149 O  OH    . TYR A 387 ? 0.074  0.1269 0.6025 0.0059  0.0166  -0.0518 388  TYR A OH    
3150 N  N     . GLY A 388 ? 0.0424 0.0938 0.5962 0.0076  0.0178  -0.051  389  GLY A N     
3151 C  CA    . GLY A 388 ? 0.0544 0.1058 0.6107 0.0071  0.0161  -0.0544 389  GLY A CA    
3152 C  C     . GLY A 388 ? 0.0709 0.1225 0.6348 0.0073  0.0161  -0.0538 389  GLY A C     
3153 O  O     . GLY A 388 ? 0.0817 0.1337 0.6478 0.008   0.0174  -0.0504 389  GLY A O     
3154 N  N     . PRO A 389 ? 0.0647 0.1163 0.6328 0.0067  0.0145  -0.0569 390  PRO A N     
3155 C  CA    . PRO A 389 ? 0.0597 0.1116 0.636  0.0066  0.0142  -0.0563 390  PRO A CA    
3156 C  C     . PRO A 389 ? 0.0624 0.1148 0.6372 0.007   0.0141  -0.0543 390  PRO A C     
3157 O  O     . PRO A 389 ? 0.0797 0.1321 0.6481 0.0068  0.0131  -0.0557 390  PRO A O     
3158 C  CB    . PRO A 389 ? 0.0658 0.1171 0.6455 0.0059  0.012   -0.0606 390  PRO A CB    
3159 C  CG    . PRO A 389 ? 0.0827 0.1336 0.6564 0.0059  0.0114  -0.0633 390  PRO A CG    
3160 C  CD    . PRO A 389 ? 0.0624 0.1136 0.6283 0.0063  0.0128  -0.0611 390  PRO A CD    
3161 N  N     . LEU A 390 ? 0.042  0.0951 0.6228 0.0075  0.0154  -0.0509 391  LEU A N     
3162 C  CA    . LEU A 390 ? 0.0443 0.0981 0.6246 0.0082  0.0156  -0.0486 391  LEU A CA    
3163 C  C     . LEU A 390 ? 0.0482 0.1027 0.637  0.0076  0.0143  -0.049  391  LEU A C     
3164 O  O     . LEU A 390 ? 0.0418 0.0965 0.6389 0.0073  0.0145  -0.0487 391  LEU A O     
3165 C  CB    . LEU A 390 ? 0.0429 0.0972 0.6233 0.0096  0.0181  -0.0437 391  LEU A CB    
3166 C  CG    . LEU A 390 ? 0.0637 0.1171 0.6362 0.0103  0.0193  -0.0426 391  LEU A CG    
3167 C  CD1   . LEU A 390 ? 0.0735 0.1274 0.6467 0.012   0.0215  -0.0379 391  LEU A CD1   
3168 C  CD2   . LEU A 390 ? 0.0692 0.1218 0.632  0.0101  0.0182  -0.0442 391  LEU A CD2   
3169 N  N     . ILE A 391 ? 0.0529 0.108  0.64   0.0075  0.0131  -0.0495 392  ILE A N     
3170 C  CA    . ILE A 391 ? 0.07   0.1261 0.6653 0.0069  0.0119  -0.0494 392  ILE A CA    
3171 C  C     . ILE A 391 ? 0.0672 0.1245 0.6686 0.0081  0.0141  -0.0441 392  ILE A C     
3172 O  O     . ILE A 391 ? 0.0777 0.1351 0.6742 0.0096  0.0162  -0.0409 392  ILE A O     
3173 C  CB    . ILE A 391 ? 0.0941 0.1507 0.6853 0.0066  0.0102  -0.0511 392  ILE A CB    
3174 C  CG1   . ILE A 391 ? 0.1227 0.1794 0.7057 0.0079  0.0117  -0.0484 392  ILE A CG1   
3175 C  CG2   . ILE A 391 ? 0.097  0.1526 0.684  0.0055  0.0079  -0.0563 392  ILE A CG2   
3176 C  CD1   . ILE A 391 ? 0.1478 0.2054 0.7287 0.008   0.0107  -0.0484 392  ILE A CD1   
3177 N  N     . LYS A 392 ? 0.0452 0.1035 0.6571 0.0076  0.0135  -0.0429 393  LYS A N     
3178 C  CA    . LYS A 392 ? 0.0443 0.1042 0.6627 0.0089  0.0156  -0.0377 393  LYS A CA    
3179 C  C     . LYS A 392 ? 0.0518 0.1128 0.6651 0.0107  0.0172  -0.0339 393  LYS A C     
3180 O  O     . LYS A 392 ? 0.0523 0.1138 0.6646 0.0125  0.0197  -0.03   393  LYS A O     
3181 C  CB    . LYS A 392 ? 0.0724 0.1334 0.703  0.008   0.0143  -0.037  393  LYS A CB    
3182 C  CG    . LYS A 392 ? 0.1085 0.1714 0.7471 0.0093  0.0167  -0.0314 393  LYS A CG    
3183 C  CD    . LYS A 392 ? 0.1378 0.2    0.7763 0.0101  0.0189  -0.0302 393  LYS A CD    
3184 C  CE    . LYS A 392 ? 0.2259 0.2901 0.8736 0.0114  0.0211  -0.0248 393  LYS A CE    
3185 N  NZ    . LYS A 392 ? 0.2854 0.3492 0.9338 0.0122  0.0232  -0.0235 393  LYS A NZ    
3186 N  N     . GLY A 393 ? 0.055  0.1163 0.6645 0.0103  0.0158  -0.0352 394  GLY A N     
3187 C  CA    . GLY A 393 ? 0.0693 0.1313 0.6732 0.0121  0.0171  -0.0321 394  GLY A CA    
3188 C  C     . GLY A 393 ? 0.0867 0.1472 0.6802 0.0135  0.0189  -0.0313 394  GLY A C     
3189 O  O     . GLY A 393 ? 0.1    0.1609 0.6905 0.0156  0.0208  -0.0274 394  GLY A O     
3190 N  N     . ALA A 394 ? 0.0824 0.1411 0.6704 0.0125  0.0182  -0.0348 395  ALA A N     
3191 C  CA    . ALA A 394 ? 0.0902 0.1475 0.6685 0.0137  0.0195  -0.0341 395  ALA A CA    
3192 C  C     . ALA A 394 ? 0.0998 0.1573 0.6807 0.0151  0.0219  -0.0304 395  ALA A C     
3193 O  O     . ALA A 394 ? 0.1158 0.173  0.6918 0.0171  0.0235  -0.0272 395  ALA A O     
3194 C  CB    . ALA A 394 ? 0.0824 0.1381 0.6544 0.0122  0.018   -0.0385 395  ALA A CB    
3195 N  N     . ILE A 395 ? 0.0866 0.1447 0.6754 0.0144  0.0221  -0.0306 396  ILE A N     
3196 C  CA    . ILE A 395 ? 0.0769 0.1355 0.669  0.0159  0.0245  -0.0269 396  ILE A CA    
3197 C  C     . ILE A 395 ? 0.0603 0.1207 0.6572 0.018   0.0262  -0.0218 396  ILE A C     
3198 O  O     . ILE A 395 ? 0.0553 0.116  0.65   0.0202  0.0285  -0.0181 396  ILE A O     
3199 C  CB    . ILE A 395 ? 0.0705 0.1292 0.6699 0.0147  0.0244  -0.0283 396  ILE A CB    
3200 C  CG1   . ILE A 395 ? 0.0812 0.1404 0.6818 0.0162  0.0269  -0.0247 396  ILE A CG1   
3201 C  CG2   . ILE A 395 ? 0.0659 0.1257 0.6763 0.0134  0.0232  -0.0289 396  ILE A CG2   
3202 C  CD1   . ILE A 395 ? 0.0961 0.1538 0.6858 0.017   0.0276  -0.0248 396  ILE A CD1   
3203 N  N     . ASN A 396 ? 0.056  0.1178 0.6586 0.0174  0.0252  -0.0216 397  ASN A N     
3204 C  CA    . ASN A 396 ? 0.0572 0.1211 0.6644 0.0195  0.0269  -0.0165 397  ASN A CA    
3205 C  C     . ASN A 396 ? 0.0738 0.1369 0.6709 0.0219  0.0282  -0.0143 397  ASN A C     
3206 O  O     . ASN A 396 ? 0.0651 0.1292 0.6626 0.0246  0.0306  -0.0096 397  ASN A O     
3207 C  CB    . ASN A 396 ? 0.0489 0.1145 0.6642 0.0182  0.0252  -0.0168 397  ASN A CB    
3208 C  CG    . ASN A 396 ? 0.0664 0.1332 0.6942 0.0169  0.0247  -0.0165 397  ASN A CG    
3209 O  OD1   . ASN A 396 ? 0.0544 0.1214 0.6861 0.0176  0.0263  -0.0147 397  ASN A OD1   
3210 N  ND2   . ASN A 396 ? 0.062  0.1295 0.6964 0.0151  0.0224  -0.0182 397  ASN A ND2   
3211 N  N     . LEU A 397 ? 0.0962 0.1575 0.684  0.0211  0.0267  -0.0176 398  LEU A N     
3212 C  CA    . LEU A 397 ? 0.1123 0.1723 0.6898 0.0232  0.0276  -0.016  398  LEU A CA    
3213 C  C     . LEU A 397 ? 0.1318 0.19   0.7026 0.0246  0.029   -0.015  398  LEU A C     
3214 O  O     . LEU A 397 ? 0.1489 0.2066 0.7148 0.0273  0.0306  -0.0117 398  LEU A O     
3215 C  CB    . LEU A 397 ? 0.1186 0.1771 0.6886 0.0218  0.0255  -0.0199 398  LEU A CB    
3216 C  CG    . LEU A 397 ? 0.1301 0.1902 0.7036 0.0214  0.0245  -0.0198 398  LEU A CG    
3217 C  CD1   . LEU A 397 ? 0.1339 0.1926 0.6996 0.02    0.0225  -0.0237 398  LEU A CD1   
3218 C  CD2   . LEU A 397 ? 0.1419 0.2032 0.7154 0.0243  0.0266  -0.0146 398  LEU A CD2   
3219 N  N     . ILE A 398 ? 0.1325 0.1898 0.7032 0.023   0.0283  -0.0177 399  ILE A N     
3220 C  CA    . ILE A 398 ? 0.1494 0.2054 0.7149 0.024   0.0295  -0.0168 399  ILE A CA    
3221 C  C     . ILE A 398 ? 0.1577 0.2153 0.7285 0.0267  0.0322  -0.0116 399  ILE A C     
3222 O  O     . ILE A 398 ? 0.17   0.2266 0.7345 0.0292  0.0336  -0.0091 399  ILE A O     
3223 C  CB    . ILE A 398 ? 0.1596 0.215  0.7267 0.0215  0.0283  -0.0204 399  ILE A CB    
3224 C  CG1   . ILE A 398 ? 0.1768 0.2302 0.7353 0.0198  0.0262  -0.0247 399  ILE A CG1   
3225 C  CG2   . ILE A 398 ? 0.1632 0.2185 0.7302 0.0225  0.0299  -0.0185 399  ILE A CG2   
3226 C  CD1   . ILE A 398 ? 0.1886 0.2421 0.7501 0.0174  0.0248  -0.0284 399  ILE A CD1   
3227 N  N     . ASP A 399 ? 0.1477 0.2079 0.7299 0.0265  0.0328  -0.0099 400  ASP A N     
3228 C  CA    . ASP A 399 ? 0.1583 0.2205 0.7467 0.029   0.0354  -0.0048 400  ASP A CA    
3229 C  C     . ASP A 399 ? 0.1728 0.2362 0.7604 0.032   0.0368  -0.0005 400  ASP A C     
3230 O  O     . ASP A 399 ? 0.1907 0.2557 0.7814 0.0348  0.0393  0.0042  400  ASP A O     
3231 C  CB    . ASP A 399 ? 0.1644 0.2289 0.7659 0.0276  0.0354  -0.0044 400  ASP A CB    
3232 C  CG    . ASP A 399 ? 0.1892 0.2528 0.7921 0.0254  0.0346  -0.0077 400  ASP A CG    
3233 O  OD1   . ASP A 399 ? 0.1946 0.2565 0.7896 0.0257  0.0348  -0.0088 400  ASP A OD1   
3234 O  OD2   . ASP A 399 ? 0.2079 0.2724 0.8198 0.0234  0.0336  -0.0093 400  ASP A OD2   
3235 N  N     . GLN A 400 ? 0.1584 0.2212 0.7421 0.0316  0.0356  -0.0018 401  GLN A N     
3236 C  CA    . GLN A 400 ? 0.1532 0.2171 0.7359 0.0344  0.037   0.0023  401  GLN A CA    
3237 C  C     . GLN A 400 ? 0.1538 0.2147 0.7228 0.0365  0.0372  0.0021  401  GLN A C     
3238 O  O     . GLN A 400 ? 0.1563 0.2171 0.7218 0.04    0.0392  0.0061  401  GLN A O     
3239 C  CB    . GLN A 400 ? 0.1634 0.229  0.7522 0.0329  0.0356  0.0017  401  GLN A CB    
3240 N  N     . ASP A 401 ? 0.1499 0.2083 0.7113 0.0343  0.0349  -0.0025 402  ASP A N     
3241 C  CA    . ASP A 401 ? 0.1585 0.2138 0.7074 0.0357  0.0346  -0.0032 402  ASP A CA    
3242 C  C     . ASP A 401 ? 0.1487 0.2018 0.692  0.0324  0.032   -0.0087 402  ASP A C     
3243 O  O     . ASP A 401 ? 0.1391 0.1926 0.6832 0.0305  0.0303  -0.0113 402  ASP A O     
3244 C  CB    . ASP A 401 ? 0.1921 0.2482 0.74   0.0374  0.0351  -0.001  402  ASP A CB    
3245 C  CG    . ASP A 401 ? 0.2953 0.3481 0.8306 0.0389  0.0347  -0.0017 402  ASP A CG    
3246 O  OD1   . ASP A 401 ? 0.3176 0.3673 0.8443 0.0394  0.0344  -0.0028 402  ASP A OD1   
3247 O  OD2   . ASP A 401 ? 0.3515 0.4047 0.8856 0.0394  0.0345  -0.0011 402  ASP A OD2   
3248 N  N     . ILE A 402 ? 0.1448 0.1957 0.6826 0.032   0.0316  -0.0102 403  ILE A N     
3249 C  CA    . ILE A 402 ? 0.147  0.1961 0.6798 0.0291  0.0293  -0.015  403  ILE A CA    
3250 C  C     . ILE A 402 ? 0.1393 0.1863 0.6632 0.029   0.028   -0.0167 403  ILE A C     
3251 O  O     . ILE A 402 ? 0.1416 0.1884 0.6645 0.0265  0.026   -0.0205 403  ILE A O     
3252 C  CB    . ILE A 402 ? 0.1598 0.2073 0.6888 0.029   0.0294  -0.0154 403  ILE A CB    
3253 C  CG1   . ILE A 402 ? 0.1879 0.2344 0.7143 0.0258  0.0272  -0.02   403  ILE A CG1   
3254 C  CG2   . ILE A 402 ? 0.1664 0.2112 0.6857 0.0318  0.0301  -0.0131 403  ILE A CG2   
3255 C  CD1   . ILE A 402 ? 0.2113 0.2597 0.7452 0.0232  0.0261  -0.0228 403  ILE A CD1   
3256 N  N     . ASN A 403 ? 0.1306 0.1762 0.6485 0.032   0.029   -0.0139 404  ASN A N     
3257 C  CA    . ASN A 403 ? 0.1265 0.1698 0.6357 0.0322  0.028   -0.0152 404  ASN A CA    
3258 C  C     . ASN A 403 ? 0.1121 0.1575 0.6257 0.0309  0.0272  -0.0164 404  ASN A C     
3259 O  O     . ASN A 403 ? 0.1107 0.1547 0.6186 0.0298  0.0257  -0.0189 404  ASN A O     
3260 C  CB    . ASN A 403 ? 0.1457 0.1866 0.6471 0.0359  0.0294  -0.0119 404  ASN A CB    
3261 C  CG    . ASN A 403 ? 0.1758 0.2138 0.6704 0.0368  0.0292  -0.0119 404  ASN A CG    
3262 O  OD1   . ASN A 403 ? 0.1731 0.2099 0.6652 0.0343  0.0275  -0.015  404  ASN A OD1   
3263 N  ND2   . ASN A 403 ? 0.1918 0.2289 0.6837 0.0403  0.031   -0.0082 404  ASN A ND2   
3264 N  N     . LYS A 404 ? 0.0983 0.1471 0.6222 0.0309  0.0281  -0.0146 405  LYS A N     
3265 C  CA    . LYS A 404 ? 0.1043 0.1553 0.6336 0.0294  0.0271  -0.0158 405  LYS A CA    
3266 C  C     . LYS A 404 ? 0.099  0.15   0.6291 0.0258  0.0247  -0.0209 405  LYS A C     
3267 O  O     . LYS A 404 ? 0.1023 0.1533 0.63   0.0246  0.0232  -0.0233 405  LYS A O     
3268 C  CB    . LYS A 404 ? 0.1352 0.1898 0.6764 0.0299  0.0283  -0.0126 405  LYS A CB    
3269 C  CG    . LYS A 404 ? 0.202  0.2588 0.7475 0.0297  0.0278  -0.012  405  LYS A CG    
3270 C  CD    . LYS A 404 ? 0.2676 0.3279 0.8242 0.0308  0.0293  -0.0077 405  LYS A CD    
3271 C  CE    . LYS A 404 ? 0.325  0.3871 0.883  0.0316  0.0293  -0.0059 405  LYS A CE    
3272 N  NZ    . LYS A 404 ? 0.3375 0.4031 0.9059 0.0331  0.0309  -0.0009 405  LYS A NZ    
3273 N  N     . LEU A 405 ? 0.1022 0.1531 0.6351 0.0244  0.0243  -0.0225 406  LEU A N     
3274 C  CA    . LEU A 405 ? 0.11   0.1607 0.6433 0.0214  0.0223  -0.0271 406  LEU A CA    
3275 C  C     . LEU A 405 ? 0.1233 0.1714 0.6457 0.0209  0.0211  -0.0295 406  LEU A C     
3276 O  O     . LEU A 405 ? 0.1283 0.1765 0.649  0.0192  0.0194  -0.0327 406  LEU A O     
3277 C  CB    . LEU A 405 ? 0.1111 0.1623 0.6495 0.0208  0.0228  -0.0271 406  LEU A CB    
3278 C  CG    . LEU A 405 ? 0.132  0.1836 0.6738 0.018   0.0211  -0.0312 406  LEU A CG    
3279 C  CD1   . LEU A 405 ? 0.1308 0.1844 0.68   0.0166  0.0198  -0.0329 406  LEU A CD1   
3280 C  CD2   . LEU A 405 ? 0.142  0.1941 0.6893 0.0179  0.022   -0.0304 406  LEU A CD2   
3281 N  N     . ALA A 406 ? 0.1229 0.1684 0.6378 0.0225  0.0219  -0.0278 407  ALA A N     
3282 C  CA    . ALA A 406 ? 0.131  0.1736 0.6355 0.0222  0.0208  -0.0295 407  ALA A CA    
3283 C  C     . ALA A 406 ? 0.1504 0.1925 0.6503 0.0226  0.0202  -0.03   407  ALA A C     
3284 O  O     . ALA A 406 ? 0.1514 0.1923 0.6456 0.0213  0.0186  -0.0327 407  ALA A O     
3285 C  CB    . ALA A 406 ? 0.1277 0.1677 0.626  0.0244  0.0218  -0.027  407  ALA A CB    
3286 N  N     . LYS A 407 ? 0.1567 0.2001 0.6595 0.0245  0.0214  -0.0272 408  LYS A N     
3287 C  CA    . LYS A 407 ? 0.1737 0.2168 0.6724 0.0251  0.0211  -0.0273 408  LYS A CA    
3288 C  C     . LYS A 407 ? 0.1856 0.2307 0.6876 0.0226  0.0194  -0.0308 408  LYS A C     
3289 O  O     . LYS A 407 ? 0.1966 0.2408 0.6926 0.0222  0.0184  -0.0324 408  LYS A O     
3290 C  CB    . LYS A 407 ? 0.2056 0.2498 0.7069 0.0279  0.0231  -0.0231 408  LYS A CB    
3291 C  CG    . LYS A 407 ? 0.2782 0.3224 0.7756 0.0288  0.023   -0.0227 408  LYS A CG    
3292 C  CD    . LYS A 407 ? 0.373  0.4182 0.8724 0.032   0.0252  -0.018  408  LYS A CD    
3293 C  CE    . LYS A 407 ? 0.4514 0.4928 0.9403 0.035   0.0262  -0.0159 408  LYS A CE    
3294 N  NZ    . LYS A 407 ? 0.4896 0.5317 0.9775 0.0378  0.0277  -0.0125 408  LYS A NZ    
3295 N  N     . ARG A 408 ? 0.1918 0.2395 0.7028 0.0209  0.0188  -0.0321 409  ARG A N     
3296 C  CA    . ARG A 408 ? 0.2098 0.2594 0.7241 0.0188  0.0171  -0.0354 409  ARG A CA    
3297 C  C     . ARG A 408 ? 0.2065 0.2557 0.7193 0.0166  0.0154  -0.0394 409  ARG A C     
3298 O  O     . ARG A 408 ? 0.2209 0.271  0.733  0.0152  0.0138  -0.0424 409  ARG A O     
3299 C  CB    . ARG A 408 ? 0.2512 0.3039 0.7764 0.0184  0.0171  -0.0345 409  ARG A CB    
3300 C  CG    . ARG A 408 ? 0.3271 0.3805 0.8594 0.0182  0.0179  -0.0334 409  ARG A CG    
3301 C  CD    . ARG A 408 ? 0.3859 0.442  0.9286 0.0185  0.0184  -0.0311 409  ARG A CD    
3302 N  NE    . ARG A 408 ? 0.4436 0.5014 0.9932 0.0162  0.0163  -0.0343 409  ARG A NE    
3303 C  CZ    . ARG A 408 ? 0.4816 0.5397 1.0372 0.0147  0.0156  -0.0362 409  ARG A CZ    
3304 N  NH1   . ARG A 408 ? 0.4797 0.5391 1.0411 0.0128  0.0135  -0.0392 409  ARG A NH1   
3305 N  NH2   . ARG A 408 ? 0.4795 0.5366 1.0352 0.0152  0.0169  -0.0351 409  ARG A NH2   
3306 N  N     . ASN A 409 ? 0.1802 0.2281 0.6921 0.0163  0.0157  -0.0395 410  ASN A N     
3307 C  CA    . ASN A 409 ? 0.163  0.2108 0.674  0.0144  0.0143  -0.043  410  ASN A CA    
3308 C  C     . ASN A 409 ? 0.1461 0.1912 0.6483 0.0145  0.0142  -0.0431 410  ASN A C     
3309 O  O     . ASN A 409 ? 0.1542 0.1978 0.6546 0.0156  0.0153  -0.0406 410  ASN A O     
3310 C  CB    . ASN A 409 ? 0.1766 0.2257 0.6961 0.0136  0.0145  -0.0434 410  ASN A CB    
3311 C  CG    . ASN A 409 ? 0.2196 0.2689 0.7391 0.0118  0.0132  -0.047  410  ASN A CG    
3312 O  OD1   . ASN A 409 ? 0.2355 0.2835 0.7506 0.0115  0.0132  -0.0472 410  ASN A OD1   
3313 N  ND2   . ASN A 409 ? 0.2318 0.2829 0.7564 0.0106  0.0119  -0.0497 410  ASN A ND2   
3314 N  N     . GLY A 410 ? 0.1167 0.1614 0.6137 0.0133  0.0127  -0.0457 411  GLY A N     
3315 C  CA    . GLY A 410 ? 0.106  0.1484 0.5953 0.0131  0.0122  -0.046  411  GLY A CA    
3316 C  C     . GLY A 410 ? 0.0931 0.135  0.5836 0.0125  0.0124  -0.0458 411  GLY A C     
3317 O  O     . GLY A 410 ? 0.0988 0.1384 0.5838 0.0129  0.0126  -0.0443 411  GLY A O     
3318 N  N     . LEU A 411 ? 0.0796 0.1236 0.5772 0.0115  0.0124  -0.0472 412  LEU A N     
3319 C  CA    . LEU A 411 ? 0.0773 0.121  0.5765 0.011   0.0128  -0.0468 412  LEU A CA    
3320 C  C     . LEU A 411 ? 0.073  0.1158 0.5736 0.0126  0.0144  -0.0434 412  LEU A C     
3321 O  O     . LEU A 411 ? 0.0698 0.111  0.5666 0.0129  0.0147  -0.042  412  LEU A O     
3322 C  CB    . LEU A 411 ? 0.0745 0.1204 0.5808 0.0098  0.0124  -0.0492 412  LEU A CB    
3323 C  CG    . LEU A 411 ? 0.0962 0.142  0.604  0.0094  0.013   -0.0487 412  LEU A CG    
3324 C  CD1   . LEU A 411 ? 0.1166 0.161  0.6169 0.0089  0.0122  -0.0488 412  LEU A CD1   
3325 C  CD2   . LEU A 411 ? 0.1037 0.1512 0.6183 0.0086  0.0127  -0.0509 412  LEU A CD2   
3326 N  N     . TRP A 412 ? 0.0624 0.1064 0.5687 0.0136  0.0155  -0.0419 413  TRP A N     
3327 C  CA    . TRP A 412 ? 0.0577 0.1012 0.5656 0.0154  0.0172  -0.0383 413  TRP A CA    
3328 C  C     . TRP A 412 ? 0.0574 0.0982 0.5566 0.0171  0.0176  -0.0362 413  TRP A C     
3329 O  O     . TRP A 412 ? 0.0663 0.1058 0.5636 0.0183  0.0185  -0.0339 413  TRP A O     
3330 C  CB    . TRP A 412 ? 0.0468 0.0924 0.563  0.0162  0.0183  -0.0369 413  TRP A CB    
3331 C  CG    . TRP A 412 ? 0.0459 0.0935 0.5712 0.0149  0.0182  -0.0381 413  TRP A CG    
3332 C  CD1   . TRP A 412 ? 0.0449 0.0942 0.5761 0.0135  0.0171  -0.0406 413  TRP A CD1   
3333 C  CD2   . TRP A 412 ? 0.046  0.0938 0.5751 0.015   0.0193  -0.0369 413  TRP A CD2   
3334 N  NE1   . TRP A 412 ? 0.047  0.0973 0.5854 0.0128  0.0174  -0.0411 413  TRP A NE1   
3335 C  CE2   . TRP A 412 ? 0.0489 0.0984 0.5863 0.0137  0.0188  -0.0388 413  TRP A CE2   
3336 C  CE3   . TRP A 412 ? 0.0515 0.0982 0.5777 0.0162  0.0205  -0.0344 413  TRP A CE3   
3337 C  CZ2   . TRP A 412 ? 0.0582 0.1084 0.6013 0.0135  0.0197  -0.0381 413  TRP A CZ2   
3338 C  CZ3   . TRP A 412 ? 0.0569 0.1045 0.5886 0.0159  0.0214  -0.0338 413  TRP A CZ3   
3339 C  CH2   . TRP A 412 ? 0.062  0.1114 0.602  0.0146  0.021   -0.0357 413  TRP A CH2   
3340 N  N     . LYS A 413 ? 0.0475 0.0846 0.5379 0.0159  0.0165  -0.037  414  LYS A N     
3341 C  CA    . LYS A 413 ? 0.0603 0.0968 0.5448 0.0188  0.0167  -0.0354 414  LYS A CA    
3342 C  C     . LYS A 413 ? 0.0728 0.107  0.5515 0.018   0.0157  -0.0359 414  LYS A C     
3343 O  O     . LYS A 413 ? 0.0746 0.1063 0.5483 0.0196  0.0162  -0.0337 414  LYS A O     
3344 C  CB    . LYS A 413 ? 0.0996 0.1356 0.5796 0.0186  0.0157  -0.0368 414  LYS A CB    
3345 C  CG    . LYS A 413 ? 0.1567 0.1896 0.6287 0.0208  0.0161  -0.0347 414  LYS A CG    
3346 C  CD    . LYS A 413 ? 0.2524 0.2846 0.7195 0.0202  0.015   -0.0364 414  LYS A CD    
3347 C  CE    . LYS A 413 ? 0.3106 0.3461 0.7834 0.0195  0.0149  -0.0377 414  LYS A CE    
3348 N  NZ    . LYS A 413 ? 0.3348 0.3722 0.8137 0.0211  0.0166  -0.0352 414  LYS A NZ    
3349 N  N     . SER A 414 ? 0.0678 0.1029 0.547  0.0158  0.0144  -0.0385 415  SER A N     
3350 C  CA    . SER A 414 ? 0.0797 0.1132 0.5545 0.0147  0.0134  -0.0389 415  SER A CA    
3351 C  C     . SER A 414 ? 0.067  0.1008 0.5451 0.0154  0.0145  -0.0369 415  SER A C     
3352 O  O     . SER A 414 ? 0.0587 0.09   0.5316 0.0161  0.0143  -0.0353 415  SER A O     
3353 C  CB    . SER A 414 ? 0.1196 0.155  0.5962 0.0124  0.0121  -0.0419 415  SER A CB    
3354 O  OG    . SER A 414 ? 0.1841 0.2181 0.6557 0.0114  0.0109  -0.0421 415  SER A OG    
3355 N  N     . PHE A 415 ? 0.0595 0.096  0.5461 0.0153  0.0157  -0.0369 416  PHE A N     
3356 C  CA    . PHE A 415 ? 0.0698 0.1068 0.5603 0.016   0.017   -0.0349 416  PHE A CA    
3357 C  C     . PHE A 415 ? 0.071  0.1064 0.5589 0.0186  0.0183  -0.0316 416  PHE A C     
3358 O  O     . PHE A 415 ? 0.0881 0.1223 0.5735 0.0193  0.0186  -0.03   416  PHE A O     
3359 C  CB    . PHE A 415 ? 0.0656 0.1057 0.5662 0.0154  0.018   -0.0354 416  PHE A CB    
3360 C  CG    . PHE A 415 ? 0.0783 0.12   0.5821 0.0132  0.017   -0.0385 416  PHE A CG    
3361 C  CD1   . PHE A 415 ? 0.0864 0.1273 0.585  0.0119  0.0156  -0.04   416  PHE A CD1   
3362 C  CD2   . PHE A 415 ? 0.0905 0.1345 0.6026 0.0126  0.0174  -0.0398 416  PHE A CD2   
3363 C  CE1   . PHE A 415 ? 0.0989 0.1414 0.6002 0.0102  0.0149  -0.0426 416  PHE A CE1   
3364 C  CE2   . PHE A 415 ? 0.1013 0.1466 0.6158 0.0109  0.0164  -0.0428 416  PHE A CE2   
3365 C  CZ    . PHE A 415 ? 0.0978 0.1424 0.6068 0.0099  0.0153  -0.0441 416  PHE A CZ    
3366 N  N     . VAL A 416 ? 0.0589 0.0945 0.5476 0.0202  0.0192  -0.0304 417  VAL A N     
3367 C  CA    . VAL A 416 ? 0.065  0.0994 0.5517 0.0231  0.0207  -0.027  417  VAL A CA    
3368 C  C     . VAL A 416 ? 0.069  0.0993 0.5449 0.0244  0.0197  -0.0264 417  VAL A C     
3369 O  O     . VAL A 416 ? 0.0733 0.1021 0.5461 0.0266  0.0206  -0.0238 417  VAL A O     
3370 C  CB    . VAL A 416 ? 0.0644 0.1005 0.5561 0.0246  0.022   -0.0256 417  VAL A CB    
3371 C  CG1   . VAL A 416 ? 0.077  0.112  0.566  0.028   0.0237  -0.0218 417  VAL A CG1   
3372 C  CG2   . VAL A 416 ? 0.0529 0.0927 0.5557 0.0235  0.0229  -0.0259 417  VAL A CG2   
3373 N  N     . SER A 417 ? 0.0652 0.0938 0.5353 0.023   0.0179  -0.0286 418  SER A N     
3374 C  CA    . SER A 417 ? 0.0668 0.0912 0.5267 0.0241  0.0167  -0.0281 418  SER A CA    
3375 C  C     . SER A 417 ? 0.0765 0.0989 0.5323 0.0233  0.0155  -0.0282 418  SER A C     
3376 O  O     . SER A 417 ? 0.0835 0.1023 0.5318 0.0249  0.0148  -0.0269 418  SER A O     
3377 C  CB    . SER A 417 ? 0.0804 0.1036 0.5357 0.0229  0.0152  -0.0303 418  SER A CB    
3378 O  OG    . SER A 417 ? 0.0985 0.1235 0.5571 0.0237  0.0163  -0.0301 418  SER A OG    
3379 N  N     . LEU A 418 ? 0.0638 0.0885 0.5241 0.0207  0.0149  -0.0298 419  LEU A N     
3380 C  CA    . LEU A 418 ? 0.0634 0.0866 0.5202 0.0196  0.0134  -0.0299 419  LEU A CA    
3381 C  C     . LEU A 418 ? 0.065  0.0901 0.527  0.0196  0.0146  -0.0285 419  LEU A C     
3382 O  O     . LEU A 418 ? 0.0676 0.0913 0.5262 0.0189  0.0134  -0.0282 419  LEU A O     
3383 C  CB    . LEU A 418 ? 0.06   0.0837 0.516  0.0166  0.0116  -0.0325 419  LEU A CB    
3384 C  CG    . LEU A 418 ? 0.0711 0.0924 0.5206 0.0165  0.0101  -0.0336 419  LEU A CG    
3385 C  CD1   . LEU A 418 ? 0.0681 0.091  0.5184 0.0139  0.0088  -0.0361 419  LEU A CD1   
3386 C  CD2   . LEU A 418 ? 0.0787 0.0953 0.5191 0.0176  0.0087  -0.0324 419  LEU A CD2   
3387 N  N     . SER A 419 ? 0.057  0.0851 0.527  0.0205  0.0167  -0.0275 420  SER A N     
3388 C  CA    . SER A 419 ? 0.067  0.0969 0.5421 0.0206  0.0179  -0.0262 420  SER A CA    
3389 C  C     . SER A 419 ? 0.0753 0.1041 0.5489 0.0236  0.0193  -0.023  420  SER A C     
3390 O  O     . SER A 419 ? 0.0645 0.0935 0.5391 0.0258  0.0207  -0.0215 420  SER A O     
3391 C  CB    . SER A 419 ? 0.0737 0.1075 0.559  0.0197  0.0193  -0.0269 420  SER A CB    
3392 O  OG    . SER A 419 ? 0.0963 0.1313 0.5835 0.0173  0.0182  -0.0299 420  SER A OG    
3393 N  N     . ASP A 420 ? 0.0886 0.1169 0.5606 0.0238  0.0191  -0.0218 421  ASP A N     
3394 C  CA    . ASP A 420 ? 0.1071 0.135  0.5786 0.0268  0.0207  -0.0187 421  ASP A CA    
3395 C  C     . ASP A 420 ? 0.1214 0.1534 0.6034 0.0273  0.0233  -0.0172 421  ASP A C     
3396 O  O     . ASP A 420 ? 0.1322 0.1648 0.6161 0.0302  0.0253  -0.0145 421  ASP A O     
3397 C  CB    . ASP A 420 ? 0.1163 0.1421 0.5819 0.0269  0.0193  -0.0179 421  ASP A CB    
3398 C  CG    . ASP A 420 ? 0.1646 0.1858 0.6198 0.0269  0.0168  -0.0188 421  ASP A CG    
3399 O  OD1   . ASP A 420 ? 0.1729 0.1934 0.626  0.0242  0.0147  -0.0211 421  ASP A OD1   
3400 O  OD2   . ASP A 420 ? 0.1891 0.2075 0.6382 0.0298  0.0169  -0.0172 421  ASP A OD2   
3401 N  N     . PHE A 421 ? 0.123  0.1576 0.6116 0.0247  0.0233  -0.0189 422  PHE A N     
3402 C  CA    . PHE A 421 ? 0.1227 0.161  0.6217 0.0247  0.0254  -0.018  422  PHE A CA    
3403 C  C     . PHE A 421 ? 0.1206 0.1606 0.6249 0.0222  0.0248  -0.0209 422  PHE A C     
3404 O  O     . PHE A 421 ? 0.1213 0.1607 0.6228 0.0199  0.0231  -0.0233 422  PHE A O     
3405 C  CB    . PHE A 421 ? 0.1247 0.1642 0.6261 0.0244  0.026   -0.0168 422  PHE A CB    
3406 C  CG    . PHE A 421 ? 0.1387 0.1761 0.6332 0.0264  0.0258  -0.0145 422  PHE A CG    
3407 C  CD1   . PHE A 421 ? 0.1515 0.1893 0.6469 0.0297  0.0278  -0.0113 422  PHE A CD1   
3408 C  CD2   . PHE A 421 ? 0.1495 0.1846 0.6365 0.0252  0.0235  -0.0155 422  PHE A CD2   
3409 C  CE1   . PHE A 421 ? 0.1637 0.1994 0.6522 0.0319  0.0275  -0.0094 422  PHE A CE1   
3410 C  CE2   . PHE A 421 ? 0.1629 0.1957 0.6433 0.0271  0.023   -0.0136 422  PHE A CE2   
3411 C  CZ    . PHE A 421 ? 0.1613 0.1943 0.6422 0.0305  0.025   -0.0107 422  PHE A CZ    
3412 N  N     . ILE A 422 ? 0.1254 0.1675 0.6373 0.0226  0.0262  -0.0206 423  ILE A N     
3413 C  CA    . ILE A 422 ? 0.1282 0.1719 0.6457 0.0204  0.0256  -0.0235 423  ILE A CA    
3414 C  C     . ILE A 422 ? 0.1209 0.1673 0.6484 0.0202  0.0272  -0.0228 423  ILE A C     
3415 O  O     . ILE A 422 ? 0.126  0.1737 0.6589 0.0219  0.029   -0.0202 423  ILE A O     
3416 C  CB    . ILE A 422 ? 0.1373 0.1809 0.6553 0.0207  0.0253  -0.0243 423  ILE A CB    
3417 C  CG1   . ILE A 422 ? 0.1478 0.1885 0.6558 0.021   0.0237  -0.025  423  ILE A CG1   
3418 C  CG2   . ILE A 422 ? 0.1448 0.1902 0.6692 0.0185  0.0246  -0.0273 423  ILE A CG2   
3419 C  CD1   . ILE A 422 ? 0.1584 0.1991 0.6664 0.0218  0.0238  -0.025  423  ILE A CD1   
3420 N  N     . VAL A 423 ? 0.1053 0.1526 0.6353 0.0181  0.0266  -0.0249 424  VAL A N     
3421 C  CA    . VAL A 423 ? 0.1049 0.1543 0.6439 0.0178  0.0279  -0.0246 424  VAL A CA    
3422 C  C     . VAL A 423 ? 0.0869 0.1372 0.6309 0.016   0.027   -0.0278 424  VAL A C     
3423 O  O     . VAL A 423 ? 0.0757 0.1252 0.6156 0.0144  0.0253  -0.0307 424  VAL A O     
3424 C  CB    . VAL A 423 ? 0.1295 0.1793 0.6676 0.0173  0.0283  -0.024  424  VAL A CB    
3425 C  CG1   . VAL A 423 ? 0.137  0.1889 0.6844 0.0169  0.0297  -0.0237 424  VAL A CG1   
3426 C  CG2   . VAL A 423 ? 0.1472 0.1961 0.6802 0.0192  0.029   -0.0208 424  VAL A CG2   
3427 N  N     . LEU A 424 ? 0.0799 0.1316 0.6325 0.0163  0.028   -0.0273 425  LEU A N     
3428 C  CA    . LEU A 424 ? 0.075  0.1273 0.6328 0.0147  0.0269  -0.0305 425  LEU A CA    
3429 C  C     . LEU A 424 ? 0.0616 0.1152 0.6277 0.0142  0.0279  -0.0305 425  LEU A C     
3430 O  O     . LEU A 424 ? 0.067  0.1217 0.6387 0.0155  0.0297  -0.0275 425  LEU A O     
3431 C  CB    . LEU A 424 ? 0.0765 0.1292 0.6381 0.0151  0.0266  -0.0303 425  LEU A CB    
3432 C  CG    . LEU A 424 ? 0.1081 0.1598 0.6633 0.0162  0.0263  -0.0292 425  LEU A CG    
3433 C  CD1   . LEU A 424 ? 0.1074 0.1603 0.6686 0.0168  0.0265  -0.0282 425  LEU A CD1   
3434 C  CD2   . LEU A 424 ? 0.125  0.1751 0.6714 0.015   0.0243  -0.0321 425  LEU A CD2   
3435 N  N     . ASP A 425 ? 0.045  0.0984 0.6122 0.0127  0.0267  -0.0338 426  ASP A N     
3436 C  CA    . ASP A 425 ? 0.0448 0.0991 0.6202 0.0122  0.0274  -0.0344 426  ASP A CA    
3437 C  C     . ASP A 425 ? 0.0508 0.1046 0.6278 0.0109  0.0255  -0.0385 426  ASP A C     
3438 O  O     . ASP A 425 ? 0.0627 0.116  0.6364 0.0099  0.0244  -0.0413 426  ASP A O     
3439 C  CB    . ASP A 425 ? 0.0447 0.0992 0.6183 0.012   0.0281  -0.0343 426  ASP A CB    
3440 C  CG    . ASP A 425 ? 0.0503 0.1056 0.6324 0.0118  0.0291  -0.0346 426  ASP A CG    
3441 O  OD1   . ASP A 425 ? 0.0577 0.113  0.6471 0.0116  0.0289  -0.0354 426  ASP A OD1   
3442 O  OD2   . ASP A 425 ? 0.0448 0.1005 0.6263 0.0118  0.03    -0.034  426  ASP A OD2   
3443 N  N     . CYS A 426 ? 0.044  0.098  0.6258 0.0109  0.0249  -0.0386 427  CYS A N     
3444 C  CA    . CYS A 426 ? 0.0456 0.0991 0.6282 0.0098  0.0228  -0.0423 427  CYS A CA    
3445 C  C     . CYS A 426 ? 0.0464 0.1001 0.6388 0.0093  0.0223  -0.0435 427  CYS A C     
3446 O  O     . CYS A 426 ? 0.0434 0.0978 0.6424 0.0099  0.0231  -0.0409 427  CYS A O     
3447 C  CB    . CYS A 426 ? 0.0435 0.0968 0.6215 0.0101  0.022   -0.042  427  CYS A CB    
3448 S  SG    . CYS A 426 ? 0.114  0.1664 0.6797 0.0104  0.0219  -0.0414 427  CYS A SG    
3449 N  N     . PRO A 427 ? 0.0464 0.0991 0.639  0.0082  0.0204  -0.0477 428  PRO A N     
3450 C  CA    . PRO A 427 ? 0.0515 0.1039 0.6525 0.0076  0.0191  -0.0495 428  PRO A CA    
3451 C  C     . PRO A 427 ? 0.0668 0.1198 0.6687 0.0075  0.0181  -0.0488 428  PRO A C     
3452 O  O     . PRO A 427 ? 0.0627 0.1158 0.6571 0.0077  0.0176  -0.049  428  PRO A O     
3453 C  CB    . PRO A 427 ? 0.0565 0.1077 0.6547 0.0068  0.0171  -0.0544 428  PRO A CB    
3454 C  CG    . PRO A 427 ? 0.0597 0.1109 0.6499 0.0071  0.018   -0.0544 428  PRO A CG    
3455 C  CD    . PRO A 427 ? 0.0425 0.0945 0.6276 0.0077  0.0192  -0.051  428  PRO A CD    
3456 N  N     . ILE A 428 ? 0.068  0.1215 0.6792 0.0074  0.0179  -0.0476 429  ILE A N     
3457 C  CA    . ILE A 428 ? 0.0835 0.1378 0.6967 0.0073  0.0169  -0.0468 429  ILE A CA    
3458 C  C     . ILE A 428 ? 0.0869 0.1403 0.7049 0.0059  0.0141  -0.0508 429  ILE A C     
3459 O  O     . ILE A 428 ? 0.0823 0.1349 0.7079 0.0055  0.0137  -0.0517 429  ILE A O     
3460 C  CB    . ILE A 428 ? 0.0933 0.1492 0.7142 0.0082  0.0187  -0.0418 429  ILE A CB    
3461 C  CG1   . ILE A 428 ? 0.1055 0.1621 0.7222 0.0098  0.0216  -0.0378 429  ILE A CG1   
3462 C  CG2   . ILE A 428 ? 0.1026 0.1595 0.7259 0.0081  0.0176  -0.0408 429  ILE A CG2   
3463 C  CD1   . ILE A 428 ? 0.1169 0.1733 0.7229 0.0105  0.0218  -0.0376 429  ILE A CD1   
3464 N  N     . ILE A 429 ? 0.0828 0.136  0.6963 0.0054  0.0121  -0.0534 430  ILE A N     
3465 C  CA    . ILE A 429 ? 0.086  0.1382 0.7032 0.0043  0.0091  -0.0575 430  ILE A CA    
3466 C  C     . ILE A 429 ? 0.0864 0.1392 0.7152 0.0037  0.0084  -0.0557 430  ILE A C     
3467 O  O     . ILE A 429 ? 0.0874 0.1419 0.7189 0.0041  0.0092  -0.0521 430  ILE A O     
3468 C  CB    . ILE A 429 ? 0.0851 0.1376 0.6947 0.004   0.0074  -0.06   430  ILE A CB    
3469 C  CG1   . ILE A 429 ? 0.0871 0.1391 0.6863 0.0045  0.008   -0.0617 430  ILE A CG1   
3470 C  CG2   . ILE A 429 ? 0.0809 0.1326 0.6942 0.003   0.0041  -0.0641 430  ILE A CG2   
3471 C  CD1   . ILE A 429 ? 0.1014 0.1538 0.6929 0.0046  0.0072  -0.0627 430  ILE A CD1   
3472 N  N     . GLY A 430 ? 0.0813 0.1326 0.7169 0.003   0.0071  -0.058  431  GLY A N     
3473 C  CA    . GLY A 430 ? 0.0924 0.144  0.7397 0.0023  0.0062  -0.0563 431  GLY A CA    
3474 C  C     . GLY A 430 ? 0.102  0.1539 0.7564 0.0028  0.0086  -0.0528 431  GLY A C     
3475 O  O     . GLY A 430 ? 0.1091 0.1611 0.774  0.0022  0.008   -0.0512 431  GLY A O     
3476 N  N     . GLU A 431 ? 0.0934 0.1455 0.7425 0.0039  0.0113  -0.0513 432  GLU A N     
3477 C  CA    . GLU A 431 ? 0.0928 0.1453 0.7477 0.0046  0.0138  -0.0479 432  GLU A CA    
3478 C  C     . GLU A 431 ? 0.1052 0.156  0.7564 0.0047  0.0142  -0.0506 432  GLU A C     
3479 O  O     . GLU A 431 ? 0.1186 0.1686 0.7605 0.0048  0.0137  -0.0536 432  GLU A O     
3480 C  CB    . GLU A 431 ? 0.1122 0.1671 0.7646 0.0061  0.0168  -0.0426 432  GLU A CB    
3481 C  CG    . GLU A 431 ? 0.1622 0.219  0.8177 0.0063  0.0167  -0.0395 432  GLU A CG    
3482 C  CD    . GLU A 431 ? 0.2451 0.3041 0.9001 0.0082  0.0198  -0.0337 432  GLU A CD    
3483 O  OE1   . GLU A 431 ? 0.2871 0.3462 0.9385 0.0093  0.0221  -0.0323 432  GLU A OE1   
3484 O  OE2   . GLU A 431 ? 0.2841 0.3448 0.9423 0.0088  0.0201  -0.0306 432  GLU A OE2   
3485 N  N     . SER A 432 ? 0.0959 0.1462 0.7546 0.0049  0.0154  -0.0493 433  SER A N     
3486 C  CA    . SER A 432 ? 0.0863 0.135  0.7424 0.0051  0.0159  -0.0516 433  SER A CA    
3487 C  C     . SER A 432 ? 0.0683 0.1181 0.7171 0.0062  0.0188  -0.0494 433  SER A C     
3488 O  O     . SER A 432 ? 0.0743 0.1229 0.7178 0.0064  0.0188  -0.052  433  SER A O     
3489 C  CB    . SER A 432 ? 0.1165 0.1639 0.7831 0.0048  0.0159  -0.0514 433  SER A CB    
3490 O  OG    . SER A 432 ? 0.1571 0.2031 0.8308 0.0036  0.0129  -0.0537 433  SER A OG    
3491 N  N     . TYR A 433 ? 0.0479 0.1    0.6964 0.0072  0.0212  -0.0446 434  TYR A N     
3492 C  CA    . TYR A 433 ? 0.0462 0.0992 0.6882 0.0083  0.0237  -0.0424 434  TYR A CA    
3493 C  C     . TYR A 433 ? 0.0471 0.1014 0.6808 0.0089  0.0244  -0.0405 434  TYR A C     
3494 O  O     . TYR A 433 ? 0.0429 0.0978 0.6774 0.0089  0.0236  -0.0396 434  TYR A O     
3495 C  CB    . TYR A 433 ? 0.0432 0.0974 0.6925 0.0092  0.0264  -0.0384 434  TYR A CB    
3496 C  CG    . TYR A 433 ? 0.0493 0.1019 0.7059 0.0085  0.0258  -0.0405 434  TYR A CG    
3497 C  CD1   . TYR A 433 ? 0.0683 0.1193 0.7204 0.0084  0.0254  -0.0438 434  TYR A CD1   
3498 C  CD2   . TYR A 433 ? 0.062  0.1143 0.7296 0.0081  0.0251  -0.0396 434  TYR A CD2   
3499 C  CE1   . TYR A 433 ? 0.0788 0.1278 0.7371 0.008   0.0247  -0.0461 434  TYR A CE1   
3500 C  CE2   . TYR A 433 ? 0.0734 0.1237 0.7475 0.0075  0.0242  -0.042  434  TYR A CE2   
3501 C  CZ    . TYR A 433 ? 0.0879 0.1365 0.7571 0.0075  0.0241  -0.0452 434  TYR A CZ    
3502 O  OH    . TYR A 433 ? 0.1261 0.1723 0.8012 0.0071  0.0232  -0.0476 434  TYR A OH    
3503 N  N     . ASN A 434 ? 0.052  0.1065 0.6776 0.0096  0.0257  -0.0399 435  ASN A N     
3504 C  CA    . ASN A 434 ? 0.0489 0.104  0.6659 0.0102  0.026   -0.0384 435  ASN A CA    
3505 C  C     . ASN A 434 ? 0.0587 0.1155 0.6782 0.0116  0.028   -0.0334 435  ASN A C     
3506 O  O     . ASN A 434 ? 0.0595 0.1174 0.687  0.0124  0.0297  -0.0304 435  ASN A O     
3507 C  CB    . ASN A 434 ? 0.0505 0.1054 0.659  0.0104  0.0267  -0.0387 435  ASN A CB    
3508 C  CG    . ASN A 434 ? 0.0795 0.1331 0.6825 0.0093  0.0248  -0.0432 435  ASN A CG    
3509 O  OD1   . ASN A 434 ? 0.0941 0.1468 0.7007 0.0085  0.0231  -0.0465 435  ASN A OD1   
3510 N  ND2   . ASN A 434 ? 0.0803 0.1339 0.6747 0.0094  0.025   -0.0434 435  ASN A ND2   
3511 N  N     . GLU A 435 ? 0.0587 0.1156 0.6713 0.0123  0.0279  -0.0324 436  GLU A N     
3512 C  CA    . GLU A 435 ? 0.061  0.1193 0.673  0.0141  0.0297  -0.0278 436  GLU A CA    
3513 C  C     . GLU A 435 ? 0.0685 0.1263 0.6708 0.0149  0.0307  -0.0268 436  GLU A C     
3514 O  O     . GLU A 435 ? 0.0839 0.1404 0.6785 0.014   0.0292  -0.0298 436  GLU A O     
3515 C  CB    . GLU A 435 ? 0.0822 0.1406 0.6924 0.0143  0.0287  -0.0275 436  GLU A CB    
3516 C  CG    . GLU A 435 ? 0.1373 0.1969 0.7578 0.0143  0.0285  -0.026  436  GLU A CG    
3517 C  CD    . GLU A 435 ? 0.1651 0.2265 0.7952 0.0154  0.0307  -0.0219 436  GLU A CD    
3518 O  OE1   . GLU A 435 ? 0.1963 0.2588 0.8246 0.0174  0.033   -0.0179 436  GLU A OE1   
3519 O  OE2   . GLU A 435 ? 0.1518 0.2133 0.7913 0.0143  0.03    -0.0227 436  GLU A OE2   
3520 N  N     . PHE A 436 ? 0.0564 0.1153 0.6592 0.0167  0.0329  -0.0227 437  PHE A N     
3521 C  CA    . PHE A 436 ? 0.0549 0.1133 0.6486 0.0177  0.0336  -0.0215 437  PHE A CA    
3522 C  C     . PHE A 436 ? 0.0547 0.1132 0.6445 0.0197  0.0344  -0.0184 437  PHE A C     
3523 O  O     . PHE A 436 ? 0.0494 0.1095 0.6455 0.0212  0.0359  -0.015  437  PHE A O     
3524 C  CB    . PHE A 436 ? 0.048  0.1073 0.6441 0.0184  0.0356  -0.0194 437  PHE A CB    
3525 C  CG    . PHE A 436 ? 0.0536 0.1125 0.641  0.0197  0.0363  -0.0173 437  PHE A CG    
3526 C  CD1   . PHE A 436 ? 0.0658 0.1231 0.644  0.0186  0.0347  -0.0197 437  PHE A CD1   
3527 C  CD2   . PHE A 436 ? 0.0596 0.1196 0.6475 0.0222  0.0383  -0.013  437  PHE A CD2   
3528 C  CE1   . PHE A 436 ? 0.0771 0.1337 0.6471 0.0197  0.0349  -0.0179 437  PHE A CE1   
3529 C  CE2   . PHE A 436 ? 0.0795 0.1387 0.6589 0.0235  0.0386  -0.0114 437  PHE A CE2   
3530 C  CZ    . PHE A 436 ? 0.0795 0.1369 0.65   0.0222  0.0368  -0.0139 437  PHE A CZ    
3531 N  N     . ARG A 437 ? 0.0565 0.1135 0.636  0.0198  0.0334  -0.0192 438  ARG A N     
3532 C  CA    . ARG A 437 ? 0.0571 0.1137 0.6313 0.022   0.0341  -0.0164 438  ARG A CA    
3533 C  C     . ARG A 437 ? 0.0768 0.1318 0.6411 0.0226  0.0339  -0.0161 438  ARG A C     
3534 O  O     . ARG A 437 ? 0.0782 0.1319 0.6375 0.0208  0.0324  -0.019  438  ARG A O     
3535 C  CB    . ARG A 437 ? 0.066  0.1218 0.6375 0.0216  0.0326  -0.0179 438  ARG A CB    
3536 C  CG    . ARG A 437 ? 0.0829 0.1403 0.664  0.0213  0.0326  -0.0176 438  ARG A CG    
3537 C  CD    . ARG A 437 ? 0.0998 0.1593 0.6881 0.0236  0.035   -0.0128 438  ARG A CD    
3538 N  NE    . ARG A 437 ? 0.1346 0.1956 0.7319 0.0231  0.0347  -0.0124 438  ARG A NE    
3539 C  CZ    . ARG A 437 ? 0.141  0.203  0.7482 0.0216  0.0343  -0.0134 438  ARG A CZ    
3540 N  NH1   . ARG A 437 ? 0.1042 0.1659 0.7135 0.0207  0.0346  -0.0146 438  ARG A NH1   
3541 N  NH2   . ARG A 437 ? 0.1416 0.2048 0.7566 0.021   0.0337  -0.013  438  ARG A NH2   
3542 N  N     . LEU A 438 ? 0.0843 0.1393 0.6456 0.0252  0.0354  -0.0125 439  LEU A N     
3543 C  CA    . LEU A 438 ? 0.0994 0.1524 0.6507 0.0261  0.035   -0.0119 439  LEU A CA    
3544 C  C     . LEU A 438 ? 0.1134 0.1653 0.6594 0.0285  0.0352  -0.0099 439  LEU A C     
3545 O  O     . LEU A 438 ? 0.1089 0.1621 0.6581 0.0312  0.0373  -0.0062 439  LEU A O     
3546 C  CB    . LEU A 438 ? 0.1035 0.1574 0.6555 0.0273  0.0366  -0.0094 439  LEU A CB    
3547 C  CG    . LEU A 438 ? 0.1479 0.1997 0.6894 0.0288  0.0361  -0.0082 439  LEU A CG    
3548 C  CD1   . LEU A 438 ? 0.1603 0.2095 0.6932 0.0266  0.0334  -0.0116 439  LEU A CD1   
3549 C  CD2   . LEU A 438 ? 0.1657 0.2187 0.7085 0.0295  0.0373  -0.0062 439  LEU A CD2   
3550 N  N     . ILE A 439 ? 0.1163 0.1659 0.6545 0.0276  0.0333  -0.0123 440  ILE A N     
3551 C  CA    . ILE A 439 ? 0.1209 0.1689 0.6531 0.0297  0.0333  -0.0109 440  ILE A CA    
3552 C  C     . ILE A 439 ? 0.1185 0.1636 0.6399 0.031   0.0325  -0.0104 440  ILE A C     
3553 O  O     . ILE A 439 ? 0.1091 0.1524 0.6249 0.029   0.0306  -0.013  440  ILE A O     
3554 C  CB    . ILE A 439 ? 0.134  0.1812 0.6647 0.0279  0.0315  -0.014  440  ILE A CB    
3555 C  CG1   . ILE A 439 ? 0.1488 0.1986 0.6899 0.026   0.0315  -0.0155 440  ILE A CG1   
3556 C  CG2   . ILE A 439 ? 0.1393 0.185  0.6644 0.0303  0.0317  -0.0124 440  ILE A CG2   
3557 C  CD1   . ILE A 439 ? 0.1814 0.2334 0.7308 0.0278  0.0333  -0.0124 440  ILE A CD1   
3558 N  N     . ILE A 440 ? 0.1229 0.1676 0.6415 0.0345  0.034   -0.0068 441  ILE A N     
3559 C  CA    . ILE A 440 ? 0.1285 0.1699 0.6363 0.0361  0.0331  -0.0063 441  ILE A CA    
3560 C  C     . ILE A 440 ? 0.1299 0.1688 0.6308 0.0368  0.0321  -0.0071 441  ILE A C     
3561 O  O     . ILE A 440 ? 0.1392 0.1783 0.6401 0.0397  0.0335  -0.0045 441  ILE A O     
3562 C  CB    . ILE A 440 ? 0.1337 0.1757 0.6412 0.0397  0.0352  -0.0022 441  ILE A CB    
3563 C  CG1   . ILE A 440 ? 0.1418 0.187  0.6578 0.0389  0.0367  -0.0012 441  ILE A CG1   
3564 C  CG2   . ILE A 440 ? 0.1403 0.1784 0.636  0.0412  0.0338  -0.0021 441  ILE A CG2   
3565 C  CD1   . ILE A 440 ? 0.161  0.2055 0.675  0.0361  0.035   -0.0036 441  ILE A CD1   
3566 N  N     . ASN A 441 ? 0.1207 0.1574 0.6163 0.0343  0.0296  -0.0105 442  ASN A N     
3567 C  CA    . ASN A 441 ? 0.122  0.1564 0.6116 0.0345  0.0285  -0.0116 442  ASN A CA    
3568 C  C     . ASN A 441 ? 0.1383 0.1683 0.6159 0.036   0.027   -0.0116 442  ASN A C     
3569 O  O     . ASN A 441 ? 0.1391 0.1668 0.6111 0.0358  0.0257  -0.013  442  ASN A O     
3570 C  CB    . ASN A 441 ? 0.117  0.1521 0.6088 0.0308  0.0267  -0.0155 442  ASN A CB    
3571 C  CG    . ASN A 441 ? 0.1298 0.1639 0.6189 0.0307  0.026   -0.0167 442  ASN A CG    
3572 O  OD1   . ASN A 441 ? 0.1222 0.1579 0.6154 0.0322  0.0274  -0.0151 442  ASN A OD1   
3573 N  ND2   . ASN A 441 ? 0.1408 0.1725 0.6229 0.029   0.0238  -0.0193 442  ASN A ND2   
3574 N  N     . LYS A 442 ? 0.1554 0.1841 0.6291 0.0375  0.027   -0.0101 443  LYS A N     
3575 C  CA    . LYS A 442 ? 0.1783 0.2023 0.6405 0.0387  0.0252  -0.0102 443  LYS A CA    
3576 C  C     . LYS A 442 ? 0.184  0.2051 0.6394 0.0417  0.0254  -0.0092 443  LYS A C     
3577 O  O     . LYS A 442 ? 0.1911 0.2087 0.6388 0.0409  0.0232  -0.0112 443  LYS A O     
3578 C  CB    . LYS A 442 ? 0.2279 0.2512 0.6877 0.0404  0.0255  -0.0082 443  LYS A CB    
3579 C  CG    . LYS A 442 ? 0.3237 0.3476 0.7846 0.0372  0.0239  -0.0099 443  LYS A CG    
3580 C  CD    . LYS A 442 ? 0.423  0.4442 0.8768 0.0388  0.0228  -0.0086 443  LYS A CD    
3581 C  CE    . LYS A 442 ? 0.5041 0.5232 0.9533 0.0356  0.0197  -0.0109 443  LYS A CE    
3582 N  NZ    . LYS A 442 ? 0.5558 0.5704 0.996  0.035   0.017   -0.0129 443  LYS A NZ    
3583 N  N     . ASN A 443 ? 0.1818 0.2044 0.6398 0.0453  0.0279  -0.0059 444  ASN A N     
3584 C  CA    . ASN A 443 ? 0.1973 0.2174 0.649  0.0487  0.0285  -0.0044 444  ASN A CA    
3585 C  C     . ASN A 443 ? 0.1911 0.2112 0.6433 0.0469  0.0278  -0.0064 444  ASN A C     
3586 O  O     . ASN A 443 ? 0.2109 0.2273 0.6545 0.048   0.0267  -0.007  444  ASN A O     
3587 C  CB    . ASN A 443 ? 0.2272 0.2499 0.6834 0.0528  0.0317  -0.0001 444  ASN A CB    
3588 C  CG    . ASN A 443 ? 0.2938 0.315  0.7453 0.056   0.0323  0.0022  444  ASN A CG    
3589 O  OD1   . ASN A 443 ? 0.3306 0.3477 0.7729 0.056   0.03    0.0008  444  ASN A OD1   
3590 N  ND2   . ASN A 443 ? 0.3034 0.3281 0.7613 0.0588  0.0351  0.0058  444  ASN A ND2   
3591 N  N     . ASN A 444 ? 0.1588 0.183  0.6208 0.0442  0.0284  -0.0074 445  ASN A N     
3592 C  CA    . ASN A 444 ? 0.1367 0.1616 0.6004 0.0424  0.0278  -0.0093 445  ASN A CA    
3593 C  C     . ASN A 444 ? 0.1381 0.1599 0.5949 0.0396  0.0249  -0.013  445  ASN A C     
3594 O  O     . ASN A 444 ? 0.1478 0.1673 0.5989 0.04    0.0241  -0.0138 445  ASN A O     
3595 C  CB    . ASN A 444 ? 0.1287 0.1584 0.6045 0.0401  0.0287  -0.0098 445  ASN A CB    
3596 C  CG    . ASN A 444 ? 0.1618 0.1927 0.6403 0.0388  0.0284  -0.0112 445  ASN A CG    
3597 O  OD1   . ASN A 444 ? 0.1897 0.2191 0.6633 0.0407  0.0286  -0.0103 445  ASN A OD1   
3598 N  ND2   . ASN A 444 ? 0.1566 0.1905 0.6433 0.0358  0.028   -0.0132 445  ASN A ND2   
3599 N  N     . LYS A 445 ? 0.126  0.1476 0.5827 0.037   0.0233  -0.0149 446  LYS A N     
3600 C  CA    . LYS A 445 ? 0.1234 0.1421 0.5738 0.0343  0.0205  -0.018  446  LYS A CA    
3601 C  C     . LYS A 445 ? 0.1334 0.1469 0.5723 0.0365  0.0193  -0.0175 446  LYS A C     
3602 O  O     . LYS A 445 ? 0.1208 0.1321 0.5547 0.0358  0.0179  -0.0191 446  LYS A O     
3603 C  CB    . LYS A 445 ? 0.1186 0.1382 0.5711 0.0317  0.0194  -0.0192 446  LYS A CB    
3604 C  CG    . LYS A 445 ? 0.1266 0.1429 0.5716 0.0295  0.0164  -0.0215 446  LYS A CG    
3605 C  CD    . LYS A 445 ? 0.1478 0.1655 0.5957 0.0268  0.0154  -0.0224 446  LYS A CD    
3606 C  CE    . LYS A 445 ? 0.1294 0.1443 0.5707 0.0246  0.0125  -0.0243 446  LYS A CE    
3607 N  NZ    . LYS A 445 ? 0.1051 0.1219 0.5498 0.022   0.0116  -0.0249 446  LYS A NZ    
3608 N  N     . GLU A 446 ? 0.1579 0.1696 0.5929 0.0395  0.0199  -0.0151 447  GLU A N     
3609 C  CA    . GLU A 446 ? 0.1986 0.2048 0.6222 0.042   0.0186  -0.0146 447  GLU A CA    
3610 C  C     . GLU A 446 ? 0.2065 0.2112 0.6265 0.0443  0.0194  -0.014  447  GLU A C     
3611 O  O     . GLU A 446 ? 0.2189 0.2194 0.6305 0.0443  0.0175  -0.0153 447  GLU A O     
3612 C  CB    . GLU A 446 ? 0.2584 0.2632 0.6789 0.0453  0.0194  -0.012  447  GLU A CB    
3613 C  CG    . GLU A 446 ? 0.3648 0.3689 0.7843 0.0433  0.0175  -0.0129 447  GLU A CG    
3614 C  CD    . GLU A 446 ? 0.5344 0.5379 0.952  0.0466  0.0185  -0.0102 447  GLU A CD    
3615 O  OE1   . GLU A 446 ? 0.5765 0.5803 0.9936 0.0507  0.0208  -0.0075 447  GLU A OE1   
3616 O  OE2   . GLU A 446 ? 0.5876 0.5907 1.0045 0.0451  0.017   -0.0107 447  GLU A OE2   
3617 N  N     . SER A 447 ? 0.198  0.2064 0.6249 0.046   0.0222  -0.0119 448  SER A N     
3618 C  CA    . SER A 447 ? 0.202  0.2099 0.6267 0.0481  0.0232  -0.011  448  SER A CA    
3619 C  C     . SER A 447 ? 0.1774 0.1851 0.6016 0.0448  0.0215  -0.0141 448  SER A C     
3620 O  O     . SER A 447 ? 0.1752 0.1797 0.5924 0.046   0.0209  -0.0144 448  SER A O     
3621 C  CB    . SER A 447 ? 0.2413 0.2539 0.6751 0.0499  0.0263  -0.0081 448  SER A CB    
3622 O  OG    . SER A 447 ? 0.3079 0.3199 0.7397 0.0543  0.0282  -0.0045 448  SER A OG    
3623 N  N     . ILE A 448 ? 0.156  0.1669 0.5874 0.0409  0.0208  -0.0164 449  ILE A N     
3624 C  CA    . ILE A 448 ? 0.1465 0.1579 0.5781 0.0379  0.0193  -0.0193 449  ILE A CA    
3625 C  C     . ILE A 448 ? 0.1532 0.1599 0.5754 0.0367  0.0166  -0.0213 449  ILE A C     
3626 O  O     . ILE A 448 ? 0.1516 0.1565 0.5694 0.0363  0.0156  -0.0226 449  ILE A O     
3627 C  CB    . ILE A 448 ? 0.1391 0.1552 0.5809 0.0344  0.0194  -0.021  449  ILE A CB    
3628 C  CG1   . ILE A 448 ? 0.1323 0.1529 0.5837 0.0355  0.0219  -0.0191 449  ILE A CG1   
3629 C  CG2   . ILE A 448 ? 0.1444 0.1607 0.5854 0.0313  0.0175  -0.0243 449  ILE A CG2   
3630 C  CD1   . ILE A 448 ? 0.137  0.1617 0.5985 0.0329  0.0221  -0.0202 449  ILE A CD1   
3631 N  N     . LEU A 449 ? 0.1579 0.1623 0.5766 0.0363  0.0152  -0.0214 450  LEU A N     
3632 C  CA    . LEU A 449 ? 0.1677 0.1676 0.578  0.035   0.0123  -0.0232 450  LEU A CA    
3633 C  C     . LEU A 449 ? 0.1886 0.183  0.5884 0.0381  0.0117  -0.0223 450  LEU A C     
3634 O  O     . LEU A 449 ? 0.1735 0.1641 0.5666 0.0369  0.0093  -0.0239 450  LEU A O     
3635 C  CB    . LEU A 449 ? 0.1603 0.1597 0.5706 0.0333  0.0108  -0.0235 450  LEU A CB    
3636 C  CG    . LEU A 449 ? 0.1525 0.1569 0.5723 0.0301  0.0112  -0.0246 450  LEU A CG    
3637 C  CD1   . LEU A 449 ? 0.1619 0.1658 0.5813 0.0289  0.0099  -0.0245 450  LEU A CD1   
3638 C  CD2   . LEU A 449 ? 0.1429 0.1489 0.5647 0.0269  0.01    -0.0273 450  LEU A CD2   
3639 N  N     . ARG A 450 ? 0.2213 0.2154 0.6201 0.0422  0.014   -0.0196 451  ARG A N     
3640 C  CA    . ARG A 450 ? 0.2599 0.2489 0.6488 0.0457  0.0138  -0.0186 451  ARG A CA    
3641 C  C     . ARG A 450 ? 0.2817 0.2721 0.6717 0.0465  0.0153  -0.0184 451  ARG A C     
3642 O  O     . ARG A 450 ? 0.2931 0.2793 0.6749 0.0488  0.0149  -0.0181 451  ARG A O     
3643 C  CB    . ARG A 450 ? 0.2925 0.28   0.6784 0.0504  0.0156  -0.0155 451  ARG A CB    
3644 C  CG    . ARG A 450 ? 0.3821 0.3688 0.7673 0.0504  0.0146  -0.0151 451  ARG A CG    
3645 C  CD    . ARG A 450 ? 0.4623 0.4473 0.8435 0.0555  0.0164  -0.012  451  ARG A CD    
3646 N  NE    . ARG A 450 ? 0.5075 0.4969 0.8954 0.0582  0.02    -0.0091 451  ARG A NE    
3647 C  CZ    . ARG A 450 ? 0.5382 0.5325 0.9349 0.0587  0.0222  -0.007  451  ARG A CZ    
3648 N  NH1   . ARG A 450 ? 0.5168 0.5124 0.9167 0.0566  0.0213  -0.0077 451  ARG A NH1   
3649 N  NH2   . ARG A 450 ? 0.5359 0.5339 0.9385 0.0611  0.0254  -0.0042 451  ARG A NH2   
3650 N  N     . LYS A 451 ? 0.289  0.285  0.6888 0.0449  0.0169  -0.0184 452  LYS A N     
3651 C  CA    . LYS A 451 ? 0.3127 0.3108 0.7149 0.0455  0.0183  -0.018  452  LYS A CA    
3652 C  C     . LYS A 451 ? 0.3286 0.3248 0.7263 0.0434  0.0165  -0.0206 452  LYS A C     
3653 O  O     . LYS A 451 ? 0.3359 0.3325 0.7348 0.0397  0.0144  -0.0233 452  LYS A O     
3654 C  CB    . LYS A 451 ? 0.346  0.3506 0.7603 0.0439  0.0201  -0.0176 452  LYS A CB    
3655 C  CG    . LYS A 451 ? 0.4162 0.4233 0.8345 0.0474  0.023   -0.014  452  LYS A CG    
3656 C  CD    . LYS A 451 ? 0.4861 0.4979 0.9149 0.0468  0.0245  -0.0127 452  LYS A CD    
3657 C  CE    . LYS A 451 ? 0.5533 0.5675 0.9862 0.0506  0.0275  -0.0085 452  LYS A CE    
3658 N  NZ    . LYS A 451 ? 0.5861 0.6041 1.0282 0.0502  0.0288  -0.0071 452  LYS A NZ    
3659 N  N     . THR A 452 ? 0.3274 0.3217 0.7203 0.0459  0.0173  -0.0194 453  THR A N     
3660 C  CA    . THR A 452 ? 0.3359 0.3286 0.7246 0.0446  0.0161  -0.0213 453  THR A CA    
3661 C  C     . THR A 452 ? 0.3292 0.3247 0.7208 0.0466  0.0184  -0.0196 453  THR A C     
3662 O  O     . THR A 452 ? 0.3316 0.3274 0.7232 0.0503  0.0206  -0.0164 453  THR A O     
3663 C  CB    . THR A 452 ? 0.3635 0.349  0.74   0.0462  0.0142  -0.0217 453  THR A CB    
3664 O  OG1   . THR A 452 ? 0.3751 0.3577 0.7461 0.0511  0.0159  -0.0189 453  THR A OG1   
3665 C  CG2   . THR A 452 ? 0.3741 0.3566 0.7474 0.0441  0.0115  -0.0235 453  THR A CG2   
3666 N  N     . SER A 453 ? 0.3186 0.3162 0.7125 0.0443  0.018   -0.0213 454  SER A N     
3667 C  CA    . SER A 453 ? 0.3173 0.3174 0.7134 0.0461  0.02    -0.0196 454  SER A CA    
3668 C  C     . SER A 453 ? 0.3314 0.3262 0.7168 0.0499  0.0203  -0.018  454  SER A C     
3669 O  O     . SER A 453 ? 0.3356 0.3247 0.712  0.0503  0.0186  -0.0191 454  SER A O     
3670 C  CB    . SER A 453 ? 0.3166 0.3205 0.7178 0.0428  0.0193  -0.0219 454  SER A CB    
3671 O  OG    . SER A 453 ? 0.3369 0.3375 0.7313 0.0412  0.0172  -0.0244 454  SER A OG    
3672 N  N     . LYS A 454 ? 0.3287 0.3253 0.7151 0.0527  0.0226  -0.0154 455  LYS A N     
3673 C  CA    . LYS A 454 ? 0.3346 0.3269 0.7119 0.0567  0.0236  -0.0134 455  LYS A CA    
3674 C  C     . LYS A 454 ? 0.3333 0.3202 0.7012 0.0557  0.0213  -0.016  455  LYS A C     
3675 O  O     . LYS A 454 ? 0.3261 0.3148 0.6963 0.0523  0.02    -0.0185 455  LYS A O     
3676 C  CB    . LYS A 454 ? 0.3675 0.3642 0.7498 0.0581  0.026   -0.0111 455  LYS A CB    
3677 C  CG    . LYS A 454 ? 0.4517 0.4449 0.8255 0.0624  0.0273  -0.0087 455  LYS A CG    
3678 C  CD    . LYS A 454 ? 0.5274 0.5255 0.9068 0.0632  0.0295  -0.0066 455  LYS A CD    
3679 C  CE    . LYS A 454 ? 0.5908 0.5852 0.9612 0.0674  0.0308  -0.0044 455  LYS A CE    
3680 N  NZ    . LYS A 454 ? 0.6197 0.6191 0.9956 0.0682  0.0329  -0.002  455  LYS A NZ    
3681 N  N     . GLN A 455 ? 0.3362 0.3164 0.6935 0.0587  0.0207  -0.0153 456  GLN A N     
3682 C  CA    . GLN A 455 ? 0.3512 0.3258 0.6994 0.058   0.0183  -0.0176 456  GLN A CA    
3683 C  C     . GLN A 455 ? 0.3456 0.3206 0.6916 0.0594  0.0197  -0.0167 456  GLN A C     
3684 O  O     . GLN A 455 ? 0.3447 0.32   0.6895 0.0635  0.0222  -0.0136 456  GLN A O     
3685 C  CB    . GLN A 455 ? 0.392  0.359  0.7293 0.0611  0.0171  -0.0171 456  GLN A CB    
3686 C  CG    . GLN A 455 ? 0.4684 0.4346 0.807  0.0598  0.0157  -0.0179 456  GLN A CG    
3687 C  CD    . GLN A 455 ? 0.5553 0.5226 0.8973 0.0545  0.0129  -0.0212 456  GLN A CD    
3688 O  OE1   . GLN A 455 ? 0.5888 0.5528 0.926  0.0526  0.0107  -0.0233 456  GLN A OE1   
3689 N  NE2   . GLN A 455 ? 0.5622 0.5341 0.9127 0.0522  0.013   -0.0215 456  GLN A NE2   
3690 N  N     . GLN A 456 ? 0.3313 0.3067 0.6773 0.0563  0.0182  -0.0192 457  GLN A N     
3691 C  CA    . GLN A 456 ? 0.3249 0.3009 0.6689 0.0573  0.0193  -0.0186 457  GLN A CA    
3692 C  C     . GLN A 456 ? 0.2983 0.2732 0.6404 0.0538  0.017   -0.0217 457  GLN A C     
3693 O  O     . GLN A 456 ? 0.2909 0.2679 0.6376 0.0498  0.0152  -0.0241 457  GLN A O     
3694 C  CB    . GLN A 456 ? 0.3469 0.3302 0.7005 0.0575  0.0219  -0.0166 457  GLN A CB    
3695 C  CG    . GLN A 456 ? 0.4096 0.3992 0.7737 0.053   0.0212  -0.0188 457  GLN A CG    
3696 C  CD    . GLN A 456 ? 0.4994 0.4956 0.8723 0.0531  0.0233  -0.017  457  GLN A CD    
3697 O  OE1   . GLN A 456 ? 0.5229 0.5243 0.9054 0.0512  0.0236  -0.0171 457  GLN A OE1   
3698 N  NE2   . GLN A 456 ? 0.5197 0.5159 0.8895 0.0554  0.0248  -0.0153 457  GLN A NE2   
3699 N  N     . ASN A 457 ? 0.2818 0.2533 0.6169 0.0555  0.0172  -0.0214 458  ASN A N     
3700 C  CA    . ASN A 457 ? 0.2709 0.2413 0.6037 0.0527  0.0153  -0.0238 458  ASN A CA    
3701 C  C     . ASN A 457 ? 0.248  0.2259 0.5898 0.05    0.0162  -0.0246 458  ASN A C     
3702 O  O     . ASN A 457 ? 0.2464 0.229  0.5936 0.0514  0.0185  -0.0226 458  ASN A O     
3703 C  CB    . ASN A 457 ? 0.2777 0.242  0.6001 0.0557  0.0154  -0.023  458  ASN A CB    
3704 C  CG    . ASN A 457 ? 0.3095 0.2655 0.6219 0.0583  0.0139  -0.0228 458  ASN A CG    
3705 O  OD1   . ASN A 457 ? 0.3358 0.2867 0.6397 0.0624  0.0148  -0.0212 458  ASN A OD1   
3706 N  ND2   . ASN A 457 ? 0.2925 0.2467 0.6052 0.0562  0.0116  -0.0244 458  ASN A ND2   
3707 N  N     . ILE A 458 ? 0.2231 0.2022 0.5668 0.0462  0.0141  -0.0273 459  ILE A N     
3708 C  CA    . ILE A 458 ? 0.2129 0.1987 0.5643 0.0437  0.0146  -0.0284 459  ILE A CA    
3709 C  C     . ILE A 458 ? 0.2017 0.1864 0.5491 0.0425  0.0137  -0.0298 459  ILE A C     
3710 O  O     . ILE A 458 ? 0.2032 0.183  0.5446 0.0417  0.0116  -0.031  459  ILE A O     
3711 C  CB    . ILE A 458 ? 0.2223 0.2131 0.5827 0.0402  0.0137  -0.0302 459  ILE A CB    
3712 C  CG1   . ILE A 458 ? 0.2401 0.2333 0.606  0.0417  0.0154  -0.0283 459  ILE A CG1   
3713 C  CG2   . ILE A 458 ? 0.2236 0.2205 0.5908 0.0375  0.0136  -0.0319 459  ILE A CG2   
3714 C  CD1   . ILE A 458 ? 0.2592 0.2546 0.6308 0.0393  0.0144  -0.0296 459  ILE A CD1   
3715 N  N     . LEU A 459 ? 0.1829 0.1721 0.5336 0.0428  0.0152  -0.0293 460  LEU A N     
3716 C  CA    . LEU A 459 ? 0.1842 0.174  0.533  0.0417  0.0148  -0.0304 460  LEU A CA    
3717 C  C     . LEU A 459 ? 0.173  0.1707 0.5309 0.0402  0.0159  -0.0307 460  LEU A C     
3718 O  O     . LEU A 459 ? 0.1963 0.1967 0.5566 0.0423  0.018   -0.0286 460  LEU A O     
3719 C  CB    . LEU A 459 ? 0.2022 0.1877 0.5428 0.0452  0.0161  -0.0283 460  LEU A CB    
3720 C  CG    . LEU A 459 ? 0.2295 0.2157 0.5679 0.0443  0.0158  -0.0292 460  LEU A CG    
3721 C  CD1   . LEU A 459 ? 0.2389 0.2217 0.5739 0.0418  0.0131  -0.0315 460  LEU A CD1   
3722 C  CD2   . LEU A 459 ? 0.2468 0.2297 0.5784 0.048   0.0176  -0.0269 460  LEU A CD2   
3723 N  N     . VAL A 460 ? 0.1434 0.145  0.5069 0.0368  0.0144  -0.0332 461  VAL A N     
3724 C  CA    . VAL A 460 ? 0.1184 0.1274 0.4906 0.0353  0.0151  -0.034  461  VAL A CA    
3725 C  C     . VAL A 460 ? 0.1104 0.1214 0.4811 0.036   0.016   -0.0336 461  VAL A C     
3726 O  O     . VAL A 460 ? 0.1083 0.1167 0.4736 0.0356  0.0151  -0.0344 461  VAL A O     
3727 C  CB    . VAL A 460 ? 0.111  0.1233 0.4888 0.0318  0.0133  -0.0369 461  VAL A CB    
3728 C  CG1   . VAL A 460 ? 0.1006 0.1201 0.4871 0.0305  0.0138  -0.0378 461  VAL A CG1   
3729 C  CG2   . VAL A 460 ? 0.1093 0.1193 0.488  0.0311  0.0123  -0.0372 461  VAL A CG2   
3730 N  N     . ASP A 461 ? 0.1003 0.1156 0.4756 0.0372  0.0177  -0.0322 462  ASP A N     
3731 C  CA    . ASP A 461 ? 0.107  0.1247 0.4813 0.0379  0.0186  -0.0317 462  ASP A CA    
3732 C  C     . ASP A 461 ? 0.1013 0.1241 0.4806 0.0348  0.0173  -0.0346 462  ASP A C     
3733 O  O     . ASP A 461 ? 0.088  0.1149 0.4746 0.0329  0.0165  -0.0361 462  ASP A O     
3734 C  CB    . ASP A 461 ? 0.1406 0.1615 0.5186 0.0401  0.0208  -0.0289 462  ASP A CB    
3735 C  CG    . ASP A 461 ? 0.2411 0.2642 0.6174 0.0411  0.0218  -0.028  462  ASP A CG    
3736 O  OD1   . ASP A 461 ? 0.2824 0.301  0.6509 0.0435  0.0228  -0.0263 462  ASP A OD1   
3737 O  OD2   . ASP A 461 ? 0.2728 0.3018 0.6554 0.0394  0.0216  -0.0291 462  ASP A OD2   
3738 N  N     . PRO A 462 ? 0.1127 0.1354 0.4881 0.0345  0.017   -0.0353 463  PRO A N     
3739 C  CA    . PRO A 462 ? 0.1205 0.148  0.5001 0.0319  0.0157  -0.038  463  PRO A CA    
3740 C  C     . PRO A 462 ? 0.1241 0.1587 0.5111 0.0315  0.0162  -0.0384 463  PRO A C     
3741 O  O     . PRO A 462 ? 0.1286 0.1673 0.5188 0.0297  0.0152  -0.0407 463  PRO A O     
3742 C  CB    . PRO A 462 ? 0.1312 0.156  0.504  0.0321  0.0153  -0.0382 463  PRO A CB    
3743 C  CG    . PRO A 462 ? 0.1405 0.158  0.5052 0.0344  0.0159  -0.0362 463  PRO A CG    
3744 C  CD    . PRO A 462 ? 0.1155 0.1332 0.4821 0.0365  0.0176  -0.0339 463  PRO A CD    
3745 N  N     . THR A 463 ? 0.1223 0.1583 0.5122 0.0331  0.0177  -0.0362 464  THR A N     
3746 C  CA    . THR A 463 ? 0.1147 0.1572 0.5121 0.0325  0.018   -0.0365 464  THR A CA    
3747 C  C     . THR A 463 ? 0.1243 0.1685 0.5289 0.0317  0.0176  -0.0365 464  THR A C     
3748 O  O     . THR A 463 ? 0.1284 0.1701 0.5326 0.0334  0.0188  -0.0341 464  THR A O     
3749 C  CB    . THR A 463 ? 0.1179 0.1616 0.5138 0.0349  0.0199  -0.0336 464  THR A CB    
3750 O  OG1   . THR A 463 ? 0.1254 0.1676 0.5147 0.0355  0.0201  -0.0337 464  THR A OG1   
3751 C  CG2   . THR A 463 ? 0.1122 0.1626 0.5163 0.0343  0.02    -0.0335 464  THR A CG2   
3752 N  N     . PRO A 464 ? 0.1262 0.1744 0.5371 0.0293  0.0161  -0.0394 465  PRO A N     
3753 C  CA    . PRO A 464 ? 0.1256 0.1753 0.5437 0.0284  0.0156  -0.0396 465  PRO A CA    
3754 C  C     . PRO A 464 ? 0.1273 0.1813 0.5523 0.029   0.0164  -0.0378 465  PRO A C     
3755 O  O     . PRO A 464 ? 0.1309 0.1871 0.5552 0.03    0.0171  -0.0367 465  PRO A O     
3756 C  CB    . PRO A 464 ? 0.1282 0.1802 0.5496 0.0258  0.0136  -0.0434 465  PRO A CB    
3757 C  CG    . PRO A 464 ? 0.1366 0.1916 0.5566 0.0255  0.0132  -0.0448 465  PRO A CG    
3758 C  CD    . PRO A 464 ? 0.1236 0.1752 0.5356 0.0275  0.0147  -0.0424 465  PRO A CD    
3759 N  N     . ASN A 465 ? 0.1265 0.1817 0.5582 0.0285  0.0162  -0.0375 466  ASN A N     
3760 C  CA    . ASN A 465 ? 0.1311 0.1904 0.5707 0.0288  0.0166  -0.0356 466  ASN A CA    
3761 C  C     . ASN A 465 ? 0.1315 0.196  0.5752 0.0275  0.0154  -0.0376 466  ASN A C     
3762 O  O     . ASN A 465 ? 0.1349 0.2023 0.5812 0.0284  0.0161  -0.0354 466  ASN A O     
3763 C  CB    . ASN A 465 ? 0.1367 0.1965 0.5835 0.0277  0.016   -0.0359 466  ASN A CB    
3764 C  CG    . ASN A 465 ? 0.1748 0.2389 0.6309 0.0276  0.0161  -0.0341 466  ASN A CG    
3765 O  OD1   . ASN A 465 ? 0.1672 0.2349 0.6306 0.0256  0.0143  -0.0364 466  ASN A OD1   
3766 N  ND2   . ASN A 465 ? 0.1915 0.2552 0.6475 0.03    0.0181  -0.0298 466  ASN A ND2   
3767 N  N     . HIS A 466 ? 0.1253 0.191  0.5695 0.0254  0.0135  -0.0416 467  HIS A N     
3768 C  CA    . HIS A 466 ? 0.1215 0.1919 0.5688 0.0242  0.012   -0.0441 467  HIS A CA    
3769 C  C     . HIS A 466 ? 0.1179 0.1879 0.562  0.0227  0.0106  -0.048  467  HIS A C     
3770 O  O     . HIS A 466 ? 0.1221 0.1887 0.5637 0.0223  0.0104  -0.0488 467  HIS A O     
3771 C  CB    . HIS A 466 ? 0.1191 0.1936 0.5764 0.023   0.0107  -0.0447 467  HIS A CB    
3772 C  CG    . HIS A 466 ? 0.1523 0.2261 0.6141 0.0213  0.0094  -0.047  467  HIS A CG    
3773 N  ND1   . HIS A 466 ? 0.1769 0.2481 0.6407 0.0217  0.0102  -0.045  467  HIS A ND1   
3774 C  CD2   . HIS A 466 ? 0.1712 0.2466 0.6356 0.0195  0.0073  -0.051  467  HIS A CD2   
3775 C  CE1   . HIS A 466 ? 0.1895 0.2608 0.6571 0.02    0.0087  -0.0478 467  HIS A CE1   
3776 N  NE2   . HIS A 466 ? 0.1861 0.2598 0.6541 0.0187  0.0069  -0.0515 467  HIS A NE2   
3777 N  N     . TYR A 467 ? 0.1014 0.175  0.5458 0.0222  0.0095  -0.0502 468  TYR A N     
3778 C  CA    . TYR A 467 ? 0.0892 0.1631 0.531  0.0211  0.0083  -0.0535 468  TYR A CA    
3779 C  C     . TYR A 467 ? 0.0884 0.1649 0.5367 0.0195  0.0062  -0.0568 468  TYR A C     
3780 O  O     . TYR A 467 ? 0.0857 0.1657 0.5401 0.019   0.0052  -0.0575 468  TYR A O     
3781 C  CB    . TYR A 467 ? 0.0808 0.1567 0.5181 0.0218  0.0085  -0.0539 468  TYR A CB    
3782 C  CG    . TYR A 467 ? 0.0781 0.1507 0.5088 0.0235  0.0105  -0.0506 468  TYR A CG    
3783 C  CD1   . TYR A 467 ? 0.0789 0.1469 0.503  0.0238  0.0111  -0.0501 468  TYR A CD1   
3784 C  CD2   . TYR A 467 ? 0.078  0.1516 0.5093 0.0249  0.0119  -0.0477 468  TYR A CD2   
3785 C  CE1   . TYR A 467 ? 0.0892 0.1534 0.5071 0.0255  0.0128  -0.0472 468  TYR A CE1   
3786 C  CE2   . TYR A 467 ? 0.0853 0.1552 0.5104 0.0268  0.0138  -0.0445 468  TYR A CE2   
3787 C  CZ    . TYR A 467 ? 0.097  0.1621 0.5152 0.0271  0.0142  -0.0445 468  TYR A CZ    
3788 O  OH    . TYR A 467 ? 0.1097 0.1707 0.5212 0.0291  0.016   -0.0416 468  TYR A OH    
3789 N  N     . GLN A 468 ? 0.0813 0.1561 0.5284 0.0186  0.0055  -0.0589 469  GLN A N     
3790 C  CA    . GLN A 468 ? 0.084  0.1607 0.5367 0.0172  0.0037  -0.062  469  GLN A CA    
3791 C  C     . GLN A 468 ? 0.0896 0.1663 0.539  0.0167  0.0028  -0.0648 469  GLN A C     
3792 O  O     . GLN A 468 ? 0.0925 0.1692 0.5363 0.0173  0.0033  -0.0646 469  GLN A O     
3793 C  CB    . GLN A 468 ? 0.1076 0.1822 0.5652 0.0167  0.0038  -0.0608 469  GLN A CB    
3794 C  CG    . GLN A 468 ? 0.1589 0.2288 0.6123 0.0175  0.0056  -0.0578 469  GLN A CG    
3795 C  CD    . GLN A 468 ? 0.2245 0.2917 0.6729 0.0171  0.0055  -0.0589 469  GLN A CD    
3796 O  OE1   . GLN A 468 ? 0.2558 0.3235 0.6997 0.0171  0.0051  -0.0601 469  GLN A OE1   
3797 N  NE2   . GLN A 468 ? 0.2243 0.2885 0.6733 0.0167  0.0057  -0.0583 469  GLN A NE2   
3798 N  N     . GLU A 469 ? 0.094  0.1711 0.5471 0.0157  0.0014  -0.0673 470  GLU A N     
3799 C  CA    . GLU A 469 ? 0.1041 0.1818 0.5551 0.0154  0.0006  -0.0698 470  GLU A CA    
3800 C  C     . GLU A 469 ? 0.096  0.1706 0.5402 0.0156  0.0017  -0.0683 470  GLU A C     
3801 O  O     . GLU A 469 ? 0.0997 0.1759 0.5408 0.0158  0.0013  -0.0696 470  GLU A O     
3802 C  CB    . GLU A 469 ? 0.157  0.2346 0.613  0.0144  -0.0006 -0.072  470  GLU A CB    
3803 C  CG    . GLU A 469 ? 0.2539 0.3276 0.7105 0.0139  0.0002  -0.0704 470  GLU A CG    
3804 C  CD    . GLU A 469 ? 0.3391 0.4118 0.8009 0.0136  0.0006  -0.0686 470  GLU A CD    
3805 O  OE1   . GLU A 469 ? 0.3116 0.3854 0.7744 0.0142  0.001   -0.067  470  GLU A OE1   
3806 O  OE2   . GLU A 469 ? 0.3959 0.4669 0.8609 0.013   0.0005  -0.0687 470  GLU A OE2   
3807 N  N     . ASN A 470 ? 0.0915 0.1621 0.5336 0.0157  0.0029  -0.0656 471  ASN A N     
3808 C  CA    . ASN A 470 ? 0.0955 0.1628 0.5311 0.0158  0.0036  -0.0641 471  ASN A CA    
3809 C  C     . ASN A 470 ? 0.0844 0.1526 0.515  0.0168  0.0041  -0.0634 471  ASN A C     
3810 O  O     . ASN A 470 ? 0.0905 0.1583 0.5171 0.0167  0.004   -0.0635 471  ASN A O     
3811 C  CB    . ASN A 470 ? 0.1224 0.1849 0.5561 0.0161  0.0047  -0.0613 471  ASN A CB    
3812 C  CG    . ASN A 470 ? 0.1963 0.2572 0.6333 0.0152  0.0043  -0.0617 471  ASN A CG    
3813 O  OD1   . ASN A 470 ? 0.2222 0.2822 0.6627 0.0153  0.0048  -0.0605 471  ASN A OD1   
3814 N  ND2   . ASN A 470 ? 0.2158 0.2763 0.6518 0.0144  0.0036  -0.0629 471  ASN A ND2   
3815 N  N     . ASP A 471 ? 0.0662 0.1358 0.4976 0.0176  0.0048  -0.0623 472  ASP A N     
3816 C  CA    . ASP A 471 ? 0.0743 0.145  0.5014 0.0186  0.0055  -0.0614 472  ASP A CA    
3817 C  C     . ASP A 471 ? 0.0877 0.163  0.5155 0.0186  0.0045  -0.0639 472  ASP A C     
3818 O  O     . ASP A 471 ? 0.0883 0.164  0.5116 0.0191  0.0049  -0.0635 472  ASP A O     
3819 C  CB    . ASP A 471 ? 0.0794 0.1503 0.5075 0.0196  0.0065  -0.0592 472  ASP A CB    
3820 C  CG    . ASP A 471 ? 0.1085 0.1747 0.5351 0.0201  0.0077  -0.0565 472  ASP A CG    
3821 O  OD1   . ASP A 471 ? 0.1192 0.1813 0.5398 0.0205  0.0083  -0.0551 472  ASP A OD1   
3822 O  OD2   . ASP A 471 ? 0.102  0.1685 0.5335 0.02    0.0078  -0.0558 472  ASP A OD2   
3823 N  N     . VAL A 472 ? 0.0966 0.1754 0.5299 0.0181  0.0032  -0.0665 473  VAL A N     
3824 C  CA    . VAL A 472 ? 0.1127 0.1959 0.5466 0.0183  0.0021  -0.0692 473  VAL A CA    
3825 C  C     . VAL A 472 ? 0.1279 0.2103 0.5586 0.0182  0.0019  -0.0699 473  VAL A C     
3826 O  O     . VAL A 472 ? 0.1402 0.2249 0.5679 0.0189  0.002   -0.0703 473  VAL A O     
3827 C  CB    . VAL A 472 ? 0.1155 0.2016 0.5559 0.0178  0.0005  -0.072  473  VAL A CB    
3828 C  CG1   . VAL A 472 ? 0.1221 0.2124 0.5624 0.0184  -0.0008 -0.0751 473  VAL A CG1   
3829 C  CG2   . VAL A 472 ? 0.1138 0.2011 0.5579 0.0179  0.0004  -0.0711 473  VAL A CG2   
3830 N  N     . ASP A 473 ? 0.1175 0.1968 0.5489 0.0173  0.0018  -0.0697 474  ASP A N     
3831 C  CA    . ASP A 473 ? 0.1164 0.1948 0.5454 0.0169  0.0016  -0.0699 474  ASP A CA    
3832 C  C     . ASP A 473 ? 0.103  0.1791 0.5259 0.0173  0.0026  -0.0675 474  ASP A C     
3833 O  O     . ASP A 473 ? 0.1077 0.1854 0.5284 0.0175  0.0024  -0.0677 474  ASP A O     
3834 C  CB    . ASP A 473 ? 0.1541 0.2293 0.5852 0.0159  0.0014  -0.0697 474  ASP A CB    
3835 C  CG    . ASP A 473 ? 0.2779 0.3527 0.7075 0.0155  0.0011  -0.07   474  ASP A CG    
3836 O  OD1   . ASP A 473 ? 0.312  0.3903 0.7428 0.0159  0.0004  -0.0721 474  ASP A OD1   
3837 O  OD2   . ASP A 473 ? 0.3267 0.3976 0.7536 0.0149  0.0015  -0.068  474  ASP A OD2   
3838 N  N     . THR A 474 ? 0.0778 0.1502 0.4982 0.0174  0.0036  -0.065  475  THR A N     
3839 C  CA    . THR A 474 ? 0.0707 0.1404 0.4853 0.0178  0.0043  -0.0628 475  THR A CA    
3840 C  C     . THR A 474 ? 0.0744 0.1478 0.4871 0.0188  0.0047  -0.063  475  THR A C     
3841 O  O     . THR A 474 ? 0.0718 0.145  0.4811 0.0189  0.0047  -0.0623 475  THR A O     
3842 C  CB    . THR A 474 ? 0.0759 0.141  0.4882 0.0181  0.0053  -0.0603 475  THR A CB    
3843 O  OG1   . THR A 474 ? 0.0881 0.1498 0.5017 0.0173  0.005   -0.06   475  THR A OG1   
3844 C  CG2   . THR A 474 ? 0.0755 0.1374 0.4813 0.0188  0.006   -0.0581 475  THR A CG2   
3845 N  N     . VAL A 475 ? 0.0769 0.1536 0.4921 0.0195  0.0048  -0.0638 476  VAL A N     
3846 C  CA    . VAL A 475 ? 0.0943 0.1749 0.5079 0.0205  0.0052  -0.0641 476  VAL A CA    
3847 C  C     . VAL A 475 ? 0.1098 0.1945 0.5243 0.0207  0.0043  -0.0662 476  VAL A C     
3848 O  O     . VAL A 475 ? 0.1149 0.2009 0.5262 0.0214  0.0048  -0.0655 476  VAL A O     
3849 C  CB    . VAL A 475 ? 0.1055 0.189  0.5221 0.0211  0.0053  -0.0645 476  VAL A CB    
3850 C  CG1   . VAL A 475 ? 0.1173 0.2057 0.5331 0.0222  0.0054  -0.0653 476  VAL A CG1   
3851 C  CG2   . VAL A 475 ? 0.1129 0.1927 0.5279 0.0215  0.0065  -0.0618 476  VAL A CG2   
3852 N  N     . ILE A 476 ? 0.1132 0.1998 0.5319 0.0203  0.0031  -0.0687 477  ILE A N     
3853 C  CA    . ILE A 476 ? 0.1234 0.214  0.5428 0.0208  0.0024  -0.0707 477  ILE A CA    
3854 C  C     . ILE A 476 ? 0.134  0.2228 0.5502 0.0205  0.0027  -0.0692 477  ILE A C     
3855 O  O     . ILE A 476 ? 0.1321 0.2239 0.5464 0.0215  0.0029  -0.0691 477  ILE A O     
3856 C  CB    . ILE A 476 ? 0.1312 0.2233 0.5555 0.0204  0.001   -0.0737 477  ILE A CB    
3857 C  CG1   . ILE A 476 ? 0.1349 0.2299 0.5625 0.0209  0.0003  -0.0755 477  ILE A CG1   
3858 C  CG2   . ILE A 476 ? 0.1406 0.2354 0.565  0.0211  0.0004  -0.0754 477  ILE A CG2   
3859 C  CD1   . ILE A 476 ? 0.1468 0.2466 0.573  0.0224  0.0002  -0.0764 477  ILE A CD1   
3860 N  N     . TYR A 477 ? 0.1388 0.2229 0.5546 0.0193  0.0027  -0.0679 478  TYR A N     
3861 C  CA    . TYR A 477 ? 0.1509 0.2328 0.564  0.0188  0.0027  -0.0662 478  TYR A CA    
3862 C  C     . TYR A 477 ? 0.1415 0.2226 0.5502 0.0192  0.0035  -0.0639 478  TYR A C     
3863 O  O     . TYR A 477 ? 0.1388 0.2215 0.5461 0.0195  0.0035  -0.0632 478  TYR A O     
3864 C  CB    . TYR A 477 ? 0.1698 0.2466 0.5832 0.0174  0.0025  -0.0651 478  TYR A CB    
3865 C  CG    . TYR A 477 ? 0.1993 0.2739 0.6107 0.0166  0.0022  -0.0635 478  TYR A CG    
3866 C  CD1   . TYR A 477 ? 0.2248 0.3017 0.6384 0.0164  0.0016  -0.0644 478  TYR A CD1   
3867 C  CD2   . TYR A 477 ? 0.2197 0.2897 0.627  0.016   0.0024  -0.0609 478  TYR A CD2   
3868 C  CE1   . TYR A 477 ? 0.2401 0.3153 0.6525 0.0156  0.0012  -0.0626 478  TYR A CE1   
3869 C  CE2   . TYR A 477 ? 0.2412 0.309  0.647  0.0151  0.0018  -0.0594 478  TYR A CE2   
3870 C  CZ    . TYR A 477 ? 0.2586 0.3293 0.6672 0.0148  0.0012  -0.0601 478  TYR A CZ    
3871 O  OH    . TYR A 477 ? 0.2953 0.364  0.7026 0.0138  0.0006  -0.0581 478  TYR A OH    
3872 N  N     . SER A 478 ? 0.1413 0.22   0.5478 0.0195  0.0043  -0.0626 479  SER A N     
3873 C  CA    . SER A 478 ? 0.148  0.2253 0.5499 0.0201  0.0051  -0.0604 479  SER A CA    
3874 C  C     . SER A 478 ? 0.1563 0.2392 0.558  0.0213  0.0055  -0.061  479  SER A C     
3875 O  O     . SER A 478 ? 0.1683 0.2513 0.5674 0.0216  0.0058  -0.0594 479  SER A O     
3876 C  CB    . SER A 478 ? 0.1609 0.2347 0.5605 0.0204  0.006   -0.059  479  SER A CB    
3877 O  OG    . SER A 478 ? 0.1884 0.2572 0.588  0.0195  0.0057  -0.0584 479  SER A OG    
3878 N  N     . ILE A 479 ? 0.1495 0.2369 0.554  0.0222  0.0054  -0.0631 480  ILE A N     
3879 C  CA    . ILE A 479 ? 0.1643 0.2573 0.5688 0.0236  0.0057  -0.0639 480  ILE A CA    
3880 C  C     . ILE A 479 ? 0.1845 0.2807 0.5897 0.0241  0.0052  -0.0645 480  ILE A C     
3881 O  O     . ILE A 479 ? 0.1897 0.2881 0.5928 0.025   0.0058  -0.0632 480  ILE A O     
3882 C  CB    . ILE A 479 ? 0.1718 0.2685 0.5794 0.0243  0.0053  -0.0663 480  ILE A CB    
3883 C  CG1   . ILE A 479 ? 0.1835 0.2783 0.59   0.0244  0.0062  -0.0648 480  ILE A CG1   
3884 C  CG2   . ILE A 479 ? 0.1797 0.2829 0.5882 0.0259  0.005   -0.0681 480  ILE A CG2   
3885 C  CD1   . ILE A 479 ? 0.2004 0.2979 0.6106 0.0246  0.0056  -0.0667 480  ILE A CD1   
3886 N  N     . PHE A 480 ? 0.1893 0.2859 0.5974 0.0235  0.0042  -0.0663 481  PHE A N     
3887 C  CA    . PHE A 480 ? 0.2003 0.3003 0.6094 0.0242  0.0038  -0.0669 481  PHE A CA    
3888 C  C     . PHE A 480 ? 0.2349 0.3321 0.6427 0.0233  0.0039  -0.0645 481  PHE A C     
3889 O  O     . PHE A 480 ? 0.2412 0.3416 0.6496 0.024   0.0038  -0.0643 481  PHE A O     
3890 C  CB    . PHE A 480 ? 0.1854 0.2876 0.5982 0.0245  0.0028  -0.0701 481  PHE A CB    
3891 C  CG    . PHE A 480 ? 0.1784 0.2849 0.5926 0.0259  0.0024  -0.0726 481  PHE A CG    
3892 C  CD1   . PHE A 480 ? 0.1774 0.2891 0.5905 0.0279  0.0027  -0.0733 481  PHE A CD1   
3893 C  CD2   . PHE A 480 ? 0.1884 0.2936 0.605  0.0252  0.0018  -0.0743 481  PHE A CD2   
3894 C  CE1   . PHE A 480 ? 0.1857 0.3012 0.5999 0.0292  0.0021  -0.0757 481  PHE A CE1   
3895 C  CE2   . PHE A 480 ? 0.196  0.3051 0.614  0.0264  0.0012  -0.0765 481  PHE A CE2   
3896 C  CZ    . PHE A 480 ? 0.1876 0.3018 0.6043 0.0283  0.0013  -0.0773 481  PHE A CZ    
3897 N  N     . LYS A 481 ? 0.2599 0.3513 0.6661 0.0217  0.0038  -0.0627 482  LYS A N     
3898 C  CA    . LYS A 481 ? 0.295  0.3833 0.7    0.0205  0.0035  -0.0604 482  LYS A CA    
3899 C  C     . LYS A 481 ? 0.3222 0.4081 0.7234 0.0204  0.004   -0.0575 482  LYS A C     
3900 O  O     . LYS A 481 ? 0.3255 0.4108 0.7261 0.0199  0.0037  -0.0555 482  LYS A O     
3901 C  CB    . LYS A 481 ? 0.3325 0.4157 0.7384 0.0188  0.0028  -0.0603 482  LYS A CB    
3902 C  CG    . LYS A 481 ? 0.3904 0.4747 0.7988 0.0183  0.0021  -0.0605 482  LYS A CG    
3903 C  CD    . LYS A 481 ? 0.4293 0.5188 0.8411 0.0195  0.002   -0.0634 482  LYS A CD    
3904 C  CE    . LYS A 481 ? 0.4581 0.5497 0.8716 0.0197  0.0016  -0.0631 482  LYS A CE    
3905 N  NZ    . LYS A 481 ? 0.4693 0.5658 0.8855 0.0213  0.0015  -0.066  482  LYS A NZ    
3906 N  N     . TYR A 482 ? 0.3345 0.419  0.7334 0.0209  0.0048  -0.0572 483  TYR A N     
3907 C  CA    . TYR A 482 ? 0.3481 0.4297 0.7431 0.0208  0.0052  -0.0546 483  TYR A CA    
3908 C  C     . TYR A 482 ? 0.3605 0.446  0.7542 0.0225  0.0064  -0.0543 483  TYR A C     
3909 O  O     . TYR A 482 ? 0.3681 0.454  0.76   0.0228  0.0067  -0.0523 483  TYR A O     
3910 C  CB    . TYR A 482 ? 0.3529 0.4275 0.745  0.0198  0.0052  -0.0536 483  TYR A CB    
3911 C  CG    . TYR A 482 ? 0.3725 0.4429 0.7655 0.0182  0.004   -0.0534 483  TYR A CG    
3912 C  CD1   . TYR A 482 ? 0.385  0.4541 0.7779 0.0172  0.0031  -0.0519 483  TYR A CD1   
3913 C  CD2   . TYR A 482 ? 0.3904 0.4585 0.7846 0.0178  0.0039  -0.0547 483  TYR A CD2   
3914 C  CE1   . TYR A 482 ? 0.4016 0.4671 0.7953 0.0157  0.002   -0.0517 483  TYR A CE1   
3915 C  CE2   . TYR A 482 ? 0.4077 0.4724 0.8029 0.0164  0.0029  -0.0546 483  TYR A CE2   
3916 C  CZ    . TYR A 482 ? 0.4218 0.4851 0.8165 0.0154  0.002   -0.0531 483  TYR A CZ    
3917 O  OH    . TYR A 482 ? 0.4525 0.5126 0.8482 0.014   0.001   -0.0529 483  TYR A OH    
3918 N  N     . ILE A 483 ? 0.3625 0.4509 0.7573 0.0235  0.0069  -0.0562 484  ILE A N     
3919 C  CA    . ILE A 483 ? 0.37   0.462  0.7634 0.0251  0.008   -0.0559 484  ILE A CA    
3920 C  C     . ILE A 483 ? 0.3752 0.4742 0.7704 0.0265  0.0081  -0.0567 484  ILE A C     
3921 O  O     . ILE A 483 ? 0.3742 0.4747 0.7677 0.0272  0.0088  -0.0548 484  ILE A O     
3922 C  CB    . ILE A 483 ? 0.3713 0.4637 0.765  0.0256  0.0085  -0.0572 484  ILE A CB    
3923 C  CG1   . ILE A 483 ? 0.3774 0.4629 0.7688 0.0246  0.0087  -0.0558 484  ILE A CG1   
3924 C  CG2   . ILE A 483 ? 0.3758 0.4725 0.7684 0.0273  0.0096  -0.0568 484  ILE A CG2   
3925 C  CD1   . ILE A 483 ? 0.3844 0.4701 0.7769 0.025   0.0091  -0.0567 484  ILE A CD1   
3926 N  N     . VAL A 484 ? 0.3791 0.4821 0.7774 0.0271  0.0075  -0.0594 485  VAL A N     
3927 C  CA    . VAL A 484 ? 0.3921 0.5017 0.7918 0.0289  0.0076  -0.0605 485  VAL A CA    
3928 C  C     . VAL A 484 ? 0.4159 0.5264 0.8157 0.0289  0.0076  -0.0585 485  VAL A C     
3929 O  O     . VAL A 484 ? 0.4167 0.5315 0.8158 0.0305  0.0084  -0.0573 485  VAL A O     
3930 C  CB    . VAL A 484 ? 0.39   0.503  0.7928 0.0296  0.0067  -0.064  485  VAL A CB    
3931 C  CG1   . VAL A 484 ? 0.3946 0.5143 0.7981 0.0318  0.0068  -0.0651 485  VAL A CG1   
3932 C  CG2   . VAL A 484 ? 0.3921 0.5049 0.7953 0.0295  0.0066  -0.0655 485  VAL A CG2   
3933 N  N     . PRO A 485 ? 0.4344 0.5412 0.835  0.0273  0.0068  -0.0577 486  PRO A N     
3934 C  CA    . PRO A 485 ? 0.4555 0.5635 0.8564 0.0273  0.0068  -0.0553 486  PRO A CA    
3935 C  C     . PRO A 485 ? 0.4844 0.5885 0.8828 0.0263  0.007   -0.0518 486  PRO A C     
3936 O  O     . PRO A 485 ? 0.4902 0.5957 0.8893 0.0264  0.007   -0.0495 486  PRO A O     
3937 C  CB    . PRO A 485 ? 0.4606 0.5664 0.8637 0.026   0.0057  -0.0561 486  PRO A CB    
3938 C  CG    . PRO A 485 ? 0.4618 0.5622 0.8644 0.0245  0.0052  -0.0573 486  PRO A CG    
3939 C  CD    . PRO A 485 ? 0.4324 0.534  0.8339 0.0254  0.0059  -0.0586 486  PRO A CD    
3940 N  N     . ASN A 486 ? 0.5019 0.6012 0.8977 0.0254  0.0072  -0.0513 487  ASN A N     
3941 C  CA    . ASN A 486 ? 0.5286 0.6228 0.9213 0.0244  0.0073  -0.0483 487  ASN A CA    
3942 C  C     . ASN A 486 ? 0.5442 0.6337 0.9372 0.0224  0.0059  -0.0466 487  ASN A C     
3943 O  O     . ASN A 486 ? 0.5417 0.6315 0.935  0.0221  0.0057  -0.044  487  ASN A O     
3944 C  CB    . ASN A 486 ? 0.5489 0.6468 0.9406 0.0258  0.0083  -0.0463 487  ASN A CB    
3945 C  CG    . ASN A 486 ? 0.5885 0.6877 0.9781 0.0272  0.0096  -0.047  487  ASN A CG    
3946 O  OD1   . ASN A 486 ? 0.596  0.6981 0.9867 0.0281  0.0099  -0.0496 487  ASN A OD1   
3947 N  ND2   . ASN A 486 ? 0.6012 0.6982 0.988  0.0273  0.0103  -0.0446 487  ASN A ND2   
3948 N  N     . CYS A 487 ? 0.5568 0.6423 0.9502 0.0211  0.0051  -0.048  488  CYS A N     
3949 C  CA    . CYS A 487 ? 0.5753 0.6562 0.9691 0.0191  0.0037  -0.0468 488  CYS A CA    
3950 C  C     . CYS A 487 ? 0.584  0.6571 0.9744 0.0178  0.0032  -0.0465 488  CYS A C     
3951 O  O     . CYS A 487 ? 0.5893 0.6611 0.9778 0.0185  0.004   -0.0476 488  CYS A O     
3952 C  CB    . CYS A 487 ? 0.5956 0.679  0.993  0.0189  0.0032  -0.0487 488  CYS A CB    
3953 S  SG    . CYS A 487 ? 0.682  0.7743 1.0828 0.0209  0.0039  -0.0492 488  CYS A SG    
3954 N  N     . PHE A 488 ? 0.5844 0.6524 0.9741 0.0161  0.0018  -0.0449 489  PHE A N     
3955 C  CA    . PHE A 488 ? 0.5938 0.6542 0.98   0.015   0.0011  -0.0447 489  PHE A CA    
3956 C  C     . PHE A 488 ? 0.5965 0.654  0.9843 0.0135  -0.0002 -0.0451 489  PHE A C     
3957 O  O     . PHE A 488 ? 0.5986 0.65   0.9836 0.0128  -0.0009 -0.045  489  PHE A O     
3958 C  CB    . PHE A 488 ? 0.5964 0.6517 0.9785 0.0146  0.0005  -0.0421 489  PHE A CB    
3959 C  CG    . PHE A 488 ? 0.6044 0.6578 0.9871 0.013   -0.0012 -0.0397 489  PHE A CG    
3960 C  CD1   . PHE A 488 ? 0.6143 0.662  0.9962 0.0113  -0.003  -0.0391 489  PHE A CD1   
3961 C  CD2   . PHE A 488 ? 0.6139 0.6706 0.9976 0.0133  -0.001  -0.0377 489  PHE A CD2   
3962 C  CE1   . PHE A 488 ? 0.6232 0.6689 1.0057 0.0097  -0.0048 -0.0366 489  PHE A CE1   
3963 C  CE2   . PHE A 488 ? 0.6227 0.6775 1.0072 0.0118  -0.0027 -0.0351 489  PHE A CE2   
3964 C  CZ    . PHE A 488 ? 0.6208 0.6701 1.0048 0.0099  -0.0047 -0.0346 489  PHE A CZ    
3965 N  N     . SER A 489 ? 0.5969 0.6585 0.9887 0.0131  -0.0006 -0.0454 490  SER A N     
3966 C  CA    . SER A 489 ? 0.6098 0.6691 1.0034 0.0117  -0.0017 -0.0457 490  SER A CA    
3967 C  C     . SER A 489 ? 0.6184 0.6839 1.0167 0.0122  -0.0013 -0.0473 490  SER A C     
3968 O  O     . SER A 489 ? 0.6158 0.6872 1.0157 0.0137  -0.0003 -0.0479 490  SER A O     
3969 C  CB    . SER A 489 ? 0.6238 0.6792 1.0164 0.0099  -0.0035 -0.0429 490  SER A CB    
3970 O  OG    . SER A 489 ? 0.644  0.7039 1.0389 0.01    -0.0036 -0.0411 490  SER A OG    
3971 N  N     . GLY A 490 ? 0.6264 0.6904 1.0266 0.0112  -0.002  -0.0479 491  GLY A N     
3972 C  CA    . GLY A 490 ? 0.6381 0.707  1.0425 0.0116  -0.0017 -0.0493 491  GLY A CA    
3973 C  C     . GLY A 490 ? 0.6487 0.7219 1.0552 0.0118  -0.0019 -0.0474 491  GLY A C     
3974 O  O     . GLY A 490 ? 0.6489 0.7277 1.0583 0.0131  -0.0013 -0.0486 491  GLY A O     
3975 N  N     . MET A 491 ? 0.654  0.7247 1.0592 0.0106  -0.0029 -0.0444 492  MET A N     
3976 C  CA    . MET A 491 ? 0.6632 0.7379 1.0707 0.0108  -0.0031 -0.0419 492  MET A CA    
3977 C  C     . MET A 491 ? 0.6587 0.7369 1.0651 0.0123  -0.0021 -0.0412 492  MET A C     
3978 O  O     . MET A 491 ? 0.6601 0.7358 1.0646 0.0116  -0.0027 -0.0388 492  MET A O     
3979 C  CB    . MET A 491 ? 0.6854 0.7557 1.0926 0.0085  -0.005  -0.0387 492  MET A CB    
3980 C  CG    . MET A 491 ? 0.7407 0.8039 1.1456 0.0068  -0.0062 -0.0392 492  MET A CG    
3981 S  SD    . MET A 491 ? 0.8545 0.918  1.262  0.0066  -0.006  -0.0417 492  MET A SD    
3982 C  CE    . MET A 491 ? 0.8412 0.9048 1.2516 0.0048  -0.0076 -0.0387 492  MET A CE    
3983 N  N     . CYS A 492 ? 0.6508 0.7345 1.0583 0.0145  -0.0007 -0.0434 493  CYS A N     
3984 C  CA    . CYS A 492 ? 0.6483 0.7362 1.0549 0.0164  0.0004  -0.0431 493  CYS A CA    
3985 C  C     . CYS A 492 ? 0.6371 0.7321 1.0458 0.0188  0.0017  -0.0453 493  CYS A C     
3986 O  O     . CYS A 492 ? 0.6389 0.7347 1.0493 0.0191  0.0016  -0.0478 493  CYS A O     
3987 C  CB    . CYS A 492 ? 0.6604 0.7445 1.0633 0.0163  0.0008  -0.0439 493  CYS A CB    
3988 N  N     . ASN A 493 ? 0.6194 0.7195 1.028  0.0208  0.0027  -0.0445 494  ASN A N     
3989 C  CA    . ASN A 493 ? 0.5997 0.7068 1.0095 0.0236  0.0038  -0.0463 494  ASN A CA    
3990 C  C     . ASN A 493 ? 0.5691 0.6783 0.9813 0.0243  0.0036  -0.0489 494  ASN A C     
3991 O  O     . ASN A 493 ? 0.5741 0.6806 0.9877 0.0227  0.0028  -0.0478 494  ASN A O     
3992 C  CB    . ASN A 493 ? 0.6197 0.7273 1.0272 0.0247  0.0046  -0.0484 494  ASN A CB    
3993 C  CG    . ASN A 493 ? 0.6643 0.7763 1.0708 0.0266  0.0057  -0.0468 494  ASN A CG    
3994 O  OD1   . ASN A 493 ? 0.6763 0.7897 1.0811 0.0277  0.0065  -0.0482 494  ASN A OD1   
3995 N  ND2   . ASN A 493 ? 0.6705 0.7852 1.0784 0.027   0.0059  -0.0435 494  ASN A ND2   
3996 N  N     . PRO A 494 ? 0.5358 0.6496 0.9486 0.0266  0.0042  -0.052  495  PRO A N     
3997 C  CA    . PRO A 494 ? 0.513  0.6277 0.9279 0.0271  0.0038  -0.0543 495  PRO A CA    
3998 C  C     . PRO A 494 ? 0.4851 0.5939 0.9002 0.0247  0.0029  -0.0561 495  PRO A C     
3999 O  O     . PRO A 494 ? 0.484  0.5903 0.8977 0.0242  0.0029  -0.0576 495  PRO A O     
4000 C  CB    . PRO A 494 ? 0.5233 0.6434 0.9382 0.03    0.0044  -0.0574 495  PRO A CB    
4001 C  CG    . PRO A 494 ? 0.5326 0.6528 0.9453 0.0303  0.0048  -0.0577 495  PRO A CG    
4002 C  CD    . PRO A 494 ? 0.5215 0.6394 0.933  0.0289  0.0051  -0.0538 495  PRO A CD    
4003 N  N     . PRO A 495 ? 0.4591 0.5656 0.876  0.0234  0.0023  -0.0554 496  PRO A N     
4004 C  CA    . PRO A 495 ? 0.4419 0.5428 0.859  0.0212  0.0016  -0.0567 496  PRO A CA    
4005 C  C     . PRO A 495 ? 0.4196 0.5208 0.8376 0.0219  0.0015  -0.0607 496  PRO A C     
4006 O  O     . PRO A 495 ? 0.4208 0.5178 0.8387 0.0205  0.0011  -0.0618 496  PRO A O     
4007 C  CB    . PRO A 495 ? 0.454  0.5534 0.8729 0.0199  0.001   -0.0548 496  PRO A CB    
4008 C  CG    . PRO A 495 ? 0.461  0.5647 0.8806 0.0211  0.0014  -0.0518 496  PRO A CG    
4009 C  CD    . PRO A 495 ? 0.4452 0.5542 0.8641 0.0238  0.0024  -0.0532 496  PRO A CD    
4010 N  N     . GLY A 496 ? 0.3934 0.4996 0.8125 0.0243  0.0018  -0.0628 497  GLY A N     
4011 C  CA    . GLY A 496 ? 0.3736 0.4805 0.7941 0.0251  0.0014  -0.0668 497  GLY A CA    
4012 C  C     . GLY A 496 ? 0.3488 0.4524 0.7715 0.0237  0.0009  -0.0677 497  GLY A C     
4013 O  O     . GLY A 496 ? 0.35   0.4529 0.7736 0.023   0.0008  -0.0658 497  GLY A O     
4014 N  N     . GLY A 497 ? 0.3268 0.4284 0.7508 0.0231  0.0004  -0.0704 498  GLY A N     
4015 C  CA    . GLY A 497 ? 0.3153 0.4137 0.7417 0.0218  -0.0001 -0.0714 498  GLY A CA    
4016 C  C     . GLY A 497 ? 0.3011 0.3956 0.7283 0.0203  -0.0005 -0.0725 498  GLY A C     
4017 O  O     . GLY A 497 ? 0.2886 0.3831 0.7147 0.0204  -0.0004 -0.0731 498  GLY A O     
4018 N  N     . ASP A 498 ? 0.2986 0.39   0.7279 0.0189  -0.0008 -0.0726 499  ASP A N     
4019 C  CA    . ASP A 498 ? 0.306  0.3937 0.7369 0.0176  -0.001  -0.0735 499  ASP A CA    
4020 C  C     . ASP A 498 ? 0.3172 0.4039 0.7515 0.0171  -0.0014 -0.0747 499  ASP A C     
4021 O  O     . ASP A 498 ? 0.3168 0.406  0.752  0.0182  -0.0014 -0.0755 499  ASP A O     
4022 C  CB    . ASP A 498 ? 0.3233 0.4067 0.7518 0.0159  -0.0007 -0.0706 499  ASP A CB    
4023 C  CG    . ASP A 498 ? 0.3706 0.4514 0.7981 0.0147  -0.0007 -0.0678 499  ASP A CG    
4024 O  OD1   . ASP A 498 ? 0.3729 0.4551 0.8023 0.0148  -0.0009 -0.0679 499  ASP A OD1   
4025 O  OD2   . ASP A 498 ? 0.3889 0.4664 0.8137 0.0136  -0.0007 -0.0655 499  ASP A OD2   
4026 N  N     . TRP A 499 ? 0.3251 0.4082 0.7613 0.0157  -0.0015 -0.0747 500  TRP A N     
4027 C  CA    . TRP A 499 ? 0.3396 0.4214 0.7791 0.0153  -0.0017 -0.0757 500  TRP A CA    
4028 C  C     . TRP A 499 ? 0.3371 0.4184 0.7763 0.0148  -0.0015 -0.0736 500  TRP A C     
4029 O  O     . TRP A 499 ? 0.3468 0.4284 0.7887 0.0149  -0.0015 -0.0746 500  TRP A O     
4030 C  CB    . TRP A 499 ? 0.3535 0.4316 0.7951 0.0139  -0.0017 -0.0756 500  TRP A CB    
4031 C  CG    . TRP A 499 ? 0.3803 0.4545 0.8195 0.0125  -0.0013 -0.0725 500  TRP A CG    
4032 C  CD1   . TRP A 499 ? 0.4005 0.4729 0.8364 0.0122  -0.001  -0.0707 500  TRP A CD1   
4033 C  CD2   . TRP A 499 ? 0.3914 0.4629 0.8312 0.0113  -0.0012 -0.0708 500  TRP A CD2   
4034 N  NE1   . TRP A 499 ? 0.4126 0.4811 0.8468 0.011   -0.0008 -0.0682 500  TRP A NE1   
4035 C  CE2   . TRP A 499 ? 0.4086 0.4766 0.8452 0.0104  -0.001  -0.0681 500  TRP A CE2   
4036 C  CE3   . TRP A 499 ? 0.4038 0.4754 0.8466 0.0111  -0.0012 -0.0712 500  TRP A CE3   
4037 C  CZ2   . TRP A 499 ? 0.4216 0.4862 0.8577 0.0092  -0.001  -0.0661 500  TRP A CZ2   
4038 C  CZ3   . TRP A 499 ? 0.4191 0.4877 0.8616 0.0098  -0.0011 -0.0689 500  TRP A CZ3   
4039 C  CH2   . TRP A 499 ? 0.4234 0.4886 0.8626 0.0089  -0.0011 -0.0665 500  TRP A CH2   
4040 N  N     . SER A 500 ? 0.3218 0.4023 0.7579 0.0141  -0.0012 -0.0707 501  SER A N     
4041 C  CA    . SER A 500 ? 0.3157 0.3956 0.7516 0.0134  -0.0012 -0.0683 501  SER A CA    
4042 C  C     . SER A 500 ? 0.3039 0.3881 0.7395 0.0148  -0.001  -0.0677 501  SER A C     
4043 O  O     . SER A 500 ? 0.3057 0.3899 0.7417 0.0143  -0.001  -0.0655 501  SER A O     
4044 C  CB    . SER A 500 ? 0.3246 0.4008 0.7577 0.0118  -0.0013 -0.0652 501  SER A CB    
4045 O  OG    . SER A 500 ? 0.3533 0.431  0.7835 0.0123  -0.0013 -0.0638 501  SER A OG    
4046 N  N     . GLY A 501 ? 0.2876 0.3754 0.7223 0.0167  -0.0009 -0.0693 502  GLY A N     
4047 C  CA    . GLY A 501 ? 0.277  0.3692 0.7112 0.0185  -0.0005 -0.0686 502  GLY A CA    
4048 C  C     . GLY A 501 ? 0.2681 0.3638 0.7003 0.0202  -0.0003 -0.0694 502  GLY A C     
4049 O  O     . GLY A 501 ? 0.2715 0.3659 0.7021 0.0197  -0.0004 -0.0696 502  GLY A O     
4050 N  N     . LEU A 502 ? 0.2546 0.3548 0.6867 0.0226  0       -0.0698 503  LEU A N     
4051 C  CA    . LEU A 502 ? 0.2439 0.3481 0.6741 0.0246  0.0002  -0.0706 503  LEU A CA    
4052 C  C     . LEU A 502 ? 0.2482 0.3557 0.6772 0.0257  0.0009  -0.0674 503  LEU A C     
4053 O  O     . LEU A 502 ? 0.247  0.3567 0.6772 0.0268  0.0013  -0.0664 503  LEU A O     
4054 C  CB    . LEU A 502 ? 0.2298 0.3368 0.6608 0.0271  -0.0001 -0.0747 503  LEU A CB    
4055 C  CG    . LEU A 502 ? 0.2291 0.341  0.6581 0.0298  0.0002  -0.0757 503  LEU A CG    
4056 C  CD1   . LEU A 502 ? 0.2311 0.3425 0.6584 0.0291  0.0001  -0.0756 503  LEU A CD1   
4057 C  CD2   . LEU A 502 ? 0.2299 0.3441 0.6595 0.0323  -0.0004 -0.0797 503  LEU A CD2   
4058 N  N     . SER A 503 ? 0.2455 0.3537 0.6725 0.0255  0.0012  -0.0655 504  SER A N     
4059 C  CA    . SER A 503 ? 0.2542 0.3658 0.6803 0.0266  0.0018  -0.0622 504  SER A CA    
4060 C  C     . SER A 503 ? 0.2672 0.3838 0.6918 0.0295  0.0024  -0.0635 504  SER A C     
4061 O  O     . SER A 503 ? 0.2738 0.3899 0.6971 0.0295  0.0022  -0.0654 504  SER A O     
4062 C  CB    . SER A 503 ? 0.2668 0.3753 0.6919 0.0242  0.0016  -0.0586 504  SER A CB    
4063 O  OG    . SER A 503 ? 0.2846 0.3895 0.7111 0.0219  0.0011  -0.0568 504  SER A OG    
4064 N  N     . ILE A 504 ? 0.272  0.3936 0.6968 0.032   0.0031  -0.0622 505  ILE A N     
4065 C  CA    . ILE A 504 ? 0.2833 0.4103 0.7066 0.0351  0.0037  -0.0629 505  ILE A CA    
4066 C  C     . ILE A 504 ? 0.2955 0.4253 0.7187 0.0357  0.0046  -0.0582 505  ILE A C     
4067 O  O     . ILE A 504 ? 0.2933 0.4239 0.7182 0.0356  0.0048  -0.0555 505  ILE A O     
4068 C  CB    . ILE A 504 ? 0.288  0.4186 0.7114 0.0385  0.0039  -0.0659 505  ILE A CB    
4069 C  CG1   . ILE A 504 ? 0.3023 0.4297 0.7266 0.0378  0.0028  -0.0703 505  ILE A CG1   
4070 C  CG2   . ILE A 504 ? 0.2932 0.4294 0.7147 0.042   0.0045  -0.0666 505  ILE A CG2   
4071 C  CD1   . ILE A 504 ? 0.3213 0.447  0.7447 0.037   0.0021  -0.0731 505  ILE A CD1   
4072 N  N     . ILE A 505 ? 0.3029 0.4346 0.7245 0.0362  0.0051  -0.0568 506  ILE A N     
4073 C  CA    . ILE A 505 ? 0.3217 0.4565 0.7438 0.0368  0.0059  -0.0521 506  ILE A CA    
4074 C  C     . ILE A 505 ? 0.3429 0.4847 0.7642 0.0409  0.007   -0.0521 506  ILE A C     
4075 O  O     . ILE A 505 ? 0.3404 0.484  0.76   0.0429  0.007   -0.0558 506  ILE A O     
4076 C  CB    . ILE A 505 ? 0.3307 0.462  0.752  0.034   0.0056  -0.0494 506  ILE A CB    
4077 C  CG1   . ILE A 505 ? 0.3455 0.4772 0.7644 0.0346  0.0058  -0.0514 506  ILE A CG1   
4078 C  CG2   . ILE A 505 ? 0.3362 0.4607 0.7582 0.0302  0.0044  -0.049  506  ILE A CG2   
4079 C  CD1   . ILE A 505 ? 0.3678 0.4985 0.7858 0.0334  0.0061  -0.0481 506  ILE A CD1   
4080 N  N     . ASP A 506 ? 0.3616 0.5074 0.784  0.0422  0.0079  -0.0479 507  ASP A N     
4081 C  CA    . ASP A 506 ? 0.389  0.5416 0.8106 0.0462  0.0092  -0.0469 507  ASP A CA    
4082 C  C     . ASP A 506 ? 0.4098 0.5641 0.8326 0.0455  0.0099  -0.0415 507  ASP A C     
4083 O  O     . ASP A 506 ? 0.4182 0.5677 0.8409 0.042   0.0091  -0.0403 507  ASP A O     
4084 C  CB    . ASP A 506 ? 0.423  0.5801 0.8451 0.0499  0.0099  -0.0477 507  ASP A CB    
4085 C  CG    . ASP A 506 ? 0.5021 0.6602 0.9269 0.0497  0.0103  -0.0436 507  ASP A CG    
4086 O  OD1   . ASP A 506 ? 0.5128 0.6685 0.9396 0.0466  0.01    -0.0397 507  ASP A OD1   
4087 O  OD2   . ASP A 506 ? 0.5396 0.701  0.9647 0.0527  0.0109  -0.0442 507  ASP A OD2   
4088 N  N     . ASN A 507 ? 0.4171 0.5778 0.8407 0.0487  0.0112  -0.0384 508  ASN A N     
4089 C  CA    . ASN A 507 ? 0.4302 0.5926 0.8554 0.048   0.0118  -0.0331 508  ASN A CA    
4090 C  C     . ASN A 507 ? 0.4277 0.5877 0.8562 0.0452  0.0111  -0.0286 508  ASN A C     
4091 O  O     . ASN A 507 ? 0.4307 0.59   0.8606 0.0434  0.0109  -0.0244 508  ASN A O     
4092 C  CB    . ASN A 507 ? 0.4568 0.6272 0.882  0.0526  0.0135  -0.0311 508  ASN A CB    
4093 C  CG    . ASN A 507 ? 0.5167 0.6891 0.94   0.0535  0.0142  -0.0313 508  ASN A CG    
4094 O  OD1   . ASN A 507 ? 0.5379 0.7152 0.9623 0.0554  0.0154  -0.0274 508  ASN A OD1   
4095 N  ND2   . ASN A 507 ? 0.5295 0.6981 0.9501 0.0522  0.0134  -0.0357 508  ASN A ND2   
4096 N  N     . VAL A 508 ? 0.4201 0.5787 0.8498 0.0448  0.0107  -0.0293 509  VAL A N     
4097 C  CA    . VAL A 508 ? 0.414  0.5711 0.8471 0.0424  0.01    -0.0249 509  VAL A CA    
4098 C  C     . VAL A 508 ? 0.403  0.5536 0.8363 0.039   0.0085  -0.027  509  VAL A C     
4099 O  O     . VAL A 508 ? 0.4036 0.5503 0.8387 0.0356  0.0074  -0.0241 509  VAL A O     
4100 C  CB    . VAL A 508 ? 0.421  0.585  0.8564 0.046   0.0115  -0.0214 509  VAL A CB    
4101 C  CG1   . VAL A 508 ? 0.4302 0.597  0.8639 0.0496  0.0123  -0.0256 509  VAL A CG1   
4102 C  CG2   . VAL A 508 ? 0.4256 0.5886 0.8649 0.0437  0.0108  -0.0166 509  VAL A CG2   
4103 N  N     . HIS A 509 ? 0.3904 0.5395 0.8218 0.0399  0.0085  -0.0321 510  HIS A N     
4104 C  CA    . HIS A 509 ? 0.3863 0.5298 0.8182 0.0371  0.0073  -0.034  510  HIS A CA    
4105 C  C     . HIS A 509 ? 0.3582 0.4964 0.7878 0.0353  0.0064  -0.0389 510  HIS A C     
4106 O  O     . HIS A 509 ? 0.3579 0.4972 0.7852 0.0368  0.0067  -0.042  510  HIS A O     
4107 C  CB    . HIS A 509 ? 0.4144 0.5606 0.8475 0.0394  0.0079  -0.0349 510  HIS A CB    
4108 C  CG    . HIS A 509 ? 0.4752 0.6263 0.9111 0.0411  0.0088  -0.0298 510  HIS A CG    
4109 N  ND1   . HIS A 509 ? 0.5044 0.6625 0.94   0.0457  0.0105  -0.029  510  HIS A ND1   
4110 C  CD2   . HIS A 509 ? 0.4992 0.6493 0.9382 0.0388  0.0083  -0.0254 510  HIS A CD2   
4111 C  CE1   . HIS A 509 ? 0.5155 0.6766 0.9542 0.0461  0.011   -0.0239 510  HIS A CE1   
4112 N  NE2   . HIS A 509 ? 0.5156 0.6722 0.9566 0.0419  0.0097  -0.0215 510  HIS A NE2   
4113 N  N     . GLU A 510 ? 0.3329 0.4655 0.7632 0.0321  0.0052  -0.0396 511  GLU A N     
4114 C  CA    . GLU A 510 ? 0.3169 0.4444 0.7457 0.0305  0.0044  -0.0439 511  GLU A CA    
4115 C  C     . GLU A 510 ? 0.3023 0.4293 0.7326 0.0309  0.0043  -0.0457 511  GLU A C     
4116 O  O     . GLU A 510 ? 0.3038 0.4295 0.7361 0.0293  0.004   -0.043  511  GLU A O     
4117 C  CB    . GLU A 510 ? 0.3367 0.4578 0.765  0.0266  0.0032  -0.0427 511  GLU A CB    
4118 C  CG    . GLU A 510 ? 0.3597 0.4758 0.7866 0.0251  0.0025  -0.0469 511  GLU A CG    
4119 C  CD    . GLU A 510 ? 0.3988 0.5084 0.825  0.0216  0.0013  -0.0459 511  GLU A CD    
4120 O  OE1   . GLU A 510 ? 0.4132 0.5216 0.8391 0.0202  0.0008  -0.0423 511  GLU A OE1   
4121 O  OE2   . GLU A 510 ? 0.3957 0.5012 0.8214 0.0204  0.0009  -0.0486 511  GLU A OE2   
4122 N  N     . PHE A 511 ? 0.2873 0.4155 0.7167 0.033   0.0046  -0.05   512  PHE A N     
4123 C  CA    . PHE A 511 ? 0.278  0.4055 0.7086 0.0336  0.0045  -0.0524 512  PHE A CA    
4124 C  C     . PHE A 511 ? 0.2619 0.3835 0.6923 0.031   0.0035  -0.0556 512  PHE A C     
4125 O  O     . PHE A 511 ? 0.2609 0.3811 0.6896 0.0306  0.0032  -0.0579 512  PHE A O     
4126 C  CB    . PHE A 511 ? 0.2812 0.4133 0.7107 0.0377  0.0053  -0.0554 512  PHE A CB    
4127 C  CG    . PHE A 511 ? 0.2948 0.4332 0.7242 0.0409  0.0065  -0.0523 512  PHE A CG    
4128 C  CD1   . PHE A 511 ? 0.3088 0.4501 0.7398 0.0424  0.0073  -0.0494 512  PHE A CD1   
4129 C  CD2   . PHE A 511 ? 0.3087 0.4503 0.7362 0.0425  0.0069  -0.0521 512  PHE A CD2   
4130 C  CE1   . PHE A 511 ? 0.3169 0.4643 0.7479 0.0456  0.0085  -0.0462 512  PHE A CE1   
4131 C  CE2   . PHE A 511 ? 0.3191 0.4666 0.7466 0.0456  0.0082  -0.0489 512  PHE A CE2   
4132 C  CZ    . PHE A 511 ? 0.3152 0.4658 0.7446 0.0472  0.009   -0.0459 512  PHE A CZ    
4133 N  N     . ARG A 512 ? 0.2446 0.3631 0.6768 0.0293  0.0031  -0.0556 513  ARG A N     
4134 C  CA    . ARG A 512 ? 0.236  0.3491 0.6684 0.0269  0.0022  -0.0582 513  ARG A CA    
4135 C  C     . ARG A 512 ? 0.2265 0.3384 0.6607 0.0272  0.0022  -0.0606 513  ARG A C     
4136 O  O     . ARG A 512 ? 0.2227 0.3356 0.6586 0.0274  0.0025  -0.0587 513  ARG A O     
4137 C  CB    . ARG A 512 ? 0.244  0.3526 0.6764 0.0234  0.0015  -0.0551 513  ARG A CB    
4138 C  CG    . ARG A 512 ? 0.2654 0.3684 0.6975 0.021   0.0008  -0.0573 513  ARG A CG    
4139 C  CD    . ARG A 512 ? 0.2932 0.3922 0.724  0.0184  0.0001  -0.0546 513  ARG A CD    
4140 N  NE    . ARG A 512 ? 0.3138 0.4076 0.7443 0.0164  -0.0005 -0.0563 513  ARG A NE    
4141 C  CZ    . ARG A 512 ? 0.3258 0.4179 0.7549 0.0164  -0.0005 -0.0586 513  ARG A CZ    
4142 N  NH1   . ARG A 512 ? 0.3232 0.4184 0.7508 0.0181  -0.0001 -0.0597 513  ARG A NH1   
4143 N  NH2   . ARG A 512 ? 0.3131 0.4006 0.7421 0.0148  -0.0009 -0.0596 513  ARG A NH2   
4144 N  N     . TRP A 513 ? 0.2173 0.3272 0.6515 0.0272  0.0017  -0.0648 514  TRP A N     
4145 C  CA    . TRP A 513 ? 0.2175 0.3256 0.6537 0.0272  0.0014  -0.0674 514  TRP A CA    
4146 C  C     . TRP A 513 ? 0.2106 0.3133 0.6478 0.0239  0.0008  -0.0671 514  TRP A C     
4147 O  O     . TRP A 513 ? 0.2203 0.3207 0.6564 0.0227  0.0004  -0.068  514  TRP A O     
4148 C  CB    . TRP A 513 ? 0.2237 0.3329 0.6596 0.0293  0.001   -0.0722 514  TRP A CB    
4149 C  CG    . TRP A 513 ? 0.2365 0.3505 0.6713 0.0331  0.0015  -0.0734 514  TRP A CG    
4150 C  CD1   . TRP A 513 ? 0.2467 0.3619 0.6824 0.0352  0.0017  -0.0751 514  TRP A CD1   
4151 C  CD2   . TRP A 513 ? 0.2422 0.3606 0.6746 0.0354  0.0019  -0.0729 514  TRP A CD2   
4152 N  NE1   . TRP A 513 ? 0.2508 0.3708 0.6845 0.0389  0.0021  -0.0758 514  TRP A NE1   
4153 C  CE2   . TRP A 513 ? 0.252  0.3742 0.6838 0.0391  0.0023  -0.0744 514  TRP A CE2   
4154 C  CE3   . TRP A 513 ? 0.2571 0.3767 0.6878 0.0349  0.0021  -0.0713 514  TRP A CE3   
4155 C  CZ2   . TRP A 513 ? 0.2643 0.3915 0.6938 0.0424  0.0029  -0.0742 514  TRP A CZ2   
4156 C  CZ3   . TRP A 513 ? 0.2729 0.3975 0.7017 0.038   0.0027  -0.0711 514  TRP A CZ3   
4157 C  CH2   . TRP A 513 ? 0.2723 0.4007 0.7005 0.0417  0.0031  -0.0725 514  TRP A CH2   
4158 N  N     . LEU A 514 ? 0.1993 0.2999 0.6384 0.0226  0.0009  -0.0657 515  LEU A N     
4159 C  CA    . LEU A 514 ? 0.2    0.2956 0.6401 0.0197  0.0004  -0.0653 515  LEU A CA    
4160 C  C     . LEU A 514 ? 0.1964 0.2905 0.639  0.0199  0.0003  -0.0685 515  LEU A C     
4161 O  O     . LEU A 514 ? 0.2    0.2966 0.6433 0.0221  0.0005  -0.0707 515  LEU A O     
4162 C  CB    . LEU A 514 ? 0.2037 0.2983 0.6445 0.018   0.0004  -0.0612 515  LEU A CB    
4163 C  CG    . LEU A 514 ? 0.2169 0.3131 0.656  0.0177  0.0003  -0.0575 515  LEU A CG    
4164 C  CD1   . LEU A 514 ? 0.2227 0.3185 0.6632 0.0163  0.0002  -0.0536 515  LEU A CD1   
4165 C  CD2   . LEU A 514 ? 0.221  0.3142 0.6578 0.0161  -0.0003 -0.0572 515  LEU A CD2   
4166 N  N     . SER A 515 ? 0.1896 0.2793 0.6334 0.0176  -0.0001 -0.0686 516  SER A N     
4167 C  CA    . SER A 515 ? 0.1934 0.2812 0.6401 0.0175  -0.0002 -0.0711 516  SER A CA    
4168 C  C     . SER A 515 ? 0.2044 0.2937 0.6517 0.0193  -0.0005 -0.0753 516  SER A C     
4169 O  O     . SER A 515 ? 0.2041 0.2947 0.653  0.0209  -0.0005 -0.0775 516  SER A O     
4170 C  CB    . SER A 515 ? 0.2031 0.2916 0.6518 0.0178  0.0003  -0.07   516  SER A CB    
4171 O  OG    . SER A 515 ? 0.2184 0.3057 0.6667 0.0161  0.0005  -0.0661 516  SER A OG    
4172 N  N     . LEU A 516 ? 0.2105 0.2996 0.6565 0.0192  -0.001  -0.0764 517  LEU A N     
4173 C  CA    . LEU A 516 ? 0.218  0.3085 0.6646 0.0206  -0.0016 -0.0802 517  LEU A CA    
4174 C  C     . LEU A 516 ? 0.23   0.3173 0.68   0.0195  -0.0021 -0.0823 517  LEU A C     
4175 O  O     . LEU A 516 ? 0.2344 0.3187 0.6851 0.0175  -0.0021 -0.0811 517  LEU A O     
4176 C  CB    . LEU A 516 ? 0.223  0.3143 0.667  0.0207  -0.0019 -0.0802 517  LEU A CB    
4177 C  CG    . LEU A 516 ? 0.2441 0.3383 0.6849 0.0215  -0.0013 -0.0779 517  LEU A CG    
4178 C  CD1   . LEU A 516 ? 0.2412 0.3363 0.6799 0.0218  -0.0016 -0.0785 517  LEU A CD1   
4179 C  CD2   . LEU A 516 ? 0.2523 0.3507 0.6925 0.0242  -0.001  -0.0784 517  LEU A CD2   
4180 N  N     . PRO A 517 ? 0.232  0.32   0.6842 0.0209  -0.0027 -0.0854 518  PRO A N     
4181 C  CA    . PRO A 517 ? 0.2339 0.319  0.69   0.0198  -0.0033 -0.0874 518  PRO A CA    
4182 C  C     . PRO A 517 ? 0.2421 0.3269 0.6988 0.0194  -0.0042 -0.0891 518  PRO A C     
4183 O  O     . PRO A 517 ? 0.2415 0.3288 0.6957 0.0206  -0.0046 -0.0899 518  PRO A O     
4184 C  CB    . PRO A 517 ? 0.2371 0.3232 0.6949 0.0217  -0.0037 -0.0902 518  PRO A CB    
4185 C  CG    . PRO A 517 ? 0.2374 0.3273 0.6917 0.0243  -0.0037 -0.0909 518  PRO A CG    
4186 C  CD    . PRO A 517 ? 0.2225 0.3137 0.6737 0.0237  -0.0028 -0.0872 518  PRO A CD    
4187 N  N     . ARG A 518 ? 0.2469 0.3289 0.7071 0.0178  -0.0046 -0.0896 519  ARG A N     
4188 C  CA    . ARG A 518 ? 0.2567 0.3384 0.7183 0.0173  -0.0054 -0.0909 519  ARG A CA    
4189 C  C     . ARG A 518 ? 0.2597 0.3437 0.7218 0.0191  -0.0069 -0.0948 519  ARG A C     
4190 O  O     . ARG A 518 ? 0.253  0.3386 0.714  0.0195  -0.0076 -0.0957 519  ARG A O     
4191 C  CB    . ARG A 518 ? 0.2804 0.3589 0.7464 0.0156  -0.0055 -0.0904 519  ARG A CB    
4192 C  CG    . ARG A 518 ? 0.3407 0.4188 0.8083 0.0148  -0.0061 -0.0907 519  ARG A CG    
4193 C  CD    . ARG A 518 ? 0.4059 0.4816 0.879  0.0136  -0.0063 -0.0907 519  ARG A CD    
4194 N  NE    . ARG A 518 ? 0.4575 0.5329 0.9344 0.0141  -0.0074 -0.0936 519  ARG A NE    
4195 C  CZ    . ARG A 518 ? 0.4871 0.5634 0.9668 0.0147  -0.0091 -0.0968 519  ARG A CZ    
4196 N  NH1   . ARG A 518 ? 0.4705 0.5481 0.95   0.0147  -0.01   -0.0974 519  ARG A NH1   
4197 N  NH2   . ARG A 518 ? 0.4939 0.5696 0.9766 0.0152  -0.0101 -0.0995 519  ARG A NH2   
4198 N  N     . VAL A 519 ? 0.2671 0.3515 0.7306 0.0204  -0.0075 -0.0971 520  VAL A N     
4199 C  CA    . VAL A 519 ? 0.2869 0.3731 0.7503 0.0225  -0.0091 -0.1011 520  VAL A CA    
4200 C  C     . VAL A 519 ? 0.3121 0.3999 0.7734 0.0248  -0.0088 -0.1022 520  VAL A C     
4201 O  O     . VAL A 519 ? 0.3203 0.4072 0.7817 0.0246  -0.0076 -0.1002 520  VAL A O     
4202 C  CB    . VAL A 519 ? 0.2898 0.3739 0.7585 0.0217  -0.0108 -0.104  520  VAL A CB    
4203 C  CG1   . VAL A 519 ? 0.2984 0.3817 0.7693 0.0199  -0.0112 -0.1032 520  VAL A CG1   
4204 C  CG2   . VAL A 519 ? 0.294  0.3753 0.7663 0.0209  -0.0103 -0.1036 520  VAL A CG2   
4205 N  N     . SER A 520 ? 0.3231 0.4133 0.7824 0.0273  -0.0099 -0.1052 521  SER A N     
4206 C  CA    . SER A 520 ? 0.3404 0.4321 0.7977 0.0302  -0.0099 -0.1069 521  SER A CA    
4207 C  C     . SER A 520 ? 0.3513 0.4418 0.8108 0.0314  -0.0123 -0.1118 521  SER A C     
4208 O  O     . SER A 520 ? 0.3473 0.4359 0.8104 0.0296  -0.0137 -0.1131 521  SER A O     
4209 C  CB    . SER A 520 ? 0.3604 0.4562 0.8127 0.0325  -0.0092 -0.1059 521  SER A CB    
4210 O  OG    . SER A 520 ? 0.3883 0.4861 0.8389 0.0339  -0.0106 -0.1086 521  SER A OG    
4211 N  N     . GLU A 521 ? 0.3616 0.453  0.8192 0.0344  -0.0128 -0.1144 522  GLU A N     
4212 C  CA    . GLU A 521 ? 0.3749 0.4646 0.8343 0.0356  -0.0153 -0.1192 522  GLU A CA    
4213 C  C     . GLU A 521 ? 0.3702 0.4607 0.8298 0.0354  -0.0175 -0.1218 522  GLU A C     
4214 O  O     . GLU A 521 ? 0.3752 0.4632 0.8391 0.0339  -0.0194 -0.124  522  GLU A O     
4215 C  CB    . GLU A 521 ? 0.4221 0.5128 0.8783 0.0395  -0.0154 -0.1215 522  GLU A CB    
4216 C  CG    . GLU A 521 ? 0.5191 0.6074 0.9767 0.0409  -0.0182 -0.1266 522  GLU A CG    
4217 C  CD    . GLU A 521 ? 0.6338 0.7178 1.0963 0.0394  -0.0186 -0.1275 522  GLU A CD    
4218 O  OE1   . GLU A 521 ? 0.656  0.739  1.1207 0.0373  -0.0166 -0.1239 522  GLU A OE1   
4219 O  OE2   . GLU A 521 ? 0.6714 0.753  1.1355 0.0403  -0.021  -0.1317 522  GLU A OE2   
4220 N  N     . ASN A 522 ? 0.3623 0.4564 0.8178 0.0368  -0.0171 -0.1212 523  ASN A N     
4221 C  CA    . ASN A 522 ? 0.3559 0.4514 0.8113 0.0367  -0.019  -0.1232 523  ASN A CA    
4222 C  C     . ASN A 522 ? 0.3281 0.4255 0.7827 0.0349  -0.0177 -0.1197 523  ASN A C     
4223 O  O     . ASN A 522 ? 0.3248 0.4239 0.7789 0.035   -0.0189 -0.1209 523  ASN A O     
4224 C  CB    . ASN A 522 ? 0.3869 0.4852 0.8378 0.0406  -0.0202 -0.1265 523  ASN A CB    
4225 C  CG    . ASN A 522 ? 0.4537 0.5497 0.9054 0.0426  -0.0224 -0.1309 523  ASN A CG    
4226 O  OD1   . ASN A 522 ? 0.4713 0.5669 0.9212 0.0447  -0.0214 -0.1311 523  ASN A OD1   
4227 N  ND2   . ASN A 522 ? 0.4692 0.5636 0.9235 0.0419  -0.0254 -0.1345 523  ASN A ND2   
4228 N  N     . GLY A 523 ? 0.3076 0.4046 0.7619 0.0333  -0.0153 -0.1155 524  GLY A N     
4229 C  CA    . GLY A 523 ? 0.2862 0.3845 0.7393 0.0317  -0.014  -0.1121 524  GLY A CA    
4230 C  C     . GLY A 523 ? 0.2546 0.3499 0.7108 0.0284  -0.013  -0.1091 524  GLY A C     
4231 O  O     . GLY A 523 ? 0.2593 0.3517 0.7187 0.0271  -0.0127 -0.1086 524  GLY A O     
4232 N  N     . LYS A 524 ? 0.2189 0.3151 0.6741 0.0272  -0.0124 -0.1069 525  LYS A N     
4233 C  CA    . LYS A 524 ? 0.201  0.2946 0.6582 0.0244  -0.0112 -0.1036 525  LYS A CA    
4234 C  C     . LYS A 524 ? 0.167  0.2618 0.6199 0.0243  -0.0094 -0.0999 525  LYS A C     
4235 O  O     . LYS A 524 ? 0.1602 0.2581 0.6099 0.0257  -0.0093 -0.1    525  LYS A O     
4236 C  CB    . LYS A 524 ? 0.2354 0.3281 0.6959 0.0229  -0.0124 -0.1044 525  LYS A CB    
4237 C  CG    . LYS A 524 ? 0.32   0.4103 0.7857 0.0222  -0.0141 -0.1069 525  LYS A CG    
4238 C  CD    . LYS A 524 ? 0.4081 0.4966 0.8782 0.02    -0.0144 -0.1056 525  LYS A CD    
4239 C  CE    . LYS A 524 ? 0.467  0.5527 0.9429 0.0189  -0.0154 -0.1069 525  LYS A CE    
4240 N  NZ    . LYS A 524 ? 0.506  0.5922 0.9834 0.0203  -0.0179 -0.1114 525  LYS A NZ    
4241 N  N     . ARG A 525 ? 0.1455 0.238  0.5987 0.0226  -0.0079 -0.0967 526  ARG A N     
4242 C  CA    . ARG A 525 ? 0.1365 0.2295 0.586  0.0223  -0.0064 -0.0932 526  ARG A CA    
4243 C  C     . ARG A 525 ? 0.1343 0.2276 0.5824 0.0216  -0.0063 -0.0921 526  ARG A C     
4244 O  O     . ARG A 525 ? 0.1368 0.2279 0.5874 0.02    -0.0065 -0.0917 526  ARG A O     
4245 C  CB    . ARG A 525 ? 0.1344 0.2242 0.5847 0.0205  -0.0053 -0.0903 526  ARG A CB    
4246 C  CG    . ARG A 525 ? 0.137  0.2269 0.5836 0.02    -0.0041 -0.0867 526  ARG A CG    
4247 C  CD    . ARG A 525 ? 0.1607 0.2473 0.6081 0.0182  -0.0033 -0.084  526  ARG A CD    
4248 N  NE    . ARG A 525 ? 0.1907 0.274  0.6405 0.0165  -0.0034 -0.0836 526  ARG A NE    
4249 C  CZ    . ARG A 525 ? 0.2171 0.2973 0.6691 0.0152  -0.0031 -0.0825 526  ARG A CZ    
4250 N  NH1   . ARG A 525 ? 0.2024 0.2825 0.6547 0.0152  -0.0027 -0.0817 526  ARG A NH1   
4251 N  NH2   . ARG A 525 ? 0.2207 0.2983 0.6748 0.014   -0.0031 -0.082  526  ARG A NH2   
4252 N  N     . PRO A 526 ? 0.1331 0.2295 0.5776 0.0229  -0.0059 -0.0916 527  PRO A N     
4253 C  CA    . PRO A 526 ? 0.1343 0.231  0.5773 0.0224  -0.0057 -0.0903 527  PRO A CA    
4254 C  C     . PRO A 526 ? 0.1344 0.2278 0.5763 0.0204  -0.0044 -0.0867 527  PRO A C     
4255 O  O     . PRO A 526 ? 0.1339 0.2256 0.575  0.0198  -0.0037 -0.0847 527  PRO A O     
4256 C  CB    . PRO A 526 ? 0.1418 0.2427 0.581  0.0244  -0.0054 -0.0904 527  PRO A CB    
4257 C  CG    . PRO A 526 ? 0.141  0.244  0.5799 0.0263  -0.0056 -0.092  527  PRO A CG    
4258 C  CD    . PRO A 526 ? 0.1242 0.2239 0.5657 0.025   -0.0055 -0.0915 527  PRO A CD    
4259 N  N     . ASP A 527 ? 0.1351 0.2274 0.5768 0.0196  -0.0043 -0.0857 528  ASP A N     
4260 C  CA    . ASP A 527 ? 0.1461 0.2351 0.586  0.0182  -0.0031 -0.0823 528  ASP A CA    
4261 C  C     . ASP A 527 ? 0.1535 0.2434 0.5888 0.0187  -0.0023 -0.0801 528  ASP A C     
4262 O  O     . ASP A 527 ? 0.155  0.2422 0.5886 0.0177  -0.0016 -0.0775 528  ASP A O     
4263 C  CB    . ASP A 527 ? 0.1884 0.2761 0.629  0.0175  -0.003  -0.0817 528  ASP A CB    
4264 C  CG    . ASP A 527 ? 0.2585 0.3449 0.7041 0.0168  -0.0038 -0.0831 528  ASP A CG    
4265 O  OD1   . ASP A 527 ? 0.266  0.3513 0.7143 0.0163  -0.0042 -0.0841 528  ASP A OD1   
4266 O  OD2   . ASP A 527 ? 0.3285 0.415  0.7755 0.0166  -0.004  -0.083  528  ASP A OD2   
4267 N  N     . HIS A 528 ? 0.1545 0.2484 0.588  0.0203  -0.0024 -0.081  529  HIS A N     
4268 C  CA    . HIS A 528 ? 0.1557 0.2512 0.5854 0.021   -0.0015 -0.0789 529  HIS A CA    
4269 C  C     . HIS A 528 ? 0.1483 0.2488 0.5775 0.0232  -0.0018 -0.0807 529  HIS A C     
4270 O  O     . HIS A 528 ? 0.1508 0.2537 0.5813 0.0244  -0.0027 -0.0836 529  HIS A O     
4271 C  CB    . HIS A 528 ? 0.1688 0.2637 0.5959 0.0208  -0.0009 -0.0772 529  HIS A CB    
4272 C  CG    . HIS A 528 ? 0.198  0.288  0.625  0.0191  -0.0005 -0.0752 529  HIS A CG    
4273 N  ND1   . HIS A 528 ? 0.2176 0.304  0.6426 0.0179  0       -0.0726 529  HIS A ND1   
4274 C  CD2   . HIS A 528 ? 0.2051 0.2934 0.6336 0.0185  -0.0005 -0.0755 529  HIS A CD2   
4275 C  CE1   . HIS A 528 ? 0.2277 0.3102 0.6527 0.0169  0.0002  -0.0715 529  HIS A CE1   
4276 N  NE2   . HIS A 528 ? 0.2196 0.3032 0.6467 0.0173  0       -0.0731 529  HIS A NE2   
4277 N  N     . VAL A 529 ? 0.1354 0.2375 0.5626 0.024   -0.0012 -0.079  530  VAL A N     
4278 C  CA    . VAL A 529 ? 0.1387 0.2459 0.5648 0.0265  -0.0012 -0.0801 530  VAL A CA    
4279 C  C     . VAL A 529 ? 0.1428 0.2514 0.5657 0.0268  -0.0001 -0.077  530  VAL A C     
4280 O  O     . VAL A 529 ? 0.1348 0.2409 0.5567 0.0255  0.0004  -0.0739 530  VAL A O     
4281 C  CB    . VAL A 529 ? 0.1493 0.258  0.5764 0.0276  -0.0013 -0.0807 530  VAL A CB    
4282 C  CG1   . VAL A 529 ? 0.1601 0.2742 0.5857 0.0307  -0.0012 -0.0818 530  VAL A CG1   
4283 C  CG2   . VAL A 529 ? 0.144  0.2507 0.5744 0.0271  -0.0023 -0.0835 530  VAL A CG2   
4284 N  N     . ILE A 530 ? 0.1427 0.2548 0.5641 0.0285  0       -0.0779 531  ILE A N     
4285 C  CA    . ILE A 530 ? 0.1555 0.2692 0.5742 0.0289  0.001   -0.0751 531  ILE A CA    
4286 C  C     . ILE A 530 ? 0.1715 0.2908 0.5892 0.0317  0.0015  -0.0751 531  ILE A C     
4287 O  O     . ILE A 530 ? 0.1746 0.2973 0.5926 0.0337  0.0009  -0.0781 531  ILE A O     
4288 C  CB    . ILE A 530 ? 0.153  0.2664 0.5705 0.0287  0.0012  -0.0754 531  ILE A CB    
4289 C  CG1   . ILE A 530 ? 0.1641 0.2725 0.5829 0.0264  0.0008  -0.0757 531  ILE A CG1   
4290 C  CG2   . ILE A 530 ? 0.1504 0.2645 0.565  0.0289  0.0023  -0.0723 531  ILE A CG2   
4291 C  CD1   . ILE A 530 ? 0.1811 0.2844 0.5992 0.0244  0.0012  -0.0728 531  ILE A CD1   
4292 N  N     . GLN A 531 ? 0.1781 0.2983 0.5945 0.0319  0.0023  -0.0718 532  GLN A N     
4293 C  CA    . GLN A 531 ? 0.1934 0.3193 0.609  0.0347  0.003   -0.0713 532  GLN A CA    
4294 C  C     . GLN A 531 ? 0.2116 0.3399 0.625  0.0356  0.0039  -0.0694 532  GLN A C     
4295 O  O     . GLN A 531 ? 0.218  0.3435 0.6305 0.0338  0.0044  -0.0664 532  GLN A O     
4296 C  CB    . GLN A 531 ? 0.1973 0.3238 0.6137 0.0349  0.0034  -0.0686 532  GLN A CB    
4297 C  CG    . GLN A 531 ? 0.2204 0.3532 0.6361 0.0383  0.0042  -0.0678 532  GLN A CG    
4298 C  CD    . GLN A 531 ? 0.2675 0.4017 0.6845 0.0388  0.0047  -0.0651 532  GLN A CD    
4299 O  OE1   . GLN A 531 ? 0.2983 0.4285 0.7166 0.0364  0.0044  -0.0633 532  GLN A OE1   
4300 N  NE2   . GLN A 531 ? 0.2469 0.3867 0.6634 0.0421  0.0055  -0.0645 532  GLN A NE2   
4301 N  N     . ILE A 532 ? 0.2221 0.3556 0.6346 0.0383  0.0041  -0.0712 533  ILE A N     
4302 C  CA    . ILE A 532 ? 0.2457 0.3822 0.6563 0.0394  0.0051  -0.0694 533  ILE A CA    
4303 C  C     . ILE A 532 ? 0.2776 0.4203 0.6875 0.0427  0.0059  -0.0684 533  ILE A C     
4304 O  O     . ILE A 532 ? 0.2775 0.4238 0.6875 0.0452  0.0054  -0.0713 533  ILE A O     
4305 C  CB    . ILE A 532 ? 0.2399 0.3766 0.6496 0.0395  0.0047  -0.0718 533  ILE A CB    
4306 C  CG1   . ILE A 532 ? 0.2535 0.3841 0.6637 0.0364  0.0042  -0.0718 533  ILE A CG1   
4307 C  CG2   . ILE A 532 ? 0.2341 0.3747 0.6418 0.0411  0.0058  -0.0701 533  ILE A CG2   
4308 C  CD1   . ILE A 532 ? 0.2649 0.3954 0.6756 0.0363  0.0034  -0.0746 533  ILE A CD1   
4309 N  N     . LEU A 533 ? 0.3019 0.4459 0.7114 0.0429  0.0071  -0.0643 534  LEU A N     
4310 C  CA    . LEU A 533 ? 0.3304 0.4806 0.7398 0.0461  0.0081  -0.0627 534  LEU A CA    
4311 C  C     . LEU A 533 ? 0.3551 0.5102 0.7627 0.0484  0.0092  -0.0617 534  LEU A C     
4312 O  O     . LEU A 533 ? 0.3574 0.5183 0.7648 0.0517  0.01    -0.0608 534  LEU A O     
4313 C  CB    . LEU A 533 ? 0.3382 0.4874 0.749  0.0451  0.0086  -0.0584 534  LEU A CB    
4314 C  CG    . LEU A 533 ? 0.37   0.5156 0.7826 0.0434  0.0077  -0.0589 534  LEU A CG    
4315 C  CD1   . LEU A 533 ? 0.3799 0.5192 0.7931 0.0395  0.0072  -0.0567 534  LEU A CD1   
4316 C  CD2   . LEU A 533 ? 0.3855 0.5352 0.7994 0.0457  0.0084  -0.0569 534  LEU A CD2   
4317 N  N     . ASP A 534 ? 0.368  0.5211 0.7745 0.047   0.0093  -0.0615 535  ASP A N     
4318 C  CA    . ASP A 534 ? 0.3821 0.5397 0.787  0.049   0.0105  -0.0601 535  ASP A CA    
4319 C  C     . ASP A 534 ? 0.3937 0.5535 0.7973 0.0504  0.0101  -0.0638 535  ASP A C     
4320 O  O     . ASP A 534 ? 0.399  0.5599 0.8012 0.0505  0.0108  -0.0629 535  ASP A O     
4321 C  CB    . ASP A 534 ? 0.409  0.563  0.8134 0.0466  0.0113  -0.0564 535  ASP A CB    
4322 N  N     . LEU A 535 ? 0.391  0.5516 0.795  0.0514  0.0088  -0.0679 536  LEU A N     
4323 C  CA    . LEU A 535 ? 0.3935 0.556  0.7966 0.0526  0.0079  -0.0716 536  LEU A CA    
4324 C  C     . LEU A 535 ? 0.404  0.5725 0.8063 0.0566  0.0075  -0.0741 536  LEU A C     
4325 O  O     . LEU A 535 ? 0.4074 0.5809 0.8081 0.0592  0.0081  -0.0743 536  LEU A O     
4326 C  CB    . LEU A 535 ? 0.388  0.545  0.7924 0.0497  0.0063  -0.0745 536  LEU A CB    
4327 C  CG    . LEU A 535 ? 0.3965 0.555  0.8009 0.0505  0.0049  -0.0785 536  LEU A CG    
4328 C  CD1   . LEU A 535 ? 0.3969 0.5584 0.7996 0.0513  0.0057  -0.0775 536  LEU A CD1   
4329 C  CD2   . LEU A 535 ? 0.406  0.5587 0.8124 0.0474  0.0035  -0.0804 536  LEU A CD2   
4330 N  N     . PHE A 536 ? 0.4062 0.5741 0.8093 0.0574  0.0067  -0.0759 537  PHE A N     
4331 C  CA    . PHE A 536 ? 0.4139 0.587  0.8159 0.0615  0.0062  -0.0784 537  PHE A CA    
4332 C  C     . PHE A 536 ? 0.426  0.6024 0.8279 0.0638  0.0078  -0.075  537  PHE A C     
4333 O  O     . PHE A 536 ? 0.433  0.6071 0.8363 0.0617  0.0088  -0.0711 537  PHE A O     
4334 C  CB    . PHE A 536 ? 0.4102 0.5803 0.813  0.0611  0.0041  -0.083  537  PHE A CB    
4335 C  CG    . PHE A 536 ? 0.4183 0.5853 0.8219 0.0588  0.0024  -0.0861 537  PHE A CG    
4336 C  CD1   . PHE A 536 ? 0.4275 0.5979 0.8298 0.0604  0.0018  -0.0882 537  PHE A CD1   
4337 C  CD2   . PHE A 536 ? 0.4274 0.5883 0.8333 0.0552  0.0014  -0.0869 537  PHE A CD2   
4338 C  CE1   . PHE A 536 ? 0.4354 0.6032 0.8388 0.0583  0.0002  -0.0907 537  PHE A CE1   
4339 C  CE2   . PHE A 536 ? 0.435  0.5933 0.842  0.0532  0       -0.0894 537  PHE A CE2   
4340 C  CZ    . PHE A 536 ? 0.4331 0.5949 0.8391 0.0547  -0.0007 -0.0912 537  PHE A CZ    
4341 N  N     . GLU A 537 ? 0.4244 0.6061 0.8247 0.0682  0.0079  -0.0764 538  GLU A N     
4342 C  CA    . GLU A 537 ? 0.429  0.6143 0.8294 0.0709  0.0094  -0.0732 538  GLU A CA    
4343 C  C     . GLU A 537 ? 0.4216 0.6023 0.824  0.0688  0.0089  -0.0729 538  GLU A C     
4344 O  O     . GLU A 537 ? 0.4257 0.6065 0.8297 0.0681  0.0102  -0.0686 538  GLU A O     
4345 C  CB    . GLU A 537 ? 0.4715 0.663  0.8693 0.0764  0.0094  -0.0755 538  GLU A CB    
4346 C  CG    . GLU A 537 ? 0.5638 0.7538 0.9603 0.0773  0.007   -0.0816 538  GLU A CG    
4347 C  CD    . GLU A 537 ? 0.6804 0.876  1.0739 0.0829  0.0068  -0.084  538  GLU A CD    
4348 O  OE1   . GLU A 537 ? 0.7117 0.9129 1.1034 0.0859  0.0079  -0.0827 538  GLU A OE1   
4349 O  OE2   . GLU A 537 ? 0.713  0.9073 1.1058 0.0845  0.0055  -0.0872 538  GLU A OE2   
4350 N  N     . LYS A 538 ? 0.4034 0.5801 0.8062 0.0675  0.007   -0.0772 539  LYS A N     
4351 C  CA    . LYS A 538 ? 0.3883 0.5603 0.7931 0.0653  0.0064  -0.0774 539  LYS A CA    
4352 C  C     . LYS A 538 ? 0.3754 0.541  0.7821 0.0601  0.0058  -0.0768 539  LYS A C     
4353 O  O     . LYS A 538 ? 0.3796 0.5437 0.786  0.0587  0.005   -0.0786 539  LYS A O     
4354 C  CB    . LYS A 538 ? 0.4015 0.5727 0.8056 0.067   0.0046  -0.0826 539  LYS A CB    
4355 C  CG    . LYS A 538 ? 0.4382 0.6151 0.8397 0.0725  0.0049  -0.0839 539  LYS A CG    
4356 C  CD    . LYS A 538 ? 0.477  0.652  0.8777 0.0739  0.0028  -0.0894 539  LYS A CD    
4357 C  CE    . LYS A 538 ? 0.507  0.6872 0.9045 0.0797  0.003   -0.0908 539  LYS A CE    
4358 N  NZ    . LYS A 538 ? 0.5222 0.7    0.9187 0.0812  0.0009  -0.0961 539  LYS A NZ    
4359 N  N     . PRO A 539 ? 0.3503 0.512  0.7591 0.0575  0.006   -0.0744 540  PRO A N     
4360 C  CA    . PRO A 539 ? 0.3308 0.4862 0.7411 0.0529  0.0054  -0.074  540  PRO A CA    
4361 C  C     . PRO A 539 ? 0.2993 0.4512 0.7102 0.0516  0.0036  -0.0787 540  PRO A C     
4362 O  O     . PRO A 539 ? 0.2909 0.4435 0.7018 0.0534  0.0026  -0.082  540  PRO A O     
4363 C  CB    . PRO A 539 ? 0.3435 0.4962 0.7557 0.0511  0.0058  -0.071  540  PRO A CB    
4364 C  CG    . PRO A 539 ? 0.3528 0.5107 0.7647 0.0545  0.007   -0.0688 540  PRO A CG    
4365 C  CD    . PRO A 539 ? 0.3356 0.4986 0.7454 0.0587  0.0069  -0.0718 540  PRO A CD    
4366 N  N     . LEU A 540 ? 0.2812 0.4292 0.6926 0.0485  0.0032  -0.0788 541  LEU A N     
4367 C  CA    . LEU A 540 ? 0.2619 0.4066 0.6745 0.047   0.0015  -0.0826 541  LEU A CA    
4368 C  C     . LEU A 540 ? 0.2448 0.3835 0.6596 0.0435  0.0012  -0.0818 541  LEU A C     
4369 O  O     . LEU A 540 ? 0.2454 0.3815 0.6603 0.0414  0.002   -0.0784 541  LEU A O     
4370 C  CB    . LEU A 540 ? 0.2604 0.4052 0.6722 0.0461  0.0014  -0.0831 541  LEU A CB    
4371 C  CG    . LEU A 540 ? 0.2746 0.4152 0.6883 0.0436  -0.0001 -0.0856 541  LEU A CG    
4372 C  CD1   . LEU A 540 ? 0.2789 0.4207 0.6935 0.0452  -0.002  -0.0903 541  LEU A CD1   
4373 C  CD2   . LEU A 540 ? 0.278  0.418  0.691  0.0423  0.0003  -0.0844 541  LEU A CD2   
4374 N  N     . LEU A 541 ? 0.2275 0.3639 0.6441 0.0431  -0.0002 -0.0851 542  LEU A N     
4375 C  CA    . LEU A 541 ? 0.2171 0.348  0.636  0.04    -0.0006 -0.0848 542  LEU A CA    
4376 C  C     . LEU A 541 ? 0.207  0.3357 0.6274 0.0387  -0.002  -0.0879 542  LEU A C     
4377 O  O     . LEU A 541 ? 0.2126 0.3426 0.6337 0.0401  -0.0034 -0.0916 542  LEU A O     
4378 C  CB    . LEU A 541 ? 0.2145 0.3447 0.6347 0.0406  -0.0009 -0.0855 542  LEU A CB    
4379 C  CG    . LEU A 541 ? 0.2265 0.3591 0.6459 0.0418  0.0005  -0.0821 542  LEU A CG    
4380 C  CD1   . LEU A 541 ? 0.2342 0.3667 0.6548 0.0431  0.0003  -0.0832 542  LEU A CD1   
4381 C  CD2   . LEU A 541 ? 0.2258 0.3554 0.6455 0.039   0.0014  -0.0778 542  LEU A CD2   
4382 N  N     . LEU A 542 ? 0.1925 0.3181 0.6132 0.0361  -0.0017 -0.0862 543  LEU A N     
4383 C  CA    . LEU A 542 ? 0.1811 0.3046 0.6035 0.0347  -0.0028 -0.0883 543  LEU A CA    
4384 C  C     . LEU A 542 ? 0.1669 0.2853 0.5922 0.0321  -0.0032 -0.0882 543  LEU A C     
4385 O  O     . LEU A 542 ? 0.1643 0.2794 0.5891 0.0302  -0.0023 -0.0852 543  LEU A O     
4386 C  CB    . LEU A 542 ? 0.1766 0.3004 0.5974 0.034   -0.002  -0.0862 543  LEU A CB    
4387 C  CG    . LEU A 542 ? 0.1846 0.3064 0.6073 0.0325  -0.0029 -0.0875 543  LEU A CG    
4388 C  CD1   . LEU A 542 ? 0.1843 0.3094 0.6081 0.0341  -0.0045 -0.0914 543  LEU A CD1   
4389 C  CD2   . LEU A 542 ? 0.1886 0.3095 0.6093 0.0316  -0.0016 -0.0846 543  LEU A CD2   
4390 N  N     . SER A 543 ? 0.1536 0.271  0.5815 0.0321  -0.0047 -0.0914 544  SER A N     
4391 C  CA    . SER A 543 ? 0.1539 0.2667 0.585  0.0298  -0.0051 -0.0915 544  SER A CA    
4392 C  C     . SER A 543 ? 0.1577 0.2685 0.5909 0.0281  -0.0058 -0.0919 544  SER A C     
4393 O  O     . SER A 543 ? 0.1674 0.2803 0.6015 0.0289  -0.007  -0.0944 544  SER A O     
4394 C  CB    . SER A 543 ? 0.1618 0.2747 0.5949 0.0308  -0.0063 -0.0945 544  SER A CB    
4395 O  OG    . SER A 543 ? 0.1874 0.3028 0.6184 0.0328  -0.0056 -0.094  544  SER A OG    
4396 N  N     . ILE A 544 ? 0.1518 0.2586 0.5858 0.0258  -0.005  -0.0894 545  ILE A N     
4397 C  CA    . ILE A 544 ? 0.1532 0.2582 0.5891 0.0244  -0.0053 -0.0892 545  ILE A CA    
4398 C  C     . ILE A 544 ? 0.1622 0.2631 0.6018 0.0225  -0.0056 -0.0891 545  ILE A C     
4399 O  O     . ILE A 544 ? 0.1769 0.2751 0.6163 0.0217  -0.0049 -0.0875 545  ILE A O     
4400 C  CB    . ILE A 544 ? 0.1535 0.2577 0.5862 0.0239  -0.0038 -0.0858 545  ILE A CB    
4401 C  CG1   . ILE A 544 ? 0.158  0.2661 0.5869 0.0257  -0.0031 -0.0852 545  ILE A CG1   
4402 C  CG2   . ILE A 544 ? 0.1546 0.2576 0.5889 0.0229  -0.0039 -0.0852 545  ILE A CG2   
4403 C  CD1   . ILE A 544 ? 0.1715 0.2782 0.597  0.0252  -0.0016 -0.0817 545  ILE A CD1   
4404 N  N     . VAL A 545 ? 0.1587 0.2592 0.6018 0.0219  -0.0067 -0.0905 546  VAL A N     
4405 C  CA    . VAL A 545 ? 0.1672 0.2641 0.6143 0.0202  -0.0069 -0.0901 546  VAL A CA    
4406 C  C     . VAL A 545 ? 0.1649 0.2609 0.6124 0.0193  -0.0064 -0.0879 546  VAL A C     
4407 O  O     . VAL A 545 ? 0.1658 0.2647 0.6126 0.0201  -0.0067 -0.0884 546  VAL A O     
4408 C  CB    . VAL A 545 ? 0.1852 0.2825 0.637  0.0202  -0.0089 -0.0936 546  VAL A CB    
4409 C  CG1   . VAL A 545 ? 0.193  0.2938 0.6458 0.0213  -0.0106 -0.0962 546  VAL A CG1   
4410 C  CG2   . VAL A 545 ? 0.1937 0.2876 0.6503 0.0184  -0.0091 -0.0928 546  VAL A CG2   
4411 N  N     . SER A 546 ? 0.1639 0.2563 0.6122 0.018   -0.0053 -0.0854 547  SER A N     
4412 C  CA    . SER A 546 ? 0.1768 0.2681 0.6253 0.0175  -0.0046 -0.083  547  SER A CA    
4413 C  C     . SER A 546 ? 0.163  0.2524 0.617  0.0163  -0.0051 -0.0828 547  SER A C     
4414 O  O     . SER A 546 ? 0.166  0.2529 0.6219 0.0156  -0.005  -0.0828 547  SER A O     
4415 C  CB    . SER A 546 ? 0.227  0.3159 0.6706 0.0174  -0.0027 -0.0796 547  SER A CB    
4416 O  OG    . SER A 546 ? 0.3132 0.3986 0.7566 0.0165  -0.0022 -0.0785 547  SER A OG    
4417 N  N     . LYS A 547 ? 0.1435 0.2344 0.6003 0.0163  -0.0056 -0.0827 548  LYS A N     
4418 C  CA    . LYS A 547 ? 0.1381 0.2276 0.6007 0.0153  -0.0061 -0.0822 548  LYS A CA    
4419 C  C     . LYS A 547 ? 0.1295 0.2188 0.5921 0.0153  -0.0049 -0.079  548  LYS A C     
4420 O  O     . LYS A 547 ? 0.1339 0.225  0.5926 0.0162  -0.0043 -0.0782 548  LYS A O     
4421 C  CB    . LYS A 547 ? 0.1556 0.2476 0.6236 0.0151  -0.0086 -0.0856 548  LYS A CB    
4422 C  CG    . LYS A 547 ? 0.1929 0.2848 0.6615 0.0153  -0.0098 -0.0888 548  LYS A CG    
4423 C  CD    . LYS A 547 ? 0.2531 0.3413 0.7241 0.0143  -0.0091 -0.0879 548  LYS A CD    
4424 C  CE    . LYS A 547 ? 0.3201 0.4081 0.7908 0.0146  -0.0099 -0.0906 548  LYS A CE    
4425 N  NZ    . LYS A 547 ? 0.36   0.4452 0.8352 0.0136  -0.01   -0.0905 548  LYS A NZ    
4426 N  N     . GLU A 548 ? 0.1204 0.2078 0.5872 0.0146  -0.0046 -0.0771 549  GLU A N     
4427 C  CA    . GLU A 548 ? 0.1172 0.2045 0.5842 0.0149  -0.0034 -0.0738 549  GLU A CA    
4428 C  C     . GLU A 548 ? 0.1149 0.2063 0.5849 0.0151  -0.0047 -0.0748 549  GLU A C     
4429 O  O     . GLU A 548 ? 0.1032 0.196  0.5703 0.0159  -0.0038 -0.073  549  GLU A O     
4430 C  CB    . GLU A 548 ? 0.1365 0.2213 0.608  0.0143  -0.0027 -0.0714 549  GLU A CB    
4431 C  CG    . GLU A 548 ? 0.1708 0.2557 0.6431 0.0149  -0.0013 -0.0676 549  GLU A CG    
4432 C  CD    . GLU A 548 ? 0.2434 0.326  0.7202 0.0146  -0.0005 -0.065  549  GLU A CD    
4433 O  OE1   . GLU A 548 ? 0.2899 0.3711 0.7701 0.0137  -0.0012 -0.0663 549  GLU A OE1   
4434 O  OE2   . GLU A 548 ? 0.226  0.3083 0.703  0.0154  0.0009  -0.0614 549  GLU A OE2   
4435 N  N     . LYS A 549 ? 0.116  0.2092 0.5918 0.0144  -0.0071 -0.0778 550  LYS A N     
4436 C  CA    . LYS A 549 ? 0.1234 0.2204 0.603  0.0143  -0.009  -0.0791 550  LYS A CA    
4437 C  C     . LYS A 549 ? 0.1347 0.234  0.6143 0.0145  -0.0114 -0.0837 550  LYS A C     
4438 O  O     . LYS A 549 ? 0.1234 0.2213 0.603  0.0144  -0.0121 -0.0861 550  LYS A O     
4439 C  CB    . LYS A 549 ? 0.1309 0.2277 0.6187 0.0132  -0.01   -0.0779 550  LYS A CB    
4440 C  CG    . LYS A 549 ? 0.153  0.2479 0.6411 0.0134  -0.0076 -0.0731 550  LYS A CG    
4441 C  CD    . LYS A 549 ? 0.1693 0.2645 0.6658 0.0124  -0.0083 -0.0713 550  LYS A CD    
4442 C  CE    . LYS A 549 ? 0.1973 0.2911 0.6923 0.0133  -0.0055 -0.0663 550  LYS A CE    
4443 N  NZ    . LYS A 549 ? 0.2036 0.2984 0.7064 0.0128  -0.0058 -0.0634 550  LYS A NZ    
4444 N  N     . PRO A 550 ? 0.1534 0.2564 0.6332 0.015   -0.0128 -0.0851 551  PRO A N     
4445 C  CA    . PRO A 550 ? 0.163  0.2682 0.6424 0.0156  -0.0152 -0.0897 551  PRO A CA    
4446 C  C     . PRO A 550 ? 0.1877 0.2918 0.6729 0.0147  -0.0177 -0.0927 551  PRO A C     
4447 O  O     . PRO A 550 ? 0.1973 0.3013 0.6806 0.0154  -0.0188 -0.0961 551  PRO A O     
4448 C  CB    . PRO A 550 ? 0.168  0.2773 0.6474 0.0162  -0.0163 -0.09   551  PRO A CB    
4449 C  CG    . PRO A 550 ? 0.1642 0.2735 0.6465 0.0155  -0.015  -0.0859 551  PRO A CG    
4450 C  CD    . PRO A 550 ? 0.1477 0.2532 0.6278 0.0153  -0.0122 -0.0826 551  PRO A CD    
4451 N  N     . ASN A 551 ? 0.1933 0.2964 0.6855 0.0133  -0.0186 -0.0915 552  ASN A N     
4452 C  CA    . ASN A 551 ? 0.2065 0.3082 0.7046 0.0123  -0.0211 -0.0943 552  ASN A CA    
4453 C  C     . ASN A 551 ? 0.21   0.308  0.7073 0.0121  -0.0198 -0.0944 552  ASN A C     
4454 O  O     . ASN A 551 ? 0.2027 0.2994 0.7037 0.0116  -0.0217 -0.0971 552  ASN A O     
4455 C  CB    . ASN A 551 ? 0.2363 0.3383 0.7427 0.0109  -0.0228 -0.0931 552  ASN A CB    
4456 C  CG    . ASN A 551 ? 0.3029 0.4087 0.8111 0.011   -0.0252 -0.0945 552  ASN A CG    
4457 O  OD1   . ASN A 551 ? 0.3197 0.4275 0.8238 0.0121  -0.0264 -0.0977 552  ASN A OD1   
4458 N  ND2   . ASN A 551 ? 0.3235 0.4305 0.8379 0.0099  -0.0257 -0.0918 552  ASN A ND2   
4459 N  N     . ASP A 552 ? 0.2082 0.3047 0.7005 0.0125  -0.0168 -0.0915 553  ASP A N     
4460 C  CA    . ASP A 552 ? 0.2095 0.3028 0.7002 0.0124  -0.0157 -0.0916 553  ASP A CA    
4461 C  C     . ASP A 552 ? 0.2081 0.3022 0.6941 0.0136  -0.0163 -0.0951 553  ASP A C     
4462 O  O     . ASP A 552 ? 0.2162 0.3081 0.7015 0.0136  -0.0159 -0.0958 553  ASP A O     
4463 C  CB    . ASP A 552 ? 0.2354 0.3267 0.7223 0.0125  -0.0125 -0.0874 553  ASP A CB    
4464 C  CG    . ASP A 552 ? 0.29   0.3804 0.7811 0.0117  -0.0116 -0.0837 553  ASP A CG    
4465 O  OD1   . ASP A 552 ? 0.2942 0.3847 0.7924 0.0108  -0.0131 -0.0841 553  ASP A OD1   
4466 O  OD2   . ASP A 552 ? 0.3123 0.4018 0.7995 0.0122  -0.0093 -0.0803 553  ASP A OD2   
4467 N  N     . LEU A 553 ? 0.2019 0.2991 0.6845 0.0148  -0.0172 -0.097  554  LEU A N     
4468 C  CA    . LEU A 553 ? 0.2116 0.31   0.6899 0.0163  -0.0178 -0.1001 554  LEU A CA    
4469 C  C     . LEU A 553 ? 0.2275 0.3254 0.7102 0.0163  -0.0207 -0.1041 554  LEU A C     
4470 O  O     . LEU A 553 ? 0.2244 0.3238 0.7108 0.016   -0.0231 -0.1059 554  LEU A O     
4471 C  CB    . LEU A 553 ? 0.2046 0.3068 0.6784 0.0178  -0.018  -0.1007 554  LEU A CB    
4472 C  CG    . LEU A 553 ? 0.2109 0.3136 0.6794 0.0182  -0.0152 -0.0972 554  LEU A CG    
4473 C  CD1   . LEU A 553 ? 0.2116 0.3182 0.6769 0.0195  -0.0156 -0.0979 554  LEU A CD1   
4474 C  CD2   . LEU A 553 ? 0.2148 0.3157 0.6789 0.0187  -0.0134 -0.0964 554  LEU A CD2   
4475 N  N     . GLU A 554 ? 0.2421 0.3377 0.7247 0.0164  -0.0205 -0.1053 555  GLU A N     
4476 C  CA    . GLU A 554 ? 0.2638 0.3582 0.7506 0.0164  -0.0229 -0.1089 555  GLU A CA    
4477 C  C     . GLU A 554 ? 0.2725 0.3691 0.7568 0.0183  -0.0252 -0.1132 555  GLU A C     
4478 O  O     . GLU A 554 ? 0.2756 0.3747 0.7541 0.0199  -0.0244 -0.1134 555  GLU A O     
4479 C  CB    . GLU A 554 ? 0.3177 0.4091 0.8042 0.0162  -0.0215 -0.1084 555  GLU A CB    
4480 C  CG    . GLU A 554 ? 0.4277 0.5163 0.9187 0.0143  -0.0202 -0.1051 555  GLU A CG    
4481 C  CD    . GLU A 554 ? 0.5707 0.6567 1.0604 0.0141  -0.0182 -0.1037 555  GLU A CD    
4482 O  OE1   . GLU A 554 ? 0.6115 0.6981 1.0955 0.0149  -0.0164 -0.1023 555  GLU A OE1   
4483 O  OE2   . GLU A 554 ? 0.6171 0.7008 1.1118 0.0131  -0.0186 -0.1037 555  GLU A OE2   
4484 N  N     . PRO A 555 ? 0.2747 0.3704 0.7634 0.0181  -0.0283 -0.1168 556  PRO A N     
4485 C  CA    . PRO A 555 ? 0.2703 0.3678 0.7562 0.0203  -0.0307 -0.1213 556  PRO A CA    
4486 C  C     . PRO A 555 ? 0.2658 0.3637 0.7454 0.0226  -0.0293 -0.1223 556  PRO A C     
4487 O  O     . PRO A 555 ? 0.2641 0.3597 0.7437 0.0224  -0.0277 -0.1213 556  PRO A O     
4488 C  CB    . PRO A 555 ? 0.2812 0.3763 0.7733 0.0195  -0.034  -0.1246 556  PRO A CB    
4489 C  CG    . PRO A 555 ? 0.2874 0.3808 0.7863 0.0167  -0.0337 -0.1214 556  PRO A CG    
4490 C  CD    . PRO A 555 ? 0.2699 0.3628 0.7662 0.0162  -0.0297 -0.1169 556  PRO A CD    
4491 N  N     . LYS A 556 ? 0.2638 0.3651 0.7383 0.0249  -0.0296 -0.1239 557  LYS A N     
4492 C  CA    . LYS A 556 ? 0.2708 0.3735 0.739  0.0275  -0.0283 -0.1247 557  LYS A CA    
4493 C  C     . LYS A 556 ? 0.2683 0.371  0.7333 0.0272  -0.0247 -0.1204 557  LYS A C     
4494 O  O     . LYS A 556 ? 0.2754 0.3788 0.7364 0.029   -0.0235 -0.1206 557  LYS A O     
4495 C  CB    . LYS A 556 ? 0.304  0.4047 0.7725 0.029   -0.0299 -0.1285 557  LYS A CB    
4496 C  CG    . LYS A 556 ? 0.3601 0.4603 0.8313 0.0296  -0.034  -0.1331 557  LYS A CG    
4497 C  CD    . LYS A 556 ? 0.4293 0.526  0.9024 0.0302  -0.0355 -0.1362 557  LYS A CD    
4498 C  CE    . LYS A 556 ? 0.4822 0.5797 0.9494 0.0336  -0.0347 -0.138  557  LYS A CE    
4499 N  NZ    . LYS A 556 ? 0.5021 0.5963 0.9708 0.0347  -0.037  -0.142  557  LYS A NZ    
4500 N  N     . ILE A 557 ? 0.2574 0.3593 0.7239 0.025   -0.0229 -0.1166 558  ILE A N     
4501 C  CA    . ILE A 557 ? 0.2537 0.3552 0.717  0.0246  -0.0198 -0.1126 558  ILE A CA    
4502 C  C     . ILE A 557 ? 0.2477 0.3527 0.7049 0.0268  -0.0185 -0.1121 558  ILE A C     
4503 O  O     . ILE A 557 ? 0.2513 0.356  0.7056 0.0275  -0.0168 -0.1106 558  ILE A O     
4504 C  CB    . ILE A 557 ? 0.2591 0.359  0.7246 0.0222  -0.0183 -0.1087 558  ILE A CB    
4505 C  CG1   . ILE A 557 ? 0.2707 0.369  0.7335 0.0216  -0.0155 -0.105  558  ILE A CG1   
4506 C  CG2   . ILE A 557 ? 0.261  0.3637 0.7257 0.0222  -0.0185 -0.1078 558  ILE A CG2   
4507 C  CD1   . ILE A 557 ? 0.2821 0.3778 0.746  0.0214  -0.0151 -0.1052 558  ILE A CD1   
4508 N  N     . GLY A 558 ? 0.2397 0.3479 0.6951 0.028   -0.0195 -0.1133 559  GLY A N     
4509 C  CA    . GLY A 558 ? 0.2334 0.3453 0.6832 0.0304  -0.0184 -0.1129 559  GLY A CA    
4510 C  C     . GLY A 558 ? 0.228  0.3409 0.675  0.033   -0.0187 -0.1152 559  GLY A C     
4511 O  O     . GLY A 558 ? 0.2284 0.3427 0.6718 0.0341  -0.0167 -0.1131 559  GLY A O     
4512 N  N     . VAL A 559 ? 0.2232 0.3352 0.6722 0.0339  -0.0212 -0.1192 560  VAL A N     
4513 C  CA    . VAL A 559 ? 0.2257 0.3383 0.6722 0.0367  -0.0216 -0.1217 560  VAL A CA    
4514 C  C     . VAL A 559 ? 0.2241 0.334  0.671  0.0359  -0.0197 -0.1195 560  VAL A C     
4515 O  O     . VAL A 559 ? 0.2299 0.3414 0.6734 0.0381  -0.0183 -0.1189 560  VAL A O     
4516 C  CB    . VAL A 559 ? 0.2384 0.35   0.6869 0.0377  -0.025  -0.1268 560  VAL A CB    
4517 C  CG1   . VAL A 559 ? 0.2523 0.3639 0.698  0.0408  -0.0253 -0.1293 560  VAL A CG1   
4518 C  CG2   . VAL A 559 ? 0.2406 0.3553 0.6881 0.0387  -0.027  -0.1289 560  VAL A CG2   
4519 N  N     . GLN A 560 ? 0.2169 0.3231 0.6682 0.033   -0.0195 -0.1181 561  GLN A N     
4520 C  CA    . GLN A 560 ? 0.2152 0.3187 0.6674 0.032   -0.0178 -0.116  561  GLN A CA    
4521 C  C     . GLN A 560 ? 0.2157 0.3205 0.6644 0.0318  -0.015  -0.1117 561  GLN A C     
4522 O  O     . GLN A 560 ? 0.2189 0.3232 0.6665 0.0323  -0.0136 -0.1102 561  GLN A O     
4523 C  CB    . GLN A 560 ? 0.2357 0.3353 0.6935 0.0289  -0.0181 -0.1152 561  GLN A CB    
4524 C  CG    . GLN A 560 ? 0.304  0.4018 0.766  0.0289  -0.0209 -0.1192 561  GLN A CG    
4525 C  CD    . GLN A 560 ? 0.3896 0.484  0.8575 0.0259  -0.0212 -0.118  561  GLN A CD    
4526 O  OE1   . GLN A 560 ? 0.4172 0.5116 0.8879 0.0243  -0.022  -0.1174 561  GLN A OE1   
4527 N  NE2   . GLN A 560 ? 0.4155 0.507  0.8854 0.0252  -0.0204 -0.1175 561  GLN A NE2   
4528 N  N     . LEU A 561 ? 0.2063 0.3128 0.6536 0.0311  -0.0142 -0.1095 562  LEU A N     
4529 C  CA    . LEU A 561 ? 0.2109 0.3184 0.6549 0.0309  -0.0118 -0.1055 562  LEU A CA    
4530 C  C     . LEU A 561 ? 0.2235 0.3345 0.6634 0.0339  -0.0112 -0.1058 562  LEU A C     
4531 O  O     . LEU A 561 ? 0.2311 0.3422 0.6695 0.034   -0.0095 -0.1031 562  LEU A O     
4532 C  CB    . LEU A 561 ? 0.2064 0.3147 0.6495 0.0297  -0.0112 -0.1034 562  LEU A CB    
4533 C  CG    . LEU A 561 ? 0.2236 0.3285 0.6704 0.0269  -0.0114 -0.1022 562  LEU A CG    
4534 C  CD1   . LEU A 561 ? 0.237  0.343  0.6824 0.0262  -0.0107 -0.1002 562  LEU A CD1   
4535 C  CD2   . LEU A 561 ? 0.2295 0.3307 0.6777 0.025   -0.0101 -0.0998 562  LEU A CD2   
4536 N  N     . ILE A 562 ? 0.2229 0.3371 0.6611 0.0364  -0.0125 -0.1088 563  ILE A N     
4537 C  CA    . ILE A 562 ? 0.2275 0.3456 0.6618 0.0398  -0.012  -0.1092 563  ILE A CA    
4538 C  C     . ILE A 562 ? 0.2359 0.3528 0.6703 0.0412  -0.0119 -0.1102 563  ILE A C     
4539 O  O     . ILE A 562 ? 0.2356 0.3542 0.6678 0.0425  -0.0102 -0.1077 563  ILE A O     
4540 C  CB    . ILE A 562 ? 0.2312 0.3526 0.6637 0.0424  -0.0137 -0.1127 563  ILE A CB    
4541 C  CG1   . ILE A 562 ? 0.2378 0.3607 0.67   0.0412  -0.0136 -0.1115 563  ILE A CG1   
4542 C  CG2   . ILE A 562 ? 0.2353 0.3607 0.6636 0.0464  -0.0131 -0.1133 563  ILE A CG2   
4543 C  CD1   . ILE A 562 ? 0.2527 0.3778 0.682  0.0413  -0.0113 -0.1075 563  ILE A CD1   
4544 N  N     . LYS A 563 ? 0.2407 0.3546 0.6783 0.0406  -0.0136 -0.1133 564  LYS A N     
4545 C  CA    . LYS A 563 ? 0.2511 0.3634 0.6892 0.0418  -0.0136 -0.1144 564  LYS A CA    
4546 C  C     . LYS A 563 ? 0.2525 0.3629 0.6915 0.04    -0.0115 -0.1105 564  LYS A C     
4547 O  O     . LYS A 563 ? 0.2588 0.3696 0.6968 0.0417  -0.0107 -0.11   564  LYS A O     
4548 C  CB    . LYS A 563 ? 0.2926 0.4017 0.7341 0.0413  -0.0161 -0.1186 564  LYS A CB    
4549 C  CG    . LYS A 563 ? 0.3777 0.4884 0.8181 0.0434  -0.0187 -0.123  564  LYS A CG    
4550 C  CD    . LYS A 563 ? 0.4647 0.5793 0.8999 0.048   -0.0186 -0.1246 564  LYS A CD    
4551 C  CE    . LYS A 563 ? 0.5292 0.6441 0.9637 0.0501  -0.0218 -0.1298 564  LYS A CE    
4552 N  NZ    . LYS A 563 ? 0.557  0.6763 0.986  0.0546  -0.0217 -0.1311 564  LYS A NZ    
4553 N  N     . TYR A 564 ? 0.242  0.3506 0.6827 0.0368  -0.0106 -0.1075 565  TYR A N     
4554 C  CA    . TYR A 564 ? 0.2306 0.3375 0.6719 0.035   -0.0088 -0.1035 565  TYR A CA    
4555 C  C     . TYR A 564 ? 0.238  0.3483 0.6756 0.0366  -0.007  -0.1004 565  TYR A C     
4556 O  O     . TYR A 564 ? 0.2466 0.3568 0.684  0.0369  -0.0059 -0.0983 565  TYR A O     
4557 C  CB    . TYR A 564 ? 0.2153 0.3193 0.6587 0.0316  -0.0084 -0.1013 565  TYR A CB    
4558 C  CG    . TYR A 564 ? 0.2048 0.3062 0.6494 0.0296  -0.0071 -0.098  565  TYR A CG    
4559 C  CD1   . TYR A 564 ? 0.2056 0.3037 0.6537 0.0283  -0.0074 -0.0988 565  TYR A CD1   
4560 C  CD2   . TYR A 564 ? 0.2086 0.3106 0.6507 0.0289  -0.0055 -0.094  565  TYR A CD2   
4561 C  CE1   . TYR A 564 ? 0.2114 0.3071 0.6605 0.0265  -0.0062 -0.0957 565  TYR A CE1   
4562 C  CE2   . TYR A 564 ? 0.2096 0.309  0.6527 0.027   -0.0045 -0.0911 565  TYR A CE2   
4563 C  CZ    . TYR A 564 ? 0.216  0.3124 0.6625 0.0259  -0.0048 -0.0919 565  TYR A CZ    
4564 O  OH    . TYR A 564 ? 0.2236 0.3175 0.671  0.0241  -0.0039 -0.089  565  TYR A OH    
4565 N  N     . ILE A 565 ? 0.2339 0.3474 0.6688 0.0377  -0.0069 -0.1    566  ILE A N     
4566 C  CA    . ILE A 565 ? 0.2367 0.3539 0.6685 0.0394  -0.0053 -0.097  566  ILE A CA    
4567 C  C     . ILE A 565 ? 0.248  0.368  0.6781 0.0432  -0.0052 -0.0985 566  ILE A C     
4568 O  O     . ILE A 565 ? 0.2502 0.3718 0.6793 0.0441  -0.0038 -0.0956 566  ILE A O     
4569 C  CB    . ILE A 565 ? 0.236  0.356  0.6655 0.0399  -0.0052 -0.0964 566  ILE A CB    
4570 C  CG1   . ILE A 565 ? 0.2435 0.3603 0.6744 0.0365  -0.0052 -0.095  566  ILE A CG1   
4571 C  CG2   . ILE A 565 ? 0.2352 0.3591 0.6618 0.0417  -0.0035 -0.093  566  ILE A CG2   
4572 C  CD1   . ILE A 565 ? 0.2543 0.3682 0.6859 0.0339  -0.004  -0.0911 566  ILE A CD1   
4573 N  N     . GLU A 566 ? 0.2532 0.3737 0.6831 0.0452  -0.0069 -0.103  567  GLU A N     
4574 C  CA    . GLU A 566 ? 0.2591 0.3816 0.687  0.0491  -0.0071 -0.105  567  GLU A CA    
4575 C  C     . GLU A 566 ? 0.2624 0.3826 0.692  0.0487  -0.0063 -0.1039 567  GLU A C     
4576 O  O     . GLU A 566 ? 0.2692 0.3919 0.697  0.0515  -0.0052 -0.1028 567  GLU A O     
4577 C  CB    . GLU A 566 ? 0.2918 0.4142 0.7194 0.051   -0.0095 -0.1104 567  GLU A CB    
4578 C  CG    . GLU A 566 ? 0.364  0.4892 0.7896 0.0518  -0.0104 -0.1118 567  GLU A CG    
4579 C  CD    . GLU A 566 ? 0.4707 0.6013 0.8919 0.056   -0.0096 -0.1115 567  GLU A CD    
4580 O  OE1   . GLU A 566 ? 0.4897 0.6228 0.9094 0.0574  -0.0075 -0.1079 567  GLU A OE1   
4581 O  OE2   . GLU A 566 ? 0.5069 0.6396 0.9263 0.058   -0.0111 -0.1146 567  GLU A OE2   
4582 N  N     . TYR A 567 ? 0.2572 0.3729 0.6906 0.0453  -0.0068 -0.1041 568  TYR A N     
4583 C  CA    . TYR A 567 ? 0.2594 0.3725 0.6949 0.0444  -0.006  -0.1028 568  TYR A CA    
4584 C  C     . TYR A 567 ? 0.2609 0.3757 0.6955 0.0439  -0.0039 -0.0976 568  TYR A C     
4585 O  O     . TYR A 567 ? 0.2643 0.3804 0.6984 0.0458  -0.0029 -0.0964 568  TYR A O     
4586 C  CB    . TYR A 567 ? 0.2655 0.3738 0.7051 0.0408  -0.0069 -0.1035 568  TYR A CB    
4587 C  CG    . TYR A 567 ? 0.2905 0.396  0.7325 0.0387  -0.0058 -0.1009 568  TYR A CG    
4588 C  CD1   . TYR A 567 ? 0.3109 0.4153 0.7539 0.0401  -0.0057 -0.1022 568  TYR A CD1   
4589 C  CD2   . TYR A 567 ? 0.3106 0.4143 0.754  0.0354  -0.0049 -0.0974 568  TYR A CD2   
4590 C  CE1   . TYR A 567 ? 0.3288 0.4309 0.7743 0.0382  -0.0047 -0.0997 568  TYR A CE1   
4591 C  CE2   . TYR A 567 ? 0.3248 0.4259 0.7705 0.0336  -0.0041 -0.0951 568  TYR A CE2   
4592 C  CZ    . TYR A 567 ? 0.3396 0.4401 0.7865 0.0349  -0.0039 -0.0962 568  TYR A CZ    
4593 O  OH    . TYR A 567 ? 0.3589 0.4571 0.8082 0.0331  -0.0031 -0.0939 568  TYR A OH    
4594 N  N     . LEU A 568 ? 0.2543 0.3692 0.6887 0.0416  -0.0033 -0.0945 569  LEU A N     
4595 C  CA    . LEU A 568 ? 0.2547 0.371  0.6885 0.0409  -0.0016 -0.0896 569  LEU A CA    
4596 C  C     . LEU A 568 ? 0.2706 0.3921 0.7017 0.0446  -0.0006 -0.0882 569  LEU A C     
4597 O  O     . LEU A 568 ? 0.2771 0.3998 0.7084 0.0452  0.0007  -0.0852 569  LEU A O     
4598 C  CB    . LEU A 568 ? 0.2472 0.3623 0.6811 0.0379  -0.0014 -0.087  569  LEU A CB    
4599 C  CG    . LEU A 568 ? 0.2569 0.3669 0.6933 0.0344  -0.0021 -0.0878 569  LEU A CG    
4600 C  CD1   . LEU A 568 ? 0.2625 0.3715 0.6983 0.032   -0.0019 -0.0853 569  LEU A CD1   
4601 C  CD2   . LEU A 568 ? 0.261  0.3681 0.7    0.0328  -0.0018 -0.0865 569  LEU A CD2   
4602 N  N     . PHE A 569 ? 0.2755 0.4002 0.704  0.0472  -0.001  -0.0904 570  PHE A N     
4603 C  CA    . PHE A 569 ? 0.2868 0.4168 0.7125 0.0513  0       -0.0893 570  PHE A CA    
4604 C  C     . PHE A 569 ? 0.2974 0.4282 0.7226 0.0545  0.0003  -0.0904 570  PHE A C     
4605 O  O     . PHE A 569 ? 0.3027 0.4376 0.7263 0.0575  0.0017  -0.0879 570  PHE A O     
4606 C  CB    . PHE A 569 ? 0.2902 0.4232 0.7131 0.0536  -0.0007 -0.0918 570  PHE A CB    
4607 C  CG    . PHE A 569 ? 0.303  0.4381 0.7251 0.0524  0       -0.0888 570  PHE A CG    
4608 C  CD1   . PHE A 569 ? 0.3143 0.4463 0.7375 0.0489  -0.0007 -0.0891 570  PHE A CD1   
4609 C  CD2   . PHE A 569 ? 0.3136 0.4537 0.7338 0.0549  0.0015  -0.0857 570  PHE A CD2   
4610 C  CE1   . PHE A 569 ? 0.324  0.4576 0.7462 0.048   0       -0.0864 570  PHE A CE1   
4611 C  CE2   . PHE A 569 ? 0.3264 0.468  0.7459 0.0538  0.0021  -0.0829 570  PHE A CE2   
4612 C  CZ    . PHE A 569 ? 0.324  0.4623 0.7444 0.0504  0.0014  -0.0834 570  PHE A CZ    
4613 N  N     . ASP A 570 ? 0.2984 0.4254 0.7252 0.0539  -0.0008 -0.0938 571  ASP A N     
4614 C  CA    . ASP A 570 ? 0.3061 0.4334 0.7325 0.0568  -0.0005 -0.0948 571  ASP A CA    
4615 C  C     . ASP A 570 ? 0.3172 0.4445 0.7453 0.0558  0.0013  -0.0901 571  ASP A C     
4616 O  O     . ASP A 570 ? 0.3231 0.4509 0.7509 0.0582  0.0019  -0.0903 571  ASP A O     
4617 C  CB    . ASP A 570 ? 0.3201 0.4428 0.7482 0.0561  -0.0023 -0.0996 571  ASP A CB    
4618 C  CG    . ASP A 570 ? 0.379  0.5018 0.8052 0.0582  -0.0043 -0.1048 571  ASP A CG    
4619 O  OD1   . ASP A 570 ? 0.3874 0.5143 0.8103 0.0611  -0.0042 -0.1051 571  ASP A OD1   
4620 O  OD2   . ASP A 570 ? 0.407  0.5258 0.8353 0.057   -0.0061 -0.1086 571  ASP A OD2   
4621 N  N     . PHE A 571 ? 0.3116 0.4381 0.7416 0.0522  0.0019  -0.0861 572  PHE A N     
4622 C  CA    . PHE A 571 ? 0.3112 0.4374 0.7432 0.0506  0.0032  -0.0816 572  PHE A CA    
4623 C  C     . PHE A 571 ? 0.3062 0.4351 0.7379 0.0495  0.0043  -0.0766 572  PHE A C     
4624 O  O     . PHE A 571 ? 0.301  0.4306 0.7317 0.0486  0.0039  -0.0765 572  PHE A O     
4625 C  CB    . PHE A 571 ? 0.3127 0.4334 0.7479 0.0465  0.0025  -0.0821 572  PHE A CB    
4626 C  CG    . PHE A 571 ? 0.3287 0.4464 0.7648 0.0472  0.0014  -0.0869 572  PHE A CG    
4627 C  CD1   . PHE A 571 ? 0.3421 0.4601 0.7783 0.0497  0.0019  -0.0877 572  PHE A CD1   
4628 C  CD2   . PHE A 571 ? 0.3449 0.4596 0.7819 0.0455  -0.0002 -0.0906 572  PHE A CD2   
4629 C  CE1   . PHE A 571 ? 0.3535 0.4683 0.7905 0.0504  0.0008  -0.0922 572  PHE A CE1   
4630 C  CE2   . PHE A 571 ? 0.3571 0.4688 0.7954 0.046   -0.0014 -0.0949 572  PHE A CE2   
4631 C  CZ    . PHE A 571 ? 0.3539 0.4656 0.7922 0.0484  -0.001  -0.0957 572  PHE A CZ    
4632 N  N     . THR A 572 ? 0.3    0.4306 0.7329 0.0496  0.0056  -0.0721 573  THR A N     
4633 C  CA    . THR A 572 ? 0.3003 0.4334 0.7337 0.0485  0.0064  -0.0668 573  THR A CA    
4634 C  C     . THR A 572 ? 0.2931 0.4218 0.728  0.0436  0.0055  -0.0658 573  THR A C     
4635 O  O     . THR A 572 ? 0.2932 0.4175 0.7299 0.041   0.0049  -0.0668 573  THR A O     
4636 C  CB    . THR A 572 ? 0.323  0.4581 0.758  0.0493  0.0077  -0.0625 573  THR A CB    
4637 O  OG1   . THR A 572 ? 0.344  0.4833 0.7772 0.0542  0.0087  -0.0632 573  THR A OG1   
4638 C  CG2   . THR A 572 ? 0.322  0.459  0.7583 0.0475  0.0083  -0.0567 573  THR A CG2   
4639 N  N     . PRO A 573 ? 0.2901 0.4196 0.724  0.0423  0.0054  -0.0638 574  PRO A N     
4640 C  CA    . PRO A 573 ? 0.2911 0.4161 0.7261 0.0379  0.0046  -0.0627 574  PRO A CA    
4641 C  C     . PRO A 573 ? 0.286  0.4084 0.7234 0.0353  0.0046  -0.0594 574  PRO A C     
4642 O  O     . PRO A 573 ? 0.2919 0.4173 0.7303 0.0365  0.0055  -0.056  574  PRO A O     
4643 C  CB    . PRO A 573 ? 0.3017 0.4291 0.7353 0.0378  0.0049  -0.0598 574  PRO A CB    
4644 C  CG    . PRO A 573 ? 0.3061 0.4388 0.7377 0.0421  0.0056  -0.0611 574  PRO A CG    
4645 C  CD    . PRO A 573 ? 0.2814 0.416  0.7135 0.045   0.0062  -0.0621 574  PRO A CD    
4646 N  N     . SER A 574 ? 0.2705 0.3877 0.709  0.0319  0.0038  -0.0603 575  SER A N     
4647 C  CA    . SER A 574 ? 0.2616 0.3762 0.7023 0.0293  0.0036  -0.0573 575  SER A CA    
4648 C  C     . SER A 574 ? 0.2632 0.3797 0.7042 0.0283  0.0038  -0.0519 575  SER A C     
4649 O  O     . SER A 574 ? 0.2607 0.3791 0.7036 0.0287  0.0044  -0.0488 575  SER A O     
4650 C  CB    . SER A 574 ? 0.2567 0.3656 0.6978 0.0259  0.0026  -0.0587 575  SER A CB    
4651 O  OG    . SER A 574 ? 0.2499 0.3569 0.6913 0.0264  0.0024  -0.0633 575  SER A OG    
4652 N  N     . VAL A 575 ? 0.26   0.3765 0.6995 0.0274  0.0034  -0.0507 576  VAL A N     
4653 C  CA    . VAL A 575 ? 0.2629 0.3808 0.7029 0.0263  0.0033  -0.0457 576  VAL A CA    
4654 C  C     . VAL A 575 ? 0.2683 0.3897 0.7065 0.0281  0.0037  -0.0451 576  VAL A C     
4655 O  O     . VAL A 575 ? 0.2653 0.3873 0.7016 0.0296  0.0039  -0.0486 576  VAL A O     
4656 C  CB    . VAL A 575 ? 0.2682 0.3805 0.7085 0.0222  0.002   -0.0441 576  VAL A CB    
4657 C  CG1   . VAL A 575 ? 0.2727 0.3827 0.7152 0.0206  0.0017  -0.043  576  VAL A CG1   
4658 C  CG2   . VAL A 575 ? 0.2712 0.3793 0.7093 0.0209  0.0014  -0.0475 576  VAL A CG2   
4659 N  N     . GLN A 576 ? 0.275  0.399  0.7141 0.0279  0.0039  -0.0404 577  GLN A N     
4660 C  CA    . GLN A 576 ? 0.29   0.4172 0.7278 0.0293  0.0043  -0.0389 577  GLN A CA    
4661 C  C     . GLN A 576 ? 0.3074 0.4342 0.7467 0.027   0.0036  -0.0336 577  GLN A C     
4662 O  O     . GLN A 576 ? 0.3011 0.4267 0.7428 0.0251  0.003   -0.0306 577  GLN A O     
4663 C  CB    . GLN A 576 ? 0.3084 0.4422 0.746  0.0338  0.0058  -0.0392 577  GLN A CB    
4664 C  CG    . GLN A 576 ? 0.3687 0.5066 0.8089 0.0351  0.0066  -0.0347 577  GLN A CG    
4665 C  CD    . GLN A 576 ? 0.4401 0.5846 0.8795 0.0399  0.0082  -0.0347 577  GLN A CD    
4666 O  OE1   . GLN A 576 ? 0.4755 0.6211 0.9132 0.0427  0.0087  -0.0388 577  GLN A OE1   
4667 N  NE2   . GLN A 576 ? 0.441  0.5901 0.8817 0.0411  0.0089  -0.0299 577  GLN A NE2   
4668 N  N     . ARG A 577 ? 0.3268 0.4544 0.7648 0.027   0.0036  -0.0324 578  ARG A N     
4669 C  CA    . ARG A 577 ? 0.3546 0.4818 0.794  0.025   0.0028  -0.0275 578  ARG A CA    
4670 C  C     . ARG A 577 ? 0.3945 0.5259 0.8331 0.027   0.0036  -0.0262 578  ARG A C     
4671 O  O     . ARG A 577 ? 0.3983 0.5311 0.8344 0.0291  0.0044  -0.0297 578  ARG A O     
4672 C  CB    . ARG A 577 ? 0.3676 0.4875 0.8059 0.0208  0.0009  -0.0276 578  ARG A CB    
4673 C  CG    . ARG A 577 ? 0.3989 0.5156 0.8339 0.0203  0.0007  -0.0308 578  ARG A CG    
4674 C  CD    . ARG A 577 ? 0.4213 0.5309 0.8549 0.0167  -0.001  -0.0302 578  ARG A CD    
4675 N  NE    . ARG A 577 ? 0.4455 0.5516 0.8758 0.0164  -0.0011 -0.0338 578  ARG A NE    
4676 C  CZ    . ARG A 577 ? 0.4627 0.5625 0.891  0.0138  -0.0023 -0.0341 578  ARG A CZ    
4677 N  NH1   . ARG A 577 ? 0.4591 0.5551 0.8881 0.0112  -0.0039 -0.0312 578  ARG A NH1   
4678 N  NH2   . ARG A 577 ? 0.4399 0.537  0.8652 0.0139  -0.0021 -0.0372 578  ARG A NH2   
4679 N  N     . LYS A 578 ? 0.4223 0.5558 0.863  0.0264  0.0034  -0.021  579  LYS A N     
4680 C  CA    . LYS A 578 ? 0.4506 0.588  0.891  0.0282  0.0042  -0.0191 579  LYS A CA    
4681 C  C     . LYS A 578 ? 0.4824 0.6141 0.9204 0.0253  0.0029  -0.0201 579  LYS A C     
4682 O  O     . LYS A 578 ? 0.4863 0.6125 0.9247 0.0218  0.0012  -0.0186 579  LYS A O     
4683 C  CB    . LYS A 578 ? 0.4735 0.6152 0.9177 0.0285  0.0044  -0.0128 579  LYS A CB    
4684 C  CG    . LYS A 578 ? 0.5352 0.6819 0.982  0.031   0.0055  -0.0111 579  LYS A CG    
4685 C  CD    . LYS A 578 ? 0.6087 0.7586 1.0601 0.0303  0.0053  -0.0044 579  LYS A CD    
4686 C  CE    . LYS A 578 ? 0.6683 0.8122 1.1214 0.0256  0.0029  -0.0021 579  LYS A CE    
4687 N  NZ    . LYS A 578 ? 0.6924 0.8396 1.1505 0.0248  0.0024  0.0047  579  LYS A NZ    
4688 N  N     . ILE A 579 ? 0.5057 0.6384 0.941  0.0269  0.0037  -0.0225 580  ILE A N     
4689 C  CA    . ILE A 579 ? 0.5399 0.6675 0.9726 0.0247  0.0028  -0.0235 580  ILE A CA    
4690 C  C     . ILE A 579 ? 0.5623 0.6884 0.9965 0.0226  0.0018  -0.0184 580  ILE A C     
4691 O  O     . ILE A 579 ? 0.5652 0.6852 0.9977 0.0198  0.0003  -0.0185 580  ILE A O     
4692 C  CB    . ILE A 579 ? 0.5552 0.6849 0.985  0.0271  0.004   -0.027  580  ILE A CB    
4693 C  CG1   . ILE A 579 ? 0.5764 0.6998 1.0029 0.0248  0.0032  -0.0293 580  ILE A CG1   
4694 C  CG2   . ILE A 579 ? 0.5627 0.6991 0.9933 0.03    0.0054  -0.0243 580  ILE A CG2   
4695 C  CD1   . ILE A 579 ? 0.5982 0.7166 1.0234 0.0233  0.0024  -0.0333 580  ILE A CD1   
4696 N  N     . ALA A 580 ? 0.5759 0.7075 1.0136 0.0239  0.0023  -0.0139 581  ALA A N     
4697 C  CA    . ALA A 580 ? 0.5959 0.7267 1.036  0.0219  0.0012  -0.0086 581  ALA A CA    
4698 C  C     . ALA A 580 ? 0.6128 0.7396 1.0554 0.0186  -0.0009 -0.0061 581  ALA A C     
4699 O  O     . ALA A 580 ? 0.6199 0.7416 1.0626 0.0155  -0.0028 -0.0039 581  ALA A O     
4700 C  CB    . ALA A 580 ? 0.595  0.7339 1.0382 0.025   0.0028  -0.0046 581  ALA A CB    
4701 N  N     . GLY A 581 ? 0.6153 0.7442 1.0597 0.0194  -0.0004 -0.0063 582  GLY A N     
4702 C  CA    . GLY A 581 ? 0.6243 0.7503 1.0713 0.0166  -0.0022 -0.004  582  GLY A CA    
4703 C  C     . GLY A 581 ? 0.6345 0.7524 1.0785 0.0136  -0.0038 -0.0075 582  GLY A C     
4704 O  O     . GLY A 581 ? 0.6387 0.7557 1.0808 0.0144  -0.0031 -0.0118 582  GLY A O     
4705 N  N     . ASN A 582 ? 0.3356 0.4506 0.7816 0.0124  -0.004  -0.0119 584  ASN A N     
4706 C  CA    . ASN A 582 ? 0.3391 0.4513 0.7855 0.0112  -0.0045 -0.0135 584  ASN A CA    
4707 C  C     . ASN A 582 ? 0.332  0.4471 0.7777 0.0142  -0.0025 -0.0176 584  ASN A C     
4708 O  O     . ASN A 582 ? 0.3283 0.4495 0.7748 0.0174  -0.0007 -0.0172 584  ASN A O     
4709 C  CB    . ASN A 582 ? 0.3603 0.4742 0.8109 0.0099  -0.0053 -0.0087 584  ASN A CB    
4710 C  CG    . ASN A 582 ? 0.4153 0.5249 0.8669 0.0063  -0.0079 -0.0051 584  ASN A CG    
4711 O  OD1   . ASN A 582 ? 0.4368 0.5405 0.8853 0.0043  -0.0094 -0.0066 584  ASN A OD1   
4712 N  ND2   . ASN A 582 ? 0.421  0.5332 0.8768 0.0055  -0.0087 -0.0001 584  ASN A ND2   
4713 N  N     . TRP A 583 ? 0.328  0.4387 0.7721 0.0131  -0.0028 -0.0214 585  TRP A N     
4714 C  CA    . TRP A 583 ? 0.3299 0.4426 0.7735 0.0156  -0.0012 -0.0255 585  TRP A CA    
4715 C  C     . TRP A 583 ? 0.3338 0.4504 0.7805 0.017   -0.0003 -0.0236 585  TRP A C     
4716 O  O     . TRP A 583 ? 0.3395 0.4547 0.7885 0.0149  -0.0013 -0.0207 585  TRP A O     
4717 C  CB    . TRP A 583 ? 0.3244 0.4312 0.766  0.0139  -0.0018 -0.0297 585  TRP A CB    
4718 C  CG    . TRP A 583 ? 0.3247 0.4281 0.7629 0.0134  -0.0021 -0.0325 585  TRP A CG    
4719 C  CD1   . TRP A 583 ? 0.336  0.4336 0.7723 0.0107  -0.0036 -0.0322 585  TRP A CD1   
4720 C  CD2   . TRP A 583 ? 0.3218 0.4272 0.7581 0.0158  -0.001  -0.0361 585  TRP A CD2   
4721 N  NE1   . TRP A 583 ? 0.3418 0.4378 0.7751 0.0113  -0.0033 -0.0353 585  TRP A NE1   
4722 C  CE2   . TRP A 583 ? 0.3355 0.4364 0.769  0.0143  -0.0017 -0.0377 585  TRP A CE2   
4723 C  CE3   . TRP A 583 ? 0.3233 0.4339 0.7599 0.0192  0.0005  -0.0382 585  TRP A CE3   
4724 C  CZ2   . TRP A 583 ? 0.3391 0.4407 0.7704 0.0159  -0.001  -0.041  585  TRP A CZ2   
4725 C  CZ3   . TRP A 583 ? 0.335  0.4461 0.7693 0.0207  0.001   -0.0418 585  TRP A CZ3   
4726 C  CH2   . TRP A 583 ? 0.3373 0.4441 0.7692 0.019   0.0003  -0.0431 585  TRP A CH2   
4727 N  N     . GLU A 584 ? 0.3273 0.4487 0.7739 0.0206  0.0014  -0.0255 586  GLU A N     
4728 C  CA    . GLU A 584 ? 0.3275 0.4529 0.7764 0.0228  0.0026  -0.0244 586  GLU A CA    
4729 C  C     . GLU A 584 ? 0.3332 0.4581 0.7804 0.0249  0.0036  -0.0299 586  GLU A C     
4730 O  O     . GLU A 584 ? 0.3404 0.4635 0.785  0.0252  0.0035  -0.0339 586  GLU A O     
4731 C  CB    . GLU A 584 ? 0.3597 0.4921 0.8097 0.0261  0.004   -0.0212 586  GLU A CB    
4732 C  CG    . GLU A 584 ? 0.4623 0.5963 0.9145 0.0246  0.0033  -0.0156 586  GLU A CG    
4733 C  CD    . GLU A 584 ? 0.581  0.7224 1.0343 0.0283  0.0049  -0.0125 586  GLU A CD    
4734 O  OE1   . GLU A 584 ? 0.6046 0.7491 1.0557 0.0319  0.0064  -0.0156 586  GLU A OE1   
4735 O  OE2   . GLU A 584 ? 0.6087 0.7528 1.0652 0.0276  0.0046  -0.0069 586  GLU A OE2   
4736 N  N     . PHE A 585 ? 0.3243 0.4512 0.773  0.0266  0.0045  -0.0301 587  PHE A N     
4737 C  CA    . PHE A 585 ? 0.3264 0.4533 0.7737 0.029   0.0054  -0.0351 587  PHE A CA    
4738 C  C     . PHE A 585 ? 0.3455 0.4771 0.7907 0.0329  0.0065  -0.0367 587  PHE A C     
4739 O  O     . PHE A 585 ? 0.3402 0.4764 0.786  0.0346  0.0072  -0.033  587  PHE A O     
4740 C  CB    . PHE A 585 ? 0.3134 0.4416 0.7626 0.0303  0.0062  -0.0345 587  PHE A CB    
4741 C  CG    . PHE A 585 ? 0.3093 0.4326 0.76   0.027   0.0053  -0.0347 587  PHE A CG    
4742 C  CD1   . PHE A 585 ? 0.3136 0.4317 0.7632 0.0251  0.0045  -0.0388 587  PHE A CD1   
4743 C  CD2   . PHE A 585 ? 0.3032 0.4274 0.7568 0.0262  0.0055  -0.0308 587  PHE A CD2   
4744 C  CE1   . PHE A 585 ? 0.3204 0.4342 0.7714 0.0224  0.0038  -0.0389 587  PHE A CE1   
4745 C  CE2   . PHE A 585 ? 0.309  0.429  0.764  0.0234  0.0048  -0.031  587  PHE A CE2   
4746 C  CZ    . PHE A 585 ? 0.3119 0.4267 0.7655 0.0216  0.0039  -0.0351 587  PHE A CZ    
4747 N  N     . GLY A 586 ? 0.3604 0.4907 0.8034 0.0343  0.0065  -0.042  588  GLY A N     
4748 C  CA    . GLY A 586 ? 0.38   0.5143 0.8207 0.038   0.0073  -0.0442 588  GLY A CA    
4749 C  C     . GLY A 586 ? 0.4017 0.5415 0.8428 0.0422  0.0088  -0.0426 588  GLY A C     
4750 O  O     . GLY A 586 ? 0.3996 0.539  0.8418 0.0429  0.0092  -0.0428 588  GLY A O     
4751 N  N     . ASN A 587 ? 0.4226 0.5675 0.8626 0.0451  0.0097  -0.0407 589  ASN A N     
4752 C  CA    . ASN A 587 ? 0.4504 0.6012 0.8907 0.0495  0.0113  -0.0385 589  ASN A CA    
4753 C  C     . ASN A 587 ? 0.4691 0.6229 0.9059 0.0542  0.0119  -0.0426 589  ASN A C     
4754 O  O     . ASN A 587 ? 0.4653 0.621  0.9013 0.0577  0.0128  -0.044  589  ASN A O     
4755 C  CB    . ASN A 587 ? 0.4737 0.6287 0.916  0.0493  0.0119  -0.032  589  ASN A CB    
4756 C  CG    . ASN A 587 ? 0.5308 0.6926 0.9737 0.0539  0.0137  -0.0285 589  ASN A CG    
4757 O  OD1   . ASN A 587 ? 0.5557 0.7186 0.9989 0.0561  0.0146  -0.0285 589  ASN A OD1   
4758 N  ND2   . ASN A 587 ? 0.5377 0.7042 0.9808 0.0556  0.0145  -0.0251 589  ASN A ND2   
4759 N  N     . LYS A 588 ? 0.4863 0.6405 0.921  0.0543  0.0115  -0.0445 590  LYS A N     
4760 C  CA    . LYS A 588 ? 0.5033 0.6605 0.9347 0.0586  0.0119  -0.0483 590  LYS A CA    
4761 C  C     . LYS A 588 ? 0.513  0.6657 0.9425 0.0573  0.0104  -0.0546 590  LYS A C     
4762 O  O     . LYS A 588 ? 0.5112 0.6597 0.9415 0.0532  0.0093  -0.0551 590  LYS A O     
4763 C  CB    . LYS A 588 ? 0.5341 0.6963 0.9646 0.0605  0.0127  -0.0454 590  LYS A CB    
4764 C  CG    . LYS A 588 ? 0.5995 0.7674 1.032  0.0627  0.0143  -0.0391 590  LYS A CG    
4765 C  CD    . LYS A 588 ? 0.6661 0.8388 1.0982 0.0642  0.0151  -0.0361 590  LYS A CD    
4766 C  CE    . LYS A 588 ? 0.7087 0.8865 1.144  0.0653  0.0165  -0.029  590  LYS A CE    
4767 N  NZ    . LYS A 588 ? 0.7283 0.9102 1.1638 0.0661  0.0171  -0.0258 590  LYS A NZ    
4768 N  N     . SER A 589 ? 0.519  0.6726 0.946  0.0609  0.0103  -0.0591 591  SER A N     
4769 C  CA    . SER A 589 ? 0.5267 0.6767 0.9522 0.0602  0.0087  -0.0651 591  SER A CA    
4770 C  C     . SER A 589 ? 0.5348 0.6872 0.9579 0.0613  0.0085  -0.0663 591  SER A C     
4771 O  O     . SER A 589 ? 0.5339 0.6918 0.9557 0.0647  0.0097  -0.064  591  SER A O     
4772 C  CB    . SER A 589 ? 0.543  0.6927 0.9668 0.0636  0.0084  -0.0694 591  SER A CB    
4773 O  OG    . SER A 589 ? 0.5692 0.7134 0.9949 0.0608  0.0075  -0.0718 591  SER A OG    
4774 N  N     . LEU A 590 ? 0.5404 0.6891 0.9632 0.0587  0.0071  -0.0697 592  LEU A N     
4775 C  CA    . LEU A 590 ? 0.5458 0.6966 0.9666 0.0595  0.0068  -0.071  592  LEU A CA    
4776 C  C     . LEU A 590 ? 0.5506 0.7025 0.9686 0.0631  0.0059  -0.0764 592  LEU A C     
4777 O  O     . LEU A 590 ? 0.5537 0.7031 0.9718 0.0636  0.005   -0.0799 592  LEU A O     
4778 C  CB    . LEU A 590 ? 0.5503 0.6966 0.9722 0.0548  0.0058  -0.0713 592  LEU A CB    
4779 C  CG    . LEU A 590 ? 0.5684 0.7147 0.9915 0.0521  0.0065  -0.0661 592  LEU A CG    
4780 C  CD1   . LEU A 590 ? 0.5745 0.7201 1.0001 0.0507  0.0071  -0.062  592  LEU A CD1   
4781 C  CD2   . LEU A 590 ? 0.5742 0.7157 0.9976 0.0481  0.0054  -0.0672 592  LEU A CD2   
4782 N  N     . VAL A 591 ? 0.5493 0.705  0.9648 0.0655  0.006   -0.0771 593  VAL A N     
4783 C  CA    . VAL A 591 ? 0.5527 0.7099 0.9653 0.0691  0.0049  -0.0822 593  VAL A CA    
4784 C  C     . VAL A 591 ? 0.5434 0.6984 0.9556 0.0669  0.0033  -0.0857 593  VAL A C     
4785 O  O     . VAL A 591 ? 0.5432 0.6999 0.9551 0.0659  0.0037  -0.0838 593  VAL A O     
4786 C  CB    . VAL A 591 ? 0.5686 0.7327 0.9784 0.0745  0.0064  -0.0805 593  VAL A CB    
4787 C  CG1   . VAL A 591 ? 0.5824 0.7485 0.9887 0.0781  0.0052  -0.0854 593  VAL A CG1   
4788 C  CG2   . VAL A 591 ? 0.5755 0.7414 0.9854 0.0774  0.0077  -0.0784 593  VAL A CG2   
4789 N  N     . PRO A 592 ? 0.5307 0.6819 0.9431 0.0663  0.0013  -0.0908 594  PRO A N     
4790 C  CA    . PRO A 592 ? 0.5219 0.671  0.9345 0.0641  -0.0003 -0.0939 594  PRO A CA    
4791 C  C     . PRO A 592 ? 0.5068 0.6605 0.9165 0.067   -0.0005 -0.0952 594  PRO A C     
4792 O  O     . PRO A 592 ? 0.5062 0.6594 0.9162 0.0647  -0.001  -0.0952 594  PRO A O     
4793 C  CB    . PRO A 592 ? 0.5357 0.6805 0.9494 0.0636  -0.0024 -0.0988 594  PRO A CB    
4794 C  CG    . PRO A 592 ? 0.5426 0.6886 0.9551 0.0671  -0.0019 -0.0993 594  PRO A CG    
4795 C  CD    . PRO A 592 ? 0.5234 0.6719 0.9364 0.0673  0.0005  -0.0936 594  PRO A CD    
4796 N  N     . ASN A 593 ? 0.4911 0.6494 0.8976 0.0721  -0.0001 -0.096  595  ASN A N     
4797 C  CA    . ASN A 593 ? 0.4769 0.6401 0.8804 0.0752  -0.0001 -0.0969 595  ASN A CA    
4798 C  C     . ASN A 593 ? 0.4604 0.627  0.8641 0.0744  0.0018  -0.0919 595  ASN A C     
4799 O  O     . ASN A 593 ? 0.4669 0.6367 0.8688 0.0758  0.0018  -0.0924 595  ASN A O     
4800 C  CB    . ASN A 593 ? 0.4888 0.6561 0.8886 0.0812  -0.0001 -0.0989 595  ASN A CB    
4801 C  CG    . ASN A 593 ? 0.51   0.6824 0.9063 0.085   -0.0004 -0.1005 595  ASN A CG    
4802 O  OD1   . ASN A 593 ? 0.5155 0.6873 0.9116 0.0836  -0.0018 -0.1029 595  ASN A OD1   
4803 N  ND2   . ASN A 593 ? 0.5079 0.6855 0.9011 0.0902  0.0011  -0.099  595  ASN A ND2   
4804 N  N     . ASP A 594 ? 0.4396 0.6052 0.8457 0.0719  0.0034  -0.087  596  ASP A N     
4805 C  CA    . ASP A 594 ? 0.4227 0.5905 0.8294 0.0705  0.005   -0.0822 596  ASP A CA    
4806 C  C     . ASP A 594 ? 0.4028 0.5666 0.8109 0.0659  0.0041  -0.0827 596  ASP A C     
4807 O  O     . ASP A 594 ? 0.4092 0.5739 0.8177 0.0644  0.0052  -0.079  596  ASP A O     
4808 C  CB    . ASP A 594 ? 0.4408 0.6087 0.8497 0.0695  0.0067  -0.0769 596  ASP A CB    
4809 C  CG    . ASP A 594 ? 0.4931 0.6669 0.9007 0.0742  0.0084  -0.0742 596  ASP A CG    
4810 O  OD1   . ASP A 594 ? 0.4996 0.6769 0.9043 0.0787  0.0082  -0.077  596  ASP A OD1   
4811 O  OD2   . ASP A 594 ? 0.5142 0.6891 0.9239 0.0735  0.0098  -0.0691 596  ASP A OD2   
4812 N  N     . PHE A 595 ? 0.378  0.5372 0.787  0.0638  0.0022  -0.0869 597  PHE A N     
4813 C  CA    . PHE A 595 ? 0.3649 0.5201 0.7753 0.0596  0.0014  -0.0872 597  PHE A CA    
4814 C  C     . PHE A 595 ? 0.3483 0.5028 0.7582 0.0597  -0.0005 -0.0921 597  PHE A C     
4815 O  O     . PHE A 595 ? 0.3494 0.5039 0.7586 0.0619  -0.002  -0.0961 597  PHE A O     
4816 C  CB    . PHE A 595 ? 0.3646 0.514  0.778  0.0556  0.0011  -0.0864 597  PHE A CB    
4817 C  CG    . PHE A 595 ? 0.3794 0.5287 0.7939 0.0546  0.0027  -0.0814 597  PHE A CG    
4818 C  CD1   . PHE A 595 ? 0.3912 0.5419 0.806  0.0566  0.0034  -0.0804 597  PHE A CD1   
4819 C  CD2   . PHE A 595 ? 0.3899 0.5376 0.8051 0.0517  0.0035  -0.0776 597  PHE A CD2   
4820 C  CE1   . PHE A 595 ? 0.4004 0.5513 0.8164 0.0556  0.0047  -0.0756 597  PHE A CE1   
4821 C  CE2   . PHE A 595 ? 0.4    0.5475 0.8163 0.0506  0.0047  -0.0731 597  PHE A CE2   
4822 C  CZ    . PHE A 595 ? 0.3965 0.5459 0.8135 0.0526  0.0052  -0.072  597  PHE A CZ    
4823 N  N     . ILE A 596 ? 0.3298 0.4831 0.7401 0.0573  -0.0007 -0.0917 598  ILE A N     
4824 C  CA    . ILE A 596 ? 0.3167 0.4688 0.7273 0.0566  -0.0026 -0.0957 598  ILE A CA    
4825 C  C     . ILE A 596 ? 0.3014 0.4474 0.7152 0.0524  -0.0035 -0.096  598  ILE A C     
4826 O  O     . ILE A 596 ? 0.3033 0.4467 0.7181 0.0496  -0.0023 -0.0925 598  ILE A O     
4827 C  CB    . ILE A 596 ? 0.3148 0.4697 0.724  0.0567  -0.0022 -0.0947 598  ILE A CB    
4828 C  CG1   . ILE A 596 ? 0.329  0.4903 0.7353 0.0608  -0.0009 -0.0934 598  ILE A CG1   
4829 C  CG2   . ILE A 596 ? 0.3153 0.4692 0.7253 0.0559  -0.0044 -0.0987 598  ILE A CG2   
4830 C  CD1   . ILE A 596 ? 0.3509 0.5155 0.7552 0.0649  -0.0021 -0.0971 598  ILE A CD1   
4831 N  N     . LEU A 597 ? 0.2782 0.4215 0.6936 0.052   -0.0055 -0.1001 599  LEU A N     
4832 C  CA    . LEU A 597 ? 0.2664 0.4042 0.6851 0.0482  -0.0062 -0.1003 599  LEU A CA    
4833 C  C     . LEU A 597 ? 0.2566 0.3933 0.6768 0.0467  -0.0079 -0.1028 599  LEU A C     
4834 O  O     . LEU A 597 ? 0.253  0.3911 0.673  0.0484  -0.0098 -0.1067 599  LEU A O     
4835 C  CB    . LEU A 597 ? 0.2649 0.4    0.6853 0.0483  -0.0071 -0.1023 599  LEU A CB    
4836 C  CG    . LEU A 597 ? 0.2849 0.4211 0.7044 0.0499  -0.0056 -0.1001 599  LEU A CG    
4837 C  CD1   . LEU A 597 ? 0.2896 0.4228 0.7109 0.0499  -0.0066 -0.1024 599  LEU A CD1   
4838 C  CD2   . LEU A 597 ? 0.2974 0.4324 0.7174 0.0475  -0.0037 -0.0952 599  LEU A CD2   
4839 N  N     . LEU A 598 ? 0.2472 0.3812 0.669  0.0435  -0.0073 -0.1005 600  LEU A N     
4840 C  CA    . LEU A 598 ? 0.24   0.3728 0.6636 0.0419  -0.0087 -0.1021 600  LEU A CA    
4841 C  C     . LEU A 598 ? 0.2244 0.3518 0.6515 0.0384  -0.0089 -0.1012 600  LEU A C     
4842 O  O     . LEU A 598 ? 0.224  0.3489 0.6512 0.037   -0.0075 -0.0986 600  LEU A O     
4843 C  CB    . LEU A 598 ? 0.2477 0.383  0.6695 0.0418  -0.0076 -0.0999 600  LEU A CB    
4844 C  CG    . LEU A 598 ? 0.2696 0.4106 0.6882 0.0452  -0.0075 -0.1007 600  LEU A CG    
4845 C  CD1   . LEU A 598 ? 0.2772 0.42   0.6944 0.0447  -0.0063 -0.0982 600  LEU A CD1   
4846 C  CD2   . LEU A 598 ? 0.2757 0.4185 0.6947 0.0471  -0.01   -0.1055 600  LEU A CD2   
4847 N  N     . SER A 599 ? 0.2085 0.3344 0.6386 0.037   -0.0105 -0.1033 601  SER A N     
4848 C  CA    . SER A 599 ? 0.2022 0.3234 0.6358 0.0339  -0.0106 -0.1023 601  SER A CA    
4849 C  C     . SER A 599 ? 0.1961 0.317  0.6307 0.0323  -0.0106 -0.1011 601  SER A C     
4850 O  O     . SER A 599 ? 0.2065 0.3308 0.6401 0.0336  -0.0113 -0.1021 601  SER A O     
4851 C  CB    . SER A 599 ? 0.2158 0.3348 0.653  0.0336  -0.0127 -0.1058 601  SER A CB    
4852 O  OG    . SER A 599 ? 0.2378 0.3589 0.6761 0.0345  -0.015  -0.1091 601  SER A OG    
4853 N  N     . ALA A 600 ? 0.1803 0.2974 0.6169 0.0298  -0.0098 -0.0987 602  ALA A N     
4854 C  CA    . ALA A 600 ? 0.1616 0.2781 0.5991 0.0284  -0.0095 -0.0969 602  ALA A CA    
4855 C  C     . ALA A 600 ? 0.1459 0.2581 0.5874 0.026   -0.0096 -0.096  602  ALA A C     
4856 O  O     . ALA A 600 ? 0.1556 0.2647 0.5976 0.0251  -0.009  -0.095  602  ALA A O     
4857 C  CB    . ALA A 600 ? 0.1596 0.2765 0.5931 0.0285  -0.0072 -0.0933 602  ALA A CB    
4858 N  N     . GLY A 601 ? 0.1198 0.2321 0.5642 0.0251  -0.0105 -0.0962 603  GLY A N     
4859 C  CA    . GLY A 601 ? 0.1111 0.2197 0.5595 0.023   -0.0105 -0.0949 603  GLY A CA    
4860 C  C     . GLY A 601 ? 0.1144 0.2225 0.5616 0.0223  -0.009  -0.0915 603  GLY A C     
4861 O  O     . GLY A 601 ? 0.1147 0.2259 0.561  0.0231  -0.0092 -0.0915 603  GLY A O     
4862 N  N     . ALA A 602 ? 0.1144 0.2187 0.5611 0.0211  -0.0073 -0.0884 604  ALA A N     
4863 C  CA    . ALA A 602 ? 0.1183 0.2217 0.5633 0.0208  -0.0057 -0.085  604  ALA A CA    
4864 C  C     . ALA A 602 ? 0.1159 0.2166 0.5653 0.0194  -0.0058 -0.0836 604  ALA A C     
4865 O  O     . ALA A 602 ? 0.1142 0.2124 0.5666 0.0184  -0.0062 -0.0841 604  ALA A O     
4866 C  CB    . ALA A 602 ? 0.126  0.2271 0.5658 0.0209  -0.0037 -0.0823 604  ALA A CB    
4867 N  N     . PHE A 603 ? 0.1177 0.2189 0.5675 0.0193  -0.0051 -0.0815 605  PHE A N     
4868 C  CA    . PHE A 603 ? 0.1203 0.2196 0.5746 0.0183  -0.0051 -0.0798 605  PHE A CA    
4869 C  C     . PHE A 603 ? 0.125  0.2245 0.5777 0.0187  -0.0036 -0.0765 605  PHE A C     
4870 O  O     . PHE A 603 ? 0.1246 0.2262 0.5732 0.0197  -0.0028 -0.076  605  PHE A O     
4871 C  CB    . PHE A 603 ? 0.1157 0.217  0.5767 0.0176  -0.0076 -0.0826 605  PHE A CB    
4872 C  CG    . PHE A 603 ? 0.1186 0.2244 0.5797 0.0185  -0.0091 -0.0848 605  PHE A CG    
4873 C  CD1   . PHE A 603 ? 0.1206 0.2287 0.5824 0.0187  -0.0089 -0.083  605  PHE A CD1   
4874 C  CD2   . PHE A 603 ? 0.1275 0.2355 0.5877 0.0193  -0.0108 -0.0885 605  PHE A CD2   
4875 C  CE1   . PHE A 603 ? 0.1272 0.2396 0.5888 0.0196  -0.0103 -0.0849 605  PHE A CE1   
4876 C  CE2   . PHE A 603 ? 0.1337 0.2459 0.5933 0.0203  -0.0122 -0.0905 605  PHE A CE2   
4877 C  CZ    . PHE A 603 ? 0.1293 0.2436 0.5898 0.0204  -0.012  -0.0888 605  PHE A CZ    
4878 N  N     . ILE A 604 ? 0.1273 0.2249 0.5835 0.0181  -0.003  -0.0741 606  ILE A N     
4879 C  CA    . ILE A 604 ? 0.1348 0.2329 0.5901 0.0187  -0.0016 -0.0708 606  ILE A CA    
4880 C  C     . ILE A 604 ? 0.143  0.2447 0.6046 0.0183  -0.0033 -0.0714 606  ILE A C     
4881 O  O     . ILE A 604 ? 0.1352 0.2365 0.6029 0.0172  -0.0047 -0.0722 606  ILE A O     
4882 C  CB    . ILE A 604 ? 0.1417 0.2355 0.5958 0.0187  0.0004  -0.0671 606  ILE A CB    
4883 C  CG1   . ILE A 604 ? 0.1694 0.2598 0.6162 0.0192  0.002   -0.0661 606  ILE A CG1   
4884 C  CG2   . ILE A 604 ? 0.1348 0.2294 0.5896 0.0195  0.0017  -0.0637 606  ILE A CG2   
4885 C  CD1   . ILE A 604 ? 0.1929 0.2786 0.6385 0.0192  0.0035  -0.0634 606  ILE A CD1   
4886 N  N     . ASP A 605 ? 0.1499 0.255  0.61   0.0191  -0.0031 -0.0708 607  ASP A N     
4887 C  CA    . ASP A 605 ? 0.1564 0.2651 0.6221 0.0188  -0.0047 -0.071  607  ASP A CA    
4888 C  C     . ASP A 605 ? 0.1683 0.2783 0.632  0.0198  -0.0028 -0.0673 607  ASP A C     
4889 O  O     . ASP A 605 ? 0.1759 0.2869 0.6339 0.0209  -0.0016 -0.0668 607  ASP A O     
4890 C  CB    . ASP A 605 ? 0.1785 0.2911 0.6452 0.0189  -0.0072 -0.0752 607  ASP A CB    
4891 C  CG    . ASP A 605 ? 0.2317 0.3479 0.7046 0.0183  -0.0092 -0.0753 607  ASP A CG    
4892 O  OD1   . ASP A 605 ? 0.2403 0.3556 0.7198 0.0171  -0.0105 -0.0751 607  ASP A OD1   
4893 O  OD2   . ASP A 605 ? 0.2469 0.3668 0.7182 0.0192  -0.0095 -0.0754 607  ASP A OD2   
4894 N  N     . TYR A 606 ? 0.1648 0.275  0.6335 0.0194  -0.0026 -0.0645 608  TYR A N     
4895 C  CA    . TYR A 606 ? 0.1757 0.2873 0.6429 0.0205  -0.0007 -0.0606 608  TYR A CA    
4896 C  C     . TYR A 606 ? 0.2029 0.3199 0.6739 0.0204  -0.0025 -0.0613 608  TYR A C     
4897 O  O     . TYR A 606 ? 0.2079 0.3267 0.6843 0.0202  -0.0028 -0.0588 608  TYR A O     
4898 C  CB    . TYR A 606 ? 0.1589 0.2678 0.6287 0.0207  0.0009  -0.0564 608  TYR A CB    
4899 C  CG    . TYR A 606 ? 0.152  0.2556 0.6163 0.0212  0.003   -0.0553 608  TYR A CG    
4900 C  CD1   . TYR A 606 ? 0.1579 0.2594 0.6144 0.0227  0.0054  -0.0533 608  TYR A CD1   
4901 C  CD2   . TYR A 606 ? 0.149  0.2496 0.6161 0.0203  0.0025  -0.0561 608  TYR A CD2   
4902 C  CE1   . TYR A 606 ? 0.1601 0.2565 0.6116 0.0232  0.0069  -0.0523 608  TYR A CE1   
4903 C  CE2   . TYR A 606 ? 0.1538 0.2495 0.616  0.0208  0.0042  -0.0548 608  TYR A CE2   
4904 C  CZ    . TYR A 606 ? 0.1614 0.255  0.6157 0.0222  0.0064  -0.053  608  TYR A CZ    
4905 O  OH    . TYR A 606 ? 0.1636 0.2523 0.6129 0.0227  0.0078  -0.052  608  TYR A OH    
4906 N  N     . ASP A 607 ? 0.2217 0.3414 0.69   0.0207  -0.0038 -0.0647 609  ASP A N     
4907 C  CA    . ASP A 607 ? 0.2511 0.3761 0.7219 0.0208  -0.0058 -0.0662 609  ASP A CA    
4908 C  C     . ASP A 607 ? 0.2699 0.3968 0.7495 0.0193  -0.0089 -0.0674 609  ASP A C     
4909 O  O     . ASP A 607 ? 0.2761 0.4069 0.7593 0.0192  -0.01   -0.0666 609  ASP A O     
4910 C  CB    . ASP A 607 ? 0.2893 0.4167 0.7571 0.0221  -0.0037 -0.0626 609  ASP A CB    
4911 C  CG    . ASP A 607 ? 0.3759 0.5017 0.835  0.0237  -0.0011 -0.0619 609  ASP A CG    
4912 O  OD1   . ASP A 607 ? 0.393  0.5179 0.8486 0.0237  -0.0016 -0.065  609  ASP A OD1   
4913 O  OD2   . ASP A 607 ? 0.4174 0.5426 0.8731 0.0248  0.0015  -0.0581 609  ASP A OD2   
4914 N  N     . ASN A 608 ? 0.2795 0.4038 0.7628 0.0181  -0.0103 -0.0695 610  ASN A N     
4915 C  CA    . ASN A 608 ? 0.2933 0.4187 0.7852 0.0165  -0.0135 -0.0711 610  ASN A CA    
4916 C  C     . ASN A 608 ? 0.308  0.4346 0.8004 0.0161  -0.0169 -0.0768 610  ASN A C     
4917 O  O     . ASN A 608 ? 0.3078 0.4337 0.8062 0.0148  -0.0196 -0.079  610  ASN A O     
4918 C  CB    . ASN A 608 ? 0.3028 0.4242 0.7988 0.0155  -0.0128 -0.0693 610  ASN A CB    
4919 C  CG    . ASN A 608 ? 0.3464 0.4689 0.852  0.0138  -0.0156 -0.0694 610  ASN A CG    
4920 O  OD1   . ASN A 608 ? 0.352  0.4783 0.862  0.0135  -0.0171 -0.0684 610  ASN A OD1   
4921 N  ND2   . ASN A 608 ? 0.3595 0.4789 0.869  0.0128  -0.0163 -0.0703 610  ASN A ND2   
4922 N  N     . LEU A 609 ? 0.3174 0.4458 0.8034 0.0174  -0.0167 -0.0791 611  LEU A N     
4923 C  CA    . LEU A 609 ? 0.3291 0.4589 0.8147 0.0176  -0.0196 -0.0844 611  LEU A CA    
4924 C  C     . LEU A 609 ? 0.3542 0.489  0.8387 0.0186  -0.0212 -0.0859 611  LEU A C     
4925 O  O     . LEU A 609 ? 0.3599 0.4967 0.8389 0.02    -0.0191 -0.0844 611  LEU A O     
4926 C  CB    . LEU A 609 ? 0.3239 0.4512 0.8033 0.0186  -0.0183 -0.0864 611  LEU A CB    
4927 C  CG    . LEU A 609 ? 0.333  0.4554 0.8136 0.0176  -0.0175 -0.0861 611  LEU A CG    
4928 C  CD1   . LEU A 609 ? 0.3396 0.4602 0.8138 0.0187  -0.016  -0.0873 611  LEU A CD1   
4929 C  CD2   . LEU A 609 ? 0.3375 0.459  0.8252 0.0162  -0.0207 -0.0888 611  LEU A CD2   
4930 N  N     . THR A 610 ? 0.3679 0.5047 0.8577 0.0178  -0.025  -0.0889 612  THR A N     
4931 C  CA    . THR A 610 ? 0.3919 0.5334 0.881  0.0187  -0.0272 -0.091  612  THR A CA    
4932 C  C     . THR A 610 ? 0.4152 0.5573 0.8988 0.0203  -0.0283 -0.0958 612  THR A C     
4933 O  O     . THR A 610 ? 0.4269 0.5657 0.9084 0.0205  -0.0277 -0.0974 612  THR A O     
4934 C  CB    . THR A 610 ? 0.4078 0.5509 0.9054 0.017   -0.0311 -0.0919 612  THR A CB    
4935 O  OG1   . THR A 610 ? 0.421  0.5613 0.9216 0.0162  -0.034  -0.0961 612  THR A OG1   
4936 C  CG2   . THR A 610 ? 0.4069 0.5495 0.9106 0.0154  -0.03   -0.0869 612  THR A CG2   
4937 N  N     . GLU A 611 ? 0.4184 0.5649 0.9    0.0216  -0.0301 -0.0982 613  GLU A N     
4938 C  CA    . GLU A 611 ? 0.4276 0.5751 0.9043 0.0235  -0.0314 -0.1027 613  GLU A CA    
4939 C  C     . GLU A 611 ? 0.4209 0.5654 0.9011 0.0228  -0.0346 -0.107  613  GLU A C     
4940 O  O     . GLU A 611 ? 0.4215 0.5643 0.8977 0.0241  -0.0343 -0.1096 613  GLU A O     
4941 C  CB    . GLU A 611 ? 0.4747 0.6276 0.9499 0.025   -0.0334 -0.1046 613  GLU A CB    
4942 C  CG    . GLU A 611 ? 0.5731 0.7295 1.0453 0.0258  -0.0306 -0.1007 613  GLU A CG    
4943 C  CD    . GLU A 611 ? 0.6895 0.8504 1.1656 0.0254  -0.0331 -0.1005 613  GLU A CD    
4944 O  OE1   . GLU A 611 ? 0.7169 0.879  1.1956 0.0254  -0.0372 -0.1046 613  GLU A OE1   
4945 O  OE2   . GLU A 611 ? 0.7182 0.8811 1.1946 0.0252  -0.0309 -0.0963 613  GLU A OE2   
4946 N  N     . ASN A 612 ? 0.4127 0.5565 0.9005 0.0208  -0.0377 -0.1075 614  ASN A N     
4947 C  CA    . ASN A 612 ? 0.4142 0.5549 0.9063 0.0199  -0.0411 -0.1114 614  ASN A CA    
4948 C  C     . ASN A 612 ? 0.3927 0.5285 0.8854 0.019   -0.0391 -0.1102 614  ASN A C     
4949 O  O     . ASN A 612 ? 0.3946 0.5278 0.8871 0.0193  -0.0406 -0.1138 614  ASN A O     
4950 C  CB    . ASN A 612 ? 0.451  0.5924 0.9516 0.0178  -0.0449 -0.1116 614  ASN A CB    
4951 C  CG    . ASN A 612 ? 0.5291 0.6745 1.0296 0.0187  -0.0486 -0.1149 614  ASN A CG    
4952 O  OD1   . ASN A 612 ? 0.5603 0.707  1.0549 0.021   -0.0495 -0.1186 614  ASN A OD1   
4953 N  ND2   . ASN A 612 ? 0.5408 0.6883 1.0478 0.017   -0.051  -0.1134 614  ASN A ND2   
4954 N  N     . ASP A 613 ? 0.3757 0.5103 0.8691 0.018   -0.0357 -0.1053 615  ASP A N     
4955 C  CA    . ASP A 613 ? 0.3676 0.4977 0.8612 0.0172  -0.0334 -0.1037 615  ASP A CA    
4956 C  C     . ASP A 613 ? 0.3522 0.4813 0.8382 0.0191  -0.0315 -0.1054 615  ASP A C     
4957 O  O     . ASP A 613 ? 0.3428 0.4689 0.8288 0.0191  -0.032  -0.1076 615  ASP A O     
4958 C  CB    . ASP A 613 ? 0.3877 0.517  0.8826 0.0163  -0.0301 -0.0979 615  ASP A CB    
4959 C  CG    . ASP A 613 ? 0.4393 0.5688 0.9428 0.0143  -0.0316 -0.0956 615  ASP A CG    
4960 O  OD1   . ASP A 613 ? 0.455  0.584  0.9644 0.0132  -0.0352 -0.0984 615  ASP A OD1   
4961 O  OD2   . ASP A 613 ? 0.4467 0.5767 0.951  0.014   -0.0291 -0.0908 615  ASP A OD2   
4962 N  N     . TYR A 614 ? 0.3484 0.4804 0.8281 0.0209  -0.0295 -0.1044 616  TYR A N     
4963 C  CA    . TYR A 614 ? 0.3525 0.4843 0.8252 0.0228  -0.0277 -0.1056 616  TYR A CA    
4964 C  C     . TYR A 614 ? 0.3532 0.4855 0.8248 0.0242  -0.0305 -0.1108 616  TYR A C     
4965 O  O     . TYR A 614 ? 0.3559 0.486  0.8248 0.0249  -0.0297 -0.1121 616  TYR A O     
4966 C  CB    . TYR A 614 ? 0.3524 0.4877 0.8194 0.0244  -0.0254 -0.1035 616  TYR A CB    
4967 C  CG    . TYR A 614 ? 0.3627 0.4962 0.8276 0.0238  -0.0216 -0.0986 616  TYR A CG    
4968 C  CD1   . TYR A 614 ? 0.3767 0.5067 0.8389 0.0237  -0.0193 -0.0975 616  TYR A CD1   
4969 C  CD2   . TYR A 614 ? 0.3712 0.5065 0.8369 0.0234  -0.0203 -0.0951 616  TYR A CD2   
4970 C  CE1   . TYR A 614 ? 0.3907 0.5185 0.8505 0.0233  -0.0161 -0.0932 616  TYR A CE1   
4971 C  CE2   . TYR A 614 ? 0.3864 0.5196 0.8496 0.0232  -0.0168 -0.0907 616  TYR A CE2   
4972 C  CZ    . TYR A 614 ? 0.4031 0.5324 0.8632 0.0231  -0.0149 -0.0899 616  TYR A CZ    
4973 O  OH    . TYR A 614 ? 0.4293 0.5561 0.8868 0.0229  -0.0118 -0.0858 616  TYR A OH    
4974 N  N     . GLU A 615 ? 0.3462 0.4812 0.8201 0.0245  -0.034  -0.1138 617  GLU A N     
4975 C  CA    . GLU A 615 ? 0.3529 0.4881 0.8258 0.026   -0.0372 -0.1191 617  GLU A CA    
4976 C  C     . GLU A 615 ? 0.3429 0.4734 0.8197 0.0248  -0.0385 -0.121  617  GLU A C     
4977 O  O     . GLU A 615 ? 0.3431 0.4723 0.8167 0.0264  -0.0388 -0.1238 617  GLU A O     
4978 C  CB    . GLU A 615 ? 0.3988 0.5373 0.8744 0.0262  -0.041  -0.1216 617  GLU A CB    
4979 C  CG    . GLU A 615 ? 0.4966 0.6351 0.9709 0.0279  -0.0447 -0.1274 617  GLU A CG    
4980 C  CD    . GLU A 615 ? 0.6164 0.7582 1.0927 0.0283  -0.0487 -0.13   617  GLU A CD    
4981 O  OE1   . GLU A 615 ? 0.6437 0.7848 1.1201 0.0294  -0.0525 -0.135  617  GLU A OE1   
4982 O  OE2   . GLU A 615 ? 0.6474 0.7924 1.125  0.0275  -0.0481 -0.1272 617  GLU A OE2   
4983 N  N     . LYS A 616 ? 0.3355 0.4636 0.8191 0.0221  -0.0391 -0.119  618  LYS A N     
4984 C  CA    . LYS A 616 ? 0.3391 0.4628 0.8272 0.0207  -0.0402 -0.1202 618  LYS A CA    
4985 C  C     . LYS A 616 ? 0.329  0.4498 0.8137 0.021   -0.0368 -0.1185 618  LYS A C     
4986 O  O     . LYS A 616 ? 0.341  0.4592 0.8256 0.0215  -0.0376 -0.1211 618  LYS A O     
4987 C  CB    . LYS A 616 ? 0.3792 0.5017 0.8757 0.0179  -0.0414 -0.1178 618  LYS A CB    
4988 C  CG    . LYS A 616 ? 0.4518 0.5698 0.9539 0.0162  -0.0421 -0.1182 618  LYS A CG    
4989 C  CD    . LYS A 616 ? 0.516  0.6322 1.0195 0.0168  -0.046  -0.1237 618  LYS A CD    
4990 C  CE    . LYS A 616 ? 0.5628 0.6747 1.0731 0.0148  -0.0471 -0.1237 618  LYS A CE    
4991 N  NZ    . LYS A 616 ? 0.5923 0.7016 1.1021 0.0159  -0.0498 -0.1289 618  LYS A NZ    
4992 N  N     . ILE A 617 ? 0.3089 0.4302 0.7904 0.021   -0.033  -0.1142 619  ILE A N     
4993 C  CA    . ILE A 617 ? 0.2932 0.4118 0.7712 0.0212  -0.0299 -0.1124 619  ILE A CA    
4994 C  C     . ILE A 617 ? 0.2802 0.3997 0.7522 0.0236  -0.0297 -0.1153 619  ILE A C     
4995 O  O     . ILE A 617 ? 0.2904 0.4073 0.7617 0.0238  -0.0292 -0.1161 619  ILE A O     
4996 C  CB    . ILE A 617 ? 0.2985 0.4172 0.7743 0.0206  -0.0262 -0.1072 619  ILE A CB    
4997 C  CG1   . ILE A 617 ? 0.3092 0.427  0.7912 0.0185  -0.0262 -0.1042 619  ILE A CG1   
4998 C  CG2   . ILE A 617 ? 0.3053 0.4211 0.7775 0.0208  -0.0234 -0.1055 619  ILE A CG2   
4999 C  CD1   . ILE A 617 ? 0.3289 0.4472 0.8084 0.0184  -0.023  -0.0994 619  ILE A CD1   
5000 N  N     . PHE A 618 ? 0.2616 0.3851 0.7295 0.0257  -0.0303 -0.1168 620  PHE A N     
5001 C  CA    . PHE A 618 ? 0.2558 0.3808 0.7181 0.0284  -0.0302 -0.1194 620  PHE A CA    
5002 C  C     . PHE A 618 ? 0.251  0.3741 0.7151 0.0291  -0.0333 -0.124  620  PHE A C     
5003 O  O     . PHE A 618 ? 0.2509 0.3727 0.712  0.0305  -0.0325 -0.1253 620  PHE A O     
5004 C  CB    . PHE A 618 ? 0.2564 0.3863 0.7145 0.0305  -0.0305 -0.1202 620  PHE A CB    
5005 C  CG    . PHE A 618 ? 0.2749 0.4068 0.7291 0.0309  -0.027  -0.116  620  PHE A CG    
5006 C  CD1   . PHE A 618 ? 0.2911 0.4215 0.7418 0.0312  -0.0239 -0.1136 620  PHE A CD1   
5007 C  CD2   . PHE A 618 ? 0.288  0.4232 0.7419 0.0309  -0.0268 -0.1144 620  PHE A CD2   
5008 C  CE1   . PHE A 618 ? 0.3032 0.4351 0.7502 0.0315  -0.021  -0.1099 620  PHE A CE1   
5009 C  CE2   . PHE A 618 ? 0.3019 0.4386 0.752  0.0312  -0.0236 -0.1106 620  PHE A CE2   
5010 C  CZ    . PHE A 618 ? 0.2997 0.4346 0.7464 0.0315  -0.0207 -0.1084 620  PHE A CZ    
5011 N  N     . GLU A 619 ? 0.2365 0.3592 0.7057 0.0281  -0.0368 -0.1265 621  GLU A N     
5012 C  CA    . GLU A 619 ? 0.2307 0.3512 0.7018 0.0287  -0.0401 -0.1311 621  GLU A CA    
5013 C  C     . GLU A 619 ? 0.2311 0.3469 0.7052 0.0272  -0.0391 -0.1304 621  GLU A C     
5014 O  O     . GLU A 619 ? 0.2378 0.3518 0.7101 0.0286  -0.0397 -0.1331 621  GLU A O     
5015 C  CB    . GLU A 619 ? 0.2479 0.3689 0.7244 0.0275  -0.0443 -0.1336 621  GLU A CB    
5016 N  N     . VAL A 620 ? 0.2251 0.3391 0.7037 0.0245  -0.0376 -0.1266 622  VAL A N     
5017 C  CA    . VAL A 620 ? 0.2278 0.3376 0.7098 0.0229  -0.0366 -0.1255 622  VAL A CA    
5018 C  C     . VAL A 620 ? 0.2281 0.337  0.7047 0.0241  -0.0333 -0.1241 622  VAL A C     
5019 O  O     . VAL A 620 ? 0.2283 0.3347 0.7049 0.0247  -0.0336 -0.1259 622  VAL A O     
5020 C  CB    . VAL A 620 ? 0.2393 0.3477 0.7272 0.02    -0.0357 -0.1215 622  VAL A CB    
5021 C  CG1   . VAL A 620 ? 0.2538 0.3583 0.7441 0.0187  -0.0338 -0.1195 622  VAL A CG1   
5022 C  CG2   . VAL A 620 ? 0.236  0.3447 0.7307 0.0185  -0.0392 -0.1229 622  VAL A CG2   
5023 N  N     . THR A 621 ? 0.2175 0.3285 0.6897 0.0246  -0.0304 -0.1208 623  THR A N     
5024 C  CA    . THR A 621 ? 0.2187 0.3288 0.6864 0.0254  -0.0273 -0.1188 623  THR A CA    
5025 C  C     . THR A 621 ? 0.2237 0.3362 0.6854 0.0285  -0.0271 -0.121  623  THR A C     
5026 O  O     . THR A 621 ? 0.2304 0.3415 0.6899 0.0292  -0.0257 -0.1206 623  THR A O     
5027 C  CB    . THR A 621 ? 0.222  0.3327 0.6879 0.0244  -0.0243 -0.114  623  THR A CB    
5028 O  OG1   . THR A 621 ? 0.2301 0.3448 0.6926 0.0257  -0.0242 -0.1138 623  THR A OG1   
5029 C  CG2   . THR A 621 ? 0.2172 0.3256 0.6886 0.0217  -0.024  -0.1113 623  THR A CG2   
5030 N  N     . GLY A 622 ? 0.2216 0.3378 0.6806 0.0302  -0.0283 -0.1227 624  GLY A N     
5031 C  CA    . GLY A 622 ? 0.2332 0.3522 0.6862 0.0335  -0.0278 -0.1242 624  GLY A CA    
5032 C  C     . GLY A 622 ? 0.2432 0.3642 0.6917 0.034   -0.0243 -0.1202 624  GLY A C     
5033 O  O     . GLY A 622 ? 0.2474 0.3706 0.6914 0.0365  -0.0233 -0.1205 624  GLY A O     
5034 N  N     . CYS A 623 ? 0.2431 0.3634 0.693  0.0318  -0.0225 -0.1164 625  CYS A N     
5035 C  CA    . CYS A 623 ? 0.2439 0.3654 0.6899 0.0319  -0.0194 -0.1124 625  CYS A CA    
5036 C  C     . CYS A 623 ? 0.2355 0.3617 0.6774 0.0342  -0.0193 -0.1127 625  CYS A C     
5037 O  O     . CYS A 623 ? 0.2429 0.3712 0.6861 0.0344  -0.0212 -0.1145 625  CYS A O     
5038 C  CB    . CYS A 623 ? 0.26   0.3792 0.7083 0.0292  -0.018  -0.1087 625  CYS A CB    
5039 S  SG    . CYS A 623 ? 0.3316 0.4453 0.7835 0.0268  -0.0171 -0.1071 625  CYS A SG    
5040 N  N     . ASP A 624 ? 0.2216 0.3498 0.659  0.0358  -0.0171 -0.1108 626  ASP A N     
5041 C  CA    . ASP A 624 ? 0.2224 0.3554 0.656  0.038   -0.0165 -0.1106 626  ASP A CA    
5042 C  C     . ASP A 624 ? 0.2138 0.3472 0.6473 0.0365  -0.015  -0.1071 626  ASP A C     
5043 O  O     . ASP A 624 ? 0.2158 0.3531 0.6474 0.0378  -0.0151 -0.1072 626  ASP A O     
5044 C  CB    . ASP A 624 ? 0.2602 0.3952 0.6894 0.0403  -0.0146 -0.1093 626  ASP A CB    
5045 C  CG    . ASP A 624 ? 0.3265 0.4615 0.7551 0.0423  -0.0158 -0.1124 626  ASP A CG    
5046 O  OD1   . ASP A 624 ? 0.3497 0.4874 0.7772 0.0448  -0.0178 -0.1159 626  ASP A OD1   
5047 O  OD2   . ASP A 624 ? 0.3407 0.4728 0.77   0.0416  -0.0149 -0.1114 626  ASP A OD2   
5048 N  N     . LEU A 625 ? 0.1996 0.3292 0.6349 0.0339  -0.0136 -0.1041 627  LEU A N     
5049 C  CA    . LEU A 625 ? 0.1863 0.3158 0.621  0.0327  -0.0119 -0.1006 627  LEU A CA    
5050 C  C     . LEU A 625 ? 0.179  0.3042 0.6177 0.0299  -0.012  -0.0992 627  LEU A C     
5051 O  O     . LEU A 625 ? 0.1907 0.3124 0.6312 0.0288  -0.012  -0.0992 627  LEU A O     
5052 C  CB    . LEU A 625 ? 0.1771 0.3063 0.6075 0.0331  -0.0092 -0.0972 627  LEU A CB    
5053 C  CG    . LEU A 625 ? 0.1914 0.3198 0.6203 0.0321  -0.0072 -0.0933 627  LEU A CG    
5054 C  CD1   . LEU A 625 ? 0.2018 0.3344 0.6295 0.0333  -0.0073 -0.0934 627  LEU A CD1   
5055 C  CD2   . LEU A 625 ? 0.2037 0.331  0.629  0.0322  -0.005  -0.0903 627  LEU A CD2   
5056 N  N     . LEU A 626 ? 0.1598 0.2855 0.6001 0.029   -0.012  -0.0977 628  LEU A N     
5057 C  CA    . LEU A 626 ? 0.1531 0.275  0.5969 0.0267  -0.0116 -0.0956 628  LEU A CA    
5058 C  C     . LEU A 626 ? 0.1478 0.2691 0.5885 0.0264  -0.009  -0.0915 628  LEU A C     
5059 O  O     . LEU A 626 ? 0.1523 0.2768 0.5902 0.0276  -0.0083 -0.0907 628  LEU A O     
5060 C  CB    . LEU A 626 ? 0.1508 0.2736 0.5998 0.0258  -0.0139 -0.0972 628  LEU A CB    
5061 C  CG    . LEU A 626 ? 0.1728 0.2954 0.6253 0.0258  -0.0168 -0.1014 628  LEU A CG    
5062 C  CD1   . LEU A 626 ? 0.1753 0.2995 0.6329 0.0251  -0.0194 -0.103  628  LEU A CD1   
5063 C  CD2   . LEU A 626 ? 0.1839 0.3021 0.6385 0.0246  -0.0165 -0.1013 628  LEU A CD2   
5064 N  N     . ILE A 627 ? 0.1425 0.2595 0.5832 0.025   -0.0075 -0.0888 629  ILE A N     
5065 C  CA    . ILE A 627 ? 0.145  0.2605 0.5823 0.0248  -0.0051 -0.0849 629  ILE A CA    
5066 C  C     . ILE A 627 ? 0.1458 0.2587 0.5864 0.0234  -0.0049 -0.0829 629  ILE A C     
5067 O  O     . ILE A 627 ? 0.1483 0.2576 0.5911 0.0222  -0.0048 -0.0823 629  ILE A O     
5068 C  CB    . ILE A 627 ? 0.1531 0.2656 0.5865 0.0248  -0.0035 -0.0831 629  ILE A CB    
5069 C  CG1   . ILE A 627 ? 0.1718 0.2872 0.6029 0.0262  -0.0038 -0.0851 629  ILE A CG1   
5070 C  CG2   . ILE A 627 ? 0.1511 0.262  0.5806 0.0248  -0.0013 -0.0793 629  ILE A CG2   
5071 C  CD1   . ILE A 627 ? 0.1945 0.3072 0.6226 0.026   -0.0026 -0.0834 629  ILE A CD1   
5072 N  N     . ALA A 628 ? 0.1373 0.2527 0.5788 0.0237  -0.0049 -0.0819 630  ALA A N     
5073 C  CA    . ALA A 628 ? 0.1415 0.2551 0.5864 0.0226  -0.0045 -0.0796 630  ALA A CA    
5074 C  C     . ALA A 628 ? 0.1499 0.2611 0.5904 0.023   -0.0019 -0.0756 630  ALA A C     
5075 O  O     . ALA A 628 ? 0.1579 0.2711 0.5946 0.0241  -0.0008 -0.0745 630  ALA A O     
5076 C  CB    . ALA A 628 ? 0.1341 0.2517 0.5829 0.0227  -0.0062 -0.0806 630  ALA A CB    
5077 N  N     . ILE A 629 ? 0.154  0.2608 0.5951 0.0221  -0.0008 -0.0735 631  ILE A N     
5078 C  CA    . ILE A 629 ? 0.1738 0.2772 0.6103 0.0225  0.0015  -0.0698 631  ILE A CA    
5079 C  C     . ILE A 629 ? 0.1763 0.2784 0.6156 0.0223  0.0023  -0.067  631  ILE A C     
5080 O  O     . ILE A 629 ? 0.1731 0.2752 0.6181 0.0213  0.0011  -0.0676 631  ILE A O     
5081 C  CB    . ILE A 629 ? 0.1958 0.2949 0.6302 0.0219  0.002   -0.0698 631  ILE A CB    
5082 C  CG1   . ILE A 629 ? 0.2191 0.3196 0.6503 0.0223  0.0016  -0.0717 631  ILE A CG1   
5083 C  CG2   . ILE A 629 ? 0.2071 0.3013 0.6378 0.0219  0.0039  -0.0663 631  ILE A CG2   
5084 C  CD1   . ILE A 629 ? 0.2529 0.3504 0.6841 0.0215  0.0013  -0.0725 631  ILE A CD1   
5085 N  N     . LYS A 630 ? 0.1773 0.2785 0.6129 0.0233  0.0043  -0.0638 632  LYS A N     
5086 C  CA    . LYS A 630 ? 0.1762 0.2758 0.6134 0.0235  0.0054  -0.0605 632  LYS A CA    
5087 C  C     . LYS A 630 ? 0.1696 0.2657 0.6003 0.0247  0.0079  -0.0573 632  LYS A C     
5088 O  O     . LYS A 630 ? 0.1676 0.2646 0.5935 0.0256  0.0086  -0.0572 632  LYS A O     
5089 C  CB    . LYS A 630 ? 0.2021 0.3063 0.6442 0.0236  0.0047  -0.0602 632  LYS A CB    
5090 C  CG    . LYS A 630 ? 0.2706 0.3787 0.7098 0.0247  0.0051  -0.0601 632  LYS A CG    
5091 C  CD    . LYS A 630 ? 0.3561 0.4676 0.7995 0.0249  0.0049  -0.0583 632  LYS A CD    
5092 C  CE    . LYS A 630 ? 0.4319 0.5476 0.8725 0.0261  0.0053  -0.0584 632  LYS A CE    
5093 N  NZ    . LYS A 630 ? 0.4761 0.5949 0.9165 0.0258  0.0034  -0.0625 632  LYS A NZ    
5094 N  N     . ASN A 631 ? 0.1683 0.2603 0.5985 0.0249  0.0091  -0.0546 633  ASN A N     
5095 C  CA    . ASN A 631 ? 0.1746 0.2627 0.5982 0.0264  0.0114  -0.0514 633  ASN A CA    
5096 C  C     . ASN A 631 ? 0.2035 0.2938 0.6275 0.0277  0.0127  -0.0485 633  ASN A C     
5097 O  O     . ASN A 631 ? 0.2057 0.2988 0.6356 0.0275  0.0122  -0.0479 633  ASN A O     
5098 C  CB    . ASN A 631 ? 0.1632 0.2457 0.5856 0.0264  0.0121  -0.0497 633  ASN A CB    
5099 C  CG    . ASN A 631 ? 0.1455 0.2286 0.5743 0.0261  0.0119  -0.0486 633  ASN A CG    
5100 O  OD1   . ASN A 631 ? 0.1434 0.2289 0.5782 0.0247  0.0101  -0.0509 633  ASN A OD1   
5101 N  ND2   . ASN A 631 ? 0.1169 0.1978 0.5444 0.0275  0.0137  -0.0449 633  ASN A ND2   
5102 N  N     . GLN A 632 ? 0.2236 0.3123 0.6413 0.0292  0.0144  -0.0466 634  GLN A N     
5103 C  CA    . GLN A 632 ? 0.2493 0.3391 0.6655 0.0309  0.0162  -0.0434 634  GLN A CA    
5104 C  C     . GLN A 632 ? 0.2716 0.3549 0.6822 0.0323  0.0181  -0.0404 634  GLN A C     
5105 O  O     . GLN A 632 ? 0.2853 0.3643 0.6906 0.0321  0.0181  -0.0411 634  GLN A O     
5106 C  CB    . GLN A 632 ? 0.2756 0.3682 0.6879 0.0316  0.0166  -0.0439 634  GLN A CB    
5107 C  CG    . GLN A 632 ? 0.322  0.415  0.731  0.0336  0.0188  -0.0404 634  GLN A CG    
5108 C  CD    . GLN A 632 ? 0.373  0.4682 0.778  0.0342  0.0192  -0.0411 634  GLN A CD    
5109 O  OE1   . GLN A 632 ? 0.397  0.498  0.8052 0.0337  0.0181  -0.0429 634  GLN A OE1   
5110 N  NE2   . GLN A 632 ? 0.3679 0.4587 0.7659 0.0352  0.0207  -0.0398 634  GLN A NE2   
5111 N  N     . ASN A 633 ? 0.2712 0.3535 0.6828 0.0336  0.0195  -0.037  635  ASN A N     
5112 C  CA    . ASN A 633 ? 0.2857 0.3617 0.6918 0.0352  0.0212  -0.0343 635  ASN A CA    
5113 C  C     . ASN A 633 ? 0.319  0.3922 0.7173 0.0376  0.0234  -0.0317 635  ASN A C     
5114 O  O     . ASN A 633 ? 0.3313 0.3983 0.7232 0.0386  0.0242  -0.0307 635  ASN A O     
5115 C  CB    . ASN A 633 ? 0.2795 0.355  0.6901 0.0357  0.0218  -0.032  635  ASN A CB    
5116 C  CG    . ASN A 633 ? 0.29   0.3656 0.7062 0.0336  0.0198  -0.0345 635  ASN A CG    
5117 O  OD1   . ASN A 633 ? 0.2901 0.3637 0.7045 0.0322  0.0186  -0.0374 635  ASN A OD1   
5118 N  ND2   . ASN A 633 ? 0.2827 0.3606 0.706  0.0333  0.0196  -0.0333 635  ASN A ND2   
5119 N  N     . ASN A 634 ? 0.332  0.4094 0.7306 0.0384  0.0242  -0.0305 636  ASN A N     
5120 C  CA    . ASN A 634 ? 0.3524 0.4271 0.7436 0.0408  0.0264  -0.0279 636  ASN A CA    
5121 C  C     . ASN A 634 ? 0.3503 0.4289 0.74   0.0406  0.0264  -0.0291 636  ASN A C     
5122 O  O     . ASN A 634 ? 0.3504 0.4347 0.7439 0.0409  0.0266  -0.0283 636  ASN A O     
5123 C  CB    . ASN A 634 ? 0.3835 0.4586 0.7751 0.0432  0.0286  -0.0236 636  ASN A CB    
5124 C  CG    . ASN A 634 ? 0.4555 0.5283 0.8501 0.0436  0.0288  -0.0219 636  ASN A CG    
5125 O  OD1   . ASN A 634 ? 0.4852 0.5517 0.8746 0.0448  0.0295  -0.0209 636  ASN A OD1   
5126 N  ND2   . ASN A 634 ? 0.465  0.5428 0.8682 0.0426  0.028   -0.0216 636  ASN A ND2   
5127 N  N     . PRO A 635 ? 0.3481 0.4239 0.7325 0.0403  0.026   -0.0307 637  PRO A N     
5128 C  CA    . PRO A 635 ? 0.3474 0.4168 0.7274 0.0398  0.0254  -0.0318 637  PRO A CA    
5129 C  C     . PRO A 635 ? 0.3397 0.4106 0.7248 0.0372  0.023   -0.0352 637  PRO A C     
5130 O  O     . PRO A 635 ? 0.3325 0.4093 0.723  0.0358  0.0218  -0.0373 637  PRO A O     
5131 C  CB    . PRO A 635 ? 0.3598 0.4274 0.7334 0.0403  0.0259  -0.0318 637  PRO A CB    
5132 C  CG    . PRO A 635 ? 0.3616 0.4367 0.7389 0.0399  0.0257  -0.033  637  PRO A CG    
5133 C  CD    . PRO A 635 ? 0.3406 0.4204 0.7237 0.0403  0.0261  -0.0317 637  PRO A CD    
5134 N  N     . GLN A 636 ? 0.3339 0.3994 0.7171 0.0365  0.0223  -0.0358 638  GLN A N     
5135 C  CA    . GLN A 636 ? 0.3293 0.3959 0.7171 0.0342  0.0202  -0.0388 638  GLN A CA    
5136 C  C     . GLN A 636 ? 0.3102 0.3804 0.6988 0.0328  0.0189  -0.0417 638  GLN A C     
5137 O  O     . GLN A 636 ? 0.3166 0.3846 0.7001 0.0331  0.0191  -0.0416 638  GLN A O     
5138 C  CB    . GLN A 636 ? 0.3627 0.4227 0.7473 0.034   0.0198  -0.0387 638  GLN A CB    
5139 C  CG    . GLN A 636 ? 0.4159 0.4736 0.8026 0.0347  0.0204  -0.037  638  GLN A CG    
5140 C  CD    . GLN A 636 ? 0.5012 0.5524 0.8839 0.0344  0.0198  -0.0371 638  GLN A CD    
5141 O  OE1   . GLN A 636 ? 0.529  0.575  0.9045 0.0353  0.0202  -0.0363 638  GLN A OE1   
5142 N  NE2   . GLN A 636 ? 0.5146 0.5658 0.9018 0.0332  0.0188  -0.0382 638  GLN A NE2   
5143 N  N     . LYS A 637 ? 0.2863 0.3623 0.6813 0.0316  0.0176  -0.0439 639  LYS A N     
5144 C  CA    . LYS A 637 ? 0.2732 0.3531 0.6692 0.0306  0.0163  -0.0467 639  LYS A CA    
5145 C  C     . LYS A 637 ? 0.2374 0.3209 0.6402 0.029   0.0144  -0.0496 639  LYS A C     
5146 O  O     . LYS A 637 ? 0.2311 0.3161 0.6388 0.0288  0.0141  -0.0494 639  LYS A O     
5147 C  CB    . LYS A 637 ? 0.3059 0.3907 0.7014 0.0317  0.0171  -0.0463 639  LYS A CB    
5148 C  CG    . LYS A 637 ? 0.3785 0.4611 0.7673 0.0328  0.0184  -0.0448 639  LYS A CG    
5149 C  CD    . LYS A 637 ? 0.4512 0.5387 0.8398 0.0341  0.0195  -0.0438 639  LYS A CD    
5150 C  CE    . LYS A 637 ? 0.5085 0.6003 0.8969 0.0339  0.0189  -0.0457 639  LYS A CE    
5151 N  NZ    . LYS A 637 ? 0.5486 0.6369 0.9307 0.0347  0.02    -0.0443 639  LYS A NZ    
5152 N  N     . TRP A 638 ? 0.209  0.2941 0.6124 0.028   0.0131  -0.0523 640  TRP A N     
5153 C  CA    . TRP A 638 ? 0.1816 0.2702 0.5909 0.0267  0.0112  -0.0553 640  TRP A CA    
5154 C  C     . TRP A 638 ? 0.1688 0.2636 0.5796 0.0272  0.0106  -0.0569 640  TRP A C     
5155 O  O     . TRP A 638 ? 0.1742 0.2701 0.5815 0.0277  0.011   -0.0572 640  TRP A O     
5156 C  CB    . TRP A 638 ? 0.1682 0.2544 0.5769 0.0256  0.0101  -0.057  640  TRP A CB    
5157 C  CG    . TRP A 638 ? 0.1601 0.2413 0.5692 0.0248  0.0101  -0.0562 640  TRP A CG    
5158 C  CD1   . TRP A 638 ? 0.1678 0.2435 0.5724 0.0247  0.0105  -0.0549 640  TRP A CD1   
5159 C  CD2   . TRP A 638 ? 0.1503 0.2314 0.5647 0.0241  0.0094  -0.0567 640  TRP A CD2   
5160 N  NE1   . TRP A 638 ? 0.1654 0.2378 0.5719 0.0241  0.0103  -0.0545 640  TRP A NE1   
5161 C  CE2   . TRP A 638 ? 0.157  0.2327 0.5696 0.0237  0.0097  -0.0556 640  TRP A CE2   
5162 C  CE3   . TRP A 638 ? 0.1512 0.2363 0.5718 0.0238  0.0085  -0.0579 640  TRP A CE3   
5163 C  CZ2   . TRP A 638 ? 0.1593 0.2336 0.5762 0.0231  0.0094  -0.0555 640  TRP A CZ2   
5164 C  CZ3   . TRP A 638 ? 0.1543 0.2379 0.5795 0.023   0.008   -0.0579 640  TRP A CZ3   
5165 C  CH2   . TRP A 638 ? 0.1555 0.2339 0.5788 0.0227  0.0086  -0.0566 640  TRP A CH2   
5166 N  N     . VAL A 639 ? 0.1555 0.2542 0.5714 0.027   0.0098  -0.0579 641  VAL A N     
5167 C  CA    . VAL A 639 ? 0.1584 0.2632 0.5761 0.0275  0.0089  -0.0597 641  VAL A CA    
5168 C  C     . VAL A 639 ? 0.1613 0.2685 0.5828 0.0266  0.0067  -0.0635 641  VAL A C     
5169 O  O     . VAL A 639 ? 0.1533 0.2597 0.5794 0.0255  0.0054  -0.0647 641  VAL A O     
5170 C  CB    . VAL A 639 ? 0.1673 0.2752 0.5883 0.028   0.0091  -0.0583 641  VAL A CB    
5171 C  CG1   . VAL A 639 ? 0.1693 0.2836 0.5923 0.0284  0.0079  -0.0604 641  VAL A CG1   
5172 C  CG2   . VAL A 639 ? 0.1723 0.2776 0.5889 0.0293  0.0116  -0.0543 641  VAL A CG2   
5173 N  N     . ILE A 640 ? 0.1665 0.2762 0.5858 0.0271  0.0063  -0.0652 642  ILE A N     
5174 C  CA    . ILE A 640 ? 0.176  0.2878 0.5977 0.0267  0.0044  -0.0687 642  ILE A CA    
5175 C  C     . ILE A 640 ? 0.1995 0.3175 0.6232 0.0276  0.0031  -0.0711 642  ILE A C     
5176 O  O     . ILE A 640 ? 0.2134 0.3342 0.634  0.0289  0.004   -0.0704 642  ILE A O     
5177 C  CB    . ILE A 640 ? 0.1705 0.2805 0.5885 0.0268  0.0049  -0.0689 642  ILE A CB    
5178 C  CG1   . ILE A 640 ? 0.1804 0.2843 0.595  0.0262  0.0063  -0.066  642  ILE A CG1   
5179 C  CG2   . ILE A 640 ? 0.1679 0.279  0.5887 0.0264  0.003   -0.0722 642  ILE A CG2   
5180 C  CD1   . ILE A 640 ? 0.1955 0.2954 0.6128 0.0249  0.0058  -0.066  642  ILE A CD1   
5181 N  N     . LYS A 641 ? 0.2051 0.3248 0.6335 0.027   0.0008  -0.0741 643  LYS A N     
5182 C  CA    . LYS A 641 ? 0.2259 0.351  0.6563 0.0278  -0.001  -0.077  643  LYS A CA    
5183 C  C     . LYS A 641 ? 0.2348 0.3607 0.6658 0.0281  -0.0026 -0.0805 643  LYS A C     
5184 O  O     . LYS A 641 ? 0.2395 0.3628 0.6736 0.0269  -0.0037 -0.0819 643  LYS A O     
5185 C  CB    . LYS A 641 ? 0.261  0.3874 0.6971 0.027   -0.0025 -0.0774 643  LYS A CB    
5186 C  CG    . LYS A 641 ? 0.3311 0.463  0.7692 0.0278  -0.0046 -0.0802 643  LYS A CG    
5187 C  CD    . LYS A 641 ? 0.3937 0.5267 0.8376 0.0267  -0.0062 -0.0801 643  LYS A CD    
5188 C  CE    . LYS A 641 ? 0.4532 0.5916 0.8989 0.0275  -0.0085 -0.0826 643  LYS A CE    
5189 N  NZ    . LYS A 641 ? 0.479  0.6186 0.931  0.0263  -0.0103 -0.0823 643  LYS A NZ    
5190 N  N     . PHE A 642 ? 0.239  0.3685 0.667  0.0297  -0.0025 -0.0817 644  PHE A N     
5191 C  CA    . PHE A 642 ? 0.2471 0.3776 0.6751 0.0304  -0.0039 -0.0848 644  PHE A CA    
5192 C  C     . PHE A 642 ? 0.2527 0.3876 0.6831 0.0314  -0.0063 -0.0884 644  PHE A C     
5193 O  O     . PHE A 642 ? 0.2573 0.3965 0.6863 0.0328  -0.0062 -0.0885 644  PHE A O     
5194 C  CB    . PHE A 642 ? 0.2515 0.3833 0.6746 0.0319  -0.0022 -0.0838 644  PHE A CB    
5195 C  CG    . PHE A 642 ? 0.2658 0.3929 0.6865 0.0309  -0.0003 -0.0807 644  PHE A CG    
5196 C  CD1   . PHE A 642 ? 0.277  0.4008 0.6985 0.03    -0.0007 -0.0812 644  PHE A CD1   
5197 C  CD2   . PHE A 642 ? 0.2767 0.4028 0.6942 0.031   0.0017  -0.0773 644  PHE A CD2   
5198 C  CE1   . PHE A 642 ? 0.288  0.4075 0.7072 0.029   0.0008  -0.0784 644  PHE A CE1   
5199 C  CE2   . PHE A 642 ? 0.2876 0.409  0.7026 0.0301  0.0032  -0.0747 644  PHE A CE2   
5200 C  CZ    . PHE A 642 ? 0.2863 0.4044 0.7022 0.0291  0.0026  -0.0753 644  PHE A CZ    
5201 N  N     . LYS A 643 ? 0.2518 0.3856 0.686  0.0307  -0.0086 -0.0914 645  LYS A N     
5202 C  CA    . LYS A 643 ? 0.2588 0.3961 0.6955 0.0315  -0.0114 -0.0951 645  LYS A CA    
5203 C  C     . LYS A 643 ? 0.2619 0.4003 0.6972 0.0331  -0.0126 -0.0985 645  LYS A C     
5204 O  O     . LYS A 643 ? 0.2628 0.3982 0.7002 0.0323  -0.0135 -0.1    645  LYS A O     
5205 C  CB    . LYS A 643 ? 0.2918 0.427  0.7345 0.0295  -0.0134 -0.096  645  LYS A CB    
5206 C  CG    . LYS A 643 ? 0.3754 0.5121 0.8203 0.0287  -0.0132 -0.0937 645  LYS A CG    
5207 C  CD    . LYS A 643 ? 0.4501 0.5918 0.896  0.0299  -0.0155 -0.0963 645  LYS A CD    
5208 C  CE    . LYS A 643 ? 0.5083 0.6513 0.9583 0.0287  -0.0163 -0.0947 645  LYS A CE    
5209 N  NZ    . LYS A 643 ? 0.5456 0.6937 0.9961 0.0299  -0.0186 -0.0971 645  LYS A NZ    
5210 N  N     . PRO A 644 ? 0.2568 0.3996 0.6885 0.0355  -0.0125 -0.0995 646  PRO A N     
5211 C  CA    . PRO A 644 ? 0.2597 0.4038 0.6897 0.0375  -0.0135 -0.1026 646  PRO A CA    
5212 C  C     . PRO A 644 ? 0.2714 0.4167 0.7041 0.0382  -0.017  -0.1072 646  PRO A C     
5213 O  O     . PRO A 644 ? 0.2709 0.4184 0.7056 0.0379  -0.0187 -0.1082 646  PRO A O     
5214 C  CB    . PRO A 644 ? 0.264  0.4125 0.6892 0.0401  -0.0118 -0.1014 646  PRO A CB    
5215 C  CG    . PRO A 644 ? 0.2653 0.4161 0.6904 0.0398  -0.0112 -0.0995 646  PRO A CG    
5216 C  CD    . PRO A 644 ? 0.2462 0.3931 0.6751 0.0368  -0.0112 -0.0978 646  PRO A CD    
5217 N  N     . LYS A 645 ? 0.278  0.4219 0.7109 0.0389  -0.0182 -0.11   647  LYS A N     
5218 C  CA    . LYS A 645 ? 0.2985 0.443  0.7334 0.0398  -0.0217 -0.1146 647  LYS A CA    
5219 C  C     . LYS A 645 ? 0.3206 0.47   0.7514 0.0433  -0.0224 -0.117  647  LYS A C     
5220 O  O     . LYS A 645 ? 0.3213 0.4728 0.753  0.0442  -0.0253 -0.1203 647  LYS A O     
5221 C  CB    . LYS A 645 ? 0.3169 0.4573 0.7536 0.0393  -0.0226 -0.1166 647  LYS A CB    
5222 C  CG    . LYS A 645 ? 0.3607 0.5008 0.7999 0.0399  -0.0265 -0.1216 647  LYS A CG    
5223 C  CD    . LYS A 645 ? 0.431  0.567  0.8718 0.0396  -0.0274 -0.1236 647  LYS A CD    
5224 C  CE    . LYS A 645 ? 0.5043 0.6413 0.9404 0.0423  -0.0256 -0.1236 647  LYS A CE    
5225 N  NZ    . LYS A 645 ? 0.5539 0.6873 0.9913 0.0424  -0.0267 -0.1259 647  LYS A NZ    
5226 N  N     . ASN A 646 ? 0.3316 0.483  0.7578 0.0454  -0.0199 -0.1153 648  ASN A N     
5227 C  CA    . ASN A 646 ? 0.3471 0.5033 0.7691 0.0493  -0.0202 -0.1171 648  ASN A CA    
5228 C  C     . ASN A 646 ? 0.3624 0.5221 0.7805 0.0507  -0.017  -0.1133 648  ASN A C     
5229 O  O     . ASN A 646 ? 0.3707 0.5288 0.7894 0.0485  -0.0147 -0.1094 648  ASN A O     
5230 C  CB    . ASN A 646 ? 0.36   0.5148 0.7807 0.0512  -0.0209 -0.1197 648  ASN A CB    
5231 C  CG    . ASN A 646 ? 0.4029 0.5541 0.8241 0.0497  -0.0186 -0.1169 648  ASN A CG    
5232 O  OD1   . ASN A 646 ? 0.4235 0.5749 0.8433 0.049   -0.0158 -0.1128 648  ASN A OD1   
5233 N  ND2   . ASN A 646 ? 0.4066 0.554  0.8297 0.0491  -0.0199 -0.119  648  ASN A ND2   
5234 N  N     . THR A 647 ? 0.3631 0.5277 0.7773 0.0544  -0.0168 -0.1145 649  THR A N     
5235 C  CA    . THR A 647 ? 0.3675 0.5362 0.7783 0.0562  -0.0139 -0.111  649  THR A CA    
5236 C  C     . THR A 647 ? 0.3608 0.5276 0.7705 0.0557  -0.011  -0.1073 649  THR A C     
5237 O  O     . THR A 647 ? 0.3623 0.5303 0.7706 0.0554  -0.0085 -0.1035 649  THR A O     
5238 C  CB    . THR A 647 ? 0.3915 0.5659 0.7985 0.0606  -0.0147 -0.1134 649  THR A CB    
5239 O  OG1   . THR A 647 ? 0.4102 0.584  0.8161 0.0628  -0.0158 -0.1162 649  THR A OG1   
5240 C  CG2   . THR A 647 ? 0.3924 0.5694 0.8002 0.061   -0.0173 -0.1163 649  THR A CG2   
5241 N  N     . ILE A 648 ? 0.3536 0.5173 0.764  0.0556  -0.0114 -0.1084 650  ILE A N     
5242 C  CA    . ILE A 648 ? 0.3511 0.5129 0.7608 0.0549  -0.0089 -0.1048 650  ILE A CA    
5243 C  C     . ILE A 648 ? 0.3291 0.4864 0.7412 0.0509  -0.0077 -0.1017 650  ILE A C     
5244 O  O     . ILE A 648 ? 0.3268 0.4841 0.7376 0.0503  -0.0054 -0.0978 650  ILE A O     
5245 C  CB    . ILE A 648 ? 0.3714 0.5315 0.7813 0.056   -0.0095 -0.1066 650  ILE A CB    
5246 C  CG1   . ILE A 648 ? 0.393  0.5582 0.7994 0.0607  -0.0098 -0.1085 650  ILE A CG1   
5247 C  CG2   . ILE A 648 ? 0.3798 0.5369 0.7902 0.0543  -0.0074 -0.1029 650  ILE A CG2   
5248 C  CD1   . ILE A 648 ? 0.4137 0.5835 0.8171 0.063   -0.0069 -0.1046 650  ILE A CD1   
5249 N  N     . ALA A 649 ? 0.3138 0.4672 0.7292 0.0483  -0.0095 -0.1034 651  ALA A N     
5250 C  CA    . ALA A 649 ? 0.3065 0.4557 0.7241 0.0448  -0.0085 -0.1006 651  ALA A CA    
5251 C  C     . ALA A 649 ? 0.3024 0.4536 0.7188 0.0445  -0.0072 -0.098  651  ALA A C     
5252 O  O     . ALA A 649 ? 0.2958 0.4443 0.7118 0.0427  -0.0053 -0.0945 651  ALA A O     
5253 C  CB    . ALA A 649 ? 0.3033 0.4488 0.7251 0.0426  -0.0107 -0.1029 651  ALA A CB    
5254 N  N     . GLU A 650 ? 0.3022 0.4581 0.7175 0.0465  -0.008  -0.0996 652  GLU A N     
5255 C  CA    . GLU A 650 ? 0.3092 0.4677 0.7231 0.0466  -0.0067 -0.0972 652  GLU A CA    
5256 C  C     . GLU A 650 ? 0.304  0.4639 0.7146 0.0477  -0.0038 -0.0935 652  GLU A C     
5257 O  O     . GLU A 650 ? 0.3056 0.4644 0.7155 0.0464  -0.002  -0.0901 652  GLU A O     
5258 C  CB    . GLU A 650 ? 0.3506 0.5141 0.7641 0.0487  -0.0084 -0.1    652  GLU A CB    
5259 C  CG    . GLU A 650 ? 0.4349 0.6012 0.8473 0.0488  -0.0071 -0.0975 652  GLU A CG    
5260 C  CD    . GLU A 650 ? 0.5426 0.7132 0.9557 0.05    -0.0093 -0.1002 652  GLU A CD    
5261 O  OE1   . GLU A 650 ? 0.5523 0.724  0.966  0.0513  -0.0119 -0.1043 652  GLU A OE1   
5262 O  OE2   . GLU A 650 ? 0.5765 0.7492 0.9893 0.0498  -0.0084 -0.0982 652  GLU A OE2   
5263 N  N     . LYS A 651 ? 0.2931 0.4554 0.7018 0.0501  -0.0034 -0.0939 653  LYS A N     
5264 C  CA    . LYS A 651 ? 0.2933 0.457  0.6994 0.0512  -0.0008 -0.0902 653  LYS A CA    
5265 C  C     . LYS A 651 ? 0.2847 0.4428 0.6916 0.0482  0.0005  -0.0871 653  LYS A C     
5266 O  O     . LYS A 651 ? 0.2903 0.448  0.6957 0.0477  0.0024  -0.0834 653  LYS A O     
5267 C  CB    . LYS A 651 ? 0.3213 0.4888 0.7257 0.0544  -0.0008 -0.0913 653  LYS A CB    
5268 C  CG    . LYS A 651 ? 0.3787 0.5523 0.7813 0.0579  -0.0016 -0.0937 653  LYS A CG    
5269 C  CD    . LYS A 651 ? 0.4465 0.6246 0.8467 0.0617  -0.0006 -0.0933 653  LYS A CD    
5270 C  CE    . LYS A 651 ? 0.5042 0.6888 0.9019 0.065   0       -0.0931 653  LYS A CE    
5271 N  NZ    . LYS A 651 ? 0.5374 0.7268 0.9327 0.0692  0.0005  -0.0935 653  LYS A NZ    
5272 N  N     . LEU A 652 ? 0.2675 0.421  0.6768 0.0462  -0.0007 -0.0885 654  LEU A N     
5273 C  CA    . LEU A 652 ? 0.2574 0.4053 0.6676 0.0434  0.0002  -0.0859 654  LEU A CA    
5274 C  C     . LEU A 652 ? 0.259  0.4042 0.6693 0.0413  0.0009  -0.0839 654  LEU A C     
5275 O  O     . LEU A 652 ? 0.2652 0.4078 0.6741 0.0401  0.0025  -0.0805 654  LEU A O     
5276 C  CB    . LEU A 652 ? 0.25   0.394  0.6628 0.042   -0.0014 -0.0882 654  LEU A CB    
5277 C  CG    . LEU A 652 ? 0.2627 0.4007 0.6767 0.039   -0.0007 -0.0859 654  LEU A CG    
5278 C  CD1   . LEU A 652 ? 0.2678 0.4051 0.6798 0.0389  0.0011  -0.0823 654  LEU A CD1   
5279 C  CD2   . LEU A 652 ? 0.2734 0.4085 0.6903 0.0379  -0.0022 -0.0883 654  LEU A CD2   
5280 N  N     . VAL A 653 ? 0.2487 0.3947 0.6606 0.0409  -0.0004 -0.0859 655  VAL A N     
5281 C  CA    . VAL A 653 ? 0.2566 0.4006 0.6687 0.0393  0.0003  -0.0839 655  VAL A CA    
5282 C  C     . VAL A 653 ? 0.2635 0.4098 0.6725 0.0404  0.0024  -0.0808 655  VAL A C     
5283 O  O     . VAL A 653 ? 0.2656 0.4083 0.6733 0.039   0.0039  -0.0777 655  VAL A O     
5284 C  CB    . VAL A 653 ? 0.2607 0.4061 0.6756 0.0391  -0.0016 -0.0866 655  VAL A CB    
5285 C  CG1   . VAL A 653 ? 0.265  0.4096 0.68   0.038   -0.0006 -0.0842 655  VAL A CG1   
5286 C  CG2   . VAL A 653 ? 0.2642 0.4062 0.6829 0.0375  -0.0035 -0.089  655  VAL A CG2   
5287 N  N     . ASN A 654 ? 0.2634 0.4155 0.6707 0.043   0.0025  -0.0816 656  ASN A N     
5288 C  CA    . ASN A 654 ? 0.2693 0.4241 0.6738 0.0443  0.0046  -0.0787 656  ASN A CA    
5289 C  C     . ASN A 654 ? 0.2714 0.4235 0.6742 0.0438  0.0063  -0.0754 656  ASN A C     
5290 O  O     . ASN A 654 ? 0.2821 0.4332 0.6829 0.0435  0.008   -0.0722 656  ASN A O     
5291 C  CB    . ASN A 654 ? 0.2856 0.4473 0.6888 0.0475  0.0044  -0.0802 656  ASN A CB    
5292 C  CG    . ASN A 654 ? 0.3334 0.4982 0.738  0.0481  0.0026  -0.0831 656  ASN A CG    
5293 O  OD1   . ASN A 654 ? 0.3638 0.5262 0.7701 0.0462  0.0021  -0.0831 656  ASN A OD1   
5294 N  ND2   . ASN A 654 ? 0.3394 0.5095 0.7433 0.0509  0.0016  -0.0856 656  ASN A ND2   
5295 N  N     . TYR A 655 ? 0.2592 0.41   0.6627 0.0437  0.0057  -0.0761 657  TYR A N     
5296 C  CA    . TYR A 655 ? 0.2566 0.4048 0.659  0.043   0.007   -0.0729 657  TYR A CA    
5297 C  C     . TYR A 655 ? 0.2707 0.4121 0.673  0.0401  0.0074  -0.0708 657  TYR A C     
5298 O  O     . TYR A 655 ? 0.274  0.4133 0.6746 0.0395  0.0088  -0.0675 657  TYR A O     
5299 C  CB    . TYR A 655 ? 0.2392 0.3879 0.6428 0.0437  0.0062  -0.0742 657  TYR A CB    
5300 C  CG    . TYR A 655 ? 0.2323 0.3778 0.6356 0.0425  0.0071  -0.0711 657  TYR A CG    
5301 C  CD1   . TYR A 655 ? 0.2358 0.3844 0.6378 0.044   0.0084  -0.0683 657  TYR A CD1   
5302 C  CD2   . TYR A 655 ? 0.2377 0.3773 0.6422 0.0398  0.0065  -0.0709 657  TYR A CD2   
5303 C  CE1   . TYR A 655 ? 0.2397 0.3852 0.6418 0.0427  0.009   -0.0653 657  TYR A CE1   
5304 C  CE2   . TYR A 655 ? 0.2423 0.3787 0.6465 0.0386  0.0071  -0.068  657  TYR A CE2   
5305 C  CZ    . TYR A 655 ? 0.2475 0.3869 0.6507 0.0399  0.0082  -0.0652 657  TYR A CZ    
5306 O  OH    . TYR A 655 ? 0.2534 0.3898 0.6567 0.0385  0.0085  -0.0622 657  TYR A OH    
5307 N  N     . ILE A 656 ? 0.2748 0.4127 0.6792 0.0383  0.0062  -0.0727 658  ILE A N     
5308 C  CA    . ILE A 656 ? 0.2869 0.4185 0.6913 0.0358  0.0064  -0.071  658  ILE A CA    
5309 C  C     . ILE A 656 ? 0.3037 0.4346 0.7059 0.0358  0.0078  -0.0687 658  ILE A C     
5310 O  O     . ILE A 656 ? 0.3034 0.4301 0.7034 0.0348  0.0089  -0.0658 658  ILE A O     
5311 C  CB    . ILE A 656 ? 0.2854 0.4144 0.6929 0.0344  0.0049  -0.0736 658  ILE A CB    
5312 C  CG1   . ILE A 656 ? 0.2873 0.416  0.6968 0.0343  0.0037  -0.0755 658  ILE A CG1   
5313 C  CG2   . ILE A 656 ? 0.2921 0.4152 0.6995 0.0323  0.0053  -0.0717 658  ILE A CG2   
5314 C  CD1   . ILE A 656 ? 0.2984 0.4258 0.7114 0.0333  0.002   -0.0786 658  ILE A CD1   
5315 N  N     . LYS A 657 ? 0.3161 0.4513 0.7186 0.0371  0.0077  -0.0699 659  LYS A N     
5316 C  CA    . LYS A 657 ? 0.3369 0.4725 0.7374 0.0374  0.0091  -0.0678 659  LYS A CA    
5317 C  C     . LYS A 657 ? 0.3607 0.497  0.758  0.0384  0.0108  -0.0648 659  LYS A C     
5318 O  O     . LYS A 657 ? 0.378  0.5107 0.7731 0.0377  0.0121  -0.062  659  LYS A O     
5319 C  CB    . LYS A 657 ? 0.3572 0.4983 0.759  0.0389  0.0084  -0.0699 659  LYS A CB    
5320 C  CG    . LYS A 657 ? 0.4073 0.5467 0.8119 0.0375  0.0072  -0.0713 659  LYS A CG    
5321 C  CD    . LYS A 657 ? 0.4667 0.6106 0.8742 0.0384  0.0052  -0.075  659  LYS A CD    
5322 C  CE    . LYS A 657 ? 0.5148 0.6634 0.9222 0.0396  0.0052  -0.0751 659  LYS A CE    
5323 N  NZ    . LYS A 657 ? 0.5409 0.6913 0.9522 0.0392  0.0028  -0.0782 659  LYS A NZ    
5324 N  N     . LEU A 658 ? 0.3631 0.5039 0.7603 0.0401  0.0109  -0.0651 660  LEU A N     
5325 C  CA    . LEU A 658 ? 0.3781 0.5202 0.773  0.0411  0.0125  -0.0621 660  LEU A CA    
5326 C  C     . LEU A 658 ? 0.3789 0.515  0.7727 0.0393  0.0129  -0.0595 660  LEU A C     
5327 O  O     . LEU A 658 ? 0.3813 0.5157 0.7728 0.0393  0.0142  -0.0565 660  LEU A O     
5328 C  CB    . LEU A 658 ? 0.3906 0.5391 0.786  0.0436  0.0125  -0.063  660  LEU A CB    
5329 C  CG    . LEU A 658 ? 0.4233 0.5782 0.8175 0.0461  0.0135  -0.0626 660  LEU A CG    
5330 C  CD1   . LEU A 658 ? 0.4356 0.5924 0.8304 0.0463  0.0128  -0.065  660  LEU A CD1   
5331 C  CD2   . LEU A 658 ? 0.4323 0.5933 0.8268 0.0488  0.0135  -0.0633 660  LEU A CD2   
5332 N  N     . ASN A 659 ? 0.3769 0.5097 0.7723 0.0378  0.0117  -0.0606 661  ASN A N     
5333 C  CA    . ASN A 659 ? 0.3794 0.5066 0.7741 0.036   0.0117  -0.0584 661  ASN A CA    
5334 C  C     . ASN A 659 ? 0.3675 0.4877 0.7614 0.0338  0.0114  -0.058  661  ASN A C     
5335 O  O     . ASN A 659 ? 0.3664 0.4817 0.7601 0.0322  0.0109  -0.0569 661  ASN A O     
5336 C  CB    . ASN A 659 ? 0.4081 0.5363 0.8049 0.0359  0.0107  -0.0593 661  ASN A CB    
5337 C  CG    . ASN A 659 ? 0.4678 0.602  0.8647 0.0382  0.0113  -0.0586 661  ASN A CG    
5338 O  OD1   . ASN A 659 ? 0.4808 0.6205 0.8789 0.0402  0.011   -0.061  661  ASN A OD1   
5339 N  ND2   . ASN A 659 ? 0.4831 0.6166 0.8789 0.0381  0.0122  -0.0552 661  ASN A ND2   
5340 N  N     . PHE A 660 ? 0.3535 0.4734 0.7472 0.0339  0.0116  -0.0588 662  PHE A N     
5341 C  CA    . PHE A 660 ? 0.3491 0.4627 0.742  0.0323  0.0115  -0.0581 662  PHE A CA    
5342 C  C     . PHE A 660 ? 0.3556 0.4654 0.7445 0.0322  0.0129  -0.0549 662  PHE A C     
5343 O  O     . PHE A 660 ? 0.355  0.4639 0.7422 0.0327  0.0138  -0.054  662  PHE A O     
5344 C  CB    . PHE A 660 ? 0.3377 0.4528 0.7323 0.0325  0.0113  -0.0599 662  PHE A CB    
5345 C  CG    . PHE A 660 ? 0.3341 0.4438 0.7297 0.0308  0.0107  -0.0602 662  PHE A CG    
5346 C  CD1   . PHE A 660 ? 0.3331 0.4424 0.732  0.0298  0.0092  -0.0625 662  PHE A CD1   
5347 C  CD2   . PHE A 660 ? 0.3383 0.4432 0.7314 0.0303  0.0116  -0.058  662  PHE A CD2   
5348 C  CE1   . PHE A 660 ? 0.339  0.4435 0.739  0.0284  0.0088  -0.0625 662  PHE A CE1   
5349 C  CE2   . PHE A 660 ? 0.3453 0.4453 0.7392 0.0291  0.0112  -0.058  662  PHE A CE2   
5350 C  CZ    . PHE A 660 ? 0.3397 0.4397 0.7371 0.0281  0.0098  -0.0602 662  PHE A CZ    
5351 N  N     . LYS A 661 ? 0.3549 0.4624 0.7425 0.0317  0.0129  -0.053  663  LYS A N     
5352 C  CA    . LYS A 661 ? 0.3676 0.471  0.7515 0.0315  0.0138  -0.0499 663  LYS A CA    
5353 C  C     . LYS A 661 ? 0.3588 0.4568 0.7423 0.0297  0.0127  -0.0488 663  LYS A C     
5354 O  O     . LYS A 661 ? 0.359  0.4586 0.7452 0.0292  0.0117  -0.0499 663  LYS A O     
5355 C  CB    . LYS A 661 ? 0.407  0.5158 0.7905 0.0332  0.0148  -0.0486 663  LYS A CB    
5356 C  CG    . LYS A 661 ? 0.4895 0.5947 0.8692 0.0333  0.016   -0.0455 663  LYS A CG    
5357 C  CD    . LYS A 661 ? 0.5636 0.6718 0.9437 0.034   0.0163  -0.0434 663  LYS A CD    
5358 C  CE    . LYS A 661 ? 0.622  0.7263 0.9986 0.0341  0.0173  -0.0404 663  LYS A CE    
5359 N  NZ    . LYS A 661 ? 0.6559 0.763  1.0334 0.0346  0.0175  -0.0381 663  LYS A NZ    
5360 N  N     . SER A 662 ? 0.3533 0.4448 0.7333 0.0289  0.0128  -0.0466 664  SER A N     
5361 C  CA    . SER A 662 ? 0.3559 0.4418 0.7352 0.0272  0.0116  -0.0454 664  SER A CA    
5362 C  C     . SER A 662 ? 0.3638 0.4432 0.7388 0.0267  0.0117  -0.0428 664  SER A C     
5363 O  O     . SER A 662 ? 0.367  0.4434 0.7388 0.0274  0.0126  -0.0423 664  SER A O     
5364 C  CB    . SER A 662 ? 0.3659 0.4485 0.7465 0.0258  0.0105  -0.0471 664  SER A CB    
5365 O  OG    . SER A 662 ? 0.3881 0.466  0.7684 0.0242  0.0091  -0.0461 664  SER A OG    
5366 N  N     . ASN A 663 ? 0.3656 0.4425 0.7403 0.0256  0.0107  -0.041  665  ASN A N     
5367 C  CA    . ASN A 663 ? 0.375  0.4448 0.7456 0.0249  0.0103  -0.0386 665  ASN A CA    
5368 C  C     . ASN A 663 ? 0.3628 0.425  0.7314 0.0235  0.0089  -0.039  665  ASN A C     
5369 O  O     . ASN A 663 ? 0.3763 0.4317 0.7404 0.0234  0.0087  -0.0377 665  ASN A O     
5370 C  CB    . ASN A 663 ? 0.4059 0.4765 0.7777 0.0243  0.0096  -0.0363 665  ASN A CB    
5371 C  CG    . ASN A 663 ? 0.4658 0.5425 0.8383 0.026   0.0111  -0.0352 665  ASN A CG    
5372 O  OD1   . ASN A 663 ? 0.4853 0.5631 0.8557 0.0275  0.0127  -0.0353 665  ASN A OD1   
5373 N  ND2   . ASN A 663 ? 0.4762 0.5574 0.8519 0.026   0.0108  -0.0339 665  ASN A ND2   
5374 N  N     . ILE A 664 ? 0.3374 0.4006 0.7091 0.0225  0.008   -0.0407 666  ILE A N     
5375 C  CA    . ILE A 664 ? 0.325  0.382  0.6954 0.0212  0.0067  -0.0413 666  ILE A CA    
5376 C  C     . ILE A 664 ? 0.2998 0.3561 0.6697 0.022   0.0076  -0.043  666  ILE A C     
5377 O  O     . ILE A 664 ? 0.2955 0.3456 0.6616 0.0221  0.0076  -0.0424 666  ILE A O     
5378 C  CB    . ILE A 664 ? 0.3315 0.3903 0.706  0.0197  0.0053  -0.0418 666  ILE A CB    
5379 C  CG1   . ILE A 664 ? 0.3507 0.4101 0.726  0.0189  0.0044  -0.0396 666  ILE A CG1   
5380 C  CG2   . ILE A 664 ? 0.3414 0.3944 0.715  0.0184  0.0041  -0.0425 666  ILE A CG2   
5381 C  CD1   . ILE A 664 ? 0.3672 0.4321 0.7476 0.0183  0.0038  -0.04   666  ILE A CD1   
5382 N  N     . PHE A 665 ? 0.2768 0.3395 0.6505 0.0227  0.0084  -0.045  667  PHE A N     
5383 C  CA    . PHE A 665 ? 0.2652 0.3282 0.6397 0.0232  0.009   -0.0465 667  PHE A CA    
5384 C  C     . PHE A 665 ? 0.2651 0.3291 0.6373 0.0249  0.0107  -0.046  667  PHE A C     
5385 O  O     . PHE A 665 ? 0.2673 0.3361 0.64   0.026   0.0116  -0.0457 667  PHE A O     
5386 C  CB    . PHE A 665 ? 0.2521 0.3211 0.632  0.023   0.0087  -0.0491 667  PHE A CB    
5387 C  CG    . PHE A 665 ? 0.2538 0.3208 0.6353 0.0226  0.0084  -0.0504 667  PHE A CG    
5388 C  CD1   . PHE A 665 ? 0.266  0.3339 0.6476 0.0236  0.0095  -0.0508 667  PHE A CD1   
5389 C  CD2   . PHE A 665 ? 0.2596 0.3241 0.6428 0.0212  0.0072  -0.051  667  PHE A CD2   
5390 C  CE1   . PHE A 665 ? 0.2732 0.3393 0.6566 0.0233  0.0093  -0.0517 667  PHE A CE1   
5391 C  CE2   . PHE A 665 ? 0.2681 0.3307 0.6529 0.0209  0.0071  -0.052  667  PHE A CE2   
5392 C  CZ    . PHE A 665 ? 0.2688 0.3323 0.6538 0.0219  0.0081  -0.0523 667  PHE A CZ    
5393 N  N     . ASP A 666 ? 0.2591 0.319  0.6292 0.0254  0.0112  -0.0457 668  ASP A N     
5394 C  CA    . ASP A 666 ? 0.259  0.3197 0.6271 0.027   0.0129  -0.0449 668  ASP A CA    
5395 C  C     . ASP A 666 ? 0.2592 0.3266 0.6322 0.0275  0.0133  -0.0469 668  ASP A C     
5396 O  O     . ASP A 666 ? 0.2594 0.3261 0.6344 0.0273  0.0131  -0.0477 668  ASP A O     
5397 C  CB    . ASP A 666 ? 0.2795 0.3333 0.6437 0.0275  0.0132  -0.0437 668  ASP A CB    
5398 C  CG    . ASP A 666 ? 0.3378 0.3914 0.6992 0.0295  0.0151  -0.0423 668  ASP A CG    
5399 O  OD1   . ASP A 666 ? 0.3252 0.385  0.6889 0.0303  0.0161  -0.0427 668  ASP A OD1   
5400 O  OD2   . ASP A 666 ? 0.3937 0.4409 0.7502 0.0303  0.0155  -0.0407 668  ASP A OD2   
5401 N  N     . THR A 667 ? 0.2599 0.3338 0.6349 0.0281  0.0137  -0.0475 669  THR A N     
5402 C  CA    . THR A 667 ? 0.2687 0.3492 0.6482 0.0286  0.0138  -0.0496 669  THR A CA    
5403 C  C     . THR A 667 ? 0.2783 0.3595 0.6573 0.0298  0.0151  -0.0489 669  THR A C     
5404 O  O     . THR A 667 ? 0.2855 0.3715 0.6684 0.0301  0.0149  -0.0505 669  THR A O     
5405 C  CB    . THR A 667 ? 0.2868 0.3739 0.6681 0.0292  0.0137  -0.0505 669  THR A CB    
5406 O  OG1   . THR A 667 ? 0.2978 0.386  0.676  0.0306  0.0151  -0.0487 669  THR A OG1   
5407 C  CG2   . THR A 667 ? 0.2869 0.374  0.6692 0.0282  0.0126  -0.0509 669  THR A CG2   
5408 N  N     . GLY A 668 ? 0.2795 0.3559 0.6538 0.0306  0.0162  -0.0465 670  GLY A N     
5409 C  CA    . GLY A 668 ? 0.2853 0.3618 0.6586 0.032   0.0177  -0.0452 670  GLY A CA    
5410 C  C     . GLY A 668 ? 0.2897 0.3653 0.6659 0.0317  0.0174  -0.0457 670  GLY A C     
5411 O  O     . GLY A 668 ? 0.2927 0.3702 0.6699 0.0327  0.0184  -0.0449 670  GLY A O     
5412 N  N     . PHE A 669 ? 0.2901 0.3629 0.668  0.0303  0.0161  -0.0468 671  PHE A N     
5413 C  CA    . PHE A 669 ? 0.3014 0.3735 0.6826 0.0298  0.0157  -0.0474 671  PHE A CA    
5414 C  C     . PHE A 669 ? 0.3003 0.3791 0.6881 0.0292  0.0147  -0.0499 671  PHE A C     
5415 O  O     . PHE A 669 ? 0.2982 0.3772 0.6897 0.0288  0.0143  -0.0504 671  PHE A O     
5416 C  CB    . PHE A 669 ? 0.3089 0.3754 0.6891 0.0287  0.0147  -0.0475 671  PHE A CB    
5417 C  CG    . PHE A 669 ? 0.3206 0.3834 0.7012 0.0289  0.0151  -0.0465 671  PHE A CG    
5418 C  CD1   . PHE A 669 ? 0.335  0.392  0.7102 0.0303  0.0162  -0.044  671  PHE A CD1   
5419 C  CD2   . PHE A 669 ? 0.3285 0.3933 0.7147 0.028   0.0142  -0.048  671  PHE A CD2   
5420 C  CE1   . PHE A 669 ? 0.3454 0.3992 0.7208 0.0308  0.0167  -0.0428 671  PHE A CE1   
5421 C  CE2   . PHE A 669 ? 0.3375 0.3991 0.7244 0.0284  0.0147  -0.0468 671  PHE A CE2   
5422 C  CZ    . PHE A 669 ? 0.3372 0.3936 0.7187 0.0299  0.016   -0.0441 671  PHE A CZ    
5423 N  N     . PHE A 670 ? 0.2981 0.3823 0.6873 0.0293  0.0143  -0.0514 672  PHE A N     
5424 C  CA    . PHE A 670 ? 0.2982 0.3885 0.6927 0.0289  0.0132  -0.054  672  PHE A CA    
5425 C  C     . PHE A 670 ? 0.3145 0.4103 0.7094 0.0302  0.0139  -0.0539 672  PHE A C     
5426 O  O     . PHE A 670 ? 0.315  0.4108 0.706  0.0313  0.0151  -0.0522 672  PHE A O     
5427 C  CB    . PHE A 670 ? 0.2885 0.3805 0.684  0.0282  0.0119  -0.0562 672  PHE A CB    
5428 C  CG    . PHE A 670 ? 0.2849 0.3728 0.6812 0.0268  0.0109  -0.0567 672  PHE A CG    
5429 C  CD1   . PHE A 670 ? 0.2902 0.3727 0.6825 0.0264  0.0112  -0.0551 672  PHE A CD1   
5430 C  CD2   . PHE A 670 ? 0.2881 0.3772 0.6892 0.0259  0.0096  -0.0589 672  PHE A CD2   
5431 C  CE1   . PHE A 670 ? 0.2986 0.3774 0.6916 0.025   0.0102  -0.0555 672  PHE A CE1   
5432 C  CE2   . PHE A 670 ? 0.296  0.3813 0.6979 0.0246  0.0088  -0.0593 672  PHE A CE2   
5433 C  CZ    . PHE A 670 ? 0.2944 0.3748 0.6922 0.0242  0.0092  -0.0576 672  PHE A CZ    
5434 N  N     . HIS A 671 ? 0.3275 0.4281 0.7274 0.0301  0.0129  -0.0558 673  HIS A N     
5435 C  CA    . HIS A 671 ? 0.3532 0.4597 0.754  0.0312  0.0131  -0.0561 673  HIS A CA    
5436 C  C     . HIS A 671 ? 0.3858 0.4971 0.7911 0.0307  0.011   -0.0597 673  HIS A C     
5437 O  O     . HIS A 671 ? 0.3857 0.4969 0.7955 0.0297  0.0097  -0.0611 673  HIS A O     
5438 C  CB    . HIS A 671 ? 0.361  0.4682 0.7633 0.0317  0.0139  -0.0543 673  HIS A CB    
5439 C  CG    . HIS A 671 ? 0.3993 0.5129 0.8031 0.0327  0.0139  -0.0547 673  HIS A CG    
5440 N  ND1   . HIS A 671 ? 0.4256 0.5437 0.835  0.0322  0.0121  -0.0568 673  HIS A ND1   
5441 C  CD2   . HIS A 671 ? 0.4149 0.5311 0.8155 0.0341  0.0152  -0.0534 673  HIS A CD2   
5442 C  CE1   . HIS A 671 ? 0.4278 0.5511 0.837  0.0334  0.0124  -0.0567 673  HIS A CE1   
5443 N  NE2   . HIS A 671 ? 0.4255 0.5479 0.8295 0.0346  0.0144  -0.0546 673  HIS A NE2   
5444 N  N     . ILE A 672 ? 0.4134 0.5285 0.8177 0.0314  0.0108  -0.061  674  ILE A N     
5445 C  CA    . ILE A 672 ? 0.4526 0.5722 0.8605 0.0314  0.0088  -0.0645 674  ILE A CA    
5446 C  C     . ILE A 672 ? 0.4911 0.6166 0.9007 0.0325  0.0084  -0.0653 674  ILE A C     
5447 O  O     . ILE A 672 ? 0.4979 0.6265 0.9048 0.0339  0.0096  -0.0643 674  ILE A O     
5448 C  CB    . ILE A 672 ? 0.4665 0.5867 0.873  0.0316  0.0084  -0.0658 674  ILE A CB    
5449 C  CG1   . ILE A 672 ? 0.4871 0.6091 0.8894 0.033   0.01    -0.064  674  ILE A CG1   
5450 C  CG2   . ILE A 672 ? 0.476  0.5903 0.8821 0.0302  0.0083  -0.0653 674  ILE A CG2   
5451 C  CD1   . ILE A 672 ? 0.5062 0.6292 0.9074 0.0334  0.0097  -0.0648 674  ILE A CD1   
5452 N  N     . GLU A 673 ? 0.5123 0.6391 0.9266 0.0318  0.0069  -0.0667 675  GLU A N     
5453 C  CA    . GLU A 673 ? 0.5353 0.6675 0.9521 0.0325  0.0061  -0.0676 675  GLU A CA    
5454 C  C     . GLU A 673 ? 0.5489 0.6864 0.9651 0.0338  0.005   -0.0704 675  GLU A C     
5455 O  O     . GLU A 673 ? 0.5514 0.6933 0.9663 0.0352  0.0056  -0.0699 675  GLU A O     
5456 C  CB    . GLU A 673 ? 0.575  0.7071 0.9977 0.0311  0.0041  -0.069  675  GLU A CB    
5457 C  CG    . GLU A 673 ? 0.6634 0.801  1.0895 0.0316  0.0026  -0.0703 675  GLU A CG    
5458 C  CD    . GLU A 673 ? 0.7889 0.9264 1.2212 0.0301  0.0001  -0.072  675  GLU A CD    
5459 O  OE1   . GLU A 673 ? 0.8265 0.9596 1.2607 0.0288  0.0004  -0.0708 675  GLU A OE1   
5460 O  OE2   . GLU A 673 ? 0.8208 0.9626 1.2563 0.0303  -0.0022 -0.0747 675  GLU A OE2   
5461 N  N     . GLY A 674 ? 0.5527 0.6898 0.9696 0.0336  0.0037  -0.073  676  GLY A N     
5462 C  CA    . GLY A 674 ? 0.557  0.6987 0.9732 0.0351  0.0027  -0.0757 676  GLY A CA    
5463 C  C     . GLY A 674 ? 0.5581 0.6986 0.9764 0.0346  0.0008  -0.0788 676  GLY A C     
5464 O  O     . GLY A 674 ? 0.5558 0.6991 0.9768 0.0349  -0.0014 -0.0821 676  GLY A O     
5465 O  "O5'" . DG  B 1   ? 0.3354 0.3966 0.9221 0.0015  -0.0081 -0.0727 1    DG  E "O5'" 
5466 C  "C5'" . DG  B 1   ? 0.3267 0.3896 0.9198 0.001   -0.0093 -0.0709 1    DG  E "C5'" 
5467 C  "C4'" . DG  B 1   ? 0.3226 0.387  0.9139 0.0019  -0.0066 -0.0656 1    DG  E "C4'" 
5468 O  "O4'" . DG  B 1   ? 0.3152 0.3816 0.9051 0.0018  -0.0078 -0.0656 1    DG  E "O4'" 
5469 C  "C3'" . DG  B 1   ? 0.3285 0.3921 0.9104 0.0032  -0.0038 -0.0642 1    DG  E "C3'" 
5470 O  "O3'" . DG  B 1   ? 0.3388 0.4015 0.9234 0.0037  -0.0015 -0.061  1    DG  E "O3'" 
5471 C  "C2'" . DG  B 1   ? 0.3209 0.386  0.8985 0.004   -0.0028 -0.0614 1    DG  E "C2'" 
5472 C  "C1'" . DG  B 1   ? 0.3081 0.3749 0.8895 0.0031  -0.0056 -0.0634 1    DG  E "C1'" 
5473 N  N9    . DG  B 1   ? 0.2841 0.3511 0.8578 0.0031  -0.007  -0.0672 1    DG  E N9    
5474 C  C8    . DG  B 1   ? 0.2728 0.3399 0.8472 0.0023  -0.0099 -0.0721 1    DG  E C8    
5475 N  N7    . DG  B 1   ? 0.2631 0.3308 0.83   0.0027  -0.0105 -0.0743 1    DG  E N7    
5476 C  C5    . DG  B 1   ? 0.2594 0.3274 0.8205 0.0037  -0.0079 -0.0708 1    DG  E C5    
5477 C  C6    . DG  B 1   ? 0.2613 0.33   0.8137 0.0045  -0.0072 -0.071  1    DG  E C6    
5478 O  O6    . DG  B 1   ? 0.2643 0.3338 0.8124 0.0045  -0.0087 -0.0743 1    DG  E O6    
5479 N  N1    . DG  B 1   ? 0.2609 0.3291 0.8094 0.0055  -0.0045 -0.0668 1    DG  E N1    
5480 C  C2    . DG  B 1   ? 0.2594 0.327  0.812  0.0059  -0.0026 -0.0629 1    DG  E C2    
5481 N  N2    . DG  B 1   ? 0.2622 0.3292 0.8094 0.0073  -0.0001 -0.0593 1    DG  E N2    
5482 N  N3    . DG  B 1   ? 0.2549 0.3223 0.816  0.0053  -0.003  -0.0624 1    DG  E N3    
5483 C  C4    . DG  B 1   ? 0.2626 0.3302 0.8277 0.0041  -0.0057 -0.0665 1    DG  E C4    
5484 P  P     . DT  B 2   ? 0.3471 0.4081 0.9238 0.0046  0.0006  -0.0609 2    DT  E P     
5485 O  OP1   . DT  B 2   ? 0.3526 0.4131 0.9342 0.005   0.0027  -0.0575 2    DT  E OP1   
5486 O  OP2   . DT  B 2   ? 0.3527 0.4127 0.925  0.004   -0.001  -0.0658 2    DT  E OP2   
5487 O  "O5'" . DT  B 2   ? 0.3289 0.3903 0.8969 0.0057  0.0022  -0.0586 2    DT  E "O5'" 
5488 C  "C5'" . DT  B 2   ? 0.3057 0.3679 0.875  0.0069  0.0042  -0.0537 2    DT  E "C5'" 
5489 C  "C4'" . DT  B 2   ? 0.2864 0.3479 0.8456 0.0081  0.0056  -0.0524 2    DT  E "C4'" 
5490 O  "O4'" . DT  B 2   ? 0.2705 0.3329 0.8255 0.0077  0.004   -0.055  2    DT  E "O4'" 
5491 C  "C3'" . DT  B 2   ? 0.2827 0.3422 0.8345 0.0085  0.0066  -0.0533 2    DT  E "C3'" 
5492 O  "O3'" . DT  B 2   ? 0.2902 0.3487 0.8359 0.01    0.0086  -0.05   2    DT  E "O3'" 
5493 C  "C2'" . DT  B 2   ? 0.271  0.3304 0.8173 0.0076  0.0048  -0.0577 2    DT  E "C2'" 
5494 C  "C1'" . DT  B 2   ? 0.2611 0.3222 0.8074 0.0077  0.0038  -0.0576 2    DT  E "C1'" 
5495 N  N1    . DT  B 2   ? 0.2399 0.3019 0.7855 0.0067  0.0014  -0.062  2    DT  E N1    
5496 C  C2    . DT  B 2   ? 0.2258 0.2881 0.7639 0.007   0.001   -0.0633 2    DT  E C2    
5497 O  O2    . DT  B 2   ? 0.2253 0.287  0.7574 0.008   0.0025  -0.0609 2    DT  E O2    
5498 N  N3    . DT  B 2   ? 0.2187 0.2819 0.7563 0.0063  -0.0012 -0.0674 2    DT  E N3    
5499 C  C4    . DT  B 2   ? 0.2223 0.2859 0.7658 0.0053  -0.0032 -0.0706 2    DT  E C4    
5500 O  O4    . DT  B 2   ? 0.2248 0.2892 0.7666 0.0051  -0.0052 -0.0742 2    DT  E O4    
5501 C  C5    . DT  B 2   ? 0.2226 0.2854 0.7737 0.0049  -0.0028 -0.0692 2    DT  E C5    
5502 C  C7    . DT  B 2   ? 0.2165 0.2791 0.7743 0.004   -0.005  -0.0725 2    DT  E C7    
5503 C  C6    . DT  B 2   ? 0.2298 0.292  0.7817 0.0056  -0.0005 -0.065  2    DT  E C6    
5504 P  P     . DC  B 3   ? 0.2985 0.3548 0.8378 0.0106  0.0101  -0.0492 3    DC  E P     
5505 O  OP1   . DC  B 3   ? 0.3091 0.3648 0.8482 0.0124  0.0123  -0.0445 3    DC  E OP1   
5506 O  OP2   . DC  B 3   ? 0.3014 0.3573 0.8437 0.0094  0.0094  -0.0517 3    DC  E OP2   
5507 O  "O5'" . DC  B 3   ? 0.2736 0.3289 0.8027 0.0107  0.0095  -0.0509 3    DC  E "O5'" 
5508 C  "C5'" . DC  B 3   ? 0.2453 0.3007 0.7703 0.0116  0.0098  -0.0494 3    DC  E "C5'" 
5509 C  "C4'" . DC  B 3   ? 0.2238 0.2785 0.7404 0.0113  0.0089  -0.0518 3    DC  E "C4'" 
5510 O  "O4'" . DC  B 3   ? 0.2082 0.2646 0.7271 0.01    0.0069  -0.0556 3    DC  E "O4'" 
5511 C  "C3'" . DC  B 3   ? 0.2139 0.2665 0.7247 0.011   0.0091  -0.0527 3    DC  E "C3'" 
5512 O  "O3'" . DC  B 3   ? 0.2065 0.2574 0.7087 0.0117  0.0094  -0.0518 3    DC  E "O3'" 
5513 C  "C2'" . DC  B 3   ? 0.2049 0.2586 0.7171 0.0095  0.0073  -0.0568 3    DC  E "C2'" 
5514 C  "C1'" . DC  B 3   ? 0.1922 0.2478 0.7061 0.0093  0.0061  -0.0584 3    DC  E "C1'" 
5515 N  N1    . DC  B 3   ? 0.165  0.2223 0.6836 0.0081  0.0043  -0.0621 3    DC  E N1    
5516 C  C2    . DC  B 3   ? 0.1548 0.2132 0.6702 0.0078  0.0028  -0.0649 3    DC  E C2    
5517 O  O2    . DC  B 3   ? 0.151  0.2092 0.66   0.0083  0.0032  -0.0642 3    DC  E O2    
5518 N  N3    . DC  B 3   ? 0.1528 0.2126 0.6721 0.0071  0.001   -0.0684 3    DC  E N3    
5519 C  C4    . DC  B 3   ? 0.1544 0.214  0.6805 0.0065  0.0007  -0.0691 3    DC  E C4    
5520 N  N4    . DC  B 3   ? 0.1507 0.2111 0.6799 0.006   -0.0013 -0.0728 3    DC  E N4    
5521 C  C5    . DC  B 3   ? 0.1563 0.2148 0.6862 0.0067  0.0022  -0.0661 3    DC  E C5    
5522 C  C6    . DC  B 3   ? 0.1588 0.2162 0.6846 0.0076  0.0041  -0.0626 3    DC  E C6    
5523 P  P     . DT  B 4   ? 0.197  0.2454 0.6925 0.0119  0.0098  -0.0512 4    DT  E P     
5524 O  OP1   . DT  B 4   ? 0.2129 0.259  0.702  0.0135  0.0108  -0.0484 4    DT  E OP1   
5525 O  OP2   . DT  B 4   ? 0.1945 0.2427 0.6944 0.0114  0.0103  -0.051  4    DT  E OP2   
5526 O  "O5'" . DT  B 4   ? 0.1844 0.2332 0.6755 0.0107  0.0082  -0.0546 4    DT  E "O5'" 
5527 C  "C5'" . DT  B 4   ? 0.1816 0.2306 0.6677 0.011   0.0077  -0.0551 4    DT  E "C5'" 
5528 C  "C4'" . DT  B 4   ? 0.1763 0.2265 0.6602 0.0099  0.0063  -0.0583 4    DT  E "C4'" 
5529 O  "O4'" . DT  B 4   ? 0.1675 0.2202 0.6581 0.0091  0.0054  -0.0609 4    DT  E "O4'" 
5530 C  "C3'" . DT  B 4   ? 0.1814 0.2304 0.6614 0.0092  0.006   -0.0588 4    DT  E "C3'" 
5531 O  "O3'" . DT  B 4   ? 0.1997 0.2487 0.6738 0.009   0.0052  -0.06   4    DT  E "O3'" 
5532 C  "C2'" . DT  B 4   ? 0.166  0.2167 0.6518 0.0084  0.0055  -0.061  4    DT  E "C2'" 
5533 C  "C1'" . DT  B 4   ? 0.1528 0.2059 0.6425 0.0083  0.0046  -0.0631 4    DT  E "C1'" 
5534 N  N1    . DT  B 4   ? 0.1344 0.1889 0.6313 0.0078  0.004   -0.0651 4    DT  E N1    
5535 C  C2    . DT  B 4   ? 0.1293 0.1858 0.6275 0.0075  0.0025  -0.0684 4    DT  E C2    
5536 O  O2    . DT  B 4   ? 0.1328 0.1902 0.6267 0.0076  0.0019  -0.0696 4    DT  E O2    
5537 N  N3    . DT  B 4   ? 0.119  0.1764 0.624  0.0071  0.0018  -0.0703 4    DT  E N3    
5538 C  C4    . DT  B 4   ? 0.1147 0.1713 0.6253 0.0069  0.0026  -0.0691 4    DT  E C4    
5539 O  O4    . DT  B 4   ? 0.1171 0.1743 0.6335 0.0065  0.0017  -0.0711 4    DT  E O4    
5540 C  C5    . DT  B 4   ? 0.1135 0.1684 0.6226 0.0073  0.0043  -0.0654 4    DT  E C5    
5541 C  C7    . DT  B 4   ? 0.1042 0.1584 0.6192 0.0073  0.0053  -0.0636 4    DT  E C7    
5542 C  C6    . DT  B 4   ? 0.1249 0.1788 0.6271 0.0077  0.0048  -0.0637 4    DT  E C6    
5543 P  P     . DG  B 5   ? 0.2064 0.2531 0.6734 0.0088  0.005   -0.0588 5    DG  E P     
5544 O  OP1   . DG  B 5   ? 0.2188 0.263  0.6805 0.0098  0.0055  -0.0567 5    DG  E OP1   
5545 O  OP2   . DG  B 5   ? 0.2113 0.2571 0.6801 0.0083  0.0053  -0.0582 5    DG  E OP2   
5546 O  "O5'" . DG  B 5   ? 0.2083 0.2571 0.6733 0.0082  0.0039  -0.0613 5    DG  E "O5'" 
5547 C  "C5'" . DG  B 5   ? 0.2189 0.2695 0.6835 0.0085  0.0034  -0.0627 5    DG  E "C5'" 
5548 C  "C4'" . DG  B 5   ? 0.2316 0.2852 0.6978 0.0081  0.0024  -0.0657 5    DG  E "C4'" 
5549 O  "O4'" . DG  B 5   ? 0.2183 0.2735 0.6913 0.0079  0.0022  -0.0674 5    DG  E "O4'" 
5550 C  "C3'" . DG  B 5   ? 0.2498 0.3034 0.7131 0.0076  0.002   -0.0659 5    DG  E "C3'" 
5551 O  "O3'" . DG  B 5   ? 0.2803 0.3358 0.7403 0.0077  0.0013  -0.0672 5    DG  E "O3'" 
5552 C  "C2'" . DG  B 5   ? 0.2315 0.2864 0.7001 0.0072  0.0019  -0.0675 5    DG  E "C2'" 
5553 C  "C1'" . DG  B 5   ? 0.2114 0.2679 0.6852 0.0076  0.0017  -0.0693 5    DG  E "C1'" 
5554 N  N9    . DG  B 5   ? 0.1851 0.2417 0.6652 0.0073  0.0018  -0.0699 5    DG  E N9    
5555 C  C8    . DG  B 5   ? 0.1783 0.233  0.6606 0.0071  0.0028  -0.0679 5    DG  E C8    
5556 N  N7    . DG  B 5   ? 0.1653 0.2206 0.6536 0.007   0.0027  -0.069  5    DG  E N7    
5557 C  C5    . DG  B 5   ? 0.161  0.2184 0.6508 0.0071  0.0016  -0.0721 5    DG  E C5    
5558 C  C6    . DG  B 5   ? 0.1493 0.2078 0.6447 0.0071  0.0008  -0.0747 5    DG  E C6    
5559 O  O6    . DG  B 5   ? 0.1426 0.2004 0.6431 0.0068  0.0012  -0.0745 5    DG  E O6    
5560 N  N1    . DG  B 5   ? 0.1445 0.2049 0.6391 0.0075  -0.0005 -0.0777 5    DG  E N1    
5561 C  C2    . DG  B 5   ? 0.1491 0.2106 0.6383 0.0079  -0.0009 -0.078  5    DG  E C2    
5562 N  N2    . DG  B 5   ? 0.1389 0.2026 0.6282 0.0085  -0.0022 -0.0811 5    DG  E N2    
5563 N  N3    . DG  B 5   ? 0.1612 0.2218 0.6455 0.0078  -0.0001 -0.0755 5    DG  E N3    
5564 C  C4    . DG  B 5   ? 0.1685 0.2269 0.6533 0.0074  0.001   -0.0727 5    DG  E C4    
5565 P  P     . DC  B 6   ? 0.3202 0.3762 0.7766 0.0074  0.0009  -0.067  6    DC  E P     
5566 O  OP1   . DC  B 6   ? 0.3338 0.3908 0.7859 0.0078  0.0005  -0.0671 6    DC  E OP1   
5567 O  OP2   . DC  B 6   ? 0.3209 0.3742 0.776  0.0067  0.0011  -0.0647 6    DC  E OP2   
5568 O  "O5'" . DC  B 6   ? 0.311  0.37   0.7716 0.0076  0.0005  -0.0696 6    DC  E "O5'" 
5569 C  "C5'" . DC  B 6   ? 0.3091 0.3709 0.7715 0.0083  -0.0001 -0.0723 6    DC  E "C5'" 
5570 C  "C4'" . DC  B 6   ? 0.3101 0.3737 0.7764 0.0086  -0.0004 -0.0746 6    DC  E "C4'" 
5571 O  "O4'" . DC  B 6   ? 0.3005 0.3627 0.7719 0.0082  -0.0001 -0.0747 6    DC  E "O4'" 
5572 C  "C3'" . DC  B 6   ? 0.3225 0.3865 0.7872 0.0085  -0.0002 -0.0737 6    DC  E "C3'" 
5573 O  "O3'" . DC  B 6   ? 0.3406 0.4075 0.8035 0.0095  -0.0007 -0.0752 6    DC  E "O3'" 
5574 C  "C2'" . DC  B 6   ? 0.3097 0.373  0.7791 0.0083  0.0001  -0.0743 6    DC  E "C2'" 
5575 C  "C1'" . DC  B 6   ? 0.2946 0.3574 0.7684 0.0083  -0.0001 -0.0757 6    DC  E "C1'" 
5576 N  N1    . DC  B 6   ? 0.2753 0.3361 0.7531 0.0077  0.0005  -0.0745 6    DC  E N1    
5577 C  C2    . DC  B 6   ? 0.2648 0.326  0.7479 0.0079  0.0003  -0.0765 6    DC  E C2    
5578 O  O2    . DC  B 6   ? 0.2678 0.3308 0.752  0.0086  -0.0006 -0.0794 6    DC  E O2    
5579 N  N3    . DC  B 6   ? 0.256  0.3157 0.7429 0.0074  0.0011  -0.0752 6    DC  E N3    
5580 C  C4    . DC  B 6   ? 0.2555 0.3132 0.7406 0.0068  0.002   -0.0721 6    DC  E C4    
5581 N  N4    . DC  B 6   ? 0.2506 0.307  0.7396 0.0065  0.0028  -0.0708 6    DC  E N4    
5582 C  C5    . DC  B 6   ? 0.2637 0.3207 0.743  0.0066  0.002   -0.0702 6    DC  E C5    
5583 C  C6    . DC  B 6   ? 0.2712 0.3298 0.7471 0.007   0.0013  -0.0715 6    DC  E C6    
5584 P  P     . DA  B 7   ? 0.3492 0.4171 0.8095 0.0096  -0.0005 -0.0737 7    DA  E P     
5585 O  OP1   . DA  B 7   ? 0.3568 0.4275 0.8138 0.0106  -0.0008 -0.0743 7    DA  E OP1   
5586 O  OP2   . DA  B 7   ? 0.3459 0.4111 0.8048 0.0083  -0.0001 -0.0705 7    DA  E OP2   
5587 O  "O5'" . DA  B 7   ? 0.3483 0.4174 0.8126 0.0103  -0.0004 -0.0754 7    DA  E "O5'" 
5588 C  "C5'" . DA  B 7   ? 0.3497 0.4199 0.817  0.0113  -0.0009 -0.0788 7    DA  E "C5'" 
5589 C  "C4'" . DA  B 7   ? 0.3481 0.4179 0.8193 0.0115  -0.0007 -0.0798 7    DA  E "C4'" 
5590 O  "O4'" . DA  B 7   ? 0.3442 0.4113 0.8191 0.0103  -0.0003 -0.079  7    DA  E "O4'" 
5591 C  "C3'" . DA  B 7   ? 0.3522 0.4228 0.8222 0.0117  0       -0.0779 7    DA  E "C3'" 
5592 O  "O3'" . DA  B 7   ? 0.3672 0.4392 0.8392 0.0132  -0.0001 -0.0802 7    DA  E "O3'" 
5593 C  "C2'" . DA  B 7   ? 0.3433 0.411  0.8153 0.0101  0.0007  -0.0755 7    DA  E "C2'" 
5594 C  "C1'" . DA  B 7   ? 0.3317 0.3981 0.808  0.01    0.0004  -0.0777 7    DA  E "C1'" 
5595 N  N9    . DA  B 7   ? 0.3078 0.3716 0.7866 0.0087  0.001   -0.0757 7    DA  E N9    
5596 C  C8    . DA  B 7   ? 0.3024 0.3645 0.7786 0.0077  0.0014  -0.0728 7    DA  E C8    
5597 N  N7    . DA  B 7   ? 0.2931 0.3531 0.772  0.007   0.0021  -0.0713 7    DA  E N7    
5598 C  C5    . DA  B 7   ? 0.2827 0.3433 0.7666 0.0074  0.0022  -0.0733 7    DA  E C5    
5599 C  C6    . DA  B 7   ? 0.2647 0.324  0.7535 0.0071  0.0028  -0.0729 7    DA  E C6    
5600 N  N6    . DA  B 7   ? 0.2587 0.316  0.7481 0.0064  0.0036  -0.0702 7    DA  E N6    
5601 N  N1    . DA  B 7   ? 0.2555 0.3154 0.7486 0.0078  0.0026  -0.0754 7    DA  E N1    
5602 C  C2    . DA  B 7   ? 0.2627 0.3244 0.7548 0.0088  0.0017  -0.0781 7    DA  E C2    
5603 N  N3    . DA  B 7   ? 0.2784 0.3417 0.7659 0.0094  0.0011  -0.0787 7    DA  E N3    
5604 C  C4    . DA  B 7   ? 0.291  0.3537 0.7747 0.0085  0.0014  -0.0761 7    DA  E C4    
5605 P  P     . DT  B 8   ? 0.3753 0.4503 0.8446 0.0149  0.0002  -0.08   8    DT  E P     
5606 O  OP1   . DT  B 8   ? 0.3809 0.4582 0.8473 0.0162  -0.0005 -0.0817 8    DT  E OP1   
5607 O  OP2   . DT  B 8   ? 0.3775 0.4525 0.8454 0.0139  0.001   -0.0761 8    DT  E OP2   
5608 O  "O5'" . DT  B 8   ? 0.3672 0.4423 0.8399 0.0163  0.0003  -0.0825 8    DT  E "O5'" 
5609 C  "C5'" . DT  B 8   ? 0.3575 0.4315 0.8331 0.0168  -0.0007 -0.0861 8    DT  E "C5'" 
5610 C  "C4'" . DT  B 8   ? 0.3483 0.4205 0.8284 0.0167  -0.0004 -0.0871 8    DT  E "C4'" 
5611 O  "O4'" . DT  B 8   ? 0.3406 0.4103 0.8235 0.0145  0.0001  -0.0848 8    DT  E "O4'" 
5612 C  "C3'" . DT  B 8   ? 0.3417 0.4149 0.8214 0.0179  0.0006  -0.0861 8    DT  E "C3'" 
5613 O  "O3'" . DT  B 8   ? 0.3442 0.4167 0.8265 0.0194  0.0002  -0.0892 8    DT  E "O3'" 
5614 C  "C2'" . DT  B 8   ? 0.3308 0.4024 0.8122 0.016   0.0017  -0.0826 8    DT  E "C2'" 
5615 C  "C1'" . DT  B 8   ? 0.3242 0.3932 0.8089 0.0144  0.0012  -0.0833 8    DT  E "C1'" 
5616 N  N1    . DT  B 8   ? 0.3032 0.3707 0.7884 0.0124  0.002   -0.0798 8    DT  E N1    
5617 C  C2    . DT  B 8   ? 0.2934 0.3588 0.7829 0.0115  0.0025  -0.0793 8    DT  E C2    
5618 O  O2    . DT  B 8   ? 0.2902 0.3548 0.7836 0.012   0.0023  -0.0816 8    DT  E O2    
5619 N  N3    . DT  B 8   ? 0.292  0.3561 0.7811 0.01    0.0033  -0.076  8    DT  E N3    
5620 C  C4    . DT  B 8   ? 0.2905 0.3548 0.7752 0.0092  0.0033  -0.0733 8    DT  E C4    
5621 O  O4    . DT  B 8   ? 0.2887 0.3514 0.7732 0.008   0.0038  -0.0706 8    DT  E O4    
5622 C  C5    . DT  B 8   ? 0.2955 0.362  0.7761 0.01    0.0027  -0.0739 8    DT  E C5    
5623 C  C7    . DT  B 8   ? 0.3013 0.3681 0.7773 0.0093  0.0026  -0.0711 8    DT  E C7    
5624 C  C6    . DT  B 8   ? 0.3006 0.3686 0.7816 0.0117  0.0022  -0.077  8    DT  E C6    
5625 P  P     . DT  B 9   ? 0.3542 0.4281 0.8356 0.0217  0.001   -0.0893 9    DT  E P     
5626 O  OP1   . DT  B 9   ? 0.3643 0.4394 0.8438 0.0244  -0.0001 -0.0931 9    DT  E OP1   
5627 O  OP2   . DT  B 9   ? 0.3585 0.4342 0.8374 0.0213  0.0023  -0.0851 9    DT  E OP2   
5628 O  "O5'" . DT  B 9   ? 0.337  0.4082 0.8234 0.0211  0.0014  -0.0898 9    DT  E "O5'" 
5629 C  "C5'" . DT  B 9   ? 0.3124 0.3811 0.8027 0.0206  0.0002  -0.0929 9    DT  E "C5'" 
5630 C  "C4'" . DT  B 9   ? 0.287  0.3534 0.7824 0.0192  0.001   -0.0917 9    DT  E "C4'" 
5631 O  "O4'" . DT  B 9   ? 0.2706 0.3366 0.7663 0.0169  0.002   -0.0879 9    DT  E "O4'" 
5632 C  "C3'" . DT  B 9   ? 0.2783 0.3446 0.7746 0.0206  0.0022  -0.0912 9    DT  E "C3'" 
5633 O  "O3'" . DT  B 9   ? 0.2815 0.345  0.7831 0.0202  0.0019  -0.093  9    DT  E "O3'" 
5634 C  "C2'" . DT  B 9   ? 0.2633 0.3305 0.7587 0.0191  0.0039  -0.0865 9    DT  E "C2'" 
5635 C  "C1'" . DT  B 9   ? 0.2466 0.3123 0.7439 0.0166  0.0035  -0.0854 9    DT  E "C1'" 
5636 N  N1    . DT  B 9   ? 0.2155 0.2819 0.7104 0.015   0.0043  -0.0813 9    DT  E N1    
5637 C  C2    . DT  B 9   ? 0.2029 0.2675 0.7005 0.0132  0.005   -0.079  9    DT  E C2    
5638 O  O2    . DT  B 9   ? 0.2035 0.2664 0.7058 0.0128  0.0052  -0.0797 9    DT  E O2    
5639 N  N3    . DT  B 9   ? 0.1894 0.2545 0.6841 0.0119  0.0055  -0.0755 9    DT  E N3    
5640 C  C4    . DT  B 9   ? 0.1917 0.2587 0.6816 0.0121  0.0052  -0.0742 9    DT  E C4    
5641 O  O4    . DT  B 9   ? 0.1915 0.2582 0.6793 0.0107  0.0054  -0.0712 9    DT  E O4    
5642 C  C5    . DT  B 9   ? 0.1947 0.2638 0.6824 0.014   0.0047  -0.0766 9    DT  E C5    
5643 C  C7    . DT  B 9   ? 0.1935 0.265  0.6763 0.0145  0.0045  -0.0751 9    DT  E C7    
5644 C  C6    . DT  B 9   ? 0.2035 0.2722 0.6935 0.0155  0.0043  -0.0801 9    DT  E C6    
5645 P  P     . DC  B 10  ? 0.2764 0.339  0.7804 0.0214  0.0031  -0.0929 10   DC  E P     
5646 O  OP1   . DC  B 10  ? 0.2836 0.3435 0.7915 0.0221  0.0017  -0.0968 10   DC  E OP1   
5647 O  OP2   . DC  B 10  ? 0.2772 0.3422 0.7767 0.0234  0.0042  -0.0916 10   DC  E OP2   
5648 O  "O5'" . DC  B 10  ? 0.2476 0.3094 0.755  0.019   0.0046  -0.0889 10   DC  E "O5'" 
5649 C  "C5'" . DC  B 10  ? 0.217  0.2767 0.7288 0.017   0.0041  -0.089  10   DC  E "C5'" 
5650 C  "C4'" . DC  B 10  ? 0.195  0.2541 0.7098 0.0155  0.0058  -0.0853 10   DC  E "C4'" 
5651 O  "O4'" . DC  B 10  ? 0.1834 0.2442 0.6942 0.0145  0.0066  -0.0817 10   DC  E "O4'" 
5652 C  "C3'" . DC  B 10  ? 0.1809 0.2397 0.6978 0.0166  0.0071  -0.0848 10   DC  E "C3'" 
5653 O  "O3'" . DC  B 10  ? 0.1755 0.2325 0.6979 0.0152  0.0079  -0.0834 10   DC  E "O3'" 
5654 C  "C2'" . DC  B 10  ? 0.1721 0.2333 0.6845 0.0168  0.0085  -0.0814 10   DC  E "C2'" 
5655 C  "C1'" . DC  B 10  ? 0.1668 0.2284 0.6775 0.0147  0.0082  -0.079  10   DC  E "C1'" 
5656 N  N1    . DC  B 10  ? 0.1469 0.2109 0.6522 0.0147  0.0085  -0.0766 10   DC  E N1    
5657 C  C2    . DC  B 10  ? 0.1296 0.1939 0.6341 0.0131  0.0093  -0.0727 10   DC  E C2    
5658 O  O2    . DC  B 10  ? 0.1153 0.1782 0.6232 0.012   0.01    -0.0711 10   DC  E O2    
5659 N  N3    . DC  B 10  ? 0.1318 0.1979 0.6316 0.0128  0.0091  -0.0706 10   DC  E N3    
5660 C  C4    . DC  B 10  ? 0.1359 0.2037 0.6322 0.0141  0.0084  -0.0721 10   DC  E C4    
5661 N  N4    . DC  B 10  ? 0.1383 0.2079 0.6305 0.0138  0.0082  -0.0698 10   DC  E N4    
5662 C  C5    . DC  B 10  ? 0.1378 0.2055 0.6347 0.016   0.0077  -0.0761 10   DC  E C5    
5663 C  C6    . DC  B 10  ? 0.145  0.2107 0.6464 0.0161  0.0076  -0.0784 10   DC  E C6    
5664 P  P     . DC  B 11  ? 0.1656 0.2215 0.6921 0.016   0.0092  -0.0832 11   DC  E P     
5665 O  OP1   . DC  B 11  ? 0.1723 0.226  0.7054 0.0149  0.0089  -0.0839 11   DC  E OP1   
5666 O  OP2   . DC  B 11  ? 0.1675 0.2238 0.6916 0.0185  0.009   -0.0857 11   DC  E OP2   
5667 O  "O5'" . DC  B 11  ? 0.1334 0.1909 0.6587 0.0151  0.0112  -0.0785 11   DC  E "O5'" 
5668 C  "C5'" . DC  B 11  ? 0.1328 0.1901 0.6595 0.0132  0.0116  -0.0757 11   DC  E "C5'" 
5669 C  "C4'" . DC  B 11  ? 0.1426 0.2014 0.6673 0.0126  0.0132  -0.0716 11   DC  E "C4'" 
5670 O  "O4'" . DC  B 11  ? 0.1374 0.1981 0.6561 0.0127  0.0127  -0.0706 11   DC  E "O4'" 
5671 C  "C3'" . DC  B 11  ? 0.1566 0.2158 0.6833 0.0136  0.0147  -0.0706 11   DC  E "C3'" 
5672 O  "O3'" . DC  B 11  ? 0.1703 0.2293 0.6997 0.0124  0.0161  -0.0672 11   DC  E "O3'" 
5673 C  "C2'" . DC  B 11  ? 0.1466 0.2082 0.6678 0.0147  0.0149  -0.0695 11   DC  E "C2'" 
5674 C  "C1'" . DC  B 11  ? 0.1417 0.2041 0.6588 0.0133  0.0139  -0.0682 11   DC  E "C1'" 
5675 N  N1    . DC  B 11  ? 0.1376 0.2022 0.6494 0.0142  0.0133  -0.0685 11   DC  E N1    
5676 C  C2    . DC  B 11  ? 0.1353 0.2015 0.6433 0.0132  0.0132  -0.0653 11   DC  E C2    
5677 O  O2    . DC  B 11  ? 0.1319 0.1977 0.6408 0.0116  0.0137  -0.0623 11   DC  E O2    
5678 N  N3    . DC  B 11  ? 0.1381 0.2063 0.6417 0.014   0.0126  -0.0654 11   DC  E N3    
5679 C  C4    . DC  B 11  ? 0.1378 0.2065 0.6403 0.016   0.0121  -0.0686 11   DC  E C4    
5680 N  N4    . DC  B 11  ? 0.1394 0.2105 0.6376 0.0169  0.0116  -0.0684 11   DC  E N4    
5681 C  C5    . DC  B 11  ? 0.1359 0.2027 0.6417 0.0172  0.0119  -0.0722 11   DC  E C5    
5682 C  C6    . DC  B 11  ? 0.1369 0.2016 0.6474 0.0161  0.0125  -0.072  11   DC  E C6    
5683 P  P     . DT  B 12  ? 0.1725 0.2318 0.7054 0.0129  0.018   -0.0653 12   DT  E P     
5684 O  OP1   . DT  B 12  ? 0.1711 0.2284 0.7101 0.0123  0.0185  -0.0654 12   DT  E OP1   
5685 O  OP2   . DT  B 12  ? 0.172  0.232  0.7035 0.015   0.0183  -0.067  12   DT  E OP2   
5686 O  "O5'" . DT  B 12  ? 0.1899 0.251  0.7199 0.0118  0.0188  -0.0608 12   DT  E "O5'" 
5687 C  "C5'" . DT  B 12  ? 0.2059 0.2667 0.7338 0.0102  0.0181  -0.0592 12   DT  E "C5'" 
5688 C  "C4'" . DT  B 12  ? 0.2245 0.2869 0.7486 0.0093  0.0184  -0.0554 12   DT  E "C4'" 
5689 O  "O4'" . DT  B 12  ? 0.2195 0.2834 0.7385 0.0096  0.0173  -0.0559 12   DT  E "O4'" 
5690 C  "C3'" . DT  B 12  ? 0.2524 0.3162 0.7784 0.0097  0.02    -0.0529 12   DT  E "C3'" 
5691 O  "O3'" . DT  B 12  ? 0.3005 0.3645 0.8255 0.0083  0.0203  -0.0492 12   DT  E "O3'" 
5692 C  "C2'" . DT  B 12  ? 0.2314 0.2974 0.7539 0.0108  0.0199  -0.0529 12   DT  E "C2'" 
5693 C  "C1'" . DT  B 12  ? 0.2153 0.2814 0.733  0.0101  0.0181  -0.0536 12   DT  E "C1'" 
5694 N  N1    . DT  B 12  ? 0.2001 0.2677 0.7148 0.0116  0.0176  -0.0555 12   DT  E N1    
5695 C  C2    . DT  B 12  ? 0.1925 0.2618 0.7025 0.0111  0.0166  -0.054  12   DT  E C2    
5696 O  O2    . DT  B 12  ? 0.189  0.2583 0.6971 0.0094  0.0161  -0.0512 12   DT  E O2    
5697 N  N3    . DT  B 12  ? 0.1904 0.2611 0.698  0.0128  0.0162  -0.0558 12   DT  E N3    
5698 C  C4    . DT  B 12  ? 0.1949 0.2654 0.7038 0.0149  0.0165  -0.0592 12   DT  E C4    
5699 O  O4    . DT  B 12  ? 0.1986 0.2706 0.7045 0.0165  0.0161  -0.0606 12   DT  E O4    
5700 C  C5    . DT  B 12  ? 0.1914 0.2597 0.705  0.0152  0.0173  -0.0608 12   DT  E C5    
5701 C  C7    . DT  B 12  ? 0.1896 0.257  0.7049 0.0175  0.0174  -0.0646 12   DT  E C7    
5702 C  C6    . DT  B 12  ? 0.1938 0.2609 0.7103 0.0135  0.0178  -0.0588 12   DT  E C6    
5703 P  P     . DC  B 13  ? 0.3401 0.4054 0.8678 0.0083  0.022   -0.0459 13   DC  E P     
5704 O  OP1   . DC  B 13  ? 0.3504 0.4146 0.8793 0.0072  0.0222  -0.0437 13   DC  E OP1   
5705 O  OP2   . DC  B 13  ? 0.3378 0.4032 0.8695 0.0099  0.0234  -0.0475 13   DC  E OP2   
5706 O  "O5'" . DC  B 13  ? 0.3502 0.4179 0.8734 0.0079  0.0215  -0.0433 13   DC  E "O5'" 
5707 C  "C5'" . DC  B 13  ? 0.3606 0.4281 0.8793 0.0065  0.02    -0.0417 13   DC  E "C5'" 
5708 C  "C4'" . DC  B 13  ? 0.3689 0.4389 0.8842 0.0064  0.0194  -0.0399 13   DC  E "C4'" 
5709 O  "O4'" . DC  B 13  ? 0.3665 0.4371 0.8803 0.0077  0.019   -0.0428 13   DC  E "O4'" 
5710 C  "C3'" . DC  B 13  ? 0.3726 0.445  0.8898 0.007   0.0209  -0.0372 13   DC  E "C3'" 
5711 O  "O3'" . DC  B 13  ? 0.3788 0.4522 0.8945 0.0054  0.0203  -0.0332 13   DC  E "O3'" 
5712 C  "C2'" . DC  B 13  ? 0.3689 0.4436 0.8847 0.0085  0.021   -0.0381 13   DC  E "C2'" 
5713 C  "C1'" . DC  B 13  ? 0.3588 0.4322 0.8713 0.0085  0.0194  -0.041  13   DC  E "C1'" 
5714 N  N1    . DC  B 13  ? 0.3365 0.4105 0.849  0.0107  0.0197  -0.0442 13   DC  E N1    
5715 C  C2    . DC  B 13  ? 0.3214 0.3969 0.83   0.0113  0.0187  -0.0448 13   DC  E C2    
5716 O  O2    . DC  B 13  ? 0.3156 0.3918 0.8212 0.0098  0.0174  -0.0426 13   DC  E O2    
5717 N  N3    . DC  B 13  ? 0.3163 0.3924 0.8245 0.0135  0.019   -0.0478 13   DC  E N3    
5718 C  C4    . DC  B 13  ? 0.3186 0.3935 0.8301 0.0151  0.0201  -0.0501 13   DC  E C4    
5719 N  N4    . DC  B 13  ? 0.3178 0.393  0.8284 0.0174  0.0201  -0.0532 13   DC  E N4    
5720 C  C5    . DC  B 13  ? 0.3219 0.3952 0.8376 0.0143  0.0212  -0.0495 13   DC  E C5    
5721 C  C6    . DC  B 13  ? 0.3289 0.402  0.845  0.0122  0.021   -0.0464 13   DC  E C6    
5722 O  "O5'" . DG  C 1   ? 0.4512 0.5477 0.9364 0.0272  0.0174  -0.0468 1    DG  F "O5'" 
5723 C  "C5'" . DG  C 1   ? 0.4437 0.5434 0.9286 0.0258  0.0173  -0.0415 1    DG  F "C5'" 
5724 C  "C4'" . DG  C 1   ? 0.4346 0.532  0.9208 0.0217  0.016   -0.0395 1    DG  F "C4'" 
5725 O  "O4'" . DG  C 1   ? 0.4261 0.5206 0.9152 0.0205  0.0166  -0.0404 1    DG  F "O4'" 
5726 C  "C3'" . DG  C 1   ? 0.4327 0.5277 0.9169 0.0198  0.0142  -0.0418 1    DG  F "C3'" 
5727 O  "O3'" . DG  C 1   ? 0.4403 0.5354 0.9243 0.0168  0.013   -0.0381 1    DG  F "O3'" 
5728 C  "C2'" . DG  C 1   ? 0.4212 0.512  0.9071 0.0189  0.0141  -0.0457 1    DG  F "C2'" 
5729 C  "C1'" . DG  C 1   ? 0.4102 0.5008 0.8992 0.0184  0.0153  -0.0433 1    DG  F "C1'" 
5730 N  N9    . DG  C 1   ? 0.3835 0.4715 0.875  0.0192  0.0161  -0.0468 1    DG  F N9    
5731 C  C8    . DG  C 1   ? 0.3759 0.4633 0.8672 0.0219  0.0166  -0.0508 1    DG  F C8    
5732 N  N7    . DG  C 1   ? 0.3674 0.4521 0.8615 0.0219  0.0171  -0.0531 1    DG  F N7    
5733 C  C5    . DG  C 1   ? 0.3585 0.4421 0.8548 0.0191  0.0172  -0.0502 1    DG  F C5    
5734 C  C6    . DG  C 1   ? 0.3488 0.4299 0.8487 0.018   0.0178  -0.0507 1    DG  F C6    
5735 O  O6    . DG  C 1   ? 0.3502 0.4292 0.8526 0.0191  0.0183  -0.0538 1    DG  F O6    
5736 N  N1    . DG  C 1   ? 0.3395 0.4203 0.8402 0.0154  0.0176  -0.0472 1    DG  F N1    
5737 C  C2    . DG  C 1   ? 0.3397 0.4223 0.838  0.0139  0.0166  -0.0437 1    DG  F C2    
5738 N  N2    . DG  C 1   ? 0.3363 0.418  0.8355 0.0115  0.0163  -0.0408 1    DG  F N2    
5739 N  N3    . DG  C 1   ? 0.3468 0.4317 0.8421 0.0147  0.016   -0.0432 1    DG  F N3    
5740 C  C4    . DG  C 1   ? 0.363  0.4484 0.8574 0.0174  0.0164  -0.0465 1    DG  F C4    
5741 P  P     . DA  C 2   ? 0.4436 0.5362 0.9252 0.0145  0.0111  -0.0393 2    DA  F P     
5742 O  OP1   . DA  C 2   ? 0.4506 0.5455 0.9311 0.0133  0.01    -0.035  2    DA  F OP1   
5743 O  OP2   . DA  C 2   ? 0.4459 0.5374 0.926  0.0162  0.0109  -0.0441 2    DA  F OP2   
5744 O  "O5'" . DA  C 2   ? 0.412  0.5006 0.8954 0.0118  0.0106  -0.0394 2    DA  F "O5'" 
5745 C  "C5'" . DA  C 2   ? 0.3692 0.4582 0.8544 0.01    0.0106  -0.0352 2    DA  F "C5'" 
5746 C  "C4'" . DA  C 2   ? 0.3263 0.4113 0.8122 0.0077  0.01    -0.0358 2    DA  F "C4'" 
5747 O  "O4'" . DA  C 2   ? 0.3021 0.3855 0.7905 0.0089  0.0113  -0.0389 2    DA  F "O4'" 
5748 C  "C3'" . DA  C 2   ? 0.3004 0.3823 0.7837 0.0061  0.0083  -0.0374 2    DA  F "C3'" 
5749 O  "O3'" . DA  C 2   ? 0.2832 0.3625 0.7665 0.0037  0.0073  -0.0353 2    DA  F "O3'" 
5750 C  "C2'" . DA  C 2   ? 0.2911 0.371  0.7752 0.0074  0.009   -0.0421 2    DA  F "C2'" 
5751 C  "C1'" . DA  C 2   ? 0.2829 0.363  0.7707 0.0082  0.0106  -0.0421 2    DA  F "C1'" 
5752 N  N9    . DA  C 2   ? 0.2553 0.335  0.7446 0.0103  0.0116  -0.0461 2    DA  F N9    
5753 C  C8    . DA  C 2   ? 0.2456 0.327  0.7336 0.0125  0.0118  -0.0486 2    DA  F C8    
5754 N  N7    . DA  C 2   ? 0.2324 0.3128 0.7224 0.0142  0.0126  -0.0519 2    DA  F N7    
5755 C  C5    . DA  C 2   ? 0.2271 0.3053 0.7201 0.0129  0.0131  -0.0514 2    DA  F C5    
5756 C  C6    . DA  C 2   ? 0.2216 0.2978 0.718  0.0135  0.014   -0.0538 2    DA  F C6    
5757 N  N6    . DA  C 2   ? 0.2193 0.2952 0.7166 0.0157  0.0142  -0.0574 2    DA  F N6    
5758 N  N1    . DA  C 2   ? 0.2215 0.2961 0.7207 0.012   0.0144  -0.0521 2    DA  F N1    
5759 C  C2    . DA  C 2   ? 0.22   0.2947 0.718  0.0099  0.0139  -0.0487 2    DA  F C2    
5760 N  N3    . DA  C 2   ? 0.2259 0.302  0.7206 0.0091  0.0129  -0.0463 2    DA  F N3    
5761 C  C4    . DA  C 2   ? 0.2352 0.313  0.7277 0.0106  0.0126  -0.0478 2    DA  F C4    
5762 P  P     . DG  C 3   ? 0.2735 0.3496 0.7535 0.0018  0.0054  -0.0356 3    DG  F P     
5763 O  OP1   . DG  C 3   ? 0.2726 0.3475 0.7521 -0.0005 0.0041  -0.0319 3    DG  F OP1   
5764 O  OP2   . DG  C 3   ? 0.2802 0.3576 0.7576 0.0026  0.0047  -0.0367 3    DG  F OP2   
5765 O  "O5'" . DG  C 3   ? 0.2225 0.2953 0.7032 0.002   0.0059  -0.0392 3    DG  F "O5'" 
5766 C  "C5'" . DG  C 3   ? 0.1748 0.2459 0.6579 0.0014  0.0066  -0.0388 3    DG  F "C5'" 
5767 C  "C4'" . DG  C 3   ? 0.1288 0.1976 0.6132 0.0022  0.0073  -0.0424 3    DG  F "C4'" 
5768 O  "O4'" . DG  C 3   ? 0.1138 0.1845 0.6007 0.0042  0.0086  -0.045  3    DG  F "O4'" 
5769 C  "C3'" . DG  C 3   ? 0.1036 0.1702 0.5851 0.0019  0.0062  -0.0444 3    DG  F "C3'" 
5770 O  "O3'" . DG  C 3   ? 0.0827 0.1463 0.5652 0.0015  0.0065  -0.0454 3    DG  F "O3'" 
5771 C  "C2'" . DG  C 3   ? 0.1094 0.1777 0.5914 0.0037  0.0067  -0.0476 3    DG  F "C2'" 
5772 C  "C1'" . DG  C 3   ? 0.1119 0.1812 0.5982 0.0048  0.0083  -0.0484 3    DG  F "C1'" 
5773 N  N9    . DG  C 3   ? 0.1091 0.1803 0.5964 0.0069  0.009   -0.0511 3    DG  F N9    
5774 C  C8    . DG  C 3   ? 0.1119 0.1853 0.5967 0.008   0.0086  -0.0519 3    DG  F C8    
5775 N  N7    . DG  C 3   ? 0.1175 0.192  0.6037 0.01    0.0092  -0.0548 3    DG  F N7    
5776 C  C5    . DG  C 3   ? 0.1135 0.1862 0.6034 0.0101  0.0101  -0.056  3    DG  F C5    
5777 C  C6    . DG  C 3   ? 0.1125 0.1848 0.6052 0.0118  0.0108  -0.0591 3    DG  F C6    
5778 O  O6    . DG  C 3   ? 0.1127 0.1862 0.6047 0.0138  0.0108  -0.0617 3    DG  F O6    
5779 N  N1    . DG  C 3   ? 0.1122 0.1826 0.6088 0.0111  0.0116  -0.059  3    DG  F N1    
5780 C  C2    . DG  C 3   ? 0.1058 0.1749 0.6031 0.0092  0.0117  -0.0563 3    DG  F C2    
5781 N  N2    . DG  C 3   ? 0.0975 0.1649 0.5988 0.0089  0.0126  -0.0564 3    DG  F N2    
5782 N  N3    . DG  C 3   ? 0.1061 0.1753 0.6004 0.0077  0.0109  -0.0535 3    DG  F N3    
5783 C  C4    . DG  C 3   ? 0.1105 0.1814 0.6013 0.0082  0.0101  -0.0536 3    DG  F C4    
5784 P  P     . DG  C 4   ? 0.0672 0.1275 0.5464 0.0002  0.0052  -0.0443 4    DG  F P     
5785 O  OP1   . DG  C 4   ? 0.0742 0.1341 0.552  -0.0012 0.0044  -0.0407 4    DG  F OP1   
5786 O  OP2   . DG  C 4   ? 0.059  0.1186 0.535  0.0003  0.0043  -0.0459 4    DG  F OP2   
5787 O  "O5'" . DG  C 4   ? 0.0791 0.1374 0.5615 0.0006  0.0064  -0.0455 4    DG  F "O5'" 
5788 C  "C5'" . DG  C 4   ? 0.0696 0.1284 0.5557 0.0007  0.0076  -0.0444 4    DG  F "C5'" 
5789 C  "C4'" . DG  C 4   ? 0.0667 0.1258 0.5575 0.002   0.0091  -0.0469 4    DG  F "C4'" 
5790 O  "O4'" . DG  C 4   ? 0.0615 0.1229 0.5535 0.003   0.0094  -0.0491 4    DG  F "O4'" 
5791 C  "C3'" . DG  C 4   ? 0.0652 0.1221 0.5565 0.0023  0.0091  -0.0488 4    DG  F "C3'" 
5792 O  "O3'" . DG  C 4   ? 0.055  0.1115 0.5513 0.0028  0.0105  -0.0491 4    DG  F "O3'" 
5793 C  "C2'" . DG  C 4   ? 0.0651 0.1232 0.5562 0.0031  0.0087  -0.0519 4    DG  F "C2'" 
5794 C  "C1'" . DG  C 4   ? 0.0631 0.1236 0.5566 0.0038  0.0095  -0.0523 4    DG  F "C1'" 
5795 N  N9    . DG  C 4   ? 0.0654 0.1277 0.5574 0.0047  0.009   -0.0544 4    DG  F N9    
5796 C  C8    . DG  C 4   ? 0.0638 0.1269 0.5514 0.0045  0.0078  -0.054  4    DG  F C8    
5797 N  N7    . DG  C 4   ? 0.0646 0.1295 0.5518 0.0057  0.0077  -0.0563 4    DG  F N7    
5798 C  C5    . DG  C 4   ? 0.0669 0.1318 0.5583 0.0068  0.0086  -0.0586 4    DG  F C5    
5799 C  C6    . DG  C 4   ? 0.0714 0.1376 0.5641 0.0085  0.0088  -0.0617 4    DG  F C6    
5800 O  O6    . DG  C 4   ? 0.0774 0.1452 0.5675 0.0096  0.0082  -0.0631 4    DG  F O6    
5801 N  N1    . DG  C 4   ? 0.0658 0.131  0.5631 0.0091  0.0095  -0.0634 4    DG  F N1    
5802 C  C2    . DG  C 4   ? 0.0644 0.128  0.565  0.0082  0.0104  -0.0618 4    DG  F C2    
5803 N  N2    . DG  C 4   ? 0.0591 0.122  0.5644 0.009   0.0111  -0.0636 4    DG  F N2    
5804 N  N3    . DG  C 4   ? 0.0623 0.125  0.5616 0.0068  0.0104  -0.0587 4    DG  F N3    
5805 C  C4    . DG  C 4   ? 0.0622 0.1255 0.5568 0.0061  0.0094  -0.0574 4    DG  F C4    
5806 P  P     . DA  C 5   ? 0.0599 0.1148 0.559  0.0033  0.011   -0.0507 5    DA  F P     
5807 O  OP1   . DA  C 5   ? 0.0696 0.1235 0.5716 0.0033  0.0121  -0.0487 5    DA  F OP1   
5808 O  OP2   . DA  C 5   ? 0.067  0.1207 0.5622 0.0031  0.0098  -0.0515 5    DA  F OP2   
5809 O  "O5'" . DA  C 5   ? 0.0511 0.1073 0.5546 0.0043  0.0115  -0.0538 5    DA  F "O5'" 
5810 C  "C5'" . DA  C 5   ? 0.0415 0.099  0.5488 0.0047  0.0126  -0.0537 5    DA  F "C5'" 
5811 C  "C4'" . DA  C 5   ? 0.0494 0.107  0.5614 0.0057  0.013   -0.0568 5    DA  F "C4'" 
5812 O  "O4'" . DA  C 5   ? 0.0555 0.1141 0.5653 0.0063  0.012   -0.0595 5    DA  F "O4'" 
5813 C  "C3'" . DA  C 5   ? 0.0514 0.1074 0.5666 0.0057  0.013   -0.0578 5    DA  F "C3'" 
5814 O  "O3'" . DA  C 5   ? 0.0469 0.1028 0.5682 0.0063  0.0137  -0.0593 5    DA  F "O3'" 
5815 C  "C2'" . DA  C 5   ? 0.0531 0.1091 0.5651 0.0058  0.0115  -0.0601 5    DA  F "C2'" 
5816 C  "C1'" . DA  C 5   ? 0.0613 0.1189 0.5715 0.0064  0.0111  -0.0618 5    DA  F "C1'" 
5817 N  N9    . DA  C 5   ? 0.0733 0.1318 0.5783 0.0064  0.0099  -0.0625 5    DA  F N9    
5818 C  C8    . DA  C 5   ? 0.076  0.1341 0.5761 0.0055  0.0093  -0.0604 5    DA  F C8    
5819 N  N7    . DA  C 5   ? 0.0801 0.1391 0.5763 0.0057  0.0083  -0.0615 5    DA  F N7    
5820 C  C5    . DA  C 5   ? 0.0768 0.137  0.5752 0.0069  0.0082  -0.0646 5    DA  F C5    
5821 C  C6    . DA  C 5   ? 0.0713 0.133  0.5674 0.0079  0.0073  -0.067  5    DA  F C6    
5822 N  N6    . DA  C 5   ? 0.06   0.1225 0.5512 0.0076  0.0065  -0.0664 5    DA  F N6    
5823 N  N1    . DA  C 5   ? 0.0766 0.1388 0.5754 0.0092  0.0072  -0.07   5    DA  F N1    
5824 C  C2    . DA  C 5   ? 0.0808 0.1419 0.5847 0.0093  0.008   -0.0706 5    DA  F C2    
5825 N  N3    . DA  C 5   ? 0.0774 0.1373 0.5842 0.0084  0.009   -0.0684 5    DA  F N3    
5826 C  C4    . DA  C 5   ? 0.0769 0.1365 0.5806 0.0073  0.009   -0.0654 5    DA  F C4    
5827 P  P     . DA  C 6   ? 0.0417 0.0962 0.5683 0.0064  0.0139  -0.06   6    DA  F P     
5828 O  OP1   . DA  C 6   ? 0.0419 0.0964 0.5748 0.0068  0.0151  -0.0602 6    DA  F OP1   
5829 O  OP2   . DA  C 6   ? 0.0415 0.0952 0.5661 0.0059  0.0141  -0.0575 6    DA  F OP2   
5830 O  "O5'" . DA  C 6   ? 0.0417 0.0962 0.568  0.0067  0.0124  -0.0636 6    DA  F "O5'" 
5831 C  "C5'" . DA  C 6   ? 0.0512 0.1064 0.5778 0.0074  0.0118  -0.0665 6    DA  F "C5'" 
5832 C  "C4'" . DA  C 6   ? 0.062  0.1174 0.5866 0.0077  0.0102  -0.0696 6    DA  F "C4'" 
5833 O  "O4'" . DA  C 6   ? 0.0597 0.116  0.5778 0.0075  0.0096  -0.0688 6    DA  F "O4'" 
5834 C  "C3'" . DA  C 6   ? 0.0664 0.1207 0.5943 0.0074  0.0094  -0.0707 6    DA  F "C3'" 
5835 O  "O3'" . DA  C 6   ? 0.0795 0.1332 0.6124 0.0079  0.0087  -0.0737 6    DA  F "O3'" 
5836 C  "C2'" . DA  C 6   ? 0.0548 0.1097 0.5773 0.0073  0.0081  -0.0716 6    DA  F "C2'" 
5837 C  "C1'" . DA  C 6   ? 0.0538 0.1101 0.5707 0.0077  0.0082  -0.0713 6    DA  F "C1'" 
5838 N  N9    . DA  C 6   ? 0.054  0.1108 0.5651 0.0072  0.0077  -0.0701 6    DA  F N9    
5839 C  C8    . DA  C 6   ? 0.0494 0.1055 0.5577 0.0064  0.0082  -0.067  6    DA  F C8    
5840 N  N7    . DA  C 6   ? 0.0441 0.1006 0.547  0.0062  0.0074  -0.0666 6    DA  F N7    
5841 C  C5    . DA  C 6   ? 0.0432 0.1011 0.5453 0.007   0.0065  -0.0696 6    DA  F C5    
5842 C  C6    . DA  C 6   ? 0.0416 0.1007 0.5391 0.0073  0.0056  -0.0706 6    DA  F C6    
5843 N  N6    . DA  C 6   ? 0.0407 0.0863 0.5199 0.0047  0.0049  -0.0686 6    DA  F N6    
5844 N  N1    . DA  C 6   ? 0.0479 0.1084 0.5457 0.0084  0.0049  -0.0737 6    DA  F N1    
5845 C  C2    . DA  C 6   ? 0.0578 0.118  0.5601 0.0091  0.0049  -0.0757 6    DA  F C2    
5846 N  N3    . DA  C 6   ? 0.0588 0.1177 0.566  0.0088  0.0058  -0.0751 6    DA  F N3    
5847 C  C4    . DA  C 6   ? 0.054  0.112  0.5609 0.0077  0.0066  -0.0718 6    DA  F C4    
5848 P  P     . DT  C 7   ? 0.0836 0.1364 0.6221 0.0075  0.0077  -0.0749 7    DT  F P     
5849 O  OP1   . DT  C 7   ? 0.0798 0.1316 0.6244 0.0079  0.0074  -0.0771 7    DT  F OP1   
5850 O  OP2   . DT  C 7   ? 0.0753 0.1278 0.6146 0.0068  0.0086  -0.0716 7    DT  F OP2   
5851 O  "O5'" . DT  C 7   ? 0.1092 0.1625 0.6438 0.0077  0.0058  -0.0777 7    DT  F "O5'" 
5852 C  "C5'" . DT  C 7   ? 0.1251 0.1789 0.6577 0.0088  0.0047  -0.0811 7    DT  F "C5'" 
5853 C  "C4'" . DT  C 7   ? 0.1303 0.1852 0.6578 0.009   0.0033  -0.0828 7    DT  F "C4'" 
5854 O  "O4'" . DT  C 7   ? 0.1243 0.1803 0.6457 0.0088  0.0042  -0.0803 7    DT  F "O4'" 
5855 C  "C3'" . DT  C 7   ? 0.1385 0.1931 0.6681 0.0083  0.0022  -0.0833 7    DT  F "C3'" 
5856 O  "O3'" . DT  C 7   ? 0.161  0.2149 0.6951 0.0086  0.0005  -0.0868 7    DT  F "O3'" 
5857 C  "C2'" . DT  C 7   ? 0.1273 0.1834 0.6499 0.0085  0.0016  -0.0834 7    DT  F "C2'" 
5858 C  "C1'" . DT  C 7   ? 0.1155 0.1723 0.6333 0.0088  0.003   -0.0814 7    DT  F "C1'" 
5859 N  N1    . DT  C 7   ? 0.0998 0.1568 0.6134 0.008   0.0037  -0.0782 7    DT  F N1    
5860 C  C2    . DT  C 7   ? 0.108  0.1661 0.616  0.0082  0.0031  -0.0786 7    DT  F C2    
5861 O  O2    . DT  C 7   ? 0.1211 0.1804 0.6273 0.0091  0.002   -0.0813 7    DT  F O2    
5862 N  N3    . DT  C 7   ? 0.0933 0.1511 0.5977 0.0075  0.0037  -0.0756 7    DT  F N3    
5863 C  C4    . DT  C 7   ? 0.0824 0.1389 0.5879 0.0067  0.0048  -0.0726 7    DT  F C4    
5864 O  O4    . DT  C 7   ? 0.0883 0.1442 0.5897 0.0063  0.005   -0.0704 7    DT  F O4    
5865 C  C5    . DT  C 7   ? 0.0681 0.1237 0.5797 0.0067  0.0055  -0.0723 7    DT  F C5    
5866 C  C7    . DT  C 7   ? 0.0508 0.1052 0.5641 0.0061  0.0069  -0.0689 7    DT  F C7    
5867 C  C6    . DT  C 7   ? 0.0781 0.134  0.5936 0.0072  0.005   -0.0751 7    DT  F C6    
5868 P  P     . DG  C 8   ? 0.1904 0.2439 0.7291 0.0078  -0.001  -0.0875 8    DG  F P     
5869 O  OP1   . DG  C 8   ? 0.1897 0.2418 0.7344 0.008   -0.0025 -0.0905 8    DG  F OP1   
5870 O  OP2   . DG  C 8   ? 0.1949 0.2484 0.7352 0.0069  0.0004  -0.0835 8    DG  F OP2   
5871 O  "O5'" . DG  C 8   ? 0.2031 0.258  0.7361 0.0083  -0.0024 -0.0894 8    DG  F "O5'" 
5872 C  "C5'" . DG  C 8   ? 0.2069 0.2624 0.7363 0.0096  -0.0036 -0.0928 8    DG  F "C5'" 
5873 C  "C4'" . DG  C 8   ? 0.2094 0.2667 0.7333 0.01    -0.0045 -0.0938 8    DG  F "C4'" 
5874 O  "O4'" . DG  C 8   ? 0.1971 0.2554 0.7158 0.0097  -0.0028 -0.0905 8    DG  F "O4'" 
5875 C  "C3'" . DG  C 8   ? 0.2159 0.2733 0.7425 0.0092  -0.006  -0.0945 8    DG  F "C3'" 
5876 O  "O3'" . DG  C 8   ? 0.244  0.3026 0.767  0.0102  -0.0077 -0.0976 8    DG  F "O3'" 
5877 C  "C2'" . DG  C 8   ? 0.2023 0.2603 0.7265 0.0083  -0.0044 -0.0905 8    DG  F "C2'" 
5878 C  "C1'" . DG  C 8   ? 0.1894 0.2482 0.7068 0.009   -0.0032 -0.0894 8    DG  F "C1'" 
5879 N  N9    . DG  C 8   ? 0.1753 0.2339 0.6905 0.0082  -0.0014 -0.0854 8    DG  F N9    
5880 C  C8    . DG  C 8   ? 0.1708 0.2281 0.6896 0.0074  0       -0.0825 8    DG  F C8    
5881 N  N7    . DG  C 8   ? 0.1718 0.2289 0.6868 0.0071  0.0012  -0.0794 8    DG  F N7    
5882 C  C5    . DG  C 8   ? 0.1709 0.2292 0.6799 0.0074  0.0006  -0.0801 8    DG  F C5    
5883 C  C6    . DG  C 8   ? 0.1748 0.2332 0.6781 0.0072  0.0012  -0.0778 8    DG  F C6    
5884 O  O6    . DG  C 8   ? 0.1785 0.2357 0.6803 0.0067  0.0023  -0.0747 8    DG  F O6    
5885 N  N1    . DG  C 8   ? 0.1801 0.24   0.6787 0.0078  0.0003  -0.0794 8    DG  F N1    
5886 C  C2    . DG  C 8   ? 0.1814 0.2428 0.6807 0.0086  -0.001  -0.0829 8    DG  F C2    
5887 N  N2    . DG  C 8   ? 0.1894 0.2523 0.6836 0.0092  -0.0015 -0.0838 8    DG  F N2    
5888 N  N3    . DG  C 8   ? 0.1766 0.2376 0.6808 0.0089  -0.0017 -0.0852 8    DG  F N3    
5889 C  C4    . DG  C 8   ? 0.1763 0.2358 0.6854 0.0082  -0.0009 -0.0837 8    DG  F C4    
5890 P  P     . DC  C 9   ? 0.2708 0.3297 0.7969 0.0099  -0.0102 -0.1    9    DC  F P     
5891 O  OP1   . DC  C 9   ? 0.2833 0.3415 0.8104 0.0111  -0.0124 -0.1045 9    DC  F OP1   
5892 O  OP2   . DC  C 9   ? 0.2633 0.3214 0.7955 0.0083  -0.0099 -0.0975 9    DC  F OP2   
5893 O  "O5'" . DC  C 9   ? 0.2845 0.3457 0.8039 0.0103  -0.0101 -0.0996 9    DC  F "O5'" 
5894 C  "C5'" . DC  C 9   ? 0.2981 0.3606 0.8109 0.0118  -0.0097 -0.1006 9    DC  F "C5'" 
5895 C  "C4'" . DC  C 9   ? 0.3127 0.3773 0.8201 0.0118  -0.0094 -0.0993 9    DC  F "C4'" 
5896 O  "O4'" . DC  C 9   ? 0.3129 0.3772 0.8185 0.0109  -0.0072 -0.0951 9    DC  F "O4'" 
5897 C  "C3'" . DC  C 9   ? 0.325  0.3903 0.8345 0.0112  -0.0109 -0.1001 9    DC  F "C3'" 
5898 O  "O3'" . DC  C 9   ? 0.348  0.4156 0.8519 0.0123  -0.0115 -0.1012 9    DC  F "O3'" 
5899 C  "C2'" . DC  C 9   ? 0.3165 0.3812 0.8277 0.0097  -0.0094 -0.096  9    DC  F "C2'" 
5900 C  "C1'" . DC  C 9   ? 0.3072 0.3717 0.8134 0.0099  -0.0072 -0.0934 9    DC  F "C1'" 
5901 N  N1    . DC  C 9   ? 0.2901 0.353  0.7984 0.0088  -0.0055 -0.0897 9    DC  F N1    
5902 C  C2    . DC  C 9   ? 0.2791 0.342  0.7829 0.0085  -0.004  -0.0865 9    DC  F C2    
5903 O  O2    . DC  C 9   ? 0.2767 0.3409 0.7749 0.009   -0.0041 -0.0867 9    DC  F O2    
5904 N  N3    . DC  C 9   ? 0.2693 0.3306 0.7746 0.0077  -0.0026 -0.0832 9    DC  F N3    
5905 C  C4    . DC  C 9   ? 0.2609 0.321  0.7724 0.0073  -0.0024 -0.0829 9    DC  F C4    
5906 N  N4    . DC  C 9   ? 0.2461 0.3049 0.7588 0.0068  -0.0008 -0.0795 9    DC  F N4    
5907 C  C5    . DC  C 9   ? 0.2695 0.3297 0.7863 0.0074  -0.0038 -0.086  9    DC  F C5    
5908 C  C6    . DC  C 9   ? 0.28   0.3414 0.7948 0.0082  -0.0054 -0.0894 9    DC  F C6    
5909 P  P     . DA  C 10  ? 0.3677 0.4366 0.8727 0.0122  -0.0135 -0.1032 10   DA  F P     
5910 O  OP1   . DA  C 10  ? 0.3724 0.4431 0.873  0.0141  -0.0148 -0.1066 10   DA  F OP1   
5911 O  OP2   . DA  C 10  ? 0.3685 0.4359 0.881  0.011   -0.0148 -0.1037 10   DA  F OP2   
5912 O  "O5'" . DA  C 10  ? 0.3703 0.4403 0.872  0.0115  -0.012  -0.0996 10   DA  F "O5'" 
5913 C  "C5'" . DA  C 10  ? 0.3665 0.4368 0.8628 0.0118  -0.01   -0.0971 10   DA  F "C5'" 
5914 C  "C4'" . DA  C 10  ? 0.3624 0.4328 0.8566 0.0109  -0.0087 -0.0937 10   DA  F "C4'" 
5915 O  "O4'" . DA  C 10  ? 0.3491 0.4173 0.8455 0.0098  -0.0072 -0.0905 10   DA  F "O4'" 
5916 C  "C3'" . DA  C 10  ? 0.3668 0.4382 0.8633 0.0105  -0.0099 -0.094  10   DA  F "C3'" 
5917 O  "O3'" . DA  C 10  ? 0.3866 0.4593 0.878  0.0108  -0.009  -0.0923 10   DA  F "O3'" 
5918 C  "C2'" . DA  C 10  ? 0.3493 0.4188 0.8517 0.0092  -0.0093 -0.0917 10   DA  F "C2'" 
5919 C  "C1'" . DA  C 10  ? 0.3295 0.3973 0.8293 0.009   -0.0071 -0.0888 10   DA  F "C1'" 
5920 N  N9    . DA  C 10  ? 0.2851 0.3509 0.7904 0.0082  -0.0065 -0.0873 10   DA  F N9    
5921 C  C8    . DA  C 10  ? 0.2711 0.3363 0.7827 0.0079  -0.0076 -0.0891 10   DA  F C8    
5922 N  N7    . DA  C 10  ? 0.2598 0.3233 0.7755 0.0072  -0.0065 -0.0869 10   DA  F N7    
5923 C  C5    . DA  C 10  ? 0.2486 0.3115 0.7602 0.0071  -0.0046 -0.0834 10   DA  F C5    
5924 C  C6    . DA  C 10  ? 0.2297 0.291  0.7424 0.0068  -0.0028 -0.0798 10   DA  F C6    
5925 N  N6    . DA  C 10  ? 0.2176 0.2779 0.7365 0.0064  -0.0024 -0.079  10   DA  F N6    
5926 N  N1    . DA  C 10  ? 0.2272 0.2881 0.7345 0.007   -0.0015 -0.0771 10   DA  F N1    
5927 C  C2    . DA  C 10  ? 0.2374 0.2992 0.7388 0.0074  -0.0018 -0.0778 10   DA  F C2    
5928 N  N3    . DA  C 10  ? 0.2481 0.3118 0.7481 0.0078  -0.0033 -0.0809 10   DA  F N3    
5929 C  C4    . DA  C 10  ? 0.2575 0.3217 0.7627 0.0077  -0.0046 -0.0836 10   DA  F C4    
5930 P  P     . DG  C 11  ? 0.4022 0.4771 0.8934 0.011   -0.0103 -0.0932 11   DG  F P     
5931 O  OP1   . DG  C 11  ? 0.4103 0.4875 0.8959 0.0124  -0.0107 -0.0951 11   DG  F OP1   
5932 O  OP2   . DG  C 11  ? 0.3965 0.4712 0.8945 0.0104  -0.0121 -0.0949 11   DG  F OP2   
5933 O  "O5'" . DG  C 11  ? 0.3985 0.4726 0.8876 0.0105  -0.0085 -0.0891 11   DG  F "O5'" 
5934 C  "C5'" . DG  C 11  ? 0.3914 0.464  0.8759 0.0104  -0.0066 -0.0865 11   DG  F "C5'" 
5935 C  "C4'" . DG  C 11  ? 0.3831 0.4538 0.868  0.0098  -0.0051 -0.0828 11   DG  F "C4'" 
5936 O  "O4'" . DG  C 11  ? 0.367  0.4358 0.8572 0.0091  -0.0048 -0.0819 11   DG  F "O4'" 
5937 C  "C3'" . DG  C 11  ? 0.3875 0.4594 0.874  0.0098  -0.0054 -0.0819 11   DG  F "C3'" 
5938 O  "O3'" . DG  C 11  ? 0.4153 0.4858 0.8976 0.01    -0.0037 -0.0786 11   DG  F "O3'" 
5939 C  "C2'" . DG  C 11  ? 0.3636 0.4348 0.8578 0.0091  -0.006  -0.0818 11   DG  F "C2'" 
5940 C  "C1'" . DG  C 11  ? 0.3451 0.4138 0.8395 0.0087  -0.0047 -0.0803 11   DG  F "C1'" 
5941 N  N9    . DG  C 11  ? 0.3028 0.3707 0.8044 0.0081  -0.0052 -0.0807 11   DG  F N9    
5942 C  C8    . DG  C 11  ? 0.2852 0.3539 0.7918 0.0078  -0.0071 -0.0839 11   DG  F C8    
5943 N  N7    . DG  C 11  ? 0.2726 0.3399 0.785  0.0072  -0.007  -0.0834 11   DG  F N7    
5944 C  C5    . DG  C 11  ? 0.2634 0.3291 0.7743 0.0072  -0.0049 -0.0797 11   DG  F C5    
5945 C  C6    . DG  C 11  ? 0.2468 0.3108 0.7621 0.0068  -0.0037 -0.0774 11   DG  F C6    
5946 O  O6    . DG  C 11  ? 0.2333 0.2968 0.7551 0.0063  -0.0043 -0.0782 11   DG  F O6    
5947 N  N1    . DG  C 11  ? 0.2472 0.3099 0.7585 0.0072  -0.0017 -0.0738 11   DG  F N1    
5948 C  C2    . DG  C 11  ? 0.2485 0.3111 0.7526 0.0077  -0.001  -0.0727 11   DG  F C2    
5949 N  N2    . DG  C 11  ? 0.2423 0.3031 0.743  0.0081  0.0007  -0.0695 11   DG  F N2    
5950 N  N3    . DG  C 11  ? 0.2613 0.3254 0.7616 0.008   -0.002  -0.0748 11   DG  F N3    
5951 C  C4    . DG  C 11  ? 0.2759 0.3417 0.78   0.0077  -0.0038 -0.0781 11   DG  F C4    
5952 P  P     . DA  C 12  ? 0.4377 0.5097 0.9175 0.0105  -0.0036 -0.0774 12   DA  F P     
5953 O  OP1   . DA  C 12  ? 0.4419 0.5139 0.9143 0.0111  -0.0029 -0.077  12   DA  F OP1   
5954 O  OP2   . DA  C 12  ? 0.4336 0.5084 0.9181 0.0104  -0.0053 -0.0798 12   DA  F OP2   
5955 O  "O5'" . DA  C 12  ? 0.4352 0.5051 0.9164 0.0104  -0.002  -0.0736 12   DA  F "O5'" 
5956 C  "C5'" . DA  C 12  ? 0.4256 0.4925 0.9055 0.0103  -0.0007 -0.0715 12   DA  F "C5'" 
5957 C  "C4'" . DA  C 12  ? 0.4136 0.4793 0.8984 0.0103  0.0001  -0.0689 12   DA  F "C4'" 
5958 O  "O4'" . DA  C 12  ? 0.3976 0.4636 0.8892 0.0095  -0.0007 -0.0704 12   DA  F "O4'" 
5959 C  "C3'" . DA  C 12  ? 0.4114 0.4788 0.8987 0.0107  0.0002  -0.0675 12   DA  F "C3'" 
5960 O  "O3'" . DA  C 12  ? 0.4316 0.497  0.9159 0.0116  0.002   -0.0636 12   DA  F "O3'" 
5961 C  "C2'" . DA  C 12  ? 0.3909 0.4595 0.8873 0.01    -0.0009 -0.0682 12   DA  F "C2'" 
5962 C  "C1'" . DA  C 12  ? 0.3764 0.443  0.8742 0.0094  -0.0007 -0.0688 12   DA  F "C1'" 
5963 N  N9    . DA  C 12  ? 0.3403 0.4079 0.8454 0.0086  -0.0023 -0.0712 12   DA  F N9    
5964 C  C8    . DA  C 12  ? 0.326  0.3957 0.8335 0.0081  -0.0044 -0.0748 12   DA  F C8    
5965 N  N7    . DA  C 12  ? 0.3105 0.38   0.8246 0.0074  -0.0057 -0.0765 12   DA  F N7    
5966 C  C5    . DA  C 12  ? 0.3021 0.3697 0.8186 0.0073  -0.0041 -0.0736 12   DA  F C5    
5967 C  C6    . DA  C 12  ? 0.2847 0.3513 0.808  0.0067  -0.0042 -0.0734 12   DA  F C6    
5968 N  N6    . DA  C 12  ? 0.2769 0.3441 0.806  0.006   -0.0062 -0.0764 12   DA  F N6    
5969 N  N1    . DA  C 12  ? 0.2858 0.3508 0.8098 0.007   -0.0022 -0.0699 12   DA  F N1    
5970 C  C2    . DA  C 12  ? 0.3002 0.3643 0.8181 0.0079  -0.0003 -0.0671 12   DA  F C2    
5971 N  N3    . DA  C 12  ? 0.3133 0.3778 0.8243 0.0084  -0.0001 -0.0671 12   DA  F N3    
5972 C  C4    . DA  C 12  ? 0.3189 0.3854 0.8299 0.0081  -0.002  -0.0704 12   DA  F C4    
5973 P  P     . DC  C 13  ? 0.4522 0.5187 0.9368 0.0126  0.0028  -0.061  13   DC  F P     
5974 O  OP1   . DC  C 13  ? 0.4588 0.5228 0.9355 0.0138  0.0044  -0.0586 13   DC  F OP1   
5975 O  OP2   . DC  C 13  ? 0.4507 0.5208 0.9384 0.0121  0.0012  -0.0633 13   DC  F OP2   
5976 O  "O5'" . DC  C 13  ? 0.4499 0.5161 0.9416 0.0127  0.0035  -0.0584 13   DC  F "O5'" 
5977 C  "C5'" . DC  C 13  ? 0.4489 0.5125 0.9411 0.0127  0.0044  -0.0573 13   DC  F "C5'" 
5978 C  "C4'" . DC  C 13  ? 0.4408 0.5053 0.942  0.0123  0.0044  -0.0561 13   DC  F "C4'" 
5979 O  "O4'" . DC  C 13  ? 0.4333 0.4992 0.94   0.0108  0.0024  -0.0597 13   DC  F "O4'" 
5980 C  "C3'" . DC  C 13  ? 0.4339 0.5004 0.9401 0.0129  0.0047  -0.0535 13   DC  F "C3'" 
5981 O  "O3'" . DC  C 13  ? 0.4372 0.5022 0.9432 0.0144  0.0069  -0.0492 13   DC  F "O3'" 
5982 C  "C2'" . DC  C 13  ? 0.4214 0.4902 0.9374 0.0115  0.0028  -0.0554 13   DC  F "C2'" 
5983 C  "C1'" . DC  C 13  ? 0.4174 0.4847 0.9329 0.0105  0.0021  -0.0584 13   DC  F "C1'" 
5984 N  N1    . DC  C 13  ? 0.3979 0.4668 0.9189 0.0091  -0.0004 -0.0623 13   DC  F N1    
5985 C  C2    . DC  C 13  ? 0.3857 0.4543 0.9142 0.0082  -0.001  -0.0627 13   DC  F C2    
5986 O  O2    . DC  C 13  ? 0.3892 0.4564 0.9195 0.0087  0.0007  -0.0598 13   DC  F O2    
5987 N  N3    . DC  C 13  ? 0.3717 0.4414 0.905  0.0071  -0.0035 -0.0664 13   DC  F N3    
5988 C  C4    . DC  C 13  ? 0.369  0.4403 0.8999 0.0068  -0.0052 -0.0694 13   DC  F C4    
5989 N  N4    . DC  C 13  ? 0.365  0.4371 0.9004 0.0059  -0.0078 -0.0732 13   DC  F N4    
5990 C  C5    . DC  C 13  ? 0.3781 0.4501 0.9017 0.0077  -0.0045 -0.0689 13   DC  F C5    
5991 C  C6    . DC  C 13  ? 0.3885 0.4593 0.9075 0.0087  -0.0021 -0.0653 13   DC  F C6    
5992 CL CL    . CL  D .   ? 0.4365 0.4969 0.8959 -0.0218 -0.0253 -0.0022 701  CL  A CL    
5993 O  O1    . MES E .   ? 0.175  0.2431 0.7224 0.0235  0.0415  0.005   702  MES A O1    
5994 C  C2    . MES E .   ? 0.1793 0.2452 0.7204 0.0212  0.0384  0.0024  702  MES A C2    
5995 C  C3    . MES E .   ? 0.1854 0.2529 0.7283 0.0189  0.0381  0.0017  702  MES A C3    
5996 N  N4    . MES E .   ? 0.1871 0.2564 0.739  0.0186  0.0404  0.0007  702  MES A N4    
5997 C  C5    . MES E .   ? 0.1763 0.2476 0.7351 0.0209  0.0435  0.0033  702  MES A C5    
5998 C  C6    . MES E .   ? 0.1743 0.2441 0.7309 0.0231  0.0436  0.0042  702  MES A C6    
5999 C  C7    . MES E .   ? 0.1967 0.2676 0.7501 0.0168  0.0403  0.0003  702  MES A C7    
6000 C  C8    . MES E .   ? 0.2121 0.2831 0.771  0.0159  0.0411  -0.0025 702  MES A C8    
6001 S  S     . MES E .   ? 0.2291 0.3022 0.79   0.0144  0.0415  -0.0026 702  MES A S     
6002 O  O1S   . MES E .   ? 0.2251 0.297  0.7796 0.0126  0.0387  -0.0043 702  MES A O1S   
6003 O  O2S   . MES E .   ? 0.2283 0.3036 0.7897 0.0151  0.0426  0.001   702  MES A O2S   
6004 O  O3S   . MES E .   ? 0.2267 0.3003 0.7952 0.0146  0.0434  -0.0042 702  MES A O3S   
6005 O  O     . HOH F .   ? 0.167  0.2525 0.6021 0.0173  -0.0011 -0.0767 801  HOH A O     
6006 O  O     . HOH F .   ? 0.0722 0.1    0.4863 0.0226  0.0104  -0.0435 802  HOH A O     
6007 O  O     . HOH F .   ? 0.4695 0.6183 0.895  0.036   -0.0059 -0.0883 803  HOH A O     
6008 O  O     . HOH F .   ? 0.2603 0.3417 0.7468 -0.019  -0.0128 0.0087  804  HOH A O     
6009 O  O     . HOH F .   ? 0.2193 0.2151 0.5624 0.0316  0.0092  -0.0381 805  HOH A O     
6010 O  O     . HOH F .   ? 0.1394 0.1808 0.6164 0.0218  0.0179  -0.0009 806  HOH A O     
6011 O  O     . HOH F .   ? 0.2635 0.262  0.6492 0.0457  0.0193  -0.0218 807  HOH A O     
6012 O  O     . HOH F .   ? 0.3784 0.5315 0.7868 0.0648  -0.0058 -0.105  808  HOH A O     
6013 O  O     . HOH F .   ? 0.1541 0.2028 0.7325 0.0077  0.0151  -0.0669 809  HOH A O     
6014 O  O     . HOH F .   ? 0.1242 0.218  0.5724 0.0185  0.0015  -0.0618 810  HOH A O     
6015 O  O     . HOH F .   ? 0.0716 0.1365 0.6944 0.0193  0.0297  -0.0142 811  HOH A O     
6016 O  O     . HOH F .   ? 0.1303 0.1787 0.5666 0.0133  0.0046  -0.0582 812  HOH A O     
6017 O  O     . HOH F .   ? 0.2163 0.2317 0.6173 0.0391  0.0197  -0.0264 813  HOH A O     
6018 O  O     . HOH F .   ? 0.0398 0.0688 0.5029 -0.0011 0.0068  -0.0296 814  HOH A O     
6019 O  O     . HOH F .   ? 0.2955 0.35   0.9796 0.0025  0.0101  -0.0433 815  HOH A O     
6020 O  O     . HOH F .   ? 0.4002 0.4747 0.8779 -0.0142 -0.0093 -0.0055 816  HOH A O     
6021 O  O     . HOH F .   ? 0.2352 0.305  0.836  0.0402  0.0435  0.0142  817  HOH A O     
6022 O  O     . HOH F .   ? 0.1795 0.116  0.4992 0.0082  -0.0322 -0.0386 818  HOH A O     
6023 O  O     . HOH F .   ? 0.4488 0.5006 0.9948 0.0306  0.0333  -0.01   819  HOH A O     
6024 O  O     . HOH F .   ? 0.0402 0.0491 0.4892 0.0005  0.0094  -0.0435 820  HOH A O     
6025 O  O     . HOH F .   ? 0.3207 0.3367 0.7487 -0.0286 -0.0437 -0.0071 821  HOH A O     
6026 O  O     . HOH F .   ? 0.1817 0.2206 0.6155 0.0072  0.0009  -0.0559 822  HOH A O     
6027 O  O     . HOH F .   ? 0.2665 0.3851 0.6863 0.0299  0.0031  -0.0621 823  HOH A O     
6028 O  O     . HOH F .   ? 0.2994 0.3794 0.7351 0.015   -0.0013 -0.075  824  HOH A O     
6029 O  O     . HOH F .   ? 0.2661 0.419  0.6829 0.0499  0.0079  -0.0603 825  HOH A O     
6030 O  O     . HOH F .   ? 0.4429 0.5762 0.9137 0.0212  -0.0123 -0.077  826  HOH A O     
6031 O  O     . HOH F .   ? 0.3243 0.4393 0.7645 0.0351  0.0035  -0.0691 827  HOH A O     
6032 O  O     . HOH F .   ? 0.1996 0.1665 0.5554 -0.0084 -0.0371 -0.0307 828  HOH A O     
6033 O  O     . HOH F .   ? 0.1038 0.1564 0.6574 0.0054  0.0008  -0.0797 829  HOH A O     
6034 O  O     . HOH F .   ? 0.2689 0.3824 0.7435 0.0043  -0.0029 -0.0012 830  HOH A O     
6035 O  O     . HOH F .   ? 0.2021 0.3115 0.6475 0.0315  0.0038  -0.067  831  HOH A O     
6036 O  O     . HOH F .   ? 0.4927 0.5464 1.0226 0.0248  0.0225  -0.0227 832  HOH A O     
6037 O  O     . HOH F .   ? 0.0759 0.1272 0.6425 0.007   0.0168  -0.058  833  HOH A O     
6038 O  O     . HOH F .   ? 0.1315 0.1611 0.5706 0.0002  -0.003  -0.0436 834  HOH A O     
6039 O  O     . HOH F .   ? 0.3911 0.4424 0.7883 0.0302  0.0165  -0.0408 835  HOH A O     
6040 O  O     . HOH F .   ? 0.2041 0.2346 0.6228 -0.0118 -0.0216 -0.0297 836  HOH A O     
6041 O  O     . HOH F .   ? 0.1259 0.1264 0.5359 0.0021  -0.0143 -0.0285 837  HOH A O     
6042 O  O     . HOH F .   ? 0.1519 0.2351 0.5922 0.0134  -0.0008 -0.0642 838  HOH A O     
6043 O  O     . HOH F .   ? 0.2855 0.3045 0.7062 0.0291  0.0147  -0.0336 839  HOH A O     
6044 O  O     . HOH F .   ? 0.4187 0.3751 0.7565 0.0182  -0.0165 -0.0389 840  HOH A O     
6045 O  O     . HOH F .   ? 0.1981 0.2406 0.8644 0.0077  0.0226  -0.0541 841  HOH A O     
6046 O  O     . HOH F .   ? 0.1988 0.2132 0.6353 0.0173  0.0043  -0.0194 842  HOH A O     
6047 O  O     . HOH F .   ? 0.1582 0.1065 0.4616 0.0304  -0.0059 -0.0377 843  HOH A O     
6048 O  O     . HOH F .   ? 0.2271 0.2657 0.6547 -0.0185 -0.0302 -0.0136 844  HOH A O     
6049 O  O     . HOH F .   ? 0.2839 0.3231 0.7406 0.0077  0.0048  -0.0539 845  HOH A O     
6050 O  O     . HOH F .   ? 0.0624 0.0937 0.4595 0.032   0.0178  -0.0338 846  HOH A O     
6051 O  O     . HOH F .   ? 0.1319 0.1589 0.5653 -0.0248 -0.0354 -0.0108 847  HOH A O     
6052 O  O     . HOH F .   ? 0.2959 0.3564 0.8775 0.0305  0.0379  -0.0038 848  HOH A O     
6053 O  O     . HOH F .   ? 0.1518 0.2045 0.6149 -0.0112 -0.008  -0.0225 849  HOH A O     
6054 O  O     . HOH F .   ? 0.1274 0.1898 0.6101 -0.0019 0.0056  -0.0359 850  HOH A O     
6055 O  O     . HOH F .   ? 0.3394 0.3237 0.6937 -0.0008 -0.0252 -0.0245 851  HOH A O     
6056 O  O     . HOH F .   ? 0.0442 0.094  0.5083 -0.0079 -0.0041 -0.0284 852  HOH A O     
6057 O  O     . HOH F .   ? 0.445  0.5922 0.8846 0.0326  0.0065  -0.0141 853  HOH A O     
6058 O  O     . HOH F .   ? 0.2471 0.207  0.5878 0.0276  -0.0081 -0.0361 854  HOH A O     
6059 O  O     . HOH F .   ? 0.4084 0.3932 0.8036 -0.0241 -0.0497 -0.0177 855  HOH A O     
6060 O  O     . HOH F .   ? 0.1751 0.2303 0.7116 0.0062  -0.001  -0.0827 856  HOH A O     
6061 O  O     . HOH F .   ? 0.3097 0.3547 0.7846 0.0171  0.0133  0.0033  857  HOH A O     
6062 O  O     . HOH F .   ? 0.1323 0.1315 0.5389 0.0082  -0.008  -0.0336 858  HOH A O     
6063 O  O     . HOH F .   ? 0.2527 0.3047 0.6464 0.0111  -0.0016 -0.0497 859  HOH A O     
6064 O  O     . HOH F .   ? 0.5624 0.6315 1.0539 0.0014  0.0097  -0.0377 860  HOH A O     
6065 O  O     . HOH F .   ? 0.3563 0.3927 0.8052 0.0138  0.0077  -0.0498 861  HOH A O     
6066 O  O     . HOH F .   ? 0.0403 0.0747 0.5215 0.0011  0.0126  -0.0442 862  HOH A O     
6067 O  O     . HOH F .   ? 0.1379 0.2002 0.6513 0.0054  0.0217  -0.0056 863  HOH A O     
6068 O  O     . HOH F .   ? 0.3313 0.441  0.7532 0.0314  0.0142  -0.0468 864  HOH A O     
6069 O  O     . HOH F .   ? 0.4162 0.4218 0.836  0.0335  0.0084  -0.012  865  HOH A O     
6070 O  O     . HOH F .   ? 0.2045 0.3064 0.6507 0.0234  0.0024  -0.0618 866  HOH A O     
6071 O  O     . HOH F .   ? 0.1028 0.1486 0.4992 0.0036  -0.0095 -0.038  867  HOH A O     
6072 O  O     . HOH F .   ? 0.1434 0.1466 0.5455 -0.008  -0.0226 -0.0337 868  HOH A O     
6073 O  O     . HOH F .   ? 0.1655 0.2516 0.6072 0.0091  -0.0023 -0.0459 869  HOH A O     
6074 O  O     . HOH F .   ? 0.1275 0.2276 0.5925 0.0152  0.0051  -0.0381 870  HOH A O     
6075 O  O     . HOH F .   ? 0.118  0.1717 0.6815 0.008   0.0128  -0.0515 871  HOH A O     
6076 O  O     . HOH F .   ? 0.1806 0.1533 0.5306 0.0363  0.0041  -0.0327 872  HOH A O     
6077 O  O     . HOH F .   ? 0.4617 0.5515 0.9414 0.0195  -0.0208 -0.1126 873  HOH A O     
6078 O  O     . HOH F .   ? 0.2794 0.3665 0.734  0.0202  -0.0002 -0.0786 874  HOH A O     
6079 O  O     . HOH F .   ? 0.0771 0.132  0.5984 0.0061  0.0037  -0.0702 875  HOH A O     
6080 O  O     . HOH F .   ? 0.1673 0.2182 0.617  -0.0011 -0.0028 -0.0479 876  HOH A O     
6081 O  O     . HOH F .   ? 0.2139 0.2806 0.6376 0.0134  0.001   -0.066  877  HOH A O     
6082 O  O     . HOH F .   ? 0.4582 0.539  0.9049 0.0146  -0.0013 -0.0745 878  HOH A O     
6083 O  O     . HOH F .   ? 0.0904 0.1809 0.5621 -0.0056 -0.0072 -0.0088 879  HOH A O     
6084 O  O     . HOH F .   ? 0.0419 0.0943 0.6697 0.0068  0.0183  -0.0483 880  HOH A O     
6085 O  O     . HOH F .   ? 0.5255 0.5984 1.0253 -0.0068 0.0084  -0.0097 881  HOH A O     
6086 O  O     . HOH F .   ? 0.1562 0.1713 0.5724 0.0185  0.0065  -0.0419 882  HOH A O     
6087 O  O     . HOH F .   ? 0.1895 0.1946 0.5507 0.0464  0.022   -0.0245 883  HOH A O     
6088 O  O     . HOH F .   ? 0.087  0.1478 0.5297 0.0213  0.0102  -0.049  884  HOH A O     
6089 O  O     . HOH F .   ? 0.3551 0.4517 0.8558 0.0131  -0.0268 -0.1069 885  HOH A O     
6090 O  O     . HOH F .   ? 0.0486 0.1005 0.4984 -0.0206 -0.0258 -0.0088 886  HOH A O     
6091 O  O     . HOH F .   ? 0.4048 0.5303 0.8408 0.0398  -0.0186 -0.1167 887  HOH A O     
6092 O  O     . HOH F .   ? 0.2737 0.2361 0.624  0.0039  -0.0267 -0.0383 888  HOH A O     
6093 O  O     . HOH F .   ? 0.2437 0.3101 0.8774 0.0222  0.0375  -0.0077 889  HOH A O     
6094 O  O     . HOH F .   ? 0.4571 0.5081 0.963  0.0162  0.0132  -0.0423 890  HOH A O     
6095 O  O     . HOH F .   ? 0.2249 0.2639 0.6688 -0.0296 -0.0413 0.002   891  HOH A O     
6096 O  O     . HOH F .   ? 0.0943 0.1584 0.6037 0.0027  0.0162  -0.0373 892  HOH A O     
6097 O  O     . HOH F .   ? 0.3943 0.5515 0.8013 0.0518  0.0058  -0.0745 893  HOH A O     
6098 O  O     . HOH F .   ? 0.2942 0.3578 0.7057 0.0327  0.0191  -0.0358 894  HOH A O     
6099 O  O     . HOH F .   ? 0.1352 0.1285 0.5327 0.0164  -0.0037 -0.0335 895  HOH A O     
6100 O  O     . HOH F .   ? 0.2166 0.249  0.6782 0.026   0.0154  -0.0026 896  HOH A O     
6101 O  O     . HOH F .   ? 0.2463 0.3613 0.6958 0.0225  -0.0022 -0.0714 897  HOH A O     
6102 O  O     . HOH F .   ? 0.2908 0.3704 0.753  0.0092  0.0024  -0.0537 898  HOH A O     
6103 O  O     . HOH F .   ? 0.0398 0.0851 0.4931 0.0007  0.003   -0.0465 899  HOH A O     
6104 O  O     . HOH F .   ? 0.1024 0.1847 0.5555 0.0227  0.0091  -0.0485 900  HOH A O     
6105 O  O     . HOH F .   ? 0.3855 0.4103 0.8451 0.0438  0.0281  -0.0101 901  HOH A O     
6106 O  O     . HOH F .   ? 0.0395 0.0453 0.4585 -0.0005 0.0041  -0.0495 902  HOH A O     
6107 O  O     . HOH F .   ? 0.1241 0.0922 0.4563 0.0434  0.0085  -0.0305 903  HOH A O     
6108 O  O     . HOH F .   ? 0.5357 0.584  0.9701 0.0322  0.0193  -0.0304 904  HOH A O     
6109 O  O     . HOH F .   ? 0.1571 0.2024 0.6402 0.0047  0.0106  -0.0121 905  HOH A O     
6110 O  O     . HOH F .   ? 0.3176 0.3438 0.7463 0.0316  0.0177  -0.0306 906  HOH A O     
6111 O  O     . HOH F .   ? 0.4812 0.5203 0.9588 0.0232  0.0173  -0.0336 907  HOH A O     
6112 O  O     . HOH F .   ? 0.3356 0.2457 0.6421 -0.0023 -0.0495 -0.0301 908  HOH A O     
6113 O  O     . HOH F .   ? 0.2162 0.1813 0.5533 0.0322  -0.0011 -0.0361 909  HOH A O     
6114 O  O     . HOH F .   ? 0.318  0.3895 0.9322 0.0263  0.0519  0.0014  910  HOH A O     
6115 O  O     . HOH F .   ? 0.3484 0.2443 0.6304 0.0096  -0.043  -0.0351 911  HOH A O     
6116 O  O     . HOH F .   ? 0.0565 0.1227 0.5141 0.0347  0.0219  -0.0211 912  HOH A O     
6117 O  O     . HOH F .   ? 0.3256 0.3523 0.7886 0.0406  0.0258  -0.004  913  HOH A O     
6118 O  O     . HOH F .   ? 0.2119 0.2155 0.6199 0.0337  0.0136  -0.0279 914  HOH A O     
6119 O  O     . HOH F .   ? 0.0404 0.108  0.5043 -0.0056 -0.004  -0.0259 915  HOH A O     
6120 O  O     . HOH F .   ? 0.3271 0.2706 0.6485 0.0131  -0.0246 -0.0396 916  HOH A O     
6121 O  O     . HOH F .   ? 0.3411 0.4023 0.9717 0.016   0.0349  -0.021  917  HOH A O     
6122 O  O     . HOH F .   ? 0.1135 0.1772 0.5859 -0.0131 -0.008  -0.0136 918  HOH A O     
6123 O  O     . HOH F .   ? 0.2822 0.268  0.6637 -0.0166 -0.0402 -0.0247 919  HOH A O     
6124 O  O     . HOH F .   ? 0.2743 0.2828 0.6934 -0.0043 -0.0166 -0.0274 920  HOH A O     
6125 O  O     . HOH F .   ? 0.2119 0.2753 0.6991 -0.003  0.0066  -0.0305 921  HOH A O     
6126 O  O     . HOH F .   ? 0.2628 0.3049 0.7077 0.014   0.0067  -0.0534 922  HOH A O     
6127 O  O     . HOH F .   ? 0.2595 0.2964 0.7456 0.0323  0.0249  -0.0193 923  HOH A O     
6128 O  O     . HOH F .   ? 0.1474 0.2429 0.5978 0.0279  -0.0012 -0.086  924  HOH A O     
6129 O  O     . HOH F .   ? 0.2386 0.3058 0.8042 0.0298  0.0469  0.0054  925  HOH A O     
6130 O  O     . HOH F .   ? 0.2542 0.3446 0.7657 0.0112  -0.0064 -0.0641 926  HOH A O     
6131 O  O     . HOH F .   ? 0.2198 0.2214 0.629  0.0549  0.0245  -0.0086 927  HOH A O     
6132 O  O     . HOH F .   ? 0.2818 0.37   0.709  0.0119  -0.0024 -0.0467 928  HOH A O     
6133 O  O     . HOH F .   ? 0.0587 0.0835 0.4564 0.0228  0.0091  -0.0448 929  HOH A O     
6134 O  O     . HOH F .   ? 0.4528 0.5031 0.8952 0.0001  -0.0036 -0.0505 930  HOH A O     
6135 O  O     . HOH F .   ? 0.0953 0.1531 0.5082 0.0191  0.0071  -0.0564 931  HOH A O     
6136 O  O     . HOH F .   ? 0.3581 0.4132 0.8563 0.0043  0.0155  -0.0071 932  HOH A O     
6137 O  O     . HOH F .   ? 0.1923 0.2579 0.6377 0.0334  0.0204  -0.0264 933  HOH A O     
6138 O  O     . HOH F .   ? 0.1721 0.1681 0.5    0.0295  0.0076  -0.037  934  HOH A O     
6139 O  O     . HOH F .   ? 0.3544 0.395  0.7864 0.0104  0.0028  -0.0566 935  HOH A O     
6140 O  O     . HOH F .   ? 0.1369 0.1897 0.6658 0.0061  0.0097  -0.0662 936  HOH A O     
6141 O  O     . HOH F .   ? 0.1552 0.2052 0.7198 0.0065  0.0105  -0.0696 937  HOH A O     
6142 O  O     . HOH F .   ? 0.2036 0.2399 0.6147 -0.0086 -0.0206 -0.0285 938  HOH A O     
6143 O  O     . HOH F .   ? 0.2914 0.3917 0.7385 0.0405  -0.0127 -0.1155 939  HOH A O     
6144 O  O     . HOH F .   ? 0.1569 0.2048 0.5376 0.0183  0.0049  -0.0501 940  HOH A O     
6145 O  O     . HOH F .   ? 0.3976 0.4327 0.8408 -0.0298 -0.0406 -0.0005 941  HOH A O     
6146 O  O     . HOH F .   ? 0.1489 0.2026 0.7422 0.0029  0.0006  -0.0689 942  HOH A O     
6147 O  O     . HOH F .   ? 0.1113 0.2054 0.6072 0.0158  -0.0006 -0.0547 943  HOH A O     
6148 O  O     . HOH F .   ? 0.2892 0.3671 0.7428 0.01    0.0004  -0.06   944  HOH A O     
6149 O  O     . HOH F .   ? 0.237  0.2587 0.6736 -0.0287 -0.0421 -0.0019 945  HOH A O     
6150 O  O     . HOH F .   ? 0.4112 0.4001 0.8042 0.0322  0.0043  -0.0243 946  HOH A O     
6151 O  O     . HOH F .   ? 0.2767 0.3722 0.7142 0.0218  -0.0027 -0.0826 947  HOH A O     
6152 O  O     . HOH F .   ? 0.0574 0.1143 0.5793 0.0108  0.0078  -0.0779 948  HOH A O     
6153 O  O     . HOH F .   ? 0.3288 0.3018 0.6671 0.0053  -0.0215 -0.0202 949  HOH A O     
6154 O  O     . HOH F .   ? 0.1408 0.1399 0.5048 0.0461  0.0201  -0.0246 950  HOH A O     
6155 O  O     . HOH F .   ? 0.2245 0.2319 0.6475 -0.0287 -0.0488 -0.0039 951  HOH A O     
6156 O  O     . HOH F .   ? 0.202  0.2558 0.7352 0.0072  0.0073  -0.0603 952  HOH A O     
6157 O  O     . HOH F .   ? 0.2185 0.2847 0.794  0.0179  0.0426  -0.0095 953  HOH A O     
6158 O  O     . HOH F .   ? 0.376  0.4597 0.8233 0.0163  -0.0035 -0.0831 954  HOH A O     
6159 O  O     . HOH F .   ? 0.0737 0.1193 0.5284 0.0027  0.001   -0.0549 955  HOH A O     
6160 O  O     . HOH F .   ? 0.183  0.2041 0.6052 -0.0244 -0.0389 -0.012  956  HOH A O     
6161 O  O     . HOH F .   ? 0.3201 0.3658 0.7852 -0.0127 -0.0099 -0.0117 957  HOH A O     
6162 O  O     . HOH F .   ? 0.1026 0.1682 0.5683 -0.0043 -0.0023 -0.0331 958  HOH A O     
6163 O  O     . HOH F .   ? 0.2292 0.182  0.5425 0.0245  -0.0096 -0.0392 959  HOH A O     
6164 O  O     . HOH F .   ? 0.1878 0.2316 0.67   0.0351  0.0272  0.0062  960  HOH A O     
6165 O  O     . HOH F .   ? 0.1249 0.1721 0.7534 0.0027  0.0044  -0.0673 961  HOH A O     
6166 O  O     . HOH F .   ? 0.4535 0.4912 0.9015 0.0099  0.0049  -0.0536 962  HOH A O     
6167 O  O     . HOH F .   ? 0.125  0.1568 0.5319 0.0188  0.0071  -0.0491 963  HOH A O     
6168 O  O     . HOH F .   ? 0.1957 0.2054 0.6212 0.01    -0.0059 -0.0188 964  HOH A O     
6169 O  O     . HOH F .   ? 0.0401 0.0641 0.5063 0.0012  0.0081  -0.0532 965  HOH A O     
6170 O  O     . HOH F .   ? 0.2522 0.311  0.6436 0.0183  0.0051  -0.0544 966  HOH A O     
6171 O  O     . HOH F .   ? 0.1968 0.2062 0.6273 0.0283  0.0108  -0.0194 967  HOH A O     
6172 O  O     . HOH F .   ? 0.1367 0.1604 0.536  -0.0069 -0.0205 -0.0331 968  HOH A O     
6173 O  O     . HOH F .   ? 0.1091 0.0452 0.4155 0.0139  -0.0244 -0.0374 969  HOH A O     
6174 O  O     . HOH F .   ? 0.363  0.3027 0.6946 0.0026  -0.0385 -0.0365 970  HOH A O     
6175 O  O     . HOH F .   ? 0.4331 0.4916 1.0053 0.0122  0.0151  -0.0385 971  HOH A O     
6176 O  O     . HOH F .   ? 0.059  0.1216 0.4811 0.015   0.0031  -0.0632 972  HOH A O     
6177 O  O     . HOH F .   ? 0.1627 0.2125 0.6965 0.0388  0.0386  -0.0004 973  HOH A O     
6178 O  O     . HOH F .   ? 0.5008 0.595  0.9461 0.0053  -0.006  -0.0252 974  HOH A O     
6179 O  O     . HOH F .   ? 0.0429 0.0498 0.4371 -0.0026 -0.0217 -0.0302 975  HOH A O     
6180 O  O     . HOH F .   ? 0.1689 0.2321 0.6244 -0.0171 -0.021  -0.0087 976  HOH A O     
6181 O  O     . HOH F .   ? 0.2575 0.2485 0.6526 0.0438  0.0121  -0.017  977  HOH A O     
6182 O  O     . HOH F .   ? 0.1031 0.1532 0.7205 0.007   0.019   -0.0534 978  HOH A O     
6183 O  O     . HOH F .   ? 0.3212 0.3842 0.8635 0.0069  0.0273  -0.0346 979  HOH A O     
6184 O  O     . HOH F .   ? 0.2606 0.3211 0.671  0.0102  -0.0015 -0.0564 980  HOH A O     
6185 O  O     . HOH F .   ? 0.1369 0.1914 0.5912 -0.0277 -0.0376 0.0079  981  HOH A O     
6186 O  O     . HOH F .   ? 0.1844 0.3221 0.6098 0.0535  0.0042  -0.0773 982  HOH A O     
6187 O  O     . HOH F .   ? 0.2787 0.3477 0.7587 0.0067  0.0062  -0.0563 983  HOH A O     
6188 O  O     . HOH F .   ? 0.4719 0.451  0.8329 0.0578  0.0188  -0.0155 984  HOH A O     
6189 O  O     . HOH F .   ? 0.3835 0.4537 0.9077 0.0018  0.0235  -0.0143 985  HOH A O     
6190 O  O     . HOH F .   ? 0.0613 0.1167 0.5769 0.0041  0.0192  -0.0326 986  HOH A O     
6191 O  O     . HOH F .   ? 0.2459 0.2037 0.5838 0.0145  -0.0184 -0.0399 987  HOH A O     
6192 O  O     . HOH F .   ? 0.0548 0.1114 0.675  0.0044  0.0078  -0.0517 988  HOH A O     
6193 O  O     . HOH F .   ? 0.1161 0.123  0.5258 -0.0237 -0.0416 -0.0161 989  HOH A O     
6194 O  O     . HOH F .   ? 0.1512 0.2046 0.6953 0.0126  0.0148  -0.0735 990  HOH A O     
6195 O  O     . HOH F .   ? 0.1322 0.2427 0.5474 0.0268  0.0027  -0.0652 991  HOH A O     
6196 O  O     . HOH F .   ? 0.3518 0.4379 0.8467 0.0112  -0.0149 -0.093  992  HOH A O     
6197 O  O     . HOH F .   ? 0.3305 0.3352 0.748  0.0046  -0.0118 -0.023  993  HOH A O     
6198 O  O     . HOH F .   ? 0.2853 0.3778 0.7601 0.0166  -0.0153 -0.1003 994  HOH A O     
6199 O  O     . HOH F .   ? 0.1864 0.2327 0.6343 -0.0252 -0.0329 -0.0032 995  HOH A O     
6200 O  O     . HOH F .   ? 0.154  0.1529 0.5002 0.0412  0.017   -0.031  996  HOH A O     
6201 O  O     . HOH F .   ? 0.2479 0.3348 0.6741 0.0158  -0.0006 -0.0635 997  HOH A O     
6202 O  O     . HOH F .   ? 0.4878 0.4323 0.7783 0.0467  0.0052  -0.0318 998  HOH A O     
6203 O  O     . HOH F .   ? 0.3617 0.4442 0.7932 0.0114  -0.0019 -0.0551 999  HOH A O     
6204 O  O     . HOH F .   ? 0.1327 0.0793 0.4804 -0.0126 -0.0497 -0.0297 1000 HOH A O     
6205 O  O     . HOH F .   ? 0.2284 0.2704 0.7007 0.0092  0.0074  -0.0534 1001 HOH A O     
6206 O  O     . HOH F .   ? 0.4074 0.5613 0.8049 0.0462  0.0125  -0.0608 1002 HOH A O     
6207 O  O     . HOH F .   ? 0.2598 0.2268 0.5843 0.0657  0.0219  -0.0149 1003 HOH A O     
6208 O  O     . HOH F .   ? 0.2571 0.2547 0.6639 -0.0278 -0.0495 -0.0124 1004 HOH A O     
6209 O  O     . HOH F .   ? 0.5191 0.5669 0.9342 0.0364  0.0217  -0.0281 1005 HOH A O     
6210 O  O     . HOH F .   ? 0.2441 0.3488 0.6983 0.0059  -0.006  -0.014  1006 HOH A O     
6211 O  O     . HOH F .   ? 0.381  0.4442 1.0301 0.0135  0.0271  -0.0218 1007 HOH A O     
6212 O  O     . HOH F .   ? 0.1265 0.1608 0.589  0.0101  0.0081  -0.0469 1008 HOH A O     
6213 O  O     . HOH F .   ? 0.257  0.3047 0.7109 -0.0296 -0.0377 0.0046  1009 HOH A O     
6214 O  O     . HOH F .   ? 0.1803 0.2351 0.7628 0.0095  0.0284  -0.0449 1010 HOH A O     
6215 O  O     . HOH F .   ? 0.0967 0.1265 0.5288 0.0029  -0.0022 -0.0485 1011 HOH A O     
6216 O  O     . HOH F .   ? 0.2131 0.2569 0.6572 -0.0031 -0.0052 -0.0439 1012 HOH A O     
6217 O  O     . HOH F .   ? 0.2581 0.3015 0.7031 -0.0006 -0.0028 -0.0487 1013 HOH A O     
6218 O  O     . HOH F .   ? 0.4204 0.4556 0.8866 0.0146  0.011   -0.0443 1014 HOH A O     
6219 O  O     . HOH F .   ? 0.351  0.4116 0.9017 0.008   0.028   -0.0384 1015 HOH A O     
6220 O  O     . HOH F .   ? 0.146  0.1967 0.762  0.0086  0.0245  -0.0498 1016 HOH A O     
6221 O  O     . HOH F .   ? 0.3837 0.4541 0.7779 0.0141  -0.0003 -0.0408 1017 HOH A O     
6222 O  O     . HOH F .   ? 0.195  0.3026 0.6779 0.0169  -0.005  -0.0644 1018 HOH A O     
6223 O  O     . HOH F .   ? 0.2368 0.2661 0.6013 0.0371  0.0198  -0.0341 1019 HOH A O     
6224 O  O     . HOH F .   ? 0.2599 0.3044 0.7046 0.0088  0.0028  -0.0588 1020 HOH A O     
6225 O  O     . HOH F .   ? 0.3218 0.3683 0.6865 0.0283  0.0138  -0.0436 1021 HOH A O     
6226 O  O     . HOH F .   ? 0.1233 0.2097 0.5839 0.0133  0.0031  -0.0551 1022 HOH A O     
6227 O  O     . HOH F .   ? 0.0407 0.0798 0.5366 0.0033  0.0104  -0.0576 1023 HOH A O     
6228 O  O     . HOH F .   ? 0.2954 0.3592 0.7717 -0.0041 0.0019  -0.0319 1024 HOH A O     
6229 O  O     . HOH F .   ? 0.2834 0.2214 0.5845 0.0179  -0.0192 -0.0362 1025 HOH A O     
6230 O  O     . HOH F .   ? 0.5501 0.5962 0.9077 0.0253  0.0105  -0.04   1026 HOH A O     
6231 O  O     . HOH F .   ? 0.1509 0.1536 0.5638 -0.0032 -0.0194 -0.0248 1027 HOH A O     
6232 O  O     . HOH F .   ? 0.0648 0.1276 0.6859 0.0197  0.0372  -0.0145 1028 HOH A O     
6233 O  O     . HOH F .   ? 0.234  0.28   0.6702 0.0054  -0.0007 -0.0582 1029 HOH A O     
6234 O  O     . HOH F .   ? 0.5032 0.4582 0.8193 0.0601  0.0134  -0.0213 1030 HOH A O     
6235 O  O     . HOH F .   ? 0.1955 0.2574 0.664  -0.0193 -0.0173 -0.0044 1031 HOH A O     
6236 O  O     . HOH F .   ? 0.3271 0.3968 0.9415 0.0267  0.032   -0.0017 1032 HOH A O     
6237 O  O     . HOH F .   ? 0.2522 0.1842 0.5986 -0.0215 -0.0656 -0.0235 1033 HOH A O     
6238 O  O     . HOH F .   ? 0.4512 0.5323 0.8237 0.0296  0.0147  -0.0448 1034 HOH A O     
6239 O  O     . HOH F .   ? 0.3626 0.2925 0.684  0.0028  -0.0419 -0.0368 1035 HOH A O     
6240 O  O     . HOH F .   ? 0.1477 0.2055 0.7535 0.0135  0.0331  -0.0292 1036 HOH A O     
6241 O  O     . HOH F .   ? 0.1606 0.244  0.6187 0.0174  0.0008  -0.0742 1037 HOH A O     
6242 O  O     . HOH F .   ? 0.3223 0.3789 0.8312 0.0396  0.0379  0.0136  1038 HOH A O     
6243 O  O     . HOH F .   ? 0.1869 0.2401 0.7326 0.0083  0.011   -0.0534 1039 HOH A O     
6244 O  O     . HOH F .   ? 0.0586 0.1118 0.6109 0.0102  0.0146  -0.0464 1040 HOH A O     
6245 O  O     . HOH F .   ? 0.3516 0.4056 0.798  0.0138  0.0049  -0.0594 1041 HOH A O     
6246 O  O     . HOH F .   ? 0.3689 0.3042 0.6505 0.0628  0.0107  -0.0241 1042 HOH A O     
6247 O  O     . HOH F .   ? 0.3053 0.2359 0.6393 -0.0112 -0.0553 -0.0308 1043 HOH A O     
6248 O  O     . HOH F .   ? 0.204  0.3197 0.641  0.025   0.0016  -0.0686 1044 HOH A O     
6249 O  O     . HOH F .   ? 0.3604 0.3885 0.7315 0.0397  0.0216  -0.0304 1045 HOH A O     
6250 O  O     . HOH F .   ? 0.0478 0.0593 0.4259 0.0103  0.0094  -0.0393 1046 HOH A O     
6251 O  O     . HOH F .   ? 0.4358 0.5027 1.0646 0.0214  0.0465  -0.0085 1047 HOH A O     
6252 O  O     . HOH F .   ? 0.1033 0.0681 0.4577 -0.0095 -0.0394 -0.0182 1048 HOH A O     
6253 O  O     . HOH F .   ? 0.3489 0.3796 0.7502 -0.0058 -0.0192 -0.0317 1049 HOH A O     
6254 O  O     . HOH F .   ? 0.3675 0.4601 0.7902 0.0178  0       -0.0606 1050 HOH A O     
6255 O  O     . HOH F .   ? 0.3511 0.4083 0.8152 0.0056  0.0014  -0.0655 1051 HOH A O     
6256 O  O     . HOH F .   ? 0.3458 0.4463 0.7877 0.0278  0.012   -0.044  1052 HOH A O     
6257 O  O     . HOH F .   ? 0.2658 0.3299 0.6925 -0.0018 -0.0118 -0.0322 1053 HOH A O     
6258 O  O     . HOH F .   ? 0.3212 0.4369 0.7309 0.0293  0.0045  -0.0639 1054 HOH A O     
6259 O  O     . HOH F .   ? 0.3197 0.3001 0.6322 0.0307  0.0053  -0.0343 1055 HOH A O     
6260 O  O     . HOH F .   ? 0.1297 0.1235 0.5297 0.0142  -0.0058 -0.0318 1056 HOH A O     
6261 O  O     . HOH F .   ? 0.2393 0.2724 0.7227 0.0451  0.033   -0.0028 1057 HOH A O     
6262 O  O     . HOH F .   ? 0.4148 0.4749 0.8574 0.0061  -0.0012 -0.0623 1058 HOH A O     
6263 O  O     . HOH F .   ? 0.138  0.0966 0.5081 -0.0236 -0.0585 -0.0209 1059 HOH A O     
6264 O  O     . HOH F .   ? 0.3214 0.3882 0.7606 -0.0099 -0.0196 -0.0137 1060 HOH A O     
6265 O  O     . HOH F .   ? 0.1037 0.1715 0.6084 -0.0028 0.0135  -0.0178 1061 HOH A O     
6266 O  O     . HOH F .   ? 0.0874 0.0854 0.4926 -0.0066 -0.0244 -0.0269 1062 HOH A O     
6267 O  O     . HOH F .   ? 0.4958 0.5306 0.8888 -0.0017 -0.0171 -0.0259 1063 HOH A O     
6268 O  O     . HOH F .   ? 0.2832 0.2921 0.7072 0.0163  -0.0027 -0.0155 1064 HOH A O     
6269 O  O     . HOH F .   ? 0.4497 0.4036 0.7955 0.004   -0.0315 -0.0365 1065 HOH A O     
6270 O  O     . HOH F .   ? 0.2084 0.2572 0.6823 -0.008  -0.0017 -0.0154 1066 HOH A O     
6271 O  O     . HOH F .   ? 0.3225 0.3846 0.7798 0.0194  0.0091  -0.0497 1067 HOH A O     
6272 O  O     . HOH F .   ? 0.2599 0.2995 0.7388 0.0299  0.0235  -0.0001 1068 HOH A O     
6273 O  O     . HOH F .   ? 0.3108 0.3421 0.7481 0.0219  0.0121  -0.0413 1069 HOH A O     
6274 O  O     . HOH F .   ? 0.3242 0.4782 0.8113 0.0208  -0.0296 -0.091  1070 HOH A O     
6275 O  O     . HOH F .   ? 0.1923 0.2968 0.6927 0.0119  -0.017  -0.0833 1071 HOH A O     
6276 O  O     . HOH F .   ? 0.2511 0.2831 0.7307 0.0471  0.0335  -0.0005 1072 HOH A O     
6277 O  O     . HOH F .   ? 0.4728 0.6204 0.9229 0.0403  0.01    -0.0244 1073 HOH A O     
6278 O  O     . HOH F .   ? 0.4154 0.4649 0.8566 0.0069  0.0004  -0.0614 1074 HOH A O     
6279 O  O     . HOH F .   ? 0.2319 0.3147 0.6988 0.0242  -0.0002 -0.088  1075 HOH A O     
6280 O  O     . HOH F .   ? 0.2303 0.2809 0.7252 0.0189  0.0225  0.0003  1076 HOH A O     
6281 O  O     . HOH F .   ? 0.1875 0.2633 0.6488 -0.0181 -0.0253 0.0051  1077 HOH A O     
6282 O  O     . HOH F .   ? 0.2923 0.2565 0.6536 0.0006  -0.0315 -0.0338 1078 HOH A O     
6283 O  O     . HOH F .   ? 0.1521 0.212  0.7314 0.0295  0.0401  -0.0044 1079 HOH A O     
6284 O  O     . HOH F .   ? 0.2257 0.3596 0.6337 0.037   0.0075  -0.0582 1080 HOH A O     
6285 O  O     . HOH F .   ? 0.1652 0.2226 0.7518 0.0107  0.0329  -0.0377 1081 HOH A O     
6286 O  O     . HOH F .   ? 0.5418 0.4303 0.8323 -0.0001 -0.0534 -0.0274 1082 HOH A O     
6287 O  O     . HOH F .   ? 0.5454 0.555  0.9715 0.0469  0.019   -0.005  1083 HOH A O     
6288 O  O     . HOH F .   ? 0.4478 0.6372 0.8516 0.0876  0.0126  -0.0681 1084 HOH A O     
6289 O  O     . HOH F .   ? 0.3395 0.4918 0.8358 0.0193  -0.0412 -0.1041 1085 HOH A O     
6290 O  O     . HOH F .   ? 0.3248 0.458  0.7441 0.0612  -0.0045 -0.1042 1086 HOH A O     
6291 O  O     . HOH F .   ? 0.4425 0.4905 0.8862 0.0035  -0.0009 -0.0571 1087 HOH A O     
6292 O  O     . HOH F .   ? 0.2274 0.2904 0.8385 0.0202  0.0409  -0.0135 1088 HOH A O     
6293 O  O     . HOH F .   ? 0.245  0.2836 0.6904 0.0018  -0.0006 -0.0505 1089 HOH A O     
6294 O  O     . HOH F .   ? 0.2066 0.2427 0.6541 -0.0321 -0.0426 0.0035  1090 HOH A O     
6295 O  O     . HOH F .   ? 0.3375 0.4376 0.7464 0.0385  0.0238  -0.0306 1091 HOH A O     
6296 O  O     . HOH F .   ? 0.1407 0.2291 0.6114 0.017   0.001   -0.0613 1092 HOH A O     
6297 O  O     . HOH F .   ? 0.3626 0.4137 0.8993 0.0384  0.0362  -0.002  1093 HOH A O     
6298 O  O     . HOH F .   ? 0.0438 0.0973 0.6698 0.0097  0.0278  -0.0415 1094 HOH A O     
6299 O  O     . HOH F .   ? 0.2068 0.2747 0.6784 -0.0015 0.0014  -0.037  1095 HOH A O     
6300 O  O     . HOH F .   ? 0.2141 0.2301 0.6311 0.0225  0.0095  -0.0393 1096 HOH A O     
6301 O  O     . HOH F .   ? 0.6274 0.6383 0.9789 0.0457  0.023   -0.0261 1097 HOH A O     
6302 O  O     . HOH F .   ? 0.202  0.2497 0.7947 0.0037  -0.0001 -0.0791 1098 HOH A O     
6303 O  O     . HOH F .   ? 0.2628 0.4454 0.6518 0.0906  -0.0029 -0.1066 1099 HOH A O     
6304 O  O     . HOH F .   ? 0.215  0.2733 0.8667 0.005   0.0117  -0.0417 1100 HOH A O     
6305 O  O     . HOH F .   ? 0.2755 0.3522 0.7394 0.0149  -0.0027 -0.0847 1101 HOH A O     
6306 O  O     . HOH F .   ? 0.3799 0.4478 0.8829 0.0012  0.014   -0.0328 1102 HOH A O     
6307 O  O     . HOH F .   ? 0.0428 0.101  0.589  0.0076  0.0246  -0.0447 1103 HOH A O     
6308 O  O     . HOH F .   ? 0.0413 0.0946 0.5604 0.0058  0.0106  -0.063  1104 HOH A O     
6309 O  O     . HOH F .   ? 0.4909 0.5364 1.1597 0.0007  0.0035  -0.0613 1105 HOH A O     
6310 O  O     . HOH F .   ? 0.0857 0.1316 0.5643 0.0034  0.0072  -0.0064 1106 HOH A O     
6311 O  O     . HOH F .   ? 0.3429 0.4219 0.7973 0.0139  -0.0034 -0.0808 1107 HOH A O     
6312 O  O     . HOH F .   ? 0.2196 0.2948 0.6848 -0.0052 -0.0052 -0.0241 1108 HOH A O     
6313 O  O     . HOH F .   ? 0.3285 0.2266 0.6239 0.0011  -0.0554 -0.0363 1109 HOH A O     
6314 O  O     . HOH F .   ? 0.3327 0.4199 0.8034 0.0256  -0.0177 -0.1158 1110 HOH A O     
6315 O  O     . HOH F .   ? 0.4969 0.5683 1.0939 0.0317  0.0523  0.0076  1111 HOH A O     
6316 O  O     . HOH F .   ? 0.2613 0.355  0.7147 0.0369  -0.0084 -0.1083 1112 HOH A O     
6317 O  O     . HOH F .   ? 0.3822 0.3325 0.7079 0.0246  -0.0132 -0.0385 1113 HOH A O     
6318 O  O     . HOH F .   ? 0.1347 0.1909 0.6004 -0.0245 -0.025  0.0018  1114 HOH A O     
6319 O  O     . HOH F .   ? 0.4261 0.4155 0.8213 0.0187  -0.0062 -0.0271 1115 HOH A O     
6320 O  O     . HOH F .   ? 0.2398 0.2538 0.6496 -0.0213 -0.0385 -0.0153 1116 HOH A O     
6321 O  O     . HOH F .   ? 0.3218 0.3243 0.6743 0.0454  0.0208  -0.0266 1117 HOH A O     
6322 O  O     . HOH F .   ? 0.2922 0.3785 0.7833 -0.0109 -0.002  0       1118 HOH A O     
6323 O  O     . HOH F .   ? 0.041  0.0746 0.4462 -0.0041 -0.016  -0.0273 1119 HOH A O     
6324 O  O     . HOH F .   ? 0.2737 0.3643 0.7117 0.0332  0.0191  -0.0302 1120 HOH A O     
6325 O  O     . HOH F .   ? 0.4487 0.6202 0.8581 0.0631  -0.0246 -0.1273 1121 HOH A O     
6326 O  O     . HOH F .   ? 0.3223 0.3581 0.7921 0.0473  0.0304  0.0079  1122 HOH A O     
6327 O  O     . HOH F .   ? 0.3258 0.3726 0.9525 0.0051  0.0128  -0.0617 1123 HOH A O     
6328 O  O     . HOH F .   ? 0.2289 0.2936 0.8654 0.017   0.0296  -0.0163 1124 HOH A O     
6329 O  O     . HOH F .   ? 0.5019 0.5556 0.9209 0.0039  -0.0054 -0.0512 1125 HOH A O     
6330 O  O     . HOH F .   ? 0.3503 0.4193 0.9768 0.0281  0.0396  0.0013  1126 HOH A O     
6331 O  O     . HOH F .   ? 0.2296 0.158  0.5289 0.0175  -0.0246 -0.0387 1127 HOH A O     
6332 O  O     . HOH F .   ? 0.1224 0.1894 0.7544 0.0112  0.016   -0.0261 1128 HOH A O     
6333 O  O     . HOH F .   ? 0.46   0.6122 0.8962 0.0358  0.0083  -0.0138 1129 HOH A O     
6334 O  O     . HOH F .   ? 0.3447 0.4624 0.7954 0.0374  0.0083  -0.0567 1130 HOH A O     
6335 O  O     . HOH F .   ? 0.2233 0.2908 0.8111 0.0396  0.0508  0.0121  1131 HOH A O     
6336 O  O     . HOH F .   ? 0.1606 0.1097 0.5003 -0.0062 -0.0406 -0.0317 1132 HOH A O     
6337 O  O     . HOH F .   ? 0.4157 0.4625 1.1033 0.0011  0.0073  -0.0534 1133 HOH A O     
6338 O  O     . HOH F .   ? 0.3832 0.4274 0.8235 0.012   0.0045  -0.057  1134 HOH A O     
6339 O  O     . HOH F .   ? 0.3242 0.3872 0.8494 0.0356  0.0409  0.0135  1135 HOH A O     
6340 O  O     . HOH F .   ? 0.4506 0.5603 0.9113 0.0279  0.0086  -0.0477 1136 HOH A O     
6341 O  O     . HOH F .   ? 0.4727 0.4377 0.829  0.0242  -0.0118 -0.0323 1137 HOH A O     
6342 O  O     . HOH F .   ? 0.2794 0.4075 0.7143 0.0531  0.0063  -0.0751 1138 HOH A O     
6343 O  O     . HOH F .   ? 0.2504 0.3094 0.679  0.0046  -0.0038 -0.0546 1139 HOH A O     
6344 O  O     . HOH F .   ? 0.3226 0.3878 0.9377 0.0178  0.045   -0.0152 1140 HOH A O     
6345 O  O     . HOH F .   ? 0.083  0.1799 0.5599 0.0165  -0.0024 -0.0645 1141 HOH A O     
6346 O  O     . HOH F .   ? 0.1282 0.2091 0.6028 0.0127  -0.0043 -0.0761 1142 HOH A O     
6347 O  O     . HOH F .   ? 0.3605 0.5048 0.7737 0.0609  -0.0065 -0.1059 1143 HOH A O     
6348 O  O     . HOH F .   ? 0.3844 0.4424 0.9455 0.0381  0.0391  0.0025  1144 HOH A O     
6349 O  O     . HOH F .   ? 0.2185 0.3128 0.6875 0.0254  0.0088  -0.0609 1145 HOH A O     
6350 O  O     . HOH F .   ? 0.5786 0.6565 1.0342 0.0137  -0.0024 -0.0774 1146 HOH A O     
6351 O  O     . HOH F .   ? 0.3145 0.2742 0.663  0.0183  -0.0172 -0.0359 1147 HOH A O     
6352 O  O     . HOH F .   ? 0.3261 0.2881 0.6543 0.0457  0.0072  -0.0294 1148 HOH A O     
6353 O  O     . HOH F .   ? 0.5224 0.6855 0.9322 0.0607  -0.0179 -0.12   1149 HOH A O     
6354 O  O     . HOH F .   ? 0.4035 0.5371 0.8826 0.0068  -0.0071 0.0211  1150 HOH A O     
6355 O  O     . HOH F .   ? 0.3795 0.5371 0.8026 0.0434  0.0117  -0.0281 1151 HOH A O     
6356 O  O     . HOH F .   ? 0.3015 0.355  0.8317 0.0128  0.0029  -0.0895 1152 HOH A O     
6357 O  O     . HOH F .   ? 0.2363 0.2956 0.7161 0.0246  0.0154  -0.0338 1153 HOH A O     
6358 O  O     . HOH F .   ? 0.3595 0.4162 0.9201 0.0113  0.0259  -0.0547 1154 HOH A O     
6359 O  O     . HOH F .   ? 0.3084 0.2918 0.6698 -0.0056 -0.0308 -0.0183 1155 HOH A O     
6360 O  O     . HOH F .   ? 0.3803 0.4497 0.8672 -0.0016 0.0068  -0.0314 1156 HOH A O     
6361 O  O     . HOH F .   ? 0.1104 0.21   0.5891 -0.0022 -0.0031 -0.0052 1157 HOH A O     
6362 O  O     . HOH F .   ? 0.1762 0.2321 0.7433 0.0042  0.001   -0.0695 1158 HOH A O     
6363 O  O     . HOH F .   ? 0.1087 0.1769 0.7532 0.0211  0.0347  -0.007  1159 HOH A O     
6364 O  O     . HOH F .   ? 0.4106 0.3806 0.788  -0.0147 -0.0471 -0.0235 1160 HOH A O     
6365 O  O     . HOH F .   ? 0.2814 0.332  0.7466 -0.023  -0.023  0.0014  1161 HOH A O     
6366 O  O     . HOH F .   ? 0.3152 0.3847 0.9537 0.025   0.0479  -0.0016 1162 HOH A O     
6367 O  O     . HOH F .   ? 0.2939 0.376  0.7507 0.0156  -0.0052 -0.0874 1163 HOH A O     
6368 O  O     . HOH F .   ? 0.1801 0.166  0.5419 -0.005  -0.0291 -0.0244 1164 HOH A O     
6369 O  O     . HOH F .   ? 0.3066 0.3723 0.7315 0.0028  -0.0072 -0.043  1165 HOH A O     
6370 O  O     . HOH F .   ? 0.4032 0.3756 0.7765 0.0057  -0.0267 -0.0283 1166 HOH A O     
6371 O  O     . HOH F .   ? 0.2961 0.4367 0.789  0.0177  -0.0189 -0.0747 1167 HOH A O     
6372 O  O     . HOH F .   ? 0.2472 0.3101 0.6733 0.0339  0.0204  -0.0303 1168 HOH A O     
6373 O  O     . HOH F .   ? 0.2153 0.2906 0.6934 -0.0184 -0.0148 0.0022  1169 HOH A O     
6374 O  O     . HOH F .   ? 0.3058 0.3546 0.9203 0.0049  0.0114  -0.0617 1170 HOH A O     
6375 O  O     . HOH F .   ? 0.1433 0.2039 0.7546 0.0061  0.0083  -0.0461 1171 HOH A O     
6376 O  O     . HOH F .   ? 0.3985 0.4261 0.7439 0.0312  0.0145  -0.0383 1172 HOH A O     
6377 O  O     . HOH F .   ? 0.4345 0.4569 0.8277 -0.0078 -0.0252 -0.0197 1173 HOH A O     
6378 O  O     . HOH F .   ? 0.2475 0.2213 0.5568 0.0387  0.0096  -0.0335 1174 HOH A O     
6379 O  O     . HOH F .   ? 0.3226 0.4178 0.791  -0.008  -0.014  0.0019  1175 HOH A O     
6380 O  O     . HOH F .   ? 0.5624 0.4761 0.8611 0.0119  -0.0394 -0.0389 1176 HOH A O     
6381 O  O     . HOH F .   ? 0.2668 0.4189 0.6764 0.062   -0.0088 -0.1093 1177 HOH A O     
6382 O  O     . HOH F .   ? 0.364  0.2802 0.6524 0.017   -0.0286 -0.0372 1178 HOH A O     
6383 O  O     . HOH F .   ? 0.2887 0.2623 0.6022 0.0385  0.0091  -0.034  1179 HOH A O     
6384 O  O     . HOH F .   ? 0.5966 0.5599 0.9052 0.0214  -0.0073 -0.0291 1180 HOH A O     
6385 O  O     . HOH F .   ? 0.1218 0.1717 0.6968 0.0067  0.014   -0.0642 1181 HOH A O     
6386 O  O     . HOH F .   ? 0.3003 0.3486 0.8965 0.0049  0.0082  -0.0688 1182 HOH A O     
6387 O  O     . HOH F .   ? 0.3643 0.3906 0.8253 0.0393  0.0258  -0.015  1183 HOH A O     
6388 O  O     . HOH F .   ? 0.3345 0.4013 0.9635 0.0245  0.0411  -0.0046 1184 HOH A O     
6389 O  O     . HOH F .   ? 0.3619 0.3463 0.7489 0.017   -0.0092 -0.0297 1185 HOH A O     
6390 O  O     . HOH F .   ? 0.174  0.2424 0.7675 0.0276  0.0292  -0.0039 1186 HOH A O     
6391 O  O     . HOH F .   ? 0.4291 0.446  0.8611 0.0059  -0.01   -0.0099 1187 HOH A O     
6392 O  O     . HOH F .   ? 0.3409 0.4118 0.816  0.0049  0.0049  -0.0499 1188 HOH A O     
6393 O  O     . HOH F .   ? 0.3997 0.3529 0.7092 0.0688  0.0182  -0.0159 1189 HOH A O     
6394 O  O     . HOH F .   ? 0.2661 0.3349 0.8733 0.0244  0.0284  -0.0066 1190 HOH A O     
6395 O  O     . HOH F .   ? 0.4386 0.4485 0.7753 0.0312  0.0118  -0.0375 1191 HOH A O     
6396 O  O     . HOH F .   ? 0.1974 0.2848 0.6654 0.0216  0.0076  -0.0471 1192 HOH A O     
6397 O  O     . HOH F .   ? 0.3377 0.3676 0.7781 -0.0327 -0.0464 0.0025  1193 HOH A O     
6398 O  O     . HOH F .   ? 1.5244 1.6915 1.9223 0.0881  0.0014  -0.0988 1194 HOH A O     
6399 O  O     . HOH F .   ? 0.3732 0.3543 0.7519 0.0407  0.0057  -0.0212 1195 HOH A O     
6400 O  O     . HOH G .   ? 0.5667 0.6086 1.0313 0.0116  0.0075  -0.0527 101  HOH E O     
6401 O  O     . HOH G .   ? 0.2915 0.3502 0.8219 0.0186  0.0169  -0.0737 102  HOH E O     
6402 O  O     . HOH G .   ? 0.0674 0.1265 0.5836 0.01    0.0104  -0.0708 103  HOH E O     
6403 O  O     . HOH G .   ? 0.4982 0.5426 0.9884 0.017   0.014   -0.0416 104  HOH E O     
6404 O  O     . HOH G .   ? 0.2032 0.2631 0.7457 0.0049  -0.0035 -0.0766 105  HOH E O     
6405 O  O     . HOH G .   ? 0.1324 0.1885 0.6888 0.0093  0.0109  -0.0492 106  HOH E O     
6406 O  O     . HOH G .   ? 0.4792 0.545  0.9689 0.0119  -0.001  -0.0859 107  HOH E O     
6407 O  O     . HOH G .   ? 0.441  0.5013 0.9617 0.0106  0.0058  -0.0546 108  HOH E O     
6408 O  O     . HOH G .   ? 0.1626 0.2247 0.677  0.0087  0.0143  -0.0596 109  HOH E O     
6409 O  O     . HOH G .   ? 0.3339 0.3825 0.8241 0.015   0.0111  -0.0469 110  HOH E O     
6410 O  O     . HOH G .   ? 0.1276 0.1838 0.659  0.0059  0.0023  -0.0704 111  HOH E O     
6411 O  O     . HOH G .   ? 0.2588 0.3101 0.8021 0.0152  0.0118  -0.0817 112  HOH E O     
6412 O  O     . HOH G .   ? 0.5234 0.565  0.999  0.0124  0.0097  -0.0494 113  HOH E O     
6413 O  O     . HOH G .   ? 0.1753 0.2353 0.7098 0.007   0.0219  -0.0466 114  HOH E O     
6414 O  O     . HOH G .   ? 0.3841 0.4313 0.8556 0.0065  0.0046  -0.0597 115  HOH E O     
6415 O  O     . HOH G .   ? 0.3343 0.3832 0.8748 0.016   0.0043  -0.0931 116  HOH E O     
6416 O  O     . HOH G .   ? 0.3066 0.3812 0.7915 0.0182  0.0069  -0.074  117  HOH E O     
6417 O  O     . HOH G .   ? 0.315  0.3762 0.7982 0.0084  0       -0.0729 118  HOH E O     
6418 O  O     . HOH G .   ? 0.4139 0.4931 0.8693 0.0147  -0.0008 -0.0765 119  HOH E O     
6419 O  O     . HOH G .   ? 0.3465 0.4028 0.8878 0.0062  0.004   -0.0646 120  HOH E O     
6420 O  O     . HOH H .   ? 0.3676 0.4449 0.8441 0.0052  0.0055  -0.043  101  HOH F O     
6421 O  O     . HOH H .   ? 0.5087 0.5825 1.0032 0.0096  -0.0052 -0.0769 102  HOH F O     
6422 O  O     . HOH H .   ? 0.4512 0.529  0.9433 0.0101  -0.009  -0.0854 103  HOH F O     
6423 O  O     . HOH H .   ? 0.4139 0.4902 0.911  0.0124  -0.0153 -0.102  104  HOH F O     
6424 O  O     . HOH H .   ? 0.0409 0.0805 0.5443 0.0035  0.0129  -0.0539 105  HOH F O     
6425 O  O     . HOH H .   ? 0.3756 0.4363 0.8762 0.0102  0.0034  -0.0613 106  HOH F O     
6426 O  O     . HOH H .   ? 0.1937 0.2439 0.7505 0.0077  0.0096  -0.0743 107  HOH F O     
6427 O  O     . HOH H .   ? 0.2735 0.3317 0.8094 0.0064  -0.0071 -0.09   108  HOH F O     
6428 O  O     . HOH H .   ? 0.2951 0.3693 0.7888 0.005   0.0116  -0.0404 109  HOH F O     
6429 O  O     . HOH H .   ? 0.0402 0.0711 0.5159 0.0017  0.0088  -0.0555 110  HOH F O     
6430 O  O     . HOH H .   ? 0.3771 0.4428 0.8651 0.0087  -0.0032 -0.0806 111  HOH F O     
6431 O  O     . HOH H .   ? 0.1328 0.1932 0.6192 0.005   0.0066  -0.0597 112  HOH F O     
6432 O  O     . HOH H .   ? 0.0717 0.1347 0.5451 -0.0025 0.0019  -0.037  113  HOH F O     
6433 O  O     . HOH H .   ? 0.1225 0.1856 0.6267 0.0063  0.0127  -0.0543 114  HOH F O     
6434 O  O     . HOH H .   ? 0.0397 0.0724 0.4855 -0.0005 0.0018  -0.0461 115  HOH F O     
6435 O  O     . HOH H .   ? 0.0911 0.1499 0.6046 0.011   0.0057  -0.0796 116  HOH F O     
6436 O  O     . HOH H .   ? 0.1058 0.1724 0.6015 0.0048  0.0112  -0.048  117  HOH F O     
6437 O  O     . HOH H .   ? 0.041  0.0938 0.5459 0.0058  0.0048  -0.0696 118  HOH F O     
6438 O  O     . HOH H .   ? 0.3717 0.4459 0.8326 0.0123  -0.0026 -0.0778 119  HOH F O     
6439 O  O     . HOH H .   ? 0.2544 0.3113 0.7815 0.0061  -0.0004 -0.079  120  HOH F O     
6440 O  O     . HOH H .   ? 0.3594 0.4239 0.892  0.0055  -0.009  -0.0852 121  HOH F O     
6441 O  O     . HOH H .   ? 0.3465 0.4147 0.8689 0.0068  -0.0118 -0.0907 122  HOH F O     
6442 O  O     . HOH H .   ? 0.3906 0.464  0.8964 0.0107  -0.0009 -0.0631 123  HOH F O     
6443 O  O     . HOH H .   ? 0.1395 0.1983 0.6596 0.0087  0.0135  -0.064  124  HOH F O     
# 
