data_9EZD
# 
_entry.id   9EZD 
# 
_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   9EZD         pdb_00009ezd 10.2210/pdb9ezd/pdb 
WWPDB D_1292137871 ?            ?                   
# 
_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                        9EZD 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'BsmI (Inactive mutant)'    9EZ5 unspecified 
PDB 'BsmI (Top nicking mutant)' 9EZ7 unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              marc.delarue@pasteur.fr 
_pdbx_contact_author.name_first         Marc 
_pdbx_contact_author.name_last          DELARUE 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0723-8102 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Sieskind, R.' 1  0000-0002-6511-6069 
'Missoury, S.' 2  0000-0001-7478-6956 
'Madru, C.'    3  0000-0002-5412-8822 
'Commenge, I.' 4  ?                   
'Niogret, G.'  5  0009-0002-6185-0183 
'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                                   78190.234 1  ? 'R507D, G509V, E546V' ? ? 
2 polymer     syn 
;DNA (Bottom strand - 5'-part)
;
2337.555  1  ? ?                     ? ? 
3 polymer     syn 'DNA (Top strand)'                     4049.661  1  ? ?                     ? ? 
4 polymer     syn 
;DNA (Bottom strand - 3'-part)
;
1511.022  1  ? ?                     ? ? 
5 non-polymer syn 'MAGNESIUM ION'                        24.305    1  ? ?                     ? ? 
6 non-polymer syn 'CHLORIDE ION'                         35.453    1  ? ?                     ? ? 
7 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' 195.237   1  ? ?                     ? ? 
8 water       nat water                                  18.015    51 ? ?                     ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)'        no no 
;MNVFRIHGDNIIECERVIDLILSKINPQKVKRGFISLSCPFIEIIFKEGHDYFHWRFDMFPGFNKNTNDRWNSNILDLLS
QKGSFLYETPDVIITSLNNGKEEILMAIEFCSALQAGNQAWQRSGRAYSVGRTGYPYIYIVDFVKYELNNSDRSRKNLRF
PNPAIPYSYISHSKNTGNFIVQAYFRGEEYQPKYDKKLKFFDETIFAEDDIADYIIAKLQHRDTSNIEQLLINKNLKMVE
FLSKNTKNDNNFTYSEWESIYNGTYRITNLPSLGRFKFRKKIAEKSLSGKVKEFNNIVQRYSVGLASSDLPFGVIRKESR
NDFINDVCKLYNINDMKIIKELKEDADLIVCMLKGFKPRGDDNRPDRGALPLVAMLAGENAQIFTFIYGPLIKGAINLID
QDINKLAKRNGLWKSFVSLSDFIVLDCPIIGESYNEFRLIINKNNKESILRKTSKQQNILVDPTPNHYQENDVDTVIYSI
FKYIVPNCFSGMCNPPGGDWSGLSIIDNVHEFRWLSLPRVSENGKRPDHVIQILDLFEKPLLLSIVSKEKPNDLEPKIGV
QLIKYIEYLFDFTPSVQRKIAGGNWEFGNKSLVPNDFILLSAGAFIDYDNLTENDYEKIFEVTGCDLLIAIKNQNNPQKW
VIKFKPKNTIAEKLVNYIKLNFKSNIFDTGFFHIEG
;
;MNVFRIHGDNIIECERVIDLILSKINPQKVKRGFISLSCPFIEIIFKEGHDYFHWRFDMFPGFNKNTNDRWNSNILDLLS
QKGSFLYETPDVIITSLNNGKEEILMAIEFCSALQAGNQAWQRSGRAYSVGRTGYPYIYIVDFVKYELNNSDRSRKNLRF
PNPAIPYSYISHSKNTGNFIVQAYFRGEEYQPKYDKKLKFFDETIFAEDDIADYIIAKLQHRDTSNIEQLLINKNLKMVE
FLSKNTKNDNNFTYSEWESIYNGTYRITNLPSLGRFKFRKKIAEKSLSGKVKEFNNIVQRYSVGLASSDLPFGVIRKESR
NDFINDVCKLYNINDMKIIKELKEDADLIVCMLKGFKPRGDDNRPDRGALPLVAMLAGENAQIFTFIYGPLIKGAINLID
QDINKLAKRNGLWKSFVSLSDFIVLDCPIIGESYNEFRLIINKNNKESILRKTSKQQNILVDPTPNHYQENDVDTVIYSI
FKYIVPNCFSGMCNPPGGDWSGLSIIDNVHEFRWLSLPRVSENGKRPDHVIQILDLFEKPLLLSIVSKEKPNDLEPKIGV
QLIKYIEYLFDFTPSVQRKIAGGNWEFGNKSLVPNDFILLSAGAFIDYDNLTENDYEKIFEVTGCDLLIAIKNQNNPQKW
VIKFKPKNTIAEKLVNYIKLNFKSNIFDTGFFHIEG
;
A ? 
2 polydeoxyribonucleotide no no '(DC)(DA)(DT)(DT)(DC)(DC)(DT)(DC)' CATTCCTC E ? 
3 polydeoxyribonucleotide no no '(DG)(DA)(DG)(DG)(DA)(DA)(DT)(DG)(DC)(DA)(DG)(DA)(DC)' GAGGAATGCAGAC F ? 
4 polydeoxyribonucleotide no no '(DG)(DT)(DC)(DT)(DG)' GTCTG G ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
5 'MAGNESIUM ION'                        MG  
6 'CHLORIDE ION'                         CL  
7 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' MES 
8 water                                  HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ASN n 
1 3   VAL n 
1 4   PHE n 
1 5   ARG n 
1 6   ILE n 
1 7   HIS n 
1 8   GLY n 
1 9   ASP n 
1 10  ASN n 
1 11  ILE n 
1 12  ILE n 
1 13  GLU n 
1 14  CYS n 
1 15  GLU n 
1 16  ARG n 
1 17  VAL n 
1 18  ILE n 
1 19  ASP n 
1 20  LEU n 
1 21  ILE n 
1 22  LEU n 
1 23  SER n 
1 24  LYS n 
1 25  ILE n 
1 26  ASN n 
1 27  PRO n 
1 28  GLN n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  ARG n 
1 33  GLY n 
1 34  PHE n 
1 35  ILE n 
1 36  SER n 
1 37  LEU n 
1 38  SER n 
1 39  CYS n 
1 40  PRO n 
1 41  PHE n 
1 42  ILE n 
1 43  GLU n 
1 44  ILE n 
1 45  ILE n 
1 46  PHE n 
1 47  LYS n 
1 48  GLU n 
1 49  GLY n 
1 50  HIS n 
1 51  ASP n 
1 52  TYR n 
1 53  PHE n 
1 54  HIS n 
1 55  TRP n 
1 56  ARG n 
1 57  PHE n 
1 58  ASP n 
1 59  MET n 
1 60  PHE n 
1 61  PRO n 
1 62  GLY n 
1 63  PHE n 
1 64  ASN n 
1 65  LYS n 
1 66  ASN n 
1 67  THR n 
1 68  ASN n 
1 69  ASP n 
1 70  ARG n 
1 71  TRP n 
1 72  ASN n 
1 73  SER n 
1 74  ASN n 
1 75  ILE n 
1 76  LEU n 
1 77  ASP n 
1 78  LEU n 
1 79  LEU n 
1 80  SER n 
1 81  GLN n 
1 82  LYS n 
1 83  GLY n 
1 84  SER n 
1 85  PHE n 
1 86  LEU n 
1 87  TYR n 
1 88  GLU n 
1 89  THR n 
1 90  PRO n 
1 91  ASP n 
1 92  VAL n 
1 93  ILE n 
1 94  ILE n 
1 95  THR n 
1 96  SER n 
1 97  LEU n 
1 98  ASN n 
1 99  ASN n 
1 100 GLY n 
1 101 LYS n 
1 102 GLU n 
1 103 GLU n 
1 104 ILE n 
1 105 LEU n 
1 106 MET n 
1 107 ALA n 
1 108 ILE n 
1 109 GLU n 
1 110 PHE n 
1 111 CYS n 
1 112 SER n 
1 113 ALA n 
1 114 LEU n 
1 115 GLN n 
1 116 ALA n 
1 117 GLY n 
1 118 ASN n 
1 119 GLN n 
1 120 ALA n 
1 121 TRP n 
1 122 GLN n 
1 123 ARG n 
1 124 SER n 
1 125 GLY n 
1 126 ARG n 
1 127 ALA n 
1 128 TYR n 
1 129 SER n 
1 130 VAL n 
1 131 GLY n 
1 132 ARG n 
1 133 THR n 
1 134 GLY n 
1 135 TYR n 
1 136 PRO n 
1 137 TYR n 
1 138 ILE n 
1 139 TYR n 
1 140 ILE n 
1 141 VAL n 
1 142 ASP n 
1 143 PHE n 
1 144 VAL n 
1 145 LYS n 
1 146 TYR n 
1 147 GLU n 
1 148 LEU n 
1 149 ASN n 
1 150 ASN n 
1 151 SER n 
1 152 ASP n 
1 153 ARG n 
1 154 SER n 
1 155 ARG n 
1 156 LYS n 
1 157 ASN n 
1 158 LEU n 
1 159 ARG n 
1 160 PHE n 
1 161 PRO n 
1 162 ASN n 
1 163 PRO n 
1 164 ALA n 
1 165 ILE n 
1 166 PRO n 
1 167 TYR n 
1 168 SER n 
1 169 TYR n 
1 170 ILE n 
1 171 SER n 
1 172 HIS n 
1 173 SER n 
1 174 LYS n 
1 175 ASN n 
1 176 THR n 
1 177 GLY n 
1 178 ASN n 
1 179 PHE n 
1 180 ILE n 
1 181 VAL n 
1 182 GLN n 
1 183 ALA n 
1 184 TYR n 
1 185 PHE n 
1 186 ARG n 
1 187 GLY n 
1 188 GLU n 
1 189 GLU n 
1 190 TYR n 
1 191 GLN n 
1 192 PRO n 
1 193 LYS n 
1 194 TYR n 
1 195 ASP n 
1 196 LYS n 
1 197 LYS n 
1 198 LEU n 
1 199 LYS n 
1 200 PHE n 
1 201 PHE n 
1 202 ASP n 
1 203 GLU n 
1 204 THR n 
1 205 ILE n 
1 206 PHE n 
1 207 ALA n 
1 208 GLU n 
1 209 ASP n 
1 210 ASP n 
1 211 ILE n 
1 212 ALA n 
1 213 ASP n 
1 214 TYR n 
1 215 ILE n 
1 216 ILE n 
1 217 ALA n 
1 218 LYS n 
1 219 LEU n 
1 220 GLN n 
1 221 HIS n 
1 222 ARG n 
1 223 ASP n 
1 224 THR n 
1 225 SER n 
1 226 ASN n 
1 227 ILE n 
1 228 GLU n 
1 229 GLN n 
1 230 LEU n 
1 231 LEU n 
1 232 ILE n 
1 233 ASN n 
1 234 LYS n 
1 235 ASN n 
1 236 LEU n 
1 237 LYS n 
1 238 MET n 
1 239 VAL n 
1 240 GLU n 
1 241 PHE n 
1 242 LEU n 
1 243 SER n 
1 244 LYS n 
1 245 ASN n 
1 246 THR n 
1 247 LYS n 
1 248 ASN n 
1 249 ASP n 
1 250 ASN n 
1 251 ASN n 
1 252 PHE n 
1 253 THR n 
1 254 TYR n 
1 255 SER n 
1 256 GLU n 
1 257 TRP n 
1 258 GLU n 
1 259 SER n 
1 260 ILE n 
1 261 TYR n 
1 262 ASN n 
1 263 GLY n 
1 264 THR n 
1 265 TYR n 
1 266 ARG n 
1 267 ILE n 
1 268 THR n 
1 269 ASN n 
1 270 LEU n 
1 271 PRO n 
1 272 SER n 
1 273 LEU n 
1 274 GLY n 
1 275 ARG n 
1 276 PHE n 
1 277 LYS n 
1 278 PHE n 
1 279 ARG n 
1 280 LYS n 
1 281 LYS n 
1 282 ILE n 
1 283 ALA n 
1 284 GLU n 
1 285 LYS n 
1 286 SER n 
1 287 LEU n 
1 288 SER n 
1 289 GLY n 
1 290 LYS n 
1 291 VAL n 
1 292 LYS n 
1 293 GLU n 
1 294 PHE n 
1 295 ASN n 
1 296 ASN n 
1 297 ILE n 
1 298 VAL n 
1 299 GLN n 
1 300 ARG n 
1 301 TYR n 
1 302 SER n 
1 303 VAL n 
1 304 GLY n 
1 305 LEU n 
1 306 ALA n 
1 307 SER n 
1 308 SER n 
1 309 ASP n 
1 310 LEU n 
1 311 PRO n 
1 312 PHE n 
1 313 GLY n 
1 314 VAL n 
1 315 ILE n 
1 316 ARG n 
1 317 LYS n 
1 318 GLU n 
1 319 SER n 
1 320 ARG n 
1 321 ASN n 
1 322 ASP n 
1 323 PHE n 
1 324 ILE n 
1 325 ASN n 
1 326 ASP n 
1 327 VAL n 
1 328 CYS n 
1 329 LYS n 
1 330 LEU n 
1 331 TYR n 
1 332 ASN n 
1 333 ILE n 
1 334 ASN n 
1 335 ASP n 
1 336 MET n 
1 337 LYS n 
1 338 ILE n 
1 339 ILE n 
1 340 LYS n 
1 341 GLU n 
1 342 LEU n 
1 343 LYS n 
1 344 GLU n 
1 345 ASP n 
1 346 ALA n 
1 347 ASP n 
1 348 LEU n 
1 349 ILE n 
1 350 VAL n 
1 351 CYS n 
1 352 MET n 
1 353 LEU n 
1 354 LYS n 
1 355 GLY n 
1 356 PHE n 
1 357 LYS n 
1 358 PRO n 
1 359 ARG n 
1 360 GLY n 
1 361 ASP n 
1 362 ASP n 
1 363 ASN n 
1 364 ARG n 
1 365 PRO n 
1 366 ASP n 
1 367 ARG n 
1 368 GLY n 
1 369 ALA n 
1 370 LEU n 
1 371 PRO n 
1 372 LEU n 
1 373 VAL n 
1 374 ALA n 
1 375 MET n 
1 376 LEU n 
1 377 ALA n 
1 378 GLY n 
1 379 GLU n 
1 380 ASN n 
1 381 ALA n 
1 382 GLN n 
1 383 ILE n 
1 384 PHE n 
1 385 THR n 
1 386 PHE n 
1 387 ILE n 
1 388 TYR n 
1 389 GLY n 
1 390 PRO n 
1 391 LEU n 
1 392 ILE n 
1 393 LYS n 
1 394 GLY n 
1 395 ALA n 
1 396 ILE n 
1 397 ASN n 
1 398 LEU n 
1 399 ILE n 
1 400 ASP n 
1 401 GLN n 
1 402 ASP n 
1 403 ILE n 
1 404 ASN n 
1 405 LYS n 
1 406 LEU n 
1 407 ALA n 
1 408 LYS n 
1 409 ARG n 
1 410 ASN n 
1 411 GLY n 
1 412 LEU n 
1 413 TRP n 
1 414 LYS n 
1 415 SER n 
1 416 PHE n 
1 417 VAL n 
1 418 SER n 
1 419 LEU n 
1 420 SER n 
1 421 ASP n 
1 422 PHE n 
1 423 ILE n 
1 424 VAL n 
1 425 LEU n 
1 426 ASP n 
1 427 CYS n 
1 428 PRO n 
1 429 ILE n 
1 430 ILE n 
1 431 GLY n 
1 432 GLU n 
1 433 SER n 
1 434 TYR n 
1 435 ASN n 
1 436 GLU n 
1 437 PHE n 
1 438 ARG n 
1 439 LEU n 
1 440 ILE n 
1 441 ILE n 
1 442 ASN n 
1 443 LYS n 
1 444 ASN n 
1 445 ASN n 
1 446 LYS n 
1 447 GLU n 
1 448 SER n 
1 449 ILE n 
1 450 LEU n 
1 451 ARG n 
1 452 LYS n 
1 453 THR n 
1 454 SER n 
1 455 LYS n 
1 456 GLN n 
1 457 GLN n 
1 458 ASN n 
1 459 ILE n 
1 460 LEU n 
1 461 VAL n 
1 462 ASP n 
1 463 PRO n 
1 464 THR n 
1 465 PRO n 
1 466 ASN n 
1 467 HIS n 
1 468 TYR n 
1 469 GLN n 
1 470 GLU n 
1 471 ASN n 
1 472 ASP n 
1 473 VAL n 
1 474 ASP n 
1 475 THR n 
1 476 VAL n 
1 477 ILE n 
1 478 TYR n 
1 479 SER n 
1 480 ILE n 
1 481 PHE n 
1 482 LYS n 
1 483 TYR n 
1 484 ILE n 
1 485 VAL n 
1 486 PRO n 
1 487 ASN n 
1 488 CYS n 
1 489 PHE n 
1 490 SER n 
1 491 GLY n 
1 492 MET n 
1 493 CYS n 
1 494 ASN n 
1 495 PRO n 
1 496 PRO n 
1 497 GLY n 
1 498 GLY n 
1 499 ASP n 
1 500 TRP n 
1 501 SER n 
1 502 GLY n 
1 503 LEU n 
1 504 SER n 
1 505 ILE n 
1 506 ILE n 
1 507 ASP n 
1 508 ASN n 
1 509 VAL n 
1 510 HIS n 
1 511 GLU n 
1 512 PHE n 
1 513 ARG n 
1 514 TRP n 
1 515 LEU n 
1 516 SER n 
1 517 LEU n 
1 518 PRO n 
1 519 ARG n 
1 520 VAL n 
1 521 SER n 
1 522 GLU n 
1 523 ASN n 
1 524 GLY n 
1 525 LYS n 
1 526 ARG n 
1 527 PRO n 
1 528 ASP n 
1 529 HIS n 
1 530 VAL n 
1 531 ILE n 
1 532 GLN n 
1 533 ILE n 
1 534 LEU n 
1 535 ASP n 
1 536 LEU n 
1 537 PHE n 
1 538 GLU n 
1 539 LYS n 
1 540 PRO n 
1 541 LEU n 
1 542 LEU n 
1 543 LEU n 
1 544 SER n 
1 545 ILE n 
1 546 VAL n 
1 547 SER n 
1 548 LYS n 
1 549 GLU n 
1 550 LYS n 
1 551 PRO n 
1 552 ASN n 
1 553 ASP n 
1 554 LEU n 
1 555 GLU n 
1 556 PRO n 
1 557 LYS n 
1 558 ILE n 
1 559 GLY n 
1 560 VAL n 
1 561 GLN n 
1 562 LEU n 
1 563 ILE n 
1 564 LYS n 
1 565 TYR n 
1 566 ILE n 
1 567 GLU n 
1 568 TYR n 
1 569 LEU n 
1 570 PHE n 
1 571 ASP n 
1 572 PHE n 
1 573 THR n 
1 574 PRO n 
1 575 SER n 
1 576 VAL n 
1 577 GLN n 
1 578 ARG n 
1 579 LYS n 
1 580 ILE n 
1 581 ALA n 
1 582 GLY n 
1 583 GLY n 
1 584 ASN n 
1 585 TRP n 
1 586 GLU n 
1 587 PHE n 
1 588 GLY n 
1 589 ASN n 
1 590 LYS n 
1 591 SER n 
1 592 LEU n 
1 593 VAL n 
1 594 PRO n 
1 595 ASN n 
1 596 ASP n 
1 597 PHE n 
1 598 ILE n 
1 599 LEU n 
1 600 LEU n 
1 601 SER n 
1 602 ALA n 
1 603 GLY n 
1 604 ALA n 
1 605 PHE n 
1 606 ILE n 
1 607 ASP n 
1 608 TYR n 
1 609 ASP n 
1 610 ASN n 
1 611 LEU n 
1 612 THR n 
1 613 GLU n 
1 614 ASN n 
1 615 ASP n 
1 616 TYR n 
1 617 GLU n 
1 618 LYS n 
1 619 ILE n 
1 620 PHE n 
1 621 GLU n 
1 622 VAL n 
1 623 THR n 
1 624 GLY n 
1 625 CYS n 
1 626 ASP n 
1 627 LEU n 
1 628 LEU n 
1 629 ILE n 
1 630 ALA n 
1 631 ILE n 
1 632 LYS n 
1 633 ASN n 
1 634 GLN n 
1 635 ASN n 
1 636 ASN n 
1 637 PRO n 
1 638 GLN n 
1 639 LYS n 
1 640 TRP n 
1 641 VAL n 
1 642 ILE n 
1 643 LYS n 
1 644 PHE n 
1 645 LYS n 
1 646 PRO n 
1 647 LYS n 
1 648 ASN n 
1 649 THR n 
1 650 ILE n 
1 651 ALA n 
1 652 GLU n 
1 653 LYS n 
1 654 LEU n 
1 655 VAL n 
1 656 ASN n 
1 657 TYR n 
1 658 ILE n 
1 659 LYS n 
1 660 LEU n 
1 661 ASN n 
1 662 PHE n 
1 663 LYS n 
1 664 SER n 
1 665 ASN n 
1 666 ILE n 
1 667 PHE n 
1 668 ASP n 
1 669 THR n 
1 670 GLY n 
1 671 PHE n 
1 672 PHE n 
1 673 HIS n 
1 674 ILE n 
1 675 GLU n 
1 676 GLY n 
2 1   DC  n 
2 2   DA  n 
2 3   DT  n 
2 4   DT  n 
2 5   DC  n 
2 6   DC  n 
2 7   DT  n 
2 8   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 
4 1   DG  n 
4 2   DT  n 
4 3   DC  n 
4 4   DT  n 
4 5   DG  n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   676 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 bsmIR 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Geobacillus stearothermophilus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1422 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_pdbx_entity_src_syn.entity_id 
_pdbx_entity_src_syn.pdbx_src_id 
_pdbx_entity_src_syn.pdbx_alt_source_flag 
_pdbx_entity_src_syn.pdbx_beg_seq_num 
_pdbx_entity_src_syn.pdbx_end_seq_num 
_pdbx_entity_src_syn.organism_scientific 
_pdbx_entity_src_syn.organism_common_name 
_pdbx_entity_src_syn.ncbi_taxonomy_id 
_pdbx_entity_src_syn.details 
2 1 sample 1 8  'Geobacillus stearothermophilus' ? 1422 ? 
3 1 sample 1 13 'Geobacillus stearothermophilus' ? 1422 ? 
4 1 sample 1 5  '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 
MG  non-polymer         . 'MAGNESIUM ION'                        ? 'Mg 2'            24.305  
PHE 'L-peptide linking' y PHENYLALANINE                          ? 'C9 H11 N O2'     165.189 
PRO 'L-peptide linking' y PROLINE                                ? 'C5 H9 N O2'      115.130 
SER 'L-peptide linking' y SERINE                                 ? 'C3 H7 N O3'      105.093 
THR 'L-peptide linking' y THREONINE                              ? 'C4 H9 N O3'      119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                             ? 'C11 H12 N2 O2'   204.225 
TYR 'L-peptide linking' y TYROSINE                               ? 'C9 H11 N O3'     181.189 
VAL 'L-peptide linking' y VALINE                                 ? 'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   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  ?   ?   ?   A . n 
A 1 67  THR 67  67  ?   ?   ?   A . n 
A 1 68  ASN 68  68  68  ASN ASN A . n 
A 1 69  ASP 69  69  69  ASP ASP A . n 
A 1 70  ARG 70  70  70  ARG ARG A . n 
A 1 71  TRP 71  71  71  TRP TRP A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  ASN 74  74  74  ASN ASN A . n 
A 1 75  ILE 75  75  75  ILE ILE A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  ASP 77  77  77  ASP ASP A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  GLN 81  81  81  GLN GLN A . n 
A 1 82  LYS 82  82  82  LYS LYS A . n 
A 1 83  GLY 83  83  83  GLY GLY A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  PHE 85  85  85  PHE PHE A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  TYR 87  87  87  TYR TYR A . n 
A 1 88  GLU 88  88  88  GLU GLU A . n 
A 1 89  THR 89  89  89  THR THR A . n 
A 1 90  PRO 90  90  90  PRO PRO A . n 
A 1 91  ASP 91  91  91  ASP ASP A . n 
A 1 92  VAL 92  92  92  VAL VAL A . n 
A 1 93  ILE 93  93  93  ILE ILE A . n 
A 1 94  ILE 94  94  94  ILE ILE A . n 
A 1 95  THR 95  95  95  THR THR A . n 
A 1 96  SER 96  96  96  SER SER A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  ASN 98  98  98  ASN ASN A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 LYS 101 101 101 LYS LYS A . n 
A 1 102 GLU 102 102 102 GLU GLU A . n 
A 1 103 GLU 103 103 103 GLU GLU A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 MET 106 106 106 MET MET A . n 
A 1 107 ALA 107 107 107 ALA ALA A . n 
A 1 108 ILE 108 108 108 ILE ILE A . n 
A 1 109 GLU 109 109 109 GLU GLU A . n 
A 1 110 PHE 110 110 110 PHE PHE A . n 
A 1 111 CYS 111 111 111 CYS CYS A . n 
A 1 112 SER 112 112 112 SER SER A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 LEU 114 114 114 LEU LEU A . n 
A 1 115 GLN 115 115 115 GLN GLN A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLY 117 117 117 GLY GLY A . n 
A 1 118 ASN 118 118 118 ASN ASN A . n 
A 1 119 GLN 119 119 119 GLN GLN A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 TRP 121 121 121 TRP TRP A . n 
A 1 122 GLN 122 122 122 GLN GLN A . n 
A 1 123 ARG 123 123 123 ARG ARG A . n 
A 1 124 SER 124 124 124 SER SER A . n 
A 1 125 GLY 125 125 125 GLY GLY A . n 
A 1 126 ARG 126 126 126 ARG ARG A . n 
A 1 127 ALA 127 127 127 ALA ALA A . n 
A 1 128 TYR 128 128 128 TYR TYR A . n 
A 1 129 SER 129 129 129 SER SER A . n 
A 1 130 VAL 130 130 130 VAL VAL A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 ARG 132 132 132 ARG ARG A . n 
A 1 133 THR 133 133 133 THR THR A . n 
A 1 134 GLY 134 134 134 GLY GLY A . n 
A 1 135 TYR 135 135 135 TYR TYR A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 TYR 137 137 137 TYR TYR A . n 
A 1 138 ILE 138 138 138 ILE ILE A . n 
A 1 139 TYR 139 139 139 TYR TYR A . n 
A 1 140 ILE 140 140 140 ILE ILE A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 ASP 142 142 142 ASP ASP A . n 
A 1 143 PHE 143 143 143 PHE PHE A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 LYS 145 145 145 LYS LYS A . n 
A 1 146 TYR 146 146 146 TYR TYR A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 LEU 148 148 148 LEU LEU A . n 
A 1 149 ASN 149 149 149 ASN ASN A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 SER 151 151 151 SER SER A . n 
A 1 152 ASP 152 152 152 ASP ASP A . n 
A 1 153 ARG 153 153 153 ARG ARG A . n 
A 1 154 SER 154 154 154 SER SER A . n 
A 1 155 ARG 155 155 155 ARG ARG A . n 
A 1 156 LYS 156 156 156 LYS LYS A . n 
A 1 157 ASN 157 157 157 ASN ASN A . n 
A 1 158 LEU 158 158 158 LEU LEU A . n 
A 1 159 ARG 159 159 159 ARG ARG A . n 
A 1 160 PHE 160 160 160 PHE PHE A . n 
A 1 161 PRO 161 161 161 PRO PRO A . n 
A 1 162 ASN 162 162 162 ASN ASN A . n 
A 1 163 PRO 163 163 163 PRO PRO A . n 
A 1 164 ALA 164 164 164 ALA ALA A . n 
A 1 165 ILE 165 165 165 ILE ILE A . n 
A 1 166 PRO 166 166 166 PRO PRO A . n 
A 1 167 TYR 167 167 167 TYR TYR A . n 
A 1 168 SER 168 168 168 SER SER A . n 
A 1 169 TYR 169 169 169 TYR TYR A . n 
A 1 170 ILE 170 170 170 ILE ILE A . n 
A 1 171 SER 171 171 171 SER SER A . n 
A 1 172 HIS 172 172 172 HIS HIS A . n 
A 1 173 SER 173 173 173 SER SER A . n 
A 1 174 LYS 174 174 174 LYS LYS A . n 
A 1 175 ASN 175 175 175 ASN ASN A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 GLY 177 177 177 GLY GLY A . n 
A 1 178 ASN 178 178 178 ASN ASN A . n 
A 1 179 PHE 179 179 179 PHE PHE A . n 
A 1 180 ILE 180 180 180 ILE ILE A . n 
A 1 181 VAL 181 181 181 VAL VAL A . n 
A 1 182 GLN 182 182 182 GLN GLN A . n 
A 1 183 ALA 183 183 183 ALA ALA A . n 
A 1 184 TYR 184 184 184 TYR TYR A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 ARG 186 186 186 ARG ARG A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 GLU 188 188 188 GLU GLU A . n 
A 1 189 GLU 189 189 189 GLU GLU A . n 
A 1 190 TYR 190 190 190 TYR TYR A . n 
A 1 191 GLN 191 191 191 GLN GLN A . n 
A 1 192 PRO 192 192 192 PRO PRO A . n 
A 1 193 LYS 193 193 193 LYS LYS A . n 
A 1 194 TYR 194 194 194 TYR TYR A . n 
A 1 195 ASP 195 195 195 ASP ASP A . n 
A 1 196 LYS 196 196 196 LYS LYS A . n 
A 1 197 LYS 197 197 197 LYS LYS A . n 
A 1 198 LEU 198 198 198 LEU LEU A . n 
A 1 199 LYS 199 199 199 LYS LYS A . n 
A 1 200 PHE 200 200 200 PHE PHE A . n 
A 1 201 PHE 201 201 201 PHE PHE A . n 
A 1 202 ASP 202 202 202 ASP ASP A . n 
A 1 203 GLU 203 203 203 GLU GLU A . n 
A 1 204 THR 204 204 204 THR THR A . n 
A 1 205 ILE 205 205 205 ILE ILE A . n 
A 1 206 PHE 206 206 206 PHE PHE A . n 
A 1 207 ALA 207 207 207 ALA ALA A . n 
A 1 208 GLU 208 208 208 GLU GLU A . n 
A 1 209 ASP 209 209 209 ASP ASP A . n 
A 1 210 ASP 210 210 210 ASP ASP A . n 
A 1 211 ILE 211 211 211 ILE ILE A . n 
A 1 212 ALA 212 212 212 ALA ALA A . n 
A 1 213 ASP 213 213 213 ASP ASP A . n 
A 1 214 TYR 214 214 214 TYR TYR A . n 
A 1 215 ILE 215 215 215 ILE ILE A . n 
A 1 216 ILE 216 216 216 ILE ILE A . n 
A 1 217 ALA 217 217 217 ALA ALA A . n 
A 1 218 LYS 218 218 218 LYS LYS A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 GLN 220 220 220 GLN GLN A . n 
A 1 221 HIS 221 221 221 HIS HIS A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 ASP 223 223 223 ASP ASP A . n 
A 1 224 THR 224 224 224 THR THR A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 ASN 226 226 226 ASN ASN A . n 
A 1 227 ILE 227 227 227 ILE ILE A . n 
A 1 228 GLU 228 228 228 GLU GLU A . n 
A 1 229 GLN 229 229 229 GLN GLN A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 LEU 231 231 231 LEU LEU A . n 
A 1 232 ILE 232 232 232 ILE ILE A . n 
A 1 233 ASN 233 233 233 ASN ASN A . n 
A 1 234 LYS 234 234 234 LYS LYS A . n 
A 1 235 ASN 235 235 235 ASN ASN A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 LYS 237 237 237 LYS LYS A . n 
A 1 238 MET 238 238 238 MET MET A . n 
A 1 239 VAL 239 239 239 VAL VAL A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 PHE 241 241 241 PHE PHE A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 SER 243 243 243 SER SER A . n 
A 1 244 LYS 244 244 244 LYS LYS A . n 
A 1 245 ASN 245 245 245 ASN ASN A . n 
A 1 246 THR 246 246 246 THR THR A . n 
A 1 247 LYS 247 247 247 LYS LYS A . n 
A 1 248 ASN 248 248 248 ASN ASN A . n 
A 1 249 ASP 249 249 249 ASP ASP A . n 
A 1 250 ASN 250 250 250 ASN ASN A . n 
A 1 251 ASN 251 251 251 ASN ASN A . n 
A 1 252 PHE 252 252 252 PHE PHE A . n 
A 1 253 THR 253 253 253 THR THR A . n 
A 1 254 TYR 254 254 254 TYR TYR A . n 
A 1 255 SER 255 255 255 SER SER A . n 
A 1 256 GLU 256 256 256 GLU GLU A . n 
A 1 257 TRP 257 257 257 TRP TRP A . n 
A 1 258 GLU 258 258 258 GLU GLU A . n 
A 1 259 SER 259 259 259 SER SER A . n 
A 1 260 ILE 260 260 260 ILE ILE A . n 
A 1 261 TYR 261 261 261 TYR TYR A . n 
A 1 262 ASN 262 262 262 ASN ASN A . n 
A 1 263 GLY 263 263 263 GLY GLY A . n 
A 1 264 THR 264 264 264 THR THR A . n 
A 1 265 TYR 265 265 265 TYR TYR A . n 
A 1 266 ARG 266 266 266 ARG ARG A . n 
A 1 267 ILE 267 267 267 ILE ILE A . n 
A 1 268 THR 268 268 268 THR THR A . n 
A 1 269 ASN 269 269 269 ASN ASN A . n 
A 1 270 LEU 270 270 270 LEU LEU A . n 
A 1 271 PRO 271 271 271 PRO PRO A . n 
A 1 272 SER 272 272 272 SER SER A . n 
A 1 273 LEU 273 273 273 LEU LEU A . n 
A 1 274 GLY 274 274 274 GLY GLY A . n 
A 1 275 ARG 275 275 275 ARG ARG A . n 
A 1 276 PHE 276 276 276 PHE PHE A . n 
A 1 277 LYS 277 277 277 LYS LYS A . n 
A 1 278 PHE 278 278 278 PHE PHE A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 LYS 280 280 280 LYS LYS A . n 
A 1 281 LYS 281 281 281 LYS LYS A . n 
A 1 282 ILE 282 282 282 ILE ILE A . n 
A 1 283 ALA 283 283 283 ALA ALA A . n 
A 1 284 GLU 284 284 284 GLU GLU A . n 
A 1 285 LYS 285 285 285 LYS LYS A . n 
A 1 286 SER 286 286 286 SER SER A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 SER 288 288 288 SER SER A . n 
A 1 289 GLY 289 289 289 GLY GLY A . n 
A 1 290 LYS 290 290 290 LYS LYS A . n 
A 1 291 VAL 291 291 291 VAL VAL A . n 
A 1 292 LYS 292 292 292 LYS LYS A . n 
A 1 293 GLU 293 293 293 GLU GLU A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 ASN 295 295 295 ASN ASN A . n 
A 1 296 ASN 296 296 296 ASN ASN A . n 
A 1 297 ILE 297 297 297 ILE ILE A . n 
A 1 298 VAL 298 298 298 VAL VAL A . n 
A 1 299 GLN 299 299 299 GLN GLN A . n 
A 1 300 ARG 300 300 300 ARG ARG A . n 
A 1 301 TYR 301 301 301 TYR TYR A . n 
A 1 302 SER 302 302 302 SER SER A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 GLY 304 304 304 GLY GLY A . n 
A 1 305 LEU 305 305 305 LEU LEU A . n 
A 1 306 ALA 306 306 306 ALA ALA A . n 
A 1 307 SER 307 307 307 SER SER A . n 
A 1 308 SER 308 308 308 SER SER A . n 
A 1 309 ASP 309 309 309 ASP ASP A . n 
A 1 310 LEU 310 310 310 LEU LEU A . n 
A 1 311 PRO 311 311 311 PRO PRO A . n 
A 1 312 PHE 312 312 312 PHE PHE A . n 
A 1 313 GLY 313 313 313 GLY GLY A . n 
A 1 314 VAL 314 314 314 VAL VAL A . n 
A 1 315 ILE 315 315 315 ILE ILE A . n 
A 1 316 ARG 316 316 316 ARG ARG A . n 
A 1 317 LYS 317 317 317 LYS LYS A . n 
A 1 318 GLU 318 318 318 GLU GLU A . n 
A 1 319 SER 319 319 319 SER SER A . n 
A 1 320 ARG 320 320 320 ARG ARG A . n 
A 1 321 ASN 321 321 321 ASN ASN A . n 
A 1 322 ASP 322 322 322 ASP ASP A . n 
A 1 323 PHE 323 323 323 PHE PHE A . n 
A 1 324 ILE 324 324 324 ILE ILE A . n 
A 1 325 ASN 325 325 325 ASN ASN A . n 
A 1 326 ASP 326 326 326 ASP ASP A . n 
A 1 327 VAL 327 327 327 VAL VAL A . n 
A 1 328 CYS 328 328 328 CYS CYS A . n 
A 1 329 LYS 329 329 329 LYS LYS A . n 
A 1 330 LEU 330 330 330 LEU LEU A . n 
A 1 331 TYR 331 331 331 TYR TYR A . n 
A 1 332 ASN 332 332 332 ASN ASN A . n 
A 1 333 ILE 333 333 333 ILE ILE A . n 
A 1 334 ASN 334 334 334 ASN ASN A . n 
A 1 335 ASP 335 335 335 ASP ASP A . n 
A 1 336 MET 336 336 336 MET MET A . n 
A 1 337 LYS 337 337 337 LYS LYS A . n 
A 1 338 ILE 338 338 338 ILE ILE A . n 
A 1 339 ILE 339 339 339 ILE ILE A . n 
A 1 340 LYS 340 340 340 LYS LYS A . n 
A 1 341 GLU 341 341 341 GLU GLU A . n 
A 1 342 LEU 342 342 342 LEU LEU A . n 
A 1 343 LYS 343 343 343 LYS LYS A . n 
A 1 344 GLU 344 344 344 GLU GLU A . n 
A 1 345 ASP 345 345 345 ASP ASP A . n 
A 1 346 ALA 346 346 346 ALA ALA A . n 
A 1 347 ASP 347 347 347 ASP ASP A . n 
A 1 348 LEU 348 348 348 LEU LEU A . n 
A 1 349 ILE 349 349 349 ILE ILE A . n 
A 1 350 VAL 350 350 350 VAL VAL A . n 
A 1 351 CYS 351 351 351 CYS CYS A . n 
A 1 352 MET 352 352 352 MET MET A . n 
A 1 353 LEU 353 353 353 LEU LEU A . n 
A 1 354 LYS 354 354 354 LYS LYS A . n 
A 1 355 GLY 355 355 355 GLY GLY A . n 
A 1 356 PHE 356 356 356 PHE PHE A . n 
A 1 357 LYS 357 357 357 LYS LYS A . n 
A 1 358 PRO 358 358 358 PRO PRO A . n 
A 1 359 ARG 359 359 359 ARG ARG A . n 
A 1 360 GLY 360 360 360 GLY GLY A . n 
A 1 361 ASP 361 361 361 ASP ASP A . n 
A 1 362 ASP 362 362 362 ASP ASP A . n 
A 1 363 ASN 363 363 363 ASN ASN A . n 
A 1 364 ARG 364 364 364 ARG ARG A . n 
A 1 365 PRO 365 365 365 PRO PRO A . n 
A 1 366 ASP 366 366 366 ASP ASP A . n 
A 1 367 ARG 367 367 367 ARG ARG A . n 
A 1 368 GLY 368 368 368 GLY GLY A . n 
A 1 369 ALA 369 369 369 ALA ALA A . n 
A 1 370 LEU 370 370 370 LEU LEU A . n 
A 1 371 PRO 371 371 371 PRO PRO A . n 
A 1 372 LEU 372 372 372 LEU LEU A . n 
A 1 373 VAL 373 373 373 VAL VAL A . n 
A 1 374 ALA 374 374 374 ALA ALA A . n 
A 1 375 MET 375 375 375 MET MET A . n 
A 1 376 LEU 376 376 376 LEU LEU A . n 
A 1 377 ALA 377 377 377 ALA ALA A . n 
A 1 378 GLY 378 378 378 GLY GLY A . n 
A 1 379 GLU 379 379 379 GLU GLU A . n 
A 1 380 ASN 380 380 380 ASN ASN A . n 
A 1 381 ALA 381 381 381 ALA ALA A . n 
A 1 382 GLN 382 382 382 GLN GLN A . n 
A 1 383 ILE 383 383 383 ILE ILE A . n 
A 1 384 PHE 384 384 384 PHE PHE A . n 
A 1 385 THR 385 385 385 THR THR A . n 
A 1 386 PHE 386 386 386 PHE PHE A . n 
A 1 387 ILE 387 387 387 ILE ILE A . n 
A 1 388 TYR 388 388 388 TYR TYR A . n 
A 1 389 GLY 389 389 389 GLY GLY A . n 
A 1 390 PRO 390 390 390 PRO PRO A . n 
A 1 391 LEU 391 391 391 LEU LEU A . n 
A 1 392 ILE 392 392 392 ILE ILE A . n 
A 1 393 LYS 393 393 393 LYS LYS A . n 
A 1 394 GLY 394 394 394 GLY GLY A . n 
A 1 395 ALA 395 395 395 ALA ALA A . n 
A 1 396 ILE 396 396 396 ILE ILE A . n 
A 1 397 ASN 397 397 397 ASN ASN A . n 
A 1 398 LEU 398 398 398 LEU LEU A . n 
A 1 399 ILE 399 399 399 ILE ILE A . n 
A 1 400 ASP 400 400 400 ASP ASP A . n 
A 1 401 GLN 401 401 401 GLN GLN A . n 
A 1 402 ASP 402 402 402 ASP ASP A . n 
A 1 403 ILE 403 403 403 ILE ILE A . n 
A 1 404 ASN 404 404 404 ASN ASN A . n 
A 1 405 LYS 405 405 405 LYS LYS A . n 
A 1 406 LEU 406 406 406 LEU LEU A . n 
A 1 407 ALA 407 407 407 ALA ALA A . n 
A 1 408 LYS 408 408 408 LYS LYS A . n 
A 1 409 ARG 409 409 409 ARG ARG A . n 
A 1 410 ASN 410 410 410 ASN ASN A . n 
A 1 411 GLY 411 411 411 GLY GLY A . n 
A 1 412 LEU 412 412 412 LEU LEU A . n 
A 1 413 TRP 413 413 413 TRP TRP A . n 
A 1 414 LYS 414 414 414 LYS LYS A . n 
A 1 415 SER 415 415 415 SER SER A . n 
A 1 416 PHE 416 416 416 PHE PHE A . n 
A 1 417 VAL 417 417 417 VAL VAL A . n 
A 1 418 SER 418 418 418 SER SER A . n 
A 1 419 LEU 419 419 419 LEU LEU A . n 
A 1 420 SER 420 420 420 SER SER A . n 
A 1 421 ASP 421 421 421 ASP ASP A . n 
A 1 422 PHE 422 422 422 PHE PHE A . n 
A 1 423 ILE 423 423 423 ILE ILE A . n 
A 1 424 VAL 424 424 424 VAL VAL A . n 
A 1 425 LEU 425 425 425 LEU LEU A . n 
A 1 426 ASP 426 426 426 ASP ASP A . n 
A 1 427 CYS 427 427 427 CYS CYS A . n 
A 1 428 PRO 428 428 428 PRO PRO A . n 
A 1 429 ILE 429 429 429 ILE ILE A . n 
A 1 430 ILE 430 430 430 ILE ILE A . n 
A 1 431 GLY 431 431 431 GLY GLY A . n 
A 1 432 GLU 432 432 432 GLU GLU A . n 
A 1 433 SER 433 433 433 SER SER A . n 
A 1 434 TYR 434 434 434 TYR TYR A . n 
A 1 435 ASN 435 435 435 ASN ASN A . n 
A 1 436 GLU 436 436 436 GLU GLU A . n 
A 1 437 PHE 437 437 437 PHE PHE A . n 
A 1 438 ARG 438 438 438 ARG ARG A . n 
A 1 439 LEU 439 439 439 LEU LEU A . n 
A 1 440 ILE 440 440 440 ILE ILE A . n 
A 1 441 ILE 441 441 441 ILE ILE A . n 
A 1 442 ASN 442 442 442 ASN ASN A . n 
A 1 443 LYS 443 443 443 LYS LYS A . n 
A 1 444 ASN 444 444 444 ASN ASN A . n 
A 1 445 ASN 445 445 445 ASN ASN A . n 
A 1 446 LYS 446 446 446 LYS LYS A . n 
A 1 447 GLU 447 447 447 GLU GLU A . n 
A 1 448 SER 448 448 448 SER SER A . n 
A 1 449 ILE 449 449 449 ILE ILE A . n 
A 1 450 LEU 450 450 450 LEU LEU A . n 
A 1 451 ARG 451 451 451 ARG ARG A . n 
A 1 452 LYS 452 452 452 LYS LYS A . n 
A 1 453 THR 453 453 453 THR THR A . n 
A 1 454 SER 454 454 454 SER SER A . n 
A 1 455 LYS 455 455 455 LYS LYS A . n 
A 1 456 GLN 456 456 456 GLN GLN A . n 
A 1 457 GLN 457 457 457 GLN GLN A . n 
A 1 458 ASN 458 458 458 ASN ASN A . n 
A 1 459 ILE 459 459 459 ILE ILE A . n 
A 1 460 LEU 460 460 460 LEU LEU A . n 
A 1 461 VAL 461 461 461 VAL VAL A . n 
A 1 462 ASP 462 462 462 ASP ASP A . n 
A 1 463 PRO 463 463 463 PRO PRO A . n 
A 1 464 THR 464 464 464 THR THR A . n 
A 1 465 PRO 465 465 465 PRO PRO A . n 
A 1 466 ASN 466 466 466 ASN ASN A . n 
A 1 467 HIS 467 467 467 HIS HIS A . n 
A 1 468 TYR 468 468 468 TYR TYR A . n 
A 1 469 GLN 469 469 469 GLN GLN A . n 
A 1 470 GLU 470 470 470 GLU GLU A . n 
A 1 471 ASN 471 471 471 ASN ASN A . n 
A 1 472 ASP 472 472 472 ASP ASP A . n 
A 1 473 VAL 473 473 473 VAL VAL A . n 
A 1 474 ASP 474 474 474 ASP ASP A . n 
A 1 475 THR 475 475 475 THR THR A . n 
A 1 476 VAL 476 476 476 VAL VAL A . n 
A 1 477 ILE 477 477 477 ILE ILE A . n 
A 1 478 TYR 478 478 478 TYR TYR A . n 
A 1 479 SER 479 479 479 SER SER A . n 
A 1 480 ILE 480 480 480 ILE ILE A . n 
A 1 481 PHE 481 481 481 PHE PHE A . n 
A 1 482 LYS 482 482 482 LYS LYS A . n 
A 1 483 TYR 483 483 483 TYR TYR A . n 
A 1 484 ILE 484 484 484 ILE ILE A . n 
A 1 485 VAL 485 485 485 VAL VAL A . n 
A 1 486 PRO 486 486 486 PRO PRO A . n 
A 1 487 ASN 487 487 ?   ?   ?   A . n 
A 1 488 CYS 488 488 ?   ?   ?   A . n 
A 1 489 PHE 489 489 ?   ?   ?   A . n 
A 1 490 SER 490 490 ?   ?   ?   A . n 
A 1 491 GLY 491 491 ?   ?   ?   A . n 
A 1 492 MET 492 492 ?   ?   ?   A . n 
A 1 493 CYS 493 493 ?   ?   ?   A . n 
A 1 494 ASN 494 494 494 ASN ASN A . n 
A 1 495 PRO 495 495 495 PRO PRO A . n 
A 1 496 PRO 496 496 496 PRO PRO A . n 
A 1 497 GLY 497 497 497 GLY GLY A . n 
A 1 498 GLY 498 498 498 GLY GLY A . n 
A 1 499 ASP 499 499 499 ASP ASP A . n 
A 1 500 TRP 500 500 500 TRP TRP A . n 
A 1 501 SER 501 501 501 SER SER A . n 
A 1 502 GLY 502 502 502 GLY GLY A . n 
A 1 503 LEU 503 503 503 LEU LEU A . n 
A 1 504 SER 504 504 504 SER SER A . n 
A 1 505 ILE 505 505 505 ILE ILE A . n 
A 1 506 ILE 506 506 506 ILE ILE A . n 
A 1 507 ASP 507 507 507 ASP ASP A . n 
A 1 508 ASN 508 508 508 ASN ASN A . n 
A 1 509 VAL 509 509 509 VAL VAL A . n 
A 1 510 HIS 510 510 510 HIS HIS A . n 
A 1 511 GLU 511 511 511 GLU GLU A . n 
A 1 512 PHE 512 512 512 PHE PHE A . n 
A 1 513 ARG 513 513 513 ARG ARG A . n 
A 1 514 TRP 514 514 514 TRP TRP A . n 
A 1 515 LEU 515 515 515 LEU LEU A . n 
A 1 516 SER 516 516 516 SER SER A . n 
A 1 517 LEU 517 517 517 LEU LEU A . n 
A 1 518 PRO 518 518 518 PRO PRO A . n 
A 1 519 ARG 519 519 519 ARG ARG A . n 
A 1 520 VAL 520 520 520 VAL VAL A . n 
A 1 521 SER 521 521 521 SER SER A . n 
A 1 522 GLU 522 522 522 GLU GLU A . n 
A 1 523 ASN 523 523 523 ASN ASN A . n 
A 1 524 GLY 524 524 524 GLY GLY A . n 
A 1 525 LYS 525 525 525 LYS LYS A . n 
A 1 526 ARG 526 526 526 ARG ARG A . n 
A 1 527 PRO 527 527 527 PRO PRO A . n 
A 1 528 ASP 528 528 528 ASP ASP A . n 
A 1 529 HIS 529 529 529 HIS HIS A . n 
A 1 530 VAL 530 530 530 VAL VAL A . n 
A 1 531 ILE 531 531 531 ILE ILE A . n 
A 1 532 GLN 532 532 532 GLN GLN A . n 
A 1 533 ILE 533 533 533 ILE ILE A . n 
A 1 534 LEU 534 534 534 LEU LEU A . n 
A 1 535 ASP 535 535 535 ASP ASP A . n 
A 1 536 LEU 536 536 536 LEU LEU A . n 
A 1 537 PHE 537 537 537 PHE PHE A . n 
A 1 538 GLU 538 538 538 GLU GLU A . n 
A 1 539 LYS 539 539 539 LYS LYS A . n 
A 1 540 PRO 540 540 540 PRO PRO A . n 
A 1 541 LEU 541 541 541 LEU LEU A . n 
A 1 542 LEU 542 542 542 LEU LEU A . n 
A 1 543 LEU 543 543 543 LEU LEU A . n 
A 1 544 SER 544 544 544 SER SER A . n 
A 1 545 ILE 545 545 545 ILE ILE A . n 
A 1 546 VAL 546 546 546 VAL VAL A . n 
A 1 547 SER 547 547 547 SER SER A . n 
A 1 548 LYS 548 548 548 LYS LYS A . n 
A 1 549 GLU 549 549 549 GLU GLU A . n 
A 1 550 LYS 550 550 550 LYS LYS A . n 
A 1 551 PRO 551 551 551 PRO PRO A . n 
A 1 552 ASN 552 552 552 ASN ASN A . n 
A 1 553 ASP 553 553 553 ASP ASP A . n 
A 1 554 LEU 554 554 554 LEU LEU A . n 
A 1 555 GLU 555 555 555 GLU GLU A . n 
A 1 556 PRO 556 556 556 PRO PRO A . n 
A 1 557 LYS 557 557 557 LYS LYS A . n 
A 1 558 ILE 558 558 558 ILE ILE A . n 
A 1 559 GLY 559 559 559 GLY GLY A . n 
A 1 560 VAL 560 560 560 VAL VAL A . n 
A 1 561 GLN 561 561 561 GLN GLN A . n 
A 1 562 LEU 562 562 562 LEU LEU A . n 
A 1 563 ILE 563 563 563 ILE ILE A . n 
A 1 564 LYS 564 564 564 LYS LYS A . n 
A 1 565 TYR 565 565 565 TYR TYR A . n 
A 1 566 ILE 566 566 566 ILE ILE A . n 
A 1 567 GLU 567 567 567 GLU GLU A . n 
A 1 568 TYR 568 568 568 TYR TYR A . n 
A 1 569 LEU 569 569 569 LEU LEU A . n 
A 1 570 PHE 570 570 570 PHE PHE A . n 
A 1 571 ASP 571 571 571 ASP ASP A . n 
A 1 572 PHE 572 572 572 PHE PHE A . n 
A 1 573 THR 573 573 573 THR THR A . n 
A 1 574 PRO 574 574 574 PRO PRO A . n 
A 1 575 SER 575 575 575 SER SER A . n 
A 1 576 VAL 576 576 576 VAL VAL A . n 
A 1 577 GLN 577 577 577 GLN GLN A . n 
A 1 578 ARG 578 578 578 ARG ARG A . n 
A 1 579 LYS 579 579 579 LYS LYS A . n 
A 1 580 ILE 580 580 580 ILE ILE A . n 
A 1 581 ALA 581 581 581 ALA ALA A . n 
A 1 582 GLY 582 582 582 GLY GLY A . n 
A 1 583 GLY 583 583 583 GLY GLY A . n 
A 1 584 ASN 584 584 584 ASN ASN A . n 
A 1 585 TRP 585 585 585 TRP TRP A . n 
A 1 586 GLU 586 586 586 GLU GLU A . n 
A 1 587 PHE 587 587 587 PHE PHE A . n 
A 1 588 GLY 588 588 588 GLY GLY A . n 
A 1 589 ASN 589 589 589 ASN ASN A . n 
A 1 590 LYS 590 590 590 LYS LYS A . n 
A 1 591 SER 591 591 591 SER SER A . n 
A 1 592 LEU 592 592 592 LEU LEU A . n 
A 1 593 VAL 593 593 593 VAL VAL A . n 
A 1 594 PRO 594 594 594 PRO PRO A . n 
A 1 595 ASN 595 595 595 ASN ASN A . n 
A 1 596 ASP 596 596 596 ASP ASP A . n 
A 1 597 PHE 597 597 597 PHE PHE A . n 
A 1 598 ILE 598 598 598 ILE ILE A . n 
A 1 599 LEU 599 599 599 LEU LEU A . n 
A 1 600 LEU 600 600 600 LEU LEU A . n 
A 1 601 SER 601 601 601 SER SER A . n 
A 1 602 ALA 602 602 602 ALA ALA A . n 
A 1 603 GLY 603 603 603 GLY GLY A . n 
A 1 604 ALA 604 604 604 ALA ALA A . n 
A 1 605 PHE 605 605 605 PHE PHE A . n 
A 1 606 ILE 606 606 606 ILE ILE A . n 
A 1 607 ASP 607 607 607 ASP ASP A . n 
A 1 608 TYR 608 608 608 TYR TYR A . n 
A 1 609 ASP 609 609 609 ASP ASP A . n 
A 1 610 ASN 610 610 610 ASN ASN A . n 
A 1 611 LEU 611 611 611 LEU LEU A . n 
A 1 612 THR 612 612 612 THR THR A . n 
A 1 613 GLU 613 613 613 GLU GLU A . n 
A 1 614 ASN 614 614 614 ASN ASN A . n 
A 1 615 ASP 615 615 615 ASP ASP A . n 
A 1 616 TYR 616 616 616 TYR TYR A . n 
A 1 617 GLU 617 617 617 GLU GLU A . n 
A 1 618 LYS 618 618 618 LYS LYS A . n 
A 1 619 ILE 619 619 619 ILE ILE A . n 
A 1 620 PHE 620 620 620 PHE PHE A . n 
A 1 621 GLU 621 621 621 GLU GLU A . n 
A 1 622 VAL 622 622 622 VAL VAL A . n 
A 1 623 THR 623 623 623 THR THR A . n 
A 1 624 GLY 624 624 624 GLY GLY A . n 
A 1 625 CYS 625 625 625 CYS CYS A . n 
A 1 626 ASP 626 626 626 ASP ASP A . n 
A 1 627 LEU 627 627 627 LEU LEU A . n 
A 1 628 LEU 628 628 628 LEU LEU A . n 
A 1 629 ILE 629 629 629 ILE ILE A . n 
A 1 630 ALA 630 630 630 ALA ALA A . n 
A 1 631 ILE 631 631 631 ILE ILE A . n 
A 1 632 LYS 632 632 632 LYS LYS A . n 
A 1 633 ASN 633 633 633 ASN ASN A . n 
A 1 634 GLN 634 634 634 GLN GLN A . n 
A 1 635 ASN 635 635 635 ASN ASN A . n 
A 1 636 ASN 636 636 636 ASN ASN A . n 
A 1 637 PRO 637 637 637 PRO PRO A . n 
A 1 638 GLN 638 638 638 GLN GLN A . n 
A 1 639 LYS 639 639 639 LYS LYS A . n 
A 1 640 TRP 640 640 640 TRP TRP A . n 
A 1 641 VAL 641 641 641 VAL VAL A . n 
A 1 642 ILE 642 642 642 ILE ILE A . n 
A 1 643 LYS 643 643 643 LYS LYS A . n 
A 1 644 PHE 644 644 644 PHE PHE A . n 
A 1 645 LYS 645 645 645 LYS LYS A . n 
A 1 646 PRO 646 646 646 PRO PRO A . n 
A 1 647 LYS 647 647 647 LYS LYS A . n 
A 1 648 ASN 648 648 648 ASN ASN A . n 
A 1 649 THR 649 649 649 THR THR A . n 
A 1 650 ILE 650 650 650 ILE ILE A . n 
A 1 651 ALA 651 651 651 ALA ALA A . n 
A 1 652 GLU 652 652 652 GLU GLU A . n 
A 1 653 LYS 653 653 653 LYS LYS A . n 
A 1 654 LEU 654 654 654 LEU LEU A . n 
A 1 655 VAL 655 655 655 VAL VAL A . n 
A 1 656 ASN 656 656 656 ASN ASN A . n 
A 1 657 TYR 657 657 657 TYR TYR A . n 
A 1 658 ILE 658 658 658 ILE ILE A . n 
A 1 659 LYS 659 659 659 LYS LYS A . n 
A 1 660 LEU 660 660 660 LEU LEU A . n 
A 1 661 ASN 661 661 661 ASN ASN A . n 
A 1 662 PHE 662 662 662 PHE PHE A . n 
A 1 663 LYS 663 663 663 LYS LYS A . n 
A 1 664 SER 664 664 664 SER SER A . n 
A 1 665 ASN 665 665 665 ASN ASN A . n 
A 1 666 ILE 666 666 666 ILE ILE A . n 
A 1 667 PHE 667 667 667 PHE PHE A . n 
A 1 668 ASP 668 668 668 ASP ASP A . n 
A 1 669 THR 669 669 669 THR THR A . n 
A 1 670 GLY 670 670 670 GLY GLY A . n 
A 1 671 PHE 671 671 671 PHE PHE A . n 
A 1 672 PHE 672 672 672 PHE PHE A . n 
A 1 673 HIS 673 673 673 HIS HIS A . n 
A 1 674 ILE 674 674 674 ILE ILE A . n 
A 1 675 GLU 675 675 675 GLU GLU A . n 
A 1 676 GLY 676 676 676 GLY GLY A . n 
B 2 1   DC  1   1   1   DC  DC  E . n 
B 2 2   DA  2   2   2   DA  DA  E . n 
B 2 3   DT  3   3   3   DT  DT  E . n 
B 2 4   DT  4   4   4   DT  DT  E . n 
B 2 5   DC  5   5   5   DC  DC  E . n 
B 2 6   DC  6   6   6   DC  DC  E . n 
B 2 7   DT  7   7   7   DT  DT  E . n 
B 2 8   DC  8   8   8   DC  DC  E . n 
C 3 1   DG  1   1   1   DG  DG  F . n 
C 3 2   DA  2   2   2   DA  DA  F . n 
C 3 3   DG  3   3   3   DG  DG  F . n 
C 3 4   DG  4   4   4   DG  DG  F . n 
C 3 5   DA  5   5   5   DA  DA  F . n 
C 3 6   DA  6   6   6   DA  DA  F . n 
C 3 7   DT  7   7   7   DT  DT  F . n 
C 3 8   DG  8   8   8   DG  DG  F . n 
C 3 9   DC  9   9   9   DC  DC  F . n 
C 3 10  DA  10  10  10  DA  DA  F . n 
C 3 11  DG  11  11  11  DG  DG  F . n 
C 3 12  DA  12  12  12  DA  DA  F . n 
C 3 13  DC  13  13  13  DC  DC  F . n 
D 4 1   DG  1   1   1   DG  DG  G . n 
D 4 2   DT  2   2   2   DT  DT  G . n 
D 4 3   DC  3   3   3   DC  DC  G . n 
D 4 4   DT  4   4   4   DT  DT  G . n 
D 4 5   DG  5   5   5   DG  DG  G . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        MG 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   MG 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 5 MG  1  701 1  MG  MG  A . 
F 6 CL  1  702 1  CL  CL  A . 
G 7 MES 1  703 1  MES MES A . 
H 8 HOH 1  801 34 HOH HOH A . 
H 8 HOH 2  802 50 HOH HOH A . 
H 8 HOH 3  803 3  HOH HOH A . 
H 8 HOH 4  804 9  HOH HOH A . 
H 8 HOH 5  805 1  HOH HOH A . 
H 8 HOH 6  806 47 HOH HOH A . 
H 8 HOH 7  807 11 HOH HOH A . 
H 8 HOH 8  808 33 HOH HOH A . 
H 8 HOH 9  809 36 HOH HOH A . 
H 8 HOH 10 810 37 HOH HOH A . 
H 8 HOH 11 811 39 HOH HOH A . 
H 8 HOH 12 812 30 HOH HOH A . 
H 8 HOH 13 813 4  HOH HOH A . 
H 8 HOH 14 814 24 HOH HOH A . 
H 8 HOH 15 815 21 HOH HOH A . 
H 8 HOH 16 816 25 HOH HOH A . 
H 8 HOH 17 817 38 HOH HOH A . 
H 8 HOH 18 818 16 HOH HOH A . 
H 8 HOH 19 819 40 HOH HOH A . 
H 8 HOH 20 820 7  HOH HOH A . 
H 8 HOH 21 821 45 HOH HOH A . 
H 8 HOH 22 822 20 HOH HOH A . 
H 8 HOH 23 823 15 HOH HOH A . 
H 8 HOH 24 824 17 HOH HOH A . 
H 8 HOH 25 825 44 HOH HOH A . 
H 8 HOH 26 826 19 HOH HOH A . 
H 8 HOH 27 827 48 HOH HOH A . 
H 8 HOH 28 828 14 HOH HOH A . 
H 8 HOH 29 829 5  HOH HOH A . 
H 8 HOH 30 830 27 HOH HOH A . 
H 8 HOH 31 831 42 HOH HOH A . 
H 8 HOH 32 832 28 HOH HOH A . 
H 8 HOH 33 833 43 HOH HOH A . 
H 8 HOH 34 834 2  HOH HOH A . 
H 8 HOH 35 835 8  HOH HOH A . 
H 8 HOH 36 836 22 HOH HOH A . 
H 8 HOH 37 837 35 HOH HOH A . 
H 8 HOH 38 838 29 HOH HOH A . 
H 8 HOH 39 839 10 HOH HOH A . 
H 8 HOH 40 840 13 HOH HOH A . 
H 8 HOH 41 841 31 HOH HOH A . 
H 8 HOH 42 842 41 HOH HOH A . 
H 8 HOH 43 843 32 HOH HOH A . 
H 8 HOH 44 844 12 HOH HOH A . 
H 8 HOH 45 845 26 HOH HOH A . 
I 8 HOH 1  101 49 HOH HOH F . 
I 8 HOH 2  102 51 HOH HOH F . 
I 8 HOH 3  103 6  HOH HOH F . 
I 8 HOH 4  104 18 HOH HOH F . 
J 8 HOH 1  101 46 HOH HOH G . 
J 8 HOH 2  102 23 HOH HOH G . 
# 
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 TYR 87  ? CG    ? A TYR 87  CG    
2  1 Y 1 A TYR 87  ? CD1   ? A TYR 87  CD1   
3  1 Y 1 A TYR 87  ? CD2   ? A TYR 87  CD2   
4  1 Y 1 A TYR 87  ? CE1   ? A TYR 87  CE1   
5  1 Y 1 A TYR 87  ? CE2   ? A TYR 87  CE2   
6  1 Y 1 A TYR 87  ? CZ    ? A TYR 87  CZ    
7  1 Y 1 A TYR 87  ? OH    ? A TYR 87  OH    
8  1 Y 1 A ARG 123 ? CG    ? A ARG 123 CG    
9  1 Y 1 A ARG 123 ? CD    ? A ARG 123 CD    
10 1 Y 1 A ARG 123 ? NE    ? A ARG 123 NE    
11 1 Y 1 A ARG 123 ? CZ    ? A ARG 123 CZ    
12 1 Y 1 A ARG 123 ? NH1   ? A ARG 123 NH1   
13 1 Y 1 A ARG 123 ? NH2   ? A ARG 123 NH2   
14 1 Y 1 A ASP 249 ? CG    ? A ASP 249 CG    
15 1 Y 1 A ASP 249 ? OD1   ? A ASP 249 OD1   
16 1 Y 1 A ASP 249 ? OD2   ? A ASP 249 OD2   
17 1 Y 1 A GLU 341 ? CG    ? A GLU 341 CG    
18 1 Y 1 A GLU 341 ? CD    ? A GLU 341 CD    
19 1 Y 1 A GLU 341 ? OE1   ? A GLU 341 OE1   
20 1 Y 1 A GLU 341 ? OE2   ? A GLU 341 OE2   
21 1 Y 1 A GLU 447 ? CG    ? A GLU 447 CG    
22 1 Y 1 A GLU 447 ? CD    ? A GLU 447 CD    
23 1 Y 1 A GLU 447 ? OE1   ? A GLU 447 OE1   
24 1 Y 1 A GLU 447 ? OE2   ? A GLU 447 OE2   
25 1 Y 1 A TRP 500 ? CG    ? A TRP 500 CG    
26 1 Y 1 A TRP 500 ? CD1   ? A TRP 500 CD1   
27 1 Y 1 A TRP 500 ? CD2   ? A TRP 500 CD2   
28 1 Y 1 A TRP 500 ? NE1   ? A TRP 500 NE1   
29 1 Y 1 A TRP 500 ? CE2   ? A TRP 500 CE2   
30 1 Y 1 A TRP 500 ? CE3   ? A TRP 500 CE3   
31 1 Y 1 A TRP 500 ? CZ2   ? A TRP 500 CZ2   
32 1 Y 1 A TRP 500 ? CZ3   ? A TRP 500 CZ3   
33 1 Y 1 A TRP 500 ? CH2   ? A TRP 500 CH2   
34 1 Y 1 G DG  1   ? "O5'" ? D DG  1   "O5'" 
# 
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                     9EZD 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     98.213 
_cell.length_a_esd                 ? 
_cell.length_b                     130.419 
_cell.length_b_esd                 ? 
_cell.length_c                     62.542 
_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                         9EZD 
_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                   9EZD 
_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             2.35 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.72 
_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              6.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;100 mM MES pH6.5
100 mM MgCl2
25% PEG400
35% Guanidine HCl
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-09-23 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97856 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SOLEIL BEAMLINE PROXIMA 1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97856 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'PROXIMA 1' 
_diffrn_source.pdbx_synchrotron_site       SOLEIL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9EZD 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.635 
_reflns.d_resolution_low                               78.455 
_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                                     12735 
_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                           91.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                11.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.546 
_reflns.pdbx_Rpim_I_all                                0.162 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.985 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.520 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.635 
_reflns_shell.d_res_low                                     2.957 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             637 
_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                               9.7 
_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                               2.577 
_reflns_shell.pdbx_Rpim_I_all                               0.820 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.433 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          65.7 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  2.439 
_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]                            1.4282 
_refine.aniso_B[1][2]                            0 
_refine.aniso_B[1][3]                            0 
_refine.aniso_B[2][2]                            -1.7398 
_refine.aniso_B[2][3]                            0 
_refine.aniso_B[3][3]                            0.3116 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               41.31 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.885 
_refine.correlation_coeff_Fo_to_Fc_free          0.857 
_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                                 9EZD 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.635 
_refine.ls_d_res_low                             78.45 
_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                     12735 
_refine.ls_number_reflns_R_free                  653 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    52.1 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2205 
_refine.ls_R_factor_R_free                       0.2516 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2188 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.557 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_analyze.entry_id                        9EZD 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.4 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.635 
_refine_hist.d_res_low                        78.45 
_refine_hist.number_atoms_solvent             51 
_refine_hist.number_atoms_total               6013 
_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        5422 
_refine_hist.pdbx_number_atoms_nucleic_acid   526 
_refine_hist.pdbx_number_atoms_ligand         14 
_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' ? 0.007 ? 6145 ? t_bond_d                  2  HARMONIC     
'X-RAY DIFFRACTION' ? 0.87  ? 8408 ? t_angle_deg               2  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 2098 ? t_dihedral_angle_d        2  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? 965  ? t_gen_planes              5  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 6145 ? t_it                      10 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 798  ? t_chiral_improper_torsion 5  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? 4502 ? t_ideal_dist_contact      4  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? 2.95  ? ?    ? t_omega_torsion           ?  ?            
'X-RAY DIFFRACTION' ? 19.14 ? ?    ? t_other_torsion           ?  ?            
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.635 
_refine_ls_shell.d_res_low                        2.89 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             26 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.percent_reflns_obs               6.94 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2961 
_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                  0.3107 
# 
_struct.entry_id                     9EZD 
_struct.title                        
'BsmI (Bottom Nicking mutant) crystallized with Mg2+ and cognate dsDNA (Post-reactive complex)' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9EZD 
_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 7 ? 
H N N 8 ? 
I N N 8 ? 
J N N 8 ? 
# 
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 9EZD         9EZD   ? 2 ? 1 
3 PDB 9EZD         9EZD   ? 3 ? 1 
4 PDB 9EZD         9EZD   ? 4 ? 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 9EZD A 1 ? 676 ? Q8RLN4 1 ? 676 ? 1 676 
2 2 9EZD E 1 ? 8   ? 9EZD   1 ? 8   ? 1 8   
3 3 9EZD F 1 ? 13  ? 9EZD   1 ? 13  ? 1 13  
4 4 9EZD G 1 ? 5   ? 9EZD   1 ? 5   ? 1 5   
# 
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 9EZD ASP A 507 ? UNP Q8RLN4 ARG 507 'engineered mutation' 507 1 
1 9EZD VAL A 509 ? UNP Q8RLN4 GLY 509 'engineered mutation' 509 2 
1 9EZD VAL A 546 ? UNP Q8RLN4 GLU 546 'engineered mutation' 546 3 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_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                'Analyticial 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]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 ASP A 195 ? LYS A 199 ? ASP A 195 LYS A 199 5 ? 5  
HELX_P HELX_P7  AA7 ASP A 202 ? PHE A 206 ? ASP A 202 PHE A 206 5 ? 5  
HELX_P HELX_P8  AA8 ALA A 207 ? GLN A 220 ? ALA A 207 GLN A 220 1 ? 14 
HELX_P HELX_P9  AA9 THR A 224 ? LYS A 244 ? THR A 224 LYS A 244 1 ? 21 
HELX_P HELX_P10 AB1 THR A 253 ? ASN A 262 ? THR A 253 ASN A 262 1 ? 10 
HELX_P HELX_P11 AB2 ALA A 283 ? LEU A 287 ? ALA A 283 LEU A 287 5 ? 5  
HELX_P HELX_P12 AB3 LYS A 290 ? SER A 302 ? LYS A 290 SER A 302 1 ? 13 
HELX_P HELX_P13 AB4 ARG A 316 ? ASN A 332 ? ARG A 316 ASN A 332 1 ? 17 
HELX_P HELX_P14 AB5 ASP A 335 ? LYS A 343 ? ASP A 335 LYS A 343 1 ? 9  
HELX_P HELX_P15 AB6 ARG A 364 ? ARG A 367 ? ARG A 364 ARG A 367 5 ? 4  
HELX_P HELX_P16 AB7 GLY A 368 ? GLY A 378 ? GLY A 368 GLY A 378 1 ? 11 
HELX_P HELX_P17 AB8 ILE A 392 ? ASP A 402 ? ILE A 392 ASP A 402 1 ? 11 
HELX_P HELX_P18 AB9 ASP A 402 ? ASN A 410 ? ASP A 402 ASN A 410 1 ? 9  
HELX_P HELX_P19 AC1 ASN A 410 ? SER A 420 ? ASN A 410 SER A 420 1 ? 11 
HELX_P HELX_P20 AC2 ASN A 442 ? LEU A 450 ? ASN A 442 LEU A 450 1 ? 9  
HELX_P HELX_P21 AC3 GLN A 469 ? TYR A 483 ? GLN A 469 TYR A 483 1 ? 15 
HELX_P HELX_P22 AC4 LYS A 550 ? LEU A 554 ? LYS A 550 LEU A 554 5 ? 5  
HELX_P HELX_P23 AC5 LYS A 557 ? ASP A 571 ? LYS A 557 ASP A 571 1 ? 15 
HELX_P HELX_P24 AC6 VAL A 593 ? PHE A 597 ? VAL A 593 PHE A 597 5 ? 5  
HELX_P HELX_P25 AC7 THR A 612 ? GLY A 624 ? THR A 612 GLY A 624 1 ? 13 
HELX_P HELX_P26 AC8 ASN A 648 ? ASN A 661 ? ASN A 648 ASN A 661 1 ? 14 
HELX_P HELX_P27 AC9 ASP A 668 ? GLY A 670 ? ASP A 668 GLY A 670 5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A ASP 91  OD1 ? ? ? 1_555 E MG . MG ? ? A ASP 91  A MG 701 1_555 ? ? ? ? ? ? ?            1.921 ? ? 
metalc2  metalc ? ? A ASP 91  OD2 ? ? ? 1_555 E MG . MG ? ? A ASP 91  A MG 701 1_555 ? ? ? ? ? ? ?            2.379 ? ? 
metalc3  metalc ? ? A GLU 109 OE1 ? ? ? 1_555 E MG . MG ? ? A GLU 109 A MG 701 1_555 ? ? ? ? ? ? ?            1.941 ? ? 
metalc4  metalc ? ? A GLU 109 OE2 ? ? ? 1_555 E MG . MG ? ? A GLU 109 A MG 701 1_555 ? ? ? ? ? ? ?            1.961 ? ? 
hydrog1  hydrog ? ? B DC  1   N3  ? ? ? 1_555 C DG 8 N1 ? ? E DC  1   F DG 8   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog2  hydrog ? ? B DC  1   N4  ? ? ? 1_555 C DG 8 O6 ? ? E DC  1   F DG 8   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog3  hydrog ? ? B DC  1   O2  ? ? ? 1_555 C DG 8 N2 ? ? E DC  1   F DG 8   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog4  hydrog ? ? B DA  2   N1  ? ? ? 1_555 C DT 7 N3 ? ? E DA  2   F DT 7   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog5  hydrog ? ? B DA  2   N6  ? ? ? 1_555 C DT 7 O4 ? ? E DA  2   F DT 7   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog6  hydrog ? ? B DT  3   N3  ? ? ? 1_555 C DA 6 N1 ? ? E DT  3   F DA 6   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog7  hydrog ? ? B DT  3   O4  ? ? ? 1_555 C DA 6 N6 ? ? E DT  3   F DA 6   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog8  hydrog ? ? B DT  4   N3  ? ? ? 1_555 C DA 5 N1 ? ? E DT  4   F DA 5   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog9  hydrog ? ? B DT  4   O4  ? ? ? 1_555 C DA 5 N6 ? ? E DT  4   F DA 5   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog10 hydrog ? ? B DC  5   N3  ? ? ? 1_555 C DG 4 N1 ? ? E DC  5   F DG 4   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog11 hydrog ? ? B DC  5   N4  ? ? ? 1_555 C DG 4 O6 ? ? E DC  5   F DG 4   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog12 hydrog ? ? B DC  5   O2  ? ? ? 1_555 C DG 4 N2 ? ? E DC  5   F DG 4   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog13 hydrog ? ? B DC  6   N3  ? ? ? 1_555 C DG 3 N1 ? ? E DC  6   F DG 3   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog14 hydrog ? ? B DC  6   N4  ? ? ? 1_555 C DG 3 O6 ? ? E DC  6   F DG 3   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog15 hydrog ? ? B DC  6   O2  ? ? ? 1_555 C DG 3 N2 ? ? E DC  6   F DG 3   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog16 hydrog ? ? B DT  7   N3  ? ? ? 1_555 C DA 2 N1 ? ? E DT  7   F DA 2   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog17 hydrog ? ? B DT  7   O4  ? ? ? 1_555 C DA 2 N6 ? ? E DT  7   F DA 2   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog18 hydrog ? ? B DC  8   N3  ? ? ? 1_555 C DG 1 N1 ? ? E DC  8   F DG 1   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog19 hydrog ? ? B DC  8   N4  ? ? ? 1_555 C DG 1 O6 ? ? E DC  8   F DG 1   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog20 hydrog ? ? B DC  8   O2  ? ? ? 1_555 C DG 1 N2 ? ? E DC  8   F DG 1   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog21 hydrog ? ? C DC  9   N3  ? ? ? 1_555 D DG 5 N1 ? ? F DC  9   G DG 5   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog22 hydrog ? ? C DC  9   N4  ? ? ? 1_555 D DG 5 O6 ? ? F DC  9   G DG 5   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog23 hydrog ? ? C DC  9   O2  ? ? ? 1_555 D DG 5 N2 ? ? F DC  9   G DG 5   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog24 hydrog ? ? C DA  10  N1  ? ? ? 1_555 D DT 4 N3 ? ? F DA  10  G DT 4   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog25 hydrog ? ? C DA  10  N6  ? ? ? 1_555 D DT 4 O4 ? ? F DA  10  G DT 4   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog26 hydrog ? ? C DG  11  N1  ? ? ? 1_555 D DC 3 N3 ? ? F DG  11  G DC 3   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog27 hydrog ? ? C DG  11  N2  ? ? ? 1_555 D DC 3 O2 ? ? F DG  11  G DC 3   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog28 hydrog ? ? C DG  11  O6  ? ? ? 1_555 D DC 3 N4 ? ? F DG  11  G DC 3   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog29 hydrog ? ? C DA  12  N1  ? ? ? 1_555 D DT 2 N3 ? ? F DA  12  G DT 2   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog30 hydrog ? ? C DA  12  N6  ? ? ? 1_555 D DT 2 O4 ? ? F DA  12  G DT 2   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog31 hydrog ? ? C DC  13  N3  ? ? ? 1_555 D DG 1 N1 ? ? F DC  13  G DG 1   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog32 hydrog ? ? C DC  13  N4  ? ? ? 1_555 D DG 1 O6 ? ? F DC  13  G DG 1   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog33 hydrog ? ? C DC  13  O2  ? ? ? 1_555 D DG 1 N2 ? ? F DC  13  G DG 1   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
metalc ? ? 
hydrog ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 OD1 ? A ASP 91  ? A ASP 91  ? 1_555 MG ? E MG . ? A MG 701 ? 1_555 OD2 ? A ASP 91  ? A ASP 91  ? 1_555 60.5  ? 
2 OD1 ? A ASP 91  ? A ASP 91  ? 1_555 MG ? E MG . ? A MG 701 ? 1_555 OE1 ? A GLU 109 ? A GLU 109 ? 1_555 157.2 ? 
3 OD2 ? A ASP 91  ? A ASP 91  ? 1_555 MG ? E MG . ? A MG 701 ? 1_555 OE1 ? A GLU 109 ? A GLU 109 ? 1_555 140.4 ? 
4 OD1 ? A ASP 91  ? A ASP 91  ? 1_555 MG ? E MG . ? A MG 701 ? 1_555 OE2 ? A GLU 109 ? A GLU 109 ? 1_555 126.4 ? 
5 OD2 ? A ASP 91  ? A ASP 91  ? 1_555 MG ? E MG . ? A MG 701 ? 1_555 OE2 ? A GLU 109 ? A GLU 109 ? 1_555 95.4  ? 
6 OE1 ? A GLU 109 ? A GLU 109 ? 1_555 MG ? E MG . ? A MG 701 ? 1_555 OE2 ? A GLU 109 ? A GLU 109 ? 1_555 68.8  ? 
# 
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 -1.01 
2 ASN 636 A . ? ASN 636 A PRO 637 A ? PRO 637 A 1 -4.15 
# 
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 303 ? GLY A 304 ? VAL A 303 GLY A 304 
AA2 2 PHE A 312 ? ILE A 315 ? PHE A 312 ILE A 315 
AA2 3 LEU A 348 ? LEU A 353 ? LEU A 348 LEU A 353 
AA2 4 GLN A 382 ? ILE A 387 ? GLN A 382 ILE A 387 
AA2 5 PHE A 422 ? PRO A 428 ? PHE A 422 PRO A 428 
AA2 6 ASN A 435 ? ILE A 441 ? ASN A 435 ILE A 441 
AA3 1 GLY A 498 ? ASP A 499 ? GLY A 498 ASP A 499 
AA3 2 GLY A 502 ? ILE A 506 ? GLY A 502 ILE A 506 
AA3 3 HIS A 510 ? LEU A 515 ? HIS A 510 LEU A 515 
AA3 4 VAL A 576 ? LYS A 579 ? VAL A 576 LYS A 579 
AA3 5 GLU A 586 ? PHE A 587 ? GLU A 586 PHE A 587 
AA4 1 HIS A 529 ? ILE A 533 ? HIS A 529 ILE A 533 
AA4 2 LEU A 541 ? SER A 547 ? LEU A 541 SER A 547 
AA4 3 ILE A 598 ? ILE A 606 ? ILE A 598 ILE A 606 
AA4 4 LEU A 627 ? GLN A 634 ? LEU A 627 GLN A 634 
AA4 5 LYS A 639 ? PRO A 646 ? LYS A 639 PRO A 646 
AA4 6 PHE A 672 ? GLY A 676 ? PHE A 672 GLY A 676 
# 
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 HIS A 7   ? N HIS A 7   O ILE A 93  ? O ILE A 93  
AA1 5 6 N ILE A 94  ? N ILE A 94  O LEU A 105 ? O LEU A 105 
AA1 6 7 N GLU A 109 ? N GLU 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 303 ? N VAL A 303 O VAL A 314 ? O VAL A 314 
AA2 2 3 N ILE A 315 ? N ILE A 315 O LEU A 348 ? O LEU A 348 
AA2 3 4 N CYS A 351 ? N CYS A 351 O PHE A 386 ? O PHE A 386 
AA2 4 5 N THR A 385 ? N THR A 385 O VAL A 424 ? O VAL A 424 
AA2 5 6 N ILE A 423 ? N ILE A 423 O ILE A 440 ? O ILE A 440 
AA3 1 2 N ASP A 499 ? N ASP A 499 O GLY A 502 ? O GLY A 502 
AA3 2 3 N ILE A 505 ? N ILE A 505 O PHE A 512 ? O PHE A 512 
AA3 3 4 N ARG A 513 ? N ARG A 513 O VAL A 576 ? O VAL A 576 
AA3 4 5 N GLN A 577 ? N GLN A 577 O GLU A 586 ? O GLU A 586 
AA4 1 2 N HIS A 529 ? N HIS A 529 O ILE A 545 ? O ILE A 545 
AA4 2 3 N LEU A 542 ? N LEU A 542 O ILE A 598 ? O ILE A 598 
AA4 3 4 N PHE A 605 ? N PHE A 605 O ILE A 631 ? O ILE A 631 
AA4 4 5 N LEU A 628 ? N LEU A 628 O LYS A 645 ? O LYS A 645 
AA4 5 6 N PHE A 644 ? N PHE A 644 O GLY A 676 ? O GLY A 676 
# 
_pdbx_entry_details.entry_id                   9EZD 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             "O4'" 
_pdbx_validate_rmsd_angle.auth_asym_id_1             F 
_pdbx_validate_rmsd_angle.auth_comp_id_1             DG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              3 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             "C1'" 
_pdbx_validate_rmsd_angle.auth_asym_id_2             F 
_pdbx_validate_rmsd_angle.auth_comp_id_2             DG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              3 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             N9 
_pdbx_validate_rmsd_angle.auth_asym_id_3             F 
_pdbx_validate_rmsd_angle.auth_comp_id_3             DG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                110.28 
_pdbx_validate_rmsd_angle.angle_target_value         108.30 
_pdbx_validate_rmsd_angle.angle_deviation            1.98 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.30 
_pdbx_validate_rmsd_angle.linker_flag                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 GLU A 48  ? ? -112.76 73.51   
2 1 ALA A 306 ? ? 74.71   -48.78  
3 1 ASP A 402 ? ? -162.95 96.01   
4 1 GLN A 469 ? ? -139.49 -158.84 
5 1 ASP A 507 ? ? -130.17 -152.32 
6 1 ASP A 535 ? ? -104.09 40.37   
7 1 ASN A 584 ? ? 63.55   117.72  
# 
_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         16.3696 
_pdbx_refine_tls.origin_y         22.2859 
_pdbx_refine_tls.origin_z         10.5333 
_pdbx_refine_tls.T[1][1]          -0.0676 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0157 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0301 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          -0.1185 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0045 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.0997 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.2134 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.0951 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.2187 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.4664 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.1969 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.2851 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0335 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0289 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0494 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0289 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0239 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0351 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0494 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0351 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0095 
_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 ? ? B 1 ? ? ? B 1   ? ? '{ *|* }' 
3 'X-RAY DIFFRACTION' 1 ? ? C 1 ? ? ? C 1   ? ? '{ *|* }' 
4 'X-RAY DIFFRACTION' 1 ? ? E 1 ? ? ? E 8   ? ? '{ *|* }' 
5 'X-RAY DIFFRACTION' 1 ? ? F 1 ? ? ? F 13  ? ? '{ *|* }' 
6 'X-RAY DIFFRACTION' 1 ? ? G 1 ? ? ? G 5   ? ? '{ *|* }' 
7 'X-RAY DIFFRACTION' 1 ? ? L 1 ? ? ? L 1   ? ? '{ *|* }' 
8 'X-RAY DIFFRACTION' 1 ? ? W 1 ? ? ? W 51  ? ? '{ *|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A ASN 66  ? A ASN 66  
2 1 Y 1 A THR 67  ? A THR 67  
3 1 Y 1 A ASN 487 ? A ASN 487 
4 1 Y 1 A CYS 488 ? A CYS 488 
5 1 Y 1 A PHE 489 ? A PHE 489 
6 1 Y 1 A SER 490 ? A SER 490 
7 1 Y 1 A GLY 491 ? A GLY 491 
8 1 Y 1 A MET 492 ? A MET 492 
9 1 Y 1 A CYS 493 ? A CYS 493 
# 
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 
MG  MG     MG N N 419 
PHE N      N  N N 420 
PHE CA     C  N S 421 
PHE C      C  N N 422 
PHE O      O  N N 423 
PHE CB     C  N N 424 
PHE CG     C  Y N 425 
PHE CD1    C  Y N 426 
PHE CD2    C  Y N 427 
PHE CE1    C  Y N 428 
PHE CE2    C  Y N 429 
PHE CZ     C  Y N 430 
PHE OXT    O  N N 431 
PHE H      H  N N 432 
PHE H2     H  N N 433 
PHE HA     H  N N 434 
PHE HB2    H  N N 435 
PHE HB3    H  N N 436 
PHE HD1    H  N N 437 
PHE HD2    H  N N 438 
PHE HE1    H  N N 439 
PHE HE2    H  N N 440 
PHE HZ     H  N N 441 
PHE HXT    H  N N 442 
PRO N      N  N N 443 
PRO CA     C  N S 444 
PRO C      C  N N 445 
PRO O      O  N N 446 
PRO CB     C  N N 447 
PRO CG     C  N N 448 
PRO CD     C  N N 449 
PRO OXT    O  N N 450 
PRO H      H  N N 451 
PRO HA     H  N N 452 
PRO HB2    H  N N 453 
PRO HB3    H  N N 454 
PRO HG2    H  N N 455 
PRO HG3    H  N N 456 
PRO HD2    H  N N 457 
PRO HD3    H  N N 458 
PRO HXT    H  N N 459 
SER N      N  N N 460 
SER CA     C  N S 461 
SER C      C  N N 462 
SER O      O  N N 463 
SER CB     C  N N 464 
SER OG     O  N N 465 
SER OXT    O  N N 466 
SER H      H  N N 467 
SER H2     H  N N 468 
SER HA     H  N N 469 
SER HB2    H  N N 470 
SER HB3    H  N N 471 
SER HG     H  N N 472 
SER HXT    H  N N 473 
THR N      N  N N 474 
THR CA     C  N S 475 
THR C      C  N N 476 
THR O      O  N N 477 
THR CB     C  N R 478 
THR OG1    O  N N 479 
THR CG2    C  N N 480 
THR OXT    O  N N 481 
THR H      H  N N 482 
THR H2     H  N N 483 
THR HA     H  N N 484 
THR HB     H  N N 485 
THR HG1    H  N N 486 
THR HG21   H  N N 487 
THR HG22   H  N N 488 
THR HG23   H  N N 489 
THR HXT    H  N N 490 
TRP N      N  N N 491 
TRP CA     C  N S 492 
TRP C      C  N N 493 
TRP O      O  N N 494 
TRP CB     C  N N 495 
TRP CG     C  Y N 496 
TRP CD1    C  Y N 497 
TRP CD2    C  Y N 498 
TRP NE1    N  Y N 499 
TRP CE2    C  Y N 500 
TRP CE3    C  Y N 501 
TRP CZ2    C  Y N 502 
TRP CZ3    C  Y N 503 
TRP CH2    C  Y N 504 
TRP OXT    O  N N 505 
TRP H      H  N N 506 
TRP H2     H  N N 507 
TRP HA     H  N N 508 
TRP HB2    H  N N 509 
TRP HB3    H  N N 510 
TRP HD1    H  N N 511 
TRP HE1    H  N N 512 
TRP HE3    H  N N 513 
TRP HZ2    H  N N 514 
TRP HZ3    H  N N 515 
TRP HH2    H  N N 516 
TRP HXT    H  N N 517 
TYR N      N  N N 518 
TYR CA     C  N S 519 
TYR C      C  N N 520 
TYR O      O  N N 521 
TYR CB     C  N N 522 
TYR CG     C  Y N 523 
TYR CD1    C  Y N 524 
TYR CD2    C  Y N 525 
TYR CE1    C  Y N 526 
TYR CE2    C  Y N 527 
TYR CZ     C  Y N 528 
TYR OH     O  N N 529 
TYR OXT    O  N N 530 
TYR H      H  N N 531 
TYR H2     H  N N 532 
TYR HA     H  N N 533 
TYR HB2    H  N N 534 
TYR HB3    H  N N 535 
TYR HD1    H  N N 536 
TYR HD2    H  N N 537 
TYR HE1    H  N N 538 
TYR HE2    H  N N 539 
TYR HH     H  N N 540 
TYR HXT    H  N N 541 
VAL N      N  N N 542 
VAL CA     C  N S 543 
VAL C      C  N N 544 
VAL O      O  N N 545 
VAL CB     C  N N 546 
VAL CG1    C  N N 547 
VAL CG2    C  N N 548 
VAL OXT    O  N N 549 
VAL H      H  N N 550 
VAL H2     H  N N 551 
VAL HA     H  N N 552 
VAL HB     H  N N 553 
VAL HG11   H  N N 554 
VAL HG12   H  N N 555 
VAL HG13   H  N N 556 
VAL HG21   H  N N 557 
VAL HG22   H  N N 558 
VAL HG23   H  N N 559 
VAL HXT    H  N N 560 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
DA  OP3   P      sing N N 83  
DA  OP3   HOP3   sing N N 84  
DA  P     OP1    doub N N 85  
DA  P     OP2    sing N N 86  
DA  P     "O5'"  sing N N 87  
DA  OP2   HOP2   sing N N 88  
DA  "O5'" "C5'"  sing N N 89  
DA  "C5'" "C4'"  sing N N 90  
DA  "C5'" "H5'"  sing N N 91  
DA  "C5'" "H5''" sing N N 92  
DA  "C4'" "O4'"  sing N N 93  
DA  "C4'" "C3'"  sing N N 94  
DA  "C4'" "H4'"  sing N N 95  
DA  "O4'" "C1'"  sing N N 96  
DA  "C3'" "O3'"  sing N N 97  
DA  "C3'" "C2'"  sing N N 98  
DA  "C3'" "H3'"  sing N N 99  
DA  "O3'" "HO3'" sing N N 100 
DA  "C2'" "C1'"  sing N N 101 
DA  "C2'" "H2'"  sing N N 102 
DA  "C2'" "H2''" sing N N 103 
DA  "C1'" N9     sing N N 104 
DA  "C1'" "H1'"  sing N N 105 
DA  N9    C8     sing Y N 106 
DA  N9    C4     sing Y N 107 
DA  C8    N7     doub Y N 108 
DA  C8    H8     sing N N 109 
DA  N7    C5     sing Y N 110 
DA  C5    C6     sing Y N 111 
DA  C5    C4     doub Y N 112 
DA  C6    N6     sing N N 113 
DA  C6    N1     doub Y N 114 
DA  N6    H61    sing N N 115 
DA  N6    H62    sing N N 116 
DA  N1    C2     sing Y N 117 
DA  C2    N3     doub Y N 118 
DA  C2    H2     sing N N 119 
DA  N3    C4     sing Y N 120 
DC  OP3   P      sing N N 121 
DC  OP3   HOP3   sing N N 122 
DC  P     OP1    doub N N 123 
DC  P     OP2    sing N N 124 
DC  P     "O5'"  sing N N 125 
DC  OP2   HOP2   sing N N 126 
DC  "O5'" "C5'"  sing N N 127 
DC  "C5'" "C4'"  sing N N 128 
DC  "C5'" "H5'"  sing N N 129 
DC  "C5'" "H5''" sing N N 130 
DC  "C4'" "O4'"  sing N N 131 
DC  "C4'" "C3'"  sing N N 132 
DC  "C4'" "H4'"  sing N N 133 
DC  "O4'" "C1'"  sing N N 134 
DC  "C3'" "O3'"  sing N N 135 
DC  "C3'" "C2'"  sing N N 136 
DC  "C3'" "H3'"  sing N N 137 
DC  "O3'" "HO3'" sing N N 138 
DC  "C2'" "C1'"  sing N N 139 
DC  "C2'" "H2'"  sing N N 140 
DC  "C2'" "H2''" sing N N 141 
DC  "C1'" N1     sing N N 142 
DC  "C1'" "H1'"  sing N N 143 
DC  N1    C2     sing N N 144 
DC  N1    C6     sing N N 145 
DC  C2    O2     doub N N 146 
DC  C2    N3     sing N N 147 
DC  N3    C4     doub N N 148 
DC  C4    N4     sing N N 149 
DC  C4    C5     sing N N 150 
DC  N4    H41    sing N N 151 
DC  N4    H42    sing N N 152 
DC  C5    C6     doub N N 153 
DC  C5    H5     sing N N 154 
DC  C6    H6     sing N N 155 
DG  OP3   P      sing N N 156 
DG  OP3   HOP3   sing N N 157 
DG  P     OP1    doub N N 158 
DG  P     OP2    sing N N 159 
DG  P     "O5'"  sing N N 160 
DG  OP2   HOP2   sing N N 161 
DG  "O5'" "C5'"  sing N N 162 
DG  "C5'" "C4'"  sing N N 163 
DG  "C5'" "H5'"  sing N N 164 
DG  "C5'" "H5''" sing N N 165 
DG  "C4'" "O4'"  sing N N 166 
DG  "C4'" "C3'"  sing N N 167 
DG  "C4'" "H4'"  sing N N 168 
DG  "O4'" "C1'"  sing N N 169 
DG  "C3'" "O3'"  sing N N 170 
DG  "C3'" "C2'"  sing N N 171 
DG  "C3'" "H3'"  sing N N 172 
DG  "O3'" "HO3'" sing N N 173 
DG  "C2'" "C1'"  sing N N 174 
DG  "C2'" "H2'"  sing N N 175 
DG  "C2'" "H2''" sing N N 176 
DG  "C1'" N9     sing N N 177 
DG  "C1'" "H1'"  sing N N 178 
DG  N9    C8     sing Y N 179 
DG  N9    C4     sing Y N 180 
DG  C8    N7     doub Y N 181 
DG  C8    H8     sing N N 182 
DG  N7    C5     sing Y N 183 
DG  C5    C6     sing N N 184 
DG  C5    C4     doub Y N 185 
DG  C6    O6     doub N N 186 
DG  C6    N1     sing N N 187 
DG  N1    C2     sing N N 188 
DG  N1    H1     sing N N 189 
DG  C2    N2     sing N N 190 
DG  C2    N3     doub N N 191 
DG  N2    H21    sing N N 192 
DG  N2    H22    sing N N 193 
DG  N3    C4     sing N N 194 
DT  OP3   P      sing N N 195 
DT  OP3   HOP3   sing N N 196 
DT  P     OP1    doub N N 197 
DT  P     OP2    sing N N 198 
DT  P     "O5'"  sing N N 199 
DT  OP2   HOP2   sing N N 200 
DT  "O5'" "C5'"  sing N N 201 
DT  "C5'" "C4'"  sing N N 202 
DT  "C5'" "H5'"  sing N N 203 
DT  "C5'" "H5''" sing N N 204 
DT  "C4'" "O4'"  sing N N 205 
DT  "C4'" "C3'"  sing N N 206 
DT  "C4'" "H4'"  sing N N 207 
DT  "O4'" "C1'"  sing N N 208 
DT  "C3'" "O3'"  sing N N 209 
DT  "C3'" "C2'"  sing N N 210 
DT  "C3'" "H3'"  sing N N 211 
DT  "O3'" "HO3'" sing N N 212 
DT  "C2'" "C1'"  sing N N 213 
DT  "C2'" "H2'"  sing N N 214 
DT  "C2'" "H2''" sing N N 215 
DT  "C1'" N1     sing N N 216 
DT  "C1'" "H1'"  sing N N 217 
DT  N1    C2     sing N N 218 
DT  N1    C6     sing N N 219 
DT  C2    O2     doub N N 220 
DT  C2    N3     sing N N 221 
DT  N3    C4     sing N N 222 
DT  N3    H3     sing N N 223 
DT  C4    O4     doub N N 224 
DT  C4    C5     sing N N 225 
DT  C5    C7     sing N N 226 
DT  C5    C6     doub N N 227 
DT  C7    H71    sing N N 228 
DT  C7    H72    sing N N 229 
DT  C7    H73    sing N N 230 
DT  C6    H6     sing N N 231 
GLN N     CA     sing N N 232 
GLN N     H      sing N N 233 
GLN N     H2     sing N N 234 
GLN CA    C      sing N N 235 
GLN CA    CB     sing N N 236 
GLN CA    HA     sing N N 237 
GLN C     O      doub N N 238 
GLN C     OXT    sing N N 239 
GLN CB    CG     sing N N 240 
GLN CB    HB2    sing N N 241 
GLN CB    HB3    sing N N 242 
GLN CG    CD     sing N N 243 
GLN CG    HG2    sing N N 244 
GLN CG    HG3    sing N N 245 
GLN CD    OE1    doub N N 246 
GLN CD    NE2    sing N N 247 
GLN NE2   HE21   sing N N 248 
GLN NE2   HE22   sing N N 249 
GLN OXT   HXT    sing N N 250 
GLU N     CA     sing N N 251 
GLU N     H      sing N N 252 
GLU N     H2     sing N N 253 
GLU CA    C      sing N N 254 
GLU CA    CB     sing N N 255 
GLU CA    HA     sing N N 256 
GLU C     O      doub N N 257 
GLU C     OXT    sing N N 258 
GLU CB    CG     sing N N 259 
GLU CB    HB2    sing N N 260 
GLU CB    HB3    sing N N 261 
GLU CG    CD     sing N N 262 
GLU CG    HG2    sing N N 263 
GLU CG    HG3    sing N N 264 
GLU CD    OE1    doub N N 265 
GLU CD    OE2    sing N N 266 
GLU OE2   HE2    sing N N 267 
GLU OXT   HXT    sing N N 268 
GLY N     CA     sing N N 269 
GLY N     H      sing N N 270 
GLY N     H2     sing N N 271 
GLY CA    C      sing N N 272 
GLY CA    HA2    sing N N 273 
GLY CA    HA3    sing N N 274 
GLY C     O      doub N N 275 
GLY C     OXT    sing N N 276 
GLY OXT   HXT    sing N N 277 
HIS N     CA     sing N N 278 
HIS N     H      sing N N 279 
HIS N     H2     sing N N 280 
HIS CA    C      sing N N 281 
HIS CA    CB     sing N N 282 
HIS CA    HA     sing N N 283 
HIS C     O      doub N N 284 
HIS C     OXT    sing N N 285 
HIS CB    CG     sing N N 286 
HIS CB    HB2    sing N N 287 
HIS CB    HB3    sing N N 288 
HIS CG    ND1    sing Y N 289 
HIS CG    CD2    doub Y N 290 
HIS ND1   CE1    doub Y N 291 
HIS ND1   HD1    sing N N 292 
HIS CD2   NE2    sing Y N 293 
HIS CD2   HD2    sing N N 294 
HIS CE1   NE2    sing Y N 295 
HIS CE1   HE1    sing N N 296 
HIS NE2   HE2    sing N N 297 
HIS OXT   HXT    sing N N 298 
HOH O     H1     sing N N 299 
HOH O     H2     sing N N 300 
ILE N     CA     sing N N 301 
ILE N     H      sing N N 302 
ILE N     H2     sing N N 303 
ILE CA    C      sing N N 304 
ILE CA    CB     sing N N 305 
ILE CA    HA     sing N N 306 
ILE C     O      doub N N 307 
ILE C     OXT    sing N N 308 
ILE CB    CG1    sing N N 309 
ILE CB    CG2    sing N N 310 
ILE CB    HB     sing N N 311 
ILE CG1   CD1    sing N N 312 
ILE CG1   HG12   sing N N 313 
ILE CG1   HG13   sing N N 314 
ILE CG2   HG21   sing N N 315 
ILE CG2   HG22   sing N N 316 
ILE CG2   HG23   sing N N 317 
ILE CD1   HD11   sing N N 318 
ILE CD1   HD12   sing N N 319 
ILE CD1   HD13   sing N N 320 
ILE OXT   HXT    sing N N 321 
LEU N     CA     sing N N 322 
LEU N     H      sing N N 323 
LEU N     H2     sing N N 324 
LEU CA    C      sing N N 325 
LEU CA    CB     sing N N 326 
LEU CA    HA     sing N N 327 
LEU C     O      doub N N 328 
LEU C     OXT    sing N N 329 
LEU CB    CG     sing N N 330 
LEU CB    HB2    sing N N 331 
LEU CB    HB3    sing N N 332 
LEU CG    CD1    sing N N 333 
LEU CG    CD2    sing N N 334 
LEU CG    HG     sing N N 335 
LEU CD1   HD11   sing N N 336 
LEU CD1   HD12   sing N N 337 
LEU CD1   HD13   sing N N 338 
LEU CD2   HD21   sing N N 339 
LEU CD2   HD22   sing N N 340 
LEU CD2   HD23   sing N N 341 
LEU OXT   HXT    sing N N 342 
LYS N     CA     sing N N 343 
LYS N     H      sing N N 344 
LYS N     H2     sing N N 345 
LYS CA    C      sing N N 346 
LYS CA    CB     sing N N 347 
LYS CA    HA     sing N N 348 
LYS C     O      doub N N 349 
LYS C     OXT    sing N N 350 
LYS CB    CG     sing N N 351 
LYS CB    HB2    sing N N 352 
LYS CB    HB3    sing N N 353 
LYS CG    CD     sing N N 354 
LYS CG    HG2    sing N N 355 
LYS CG    HG3    sing N N 356 
LYS CD    CE     sing N N 357 
LYS CD    HD2    sing N N 358 
LYS CD    HD3    sing N N 359 
LYS CE    NZ     sing N N 360 
LYS CE    HE2    sing N N 361 
LYS CE    HE3    sing N N 362 
LYS NZ    HZ1    sing N N 363 
LYS NZ    HZ2    sing N N 364 
LYS NZ    HZ3    sing N N 365 
LYS OXT   HXT    sing N N 366 
MES O1    C2     sing N N 367 
MES O1    C6     sing N N 368 
MES C2    C3     sing N N 369 
MES C2    H21    sing N N 370 
MES C2    H22    sing N N 371 
MES C3    N4     sing N N 372 
MES C3    H31    sing N N 373 
MES C3    H32    sing N N 374 
MES N4    C5     sing N N 375 
MES N4    C7     sing N N 376 
MES N4    HN4    sing N N 377 
MES C5    C6     sing N N 378 
MES C5    H51    sing N N 379 
MES C5    H52    sing N N 380 
MES C6    H61    sing N N 381 
MES C6    H62    sing N N 382 
MES C7    C8     sing N N 383 
MES C7    H71    sing N N 384 
MES C7    H72    sing N N 385 
MES C8    S      sing N N 386 
MES C8    H81    sing N N 387 
MES C8    H82    sing N N 388 
MES S     O1S    doub N N 389 
MES S     O2S    doub N N 390 
MES S     O3S    sing N N 391 
MET N     CA     sing N N 392 
MET N     H      sing N N 393 
MET N     H2     sing N N 394 
MET CA    C      sing N N 395 
MET CA    CB     sing N N 396 
MET CA    HA     sing N N 397 
MET C     O      doub N N 398 
MET C     OXT    sing N N 399 
MET CB    CG     sing N N 400 
MET CB    HB2    sing N N 401 
MET CB    HB3    sing N N 402 
MET CG    SD     sing N N 403 
MET CG    HG2    sing N N 404 
MET CG    HG3    sing N N 405 
MET SD    CE     sing N N 406 
MET CE    HE1    sing N N 407 
MET CE    HE2    sing N N 408 
MET CE    HE3    sing N N 409 
MET OXT   HXT    sing N N 410 
PHE N     CA     sing N N 411 
PHE N     H      sing N N 412 
PHE N     H2     sing N N 413 
PHE CA    C      sing N N 414 
PHE CA    CB     sing N N 415 
PHE CA    HA     sing N N 416 
PHE C     O      doub N N 417 
PHE C     OXT    sing N N 418 
PHE CB    CG     sing N N 419 
PHE CB    HB2    sing N N 420 
PHE CB    HB3    sing N N 421 
PHE CG    CD1    doub Y N 422 
PHE CG    CD2    sing Y N 423 
PHE CD1   CE1    sing Y N 424 
PHE CD1   HD1    sing N N 425 
PHE CD2   CE2    doub Y N 426 
PHE CD2   HD2    sing N N 427 
PHE CE1   CZ     doub Y N 428 
PHE CE1   HE1    sing N N 429 
PHE CE2   CZ     sing Y N 430 
PHE CE2   HE2    sing N N 431 
PHE CZ    HZ     sing N N 432 
PHE OXT   HXT    sing N N 433 
PRO N     CA     sing N N 434 
PRO N     CD     sing N N 435 
PRO N     H      sing N N 436 
PRO CA    C      sing N N 437 
PRO CA    CB     sing N N 438 
PRO CA    HA     sing N N 439 
PRO C     O      doub N N 440 
PRO C     OXT    sing N N 441 
PRO CB    CG     sing N N 442 
PRO CB    HB2    sing N N 443 
PRO CB    HB3    sing N N 444 
PRO CG    CD     sing N N 445 
PRO CG    HG2    sing N N 446 
PRO CG    HG3    sing N N 447 
PRO CD    HD2    sing N N 448 
PRO CD    HD3    sing N N 449 
PRO OXT   HXT    sing N N 450 
SER N     CA     sing N N 451 
SER N     H      sing N N 452 
SER N     H2     sing N N 453 
SER CA    C      sing N N 454 
SER CA    CB     sing N N 455 
SER CA    HA     sing N N 456 
SER C     O      doub N N 457 
SER C     OXT    sing N N 458 
SER CB    OG     sing N N 459 
SER CB    HB2    sing N N 460 
SER CB    HB3    sing N N 461 
SER OG    HG     sing N N 462 
SER OXT   HXT    sing N N 463 
THR N     CA     sing N N 464 
THR N     H      sing N N 465 
THR N     H2     sing N N 466 
THR CA    C      sing N N 467 
THR CA    CB     sing N N 468 
THR CA    HA     sing N N 469 
THR C     O      doub N N 470 
THR C     OXT    sing N N 471 
THR CB    OG1    sing N N 472 
THR CB    CG2    sing N N 473 
THR CB    HB     sing N N 474 
THR OG1   HG1    sing N N 475 
THR CG2   HG21   sing N N 476 
THR CG2   HG22   sing N N 477 
THR CG2   HG23   sing N N 478 
THR OXT   HXT    sing N N 479 
TRP N     CA     sing N N 480 
TRP N     H      sing N N 481 
TRP N     H2     sing N N 482 
TRP CA    C      sing N N 483 
TRP CA    CB     sing N N 484 
TRP CA    HA     sing N N 485 
TRP C     O      doub N N 486 
TRP C     OXT    sing N N 487 
TRP CB    CG     sing N N 488 
TRP CB    HB2    sing N N 489 
TRP CB    HB3    sing N N 490 
TRP CG    CD1    doub Y N 491 
TRP CG    CD2    sing Y N 492 
TRP CD1   NE1    sing Y N 493 
TRP CD1   HD1    sing N N 494 
TRP CD2   CE2    doub Y N 495 
TRP CD2   CE3    sing Y N 496 
TRP NE1   CE2    sing Y N 497 
TRP NE1   HE1    sing N N 498 
TRP CE2   CZ2    sing Y N 499 
TRP CE3   CZ3    doub Y N 500 
TRP CE3   HE3    sing N N 501 
TRP CZ2   CH2    doub Y N 502 
TRP CZ2   HZ2    sing N N 503 
TRP CZ3   CH2    sing Y N 504 
TRP CZ3   HZ3    sing N N 505 
TRP CH2   HH2    sing N N 506 
TRP OXT   HXT    sing N N 507 
TYR N     CA     sing N N 508 
TYR N     H      sing N N 509 
TYR N     H2     sing N N 510 
TYR CA    C      sing N N 511 
TYR CA    CB     sing N N 512 
TYR CA    HA     sing N N 513 
TYR C     O      doub N N 514 
TYR C     OXT    sing N N 515 
TYR CB    CG     sing N N 516 
TYR CB    HB2    sing N N 517 
TYR CB    HB3    sing N N 518 
TYR CG    CD1    doub Y N 519 
TYR CG    CD2    sing Y N 520 
TYR CD1   CE1    sing Y N 521 
TYR CD1   HD1    sing N N 522 
TYR CD2   CE2    doub Y N 523 
TYR CD2   HD2    sing N N 524 
TYR CE1   CZ     doub Y N 525 
TYR CE1   HE1    sing N N 526 
TYR CE2   CZ     sing Y N 527 
TYR CE2   HE2    sing N N 528 
TYR CZ    OH     sing N N 529 
TYR OH    HH     sing N N 530 
TYR OXT   HXT    sing N N 531 
VAL N     CA     sing N N 532 
VAL N     H      sing N N 533 
VAL N     H2     sing N N 534 
VAL CA    C      sing N N 535 
VAL CA    CB     sing N N 536 
VAL CA    HA     sing N N 537 
VAL C     O      doub N N 538 
VAL C     OXT    sing N N 539 
VAL CB    CG1    sing N N 540 
VAL CB    CG2    sing N N 541 
VAL CB    HB     sing N N 542 
VAL CG1   HG11   sing N N 543 
VAL CG1   HG12   sing N N 544 
VAL CG1   HG13   sing N N 545 
VAL CG2   HG21   sing N N 546 
VAL CG2   HG22   sing N N 547 
VAL CG2   HG23   sing N N 548 
VAL OXT   HXT    sing N N 549 
# 
loop_
_ndb_struct_conf_na.entry_id 
_ndb_struct_conf_na.feature 
9EZD 'double helix'        
9EZD 'a-form double helix' 
9EZD '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 C DG 1  1_555 B DC 8 1_555 0.039  -0.116 -0.220 -4.962 -17.125 -1.684 1  F_DG1:DC8_E  F 1  ? E 8 ? 19 1 
1 C DA 2  1_555 B DT 7 1_555 -0.158 -0.247 0.526  5.051  -15.491 1.702  2  F_DA2:DT7_E  F 2  ? E 7 ? 20 1 
1 C DG 3  1_555 B DC 6 1_555 -0.020 -0.154 0.088  10.450 -2.030  -0.574 3  F_DG3:DC6_E  F 3  ? E 6 ? 19 1 
1 C DG 4  1_555 B DC 5 1_555 -0.049 -0.108 0.895  20.603 -11.591 -2.079 4  F_DG4:DC5_E  F 4  ? E 5 ? 19 1 
1 C DA 5  1_555 B DT 4 1_555 -0.166 -0.181 -0.214 -9.326 -16.743 1.166  5  F_DA5:DT4_E  F 5  ? E 4 ? 20 1 
1 C DA 6  1_555 B DT 3 1_555 0.142  -0.198 -0.214 -6.610 -13.258 0.953  6  F_DA6:DT3_E  F 6  ? E 3 ? 20 1 
1 C DT 7  1_555 B DA 2 1_555 -0.341 -0.287 0.025  2.177  1.277   5.156  7  F_DT7:DA2_E  F 7  ? E 2 ? 20 1 
1 C DG 8  1_555 B DC 1 1_555 0.124  -0.114 0.230  15.536 -8.884  -2.052 8  F_DG8:DC1_E  F 8  ? E 1 ? 19 1 
1 C DC 9  1_555 D DG 5 1_555 0.441  -0.295 -0.022 10.275 -18.306 -3.100 9  F_DC9:DG5_G  F 9  ? G 5 ? 19 1 
1 C DA 10 1_555 D DT 4 1_555 0.445  -0.375 0.613  6.048  -3.245  3.944  10 F_DA10:DT4_G F 10 ? G 4 ? 20 1 
1 C DG 11 1_555 D DC 3 1_555 0.077  -0.092 0.187  3.450  -3.256  -0.935 11 F_DG11:DC3_G F 11 ? G 3 ? 19 1 
1 C DA 12 1_555 D DT 2 1_555 0.228  -0.146 -0.180 -0.065 -9.389  -1.869 12 F_DA12:DT2_G F 12 ? G 2 ? 20 1 
1 C DC 13 1_555 D DG 1 1_555 0.914  -0.400 0.274  6.045  0.002   -4.437 13 F_DC13:DG1_G F 13 ? G 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 C DG 1  1_555 B DC 8 1_555 C DA 2  1_555 B DT 7 1_555 -0.270 0.224  3.004 -7.854 -1.953 36.730 0.583  -0.529 2.981 -3.053  
12.282 37.581 1  FF_DG1DA2:DT7DC8_EE   F 1  ? E 8 ? F 2  ? E 7 ? 
1 C DA 2  1_555 B DT 7 1_555 C DG 3  1_555 B DC 6 1_555 0.907  0.235  3.441 1.871  -0.539 31.736 0.534  -1.293 3.483 -0.984  
-3.418 31.794 2  FF_DA2DG3:DC6DT7_EE   F 2  ? E 7 ? F 3  ? E 6 ? 
1 C DG 3  1_555 B DC 6 1_555 C DG 4  1_555 B DC 5 1_555 -0.310 0.074  3.063 -6.563 -5.565 37.304 0.774  -0.305 3.031 -8.560  
10.097 38.250 3  FF_DG3DG4:DC5DC6_EE   F 3  ? E 6 ? F 4  ? E 5 ? 
1 C DG 4  1_555 B DC 5 1_555 C DA 5  1_555 B DT 4 1_555 -0.036 -0.645 4.154 6.042  -8.129 44.007 0.099  0.746  4.165 -10.680 
-7.939 45.101 4  FF_DG4DA5:DT4DC5_EE   F 4  ? E 5 ? F 5  ? E 4 ? 
1 C DA 5  1_555 B DT 4 1_555 C DA 6  1_555 B DT 3 1_555 0.382  -0.446 3.324 0.207  -6.124 33.600 0.239  -0.617 3.353 -10.486 
-0.354 34.138 5  FF_DA5DA6:DT3DT4_EE   F 5  ? E 4 ? F 6  ? E 3 ? 
1 C DA 6  1_555 B DT 3 1_555 C DT 7  1_555 B DA 2 1_555 0.826  -0.785 3.404 -5.250 -8.405 31.964 0.098  -2.351 3.325 -14.824 9.260 
33.427 6  FF_DA6DT7:DA2DT3_EE   F 6  ? E 3 ? F 7  ? E 2 ? 
1 C DT 7  1_555 B DA 2 1_555 C DG 8  1_555 B DC 1 1_555 -0.871 -0.903 3.412 0.270  10.090 26.775 -4.108 1.824  2.879 20.871  
-0.559 28.582 7  FF_DT7DG8:DC1DA2_EE   F 7  ? E 2 ? F 8  ? E 1 ? 
1 C DG 8  1_555 B DC 1 1_555 C DC 9  1_555 D DG 5 1_555 -1.057 -0.482 3.474 -1.642 -2.101 34.809 -0.463 1.495  3.541 -3.505  2.740 
34.908 8  FF_DG8DC9:DG5DC1_GE   F 8  ? E 1 ? F 9  ? G 5 ? 
1 C DC 9  1_555 D DG 5 1_555 C DA 10 1_555 D DT 4 1_555 0.764  -0.006 3.465 -4.844 -1.176 39.381 0.135  -1.716 3.350 -1.737  7.153 
39.683 9  FF_DC9DA10:DT4DG5_GG  F 9  ? G 5 ? F 10 ? G 4 ? 
1 C DA 10 1_555 D DT 4 1_555 C DG 11 1_555 D DC 3 1_555 -0.441 0.110  3.622 2.411  1.265  30.864 -0.062 1.339  3.580 2.371   
-4.519 30.981 10 FF_DA10DG11:DC3DT4_GG F 10 ? G 4 ? F 11 ? G 3 ? 
1 C DG 11 1_555 D DC 3 1_555 C DA 12 1_555 D DT 2 1_555 0.341  0.073  3.461 3.214  5.322  35.764 -0.676 -0.069 3.453 8.586   
-5.186 36.283 11 FF_DG11DA12:DT2DC3_GG F 11 ? G 3 ? F 12 ? G 2 ? 
1 C DA 12 1_555 D DT 2 1_555 C DC 13 1_555 D DG 1 1_555 0.725  -0.759 3.315 -5.032 -1.796 37.380 -0.940 -1.774 3.225 -2.785  7.802 
37.746 12 FF_DA12DC13:DG1DT2_GG F 12 ? G 2 ? F 13 ? G 1 ? 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'Model obtained after experimental phasing' 
# 
_atom_sites.entry_id                    9EZD 
_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]   0.010182 
_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]   0.007668 
_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]   0.015989 
_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 
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
_atom_site.pdbx_tls_group_id 
ATOM   1    N  N     . MET A 1 1   ? 26.424  -9.773  4.663   1 22.33  ? 1   MET A N     1 1 
ATOM   2    C  CA    . MET A 1 1   ? 26.204  -8.578  5.46    1 22.91  ? 1   MET A CA    1 1 
ATOM   3    C  C     . MET A 1 1   ? 26.146  -7.342  4.584   1 23.37  ? 1   MET A C     1 1 
ATOM   4    O  O     . MET A 1 1   ? 26.871  -7.243  3.604   1 23.31  ? 1   MET A O     1 1 
ATOM   5    C  CB    . MET A 1 1   ? 27.319  -8.428  6.516   1 23.81  ? 1   MET A CB    1 1 
ATOM   6    C  CG    . MET A 1 1   ? 27.236  -7.136  7.318   1 26.54  ? 1   MET A CG    1 1 
ATOM   7    S  SD    . MET A 1 1   ? 28.49   -6.971  8.598   1 31.53  ? 1   MET A SD    1 1 
ATOM   8    C  CE    . MET A 1 1   ? 29.939  -6.849  7.614   1 28.35  ? 1   MET A CE    1 1 
ATOM   9    N  N     . ASN A 1 2   ? 25.297  -6.389  4.951   1 23.77  ? 2   ASN A N     1 1 
ATOM   10   C  CA    . ASN A 1 2   ? 25.219  -5.11   4.266   1 24.63  ? 2   ASN A CA    1 1 
ATOM   11   C  C     . ASN A 1 2   ? 25.625  -4.024  5.242   1 24.31  ? 2   ASN A C     1 1 
ATOM   12   O  O     . ASN A 1 2   ? 25.225  -4.06   6.408   1 24.52  ? 2   ASN A O     1 1 
ATOM   13   C  CB    . ASN A 1 2   ? 23.825  -4.849  3.721   1 26.77  ? 2   ASN A CB    1 1 
ATOM   14   C  CG    . ASN A 1 2   ? 23.629  -5.44   2.35    1 31.41  ? 2   ASN A CG    1 1 
ATOM   15   O  OD1   . ASN A 1 2   ? 24.577  -5.566  1.559   1 32.81  ? 2   ASN A OD1   1 1 
ATOM   16   N  ND2   . ASN A 1 2   ? 22.391  -5.81   2.037   1 32.59  ? 2   ASN A ND2   1 1 
ATOM   17   N  N     . VAL A 1 3   ? 26.448  -3.085  4.784   1 23.61  ? 3   VAL A N     1 1 
ATOM   18   C  CA    . VAL A 1 3   ? 26.902  -2.002  5.637   1 23.69  ? 3   VAL A CA    1 1 
ATOM   19   C  C     . VAL A 1 3   ? 26.299  -0.703  5.15    1 23.69  ? 3   VAL A C     1 1 
ATOM   20   O  O     . VAL A 1 3   ? 26.297  -0.44   3.949   1 24.24  ? 3   VAL A O     1 1 
ATOM   21   C  CB    . VAL A 1 3   ? 28.444  -1.929  5.709   1 24.43  ? 3   VAL A CB    1 1 
ATOM   22   C  CG1   . VAL A 1 3   ? 28.901  -0.726  6.517   1 24.92  ? 3   VAL A CG1   1 1 
ATOM   23   C  CG2   . VAL A 1 3   ? 29.015  -3.202  6.306   1 25.12  ? 3   VAL A CG2   1 1 
ATOM   24   N  N     . PHE A 1 4   ? 25.752  0.09    6.082   1 22.69  ? 4   PHE A N     1 1 
ATOM   25   C  CA    . PHE A 1 4   ? 25.167  1.396   5.816   1 21.7   ? 4   PHE A CA    1 1 
ATOM   26   C  C     . PHE A 1 4   ? 25.871  2.437   6.648   1 20.96  ? 4   PHE A C     1 1 
ATOM   27   O  O     . PHE A 1 4   ? 26.321  2.143   7.75    1 20.77  ? 4   PHE A O     1 1 
ATOM   28   C  CB    . PHE A 1 4   ? 23.697  1.408   6.199   1 21.36  ? 4   PHE A CB    1 1 
ATOM   29   C  CG    . PHE A 1 4   ? 22.89   0.346   5.509   1 21.79  ? 4   PHE A CG    1 1 
ATOM   30   C  CD1   . PHE A 1 4   ? 22.427  0.536   4.221   1 22.29  ? 4   PHE A CD1   1 1 
ATOM   31   C  CD2   . PHE A 1 4   ? 22.583  -0.837  6.151   1 22.36  ? 4   PHE A CD2   1 1 
ATOM   32   C  CE1   . PHE A 1 4   ? 21.675  -0.434  3.592   1 22.64  ? 4   PHE A CE1   1 1 
ATOM   33   C  CE2   . PHE A 1 4   ? 21.838  -1.808  5.517   1 22.87  ? 4   PHE A CE2   1 1 
ATOM   34   C  CZ    . PHE A 1 4   ? 21.389  -1.6    4.241   1 22.55  ? 4   PHE A CZ    1 1 
ATOM   35   N  N     . ARG A 1 5   ? 25.941  3.663   6.15    1 20.6   ? 5   ARG A N     1 1 
ATOM   36   C  CA    . ARG A 1 5   ? 26.544  4.753   6.902   1 20.61  ? 5   ARG A CA    1 1 
ATOM   37   C  C     . ARG A 1 5   ? 25.529  5.835   7.179   1 21.05  ? 5   ARG A C     1 1 
ATOM   38   O  O     . ARG A 1 5   ? 24.732  6.173   6.307   1 21.13  ? 5   ARG A O     1 1 
ATOM   39   C  CB    . ARG A 1 5   ? 27.774  5.31    6.2     1 21.25  ? 5   ARG A CB    1 1 
ATOM   40   C  CG    . ARG A 1 5   ? 28.974  4.397   6.341   1 23.37  ? 5   ARG A CG    1 1 
ATOM   41   C  CD    . ARG A 1 5   ? 30.062  4.794   5.38    1 25.77  ? 5   ARG A CD    1 1 
ATOM   42   N  NE    . ARG A 1 5   ? 31.315  4.085   5.636   1 27.58  ? 5   ARG A NE    1 1 
ATOM   43   C  CZ    . ARG A 1 5   ? 32.512  4.516   5.249   1 27.72  ? 5   ARG A CZ    1 1 
ATOM   44   N  NH1   . ARG A 1 5   ? 32.633  5.669   4.598   1 26.35  ? 5   ARG A NH1   1 1 
ATOM   45   N  NH2   . ARG A 1 5   ? 33.598  3.81    5.527   1 27.01  ? 5   ARG A NH2   1 1 
ATOM   46   N  N     . ILE A 1 6   ? 25.511  6.332   8.41    1 21.08  ? 6   ILE A N     1 1 
ATOM   47   C  CA    . ILE A 1 6   ? 24.594  7.392   8.78    1 21.63  ? 6   ILE A CA    1 1 
ATOM   48   C  C     . ILE A 1 6   ? 25.436  8.624   8.985   1 22.2   ? 6   ILE A C     1 1 
ATOM   49   O  O     . ILE A 1 6   ? 26.128  8.712   9.986   1 22.31  ? 6   ILE A O     1 1 
ATOM   50   C  CB    . ILE A 1 6   ? 23.798  7.051   10.056  1 21.88  ? 6   ILE A CB    1 1 
ATOM   51   C  CG1   . ILE A 1 6   ? 23.136  5.674   9.956   1 22.92  ? 6   ILE A CG1   1 1 
ATOM   52   C  CG2   . ILE A 1 6   ? 22.792  8.153   10.385  1 21.86  ? 6   ILE A CG2   1 1 
ATOM   53   C  CD1   . ILE A 1 6   ? 22.113  5.576   8.894   1 24.49  ? 6   ILE A CD1   1 1 
ATOM   54   N  N     . HIS A 1 7   ? 25.414  9.557   8.036   1 22.34  ? 7   HIS A N     1 1 
ATOM   55   C  CA    . HIS A 1 7   ? 26.164  10.8    8.154   1 22.99  ? 7   HIS A CA    1 1 
ATOM   56   C  C     . HIS A 1 7   ? 25.227  11.825  8.756   1 23.79  ? 7   HIS A C     1 1 
ATOM   57   O  O     . HIS A 1 7   ? 24.204  12.11   8.15    1 24.4   ? 7   HIS A O     1 1 
ATOM   58   C  CB    . HIS A 1 7   ? 26.619  11.255  6.762   1 23.76  ? 7   HIS A CB    1 1 
ATOM   59   C  CG    . HIS A 1 7   ? 27.52   10.267  6.087   1 26.18  ? 7   HIS A CG    1 1 
ATOM   60   N  ND1   . HIS A 1 7   ? 28.897  10.365  6.179   1 27.52  ? 7   HIS A ND1   1 1 
ATOM   61   C  CD2   . HIS A 1 7   ? 27.211  9.17    5.358   1 27.53  ? 7   HIS A CD2   1 1 
ATOM   62   C  CE1   . HIS A 1 7   ? 29.379  9.338   5.5     1 27.95  ? 7   HIS A CE1   1 1 
ATOM   63   N  NE2   . HIS A 1 7   ? 28.407  8.596   4.979   1 28.41  ? 7   HIS A NE2   1 1 
ATOM   64   N  N     . GLY A 1 8   ? 25.519  12.317  9.953   1 23.98  ? 8   GLY A N     1 1 
ATOM   65   C  CA    . GLY A 1 8   ? 24.638  13.28   10.608  1 25.13  ? 8   GLY A CA    1 1 
ATOM   66   C  C     . GLY A 1 8   ? 25.328  14.523  11.123  1 26.18  ? 8   GLY A C     1 1 
ATOM   67   O  O     . GLY A 1 8   ? 26.553  14.582  11.099  1 26.27  ? 8   GLY A O     1 1 
ATOM   68   N  N     . ASP A 1 9   ? 24.562  15.538  11.58   1 27.13  ? 9   ASP A N     1 1 
ATOM   69   C  CA    . ASP A 1 9   ? 25.191  16.743  12.14   1 28.83  ? 9   ASP A CA    1 1 
ATOM   70   C  C     . ASP A 1 9   ? 25.802  16.455  13.526  1 29.1   ? 9   ASP A C     1 1 
ATOM   71   O  O     . ASP A 1 9   ? 26.796  17.081  13.885  1 29.41  ? 9   ASP A O     1 1 
ATOM   72   C  CB    . ASP A 1 9   ? 24.311  18.025  12.138  1 32.21  ? 9   ASP A CB    1 1 
ATOM   73   C  CG    . ASP A 1 9   ? 22.857  17.902  11.689  1 40.16  ? 9   ASP A CG    1 1 
ATOM   74   O  OD1   . ASP A 1 9   ? 22.206  16.885  12.04   1 41.42  ? 9   ASP A OD1   1 1 
ATOM   75   O  OD2   . ASP A 1 9   ? 22.352  18.854  11.019  1 43.15  ? 9   ASP A OD2   1 1 
ATOM   76   N  N     . ASN A 1 10  ? 25.259  15.477  14.265  1 28.75  ? 10  ASN A N     1 1 
ATOM   77   C  CA    . ASN A 1 10  ? 25.792  15.032  15.555  1 29.4   ? 10  ASN A CA    1 1 
ATOM   78   C  C     . ASN A 1 10  ? 25.345  13.58   15.868  1 30.04  ? 10  ASN A C     1 1 
ATOM   79   O  O     . ASN A 1 10  ? 24.504  13.03   15.149  1 30.31  ? 10  ASN A O     1 1 
ATOM   80   C  CB    . ASN A 1 10  ? 25.432  15.995  16.679  1 30.6   ? 10  ASN A CB    1 1 
ATOM   81   C  CG    . ASN A 1 10  ? 23.974  16.266  16.766  1 34.16  ? 10  ASN A CG    1 1 
ATOM   82   O  OD1   . ASN A 1 10  ? 23.177  15.366  17.033  1 36.28  ? 10  ASN A OD1   1 1 
ATOM   83   N  ND2   . ASN A 1 10  ? 23.589  17.514  16.545  1 34.58  ? 10  ASN A ND2   1 1 
ATOM   84   N  N     . ILE A 1 11  ? 25.911  12.948  16.923  1 29.87  ? 11  ILE A N     1 1 
ATOM   85   C  CA    . ILE A 1 11  ? 25.57   11.568  17.274  1 29.74  ? 11  ILE A CA    1 1 
ATOM   86   C  C     . ILE A 1 11  ? 24.1    11.384  17.62   1 29.33  ? 11  ILE A C     1 1 
ATOM   87   O  O     . ILE A 1 11  ? 23.537  10.331  17.322  1 29.64  ? 11  ILE A O     1 1 
ATOM   88   C  CB    . ILE A 1 11  ? 26.48   11.017  18.388  1 30.41  ? 11  ILE A CB    1 1 
ATOM   89   C  CG1   . ILE A 1 11  ? 26.275  9.506   18.581  1 31.18  ? 11  ILE A CG1   1 1 
ATOM   90   C  CG2   . ILE A 1 11  ? 26.267  11.775  19.686  1 31.11  ? 11  ILE A CG2   1 1 
ATOM   91   C  CD1   . ILE A 1 11  ? 26.587  8.69    17.373  1 32.34  ? 11  ILE A CD1   1 1 
ATOM   92   N  N     . ILE A 1 12  ? 23.456  12.411  18.192  1 28.38  ? 12  ILE A N     1 1 
ATOM   93   C  CA    . ILE A 1 12  ? 22.045  12.324  18.543  1 28.02  ? 12  ILE A CA    1 1 
ATOM   94   C  C     . ILE A 1 12  ? 21.198  12.157  17.293  1 27.41  ? 12  ILE A C     1 1 
ATOM   95   O  O     . ILE A 1 12  ? 20.299  11.317  17.281  1 27.36  ? 12  ILE A O     1 1 
ATOM   96   C  CB    . ILE A 1 12  ? 21.599  13.523  19.407  1 28.68  ? 12  ILE A CB    1 1 
ATOM   97   C  CG1   . ILE A 1 12  ? 22.297  13.5    20.77   1 29.85  ? 12  ILE A CG1   1 1 
ATOM   98   C  CG2   . ILE A 1 12  ? 20.082  13.542  19.583  1 29.39  ? 12  ILE A CG2   1 1 
ATOM   99   C  CD1   . ILE A 1 12  ? 23.585  14.345  20.846  1 31.45  ? 12  ILE A CD1   1 1 
ATOM   100  N  N     . GLU A 1 13  ? 21.531  12.903  16.221  1 26.77  ? 13  GLU A N     1 1 
ATOM   101  C  CA    . GLU A 1 13  ? 20.806  12.817  14.953  1 26.85  ? 13  GLU A CA    1 1 
ATOM   102  C  C     . GLU A 1 13  ? 20.973  11.435  14.326  1 26.49  ? 13  GLU A C     1 1 
ATOM   103  O  O     . GLU A 1 13  ? 20      10.864  13.813  1 26.37  ? 13  GLU A O     1 1 
ATOM   104  C  CB    . GLU A 1 13  ? 21.26   13.914  13.977  1 28.79  ? 13  GLU A CB    1 1 
ATOM   105  C  CG    . GLU A 1 13  ? 21.052  15.315  14.516  1 33.76  ? 13  GLU A CG    1 1 
ATOM   106  C  CD    . GLU A 1 13  ? 19.605  15.753  14.644  1 42.34  ? 13  GLU A CD    1 1 
ATOM   107  O  OE1   . GLU A 1 13  ? 19.262  16.393  15.666  1 44.36  ? 13  GLU A OE1   1 1 
ATOM   108  O  OE2   . GLU A 1 13  ? 18.813  15.458  13.72   1 44.53  ? 13  GLU A OE2   1 1 
ATOM   109  N  N     . CYS A 1 14  ? 22.2    10.889  14.406  1 25.94  ? 14  CYS A N     1 1 
ATOM   110  C  CA    . CYS A 1 14  ? 22.531  9.564   13.886  1 25.77  ? 14  CYS A CA    1 1 
ATOM   111  C  C     . CYS A 1 14  ? 21.751  8.506   14.639  1 26.39  ? 14  CYS A C     1 1 
ATOM   112  O  O     . CYS A 1 14  ? 21.144  7.645   14.016  1 26.75  ? 14  CYS A O     1 1 
ATOM   113  C  CB    . CYS A 1 14  ? 24.035  9.309   13.943  1 25.13  ? 14  CYS A CB    1 1 
ATOM   114  S  SG    . CYS A 1 14  ? 25.033  10.559  13.08   1 24.7   ? 14  CYS A SG    1 1 
ATOM   115  N  N     . GLU A 1 15  ? 21.69   8.615   15.966  1 26.52  ? 15  GLU A N     1 1 
ATOM   116  C  CA    . GLU A 1 15  ? 20.938  7.672   16.779  1 27.32  ? 15  GLU A CA    1 1 
ATOM   117  C  C     . GLU A 1 15  ? 19.441  7.744   16.573  1 28.28  ? 15  GLU A C     1 1 
ATOM   118  O  O     . GLU A 1 15  ? 18.778  6.728   16.73   1 28.83  ? 15  GLU A O     1 1 
ATOM   119  C  CB    . GLU A 1 15  ? 21.289  7.802   18.255  1 29.63  ? 15  GLU A CB    1 1 
ATOM   120  C  CG    . GLU A 1 15  ? 22.694  7.324   18.544  1 35.74  ? 15  GLU A CG    1 1 
ATOM   121  C  CD    . GLU A 1 15  ? 22.928  5.836   18.341  1 43.13  ? 15  GLU A CD    1 1 
ATOM   122  O  OE1   . GLU A 1 15  ? 21.931  5.085   18.207  1 44.47  ? 15  GLU A OE1   1 1 
ATOM   123  O  OE2   . GLU A 1 15  ? 24.11   5.417   18.356  1 44.83  ? 15  GLU A OE2   1 1 
ATOM   124  N  N     . ARG A 1 16  ? 18.894  8.903   16.175  1 28.4   ? 16  ARG A N     1 1 
ATOM   125  C  CA    . ARG A 1 16  ? 17.453  9.026   15.91   1 28.48  ? 16  ARG A CA    1 1 
ATOM   126  C  C     . ARG A 1 16  ? 17.048  8.106   14.77   1 28.02  ? 16  ARG A C     1 1 
ATOM   127  O  O     . ARG A 1 16  ? 16.002  7.493   14.854  1 28.28  ? 16  ARG A O     1 1 
ATOM   128  C  CB    . ARG A 1 16  ? 17.055  10.48   15.6    1 30.43  ? 16  ARG A CB    1 1 
ATOM   129  C  CG    . ARG A 1 16  ? 17.091  11.385  16.825  1 35.01  ? 16  ARG A CG    1 1 
ATOM   130  C  CD    . ARG A 1 16  ? 15.856  12.247  16.952  1 40.01  ? 16  ARG A CD    1 1 
ATOM   131  N  NE    . ARG A 1 16  ? 16      13.525  16.252  1 44.67  ? 16  ARG A NE    1 1 
ATOM   132  C  CZ    . ARG A 1 16  ? 16.2    14.696  16.854  1 47.49  ? 16  ARG A CZ    1 1 
ATOM   133  N  NH1   . ARG A 1 16  ? 16.289  14.764  18.177  1 47.18  ? 16  ARG A NH1   1 1 
ATOM   134  N  NH2   . ARG A 1 16  ? 16.304  15.81   16.136  1 47.7   ? 16  ARG A NH2   1 1 
ATOM   135  N  N     . VAL A 1 17  ? 17.9    7.949   13.747  1 27.61  ? 17  VAL A N     1 1 
ATOM   136  C  CA    . VAL A 1 17  ? 17.647  7.061   12.617  1 27.93  ? 17  VAL A CA    1 1 
ATOM   137  C  C     . VAL A 1 17  ? 17.661  5.606   13.075  1 28.82  ? 17  VAL A C     1 1 
ATOM   138  O  O     . VAL A 1 17  ? 16.777  4.832   12.71   1 29.35  ? 17  VAL A O     1 1 
ATOM   139  C  CB    . VAL A 1 17  ? 18.653  7.317   11.483  1 28.36  ? 17  VAL A CB    1 1 
ATOM   140  C  CG1   . VAL A 1 17  ? 18.517  6.283   10.379  1 28.76  ? 17  VAL A CG1   1 1 
ATOM   141  C  CG2   . VAL A 1 17  ? 18.473  8.712   10.925  1 29.04  ? 17  VAL A CG2   1 1 
ATOM   142  N  N     . ILE A 1 18  ? 18.618  5.245   13.929  1 28.87  ? 18  ILE A N     1 1 
ATOM   143  C  CA    . ILE A 1 18  ? 18.71   3.896   14.48   1 29.28  ? 18  ILE A CA    1 1 
ATOM   144  C  C     . ILE A 1 18  ? 17.484  3.577   15.314  1 29.73  ? 18  ILE A C     1 1 
ATOM   145  O  O     . ILE A 1 18  ? 16.942  2.49    15.187  1 29.82  ? 18  ILE A O     1 1 
ATOM   146  C  CB    . ILE A 1 18  ? 19.995  3.743   15.302  1 29.74  ? 18  ILE A CB    1 1 
ATOM   147  C  CG1   . ILE A 1 18  ? 21.226  4.091   14.459  1 30.94  ? 18  ILE A CG1   1 1 
ATOM   148  C  CG2   . ILE A 1 18  ? 20.098  2.354   15.888  1 30.12  ? 18  ILE A CG2   1 1 
ATOM   149  C  CD1   . ILE A 1 18  ? 21.39   3.258   13.216  1 32.44  ? 18  ILE A CD1   1 1 
ATOM   150  N  N     . ASP A 1 19  ? 17.003  4.542   16.111  1 29.99  ? 19  ASP A N     1 1 
ATOM   151  C  CA    . ASP A 1 19  ? 15.804  4.366   16.929  1 30.77  ? 19  ASP A CA    1 1 
ATOM   152  C  C     . ASP A 1 19  ? 14.557  4.142   16.074  1 31.15  ? 19  ASP A C     1 1 
ATOM   153  O  O     . ASP A 1 19  ? 13.698  3.352   16.47   1 31.54  ? 19  ASP A O     1 1 
ATOM   154  C  CB    . ASP A 1 19  ? 15.606  5.536   17.901  1 32.71  ? 19  ASP A CB    1 1 
ATOM   155  C  CG    . ASP A 1 19  ? 16.727  5.708   18.91   1 37.96  ? 19  ASP A CG    1 1 
ATOM   156  O  OD1   . ASP A 1 19  ? 17.524  4.749   19.09   1 38.63  ? 19  ASP A OD1   1 1 
ATOM   157  O  OD2   . ASP A 1 19  ? 16.828  6.808   19.502  1 40.51  ? 19  ASP A OD2   1 1 
ATOM   158  N  N     . LEU A 1 20  ? 14.475  4.794   14.891  1 30.85  ? 20  LEU A N     1 1 
ATOM   159  C  CA    . LEU A 1 20  ? 13.37   4.607   13.947  1 31.25  ? 20  LEU A CA    1 1 
ATOM   160  C  C     . LEU A 1 20  ? 13.363  3.171   13.425  1 32.13  ? 20  LEU A C     1 1 
ATOM   161  O  O     . LEU A 1 20  ? 12.319  2.535   13.416  1 32.03  ? 20  LEU A O     1 1 
ATOM   162  C  CB    . LEU A 1 20  ? 13.485  5.575   12.766  1 31.17  ? 20  LEU A CB    1 1 
ATOM   163  C  CG    . LEU A 1 20  ? 12.969  6.967   13.005  1 32.62  ? 20  LEU A CG    1 1 
ATOM   164  C  CD1   . LEU A 1 20  ? 13.261  7.844   11.831  1 32.98  ? 20  LEU A CD1   1 1 
ATOM   165  C  CD2   . LEU A 1 20  ? 11.483  6.951   13.243  1 33.8   ? 20  LEU A CD2   1 1 
ATOM   166  N  N     . ILE A 1 21  ? 14.534  2.654   13.028  1 32.94  ? 21  ILE A N     1 1 
ATOM   167  C  CA    . ILE A 1 21  ? 14.706  1.287   12.542  1 34     ? 21  ILE A CA    1 1 
ATOM   168  C  C     . ILE A 1 21  ? 14.371  0.285   13.663  1 35.39  ? 21  ILE A C     1 1 
ATOM   169  O  O     . ILE A 1 21  ? 13.531  -0.591  13.469  1 35.45  ? 21  ILE A O     1 1 
ATOM   170  C  CB    . ILE A 1 21  ? 16.156  1.095   12.003  1 34.21  ? 21  ILE A CB    1 1 
ATOM   171  C  CG1   . ILE A 1 21  ? 16.393  1.913   10.732  1 34.85  ? 21  ILE A CG1   1 1 
ATOM   172  C  CG2   . ILE A 1 21  ? 16.473  -0.373  11.766  1 34.59  ? 21  ILE A CG2   1 1 
ATOM   173  C  CD1   . ILE A 1 21  ? 17.787  2.11    10.425  1 35.99  ? 21  ILE A CD1   1 1 
ATOM   174  N  N     . LEU A 1 22  ? 14.982  0.456   14.848  1 36.34  ? 22  LEU A N     1 1 
ATOM   175  C  CA    . LEU A 1 22  ? 14.781  -0.413  16.003  1 37.91  ? 22  LEU A CA    1 1 
ATOM   176  C  C     . LEU A 1 22  ? 13.373  -0.423  16.568  1 40.04  ? 22  LEU A C     1 1 
ATOM   177  O  O     . LEU A 1 22  ? 13.014  -1.345  17.298  1 40.04  ? 22  LEU A O     1 1 
ATOM   178  C  CB    . LEU A 1 22  ? 15.776  -0.072  17.104  1 37.81  ? 22  LEU A CB    1 1 
ATOM   179  C  CG    . LEU A 1 22  ? 17.238  -0.326  16.785  1 38.88  ? 22  LEU A CG    1 1 
ATOM   180  C  CD1   . LEU A 1 22  ? 18.085  0.013   17.965  1 39.61  ? 22  LEU A CD1   1 1 
ATOM   181  C  CD2   . LEU A 1 22  ? 17.49   -1.767  16.386  1 39.23  ? 22  LEU A CD2   1 1 
ATOM   182  N  N     . SER A 1 23  ? 12.582  0.601   16.257  1 41.61  ? 23  SER A N     1 1 
ATOM   183  C  CA    . SER A 1 23  ? 11.2    0.666   16.705  1 43.41  ? 23  SER A CA    1 1 
ATOM   184  C  C     . SER A 1 23  ? 10.333  -0.381  15.99   1 45.22  ? 23  SER A C     1 1 
ATOM   185  O  O     . SER A 1 23  ? 9.301   -0.776  16.528  1 45.77  ? 23  SER A O     1 1 
ATOM   186  C  CB    . SER A 1 23  ? 10.632  2.062   16.474  1 44.91  ? 23  SER A CB    1 1 
ATOM   187  O  OG    . SER A 1 23  ? 10.484  2.345   15.091  1 47.37  ? 23  SER A OG    1 1 
ATOM   188  N  N     . LYS A 1 24  ? 10.727  -0.82   14.781  1 46.1   ? 24  LYS A N     1 1 
ATOM   189  C  CA    . LYS A 1 24  ? 9.967   -1.825  14.042  1 47.52  ? 24  LYS A CA    1 1 
ATOM   190  C  C     . LYS A 1 24  ? 10.728  -3.165  14.021  1 47.75  ? 24  LYS A C     1 1 
ATOM   191  O  O     . LYS A 1 24  ? 10.118  -4.223  14.165  1 47.6   ? 24  LYS A O     1 1 
ATOM   192  C  CB    . LYS A 1 24  ? 9.621   -1.316  12.625  1 50.47  ? 24  LYS A CB    1 1 
ATOM   193  C  CG    . LYS A 1 24  ? 8.551   -2.14   11.912  1 56.02  ? 24  LYS A CG    1 1 
ATOM   194  C  CD    . LYS A 1 24  ? 9.084   -2.69   10.588  1 61.3   ? 24  LYS A CD    1 1 
ATOM   195  C  CE    . LYS A 1 24  ? 8.388   -3.937  10.088  1 65.12  ? 24  LYS A CE    1 1 
ATOM   196  N  NZ    . LYS A 1 24  ? 9.081   -4.492  8.891   1 67.28  ? 24  LYS A NZ    1 1 
ATOM   197  N  N     . ILE A 1 25  ? 12.066  -3.102  13.896  1 48.03  ? 25  ILE A N     1 1 
ATOM   198  C  CA    . ILE A 1 25  ? 12.961  -4.26   13.898  1 48.59  ? 25  ILE A CA    1 1 
ATOM   199  C  C     . ILE A 1 25  ? 13.196  -4.713  15.33   1 48.78  ? 25  ILE A C     1 1 
ATOM   200  O  O     . ILE A 1 25  ? 13.688  -3.924  16.144  1 48.95  ? 25  ILE A O     1 1 
ATOM   201  C  CB    . ILE A 1 25  ? 14.335  -3.871  13.279  1 49.35  ? 25  ILE A CB    1 1 
ATOM   202  C  CG1   . ILE A 1 25  ? 14.214  -3.467  11.811  1 50.35  ? 25  ILE A CG1   1 1 
ATOM   203  C  CG2   . ILE A 1 25  ? 15.389  -4.968  13.472  1 49.94  ? 25  ILE A CG2   1 1 
ATOM   204  C  CD1   . ILE A 1 25  ? 13.719  -4.559  10.915  1 51.76  ? 25  ILE A CD1   1 1 
ATOM   205  N  N     . ASN A 1 26  ? 12.898  -5.98   15.635  1 48.5   ? 26  ASN A N     1 1 
ATOM   206  C  CA    . ASN A 1 26  ? 13.193  -6.524  16.955  1 48.58  ? 26  ASN A CA    1 1 
ATOM   207  C  C     . ASN A 1 26  ? 14.374  -7.457  16.728  1 48.05  ? 26  ASN A C     1 1 
ATOM   208  O  O     . ASN A 1 26  ? 14.208  -8.549  16.184  1 48.43  ? 26  ASN A O     1 1 
ATOM   209  C  CB    . ASN A 1 26  ? 11.972  -7.214  17.573  1 50     ? 26  ASN A CB    1 1 
ATOM   210  C  CG    . ASN A 1 26  ? 10.922  -6.214  18.049  1 54.07  ? 26  ASN A CG    1 1 
ATOM   211  O  OD1   . ASN A 1 26  ? 11.211  -5.255  18.788  1 55.2   ? 26  ASN A OD1   1 1 
ATOM   212  N  ND2   . ASN A 1 26  ? 9.675   -6.402  17.628  1 55.11  ? 26  ASN A ND2   1 1 
ATOM   213  N  N     . PRO A 1 27  ? 15.602  -6.967  16.985  1 46.92  ? 27  PRO A N     1 1 
ATOM   214  C  CA    . PRO A 1 27  ? 16.784  -7.768  16.663  1 46.24  ? 27  PRO A CA    1 1 
ATOM   215  C  C     . PRO A 1 27  ? 17.081  -8.892  17.632  1 45.7   ? 27  PRO A C     1 1 
ATOM   216  O  O     . PRO A 1 27  ? 16.804  -8.794  18.823  1 46.05  ? 27  PRO A O     1 1 
ATOM   217  C  CB    . PRO A 1 27  ? 17.923  -6.744  16.626  1 47.01  ? 27  PRO A CB    1 1 
ATOM   218  C  CG    . PRO A 1 27  ? 17.296  -5.408  16.895  1 47.64  ? 27  PRO A CG    1 1 
ATOM   219  C  CD    . PRO A 1 27  ? 15.98   -5.661  17.545  1 46.24  ? 27  PRO A CD    1 1 
ATOM   220  N  N     . GLN A 1 28  ? 17.661  -9.958  17.102  1 44.64  ? 28  GLN A N     1 1 
ATOM   221  C  CA    . GLN A 1 28  ? 18.052  -11.14  17.852  1 44.04  ? 28  GLN A CA    1 1 
ATOM   222  C  C     . GLN A 1 28  ? 19.413  -10.898 18.522  1 42.5   ? 28  GLN A C     1 1 
ATOM   223  O  O     . GLN A 1 28  ? 19.628  -11.314 19.661  1 42.56  ? 28  GLN A O     1 1 
ATOM   224  C  CB    . GLN A 1 28  ? 18.133  -12.347 16.904  1 46.39  ? 28  GLN A CB    1 1 
ATOM   225  C  CG    . GLN A 1 28  ? 16.94   -12.491 15.966  1 51.47  ? 28  GLN A CG    1 1 
ATOM   226  C  CD    . GLN A 1 28  ? 15.673  -12.817 16.715  1 58     ? 28  GLN A CD    1 1 
ATOM   227  O  OE1   . GLN A 1 28  ? 15.556  -13.887 17.332  1 60.56  ? 28  GLN A OE1   1 1 
ATOM   228  N  NE2   . GLN A 1 28  ? 14.692  -11.91  16.668  1 58.22  ? 28  GLN A NE2   1 1 
ATOM   229  N  N     . LYS A 1 29  ? 20.341  -10.244 17.805  1 40.85  ? 29  LYS A N     1 1 
ATOM   230  C  CA    . LYS A 1 29  ? 21.669  -9.934  18.322  1 39.6   ? 29  LYS A CA    1 1 
ATOM   231  C  C     . LYS A 1 29  ? 21.995  -8.488  17.97   1 38.51  ? 29  LYS A C     1 1 
ATOM   232  O  O     . LYS A 1 29  ? 21.827  -8.093  16.821  1 38.45  ? 29  LYS A O     1 1 
ATOM   233  C  CB    . LYS A 1 29  ? 22.722  -10.85  17.683  1 40.86  ? 29  LYS A CB    1 1 
ATOM   234  C  CG    . LYS A 1 29  ? 22.446  -12.348 17.797  1 44.45  ? 29  LYS A CG    1 1 
ATOM   235  C  CD    . LYS A 1 29  ? 23.317  -13.164 16.818  1 48.15  ? 29  LYS A CD    1 1 
ATOM   236  C  CE    . LYS A 1 29  ? 23.033  -14.654 16.812  1 51.03  ? 29  LYS A CE    1 1 
ATOM   237  N  NZ    . LYS A 1 29  ? 23.735  -15.347 15.697  1 52.56  ? 29  LYS A NZ    1 1 
ATOM   238  N  N     . VAL A 1 30  ? 22.432  -7.688  18.956  1 37.53  ? 30  VAL A N     1 1 
ATOM   239  C  CA    . VAL A 1 30  ? 22.821  -6.285  18.752  1 36.82  ? 30  VAL A CA    1 1 
ATOM   240  C  C     . VAL A 1 30  ? 24.195  -6.082  19.358  1 36.32  ? 30  VAL A C     1 1 
ATOM   241  O  O     . VAL A 1 30  ? 24.416  -6.461  20.505  1 36.71  ? 30  VAL A O     1 1 
ATOM   242  C  CB    . VAL A 1 30  ? 21.847  -5.281  19.399  1 37.1   ? 30  VAL A CB    1 1 
ATOM   243  C  CG1   . VAL A 1 30  ? 22.324  -3.851  19.177  1 37.55  ? 30  VAL A CG1   1 1 
ATOM   244  C  CG2   . VAL A 1 30  ? 20.433  -5.464  18.88   1 37.32  ? 30  VAL A CG2   1 1 
ATOM   245  N  N     . LYS A 1 31  ? 25.107  -5.465  18.617  1 35.26  ? 31  LYS A N     1 1 
ATOM   246  C  CA    . LYS A 1 31  ? 26.45   -5.207  19.101  1 34.6   ? 31  LYS A CA    1 1 
ATOM   247  C  C     . LYS A 1 31  ? 26.803  -3.769  18.772  1 34.56  ? 31  LYS A C     1 1 
ATOM   248  O  O     . LYS A 1 31  ? 26.589  -3.327  17.653  1 34.73  ? 31  LYS A O     1 1 
ATOM   249  C  CB    . LYS A 1 31  ? 27.424  -6.158  18.408  1 35.42  ? 31  LYS A CB    1 1 
ATOM   250  C  CG    . LYS A 1 31  ? 28.883  -5.981  18.785  1 38.35  ? 31  LYS A CG    1 1 
ATOM   251  C  CD    . LYS A 1 31  ? 29.733  -6.825  17.849  1 41.29  ? 31  LYS A CD    1 1 
ATOM   252  C  CE    . LYS A 1 31  ? 31.186  -6.88   18.205  1 44.55  ? 31  LYS A CE    1 1 
ATOM   253  N  NZ    . LYS A 1 31  ? 31.937  -7.667  17.195  1 46.84  ? 31  LYS A NZ    1 1 
ATOM   254  N  N     . ARG A 1 32  ? 27.308  -3.026  19.745  1 34.08  ? 32  ARG A N     1 1 
ATOM   255  C  CA    . ARG A 1 32  ? 27.718  -1.645  19.529  1 33.93  ? 32  ARG A CA    1 1 
ATOM   256  C  C     . ARG A 1 32  ? 29.225  -1.485  19.805  1 33.49  ? 32  ARG A C     1 1 
ATOM   257  O  O     . ARG A 1 32  ? 29.837  -2.313  20.478  1 33.55  ? 32  ARG A O     1 1 
ATOM   258  C  CB    . ARG A 1 32  ? 26.898  -0.696  20.405  1 35.27  ? 32  ARG A CB    1 1 
ATOM   259  C  CG    . ARG A 1 32  ? 25.46   -0.51   19.969  1 38.52  ? 32  ARG A CG    1 1 
ATOM   260  C  CD    . ARG A 1 32  ? 24.771  0.414   20.954  1 42.14  ? 32  ARG A CD    1 1 
ATOM   261  N  NE    . ARG A 1 32  ? 23.404  0.766   20.569  1 45.4   ? 32  ARG A NE    1 1 
ATOM   262  C  CZ    . ARG A 1 32  ? 23.088  1.776   19.764  1 48.06  ? 32  ARG A CZ    1 1 
ATOM   263  N  NH1   . ARG A 1 32  ? 24.042  2.525   19.218  1 48.1   ? 32  ARG A NH1   1 1 
ATOM   264  N  NH2   . ARG A 1 32  ? 21.815  2.04    19.49   1 47.92  ? 32  ARG A NH2   1 1 
ATOM   265  N  N     . GLY A 1 33  ? 29.812  -0.435  19.263  1 32.74  ? 33  GLY A N     1 1 
ATOM   266  C  CA    . GLY A 1 33  ? 31.228  -0.16   19.455  1 32.68  ? 33  GLY A CA    1 1 
ATOM   267  C  C     . GLY A 1 33  ? 31.704  0.95    18.547  1 32.23  ? 33  GLY A C     1 1 
ATOM   268  O  O     . GLY A 1 33  ? 30.923  1.83    18.191  1 32.67  ? 33  GLY A O     1 1 
ATOM   269  N  N     . PHE A 1 34  ? 32.973  0.913   18.145  1 31.18  ? 34  PHE A N     1 1 
ATOM   270  C  CA    . PHE A 1 34  ? 33.506  1.916   17.232  1 30.65  ? 34  PHE A CA    1 1 
ATOM   271  C  C     . PHE A 1 34  ? 34.256  1.225   16.108  1 29.84  ? 34  PHE A C     1 1 
ATOM   272  O  O     . PHE A 1 34  ? 35.004  0.288   16.366  1 29.89  ? 34  PHE A O     1 1 
ATOM   273  C  CB    . PHE A 1 34  ? 34.472  2.873   17.97   1 30.41  ? 34  PHE A CB    1 1 
ATOM   274  C  CG    . PHE A 1 34  ? 33.847  3.951   18.824  1 30.6   ? 34  PHE A CG    1 1 
ATOM   275  C  CD1   . PHE A 1 34  ? 33.419  3.679   20.106  1 31.42  ? 34  PHE A CD1   1 1 
ATOM   276  C  CD2   . PHE A 1 34  ? 33.735  5.245   18.36   1 31.16  ? 34  PHE A CD2   1 1 
ATOM   277  C  CE1   . PHE A 1 34  ? 32.843  4.671   20.885  1 32.14  ? 34  PHE A CE1   1 1 
ATOM   278  C  CE2   . PHE A 1 34  ? 33.17   6.238   19.147  1 31.92  ? 34  PHE A CE2   1 1 
ATOM   279  C  CZ    . PHE A 1 34  ? 32.717  5.943   20.4    1 31.81  ? 34  PHE A CZ    1 1 
ATOM   280  N  N     . ILE A 1 35  ? 34.078  1.687   14.869  1 28.96  ? 35  ILE A N     1 1 
ATOM   281  C  CA    . ILE A 1 35  ? 34.881  1.186   13.749  1 28.53  ? 35  ILE A CA    1 1 
ATOM   282  C  C     . ILE A 1 35  ? 36.222  1.991   13.662  1 28.58  ? 35  ILE A C     1 1 
ATOM   283  O  O     . ILE A 1 35  ? 37.248  1.467   13.205  1 29.07  ? 35  ILE A O     1 1 
ATOM   284  C  CB    . ILE A 1 35  ? 34.109  1.193   12.418  1 28.5   ? 35  ILE A CB    1 1 
ATOM   285  C  CG1   . ILE A 1 35  ? 33.683  2.611   12.025  1 29.18  ? 35  ILE A CG1   1 1 
ATOM   286  C  CG2   . ILE A 1 35  ? 32.92   0.266   12.5    1 28.83  ? 35  ILE A CG2   1 1 
ATOM   287  C  CD1   . ILE A 1 35  ? 33.549  2.814   10.581  1 30.41  ? 35  ILE A CD1   1 1 
ATOM   288  N  N     . SER A 1 36  ? 36.189  3.263   14.121  1 27.63  ? 36  SER A N     1 1 
ATOM   289  C  CA    . SER A 1 36  ? 37.275  4.23    14.221  1 26.89  ? 36  SER A CA    1 1 
ATOM   290  C  C     . SER A 1 36  ? 36.998  5.119   15.461  1 26.36  ? 36  SER A C     1 1 
ATOM   291  O  O     . SER A 1 36  ? 35.963  4.978   16.087  1 26.34  ? 36  SER A O     1 1 
ATOM   292  C  CB    . SER A 1 36  ? 37.346  5.072   12.951  1 27.71  ? 36  SER A CB    1 1 
ATOM   293  O  OG    . SER A 1 36  ? 36.333  6.064   12.918  1 29.26  ? 36  SER A OG    1 1 
ATOM   294  N  N     . LEU A 1 37  ? 37.902  6.03    15.809  1 26.19  ? 37  LEU A N     1 1 
ATOM   295  C  CA    . LEU A 1 37  ? 37.742  6.903   16.967  1 26.29  ? 37  LEU A CA    1 1 
ATOM   296  C  C     . LEU A 1 37  ? 36.536  7.822   16.834  1 27.01  ? 37  LEU A C     1 1 
ATOM   297  O  O     . LEU A 1 37  ? 35.839  8.083   17.817  1 27.28  ? 37  LEU A O     1 1 
ATOM   298  C  CB    . LEU A 1 37  ? 39.031  7.699   17.177  1 26.24  ? 37  LEU A CB    1 1 
ATOM   299  C  CG    . LEU A 1 37  ? 40.227  6.847   17.631  1 27.47  ? 37  LEU A CG    1 1 
ATOM   300  C  CD1   . LEU A 1 37  ? 41.548  7.471   17.239  1 28.13  ? 37  LEU A CD1   1 1 
ATOM   301  C  CD2   . LEU A 1 37  ? 40.174  6.59    19.115  1 27.93  ? 37  LEU A CD2   1 1 
ATOM   302  N  N     . SER A 1 38  ? 36.238  8.254   15.609  1 27.11  ? 38  SER A N     1 1 
ATOM   303  C  CA    . SER A 1 38  ? 35.113  9.148   15.336  1 27.47  ? 38  SER A CA    1 1 
ATOM   304  C  C     . SER A 1 38  ? 33.801  8.463   15.001  1 27.18  ? 38  SER A C     1 1 
ATOM   305  O  O     . SER A 1 38  ? 32.763  9.115   15.02   1 27.44  ? 38  SER A O     1 1 
ATOM   306  C  CB    . SER A 1 38  ? 35.453  10.026  14.142  1 29.19  ? 38  SER A CB    1 1 
ATOM   307  O  OG    . SER A 1 38  ? 36.352  11.051  14.514  1 31.74  ? 38  SER A OG    1 1 
ATOM   308  N  N     . CYS A 1 39  ? 33.856  7.204   14.583  1 26.54  ? 39  CYS A N     1 1 
ATOM   309  C  CA    . CYS A 1 39  ? 32.687  6.513   14.096  1 26.45  ? 39  CYS A CA    1 1 
ATOM   310  C  C     . CYS A 1 39  ? 32.206  5.388   14.946  1 25.81  ? 39  CYS A C     1 1 
ATOM   311  O  O     . CYS A 1 39  ? 32.69   4.258   14.79   1 25.66  ? 39  CYS A O     1 1 
ATOM   312  C  CB    . CYS A 1 39  ? 32.932  6.024   12.676  1 27.89  ? 39  CYS A CB    1 1 
ATOM   313  S  SG    . CYS A 1 39  ? 33.503  7.308   11.543  1 34.06  ? 39  CYS A SG    1 1 
ATOM   314  N  N     . PRO A 1 40  ? 31.132  5.616   15.723  1 24.97  ? 40  PRO A N     1 1 
ATOM   315  C  CA    . PRO A 1 40  ? 30.506  4.485   16.417  1 24.03  ? 40  PRO A CA    1 1 
ATOM   316  C  C     . PRO A 1 40  ? 29.732  3.619   15.43   1 23.23  ? 40  PRO A C     1 1 
ATOM   317  O  O     . PRO A 1 40  ? 29.46   4.036   14.304  1 23.05  ? 40  PRO A O     1 1 
ATOM   318  C  CB    . PRO A 1 40  ? 29.545  5.143   17.413  1 24.84  ? 40  PRO A CB    1 1 
ATOM   319  C  CG    . PRO A 1 40  ? 29.631  6.599   17.182  1 25.68  ? 40  PRO A CG    1 1 
ATOM   320  C  CD    . PRO A 1 40  ? 30.393  6.874   15.937  1 24.36  ? 40  PRO A CD    1 1 
ATOM   321  N  N     . PHE A 1 41  ? 29.368  2.422   15.854  1 22.96  ? 41  PHE A N     1 1 
ATOM   322  C  CA    . PHE A 1 41  ? 28.567  1.543   15.028  1 23.21  ? 41  PHE A CA    1 1 
ATOM   323  C  C     . PHE A 1 41  ? 27.503  0.827   15.845  1 24.12  ? 41  PHE A C     1 1 
ATOM   324  O  O     . PHE A 1 41  ? 27.581  0.769   17.074  1 24.63  ? 41  PHE A O     1 1 
ATOM   325  C  CB    . PHE A 1 41  ? 29.442  0.556   14.223  1 22.77  ? 41  PHE A CB    1 1 
ATOM   326  C  CG    . PHE A 1 41  ? 29.952  -0.631  15      1 23.4   ? 41  PHE A CG    1 1 
ATOM   327  C  CD1   . PHE A 1 41  ? 29.17   -1.758  15.17   1 24.04  ? 41  PHE A CD1   1 1 
ATOM   328  C  CD2   . PHE A 1 41  ? 31.233  -0.647  15.505  1 24.52  ? 41  PHE A CD2   1 1 
ATOM   329  C  CE1   . PHE A 1 41  ? 29.626  -2.836  15.912  1 24.65  ? 41  PHE A CE1   1 1 
ATOM   330  C  CE2   . PHE A 1 41  ? 31.703  -1.75   16.21   1 25.18  ? 41  PHE A CE2   1 1 
ATOM   331  C  CZ    . PHE A 1 41  ? 30.891  -2.83   16.42   1 24.59  ? 41  PHE A CZ    1 1 
ATOM   332  N  N     . ILE A 1 42  ? 26.494  0.293   15.145  1 23.92  ? 42  ILE A N     1 1 
ATOM   333  C  CA    . ILE A 1 42  ? 25.51   -0.621  15.688  1 23.73  ? 42  ILE A CA    1 1 
ATOM   334  C  C     . ILE A 1 42  ? 25.388  -1.765  14.679  1 23.31  ? 42  ILE A C     1 1 
ATOM   335  O  O     . ILE A 1 42  ? 25.129  -1.524  13.506  1 23.61  ? 42  ILE A O     1 1 
ATOM   336  C  CB    . ILE A 1 42  ? 24.157  -0.005  16.102  1 24.13  ? 42  ILE A CB    1 1 
ATOM   337  C  CG1   . ILE A 1 42  ? 23.217  -1.117  16.621  1 24.87  ? 42  ILE A CG1   1 1 
ATOM   338  C  CG2   . ILE A 1 42  ? 23.529  0.783   14.963  1 24.56  ? 42  ILE A CG2   1 1 
ATOM   339  C  CD1   . ILE A 1 42  ? 22.034  -0.66   17.273  1 26.11  ? 42  ILE A CD1   1 1 
ATOM   340  N  N     . GLU A 1 43  ? 25.668  -2.983  15.106  1 22.57  ? 43  GLU A N     1 1 
ATOM   341  C  CA    . GLU A 1 43  ? 25.59   -4.151  14.254  1 22.95  ? 43  GLU A CA    1 1 
ATOM   342  C  C     . GLU A 1 43  ? 24.38   -4.95   14.713  1 23.66  ? 43  GLU A C     1 1 
ATOM   343  O  O     . GLU A 1 43  ? 24.242  -5.231  15.902  1 23.36  ? 43  GLU A O     1 1 
ATOM   344  C  CB    . GLU A 1 43  ? 26.874  -4.981  14.382  1 24.95  ? 43  GLU A CB    1 1 
ATOM   345  C  CG    . GLU A 1 43  ? 27.038  -5.989  13.269  1 29.48  ? 43  GLU A CG    1 1 
ATOM   346  C  CD    . GLU A 1 43  ? 28.34   -6.761  13.27   1 38.17  ? 43  GLU A CD    1 1 
ATOM   347  O  OE1   . GLU A 1 43  ? 29.29   -6.37   13.986  1 39.76  ? 43  GLU A OE1   1 1 
ATOM   348  O  OE2   . GLU A 1 43  ? 28.411  -7.77   12.536  1 42.2   ? 43  GLU A OE2   1 1 
ATOM   349  N  N     . ILE A 1 44  ? 23.46   -5.254  13.793  1 24.57  ? 44  ILE A N     1 1 
ATOM   350  C  CA    . ILE A 1 44  ? 22.246  -5.982  14.149  1 25.92  ? 44  ILE A CA    1 1 
ATOM   351  C  C     . ILE A 1 44  ? 22.002  -7.25   13.308  1 26.79  ? 44  ILE A C     1 1 
ATOM   352  O  O     . ILE A 1 44  ? 22.251  -7.294  12.101  1 27.26  ? 44  ILE A O     1 1 
ATOM   353  C  CB    . ILE A 1 44  ? 20.99   -5.066  14.145  1 26.61  ? 44  ILE A CB    1 1 
ATOM   354  C  CG1   . ILE A 1 44  ? 20.597  -4.628  12.735  1 27.83  ? 44  ILE A CG1   1 1 
ATOM   355  C  CG2   . ILE A 1 44  ? 21.139  -3.861  15.074  1 27.09  ? 44  ILE A CG2   1 1 
ATOM   356  C  CD1   . ILE A 1 44  ? 19.176  -4.01   12.679  1 29.32  ? 44  ILE A CD1   1 1 
ATOM   357  N  N     . ILE A 1 45  ? 21.523  -8.287  13.977  1 26.68  ? 45  ILE A N     1 1 
ATOM   358  C  CA    . ILE A 1 45  ? 21.111  -9.523  13.342  1 27.41  ? 45  ILE A CA    1 1 
ATOM   359  C  C     . ILE A 1 45  ? 19.628  -9.604  13.647  1 27.58  ? 45  ILE A C     1 1 
ATOM   360  O  O     . ILE A 1 45  ? 19.256  -9.627  14.816  1 27.54  ? 45  ILE A O     1 1 
ATOM   361  C  CB    . ILE A 1 45  ? 21.811  -10.767 13.927  1 28.35  ? 45  ILE A CB    1 1 
ATOM   362  C  CG1   . ILE A 1 45  ? 23.325  -10.731 13.72   1 29.79  ? 45  ILE A CG1   1 1 
ATOM   363  C  CG2   . ILE A 1 45  ? 21.193  -12.043 13.352  1 28.79  ? 45  ILE A CG2   1 1 
ATOM   364  C  CD1   . ILE A 1 45  ? 23.773  -10.82  12.303  1 31.4   ? 45  ILE A CD1   1 1 
ATOM   365  N  N     . PHE A 1 46  ? 18.783  -9.606  12.625  1 27.52  ? 46  PHE A N     1 1 
ATOM   366  C  CA    . PHE A 1 46  ? 17.34   -9.706  12.825  1 27.98  ? 46  PHE A CA    1 1 
ATOM   367  C  C     . PHE A 1 46  ? 16.724  -10.685 11.832  1 28.11  ? 46  PHE A C     1 1 
ATOM   368  O  O     . PHE A 1 46  ? 17.416  -11.131 10.92   1 28.4   ? 46  PHE A O     1 1 
ATOM   369  C  CB    . PHE A 1 46  ? 16.677  -8.323  12.748  1 28.1   ? 46  PHE A CB    1 1 
ATOM   370  C  CG    . PHE A 1 46  ? 16.674  -7.688  11.38   1 28.91  ? 46  PHE A CG    1 1 
ATOM   371  C  CD1   . PHE A 1 46  ? 17.742  -6.922  10.954  1 29.85  ? 46  PHE A CD1   1 1 
ATOM   372  C  CD2   . PHE A 1 46  ? 15.57   -7.792  10.553  1 29.6   ? 46  PHE A CD2   1 1 
ATOM   373  C  CE1   . PHE A 1 46  ? 17.722  -6.307  9.713   1 30.49  ? 46  PHE A CE1   1 1 
ATOM   374  C  CE2   . PHE A 1 46  ? 15.57   -7.212  9.297   1 30.27  ? 46  PHE A CE2   1 1 
ATOM   375  C  CZ    . PHE A 1 46  ? 16.638  -6.457  8.894   1 30.22  ? 46  PHE A CZ    1 1 
ATOM   376  N  N     . LYS A 1 47  ? 15.44   -11.034 12.002  1 27.83  ? 47  LYS A N     1 1 
ATOM   377  C  CA    . LYS A 1 47  ? 14.81   -11.977 11.093  1 28.34  ? 47  LYS A CA    1 1 
ATOM   378  C  C     . LYS A 1 47  ? 13.382  -11.633 10.726  1 28.83  ? 47  LYS A C     1 1 
ATOM   379  O  O     . LYS A 1 47  ? 12.631  -11.053 11.515  1 29.61  ? 47  LYS A O     1 1 
ATOM   380  C  CB    . LYS A 1 47  ? 14.887  -13.399 11.658  1 30.18  ? 47  LYS A CB    1 1 
ATOM   381  C  CG    . LYS A 1 47  ? 14.089  -13.554 12.943  1 34.11  ? 47  LYS A CG    1 1 
ATOM   382  C  CD    . LYS A 1 47  ? 14.473  -14.797 13.708  1 38.63  ? 47  LYS A CD    1 1 
ATOM   383  C  CE    . LYS A 1 47  ? 13.256  -15.557 14.183  1 42.7   ? 47  LYS A CE    1 1 
ATOM   384  N  NZ    . LYS A 1 47  ? 12.099  -14.669 14.504  1 45.02  ? 47  LYS A NZ    1 1 
ATOM   385  N  N     . GLU A 1 48  ? 13.003  -12.008 9.513   1 28.1   ? 48  GLU A N     1 1 
ATOM   386  C  CA    . GLU A 1 48  ? 11.654  -11.841 9.025   1 27.61  ? 48  GLU A CA    1 1 
ATOM   387  C  C     . GLU A 1 48  ? 11.149  -13.249 8.89    1 27.45  ? 48  GLU A C     1 1 
ATOM   388  O  O     . GLU A 1 48  ? 11.08   -13.8   7.792   1 27.45  ? 48  GLU A O     1 1 
ATOM   389  C  CB    . GLU A 1 48  ? 11.666  -11.128 7.686   1 28.77  ? 48  GLU A CB    1 1 
ATOM   390  C  CG    . GLU A 1 48  ? 12.194  -9.722  7.818   1 31.85  ? 48  GLU A CG    1 1 
ATOM   391  C  CD    . GLU A 1 48  ? 12.171  -8.921  6.536   1 36.62  ? 48  GLU A CD    1 1 
ATOM   392  O  OE1   . GLU A 1 48  ? 11.961  -9.522  5.457   1 36.58  ? 48  GLU A OE1   1 1 
ATOM   393  O  OE2   . GLU A 1 48  ? 12.388  -7.689  6.609   1 39.19  ? 48  GLU A OE2   1 1 
ATOM   394  N  N     . GLY A 1 49  ? 10.876  -13.848 10.038  1 27.2   ? 49  GLY A N     1 1 
ATOM   395  C  CA    . GLY A 1 49  ? 10.438  -15.229 10.111  1 27.4   ? 49  GLY A CA    1 1 
ATOM   396  C  C     . GLY A 1 49  ? 11.655  -16.107 9.983   1 27.32  ? 49  GLY A C     1 1 
ATOM   397  O  O     . GLY A 1 49  ? 12.508  -16.11  10.868  1 27.59  ? 49  GLY A O     1 1 
ATOM   398  N  N     . HIS A 1 50  ? 11.777  -16.799 8.854   1 26.78  ? 50  HIS A N     1 1 
ATOM   399  C  CA    . HIS A 1 50  ? 12.934  -17.642 8.57    1 26.7   ? 50  HIS A CA    1 1 
ATOM   400  C  C     . HIS A 1 50  ? 14.101  -16.867 7.901   1 26.8   ? 50  HIS A C     1 1 
ATOM   401  O  O     . HIS A 1 50  ? 15.233  -17.364 7.867   1 27.2   ? 50  HIS A O     1 1 
ATOM   402  C  CB    . HIS A 1 50  ? 12.517  -18.801 7.662   1 26.88  ? 50  HIS A CB    1 1 
ATOM   403  C  CG    . HIS A 1 50  ? 11.655  -19.829 8.321   1 28.12  ? 50  HIS A CG    1 1 
ATOM   404  N  ND1   . HIS A 1 50  ? 12.204  -20.859 9.061   1 29.47  ? 50  HIS A ND1   1 1 
ATOM   405  C  CD2   . HIS A 1 50  ? 10.314  -19.986 8.283   1 29.12  ? 50  HIS A CD2   1 1 
ATOM   406  C  CE1   . HIS A 1 50  ? 11.185  -21.599 9.46    1 29.95  ? 50  HIS A CE1   1 1 
ATOM   407  N  NE2   . HIS A 1 50  ? 10.028  -21.122 9.01    1 30.07  ? 50  HIS A NE2   1 1 
ATOM   408  N  N     . ASP A 1 51  ? 13.825  -15.675 7.344   1 26.32  ? 51  ASP A N     1 1 
ATOM   409  C  CA    . ASP A 1 51  ? 14.836  -14.894 6.633   1 26.42  ? 51  ASP A CA    1 1 
ATOM   410  C  C     . ASP A 1 51  ? 15.702  -14.026 7.56    1 26.63  ? 51  ASP A C     1 1 
ATOM   411  O  O     . ASP A 1 51  ? 15.238  -13.002 8.043   1 26.97  ? 51  ASP A O     1 1 
ATOM   412  C  CB    . ASP A 1 51  ? 14.168  -14.026 5.545   1 27.46  ? 51  ASP A CB    1 1 
ATOM   413  C  CG    . ASP A 1 51  ? 13.251  -14.778 4.592   1 30.2   ? 51  ASP A CG    1 1 
ATOM   414  O  OD1   . ASP A 1 51  ? 13.232  -16.018 4.64    1 30.09  ? 51  ASP A OD1   1 1 
ATOM   415  O  OD2   . ASP A 1 51  ? 12.551  -14.12  3.798   1 32.44  ? 51  ASP A OD2   1 1 
ATOM   416  N  N     . TYR A 1 52  ? 16.963  -14.408 7.781   1 26.36  ? 52  TYR A N     1 1 
ATOM   417  C  CA    . TYR A 1 52  ? 17.869  -13.64  8.633   1 26.56  ? 52  TYR A CA    1 1 
ATOM   418  C  C     . TYR A 1 52  ? 18.578  -12.527 7.867   1 26.34  ? 52  TYR A C     1 1 
ATOM   419  O  O     . TYR A 1 52  ? 18.874  -12.69  6.69    1 26.7   ? 52  TYR A O     1 1 
ATOM   420  C  CB    . TYR A 1 52  ? 18.915  -14.558 9.245   1 26.81  ? 52  TYR A CB    1 1 
ATOM   421  C  CG    . TYR A 1 52  ? 18.488  -15.18  10.548  1 28.04  ? 52  TYR A CG    1 1 
ATOM   422  C  CD1   . TYR A 1 52  ? 18.723  -14.541 11.755  1 29.22  ? 52  TYR A CD1   1 1 
ATOM   423  C  CD2   . TYR A 1 52  ? 17.877  -16.421 10.578  1 29.36  ? 52  TYR A CD2   1 1 
ATOM   424  C  CE1   . TYR A 1 52  ? 18.369  -15.126 12.961  1 30.48  ? 52  TYR A CE1   1 1 
ATOM   425  C  CE2   . TYR A 1 52  ? 17.503  -17.01  11.777  1 30.61  ? 52  TYR A CE2   1 1 
ATOM   426  C  CZ    . TYR A 1 52  ? 17.758  -16.362 12.969  1 31.79  ? 52  TYR A CZ    1 1 
ATOM   427  O  OH    . TYR A 1 52  ? 17.402  -16.935 14.166  1 34.01  ? 52  TYR A OH    1 1 
ATOM   428  N  N     . PHE A 1 53  ? 18.876  -11.409 8.544   1 25.5   ? 53  PHE A N     1 1 
ATOM   429  C  CA    . PHE A 1 53  ? 19.562  -10.26  7.963   1 25.04  ? 53  PHE A CA    1 1 
ATOM   430  C  C     . PHE A 1 53  ? 20.647  -9.768  8.897   1 24.27  ? 53  PHE A C     1 1 
ATOM   431  O  O     . PHE A 1 53  ? 20.473  -9.778  10.112  1 24.62  ? 53  PHE A O     1 1 
ATOM   432  C  CB    . PHE A 1 53  ? 18.586  -9.13   7.662   1 25.08  ? 53  PHE A CB    1 1 
ATOM   433  C  CG    . PHE A 1 53  ? 17.559  -9.518  6.636   1 26.17  ? 53  PHE A CG    1 1 
ATOM   434  C  CD1   . PHE A 1 53  ? 17.87   -9.518  5.29    1 27.21  ? 53  PHE A CD1   1 1 
ATOM   435  C  CD2   . PHE A 1 53  ? 16.299  -9.937  7.018   1 27.08  ? 53  PHE A CD2   1 1 
ATOM   436  C  CE1   . PHE A 1 53  ? 16.931  -9.907  4.345   1 27.95  ? 53  PHE A CE1   1 1 
ATOM   437  C  CE2   . PHE A 1 53  ? 15.368  -10.338 6.072   1 27.83  ? 53  PHE A CE2   1 1 
ATOM   438  C  CZ    . PHE A 1 53  ? 15.686  -10.311 4.741   1 27.67  ? 53  PHE A CZ    1 1 
ATOM   439  N  N     . HIS A 1 54  ? 21.768  -9.337  8.334   1 23.02  ? 54  HIS A N     1 1 
ATOM   440  C  CA    . HIS A 1 54  ? 22.895  -8.861  9.112   1 22.52  ? 54  HIS A CA    1 1 
ATOM   441  C  C     . HIS A 1 54  ? 23.246  -7.502  8.575   1 22.18  ? 54  HIS A C     1 1 
ATOM   442  O  O     . HIS A 1 54  ? 23.644  -7.389  7.419   1 22.54  ? 54  HIS A O     1 1 
ATOM   443  C  CB    . HIS A 1 54  ? 24.084  -9.814  8.905   1 23.12  ? 54  HIS A CB    1 1 
ATOM   444  C  CG    . HIS A 1 54  ? 25.28   -9.554  9.775   1 23.92  ? 54  HIS A CG    1 1 
ATOM   445  N  ND1   . HIS A 1 54  ? 26.443  -10.281 9.629   1 25.19  ? 54  HIS A ND1   1 1 
ATOM   446  C  CD2   . HIS A 1 54  ? 25.446  -8.667  10.783  1 24.75  ? 54  HIS A CD2   1 1 
ATOM   447  C  CE1   . HIS A 1 54  ? 27.269  -9.823  10.549  1 25.62  ? 54  HIS A CE1   1 1 
ATOM   448  N  NE2   . HIS A 1 54  ? 26.714  -8.849  11.263  1 25.58  ? 54  HIS A NE2   1 1 
ATOM   449  N  N     . TRP A 1 55  ? 23.092  -6.469  9.392   1 21.46  ? 55  TRP A N     1 1 
ATOM   450  C  CA    . TRP A 1 55  ? 23.399  -5.109  8.967   1 21.06  ? 55  TRP A CA    1 1 
ATOM   451  C  C     . TRP A 1 55  ? 24.338  -4.446  9.947   1 20.38  ? 55  TRP A C     1 1 
ATOM   452  O  O     . TRP A 1 55  ? 24.3    -4.736  11.138  1 20.2   ? 55  TRP A O     1 1 
ATOM   453  C  CB    . TRP A 1 55  ? 22.12   -4.263  8.909   1 21.02  ? 55  TRP A CB    1 1 
ATOM   454  C  CG    . TRP A 1 55  ? 21.136  -4.604  7.827   1 21.8   ? 55  TRP A CG    1 1 
ATOM   455  C  CD1   . TRP A 1 55  ? 21.345  -5.382  6.725   1 22.74  ? 55  TRP A CD1   1 1 
ATOM   456  C  CD2   . TRP A 1 55  ? 19.79   -4.112  7.722   1 22.09  ? 55  TRP A CD2   1 1 
ATOM   457  N  NE1   . TRP A 1 55  ? 20.201  -5.429  5.955   1 23.15  ? 55  TRP A NE1   1 1 
ATOM   458  C  CE2   . TRP A 1 55  ? 19.238  -4.643  6.54    1 22.93  ? 55  TRP A CE2   1 1 
ATOM   459  C  CE3   . TRP A 1 55  ? 19.003  -3.267  8.511   1 22.46  ? 55  TRP A CE3   1 1 
ATOM   460  C  CZ2   . TRP A 1 55  ? 17.941  -4.344  6.129   1 23.44  ? 55  TRP A CZ2   1 1 
ATOM   461  C  CZ3   . TRP A 1 55  ? 17.717  -2.993  8.111   1 23.22  ? 55  TRP A CZ3   1 1 
ATOM   462  C  CH2   . TRP A 1 55  ? 17.196  -3.53   6.937   1 23.37  ? 55  TRP A CH2   1 1 
ATOM   463  N  N     . ARG A 1 56  ? 25.157  -3.523  9.459   1 19.98  ? 56  ARG A N     1 1 
ATOM   464  C  CA    . ARG A 1 56  ? 26.009  -2.72   10.327  1 20.08  ? 56  ARG A CA    1 1 
ATOM   465  C  C     . ARG A 1 56  ? 25.861  -1.282  9.926   1 20.15  ? 56  ARG A C     1 1 
ATOM   466  O  O     . ARG A 1 56  ? 25.926  -0.953  8.747   1 20.33  ? 56  ARG A O     1 1 
ATOM   467  C  CB    . ARG A 1 56  ? 27.49   -3.131  10.334  1 21.04  ? 56  ARG A CB    1 1 
ATOM   468  C  CG    . ARG A 1 56  ? 28.228  -2.493  11.515  1 22.45  ? 56  ARG A CG    1 1 
ATOM   469  C  CD    . ARG A 1 56  ? 29.697  -2.787  11.517  1 24.39  ? 56  ARG A CD    1 1 
ATOM   470  N  NE    . ARG A 1 56  ? 30.385  -2.005  10.494  1 27.09  ? 56  ARG A NE    1 1 
ATOM   471  C  CZ    . ARG A 1 56  ? 31.121  -2.525  9.516   1 29.74  ? 56  ARG A CZ    1 1 
ATOM   472  N  NH1   . ARG A 1 56  ? 31.282  -3.84   9.423   1 29.69  ? 56  ARG A NH1   1 1 
ATOM   473  N  NH2   . ARG A 1 56  ? 31.715  -1.733  8.633   1 29.77  ? 56  ARG A NH2   1 1 
ATOM   474  N  N     . PHE A 1 57  ? 25.613  -0.43   10.903  1 19.92  ? 57  PHE A N     1 1 
ATOM   475  C  CA    . PHE A 1 57  ? 25.438  0.984   10.67   1 20     ? 57  PHE A CA    1 1 
ATOM   476  C  C     . PHE A 1 57  ? 26.628  1.732   11.251  1 20.58  ? 57  PHE A C     1 1 
ATOM   477  O  O     . PHE A 1 57  ? 26.811  1.726   12.456  1 20.63  ? 57  PHE A O     1 1 
ATOM   478  C  CB    . PHE A 1 57  ? 24.126  1.458   11.31   1 19.21  ? 57  PHE A CB    1 1 
ATOM   479  C  CG    . PHE A 1 57  ? 22.889  0.861   10.681  1 19.14  ? 57  PHE A CG    1 1 
ATOM   480  C  CD1   . PHE A 1 57  ? 22.343  1.407   9.535   1 19.46  ? 57  PHE A CD1   1 1 
ATOM   481  C  CD2   . PHE A 1 57  ? 22.265  -0.239  11.243  1 19.38  ? 57  PHE A CD2   1 1 
ATOM   482  C  CE1   . PHE A 1 57  ? 21.203  0.856   8.96    1 19.56  ? 57  PHE A CE1   1 1 
ATOM   483  C  CE2   . PHE A 1 57  ? 21.128  -0.784  10.661  1 19.4   ? 57  PHE A CE2   1 1 
ATOM   484  C  CZ    . PHE A 1 57  ? 20.61   -0.236  9.523   1 19.01  ? 57  PHE A CZ    1 1 
ATOM   485  N  N     . ASP A 1 58  ? 27.453  2.342   10.398  1 20.9   ? 58  ASP A N     1 1 
ATOM   486  C  CA    . ASP A 1 58  ? 28.61   3.131   10.834  1 21.65  ? 58  ASP A CA    1 1 
ATOM   487  C  C     . ASP A 1 58  ? 28.192  4.604   10.848  1 22.45  ? 58  ASP A C     1 1 
ATOM   488  O  O     . ASP A 1 58  ? 27.757  5.134   9.828   1 22.82  ? 58  ASP A O     1 1 
ATOM   489  C  CB    . ASP A 1 58  ? 29.819  2.903   9.905   1 22.25  ? 58  ASP A CB    1 1 
ATOM   490  C  CG    . ASP A 1 58  ? 30.282  1.46    9.869   1 25.81  ? 58  ASP A CG    1 1 
ATOM   491  O  OD1   . ASP A 1 58  ? 29.995  0.719   10.837  1 27.18  ? 58  ASP A OD1   1 1 
ATOM   492  O  OD2   . ASP A 1 58  ? 30.932  1.07    8.876   1 26.62  ? 58  ASP A OD2   1 1 
ATOM   493  N  N     . MET A 1 59  ? 28.284  5.244   12.005  1 22.29  ? 59  MET A N     1 1 
ATOM   494  C  CA    . MET A 1 59  ? 27.847  6.612   12.156  1 22.77  ? 59  MET A CA    1 1 
ATOM   495  C  C     . MET A 1 59  ? 28.966  7.63    11.959  1 22.94  ? 59  MET A C     1 1 
ATOM   496  O  O     . MET A 1 59  ? 30.047  7.451   12.476  1 22.95  ? 59  MET A O     1 1 
ATOM   497  C  CB    . MET A 1 59  ? 27.146  6.754   13.498  1 23.5   ? 59  MET A CB    1 1 
ATOM   498  C  CG    . MET A 1 59  ? 25.886  5.958   13.534  1 25.92  ? 59  MET A CG    1 1 
ATOM   499  S  SD    . MET A 1 59  ? 25.179  5.764   15.175  1 33.21  ? 59  MET A SD    1 1 
ATOM   500  C  CE    . MET A 1 59  ? 25.678  4.087   15.54   1 35.43  ? 59  MET A CE    1 1 
ATOM   501  N  N     . PHE A 1 60  ? 28.71   8.677   11.178  1 23.17  ? 60  PHE A N     1 1 
ATOM   502  C  CA    . PHE A 1 60  ? 29.669  9.732   10.883  1 24.21  ? 60  PHE A CA    1 1 
ATOM   503  C  C     . PHE A 1 60  ? 29.152  11.082  11.407  1 25.58  ? 60  PHE A C     1 1 
ATOM   504  O  O     . PHE A 1 60  ? 28.525  11.859  10.679  1 25.41  ? 60  PHE A O     1 1 
ATOM   505  C  CB    . PHE A 1 60  ? 29.931  9.806   9.378   1 24     ? 60  PHE A CB    1 1 
ATOM   506  C  CG    . PHE A 1 60  ? 30.847  8.725   8.878   1 24.54  ? 60  PHE A CG    1 1 
ATOM   507  C  CD1   . PHE A 1 60  ? 30.414  7.415   8.789   1 25.28  ? 60  PHE A CD1   1 1 
ATOM   508  C  CD2   . PHE A 1 60  ? 32.146  9.015   8.497   1 25.15  ? 60  PHE A CD2   1 1 
ATOM   509  C  CE1   . PHE A 1 60  ? 31.272  6.413   8.352   1 25.92  ? 60  PHE A CE1   1 1 
ATOM   510  C  CE2   . PHE A 1 60  ? 32.994  8.012   8.037   1 25.56  ? 60  PHE A CE2   1 1 
ATOM   511  C  CZ    . PHE A 1 60  ? 32.553  6.718   7.973   1 25.35  ? 60  PHE A CZ    1 1 
ATOM   512  N  N     . PRO A 1 61  ? 29.427  11.378  12.683  1 26.51  ? 61  PRO A N     1 1 
ATOM   513  C  CA    . PRO A 1 61  ? 28.922  12.623  13.266  1 27.42  ? 61  PRO A CA    1 1 
ATOM   514  C  C     . PRO A 1 61  ? 29.694  13.884  12.862  1 29.09  ? 61  PRO A C     1 1 
ATOM   515  O  O     . PRO A 1 61  ? 30.918  13.911  12.896  1 29.29  ? 61  PRO A O     1 1 
ATOM   516  C  CB    . PRO A 1 61  ? 28.973  12.351  14.781  1 27.79  ? 61  PRO A CB    1 1 
ATOM   517  C  CG    . PRO A 1 61  ? 29.461  10.91   14.94   1 27.92  ? 61  PRO A CG    1 1 
ATOM   518  C  CD    . PRO A 1 61  ? 30.154  10.571  13.68   1 26.1   ? 61  PRO A CD    1 1 
ATOM   519  N  N     . GLY A 1 62  ? 28.954  14.924  12.504  1 30.05  ? 62  GLY A N     1 1 
ATOM   520  C  CA    . GLY A 1 62  ? 29.496  16.217  12.116  1 31.53  ? 62  GLY A CA    1 1 
ATOM   521  C  C     . GLY A 1 62  ? 29.829  16.332  10.647  1 33.26  ? 62  GLY A C     1 1 
ATOM   522  O  O     . GLY A 1 62  ? 30.762  15.687  10.183  1 33.79  ? 62  GLY A O     1 1 
ATOM   523  N  N     . PHE A 1 63  ? 29.096  17.159  9.908   1 34.42  ? 63  PHE A N     1 1 
ATOM   524  C  CA    . PHE A 1 63  ? 29.357  17.357  8.482   1 36.34  ? 63  PHE A CA    1 1 
ATOM   525  C  C     . PHE A 1 63  ? 30.475  18.376  8.244   1 38.38  ? 63  PHE A C     1 1 
ATOM   526  O  O     . PHE A 1 63  ? 30.734  19.221  9.102   1 38.81  ? 63  PHE A O     1 1 
ATOM   527  C  CB    . PHE A 1 63  ? 28.099  17.883  7.777   1 36.34  ? 63  PHE A CB    1 1 
ATOM   528  C  CG    . PHE A 1 63  ? 26.972  16.905  7.603   1 36.74  ? 63  PHE A CG    1 1 
ATOM   529  C  CD1   . PHE A 1 63  ? 27.075  15.86   6.706   1 37.4   ? 63  PHE A CD1   1 1 
ATOM   530  C  CD2   . PHE A 1 63  ? 25.794  17.062  8.297   1 37.46  ? 63  PHE A CD2   1 1 
ATOM   531  C  CE1   . PHE A 1 63  ? 26.028  14.978  6.528   1 38.15  ? 63  PHE A CE1   1 1 
ATOM   532  C  CE2   . PHE A 1 63  ? 24.747  16.183  8.112   1 38.3   ? 63  PHE A CE2   1 1 
ATOM   533  C  CZ    . PHE A 1 63  ? 24.867  15.15   7.225   1 38.07  ? 63  PHE A CZ    1 1 
ATOM   534  N  N     . ASN A 1 64  ? 31.092  18.338  7.045   1 39.35  ? 64  ASN A N     1 1 
ATOM   535  C  CA    . ASN A 1 64  ? 32.121  19.296  6.641   1 40.45  ? 64  ASN A CA    1 1 
ATOM   536  C  C     . ASN A 1 64  ? 31.486  20.629  6.251   1 42.21  ? 64  ASN A C     1 1 
ATOM   537  O  O     . ASN A 1 64  ? 30.34   20.678  5.78    1 42.1   ? 64  ASN A O     1 1 
ATOM   538  C  CB    . ASN A 1 64  ? 32.867  18.79   5.414   1 40.72  ? 64  ASN A CB    1 1 
ATOM   539  C  CG    . ASN A 1 64  ? 33.874  17.732  5.693   1 43.58  ? 64  ASN A CG    1 1 
ATOM   540  O  OD1   . ASN A 1 64  ? 33.996  17.23   6.808   1 44.59  ? 64  ASN A OD1   1 1 
ATOM   541  N  ND2   . ASN A 1 64  ? 34.637  17.372  4.683   1 44.47  ? 64  ASN A ND2   1 1 
ATOM   542  N  N     . LYS A 1 65  ? 32.264  21.707  6.397   1 43.39  ? 65  LYS A N     1 1 
ATOM   543  C  CA    . LYS A 1 65  ? 31.851  23.041  5.975   1 44.77  ? 65  LYS A CA    1 1 
ATOM   544  C  C     . LYS A 1 65  ? 32.744  23.326  4.751   1 45.97  ? 65  LYS A C     1 1 
ATOM   545  O  O     . LYS A 1 65  ? 32.744  24.423  4.201   1 46.65  ? 65  LYS A O     1 1 
ATOM   546  C  CB    . LYS A 1 65  ? 32.088  24.104  7.082   1 46.42  ? 65  LYS A CB    1 1 
ATOM   547  C  CG    . LYS A 1 65  ? 31.808  23.647  8.518   1 50.03  ? 65  LYS A CG    1 1 
ATOM   548  C  CD    . LYS A 1 65  ? 30.404  23.953  8.969   1 54.25  ? 65  LYS A CD    1 1 
ATOM   549  C  CE    . LYS A 1 65  ? 29.825  22.88   9.86    1 57.59  ? 65  LYS A CE    1 1 
ATOM   550  N  NZ    . LYS A 1 65  ? 29.241  21.765  9.064   1 59.5   ? 65  LYS A NZ    1 1 
ATOM   551  N  N     . ASN A 1 68  ? 37.185  19.058  2.699   1 42.17  ? 68  ASN A N     1 1 
ATOM   552  C  CA    . ASN A 1 68  ? 38.164  18.351  3.528   1 42.72  ? 68  ASN A CA    1 1 
ATOM   553  C  C     . ASN A 1 68  ? 38.404  19.015  4.899   1 42.47  ? 68  ASN A C     1 1 
ATOM   554  O  O     . ASN A 1 68  ? 39.471  18.832  5.495   1 42.76  ? 68  ASN A O     1 1 
ATOM   555  C  CB    . ASN A 1 68  ? 39.483  18.155  2.771   1 44.57  ? 68  ASN A CB    1 1 
ATOM   556  C  CG    . ASN A 1 68  ? 40      19.402  2.07    1 48.98  ? 68  ASN A CG    1 1 
ATOM   557  O  OD1   . ASN A 1 68  ? 39.716  20.551  2.456   1 50.5   ? 68  ASN A OD1   1 1 
ATOM   558  N  ND2   . ASN A 1 68  ? 40.781  19.205  1.012   1 49.88  ? 68  ASN A ND2   1 1 
ATOM   559  N  N     . ASP A 1 69  ? 37.391  19.755  5.396   1 41.61  ? 69  ASP A N     1 1 
ATOM   560  C  CA    . ASP A 1 69  ? 37.359  20.483  6.667   1 41.24  ? 69  ASP A CA    1 1 
ATOM   561  C  C     . ASP A 1 69  ? 37.5    19.559  7.914   1 40.33  ? 69  ASP A C     1 1 
ATOM   562  O  O     . ASP A 1 69  ? 38.385  19.769  8.744   1 40.46  ? 69  ASP A O     1 1 
ATOM   563  C  CB    . ASP A 1 69  ? 36.067  21.327  6.699   1 43.24  ? 69  ASP A CB    1 1 
ATOM   564  C  CG    . ASP A 1 69  ? 35.691  21.928  8.034   1 48.63  ? 69  ASP A CG    1 1 
ATOM   565  O  OD1   . ASP A 1 69  ? 36.555  22.566  8.657   1 49.85  ? 69  ASP A OD1   1 1 
ATOM   566  O  OD2   . ASP A 1 69  ? 34.527  21.768  8.447   1 50.97  ? 69  ASP A OD2   1 1 
ATOM   567  N  N     . ARG A 1 70  ? 36.639  18.543  8.029   1 39.34  ? 70  ARG A N     1 1 
ATOM   568  C  CA    . ARG A 1 70  ? 36.658  17.571  9.12    1 38.89  ? 70  ARG A CA    1 1 
ATOM   569  C  C     . ARG A 1 70  ? 37.028  16.187  8.526   1 38.58  ? 70  ARG A C     1 1 
ATOM   570  O  O     . ARG A 1 70  ? 38.122  15.687  8.776   1 38.76  ? 70  ARG A O     1 1 
ATOM   571  C  CB    . ARG A 1 70  ? 35.297  17.583  9.863   1 39.46  ? 70  ARG A CB    1 1 
ATOM   572  C  CG    . ARG A 1 70  ? 34.935  16.327  10.649  1 40.8   ? 70  ARG A CG    1 1 
ATOM   573  C  CD    . ARG A 1 70  ? 33.914  16.643  11.731  1 42.36  ? 70  ARG A CD    1 1 
ATOM   574  N  NE    . ARG A 1 70  ? 33.439  15.466  12.468  1 44.17  ? 70  ARG A NE    1 1 
ATOM   575  C  CZ    . ARG A 1 70  ? 34.13   14.845  13.421  1 46.04  ? 70  ARG A CZ    1 1 
ATOM   576  N  NH1   . ARG A 1 70  ? 35.361  15.234  13.718  1 45.96  ? 70  ARG A NH1   1 1 
ATOM   577  N  NH2   . ARG A 1 70  ? 33.614  13.799  14.046  1 46.01  ? 70  ARG A NH2   1 1 
ATOM   578  N  N     . TRP A 1 71  ? 36.161  15.627  7.671   1 37.78  ? 71  TRP A N     1 1 
ATOM   579  C  CA    . TRP A 1 71  ? 36.377  14.351  6.999   1 37.44  ? 71  TRP A CA    1 1 
ATOM   580  C  C     . TRP A 1 71  ? 37.203  14.56   5.736   1 36.99  ? 71  TRP A C     1 1 
ATOM   581  O  O     . TRP A 1 71  ? 37.116  15.626  5.119   1 36.83  ? 71  TRP A O     1 1 
ATOM   582  C  CB    . TRP A 1 71  ? 35.032  13.72   6.64    1 37.31  ? 71  TRP A CB    1 1 
ATOM   583  C  CG    . TRP A 1 71  ? 34.11   13.582  7.812   1 37.62  ? 71  TRP A CG    1 1 
ATOM   584  C  CD1   . TRP A 1 71  ? 33.056  14.386  8.128   1 38.32  ? 71  TRP A CD1   1 1 
ATOM   585  C  CD2   . TRP A 1 71  ? 34.19   12.596  8.849   1 37.75  ? 71  TRP A CD2   1 1 
ATOM   586  N  NE1   . TRP A 1 71  ? 32.461  13.949  9.287   1 38.58  ? 71  TRP A NE1   1 1 
ATOM   587  C  CE2   . TRP A 1 71  ? 33.139  12.851  9.752   1 38.46  ? 71  TRP A CE2   1 1 
ATOM   588  C  CE3   . TRP A 1 71  ? 35.042  11.512  9.097   1 38.35  ? 71  TRP A CE3   1 1 
ATOM   589  C  CZ2   . TRP A 1 71  ? 32.92   12.062  10.881  1 39.05  ? 71  TRP A CZ2   1 1 
ATOM   590  C  CZ3   . TRP A 1 71  ? 34.821  10.733  10.216  1 39.08  ? 71  TRP A CZ3   1 1 
ATOM   591  C  CH2   . TRP A 1 71  ? 33.77   11.011  11.092  1 39.08  ? 71  TRP A CH2   1 1 
ATOM   592  N  N     . ASN A 1 72  ? 37.986  13.53   5.334   1 36.59  ? 72  ASN A N     1 1 
ATOM   593  C  CA    . ASN A 1 72  ? 38.865  13.584  4.157   1 36.47  ? 72  ASN A CA    1 1 
ATOM   594  C  C     . ASN A 1 72  ? 38.129  13.949  2.853   1 35.85  ? 72  ASN A C     1 1 
ATOM   595  O  O     . ASN A 1 72  ? 38.726  14.51   1.933   1 36.41  ? 72  ASN A O     1 1 
ATOM   596  C  CB    . ASN A 1 72  ? 39.661  12.29   4.004   1 37.59  ? 72  ASN A CB    1 1 
ATOM   597  C  CG    . ASN A 1 72  ? 38.893  11.149  3.388   1 40.78  ? 72  ASN A CG    1 1 
ATOM   598  O  OD1   . ASN A 1 72  ? 37.71   10.945  3.669   1 41.62  ? 72  ASN A OD1   1 1 
ATOM   599  N  ND2   . ASN A 1 72  ? 39.548  10.382  2.525   1 41.87  ? 72  ASN A ND2   1 1 
ATOM   600  N  N     . SER A 1 73  ? 36.847  13.592  2.778   1 34.29  ? 73  SER A N     1 1 
ATOM   601  C  CA    . SER A 1 73  ? 35.972  13.896  1.659   1 33.23  ? 73  SER A CA    1 1 
ATOM   602  C  C     . SER A 1 73  ? 34.587  14.215  2.205   1 31.81  ? 73  SER A C     1 1 
ATOM   603  O  O     . SER A 1 73  ? 34.226  13.771  3.298   1 31.81  ? 73  SER A O     1 1 
ATOM   604  C  CB    . SER A 1 73  ? 35.937  12.755  0.643   1 34.81  ? 73  SER A CB    1 1 
ATOM   605  O  OG    . SER A 1 73  ? 35.873  11.466  1.233   1 37.51  ? 73  SER A OG    1 1 
ATOM   606  N  N     . ASN A 1 74  ? 33.832  15.031  1.477   1 30.61  ? 74  ASN A N     1 1 
ATOM   607  C  CA    . ASN A 1 74  ? 32.514  15.433  1.929   1 30.25  ? 74  ASN A CA    1 1 
ATOM   608  C  C     . ASN A 1 74  ? 31.432  14.556  1.335   1 29.05  ? 74  ASN A C     1 1 
ATOM   609  O  O     . ASN A 1 74  ? 31.284  14.53   0.116   1 29.17  ? 74  ASN A O     1 1 
ATOM   610  C  CB    . ASN A 1 74  ? 32.262  16.892  1.562   1 31.69  ? 74  ASN A CB    1 1 
ATOM   611  C  CG    . ASN A 1 74  ? 31.075  17.496  2.273   1 34.7   ? 74  ASN A CG    1 1 
ATOM   612  O  OD1   . ASN A 1 74  ? 30.336  16.821  3.022   1 34.69  ? 74  ASN A OD1   1 1 
ATOM   613  N  ND2   . ASN A 1 74  ? 30.87   18.793  2.051   1 36.19  ? 74  ASN A ND2   1 1 
ATOM   614  N  N     . ILE A 1 75  ? 30.632  13.887  2.183   1 27.78  ? 75  ILE A N     1 1 
ATOM   615  C  CA    . ILE A 1 75  ? 29.515  13.075  1.678   1 27.05  ? 75  ILE A CA    1 1 
ATOM   616  C  C     . ILE A 1 75  ? 28.482  13.939  0.946   1 26.38  ? 75  ILE A C     1 1 
ATOM   617  O  O     . ILE A 1 75  ? 27.916  13.499  -0.048  1 26.41  ? 75  ILE A O     1 1 
ATOM   618  C  CB    . ILE A 1 75  ? 28.864  12.174  2.761   1 27.1   ? 75  ILE A CB    1 1 
ATOM   619  C  CG1   . ILE A 1 75  ? 28.086  11.012  2.121   1 27.71  ? 75  ILE A CG1   1 1 
ATOM   620  C  CG2   . ILE A 1 75  ? 27.997  12.976  3.729   1 27.29  ? 75  ILE A CG2   1 1 
ATOM   621  C  CD1   . ILE A 1 75  ? 28.94   10.095  1.282   1 28.48  ? 75  ILE A CD1   1 1 
ATOM   622  N  N     . LEU A 1 76  ? 28.299  15.19   1.38    1 25.77  ? 76  LEU A N     1 1 
ATOM   623  C  CA    . LEU A 1 76  ? 27.388  16.113  0.719   1 26.11  ? 76  LEU A CA    1 1 
ATOM   624  C  C     . LEU A 1 76  ? 27.754  16.401  -0.744  1 26.65  ? 76  LEU A C     1 1 
ATOM   625  O  O     . LEU A 1 76  ? 26.921  16.937  -1.482  1 27.12  ? 76  LEU A O     1 1 
ATOM   626  C  CB    . LEU A 1 76  ? 27.272  17.413  1.514   1 26.09  ? 76  LEU A CB    1 1 
ATOM   627  C  CG    . LEU A 1 76  ? 26.793  17.245  2.947   1 27.44  ? 76  LEU A CG    1 1 
ATOM   628  C  CD1   . LEU A 1 76  ? 26.867  18.552  3.692   1 28.04  ? 76  LEU A CD1   1 1 
ATOM   629  C  CD2   . LEU A 1 76  ? 25.381  16.654  3.003   1 27.9   ? 76  LEU A CD2   1 1 
ATOM   630  N  N     . ASP A 1 77  ? 28.974  16.028  -1.175  1 26.38  ? 77  ASP A N     1 1 
ATOM   631  C  CA    . ASP A 1 77  ? 29.389  16.199  -2.557  1 26.69  ? 77  ASP A CA    1 1 
ATOM   632  C  C     . ASP A 1 77  ? 28.549  15.303  -3.477  1 26.69  ? 77  ASP A C     1 1 
ATOM   633  O  O     . ASP A 1 77  ? 28.258  15.707  -4.597  1 26.64  ? 77  ASP A O     1 1 
ATOM   634  C  CB    . ASP A 1 77  ? 30.887  15.927  -2.724  1 28.6   ? 77  ASP A CB    1 1 
ATOM   635  C  CG    . ASP A 1 77  ? 31.504  16.659  -3.891  1 33.83  ? 77  ASP A CG    1 1 
ATOM   636  O  OD1   . ASP A 1 77  ? 31.281  17.88   -4.005  1 34.71  ? 77  ASP A OD1   1 1 
ATOM   637  O  OD2   . ASP A 1 77  ? 32.223  16.013  -4.686  1 36.34  ? 77  ASP A OD2   1 1 
ATOM   638  N  N     . LEU A 1 78  ? 28.102  14.127  -2.996  1 26.7   ? 78  LEU A N     1 1 
ATOM   639  C  CA    . LEU A 1 78  ? 27.236  13.257  -3.792  1 27.65  ? 78  LEU A CA    1 1 
ATOM   640  C  C     . LEU A 1 78  ? 25.901  13.95   -4.138  1 28.25  ? 78  LEU A C     1 1 
ATOM   641  O  O     . LEU A 1 78  ? 25.295  13.628  -5.161  1 28.41  ? 78  LEU A O     1 1 
ATOM   642  C  CB    . LEU A 1 78  ? 26.959  11.927  -3.071  1 28.09  ? 78  LEU A CB    1 1 
ATOM   643  C  CG    . LEU A 1 78  ? 28.143  10.989  -2.897  1 29.89  ? 78  LEU A CG    1 1 
ATOM   644  C  CD1   . LEU A 1 78  ? 27.76   9.796   -2.072  1 30.29  ? 78  LEU A CD1   1 1 
ATOM   645  C  CD2   . LEU A 1 78  ? 28.693  10.535  -4.242  1 30.72  ? 78  LEU A CD2   1 1 
ATOM   646  N  N     . LEU A 1 79  ? 25.444  14.888  -3.29   1 28.26  ? 79  LEU A N     1 1 
ATOM   647  C  CA    . LEU A 1 79  ? 24.228  15.625  -3.563  1 28.98  ? 79  LEU A CA    1 1 
ATOM   648  C  C     . LEU A 1 79  ? 24.496  16.674  -4.626  1 29.62  ? 79  LEU A C     1 1 
ATOM   649  O  O     . LEU A 1 79  ? 23.726  16.763  -5.582  1 30.17  ? 79  LEU A O     1 1 
ATOM   650  C  CB    . LEU A 1 79  ? 23.683  16.279  -2.297  1 29.24  ? 79  LEU A CB    1 1 
ATOM   651  C  CG    . LEU A 1 79  ? 23.208  15.327  -1.233  1 30.84  ? 79  LEU A CG    1 1 
ATOM   652  C  CD1   . LEU A 1 79  ? 22.8    16.081  -0.003  1 31.75  ? 79  LEU A CD1   1 1 
ATOM   653  C  CD2   . LEU A 1 79  ? 22.04   14.507  -1.722  1 31.21  ? 79  LEU A CD2   1 1 
ATOM   654  N  N     . SER A 1 80  ? 25.595  17.447  -4.499  1 29.37  ? 80  SER A N     1 1 
ATOM   655  C  CA    . SER A 1 80  ? 25.908  18.469  -5.503  1 29.71  ? 80  SER A CA    1 1 
ATOM   656  C  C     . SER A 1 80  ? 26.25   17.879  -6.874  1 29.84  ? 80  SER A C     1 1 
ATOM   657  O  O     . SER A 1 80  ? 26.074  18.555  -7.887  1 29.55  ? 80  SER A O     1 1 
ATOM   658  C  CB    . SER A 1 80  ? 26.987  19.427  -5.016  1 31.02  ? 80  SER A CB    1 1 
ATOM   659  O  OG    . SER A 1 80  ? 28.151  18.743  -4.592  1 33.37  ? 80  SER A OG    1 1 
ATOM   660  N  N     . GLN A 1 81  ? 26.712  16.614  -6.913  1 30.14  ? 81  GLN A N     1 1 
ATOM   661  C  CA    . GLN A 1 81  ? 26.979  15.906  -8.168  1 30.62  ? 81  GLN A CA    1 1 
ATOM   662  C  C     . GLN A 1 81  ? 25.667  15.606  -8.913  1 31.34  ? 81  GLN A C     1 1 
ATOM   663  O  O     . GLN A 1 81  ? 25.698  15.434  -10.124 1 31.69  ? 81  GLN A O     1 1 
ATOM   664  C  CB    . GLN A 1 81  ? 27.697  14.579  -7.906  1 31.42  ? 81  GLN A CB    1 1 
ATOM   665  C  CG    . GLN A 1 81  ? 29.125  14.728  -7.435  1 34.05  ? 81  GLN A CG    1 1 
ATOM   666  C  CD    . GLN A 1 81  ? 29.784  13.394  -7.156  1 37.01  ? 81  GLN A CD    1 1 
ATOM   667  O  OE1   . GLN A 1 81  ? 29.563  12.397  -7.853  1 38.17  ? 81  GLN A OE1   1 1 
ATOM   668  N  NE2   . GLN A 1 81  ? 30.649  13.349  -6.158  1 36.6   ? 81  GLN A NE2   1 1 
ATOM   669  N  N     . LYS A 1 82  ? 24.534  15.495  -8.195  1 31.36  ? 82  LYS A N     1 1 
ATOM   670  C  CA    . LYS A 1 82  ? 23.241  15.191  -8.796  1 31.98  ? 82  LYS A CA    1 1 
ATOM   671  C  C     . LYS A 1 82  ? 22.315  16.4    -8.963  1 32.21  ? 82  LYS A C     1 1 
ATOM   672  O  O     . LYS A 1 82  ? 21.141  16.212  -9.276  1 32.66  ? 82  LYS A O     1 1 
ATOM   673  C  CB    . LYS A 1 82  ? 22.524  14.067  -8.028  1 34.01  ? 82  LYS A CB    1 1 
ATOM   674  C  CG    . LYS A 1 82  ? 23.132  12.693  -8.266  1 38.76  ? 82  LYS A CG    1 1 
ATOM   675  C  CD    . LYS A 1 82  ? 22.876  12.21   -9.689  1 44.22  ? 82  LYS A CD    1 1 
ATOM   676  C  CE    . LYS A 1 82  ? 23.469  10.847  -9.953  1 49.15  ? 82  LYS A CE    1 1 
ATOM   677  N  NZ    . LYS A 1 82  ? 22.873  10.2    -11.158 1 52.02  ? 82  LYS A NZ    1 1 
ATOM   678  N  N     . GLY A 1 83  ? 22.826  17.612  -8.775  1 31.71  ? 83  GLY A N     1 1 
ATOM   679  C  CA    . GLY A 1 83  ? 22.017  18.806  -8.964  1 31.71  ? 83  GLY A CA    1 1 
ATOM   680  C  C     . GLY A 1 83  ? 21.621  19.583  -7.728  1 31.54  ? 83  GLY A C     1 1 
ATOM   681  O  O     . GLY A 1 83  ? 20.869  20.555  -7.853  1 31.83  ? 83  GLY A O     1 1 
ATOM   682  N  N     . SER A 1 84  ? 22.103  19.191  -6.536  1 30.99  ? 84  SER A N     1 1 
ATOM   683  C  CA    . SER A 1 84  ? 21.796  19.964  -5.339  1 31.56  ? 84  SER A CA    1 1 
ATOM   684  C  C     . SER A 1 84  ? 22.755  21.161  -5.32   1 32.67  ? 84  SER A C     1 1 
ATOM   685  O  O     . SER A 1 84  ? 23.814  21.096  -4.689  1 32.84  ? 84  SER A O     1 1 
ATOM   686  C  CB    . SER A 1 84  ? 21.959  19.127  -4.081  1 32.44  ? 84  SER A CB    1 1 
ATOM   687  O  OG    . SER A 1 84  ? 21.443  19.815  -2.955  1 34.7   ? 84  SER A OG    1 1 
ATOM   688  N  N     . PHE A 1 85  ? 22.397  22.25   -6.039  1 33.09  ? 85  PHE A N     1 1 
ATOM   689  C  CA    . PHE A 1 85  ? 23.258  23.428  -6.164  1 33.91  ? 85  PHE A CA    1 1 
ATOM   690  C  C     . PHE A 1 85  ? 23.159  24.434  -5.015  1 34.9   ? 85  PHE A C     1 1 
ATOM   691  O  O     . PHE A 1 85  ? 23.944  25.383  -4.983  1 35.07  ? 85  PHE A O     1 1 
ATOM   692  C  CB    . PHE A 1 85  ? 23.052  24.139  -7.504  1 33.6   ? 85  PHE A CB    1 1 
ATOM   693  C  CG    . PHE A 1 85  ? 21.631  24.548  -7.781  1 34.01  ? 85  PHE A CG    1 1 
ATOM   694  C  CD1   . PHE A 1 85  ? 21.062  25.624  -7.124  1 34.64  ? 85  PHE A CD1   1 1 
ATOM   695  C  CD2   . PHE A 1 85  ? 20.881  23.892  -8.735  1 34.59  ? 85  PHE A CD2   1 1 
ATOM   696  C  CE1   . PHE A 1 85  ? 19.751  25.994  -7.375  1 35.12  ? 85  PHE A CE1   1 1 
ATOM   697  C  CE2   . PHE A 1 85  ? 19.585  24.293  -9.011  1 35.07  ? 85  PHE A CE2   1 1 
ATOM   698  C  CZ    . PHE A 1 85  ? 19.033  25.347  -8.338  1 34.8   ? 85  PHE A CZ    1 1 
ATOM   699  N  N     . LEU A 1 86  ? 22.198  24.26   -4.104  1 35.43  ? 86  LEU A N     1 1 
ATOM   700  C  CA    . LEU A 1 86  ? 22.117  25.147  -2.951  1 36.38  ? 86  LEU A CA    1 1 
ATOM   701  C  C     . LEU A 1 86  ? 23.031  24.601  -1.846  1 37.89  ? 86  LEU A C     1 1 
ATOM   702  O  O     . LEU A 1 86  ? 23.286  23.39   -1.798  1 38.29  ? 86  LEU A O     1 1 
ATOM   703  C  CB    . LEU A 1 86  ? 20.668  25.32   -2.468  1 36.01  ? 86  LEU A CB    1 1 
ATOM   704  C  CG    . LEU A 1 86  ? 19.701  25.993  -3.444  1 36.78  ? 86  LEU A CG    1 1 
ATOM   705  C  CD1   . LEU A 1 86  ? 18.371  26.212  -2.798  1 37.19  ? 86  LEU A CD1   1 1 
ATOM   706  C  CD2   . LEU A 1 86  ? 20.223  27.334  -3.935  1 37.35  ? 86  LEU A CD2   1 1 
ATOM   707  N  N     . TYR A 1 87  ? 23.565  25.485  -0.987  1 38.47  ? 87  TYR A N     1 1 
ATOM   708  C  CA    . TYR A 1 87  ? 24.399  25.038  0.128   1 39.57  ? 87  TYR A CA    1 1 
ATOM   709  C  C     . TYR A 1 87  ? 23.434  24.576  1.223   1 40.02  ? 87  TYR A C     1 1 
ATOM   710  O  O     . TYR A 1 87  ? 23.14   25.32   2.168   1 40.41  ? 87  TYR A O     1 1 
ATOM   711  C  CB    . TYR A 1 87  ? 25.305  26.17   0.634   1 39.94  ? 87  TYR A CB    1 1 
ATOM   712  N  N     . GLU A 1 88  ? 22.871  23.368  1.037   1 39.42  ? 88  GLU A N     1 1 
ATOM   713  C  CA    . GLU A 1 88  ? 21.899  22.816  1.95    1 39.01  ? 88  GLU A CA    1 1 
ATOM   714  C  C     . GLU A 1 88  ? 22.32   21.495  2.52    1 38.6   ? 88  GLU A C     1 1 
ATOM   715  O  O     . GLU A 1 88  ? 22.602  20.538  1.795   1 38.71  ? 88  GLU A O     1 1 
ATOM   716  C  CB    . GLU A 1 88  ? 20.525  22.737  1.297   1 40.94  ? 88  GLU A CB    1 1 
ATOM   717  C  CG    . GLU A 1 88  ? 19.989  24.104  0.899   1 44.65  ? 88  GLU A CG    1 1 
ATOM   718  C  CD    . GLU A 1 88  ? 19.635  25.092  2.002   1 48.18  ? 88  GLU A CD    1 1 
ATOM   719  O  OE1   . GLU A 1 88  ? 19.974  24.847  3.184   1 48.21  ? 88  GLU A OE1   1 1 
ATOM   720  O  OE2   . GLU A 1 88  ? 18.994  26.116  1.674   1 49.32  ? 88  GLU A OE2   1 1 
ATOM   721  N  N     . THR A 1 89  ? 22.364  21.452  3.842   1 37.98  ? 89  THR A N     1 1 
ATOM   722  C  CA    . THR A 1 89  ? 22.767  20.277  4.591   1 37.63  ? 89  THR A CA    1 1 
ATOM   723  C  C     . THR A 1 89  ? 21.579  19.696  5.344   1 37.27  ? 89  THR A C     1 1 
ATOM   724  O  O     . THR A 1 89  ? 21.018  20.353  6.236   1 38.1   ? 89  THR A O     1 1 
ATOM   725  C  CB    . THR A 1 89  ? 23.835  20.699  5.586   1 38.61  ? 89  THR A CB    1 1 
ATOM   726  O  OG1   . THR A 1 89  ? 24.948  21.214  4.865   1 39.54  ? 89  THR A OG1   1 1 
ATOM   727  C  CG2   . THR A 1 89  ? 24.26   19.581  6.487   1 38.87  ? 89  THR A CG2   1 1 
ATOM   728  N  N     . PRO A 1 90  ? 21.152  18.472  4.987   1 35.46  ? 90  PRO A N     1 1 
ATOM   729  C  CA    . PRO A 1 90  ? 20.071  17.836  5.764   1 33.95  ? 90  PRO A CA    1 1 
ATOM   730  C  C     . PRO A 1 90  ? 20.606  17.362  7.128   1 32.27  ? 90  PRO A C     1 1 
ATOM   731  O  O     . PRO A 1 90  ? 21.821  17.408  7.367   1 32.07  ? 90  PRO A O     1 1 
ATOM   732  C  CB    . PRO A 1 90  ? 19.647  16.668  4.879   1 34.73  ? 90  PRO A CB    1 1 
ATOM   733  C  CG    . PRO A 1 90  ? 20.843  16.347  4.09    1 35.53  ? 90  PRO A CG    1 1 
ATOM   734  C  CD    . PRO A 1 90  ? 21.708  17.564  3.964   1 34.44  ? 90  PRO A CD    1 1 
ATOM   735  N  N     . ASP A 1 91  ? 19.719  16.922  8.022   1 30.87  ? 91  ASP A N     1 1 
ATOM   736  C  CA    . ASP A 1 91  ? 20.17   16.474  9.334   1 30.02  ? 91  ASP A CA    1 1 
ATOM   737  C  C     . ASP A 1 91  ? 20.897  15.13   9.247   1 28.46  ? 91  ASP A C     1 1 
ATOM   738  O  O     . ASP A 1 91  ? 21.892  14.944  9.936   1 28.45  ? 91  ASP A O     1 1 
ATOM   739  C  CB    . ASP A 1 91  ? 19.028  16.488  10.36   1 31.9   ? 91  ASP A CB    1 1 
ATOM   740  C  CG    . ASP A 1 91  ? 18.577  17.894  10.73   1 36.88  ? 91  ASP A CG    1 1 
ATOM   741  O  OD1   . ASP A 1 91  ? 19.39   18.841  10.59   1 37.8   ? 91  ASP A OD1   1 1 
ATOM   742  O  OD2   . ASP A 1 91  ? 17.426  18.047  11.189  1 39.26  ? 91  ASP A OD2   1 1 
ATOM   743  N  N     . VAL A 1 92  ? 20.439  14.222  8.36    1 26.94  ? 92  VAL A N     1 1 
ATOM   744  C  CA    . VAL A 1 92  ? 21.015  12.89   8.174   1 25.91  ? 92  VAL A CA    1 1 
ATOM   745  C  C     . VAL A 1 92  ? 21.02   12.488  6.687   1 24.04  ? 92  VAL A C     1 1 
ATOM   746  O  O     . VAL A 1 92  ? 20.106  12.831  5.951   1 23.61  ? 92  VAL A O     1 1 
ATOM   747  C  CB    . VAL A 1 92  ? 20.211  11.837  8.996   1 27.12  ? 92  VAL A CB    1 1 
ATOM   748  C  CG1   . VAL A 1 92  ? 20.622  10.41   8.641   1 27.85  ? 92  VAL A CG1   1 1 
ATOM   749  C  CG2   . VAL A 1 92  ? 20.317  12.07   10.502  1 27.79  ? 92  VAL A CG2   1 1 
ATOM   750  N  N     . ILE A 1 93  ? 22.04   11.731  6.268   1 22.83  ? 93  ILE A N     1 1 
ATOM   751  C  CA    . ILE A 1 93  ? 22.16   11.122  4.944   1 22.2   ? 93  ILE A CA    1 1 
ATOM   752  C  C     . ILE A 1 93  ? 22.445  9.648   5.209   1 21.65  ? 93  ILE A C     1 1 
ATOM   753  O  O     . ILE A 1 93  ? 23.432  9.34    5.877   1 21.65  ? 93  ILE A O     1 1 
ATOM   754  C  CB    . ILE A 1 93  ? 23.312  11.711  4.097   1 22.37  ? 93  ILE A CB    1 1 
ATOM   755  C  CG1   . ILE A 1 93  ? 23.1    13.197  3.787   1 23.42  ? 93  ILE A CG1   1 1 
ATOM   756  C  CG2   . ILE A 1 93  ? 23.526  10.881  2.821   1 22.57  ? 93  ILE A CG2   1 1 
ATOM   757  C  CD1   . ILE A 1 93  ? 22.003  13.469  2.826   1 25.03  ? 93  ILE A CD1   1 1 
ATOM   758  N  N     . ILE A 1 94  ? 21.594  8.744   4.724   1 21.08  ? 94  ILE A N     1 1 
ATOM   759  C  CA    . ILE A 1 94  ? 21.824  7.316   4.916   1 20.99  ? 94  ILE A CA    1 1 
ATOM   760  C  C     . ILE A 1 94  ? 22.398  6.793   3.634   1 21.77  ? 94  ILE A C     1 1 
ATOM   761  O  O     . ILE A 1 94  ? 21.789  6.987   2.593   1 21.87  ? 94  ILE A O     1 1 
ATOM   762  C  CB    . ILE A 1 94  ? 20.53   6.558   5.262   1 20.82  ? 94  ILE A CB    1 1 
ATOM   763  C  CG1   . ILE A 1 94  ? 19.822  7.163   6.485   1 21.41  ? 94  ILE A CG1   1 1 
ATOM   764  C  CG2   . ILE A 1 94  ? 20.83   5.083   5.459   1 20.96  ? 94  ILE A CG2   1 1 
ATOM   765  C  CD1   . ILE A 1 94  ? 18.463  6.581   6.754   1 22.21  ? 94  ILE A CD1   1 1 
ATOM   766  N  N     . THR A 1 95  ? 23.583  6.177   3.679   1 22.27  ? 95  THR A N     1 1 
ATOM   767  C  CA    . THR A 1 95  ? 24.19   5.622   2.48    1 23.38  ? 95  THR A CA    1 1 
ATOM   768  C  C     . THR A 1 95  ? 24.306  4.085   2.562   1 25.5   ? 95  THR A C     1 1 
ATOM   769  O  O     . THR A 1 95  ? 24.2    3.483   3.632   1 25.74  ? 95  THR A O     1 1 
ATOM   770  C  CB    . THR A 1 95  ? 25.531  6.284   2.178   1 23.88  ? 95  THR A CB    1 1 
ATOM   771  O  OG1   . THR A 1 95  ? 26.487  5.862   3.143   1 24.66  ? 95  THR A OG1   1 1 
ATOM   772  C  CG2   . THR A 1 95  ? 25.452  7.775   2.152   1 24.22  ? 95  THR A CG2   1 1 
ATOM   773  N  N     . SER A 1 96  ? 24.493  3.454   1.412   1 26.47  ? 96  SER A N     1 1 
ATOM   774  C  CA    . SER A 1 96  ? 24.697  2.036   1.315   1 27.59  ? 96  SER A CA    1 1 
ATOM   775  C  C     . SER A 1 96  ? 26.113  1.856   0.783   1 29.01  ? 96  SER A C     1 1 
ATOM   776  O  O     . SER A 1 96  ? 26.499  2.526   -0.176  1 29.03  ? 96  SER A O     1 1 
ATOM   777  C  CB    . SER A 1 96  ? 23.705  1.434   0.331   1 28.86  ? 96  SER A CB    1 1 
ATOM   778  O  OG    . SER A 1 96  ? 23.908  0.036   0.218   1 31.49  ? 96  SER A OG    1 1 
ATOM   779  N  N     . LEU A 1 97  ? 26.897  0.977   1.417   1 30.02  ? 97  LEU A N     1 1 
ATOM   780  C  CA    . LEU A 1 97  ? 28.239  0.687   0.95    1 31.53  ? 97  LEU A CA    1 1 
ATOM   781  C  C     . LEU A 1 97  ? 28.138  -0.443  -0.042  1 33.88  ? 97  LEU A C     1 1 
ATOM   782  O  O     . LEU A 1 97  ? 27.677  -1.532  0.298   1 34.36  ? 97  LEU A O     1 1 
ATOM   783  C  CB    . LEU A 1 97  ? 29.166  0.265   2.096   1 31.41  ? 97  LEU A CB    1 1 
ATOM   784  C  CG    . LEU A 1 97  ? 29.732  1.365   2.976   1 32.51  ? 97  LEU A CG    1 1 
ATOM   785  C  CD1   . LEU A 1 97  ? 30.774  0.816   3.897   1 32.86  ? 97  LEU A CD1   1 1 
ATOM   786  C  CD2   . LEU A 1 97  ? 30.385  2.435   2.163   1 33.21  ? 97  LEU A CD2   1 1 
ATOM   787  N  N     . ASN A 1 98  ? 28.533  -0.179  -1.278  1 35.06  ? 98  ASN A N     1 1 
ATOM   788  C  CA    . ASN A 1 98  ? 28.488  -1.176  -2.34   1 36.46  ? 98  ASN A CA    1 1 
ATOM   789  C  C     . ASN A 1 98  ? 29.635  -0.936  -3.305  1 36.89  ? 98  ASN A C     1 1 
ATOM   790  O  O     . ASN A 1 98  ? 29.857  0.196   -3.734  1 36.94  ? 98  ASN A O     1 1 
ATOM   791  C  CB    . ASN A 1 98  ? 27.118  -1.175  -3.076  1 38.34  ? 98  ASN A CB    1 1 
ATOM   792  C  CG    . ASN A 1 98  ? 26.465  0.186   -3.289  1 42.58  ? 98  ASN A CG    1 1 
ATOM   793  O  OD1   . ASN A 1 98  ? 25.339  0.431   -2.846  1 44.25  ? 98  ASN A OD1   1 1 
ATOM   794  N  ND2   . ASN A 1 98  ? 27.135  1.107   -3.981  1 43.42  ? 98  ASN A ND2   1 1 
ATOM   795  N  N     . ASN A 1 99  ? 30.371  -1.994  -3.637  1 37.13  ? 99  ASN A N     1 1 
ATOM   796  C  CA    . ASN A 1 99  ? 31.495  -1.938  -4.571  1 37.88  ? 99  ASN A CA    1 1 
ATOM   797  C  C     . ASN A 1 99  ? 32.584  -0.942  -4.133  1 38.18  ? 99  ASN A C     1 1 
ATOM   798  O  O     . ASN A 1 99  ? 33.159  -0.246  -4.97   1 38.5   ? 99  ASN A O     1 1 
ATOM   799  C  CB    . ASN A 1 99  ? 31.038  -1.664  -6.03   1 39.41  ? 99  ASN A CB    1 1 
ATOM   800  C  CG    . ASN A 1 99  ? 29.618  -2.077  -6.388  1 42.75  ? 99  ASN A CG    1 1 
ATOM   801  O  OD1   . ASN A 1 99  ? 28.784  -1.242  -6.779  1 43.87  ? 99  ASN A OD1   1 1 
ATOM   802  N  ND2   . ASN A 1 99  ? 29.31   -3.366  -6.25   1 43.26  ? 99  ASN A ND2   1 1 
ATOM   803  N  N     . GLY A 1 100 ? 32.834  -0.869  -2.827  1 37.89  ? 100 GLY A N     1 1 
ATOM   804  C  CA    . GLY A 1 100 ? 33.864  -0.009  -2.248  1 38     ? 100 GLY A CA    1 1 
ATOM   805  C  C     . GLY A 1 100 ? 33.599  1.483   -2.277  1 37.94  ? 100 GLY A C     1 1 
ATOM   806  O  O     . GLY A 1 100 ? 34.533  2.273   -2.125  1 38.38  ? 100 GLY A O     1 1 
ATOM   807  N  N     . LYS A 1 101 ? 32.33   1.883   -2.462  1 37.12  ? 101 LYS A N     1 1 
ATOM   808  C  CA    . LYS A 1 101 ? 31.922  3.287   -2.515  1 36.9   ? 101 LYS A CA    1 1 
ATOM   809  C  C     . LYS A 1 101 ? 30.535  3.497   -1.849  1 36.01  ? 101 LYS A C     1 1 
ATOM   810  O  O     . LYS A 1 101 ? 29.797  2.532   -1.635  1 36.21  ? 101 LYS A O     1 1 
ATOM   811  C  CB    . LYS A 1 101 ? 31.897  3.765   -3.982  1 39.32  ? 101 LYS A CB    1 1 
ATOM   812  C  CG    . LYS A 1 101 ? 30.72   3.201   -4.78   1 44.35  ? 101 LYS A CG    1 1 
ATOM   813  C  CD    . LYS A 1 101 ? 30.738  3.61    -6.229  1 49.38  ? 101 LYS A CD    1 1 
ATOM   814  C  CE    . LYS A 1 101 ? 29.423  3.323   -6.899  1 53.53  ? 101 LYS A CE    1 1 
ATOM   815  N  NZ    . LYS A 1 101 ? 28.335  4.167   -6.336  1 56.42  ? 101 LYS A NZ    1 1 
ATOM   816  N  N     . GLU A 1 102 ? 30.169  4.753   -1.55   1 34.84  ? 102 GLU A N     1 1 
ATOM   817  C  CA    . GLU A 1 102 ? 28.873  5.037   -0.935  1 34.34  ? 102 GLU A CA    1 1 
ATOM   818  C  C     . GLU A 1 102 ? 27.838  5.484   -1.953  1 33.46  ? 102 GLU A C     1 1 
ATOM   819  O  O     . GLU A 1 102 ? 28.159  6.192   -2.905  1 33.48  ? 102 GLU A O     1 1 
ATOM   820  C  CB    . GLU A 1 102 ? 28.991  6.098   0.167   1 36.28  ? 102 GLU A CB    1 1 
ATOM   821  C  CG    . GLU A 1 102 ? 30.064  5.808   1.192   1 40.44  ? 102 GLU A CG    1 1 
ATOM   822  C  CD    . GLU A 1 102 ? 29.996  6.699   2.413   1 45.94  ? 102 GLU A CD    1 1 
ATOM   823  O  OE1   . GLU A 1 102 ? 28.881  6.887   2.949   1 45.89  ? 102 GLU A OE1   1 1 
ATOM   824  O  OE2   . GLU A 1 102 ? 31.061  7.199   2.844   1 49.02  ? 102 GLU A OE2   1 1 
ATOM   825  N  N     . GLU A 1 103 ? 26.594  5.078   -1.745  1 32.56  ? 103 GLU A N     1 1 
ATOM   826  C  CA    . GLU A 1 103 ? 25.508  5.508   -2.596  1 32.42  ? 103 GLU A CA    1 1 
ATOM   827  C  C     . GLU A 1 103 ? 24.387  6       -1.678  1 31.45  ? 103 GLU A C     1 1 
ATOM   828  O  O     . GLU A 1 103 ? 24.038  5.308   -0.734  1 31.8   ? 103 GLU A O     1 1 
ATOM   829  C  CB    . GLU A 1 103 ? 25.066  4.387   -3.547  1 35.59  ? 103 GLU A CB    1 1 
ATOM   830  C  CG    . GLU A 1 103 ? 23.856  4.766   -4.394  1 43.1   ? 103 GLU A CG    1 1 
ATOM   831  C  CD    . GLU A 1 103 ? 24.019  5.886   -5.41   1 51.25  ? 103 GLU A CD    1 1 
ATOM   832  O  OE1   . GLU A 1 103 ? 24.107  5.578   -6.621  1 53.09  ? 103 GLU A OE1   1 1 
ATOM   833  O  OE2   . GLU A 1 103 ? 24.039  7.072   -5.003  1 53.67  ? 103 GLU A OE2   1 1 
ATOM   834  N  N     . ILE A 1 104 ? 23.882  7.215   -1.895  1 30.26  ? 104 ILE A N     1 1 
ATOM   835  C  CA    . ILE A 1 104 ? 22.825  7.765   -1.046  1 29.88  ? 104 ILE A CA    1 1 
ATOM   836  C  C     . ILE A 1 104 ? 21.487  7.039   -1.198  1 29.28  ? 104 ILE A C     1 1 
ATOM   837  O  O     . ILE A 1 104 ? 20.995  6.866   -2.307  1 29.28  ? 104 ILE A O     1 1 
ATOM   838  C  CB    . ILE A 1 104 ? 22.685  9.283   -1.262  1 30.21  ? 104 ILE A CB    1 1 
ATOM   839  C  CG1   . ILE A 1 104 ? 23.971  9.991   -0.794  1 31.15  ? 104 ILE A CG1   1 1 
ATOM   840  C  CG2   . ILE A 1 104 ? 21.436  9.829   -0.563  1 30.52  ? 104 ILE A CG2   1 1 
ATOM   841  C  CD1   . ILE A 1 104 ? 23.977  11.468  -0.919  1 32.45  ? 104 ILE A CD1   1 1 
ATOM   842  N  N     . LEU A 1 105 ? 20.901  6.629   -0.071  1 28.72  ? 105 LEU A N     1 1 
ATOM   843  C  CA    . LEU A 1 105 ? 19.601  5.97    -0.034  1 28.73  ? 105 LEU A CA    1 1 
ATOM   844  C  C     . LEU A 1 105 ? 18.503  7.004   0.198   1 28.37  ? 105 LEU A C     1 1 
ATOM   845  O  O     . LEU A 1 105 ? 17.464  6.953   -0.457  1 28.03  ? 105 LEU A O     1 1 
ATOM   846  C  CB    . LEU A 1 105 ? 19.54   4.913   1.084   1 28.96  ? 105 LEU A CB    1 1 
ATOM   847  C  CG    . LEU A 1 105 ? 20.404  3.693   0.931   1 30.17  ? 105 LEU A CG    1 1 
ATOM   848  C  CD1   . LEU A 1 105 ? 20.207  2.784   2.096   1 30.55  ? 105 LEU A CD1   1 1 
ATOM   849  C  CD2   . LEU A 1 105 ? 20.071  2.945   -0.334  1 30.87  ? 105 LEU A CD2   1 1 
ATOM   850  N  N     . MET A 1 106 ? 18.734  7.929   1.139   1 28.36  ? 106 MET A N     1 1 
ATOM   851  C  CA    . MET A 1 106 ? 17.791  8.992   1.459   1 28.93  ? 106 MET A CA    1 1 
ATOM   852  C  C     . MET A 1 106 ? 18.438  10.092  2.316   1 29.38  ? 106 MET A C     1 1 
ATOM   853  O  O     . MET A 1 106 ? 19.484  9.895   2.936   1 29.42  ? 106 MET A O     1 1 
ATOM   854  C  CB    . MET A 1 106 ? 16.554  8.423   2.175   1 29.33  ? 106 MET A CB    1 1 
ATOM   855  C  CG    . MET A 1 106 ? 16.857  7.942   3.565   1 31.21  ? 106 MET A CG    1 1 
ATOM   856  S  SD    . MET A 1 106 ? 15.506  7.01    4.266   1 33.34  ? 106 MET A SD    1 1 
ATOM   857  C  CE    . MET A 1 106 ? 15.63   5.583   3.321   1 31.6   ? 106 MET A CE    1 1 
ATOM   858  N  N     . ALA A 1 107 ? 17.785  11.241  2.361   1 29.54  ? 107 ALA A N     1 1 
ATOM   859  C  CA    . ALA A 1 107 ? 18.166  12.363  3.191   1 30.27  ? 107 ALA A CA    1 1 
ATOM   860  C  C     . ALA A 1 107 ? 17.005  12.578  4.169   1 30.96  ? 107 ALA A C     1 1 
ATOM   861  O  O     . ALA A 1 107 ? 15.842  12.485  3.777   1 31.15  ? 107 ALA A O     1 1 
ATOM   862  C  CB    . ALA A 1 107 ? 18.359  13.598  2.332   1 30.42  ? 107 ALA A CB    1 1 
ATOM   863  N  N     . ILE A 1 108 ? 17.308  12.81   5.445   1 31.21  ? 108 ILE A N     1 1 
ATOM   864  C  CA    . ILE A 1 108 ? 16.282  13.026  6.456   1 31.95  ? 108 ILE A CA    1 1 
ATOM   865  C  C     . ILE A 1 108 ? 16.545  14.324  7.218   1 33.57  ? 108 ILE A C     1 1 
ATOM   866  O  O     . ILE A 1 108 ? 17.684  14.617  7.57    1 33.55  ? 108 ILE A O     1 1 
ATOM   867  C  CB    . ILE A 1 108 ? 16.196  11.816  7.408   1 31.8   ? 108 ILE A CB    1 1 
ATOM   868  C  CG1   . ILE A 1 108 ? 15.856  10.537  6.647   1 31.95  ? 108 ILE A CG1   1 1 
ATOM   869  C  CG2   . ILE A 1 108 ? 15.188  12.069  8.518   1 32.45  ? 108 ILE A CG2   1 1 
ATOM   870  C  CD1   . ILE A 1 108 ? 16.033  9.322   7.437   1 32.69  ? 108 ILE A CD1   1 1 
ATOM   871  N  N     . GLU A 1 109 ? 15.5    15.121  7.432   1 34.84  ? 109 GLU A N     1 1 
ATOM   872  C  CA    . GLU A 1 109 ? 15.606  16.358  8.195   1 36.68  ? 109 GLU A CA    1 1 
ATOM   873  C  C     . GLU A 1 109 ? 14.602  16.265  9.324   1 38.46  ? 109 GLU A C     1 1 
ATOM   874  O  O     . GLU A 1 109 ? 13.457  15.888  9.092   1 38.7   ? 109 GLU A O     1 1 
ATOM   875  C  CB    . GLU A 1 109 ? 15.326  17.593  7.318   1 38.95  ? 109 GLU A CB    1 1 
ATOM   876  C  CG    . GLU A 1 109 ? 15.265  18.91   8.08    1 44.47  ? 109 GLU A CG    1 1 
ATOM   877  C  CD    . GLU A 1 109 ? 16.558  19.694  8.238   1 51.98  ? 109 GLU A CD    1 1 
ATOM   878  O  OE1   . GLU A 1 109 ? 17.471  19.52   7.398   1 53.34  ? 109 GLU A OE1   1 1 
ATOM   879  O  OE2   . GLU A 1 109 ? 16.663  20.476  9.212   1 54.48  ? 109 GLU A OE2   1 1 
ATOM   880  N  N     . PHE A 1 110 ? 15.032  16.549  10.549  1 39.69  ? 110 PHE A N     1 1 
ATOM   881  C  CA    . PHE A 1 110 ? 14.146  16.506  11.7    1 41.43  ? 110 PHE A CA    1 1 
ATOM   882  C  C     . PHE A 1 110 ? 13.819  17.922  12.124  1 43.2   ? 110 PHE A C     1 1 
ATOM   883  O  O     . PHE A 1 110 ? 14.712  18.759  12.231  1 43.43  ? 110 PHE A O     1 1 
ATOM   884  C  CB    . PHE A 1 110 ? 14.779  15.741  12.863  1 41.35  ? 110 PHE A CB    1 1 
ATOM   885  C  CG    . PHE A 1 110 ? 15.044  14.28   12.587  1 42.04  ? 110 PHE A CG    1 1 
ATOM   886  C  CD1   . PHE A 1 110 ? 14.01   13.363  12.576  1 42.72  ? 110 PHE A CD1   1 1 
ATOM   887  C  CD2   . PHE A 1 110 ? 16.334  13.816  12.399  1 42.84  ? 110 PHE A CD2   1 1 
ATOM   888  C  CE1   . PHE A 1 110 ? 14.26   12.018  12.36   1 43.41  ? 110 PHE A CE1   1 1 
ATOM   889  C  CE2   . PHE A 1 110 ? 16.583  12.469  12.196  1 43.52  ? 110 PHE A CE2   1 1 
ATOM   890  C  CZ    . PHE A 1 110 ? 15.543  11.58   12.168  1 43.3   ? 110 PHE A CZ    1 1 
ATOM   891  N  N     . CYS A 1 111 ? 12.536  18.188  12.357  1 44.26  ? 111 CYS A N     1 1 
ATOM   892  C  CA    . CYS A 1 111 ? 12.056  19.491  12.779  1 45.76  ? 111 CYS A CA    1 1 
ATOM   893  C  C     . CYS A 1 111 ? 11.276  19.326  14.073  1 47.37  ? 111 CYS A C     1 1 
ATOM   894  O  O     . CYS A 1 111 ? 10.376  18.492  14.149  1 47.6   ? 111 CYS A O     1 1 
ATOM   895  C  CB    . CYS A 1 111 ? 11.202  20.124  11.691  1 46.24  ? 111 CYS A CB    1 1 
ATOM   896  S  SG    . CYS A 1 111 ? 10.514  21.729  12.145  1 49.66  ? 111 CYS A SG    1 1 
ATOM   897  N  N     . SER A 1 112 ? 11.64   20.104  15.097  1 48.26  ? 112 SER A N     1 1 
ATOM   898  C  CA    . SER A 1 112 ? 11.041  20.02   16.424  1 49.45  ? 112 SER A CA    1 1 
ATOM   899  C  C     . SER A 1 112 ? 9.607   20.503  16.498  1 50.45  ? 112 SER A C     1 1 
ATOM   900  O  O     . SER A 1 112 ? 8.886   20.109  17.413  1 51.04  ? 112 SER A O     1 1 
ATOM   901  C  CB    . SER A 1 112 ? 11.889  20.785  17.435  1 50.82  ? 112 SER A CB    1 1 
ATOM   902  O  OG    . SER A 1 112 ? 12.054  22.139  17.046  1 53.08  ? 112 SER A OG    1 1 
ATOM   903  N  N     . ALA A 1 113 ? 9.189   21.361  15.563  1 50.56  ? 113 ALA A N     1 1 
ATOM   904  C  CA    . ALA A 1 113 ? 7.834   21.904  15.592  1 51.15  ? 113 ALA A CA    1 1 
ATOM   905  C  C     . ALA A 1 113 ? 7.313   22.211  14.203  1 51.33  ? 113 ALA A C     1 1 
ATOM   906  O  O     . ALA A 1 113 ? 8.108   22.53   13.313  1 51.65  ? 113 ALA A O     1 1 
ATOM   907  C  CB    . ALA A 1 113 ? 7.821   23.178  16.426  1 51.43  ? 113 ALA A CB    1 1 
ATOM   908  N  N     . LEU A 1 114 ? 5.976   22.173  14.02   1 50.8   ? 114 LEU A N     1 1 
ATOM   909  C  CA    . LEU A 1 114 ? 5.403   22.562  12.736  1 50.87  ? 114 LEU A CA    1 1 
ATOM   910  C  C     . LEU A 1 114 ? 5.478   24.087  12.699  1 50.66  ? 114 LEU A C     1 1 
ATOM   911  O  O     . LEU A 1 114 ? 4.648   24.76   13.311  1 51.13  ? 114 LEU A O     1 1 
ATOM   912  C  CB    . LEU A 1 114 ? 3.953   22.084  12.583  1 51.2   ? 114 LEU A CB    1 1 
ATOM   913  C  CG    . LEU A 1 114 ? 3.336   22.267  11.187  1 52.84  ? 114 LEU A CG    1 1 
ATOM   914  C  CD1   . LEU A 1 114 ? 4.153   21.541  10.11   1 53.49  ? 114 LEU A CD1   1 1 
ATOM   915  C  CD2   . LEU A 1 114 ? 1.898   21.79   11.157  1 53.38  ? 114 LEU A CD2   1 1 
ATOM   916  N  N     . GLN A 1 115 ? 6.532   24.625  12.072  1 49.72  ? 115 GLN A N     1 1 
ATOM   917  C  CA    . GLN A 1 115 ? 6.752   26.058  12.024  1 49.41  ? 115 GLN A CA    1 1 
ATOM   918  C  C     . GLN A 1 115 ? 5.694   26.784  11.187  1 48.69  ? 115 GLN A C     1 1 
ATOM   919  O  O     . GLN A 1 115 ? 5.053   26.184  10.323  1 48.65  ? 115 GLN A O     1 1 
ATOM   920  C  CB    . GLN A 1 115 ? 8.18    26.355  11.573  1 51.23  ? 115 GLN A CB    1 1 
ATOM   921  C  CG    . GLN A 1 115 ? 9.204   25.721  12.515  1 55.31  ? 115 GLN A CG    1 1 
ATOM   922  C  CD    . GLN A 1 115 ? 10.566  25.506  11.891  1 60.23  ? 115 GLN A CD    1 1 
ATOM   923  O  OE1   . GLN A 1 115 ? 10.729  25.473  10.663  1 62.14  ? 115 GLN A OE1   1 1 
ATOM   924  N  NE2   . GLN A 1 115 ? 11.58   25.332  12.727  1 60.58  ? 115 GLN A NE2   1 1 
ATOM   925  N  N     . ALA A 1 116 ? 5.473   28.066  11.491  1 47.74  ? 116 ALA A N     1 1 
ATOM   926  C  CA    . ALA A 1 116 ? 4.453   28.871  10.827  1 47.07  ? 116 ALA A CA    1 1 
ATOM   927  C  C     . ALA A 1 116 ? 5.007   30.234  10.329  1 46.46  ? 116 ALA A C     1 1 
ATOM   928  O  O     . ALA A 1 116 ? 6.106   30.632  10.724  1 46.83  ? 116 ALA A O     1 1 
ATOM   929  C  CB    . ALA A 1 116 ? 3.296   29.079  11.786  1 47.1   ? 116 ALA A CB    1 1 
ATOM   930  N  N     . GLY A 1 117 ? 4.26    30.926  9.46    1 45.34  ? 117 GLY A N     1 1 
ATOM   931  C  CA    . GLY A 1 117 ? 4.698   32.201  8.901   1 44.43  ? 117 GLY A CA    1 1 
ATOM   932  C  C     . GLY A 1 117 ? 5.818   31.964  7.917   1 43.16  ? 117 GLY A C     1 1 
ATOM   933  O  O     . GLY A 1 117 ? 5.833   30.922  7.25    1 43.47  ? 117 GLY A O     1 1 
ATOM   934  N  N     . ASN A 1 118 ? 6.781   32.893  7.835   1 41.64  ? 118 ASN A N     1 1 
ATOM   935  C  CA    . ASN A 1 118 ? 7.916   32.671  6.935   1 40.79  ? 118 ASN A CA    1 1 
ATOM   936  C  C     . ASN A 1 118 ? 8.911   31.647  7.49    1 40     ? 118 ASN A C     1 1 
ATOM   937  O  O     . ASN A 1 118 ? 9.728   31.144  6.728   1 39.91  ? 118 ASN A O     1 1 
ATOM   938  C  CB    . ASN A 1 118 ? 8.6     33.954  6.475   1 41.29  ? 118 ASN A CB    1 1 
ATOM   939  C  CG    . ASN A 1 118 ? 9.149   34.845  7.541   1 42.84  ? 118 ASN A CG    1 1 
ATOM   940  O  OD1   . ASN A 1 118 ? 9.39    34.438  8.681   1 43.55  ? 118 ASN A OD1   1 1 
ATOM   941  N  ND2   . ASN A 1 118 ? 9.383   36.087  7.166   1 42.8   ? 118 ASN A ND2   1 1 
ATOM   942  N  N     . GLN A 1 119 ? 8.811   31.296  8.785   1 39.43  ? 119 GLN A N     1 1 
ATOM   943  C  CA    . GLN A 1 119 ? 9.649   30.261  9.368   1 39.68  ? 119 GLN A CA    1 1 
ATOM   944  C  C     . GLN A 1 119 ? 9.334   28.886  8.742   1 38.55  ? 119 GLN A C     1 1 
ATOM   945  O  O     . GLN A 1 119 ? 10.221  28.036  8.688   1 38.57  ? 119 GLN A O     1 1 
ATOM   946  C  CB    . GLN A 1 119 ? 9.467   30.212  10.887  1 42.78  ? 119 GLN A CB    1 1 
ATOM   947  C  CG    . GLN A 1 119 ? 10.588  29.471  11.603  1 48.93  ? 119 GLN A CG    1 1 
ATOM   948  C  CD    . GLN A 1 119 ? 10.244  29.176  13.039  1 56.56  ? 119 GLN A CD    1 1 
ATOM   949  O  OE1   . GLN A 1 119 ? 9.064   28.999  13.401  1 59.5   ? 119 GLN A OE1   1 1 
ATOM   950  N  NE2   . GLN A 1 119 ? 11.272  29.112  13.89   1 57.32  ? 119 GLN A NE2   1 1 
ATOM   951  N  N     . ALA A 1 120 ? 8.093   28.688  8.233   1 37.55  ? 120 ALA A N     1 1 
ATOM   952  C  CA    . ALA A 1 120 ? 7.635   27.461  7.578   1 37.01  ? 120 ALA A CA    1 1 
ATOM   953  C  C     . ALA A 1 120 ? 8.43    27.15   6.317   1 36.25  ? 120 ALA A C     1 1 
ATOM   954  O  O     . ALA A 1 120 ? 8.712   25.979  6.045   1 36.72  ? 120 ALA A O     1 1 
ATOM   955  C  CB    . ALA A 1 120 ? 6.159   27.568  7.232   1 37.14  ? 120 ALA A CB    1 1 
ATOM   956  N  N     . TRP A 1 121 ? 8.789   28.186  5.546   1 34.85  ? 121 TRP A N     1 1 
ATOM   957  C  CA    . TRP A 1 121 ? 9.559   27.972  4.328   1 33.99  ? 121 TRP A CA    1 1 
ATOM   958  C  C     . TRP A 1 121 ? 11.034  28.339  4.437   1 33.85  ? 121 TRP A C     1 1 
ATOM   959  O  O     . TRP A 1 121 ? 11.74   28.232  3.442   1 33.87  ? 121 TRP A O     1 1 
ATOM   960  C  CB    . TRP A 1 121 ? 8.924   28.677  3.133   1 33.27  ? 121 TRP A CB    1 1 
ATOM   961  C  CG    . TRP A 1 121 ? 8.846   30.171  3.246   1 33.03  ? 121 TRP A CG    1 1 
ATOM   962  C  CD1   . TRP A 1 121 ? 9.857   31.069  3.052   1 33.55  ? 121 TRP A CD1   1 1 
ATOM   963  C  CD2   . TRP A 1 121 ? 7.654   30.941  3.424   1 32.68  ? 121 TRP A CD2   1 1 
ATOM   964  N  NE1   . TRP A 1 121 ? 9.374   32.349  3.156   1 33.66  ? 121 TRP A NE1   1 1 
ATOM   965  C  CE2   . TRP A 1 121 ? 8.02    32.3    3.368   1 33.39  ? 121 TRP A CE2   1 1 
ATOM   966  C  CE3   . TRP A 1 121 ? 6.317   30.614  3.654   1 32.8   ? 121 TRP A CE3   1 1 
ATOM   967  C  CZ2   . TRP A 1 121 ? 7.084   33.326  3.496   1 33.88  ? 121 TRP A CZ2   1 1 
ATOM   968  C  CZ3   . TRP A 1 121 ? 5.4     31.628  3.801   1 33.57  ? 121 TRP A CZ3   1 1 
ATOM   969  C  CH2   . TRP A 1 121 ? 5.787   32.967  3.741   1 33.85  ? 121 TRP A CH2   1 1 
ATOM   970  N  N     . GLN A 1 122 ? 11.512  28.739  5.624   1 33.47  ? 122 GLN A N     1 1 
ATOM   971  C  CA    . GLN A 1 122 ? 12.9    29.137  5.874   1 33.44  ? 122 GLN A CA    1 1 
ATOM   972  C  C     . GLN A 1 122 ? 13.89   28.079  5.39    1 33.36  ? 122 GLN A C     1 1 
ATOM   973  O  O     . GLN A 1 122 ? 14.905  28.417  4.771   1 33.19  ? 122 GLN A O     1 1 
ATOM   974  C  CB    . GLN A 1 122 ? 13.083  29.409  7.374   1 34.76  ? 122 GLN A CB    1 1 
ATOM   975  C  CG    . GLN A 1 122 ? 14.462  29.888  7.773   1 37.92  ? 122 GLN A CG    1 1 
ATOM   976  C  CD    . GLN A 1 122 ? 14.45   30.474  9.166   1 42.03  ? 122 GLN A CD    1 1 
ATOM   977  O  OE1   . GLN A 1 122 ? 14.603  31.687  9.347   1 43.52  ? 122 GLN A OE1   1 1 
ATOM   978  N  NE2   . GLN A 1 122 ? 14.258  29.635  10.182  1 42.21  ? 122 GLN A NE2   1 1 
ATOM   979  N  N     . ARG A 1 123 ? 13.54   26.788  5.618   1 33.12  ? 123 ARG A N     1 1 
ATOM   980  C  CA    . ARG A 1 123 ? 14.328  25.606  5.247   1 32.97  ? 123 ARG A CA    1 1 
ATOM   981  C  C     . ARG A 1 123 ? 13.789  24.87   4.012   1 32.38  ? 123 ARG A C     1 1 
ATOM   982  O  O     . ARG A 1 123 ? 14.066  23.686  3.841   1 32.61  ? 123 ARG A O     1 1 
ATOM   983  C  CB    . ARG A 1 123 ? 14.4    24.627  6.426   1 34.29  ? 123 ARG A CB    1 1 
ATOM   984  N  N     . SER A 1 124 ? 13.011  25.552  3.167   1 31.54  ? 124 SER A N     1 1 
ATOM   985  C  CA    . SER A 1 124 ? 12.493  24.94   1.939   1 30.88  ? 124 SER A CA    1 1 
ATOM   986  C  C     . SER A 1 124 ? 13.579  24.75   0.868   1 30.12  ? 124 SER A C     1 1 
ATOM   987  O  O     . SER A 1 124 ? 13.404  23.941  -0.04   1 29.91  ? 124 SER A O     1 1 
ATOM   988  C  CB    . SER A 1 124 ? 11.305  25.722  1.386   1 31.44  ? 124 SER A CB    1 1 
ATOM   989  O  OG    . SER A 1 124 ? 10.123  25.407  2.102   1 32.54  ? 124 SER A OG    1 1 
ATOM   990  N  N     . GLY A 1 125 ? 14.69   25.475  0.993   1 29.6   ? 125 GLY A N     1 1 
ATOM   991  C  CA    . GLY A 1 125 ? 15.819  25.336  0.09    1 29.83  ? 125 GLY A CA    1 1 
ATOM   992  C  C     . GLY A 1 125 ? 16.408  23.943  0.142   1 29.76  ? 125 GLY A C     1 1 
ATOM   993  O  O     . GLY A 1 125 ? 16.783  23.396  -0.889  1 29.53  ? 125 GLY A O     1 1 
ATOM   994  N  N     . ARG A 1 126 ? 16.432  23.341  1.347   1 29.86  ? 126 ARG A N     1 1 
ATOM   995  C  CA    . ARG A 1 126 ? 16.921  21.987  1.581   1 30.34  ? 126 ARG A CA    1 1 
ATOM   996  C  C     . ARG A 1 126 ? 16.069  21.011  0.783   1 29.57  ? 126 ARG A C     1 1 
ATOM   997  O  O     . ARG A 1 126 ? 16.614  20.226  0.014   1 29.94  ? 126 ARG A O     1 1 
ATOM   998  C  CB    . ARG A 1 126 ? 16.826  21.617  3.075   1 33.14  ? 126 ARG A CB    1 1 
ATOM   999  C  CG    . ARG A 1 126 ? 18.008  22.007  3.914   1 39.36  ? 126 ARG A CG    1 1 
ATOM   1000 C  CD    . ARG A 1 126 ? 17.563  22.137  5.35    1 45.66  ? 126 ARG A CD    1 1 
ATOM   1001 N  NE    . ARG A 1 126 ? 18.425  23.056  6.093   1 51.26  ? 126 ARG A NE    1 1 
ATOM   1002 C  CZ    . ARG A 1 126 ? 18.124  23.574  7.279   1 54.77  ? 126 ARG A CZ    1 1 
ATOM   1003 N  NH1   . ARG A 1 126 ? 18.967  24.406  7.88    1 54.74  ? 126 ARG A NH1   1 1 
ATOM   1004 N  NH2   . ARG A 1 126 ? 16.975  23.266  7.876   1 54.88  ? 126 ARG A NH2   1 1 
ATOM   1005 N  N     . ALA A 1 127 ? 14.734  21.075  0.942   1 28.29  ? 127 ALA A N     1 1 
ATOM   1006 C  CA    . ALA A 1 127 ? 13.831  20.173  0.25    1 27.61  ? 127 ALA A CA    1 1 
ATOM   1007 C  C     . ALA A 1 127 ? 13.865  20.375  -1.238  1 26.65  ? 127 ALA A C     1 1 
ATOM   1008 O  O     . ALA A 1 127 ? 13.757  19.399  -1.969  1 26.86  ? 127 ALA A O     1 1 
ATOM   1009 C  CB    . ALA A 1 127 ? 12.419  20.359  0.755   1 28     ? 127 ALA A CB    1 1 
ATOM   1010 N  N     . TYR A 1 128 ? 13.991  21.625  -1.697  1 25.64  ? 128 TYR A N     1 1 
ATOM   1011 C  CA    . TYR A 1 128 ? 14.029  21.896  -3.122  1 25.48  ? 128 TYR A CA    1 1 
ATOM   1012 C  C     . TYR A 1 128 ? 15.305  21.322  -3.727  1 26.06  ? 128 TYR A C     1 1 
ATOM   1013 O  O     . TYR A 1 128 ? 15.236  20.595  -4.715  1 26.49  ? 128 TYR A O     1 1 
ATOM   1014 C  CB    . TYR A 1 128 ? 13.891  23.409  -3.419  1 25.08  ? 128 TYR A CB    1 1 
ATOM   1015 C  CG    . TYR A 1 128 ? 14.346  23.763  -4.817  1 25.13  ? 128 TYR A CG    1 1 
ATOM   1016 C  CD1   . TYR A 1 128 ? 13.645  23.317  -5.929  1 25.73  ? 128 TYR A CD1   1 1 
ATOM   1017 C  CD2   . TYR A 1 128 ? 15.545  24.428  -5.029  1 25.67  ? 128 TYR A CD2   1 1 
ATOM   1018 C  CE1   . TYR A 1 128 ? 14.106  23.549  -7.213  1 26.71  ? 128 TYR A CE1   1 1 
ATOM   1019 C  CE2   . TYR A 1 128 ? 16.016  24.67   -6.309  1 26.69  ? 128 TYR A CE2   1 1 
ATOM   1020 C  CZ    . TYR A 1 128 ? 15.289  24.237  -7.401  1 28.12  ? 128 TYR A CZ    1 1 
ATOM   1021 O  OH    . TYR A 1 128 ? 15.762  24.471  -8.672  1 30.58  ? 128 TYR A OH    1 1 
ATOM   1022 N  N     . SER A 1 129 ? 16.462  21.697  -3.165  1 25.86  ? 129 SER A N     1 1 
ATOM   1023 C  CA    . SER A 1 129 ? 17.774  21.315  -3.652  1 25.99  ? 129 SER A CA    1 1 
ATOM   1024 C  C     . SER A 1 129 ? 18.005  19.812  -3.578  1 26.2   ? 129 SER A C     1 1 
ATOM   1025 O  O     . SER A 1 129 ? 18.414  19.218  -4.573  1 26.92  ? 129 SER A O     1 1 
ATOM   1026 C  CB    . SER A 1 129 ? 18.853  22.066  -2.883  1 27.25  ? 129 SER A CB    1 1 
ATOM   1027 O  OG    . SER A 1 129 ? 20.074  22.081  -3.595  1 30.01  ? 129 SER A OG    1 1 
ATOM   1028 N  N     . VAL A 1 130 ? 17.742  19.184  -2.42   1 25.3   ? 130 VAL A N     1 1 
ATOM   1029 C  CA    . VAL A 1 130 ? 17.922  17.735  -2.286  1 24.72  ? 130 VAL A CA    1 1 
ATOM   1030 C  C     . VAL A 1 130 ? 16.879  16.967  -3.128  1 24.01  ? 130 VAL A C     1 1 
ATOM   1031 O  O     . VAL A 1 130 ? 17.2    15.937  -3.724  1 24.14  ? 130 VAL A O     1 1 
ATOM   1032 C  CB    . VAL A 1 130 ? 17.957  17.272  -0.806  1 24.99  ? 130 VAL A CB    1 1 
ATOM   1033 C  CG1   . VAL A 1 130 ? 18.004  15.75   -0.701  1 25.27  ? 130 VAL A CG1   1 1 
ATOM   1034 C  CG2   . VAL A 1 130 ? 19.133  17.898  -0.066  1 25.15  ? 130 VAL A CG2   1 1 
ATOM   1035 N  N     . GLY A 1 131 ? 15.668  17.508  -3.214  1 22.83  ? 131 GLY A N     1 1 
ATOM   1036 C  CA    . GLY A 1 131 ? 14.595  16.915  -3.994  1 22.28  ? 131 GLY A CA    1 1 
ATOM   1037 C  C     . GLY A 1 131 ? 14.861  16.819  -5.482  1 21.78  ? 131 GLY A C     1 1 
ATOM   1038 O  O     . GLY A 1 131 ? 14.416  15.866  -6.115  1 21.37  ? 131 GLY A O     1 1 
ATOM   1039 N  N     . ARG A 1 132 ? 15.603  17.778  -6.064  1 21.9   ? 132 ARG A N     1 1 
ATOM   1040 C  CA    . ARG A 1 132 ? 15.89   17.728  -7.503  1 22.45  ? 132 ARG A CA    1 1 
ATOM   1041 C  C     . ARG A 1 132 ? 17.054  16.798  -7.877  1 22.96  ? 132 ARG A C     1 1 
ATOM   1042 O  O     . ARG A 1 132 ? 17.38   16.684  -9.056  1 23.01  ? 132 ARG A O     1 1 
ATOM   1043 C  CB    . ARG A 1 132 ? 16.091  19.124  -8.092  1 23.56  ? 132 ARG A CB    1 1 
ATOM   1044 C  CG    . ARG A 1 132 ? 17.36   19.814  -7.643  1 25.64  ? 132 ARG A CG    1 1 
ATOM   1045 C  CD    . ARG A 1 132 ? 17.383  21.265  -8.099  1 27.39  ? 132 ARG A CD    1 1 
ATOM   1046 N  NE    . ARG A 1 132 ? 18.476  21.501  -9.041  1 29.38  ? 132 ARG A NE    1 1 
ATOM   1047 C  CZ    . ARG A 1 132 ? 18.386  21.347  -10.358 1 31.03  ? 132 ARG A CZ    1 1 
ATOM   1048 N  NH1   . ARG A 1 132 ? 17.239  20.991  -10.913 1 30.81  ? 132 ARG A NH1   1 1 
ATOM   1049 N  NH2   . ARG A 1 132 ? 19.441  21.559  -11.128 1 30.84  ? 132 ARG A NH2   1 1 
ATOM   1050 N  N     . THR A 1 133 ? 17.643  16.099  -6.898  1 23.25  ? 133 THR A N     1 1 
ATOM   1051 C  CA    . THR A 1 133 ? 18.729  15.159  -7.139  1 24.13  ? 133 THR A CA    1 1 
ATOM   1052 C  C     . THR A 1 133 ? 18.271  13.762  -7.531  1 25.08  ? 133 THR A C     1 1 
ATOM   1053 O  O     . THR A 1 133 ? 19.042  13.031  -8.128  1 25.7   ? 133 THR A O     1 1 
ATOM   1054 C  CB    . THR A 1 133 ? 19.585  15.012  -5.881  1 25.52  ? 133 THR A CB    1 1 
ATOM   1055 O  OG1   . THR A 1 133 ? 18.812  14.413  -4.836  1 26.32  ? 133 THR A OG1   1 1 
ATOM   1056 C  CG2   . THR A 1 133 ? 20.154  16.324  -5.418  1 26.14  ? 133 THR A CG2   1 1 
ATOM   1057 N  N     . GLY A 1 134 ? 17.073  13.365  -7.128  1 25.26  ? 134 GLY A N     1 1 
ATOM   1058 C  CA    . GLY A 1 134 ? 16.6    12.004  -7.349  1 25.68  ? 134 GLY A CA    1 1 
ATOM   1059 C  C     . GLY A 1 134 ? 16.709  11.153  -6.092  1 26.19  ? 134 GLY A C     1 1 
ATOM   1060 O  O     . GLY A 1 134 ? 16.165  10.043  -6.05   1 26.55  ? 134 GLY A O     1 1 
ATOM   1061 N  N     . TYR A 1 135 ? 17.398  11.676  -5.039  1 26     ? 135 TYR A N     1 1 
ATOM   1062 C  CA    . TYR A 1 135 ? 17.553  11.038  -3.733  1 26.13  ? 135 TYR A CA    1 1 
ATOM   1063 C  C     . TYR A 1 135 ? 16.389  11.479  -2.846  1 26.61  ? 135 TYR A C     1 1 
ATOM   1064 O  O     . TYR A 1 135 ? 16.119  12.672  -2.723  1 26.44  ? 135 TYR A O     1 1 
ATOM   1065 C  CB    . TYR A 1 135 ? 18.872  11.444  -3.071  1 25.77  ? 135 TYR A CB    1 1 
ATOM   1066 C  CG    . TYR A 1 135 ? 20.093  11.027  -3.853  1 26.7   ? 135 TYR A CG    1 1 
ATOM   1067 C  CD1   . TYR A 1 135 ? 20.315  9.695   -4.175  1 27.69  ? 135 TYR A CD1   1 1 
ATOM   1068 C  CD2   . TYR A 1 135 ? 21.064  11.951  -4.209  1 27.68  ? 135 TYR A CD2   1 1 
ATOM   1069 C  CE1   . TYR A 1 135 ? 21.448  9.3     -4.878  1 28.47  ? 135 TYR A CE1   1 1 
ATOM   1070 C  CE2   . TYR A 1 135 ? 22.207  11.569  -4.903  1 28.49  ? 135 TYR A CE2   1 1 
ATOM   1071 C  CZ    . TYR A 1 135 ? 22.396  10.241  -5.236  1 29.46  ? 135 TYR A CZ    1 1 
ATOM   1072 O  OH    . TYR A 1 135 ? 23.526  9.869   -5.925  1 31.04  ? 135 TYR A OH    1 1 
ATOM   1073 N  N     . PRO A 1 136 ? 15.671  10.524  -2.239  1 26.87  ? 136 PRO A N     1 1 
ATOM   1074 C  CA    . PRO A 1 136 ? 14.517  10.888  -1.41   1 26.99  ? 136 PRO A CA    1 1 
ATOM   1075 C  C     . PRO A 1 136 ? 14.826  11.847  -0.281  1 27.23  ? 136 PRO A C     1 1 
ATOM   1076 O  O     . PRO A 1 136 ? 15.893  11.807  0.307   1 27.12  ? 136 PRO A O     1 1 
ATOM   1077 C  CB    . PRO A 1 136 ? 14.032  9.546   -0.868  1 27.68  ? 136 PRO A CB    1 1 
ATOM   1078 C  CG    . PRO A 1 136 ? 14.515  8.552   -1.856  1 28.18  ? 136 PRO A CG    1 1 
ATOM   1079 C  CD    . PRO A 1 136 ? 15.84   9.064   -2.322  1 26.52  ? 136 PRO A CD    1 1 
ATOM   1080 N  N     . TYR A 1 137 ? 13.883  12.722  0       1 27.59  ? 137 TYR A N     1 1 
ATOM   1081 C  CA    . TYR A 1 137 ? 14.021  13.703  1.06    1 28.48  ? 137 TYR A CA    1 1 
ATOM   1082 C  C     . TYR A 1 137 ? 12.833  13.555  1.992   1 29.65  ? 137 TYR A C     1 1 
ATOM   1083 O  O     . TYR A 1 137 ? 11.686  13.744  1.579   1 30.08  ? 137 TYR A O     1 1 
ATOM   1084 C  CB    . TYR A 1 137 ? 14.085  15.114  0.477   1 28.25  ? 137 TYR A CB    1 1 
ATOM   1085 C  CG    . TYR A 1 137 ? 14.297  16.18   1.521   1 29.03  ? 137 TYR A CG    1 1 
ATOM   1086 C  CD1   . TYR A 1 137 ? 15.571  16.536  1.932   1 29.68  ? 137 TYR A CD1   1 1 
ATOM   1087 C  CD2   . TYR A 1 137 ? 13.226  16.86   2.07    1 30.56  ? 137 TYR A CD2   1 1 
ATOM   1088 C  CE1   . TYR A 1 137 ? 15.77   17.524  2.885   1 30.78  ? 137 TYR A CE1   1 1 
ATOM   1089 C  CE2   . TYR A 1 137 ? 13.411  17.852  3.022   1 31.61  ? 137 TYR A CE2   1 1 
ATOM   1090 C  CZ    . TYR A 1 137 ? 14.685  18.192  3.418   1 32.29  ? 137 TYR A CZ    1 1 
ATOM   1091 O  OH    . TYR A 1 137 ? 14.839  19.182  4.356   1 34.26  ? 137 TYR A OH    1 1 
ATOM   1092 N  N     . ILE A 1 138 ? 13.102  13.177  3.242   1 29.68  ? 138 ILE A N     1 1 
ATOM   1093 C  CA    . ILE A 1 138 ? 12.05   12.968  4.224   1 29.73  ? 138 ILE A CA    1 1 
ATOM   1094 C  C     . ILE A 1 138 ? 12.155  14.051  5.29    1 29.8   ? 138 ILE A C     1 1 
ATOM   1095 O  O     . ILE A 1 138 ? 13.162  14.138  5.992   1 29.82  ? 138 ILE A O     1 1 
ATOM   1096 C  CB    . ILE A 1 138 ? 12.137  11.56   4.855   1 30.09  ? 138 ILE A CB    1 1 
ATOM   1097 C  CG1   . ILE A 1 138 ? 12.42   10.444  3.814   1 31.02  ? 138 ILE A CG1   1 1 
ATOM   1098 C  CG2   . ILE A 1 138 ? 10.893  11.271  5.677   1 30.49  ? 138 ILE A CG2   1 1 
ATOM   1099 C  CD1   . ILE A 1 138 ? 11.419  10.288  2.791   1 32.43  ? 138 ILE A CD1   1 1 
ATOM   1100 N  N     . TYR A 1 139 ? 11.129  14.888  5.396   1 29.56  ? 139 TYR A N     1 1 
ATOM   1101 C  CA    . TYR A 1 139 ? 11.1    15.951  6.38    1 29.79  ? 139 TYR A CA    1 1 
ATOM   1102 C  C     . TYR A 1 139 ? 10.182  15.491  7.501   1 29.64  ? 139 TYR A C     1 1 
ATOM   1103 O  O     . TYR A 1 139 ? 8.986   15.381  7.287   1 29.59  ? 139 TYR A O     1 1 
ATOM   1104 C  CB    . TYR A 1 139 ? 10.568  17.214  5.712   1 30.23  ? 139 TYR A CB    1 1 
ATOM   1105 C  CG    . TYR A 1 139 ? 10.657  18.457  6.562   1 31.73  ? 139 TYR A CG    1 1 
ATOM   1106 C  CD1   . TYR A 1 139 ? 11.71   18.648  7.439   1 33.13  ? 139 TYR A CD1   1 1 
ATOM   1107 C  CD2   . TYR A 1 139 ? 9.725   19.469  6.441   1 33.07  ? 139 TYR A CD2   1 1 
ATOM   1108 C  CE1   . TYR A 1 139 ? 11.813  19.804  8.201   1 34.24  ? 139 TYR A CE1   1 1 
ATOM   1109 C  CE2   . TYR A 1 139 ? 9.822   20.634  7.187   1 34.26  ? 139 TYR A CE2   1 1 
ATOM   1110 C  CZ    . TYR A 1 139 ? 10.859  20.793  8.08    1 35.29  ? 139 TYR A CZ    1 1 
ATOM   1111 O  OH    . TYR A 1 139 ? 10.939  21.946  8.822   1 37.1   ? 139 TYR A OH    1 1 
ATOM   1112 N  N     . ILE A 1 140 ? 10.737  15.164  8.67    1 29.52  ? 140 ILE A N     1 1 
ATOM   1113 C  CA    . ILE A 1 140 ? 9.964   14.647  9.795   1 30.15  ? 140 ILE A CA    1 1 
ATOM   1114 C  C     . ILE A 1 140 ? 9.735   15.723  10.827  1 31.17  ? 140 ILE A C     1 1 
ATOM   1115 O  O     . ILE A 1 140 ? 10.695  16.204  11.413  1 31.02  ? 140 ILE A O     1 1 
ATOM   1116 C  CB    . ILE A 1 140 ? 10.694  13.435  10.394  1 30.57  ? 140 ILE A CB    1 1 
ATOM   1117 C  CG1   . ILE A 1 140 ? 10.863  12.333  9.34    1 31.4   ? 140 ILE A CG1   1 1 
ATOM   1118 C  CG2   . ILE A 1 140 ? 9.964   12.927  11.622  1 31.05  ? 140 ILE A CG2   1 1 
ATOM   1119 C  CD1   . ILE A 1 140 ? 11.741  11.23   9.746   1 32.64  ? 140 ILE A CD1   1 1 
ATOM   1120 N  N     . VAL A 1 141 ? 8.47    16.132  11.036  1 32.24  ? 141 VAL A N     1 1 
ATOM   1121 C  CA    . VAL A 1 141 ? 8.163   17.228  11.959  1 33.74  ? 141 VAL A CA    1 1 
ATOM   1122 C  C     . VAL A 1 141 ? 7.264   16.779  13.12   1 35.52  ? 141 VAL A C     1 1 
ATOM   1123 O  O     . VAL A 1 141 ? 6.395   15.923  12.944  1 35.42  ? 141 VAL A O     1 1 
ATOM   1124 C  CB    . VAL A 1 141 ? 7.613   18.515  11.25   1 34.35  ? 141 VAL A CB    1 1 
ATOM   1125 C  CG1   . VAL A 1 141 ? 8.215   18.719  9.858   1 34.95  ? 141 VAL A CG1   1 1 
ATOM   1126 C  CG2   . VAL A 1 141 ? 6.104   18.529  11.166  1 34.92  ? 141 VAL A CG2   1 1 
ATOM   1127 N  N     . ASP A 1 142 ? 7.483   17.356  14.31   1 37.01  ? 142 ASP A N     1 1 
ATOM   1128 C  CA    . ASP A 1 142 ? 6.675   17.023  15.481  1 39.1   ? 142 ASP A CA    1 1 
ATOM   1129 C  C     . ASP A 1 142 ? 5.415   17.874  15.47   1 40.07  ? 142 ASP A C     1 1 
ATOM   1130 O  O     . ASP A 1 142 ? 5.502   19.098  15.401  1 40.69  ? 142 ASP A O     1 1 
ATOM   1131 C  CB    . ASP A 1 142 ? 7.459   17.272  16.779  1 42.06  ? 142 ASP A CB    1 1 
ATOM   1132 C  CG    . ASP A 1 142 ? 8.09    16.034  17.39   1 49.63  ? 142 ASP A CG    1 1 
ATOM   1133 O  OD1   . ASP A 1 142 ? 8.368   15.06   16.633  1 50.86  ? 142 ASP A OD1   1 1 
ATOM   1134 O  OD2   . ASP A 1 142 ? 8.319   16.035  18.614  1 53.03  ? 142 ASP A OD2   1 1 
ATOM   1135 N  N     . PHE A 1 143 ? 4.252   17.236  15.514  1 39.92  ? 143 PHE A N     1 1 
ATOM   1136 C  CA    . PHE A 1 143 ? 2.977   17.928  15.514  1 40.45  ? 143 PHE A CA    1 1 
ATOM   1137 C  C     . PHE A 1 143 ? 2.297   17.547  16.822  1 41.39  ? 143 PHE A C     1 1 
ATOM   1138 O  O     . PHE A 1 143 ? 1.941   16.377  16.974  1 41.51  ? 143 PHE A O     1 1 
ATOM   1139 C  CB    . PHE A 1 143 ? 2.134   17.429  14.32   1 40.21  ? 143 PHE A CB    1 1 
ATOM   1140 C  CG    . PHE A 1 143 ? 0.797   18.116  14.142  1 40.75  ? 143 PHE A CG    1 1 
ATOM   1141 C  CD1   . PHE A 1 143 ? -0.336  17.652  14.794  1 41.21  ? 143 PHE A CD1   1 1 
ATOM   1142 C  CD2   . PHE A 1 143 ? 0.672   19.218  13.316  1 41.44  ? 143 PHE A CD2   1 1 
ATOM   1143 C  CE1   . PHE A 1 143 ? -1.551  18.304  14.658  1 41.61  ? 143 PHE A CE1   1 1 
ATOM   1144 C  CE2   . PHE A 1 143 ? -0.552  19.849  13.16   1 42     ? 143 PHE A CE2   1 1 
ATOM   1145 C  CZ    . PHE A 1 143 ? -1.657  19.385  13.829  1 41.53  ? 143 PHE A CZ    1 1 
ATOM   1146 N  N     . VAL A 1 144 ? 2.116   18.479  17.784  1 41.85  ? 144 VAL A N     1 1 
ATOM   1147 C  CA    . VAL A 1 144 ? 2.524   19.887  17.752  1 42.78  ? 144 VAL A CA    1 1 
ATOM   1148 C  C     . VAL A 1 144 ? 3.442   20.193  18.954  1 44.25  ? 144 VAL A C     1 1 
ATOM   1149 O  O     . VAL A 1 144 ? 3.497   19.425  19.916  1 44.54  ? 144 VAL A O     1 1 
ATOM   1150 C  CB    . VAL A 1 144 ? 1.295   20.839  17.794  1 42.94  ? 144 VAL A CB    1 1 
ATOM   1151 C  CG1   . VAL A 1 144 ? 0.525   20.842  16.489  1 43.14  ? 144 VAL A CG1   1 1 
ATOM   1152 C  CG2   . VAL A 1 144 ? 0.395   20.521  18.975  1 43.37  ? 144 VAL A CG2   1 1 
ATOM   1153 N  N     . LYS A 1 145 ? 4.139   21.33   18.907  1 45.19  ? 145 LYS A N     1 1 
ATOM   1154 C  CA    . LYS A 1 145 ? 4.98    21.804  19.995  1 46.94  ? 145 LYS A CA    1 1 
ATOM   1155 C  C     . LYS A 1 145 ? 4.582   23.259  20.192  1 48.45  ? 145 LYS A C     1 1 
ATOM   1156 O  O     . LYS A 1 145 ? 4.642   24.036  19.235  1 48.67  ? 145 LYS A O     1 1 
ATOM   1157 C  CB    . LYS A 1 145 ? 6.462   21.754  19.595  1 49.18  ? 145 LYS A CB    1 1 
ATOM   1158 C  CG    . LYS A 1 145 ? 7.369   20.94   20.522  1 53.83  ? 145 LYS A CG    1 1 
ATOM   1159 C  CD    . LYS A 1 145 ? 8.75    21.61   20.864  1 58.07  ? 145 LYS A CD    1 1 
ATOM   1160 C  CE    . LYS A 1 145 ? 9.381   22.537  19.842  1 61.22  ? 145 LYS A CE    1 1 
ATOM   1161 N  NZ    . LYS A 1 145 ? 9.25    23.965  20.24   1 63.38  ? 145 LYS A NZ    1 1 
ATOM   1162 N  N     . TYR A 1 146 ? 4.157   23.634  21.405  1 49.24  ? 146 TYR A N     1 1 
ATOM   1163 C  CA    . TYR A 1 146 ? 3.747   25.008  21.664  1 50.39  ? 146 TYR A CA    1 1 
ATOM   1164 C  C     . TYR A 1 146 ? 4.935   25.901  21.828  1 51.68  ? 146 TYR A C     1 1 
ATOM   1165 O  O     . TYR A 1 146 ? 5.91    25.524  22.472  1 51.91  ? 146 TYR A O     1 1 
ATOM   1166 C  CB    . TYR A 1 146 ? 2.918   25.104  22.945  1 50.41  ? 146 TYR A CB    1 1 
ATOM   1167 C  CG    . TYR A 1 146 ? 1.525   24.548  22.809  1 51.09  ? 146 TYR A CG    1 1 
ATOM   1168 C  CD1   . TYR A 1 146 ? 1.263   23.213  23.06   1 51.99  ? 146 TYR A CD1   1 1 
ATOM   1169 C  CD2   . TYR A 1 146 ? 0.458   25.368  22.472  1 52.02  ? 146 TYR A CD2   1 1 
ATOM   1170 C  CE1   . TYR A 1 146 ? -0.017  22.695  22.941  1 53.02  ? 146 TYR A CE1   1 1 
ATOM   1171 C  CE2   . TYR A 1 146 ? -0.832  24.868  22.369  1 52.99  ? 146 TYR A CE2   1 1 
ATOM   1172 C  CZ    . TYR A 1 146 ? -1.065  23.525  22.595  1 54.04  ? 146 TYR A CZ    1 1 
ATOM   1173 O  OH    . TYR A 1 146 ? -2.329  23.001  22.49   1 55.54  ? 146 TYR A OH    1 1 
ATOM   1174 N  N     . GLU A 1 147 ? 4.843   27.104  21.28   1 52.43  ? 147 GLU A N     1 1 
ATOM   1175 C  CA    . GLU A 1 147 ? 5.872   28.111  21.483  1 53.48  ? 147 GLU A CA    1 1 
ATOM   1176 C  C     . GLU A 1 147 ? 5.634   28.658  22.891  1 53.88  ? 147 GLU A C     1 1 
ATOM   1177 O  O     . GLU A 1 147 ? 4.484   28.751  23.327  1 54.01  ? 147 GLU A O     1 1 
ATOM   1178 C  CB    . GLU A 1 147 ? 5.736   29.224  20.433  1 56.44  ? 147 GLU A CB    1 1 
ATOM   1179 C  CG    . GLU A 1 147 ? 6.298   28.824  19.08   1 62.04  ? 147 GLU A CG    1 1 
ATOM   1180 C  CD    . GLU A 1 147 ? 5.695   29.526  17.879  1 68.54  ? 147 GLU A CD    1 1 
ATOM   1181 O  OE1   . GLU A 1 147 ? 6.176   29.276  16.749  1 69.82  ? 147 GLU A OE1   1 1 
ATOM   1182 O  OE2   . GLU A 1 147 ? 4.745   30.322  18.062  1 70.36  ? 147 GLU A OE2   1 1 
ATOM   1183 N  N     . LEU A 1 148 ? 6.703   28.973  23.619  1 53.99  ? 148 LEU A N     1 1 
ATOM   1184 C  CA    . LEU A 1 148 ? 6.556   29.464  24.983  1 54.71  ? 148 LEU A CA    1 1 
ATOM   1185 C  C     . LEU A 1 148 ? 7.05    30.885  25.171  1 55.46  ? 148 LEU A C     1 1 
ATOM   1186 O  O     . LEU A 1 148 ? 7.95    31.34   24.461  1 55.9   ? 148 LEU A O     1 1 
ATOM   1187 C  CB    . LEU A 1 148 ? 7.344   28.562  25.936  1 54.86  ? 148 LEU A CB    1 1 
ATOM   1188 C  CG    . LEU A 1 148 ? 7.029   27.093  25.905  1 56.43  ? 148 LEU A CG    1 1 
ATOM   1189 C  CD1   . LEU A 1 148 ? 7.982   26.342  26.797  1 57.09  ? 148 LEU A CD1   1 1 
ATOM   1190 C  CD2   . LEU A 1 148 ? 5.595   26.827  26.319  1 57.07  ? 148 LEU A CD2   1 1 
ATOM   1191 N  N     . ASN A 1 149 ? 6.506   31.565  26.182  1 55.34  ? 149 ASN A N     1 1 
ATOM   1192 C  CA    . ASN A 1 149 ? 7.018   32.856  26.601  1 55.83  ? 149 ASN A CA    1 1 
ATOM   1193 C  C     . ASN A 1 149 ? 8.119   32.421  27.561  1 55.81  ? 149 ASN A C     1 1 
ATOM   1194 O  O     . ASN A 1 149 ? 7.798   31.884  28.613  1 55.69  ? 149 ASN A O     1 1 
ATOM   1195 C  CB    . ASN A 1 149 ? 5.937   33.612  27.355  1 57.31  ? 149 ASN A CB    1 1 
ATOM   1196 C  CG    . ASN A 1 149 ? 4.805   34.023  26.459  1 61.06  ? 149 ASN A CG    1 1 
ATOM   1197 O  OD1   . ASN A 1 149 ? 3.78    33.338  26.347  1 62.04  ? 149 ASN A OD1   1 1 
ATOM   1198 N  ND2   . ASN A 1 149 ? 4.977   35.156  25.791  1 62.17  ? 149 ASN A ND2   1 1 
ATOM   1199 N  N     . ASN A 1 150 ? 9.403   32.55   27.177  1 55.82  ? 150 ASN A N     1 1 
ATOM   1200 C  CA    . ASN A 1 150 ? 10.528  32.045  27.983  1 56.31  ? 150 ASN A CA    1 1 
ATOM   1201 C  C     . ASN A 1 150 ? 10.659  32.66   29.389  1 56.33  ? 150 ASN A C     1 1 
ATOM   1202 O  O     . ASN A 1 150 ? 11.399  32.138  30.225  1 56.34  ? 150 ASN A O     1 1 
ATOM   1203 C  CB    . ASN A 1 150 ? 11.848  32.164  27.219  1 57.55  ? 150 ASN A CB    1 1 
ATOM   1204 C  CG    . ASN A 1 150 ? 11.914  31.287  25.986  1 60.83  ? 150 ASN A CG    1 1 
ATOM   1205 O  OD1   . ASN A 1 150 ? 11.649  30.073  26.024  1 61.98  ? 150 ASN A OD1   1 1 
ATOM   1206 N  ND2   . ASN A 1 150 ? 12.278  31.884  24.864  1 61.46  ? 150 ASN A ND2   1 1 
ATOM   1207 N  N     . SER A 1 151 ? 9.924   33.736  29.656  1 56.12  ? 151 SER A N     1 1 
ATOM   1208 C  CA    . SER A 1 151 ? 9.937   34.386  30.956  1 56.3   ? 151 SER A CA    1 1 
ATOM   1209 C  C     . SER A 1 151 ? 9.236   33.497  31.998  1 56.02  ? 151 SER A C     1 1 
ATOM   1210 O  O     . SER A 1 151 ? 9.757   33.319  33.098  1 56.16  ? 151 SER A O     1 1 
ATOM   1211 C  CB    . SER A 1 151 ? 9.24    35.744  30.871  1 57.88  ? 151 SER A CB    1 1 
ATOM   1212 O  OG    . SER A 1 151 ? 9.655   36.499  29.743  1 60.3   ? 151 SER A OG    1 1 
ATOM   1213 N  N     . ASP A 1 152 ? 8.079   32.91   31.645  1 55.49  ? 152 ASP A N     1 1 
ATOM   1214 C  CA    . ASP A 1 152 ? 7.324   32.084  32.591  1 55.5   ? 152 ASP A CA    1 1 
ATOM   1215 C  C     . ASP A 1 152 ? 6.891   30.708  32.064  1 54.86  ? 152 ASP A C     1 1 
ATOM   1216 O  O     . ASP A 1 152 ? 6.022   30.074  32.672  1 55.17  ? 152 ASP A O     1 1 
ATOM   1217 C  CB    . ASP A 1 152 ? 6.091   32.851  33.108  1 57.34  ? 152 ASP A CB    1 1 
ATOM   1218 C  CG    . ASP A 1 152 ? 5.02    33.075  32.059  1 61.96  ? 152 ASP A CG    1 1 
ATOM   1219 O  OD1   . ASP A 1 152 ? 5.363   33.106  30.853  1 62.38  ? 152 ASP A OD1   1 1 
ATOM   1220 O  OD2   . ASP A 1 152 ? 3.84    33.212  32.441  1 64.72  ? 152 ASP A OD2   1 1 
ATOM   1221 N  N     . ARG A 1 153 ? 7.447   30.273  30.925  1 53.69  ? 153 ARG A N     1 1 
ATOM   1222 C  CA    . ARG A 1 153 ? 7.11    29.002  30.273  1 52.9   ? 153 ARG A CA    1 1 
ATOM   1223 C  C     . ARG A 1 153 ? 5.616   28.815  29.97   1 51.87  ? 153 ARG A C     1 1 
ATOM   1224 O  O     . ARG A 1 153 ? 5.164   27.677  29.854  1 52.04  ? 153 ARG A O     1 1 
ATOM   1225 C  CB    . ARG A 1 153 ? 7.647   27.798  31.054  1 53.85  ? 153 ARG A CB    1 1 
ATOM   1226 C  CG    . ARG A 1 153 ? 9.156   27.757  31.14   1 56.01  ? 153 ARG A CG    1 1 
ATOM   1227 C  CD    . ARG A 1 153 ? 9.635   26.343  31.383  1 58.07  ? 153 ARG A CD    1 1 
ATOM   1228 N  NE    . ARG A 1 153 ? 10.535  25.913  30.317  1 59.71  ? 153 ARG A NE    1 1 
ATOM   1229 C  CZ    . ARG A 1 153 ? 10.262  24.955  29.442  1 60.64  ? 153 ARG A CZ    1 1 
ATOM   1230 N  NH1   . ARG A 1 153 ? 9.123   24.279  29.52   1 59.33  ? 153 ARG A NH1   1 1 
ATOM   1231 N  NH2   . ARG A 1 153 ? 11.137  24.645  28.499  1 60.85  ? 153 ARG A NH2   1 1 
ATOM   1232 N  N     . SER A 1 154 ? 4.854   29.911  29.841  1 50.61  ? 154 SER A N     1 1 
ATOM   1233 C  CA    . SER A 1 154 ? 3.438   29.809  29.504  1 49.96  ? 154 SER A CA    1 1 
ATOM   1234 C  C     . SER A 1 154 ? 3.309   29.603  27.993  1 49.25  ? 154 SER A C     1 1 
ATOM   1235 O  O     . SER A 1 154 ? 4.113   30.133  27.225  1 49.61  ? 154 SER A O     1 1 
ATOM   1236 C  CB    . SER A 1 154 ? 2.685   31.057  29.94   1 51.1   ? 154 SER A CB    1 1 
ATOM   1237 O  OG    . SER A 1 154 ? 3.138   32.186  29.214  1 53.53  ? 154 SER A OG    1 1 
ATOM   1238 N  N     . ARG A 1 155 ? 2.313   28.824  27.565  1 48.22  ? 155 ARG A N     1 1 
ATOM   1239 C  CA    . ARG A 1 155 ? 2.116   28.518  26.15   1 47.61  ? 155 ARG A CA    1 1 
ATOM   1240 C  C     . ARG A 1 155 ? 1.449   29.6    25.327  1 47.38  ? 155 ARG A C     1 1 
ATOM   1241 O  O     . ARG A 1 155 ? 0.429   30.165  25.731  1 47.67  ? 155 ARG A O     1 1 
ATOM   1242 C  CB    . ARG A 1 155 ? 1.299   27.242  25.991  1 48.03  ? 155 ARG A CB    1 1 
ATOM   1243 C  CG    . ARG A 1 155 ? 1.988   26.043  26.545  1 49.6   ? 155 ARG A CG    1 1 
ATOM   1244 C  CD    . ARG A 1 155 ? 1.09    24.842  26.487  1 51.12  ? 155 ARG A CD    1 1 
ATOM   1245 N  NE    . ARG A 1 155 ? 1.803   23.665  26.96   1 52.58  ? 155 ARG A NE    1 1 
ATOM   1246 C  CZ    . ARG A 1 155 ? 1.839   23.265  28.224  1 54.44  ? 155 ARG A CZ    1 1 
ATOM   1247 N  NH1   . ARG A 1 155 ? 1.179   23.936  29.161  1 53.76  ? 155 ARG A NH1   1 1 
ATOM   1248 N  NH2   . ARG A 1 155 ? 2.531   22.191  28.563  1 55.03  ? 155 ARG A NH2   1 1 
ATOM   1249 N  N     . LYS A 1 156 ? 1.973   29.806  24.119  1 46.62  ? 156 LYS A N     1 1 
ATOM   1250 C  CA    . LYS A 1 156 ? 1.421   30.728  23.132  1 46.42  ? 156 LYS A CA    1 1 
ATOM   1251 C  C     . LYS A 1 156 ? 0.431   29.956  22.234  1 45.92  ? 156 LYS A C     1 1 
ATOM   1252 O  O     . LYS A 1 156 ? 0.528   28.729  22.125  1 46.22  ? 156 LYS A O     1 1 
ATOM   1253 C  CB    . LYS A 1 156 ? 2.549   31.32   22.271  1 48.09  ? 156 LYS A CB    1 1 
ATOM   1254 C  CG    . LYS A 1 156 ? 3.603   32.076  23.064  1 51.42  ? 156 LYS A CG    1 1 
ATOM   1255 C  CD    . LYS A 1 156 ? 4.624   32.699  22.138  1 55.52  ? 156 LYS A CD    1 1 
ATOM   1256 C  CE    . LYS A 1 156 ? 5.576   33.588  22.893  1 59.6   ? 156 LYS A CE    1 1 
ATOM   1257 N  NZ    . LYS A 1 156 ? 6.391   34.432  21.988  1 61.93  ? 156 LYS A NZ    1 1 
ATOM   1258 N  N     . ASN A 1 157 ? -0.507  30.662  21.576  1 44.89  ? 157 ASN A N     1 1 
ATOM   1259 C  CA    . ASN A 1 157 ? -1.475  30      20.697  1 44.06  ? 157 ASN A CA    1 1 
ATOM   1260 C  C     . ASN A 1 157 ? -0.779  29.266  19.558  1 42.81  ? 157 ASN A C     1 1 
ATOM   1261 O  O     . ASN A 1 157 ? 0.277   29.701  19.086  1 42.8   ? 157 ASN A O     1 1 
ATOM   1262 C  CB    . ASN A 1 157 ? -2.507  30.985  20.153  1 45.14  ? 157 ASN A CB    1 1 
ATOM   1263 C  CG    . ASN A 1 157 ? -3.671  31.195  21.087  1 48.64  ? 157 ASN A CG    1 1 
ATOM   1264 O  OD1   . ASN A 1 157 ? -4.288  30.246  21.575  1 49.65  ? 157 ASN A OD1   1 1 
ATOM   1265 N  ND2   . ASN A 1 157 ? -4.011  32.446  21.35   1 49.8   ? 157 ASN A ND2   1 1 
ATOM   1266 N  N     . LEU A 1 158 ? -1.345  28.123  19.155  1 41.54  ? 158 LEU A N     1 1 
ATOM   1267 C  CA    . LEU A 1 158 ? -0.794  27.316  18.079  1 40.42  ? 158 LEU A CA    1 1 
ATOM   1268 C  C     . LEU A 1 158 ? -0.731  28.09   16.783  1 39.41  ? 158 LEU A C     1 1 
ATOM   1269 O  O     . LEU A 1 158 ? -1.657  28.833  16.431  1 39.57  ? 158 LEU A O     1 1 
ATOM   1270 C  CB    . LEU A 1 158 ? -1.621  26.046  17.855  1 40.16  ? 158 LEU A CB    1 1 
ATOM   1271 C  CG    . LEU A 1 158 ? -1.379  24.906  18.806  1 41.44  ? 158 LEU A CG    1 1 
ATOM   1272 C  CD1   . LEU A 1 158 ? -2.224  23.729  18.429  1 41.87  ? 158 LEU A CD1   1 1 
ATOM   1273 C  CD2   . LEU A 1 158 ? 0.083   24.478  18.798  1 42.45  ? 158 LEU A CD2   1 1 
ATOM   1274 N  N     . ARG A 1 159 ? 0.381   27.928  16.09   1 38     ? 159 ARG A N     1 1 
ATOM   1275 C  CA    . ARG A 1 159 ? 0.582   28.571  14.812  1 37.09  ? 159 ARG A CA    1 1 
ATOM   1276 C  C     . ARG A 1 159 ? 0.753   27.492  13.749  1 35.18  ? 159 ARG A C     1 1 
ATOM   1277 O  O     . ARG A 1 159 ? 1.421   26.488  13.99   1 35.12  ? 159 ARG A O     1 1 
ATOM   1278 C  CB    . ARG A 1 159 ? 1.775   29.521  14.886  1 39.07  ? 159 ARG A CB    1 1 
ATOM   1279 C  CG    . ARG A 1 159 ? 1.415   30.857  15.543  1 43.28  ? 159 ARG A CG    1 1 
ATOM   1280 C  CD    . ARG A 1 159 ? 1.953   32.082  14.805  1 47.53  ? 159 ARG A CD    1 1 
ATOM   1281 N  NE    . ARG A 1 159 ? 1.93    31.909  13.351  1 51.11  ? 159 ARG A NE    1 1 
ATOM   1282 C  CZ    . ARG A 1 159 ? 2.033   32.895  12.469  1 53.6   ? 159 ARG A CZ    1 1 
ATOM   1283 N  NH1   . ARG A 1 159 ? 2.029   32.631  11.17   1 53.37  ? 159 ARG A NH1   1 1 
ATOM   1284 N  NH2   . ARG A 1 159 ? 2.143   34.155  12.879  1 53.59  ? 159 ARG A NH2   1 1 
ATOM   1285 N  N     . PHE A 1 160 ? 0.1     27.665  12.599  1 33.5   ? 160 PHE A N     1 1 
ATOM   1286 C  CA    . PHE A 1 160 ? 0.161   26.676  11.532  1 32.29  ? 160 PHE A CA    1 1 
ATOM   1287 C  C     . PHE A 1 160 ? 0.706   27.26   10.258  1 31.28  ? 160 PHE A C     1 1 
ATOM   1288 O  O     . PHE A 1 160 ? 0.446   28.424  9.933   1 31.19  ? 160 PHE A O     1 1 
ATOM   1289 C  CB    . PHE A 1 160 ? -1.234  26.101  11.245  1 31.92  ? 160 PHE A CB    1 1 
ATOM   1290 C  CG    . PHE A 1 160 ? -1.838  25.395  12.423  1 32.35  ? 160 PHE A CG    1 1 
ATOM   1291 C  CD1   . PHE A 1 160 ? -1.468  24.102  12.741  1 32.95  ? 160 PHE A CD1   1 1 
ATOM   1292 C  CD2   . PHE A 1 160 ? -2.772  26.026  13.22   1 33.26  ? 160 PHE A CD2   1 1 
ATOM   1293 C  CE1   . PHE A 1 160 ? -2.021  23.452  13.838  1 33.75  ? 160 PHE A CE1   1 1 
ATOM   1294 C  CE2   . PHE A 1 160 ? -3.331  25.37   14.31   1 34.19  ? 160 PHE A CE2   1 1 
ATOM   1295 C  CZ    . PHE A 1 160 ? -2.948  24.088  14.615  1 33.83  ? 160 PHE A CZ    1 1 
ATOM   1296 N  N     . PRO A 1 161 ? 1.444   26.449  9.494   1 30.59  ? 161 PRO A N     1 1 
ATOM   1297 C  CA    . PRO A 1 161 ? 1.942   26.937  8.211   1 30.57  ? 161 PRO A CA    1 1 
ATOM   1298 C  C     . PRO A 1 161 ? 0.82    27.094  7.194   1 30.48  ? 161 PRO A C     1 1 
ATOM   1299 O  O     . PRO A 1 161 ? -0.238  26.482  7.327   1 30.81  ? 161 PRO A O     1 1 
ATOM   1300 C  CB    . PRO A 1 161 ? 2.903   25.83   7.772   1 31.26  ? 161 PRO A CB    1 1 
ATOM   1301 C  CG    . PRO A 1 161 ? 2.371   24.606  8.407   1 31.6   ? 161 PRO A CG    1 1 
ATOM   1302 C  CD    . PRO A 1 161 ? 1.867   25.057  9.745   1 29.97  ? 161 PRO A CD    1 1 
ATOM   1303 N  N     . ASN A 1 162 ? 1.066   27.885  6.148   1 30.21  ? 162 ASN A N     1 1 
ATOM   1304 C  CA    . ASN A 1 162 ? 0.134   28.05   5.037   1 30.53  ? 162 ASN A CA    1 1 
ATOM   1305 C  C     . ASN A 1 162 ? -0.01   26.686  4.336   1 30.03  ? 162 ASN A C     1 1 
ATOM   1306 O  O     . ASN A 1 162 ? 0.993   25.989  4.175   1 29.82  ? 162 ASN A O     1 1 
ATOM   1307 C  CB    . ASN A 1 162 ? 0.708   29.067  4.052   1 32.49  ? 162 ASN A CB    1 1 
ATOM   1308 C  CG    . ASN A 1 162 ? -0.21   29.416  2.911   1 37.51  ? 162 ASN A CG    1 1 
ATOM   1309 O  OD1   . ASN A 1 162 ? -0.56   28.586  2.068   1 38.77  ? 162 ASN A OD1   1 1 
ATOM   1310 N  ND2   . ASN A 1 162 ? -0.622  30.669  2.858   1 39.38  ? 162 ASN A ND2   1 1 
ATOM   1311 N  N     . PRO A 1 163 ? -1.234  26.272  3.943   1 29.47  ? 163 PRO A N     1 1 
ATOM   1312 C  CA    . PRO A 1 163 ? -1.394  24.959  3.289   1 29.07  ? 163 PRO A CA    1 1 
ATOM   1313 C  C     . PRO A 1 163 ? -0.477  24.733  2.088   1 28.83  ? 163 PRO A C     1 1 
ATOM   1314 O  O     . PRO A 1 163 ? -0.196  23.588  1.746   1 29.26  ? 163 PRO A O     1 1 
ATOM   1315 C  CB    . PRO A 1 163 ? -2.865  24.932  2.87    1 29.85  ? 163 PRO A CB    1 1 
ATOM   1316 C  CG    . PRO A 1 163 ? -3.537  25.91   3.749   1 30.57  ? 163 PRO A CG    1 1 
ATOM   1317 C  CD    . PRO A 1 163 ? -2.524  26.968  4.091   1 29.06  ? 163 PRO A CD    1 1 
ATOM   1318 N  N     . ALA A 1 164 ? 0.019   25.813  1.47    1 27.96  ? 164 ALA A N     1 1 
ATOM   1319 C  CA    . ALA A 1 164 ? 0.922   25.701  0.339   1 27.47  ? 164 ALA A CA    1 1 
ATOM   1320 C  C     . ALA A 1 164 ? 2.263   25.087  0.724   1 26.77  ? 164 ALA A C     1 1 
ATOM   1321 O  O     . ALA A 1 164 ? 2.878   24.443  -0.117  1 26.98  ? 164 ALA A O     1 1 
ATOM   1322 C  CB    . ALA A 1 164 ? 1.129   27.058  -0.311  1 27.54  ? 164 ALA A CB    1 1 
ATOM   1323 N  N     . ILE A 1 165 ? 2.713   25.258  1.977   1 25.91  ? 165 ILE A N     1 1 
ATOM   1324 C  CA    . ILE A 1 165 ? 4.007   24.707  2.409   1 25.54  ? 165 ILE A CA    1 1 
ATOM   1325 C  C     . ILE A 1 165 ? 4.008   23.178  2.396   1 24.71  ? 165 ILE A C     1 1 
ATOM   1326 O  O     . ILE A 1 165 ? 4.769   22.597  1.618   1 24.7   ? 165 ILE A O     1 1 
ATOM   1327 C  CB    . ILE A 1 165 ? 4.527   25.28   3.751   1 26.08  ? 165 ILE A CB    1 1 
ATOM   1328 C  CG1   . ILE A 1 165 ? 4.288   26.786  3.877   1 26.92  ? 165 ILE A CG1   1 1 
ATOM   1329 C  CG2   . ILE A 1 165 ? 5.978   24.914  3.964   1 26.79  ? 165 ILE A CG2   1 1 
ATOM   1330 C  CD1   . ILE A 1 165 ? 4.816   27.57   2.801   1 28.22  ? 165 ILE A CD1   1 1 
ATOM   1331 N  N     . PRO A 1 166 ? 3.127   22.492  3.156   1 23.73  ? 166 PRO A N     1 1 
ATOM   1332 C  CA    . PRO A 1 166 ? 3.082   21.027  3.066   1 23.21  ? 166 PRO A CA    1 1 
ATOM   1333 C  C     . PRO A 1 166 ? 2.788   20.55   1.648   1 22.61  ? 166 PRO A C     1 1 
ATOM   1334 O  O     . PRO A 1 166 ? 3.335   19.534  1.239   1 22.64  ? 166 PRO A O     1 1 
ATOM   1335 C  CB    . PRO A 1 166 ? 1.939   20.656  4.009   1 24.05  ? 166 PRO A CB    1 1 
ATOM   1336 C  CG    . PRO A 1 166 ? 1.882   21.787  4.969   1 24.71  ? 166 PRO A CG    1 1 
ATOM   1337 C  CD    . PRO A 1 166 ? 2.142   22.986  4.132   1 23.12  ? 166 PRO A CD    1 1 
ATOM   1338 N  N     . TYR A 1 167 ? 1.973   21.307  0.881   1 22.02  ? 167 TYR A N     1 1 
ATOM   1339 C  CA    . TYR A 1 167 ? 1.655   20.924  -0.492  1 21.73  ? 167 TYR A CA    1 1 
ATOM   1340 C  C     . TYR A 1 167 ? 2.866   21      -1.413  1 21.49  ? 167 TYR A C     1 1 
ATOM   1341 O  O     . TYR A 1 167 ? 2.99    20.168  -2.31   1 21.75  ? 167 TYR A O     1 1 
ATOM   1342 C  CB    . TYR A 1 167 ? 0.455   21.694  -1.081  1 21.43  ? 167 TYR A CB    1 1 
ATOM   1343 C  CG    . TYR A 1 167 ? 0.045   21.099  -2.407  1 21.94  ? 167 TYR A CG    1 1 
ATOM   1344 C  CD1   . TYR A 1 167 ? -0.764  19.979  -2.464  1 22.85  ? 167 TYR A CD1   1 1 
ATOM   1345 C  CD2   . TYR A 1 167 ? 0.586   21.565  -3.597  1 22.93  ? 167 TYR A CD2   1 1 
ATOM   1346 C  CE1   . TYR A 1 167 ? -1.079  19.376  -3.676  1 23.77  ? 167 TYR A CE1   1 1 
ATOM   1347 C  CE2   . TYR A 1 167 ? 0.309   20.949  -4.809  1 23.73  ? 167 TYR A CE2   1 1 
ATOM   1348 C  CZ    . TYR A 1 167 ? -0.536  19.863  -4.848  1 24.53  ? 167 TYR A CZ    1 1 
ATOM   1349 O  OH    . TYR A 1 167 ? -0.804  19.273  -6.054  1 25.83  ? 167 TYR A OH    1 1 
ATOM   1350 N  N     . SER A 1 168 ? 3.785   21.943  -1.168  1 20.88  ? 168 SER A N     1 1 
ATOM   1351 C  CA    . SER A 1 168 ? 4.985   22.094  -1.993  1 20.6   ? 168 SER A CA    1 1 
ATOM   1352 C  C     . SER A 1 168 ? 5.817   20.824  -2.079  1 20.61  ? 168 SER A C     1 1 
ATOM   1353 O  O     . SER A 1 168 ? 6.418   20.564  -3.116  1 20.73  ? 168 SER A O     1 1 
ATOM   1354 C  CB    . SER A 1 168 ? 5.828   23.272  -1.526  1 21.29  ? 168 SER A CB    1 1 
ATOM   1355 O  OG    . SER A 1 168 ? 6.307   23.06   -0.211  1 23.12  ? 168 SER A OG    1 1 
ATOM   1356 N  N     . TYR A 1 169 ? 5.805   20.008  -1.024  1 20.55  ? 169 TYR A N     1 1 
ATOM   1357 C  CA    . TYR A 1 169 ? 6.542   18.75   -0.998  1 21.07  ? 169 TYR A CA    1 1 
ATOM   1358 C  C     . TYR A 1 169 ? 5.922   17.774  -1.987  1 21.04  ? 169 TYR A C     1 1 
ATOM   1359 O  O     . TYR A 1 169 ? 6.654   17.135  -2.743  1 21.36  ? 169 TYR A O     1 1 
ATOM   1360 C  CB    . TYR A 1 169 ? 6.597   18.173  0.431   1 21.51  ? 169 TYR A CB    1 1 
ATOM   1361 C  CG    . TYR A 1 169 ? 7.542   18.952  1.32    1 22.73  ? 169 TYR A CG    1 1 
ATOM   1362 C  CD1   . TYR A 1 169 ? 7.216   20.224  1.768   1 23.9   ? 169 TYR A CD1   1 1 
ATOM   1363 C  CD2   . TYR A 1 169 ? 8.786   18.448  1.656   1 24.11  ? 169 TYR A CD2   1 1 
ATOM   1364 C  CE1   . TYR A 1 169 ? 8.105   20.973  2.531   1 24.95  ? 169 TYR A CE1   1 1 
ATOM   1365 C  CE2   . TYR A 1 169 ? 9.682   19.183  2.425   1 25.29  ? 169 TYR A CE2   1 1 
ATOM   1366 C  CZ    . TYR A 1 169 ? 9.345   20.455  2.849   1 26.01  ? 169 TYR A CZ    1 1 
ATOM   1367 O  OH    . TYR A 1 169 ? 10.23   21.186  3.608   1 27.15  ? 169 TYR A OH    1 1 
ATOM   1368 N  N     . ILE A 1 170 ? 4.574   17.7    -2.026  1 20.39  ? 170 ILE A N     1 1 
ATOM   1369 C  CA    . ILE A 1 170 ? 3.85    16.835  -2.959  1 20.08  ? 170 ILE A CA    1 1 
ATOM   1370 C  C     . ILE A 1 170 ? 4.081   17.299  -4.388  1 20.4   ? 170 ILE A C     1 1 
ATOM   1371 O  O     . ILE A 1 170 ? 4.388   16.471  -5.235  1 20.87  ? 170 ILE A O     1 1 
ATOM   1372 C  CB    . ILE A 1 170 ? 2.34    16.78   -2.661  1 20.17  ? 170 ILE A CB    1 1 
ATOM   1373 C  CG1   . ILE A 1 170 ? 2.041   16.341  -1.237  1 20.87  ? 170 ILE A CG1   1 1 
ATOM   1374 C  CG2   . ILE A 1 170 ? 1.602   15.907  -3.667  1 20.56  ? 170 ILE A CG2   1 1 
ATOM   1375 C  CD1   . ILE A 1 170 ? 0.574   16.65   -0.847  1 21.56  ? 170 ILE A CD1   1 1 
ATOM   1376 N  N     . SER A 1 171 ? 3.983   18.61   -4.66   1 20.18  ? 171 SER A N     1 1 
ATOM   1377 C  CA    . SER A 1 171 ? 4.178   19.121  -6.016  1 20.96  ? 171 SER A CA    1 1 
ATOM   1378 C  C     . SER A 1 171 ? 5.579   18.922  -6.502  1 21.69  ? 171 SER A C     1 1 
ATOM   1379 O  O     . SER A 1 171 ? 5.769   18.617  -7.675  1 21.62  ? 171 SER A O     1 1 
ATOM   1380 C  CB    . SER A 1 171 ? 3.812   20.594  -6.107  1 22.79  ? 171 SER A CB    1 1 
ATOM   1381 O  OG    . SER A 1 171 ? 4.643   21.369  -5.261  1 25.35  ? 171 SER A OG    1 1 
ATOM   1382 N  N     . HIS A 1 172 ? 6.567   19.073  -5.608  1 22.46  ? 172 HIS A N     1 1 
ATOM   1383 C  CA    . HIS A 1 172 ? 7.963   18.842  -5.962  1 23.76  ? 172 HIS A CA    1 1 
ATOM   1384 C  C     . HIS A 1 172 ? 8.167   17.367  -6.299  1 24.42  ? 172 HIS A C     1 1 
ATOM   1385 O  O     . HIS A 1 172 ? 8.875   17.06   -7.247  1 24.61  ? 172 HIS A O     1 1 
ATOM   1386 C  CB    . HIS A 1 172 ? 8.91    19.29   -4.836  1 25.18  ? 172 HIS A CB    1 1 
ATOM   1387 C  CG    . HIS A 1 172 ? 10.312  19.591  -5.29   1 27.44  ? 172 HIS A CG    1 1 
ATOM   1388 N  ND1   . HIS A 1 172 ? 10.575  20.068  -6.561  1 29.22  ? 172 HIS A ND1   1 1 
ATOM   1389 C  CD2   . HIS A 1 172 ? 11.477  19.512  -4.606  1 28.62  ? 172 HIS A CD2   1 1 
ATOM   1390 C  CE1   . HIS A 1 172 ? 11.885  20.242  -6.619  1 29.92  ? 172 HIS A CE1   1 1 
ATOM   1391 N  NE2   . HIS A 1 172 ? 12.472  19.926  -5.466  1 29.89  ? 172 HIS A NE2   1 1 
ATOM   1392 N  N     . SER A 1 173 ? 7.502   16.459  -5.566  1 24.86  ? 173 SER A N     1 1 
ATOM   1393 C  CA    . SER A 1 173 ? 7.557   15.023  -5.828  1 25.61  ? 173 SER A CA    1 1 
ATOM   1394 C  C     . SER A 1 173 ? 7.041   14.716  -7.234  1 26.78  ? 173 SER A C     1 1 
ATOM   1395 O  O     . SER A 1 173 ? 7.689   13.972  -7.976  1 26.75  ? 173 SER A O     1 1 
ATOM   1396 C  CB    . SER A 1 173 ? 6.736   14.255  -4.795  1 25.86  ? 173 SER A CB    1 1 
ATOM   1397 O  OG    . SER A 1 173 ? 7.335   14.298  -3.514  1 26.9   ? 173 SER A OG    1 1 
ATOM   1398 N  N     . LYS A 1 174 ? 5.893   15.318  -7.606  1 27.47  ? 174 LYS A N     1 1 
ATOM   1399 C  CA    . LYS A 1 174 ? 5.299   15.125  -8.921  1 28.81  ? 174 LYS A CA    1 1 
ATOM   1400 C  C     . LYS A 1 174 ? 6.231   15.655  -10.002 1 30.1   ? 174 LYS A C     1 1 
ATOM   1401 O  O     . LYS A 1 174 ? 6.554   14.913  -10.926 1 30.63  ? 174 LYS A O     1 1 
ATOM   1402 C  CB    . LYS A 1 174 ? 3.897   15.773  -9.024  1 30.81  ? 174 LYS A CB    1 1 
ATOM   1403 C  CG    . LYS A 1 174 ? 2.853   15.239  -8.028  1 35.29  ? 174 LYS A CG    1 1 
ATOM   1404 C  CD    . LYS A 1 174 ? 2.65    13.705  -8.126  1 40.58  ? 174 LYS A CD    1 1 
ATOM   1405 C  CE    . LYS A 1 174 ? 1.927   13.089  -6.944  1 44.16  ? 174 LYS A CE    1 1 
ATOM   1406 N  NZ    . LYS A 1 174 ? 2.069   11.605  -6.919  1 46.23  ? 174 LYS A NZ    1 1 
ATOM   1407 N  N     . ASN A 1 175 ? 6.72    16.9    -9.86   1 30.49  ? 175 ASN A N     1 1 
ATOM   1408 C  CA    . ASN A 1 175 ? 7.606   17.515  -10.856 1 31.36  ? 175 ASN A CA    1 1 
ATOM   1409 C  C     . ASN A 1 175 ? 8.896   16.746  -11.106 1 31.87  ? 175 ASN A C     1 1 
ATOM   1410 O  O     . ASN A 1 175 ? 9.287   16.535  -12.256 1 32.25  ? 175 ASN A O     1 1 
ATOM   1411 C  CB    . ASN A 1 175 ? 7.954   18.959  -10.472 1 32.6   ? 175 ASN A CB    1 1 
ATOM   1412 C  CG    . ASN A 1 175 ? 6.788   19.877  -10.491 1 36.66  ? 175 ASN A CG    1 1 
ATOM   1413 O  OD1   . ASN A 1 175 ? 5.783   19.62   -11.164 1 38.42  ? 175 ASN A OD1   1 1 
ATOM   1414 N  ND2   . ASN A 1 175 ? 6.89    20.961  -9.736  1 37.7   ? 175 ASN A ND2   1 1 
ATOM   1415 N  N     . THR A 1 176 ? 9.56    16.341  -10.027 1 31.56  ? 176 THR A N     1 1 
ATOM   1416 C  CA    . THR A 1 176 ? 10.861  15.703  -10.098 1 31.34  ? 176 THR A CA    1 1 
ATOM   1417 C  C     . THR A 1 176 ? 10.85   14.208  -10.291 1 31.76  ? 176 THR A C     1 1 
ATOM   1418 O  O     . THR A 1 176 ? 11.911  13.642  -10.559 1 32.35  ? 176 THR A O     1 1 
ATOM   1419 C  CB    . THR A 1 176 ? 11.618  16.001  -8.814  1 31.56  ? 176 THR A CB    1 1 
ATOM   1420 O  OG1   . THR A 1 176 ? 10.916  15.41   -7.72   1 32.18  ? 176 THR A OG1   1 1 
ATOM   1421 C  CG2   . THR A 1 176 ? 11.782  17.482  -8.576  1 31.66  ? 176 THR A CG2   1 1 
ATOM   1422 N  N     . GLY A 1 177 ? 9.712   13.56   -10.054 1 31.12  ? 177 GLY A N     1 1 
ATOM   1423 C  CA    . GLY A 1 177 ? 9.665   12.103  -10.089 1 30.9   ? 177 GLY A CA    1 1 
ATOM   1424 C  C     . GLY A 1 177 ? 10.382  11.469  -8.903  1 30.44  ? 177 GLY A C     1 1 
ATOM   1425 O  O     . GLY A 1 177 ? 10.598  10.259  -8.883  1 30.41  ? 177 GLY A O     1 1 
ATOM   1426 N  N     . ASN A 1 178 ? 10.756  12.286  -7.903  1 30.15  ? 178 ASN A N     1 1 
ATOM   1427 C  CA    . ASN A 1 178 ? 11.455  11.894  -6.689  1 30.4   ? 178 ASN A CA    1 1 
ATOM   1428 C  C     . ASN A 1 178 ? 10.489  11.886  -5.495  1 29.85  ? 178 ASN A C     1 1 
ATOM   1429 O  O     . ASN A 1 178 ? 9.408   12.462  -5.563  1 30.2   ? 178 ASN A O     1 1 
ATOM   1430 C  CB    . ASN A 1 178 ? 12.618  12.87   -6.434  1 32.18  ? 178 ASN A CB    1 1 
ATOM   1431 C  CG    . ASN A 1 178 ? 13.603  12.427  -5.377  1 36.38  ? 178 ASN A CG    1 1 
ATOM   1432 O  OD1   . ASN A 1 178 ? 13.673  11.251  -4.993  1 38.29  ? 178 ASN A OD1   1 1 
ATOM   1433 N  ND2   . ASN A 1 178 ? 14.393  13.357  -4.882  1 36.57  ? 178 ASN A ND2   1 1 
ATOM   1434 N  N     . PHE A 1 179 ? 10.875  11.227  -4.405  1 28.87  ? 179 PHE A N     1 1 
ATOM   1435 C  CA    . PHE A 1 179 ? 10.068  11.15   -3.203  1 28.34  ? 179 PHE A CA    1 1 
ATOM   1436 C  C     . PHE A 1 179 ? 10.495  12.204  -2.203  1 27.83  ? 179 PHE A C     1 1 
ATOM   1437 O  O     . PHE A 1 179 ? 11.502  12.04   -1.519  1 27.73  ? 179 PHE A O     1 1 
ATOM   1438 C  CB    . PHE A 1 179 ? 10.201  9.768   -2.579  1 28.24  ? 179 PHE A CB    1 1 
ATOM   1439 C  CG    . PHE A 1 179 ? 9.291   9.546   -1.406  1 28.82  ? 179 PHE A CG    1 1 
ATOM   1440 C  CD1   . PHE A 1 179 ? 7.931   9.757   -1.517  1 29.8   ? 179 PHE A CD1   1 1 
ATOM   1441 C  CD2   . PHE A 1 179 ? 9.784   9.065   -0.214  1 29.55  ? 179 PHE A CD2   1 1 
ATOM   1442 C  CE1   . PHE A 1 179 ? 7.086   9.525   -0.442  1 30.55  ? 179 PHE A CE1   1 1 
ATOM   1443 C  CE2   . PHE A 1 179 ? 8.937   8.815   0.851   1 30.39  ? 179 PHE A CE2   1 1 
ATOM   1444 C  CZ    . PHE A 1 179 ? 7.592   9.043   0.731   1 30.31  ? 179 PHE A CZ    1 1 
ATOM   1445 N  N     . ILE A 1 180 ? 9.742   13.307  -2.146  1 27.23  ? 180 ILE A N     1 1 
ATOM   1446 C  CA    . ILE A 1 180 ? 9.963   14.419  -1.225  1 26.7   ? 180 ILE A CA    1 1 
ATOM   1447 C  C     . ILE A 1 180 ? 8.675   14.534  -0.431  1 26.46  ? 180 ILE A C     1 1 
ATOM   1448 O  O     . ILE A 1 180 ? 7.614   14.76   -1.02   1 26.31  ? 180 ILE A O     1 1 
ATOM   1449 C  CB    . ILE A 1 180 ? 10.26   15.713  -1.998  1 26.68  ? 180 ILE A CB    1 1 
ATOM   1450 C  CG1   . ILE A 1 180 ? 11.429  15.521  -2.952  1 27.43  ? 180 ILE A CG1   1 1 
ATOM   1451 C  CG2   . ILE A 1 180 ? 10.526  16.845  -1.046  1 26.96  ? 180 ILE A CG2   1 1 
ATOM   1452 C  CD1   . ILE A 1 180 ? 11.062  15.646  -4.366  1 28.55  ? 180 ILE A CD1   1 1 
ATOM   1453 N  N     . VAL A 1 181 ? 8.744   14.308  0.884   1 26.3   ? 181 VAL A N     1 1 
ATOM   1454 C  CA    . VAL A 1 181 ? 7.542   14.297  1.693   1 26.85  ? 181 VAL A CA    1 1 
ATOM   1455 C  C     . VAL A 1 181 ? 7.733   14.903  3.06    1 27.25  ? 181 VAL A C     1 1 
ATOM   1456 O  O     . VAL A 1 181 ? 8.824   14.889  3.631   1 26.84  ? 181 VAL A O     1 1 
ATOM   1457 C  CB    . VAL A 1 181 ? 7.039   12.84   1.81    1 27.75  ? 181 VAL A CB    1 1 
ATOM   1458 C  CG1   . VAL A 1 181 ? 7.954   12.026  2.722   1 28.41  ? 181 VAL A CG1   1 1 
ATOM   1459 C  CG2   . VAL A 1 181 ? 5.58    12.766  2.271   1 28.2   ? 181 VAL A CG2   1 1 
ATOM   1460 N  N     . GLN A 1 182 ? 6.644   15.427  3.591   1 27.85  ? 182 GLN A N     1 1 
ATOM   1461 C  CA    . GLN A 1 182 ? 6.606   15.938  4.936   1 28.9   ? 182 GLN A CA    1 1 
ATOM   1462 C  C     . GLN A 1 182 ? 5.823   14.896  5.743   1 29.57  ? 182 GLN A C     1 1 
ATOM   1463 O  O     . GLN A 1 182 ? 4.716   14.514  5.367   1 29.77  ? 182 GLN A O     1 1 
ATOM   1464 C  CB    . GLN A 1 182 ? 5.91    17.289  4.963   1 30.84  ? 182 GLN A CB    1 1 
ATOM   1465 C  CG    . GLN A 1 182 ? 6.33    18.124  6.141   1 35.55  ? 182 GLN A CG    1 1 
ATOM   1466 C  CD    . GLN A 1 182 ? 5.817   19.519  5.949   1 41.49  ? 182 GLN A CD    1 1 
ATOM   1467 O  OE1   . GLN A 1 182 ? 4.622   19.743  5.754   1 43.18  ? 182 GLN A OE1   1 1 
ATOM   1468 N  NE2   . GLN A 1 182 ? 6.7     20.491  5.972   1 42.54  ? 182 GLN A NE2   1 1 
ATOM   1469 N  N     . ALA A 1 183 ? 6.442   14.362  6.787   1 29.69  ? 183 ALA A N     1 1 
ATOM   1470 C  CA    . ALA A 1 183 ? 5.843   13.346  7.641   1 30.21  ? 183 ALA A CA    1 1 
ATOM   1471 C  C     . ALA A 1 183 ? 5.673   13.923  9.029   1 30.48  ? 183 ALA A C     1 1 
ATOM   1472 O  O     . ALA A 1 183 ? 6.552   14.633  9.519   1 30.21  ? 183 ALA A O     1 1 
ATOM   1473 C  CB    . ALA A 1 183 ? 6.733   12.116  7.695   1 30.42  ? 183 ALA A CB    1 1 
ATOM   1474 N  N     . TYR A 1 184 ? 4.542   13.618  9.669   1 30.76  ? 184 TYR A N     1 1 
ATOM   1475 C  CA    . TYR A 1 184 ? 4.246   14.186  10.979  1 31.3   ? 184 TYR A CA    1 1 
ATOM   1476 C  C     . TYR A 1 184 ? 4.257   13.144  12.054  1 31.71  ? 184 TYR A C     1 1 
ATOM   1477 O  O     . TYR A 1 184 ? 3.636   12.102  11.926  1 31.58  ? 184 TYR A O     1 1 
ATOM   1478 C  CB    . TYR A 1 184 ? 2.935   15.006  10.971  1 31.18  ? 184 TYR A CB    1 1 
ATOM   1479 C  CG    . TYR A 1 184 ? 2.838   15.891  9.749   1 32     ? 184 TYR A CG    1 1 
ATOM   1480 C  CD1   . TYR A 1 184 ? 3.41    17.154  9.736   1 32.76  ? 184 TYR A CD1   1 1 
ATOM   1481 C  CD2   . TYR A 1 184 ? 2.324   15.403  8.558   1 33.17  ? 184 TYR A CD2   1 1 
ATOM   1482 C  CE1   . TYR A 1 184 ? 3.425   17.929  8.585   1 33.67  ? 184 TYR A CE1   1 1 
ATOM   1483 C  CE2   . TYR A 1 184 ? 2.324   16.17   7.404   1 34.14  ? 184 TYR A CE2   1 1 
ATOM   1484 C  CZ    . TYR A 1 184 ? 2.871   17.435  7.422   1 34.91  ? 184 TYR A CZ    1 1 
ATOM   1485 O  OH    . TYR A 1 184 ? 2.85    18.192  6.28    1 36.65  ? 184 TYR A OH    1 1 
ATOM   1486 N  N     . PHE A 1 185 ? 5.023   13.404  13.086  1 32.21  ? 185 PHE A N     1 1 
ATOM   1487 C  CA    . PHE A 1 185 ? 5.115   12.515  14.218  1 33.39  ? 185 PHE A CA    1 1 
ATOM   1488 C  C     . PHE A 1 185 ? 4.339   13.155  15.348  1 34.23  ? 185 PHE A C     1 1 
ATOM   1489 O  O     . PHE A 1 185 ? 4.362   14.377  15.507  1 34.35  ? 185 PHE A O     1 1 
ATOM   1490 C  CB    . PHE A 1 185 ? 6.584   12.307  14.617  1 33.69  ? 185 PHE A CB    1 1 
ATOM   1491 C  CG    . PHE A 1 185 ? 7.359   11.284  13.809  1 34.69  ? 185 PHE A CG    1 1 
ATOM   1492 C  CD1   . PHE A 1 185 ? 6.902   10.853  12.573  1 35.5   ? 185 PHE A CD1   1 1 
ATOM   1493 C  CD2   . PHE A 1 185 ? 8.553   10.767  14.278  1 35.62  ? 185 PHE A CD2   1 1 
ATOM   1494 C  CE1   . PHE A 1 185 ? 7.625   9.928   11.83   1 36.08  ? 185 PHE A CE1   1 1 
ATOM   1495 C  CE2   . PHE A 1 185 ? 9.266   9.833   13.536  1 36.25  ? 185 PHE A CE2   1 1 
ATOM   1496 C  CZ    . PHE A 1 185 ? 8.798   9.42    12.318  1 35.91  ? 185 PHE A CZ    1 1 
ATOM   1497 N  N     . ARG A 1 186 ? 3.632   12.337  16.119  1 34.67  ? 186 ARG A N     1 1 
ATOM   1498 C  CA    . ARG A 1 186 ? 2.853   12.803  17.248  1 35.5   ? 186 ARG A CA    1 1 
ATOM   1499 C  C     . ARG A 1 186 ? 3.758   13.352  18.338  1 36.86  ? 186 ARG A C     1 1 
ATOM   1500 O  O     . ARG A 1 186 ? 4.484   12.602  18.992  1 37     ? 186 ARG A O     1 1 
ATOM   1501 C  CB    . ARG A 1 186 ? 1.96    11.683  17.789  1 35.94  ? 186 ARG A CB    1 1 
ATOM   1502 C  CG    . ARG A 1 186 ? 1.155   12.105  18.998  1 38.18  ? 186 ARG A CG    1 1 
ATOM   1503 C  CD    . ARG A 1 186 ? 0.691   10.911  19.786  1 40.92  ? 186 ARG A CD    1 1 
ATOM   1504 N  NE    . ARG A 1 186 ? -0.514  10.307  19.219  1 43.45  ? 186 ARG A NE    1 1 
ATOM   1505 C  CZ    . ARG A 1 186 ? -1.748  10.546  19.656  1 45.34  ? 186 ARG A CZ    1 1 
ATOM   1506 N  NH1   . ARG A 1 186 ? -1.954  11.399  20.655  1 44.44  ? 186 ARG A NH1   1 1 
ATOM   1507 N  NH2   . ARG A 1 186 ? -2.785  9.944   19.091  1 45.35  ? 186 ARG A NH2   1 1 
ATOM   1508 N  N     . GLY A 1 187 ? 3.715   14.663  18.502  1 37.63  ? 187 GLY A N     1 1 
ATOM   1509 C  CA    . GLY A 1 187 ? 4.477   15.34   19.535  1 38.89  ? 187 GLY A CA    1 1 
ATOM   1510 C  C     . GLY A 1 187 ? 3.85    15.1    20.891  1 39.98  ? 187 GLY A C     1 1 
ATOM   1511 O  O     . GLY A 1 187 ? 2.663   14.776  20.993  1 40.05  ? 187 GLY A O     1 1 
ATOM   1512 N  N     . GLU A 1 188 ? 4.644   15.251  21.944  1 40.78  ? 188 GLU A N     1 1 
ATOM   1513 C  CA    . GLU A 1 188 ? 4.153   15.072  23.303  1 42.09  ? 188 GLU A CA    1 1 
ATOM   1514 C  C     . GLU A 1 188 ? 3.08    16.117  23.631  1 43.07  ? 188 GLU A C     1 1 
ATOM   1515 O  O     . GLU A 1 188 ? 2.138   15.805  24.362  1 43.43  ? 188 GLU A O     1 1 
ATOM   1516 C  CB    . GLU A 1 188 ? 5.307   15.156  24.31   1 44.91  ? 188 GLU A CB    1 1 
ATOM   1517 C  CG    . GLU A 1 188 ? 6.435   14.171  24.044  1 50.78  ? 188 GLU A CG    1 1 
ATOM   1518 C  CD    . GLU A 1 188 ? 7.628   14.748  23.306  1 57.29  ? 188 GLU A CD    1 1 
ATOM   1519 O  OE1   . GLU A 1 188 ? 7.415   15.589  22.402  1 58.37  ? 188 GLU A OE1   1 1 
ATOM   1520 O  OE2   . GLU A 1 188 ? 8.775   14.356  23.627  1 59.38  ? 188 GLU A OE2   1 1 
ATOM   1521 N  N     . GLU A 1 189 ? 3.181   17.336  23.048  1 43.15  ? 189 GLU A N     1 1 
ATOM   1522 C  CA    . GLU A 1 189 ? 2.186   18.374  23.295  1 43.54  ? 189 GLU A CA    1 1 
ATOM   1523 C  C     . GLU A 1 189 ? 0.962   18.314  22.364  1 44.46  ? 189 GLU A C     1 1 
ATOM   1524 O  O     . GLU A 1 189 ? 0.165   19.253  22.359  1 44.78  ? 189 GLU A O     1 1 
ATOM   1525 C  CB    . GLU A 1 189 ? 2.816   19.759  23.301  1 44.43  ? 189 GLU A CB    1 1 
ATOM   1526 C  CG    . GLU A 1 189 ? 3.374   20.087  24.668  1 46.67  ? 189 GLU A CG    1 1 
ATOM   1527 C  CD    . GLU A 1 189 ? 4.051   21.433  24.758  1 50.46  ? 189 GLU A CD    1 1 
ATOM   1528 O  OE1   . GLU A 1 189 ? 4.579   21.904  23.726  1 50.99  ? 189 GLU A OE1   1 1 
ATOM   1529 O  OE2   . GLU A 1 189 ? 4.068   22.015  25.865  1 51.99  ? 189 GLU A OE2   1 1 
ATOM   1530 N  N     . TYR A 1 190 ? 0.768   17.2    21.63   1 44.83  ? 190 TYR A N     1 1 
ATOM   1531 C  CA    . TYR A 1 190 ? -0.441  17.028  20.823  1 45.59  ? 190 TYR A CA    1 1 
ATOM   1532 C  C     . TYR A 1 190 ? -1.519  16.623  21.822  1 46.65  ? 190 TYR A C     1 1 
ATOM   1533 O  O     . TYR A 1 190 ? -1.54   15.482  22.283  1 46.87  ? 190 TYR A O     1 1 
ATOM   1534 C  CB    . TYR A 1 190 ? -0.273  15.942  19.73   1 45.35  ? 190 TYR A CB    1 1 
ATOM   1535 C  CG    . TYR A 1 190 ? -1.572  15.586  19.035  1 45.82  ? 190 TYR A CG    1 1 
ATOM   1536 C  CD1   . TYR A 1 190 ? -2.199  16.486  18.187  1 46.65  ? 190 TYR A CD1   1 1 
ATOM   1537 C  CD2   . TYR A 1 190 ? -2.186  14.361  19.248  1 46.64  ? 190 TYR A CD2   1 1 
ATOM   1538 C  CE1   . TYR A 1 190 ? -3.41   16.181  17.576  1 47.39  ? 190 TYR A CE1   1 1 
ATOM   1539 C  CE2   . TYR A 1 190 ? -3.391  14.041  18.635  1 47.49  ? 190 TYR A CE2   1 1 
ATOM   1540 C  CZ    . TYR A 1 190 ? -4.003  14.956  17.801  1 48.26  ? 190 TYR A CZ    1 1 
ATOM   1541 O  OH    . TYR A 1 190 ? -5.204  14.663  17.2    1 49.66  ? 190 TYR A OH    1 1 
ATOM   1542 N  N     . GLN A 1 191 ? -2.361  17.573  22.217  1 47.13  ? 191 GLN A N     1 1 
ATOM   1543 C  CA    . GLN A 1 191 ? -3.412  17.31   23.192  1 48.06  ? 191 GLN A CA    1 1 
ATOM   1544 C  C     . GLN A 1 191 ? -4.742  17.82   22.641  1 48.6   ? 191 GLN A C     1 1 
ATOM   1545 O  O     . GLN A 1 191 ? -5.142  18.944  22.938  1 48.75  ? 191 GLN A O     1 1 
ATOM   1546 C  CB    . GLN A 1 191 ? -3.058  18.022  24.504  1 49.86  ? 191 GLN A CB    1 1 
ATOM   1547 C  CG    . GLN A 1 191 ? -3.182  17.16   25.747  1 53.04  ? 191 GLN A CG    1 1 
ATOM   1548 C  CD    . GLN A 1 191 ? -2.274  15.974  25.681  1 56.9   ? 191 GLN A CD    1 1 
ATOM   1549 O  OE1   . GLN A 1 191 ? -1.071  16.096  25.449  1 57.53  ? 191 GLN A OE1   1 1 
ATOM   1550 N  NE2   . GLN A 1 191 ? -2.845  14.796  25.859  1 58.26  ? 191 GLN A NE2   1 1 
ATOM   1551 N  N     . PRO A 1 192 ? -5.425  17.014  21.804  1 48.77  ? 192 PRO A N     1 1 
ATOM   1552 C  CA    . PRO A 1 192 ? -6.67   17.486  21.174  1 48.86  ? 192 PRO A CA    1 1 
ATOM   1553 C  C     . PRO A 1 192 ? -7.846  17.703  22.117  1 49.24  ? 192 PRO A C     1 1 
ATOM   1554 O  O     . PRO A 1 192 ? -8.727  18.498  21.791  1 49.65  ? 192 PRO A O     1 1 
ATOM   1555 C  CB    . PRO A 1 192 ? -6.969  16.419  20.12   1 49.53  ? 192 PRO A CB    1 1 
ATOM   1556 C  CG    . PRO A 1 192 ? -6.296  15.192  20.628  1 50.05  ? 192 PRO A CG    1 1 
ATOM   1557 C  CD    . PRO A 1 192 ? -5.058  15.663  21.34   1 48.5   ? 192 PRO A CD    1 1 
ATOM   1558 N  N     . LYS A 1 193 ? -7.866  17.019  23.281  1 48.83  ? 193 LYS A N     1 1 
ATOM   1559 C  CA    . LYS A 1 193 ? -8.93   17.205  24.275  1 48.62  ? 193 LYS A CA    1 1 
ATOM   1560 C  C     . LYS A 1 193 ? -8.888  18.621  24.893  1 48.5   ? 193 LYS A C     1 1 
ATOM   1561 O  O     . LYS A 1 193 ? -9.896  19.073  25.432  1 48.81  ? 193 LYS A O     1 1 
ATOM   1562 C  CB    . LYS A 1 193 ? -8.795  16.18   25.413  1 49.96  ? 193 LYS A CB    1 1 
ATOM   1563 C  CG    . LYS A 1 193 ? -8.794  14.728  24.976  1 53.79  ? 193 LYS A CG    1 1 
ATOM   1564 C  CD    . LYS A 1 193 ? -8.825  13.789  26.192  1 57.9   ? 193 LYS A CD    1 1 
ATOM   1565 C  CE    . LYS A 1 193 ? -9.468  12.452  25.889  1 61.2   ? 193 LYS A CE    1 1 
ATOM   1566 N  NZ    . LYS A 1 193 ? -9.564  11.587  27.096  1 63.09  ? 193 LYS A NZ    1 1 
ATOM   1567 N  N     . TYR A 1 194 ? -7.729  19.308  24.833  1 47.8   ? 194 TYR A N     1 1 
ATOM   1568 C  CA    . TYR A 1 194 ? -7.562  20.615  25.439  1 47.83  ? 194 TYR A CA    1 1 
ATOM   1569 C  C     . TYR A 1 194 ? -7.374  21.757  24.453  1 47.38  ? 194 TYR A C     1 1 
ATOM   1570 O  O     . TYR A 1 194 ? -7.473  22.912  24.87   1 47.76  ? 194 TYR A O     1 1 
ATOM   1571 C  CB    . TYR A 1 194 ? -6.415  20.585  26.45   1 48.24  ? 194 TYR A CB    1 1 
ATOM   1572 C  CG    . TYR A 1 194 ? -6.67   19.59   27.554  1 49.5   ? 194 TYR A CG    1 1 
ATOM   1573 C  CD1   . TYR A 1 194 ? -7.586  19.858  28.559  1 50.7   ? 194 TYR A CD1   1 1 
ATOM   1574 C  CD2   . TYR A 1 194 ? -6.055  18.348  27.55   1 50.72  ? 194 TYR A CD2   1 1 
ATOM   1575 C  CE1   . TYR A 1 194 ? -7.855  18.932  29.558  1 51.94  ? 194 TYR A CE1   1 1 
ATOM   1576 C  CE2   . TYR A 1 194 ? -6.305  17.416  28.55   1 52.01  ? 194 TYR A CE2   1 1 
ATOM   1577 C  CZ    . TYR A 1 194 ? -7.219  17.706  29.547  1 53.21  ? 194 TYR A CZ    1 1 
ATOM   1578 O  OH    . TYR A 1 194 ? -7.507  16.778  30.525  1 55.15  ? 194 TYR A OH    1 1 
ATOM   1579 N  N     . ASP A 1 195 ? -7.086  21.466  23.17   1 46.41  ? 195 ASP A N     1 1 
ATOM   1580 C  CA    . ASP A 1 195 ? -6.942  22.542  22.186  1 46.05  ? 195 ASP A CA    1 1 
ATOM   1581 C  C     . ASP A 1 195 ? -7.97   22.416  21.081  1 45.69  ? 195 ASP A C     1 1 
ATOM   1582 O  O     . ASP A 1 195 ? -7.982  21.437  20.339  1 46.09  ? 195 ASP A O     1 1 
ATOM   1583 C  CB    . ASP A 1 195 ? -5.528  22.653  21.617  1 47.28  ? 195 ASP A CB    1 1 
ATOM   1584 C  CG    . ASP A 1 195 ? -5.206  24.024  21.028  1 50.94  ? 195 ASP A CG    1 1 
ATOM   1585 O  OD1   . ASP A 1 195 ? -6.087  24.614  20.379  1 51.04  ? 195 ASP A OD1   1 1 
ATOM   1586 O  OD2   . ASP A 1 195 ? -4.063  24.495  21.208  1 53.29  ? 195 ASP A OD2   1 1 
ATOM   1587 N  N     . LYS A 1 196 ? -8.81   23.442  20.964  1 44.67  ? 196 LYS A N     1 1 
ATOM   1588 C  CA    . LYS A 1 196 ? -9.892  23.538  19.996  1 44.15  ? 196 LYS A CA    1 1 
ATOM   1589 C  C     . LYS A 1 196 ? -9.39   23.615  18.546  1 43.22  ? 196 LYS A C     1 1 
ATOM   1590 O  O     . LYS A 1 196 ? -10.12  23.235  17.635  1 43.5   ? 196 LYS A O     1 1 
ATOM   1591 C  CB    . LYS A 1 196 ? -10.789 24.739  20.346  1 46.15  ? 196 LYS A CB    1 1 
ATOM   1592 C  CG    . LYS A 1 196 ? -11.079 24.879  21.852  1 50.69  ? 196 LYS A CG    1 1 
ATOM   1593 C  CD    . LYS A 1 196 ? -11.842 23.672  22.432  1 55.51  ? 196 LYS A CD    1 1 
ATOM   1594 C  CE    . LYS A 1 196 ? -11.174 23.054  23.645  1 59.02  ? 196 LYS A CE    1 1 
ATOM   1595 N  NZ    . LYS A 1 196 ? -11.67  21.668  23.907  1 60.94  ? 196 LYS A NZ    1 1 
ATOM   1596 N  N     . LYS A 1 197 ? -8.144  24.078  18.33   1 41.96  ? 197 LYS A N     1 1 
ATOM   1597 C  CA    . LYS A 1 197 ? -7.559  24.171  16.99   1 41.23  ? 197 LYS A CA    1 1 
ATOM   1598 C  C     . LYS A 1 197 ? -7.332  22.802  16.36   1 40.16  ? 197 LYS A C     1 1 
ATOM   1599 O  O     . LYS A 1 197 ? -7.381  22.684  15.139  1 40.24  ? 197 LYS A O     1 1 
ATOM   1600 C  CB    . LYS A 1 197 ? -6.253  24.994  17.003  1 43.09  ? 197 LYS A CB    1 1 
ATOM   1601 C  CG    . LYS A 1 197 ? -6.487  26.497  17.194  1 47.47  ? 197 LYS A CG    1 1 
ATOM   1602 C  CD    . LYS A 1 197 ? -5.202  27.321  17.253  1 52.29  ? 197 LYS A CD    1 1 
ATOM   1603 C  CE    . LYS A 1 197 ? -5.458  28.737  17.732  1 56.25  ? 197 LYS A CE    1 1 
ATOM   1604 N  NZ    . LYS A 1 197 ? -4.622  29.751  17.023  1 58.81  ? 197 LYS A NZ    1 1 
ATOM   1605 N  N     . LEU A 1 198 ? -7.111  21.768  17.189  1 39.1   ? 198 LEU A N     1 1 
ATOM   1606 C  CA    . LEU A 1 198 ? -6.877  20.389  16.758  1 38.53  ? 198 LEU A CA    1 1 
ATOM   1607 C  C     . LEU A 1 198 ? -8.16   19.533  16.71   1 38.54  ? 198 LEU A C     1 1 
ATOM   1608 O  O     . LEU A 1 198 ? -8.059  18.315  16.529  1 38.98  ? 198 LEU A O     1 1 
ATOM   1609 C  CB    . LEU A 1 198 ? -5.898  19.714  17.713  1 38.12  ? 198 LEU A CB    1 1 
ATOM   1610 C  CG    . LEU A 1 198 ? -4.595  20.421  17.937  1 38.91  ? 198 LEU A CG    1 1 
ATOM   1611 C  CD1   . LEU A 1 198 ? -3.838  19.793  19.075  1 39.28  ? 198 LEU A CD1   1 1 
ATOM   1612 C  CD2   . LEU A 1 198 ? -3.771  20.43   16.684  1 39.46  ? 198 LEU A CD2   1 1 
ATOM   1613 N  N     . LYS A 1 199 ? -9.354  20.14   16.876  1 37.69  ? 199 LYS A N     1 1 
ATOM   1614 C  CA    . LYS A 1 199 ? -10.614 19.392  16.858  1 37.48  ? 199 LYS A CA    1 1 
ATOM   1615 C  C     . LYS A 1 199 ? -10.792 18.623  15.556  1 37.58  ? 199 LYS A C     1 1 
ATOM   1616 O  O     . LYS A 1 199 ? -11.255 17.485  15.58   1 37.91  ? 199 LYS A O     1 1 
ATOM   1617 C  CB    . LYS A 1 199 ? -11.823 20.323  17.098  1 38.32  ? 199 LYS A CB    1 1 
ATOM   1618 C  CG    . LYS A 1 199 ? -13.156 19.602  17.241  1 40.68  ? 199 LYS A CG    1 1 
ATOM   1619 C  CD    . LYS A 1 199 ? -14.314 20.585  17.341  1 44.65  ? 199 LYS A CD    1 1 
ATOM   1620 C  CE    . LYS A 1 199 ? -15.678 19.935  17.228  1 47.9   ? 199 LYS A CE    1 1 
ATOM   1621 N  NZ    . LYS A 1 199 ? -16.752 20.922  16.9    1 49.52  ? 199 LYS A NZ    1 1 
ATOM   1622 N  N     . PHE A 1 200 ? -10.353 19.207  14.438  1 37.24  ? 200 PHE A N     1 1 
ATOM   1623 C  CA    . PHE A 1 200 ? -10.51  18.556  13.152  1 37.67  ? 200 PHE A CA    1 1 
ATOM   1624 C  C     . PHE A 1 200 ? -9.234  17.973  12.597  1 37.88  ? 200 PHE A C     1 1 
ATOM   1625 O  O     . PHE A 1 200 ? -9.11   17.843  11.382  1 38.25  ? 200 PHE A O     1 1 
ATOM   1626 C  CB    . PHE A 1 200 ? -11.178 19.485  12.149  1 37.77  ? 200 PHE A CB    1 1 
ATOM   1627 C  CG    . PHE A 1 200 ? -12.516 19.954  12.651  1 38.59  ? 200 PHE A CG    1 1 
ATOM   1628 C  CD1   . PHE A 1 200 ? -13.566 19.062  12.807  1 39.58  ? 200 PHE A CD1   1 1 
ATOM   1629 C  CD2   . PHE A 1 200 ? -12.703 21.266  13.043  1 39.49  ? 200 PHE A CD2   1 1 
ATOM   1630 C  CE1   . PHE A 1 200 ? -14.796 19.487  13.297  1 40.37  ? 200 PHE A CE1   1 1 
ATOM   1631 C  CE2   . PHE A 1 200 ? -13.929 21.69   13.543  1 40.44  ? 200 PHE A CE2   1 1 
ATOM   1632 C  CZ    . PHE A 1 200 ? -14.97  20.797  13.664  1 40.36  ? 200 PHE A CZ    1 1 
ATOM   1633 N  N     . PHE A 1 201 ? -8.31   17.554  13.473  1 37.47  ? 201 PHE A N     1 1 
ATOM   1634 C  CA    . PHE A 1 201 ? -7.095  16.898  13.016  1 37.36  ? 201 PHE A CA    1 1 
ATOM   1635 C  C     . PHE A 1 201 ? -7.342  15.395  12.907  1 37.36  ? 201 PHE A C     1 1 
ATOM   1636 O  O     . PHE A 1 201 ? -7.851  14.778  13.848  1 37.55  ? 201 PHE A O     1 1 
ATOM   1637 C  CB    . PHE A 1 201 ? -5.914  17.16   13.953  1 37.18  ? 201 PHE A CB    1 1 
ATOM   1638 C  CG    . PHE A 1 201 ? -4.623  16.6    13.402  1 37.58  ? 201 PHE A CG    1 1 
ATOM   1639 C  CD1   . PHE A 1 201 ? -4.034  17.152  12.279  1 38.29  ? 201 PHE A CD1   1 1 
ATOM   1640 C  CD2   . PHE A 1 201 ? -4.022  15.5    13.983  1 38.32  ? 201 PHE A CD2   1 1 
ATOM   1641 C  CE1   . PHE A 1 201 ? -2.848  16.636  11.772  1 39.07  ? 201 PHE A CE1   1 1 
ATOM   1642 C  CE2   . PHE A 1 201 ? -2.842  14.979  13.463  1 39.08  ? 201 PHE A CE2   1 1 
ATOM   1643 C  CZ    . PHE A 1 201 ? -2.256  15.558  12.37   1 38.81  ? 201 PHE A CZ    1 1 
ATOM   1644 N  N     . ASP A 1 202 ? -6.983  14.807  11.758  1 36.88  ? 202 ASP A N     1 1 
ATOM   1645 C  CA    . ASP A 1 202 ? -7.123  13.374  11.515  1 36.65  ? 202 ASP A CA    1 1 
ATOM   1646 C  C     . ASP A 1 202 ? -5.855  12.704  12.024  1 35.95  ? 202 ASP A C     1 1 
ATOM   1647 O  O     . ASP A 1 202 ? -4.793  12.924  11.451  1 35.97  ? 202 ASP A O     1 1 
ATOM   1648 C  CB    . ASP A 1 202 ? -7.261  13.118  10.007  1 38.4   ? 202 ASP A CB    1 1 
ATOM   1649 C  CG    . ASP A 1 202 ? -7.63   11.697  9.628   1 42.97  ? 202 ASP A CG    1 1 
ATOM   1650 O  OD1   . ASP A 1 202 ? -7.679  10.829  10.532  1 43.34  ? 202 ASP A OD1   1 1 
ATOM   1651 O  OD2   . ASP A 1 202 ? -7.86   11.445  8.422   1 45.48  ? 202 ASP A OD2   1 1 
ATOM   1652 N  N     . GLU A 1 203 ? -5.956  11.884  13.081  1 35.11  ? 203 GLU A N     1 1 
ATOM   1653 C  CA    . GLU A 1 203 ? -4.778  11.219  13.633  1 34.81  ? 203 GLU A CA    1 1 
ATOM   1654 C  C     . GLU A 1 203 ? -4.136  10.208  12.695  1 34.37  ? 203 GLU A C     1 1 
ATOM   1655 O  O     . GLU A 1 203 ? -3.007  9.801   12.954  1 34.34  ? 203 GLU A O     1 1 
ATOM   1656 C  CB    . GLU A 1 203 ? -5.063  10.599  14.991  1 36.71  ? 203 GLU A CB    1 1 
ATOM   1657 C  CG    . GLU A 1 203 ? -5.211  11.665  16.047  1 41.16  ? 203 GLU A CG    1 1 
ATOM   1658 C  CD    . GLU A 1 203 ? -5.605  11.172  17.42   1 47.73  ? 203 GLU A CD    1 1 
ATOM   1659 O  OE1   . GLU A 1 203 ? -5.487  9.951   17.673  1 48.81  ? 203 GLU A OE1   1 1 
ATOM   1660 O  OE2   . GLU A 1 203 ? -6.022  12.011  18.25   1 50.54  ? 203 GLU A OE2   1 1 
ATOM   1661 N  N     . THR A 1 204 ? -4.807  9.845   11.583  1 33.86  ? 204 THR A N     1 1 
ATOM   1662 C  CA    . THR A 1 204 ? -4.195  8.959   10.596  1 34.14  ? 204 THR A CA    1 1 
ATOM   1663 C  C     . THR A 1 204 ? -3.029  9.635   9.844   1 34.06  ? 204 THR A C     1 1 
ATOM   1664 O  O     . THR A 1 204 ? -2.255  8.941   9.189   1 34.33  ? 204 THR A O     1 1 
ATOM   1665 C  CB    . THR A 1 204 ? -5.228  8.357   9.644   1 35.78  ? 204 THR A CB    1 1 
ATOM   1666 O  OG1   . THR A 1 204 ? -5.679  9.353   8.73    1 36.87  ? 204 THR A OG1   1 1 
ATOM   1667 C  CG2   . THR A 1 204 ? -6.392  7.682   10.373  1 36.27  ? 204 THR A CG2   1 1 
ATOM   1668 N  N     . ILE A 1 205 ? -2.889  10.975  9.963   1 33.5   ? 205 ILE A N     1 1 
ATOM   1669 C  CA    . ILE A 1 205 ? -1.815  11.759  9.376   1 33.29  ? 205 ILE A CA    1 1 
ATOM   1670 C  C     . ILE A 1 205 ? -0.469  11.384  10.033  1 33.64  ? 205 ILE A C     1 1 
ATOM   1671 O  O     . ILE A 1 205 ? 0.556   11.412  9.355   1 34.07  ? 205 ILE A O     1 1 
ATOM   1672 C  CB    . ILE A 1 205 ? -2.147  13.274  9.485   1 33.46  ? 205 ILE A CB    1 1 
ATOM   1673 C  CG1   . ILE A 1 205 ? -3.34   13.65   8.596   1 34.18  ? 205 ILE A CG1   1 1 
ATOM   1674 C  CG2   . ILE A 1 205 ? -0.944  14.152  9.168   1 33.91  ? 205 ILE A CG2   1 1 
ATOM   1675 C  CD1   . ILE A 1 205 ? -3.861  15.066  8.8     1 35.41  ? 205 ILE A CD1   1 1 
ATOM   1676 N  N     . PHE A 1 206 ? -0.459  10.966  11.323  1 33.35  ? 206 PHE A N     1 1 
ATOM   1677 C  CA    . PHE A 1 206 ? 0.786   10.56   11.983  1 33.75  ? 206 PHE A CA    1 1 
ATOM   1678 C  C     . PHE A 1 206 ? 1.458   9.418   11.23   1 34.45  ? 206 PHE A C     1 1 
ATOM   1679 O  O     . PHE A 1 206 ? 0.784   8.485   10.801  1 34.39  ? 206 PHE A O     1 1 
ATOM   1680 C  CB    . PHE A 1 206 ? 0.564   10.202  13.453  1 33.59  ? 206 PHE A CB    1 1 
ATOM   1681 C  CG    . PHE A 1 206 ? 0.079   11.36   14.287  1 34.11  ? 206 PHE A CG    1 1 
ATOM   1682 C  CD1   . PHE A 1 206 ? 0.724   12.578  14.247  1 34.65  ? 206 PHE A CD1   1 1 
ATOM   1683 C  CD2   . PHE A 1 206 ? -1.019  11.225  15.116  1 34.94  ? 206 PHE A CD2   1 1 
ATOM   1684 C  CE1   . PHE A 1 206 ? 0.265   13.649  15      1 35.37  ? 206 PHE A CE1   1 1 
ATOM   1685 C  CE2   . PHE A 1 206 ? -1.468  12.293  15.875  1 35.61  ? 206 PHE A CE2   1 1 
ATOM   1686 C  CZ    . PHE A 1 206 ? -0.809  13.493  15.829  1 35.28  ? 206 PHE A CZ    1 1 
ATOM   1687 N  N     . ALA A 1 207 ? 2.769   9.538   10.998  1 35     ? 207 ALA A N     1 1 
ATOM   1688 C  CA    . ALA A 1 207 ? 3.5     8.591   10.171  1 35.81  ? 207 ALA A CA    1 1 
ATOM   1689 C  C     . ALA A 1 207 ? 4.639   7.835   10.853  1 36.77  ? 207 ALA A C     1 1 
ATOM   1690 O  O     . ALA A 1 207 ? 5.544   7.383   10.145  1 37.12  ? 207 ALA A O     1 1 
ATOM   1691 C  CB    . ALA A 1 207 ? 4.033   9.319   8.943   1 35.88  ? 207 ALA A CB    1 1 
ATOM   1692 N  N     . GLU A 1 208 ? 4.611   7.652   12.19   1 37.01  ? 208 GLU A N     1 1 
ATOM   1693 C  CA    . GLU A 1 208 ? 5.714   6.938   12.865  1 37.55  ? 208 GLU A CA    1 1 
ATOM   1694 C  C     . GLU A 1 208 ? 5.981   5.55    12.314  1 37.8   ? 208 GLU A C     1 1 
ATOM   1695 O  O     . GLU A 1 208 ? 7.126   5.236   11.982  1 38.21  ? 208 GLU A O     1 1 
ATOM   1696 C  CB    . GLU A 1 208 ? 5.534   6.875   14.386  1 39.65  ? 208 GLU A CB    1 1 
ATOM   1697 C  CG    . GLU A 1 208 ? 5.794   8.198   15.075  1 43.23  ? 208 GLU A CG    1 1 
ATOM   1698 C  CD    . GLU A 1 208 ? 4.53    8.931   15.468  1 47.17  ? 208 GLU A CD    1 1 
ATOM   1699 O  OE1   . GLU A 1 208 ? 3.484   8.731   14.809  1 47.57  ? 208 GLU A OE1   1 1 
ATOM   1700 O  OE2   . GLU A 1 208 ? 4.591   9.714   16.442  1 48.4   ? 208 GLU A OE2   1 1 
ATOM   1701 N  N     . ASP A 1 209 ? 4.933   4.73    12.191  1 37.5   ? 209 ASP A N     1 1 
ATOM   1702 C  CA    . ASP A 1 209 ? 5.096   3.379   11.68   1 37.85  ? 209 ASP A CA    1 1 
ATOM   1703 C  C     . ASP A 1 209 ? 5.444   3.378   10.209  1 37.08  ? 209 ASP A C     1 1 
ATOM   1704 O  O     . ASP A 1 209 ? 6.307   2.62    9.8     1 37.19  ? 209 ASP A O     1 1 
ATOM   1705 C  CB    . ASP A 1 209 ? 3.846   2.531   11.943  1 40.82  ? 209 ASP A CB    1 1 
ATOM   1706 C  CG    . ASP A 1 209 ? 3.481   2.42    13.415  1 47.49  ? 209 ASP A CG    1 1 
ATOM   1707 O  OD1   . ASP A 1 209 ? 2.943   3.42    13.976  1 48.58  ? 209 ASP A OD1   1 1 
ATOM   1708 O  OD2   . ASP A 1 209 ? 3.721   1.329   14.011  1 50.02  ? 209 ASP A OD2   1 1 
ATOM   1709 N  N     . ASP A 1 210 ? 4.821   4.253   9.423   1 36.29  ? 210 ASP A N     1 1 
ATOM   1710 C  CA    . ASP A 1 210 ? 5.067   4.326   7.982   1 36.13  ? 210 ASP A CA    1 1 
ATOM   1711 C  C     . ASP A 1 210 ? 6.484   4.734   7.622   1 35.39  ? 210 ASP A C     1 1 
ATOM   1712 O  O     . ASP A 1 210 ? 7.019   4.215   6.643   1 35.66  ? 210 ASP A O     1 1 
ATOM   1713 C  CB    . ASP A 1 210 ? 4.08    5.264   7.288   1 38.22  ? 210 ASP A CB    1 1 
ATOM   1714 C  CG    . ASP A 1 210 ? 2.65    5.136   7.764   1 43.57  ? 210 ASP A CG    1 1 
ATOM   1715 O  OD1   . ASP A 1 210 ? 2.385   5.462   8.949   1 44.42  ? 210 ASP A OD1   1 1 
ATOM   1716 O  OD2   . ASP A 1 210 ? 1.79    4.731   6.951   1 46.06  ? 210 ASP A OD2   1 1 
ATOM   1717 N  N     . ILE A 1 211 ? 7.091   5.663   8.392   1 34.25  ? 211 ILE A N     1 1 
ATOM   1718 C  CA    . ILE A 1 211 ? 8.462   6.125   8.14    1 33.46  ? 211 ILE A CA    1 1 
ATOM   1719 C  C     . ILE A 1 211 ? 9.446   5.005   8.411   1 31.24  ? 211 ILE A C     1 1 
ATOM   1720 O  O     . ILE A 1 211 ? 10.303  4.722   7.572   1 31.03  ? 211 ILE A O     1 1 
ATOM   1721 C  CB    . ILE A 1 211 ? 8.791   7.429   8.921   1 34.97  ? 211 ILE A CB    1 1 
ATOM   1722 C  CG1   . ILE A 1 211 ? 8.011   8.62    8.333   1 37.02  ? 211 ILE A CG1   1 1 
ATOM   1723 C  CG2   . ILE A 1 211 ? 10.294  7.74    8.944   1 35.4   ? 211 ILE A CG2   1 1 
ATOM   1724 C  CD1   . ILE A 1 211 ? 8.323   8.914   6.867   1 38.93  ? 211 ILE A CD1   1 1 
ATOM   1725 N  N     . ALA A 1 212 ? 9.253   4.285   9.527   1 29.49  ? 212 ALA A N     1 1 
ATOM   1726 C  CA    . ALA A 1 212 ? 10.102  3.154   9.876   1 28.38  ? 212 ALA A CA    1 1 
ATOM   1727 C  C     . ALA A 1 212 ? 9.987   2.081   8.807   1 27.69  ? 212 ALA A C     1 1 
ATOM   1728 O  O     . ALA A 1 212 ? 11.007  1.609   8.335   1 27.85  ? 212 ALA A O     1 1 
ATOM   1729 C  CB    . ALA A 1 212 ? 9.713   2.6     11.235  1 28.28  ? 212 ALA A CB    1 1 
ATOM   1730 N  N     . ASP A 1 213 ? 8.757   1.796   8.334   1 27.08  ? 213 ASP A N     1 1 
ATOM   1731 C  CA    . ASP A 1 213 ? 8.507   0.81    7.277   1 26.73  ? 213 ASP A CA    1 1 
ATOM   1732 C  C     . ASP A 1 213 ? 9.204   1.203   5.983   1 26.02  ? 213 ASP A C     1 1 
ATOM   1733 O  O     . ASP A 1 213 ? 9.756   0.335   5.308   1 26.49  ? 213 ASP A O     1 1 
ATOM   1734 C  CB    . ASP A 1 213 ? 7.002   0.629   7.018   1 28.27  ? 213 ASP A CB    1 1 
ATOM   1735 C  CG    . ASP A 1 213 ? 6.258   -0.13   8.102   1 33.38  ? 213 ASP A CG    1 1 
ATOM   1736 O  OD1   . ASP A 1 213 ? 6.923   -0.72   8.982   1 34.23  ? 213 ASP A OD1   1 1 
ATOM   1737 O  OD2   . ASP A 1 213 ? 5.011   -0.117  8.084   1 36.04  ? 213 ASP A OD2   1 1 
ATOM   1738 N  N     . TYR A 1 214 ? 9.194   2.505   5.648   1 24.49  ? 214 TYR A N     1 1 
ATOM   1739 C  CA    . TYR A 1 214 ? 9.835   3.018   4.447   1 23.29  ? 214 TYR A CA    1 1 
ATOM   1740 C  C     . TYR A 1 214 ? 11.342  2.844   4.535   1 21.53  ? 214 TYR A C     1 1 
ATOM   1741 O  O     . TYR A 1 214 ? 11.937  2.314   3.6     1 21.49  ? 214 TYR A O     1 1 
ATOM   1742 C  CB    . TYR A 1 214 ? 9.462   4.493   4.212   1 23.54  ? 214 TYR A CB    1 1 
ATOM   1743 C  CG    . TYR A 1 214 ? 10.218  5.113   3.062   1 24.82  ? 214 TYR A CG    1 1 
ATOM   1744 C  CD1   . TYR A 1 214 ? 9.851   4.861   1.75    1 25.95  ? 214 TYR A CD1   1 1 
ATOM   1745 C  CD2   . TYR A 1 214 ? 11.328  5.918   3.286   1 26.1   ? 214 TYR A CD2   1 1 
ATOM   1746 C  CE1   . TYR A 1 214 ? 10.558  5.405   0.686   1 27.23  ? 214 TYR A CE1   1 1 
ATOM   1747 C  CE2   . TYR A 1 214 ? 12.046  6.469   2.231   1 27.29  ? 214 TYR A CE2   1 1 
ATOM   1748 C  CZ    . TYR A 1 214 ? 11.655  6.212   0.929   1 28.45  ? 214 TYR A CZ    1 1 
ATOM   1749 O  OH    . TYR A 1 214 ? 12.339  6.757   -0.131  1 30.32  ? 214 TYR A OH    1 1 
ATOM   1750 N  N     . ILE A 1 215 ? 11.96   3.289   5.647   1 19.9   ? 215 ILE A N     1 1 
ATOM   1751 C  CA    . ILE A 1 215 ? 13.404  3.202   5.851   1 18.73  ? 215 ILE A CA    1 1 
ATOM   1752 C  C     . ILE A 1 215 ? 13.89   1.776   5.745   1 18.28  ? 215 ILE A C     1 1 
ATOM   1753 O  O     . ILE A 1 215 ? 14.819  1.505   4.988   1 18.88  ? 215 ILE A O     1 1 
ATOM   1754 C  CB    . ILE A 1 215 ? 13.814  3.859   7.184   1 18.97  ? 215 ILE A CB    1 1 
ATOM   1755 C  CG1   . ILE A 1 215 ? 13.56   5.372   7.141   1 19.97  ? 215 ILE A CG1   1 1 
ATOM   1756 C  CG2   . ILE A 1 215 ? 15.262  3.556   7.529   1 19.55  ? 215 ILE A CG2   1 1 
ATOM   1757 C  CD1   . ILE A 1 215 ? 13.699  6.059   8.477   1 21.21  ? 215 ILE A CD1   1 1 
ATOM   1758 N  N     . ILE A 1 216 ? 13.234  0.855   6.463   1 17.05  ? 216 ILE A N     1 1 
ATOM   1759 C  CA    . ILE A 1 216 ? 13.58   -0.56   6.432   1 16.04  ? 216 ILE A CA    1 1 
ATOM   1760 C  C     . ILE A 1 216 ? 13.446  -1.13   5.018   1 15.82  ? 216 ILE A C     1 1 
ATOM   1761 O  O     . ILE A 1 216 ? 14.369  -1.79   4.558   1 15.74  ? 216 ILE A O     1 1 
ATOM   1762 C  CB    . ILE A 1 216 ? 12.758  -1.33   7.481   1 15.67  ? 216 ILE A CB    1 1 
ATOM   1763 C  CG1   . ILE A 1 216 ? 13.158  -0.881  8.88    1 15.66  ? 216 ILE A CG1   1 1 
ATOM   1764 C  CG2   . ILE A 1 216 ? 12.946  -2.829  7.326   1 16.26  ? 216 ILE A CG2   1 1 
ATOM   1765 C  CD1   . ILE A 1 216 ? 12.211  -1.216  9.896   1 16.09  ? 216 ILE A CD1   1 1 
ATOM   1766 N  N     . ALA A 1 217 ? 12.353  -0.804  4.295   1 15.51  ? 217 ALA A N     1 1 
ATOM   1767 C  CA    . ALA A 1 217 ? 12.174  -1.26   2.915   1 15.82  ? 217 ALA A CA    1 1 
ATOM   1768 C  C     . ALA A 1 217 ? 13.268  -0.751  1.967   1 16.27  ? 217 ALA A C     1 1 
ATOM   1769 O  O     . ALA A 1 217 ? 13.675  -1.5    1.087   1 16.19  ? 217 ALA A O     1 1 
ATOM   1770 C  CB    . ALA A 1 217 ? 10.81   -0.866  2.39    1 15.93  ? 217 ALA A CB    1 1 
ATOM   1771 N  N     . LYS A 1 218 ? 13.754  0.502   2.144   1 16.55  ? 218 LYS A N     1 1 
ATOM   1772 C  CA    . LYS A 1 218 ? 14.837  1.046   1.312   1 17.17  ? 218 LYS A CA    1 1 
ATOM   1773 C  C     . LYS A 1 218 ? 16.146  0.336   1.637   1 17.57  ? 218 LYS A C     1 1 
ATOM   1774 O  O     . LYS A 1 218 ? 16.87   -0.044  0.723   1 17.11  ? 218 LYS A O     1 1 
ATOM   1775 C  CB    . LYS A 1 218 ? 14.992  2.548   1.525   1 18.97  ? 218 LYS A CB    1 1 
ATOM   1776 C  CG    . LYS A 1 218 ? 13.819  3.339   1.012   1 23.76  ? 218 LYS A CG    1 1 
ATOM   1777 C  CD    . LYS A 1 218 ? 13.798  3.423   -0.499  1 28.48  ? 218 LYS A CD    1 1 
ATOM   1778 C  CE    . LYS A 1 218 ? 14.719  4.505   -1.007  1 32.2   ? 218 LYS A CE    1 1 
ATOM   1779 N  NZ    . LYS A 1 218 ? 14.358  4.922   -2.388  1 34.61  ? 218 LYS A NZ    1 1 
ATOM   1780 N  N     . LEU A 1 219 ? 16.414  0.095   2.931   1 18.41  ? 219 LEU A N     1 1 
ATOM   1781 C  CA    . LEU A 1 219 ? 17.594  -0.653  3.374   1 19.98  ? 219 LEU A CA    1 1 
ATOM   1782 C  C     . LEU A 1 219 ? 17.573  -2.092  2.81    1 21.32  ? 219 LEU A C     1 1 
ATOM   1783 O  O     . LEU A 1 219 ? 18.616  -2.641  2.477   1 21.29  ? 219 LEU A O     1 1 
ATOM   1784 C  CB    . LEU A 1 219 ? 17.663  -0.705  4.912   1 20.46  ? 219 LEU A CB    1 1 
ATOM   1785 C  CG    . LEU A 1 219 ? 17.741  0.629   5.65    1 22.29  ? 219 LEU A CG    1 1 
ATOM   1786 C  CD1   . LEU A 1 219 ? 17.649  0.432   7.147   1 22.85  ? 219 LEU A CD1   1 1 
ATOM   1787 C  CD2   . LEU A 1 219 ? 18.999  1.371   5.296   1 23.18  ? 219 LEU A CD2   1 1 
ATOM   1788 N  N     . GLN A 1 220 ? 16.38   -2.687  2.689   1 22.33  ? 220 GLN A N     1 1 
ATOM   1789 C  CA    . GLN A 1 220 ? 16.187  -4.025  2.144   1 23.93  ? 220 GLN A CA    1 1 
ATOM   1790 C  C     . GLN A 1 220 ? 16.125  -4.072  0.611   1 25.12  ? 220 GLN A C     1 1 
ATOM   1791 O  O     . GLN A 1 220 ? 15.86   -5.142  0.069   1 25.21  ? 220 GLN A O     1 1 
ATOM   1792 C  CB    . GLN A 1 220 ? 14.87   -4.616  2.674   1 26.38  ? 220 GLN A CB    1 1 
ATOM   1793 C  CG    . GLN A 1 220 ? 14.838  -4.916  4.161   1 30.96  ? 220 GLN A CG    1 1 
ATOM   1794 C  CD    . GLN A 1 220 ? 15.474  -6.241  4.479   1 36.89  ? 220 GLN A CD    1 1 
ATOM   1795 O  OE1   . GLN A 1 220 ? 16.459  -6.658  3.861   1 39.46  ? 220 GLN A OE1   1 1 
ATOM   1796 N  NE2   . GLN A 1 220 ? 14.936  -6.932  5.465   1 37.31  ? 220 GLN A NE2   1 1 
ATOM   1797 N  N     . HIS A 1 221 ? 16.304  -2.932  -0.081  1 26.02  ? 221 HIS A N     1 1 
ATOM   1798 C  CA    . HIS A 1 221 ? 16.202  -2.812  -1.538  1 27.49  ? 221 HIS A CA    1 1 
ATOM   1799 C  C     . HIS A 1 221 ? 14.854  -3.321  -2.03   1 28.66  ? 221 HIS A C     1 1 
ATOM   1800 O  O     . HIS A 1 221 ? 14.772  -4.073  -2.999  1 28.64  ? 221 HIS A O     1 1 
ATOM   1801 C  CB    . HIS A 1 221 ? 17.372  -3.486  -2.273  1 28.73  ? 221 HIS A CB    1 1 
ATOM   1802 C  CG    . HIS A 1 221 ? 17.447  -3.126  -3.727  1 31.68  ? 221 HIS A CG    1 1 
ATOM   1803 N  ND1   . HIS A 1 221 ? 17.765  -1.838  -4.139  1 33.82  ? 221 HIS A ND1   1 1 
ATOM   1804 C  CD2   . HIS A 1 221 ? 17.231  -3.894  -4.821  1 33.02  ? 221 HIS A CD2   1 1 
ATOM   1805 C  CE1   . HIS A 1 221 ? 17.73   -1.866  -5.463  1 34.41  ? 221 HIS A CE1   1 1 
ATOM   1806 N  NE2   . HIS A 1 221 ? 17.413  -3.082  -5.919  1 34.29  ? 221 HIS A NE2   1 1 
ATOM   1807 N  N     . ARG A 1 222 ? 13.795  -2.933  -1.33   1 29.57  ? 222 ARG A N     1 1 
ATOM   1808 C  CA    . ARG A 1 222 ? 12.451  -3.353  -1.679  1 31.17  ? 222 ARG A CA    1 1 
ATOM   1809 C  C     . ARG A 1 222 ? 11.655  -2.27   -2.359  1 32.36  ? 222 ARG A C     1 1 
ATOM   1810 O  O     . ARG A 1 222 ? 12.048  -1.111  -2.327  1 32.29  ? 222 ARG A O     1 1 
ATOM   1811 C  CB    . ARG A 1 222 ? 11.723  -3.905  -0.46   1 32.71  ? 222 ARG A CB    1 1 
ATOM   1812 C  CG    . ARG A 1 222 ? 12.241  -5.268  -0.105  1 35.47  ? 222 ARG A CG    1 1 
ATOM   1813 C  CD    . ARG A 1 222 ? 11.617  -5.775  1.154   1 38.57  ? 222 ARG A CD    1 1 
ATOM   1814 N  NE    . ARG A 1 222 ? 12.2    -7.062  1.511   1 41.58  ? 222 ARG A NE    1 1 
ATOM   1815 C  CZ    . ARG A 1 222 ? 12.188  -7.574  2.732   1 43.61  ? 222 ARG A CZ    1 1 
ATOM   1816 N  NH1   . ARG A 1 222 ? 11.626  -6.908  3.735   1 43.77  ? 222 ARG A NH1   1 1 
ATOM   1817 N  NH2   . ARG A 1 222 ? 12.742  -8.756  2.965   1 42.97  ? 222 ARG A NH2   1 1 
ATOM   1818 N  N     . ASP A 1 223 ? 10.562  -2.658  -3.024  1 33.42  ? 223 ASP A N     1 1 
ATOM   1819 C  CA    . ASP A 1 223 ? 9.711   -1.717  -3.725  1 34.95  ? 223 ASP A CA    1 1 
ATOM   1820 C  C     . ASP A 1 223 ? 8.964   -0.858  -2.714  1 35.41  ? 223 ASP A C     1 1 
ATOM   1821 O  O     . ASP A 1 223 ? 8.164   -1.367  -1.928  1 35.75  ? 223 ASP A O     1 1 
ATOM   1822 C  CB    . ASP A 1 223 ? 8.735   -2.459  -4.645  1 37.86  ? 223 ASP A CB    1 1 
ATOM   1823 C  CG    . ASP A 1 223 ? 8.038   -1.536  -5.621  1 44.63  ? 223 ASP A CG    1 1 
ATOM   1824 O  OD1   . ASP A 1 223 ? 7.063   -0.856  -5.206  1 45.27  ? 223 ASP A OD1   1 1 
ATOM   1825 O  OD2   . ASP A 1 223 ? 8.469   -1.483  -6.798  1 48.08  ? 223 ASP A OD2   1 1 
ATOM   1826 N  N     . THR A 1 224 ? 9.225   0.442   -2.738  1 35.29  ? 224 THR A N     1 1 
ATOM   1827 C  CA    . THR A 1 224 ? 8.608   1.359   -1.799  1 35.8   ? 224 THR A CA    1 1 
ATOM   1828 C  C     . THR A 1 224 ? 7.409   2.127   -2.361  1 35.92  ? 224 THR A C     1 1 
ATOM   1829 O  O     . THR A 1 224 ? 6.874   2.952   -1.64   1 35.93  ? 224 THR A O     1 1 
ATOM   1830 C  CB    . THR A 1 224 ? 9.668   2.31    -1.238  1 37.18  ? 224 THR A CB    1 1 
ATOM   1831 O  OG1   . THR A 1 224 ? 10.396  2.915   -2.316  1 38.24  ? 224 THR A OG1   1 1 
ATOM   1832 C  CG2   . THR A 1 224 ? 10.621  1.608   -0.293  1 37.31  ? 224 THR A CG2   1 1 
ATOM   1833 N  N     . SER A 1 225 ? 6.962   1.85    -3.606  1 35.75  ? 225 SER A N     1 1 
ATOM   1834 C  CA    . SER A 1 225 ? 5.838   2.568   -4.232  1 35.83  ? 225 SER A CA    1 1 
ATOM   1835 C  C     . SER A 1 225 ? 4.608   2.689   -3.35   1 35.71  ? 225 SER A C     1 1 
ATOM   1836 O  O     . SER A 1 225 ? 4.051   3.777   -3.232  1 35.98  ? 225 SER A O     1 1 
ATOM   1837 C  CB    . SER A 1 225 ? 5.439   1.933   -5.563  1 37.32  ? 225 SER A CB    1 1 
ATOM   1838 O  OG    . SER A 1 225 ? 6.523   1.828   -6.471  1 39.93  ? 225 SER A OG    1 1 
ATOM   1839 N  N     . ASN A 1 226 ? 4.19    1.582   -2.725  1 35.22  ? 226 ASN A N     1 1 
ATOM   1840 C  CA    . ASN A 1 226 ? 3.009   1.568   -1.869  1 35.12  ? 226 ASN A CA    1 1 
ATOM   1841 C  C     . ASN A 1 226 ? 3.216   2.323   -0.559  1 34.03  ? 226 ASN A C     1 1 
ATOM   1842 O  O     . ASN A 1 226 ? 2.31    3.028   -0.115  1 34.13  ? 226 ASN A O     1 1 
ATOM   1843 C  CB    . ASN A 1 226 ? 2.534   0.138   -1.635  1 37.06  ? 226 ASN A CB    1 1 
ATOM   1844 C  CG    . ASN A 1 226 ? 2.043   -0.543  -2.894  1 41.45  ? 226 ASN A CG    1 1 
ATOM   1845 O  OD1   . ASN A 1 226 ? 1.93    0.066   -3.968  1 42.73  ? 226 ASN A OD1   1 1 
ATOM   1846 N  ND2   . ASN A 1 226 ? 1.735   -1.831  -2.791  1 42.8   ? 226 ASN A ND2   1 1 
ATOM   1847 N  N     . ILE A 1 227 ? 4.41    2.212   0.04    1 32.76  ? 227 ILE A N     1 1 
ATOM   1848 C  CA    . ILE A 1 227 ? 4.705   2.941   1.271   1 31.75  ? 227 ILE A CA    1 1 
ATOM   1849 C  C     . ILE A 1 227 ? 4.751   4.445   0.968   1 30.36  ? 227 ILE A C     1 1 
ATOM   1850 O  O     . ILE A 1 227 ? 4.207   5.239   1.731   1 30.7   ? 227 ILE A O     1 1 
ATOM   1851 C  CB    . ILE A 1 227 ? 6.007   2.437   1.939   1 32.26  ? 227 ILE A CB    1 1 
ATOM   1852 C  CG1   . ILE A 1 227 ? 6.014   0.904   2.055   1 33.2   ? 227 ILE A CG1   1 1 
ATOM   1853 C  CG2   . ILE A 1 227 ? 6.193   3.092   3.307   1 32.81  ? 227 ILE A CG2   1 1 
ATOM   1854 C  CD1   . ILE A 1 227 ? 7.293   0.323   2.536   1 34.43  ? 227 ILE A CD1   1 1 
ATOM   1855 N  N     . GLU A 1 228 ? 5.35    4.828   -0.177  1 28.69  ? 228 GLU A N     1 1 
ATOM   1856 C  CA    . GLU A 1 228 ? 5.459   6.213   -0.62   1 27.54  ? 228 GLU A CA    1 1 
ATOM   1857 C  C     . GLU A 1 228 ? 4.077   6.808   -0.791  1 27.28  ? 228 GLU A C     1 1 
ATOM   1858 O  O     . GLU A 1 228 ? 3.84    7.91    -0.314  1 27.3   ? 228 GLU A O     1 1 
ATOM   1859 C  CB    . GLU A 1 228 ? 6.232   6.313   -1.946  1 28.12  ? 228 GLU A CB    1 1 
ATOM   1860 C  CG    . GLU A 1 228 ? 7.731   6.121   -1.813  1 30.49  ? 228 GLU A CG    1 1 
ATOM   1861 C  CD    . GLU A 1 228 ? 8.455   5.948   -3.133  1 33.04  ? 228 GLU A CD    1 1 
ATOM   1862 O  OE1   . GLU A 1 228 ? 8.013   6.549   -4.139  1 33.73  ? 228 GLU A OE1   1 1 
ATOM   1863 O  OE2   . GLU A 1 228 ? 9.463   5.207   -3.163  1 32.77  ? 228 GLU A OE2   1 1 
ATOM   1864 N  N     . GLN A 1 229 ? 3.145   6.057   -1.406  1 26.78  ? 229 GLN A N     1 1 
ATOM   1865 C  CA    . GLN A 1 229 ? 1.787   6.542   -1.612  1 26.8   ? 229 GLN A CA    1 1 
ATOM   1866 C  C     . GLN A 1 229 ? 1.035   6.804   -0.313  1 26.57  ? 229 GLN A C     1 1 
ATOM   1867 O  O     . GLN A 1 229 ? 0.31    7.79    -0.219  1 26.49  ? 229 GLN A O     1 1 
ATOM   1868 C  CB    . GLN A 1 229 ? 0.988   5.627   -2.546  1 28.41  ? 229 GLN A CB    1 1 
ATOM   1869 C  CG    . GLN A 1 229 ? -0.216  6.32    -3.166  1 32.16  ? 229 GLN A CG    1 1 
ATOM   1870 C  CD    . GLN A 1 229 ? 0.152   7.602   -3.883  1 37.64  ? 229 GLN A CD    1 1 
ATOM   1871 O  OE1   . GLN A 1 229 ? 0.893   7.588   -4.873  1 39.03  ? 229 GLN A OE1   1 1 
ATOM   1872 N  NE2   . GLN A 1 229 ? -0.34   8.743   -3.381  1 39.21  ? 229 GLN A NE2   1 1 
ATOM   1873 N  N     . LEU A 1 230 ? 1.255   5.974   0.71    1 26.42  ? 230 LEU A N     1 1 
ATOM   1874 C  CA    . LEU A 1 230 ? 0.628   6.182   2.012   1 26.79  ? 230 LEU A CA    1 1 
ATOM   1875 C  C     . LEU A 1 230 ? 1.117   7.476   2.626   1 26.87  ? 230 LEU A C     1 1 
ATOM   1876 O  O     . LEU A 1 230 ? 0.313   8.249   3.135   1 27.11  ? 230 LEU A O     1 1 
ATOM   1877 C  CB    . LEU A 1 230 ? 0.958   5.035   2.968   1 27.24  ? 230 LEU A CB    1 1 
ATOM   1878 C  CG    . LEU A 1 230 ? 0.273   3.727   2.714   1 29.22  ? 230 LEU A CG    1 1 
ATOM   1879 C  CD1   . LEU A 1 230 ? 0.745   2.69    3.713   1 30.21  ? 230 LEU A CD1   1 1 
ATOM   1880 C  CD2   . LEU A 1 230 ? -1.229  3.879   2.783   1 29.94  ? 230 LEU A CD2   1 1 
ATOM   1881 N  N     . LEU A 1 231 ? 2.431   7.724   2.546   1 26.62  ? 231 LEU A N     1 1 
ATOM   1882 C  CA    . LEU A 1 231 ? 3.057   8.923   3.086   1 27.06  ? 231 LEU A CA    1 1 
ATOM   1883 C  C     . LEU A 1 231 ? 2.622   10.202  2.329   1 27.21  ? 231 LEU A C     1 1 
ATOM   1884 O  O     . LEU A 1 231 ? 2.415   11.253  2.947   1 27.25  ? 231 LEU A O     1 1 
ATOM   1885 C  CB    . LEU A 1 231 ? 4.58    8.751   3.101   1 27.24  ? 231 LEU A CB    1 1 
ATOM   1886 C  CG    . LEU A 1 231 ? 5.096   7.735   4.128   1 28.77  ? 231 LEU A CG    1 1 
ATOM   1887 C  CD1   . LEU A 1 231 ? 6.562   7.405   3.897   1 29.06  ? 231 LEU A CD1   1 1 
ATOM   1888 C  CD2   . LEU A 1 231 ? 4.891   8.242   5.528   1 29.57  ? 231 LEU A CD2   1 1 
ATOM   1889 N  N     . ILE A 1 232 ? 2.45    10.094  1.002   1 26.74  ? 232 ILE A N     1 1 
ATOM   1890 C  CA    . ILE A 1 232 ? 1.994   11.203  0.173   1 26.65  ? 232 ILE A CA    1 1 
ATOM   1891 C  C     . ILE A 1 232 ? 0.556   11.536  0.547   1 26.81  ? 232 ILE A C     1 1 
ATOM   1892 O  O     . ILE A 1 232 ? 0.225   12.708  0.732   1 27.12  ? 232 ILE A O     1 1 
ATOM   1893 C  CB    . ILE A 1 232 ? 2.135   10.843  -1.327  1 27.03  ? 232 ILE A CB    1 1 
ATOM   1894 C  CG1   . ILE A 1 232 ? 3.614   10.733  -1.744  1 27.84  ? 232 ILE A CG1   1 1 
ATOM   1895 C  CG2   . ILE A 1 232 ? 1.38    11.814  -2.227  1 27.62  ? 232 ILE A CG2   1 1 
ATOM   1896 C  CD1   . ILE A 1 232 ? 4.466   11.913  -1.43   1 28.9   ? 232 ILE A CD1   1 1 
ATOM   1897 N  N     . ASN A 1 233 ? -0.286  10.503  0.719   1 26.27  ? 233 ASN A N     1 1 
ATOM   1898 C  CA    . ASN A 1 233 ? -1.68   10.682  1.118   1 25.95  ? 233 ASN A CA    1 1 
ATOM   1899 C  C     . ASN A 1 233 ? -1.792  11.402  2.471   1 25.36  ? 233 ASN A C     1 1 
ATOM   1900 O  O     . ASN A 1 233 ? -2.658  12.255  2.625   1 25.4   ? 233 ASN A O     1 1 
ATOM   1901 C  CB    . ASN A 1 233 ? -2.406  9.338   1.154   1 26.58  ? 233 ASN A CB    1 1 
ATOM   1902 C  CG    . ASN A 1 233 ? -2.71   8.773   -0.212  1 29.05  ? 233 ASN A CG    1 1 
ATOM   1903 O  OD1   . ASN A 1 233 ? -2.6    9.455   -1.244  1 29.12  ? 233 ASN A OD1   1 1 
ATOM   1904 N  ND2   . ASN A 1 233 ? -3.1    7.498   -0.244  1 30.25  ? 233 ASN A ND2   1 1 
ATOM   1905 N  N     . LYS A 1 234 ? -0.89   11.101  3.423   1 24.59  ? 234 LYS A N     1 1 
ATOM   1906 C  CA    . LYS A 1 234 ? -0.873  11.742  4.738   1 24.1   ? 234 LYS A CA    1 1 
ATOM   1907 C  C     . LYS A 1 234 ? -0.46   13.211  4.631   1 24.02  ? 234 LYS A C     1 1 
ATOM   1908 O  O     . LYS A 1 234 ? -1.05   14.071  5.291   1 24.04  ? 234 LYS A O     1 1 
ATOM   1909 C  CB    . LYS A 1 234 ? 0.035   10.972  5.697   1 24.85  ? 234 LYS A CB    1 1 
ATOM   1910 C  CG    . LYS A 1 234 ? -0.537  9.614   6.039   1 27.19  ? 234 LYS A CG    1 1 
ATOM   1911 C  CD    . LYS A 1 234 ? 0.318   8.864   7.009   1 30.32  ? 234 LYS A CD    1 1 
ATOM   1912 C  CE    . LYS A 1 234 ? -0.282  7.518   7.264   1 34.22  ? 234 LYS A CE    1 1 
ATOM   1913 N  NZ    . LYS A 1 234 ? 0.135   6.978   8.579   1 36.93  ? 234 LYS A NZ    1 1 
ATOM   1914 N  N     . ASN A 1 235 ? 0.513   13.501  3.752   1 23.72  ? 235 ASN A N     1 1 
ATOM   1915 C  CA    . ASN A 1 235 ? 0.973   14.861  3.457   1 23.69  ? 235 ASN A CA    1 1 
ATOM   1916 C  C     . ASN A 1 235 ? -0.221  15.661  2.856   1 23.56  ? 235 ASN A C     1 1 
ATOM   1917 O  O     . ASN A 1 235 ? -0.428  16.823  3.206   1 23.73  ? 235 ASN A O     1 1 
ATOM   1918 C  CB    . ASN A 1 235 ? 2.155   14.805  2.471   1 24.49  ? 235 ASN A CB    1 1 
ATOM   1919 C  CG    . ASN A 1 235 ? 2.967   16.073  2.353   1 27.82  ? 235 ASN A CG    1 1 
ATOM   1920 O  OD1   . ASN A 1 235 ? 2.513   17.165  2.673   1 29.61  ? 235 ASN A OD1   1 1 
ATOM   1921 N  ND2   . ASN A 1 235 ? 4.197   15.969  1.877   1 28.51  ? 235 ASN A ND2   1 1 
ATOM   1922 N  N     . LEU A 1 236 ? -1.027  15.016  1.992   1 22.69  ? 236 LEU A N     1 1 
ATOM   1923 C  CA    . LEU A 1 236 ? -2.191  15.632  1.377   1 21.98  ? 236 LEU A CA    1 1 
ATOM   1924 C  C     . LEU A 1 236 ? -3.288  15.851  2.387   1 22.44  ? 236 LEU A C     1 1 
ATOM   1925 O  O     . LEU A 1 236 ? -3.977  16.855  2.312   1 22.68  ? 236 LEU A O     1 1 
ATOM   1926 C  CB    . LEU A 1 236 ? -2.689  14.777  0.222   1 21.41  ? 236 LEU A CB    1 1 
ATOM   1927 C  CG    . LEU A 1 236 ? -3.732  15.426  -0.634  1 22.04  ? 236 LEU A CG    1 1 
ATOM   1928 C  CD1   . LEU A 1 236 ? -3.165  16.566  -1.405  1 22.17  ? 236 LEU A CD1   1 1 
ATOM   1929 C  CD2   . LEU A 1 236 ? -4.319  14.446  -1.569  1 22.72  ? 236 LEU A CD2   1 1 
ATOM   1930 N  N     . LYS A 1 237 ? -3.447  14.945  3.354   1 22.72  ? 237 LYS A N     1 1 
ATOM   1931 C  CA    . LYS A 1 237 ? -4.438  15.118  4.415   1 23.35  ? 237 LYS A CA    1 1 
ATOM   1932 C  C     . LYS A 1 237 ? -4.048  16.308  5.317   1 23.21  ? 237 LYS A C     1 1 
ATOM   1933 O  O     . LYS A 1 237 ? -4.933  16.998  5.805   1 23.03  ? 237 LYS A O     1 1 
ATOM   1934 C  CB    . LYS A 1 237 ? -4.643  13.822  5.215   1 25.67  ? 237 LYS A CB    1 1 
ATOM   1935 C  CG    . LYS A 1 237 ? -5.376  12.755  4.414   1 30.78  ? 237 LYS A CG    1 1 
ATOM   1936 C  CD    . LYS A 1 237 ? -5.582  11.421  5.173   1 35.35  ? 237 LYS A CD    1 1 
ATOM   1937 C  CE    . LYS A 1 237 ? -4.318  10.602  5.356   1 38.1   ? 237 LYS A CE    1 1 
ATOM   1938 N  NZ    . LYS A 1 237 ? -4.62   9.193   5.727   1 38.89  ? 237 LYS A NZ    1 1 
ATOM   1939 N  N     . MET A 1 238 ? -2.74   16.61   5.466   1 23.09  ? 238 MET A N     1 1 
ATOM   1940 C  CA    . MET A 1 238 ? -2.313  17.791  6.223   1 23.3   ? 238 MET A CA    1 1 
ATOM   1941 C  C     . MET A 1 238 ? -2.74   19.086  5.48    1 23.78  ? 238 MET A C     1 1 
ATOM   1942 O  O     . MET A 1 238 ? -3.214  20.038  6.106   1 23.98  ? 238 MET A O     1 1 
ATOM   1943 C  CB    . MET A 1 238 ? -0.806  17.772  6.497   1 23.16  ? 238 MET A CB    1 1 
ATOM   1944 C  CG    . MET A 1 238 ? -0.317  19.007  7.203   1 24.31  ? 238 MET A CG    1 1 
ATOM   1945 S  SD    . MET A 1 238 ? -1.096  19.246  8.808   1 25.83  ? 238 MET A SD    1 1 
ATOM   1946 C  CE    . MET A 1 238 ? -0.113  18.194  9.778   1 24.74  ? 238 MET A CE    1 1 
ATOM   1947 N  N     . VAL A 1 239 ? -2.632  19.083  4.139   1 23.49  ? 239 VAL A N     1 1 
ATOM   1948 C  CA    . VAL A 1 239 ? -3.093  20.165  3.271   1 23.42  ? 239 VAL A CA    1 1 
ATOM   1949 C  C     . VAL A 1 239 ? -4.609  20.328  3.435   1 24.22  ? 239 VAL A C     1 1 
ATOM   1950 O  O     . VAL A 1 239 ? -5.092  21.447  3.47    1 24.64  ? 239 VAL A O     1 1 
ATOM   1951 C  CB    . VAL A 1 239 ? -2.718  19.865  1.807   1 23.43  ? 239 VAL A CB    1 1 
ATOM   1952 C  CG1   . VAL A 1 239 ? -3.369  20.85   0.848   1 23.73  ? 239 VAL A CG1   1 1 
ATOM   1953 C  CG2   . VAL A 1 239 ? -1.211  19.85   1.636   1 23.83  ? 239 VAL A CG2   1 1 
ATOM   1954 N  N     . GLU A 1 240 ? -5.355  19.221  3.58    1 24.48  ? 240 GLU A N     1 1 
ATOM   1955 C  CA    . GLU A 1 240 ? -6.794  19.274  3.789   1 25.3   ? 240 GLU A CA    1 1 
ATOM   1956 C  C     . GLU A 1 240 ? -7.102  19.846  5.148   1 25.81  ? 240 GLU A C     1 1 
ATOM   1957 O  O     . GLU A 1 240 ? -7.953  20.72   5.255   1 26.35  ? 240 GLU A O     1 1 
ATOM   1958 C  CB    . GLU A 1 240 ? -7.446  17.894  3.645   1 27.91  ? 240 GLU A CB    1 1 
ATOM   1959 C  CG    . GLU A 1 240 ? -8.963  17.971  3.711   1 32.46  ? 240 GLU A CG    1 1 
ATOM   1960 C  CD    . GLU A 1 240 ? -9.698  16.653  3.598   1 39.14  ? 240 GLU A CD    1 1 
ATOM   1961 O  OE1   . GLU A 1 240 ? -9.034  15.592  3.573   1 41.83  ? 240 GLU A OE1   1 1 
ATOM   1962 O  OE2   . GLU A 1 240 ? -10.946 16.683  3.535   1 40.82  ? 240 GLU A OE2   1 1 
ATOM   1963 N  N     . PHE A 1 241 ? -6.386  19.405  6.187   1 25.58  ? 241 PHE A N     1 1 
ATOM   1964 C  CA    . PHE A 1 241 ? -6.59   19.913  7.539   1 26.25  ? 241 PHE A CA    1 1 
ATOM   1965 C  C     . PHE A 1 241 ? -6.362  21.426  7.594   1 26.64  ? 241 PHE A C     1 1 
ATOM   1966 O  O     . PHE A 1 241 ? -7.184  22.16   8.136   1 27.02  ? 241 PHE A O     1 1 
ATOM   1967 C  CB    . PHE A 1 241 ? -5.658  19.189  8.531   1 26.48  ? 241 PHE A CB    1 1 
ATOM   1968 C  CG    . PHE A 1 241 ? -5.561  19.846  9.891   1 27.37  ? 241 PHE A CG    1 1 
ATOM   1969 C  CD1   . PHE A 1 241 ? -6.644  19.847  10.755  1 28.03  ? 241 PHE A CD1   1 1 
ATOM   1970 C  CD2   . PHE A 1 241 ? -4.402  20.497  10.287  1 28.26  ? 241 PHE A CD2   1 1 
ATOM   1971 C  CE1   . PHE A 1 241 ? -6.562  20.455  11.997  1 28.76  ? 241 PHE A CE1   1 1 
ATOM   1972 C  CE2   . PHE A 1 241 ? -4.33   21.125  11.524  1 28.99  ? 241 PHE A CE2   1 1 
ATOM   1973 C  CZ    . PHE A 1 241 ? -5.414  21.101  12.37   1 28.75  ? 241 PHE A CZ    1 1 
ATOM   1974 N  N     . LEU A 1 242 ? -5.267  21.877  7.006   1 26.51  ? 242 LEU A N     1 1 
ATOM   1975 C  CA    . LEU A 1 242 ? -4.915  23.276  7.021   1 26.86  ? 242 LEU A CA    1 1 
ATOM   1976 C  C     . LEU A 1 242 ? -5.817  24.112  6.152   1 26.67  ? 242 LEU A C     1 1 
ATOM   1977 O  O     . LEU A 1 242 ? -6.239  25.167  6.611   1 27.58  ? 242 LEU A O     1 1 
ATOM   1978 C  CB    . LEU A 1 242 ? -3.448  23.473  6.613   1 27.35  ? 242 LEU A CB    1 1 
ATOM   1979 C  CG    . LEU A 1 242 ? -2.415  22.837  7.528   1 29.01  ? 242 LEU A CG    1 1 
ATOM   1980 C  CD1   . LEU A 1 242 ? -1.052  22.887  6.908   1 29.44  ? 242 LEU A CD1   1 1 
ATOM   1981 C  CD2   . LEU A 1 242 ? -2.396  23.498  8.882   1 29.9   ? 242 LEU A CD2   1 1 
ATOM   1982 N  N     . SER A 1 243 ? -6.119  23.676  4.915   1 25.51  ? 243 SER A N     1 1 
ATOM   1983 C  CA    . SER A 1 243 ? -6.91   24.507  4.008   1 25.3   ? 243 SER A CA    1 1 
ATOM   1984 C  C     . SER A 1 243 ? -8.364  24.643  4.431   1 25.52  ? 243 SER A C     1 1 
ATOM   1985 O  O     . SER A 1 243 ? -8.958  25.711  4.258   1 25.52  ? 243 SER A O     1 1 
ATOM   1986 C  CB    . SER A 1 243 ? -6.784  24.049  2.561   1 25.51  ? 243 SER A CB    1 1 
ATOM   1987 O  OG    . SER A 1 243 ? -7.148  22.692  2.4     1 26.39  ? 243 SER A OG    1 1 
ATOM   1988 N  N     . LYS A 1 244 ? -8.916  23.596  5.046   1 25.45  ? 244 LYS A N     1 1 
ATOM   1989 C  CA    . LYS A 1 244 ? -10.283 23.653  5.55    1 25.58  ? 244 LYS A CA    1 1 
ATOM   1990 C  C     . LYS A 1 244 ? -10.416 24.5    6.843   1 26.33  ? 244 LYS A C     1 1 
ATOM   1991 O  O     . LYS A 1 244 ? -11.527 24.819  7.256   1 26.2   ? 244 LYS A O     1 1 
ATOM   1992 C  CB    . LYS A 1 244 ? -10.86  22.244  5.706   1 26.3   ? 244 LYS A CB    1 1 
ATOM   1993 C  CG    . LYS A 1 244 ? -11.054 21.56   4.364   1 28.33  ? 244 LYS A CG    1 1 
ATOM   1994 C  CD    . LYS A 1 244 ? -11.864 20.294  4.473   1 31.12  ? 244 LYS A CD    1 1 
ATOM   1995 C  CE    . LYS A 1 244 ? -12.256 19.78   3.113   1 33.93  ? 244 LYS A CE    1 1 
ATOM   1996 N  NZ    . LYS A 1 244 ? -13.152 18.604  3.207   1 35.98  ? 244 LYS A NZ    1 1 
ATOM   1997 N  N     . ASN A 1 245 ? -9.289  24.893  7.455   1 27     ? 245 ASN A N     1 1 
ATOM   1998 C  CA    . ASN A 1 245 ? -9.277  25.758  8.629   1 28     ? 245 ASN A CA    1 1 
ATOM   1999 C  C     . ASN A 1 245 ? -8.955  27.229  8.292   1 28.93  ? 245 ASN A C     1 1 
ATOM   2000 O  O     . ASN A 1 245 ? -8.929  28.058  9.197   1 28.68  ? 245 ASN A O     1 1 
ATOM   2001 C  CB    . ASN A 1 245 ? -8.328  25.215  9.695   1 29     ? 245 ASN A CB    1 1 
ATOM   2002 C  CG    . ASN A 1 245 ? -8.927  24.095  10.514  1 32.08  ? 245 ASN A CG    1 1 
ATOM   2003 O  OD1   . ASN A 1 245 ? -10.144 23.892  10.553  1 32.61  ? 245 ASN A OD1   1 1 
ATOM   2004 N  ND2   . ASN A 1 245 ? -8.081  23.355  11.204  1 33.08  ? 245 ASN A ND2   1 1 
ATOM   2005 N  N     . THR A 1 246 ? -8.713  27.558  7.005   1 30.08  ? 246 THR A N     1 1 
ATOM   2006 C  CA    . THR A 1 246 ? -8.426  28.93   6.571   1 31.87  ? 246 THR A CA    1 1 
ATOM   2007 C  C     . THR A 1 246 ? -9.629  29.551  5.834   1 33.59  ? 246 THR A C     1 1 
ATOM   2008 O  O     . THR A 1 246 ? -10.462 28.816  5.286   1 33.68  ? 246 THR A O     1 1 
ATOM   2009 C  CB    . THR A 1 246 ? -7.143  29.002  5.717   1 33.27  ? 246 THR A CB    1 1 
ATOM   2010 O  OG1   . THR A 1 246 ? -7.29   28.198  4.546   1 34.39  ? 246 THR A OG1   1 1 
ATOM   2011 C  CG2   . THR A 1 246 ? -5.907  28.585  6.484   1 33.61  ? 246 THR A CG2   1 1 
ATOM   2012 N  N     . LYS A 1 247 ? -9.728  30.907  5.839   1 34.42  ? 247 LYS A N     1 1 
ATOM   2013 C  CA    . LYS A 1 247 ? -10.82  31.621  5.16    1 35.5   ? 247 LYS A CA    1 1 
ATOM   2014 C  C     . LYS A 1 247 ? -10.647 31.473  3.654   1 36.54  ? 247 LYS A C     1 1 
ATOM   2015 O  O     . LYS A 1 247 ? -9.593  31.8    3.107   1 36.67  ? 247 LYS A O     1 1 
ATOM   2016 C  CB    . LYS A 1 247 ? -10.943 33.1    5.576   1 37.48  ? 247 LYS A CB    1 1 
ATOM   2017 C  CG    . LYS A 1 247 ? -10.031 33.545  6.711   1 43.09  ? 247 LYS A CG    1 1 
ATOM   2018 C  CD    . LYS A 1 247 ? -8.714  34.143  6.174   1 48.77  ? 247 LYS A CD    1 1 
ATOM   2019 C  CE    . LYS A 1 247 ? -7.507  33.799  7.021   1 52.48  ? 247 LYS A CE    1 1 
ATOM   2020 N  NZ    . LYS A 1 247 ? -7.103  32.376  6.865   1 54.6   ? 247 LYS A NZ    1 1 
ATOM   2021 N  N     . ASN A 1 248 ? -11.672 30.914  3.001   1 37.09  ? 248 ASN A N     1 1 
ATOM   2022 C  CA    . ASN A 1 248 ? -11.696 30.58   1.581   1 38.06  ? 248 ASN A CA    1 1 
ATOM   2023 C  C     . ASN A 1 248 ? -11.607 31.778  0.661   1 38.1   ? 248 ASN A C     1 1 
ATOM   2024 O  O     . ASN A 1 248 ? -11.158 31.62   -0.465  1 38.29  ? 248 ASN A O     1 1 
ATOM   2025 C  CB    . ASN A 1 248 ? -12.964 29.79   1.243   1 40.47  ? 248 ASN A CB    1 1 
ATOM   2026 C  CG    . ASN A 1 248 ? -13.307 28.669  2.209   1 45.43  ? 248 ASN A CG    1 1 
ATOM   2027 O  OD1   . ASN A 1 248 ? -14.476 28.496  2.614   1 46.75  ? 248 ASN A OD1   1 1 
ATOM   2028 N  ND2   . ASN A 1 248 ? -12.295 27.89   2.607   1 46.42  ? 248 ASN A ND2   1 1 
ATOM   2029 N  N     . ASP A 1 249 ? -12.048 32.962  1.12    1 37.8   ? 249 ASP A N     1 1 
ATOM   2030 C  CA    . ASP A 1 249 ? -12.101 34.194  0.326   1 37.88  ? 249 ASP A CA    1 1 
ATOM   2031 C  C     . ASP A 1 249 ? -10.774 34.636  -0.285  1 37.78  ? 249 ASP A C     1 1 
ATOM   2032 O  O     . ASP A 1 249 ? -10.765 35.11   -1.422  1 37.83  ? 249 ASP A O     1 1 
ATOM   2033 C  CB    . ASP A 1 249 ? -12.71  35.341  1.149   1 39.33  ? 249 ASP A CB    1 1 
ATOM   2034 N  N     . ASN A 1 250 ? -9.663  34.495  0.462   1 37.51  ? 250 ASN A N     1 1 
ATOM   2035 C  CA    . ASN A 1 250 ? -8.339  34.914  -0.014  1 37.61  ? 250 ASN A CA    1 1 
ATOM   2036 C  C     . ASN A 1 250 ? -7.273  33.783  -0.004  1 37.41  ? 250 ASN A C     1 1 
ATOM   2037 O  O     . ASN A 1 250 ? -6.08   34.061  -0.154  1 37.62  ? 250 ASN A O     1 1 
ATOM   2038 C  CB    . ASN A 1 250 ? -7.855  36.145  0.762   1 38.48  ? 250 ASN A CB    1 1 
ATOM   2039 C  CG    . ASN A 1 250 ? -7.58   35.885  2.226   1 41.37  ? 250 ASN A CG    1 1 
ATOM   2040 O  OD1   . ASN A 1 250 ? -6.437  35.62   2.628   1 42.93  ? 250 ASN A OD1   1 1 
ATOM   2041 N  ND2   . ASN A 1 250 ? -8.618  35.957  3.055   1 41.21  ? 250 ASN A ND2   1 1 
ATOM   2042 N  N     . ASN A 1 251 ? -7.705  32.521  0.166   1 36.74  ? 251 ASN A N     1 1 
ATOM   2043 C  CA    . ASN A 1 251 ? -6.814  31.355  0.168   1 36.72  ? 251 ASN A CA    1 1 
ATOM   2044 C  C     . ASN A 1 251 ? -7.445  30.218  -0.637  1 35.79  ? 251 ASN A C     1 1 
ATOM   2045 O  O     . ASN A 1 251 ? -8.666  30.158  -0.741  1 35.93  ? 251 ASN A O     1 1 
ATOM   2046 C  CB    . ASN A 1 251 ? -6.576  30.852  1.596   1 38.52  ? 251 ASN A CB    1 1 
ATOM   2047 C  CG    . ASN A 1 251 ? -6.109  31.893  2.578   1 42.54  ? 251 ASN A CG    1 1 
ATOM   2048 O  OD1   . ASN A 1 251 ? -6.874  32.375  3.425   1 43.7   ? 251 ASN A OD1   1 1 
ATOM   2049 N  ND2   . ASN A 1 251 ? -4.841  32.257  2.494   1 43.68  ? 251 ASN A ND2   1 1 
ATOM   2050 N  N     . PHE A 1 252 ? -6.63   29.287  -1.162  1 34.71  ? 252 PHE A N     1 1 
ATOM   2051 C  CA    . PHE A 1 252 ? -7.139  28.134  -1.907  1 34.1   ? 252 PHE A CA    1 1 
ATOM   2052 C  C     . PHE A 1 252 ? -7.977  27.263  -0.996  1 33.56  ? 252 PHE A C     1 1 
ATOM   2053 O  O     . PHE A 1 252 ? -7.663  27.109  0.179   1 33.81  ? 252 PHE A O     1 1 
ATOM   2054 C  CB    . PHE A 1 252 ? -6      27.251  -2.455  1 33.94  ? 252 PHE A CB    1 1 
ATOM   2055 C  CG    . PHE A 1 252 ? -5.406  27.6    -3.798  1 34.69  ? 252 PHE A CG    1 1 
ATOM   2056 C  CD1   . PHE A 1 252 ? -5.805  28.733  -4.477  1 35.85  ? 252 PHE A CD1   1 1 
ATOM   2057 C  CD2   . PHE A 1 252 ? -4.421  26.813  -4.362  1 35.49  ? 252 PHE A CD2   1 1 
ATOM   2058 C  CE1   . PHE A 1 252 ? -5.235  29.064  -5.701  1 36.75  ? 252 PHE A CE1   1 1 
ATOM   2059 C  CE2   . PHE A 1 252 ? -3.861  27.141  -5.588  1 36.41  ? 252 PHE A CE2   1 1 
ATOM   2060 C  CZ    . PHE A 1 252 ? -4.27   28.264  -6.249  1 36.49  ? 252 PHE A CZ    1 1 
ATOM   2061 N  N     . THR A 1 253 ? -9.036  26.689  -1.537  1 32.78  ? 253 THR A N     1 1 
ATOM   2062 C  CA    . THR A 1 253 ? -9.866  25.741  -0.803  1 32.61  ? 253 THR A CA    1 1 
ATOM   2063 C  C     . THR A 1 253 ? -9.231  24.341  -0.966  1 31.96  ? 253 THR A C     1 1 
ATOM   2064 O  O     . THR A 1 253 ? -8.315  24.17   -1.799  1 32.1   ? 253 THR A O     1 1 
ATOM   2065 C  CB    . THR A 1 253 ? -11.289 25.746  -1.39   1 34.13  ? 253 THR A CB    1 1 
ATOM   2066 O  OG1   . THR A 1 253 ? -11.244 25.317  -2.756  1 35.12  ? 253 THR A OG1   1 1 
ATOM   2067 C  CG2   . THR A 1 253 ? -11.959 27.099  -1.284  1 34.71  ? 253 THR A CG2   1 1 
ATOM   2068 N  N     . TYR A 1 254 ? -9.727  23.325  -0.207  1 30.72  ? 254 TYR A N     1 1 
ATOM   2069 C  CA    . TYR A 1 254 ? -9.202  21.983  -0.4    1 29.89  ? 254 TYR A CA    1 1 
ATOM   2070 C  C     . TYR A 1 254 ? -9.596  21.465  -1.775  1 29.54  ? 254 TYR A C     1 1 
ATOM   2071 O  O     . TYR A 1 254 ? -8.772  20.828  -2.414  1 29.89  ? 254 TYR A O     1 1 
ATOM   2072 C  CB    . TYR A 1 254 ? -9.579  21.002  0.704   1 29.57  ? 254 TYR A CB    1 1 
ATOM   2073 C  CG    . TYR A 1 254 ? -8.997  19.631  0.43    1 30.22  ? 254 TYR A CG    1 1 
ATOM   2074 C  CD1   . TYR A 1 254 ? -7.625  19.441  0.358   1 31.05  ? 254 TYR A CD1   1 1 
ATOM   2075 C  CD2   . TYR A 1 254 ? -9.817  18.563  0.091   1 31.11  ? 254 TYR A CD2   1 1 
ATOM   2076 C  CE1   . TYR A 1 254 ? -7.084  18.201  0.043   1 32.05  ? 254 TYR A CE1   1 1 
ATOM   2077 C  CE2   . TYR A 1 254 ? -9.29   17.319  -0.224  1 32.05  ? 254 TYR A CE2   1 1 
ATOM   2078 C  CZ    . TYR A 1 254 ? -7.922  17.136  -0.234  1 33.2   ? 254 TYR A CZ    1 1 
ATOM   2079 O  OH    . TYR A 1 254 ? -7.41   15.89   -0.516  1 34.96  ? 254 TYR A OH    1 1 
ATOM   2080 N  N     . SER A 1 255 ? -10.799 21.806  -2.28   1 29.01  ? 255 SER A N     1 1 
ATOM   2081 C  CA    . SER A 1 255 ? -11.205 21.348  -3.612  1 29.06  ? 255 SER A CA    1 1 
ATOM   2082 C  C     . SER A 1 255 ? -10.246 21.854  -4.696  1 28.97  ? 255 SER A C     1 1 
ATOM   2083 O  O     . SER A 1 255 ? -9.912  21.098  -5.61   1 29.32  ? 255 SER A O     1 1 
ATOM   2084 C  CB    . SER A 1 255 ? -12.669 21.668  -3.918  1 29.89  ? 255 SER A CB    1 1 
ATOM   2085 O  OG    . SER A 1 255 ? -13.055 22.995  -3.603  1 31.97  ? 255 SER A OG    1 1 
ATOM   2086 N  N     . GLU A 1 256 ? -9.723  23.079  -4.529  1 28.31  ? 256 GLU A N     1 1 
ATOM   2087 C  CA    . GLU A 1 256 ? -8.75   23.64   -5.458  1 28.42  ? 256 GLU A CA    1 1 
ATOM   2088 C  C     . GLU A 1 256 ? -7.424  22.9    -5.398  1 28.41  ? 256 GLU A C     1 1 
ATOM   2089 O  O     . GLU A 1 256 ? -6.89   22.558  -6.45   1 28.52  ? 256 GLU A O     1 1 
ATOM   2090 C  CB    . GLU A 1 256 ? -8.556  25.136  -5.214  1 30.2   ? 256 GLU A CB    1 1 
ATOM   2091 C  CG    . GLU A 1 256 ? -9.659  25.961  -5.841  1 34.31  ? 256 GLU A CG    1 1 
ATOM   2092 C  CD    . GLU A 1 256 ? -9.723  27.384  -5.329  1 40.33  ? 256 GLU A CD    1 1 
ATOM   2093 O  OE1   . GLU A 1 256 ? -9.321  27.615  -4.169  1 41.76  ? 256 GLU A OE1   1 1 
ATOM   2094 O  OE2   . GLU A 1 256 ? -10.181 28.271  -6.082  1 42.14  ? 256 GLU A OE2   1 1 
ATOM   2095 N  N     . TRP A 1 257 ? -6.913  22.607  -4.185  1 28.29  ? 257 TRP A N     1 1 
ATOM   2096 C  CA    . TRP A 1 257 ? -5.666  21.847  -4.029  1 28.81  ? 257 TRP A CA    1 1 
ATOM   2097 C  C     . TRP A 1 257 ? -5.803  20.448  -4.608  1 28.65  ? 257 TRP A C     1 1 
ATOM   2098 O  O     . TRP A 1 257 ? -4.914  19.975  -5.304  1 28.3   ? 257 TRP A O     1 1 
ATOM   2099 C  CB    . TRP A 1 257 ? -5.247  21.739  -2.557  1 28.98  ? 257 TRP A CB    1 1 
ATOM   2100 C  CG    . TRP A 1 257 ? -4.675  22.991  -1.965  1 29.73  ? 257 TRP A CG    1 1 
ATOM   2101 C  CD1   . TRP A 1 257 ? -5.149  23.664  -0.881  1 30.79  ? 257 TRP A CD1   1 1 
ATOM   2102 C  CD2   . TRP A 1 257 ? -3.479  23.68   -2.376  1 29.86  ? 257 TRP A CD2   1 1 
ATOM   2103 N  NE1   . TRP A 1 257 ? -4.333  24.735  -0.595  1 31.07  ? 257 TRP A NE1   1 1 
ATOM   2104 C  CE2   . TRP A 1 257 ? -3.301  24.766  -1.5    1 30.77  ? 257 TRP A CE2   1 1 
ATOM   2105 C  CE3   . TRP A 1 257 ? -2.542  23.488  -3.405  1 30.36  ? 257 TRP A CE3   1 1 
ATOM   2106 C  CZ2   . TRP A 1 257 ? -2.227  25.656  -1.623  1 31.36  ? 257 TRP A CZ2   1 1 
ATOM   2107 C  CZ3   . TRP A 1 257 ? -1.489  24.378  -3.53   1 30.98  ? 257 TRP A CZ3   1 1 
ATOM   2108 C  CH2   . TRP A 1 257 ? -1.328  25.433  -2.636  1 31.15  ? 257 TRP A CH2   1 1 
ATOM   2109 N  N     . GLU A 1 258 ? -6.931  19.81   -4.341  1 29.02  ? 258 GLU A N     1 1 
ATOM   2110 C  CA    . GLU A 1 258 ? -7.248  18.488  -4.84   1 30.06  ? 258 GLU A CA    1 1 
ATOM   2111 C  C     . GLU A 1 258 ? -7.28   18.463  -6.371  1 30.4   ? 258 GLU A C     1 1 
ATOM   2112 O  O     . GLU A 1 258 ? -6.747  17.529  -6.955  1 30.65  ? 258 GLU A O     1 1 
ATOM   2113 C  CB    . GLU A 1 258 ? -8.591  18.023  -4.278  1 32.95  ? 258 GLU A CB    1 1 
ATOM   2114 C  CG    . GLU A 1 258 ? -8.874  16.567  -4.566  1 38.63  ? 258 GLU A CG    1 1 
ATOM   2115 C  CD    . GLU A 1 258 ? -10.224 16.143  -4.044  1 46.48  ? 258 GLU A CD    1 1 
ATOM   2116 O  OE1   . GLU A 1 258 ? -11.195 16.916  -4.215  1 47.73  ? 258 GLU A OE1   1 1 
ATOM   2117 O  OE2   . GLU A 1 258 ? -10.309 15.039  -3.459  1 49.47  ? 258 GLU A OE2   1 1 
ATOM   2118 N  N     . SER A 1 259 ? -7.855  19.489  -7.028  1 30.2   ? 259 SER A N     1 1 
ATOM   2119 C  CA    . SER A 1 259 ? -7.88   19.535  -8.497  1 30.45  ? 259 SER A CA    1 1 
ATOM   2120 C  C     . SER A 1 259 ? -6.48   19.658  -9.104  1 30.59  ? 259 SER A C     1 1 
ATOM   2121 O  O     . SER A 1 259 ? -6.267  19.204  -10.228 1 31.04  ? 259 SER A O     1 1 
ATOM   2122 C  CB    . SER A 1 259 ? -8.775  20.661  -9.005  1 31.8   ? 259 SER A CB    1 1 
ATOM   2123 O  OG    . SER A 1 259 ? -8.223  21.948  -8.78   1 33.65  ? 259 SER A OG    1 1 
ATOM   2124 N  N     . ILE A 1 260 ? -5.525  20.245  -8.356  1 29.95  ? 260 ILE A N     1 1 
ATOM   2125 C  CA    . ILE A 1 260 ? -4.134  20.371  -8.781  1 29.71  ? 260 ILE A CA    1 1 
ATOM   2126 C  C     . ILE A 1 260 ? -3.453  19.025  -8.578  1 29.97  ? 260 ILE A C     1 1 
ATOM   2127 O  O     . ILE A 1 260 ? -2.787  18.536  -9.491  1 30.12  ? 260 ILE A O     1 1 
ATOM   2128 C  CB    . ILE A 1 260 ? -3.417  21.497  -7.996  1 29.7   ? 260 ILE A CB    1 1 
ATOM   2129 C  CG1   . ILE A 1 260 ? -4.028  22.863  -8.303  1 30.08  ? 260 ILE A CG1   1 1 
ATOM   2130 C  CG2   . ILE A 1 260 ? -1.935  21.507  -8.294  1 30.23  ? 260 ILE A CG2   1 1 
ATOM   2131 C  CD1   . ILE A 1 260 ? -3.67   23.876  -7.327  1 30.98  ? 260 ILE A CD1   1 1 
ATOM   2132 N  N     . TYR A 1 261 ? -3.661  18.411  -7.39   1 29.92  ? 261 TYR A N     1 1 
ATOM   2133 C  CA    . TYR A 1 261 ? -3.116  17.117  -6.978  1 30.2   ? 261 TYR A CA    1 1 
ATOM   2134 C  C     . TYR A 1 261 ? -3.467  16.015  -7.945  1 31.2   ? 261 TYR A C     1 1 
ATOM   2135 O  O     . TYR A 1 261 ? -2.572  15.313  -8.408  1 31.44  ? 261 TYR A O     1 1 
ATOM   2136 C  CB    . TYR A 1 261 ? -3.565  16.756  -5.546  1 29.79  ? 261 TYR A CB    1 1 
ATOM   2137 C  CG    . TYR A 1 261 ? -3.116  15.384  -5.105  1 30.43  ? 261 TYR A CG    1 1 
ATOM   2138 C  CD1   . TYR A 1 261 ? -1.82   15.163  -4.671  1 31.65  ? 261 TYR A CD1   1 1 
ATOM   2139 C  CD2   . TYR A 1 261 ? -3.974  14.296  -5.168  1 31.24  ? 261 TYR A CD2   1 1 
ATOM   2140 C  CE1   . TYR A 1 261 ? -1.386  13.894  -4.299  1 32.65  ? 261 TYR A CE1   1 1 
ATOM   2141 C  CE2   . TYR A 1 261 ? -3.55   13.019  -4.809  1 32.23  ? 261 TYR A CE2   1 1 
ATOM   2142 C  CZ    . TYR A 1 261 ? -2.257  12.823  -4.359  1 33.23  ? 261 TYR A CZ    1 1 
ATOM   2143 O  OH    . TYR A 1 261 ? -1.823  11.57   -3.981  1 34.51  ? 261 TYR A OH    1 1 
ATOM   2144 N  N     . ASN A 1 262 ? -4.758  15.852  -8.26   1 31.93  ? 262 ASN A N     1 1 
ATOM   2145 C  CA    . ASN A 1 262 ? -5.182  14.795  -9.172  1 33.09  ? 262 ASN A CA    1 1 
ATOM   2146 C  C     . ASN A 1 262 ? -4.848  15.076  -10.659 1 34.12  ? 262 ASN A C     1 1 
ATOM   2147 O  O     . ASN A 1 262 ? -5.245  14.308  -11.529 1 34.44  ? 262 ASN A O     1 1 
ATOM   2148 C  CB    . ASN A 1 262 ? -6.659  14.434  -8.98   1 34.3   ? 262 ASN A CB    1 1 
ATOM   2149 C  CG    . ASN A 1 262 ? -7.648  15.55   -9.218  1 38.58  ? 262 ASN A CG    1 1 
ATOM   2150 O  OD1   . ASN A 1 262 ? -7.404  16.5    -9.973  1 39.97  ? 262 ASN A OD1   1 1 
ATOM   2151 N  ND2   . ASN A 1 262 ? -8.811  15.457  -8.581  1 39.55  ? 262 ASN A ND2   1 1 
ATOM   2152 N  N     . GLY A 1 263 ? -4.115  16.149  -10.933 1 34.48  ? 263 GLY A N     1 1 
ATOM   2153 C  CA    . GLY A 1 263 ? -3.681  16.482  -12.278 1 35.53  ? 263 GLY A CA    1 1 
ATOM   2154 C  C     . GLY A 1 263 ? -4.729  17.082  -13.184 1 36.62  ? 263 GLY A C     1 1 
ATOM   2155 O  O     . GLY A 1 263 ? -4.493  17.19   -14.388 1 36.77  ? 263 GLY A O     1 1 
ATOM   2156 N  N     . THR A 1 264 ? -5.887  17.48   -12.633 1 37.33  ? 264 THR A N     1 1 
ATOM   2157 C  CA    . THR A 1 264 ? -6.939  18.085  -13.455 1 38.65  ? 264 THR A CA    1 1 
ATOM   2158 C  C     . THR A 1 264 ? -6.458  19.422  -14.005 1 39.69  ? 264 THR A C     1 1 
ATOM   2159 O  O     . THR A 1 264 ? -6.606  19.707  -15.193 1 39.67  ? 264 THR A O     1 1 
ATOM   2160 C  CB    . THR A 1 264 ? -8.264  18.224  -12.685 1 39.91  ? 264 THR A CB    1 1 
ATOM   2161 O  OG1   . THR A 1 264 ? -8.661  16.949  -12.17  1 40.73  ? 264 THR A OG1   1 1 
ATOM   2162 C  CG2   . THR A 1 264 ? -9.376  18.768  -13.565 1 40.31  ? 264 THR A CG2   1 1 
ATOM   2163 N  N     . TYR A 1 265 ? -5.839  20.217  -13.143 1 40.56  ? 265 TYR A N     1 1 
ATOM   2164 C  CA    . TYR A 1 265 ? -5.291  21.511  -13.515 1 41.9   ? 265 TYR A CA    1 1 
ATOM   2165 C  C     . TYR A 1 265 ? -3.884  21.676  -12.939 1 42.52  ? 265 TYR A C     1 1 
ATOM   2166 O  O     . TYR A 1 265 ? -3.517  21.012  -11.965 1 42.62  ? 265 TYR A O     1 1 
ATOM   2167 C  CB    . TYR A 1 265 ? -6.183  22.645  -12.96  1 42.42  ? 265 TYR A CB    1 1 
ATOM   2168 C  CG    . TYR A 1 265 ? -7.644  22.542  -13.34  1 43.79  ? 265 TYR A CG    1 1 
ATOM   2169 C  CD1   . TYR A 1 265 ? -8.067  22.799  -14.637 1 44.86  ? 265 TYR A CD1   1 1 
ATOM   2170 C  CD2   . TYR A 1 265 ? -8.609  22.213  -12.394 1 44.89  ? 265 TYR A CD2   1 1 
ATOM   2171 C  CE1   . TYR A 1 265 ? -9.41   22.71   -14.99  1 45.76  ? 265 TYR A CE1   1 1 
ATOM   2172 C  CE2   . TYR A 1 265 ? -9.958  22.137  -12.732 1 45.69  ? 265 TYR A CE2   1 1 
ATOM   2173 C  CZ    . TYR A 1 265 ? -10.351 22.37   -14.037 1 46.6   ? 265 TYR A CZ    1 1 
ATOM   2174 O  OH    . TYR A 1 265 ? -11.674 22.282  -14.391 1 48.2   ? 265 TYR A OH    1 1 
ATOM   2175 N  N     . ARG A 1 266 ? -3.096  22.568  -13.537 1 42.65  ? 266 ARG A N     1 1 
ATOM   2176 C  CA    . ARG A 1 266 ? -1.801  22.933  -12.976 1 43.22  ? 266 ARG A CA    1 1 
ATOM   2177 C  C     . ARG A 1 266 ? -2.064  24.166  -12.094 1 43.35  ? 266 ARG A C     1 1 
ATOM   2178 O  O     . ARG A 1 266 ? -3.107  24.81   -12.229 1 43.08  ? 266 ARG A O     1 1 
ATOM   2179 C  CB    . ARG A 1 266 ? -0.729  23.171  -14.057 1 44.8   ? 266 ARG A CB    1 1 
ATOM   2180 C  CG    . ARG A 1 266 ? -0.899  24.452  -14.851 1 48.75  ? 266 ARG A CG    1 1 
ATOM   2181 C  CD    . ARG A 1 266 ? 0.075   24.563  -16.018 1 52.43  ? 266 ARG A CD    1 1 
ATOM   2182 N  NE    . ARG A 1 266 ? 0.133   25.93   -16.546 1 55.07  ? 266 ARG A NE    1 1 
ATOM   2183 C  CZ    . ARG A 1 266 ? -0.471  26.337  -17.659 1 56.7   ? 266 ARG A CZ    1 1 
ATOM   2184 N  NH1   . ARG A 1 266 ? -1.175  25.482  -18.391 1 55.48  ? 266 ARG A NH1   1 1 
ATOM   2185 N  NH2   . ARG A 1 266 ? -0.369  27.6    -18.052 1 56.98  ? 266 ARG A NH2   1 1 
ATOM   2186 N  N     . ILE A 1 267 ? -1.163  24.472  -11.163 1 43.76  ? 267 ILE A N     1 1 
ATOM   2187 C  CA    . ILE A 1 267 ? -1.364  25.577  -10.222 1 44.71  ? 267 ILE A CA    1 1 
ATOM   2188 C  C     . ILE A 1 267 ? -1.561  26.95   -10.917 1 45.61  ? 267 ILE A C     1 1 
ATOM   2189 O  O     . ILE A 1 267 ? -2.225  27.834  -10.365 1 45.73  ? 267 ILE A O     1 1 
ATOM   2190 C  CB    . ILE A 1 267 ? -0.229  25.598  -9.169  1 45.07  ? 267 ILE A CB    1 1 
ATOM   2191 C  CG1   . ILE A 1 267 ? -0.64   26.356  -7.896  1 45.9   ? 267 ILE A CG1   1 1 
ATOM   2192 C  CG2   . ILE A 1 267 ? 1.069   26.114  -9.755  1 45.56  ? 267 ILE A CG2   1 1 
ATOM   2193 C  CD1   . ILE A 1 267 ? 0.213   26.067  -6.716  1 46.99  ? 267 ILE A CD1   1 1 
ATOM   2194 N  N     . THR A 1 268 ? -1.05   27.099  -12.148 1 45.92  ? 268 THR A N     1 1 
ATOM   2195 C  CA    . THR A 1 268 ? -1.169  28.35   -12.893 1 46.52  ? 268 THR A CA    1 1 
ATOM   2196 C  C     . THR A 1 268 ? -2.349  28.377  -13.88  1 46.72  ? 268 THR A C     1 1 
ATOM   2197 O  O     . THR A 1 268 ? -2.664  29.445  -14.401 1 47.07  ? 268 THR A O     1 1 
ATOM   2198 C  CB    . THR A 1 268 ? 0.162   28.689  -13.581 1 47.89  ? 268 THR A CB    1 1 
ATOM   2199 O  OG1   . THR A 1 268 ? 0.617   27.554  -14.325 1 49.06  ? 268 THR A OG1   1 1 
ATOM   2200 C  CG2   . THR A 1 268 ? 1.233   29.101  -12.589 1 48.13  ? 268 THR A CG2   1 1 
ATOM   2201 N  N     . ASN A 1 269 ? -2.989  27.23   -14.151 1 46.49  ? 269 ASN A N     1 1 
ATOM   2202 C  CA    . ASN A 1 269 ? -4.133  27.205  -15.066 1 47.02  ? 269 ASN A CA    1 1 
ATOM   2203 C  C     . ASN A 1 269 ? -5.439  26.816  -14.358 1 46.81  ? 269 ASN A C     1 1 
ATOM   2204 O  O     . ASN A 1 269 ? -6.368  26.332  -15.007 1 47.14  ? 269 ASN A O     1 1 
ATOM   2205 C  CB    . ASN A 1 269 ? -3.872  26.353  -16.338 1 48.95  ? 269 ASN A CB    1 1 
ATOM   2206 C  CG    . ASN A 1 269 ? -4.1    24.838  -16.284 1 53     ? 269 ASN A CG    1 1 
ATOM   2207 O  OD1   . ASN A 1 269 ? -4.642  24.269  -15.326 1 54.28  ? 269 ASN A OD1   1 1 
ATOM   2208 N  ND2   . ASN A 1 269 ? -3.685  24.138  -17.336 1 53.75  ? 269 ASN A ND2   1 1 
ATOM   2209 N  N     . LEU A 1 270 ? -5.52   27.042  -13.032 1 46.06  ? 270 LEU A N     1 1 
ATOM   2210 C  CA    . LEU A 1 270 ? -6.714  26.765  -12.235 1 45.72  ? 270 LEU A CA    1 1 
ATOM   2211 C  C     . LEU A 1 270 ? -7.84   27.678  -12.755 1 45.14  ? 270 LEU A C     1 1 
ATOM   2212 O  O     . LEU A 1 270 ? -7.622  28.878  -12.972 1 45.34  ? 270 LEU A O     1 1 
ATOM   2213 C  CB    . LEU A 1 270 ? -6.4    27.094  -10.768 1 45.92  ? 270 LEU A CB    1 1 
ATOM   2214 C  CG    . LEU A 1 270 ? -7.134  26.299  -9.709  1 47.4   ? 270 LEU A CG    1 1 
ATOM   2215 C  CD1   . LEU A 1 270 ? -6.86   24.822  -9.851  1 47.82  ? 270 LEU A CD1   1 1 
ATOM   2216 C  CD2   . LEU A 1 270 ? -6.742  26.778  -8.331  1 48.28  ? 270 LEU A CD2   1 1 
ATOM   2217 N  N     . PRO A 1 271 ? -9.017  27.114  -13.053 1 43.93  ? 271 PRO A N     1 1 
ATOM   2218 C  CA    . PRO A 1 271 ? -10.102 27.937  -13.611 1 43.17  ? 271 PRO A CA    1 1 
ATOM   2219 C  C     . PRO A 1 271 ? -10.574 29.06   -12.689 1 42.19  ? 271 PRO A C     1 1 
ATOM   2220 O  O     . PRO A 1 271 ? -11.007 30.112  -13.155 1 42.18  ? 271 PRO A O     1 1 
ATOM   2221 C  CB    . PRO A 1 271 ? -11.197 26.915  -13.9   1 44.09  ? 271 PRO A CB    1 1 
ATOM   2222 C  CG    . PRO A 1 271 ? -10.91  25.778  -12.974 1 44.6   ? 271 PRO A CG    1 1 
ATOM   2223 C  CD    . PRO A 1 271 ? -9.424  25.71   -12.89  1 43.19  ? 271 PRO A CD    1 1 
ATOM   2224 N  N     . SER A 1 272 ? -10.456 28.848  -11.38  1 41.33  ? 272 SER A N     1 1 
ATOM   2225 C  CA    . SER A 1 272 ? -10.833 29.825  -10.367 1 41.1   ? 272 SER A CA    1 1 
ATOM   2226 C  C     . SER A 1 272 ? -9.712  30.786  -9.99   1 40.43  ? 272 SER A C     1 1 
ATOM   2227 O  O     . SER A 1 272 ? -9.897  31.558  -9.056  1 40.33  ? 272 SER A O     1 1 
ATOM   2228 C  CB    . SER A 1 272 ? -11.296 29.108  -9.109  1 42.76  ? 272 SER A CB    1 1 
ATOM   2229 O  OG    . SER A 1 272 ? -10.307 28.185  -8.684  1 45.46  ? 272 SER A OG    1 1 
ATOM   2230 N  N     . LEU A 1 273 ? -8.548  30.737  -10.681 1 39.85  ? 273 LEU A N     1 1 
ATOM   2231 C  CA    . LEU A 1 273 ? -7.421  31.629  -10.4   1 39.65  ? 273 LEU A CA    1 1 
ATOM   2232 C  C     . LEU A 1 273 ? -7.854  33.044  -10.718 1 39.1   ? 273 LEU A C     1 1 
ATOM   2233 O  O     . LEU A 1 273 ? -8.454  33.285  -11.766 1 39.31  ? 273 LEU A O     1 1 
ATOM   2234 C  CB    . LEU A 1 273 ? -6.187  31.249  -11.233 1 39.86  ? 273 LEU A CB    1 1 
ATOM   2235 C  CG    . LEU A 1 273 ? -4.823  31.493  -10.582 1 41.07  ? 273 LEU A CG    1 1 
ATOM   2236 C  CD1   . LEU A 1 273 ? -4.613  30.583  -9.396  1 41.4   ? 273 LEU A CD1   1 1 
ATOM   2237 C  CD2   . LEU A 1 273 ? -3.709  31.261  -11.576 1 41.73  ? 273 LEU A CD2   1 1 
ATOM   2238 N  N     . GLY A 1 274 ? -7.644  33.94   -9.77   1 38.24  ? 274 GLY A N     1 1 
ATOM   2239 C  CA    . GLY A 1 274 ? -8.069  35.317  -9.933  1 37.86  ? 274 GLY A CA    1 1 
ATOM   2240 C  C     . GLY A 1 274 ? -9.174  35.729  -8.986  1 37.23  ? 274 GLY A C     1 1 
ATOM   2241 O  O     . GLY A 1 274 ? -9.409  36.929  -8.828  1 37.84  ? 274 GLY A O     1 1 
ATOM   2242 N  N     . ARG A 1 275 ? -9.862  34.759  -8.334  1 35.8   ? 275 ARG A N     1 1 
ATOM   2243 C  CA    . ARG A 1 275 ? -10.917 35.09   -7.357  1 34.96  ? 275 ARG A CA    1 1 
ATOM   2244 C  C     . ARG A 1 275 ? -10.405 35.899  -6.15   1 34.31  ? 275 ARG A C     1 1 
ATOM   2245 O  O     . ARG A 1 275 ? -11.194 36.492  -5.415  1 34.15  ? 275 ARG A O     1 1 
ATOM   2246 C  CB    . ARG A 1 275 ? -11.682 33.857  -6.909  1 35.81  ? 275 ARG A CB    1 1 
ATOM   2247 C  CG    . ARG A 1 275 ? -10.818 32.828  -6.257  1 37.86  ? 275 ARG A CG    1 1 
ATOM   2248 C  CD    . ARG A 1 275 ? -11.661 31.617  -5.96   1 40.03  ? 275 ARG A CD    1 1 
ATOM   2249 N  NE    . ARG A 1 275 ? -11.022 30.698  -5.021  1 42.04  ? 275 ARG A NE    1 1 
ATOM   2250 C  CZ    . ARG A 1 275 ? -10.965 30.885  -3.706  1 43.53  ? 275 ARG A CZ    1 1 
ATOM   2251 N  NH1   . ARG A 1 275 ? -11.451 31.997  -3.164  1 42.69  ? 275 ARG A NH1   1 1 
ATOM   2252 N  NH2   . ARG A 1 275 ? -10.388 29.981  -2.928  1 43.31  ? 275 ARG A NH2   1 1 
ATOM   2253 N  N     . PHE A 1 276 ? -9.082  35.903  -5.956  1 33.72  ? 276 PHE A N     1 1 
ATOM   2254 C  CA    . PHE A 1 276 ? -8.326  36.738  -5.047  1 33.6   ? 276 PHE A CA    1 1 
ATOM   2255 C  C     . PHE A 1 276 ? -7.032  37.135  -5.789  1 33.76  ? 276 PHE A C     1 1 
ATOM   2256 O  O     . PHE A 1 276 ? -6.529  36.375  -6.63   1 34.2   ? 276 PHE A O     1 1 
ATOM   2257 C  CB    . PHE A 1 276 ? -8.075  36.087  -3.676  1 33.3   ? 276 PHE A CB    1 1 
ATOM   2258 C  CG    . PHE A 1 276 ? -7.317  34.784  -3.677  1 33.9   ? 276 PHE A CG    1 1 
ATOM   2259 C  CD1   . PHE A 1 276 ? -5.935  34.768  -3.701  1 34.68  ? 276 PHE A CD1   1 1 
ATOM   2260 C  CD2   . PHE A 1 276 ? -7.982  33.579  -3.579  1 34.78  ? 276 PHE A CD2   1 1 
ATOM   2261 C  CE1   . PHE A 1 276 ? -5.24   33.57   -3.689  1 35.35  ? 276 PHE A CE1   1 1 
ATOM   2262 C  CE2   . PHE A 1 276 ? -7.283  32.382  -3.555  1 35.4   ? 276 PHE A CE2   1 1 
ATOM   2263 C  CZ    . PHE A 1 276 ? -5.917  32.386  -3.612  1 35.22  ? 276 PHE A CZ    1 1 
ATOM   2264 N  N     . LYS A 1 277 ? -6.535  38.347  -5.542  1 33.03  ? 277 LYS A N     1 1 
ATOM   2265 C  CA    . LYS A 1 277 ? -5.326  38.833  -6.214  1 32.48  ? 277 LYS A CA    1 1 
ATOM   2266 C  C     . LYS A 1 277 ? -4.067  38.581  -5.374  1 31.57  ? 277 LYS A C     1 1 
ATOM   2267 O  O     . LYS A 1 277 ? -4.163  38.071  -4.26   1 31.25  ? 277 LYS A O     1 1 
ATOM   2268 C  CB    . LYS A 1 277 ? -5.469  40.344  -6.527  1 34.08  ? 277 LYS A CB    1 1 
ATOM   2269 C  CG    . LYS A 1 277 ? -6.425  40.642  -7.661  1 37.84  ? 277 LYS A CG    1 1 
ATOM   2270 C  CD    . LYS A 1 277 ? -6.167  41.997  -8.261  1 42.11  ? 277 LYS A CD    1 1 
ATOM   2271 C  CE    . LYS A 1 277 ? -6.416  41.99   -9.748  1 46.29  ? 277 LYS A CE    1 1 
ATOM   2272 N  NZ    . LYS A 1 277 ? -6.799  43.334  -10.247 1 49.15  ? 277 LYS A NZ    1 1 
ATOM   2273 N  N     . PHE A 1 278 ? -2.878  38.894  -5.929  1 30.8   ? 278 PHE A N     1 1 
ATOM   2274 C  CA    . PHE A 1 278 ? -1.645  38.796  -5.171  1 30.17  ? 278 PHE A CA    1 1 
ATOM   2275 C  C     . PHE A 1 278 ? -1.45   40.212  -4.658  1 29.08  ? 278 PHE A C     1 1 
ATOM   2276 O  O     . PHE A 1 278 ? -1.313  41.156  -5.434  1 29.11  ? 278 PHE A O     1 1 
ATOM   2277 C  CB    . PHE A 1 278 ? -0.461  38.293  -6.02   1 30.05  ? 278 PHE A CB    1 1 
ATOM   2278 C  CG    . PHE A 1 278 ? 0.921   38.623  -5.489  1 30.82  ? 278 PHE A CG    1 1 
ATOM   2279 C  CD1   . PHE A 1 278 ? 1.245   38.406  -4.162  1 31.62  ? 278 PHE A CD1   1 1 
ATOM   2280 C  CD2   . PHE A 1 278 ? 1.911   39.097  -6.331  1 31.41  ? 278 PHE A CD2   1 1 
ATOM   2281 C  CE1   . PHE A 1 278 ? 2.511   38.724  -3.678  1 32.03  ? 278 PHE A CE1   1 1 
ATOM   2282 C  CE2   . PHE A 1 278 ? 3.187   39.368  -5.85   1 31.83  ? 278 PHE A CE2   1 1 
ATOM   2283 C  CZ    . PHE A 1 278 ? 3.477   39.184  -4.526  1 31.62  ? 278 PHE A CZ    1 1 
ATOM   2284 N  N     . ARG A 1 279 ? -1.558  40.359  -3.345  1 27.88  ? 279 ARG A N     1 1 
ATOM   2285 C  CA    . ARG A 1 279 ? -1.432  41.623  -2.661  1 27.17  ? 279 ARG A CA    1 1 
ATOM   2286 C  C     . ARG A 1 279 ? -0.381  41.495  -1.581  1 25.53  ? 279 ARG A C     1 1 
ATOM   2287 O  O     . ARG A 1 279 ? -0.693  41.087  -0.463  1 25.54  ? 279 ARG A O     1 1 
ATOM   2288 C  CB    . ARG A 1 279 ? -2.787  42.017  -2.064  1 29.04  ? 279 ARG A CB    1 1 
ATOM   2289 C  CG    . ARG A 1 279 ? -3.887  42.086  -3.12   1 32.95  ? 279 ARG A CG    1 1 
ATOM   2290 C  CD    . ARG A 1 279 ? -5.107  42.829  -2.637  1 36.9   ? 279 ARG A CD    1 1 
ATOM   2291 N  NE    . ARG A 1 279 ? -6.147  42.911  -3.666  1 40.08  ? 279 ARG A NE    1 1 
ATOM   2292 C  CZ    . ARG A 1 279 ? -6.303  43.937  -4.498  1 41.52  ? 279 ARG A CZ    1 1 
ATOM   2293 N  NH1   . ARG A 1 279 ? -5.479  44.979  -4.443  1 39.98  ? 279 ARG A NH1   1 1 
ATOM   2294 N  NH2   . ARG A 1 279 ? -7.283  43.929  -5.392  1 41.62  ? 279 ARG A NH2   1 1 
ATOM   2295 N  N     . LYS A 1 280 ? 0.87    41.817  -1.934  1 24.12  ? 280 LYS A N     1 1 
ATOM   2296 C  CA    . LYS A 1 280 ? 2.027   41.768  -1.035  1 23.31  ? 280 LYS A CA    1 1 
ATOM   2297 C  C     . LYS A 1 280 ? 1.921   42.801  0.095   1 22.51  ? 280 LYS A C     1 1 
ATOM   2298 O  O     . LYS A 1 280 ? 1.651   43.985  -0.14   1 22.48  ? 280 LYS A O     1 1 
ATOM   2299 C  CB    . LYS A 1 280 ? 3.35    41.94   -1.829  1 24.06  ? 280 LYS A CB    1 1 
ATOM   2300 C  CG    . LYS A 1 280 ? 4.61    42.216  -0.993  1 26.17  ? 280 LYS A CG    1 1 
ATOM   2301 C  CD    . LYS A 1 280 ? 5.239   40.987  -0.359  1 28.34  ? 280 LYS A CD    1 1 
ATOM   2302 C  CE    . LYS A 1 280 ? 6.381   41.398  0.529   1 30.83  ? 280 LYS A CE    1 1 
ATOM   2303 N  NZ    . LYS A 1 280 ? 7.218   40.254  0.954   1 33.06  ? 280 LYS A NZ    1 1 
ATOM   2304 N  N     . LYS A 1 281 ? 2.136   42.337  1.325   1 21.59  ? 281 LYS A N     1 1 
ATOM   2305 C  CA    . LYS A 1 281 ? 2.102   43.207  2.479   1 21.37  ? 281 LYS A CA    1 1 
ATOM   2306 C  C     . LYS A 1 281 ? 3.505   43.73   2.731   1 21.29  ? 281 LYS A C     1 1 
ATOM   2307 O  O     . LYS A 1 281 ? 4.433   42.935  2.957   1 21.49  ? 281 LYS A O     1 1 
ATOM   2308 C  CB    . LYS A 1 281 ? 1.609   42.435  3.708   1 23.15  ? 281 LYS A CB    1 1 
ATOM   2309 C  CG    . LYS A 1 281 ? 0.139   42.03   3.655   1 27.06  ? 281 LYS A CG    1 1 
ATOM   2310 C  CD    . LYS A 1 281 ? -0.234  41.251  4.902   1 30.89  ? 281 LYS A CD    1 1 
ATOM   2311 C  CE    . LYS A 1 281 ? -1.717  41.021  5.028   1 34.09  ? 281 LYS A CE    1 1 
ATOM   2312 N  NZ    . LYS A 1 281 ? -2.06   40.367  6.321   1 36.31  ? 281 LYS A NZ    1 1 
ATOM   2313 N  N     . ILE A 1 282 ? 3.681   45.066  2.656   1 20.61  ? 282 ILE A N     1 1 
ATOM   2314 C  CA    . ILE A 1 282 ? 4.977   45.697  2.944   1 19.92  ? 282 ILE A CA    1 1 
ATOM   2315 C  C     . ILE A 1 282 ? 4.794   46.648  4.13    1 20.21  ? 282 ILE A C     1 1 
ATOM   2316 O  O     . ILE A 1 282 ? 3.892   47.49   4.107   1 20.02  ? 282 ILE A O     1 1 
ATOM   2317 C  CB    . ILE A 1 282 ? 5.622   46.418  1.729   1 19.19  ? 282 ILE A CB    1 1 
ATOM   2318 C  CG1   . ILE A 1 282 ? 5.738   45.496  0.511   1 19.3   ? 282 ILE A CG1   1 1 
ATOM   2319 C  CG2   . ILE A 1 282 ? 6.98    46.977  2.112   1 19.18  ? 282 ILE A CG2   1 1 
ATOM   2320 C  CD1   . ILE A 1 282 ? 6.147   46.186  -0.743  1 19.94  ? 282 ILE A CD1   1 1 
ATOM   2321 N  N     . ALA A 1 283 ? 5.611   46.477  5.187   1 20.6   ? 283 ALA A N     1 1 
ATOM   2322 C  CA    . ALA A 1 283 ? 5.551   47.333  6.366   1 21.77  ? 283 ALA A CA    1 1 
ATOM   2323 C  C     . ALA A 1 283 ? 5.979   48.736  5.961   1 23.35  ? 283 ALA A C     1 1 
ATOM   2324 O  O     . ALA A 1 283 ? 6.857   48.884  5.105   1 24.03  ? 283 ALA A O     1 1 
ATOM   2325 C  CB    . ALA A 1 283 ? 6.482   46.808  7.431   1 21.84  ? 283 ALA A CB    1 1 
ATOM   2326 N  N     . GLU A 1 284 ? 5.38    49.774  6.568   1 23.54  ? 284 GLU A N     1 1 
ATOM   2327 C  CA    . GLU A 1 284 ? 5.673   51.157  6.209   1 24.14  ? 284 GLU A CA    1 1 
ATOM   2328 C  C     . GLU A 1 284 ? 7.137   51.481  6.316   1 24.45  ? 284 GLU A C     1 1 
ATOM   2329 O  O     . GLU A 1 284 ? 7.708   51.997  5.363   1 25.02  ? 284 GLU A O     1 1 
ATOM   2330 C  CB    . GLU A 1 284 ? 4.827   52.131  7.035   1 27.08  ? 284 GLU A CB    1 1 
ATOM   2331 C  CG    . GLU A 1 284 ? 5.036   53.579  6.643   1 32.95  ? 284 GLU A CG    1 1 
ATOM   2332 C  CD    . GLU A 1 284 ? 4.03    54.525  7.256   1 42.01  ? 284 GLU A CD    1 1 
ATOM   2333 O  OE1   . GLU A 1 284 ? 2.901   54.081  7.572   1 44.6   ? 284 GLU A OE1   1 1 
ATOM   2334 O  OE2   . GLU A 1 284 ? 4.364   55.721  7.404   1 45.14  ? 284 GLU A OE2   1 1 
ATOM   2335 N  N     . LYS A 1 285 ? 7.773   51.051  7.412   1 24.04  ? 285 LYS A N     1 1 
ATOM   2336 C  CA    . LYS A 1 285 ? 9.194   51.269  7.662   1 23.9   ? 285 LYS A CA    1 1 
ATOM   2337 C  C     . LYS A 1 285 ? 10.112  50.7    6.569   1 24.7   ? 285 LYS A C     1 1 
ATOM   2338 O  O     . LYS A 1 285 ? 11.246  51.162  6.417   1 25.26  ? 285 LYS A O     1 1 
ATOM   2339 C  CB    . LYS A 1 285 ? 9.574   50.724  9.049   1 24.91  ? 285 LYS A CB    1 1 
ATOM   2340 C  CG    . LYS A 1 285 ? 9.407   49.219  9.184   1 28.99  ? 285 LYS A CG    1 1 
ATOM   2341 C  CD    . LYS A 1 285 ? 9.677   48.722  10.59   1 33.44  ? 285 LYS A CD    1 1 
ATOM   2342 C  CE    . LYS A 1 285 ? 9.572   47.218  10.671  1 37.13  ? 285 LYS A CE    1 1 
ATOM   2343 N  NZ    . LYS A 1 285 ? 9.936   46.714  12.015  1 39.76  ? 285 LYS A NZ    1 1 
ATOM   2344 N  N     . SER A 1 286 ? 9.626   49.721  5.795   1 24.76  ? 286 SER A N     1 1 
ATOM   2345 C  CA    . SER A 1 286 ? 10.397  49.085  4.725   1 25.21  ? 286 SER A CA    1 1 
ATOM   2346 C  C     . SER A 1 286 ? 10.354  49.857  3.403   1 25.34  ? 286 SER A C     1 1 
ATOM   2347 O  O     . SER A 1 286 ? 11.231  49.659  2.558   1 25.36  ? 286 SER A O     1 1 
ATOM   2348 C  CB    . SER A 1 286 ? 9.889   47.668  4.479   1 26.55  ? 286 SER A CB    1 1 
ATOM   2349 O  OG    . SER A 1 286 ? 9.84    46.909  5.674   1 29.16  ? 286 SER A OG    1 1 
ATOM   2350 N  N     . LEU A 1 287 ? 9.325   50.699  3.201   1 25.15  ? 287 LEU A N     1 1 
ATOM   2351 C  CA    . LEU A 1 287 ? 9.162   51.43   1.952   1 25.8   ? 287 LEU A CA    1 1 
ATOM   2352 C  C     . LEU A 1 287 ? 10.266  52.46   1.661   1 27.23  ? 287 LEU A C     1 1 
ATOM   2353 O  O     . LEU A 1 287 ? 10.761  53.144  2.56    1 27.55  ? 287 LEU A O     1 1 
ATOM   2354 C  CB    . LEU A 1 287 ? 7.783   52.077  1.888   1 25.55  ? 287 LEU A CB    1 1 
ATOM   2355 C  CG    . LEU A 1 287 ? 6.623   51.103  1.865   1 26.3   ? 287 LEU A CG    1 1 
ATOM   2356 C  CD1   . LEU A 1 287 ? 5.309   51.827  2.024   1 26.56  ? 287 LEU A CD1   1 1 
ATOM   2357 C  CD2   . LEU A 1 287 ? 6.624   50.312  0.584   1 26.79  ? 287 LEU A CD2   1 1 
ATOM   2358 N  N     . SER A 1 288 ? 10.657  52.533  0.385   1 27.86  ? 288 SER A N     1 1 
ATOM   2359 C  CA    . SER A 1 288 ? 11.686  53.424  -0.167  1 28.74  ? 288 SER A CA    1 1 
ATOM   2360 C  C     . SER A 1 288 ? 11.557  53.447  -1.711  1 29.07  ? 288 SER A C     1 1 
ATOM   2361 O  O     . SER A 1 288 ? 10.777  52.68   -2.27   1 29.24  ? 288 SER A O     1 1 
ATOM   2362 C  CB    . SER A 1 288 ? 13.077  52.935  0.229   1 30.26  ? 288 SER A CB    1 1 
ATOM   2363 O  OG    . SER A 1 288 ? 13.371  51.712  -0.427  1 33.08  ? 288 SER A OG    1 1 
ATOM   2364 N  N     . GLY A 1 289 ? 12.286  54.338  -2.387  1 28.82  ? 289 GLY A N     1 1 
ATOM   2365 C  CA    . GLY A 1 289 ? 12.272  54.447  -3.847  1 28.93  ? 289 GLY A CA    1 1 
ATOM   2366 C  C     . GLY A 1 289 ? 10.892  54.436  -4.47   1 28.58  ? 289 GLY A C     1 1 
ATOM   2367 O  O     . GLY A 1 289 ? 9.992   55.107  -3.971  1 29.02  ? 289 GLY A O     1 1 
ATOM   2368 N  N     . LYS A 1 290 ? 10.692  53.626  -5.508  1 27.8   ? 290 LYS A N     1 1 
ATOM   2369 C  CA    . LYS A 1 290 ? 9.376   53.494  -6.133  1 27.71  ? 290 LYS A CA    1 1 
ATOM   2370 C  C     . LYS A 1 290 ? 8.708   52.157  -5.751  1 27.62  ? 290 LYS A C     1 1 
ATOM   2371 O  O     . LYS A 1 290 ? 7.896   51.626  -6.52   1 27.49  ? 290 LYS A O     1 1 
ATOM   2372 C  CB    . LYS A 1 290 ? 9.497   53.627  -7.656  1 29.2   ? 290 LYS A CB    1 1 
ATOM   2373 C  CG    . LYS A 1 290 ? 10.059  54.969  -8.089  1 32.38  ? 290 LYS A CG    1 1 
ATOM   2374 C  CD    . LYS A 1 290 ? 10.548  54.969  -9.525  1 36.11  ? 290 LYS A CD    1 1 
ATOM   2375 C  CE    . LYS A 1 290 ? 11.024  56.347  -9.908  1 40.23  ? 290 LYS A CE    1 1 
ATOM   2376 N  NZ    . LYS A 1 290 ? 11.822  56.351  -11.165 1 43.03  ? 290 LYS A NZ    1 1 
ATOM   2377 N  N     . VAL A 1 291 ? 9.049   51.625  -4.56   1 27.42  ? 291 VAL A N     1 1 
ATOM   2378 C  CA    . VAL A 1 291 ? 8.546   50.349  -4.076  1 27.78  ? 291 VAL A CA    1 1 
ATOM   2379 C  C     . VAL A 1 291 ? 7.033   50.345  -3.974  1 28.15  ? 291 VAL A C     1 1 
ATOM   2380 O  O     . VAL A 1 291 ? 6.41    49.435  -4.527  1 28.5   ? 291 VAL A O     1 1 
ATOM   2381 C  CB    . VAL A 1 291 ? 9.24    49.896  -2.768  1 28.1   ? 291 VAL A CB    1 1 
ATOM   2382 C  CG1   . VAL A 1 291 ? 8.568   48.668  -2.171  1 28.5   ? 291 VAL A CG1   1 1 
ATOM   2383 C  CG2   . VAL A 1 291 ? 10.716  49.624  -3.018  1 28.45  ? 291 VAL A CG2   1 1 
ATOM   2384 N  N     . LYS A 1 292 ? 6.431   51.376  -3.353  1 27.88  ? 292 LYS A N     1 1 
ATOM   2385 C  CA    . LYS A 1 292 ? 4.977   51.417  -3.242  1 28.38  ? 292 LYS A CA    1 1 
ATOM   2386 C  C     . LYS A 1 292 ? 4.297   51.433  -4.61   1 29.37  ? 292 LYS A C     1 1 
ATOM   2387 O  O     . LYS A 1 292 ? 3.351   50.666  -4.816  1 29.49  ? 292 LYS A O     1 1 
ATOM   2388 C  CB    . LYS A 1 292 ? 4.48    52.559  -2.34   1 29.6   ? 292 LYS A CB    1 1 
ATOM   2389 C  CG    . LYS A 1 292 ? 2.951   52.584  -2.214  1 33.04  ? 292 LYS A CG    1 1 
ATOM   2390 C  CD    . LYS A 1 292 ? 2.437   53.28   -0.961  1 37.06  ? 292 LYS A CD    1 1 
ATOM   2391 C  CE    . LYS A 1 292 ? 0.942   53.125  -0.792  1 40.12  ? 292 LYS A CE    1 1 
ATOM   2392 N  NZ    . LYS A 1 292 ? 0.538   51.691  -0.716  1 42.05  ? 292 LYS A NZ    1 1 
ATOM   2393 N  N     . GLU A 1 293 ? 4.833   52.218  -5.574  1 29.86  ? 293 GLU A N     1 1 
ATOM   2394 C  CA    . GLU A 1 293 ? 4.218   52.262  -6.904  1 30.65  ? 293 GLU A CA    1 1 
ATOM   2395 C  C     . GLU A 1 293 ? 4.4     50.941  -7.66   1 30.67  ? 293 GLU A C     1 1 
ATOM   2396 O  O     . GLU A 1 293 ? 3.479   50.52   -8.362  1 30.56  ? 293 GLU A O     1 1 
ATOM   2397 C  CB    . GLU A 1 293 ? 4.647   53.49   -7.733  1 33.09  ? 293 GLU A CB    1 1 
ATOM   2398 C  CG    . GLU A 1 293 ? 3.838   53.683  -9.02   1 39.59  ? 293 GLU A CG    1 1 
ATOM   2399 C  CD    . GLU A 1 293 ? 2.334   53.383  -9.055  1 46.46  ? 293 GLU A CD    1 1 
ATOM   2400 O  OE1   . GLU A 1 293 ? 1.915   52.605  -9.944  1 48.28  ? 293 GLU A OE1   1 1 
ATOM   2401 O  OE2   . GLU A 1 293 ? 1.572   53.93   -8.221  1 47.28  ? 293 GLU A OE2   1 1 
ATOM   2402 N  N     . PHE A 1 294 ? 5.52    50.223  -7.429  1 30.48  ? 294 PHE A N     1 1 
ATOM   2403 C  CA    . PHE A 1 294 ? 5.701   48.906  -8.044  1 30.54  ? 294 PHE A CA    1 1 
ATOM   2404 C  C     . PHE A 1 294 ? 4.654   47.948  -7.489  1 30.35  ? 294 PHE A C     1 1 
ATOM   2405 O  O     . PHE A 1 294 ? 4.012   47.235  -8.256  1 30.54  ? 294 PHE A O     1 1 
ATOM   2406 C  CB    . PHE A 1 294 ? 7.106   48.336  -7.798  1 30.56  ? 294 PHE A CB    1 1 
ATOM   2407 C  CG    . PHE A 1 294 ? 7.26    46.935  -8.347  1 31.35  ? 294 PHE A CG    1 1 
ATOM   2408 C  CD1   . PHE A 1 294 ? 7.47    46.722  -9.696  1 32.27  ? 294 PHE A CD1   1 1 
ATOM   2409 C  CD2   . PHE A 1 294 ? 7.137   45.833  -7.523  1 32.23  ? 294 PHE A CD2   1 1 
ATOM   2410 C  CE1   . PHE A 1 294 ? 7.585   45.434  -10.203 1 32.94  ? 294 PHE A CE1   1 1 
ATOM   2411 C  CE2   . PHE A 1 294 ? 7.252   44.548  -8.035  1 32.93  ? 294 PHE A CE2   1 1 
ATOM   2412 C  CZ    . PHE A 1 294 ? 7.489   44.357  -9.368  1 32.67  ? 294 PHE A CZ    1 1 
ATOM   2413 N  N     . ASN A 1 295 ? 4.422   47.98   -6.17   1 29.91  ? 295 ASN A N     1 1 
ATOM   2414 C  CA    . ASN A 1 295 ? 3.42    47.118  -5.552  1 30.1   ? 295 ASN A CA    1 1 
ATOM   2415 C  C     . ASN A 1 295 ? 2.043   47.376  -6.132  1 29.93  ? 295 ASN A C     1 1 
ATOM   2416 O  O     . ASN A 1 295 ? 1.314   46.426  -6.395  1 30.37  ? 295 ASN A O     1 1 
ATOM   2417 C  CB    . ASN A 1 295 ? 3.404   47.257  -4.032  1 31.42  ? 295 ASN A CB    1 1 
ATOM   2418 C  CG    . ASN A 1 295 ? 2.889   46.012  -3.329  1 34.78  ? 295 ASN A CG    1 1 
ATOM   2419 O  OD1   . ASN A 1 295 ? 2.678   44.949  -3.937  1 35.64  ? 295 ASN A OD1   1 1 
ATOM   2420 N  ND2   . ASN A 1 295 ? 2.675   46.112  -2.025  1 35.65  ? 295 ASN A ND2   1 1 
ATOM   2421 N  N     . ASN A 1 296 ? 1.725   48.642  -6.423  1 29.15  ? 296 ASN A N     1 1 
ATOM   2422 C  CA    . ASN A 1 296 ? 0.451   48.98   -7.043  1 29.03  ? 296 ASN A CA    1 1 
ATOM   2423 C  C     . ASN A 1 296 ? 0.355   48.385  -8.449  1 27.97  ? 296 ASN A C     1 1 
ATOM   2424 O  O     . ASN A 1 296 ? -0.706  47.897  -8.822  1 27.78  ? 296 ASN A O     1 1 
ATOM   2425 C  CB    . ASN A 1 296 ? 0.244   50.492  -7.084  1 31.1   ? 296 ASN A CB    1 1 
ATOM   2426 C  CG    . ASN A 1 296 ? 0.252   51.178  -5.734  1 35.56  ? 296 ASN A CG    1 1 
ATOM   2427 O  OD1   . ASN A 1 296 ? 0.672   52.345  -5.61   1 37.36  ? 296 ASN A OD1   1 1 
ATOM   2428 N  ND2   . ASN A 1 296 ? -0.198  50.477  -4.69   1 36.04  ? 296 ASN A ND2   1 1 
ATOM   2429 N  N     . ILE A 1 297 ? 1.463   48.389  -9.212  1 27.2   ? 297 ILE A N     1 1 
ATOM   2430 C  CA    . ILE A 1 297 ? 1.492   47.809  -10.557 1 26.99  ? 297 ILE A CA    1 1 
ATOM   2431 C  C     . ILE A 1 297 ? 1.241   46.32   -10.483 1 27.07  ? 297 ILE A C     1 1 
ATOM   2432 O  O     . ILE A 1 297 ? 0.408   45.803  -11.233 1 27.33  ? 297 ILE A O     1 1 
ATOM   2433 C  CB    . ILE A 1 297 ? 2.788   48.139  -11.318 1 27.11  ? 297 ILE A CB    1 1 
ATOM   2434 C  CG1   . ILE A 1 297 ? 2.865   49.644  -11.605 1 28.03  ? 297 ILE A CG1   1 1 
ATOM   2435 C  CG2   . ILE A 1 297 ? 2.902   47.327  -12.613 1 27.19  ? 297 ILE A CG2   1 1 
ATOM   2436 C  CD1   . ILE A 1 297 ? 4.215   50.098  -12.015 1 29.23  ? 297 ILE A CD1   1 1 
ATOM   2437 N  N     . VAL A 1 298 ? 1.891   45.635  -9.533  1 26.51  ? 298 VAL A N     1 1 
ATOM   2438 C  CA    . VAL A 1 298 ? 1.648   44.204  -9.344  1 26.55  ? 298 VAL A CA    1 1 
ATOM   2439 C  C     . VAL A 1 298 ? 0.155   43.915  -9.028  1 26.63  ? 298 VAL A C     1 1 
ATOM   2440 O  O     . VAL A 1 298 ? -0.485  43.13   -9.725  1 26.87  ? 298 VAL A O     1 1 
ATOM   2441 C  CB    . VAL A 1 298 ? 2.578   43.604  -8.271  1 26.89  ? 298 VAL A CB    1 1 
ATOM   2442 C  CG1   . VAL A 1 298 ? 2.214   42.156  -8.004  1 27.55  ? 298 VAL A CG1   1 1 
ATOM   2443 C  CG2   . VAL A 1 298 ? 4.026   43.709  -8.7    1 27.06  ? 298 VAL A CG2   1 1 
ATOM   2444 N  N     . GLN A 1 299 ? -0.403  44.615  -8.031  1 26.04  ? 299 GLN A N     1 1 
ATOM   2445 C  CA    . GLN A 1 299 ? -1.789  44.439  -7.623  1 26.01  ? 299 GLN A CA    1 1 
ATOM   2446 C  C     . GLN A 1 299 ? -2.807  44.809  -8.711  1 26.74  ? 299 GLN A C     1 1 
ATOM   2447 O  O     . GLN A 1 299 ? -3.959  44.409  -8.624  1 26.79  ? 299 GLN A O     1 1 
ATOM   2448 C  CB    . GLN A 1 299 ? -2.052  45.197  -6.314  1 26.61  ? 299 GLN A CB    1 1 
ATOM   2449 C  CG    . GLN A 1 299 ? -1.118  44.753  -5.188  1 27.67  ? 299 GLN A CG    1 1 
ATOM   2450 C  CD    . GLN A 1 299 ? -1.504  45.242  -3.81   1 29.38  ? 299 GLN A CD    1 1 
ATOM   2451 O  OE1   . GLN A 1 299 ? -2.657  45.574  -3.535  1 30.88  ? 299 GLN A OE1   1 1 
ATOM   2452 N  NE2   . GLN A 1 299 ? -0.551  45.266  -2.9    1 28.54  ? 299 GLN A NE2   1 1 
ATOM   2453 N  N     . ARG A 1 300 ? -2.38   45.534  -9.747  1 27.27  ? 300 ARG A N     1 1 
ATOM   2454 C  CA    . ARG A 1 300 ? -3.218  45.933  -10.874 1 28.05  ? 300 ARG A CA    1 1 
ATOM   2455 C  C     . ARG A 1 300 ? -3.424  44.755  -11.851 1 28.78  ? 300 ARG A C     1 1 
ATOM   2456 O  O     . ARG A 1 300 ? -4.479  44.676  -12.49  1 28.97  ? 300 ARG A O     1 1 
ATOM   2457 C  CB    . ARG A 1 300 ? -2.543  47.113  -11.592 1 29.36  ? 300 ARG A CB    1 1 
ATOM   2458 C  CG    . ARG A 1 300 ? -3.348  47.772  -12.685 1 32.17  ? 300 ARG A CG    1 1 
ATOM   2459 C  CD    . ARG A 1 300 ? -2.593  48.952  -13.274 1 35.08  ? 300 ARG A CD    1 1 
ATOM   2460 N  NE    . ARG A 1 300 ? -2.34   50.011  -12.292 1 37.79  ? 300 ARG A NE    1 1 
ATOM   2461 C  CZ    . ARG A 1 300 ? -1.249  50.781  -12.28  1 39.81  ? 300 ARG A CZ    1 1 
ATOM   2462 N  NH1   . ARG A 1 300 ? -0.302  50.617  -13.195 1 39.15  ? 300 ARG A NH1   1 1 
ATOM   2463 N  NH2   . ARG A 1 300 ? -1.107  51.73   -11.362 1 39.47  ? 300 ARG A NH2   1 1 
ATOM   2464 N  N     . TYR A 1 301 ? -2.436  43.821  -11.95  1 28.96  ? 301 TYR A N     1 1 
ATOM   2465 C  CA    . TYR A 1 301 ? -2.504  42.702  -12.905 1 29.43  ? 301 TYR A CA    1 1 
ATOM   2466 C  C     . TYR A 1 301 ? -2.384  41.289  -12.347 1 30.13  ? 301 TYR A C     1 1 
ATOM   2467 O  O     . TYR A 1 301 ? -2.495  40.333  -13.113 1 30.27  ? 301 TYR A O     1 1 
ATOM   2468 C  CB    . TYR A 1 301 ? -1.406  42.854  -13.959 1 29.15  ? 301 TYR A CB    1 1 
ATOM   2469 C  CG    . TYR A 1 301 ? -1.432  44.178  -14.676 1 29.72  ? 301 TYR A CG    1 1 
ATOM   2470 C  CD1   . TYR A 1 301 ? -2.341  44.421  -15.696 1 30.41  ? 301 TYR A CD1   1 1 
ATOM   2471 C  CD2   . TYR A 1 301 ? -0.538  45.182  -14.348 1 30.56  ? 301 TYR A CD2   1 1 
ATOM   2472 C  CE1   . TYR A 1 301 ? -2.37   45.637  -16.358 1 31.04  ? 301 TYR A CE1   1 1 
ATOM   2473 C  CE2   . TYR A 1 301 ? -0.561  46.402  -15     1 31.45  ? 301 TYR A CE2   1 1 
ATOM   2474 C  CZ    . TYR A 1 301 ? -1.474  46.622  -16.01  1 32.31  ? 301 TYR A CZ    1 1 
ATOM   2475 O  OH    . TYR A 1 301 ? -1.484  47.821  -16.663 1 34.47  ? 301 TYR A OH    1 1 
ATOM   2476 N  N     . SER A 1 302 ? -2.092  41.142  -11.061 1 30.41  ? 302 SER A N     1 1 
ATOM   2477 C  CA    . SER A 1 302 ? -1.848  39.832  -10.477 1 31.03  ? 302 SER A CA    1 1 
ATOM   2478 C  C     . SER A 1 302 ? -3.074  39.028  -10.138 1 31.86  ? 302 SER A C     1 1 
ATOM   2479 O  O     . SER A 1 302 ? -4.134  39.578  -9.881  1 32.03  ? 302 SER A O     1 1 
ATOM   2480 C  CB    . SER A 1 302 ? -0.975  39.969  -9.233  1 31.96  ? 302 SER A CB    1 1 
ATOM   2481 O  OG    . SER A 1 302 ? -1.703  40.588  -8.184  1 33.48  ? 302 SER A OG    1 1 
ATOM   2482 N  N     . VAL A 1 303 ? -2.907  37.701  -10.131 1 32.37  ? 303 VAL A N     1 1 
ATOM   2483 C  CA    . VAL A 1 303 ? -3.864  36.699  -9.669  1 33.01  ? 303 VAL A CA    1 1 
ATOM   2484 C  C     . VAL A 1 303 ? -3.132  35.95   -8.544  1 33.62  ? 303 VAL A C     1 1 
ATOM   2485 O  O     . VAL A 1 303 ? -1.916  35.723  -8.622  1 33.8   ? 303 VAL A O     1 1 
ATOM   2486 C  CB    . VAL A 1 303 ? -4.414  35.76   -10.773 1 33.53  ? 303 VAL A CB    1 1 
ATOM   2487 C  CG1   . VAL A 1 303 ? -5.233  36.547  -11.783 1 34.15  ? 303 VAL A CG1   1 1 
ATOM   2488 C  CG2   . VAL A 1 303 ? -3.303  34.988  -11.47  1 33.77  ? 303 VAL A CG2   1 1 
ATOM   2489 N  N     . GLY A 1 304 ? -3.844  35.671  -7.466  1 33.74  ? 304 GLY A N     1 1 
ATOM   2490 C  CA    . GLY A 1 304 ? -3.248  35.038  -6.3    1 34.31  ? 304 GLY A CA    1 1 
ATOM   2491 C  C     . GLY A 1 304 ? -2.777  33.617  -6.523  1 34.62  ? 304 GLY A C     1 1 
ATOM   2492 O  O     . GLY A 1 304 ? -3.443  32.834  -7.208  1 35     ? 304 GLY A O     1 1 
ATOM   2493 N  N     . LEU A 1 305 ? -1.619  33.274  -5.949  1 34.2   ? 305 LEU A N     1 1 
ATOM   2494 C  CA    . LEU A 1 305 ? -1.1    31.919  -6.047  1 34.37  ? 305 LEU A CA    1 1 
ATOM   2495 C  C     . LEU A 1 305 ? -1.153  31.287  -4.65   1 34.38  ? 305 LEU A C     1 1 
ATOM   2496 O  O     . LEU A 1 305 ? -0.299  31.606  -3.819  1 34.67  ? 305 LEU A O     1 1 
ATOM   2497 C  CB    . LEU A 1 305 ? 0.331   31.927  -6.579  1 34.48  ? 305 LEU A CB    1 1 
ATOM   2498 C  CG    . LEU A 1 305 ? 0.899   30.55   -6.887  1 36.05  ? 305 LEU A CG    1 1 
ATOM   2499 C  CD1   . LEU A 1 305 ? 0.182   29.914  -8.056  1 36.51  ? 305 LEU A CD1   1 1 
ATOM   2500 C  CD2   . LEU A 1 305 ? 2.375   30.637  -7.181  1 37.1   ? 305 LEU A CD2   1 1 
ATOM   2501 N  N     . ALA A 1 306 ? -2.186  30.427  -4.377  1 33.58  ? 306 ALA A N     1 1 
ATOM   2502 C  CA    . ALA A 1 306 ? -2.451  29.741  -3.097  1 33.24  ? 306 ALA A CA    1 1 
ATOM   2503 C  C     . ALA A 1 306 ? -3.024  30.673  -2.029  1 32.53  ? 306 ALA A C     1 1 
ATOM   2504 O  O     . ALA A 1 306 ? -4.008  30.331  -1.394  1 32.41  ? 306 ALA A O     1 1 
ATOM   2505 C  CB    . ALA A 1 306 ? -1.207  29.018  -2.573  1 33.68  ? 306 ALA A CB    1 1 
ATOM   2506 N  N     . SER A 1 307 ? -2.407  31.844  -1.819  1 31.92  ? 307 SER A N     1 1 
ATOM   2507 C  CA    . SER A 1 307 ? -2.871  32.837  -0.85   1 31.53  ? 307 SER A CA    1 1 
ATOM   2508 C  C     . SER A 1 307 ? -2.616  34.234  -1.384  1 30.82  ? 307 SER A C     1 1 
ATOM   2509 O  O     . SER A 1 307 ? -1.583  34.482  -2.017  1 30.89  ? 307 SER A O     1 1 
ATOM   2510 C  CB    . SER A 1 307 ? -2.161  32.666  0.487   1 32.64  ? 307 SER A CB    1 1 
ATOM   2511 O  OG    . SER A 1 307 ? -2.564  31.477  1.147   1 34.66  ? 307 SER A OG    1 1 
ATOM   2512 N  N     . SER A 1 308 ? -3.539  35.156  -1.114  1 29.92  ? 308 SER A N     1 1 
ATOM   2513 C  CA    . SER A 1 308 ? -3.392  36.529  -1.582  1 29.49  ? 308 SER A CA    1 1 
ATOM   2514 C  C     . SER A 1 308 ? -2.209  37.242  -0.948  1 28.83  ? 308 SER A C     1 1 
ATOM   2515 O  O     . SER A 1 308 ? -1.642  38.126  -1.575  1 29.05  ? 308 SER A O     1 1 
ATOM   2516 C  CB    . SER A 1 308 ? -4.664  37.326  -1.325  1 30.77  ? 308 SER A CB    1 1 
ATOM   2517 O  OG    . SER A 1 308 ? -4.847  37.556  0.06    1 33.4   ? 308 SER A OG    1 1 
ATOM   2518 N  N     . ASP A 1 309 ? -1.833  36.87   0.283   1 27.98  ? 309 ASP A N     1 1 
ATOM   2519 C  CA    . ASP A 1 309 ? -0.742  37.542  0.958   1 27.69  ? 309 ASP A CA    1 1 
ATOM   2520 C  C     . ASP A 1 309 ? 0.546   36.736  1.057   1 26.76  ? 309 ASP A C     1 1 
ATOM   2521 O  O     . ASP A 1 309 ? 1.436   37.153  1.798   1 27.55  ? 309 ASP A O     1 1 
ATOM   2522 C  CB    . ASP A 1 309 ? -1.164  38.062  2.326   1 30.19  ? 309 ASP A CB    1 1 
ATOM   2523 C  CG    . ASP A 1 309 ? -1.468  36.995  3.344   1 36.71  ? 309 ASP A CG    1 1 
ATOM   2524 O  OD1   . ASP A 1 309 ? -1.865  35.882  2.937   1 38.24  ? 309 ASP A OD1   1 1 
ATOM   2525 O  OD2   . ASP A 1 309 ? -1.329  37.277  4.553   1 39.45  ? 309 ASP A OD2   1 1 
ATOM   2526 N  N     . LEU A 1 310 ? 0.706   35.654  0.27    1 25.12  ? 310 LEU A N     1 1 
ATOM   2527 C  CA    . LEU A 1 310 ? 2.009   34.971  0.228   1 24.25  ? 310 LEU A CA    1 1 
ATOM   2528 C  C     . LEU A 1 310 ? 2.979   35.928  -0.549  1 23.76  ? 310 LEU A C     1 1 
ATOM   2529 O  O     . LEU A 1 310 ? 2.488   36.776  -1.301  1 23.76  ? 310 LEU A O     1 1 
ATOM   2530 C  CB    . LEU A 1 310 ? 1.903   33.586  -0.449  1 23.83  ? 310 LEU A CB    1 1 
ATOM   2531 C  CG    . LEU A 1 310 ? 1.519   32.425  0.472   1 24.42  ? 310 LEU A CG    1 1 
ATOM   2532 C  CD1   . LEU A 1 310 ? 1.321   31.139  -0.306  1 24.74  ? 310 LEU A CD1   1 1 
ATOM   2533 C  CD2   . LEU A 1 310 ? 2.539   32.23   1.551   1 24.79  ? 310 LEU A CD2   1 1 
ATOM   2534 N  N     . PRO A 1 311 ? 4.325   35.871  -0.38   1 23.01  ? 311 PRO A N     1 1 
ATOM   2535 C  CA    . PRO A 1 311 ? 5.191   36.819  -1.107  1 22.89  ? 311 PRO A CA    1 1 
ATOM   2536 C  C     . PRO A 1 311 ? 5.318   36.593  -2.613  1 23.06  ? 311 PRO A C     1 1 
ATOM   2537 O  O     . PRO A 1 311 ? 6.25    37.107  -3.21   1 23.05  ? 311 PRO A O     1 1 
ATOM   2538 C  CB    . PRO A 1 311 ? 6.539   36.672  -0.405  1 23.39  ? 311 PRO A CB    1 1 
ATOM   2539 C  CG    . PRO A 1 311 ? 6.532   35.281  0.091   1 23.61  ? 311 PRO A CG    1 1 
ATOM   2540 C  CD    . PRO A 1 311 ? 5.12    34.992  0.5     1 22.19  ? 311 PRO A CD    1 1 
ATOM   2541 N  N     . PHE A 1 312 ? 4.389   35.864  -3.229  1 23.15  ? 312 PHE A N     1 1 
ATOM   2542 C  CA    . PHE A 1 312 ? 4.409   35.612  -4.661  1 24.2   ? 312 PHE A CA    1 1 
ATOM   2543 C  C     . PHE A 1 312 ? 3.006   35.478  -5.26   1 25.65  ? 312 PHE A C     1 1 
ATOM   2544 O  O     . PHE A 1 312 ? 2.038   35.16   -4.565  1 26.01  ? 312 PHE A O     1 1 
ATOM   2545 C  CB    . PHE A 1 312 ? 5.29    34.406  -5.016  1 24.24  ? 312 PHE A CB    1 1 
ATOM   2546 C  CG    . PHE A 1 312 ? 5.059   33.213  -4.124  1 25.07  ? 312 PHE A CG    1 1 
ATOM   2547 C  CD1   . PHE A 1 312 ? 3.983   32.371  -4.331  1 25.74  ? 312 PHE A CD1   1 1 
ATOM   2548 C  CD2   . PHE A 1 312 ? 5.897   32.956  -3.053  1 25.92  ? 312 PHE A CD2   1 1 
ATOM   2549 C  CE1   . PHE A 1 312 ? 3.753   31.294  -3.489  1 26.39  ? 312 PHE A CE1   1 1 
ATOM   2550 C  CE2   . PHE A 1 312 ? 5.681   31.86   -2.231  1 26.48  ? 312 PHE A CE2   1 1 
ATOM   2551 C  CZ    . PHE A 1 312 ? 4.602   31.047  -2.444  1 26.19  ? 312 PHE A CZ    1 1 
ATOM   2552 N  N     . GLY A 1 313 ? 2.915   35.736  -6.553  1 26.34  ? 313 GLY A N     1 1 
ATOM   2553 C  CA    . GLY A 1 313 ? 1.672   35.656  -7.313  1 27.44  ? 313 GLY A CA    1 1 
ATOM   2554 C  C     . GLY A 1 313 ? 1.933   35.483  -8.795  1 28.47  ? 313 GLY A C     1 1 
ATOM   2555 O  O     . GLY A 1 313 ? 3.086   35.33   -9.209  1 28.5   ? 313 GLY A O     1 1 
ATOM   2556 N  N     . VAL A 1 314 ? 0.875   35.481  -9.612  1 29.19  ? 314 VAL A N     1 1 
ATOM   2557 C  CA    . VAL A 1 314 ? 1.043   35.261  -11.044 1 30.49  ? 314 VAL A CA    1 1 
ATOM   2558 C  C     . VAL A 1 314 ? 0.519   36.4    -11.874 1 31.6   ? 314 VAL A C     1 1 
ATOM   2559 O  O     . VAL A 1 314 ? -0.536  36.948  -11.572 1 31.76  ? 314 VAL A O     1 1 
ATOM   2560 C  CB    . VAL A 1 314 ? 0.389   33.932  -11.489 1 31.52  ? 314 VAL A CB    1 1 
ATOM   2561 C  CG1   . VAL A 1 314 ? 0.692   33.637  -12.953 1 32.41  ? 314 VAL A CG1   1 1 
ATOM   2562 C  CG2   . VAL A 1 314 ? 0.834   32.769  -10.61  1 32.02  ? 314 VAL A CG2   1 1 
ATOM   2563 N  N     . ILE A 1 315 ? 1.264   36.757  -12.927 1 32.19  ? 315 ILE A N     1 1 
ATOM   2564 C  CA    . ILE A 1 315 ? 0.862   37.721  -13.939 1 33.3   ? 315 ILE A CA    1 1 
ATOM   2565 C  C     . ILE A 1 315 ? 0.653   36.824  -15.153 1 34.24  ? 315 ILE A C     1 1 
ATOM   2566 O  O     . ILE A 1 315 ? 1.632   36.301  -15.681 1 34.37  ? 315 ILE A O     1 1 
ATOM   2567 C  CB    . ILE A 1 315 ? 1.934   38.809  -14.235 1 33.65  ? 315 ILE A CB    1 1 
ATOM   2568 C  CG1   . ILE A 1 315 ? 2.304   39.624  -12.982 1 34.26  ? 315 ILE A CG1   1 1 
ATOM   2569 C  CG2   . ILE A 1 315 ? 1.481   39.724  -15.378 1 34.17  ? 315 ILE A CG2   1 1 
ATOM   2570 C  CD1   . ILE A 1 315 ? 1.243   40.5    -12.419 1 35.18  ? 315 ILE A CD1   1 1 
ATOM   2571 N  N     . ARG A 1 316 ? -0.605  36.572  -15.539 1 34.59  ? 316 ARG A N     1 1 
ATOM   2572 C  CA    . ARG A 1 316 ? -0.907  35.708  -16.674 1 35.6   ? 316 ARG A CA    1 1 
ATOM   2573 C  C     . ARG A 1 316 ? -0.352  36.288  -17.972 1 36.33  ? 316 ARG A C     1 1 
ATOM   2574 O  O     . ARG A 1 316 ? -0.233  37.506  -18.09  1 36.43  ? 316 ARG A O     1 1 
ATOM   2575 C  CB    . ARG A 1 316 ? -2.42   35.484  -16.774 1 37.6   ? 316 ARG A CB    1 1 
ATOM   2576 C  CG    . ARG A 1 316 ? -3.021  34.91   -15.497 1 41.39  ? 316 ARG A CG    1 1 
ATOM   2577 C  CD    . ARG A 1 316 ? -4.181  33.98   -15.78  1 45.11  ? 316 ARG A CD    1 1 
ATOM   2578 N  NE    . ARG A 1 316 ? -5.46   34.635  -15.534 1 48.77  ? 316 ARG A NE    1 1 
ATOM   2579 C  CZ    . ARG A 1 316 ? -6.458  34.099  -14.836 1 51.67  ? 316 ARG A CZ    1 1 
ATOM   2580 N  NH1   . ARG A 1 316 ? -6.339  32.881  -14.318 1 51.27  ? 316 ARG A NH1   1 1 
ATOM   2581 N  NH2   . ARG A 1 316 ? -7.588  34.777  -14.655 1 51.94  ? 316 ARG A NH2   1 1 
ATOM   2582 N  N     . LYS A 1 317 ? 0       35.432  -18.948 1 36.91  ? 317 LYS A N     1 1 
ATOM   2583 C  CA    . LYS A 1 317 ? 0.568   35.9    -20.221 1 37.95  ? 317 LYS A CA    1 1 
ATOM   2584 C  C     . LYS A 1 317 ? -0.315  36.912  -20.946 1 39.24  ? 317 LYS A C     1 1 
ATOM   2585 O  O     . LYS A 1 317 ? 0.207   37.814  -21.602 1 39.62  ? 317 LYS A O     1 1 
ATOM   2586 C  CB    . LYS A 1 317 ? 0.945   34.733  -21.148 1 39.16  ? 317 LYS A CB    1 1 
ATOM   2587 C  CG    . LYS A 1 317 ? -0.204  33.823  -21.552 1 42.08  ? 317 LYS A CG    1 1 
ATOM   2588 C  CD    . LYS A 1 317 ? 0.311   32.71   -22.439 1 45.21  ? 317 LYS A CD    1 1 
ATOM   2589 C  CE    . LYS A 1 317 ? -0.699  31.652  -22.793 1 48.06  ? 317 LYS A CE    1 1 
ATOM   2590 N  NZ    . LYS A 1 317 ? -0.048  30.543  -23.551 1 49.74  ? 317 LYS A NZ    1 1 
ATOM   2591 N  N     . GLU A 1 318 ? -1.645  36.805  -20.769 1 39.67  ? 318 GLU A N     1 1 
ATOM   2592 C  CA    . GLU A 1 318 ? -2.626  37.712  -21.356 1 40.39  ? 318 GLU A CA    1 1 
ATOM   2593 C  C     . GLU A 1 318 ? -2.494  39.139  -20.817 1 41.33  ? 318 GLU A C     1 1 
ATOM   2594 O  O     . GLU A 1 318 ? -2.856  40.077  -21.513 1 41.62  ? 318 GLU A O     1 1 
ATOM   2595 C  CB    . GLU A 1 318 ? -4.048  37.186  -21.131 1 42.18  ? 318 GLU A CB    1 1 
ATOM   2596 C  CG    . GLU A 1 318 ? -4.338  35.868  -21.831 1 46.25  ? 318 GLU A CG    1 1 
ATOM   2597 C  CD    . GLU A 1 318 ? -4.001  34.62   -21.038 1 52.12  ? 318 GLU A CD    1 1 
ATOM   2598 O  OE1   . GLU A 1 318 ? -3.677  34.747  -19.836 1 52.75  ? 318 GLU A OE1   1 1 
ATOM   2599 O  OE2   . GLU A 1 318 ? -4.059  33.512  -21.617 1 54.83  ? 318 GLU A OE2   1 1 
ATOM   2600 N  N     . SER A 1 319 ? -1.977  39.31   -19.592 1 41.76  ? 319 SER A N     1 1 
ATOM   2601 C  CA    . SER A 1 319 ? -1.779  40.63   -18.981 1 42.61  ? 319 SER A CA    1 1 
ATOM   2602 C  C     . SER A 1 319 ? -0.297  41.01   -18.788 1 42.91  ? 319 SER A C     1 1 
ATOM   2603 O  O     . SER A 1 319 ? -0.011  42.088  -18.26  1 43.28  ? 319 SER A O     1 1 
ATOM   2604 C  CB    . SER A 1 319 ? -2.516  40.727  -17.649 1 44.53  ? 319 SER A CB    1 1 
ATOM   2605 O  OG    . SER A 1 319 ? -2.267  39.596  -16.829 1 47.85  ? 319 SER A OG    1 1 
ATOM   2606 N  N     . ARG A 1 320 ? 0.637   40.138  -19.211 1 42.51  ? 320 ARG A N     1 1 
ATOM   2607 C  CA    . ARG A 1 320 ? 2.07    40.37   -19.074 1 42.58  ? 320 ARG A CA    1 1 
ATOM   2608 C  C     . ARG A 1 320 ? 2.55    41.618  -19.827 1 43.03  ? 320 ARG A C     1 1 
ATOM   2609 O  O     . ARG A 1 320 ? 3.317   42.397  -19.267 1 43.27  ? 320 ARG A O     1 1 
ATOM   2610 C  CB    . ARG A 1 320 ? 2.869   39.118  -19.484 1 42.98  ? 320 ARG A CB    1 1 
ATOM   2611 C  CG    . ARG A 1 320 ? 4.373   39.24   -19.243 1 44.73  ? 320 ARG A CG    1 1 
ATOM   2612 C  CD    . ARG A 1 320 ? 5.072   37.914  -19.436 1 46.42  ? 320 ARG A CD    1 1 
ATOM   2613 N  NE    . ARG A 1 320 ? 6.53    38.017  -19.374 1 47.7   ? 320 ARG A NE    1 1 
ATOM   2614 C  CZ    . ARG A 1 320 ? 7.347   36.987  -19.177 1 49.26  ? 320 ARG A CZ    1 1 
ATOM   2615 N  NH1   . ARG A 1 320 ? 6.858   35.761  -19.024 1 49.06  ? 320 ARG A NH1   1 1 
ATOM   2616 N  NH2   . ARG A 1 320 ? 8.66    37.171  -19.145 1 48.65  ? 320 ARG A NH2   1 1 
ATOM   2617 N  N     . ASN A 1 321 ? 2.078   41.838  -21.067 1 42.92  ? 321 ASN A N     1 1 
ATOM   2618 C  CA    . ASN A 1 321 ? 2.492   42.997  -21.854 1 43.32  ? 321 ASN A CA    1 1 
ATOM   2619 C  C     . ASN A 1 321 ? 2.208   44.317  -21.129 1 42.99  ? 321 ASN A C     1 1 
ATOM   2620 O  O     . ASN A 1 321 ? 3.085   45.173  -21.042 1 42.84  ? 321 ASN A O     1 1 
ATOM   2621 C  CB    . ASN A 1 321 ? 1.838   42.975  -23.239 1 45.26  ? 321 ASN A CB    1 1 
ATOM   2622 C  CG    . ASN A 1 321 ? 2.201   44.159  -24.11  1 50.06  ? 321 ASN A CG    1 1 
ATOM   2623 O  OD1   . ASN A 1 321 ? 3.133   44.095  -24.914 1 51.99  ? 321 ASN A OD1   1 1 
ATOM   2624 N  ND2   . ASN A 1 321 ? 1.481   45.273  -23.969 1 50.86  ? 321 ASN A ND2   1 1 
ATOM   2625 N  N     . ASP A 1 322 ? 0.997   44.463  -20.594 1 42.76  ? 322 ASP A N     1 1 
ATOM   2626 C  CA    . ASP A 1 322 ? 0.596   45.674  -19.888 1 43.04  ? 322 ASP A CA    1 1 
ATOM   2627 C  C     . ASP A 1 322 ? 1.343   45.847  -18.575 1 42.44  ? 322 ASP A C     1 1 
ATOM   2628 O  O     . ASP A 1 322 ? 1.69    46.968  -18.21  1 42.69  ? 322 ASP A O     1 1 
ATOM   2629 C  CB    . ASP A 1 322 ? -0.92   45.681  -19.664 1 45.27  ? 322 ASP A CB    1 1 
ATOM   2630 C  CG    . ASP A 1 322 ? -1.729  45.695  -20.945 1 50.66  ? 322 ASP A CG    1 1 
ATOM   2631 O  OD1   . ASP A 1 322 ? -1.163  46.059  -22.006 1 51.47  ? 322 ASP A OD1   1 1 
ATOM   2632 O  OD2   . ASP A 1 322 ? -2.925  45.339  -20.893 1 53.41  ? 322 ASP A OD2   1 1 
ATOM   2633 N  N     . PHE A 1 323 ? 1.626   44.743  -17.878 1 41.54  ? 323 PHE A N     1 1 
ATOM   2634 C  CA    . PHE A 1 323 ? 2.387   44.797  -16.633 1 41.14  ? 323 PHE A CA    1 1 
ATOM   2635 C  C     . PHE A 1 323 ? 3.806   45.295  -16.942 1 41.09  ? 323 PHE A C     1 1 
ATOM   2636 O  O     . PHE A 1 323 ? 4.253   46.257  -16.325 1 41.53  ? 323 PHE A O     1 1 
ATOM   2637 C  CB    . PHE A 1 323 ? 2.413   43.412  -15.957 1 40.65  ? 323 PHE A CB    1 1 
ATOM   2638 C  CG    . PHE A 1 323 ? 3.459   43.248  -14.88  1 40.64  ? 323 PHE A CG    1 1 
ATOM   2639 C  CD1   . PHE A 1 323 ? 3.258   43.765  -13.617 1 41.17  ? 323 PHE A CD1   1 1 
ATOM   2640 C  CD2   . PHE A 1 323 ? 4.638   42.572  -15.134 1 41.11  ? 323 PHE A CD2   1 1 
ATOM   2641 C  CE1   . PHE A 1 323 ? 4.212   43.602  -12.626 1 41.69  ? 323 PHE A CE1   1 1 
ATOM   2642 C  CE2   . PHE A 1 323 ? 5.594   42.415  -14.143 1 41.61  ? 323 PHE A CE2   1 1 
ATOM   2643 C  CZ    . PHE A 1 323 ? 5.373   42.93   -12.895 1 41.39  ? 323 PHE A CZ    1 1 
ATOM   2644 N  N     . ILE A 1 324 ? 4.47    44.689  -17.95  1 40.35  ? 324 ILE A N     1 1 
ATOM   2645 C  CA    . ILE A 1 324 ? 5.818   45.064  -18.368 1 39.92  ? 324 ILE A CA    1 1 
ATOM   2646 C  C     . ILE A 1 324 ? 5.884   46.513  -18.798 1 39.59  ? 324 ILE A C     1 1 
ATOM   2647 O  O     . ILE A 1 324 ? 6.836   47.194  -18.427 1 39.71  ? 324 ILE A O     1 1 
ATOM   2648 C  CB    . ILE A 1 324 ? 6.355   44.106  -19.451 1 40.35  ? 324 ILE A CB    1 1 
ATOM   2649 C  CG1   . ILE A 1 324 ? 6.514   42.663  -18.901 1 41.41  ? 324 ILE A CG1   1 1 
ATOM   2650 C  CG2   . ILE A 1 324 ? 7.647   44.628  -20.065 1 40.73  ? 324 ILE A CG2   1 1 
ATOM   2651 C  CD1   . ILE A 1 324 ? 7.359   42.504  -17.625 1 42.65  ? 324 ILE A CD1   1 1 
ATOM   2652 N  N     . ASN A 1 325 ? 4.862   46.997  -19.534 1 39.24  ? 325 ASN A N     1 1 
ATOM   2653 C  CA    . ASN A 1 325 ? 4.785   48.387  -19.994 1 39.47  ? 325 ASN A CA    1 1 
ATOM   2654 C  C     . ASN A 1 325 ? 4.785   49.35   -18.812 1 38.94  ? 325 ASN A C     1 1 
ATOM   2655 O  O     . ASN A 1 325 ? 5.513   50.35   -18.817 1 38.78  ? 325 ASN A O     1 1 
ATOM   2656 C  CB    . ASN A 1 325 ? 3.532   48.616  -20.841 1 41.25  ? 325 ASN A CB    1 1 
ATOM   2657 C  CG    . ASN A 1 325 ? 3.65    48.186  -22.279 1 45.69  ? 325 ASN A CG    1 1 
ATOM   2658 O  OD1   . ASN A 1 325 ? 4.737   47.88   -22.763 1 47.19  ? 325 ASN A OD1   1 1 
ATOM   2659 N  ND2   . ASN A 1 325 ? 2.53    48.154  -22.997 1 46.75  ? 325 ASN A ND2   1 1 
ATOM   2660 N  N     . ASP A 1 326 ? 3.987   49.03   -17.79  1 38.37  ? 326 ASP A N     1 1 
ATOM   2661 C  CA    . ASP A 1 326 ? 3.899   49.85   -16.594 1 38.36  ? 326 ASP A CA    1 1 
ATOM   2662 C  C     . ASP A 1 326 ? 5.204   49.864  -15.79  1 38.01  ? 326 ASP A C     1 1 
ATOM   2663 O  O     . ASP A 1 326 ? 5.596   50.92   -15.293 1 37.89  ? 326 ASP A O     1 1 
ATOM   2664 C  CB    . ASP A 1 326 ? 2.7     49.417  -15.733 1 39.74  ? 326 ASP A CB    1 1 
ATOM   2665 C  CG    . ASP A 1 326 ? 1.358   49.919  -16.234 1 44.04  ? 326 ASP A CG    1 1 
ATOM   2666 O  OD1   . ASP A 1 326 ? 1.341   50.767  -17.148 1 44.76  ? 326 ASP A OD1   1 1 
ATOM   2667 O  OD2   . ASP A 1 326 ? 0.329   49.48   -15.7   1 46.27  ? 326 ASP A OD2   1 1 
ATOM   2668 N  N     . VAL A 1 327 ? 5.885   48.708  -15.69  1 37.67  ? 327 VAL A N     1 1 
ATOM   2669 C  CA    . VAL A 1 327 ? 7.154   48.606  -14.975 1 38.01  ? 327 VAL A CA    1 1 
ATOM   2670 C  C     . VAL A 1 327 ? 8.229   49.455  -15.674 1 38.76  ? 327 VAL A C     1 1 
ATOM   2671 O  O     . VAL A 1 327 ? 8.977   50.187  -15.018 1 38.8   ? 327 VAL A O     1 1 
ATOM   2672 C  CB    . VAL A 1 327 ? 7.581   47.13   -14.793 1 38.19  ? 327 VAL A CB    1 1 
ATOM   2673 C  CG1   . VAL A 1 327 ? 8.986   47.026  -14.202 1 38.57  ? 327 VAL A CG1   1 1 
ATOM   2674 C  CG2   . VAL A 1 327 ? 6.573   46.383  -13.925 1 38.28  ? 327 VAL A CG2   1 1 
ATOM   2675 N  N     . CYS A 1 328 ? 8.256   49.41   -17.008 1 39.06  ? 328 CYS A N     1 1 
ATOM   2676 C  CA    . CYS A 1 328 ? 9.197   50.197  -17.795 1 39.69  ? 328 CYS A CA    1 1 
ATOM   2677 C  C     . CYS A 1 328 ? 8.917   51.677  -17.69  1 39.95  ? 328 CYS A C     1 1 
ATOM   2678 O  O     . CYS A 1 328 ? 9.86    52.467  -17.665 1 40.69  ? 328 CYS A O     1 1 
ATOM   2679 C  CB    . CYS A 1 328 ? 9.204   49.739  -19.245 1 40.97  ? 328 CYS A CB    1 1 
ATOM   2680 S  SG    . CYS A 1 328 ? 9.743   48.029  -19.463 1 47.06  ? 328 CYS A SG    1 1 
ATOM   2681 N  N     . LYS A 1 329 ? 7.642   52.065  -17.635 1 39.35  ? 329 LYS A N     1 1 
ATOM   2682 C  CA    . LYS A 1 329 ? 7.309   53.473  -17.504 1 39.51  ? 329 LYS A CA    1 1 
ATOM   2683 C  C     . LYS A 1 329 ? 7.683   53.991  -16.117 1 39.29  ? 329 LYS A C     1 1 
ATOM   2684 O  O     . LYS A 1 329 ? 8.262   55.069  -16.012 1 39.32  ? 329 LYS A O     1 1 
ATOM   2685 C  CB    . LYS A 1 329 ? 5.855   53.747  -17.905 1 41.86  ? 329 LYS A CB    1 1 
ATOM   2686 C  CG    . LYS A 1 329 ? 5.612   53.578  -19.421 1 46.75  ? 329 LYS A CG    1 1 
ATOM   2687 C  CD    . LYS A 1 329 ? 6.524   54.486  -20.31  1 51.89  ? 329 LYS A CD    1 1 
ATOM   2688 C  CE    . LYS A 1 329 ? 7.427   53.731  -21.28  1 55.7   ? 329 LYS A CE    1 1 
ATOM   2689 N  NZ    . LYS A 1 329 ? 8.874   53.81   -20.916 1 57.32  ? 329 LYS A NZ    1 1 
ATOM   2690 N  N     . LEU A 1 330 ? 7.479   53.175  -15.076 1 39.1   ? 330 LEU A N     1 1 
ATOM   2691 C  CA    . LEU A 1 330 ? 7.841   53.531  -13.699 1 39.37  ? 330 LEU A CA    1 1 
ATOM   2692 C  C     . LEU A 1 330 ? 9.36    53.741  -13.496 1 39.63  ? 330 LEU A C     1 1 
ATOM   2693 O  O     . LEU A 1 330 ? 9.773   54.725  -12.887 1 39.4   ? 330 LEU A O     1 1 
ATOM   2694 C  CB    . LEU A 1 330 ? 7.314   52.457  -12.712 1 39.3   ? 330 LEU A CB    1 1 
ATOM   2695 C  CG    . LEU A 1 330 ? 7.698   52.644  -11.241 1 40.24  ? 330 LEU A CG    1 1 
ATOM   2696 C  CD1   . LEU A 1 330 ? 7.148   53.94   -10.692 1 40.88  ? 330 LEU A CD1   1 1 
ATOM   2697 C  CD2   . LEU A 1 330 ? 7.259   51.471  -10.4   1 40.42  ? 330 LEU A CD2   1 1 
ATOM   2698 N  N     . TYR A 1 331 ? 10.179  52.813  -13.99  1 39.99  ? 331 TYR A N     1 1 
ATOM   2699 C  CA    . TYR A 1 331 ? 11.622  52.87   -13.791 1 40.9   ? 331 TYR A CA    1 1 
ATOM   2700 C  C     . TYR A 1 331 ? 12.432  53.427  -14.973 1 42.26  ? 331 TYR A C     1 1 
ATOM   2701 O  O     . TYR A 1 331 ? 13.667  53.366  -14.949 1 42.31  ? 331 TYR A O     1 1 
ATOM   2702 C  CB    . TYR A 1 331 ? 12.134  51.49   -13.396 1 40.53  ? 331 TYR A CB    1 1 
ATOM   2703 C  CG    . TYR A 1 331 ? 11.667  51.073  -12.021 1 40.7   ? 331 TYR A CG    1 1 
ATOM   2704 C  CD1   . TYR A 1 331 ? 12.116  51.729  -10.886 1 41.34  ? 331 TYR A CD1   1 1 
ATOM   2705 C  CD2   . TYR A 1 331 ? 10.798  50.005  -11.854 1 41.21  ? 331 TYR A CD2   1 1 
ATOM   2706 C  CE1   . TYR A 1 331 ? 11.717  51.33   -9.617  1 41.97  ? 331 TYR A CE1   1 1 
ATOM   2707 C  CE2   . TYR A 1 331 ? 10.387  49.599  -10.588 1 41.82  ? 331 TYR A CE2   1 1 
ATOM   2708 C  CZ    . TYR A 1 331 ? 10.85   50.263  -9.471  1 42.37  ? 331 TYR A CZ    1 1 
ATOM   2709 O  OH    . TYR A 1 331 ? 10.448  49.87   -8.219  1 43.05  ? 331 TYR A OH    1 1 
ATOM   2710 N  N     . ASN A 1 332 ? 11.74   54.01   -15.967 1 43.04  ? 332 ASN A N     1 1 
ATOM   2711 C  CA    . ASN A 1 332 ? 12.341  54.602  -17.155 1 44.19  ? 332 ASN A CA    1 1 
ATOM   2712 C  C     . ASN A 1 332 ? 13.2    53.618  -17.942 1 44.96  ? 332 ASN A C     1 1 
ATOM   2713 O  O     . ASN A 1 332 ? 14.345  53.922  -18.299 1 45.03  ? 332 ASN A O     1 1 
ATOM   2714 C  CB    . ASN A 1 332 ? 13.103  55.88   -16.832 1 45.7   ? 332 ASN A CB    1 1 
ATOM   2715 C  CG    . ASN A 1 332 ? 13.185  56.803  -18.017 1 50.05  ? 332 ASN A CG    1 1 
ATOM   2716 O  OD1   . ASN A 1 332 ? 12.207  56.992  -18.747 1 51.54  ? 332 ASN A OD1   1 1 
ATOM   2717 N  ND2   . ASN A 1 332 ? 14.359  57.39   -18.244 1 51.31  ? 332 ASN A ND2   1 1 
ATOM   2718 N  N     . ILE A 1 333 ? 12.649  52.422  -18.195 1 45.24  ? 333 ILE A N     1 1 
ATOM   2719 C  CA    . ILE A 1 333 ? 13.325  51.412  -18.996 1 46.16  ? 333 ILE A CA    1 1 
ATOM   2720 C  C     . ILE A 1 333 ? 12.898  51.655  -20.433 1 47.35  ? 333 ILE A C     1 1 
ATOM   2721 O  O     . ILE A 1 333 ? 11.714  51.573  -20.744 1 47.58  ? 333 ILE A O     1 1 
ATOM   2722 C  CB    . ILE A 1 333 ? 13.006  49.988  -18.522 1 46.43  ? 333 ILE A CB    1 1 
ATOM   2723 C  CG1   . ILE A 1 333 ? 13.399  49.817  -17.054 1 47.3   ? 333 ILE A CG1   1 1 
ATOM   2724 C  CG2   . ILE A 1 333 ? 13.709  48.968  -19.405 1 46.84  ? 333 ILE A CG2   1 1 
ATOM   2725 C  CD1   . ILE A 1 333 ? 12.858  48.605  -16.445 1 48.7   ? 333 ILE A CD1   1 1 
ATOM   2726 N  N     . ASN A 1 334 ? 13.845  52.044  -21.291 1 48.01  ? 334 ASN A N     1 1 
ATOM   2727 C  CA    . ASN A 1 334 ? 13.536  52.387  -22.671 1 48.87  ? 334 ASN A CA    1 1 
ATOM   2728 C  C     . ASN A 1 334 ? 14.071  51.379  -23.681 1 49.43  ? 334 ASN A C     1 1 
ATOM   2729 O  O     . ASN A 1 334 ? 13.449  51.182  -24.729 1 49.48  ? 334 ASN A O     1 1 
ATOM   2730 C  CB    . ASN A 1 334 ? 14.055  53.793  -22.982 1 50.03  ? 334 ASN A CB    1 1 
ATOM   2731 C  CG    . ASN A 1 334 ? 13.222  54.903  -22.377 1 53.2   ? 334 ASN A CG    1 1 
ATOM   2732 O  OD1   . ASN A 1 334 ? 12.114  54.688  -21.861 1 54.56  ? 334 ASN A OD1   1 1 
ATOM   2733 N  ND2   . ASN A 1 334 ? 13.732  56.125  -22.444 1 53.65  ? 334 ASN A ND2   1 1 
ATOM   2734 N  N     . ASP A 1 335 ? 15.22   50.748  -23.364 1 49.55  ? 335 ASP A N     1 1 
ATOM   2735 C  CA    . ASP A 1 335 ? 15.887  49.769  -24.222 1 50.09  ? 335 ASP A CA    1 1 
ATOM   2736 C  C     . ASP A 1 335 ? 14.963  48.681  -24.789 1 50.83  ? 335 ASP A C     1 1 
ATOM   2737 O  O     . ASP A 1 335 ? 14.469  47.838  -24.04  1 51.09  ? 335 ASP A O     1 1 
ATOM   2738 C  CB    . ASP A 1 335 ? 17.078  49.133  -23.503 1 51.14  ? 335 ASP A CB    1 1 
ATOM   2739 C  CG    . ASP A 1 335 ? 17.974  48.365  -24.452 1 54.63  ? 335 ASP A CG    1 1 
ATOM   2740 O  OD1   . ASP A 1 335 ? 18.696  49.011  -25.243 1 55.51  ? 335 ASP A OD1   1 1 
ATOM   2741 O  OD2   . ASP A 1 335 ? 17.941  47.127  -24.419 1 55.88  ? 335 ASP A OD2   1 1 
ATOM   2742 N  N     . MET A 1 336 ? 14.754  48.7    -26.122 1 50.85  ? 336 MET A N     1 1 
ATOM   2743 C  CA    . MET A 1 336 ? 13.906  47.755  -26.855 1 51.1   ? 336 MET A CA    1 1 
ATOM   2744 C  C     . MET A 1 336 ? 14.338  46.284  -26.693 1 50.2   ? 336 MET A C     1 1 
ATOM   2745 O  O     . MET A 1 336 ? 13.473  45.416  -26.645 1 50.38  ? 336 MET A O     1 1 
ATOM   2746 C  CB    . MET A 1 336 ? 13.786  48.149  -28.341 1 52.75  ? 336 MET A CB    1 1 
ATOM   2747 C  CG    . MET A 1 336 ? 15.101  48.07   -29.111 1 57     ? 336 MET A CG    1 1 
ATOM   2748 S  SD    . MET A 1 336 ? 16.289  49.421  -28.794 1 65.32  ? 336 MET A SD    1 1 
ATOM   2749 C  CE    . MET A 1 336 ? 17.857  48.589  -29.241 1 62.23  ? 336 MET A CE    1 1 
ATOM   2750 N  N     . LYS A 1 337 ? 15.644  46.003  -26.558 1 49.23  ? 337 LYS A N     1 1 
ATOM   2751 C  CA    . LYS A 1 337 ? 16.109  44.631  -26.35  1 48.91  ? 337 LYS A CA    1 1 
ATOM   2752 C  C     . LYS A 1 337 ? 15.659  44.107  -24.975 1 47.61  ? 337 LYS A C     1 1 
ATOM   2753 O  O     . LYS A 1 337 ? 15.143  42.993  -24.886 1 47.72  ? 337 LYS A O     1 1 
ATOM   2754 C  CB    . LYS A 1 337 ? 17.639  44.539  -26.478 1 51.38  ? 337 LYS A CB    1 1 
ATOM   2755 C  CG    . LYS A 1 337 ? 18.146  44.314  -27.897 1 55.89  ? 337 LYS A CG    1 1 
ATOM   2756 C  CD    . LYS A 1 337 ? 18.803  42.938  -28.023 1 60.1   ? 337 LYS A CD    1 1 
ATOM   2757 C  CE    . LYS A 1 337 ? 19.742  42.842  -29.204 1 63.56  ? 337 LYS A CE    1 1 
ATOM   2758 N  NZ    . LYS A 1 337 ? 20.358  41.488  -29.312 1 65.51  ? 337 LYS A NZ    1 1 
ATOM   2759 N  N     . ILE A 1 338 ? 15.831  44.923  -23.916 1 46.17  ? 338 ILE A N     1 1 
ATOM   2760 C  CA    . ILE A 1 338 ? 15.437  44.58   -22.544 1 45.09  ? 338 ILE A CA    1 1 
ATOM   2761 C  C     . ILE A 1 338 ? 13.932  44.318  -22.451 1 43.41  ? 338 ILE A C     1 1 
ATOM   2762 O  O     . ILE A 1 338 ? 13.507  43.336  -21.851 1 43.55  ? 338 ILE A O     1 1 
ATOM   2763 C  CB    . ILE A 1 338 ? 15.877  45.698  -21.557 1 45.71  ? 338 ILE A CB    1 1 
ATOM   2764 C  CG1   . ILE A 1 338 ? 17.407  45.8    -21.465 1 46.79  ? 338 ILE A CG1   1 1 
ATOM   2765 C  CG2   . ILE A 1 338 ? 15.27   45.492  -20.178 1 46.11  ? 338 ILE A CG2   1 1 
ATOM   2766 C  CD1   . ILE A 1 338 ? 17.933  46.983  -20.581 1 48.06  ? 338 ILE A CD1   1 1 
ATOM   2767 N  N     . ILE A 1 339 ? 13.134  45.193  -23.05  1 41.81  ? 339 ILE A N     1 1 
ATOM   2768 C  CA    . ILE A 1 339 ? 11.686  45.068  -23.037 1 40.81  ? 339 ILE A CA    1 1 
ATOM   2769 C  C     . ILE A 1 339 ? 11.242  43.807  -23.777 1 39.76  ? 339 ILE A C     1 1 
ATOM   2770 O  O     . ILE A 1 339 ? 10.341  43.114  -23.31  1 39.71  ? 339 ILE A O     1 1 
ATOM   2771 C  CB    . ILE A 1 339 ? 11.044  46.358  -23.593 1 41.26  ? 339 ILE A CB    1 1 
ATOM   2772 C  CG1   . ILE A 1 339 ? 11.51   47.595  -22.793 1 42.12  ? 339 ILE A CG1   1 1 
ATOM   2773 C  CG2   . ILE A 1 339 ? 9.537   46.257  -23.587 1 41.81  ? 339 ILE A CG2   1 1 
ATOM   2774 C  CD1   . ILE A 1 339 ? 11.11   48.93   -23.387 1 43.18  ? 339 ILE A CD1   1 1 
ATOM   2775 N  N     . LYS A 1 340 ? 11.917  43.46   -24.882 1 38.85  ? 340 LYS A N     1 1 
ATOM   2776 C  CA    . LYS A 1 340 ? 11.585  42.249  -25.632 1 38.58  ? 340 LYS A CA    1 1 
ATOM   2777 C  C     . LYS A 1 340 ? 11.806  41.006  -24.78  1 37.95  ? 340 LYS A C     1 1 
ATOM   2778 O  O     . LYS A 1 340 ? 10.987  40.09   -24.813 1 38.16  ? 340 LYS A O     1 1 
ATOM   2779 C  CB    . LYS A 1 340 ? 12.399  42.147  -26.932 1 40.55  ? 340 LYS A CB    1 1 
ATOM   2780 C  CG    . LYS A 1 340 ? 11.802  42.911  -28.114 1 44.8   ? 340 LYS A CG    1 1 
ATOM   2781 C  CD    . LYS A 1 340 ? 12.635  42.724  -29.386 1 49.36  ? 340 LYS A CD    1 1 
ATOM   2782 C  CE    . LYS A 1 340 ? 12.696  43.954  -30.273 1 53.1   ? 340 LYS A CE    1 1 
ATOM   2783 N  NZ    . LYS A 1 340 ? 14.035  44.622  -30.231 1 55.35  ? 340 LYS A NZ    1 1 
ATOM   2784 N  N     . GLU A 1 341 ? 12.89   40.984  -23.994 1 37.14  ? 341 GLU A N     1 1 
ATOM   2785 C  CA    . GLU A 1 341 ? 13.19   39.856  -23.113 1 36.85  ? 341 GLU A CA    1 1 
ATOM   2786 C  C     . GLU A 1 341 ? 12.122  39.721  -22.019 1 36.48  ? 341 GLU A C     1 1 
ATOM   2787 O  O     . GLU A 1 341 ? 11.664  38.62   -21.717 1 36.44  ? 341 GLU A O     1 1 
ATOM   2788 C  CB    . GLU A 1 341 ? 14.591  40.016  -22.497 1 38.43  ? 341 GLU A CB    1 1 
ATOM   2789 N  N     . LEU A 1 342 ? 11.702  40.85   -21.464 1 36.2   ? 342 LEU A N     1 1 
ATOM   2790 C  CA    . LEU A 1 342 ? 10.679  40.892  -20.435 1 36.68  ? 342 LEU A CA    1 1 
ATOM   2791 C  C     . LEU A 1 342 ? 9.306   40.459  -20.96  1 37.7   ? 342 LEU A C     1 1 
ATOM   2792 O  O     . LEU A 1 342 ? 8.515   39.911  -20.2   1 38.01  ? 342 LEU A O     1 1 
ATOM   2793 C  CB    . LEU A 1 342 ? 10.554  42.321  -19.9   1 36.37  ? 342 LEU A CB    1 1 
ATOM   2794 C  CG    . LEU A 1 342 ? 11.665  42.82   -19.017 1 37.11  ? 342 LEU A CG    1 1 
ATOM   2795 C  CD1   . LEU A 1 342 ? 11.482  44.268  -18.736 1 37.74  ? 342 LEU A CD1   1 1 
ATOM   2796 C  CD2   . LEU A 1 342 ? 11.675  42.095  -17.72  1 37.41  ? 342 LEU A CD2   1 1 
ATOM   2797 N  N     . LYS A 1 343 ? 9.004   40.733  -22.233 1 37.99  ? 343 LYS A N     1 1 
ATOM   2798 C  CA    . LYS A 1 343 ? 7.681   40.445  -22.782 1 38.64  ? 343 LYS A CA    1 1 
ATOM   2799 C  C     . LYS A 1 343 ? 7.494   39.058  -23.392 1 39.38  ? 343 LYS A C     1 1 
ATOM   2800 O  O     . LYS A 1 343 ? 6.575   38.892  -24.196 1 39.75  ? 343 LYS A O     1 1 
ATOM   2801 C  CB    . LYS A 1 343 ? 7.28    41.513  -23.802 1 40.05  ? 343 LYS A CB    1 1 
ATOM   2802 C  CG    . LYS A 1 343 ? 6.941   42.849  -23.167 1 43.2   ? 343 LYS A CG    1 1 
ATOM   2803 C  CD    . LYS A 1 343 ? 6.572   43.884  -24.217 1 45.98  ? 343 LYS A CD    1 1 
ATOM   2804 C  CE    . LYS A 1 343 ? 6.038   45.151  -23.618 1 47.77  ? 343 LYS A CE    1 1 
ATOM   2805 N  NZ    . LYS A 1 343 ? 5.451   46.02   -24.666 1 48.99  ? 343 LYS A NZ    1 1 
ATOM   2806 N  N     . GLU A 1 344 ? 8.291   38.047  -22.987 1 39.39  ? 344 GLU A N     1 1 
ATOM   2807 C  CA    . GLU A 1 344 ? 8.117   36.687  -23.524 1 39.85  ? 344 GLU A CA    1 1 
ATOM   2808 C  C     . GLU A 1 344 ? 6.692   36.159  -23.234 1 39.87  ? 344 GLU A C     1 1 
ATOM   2809 O  O     . GLU A 1 344 ? 6.165   36.412  -22.152 1 40.26  ? 344 GLU A O     1 1 
ATOM   2810 C  CB    . GLU A 1 344 ? 9.184   35.737  -22.965 1 42.19  ? 344 GLU A CB    1 1 
ATOM   2811 C  CG    . GLU A 1 344 ? 9.196   34.38   -23.647 1 46.94  ? 344 GLU A CG    1 1 
ATOM   2812 C  CD    . GLU A 1 344 ? 10.271  33.435  -23.146 1 53.15  ? 344 GLU A CD    1 1 
ATOM   2813 O  OE1   . GLU A 1 344 ? 11.324  33.926  -22.68  1 53.27  ? 344 GLU A OE1   1 1 
ATOM   2814 O  OE2   . GLU A 1 344 ? 10.051  32.204  -23.198 1 56.13  ? 344 GLU A OE2   1 1 
ATOM   2815 N  N     . ASP A 1 345 ? 6.038   35.517  -24.222 1 39.11  ? 345 ASP A N     1 1 
ATOM   2816 C  CA    . ASP A 1 345 ? 4.656   35.057  -24.067 1 38.52  ? 345 ASP A CA    1 1 
ATOM   2817 C  C     . ASP A 1 345 ? 4.493   33.845  -23.156 1 36.76  ? 345 ASP A C     1 1 
ATOM   2818 O  O     . ASP A 1 345 ? 4.327   32.722  -23.625 1 36.84  ? 345 ASP A O     1 1 
ATOM   2819 C  CB    . ASP A 1 345 ? 4.003   34.8    -25.432 1 41.32  ? 345 ASP A CB    1 1 
ATOM   2820 C  CG    . ASP A 1 345 ? 2.509   34.527  -25.351 1 48.14  ? 345 ASP A CG    1 1 
ATOM   2821 O  OD1   . ASP A 1 345 ? 1.774   35.381  -24.783 1 49.54  ? 345 ASP A OD1   1 1 
ATOM   2822 O  OD2   . ASP A 1 345 ? 2.072   33.459  -25.85  1 50.85  ? 345 ASP A OD2   1 1 
ATOM   2823 N  N     . ALA A 1 346 ? 4.512   34.081  -21.851 1 35.21  ? 346 ALA A N     1 1 
ATOM   2824 C  CA    . ALA A 1 346 ? 4.33    33.037  -20.851 1 34.46  ? 346 ALA A CA    1 1 
ATOM   2825 C  C     . ALA A 1 346 ? 3.901   33.656  -19.528 1 33.52  ? 346 ALA A C     1 1 
ATOM   2826 O  O     . ALA A 1 346 ? 4.162   34.831  -19.287 1 33.55  ? 346 ALA A O     1 1 
ATOM   2827 C  CB    . ALA A 1 346 ? 5.623   32.26   -20.656 1 34.62  ? 346 ALA A CB    1 1 
ATOM   2828 N  N     . ASP A 1 347 ? 3.259   32.871  -18.649 1 32.51  ? 347 ASP A N     1 1 
ATOM   2829 C  CA    . ASP A 1 347 ? 2.871   33.351  -17.323 1 31.88  ? 347 ASP A CA    1 1 
ATOM   2830 C  C     . ASP A 1 347 ? 4.143   33.709  -16.53  1 30.91  ? 347 ASP A C     1 1 
ATOM   2831 O  O     . ASP A 1 347 ? 5.185   33.057  -16.674 1 30.97  ? 347 ASP A O     1 1 
ATOM   2832 C  CB    . ASP A 1 347 ? 2.063   32.286  -16.558 1 33.53  ? 347 ASP A CB    1 1 
ATOM   2833 C  CG    . ASP A 1 347 ? 0.785   31.85   -17.243 1 38.21  ? 347 ASP A CG    1 1 
ATOM   2834 O  OD1   . ASP A 1 347 ? 0.189   32.679  -17.962 1 39.27  ? 347 ASP A OD1   1 1 
ATOM   2835 O  OD2   . ASP A 1 347 ? 0.375   30.675  -17.052 1 40.03  ? 347 ASP A OD2   1 1 
ATOM   2836 N  N     . LEU A 1 348 ? 4.065   34.77   -15.74  1 29.64  ? 348 LEU A N     1 1 
ATOM   2837 C  CA    . LEU A 1 348 ? 5.203   35.243  -14.971 1 28.72  ? 348 LEU A CA    1 1 
ATOM   2838 C  C     . LEU A 1 348 ? 4.861   35.195  -13.497 1 27.91  ? 348 LEU A C     1 1 
ATOM   2839 O  O     . LEU A 1 348 ? 3.81    35.687  -13.103 1 27.99  ? 348 LEU A O     1 1 
ATOM   2840 C  CB    . LEU A 1 348 ? 5.475   36.679  -15.391 1 28.82  ? 348 LEU A CB    1 1 
ATOM   2841 C  CG    . LEU A 1 348 ? 6.647   37.352  -14.764 1 30.55  ? 348 LEU A CG    1 1 
ATOM   2842 C  CD1   . LEU A 1 348 ? 7.944   36.792  -15.313 1 31.37  ? 348 LEU A CD1   1 1 
ATOM   2843 C  CD2   . LEU A 1 348 ? 6.586   38.825  -15.026 1 31.51  ? 348 LEU A CD2   1 1 
ATOM   2844 N  N     . ILE A 1 349 ? 5.699   34.551  -12.692 1 27.02  ? 349 ILE A N     1 1 
ATOM   2845 C  CA    . ILE A 1 349 ? 5.466   34.491  -11.259 1 27.05  ? 349 ILE A CA    1 1 
ATOM   2846 C  C     . ILE A 1 349 ? 6.245   35.612  -10.66  1 27.34  ? 349 ILE A C     1 1 
ATOM   2847 O  O     . ILE A 1 349 ? 7.454   35.68   -10.852 1 27.87  ? 349 ILE A O     1 1 
ATOM   2848 C  CB    . ILE A 1 349 ? 5.851   33.136  -10.647 1 27.61  ? 349 ILE A CB    1 1 
ATOM   2849 C  CG1   . ILE A 1 349 ? 4.906   32.044  -11.161 1 28.74  ? 349 ILE A CG1   1 1 
ATOM   2850 C  CG2   . ILE A 1 349 ? 5.839   33.214  -9.114  1 28.11  ? 349 ILE A CG2   1 1 
ATOM   2851 C  CD1   . ILE A 1 349 ? 5.208   30.69   -10.695 1 30.16  ? 349 ILE A CD1   1 1 
ATOM   2852 N  N     . VAL A 1 350 ? 5.567   36.519  -9.972  1 27.08  ? 350 VAL A N     1 1 
ATOM   2853 C  CA    . VAL A 1 350 ? 6.235   37.652  -9.354  1 27.25  ? 350 VAL A CA    1 1 
ATOM   2854 C  C     . VAL A 1 350 ? 6.437   37.362  -7.89   1 27.62  ? 350 VAL A C     1 1 
ATOM   2855 O  O     . VAL A 1 350 ? 5.487   37.032  -7.2    1 27.88  ? 350 VAL A O     1 1 
ATOM   2856 C  CB    . VAL A 1 350 ? 5.46    38.963  -9.582  1 27.49  ? 350 VAL A CB    1 1 
ATOM   2857 C  CG1   . VAL A 1 350 ? 6.137   40.131  -8.87   1 28.1   ? 350 VAL A CG1   1 1 
ATOM   2858 C  CG2   . VAL A 1 350 ? 5.328   39.245  -11.071 1 27.65  ? 350 VAL A CG2   1 1 
ATOM   2859 N  N     . CYS A 1 351 ? 7.674   37.432  -7.426  1 27.48  ? 351 CYS A N     1 1 
ATOM   2860 C  CA    . CYS A 1 351 ? 7.993   37.211  -6.027  1 27.79  ? 351 CYS A CA    1 1 
ATOM   2861 C  C     . CYS A 1 351 ? 8.562   38.52   -5.484  1 27.58  ? 351 CYS A C     1 1 
ATOM   2862 O  O     . CYS A 1 351 ? 9.463   39.082  -6.088  1 27.77  ? 351 CYS A O     1 1 
ATOM   2863 C  CB    . CYS A 1 351 ? 8.988   36.066  -5.881  1 28.62  ? 351 CYS A CB    1 1 
ATOM   2864 S  SG    . CYS A 1 351 ? 9.329   35.606  -4.169  1 32.12  ? 351 CYS A SG    1 1 
ATOM   2865 N  N     . MET A 1 352 ? 8.012   39.034  -4.386  1 27.03  ? 352 MET A N     1 1 
ATOM   2866 C  CA    . MET A 1 352 ? 8.485   40.284  -3.797  1 26.85  ? 352 MET A CA    1 1 
ATOM   2867 C  C     . MET A 1 352 ? 9.043   39.995  -2.414  1 26.62  ? 352 MET A C     1 1 
ATOM   2868 O  O     . MET A 1 352 ? 8.357   39.404  -1.578  1 27.1   ? 352 MET A O     1 1 
ATOM   2869 C  CB    . MET A 1 352 ? 7.352   41.315  -3.738  1 27.32  ? 352 MET A CB    1 1 
ATOM   2870 C  CG    . MET A 1 352 ? 6.819   41.668  -5.097  1 29.31  ? 352 MET A CG    1 1 
ATOM   2871 S  SD    . MET A 1 352 ? 5.374   42.73   -5.006  1 35.51  ? 352 MET A SD    1 1 
ATOM   2872 C  CE    . MET A 1 352 ? 6.092   44.194  -4.274  1 33.98  ? 352 MET A CE    1 1 
ATOM   2873 N  N     . LEU A 1 353 ? 10.312  40.341  -2.194  1 25.72  ? 353 LEU A N     1 1 
ATOM   2874 C  CA    . LEU A 1 353 ? 10.971  40.054  -0.931  1 25.18  ? 353 LEU A CA    1 1 
ATOM   2875 C  C     . LEU A 1 353 ? 11.788  41.232  -0.49   1 24.29  ? 353 LEU A C     1 1 
ATOM   2876 O  O     . LEU A 1 353 ? 12.467  41.835  -1.315  1 24.08  ? 353 LEU A O     1 1 
ATOM   2877 C  CB    . LEU A 1 353 ? 11.924  38.862  -1.111  1 25.51  ? 353 LEU A CB    1 1 
ATOM   2878 C  CG    . LEU A 1 353 ? 11.291  37.525  -1.451  1 27.65  ? 353 LEU A CG    1 1 
ATOM   2879 C  CD1   . LEU A 1 353 ? 12.333  36.535  -1.876  1 28.44  ? 353 LEU A CD1   1 1 
ATOM   2880 C  CD2   . LEU A 1 353 ? 10.479  36.98   -0.281  1 28.59  ? 353 LEU A CD2   1 1 
ATOM   2881 N  N     . LYS A 1 354 ? 11.772  41.545  0.815   1 23.75  ? 354 LYS A N     1 1 
ATOM   2882 C  CA    . LYS A 1 354 ? 12.639  42.601  1.336   1 23.81  ? 354 LYS A CA    1 1 
ATOM   2883 C  C     . LYS A 1 354 ? 14.095  42.135  1.221   1 23.76  ? 354 LYS A C     1 1 
ATOM   2884 O  O     . LYS A 1 354 ? 14.952  42.892  0.788   1 23.86  ? 354 LYS A O     1 1 
ATOM   2885 C  CB    . LYS A 1 354 ? 12.288  42.985  2.783   1 25.18  ? 354 LYS A CB    1 1 
ATOM   2886 C  CG    . LYS A 1 354 ? 13.035  44.243  3.242   1 27.63  ? 354 LYS A CG    1 1 
ATOM   2887 C  CD    . LYS A 1 354 ? 12.453  44.82   4.509   1 30.53  ? 354 LYS A CD    1 1 
ATOM   2888 C  CE    . LYS A 1 354 ? 13.141  46.095  4.912   1 34.04  ? 354 LYS A CE    1 1 
ATOM   2889 N  NZ    . LYS A 1 354 ? 14.423  45.866  5.626   1 36.42  ? 354 LYS A NZ    1 1 
ATOM   2890 N  N     . GLY A 1 355 ? 14.341  40.873  1.548   1 23.48  ? 355 GLY A N     1 1 
ATOM   2891 C  CA    . GLY A 1 355 ? 15.649  40.267  1.414   1 24.1   ? 355 GLY A CA    1 1 
ATOM   2892 C  C     . GLY A 1 355 ? 16.632  40.603  2.508   1 24.77  ? 355 GLY A C     1 1 
ATOM   2893 O  O     . GLY A 1 355 ? 17.369  39.725  2.962   1 25.03  ? 355 GLY A O     1 1 
ATOM   2894 N  N     . PHE A 1 356 ? 16.696  41.88   2.902   1 24.79  ? 356 PHE A N     1 1 
ATOM   2895 C  CA    . PHE A 1 356 ? 17.705  42.304  3.857   1 25.46  ? 356 PHE A CA    1 1 
ATOM   2896 C  C     . PHE A 1 356 ? 17.156  43.122  4.999   1 27.21  ? 356 PHE A C     1 1 
ATOM   2897 O  O     . PHE A 1 356 ? 16.163  43.835  4.845   1 27.76  ? 356 PHE A O     1 1 
ATOM   2898 C  CB    . PHE A 1 356 ? 18.836  43.049  3.123   1 24.69  ? 356 PHE A CB    1 1 
ATOM   2899 C  CG    . PHE A 1 356 ? 19.347  42.261  1.943   1 24.33  ? 356 PHE A CG    1 1 
ATOM   2900 C  CD1   . PHE A 1 356 ? 18.757  42.389  0.7     1 24.63  ? 356 PHE A CD1   1 1 
ATOM   2901 C  CD2   . PHE A 1 356 ? 20.288  41.267  2.115   1 24.55  ? 356 PHE A CD2   1 1 
ATOM   2902 C  CE1   . PHE A 1 356 ? 19.141  41.577  -0.349  1 24.97  ? 356 PHE A CE1   1 1 
ATOM   2903 C  CE2   . PHE A 1 356 ? 20.691  40.483  1.053   1 24.96  ? 356 PHE A CE2   1 1 
ATOM   2904 C  CZ    . PHE A 1 356 ? 20.117  40.644  -0.169  1 24.59  ? 356 PHE A CZ    1 1 
ATOM   2905 N  N     . LYS A 1 357 ? 17.795  42.991  6.165   1 27.81  ? 357 LYS A N     1 1 
ATOM   2906 C  CA    . LYS A 1 357 ? 17.454  43.737  7.372   1 28.75  ? 357 LYS A CA    1 1 
ATOM   2907 C  C     . LYS A 1 357 ? 18.094  45.169  7.33    1 29.77  ? 357 LYS A C     1 1 
ATOM   2908 O  O     . LYS A 1 357 ? 18.855  45.468  6.405   1 30.26  ? 357 LYS A O     1 1 
ATOM   2909 C  CB    . LYS A 1 357 ? 17.865  42.914  8.605   1 29.92  ? 357 LYS A CB    1 1 
ATOM   2910 C  CG    . LYS A 1 357 ? 16.825  41.862  8.965   1 32.85  ? 357 LYS A CG    1 1 
ATOM   2911 C  CD    . LYS A 1 357 ? 17.392  40.804  9.875   1 37.05  ? 357 LYS A CD    1 1 
ATOM   2912 C  CE    . LYS A 1 357 ? 18.113  39.754  9.078   1 40.89  ? 357 LYS A CE    1 1 
ATOM   2913 N  NZ    . LYS A 1 357 ? 18.953  38.878  9.932   1 43.14  ? 357 LYS A NZ    1 1 
ATOM   2914 N  N     . PRO A 1 358 ? 17.758  46.085  8.265   1 29.87  ? 358 PRO A N     1 1 
ATOM   2915 C  CA    . PRO A 1 358 ? 18.311  47.441  8.206   1 30.04  ? 358 PRO A CA    1 1 
ATOM   2916 C  C     . PRO A 1 358 ? 19.814  47.573  7.968   1 31.13  ? 358 PRO A C     1 1 
ATOM   2917 O  O     . PRO A 1 358 ? 20.226  48.517  7.296   1 31.48  ? 358 PRO A O     1 1 
ATOM   2918 C  CB    . PRO A 1 358 ? 17.927  48.023  9.564   1 30.47  ? 358 PRO A CB    1 1 
ATOM   2919 C  CG    . PRO A 1 358 ? 16.705  47.337  9.924   1 30.95  ? 358 PRO A CG    1 1 
ATOM   2920 C  CD    . PRO A 1 358 ? 16.839  45.944  9.408   1 29.47  ? 358 PRO A CD    1 1 
ATOM   2921 N  N     . ARG A 1 359 ? 20.636  46.67   8.52    1 31.41  ? 359 ARG A N     1 1 
ATOM   2922 C  CA    . ARG A 1 359 ? 22.089  46.774  8.345   1 32.33  ? 359 ARG A CA    1 1 
ATOM   2923 C  C     . ARG A 1 359 ? 22.625  46.13   7.051   1 32.71  ? 359 ARG A C     1 1 
ATOM   2924 O  O     . ARG A 1 359 ? 23.818  46.189  6.797   1 32.39  ? 359 ARG A O     1 1 
ATOM   2925 C  CB    . ARG A 1 359 ? 22.818  46.229  9.582   1 34.1   ? 359 ARG A CB    1 1 
ATOM   2926 C  CG    . ARG A 1 359 ? 22.386  46.953  10.85   1 38     ? 359 ARG A CG    1 1 
ATOM   2927 C  CD    . ARG A 1 359 ? 23.061  46.435  12.098  1 42.49  ? 359 ARG A CD    1 1 
ATOM   2928 N  NE    . ARG A 1 359 ? 22.583  45.104  12.461  1 47.37  ? 359 ARG A NE    1 1 
ATOM   2929 C  CZ    . ARG A 1 359 ? 22.66   44.585  13.683  1 50.82  ? 359 ARG A CZ    1 1 
ATOM   2930 N  NH1   . ARG A 1 359 ? 23.178  45.293  14.682  1 50.91  ? 359 ARG A NH1   1 1 
ATOM   2931 N  NH2   . ARG A 1 359 ? 22.199  43.363  13.922  1 50.63  ? 359 ARG A NH2   1 1 
ATOM   2932 N  N     . GLY A 1 360 ? 21.75   45.556  6.238   1 33.34  ? 360 GLY A N     1 1 
ATOM   2933 C  CA    . GLY A 1 360 ? 22.155  44.898  5.004   1 34.57  ? 360 GLY A CA    1 1 
ATOM   2934 C  C     . GLY A 1 360 ? 22.368  43.401  5.147   1 36.03  ? 360 GLY A C     1 1 
ATOM   2935 O  O     . GLY A 1 360 ? 22.736  42.734  4.176   1 36.49  ? 360 GLY A O     1 1 
ATOM   2936 N  N     . ASP A 1 361 ? 22.167  42.854  6.364   1 36.41  ? 361 ASP A N     1 1 
ATOM   2937 C  CA    . ASP A 1 361 ? 22.324  41.425  6.626   1 37.01  ? 361 ASP A CA    1 1 
ATOM   2938 C  C     . ASP A 1 361 ? 21.122  40.668  6.062   1 37.22  ? 361 ASP A C     1 1 
ATOM   2939 O  O     . ASP A 1 361 ? 19.999  41.156  6.17    1 37.15  ? 361 ASP A O     1 1 
ATOM   2940 C  CB    . ASP A 1 361 ? 22.565  41.144  8.125   1 39.04  ? 361 ASP A CB    1 1 
ATOM   2941 C  CG    . ASP A 1 361 ? 21.58   41.76   9.104   1 44.29  ? 361 ASP A CG    1 1 
ATOM   2942 O  OD1   . ASP A 1 361 ? 21.324  42.978  9.004   1 45.19  ? 361 ASP A OD1   1 1 
ATOM   2943 O  OD2   . ASP A 1 361 ? 21.092  41.029  9.995   1 46.8   ? 361 ASP A OD2   1 1 
ATOM   2944 N  N     . ASP A 1 362 ? 21.356  39.518  5.408   1 37.24  ? 362 ASP A N     1 1 
ATOM   2945 C  CA    . ASP A 1 362 ? 20.276  38.8    4.745   1 37.91  ? 362 ASP A CA    1 1 
ATOM   2946 C  C     . ASP A 1 362 ? 19.264  38.168  5.689   1 37.98  ? 362 ASP A C     1 1 
ATOM   2947 O  O     . ASP A 1 362 ? 19.615  37.728  6.787   1 38.22  ? 362 ASP A O     1 1 
ATOM   2948 C  CB    . ASP A 1 362 ? 20.81   37.769  3.736   1 40.4   ? 362 ASP A CB    1 1 
ATOM   2949 C  CG    . ASP A 1 362 ? 21.144  36.39   4.285   1 46.7   ? 362 ASP A CG    1 1 
ATOM   2950 O  OD1   . ASP A 1 362 ? 20.225  35.528  4.343   1 47.21  ? 362 ASP A OD1   1 1 
ATOM   2951 O  OD2   . ASP A 1 362 ? 22.325  36.163  4.641   1 49.83  ? 362 ASP A OD2   1 1 
ATOM   2952 N  N     . ASN A 1 363 ? 18.003  38.105  5.215   1 37.49  ? 363 ASN A N     1 1 
ATOM   2953 C  CA    . ASN A 1 363 ? 16.855  37.528  5.902   1 37.43  ? 363 ASN A CA    1 1 
ATOM   2954 C  C     . ASN A 1 363 ? 16.921  36.038  5.717   1 36.8   ? 363 ASN A C     1 1 
ATOM   2955 O  O     . ASN A 1 363 ? 16.798  35.583  4.582   1 37.28  ? 363 ASN A O     1 1 
ATOM   2956 C  CB    . ASN A 1 363 ? 15.541  38.012  5.25    1 38.93  ? 363 ASN A CB    1 1 
ATOM   2957 C  CG    . ASN A 1 363 ? 15.217  39.484  5.41    1 42.18  ? 363 ASN A CG    1 1 
ATOM   2958 O  OD1   . ASN A 1 363 ? 15.919  40.23   6.111   1 43.29  ? 363 ASN A OD1   1 1 
ATOM   2959 N  ND2   . ASN A 1 363 ? 14.132  39.941  4.77    1 42.55  ? 363 ASN A ND2   1 1 
ATOM   2960 N  N     . ARG A 1 364 ? 17.074  35.269  6.805   1 35.77  ? 364 ARG A N     1 1 
ATOM   2961 C  CA    . ARG A 1 364 ? 17.101  33.805  6.69    1 35.11  ? 364 ARG A CA    1 1 
ATOM   2962 C  C     . ARG A 1 364 ? 15.856  33.194  6.046   1 34.41  ? 364 ARG A C     1 1 
ATOM   2963 O  O     . ARG A 1 364 ? 16.013  32.354  5.167   1 34.51  ? 364 ARG A O     1 1 
ATOM   2964 C  CB    . ARG A 1 364 ? 17.375  33.129  8.037   1 35.84  ? 364 ARG A CB    1 1 
ATOM   2965 C  CG    . ARG A 1 364 ? 18.162  31.833  7.908   1 37.62  ? 364 ARG A CG    1 1 
ATOM   2966 C  CD    . ARG A 1 364 ? 19.634  32.09   7.619   1 39.91  ? 364 ARG A CD    1 1 
ATOM   2967 N  NE    . ARG A 1 364 ? 20.242  32.946  8.639   1 41.72  ? 364 ARG A NE    1 1 
ATOM   2968 C  CZ    . ARG A 1 364 ? 20.563  34.226  8.456   1 43.31  ? 364 ARG A CZ    1 1 
ATOM   2969 N  NH1   . ARG A 1 364 ? 20.378  34.802  7.276   1 42.87  ? 364 ARG A NH1   1 1 
ATOM   2970 N  NH2   . ARG A 1 364 ? 21.074  34.936  9.452   1 42.98  ? 364 ARG A NH2   1 1 
ATOM   2971 N  N     . PRO A 1 365 ? 14.626  33.591  6.429   1 33.65  ? 365 PRO A N     1 1 
ATOM   2972 C  CA    . PRO A 1 365 ? 13.441  32.982  5.808   1 33.47  ? 365 PRO A CA    1 1 
ATOM   2973 C  C     . PRO A 1 365 ? 13.343  33.193  4.307   1 33.45  ? 365 PRO A C     1 1 
ATOM   2974 O  O     . PRO A 1 365 ? 12.781  32.354  3.612   1 33.7   ? 365 PRO A O     1 1 
ATOM   2975 C  CB    . PRO A 1 365 ? 12.278  33.679  6.508   1 34.15  ? 365 PRO A CB    1 1 
ATOM   2976 C  CG    . PRO A 1 365 ? 12.839  34.197  7.773   1 34.71  ? 365 PRO A CG    1 1 
ATOM   2977 C  CD    . PRO A 1 365 ? 14.237  34.576  7.455   1 33.12  ? 365 PRO A CD    1 1 
ATOM   2978 N  N     . ASP A 1 366 ? 13.879  34.31   3.806   1 33.03  ? 366 ASP A N     1 1 
ATOM   2979 C  CA    . ASP A 1 366 ? 13.821  34.627  2.376   1 32.84  ? 366 ASP A CA    1 1 
ATOM   2980 C  C     . ASP A 1 366 ? 14.591  33.634  1.497   1 32.44  ? 366 ASP A C     1 1 
ATOM   2981 O  O     . ASP A 1 366 ? 14.289  33.496  0.307   1 32.15  ? 366 ASP A O     1 1 
ATOM   2982 C  CB    . ASP A 1 366 ? 14.264  36.084  2.115   1 33.48  ? 366 ASP A CB    1 1 
ATOM   2983 C  CG    . ASP A 1 366 ? 13.299  37.136  2.644   1 35.3   ? 366 ASP A CG    1 1 
ATOM   2984 O  OD1   . ASP A 1 366 ? 12.324  36.763  3.338   1 35.3   ? 366 ASP A OD1   1 1 
ATOM   2985 O  OD2   . ASP A 1 366 ? 13.523  38.32   2.381   1 36.69  ? 366 ASP A OD2   1 1 
ATOM   2986 N  N     . ARG A 1 367 ? 15.554  32.92   2.085   1 32.32  ? 367 ARG A N     1 1 
ATOM   2987 C  CA    . ARG A 1 367 ? 16.322  31.928  1.351   1 32.83  ? 367 ARG A CA    1 1 
ATOM   2988 C  C     . ARG A 1 367 ? 15.43   30.78   0.831   1 33.67  ? 367 ARG A C     1 1 
ATOM   2989 O  O     . ARG A 1 367 ? 15.779  30.16   -0.168  1 34.63  ? 367 ARG A O     1 1 
ATOM   2990 C  CB    . ARG A 1 367 ? 17.463  31.374  2.214   1 33.49  ? 367 ARG A CB    1 1 
ATOM   2991 C  CG    . ARG A 1 367 ? 18.406  32.429  2.75    1 35.58  ? 367 ARG A CG    1 1 
ATOM   2992 C  CD    . ARG A 1 367 ? 19.482  31.783  3.586   1 38.1   ? 367 ARG A CD    1 1 
ATOM   2993 N  NE    . ARG A 1 367 ? 20.557  32.723  3.894   1 40.09  ? 367 ARG A NE    1 1 
ATOM   2994 C  CZ    . ARG A 1 367 ? 21.807  32.369  4.164   1 41.75  ? 367 ARG A CZ    1 1 
ATOM   2995 N  NH1   . ARG A 1 367 ? 22.16   31.087  4.158   1 41.24  ? 367 ARG A NH1   1 1 
ATOM   2996 N  NH2   . ARG A 1 367 ? 22.72   33.293  4.431   1 41.62  ? 367 ARG A NH2   1 1 
ATOM   2997 N  N     . GLY A 1 368 ? 14.307  30.505  1.499   1 32.81  ? 368 GLY A N     1 1 
ATOM   2998 C  CA    . GLY A 1 368 ? 13.399  29.445  1.083   1 32.36  ? 368 GLY A CA    1 1 
ATOM   2999 C  C     . GLY A 1 368 ? 12.21   29.902  0.257   1 31.61  ? 368 GLY A C     1 1 
ATOM   3000 O  O     . GLY A 1 368 ? 11.434  29.074  -0.217  1 31.39  ? 368 GLY A O     1 1 
ATOM   3001 N  N     . ALA A 1 369 ? 12.072  31.213  0.045   1 31.19  ? 369 ALA A N     1 1 
ATOM   3002 C  CA    . ALA A 1 369 ? 10.971  31.772  -0.731  1 31.22  ? 369 ALA A CA    1 1 
ATOM   3003 C  C     . ALA A 1 369 ? 11.018  31.317  -2.201  1 30.92  ? 369 ALA A C     1 1 
ATOM   3004 O  O     . ALA A 1 369 ? 10.052  30.719  -2.665  1 30.85  ? 369 ALA A O     1 1 
ATOM   3005 C  CB    . ALA A 1 369 ? 10.955  33.3    -0.614  1 31.4   ? 369 ALA A CB    1 1 
ATOM   3006 N  N     . LEU A 1 370 ? 12.144  31.541  -2.915  1 30.54  ? 370 LEU A N     1 1 
ATOM   3007 C  CA    . LEU A 1 370 ? 12.251  31.077  -4.298  1 30.08  ? 370 LEU A CA    1 1 
ATOM   3008 C  C     . LEU A 1 370 ? 12.173  29.552  -4.389  1 29.28  ? 370 LEU A C     1 1 
ATOM   3009 O  O     . LEU A 1 370 ? 11.341  29.064  -5.149  1 29.18  ? 370 LEU A O     1 1 
ATOM   3010 C  CB    . LEU A 1 370 ? 13.465  31.666  -5.033  1 30.01  ? 370 LEU A CB    1 1 
ATOM   3011 C  CG    . LEU A 1 370 ? 13.4    33.171  -5.311  1 31.1   ? 370 LEU A CG    1 1 
ATOM   3012 C  CD1   . LEU A 1 370 ? 14.463  33.552  -6.263  1 31.64  ? 370 LEU A CD1   1 1 
ATOM   3013 C  CD2   . LEU A 1 370 ? 12.054  33.595  -5.933  1 31.51  ? 370 LEU A CD2   1 1 
ATOM   3014 N  N     . PRO A 1 371 ? 12.884  28.78   -3.532  1 28.55  ? 371 PRO A N     1 1 
ATOM   3015 C  CA    . PRO A 1 371 ? 12.711  27.321  -3.54   1 28.05  ? 371 PRO A CA    1 1 
ATOM   3016 C  C     . PRO A 1 371 ? 11.254  26.89   -3.362  1 27.74  ? 371 PRO A C     1 1 
ATOM   3017 O  O     . PRO A 1 371 ? 10.834  25.934  -4.007  1 28.31  ? 371 PRO A O     1 1 
ATOM   3018 C  CB    . PRO A 1 371 ? 13.56   26.875  -2.35   1 28.58  ? 371 PRO A CB    1 1 
ATOM   3019 C  CG    . PRO A 1 371 ? 14.62   27.912  -2.25   1 28.99  ? 371 PRO A CG    1 1 
ATOM   3020 C  CD    . PRO A 1 371 ? 13.915  29.184  -2.557  1 27.72  ? 371 PRO A CD    1 1 
ATOM   3021 N  N     . LEU A 1 372 ? 10.472  27.611  -2.534  1 26.42  ? 372 LEU A N     1 1 
ATOM   3022 C  CA    . LEU A 1 372 ? 9.07    27.272  -2.334  1 25.84  ? 372 LEU A CA    1 1 
ATOM   3023 C  C     . LEU A 1 372 ? 8.286   27.466  -3.636  1 26.11  ? 372 LEU A C     1 1 
ATOM   3024 O  O     . LEU A 1 372 ? 7.484   26.602  -3.997  1 26.45  ? 372 LEU A O     1 1 
ATOM   3025 C  CB    . LEU A 1 372 ? 8.488   28.102  -1.188  1 25.42  ? 372 LEU A CB    1 1 
ATOM   3026 C  CG    . LEU A 1 372 ? 6.986   28.076  -0.991  1 26.06  ? 372 LEU A CG    1 1 
ATOM   3027 C  CD1   . LEU A 1 372 ? 6.508   26.701  -0.546  1 26.56  ? 372 LEU A CD1   1 1 
ATOM   3028 C  CD2   . LEU A 1 372 ? 6.587   29.114  0.007   1 26.3   ? 372 LEU A CD2   1 1 
ATOM   3029 N  N     . VAL A 1 373 ? 8.567   28.56   -4.37   1 25.81  ? 373 VAL A N     1 1 
ATOM   3030 C  CA    . VAL A 1 373 ? 7.942   28.868  -5.659  1 25.92  ? 373 VAL A CA    1 1 
ATOM   3031 C  C     . VAL A 1 373 ? 8.303   27.807  -6.689  1 26.28  ? 373 VAL A C     1 1 
ATOM   3032 O  O     . VAL A 1 373 ? 7.443   27.355  -7.443  1 26.2   ? 373 VAL A O     1 1 
ATOM   3033 C  CB    . VAL A 1 373 ? 8.361   30.265  -6.153  1 26.48  ? 373 VAL A CB    1 1 
ATOM   3034 C  CG1   . VAL A 1 373 ? 7.844   30.53   -7.559  1 27.06  ? 373 VAL A CG1   1 1 
ATOM   3035 C  CG2   . VAL A 1 373 ? 7.871   31.334  -5.205  1 26.92  ? 373 VAL A CG2   1 1 
ATOM   3036 N  N     . ALA A 1 374 ? 9.577   27.411  -6.716  1 26.58  ? 374 ALA A N     1 1 
ATOM   3037 C  CA    . ALA A 1 374 ? 10.072  26.393  -7.627  1 27.45  ? 374 ALA A CA    1 1 
ATOM   3038 C  C     . ALA A 1 374 ? 9.468   25.024  -7.307  1 28.51  ? 374 ALA A C     1 1 
ATOM   3039 O  O     . ALA A 1 374 ? 9.193   24.254  -8.221  1 28.99  ? 374 ALA A O     1 1 
ATOM   3040 C  CB    . ALA A 1 374 ? 11.581  26.327  -7.554  1 27.6   ? 374 ALA A CB    1 1 
ATOM   3041 N  N     . MET A 1 375 ? 9.236   24.723  -6.028  1 28.68  ? 375 MET A N     1 1 
ATOM   3042 C  CA    . MET A 1 375 ? 8.624   23.456  -5.642  1 29.46  ? 375 MET A CA    1 1 
ATOM   3043 C  C     . MET A 1 375 ? 7.161   23.418  -6.066  1 30.05  ? 375 MET A C     1 1 
ATOM   3044 O  O     . MET A 1 375 ? 6.677   22.38   -6.511  1 30.37  ? 375 MET A O     1 1 
ATOM   3045 C  CB    . MET A 1 375 ? 8.747   23.238  -4.133  1 30.37  ? 375 MET A CB    1 1 
ATOM   3046 C  CG    . MET A 1 375 ? 10.138  22.871  -3.703  1 32.89  ? 375 MET A CG    1 1 
ATOM   3047 S  SD    . MET A 1 375 ? 10.292  22.767  -1.917  1 36.71  ? 375 MET A SD    1 1 
ATOM   3048 C  CE    . MET A 1 375 ? 9.515   21.178  -1.632  1 32.33  ? 375 MET A CE    1 1 
ATOM   3049 N  N     . LEU A 1 376 ? 6.458   24.549  -5.934  1 30.08  ? 376 LEU A N     1 1 
ATOM   3050 C  CA    . LEU A 1 376 ? 5.047   24.661  -6.286  1 30.49  ? 376 LEU A CA    1 1 
ATOM   3051 C  C     . LEU A 1 376 ? 4.781   24.707  -7.794  1 30.79  ? 376 LEU A C     1 1 
ATOM   3052 O  O     . LEU A 1 376 ? 3.924   23.973  -8.286  1 31.04  ? 376 LEU A O     1 1 
ATOM   3053 C  CB    . LEU A 1 376 ? 4.436   25.905  -5.621  1 30.63  ? 376 LEU A CB    1 1 
ATOM   3054 C  CG    . LEU A 1 376 ? 4.227   25.826  -4.127  1 31.99  ? 376 LEU A CG    1 1 
ATOM   3055 C  CD1   . LEU A 1 376 ? 3.857   27.171  -3.578  1 32.41  ? 376 LEU A CD1   1 1 
ATOM   3056 C  CD2   . LEU A 1 376 ? 3.142   24.843  -3.798  1 32.83  ? 376 LEU A CD2   1 1 
ATOM   3057 N  N     . ALA A 1 377 ? 5.492   25.574  -8.523  1 30.55  ? 377 ALA A N     1 1 
ATOM   3058 C  CA    . ALA A 1 377 ? 5.232   25.769  -9.94   1 30.73  ? 377 ALA A CA    1 1 
ATOM   3059 C  C     . ALA A 1 377 ? 6.302   25.281  -10.907 1 30.64  ? 377 ALA A C     1 1 
ATOM   3060 O  O     . ALA A 1 377 ? 6.182   25.533  -12.107 1 30.82  ? 377 ALA A O     1 1 
ATOM   3061 C  CB    . ALA A 1 377 ? 4.962   27.229  -10.194 1 30.89  ? 377 ALA A CB    1 1 
ATOM   3062 N  N     . GLY A 1 378 ? 7.318   24.6    -10.41  1 30.26  ? 378 GLY A N     1 1 
ATOM   3063 C  CA    . GLY A 1 378 ? 8.392   24.123  -11.269 1 30.8   ? 378 GLY A CA    1 1 
ATOM   3064 C  C     . GLY A 1 378 ? 9.503   25.148  -11.407 1 31.17  ? 378 GLY A C     1 1 
ATOM   3065 O  O     . GLY A 1 378 ? 9.246   26.346  -11.522 1 31.22  ? 378 GLY A O     1 1 
ATOM   3066 N  N     . GLU A 1 379 ? 10.753  24.687  -11.364 1 31.25  ? 379 GLU A N     1 1 
ATOM   3067 C  CA    . GLU A 1 379 ? 11.904  25.572  -11.499 1 31.71  ? 379 GLU A CA    1 1 
ATOM   3068 C  C     . GLU A 1 379 ? 11.986  26.194  -12.889 1 32.58  ? 379 GLU A C     1 1 
ATOM   3069 O  O     . GLU A 1 379 ? 12.54   27.269  -13.028 1 32.89  ? 379 GLU A O     1 1 
ATOM   3070 C  CB    . GLU A 1 379 ? 13.202  24.833  -11.162 1 33.06  ? 379 GLU A CB    1 1 
ATOM   3071 C  CG    . GLU A 1 379 ? 13.571  23.758  -12.165 1 36.56  ? 379 GLU A CG    1 1 
ATOM   3072 C  CD    . GLU A 1 379 ? 14.789  22.956  -11.764 1 41.94  ? 379 GLU A CD    1 1 
ATOM   3073 O  OE1   . GLU A 1 379 ? 14.915  22.632  -10.56  1 43.2   ? 379 GLU A OE1   1 1 
ATOM   3074 O  OE2   . GLU A 1 379 ? 15.619  22.647  -12.649 1 43.49  ? 379 GLU A OE2   1 1 
ATOM   3075 N  N     . ASN A 1 380 ? 11.417  25.55   -13.907 1 33.01  ? 380 ASN A N     1 1 
ATOM   3076 C  CA    . ASN A 1 380 ? 11.414  26.057  -15.271 1 34.15  ? 380 ASN A CA    1 1 
ATOM   3077 C  C     . ASN A 1 380 ? 10.466  27.265  -15.469 1 34.34  ? 380 ASN A C     1 1 
ATOM   3078 O  O     . ASN A 1 380 ? 10.59   27.953  -16.483 1 34.61  ? 380 ASN A O     1 1 
ATOM   3079 C  CB    . ASN A 1 380 ? 11.093  24.929  -16.255 1 36.44  ? 380 ASN A CB    1 1 
ATOM   3080 C  CG    . ASN A 1 380 ? 9.952   24.032  -15.797 1 42.22  ? 380 ASN A CG    1 1 
ATOM   3081 O  OD1   . ASN A 1 380 ? 10.169  22.928  -15.249 1 44.1   ? 380 ASN A OD1   1 1 
ATOM   3082 N  ND2   . ASN A 1 380 ? 8.705   24.499  -15.985 1 43.43  ? 380 ASN A ND2   1 1 
ATOM   3083 N  N     . ALA A 1 381 ? 9.54    27.533  -14.514 1 33.92  ? 381 ALA A N     1 1 
ATOM   3084 C  CA    . ALA A 1 381 ? 8.616   28.672  -14.611 1 34.18  ? 381 ALA A CA    1 1 
ATOM   3085 C  C     . ALA A 1 381 ? 9.374   29.992  -14.583 1 34.65  ? 381 ALA A C     1 1 
ATOM   3086 O  O     . ALA A 1 381 ? 10.414  30.084  -13.928 1 35     ? 381 ALA A O     1 1 
ATOM   3087 C  CB    . ALA A 1 381 ? 7.612   28.643  -13.473 1 34.11  ? 381 ALA A CB    1 1 
ATOM   3088 N  N     . GLN A 1 382 ? 8.871   31.007  -15.3   1 34.44  ? 382 GLN A N     1 1 
ATOM   3089 C  CA    . GLN A 1 382 ? 9.542   32.298  -15.336 1 34.88  ? 382 GLN A CA    1 1 
ATOM   3090 C  C     . GLN A 1 382 ? 9.282   33.075  -14.062 1 34.98  ? 382 GLN A C     1 1 
ATOM   3091 O  O     . GLN A 1 382 ? 8.134   33.318  -13.714 1 35.46  ? 382 GLN A O     1 1 
ATOM   3092 C  CB    . GLN A 1 382 ? 9.17    33.087  -16.587 1 36.67  ? 382 GLN A CB    1 1 
ATOM   3093 C  CG    . GLN A 1 382 ? 9.694   32.42   -17.837 1 40.2   ? 382 GLN A CG    1 1 
ATOM   3094 C  CD    . GLN A 1 382 ? 9.452   33.256  -19.051 1 44.8   ? 382 GLN A CD    1 1 
ATOM   3095 O  OE1   . GLN A 1 382 ? 9.612   34.48   -19.038 1 45.54  ? 382 GLN A OE1   1 1 
ATOM   3096 N  NE2   . GLN A 1 382 ? 9.072   32.596  -20.13  1 46.03  ? 382 GLN A NE2   1 1 
ATOM   3097 N  N     . ILE A 1 383 ? 10.343  33.406  -13.327 1 34.32  ? 383 ILE A N     1 1 
ATOM   3098 C  CA    . ILE A 1 383 ? 10.212  34.097  -12.053 1 33.88  ? 383 ILE A CA    1 1 
ATOM   3099 C  C     . ILE A 1 383 ? 10.834  35.488  -12.093 1 33.14  ? 383 ILE A C     1 1 
ATOM   3100 O  O     . ILE A 1 383 ? 11.984  35.668  -12.488 1 33.2   ? 383 ILE A O     1 1 
ATOM   3101 C  CB    . ILE A 1 383 ? 10.804  33.21   -10.924 1 34.41  ? 383 ILE A CB    1 1 
ATOM   3102 C  CG1   . ILE A 1 383 ? 10.079  31.846  -10.856 1 35.06  ? 383 ILE A CG1   1 1 
ATOM   3103 C  CG2   . ILE A 1 383 ? 10.784  33.923  -9.576  1 35     ? 383 ILE A CG2   1 1 
ATOM   3104 C  CD1   . ILE A 1 383 ? 10.739  30.823  -9.991  1 36.18  ? 383 ILE A CD1   1 1 
ATOM   3105 N  N     . PHE A 1 384 ? 10.056  36.47   -11.695 1 32.2   ? 384 PHE A N     1 1 
ATOM   3106 C  CA    . PHE A 1 384 ? 10.473  37.857  -11.62  1 31.96  ? 384 PHE A CA    1 1 
ATOM   3107 C  C     . PHE A 1 384 ? 10.615  38.143  -10.126 1 31.46  ? 384 PHE A C     1 1 
ATOM   3108 O  O     . PHE A 1 384 ? 9.604   38.183  -9.429  1 31.89  ? 384 PHE A O     1 1 
ATOM   3109 C  CB    . PHE A 1 384 ? 9.349   38.716  -12.206 1 31.81  ? 384 PHE A CB    1 1 
ATOM   3110 C  CG    . PHE A 1 384 ? 9.607   40.193  -12.334 1 32.38  ? 384 PHE A CG    1 1 
ATOM   3111 C  CD1   . PHE A 1 384 ? 9.513   41.028  -11.235 1 33.13  ? 384 PHE A CD1   1 1 
ATOM   3112 C  CD2   . PHE A 1 384 ? 9.847   40.761  -13.57  1 33.23  ? 384 PHE A CD2   1 1 
ATOM   3113 C  CE1   . PHE A 1 384 ? 9.712   42.392  -11.362 1 33.82  ? 384 PHE A CE1   1 1 
ATOM   3114 C  CE2   . PHE A 1 384 ? 10.042  42.127  -13.694 1 33.93  ? 384 PHE A CE2   1 1 
ATOM   3115 C  CZ    . PHE A 1 384 ? 9.942   42.936  -12.594 1 33.7   ? 384 PHE A CZ    1 1 
ATOM   3116 N  N     . THR A 1 385 ? 11.845  38.312  -9.625  1 30.21  ? 385 THR A N     1 1 
ATOM   3117 C  CA    . THR A 1 385 ? 12.091  38.554  -8.204  1 29.51  ? 385 THR A CA    1 1 
ATOM   3118 C  C     . THR A 1 385 ? 12.365  40.025  -7.923  1 28.48  ? 385 THR A C     1 1 
ATOM   3119 O  O     . THR A 1 385 ? 13.328  40.573  -8.434  1 28.83  ? 385 THR A O     1 1 
ATOM   3120 C  CB    . THR A 1 385 ? 13.253  37.673  -7.743  1 30.89  ? 385 THR A CB    1 1 
ATOM   3121 O  OG1   . THR A 1 385 ? 12.926  36.308  -8.007  1 32.02  ? 385 THR A OG1   1 1 
ATOM   3122 C  CG2   . THR A 1 385 ? 13.593  37.859  -6.275  1 31.3   ? 385 THR A CG2   1 1 
ATOM   3123 N  N     . PHE A 1 386 ? 11.543  40.655  -7.101  1 27.32  ? 386 PHE A N     1 1 
ATOM   3124 C  CA    . PHE A 1 386 ? 11.705  42.054  -6.761  1 27.12  ? 386 PHE A CA    1 1 
ATOM   3125 C  C     . PHE A 1 386 ? 12.203  42.193  -5.333  1 27.24  ? 386 PHE A C     1 1 
ATOM   3126 O  O     . PHE A 1 386 ? 11.52   41.771  -4.404  1 27.56  ? 386 PHE A O     1 1 
ATOM   3127 C  CB    . PHE A 1 386 ? 10.38   42.779  -6.939  1 26.7   ? 386 PHE A CB    1 1 
ATOM   3128 C  CG    . PHE A 1 386 ? 10.403  44.25   -6.62   1 27.06  ? 386 PHE A CG    1 1 
ATOM   3129 C  CD1   . PHE A 1 386 ? 10.762  45.178  -7.582  1 27.73  ? 386 PHE A CD1   1 1 
ATOM   3130 C  CD2   . PHE A 1 386 ? 9.96    44.714  -5.396  1 27.61  ? 386 PHE A CD2   1 1 
ATOM   3131 C  CE1   . PHE A 1 386 ? 10.723  46.537  -7.31   1 28.18  ? 386 PHE A CE1   1 1 
ATOM   3132 C  CE2   . PHE A 1 386 ? 9.936   46.072  -5.122  1 28.19  ? 386 PHE A CE2   1 1 
ATOM   3133 C  CZ    . PHE A 1 386 ? 10.318  46.974  -6.08   1 27.92  ? 386 PHE A CZ    1 1 
ATOM   3134 N  N     . ILE A 1 387 ? 13.386  42.806  -5.164  1 26.7   ? 387 ILE A N     1 1 
ATOM   3135 C  CA    . ILE A 1 387 ? 14.044  43.037  -3.88   1 26.82  ? 387 ILE A CA    1 1 
ATOM   3136 C  C     . ILE A 1 387 ? 14.024  44.523  -3.531  1 27.28  ? 387 ILE A C     1 1 
ATOM   3137 O  O     . ILE A 1 387 ? 14.334  45.352  -4.386  1 27.59  ? 387 ILE A O     1 1 
ATOM   3138 C  CB    . ILE A 1 387 ? 15.491  42.496  -3.936  1 27.08  ? 387 ILE A CB    1 1 
ATOM   3139 C  CG1   . ILE A 1 387 ? 15.531  41.027  -4.383  1 28.05  ? 387 ILE A CG1   1 1 
ATOM   3140 C  CG2   . ILE A 1 387 ? 16.204  42.688  -2.613  1 27.39  ? 387 ILE A CG2   1 1 
ATOM   3141 C  CD1   . ILE A 1 387 ? 14.714  40.119  -3.533  1 29.49  ? 387 ILE A CD1   1 1 
ATOM   3142 N  N     . TYR A 1 388 ? 13.682  44.869  -2.282  1 27.03  ? 388 TYR A N     1 1 
ATOM   3143 C  CA    . TYR A 1 388 ? 13.601  46.276  -1.884  1 27.14  ? 388 TYR A CA    1 1 
ATOM   3144 C  C     . TYR A 1 388 ? 14.317  46.64   -0.564  1 27.2   ? 388 TYR A C     1 1 
ATOM   3145 O  O     . TYR A 1 388 ? 14.233  47.786  -0.112  1 27.21  ? 388 TYR A O     1 1 
ATOM   3146 C  CB    . TYR A 1 388 ? 12.135  46.721  -1.833  1 27.01  ? 388 TYR A CB    1 1 
ATOM   3147 C  CG    . TYR A 1 388 ? 11.243  45.837  -0.988  1 27.32  ? 388 TYR A CG    1 1 
ATOM   3148 C  CD1   . TYR A 1 388 ? 10.583  44.751  -1.541  1 28.02  ? 388 TYR A CD1   1 1 
ATOM   3149 C  CD2   . TYR A 1 388 ? 11.041  46.103  0.356   1 28.05  ? 388 TYR A CD2   1 1 
ATOM   3150 C  CE1   . TYR A 1 388 ? 9.752   43.946  -0.774  1 28.85  ? 388 TYR A CE1   1 1 
ATOM   3151 C  CE2   . TYR A 1 388 ? 10.21   45.309  1.133   1 28.89  ? 388 TYR A CE2   1 1 
ATOM   3152 C  CZ    . TYR A 1 388 ? 9.57    44.225  0.567   1 29.7   ? 388 TYR A CZ    1 1 
ATOM   3153 O  OH    . TYR A 1 388 ? 8.771   43.424  1.349   1 31.17  ? 388 TYR A OH    1 1 
ATOM   3154 N  N     . GLY A 1 389 ? 14.992  45.676  0.04    1 27.02  ? 389 GLY A N     1 1 
ATOM   3155 C  CA    . GLY A 1 389 ? 15.707  45.892  1.289   1 27.32  ? 389 GLY A CA    1 1 
ATOM   3156 C  C     . GLY A 1 389 ? 17.061  46.528  1.092   1 27.18  ? 389 GLY A C     1 1 
ATOM   3157 O  O     . GLY A 1 389 ? 17.555  46.625  -0.032  1 27.13  ? 389 GLY A O     1 1 
ATOM   3158 N  N     . PRO A 1 390 ? 17.69   46.965  2.186   1 27.01  ? 390 PRO A N     1 1 
ATOM   3159 C  CA    . PRO A 1 390 ? 18.968  47.669  2.047   1 27.05  ? 390 PRO A CA    1 1 
ATOM   3160 C  C     . PRO A 1 390 ? 20.135  46.783  1.685   1 27.64  ? 390 PRO A C     1 1 
ATOM   3161 O  O     . PRO A 1 390 ? 20.266  45.68   2.205   1 28.23  ? 390 PRO A O     1 1 
ATOM   3162 C  CB    . PRO A 1 390 ? 19.169  48.343  3.403   1 27.62  ? 390 PRO A CB    1 1 
ATOM   3163 C  CG    . PRO A 1 390 ? 17.95   48.074  4.198   1 28.19  ? 390 PRO A CG    1 1 
ATOM   3164 C  CD    . PRO A 1 390 ? 17.227  46.932  3.582   1 26.53  ? 390 PRO A CD    1 1 
ATOM   3165 N  N     . LEU A 1 391 ? 20.993  47.273  0.791   1 27.43  ? 391 LEU A N     1 1 
ATOM   3166 C  CA    . LEU A 1 391 ? 22.188  46.546  0.38    1 27.68  ? 391 LEU A CA    1 1 
ATOM   3167 C  C     . LEU A 1 391 ? 23.455  47.262  0.869   1 28.37  ? 391 LEU A C     1 1 
ATOM   3168 O  O     . LEU A 1 391 ? 23.53   48.492  0.816   1 28.53  ? 391 LEU A O     1 1 
ATOM   3169 C  CB    . LEU A 1 391 ? 22.26   46.456  -1.148  1 27.18  ? 391 LEU A CB    1 1 
ATOM   3170 C  CG    . LEU A 1 391 ? 21.087  45.865  -1.858  1 27.51  ? 391 LEU A CG    1 1 
ATOM   3171 C  CD1   . LEU A 1 391 ? 21.308  45.91   -3.341  1 27.85  ? 391 LEU A CD1   1 1 
ATOM   3172 C  CD2   . LEU A 1 391 ? 20.88   44.458  -1.435  1 27.89  ? 391 LEU A CD2   1 1 
ATOM   3173 N  N     . ILE A 1 392 ? 24.452  46.496  1.315   1 28.41  ? 392 ILE A N     1 1 
ATOM   3174 C  CA    . ILE A 1 392 ? 25.735  47.08   1.678   1 29.14  ? 392 ILE A CA    1 1 
ATOM   3175 C  C     . ILE A 1 392 ? 26.432  47.45   0.353   1 29.12  ? 392 ILE A C     1 1 
ATOM   3176 O  O     . ILE A 1 392 ? 26.148  46.842  -0.691  1 29.28  ? 392 ILE A O     1 1 
ATOM   3177 C  CB    . ILE A 1 392 ? 26.576  46.107  2.539   1 30.2   ? 392 ILE A CB    1 1 
ATOM   3178 C  CG1   . ILE A 1 392 ? 26.782  44.764  1.804   1 31.59  ? 392 ILE A CG1   1 1 
ATOM   3179 C  CG2   . ILE A 1 392 ? 25.923  45.914  3.907   1 30.74  ? 392 ILE A CG2   1 1 
ATOM   3180 C  CD1   . ILE A 1 392 ? 27.637  43.764  2.513   1 33.39  ? 392 ILE A CD1   1 1 
ATOM   3181 N  N     . LYS A 1 393 ? 27.324  48.454  0.375   1 28.62  ? 393 LYS A N     1 1 
ATOM   3182 C  CA    . LYS A 1 393 ? 28.007  48.88   -0.844  1 28.68  ? 393 LYS A CA    1 1 
ATOM   3183 C  C     . LYS A 1 393 ? 28.736  47.731  -1.57   1 28.79  ? 393 LYS A C     1 1 
ATOM   3184 O  O     . LYS A 1 393 ? 28.689  47.646  -2.793  1 29.1   ? 393 LYS A O     1 1 
ATOM   3185 C  CB    . LYS A 1 393 ? 28.936  50.054  -0.556  1 30.33  ? 393 LYS A CB    1 1 
ATOM   3186 C  CG    . LYS A 1 393 ? 29.627  50.607  -1.79   1 34.45  ? 393 LYS A CG    1 1 
ATOM   3187 C  CD    . LYS A 1 393 ? 28.653  51.191  -2.813  1 38.43  ? 393 LYS A CD    1 1 
ATOM   3188 C  CE    . LYS A 1 393 ? 29.373  52.157  -3.717  1 42.36  ? 393 LYS A CE    1 1 
ATOM   3189 N  NZ    . LYS A 1 393 ? 30.741  51.668  -4.083  1 44.45  ? 393 LYS A NZ    1 1 
ATOM   3190 N  N     . GLY A 1 394 ? 29.32   46.814  -0.81   1 28.35  ? 394 GLY A N     1 1 
ATOM   3191 C  CA    . GLY A 1 394 ? 29.992  45.657  -1.384  1 28.21  ? 394 GLY A CA    1 1 
ATOM   3192 C  C     . GLY A 1 394 ? 29.072  44.751  -2.184  1 27.88  ? 394 GLY A C     1 1 
ATOM   3193 O  O     . GLY A 1 394 ? 29.497  44.175  -3.184  1 27.76  ? 394 GLY A O     1 1 
ATOM   3194 N  N     . ALA A 1 395 ? 27.794  44.628  -1.77   1 27.5   ? 395 ALA A N     1 1 
ATOM   3195 C  CA    . ALA A 1 395 ? 26.837  43.767  -2.469  1 27.39  ? 395 ALA A CA    1 1 
ATOM   3196 C  C     . ALA A 1 395 ? 26.428  44.341  -3.807  1 27.39  ? 395 ALA A C     1 1 
ATOM   3197 O  O     . ALA A 1 395 ? 26.423  43.615  -4.796  1 27.29  ? 395 ALA A O     1 1 
ATOM   3198 C  CB    . ALA A 1 395 ? 25.618  43.505  -1.605  1 27.24  ? 395 ALA A CB    1 1 
ATOM   3199 N  N     . ILE A 1 396 ? 26.153  45.647  -3.862  1 27.55  ? 396 ILE A N     1 1 
ATOM   3200 C  CA    . ILE A 1 396 ? 25.77   46.279  -5.12   1 28.42  ? 396 ILE A CA    1 1 
ATOM   3201 C  C     . ILE A 1 396 ? 26.943  46.306  -6.103  1 29.17  ? 396 ILE A C     1 1 
ATOM   3202 O  O     . ILE A 1 396 ? 26.735  46.113  -7.298  1 29.12  ? 396 ILE A O     1 1 
ATOM   3203 C  CB    . ILE A 1 396 ? 25.104  47.66   -4.907  1 29.03  ? 396 ILE A CB    1 1 
ATOM   3204 C  CG1   . ILE A 1 396 ? 24.392  48.15   -6.177  1 30.14  ? 396 ILE A CG1   1 1 
ATOM   3205 C  CG2   . ILE A 1 396 ? 26.076  48.692  -4.374  1 29.51  ? 396 ILE A CG2   1 1 
ATOM   3206 C  CD1   . ILE A 1 396 ? 23.314  47.223  -6.711  1 31.65  ? 396 ILE A CD1   1 1 
ATOM   3207 N  N     . ASN A 1 397 ? 28.18   46.432  -5.596  1 29.74  ? 397 ASN A N     1 1 
ATOM   3208 C  CA    . ASN A 1 397 ? 29.38   46.421  -6.421  1 30.41  ? 397 ASN A CA    1 1 
ATOM   3209 C  C     . ASN A 1 397 ? 29.538  45.059  -7.093  1 31.06  ? 397 ASN A C     1 1 
ATOM   3210 O  O     . ASN A 1 397 ? 29.846  44.993  -8.285  1 31.17  ? 397 ASN A O     1 1 
ATOM   3211 C  CB    . ASN A 1 397 ? 30.597  46.732  -5.567  1 31.59  ? 397 ASN A CB    1 1 
ATOM   3212 C  CG    . ASN A 1 397 ? 30.884  48.197  -5.444  1 35.08  ? 397 ASN A CG    1 1 
ATOM   3213 O  OD1   . ASN A 1 397 ? 30.419  49.017  -6.243  1 36.04  ? 397 ASN A OD1   1 1 
ATOM   3214 N  ND2   . ASN A 1 397 ? 31.676  48.56   -4.447  1 36.27  ? 397 ASN A ND2   1 1 
ATOM   3215 N  N     . LEU A 1 398 ? 29.299  43.973  -6.337  1 31.22  ? 398 LEU A N     1 1 
ATOM   3216 C  CA    . LEU A 1 398 ? 29.395  42.621  -6.877  1 31.62  ? 398 LEU A CA    1 1 
ATOM   3217 C  C     . LEU A 1 398 ? 28.277  42.33   -7.866  1 32.39  ? 398 LEU A C     1 1 
ATOM   3218 O  O     . LEU A 1 398 ? 28.498  41.594  -8.814  1 32.28  ? 398 LEU A O     1 1 
ATOM   3219 C  CB    . LEU A 1 398 ? 29.425  41.577  -5.766  1 31.5   ? 398 LEU A CB    1 1 
ATOM   3220 C  CG    . LEU A 1 398 ? 30.804  41.051  -5.444  1 32.6   ? 398 LEU A CG    1 1 
ATOM   3221 C  CD1   . LEU A 1 398 ? 31.611  42.08   -4.73   1 33.38  ? 398 LEU A CD1   1 1 
ATOM   3222 C  CD2   . LEU A 1 398 ? 30.728  39.824  -4.599  1 33.15  ? 398 LEU A CD2   1 1 
ATOM   3223 N  N     . ILE A 1 399 ? 27.104  42.947  -7.694  1 33.03  ? 399 ILE A N     1 1 
ATOM   3224 C  CA    . ILE A 1 399 ? 26.003  42.794  -8.635  1 34.47  ? 399 ILE A CA    1 1 
ATOM   3225 C  C     . ILE A 1 399 ? 26.419  43.397  -9.995  1 35.49  ? 399 ILE A C     1 1 
ATOM   3226 O  O     . ILE A 1 399 ? 26.189  42.783  -11.041 1 36.14  ? 399 ILE A O     1 1 
ATOM   3227 C  CB    . ILE A 1 399 ? 24.72   43.462  -8.055  1 35.26  ? 399 ILE A CB    1 1 
ATOM   3228 C  CG1   . ILE A 1 399 ? 24.099  42.59   -6.955  1 36.04  ? 399 ILE A CG1   1 1 
ATOM   3229 C  CG2   . ILE A 1 399 ? 23.686  43.792  -9.142  1 35.78  ? 399 ILE A CG2   1 1 
ATOM   3230 C  CD1   . ILE A 1 399 ? 23.204  43.319  -6.033  1 37.04  ? 399 ILE A CD1   1 1 
ATOM   3231 N  N     . ASP A 1 400 ? 27.081  44.561  -9.974  1 35.32  ? 400 ASP A N     1 1 
ATOM   3232 C  CA    . ASP A 1 400 ? 27.523  45.216  -11.201 1 35.98  ? 400 ASP A CA    1 1 
ATOM   3233 C  C     . ASP A 1 400 ? 28.854  44.672  -11.765 1 36.74  ? 400 ASP A C     1 1 
ATOM   3234 O  O     . ASP A 1 400 ? 29.247  45.032  -12.871 1 37.05  ? 400 ASP A O     1 1 
ATOM   3235 C  CB    . ASP A 1 400 ? 27.634  46.724  -10.961 1 37.84  ? 400 ASP A CB    1 1 
ATOM   3236 C  CG    . ASP A 1 400 ? 26.369  47.369  -10.435 1 41.73  ? 400 ASP A CG    1 1 
ATOM   3237 O  OD1   . ASP A 1 400 ? 25.278  46.819  -10.685 1 42.46  ? 400 ASP A OD1   1 1 
ATOM   3238 O  OD2   . ASP A 1 400 ? 26.473  48.425  -9.769  1 43.31  ? 400 ASP A OD2   1 1 
ATOM   3239 N  N     . GLN A 1 401 ? 29.552  43.829  -11.012 1 36.92  ? 401 GLN A N     1 1 
ATOM   3240 C  CA    . GLN A 1 401 ? 30.823  43.271  -11.44  1 37.58  ? 401 GLN A CA    1 1 
ATOM   3241 C  C     . GLN A 1 401 ? 30.678  41.792  -11.899 1 37.45  ? 401 GLN A C     1 1 
ATOM   3242 O  O     . GLN A 1 401 ? 31.065  41.455  -13.019 1 37.59  ? 401 GLN A O     1 1 
ATOM   3243 C  CB    . GLN A 1 401 ? 31.871  43.447  -10.308 1 39.63  ? 401 GLN A CB    1 1 
ATOM   3244 C  CG    . GLN A 1 401 ? 33.148  42.608  -10.461 1 43.82  ? 401 GLN A CG    1 1 
ATOM   3245 C  CD    . GLN A 1 401 ? 33.794  42.265  -9.131  1 48.27  ? 401 GLN A CD    1 1 
ATOM   3246 O  OE1   . GLN A 1 401 ? 33.541  42.916  -8.1    1 50.25  ? 401 GLN A OE1   1 1 
ATOM   3247 N  NE2   . GLN A 1 401 ? 34.65   41.236  -9.131  1 47.84  ? 401 GLN A NE2   1 1 
ATOM   3248 N  N     . ASP A 1 402 ? 30.113  40.931  -11.037 1 36.89  ? 402 ASP A N     1 1 
ATOM   3249 C  CA    . ASP A 1 402 ? 29.972  39.496  -11.262 1 37.08  ? 402 ASP A CA    1 1 
ATOM   3250 C  C     . ASP A 1 402 ? 28.927  38.997  -10.271 1 36.92  ? 402 ASP A C     1 1 
ATOM   3251 O  O     . ASP A 1 402 ? 29.262  38.75   -9.114  1 37.25  ? 402 ASP A O     1 1 
ATOM   3252 C  CB    . ASP A 1 402 ? 31.326  38.825  -10.952 1 38.98  ? 402 ASP A CB    1 1 
ATOM   3253 C  CG    . ASP A 1 402 ? 31.43   37.345  -11.251 1 43.56  ? 402 ASP A CG    1 1 
ATOM   3254 O  OD1   . ASP A 1 402 ? 30.417  36.754  -11.712 1 44.85  ? 402 ASP A OD1   1 1 
ATOM   3255 O  OD2   . ASP A 1 402 ? 32.521  36.771  -11.021 1 44.75  ? 402 ASP A OD2   1 1 
ATOM   3256 N  N     . ILE A 1 403 ? 27.664  38.884  -10.697 1 36.15  ? 403 ILE A N     1 1 
ATOM   3257 C  CA    . ILE A 1 403 ? 26.592  38.469  -9.802  1 35.89  ? 403 ILE A CA    1 1 
ATOM   3258 C  C     . ILE A 1 403 ? 26.818  37.049  -9.247  1 35.38  ? 403 ILE A C     1 1 
ATOM   3259 O  O     . ILE A 1 403 ? 26.47   36.795  -8.095  1 35.51  ? 403 ILE A O     1 1 
ATOM   3260 C  CB    . ILE A 1 403 ? 25.202  38.665  -10.473 1 36.52  ? 403 ILE A CB    1 1 
ATOM   3261 C  CG1   . ILE A 1 403 ? 24.035  38.411  -9.5    1 37.49  ? 403 ILE A CG1   1 1 
ATOM   3262 C  CG2   . ILE A 1 403 ? 25.05   37.856  -11.752 1 37.01  ? 403 ILE A CG2   1 1 
ATOM   3263 C  CD1   . ILE A 1 403 ? 24.04   39.25   -8.27   1 38.91  ? 403 ILE A CD1   1 1 
ATOM   3264 N  N     . ASN A 1 404 ? 27.472  36.156  -10.013 1 34.61  ? 404 ASN A N     1 1 
ATOM   3265 C  CA    . ASN A 1 404 ? 27.739  34.792  -9.541  1 34.37  ? 404 ASN A CA    1 1 
ATOM   3266 C  C     . ASN A 1 404 ? 28.749  34.731  -8.402  1 34.37  ? 404 ASN A C     1 1 
ATOM   3267 O  O     . ASN A 1 404 ? 28.713  33.799  -7.597  1 34.3   ? 404 ASN A O     1 1 
ATOM   3268 C  CB    . ASN A 1 404 ? 28.162  33.889  -10.681 1 34.87  ? 404 ASN A CB    1 1 
ATOM   3269 C  CG    . ASN A 1 404 ? 27.027  33.603  -11.61  1 37.12  ? 404 ASN A CG    1 1 
ATOM   3270 O  OD1   . ASN A 1 404 ? 25.873  33.514  -11.199 1 37.52  ? 404 ASN A OD1   1 1 
ATOM   3271 N  ND2   . ASN A 1 404 ? 27.327  33.454  -12.885 1 38.13  ? 404 ASN A ND2   1 1 
ATOM   3272 N  N     . LYS A 1 405 ? 29.64   35.727  -8.323  1 34.1   ? 405 LYS A N     1 1 
ATOM   3273 C  CA    . LYS A 1 405 ? 30.61   35.813  -7.239  1 34.22  ? 405 LYS A CA    1 1 
ATOM   3274 C  C     . LYS A 1 405 ? 29.877  36.137  -5.931  1 34.01  ? 405 LYS A C     1 1 
ATOM   3275 O  O     . LYS A 1 405 ? 30.231  35.581  -4.888  1 34.52  ? 405 LYS A O     1 1 
ATOM   3276 C  CB    . LYS A 1 405 ? 31.683  36.869  -7.543  1 36.06  ? 405 LYS A CB    1 1 
ATOM   3277 C  CG    . LYS A 1 405 ? 32.891  36.757  -6.629  1 40.36  ? 405 LYS A CG    1 1 
ATOM   3278 C  CD    . LYS A 1 405 ? 34.061  37.597  -7.126  1 44.76  ? 405 LYS A CD    1 1 
ATOM   3279 C  CE    . LYS A 1 405 ? 35.317  37.315  -6.338  1 48.53  ? 405 LYS A CE    1 1 
ATOM   3280 N  NZ    . LYS A 1 405 ? 35.994  38.569  -5.909  1 51.23  ? 405 LYS A NZ    1 1 
ATOM   3281 N  N     . LEU A 1 406 ? 28.827  36.995  -5.997  1 32.9   ? 406 LEU A N     1 1 
ATOM   3282 C  CA    . LEU A 1 406 ? 27.995  37.35   -4.853  1 32.49  ? 406 LEU A CA    1 1 
ATOM   3283 C  C     . LEU A 1 406 ? 27.176  36.134  -4.427  1 32.48  ? 406 LEU A C     1 1 
ATOM   3284 O  O     . LEU A 1 406 ? 27.128  35.81   -3.24   1 32.83  ? 406 LEU A O     1 1 
ATOM   3285 C  CB    . LEU A 1 406 ? 27.07   38.527  -5.21   1 32.24  ? 406 LEU A CB    1 1 
ATOM   3286 C  CG    . LEU A 1 406 ? 26.141  39.004  -4.11   1 33.27  ? 406 LEU A CG    1 1 
ATOM   3287 C  CD1   . LEU A 1 406 ? 26.916  39.437  -2.894  1 33.76  ? 406 LEU A CD1   1 1 
ATOM   3288 C  CD2   . LEU A 1 406 ? 25.287  40.146  -4.586  1 33.88  ? 406 LEU A CD2   1 1 
ATOM   3289 N  N     . ALA A 1 407 ? 26.58   35.432  -5.403  1 31.87  ? 407 ALA A N     1 1 
ATOM   3290 C  CA    . ALA A 1 407 ? 25.809  34.218  -5.162  1 31.88  ? 407 ALA A CA    1 1 
ATOM   3291 C  C     . ALA A 1 407 ? 26.663  33.15   -4.466  1 32.02  ? 407 ALA A C     1 1 
ATOM   3292 O  O     . ALA A 1 407 ? 26.152  32.387  -3.648  1 31.84  ? 407 ALA A O     1 1 
ATOM   3293 C  CB    . ALA A 1 407 ? 25.287  33.68   -6.48   1 31.96  ? 407 ALA A CB    1 1 
ATOM   3294 N  N     . LYS A 1 408 ? 27.97   33.11   -4.777  1 32.11  ? 408 LYS A N     1 1 
ATOM   3295 C  CA    . LYS A 1 408 ? 28.882  32.152  -4.18   1 32.56  ? 408 LYS A CA    1 1 
ATOM   3296 C  C     . LYS A 1 408 ? 29.109  32.412  -2.694  1 32.44  ? 408 LYS A C     1 1 
ATOM   3297 O  O     . LYS A 1 408 ? 29.193  31.45   -1.931  1 32.59  ? 408 LYS A O     1 1 
ATOM   3298 C  CB    . LYS A 1 408 ? 30.21   32.117  -4.941  1 35.04  ? 408 LYS A CB    1 1 
ATOM   3299 C  CG    . LYS A 1 408 ? 30.331  30.944  -5.913  1 39.58  ? 408 LYS A CG    1 1 
ATOM   3300 C  CD    . LYS A 1 408 ? 31.757  30.801  -6.484  1 44.04  ? 408 LYS A CD    1 1 
ATOM   3301 C  CE    . LYS A 1 408 ? 32.105  31.921  -7.432  1 48.5   ? 408 LYS A CE    1 1 
ATOM   3302 N  NZ    . LYS A 1 408 ? 31.01   32.17   -8.412  1 51.93  ? 408 LYS A NZ    1 1 
ATOM   3303 N  N     . ARG A 1 409 ? 29.176  33.691  -2.266  1 32.12  ? 409 ARG A N     1 1 
ATOM   3304 C  CA    . ARG A 1 409 ? 29.416  34.001  -0.847  1 32.5   ? 409 ARG A CA    1 1 
ATOM   3305 C  C     . ARG A 1 409 ? 28.193  34.034  0.049   1 31.56  ? 409 ARG A C     1 1 
ATOM   3306 O  O     . ARG A 1 409 ? 28.335  33.867  1.259   1 31.35  ? 409 ARG A O     1 1 
ATOM   3307 C  CB    . ARG A 1 409 ? 30.114  35.351  -0.645  1 35.15  ? 409 ARG A CB    1 1 
ATOM   3308 C  CG    . ARG A 1 409 ? 31.116  35.808  -1.686  1 40.21  ? 409 ARG A CG    1 1 
ATOM   3309 C  CD    . ARG A 1 409 ? 31.795  37.075  -1.184  1 45.59  ? 409 ARG A CD    1 1 
ATOM   3310 N  NE    . ARG A 1 409 ? 30.843  38.111  -0.758  1 50.68  ? 409 ARG A NE    1 1 
ATOM   3311 C  CZ    . ARG A 1 409 ? 31.148  39.122  0.054   1 54.47  ? 409 ARG A CZ    1 1 
ATOM   3312 N  NH1   . ARG A 1 409 ? 32.381  39.244  0.541   1 53.87  ? 409 ARG A NH1   1 1 
ATOM   3313 N  NH2   . ARG A 1 409 ? 30.227  40.026  0.376   1 54.98  ? 409 ARG A NH2   1 1 
ATOM   3314 N  N     . ASN A 1 410 ? 27.034  34.36   -0.5    1 30.91  ? 410 ASN A N     1 1 
ATOM   3315 C  CA    . ASN A 1 410 ? 25.841  34.51   0.309   1 31.13  ? 410 ASN A CA    1 1 
ATOM   3316 C  C     . ASN A 1 410 ? 24.726  33.579  -0.142  1 31.76  ? 410 ASN A C     1 1 
ATOM   3317 O  O     . ASN A 1 410 ? 24.338  33.599  -1.31   1 32.3   ? 410 ASN A O     1 1 
ATOM   3318 C  CB    . ASN A 1 410 ? 25.406  35.962  0.263   1 31.76  ? 410 ASN A CB    1 1 
ATOM   3319 C  CG    . ASN A 1 410 ? 24.247  36.279  1.144   1 33.9   ? 410 ASN A CG    1 1 
ATOM   3320 O  OD1   . ASN A 1 410 ? 23.1    36.107  0.758   1 35.13  ? 410 ASN A OD1   1 1 
ATOM   3321 N  ND2   . ASN A 1 410 ? 24.516  36.767  2.341   1 34.13  ? 410 ASN A ND2   1 1 
ATOM   3322 N  N     . GLY A 1 411 ? 24.199  32.801  0.801   1 31.4   ? 411 GLY A N     1 1 
ATOM   3323 C  CA    . GLY A 1 411 ? 23.125  31.84   0.564   1 31.36  ? 411 GLY A CA    1 1 
ATOM   3324 C  C     . GLY A 1 411 ? 21.823  32.418  0.038   1 30.95  ? 411 GLY A C     1 1 
ATOM   3325 O  O     . GLY A 1 411 ? 21.114  31.756  -0.725  1 30.79  ? 411 GLY A O     1 1 
ATOM   3326 N  N     . LEU A 1 412 ? 21.494  33.65   0.439   1 30.59  ? 412 LEU A N     1 1 
ATOM   3327 C  CA    . LEU A 1 412 ? 20.287  34.301  -0.048  1 30.58  ? 412 LEU A CA    1 1 
ATOM   3328 C  C     . LEU A 1 412 ? 20.491  34.712  -1.499  1 30.62  ? 412 LEU A C     1 1 
ATOM   3329 O  O     . LEU A 1 412 ? 19.617  34.461  -2.328  1 30.74  ? 412 LEU A O     1 1 
ATOM   3330 C  CB    . LEU A 1 412 ? 19.888  35.503  0.817   1 30.61  ? 412 LEU A CB    1 1 
ATOM   3331 C  CG    . LEU A 1 412 ? 18.658  36.225  0.328   1 32.17  ? 412 LEU A CG    1 1 
ATOM   3332 C  CD1   . LEU A 1 412 ? 17.455  35.341  0.364   1 32.73  ? 412 LEU A CD1   1 1 
ATOM   3333 C  CD2   . LEU A 1 412 ? 18.397  37.448  1.105   1 32.9   ? 412 LEU A CD2   1 1 
ATOM   3334 N  N     . TRP A 1 413 ? 21.662  35.291  -1.824  1 30.34  ? 413 TRP A N     1 1 
ATOM   3335 C  CA    . TRP A 1 413 ? 21.954  35.654  -3.208  1 30.39  ? 413 TRP A CA    1 1 
ATOM   3336 C  C     . TRP A 1 413 ? 22.023  34.426  -4.093  1 30.38  ? 413 TRP A C     1 1 
ATOM   3337 O  O     . TRP A 1 413 ? 21.512  34.468  -5.208  1 30.8   ? 413 TRP A O     1 1 
ATOM   3338 C  CB    . TRP A 1 413 ? 23.2    36.53   -3.331  1 30.21  ? 413 TRP A CB    1 1 
ATOM   3339 C  CG    . TRP A 1 413 ? 22.926  37.952  -2.96   1 30.75  ? 413 TRP A CG    1 1 
ATOM   3340 C  CD1   . TRP A 1 413 ? 23.306  38.584  -1.816  1 31.75  ? 413 TRP A CD1   1 1 
ATOM   3341 C  CD2   . TRP A 1 413 ? 22.112  38.888  -3.686  1 30.87  ? 413 TRP A CD2   1 1 
ATOM   3342 N  NE1   . TRP A 1 413 ? 22.821  39.874  -1.803  1 32     ? 413 TRP A NE1   1 1 
ATOM   3343 C  CE2   . TRP A 1 413 ? 22.082  40.084  -2.94   1 31.56  ? 413 TRP A CE2   1 1 
ATOM   3344 C  CE3   . TRP A 1 413 ? 21.432  38.843  -4.91   1 31.34  ? 413 TRP A CE3   1 1 
ATOM   3345 C  CZ2   . TRP A 1 413 ? 21.406  41.223  -3.381  1 31.78  ? 413 TRP A CZ2   1 1 
ATOM   3346 C  CZ3   . TRP A 1 413 ? 20.746  39.967  -5.333  1 31.81  ? 413 TRP A CZ3   1 1 
ATOM   3347 C  CH2   . TRP A 1 413 ? 20.737  41.137  -4.571  1 31.75  ? 413 TRP A CH2   1 1 
ATOM   3348 N  N     . LYS A 1 414 ? 22.535  33.298  -3.557  1 29.5   ? 414 LYS A N     1 1 
ATOM   3349 C  CA    . LYS A 1 414 ? 22.598  32.014  -4.253  1 29.14  ? 414 LYS A CA    1 1 
ATOM   3350 C  C     . LYS A 1 414 ? 21.193  31.584  -4.665  1 28.31  ? 414 LYS A C     1 1 
ATOM   3351 O  O     . LYS A 1 414 ? 20.995  31.167  -5.797  1 28.45  ? 414 LYS A O     1 1 
ATOM   3352 C  CB    . LYS A 1 414 ? 23.218  30.948  -3.33   1 31.19  ? 414 LYS A CB    1 1 
ATOM   3353 C  CG    . LYS A 1 414 ? 23.85   29.763  -4.054  1 35.05  ? 414 LYS A CG    1 1 
ATOM   3354 C  CD    . LYS A 1 414 ? 24.302  28.689  -3.063  1 38.92  ? 414 LYS A CD    1 1 
ATOM   3355 C  CE    . LYS A 1 414 ? 25.798  28.63   -2.876  1 42.94  ? 414 LYS A CE    1 1 
ATOM   3356 N  NZ    . LYS A 1 414 ? 26.352  29.867  -2.257  1 45.59  ? 414 LYS A NZ    1 1 
ATOM   3357 N  N     . SER A 1 415 ? 20.223  31.742  -3.756  1 27.41  ? 415 SER A N     1 1 
ATOM   3358 C  CA    . SER A 1 415 ? 18.823  31.402  -3.966  1 27.2   ? 415 SER A CA    1 1 
ATOM   3359 C  C     . SER A 1 415 ? 18.227  32.264  -5.084  1 26.83  ? 415 SER A C     1 1 
ATOM   3360 O  O     . SER A 1 415 ? 17.596  31.736  -5.998  1 26.84  ? 415 SER A O     1 1 
ATOM   3361 C  CB    . SER A 1 415 ? 18.052  31.596  -2.663  1 28.4   ? 415 SER A CB    1 1 
ATOM   3362 O  OG    . SER A 1 415 ? 16.738  31.085  -2.742  1 31     ? 415 SER A OG    1 1 
ATOM   3363 N  N     . PHE A 1 416 ? 18.484  33.582  -5.039  1 26.3   ? 416 PHE A N     1 1 
ATOM   3364 C  CA    . PHE A 1 416 ? 17.989  34.54   -6.023  1 26.14  ? 416 PHE A CA    1 1 
ATOM   3365 C  C     . PHE A 1 416 ? 18.552  34.317  -7.416  1 25.42  ? 416 PHE A C     1 1 
ATOM   3366 O  O     . PHE A 1 416 ? 17.808  34.34   -8.388  1 25.48  ? 416 PHE A O     1 1 
ATOM   3367 C  CB    . PHE A 1 416 ? 18.31   35.975  -5.593  1 26.42  ? 416 PHE A CB    1 1 
ATOM   3368 C  CG    . PHE A 1 416 ? 17.636  36.476  -4.349  1 27.47  ? 416 PHE A CG    1 1 
ATOM   3369 C  CD1   . PHE A 1 416 ? 16.458  35.907  -3.906  1 28.68  ? 416 PHE A CD1   1 1 
ATOM   3370 C  CD2   . PHE A 1 416 ? 18.138  37.57   -3.666  1 28.35  ? 416 PHE A CD2   1 1 
ATOM   3371 C  CE1   . PHE A 1 416 ? 15.822  36.391  -2.776  1 29.71  ? 416 PHE A CE1   1 1 
ATOM   3372 C  CE2   . PHE A 1 416 ? 17.497  38.059  -2.543  1 29.42  ? 416 PHE A CE2   1 1 
ATOM   3373 C  CZ    . PHE A 1 416 ? 16.338  37.47   -2.108  1 29.62  ? 416 PHE A CZ    1 1 
ATOM   3374 N  N     . VAL A 1 417 ? 19.866  34.161  -7.521  1 24.73  ? 417 VAL A N     1 1 
ATOM   3375 C  CA    . VAL A 1 417 ? 20.517  34.004  -8.809  1 24.74  ? 417 VAL A CA    1 1 
ATOM   3376 C  C     . VAL A 1 417 ? 20.168  32.669  -9.47   1 24.98  ? 417 VAL A C     1 1 
ATOM   3377 O  O     . VAL A 1 417 ? 20.036  32.599  -10.688 1 25.11  ? 417 VAL A O     1 1 
ATOM   3378 C  CB    . VAL A 1 417 ? 22.039  34.245  -8.674  1 25.06  ? 417 VAL A CB    1 1 
ATOM   3379 C  CG1   . VAL A 1 417 ? 22.73   34.137  -10.015 1 25.27  ? 417 VAL A CG1   1 1 
ATOM   3380 C  CG2   . VAL A 1 417 ? 22.309  35.615  -8.07   1 25.6   ? 417 VAL A CG2   1 1 
ATOM   3381 N  N     . SER A 1 418 ? 19.953  31.627  -8.67   1 24.89  ? 418 SER A N     1 1 
ATOM   3382 C  CA    . SER A 1 418 ? 19.658  30.303  -9.2    1 25.1   ? 418 SER A CA    1 1 
ATOM   3383 C  C     . SER A 1 418 ? 18.236  30.138  -9.694  1 25.62  ? 418 SER A C     1 1 
ATOM   3384 O  O     . SER A 1 418 ? 18.014  29.321  -10.589 1 26.17  ? 418 SER A O     1 1 
ATOM   3385 C  CB    . SER A 1 418 ? 19.943  29.233  -8.152  1 25.79  ? 418 SER A CB    1 1 
ATOM   3386 O  OG    . SER A 1 418 ? 21.279  29.247  -7.677  1 27.34  ? 418 SER A OG    1 1 
ATOM   3387 N  N     . LEU A 1 419 ? 17.259  30.857  -9.1    1 25.23  ? 419 LEU A N     1 1 
ATOM   3388 C  CA    . LEU A 1 419 ? 15.861  30.628  -9.468  1 25.09  ? 419 LEU A CA    1 1 
ATOM   3389 C  C     . LEU A 1 419 ? 15.117  31.771  -10.15  1 25.05  ? 419 LEU A C     1 1 
ATOM   3390 O  O     . LEU A 1 419 ? 14.012  31.532  -10.63  1 25.26  ? 419 LEU A O     1 1 
ATOM   3391 C  CB    . LEU A 1 419 ? 15.077  30.168  -8.248  1 24.97  ? 419 LEU A CB    1 1 
ATOM   3392 C  CG    . LEU A 1 419 ? 15.469  28.773  -7.792  1 25.62  ? 419 LEU A CG    1 1 
ATOM   3393 C  CD1   . LEU A 1 419 ? 14.957  28.476  -6.412  1 26.06  ? 419 LEU A CD1   1 1 
ATOM   3394 C  CD2   . LEU A 1 419 ? 15.022  27.739  -8.783  1 25.88  ? 419 LEU A CD2   1 1 
ATOM   3395 N  N     . SER A 1 420 ? 15.697  32.964  -10.24  1 25.01  ? 420 SER A N     1 1 
ATOM   3396 C  CA    . SER A 1 420 ? 15.031  34.081  -10.906 1 25.95  ? 420 SER A CA    1 1 
ATOM   3397 C  C     . SER A 1 420 ? 15.411  34.203  -12.369 1 27.61  ? 420 SER A C     1 1 
ATOM   3398 O  O     . SER A 1 420 ? 16.592  34.19   -12.704 1 28.46  ? 420 SER A O     1 1 
ATOM   3399 C  CB    . SER A 1 420 ? 15.384  35.41   -10.243 1 26.42  ? 420 SER A CB    1 1 
ATOM   3400 O  OG    . SER A 1 420 ? 15.402  35.36   -8.83   1 27.92  ? 420 SER A OG    1 1 
ATOM   3401 N  N     . ASP A 1 421 ? 14.426  34.411  -13.231 1 28.1   ? 421 ASP A N     1 1 
ATOM   3402 C  CA    . ASP A 1 421 ? 14.687  34.725  -14.628 1 29.05  ? 421 ASP A CA    1 1 
ATOM   3403 C  C     . ASP A 1 421 ? 14.984  36.239  -14.741 1 29.2   ? 421 ASP A C     1 1 
ATOM   3404 O  O     . ASP A 1 421 ? 15.768  36.638  -15.593 1 29.21  ? 421 ASP A O     1 1 
ATOM   3405 C  CB    . ASP A 1 421 ? 13.512  34.311  -15.512 1 31.63  ? 421 ASP A CB    1 1 
ATOM   3406 C  CG    . ASP A 1 421 ? 13.379  32.808  -15.584 1 37.73  ? 421 ASP A CG    1 1 
ATOM   3407 O  OD1   . ASP A 1 421 ? 12.748  32.229  -14.68  1 39.17  ? 421 ASP A OD1   1 1 
ATOM   3408 O  OD2   . ASP A 1 421 ? 13.935  32.206  -16.531 1 39.94  ? 421 ASP A OD2   1 1 
ATOM   3409 N  N     . PHE A 1 422 ? 14.379  37.076  -13.87  1 29.14  ? 422 PHE A N     1 1 
ATOM   3410 C  CA    . PHE A 1 422 ? 14.603  38.521  -13.831 1 29.45  ? 422 PHE A CA    1 1 
ATOM   3411 C  C     . PHE A 1 422 ? 14.76   38.934  -12.385 1 29.34  ? 422 PHE A C     1 1 
ATOM   3412 O  O     . PHE A 1 422 ? 13.957  38.534  -11.551 1 29.66  ? 422 PHE A O     1 1 
ATOM   3413 C  CB    . PHE A 1 422 ? 13.421  39.293  -14.434 1 29.59  ? 422 PHE A CB    1 1 
ATOM   3414 C  CG    . PHE A 1 422 ? 12.945  38.747  -15.751 1 30.6   ? 422 PHE A CG    1 1 
ATOM   3415 C  CD1   . PHE A 1 422 ? 13.593  39.074  -16.928 1 31.41  ? 422 PHE A CD1   1 1 
ATOM   3416 C  CD2   . PHE A 1 422 ? 11.874  37.871  -15.809 1 31.66  ? 422 PHE A CD2   1 1 
ATOM   3417 C  CE1   . PHE A 1 422 ? 13.165  38.556  -18.14  1 32.33  ? 422 PHE A CE1   1 1 
ATOM   3418 C  CE2   . PHE A 1 422 ? 11.455  37.344  -17.021 1 32.53  ? 422 PHE A CE2   1 1 
ATOM   3419 C  CZ    . PHE A 1 422 ? 12.105  37.688  -18.179 1 32.29  ? 422 PHE A CZ    1 1 
ATOM   3420 N  N     . ILE A 1 423 ? 15.789  39.711  -12.077 1 28.89  ? 423 ILE A N     1 1 
ATOM   3421 C  CA    . ILE A 1 423 ? 15.998  40.192  -10.717 1 29.08  ? 423 ILE A CA    1 1 
ATOM   3422 C  C     . ILE A 1 423 ? 15.861  41.69   -10.763 1 29.14  ? 423 ILE A C     1 1 
ATOM   3423 O  O     . ILE A 1 423 ? 16.614  42.344  -11.474 1 29.1   ? 423 ILE A O     1 1 
ATOM   3424 C  CB    . ILE A 1 423 ? 17.386  39.794  -10.16  1 29.58  ? 423 ILE A CB    1 1 
ATOM   3425 C  CG1   . ILE A 1 423 ? 17.541  38.273  -10.055 1 30.19  ? 423 ILE A CG1   1 1 
ATOM   3426 C  CG2   . ILE A 1 423 ? 17.64   40.467  -8.811  1 30.13  ? 423 ILE A CG2   1 1 
ATOM   3427 C  CD1   . ILE A 1 423 ? 18.95   37.816  -9.853  1 31.06  ? 423 ILE A CD1   1 1 
ATOM   3428 N  N     . VAL A 1 424 ? 14.897  42.237  -10.035 1 28.91  ? 424 VAL A N     1 1 
ATOM   3429 C  CA    . VAL A 1 424 ? 14.699  43.669  -9.988  1 29.28  ? 424 VAL A CA    1 1 
ATOM   3430 C  C     . VAL A 1 424 ? 14.988  44.182  -8.615  1 29.49  ? 424 VAL A C     1 1 
ATOM   3431 O  O     . VAL A 1 424 ? 14.416  43.689  -7.654  1 29.84  ? 424 VAL A O     1 1 
ATOM   3432 C  CB    . VAL A 1 424 ? 13.301  44.051  -10.437 1 30.08  ? 424 VAL A CB    1 1 
ATOM   3433 C  CG1   . VAL A 1 424 ? 13.1    45.558  -10.333 1 30.68  ? 424 VAL A CG1   1 1 
ATOM   3434 C  CG2   . VAL A 1 424 ? 13.083  43.573  -11.854 1 30.63  ? 424 VAL A CG2   1 1 
ATOM   3435 N  N     . LEU A 1 425 ? 15.889  45.151  -8.514  1 28.96  ? 425 LEU A N     1 1 
ATOM   3436 C  CA    . LEU A 1 425 ? 16.251  45.716  -7.231  1 28.85  ? 425 LEU A CA    1 1 
ATOM   3437 C  C     . LEU A 1 425 ? 15.787  47.127  -7.206  1 28.56  ? 425 LEU A C     1 1 
ATOM   3438 O  O     . LEU A 1 425 ? 16.011  47.84   -8.168  1 29.16  ? 425 LEU A O     1 1 
ATOM   3439 C  CB    . LEU A 1 425 ? 17.78   45.742  -7.071  1 29.18  ? 425 LEU A CB    1 1 
ATOM   3440 C  CG    . LEU A 1 425 ? 18.535  44.469  -7.416  1 31.36  ? 425 LEU A CG    1 1 
ATOM   3441 C  CD1   . LEU A 1 425 ? 20.034  44.68   -7.323  1 31.8   ? 425 LEU A CD1   1 1 
ATOM   3442 C  CD2   . LEU A 1 425 ? 18.084  43.303  -6.546  1 32.34  ? 425 LEU A CD2   1 1 
ATOM   3443 N  N     . ASP A 1 426 ? 15.197  47.563  -6.107  1 27.79  ? 426 ASP A N     1 1 
ATOM   3444 C  CA    . ASP A 1 426 ? 14.863  48.971  -5.878  1 27.72  ? 426 ASP A CA    1 1 
ATOM   3445 C  C     . ASP A 1 426 ? 15.24   49.103  -4.43   1 27.39  ? 426 ASP A C     1 1 
ATOM   3446 O  O     . ASP A 1 426 ? 14.38   49.035  -3.55   1 27.95  ? 426 ASP A O     1 1 
ATOM   3447 C  CB    . ASP A 1 426 ? 13.376  49.28   -6.094  1 29.16  ? 426 ASP A CB    1 1 
ATOM   3448 C  CG    . ASP A 1 426 ? 13.037  50.756  -6.043  1 33.92  ? 426 ASP A CG    1 1 
ATOM   3449 O  OD1   . ASP A 1 426 ? 13.928  51.57   -5.698  1 34.39  ? 426 ASP A OD1   1 1 
ATOM   3450 O  OD2   . ASP A 1 426 ? 11.886  51.101  -6.339  1 37.14  ? 426 ASP A OD2   1 1 
ATOM   3451 N  N     . CYS A 1 427 ? 16.552  49.19   -4.186  1 26.33  ? 427 CYS A N     1 1 
ATOM   3452 C  CA    . CYS A 1 427 ? 17.14   49.102  -2.862  1 25.88  ? 427 CYS A CA    1 1 
ATOM   3453 C  C     . CYS A 1 427 ? 17.869  50.313  -2.378  1 25.43  ? 427 CYS A C     1 1 
ATOM   3454 O  O     . CYS A 1 427 ? 18.778  50.777  -3.058  1 25.57  ? 427 CYS A O     1 1 
ATOM   3455 C  CB    . CYS A 1 427 ? 18.081  47.898  -2.808  1 26.1   ? 427 CYS A CB    1 1 
ATOM   3456 S  SG    . CYS A 1 427 ? 17.326  46.32   -3.263  1 28.65  ? 427 CYS A SG    1 1 
ATOM   3457 N  N     . PRO A 1 428 ? 17.698  50.648  -1.09   1 24.76  ? 428 PRO A N     1 1 
ATOM   3458 C  CA    . PRO A 1 428 ? 18.589  51.632  -0.478  1 24.81  ? 428 PRO A CA    1 1 
ATOM   3459 C  C     . PRO A 1 428 ? 20.007  51.039  -0.381  1 25.38  ? 428 PRO A C     1 1 
ATOM   3460 O  O     . PRO A 1 428 ? 20.153  49.829  -0.226  1 25.86  ? 428 PRO A O     1 1 
ATOM   3461 C  CB    . PRO A 1 428 ? 18.01   51.789  0.934   1 25.25  ? 428 PRO A CB    1 1 
ATOM   3462 C  CG    . PRO A 1 428 ? 16.67   51.182  0.898   1 25.48  ? 428 PRO A CG    1 1 
ATOM   3463 C  CD    . PRO A 1 428 ? 16.754  50.1    -0.103  1 24.08  ? 428 PRO A CD    1 1 
ATOM   3464 N  N     . ILE A 1 429 ? 21.048  51.862  -0.487  1 25.31  ? 429 ILE A N     1 1 
ATOM   3465 C  CA    . ILE A 1 429 ? 22.426  51.383  -0.34   1 25.66  ? 429 ILE A CA    1 1 
ATOM   3466 C  C     . ILE A 1 429 ? 22.962  51.993  0.937   1 26.7   ? 429 ILE A C     1 1 
ATOM   3467 O  O     . ILE A 1 429 ? 22.907  53.221  1.084   1 27.22  ? 429 ILE A O     1 1 
ATOM   3468 C  CB    . ILE A 1 429 ? 23.277  51.782  -1.545  1 25.41  ? 429 ILE A CB    1 1 
ATOM   3469 C  CG1   . ILE A 1 429 ? 22.65   51.291  -2.839  1 26.03  ? 429 ILE A CG1   1 1 
ATOM   3470 C  CG2   . ILE A 1 429 ? 24.698  51.307  -1.376  1 25.62  ? 429 ILE A CG2   1 1 
ATOM   3471 C  CD1   . ILE A 1 429 ? 22.517  49.837  -2.949  1 27.38  ? 429 ILE A CD1   1 1 
ATOM   3472 N  N     . ILE A 1 430 ? 23.433  51.165  1.891   1 26.78  ? 430 ILE A N     1 1 
ATOM   3473 C  CA    . ILE A 1 430 ? 23.912  51.693  3.171   1 27.7   ? 430 ILE A CA    1 1 
ATOM   3474 C  C     . ILE A 1 430 ? 25.071  52.68   2.956   1 28.98  ? 430 ILE A C     1 1 
ATOM   3475 O  O     . ILE A 1 430 ? 26.04   52.366  2.259   1 29.17  ? 430 ILE A O     1 1 
ATOM   3476 C  CB    . ILE A 1 430 ? 24.254  50.597  4.211   1 28.2   ? 430 ILE A CB    1 1 
ATOM   3477 C  CG1   . ILE A 1 430 ? 23.278  49.407  4.171   1 28.94  ? 430 ILE A CG1   1 1 
ATOM   3478 C  CG2   . ILE A 1 430 ? 24.361  51.203  5.619   1 28.81  ? 430 ILE A CG2   1 1 
ATOM   3479 C  CD1   . ILE A 1 430 ? 21.947  49.736  4.627   1 30.51  ? 430 ILE A CD1   1 1 
ATOM   3480 N  N     . GLY A 1 431 ? 24.907  53.891  3.469   1 29.49  ? 431 GLY A N     1 1 
ATOM   3481 C  CA    . GLY A 1 431 ? 25.898  54.94   3.263   1 30.37  ? 431 GLY A CA    1 1 
ATOM   3482 C  C     . GLY A 1 431 ? 25.575  55.872  2.104   1 31.14  ? 431 GLY A C     1 1 
ATOM   3483 O  O     . GLY A 1 431 ? 26.287  56.854  1.886   1 31.41  ? 431 GLY A O     1 1 
ATOM   3484 N  N     . GLU A 1 432 ? 24.497  55.578  1.345   1 31.26  ? 432 GLU A N     1 1 
ATOM   3485 C  CA    . GLU A 1 432 ? 24.049  56.397  0.226   1 31.6   ? 432 GLU A CA    1 1 
ATOM   3486 C  C     . GLU A 1 432 ? 22.678  57.018  0.502   1 31.7   ? 432 GLU A C     1 1 
ATOM   3487 O  O     . GLU A 1 432 ? 21.91   56.505  1.312   1 31.73  ? 432 GLU A O     1 1 
ATOM   3488 C  CB    . GLU A 1 432 ? 24.112  55.629  -1.101  1 33.77  ? 432 GLU A CB    1 1 
ATOM   3489 C  CG    . GLU A 1 432 ? 25.55   55.285  -1.462  1 39.52  ? 432 GLU A CG    1 1 
ATOM   3490 C  CD    . GLU A 1 432 ? 25.89   55.252  -2.939  1 46.34  ? 432 GLU A CD    1 1 
ATOM   3491 O  OE1   . GLU A 1 432 ? 25.187  54.537  -3.687  1 48.03  ? 432 GLU A OE1   1 1 
ATOM   3492 O  OE2   . GLU A 1 432 ? 26.853  55.937  -3.352  1 48.25  ? 432 GLU A OE2   1 1 
ATOM   3493 N  N     . SER A 1 433 ? 22.399  58.16   -0.126  1 31.61  ? 433 SER A N     1 1 
ATOM   3494 C  CA    . SER A 1 433 ? 21.168  58.915  0.101   1 32.07  ? 433 SER A CA    1 1 
ATOM   3495 C  C     . SER A 1 433 ? 19.928  58.364  -0.593  1 32     ? 433 SER A C     1 1 
ATOM   3496 O  O     . SER A 1 433 ? 18.821  58.608  -0.117  1 32.13  ? 433 SER A O     1 1 
ATOM   3497 C  CB    . SER A 1 433 ? 21.339  60.38   -0.311  1 33.6   ? 433 SER A CB    1 1 
ATOM   3498 O  OG    . SER A 1 433 ? 22.634  60.912  -0.082  1 35.83  ? 433 SER A OG    1 1 
ATOM   3499 N  N     . TYR A 1 434 ? 20.088  57.703  -1.742  1 31.68  ? 434 TYR A N     1 1 
ATOM   3500 C  CA    . TYR A 1 434 ? 18.944  57.226  -2.512  1 32.03  ? 434 TYR A CA    1 1 
ATOM   3501 C  C     . TYR A 1 434 ? 19.042  55.748  -2.923  1 32.27  ? 434 TYR A C     1 1 
ATOM   3502 O  O     . TYR A 1 434 ? 20.067  55.109  -2.703  1 32.02  ? 434 TYR A O     1 1 
ATOM   3503 C  CB    . TYR A 1 434 ? 18.731  58.152  -3.726  1 31.96  ? 434 TYR A CB    1 1 
ATOM   3504 C  CG    . TYR A 1 434 ? 18.232  59.508  -3.294  1 32.68  ? 434 TYR A CG    1 1 
ATOM   3505 C  CD1   . TYR A 1 434 ? 16.93   59.677  -2.851  1 33.83  ? 434 TYR A CD1   1 1 
ATOM   3506 C  CD2   . TYR A 1 434 ? 19.097  60.586  -3.188  1 33.41  ? 434 TYR A CD2   1 1 
ATOM   3507 C  CE1   . TYR A 1 434 ? 16.48   60.902  -2.383  1 34.82  ? 434 TYR A CE1   1 1 
ATOM   3508 C  CE2   . TYR A 1 434 ? 18.664  61.815  -2.711  1 34.4   ? 434 TYR A CE2   1 1 
ATOM   3509 C  CZ    . TYR A 1 434 ? 17.351  61.971  -2.315  1 35.79  ? 434 TYR A CZ    1 1 
ATOM   3510 O  OH    . TYR A 1 434 ? 16.888  63.18   -1.857  1 37.7   ? 434 TYR A OH    1 1 
ATOM   3511 N  N     . ASN A 1 435 ? 17.967  55.203  -3.499  1 32.59  ? 435 ASN A N     1 1 
ATOM   3512 C  CA    . ASN A 1 435 ? 17.959  53.817  -3.943  1 33.56  ? 435 ASN A CA    1 1 
ATOM   3513 C  C     . ASN A 1 435 ? 18.728  53.568  -5.249  1 33.16  ? 435 ASN A C     1 1 
ATOM   3514 O  O     . ASN A 1 435 ? 18.952  54.481  -6.042  1 33.62  ? 435 ASN A O     1 1 
ATOM   3515 C  CB    . ASN A 1 435 ? 16.526  53.319  -4.103  1 36.05  ? 435 ASN A CB    1 1 
ATOM   3516 C  CG    . ASN A 1 435 ? 15.863  53.005  -2.798  1 41.29  ? 435 ASN A CG    1 1 
ATOM   3517 O  OD1   . ASN A 1 435 ? 16.239  53.535  -1.743  1 43.21  ? 435 ASN A OD1   1 1 
ATOM   3518 N  ND2   . ASN A 1 435 ? 14.853  52.146  -2.845  1 42.35  ? 435 ASN A ND2   1 1 
ATOM   3519 N  N     . GLU A 1 436 ? 19.117  52.312  -5.466  1 32.13  ? 436 GLU A N     1 1 
ATOM   3520 C  CA    . GLU A 1 436 ? 19.746  51.858  -6.694  1 31.56  ? 436 GLU A CA    1 1 
ATOM   3521 C  C     . GLU A 1 436 ? 18.72   50.986  -7.374  1 30.56  ? 436 GLU A C     1 1 
ATOM   3522 O  O     . GLU A 1 436 ? 18.152  50.109  -6.721  1 30.63  ? 436 GLU A O     1 1 
ATOM   3523 C  CB    . GLU A 1 436 ? 20.969  50.967  -6.411  1 33.46  ? 436 GLU A CB    1 1 
ATOM   3524 C  CG    . GLU A 1 436 ? 22.269  51.695  -6.15   1 36.71  ? 436 GLU A CG    1 1 
ATOM   3525 C  CD    . GLU A 1 436 ? 22.729  52.653  -7.222  1 41.8   ? 436 GLU A CD    1 1 
ATOM   3526 O  OE1   . GLU A 1 436 ? 22.451  52.405  -8.415  1 42.11  ? 436 GLU A OE1   1 1 
ATOM   3527 O  OE2   . GLU A 1 436 ? 23.378  53.66   -6.863  1 44.17  ? 436 GLU A OE2   1 1 
ATOM   3528 N  N     . PHE A 1 437 ? 18.487  51.199  -8.671  1 29.48  ? 437 PHE A N     1 1 
ATOM   3529 C  CA    . PHE A 1 437 ? 17.571  50.343  -9.407  1 28.84  ? 437 PHE A CA    1 1 
ATOM   3530 C  C     . PHE A 1 437 ? 18.369  49.476  -10.35  1 28.72  ? 437 PHE A C     1 1 
ATOM   3531 O  O     . PHE A 1 437 ? 19.255  49.972  -11.05  1 28.53  ? 437 PHE A O     1 1 
ATOM   3532 C  CB    . PHE A 1 437 ? 16.491  51.129  -10.17  1 28.27  ? 437 PHE A CB    1 1 
ATOM   3533 C  CG    . PHE A 1 437 ? 15.768  50.318  -11.223 1 28.59  ? 437 PHE A CG    1 1 
ATOM   3534 C  CD1   . PHE A 1 437 ? 14.794  49.399  -10.869 1 29.41  ? 437 PHE A CD1   1 1 
ATOM   3535 C  CD2   . PHE A 1 437 ? 16.099  50.437  -12.56  1 29.28  ? 437 PHE A CD2   1 1 
ATOM   3536 C  CE1   . PHE A 1 437 ? 14.157  48.627  -11.831 1 29.91  ? 437 PHE A CE1   1 1 
ATOM   3537 C  CE2   . PHE A 1 437 ? 15.448  49.674  -13.521 1 30.12  ? 437 PHE A CE2   1 1 
ATOM   3538 C  CZ    . PHE A 1 437 ? 14.481  48.773  -13.149 1 29.79  ? 437 PHE A CZ    1 1 
ATOM   3539 N  N     . ARG A 1 438 ? 18.035  48.181  -10.388 1 28.43  ? 438 ARG A N     1 1 
ATOM   3540 C  CA    . ARG A 1 438 ? 18.654  47.251  -11.319 1 28.5   ? 438 ARG A CA    1 1 
ATOM   3541 C  C     . ARG A 1 438 ? 17.579  46.364  -11.904 1 28.31  ? 438 ARG A C     1 1 
ATOM   3542 O  O     . ARG A 1 438 ? 16.68   45.936  -11.196 1 28.04  ? 438 ARG A O     1 1 
ATOM   3543 C  CB    . ARG A 1 438 ? 19.708  46.353  -10.64  1 29.7   ? 438 ARG A CB    1 1 
ATOM   3544 C  CG    . ARG A 1 438 ? 20.901  47.059  -10.024 1 32.38  ? 438 ARG A CG    1 1 
ATOM   3545 C  CD    . ARG A 1 438 ? 21.795  47.733  -11.036 1 35.16  ? 438 ARG A CD    1 1 
ATOM   3546 N  NE    . ARG A 1 438 ? 22.963  48.323  -10.377 1 37.49  ? 438 ARG A NE    1 1 
ATOM   3547 C  CZ    . ARG A 1 438 ? 23.048  49.588  -9.978  1 38.6   ? 438 ARG A CZ    1 1 
ATOM   3548 N  NH1   . ARG A 1 438 ? 22.04   50.423  -10.178 1 38.02  ? 438 ARG A NH1   1 1 
ATOM   3549 N  NH2   . ARG A 1 438 ? 24.139  50.025  -9.372  1 38.59  ? 438 ARG A NH2   1 1 
ATOM   3550 N  N     . LEU A 1 439 ? 17.665  46.097  -13.195 1 28.5   ? 439 LEU A N     1 1 
ATOM   3551 C  CA    . LEU A 1 439 ? 16.815  45.126  -13.851 1 29.34  ? 439 LEU A CA    1 1 
ATOM   3552 C  C     . LEU A 1 439 ? 17.821  44.149  -14.447 1 30.34  ? 439 LEU A C     1 1 
ATOM   3553 O  O     . LEU A 1 439 ? 18.581  44.515  -15.349 1 31.1   ? 439 LEU A O     1 1 
ATOM   3554 C  CB    . LEU A 1 439 ? 15.916  45.722  -14.936 1 29.6   ? 439 LEU A CB    1 1 
ATOM   3555 C  CG    . LEU A 1 439 ? 15.248  44.69   -15.871 1 31.62  ? 439 LEU A CG    1 1 
ATOM   3556 C  CD1   . LEU A 1 439 ? 14.477  43.614  -15.11  1 32     ? 439 LEU A CD1   1 1 
ATOM   3557 C  CD2   . LEU A 1 439 ? 14.33   45.355  -16.814 1 32.54  ? 439 LEU A CD2   1 1 
ATOM   3558 N  N     . ILE A 1 440 ? 17.895  42.941  -13.885 1 29.91  ? 440 ILE A N     1 1 
ATOM   3559 C  CA    . ILE A 1 440 ? 18.857  41.949  -14.326 1 29.73  ? 440 ILE A CA    1 1 
ATOM   3560 C  C     . ILE A 1 440 ? 18.151  40.887  -15.115 1 29.62  ? 440 ILE A C     1 1 
ATOM   3561 O  O     . ILE A 1 440 ? 17.299  40.198  -14.568 1 29.38  ? 440 ILE A O     1 1 
ATOM   3562 C  CB    . ILE A 1 440 ? 19.582  41.316  -13.118 1 30.08  ? 440 ILE A CB    1 1 
ATOM   3563 C  CG1   . ILE A 1 440 ? 20.222  42.377  -12.189 1 30.97  ? 440 ILE A CG1   1 1 
ATOM   3564 C  CG2   . ILE A 1 440 ? 20.586  40.262  -13.579 1 30.45  ? 440 ILE A CG2   1 1 
ATOM   3565 C  CD1   . ILE A 1 440 ? 21.384  43.127  -12.768 1 32.17  ? 440 ILE A CD1   1 1 
ATOM   3566 N  N     . ILE A 1 441 ? 18.496  40.744  -16.394 1 29.75  ? 441 ILE A N     1 1 
ATOM   3567 C  CA    . ILE A 1 441 ? 17.918  39.69   -17.215 1 30.42  ? 441 ILE A CA    1 1 
ATOM   3568 C  C     . ILE A 1 441 ? 18.797  38.475  -16.94  1 30.91  ? 441 ILE A C     1 1 
ATOM   3569 O  O     . ILE A 1 441 ? 19.869  38.345  -17.514 1 31.36  ? 441 ILE A O     1 1 
ATOM   3570 C  CB    . ILE A 1 441 ? 17.909  40.092  -18.704 1 31     ? 441 ILE A CB    1 1 
ATOM   3571 C  CG1   . ILE A 1 441 ? 17.249  41.471  -18.913 1 31.77  ? 441 ILE A CG1   1 1 
ATOM   3572 C  CG2   . ILE A 1 441 ? 17.24   39.017  -19.547 1 31.65  ? 441 ILE A CG2   1 1 
ATOM   3573 C  CD1   . ILE A 1 441 ? 15.82   41.565  -18.505 1 32.71  ? 441 ILE A CD1   1 1 
ATOM   3574 N  N     . ASN A 1 442 ? 18.391  37.644  -15.994 1 30.77  ? 442 ASN A N     1 1 
ATOM   3575 C  CA    . ASN A 1 442 ? 19.165  36.5    -15.525 1 31.25  ? 442 ASN A CA    1 1 
ATOM   3576 C  C     . ASN A 1 442 ? 18.807  35.171  -16.193 1 31.76  ? 442 ASN A C     1 1 
ATOM   3577 O  O     . ASN A 1 442 ? 19.279  34.135  -15.739 1 31.94  ? 442 ASN A O     1 1 
ATOM   3578 C  CB    . ASN A 1 442 ? 18.964  36.396  -14.011 1 32.21  ? 442 ASN A CB    1 1 
ATOM   3579 C  CG    . ASN A 1 442 ? 19.928  35.522  -13.273 1 35.09  ? 442 ASN A CG    1 1 
ATOM   3580 O  OD1   . ASN A 1 442 ? 21.15   35.701  -13.333 1 36.71  ? 442 ASN A OD1   1 1 
ATOM   3581 N  ND2   . ASN A 1 442 ? 19.387  34.566  -12.552 1 34.88  ? 442 ASN A ND2   1 1 
ATOM   3582 N  N     . LYS A 1 443 ? 17.987  35.191  -17.257 1 31.96  ? 443 LYS A N     1 1 
ATOM   3583 C  CA    . LYS A 1 443 ? 17.524  33.982  -17.946 1 32.71  ? 443 LYS A CA    1 1 
ATOM   3584 C  C     . LYS A 1 443 ? 18.625  32.974  -18.324 1 33.12  ? 443 LYS A C     1 1 
ATOM   3585 O  O     . LYS A 1 443 ? 18.518  31.801  -17.96  1 33.57  ? 443 LYS A O     1 1 
ATOM   3586 C  CB    . LYS A 1 443 ? 16.683  34.329  -19.178 1 34.73  ? 443 LYS A CB    1 1 
ATOM   3587 C  CG    . LYS A 1 443 ? 15.213  34.462  -18.868 1 39.08  ? 443 LYS A CG    1 1 
ATOM   3588 C  CD    . LYS A 1 443 ? 14.37   34.359  -20.124 1 44.66  ? 443 LYS A CD    1 1 
ATOM   3589 C  CE    . LYS A 1 443 ? 12.893  34.546  -19.818 1 49.59  ? 443 LYS A CE    1 1 
ATOM   3590 N  NZ    . LYS A 1 443 ? 12.278  35.681  -20.579 1 51.48  ? 443 LYS A NZ    1 1 
ATOM   3591 N  N     . ASN A 1 444 ? 19.664  33.409  -19.038 1 32.69  ? 444 ASN A N     1 1 
ATOM   3592 C  CA    . ASN A 1 444 ? 20.734  32.504  -19.444 1 32.87  ? 444 ASN A CA    1 1 
ATOM   3593 C  C     . ASN A 1 444 ? 21.485  31.927  -18.262 1 32.75  ? 444 ASN A C     1 1 
ATOM   3594 O  O     . ASN A 1 444 ? 21.924  30.777  -18.303 1 32.84  ? 444 ASN A O     1 1 
ATOM   3595 C  CB    . ASN A 1 444 ? 21.712  33.241  -20.332 1 34.35  ? 444 ASN A CB    1 1 
ATOM   3596 C  CG    . ASN A 1 444 ? 21.501  33.012  -21.794 1 37.74  ? 444 ASN A CG    1 1 
ATOM   3597 O  OD1   . ASN A 1 444 ? 20.509  32.408  -22.229 1 38.72  ? 444 ASN A OD1   1 1 
ATOM   3598 N  ND2   . ASN A 1 444 ? 22.45   33.493  -22.58  1 38.61  ? 444 ASN A ND2   1 1 
ATOM   3599 N  N     . ASN A 1 445 ? 21.669  32.745  -17.225 1 32.35  ? 445 ASN A N     1 1 
ATOM   3600 C  CA    . ASN A 1 445 ? 22.403  32.363  -16.035 1 32.3   ? 445 ASN A CA    1 1 
ATOM   3601 C  C     . ASN A 1 445 ? 21.633  31.351  -15.231 1 31.51  ? 445 ASN A C     1 1 
ATOM   3602 O  O     . ASN A 1 445 ? 22.215  30.369  -14.782 1 31.84  ? 445 ASN A O     1 1 
ATOM   3603 C  CB    . ASN A 1 445 ? 22.707  33.588  -15.203 1 33.94  ? 445 ASN A CB    1 1 
ATOM   3604 C  CG    . ASN A 1 445 ? 23.846  33.381  -14.251 1 37.24  ? 445 ASN A CG    1 1 
ATOM   3605 O  OD1   . ASN A 1 445 ? 24.846  32.73   -14.562 1 37.84  ? 445 ASN A OD1   1 1 
ATOM   3606 N  ND2   . ASN A 1 445 ? 23.722  33.953  -13.076 1 38.31  ? 445 ASN A ND2   1 1 
ATOM   3607 N  N     . LYS A 1 446 ? 20.317  31.545  -15.096 1 30.43  ? 446 LYS A N     1 1 
ATOM   3608 C  CA    . LYS A 1 446 ? 19.458  30.607  -14.384 1 29.73  ? 446 LYS A CA    1 1 
ATOM   3609 C  C     . LYS A 1 446 ? 19.471  29.244  -15.094 1 29.59  ? 446 LYS A C     1 1 
ATOM   3610 O  O     . LYS A 1 446 ? 19.627  28.215  -14.438 1 29.36  ? 446 LYS A O     1 1 
ATOM   3611 C  CB    . LYS A 1 446 ? 18.025  31.162  -14.271 1 30.08  ? 446 LYS A CB    1 1 
ATOM   3612 C  CG    . LYS A 1 446 ? 17.014  30.137  -13.781 1 32.37  ? 446 LYS A CG    1 1 
ATOM   3613 C  CD    . LYS A 1 446 ? 15.633  30.706  -13.629 1 35.23  ? 446 LYS A CD    1 1 
ATOM   3614 C  CE    . LYS A 1 446 ? 14.652  29.612  -13.306 1 36.85  ? 446 LYS A CE    1 1 
ATOM   3615 N  NZ    . LYS A 1 446 ? 13.296  30.141  -12.998 1 36.93  ? 446 LYS A NZ    1 1 
ATOM   3616 N  N     . GLU A 1 447 ? 19.356  29.25   -16.432 1 29.47  ? 447 GLU A N     1 1 
ATOM   3617 C  CA    . GLU A 1 447 ? 19.357  28.036  -17.239 1 29.87  ? 447 GLU A CA    1 1 
ATOM   3618 C  C     . GLU A 1 447 ? 20.648  27.238  -17.03  1 30.61  ? 447 GLU A C     1 1 
ATOM   3619 O  O     . GLU A 1 447 ? 20.602  26.005  -16.899 1 31.13  ? 447 GLU A O     1 1 
ATOM   3620 C  CB    . GLU A 1 447 ? 19.164  28.379  -18.724 1 31.46  ? 447 GLU A CB    1 1 
ATOM   3621 N  N     . SER A 1 448 ? 21.79   27.948  -16.97  1 30.2   ? 448 SER A N     1 1 
ATOM   3622 C  CA    . SER A 1 448 ? 23.092  27.328  -16.748 1 30.39  ? 448 SER A CA    1 1 
ATOM   3623 C  C     . SER A 1 448 ? 23.208  26.779  -15.338 1 30.12  ? 448 SER A C     1 1 
ATOM   3624 O  O     . SER A 1 448 ? 23.744  25.684  -15.156 1 30.2   ? 448 SER A O     1 1 
ATOM   3625 C  CB    . SER A 1 448 ? 24.215  28.327  -17.004 1 31.85  ? 448 SER A CB    1 1 
ATOM   3626 O  OG    . SER A 1 448 ? 24.319  28.583  -18.392 1 34.45  ? 448 SER A OG    1 1 
ATOM   3627 N  N     . ILE A 1 449 ? 22.708  27.523  -14.34  1 29.54  ? 449 ILE A N     1 1 
ATOM   3628 C  CA    . ILE A 1 449 ? 22.776  27.077  -12.957 1 29.63  ? 449 ILE A CA    1 1 
ATOM   3629 C  C     . ILE A 1 449 ? 21.953  25.811  -12.735 1 30.73  ? 449 ILE A C     1 1 
ATOM   3630 O  O     . ILE A 1 449 ? 22.409  24.914  -12.03  1 30.67  ? 449 ILE A O     1 1 
ATOM   3631 C  CB    . ILE A 1 449 ? 22.424  28.213  -11.979 1 29.52  ? 449 ILE A CB    1 1 
ATOM   3632 C  CG1   . ILE A 1 449 ? 23.48   29.313  -12.034 1 29.74  ? 449 ILE A CG1   1 1 
ATOM   3633 C  CG2   . ILE A 1 449 ? 22.303  27.692  -10.563 1 30.13  ? 449 ILE A CG2   1 1 
ATOM   3634 C  CD1   . ILE A 1 449 ? 23.053  30.583  -11.401 1 30.56  ? 449 ILE A CD1   1 1 
ATOM   3635 N  N     . LEU A 1 450 ? 20.787  25.691  -13.395 1 31.75  ? 450 LEU A N     1 1 
ATOM   3636 C  CA    . LEU A 1 450 ? 19.958  24.498  -13.271 1 33.03  ? 450 LEU A CA    1 1 
ATOM   3637 C  C     . LEU A 1 450 ? 20.593  23.234  -13.909 1 34.74  ? 450 LEU A C     1 1 
ATOM   3638 O  O     . LEU A 1 450 ? 20.118  22.126  -13.664 1 35.06  ? 450 LEU A O     1 1 
ATOM   3639 C  CB    . LEU A 1 450 ? 18.544  24.75   -13.796 1 33.33  ? 450 LEU A CB    1 1 
ATOM   3640 C  CG    . LEU A 1 450 ? 17.751  25.87   -13.093 1 34.73  ? 450 LEU A CG    1 1 
ATOM   3641 C  CD1   . LEU A 1 450 ? 16.368  26.002  -13.677 1 34.93  ? 450 LEU A CD1   1 1 
ATOM   3642 C  CD2   . LEU A 1 450 ? 17.603  25.614  -11.617 1 35.38  ? 450 LEU A CD2   1 1 
ATOM   3643 N  N     . ARG A 1 451 ? 21.68   23.391  -14.684 1 35.49  ? 451 ARG A N     1 1 
ATOM   3644 C  CA    . ARG A 1 451 ? 22.432  22.269  -15.25  1 36.56  ? 451 ARG A CA    1 1 
ATOM   3645 C  C     . ARG A 1 451 ? 23.74   22.02   -14.484 1 37.24  ? 451 ARG A C     1 1 
ATOM   3646 O  O     . ARG A 1 451 ? 24.406  21.024  -14.748 1 37.64  ? 451 ARG A O     1 1 
ATOM   3647 C  CB    . ARG A 1 451 ? 22.826  22.532  -16.707 1 38.62  ? 451 ARG A CB    1 1 
ATOM   3648 C  CG    . ARG A 1 451 ? 21.688  22.749  -17.685 1 43.33  ? 451 ARG A CG    1 1 
ATOM   3649 C  CD    . ARG A 1 451 ? 22.196  22.783  -19.127 1 48.12  ? 451 ARG A CD    1 1 
ATOM   3650 N  NE    . ARG A 1 451 ? 23.338  23.685  -19.321 1 52.58  ? 451 ARG A NE    1 1 
ATOM   3651 C  CZ    . ARG A 1 451 ? 23.238  24.98   -19.619 1 55.81  ? 451 ARG A CZ    1 1 
ATOM   3652 N  NH1   . ARG A 1 451 ? 22.045  25.539  -19.793 1 55.19  ? 451 ARG A NH1   1 1 
ATOM   3653 N  NH2   . ARG A 1 451 ? 24.331  25.72   -19.768 1 56.42  ? 451 ARG A NH2   1 1 
ATOM   3654 N  N     . LYS A 1 452 ? 24.165  22.948  -13.618 1 37.32  ? 452 LYS A N     1 1 
ATOM   3655 C  CA    . LYS A 1 452 ? 25.423  22.842  -12.884 1 37.6   ? 452 LYS A CA    1 1 
ATOM   3656 C  C     . LYS A 1 452 ? 25.429  21.694  -11.868 1 37.77  ? 452 LYS A C     1 1 
ATOM   3657 O  O     . LYS A 1 452 ? 24.522  21.574  -11.037 1 37.98  ? 452 LYS A O     1 1 
ATOM   3658 C  CB    . LYS A 1 452 ? 25.762  24.185  -12.199 1 38.7   ? 452 LYS A CB    1 1 
ATOM   3659 C  CG    . LYS A 1 452 ? 27.112  24.781  -12.594 1 41.05  ? 452 LYS A CG    1 1 
ATOM   3660 C  CD    . LYS A 1 452 ? 26.97   26.279  -12.907 1 43.7   ? 452 LYS A CD    1 1 
ATOM   3661 C  CE    . LYS A 1 452 ? 28.09   27.17   -12.388 1 45.55  ? 452 LYS A CE    1 1 
ATOM   3662 N  NZ    . LYS A 1 452 ? 27.752  28.625  -12.488 1 45.58  ? 452 LYS A NZ    1 1 
ATOM   3663 N  N     . THR A 1 453 ? 26.439  20.828  -11.98  1 37.57  ? 453 THR A N     1 1 
ATOM   3664 C  CA    . THR A 1 453 ? 26.681  19.702  -11.078 1 37.98  ? 453 THR A CA    1 1 
ATOM   3665 C  C     . THR A 1 453 ? 28.166  19.692  -10.727 1 38.33  ? 453 THR A C     1 1 
ATOM   3666 O  O     . THR A 1 453 ? 29.002  20.057  -11.56  1 38.28  ? 453 THR A O     1 1 
ATOM   3667 C  CB    . THR A 1 453 ? 26.31   18.353  -11.72  1 39.14  ? 453 THR A CB    1 1 
ATOM   3668 O  OG1   . THR A 1 453 ? 27.076  18.166  -12.911 1 40.24  ? 453 THR A OG1   1 1 
ATOM   3669 C  CG2   . THR A 1 453 ? 24.818  18.209  -12.006 1 39.31  ? 453 THR A CG2   1 1 
ATOM   3670 N  N     . SER A 1 454 ? 28.5    19.265  -9.509  1 38.48  ? 454 SER A N     1 1 
ATOM   3671 C  CA    . SER A 1 454 ? 29.897  19.176  -9.096  1 39.07  ? 454 SER A CA    1 1 
ATOM   3672 C  C     . SER A 1 454 ? 30.569  17.929  -9.709  1 39.08  ? 454 SER A C     1 1 
ATOM   3673 O  O     . SER A 1 454 ? 29.879  17.027  -10.194 1 39.19  ? 454 SER A O     1 1 
ATOM   3674 C  CB    . SER A 1 454 ? 30.013  19.177  -7.574  1 40.88  ? 454 SER A CB    1 1 
ATOM   3675 O  OG    . SER A 1 454 ? 29.677  17.915  -7.022  1 43.85  ? 454 SER A OG    1 1 
ATOM   3676 N  N     . LYS A 1 455 ? 31.914  17.895  -9.699  1 38.81  ? 455 LYS A N     1 1 
ATOM   3677 C  CA    . LYS A 1 455 ? 32.751  16.826  -10.249 1 38.94  ? 455 LYS A CA    1 1 
ATOM   3678 C  C     . LYS A 1 455 ? 32.269  15.448  -9.833  1 38.63  ? 455 LYS A C     1 1 
ATOM   3679 O  O     . LYS A 1 455 ? 32.114  15.196  -8.641  1 38.73  ? 455 LYS A O     1 1 
ATOM   3680 C  CB    . LYS A 1 455 ? 34.221  17.042  -9.818  1 41.04  ? 455 LYS A CB    1 1 
ATOM   3681 C  CG    . LYS A 1 455 ? 35.193  15.915  -10.166 1 45.11  ? 455 LYS A CG    1 1 
ATOM   3682 C  CD    . LYS A 1 455 ? 36.524  16.07   -9.423  1 49.37  ? 455 LYS A CD    1 1 
ATOM   3683 C  CE    . LYS A 1 455 ? 37.454  14.898  -9.662  1 53.18  ? 455 LYS A CE    1 1 
ATOM   3684 N  NZ    . LYS A 1 455 ? 38.693  14.986  -8.845  1 55.21  ? 455 LYS A NZ    1 1 
ATOM   3685 N  N     . GLN A 1 456 ? 31.977  14.585  -10.819 1 38.11  ? 456 GLN A N     1 1 
ATOM   3686 C  CA    . GLN A 1 456 ? 31.529  13.217  -10.573 1 38     ? 456 GLN A CA    1 1 
ATOM   3687 C  C     . GLN A 1 456 ? 32.683  12.41   -10.025 1 37.76  ? 456 GLN A C     1 1 
ATOM   3688 O  O     . GLN A 1 456 ? 33.74   12.344  -10.647 1 38.08  ? 456 GLN A O     1 1 
ATOM   3689 C  CB    . GLN A 1 456 ? 31.045  12.56   -11.871 1 39.38  ? 456 GLN A CB    1 1 
ATOM   3690 C  CG    . GLN A 1 456 ? 29.962  13.343  -12.573 1 42.66  ? 456 GLN A CG    1 1 
ATOM   3691 C  CD    . GLN A 1 456 ? 28.694  13.356  -11.766 1 46.62  ? 456 GLN A CD    1 1 
ATOM   3692 O  OE1   . GLN A 1 456 ? 28.268  12.328  -11.222 1 47.69  ? 456 GLN A OE1   1 1 
ATOM   3693 N  NE2   . GLN A 1 456 ? 28.067  14.528  -11.667 1 46.93  ? 456 GLN A NE2   1 1 
ATOM   3694 N  N     . GLN A 1 457 ? 32.493  11.802  -8.865  1 37.08  ? 457 GLN A N     1 1 
ATOM   3695 C  CA    . GLN A 1 457 ? 33.519  10.978  -8.245  1 36.94  ? 457 GLN A CA    1 1 
ATOM   3696 C  C     . GLN A 1 457 ? 32.897  10.068  -7.203  1 36.51  ? 457 GLN A C     1 1 
ATOM   3697 O  O     . GLN A 1 457 ? 31.922  10.441  -6.544  1 36.68  ? 457 GLN A O     1 1 
ATOM   3698 C  CB    . GLN A 1 457 ? 34.633  11.837  -7.615  1 38.11  ? 457 GLN A CB    1 1 
ATOM   3699 C  CG    . GLN A 1 457 ? 34.116  12.802  -6.568  1 40.81  ? 457 GLN A CG    1 1 
ATOM   3700 C  CD    . GLN A 1 457 ? 35.194  13.568  -5.861  1 44.83  ? 457 GLN A CD    1 1 
ATOM   3701 O  OE1   . GLN A 1 457 ? 35.066  14.775  -5.649  1 46.89  ? 457 GLN A OE1   1 1 
ATOM   3702 N  NE2   . GLN A 1 457 ? 36.268  12.892  -5.464  1 44.86  ? 457 GLN A NE2   1 1 
ATOM   3703 N  N     . ASN A 1 458 ? 33.446  8.864   -7.069  1 35.9   ? 458 ASN A N     1 1 
ATOM   3704 C  CA    . ASN A 1 458 ? 32.978  7.933   -6.052  1 36     ? 458 ASN A CA    1 1 
ATOM   3705 C  C     . ASN A 1 458 ? 33.46   8.45    -4.711  1 34.92  ? 458 ASN A C     1 1 
ATOM   3706 O  O     . ASN A 1 458 ? 34.577  8.971   -4.621  1 35.32  ? 458 ASN A O     1 1 
ATOM   3707 C  CB    . ASN A 1 458 ? 33.525  6.518   -6.297  1 38.2   ? 458 ASN A CB    1 1 
ATOM   3708 C  CG    . ASN A 1 458 ? 33.092  5.876   -7.599  1 42.74  ? 458 ASN A CG    1 1 
ATOM   3709 O  OD1   . ASN A 1 458 ? 33.776  4.992   -8.136  1 43.8   ? 458 ASN A OD1   1 1 
ATOM   3710 N  ND2   . ASN A 1 458 ? 31.938  6.287   -8.134  1 44.38  ? 458 ASN A ND2   1 1 
ATOM   3711 N  N     . ILE A 1 459 ? 32.621  8.358   -3.682  1 33.53  ? 459 ILE A N     1 1 
ATOM   3712 C  CA    . ILE A 1 459 ? 33.014  8.844   -2.367  1 32.83  ? 459 ILE A CA    1 1 
ATOM   3713 C  C     . ILE A 1 459 ? 32.945  7.74    -1.353  1 32.33  ? 459 ILE A C     1 1 
ATOM   3714 O  O     . ILE A 1 459 ? 31.999  6.962   -1.341  1 32.27  ? 459 ILE A O     1 1 
ATOM   3715 C  CB    . ILE A 1 459 ? 32.232  10.121  -1.941  1 32.93  ? 459 ILE A CB    1 1 
ATOM   3716 C  CG1   . ILE A 1 459 ? 32.635  11.317  -2.807  1 33.6   ? 459 ILE A CG1   1 1 
ATOM   3717 C  CG2   . ILE A 1 459 ? 32.416  10.452  -0.453  1 33.19  ? 459 ILE A CG2   1 1 
ATOM   3718 C  CD1   . ILE A 1 459 ? 31.73   12.432  -2.711  1 34.67  ? 459 ILE A CD1   1 1 
ATOM   3719 N  N     . LEU A 1 460 ? 33.98   7.638   -0.544  1 31.91  ? 460 LEU A N     1 1 
ATOM   3720 C  CA    . LEU A 1 460 ? 34.045  6.704   0.551   1 32.32  ? 460 LEU A CA    1 1 
ATOM   3721 C  C     . LEU A 1 460 ? 34.682  7.522   1.633   1 32.5   ? 460 LEU A C     1 1 
ATOM   3722 O  O     . LEU A 1 460 ? 35.891  7.763   1.584   1 32.52  ? 460 LEU A O     1 1 
ATOM   3723 C  CB    . LEU A 1 460 ? 34.927  5.499   0.209   1 32.73  ? 460 LEU A CB    1 1 
ATOM   3724 C  CG    . LEU A 1 460 ? 34.948  4.404   1.269   1 34.15  ? 460 LEU A CG    1 1 
ATOM   3725 C  CD1   . LEU A 1 460 ? 33.577  3.776   1.436   1 34.45  ? 460 LEU A CD1   1 1 
ATOM   3726 C  CD2   . LEU A 1 460 ? 35.932  3.35    0.915   1 34.9   ? 460 LEU A CD2   1 1 
ATOM   3727 N  N     . VAL A 1 461 ? 33.866  8.043   2.549   1 32.56  ? 461 VAL A N     1 1 
ATOM   3728 C  CA    . VAL A 1 461 ? 34.385  8.897   3.606   1 33.4   ? 461 VAL A CA    1 1 
ATOM   3729 C  C     . VAL A 1 461 ? 35.253  8.11    4.559   1 34.46  ? 461 VAL A C     1 1 
ATOM   3730 O  O     . VAL A 1 461 ? 34.775  7.145   5.137   1 35.24  ? 461 VAL A O     1 1 
ATOM   3731 C  CB    . VAL A 1 461 ? 33.254  9.626   4.335   1 33.79  ? 461 VAL A CB    1 1 
ATOM   3732 C  CG1   . VAL A 1 461 ? 33.808  10.507  5.442   1 34.43  ? 461 VAL A CG1   1 1 
ATOM   3733 C  CG2   . VAL A 1 461 ? 32.447  10.452  3.352   1 33.99  ? 461 VAL A CG2   1 1 
ATOM   3734 N  N     . ASP A 1 462 ? 36.532  8.482   4.696   1 34.34  ? 462 ASP A N     1 1 
ATOM   3735 C  CA    . ASP A 1 462 ? 37.451  7.774   5.585   1 34.71  ? 462 ASP A CA    1 1 
ATOM   3736 C  C     . ASP A 1 462 ? 37      7.955   7.031   1 34.86  ? 462 ASP A C     1 1 
ATOM   3737 O  O     . ASP A 1 462 ? 36.707  9.076   7.456   1 34.75  ? 462 ASP A O     1 1 
ATOM   3738 C  CB    . ASP A 1 462 ? 38.885  8.288   5.391   1 36.24  ? 462 ASP A CB    1 1 
ATOM   3739 C  CG    . ASP A 1 462 ? 39.937  7.516   6.151   1 41.11  ? 462 ASP A CG    1 1 
ATOM   3740 O  OD1   . ASP A 1 462 ? 39.895  6.269   6.12    1 41.62  ? 462 ASP A OD1   1 1 
ATOM   3741 O  OD2   . ASP A 1 462 ? 40.819  8.158   6.759   1 43.77  ? 462 ASP A OD2   1 1 
ATOM   3742 N  N     . PRO A 1 463 ? 36.905  6.846   7.791   1 34.81  ? 463 PRO A N     1 1 
ATOM   3743 C  CA    . PRO A 1 463 ? 36.422  6.933   9.177   1 35.19  ? 463 PRO A CA    1 1 
ATOM   3744 C  C     . PRO A 1 463 ? 37.298  7.744   10.141  1 36.35  ? 463 PRO A C     1 1 
ATOM   3745 O  O     . PRO A 1 463 ? 36.851  8.081   11.238  1 36.58  ? 463 PRO A O     1 1 
ATOM   3746 C  CB    . PRO A 1 463 ? 36.302  5.465   9.597   1 35.3   ? 463 PRO A CB    1 1 
ATOM   3747 C  CG    . PRO A 1 463 ? 36.251  4.698   8.326   1 35.46  ? 463 PRO A CG    1 1 
ATOM   3748 C  CD    . PRO A 1 463 ? 37.138  5.446   7.4     1 34.06  ? 463 PRO A CD    1 1 
ATOM   3749 N  N     . THR A 1 464 ? 38.53   8.073   9.737   1 36.84  ? 464 THR A N     1 1 
ATOM   3750 C  CA    . THR A 1 464 ? 39.433  8.884   10.55   1 37.62  ? 464 THR A CA    1 1 
ATOM   3751 C  C     . THR A 1 464 ? 39.495  10.319  10.003  1 38.09  ? 464 THR A C     1 1 
ATOM   3752 O  O     . THR A 1 464 ? 39.836  10.537  8.844   1 37.96  ? 464 THR A O     1 1 
ATOM   3753 C  CB    . THR A 1 464 ? 40.789  8.193   10.678  1 38.94  ? 464 THR A CB    1 1 
ATOM   3754 O  OG1   . THR A 1 464 ? 40.621  7.055   11.53   1 39.71  ? 464 THR A OG1   1 1 
ATOM   3755 C  CG2   . THR A 1 464 ? 41.871  9.122   11.228  1 39.36  ? 464 THR A CG2   1 1 
ATOM   3756 N  N     . PRO A 1 465 ? 39.091  11.305  10.813  1 38.66  ? 465 PRO A N     1 1 
ATOM   3757 C  CA    . PRO A 1 465 ? 39.074  12.696  10.334  1 39.31  ? 465 PRO A CA    1 1 
ATOM   3758 C  C     . PRO A 1 465 ? 40.442  13.391  10.388  1 40.21  ? 465 PRO A C     1 1 
ATOM   3759 O  O     . PRO A 1 465 ? 41.423  12.821  10.878  1 40.54  ? 465 PRO A O     1 1 
ATOM   3760 C  CB    . PRO A 1 465 ? 38.061  13.366  11.275  1 39.94  ? 465 PRO A CB    1 1 
ATOM   3761 C  CG    . PRO A 1 465 ? 38.264  12.656  12.553  1 40.38  ? 465 PRO A CG    1 1 
ATOM   3762 C  CD    . PRO A 1 465 ? 38.606  11.208  12.201  1 38.5   ? 465 PRO A CD    1 1 
ATOM   3763 N  N     . ASN A 1 466 ? 40.497  14.638  9.886   1 40.36  ? 466 ASN A N     1 1 
ATOM   3764 C  CA    . ASN A 1 466 ? 41.674  15.501  9.853   1 41.01  ? 466 ASN A CA    1 1 
ATOM   3765 C  C     . ASN A 1 466 ? 42.183  15.672  11.288  1 41.26  ? 466 ASN A C     1 1 
ATOM   3766 O  O     . ASN A 1 466 ? 43.349  15.393  11.569  1 41.54  ? 466 ASN A O     1 1 
ATOM   3767 C  CB    . ASN A 1 466 ? 41.291  16.852  9.198   1 42.3   ? 466 ASN A CB    1 1 
ATOM   3768 C  CG    . ASN A 1 466 ? 42.335  17.936  9.27    1 45.37  ? 466 ASN A CG    1 1 
ATOM   3769 O  OD1   . ASN A 1 466 ? 42.132  18.976  9.912   1 46.28  ? 466 ASN A OD1   1 1 
ATOM   3770 N  ND2   . ASN A 1 466 ? 43.467  17.727  8.603   1 46.12  ? 466 ASN A ND2   1 1 
ATOM   3771 N  N     . HIS A 1 467 ? 41.264  16.004  12.205  1 41.1   ? 467 HIS A N     1 1 
ATOM   3772 C  CA    . HIS A 1 467 ? 41.543  16.16   13.626  1 41.43  ? 467 HIS A CA    1 1 
ATOM   3773 C  C     . HIS A 1 467 ? 40.276  15.924  14.472  1 40.51  ? 467 HIS A C     1 1 
ATOM   3774 O  O     . HIS A 1 467 ? 39.151  15.987  13.969  1 40.38  ? 467 HIS A O     1 1 
ATOM   3775 C  CB    . HIS A 1 467 ? 42.216  17.518  13.937  1 43.17  ? 467 HIS A CB    1 1 
ATOM   3776 C  CG    . HIS A 1 467 ? 41.301  18.697  13.844  1 46.96  ? 467 HIS A CG    1 1 
ATOM   3777 N  ND1   . HIS A 1 467 ? 40.995  19.282  12.626  1 49.3   ? 467 HIS A ND1   1 1 
ATOM   3778 C  CD2   . HIS A 1 467 ? 40.661  19.374  14.827  1 48.52  ? 467 HIS A CD2   1 1 
ATOM   3779 C  CE1   . HIS A 1 467 ? 40.169  20.282  12.902  1 49.94  ? 467 HIS A CE1   1 1 
ATOM   3780 N  NE2   . HIS A 1 467 ? 39.943  20.381  14.214  1 49.8   ? 467 HIS A NE2   1 1 
ATOM   3781 N  N     . TYR A 1 468 ? 40.473  15.611  15.749  1 39.65  ? 468 TYR A N     1 1 
ATOM   3782 C  CA    . TYR A 1 468 ? 39.376  15.338  16.656  1 39.25  ? 468 TYR A CA    1 1 
ATOM   3783 C  C     . TYR A 1 468 ? 38.947  16.608  17.367  1 39.14  ? 468 TYR A C     1 1 
ATOM   3784 O  O     . TYR A 1 468 ? 39.788  17.344  17.87   1 38.98  ? 468 TYR A O     1 1 
ATOM   3785 C  CB    . TYR A 1 468 ? 39.742  14.196  17.618  1 38.98  ? 468 TYR A CB    1 1 
ATOM   3786 C  CG    . TYR A 1 468 ? 40.082  12.928  16.869  1 39.41  ? 468 TYR A CG    1 1 
ATOM   3787 C  CD1   . TYR A 1 468 ? 39.088  12.094  16.389  1 40.04  ? 468 TYR A CD1   1 1 
ATOM   3788 C  CD2   . TYR A 1 468 ? 41.398  12.603  16.574  1 40.38  ? 468 TYR A CD2   1 1 
ATOM   3789 C  CE1   . TYR A 1 468 ? 39.393  10.949  15.664  1 40.9   ? 468 TYR A CE1   1 1 
ATOM   3790 C  CE2   . TYR A 1 468 ? 41.714  11.467  15.838  1 41.28  ? 468 TYR A CE2   1 1 
ATOM   3791 C  CZ    . TYR A 1 468 ? 40.708  10.639  15.386  1 42     ? 468 TYR A CZ    1 1 
ATOM   3792 O  OH    . TYR A 1 468 ? 41.011  9.513   14.657  1 43.63  ? 468 TYR A OH    1 1 
ATOM   3793 N  N     . GLN A 1 469 ? 37.642  16.894  17.371  1 39.27  ? 469 GLN A N     1 1 
ATOM   3794 C  CA    . GLN A 1 469 ? 37.134  18.127  17.966  1 40.22  ? 469 GLN A CA    1 1 
ATOM   3795 C  C     . GLN A 1 469 ? 35.812  17.926  18.768  1 40.09  ? 469 GLN A C     1 1 
ATOM   3796 O  O     . GLN A 1 469 ? 35.554  16.809  19.201  1 40.06  ? 469 GLN A O     1 1 
ATOM   3797 C  CB    . GLN A 1 469 ? 37.018  19.227  16.879  1 42.94  ? 469 GLN A CB    1 1 
ATOM   3798 C  CG    . GLN A 1 469 ? 36.72   18.729  15.47   1 48.02  ? 469 GLN A CG    1 1 
ATOM   3799 C  CD    . GLN A 1 469 ? 35.306  18.273  15.336  1 55.08  ? 469 GLN A CD    1 1 
ATOM   3800 O  OE1   . GLN A 1 469 ? 34.882  17.295  15.961  1 57.69  ? 469 GLN A OE1   1 1 
ATOM   3801 N  NE2   . GLN A 1 469 ? 34.544  18.969  14.508  1 56.69  ? 469 GLN A NE2   1 1 
ATOM   3802 N  N     . GLU A 1 470 ? 35.011  18.998  18.998  1 39.97  ? 470 GLU A N     1 1 
ATOM   3803 C  CA    . GLU A 1 470 ? 33.753  18.964  19.747  1 40.71  ? 470 GLU A CA    1 1 
ATOM   3804 C  C     . GLU A 1 470 ? 32.854  17.785  19.412  1 40.73  ? 470 GLU A C     1 1 
ATOM   3805 O  O     . GLU A 1 470 ? 32.322  17.166  20.329  1 40.71  ? 470 GLU A O     1 1 
ATOM   3806 C  CB    . GLU A 1 470 ? 32.962  20.274  19.586  1 43.65  ? 470 GLU A CB    1 1 
ATOM   3807 C  CG    . GLU A 1 470 ? 31.924  20.465  20.681  1 50.54  ? 470 GLU A CG    1 1 
ATOM   3808 C  CD    . GLU A 1 470 ? 30.502  20.796  20.255  1 60.52  ? 470 GLU A CD    1 1 
ATOM   3809 O  OE1   . GLU A 1 470 ? 30.043  21.919  20.575  1 63.05  ? 470 GLU A OE1   1 1 
ATOM   3810 O  OE2   . GLU A 1 470 ? 29.837  19.933  19.63   1 62.6   ? 470 GLU A OE2   1 1 
ATOM   3811 N  N     . ASN A 1 471 ? 32.689  17.463  18.113  1 40.6   ? 471 ASN A N     1 1 
ATOM   3812 C  CA    . ASN A 1 471 ? 31.846  16.352  17.662  1 40.88  ? 471 ASN A CA    1 1 
ATOM   3813 C  C     . ASN A 1 471 ? 32.29   15.048  18.248  1 41.15  ? 471 ASN A C     1 1 
ATOM   3814 O  O     . ASN A 1 471 ? 31.459  14.257  18.681  1 41.4   ? 471 ASN A O     1 1 
ATOM   3815 C  CB    . ASN A 1 471 ? 31.841  16.233  16.142  1 41.75  ? 471 ASN A CB    1 1 
ATOM   3816 C  CG    . ASN A 1 471 ? 31.018  17.284  15.483  1 44.72  ? 471 ASN A CG    1 1 
ATOM   3817 O  OD1   . ASN A 1 471 ? 31.543  18.18   14.806  1 45.41  ? 471 ASN A OD1   1 1 
ATOM   3818 N  ND2   . ASN A 1 471 ? 29.705  17.196  15.688  1 45.52  ? 471 ASN A ND2   1 1 
ATOM   3819 N  N     . ASP A 1 472 ? 33.599  14.823  18.272  1 41.17  ? 472 ASP A N     1 1 
ATOM   3820 C  CA    . ASP A 1 472 ? 34.179  13.593  18.79   1 41.74  ? 472 ASP A CA    1 1 
ATOM   3821 C  C     . ASP A 1 472 ? 34.05   13.499  20.304  1 41.92  ? 472 ASP A C     1 1 
ATOM   3822 O  O     . ASP A 1 472 ? 33.771  12.424  20.829  1 41.72  ? 472 ASP A O     1 1 
ATOM   3823 C  CB    . ASP A 1 472 ? 35.621  13.454  18.309  1 43.43  ? 472 ASP A CB    1 1 
ATOM   3824 C  CG    . ASP A 1 472 ? 35.668  13.494  16.8    1 47.96  ? 472 ASP A CG    1 1 
ATOM   3825 O  OD1   . ASP A 1 472 ? 35.024  12.639  16.167  1 48.59  ? 472 ASP A OD1   1 1 
ATOM   3826 O  OD2   . ASP A 1 472 ? 36.286  14.42   16.252  1 50.58  ? 472 ASP A OD2   1 1 
ATOM   3827 N  N     . VAL A 1 473 ? 34.171  14.641  21.004  1 42.03  ? 473 VAL A N     1 1 
ATOM   3828 C  CA    . VAL A 1 473 ? 33.978  14.697  22.454  1 42.32  ? 473 VAL A CA    1 1 
ATOM   3829 C  C     . VAL A 1 473 ? 32.533  14.331  22.767  1 42.36  ? 473 VAL A C     1 1 
ATOM   3830 O  O     . VAL A 1 473 ? 32.282  13.483  23.615  1 42.53  ? 473 VAL A O     1 1 
ATOM   3831 C  CB    . VAL A 1 473 ? 34.338  16.086  23.025  1 42.96  ? 473 VAL A CB    1 1 
ATOM   3832 C  CG1   . VAL A 1 473 ? 34.04   16.154  24.509  1 43.56  ? 473 VAL A CG1   1 1 
ATOM   3833 C  CG2   . VAL A 1 473 ? 35.795  16.405  22.772  1 43.31  ? 473 VAL A CG2   1 1 
ATOM   3834 N  N     . ASP A 1 474 ? 31.597  14.909  22.006  1 42.22  ? 474 ASP A N     1 1 
ATOM   3835 C  CA    . ASP A 1 474 ? 30.169  14.659  22.123  1 42.48  ? 474 ASP A CA    1 1 
ATOM   3836 C  C     . ASP A 1 474 ? 29.828  13.182  21.867  1 41.81  ? 474 ASP A C     1 1 
ATOM   3837 O  O     . ASP A 1 474 ? 29.059  12.599  22.621  1 41.95  ? 474 ASP A O     1 1 
ATOM   3838 C  CB    . ASP A 1 474 ? 29.406  15.556  21.146  1 44.78  ? 474 ASP A CB    1 1 
ATOM   3839 C  CG    . ASP A 1 474 ? 27.921  15.438  21.337  1 50.82  ? 474 ASP A CG    1 1 
ATOM   3840 O  OD1   . ASP A 1 474 ? 27.441  15.776  22.442  1 52.04  ? 474 ASP A OD1   1 1 
ATOM   3841 O  OD2   . ASP A 1 474 ? 27.236  14.974  20.394  1 53.28  ? 474 ASP A OD2   1 1 
ATOM   3842 N  N     . THR A 1 475 ? 30.406  12.582  20.815  1 40.91  ? 475 THR A N     1 1 
ATOM   3843 C  CA    . THR A 1 475 ? 30.187  11.181  20.465  1 40.42  ? 475 THR A CA    1 1 
ATOM   3844 C  C     . THR A 1 475 ? 30.626  10.279  21.614  1 39.92  ? 475 THR A C     1 1 
ATOM   3845 O  O     . THR A 1 475 ? 29.874  9.401   22.029  1 39.88  ? 475 THR A O     1 1 
ATOM   3846 C  CB    . THR A 1 475 ? 30.931  10.847  19.167  1 41.33  ? 475 THR A CB    1 1 
ATOM   3847 O  OG1   . THR A 1 475 ? 30.365  11.595  18.097  1 42.45  ? 475 THR A OG1   1 1 
ATOM   3848 C  CG2   . THR A 1 475 ? 30.875  9.389   18.837  1 41.48  ? 475 THR A CG2   1 1 
ATOM   3849 N  N     . VAL A 1 476 ? 31.814  10.544  22.166  1 39.43  ? 476 VAL A N     1 1 
ATOM   3850 C  CA    . VAL A 1 476 ? 32.358  9.781   23.277  1 39.5   ? 476 VAL A CA    1 1 
ATOM   3851 C  C     . VAL A 1 476 ? 31.505  9.945   24.541  1 39.6   ? 476 VAL A C     1 1 
ATOM   3852 O  O     . VAL A 1 476 ? 31.146  8.947   25.164  1 40.18  ? 476 VAL A O     1 1 
ATOM   3853 C  CB    . VAL A 1 476 ? 33.846  10.117  23.496  1 40.15  ? 476 VAL A CB    1 1 
ATOM   3854 C  CG1   . VAL A 1 476 ? 34.358  9.532   24.804  1 40.81  ? 476 VAL A CG1   1 1 
ATOM   3855 C  CG2   . VAL A 1 476 ? 34.683  9.619   22.328  1 40.66  ? 476 VAL A CG2   1 1 
ATOM   3856 N  N     . ILE A 1 477 ? 31.116  11.176  24.879  1 38.88  ? 477 ILE A N     1 1 
ATOM   3857 C  CA    . ILE A 1 477 ? 30.287  11.427  26.052  1 38.88  ? 477 ILE A CA    1 1 
ATOM   3858 C  C     . ILE A 1 477 ? 28.933  10.716  25.935  1 39.28  ? 477 ILE A C     1 1 
ATOM   3859 O  O     . ILE A 1 477 ? 28.482  10.067  26.881  1 39.62  ? 477 ILE A O     1 1 
ATOM   3860 C  CB    . ILE A 1 477 ? 30.146  12.95   26.272  1 39.13  ? 477 ILE A CB    1 1 
ATOM   3861 C  CG1   . ILE A 1 477 ? 31.462  13.542  26.779  1 40.24  ? 477 ILE A CG1   1 1 
ATOM   3862 C  CG2   . ILE A 1 477 ? 28.988  13.304  27.206  1 39.55  ? 477 ILE A CG2   1 1 
ATOM   3863 C  CD1   . ILE A 1 477 ? 31.932  13.004  28.093  1 41.66  ? 477 ILE A CD1   1 1 
ATOM   3864 N  N     . TYR A 1 478 ? 28.31   10.804  24.759  1 38.86  ? 478 TYR A N     1 1 
ATOM   3865 C  CA    . TYR A 1 478 ? 27.027  10.17   24.519  1 38.71  ? 478 TYR A CA    1 1 
ATOM   3866 C  C     . TYR A 1 478 ? 27.156  8.66    24.605  1 38.82  ? 478 TYR A C     1 1 
ATOM   3867 O  O     . TYR A 1 478 ? 26.329  8.037   25.249  1 38.92  ? 478 TYR A O     1 1 
ATOM   3868 C  CB    . TYR A 1 478 ? 26.474  10.589  23.154  1 38.75  ? 478 TYR A CB    1 1 
ATOM   3869 C  CG    . TYR A 1 478 ? 25.062  10.119  22.887  1 39.86  ? 478 TYR A CG    1 1 
ATOM   3870 C  CD1   . TYR A 1 478 ? 23.971  10.821  23.375  1 40.91  ? 478 TYR A CD1   1 1 
ATOM   3871 C  CD2   . TYR A 1 478 ? 24.817  8.995   22.112  1 40.95  ? 478 TYR A CD2   1 1 
ATOM   3872 C  CE1   . TYR A 1 478 ? 22.67   10.4    23.123  1 41.97  ? 478 TYR A CE1   1 1 
ATOM   3873 C  CE2   . TYR A 1 478 ? 23.524  8.554   21.867  1 41.99  ? 478 TYR A CE2   1 1 
ATOM   3874 C  CZ    . TYR A 1 478 ? 22.449  9.263   22.367  1 43.08  ? 478 TYR A CZ    1 1 
ATOM   3875 O  OH    . TYR A 1 478 ? 21.165  8.824   22.111  1 44.87  ? 478 TYR A OH    1 1 
ATOM   3876 N  N     . SER A 1 479 ? 28.205  8.069   24.005  1 38.66  ? 479 SER A N     1 1 
ATOM   3877 C  CA    . SER A 1 479 ? 28.394  6.618   24.033  1 38.96  ? 479 SER A CA    1 1 
ATOM   3878 C  C     . SER A 1 479 ? 28.586  6.074   25.441  1 39.09  ? 479 SER A C     1 1 
ATOM   3879 O  O     . SER A 1 479 ? 27.998  5.056   25.783  1 39.37  ? 479 SER A O     1 1 
ATOM   3880 C  CB    . SER A 1 479 ? 29.571  6.206   23.158  1 40.42  ? 479 SER A CB    1 1 
ATOM   3881 O  OG    . SER A 1 479 ? 29.39   6.635   21.821  1 43.06  ? 479 SER A OG    1 1 
ATOM   3882 N  N     . ILE A 1 480 ? 29.389  6.755   26.261  1 38.87  ? 480 ILE A N     1 1 
ATOM   3883 C  CA    . ILE A 1 480 ? 29.66   6.33    27.63   1 39.15  ? 480 ILE A CA    1 1 
ATOM   3884 C  C     . ILE A 1 480 ? 28.419  6.4     28.517  1 39.98  ? 480 ILE A C     1 1 
ATOM   3885 O  O     . ILE A 1 480 ? 28.077  5.428   29.177  1 39.97  ? 480 ILE A O     1 1 
ATOM   3886 C  CB    . ILE A 1 480 ? 30.839  7.16    28.213  1 39.13  ? 480 ILE A CB    1 1 
ATOM   3887 C  CG1   . ILE A 1 480 ? 32.164  6.774   27.554  1 39.88  ? 480 ILE A CG1   1 1 
ATOM   3888 C  CG2   . ILE A 1 480 ? 30.926  7.059   29.741  1 39.37  ? 480 ILE A CG2   1 1 
ATOM   3889 C  CD1   . ILE A 1 480 ? 33.256  7.754   27.825  1 41.12  ? 480 ILE A CD1   1 1 
ATOM   3890 N  N     . PHE A 1 481 ? 27.749  7.547   28.535  1 40.68  ? 481 PHE A N     1 1 
ATOM   3891 C  CA    . PHE A 1 481 ? 26.624  7.775   29.424  1 41.59  ? 481 PHE A CA    1 1 
ATOM   3892 C  C     . PHE A 1 481 ? 25.303  7.218   28.935  1 42.86  ? 481 PHE A C     1 1 
ATOM   3893 O  O     . PHE A 1 481 ? 24.421  6.981   29.754  1 42.78  ? 481 PHE A O     1 1 
ATOM   3894 C  CB    . PHE A 1 481 ? 26.516  9.27    29.748  1 41.19  ? 481 PHE A CB    1 1 
ATOM   3895 C  CG    . PHE A 1 481 ? 27.641  9.716   30.656  1 41.49  ? 481 PHE A CG    1 1 
ATOM   3896 C  CD1   . PHE A 1 481 ? 27.659  9.356   31.99   1 42.06  ? 481 PHE A CD1   1 1 
ATOM   3897 C  CD2   . PHE A 1 481 ? 28.72   10.418  30.155  1 42.09  ? 481 PHE A CD2   1 1 
ATOM   3898 C  CE1   . PHE A 1 481 ? 28.71   9.725   32.813  1 42.52  ? 481 PHE A CE1   1 1 
ATOM   3899 C  CE2   . PHE A 1 481 ? 29.778  10.773  30.978  1 42.7   ? 481 PHE A CE2   1 1 
ATOM   3900 C  CZ    . PHE A 1 481 ? 29.761  10.432  32.303  1 42.36  ? 481 PHE A CZ    1 1 
ATOM   3901 N  N     . LYS A 1 482 ? 25.167  6.974   27.633  1 44.01  ? 482 LYS A N     1 1 
ATOM   3902 C  CA    . LYS A 1 482 ? 23.923  6.446   27.086  1 45.73  ? 482 LYS A CA    1 1 
ATOM   3903 C  C     . LYS A 1 482 ? 23.953  4.944   26.827  1 47.34  ? 482 LYS A C     1 1 
ATOM   3904 O  O     . LYS A 1 482 ? 22.899  4.314   26.88   1 47.13  ? 482 LYS A O     1 1 
ATOM   3905 C  CB    . LYS A 1 482 ? 23.521  7.196   25.807  1 47.76  ? 482 LYS A CB    1 1 
ATOM   3906 C  CG    . LYS A 1 482 ? 22.186  7.915   25.914  1 52.76  ? 482 LYS A CG    1 1 
ATOM   3907 C  CD    . LYS A 1 482 ? 22.192  9.037   26.957  1 57.45  ? 482 LYS A CD    1 1 
ATOM   3908 C  CE    . LYS A 1 482 ? 20.794  9.574   27.172  1 61.01  ? 482 LYS A CE    1 1 
ATOM   3909 N  NZ    . LYS A 1 482 ? 20.742  10.616  28.234  1 62.88  ? 482 LYS A NZ    1 1 
ATOM   3910 N  N     . TYR A 1 483 ? 25.14   4.363   26.549  1 48.62  ? 483 TYR A N     1 1 
ATOM   3911 C  CA    . TYR A 1 483 ? 25.212  2.94    26.222  1 50.2   ? 483 TYR A CA    1 1 
ATOM   3912 C  C     . TYR A 1 483 ? 26.045  2.087   27.165  1 51.4   ? 483 TYR A C     1 1 
ATOM   3913 O  O     . TYR A 1 483 ? 25.617  0.981   27.501  1 51.77  ? 483 TYR A O     1 1 
ATOM   3914 C  CB    . TYR A 1 483 ? 25.688  2.742   24.776  1 50.56  ? 483 TYR A CB    1 1 
ATOM   3915 C  CG    . TYR A 1 483 ? 24.715  3.356   23.804  1 51.82  ? 483 TYR A CG    1 1 
ATOM   3916 C  CD1   . TYR A 1 483 ? 23.384  2.974   23.795  1 53.07  ? 483 TYR A CD1   1 1 
ATOM   3917 C  CD2   . TYR A 1 483 ? 25.098  4.394   22.968  1 52.95  ? 483 TYR A CD2   1 1 
ATOM   3918 C  CE1   . TYR A 1 483 ? 22.459  3.594   22.968  1 54.22  ? 483 TYR A CE1   1 1 
ATOM   3919 C  CE2   . TYR A 1 483 ? 24.186  5.011   22.121  1 54.02  ? 483 TYR A CE2   1 1 
ATOM   3920 C  CZ    . TYR A 1 483 ? 22.863  4.609   22.127  1 55.2   ? 483 TYR A CZ    1 1 
ATOM   3921 O  OH    . TYR A 1 483 ? 21.926  5.196   21.309  1 56.97  ? 483 TYR A OH    1 1 
ATOM   3922 N  N     . ILE A 1 484 ? 27.229  2.553   27.56   1 51.85  ? 484 ILE A N     1 1 
ATOM   3923 C  CA    . ILE A 1 484 ? 28.097  1.758   28.424  1 52.91  ? 484 ILE A CA    1 1 
ATOM   3924 C  C     . ILE A 1 484 ? 27.624  1.742   29.882  1 53.54  ? 484 ILE A C     1 1 
ATOM   3925 O  O     . ILE A 1 484 ? 27.378  0.669   30.422  1 53.87  ? 484 ILE A O     1 1 
ATOM   3926 C  CB    . ILE A 1 484 ? 29.576  2.186   28.289  1 53.82  ? 484 ILE A CB    1 1 
ATOM   3927 C  CG1   . ILE A 1 484 ? 30.057  2.031   26.843  1 55.08  ? 484 ILE A CG1   1 1 
ATOM   3928 C  CG2   . ILE A 1 484 ? 30.458  1.403   29.254  1 54.35  ? 484 ILE A CG2   1 1 
ATOM   3929 C  CD1   . ILE A 1 484 ? 31.405  2.644   26.582  1 56.53  ? 484 ILE A CD1   1 1 
ATOM   3930 N  N     . VAL A 1 485 ? 27.487  2.913   30.508  1 53.64  ? 485 VAL A N     1 1 
ATOM   3931 C  CA    . VAL A 1 485 ? 27.083  3.037   31.898  1 54.45  ? 485 VAL A CA    1 1 
ATOM   3932 C  C     . VAL A 1 485 ? 25.587  2.751   32.099  1 55.34  ? 485 VAL A C     1 1 
ATOM   3933 O  O     . VAL A 1 485 ? 24.724  3.495   31.627  1 55.27  ? 485 VAL A O     1 1 
ATOM   3934 C  CB    . VAL A 1 485 ? 27.487  4.424   32.447  1 55.17  ? 485 VAL A CB    1 1 
ATOM   3935 C  CG1   . VAL A 1 485 ? 26.993  4.619   33.871  1 55.89  ? 485 VAL A CG1   1 1 
ATOM   3936 C  CG2   . VAL A 1 485 ? 28.995  4.631   32.365  1 55.49  ? 485 VAL A CG2   1 1 
ATOM   3937 N  N     . PRO A 1 486 ? 25.265  1.666   32.82   1 56     ? 486 PRO A N     1 1 
ATOM   3938 C  CA    . PRO A 1 486 ? 23.851  1.34    33.06   1 56.37  ? 486 PRO A CA    1 1 
ATOM   3939 C  C     . PRO A 1 486 ? 23.257  2.042   34.288  1 56.89  ? 486 PRO A C     1 1 
ATOM   3940 O  O     . PRO A 1 486 ? 22.887  1.388   35.266  1 57.11  ? 486 PRO A O     1 1 
ATOM   3941 C  CB    . PRO A 1 486 ? 23.868  -0.181  33.233  1 57.1   ? 486 PRO A CB    1 1 
ATOM   3942 C  CG    . PRO A 1 486 ? 25.266  -0.513  33.698  1 57.49  ? 486 PRO A CG    1 1 
ATOM   3943 C  CD    . PRO A 1 486 ? 26.17   0.664   33.422  1 55.78  ? 486 PRO A CD    1 1 
ATOM   3944 N  N     . ASN A 1 494 ? 17.507  2.7     31.12   1 63.22  ? 494 ASN A N     1 1 
ATOM   3945 C  CA    . ASN A 1 494 ? 16.085  3.034   31.203  1 63.93  ? 494 ASN A CA    1 1 
ATOM   3946 C  C     . ASN A 1 494 ? 15.748  4.555   31.14   1 64.04  ? 494 ASN A C     1 1 
ATOM   3947 O  O     . ASN A 1 494 ? 14.798  4.896   30.421  1 64.13  ? 494 ASN A O     1 1 
ATOM   3948 C  CB    . ASN A 1 494 ? 15.433  2.397   32.429  1 65.44  ? 494 ASN A CB    1 1 
ATOM   3949 C  CG    . ASN A 1 494 ? 14.798  1.068   32.134  1 69.06  ? 494 ASN A CG    1 1 
ATOM   3950 O  OD1   . ASN A 1 494 ? 15.366  0.225   31.427  1 70.35  ? 494 ASN A OD1   1 1 
ATOM   3951 N  ND2   . ASN A 1 494 ? 13.602  0.853   32.668  1 69.72  ? 494 ASN A ND2   1 1 
ATOM   3952 N  N     . PRO A 1 495 ? 16.44   5.484   31.867  1 63.62  ? 495 PRO A N     1 1 
ATOM   3953 C  CA    . PRO A 1 495 ? 16.043  6.899   31.776  1 63.34  ? 495 PRO A CA    1 1 
ATOM   3954 C  C     . PRO A 1 495 ? 16.5    7.586   30.491  1 63.29  ? 495 PRO A C     1 1 
ATOM   3955 O  O     . PRO A 1 495 ? 17.613  7.363   30.016  1 63.3   ? 495 PRO A O     1 1 
ATOM   3956 C  CB    . PRO A 1 495 ? 16.659  7.528   33.03   1 63.89  ? 495 PRO A CB    1 1 
ATOM   3957 C  CG    . PRO A 1 495 ? 17.822  6.699   33.335  1 64.29  ? 495 PRO A CG    1 1 
ATOM   3958 C  CD    . PRO A 1 495 ? 17.572  5.308   32.804  1 62.91  ? 495 PRO A CD    1 1 
ATOM   3959 N  N     . PRO A 1 496 ? 15.636  8.435   29.91   1 62.96  ? 496 PRO A N     1 1 
ATOM   3960 C  CA    . PRO A 1 496 ? 16.016  9.128   28.67   1 62.66  ? 496 PRO A CA    1 1 
ATOM   3961 C  C     . PRO A 1 496 ? 17.002  10.283  28.887  1 62.16  ? 496 PRO A C     1 1 
ATOM   3962 O  O     . PRO A 1 496 ? 17.842  10.54   28.027  1 62.41  ? 496 PRO A O     1 1 
ATOM   3963 C  CB    . PRO A 1 496 ? 14.67   9.632   28.112  1 63.35  ? 496 PRO A CB    1 1 
ATOM   3964 C  CG    . PRO A 1 496 ? 13.594  9.047   29.013  1 63.8   ? 496 PRO A CG    1 1 
ATOM   3965 C  CD    . PRO A 1 496 ? 14.263  8.779   30.321  1 62.38  ? 496 PRO A CD    1 1 
ATOM   3966 N  N     . GLY A 1 497 ? 16.896  10.961  30.026  1 61.17  ? 497 GLY A N     1 1 
ATOM   3967 C  CA    . GLY A 1 497 ? 17.756  12.097  30.328  1 60.61  ? 497 GLY A CA    1 1 
ATOM   3968 C  C     . GLY A 1 497 ? 17.354  13.302  29.508  1 59.74  ? 497 GLY A C     1 1 
ATOM   3969 O  O     . GLY A 1 497 ? 16.177  13.473  29.204  1 59.79  ? 497 GLY A O     1 1 
ATOM   3970 N  N     . GLY A 1 498 ? 18.325  14.103  29.1    1 58.99  ? 498 GLY A N     1 1 
ATOM   3971 C  CA    . GLY A 1 498 ? 18.046  15.281  28.295  1 58.94  ? 498 GLY A CA    1 1 
ATOM   3972 C  C     . GLY A 1 498 ? 19.093  15.637  27.265  1 58.89  ? 498 GLY A C     1 1 
ATOM   3973 O  O     . GLY A 1 498 ? 20.189  15.07   27.245  1 59.15  ? 498 GLY A O     1 1 
ATOM   3974 N  N     . ASP A 1 499 ? 18.742  16.6    26.406  1 58.54  ? 499 ASP A N     1 1 
ATOM   3975 C  CA    . ASP A 1 499 ? 19.579  17.182  25.353  1 58.71  ? 499 ASP A CA    1 1 
ATOM   3976 C  C     . ASP A 1 499 ? 19.003  18.577  24.936  1 58.24  ? 499 ASP A C     1 1 
ATOM   3977 O  O     . ASP A 1 499 ? 18.231  19.158  25.7    1 58.47  ? 499 ASP A O     1 1 
ATOM   3978 C  CB    . ASP A 1 499 ? 19.761  16.2    24.17   1 60.9   ? 499 ASP A CB    1 1 
ATOM   3979 C  CG    . ASP A 1 499 ? 18.497  15.851  23.406  1 66.42  ? 499 ASP A CG    1 1 
ATOM   3980 O  OD1   . ASP A 1 499 ? 17.449  16.484  23.661  1 67.2   ? 499 ASP A OD1   1 1 
ATOM   3981 O  OD2   . ASP A 1 499 ? 18.557  14.949  22.547  1 69.24  ? 499 ASP A OD2   1 1 
ATOM   3982 N  N     . TRP A 1 500 ? 19.357  19.112  23.75   1 57.34  ? 500 TRP A N     1 1 
ATOM   3983 C  CA    . TRP A 1 500 ? 18.834  20.402  23.305  1 56.89  ? 500 TRP A CA    1 1 
ATOM   3984 C  C     . TRP A 1 500 ? 17.335  20.366  22.993  1 56.09  ? 500 TRP A C     1 1 
ATOM   3985 O  O     . TRP A 1 500 ? 16.689  21.414  23.045  1 56.36  ? 500 TRP A O     1 1 
ATOM   3986 C  CB    . TRP A 1 500 ? 19.611  20.913  22.09   1 56.87  ? 500 TRP A CB    1 1 
ATOM   3987 N  N     . SER A 1 501 ? 16.778  19.169  22.684  1 54.91  ? 501 SER A N     1 1 
ATOM   3988 C  CA    . SER A 1 501 ? 15.361  18.979  22.333  1 54.07  ? 501 SER A CA    1 1 
ATOM   3989 C  C     . SER A 1 501 ? 14.402  18.871  23.527  1 52.79  ? 501 SER A C     1 1 
ATOM   3990 O  O     . SER A 1 501 ? 13.193  19.034  23.357  1 52.77  ? 501 SER A O     1 1 
ATOM   3991 C  CB    . SER A 1 501 ? 15.188  17.768  21.419  1 55.33  ? 501 SER A CB    1 1 
ATOM   3992 O  OG    . SER A 1 501 ? 15.304  16.54   22.122  1 57.41  ? 501 SER A OG    1 1 
ATOM   3993 N  N     . GLY A 1 502 ? 14.932  18.58   24.705  1 51.58  ? 502 GLY A N     1 1 
ATOM   3994 C  CA    . GLY A 1 502 ? 14.105  18.462  25.895  1 50.9   ? 502 GLY A CA    1 1 
ATOM   3995 C  C     . GLY A 1 502 ? 14.766  17.719  27.03   1 49.9   ? 502 GLY A C     1 1 
ATOM   3996 O  O     . GLY A 1 502 ? 15.736  16.99   26.82   1 49.85  ? 502 GLY A O     1 1 
ATOM   3997 N  N     . LEU A 1 503 ? 14.235  17.897  28.243  1 48.94  ? 503 LEU A N     1 1 
ATOM   3998 C  CA    . LEU A 1 503 ? 14.736  17.222  29.433  1 48.36  ? 503 LEU A CA    1 1 
ATOM   3999 C  C     . LEU A 1 503 ? 13.662  16.293  30.015  1 48.14  ? 503 LEU A C     1 1 
ATOM   4000 O  O     . LEU A 1 503 ? 12.58   16.738  30.376  1 48.12  ? 503 LEU A O     1 1 
ATOM   4001 C  CB    . LEU A 1 503 ? 15.186  18.242  30.491  1 48.04  ? 503 LEU A CB    1 1 
ATOM   4002 C  CG    . LEU A 1 503 ? 15.533  17.668  31.856  1 49.07  ? 503 LEU A CG    1 1 
ATOM   4003 C  CD1   . LEU A 1 503 ? 16.736  16.756  31.775  1 49.77  ? 503 LEU A CD1   1 1 
ATOM   4004 C  CD2   . LEU A 1 503 ? 15.721  18.752  32.86   1 49.46  ? 503 LEU A CD2   1 1 
ATOM   4005 N  N     . SER A 1 504 ? 13.996  15.019  30.159  1 47.73  ? 504 SER A N     1 1 
ATOM   4006 C  CA    . SER A 1 504 ? 13.113  14.047  30.768  1 47.67  ? 504 SER A CA    1 1 
ATOM   4007 C  C     . SER A 1 504 ? 13.682  13.616  32.112  1 47.75  ? 504 SER A C     1 1 
ATOM   4008 O  O     . SER A 1 504 ? 14.884  13.353  32.235  1 47.95  ? 504 SER A O     1 1 
ATOM   4009 C  CB    . SER A 1 504 ? 12.962  12.825  29.875  1 48.72  ? 504 SER A CB    1 1 
ATOM   4010 O  OG    . SER A 1 504 ? 12.326  13.158  28.656  1 50.7   ? 504 SER A OG    1 1 
ATOM   4011 N  N     . ILE A 1 505 ? 12.81   13.548  33.12   1 47.35  ? 505 ILE A N     1 1 
ATOM   4012 C  CA    . ILE A 1 505 ? 13.137  13.1    34.465  1 47.59  ? 505 ILE A CA    1 1 
ATOM   4013 C  C     . ILE A 1 505 ? 12.161  11.973  34.816  1 48.17  ? 505 ILE A C     1 1 
ATOM   4014 O  O     . ILE A 1 505 ? 10.959  12.182  34.726  1 48     ? 505 ILE A O     1 1 
ATOM   4015 C  CB    . ILE A 1 505 ? 13.022  14.253  35.483  1 47.7   ? 505 ILE A CB    1 1 
ATOM   4016 C  CG1   . ILE A 1 505 ? 13.969  15.418  35.131  1 48.68  ? 505 ILE A CG1   1 1 
ATOM   4017 C  CG2   . ILE A 1 505 ? 13.268  13.722  36.876  1 47.92  ? 505 ILE A CG2   1 1 
ATOM   4018 C  CD1   . ILE A 1 505 ? 14.022  16.576  36.146  1 50     ? 505 ILE A CD1   1 1 
ATOM   4019 N  N     . ILE A 1 506 ? 12.656  10.779  35.185  1 48.66  ? 506 ILE A N     1 1 
ATOM   4020 C  CA    . ILE A 1 506 ? 11.769  9.669   35.529  1 49.57  ? 506 ILE A CA    1 1 
ATOM   4021 C  C     . ILE A 1 506 ? 11.821  9.3     37.013  1 50.07  ? 506 ILE A C     1 1 
ATOM   4022 O  O     . ILE A 1 506 ? 12.814  9.57    37.698  1 50.19  ? 506 ILE A O     1 1 
ATOM   4023 C  CB    . ILE A 1 506 ? 12.036  8.423   34.642  1 50.37  ? 506 ILE A CB    1 1 
ATOM   4024 C  CG1   . ILE A 1 506 ? 13.378  7.754   34.982  1 51.66  ? 506 ILE A CG1   1 1 
ATOM   4025 C  CG2   . ILE A 1 506 ? 11.954  8.756   33.172  1 50.84  ? 506 ILE A CG2   1 1 
ATOM   4026 C  CD1   . ILE A 1 506 ? 13.412  6.283   34.685  1 53.14  ? 506 ILE A CD1   1 1 
ATOM   4027 N  N     . ASP A 1 507 ? 10.741  8.673   37.502  1 50.09  ? 507 ASP A N     1 1 
ATOM   4028 C  CA    . ASP A 1 507 ? 10.677  8.121   38.853  1 50.63  ? 507 ASP A CA    1 1 
ATOM   4029 C  C     . ASP A 1 507 ? 10.159  6.645   38.757  1 51.06  ? 507 ASP A C     1 1 
ATOM   4030 O  O     . ASP A 1 507 ? 10.416  5.997   37.731  1 51.18  ? 507 ASP A O     1 1 
ATOM   4031 C  CB    . ASP A 1 507 ? 9.934   9.046   39.858  1 51.95  ? 507 ASP A CB    1 1 
ATOM   4032 C  CG    . ASP A 1 507 ? 8.475   9.297   39.566  1 55.72  ? 507 ASP A CG    1 1 
ATOM   4033 O  OD1   . ASP A 1 507 ? 7.948   8.666   38.65   1 56.24  ? 507 ASP A OD1   1 1 
ATOM   4034 O  OD2   . ASP A 1 507 ? 7.861   10.134  40.266  1 57.81  ? 507 ASP A OD2   1 1 
ATOM   4035 N  N     . ASN A 1 508 ? 9.491   6.098   39.792  1 51     ? 508 ASN A N     1 1 
ATOM   4036 C  CA    . ASN A 1 508 ? 9.014   4.715   39.718  1 51.46  ? 508 ASN A CA    1 1 
ATOM   4037 C  C     . ASN A 1 508 ? 7.664   4.565   38.989  1 51.49  ? 508 ASN A C     1 1 
ATOM   4038 O  O     . ASN A 1 508 ? 7.281   3.443   38.656  1 51.54  ? 508 ASN A O     1 1 
ATOM   4039 C  CB    . ASN A 1 508 ? 8.987   4.056   41.099  1 52.6   ? 508 ASN A CB    1 1 
ATOM   4040 C  CG    . ASN A 1 508 ? 10.208  3.206   41.41   1 55.44  ? 508 ASN A CG    1 1 
ATOM   4041 O  OD1   . ASN A 1 508 ? 10.127  2.227   42.156  1 56.42  ? 508 ASN A OD1   1 1 
ATOM   4042 N  ND2   . ASN A 1 508 ? 11.369  3.549   40.852  1 55.96  ? 508 ASN A ND2   1 1 
ATOM   4043 N  N     . VAL A 1 509 ? 6.97    5.678   38.7    1 51.15  ? 509 VAL A N     1 1 
ATOM   4044 C  CA    . VAL A 1 509 ? 5.684   5.614   38.019  1 51.42  ? 509 VAL A CA    1 1 
ATOM   4045 C  C     . VAL A 1 509 ? 5.612   6.499   36.763  1 51.9   ? 509 VAL A C     1 1 
ATOM   4046 O  O     . VAL A 1 509 ? 5.035   6.075   35.767  1 52.01  ? 509 VAL A O     1 1 
ATOM   4047 C  CB    . VAL A 1 509 ? 4.511   5.907   38.999  1 51.99  ? 509 VAL A CB    1 1 
ATOM   4048 C  CG1   . VAL A 1 509 ? 4.763   7.162   39.827  1 52.56  ? 509 VAL A CG1   1 1 
ATOM   4049 C  CG2   . VAL A 1 509 ? 3.174   5.999   38.271  1 52.32  ? 509 VAL A CG2   1 1 
ATOM   4050 N  N     . HIS A 1 510 ? 6.188   7.721   36.806  1 51.97  ? 510 HIS A N     1 1 
ATOM   4051 C  CA    . HIS A 1 510 ? 6.107   8.711   35.725  1 52.14  ? 510 HIS A CA    1 1 
ATOM   4052 C  C     . HIS A 1 510 ? 7.417   9.151   35.071  1 51.13  ? 510 HIS A C     1 1 
ATOM   4053 O  O     . HIS A 1 510 ? 8.502   9.013   35.635  1 51.04  ? 510 HIS A O     1 1 
ATOM   4054 C  CB    . HIS A 1 510 ? 5.421   9.997   36.239  1 53.95  ? 510 HIS A CB    1 1 
ATOM   4055 C  CG    . HIS A 1 510 ? 4.022   9.828   36.719  1 57.91  ? 510 HIS A CG    1 1 
ATOM   4056 N  ND1   . HIS A 1 510 ? 3.727   9.789   38.071  1 60.17  ? 510 HIS A ND1   1 1 
ATOM   4057 C  CD2   . HIS A 1 510 ? 2.87    9.758   36.015  1 59.75  ? 510 HIS A CD2   1 1 
ATOM   4058 C  CE1   . HIS A 1 510 ? 2.412   9.671   38.146  1 61.09  ? 510 HIS A CE1   1 1 
ATOM   4059 N  NE2   . HIS A 1 510 ? 1.851   9.649   36.934  1 61.17  ? 510 HIS A NE2   1 1 
ATOM   4060 N  N     . GLU A 1 511 ? 7.275   9.754   33.885  1 50.18  ? 511 GLU A N     1 1 
ATOM   4061 C  CA    . GLU A 1 511 ? 8.327   10.42   33.147  1 49.85  ? 511 GLU A CA    1 1 
ATOM   4062 C  C     . GLU A 1 511 ? 7.808   11.852  32.95   1 49.54  ? 511 GLU A C     1 1 
ATOM   4063 O  O     . GLU A 1 511 ? 6.717   12.035  32.425  1 49.7   ? 511 GLU A O     1 1 
ATOM   4064 C  CB    . GLU A 1 511 ? 8.573   9.757   31.786  1 51.46  ? 511 GLU A CB    1 1 
ATOM   4065 C  CG    . GLU A 1 511 ? 9.605   10.511  30.965  1 55.01  ? 511 GLU A CG    1 1 
ATOM   4066 C  CD    . GLU A 1 511 ? 9.868   9.962   29.579  1 59.62  ? 511 GLU A CD    1 1 
ATOM   4067 O  OE1   . GLU A 1 511 ? 9.374   8.853   29.273  1 60.33  ? 511 GLU A OE1   1 1 
ATOM   4068 O  OE2   . GLU A 1 511 ? 10.558  10.648  28.791  1 61.17  ? 511 GLU A OE2   1 1 
ATOM   4069 N  N     . PHE A 1 512 ? 8.552   12.853  33.424  1 48.88  ? 512 PHE A N     1 1 
ATOM   4070 C  CA    . PHE A 1 512 ? 8.215   14.276  33.308  1 48.62  ? 512 PHE A CA    1 1 
ATOM   4071 C  C     . PHE A 1 512 ? 9.13    14.874  32.245  1 47.69  ? 512 PHE A C     1 1 
ATOM   4072 O  O     . PHE A 1 512 ? 10.312  14.558  32.234  1 47.95  ? 512 PHE A O     1 1 
ATOM   4073 C  CB    . PHE A 1 512 ? 8.436   14.985  34.652  1 48.92  ? 512 PHE A CB    1 1 
ATOM   4074 C  CG    . PHE A 1 512 ? 7.707   14.329  35.801  1 50.22  ? 512 PHE A CG    1 1 
ATOM   4075 C  CD1   . PHE A 1 512 ? 6.388   14.644  36.076  1 51.31  ? 512 PHE A CD1   1 1 
ATOM   4076 C  CD2   . PHE A 1 512 ? 8.341   13.396  36.606  1 51.34  ? 512 PHE A CD2   1 1 
ATOM   4077 C  CE1   . PHE A 1 512 ? 5.716   14.03   37.13   1 52.14  ? 512 PHE A CE1   1 1 
ATOM   4078 C  CE2   . PHE A 1 512 ? 7.66    12.774  37.652  1 52.19  ? 512 PHE A CE2   1 1 
ATOM   4079 C  CZ    . PHE A 1 512 ? 6.355   13.099  37.91   1 51.95  ? 512 PHE A CZ    1 1 
ATOM   4080 N  N     . ARG A 1 513 ? 8.605   15.706  31.345  1 46.61  ? 513 ARG A N     1 1 
ATOM   4081 C  CA    . ARG A 1 513 ? 9.416   16.249  30.266  1 46.1   ? 513 ARG A CA    1 1 
ATOM   4082 C  C     . ARG A 1 513 ? 9.192   17.74   30.013  1 45.42  ? 513 ARG A C     1 1 
ATOM   4083 O  O     . ARG A 1 513 ? 8.056   18.193  29.921  1 45.35  ? 513 ARG A O     1 1 
ATOM   4084 C  CB    . ARG A 1 513 ? 9.213   15.412  28.991  1 47.22  ? 513 ARG A CB    1 1 
ATOM   4085 C  CG    . ARG A 1 513 ? 10.153  15.77   27.854  1 50.18  ? 513 ARG A CG    1 1 
ATOM   4086 C  CD    . ARG A 1 513 ? 10.193  14.695  26.781  1 53.18  ? 513 ARG A CD    1 1 
ATOM   4087 N  NE    . ARG A 1 513 ? 11.01   15.085  25.629  1 56.69  ? 513 ARG A NE    1 1 
ATOM   4088 C  CZ    . ARG A 1 513 ? 12.338  14.972  25.572  1 60.21  ? 513 ARG A CZ    1 1 
ATOM   4089 N  NH1   . ARG A 1 513 ? 13.018  14.485  26.605  1 60.06  ? 513 ARG A NH1   1 1 
ATOM   4090 N  NH2   . ARG A 1 513 ? 12.996  15.346  24.481  1 60.8   ? 513 ARG A NH2   1 1 
ATOM   4091 N  N     . TRP A 1 514 ? 10.292  18.501  29.921  1 44.82  ? 514 TRP A N     1 1 
ATOM   4092 C  CA    . TRP A 1 514 ? 10.272  19.933  29.632  1 44.78  ? 514 TRP A CA    1 1 
ATOM   4093 C  C     . TRP A 1 514 ? 10.643  20.076  28.178  1 45.33  ? 514 TRP A C     1 1 
ATOM   4094 O  O     . TRP A 1 514 ? 11.72   19.655  27.78   1 45.34  ? 514 TRP A O     1 1 
ATOM   4095 C  CB    . TRP A 1 514 ? 11.309  20.693  30.469  1 44.17  ? 514 TRP A CB    1 1 
ATOM   4096 C  CG    . TRP A 1 514 ? 10.907  20.987  31.881  1 44.2   ? 514 TRP A CG    1 1 
ATOM   4097 C  CD1   . TRP A 1 514 ? 10.425  22.165  32.367  1 45.04  ? 514 TRP A CD1   1 1 
ATOM   4098 C  CD2   . TRP A 1 514 ? 11.052  20.117  33.011  1 44.25  ? 514 TRP A CD2   1 1 
ATOM   4099 N  NE1   . TRP A 1 514 ? 10.238  22.074  33.727  1 45.35  ? 514 TRP A NE1   1 1 
ATOM   4100 C  CE2   . TRP A 1 514 ? 10.614  20.826  34.147  1 44.97  ? 514 TRP A CE2   1 1 
ATOM   4101 C  CE3   . TRP A 1 514 ? 11.486  18.798  33.171  1 44.93  ? 514 TRP A CE3   1 1 
ATOM   4102 C  CZ2   . TRP A 1 514 ? 10.598  20.258  35.421  1 45.53  ? 514 TRP A CZ2   1 1 
ATOM   4103 C  CZ3   . TRP A 1 514 ? 11.451  18.232  34.429  1 45.74  ? 514 TRP A CZ3   1 1 
ATOM   4104 C  CH2   . TRP A 1 514 ? 11.023  18.962  35.538  1 45.73  ? 514 TRP A CH2   1 1 
ATOM   4105 N  N     . LEU A 1 515 ? 9.759   20.652  27.383  1 45.67  ? 515 LEU A N     1 1 
ATOM   4106 C  CA    . LEU A 1 515 ? 9.991   20.839  25.955  1 46.45  ? 515 LEU A CA    1 1 
ATOM   4107 C  C     . LEU A 1 515 ? 10.292  22.306  25.64   1 46.94  ? 515 LEU A C     1 1 
ATOM   4108 O  O     . LEU A 1 515 ? 10.055  23.173  26.483  1 47.05  ? 515 LEU A O     1 1 
ATOM   4109 C  CB    . LEU A 1 515 ? 8.75    20.389  25.172  1 46.86  ? 515 LEU A CB    1 1 
ATOM   4110 C  CG    . LEU A 1 515 ? 8.271   18.985  25.447  1 48.45  ? 515 LEU A CG    1 1 
ATOM   4111 C  CD1   . LEU A 1 515 ? 6.892   18.774  24.88   1 49.14  ? 515 LEU A CD1   1 1 
ATOM   4112 C  CD2   . LEU A 1 515 ? 9.248   17.977  24.905  1 49.21  ? 515 LEU A CD2   1 1 
ATOM   4113 N  N     . SER A 1 516 ? 10.787  22.583  24.416  1 47.11  ? 516 SER A N     1 1 
ATOM   4114 C  CA    . SER A 1 516 ? 11.116  23.933  23.956  1 47.8   ? 516 SER A CA    1 1 
ATOM   4115 C  C     . SER A 1 516 ? 12.142  24.602  24.873  1 48.26  ? 516 SER A C     1 1 
ATOM   4116 O  O     . SER A 1 516 ? 11.881  25.666  25.445  1 48.66  ? 516 SER A O     1 1 
ATOM   4117 C  CB    . SER A 1 516 ? 9.857   24.787  23.812  1 49.12  ? 516 SER A CB    1 1 
ATOM   4118 O  OG    . SER A 1 516 ? 8.875   24.114  23.042  1 51.43  ? 516 SER A OG    1 1 
ATOM   4119 N  N     . LEU A 1 517 ? 13.307  23.965  25.023  1 47.97  ? 517 LEU A N     1 1 
ATOM   4120 C  CA    . LEU A 1 517 ? 14.353  24.493  25.889  1 48.12  ? 517 LEU A CA    1 1 
ATOM   4121 C  C     . LEU A 1 517 ? 15.106  25.677  25.286  1 48.21  ? 517 LEU A C     1 1 
ATOM   4122 O  O     . LEU A 1 517 ? 15.776  25.517  24.265  1 48.18  ? 517 LEU A O     1 1 
ATOM   4123 C  CB    . LEU A 1 517 ? 15.356  23.387  26.241  1 48.11  ? 517 LEU A CB    1 1 
ATOM   4124 C  CG    . LEU A 1 517 ? 14.824  22.127  26.897  1 49.18  ? 517 LEU A CG    1 1 
ATOM   4125 C  CD1   . LEU A 1 517 ? 15.969  21.241  27.303  1 49.61  ? 517 LEU A CD1   1 1 
ATOM   4126 C  CD2   . LEU A 1 517 ? 13.974  22.441  28.12   1 49.7   ? 517 LEU A CD2   1 1 
ATOM   4127 N  N     . PRO A 1 518 ? 15.074  26.861  25.936  1 48.08  ? 518 PRO A N     1 1 
ATOM   4128 C  CA    . PRO A 1 518 ? 15.861  27.99   25.418  1 48.11  ? 518 PRO A CA    1 1 
ATOM   4129 C  C     . PRO A 1 518 ? 17.375  27.746  25.544  1 48.24  ? 518 PRO A C     1 1 
ATOM   4130 O  O     . PRO A 1 518 ? 17.82   26.955  26.371  1 48.34  ? 518 PRO A O     1 1 
ATOM   4131 C  CB    . PRO A 1 518 ? 15.403  29.163  26.291  1 48.62  ? 518 PRO A CB    1 1 
ATOM   4132 C  CG    . PRO A 1 518 ? 14.978  28.539  27.565  1 48.91  ? 518 PRO A CG    1 1 
ATOM   4133 C  CD    . PRO A 1 518 ? 14.342  27.233  27.165  1 47.45  ? 518 PRO A CD    1 1 
ATOM   4134 N  N     . ARG A 1 519 ? 18.164  28.413  24.704  1 47.88  ? 519 ARG A N     1 1 
ATOM   4135 C  CA    . ARG A 1 519 ? 19.617  28.284  24.703  1 47.77  ? 519 ARG A CA    1 1 
ATOM   4136 C  C     . ARG A 1 519 ? 20.206  28.757  26.042  1 47     ? 519 ARG A C     1 1 
ATOM   4137 O  O     . ARG A 1 519 ? 21.147  28.158  26.552  1 46.75  ? 519 ARG A O     1 1 
ATOM   4138 C  CB    . ARG A 1 519 ? 20.17   29.072  23.514  1 49.88  ? 519 ARG A CB    1 1 
ATOM   4139 C  CG    . ARG A 1 519 ? 21.672  29.015  23.307  1 54.88  ? 519 ARG A CG    1 1 
ATOM   4140 C  CD    . ARG A 1 519 ? 22.119  30.133  22.375  1 60.14  ? 519 ARG A CD    1 1 
ATOM   4141 N  NE    . ARG A 1 519 ? 21.621  31.439  22.82   1 65.42  ? 519 ARG A NE    1 1 
ATOM   4142 C  CZ    . ARG A 1 519 ? 22.292  32.271  23.614  1 69.14  ? 519 ARG A CZ    1 1 
ATOM   4143 N  NH1   . ARG A 1 519 ? 23.539  31.988  23.984  1 68.98  ? 519 ARG A NH1   1 1 
ATOM   4144 N  NH2   . ARG A 1 519 ? 21.755  33.433  23.975  1 69.27  ? 519 ARG A NH2   1 1 
ATOM   4145 N  N     . VAL A 1 520 ? 19.617  29.802  26.633  1 46.71  ? 520 VAL A N     1 1 
ATOM   4146 C  CA    . VAL A 1 520 ? 20.025  30.333  27.933  1 46.93  ? 520 VAL A CA    1 1 
ATOM   4147 C  C     . VAL A 1 520 ? 18.8    30.8    28.753  1 46.92  ? 520 VAL A C     1 1 
ATOM   4148 O  O     . VAL A 1 520 ? 17.721  31.061  28.208  1 46.89  ? 520 VAL A O     1 1 
ATOM   4149 C  CB    . VAL A 1 520 ? 21.021  31.523  27.802  1 47.67  ? 520 VAL A CB    1 1 
ATOM   4150 C  CG1   . VAL A 1 520 ? 22.358  31.104  27.206  1 48.35  ? 520 VAL A CG1   1 1 
ATOM   4151 C  CG2   . VAL A 1 520 ? 20.395  32.685  27.036  1 48.03  ? 520 VAL A CG2   1 1 
ATOM   4152 N  N     . SER A 1 521 ? 18.992  30.909  30.074  1 46.67  ? 521 SER A N     1 1 
ATOM   4153 C  CA    . SER A 1 521 ? 18.065  31.511  31.024  1 46.93  ? 521 SER A CA    1 1 
ATOM   4154 C  C     . SER A 1 521 ? 18.845  32.705  31.673  1 46.88  ? 521 SER A C     1 1 
ATOM   4155 O  O     . SER A 1 521 ? 19.998  32.953  31.292  1 47.05  ? 521 SER A O     1 1 
ATOM   4156 C  CB    . SER A 1 521 ? 17.604  30.488  32.062  1 48.25  ? 521 SER A CB    1 1 
ATOM   4157 O  OG    . SER A 1 521 ? 18.61   30.203  33.019  1 50.25  ? 521 SER A OG    1 1 
ATOM   4158 N  N     . GLU A 1 522 ? 18.244  33.451  32.623  1 46.54  ? 522 GLU A N     1 1 
ATOM   4159 C  CA    . GLU A 1 522 ? 18.932  34.588  33.246  1 46.92  ? 522 GLU A CA    1 1 
ATOM   4160 C  C     . GLU A 1 522 ? 20.302  34.21   33.842  1 46.76  ? 522 GLU A C     1 1 
ATOM   4161 O  O     . GLU A 1 522 ? 21.306  34.899  33.615  1 46.83  ? 522 GLU A O     1 1 
ATOM   4162 C  CB    . GLU A 1 522 ? 18.046  35.262  34.302  1 49.67  ? 522 GLU A CB    1 1 
ATOM   4163 C  CG    . GLU A 1 522 ? 18.697  36.478  34.946  1 55.49  ? 522 GLU A CG    1 1 
ATOM   4164 C  CD    . GLU A 1 522 ? 17.835  37.722  35.011  1 63.82  ? 522 GLU A CD    1 1 
ATOM   4165 O  OE1   . GLU A 1 522 ? 16.643  37.648  34.63   1 65.98  ? 522 GLU A OE1   1 1 
ATOM   4166 O  OE2   . GLU A 1 522 ? 18.353  38.775  35.447  1 66.38  ? 522 GLU A OE2   1 1 
ATOM   4167 N  N     . ASN A 1 523 ? 20.348  33.078  34.542  1 46.17  ? 523 ASN A N     1 1 
ATOM   4168 C  CA    . ASN A 1 523 ? 21.583  32.62   35.167  1 45.94  ? 523 ASN A CA    1 1 
ATOM   4169 C  C     . ASN A 1 523 ? 22.123  31.28   34.645  1 45.38  ? 523 ASN A C     1 1 
ATOM   4170 O  O     . ASN A 1 523 ? 23.18   30.835  35.1    1 45.53  ? 523 ASN A O     1 1 
ATOM   4171 C  CB    . ASN A 1 523 ? 21.386  32.551  36.673  1 46.87  ? 523 ASN A CB    1 1 
ATOM   4172 C  CG    . ASN A 1 523 ? 20.979  33.873  37.252  1 49.36  ? 523 ASN A CG    1 1 
ATOM   4173 O  OD1   . ASN A 1 523 ? 19.83   34.076  37.665  1 50.47  ? 523 ASN A OD1   1 1 
ATOM   4174 N  ND2   . ASN A 1 523 ? 21.927  34.794  37.305  1 49.59  ? 523 ASN A ND2   1 1 
ATOM   4175 N  N     . GLY A 1 524 ? 21.414  30.65   33.714  1 44.48  ? 524 GLY A N     1 1 
ATOM   4176 C  CA    . GLY A 1 524 ? 21.822  29.352  33.204  1 43.92  ? 524 GLY A CA    1 1 
ATOM   4177 C  C     . GLY A 1 524 ? 22.1    29.243  31.722  1 42.93  ? 524 GLY A C     1 1 
ATOM   4178 O  O     . GLY A 1 524 ? 21.765  30.131  30.936  1 43.07  ? 524 GLY A O     1 1 
ATOM   4179 N  N     . LYS A 1 525 ? 22.734  28.126  31.351  1 41.7   ? 525 LYS A N     1 1 
ATOM   4180 C  CA    . LYS A 1 525 ? 23.077  27.749  29.987  1 40.81  ? 525 LYS A CA    1 1 
ATOM   4181 C  C     . LYS A 1 525 ? 22.57   26.323  29.757  1 39.98  ? 525 LYS A C     1 1 
ATOM   4182 O  O     . LYS A 1 525 ? 22.782  25.448  30.599  1 39.94  ? 525 LYS A O     1 1 
ATOM   4183 C  CB    . LYS A 1 525 ? 24.595  27.799  29.776  1 41.82  ? 525 LYS A CB    1 1 
ATOM   4184 C  CG    . LYS A 1 525 ? 25.128  29.198  29.539  1 45.04  ? 525 LYS A CG    1 1 
ATOM   4185 C  CD    . LYS A 1 525 ? 26.08   29.239  28.351  1 48.52  ? 525 LYS A CD    1 1 
ATOM   4186 C  CE    . LYS A 1 525 ? 26.773  30.568  28.169  1 51.17  ? 525 LYS A CE    1 1 
ATOM   4187 N  NZ    . LYS A 1 525 ? 28.087  30.612  28.869  1 52.58  ? 525 LYS A NZ    1 1 
ATOM   4188 N  N     . ARG A 1 526 ? 21.895  26.09   28.627  1 39.08  ? 526 ARG A N     1 1 
ATOM   4189 C  CA    . ARG A 1 526 ? 21.339  24.78   28.287  1 38.57  ? 526 ARG A CA    1 1 
ATOM   4190 C  C     . ARG A 1 526 ? 22.439  23.735  28.119  1 38.73  ? 526 ARG A C     1 1 
ATOM   4191 O  O     . ARG A 1 526 ? 23.33   23.906  27.287  1 38.85  ? 526 ARG A O     1 1 
ATOM   4192 C  CB    . ARG A 1 526 ? 20.498  24.889  27.009  1 38.69  ? 526 ARG A CB    1 1 
ATOM   4193 C  CG    . ARG A 1 526 ? 19.886  23.596  26.558  1 39.91  ? 526 ARG A CG    1 1 
ATOM   4194 C  CD    . ARG A 1 526 ? 19.062  23.813  25.312  1 41.69  ? 526 ARG A CD    1 1 
ATOM   4195 N  NE    . ARG A 1 526 ? 19.894  24.09   24.141  1 43.11  ? 526 ARG A NE    1 1 
ATOM   4196 C  CZ    . ARG A 1 526 ? 19.466  24.721  23.048  1 44.77  ? 526 ARG A CZ    1 1 
ATOM   4197 N  NH1   . ARG A 1 526 ? 18.222  25.178  22.981  1 44.41  ? 526 ARG A NH1   1 1 
ATOM   4198 N  NH2   . ARG A 1 526 ? 20.285  24.92   22.026  1 44.47  ? 526 ARG A NH2   1 1 
ATOM   4199 N  N     . PRO A 1 527 ? 22.414  22.653  28.92   1 38.57  ? 527 PRO A N     1 1 
ATOM   4200 C  CA    . PRO A 1 527 ? 23.46   21.627  28.789  1 38.5   ? 527 PRO A CA    1 1 
ATOM   4201 C  C     . PRO A 1 527 ? 23.403  20.871  27.472  1 38.46  ? 527 PRO A C     1 1 
ATOM   4202 O  O     . PRO A 1 527 ? 22.358  20.83   26.819  1 38.51  ? 527 PRO A O     1 1 
ATOM   4203 C  CB    . PRO A 1 527 ? 23.197  20.684  29.975  1 39.09  ? 527 PRO A CB    1 1 
ATOM   4204 C  CG    . PRO A 1 527 ? 22.22   21.403  30.867  1 39.37  ? 527 PRO A CG    1 1 
ATOM   4205 C  CD    . PRO A 1 527 ? 21.44   22.301  29.968  1 37.97  ? 527 PRO A CD    1 1 
ATOM   4206 N  N     . ASP A 1 528 ? 24.538  20.3    27.063  1 38.26  ? 528 ASP A N     1 1 
ATOM   4207 C  CA    . ASP A 1 528 ? 24.57   19.487  25.856  1 38.74  ? 528 ASP A CA    1 1 
ATOM   4208 C  C     . ASP A 1 528 ? 23.813  18.194  26.14   1 39.11  ? 528 ASP A C     1 1 
ATOM   4209 O  O     . ASP A 1 528 ? 22.988  17.769  25.327  1 39.25  ? 528 ASP A O     1 1 
ATOM   4210 C  CB    . ASP A 1 528 ? 26.009  19.175  25.429  1 40.15  ? 528 ASP A CB    1 1 
ATOM   4211 C  CG    . ASP A 1 528 ? 26.754  20.336  24.819  1 45.13  ? 528 ASP A CG    1 1 
ATOM   4212 O  OD1   . ASP A 1 528 ? 26.116  21.377  24.546  1 45.4   ? 528 ASP A OD1   1 1 
ATOM   4213 O  OD2   . ASP A 1 528 ? 27.979  20.206  24.606  1 48.26  ? 528 ASP A OD2   1 1 
ATOM   4214 N  N     . HIS A 1 529 ? 24.069  17.592  27.319  1 38.96  ? 529 HIS A N     1 1 
ATOM   4215 C  CA    . HIS A 1 529 ? 23.437  16.358  27.752  1 39.2   ? 529 HIS A CA    1 1 
ATOM   4216 C  C     . HIS A 1 529 ? 23.134  16.392  29.238  1 38.69  ? 529 HIS A C     1 1 
ATOM   4217 O  O     . HIS A 1 529 ? 23.877  16.977  30.012  1 38.76  ? 529 HIS A O     1 1 
ATOM   4218 C  CB    . HIS A 1 529 ? 24.362  15.162  27.462  1 40.27  ? 529 HIS A CB    1 1 
ATOM   4219 C  CG    . HIS A 1 529 ? 24.761  15.052  26.026  1 42.55  ? 529 HIS A CG    1 1 
ATOM   4220 N  ND1   . HIS A 1 529 ? 23.879  14.583  25.072  1 44.5   ? 529 HIS A ND1   1 1 
ATOM   4221 C  CD2   . HIS A 1 529 ? 25.923  15.389  25.423  1 43.59  ? 529 HIS A CD2   1 1 
ATOM   4222 C  CE1   . HIS A 1 529 ? 24.53   14.647  23.922  1 44.91  ? 529 HIS A CE1   1 1 
ATOM   4223 N  NE2   . HIS A 1 529 ? 25.763  15.126  24.084  1 44.73  ? 529 HIS A NE2   1 1 
ATOM   4224 N  N     . VAL A 1 530 ? 22.049  15.757  29.638  1 37.99  ? 530 VAL A N     1 1 
ATOM   4225 C  CA    . VAL A 1 530 ? 21.702  15.614  31.039  1 38.05  ? 530 VAL A CA    1 1 
ATOM   4226 C  C     . VAL A 1 530 ? 21.518  14.125  31.244  1 38.51  ? 530 VAL A C     1 1 
ATOM   4227 O  O     . VAL A 1 530 ? 20.79   13.48   30.494  1 38.75  ? 530 VAL A O     1 1 
ATOM   4228 C  CB    . VAL A 1 530 ? 20.47   16.425  31.468  1 38.35  ? 530 VAL A CB    1 1 
ATOM   4229 C  CG1   . VAL A 1 530 ? 20.204  16.242  32.956  1 38.8   ? 530 VAL A CG1   1 1 
ATOM   4230 C  CG2   . VAL A 1 530 ? 20.651  17.895  31.136  1 38.73  ? 530 VAL A CG2   1 1 
ATOM   4231 N  N     . ILE A 1 531 ? 22.249  13.556  32.192  1 38.58  ? 531 ILE A N     1 1 
ATOM   4232 C  CA    . ILE A 1 531 ? 22.222  12.116  32.428  1 38.91  ? 531 ILE A CA    1 1 
ATOM   4233 C  C     . ILE A 1 531 ? 21.556  11.825  33.756  1 39.25  ? 531 ILE A C     1 1 
ATOM   4234 O  O     . ILE A 1 531 ? 21.901  12.459  34.749  1 39.24  ? 531 ILE A O     1 1 
ATOM   4235 C  CB    . ILE A 1 531 ? 23.673  11.551  32.386  1 39.19  ? 531 ILE A CB    1 1 
ATOM   4236 C  CG1   . ILE A 1 531 ? 24.427  11.999  31.124  1 39.92  ? 531 ILE A CG1   1 1 
ATOM   4237 C  CG2   . ILE A 1 531 ? 23.692  10.041  32.514  1 39.73  ? 531 ILE A CG2   1 1 
ATOM   4238 C  CD1   . ILE A 1 531 ? 23.762  11.602  29.817  1 41.11  ? 531 ILE A CD1   1 1 
ATOM   4239 N  N     . GLN A 1 532 ? 20.604  10.885  33.786  1 39.41  ? 532 GLN A N     1 1 
ATOM   4240 C  CA    . GLN A 1 532 ? 19.97   10.531  35.044  1 40.24  ? 532 GLN A CA    1 1 
ATOM   4241 C  C     . GLN A 1 532 ? 20.505  9.217   35.533  1 41.15  ? 532 GLN A C     1 1 
ATOM   4242 O  O     . GLN A 1 532 ? 20.552  8.25    34.778  1 41.13  ? 532 GLN A O     1 1 
ATOM   4243 C  CB    . GLN A 1 532 ? 18.448  10.5    34.945  1 41.64  ? 532 GLN A CB    1 1 
ATOM   4244 C  CG    . GLN A 1 532 ? 17.782  10.406  36.316  1 44.19  ? 532 GLN A CG    1 1 
ATOM   4245 C  CD    . GLN A 1 532 ? 16.277  10.529  36.267  1 47.23  ? 532 GLN A CD    1 1 
ATOM   4246 O  OE1   . GLN A 1 532 ? 15.656  10.615  35.194  1 48     ? 532 GLN A OE1   1 1 
ATOM   4247 N  NE2   . GLN A 1 532 ? 15.651  10.533  37.44   1 47.56  ? 532 GLN A NE2   1 1 
ATOM   4248 N  N     . ILE A 1 533 ? 20.966  9.195   36.785  1 41.93  ? 533 ILE A N     1 1 
ATOM   4249 C  CA    . ILE A 1 533 ? 21.483  7.989   37.427  1 43.24  ? 533 ILE A CA    1 1 
ATOM   4250 C  C     . ILE A 1 533 ? 20.664  7.755   38.698  1 44.79  ? 533 ILE A C     1 1 
ATOM   4251 O  O     . ILE A 1 533 ? 20.653  8.603   39.589  1 44.84  ? 533 ILE A O     1 1 
ATOM   4252 C  CB    . ILE A 1 533 ? 23.007  8.081   37.689  1 43.36  ? 533 ILE A CB    1 1 
ATOM   4253 C  CG1   . ILE A 1 533 ? 23.768  8.123   36.364  1 44.15  ? 533 ILE A CG1   1 1 
ATOM   4254 C  CG2   . ILE A 1 533 ? 23.473  6.903   38.523  1 43.75  ? 533 ILE A CG2   1 1 
ATOM   4255 C  CD1   . ILE A 1 533 ? 25.141  8.526   36.483  1 45.54  ? 533 ILE A CD1   1 1 
ATOM   4256 N  N     . LEU A 1 534 ? 19.935  6.635   38.761  1 45.75  ? 534 LEU A N     1 1 
ATOM   4257 C  CA    . LEU A 1 534 ? 19.043  6.379   39.887  1 47.11  ? 534 LEU A CA    1 1 
ATOM   4258 C  C     . LEU A 1 534 ? 19.577  5.406   40.921  1 48.4   ? 534 LEU A C     1 1 
ATOM   4259 O  O     . LEU A 1 534 ? 19.104  5.416   42.059  1 48.44  ? 534 LEU A O     1 1 
ATOM   4260 C  CB    . LEU A 1 534 ? 17.679  5.91    39.371  1 47.27  ? 534 LEU A CB    1 1 
ATOM   4261 C  CG    . LEU A 1 534 ? 16.928  6.908   38.496  1 48.57  ? 534 LEU A CG    1 1 
ATOM   4262 C  CD1   . LEU A 1 534 ? 16.881  6.453   37.047  1 48.86  ? 534 LEU A CD1   1 1 
ATOM   4263 C  CD2   . LEU A 1 534 ? 15.528  7.122   39.013  1 49.37  ? 534 LEU A CD2   1 1 
ATOM   4264 N  N     . ASP A 1 535 ? 20.525  4.541   40.532  1 49.22  ? 535 ASP A N     1 1 
ATOM   4265 C  CA    . ASP A 1 535 ? 21.057  3.543   41.455  1 50.62  ? 535 ASP A CA    1 1 
ATOM   4266 C  C     . ASP A 1 535 ? 22.453  3.877   41.998  1 51.1   ? 535 ASP A C     1 1 
ATOM   4267 O  O     . ASP A 1 535 ? 23.289  2.98    42.151  1 51.29  ? 535 ASP A O     1 1 
ATOM   4268 C  CB    . ASP A 1 535 ? 21.031  2.139   40.83   1 53.47  ? 535 ASP A CB    1 1 
ATOM   4269 C  CG    . ASP A 1 535 ? 19.702  1.416   40.976  1 60.42  ? 535 ASP A CG    1 1 
ATOM   4270 O  OD1   . ASP A 1 535 ? 18.658  2.104   41.085  1 61.65  ? 535 ASP A OD1   1 1 
ATOM   4271 O  OD2   . ASP A 1 535 ? 19.703  0.157   40.98   1 63.35  ? 535 ASP A OD2   1 1 
ATOM   4272 N  N     . LEU A 1 536 ? 22.696  5.154   42.322  1 50.99  ? 536 LEU A N     1 1 
ATOM   4273 C  CA    . LEU A 1 536 ? 23.979  5.562   42.884  1 51.39  ? 536 LEU A CA    1 1 
ATOM   4274 C  C     . LEU A 1 536 ? 23.771  6.154   44.273  1 52.17  ? 536 LEU A C     1 1 
ATOM   4275 O  O     . LEU A 1 536 ? 24.32   5.641   45.247  1 52.34  ? 536 LEU A O     1 1 
ATOM   4276 C  CB    . LEU A 1 536 ? 24.713  6.533   41.948  1 51.31  ? 536 LEU A CB    1 1 
ATOM   4277 C  CG    . LEU A 1 536 ? 26.025  7.119   42.45   1 52.63  ? 536 LEU A CG    1 1 
ATOM   4278 C  CD1   . LEU A 1 536 ? 27.01   6.031   42.861  1 53.29  ? 536 LEU A CD1   1 1 
ATOM   4279 C  CD2   . LEU A 1 536 ? 26.66   7.978   41.387  1 53.18  ? 536 LEU A CD2   1 1 
ATOM   4280 N  N     . PHE A 1 537 ? 22.947  7.2     44.375  1 52.55  ? 537 PHE A N     1 1 
ATOM   4281 C  CA    . PHE A 1 537 ? 22.623  7.827   45.653  1 53.37  ? 537 PHE A CA    1 1 
ATOM   4282 C  C     . PHE A 1 537 ? 21.155  7.544   46.012  1 53.48  ? 537 PHE A C     1 1 
ATOM   4283 O  O     . PHE A 1 537 ? 20.405  7.067   45.153  1 53.7   ? 537 PHE A O     1 1 
ATOM   4284 C  CB    . PHE A 1 537 ? 22.857  9.341   45.565  1 53.71  ? 537 PHE A CB    1 1 
ATOM   4285 C  CG    . PHE A 1 537 ? 24.236  9.741   45.101  1 54.85  ? 537 PHE A CG    1 1 
ATOM   4286 C  CD1   . PHE A 1 537 ? 25.341  9.547   45.91   1 55.93  ? 537 PHE A CD1   1 1 
ATOM   4287 C  CD2   . PHE A 1 537 ? 24.418  10.365  43.88   1 55.79  ? 537 PHE A CD2   1 1 
ATOM   4288 C  CE1   . PHE A 1 537 ? 26.609  9.931   45.486  1 56.77  ? 537 PHE A CE1   1 1 
ATOM   4289 C  CE2   . PHE A 1 537 ? 25.683  10.762  43.466  1 56.59  ? 537 PHE A CE2   1 1 
ATOM   4290 C  CZ    . PHE A 1 537 ? 26.772  10.537  44.268  1 56.53  ? 537 PHE A CZ    1 1 
ATOM   4291 N  N     . GLU A 1 538 ? 20.728  7.846   47.264  1 53.16  ? 538 GLU A N     1 1 
ATOM   4292 C  CA    . GLU A 1 538 ? 19.322  7.64    47.632  1 53.27  ? 538 GLU A CA    1 1 
ATOM   4293 C  C     . GLU A 1 538 ? 18.395  8.527   46.769  1 52.46  ? 538 GLU A C     1 1 
ATOM   4294 O  O     . GLU A 1 538 ? 17.299  8.102   46.411  1 52.51  ? 538 GLU A O     1 1 
ATOM   4295 C  CB    . GLU A 1 538 ? 19.078  7.78    49.151  1 56.25  ? 538 GLU A CB    1 1 
ATOM   4296 C  CG    . GLU A 1 538 ? 18.891  9.196   49.668  1 62.68  ? 538 GLU A CG    1 1 
ATOM   4297 C  CD    . GLU A 1 538 ? 17.68   9.405   50.567  1 70.86  ? 538 GLU A CD    1 1 
ATOM   4298 O  OE1   . GLU A 1 538 ? 17.005  8.403   50.905  1 72.05  ? 538 GLU A OE1   1 1 
ATOM   4299 O  OE2   . GLU A 1 538 ? 17.403  10.574  50.928  1 73.58  ? 538 GLU A OE2   1 1 
ATOM   4300 N  N     . LYS A 1 539 ? 18.884  9.708   46.35   1 51.53  ? 539 LYS A N     1 1 
ATOM   4301 C  CA    . LYS A 1 539 ? 18.171  10.613  45.453  1 50.99  ? 539 LYS A CA    1 1 
ATOM   4302 C  C     . LYS A 1 539 ? 18.715  10.408  44.02   1 50.04  ? 539 LYS A C     1 1 
ATOM   4303 O  O     . LYS A 1 539 ? 19.902  10.091  43.841  1 50.22  ? 539 LYS A O     1 1 
ATOM   4304 C  CB    . LYS A 1 539 ? 18.412  12.08   45.873  1 52.46  ? 539 LYS A CB    1 1 
ATOM   4305 C  CG    . LYS A 1 539 ? 18.012  12.42   47.3    1 55.59  ? 539 LYS A CG    1 1 
ATOM   4306 C  CD    . LYS A 1 539 ? 18.448  13.834  47.63   1 59.65  ? 539 LYS A CD    1 1 
ATOM   4307 C  CE    . LYS A 1 539 ? 18.088  14.267  49.03   1 63.3   ? 539 LYS A CE    1 1 
ATOM   4308 N  NZ    . LYS A 1 539 ? 18.388  15.715  49.256  1 65.3   ? 539 LYS A NZ    1 1 
ATOM   4309 N  N     . PRO A 1 540 ? 17.878  10.614  42.984  1 48.7   ? 540 PRO A N     1 1 
ATOM   4310 C  CA    . PRO A 1 540 ? 18.385  10.489  41.608  1 47.75  ? 540 PRO A CA    1 1 
ATOM   4311 C  C     . PRO A 1 540 ? 19.399  11.587  41.291  1 46.51  ? 540 PRO A C     1 1 
ATOM   4312 O  O     . PRO A 1 540 ? 19.266  12.713  41.765  1 46.64  ? 540 PRO A O     1 1 
ATOM   4313 C  CB    . PRO A 1 540 ? 17.13   10.65   40.737  1 48.63  ? 540 PRO A CB    1 1 
ATOM   4314 C  CG    . PRO A 1 540 ? 15.972  10.588  41.658  1 49.28  ? 540 PRO A CG    1 1 
ATOM   4315 C  CD    . PRO A 1 540 ? 16.457  10.998  43.008  1 47.93  ? 540 PRO A CD    1 1 
ATOM   4316 N  N     . LEU A 1 541 ? 20.416  11.258  40.505  1 45.06  ? 541 LEU A N     1 1 
ATOM   4317 C  CA    . LEU A 1 541 ? 21.439  12.22   40.114  1 44.12  ? 541 LEU A CA    1 1 
ATOM   4318 C  C     . LEU A 1 541 ? 21.142  12.723  38.713  1 43.12  ? 541 LEU A C     1 1 
ATOM   4319 O  O     . LEU A 1 541 ? 20.864  11.931  37.823  1 43.36  ? 541 LEU A O     1 1 
ATOM   4320 C  CB    . LEU A 1 541 ? 22.835  11.554  40.141  1 44.11  ? 541 LEU A CB    1 1 
ATOM   4321 C  CG    . LEU A 1 541 ? 23.955  12.242  39.354  1 45.28  ? 541 LEU A CG    1 1 
ATOM   4322 C  CD1   . LEU A 1 541 ? 24.432  13.463  40.058  1 45.81  ? 541 LEU A CD1   1 1 
ATOM   4323 C  CD2   . LEU A 1 541 ? 25.072  11.296  39.051  1 45.87  ? 541 LEU A CD2   1 1 
ATOM   4324 N  N     . LEU A 1 542 ? 21.277  14.02   38.506  1 42.02  ? 542 LEU A N     1 1 
ATOM   4325 C  CA    . LEU A 1 542 ? 21.14   14.614  37.198  1 41.59  ? 542 LEU A CA    1 1 
ATOM   4326 C  C     . LEU A 1 542 ? 22.488  15.241  36.905  1 41.67  ? 542 LEU A C     1 1 
ATOM   4327 O  O     . LEU A 1 542 ? 22.915  16.148  37.613  1 42.17  ? 542 LEU A O     1 1 
ATOM   4328 C  CB    . LEU A 1 542 ? 20.04   15.664  37.214  1 41.49  ? 542 LEU A CB    1 1 
ATOM   4329 C  CG    . LEU A 1 542 ? 18.669  15.117  37.538  1 42.86  ? 542 LEU A CG    1 1 
ATOM   4330 C  CD1   . LEU A 1 542 ? 17.678  16.226  37.731  1 43.64  ? 542 LEU A CD1   1 1 
ATOM   4331 C  CD2   . LEU A 1 542 ? 18.193  14.179  36.458  1 43.52  ? 542 LEU A CD2   1 1 
ATOM   4332 N  N     . LEU A 1 543 ? 23.202  14.703  35.923  1 40.99  ? 543 LEU A N     1 1 
ATOM   4333 C  CA    . LEU A 1 543 ? 24.526  15.183  35.546  1 40.56  ? 543 LEU A CA    1 1 
ATOM   4334 C  C     . LEU A 1 543 ? 24.45   15.996  34.251  1 40.6   ? 543 LEU A C     1 1 
ATOM   4335 O  O     . LEU A 1 543 ? 24.239  15.431  33.18   1 40.86  ? 543 LEU A O     1 1 
ATOM   4336 C  CB    . LEU A 1 543 ? 25.457  13.987  35.349  1 40.32  ? 543 LEU A CB    1 1 
ATOM   4337 C  CG    . LEU A 1 543 ? 26.859  14.307  34.877  1 41.27  ? 543 LEU A CG    1 1 
ATOM   4338 C  CD1   . LEU A 1 543 ? 27.634  15.046  35.943  1 41.67  ? 543 LEU A CD1   1 1 
ATOM   4339 C  CD2   . LEU A 1 543 ? 27.58   13.051  34.472  1 41.69  ? 543 LEU A CD2   1 1 
ATOM   4340 N  N     . SER A 1 544 ? 24.628  17.315  34.341  1 40.11  ? 544 SER A N     1 1 
ATOM   4341 C  CA    . SER A 1 544 ? 24.596  18.179  33.169  1 40.27  ? 544 SER A CA    1 1 
ATOM   4342 C  C     . SER A 1 544 ? 25.995  18.323  32.568  1 40.46  ? 544 SER A C     1 1 
ATOM   4343 O  O     . SER A 1 544 ? 26.932  18.709  33.258  1 40.64  ? 544 SER A O     1 1 
ATOM   4344 C  CB    . SER A 1 544 ? 24.039  19.538  33.547  1 41.56  ? 544 SER A CB    1 1 
ATOM   4345 O  OG    . SER A 1 544 ? 22.723  19.366  34.037  1 43.97  ? 544 SER A OG    1 1 
ATOM   4346 N  N     . ILE A 1 545 ? 26.14   18.016  31.28   1 39.97  ? 545 ILE A N     1 1 
ATOM   4347 C  CA    . ILE A 1 545 ? 27.441  18.019  30.623  1 39.61  ? 545 ILE A CA    1 1 
ATOM   4348 C  C     . ILE A 1 545 ? 27.537  18.992  29.462  1 39.38  ? 545 ILE A C     1 1 
ATOM   4349 O  O     . ILE A 1 545 ? 26.617  19.114  28.665  1 39.35  ? 545 ILE A O     1 1 
ATOM   4350 C  CB    . ILE A 1 545 ? 27.771  16.582  30.12   1 39.95  ? 545 ILE A CB    1 1 
ATOM   4351 C  CG1   . ILE A 1 545 ? 27.479  15.487  31.163  1 40.72  ? 545 ILE A CG1   1 1 
ATOM   4352 C  CG2   . ILE A 1 545 ? 29.2    16.484  29.61   1 40.5   ? 545 ILE A CG2   1 1 
ATOM   4353 C  CD1   . ILE A 1 545 ? 27.508  14.103  30.59   1 41.95  ? 545 ILE A CD1   1 1 
ATOM   4354 N  N     . VAL A 1 546 ? 28.68   19.645  29.339  1 39.44  ? 546 VAL A N     1 1 
ATOM   4355 C  CA    . VAL A 1 546 ? 28.999  20.502  28.212  1 40.25  ? 546 VAL A CA    1 1 
ATOM   4356 C  C     . VAL A 1 546 ? 30.285  19.942  27.576  1 40.77  ? 546 VAL A C     1 1 
ATOM   4357 O  O     . VAL A 1 546 ? 31.214  19.536  28.285  1 40.77  ? 546 VAL A O     1 1 
ATOM   4358 C  CB    . VAL A 1 546 ? 29.128  21.996  28.599  1 41.37  ? 546 VAL A CB    1 1 
ATOM   4359 C  CG1   . VAL A 1 546 ? 30.136  22.191  29.727  1 42.27  ? 546 VAL A CG1   1 1 
ATOM   4360 C  CG2   . VAL A 1 546 ? 29.493  22.852  27.389  1 41.95  ? 546 VAL A CG2   1 1 
ATOM   4361 N  N     . SER A 1 547 ? 30.312  19.854  26.248  1 41.02  ? 547 SER A N     1 1 
ATOM   4362 C  CA    . SER A 1 547 ? 31.478  19.341  25.547  1 41.84  ? 547 SER A CA    1 1 
ATOM   4363 C  C     . SER A 1 547 ? 32.094  20.433  24.685  1 42.08  ? 547 SER A C     1 1 
ATOM   4364 O  O     . SER A 1 547 ? 31.384  21.19   24.018  1 42.47  ? 547 SER A O     1 1 
ATOM   4365 C  CB    . SER A 1 547 ? 31.102  18.138  24.693  1 43.93  ? 547 SER A CB    1 1 
ATOM   4366 O  OG    . SER A 1 547 ? 30.068  18.47   23.78   1 47.53  ? 547 SER A OG    1 1 
ATOM   4367 N  N     . LYS A 1 548 ? 33.418  20.542  24.741  1 41.61  ? 548 LYS A N     1 1 
ATOM   4368 C  CA    . LYS A 1 548 ? 34.193  21.502  23.966  1 41.7   ? 548 LYS A CA    1 1 
ATOM   4369 C  C     . LYS A 1 548 ? 35.421  20.802  23.356  1 41.67  ? 548 LYS A C     1 1 
ATOM   4370 O  O     . LYS A 1 548 ? 35.77   19.695  23.759  1 41.56  ? 548 LYS A O     1 1 
ATOM   4371 C  CB    . LYS A 1 548 ? 34.631  22.68   24.854  1 43.42  ? 548 LYS A CB    1 1 
ATOM   4372 C  CG    . LYS A 1 548 ? 33.477  23.513  25.4    1 47.34  ? 548 LYS A CG    1 1 
ATOM   4373 C  CD    . LYS A 1 548 ? 32.696  24.233  24.301  1 51.15  ? 548 LYS A CD    1 1 
ATOM   4374 C  CE    . LYS A 1 548 ? 31.405  24.833  24.806  1 53.71  ? 548 LYS A CE    1 1 
ATOM   4375 N  NZ    . LYS A 1 548 ? 31.634  25.876  25.842  1 55.13  ? 548 LYS A NZ    1 1 
ATOM   4376 N  N     . GLU A 1 549 ? 36.068  21.439  22.377  1 41.59  ? 549 GLU A N     1 1 
ATOM   4377 C  CA    . GLU A 1 549 ? 37.252  20.878  21.742  1 41.93  ? 549 GLU A CA    1 1 
ATOM   4378 C  C     . GLU A 1 549 ? 38.458  20.961  22.695  1 42.38  ? 549 GLU A C     1 1 
ATOM   4379 O  O     . GLU A 1 549 ? 39.141  19.961  22.91   1 42.4   ? 549 GLU A O     1 1 
ATOM   4380 C  CB    . GLU A 1 549 ? 37.536  21.613  20.417  1 43.64  ? 549 GLU A CB    1 1 
ATOM   4381 C  CG    . GLU A 1 549 ? 38.824  21.192  19.726  1 46.68  ? 549 GLU A CG    1 1 
ATOM   4382 C  CD    . GLU A 1 549 ? 39.089  21.851  18.386  1 49.54  ? 549 GLU A CD    1 1 
ATOM   4383 O  OE1   . GLU A 1 549 ? 38.285  22.719  17.974  1 50.72  ? 549 GLU A OE1   1 1 
ATOM   4384 O  OE2   . GLU A 1 549 ? 40.101  21.494  17.743  1 49.42  ? 549 GLU A OE2   1 1 
ATOM   4385 N  N     . LYS A 1 550 ? 38.696  22.142  23.283  1 42.58  ? 550 LYS A N     1 1 
ATOM   4386 C  CA    . LYS A 1 550 ? 39.813  22.382  24.192  1 43.33  ? 550 LYS A CA    1 1 
ATOM   4387 C  C     . LYS A 1 550 ? 39.322  22.765  25.587  1 44.08  ? 550 LYS A C     1 1 
ATOM   4388 O  O     . LYS A 1 550 ? 38.242  23.334  25.718  1 44.24  ? 550 LYS A O     1 1 
ATOM   4389 C  CB    . LYS A 1 550 ? 40.691  23.513  23.63   1 45.32  ? 550 LYS A CB    1 1 
ATOM   4390 C  CG    . LYS A 1 550 ? 41.249  23.235  22.239  1 49.07  ? 550 LYS A CG    1 1 
ATOM   4391 C  CD    . LYS A 1 550 ? 41.935  24.468  21.652  1 51.76  ? 550 LYS A CD    1 1 
ATOM   4392 C  CE    . LYS A 1 550 ? 42.36   24.267  20.217  1 53.56  ? 550 LYS A CE    1 1 
ATOM   4393 N  NZ    . LYS A 1 550 ? 43.279  23.115  20.076  1 54.48  ? 550 LYS A NZ    1 1 
ATOM   4394 N  N     . PRO A 1 551 ? 40.118  22.517  26.641  1 44.72  ? 551 PRO A N     1 1 
ATOM   4395 C  CA    . PRO A 1 551 ? 39.675  22.887  27.994  1 45.68  ? 551 PRO A CA    1 1 
ATOM   4396 C  C     . PRO A 1 551 ? 39.465  24.387  28.185  1 47.41  ? 551 PRO A C     1 1 
ATOM   4397 O  O     . PRO A 1 551 ? 38.59   24.78   28.951  1 47.71  ? 551 PRO A O     1 1 
ATOM   4398 C  CB    . PRO A 1 551 ? 40.787  22.346  28.899  1 46.17  ? 551 PRO A CB    1 1 
ATOM   4399 C  CG    . PRO A 1 551 ? 41.974  22.192  28.015  1 46.31  ? 551 PRO A CG    1 1 
ATOM   4400 C  CD    . PRO A 1 551 ? 41.433  21.851  26.664  1 44.45  ? 551 PRO A CD    1 1 
ATOM   4401 N  N     . ASN A 1 552 ? 40.233  25.231  27.47   1 48.37  ? 552 ASN A N     1 1 
ATOM   4402 C  CA    . ASN A 1 552 ? 40.064  26.685  27.573  1 49.65  ? 552 ASN A CA    1 1 
ATOM   4403 C  C     . ASN A 1 552 ? 38.798  27.205  26.836  1 50.54  ? 552 ASN A C     1 1 
ATOM   4404 O  O     . ASN A 1 552 ? 38.43   28.368  26.998  1 50.74  ? 552 ASN A O     1 1 
ATOM   4405 C  CB    . ASN A 1 552 ? 41.326  27.475  27.174  1 51.27  ? 552 ASN A CB    1 1 
ATOM   4406 C  CG    . ASN A 1 552 ? 42.237  26.884  26.108  1 55.25  ? 552 ASN A CG    1 1 
ATOM   4407 O  OD1   . ASN A 1 552 ? 42.52   25.673  26.054  1 56.29  ? 552 ASN A OD1   1 1 
ATOM   4408 N  ND2   . ASN A 1 552 ? 42.774  27.762  25.265  1 56.2   ? 552 ASN A ND2   1 1 
ATOM   4409 N  N     . ASP A 1 553 ? 38.118  26.347  26.065  1 50.87  ? 553 ASP A N     1 1 
ATOM   4410 C  CA    . ASP A 1 553 ? 36.866  26.714  25.416  1 51.68  ? 553 ASP A CA    1 1 
ATOM   4411 C  C     . ASP A 1 553 ? 35.691  26.715  26.421  1 52.46  ? 553 ASP A C     1 1 
ATOM   4412 O  O     . ASP A 1 553 ? 34.644  27.303  26.132  1 52.63  ? 553 ASP A O     1 1 
ATOM   4413 C  CB    . ASP A 1 553 ? 36.569  25.773  24.247  1 53.41  ? 553 ASP A CB    1 1 
ATOM   4414 C  CG    . ASP A 1 553 ? 37.619  25.811  23.162  1 58.12  ? 553 ASP A CG    1 1 
ATOM   4415 O  OD1   . ASP A 1 553 ? 38.273  26.867  23.006  1 59     ? 553 ASP A OD1   1 1 
ATOM   4416 O  OD2   . ASP A 1 553 ? 37.787  24.787  22.466  1 60.25  ? 553 ASP A OD2   1 1 
ATOM   4417 N  N     . LEU A 1 554 ? 35.857  26.05   27.589  1 52.73  ? 554 LEU A N     1 1 
ATOM   4418 C  CA    . LEU A 1 554 ? 34.859  26.009  28.649  1 53.45  ? 554 LEU A CA    1 1 
ATOM   4419 C  C     . LEU A 1 554 ? 34.8    27.399  29.275  1 54.41  ? 554 LEU A C     1 1 
ATOM   4420 O  O     . LEU A 1 554 ? 35.724  27.797  29.987  1 54.63  ? 554 LEU A O     1 1 
ATOM   4421 C  CB    . LEU A 1 554 ? 35.261  24.97   29.702  1 53.4   ? 554 LEU A CB    1 1 
ATOM   4422 C  CG    . LEU A 1 554 ? 35.192  23.513  29.272  1 54.29  ? 554 LEU A CG    1 1 
ATOM   4423 C  CD1   . LEU A 1 554 ? 35.837  22.622  30.31   1 54.72  ? 554 LEU A CD1   1 1 
ATOM   4424 C  CD2   . LEU A 1 554 ? 33.762  23.086  29.051  1 54.74  ? 554 LEU A CD2   1 1 
ATOM   4425 N  N     . GLU A 1 555 ? 33.739  28.152  28.959  1 54.82  ? 555 GLU A N     1 1 
ATOM   4426 C  CA    . GLU A 1 555 ? 33.537  29.532  29.41   1 55.83  ? 555 GLU A CA    1 1 
ATOM   4427 C  C     . GLU A 1 555 ? 33.475  29.69   30.933  1 55.5   ? 555 GLU A C     1 1 
ATOM   4428 O  O     . GLU A 1 555 ? 33.107  28.754  31.642  1 55.8   ? 555 GLU A O     1 1 
ATOM   4429 C  CB    . GLU A 1 555 ? 32.292  30.169  28.739  1 59.64  ? 555 GLU A CB    1 1 
ATOM   4430 C  CG    . GLU A 1 555 ? 31.212  29.197  28.295  1 67.83  ? 555 GLU A CG    1 1 
ATOM   4431 C  CD    . GLU A 1 555 ? 30.807  29.383  26.846  1 77.55  ? 555 GLU A CD    1 1 
ATOM   4432 O  OE1   . GLU A 1 555 ? 30.481  28.37   26.183  1 79.87  ? 555 GLU A OE1   1 1 
ATOM   4433 O  OE2   . GLU A 1 555 ? 30.834  30.543  26.369  1 80.13  ? 555 GLU A OE2   1 1 
ATOM   4434 N  N     . PRO A 1 556 ? 33.829  30.88   31.461  1 54.59  ? 556 PRO A N     1 1 
ATOM   4435 C  CA    . PRO A 1 556 ? 33.76   31.086  32.914  1 53.67  ? 556 PRO A CA    1 1 
ATOM   4436 C  C     . PRO A 1 556 ? 32.381  30.785  33.489  1 52.3   ? 556 PRO A C     1 1 
ATOM   4437 O  O     . PRO A 1 556 ? 31.361  31.107  32.872  1 52.29  ? 556 PRO A O     1 1 
ATOM   4438 C  CB    . PRO A 1 556 ? 34.104  32.569  33.077  1 54.64  ? 556 PRO A CB    1 1 
ATOM   4439 C  CG    . PRO A 1 556 ? 34.89   32.907  31.872  1 55.44  ? 556 PRO A CG    1 1 
ATOM   4440 C  CD    . PRO A 1 556 ? 34.3    32.092  30.768  1 54.05  ? 556 PRO A CD    1 1 
ATOM   4441 N  N     . LYS A 1 557 ? 32.369  30.092  34.631  1 50.9   ? 557 LYS A N     1 1 
ATOM   4442 C  CA    . LYS A 1 557 ? 31.176  29.697  35.362  1 50.09  ? 557 LYS A CA    1 1 
ATOM   4443 C  C     . LYS A 1 557 ? 30.24   28.773  34.579  1 48.98  ? 557 LYS A C     1 1 
ATOM   4444 O  O     . LYS A 1 557 ? 29.074  28.697  34.945  1 48.99  ? 557 LYS A O     1 1 
ATOM   4445 C  CB    . LYS A 1 557 ? 30.4    30.929  35.86   1 51.53  ? 557 LYS A CB    1 1 
ATOM   4446 C  CG    . LYS A 1 557 ? 31.146  31.812  36.851  1 55     ? 557 LYS A CG    1 1 
ATOM   4447 C  CD    . LYS A 1 557 ? 30.625  33.266  36.805  1 59.29  ? 557 LYS A CD    1 1 
ATOM   4448 C  CE    . LYS A 1 557 ? 29.133  33.404  37.063  1 62.64  ? 557 LYS A CE    1 1 
ATOM   4449 N  NZ    . LYS A 1 557 ? 28.588  34.707  36.583  1 64.36  ? 557 LYS A NZ    1 1 
ATOM   4450 N  N     . ILE A 1 558 ? 30.73   28.059  33.533  1 47.91  ? 558 ILE A N     1 1 
ATOM   4451 C  CA    . ILE A 1 558 ? 29.874  27.175  32.723  1 47.05  ? 558 ILE A CA    1 1 
ATOM   4452 C  C     . ILE A 1 558 ? 29.258  26.059  33.569  1 46.35  ? 558 ILE A C     1 1 
ATOM   4453 O  O     . ILE A 1 558 ? 28.073  25.776  33.409  1 46.44  ? 558 ILE A O     1 1 
ATOM   4454 C  CB    . ILE A 1 558 ? 30.557  26.639  31.429  1 47.14  ? 558 ILE A CB    1 1 
ATOM   4455 C  CG1   . ILE A 1 558 ? 29.551  25.975  30.48   1 47.52  ? 558 ILE A CG1   1 1 
ATOM   4456 C  CG2   . ILE A 1 558 ? 31.706  25.705  31.737  1 47.67  ? 558 ILE A CG2   1 1 
ATOM   4457 C  CD1   . ILE A 1 558 ? 28.505  26.861  29.983  1 48.51  ? 558 ILE A CD1   1 1 
ATOM   4458 N  N     . GLY A 1 559 ? 30.022  25.517  34.516  1 45.45  ? 559 GLY A N     1 1 
ATOM   4459 C  CA    . GLY A 1 559 ? 29.545  24.478  35.419  1 45.17  ? 559 GLY A CA    1 1 
ATOM   4460 C  C     . GLY A 1 559 ? 28.401  24.958  36.286  1 44.63  ? 559 GLY A C     1 1 
ATOM   4461 O  O     . GLY A 1 559 ? 27.379  24.282  36.404  1 44.75  ? 559 GLY A O     1 1 
ATOM   4462 N  N     . VAL A 1 560 ? 28.546  26.156  36.858  1 43.88  ? 560 VAL A N     1 1 
ATOM   4463 C  CA    . VAL A 1 560 ? 27.514  26.767  37.693  1 43.52  ? 560 VAL A CA    1 1 
ATOM   4464 C  C     . VAL A 1 560 ? 26.268  27.099  36.841  1 42.58  ? 560 VAL A C     1 1 
ATOM   4465 O  O     . VAL A 1 560 ? 25.145  26.854  37.272  1 42.79  ? 560 VAL A O     1 1 
ATOM   4466 C  CB    . VAL A 1 560 ? 28.089  28.014  38.424  1 44.46  ? 560 VAL A CB    1 1 
ATOM   4467 C  CG1   . VAL A 1 560 ? 26.997  28.781  39.167  1 45.29  ? 560 VAL A CG1   1 1 
ATOM   4468 C  CG2   . VAL A 1 560 ? 29.226  27.624  39.368  1 44.71  ? 560 VAL A CG2   1 1 
ATOM   4469 N  N     . GLN A 1 561 ? 26.472  27.596  35.613  1 41.49  ? 561 GLN A N     1 1 
ATOM   4470 C  CA    . GLN A 1 561 ? 25.385  27.928  34.699  1 40.96  ? 561 GLN A CA    1 1 
ATOM   4471 C  C     . GLN A 1 561 ? 24.582  26.702  34.285  1 40.81  ? 561 GLN A C     1 1 
ATOM   4472 O  O     . GLN A 1 561 ? 23.375  26.817  34.104  1 41.08  ? 561 GLN A O     1 1 
ATOM   4473 C  CB    . GLN A 1 561 ? 25.91   28.662  33.463  1 41.83  ? 561 GLN A CB    1 1 
ATOM   4474 C  CG    . GLN A 1 561 ? 26.45   30.043  33.788  1 43.97  ? 561 GLN A CG    1 1 
ATOM   4475 C  CD    . GLN A 1 561 ? 27.06   30.72   32.588  1 46.79  ? 561 GLN A CD    1 1 
ATOM   4476 O  OE1   . GLN A 1 561 ? 28.272  30.641  32.334  1 47.46  ? 561 GLN A OE1   1 1 
ATOM   4477 N  NE2   . GLN A 1 561 ? 26.229  31.424  31.834  1 47.14  ? 561 GLN A NE2   1 1 
ATOM   4478 N  N     . LEU A 1 562 ? 25.225  25.529  34.151  1 40.13  ? 562 LEU A N     1 1 
ATOM   4479 C  CA    . LEU A 1 562 ? 24.503  24.311  33.786  1 39.75  ? 562 LEU A CA    1 1 
ATOM   4480 C  C     . LEU A 1 562 ? 23.552  23.914  34.893  1 39.59  ? 562 LEU A C     1 1 
ATOM   4481 O  O     . LEU A 1 562 ? 22.428  23.509  34.599  1 40.21  ? 562 LEU A O     1 1 
ATOM   4482 C  CB    . LEU A 1 562 ? 25.459  23.152  33.491  1 39.8   ? 562 LEU A CB    1 1 
ATOM   4483 C  CG    . LEU A 1 562 ? 26.381  23.326  32.304  1 41.11  ? 562 LEU A CG    1 1 
ATOM   4484 C  CD1   . LEU A 1 562 ? 27.303  22.154  32.17   1 41.8   ? 562 LEU A CD1   1 1 
ATOM   4485 C  CD2   . LEU A 1 562 ? 25.614  23.538  31.029  1 41.62  ? 562 LEU A CD2   1 1 
ATOM   4486 N  N     . ILE A 1 563 ? 23.982  24.039  36.166  1 38.75  ? 563 ILE A N     1 1 
ATOM   4487 C  CA    . ILE A 1 563 ? 23.128  23.706  37.307  1 38.52  ? 563 ILE A CA    1 1 
ATOM   4488 C  C     . ILE A 1 563 ? 21.994  24.705  37.407  1 38.71  ? 563 ILE A C     1 1 
ATOM   4489 O  O     . ILE A 1 563 ? 20.839  24.303  37.569  1 38.95  ? 563 ILE A O     1 1 
ATOM   4490 C  CB    . ILE A 1 563 ? 23.921  23.625  38.624  1 38.46  ? 563 ILE A CB    1 1 
ATOM   4491 C  CG1   . ILE A 1 563 ? 25.054  22.602  38.52   1 39.4   ? 563 ILE A CG1   1 1 
ATOM   4492 C  CG2   . ILE A 1 563 ? 22.993  23.318  39.796  1 38.59  ? 563 ILE A CG2   1 1 
ATOM   4493 C  CD1   . ILE A 1 563 ? 24.6    21.213  38.281  1 40.88  ? 563 ILE A CD1   1 1 
ATOM   4494 N  N     . LYS A 1 564 ? 22.309  26.004  37.243  1 38.28  ? 564 LYS A N     1 1 
ATOM   4495 C  CA    . LYS A 1 564 ? 21.3    27.063  37.277  1 38.41  ? 564 LYS A CA    1 1 
ATOM   4496 C  C     . LYS A 1 564 ? 20.245  26.926  36.163  1 38.05  ? 564 LYS A C     1 1 
ATOM   4497 O  O     . LYS A 1 564 ? 19.115  27.382  36.327  1 38     ? 564 LYS A O     1 1 
ATOM   4498 C  CB    . LYS A 1 564 ? 21.963  28.45   37.261  1 40.49  ? 564 LYS A CB    1 1 
ATOM   4499 C  CG    . LYS A 1 564 ? 22.874  28.725  38.465  1 44.68  ? 564 LYS A CG    1 1 
ATOM   4500 C  CD    . LYS A 1 564 ? 22.145  28.602  39.805  1 48.91  ? 564 LYS A CD    1 1 
ATOM   4501 C  CE    . LYS A 1 564 ? 23.092  28.457  40.966  1 52.07  ? 564 LYS A CE    1 1 
ATOM   4502 N  NZ    . LYS A 1 564 ? 22.435  27.772  42.112  1 53.91  ? 564 LYS A NZ    1 1 
ATOM   4503 N  N     . TYR A 1 565 ? 20.597  26.265  35.057  1 37.65  ? 565 TYR A N     1 1 
ATOM   4504 C  CA    . TYR A 1 565 ? 19.656  26.021  33.98   1 37.67  ? 565 TYR A CA    1 1 
ATOM   4505 C  C     . TYR A 1 565 ? 18.665  24.966  34.419  1 37.96  ? 565 TYR A C     1 1 
ATOM   4506 O  O     . TYR A 1 565 ? 17.471  25.134  34.19   1 38.34  ? 565 TYR A O     1 1 
ATOM   4507 C  CB    . TYR A 1 565 ? 20.368  25.555  32.721  1 37.49  ? 565 TYR A CB    1 1 
ATOM   4508 C  CG    . TYR A 1 565 ? 19.449  25.548  31.525  1 37.95  ? 565 TYR A CG    1 1 
ATOM   4509 C  CD1   . TYR A 1 565 ? 19.169  26.717  30.834  1 38.46  ? 565 TYR A CD1   1 1 
ATOM   4510 C  CD2   . TYR A 1 565 ? 18.82   24.384  31.115  1 38.84  ? 565 TYR A CD2   1 1 
ATOM   4511 C  CE1   . TYR A 1 565 ? 18.327  26.717  29.734  1 39.12  ? 565 TYR A CE1   1 1 
ATOM   4512 C  CE2   . TYR A 1 565 ? 17.967  24.374  30.022  1 39.61  ? 565 TYR A CE2   1 1 
ATOM   4513 C  CZ    . TYR A 1 565 ? 17.721  25.544  29.339  1 40.21  ? 565 TYR A CZ    1 1 
ATOM   4514 O  OH    . TYR A 1 565 ? 16.902  25.534  28.244  1 41.67  ? 565 TYR A OH    1 1 
ATOM   4515 N  N     . ILE A 1 566 ? 19.134  23.885  35.057  1 37.69  ? 566 ILE A N     1 1 
ATOM   4516 C  CA    . ILE A 1 566 ? 18.229  22.849  35.566  1 38.03  ? 566 ILE A CA    1 1 
ATOM   4517 C  C     . ILE A 1 566 ? 17.344  23.444  36.673  1 38.44  ? 566 ILE A C     1 1 
ATOM   4518 O  O     . ILE A 1 566 ? 16.148  23.165  36.716  1 38.56  ? 566 ILE A O     1 1 
ATOM   4519 C  CB    . ILE A 1 566 ? 19.006  21.591  36.03   1 38.48  ? 566 ILE A CB    1 1 
ATOM   4520 C  CG1   . ILE A 1 566 ? 19.95   21.08   34.927  1 39.37  ? 566 ILE A CG1   1 1 
ATOM   4521 C  CG2   . ILE A 1 566 ? 18.072  20.489  36.509  1 38.74  ? 566 ILE A CG2   1 1 
ATOM   4522 C  CD1   . ILE A 1 566 ? 19.266  20.596  33.679  1 40.47  ? 566 ILE A CD1   1 1 
ATOM   4523 N  N     . GLU A 1 567 ? 17.91   24.34   37.504  1 38.62  ? 567 GLU A N     1 1 
ATOM   4524 C  CA    . GLU A 1 567 ? 17.171  25.048  38.546  1 39.23  ? 567 GLU A CA    1 1 
ATOM   4525 C  C     . GLU A 1 567 ? 16.049  25.899  37.922  1 39.21  ? 567 GLU A C     1 1 
ATOM   4526 O  O     . GLU A 1 567 ? 14.974  25.994  38.506  1 39.3   ? 567 GLU A O     1 1 
ATOM   4527 C  CB    . GLU A 1 567 ? 18.123  25.944  39.367  1 41.7   ? 567 GLU A CB    1 1 
ATOM   4528 C  CG    . GLU A 1 567 ? 19.111  25.193  40.247  1 45.66  ? 567 GLU A CG    1 1 
ATOM   4529 C  CD    . GLU A 1 567 ? 18.642  24.948  41.669  1 51.26  ? 567 GLU A CD    1 1 
ATOM   4530 O  OE1   . GLU A 1 567 ? 17.43   25.125  41.942  1 52.96  ? 567 GLU A OE1   1 1 
ATOM   4531 O  OE2   . GLU A 1 567 ? 19.49   24.582  42.514  1 52.07  ? 567 GLU A OE2   1 1 
ATOM   4532 N  N     . TYR A 1 568 ? 16.296  26.494  36.733  1 38.97  ? 568 TYR A N     1 1 
ATOM   4533 C  CA    . TYR A 1 568 ? 15.321  27.306  35.995  1 39.18  ? 568 TYR A CA    1 1 
ATOM   4534 C  C     . TYR A 1 568 ? 14.148  26.451  35.561  1 38.38  ? 568 TYR A C     1 1 
ATOM   4535 O  O     . TYR A 1 568 ? 13.011  26.886  35.703  1 38.6   ? 568 TYR A O     1 1 
ATOM   4536 C  CB    . TYR A 1 568 ? 15.977  28.012  34.783  1 39.79  ? 568 TYR A CB    1 1 
ATOM   4537 C  CG    . TYR A 1 568 ? 15.034  28.437  33.67   1 40.99  ? 568 TYR A CG    1 1 
ATOM   4538 C  CD1   . TYR A 1 568 ? 14.28   29.595  33.775  1 42.03  ? 568 TYR A CD1   1 1 
ATOM   4539 C  CD2   . TYR A 1 568 ? 14.955  27.717  32.487  1 42.16  ? 568 TYR A CD2   1 1 
ATOM   4540 C  CE1   . TYR A 1 568 ? 13.452  30.014  32.741  1 43.23  ? 568 TYR A CE1   1 1 
ATOM   4541 C  CE2   . TYR A 1 568 ? 14.124  28.121  31.45   1 43.3   ? 568 TYR A CE2   1 1 
ATOM   4542 C  CZ    . TYR A 1 568 ? 13.362  29.265  31.584  1 44.44  ? 568 TYR A CZ    1 1 
ATOM   4543 O  OH    . TYR A 1 568 ? 12.514  29.656  30.57   1 46.52  ? 568 TYR A OH    1 1 
ATOM   4544 N  N     . LEU A 1 569 ? 14.416  25.249  35.032  1 37.3   ? 569 LEU A N     1 1 
ATOM   4545 C  CA    . LEU A 1 569 ? 13.354  24.344  34.609  1 36.66  ? 569 LEU A CA    1 1 
ATOM   4546 C  C     . LEU A 1 569 ? 12.554  23.852  35.811  1 37.14  ? 569 LEU A C     1 1 
ATOM   4547 O  O     . LEU A 1 569 ? 11.336  23.771  35.728  1 37.09  ? 569 LEU A O     1 1 
ATOM   4548 C  CB    . LEU A 1 569 ? 13.932  23.174  33.818  1 35.93  ? 569 LEU A CB    1 1 
ATOM   4549 C  CG    . LEU A 1 569 ? 14.669  23.558  32.552  1 36.32  ? 569 LEU A CG    1 1 
ATOM   4550 C  CD1   . LEU A 1 569 ? 15.331  22.359  31.933  1 36.61  ? 569 LEU A CD1   1 1 
ATOM   4551 C  CD2   . LEU A 1 569 ? 13.742  24.211  31.557  1 36.62  ? 569 LEU A CD2   1 1 
ATOM   4552 N  N     . PHE A 1 570 ? 13.225  23.59   36.946  1 37.68  ? 570 PHE A N     1 1 
ATOM   4553 C  CA    . PHE A 1 570 ? 12.58   23.17   38.196  1 38.75  ? 570 PHE A CA    1 1 
ATOM   4554 C  C     . PHE A 1 570 ? 11.638  24.233  38.771  1 39.74  ? 570 PHE A C     1 1 
ATOM   4555 O  O     . PHE A 1 570 ? 10.743  23.886  39.54   1 40.04  ? 570 PHE A O     1 1 
ATOM   4556 C  CB    . PHE A 1 570 ? 13.614  22.747  39.252  1 38.83  ? 570 PHE A CB    1 1 
ATOM   4557 C  CG    . PHE A 1 570 ? 13.996  21.288  39.198  1 39.47  ? 570 PHE A CG    1 1 
ATOM   4558 C  CD1   . PHE A 1 570 ? 13.086  20.305  39.523  1 40.35  ? 570 PHE A CD1   1 1 
ATOM   4559 C  CD2   . PHE A 1 570 ? 15.275  20.903  38.859  1 40.16  ? 570 PHE A CD2   1 1 
ATOM   4560 C  CE1   . PHE A 1 570 ? 13.447  18.965  39.483  1 40.97  ? 570 PHE A CE1   1 1 
ATOM   4561 C  CE2   . PHE A 1 570 ? 15.625  19.562  38.814  1 40.83  ? 570 PHE A CE2   1 1 
ATOM   4562 C  CZ    . PHE A 1 570 ? 14.709  18.603  39.117  1 40.54  ? 570 PHE A CZ    1 1 
ATOM   4563 N  N     . ASP A 1 571 ? 11.826  25.52   38.397  1 40.17  ? 571 ASP A N     1 1 
ATOM   4564 C  CA    . ASP A 1 571 ? 10.931  26.62   38.792  1 41.08  ? 571 ASP A CA    1 1 
ATOM   4565 C  C     . ASP A 1 571 ? 9.563   26.535  38.072  1 41.89  ? 571 ASP A C     1 1 
ATOM   4566 O  O     . ASP A 1 571 ? 8.643   27.276  38.421  1 42.07  ? 571 ASP A O     1 1 
ATOM   4567 C  CB    . ASP A 1 571 ? 11.557  27.991  38.468  1 42.65  ? 571 ASP A CB    1 1 
ATOM   4568 C  CG    . ASP A 1 571 ? 12.598  28.482  39.45   1 47.6   ? 571 ASP A CG    1 1 
ATOM   4569 O  OD1   . ASP A 1 571 ? 12.868  27.767  40.44   1 48.57  ? 571 ASP A OD1   1 1 
ATOM   4570 O  OD2   . ASP A 1 571 ? 13.148  29.582  39.228  1 49.82  ? 571 ASP A OD2   1 1 
ATOM   4571 N  N     . PHE A 1 572 ? 9.434   25.668  37.055  1 42.17  ? 572 PHE A N     1 1 
ATOM   4572 C  CA    . PHE A 1 572 ? 8.203   25.535  36.304  1 43.01  ? 572 PHE A CA    1 1 
ATOM   4573 C  C     . PHE A 1 572 ? 7.68    24.102  36.271  1 43.75  ? 572 PHE A C     1 1 
ATOM   4574 O  O     . PHE A 1 572 ? 8.454   23.148  36.384  1 43.89  ? 572 PHE A O     1 1 
ATOM   4575 C  CB    . PHE A 1 572 ? 8.409   26.059  34.88   1 42.93  ? 572 PHE A CB    1 1 
ATOM   4576 C  CG    . PHE A 1 572 ? 8.848   27.496  34.864  1 43.62  ? 572 PHE A CG    1 1 
ATOM   4577 C  CD1   . PHE A 1 572 ? 7.951   28.513  35.14   1 44.55  ? 572 PHE A CD1   1 1 
ATOM   4578 C  CD2   . PHE A 1 572 ? 10.171  27.828  34.644  1 44.44  ? 572 PHE A CD2   1 1 
ATOM   4579 C  CE1   . PHE A 1 572 ? 8.371   29.838  35.168  1 45.49  ? 572 PHE A CE1   1 1 
ATOM   4580 C  CE2   . PHE A 1 572 ? 10.588  29.15   34.663  1 45.17  ? 572 PHE A CE2   1 1 
ATOM   4581 C  CZ    . PHE A 1 572 ? 9.685   30.151  34.906  1 45.21  ? 572 PHE A CZ    1 1 
ATOM   4582 N  N     . THR A 1 573 ? 6.352   23.958  36.112  1 44.08  ? 573 THR A N     1 1 
ATOM   4583 C  CA    . THR A 1 573 ? 5.704   22.661  35.975  1 44.93  ? 573 THR A CA    1 1 
ATOM   4584 C  C     . THR A 1 573 ? 6.136   22.094  34.622  1 45.77  ? 573 THR A C     1 1 
ATOM   4585 O  O     . THR A 1 573 ? 6.08    22.809  33.615  1 46.08  ? 573 THR A O     1 1 
ATOM   4586 C  CB    . THR A 1 573 ? 4.168   22.814  36.064  1 45.91  ? 573 THR A CB    1 1 
ATOM   4587 O  OG1   . THR A 1 573 ? 3.793   22.94   37.436  1 46.89  ? 573 THR A OG1   1 1 
ATOM   4588 C  CG2   . THR A 1 573 ? 3.408   21.637  35.45   1 46.08  ? 573 THR A CG2   1 1 
ATOM   4589 N  N     . PRO A 1 574 ? 6.589   20.822  34.587  1 45.81  ? 574 PRO A N     1 1 
ATOM   4590 C  CA    . PRO A 1 574 ? 7.005   20.213  33.306  1 46.21  ? 574 PRO A CA    1 1 
ATOM   4591 C  C     . PRO A 1 574 ? 5.978   20.387  32.182  1 47.09  ? 574 PRO A C     1 1 
ATOM   4592 O  O     . PRO A 1 574 ? 4.775   20.453  32.453  1 47.05  ? 574 PRO A O     1 1 
ATOM   4593 C  CB    . PRO A 1 574 ? 7.169   18.729  33.646  1 46.82  ? 574 PRO A CB    1 1 
ATOM   4594 C  CG    . PRO A 1 574 ? 7.308   18.666  35.115  1 47.1   ? 574 PRO A CG    1 1 
ATOM   4595 C  CD    . PRO A 1 574 ? 6.709   19.885  35.72   1 45.26  ? 574 PRO A CD    1 1 
ATOM   4596 N  N     . SER A 1 575 ? 6.442   20.493  30.928  1 47.61  ? 575 SER A N     1 1 
ATOM   4597 C  CA    . SER A 1 575 ? 5.532   20.668  29.799  1 48.61  ? 575 SER A CA    1 1 
ATOM   4598 C  C     . SER A 1 575 ? 4.558   19.493  29.676  1 49.85  ? 575 SER A C     1 1 
ATOM   4599 O  O     . SER A 1 575 ? 3.354   19.695  29.562  1 49.74  ? 575 SER A O     1 1 
ATOM   4600 C  CB    . SER A 1 575 ? 6.312   20.843  28.5    1 49.41  ? 575 SER A CB    1 1 
ATOM   4601 O  OG    . SER A 1 575 ? 7.175   21.96   28.595  1 51.46  ? 575 SER A OG    1 1 
ATOM   4602 N  N     . VAL A 1 576 ? 5.081   18.267  29.759  1 50.88  ? 576 VAL A N     1 1 
ATOM   4603 C  CA    . VAL A 1 576 ? 4.301   17.044  29.64   1 52.33  ? 576 VAL A CA    1 1 
ATOM   4604 C  C     . VAL A 1 576 ? 4.754   15.975  30.652  1 54.29  ? 576 VAL A C     1 1 
ATOM   4605 O  O     . VAL A 1 576 ? 5.824   16.079  31.242  1 54.33  ? 576 VAL A O     1 1 
ATOM   4606 C  CB    . VAL A 1 576 ? 4.371   16.486  28.196  1 52.72  ? 576 VAL A CB    1 1 
ATOM   4607 C  CG1   . VAL A 1 576 ? 3.538   17.316  27.228  1 53.12  ? 576 VAL A CG1   1 1 
ATOM   4608 C  CG2   . VAL A 1 576 ? 5.817   16.354  27.73   1 53.09  ? 576 VAL A CG2   1 1 
ATOM   4609 N  N     . GLN A 1 577 ? 3.922   14.949  30.848  1 55.73  ? 577 GLN A N     1 1 
ATOM   4610 C  CA    . GLN A 1 577 ? 4.211   13.818  31.713  1 57.61  ? 577 GLN A CA    1 1 
ATOM   4611 C  C     . GLN A 1 577 ? 3.425   12.587  31.252  1 58.85  ? 577 GLN A C     1 1 
ATOM   4612 O  O     . GLN A 1 577 ? 2.4     12.714  30.579  1 59.19  ? 577 GLN A O     1 1 
ATOM   4613 C  CB    . GLN A 1 577 ? 3.911   14.141  33.186  1 59.93  ? 577 GLN A CB    1 1 
ATOM   4614 C  CG    . GLN A 1 577 ? 2.433   14.258  33.501  1 64.82  ? 577 GLN A CG    1 1 
ATOM   4615 C  CD    . GLN A 1 577 ? 2.213   14.336  34.981  1 70.67  ? 577 GLN A CD    1 1 
ATOM   4616 O  OE1   . GLN A 1 577 ? 2.71    15.249  35.645  1 72.72  ? 577 GLN A OE1   1 1 
ATOM   4617 N  NE2   . GLN A 1 577 ? 1.468   13.379  35.531  1 71.46  ? 577 GLN A NE2   1 1 
ATOM   4618 N  N     . ARG A 1 578 ? 3.902   11.401  31.61   1 59.4   ? 578 ARG A N     1 1 
ATOM   4619 C  CA    . ARG A 1 578 ? 3.215   10.163  31.261  1 60.68  ? 578 ARG A CA    1 1 
ATOM   4620 C  C     . ARG A 1 578 ? 3.558   9.071   32.264  1 61.76  ? 578 ARG A C     1 1 
ATOM   4621 O  O     . ARG A 1 578 ? 4.603   9.135   32.913  1 61.89  ? 578 ARG A O     1 1 
ATOM   4622 C  CB    . ARG A 1 578 ? 3.554   9.713   29.824  1 61.95  ? 578 ARG A CB    1 1 
ATOM   4623 C  CG    . ARG A 1 578 ? 5.005   9.305   29.625  1 64.43  ? 578 ARG A CG    1 1 
ATOM   4624 C  CD    . ARG A 1 578 ? 5.137   7.833   29.307  1 66.96  ? 578 ARG A CD    1 1 
ATOM   4625 N  NE    . ARG A 1 578 ? 6.471   7.511   28.81   1 69.37  ? 578 ARG A NE    1 1 
ATOM   4626 C  CZ    . ARG A 1 578 ? 6.773   7.337   27.529  1 71.58  ? 578 ARG A CZ    1 1 
ATOM   4627 N  NH1   . ARG A 1 578 ? 5.835   7.45    26.596  1 71.47  ? 578 ARG A NH1   1 1 
ATOM   4628 N  NH2   . ARG A 1 578 ? 8.013   7.044   27.168  1 71.58  ? 578 ARG A NH2   1 1 
ATOM   4629 N  N     . LYS A 1 579 ? 2.674   8.076   32.407  1 62.2   ? 579 LYS A N     1 1 
ATOM   4630 C  CA    . LYS A 1 579 ? 2.951   6.947   33.283  1 63.11  ? 579 LYS A CA    1 1 
ATOM   4631 C  C     . LYS A 1 579 ? 3.82    6.02    32.443  1 64.02  ? 579 LYS A C     1 1 
ATOM   4632 O  O     . LYS A 1 579 ? 3.424   5.67    31.33   1 64.47  ? 579 LYS A O     1 1 
ATOM   4633 C  CB    . LYS A 1 579 ? 1.651   6.231   33.675  1 65.06  ? 579 LYS A CB    1 1 
ATOM   4634 C  CG    . LYS A 1 579 ? 0.59    7.157   34.25   1 69.53  ? 579 LYS A CG    1 1 
ATOM   4635 C  CD    . LYS A 1 579 ? -0.801  6.778   33.773  1 74.42  ? 579 LYS A CD    1 1 
ATOM   4636 C  CE    . LYS A 1 579 ? -1.347  7.768   32.772  1 78.58  ? 579 LYS A CE    1 1 
ATOM   4637 N  NZ    . LYS A 1 579 ? -0.488  7.869   31.565  1 81.05  ? 579 LYS A NZ    1 1 
ATOM   4638 N  N     . ILE A 1 580 ? 5.013   5.65    32.939  1 64.06  ? 580 ILE A N     1 1 
ATOM   4639 C  CA    . ILE A 1 580 ? 5.916   4.766   32.207  1 64.6   ? 580 ILE A CA    1 1 
ATOM   4640 C  C     . ILE A 1 580 ? 5.265   3.395   31.947  1 65.44  ? 580 ILE A C     1 1 
ATOM   4641 O  O     . ILE A 1 580 ? 5.468   2.804   30.884  1 65.82  ? 580 ILE A O     1 1 
ATOM   4642 C  CB    . ILE A 1 580 ? 7.288   4.662   32.925  1 64.95  ? 580 ILE A CB    1 1 
ATOM   4643 C  CG1   . ILE A 1 580 ? 8.357   4.03    32.022  1 65.92  ? 580 ILE A CG1   1 1 
ATOM   4644 C  CG2   . ILE A 1 580 ? 7.188   3.929   34.258  1 65.36  ? 580 ILE A CG2   1 1 
ATOM   4645 C  CD1   . ILE A 1 580 ? 8.645   4.791   30.782  1 67.24  ? 580 ILE A CD1   1 1 
ATOM   4646 N  N     . ALA A 1 581 ? 4.429   2.927   32.885  1 65.47  ? 581 ALA A N     1 1 
ATOM   4647 C  CA    . ALA A 1 581 ? 3.757   1.648   32.77   1 66.11  ? 581 ALA A CA    1 1 
ATOM   4648 C  C     . ALA A 1 581 ? 2.586   1.712   31.803  1 66.64  ? 581 ALA A C     1 1 
ATOM   4649 O  O     . ALA A 1 581 ? 2.352   0.759   31.064  1 67.16  ? 581 ALA A O     1 1 
ATOM   4650 C  CB    . ALA A 1 581 ? 3.286   1.186   34.139  1 66.37  ? 581 ALA A CB    1 1 
ATOM   4651 N  N     . GLY A 1 582 ? 1.844   2.811   31.827  1 66.33  ? 582 GLY A N     1 1 
ATOM   4652 C  CA    . GLY A 1 582 ? 0.696   2.973   30.947  1 66.5   ? 582 GLY A CA    1 1 
ATOM   4653 C  C     . GLY A 1 582 ? 1.094   3.568   29.615  1 66.29  ? 582 GLY A C     1 1 
ATOM   4654 O  O     . GLY A 1 582 ? 1.591   2.869   28.73   1 66.46  ? 582 GLY A O     1 1 
ATOM   4655 N  N     . GLY A 1 583 ? 0.918   4.87    29.494  1 65.73  ? 583 GLY A N     1 1 
ATOM   4656 C  CA    . GLY A 1 583 ? 1.274   5.57    28.274  1 65.65  ? 583 GLY A CA    1 1 
ATOM   4657 C  C     . GLY A 1 583 ? 0.452   6.811   28.037  1 65.27  ? 583 GLY A C     1 1 
ATOM   4658 O  O     . GLY A 1 583 ? -0.304  7.251   28.907  1 65.13  ? 583 GLY A O     1 1 
ATOM   4659 N  N     . ASN A 1 584 ? 0.599   7.366   26.833  1 64.91  ? 584 ASN A N     1 1 
ATOM   4660 C  CA    . ASN A 1 584 ? -0.035  8.597   26.38   1 64.78  ? 584 ASN A CA    1 1 
ATOM   4661 C  C     . ASN A 1 584 ? 0.434   9.793   27.201  1 63.87  ? 584 ASN A C     1 1 
ATOM   4662 O  O     . ASN A 1 584 ? 0.27    9.855   28.426  1 63.55  ? 584 ASN A O     1 1 
ATOM   4663 C  CB    . ASN A 1 584 ? -1.558  8.5     26.281  1 66.25  ? 584 ASN A CB    1 1 
ATOM   4664 C  CG    . ASN A 1 584 ? -2.025  7.519   25.231  1 69.79  ? 584 ASN A CG    1 1 
ATOM   4665 O  OD1   . ASN A 1 584 ? -1.538  6.385   25.142  1 70.89  ? 584 ASN A OD1   1 1 
ATOM   4666 N  ND2   . ASN A 1 584 ? -2.994  7.928   24.419  1 70.76  ? 584 ASN A ND2   1 1 
ATOM   4667 N  N     . TRP A 1 585 ? 1.074   10.72   26.506  1 63.42  ? 585 TRP A N     1 1 
ATOM   4668 C  CA    . TRP A 1 585 ? 1.581   11.927  27.119  1 63.66  ? 585 TRP A CA    1 1 
ATOM   4669 C  C     . TRP A 1 585 ? 0.417   12.843  27.456  1 63.64  ? 585 TRP A C     1 1 
ATOM   4670 O  O     . TRP A 1 585 ? -0.474  13.043  26.635  1 63.86  ? 585 TRP A O     1 1 
ATOM   4671 C  CB    . TRP A 1 585 ? 2.522   12.653  26.152  1 63.66  ? 585 TRP A CB    1 1 
ATOM   4672 C  CG    . TRP A 1 585 ? 3.866   12.015  25.975  1 64.26  ? 585 TRP A CG    1 1 
ATOM   4673 C  CD1   . TRP A 1 585 ? 4.295   11.289  24.903  1 65.22  ? 585 TRP A CD1   1 1 
ATOM   4674 C  CD2   . TRP A 1 585 ? 4.985   12.116  26.864  1 64.37  ? 585 TRP A CD2   1 1 
ATOM   4675 N  NE1   . TRP A 1 585 ? 5.61    10.92   25.077  1 65.45  ? 585 TRP A NE1   1 1 
ATOM   4676 C  CE2   . TRP A 1 585 ? 6.054   11.406  26.278  1 65.09  ? 585 TRP A CE2   1 1 
ATOM   4677 C  CE3   . TRP A 1 585 ? 5.185   12.732  28.102  1 64.92  ? 585 TRP A CE3   1 1 
ATOM   4678 C  CZ2   . TRP A 1 585 ? 7.298   11.299  26.888  1 65.55  ? 585 TRP A CZ2   1 1 
ATOM   4679 C  CZ3   . TRP A 1 585 ? 6.423   12.628  28.701  1 65.65  ? 585 TRP A CZ3   1 1 
ATOM   4680 C  CH2   . TRP A 1 585 ? 7.462   11.922  28.093  1 65.66  ? 585 TRP A CH2   1 1 
ATOM   4681 N  N     . GLU A 1 586 ? 0.422   13.388  28.663  1 63.19  ? 586 GLU A N     1 1 
ATOM   4682 C  CA    . GLU A 1 586 ? -0.571  14.35   29.141  1 63.37  ? 586 GLU A CA    1 1 
ATOM   4683 C  C     . GLU A 1 586 ? 0.167   15.656  29.48   1 63.14  ? 586 GLU A C     1 1 
ATOM   4684 O  O     . GLU A 1 586 ? 1.395   15.645  29.613  1 63.42  ? 586 GLU A O     1 1 
ATOM   4685 C  CB    . GLU A 1 586 ? -1.316  13.839  30.402  1 65.94  ? 586 GLU A CB    1 1 
ATOM   4686 C  CG    . GLU A 1 586 ? -0.95   12.445  30.89   1 71.68  ? 586 GLU A CG    1 1 
ATOM   4687 C  CD    . GLU A 1 586 ? -1.038  12.251  32.393  1 78.67  ? 586 GLU A CD    1 1 
ATOM   4688 O  OE1   . GLU A 1 586 ? -0.369  11.327  32.914  1 80.21  ? 586 GLU A OE1   1 1 
ATOM   4689 O  OE2   . GLU A 1 586 ? -1.769  13.026  33.051  1 80.52  ? 586 GLU A OE2   1 1 
ATOM   4690 N  N     . PHE A 1 587 ? -0.559  16.78   29.632  1 62.38  ? 587 PHE A N     1 1 
ATOM   4691 C  CA    . PHE A 1 587 ? 0.083   18.031  30.031  1 62.04  ? 587 PHE A CA    1 1 
ATOM   4692 C  C     . PHE A 1 587 ? 0.583   17.884  31.472  1 61.94  ? 587 PHE A C     1 1 
ATOM   4693 O  O     . PHE A 1 587 ? 0.018   17.12   32.252  1 61.77  ? 587 PHE A O     1 1 
ATOM   4694 C  CB    . PHE A 1 587 ? -0.901  19.195  29.952  1 61.85  ? 587 PHE A CB    1 1 
ATOM   4695 C  CG    . PHE A 1 587 ? -1.135  19.762  28.575  1 62.22  ? 587 PHE A CG    1 1 
ATOM   4696 C  CD1   . PHE A 1 587 ? -0.076  20.042  27.736  1 62.98  ? 587 PHE A CD1   1 1 
ATOM   4697 C  CD2   . PHE A 1 587 ? -2.408  20.099  28.155  1 62.77  ? 587 PHE A CD2   1 1 
ATOM   4698 C  CE1   . PHE A 1 587 ? -0.294  20.6    26.484  1 63.56  ? 587 PHE A CE1   1 1 
ATOM   4699 C  CE2   . PHE A 1 587 ? -2.619  20.664  26.908  1 63.29  ? 587 PHE A CE2   1 1 
ATOM   4700 C  CZ    . PHE A 1 587 ? -1.564  20.906  26.078  1 63.09  ? 587 PHE A CZ    1 1 
ATOM   4701 N  N     . GLY A 1 588 ? 1.641   18.601  31.81   1 62.14  ? 588 GLY A N     1 1 
ATOM   4702 C  CA    . GLY A 1 588 ? 2.227   18.562  33.145  1 62.87  ? 588 GLY A CA    1 1 
ATOM   4703 C  C     . GLY A 1 588 ? 1.237   18.953  34.217  1 63.44  ? 588 GLY A C     1 1 
ATOM   4704 O  O     . GLY A 1 588 ? 0.532   19.952  34.08   1 63.59  ? 588 GLY A O     1 1 
ATOM   4705 N  N     . ASN A 1 589 ? 1.127   18.132  35.251  1 63.59  ? 589 ASN A N     1 1 
ATOM   4706 C  CA    . ASN A 1 589 ? 0.146   18.335  36.305  1 64.19  ? 589 ASN A CA    1 1 
ATOM   4707 C  C     . ASN A 1 589 ? 0.801   18.825  37.598  1 64.43  ? 589 ASN A C     1 1 
ATOM   4708 O  O     . ASN A 1 589 ? 0.356   19.815  38.176  1 64.44  ? 589 ASN A O     1 1 
ATOM   4709 C  CB    . ASN A 1 589 ? -0.598  17.007  36.521  1 65.53  ? 589 ASN A CB    1 1 
ATOM   4710 C  CG    . ASN A 1 589 ? -1.785  17.055  37.433  1 69.02  ? 589 ASN A CG    1 1 
ATOM   4711 O  OD1   . ASN A 1 589 ? -2.819  17.655  37.12   1 70.25  ? 589 ASN A OD1   1 1 
ATOM   4712 N  ND2   . ASN A 1 589 ? -1.678  16.374  38.562  1 69.91  ? 589 ASN A ND2   1 1 
ATOM   4713 N  N     . LYS A 1 590 ? 1.871   18.147  38.033  1 64.45  ? 590 LYS A N     1 1 
ATOM   4714 C  CA    . LYS A 1 590 ? 2.573   18.449  39.276  1 64.84  ? 590 LYS A CA    1 1 
ATOM   4715 C  C     . LYS A 1 590 ? 3.982   18.996  39.054  1 65.11  ? 590 LYS A C     1 1 
ATOM   4716 O  O     . LYS A 1 590 ? 4.665   18.573  38.123  1 65.37  ? 590 LYS A O     1 1 
ATOM   4717 C  CB    . LYS A 1 590 ? 2.611   17.201  40.184  1 66.54  ? 590 LYS A CB    1 1 
ATOM   4718 C  CG    . LYS A 1 590 ? 2.94    15.896  39.451  1 70.41  ? 590 LYS A CG    1 1 
ATOM   4719 C  CD    . LYS A 1 590 ? 3.006   14.701  40.397  1 74.73  ? 590 LYS A CD    1 1 
ATOM   4720 C  CE    . LYS A 1 590 ? 3.151   13.384  39.667  1 78.29  ? 590 LYS A CE    1 1 
ATOM   4721 N  NZ    . LYS A 1 590 ? 3.773   12.338  40.526  1 80.58  ? 590 LYS A NZ    1 1 
ATOM   4722 N  N     . SER A 1 591 ? 4.419   19.924  39.928  1 64.9   ? 591 SER A N     1 1 
ATOM   4723 C  CA    . SER A 1 591 ? 5.748   20.545  39.875  1 65     ? 591 SER A CA    1 1 
ATOM   4724 C  C     . SER A 1 591 ? 6.792   19.659  40.544  1 64.85  ? 591 SER A C     1 1 
ATOM   4725 O  O     . SER A 1 591 ? 6.499   19.014  41.549  1 64.96  ? 591 SER A O     1 1 
ATOM   4726 C  CB    . SER A 1 591 ? 5.728   21.904  40.575  1 66.2   ? 591 SER A CB    1 1 
ATOM   4727 O  OG    . SER A 1 591 ? 6.074   22.97   39.706  1 68.1   ? 591 SER A OG    1 1 
ATOM   4728 N  N     . LEU A 1 592 ? 8.013   19.647  40.01   1 64.51  ? 592 LEU A N     1 1 
ATOM   4729 C  CA    . LEU A 1 592 ? 9.096   18.859  40.6    1 64.62  ? 592 LEU A CA    1 1 
ATOM   4730 C  C     . LEU A 1 592 ? 9.912   19.711  41.577  1 64.58  ? 592 LEU A C     1 1 
ATOM   4731 O  O     . LEU A 1 592 ? 9.95    20.939  41.453  1 64.81  ? 592 LEU A O     1 1 
ATOM   4732 C  CB    . LEU A 1 592 ? 10      18.259  39.518  1 64.79  ? 592 LEU A CB    1 1 
ATOM   4733 C  CG    . LEU A 1 592 ? 9.625   16.863  39.03   1 66.22  ? 592 LEU A CG    1 1 
ATOM   4734 C  CD1   . LEU A 1 592 ? 8.237   16.85   38.402  1 66.84  ? 592 LEU A CD1   1 1 
ATOM   4735 C  CD2   . LEU A 1 592 ? 10.658  16.336  38.047  1 66.64  ? 592 LEU A CD2   1 1 
ATOM   4736 N  N     . VAL A 1 593 ? 10.551  19.065  42.556  1 64.12  ? 593 VAL A N     1 1 
ATOM   4737 C  CA    . VAL A 1 593 ? 11.316  19.778  43.578  1 64.27  ? 593 VAL A CA    1 1 
ATOM   4738 C  C     . VAL A 1 593 ? 12.825  19.503  43.47   1 63.87  ? 593 VAL A C     1 1 
ATOM   4739 O  O     . VAL A 1 593 ? 13.239  18.343  43.455  1 64.12  ? 593 VAL A O     1 1 
ATOM   4740 C  CB    . VAL A 1 593 ? 10.736  19.45   44.982  1 65.27  ? 593 VAL A CB    1 1 
ATOM   4741 C  CG1   . VAL A 1 593 ? 11.705  19.806  46.108  1 65.97  ? 593 VAL A CG1   1 1 
ATOM   4742 C  CG2   . VAL A 1 593 ? 9.391   20.138  45.188  1 65.8   ? 593 VAL A CG2   1 1 
ATOM   4743 N  N     . PRO A 1 594 ? 13.657  20.562  43.408  1 63     ? 594 PRO A N     1 1 
ATOM   4744 C  CA    . PRO A 1 594 ? 15.109  20.345  43.275  1 62.63  ? 594 PRO A CA    1 1 
ATOM   4745 C  C     . PRO A 1 594 ? 15.776  19.541  44.406  1 62.38  ? 594 PRO A C     1 1 
ATOM   4746 O  O     . PRO A 1 594 ? 16.731  18.81   44.12   1 62.53  ? 594 PRO A O     1 1 
ATOM   4747 C  CB    . PRO A 1 594 ? 15.692  21.757  43.142  1 63.24  ? 594 PRO A CB    1 1 
ATOM   4748 C  CG    . PRO A 1 594 ? 14.604  22.69   43.482  1 63.68  ? 594 PRO A CG    1 1 
ATOM   4749 C  CD    . PRO A 1 594 ? 13.297  21.991  43.366  1 62.27  ? 594 PRO A CD    1 1 
ATOM   4750 N  N     . ASN A 1 595 ? 15.277  19.622  45.665  1 61.83  ? 595 ASN A N     1 1 
ATOM   4751 C  CA    . ASN A 1 595 ? 15.869  18.818  46.752  1 61.88  ? 595 ASN A CA    1 1 
ATOM   4752 C  C     . ASN A 1 595 ? 15.684  17.302  46.545  1 61.25  ? 595 ASN A C     1 1 
ATOM   4753 O  O     . ASN A 1 595 ? 16.428  16.516  47.128  1 61.44  ? 595 ASN A O     1 1 
ATOM   4754 C  CB    . ASN A 1 595 ? 15.388  19.241  48.153  1 63.4   ? 595 ASN A CB    1 1 
ATOM   4755 C  CG    . ASN A 1 595 ? 16.052  18.449  49.279  1 66.98  ? 595 ASN A CG    1 1 
ATOM   4756 O  OD1   . ASN A 1 595 ? 17.286  18.405  49.401  1 68.35  ? 595 ASN A OD1   1 1 
ATOM   4757 N  ND2   . ASN A 1 595 ? 15.255  17.763  50.095  1 67.52  ? 595 ASN A ND2   1 1 
ATOM   4758 N  N     . ASP A 1 596 ? 14.714  16.891  45.715  1 60.31  ? 596 ASP A N     1 1 
ATOM   4759 C  CA    . ASP A 1 596 ? 14.524  15.477  45.412  1 59.87  ? 596 ASP A CA    1 1 
ATOM   4760 C  C     . ASP A 1 596 ? 15.705  14.918  44.575  1 58.76  ? 596 ASP A C     1 1 
ATOM   4761 O  O     . ASP A 1 596 ? 15.77   13.709  44.379  1 58.98  ? 596 ASP A O     1 1 
ATOM   4762 C  CB    . ASP A 1 596 ? 13.212  15.263  44.626  1 62.05  ? 596 ASP A CB    1 1 
ATOM   4763 C  CG    . ASP A 1 596 ? 11.924  15.578  45.367  1 67.63  ? 596 ASP A CG    1 1 
ATOM   4764 O  OD1   . ASP A 1 596 ? 11.909  15.457  46.611  1 68.91  ? 596 ASP A OD1   1 1 
ATOM   4765 O  OD2   . ASP A 1 596 ? 10.922  15.919  44.697  1 69.75  ? 596 ASP A OD2   1 1 
ATOM   4766 N  N     . PHE A 1 597 ? 16.616  15.784  44.061  1 57.36  ? 597 PHE A N     1 1 
ATOM   4767 C  CA    . PHE A 1 597 ? 17.699  15.371  43.177  1 56.39  ? 597 PHE A CA    1 1 
ATOM   4768 C  C     . PHE A 1 597 ? 19.062  15.89   43.575  1 55.07  ? 597 PHE A C     1 1 
ATOM   4769 O  O     . PHE A 1 597 ? 19.169  16.937  44.213  1 55.08  ? 597 PHE A O     1 1 
ATOM   4770 C  CB    . PHE A 1 597 ? 17.406  15.873  41.752  1 56.32  ? 597 PHE A CB    1 1 
ATOM   4771 C  CG    . PHE A 1 597 ? 16.097  15.375  41.205  1 57.05  ? 597 PHE A CG    1 1 
ATOM   4772 C  CD1   . PHE A 1 597 ? 14.927  16.082  41.412  1 57.75  ? 597 PHE A CD1   1 1 
ATOM   4773 C  CD2   . PHE A 1 597 ? 16.026  14.172  40.527  1 57.93  ? 597 PHE A CD2   1 1 
ATOM   4774 C  CE1   . PHE A 1 597 ? 13.718  15.603  40.939  1 58.39  ? 597 PHE A CE1   1 1 
ATOM   4775 C  CE2   . PHE A 1 597 ? 14.812  13.695  40.055  1 58.51  ? 597 PHE A CE2   1 1 
ATOM   4776 C  CZ    . PHE A 1 597 ? 13.668  14.415  40.262  1 58.18  ? 597 PHE A CZ    1 1 
ATOM   4777 N  N     . ILE A 1 598 ? 20.109  15.173  43.13   1 53.73  ? 598 ILE A N     1 1 
ATOM   4778 C  CA    . ILE A 1 598 ? 21.507  15.55   43.282  1 52.86  ? 598 ILE A CA    1 1 
ATOM   4779 C  C     . ILE A 1 598 ? 21.897  16.147  41.929  1 51.7   ? 598 ILE A C     1 1 
ATOM   4780 O  O     . ILE A 1 598 ? 21.797  15.443  40.929  1 51.88  ? 598 ILE A O     1 1 
ATOM   4781 C  CB    . ILE A 1 598 ? 22.372  14.299  43.569  1 53.29  ? 598 ILE A CB    1 1 
ATOM   4782 C  CG1   . ILE A 1 598 ? 21.854  13.503  44.777  1 54.42  ? 598 ILE A CG1   1 1 
ATOM   4783 C  CG2   . ILE A 1 598 ? 23.84   14.669  43.712  1 53.65  ? 598 ILE A CG2   1 1 
ATOM   4784 C  CD1   . ILE A 1 598 ? 21.91   14.227  46.08   1 55.96  ? 598 ILE A CD1   1 1 
ATOM   4785 N  N     . LEU A 1 599 ? 22.298  17.429  41.872  1 50.29  ? 599 LEU A N     1 1 
ATOM   4786 C  CA    . LEU A 1 599 ? 22.674  18.041  40.599  1 49.51  ? 599 LEU A CA    1 1 
ATOM   4787 C  C     . LEU A 1 599 ? 24.183  18.214  40.494  1 48.79  ? 599 LEU A C     1 1 
ATOM   4788 O  O     . LEU A 1 599 ? 24.79   18.82   41.371  1 48.95  ? 599 LEU A O     1 1 
ATOM   4789 C  CB    . LEU A 1 599 ? 22      19.405  40.431  1 49.7   ? 599 LEU A CB    1 1 
ATOM   4790 C  CG    . LEU A 1 599 ? 20.485  19.452  40.562  1 51.11  ? 599 LEU A CG    1 1 
ATOM   4791 C  CD1   . LEU A 1 599 ? 19.969  20.886  40.475  1 51.4   ? 599 LEU A CD1   1 1 
ATOM   4792 C  CD2   . LEU A 1 599 ? 19.833  18.604  39.505  1 51.9   ? 599 LEU A CD2   1 1 
ATOM   4793 N  N     . LEU A 1 600 ? 24.79   17.699  39.42   1 47.79  ? 600 LEU A N     1 1 
ATOM   4794 C  CA    . LEU A 1 600 ? 26.225  17.847  39.183  1 47.34  ? 600 LEU A CA    1 1 
ATOM   4795 C  C     . LEU A 1 600 ? 26.471  18.355  37.774  1 46.5   ? 600 LEU A C     1 1 
ATOM   4796 O  O     . LEU A 1 600 ? 25.652  18.133  36.888  1 46.39  ? 600 LEU A O     1 1 
ATOM   4797 C  CB    . LEU A 1 600 ? 26.976  16.522  39.361  1 47.77  ? 600 LEU A CB    1 1 
ATOM   4798 C  CG    . LEU A 1 600 ? 27.057  15.926  40.757  1 49.46  ? 600 LEU A CG    1 1 
ATOM   4799 C  CD1   . LEU A 1 600 ? 27.857  14.638  40.732  1 49.94  ? 600 LEU A CD1   1 1 
ATOM   4800 C  CD2   . LEU A 1 600 ? 27.661  16.896  41.745  1 50.27  ? 600 LEU A CD2   1 1 
ATOM   4801 N  N     . SER A 1 601 ? 27.597  19.034  37.559  1 45.97  ? 601 SER A N     1 1 
ATOM   4802 C  CA    . SER A 1 601 ? 27.942  19.547  36.237  1 46.04  ? 601 SER A CA    1 1 
ATOM   4803 C  C     . SER A 1 601 ? 29.276  18.994  35.794  1 46.06  ? 601 SER A C     1 1 
ATOM   4804 O  O     . SER A 1 601 ? 30.14   18.729  36.627  1 46.58  ? 601 SER A O     1 1 
ATOM   4805 C  CB    . SER A 1 601 ? 27.996  21.068  36.244  1 47.36  ? 601 SER A CB    1 1 
ATOM   4806 O  OG    . SER A 1 601 ? 29.001  21.536  37.127  1 49.35  ? 601 SER A OG    1 1 
ATOM   4807 N  N     . ALA A 1 602 ? 29.46   18.821  34.485  1 45.44  ? 602 ALA A N     1 1 
ATOM   4808 C  CA    . ALA A 1 602 ? 30.701  18.274  33.953  1 45.14  ? 602 ALA A CA    1 1 
ATOM   4809 C  C     . ALA A 1 602 ? 31.127  18.955  32.675  1 44.7   ? 602 ALA A C     1 1 
ATOM   4810 O  O     . ALA A 1 602 ? 30.299  19.357  31.87   1 44.68  ? 602 ALA A O     1 1 
ATOM   4811 C  CB    . ALA A 1 602 ? 30.561  16.78   33.721  1 45.31  ? 602 ALA A CB    1 1 
ATOM   4812 N  N     . GLY A 1 603 ? 32.423  19.079  32.5    1 44.53  ? 603 GLY A N     1 1 
ATOM   4813 C  CA    . GLY A 1 603 ? 32.988  19.674  31.303  1 45.13  ? 603 GLY A CA    1 1 
ATOM   4814 C  C     . GLY A 1 603 ? 33.889  18.671  30.624  1 45.59  ? 603 GLY A C     1 1 
ATOM   4815 O  O     . GLY A 1 603 ? 34.806  18.14   31.252  1 45.84  ? 603 GLY A O     1 1 
ATOM   4816 N  N     . ALA A 1 604 ? 33.619  18.37   29.359  1 45.59  ? 604 ALA A N     1 1 
ATOM   4817 C  CA    . ALA A 1 604 ? 34.414  17.398  28.623  1 46.15  ? 604 ALA A CA    1 1 
ATOM   4818 C  C     . ALA A 1 604 ? 35.153  18.058  27.482  1 46.32  ? 604 ALA A C     1 1 
ATOM   4819 O  O     . ALA A 1 604 ? 34.616  18.94   26.823  1 46.41  ? 604 ALA A O     1 1 
ATOM   4820 C  CB    . ALA A 1 604 ? 33.523  16.295  28.104  1 46.57  ? 604 ALA A CB    1 1 
ATOM   4821 N  N     . PHE A 1 605 ? 36.38   17.631  27.246  1 46.4   ? 605 PHE A N     1 1 
ATOM   4822 C  CA    . PHE A 1 605 ? 37.225  18.233  26.224  1 47.19  ? 605 PHE A CA    1 1 
ATOM   4823 C  C     . PHE A 1 605 ? 38.343  17.297  25.797  1 48.21  ? 605 PHE A C     1 1 
ATOM   4824 O  O     . PHE A 1 605 ? 38.584  16.281  26.452  1 48.35  ? 605 PHE A O     1 1 
ATOM   4825 C  CB    . PHE A 1 605 ? 37.842  19.537  26.766  1 47.01  ? 605 PHE A CB    1 1 
ATOM   4826 C  CG    . PHE A 1 605 ? 38.531  19.356  28.096  1 47.59  ? 605 PHE A CG    1 1 
ATOM   4827 C  CD1   . PHE A 1 605 ? 39.82   18.862  28.168  1 48.41  ? 605 PHE A CD1   1 1 
ATOM   4828 C  CD2   . PHE A 1 605 ? 37.88   19.657  29.275  1 48.54  ? 605 PHE A CD2   1 1 
ATOM   4829 C  CE1   . PHE A 1 605 ? 40.438  18.664  29.392  1 49.18  ? 605 PHE A CE1   1 1 
ATOM   4830 C  CE2   . PHE A 1 605 ? 38.503  19.464  30.498  1 49.33  ? 605 PHE A CE2   1 1 
ATOM   4831 C  CZ    . PHE A 1 605 ? 39.78   18.974  30.548  1 49.09  ? 605 PHE A CZ    1 1 
ATOM   4832 N  N     . ILE A 1 606 ? 39.068  17.663  24.731  1 48.72  ? 606 ILE A N     1 1 
ATOM   4833 C  CA    . ILE A 1 606 ? 40.206  16.883  24.298  1 49.68  ? 606 ILE A CA    1 1 
ATOM   4834 C  C     . ILE A 1 606 ? 41.484  17.506  24.854  1 50.57  ? 606 ILE A C     1 1 
ATOM   4835 O  O     . ILE A 1 606 ? 41.687  18.709  24.719  1 50.41  ? 606 ILE A O     1 1 
ATOM   4836 C  CB    . ILE A 1 606 ? 40.229  16.683  22.765  1 50.32  ? 606 ILE A CB    1 1 
ATOM   4837 C  CG1   . ILE A 1 606 ? 39.128  15.717  22.332  1 51.12  ? 606 ILE A CG1   1 1 
ATOM   4838 C  CG2   . ILE A 1 606 ? 41.57   16.136  22.313  1 51.1   ? 606 ILE A CG2   1 1 
ATOM   4839 C  CD1   . ILE A 1 606 ? 38.866  15.72   20.88   1 52.29  ? 606 ILE A CD1   1 1 
ATOM   4840 N  N     . ASP A 1 607 ? 42.325  16.697  25.514  1 51.45  ? 607 ASP A N     1 1 
ATOM   4841 C  CA    . ASP A 1 607 ? 43.598  17.171  26.051  1 52.86  ? 607 ASP A CA    1 1 
ATOM   4842 C  C     . ASP A 1 607 ? 44.691  16.143  25.828  1 54.05  ? 607 ASP A C     1 1 
ATOM   4843 O  O     . ASP A 1 607 ? 44.596  15.033  26.346  1 54.18  ? 607 ASP A O     1 1 
ATOM   4844 C  CB    . ASP A 1 607 ? 43.499  17.47   27.55   1 54.64  ? 607 ASP A CB    1 1 
ATOM   4845 C  CG    . ASP A 1 607 ? 44.823  17.931  28.126  1 58.94  ? 607 ASP A CG    1 1 
ATOM   4846 O  OD1   . ASP A 1 607 ? 45.33   18.98   27.671  1 59.72  ? 607 ASP A OD1   1 1 
ATOM   4847 O  OD2   . ASP A 1 607 ? 45.366  17.225  29.014  1 60.77  ? 607 ASP A OD2   1 1 
ATOM   4848 N  N     . TYR A 1 608 ? 45.773  16.539  25.16   1 54.83  ? 608 TYR A N     1 1 
ATOM   4849 C  CA    . TYR A 1 608 ? 46.887  15.624  24.927  1 56.13  ? 608 TYR A CA    1 1 
ATOM   4850 C  C     . TYR A 1 608 ? 47.99   15.733  25.979  1 57.11  ? 608 TYR A C     1 1 
ATOM   4851 O  O     . TYR A 1 608 ? 49.128  16.08   25.663  1 57.11  ? 608 TYR A O     1 1 
ATOM   4852 C  CB    . TYR A 1 608 ? 47.43   15.793  23.519  1 56.19  ? 608 TYR A CB    1 1 
ATOM   4853 C  CG    . TYR A 1 608 ? 46.408  15.431  22.471  1 56.75  ? 608 TYR A CG    1 1 
ATOM   4854 C  CD1   . TYR A 1 608 ? 46.16   14.109  22.143  1 57.33  ? 608 TYR A CD1   1 1 
ATOM   4855 C  CD2   . TYR A 1 608 ? 45.681  16.412  21.815  1 57.68  ? 608 TYR A CD2   1 1 
ATOM   4856 C  CE1   . TYR A 1 608 ? 45.238  13.772  21.165  1 58.22  ? 608 TYR A CE1   1 1 
ATOM   4857 C  CE2   . TYR A 1 608 ? 44.772  16.089  20.819  1 58.56  ? 608 TYR A CE2   1 1 
ATOM   4858 C  CZ    . TYR A 1 608 ? 44.54   14.766  20.508  1 59.31  ? 608 TYR A CZ    1 1 
ATOM   4859 O  OH    . TYR A 1 608 ? 43.621  14.445  19.538  1 60.83  ? 608 TYR A OH    1 1 
ATOM   4860 N  N     . ASP A 1 609 ? 47.621  15.462  27.239  1 57.77  ? 609 ASP A N     1 1 
ATOM   4861 C  CA    . ASP A 1 609 ? 48.482  15.473  28.416  1 58.82  ? 609 ASP A CA    1 1 
ATOM   4862 C  C     . ASP A 1 609 ? 49.216  16.785  28.66   1 59.61  ? 609 ASP A C     1 1 
ATOM   4863 O  O     . ASP A 1 609 ? 50.274  16.776  29.283  1 59.69  ? 609 ASP A O     1 1 
ATOM   4864 C  CB    . ASP A 1 609 ? 49.462  14.3    28.373  1 60.79  ? 609 ASP A CB    1 1 
ATOM   4865 C  CG    . ASP A 1 609 ? 48.76   12.961  28.331  1 66.2   ? 609 ASP A CG    1 1 
ATOM   4866 O  OD1   . ASP A 1 609 ? 47.644  12.858  28.894  1 67.22  ? 609 ASP A OD1   1 1 
ATOM   4867 O  OD2   . ASP A 1 609 ? 49.326  12.011  27.74   1 68.6   ? 609 ASP A OD2   1 1 
ATOM   4868 N  N     . ASN A 1 610 ? 48.653  17.912  28.204  1 60.13  ? 610 ASN A N     1 1 
ATOM   4869 C  CA    . ASN A 1 610 ? 49.266  19.228  28.429  1 61.21  ? 610 ASN A CA    1 1 
ATOM   4870 C  C     . ASN A 1 610 ? 48.72   19.957  29.678  1 61.89  ? 610 ASN A C     1 1 
ATOM   4871 O  O     . ASN A 1 610 ? 49.058  21.126  29.889  1 61.8   ? 610 ASN A O     1 1 
ATOM   4872 C  CB    . ASN A 1 610 ? 49.203  20.139  27.187  1 62.55  ? 610 ASN A CB    1 1 
ATOM   4873 C  CG    . ASN A 1 610 ? 48.046  19.892  26.246  1 66.4   ? 610 ASN A CG    1 1 
ATOM   4874 O  OD1   . ASN A 1 610 ? 48.128  19.066  25.329  1 67.69  ? 610 ASN A OD1   1 1 
ATOM   4875 N  ND2   . ASN A 1 610 ? 46.942  20.605  26.445  1 67.36  ? 610 ASN A ND2   1 1 
ATOM   4876 N  N     . LEU A 1 611 ? 47.905  19.261  30.517  1 62.24  ? 611 LEU A N     1 1 
ATOM   4877 C  CA    . LEU A 1 611 ? 47.345  19.825  31.748  1 62.83  ? 611 LEU A CA    1 1 
ATOM   4878 C  C     . LEU A 1 611 ? 48.01   19.259  33.005  1 63.27  ? 611 LEU A C     1 1 
ATOM   4879 O  O     . LEU A 1 611 ? 48.021  18.046  33.219  1 63.11  ? 611 LEU A O     1 1 
ATOM   4880 C  CB    . LEU A 1 611 ? 45.835  19.595  31.835  1 62.97  ? 611 LEU A CB    1 1 
ATOM   4881 C  CG    . LEU A 1 611 ? 44.983  20.282  30.788  1 64.48  ? 611 LEU A CG    1 1 
ATOM   4882 C  CD1   . LEU A 1 611 ? 43.536  19.875  30.923  1 65.25  ? 611 LEU A CD1   1 1 
ATOM   4883 C  CD2   . LEU A 1 611 ? 45.116  21.778  30.852  1 65.01  ? 611 LEU A CD2   1 1 
ATOM   4884 N  N     . THR A 1 612 ? 48.541  20.151  33.842  1 63.53  ? 612 THR A N     1 1 
ATOM   4885 C  CA    . THR A 1 612 ? 49.189  19.825  35.111  1 64.22  ? 612 THR A CA    1 1 
ATOM   4886 C  C     . THR A 1 612 ? 48.15   19.883  36.27   1 64.93  ? 612 THR A C     1 1 
ATOM   4887 O  O     . THR A 1 612 ? 47.002  20.25   36.03   1 64.75  ? 612 THR A O     1 1 
ATOM   4888 C  CB    . THR A 1 612 ? 50.357  20.81   35.331  1 65.18  ? 612 THR A CB    1 1 
ATOM   4889 O  OG1   . THR A 1 612 ? 49.819  22.106  35.562  1 66     ? 612 THR A OG1   1 1 
ATOM   4890 C  CG2   . THR A 1 612 ? 51.314  20.858  34.155  1 65.53  ? 612 THR A CG2   1 1 
ATOM   4891 N  N     . GLU A 1 613 ? 48.553  19.56   37.528  1 65.51  ? 613 GLU A N     1 1 
ATOM   4892 C  CA    . GLU A 1 613 ? 47.682  19.639  38.711  1 66.29  ? 613 GLU A CA    1 1 
ATOM   4893 C  C     . GLU A 1 613 ? 47.146  21.062  38.862  1 66.44  ? 613 GLU A C     1 1 
ATOM   4894 O  O     . GLU A 1 613 ? 45.968  21.241  39.163  1 66.55  ? 613 GLU A O     1 1 
ATOM   4895 C  CB    . GLU A 1 613 ? 48.462  19.286  39.998  1 69     ? 613 GLU A CB    1 1 
ATOM   4896 C  CG    . GLU A 1 613 ? 48.699  17.809  40.248  1 74.02  ? 613 GLU A CG    1 1 
ATOM   4897 C  CD    . GLU A 1 613 ? 49.259  17.513  41.629  1 79.94  ? 613 GLU A CD    1 1 
ATOM   4898 O  OE1   . GLU A 1 613 ? 49.003  18.316  42.557  1 80.97  ? 613 GLU A OE1   1 1 
ATOM   4899 O  OE2   . GLU A 1 613 ? 49.948  16.478  41.787  1 81.81  ? 613 GLU A OE2   1 1 
ATOM   4900 N  N     . ASN A 1 614 ? 48.022  22.068  38.652  1 66.26  ? 614 ASN A N     1 1 
ATOM   4901 C  CA    . ASN A 1 614 ? 47.679  23.484  38.744  1 66.7   ? 614 ASN A CA    1 1 
ATOM   4902 C  C     . ASN A 1 614 ? 46.683  23.877  37.657  1 66.93  ? 614 ASN A C     1 1 
ATOM   4903 O  O     . ASN A 1 614 ? 45.758  24.649  37.919  1 67.03  ? 614 ASN A O     1 1 
ATOM   4904 C  CB    . ASN A 1 614 ? 48.935  24.348  38.628  1 67.77  ? 614 ASN A CB    1 1 
ATOM   4905 C  CG    . ASN A 1 614 ? 49.521  24.747  39.953  1 70.83  ? 614 ASN A CG    1 1 
ATOM   4906 O  OD1   . ASN A 1 614 ? 49.065  25.699  40.598  1 71.9   ? 614 ASN A OD1   1 1 
ATOM   4907 N  ND2   . ASN A 1 614 ? 50.554  24.032  40.383  1 71.49  ? 614 ASN A ND2   1 1 
ATOM   4908 N  N     . ASP A 1 615 ? 46.868  23.34   36.44   1 66.74  ? 615 ASP A N     1 1 
ATOM   4909 C  CA    . ASP A 1 615 ? 45.983  23.622  35.317  1 66.93  ? 615 ASP A CA    1 1 
ATOM   4910 C  C     . ASP A 1 615 ? 44.583  23.114  35.617  1 66.65  ? 615 ASP A C     1 1 
ATOM   4911 O  O     . ASP A 1 615 ? 43.623  23.861  35.443  1 66.81  ? 615 ASP A O     1 1 
ATOM   4912 C  CB    . ASP A 1 615 ? 46.515  22.997  34.02   1 68.78  ? 615 ASP A CB    1 1 
ATOM   4913 C  CG    . ASP A 1 615 ? 47.686  23.73   33.39   1 73.59  ? 615 ASP A CG    1 1 
ATOM   4914 O  OD1   . ASP A 1 615 ? 47.904  24.911  33.737  1 74.46  ? 615 ASP A OD1   1 1 
ATOM   4915 O  OD2   . ASP A 1 615 ? 48.383  23.121  32.549  1 75.8   ? 615 ASP A OD2   1 1 
ATOM   4916 N  N     . TYR A 1 616 ? 44.465  21.885  36.148  1 66.11  ? 616 TYR A N     1 1 
ATOM   4917 C  CA    . TYR A 1 616 ? 43.164  21.326  36.516  1 66.1   ? 616 TYR A CA    1 1 
ATOM   4918 C  C     . TYR A 1 616 ? 42.509  22.165  37.602  1 65.42  ? 616 TYR A C     1 1 
ATOM   4919 O  O     . TYR A 1 616 ? 41.319  22.452  37.508  1 65.67  ? 616 TYR A O     1 1 
ATOM   4920 C  CB    . TYR A 1 616 ? 43.284  19.863  36.97   1 66.42  ? 616 TYR A CB    1 1 
ATOM   4921 C  CG    . TYR A 1 616 ? 43.298  18.892  35.811  1 67.6   ? 616 TYR A CG    1 1 
ATOM   4922 C  CD1   . TYR A 1 616 ? 42.164  18.684  35.04   1 68.73  ? 616 TYR A CD1   1 1 
ATOM   4923 C  CD2   . TYR A 1 616 ? 44.447  18.193  35.479  1 68.7   ? 616 TYR A CD2   1 1 
ATOM   4924 C  CE1   . TYR A 1 616 ? 42.176  17.807  33.963  1 69.76  ? 616 TYR A CE1   1 1 
ATOM   4925 C  CE2   . TYR A 1 616 ? 44.472  17.317  34.402  1 69.73  ? 616 TYR A CE2   1 1 
ATOM   4926 C  CZ    . TYR A 1 616 ? 43.334  17.123  33.647  1 70.74  ? 616 TYR A CZ    1 1 
ATOM   4927 O  OH    . TYR A 1 616 ? 43.363  16.254  32.584  1 72.45  ? 616 TYR A OH    1 1 
ATOM   4928 N  N     . GLU A 1 617 ? 43.298  22.617  38.587  1 64.32  ? 617 GLU A N     1 1 
ATOM   4929 C  CA    . GLU A 1 617 ? 42.818  23.465  39.673  1 63.64  ? 617 GLU A CA    1 1 
ATOM   4930 C  C     . GLU A 1 617 ? 42.302  24.798  39.128  1 62.25  ? 617 GLU A C     1 1 
ATOM   4931 O  O     . GLU A 1 617 ? 41.308  25.312  39.631  1 62.2   ? 617 GLU A O     1 1 
ATOM   4932 C  CB    . GLU A 1 617 ? 43.936  23.692  40.695  1 66.42  ? 617 GLU A CB    1 1 
ATOM   4933 C  CG    . GLU A 1 617 ? 43.451  23.982  42.105  1 72.42  ? 617 GLU A CG    1 1 
ATOM   4934 C  CD    . GLU A 1 617 ? 44.582  24.19   43.096  1 80.77  ? 617 GLU A CD    1 1 
ATOM   4935 O  OE1   . GLU A 1 617 ? 44.385  24.944  44.076  1 82.3   ? 617 GLU A OE1   1 1 
ATOM   4936 O  OE2   . GLU A 1 617 ? 45.675  23.614  42.883  1 83.77  ? 617 GLU A OE2   1 1 
ATOM   4937 N  N     . LYS A 1 618 ? 42.949  25.338  38.082  1 61.03  ? 618 LYS A N     1 1 
ATOM   4938 C  CA    . LYS A 1 618 ? 42.522  26.591  37.464  1 60.32  ? 618 LYS A CA    1 1 
ATOM   4939 C  C     . LYS A 1 618 ? 41.261  26.405  36.619  1 58.58  ? 618 LYS A C     1 1 
ATOM   4940 O  O     . LYS A 1 618 ? 40.385  27.259  36.656  1 58.29  ? 618 LYS A O     1 1 
ATOM   4941 C  CB    . LYS A 1 618 ? 43.661  27.24   36.655  1 62.81  ? 618 LYS A CB    1 1 
ATOM   4942 C  CG    . LYS A 1 618 ? 43.366  28.676  36.192  1 67.51  ? 618 LYS A CG    1 1 
ATOM   4943 C  CD    . LYS A 1 618 ? 43.111  29.653  37.358  1 71.71  ? 618 LYS A CD    1 1 
ATOM   4944 C  CE    . LYS A 1 618 ? 42.566  30.989  36.901  1 74.61  ? 618 LYS A CE    1 1 
ATOM   4945 N  NZ    . LYS A 1 618 ? 42.284  31.888  38.051  1 76.24  ? 618 LYS A NZ    1 1 
ATOM   4946 N  N     . ILE A 1 619 ? 41.127  25.269  35.915  1 57.4   ? 619 ILE A N     1 1 
ATOM   4947 C  CA    . ILE A 1 619 ? 39.917  24.989  35.133  1 56.77  ? 619 ILE A CA    1 1 
ATOM   4948 C  C     . ILE A 1 619 ? 38.715  24.883  36.076  1 56.2   ? 619 ILE A C     1 1 
ATOM   4949 O  O     . ILE A 1 619 ? 37.677  25.471  35.804  1 56.43  ? 619 ILE A O     1 1 
ATOM   4950 C  CB    . ILE A 1 619 ? 40.043  23.712  34.255  1 56.97  ? 619 ILE A CB    1 1 
ATOM   4951 C  CG1   . ILE A 1 619 ? 41.216  23.805  33.278  1 57.49  ? 619 ILE A CG1   1 1 
ATOM   4952 C  CG2   . ILE A 1 619 ? 38.745  23.448  33.499  1 57.48  ? 619 ILE A CG2   1 1 
ATOM   4953 C  CD1   . ILE A 1 619 ? 41.538  22.512  32.605  1 58.32  ? 619 ILE A CD1   1 1 
ATOM   4954 N  N     . PHE A 1 620 ? 38.878  24.192  37.21   1 55.36  ? 620 PHE A N     1 1 
ATOM   4955 C  CA    . PHE A 1 620 ? 37.813  24.069  38.197  1 55.22  ? 620 PHE A CA    1 1 
ATOM   4956 C  C     . PHE A 1 620 ? 37.431  25.434  38.763  1 55.46  ? 620 PHE A C     1 1 
ATOM   4957 O  O     . PHE A 1 620 ? 36.253  25.702  38.965  1 55.67  ? 620 PHE A O     1 1 
ATOM   4958 C  CB    . PHE A 1 620 ? 38.235  23.15   39.346  1 54.86  ? 620 PHE A CB    1 1 
ATOM   4959 C  CG    . PHE A 1 620 ? 38.15   21.677  39.047  1 55.35  ? 620 PHE A CG    1 1 
ATOM   4960 C  CD1   . PHE A 1 620 ? 36.985  21.119  38.558  1 56.1   ? 620 PHE A CD1   1 1 
ATOM   4961 C  CD2   . PHE A 1 620 ? 39.211  20.838  39.322  1 55.96  ? 620 PHE A CD2   1 1 
ATOM   4962 C  CE1   . PHE A 1 620 ? 36.899  19.757  38.317  1 56.65  ? 620 PHE A CE1   1 1 
ATOM   4963 C  CE2   . PHE A 1 620 ? 39.129  19.481  39.057  1 56.57  ? 620 PHE A CE2   1 1 
ATOM   4964 C  CZ    . PHE A 1 620 ? 37.972  18.95   38.564  1 56.35  ? 620 PHE A CZ    1 1 
ATOM   4965 N  N     . GLU A 1 621 ? 38.419  26.294  39.025  1 55.26  ? 621 GLU A N     1 1 
ATOM   4966 C  CA    . GLU A 1 621 ? 38.159  27.623  39.568  1 55.44  ? 621 GLU A CA    1 1 
ATOM   4967 C  C     . GLU A 1 621 ? 37.419  28.484  38.549  1 54.55  ? 621 GLU A C     1 1 
ATOM   4968 O  O     . GLU A 1 621 ? 36.525  29.23   38.922  1 54.75  ? 621 GLU A O     1 1 
ATOM   4969 C  CB    . GLU A 1 621 ? 39.478  28.301  40.001  1 58.66  ? 621 GLU A CB    1 1 
ATOM   4970 C  CG    . GLU A 1 621 ? 39.349  29.22   41.208  1 65.22  ? 621 GLU A CG    1 1 
ATOM   4971 C  CD    . GLU A 1 621 ? 39.639  30.69   40.958  1 73.81  ? 621 GLU A CD    1 1 
ATOM   4972 O  OE1   . GLU A 1 621 ? 39.235  31.206  39.89   1 75.68  ? 621 GLU A OE1   1 1 
ATOM   4973 O  OE2   . GLU A 1 621 ? 40.264  31.329  41.836  1 76.56  ? 621 GLU A OE2   1 1 
ATOM   4974 N  N     . VAL A 1 622 ? 37.785  28.378  37.268  1 53.55  ? 622 VAL A N     1 1 
ATOM   4975 C  CA    . VAL A 1 622 ? 37.166  29.155  36.197  1 53.04  ? 622 VAL A CA    1 1 
ATOM   4976 C  C     . VAL A 1 622 ? 35.738  28.676  35.861  1 52.19  ? 622 VAL A C     1 1 
ATOM   4977 O  O     . VAL A 1 622 ? 34.809  29.479  35.834  1 52.36  ? 622 VAL A O     1 1 
ATOM   4978 C  CB    . VAL A 1 622 ? 38.088  29.197  34.944  1 53.79  ? 622 VAL A CB    1 1 
ATOM   4979 C  CG1   . VAL A 1 622 ? 37.343  29.69   33.701  1 54.38  ? 622 VAL A CG1   1 1 
ATOM   4980 C  CG2   . VAL A 1 622 ? 39.327  30.049  35.206  1 54.24  ? 622 VAL A CG2   1 1 
ATOM   4981 N  N     . THR A 1 623 ? 35.564  27.38   35.627  1 51.02  ? 623 THR A N     1 1 
ATOM   4982 C  CA    . THR A 1 623 ? 34.277  26.825  35.22   1 50.49  ? 623 THR A CA    1 1 
ATOM   4983 C  C     . THR A 1 623 ? 33.299  26.492  36.343  1 50.11  ? 623 THR A C     1 1 
ATOM   4984 O  O     . THR A 1 623 ? 32.092  26.616  36.171  1 50.08  ? 623 THR A O     1 1 
ATOM   4985 C  CB    . THR A 1 623 ? 34.519  25.582  34.386  1 51.18  ? 623 THR A CB    1 1 
ATOM   4986 O  OG1   . THR A 1 623 ? 35.112  24.583  35.217  1 51.97  ? 623 THR A OG1   1 1 
ATOM   4987 C  CG2   . THR A 1 623 ? 35.406  25.855  33.194  1 51.34  ? 623 THR A CG2   1 1 
ATOM   4988 N  N     . GLY A 1 624 ? 33.816  25.988  37.449  1 49.58  ? 624 GLY A N     1 1 
ATOM   4989 C  CA    . GLY A 1 624 ? 32.981  25.566  38.567  1 49.19  ? 624 GLY A CA    1 1 
ATOM   4990 C  C     . GLY A 1 624 ? 32.411  24.169  38.409  1 48.22  ? 624 GLY A C     1 1 
ATOM   4991 O  O     . GLY A 1 624 ? 31.551  23.766  39.192  1 48.73  ? 624 GLY A O     1 1 
ATOM   4992 N  N     . CYS A 1 625 ? 32.875  23.417  37.401  1 46.74  ? 625 CYS A N     1 1 
ATOM   4993 C  CA    . CYS A 1 625 ? 32.397  22.069  37.132  1 45.97  ? 625 CYS A CA    1 1 
ATOM   4994 C  C     . CYS A 1 625 ? 32.674  21.125  38.276  1 45.14  ? 625 CYS A C     1 1 
ATOM   4995 O  O     . CYS A 1 625 ? 33.68   21.266  38.945  1 45.25  ? 625 CYS A O     1 1 
ATOM   4996 C  CB    . CYS A 1 625 ? 33.001  21.543  35.836  1 46.49  ? 625 CYS A CB    1 1 
ATOM   4997 S  SG    . CYS A 1 625 ? 32.462  22.432  34.356  1 49.14  ? 625 CYS A SG    1 1 
ATOM   4998 N  N     . ASP A 1 626 ? 31.793  20.163  38.505  1 44.49  ? 626 ASP A N     1 1 
ATOM   4999 C  CA    . ASP A 1 626 ? 32.016  19.142  39.531  1 44.44  ? 626 ASP A CA    1 1 
ATOM   5000 C  C     . ASP A 1 626 ? 32.916  18.014  38.994  1 44.15  ? 626 ASP A C     1 1 
ATOM   5001 O  O     . ASP A 1 626 ? 33.583  17.34   39.77   1 44.3   ? 626 ASP A O     1 1 
ATOM   5002 C  CB    . ASP A 1 626 ? 30.688  18.538  40.011  1 45.99  ? 626 ASP A CB    1 1 
ATOM   5003 C  CG    . ASP A 1 626 ? 29.781  19.53   40.692  1 50.16  ? 626 ASP A CG    1 1 
ATOM   5004 O  OD1   . ASP A 1 626 ? 30.06   19.888  41.856  1 50.85  ? 626 ASP A OD1   1 1 
ATOM   5005 O  OD2   . ASP A 1 626 ? 28.788  19.94   40.07   1 52.34  ? 626 ASP A OD2   1 1 
ATOM   5006 N  N     . LEU A 1 627 ? 32.925  17.8    37.673  1 43.41  ? 627 LEU A N     1 1 
ATOM   5007 C  CA    . LEU A 1 627 ? 33.709  16.75   37.05   1 43.02  ? 627 LEU A CA    1 1 
ATOM   5008 C  C     . LEU A 1 627 ? 34.308  17.24   35.727  1 43.11  ? 627 LEU A C     1 1 
ATOM   5009 O  O     . LEU A 1 627 ? 33.645  17.961  34.99   1 43.53  ? 627 LEU A O     1 1 
ATOM   5010 C  CB    . LEU A 1 627 ? 32.768  15.576  36.779  1 42.69  ? 627 LEU A CB    1 1 
ATOM   5011 C  CG    . LEU A 1 627 ? 33.372  14.391  36.079  1 43.67  ? 627 LEU A CG    1 1 
ATOM   5012 C  CD1   . LEU A 1 627 ? 34.441  13.741  36.939  1 44.14  ? 627 LEU A CD1   1 1 
ATOM   5013 C  CD2   . LEU A 1 627 ? 32.306  13.415  35.69   1 44.05  ? 627 LEU A CD2   1 1 
ATOM   5014 N  N     . LEU A 1 628 ? 35.56   16.881  35.435  1 42.55  ? 628 LEU A N     1 1 
ATOM   5015 C  CA    . LEU A 1 628 ? 36.18   17.221  34.157  1 42.46  ? 628 LEU A CA    1 1 
ATOM   5016 C  C     . LEU A 1 628 ? 36.522  15.92   33.482  1 42.52  ? 628 LEU A C     1 1 
ATOM   5017 O  O     . LEU A 1 628 ? 37.092  15.025  34.11   1 42.57  ? 628 LEU A O     1 1 
ATOM   5018 C  CB    . LEU A 1 628 ? 37.45   18.053  34.318  1 42.57  ? 628 LEU A CB    1 1 
ATOM   5019 C  CG    . LEU A 1 628 ? 37.273  19.463  34.815  1 44.16  ? 628 LEU A CG    1 1 
ATOM   5020 C  CD1   . LEU A 1 628 ? 38.624  20.114  35.056  1 44.86  ? 628 LEU A CD1   1 1 
ATOM   5021 C  CD2   . LEU A 1 628 ? 36.403  20.287  33.877  1 44.74  ? 628 LEU A CD2   1 1 
ATOM   5022 N  N     . ILE A 1 629 ? 36.147  15.788  32.217  1 42.37  ? 629 ILE A N     1 1 
ATOM   5023 C  CA    . ILE A 1 629 ? 36.427  14.57   31.478  1 42.79  ? 629 ILE A CA    1 1 
ATOM   5024 C  C     . ILE A 1 629 ? 37.424  14.882  30.39   1 43.13  ? 629 ILE A C     1 1 
ATOM   5025 O  O     . ILE A 1 629 ? 37.068  15.472  29.374  1 43.25  ? 629 ILE A O     1 1 
ATOM   5026 C  CB    . ILE A 1 629 ? 35.133  13.913  30.953  1 43.29  ? 629 ILE A CB    1 1 
ATOM   5027 C  CG1   . ILE A 1 629 ? 34.117  13.732  32.094  1 44.29  ? 629 ILE A CG1   1 1 
ATOM   5028 C  CG2   . ILE A 1 629 ? 35.445  12.58   30.3    1 43.57  ? 629 ILE A CG2   1 1 
ATOM   5029 C  CD1   . ILE A 1 629 ? 32.773  13.4    31.659  1 45.53  ? 629 ILE A CD1   1 1 
ATOM   5030 N  N     . ALA A 1 630 ? 38.694  14.567  30.643  1 43.19  ? 630 ALA A N     1 1 
ATOM   5031 C  CA    . ALA A 1 630 ? 39.738  14.822  29.671  1 43.9   ? 630 ALA A CA    1 1 
ATOM   5032 C  C     . ALA A 1 630 ? 39.83   13.607  28.792  1 44.76  ? 630 ALA A C     1 1 
ATOM   5033 O  O     . ALA A 1 630 ? 40.098  12.499  29.26   1 44.92  ? 630 ALA A O     1 1 
ATOM   5034 C  CB    . ALA A 1 630 ? 41.065  15.084  30.361  1 43.87  ? 630 ALA A CB    1 1 
ATOM   5035 N  N     . ILE A 1 631 ? 39.57   13.814  27.516  1 45.24  ? 631 ILE A N     1 1 
ATOM   5036 C  CA    . ILE A 1 631 ? 39.566  12.77   26.514  1 46.38  ? 631 ILE A CA    1 1 
ATOM   5037 C  C     . ILE A 1 631 ? 40.763  12.922  25.573  1 48.03  ? 631 ILE A C     1 1 
ATOM   5038 O  O     . ILE A 1 631 ? 41.091  14.039  25.176  1 48.26  ? 631 ILE A O     1 1 
ATOM   5039 C  CB    . ILE A 1 631 ? 38.215  12.916  25.783  1 46.36  ? 631 ILE A CB    1 1 
ATOM   5040 C  CG1   . ILE A 1 631 ? 37.093  12.438  26.68   1 47.53  ? 631 ILE A CG1   1 1 
ATOM   5041 C  CG2   . ILE A 1 631 ? 38.178  12.218  24.453  1 46.4   ? 631 ILE A CG2   1 1 
ATOM   5042 C  CD1   . ILE A 1 631 ? 35.791  12.957  26.287  1 49.25  ? 631 ILE A CD1   1 1 
ATOM   5043 N  N     . LYS A 1 632 ? 41.437  11.815  25.246  1 48.76  ? 632 LYS A N     1 1 
ATOM   5044 C  CA    . LYS A 1 632 ? 42.53   11.862  24.283  1 50.18  ? 632 LYS A CA    1 1 
ATOM   5045 C  C     . LYS A 1 632 ? 42.57   10.589  23.502  1 51.45  ? 632 LYS A C     1 1 
ATOM   5046 O  O     . LYS A 1 632 ? 42.32   9.522   24.062  1 51.93  ? 632 LYS A O     1 1 
ATOM   5047 C  CB    . LYS A 1 632 ? 43.882  12.181  24.919  1 52.43  ? 632 LYS A CB    1 1 
ATOM   5048 C  CG    . LYS A 1 632 ? 44.38   11.165  25.918  1 57.67  ? 632 LYS A CG    1 1 
ATOM   5049 C  CD    . LYS A 1 632 ? 45.863  11.383  26.181  1 63.78  ? 632 LYS A CD    1 1 
ATOM   5050 C  CE    . LYS A 1 632 ? 46.448  10.325  27.084  1 68.45  ? 632 LYS A CE    1 1 
ATOM   5051 N  NZ    . LYS A 1 632 ? 45.849  10.378  28.444  1 71.19  ? 632 LYS A NZ    1 1 
ATOM   5052 N  N     . ASN A 1 633 ? 42.825  10.688  22.197  1 51.81  ? 633 ASN A N     1 1 
ATOM   5053 C  CA    . ASN A 1 633 ? 42.87   9.488   21.373  1 52.54  ? 633 ASN A CA    1 1 
ATOM   5054 C  C     . ASN A 1 633 ? 44.267  8.938   21.281  1 53.11  ? 633 ASN A C     1 1 
ATOM   5055 O  O     . ASN A 1 633 ? 45.247  9.676   21.263  1 53.3   ? 633 ASN A O     1 1 
ATOM   5056 C  CB    . ASN A 1 633 ? 42.308  9.734   19.987  1 53.29  ? 633 ASN A CB    1 1 
ATOM   5057 C  CG    . ASN A 1 633 ? 43.047  10.803  19.259  1 55.31  ? 633 ASN A CG    1 1 
ATOM   5058 O  OD1   . ASN A 1 633 ? 42.964  11.975  19.599  1 55.91  ? 633 ASN A OD1   1 1 
ATOM   5059 N  ND2   . ASN A 1 633 ? 43.805  10.406  18.266  1 55.69  ? 633 ASN A ND2   1 1 
ATOM   5060 N  N     . GLN A 1 634 ? 44.341  7.629   21.238  1 53.21  ? 634 GLN A N     1 1 
ATOM   5061 C  CA    . GLN A 1 634 ? 45.552  6.86    21.055  1 53.89  ? 634 GLN A CA    1 1 
ATOM   5062 C  C     . GLN A 1 634 ? 45.389  6.293   19.644  1 54.41  ? 634 GLN A C     1 1 
ATOM   5063 O  O     . GLN A 1 634 ? 44.317  5.771   19.313  1 54.48  ? 634 GLN A O     1 1 
ATOM   5064 C  CB    . GLN A 1 634 ? 45.603  5.74    22.096  1 55.3   ? 634 GLN A CB    1 1 
ATOM   5065 C  CG    . GLN A 1 634 ? 46.782  4.803   21.954  1 58.09  ? 634 GLN A CG    1 1 
ATOM   5066 C  CD    . GLN A 1 634 ? 46.743  3.786   23.057  1 61.88  ? 634 GLN A CD    1 1 
ATOM   5067 O  OE1   . GLN A 1 634 ? 47.267  4.009   24.152  1 63.15  ? 634 GLN A OE1   1 1 
ATOM   5068 N  NE2   . GLN A 1 634 ? 46.093  2.659   22.803  1 62.39  ? 634 GLN A NE2   1 1 
ATOM   5069 N  N     . ASN A 1 635 ? 46.409  6.451   18.788  1 54.46  ? 635 ASN A N     1 1 
ATOM   5070 C  CA    . ASN A 1 635 ? 46.298  6.018   17.397  1 54.9   ? 635 ASN A CA    1 1 
ATOM   5071 C  C     . ASN A 1 635 ? 46.658  4.559   17.162  1 54.99  ? 635 ASN A C     1 1 
ATOM   5072 O  O     . ASN A 1 635 ? 46.033  3.911   16.319  1 54.95  ? 635 ASN A O     1 1 
ATOM   5073 C  CB    . ASN A 1 635 ? 47.092  6.933   16.488  1 56     ? 635 ASN A CB    1 1 
ATOM   5074 C  CG    . ASN A 1 635 ? 46.527  8.327   16.494  1 58.87  ? 635 ASN A CG    1 1 
ATOM   5075 O  OD1   . ASN A 1 635 ? 45.309  8.526   16.611  1 59.76  ? 635 ASN A OD1   1 1 
ATOM   5076 N  ND2   . ASN A 1 635 ? 47.398  9.323   16.383  1 59.55  ? 635 ASN A ND2   1 1 
ATOM   5077 N  N     . ASN A 1 636 ? 47.641  4.035   17.901  1 55.06  ? 636 ASN A N     1 1 
ATOM   5078 C  CA    . ASN A 1 636 ? 48.022  2.633   17.748  1 55.4   ? 636 ASN A CA    1 1 
ATOM   5079 C  C     . ASN A 1 636 ? 48.151  1.901   19.074  1 55.03  ? 636 ASN A C     1 1 
ATOM   5080 O  O     . ASN A 1 636 ? 49.13   2.096   19.791  1 54.97  ? 636 ASN A O     1 1 
ATOM   5081 C  CB    . ASN A 1 636 ? 49.277  2.48    16.896  1 56.73  ? 636 ASN A CB    1 1 
ATOM   5082 C  CG    . ASN A 1 636 ? 48.929  2.263   15.448  1 59.93  ? 636 ASN A CG    1 1 
ATOM   5083 O  OD1   . ASN A 1 636 ? 48.133  1.367   15.104  1 60.78  ? 636 ASN A OD1   1 1 
ATOM   5084 N  ND2   . ASN A 1 636 ? 49.489  3.099   14.578  1 60.47  ? 636 ASN A ND2   1 1 
ATOM   5085 N  N     . PRO A 1 637 ? 47.178  1.034   19.411  1 54.55  ? 637 PRO A N     1 1 
ATOM   5086 C  CA    . PRO A 1 637 ? 45.932  0.761   18.674  1 54.39  ? 637 PRO A CA    1 1 
ATOM   5087 C  C     . PRO A 1 637 ? 44.871  1.84    18.953  1 54.45  ? 637 PRO A C     1 1 
ATOM   5088 O  O     . PRO A 1 637 ? 44.938  2.506   19.998  1 54.79  ? 637 PRO A O     1 1 
ATOM   5089 C  CB    . PRO A 1 637 ? 45.526  -0.618  19.203  1 54.93  ? 637 PRO A CB    1 1 
ATOM   5090 C  CG    . PRO A 1 637 ? 46.015  -0.623  20.633  1 55.4   ? 637 PRO A CG    1 1 
ATOM   5091 C  CD    . PRO A 1 637 ? 47.234  0.284   20.684  1 53.97  ? 637 PRO A CD    1 1 
ATOM   5092 N  N     . GLN A 1 638 ? 43.921  2.062   18.018  1 53.69  ? 638 GLN A N     1 1 
ATOM   5093 C  CA    . GLN A 1 638 ? 42.899  3.098   18.215  1 53.07  ? 638 GLN A CA    1 1 
ATOM   5094 C  C     . GLN A 1 638 ? 42.115  2.898   19.522  1 52.21  ? 638 GLN A C     1 1 
ATOM   5095 O  O     . GLN A 1 638 ? 41.46   1.872   19.698  1 52.37  ? 638 GLN A O     1 1 
ATOM   5096 C  CB    . GLN A 1 638 ? 41.934  3.166   17.025  1 54.39  ? 638 GLN A CB    1 1 
ATOM   5097 C  CG    . GLN A 1 638 ? 42.466  3.873   15.786  1 56.53  ? 638 GLN A CG    1 1 
ATOM   5098 C  CD    . GLN A 1 638 ? 41.353  3.891   14.759  1 59.9   ? 638 GLN A CD    1 1 
ATOM   5099 O  OE1   . GLN A 1 638 ? 40.771  2.851   14.416  1 60.73  ? 638 GLN A OE1   1 1 
ATOM   5100 N  NE2   . GLN A 1 638 ? 40.983  5.073   14.291  1 60.35  ? 638 GLN A NE2   1 1 
ATOM   5101 N  N     . LYS A 1 639 ? 42.246  3.849   20.455  1 51.04  ? 639 LYS A N     1 1 
ATOM   5102 C  CA    . LYS A 1 639 ? 41.576  3.795   21.751  1 50.31  ? 639 LYS A CA    1 1 
ATOM   5103 C  C     . LYS A 1 639 ? 41.292  5.196   22.27   1 49.2   ? 639 LYS A C     1 1 
ATOM   5104 O  O     . LYS A 1 639 ? 42.067  6.116   22.021  1 49.48  ? 639 LYS A O     1 1 
ATOM   5105 C  CB    . LYS A 1 639 ? 42.462  3.079   22.776  1 52.13  ? 639 LYS A CB    1 1 
ATOM   5106 C  CG    . LYS A 1 639 ? 42.148  1.608   22.966  1 56.49  ? 639 LYS A CG    1 1 
ATOM   5107 C  CD    . LYS A 1 639 ? 43.156  0.969   23.906  1 61.07  ? 639 LYS A CD    1 1 
ATOM   5108 C  CE    . LYS A 1 639 ? 42.497  0.366   25.121  1 64.91  ? 639 LYS A CE    1 1 
ATOM   5109 N  NZ    . LYS A 1 639 ? 41.896  -0.958  24.822  1 67.49  ? 639 LYS A NZ    1 1 
ATOM   5110 N  N     . TRP A 1 640 ? 40.202  5.357   23.01   1 47.88  ? 640 TRP A N     1 1 
ATOM   5111 C  CA    . TRP A 1 640 ? 39.892  6.636   23.631  1 47.06  ? 640 TRP A CA    1 1 
ATOM   5112 C  C     . TRP A 1 640 ? 40.327  6.526   25.077  1 46.49  ? 640 TRP A C     1 1 
ATOM   5113 O  O     . TRP A 1 640 ? 39.783  5.711   25.82   1 46.9   ? 640 TRP A O     1 1 
ATOM   5114 C  CB    . TRP A 1 640 ? 38.393  6.963   23.556  1 46.61  ? 640 TRP A CB    1 1 
ATOM   5115 C  CG    . TRP A 1 640 ? 37.954  7.528   22.243  1 46.58  ? 640 TRP A CG    1 1 
ATOM   5116 C  CD1   . TRP A 1 640 ? 37.124  6.941   21.335  1 47.4   ? 640 TRP A CD1   1 1 
ATOM   5117 C  CD2   . TRP A 1 640 ? 38.323  8.798   21.689  1 46.42  ? 640 TRP A CD2   1 1 
ATOM   5118 N  NE1   . TRP A 1 640 ? 36.948  7.771   20.253  1 47.65  ? 640 TRP A NE1   1 1 
ATOM   5119 C  CE2   . TRP A 1 640 ? 37.678  8.916   20.444  1 47.23  ? 640 TRP A CE2   1 1 
ATOM   5120 C  CE3   . TRP A 1 640 ? 39.148  9.841   22.117  1 46.78  ? 640 TRP A CE3   1 1 
ATOM   5121 C  CZ2   . TRP A 1 640 ? 37.808  10.05   19.643  1 47.72  ? 640 TRP A CZ2   1 1 
ATOM   5122 C  CZ3   . TRP A 1 640 ? 39.257  10.968  21.33   1 47.53  ? 640 TRP A CZ3   1 1 
ATOM   5123 C  CH2   . TRP A 1 640 ? 38.599  11.062  20.106  1 47.65  ? 640 TRP A CH2   1 1 
ATOM   5124 N  N     . VAL A 1 641 ? 41.336  7.295   25.469  1 45.42  ? 641 VAL A N     1 1 
ATOM   5125 C  CA    . VAL A 1 641 ? 41.813  7.295   26.842  1 44.9   ? 641 VAL A CA    1 1 
ATOM   5126 C  C     . VAL A 1 641 ? 41.03   8.358   27.611  1 44.9   ? 641 VAL A C     1 1 
ATOM   5127 O  O     . VAL A 1 641 ? 41.061  9.55    27.27   1 45.02  ? 641 VAL A O     1 1 
ATOM   5128 C  CB    . VAL A 1 641 ? 43.336  7.492   26.934  1 44.99  ? 641 VAL A CB    1 1 
ATOM   5129 C  CG1   . VAL A 1 641 ? 43.809  7.347   28.371  1 45.32  ? 641 VAL A CG1   1 1 
ATOM   5130 C  CG2   . VAL A 1 641 ? 44.061  6.506   26.027  1 45.28  ? 641 VAL A CG2   1 1 
ATOM   5131 N  N     . ILE A 1 642 ? 40.277  7.912   28.618  1 44.35  ? 642 ILE A N     1 1 
ATOM   5132 C  CA    . ILE A 1 642 ? 39.429  8.809   29.39   1 44.05  ? 642 ILE A CA    1 1 
ATOM   5133 C  C     . ILE A 1 642 ? 39.99   9.034   30.789  1 43.88  ? 642 ILE A C     1 1 
ATOM   5134 O  O     . ILE A 1 642 ? 40.23   8.072   31.53   1 43.86  ? 642 ILE A O     1 1 
ATOM   5135 C  CB    . ILE A 1 642 ? 37.976  8.283   29.465  1 44.31  ? 642 ILE A CB    1 1 
ATOM   5136 C  CG1   . ILE A 1 642 ? 37.46   7.705   28.122  1 45.1   ? 642 ILE A CG1   1 1 
ATOM   5137 C  CG2   . ILE A 1 642 ? 37.06   9.353   30.002  1 44.84  ? 642 ILE A CG2   1 1 
ATOM   5138 C  CD1   . ILE A 1 642 ? 37.297  8.685   27.001  1 46.36  ? 642 ILE A CD1   1 1 
ATOM   5139 N  N     . LYS A 1 643 ? 40.193  10.306  31.15   1 43.56  ? 643 LYS A N     1 1 
ATOM   5140 C  CA    . LYS A 1 643 ? 40.676  10.674  32.472  1 44.03  ? 643 LYS A CA    1 1 
ATOM   5141 C  C     . LYS A 1 643 ? 39.605  11.511  33.166  1 44.39  ? 643 LYS A C     1 1 
ATOM   5142 O  O     . LYS A 1 643 ? 39.29   12.616  32.719  1 44.5   ? 643 LYS A O     1 1 
ATOM   5143 C  CB    . LYS A 1 643 ? 42.004  11.443  32.388  1 45.99  ? 643 LYS A CB    1 1 
ATOM   5144 C  CG    . LYS A 1 643 ? 42.617  11.738  33.759  1 50.32  ? 643 LYS A CG    1 1 
ATOM   5145 C  CD    . LYS A 1 643 ? 43.957  12.48   33.663  1 55.05  ? 643 LYS A CD    1 1 
ATOM   5146 C  CE    . LYS A 1 643 ? 44.631  12.666  35.009  1 58.4   ? 643 LYS A CE    1 1 
ATOM   5147 N  NZ    . LYS A 1 643 ? 45.95   13.343  34.886  1 59.86  ? 643 LYS A NZ    1 1 
ATOM   5148 N  N     . PHE A 1 644 ? 39.011  10.962  34.234  1 44.37  ? 644 PHE A N     1 1 
ATOM   5149 C  CA    . PHE A 1 644 ? 37.957  11.634  34.994  1 44.54  ? 644 PHE A CA    1 1 
ATOM   5150 C  C     . PHE A 1 644 ? 38.552  12.361  36.178  1 44.57  ? 644 PHE A C     1 1 
ATOM   5151 O  O     . PHE A 1 644 ? 39.101  11.723  37.074  1 44.77  ? 644 PHE A O     1 1 
ATOM   5152 C  CB    . PHE A 1 644 ? 36.936  10.613  35.517  1 44.41  ? 644 PHE A CB    1 1 
ATOM   5153 C  CG    . PHE A 1 644 ? 36.138  9.899   34.457  1 44.99  ? 644 PHE A CG    1 1 
ATOM   5154 C  CD1   . PHE A 1 644 ? 35.052  10.509  33.857  1 45.92  ? 644 PHE A CD1   1 1 
ATOM   5155 C  CD2   . PHE A 1 644 ? 36.458  8.611   34.078  1 45.61  ? 644 PHE A CD2   1 1 
ATOM   5156 C  CE1   . PHE A 1 644 ? 34.311  9.845   32.893  1 46.63  ? 644 PHE A CE1   1 1 
ATOM   5157 C  CE2   . PHE A 1 644 ? 35.714  7.952   33.114  1 46.32  ? 644 PHE A CE2   1 1 
ATOM   5158 C  CZ    . PHE A 1 644 ? 34.641  8.569   32.535  1 46.23  ? 644 PHE A CZ    1 1 
ATOM   5159 N  N     . LYS A 1 645 ? 38.435  13.682  36.197  1 44.25  ? 645 LYS A N     1 1 
ATOM   5160 C  CA    . LYS A 1 645 ? 38.947  14.478  37.299  1 44.57  ? 645 LYS A CA    1 1 
ATOM   5161 C  C     . LYS A 1 645 ? 37.802  15.054  38.126  1 44.89  ? 645 LYS A C     1 1 
ATOM   5162 O  O     . LYS A 1 645 ? 37.185  16.034  37.721  1 45.04  ? 645 LYS A O     1 1 
ATOM   5163 C  CB    . LYS A 1 645 ? 39.828  15.611  36.776  1 46.24  ? 645 LYS A CB    1 1 
ATOM   5164 C  CG    . LYS A 1 645 ? 41.254  15.197  36.463  1 50.74  ? 645 LYS A CG    1 1 
ATOM   5165 C  CD    . LYS A 1 645 ? 42.109  15.017  37.724  1 55.95  ? 645 LYS A CD    1 1 
ATOM   5166 C  CE    . LYS A 1 645 ? 42.157  16.236  38.62   1 60.23  ? 645 LYS A CE    1 1 
ATOM   5167 N  NZ    . LYS A 1 645 ? 43.081  16.041  39.773  1 62.48  ? 645 LYS A NZ    1 1 
ATOM   5168 N  N     . PRO A 1 646 ? 37.501  14.467  39.294  1 44.66  ? 646 PRO A N     1 1 
ATOM   5169 C  CA    . PRO A 1 646 ? 36.426  15.02   40.13   1 44.61  ? 646 PRO A CA    1 1 
ATOM   5170 C  C     . PRO A 1 646 ? 36.882  16.229  40.95   1 44.48  ? 646 PRO A C     1 1 
ATOM   5171 O  O     . PRO A 1 646 ? 38.022  16.264  41.404  1 44.35  ? 646 PRO A O     1 1 
ATOM   5172 C  CB    . PRO A 1 646 ? 36.064  13.846  41.037  1 45.42  ? 646 PRO A CB    1 1 
ATOM   5173 C  CG    . PRO A 1 646 ? 37.322  13.061  41.162  1 45.81  ? 646 PRO A CG    1 1 
ATOM   5174 C  CD    . PRO A 1 646 ? 38.117  13.27   39.903  1 44.22  ? 646 PRO A CD    1 1 
ATOM   5175 N  N     . LYS A 1 647 ? 36.002  17.21   41.151  1 44.38  ? 647 LYS A N     1 1 
ATOM   5176 C  CA    . LYS A 1 647 ? 36.331  18.388  41.963  1 44.83  ? 647 LYS A CA    1 1 
ATOM   5177 C  C     . LYS A 1 647 ? 36.058  18.13   43.447  1 45.01  ? 647 LYS A C     1 1 
ATOM   5178 O  O     . LYS A 1 647 ? 36.745  18.675  44.313  1 45.03  ? 647 LYS A O     1 1 
ATOM   5179 C  CB    . LYS A 1 647 ? 35.51   19.603  41.517  1 46.68  ? 647 LYS A CB    1 1 
ATOM   5180 C  CG    . LYS A 1 647 ? 35.88   20.901  42.239  1 50.61  ? 647 LYS A CG    1 1 
ATOM   5181 C  CD    . LYS A 1 647 ? 34.903  22.054  41.953  1 55.29  ? 647 LYS A CD    1 1 
ATOM   5182 C  CE    . LYS A 1 647 ? 33.466  21.723  42.321  1 59.01  ? 647 LYS A CE    1 1 
ATOM   5183 N  NZ    . LYS A 1 647 ? 32.571  22.898  42.178  1 61.19  ? 647 LYS A NZ    1 1 
ATOM   5184 N  N     . ASN A 1 648 ? 35.042  17.318  43.739  1 44.9   ? 648 ASN A N     1 1 
ATOM   5185 C  CA    . ASN A 1 648 ? 34.657  17.031  45.107  1 45.43  ? 648 ASN A CA    1 1 
ATOM   5186 C  C     . ASN A 1 648 ? 34.358  15.536  45.334  1 45.67  ? 648 ASN A C     1 1 
ATOM   5187 O  O     . ASN A 1 648 ? 34.479  14.726  44.417  1 45.79  ? 648 ASN A O     1 1 
ATOM   5188 C  CB    . ASN A 1 648 ? 33.473  17.931  45.496  1 46.79  ? 648 ASN A CB    1 1 
ATOM   5189 C  CG    . ASN A 1 648 ? 32.348  17.916  44.492  1 49.93  ? 648 ASN A CG    1 1 
ATOM   5190 O  OD1   . ASN A 1 648 ? 31.909  16.856  44.028  1 50.85  ? 648 ASN A OD1   1 1 
ATOM   5191 N  ND2   . ASN A 1 648 ? 31.876  19.1    44.125  1 50.5   ? 648 ASN A ND2   1 1 
ATOM   5192 N  N     . THR A 1 649 ? 33.976  15.184  46.566  1 45.65  ? 649 THR A N     1 1 
ATOM   5193 C  CA    . THR A 1 649 ? 33.642  13.834  47.018  1 46.05  ? 649 THR A CA    1 1 
ATOM   5194 C  C     . THR A 1 649 ? 32.425  13.212  46.337  1 46.05  ? 649 THR A C     1 1 
ATOM   5195 O  O     . THR A 1 649 ? 32.417  12.001  46.108  1 46.08  ? 649 THR A O     1 1 
ATOM   5196 C  CB    . THR A 1 649 ? 33.474  13.847  48.53   1 47.43  ? 649 THR A CB    1 1 
ATOM   5197 O  OG1   . THR A 1 649 ? 32.583  14.916  48.886  1 48.37  ? 649 THR A OG1   1 1 
ATOM   5198 C  CG2   . THR A 1 649 ? 34.812  14.009  49.246  1 47.79  ? 649 THR A CG2   1 1 
ATOM   5199 N  N     . ILE A 1 650 ? 31.402  14.021  46.016  1 45.93  ? 650 ILE A N     1 1 
ATOM   5200 C  CA    . ILE A 1 650 ? 30.205  13.512  45.333  1 46.31  ? 650 ILE A CA    1 1 
ATOM   5201 C  C     . ILE A 1 650 ? 30.583  13.076  43.923  1 46.04  ? 650 ILE A C     1 1 
ATOM   5202 O  O     . ILE A 1 650 ? 30.227  11.976  43.494  1 46.24  ? 650 ILE A O     1 1 
ATOM   5203 C  CB    . ILE A 1 650 ? 29.048  14.554  45.321  1 47.1   ? 650 ILE A CB    1 1 
ATOM   5204 C  CG1   . ILE A 1 650 ? 28.481  14.79   46.74   1 48.29  ? 650 ILE A CG1   1 1 
ATOM   5205 C  CG2   . ILE A 1 650 ? 27.935  14.157  44.331  1 47.46  ? 650 ILE A CG2   1 1 
ATOM   5206 C  CD1   . ILE A 1 650 ? 27.51   13.656  47.292  1 49.53  ? 650 ILE A CD1   1 1 
ATOM   5207 N  N     . ALA A 1 651 ? 31.344  13.919  43.22   1 45.35  ? 651 ALA A N     1 1 
ATOM   5208 C  CA    . ALA A 1 651 ? 31.801  13.592  41.881  1 45.27  ? 651 ALA A CA    1 1 
ATOM   5209 C  C     . ALA A 1 651 ? 32.721  12.376  41.902  1 45.09  ? 651 ALA A C     1 1 
ATOM   5210 O  O     . ALA A 1 651 ? 32.662  11.582  40.977  1 45.63  ? 651 ALA A O     1 1 
ATOM   5211 C  CB    . ALA A 1 651 ? 32.512  14.775  41.27   1 45.49  ? 651 ALA A CB    1 1 
ATOM   5212 N  N     . GLU A 1 652 ? 33.509  12.179  42.972  1 44.26  ? 652 GLU A N     1 1 
ATOM   5213 C  CA    . GLU A 1 652 ? 34.368  11.007  43.084  1 44.18  ? 652 GLU A CA    1 1 
ATOM   5214 C  C     . GLU A 1 652 ? 33.535  9.723   43.189  1 43.38  ? 652 GLU A C     1 1 
ATOM   5215 O  O     . GLU A 1 652 ? 33.911  8.704   42.613  1 43.25  ? 652 GLU A O     1 1 
ATOM   5216 C  CB    . GLU A 1 652 ? 35.321  11.134  44.27   1 47.14  ? 652 GLU A CB    1 1 
ATOM   5217 C  CG    . GLU A 1 652 ? 36.31   9.984   44.34   1 53.53  ? 652 GLU A CG    1 1 
ATOM   5218 C  CD    . GLU A 1 652 ? 37.311  10.086  45.47   1 62.53  ? 652 GLU A CD    1 1 
ATOM   5219 O  OE1   . GLU A 1 652 ? 37.607  11.228  45.899  1 64.81  ? 652 GLU A OE1   1 1 
ATOM   5220 O  OE2   . GLU A 1 652 ? 37.804  9.025   45.921  1 65.12  ? 652 GLU A OE2   1 1 
ATOM   5221 N  N     . LYS A 1 653 ? 32.382  9.782   43.87   1 42.7   ? 653 LYS A N     1 1 
ATOM   5222 C  CA    . LYS A 1 653 ? 31.48   8.633   43.952  1 42.65  ? 653 LYS A CA    1 1 
ATOM   5223 C  C     . LYS A 1 653 ? 30.905  8.295   42.566  1 42.47  ? 653 LYS A C     1 1 
ATOM   5224 O  O     . LYS A 1 653 ? 30.729  7.121   42.24   1 42.38  ? 653 LYS A O     1 1 
ATOM   5225 C  CB    . LYS A 1 653 ? 30.359  8.88    44.973  1 44.06  ? 653 LYS A CB    1 1 
ATOM   5226 C  CG    . LYS A 1 653 ? 30.85   8.837   46.413  1 47.34  ? 653 LYS A CG    1 1 
ATOM   5227 C  CD    . LYS A 1 653 ? 29.739  8.449   47.368  1 50.89  ? 653 LYS A CD    1 1 
ATOM   5228 C  CE    . LYS A 1 653 ? 30.253  7.7     48.572  1 54.03  ? 653 LYS A CE    1 1 
ATOM   5229 N  NZ    . LYS A 1 653 ? 31.011  8.584   49.49   1 56.07  ? 653 LYS A NZ    1 1 
ATOM   5230 N  N     . LEU A 1 654 ? 30.662  9.323   41.737  1 42.28  ? 654 LEU A N     1 1 
ATOM   5231 C  CA    . LEU A 1 654 ? 30.184  9.15    40.371  1 42.65  ? 654 LEU A CA    1 1 
ATOM   5232 C  C     . LEU A 1 654 ? 31.276  8.489   39.528  1 43.13  ? 654 LEU A C     1 1 
ATOM   5233 O  O     . LEU A 1 654 ? 30.985  7.548   38.791  1 43.12  ? 654 LEU A O     1 1 
ATOM   5234 C  CB    . LEU A 1 654 ? 29.776  10.501  39.763  1 42.58  ? 654 LEU A CB    1 1 
ATOM   5235 C  CG    . LEU A 1 654 ? 29.401  10.507  38.285  1 43.64  ? 654 LEU A CG    1 1 
ATOM   5236 C  CD1   . LEU A 1 654 ? 28.247  9.581   38.007  1 43.92  ? 654 LEU A CD1   1 1 
ATOM   5237 C  CD2   . LEU A 1 654 ? 29.012  11.889  37.847  1 44.41  ? 654 LEU A CD2   1 1 
ATOM   5238 N  N     . VAL A 1 655 ? 32.538  8.935   39.684  1 43.18  ? 655 VAL A N     1 1 
ATOM   5239 C  CA    . VAL A 1 655 ? 33.692  8.378   38.98   1 43.68  ? 655 VAL A CA    1 1 
ATOM   5240 C  C     . VAL A 1 655 ? 33.823  6.882   39.285  1 44.46  ? 655 VAL A C     1 1 
ATOM   5241 O  O     . VAL A 1 655 ? 33.97   6.091   38.357  1 44.53  ? 655 VAL A O     1 1 
ATOM   5242 C  CB    . VAL A 1 655 ? 34.981  9.175   39.299  1 44.26  ? 655 VAL A CB    1 1 
ATOM   5243 C  CG1   . VAL A 1 655 ? 36.23   8.432   38.847  1 44.97  ? 655 VAL A CG1   1 1 
ATOM   5244 C  CG2   . VAL A 1 655 ? 34.93   10.557  38.667  1 44.49  ? 655 VAL A CG2   1 1 
ATOM   5245 N  N     . ASN A 1 656 ? 33.661  6.487   40.565  1 44.93  ? 656 ASN A N     1 1 
ATOM   5246 C  CA    . ASN A 1 656 ? 33.709  5.076   40.982  1 45.54  ? 656 ASN A CA    1 1 
ATOM   5247 C  C     . ASN A 1 656 ? 32.574  4.281   40.371  1 44.7   ? 656 ASN A C     1 1 
ATOM   5248 O  O     . ASN A 1 656 ? 32.779  3.128   40.007  1 44.38  ? 656 ASN A O     1 1 
ATOM   5249 C  CB    . ASN A 1 656 ? 33.684  4.93    42.507  1 47.99  ? 656 ASN A CB    1 1 
ATOM   5250 C  CG    . ASN A 1 656 ? 34.949  5.417   43.179  1 53.38  ? 656 ASN A CG    1 1 
ATOM   5251 O  OD1   . ASN A 1 656 ? 36.038  5.449   42.578  1 54.91  ? 656 ASN A OD1   1 1 
ATOM   5252 N  ND2   . ASN A 1 656 ? 34.833  5.817   44.444  1 54.86  ? 656 ASN A ND2   1 1 
ATOM   5253 N  N     . TYR A 1 657 ? 31.382  4.897   40.258  1 44.31  ? 657 TYR A N     1 1 
ATOM   5254 C  CA    . TYR A 1 657 ? 30.198  4.285   39.656  1 44.55  ? 657 TYR A CA    1 1 
ATOM   5255 C  C     . TYR A 1 657 ? 30.453  4.018   38.17   1 45.13  ? 657 TYR A C     1 1 
ATOM   5256 O  O     . TYR A 1 657 ? 30.133  2.935   37.681  1 45.05  ? 657 TYR A O     1 1 
ATOM   5257 C  CB    . TYR A 1 657 ? 28.955  5.185   39.849  1 44.21  ? 657 TYR A CB    1 1 
ATOM   5258 C  CG    . TYR A 1 657 ? 27.678  4.657   39.221  1 44.54  ? 657 TYR A CG    1 1 
ATOM   5259 C  CD1   . TYR A 1 657 ? 26.843  3.791   39.914  1 45.15  ? 657 TYR A CD1   1 1 
ATOM   5260 C  CD2   . TYR A 1 657 ? 27.276  5.071   37.961  1 45.29  ? 657 TYR A CD2   1 1 
ATOM   5261 C  CE1   . TYR A 1 657 ? 25.665  3.312   39.348  1 45.86  ? 657 TYR A CE1   1 1 
ATOM   5262 C  CE2   . TYR A 1 657 ? 26.101  4.6     37.385  1 46.05  ? 657 TYR A CE2   1 1 
ATOM   5263 C  CZ    . TYR A 1 657 ? 25.301  3.712   38.077  1 46.74  ? 657 TYR A CZ    1 1 
ATOM   5264 O  OH    . TYR A 1 657 ? 24.135  3.253   37.508  1 48.05  ? 657 TYR A OH    1 1 
ATOM   5265 N  N     . ILE A 1 658 ? 31.045  4.999   37.458  1 45.39  ? 658 ILE A N     1 1 
ATOM   5266 C  CA    . ILE A 1 658 ? 31.365  4.867   36.035  1 45.91  ? 658 ILE A CA    1 1 
ATOM   5267 C  C     . ILE A 1 658 ? 32.415  3.779   35.816  1 46.56  ? 658 ILE A C     1 1 
ATOM   5268 O  O     . ILE A 1 658 ? 32.253  2.937   34.935  1 46.7   ? 658 ILE A O     1 1 
ATOM   5269 C  CB    . ILE A 1 658 ? 31.819  6.216   35.447  1 46.25  ? 658 ILE A CB    1 1 
ATOM   5270 C  CG1   . ILE A 1 658 ? 30.708  7.254   35.533  1 47.17  ? 658 ILE A CG1   1 1 
ATOM   5271 C  CG2   . ILE A 1 658 ? 32.293  6.055   34.013  1 46.7   ? 658 ILE A CG2   1 1 
ATOM   5272 C  CD1   . ILE A 1 658 ? 31.204  8.65    35.328  1 48.73  ? 658 ILE A CD1   1 1 
ATOM   5273 N  N     . LYS A 1 659 ? 33.466  3.77    36.64   1 46.79  ? 659 LYS A N     1 1 
ATOM   5274 C  CA    . LYS A 1 659 ? 34.521  2.766   36.539  1 47.6   ? 659 LYS A CA    1 1 
ATOM   5275 C  C     . LYS A 1 659 ? 33.991  1.353   36.792  1 48.45  ? 659 LYS A C     1 1 
ATOM   5276 O  O     . LYS A 1 659 ? 34.325  0.431   36.051  1 48.53  ? 659 LYS A O     1 1 
ATOM   5277 C  CB    . LYS A 1 659 ? 35.671  3.099   37.496  1 49.11  ? 659 LYS A CB    1 1 
ATOM   5278 C  CG    . LYS A 1 659 ? 36.539  4.235   36.996  1 52.73  ? 659 LYS A CG    1 1 
ATOM   5279 C  CD    . LYS A 1 659 ? 37.292  4.922   38.124  1 57.37  ? 659 LYS A CD    1 1 
ATOM   5280 C  CE    . LYS A 1 659 ? 38.554  4.205   38.525  1 61.52  ? 659 LYS A CE    1 1 
ATOM   5281 N  NZ    . LYS A 1 659 ? 39.515  5.124   39.188  1 63.93  ? 659 LYS A NZ    1 1 
ATOM   5282 N  N     . LEU A 1 660 ? 33.146  1.189   37.815  1 48.96  ? 660 LEU A N     1 1 
ATOM   5283 C  CA    . LEU A 1 660 ? 32.555  -0.104  38.153  1 50.1   ? 660 LEU A CA    1 1 
ATOM   5284 C  C     . LEU A 1 660 ? 31.581  -0.573  37.071  1 50.88  ? 660 LEU A C     1 1 
ATOM   5285 O  O     . LEU A 1 660 ? 31.514  -1.766  36.775  1 51.15  ? 660 LEU A O     1 1 
ATOM   5286 C  CB    . LEU A 1 660 ? 31.804  0.004   39.484  1 50.57  ? 660 LEU A CB    1 1 
ATOM   5287 C  CG    . LEU A 1 660 ? 32.455  -0.653  40.691  1 52.2   ? 660 LEU A CG    1 1 
ATOM   5288 C  CD1   . LEU A 1 660 ? 33.832  -0.063  40.976  1 52.42  ? 660 LEU A CD1   1 1 
ATOM   5289 C  CD2   . LEU A 1 660 ? 31.541  -0.551  41.909  1 53.06  ? 660 LEU A CD2   1 1 
ATOM   5290 N  N     . ASN A 1 661 ? 30.822  0.366   36.491  1 51.03  ? 661 ASN A N     1 1 
ATOM   5291 C  CA    . ASN A 1 661 ? 29.847  0.054   35.456  1 51.73  ? 661 ASN A CA    1 1 
ATOM   5292 C  C     . ASN A 1 661 ? 30.369  0.212   34.033  1 52.24  ? 661 ASN A C     1 1 
ATOM   5293 O  O     . ASN A 1 661 ? 29.568  0.266   33.103  1 52.48  ? 661 ASN A O     1 1 
ATOM   5294 C  CB    . ASN A 1 661 ? 28.575  0.863   35.656  1 52.93  ? 661 ASN A CB    1 1 
ATOM   5295 C  CG    . ASN A 1 661 ? 27.768  0.39    36.828  1 55.99  ? 661 ASN A CG    1 1 
ATOM   5296 O  OD1   . ASN A 1 661 ? 27.712  1.041   37.874  1 57.07  ? 661 ASN A OD1   1 1 
ATOM   5297 N  ND2   . ASN A 1 661 ? 27.143  -0.769  36.684  1 56.56  ? 661 ASN A ND2   1 1 
ATOM   5298 N  N     . PHE A 1 662 ? 31.698  0.262   33.843  1 52.39  ? 662 PHE A N     1 1 
ATOM   5299 C  CA    . PHE A 1 662 ? 32.271  0.357   32.499  1 53.04  ? 662 PHE A CA    1 1 
ATOM   5300 C  C     . PHE A 1 662 ? 32.373  -1.052  31.911  1 53.74  ? 662 PHE A C     1 1 
ATOM   5301 O  O     . PHE A 1 662 ? 33.446  -1.52   31.527  1 53.91  ? 662 PHE A O     1 1 
ATOM   5302 C  CB    . PHE A 1 662 ? 33.638  1.052   32.513  1 52.75  ? 662 PHE A CB    1 1 
ATOM   5303 C  CG    . PHE A 1 662 ? 33.854  1.865   31.264  1 53.19  ? 662 PHE A CG    1 1 
ATOM   5304 C  CD1   . PHE A 1 662 ? 34.365  1.282   30.12   1 53.96  ? 662 PHE A CD1   1 1 
ATOM   5305 C  CD2   . PHE A 1 662 ? 33.49   3.197   31.215  1 53.88  ? 662 PHE A CD2   1 1 
ATOM   5306 C  CE1   . PHE A 1 662 ? 34.522  2.021   28.961  1 54.75  ? 662 PHE A CE1   1 1 
ATOM   5307 C  CE2   . PHE A 1 662 ? 33.655  3.936   30.053  1 54.56  ? 662 PHE A CE2   1 1 
ATOM   5308 C  CZ    . PHE A 1 662 ? 34.171  3.345   28.934  1 54.48  ? 662 PHE A CZ    1 1 
ATOM   5309 N  N     . LYS A 1 663 ? 31.236  -1.725  31.882  1 53.88  ? 663 LYS A N     1 1 
ATOM   5310 C  CA    . LYS A 1 663 ? 31.066  -3.094  31.433  1 54.71  ? 663 LYS A CA    1 1 
ATOM   5311 C  C     . LYS A 1 663 ? 29.731  -3.156  30.682  1 55.68  ? 663 LYS A C     1 1 
ATOM   5312 O  O     . LYS A 1 663 ? 28.762  -2.485  31.068  1 55.71  ? 663 LYS A O     1 1 
ATOM   5313 C  CB    . LYS A 1 663 ? 31.059  -4.033  32.664  1 55.9   ? 663 LYS A CB    1 1 
ATOM   5314 C  CG    . LYS A 1 663 ? 30.761  -5.497  32.372  1 58.8   ? 663 LYS A CG    1 1 
ATOM   5315 C  CD    . LYS A 1 663 ? 30.571  -6.285  33.658  1 62.2   ? 663 LYS A CD    1 1 
ATOM   5316 C  CE    . LYS A 1 663 ? 30      -7.661  33.401  1 65.24  ? 663 LYS A CE    1 1 
ATOM   5317 N  NZ    . LYS A 1 663 ? 29.999  -8.505  34.628  1 66.84  ? 663 LYS A NZ    1 1 
ATOM   5318 N  N     . SER A 1 664 ? 29.688  -3.928  29.591  1 56.11  ? 664 SER A N     1 1 
ATOM   5319 C  CA    . SER A 1 664 ? 28.472  -4.044  28.805  1 56.92  ? 664 SER A CA    1 1 
ATOM   5320 C  C     . SER A 1 664 ? 28.431  -5.323  28.018  1 57.13  ? 664 SER A C     1 1 
ATOM   5321 O  O     . SER A 1 664 ? 29.454  -5.789  27.524  1 57.36  ? 664 SER A O     1 1 
ATOM   5322 C  CB    . SER A 1 664 ? 28.336  -2.864  27.847  1 58.64  ? 664 SER A CB    1 1 
ATOM   5323 O  OG    . SER A 1 664 ? 27.124  -2.934  27.111  1 61.31  ? 664 SER A OG    1 1 
ATOM   5324 N  N     . ASN A 1 665 ? 27.237  -5.869  27.875  1 56.98  ? 665 ASN A N     1 1 
ATOM   5325 C  CA    . ASN A 1 665 ? 26.996  -7.057  27.057  1 57.39  ? 665 ASN A CA    1 1 
ATOM   5326 C  C     . ASN A 1 665 ? 26.811  -6.659  25.571  1 57.53  ? 665 ASN A C     1 1 
ATOM   5327 O  O     . ASN A 1 665 ? 27.011  -7.485  24.681  1 57.57  ? 665 ASN A O     1 1 
ATOM   5328 C  CB    . ASN A 1 665 ? 25.745  -7.821  27.532  1 58.64  ? 665 ASN A CB    1 1 
ATOM   5329 C  CG    . ASN A 1 665 ? 25.225  -7.451  28.902  1 61.87  ? 665 ASN A CG    1 1 
ATOM   5330 O  OD1   . ASN A 1 665 ? 25.625  -8.033  29.915  1 63     ? 665 ASN A OD1   1 1 
ATOM   5331 N  ND2   . ASN A 1 665 ? 24.334  -6.463  28.955  1 62.46  ? 665 ASN A ND2   1 1 
ATOM   5332 N  N     . ILE A 1 666 ? 26.425  -5.398  25.31   1 57.38  ? 666 ILE A N     1 1 
ATOM   5333 C  CA    . ILE A 1 666 ? 26.164  -4.883  23.979  1 57.68  ? 666 ILE A CA    1 1 
ATOM   5334 C  C     . ILE A 1 666 ? 27.305  -4.02   23.444  1 57.72  ? 666 ILE A C     1 1 
ATOM   5335 O  O     . ILE A 1 666 ? 27.754  -4.243  22.324  1 57.9   ? 666 ILE A O     1 1 
ATOM   5336 C  CB    . ILE A 1 666 ? 24.826  -4.127  23.994  1 58.23  ? 666 ILE A CB    1 1 
ATOM   5337 C  CG1   . ILE A 1 666 ? 23.674  -5.047  24.462  1 59.22  ? 666 ILE A CG1   1 1 
ATOM   5338 C  CG2   . ILE A 1 666 ? 24.543  -3.516  22.632  1 58.71  ? 666 ILE A CG2   1 1 
ATOM   5339 C  CD1   . ILE A 1 666 ? 23.23   -4.856  25.944  1 60.46  ? 666 ILE A CD1   1 1 
ATOM   5340 N  N     . PHE A 1 667 ? 27.783  -3.054  24.234  1 57.52  ? 667 PHE A N     1 1 
ATOM   5341 C  CA    . PHE A 1 667 ? 28.861  -2.176  23.801  1 57.97  ? 667 PHE A CA    1 1 
ATOM   5342 C  C     . PHE A 1 667 ? 30.235  -2.771  24.025  1 59.02  ? 667 PHE A C     1 1 
ATOM   5343 O  O     . PHE A 1 667 ? 30.524  -3.298  25.098  1 59.11  ? 667 PHE A O     1 1 
ATOM   5344 C  CB    . PHE A 1 667 ? 28.78   -0.821  24.501  1 57.63  ? 667 PHE A CB    1 1 
ATOM   5345 C  CG    . PHE A 1 667 ? 29.308  0.319   23.668  1 58.02  ? 667 PHE A CG    1 1 
ATOM   5346 C  CD1   . PHE A 1 667 ? 30.664  0.578   23.596  1 58.74  ? 667 PHE A CD1   1 1 
ATOM   5347 C  CD2   . PHE A 1 667 ? 28.445  1.152   22.984  1 58.75  ? 667 PHE A CD2   1 1 
ATOM   5348 C  CE1   . PHE A 1 667 ? 31.148  1.625   22.826  1 59.43  ? 667 PHE A CE1   1 1 
ATOM   5349 C  CE2   . PHE A 1 667 ? 28.931  2.202   22.22   1 59.53  ? 667 PHE A CE2   1 1 
ATOM   5350 C  CZ    . PHE A 1 667 ? 30.279  2.437   22.151  1 59.27  ? 667 PHE A CZ    1 1 
ATOM   5351 N  N     . ASP A 1 668 ? 31.097  -2.64   23.013  1 59.58  ? 668 ASP A N     1 1 
ATOM   5352 C  CA    . ASP A 1 668 ? 32.475  -3.102  23.037  1 60.49  ? 668 ASP A CA    1 1 
ATOM   5353 C  C     . ASP A 1 668 ? 33.285  -2.099  23.824  1 61.04  ? 668 ASP A C     1 1 
ATOM   5354 O  O     . ASP A 1 668 ? 33.755  -1.12   23.256  1 61.05  ? 668 ASP A O     1 1 
ATOM   5355 C  CB    . ASP A 1 668 ? 33.018  -3.188  21.6    1 62.21  ? 668 ASP A CB    1 1 
ATOM   5356 C  CG    . ASP A 1 668 ? 34.247  -4.055  21.444  1 66.43  ? 668 ASP A CG    1 1 
ATOM   5357 O  OD1   . ASP A 1 668 ? 35.139  -3.985  22.322  1 67.49  ? 668 ASP A OD1   1 1 
ATOM   5358 O  OD2   . ASP A 1 668 ? 34.324  -4.797  20.439  1 67.93  ? 668 ASP A OD2   1 1 
ATOM   5359 N  N     . THR A 1 669 ? 33.468  -2.342  25.121  1 61.49  ? 669 THR A N     1 1 
ATOM   5360 C  CA    . THR A 1 669 ? 34.25   -1.438  25.964  1 62.53  ? 669 THR A CA    1 1 
ATOM   5361 C  C     . THR A 1 669 ? 35.77   -1.479  25.679  1 63.32  ? 669 THR A C     1 1 
ATOM   5362 O  O     . THR A 1 669 ? 36.504  -0.645  26.211  1 63.26  ? 669 THR A O     1 1 
ATOM   5363 C  CB    . THR A 1 669 ? 33.933  -1.684  27.444  1 64.01  ? 669 THR A CB    1 1 
ATOM   5364 O  OG1   . THR A 1 669 ? 34.387  -2.985  27.818  1 65.06  ? 669 THR A OG1   1 1 
ATOM   5365 C  CG2   . THR A 1 669 ? 32.446  -1.564  27.744  1 64.51  ? 669 THR A CG2   1 1 
ATOM   5366 N  N     . GLY A 1 670 ? 36.21   -2.417  24.832  1 63.94  ? 670 GLY A N     1 1 
ATOM   5367 C  CA    . GLY A 1 670 ? 37.602  -2.603  24.435  1 65.11  ? 670 GLY A CA    1 1 
ATOM   5368 C  C     . GLY A 1 670 ? 38.217  -1.442  23.676  1 66.1   ? 670 GLY A C     1 1 
ATOM   5369 O  O     . GLY A 1 670 ? 39.443  -1.347  23.554  1 66.26  ? 670 GLY A O     1 1 
ATOM   5370 N  N     . PHE A 1 671 ? 37.374  -0.545  23.162  1 66.46  ? 671 PHE A N     1 1 
ATOM   5371 C  CA    . PHE A 1 671 ? 37.847  0.647   22.469  1 67.3   ? 671 PHE A CA    1 1 
ATOM   5372 C  C     . PHE A 1 671 ? 38.205  1.802   23.454  1 68     ? 671 PHE A C     1 1 
ATOM   5373 O  O     . PHE A 1 671 ? 38.709  2.838   23.032  1 67.93  ? 671 PHE A O     1 1 
ATOM   5374 C  CB    . PHE A 1 671 ? 36.779  1.099   21.472  1 67.31  ? 671 PHE A CB    1 1 
ATOM   5375 C  CG    . PHE A 1 671 ? 37.342  1.75    20.238  1 68.05  ? 671 PHE A CG    1 1 
ATOM   5376 C  CD1   . PHE A 1 671 ? 37.783  0.986   19.175  1 68.76  ? 671 PHE A CD1   1 1 
ATOM   5377 C  CD2   . PHE A 1 671 ? 37.405  3.126   20.13   1 69.05  ? 671 PHE A CD2   1 1 
ATOM   5378 C  CE1   . PHE A 1 671 ? 38.299  1.586   18.038  1 69.56  ? 671 PHE A CE1   1 1 
ATOM   5379 C  CE2   . PHE A 1 671 ? 37.924  3.724   18.995  1 69.79  ? 671 PHE A CE2   1 1 
ATOM   5380 C  CZ    . PHE A 1 671 ? 38.37   2.951   17.956  1 69.53  ? 671 PHE A CZ    1 1 
ATOM   5381 N  N     . PHE A 1 672 ? 37.966  1.616   24.761  1 68.5   ? 672 PHE A N     1 1 
ATOM   5382 C  CA    . PHE A 1 672 ? 38.237  2.637   25.757  1 69.42  ? 672 PHE A CA    1 1 
ATOM   5383 C  C     . PHE A 1 672 ? 39.236  2.184   26.801  1 70.35  ? 672 PHE A C     1 1 
ATOM   5384 O  O     . PHE A 1 672 ? 39.273  1.008   27.166  1 70.65  ? 672 PHE A O     1 1 
ATOM   5385 C  CB    . PHE A 1 672 ? 36.944  2.988   26.49   1 69.32  ? 672 PHE A CB    1 1 
ATOM   5386 C  CG    . PHE A 1 672 ? 35.89   3.658   25.657  1 69.88  ? 672 PHE A CG    1 1 
ATOM   5387 C  CD1   . PHE A 1 672 ? 34.957  2.913   24.963  1 70.56  ? 672 PHE A CD1   1 1 
ATOM   5388 C  CD2   . PHE A 1 672 ? 35.81   5.033   25.594  1 70.75  ? 672 PHE A CD2   1 1 
ATOM   5389 C  CE1   . PHE A 1 672 ? 33.983  3.532   24.202  1 71.2   ? 672 PHE A CE1   1 1 
ATOM   5390 C  CE2   . PHE A 1 672 ? 34.824  5.648   24.845  1 71.48  ? 672 PHE A CE2   1 1 
ATOM   5391 C  CZ    . PHE A 1 672 ? 33.908  4.894   24.168  1 71.1   ? 672 PHE A CZ    1 1 
ATOM   5392 N  N     . HIS A 1 673 ? 39.992  3.137   27.339  1 70.6   ? 673 HIS A N     1 1 
ATOM   5393 C  CA    . HIS A 1 673 ? 40.911  2.877   28.429  1 71.42  ? 673 HIS A CA    1 1 
ATOM   5394 C  C     . HIS A 1 673 ? 40.652  3.959   29.444  1 72.09  ? 673 HIS A C     1 1 
ATOM   5395 O  O     . HIS A 1 673 ? 40.932  5.127   29.174  1 72.15  ? 673 HIS A O     1 1 
ATOM   5396 C  CB    . HIS A 1 673 ? 42.376  2.92    27.977  1 72.3   ? 673 HIS A CB    1 1 
ATOM   5397 C  CG    . HIS A 1 673 ? 43.343  2.741   29.106  1 74.44  ? 673 HIS A CG    1 1 
ATOM   5398 N  ND1   . HIS A 1 673 ? 44.024  3.814   29.648  1 76.33  ? 673 HIS A ND1   1 1 
ATOM   5399 C  CD2   . HIS A 1 673 ? 43.683  1.62    29.784  1 75.52  ? 673 HIS A CD2   1 1 
ATOM   5400 C  CE1   . HIS A 1 673 ? 44.768  3.313   30.621  1 76.84  ? 673 HIS A CE1   1 1 
ATOM   5401 N  NE2   . HIS A 1 673 ? 44.592  1.997   30.742  1 76.62  ? 673 HIS A NE2   1 1 
ATOM   5402 N  N     . ILE A 1 674 ? 40.067  3.592   30.582  1 72.49  ? 674 ILE A N     1 1 
ATOM   5403 C  CA    . ILE A 1 674 ? 39.799  4.573   31.617  1 73.46  ? 674 ILE A CA    1 1 
ATOM   5404 C  C     . ILE A 1 674 ? 40.952  4.565   32.624  1 74.42  ? 674 ILE A C     1 1 
ATOM   5405 O  O     . ILE A 1 674 ? 41.15   3.595   33.363  1 74.76  ? 674 ILE A O     1 1 
ATOM   5406 C  CB    . ILE A 1 674 ? 38.384  4.428   32.22   1 74.02  ? 674 ILE A CB    1 1 
ATOM   5407 C  CG1   . ILE A 1 674 ? 38.104  2.995   32.698  1 75.04  ? 674 ILE A CG1   1 1 
ATOM   5408 C  CG2   . ILE A 1 674 ? 37.344  4.856   31.188  1 74.5   ? 674 ILE A CG2   1 1 
ATOM   5409 C  CD1   . ILE A 1 674 ? 36.778  2.848   33.443  1 76.38  ? 674 ILE A CD1   1 1 
ATOM   5410 N  N     . GLU A 1 675 ? 41.783  5.615   32.56   1 74.6   ? 675 GLU A N     1 1 
ATOM   5411 C  CA    . GLU A 1 675 ? 42.956  5.78    33.422  1 75.16  ? 675 GLU A CA    1 1 
ATOM   5412 C  C     . GLU A 1 675 ? 42.537  5.812   34.898  1 75.47  ? 675 GLU A C     1 1 
ATOM   5413 O  O     . GLU A 1 675 ? 43.175  5.173   35.74   1 75.63  ? 675 GLU A O     1 1 
ATOM   5414 C  CB    . GLU A 1 675 ? 43.705  7.067   33.032  1 77.26  ? 675 GLU A CB    1 1 
ATOM   5415 C  CG    . GLU A 1 675 ? 44.874  7.431   33.933  1 81.99  ? 675 GLU A CG    1 1 
ATOM   5416 C  CD    . GLU A 1 675 ? 45.583  8.731   33.586  1 88.01  ? 675 GLU A CD    1 1 
ATOM   5417 O  OE1   . GLU A 1 675 ? 45.139  9.422   32.64   1 89.19  ? 675 GLU A OE1   1 1 
ATOM   5418 O  OE2   . GLU A 1 675 ? 46.588  9.057   34.26   1 89.65  ? 675 GLU A OE2   1 1 
ATOM   5419 N  N     . GLY A 1 676 ? 41.438  6.517   35.173  1 75.24  ? 676 GLY A N     1 1 
ATOM   5420 C  CA    . GLY A 1 676 ? 40.863  6.666   36.504  1 75.29  ? 676 GLY A CA    1 1 
ATOM   5421 C  C     . GLY A 1 676 ? 39.765  7.709   36.548  1 74.97  ? 676 GLY A C     1 1 
ATOM   5422 O  O     . GLY A 1 676 ? 39.605  8.49    35.61   1 74.73  ? 676 GLY A O     1 1 
ATOM   5423 P  P     . DC  B 2 1   ? 16.92   24.787  11.942  1 56.6   ? 1   DC  E P     1 1 
ATOM   5424 O  OP1   . DC  B 2 1   ? 17.525  23.436  12.097  1 56.35  ? 1   DC  E OP1   1 1 
ATOM   5425 O  OP2   . DC  B 2 1   ? 15.471  24.998  12.204  1 56.64  ? 1   DC  E OP2   1 1 
ATOM   5426 O  "O5'" . DC  B 2 1   ? 17.74   25.853  12.817  1 56.34  ? 1   DC  E "O5'" 1 ? 
ATOM   5427 C  "C5'" . DC  B 2 1   ? 18.272  25.478  14.088  1 56.05  ? 1   DC  E "C5'" 1 ? 
ATOM   5428 C  "C4'" . DC  B 2 1   ? 18.247  26.637  15.076  1 55.68  ? 1   DC  E "C4'" 1 ? 
ATOM   5429 O  "O4'" . DC  B 2 1   ? 18.922  27.781  14.514  1 55.26  ? 1   DC  E "O4'" 1 ? 
ATOM   5430 C  "C3'" . DC  B 2 1   ? 16.878  27.177  15.422  1 55.89  ? 1   DC  E "C3'" 1 ? 
ATOM   5431 O  "O3'" . DC  B 2 1   ? 16.241  26.376  16.402  1 56.73  ? 1   DC  E "O3'" 1 ? 
ATOM   5432 C  "C2'" . DC  B 2 1   ? 17.235  28.54   15.99   1 55.42  ? 1   DC  E "C2'" 1 ? 
ATOM   5433 C  "C1'" . DC  B 2 1   ? 18.416  28.956  15.128  1 54.95  ? 1   DC  E "C1'" 1 ? 
ATOM   5434 N  N1    . DC  B 2 1   ? 18.051  29.942  14.083  1 54.12  ? 1   DC  E N1    1 1 
ATOM   5435 C  C2    . DC  B 2 1   ? 17.935  31.287  14.426  1 53.54  ? 1   DC  E C2    1 1 
ATOM   5436 O  O2    . DC  B 2 1   ? 18.149  31.632  15.596  1 53.28  ? 1   DC  E O2    1 1 
ATOM   5437 N  N3    . DC  B 2 1   ? 17.621  32.18   13.46   1 53.48  ? 1   DC  E N3    1 1 
ATOM   5438 C  C4    . DC  B 2 1   ? 17.398  31.764  12.212  1 53.55  ? 1   DC  E C4    1 1 
ATOM   5439 N  N4    . DC  B 2 1   ? 17.085  32.677  11.296  1 53.61  ? 1   DC  E N4    1 1 
ATOM   5440 C  C5    . DC  B 2 1   ? 17.479  30.394  11.851  1 53.69  ? 1   DC  E C5    1 1 
ATOM   5441 C  C6    . DC  B 2 1   ? 17.807  29.525  12.808  1 53.93  ? 1   DC  E C6    1 1 
ATOM   5442 P  P     . DA  B 2 2   ? 14.64   26.312  16.444  1 57.61  ? 2   DA  E P     1 1 
ATOM   5443 O  OP1   . DA  B 2 2   ? 14.244  25.362  17.515  1 57.85  ? 2   DA  E OP1   1 1 
ATOM   5444 O  OP2   . DA  B 2 2   ? 14.162  26.099  15.053  1 57.68  ? 2   DA  E OP2   1 1 
ATOM   5445 O  "O5'" . DA  B 2 2   ? 14.217  27.8    16.887  1 57.69  ? 2   DA  E "O5'" 1 ? 
ATOM   5446 C  "C5'" . DA  B 2 2   ? 14.615  28.317  18.173  1 57.69  ? 2   DA  E "C5'" 1 ? 
ATOM   5447 C  "C4'" . DA  B 2 2   ? 14.325  29.81   18.296  1 57.75  ? 2   DA  E "C4'" 1 ? 
ATOM   5448 O  "O4'" . DA  B 2 2   ? 14.821  30.531  17.135  1 57.55  ? 2   DA  E "O4'" 1 ? 
ATOM   5449 C  "C3'" . DA  B 2 2   ? 12.843  30.18   18.442  1 57.99  ? 2   DA  E "C3'" 1 ? 
ATOM   5450 O  "O3'" . DA  B 2 2   ? 12.649  30.962  19.613  1 58.08  ? 2   DA  E "O3'" 1 ? 
ATOM   5451 C  "C2'" . DA  B 2 2   ? 12.529  30.983  17.179  1 57.86  ? 2   DA  E "C2'" 1 ? 
ATOM   5452 C  "C1'" . DA  B 2 2   ? 13.894  31.529  16.785  1 57.46  ? 2   DA  E "C1'" 1 ? 
ATOM   5453 N  N9    . DA  B 2 2   ? 14      31.792  15.352  1 56.88  ? 2   DA  E N9    1 1 
ATOM   5454 C  C8    . DA  B 2 2   ? 14.025  30.867  14.339  1 56.6   ? 2   DA  E C8    1 1 
ATOM   5455 N  N7    . DA  B 2 2   ? 14.043  31.396  13.137  1 56.33  ? 2   DA  E N7    1 1 
ATOM   5456 C  C5    . DA  B 2 2   ? 13.977  32.76   13.378  1 56.22  ? 2   DA  E C5    1 1 
ATOM   5457 C  C6    . DA  B 2 2   ? 13.963  33.878  12.522  1 55.91  ? 2   DA  E C6    1 1 
ATOM   5458 N  N6    . DA  B 2 2   ? 14.016  33.787  11.192  1 55.78  ? 2   DA  E N6    1 1 
ATOM   5459 N  N1    . DA  B 2 2   ? 13.915  35.1    13.091  1 55.84  ? 2   DA  E N1    1 1 
ATOM   5460 C  C2    . DA  B 2 2   ? 13.872  35.193  14.426  1 55.91  ? 2   DA  E C2    1 1 
ATOM   5461 N  N3    . DA  B 2 2   ? 13.866  34.222  15.333  1 56.16  ? 2   DA  E N3    1 1 
ATOM   5462 C  C4    . DA  B 2 2   ? 13.927  33.018  14.738  1 56.45  ? 2   DA  E C4    1 1 
ATOM   5463 P  P     . DT  B 2 3   ? 11.229  30.969  20.344  1 57.92  ? 3   DT  E P     1 1 
ATOM   5464 O  OP1   . DT  B 2 3   ? 11.413  30.431  21.713  1 58.05  ? 3   DT  E OP1   1 1 
ATOM   5465 O  OP2   . DT  B 2 3   ? 10.235  30.354  19.43   1 57.85  ? 3   DT  E OP2   1 1 
ATOM   5466 O  "O5'" . DT  B 2 3   ? 10.914  32.525  20.447  1 57.51  ? 3   DT  E "O5'" 1 ? 
ATOM   5467 C  "C5'" . DT  B 2 3   ? 11.898  33.405  20.918  1 57.14  ? 3   DT  E "C5'" 1 ? 
ATOM   5468 C  "C4'" . DT  B 2 3   ? 11.612  34.793  20.417  1 56.97  ? 3   DT  E "C4'" 1 ? 
ATOM   5469 O  "O4'" . DT  B 2 3   ? 11.768  34.808  18.982  1 56.94  ? 3   DT  E "O4'" 1 ? 
ATOM   5470 C  "C3'" . DT  B 2 3   ? 10.189  35.282  20.694  1 56.93  ? 3   DT  E "C3'" 1 ? 
ATOM   5471 O  "O3'" . DT  B 2 3   ? 10.227  36.52   21.388  1 56.81  ? 3   DT  E "O3'" 1 ? 
ATOM   5472 C  "C2'" . DT  B 2 3   ? 9.563   35.429  19.305  1 56.9   ? 3   DT  E "C2'" 1 ? 
ATOM   5473 C  "C1'" . DT  B 2 3   ? 10.776  35.623  18.424  1 56.93  ? 3   DT  E "C1'" 1 ? 
ATOM   5474 N  N1    . DT  B 2 3   ? 10.559  35.188  17.032  1 56.97  ? 3   DT  E N1    1 1 
ATOM   5475 C  C2    . DT  B 2 3   ? 10.747  36.088  16.009  1 57.02  ? 3   DT  E C2    1 1 
ATOM   5476 O  O2    . DT  B 2 3   ? 11.098  37.242  16.19   1 56.98  ? 3   DT  E O2    1 1 
ATOM   5477 N  N3    . DT  B 2 3   ? 10.536  35.579  14.754  1 57.07  ? 3   DT  E N3    1 1 
ATOM   5478 C  C4    . DT  B 2 3   ? 10.157  34.289  14.431  1 57.22  ? 3   DT  E C4    1 1 
ATOM   5479 O  O4    . DT  B 2 3   ? 10.004  33.979  13.254  1 57.35  ? 3   DT  E O4    1 1 
ATOM   5480 C  C5    . DT  B 2 3   ? 9.963   33.402  15.554  1 57.14  ? 3   DT  E C5    1 1 
ATOM   5481 C  C7    . DT  B 2 3   ? 9.533   31.983  15.326  1 57.03  ? 3   DT  E C7    1 1 
ATOM   5482 C  C6    . DT  B 2 3   ? 10.173  33.89   16.786  1 57.07  ? 3   DT  E C6    1 1 
ATOM   5483 P  P     . DT  B 2 4   ? 8.885   37.148  22.013  1 56.58  ? 4   DT  E P     1 1 
ATOM   5484 O  OP1   . DT  B 2 4   ? 9.2     37.614  23.384  1 56.78  ? 4   DT  E OP1   1 1 
ATOM   5485 O  OP2   . DT  B 2 4   ? 7.761   36.206  21.791  1 56.37  ? 4   DT  E OP2   1 1 
ATOM   5486 O  "O5'" . DT  B 2 4   ? 8.649   38.424  21.086  1 55.82  ? 4   DT  E "O5'" 1 ? 
ATOM   5487 C  "C5'" . DT  B 2 4   ? 9.65    39.429  21.026  1 54.67  ? 4   DT  E "C5'" 1 ? 
ATOM   5488 C  "C4'" . DT  B 2 4   ? 9.5     40.287  19.786  1 53.54  ? 4   DT  E "C4'" 1 ? 
ATOM   5489 O  "O4'" . DT  B 2 4   ? 9.479   39.462  18.587  1 52.98  ? 4   DT  E "O4'" 1 ? 
ATOM   5490 C  "C3'" . DT  B 2 4   ? 8.237   41.145  19.721  1 53.04  ? 4   DT  E "C3'" 1 ? 
ATOM   5491 O  "O3'" . DT  B 2 4   ? 8.579   42.38   19.124  1 52.82  ? 4   DT  E "O3'" 1 ? 
ATOM   5492 C  "C2'" . DT  B 2 4   ? 7.356   40.331  18.787  1 52.81  ? 4   DT  E "C2'" 1 ? 
ATOM   5493 C  "C1'" . DT  B 2 4   ? 8.402   39.884  17.794  1 52.68  ? 4   DT  E "C1'" 1 ? 
ATOM   5494 N  N1    . DT  B 2 4   ? 7.976   38.783  16.924  1 52.41  ? 4   DT  E N1    1 1 
ATOM   5495 C  C2    . DT  B 2 4   ? 8.044   38.958  15.566  1 52.43  ? 4   DT  E C2    1 1 
ATOM   5496 O  O2    . DT  B 2 4   ? 8.467   39.978  15.049  1 52.47  ? 4   DT  E O2    1 1 
ATOM   5497 N  N3    . DT  B 2 4   ? 7.596   37.897  14.829  1 52.38  ? 4   DT  E N3    1 1 
ATOM   5498 C  C4    . DT  B 2 4   ? 7.107   36.701  15.312  1 52.41  ? 4   DT  E C4    1 1 
ATOM   5499 O  O4    . DT  B 2 4   ? 6.762   35.83   14.524  1 52.66  ? 4   DT  E O4    1 1 
ATOM   5500 C  C5    . DT  B 2 4   ? 7.056   36.587  16.751  1 52.2   ? 4   DT  E C5    1 1 
ATOM   5501 C  C7    . DT  B 2 4   ? 6.549   35.328  17.387  1 52.17  ? 4   DT  E C7    1 1 
ATOM   5502 C  C6    . DT  B 2 4   ? 7.457   37.636  17.479  1 52.19  ? 4   DT  E C6    1 1 
ATOM   5503 P  P     . DC  B 2 5   ? 7.754   43.712  19.435  1 52.42  ? 5   DC  E P     1 1 
ATOM   5504 O  OP1   . DC  B 2 5   ? 8.593   44.563  20.307  1 52.48  ? 5   DC  E OP1   1 1 
ATOM   5505 O  OP2   . DC  B 2 5   ? 6.379   43.33   19.856  1 52.18  ? 5   DC  E OP2   1 1 
ATOM   5506 O  "O5'" . DC  B 2 5   ? 7.669   44.388  17.993  1 51.84  ? 5   DC  E "O5'" 1 ? 
ATOM   5507 C  "C5'" . DC  B 2 5   ? 8.733   44.189  17.062  1 51.16  ? 5   DC  E "C5'" 1 ? 
ATOM   5508 C  "C4'" . DC  B 2 5   ? 8.251   44.356  15.633  1 50.68  ? 5   DC  E "C4'" 1 ? 
ATOM   5509 O  "O4'" . DC  B 2 5   ? 7.751   43.093  15.125  1 50.33  ? 5   DC  E "O4'" 1 ? 
ATOM   5510 C  "C3'" . DC  B 2 5   ? 7.132   45.378  15.443  1 50.65  ? 5   DC  E "C3'" 1 ? 
ATOM   5511 O  "O3'" . DC  B 2 5   ? 7.456   46.259  14.382  1 50.79  ? 5   DC  E "O3'" 1 ? 
ATOM   5512 C  "C2'" . DC  B 2 5   ? 5.897   44.53   15.134  1 50.35  ? 5   DC  E "C2'" 1 ? 
ATOM   5513 C  "C1'" . DC  B 2 5   ? 6.505   43.292  14.496  1 50.15  ? 5   DC  E "C1'" 1 ? 
ATOM   5514 N  N1    . DC  B 2 5   ? 5.678   42.064  14.676  1 49.78  ? 5   DC  E N1    1 1 
ATOM   5515 C  C2    . DC  B 2 5   ? 5.016   41.52   13.579  1 49.56  ? 5   DC  E C2    1 1 
ATOM   5516 O  O2    . DC  B 2 5   ? 5.168   42.052  12.476  1 49.81  ? 5   DC  E O2    1 1 
ATOM   5517 N  N3    . DC  B 2 5   ? 4.268   40.394  13.746  1 49.07  ? 5   DC  E N3    1 1 
ATOM   5518 C  C4    . DC  B 2 5   ? 4.149   39.85   14.958  1 48.8   ? 5   DC  E C4    1 1 
ATOM   5519 N  N4    . DC  B 2 5   ? 3.411   38.747  15.083  1 48.34  ? 5   DC  E N4    1 1 
ATOM   5520 C  C5    . DC  B 2 5   ? 4.791   40.414  16.097  1 49.27  ? 5   DC  E C5    1 1 
ATOM   5521 C  C6    . DC  B 2 5   ? 5.531   41.516  15.913  1 49.57  ? 5   DC  E C6    1 1 
ATOM   5522 P  P     . DC  B 2 6   ? 6.632   47.605  14.195  1 50.61  ? 6   DC  E P     1 1 
ATOM   5523 O  OP1   . DC  B 2 6   ? 7.555   48.633  13.658  1 50.31  ? 6   DC  E OP1   1 1 
ATOM   5524 O  OP2   . DC  B 2 6   ? 5.883   47.853  15.446  1 50.68  ? 6   DC  E OP2   1 1 
ATOM   5525 O  "O5'" . DC  B 2 6   ? 5.581   47.203  13.058  1 50.63  ? 6   DC  E "O5'" 1 ? 
ATOM   5526 C  "C5'" . DC  B 2 6   ? 6.07    46.837  11.783  1 50.72  ? 6   DC  E "C5'" 1 ? 
ATOM   5527 C  "C4'" . DC  B 2 6   ? 4.971   46.317  10.892  1 50.68  ? 6   DC  E "C4'" 1 ? 
ATOM   5528 O  "O4'" . DC  B 2 6   ? 4.484   45.057  11.397  1 50.7   ? 6   DC  E "O4'" 1 ? 
ATOM   5529 C  "C3'" . DC  B 2 6   ? 3.756   47.229  10.749  1 50.84  ? 6   DC  E "C3'" 1 ? 
ATOM   5530 O  "O3'" . DC  B 2 6   ? 3.475   47.401  9.365   1 51.39  ? 6   DC  E "O3'" 1 ? 
ATOM   5531 C  "C2'" . DC  B 2 6   ? 2.647   46.462  11.474  1 50.54  ? 6   DC  E "C2'" 1 ? 
ATOM   5532 C  "C1'" . DC  B 2 6   ? 3.087   45.028  11.272  1 50.41  ? 6   DC  E "C1'" 1 ? 
ATOM   5533 N  N1    . DC  B 2 6   ? 2.55    44.083  12.283  1 50.01  ? 6   DC  E N1    1 1 
ATOM   5534 C  C2    . DC  B 2 6   ? 1.963   42.889  11.86   1 49.82  ? 6   DC  E C2    1 1 
ATOM   5535 O  O2    . DC  B 2 6   ? 1.913   42.649  10.649  1 49.84  ? 6   DC  E O2    1 1 
ATOM   5536 N  N3    . DC  B 2 6   ? 1.52    42.008  12.794  1 49.57  ? 6   DC  E N3    1 1 
ATOM   5537 C  C4    . DC  B 2 6   ? 1.629   42.307  14.092  1 49.44  ? 6   DC  E C4    1 1 
ATOM   5538 N  N4    . DC  B 2 6   ? 1.17    41.423  14.978  1 49.29  ? 6   DC  E N4    1 1 
ATOM   5539 C  C5    . DC  B 2 6   ? 2.211   43.527  14.538  1 49.59  ? 6   DC  E C5    1 1 
ATOM   5540 C  C6    . DC  B 2 6   ? 2.656   44.376  13.609  1 49.81  ? 6   DC  E C6    1 1 
ATOM   5541 P  P     . DT  B 2 7   ? 2.414   48.493  8.857   1 51.96  ? 7   DT  E P     1 1 
ATOM   5542 O  OP1   . DT  B 2 7   ? 3.134   49.492  8.034   1 51.77  ? 7   DT  E OP1   1 1 
ATOM   5543 O  OP2   . DT  B 2 7   ? 1.605   48.943  10.012  1 51.84  ? 7   DT  E OP2   1 1 
ATOM   5544 O  "O5'" . DT  B 2 7   ? 1.477   47.611  7.899   1 52.86  ? 7   DT  E "O5'" 1 ? 
ATOM   5545 C  "C5'" . DT  B 2 7   ? 2.078   46.697  6.955   1 53.56  ? 7   DT  E "C5'" 1 ? 
ATOM   5546 C  "C4'" . DT  B 2 7   ? 1.06    45.709  6.385   1 54.29  ? 7   DT  E "C4'" 1 ? 
ATOM   5547 O  "O4'" . DT  B 2 7   ? 0.691   44.746  7.4     1 54.12  ? 7   DT  E "O4'" 1 ? 
ATOM   5548 C  "C3'" . DT  B 2 7   ? -0.25   46.32   5.878   1 55.2   ? 7   DT  E "C3'" 1 ? 
ATOM   5549 O  "O3'" . DT  B 2 7   ? -0.672  45.668  4.68    1 56.62  ? 7   DT  E "O3'" 1 ? 
ATOM   5550 C  "C2'" . DT  B 2 7   ? -1.22   46.051  7.017   1 54.64  ? 7   DT  E "C2'" 1 ? 
ATOM   5551 C  "C1'" . DT  B 2 7   ? -0.708  44.72   7.542   1 54.08  ? 7   DT  E "C1'" 1 ? 
ATOM   5552 N  N1    . DT  B 2 7   ? -1.028  44.496  8.965   1 53.65  ? 7   DT  E N1    1 1 
ATOM   5553 C  C2    . DT  B 2 7   ? -1.594  43.306  9.333   1 53.66  ? 7   DT  E C2    1 1 
ATOM   5554 O  O2    . DT  B 2 7   ? -1.795  42.395  8.546   1 53.73  ? 7   DT  E O2    1 1 
ATOM   5555 N  N3    . DT  B 2 7   ? -1.882  43.199  10.67   1 53.52  ? 7   DT  E N3    1 1 
ATOM   5556 C  C4    . DT  B 2 7   ? -1.682  44.159  11.648  1 53.3   ? 7   DT  E C4    1 1 
ATOM   5557 O  O4    . DT  B 2 7   ? -2.001  43.919  12.81   1 53.21  ? 7   DT  E O4    1 1 
ATOM   5558 C  C5    . DT  B 2 7   ? -1.099  45.395  11.185  1 53.23  ? 7   DT  E C5    1 1 
ATOM   5559 C  C7    . DT  B 2 7   ? -0.845  46.514  12.146  1 53.21  ? 7   DT  E C7    1 1 
ATOM   5560 C  C6    . DT  B 2 7   ? -0.809  45.505  9.882   1 53.35  ? 7   DT  E C6    1 1 
ATOM   5561 P  P     . DC  B 2 8   ? -1.64   46.427  3.646   1 58     ? 8   DC  E P     1 1 
ATOM   5562 O  OP1   . DC  B 2 8   ? -1.041  46.311  2.296   1 58.16  ? 8   DC  E OP1   1 1 
ATOM   5563 O  OP2   . DC  B 2 8   ? -1.956  47.764  4.202   1 57.87  ? 8   DC  E OP2   1 1 
ATOM   5564 O  "O5'" . DC  B 2 8   ? -2.973  45.544  3.694   1 59     ? 8   DC  E "O5'" 1 ? 
ATOM   5565 C  "C5'" . DC  B 2 8   ? -2.939  44.202  3.221   1 59.93  ? 8   DC  E "C5'" 1 ? 
ATOM   5566 C  "C4'" . DC  B 2 8   ? -4.001  43.351  3.9     1 60.77  ? 8   DC  E "C4'" 1 ? 
ATOM   5567 O  "O4'" . DC  B 2 8   ? -3.837  43.399  5.339   1 61.13  ? 8   DC  E "O4'" 1 ? 
ATOM   5568 C  "C3'" . DC  B 2 8   ? -5.456  43.762  3.622   1 60.99  ? 8   DC  E "C3'" 1 ? 
ATOM   5569 O  "O3'" . DC  B 2 8   ? -6.165  42.662  3.052   1 61.1   ? 8   DC  E "O3'" 1 ? 
ATOM   5570 C  "C2'" . DC  B 2 8   ? -6.008  44.123  5.009   1 61.05  ? 8   DC  E "C2'" 1 ? 
ATOM   5571 C  "C1'" . DC  B 2 8   ? -5.104  43.307  5.924   1 61.11  ? 8   DC  E "C1'" 1 ? 
ATOM   5572 N  N1    . DC  B 2 8   ? -5.026  43.827  7.322   1 60.98  ? 8   DC  E N1    1 1 
ATOM   5573 C  C2    . DC  B 2 8   ? -5.149  42.938  8.402   1 60.48  ? 8   DC  E C2    1 1 
ATOM   5574 O  O2    . DC  B 2 8   ? -5.267  41.726  8.177   1 59.89  ? 8   DC  E O2    1 1 
ATOM   5575 N  N3    . DC  B 2 8   ? -5.089  43.431  9.667   1 60.7   ? 8   DC  E N3    1 1 
ATOM   5576 C  C4    . DC  B 2 8   ? -4.943  44.749  9.865   1 61.03  ? 8   DC  E C4    1 1 
ATOM   5577 N  N4    . DC  B 2 8   ? -4.899  45.196  11.127  1 61.09  ? 8   DC  E N4    1 1 
ATOM   5578 C  C5    . DC  B 2 8   ? -4.825  45.668  8.775   1 61.15  ? 8   DC  E C5    1 1 
ATOM   5579 C  C6    . DC  B 2 8   ? -4.869  45.169  7.536   1 61.12  ? 8   DC  E C6    1 1 
ATOM   5580 O  "O5'" . DG  C 3 1   ? -7.884  37.397  19.722  1 59.81  ? 1   DG  F "O5'" 1 ? 
ATOM   5581 C  "C5'" . DG  C 3 1   ? -7.66   38.158  18.532  1 59.74  ? 1   DG  F "C5'" 1 ? 
ATOM   5582 C  "C4'" . DG  C 3 1   ? -8.083  37.375  17.291  1 59.61  ? 1   DG  F "C4'" 1 ? 
ATOM   5583 O  "O4'" . DG  C 3 1   ? -8.24   38.288  16.166  1 59.33  ? 1   DG  F "O4'" 1 ? 
ATOM   5584 C  "C3'" . DG  C 3 1   ? -7.073  36.351  16.806  1 59.49  ? 1   DG  F "C3'" 1 ? 
ATOM   5585 O  "O3'" . DG  C 3 1   ? -7.726  35.366  16.003  1 59.66  ? 1   DG  F "O3'" 1 ? 
ATOM   5586 C  "C2'" . DG  C 3 1   ? -6.139  37.217  15.973  1 59.13  ? 1   DG  F "C2'" 1 ? 
ATOM   5587 C  "C1'" . DG  C 3 1   ? -7.118  38.186  15.3    1 58.86  ? 1   DG  F "C1'" 1 ? 
ATOM   5588 N  N9    . DG  C 3 1   ? -6.563  39.525  15.117  1 58.08  ? 1   DG  F N9    1 1 
ATOM   5589 C  C8    . DG  C 3 1   ? -6.119  40.368  16.105  1 57.81  ? 1   DG  F C8    1 1 
ATOM   5590 N  N7    . DG  C 3 1   ? -5.649  41.497  15.659  1 57.59  ? 1   DG  F N7    1 1 
ATOM   5591 C  C5    . DG  C 3 1   ? -5.792  41.405  14.284  1 57.41  ? 1   DG  F C5    1 1 
ATOM   5592 C  C6    . DG  C 3 1   ? -5.46   42.338  13.273  1 57.01  ? 1   DG  F C6    1 1 
ATOM   5593 O  O6    . DG  C 3 1   ? -4.961  43.465  13.406  1 56.71  ? 1   DG  F O6    1 1 
ATOM   5594 N  N1    . DG  C 3 1   ? -5.761  41.848  12.004  1 56.99  ? 1   DG  F N1    1 1 
ATOM   5595 C  C2    . DG  C 3 1   ? -6.338  40.62   11.75   1 57.13  ? 1   DG  F C2    1 1 
ATOM   5596 N  N2    . DG  C 3 1   ? -6.566  40.327  10.462  1 57.15  ? 1   DG  F N2    1 1 
ATOM   5597 N  N3    . DG  C 3 1   ? -6.664  39.738  12.692  1 57.32  ? 1   DG  F N3    1 1 
ATOM   5598 C  C4    . DG  C 3 1   ? -6.355  40.193  13.93   1 57.62  ? 1   DG  F C4    1 1 
ATOM   5599 P  P     . DA  C 3 2   ? -6.937  34.034  15.56   1 59.74  ? 2   DA  F P     1 1 
ATOM   5600 O  OP1   . DA  C 3 2   ? -7.923  32.919  15.492  1 59.88  ? 2   DA  F OP1   1 1 
ATOM   5601 O  OP2   . DA  C 3 2   ? -5.714  33.903  16.413  1 59.86  ? 2   DA  F OP2   1 1 
ATOM   5602 O  "O5'" . DA  C 3 2   ? -6.456  34.388  14.07   1 57.95  ? 2   DA  F "O5'" 1 ? 
ATOM   5603 C  "C5'" . DA  C 3 2   ? -7.412  34.502  13.018  1 55.6   ? 2   DA  F "C5'" 1 ? 
ATOM   5604 C  "C4'" . DA  C 3 2   ? -6.719  34.693  11.681  1 53.17  ? 2   DA  F "C4'" 1 ? 
ATOM   5605 O  "O4'" . DA  C 3 2   ? -6.141  36.019  11.617  1 52.31  ? 2   DA  F "O4'" 1 ? 
ATOM   5606 C  "C3'" . DA  C 3 2   ? -5.579  33.725  11.388  1 51.58  ? 2   DA  F "C3'" 1 ? 
ATOM   5607 O  "O3'" . DA  C 3 2   ? -5.577  33.417  10.011  1 50.45  ? 2   DA  F "O3'" 1 ? 
ATOM   5608 C  "C2'" . DA  C 3 2   ? -4.34   34.523  11.78   1 51.41  ? 2   DA  F "C2'" 1 ? 
ATOM   5609 C  "C1'" . DA  C 3 2   ? -4.75   35.927  11.367  1 51.35  ? 2   DA  F "C1'" 1 ? 
ATOM   5610 N  N9    . DA  C 3 2   ? -4.09   36.988  12.124  1 50.26  ? 2   DA  F N9    1 1 
ATOM   5611 C  C8    . DA  C 3 2   ? -3.907  37.039  13.476  1 49.89  ? 2   DA  F C8    1 1 
ATOM   5612 N  N7    . DA  C 3 2   ? -3.388  38.165  13.901  1 49.49  ? 2   DA  F N7    1 1 
ATOM   5613 C  C5    . DA  C 3 2   ? -3.217  38.907  12.747  1 49.14  ? 2   DA  F C5    1 1 
ATOM   5614 C  C6    . DA  C 3 2   ? -2.676  40.184  12.516  1 48.56  ? 2   DA  F C6    1 1 
ATOM   5615 N  N6    . DA  C 3 2   ? -2.208  40.97   13.489  1 48.12  ? 2   DA  F N6    1 1 
ATOM   5616 N  N1    . DA  C 3 2   ? -2.634  40.621  11.241  1 48.63  ? 2   DA  F N1    1 1 
ATOM   5617 C  C2    . DA  C 3 2   ? -3.101  39.827  10.271  1 48.85  ? 2   DA  F C2    1 1 
ATOM   5618 N  N3    . DA  C 3 2   ? -3.617  38.604  10.364  1 49.13  ? 2   DA  F N3    1 1 
ATOM   5619 C  C4    . DA  C 3 2   ? -3.647  38.199  11.641  1 49.47  ? 2   DA  F C4    1 1 
ATOM   5620 P  P     . DG  C 3 3   ? -4.761  32.153  9.468   1 49.55  ? 3   DG  F P     1 1 
ATOM   5621 O  OP1   . DG  C 3 3   ? -5.472  31.627  8.277   1 49.59  ? 3   DG  F OP1   1 1 
ATOM   5622 O  OP2   . DG  C 3 3   ? -4.462  31.259  10.62   1 49.6   ? 3   DG  F OP2   1 1 
ATOM   5623 O  "O5'" . DG  C 3 3   ? -3.384  32.8    8.992   1 48.13  ? 3   DG  F "O5'" 1 ? 
ATOM   5624 C  "C5'" . DG  C 3 3   ? -3.387  33.821  8.006   1 46.3   ? 3   DG  F "C5'" 1 ? 
ATOM   5625 C  "C4'" . DG  C 3 3   ? -2.018  34.46   7.896   1 44.22  ? 3   DG  F "C4'" 1 ? 
ATOM   5626 O  "O4'" . DG  C 3 3   ? -1.85   35.451  8.946   1 43.69  ? 3   DG  F "O4'" 1 ? 
ATOM   5627 C  "C3'" . DG  C 3 3   ? -0.831  33.498  8.052   1 42.79  ? 3   DG  F "C3'" 1 ? 
ATOM   5628 O  "O3'" . DG  C 3 3   ? 0.199   33.897  7.171   1 41.58  ? 3   DG  F "O3'" 1 ? 
ATOM   5629 C  "C2'" . DG  C 3 3   ? -0.406  33.749  9.492   1 42.81  ? 3   DG  F "C2'" 1 ? 
ATOM   5630 C  "C1'" . DG  C 3 3   ? -0.586  35.239  9.517   1 43.08  ? 3   DG  F "C1'" 1 ? 
ATOM   5631 N  N9    . DG  C 3 3   ? -0.517  35.854  10.826  1 42.64  ? 3   DG  F N9    1 1 
ATOM   5632 C  C8    . DG  C 3 3   ? -0.676  35.256  12.055  1 42.49  ? 3   DG  F C8    1 1 
ATOM   5633 N  N7    . DG  C 3 3   ? -0.485  36.079  13.054  1 42.39  ? 3   DG  F N7    1 1 
ATOM   5634 C  C5    . DG  C 3 3   ? -0.131  37.279  12.437  1 42.24  ? 3   DG  F C5    1 1 
ATOM   5635 C  C6    . DG  C 3 3   ? 0.196   38.54   12.997  1 42.11  ? 3   DG  F C6    1 1 
ATOM   5636 O  O6    . DG  C 3 3   ? 0.222   38.863  14.194  1 41.97  ? 3   DG  F O6    1 1 
ATOM   5637 N  N1    . DG  C 3 3   ? 0.48    39.488  12.004  1 42.1   ? 3   DG  F N1    1 1 
ATOM   5638 C  C2    . DG  C 3 3   ? 0.448   39.234  10.646  1 42.05  ? 3   DG  F C2    1 1 
ATOM   5639 N  N2    . DG  C 3 3   ? 0.747   40.256  9.834   1 41.9   ? 3   DG  F N2    1 1 
ATOM   5640 N  N3    . DG  C 3 3   ? 0.116   38.068  10.12   1 42.04  ? 3   DG  F N3    1 1 
ATOM   5641 C  C4    . DG  C 3 3   ? -0.141  37.142  11.07   1 42.26  ? 3   DG  F C4    1 1 
ATOM   5642 P  P     . DG  C 3 4   ? 0.826   32.866  6.129   1 40.47  ? 4   DG  F P     1 1 
ATOM   5643 O  OP1   . DG  C 3 4   ? -0.273  32.402  5.251   1 40.69  ? 4   DG  F OP1   1 1 
ATOM   5644 O  OP2   . DG  C 3 4   ? 1.658   31.881  6.881   1 40.37  ? 4   DG  F OP2   1 1 
ATOM   5645 O  "O5'" . DG  C 3 4   ? 1.806   33.791  5.271   1 39.02  ? 4   DG  F "O5'" 1 ? 
ATOM   5646 C  "C5'" . DG  C 3 4   ? 1.273   34.843  4.5     1 37.45  ? 4   DG  F "C5'" 1 ? 
ATOM   5647 C  "C4'" . DG  C 3 4   ? 1.982   36.136  4.806   1 36     ? 4   DG  F "C4'" 1 ? 
ATOM   5648 O  "O4'" . DG  C 3 4   ? 1.836   36.461  6.208   1 35.18  ? 4   DG  F "O4'" 1 ? 
ATOM   5649 C  "C3'" . DG  C 3 4   ? 3.478   36.154  4.518   1 35.57  ? 4   DG  F "C3'" 1 ? 
ATOM   5650 O  "O3'" . DG  C 3 4   ? 3.795   37.376  3.842   1 36.13  ? 4   DG  F "O3'" 1 ? 
ATOM   5651 C  "C2'" . DG  C 3 4   ? 4.083   36.088  5.921   1 34.98  ? 4   DG  F "C2'" 1 ? 
ATOM   5652 C  "C1'" . DG  C 3 4   ? 3.071   36.877  6.706   1 34.54  ? 4   DG  F "C1'" 1 ? 
ATOM   5653 N  N9    . DG  C 3 4   ? 3.101   36.604  8.127   1 33.82  ? 4   DG  F N9    1 1 
ATOM   5654 C  C8    . DG  C 3 4   ? 2.856   35.405  8.738   1 33.66  ? 4   DG  F C8    1 1 
ATOM   5655 N  N7    . DG  C 3 4   ? 2.938   35.457  10.038  1 33.7   ? 4   DG  F N7    1 1 
ATOM   5656 C  C5    . DG  C 3 4   ? 3.258   36.78   10.305  1 33.89  ? 4   DG  F C5    1 1 
ATOM   5657 C  C6    . DG  C 3 4   ? 3.491   37.435  11.546  1 34.12  ? 4   DG  F C6    1 1 
ATOM   5658 O  O6    . DG  C 3 4   ? 3.443   36.952  12.696  1 34.22  ? 4   DG  F O6    1 1 
ATOM   5659 N  N1    . DG  C 3 4   ? 3.792   38.792  11.361  1 33.93  ? 4   DG  F N1    1 1 
ATOM   5660 C  C2    . DG  C 3 4   ? 3.816   39.43   10.138  1 33.76  ? 4   DG  F C2    1 1 
ATOM   5661 N  N2    . DG  C 3 4   ? 4.137   40.729  10.149  1 33.72  ? 4   DG  F N2    1 1 
ATOM   5662 N  N3    . DG  C 3 4   ? 3.656   38.811  8.974   1 33.74  ? 4   DG  F N3    1 1 
ATOM   5663 C  C4    . DG  C 3 4   ? 3.364   37.499  9.134   1 33.78  ? 4   DG  F C4    1 1 
ATOM   5664 P  P     . DA  C 3 5   ? 5.311   37.857  3.588   1 36.85  ? 5   DA  F P     1 1 
ATOM   5665 O  OP1   . DA  C 3 5   ? 5.342   38.574  2.292   1 37.31  ? 5   DA  F OP1   1 1 
ATOM   5666 O  OP2   . DA  C 3 5   ? 6.23    36.717  3.829   1 36.82  ? 5   DA  F OP2   1 1 
ATOM   5667 O  "O5'" . DA  C 3 5   ? 5.53    38.927  4.753   1 36.49  ? 5   DA  F "O5'" 1 ? 
ATOM   5668 C  "C5'" . DA  C 3 5   ? 4.692   40.079  4.818   1 35.98  ? 5   DA  F "C5'" 1 ? 
ATOM   5669 C  "C4'" . DA  C 3 5   ? 5.335   41.177  5.642   1 35.68  ? 5   DA  F "C4'" 1 ? 
ATOM   5670 O  "O4'" . DA  C 3 5   ? 5.386   40.776  7.035   1 35.41  ? 5   DA  F "O4'" 1 ? 
ATOM   5671 C  "C3'" . DA  C 3 5   ? 6.769   41.525  5.256   1 35.85  ? 5   DA  F "C3'" 1 ? 
ATOM   5672 O  "O3'" . DA  C 3 5   ? 6.999   42.924  5.47    1 35.91  ? 5   DA  F "O3'" 1 ? 
ATOM   5673 C  "C2'" . DA  C 3 5   ? 7.6     40.654  6.202   1 35.63  ? 5   DA  F "C2'" 1 ? 
ATOM   5674 C  "C1'" . DA  C 3 5   ? 6.736   40.637  7.459   1 35.52  ? 5   DA  F "C1'" 1 ? 
ATOM   5675 N  N9    . DA  C 3 5   ? 6.837   39.398  8.234   1 35.43  ? 5   DA  F N9    1 1 
ATOM   5676 C  C8    . DA  C 3 5   ? 6.645   38.116  7.783   1 34.94  ? 5   DA  F C8    1 1 
ATOM   5677 N  N7    . DA  C 3 5   ? 6.711   37.206  8.727   1 34.62  ? 5   DA  F N7    1 1 
ATOM   5678 C  C5    . DA  C 3 5   ? 6.945   37.935  9.88    1 34.82  ? 5   DA  F C5    1 1 
ATOM   5679 C  C6    . DA  C 3 5   ? 7.111   37.553  11.225  1 34.62  ? 5   DA  F C6    1 1 
ATOM   5680 N  N6    . DA  C 3 5   ? 7.074   36.295  11.635  1 34.46  ? 5   DA  F N6    1 1 
ATOM   5681 N  N1    . DA  C 3 5   ? 7.355   38.52   12.126  1 35.06  ? 5   DA  F N1    1 1 
ATOM   5682 C  C2    . DA  C 3 5   ? 7.402   39.798  11.708  1 35.6   ? 5   DA  F C2    1 1 
ATOM   5683 N  N3    . DA  C 3 5   ? 7.266   40.288  10.47   1 35.68  ? 5   DA  F N3    1 1 
ATOM   5684 C  C4    . DA  C 3 5   ? 7.08    39.285  9.587   1 35.46  ? 5   DA  F C4    1 1 
ATOM   5685 P  P     . DA  C 3 6   ? 8.388   43.602  5.038   1 35.58  ? 6   DA  F P     1 1 
ATOM   5686 O  OP1   . DA  C 3 6   ? 8.142   45.054  4.828   1 35.57  ? 6   DA  F OP1   1 1 
ATOM   5687 O  OP2   . DA  C 3 6   ? 8.972   42.783  3.945   1 35.69  ? 6   DA  F OP2   1 1 
ATOM   5688 O  "O5'" . DA  C 3 6   ? 9.286   43.423  6.357   1 35.07  ? 6   DA  F "O5'" 1 ? 
ATOM   5689 C  "C5'" . DA  C 3 6   ? 8.799   43.924  7.594   1 34.76  ? 6   DA  F "C5'" 1 ? 
ATOM   5690 C  "C4'" . DA  C 3 6   ? 9.654   43.49   8.766   1 34.65  ? 6   DA  F "C4'" 1 ? 
ATOM   5691 O  "O4'" . DA  C 3 6   ? 9.382   42.12   9.123   1 34.27  ? 6   DA  F "O4'" 1 ? 
ATOM   5692 C  "C3'" . DA  C 3 6   ? 11.167  43.586  8.564   1 35.08  ? 6   DA  F "C3'" 1 ? 
ATOM   5693 O  "O3'" . DA  C 3 6   ? 11.675  44.674  9.355   1 36.13  ? 6   DA  F "O3'" 1 ? 
ATOM   5694 C  "C2'" . DA  C 3 6   ? 11.699  42.217  9.047   1 34.37  ? 6   DA  F "C2'" 1 ? 
ATOM   5695 C  "C1'" . DA  C 3 6   ? 10.514  41.63   9.794   1 33.68  ? 6   DA  F "C1'" 1 ? 
ATOM   5696 N  N9    . DA  C 3 6   ? 10.484  40.166  9.793   1 32.54  ? 6   DA  F N9    1 1 
ATOM   5697 C  C8    . DA  C 3 6   ? 10.477  39.338  8.703   1 31.97  ? 6   DA  F C8    1 1 
ATOM   5698 N  N7    . DA  C 3 6   ? 10.466  38.059  9.01    1 31.62  ? 6   DA  F N7    1 1 
ATOM   5699 C  C5    . DA  C 3 6   ? 10.486  38.047  10.399  1 31.43  ? 6   DA  F C5    1 1 
ATOM   5700 C  C6    . DA  C 3 6   ? 10.455  36.996  11.351  1 30.78  ? 6   DA  F C6    1 1 
ATOM   5701 N  N6    . DA  C 3 6   ? 10.403  35.706  11.025  1 30.23  ? 6   DA  F N6    1 1 
ATOM   5702 N  N1    . DA  C 3 6   ? 10.493  37.332  12.653  1 30.96  ? 6   DA  F N1    1 1 
ATOM   5703 C  C2    . DA  C 3 6   ? 10.538  38.63   12.981  1 31.43  ? 6   DA  F C2    1 1 
ATOM   5704 N  N3    . DA  C 3 6   ? 10.533  39.704  12.187  1 31.74  ? 6   DA  F N3    1 1 
ATOM   5705 C  C4    . DA  C 3 6   ? 10.539  39.338  10.894  1 31.95  ? 6   DA  F C4    1 1 
ATOM   5706 P  P     . DT  C 3 7   ? 13.17   45.224  9.167   1 36.88  ? 7   DT  F P     1 1 
ATOM   5707 O  OP1   . DT  C 3 7   ? 13.118  46.709  9.081   1 37.21  ? 7   DT  F OP1   1 1 
ATOM   5708 O  OP2   . DT  C 3 7   ? 13.821  44.443  8.081   1 36.95  ? 7   DT  F OP2   1 1 
ATOM   5709 O  "O5'" . DT  C 3 7   ? 13.84   44.827  10.553  1 37.1   ? 7   DT  F "O5'" 1 ? 
ATOM   5710 C  "C5'" . DT  C 3 7   ? 14.192  43.517  10.781  1 37.65  ? 7   DT  F "C5'" 1 ? 
ATOM   5711 C  "C4'" . DT  C 3 7   ? 14.178  43.199  12.239  1 38.53  ? 7   DT  F "C4'" 1 ? 
ATOM   5712 O  "O4'" . DT  C 3 7   ? 13.286  42.094  12.44   1 38.26  ? 7   DT  F "O4'" 1 ? 
ATOM   5713 C  "C3'" . DT  C 3 7   ? 15.537  42.772  12.759  1 40.05  ? 7   DT  F "C3'" 1 ? 
ATOM   5714 O  "O3'" . DT  C 3 7   ? 16.101  43.834  13.496  1 42.38  ? 7   DT  F "O3'" 1 ? 
ATOM   5715 C  "C2'" . DT  C 3 7   ? 15.262  41.558  13.641  1 39.08  ? 7   DT  F "C2'" 1 ? 
ATOM   5716 C  "C1'" . DT  C 3 7   ? 13.909  41.063  13.165  1 38.03  ? 7   DT  F "C1'" 1 ? 
ATOM   5717 N  N1    . DT  C 3 7   ? 13.964  39.828  12.335  1 36.68  ? 7   DT  F N1    1 1 
ATOM   5718 C  C2    . DT  C 3 7   ? 13.952  38.618  12.97   1 36.24  ? 7   DT  F C2    1 1 
ATOM   5719 O  O2    . DT  C 3 7   ? 13.884  38.512  14.185  1 36.23  ? 7   DT  F O2    1 1 
ATOM   5720 N  N3    . DT  C 3 7   ? 13.956  37.526  12.131  1 35.82  ? 7   DT  F N3    1 1 
ATOM   5721 C  C4    . DT  C 3 7   ? 13.987  37.539  10.746  1 35.37  ? 7   DT  F C4    1 1 
ATOM   5722 O  O4    . DT  C 3 7   ? 14.023  36.477  10.124  1 34.77  ? 7   DT  F O4    1 1 
ATOM   5723 C  C5    . DT  C 3 7   ? 14      38.852  10.149  1 35.64  ? 7   DT  F C5    1 1 
ATOM   5724 C  C7    . DT  C 3 7   ? 14.028  38.997  8.664   1 35.64  ? 7   DT  F C7    1 1 
ATOM   5725 C  C6    . DT  C 3 7   ? 13.999  39.918  10.961  1 36.04  ? 7   DT  F C6    1 1 
ATOM   5726 P  P     . DG  C 3 8   ? 17.677  44.065  13.496  1 44.45  ? 8   DG  F P     1 1 
ATOM   5727 O  OP1   . DG  C 3 8   ? 17.938  45.431  14.017  1 44.3   ? 8   DG  F OP1   1 1 
ATOM   5728 O  OP2   . DG  C 3 8   ? 18.206  43.661  12.173  1 44.62  ? 8   DG  F OP2   1 1 
ATOM   5729 O  "O5'" . DG  C 3 8   ? 18.154  42.994  14.567  1 46.18  ? 8   DG  F "O5'" 1 ? 
ATOM   5730 C  "C5'" . DG  C 3 8   ? 17.53   42.948  15.839  1 47.92  ? 8   DG  F "C5'" 1 ? 
ATOM   5731 C  "C4'" . DG  C 3 8   ? 18.025  41.755  16.614  1 49.74  ? 8   DG  F "C4'" 1 ? 
ATOM   5732 O  "O4'" . DG  C 3 8   ? 17.523  40.537  16.006  1 49.39  ? 8   DG  F "O4'" 1 ? 
ATOM   5733 C  "C3'" . DG  C 3 8   ? 19.546  41.622  16.649  1 51.85  ? 8   DG  F "C3'" 1 ? 
ATOM   5734 O  "O3'" . DG  C 3 8   ? 19.958  41.272  17.941  1 55.04  ? 8   DG  F "O3'" 1 ? 
ATOM   5735 C  "C2'" . DG  C 3 8   ? 19.822  40.509  15.65   1 50.59  ? 8   DG  F "C2'" 1 ? 
ATOM   5736 C  "C1'" . DG  C 3 8   ? 18.59   39.645  15.8    1 49.29  ? 8   DG  F "C1'" 1 ? 
ATOM   5737 N  N9    . DG  C 3 8   ? 18.313  38.862  14.606  1 48.01  ? 8   DG  F N9    1 1 
ATOM   5738 C  C8    . DG  C 3 8   ? 18.296  39.315  13.309  1 47.63  ? 8   DG  F C8    1 1 
ATOM   5739 N  N7    . DG  C 3 8   ? 18.074  38.377  12.43   1 47.09  ? 8   DG  F N7    1 1 
ATOM   5740 C  C5    . DG  C 3 8   ? 17.942  37.224  13.194  1 46.55  ? 8   DG  F C5    1 1 
ATOM   5741 C  C6    . DG  C 3 8   ? 17.69   35.896  12.793  1 45.57  ? 8   DG  F C6    1 1 
ATOM   5742 O  O6    . DG  C 3 8   ? 17.518  35.468  11.642  1 44.96  ? 8   DG  F O6    1 1 
ATOM   5743 N  N1    . DG  C 3 8   ? 17.66   35.024  13.887  1 45.5   ? 8   DG  F N1    1 1 
ATOM   5744 C  C2    . DG  C 3 8   ? 17.823  35.405  15.204  1 45.72  ? 8   DG  F C2    1 1 
ATOM   5745 N  N2    . DG  C 3 8   ? 17.766  34.432  16.126  1 45.44  ? 8   DG  F N2    1 1 
ATOM   5746 N  N3    . DG  C 3 8   ? 18.052  36.65   15.587  1 46.44  ? 8   DG  F N3    1 1 
ATOM   5747 C  C4    . DG  C 3 8   ? 18.116  37.501  14.534  1 47.02  ? 8   DG  F C4    1 1 
ATOM   5748 P  P     . DC  C 3 9   ? 21.478  41.477  18.416  1 57.98  ? 9   DC  F P     1 1 
ATOM   5749 O  OP1   . DC  C 3 9   ? 21.509  42.609  19.375  1 58.31  ? 9   DC  F OP1   1 1 
ATOM   5750 O  OP2   . DC  C 3 9   ? 22.37   41.494  17.225  1 58.14  ? 9   DC  F OP2   1 1 
ATOM   5751 O  "O5'" . DC  C 3 9   ? 21.721  40.121  19.213  1 59.67  ? 9   DC  F "O5'" 1 ? 
ATOM   5752 C  "C5'" . DC  C 3 9   ? 20.628  39.53   19.913  1 61.34  ? 9   DC  F "C5'" 1 ? 
ATOM   5753 C  "C4'" . DC  C 3 9   ? 20.878  38.064  20.17   1 63.15  ? 9   DC  F "C4'" 1 ? 
ATOM   5754 O  "O4'" . DC  C 3 9   ? 20.486  37.284  19.008  1 63.37  ? 9   DC  F "O4'" 1 ? 
ATOM   5755 C  "C3'" . DC  C 3 9   ? 22.327  37.703  20.454  1 64.67  ? 9   DC  F "C3'" 1 ? 
ATOM   5756 O  "O3'" . DC  C 3 9   ? 22.373  36.693  21.443  1 66.8   ? 9   DC  F "O3'" 1 ? 
ATOM   5757 C  "C2'" . DC  C 3 9   ? 22.821  37.197  19.104  1 64.04  ? 9   DC  F "C2'" 1 ? 
ATOM   5758 C  "C1'" . DC  C 3 9   ? 21.577  36.501  18.565  1 63.42  ? 9   DC  F "C1'" 1 ? 
ATOM   5759 N  N1    . DC  C 3 9   ? 21.529  36.455  17.078  1 62.78  ? 9   DC  F N1    1 1 
ATOM   5760 C  C2    . DC  C 3 9   ? 21.296  35.242  16.414  1 62.15  ? 9   DC  F C2    1 1 
ATOM   5761 O  O2    . DC  C 3 9   ? 21.125  34.212  17.078  1 61.71  ? 9   DC  F O2    1 1 
ATOM   5762 N  N3    . DC  C 3 9   ? 21.246  35.243  15.054  1 62.14  ? 9   DC  F N3    1 1 
ATOM   5763 C  C4    . DC  C 3 9   ? 21.415  36.393  14.38   1 62.29  ? 9   DC  F C4    1 1 
ATOM   5764 N  N4    . DC  C 3 9   ? 21.367  36.362  13.045  1 62.21  ? 9   DC  F N4    1 1 
ATOM   5765 C  C5    . DC  C 3 9   ? 21.665  37.622  15.044  1 62.52  ? 9   DC  F C5    1 1 
ATOM   5766 C  C6    . DC  C 3 9   ? 21.71   37.609  16.375  1 62.7   ? 9   DC  F C6    1 1 
ATOM   5767 P  P     . DA  C 3 10  ? 23.734  36.407  22.234  1 68.8   ? 10  DA  F P     1 1 
ATOM   5768 O  OP1   . DA  C 3 10  ? 23.389  36.168  23.661  1 69.02  ? 10  DA  F OP1   1 1 
ATOM   5769 O  OP2   . DA  C 3 10  ? 24.71   37.466  21.862  1 68.97  ? 10  DA  F OP2   1 1 
ATOM   5770 O  "O5'" . DA  C 3 10  ? 24.224  35.034  21.587  1 69.58  ? 10  DA  F "O5'" 1 ? 
ATOM   5771 C  "C5'" . DA  C 3 10  ? 23.251  34.139  21.042  1 70.27  ? 10  DA  F "C5'" 1 ? 
ATOM   5772 C  "C4'" . DA  C 3 10  ? 23.878  32.881  20.481  1 70.79  ? 10  DA  F "C4'" 1 ? 
ATOM   5773 O  "O4'" . DA  C 3 10  ? 23.746  32.874  19.041  1 70.65  ? 10  DA  F "O4'" 1 ? 
ATOM   5774 C  "C3'" . DA  C 3 10  ? 25.352  32.694  20.783  1 71.48  ? 10  DA  F "C3'" 1 ? 
ATOM   5775 O  "O3'" . DA  C 3 10  ? 25.624  31.322  20.991  1 72.5   ? 10  DA  F "O3'" 1 ? 
ATOM   5776 C  "C2'" . DA  C 3 10  ? 26.035  33.249  19.532  1 71.01  ? 10  DA  F "C2'" 1 ? 
ATOM   5777 C  "C1'" . DA  C 3 10  ? 25.019  32.948  18.431  1 70.4   ? 10  DA  F "C1'" 1 ? 
ATOM   5778 N  N9    . DA  C 3 10  ? 24.97   33.971  17.383  1 69.43  ? 10  DA  F N9    1 1 
ATOM   5779 C  C8    . DA  C 3 10  ? 25.02   35.328  17.545  1 68.97  ? 10  DA  F C8    1 1 
ATOM   5780 N  N7    . DA  C 3 10  ? 24.928  36.003  16.426  1 68.62  ? 10  DA  F N7    1 1 
ATOM   5781 C  C5    . DA  C 3 10  ? 24.849  35.018  15.458  1 68.52  ? 10  DA  F C5    1 1 
ATOM   5782 C  C6    . DA  C 3 10  ? 24.761  35.076  14.059  1 68.24  ? 10  DA  F C6    1 1 
ATOM   5783 N  N6    . DA  C 3 10  ? 24.743  36.223  13.375  1 68.19  ? 10  DA  F N6    1 1 
ATOM   5784 N  N1    . DA  C 3 10  ? 24.694  33.907  13.388  1 68.1   ? 10  DA  F N1    1 1 
ATOM   5785 C  C2    . DA  C 3 10  ? 24.729  32.765  14.08   1 68.18  ? 10  DA  F C2    1 1 
ATOM   5786 N  N3    . DA  C 3 10  ? 24.803  32.584  15.394  1 68.44  ? 10  DA  F N3    1 1 
ATOM   5787 C  C4    . DA  C 3 10  ? 24.874  33.761  16.03   1 68.79  ? 10  DA  F C4    1 1 
ATOM   5788 P  P     . DG  C 3 11  ? 26.906  30.867  21.842  1 73.15  ? 11  DG  F P     1 1 
ATOM   5789 O  OP1   . DG  C 3 11  ? 26.414  30.101  23.02   1 73.17  ? 11  DG  F OP1   1 1 
ATOM   5790 O  OP2   . DG  C 3 11  ? 27.796  32.054  22.031  1 73.13  ? 11  DG  F OP2   1 1 
ATOM   5791 O  "O5'" . DG  C 3 11  ? 27.625  29.858  20.828  1 72.97  ? 11  DG  F "O5'" 1 ? 
ATOM   5792 C  "C5'" . DG  C 3 11  ? 26.819  28.998  20.022  1 72.62  ? 11  DG  F "C5'" 1 ? 
ATOM   5793 C  "C4'" . DG  C 3 11  ? 27.52   28.616  18.732  1 72.12  ? 11  DG  F "C4'" 1 ? 
ATOM   5794 O  "O4'" . DG  C 3 11  ? 27.347  29.654  17.735  1 71.54  ? 11  DG  F "O4'" 1 ? 
ATOM   5795 C  "C3'" . DG  C 3 11  ? 29.021  28.379  18.841  1 72.17  ? 11  DG  F "C3'" 1 ? 
ATOM   5796 O  "O3'" . DG  C 3 11  ? 29.352  27.254  18.05   1 72.81  ? 11  DG  F "O3'" 1 ? 
ATOM   5797 C  "C2'" . DG  C 3 11  ? 29.611  29.664  18.258  1 71.5   ? 11  DG  F "C2'" 1 ? 
ATOM   5798 C  "C1'" . DG  C 3 11  ? 28.598  29.967  17.174  1 71.02  ? 11  DG  F "C1'" 1 ? 
ATOM   5799 N  N9    . DG  C 3 11  ? 28.572  31.36   16.75   1 70.15  ? 11  DG  F N9    1 1 
ATOM   5800 C  C8    . DG  C 3 11  ? 28.619  32.476  17.549  1 69.8   ? 11  DG  F C8    1 1 
ATOM   5801 N  N7    . DG  C 3 11  ? 28.495  33.595  16.886  1 69.5   ? 11  DG  F N7    1 1 
ATOM   5802 C  C5    . DG  C 3 11  ? 28.38   33.194  15.56   1 69.24  ? 11  DG  F C5    1 1 
ATOM   5803 C  C6    . DG  C 3 11  ? 28.248  33.965  14.381  1 68.77  ? 11  DG  F C6    1 1 
ATOM   5804 O  O6    . DG  C 3 11  ? 28.218  35.201  14.27   1 68.62  ? 11  DG  F O6    1 1 
ATOM   5805 N  N1    . DG  C 3 11  ? 28.158  33.158  13.245  1 68.63  ? 11  DG  F N1    1 1 
ATOM   5806 C  C2    . DG  C 3 11  ? 28.186  31.78   13.255  1 68.84  ? 11  DG  F C2    1 1 
ATOM   5807 N  N2    . DG  C 3 11  ? 28.087  31.168  12.067  1 68.67  ? 11  DG  F N2    1 1 
ATOM   5808 N  N3    . DG  C 3 11  ? 28.321  31.052  14.351  1 69.3   ? 11  DG  F N3    1 1 
ATOM   5809 C  C4    . DG  C 3 11  ? 28.415  31.822  15.462  1 69.59  ? 11  DG  F C4    1 1 
ATOM   5810 P  P     . DA  C 3 12  ? 30.583  26.314  18.439  1 73.24  ? 12  DA  F P     1 1 
ATOM   5811 O  OP1   . DA  C 3 12  ? 30.036  24.976  18.787  1 73.07  ? 12  DA  F OP1   1 1 
ATOM   5812 O  OP2   . DA  C 3 12  ? 31.45   27.044  19.4    1 73.3   ? 12  DA  F OP2   1 1 
ATOM   5813 O  "O5'" . DA  C 3 12  ? 31.367  26.22   17.053  1 73.35  ? 12  DA  F "O5'" 1 ? 
ATOM   5814 C  "C5'" . DA  C 3 12  ? 30.625  26.143  15.842  1 73.3   ? 12  DA  F "C5'" 1 ? 
ATOM   5815 C  "C4'" . DA  C 3 12  ? 31.371  26.799  14.696  1 73.14  ? 12  DA  F "C4'" 1 ? 
ATOM   5816 O  "O4'" . DA  C 3 12  ? 31.005  28.192  14.612  1 72.84  ? 12  DA  F "O4'" 1 ? 
ATOM   5817 C  "C3'" . DA  C 3 12  ? 32.902  26.756  14.786  1 73.29  ? 12  DA  F "C3'" 1 ? 
ATOM   5818 O  "O3'" . DA  C 3 12  ? 33.42   26.063  13.66   1 74.02  ? 12  DA  F "O3'" 1 ? 
ATOM   5819 C  "C2'" . DA  C 3 12  ? 33.32   28.231  14.784  1 72.8   ? 12  DA  F "C2'" 1 ? 
ATOM   5820 C  "C1'" . DA  C 3 12  ? 32.116  28.919  14.165  1 72.37  ? 12  DA  F "C1'" 1 ? 
ATOM   5821 N  N9    . DA  C 3 12  ? 31.971  30.299  14.607  1 71.52  ? 12  DA  F N9    1 1 
ATOM   5822 C  C8    . DA  C 3 12  ? 32.098  30.764  15.886  1 71.24  ? 12  DA  F C8    1 1 
ATOM   5823 N  N7    . DA  C 3 12  ? 31.965  32.062  15.993  1 70.92  ? 12  DA  F N7    1 1 
ATOM   5824 C  C5    . DA  C 3 12  ? 31.753  32.482  14.692  1 70.71  ? 12  DA  F C5    1 1 
ATOM   5825 C  C6    . DA  C 3 12  ? 31.545  33.755  14.136  1 70.42  ? 12  DA  F C6    1 1 
ATOM   5826 N  N6    . DA  C 3 12  ? 31.504  34.873  14.867  1 70.29  ? 12  DA  F N6    1 1 
ATOM   5827 N  N1    . DA  C 3 12  ? 31.382  33.834  12.796  1 70.38  ? 12  DA  F N1    1 1 
ATOM   5828 C  C2    . DA  C 3 12  ? 31.424  32.705  12.072  1 70.45  ? 12  DA  F C2    1 1 
ATOM   5829 N  N3    . DA  C 3 12  ? 31.602  31.449  12.485  1 70.57  ? 12  DA  F N3    1 1 
ATOM   5830 C  C4    . DA  C 3 12  ? 31.77   31.409  13.819  1 70.9   ? 12  DA  F C4    1 1 
ATOM   5831 P  P     . DC  C 3 13  ? 34.984  25.701  13.537  1 74.64  ? 13  DC  F P     1 1 
ATOM   5832 O  OP1   . DC  C 3 13  ? 35.071  24.302  13.039  1 74.55  ? 13  DC  F OP1   1 1 
ATOM   5833 O  OP2   . DC  C 3 13  ? 35.674  26.09   14.795  1 74.73  ? 13  DC  F OP2   1 1 
ATOM   5834 O  "O5'" . DC  C 3 13  ? 35.472  26.707  12.381  1 74.64  ? 13  DC  F "O5'" 1 ? 
ATOM   5835 C  "C5'" . DC  C 3 13  ? 34.551  27.077  11.336  1 74.47  ? 13  DC  F "C5'" 1 ? 
ATOM   5836 C  "C4'" . DC  C 3 13  ? 34.925  28.403  10.692  1 74.11  ? 13  DC  F "C4'" 1 ? 
ATOM   5837 O  "O4'" . DC  C 3 13  ? 34.479  29.498  11.514  1 73.83  ? 13  DC  F "O4'" 1 ? 
ATOM   5838 C  "C3'" . DC  C 3 13  ? 36.419  28.622  10.473  1 74.02  ? 13  DC  F "C3'" 1 ? 
ATOM   5839 O  "O3'" . DC  C 3 13  ? 36.717  28.512  9.093   1 74.18  ? 13  DC  F "O3'" 1 ? 
ATOM   5840 C  "C2'" . DC  C 3 13  ? 36.688  30.045  10.998  1 73.75  ? 13  DC  F "C2'" 1 ? 
ATOM   5841 C  "C1'" . DC  C 3 13  ? 35.29   30.606  11.248  1 73.47  ? 13  DC  F "C1'" 1 ? 
ATOM   5842 N  N1    . DC  C 3 13  ? 35.231  31.507  12.417  1 73.04  ? 13  DC  F N1    1 1 
ATOM   5843 C  C2    . DC  C 3 13  ? 35.076  32.883  12.228  1 72.91  ? 13  DC  F C2    1 1 
ATOM   5844 O  O2    . DC  C 3 13  ? 34.956  33.321  11.078  1 72.9   ? 13  DC  F O2    1 1 
ATOM   5845 N  N3    . DC  C 3 13  ? 35.04   33.695  13.317  1 72.82  ? 13  DC  F N3    1 1 
ATOM   5846 C  C4    . DC  C 3 13  ? 35.168  33.172  14.541  1 72.89  ? 13  DC  F C4    1 1 
ATOM   5847 N  N4    . DC  C 3 13  ? 35.131  34.003  15.586  1 72.86  ? 13  DC  F N4    1 1 
ATOM   5848 C  C5    . DC  C 3 13  ? 35.338  31.773  14.748  1 72.95  ? 13  DC  F C5    1 1 
ATOM   5849 C  C6    . DC  C 3 13  ? 35.381  30.991  13.668  1 72.98  ? 13  DC  F C6    1 1 
ATOM   5850 C  "C5'" . DG  D 4 1   ? 35.285  44.513  10.896  1 71.76  ? 1   DG  G "C5'" 1 ? 
ATOM   5851 C  "C4'" . DG  D 4 1   ? 34.76   43.338  10.081  1 71.88  ? 1   DG  G "C4'" 1 ? 
ATOM   5852 O  "O4'" . DG  D 4 1   ? 35.264  42.084  10.643  1 71.77  ? 1   DG  G "O4'" 1 ? 
ATOM   5853 C  "C3'" . DG  D 4 1   ? 33.222  43.192  10.047  1 71.93  ? 1   DG  G "C3'" 1 ? 
ATOM   5854 O  "O3'" . DG  D 4 1   ? 32.786  42.789  8.722   1 71.92  ? 1   DG  G "O3'" 1 ? 
ATOM   5855 C  "C2'" . DG  D 4 1   ? 32.988  42.087  11.064  1 71.78  ? 1   DG  G "C2'" 1 ? 
ATOM   5856 C  "C1'" . DG  D 4 1   ? 34.18   41.197  10.788  1 71.52  ? 1   DG  G "C1'" 1 ? 
ATOM   5857 N  N9    . DG  D 4 1   ? 34.436  40.273  11.872  1 70.96  ? 1   DG  G N9    1 1 
ATOM   5858 C  C8    . DG  D 4 1   ? 34.451  40.575  13.213  1 70.78  ? 1   DG  G C8    1 1 
ATOM   5859 N  N7    . DG  D 4 1   ? 34.523  39.527  13.978  1 70.64  ? 1   DG  G N7    1 1 
ATOM   5860 C  C5    . DG  D 4 1   ? 34.462  38.462  13.093  1 70.62  ? 1   DG  G C5    1 1 
ATOM   5861 C  C6    . DG  D 4 1   ? 34.517  37.076  13.343  1 70.58  ? 1   DG  G C6    1 1 
ATOM   5862 O  O6    . DG  D 4 1   ? 34.607  36.507  14.432  1 70.57  ? 1   DG  G O6    1 1 
ATOM   5863 N  N1    . DG  D 4 1   ? 34.463  36.334  12.164  1 70.52  ? 1   DG  G N1    1 1 
ATOM   5864 C  C2    . DG  D 4 1   ? 34.357  36.874  10.902  1 70.54  ? 1   DG  G C2    1 1 
ATOM   5865 N  N2    . DG  D 4 1   ? 34.306  36.001  9.884   1 70.46  ? 1   DG  G N2    1 1 
ATOM   5866 N  N3    . DG  D 4 1   ? 34.316  38.18   10.654  1 70.57  ? 1   DG  G N3    1 1 
ATOM   5867 C  C4    . DG  D 4 1   ? 34.38   38.908  11.795  1 70.68  ? 1   DG  G C4    1 1 
ATOM   5868 P  P     . DT  D 4 2   ? 31.219  42.578  8.368   1 71.66  ? 2   DT  G P     1 1 
ATOM   5869 O  OP1   . DT  D 4 2   ? 30.892  43.469  7.225   1 71.75  ? 2   DT  G OP1   1 1 
ATOM   5870 O  OP2   . DT  D 4 2   ? 30.422  42.675  9.617   1 71.66  ? 2   DT  G OP2   1 1 
ATOM   5871 O  "O5'" . DT  D 4 2   ? 31.173  41.038  7.869   1 70.68  ? 2   DT  G "O5'" 1 ? 
ATOM   5872 C  "C5'" . DT  D 4 2   ? 31.905  40.63   6.676   1 69.39  ? 2   DT  G "C5'" 1 ? 
ATOM   5873 C  "C4'" . DT  D 4 2   ? 31.695  39.151  6.335   1 67.87  ? 2   DT  G "C4'" 1 ? 
ATOM   5874 O  "O4'" . DT  D 4 2   ? 32.068  38.32   7.466   1 67.27  ? 2   DT  G "O4'" 1 ? 
ATOM   5875 C  "C3'" . DT  D 4 2   ? 30.267  38.75   5.969   1 66.93  ? 2   DT  G "C3'" 1 ? 
ATOM   5876 O  "O3'" . DT  D 4 2   ? 30.274  37.734  4.944   1 66.24  ? 2   DT  G "O3'" 1 ? 
ATOM   5877 C  "C2'" . DT  D 4 2   ? 29.742  38.207  7.287   1 66.77  ? 2   DT  G "C2'" 1 ? 
ATOM   5878 C  "C1'" . DT  D 4 2   ? 30.977  37.514  7.848   1 66.68  ? 2   DT  G "C1'" 1 ? 
ATOM   5879 N  N1    . DT  D 4 2   ? 30.974  37.414  9.339   1 66.13  ? 2   DT  G N1    1 1 
ATOM   5880 C  C2    . DT  D 4 2   ? 31.21   36.194  9.949   1 65.6   ? 2   DT  G C2    1 1 
ATOM   5881 O  O2    . DT  D 4 2   ? 31.424  35.162  9.335   1 65.08  ? 2   DT  G O2    1 1 
ATOM   5882 N  N3    . DT  D 4 2   ? 31.184  36.233  11.322  1 65.78  ? 2   DT  G N3    1 1 
ATOM   5883 C  C4    . DT  D 4 2   ? 30.947  37.343  12.126  1 66.02  ? 2   DT  G C4    1 1 
ATOM   5884 O  O4    . DT  D 4 2   ? 30.952  37.226  13.348  1 66.11  ? 2   DT  G O4    1 1 
ATOM   5885 C  C5    . DT  D 4 2   ? 30.701  38.575  11.42   1 66.07  ? 2   DT  G C5    1 1 
ATOM   5886 C  C7    . DT  D 4 2   ? 30.414  39.833  12.183  1 66.01  ? 2   DT  G C7    1 1 
ATOM   5887 C  C6    . DT  D 4 2   ? 30.725  38.552  10.081  1 66.11  ? 2   DT  G C6    1 1 
ATOM   5888 P  P     . DC  D 4 3   ? 28.973  37.486  4.005   1 65.53  ? 3   DC  G P     1 1 
ATOM   5889 O  OP1   . DC  D 4 3   ? 29.445  37.426  2.597   1 65.77  ? 3   DC  G OP1   1 1 
ATOM   5890 O  OP2   . DC  D 4 3   ? 27.913  38.453  4.391   1 65.45  ? 3   DC  G OP2   1 1 
ATOM   5891 O  "O5'" . DC  D 4 3   ? 28.491  36.014  4.422   1 64.07  ? 3   DC  G "O5'" 1 ? 
ATOM   5892 C  "C5'" . DC  D 4 3   ? 29.358  34.895  4.205   1 62.5   ? 3   DC  G "C5'" 1 ? 
ATOM   5893 C  "C4'" . DC  D 4 3   ? 28.823  33.643  4.881   1 60.73  ? 3   DC  G "C4'" 1 ? 
ATOM   5894 O  "O4'" . DC  D 4 3   ? 29.012  33.74   6.318   1 59.86  ? 3   DC  G "O4'" 1 ? 
ATOM   5895 C  "C3'" . DC  D 4 3   ? 27.338  33.366  4.664   1 59.76  ? 3   DC  G "C3'" 1 ? 
ATOM   5896 O  "O3'" . DC  D 4 3   ? 27.141  31.975  4.403   1 58.98  ? 3   DC  G "O3'" 1 ? 
ATOM   5897 C  "C2'" . DC  D 4 3   ? 26.711  33.786  5.992   1 59.37  ? 3   DC  G "C2'" 1 ? 
ATOM   5898 C  "C1'" . DC  D 4 3   ? 27.809  33.433  6.978   1 58.89  ? 3   DC  G "C1'" 1 ? 
ATOM   5899 N  N1    . DC  D 4 3   ? 27.761  34.226  8.232   1 57.59  ? 3   DC  G N1    1 1 
ATOM   5900 C  C2    . DC  D 4 3   ? 27.834  33.58   9.467   1 56.93  ? 3   DC  G C2    1 1 
ATOM   5901 O  O2    . DC  D 4 3   ? 27.916  32.349  9.495   1 56.72  ? 3   DC  G O2    1 1 
ATOM   5902 N  N3    . DC  D 4 3   ? 27.815  34.328  10.602  1 56.81  ? 3   DC  G N3    1 1 
ATOM   5903 C  C4    . DC  D 4 3   ? 27.735  35.662  10.522  1 56.95  ? 3   DC  G C4    1 1 
ATOM   5904 N  N4    . DC  D 4 3   ? 27.725  36.37   11.661  1 56.87  ? 3   DC  G N4    1 1 
ATOM   5905 C  C5    . DC  D 4 3   ? 27.647  36.328  9.271   1 57.16  ? 3   DC  G C5    1 1 
ATOM   5906 C  C6    . DC  D 4 3   ? 27.675  35.578  8.164   1 57.33  ? 3   DC  G C6    1 1 
ATOM   5907 P  P     . DT  D 4 4   ? 25.79   31.46   3.709   1 58.09  ? 4   DT  G P     1 1 
ATOM   5908 O  OP1   . DT  D 4 4   ? 26.157  30.711  2.481   1 58.32  ? 4   DT  G OP1   1 1 
ATOM   5909 O  OP2   . DT  D 4 4   ? 24.841  32.599  3.624   1 58.14  ? 4   DT  G OP2   1 1 
ATOM   5910 O  "O5'" . DT  D 4 4   ? 25.238  30.434  4.789   1 56.68  ? 4   DT  G "O5'" 1 ? 
ATOM   5911 C  "C5'" . DT  D 4 4   ? 26.156  29.727  5.599   1 55.26  ? 4   DT  G "C5'" 1 ? 
ATOM   5912 C  "C4'" . DT  D 4 4   ? 25.514  29.307  6.9     1 53.93  ? 4   DT  G "C4'" 1 ? 
ATOM   5913 O  "O4'" . DT  D 4 4   ? 25.628  30.381  7.862   1 53.07  ? 4   DT  G "O4'" 1 ? 
ATOM   5914 C  "C3'" . DT  D 4 4   ? 24.017  28.96   6.812   1 53.46  ? 4   DT  G "C3'" 1 ? 
ATOM   5915 O  "O3'" . DT  D 4 4   ? 23.792  27.679  7.404   1 53.28  ? 4   DT  G "O3'" 1 ? 
ATOM   5916 C  "C2'" . DT  D 4 4   ? 23.345  30.087  7.608   1 52.99  ? 4   DT  G "C2'" 1 ? 
ATOM   5917 C  "C1'" . DT  D 4 4   ? 24.434  30.446  8.596   1 52.41  ? 4   DT  G "C1'" 1 ? 
ATOM   5918 N  N1    . DT  D 4 4   ? 24.303  31.798  9.159   1 51.21  ? 4   DT  G N1    1 1 
ATOM   5919 C  C2    . DT  D 4 4   ? 24.248  31.942  10.516  1 50.63  ? 4   DT  G C2    1 1 
ATOM   5920 O  O2    . DT  D 4 4   ? 24.301  30.998  11.285  1 50.48  ? 4   DT  G O2    1 1 
ATOM   5921 N  N3    . DT  D 4 4   ? 24.167  33.24   10.95   1 50.39  ? 4   DT  G N3    1 1 
ATOM   5922 C  C4    . DT  D 4 4   ? 24.115  34.383  10.163  1 50.29  ? 4   DT  G C4    1 1 
ATOM   5923 O  O4    . DT  D 4 4   ? 24.027  35.487  10.694  1 50.11  ? 4   DT  G O4    1 1 
ATOM   5924 C  C5    . DT  D 4 4   ? 24.16   34.154  8.742   1 50.43  ? 4   DT  G C5    1 1 
ATOM   5925 C  C7    . DT  D 4 4   ? 24.096  35.315  7.791   1 50.34  ? 4   DT  G C7    1 1 
ATOM   5926 C  C6    . DT  D 4 4   ? 24.239  32.885  8.313   1 50.76  ? 4   DT  G C6    1 1 
ATOM   5927 P  P     . DG  D 4 5   ? 22.399  26.901  7.22    1 52.91  ? 5   DG  G P     1 1 
ATOM   5928 O  OP1   . DG  D 4 5   ? 22.676  25.651  6.465   1 52.78  ? 5   DG  G OP1   1 1 
ATOM   5929 O  OP2   . DG  D 4 5   ? 21.379  27.855  6.727   1 52.84  ? 5   DG  G OP2   1 1 
ATOM   5930 O  "O5'" . DG  D 4 5   ? 22.028  26.529  8.735   1 52.5   ? 5   DG  G "O5'" 1 ? 
ATOM   5931 C  "C5'" . DG  D 4 5   ? 23.053  26.015  9.608   1 51.9   ? 5   DG  G "C5'" 1 ? 
ATOM   5932 C  "C4'" . DG  D 4 5   ? 22.67   26.138  11.08   1 51.21  ? 5   DG  G "C4'" 1 ? 
ATOM   5933 O  "O4'" . DG  D 4 5   ? 22.779  27.521  11.514  1 50.92  ? 5   DG  G "O4'" 1 ? 
ATOM   5934 C  "C3'" . DG  D 4 5   ? 21.256  25.684  11.435  1 50.77  ? 5   DG  G "C3'" 1 ? 
ATOM   5935 O  "O3'" . DG  D 4 5   ? 21.279  24.953  12.646  1 50.58  ? 5   DG  G "O3'" 1 ? 
ATOM   5936 C  "C2'" . DG  D 4 5   ? 20.5    26.997  11.589  1 50.6   ? 5   DG  G "C2'" 1 ? 
ATOM   5937 C  "C1'" . DG  D 4 5   ? 21.58   27.916  12.139  1 50.49  ? 5   DG  G "C1'" 1 ? 
ATOM   5938 N  N9    . DG  D 4 5   ? 21.338  29.322  11.83   1 49.92  ? 5   DG  G N9    1 1 
ATOM   5939 C  C8    . DG  D 4 5   ? 21.013  29.853  10.602  1 49.6   ? 5   DG  G C8    1 1 
ATOM   5940 N  N7    . DG  D 4 5   ? 20.817  31.141  10.629  1 49.38  ? 5   DG  G N7    1 1 
ATOM   5941 C  C5    . DG  D 4 5   ? 21      31.486  11.964  1 49.35  ? 5   DG  G C5    1 1 
ATOM   5942 C  C6    . DG  D 4 5   ? 20.894  32.746  12.6    1 49.14  ? 5   DG  G C6    1 1 
ATOM   5943 O  O6    . DG  D 4 5   ? 20.603  33.831  12.092  1 49     ? 5   DG  G O6    1 1 
ATOM   5944 N  N1    . DG  D 4 5   ? 21.142  32.663  13.97   1 49.14  ? 5   DG  G N1    1 1 
ATOM   5945 C  C2    . DG  D 4 5   ? 21.453  31.504  14.641  1 49.33  ? 5   DG  G C2    1 1 
ATOM   5946 N  N2    . DG  D 4 5   ? 21.665  31.623  15.962  1 49.31  ? 5   DG  G N2    1 1 
ATOM   5947 N  N3    . DG  D 4 5   ? 21.572  30.312  14.054  1 49.55  ? 5   DG  G N3    1 1 
ATOM   5948 C  C4    . DG  D 4 5   ? 21.313  30.378  12.72   1 49.62  ? 5   DG  G C4    1 1 
HETATM 5949 MG MG    . MG  E 5 .   ? 18.107  19.149  9.194   1 202.98 2 701 MG  A MG    1 1 
HETATM 5950 CL CL    . CL  F 6 .   ? -9.365  17.28   6.931   1 47.82  ? 702 CL  A CL    1 1 
HETATM 5951 O  O1    . MES G 7 .   ? 0.601   50.248  -21.277 1 63.87  ? 703 MES A O1    1 1 
HETATM 5952 C  C2    . MES G 7 .   ? 0.337   49.182  -20.362 1 63.83  ? 703 MES A C2    1 1 
HETATM 5953 C  C3    . MES G 7 .   ? -0.879  49.471  -19.514 1 63.83  ? 703 MES A C3    1 1 
HETATM 5954 N  N4    . MES G 7 .   ? -0.703  50.77   -18.783 1 63.98  ? 703 MES A N4    1 1 
HETATM 5955 C  C5    . MES G 7 .   ? -0.345  51.874  -19.739 1 64.02  ? 703 MES A C5    1 1 
HETATM 5956 C  C6    . MES G 7 .   ? 0.848   51.468  -20.574 1 63.96  ? 703 MES A C6    1 1 
HETATM 5957 C  C7    . MES G 7 .   ? -1.966  51.103  -18.039 1 64.26  ? 703 MES A C7    1 1 
HETATM 5958 C  C8    . MES G 7 .   ? -1.752  51.905  -16.772 1 64.57  ? 703 MES A C8    1 1 
HETATM 5959 S  S     . MES G 7 .   ? -3.341  52.178  -16.023 1 64.82  ? 703 MES A S     1 1 
HETATM 5960 O  O1S   . MES G 7 .   ? -4.231  51.166  -16.572 1 64.83  ? 703 MES A O1S   1 1 
HETATM 5961 O  O2S   . MES G 7 .   ? -3.728  53.53   -16.378 1 64.81  ? 703 MES A O2S   1 1 
HETATM 5962 O  O3S   . MES G 7 .   ? -3.142  52.022  -14.588 1 65.03  ? 703 MES A O3S   1 1 
HETATM 5963 O  O     . HOH H 8 .   ? 26.45   -1.565  30.595  1 9.13   ? 801 HOH A O     1 1 
HETATM 5964 O  O     . HOH H 8 .   ? 19.952  41.418  12.223  1 27.94  ? 802 HOH A O     1 1 
HETATM 5965 O  O     . HOH H 8 .   ? -2.486  33.621  3.944   1 13.5   ? 803 HOH A O     1 1 
HETATM 5966 O  O     . HOH H 8 .   ? 32.661  7.831   51.366  1 13.87  ? 804 HOH A O     1 1 
HETATM 5967 O  O     . HOH H 8 .   ? 10.984  -2.662  19.105  1 10.85  ? 805 HOH A O     1 1 
HETATM 5968 O  O     . HOH H 8 .   ? 1.514   42.697  -4.632  1 46.54  ? 806 HOH A O     1 1 
HETATM 5969 O  O     . HOH H 8 .   ? 13.01   21.296  4.141   1 12.38  ? 807 HOH A O     1 1 
HETATM 5970 O  O     . HOH H 8 .   ? 31.329  17.14   48.142  1 18.98  ? 808 HOH A O     1 1 
HETATM 5971 O  O     . HOH H 8 .   ? 6.562   23.512  24.527  1 9.85   ? 809 HOH A O     1 1 
HETATM 5972 O  O     . HOH H 8 .   ? -2.06   13.638  35.661  1 12.77  ? 810 HOH A O     1 1 
HETATM 5973 O  O     . HOH H 8 .   ? -9.095  9.362   12.313  1 15.94  ? 811 HOH A O     1 1 
HETATM 5974 O  O     . HOH H 8 .   ? 21.782  1.879   37.71   1 21.73  ? 812 HOH A O     1 1 
HETATM 5975 O  O     . HOH H 8 .   ? 26.664  6.134   -7.44   1 13.43  ? 813 HOH A O     1 1 
HETATM 5976 O  O     . HOH H 8 .   ? 10.023  21.868  -9.336  1 12.27  ? 814 HOH A O     1 1 
HETATM 5977 O  O     . HOH H 8 .   ? -9.477  27.605  2.297   1 19.42  ? 815 HOH A O     1 1 
HETATM 5978 O  O     . HOH H 8 .   ? 13.925  25.906  42.213  1 26.35  ? 816 HOH A O     1 1 
HETATM 5979 O  O     . HOH H 8 .   ? 10.875  15.246  15.36   1 16.37  ? 817 HOH A O     1 1 
HETATM 5980 O  O     . HOH H 8 .   ? 22.184  -17.738 15.235  1 14.34  ? 818 HOH A O     1 1 
HETATM 5981 O  O     . HOH H 8 .   ? 12.245  -11.066 15.359  1 21.05  ? 819 HOH A O     1 1 
HETATM 5982 O  O     . HOH H 8 .   ? 26.5    -14.583 16.336  1 12.89  ? 820 HOH A O     1 1 
HETATM 5983 O  O     . HOH H 8 .   ? 26.284  59.564  3.057   1 27.51  ? 821 HOH A O     1 1 
HETATM 5984 O  O     . HOH H 8 .   ? 34.215  17.394  49.028  1 11     ? 822 HOH A O     1 1 
HETATM 5985 O  O     . HOH H 8 .   ? 14.141  22.476  14.928  1 7.39   ? 823 HOH A O     1 1 
HETATM 5986 O  O     . HOH H 8 .   ? -13.977 25.179  -5.443  1 18.53  ? 824 HOH A O     1 1 
HETATM 5987 O  O     . HOH H 8 .   ? 41.309  3.027   36.722  1 21.81  ? 825 HOH A O     1 1 
HETATM 5988 O  O     . HOH H 8 .   ? 16.687  55.142  0.764   1 16.89  ? 826 HOH A O     1 1 
HETATM 5989 O  O     . HOH H 8 .   ? -1.131  42.565  -21.893 1 40.37  ? 827 HOH A O     1 1 
HETATM 5990 O  O     . HOH H 8 .   ? 20.416  4.384   36.714  1 9.14   ? 828 HOH A O     1 1 
HETATM 5991 O  O     . HOH H 8 .   ? 8.964   43.783  12.23   1 13.38  ? 829 HOH A O     1 1 
HETATM 5992 O  O     . HOH H 8 .   ? 4.199   6.37    -4.939  1 16.09  ? 830 HOH A O     1 1 
HETATM 5993 O  O     . HOH H 8 .   ? 23.853  28.318  2.673   1 23.22  ? 831 HOH A O     1 1 
HETATM 5994 O  O     . HOH H 8 .   ? 11.137  59.304  -11.96  1 19.04  ? 832 HOH A O     1 1 
HETATM 5995 O  O     . HOH H 8 .   ? -1.077  12.499  -8.676  1 17.31  ? 833 HOH A O     1 1 
HETATM 5996 O  O     . HOH H 8 .   ? -7.924  13.992  6.401   1 15.7   ? 834 HOH A O     1 1 
HETATM 5997 O  O     . HOH H 8 .   ? -9.706  12.088  13.753  1 16.46  ? 835 HOH A O     1 1 
HETATM 5998 O  O     . HOH H 8 .   ? 0.504   12.921  22.689  1 16.14  ? 836 HOH A O     1 1 
HETATM 5999 O  O     . HOH H 8 .   ? 23.747  -0.548  29.823  1 13.3   ? 837 HOH A O     1 1 
HETATM 6000 O  O     . HOH H 8 .   ? 29.737  7.178   -5.696  1 41.17  ? 838 HOH A O     1 1 
HETATM 6001 O  O     . HOH H 8 .   ? 33.079  -4.054  6.593   1 12.51  ? 839 HOH A O     1 1 
HETATM 6002 O  O     . HOH H 8 .   ? -9.475  14.968  17.007  1 15.9   ? 840 HOH A O     1 1 
HETATM 6003 O  O     . HOH H 8 .   ? 34.786  -2.848  34.913  1 12.71  ? 841 HOH A O     1 1 
HETATM 6004 O  O     . HOH H 8 .   ? 18.678  -15.506 17.114  1 13.7   ? 842 HOH A O     1 1 
HETATM 6005 O  O     . HOH H 8 .   ? 46.714  27.937  39.042  1 14.17  ? 843 HOH A O     1 1 
HETATM 6006 O  O     . HOH H 8 .   ? 19.05   18.864  19.798  1 11.29  ? 844 HOH A O     1 1 
HETATM 6007 O  O     . HOH H 8 .   ? 30.165  -10.649 9.321   1 13.37  ? 845 HOH A O     1 1 
HETATM 6008 O  O     . HOH I 8 .   ? 26.151  36.579  20.233  1 47.86  ? 101 HOH F O     1 1 
HETATM 6009 O  O     . HOH I 8 .   ? 13.833  42.339  6.511   1 30.01  ? 102 HOH F O     1 1 
HETATM 6010 O  O     . HOH I 8 .   ? -2.313  30.648  12.211  1 12.56  ? 103 HOH F O     1 1 
HETATM 6011 O  O     . HOH I 8 .   ? 29.794  36.817  17.063  1 22.43  ? 104 HOH F O     1 1 
HETATM 6012 O  O     . HOH J 8 .   ? 26.843  29.711  0.286   1 31.67  ? 101 HOH G O     1 1 
HETATM 6013 O  O     . HOH J 8 .   ? 25.224  28.822  14.157  1 10.69  ? 102 HOH G 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   ? 0.3662 0.1608 0.3215 0.0635  -0.0382 0.0103  1   MET A N     
2    C  CA    . MET A 1   ? 0.3648 0.1723 0.3335 0.0572  -0.0336 0.0112  1   MET A CA    
3    C  C     . MET A 1   ? 0.368  0.1801 0.3399 0.0582  -0.0283 0.0113  1   MET A C     
4    O  O     . MET A 1   ? 0.3696 0.1799 0.3361 0.0647  -0.0255 0.0108  1   MET A O     
5    C  CB    . MET A 1   ? 0.3701 0.1885 0.3463 0.057   -0.0297 0.0111  1   MET A CB    
6    C  CG    . MET A 1   ? 0.3957 0.2274 0.3852 0.0512  -0.0246 0.0118  1   MET A CG    
7    S  SD    . MET A 1   ? 0.4522 0.2956 0.4502 0.0506  -0.0209 0.0118  1   MET A SD    
8    C  CE    . MET A 1   ? 0.4123 0.2575 0.4071 0.0593  -0.0163 0.0115  1   MET A CE    
9    N  N     . ASN A 2   ? 0.3681 0.1862 0.3489 0.0519  -0.0269 0.0121  2   ASN A N     
10   C  CA    . ASN A 2   ? 0.3756 0.1992 0.3611 0.0519  -0.0218 0.0123  2   ASN A CA    
11   C  C     . ASN A 2   ? 0.3625 0.2003 0.361  0.0479  -0.0163 0.0127  2   ASN A C     
12   O  O     . ASN A 2   ? 0.3616 0.2036 0.3663 0.0424  -0.0176 0.0129  2   ASN A O     
13   C  CB    . ASN A 2   ? 0.4051 0.2226 0.3895 0.0485  -0.0251 0.0129  2   ASN A CB    
14   C  CG    . ASN A 2   ? 0.4725 0.2769 0.444  0.0538  -0.0287 0.0124  2   ASN A CG    
15   O  OD1   . ASN A 2   ? 0.4932 0.2954 0.458  0.0607  -0.0262 0.0118  2   ASN A OD1   
16   N  ND2   . ASN A 2   ? 0.4917 0.2871 0.4595 0.051   -0.0347 0.0129  2   ASN A ND2   
17   N  N     . VAL A 3   ? 0.3499 0.1949 0.3524 0.0506  -0.0104 0.0129  3   VAL A N     
18   C  CA    . VAL A 3   ? 0.3425 0.2005 0.3571 0.0471  -0.0055 0.0132  3   VAL A CA    
19   C  C     . VAL A 3   ? 0.3393 0.2012 0.3597 0.0445  -0.0025 0.0137  3   VAL A C     
20   O  O     . VAL A 3   ? 0.3491 0.2072 0.3648 0.0481  -0.0013 0.014   3   VAL A O     
21   C  CB    . VAL A 3   ? 0.349  0.2136 0.3655 0.0517  -0.0012 0.0135  3   VAL A CB    
22   C  CG1   . VAL A 3   ? 0.3467 0.2242 0.3759 0.0479  0.0035  0.014   3   VAL A CG1   
23   C  CG2   . VAL A 3   ? 0.3605 0.2216 0.3723 0.0539  -0.0044 0.013   3   VAL A CG2   
24   N  N     . PHE A 4   ? 0.321  0.1901 0.3511 0.0382  -0.0014 0.0138  4   PHE A N     
25   C  CA    . PHE A 4   ? 0.3046 0.1783 0.3416 0.0351  0.0014  0.0141  4   PHE A CA    
26   C  C     . PHE A 4   ? 0.2878 0.1733 0.3355 0.0327  0.006   0.0142  4   PHE A C     
27   O  O     . PHE A 4   ? 0.2828 0.1726 0.3337 0.031   0.0058  0.0139  4   PHE A O     
28   C  CB    . PHE A 4   ? 0.3007 0.1714 0.3395 0.0295  -0.0021 0.0141  4   PHE A CB    
29   C  CG    . PHE A 4   ? 0.3134 0.172  0.3425 0.0309  -0.0078 0.0143  4   PHE A CG    
30   C  CD1   . PHE A 4   ? 0.3237 0.1757 0.3476 0.0332  -0.0087 0.0145  4   PHE A CD1   
31   C  CD2   . PHE A 4   ? 0.3236 0.1771 0.3486 0.0297  -0.0125 0.0143  4   PHE A CD2   
32   C  CE1   . PHE A 4   ? 0.3352 0.1753 0.3498 0.0343  -0.0144 0.0147  4   PHE A CE1   
33   C  CE2   . PHE A 4   ? 0.337  0.1788 0.3531 0.0307  -0.0183 0.0146  4   PHE A CE2   
34   C  CZ    . PHE A 4   ? 0.337  0.1721 0.3479 0.0331  -0.0193 0.0147  4   PHE A CZ    
35   N  N     . ARG A 5   ? 0.2796 0.1702 0.3328 0.0323  0.0098  0.0147  5   ARG A N     
36   C  CA    . ARG A 5   ? 0.2726 0.1741 0.3363 0.0298  0.0138  0.0148  5   ARG A CA    
37   C  C     . ARG A 5   ? 0.2748 0.1793 0.3455 0.0245  0.0143  0.0145  5   ARG A C     
38   O  O     . ARG A 5   ? 0.2779 0.1782 0.3467 0.0245  0.0138  0.0148  5   ARG A O     
39   C  CB    . ARG A 5   ? 0.2786 0.1848 0.344  0.0341  0.0181  0.016   5   ARG A CB    
40   C  CG    . ARG A 5   ? 0.3065 0.2131 0.3683 0.0386  0.0183  0.0163  5   ARG A CG    
41   C  CD    . ARG A 5   ? 0.3358 0.2458 0.3977 0.0438  0.0225  0.018   5   ARG A CD    
42   N  NE    . ARG A 5   ? 0.3583 0.2707 0.4191 0.0479  0.0234  0.0185  5   ARG A NE    
43   C  CZ    . ARG A 5   ? 0.3565 0.2755 0.4212 0.0515  0.0277  0.0203  5   ARG A CZ    
44   N  NH1   . ARG A 5   ? 0.3359 0.2597 0.4057 0.0513  0.0313  0.0218  5   ARG A NH1   
45   N  NH2   . ARG A 5   ? 0.347  0.2682 0.411  0.0552  0.0282  0.0209  5   ARG A NH2   
46   N  N     . ILE A 6   ? 0.2705 0.1816 0.3487 0.0203  0.0152  0.0139  6   ILE A N     
47   C  CA    . ILE A 6   ? 0.2741 0.1886 0.3593 0.0156  0.016   0.0134  6   ILE A CA    
48   C  C     . ILE A 6   ? 0.2757 0.1988 0.3691 0.0151  0.02    0.0136  6   ILE A C     
49   O  O     . ILE A 6   ? 0.2739 0.2024 0.3714 0.0138  0.0208  0.0133  6   ILE A O     
50   C  CB    . ILE A 6   ? 0.2765 0.1915 0.3635 0.011   0.0138  0.0125  6   ILE A CB    
51   C  CG1   . ILE A 6   ? 0.2951 0.2018 0.3741 0.0115  0.0094  0.0128  6   ILE A CG1   
52   C  CG2   . ILE A 6   ? 0.2727 0.1911 0.3667 0.0067  0.0149  0.012   6   ILE A CG2   
53   C  CD1   . ILE A 6   ? 0.3185 0.2183 0.3937 0.0119  0.0073  0.0133  6   ILE A CD1   
54   N  N     . HIS A 7   ? 0.2763 0.2005 0.3721 0.0161  0.0222  0.0144  7   HIS A N     
55   C  CA    . HIS A 7   ? 0.2792 0.2112 0.3831 0.0153  0.0256  0.0149  7   HIS A CA    
56   C  C     . HIS A 7   ? 0.2862 0.2209 0.3968 0.0105  0.0258  0.0138  7   HIS A C     
57   O  O     . HIS A 7   ? 0.2954 0.2265 0.4052 0.0095  0.025   0.0138  7   HIS A O     
58   C  CB    . HIS A 7   ? 0.2895 0.221  0.3922 0.019   0.028   0.0166  7   HIS A CB    
59   C  CG    . HIS A 7   ? 0.3235 0.2521 0.419  0.0245  0.0283  0.0177  7   HIS A CG    
60   N  ND1   . HIS A 7   ? 0.3374 0.2721 0.4361 0.027   0.0309  0.0191  7   HIS A ND1   
61   C  CD2   . HIS A 7   ? 0.3468 0.2671 0.4323 0.0279  0.0261  0.0177  7   HIS A CD2   
62   C  CE1   . HIS A 7   ? 0.3471 0.2773 0.4377 0.0321  0.0307  0.0197  7   HIS A CE1   
63   N  NE2   . HIS A 7   ? 0.3588 0.2798 0.4408 0.0329  0.0277  0.0188  7   HIS A NE2   
64   N  N     . GLY A 8   ? 0.2847 0.2251 0.4013 0.0075  0.0264  0.0129  8   GLY A N     
65   C  CA    . GLY A 8   ? 0.2965 0.2393 0.419  0.0032  0.0266  0.0116  8   GLY A CA    
66   C  C     . GLY A 8   ? 0.3048 0.2545 0.4354 0.0016  0.0287  0.0115  8   GLY A C     
67   O  O     . GLY A 8   ? 0.3042 0.2574 0.4365 0.0034  0.0298  0.0125  8   GLY A O     
68   N  N     . ASP A 9   ? 0.3146 0.266  0.4504 -0.0017 0.029   0.0102  9   ASP A N     
69   C  CA    . ASP A 9   ? 0.3317 0.2889 0.4749 -0.0034 0.0304  0.0098  9   ASP A CA    
70   C  C     . ASP A 9   ? 0.3339 0.2939 0.4779 -0.0048 0.0296  0.0087  9   ASP A C     
71   O  O     . ASP A 9   ? 0.3348 0.2992 0.4834 -0.0051 0.0302  0.0091  9   ASP A O     
72   C  CB    . ASP A 9   ? 0.3724 0.3304 0.521  -0.0061 0.031   0.0088  9   ASP A CB    
73   C  CG    . ASP A 9   ? 0.4752 0.4289 0.6216 -0.0068 0.0302  0.0083  9   ASP A CG    
74   O  OD1   . ASP A 9   ? 0.4938 0.4443 0.6356 -0.0071 0.0288  0.0078  9   ASP A OD1   
75   O  OD2   . ASP A 9   ? 0.512  0.4655 0.6619 -0.0073 0.0309  0.0085  9   ASP A OD2   
76   N  N     . ASN A 10  ? 0.332  0.2893 0.4712 -0.0057 0.0281  0.0077  10  ASN A N     
77   C  CA    . ASN A 10  ? 0.3398 0.2989 0.4783 -0.0068 0.027   0.0067  10  ASN A CA    
78   C  C     . ASN A 10  ? 0.3516 0.3066 0.4831 -0.0064 0.0252  0.0067  10  ASN A C     
79   O  O     . ASN A 10  ? 0.3578 0.3085 0.4855 -0.0056 0.0245  0.0072  10  ASN A O     
80   C  CB    . ASN A 10  ? 0.3527 0.3144 0.4955 -0.0101 0.0273  0.0047  10  ASN A CB    
81   C  CG    . ASN A 10  ? 0.3986 0.3582 0.5412 -0.012  0.0275  0.0035  10  ASN A CG    
82   O  OD1   . ASN A 10  ? 0.4279 0.3847 0.5661 -0.0125 0.0265  0.0034  10  ASN A OD1   
83   N  ND2   . ASN A 10  ? 0.4016 0.3628 0.5494 -0.0131 0.0286  0.0029  10  ASN A ND2   
84   N  N     . ILE A 11  ? 0.3499 0.3057 0.4795 -0.0069 0.024   0.0062  11  ILE A N     
85   C  CA    . ILE A 11  ? 0.3516 0.3036 0.4747 -0.0066 0.0219  0.0063  11  ILE A CA    
86   C  C     . ILE A 11  ? 0.3479 0.2972 0.4692 -0.0091 0.0212  0.0056  11  ILE A C     
87   O  O     . ILE A 11  ? 0.3551 0.3    0.4713 -0.0086 0.0195  0.0064  11  ILE A O     
88   C  CB    . ILE A 11  ? 0.3601 0.3136 0.4818 -0.0069 0.0206  0.006   11  ILE A CB    
89   C  CG1   . ILE A 11  ? 0.3737 0.3227 0.4883 -0.0062 0.0182  0.0066  11  ILE A CG1   
90   C  CG2   . ILE A 11  ? 0.367  0.3234 0.4917 -0.0103 0.0209  0.0043  11  ILE A CG2   
91   C  CD1   . ILE A 11  ? 0.3909 0.3364 0.5016 -0.0024 0.0175  0.008   11  ILE A CD1   
92   N  N     . ILE A 12  ? 0.3336 0.2855 0.4592 -0.0118 0.0226  0.0043  12  ILE A N     
93   C  CA    . ILE A 12  ? 0.3298 0.2801 0.4548 -0.014  0.0224  0.0039  12  ILE A CA    
94   C  C     . ILE A 12  ? 0.3235 0.2703 0.4477 -0.0131 0.022   0.0051  12  ILE A C     
95   O  O     . ILE A 12  ? 0.3251 0.2686 0.4461 -0.0138 0.0204  0.0059  12  ILE A O     
96   C  CB    . ILE A 12  ? 0.3354 0.2893 0.4651 -0.0164 0.0242  0.0021  12  ILE A CB    
97   C  CG1   . ILE A 12  ? 0.3497 0.3058 0.4785 -0.0175 0.024   0.0009  12  ILE A CG1   
98   C  CG2   . ILE A 12  ? 0.3444 0.2974 0.4746 -0.0183 0.0247  0.002   12  ILE A CG2   
99   C  CD1   . ILE A 12  ? 0.3678 0.3269 0.5002 -0.0168 0.0244  0.0003  12  ILE A CD1   
100  N  N     . GLU A 13  ? 0.3143 0.2615 0.4413 -0.0114 0.0232  0.0054  13  GLU A N     
101  C  CA    . GLU A 13  ? 0.317  0.2603 0.4429 -0.0102 0.0226  0.0065  13  GLU A CA    
102  C  C     . GLU A 13  ? 0.3166 0.2546 0.4354 -0.0079 0.0202  0.0079  13  GLU A C     
103  O  O     . GLU A 13  ? 0.3175 0.2509 0.4335 -0.0082 0.0183  0.0087  13  GLU A O     
104  C  CB    . GLU A 13  ? 0.3396 0.2846 0.4695 -0.0088 0.0244  0.0068  13  GLU A CB    
105  C  CG    . GLU A 13  ? 0.3988 0.3482 0.5356 -0.0111 0.0263  0.0054  13  GLU A CG    
106  C  CD    . GLU A 13  ? 0.5069 0.4556 0.6462 -0.0133 0.0264  0.0048  13  GLU A CD    
107  O  OE1   . GLU A 13  ? 0.5303 0.4821 0.6729 -0.0154 0.0273  0.0032  13  GLU A OE1   
108  O  OE2   . GLU A 13  ? 0.5363 0.4813 0.6742 -0.0128 0.0254  0.0058  13  GLU A OE2   
109  N  N     . CYS A 14  ? 0.3104 0.2488 0.4265 -0.0057 0.02    0.0082  14  CYS A N     
110  C  CA    . CYS A 14  ? 0.3123 0.2456 0.4212 -0.0029 0.0177  0.0093  14  CYS A CA    
111  C  C     . CYS A 14  ? 0.3225 0.2526 0.4276 -0.0049 0.015   0.0094  14  CYS A C     
112  O  O     . CYS A 14  ? 0.3307 0.2549 0.4308 -0.0041 0.0124  0.0103  14  CYS A O     
113  C  CB    . CYS A 14  ? 0.3038 0.2393 0.4118 -0.0001 0.0184  0.0095  14  CYS A CB    
114  S  SG    . CYS A 14  ? 0.295  0.2352 0.4083 0.0021  0.0217  0.0101  14  CYS A SG    
115  N  N     . GLU A 15  ? 0.3222 0.256  0.4295 -0.0077 0.0154  0.0085  15  GLU A N     
116  C  CA    . GLU A 15  ? 0.3341 0.2656 0.4383 -0.0099 0.0132  0.0089  15  GLU A CA    
117  C  C     . GLU A 15  ? 0.3464 0.2761 0.452  -0.0122 0.0125  0.0096  15  GLU A C     
118  O  O     . GLU A 15  ? 0.3559 0.2817 0.4579 -0.0133 0.0098  0.0109  15  GLU A O     
119  C  CB    . GLU A 15  ? 0.3614 0.2973 0.4671 -0.0122 0.014   0.0079  15  GLU A CB    
120  C  CG    . GLU A 15  ? 0.4393 0.3759 0.5427 -0.0101 0.0134  0.0077  15  GLU A CG    
121  C  CD    . GLU A 15  ? 0.537  0.4682 0.6335 -0.0083 0.0102  0.0089  15  GLU A CD    
122  O  OE1   . GLU A 15  ? 0.5565 0.4833 0.6497 -0.0094 0.0079  0.0099  15  GLU A OE1   
123  O  OE2   . GLU A 15  ? 0.5591 0.4905 0.6537 -0.0059 0.0097  0.0089  15  GLU A OE2   
124  N  N     . ARG A 16  ? 0.3454 0.2774 0.4564 -0.013  0.0146  0.0091  16  ARG A N     
125  C  CA    . ARG A 16  ? 0.3461 0.2767 0.4593 -0.015  0.014   0.01    16  ARG A CA    
126  C  C     . ARG A 16  ? 0.3444 0.2678 0.4526 -0.0135 0.0106  0.0117  16  ARG A C     
127  O  O     . ARG A 16  ? 0.3488 0.2695 0.4563 -0.0154 0.0083  0.013   16  ARG A O     
128  C  CB    . ARG A 16  ? 0.3674 0.3015 0.4872 -0.0157 0.0168  0.009   16  ARG A CB    
129  C  CG    . ARG A 16  ? 0.4218 0.362  0.5463 -0.0177 0.0196  0.0074  16  ARG A CG    
130  C  CD    . ARG A 16  ? 0.4826 0.425  0.6127 -0.0198 0.0211  0.0071  16  ARG A CD    
131  N  NE    . ARG A 16  ? 0.5394 0.4835 0.6742 -0.0189 0.0229  0.0061  16  ARG A NE    
132  C  CZ    . ARG A 16  ? 0.5723 0.5207 0.7116 -0.0196 0.0253  0.0043  16  ARG A CZ    
133  N  NH1   . ARG A 16  ? 0.5673 0.5188 0.7066 -0.021  0.0265  0.0031  16  ARG A NH1   
134  N  NH2   . ARG A 16  ? 0.5732 0.5225 0.7166 -0.0189 0.0265  0.0037  16  ARG A NH2   
135  N  N     . VAL A 17  ? 0.3415 0.2617 0.4459 -0.01   0.0101  0.0117  17  VAL A N     
136  C  CA    . VAL A 17  ? 0.3501 0.2626 0.4484 -0.0079 0.0067  0.013   17  VAL A CA    
137  C  C     . VAL A 17  ? 0.3649 0.273  0.4572 -0.0079 0.0032  0.0139  17  VAL A C     
138  O  O     . VAL A 17  ? 0.3746 0.2769 0.4638 -0.0087 -0.0005 0.0153  17  VAL A O     
139  C  CB    . VAL A 17  ? 0.3572 0.2678 0.4526 -0.0036 0.0078  0.0127  17  VAL A CB    
140  C  CG1   . VAL A 17  ? 0.3679 0.2696 0.4551 -0.0008 0.0041  0.0137  17  VAL A CG1   
141  C  CG2   . VAL A 17  ? 0.3627 0.2768 0.4639 -0.0039 0.0107  0.0122  17  VAL A CG2   
142  N  N     . ILE A 18  ? 0.3652 0.2759 0.456  -0.0074 0.0039  0.0132  18  ILE A N     
143  C  CA    . ILE A 18  ? 0.3735 0.2804 0.4588 -0.0076 0.0005  0.014   18  ILE A CA    
144  C  C     . ILE A 18  ? 0.3782 0.2857 0.4657 -0.0119 -0.001  0.0152  18  ILE A C     
145  O  O     . ILE A 18  ? 0.3827 0.2845 0.4659 -0.0125 -0.005  0.0168  18  ILE A O     
146  C  CB    . ILE A 18  ? 0.3783 0.2889 0.4628 -0.0065 0.0019  0.0129  18  ILE A CB    
147  C  CG1   . ILE A 18  ? 0.3937 0.3047 0.477  -0.0021 0.0036  0.0122  18  ILE A CG1   
148  C  CG2   . ILE A 18  ? 0.3863 0.293  0.4652 -0.0068 -0.0018 0.0138  18  ILE A CG2   
149  C  CD1   . ILE A 18  ? 0.4178 0.321  0.4939 0.0018  0.0009  0.0129  18  ILE A CD1   
150  N  N     . ASP A 19  ? 0.377  0.2912 0.4713 -0.0149 0.0022  0.0146  19  ASP A N     
151  C  CA    . ASP A 19  ? 0.3854 0.3012 0.4825 -0.0188 0.0017  0.016   19  ASP A CA    
152  C  C     . ASP A 19  ? 0.3914 0.3027 0.4893 -0.0198 -0.001  0.0179  19  ASP A C     
153  O  O     . ASP A 19  ? 0.3971 0.3066 0.4945 -0.0223 -0.0037 0.0201  19  ASP A O     
154  C  CB    . ASP A 19  ? 0.4051 0.3288 0.5089 -0.021  0.0061  0.0147  19  ASP A CB    
155  C  CG    . ASP A 19  ? 0.4706 0.3983 0.5735 -0.0206 0.0081  0.013   19  ASP A CG    
156  O  OD1   . ASP A 19  ? 0.4817 0.4067 0.5793 -0.0194 0.0059  0.0132  19  ASP A OD1   
157  O  OD2   . ASP A 19  ? 0.4994 0.4327 0.607  -0.0214 0.0115  0.0114  19  ASP A OD2   
158  N  N     . LEU A 20  ? 0.3879 0.2973 0.4869 -0.0179 -0.0006 0.0175  20  LEU A N     
159  C  CA    . LEU A 20  ? 0.3946 0.299  0.4939 -0.0186 -0.0036 0.0192  20  LEU A CA    
160  C  C     . LEU A 20  ? 0.4113 0.3068 0.5027 -0.0174 -0.0091 0.0208  20  LEU A C     
161  O  O     . LEU A 20  ? 0.411  0.3032 0.5027 -0.0198 -0.0127 0.0231  20  LEU A O     
162  C  CB    . LEU A 20  ? 0.3934 0.2969 0.4942 -0.0163 -0.0022 0.0182  20  LEU A CB    
163  C  CG    . LEU A 20  ? 0.4067 0.3168 0.5159 -0.0181 0.0017  0.0174  20  LEU A CG    
164  C  CD1   . LEU A 20  ? 0.4116 0.3203 0.5213 -0.0157 0.0029  0.0165  20  LEU A CD1   
165  C  CD2   . LEU A 20  ? 0.4199 0.3305 0.534  -0.0215 0.0004  0.0194  20  LEU A CD2   
166  N  N     . ILE A 21  ? 0.4251 0.3169 0.5097 -0.0137 -0.0099 0.0197  21  ILE A N     
167  C  CA    . ILE A 21  ? 0.4444 0.3271 0.5203 -0.0118 -0.0151 0.0207  21  ILE A CA    
168  C  C     . ILE A 21  ? 0.4622 0.3449 0.5374 -0.0148 -0.0177 0.0223  21  ILE A C     
169  O  O     . ILE A 21  ? 0.4657 0.3425 0.5386 -0.0164 -0.0225 0.0245  21  ILE A O     
170  C  CB    . ILE A 21  ? 0.4499 0.3303 0.5195 -0.0067 -0.0143 0.0189  21  ILE A CB    
171  C  CG1   . ILE A 21  ? 0.4587 0.3377 0.5279 -0.0036 -0.0125 0.018   21  ILE A CG1   
172  C  CG2   . ILE A 21  ? 0.4607 0.3324 0.5212 -0.0046 -0.0194 0.0196  21  ILE A CG2   
173  C  CD1   . ILE A 21  ? 0.4735 0.354  0.5399 0.0006  -0.0097 0.0165  21  ILE A CD1   
174  N  N     . LEU A 22  ? 0.4714 0.3607 0.5487 -0.0158 -0.0146 0.0213  22  LEU A N     
175  C  CA    . LEU A 22  ? 0.4913 0.3813 0.5677 -0.0186 -0.0164 0.0227  22  LEU A CA    
176  C  C     . LEU A 22  ? 0.5157 0.4081 0.5975 -0.0233 -0.0171 0.0253  22  LEU A C     
177  O  O     . LEU A 22  ? 0.5165 0.4078 0.5969 -0.0257 -0.0198 0.0273  22  LEU A O     
178  C  CB    . LEU A 22  ? 0.4874 0.3841 0.565  -0.0185 -0.0127 0.021   22  LEU A CB    
179  C  CG    . LEU A 22  ? 0.5033 0.3981 0.5757 -0.0143 -0.0126 0.0192  22  LEU A CG    
180  C  CD1   . LEU A 22  ? 0.5098 0.4112 0.5842 -0.0149 -0.0095 0.0178  22  LEU A CD1   
181  C  CD2   . LEU A 22  ? 0.5134 0.3995 0.5776 -0.0124 -0.018  0.0202  22  LEU A CD2   
182  N  N     . SER A 23  ? 0.5321 0.4283 0.6206 -0.0245 -0.0145 0.0253  23  SER A N     
183  C  CA    . SER A 23  ? 0.552  0.4509 0.6465 -0.0286 -0.0148 0.028   23  SER A CA    
184  C  C     . SER A 23  ? 0.5785 0.4694 0.6704 -0.0297 -0.0212 0.031   23  SER A C     
185  O  O     . SER A 23  ? 0.5837 0.476  0.6794 -0.0334 -0.0227 0.0341  23  SER A O     
186  C  CB    . SER A 23  ? 0.5665 0.4711 0.6687 -0.0292 -0.0107 0.0271  23  SER A CB    
187  O  OG    . SER A 23  ? 0.5997 0.499  0.7009 -0.0271 -0.0126 0.0268  23  SER A OG    
188  N  N     . LYS A 24  ? 0.5946 0.4768 0.6801 -0.0265 -0.0249 0.0304  24  LYS A N     
189  C  CA    . LYS A 24  ? 0.6168 0.4899 0.6987 -0.0273 -0.0317 0.0331  24  LYS A CA    
190  C  C     . LYS A 24  ? 0.6255 0.4908 0.6979 -0.0253 -0.0364 0.0331  24  LYS A C     
191  O  O     . LYS A 24  ? 0.6261 0.4861 0.6964 -0.0275 -0.0418 0.036   24  LYS A O     
192  C  CB    . LYS A 24  ? 0.6559 0.524  0.7375 -0.0253 -0.0331 0.0327  24  LYS A CB    
193  C  CG    . LYS A 24  ? 0.7296 0.5891 0.8096 -0.027  -0.0401 0.0359  24  LYS A CG    
194  C  CD    . LYS A 24  ? 0.8037 0.6517 0.8737 -0.0226 -0.0446 0.0346  24  LYS A CD    
195  C  CE    . LYS A 24  ? 0.8575 0.6945 0.9221 -0.0236 -0.053  0.0374  24  LYS A CE    
196  N  NZ    . LYS A 24  ? 0.8926 0.7182 0.9456 -0.0184 -0.0568 0.0355  24  LYS A NZ    
197  N  N     . ILE A 25  ? 0.631  0.4958 0.698  -0.0212 -0.0342 0.0301  25  ILE A N     
198  C  CA    . ILE A 25  ? 0.6433 0.5016 0.7014 -0.0185 -0.0378 0.0296  25  ILE A CA    
199  C  C     . ILE A 25  ? 0.6436 0.5069 0.703  -0.0211 -0.0369 0.0304  25  ILE A C     
200  O  O     . ILE A 25  ? 0.6414 0.5134 0.7051 -0.0216 -0.0314 0.0288  25  ILE A O     
201  C  CB    . ILE A 25  ? 0.6546 0.5123 0.708  -0.013  -0.0349 0.0263  25  ILE A CB    
202  C  CG1   . ILE A 25  ? 0.6701 0.5222 0.7207 -0.0098 -0.0357 0.0255  25  ILE A CG1   
203  C  CG2   . ILE A 25  ? 0.6665 0.5193 0.7117 -0.01   -0.0375 0.0255  25  ILE A CG2   
204  C  CD1   . ILE A 25  ? 0.6946 0.5345 0.7376 -0.0087 -0.0429 0.027   25  ILE A CD1   
205  N  N     . ASN A 26  ? 0.6434 0.5008 0.6987 -0.0228 -0.0425 0.0327  26  ASN A N     
206  C  CA    . ASN A 26  ? 0.6431 0.5043 0.6984 -0.025  -0.0421 0.0336  26  ASN A CA    
207  C  C     . ASN A 26  ? 0.6418 0.496  0.6879 -0.021  -0.0452 0.032   26  ASN A C     
208  O  O     . ASN A 26  ? 0.652  0.4965 0.6917 -0.0201 -0.0516 0.0333  26  ASN A O     
209  C  CB    . ASN A 26  ? 0.6603 0.5209 0.7186 -0.0302 -0.0458 0.0378  26  ASN A CB    
210  C  CG    . ASN A 26  ? 0.7055 0.5751 0.7738 -0.0341 -0.0414 0.0393  26  ASN A CG    
211  O  OD1   . ASN A 26  ? 0.7152 0.5939 0.7881 -0.0345 -0.0352 0.0376  26  ASN A OD1   
212  N  ND2   . ASN A 26  ? 0.7183 0.5855 0.7903 -0.037  -0.0448 0.0425  26  ASN A ND2   
213  N  N     . PRO A 27  ? 0.6262 0.4849 0.6715 -0.0179 -0.0409 0.0291  27  PRO A N     
214  C  CA    . PRO A 27  ? 0.6224 0.475  0.6595 -0.0133 -0.0434 0.0275  27  PRO A CA    
215  C  C     . PRO A 27  ? 0.6175 0.4679 0.6509 -0.0148 -0.0469 0.0287  27  PRO A C     
216  O  O     . PRO A 27  ? 0.6185 0.4751 0.6562 -0.0189 -0.0453 0.03    27  PRO A O     
217  C  CB    . PRO A 27  ? 0.6292 0.4886 0.6685 -0.01   -0.0373 0.0244  27  PRO A CB    
218  C  CG    . PRO A 27  ? 0.6313 0.4993 0.6793 -0.0129 -0.0321 0.0242  27  PRO A CG    
219  C  CD    . PRO A 27  ? 0.612  0.4811 0.6639 -0.0183 -0.0339 0.0271  27  PRO A CD    
220  N  N     . GLN A 28  ? 0.6099 0.4512 0.6349 -0.0112 -0.0518 0.0283  28  GLN A N     
221  C  CA    . GLN A 28  ? 0.6053 0.4426 0.6255 -0.0117 -0.056  0.0294  28  GLN A CA    
222  C  C     . GLN A 28  ? 0.5838 0.4269 0.604  -0.0093 -0.0521 0.027   28  GLN A C     
223  O  O     . GLN A 28  ? 0.5836 0.4293 0.6042 -0.0118 -0.0527 0.0279  28  GLN A O     
224  C  CB    . GLN A 28  ? 0.6425 0.4668 0.6533 -0.0082 -0.063  0.0296  28  GLN A CB    
225  C  CG    . GLN A 28  ? 0.7094 0.5269 0.7194 -0.0096 -0.0672 0.0314  28  GLN A CG    
226  C  CD    . GLN A 28  ? 0.7899 0.6088 0.8049 -0.0162 -0.0699 0.0353  28  GLN A CD    
227  O  OE1   . GLN A 28  ? 0.8247 0.6395 0.8368 -0.0184 -0.0748 0.0375  28  GLN A OE1   
228  N  NE2   . GLN A 28  ? 0.7881 0.6131 0.811  -0.0196 -0.0668 0.0365  28  GLN A NE2   
229  N  N     . LYS A 29  ? 0.5625 0.4074 0.5823 -0.0044 -0.0484 0.0243  29  LYS A N     
230  C  CA    . LYS A 29  ? 0.5445 0.395  0.5651 -0.0019 -0.0447 0.0223  29  LYS A CA    
231  C  C     . LYS A 29  ? 0.526  0.3845 0.5528 -0.0006 -0.0382 0.0205  29  LYS A C     
232  O  O     . LYS A 29  ? 0.5264 0.3823 0.5523 0.002   -0.0374 0.0199  29  LYS A O     
233  C  CB    . LYS A 29  ? 0.5656 0.4087 0.5782 0.0041  -0.0478 0.0211  29  LYS A CB    
234  C  CG    . LYS A 29  ? 0.6168 0.45   0.6221 0.0038  -0.0552 0.0226  29  LYS A CG    
235  C  CD    . LYS A 29  ? 0.6696 0.4938 0.6661 0.0107  -0.0583 0.0211  29  LYS A CD    
236  C  CE    . LYS A 29  ? 0.7126 0.5254 0.701  0.0109  -0.0662 0.0225  29  LYS A CE    
237  N  NZ    . LYS A 29  ? 0.7381 0.5414 0.7174 0.0181  -0.0692 0.0208  29  LYS A NZ    
238  N  N     . VAL A 30  ? 0.5086 0.3763 0.5412 -0.0027 -0.0337 0.0198  30  VAL A N     
239  C  CA    . VAL A 30  ? 0.4949 0.3705 0.5338 -0.0018 -0.0277 0.0181  30  VAL A CA    
240  C  C     . VAL A 30  ? 0.4864 0.3671 0.5266 0.0003  -0.0254 0.0167  30  VAL A C     
241  O  O     . VAL A 30  ? 0.4908 0.3733 0.5309 -0.0021 -0.0264 0.0171  30  VAL A O     
242  C  CB    . VAL A 30  ? 0.4936 0.3761 0.5398 -0.0069 -0.0244 0.0186  30  VAL A CB    
243  C  CG1   . VAL A 30  ? 0.4949 0.3848 0.5471 -0.0057 -0.0188 0.0168  30  VAL A CG1   
244  C  CG2   . VAL A 30  ? 0.4978 0.3761 0.544  -0.0093 -0.0268 0.0204  30  VAL A CG2   
245  N  N     . LYS A 31  ? 0.4717 0.3548 0.5133 0.0044  -0.0223 0.0153  31  LYS A N     
246  C  CA    . LYS A 31  ? 0.4608 0.3491 0.5046 0.0065  -0.02   0.0143  31  LYS A CA    
247  C  C     . LYS A 31  ? 0.4555 0.3513 0.5062 0.0071  -0.0147 0.0133  31  LYS A C     
248  O  O     . LYS A 31  ? 0.4581 0.3525 0.5088 0.0094  -0.0132 0.0132  31  LYS A O     
249  C  CB    . LYS A 31  ? 0.4751 0.3579 0.5128 0.0123  -0.0224 0.0141  31  LYS A CB    
250  C  CG    . LYS A 31  ? 0.5095 0.3977 0.5499 0.0151  -0.0203 0.0134  31  LYS A CG    
251  C  CD    . LYS A 31  ? 0.5506 0.4332 0.585  0.0216  -0.0219 0.0133  31  LYS A CD    
252  C  CE    . LYS A 31  ? 0.5895 0.4768 0.6264 0.0248  -0.0205 0.013   31  LYS A CE    
253  N  NZ    . LYS A 31  ? 0.6223 0.5043 0.6533 0.0317  -0.0216 0.0129  31  LYS A NZ    
254  N  N     . ARG A 32  ? 0.4451 0.3482 0.5014 0.0049  -0.0121 0.0127  32  ARG A N     
255  C  CA    . ARG A 32  ? 0.4386 0.3488 0.5018 0.0052  -0.0074 0.0119  32  ARG A CA    
256  C  C     . ARG A 32  ? 0.4306 0.3454 0.4965 0.0079  -0.0062 0.0116  32  ARG A C     
257  O  O     . ARG A 32  ? 0.4326 0.3462 0.4959 0.0083  -0.0086 0.0118  32  ARG A O     
258  C  CB    . ARG A 32  ? 0.4522 0.3673 0.5206 0       -0.0054 0.0115  32  ARG A CB    
259  C  CG    . ARG A 32  ? 0.4942 0.4068 0.5624 -0.0023 -0.0055 0.012   32  ARG A CG    
260  C  CD    . ARG A 32  ? 0.5366 0.4546 0.61   -0.0068 -0.0031 0.0115  32  ARG A CD    
261  N  NE    . ARG A 32  ? 0.5778 0.4947 0.6527 -0.009  -0.0026 0.012   32  ARG A NE    
262  C  CZ    . ARG A 32  ? 0.6095 0.5283 0.6884 -0.0085 0       0.0115  32  ARG A CZ    
263  N  NH1   . ARG A 32  ? 0.6079 0.5298 0.6897 -0.0058 0.0024  0.0106  32  ARG A NH1   
264  N  NH2   . ARG A 32  ? 0.6075 0.5253 0.688  -0.0106 0.0001  0.0122  32  ARG A NH2   
265  N  N     . GLY A 33  ? 0.4175 0.3375 0.4889 0.0095  -0.0025 0.0113  33  GLY A N     
266  C  CA    . GLY A 33  ? 0.4138 0.3389 0.4891 0.0119  -0.0011 0.0114  33  GLY A CA    
267  C  C     . GLY A 33  ? 0.4046 0.3345 0.4855 0.0141  0.0029  0.0117  33  GLY A C     
268  O  O     . GLY A 33  ? 0.4089 0.34   0.4925 0.0121  0.0049  0.0114  33  GLY A O     
269  N  N     . PHE A 34  ? 0.3895 0.3224 0.4725 0.0182  0.0041  0.0125  34  PHE A N     
270  C  CA    . PHE A 34  ? 0.3795 0.3172 0.4679 0.0205  0.008   0.0133  34  PHE A CA    
271  C  C     . PHE A 34  ? 0.3712 0.3067 0.4559 0.0268  0.0086  0.0144  34  PHE A C     
272  O  O     . PHE A 34  ? 0.3732 0.3073 0.4552 0.0295  0.0068  0.0147  34  PHE A O     
273  C  CB    . PHE A 34  ? 0.3706 0.3167 0.468  0.0188  0.0097  0.0138  34  PHE A CB    
274  C  CG    . PHE A 34  ? 0.3704 0.3197 0.4726 0.0133  0.0103  0.0127  34  PHE A CG    
275  C  CD1   . PHE A 34  ? 0.3818 0.3298 0.4822 0.0093  0.0078  0.0115  34  PHE A CD1   
276  C  CD2   . PHE A 34  ? 0.374  0.3275 0.4823 0.0123  0.0132  0.0128  34  PHE A CD2   
277  C  CE1   . PHE A 34  ? 0.3887 0.3394 0.4929 0.0048  0.0085  0.0104  34  PHE A CE1   
278  C  CE2   . PHE A 34  ? 0.3816 0.3375 0.4938 0.0077  0.0136  0.0116  34  PHE A CE2   
279  C  CZ    . PHE A 34  ? 0.3814 0.3358 0.4914 0.0041  0.0114  0.0103  34  PHE A CZ    
280  N  N     . ILE A 35  ? 0.3604 0.2953 0.4446 0.0295  0.0112  0.0149  35  ILE A N     
281  C  CA    . ILE A 35  ? 0.3565 0.29   0.4374 0.0361  0.0126  0.0161  35  ILE A CA    
282  C  C     . ILE A 35  ? 0.3512 0.294  0.4409 0.038   0.0163  0.0179  35  ILE A C     
283  O  O     . ILE A 35  ? 0.3572 0.3012 0.4461 0.0433  0.0173  0.0192  35  ILE A O     
284  C  CB    . ILE A 35  ? 0.3601 0.2877 0.435  0.0386  0.0134  0.016   35  ILE A CB    
285  C  CG1   . ILE A 35  ? 0.3652 0.2973 0.4463 0.036   0.0167  0.0164  35  ILE A CG1   
286  C  CG2   . ILE A 35  ? 0.3703 0.2885 0.4367 0.037   0.0092  0.0147  35  ILE A CG2   
287  C  CD1   . ILE A 35  ? 0.3829 0.3122 0.4603 0.0401  0.0189  0.0172  35  ILE A CD1   
288  N  N     . SER A 36  ? 0.3341 0.2834 0.4324 0.0338  0.0181  0.0182  36  SER A N     
289  C  CA    . SER A 36  ? 0.3183 0.2768 0.4265 0.0338  0.021   0.02    36  SER A CA    
290  C  C     . SER A 36  ? 0.3082 0.2706 0.4229 0.0274  0.0199  0.019   36  SER A C     
291  O  O     . SER A 36  ? 0.3105 0.2686 0.4216 0.0237  0.0177  0.017   36  SER A O     
292  C  CB    . SER A 36  ? 0.3271 0.2881 0.4377 0.0363  0.025   0.0216  36  SER A CB    
293  O  OG    . SER A 36  ? 0.3461 0.3068 0.4588 0.032   0.0255  0.0206  36  SER A OG    
294  N  N     . LEU A 37  ? 0.3003 0.2704 0.4244 0.0263  0.0213  0.0205  37  LEU A N     
295  C  CA    . LEU A 37  ? 0.2987 0.272  0.4284 0.0207  0.0201  0.0195  37  LEU A CA    
296  C  C     . LEU A 37  ? 0.3082 0.2799 0.4381 0.0171  0.021   0.018   37  LEU A C     
297  O  O     . LEU A 37  ? 0.3122 0.2826 0.4418 0.0127  0.0192  0.016   37  LEU A O     
298  C  CB    . LEU A 37  ? 0.2918 0.2733 0.4317 0.0207  0.0212  0.0217  37  LEU A CB    
299  C  CG    . LEU A 37  ? 0.3063 0.2899 0.4474 0.0232  0.0197  0.0231  37  LEU A CG    
300  C  CD1   . LEU A 37  ? 0.3086 0.3006 0.4595 0.0254  0.0219  0.0265  37  LEU A CD1   
301  C  CD2   . LEU A 37  ? 0.3128 0.2951 0.4532 0.0192  0.0158  0.0214  37  LEU A CD2   
302  N  N     . SER A 38  ? 0.3096 0.281  0.4394 0.0191  0.0237  0.0189  38  SER A N     
303  C  CA    . SER A 38  ? 0.3145 0.2844 0.4448 0.0162  0.0246  0.0177  38  SER A CA    
304  C  C     . SER A 38  ? 0.3161 0.2785 0.438  0.016   0.0234  0.016   38  SER A C     
305  O  O     . SER A 38  ? 0.3197 0.2808 0.4422 0.013   0.0236  0.0148  38  SER A O     
306  C  CB    . SER A 38  ? 0.3336 0.3071 0.4685 0.0183  0.028   0.0198  38  SER A CB    
307  O  OG    . SER A 38  ? 0.3602 0.341  0.5047 0.0166  0.029   0.0213  38  SER A OG    
308  N  N     . CYS A 39  ? 0.3122 0.2697 0.4267 0.0196  0.0222  0.0162  39  CYS A N     
309  C  CA    . CYS A 39  ? 0.3162 0.266  0.4226 0.0199  0.0207  0.0151  39  CYS A CA    
310  C  C     . CYS A 39  ? 0.3118 0.2566 0.4123 0.0185  0.0171  0.0139  39  CYS A C     
311  O  O     . CYS A 39  ? 0.3129 0.2543 0.4079 0.0219  0.0155  0.0143  39  CYS A O     
312  C  CB    . CYS A 39  ? 0.3374 0.2838 0.4387 0.0254  0.0219  0.0164  39  CYS A CB    
313  S  SG    . CYS A 39  ? 0.4115 0.3636 0.5192 0.0275  0.0265  0.0184  39  CYS A SG    
314  N  N     . PRO A 40  ? 0.3016 0.2451 0.4021 0.0138  0.0157  0.0124  40  PRO A N     
315  C  CA    . PRO A 40  ? 0.2935 0.2317 0.3878 0.0124  0.0122  0.0116  40  PRO A CA    
316  C  C     . PRO A 40  ? 0.2886 0.219  0.3752 0.0147  0.0106  0.0119  40  PRO A C     
317  O  O     . PRO A 40  ? 0.2868 0.2159 0.373  0.0166  0.0122  0.0123  40  PRO A O     
318  C  CB    . PRO A 40  ? 0.3023 0.2421 0.3995 0.0069  0.0121  0.0104  40  PRO A CB    
319  C  CG    . PRO A 40  ? 0.3086 0.2538 0.4131 0.0058  0.0152  0.0103  40  PRO A CG    
320  C  CD    . PRO A 40  ? 0.2911 0.2376 0.397  0.0099  0.0173  0.0117  40  PRO A CD    
321  N  N     . PHE A 41  ? 0.289  0.214  0.3694 0.0144  0.007   0.0117  41  PHE A N     
322  C  CA    . PHE A 41  ? 0.2975 0.2142 0.3703 0.0161  0.0045  0.0119  41  PHE A CA    
323  C  C     . PHE A 41  ? 0.3115 0.224  0.3811 0.0121  0.001   0.0117  41  PHE A C     
324  O  O     . PHE A 41  ? 0.3162 0.2318 0.3879 0.009   0.0004  0.0114  41  PHE A O     
325  C  CB    . PHE A 41  ? 0.2954 0.2077 0.362  0.022   0.0034  0.0125  41  PHE A CB    
326  C  CG    . PHE A 41  ? 0.3056 0.2154 0.3681 0.0227  0.0002  0.0124  41  PHE A CG    
327  C  CD1   . PHE A 41  ? 0.3186 0.2207 0.3742 0.0218  -0.0042 0.0124  41  PHE A CD1   
328  C  CD2   . PHE A 41  ? 0.3169 0.2318 0.3827 0.0244  0.0013  0.0127  41  PHE A CD2   
329  C  CE1   . PHE A 41  ? 0.3283 0.2279 0.3802 0.0222  -0.0074 0.0124  41  PHE A CE1   
330  C  CE2   . PHE A 41  ? 0.3275 0.2398 0.3895 0.0251  -0.0019 0.0127  41  PHE A CE2   
331  C  CZ    . PHE A 41  ? 0.3249 0.2295 0.38   0.024   -0.0063 0.0125  41  PHE A CZ    
332  N  N     . ILE A 42  ? 0.3129 0.2185 0.3774 0.0122  -0.0014 0.0121  42  ILE A N     
333  C  CA    . ILE A 42  ? 0.3136 0.214  0.3741 0.0093  -0.0054 0.0125  42  ILE A CA    
334  C  C     . ILE A 42  ? 0.3144 0.2052 0.3662 0.0131  -0.0091 0.0131  42  ILE A C     
335  O  O     . ILE A 42  ? 0.32   0.2075 0.3697 0.0155  -0.0087 0.0131  42  ILE A O     
336  C  CB    . ILE A 42  ? 0.3167 0.2188 0.3814 0.0042  -0.005  0.0127  42  ILE A CB    
337  C  CG1   . ILE A 42  ? 0.3294 0.226  0.3897 0.0014  -0.0094 0.0139  42  ILE A CG1   
338  C  CG2   . ILE A 42  ? 0.3218 0.223  0.3882 0.0049  -0.0034 0.0128  42  ILE A CG2   
339  C  CD1   . ILE A 42  ? 0.3426 0.2419 0.4073 -0.0035 -0.0089 0.0144  42  ILE A CD1   
340  N  N     . GLU A 43  ? 0.3083 0.1945 0.3546 0.0139  -0.0129 0.0134  43  GLU A N     
341  C  CA    . GLU A 43  ? 0.3195 0.1959 0.3568 0.0176  -0.017  0.0137  43  GLU A CA    
342  C  C     . GLU A 43  ? 0.3312 0.202  0.3658 0.0135  -0.0218 0.0148  43  GLU A C     
343  O  O     . GLU A 43  ? 0.3258 0.1993 0.3624 0.0098  -0.0229 0.0153  43  GLU A O     
344  C  CB    . GLU A 43  ? 0.3466 0.2216 0.3799 0.022   -0.018  0.0133  43  GLU A CB    
345  C  CG    . GLU A 43  ? 0.4105 0.2755 0.4341 0.0275  -0.0214 0.0133  43  GLU A CG    
346  C  CD    . GLU A 43  ? 0.5223 0.3861 0.542  0.0327  -0.022  0.0128  43  GLU A CD    
347  O  OE1   . GLU A 43  ? 0.5379 0.4096 0.5632 0.0326  -0.0191 0.0127  43  GLU A OE1   
348  O  OE2   . GLU A 43  ? 0.5795 0.4339 0.5901 0.037   -0.0255 0.0127  43  GLU A OE2   
349  N  N     . ILE A 44  ? 0.3466 0.21   0.377  0.0138  -0.0247 0.0154  44  ILE A N     
350  C  CA    . ILE A 44  ? 0.3661 0.2242 0.3946 0.0097  -0.0295 0.017   44  ILE A CA    
351  C  C     . ILE A 44  ? 0.3844 0.2302 0.4031 0.0127  -0.0357 0.0176  44  ILE A C     
352  O  O     . ILE A 44  ? 0.3941 0.2343 0.4075 0.0174  -0.0361 0.0168  44  ILE A O     
353  C  CB    . ILE A 44  ? 0.3715 0.2331 0.4065 0.0051  -0.0279 0.0178  44  ILE A CB    
354  C  CG1   . ILE A 44  ? 0.3891 0.2462 0.4221 0.0077  -0.0278 0.0176  44  ILE A CG1   
355  C  CG2   . ILE A 44  ? 0.3708 0.2437 0.4149 0.0021  -0.0224 0.0172  44  ILE A CG2   
356  C  CD1   . ILE A 44  ? 0.4057 0.264  0.4442 0.0031  -0.028  0.0189  44  ILE A CD1   
357  N  N     . ILE A 45  ? 0.3855 0.2268 0.4015 0.0099  -0.0407 0.019   45  ILE A N     
358  C  CA    . ILE A 45  ? 0.4018 0.2309 0.4088 0.0116  -0.0475 0.0198  45  ILE A CA    
359  C  C     . ILE A 45  ? 0.4033 0.2311 0.4137 0.0056  -0.0506 0.0223  45  ILE A C     
360  O  O     . ILE A 45  ? 0.3993 0.2325 0.4147 0.0007  -0.0503 0.0236  45  ILE A O     
361  C  CB    . ILE A 45  ? 0.4172 0.2418 0.4184 0.0132  -0.0515 0.0199  45  ILE A CB    
362  C  CG1   . ILE A 45  ? 0.4355 0.2623 0.4343 0.0192  -0.0483 0.0178  45  ILE A CG1   
363  C  CG2   . ILE A 45  ? 0.4301 0.2414 0.4224 0.014   -0.0594 0.021   45  ILE A CG2   
364  C  CD1   . ILE A 45  ? 0.4602 0.2805 0.4522 0.0258  -0.0484 0.0164  45  ILE A CD1   
365  N  N     . PHE A 46  ? 0.4055 0.2267 0.4135 0.0059  -0.0534 0.0229  46  PHE A N     
366  C  CA    . PHE A 46  ? 0.4106 0.2303 0.4223 0.0003  -0.0567 0.0257  46  PHE A CA    
367  C  C     . PHE A 46  ? 0.4194 0.2257 0.423  0.0017  -0.0643 0.0268  46  PHE A C     
368  O  O     . PHE A 46  ? 0.4287 0.2269 0.4234 0.0075  -0.0663 0.0251  46  PHE A O     
369  C  CB    . PHE A 46  ? 0.4062 0.2343 0.427  -0.0025 -0.0515 0.0258  46  PHE A CB    
370  C  CG    . PHE A 46  ? 0.4184 0.2431 0.4371 0.0012  -0.0504 0.0244  46  PHE A CG    
371  C  CD1   . PHE A 46  ? 0.429  0.2578 0.4474 0.0056  -0.0451 0.0219  46  PHE A CD1   
372  C  CD2   . PHE A 46  ? 0.4297 0.2476 0.4473 -0.0001 -0.0546 0.026   46  PHE A CD2   
373  C  CE1   . PHE A 46  ? 0.4388 0.2647 0.4551 0.0089  -0.0438 0.021   46  PHE A CE1   
374  C  CE2   . PHE A 46  ? 0.4404 0.2546 0.4553 0.0033  -0.0537 0.0248  46  PHE A CE2   
375  C  CZ    . PHE A 46  ? 0.4385 0.2569 0.4527 0.0078  -0.0481 0.0223  46  PHE A CZ    
376  N  N     . LYS A 47  ? 0.4159 0.2194 0.4222 -0.0034 -0.0688 0.0298  47  LYS A N     
377  C  CA    . LYS A 47  ? 0.4293 0.2194 0.4281 -0.0025 -0.0768 0.0311  47  LYS A CA    
378  C  C     . LYS A 47  ? 0.434  0.2232 0.4382 -0.0069 -0.0792 0.0338  47  LYS A C     
379  O  O     . LYS A 47  ? 0.4375 0.2359 0.4518 -0.0123 -0.0763 0.0358  47  LYS A O     
380  C  CB    . LYS A 47  ? 0.4569 0.2399 0.4501 -0.0034 -0.0834 0.0327  47  LYS A CB    
381  C  CG    . LYS A 47  ? 0.5017 0.2912 0.503  -0.0105 -0.0839 0.0361  47  LYS A CG    
382  C  CD    . LYS A 47  ? 0.562  0.3473 0.5585 -0.011  -0.0886 0.0372  47  LYS A CD    
383  C  CE    . LYS A 47  ? 0.6138 0.3957 0.6129 -0.0171 -0.0949 0.0417  47  LYS A CE    
384  N  NZ    . LYS A 47  ? 0.6364 0.4273 0.6467 -0.0227 -0.0916 0.0444  47  LYS A NZ    
385  N  N     . GLU A 48  ? 0.4309 0.2086 0.4282 -0.0045 -0.0846 0.0339  48  GLU A N     
386  C  CA    . GLU A 48  ? 0.4244 0.199  0.4257 -0.0083 -0.0884 0.0366  48  GLU A CA    
387  C  C     . GLU A 48  ? 0.4287 0.1908 0.4233 -0.0095 -0.0982 0.039   48  GLU A C     
388  O  O     . GLU A 48  ? 0.4363 0.1854 0.4214 -0.0061 -0.1042 0.0384  48  GLU A O     
389  C  CB    . GLU A 48  ? 0.4416 0.212  0.4394 -0.0044 -0.0873 0.0346  48  GLU A CB    
390  C  CG    . GLU A 48  ? 0.4742 0.2569 0.4789 -0.0033 -0.0778 0.0324  48  GLU A CG    
391  C  CD    . GLU A 48  ? 0.5366 0.3161 0.5388 0.0001  -0.0763 0.0308  48  GLU A CD    
392  O  OE1   . GLU A 48  ? 0.5434 0.3101 0.5364 0.0029  -0.0824 0.0308  48  GLU A OE1   
393  O  OE2   . GLU A 48  ? 0.5635 0.353  0.5726 0       -0.0691 0.0295  48  GLU A OE2   
394  N  N     . GLY A 49  ? 0.423  0.1887 0.4218 -0.0141 -0.0998 0.0417  49  GLY A N     
395  C  CA    . GLY A 49  ? 0.4309 0.1858 0.4243 -0.0159 -0.1091 0.0444  49  GLY A CA    
396  C  C     . GLY A 49  ? 0.4365 0.1835 0.4183 -0.0102 -0.1114 0.0416  49  GLY A C     
397  O  O     . GLY A 49  ? 0.4371 0.1911 0.42   -0.0095 -0.107  0.0403  49  GLY A O     
398  N  N     . HIS A 50  ? 0.4383 0.1707 0.4087 -0.0057 -0.118  0.0404  50  HIS A N     
399  C  CA    . HIS A 50  ? 0.4443 0.1679 0.4025 0.0007  -0.1203 0.0374  50  HIS A CA    
400  C  C     . HIS A 50  ? 0.4459 0.1723 0.3999 0.0079  -0.1131 0.0329  50  HIS A C     
401  O  O     . HIS A 50  ? 0.4546 0.1779 0.4009 0.0133  -0.1125 0.0303  50  HIS A O     
402  C  CB    . HIS A 50  ? 0.4564 0.1618 0.4033 0.0026  -0.1311 0.0382  50  HIS A CB    
403  C  CG    . HIS A 50  ? 0.4729 0.1736 0.4219 -0.0033 -0.1393 0.0425  50  HIS A CG    
404  N  ND1   . HIS A 50  ? 0.4926 0.1899 0.4372 -0.0031 -0.1427 0.0429  50  HIS A ND1   
405  C  CD2   . HIS A 50  ? 0.4846 0.1828 0.4392 -0.0094 -0.1449 0.0468  50  HIS A CD2   
406  C  CE1   . HIS A 50  ? 0.499  0.1922 0.4468 -0.0092 -0.1502 0.0474  50  HIS A CE1   
407  N  NE2   . HIS A 50  ? 0.4983 0.1919 0.4522 -0.0131 -0.1518 0.05    50  HIS A NE2   
408  N  N     . ASP A 51  ? 0.4364 0.1685 0.3953 0.008   -0.1079 0.0321  51  ASP A N     
409  C  CA    . ASP A 51  ? 0.4379 0.1727 0.3932 0.0144  -0.1012 0.0285  51  ASP A CA    
410  C  C     . ASP A 51  ? 0.4326 0.183  0.3963 0.0141  -0.0918 0.0271  51  ASP A C     
411  O  O     . ASP A 51  ? 0.4294 0.1911 0.4041 0.0098  -0.0865 0.028   51  ASP A O     
412  C  CB    . ASP A 51  ? 0.4515 0.1844 0.4076 0.0148  -0.1004 0.0283  51  ASP A CB    
413  C  CG    . ASP A 51  ? 0.494  0.2113 0.442  0.0149  -0.11   0.0297  51  ASP A CG    
414  O  OD1   . ASP A 51  ? 0.4987 0.2054 0.4393 0.0153  -0.1176 0.0305  51  ASP A OD1   
415  O  OD2   . ASP A 51  ? 0.5227 0.238  0.4719 0.0144  -0.1102 0.0301  51  ASP A OD2   
416  N  N     . TYR A 52  ? 0.4307 0.1815 0.3894 0.0189  -0.0897 0.0248  52  TYR A N     
417  C  CA    . TYR A 52  ? 0.4261 0.1907 0.3922 0.019   -0.0814 0.0235  52  TYR A CA    
418  C  C     . TYR A 52  ? 0.4214 0.1912 0.3881 0.0236  -0.0743 0.0211  52  TYR A C     
419  O  O     . TYR A 52  ? 0.4319 0.1931 0.3896 0.0292  -0.0758 0.0197  52  TYR A O     
420  C  CB    . TYR A 52  ? 0.4315 0.1945 0.3925 0.0219  -0.0826 0.0225  52  TYR A CB    
421  C  CG    . TYR A 52  ? 0.4447 0.2105 0.4104 0.0159  -0.0856 0.025   52  TYR A CG    
422  C  CD1   . TYR A 52  ? 0.452  0.231  0.4273 0.0121  -0.0799 0.0254  52  TYR A CD1   
423  C  CD2   . TYR A 52  ? 0.467  0.2217 0.4268 0.0142  -0.0944 0.0269  52  TYR A CD2   
424  C  CE1   . TYR A 52  ? 0.466  0.2474 0.4447 0.0069  -0.0824 0.0277  52  TYR A CE1   
425  C  CE2   . TYR A 52  ? 0.4806 0.2379 0.4446 0.0087  -0.0971 0.0295  52  TYR A CE2   
426  C  CZ    . TYR A 52  ? 0.488  0.2588 0.4612 0.0051  -0.0909 0.0299  52  TYR A CZ    
427  O  OH    . TYR A 52  ? 0.5141 0.2874 0.4907 -0.0002 -0.0933 0.0325  52  TYR A OH    
428  N  N     . PHE A 53  ? 0.4028 0.1864 0.3796 0.0213  -0.0668 0.0208  53  PHE A N     
429  C  CA    . PHE A 53  ? 0.394  0.1842 0.3733 0.0249  -0.0597 0.0189  53  PHE A CA    
430  C  C     . PHE A 53  ? 0.3783 0.1803 0.3638 0.0252  -0.0534 0.0179  53  PHE A C     
431  O  O     . PHE A 53  ? 0.3783 0.1869 0.3703 0.0203  -0.0529 0.0189  53  PHE A O     
432  C  CB    . PHE A 53  ? 0.3904 0.1853 0.3772 0.021   -0.0572 0.0198  53  PHE A CB    
433  C  CG    . PHE A 53  ? 0.4101 0.1934 0.391  0.021   -0.0633 0.0208  53  PHE A CG    
434  C  CD1   . PHE A 53  ? 0.429  0.204  0.4009 0.0269  -0.0641 0.0194  53  PHE A CD1   
435  C  CD2   . PHE A 53  ? 0.4215 0.2019 0.4056 0.0152  -0.0687 0.0234  53  PHE A CD2   
436  C  CE1   . PHE A 53  ? 0.4443 0.2076 0.41   0.0269  -0.0704 0.0203  53  PHE A CE1   
437  C  CE2   . PHE A 53  ? 0.4365 0.2056 0.4152 0.0151  -0.075  0.0246  53  PHE A CE2   
438  C  CZ    . PHE A 53  ? 0.4405 0.2009 0.4099 0.0209  -0.076  0.0229  53  PHE A CZ    
439  N  N     . HIS A 54  ? 0.3622 0.1668 0.3457 0.0308  -0.0488 0.016   54  HIS A N     
440  C  CA    . HIS A 54  ? 0.3504 0.1657 0.3397 0.0316  -0.0432 0.0152  54  HIS A CA    
441  C  C     . HIS A 54  ? 0.3416 0.1647 0.3363 0.033   -0.0364 0.0145  54  HIS A C     
442  O  O     . HIS A 54  ? 0.3495 0.1684 0.3386 0.0384  -0.0354 0.0137  54  HIS A O     
443  C  CB    . HIS A 54  ? 0.3624 0.1727 0.3435 0.038   -0.0445 0.014   54  HIS A CB    
444  C  CG    . HIS A 54  ? 0.3674 0.1876 0.354  0.0388  -0.04   0.0134  54  HIS A CG    
445  N  ND1   . HIS A 54  ? 0.3862 0.2037 0.3671 0.0447  -0.0404 0.0125  54  HIS A ND1   
446  C  CD2   . HIS A 54  ? 0.3704 0.2024 0.3675 0.0345  -0.0356 0.0137  54  HIS A CD2   
447  C  CE1   . HIS A 54  ? 0.3857 0.2136 0.3742 0.0435  -0.0363 0.0124  54  HIS A CE1   
448  N  NE2   . HIS A 54  ? 0.3792 0.2157 0.3771 0.0374  -0.0335 0.0131  54  HIS A NE2   
449  N  N     . TRP A 55  ? 0.3252 0.1594 0.3306 0.0283  -0.0321 0.0148  55  TRP A N     
450  C  CA    . TRP A 55  ? 0.3155 0.1575 0.327  0.029   -0.0259 0.0143  55  TRP A CA    
451  C  C     . TRP A 55  ? 0.3004 0.154  0.32   0.028   -0.0209 0.0138  55  TRP A C     
452  O  O     . TRP A 55  ? 0.2958 0.1528 0.3188 0.0243  -0.0218 0.0141  55  TRP A O     
453  C  CB    . TRP A 55  ? 0.3123 0.1564 0.3298 0.0239  -0.0255 0.0151  55  TRP A CB    
454  C  CG    . TRP A 55  ? 0.3277 0.1615 0.339  0.0246  -0.0299 0.0157  55  TRP A CG    
455  C  CD1   . TRP A 55  ? 0.3469 0.1698 0.3473 0.0299  -0.0333 0.0153  55  TRP A CD1   
456  C  CD2   . TRP A 55  ? 0.3301 0.1635 0.3458 0.0198  -0.0313 0.0168  55  TRP A CD2   
457  N  NE1   . TRP A 55  ? 0.3556 0.1709 0.3531 0.0285  -0.0373 0.0161  55  TRP A NE1   
458  C  CE2   . TRP A 55  ? 0.3473 0.1692 0.3546 0.0223  -0.036  0.0172  55  TRP A CE2   
459  C  CE3   . TRP A 55  ? 0.3286 0.1702 0.3546 0.014   -0.0291 0.0176  55  TRP A CE3   
460  C  CZ2   . TRP A 55  ? 0.3541 0.1728 0.3636 0.0188  -0.0387 0.0185  55  TRP A CZ2   
461  C  CZ3   . TRP A 55  ? 0.3384 0.1772 0.3667 0.0108  -0.0314 0.0189  55  TRP A CZ3   
462  C  CH2   . TRP A 55  ? 0.3467 0.1743 0.3671 0.013   -0.0362 0.0194  55  TRP A CH2   
463  N  N     . ARG A 56  ? 0.2922 0.1517 0.3151 0.0309  -0.0156 0.0133  56  ARG A N     
464  C  CA    . ARG A 56  ? 0.2869 0.1577 0.3186 0.0295  -0.011  0.0131  56  ARG A CA    
465  C  C     . ARG A 56  ? 0.2832 0.1606 0.322  0.0283  -0.0063 0.0131  56  ARG A C     
466  O  O     . ARG A 56  ? 0.2873 0.1619 0.3231 0.0317  -0.0049 0.0132  56  ARG A O     
467  C  CB    . ARG A 56  ? 0.299  0.1718 0.3288 0.0346  -0.0094 0.0128  56  ARG A CB    
468  C  CG    . ARG A 56  ? 0.3102 0.1936 0.349  0.0319  -0.0062 0.0128  56  ARG A CG    
469  C  CD    . ARG A 56  ? 0.3338 0.2203 0.3724 0.0368  -0.0044 0.0128  56  ARG A CD    
470  N  NE    . ARG A 56  ? 0.3663 0.2564 0.4068 0.041   0.0001  0.0133  56  ARG A NE    
471  C  CZ    . ARG A 56  ? 0.403  0.2894 0.4374 0.0476  0.0007  0.0135  56  ARG A CZ    
472  N  NH1   . ARG A 56  ? 0.4081 0.2865 0.4337 0.0511  -0.0031 0.0131  56  ARG A NH1   
473  N  NH2   . ARG A 56  ? 0.4013 0.2918 0.438  0.051   0.0053  0.0143  56  ARG A NH2   
474  N  N     . PHE A 57  ? 0.2747 0.16   0.3222 0.0233  -0.0041 0.013   57  PHE A N     
475  C  CA    . PHE A 57  ? 0.2711 0.1628 0.3259 0.0215  0.0001  0.013   57  PHE A CA    
476  C  C     . PHE A 57  ? 0.273  0.1741 0.3348 0.0219  0.0042  0.0128  57  PHE A C     
477  O  O     . PHE A 57  ? 0.2709 0.1765 0.3366 0.0188  0.004   0.0125  57  PHE A O     
478  C  CB    . PHE A 57  ? 0.2591 0.1522 0.3187 0.0156  -0.0008 0.013   57  PHE A CB    
479  C  CG    . PHE A 57  ? 0.2628 0.1474 0.3172 0.0148  -0.0048 0.0136  57  PHE A CG    
480  C  CD1   . PHE A 57  ? 0.2681 0.1496 0.3218 0.0158  -0.0044 0.0139  57  PHE A CD1   
481  C  CD2   . PHE A 57  ? 0.2689 0.1482 0.3193 0.0128  -0.0094 0.0142  57  PHE A CD2   
482  C  CE1   . PHE A 57  ? 0.2736 0.1469 0.3227 0.0149  -0.0086 0.0146  57  PHE A CE1   
483  C  CE2   . PHE A 57  ? 0.2732 0.1445 0.3193 0.0118  -0.0136 0.0151  57  PHE A CE2   
484  C  CZ    . PHE A 57  ? 0.2695 0.1378 0.3151 0.0129  -0.0133 0.0153  57  PHE A CZ    
485  N  N     . ASP A 58  ? 0.2757 0.1797 0.3388 0.0257  0.0076  0.0132  58  ASP A N     
486  C  CA    . ASP A 58  ? 0.2796 0.1927 0.3501 0.026   0.0113  0.0136  58  ASP A CA    
487  C  C     . ASP A 58  ? 0.2851 0.2041 0.3637 0.0226  0.0143  0.0135  58  ASP A C     
488  O  O     . ASP A 58  ? 0.2906 0.2077 0.3686 0.0236  0.0155  0.0139  58  ASP A O     
489  C  CB    . ASP A 58  ? 0.2881 0.2015 0.3559 0.0323  0.0135  0.0146  58  ASP A CB    
490  C  CG    . ASP A 58  ? 0.3379 0.2453 0.3975 0.0363  0.0105  0.0144  58  ASP A CG    
491  O  OD1   . ASP A 58  ? 0.3565 0.2618 0.4146 0.0338  0.0072  0.0137  58  ASP A OD1   
492  O  OD2   . ASP A 58  ? 0.3509 0.2553 0.4052 0.0422  0.0116  0.015   58  ASP A OD2   
493  N  N     . MET A 59  ? 0.2787 0.204  0.3644 0.0185  0.0152  0.013   59  MET A N     
494  C  CA    . MET A 59  ? 0.2806 0.211  0.3738 0.015   0.0175  0.0127  59  MET A CA    
495  C  C     . MET A 59  ? 0.2779 0.2156 0.378  0.0163  0.021   0.0136  59  MET A C     
496  O  O     . MET A 59  ? 0.2761 0.2177 0.3783 0.0174  0.0215  0.014   59  MET A O     
497  C  CB    . MET A 59  ? 0.2881 0.2203 0.3843 0.0099  0.0163  0.0115  59  MET A CB    
498  C  CG    . MET A 59  ? 0.3227 0.2485 0.4137 0.0082  0.0132  0.0112  59  MET A CG    
499  S  SD    . MET A 59  ? 0.4139 0.3414 0.5065 0.003   0.0116  0.0103  59  MET A SD    
500  C  CE    . MET A 59  ? 0.4463 0.3687 0.5312 0.005   0.0079  0.0107  59  MET A CE    
501  N  N     . PHE A 60  ? 0.279  0.2184 0.3827 0.0161  0.0233  0.0141  60  PHE A N     
502  C  CA    . PHE A 60  ? 0.2877 0.2339 0.3984 0.017   0.0266  0.0154  60  PHE A CA    
503  C  C     . PHE A 60  ? 0.301  0.2514 0.4194 0.0124  0.0275  0.0146  60  PHE A C     
504  O  O     . PHE A 60  ? 0.2986 0.2483 0.4185 0.0118  0.0286  0.0148  60  PHE A O     
505  C  CB    . PHE A 60  ? 0.2866 0.2309 0.3943 0.0214  0.0286  0.017   60  PHE A CB    
506  C  CG    . PHE A 60  ? 0.2961 0.2383 0.3979 0.0268  0.0286  0.0181  60  PHE A CG    
507  C  CD1   . PHE A 60  ? 0.3112 0.2457 0.4038 0.0287  0.0256  0.0172  60  PHE A CD1   
508  C  CD2   . PHE A 60  ? 0.3007 0.2486 0.4062 0.0301  0.0316  0.0202  60  PHE A CD2   
509  C  CE1   . PHE A 60  ? 0.322  0.2541 0.4087 0.034   0.0256  0.018   60  PHE A CE1   
510  C  CE2   . PHE A 60  ? 0.3084 0.2545 0.4084 0.0355  0.032   0.0212  60  PHE A CE2   
511  C  CZ    . PHE A 60  ? 0.3116 0.2496 0.4019 0.0376  0.0289  0.0199  60  PHE A CZ    
512  N  N     . PRO A 61  ? 0.31   0.2645 0.4329 0.0093  0.027   0.0136  61  PRO A N     
513  C  CA    . PRO A 61  ? 0.3182 0.276  0.4476 0.0052  0.0276  0.0125  61  PRO A CA    
514  C  C     . PRO A 61  ? 0.3349 0.2983 0.4719 0.0053  0.0299  0.0139  61  PRO A C     
515  O  O     . PRO A 61  ? 0.3351 0.3027 0.4753 0.0069  0.0307  0.0154  61  PRO A O     
516  C  CB    . PRO A 61  ? 0.3222 0.2813 0.4522 0.0023  0.0258  0.011   61  PRO A CB    
517  C  CG    . PRO A 61  ? 0.327  0.2833 0.4507 0.0048  0.0241  0.0114  61  PRO A CG    
518  C  CD    . PRO A 61  ? 0.3047 0.2603 0.4265 0.0094  0.0254  0.0133  61  PRO A CD    
519  N  N     . GLY A 62  ? 0.346  0.3095 0.4864 0.0034  0.0308  0.0135  62  GLY A N     
520  C  CA    . GLY A 62  ? 0.3606 0.329  0.5085 0.0029  0.0327  0.0148  62  GLY A CA    
521  C  C     . GLY A 62  ? 0.3828 0.3509 0.5299 0.0063  0.0347  0.0172  62  GLY A C     
522  O  O     . GLY A 62  ? 0.3899 0.359  0.535  0.0098  0.0357  0.0191  62  GLY A O     
523  N  N     . PHE A 63  ? 0.3975 0.3642 0.546  0.0054  0.0356  0.0173  63  PHE A N     
524  C  CA    . PHE A 63  ? 0.4224 0.3886 0.5697 0.0086  0.0376  0.0198  63  PHE A CA    
525  C  C     . PHE A 63  ? 0.4433 0.4163 0.5987 0.0086  0.0397  0.0223  63  PHE A C     
526  O  O     . PHE A 63  ? 0.4449 0.4221 0.6075 0.0054  0.0391  0.0218  63  PHE A O     
527  C  CB    . PHE A 63  ? 0.4243 0.3862 0.5703 0.0074  0.0373  0.019   63  PHE A CB    
528  C  CG    . PHE A 63  ? 0.4344 0.3891 0.5724 0.0078  0.0353  0.0175  63  PHE A CG    
529  C  CD1   . PHE A 63  ? 0.4471 0.3969 0.577  0.0118  0.0351  0.0185  63  PHE A CD1   
530  C  CD2   . PHE A 63  ? 0.4439 0.3966 0.5827 0.0043  0.0335  0.0152  63  PHE A CD2   
531  C  CE1   . PHE A 63  ? 0.4614 0.4041 0.5842 0.012   0.0327  0.0172  63  PHE A CE1   
532  C  CE2   . PHE A 63  ? 0.4587 0.4052 0.5912 0.0045  0.0315  0.0143  63  PHE A CE2   
533  C  CZ    . PHE A 63  ? 0.4602 0.4015 0.5848 0.0081  0.0308  0.0154  63  PHE A CZ    
534  N  N     . ASN A 64  ? 0.4557 0.4295 0.6099 0.0123  0.0421  0.0252  64  ASN A N     
535  C  CA    . ASN A 64  ? 0.4648 0.4453 0.6268 0.0126  0.0443  0.0284  64  ASN A CA    
536  C  C     . ASN A 64  ? 0.4854 0.4661 0.6522 0.0098  0.0445  0.0286  64  ASN A C     
537  O  O     . ASN A 64  ? 0.4873 0.4624 0.6498 0.0092  0.0438  0.0271  64  ASN A O     
538  C  CB    . ASN A 64  ? 0.4694 0.4504 0.6276 0.0178  0.0472  0.0316  64  ASN A CB    
539  C  CG    . ASN A 64  ? 0.5056 0.4886 0.6616 0.0212  0.0477  0.0324  64  ASN A CG    
540  O  OD1   . ASN A 64  ? 0.5181 0.5014 0.6745 0.0196  0.0456  0.0306  64  ASN A OD1   
541  N  ND2   . ASN A 64  ? 0.5173 0.5016 0.6708 0.026   0.0506  0.0354  64  ASN A ND2   
542  N  N     . LYS A 65  ? 0.4952 0.4821 0.6712 0.008   0.0453  0.0307  65  LYS A N     
543  C  CA    . LYS A 65  ? 0.5108 0.4983 0.6921 0.0054  0.0455  0.0314  65  LYS A CA    
544  C  C     . LYS A 65  ? 0.524  0.5153 0.7074 0.0083  0.0486  0.036   65  LYS A C     
545  O  O     . LYS A 65  ? 0.531  0.5232 0.7184 0.0071  0.0493  0.0377  65  LYS A O     
546  C  CB    . LYS A 65  ? 0.5274 0.5188 0.7177 0.0009  0.0435  0.0305  65  LYS A CB    
547  C  CG    . LYS A 65  ? 0.5737 0.5642 0.7631 -0.0011 0.0411  0.0271  65  LYS A CG    
548  C  CD    . LYS A 65  ? 0.629  0.6151 0.817  -0.0041 0.0391  0.0232  65  LYS A CD    
549  C  CE    . LYS A 65  ? 0.675  0.6571 0.8558 -0.0038 0.0379  0.0202  65  LYS A CE    
550  N  NZ    . LYS A 65  ? 0.7035 0.6809 0.8763 -0.0007 0.0388  0.0205  65  LYS A NZ    
551  N  N     . ASN A 68  ? 0.4773 0.4787 0.6461 0.0309  0.0596  0.0469  68  ASN A N     
552  C  CA    . ASN A 68  ? 0.4818 0.4877 0.6536 0.0322  0.0593  0.0473  68  ASN A CA    
553  C  C     . ASN A 68  ? 0.4739 0.4842 0.6554 0.0266  0.0563  0.0463  68  ASN A C     
554  O  O     . ASN A 68  ? 0.4737 0.49   0.6611 0.027   0.0563  0.0481  68  ASN A O     
555  C  CB    . ASN A 68  ? 0.502  0.5147 0.6766 0.0371  0.0636  0.0522  68  ASN A CB    
556  C  CG    . ASN A 68  ? 0.5526 0.5722 0.7362 0.036   0.0664  0.0568  68  ASN A CG    
557  O  OD1   . ASN A 68  ? 0.5686 0.5902 0.76   0.0307  0.0646  0.0568  68  ASN A OD1   
558  N  ND2   . ASN A 68  ? 0.5633 0.5863 0.7457 0.0412  0.0709  0.061   68  ASN A ND2   
559  N  N     . ASP A 69  ? 0.4636 0.4708 0.6465 0.0217  0.0537  0.0435  69  ASP A N     
560  C  CA    . ASP A 69  ? 0.4557 0.4651 0.6461 0.0163  0.0505  0.0418  69  ASP A CA    
561  C  C     . ASP A 69  ? 0.4454 0.4536 0.6335 0.0157  0.0478  0.0391  69  ASP A C     
562  O  O     . ASP A 69  ? 0.4429 0.4563 0.6381 0.014   0.0466  0.0402  69  ASP A O     
563  C  CB    . ASP A 69  ? 0.4827 0.4875 0.6725 0.0124  0.0489  0.0391  69  ASP A CB    
564  C  CG    . ASP A 69  ? 0.5497 0.5542 0.7439 0.0073  0.0454  0.0361  69  ASP A CG    
565  O  OD1   . ASP A 69  ? 0.5605 0.5706 0.7632 0.0051  0.0444  0.0377  69  ASP A OD1   
566  O  OD2   . ASP A 69  ? 0.583  0.5817 0.772  0.0055  0.0436  0.0323  69  ASP A OD2   
567  N  N     . ARG A 70  ? 0.4385 0.4396 0.6166 0.0169  0.0467  0.0358  70  ARG A N     
568  C  CA    . ARG A 70  ? 0.4346 0.4337 0.6092 0.0165  0.0441  0.0333  70  ARG A CA    
569  C  C     . ARG A 70  ? 0.4342 0.4309 0.6009 0.0221  0.0454  0.034   70  ARG A C     
570  O  O     . ARG A 70  ? 0.4342 0.4352 0.6034 0.0244  0.0459  0.0358  70  ARG A O     
571  C  CB    . ARG A 70  ? 0.4454 0.4383 0.6157 0.0128  0.0413  0.0289  70  ARG A CB    
572  C  CG    . ARG A 70  ? 0.4663 0.4547 0.6293 0.0132  0.039   0.0262  70  ARG A CG    
573  C  CD    . ARG A 70  ? 0.4871 0.4726 0.6498 0.0086  0.0364  0.0227  70  ARG A CD    
574  N  NE    . ARG A 70  ? 0.5139 0.4948 0.6694 0.0086  0.0342  0.0204  70  ARG A NE    
575  C  CZ    . ARG A 70  ? 0.537  0.5195 0.6927 0.0085  0.0326  0.0201  70  ARG A CZ    
576  N  NH1   . ARG A 70  ? 0.5316 0.5201 0.6943 0.0086  0.0329  0.0221  70  ARG A NH1   
577  N  NH2   . ARG A 70  ? 0.5404 0.5184 0.6894 0.0083  0.0306  0.0181  70  ARG A NH2   
578  N  N     . TRP A 71  ? 0.4293 0.4192 0.5867 0.0246  0.046   0.0328  71  TRP A N     
579  C  CA    . TRP A 71  ? 0.4294 0.4154 0.5779 0.0302  0.0469  0.0332  71  TRP A CA    
580  C  C     . TRP A 71  ? 0.4221 0.4119 0.5716 0.0348  0.051   0.0371  71  TRP A C     
581  O  O     . TRP A 71  ? 0.4177 0.4101 0.5718 0.0336  0.0529  0.0389  71  TRP A O     
582  C  CB    . TRP A 71  ? 0.4343 0.4108 0.5724 0.0304  0.0451  0.0303  71  TRP A CB    
583  C  CG    . TRP A 71  ? 0.4397 0.4129 0.577  0.0258  0.0415  0.0268  71  TRP A CG    
584  C  CD1   . TRP A 71  ? 0.4482 0.4199 0.5878 0.0212  0.0402  0.025   71  TRP A CD1   
585  C  CD2   . TRP A 71  ? 0.4427 0.4143 0.5773 0.0252  0.0388  0.025   71  TRP A CD2   
586  N  NE1   . TRP A 71  ? 0.4528 0.4221 0.5909 0.0181  0.0373  0.0223  71  TRP A NE1   
587  C  CE2   . TRP A 71  ? 0.4524 0.4215 0.5873 0.0204  0.0363  0.0223  71  TRP A CE2   
588  C  CE3   . TRP A 71  ? 0.4512 0.423  0.5828 0.0286  0.0384  0.0256  71  TRP A CE3   
589  C  CZ2   . TRP A 71  ? 0.4616 0.4285 0.5936 0.0186  0.0335  0.0202  71  TRP A CZ2   
590  C  CZ3   . TRP A 71  ? 0.4622 0.4315 0.5912 0.0267  0.0352  0.0234  71  TRP A CZ3   
591  C  CH2   . TRP A 71  ? 0.4629 0.4299 0.592  0.0217  0.0328  0.0208  71  TRP A CH2   
592  N  N     . ASN A 72  ? 0.4185 0.4083 0.5635 0.0404  0.0526  0.0384  72  ASN A N     
593  C  CA    . ASN A 72  ? 0.4156 0.4092 0.5608 0.0458  0.057   0.0424  72  ASN A CA    
594  C  C     . ASN A 72  ? 0.4115 0.4003 0.5505 0.0475  0.0589  0.0428  72  ASN A C     
595  O  O     . ASN A 72  ? 0.4162 0.4094 0.5579 0.0502  0.0628  0.0465  72  ASN A O     
596  C  CB    . ASN A 72  ? 0.4318 0.4248 0.5714 0.0519  0.0579  0.043   72  ASN A CB    
597  C  CG    . ASN A 72  ? 0.4806 0.4629 0.6059 0.0558  0.0567  0.0404  72  ASN A CG    
598  O  OD1   . ASN A 72  ? 0.4956 0.4704 0.6154 0.0528  0.0532  0.037   72  ASN A OD1   
599  N  ND2   . ASN A 72  ? 0.4969 0.478  0.6158 0.0628  0.0594  0.0421  72  ASN A ND2   
600  N  N     . SER A 73  ? 0.3976 0.3771 0.5281 0.0461  0.0561  0.0394  73  SER A N     
601  C  CA    . SER A 73  ? 0.3884 0.3619 0.5124 0.0471  0.0567  0.0392  73  SER A CA    
602  C  C     . SER A 73  ? 0.3724 0.3405 0.4957 0.0416  0.0529  0.0357  73  SER A C     
603  O  O     . SER A 73  ? 0.3728 0.3394 0.4963 0.0387  0.0497  0.0331  73  SER A O     
604  C  CB    . SER A 73  ? 0.4152 0.3812 0.5262 0.0537  0.0575  0.039   73  SER A CB    
605  O  OG    . SER A 73  ? 0.4532 0.4143 0.5577 0.0554  0.0546  0.0365  73  SER A OG    
606  N  N     . ASN A 74  ? 0.3581 0.3238 0.481  0.04    0.0533  0.036   74  ASN A N     
607  C  CA    . ASN A 74  ? 0.3549 0.3162 0.4781 0.035   0.05    0.0331  74  ASN A CA    
608  C  C     . ASN A 74  ? 0.3473 0.2979 0.4588 0.0368  0.0476  0.031   74  ASN A C     
609  O  O     . ASN A 74  ? 0.3522 0.2986 0.4574 0.0402  0.0489  0.0322  74  ASN A O     
610  C  CB    . ASN A 74  ? 0.3697 0.3344 0.5002 0.0318  0.0514  0.0345  74  ASN A CB    
611  C  CG    . ASN A 74  ? 0.4074 0.3699 0.5412 0.0262  0.0484  0.0317  74  ASN A CG    
612  O  OD1   . ASN A 74  ? 0.4098 0.3681 0.5402 0.0245  0.0454  0.0287  74  ASN A OD1   
613  N  ND2   . ASN A 74  ? 0.4229 0.3885 0.5637 0.0233  0.0492  0.0328  74  ASN A ND2   
614  N  N     . ILE A 75  ? 0.3336 0.2797 0.4423 0.0343  0.0439  0.0279  75  ILE A N     
615  C  CA    . ILE A 75  ? 0.3312 0.2671 0.4296 0.0353  0.0409  0.0261  75  ILE A CA    
616  C  C     . ILE A 75  ? 0.3236 0.2562 0.4223 0.0332  0.0404  0.0261  75  ILE A C     
617  O  O     . ILE A 75  ? 0.3296 0.2543 0.4195 0.0358  0.0393  0.0261  75  ILE A O     
618  C  CB    . ILE A 75  ? 0.3337 0.266  0.4299 0.0328  0.037   0.0234  75  ILE A CB    
619  C  CG1   . ILE A 75  ? 0.349  0.2705 0.4332 0.0354  0.0338  0.0223  75  ILE A CG1   
620  C  CG2   . ILE A 75  ? 0.3327 0.2676 0.4365 0.0265  0.0355  0.0218  75  ILE A CG2   
621  C  CD1   . ILE A 75  ? 0.3629 0.2809 0.4384 0.0421  0.0349  0.0235  75  ILE A CD1   
622  N  N     . LEU A 76  ? 0.3107 0.249  0.4192 0.0287  0.0413  0.0263  76  LEU A N     
623  C  CA    . LEU A 76  ? 0.3153 0.2513 0.4253 0.0266  0.041   0.0265  76  LEU A CA    
624  C  C     . LEU A 76  ? 0.3243 0.2584 0.4298 0.0306  0.0435  0.0291  76  LEU A C     
625  O  O     . LEU A 76  ? 0.3322 0.2621 0.4362 0.0297  0.0426  0.0292  76  LEU A O     
626  C  CB    . LEU A 76  ? 0.309  0.2518 0.4305 0.0215  0.0414  0.0261  76  LEU A CB    
627  C  CG    . LEU A 76  ? 0.3243 0.2685 0.4497 0.0175  0.0391  0.0235  76  LEU A CG    
628  C  CD1   . LEU A 76  ? 0.3262 0.277  0.4622 0.0133  0.0399  0.0232  76  LEU A CD1   
629  C  CD2   . LEU A 76  ? 0.3345 0.2712 0.4545 0.016   0.0358  0.0213  76  LEU A CD2   
630  N  N     . ASP A 77  ? 0.3207 0.2578 0.424  0.0353  0.0465  0.0313  77  ASP A N     
631  C  CA    . ASP A 77  ? 0.3269 0.2623 0.425  0.0398  0.0493  0.034   77  ASP A CA    
632  C  C     . ASP A 77  ? 0.3352 0.259  0.42   0.043   0.0468  0.0328  77  ASP A C     
633  O  O     . ASP A 77  ? 0.3373 0.2571 0.4177 0.0446  0.0476  0.0341  77  ASP A O     
634  C  CB    . ASP A 77  ? 0.3486 0.2903 0.4476 0.0443  0.0533  0.0367  77  ASP A CB    
635  C  CG    . ASP A 77  ? 0.4138 0.3585 0.5131 0.0472  0.0575  0.0405  77  ASP A CG    
636  O  OD1   . ASP A 77  ? 0.4213 0.3696 0.5281 0.0436  0.0582  0.0417  77  ASP A OD1   
637  O  OD2   . ASP A 77  ? 0.4483 0.3919 0.5405 0.0533  0.0602  0.0423  77  ASP A OD2   
638  N  N     . LEU A 78  ? 0.3395 0.2572 0.4179 0.0435  0.0433  0.0303  78  LEU A N     
639  C  CA    . LEU A 78  ? 0.3596 0.2655 0.4256 0.046   0.04    0.0291  78  LEU A CA    
640  C  C     . LEU A 78  ? 0.3683 0.2696 0.4353 0.042   0.0373  0.0283  78  LEU A C     
641  O  O     . LEU A 78  ? 0.3766 0.2687 0.4342 0.0443  0.0353  0.0284  78  LEU A O     
642  C  CB    . LEU A 78  ? 0.3686 0.2695 0.4292 0.0464  0.0362  0.0267  78  LEU A CB    
643  C  CG    . LEU A 78  ? 0.3922 0.2947 0.4489 0.0512  0.038   0.0271  78  LEU A CG    
644  C  CD1   . LEU A 78  ? 0.4002 0.298  0.4528 0.0506  0.0338  0.0248  78  LEU A CD1   
645  C  CD2   . LEU A 78  ? 0.4081 0.3054 0.4539 0.0584  0.04    0.0287  78  LEU A CD2   
646  N  N     . LEU A 79  ? 0.3628 0.2701 0.441  0.0362  0.037   0.0277  79  LEU A N     
647  C  CA    . LEU A 79  ? 0.3722 0.2762 0.4528 0.0325  0.0347  0.0271  79  LEU A CA    
648  C  C     . LEU A 79  ? 0.3794 0.2848 0.4611 0.0336  0.0376  0.0295  79  LEU A C     
649  O  O     . LEU A 79  ? 0.3908 0.2889 0.4667 0.0343  0.0357  0.0298  79  LEU A O     
650  C  CB    . LEU A 79  ? 0.3698 0.2796 0.4615 0.0265  0.0338  0.0255  79  LEU A CB    
651  C  CG    . LEU A 79  ? 0.391  0.2991 0.4818 0.0247  0.0307  0.0232  79  LEU A CG    
652  C  CD1   . LEU A 79  ? 0.3968 0.3113 0.4984 0.0193  0.0306  0.0219  79  LEU A CD1   
653  C  CD2   . LEU A 79  ? 0.4019 0.2997 0.4844 0.0249  0.0263  0.0223  79  LEU A CD2   
654  N  N     . SER A 80  ? 0.3708 0.2854 0.4598 0.0339  0.0418  0.0316  80  SER A N     
655  C  CA    . SER A 80  ? 0.3738 0.2904 0.4645 0.0348  0.0447  0.0344  80  SER A CA    
656  C  C     . SER A 80  ? 0.3817 0.2918 0.4601 0.041   0.046   0.0362  80  SER A C     
657  O  O     . SER A 80  ? 0.3795 0.2874 0.4559 0.0417  0.047   0.038   80  SER A O     
658  C  CB    . SER A 80  ? 0.3829 0.3108 0.4848 0.0333  0.0485  0.0365  80  SER A CB    
659  O  OG    . SER A 80  ? 0.4112 0.3438 0.5129 0.0364  0.0508  0.0373  80  SER A OG    
660  N  N     . GLN A 81  ? 0.3898 0.2961 0.4593 0.0455  0.0459  0.0355  81  GLN A N     
661  C  CA    . GLN A 81  ? 0.403  0.3016 0.459  0.052   0.0467  0.0367  81  GLN A CA    
662  C  C     . GLN A 81  ? 0.4193 0.3056 0.4658 0.0518  0.042   0.0351  81  GLN A C     
663  O  O     . GLN A 81  ? 0.4295 0.309  0.4656 0.0562  0.0426  0.0364  81  GLN A O     
664  C  CB    . GLN A 81  ? 0.416  0.313  0.465  0.0567  0.047   0.0358  81  GLN A CB    
665  C  CG    . GLN A 81  ? 0.4432 0.3513 0.4994 0.0585  0.0519  0.0379  81  GLN A CG    
666  C  CD    . GLN A 81  ? 0.4836 0.3897 0.5329 0.0633  0.0518  0.0369  81  GLN A CD    
667  O  OE1   . GLN A 81  ? 0.506  0.4021 0.542  0.068   0.05    0.0359  81  GLN A OE1   
668  N  NE2   . GLN A 81  ? 0.4726 0.3877 0.5305 0.0623  0.0535  0.0373  81  GLN A NE2   
669  N  N     . LYS A 82  ? 0.4194 0.3028 0.4692 0.0469  0.0374  0.0326  82  LYS A N     
670  C  CA    . LYS A 82  ? 0.4335 0.3057 0.4759 0.0461  0.0324  0.0313  82  LYS A CA    
671  C  C     . LYS A 82  ? 0.4337 0.3067 0.4834 0.0412  0.0312  0.0317  82  LYS A C     
672  O  O     . LYS A 82  ? 0.4435 0.3082 0.4893 0.0396  0.0266  0.0306  82  LYS A O     
673  C  CB    . LYS A 82  ? 0.4619 0.3288 0.5014 0.0446  0.0275  0.0286  82  LYS A CB    
674  C  CG    . LYS A 82  ? 0.5279 0.3889 0.5557 0.0503  0.0269  0.0281  82  LYS A CG    
675  C  CD    . LYS A 82  ? 0.606  0.455  0.6191 0.0554  0.0251  0.0286  82  LYS A CD    
676  C  CE    . LYS A 82  ? 0.6748 0.5172 0.6755 0.0615  0.0243  0.0279  82  LYS A CE    
677  N  NZ    . LYS A 82  ? 0.7211 0.549  0.7063 0.0656  0.0204  0.0276  82  LYS A NZ    
678  N  N     . GLY A 83  ? 0.4207 0.3032 0.4809 0.039   0.0349  0.0333  83  GLY A N     
679  C  CA    . GLY A 83  ? 0.4182 0.3014 0.4853 0.0347  0.0339  0.0337  83  GLY A CA    
680  C  C     . GLY A 83  ? 0.4088 0.2998 0.4897 0.0287  0.0335  0.0323  83  GLY A C     
681  O  O     . GLY A 83  ? 0.4104 0.3017 0.4972 0.0252  0.0324  0.0324  83  GLY A O     
682  N  N     . SER A 84  ? 0.3982 0.2953 0.4841 0.0276  0.0343  0.031   84  SER A N     
683  C  CA    . SER A 84  ? 0.3989 0.3032 0.4972 0.0223  0.0342  0.0297  84  SER A CA    
684  C  C     . SER A 84  ? 0.407  0.3203 0.514  0.0216  0.0382  0.0318  84  SER A C     
685  O  O     . SER A 84  ? 0.4056 0.3259 0.5164 0.0222  0.0409  0.0324  84  SER A O     
686  C  CB    . SER A 84  ? 0.4086 0.3156 0.5085 0.0214  0.0334  0.0276  84  SER A CB    
687  O  OG    . SER A 84  ? 0.4319 0.3442 0.5422 0.0164  0.0327  0.026   84  SER A OG    
688  N  N     . PHE A 85  ? 0.4115 0.3243 0.5214 0.0201  0.0385  0.0332  85  PHE A N     
689  C  CA    . PHE A 85  ? 0.4167 0.3372 0.5345 0.0193  0.0419  0.0358  85  PHE A CA    
690  C  C     . PHE A 85  ? 0.4225 0.3503 0.5532 0.0143  0.0416  0.0346  85  PHE A C     
691  O  O     . PHE A 85  ? 0.42   0.3545 0.5579 0.0133  0.044   0.0367  85  PHE A O     
692  C  CB    . PHE A 85  ? 0.415  0.3318 0.5298 0.0204  0.0424  0.0383  85  PHE A CB    
693  C  CG    . PHE A 85  ? 0.4223 0.3328 0.5372 0.0175  0.0385  0.0368  85  PHE A CG    
694  C  CD1   . PHE A 85  ? 0.4254 0.3397 0.551  0.0127  0.0373  0.0357  85  PHE A CD1   
695  C  CD2   . PHE A 85  ? 0.4364 0.337  0.5407 0.0198  0.0359  0.0366  85  PHE A CD2   
696  C  CE1   . PHE A 85  ? 0.4331 0.3419 0.5594 0.0103  0.0339  0.0344  85  PHE A CE1   
697  C  CE2   . PHE A 85  ? 0.4441 0.3391 0.5492 0.0171  0.0322  0.0355  85  PHE A CE2   
698  C  CZ    . PHE A 85  ? 0.4354 0.3349 0.5518 0.0124  0.0313  0.0345  85  PHE A CZ    
699  N  N     . LEU A 86  ? 0.4289 0.3552 0.5622 0.0112  0.0387  0.0314  86  LEU A N     
700  C  CA    . LEU A 86  ? 0.4351 0.3678 0.5794 0.007   0.0386  0.0299  86  LEU A CA    
701  C  C     . LEU A 86  ? 0.4516 0.3899 0.5981 0.0072  0.0399  0.0291  86  LEU A C     
702  O  O     . LEU A 86  ? 0.4598 0.3957 0.5992 0.0099  0.0398  0.0287  86  LEU A O     
703  C  CB    . LEU A 86  ? 0.4307 0.3599 0.5775 0.0037  0.0353  0.0271  86  LEU A CB    
704  C  CG    . LEU A 86  ? 0.4424 0.3664 0.5887 0.0028  0.0336  0.0278  86  LEU A CG    
705  C  CD1   . LEU A 86  ? 0.4468 0.369  0.5973 -0.0004 0.0308  0.0252  86  LEU A CD1   
706  C  CD2   . LEU A 86  ? 0.4463 0.3742 0.5988 0.0019  0.0353  0.03    86  LEU A CD2   
707  N  N     . TYR A 87  ? 0.4534 0.3987 0.6094 0.0045  0.0408  0.029   87  TYR A N     
708  C  CA    . TYR A 87  ? 0.4648 0.4153 0.6234 0.0043  0.0415  0.0282  87  TYR A CA    
709  C  C     . TYR A 87  ? 0.4712 0.4196 0.6296 0.002   0.0391  0.0246  87  TYR A C     
710  O  O     . TYR A 87  ? 0.4729 0.4242 0.6383 -0.0014 0.0383  0.0228  87  TYR A O     
711  C  CB    . TYR A 87  ? 0.4637 0.4217 0.6321 0.0022  0.0429  0.0296  87  TYR A CB    
712  N  N     . GLU A 88  ? 0.4683 0.4111 0.6185 0.0038  0.0377  0.0236  88  GLU A N     
713  C  CA    . GLU A 88  ? 0.4641 0.4045 0.6136 0.0018  0.0354  0.0207  88  GLU A CA    
714  C  C     . GLU A 88  ? 0.4608 0.4007 0.6049 0.0035  0.0351  0.02    88  GLU A C     
715  O  O     . GLU A 88  ? 0.4662 0.4022 0.6024 0.007   0.035   0.0211  88  GLU A O     
716  C  CB    . GLU A 88  ? 0.4919 0.4257 0.6382 0.0012  0.033   0.0202  88  GLU A CB    
717  C  CG    . GLU A 88  ? 0.5364 0.4709 0.6891 -0.001  0.033   0.0205  88  GLU A CG    
718  C  CD    . GLU A 88  ? 0.5765 0.5157 0.7384 -0.0047 0.0329  0.0185  88  GLU A CD    
719  O  OE1   . GLU A 88  ? 0.575  0.5178 0.7389 -0.0057 0.0332  0.0169  88  GLU A OE1   
720  O  OE2   . GLU A 88  ? 0.5897 0.5283 0.7561 -0.0064 0.0323  0.0184  88  GLU A OE2   
721  N  N     . THR A 89  ? 0.4505 0.3941 0.5986 0.0012  0.0347  0.0181  89  THR A N     
722  C  CA    . THR A 89  ? 0.4474 0.3911 0.5914 0.0022  0.0342  0.0173  89  THR A CA    
723  C  C     . THR A 89  ? 0.4444 0.385  0.5869 0.0001  0.0319  0.0151  89  THR A C     
724  O  O     . THR A 89  ? 0.452  0.3953 0.6003 -0.0031 0.0316  0.0135  89  THR A O     
725  C  CB    . THR A 89  ? 0.4555 0.4061 0.6054 0.0012  0.0356  0.0172  89  THR A CB    
726  O  OG1   . THR A 89  ? 0.4653 0.4194 0.6175 0.0031  0.0378  0.0198  89  THR A OG1   
727  C  CG2   . THR A 89  ? 0.4598 0.4108 0.6063 0.0019  0.035   0.0163  89  THR A CG2   
728  N  N     . PRO A 90  ? 0.4259 0.3607 0.5607 0.0018  0.03    0.0152  90  PRO A N     
729  C  CA    . PRO A 90  ? 0.4079 0.3403 0.5416 -0.0004 0.0277  0.0136  90  PRO A CA    
730  C  C     . PRO A 90  ? 0.385  0.3214 0.5198 -0.0015 0.028   0.0124  90  PRO A C     
731  O  O     . PRO A 90  ? 0.3809 0.3211 0.5166 -0.0002 0.0295  0.0129  90  PRO A O     
732  C  CB    . PRO A 90  ? 0.4234 0.3481 0.5482 0.002   0.0253  0.0145  90  PRO A CB    
733  C  CG    . PRO A 90  ? 0.4353 0.3593 0.5552 0.006   0.0267  0.016   90  PRO A CG    
734  C  CD    . PRO A 90  ? 0.4173 0.3476 0.5437 0.006   0.0299  0.0168  90  PRO A CD    
735  N  N     . ASP A 91  ? 0.3675 0.3031 0.5025 -0.0039 0.0264  0.0111  91  ASP A N     
736  C  CA    . ASP A 91  ? 0.3555 0.2944 0.4908 -0.005  0.0266  0.01    91  ASP A CA    
737  C  C     . ASP A 91  ? 0.339  0.2752 0.4672 -0.0023 0.0255  0.0108  91  ASP A C     
738  O  O     . ASP A 91  ? 0.3375 0.2772 0.4662 -0.0018 0.0263  0.0105  91  ASP A O     
739  C  CB    . ASP A 91  ? 0.3782 0.3178 0.5161 -0.0082 0.0257  0.0086  91  ASP A CB    
740  C  CG    . ASP A 91  ? 0.4374 0.3809 0.5829 -0.0106 0.0273  0.0074  91  ASP A CG    
741  O  OD1   . ASP A 91  ? 0.4467 0.3935 0.596  -0.0102 0.0289  0.0073  91  ASP A OD1   
742  O  OD2   . ASP A 91  ? 0.4669 0.4102 0.6147 -0.0127 0.0269  0.0066  91  ASP A OD2   
743  N  N     . VAL A 92  ? 0.3242 0.2538 0.4457 -0.0004 0.0234  0.0117  92  VAL A N     
744  C  CA    . VAL A 92  ? 0.315  0.2407 0.4287 0.0025  0.0218  0.0123  92  VAL A CA    
745  C  C     . VAL A 92  ? 0.2957 0.2149 0.4027 0.0062  0.0209  0.0137  92  VAL A C     
746  O  O     . VAL A 92  ? 0.2915 0.2071 0.3983 0.0055  0.0198  0.014   92  VAL A O     
747  C  CB    . VAL A 92  ? 0.3323 0.255  0.443  0.0006  0.0189  0.0118  92  VAL A CB    
748  C  CG1   . VAL A 92  ? 0.3464 0.2633 0.4483 0.0036  0.0165  0.0125  92  VAL A CG1   
749  C  CG2   . VAL A 92  ? 0.3373 0.2658 0.4528 -0.0024 0.0199  0.0106  92  VAL A CG2   
750  N  N     . ILE A 93  ? 0.2829 0.2004 0.3841 0.0101  0.0211  0.0144  93  ILE A N     
751  C  CA    . ILE A 93  ? 0.2801 0.1906 0.3728 0.0144  0.0201  0.0155  93  ILE A CA    
752  C  C     . ILE A 93  ? 0.2772 0.183  0.3622 0.0165  0.0175  0.0152  93  ILE A C     
753  O  O     . ILE A 93  ? 0.2756 0.1854 0.3615 0.0175  0.0187  0.015   93  ILE A O     
754  C  CB    . ILE A 93  ? 0.2812 0.1947 0.3741 0.018   0.0236  0.0168  93  ILE A CB    
755  C  CG1   . ILE A 93  ? 0.2905 0.2084 0.391  0.0159  0.026   0.0172  93  ILE A CG1   
756  C  CG2   . ILE A 93  ? 0.2899 0.1955 0.3722 0.0232  0.0226  0.0177  93  ILE A CG2   
757  C  CD1   . ILE A 93  ? 0.3136 0.2256 0.4117 0.0154  0.0243  0.0175  93  ILE A CD1   
758  N  N     . ILE A 94  ? 0.2754 0.1724 0.3531 0.0171  0.0136  0.0153  94  ILE A N     
759  C  CA    . ILE A 94  ? 0.2787 0.1702 0.3486 0.0192  0.0105  0.0151  94  ILE A CA    
760  C  C     . ILE A 94  ? 0.2939 0.1789 0.3545 0.025   0.0103  0.0158  94  ILE A C     
761  O  O     . ILE A 94  ? 0.2982 0.1776 0.3551 0.026   0.0091  0.0163  94  ILE A O     
762  C  CB    . ILE A 94  ? 0.2792 0.1649 0.3469 0.0161  0.0058  0.015   94  ILE A CB    
763  C  CG1   . ILE A 94  ? 0.2814 0.1737 0.3584 0.0105  0.0065  0.0145  94  ILE A CG1   
764  C  CG2   . ILE A 94  ? 0.2857 0.1653 0.3452 0.0183  0.0023  0.0149  94  ILE A CG2   
765  C  CD1   . ILE A 94  ? 0.2933 0.1809 0.3696 0.0072  0.0023  0.015   94  ILE A CD1   
766  N  N     . THR A 95  ? 0.3012 0.187  0.358  0.029   0.0115  0.0158  95  THR A N     
767  C  CA    . THR A 95  ? 0.3205 0.2002 0.3677 0.0352  0.0116  0.0164  95  THR A CA    
768  C  C     . THR A 95  ? 0.3532 0.2249 0.3908 0.0381  0.0076  0.0158  95  THR A C     
769  O  O     . THR A 95  ? 0.3553 0.2282 0.3947 0.0355  0.0055  0.0152  95  THR A O     
770  C  CB    . THR A 95  ? 0.3232 0.2103 0.3737 0.0386  0.017   0.0174  95  THR A CB    
771  O  OG1   . THR A 95  ? 0.3303 0.223  0.3838 0.039   0.0181  0.0172  95  THR A OG1   
772  C  CG2   . THR A 95  ? 0.3218 0.2164 0.3819 0.0356  0.0205  0.0181  95  THR A CG2   
773  N  N     . SER A 96  ? 0.3719 0.235  0.3988 0.0435  0.0063  0.016   96  SER A N     
774  C  CA    . SER A 96  ? 0.3923 0.2469 0.409  0.0472  0.0025  0.0154  96  SER A CA    
775  C  C     . SER A 96  ? 0.4111 0.2676 0.4237 0.054   0.0064  0.0158  96  SER A C     
776  O  O     . SER A 96  ? 0.4113 0.269  0.4228 0.0572  0.0099  0.0167  96  SER A O     
777  C  CB    . SER A 96  ? 0.4162 0.2579 0.4226 0.0486  -0.0026 0.0152  96  SER A CB    
778  O  OG    . SER A 96  ? 0.4561 0.2886 0.4519 0.0524  -0.0068 0.0146  96  SER A OG    
779  N  N     . LEU A 97  ? 0.4242 0.2815 0.435  0.0561  0.0058  0.0154  97  LEU A N     
780  C  CA    . LEU A 97  ? 0.4441 0.303  0.451  0.0629  0.0092  0.0159  97  LEU A CA    
781  C  C     . LEU A 97  ? 0.4831 0.329  0.4752 0.0689  0.0057  0.0152  97  LEU A C     
782  O  O     . LEU A 97  ? 0.4939 0.3317 0.4799 0.0685  0.0002  0.0141  97  LEU A O     
783  C  CB    . LEU A 97  ? 0.4386 0.3043 0.4506 0.0627  0.0101  0.0158  97  LEU A CB    
784  C  CG    . LEU A 97  ? 0.4435 0.3227 0.4692 0.0588  0.0145  0.0166  97  LEU A CG    
785  C  CD1   . LEU A 97  ? 0.4452 0.3296 0.4738 0.0601  0.015   0.0166  97  LEU A CD1   
786  C  CD2   . LEU A 97  ? 0.4488 0.3344 0.4785 0.0612  0.0201  0.0183  97  LEU A CD2   
787  N  N     . ASN A 98  ? 0.501  0.3443 0.487  0.0744  0.0086  0.0159  98  ASN A N     
788  C  CA    . ASN A 98  ? 0.5282 0.3584 0.4989 0.081   0.0056  0.0151  98  ASN A CA    
789  C  C     . ASN A 98  ? 0.5342 0.3667 0.5007 0.0885  0.0113  0.0163  98  ASN A C     
790  O  O     . ASN A 98  ? 0.5304 0.3702 0.5028 0.088   0.0163  0.0178  98  ASN A O     
791  C  CB    . ASN A 98  ? 0.5578 0.377  0.5219 0.0789  0.0007  0.0146  98  ASN A CB    
792  C  CG    . ASN A 98  ? 0.6069 0.4316 0.5793 0.074   0.0031  0.0157  98  ASN A CG    
793  O  OD1   . ASN A 98  ? 0.6268 0.4506 0.604  0.0677  -0.0004 0.0154  98  ASN A OD1   
794  N  ND2   . ASN A 98  ? 0.6149 0.4455 0.5895 0.0768  0.009   0.017   98  ASN A ND2   
795  N  N     . ASN A 99  ? 0.5424 0.3692 0.499  0.0956  0.0108  0.0156  99  ASN A N     
796  C  CA    . ASN A 99  ? 0.5532 0.3816 0.5046 0.1038  0.0163  0.0168  99  ASN A CA    
797  C  C     . ASN A 99  ? 0.5469 0.3917 0.5121 0.1031  0.0236  0.0191  99  ASN A C     
798  O  O     . ASN A 99  ? 0.5494 0.3986 0.5149 0.1068  0.0292  0.021   99  ASN A O     
799  C  CB    . ASN A 99  ? 0.579  0.3987 0.5198 0.1076  0.0166  0.0171  99  ASN A CB    
800  C  CG    . ASN A 99  ? 0.6289 0.4347 0.5608 0.1048  0.0092  0.0154  99  ASN A CG    
801  O  OD1   . ASN A 99  ? 0.6426 0.4475 0.5767 0.1009  0.0087  0.016   99  ASN A OD1   
802  N  ND2   . ASN A 99  ? 0.6423 0.4369 0.5645 0.1067  0.0029  0.0135  99  ASN A ND2   
803  N  N     . GLY A 100 ? 0.5366 0.3901 0.5131 0.0981  0.0233  0.019   100 GLY A N     
804  C  CA    . GLY A 100 ? 0.5284 0.397  0.5185 0.0968  0.0291  0.0212  100 GLY A CA    
805  C  C     . GLY A 100 ? 0.5211 0.3985 0.5221 0.0916  0.0326  0.0228  100 GLY A C     
806  O  O     . GLY A 100 ? 0.5195 0.4084 0.5302 0.0919  0.038   0.0251  100 GLY A O     
807  N  N     . LYS A 101 ? 0.5129 0.3848 0.5126 0.0868  0.0295  0.0218  101 LYS A N     
808  C  CA    . LYS A 101 ? 0.5046 0.3833 0.5139 0.0817  0.032   0.0231  101 LYS A CA    
809  C  C     . LYS A 101 ? 0.4934 0.3689 0.506  0.074   0.0272  0.0214  101 LYS A C     
810  O  O     . LYS A 101 ? 0.5013 0.3677 0.5069 0.0733  0.0217  0.0195  101 LYS A O     
811  C  CB    . LYS A 101 ? 0.5389 0.4139 0.5413 0.0861  0.0349  0.0245  101 LYS A CB    
812  C  CG    . LYS A 101 ? 0.6117 0.4721 0.6013 0.0869  0.0298  0.0228  101 LYS A CG    
813  C  CD    . LYS A 101 ? 0.6795 0.5355 0.6612 0.0915  0.0324  0.0241  101 LYS A CD    
814  C  CE    . LYS A 101 ? 0.74   0.5825 0.7115 0.0906  0.0268  0.0226  101 LYS A CE    
815  N  NZ    . LYS A 101 ? 0.7725 0.6176 0.7536 0.0821  0.0244  0.0222  101 LYS A NZ    
816  N  N     . GLU A 102 ? 0.4726 0.3555 0.4959 0.0684  0.029   0.0222  102 GLU A N     
817  C  CA    . GLU A 102 ? 0.4656 0.3464 0.4928 0.0615  0.0251  0.0208  102 GLU A CA    
818  C  C     . GLU A 102 ? 0.4583 0.3321 0.4808 0.0608  0.0236  0.0208  102 GLU A C     
819  O  O     . GLU A 102 ? 0.4584 0.3336 0.4801 0.0634  0.0272  0.0224  102 GLU A O     
820  C  CB    . GLU A 102 ? 0.4814 0.3739 0.5231 0.0554  0.0273  0.0211  102 GLU A CB    
821  C  CG    . GLU A 102 ? 0.5296 0.4298 0.5771 0.0556  0.0288  0.0213  102 GLU A CG    
822  C  CD    . GLU A 102 ? 0.592  0.5015 0.6521 0.0492  0.0296  0.0211  102 GLU A CD    
823  O  OE1   . GLU A 102 ? 0.5914 0.4987 0.6535 0.044   0.0267  0.0198  102 GLU A OE1   
824  O  OE2   . GLU A 102 ? 0.6253 0.544  0.6932 0.0494  0.0329  0.0224  102 GLU A OE2   
825  N  N     . GLU A 103 ? 0.4504 0.3168 0.47   0.0572  0.0183  0.0194  103 GLU A N     
826  C  CA    . GLU A 103 ? 0.452  0.3117 0.4683 0.0558  0.0162  0.0195  103 GLU A CA    
827  C  C     . GLU A 103 ? 0.4357 0.2982 0.4611 0.0482  0.0137  0.0188  103 GLU A C     
828  O  O     . GLU A 103 ? 0.44   0.3017 0.4665 0.0455  0.0105  0.0177  103 GLU A O     
829  C  CB    . GLU A 103 ? 0.5019 0.3473 0.5031 0.0602  0.0116  0.0188  103 GLU A CB    
830  C  CG    . GLU A 103 ? 0.6007 0.4384 0.5985 0.0583  0.0084  0.0189  103 GLU A CG    
831  C  CD    . GLU A 103 ? 0.703  0.5429 0.7015 0.0599  0.0124  0.0203  103 GLU A CD    
832  O  OE1   . GLU A 103 ? 0.7331 0.5643 0.7199 0.0652  0.012   0.0207  103 GLU A OE1   
833  O  OE2   . GLU A 103 ? 0.7264 0.5761 0.7366 0.0558  0.0158  0.0212  103 GLU A OE2   
834  N  N     . ILE A 104 ? 0.4169 0.2834 0.4493 0.0449  0.0154  0.0194  104 ILE A N     
835  C  CA    . ILE A 104 ? 0.4081 0.2777 0.4494 0.0381  0.0136  0.0188  104 ILE A CA    
836  C  C     . ILE A 104 ? 0.4056 0.2653 0.4415 0.0361  0.0075  0.0181  104 ILE A C     
837  O  O     . ILE A 104 ? 0.4113 0.2621 0.4393 0.0383  0.0051  0.0185  104 ILE A O     
838  C  CB    . ILE A 104 ? 0.407  0.2834 0.4574 0.0354  0.017   0.0196  104 ILE A CB    
839  C  CG1   . ILE A 104 ? 0.4126 0.3001 0.4708 0.036   0.0224  0.0204  104 ILE A CG1   
840  C  CG2   . ILE A 104 ? 0.4078 0.2858 0.4661 0.0291  0.0148  0.0189  104 ILE A CG2   
841  C  CD1   . ILE A 104 ? 0.4236 0.3181 0.491  0.0334  0.0256  0.0214  104 ILE A CD1   
842  N  N     . LEU A 105 ? 0.3966 0.2577 0.4369 0.0318  0.0049  0.0173  105 LEU A N     
843  C  CA    . LEU A 105 ? 0.4003 0.2536 0.4377 0.029   -0.0009 0.0172  105 LEU A CA    
844  C  C     . LEU A 105 ? 0.3914 0.2485 0.4382 0.0236  -0.0008 0.0175  105 LEU A C     
845  O  O     . LEU A 105 ? 0.3902 0.2404 0.4345 0.0225  -0.0045 0.018   105 LEU A O     
846  C  CB    . LEU A 105 ? 0.4034 0.2564 0.4406 0.0272  -0.0037 0.0166  105 LEU A CB    
847  C  CG    . LEU A 105 ? 0.4239 0.2714 0.4512 0.0322  -0.0052 0.0162  105 LEU A CG    
848  C  CD1   . LEU A 105 ? 0.4282 0.276  0.4566 0.0294  -0.0081 0.0159  105 LEU A CD1   
849  C  CD2   . LEU A 105 ? 0.4411 0.2757 0.456  0.0362  -0.0094 0.0164  105 LEU A CD2   
850  N  N     . MET A 106 ? 0.384  0.2519 0.4417 0.0204  0.0031  0.0172  106 MET A N     
851  C  CA    . MET A 106 ? 0.3865 0.2589 0.4537 0.0156  0.0037  0.0172  106 MET A CA    
852  C  C     . MET A 106 ? 0.385  0.269  0.4624 0.0136  0.0088  0.0167  106 MET A C     
853  O  O     . MET A 106 ? 0.3836 0.2724 0.4617 0.0149  0.0111  0.0163  106 MET A O     
854  C  CB    . MET A 106 ? 0.3916 0.2617 0.461  0.0114  -0.0004 0.0173  106 MET A CB    
855  C  CG    . MET A 106 ? 0.4124 0.288  0.4853 0.0094  0.0002  0.0166  106 MET A CG    
856  S  SD    . MET A 106 ? 0.4406 0.3122 0.5139 0.0052  -0.005  0.0174  106 MET A SD    
857  C  CE    . MET A 106 ? 0.4271 0.2863 0.4872 0.0093  -0.0102 0.0179  106 MET A CE    
858  N  N     . ALA A 107 ? 0.3831 0.2709 0.4684 0.0105  0.01    0.0167  107 ALA A N     
859  C  CA    . ALA A 107 ? 0.3858 0.2835 0.481  0.008   0.0139  0.016   107 ALA A CA    
860  C  C     . ALA A 107 ? 0.3914 0.2915 0.4933 0.0033  0.0126  0.0153  107 ALA A C     
861  O  O     . ALA A 107 ? 0.3954 0.291  0.4971 0.0017  0.0098  0.0159  107 ALA A O     
862  C  CB    . ALA A 107 ? 0.3858 0.2855 0.4843 0.0087  0.0165  0.0167  107 ALA A CB    
863  N  N     . ILE A 108 ? 0.3903 0.2975 0.4979 0.001   0.0146  0.0143  108 ILE A N     
864  C  CA    . ILE A 108 ? 0.3966 0.3068 0.5104 -0.0031 0.0141  0.0137  108 ILE A CA    
865  C  C     . ILE A 108 ? 0.4115 0.3299 0.534  -0.0051 0.0177  0.0125  108 ILE A C     
866  O  O     . ILE A 108 ? 0.4095 0.3323 0.5331 -0.004  0.02    0.012   108 ILE A O     
867  C  CB    . ILE A 108 ? 0.3962 0.3054 0.5067 -0.004  0.0121  0.0136  108 ILE A CB    
868  C  CG1   . ILE A 108 ? 0.4039 0.3041 0.5058 -0.0022 0.0078  0.0148  108 ILE A CG1   
869  C  CG2   . ILE A 108 ? 0.4009 0.3142 0.518  -0.0081 0.0122  0.0132  108 ILE A CG2   
870  C  CD1   . ILE A 108 ? 0.4152 0.3139 0.513  -0.0024 0.0058  0.0149  108 ILE A CD1   
871  N  N     . GLU A 109 ? 0.4249 0.3452 0.5537 -0.0079 0.0178  0.0121  109 GLU A N     
872  C  CA    . GLU A 109 ? 0.4433 0.3705 0.58   -0.0098 0.0208  0.0108  109 GLU A CA    
873  C  C     . GLU A 109 ? 0.4637 0.3933 0.6044 -0.0128 0.0205  0.01    109 GLU A C     
874  O  O     . GLU A 109 ? 0.4677 0.3943 0.6085 -0.014  0.0184  0.011   109 GLU A O     
875  C  CB    . GLU A 109 ? 0.4705 0.3979 0.6116 -0.0098 0.0217  0.011   109 GLU A CB    
876  C  CG    . GLU A 109 ? 0.5356 0.4691 0.685  -0.0119 0.0241  0.0095  109 GLU A CG    
877  C  CD    . GLU A 109 ? 0.6285 0.5663 0.7802 -0.011  0.0265  0.0089  109 GLU A CD    
878  O  OE1   . GLU A 109 ? 0.6473 0.5839 0.7955 -0.0086 0.0269  0.0102  109 GLU A OE1   
879  O  OE2   . GLU A 109 ? 0.6567 0.5993 0.8139 -0.0128 0.028   0.0074  109 GLU A OE2   
880  N  N     . PHE A 110 ? 0.4765 0.4115 0.62   -0.014  0.0225  0.0086  110 PHE A N     
881  C  CA    . PHE A 110 ? 0.4965 0.4342 0.6432 -0.0166 0.0229  0.0079  110 PHE A CA    
882  C  C     . PHE A 110 ? 0.515  0.4572 0.669  -0.0179 0.0252  0.0064  110 PHE A C     
883  O  O     . PHE A 110 ? 0.5164 0.4613 0.6724 -0.0173 0.0269  0.0052  110 PHE A O     
884  C  CB    . PHE A 110 ? 0.496  0.4357 0.6396 -0.0169 0.0231  0.0073  110 PHE A CB    
885  C  CG    . PHE A 110 ? 0.5086 0.4437 0.645  -0.0157 0.0205  0.0087  110 PHE A CG    
886  C  CD1   . PHE A 110 ? 0.5191 0.4507 0.6535 -0.0169 0.018   0.0102  110 PHE A CD1   
887  C  CD2   . PHE A 110 ? 0.5206 0.4548 0.6523 -0.0134 0.0204  0.0087  110 PHE A CD2   
888  C  CE1   . PHE A 110 ? 0.5316 0.4584 0.6591 -0.0159 0.0151  0.0114  110 PHE A CE1   
889  C  CE2   . PHE A 110 ? 0.533  0.4626 0.6578 -0.012  0.0179  0.0098  110 PHE A CE2   
890  C  CZ    . PHE A 110 ? 0.5323 0.458  0.6548 -0.0133 0.0151  0.011   110 PHE A CZ    
891  N  N     . CYS A 111 ? 0.5268 0.4699 0.685  -0.0197 0.0252  0.0064  111 CYS A N     
892  C  CA    . CYS A 111 ? 0.5422 0.4891 0.7072 -0.0207 0.0274  0.0049  111 CYS A CA    
893  C  C     . CYS A 111 ? 0.5608 0.5111 0.7279 -0.0224 0.0286  0.0042  111 CYS A C     
894  O  O     . CYS A 111 ? 0.5643 0.5135 0.7309 -0.0234 0.0274  0.0059  111 CYS A O     
895  C  CB    . CYS A 111 ? 0.5478 0.4925 0.7167 -0.0207 0.0265  0.0058  111 CYS A CB    
896  S  SG    . CYS A 111 ? 0.5868 0.5358 0.7643 -0.0217 0.0288  0.0038  111 CYS A SG    
897  N  N     . SER A 112 ? 0.5701 0.5244 0.7393 -0.0227 0.031   0.002   112 SER A N     
898  C  CA    . SER A 112 ? 0.5837 0.5413 0.7539 -0.0239 0.0327  0.0011  112 SER A CA    
899  C  C     . SER A 112 ? 0.5939 0.5533 0.7699 -0.0247 0.0337  0.0014  112 SER A C     
900  O  O     . SER A 112 ? 0.6003 0.5622 0.7769 -0.0257 0.0349  0.0017  112 SER A O     
901  C  CB    . SER A 112 ? 0.6002 0.5606 0.7702 -0.0236 0.0346  -0.0016 112 SER A CB    
902  O  OG    . SER A 112 ? 0.6272 0.5881 0.8015 -0.023  0.0352  -0.0031 112 SER A OG    
903  N  N     . ALA A 113 ? 0.594  0.5524 0.7746 -0.0244 0.0334  0.0014  113 ALA A N     
904  C  CA    . ALA A 113 ? 0.5988 0.559  0.7858 -0.025  0.0343  0.0018  113 ALA A CA    
905  C  C     . ALA A 113 ? 0.601  0.5581 0.7912 -0.0248 0.0322  0.0033  113 ALA A C     
906  O  O     . ALA A 113 ? 0.6066 0.5609 0.795  -0.0239 0.0311  0.0031  113 ALA A O     
907  C  CB    . ALA A 113 ? 0.6    0.5637 0.7906 -0.0245 0.0371  -0.0012 113 ALA A CB    
908  N  N     . LEU A 114 ? 0.5925 0.5501 0.7876 -0.0257 0.0318  0.0049  114 LEU A N     
909  C  CA    . LEU A 114 ? 0.5933 0.5478 0.7918 -0.0256 0.0296  0.0063  114 LEU A CA    
910  C  C     . LEU A 114 ? 0.5884 0.5446 0.7919 -0.0248 0.0314  0.0039  114 LEU A C     
911  O  O     . LEU A 114 ? 0.5913 0.5511 0.8005 -0.0249 0.0333  0.003   114 LEU A O     
912  C  CB    . LEU A 114 ? 0.5958 0.5506 0.7989 -0.0269 0.0283  0.0089  114 LEU A CB    
913  C  CG    . LEU A 114 ? 0.6172 0.5676 0.8229 -0.0271 0.0251  0.0108  114 LEU A CG    
914  C  CD1   . LEU A 114 ? 0.6301 0.5741 0.8283 -0.0264 0.0219  0.0119  114 LEU A CD1   
915  C  CD2   . LEU A 114 ? 0.6219 0.5731 0.833  -0.0286 0.0236  0.0137  114 LEU A CD2   
916  N  N     . GLN A 115 ? 0.5779 0.532  0.7791 -0.0239 0.0308  0.0029  115 GLN A N     
917  C  CA    . GLN A 115 ? 0.5723 0.5275 0.7776 -0.0233 0.032   0.0007  115 GLN A CA    
918  C  C     . GLN A 115 ? 0.5614 0.5155 0.7731 -0.0235 0.0309  0.0016  115 GLN A C     
919  O  O     . GLN A 115 ? 0.5619 0.513  0.7736 -0.024  0.0286  0.004   115 GLN A O     
920  C  CB    . GLN A 115 ? 0.5971 0.5506 0.7986 -0.0226 0.0316  0.0001  115 GLN A CB    
921  C  CG    . GLN A 115 ? 0.6501 0.6052 0.8463 -0.0224 0.0327  -0.0008 115 GLN A CG    
922  C  CD    . GLN A 115 ? 0.7145 0.6676 0.9062 -0.0216 0.0317  -0.0002 115 GLN A CD    
923  O  OE1   . GLN A 115 ? 0.7402 0.6901 0.9308 -0.021  0.0302  0.0015  115 GLN A OE1   
924  N  NE2   . GLN A 115 ? 0.7193 0.6743 0.908  -0.0214 0.0327  -0.0014 115 GLN A NE2   
925  N  N     . ALA A 116 ? 0.547  0.503  0.764  -0.0231 0.0324  -0.0005 116 ALA A N     
926  C  CA    . ALA A 116 ? 0.5364 0.4918 0.7601 -0.0231 0.0315  0       116 ALA A CA    
927  C  C     . ALA A 116 ? 0.5284 0.4824 0.7545 -0.0226 0.0312  -0.0016 116 ALA A C     
928  O  O     . ALA A 116 ? 0.5338 0.4883 0.7572 -0.0222 0.032   -0.0033 116 ALA A O     
929  C  CB    . ALA A 116 ? 0.5336 0.4932 0.7628 -0.0231 0.0336  -0.0007 116 ALA A CB    
930  N  N     . GLY A 117 ? 0.5131 0.4653 0.7443 -0.0226 0.0296  -0.0008 117 GLY A N     
931  C  CA    . GLY A 117 ? 0.5013 0.4518 0.735  -0.0223 0.0289  -0.0018 117 GLY A CA    
932  C  C     . GLY A 117 ? 0.4881 0.4352 0.7165 -0.0224 0.0273  -0.0003 117 GLY A C     
933  O  O     . GLY A 117 ? 0.4944 0.4389 0.7183 -0.0225 0.0259  0.002   117 GLY A O     
934  N  N     . ASN A 118 ? 0.4689 0.4158 0.6974 -0.0222 0.0276  -0.0015 118 ASN A N     
935  C  CA    . ASN A 118 ? 0.4606 0.4051 0.6843 -0.022  0.0266  0.0003  118 ASN A CA    
936  C  C     . ASN A 118 ? 0.4522 0.3981 0.6695 -0.0217 0.0277  0.0004  118 ASN A C     
937  O  O     . ASN A 118 ? 0.4533 0.3972 0.6659 -0.0213 0.0271  0.0022  118 ASN A O     
938  C  CB    . ASN A 118 ? 0.4662 0.4101 0.6927 -0.0222 0.0261  0       118 ASN A CB    
939  C  CG    . ASN A 118 ? 0.484  0.4306 0.7131 -0.0223 0.0273  -0.0028 118 ASN A CG    
940  O  OD1   . ASN A 118 ? 0.4927 0.442  0.72   -0.0221 0.0288  -0.0045 118 ASN A OD1   
941  N  ND2   . ASN A 118 ? 0.4824 0.4282 0.7157 -0.0226 0.0263  -0.0031 118 ASN A ND2   
942  N  N     . GLN A 119 ? 0.4441 0.3932 0.6611 -0.0218 0.0294  -0.0015 119 GLN A N     
943  C  CA    . GLN A 119 ? 0.4488 0.3991 0.6599 -0.0216 0.0302  -0.0014 119 GLN A CA    
944  C  C     . GLN A 119 ? 0.4369 0.3845 0.6432 -0.0214 0.029   0.001   119 GLN A C     
945  O  O     . GLN A 119 ? 0.4393 0.3864 0.6399 -0.0209 0.029   0.0019  119 GLN A O     
946  C  CB    . GLN A 119 ? 0.4866 0.4404 0.6983 -0.0218 0.0321  -0.0039 119 GLN A CB    
947  C  CG    . GLN A 119 ? 0.566  0.5211 0.7721 -0.0216 0.0329  -0.0042 119 GLN A CG    
948  C  CD    . GLN A 119 ? 0.6619 0.6199 0.8674 -0.0218 0.0346  -0.0062 119 GLN A CD    
949  O  OE1   . GLN A 119 ? 0.698  0.657  0.9057 -0.0219 0.0354  -0.0063 119 GLN A OE1   
950  N  NE2   . GLN A 119 ? 0.6721 0.6315 0.8745 -0.0217 0.0352  -0.0076 119 GLN A NE2   
951  N  N     . ALA A 120 ? 0.4241 0.3699 0.6328 -0.0218 0.0277  0.0022  120 ALA A N     
952  C  CA    . ALA A 120 ? 0.4198 0.3622 0.6243 -0.0218 0.0257  0.0046  120 ALA A CA    
953  C  C     . ALA A 120 ? 0.4135 0.3515 0.6125 -0.0208 0.0241  0.0065  120 ALA A C     
954  O  O     . ALA A 120 ? 0.4224 0.3578 0.6151 -0.0202 0.023   0.0079  120 ALA A O     
955  C  CB    . ALA A 120 ? 0.4201 0.3614 0.6297 -0.0226 0.0243  0.0057  120 ALA A CB    
956  N  N     . TRP A 121 ? 0.3954 0.3322 0.5964 -0.0205 0.0239  0.0066  121 TRP A N     
957  C  CA    . TRP A 121 ? 0.3876 0.3205 0.5833 -0.0192 0.0228  0.0086  121 TRP A CA    
958  C  C     . TRP A 121 ? 0.3857 0.3209 0.5796 -0.0184 0.0247  0.0083  121 TRP A C     
959  O  O     . TRP A 121 ? 0.3882 0.3209 0.578  -0.0171 0.0243  0.0101  121 TRP A O     
960  C  CB    . TRP A 121 ? 0.3791 0.3081 0.577  -0.0194 0.0209  0.0099  121 TRP A CB    
961  C  CG    . TRP A 121 ? 0.3728 0.3042 0.578  -0.0201 0.0216  0.0087  121 TRP A CG    
962  C  CD1   . TRP A 121 ? 0.3786 0.3114 0.5848 -0.0199 0.0227  0.0087  121 TRP A CD1   
963  C  CD2   . TRP A 121 ? 0.3658 0.2978 0.5783 -0.0212 0.0209  0.0078  121 TRP A CD2   
964  N  NE1   . TRP A 121 ? 0.3772 0.3111 0.5906 -0.0208 0.0225  0.0075  121 TRP A NE1   
965  C  CE2   . TRP A 121 ? 0.3727 0.3061 0.5899 -0.0215 0.0215  0.0069  121 TRP A CE2   
966  C  CE3   . TRP A 121 ? 0.3662 0.2981 0.5821 -0.0219 0.0199  0.0078  121 TRP A CE3   
967  C  CZ2   . TRP A 121 ? 0.3762 0.3102 0.6008 -0.0222 0.0209  0.0058  121 TRP A CZ2   
968  C  CZ3   . TRP A 121 ? 0.3729 0.306  0.5965 -0.0225 0.0197  0.0069  121 TRP A CZ3   
969  C  CH2   . TRP A 121 ? 0.3748 0.3088 0.6025 -0.0225 0.0202  0.0057  121 TRP A CH2   
970  N  N     . GLN A 122 ? 0.3783 0.3183 0.5752 -0.019  0.0265  0.0063  122 GLN A N     
971  C  CA    . GLN A 122 ? 0.3772 0.3199 0.5736 -0.0186 0.0279  0.0061  122 GLN A CA    
972  C  C     . GLN A 122 ? 0.3789 0.3204 0.5682 -0.017  0.0281  0.0079  122 GLN A C     
973  O  O     . GLN A 122 ? 0.3769 0.3188 0.5653 -0.0161 0.0288  0.0093  122 GLN A O     
974  C  CB    . GLN A 122 ? 0.3914 0.3385 0.5907 -0.0195 0.0293  0.0034  122 GLN A CB    
975  C  CG    . GLN A 122 ? 0.4303 0.3802 0.6301 -0.0195 0.0303  0.0031  122 GLN A CG    
976  C  CD    . GLN A 122 ? 0.4802 0.4332 0.6834 -0.0205 0.031   0.0002  122 GLN A CD    
977  O  OE1   . GLN A 122 ? 0.4972 0.4511 0.7052 -0.0212 0.0308  -0.0009 122 GLN A OE1   
978  N  NE2   . GLN A 122 ? 0.4831 0.4374 0.6834 -0.0205 0.0317  -0.001  122 GLN A NE2   
979  N  N     . ARG A 123 ? 0.3782 0.3179 0.5625 -0.0165 0.0275  0.008   123 ARG A N     
980  C  CA    . ARG A 123 ? 0.3793 0.3172 0.5561 -0.0146 0.0274  0.0095  123 ARG A CA    
981  C  C     . ARG A 123 ? 0.3759 0.3075 0.5471 -0.0133 0.0253  0.0114  123 ARG A C     
982  O  O     . ARG A 123 ? 0.3819 0.3108 0.5462 -0.0118 0.0246  0.0122  123 ARG A O     
983  C  CB    . ARG A 123 ? 0.3962 0.336  0.5707 -0.015  0.0277  0.0083  123 ARG A CB    
984  N  N     . SER A 124 ? 0.3653 0.2941 0.5389 -0.0138 0.024   0.0121  124 SER A N     
985  C  CA    . SER A 124 ? 0.3611 0.2832 0.5291 -0.0125 0.0216  0.014   124 SER A CA    
986  C  C     . SER A 124 ? 0.3545 0.2739 0.5159 -0.0098 0.0222  0.0159  124 SER A C     
987  O  O     . SER A 124 ? 0.3563 0.2697 0.5104 -0.0081 0.0203  0.0172  124 SER A O     
988  C  CB    . SER A 124 ? 0.3674 0.2871 0.5401 -0.0139 0.0198  0.0143  124 SER A CB    
989  O  OG    . SER A 124 ? 0.3799 0.3001 0.5563 -0.0157 0.0186  0.0134  124 SER A OG    
990  N  N     . GLY A 125 ? 0.3455 0.2696 0.5095 -0.0094 0.0248  0.0161  125 GLY A N     
991  C  CA    . GLY A 125 ? 0.3505 0.2736 0.5092 -0.0067 0.0261  0.0181  125 GLY A CA    
992  C  C     . GLY A 125 ? 0.353  0.2742 0.5036 -0.0043 0.0262  0.0184  125 GLY A C     
993  O  O     . GLY A 125 ? 0.354  0.2708 0.4971 -0.0014 0.026   0.0202  125 GLY A O     
994  N  N     . ARG A 126 ? 0.3529 0.277  0.5046 -0.0053 0.0263  0.0168  126 ARG A N     
995  C  CA    . ARG A 126 ? 0.3619 0.2844 0.5065 -0.0032 0.026   0.0168  126 ARG A CA    
996  C  C     . ARG A 126 ? 0.3573 0.2717 0.4944 -0.002  0.0229  0.0175  126 ARG A C     
997  O  O     . ARG A 126 ? 0.3662 0.2763 0.4951 0.0012  0.0225  0.0186  126 ARG A O     
998  C  CB    . ARG A 126 ? 0.3949 0.3215 0.5427 -0.0052 0.0262  0.0148  126 ARG A CB    
999  C  CG    . ARG A 126 ? 0.4702 0.4034 0.6217 -0.0054 0.0287  0.0143  126 ARG A CG    
1000 C  CD    . ARG A 126 ? 0.5472 0.4842 0.7036 -0.0082 0.0287  0.012   126 ARG A CD    
1001 N  NE    . ARG A 126 ? 0.6142 0.5571 0.7764 -0.0092 0.0306  0.0113  126 ARG A NE    
1002 C  CZ    . ARG A 126 ? 0.6557 0.6022 0.823  -0.0115 0.0309  0.0092  126 ARG A CZ    
1003 N  NH1   . ARG A 126 ? 0.6523 0.6033 0.8242 -0.0123 0.0321  0.0086  126 ARG A NH1   
1004 N  NH2   . ARG A 126 ? 0.6574 0.6027 0.825  -0.013  0.0299  0.0078  126 ARG A NH2   
1005 N  N     . ALA A 127 ? 0.3409 0.253  0.4809 -0.0044 0.0205  0.0168  127 ALA A N     
1006 C  CA    . ALA A 127 ? 0.3371 0.2413 0.4708 -0.0038 0.0168  0.0176  127 ALA A CA    
1007 C  C     . ALA A 127 ? 0.3287 0.2268 0.457  -0.0015 0.0158  0.0193  127 ALA A C     
1008 O  O     . ALA A 127 ? 0.3368 0.2277 0.4562 0.0007  0.0133  0.0201  127 ALA A O     
1009 C  CB    . ALA A 127 ? 0.3398 0.2442 0.4797 -0.0071 0.0147  0.017   127 ALA A CB    
1010 N  N     . TYR A 128 ? 0.3135 0.2141 0.4467 -0.0021 0.0174  0.0198  128 TYR A N     
1011 C  CA    . TYR A 128 ? 0.3151 0.2099 0.443  0       0.0166  0.0216  128 TYR A CA    
1012 C  C     . TYR A 128 ? 0.3258 0.2193 0.4452 0.0041  0.0186  0.0228  128 TYR A C     
1013 O  O     . TYR A 128 ? 0.337  0.2227 0.4467 0.0069  0.0166  0.0238  128 TYR A O     
1014 C  CB    . TYR A 128 ? 0.3063 0.2044 0.442  -0.0018 0.0179  0.022   128 TYR A CB    
1015 C  CG    . TYR A 128 ? 0.3103 0.2042 0.4403 0.0008  0.0183  0.0242  128 TYR A CG    
1016 C  CD1   . TYR A 128 ? 0.3235 0.2082 0.446  0.0021  0.0149  0.0252  128 TYR A CD1   
1017 C  CD2   . TYR A 128 ? 0.3152 0.2139 0.4465 0.0021  0.0219  0.0254  128 TYR A CD2   
1018 C  CE1   . TYR A 128 ? 0.3396 0.22   0.4554 0.0048  0.0155  0.0273  128 TYR A CE1   
1019 C  CE2   . TYR A 128 ? 0.3312 0.2263 0.4567 0.0047  0.0227  0.0278  128 TYR A CE2   
1020 C  CZ    . TYR A 128 ? 0.3551 0.2409 0.4725 0.0061  0.0196  0.0286  128 TYR A CZ    
1021 O  OH    . TYR A 128 ? 0.3898 0.2717 0.5005 0.009   0.0205  0.0309  128 TYR A OH    
1022 N  N     . SER A 129 ? 0.3196 0.2205 0.4426 0.0045  0.0223  0.0228  129 SER A N     
1023 C  CA    . SER A 129 ? 0.323  0.2246 0.4401 0.0084  0.025   0.0242  129 SER A CA    
1024 C  C     . SER A 129 ? 0.3301 0.2272 0.438  0.0112  0.0237  0.0237  129 SER A C     
1025 O  O     . SER A 129 ? 0.3443 0.2359 0.4427 0.0152  0.0236  0.025   129 SER A O     
1026 C  CB    . SER A 129 ? 0.3331 0.2442 0.4581 0.0075  0.0287  0.0244  129 SER A CB    
1027 O  OG    . SER A 129 ? 0.3688 0.2814 0.49   0.011   0.0317  0.0266  129 SER A OG    
1028 N  N     . VAL A 130 ? 0.3172 0.2164 0.4275 0.0093  0.0226  0.022   130 VAL A N     
1029 C  CA    . VAL A 130 ? 0.3143 0.209  0.4161 0.0117  0.0209  0.0215  130 VAL A CA    
1030 C  C     . VAL A 130 ? 0.3115 0.1956 0.4051 0.0126  0.0163  0.0218  130 VAL A C     
1031 O  O     . VAL A 130 ? 0.3188 0.1964 0.4021 0.0163  0.0149  0.0222  130 VAL A O     
1032 C  CB    . VAL A 130 ? 0.3144 0.2142 0.4209 0.0094  0.0209  0.0199  130 VAL A CB    
1033 C  CG1   . VAL A 130 ? 0.3228 0.217  0.4205 0.0115  0.0184  0.0195  130 VAL A CG1   
1034 C  CG2   . VAL A 130 ? 0.3113 0.2202 0.4241 0.0091  0.0249  0.0198  130 VAL A CG2   
1035 N  N     . GLY A 131 ? 0.2957 0.178  0.3939 0.0094  0.0139  0.0216  131 GLY A N     
1036 C  CA    . GLY A 131 ? 0.2941 0.1666 0.386  0.0096  0.009   0.0221  131 GLY A CA    
1037 C  C     . GLY A 131 ? 0.2938 0.1583 0.3757 0.0135  0.0082  0.0235  131 GLY A C     
1038 O  O     . GLY A 131 ? 0.2949 0.1499 0.3674 0.0153  0.0042  0.0237  131 GLY A O     
1039 N  N     . ARG A 132 ? 0.2937 0.1617 0.3769 0.0149  0.0119  0.0245  132 ARG A N     
1040 C  CA    . ARG A 132 ? 0.3064 0.167  0.3795 0.019   0.0117  0.0261  132 ARG A CA    
1041 C  C     . ARG A 132 ? 0.3171 0.1754 0.3798 0.0244  0.0136  0.0265  132 ARG A C     
1042 O  O     . ARG A 132 ? 0.323  0.1752 0.3761 0.0284  0.0139  0.0278  132 ARG A O     
1043 C  CB    . ARG A 132 ? 0.3175 0.1819 0.3958 0.0183  0.0145  0.0275  132 ARG A CB    
1044 C  CG    . ARG A 132 ? 0.3383 0.213  0.4228 0.0188  0.0201  0.0282  132 ARG A CG    
1045 C  CD    . ARG A 132 ? 0.357  0.2354 0.4483 0.017   0.022   0.0297  132 ARG A CD    
1046 N  NE    . ARG A 132 ? 0.3838 0.2628 0.4698 0.021   0.0256  0.0321  132 ARG A NE    
1047 C  CZ    . ARG A 132 ? 0.4106 0.2816 0.4866 0.0242  0.0247  0.0336  132 ARG A CZ    
1048 N  NH1   . ARG A 132 ? 0.413  0.2744 0.4832 0.0238  0.0199  0.033   132 ARG A NH1   
1049 N  NH2   . ARG A 132 ? 0.4093 0.2818 0.4808 0.0279  0.0286  0.0361  132 ARG A NH2   
1050 N  N     . THR A 133 ? 0.3189 0.1816 0.3828 0.0247  0.0148  0.0255  133 THR A N     
1051 C  CA    . THR A 133 ? 0.3337 0.1946 0.3885 0.0298  0.0164  0.0257  133 THR A CA    
1052 C  C     . THR A 133 ? 0.3535 0.203  0.3962 0.0324  0.0116  0.0249  133 THR A C     
1053 O  O     . THR A 133 ? 0.3663 0.2114 0.3987 0.0377  0.0124  0.0253  133 THR A O     
1054 C  CB    . THR A 133 ? 0.3458 0.2163 0.4075 0.0289  0.0195  0.0249  133 THR A CB    
1055 O  OG1   . THR A 133 ? 0.355  0.2252 0.4199 0.0254  0.0161  0.0232  133 THR A OG1   
1056 C  CG2   . THR A 133 ? 0.3462 0.2276 0.4195 0.0265  0.0239  0.0257  133 THR A CG2   
1057 N  N     . GLY A 134 ? 0.3568 0.202  0.4011 0.0289  0.0066  0.024   134 GLY A N     
1058 C  CA    . GLY A 134 ? 0.369  0.2036 0.403  0.0306  0.0013  0.0233  134 GLY A CA    
1059 C  C     . GLY A 134 ? 0.3733 0.2114 0.4102 0.029   0.0005  0.0221  134 GLY A C     
1060 O  O     . GLY A 134 ? 0.3828 0.2129 0.4133 0.0293  -0.0045 0.0216  134 GLY A O     
1061 N  N     . TYR A 135 ? 0.3638 0.2136 0.4105 0.0272  0.005   0.0217  135 TYR A N     
1062 C  CA    . TYR A 135 ? 0.3626 0.2169 0.4133 0.0252  0.0048  0.0206  135 TYR A CA    
1063 C  C     . TYR A 135 ? 0.3641 0.2221 0.425  0.0192  0.0029  0.0202  135 TYR A C     
1064 O  O     . TYR A 135 ? 0.357  0.2209 0.4267 0.0164  0.0052  0.0204  135 TYR A O     
1065 C  CB    . TYR A 135 ? 0.3529 0.2175 0.4088 0.0263  0.0103  0.0205  135 TYR A CB    
1066 C  CG    . TYR A 135 ? 0.3682 0.2308 0.4154 0.0324  0.0128  0.0212  135 TYR A CG    
1067 C  CD1   . TYR A 135 ? 0.3874 0.2417 0.4231 0.0365  0.0101  0.0208  135 TYR A CD1   
1068 C  CD2   . TYR A 135 ? 0.3772 0.2466 0.428  0.0342  0.018   0.0225  135 TYR A CD2   
1069 C  CE1   . TYR A 135 ? 0.4005 0.2532 0.4281 0.0427  0.0127  0.0214  135 TYR A CE1   
1070 C  CE2   . TYR A 135 ? 0.3902 0.2588 0.4336 0.0401  0.0209  0.0235  135 TYR A CE2   
1071 C  CZ    . TYR A 135 ? 0.4092 0.2694 0.4408 0.0445  0.0184  0.0229  135 TYR A CZ    
1072 O  OH    . TYR A 135 ? 0.4319 0.2913 0.4561 0.0508  0.0215  0.0238  135 TYR A OH    
1073 N  N     . PRO A 136 ? 0.3689 0.2233 0.4287 0.0172  -0.0012 0.0198  136 PRO A N     
1074 C  CA    . PRO A 136 ? 0.366  0.2241 0.4354 0.0117  -0.0027 0.0197  136 PRO A CA    
1075 C  C     . PRO A 136 ? 0.3613 0.2312 0.4421 0.0087  0.0019  0.0189  136 PRO A C     
1076 O  O     . PRO A 136 ? 0.3578 0.2333 0.4394 0.01    0.0052  0.0183  136 PRO A O     
1077 C  CB    . PRO A 136 ? 0.3777 0.2308 0.4431 0.0107  -0.0073 0.0197  136 PRO A CB    
1078 C  CG    . PRO A 136 ? 0.3919 0.2348 0.4439 0.0157  -0.01   0.0199  136 PRO A CG    
1079 C  CD    . PRO A 136 ? 0.3705 0.2171 0.4201 0.0199  -0.0049 0.0196  136 PRO A CD    
1080 N  N     . TYR A 137 ? 0.3618 0.2352 0.4514 0.0048  0.0019  0.019   137 TYR A N     
1081 C  CA    . TYR A 137 ? 0.366  0.2497 0.4663 0.0019  0.0058  0.018   137 TYR A CA    
1082 C  C     . TYR A 137 ? 0.3781 0.2638 0.4847 -0.0023 0.0038  0.0179  137 TYR A C     
1083 O  O     . TYR A 137 ? 0.3838 0.2662 0.4928 -0.0041 0.0011  0.0188  137 TYR A O     
1084 C  CB    . TYR A 137 ? 0.3603 0.2472 0.4659 0.0017  0.0085  0.0182  137 TYR A CB    
1085 C  CG    . TYR A 137 ? 0.3634 0.2602 0.4794 -0.0009 0.0122  0.0171  137 TYR A CG    
1086 C  CD1   . TYR A 137 ? 0.3692 0.2719 0.4865 0.0004  0.0159  0.0166  137 TYR A CD1   
1087 C  CD2   . TYR A 137 ? 0.3789 0.2788 0.5032 -0.0046 0.0119  0.0166  137 TYR A CD2   
1088 C  CE1   . TYR A 137 ? 0.3774 0.2883 0.5037 -0.002  0.0188  0.0155  137 TYR A CE1   
1089 C  CE2   . TYR A 137 ? 0.3867 0.2947 0.5196 -0.0066 0.0151  0.0153  137 TYR A CE2   
1090 C  CZ    . TYR A 137 ? 0.3934 0.3065 0.527  -0.0054 0.0183  0.0147  137 TYR A CZ    
1091 O  OH    . TYR A 137 ? 0.4133 0.3336 0.555  -0.0075 0.0209  0.0134  137 TYR A OH    
1092 N  N     . ILE A 138 ? 0.3758 0.2667 0.485  -0.0037 0.0051  0.0171  138 ILE A N     
1093 C  CA    . ILE A 138 ? 0.3738 0.2671 0.4886 -0.0074 0.0038  0.0173  138 ILE A CA    
1094 C  C     . ILE A 138 ? 0.3684 0.2712 0.4925 -0.0097 0.008   0.0159  138 ILE A C     
1095 O  O     . ILE A 138 ? 0.367  0.2746 0.4913 -0.009  0.0108  0.0147  138 ILE A O     
1096 C  CB    . ILE A 138 ? 0.381  0.2717 0.4905 -0.0074 0.0013  0.0176  138 ILE A CB    
1097 C  CG1   . ILE A 138 ? 0.3999 0.2806 0.4983 -0.0041 -0.0026 0.0185  138 ILE A CG1   
1098 C  CG2   . ILE A 138 ? 0.3837 0.2761 0.4987 -0.0113 -0.0005 0.0185  138 ILE A CG2   
1099 C  CD1   . ILE A 138 ? 0.421  0.294  0.517  -0.0044 -0.0068 0.0199  138 ILE A CD1   
1100 N  N     . TYR A 139 ? 0.362  0.2673 0.4937 -0.0122 0.0083  0.016   139 TYR A N     
1101 C  CA    . TYR A 139 ? 0.3594 0.2729 0.4996 -0.0141 0.0119  0.0145  139 TYR A CA    
1102 C  C     . TYR A 139 ? 0.3553 0.2716 0.4992 -0.017  0.0114  0.0148  139 TYR A C     
1103 O  O     . TYR A 139 ? 0.3544 0.2687 0.5012 -0.0186 0.0092  0.0161  139 TYR A O     
1104 C  CB    . TYR A 139 ? 0.3628 0.277  0.5088 -0.0147 0.0126  0.0145  139 TYR A CB    
1105 C  CG    . TYR A 139 ? 0.3766 0.2983 0.5306 -0.0161 0.0163  0.0127  139 TYR A CG    
1106 C  CD1   . TYR A 139 ? 0.3927 0.3193 0.5469 -0.0157 0.0191  0.0112  139 TYR A CD1   
1107 C  CD2   . TYR A 139 ? 0.3906 0.314  0.5518 -0.0176 0.0166  0.0125  139 TYR A CD2   
1108 C  CE1   . TYR A 139 ? 0.4025 0.335  0.5633 -0.0168 0.022   0.0094  139 TYR A CE1   
1109 C  CE2   . TYR A 139 ? 0.4015 0.3309 0.5695 -0.0185 0.0197  0.0107  139 TYR A CE2   
1110 C  CZ    . TYR A 139 ? 0.4132 0.347  0.5807 -0.0182 0.0222  0.0091  139 TYR A CZ    
1111 O  OH    . TYR A 139 ? 0.4324 0.3713 0.606  -0.019  0.0248  0.0072  139 TYR A OH    
1112 N  N     . ILE A 140 ? 0.3525 0.2731 0.4961 -0.0174 0.0133  0.0137  140 ILE A N     
1113 C  CA    . ILE A 140 ? 0.3586 0.2821 0.505  -0.0199 0.0131  0.0142  140 ILE A CA    
1114 C  C     . ILE A 140 ? 0.3666 0.2974 0.5203 -0.0215 0.0168  0.0125  140 ILE A C     
1115 O  O     . ILE A 140 ? 0.3634 0.2979 0.5171 -0.0208 0.0195  0.0107  140 ILE A O     
1116 C  CB    . ILE A 140 ? 0.3664 0.2887 0.5062 -0.0193 0.0121  0.0143  140 ILE A CB    
1117 C  CG1   . ILE A 140 ? 0.3824 0.2964 0.5142 -0.0174 0.0081  0.0158  140 ILE A CG1   
1118 C  CG2   . ILE A 140 ? 0.3706 0.2962 0.513  -0.022  0.0123  0.015   140 ILE A CG2   
1119 C  CD1   . ILE A 140 ? 0.4011 0.3132 0.526  -0.0162 0.0071  0.0158  140 ILE A CD1   
1120 N  N     . VAL A 141 ? 0.3773 0.3102 0.5375 -0.0234 0.017   0.0133  141 VAL A N     
1121 C  CA    . VAL A 141 ? 0.3918 0.3313 0.559  -0.0244 0.0206  0.0115  141 VAL A CA    
1122 C  C     . VAL A 141 ? 0.412  0.3554 0.5821 -0.0265 0.0215  0.0124  141 VAL A C     
1123 O  O     . VAL A 141 ? 0.4115 0.3527 0.5817 -0.0277 0.0189  0.0149  141 VAL A O     
1124 C  CB    . VAL A 141 ? 0.3972 0.3372 0.5706 -0.0243 0.0213  0.011   141 VAL A CB    
1125 C  CG1   . VAL A 141 ? 0.4076 0.3426 0.5777 -0.0225 0.0195  0.0113  141 VAL A CG1   
1126 C  CG2   . VAL A 141 ? 0.4023 0.3428 0.5817 -0.026  0.0202  0.0128  141 VAL A CG2   
1127 N  N     . ASP A 142 ? 0.4283 0.3772 0.6007 -0.0267 0.025   0.0104  142 ASP A N     
1128 C  CA    . ASP A 142 ? 0.4525 0.4056 0.6274 -0.0284 0.0266  0.0111  142 ASP A CA    
1129 C  C     . ASP A 142 ? 0.461  0.4173 0.6442 -0.0291 0.028   0.0115  142 ASP A C     
1130 O  O     . ASP A 142 ? 0.467  0.4251 0.6539 -0.0282 0.03    0.0093  142 ASP A O     
1131 C  CB    . ASP A 142 ? 0.4894 0.4464 0.6621 -0.028  0.0297  0.0086  142 ASP A CB    
1132 C  CG    . ASP A 142 ? 0.5878 0.5439 0.754  -0.0285 0.0287  0.0094  142 ASP A CG    
1133 O  OD1   . ASP A 142 ? 0.6065 0.5579 0.7682 -0.0283 0.0254  0.011   142 ASP A OD1   
1134 O  OD2   . ASP A 142 ? 0.6299 0.5896 0.7951 -0.0289 0.031   0.0082  142 ASP A OD2   
1135 N  N     . PHE A 143 ? 0.4578 0.4147 0.6442 -0.0307 0.0268  0.0144  143 PHE A N     
1136 C  CA    . PHE A 143 ? 0.4605 0.4209 0.6555 -0.0314 0.0281  0.0154  143 PHE A CA    
1137 C  C     . PHE A 143 ? 0.4698 0.4358 0.6671 -0.0326 0.0308  0.0165  143 PHE A C     
1138 O  O     . PHE A 143 ? 0.4721 0.4372 0.6677 -0.0341 0.0287  0.0195  143 PHE A O     
1139 C  CB    . PHE A 143 ? 0.4581 0.4141 0.6555 -0.0324 0.0238  0.0186  143 PHE A CB    
1140 C  CG    . PHE A 143 ? 0.4607 0.4198 0.6677 -0.0331 0.0244  0.02    143 PHE A CG    
1141 C  CD1   . PHE A 143 ? 0.4633 0.4267 0.6758 -0.0348 0.0251  0.0229  143 PHE A CD1   
1142 C  CD2   . PHE A 143 ? 0.4686 0.4265 0.6794 -0.032  0.0244  0.0187  143 PHE A CD2   
1143 C  CE1   . PHE A 143 ? 0.4639 0.4309 0.686  -0.0352 0.026   0.0244  143 PHE A CE1   
1144 C  CE2   . PHE A 143 ? 0.4717 0.4326 0.6917 -0.0325 0.0248  0.02    143 PHE A CE2   
1145 C  CZ    . PHE A 143 ? 0.4623 0.4277 0.688  -0.034  0.0257  0.0228  143 PHE A CZ    
1146 N  N     . VAL A 144 ? 0.4727 0.4442 0.6734 -0.0318 0.0352  0.0144  144 VAL A N     
1147 C  CA    . VAL A 144 ? 0.4835 0.4559 0.686  -0.0299 0.0375  0.0107  144 VAL A CA    
1148 C  C     . VAL A 144 ? 0.503  0.4777 0.7007 -0.0289 0.0406  0.0076  144 VAL A C     
1149 O  O     . VAL A 144 ? 0.5071 0.4838 0.7014 -0.0296 0.0417  0.0083  144 VAL A O     
1150 C  CB    . VAL A 144 ? 0.4812 0.4576 0.6928 -0.0296 0.0397  0.0109  144 VAL A CB    
1151 C  CG1   . VAL A 144 ? 0.483  0.4566 0.6998 -0.0303 0.0364  0.0134  144 VAL A CG1   
1152 C  CG2   . VAL A 144 ? 0.4836 0.466  0.6983 -0.0301 0.0429  0.0125  144 VAL A CG2   
1153 N  N     . LYS A 145 ? 0.5151 0.4893 0.7126 -0.0274 0.0417  0.0041  145 LYS A N     
1154 C  CA    . LYS A 145 ? 0.5381 0.5139 0.7316 -0.0264 0.0442  0.0009  145 LYS A CA    
1155 C  C     . LYS A 145 ? 0.5549 0.5326 0.7534 -0.025  0.0466  -0.0017 145 LYS A C     
1156 O  O     . LYS A 145 ? 0.5572 0.5329 0.759  -0.0245 0.0452  -0.0024 145 LYS A O     
1157 C  CB    . LYS A 145 ? 0.5696 0.5418 0.7571 -0.0261 0.0423  -0.0005 145 LYS A CB    
1158 C  CG    . LYS A 145 ? 0.6308 0.6032 0.8113 -0.0265 0.0424  -0.0008 145 LYS A CG    
1159 C  CD    . LYS A 145 ? 0.6861 0.6576 0.8627 -0.0255 0.0428  -0.004  145 LYS A CD    
1160 C  CE    . LYS A 145 ? 0.7265 0.6954 0.9043 -0.0247 0.0411  -0.005  145 LYS A CE    
1161 N  NZ    . LYS A 145 ? 0.752  0.722  0.9342 -0.0238 0.0427  -0.0077 145 LYS A NZ    
1162 N  N     . TYR A 146 ? 0.5634 0.545  0.7624 -0.0241 0.0501  -0.0032 146 TYR A N     
1163 C  CA    . TYR A 146 ? 0.576  0.5591 0.7793 -0.0224 0.0524  -0.006  146 TYR A CA    
1164 C  C     . TYR A 146 ? 0.5945 0.5749 0.7942 -0.0213 0.0519  -0.0097 146 TYR A C     
1165 O  O     . TYR A 146 ? 0.5999 0.5793 0.7931 -0.0215 0.0516  -0.0108 146 TYR A O     
1166 C  CB    . TYR A 146 ? 0.5746 0.5623 0.7785 -0.0214 0.0565  -0.0064 146 TYR A CB    
1167 C  CG    . TYR A 146 ? 0.5799 0.5714 0.7899 -0.0221 0.0576  -0.0027 146 TYR A CG    
1168 C  CD1   . TYR A 146 ? 0.5914 0.5843 0.7995 -0.024  0.0571  0.0009  146 TYR A CD1   
1169 C  CD2   . TYR A 146 ? 0.5882 0.5821 0.8064 -0.021  0.059   -0.0025 146 TYR A CD2   
1170 C  CE1   . TYR A 146 ? 0.6011 0.5976 0.8156 -0.025  0.0577  0.0048  146 TYR A CE1   
1171 C  CE2   . TYR A 146 ? 0.5969 0.5948 0.8216 -0.0218 0.0599  0.0014  146 TYR A CE2   
1172 C  CZ    . TYR A 146 ? 0.6104 0.6096 0.8334 -0.0239 0.0592  0.0051  146 TYR A CZ    
1173 O  OH    . TYR A 146 ? 0.6257 0.6289 0.8557 -0.025  0.0597  0.0094  146 TYR A OH    
1174 N  N     . GLU A 147 ? 0.6028 0.5821 0.807  -0.0203 0.0516  -0.0115 147 GLU A N     
1175 C  CA    . GLU A 147 ? 0.6178 0.5947 0.8196 -0.0194 0.051   -0.0149 147 GLU A CA    
1176 C  C     . GLU A 147 ? 0.6229 0.6017 0.8226 -0.0177 0.0541  -0.0179 147 GLU A C     
1177 O  O     . GLU A 147 ? 0.6224 0.6044 0.8253 -0.0167 0.0569  -0.0175 147 GLU A O     
1178 C  CB    . GLU A 147 ? 0.6539 0.629  0.8616 -0.0189 0.0495  -0.0156 147 GLU A CB    
1179 C  CG    . GLU A 147 ? 0.7257 0.6979 0.9336 -0.0202 0.0462  -0.0133 147 GLU A CG    
1180 C  CD    . GLU A 147 ? 0.8063 0.7773 1.0207 -0.0202 0.0449  -0.0122 147 GLU A CD    
1181 O  OE1   . GLU A 147 ? 0.8236 0.7919 1.0375 -0.0211 0.0423  -0.0102 147 GLU A OE1   
1182 O  OE2   . GLU A 147 ? 0.827  0.7996 1.0467 -0.0192 0.0463  -0.0132 147 GLU A OE2   
1183 N  N     . LEU A 148 ? 0.6269 0.6037 0.8208 -0.0173 0.0536  -0.0206 148 LEU A N     
1184 C  CA    . LEU A 148 ? 0.637  0.6146 0.8273 -0.0155 0.0563  -0.0236 148 LEU A CA    
1185 C  C     . LEU A 148 ? 0.6475 0.622  0.8378 -0.0139 0.0554  -0.0275 148 LEU A C     
1186 O  O     . LEU A 148 ? 0.6537 0.6253 0.8449 -0.0148 0.0523  -0.0279 148 LEU A O     
1187 C  CB    . LEU A 148 ? 0.6417 0.619  0.8239 -0.0162 0.0563  -0.0237 148 LEU A CB    
1188 C  CG    . LEU A 148 ? 0.6613 0.6408 0.842  -0.0178 0.0567  -0.02   148 LEU A CG    
1189 C  CD1   . LEU A 148 ? 0.6727 0.6511 0.8453 -0.0185 0.0561  -0.0204 148 LEU A CD1   
1190 C  CD2   . LEU A 148 ? 0.6669 0.6507 0.8507 -0.0171 0.0602  -0.0183 148 LEU A CD2   
1191 N  N     . ASN A 149 ? 0.6463 0.6212 0.8351 -0.0116 0.058   -0.0303 149 ASN A N     
1192 C  CA    . ASN A 149 ? 0.6544 0.6255 0.8415 -0.01   0.0569  -0.0344 149 ASN A CA    
1193 C  C     . ASN A 149 ? 0.6577 0.6267 0.8362 -0.0105 0.0559  -0.0357 149 ASN A C     
1194 O  O     . ASN A 149 ? 0.6575 0.628  0.8307 -0.0096 0.0585  -0.036  149 ASN A O     
1195 C  CB    . ASN A 149 ? 0.6725 0.6448 0.8604 -0.0068 0.0604  -0.0368 149 ASN A CB    
1196 C  CG    . ASN A 149 ? 0.7161 0.6908 0.9131 -0.0062 0.0614  -0.0353 149 ASN A CG    
1197 O  OD1   . ASN A 149 ? 0.7259 0.7051 0.9264 -0.0063 0.064   -0.0325 149 ASN A OD1   
1198 N  ND2   . ASN A 149 ? 0.7298 0.7014 0.9309 -0.0057 0.059   -0.037  149 ASN A ND2   
1199 N  N     . ASN A 150 ? 0.6593 0.6252 0.8365 -0.0121 0.0521  -0.0359 150 ASN A N     
1200 C  CA    . ASN A 150 ? 0.6686 0.6326 0.8384 -0.013  0.0505  -0.0367 150 ASN A CA    
1201 C  C     . ASN A 150 ? 0.6721 0.6332 0.835  -0.0109 0.0512  -0.0406 150 ASN A C     
1202 O  O     . ASN A 150 ? 0.675  0.6347 0.8309 -0.0114 0.0504  -0.0412 150 ASN A O     
1203 C  CB    . ASN A 150 ? 0.6845 0.6463 0.8557 -0.0149 0.0463  -0.0358 150 ASN A CB    
1204 C  CG    . ASN A 150 ? 0.724  0.688  0.8993 -0.0167 0.0457  -0.0318 150 ASN A CG    
1205 O  OD1   . ASN A 150 ? 0.7384 0.7048 0.9118 -0.0175 0.0469  -0.0294 150 ASN A OD1   
1206 N  ND2   . ASN A 150 ? 0.7305 0.6936 0.9112 -0.0174 0.0435  -0.031  150 ASN A ND2   
1207 N  N     . SER A 151 ? 0.6694 0.6293 0.8337 -0.0084 0.0526  -0.0434 151 SER A N     
1208 C  CA    . SER A 151 ? 0.6751 0.6316 0.8324 -0.0059 0.0534  -0.0474 151 SER A CA    
1209 C  C     . SER A 151 ? 0.6726 0.632  0.8239 -0.0047 0.0577  -0.047  151 SER A C     
1210 O  O     . SER A 151 ? 0.6781 0.6349 0.8208 -0.0041 0.0575  -0.0488 151 SER A O     
1211 C  CB    . SER A 151 ? 0.6946 0.6491 0.8554 -0.0032 0.054   -0.0503 151 SER A CB    
1212 O  OG    . SER A 151 ? 0.7236 0.6764 0.8913 -0.0045 0.0504  -0.05   151 SER A OG    
1213 N  N     . ASP A 152 ? 0.6624 0.6273 0.8185 -0.0045 0.0614  -0.0441 152 ASP A N     
1214 C  CA    . ASP A 152 ? 0.6629 0.6313 0.8144 -0.0034 0.0658  -0.0431 152 ASP A CA    
1215 C  C     . ASP A 152 ? 0.6519 0.6257 0.807  -0.0059 0.067   -0.0381 152 ASP A C     
1216 O  O     . ASP A 152 ? 0.6549 0.6327 0.8087 -0.0051 0.071   -0.0364 152 ASP A O     
1217 C  CB    . ASP A 152 ? 0.6853 0.6554 0.838  0.0004  0.0701  -0.045  152 ASP A CB    
1218 C  CG    . ASP A 152 ? 0.7388 0.713  0.9023 0.0006  0.0716  -0.0428 152 ASP A CG    
1219 O  OD1   . ASP A 152 ? 0.7423 0.7161 0.912  -0.0018 0.0684  -0.0411 152 ASP A OD1   
1220 O  OD2   . ASP A 152 ? 0.7718 0.7497 0.9374 0.0031  0.0761  -0.0426 152 ASP A OD2   
1221 N  N     . ARG A 153 ? 0.6356 0.6093 0.7952 -0.0087 0.0637  -0.0356 153 ARG A N     
1222 C  CA    . ARG A 153 ? 0.6232 0.6007 0.7861 -0.0111 0.0639  -0.031  153 ARG A CA    
1223 C  C     . ARG A 153 ? 0.6063 0.5888 0.7759 -0.0104 0.0674  -0.0285 153 ARG A C     
1224 O  O     . ARG A 153 ? 0.6069 0.5927 0.7775 -0.012  0.0683  -0.0247 153 ARG A O     
1225 C  CB    . ARG A 153 ? 0.6377 0.6154 0.7931 -0.0125 0.0639  -0.0296 153 ARG A CB    
1226 C  CG    . ARG A 153 ? 0.6681 0.6415 0.8185 -0.0138 0.0599  -0.031  153 ARG A CG    
1227 C  CD    . ARG A 153 ? 0.6954 0.6696 0.8413 -0.0159 0.059   -0.0283 153 ARG A CD    
1228 N  NE    . ARG A 153 ? 0.7158 0.6887 0.8643 -0.0179 0.0552  -0.0265 153 ARG A NE    
1229 C  CZ    . ARG A 153 ? 0.7258 0.7006 0.8777 -0.0195 0.0546  -0.0229 153 ARG A CZ    
1230 N  NH1   . ARG A 153 ? 0.7074 0.6857 0.8611 -0.0197 0.0572  -0.0203 153 ARG A NH1   
1231 N  NH2   . ARG A 153 ? 0.7284 0.7017 0.8819 -0.0208 0.0514  -0.0216 153 ARG A NH2   
1232 N  N     . SER A 154 ? 0.5885 0.5715 0.7628 -0.0081 0.0691  -0.0303 154 SER A N     
1233 C  CA    . SER A 154 ? 0.5761 0.5642 0.758  -0.0074 0.0722  -0.0278 154 SER A CA    
1234 C  C     . SER A 154 ? 0.5644 0.5527 0.7543 -0.0096 0.0693  -0.0248 154 SER A C     
1235 O  O     . SER A 154 ? 0.5699 0.5543 0.7607 -0.0104 0.0657  -0.0261 154 SER A O     
1236 C  CB    . SER A 154 ? 0.5898 0.5781 0.7738 -0.0037 0.0751  -0.0309 154 SER A CB    
1237 O  OG    . SER A 154 ? 0.6209 0.6051 0.808  -0.0032 0.072   -0.0335 154 SER A OG    
1238 N  N     . ARG A 155 ? 0.548  0.5406 0.7435 -0.0107 0.0705  -0.0207 155 ARG A N     
1239 C  CA    . ARG A 155 ? 0.5382 0.5305 0.7404 -0.0128 0.0675  -0.0177 155 ARG A CA    
1240 C  C     . ARG A 155 ? 0.5326 0.5248 0.7429 -0.0116 0.0672  -0.0185 155 ARG A C     
1241 O  O     . ARG A 155 ? 0.5338 0.5292 0.7483 -0.0094 0.0705  -0.019  155 ARG A O     
1242 C  CB    . ARG A 155 ? 0.5412 0.5376 0.7462 -0.0147 0.0682  -0.0128 155 ARG A CB    
1243 C  CG    . ARG A 155 ? 0.5637 0.5596 0.7613 -0.0165 0.0675  -0.0115 155 ARG A CG    
1244 C  CD    . ARG A 155 ? 0.5806 0.5804 0.7813 -0.0183 0.0682  -0.0066 155 ARG A CD    
1245 N  NE    . ARG A 155 ? 0.602  0.6007 0.7953 -0.0201 0.067   -0.0052 155 ARG A NE    
1246 C  CZ    . ARG A 155 ? 0.6268 0.6275 0.8143 -0.0197 0.0698  -0.0054 155 ARG A CZ    
1247 N  NH1   . ARG A 155 ? 0.6169 0.6209 0.8047 -0.0172 0.0743  -0.007  155 ARG A NH1   
1248 N  NH2   . ARG A 155 ? 0.6369 0.6361 0.818  -0.0215 0.0682  -0.0041 155 ARG A NH2   
1249 N  N     . LYS A 156 ? 0.5231 0.512  0.7361 -0.013  0.0633  -0.018  156 LYS A N     
1250 C  CA    . LYS A 156 ? 0.5183 0.5065 0.739  -0.0124 0.0622  -0.0182 156 LYS A CA    
1251 C  C     . LYS A 156 ? 0.5089 0.4996 0.7363 -0.0141 0.0614  -0.0136 156 LYS A C     
1252 O  O     . LYS A 156 ? 0.5133 0.5045 0.7383 -0.0162 0.0604  -0.0105 156 LYS A O     
1253 C  CB    . LYS A 156 ? 0.5415 0.5245 0.761  -0.0133 0.0583  -0.0197 156 LYS A CB    
1254 C  CG    . LYS A 156 ? 0.5868 0.5668 0.8003 -0.0121 0.058   -0.0239 156 LYS A CG    
1255 C  CD    . LYS A 156 ? 0.6399 0.6156 0.8538 -0.0131 0.0542  -0.0246 156 LYS A CD    
1256 C  CE    . LYS A 156 ? 0.6942 0.6668 0.9035 -0.012  0.0535  -0.0286 156 LYS A CE    
1257 N  NZ    . LYS A 156 ? 0.7242 0.6931 0.9357 -0.0128 0.05    -0.0292 156 LYS A NZ    
1258 N  N     . ASN A 157 ? 0.4927 0.4844 0.7284 -0.0133 0.0614  -0.013  157 ASN A N     
1259 C  CA    . ASN A 157 ? 0.4793 0.4729 0.7217 -0.0149 0.0602  -0.0086 157 ASN A CA    
1260 C  C     . ASN A 157 ? 0.4657 0.4551 0.7059 -0.0176 0.0557  -0.0065 157 ASN A C     
1261 O  O     . ASN A 157 ? 0.4682 0.4532 0.7046 -0.0177 0.0534  -0.0084 157 ASN A O     
1262 C  CB    . ASN A 157 ? 0.4895 0.4844 0.7411 -0.0135 0.0605  -0.0087 157 ASN A CB    
1263 C  CG    . ASN A 157 ? 0.5303 0.5312 0.7866 -0.0113 0.0652  -0.0084 157 ASN A CG    
1264 O  OD1   . ASN A 157 ? 0.5413 0.5467 0.7986 -0.0121 0.0671  -0.0052 157 ASN A OD1   
1265 N  ND2   . ASN A 157 ? 0.5438 0.5451 0.8031 -0.0083 0.0671  -0.0116 157 ASN A ND2   
1266 N  N     . LEU A 158 ? 0.4486 0.4392 0.6906 -0.0195 0.0544  -0.0023 158 LEU A N     
1267 C  CA    . LEU A 158 ? 0.4367 0.4229 0.676  -0.0217 0.0501  0       158 LEU A CA    
1268 C  C     . LEU A 158 ? 0.4241 0.4063 0.6669 -0.0217 0.0471  -0.0003 158 LEU A C     
1269 O  O     . LEU A 158 ? 0.4232 0.4067 0.6736 -0.0209 0.0473  -0.0001 158 LEU A O     
1270 C  CB    . LEU A 158 ? 0.4322 0.42   0.6737 -0.0237 0.0488  0.0046  158 LEU A CB    
1271 C  CG    . LEU A 158 ? 0.4497 0.4393 0.6854 -0.0246 0.0501  0.0059  158 LEU A CG    
1272 C  CD1   . LEU A 158 ? 0.4539 0.4443 0.6927 -0.0268 0.048   0.0108  158 LEU A CD1   
1273 C  CD2   . LEU A 158 ? 0.4671 0.4523 0.6934 -0.025  0.0483  0.0042  158 LEU A CD2   
1274 N  N     . ARG A 159 ? 0.4097 0.3871 0.6469 -0.0223 0.0443  -0.0008 159 ARG A N     
1275 C  CA    . ARG A 159 ? 0.3989 0.3722 0.6382 -0.0224 0.0413  -0.0008 159 ARG A CA    
1276 C  C     . ARG A 159 ? 0.3771 0.3463 0.6131 -0.0241 0.0376  0.0024  159 ARG A C     
1277 O  O     . ARG A 159 ? 0.3789 0.3472 0.6085 -0.0247 0.0371  0.0031  159 ARG A O     
1278 C  CB    . ARG A 159 ? 0.4259 0.397  0.6616 -0.0214 0.0415  -0.0043 159 ARG A CB    
1279 C  CG    . ARG A 159 ? 0.477  0.4502 0.7171 -0.0196 0.0439  -0.0074 159 ARG A CG    
1280 C  CD    . ARG A 159 ? 0.5315 0.5013 0.7732 -0.0191 0.0421  -0.0092 159 ARG A CD    
1281 N  NE    . ARG A 159 ? 0.5776 0.5438 0.8206 -0.0203 0.0387  -0.0066 159 ARG A NE    
1282 C  CZ    . ARG A 159 ? 0.6091 0.5724 0.8551 -0.0201 0.0369  -0.0071 159 ARG A CZ    
1283 N  NH1   . ARG A 159 ? 0.6073 0.5671 0.8533 -0.0211 0.0339  -0.0046 159 ARG A NH1   
1284 N  NH2   . ARG A 159 ? 0.608  0.5716 0.8567 -0.0189 0.0378  -0.0101 159 ARG A NH2   
1285 N  N     . PHE A 160 ? 0.3553 0.3219 0.5958 -0.0246 0.0349  0.0044  160 PHE A N     
1286 C  CA    . PHE A 160 ? 0.3426 0.3045 0.5797 -0.0259 0.031   0.0074  160 PHE A CA    
1287 C  C     . PHE A 160 ? 0.332  0.2887 0.5676 -0.0255 0.0283  0.0071  160 PHE A C     
1288 O  O     . PHE A 160 ? 0.3292 0.2859 0.5698 -0.0249 0.0285  0.0059  160 PHE A O     
1289 C  CB    . PHE A 160 ? 0.3357 0.2985 0.5788 -0.0271 0.0293  0.0109  160 PHE A CB    
1290 C  CG    . PHE A 160 ? 0.3388 0.3069 0.5835 -0.0277 0.0318  0.0121  160 PHE A CG    
1291 C  CD1   . PHE A 160 ? 0.3487 0.3161 0.5873 -0.0288 0.0309  0.0136  160 PHE A CD1   
1292 C  CD2   . PHE A 160 ? 0.3458 0.3199 0.5982 -0.027  0.0351  0.0117  160 PHE A CD2   
1293 C  CE1   . PHE A 160 ? 0.3566 0.329  0.5968 -0.0295 0.0333  0.015   160 PHE A CE1   
1294 C  CE2   . PHE A 160 ? 0.3552 0.3347 0.6091 -0.0274 0.0377  0.0132  160 PHE A CE2   
1295 C  CZ    . PHE A 160 ? 0.3531 0.3317 0.6008 -0.0288 0.0368  0.0149  160 PHE A CZ    
1296 N  N     . PRO A 161 ? 0.3274 0.2792 0.5559 -0.0259 0.0257  0.0084  161 PRO A N     
1297 C  CA    . PRO A 161 ? 0.3294 0.2761 0.556  -0.0254 0.0233  0.0086  161 PRO A CA    
1298 C  C     . PRO A 161 ? 0.3277 0.2713 0.5592 -0.0261 0.0201  0.0109  161 PRO A C     
1299 O  O     . PRO A 161 ? 0.3303 0.2749 0.5654 -0.0271 0.019   0.0131  161 PRO A O     
1300 C  CB    . PRO A 161 ? 0.3426 0.2852 0.5599 -0.0252 0.0216  0.0097  161 PRO A CB    
1301 C  CG    . PRO A 161 ? 0.3469 0.2908 0.563  -0.0262 0.0212  0.0113  161 PRO A CG    
1302 C  CD    . PRO A 161 ? 0.3222 0.2728 0.5439 -0.0264 0.0248  0.0098  161 PRO A CD    
1303 N  N     . ASN A 162 ? 0.3254 0.2653 0.5571 -0.0256 0.0185  0.0108  162 ASN A N     
1304 C  CA    . ASN A 162 ? 0.3296 0.2655 0.5648 -0.0262 0.015   0.013   162 ASN A CA    
1305 C  C     . ASN A 162 ? 0.3271 0.2576 0.5562 -0.0268 0.0112  0.0159  162 ASN A C     
1306 O  O     . ASN A 162 ? 0.3282 0.256  0.5488 -0.0262 0.011   0.0158  162 ASN A O     
1307 C  CB    . ASN A 162 ? 0.3559 0.2882 0.5903 -0.0254 0.014   0.0123  162 ASN A CB    
1308 C  CG    . ASN A 162 ? 0.4197 0.3477 0.6578 -0.026  0.0104  0.0143  162 ASN A CG    
1309 O  OD1   . ASN A 162 ? 0.4387 0.3613 0.6731 -0.0265 0.0067  0.0168  162 ASN A OD1   
1310 N  ND2   . ASN A 162 ? 0.4405 0.3701 0.6858 -0.0258 0.0109  0.0132  162 ASN A ND2   
1311 N  N     . PRO A 163 ? 0.3192 0.248  0.5526 -0.0281 0.0081  0.0185  163 PRO A N     
1312 C  CA    . PRO A 163 ? 0.318  0.2409 0.5454 -0.0287 0.0039  0.0212  163 PRO A CA    
1313 C  C     . PRO A 163 ? 0.3209 0.2359 0.5385 -0.0275 0.0014  0.0214  163 PRO A C     
1314 O  O     . PRO A 163 ? 0.3306 0.2407 0.5404 -0.0273 -0.0011 0.0228  163 PRO A O     
1315 C  CB    . PRO A 163 ? 0.3257 0.2476 0.5609 -0.0303 0.0005  0.024   163 PRO A CB    
1316 C  CG    . PRO A 163 ? 0.3287 0.2584 0.5745 -0.0304 0.0041  0.0228  163 PRO A CG    
1317 C  CD    . PRO A 163 ? 0.3092 0.2414 0.5535 -0.0288 0.008   0.0192  163 PRO A CD    
1318 N  N     . ALA A 164 ? 0.3103 0.2241 0.5279 -0.0265 0.0022  0.0201  164 ALA A N     
1319 C  CA    . ALA A 164 ? 0.3095 0.2165 0.5179 -0.025  0.0005  0.0205  164 ALA A CA    
1320 C  C     . ALA A 164 ? 0.3032 0.2109 0.5033 -0.0236 0.0028  0.0193  164 ALA A C     
1321 O  O     . ALA A 164 ? 0.3109 0.2125 0.5019 -0.0223 0.0009  0.0202  164 ALA A O     
1322 C  CB    . ALA A 164 ? 0.3095 0.2161 0.5208 -0.0245 0.0011  0.0197  164 ALA A CB    
1323 N  N     . ILE A 165 ? 0.2889 0.2037 0.4918 -0.0238 0.0069  0.0173  165 ILE A N     
1324 C  CA    . ILE A 165 ? 0.2864 0.2021 0.4821 -0.0225 0.009   0.0162  165 ILE A CA    
1325 C  C     . ILE A 165 ? 0.2795 0.1915 0.4681 -0.0224 0.0067  0.0177  165 ILE A C     
1326 O  O     . ILE A 165 ? 0.284  0.1906 0.4639 -0.0207 0.0053  0.0183  165 ILE A O     
1327 C  CB    . ILE A 165 ? 0.2892 0.2127 0.489  -0.0227 0.0135  0.0137  165 ILE A CB    
1328 C  CG1   . ILE A 165 ? 0.296  0.2229 0.5037 -0.023  0.0152  0.0121  165 ILE A CG1   
1329 C  CG2   . ILE A 165 ? 0.3003 0.2243 0.4932 -0.0213 0.0153  0.0127  165 ILE A CG2   
1330 C  CD1   . ILE A 165 ? 0.3142 0.2376 0.5204 -0.0222 0.0144  0.0125  165 ILE A CD1   
1331 N  N     . PRO A 166 ? 0.2651 0.1792 0.4572 -0.024  0.0059  0.0185  166 PRO A N     
1332 C  CA    . PRO A 166 ? 0.2622 0.1719 0.4476 -0.0241 0.003   0.0202  166 PRO A CA    
1333 C  C     . PRO A 166 ? 0.2597 0.16   0.4393 -0.0234 -0.002  0.0223  166 PRO A C     
1334 O  O     . PRO A 166 ? 0.265  0.1598 0.4354 -0.0221 -0.0041 0.0229  166 PRO A O     
1335 C  CB    . PRO A 166 ? 0.2691 0.1831 0.4616 -0.0264 0.0028  0.0214  166 PRO A CB    
1336 C  CG    . PRO A 166 ? 0.2721 0.1943 0.4726 -0.0267 0.0074  0.0192  166 PRO A CG    
1337 C  CD    . PRO A 166 ? 0.2519 0.1726 0.4539 -0.0257 0.0077  0.0182  166 PRO A CD    
1338 N  N     . TYR A 167 ? 0.2514 0.1496 0.4358 -0.0241 -0.004  0.0232  167 TYR A N     
1339 C  CA    . TYR A 167 ? 0.2527 0.1415 0.4314 -0.0234 -0.0091 0.0251  167 TYR A CA    
1340 C  C     . TYR A 167 ? 0.2546 0.1384 0.4234 -0.0206 -0.0086 0.0244  167 TYR A C     
1341 O  O     . TYR A 167 ? 0.2638 0.1391 0.4234 -0.0192 -0.0123 0.0256  167 TYR A O     
1342 C  CB    . TYR A 167 ? 0.2467 0.1342 0.4332 -0.0249 -0.0116 0.0264  167 TYR A CB    
1343 C  CG    . TYR A 167 ? 0.259  0.1359 0.4388 -0.0245 -0.0176 0.0287  167 TYR A CG    
1344 C  CD1   . TYR A 167 ? 0.2723 0.1448 0.451  -0.0259 -0.0224 0.031   167 TYR A CD1   
1345 C  CD2   . TYR A 167 ? 0.2757 0.1465 0.4489 -0.0226 -0.0186 0.0285  167 TYR A CD2   
1346 C  CE1   . TYR A 167 ? 0.2902 0.1518 0.4613 -0.0254 -0.0285 0.0328  167 TYR A CE1   
1347 C  CE2   . TYR A 167 ? 0.2923 0.1523 0.4572 -0.0218 -0.0242 0.0303  167 TYR A CE2   
1348 C  CZ    . TYR A 167 ? 0.3042 0.1595 0.4682 -0.0232 -0.0293 0.0324  167 TYR A CZ    
1349 O  OH    . TYR A 167 ? 0.3275 0.1712 0.4827 -0.0223 -0.0353 0.034   167 TYR A OH    
1350 N  N     . SER A 168 ? 0.2448 0.1336 0.415  -0.0196 -0.0041 0.0225  168 SER A N     
1351 C  CA    . SER A 168 ? 0.2451 0.1305 0.407  -0.0169 -0.003  0.0222  168 SER A CA    
1352 C  C     . SER A 168 ? 0.2502 0.1316 0.4015 -0.0148 -0.0036 0.0224  168 SER A C     
1353 O  O     . SER A 168 ? 0.2567 0.1318 0.399  -0.0122 -0.0047 0.023   168 SER A O     
1354 C  CB    . SER A 168 ? 0.25   0.1425 0.4166 -0.0166 0.0019  0.0204  168 SER A CB    
1355 O  OG    . SER A 168 ? 0.27   0.1694 0.4391 -0.0171 0.0051  0.0188  168 SER A OG    
1356 N  N     . TYR A 169 ? 0.248  0.1327 0.3999 -0.0156 -0.003  0.0219  169 TYR A N     
1357 C  CA    . TYR A 169 ? 0.2591 0.1401 0.4013 -0.0137 -0.0039 0.022   169 TYR A CA    
1358 C  C     . TYR A 169 ? 0.2646 0.1353 0.3994 -0.0131 -0.0097 0.0239  169 TYR A C     
1359 O  O     . TYR A 169 ? 0.2745 0.1386 0.3986 -0.0101 -0.0109 0.0241  169 TYR A O     
1360 C  CB    . TYR A 169 ? 0.2615 0.1487 0.4069 -0.0152 -0.0021 0.0211  169 TYR A CB    
1361 C  CG    . TYR A 169 ? 0.2728 0.1685 0.4223 -0.015  0.0033  0.0191  169 TYR A CG    
1362 C  CD1   . TYR A 169 ? 0.2824 0.1843 0.4413 -0.0166 0.0059  0.0181  169 TYR A CD1   
1363 C  CD2   . TYR A 169 ? 0.2918 0.1888 0.4356 -0.013  0.0054  0.0182  169 TYR A CD2   
1364 C  CE1   . TYR A 169 ? 0.2923 0.2011 0.4545 -0.0164 0.0102  0.0162  169 TYR A CE1   
1365 C  CE2   . TYR A 169 ? 0.303  0.2074 0.4506 -0.0129 0.0098  0.0166  169 TYR A CE2   
1366 C  CZ    . TYR A 169 ? 0.3073 0.2173 0.4639 -0.0146 0.012   0.0156  169 TYR A CZ    
1367 O  OH    . TYR A 169 ? 0.3183 0.2348 0.4784 -0.0146 0.0157  0.0139  169 TYR A OH    
1368 N  N     . ILE A 170 ? 0.2552 0.124  0.3954 -0.0157 -0.0134 0.0253  170 ILE A N     
1369 C  CA    . ILE A 170 ? 0.2568 0.1153 0.3908 -0.0155 -0.0197 0.0273  170 ILE A CA    
1370 C  C     . ILE A 170 ? 0.2655 0.1165 0.3929 -0.0132 -0.0213 0.0277  170 ILE A C     
1371 O  O     . ILE A 170 ? 0.2784 0.1201 0.3944 -0.0107 -0.0246 0.0283  170 ILE A O     
1372 C  CB    . ILE A 170 ? 0.2546 0.1139 0.3978 -0.0191 -0.0232 0.0292  170 ILE A CB    
1373 C  CG1   . ILE A 170 ? 0.2587 0.1257 0.4086 -0.0215 -0.0214 0.0292  170 ILE A CG1   
1374 C  CG2   . ILE A 170 ? 0.2655 0.1133 0.4023 -0.0192 -0.0305 0.0314  170 ILE A CG2   
1375 C  CD1   . ILE A 170 ? 0.2623 0.133  0.424  -0.0249 -0.023  0.031   170 ILE A CD1   
1376 N  N     . SER A 171 ? 0.2595 0.1142 0.3932 -0.0138 -0.019  0.0273  171 SER A N     
1377 C  CA    . SER A 171 ? 0.2736 0.1214 0.4013 -0.0117 -0.0204 0.0279  171 SER A CA    
1378 C  C     . SER A 171 ? 0.2871 0.1328 0.4043 -0.0078 -0.0177 0.0272  171 SER A C     
1379 O  O     . SER A 171 ? 0.2926 0.1292 0.3996 -0.0052 -0.0203 0.028   171 SER A O     
1380 C  CB    . SER A 171 ? 0.2919 0.1447 0.4293 -0.0133 -0.0184 0.0277  171 SER A CB    
1381 O  OG    . SER A 171 ? 0.3192 0.1817 0.4623 -0.0133 -0.0124 0.026   171 SER A OG    
1382 N  N     . HIS A 172 ? 0.2934 0.1473 0.4128 -0.0072 -0.0124 0.0257  172 HIS A N     
1383 C  CA    . HIS A 172 ? 0.313  0.1662 0.4235 -0.0035 -0.0094 0.0252  172 HIS A CA    
1384 C  C     . HIS A 172 ? 0.3281 0.173  0.4268 -0.001  -0.0127 0.0256  172 HIS A C     
1385 O  O     . HIS A 172 ? 0.3362 0.1748 0.4242 0.0028  -0.0129 0.026   172 HIS A O     
1386 C  CB    . HIS A 172 ? 0.3254 0.1894 0.4419 -0.0038 -0.0037 0.0237  172 HIS A CB    
1387 C  CG    . HIS A 172 ? 0.3554 0.2208 0.4666 -0.0005 0.0003  0.0237  172 HIS A CG    
1388 N  ND1   . HIS A 172 ? 0.3814 0.2417 0.4872 0.0017  0.0001  0.0249  172 HIS A ND1   
1389 C  CD2   . HIS A 172 ? 0.368  0.2398 0.4795 0.0008  0.0044  0.0228  172 HIS A CD2   
1390 C  CE1   . HIS A 172 ? 0.3899 0.2541 0.4929 0.0043  0.0043  0.025   172 HIS A CE1   
1391 N  NE2   . HIS A 172 ? 0.3861 0.2571 0.4926 0.0038  0.0069  0.0238  172 HIS A NE2   
1392 N  N     . SER A 173 ? 0.3334 0.1776 0.4337 -0.003  -0.0157 0.0256  173 SER A N     
1393 C  CA    . SER A 173 ? 0.3493 0.185  0.4389 -0.001  -0.0198 0.026   173 SER A CA    
1394 C  C     . SER A 173 ? 0.3713 0.1945 0.4516 0.0007  -0.0252 0.0273  173 SER A C     
1395 O  O     . SER A 173 ? 0.3778 0.193  0.4454 0.0047  -0.0266 0.0273  173 SER A O     
1396 C  CB    . SER A 173 ? 0.3499 0.1875 0.4449 -0.0043 -0.0224 0.0264  173 SER A CB    
1397 O  OG    . SER A 173 ? 0.358  0.2054 0.4586 -0.0052 -0.0178 0.0251  173 SER A OG    
1398 N  N     . LYS A 174 ? 0.3786 0.2    0.4651 -0.0021 -0.0284 0.0285  174 LYS A N     
1399 C  CA    . LYS A 174 ? 0.4023 0.2117 0.4807 -0.0009 -0.034  0.0298  174 LYS A CA    
1400 C  C     . LYS A 174 ? 0.4228 0.2286 0.4924 0.0031  -0.0315 0.0296  174 LYS A C     
1401 O  O     . LYS A 174 ? 0.4375 0.2327 0.4935 0.0068  -0.0344 0.0299  174 LYS A O     
1402 C  CB    . LYS A 174 ? 0.4241 0.2336 0.5127 -0.005  -0.0376 0.0313  174 LYS A CB    
1403 C  CG    . LYS A 174 ? 0.4767 0.2896 0.5744 -0.0091 -0.0404 0.0322  174 LYS A CG    
1404 C  CD    . LYS A 174 ? 0.5499 0.3536 0.6385 -0.0084 -0.0462 0.033   174 LYS A CD    
1405 C  CE    . LYS A 174 ? 0.5905 0.3995 0.6879 -0.0121 -0.0475 0.034   174 LYS A CE    
1406 N  NZ    . LYS A 174 ? 0.6226 0.4236 0.7104 -0.011  -0.0522 0.0345  174 LYS A NZ    
1407 N  N     . ASN A 175 ? 0.4224 0.2369 0.4991 0.0027  -0.0259 0.0291  175 ASN A N     
1408 C  CA    . ASN A 175 ? 0.4364 0.2488 0.5062 0.0062  -0.023  0.0294  175 ASN A CA    
1409 C  C     . ASN A 175 ? 0.4477 0.2577 0.5056 0.0112  -0.0204 0.0289  175 ASN A C     
1410 O  O     . ASN A 175 ? 0.4593 0.2608 0.5052 0.0151  -0.0213 0.0296  175 ASN A O     
1411 C  CB    . ASN A 175 ? 0.4448 0.268  0.5257 0.0045  -0.0175 0.0292  175 ASN A CB    
1412 C  CG    . ASN A 175 ? 0.4924 0.3168 0.5836 0.0006  -0.0197 0.0297  175 ASN A CG    
1413 O  OD1   . ASN A 175 ? 0.5183 0.3344 0.6071 -0.0003 -0.0254 0.0308  175 ASN A OD1   
1414 N  ND2   . ASN A 175 ? 0.4982 0.3331 0.6013 -0.0017 -0.0155 0.029   175 ASN A ND2   
1415 N  N     . THR A 176 ? 0.4402 0.2577 0.5013 0.0111  -0.017  0.0277  176 THR A N     
1416 C  CA    . THR A 176 ? 0.4404 0.2577 0.4925 0.0157  -0.0138 0.0272  176 THR A CA    
1417 C  C     . THR A 176 ? 0.453  0.2606 0.4931 0.0184  -0.0182 0.0269  176 THR A C     
1418 O  O     . THR A 176 ? 0.4644 0.2698 0.495  0.023   -0.016  0.0266  176 THR A O     
1419 C  CB    . THR A 176 ? 0.4359 0.2659 0.4973 0.0143  -0.0084 0.0262  176 THR A CB    
1420 O  OG1   . THR A 176 ? 0.441  0.2733 0.5083 0.0109  -0.0108 0.0254  176 THR A OG1   
1421 C  CG2   . THR A 176 ? 0.4303 0.2698 0.5029 0.012   -0.004  0.0263  176 THR A CG2   
1422 N  N     . GLY A 177 ? 0.4461 0.2486 0.4876 0.0155  -0.0241 0.0271  177 GLY A N     
1423 C  CA    . GLY A 177 ? 0.4497 0.2433 0.481  0.0175  -0.0287 0.0268  177 GLY A CA    
1424 C  C     . GLY A 177 ? 0.4407 0.2415 0.4746 0.0176  -0.0257 0.0256  177 GLY A C     
1425 O  O     . GLY A 177 ? 0.4454 0.2397 0.4704 0.0198  -0.0287 0.0252  177 GLY A O     
1426 N  N     . ASN A 178 ? 0.4287 0.2425 0.4745 0.0151  -0.0202 0.0251  178 ASN A N     
1427 C  CA    . ASN A 178 ? 0.4277 0.2498 0.4776 0.0147  -0.0168 0.024   178 ASN A CA    
1428 C  C     . ASN A 178 ? 0.4151 0.2429 0.4763 0.0093  -0.0183 0.024   178 ASN A C     
1429 O  O     . ASN A 178 ? 0.4172 0.245  0.4853 0.0058  -0.0205 0.0248  178 ASN A O     
1430 C  CB    . ASN A 178 ? 0.4451 0.2775 0.5    0.0159  -0.0096 0.0235  178 ASN A CB    
1431 C  CG    . ASN A 178 ? 0.4953 0.3349 0.552  0.0166  -0.0061 0.0225  178 ASN A CG    
1432 O  OD1   . ASN A 178 ? 0.5225 0.3584 0.5739 0.0175  -0.0086 0.022   178 ASN A OD1   
1433 N  ND2   . ASN A 178 ? 0.4918 0.3417 0.5561 0.0161  -0.0005 0.0221  178 ASN A ND2   
1434 N  N     . PHE A 179 ? 0.4005 0.233  0.4636 0.0086  -0.0172 0.0232  179 PHE A N     
1435 C  CA    . PHE A 179 ? 0.3884 0.2268 0.4614 0.0038  -0.018  0.0233  179 PHE A CA    
1436 C  C     . PHE A 179 ? 0.3741 0.2251 0.4581 0.0018  -0.0119 0.0223  179 PHE A C     
1437 O  O     . PHE A 179 ? 0.3712 0.2276 0.455  0.003   -0.0084 0.0212  179 PHE A O     
1438 C  CB    . PHE A 179 ? 0.39   0.2253 0.4579 0.0041  -0.0207 0.0232  179 PHE A CB    
1439 C  CG    . PHE A 179 ? 0.3926 0.2329 0.4697 -0.0007 -0.0221 0.0239  179 PHE A CG    
1440 C  CD1   . PHE A 179 ? 0.4035 0.2422 0.4866 -0.0043 -0.0256 0.0254  179 PHE A CD1   
1441 C  CD2   . PHE A 179 ? 0.3991 0.2454 0.4783 -0.0015 -0.0199 0.0231  179 PHE A CD2   
1442 C  CE1   . PHE A 179 ? 0.4085 0.2523 0.5002 -0.0085 -0.0265 0.0264  179 PHE A CE1   
1443 C  CE2   . PHE A 179 ? 0.4056 0.2564 0.4926 -0.0058 -0.021  0.024   179 PHE A CE2   
1444 C  CZ    . PHE A 179 ? 0.4029 0.2526 0.4961 -0.0092 -0.0241 0.0257  179 PHE A CZ    
1445 N  N     . ILE A 180 ? 0.3619 0.2173 0.4554 -0.0012 -0.0109 0.0225  180 ILE A N     
1446 C  CA    . ILE A 180 ? 0.3478 0.2144 0.4521 -0.0034 -0.0058 0.0215  180 ILE A CA    
1447 C  C     . ILE A 180 ? 0.3407 0.2106 0.4543 -0.0077 -0.0075 0.0219  180 ILE A C     
1448 O  O     . ILE A 180 ? 0.3393 0.2052 0.4552 -0.0092 -0.0108 0.0232  180 ILE A O     
1449 C  CB    . ILE A 180 ? 0.3462 0.2145 0.453  -0.0024 -0.0032 0.0214  180 ILE A CB    
1450 C  CG1   . ILE A 180 ? 0.3604 0.2246 0.4572 0.0021  -0.0018 0.0216  180 ILE A CG1   
1451 C  CG2   . ILE A 180 ? 0.3426 0.2216 0.46   -0.0046 0.0016  0.0203  180 ILE A CG2   
1452 C  CD1   . ILE A 180 ? 0.3796 0.235  0.47   0.0039  -0.0046 0.0228  180 ILE A CD1   
1453 N  N     . VAL A 181 ? 0.3347 0.2115 0.4532 -0.0096 -0.0055 0.0212  181 VAL A N     
1454 C  CA    . VAL A 181 ? 0.3377 0.2179 0.4645 -0.0134 -0.0067 0.022   181 VAL A CA    
1455 C  C     . VAL A 181 ? 0.3365 0.2271 0.4716 -0.0153 -0.002  0.0205  181 VAL A C     
1456 O  O     . VAL A 181 ? 0.3308 0.2252 0.4639 -0.014  0.0012  0.0191  181 VAL A O     
1457 C  CB    . VAL A 181 ? 0.3529 0.2271 0.4746 -0.0141 -0.0115 0.0235  181 VAL A CB    
1458 C  CG1   . VAL A 181 ? 0.3617 0.2385 0.4795 -0.0132 -0.0098 0.0226  181 VAL A CG1   
1459 C  CG2   . VAL A 181 ? 0.3552 0.2311 0.4852 -0.018  -0.014  0.0253  181 VAL A CG2   
1460 N  N     . GLN A 182 ? 0.3397 0.2345 0.4839 -0.0182 -0.0018 0.021   182 GLN A N     
1461 C  CA    . GLN A 182 ? 0.3475 0.2515 0.4992 -0.02   0.0022  0.0197  182 GLN A CA    
1462 C  C     . GLN A 182 ? 0.3554 0.2598 0.5083 -0.0223 0.0002  0.0213  182 GLN A C     
1463 O  O     . GLN A 182 ? 0.3583 0.2594 0.5134 -0.0239 -0.0035 0.0235  182 GLN A O     
1464 C  CB    . GLN A 182 ? 0.3674 0.2759 0.5285 -0.0214 0.0042  0.0192  182 GLN A CB    
1465 C  CG    . GLN A 182 ? 0.4223 0.3393 0.589  -0.0219 0.0091  0.017   182 GLN A CG    
1466 C  CD    . GLN A 182 ? 0.4939 0.414  0.6685 -0.0225 0.0108  0.0162  182 GLN A CD    
1467 O  OE1   . GLN A 182 ? 0.5135 0.4333 0.6938 -0.024  0.0091  0.0175  182 GLN A OE1   
1468 N  NE2   . GLN A 182 ? 0.506  0.4289 0.6815 -0.0214 0.0137  0.0143  182 GLN A NE2   
1469 N  N     . ALA A 183 ? 0.3564 0.2644 0.5073 -0.0223 0.0021  0.0205  183 ALA A N     
1470 C  CA    . ALA A 183 ? 0.3625 0.2714 0.514  -0.0244 0.0005  0.022   183 ALA A CA    
1471 C  C     . ALA A 183 ? 0.3605 0.2785 0.5189 -0.0261 0.005   0.0209  183 ALA A C     
1472 O  O     . ALA A 183 ? 0.3555 0.278  0.5143 -0.025  0.0088  0.0185  183 ALA A O     
1473 C  CB    . ALA A 183 ? 0.3698 0.2743 0.5118 -0.0229 -0.0014 0.0221  183 ALA A CB    
1474 N  N     . TYR A 184 ? 0.3613 0.2822 0.5254 -0.0287 0.0044  0.0229  184 TYR A N     
1475 C  CA    . TYR A 184 ? 0.3631 0.2926 0.5337 -0.0301 0.0088  0.022   184 TYR A CA    
1476 C  C     . TYR A 184 ? 0.3684 0.2999 0.5367 -0.0314 0.0088  0.0231  184 TYR A C     
1477 O  O     . TYR A 184 ? 0.3682 0.2964 0.5354 -0.0329 0.0051  0.026   184 TYR A O     
1478 C  CB    . TYR A 184 ? 0.3569 0.2902 0.5374 -0.0316 0.0096  0.0231  184 TYR A CB    
1479 C  CG    . TYR A 184 ? 0.3679 0.2979 0.5502 -0.0305 0.0085  0.0225  184 TYR A CG    
1480 C  CD1   . TYR A 184 ? 0.3758 0.3087 0.5601 -0.029  0.012   0.0197  184 TYR A CD1   
1481 C  CD2   . TYR A 184 ? 0.3857 0.3085 0.5661 -0.0307 0.0035  0.0248  184 TYR A CD2   
1482 C  CE1   . TYR A 184 ? 0.3882 0.3176 0.5733 -0.028  0.0108  0.0193  184 TYR A CE1   
1483 C  CE2   . TYR A 184 ? 0.3991 0.3181 0.5798 -0.0295 0.0023  0.0243  184 TYR A CE2   
1484 C  CZ    . TYR A 184 ? 0.4069 0.3295 0.5902 -0.0282 0.0061  0.0216  184 TYR A CZ    
1485 O  OH    . TYR A 184 ? 0.43   0.3489 0.6136 -0.0272 0.0048  0.0214  184 TYR A OH    
1486 N  N     . PHE A 185 ? 0.3734 0.3097 0.5405 -0.0309 0.0126  0.0209  185 PHE A N     
1487 C  CA    . PHE A 185 ? 0.3884 0.3271 0.5531 -0.0322 0.0131  0.0217  185 PHE A CA    
1488 C  C     . PHE A 185 ? 0.3941 0.3405 0.566  -0.0336 0.0171  0.0217  185 PHE A C     
1489 O  O     . PHE A 185 ? 0.3928 0.3431 0.569  -0.0328 0.0206  0.0194  185 PHE A O     
1490 C  CB    . PHE A 185 ? 0.3949 0.333  0.5524 -0.0304 0.0143  0.0193  185 PHE A CB    
1491 C  CG    . PHE A 185 ? 0.4126 0.3434 0.5619 -0.0289 0.0103  0.0198  185 PHE A CG    
1492 C  CD1   . PHE A 185 ? 0.4257 0.3498 0.5732 -0.0286 0.0061  0.0217  185 PHE A CD1   
1493 C  CD2   . PHE A 185 ? 0.4268 0.3571 0.5697 -0.0277 0.0107  0.0185  185 PHE A CD2   
1494 C  CE1   . PHE A 185 ? 0.4384 0.3552 0.5774 -0.0267 0.0026  0.0219  185 PHE A CE1   
1495 C  CE2   . PHE A 185 ? 0.4395 0.3631 0.5747 -0.0258 0.0073  0.0189  185 PHE A CE2   
1496 C  CZ    . PHE A 185 ? 0.4381 0.3549 0.5712 -0.0252 0.0034  0.0206  185 PHE A CZ    
1497 N  N     . ARG A 186 ? 0.3985 0.3472 0.5717 -0.0357 0.0167  0.0243  186 ARG A N     
1498 C  CA    . ARG A 186 ? 0.4044 0.3606 0.5838 -0.0369 0.0208  0.0247  186 ARG A CA    
1499 C  C     . ARG A 186 ? 0.4212 0.3814 0.5977 -0.0357 0.0252  0.0213  186 ARG A C     
1500 O  O     . ARG A 186 ? 0.4253 0.3849 0.5957 -0.0358 0.0249  0.021   186 ARG A O     
1501 C  CB    . ARG A 186 ? 0.409  0.3665 0.59   -0.0395 0.0192  0.0289  186 ARG A CB    
1502 C  CG    . ARG A 186 ? 0.4326 0.3984 0.6197 -0.0405 0.0239  0.0297  186 ARG A CG    
1503 C  CD    . ARG A 186 ? 0.467  0.4344 0.6532 -0.0428 0.023   0.0334  186 ARG A CD    
1504 N  NE    . ARG A 186 ? 0.4973 0.4639 0.6896 -0.0451 0.0194  0.0382  186 ARG A NE    
1505 C  CZ    . ARG A 186 ? 0.5161 0.4892 0.7173 -0.0465 0.0217  0.0412  186 ARG A CZ    
1506 N  NH1   . ARG A 186 ? 0.5011 0.4816 0.7056 -0.0456 0.0278  0.0396  186 ARG A NH1   
1507 N  NH2   . ARG A 186 ? 0.5148 0.4867 0.7217 -0.0488 0.0178  0.0458  186 ARG A NH2   
1508 N  N     . GLY A 187 ? 0.4285 0.3922 0.6091 -0.0345 0.0287  0.0186  187 GLY A N     
1509 C  CA    . GLY A 187 ? 0.444  0.4112 0.6224 -0.0333 0.0326  0.0152  187 GLY A CA    
1510 C  C     . GLY A 187 ? 0.4557 0.4283 0.6352 -0.0343 0.0357  0.0162  187 GLY A C     
1511 O  O     . GLY A 187 ? 0.4538 0.4292 0.6386 -0.0358 0.0359  0.0194  187 GLY A O     
1512 N  N     . GLU A 188 ? 0.4668 0.4411 0.6415 -0.0336 0.0381  0.0137  188 GLU A N     
1513 C  CA    . GLU A 188 ? 0.4818 0.461  0.6563 -0.0343 0.0415  0.0144  188 GLU A CA    
1514 C  C     . GLU A 188 ? 0.49   0.4745 0.6719 -0.0336 0.0454  0.014   188 GLU A C     
1515 O  O     . GLU A 188 ? 0.4922 0.4812 0.6769 -0.0345 0.0477  0.0165  188 GLU A O     
1516 C  CB    . GLU A 188 ? 0.52   0.4991 0.6873 -0.0334 0.0429  0.0114  188 GLU A CB    
1517 C  CG    . GLU A 188 ? 0.5983 0.5726 0.7586 -0.0338 0.0393  0.0116  188 GLU A CG    
1518 C  CD    . GLU A 188 ? 0.6826 0.6534 0.8408 -0.0321 0.0378  0.0087  188 GLU A CD    
1519 O  OE1   . GLU A 188 ? 0.6949 0.6651 0.8577 -0.0312 0.0377  0.0079  188 GLU A OE1   
1520 O  OE2   . GLU A 188 ? 0.7118 0.6806 0.8639 -0.0317 0.0367  0.0074  188 GLU A OE2   
1521 N  N     . GLU A 189 ? 0.49   0.474  0.6754 -0.0319 0.0462  0.0113  189 GLU A N     
1522 C  CA    . GLU A 189 ? 0.4911 0.4797 0.6836 -0.0309 0.0497  0.0107  189 GLU A CA    
1523 C  C     . GLU A 189 ? 0.4996 0.4891 0.7005 -0.0319 0.0483  0.0141  189 GLU A C     
1524 O  O     . GLU A 189 ? 0.5003 0.4931 0.708  -0.0308 0.0507  0.0136  189 GLU A O     
1525 C  CB    . GLU A 189 ? 0.5027 0.4906 0.695  -0.0286 0.0513  0.0061  189 GLU A CB    
1526 C  CG    . GLU A 189 ? 0.5324 0.5219 0.719  -0.0274 0.0545  0.0031  189 GLU A CG    
1527 C  CD    . GLU A 189 ? 0.581  0.5692 0.7669 -0.0254 0.0555  -0.0014 189 GLU A CD    
1528 O  OE1   . GLU A 189 ? 0.5884 0.5733 0.7758 -0.0252 0.053   -0.0024 189 GLU A OE1   
1529 O  OE2   . GLU A 189 ? 0.6006 0.5908 0.7841 -0.0239 0.0587  -0.0039 189 GLU A OE2   
1530 N  N     . TYR A 190 ? 0.5054 0.4918 0.7061 -0.0338 0.0441  0.0177  190 TYR A N     
1531 C  CA    . TYR A 190 ? 0.5122 0.4992 0.7208 -0.0351 0.0422  0.0214  190 TYR A CA    
1532 C  C     . TYR A 190 ? 0.5219 0.5155 0.735  -0.0362 0.0452  0.0246  190 TYR A C     
1533 O  O     . TYR A 190 ? 0.5257 0.5194 0.7356 -0.038  0.0441  0.0275  190 TYR A O     
1534 C  CB    . TYR A 190 ? 0.5121 0.4929 0.7182 -0.0368 0.0363  0.0241  190 TYR A CB    
1535 C  CG    . TYR A 190 ? 0.5154 0.4965 0.7292 -0.0386 0.0337  0.0285  190 TYR A CG    
1536 C  CD1   . TYR A 190 ? 0.5235 0.5046 0.7444 -0.0379 0.0333  0.0283  190 TYR A CD1   
1537 C  CD2   . TYR A 190 ? 0.5254 0.5069 0.74   -0.041  0.0314  0.0331  190 TYR A CD2   
1538 C  CE1   . TYR A 190 ? 0.5302 0.5116 0.7587 -0.0396 0.0306  0.0325  190 TYR A CE1   
1539 C  CE2   . TYR A 190 ? 0.5334 0.5153 0.7558 -0.0429 0.0287  0.0374  190 TYR A CE2   
1540 C  CZ    . TYR A 190 ? 0.5407 0.5227 0.7702 -0.0422 0.0283  0.0371  190 TYR A CZ    
1541 O  OH    . TYR A 190 ? 0.5557 0.538  0.7934 -0.0441 0.0252  0.0416  190 TYR A OH    
1542 N  N     . GLN A 191 ? 0.5238 0.5229 0.7439 -0.0349 0.0493  0.0242  191 GLN A N     
1543 C  CA    . GLN A 191 ? 0.5315 0.5379 0.7565 -0.0355 0.053   0.0274  191 GLN A CA    
1544 C  C     . GLN A 191 ? 0.5333 0.5434 0.7698 -0.0355 0.0535  0.03    191 GLN A C     
1545 O  O     . GLN A 191 ? 0.5325 0.5464 0.7735 -0.0332 0.0575  0.0278  191 GLN A O     
1546 C  CB    . GLN A 191 ? 0.5545 0.5646 0.7754 -0.0331 0.0587  0.0237  191 GLN A CB    
1547 C  CG    . GLN A 191 ? 0.5946 0.6087 0.8118 -0.034  0.0613  0.026   191 GLN A CG    
1548 C  CD    . GLN A 191 ? 0.648  0.657  0.857  -0.0361 0.0573  0.0269  191 GLN A CD    
1549 O  OE1   . GLN A 191 ? 0.66   0.6638 0.862  -0.0354 0.0553  0.0233  191 GLN A OE1   
1550 N  NE2   . GLN A 191 ? 0.6642 0.6749 0.8746 -0.0387 0.0559  0.032   191 GLN A NE2   
1551 N  N     . PRO A 192 ? 0.5343 0.543  0.7758 -0.0381 0.0491  0.0346  192 PRO A N     
1552 C  CA    . PRO A 192 ? 0.5306 0.5423 0.7836 -0.0383 0.0487  0.0374  192 PRO A CA    
1553 C  C     . PRO A 192 ? 0.5294 0.5506 0.7908 -0.0378 0.054   0.0402  192 PRO A C     
1554 O  O     . PRO A 192 ? 0.5304 0.5551 0.8012 -0.0368 0.0553  0.0408  192 PRO A O     
1555 C  CB    . PRO A 192 ? 0.5403 0.5469 0.7948 -0.0414 0.042   0.0417  192 PRO A CB    
1556 C  CG    . PRO A 192 ? 0.5506 0.5548 0.7964 -0.0431 0.0403  0.0429  192 PRO A CG    
1557 C  CD    . PRO A 192 ? 0.5344 0.5376 0.7709 -0.0408 0.0436  0.0375  192 PRO A CD    
1558 N  N     . LYS A 193 ? 0.5238 0.5494 0.7821 -0.0384 0.0572  0.0419  193 LYS A N     
1559 C  CA    . LYS A 193 ? 0.5156 0.5507 0.7811 -0.0376 0.063   0.0447  193 LYS A CA    
1560 C  C     . LYS A 193 ? 0.5129 0.5514 0.7784 -0.0334 0.069   0.0397  193 LYS A C     
1561 O  O     . LYS A 193 ? 0.5118 0.5578 0.785  -0.0318 0.0738  0.0415  193 LYS A O     
1562 C  CB    . LYS A 193 ? 0.5333 0.5716 0.7935 -0.039  0.0651  0.0474  193 LYS A CB    
1563 C  CG    . LYS A 193 ? 0.5833 0.6181 0.8424 -0.0431 0.0592  0.0522  193 LYS A CG    
1564 C  CD    . LYS A 193 ? 0.6354 0.6743 0.8904 -0.0445 0.0618  0.0552  193 LYS A CD    
1565 C  CE    . LYS A 193 ? 0.6761 0.7145 0.9348 -0.0488 0.0569  0.062   193 LYS A CE    
1566 N  NZ    . LYS A 193 ? 0.6997 0.7425 0.9549 -0.0502 0.0596  0.0653  193 LYS A NZ    
1567 N  N     . TYR A 194 ? 0.5088 0.5416 0.7657 -0.0314 0.0687  0.0336  194 TYR A N     
1568 C  CA    . TYR A 194 ? 0.509  0.5436 0.7645 -0.0275 0.0736  0.0286  194 TYR A CA    
1569 C  C     . TYR A 194 ? 0.5038 0.5343 0.7622 -0.0259 0.0716  0.0249  194 TYR A C     
1570 O  O     . TYR A 194 ? 0.5076 0.54   0.7671 -0.0226 0.0755  0.0213  194 TYR A O     
1571 C  CB    . TYR A 194 ? 0.519  0.5514 0.7624 -0.0263 0.0757  0.0246  194 TYR A CB    
1572 C  CG    . TYR A 194 ? 0.5345 0.5714 0.7749 -0.0275 0.0784  0.0281  194 TYR A CG    
1573 C  CD1   . TYR A 194 ? 0.5458 0.5906 0.79   -0.0255 0.0846  0.0296  194 TYR A CD1   
1574 C  CD2   . TYR A 194 ? 0.5531 0.5867 0.7873 -0.0305 0.0748  0.0302  194 TYR A CD2   
1575 C  CE1   . TYR A 194 ? 0.5609 0.6102 0.8026 -0.0267 0.0873  0.0333  194 TYR A CE1   
1576 C  CE2   . TYR A 194 ? 0.5689 0.6065 0.8006 -0.0318 0.0771  0.0337  194 TYR A CE2   
1577 C  CZ    . TYR A 194 ? 0.5802 0.6258 0.8157 -0.0301 0.0834  0.0354  194 TYR A CZ    
1578 O  OH    . TYR A 194 ? 0.6041 0.6542 0.8373 -0.0315 0.0858  0.0394  194 TYR A OH    
1579 N  N     . ASP A 195 ? 0.4931 0.5178 0.7524 -0.028  0.0657  0.0257  195 ASP A N     
1580 C  CA    . ASP A 195 ? 0.4889 0.5097 0.7512 -0.0266 0.0637  0.0227  195 ASP A CA    
1581 C  C     . ASP A 195 ? 0.4808 0.5019 0.7533 -0.0283 0.0602  0.0268  195 ASP A C     
1582 O  O     . ASP A 195 ? 0.4872 0.5048 0.7593 -0.0312 0.0553  0.0302  195 ASP A O     
1583 C  CB    . ASP A 195 ? 0.5102 0.523  0.7634 -0.0268 0.0602  0.0189  195 ASP A CB    
1584 C  CG    . ASP A 195 ? 0.557  0.5669 0.8117 -0.0246 0.0599  0.0146  195 ASP A CG    
1585 O  OD1   . ASP A 195 ? 0.5548 0.5661 0.8183 -0.0242 0.0594  0.0158  195 ASP A OD1   
1586 O  OD2   . ASP A 195 ? 0.5905 0.5967 0.8378 -0.0234 0.0599  0.0104  195 ASP A OD2   
1587 N  N     . LYS A 196 ? 0.4637 0.4885 0.745  -0.0263 0.0625  0.0264  196 LYS A N     
1588 C  CA    . LYS A 196 ? 0.453  0.4789 0.7454 -0.0275 0.0597  0.0301  196 LYS A CA    
1589 C  C     . LYS A 196 ? 0.4447 0.4621 0.7354 -0.0289 0.0534  0.0293  196 LYS A C     
1590 O  O     . LYS A 196 ? 0.4465 0.4627 0.7437 -0.0309 0.0492  0.0332  196 LYS A O     
1591 C  CB    . LYS A 196 ? 0.4733 0.5052 0.7748 -0.0244 0.0642  0.0291  196 LYS A CB    
1592 C  CG    . LYS A 196 ? 0.5286 0.568  0.8294 -0.0219 0.0713  0.0285  196 LYS A CG    
1593 C  CD    . LYS A 196 ? 0.5864 0.632  0.8908 -0.0242 0.0726  0.0345  196 LYS A CD    
1594 C  CE    . LYS A 196 ? 0.6337 0.6808 0.9281 -0.0238 0.0762  0.0334  196 LYS A CE    
1595 N  NZ    . LYS A 196 ? 0.6562 0.7068 0.9523 -0.0271 0.0754  0.0396  196 LYS A NZ    
1596 N  N     . LYS A 197 ? 0.4337 0.4452 0.7154 -0.0278 0.0525  0.0245  197 LYS A N     
1597 C  CA    . LYS A 197 ? 0.4279 0.4315 0.707  -0.0288 0.047   0.0237  197 LYS A CA    
1598 C  C     . LYS A 197 ? 0.4174 0.4162 0.6921 -0.0318 0.0419  0.0271  197 LYS A C     
1599 O  O     . LYS A 197 ? 0.4201 0.4133 0.6956 -0.0329 0.037   0.0284  197 LYS A O     
1600 C  CB    . LYS A 197 ? 0.4556 0.4549 0.7266 -0.0269 0.0477  0.0181  197 LYS A CB    
1601 C  CG    . LYS A 197 ? 0.5089 0.5103 0.7846 -0.024  0.0508  0.0146  197 LYS A CG    
1602 C  CD    . LYS A 197 ? 0.5738 0.5709 0.842  -0.0224 0.0511  0.0095  197 LYS A CD    
1603 C  CE    . LYS A 197 ? 0.6219 0.6215 0.894  -0.0194 0.0545  0.0059  197 LYS A CE    
1604 N  NZ    . LYS A 197 ? 0.6569 0.6511 0.9267 -0.0186 0.0523  0.0024  197 LYS A NZ    
1605 N  N     . LEU A 198 ? 0.405  0.4058 0.675  -0.0329 0.043   0.0287  198 LEU A N     
1606 C  CA    . LEU A 198 ? 0.4007 0.397  0.666  -0.0356 0.0383  0.0319  198 LEU A CA    
1607 C  C     . LEU A 198 ? 0.3971 0.3967 0.6706 -0.0382 0.0364  0.038   198 LEU A C     
1608 O  O     . LEU A 198 ? 0.405  0.4014 0.6747 -0.0405 0.0326  0.0411  198 LEU A O     
1609 C  CB    . LEU A 198 ? 0.3988 0.3951 0.6543 -0.0356 0.0402  0.0304  198 LEU A CB    
1610 C  CG    . LEU A 198 ? 0.4125 0.406  0.6599 -0.0334 0.042   0.0249  198 LEU A CG    
1611 C  CD1   . LEU A 198 ? 0.4193 0.4142 0.6588 -0.0334 0.0444  0.0239  198 LEU A CD1   
1612 C  CD2   . LEU A 198 ? 0.4237 0.4092 0.6663 -0.0336 0.0373  0.0236  198 LEU A CD2   
1613 N  N     . LYS A 199 ? 0.3804 0.3865 0.6651 -0.0377 0.0389  0.04    199 LYS A N     
1614 C  CA    . LYS A 199 ? 0.3733 0.3835 0.6674 -0.0402 0.0373  0.0463  199 LYS A CA    
1615 C  C     . LYS A 199 ? 0.3771 0.3797 0.6712 -0.0429 0.0294  0.0495  199 LYS A C     
1616 O  O     . LYS A 199 ? 0.3807 0.3833 0.6764 -0.0457 0.0263  0.0543  199 LYS A O     
1617 C  CB    . LYS A 199 ? 0.3769 0.3951 0.6838 -0.0387 0.041   0.0475  199 LYS A CB    
1618 C  CG    . LYS A 199 ? 0.4011 0.4254 0.7191 -0.0411 0.0402  0.0544  199 LYS A CG    
1619 C  CD    . LYS A 199 ? 0.4445 0.4762 0.7756 -0.0393 0.0437  0.0556  199 LYS A CD    
1620 C  CE    . LYS A 199 ? 0.4798 0.5169 0.8235 -0.042  0.0417  0.0629  199 LYS A CE    
1621 N  NZ    . LYS A 199 ? 0.4942 0.5364 0.851  -0.0404 0.0433  0.0639  199 LYS A NZ    
1622 N  N     . PHE A 200 ? 0.376  0.3716 0.6675 -0.042  0.026   0.0468  200 PHE A N     
1623 C  CA    . PHE A 200 ? 0.3844 0.3718 0.675  -0.0442 0.0185  0.0495  200 PHE A CA    
1624 C  C     . PHE A 200 ? 0.3946 0.3728 0.6719 -0.0441 0.015   0.047   200 PHE A C     
1625 O  O     . PHE A 200 ? 0.4028 0.373  0.6774 -0.0445 0.0095  0.0473  200 PHE A O     
1626 C  CB    . PHE A 200 ? 0.3836 0.3695 0.6821 -0.0436 0.0163  0.0496  200 PHE A CB    
1627 C  CG    . PHE A 200 ? 0.3863 0.3814 0.6987 -0.0437 0.0194  0.0526  200 PHE A CG    
1628 C  CD1   . PHE A 200 ? 0.3948 0.3937 0.7152 -0.0464 0.0173  0.0588  200 PHE A CD1   
1629 C  CD2   . PHE A 200 ? 0.3941 0.3945 0.7118 -0.0408 0.0246  0.0495  200 PHE A CD2   
1630 C  CE1   . PHE A 200 ? 0.3973 0.4055 0.7312 -0.0463 0.0206  0.0619  200 PHE A CE1   
1631 C  CE2   . PHE A 200 ? 0.3989 0.4082 0.7294 -0.0404 0.0279  0.0523  200 PHE A CE2   
1632 C  CZ    . PHE A 200 ? 0.3937 0.4072 0.7325 -0.0431 0.0261  0.0586  200 PHE A CZ    
1633 N  N     . PHE A 201 ? 0.3917 0.371  0.6608 -0.0435 0.0179  0.0448  201 PHE A N     
1634 C  CA    . PHE A 201 ? 0.3972 0.3683 0.654  -0.0433 0.0147  0.0428  201 PHE A CA    
1635 C  C     . PHE A 201 ? 0.3993 0.3667 0.6534 -0.046  0.0097  0.0472  201 PHE A C     
1636 O  O     . PHE A 201 ? 0.3988 0.3718 0.6564 -0.0476 0.0114  0.0502  201 PHE A O     
1637 C  CB    . PHE A 201 ? 0.3968 0.37   0.6458 -0.0414 0.0196  0.0385  201 PHE A CB    
1638 C  CG    . PHE A 201 ? 0.4085 0.3736 0.6457 -0.0408 0.0165  0.0364  201 PHE A CG    
1639 C  CD1   . PHE A 201 ? 0.4209 0.3797 0.6544 -0.0393 0.0142  0.034   201 PHE A CD1   
1640 C  CD2   . PHE A 201 ? 0.4208 0.3846 0.6507 -0.0416 0.0159  0.037   201 PHE A CD2   
1641 C  CE1   . PHE A 201 ? 0.4366 0.3885 0.6595 -0.0385 0.0118  0.0323  201 PHE A CE1   
1642 C  CE2   . PHE A 201 ? 0.4363 0.3929 0.6557 -0.0407 0.0132  0.0351  201 PHE A CE2   
1643 C  CZ    . PHE A 201 ? 0.4358 0.3868 0.6518 -0.039  0.0114  0.0328  201 PHE A CZ    
1644 N  N     . ASP A 202 ? 0.3986 0.3563 0.6464 -0.0464 0.0035  0.0477  202 ASP A N     
1645 C  CA    . ASP A 202 ? 0.3988 0.3511 0.6427 -0.0488 -0.0022 0.0514  202 ASP A CA    
1646 C  C     . ASP A 202 ? 0.3946 0.3443 0.6269 -0.0478 -0.0012 0.049   202 ASP A C     
1647 O  O     . ASP A 202 ? 0.3997 0.3437 0.6234 -0.0457 -0.0018 0.0453  202 ASP A O     
1648 C  CB    . ASP A 202 ? 0.4253 0.3673 0.6664 -0.0491 -0.0094 0.0526  202 ASP A CB    
1649 C  CG    . ASP A 202 ? 0.4863 0.4218 0.7246 -0.0517 -0.0165 0.0569  202 ASP A CG    
1650 O  OD1   . ASP A 202 ? 0.4901 0.4287 0.7279 -0.0533 -0.0159 0.0591  202 ASP A OD1   
1651 O  OD2   . ASP A 202 ? 0.5217 0.4484 0.7579 -0.052  -0.0229 0.0582  202 ASP A OD2   
1652 N  N     . GLU A 203 ? 0.3826 0.3366 0.6149 -0.0494 0.0002  0.0511  203 GLU A N     
1653 C  CA    . GLU A 203 ? 0.3831 0.3349 0.6047 -0.0487 0.001   0.049   203 GLU A CA    
1654 C  C     . GLU A 203 ? 0.3845 0.3253 0.5962 -0.0486 -0.0056 0.0492  203 GLU A C     
1655 O  O     . GLU A 203 ? 0.3881 0.3262 0.5905 -0.0472 -0.005  0.0467  203 GLU A O     
1656 C  CB    . GLU A 203 ? 0.4041 0.3629 0.6279 -0.0504 0.0039  0.0514  203 GLU A CB    
1657 C  CG    . GLU A 203 ? 0.4554 0.424  0.6845 -0.0491 0.0116  0.0493  203 GLU A CG    
1658 C  CD    . GLU A 203 ? 0.5353 0.5115 0.7669 -0.0506 0.0153  0.0518  203 GLU A CD    
1659 O  OE1   . GLU A 203 ? 0.5512 0.5248 0.7785 -0.0526 0.0121  0.0546  203 GLU A OE1   
1660 O  OE2   . GLU A 203 ? 0.5661 0.5506 0.8034 -0.0496 0.0213  0.051   203 GLU A OE2   
1661 N  N     . THR A 204 ? 0.3796 0.3138 0.593  -0.0498 -0.0119 0.052   204 THR A N     
1662 C  CA    . THR A 204 ? 0.3905 0.3133 0.5935 -0.0491 -0.0182 0.0518  204 THR A CA    
1663 C  C     . THR A 204 ? 0.3938 0.3117 0.5886 -0.0455 -0.017  0.0469  204 THR A C     
1664 O  O     . THR A 204 ? 0.4035 0.3127 0.5881 -0.0441 -0.0208 0.046   204 THR A O     
1665 C  CB    . THR A 204 ? 0.4124 0.3286 0.6185 -0.0513 -0.0257 0.0561  204 THR A CB    
1666 O  OG1   . THR A 204 ? 0.425  0.3401 0.6359 -0.0504 -0.0261 0.0554  204 THR A OG1   
1667 C  CG2   . THR A 204 ? 0.4138 0.3352 0.629  -0.0551 -0.0271 0.0616  204 THR A CG2   
1668 N  N     . ILE A 205 ? 0.3833 0.3069 0.5825 -0.0439 -0.0117 0.044   205 ILE A N     
1669 C  CA    . ILE A 205 ? 0.3836 0.3044 0.5769 -0.0408 -0.0097 0.0397  205 ILE A CA    
1670 C  C     . ILE A 205 ? 0.3909 0.312  0.5753 -0.0391 -0.0071 0.0368  205 ILE A C     
1671 O  O     . ILE A 205 ? 0.4008 0.3164 0.5771 -0.0366 -0.0078 0.0344  205 ILE A O     
1672 C  CB    . ILE A 205 ? 0.3807 0.3082 0.5824 -0.0401 -0.0049 0.0377  205 ILE A CB    
1673 C  CG1   . ILE A 205 ? 0.3879 0.3134 0.5972 -0.0413 -0.0084 0.0403  205 ILE A CG1   
1674 C  CG2   . ILE A 205 ? 0.3886 0.315  0.5849 -0.0371 -0.0019 0.0333  205 ILE A CG2   
1675 C  CD1   . ILE A 205 ? 0.398  0.3305 0.617  -0.0408 -0.004  0.039   205 ILE A CD1   
1676 N  N     . PHE A 206 ? 0.3847 0.3118 0.5704 -0.0404 -0.0042 0.0374  206 PHE A N     
1677 C  CA    . PHE A 206 ? 0.3925 0.3197 0.5701 -0.039  -0.0022 0.0349  206 PHE A CA    
1678 C  C     . PHE A 206 ? 0.408  0.3256 0.5754 -0.038  -0.0075 0.0354  206 PHE A C     
1679 O  O     . PHE A 206 ? 0.4091 0.3215 0.5758 -0.0396 -0.0128 0.0387  206 PHE A O     
1680 C  CB    . PHE A 206 ? 0.3871 0.3217 0.5675 -0.0408 0.0011  0.036   206 PHE A CB    
1681 C  CG    . PHE A 206 ? 0.3878 0.3316 0.5765 -0.0409 0.007   0.0349  206 PHE A CG    
1682 C  CD1   . PHE A 206 ? 0.3939 0.3399 0.5829 -0.0387 0.0109  0.0309  206 PHE A CD1   
1683 C  CD2   . PHE A 206 ? 0.3937 0.3439 0.59   -0.0432 0.0086  0.0379  206 PHE A CD2   
1684 C  CE1   . PHE A 206 ? 0.398  0.3517 0.5941 -0.0385 0.0159  0.0297  206 PHE A CE1   
1685 C  CE2   . PHE A 206 ? 0.397  0.3554 0.6005 -0.0428 0.0143  0.0367  206 PHE A CE2   
1686 C  CZ    . PHE A 206 ? 0.3926 0.3524 0.5956 -0.0404 0.0178  0.0324  206 PHE A CZ    
1687 N  N     . ALA A 207 ? 0.4183 0.3334 0.578  -0.0351 -0.0062 0.0321  207 ALA A N     
1688 C  CA    . ALA A 207 ? 0.4351 0.3409 0.5845 -0.0333 -0.0107 0.0321  207 ALA A CA    
1689 C  C     . ALA A 207 ? 0.4499 0.3553 0.5917 -0.0321 -0.0099 0.0307  207 ALA A C     
1690 O  O     . ALA A 207 ? 0.4594 0.3583 0.5927 -0.0294 -0.0119 0.0295  207 ALA A O     
1691 C  CB    . ALA A 207 ? 0.4386 0.3399 0.5848 -0.0304 -0.0108 0.03    207 ALA A CB    
1692 N  N     . GLU A 208 ? 0.4499 0.362  0.5945 -0.0338 -0.007  0.031   208 GLU A N     
1693 C  CA    . GLU A 208 ? 0.4592 0.3709 0.5967 -0.0328 -0.0065 0.0297  208 GLU A CA    
1694 C  C     . GLU A 208 ? 0.4683 0.3708 0.5972 -0.0321 -0.0123 0.0312  208 GLU A C     
1695 O  O     . GLU A 208 ? 0.4773 0.3759 0.5985 -0.0292 -0.0128 0.0292  208 GLU A O     
1696 C  CB    . GLU A 208 ? 0.482  0.4015 0.6232 -0.035  -0.003  0.0301  208 GLU A CB    
1697 C  CG    . GLU A 208 ? 0.523  0.4505 0.6691 -0.0345 0.0032  0.0273  208 GLU A CG    
1698 C  CD    . GLU A 208 ? 0.5676 0.5013 0.7234 -0.0366 0.0056  0.0288  208 GLU A CD    
1699 O  OE1   . GLU A 208 ? 0.572  0.5034 0.7318 -0.038  0.0025  0.0316  208 GLU A OE1   
1700 O  OE2   . GLU A 208 ? 0.5797 0.5203 0.739  -0.0367 0.0105  0.027   208 GLU A OE2   
1701 N  N     . ASP A 209 ? 0.4651 0.3642 0.5956 -0.0346 -0.017  0.0348  209 ASP A N     
1702 C  CA    . ASP A 209 ? 0.4753 0.365  0.5977 -0.0341 -0.0233 0.0363  209 ASP A CA    
1703 C  C     . ASP A 209 ? 0.4709 0.3513 0.5867 -0.031  -0.0267 0.0352  209 ASP A C     
1704 O  O     . ASP A 209 ? 0.4777 0.3513 0.5841 -0.0283 -0.0293 0.0342  209 ASP A O     
1705 C  CB    . ASP A 209 ? 0.5121 0.4004 0.6385 -0.0381 -0.0277 0.0408  209 ASP A CB    
1706 C  CG    . ASP A 209 ? 0.5916 0.4889 0.7237 -0.0411 -0.0243 0.0424  209 ASP A CG    
1707 O  OD1   . ASP A 209 ? 0.5996 0.5058 0.7403 -0.0423 -0.0193 0.0422  209 ASP A OD1   
1708 O  OD2   . ASP A 209 ? 0.6258 0.5211 0.7535 -0.0421 -0.0268 0.0438  209 ASP A OD2   
1709 N  N     . ASP A 210 ? 0.4594 0.3397 0.5798 -0.031  -0.0264 0.0353  210 ASP A N     
1710 C  CA    . ASP A 210 ? 0.4624 0.3339 0.5765 -0.028  -0.0295 0.0344  210 ASP A CA    
1711 C  C     . ASP A 210 ? 0.4553 0.3264 0.5629 -0.0237 -0.0261 0.0308  210 ASP A C     
1712 O  O     . ASP A 210 ? 0.4647 0.327  0.563  -0.0205 -0.0293 0.0302  210 ASP A O     
1713 C  CB    . ASP A 210 ? 0.4862 0.3585 0.6075 -0.0291 -0.0297 0.0353  210 ASP A CB    
1714 C  CG    . ASP A 210 ? 0.5496 0.4253 0.6805 -0.0335 -0.0316 0.0389  210 ASP A CG    
1715 O  OD1   . ASP A 210 ? 0.5547 0.44   0.6929 -0.0357 -0.0273 0.0393  210 ASP A OD1   
1716 O  OD2   . ASP A 210 ? 0.5833 0.4523 0.7144 -0.0347 -0.0373 0.0414  210 ASP A OD2   
1717 N  N     . ILE A 211 ? 0.4363 0.3166 0.5484 -0.0235 -0.0197 0.0286  211 ILE A N     
1718 C  CA    . ILE A 211 ? 0.4276 0.3088 0.535  -0.0197 -0.0161 0.0257  211 ILE A CA    
1719 C  C     . ILE A 211 ? 0.4036 0.2811 0.5023 -0.0177 -0.0177 0.0251  211 ILE A C     
1720 O  O     . ILE A 211 ? 0.4056 0.2773 0.4963 -0.0138 -0.0187 0.024   211 ILE A O     
1721 C  CB    . ILE A 211 ? 0.4406 0.3323 0.5557 -0.0204 -0.0096 0.0237  211 ILE A CB    
1722 C  CG1   . ILE A 211 ? 0.4637 0.3573 0.5857 -0.0212 -0.0083 0.0237  211 ILE A CG1   
1723 C  CG2   . ILE A 211 ? 0.4468 0.3404 0.5577 -0.0172 -0.0061 0.0211  211 ILE A CG2   
1724 C  CD1   . ILE A 211 ? 0.4917 0.3787 0.6088 -0.0182 -0.0099 0.0233  211 ILE A CD1   
1725 N  N     . ALA A 212 ? 0.3801 0.2602 0.48   -0.0201 -0.0183 0.0262  212 ALA A N     
1726 C  CA    . ALA A 212 ? 0.3699 0.2463 0.462  -0.0185 -0.0203 0.0259  212 ALA A CA    
1727 C  C     . ALA A 212 ? 0.3681 0.2328 0.4513 -0.0165 -0.0267 0.0271  212 ALA A C     
1728 O  O     . ALA A 212 ? 0.3745 0.2342 0.4493 -0.0126 -0.0274 0.0257  212 ALA A O     
1729 C  CB    . ALA A 212 ? 0.366  0.2471 0.4615 -0.0221 -0.0202 0.0274  212 ALA A CB    
1730 N  N     . ASP A 213 ? 0.3613 0.2212 0.4464 -0.0189 -0.0313 0.0296  213 ASP A N     
1731 C  CA    . ASP A 213 ? 0.3639 0.2114 0.4404 -0.0173 -0.0382 0.0308  213 ASP A CA    
1732 C  C     . ASP A 213 ? 0.3592 0.201  0.4286 -0.0125 -0.0378 0.0288  213 ASP A C     
1733 O  O     . ASP A 213 ? 0.3717 0.2042 0.4307 -0.009  -0.0415 0.0283  213 ASP A O     
1734 C  CB    . ASP A 213 ? 0.3826 0.2271 0.4642 -0.0211 -0.043  0.0341  213 ASP A CB    
1735 C  CG    . ASP A 213 ? 0.4449 0.2922 0.5312 -0.0256 -0.0453 0.0371  213 ASP A CG    
1736 O  OD1   . ASP A 213 ? 0.4558 0.3053 0.5395 -0.0255 -0.0442 0.0366  213 ASP A OD1   
1737 O  OD2   . ASP A 213 ? 0.4764 0.3238 0.5693 -0.0292 -0.0482 0.0402  213 ASP A OD2   
1738 N  N     . TYR A 214 ? 0.3361 0.1834 0.4111 -0.0122 -0.0333 0.0276  214 TYR A N     
1739 C  CA    . TYR A 214 ? 0.3242 0.1671 0.3935 -0.0079 -0.0322 0.026   214 TYR A CA    
1740 C  C     . TYR A 214 ? 0.3036 0.1477 0.3666 -0.0036 -0.0289 0.0238  214 TYR A C     
1741 O  O     . TYR A 214 ? 0.3093 0.145  0.3622 0.0007  -0.0311 0.0231  214 TYR A O     
1742 C  CB    . TYR A 214 ? 0.3224 0.1718 0.4002 -0.0091 -0.028  0.0255  214 TYR A CB    
1743 C  CG    . TYR A 214 ? 0.3414 0.1877 0.4138 -0.0048 -0.0261 0.024   214 TYR A CG    
1744 C  CD1   . TYR A 214 ? 0.3616 0.1975 0.427  -0.0027 -0.0306 0.0247  214 TYR A CD1   
1745 C  CD2   . TYR A 214 ? 0.3547 0.2082 0.4287 -0.0026 -0.0201 0.0221  214 TYR A CD2   
1746 C  CE1   . TYR A 214 ? 0.3806 0.2135 0.4403 0.0014  -0.0286 0.0235  214 TYR A CE1   
1747 C  CE2   . TYR A 214 ? 0.3722 0.2233 0.4416 0.0013  -0.0181 0.0211  214 TYR A CE2   
1748 C  CZ    . TYR A 214 ? 0.3926 0.2335 0.4547 0.0034  -0.0221 0.0219  214 TYR A CZ    
1749 O  OH    . TYR A 214 ? 0.4189 0.2574 0.4759 0.0074  -0.02   0.0212  214 TYR A OH    
1750 N  N     . ILE A 215 ? 0.2778 0.1318 0.3465 -0.0047 -0.0238 0.0227  215 ILE A N     
1751 C  CA    . ILE A 215 ? 0.2636 0.1201 0.3281 -0.001  -0.0204 0.0208  215 ILE A CA    
1752 C  C     . ILE A 215 ? 0.2639 0.1122 0.3183 0.0016  -0.0247 0.021   215 ILE A C     
1753 O  O     . ILE A 215 ? 0.2757 0.1195 0.3221 0.0065  -0.0245 0.0199  215 ILE A O     
1754 C  CB    . ILE A 215 ? 0.2601 0.1281 0.3328 -0.0034 -0.0152 0.0199  215 ILE A CB    
1755 C  CG1   . ILE A 215 ? 0.2673 0.1427 0.3488 -0.0049 -0.0107 0.0192  215 ILE A CG1   
1756 C  CG2   . ILE A 215 ? 0.268  0.1381 0.3366 -0.0001 -0.0128 0.0184  215 ILE A CG2   
1757 C  CD1   . ILE A 215 ? 0.2768 0.1625 0.3665 -0.0077 -0.0064 0.0184  215 ILE A CD1   
1758 N  N     . ILE A 216 ? 0.249  0.0953 0.3036 -0.0015 -0.0287 0.0225  216 ILE A N     
1759 C  CA    . ILE A 216 ? 0.2421 0.08   0.2874 0.0005  -0.0336 0.0228  216 ILE A CA    
1760 C  C     . ILE A 216 ? 0.2469 0.0722 0.282  0.0043  -0.0386 0.0229  216 ILE A C     
1761 O  O     . ILE A 216 ? 0.251  0.0704 0.2766 0.009   -0.0396 0.0218  216 ILE A O     
1762 C  CB    . ILE A 216 ? 0.236  0.0746 0.2847 -0.0043 -0.037  0.0249  216 ILE A CB    
1763 C  CG1   . ILE A 216 ? 0.2296 0.0797 0.2857 -0.0067 -0.0319 0.0243  216 ILE A CG1   
1764 C  CG2   . ILE A 216 ? 0.2502 0.0786 0.2891 -0.0025 -0.0433 0.0255  216 ILE A CG2   
1765 C  CD1   . ILE A 216 ? 0.2321 0.0854 0.2939 -0.0119 -0.0334 0.0264  216 ILE A CD1   
1766 N  N     . ALA A 217 ? 0.2438 0.065  0.2806 0.0025  -0.0414 0.0242  217 ALA A N     
1767 C  CA    . ALA A 217 ? 0.2553 0.0639 0.282  0.0059  -0.0464 0.0243  217 ALA A CA    
1768 C  C     . ALA A 217 ? 0.2635 0.0709 0.2839 0.0118  -0.0425 0.0222  217 ALA A C     
1769 O  O     . ALA A 217 ? 0.2699 0.0668 0.2785 0.0165  -0.0458 0.0216  217 ALA A O     
1770 C  CB    . ALA A 217 ? 0.2561 0.0617 0.2873 0.0025  -0.0497 0.0263  217 ALA A CB    
1771 N  N     . LYS A 218 ? 0.2611 0.0789 0.2888 0.0118  -0.0355 0.0213  218 LYS A N     
1772 C  CA    . LYS A 218 ? 0.2705 0.0886 0.2934 0.0171  -0.0312 0.0198  218 LYS A CA    
1773 C  C     . LYS A 218 ? 0.2774 0.0959 0.2944 0.0212  -0.0296 0.0185  218 LYS A C     
1774 O  O     . LYS A 218 ? 0.277  0.089  0.2841 0.0269  -0.0298 0.0178  218 LYS A O     
1775 C  CB    . LYS A 218 ? 0.286  0.1155 0.3193 0.0153  -0.0247 0.0193  218 LYS A CB    
1776 C  CG    . LYS A 218 ? 0.3452 0.1739 0.3836 0.0123  -0.0259 0.0204  218 LYS A CG    
1777 C  CD    . LYS A 218 ? 0.4112 0.2303 0.4407 0.0162  -0.0279 0.0204  218 LYS A CD    
1778 C  CE    . LYS A 218 ? 0.4561 0.2807 0.4867 0.0192  -0.0218 0.0196  218 LYS A CE    
1779 N  NZ    . LYS A 218 ? 0.4909 0.308  0.5161 0.0213  -0.0234 0.0201  218 LYS A NZ    
1780 N  N     . LEU A 219 ? 0.2838 0.1094 0.3064 0.0186  -0.0282 0.0184  219 LEU A N     
1781 C  CA    . LEU A 219 ? 0.305  0.1312 0.3229 0.022   -0.0272 0.0175  219 LEU A CA    
1782 C  C     . LEU A 219 ? 0.3306 0.1436 0.3359 0.0254  -0.0337 0.0175  219 LEU A C     
1783 O  O     . LEU A 219 ? 0.3339 0.1437 0.3315 0.0308  -0.0331 0.0165  219 LEU A O     
1784 C  CB    . LEU A 219 ? 0.3055 0.1406 0.3315 0.0177  -0.0257 0.0176  219 LEU A CB    
1785 C  CG    . LEU A 219 ? 0.3205 0.1683 0.3583 0.0144  -0.0197 0.0172  219 LEU A CG    
1786 C  CD1   . LEU A 219 ? 0.3232 0.1777 0.3672 0.0101  -0.0192 0.0174  219 LEU A CD1   
1787 C  CD2   . LEU A 219 ? 0.3298 0.1829 0.368  0.0183  -0.0141 0.0161  219 LEU A CD2   
1788 N  N     . GLN A 220 ? 0.3466 0.1518 0.3501 0.0223  -0.04   0.0189  220 GLN A N     
1789 C  CA    . GLN A 220 ? 0.3753 0.1669 0.3671 0.0249  -0.0473 0.0191  220 GLN A CA    
1790 C  C     . GLN A 220 ? 0.3976 0.178  0.3789 0.0298  -0.0497 0.0186  220 GLN A C     
1791 O  O     . GLN A 220 ? 0.4064 0.1742 0.3774 0.0319  -0.0563 0.0188  220 GLN A O     
1792 C  CB    . GLN A 220 ? 0.4064 0.1944 0.4016 0.0191  -0.0535 0.0213  220 GLN A CB    
1793 C  CG    . GLN A 220 ? 0.4593 0.2553 0.4619 0.0146  -0.0527 0.0221  220 GLN A CG    
1794 C  CD    . GLN A 220 ? 0.5392 0.3288 0.5335 0.0172  -0.0565 0.0217  220 GLN A CD    
1795 O  OE1   . GLN A 220 ? 0.5767 0.3611 0.5617 0.0233  -0.0563 0.02    220 GLN A OE1   
1796 N  NE2   . GLN A 220 ? 0.5433 0.3336 0.5409 0.0127  -0.06   0.0234  220 GLN A NE2   
1797 N  N     . HIS A 221 ? 0.4068 0.1914 0.3905 0.0313  -0.0448 0.0181  221 HIS A N     
1798 C  CA    . HIS A 221 ? 0.4318 0.2067 0.406  0.0356  -0.0465 0.0178  221 HIS A CA    
1799 C  C     . HIS A 221 ? 0.4515 0.2152 0.4222 0.0328  -0.0545 0.0192  221 HIS A C     
1800 O  O     . HIS A 221 ? 0.46   0.2102 0.4181 0.0368  -0.0598 0.0189  221 HIS A O     
1801 C  CB    . HIS A 221 ? 0.4542 0.222  0.4152 0.0436  -0.046  0.0163  221 HIS A CB    
1802 C  CG    . HIS A 221 ? 0.4972 0.2573 0.4491 0.0485  -0.0458 0.0159  221 HIS A CG    
1803 N  ND1   . HIS A 221 ? 0.5199 0.2878 0.4771 0.0489  -0.0394 0.016   221 HIS A ND1   
1804 C  CD2   . HIS A 221 ? 0.524  0.2689 0.4615 0.0531  -0.0514 0.0154  221 HIS A CD2   
1805 C  CE1   . HIS A 221 ? 0.5346 0.2923 0.4807 0.0537  -0.0411 0.0157  221 HIS A CE1   
1806 N  NE2   . HIS A 221 ? 0.542  0.2855 0.4756 0.0564  -0.0482 0.0153  221 HIS A NE2   
1807 N  N     . ARG A 222 ? 0.4574 0.2267 0.4393 0.026   -0.0556 0.0209  222 ARG A N     
1808 C  CA    . ARG A 222 ? 0.4809 0.2413 0.462  0.0225  -0.0632 0.0228  222 ARG A CA    
1809 C  C     . ARG A 222 ? 0.4939 0.2554 0.4802 0.0205  -0.0624 0.0236  222 ARG A C     
1810 O  O     . ARG A 222 ? 0.4877 0.2588 0.4804 0.0207  -0.0555 0.0228  222 ARG A O     
1811 C  CB    . ARG A 222 ? 0.4965 0.2606 0.4857 0.0165  -0.0663 0.0246  222 ARG A CB    
1812 C  CG    . ARG A 222 ? 0.5365 0.294  0.5173 0.0186  -0.0705 0.0243  222 ARG A CG    
1813 C  CD    . ARG A 222 ? 0.5714 0.3336 0.5604 0.0127  -0.0728 0.0264  222 ARG A CD    
1814 N  NE    . ARG A 222 ? 0.6143 0.3702 0.5952 0.0149  -0.0766 0.0259  222 ARG A NE    
1815 C  CZ    . ARG A 222 ? 0.6365 0.3978 0.6226 0.0113  -0.0769 0.027   222 ARG A CZ    
1816 N  NH1   . ARG A 222 ? 0.6301 0.4034 0.6294 0.0055  -0.0733 0.0286  222 ARG A NH1   
1817 N  NH2   . ARG A 222 ? 0.6334 0.388  0.6113 0.0136  -0.0807 0.0266  222 ARG A NH2   
1818 N  N     . ASP A 223 ? 0.5119 0.2631 0.495  0.0187  -0.0698 0.0252  223 ASP A N     
1819 C  CA    . ASP A 223 ? 0.5299 0.2807 0.5174 0.0167  -0.0702 0.0262  223 ASP A CA    
1820 C  C     . ASP A 223 ? 0.5256 0.2898 0.53   0.0101  -0.0668 0.0277  223 ASP A C     
1821 O  O     . ASP A 223 ? 0.5274 0.2929 0.538  0.0054  -0.0704 0.0297  223 ASP A O     
1822 C  CB    . ASP A 223 ? 0.5746 0.31   0.5541 0.0164  -0.0798 0.0277  223 ASP A CB    
1823 C  CG    . ASP A 223 ? 0.6606 0.3934 0.6416 0.0157  -0.0805 0.0283  223 ASP A CG    
1824 O  OD1   . ASP A 223 ? 0.6621 0.4021 0.656  0.0102  -0.0801 0.0302  223 ASP A OD1   
1825 O  OD2   . ASP A 223 ? 0.7115 0.4348 0.6805 0.021   -0.0814 0.0271  223 ASP A OD2   
1826 N  N     . THR A 224 ? 0.5184 0.2922 0.5301 0.01    -0.0599 0.0269  224 THR A N     
1827 C  CA    . THR A 224 ? 0.5156 0.3021 0.5426 0.0045  -0.0561 0.0279  224 THR A CA    
1828 C  C     . THR A 224 ? 0.5153 0.3009 0.5487 0.0013  -0.0583 0.0295  224 THR A C     
1829 O  O     . THR A 224 ? 0.5076 0.3037 0.5538 -0.0028 -0.0548 0.0303  224 THR A O     
1830 C  CB    . THR A 224 ? 0.5271 0.326  0.5594 0.0058  -0.0472 0.0259  224 THR A CB    
1831 O  OG1   . THR A 224 ? 0.5435 0.3398 0.5695 0.0105  -0.0443 0.0245  224 THR A OG1   
1832 C  CG2   . THR A 224 ? 0.5282 0.3309 0.5585 0.0071  -0.045  0.0248  224 THR A CG2   
1833 N  N     . SER A 225 ? 0.5201 0.2932 0.5449 0.0032  -0.0641 0.0301  225 SER A N     
1834 C  CA    . SER A 225 ? 0.52   0.2912 0.5504 0.0004  -0.0667 0.0318  225 SER A CA    
1835 C  C     . SER A 225 ? 0.5115 0.2894 0.5558 -0.0061 -0.0684 0.0344  225 SER A C     
1836 O  O     . SER A 225 ? 0.5088 0.2944 0.5638 -0.0087 -0.0653 0.035   225 SER A O     
1837 C  CB    . SER A 225 ? 0.5483 0.3032 0.5663 0.003   -0.0746 0.0324  225 SER A CB    
1838 O  OG    . SER A 225 ? 0.5882 0.3364 0.5926 0.0094  -0.0729 0.0301  225 SER A OG    
1839 N  N     . ASN A 226 ? 0.5062 0.2815 0.5506 -0.0085 -0.0732 0.0361  226 ASN A N     
1840 C  CA    . ASN A 226 ? 0.4985 0.2801 0.5558 -0.0145 -0.0749 0.0392  226 ASN A CA    
1841 C  C     . ASN A 226 ? 0.4752 0.2729 0.5448 -0.017  -0.0668 0.0386  226 ASN A C     
1842 O  O     . ASN A 226 ? 0.4697 0.2753 0.5517 -0.0209 -0.0652 0.0402  226 ASN A O     
1843 C  CB    . ASN A 226 ? 0.527  0.3006 0.5805 -0.0164 -0.0827 0.0415  226 ASN A CB    
1844 C  CG    . ASN A 226 ? 0.5915 0.3488 0.6347 -0.015  -0.0919 0.0427  226 ASN A CG    
1845 O  OD1   . ASN A 226 ? 0.6108 0.3626 0.6501 -0.0129 -0.0928 0.0419  226 ASN A OD1   
1846 N  ND2   . ASN A 226 ? 0.6131 0.3618 0.6512 -0.0161 -0.0993 0.0446  226 ASN A ND2   
1847 N  N     . ILE A 227 ? 0.4589 0.2613 0.5247 -0.0144 -0.0617 0.0361  227 ILE A N     
1848 C  CA    . ILE A 227 ? 0.4379 0.2547 0.5139 -0.0163 -0.0542 0.0353  227 ILE A CA    
1849 C  C     . ILE A 227 ? 0.4158 0.2395 0.4983 -0.0159 -0.0486 0.0338  227 ILE A C     
1850 O  O     . ILE A 227 ? 0.4129 0.2466 0.507  -0.0191 -0.0448 0.0344  227 ILE A O     
1851 C  CB    . ILE A 227 ? 0.4455 0.2648 0.5156 -0.0136 -0.0507 0.0331  227 ILE A CB    
1852 C  CG1   . ILE A 227 ? 0.4629 0.2734 0.525  -0.0134 -0.0571 0.0343  227 ILE A CG1   
1853 C  CG2   . ILE A 227 ? 0.4443 0.2776 0.5248 -0.0162 -0.044  0.0325  227 ILE A CG2   
1854 C  CD1   . ILE A 227 ? 0.4807 0.2918 0.5356 -0.0102 -0.0547 0.0323  227 ILE A CD1   
1855 N  N     . GLU A 228 ? 0.3993 0.2169 0.4738 -0.0118 -0.0483 0.0322  228 GLU A N     
1856 C  CA    . GLU A 228 ? 0.3815 0.2041 0.4608 -0.0111 -0.0436 0.031   228 GLU A CA    
1857 C  C     . GLU A 228 ? 0.3746 0.1983 0.4635 -0.0149 -0.046  0.0332  228 GLU A C     
1858 O  O     . GLU A 228 ? 0.3682 0.2016 0.4675 -0.0168 -0.0412 0.0328  228 GLU A O     
1859 C  CB    . GLU A 228 ? 0.3956 0.2095 0.4632 -0.006  -0.0441 0.0296  228 GLU A CB    
1860 C  CG    . GLU A 228 ? 0.4275 0.2432 0.4879 -0.0017 -0.0397 0.0273  228 GLU A CG    
1861 C  CD    . GLU A 228 ? 0.4673 0.2733 0.5147 0.0037  -0.0408 0.0264  228 GLU A CD    
1862 O  OE1   . GLU A 228 ? 0.4781 0.2794 0.5241 0.0043  -0.0423 0.0269  228 GLU A OE1   
1863 O  OE2   . GLU A 228 ? 0.468  0.271  0.5063 0.0076  -0.0402 0.0252  228 GLU A OE2   
1864 N  N     . GLN A 229 ? 0.3725 0.1866 0.4585 -0.0163 -0.0536 0.0356  229 GLN A N     
1865 C  CA    . GLN A 229 ? 0.3694 0.1841 0.4649 -0.02   -0.0565 0.038   229 GLN A CA    
1866 C  C     . GLN A 229 ? 0.3578 0.1843 0.4675 -0.0245 -0.0537 0.0396  229 GLN A C     
1867 O  O     . GLN A 229 ? 0.3511 0.1839 0.4714 -0.0267 -0.0517 0.0403  229 GLN A O     
1868 C  CB    . GLN A 229 ? 0.3963 0.1976 0.4855 -0.0205 -0.0659 0.0405  229 GLN A CB    
1869 C  CG    . GLN A 229 ? 0.4416 0.2418 0.5386 -0.0231 -0.069  0.0426  229 GLN A CG    
1870 C  CD    . GLN A 229 ? 0.5105 0.3123 0.6075 -0.0208 -0.0648 0.0406  229 GLN A CD    
1871 O  OE1   . GLN A 229 ? 0.5349 0.3283 0.62   -0.0167 -0.0655 0.0389  229 GLN A OE1   
1872 N  NE2   . GLN A 229 ? 0.5224 0.3349 0.6324 -0.0232 -0.0601 0.0407  229 GLN A NE2   
1873 N  N     . LEU A 230 ? 0.3547 0.1845 0.4645 -0.0257 -0.0532 0.0401  230 LEU A N     
1874 C  CA    . LEU A 230 ? 0.3515 0.1927 0.4736 -0.0296 -0.0499 0.0416  230 LEU A CA    
1875 C  C     . LEU A 230 ? 0.3464 0.1991 0.4753 -0.029  -0.0415 0.039   230 LEU A C     
1876 O  O     . LEU A 230 ? 0.343  0.2038 0.4833 -0.0317 -0.0389 0.0399  230 LEU A O     
1877 C  CB    . LEU A 230 ? 0.3579 0.1999 0.4771 -0.0306 -0.0507 0.0423  230 LEU A CB    
1878 C  CG    . LEU A 230 ? 0.3872 0.22   0.5028 -0.0324 -0.0591 0.0456  230 LEU A CG    
1879 C  CD1   . LEU A 230 ? 0.4004 0.2346 0.5129 -0.0331 -0.0592 0.0461  230 LEU A CD1   
1880 C  CD2   . LEU A 230 ? 0.3918 0.2269 0.5189 -0.0368 -0.0623 0.0496  230 LEU A CD2   
1881 N  N     . LEU A 231 ? 0.3455 0.1986 0.4673 -0.0254 -0.0375 0.0357  231 LEU A N     
1882 C  CA    . LEU A 231 ? 0.3461 0.209  0.4731 -0.0246 -0.0301 0.0331  231 LEU A CA    
1883 C  C     . LEU A 231 ? 0.3459 0.2098 0.4782 -0.0245 -0.0288 0.0327  231 LEU A C     
1884 O  O     . LEU A 231 ? 0.3402 0.2132 0.4818 -0.0258 -0.024  0.0319  231 LEU A O     
1885 C  CB    . LEU A 231 ? 0.3517 0.2138 0.4696 -0.0209 -0.027  0.0303  231 LEU A CB    
1886 C  CG    . LEU A 231 ? 0.3715 0.2354 0.4862 -0.0212 -0.0268 0.0303  231 LEU A CG    
1887 C  CD1   . LEU A 231 ? 0.3795 0.2406 0.4842 -0.0171 -0.0251 0.028   231 LEU A CD1   
1888 C  CD2   . LEU A 231 ? 0.3746 0.25   0.499  -0.024  -0.0218 0.03    231 LEU A CD2   
1889 N  N     . ILE A 232 ? 0.3452 0.1993 0.4714 -0.023  -0.0334 0.0334  232 ILE A N     
1890 C  CA    . ILE A 232 ? 0.3429 0.1964 0.4732 -0.0229 -0.0332 0.0333  232 ILE A CA    
1891 C  C     . ILE A 232 ? 0.3393 0.1973 0.482  -0.0269 -0.0347 0.0358  232 ILE A C     
1892 O  O     . ILE A 232 ? 0.338  0.2028 0.4896 -0.0278 -0.031  0.0352  232 ILE A O     
1893 C  CB    . ILE A 232 ? 0.3556 0.1964 0.4749 -0.0202 -0.0384 0.0337  232 ILE A CB    
1894 C  CG1   . ILE A 232 ? 0.3707 0.2084 0.4786 -0.0157 -0.0357 0.0312  232 ILE A CG1   
1895 C  CG2   . ILE A 232 ? 0.3623 0.201  0.486  -0.0209 -0.0399 0.0345  232 ILE A CG2   
1896 C  CD1   . ILE A 232 ? 0.3798 0.2264 0.4917 -0.0144 -0.0285 0.029   232 ILE A CD1   
1897 N  N     . ASN A 233 ? 0.3334 0.1879 0.477  -0.0293 -0.0399 0.0387  233 ASN A N     
1898 C  CA    . ASN A 233 ? 0.3236 0.1827 0.4795 -0.0332 -0.0415 0.0417  233 ASN A CA    
1899 C  C     . ASN A 233 ? 0.3081 0.1807 0.4747 -0.0348 -0.0346 0.0409  233 ASN A C     
1900 O  O     . ASN A 233 ? 0.3031 0.1815 0.4804 -0.0365 -0.033  0.0419  233 ASN A O     
1901 C  CB    . ASN A 233 ? 0.3341 0.1873 0.4885 -0.0356 -0.0483 0.0453  233 ASN A CB    
1902 C  CG    . ASN A 233 ? 0.3726 0.2121 0.5189 -0.0348 -0.0563 0.0467  233 ASN A CG    
1903 O  OD1   . ASN A 233 ? 0.3762 0.2109 0.5193 -0.0328 -0.057  0.0455  233 ASN A OD1   
1904 N  ND2   . ASN A 233 ? 0.3915 0.224  0.5338 -0.0362 -0.0628 0.0493  233 ASN A ND2   
1905 N  N     . LYS A 234 ? 0.2979 0.1751 0.4612 -0.0339 -0.0304 0.0391  234 LYS A N     
1906 C  CA    . LYS A 234 ? 0.285  0.1742 0.4567 -0.035  -0.0238 0.038   234 LYS A CA    
1907 C  C     . LYS A 234 ? 0.281  0.1752 0.4563 -0.0333 -0.0186 0.035   234 LYS A C     
1908 O  O     . LYS A 234 ? 0.2752 0.1776 0.4605 -0.0346 -0.0149 0.0349  234 LYS A O     
1909 C  CB    . LYS A 234 ? 0.2956 0.187  0.4615 -0.0344 -0.0216 0.0368  234 LYS A CB    
1910 C  CG    . LYS A 234 ? 0.3266 0.2151 0.4914 -0.0367 -0.0262 0.0401  234 LYS A CG    
1911 C  CD    . LYS A 234 ? 0.3674 0.258  0.5268 -0.0363 -0.0242 0.0391  234 LYS A CD    
1912 C  CE    . LYS A 234 ? 0.4183 0.3052 0.5766 -0.0388 -0.0295 0.0428  234 LYS A CE    
1913 N  NZ    . LYS A 234 ? 0.4509 0.3435 0.6086 -0.0397 -0.0265 0.0427  234 LYS A NZ    
1914 N  N     . ASN A 235 ? 0.2818 0.1706 0.4489 -0.0304 -0.0186 0.0328  235 ASN A N     
1915 C  CA    . ASN A 235 ? 0.2795 0.1715 0.4491 -0.0288 -0.0145 0.0303  235 ASN A CA    
1916 C  C     . ASN A 235 ? 0.2751 0.167  0.4532 -0.0303 -0.0164 0.0318  235 ASN A C     
1917 O  O     . ASN A 235 ? 0.2724 0.1709 0.4585 -0.0306 -0.0125 0.0306  235 ASN A O     
1918 C  CB    . ASN A 235 ? 0.2956 0.1806 0.4541 -0.0255 -0.0152 0.0287  235 ASN A CB    
1919 C  CG    . ASN A 235 ? 0.336  0.2251 0.4959 -0.0237 -0.0104 0.0261  235 ASN A CG    
1920 O  OD1   . ASN A 235 ? 0.3537 0.2488 0.5225 -0.0248 -0.0076 0.0254  235 ASN A OD1   
1921 N  ND2   . ASN A 235 ? 0.3487 0.2347 0.4998 -0.0208 -0.0093 0.0246  235 ASN A ND2   
1922 N  N     . LEU A 236 ? 0.2672 0.1513 0.4438 -0.0313 -0.0227 0.0346  236 LEU A N     
1923 C  CA    . LEU A 236 ? 0.2559 0.139  0.4404 -0.0329 -0.0254 0.0365  236 LEU A CA    
1924 C  C     . LEU A 236 ? 0.2544 0.1465 0.4517 -0.0357 -0.0236 0.0383  236 LEU A C     
1925 O  O     . LEU A 236 ? 0.2531 0.1492 0.4596 -0.0364 -0.0223 0.0385  236 LEU A O     
1926 C  CB    . LEU A 236 ? 0.2545 0.1261 0.4329 -0.0332 -0.0331 0.0391  236 LEU A CB    
1927 C  CG    . LEU A 236 ? 0.2612 0.1301 0.446  -0.0344 -0.0367 0.0409  236 LEU A CG    
1928 C  CD1   . LEU A 236 ? 0.2641 0.1316 0.4467 -0.0321 -0.0344 0.0385  236 LEU A CD1   
1929 C  CD2   . LEU A 236 ? 0.2754 0.1331 0.4547 -0.0351 -0.0448 0.0438  236 LEU A CD2   
1930 N  N     . LYS A 237 ? 0.2565 0.1521 0.4548 -0.0372 -0.0233 0.0397  237 LYS A N     
1931 C  CA    . LYS A 237 ? 0.2574 0.1624 0.4676 -0.0397 -0.0207 0.0416  237 LYS A CA    
1932 C  C     . LYS A 237 ? 0.2506 0.1653 0.466  -0.0385 -0.0132 0.0384  237 LYS A C     
1933 O  O     . LYS A 237 ? 0.2423 0.164  0.4686 -0.0396 -0.0108 0.0392  237 LYS A O     
1934 C  CB    . LYS A 237 ? 0.2867 0.1927 0.4959 -0.0416 -0.0223 0.0441  237 LYS A CB    
1935 C  CG    . LYS A 237 ? 0.355  0.2523 0.5622 -0.0435 -0.0303 0.0481  237 LYS A CG    
1936 C  CD    . LYS A 237 ? 0.4131 0.3108 0.6192 -0.0456 -0.0325 0.051   237 LYS A CD    
1937 C  CE    . LYS A 237 ? 0.4535 0.3469 0.6471 -0.0437 -0.0323 0.0487  237 LYS A CE    
1938 N  NZ    . LYS A 237 ? 0.4655 0.3557 0.6565 -0.0459 -0.0368 0.052   237 LYS A NZ    
1939 N  N     . MET A 238 ? 0.2515 0.1662 0.4595 -0.0362 -0.0097 0.0347  238 MET A N     
1940 C  CA    . MET A 238 ? 0.2502 0.1727 0.4624 -0.035  -0.0034 0.0315  238 MET A CA    
1941 C  C     . MET A 238 ? 0.2544 0.1768 0.4725 -0.0344 -0.0031 0.0307  238 MET A C     
1942 O  O     . MET A 238 ? 0.2516 0.1811 0.4784 -0.0346 0.0006  0.0298  238 MET A O     
1943 C  CB    . MET A 238 ? 0.2516 0.1736 0.4547 -0.0329 -0.0005 0.0283  238 MET A CB    
1944 C  CG    . MET A 238 ? 0.2626 0.1915 0.4695 -0.0318 0.0052  0.025   238 MET A CG    
1945 S  SD    . MET A 238 ? 0.2754 0.2146 0.4914 -0.0331 0.0098  0.0251  238 MET A SD    
1946 C  CE    . MET A 238 ? 0.2641 0.2042 0.4718 -0.033  0.0113  0.0243  238 MET A CE    
1947 N  N     . VAL A 239 ? 0.2551 0.1691 0.4685 -0.0337 -0.0075 0.0313  239 VAL A N     
1948 C  CA    . VAL A 239 ? 0.2531 0.1655 0.4713 -0.0334 -0.0085 0.0311  239 VAL A CA    
1949 C  C     . VAL A 239 ? 0.2581 0.1741 0.4881 -0.0356 -0.01   0.034   239 VAL A C     
1950 O  O     . VAL A 239 ? 0.2594 0.1794 0.4975 -0.0354 -0.008  0.0332  239 VAL A O     
1951 C  CB    . VAL A 239 ? 0.2598 0.1615 0.469  -0.0323 -0.0134 0.0317  239 VAL A CB    
1952 C  CG1   . VAL A 239 ? 0.2627 0.1618 0.477  -0.0324 -0.0155 0.0322  239 VAL A CG1   
1953 C  CG2   . VAL A 239 ? 0.2691 0.1684 0.4678 -0.0298 -0.0112 0.0291  239 VAL A CG2   
1954 N  N     . GLU A 240 ? 0.2613 0.176  0.4926 -0.0376 -0.0136 0.0374  240 GLU A N     
1955 C  CA    . GLU A 240 ? 0.2664 0.1852 0.5096 -0.0398 -0.015  0.0407  240 GLU A CA    
1956 C  C     . GLU A 240 ? 0.2661 0.1964 0.5181 -0.0399 -0.0086 0.0398  240 GLU A C     
1957 O  O     . GLU A 240 ? 0.2678 0.2031 0.5302 -0.0401 -0.0071 0.0403  240 GLU A O     
1958 C  CB    . GLU A 240 ? 0.3011 0.2158 0.5434 -0.0422 -0.0206 0.0449  240 GLU A CB    
1959 C  CG    . GLU A 240 ? 0.3531 0.2718 0.6086 -0.0446 -0.0228 0.049   240 GLU A CG    
1960 C  CD    . GLU A 240 ? 0.4386 0.3536 0.6948 -0.0474 -0.0287 0.0537  240 GLU A CD    
1961 O  OE1   . GLU A 240 ? 0.4781 0.3873 0.7239 -0.0474 -0.0312 0.0537  240 GLU A OE1   
1962 O  OE2   . GLU A 240 ? 0.4553 0.373  0.7225 -0.0495 -0.0312 0.0576  240 GLU A OE2   
1963 N  N     . PHE A 241 ? 0.2634 0.1976 0.511  -0.0394 -0.0047 0.0383  241 PHE A N     
1964 C  CA    . PHE A 241 ? 0.2662 0.2107 0.5204 -0.0391 0.0015  0.0371  241 PHE A CA    
1965 C  C     . PHE A 241 ? 0.2689 0.2167 0.5267 -0.0371 0.0057  0.0335  241 PHE A C     
1966 O  O     . PHE A 241 ? 0.2681 0.2227 0.5357 -0.037  0.0087  0.0337  241 PHE A O     
1967 C  CB    . PHE A 241 ? 0.271  0.2175 0.5175 -0.0388 0.0044  0.0357  241 PHE A CB    
1968 C  CG    . PHE A 241 ? 0.278  0.2337 0.5284 -0.0378 0.0112  0.0334  241 PHE A CG    
1969 C  CD1   . PHE A 241 ? 0.2806 0.244  0.5404 -0.0389 0.0138  0.0357  241 PHE A CD1   
1970 C  CD2   . PHE A 241 ? 0.2909 0.2474 0.5356 -0.0358 0.015   0.029   241 PHE A CD2   
1971 C  CE1   . PHE A 241 ? 0.2864 0.2577 0.5487 -0.0376 0.0201  0.0335  241 PHE A CE1   
1972 C  CE2   . PHE A 241 ? 0.2967 0.2607 0.5442 -0.0347 0.0208  0.0267  241 PHE A CE2   
1973 C  CZ    . PHE A 241 ? 0.2885 0.2595 0.5443 -0.0355 0.0233  0.0288  241 PHE A CZ    
1974 N  N     . LEU A 242 ? 0.2714 0.2144 0.5215 -0.0354 0.0056  0.0304  242 LEU A N     
1975 C  CA    . LEU A 242 ? 0.2743 0.2196 0.5269 -0.0336 0.009   0.027   242 LEU A CA    
1976 C  C     . LEU A 242 ? 0.2698 0.2136 0.5301 -0.0338 0.0066  0.0281  242 LEU A C     
1977 O  O     . LEU A 242 ? 0.2769 0.2261 0.5448 -0.033  0.0099  0.0266  242 LEU A O     
1978 C  CB    . LEU A 242 ? 0.2853 0.2261 0.5279 -0.0321 0.0093  0.024   242 LEU A CB    
1979 C  CG    . LEU A 242 ? 0.3081 0.2507 0.5433 -0.0315 0.0121  0.0224  242 LEU A CG    
1980 C  CD1   . LEU A 242 ? 0.3184 0.2559 0.5442 -0.0301 0.0115  0.0204  242 LEU A CD1   
1981 C  CD2   . LEU A 242 ? 0.3153 0.266  0.5549 -0.0309 0.0176  0.02    242 LEU A CD2   
1982 N  N     . SER A 243 ? 0.2583 0.1945 0.5165 -0.0348 0.0009  0.0305  243 SER A N     
1983 C  CA    . SER A 243 ? 0.2541 0.1881 0.519  -0.0349 -0.0018 0.0315  243 SER A CA    
1984 C  C     . SER A 243 ? 0.2506 0.1906 0.5284 -0.0362 -0.0017 0.0342  243 SER A C     
1985 O  O     . SER A 243 ? 0.2471 0.1894 0.533  -0.0356 -0.001  0.0337  243 SER A O     
1986 C  CB    . SER A 243 ? 0.2625 0.1861 0.5206 -0.0354 -0.0081 0.0332  243 SER A CB    
1987 O  OG    . SER A 243 ? 0.276  0.1957 0.531  -0.037  -0.0123 0.0364  243 SER A OG    
1988 N  N     . LYS A 244 ? 0.248  0.1909 0.5279 -0.0378 -0.0022 0.0372  244 LYS A N     
1989 C  CA    . LYS A 244 ? 0.2431 0.193  0.5358 -0.039  -0.0016 0.0403  244 LYS A CA    
1990 C  C     . LYS A 244 ? 0.247  0.2071 0.5462 -0.0374 0.0057  0.038   244 LYS A C     
1991 O  O     . LYS A 244 ? 0.2394 0.2061 0.5501 -0.0376 0.0073  0.04    244 LYS A O     
1992 C  CB    . LYS A 244 ? 0.2522 0.2017 0.5456 -0.0416 -0.0049 0.0449  244 LYS A CB    
1993 C  CG    . LYS A 244 ? 0.2827 0.2218 0.572  -0.0432 -0.0129 0.0476  244 LYS A CG    
1994 C  CD    . LYS A 244 ? 0.3171 0.2558 0.6094 -0.046  -0.0171 0.0526  244 LYS A CD    
1995 C  CE    . LYS A 244 ? 0.3571 0.2853 0.6468 -0.0475 -0.0255 0.0554  244 LYS A CE    
1996 N  NZ    . LYS A 244 ? 0.3817 0.3094 0.6759 -0.0506 -0.0303 0.0608  244 LYS A NZ    
1997 N  N     . ASN A 245 ? 0.2575 0.2188 0.5496 -0.0355 0.0101  0.0337  245 ASN A N     
1998 C  CA    . ASN A 245 ? 0.2661 0.2354 0.5623 -0.0336 0.0166  0.0308  245 ASN A CA    
1999 C  C     . ASN A 245 ? 0.2778 0.2461 0.5754 -0.0314 0.018   0.027   245 ASN A C     
2000 O  O     . ASN A 245 ? 0.2717 0.2456 0.5723 -0.0295 0.023   0.0242  245 ASN A O     
2001 C  CB    . ASN A 245 ? 0.2808 0.2524 0.5688 -0.0331 0.0203  0.0288  245 ASN A CB    
2002 C  CG    . ASN A 245 ? 0.3174 0.2938 0.6078 -0.0347 0.0212  0.0323  245 ASN A CG    
2003 O  OD1   . ASN A 245 ? 0.3196 0.2999 0.6195 -0.0358 0.0204  0.0361  245 ASN A OD1   
2004 N  ND2   . ASN A 245 ? 0.3327 0.3092 0.6148 -0.0348 0.0228  0.0313  245 ASN A ND2   
2005 N  N     . THR A 246 ? 0.2956 0.2565 0.5908 -0.0317 0.0136  0.027   246 THR A N     
2006 C  CA    . THR A 246 ? 0.3182 0.2777 0.615  -0.03   0.0143  0.0239  246 THR A CA    
2007 C  C     . THR A 246 ? 0.3367 0.2958 0.6438 -0.0304 0.0115  0.0261  246 THR A C     
2008 O  O     . THR A 246 ? 0.3372 0.2946 0.648  -0.0323 0.0074  0.0301  246 THR A O     
2009 C  CB    . THR A 246 ? 0.3421 0.294  0.6282 -0.0298 0.0121  0.022   246 THR A CB    
2010 O  OG1   . THR A 246 ? 0.3599 0.3045 0.6422 -0.0314 0.0065  0.0251  246 THR A OG1   
2011 C  CG2   . THR A 246 ? 0.3491 0.3019 0.6261 -0.0291 0.0152  0.0196  246 THR A CG2   
2012 N  N     . LYS A 247 ? 0.345  0.3056 0.6572 -0.0286 0.0133  0.0234  247 LYS A N     
2013 C  CA    . LYS A 247 ? 0.3554 0.3157 0.6777 -0.0287 0.0107  0.0251  247 LYS A CA    
2014 C  C     . LYS A 247 ? 0.3731 0.3242 0.691  -0.0302 0.0044  0.0268  247 LYS A C     
2015 O  O     . LYS A 247 ? 0.3794 0.325  0.6889 -0.0297 0.0037  0.0246  247 LYS A O     
2016 C  CB    . LYS A 247 ? 0.3773 0.3412 0.7056 -0.0262 0.0141  0.0217  247 LYS A CB    
2017 C  CG    . LYS A 247 ? 0.4488 0.4162 0.7721 -0.0242 0.0195  0.0174  247 LYS A CG    
2018 C  CD    . LYS A 247 ? 0.5258 0.487  0.8402 -0.0238 0.0185  0.0143  247 LYS A CD    
2019 C  CE    . LYS A 247 ? 0.5755 0.5377 0.8807 -0.0233 0.0218  0.0116  247 LYS A CE    
2020 N  NZ    . LYS A 247 ? 0.6055 0.5656 0.9033 -0.0251 0.0202  0.0139  247 LYS A NZ    
2021 N  N     . ASN A 248 ? 0.3789 0.3281 0.7023 -0.032  -0.0001 0.031   248 ASN A N     
2022 C  CA    . ASN A 248 ? 0.3958 0.3356 0.7148 -0.0335 -0.0067 0.0332  248 ASN A CA    
2023 C  C     . ASN A 248 ? 0.3975 0.3326 0.7176 -0.0327 -0.0087 0.0317  248 ASN A C     
2024 O  O     . ASN A 248 ? 0.4052 0.3318 0.7177 -0.0333 -0.0131 0.0323  248 ASN A O     
2025 C  CB    . ASN A 248 ? 0.4239 0.3635 0.7503 -0.0357 -0.0112 0.0381  248 ASN A CB    
2026 C  CG    . ASN A 248 ? 0.4842 0.4295 0.8124 -0.0367 -0.0094 0.0404  248 ASN A CG    
2027 O  OD1   . ASN A 248 ? 0.4952 0.4465 0.8347 -0.0376 -0.0093 0.0436  248 ASN A OD1   
2028 N  ND2   . ASN A 248 ? 0.5008 0.4448 0.8183 -0.0367 -0.0077 0.039   248 ASN A ND2   
2029 N  N     . ASP A 249 ? 0.3889 0.3294 0.7181 -0.0311 -0.0057 0.0299  249 ASP A N     
2030 C  CA    . ASP A 249 ? 0.3903 0.327  0.7221 -0.0304 -0.0077 0.0286  249 ASP A CA    
2031 C  C     . ASP A 249 ? 0.3947 0.3251 0.7156 -0.0298 -0.008  0.026   249 ASP A C     
2032 O  O     . ASP A 249 ? 0.3981 0.3219 0.7175 -0.0303 -0.0121 0.0267  249 ASP A O     
2033 C  CB    . ASP A 249 ? 0.4024 0.3466 0.7452 -0.0284 -0.0036 0.0266  249 ASP A CB    
2034 N  N     . ASN A 250 ? 0.393  0.3256 0.7065 -0.0289 -0.0038 0.0232  250 ASN A N     
2035 C  CA    . ASN A 250 ? 0.3991 0.3268 0.703  -0.0283 -0.0036 0.021   250 ASN A CA    
2036 C  C     . ASN A 250 ? 0.4015 0.3266 0.6935 -0.0287 -0.0032 0.0211  250 ASN A C     
2037 O  O     . ASN A 250 ? 0.4074 0.3303 0.6917 -0.0281 -0.0019 0.0192  250 ASN A O     
2038 C  CB    . ASN A 250 ? 0.4079 0.3399 0.7144 -0.0266 0.0007  0.0171  250 ASN A CB    
2039 C  CG    . ASN A 250 ? 0.4421 0.3813 0.7486 -0.0255 0.006   0.0148  250 ASN A CG    
2040 O  OD1   . ASN A 250 ? 0.4646 0.4037 0.7629 -0.0252 0.0082  0.0131  250 ASN A OD1   
2041 N  ND2   . ASN A 250 ? 0.4349 0.3805 0.7505 -0.0249 0.0082  0.0151  250 ASN A ND2   
2042 N  N     . ASN A 251 ? 0.3933 0.3187 0.684  -0.0298 -0.0045 0.0235  251 ASN A N     
2043 C  CA    . ASN A 251 ? 0.3976 0.3202 0.6775 -0.0301 -0.0046 0.0239  251 ASN A CA    
2044 C  C     . ASN A 251 ? 0.3885 0.3053 0.666  -0.0317 -0.01   0.0277  251 ASN A C     
2045 O  O     . ASN A 251 ? 0.3871 0.305  0.6732 -0.0328 -0.0125 0.0301  251 ASN A O     
2046 C  CB    . ASN A 251 ? 0.4179 0.3478 0.698  -0.0298 0.0002  0.0225  251 ASN A CB    
2047 C  CG    . ASN A 251 ? 0.4658 0.4017 0.7488 -0.0282 0.0054  0.0188  251 ASN A CG    
2048 O  OD1   . ASN A 251 ? 0.4755 0.4177 0.7671 -0.0276 0.0081  0.0181  251 ASN A OD1   
2049 N  ND2   . ASN A 251 ? 0.4834 0.4173 0.7591 -0.0273 0.0068  0.0164  251 ASN A ND2   
2050 N  N     . PHE A 252 ? 0.3806 0.2914 0.6466 -0.0317 -0.0119 0.0282  252 PHE A N     
2051 C  CA    . PHE A 252 ? 0.3765 0.2806 0.6386 -0.033  -0.0175 0.0316  252 PHE A CA    
2052 C  C     . PHE A 252 ? 0.3658 0.2753 0.6341 -0.0345 -0.0172 0.0336  252 PHE A C     
2053 O  O     . PHE A 252 ? 0.3663 0.2827 0.6355 -0.0341 -0.0124 0.0321  252 PHE A O     
2054 C  CB    . PHE A 252 ? 0.3814 0.2787 0.6293 -0.0322 -0.0188 0.0313  252 PHE A CB    
2055 C  CG    . PHE A 252 ? 0.3967 0.2853 0.6362 -0.0312 -0.0216 0.0313  252 PHE A CG    
2056 C  CD1   . PHE A 252 ? 0.4102 0.2971 0.6547 -0.0312 -0.0229 0.0313  252 PHE A CD1   
2057 C  CD2   . PHE A 252 ? 0.4133 0.2954 0.6398 -0.0299 -0.0227 0.0313  252 PHE A CD2   
2058 C  CE1   . PHE A 252 ? 0.4269 0.306  0.6633 -0.0302 -0.0253 0.0315  252 PHE A CE1   
2059 C  CE2   . PHE A 252 ? 0.4302 0.3046 0.6486 -0.0287 -0.0248 0.0314  252 PHE A CE2   
2060 C  CZ    . PHE A 252 ? 0.43   0.303  0.6534 -0.0289 -0.026  0.0316  252 PHE A CZ    
2061 N  N     . THR A 253 ? 0.3558 0.2618 0.6279 -0.0362 -0.0224 0.0372  253 THR A N     
2062 C  CA    . THR A 253 ? 0.3503 0.2607 0.6282 -0.0379 -0.0231 0.04    253 THR A CA    
2063 C  C     . THR A 253 ? 0.3479 0.2523 0.614  -0.0383 -0.0257 0.0409  253 THR A C     
2064 O  O     . THR A 253 ? 0.3562 0.2526 0.6107 -0.0371 -0.0275 0.0397  253 THR A O     
2065 C  CB    . THR A 253 ? 0.3668 0.2755 0.6545 -0.0398 -0.0283 0.0439  253 THR A CB    
2066 O  OG1   . THR A 253 ? 0.3858 0.283  0.6656 -0.0404 -0.0352 0.0455  253 THR A OG1   
2067 C  CG2   . THR A 253 ? 0.3684 0.2826 0.6679 -0.0392 -0.0262 0.0431  253 THR A CG2   
2068 N  N     . TYR A 254 ? 0.3301 0.2381 0.5991 -0.0399 -0.026  0.0433  254 TYR A N     
2069 C  CA    . TYR A 254 ? 0.3253 0.2269 0.5835 -0.0404 -0.0292 0.0443  254 TYR A CA    
2070 C  C     . TYR A 254 ? 0.3264 0.2165 0.5796 -0.0412 -0.0372 0.0469  254 TYR A C     
2071 O  O     . TYR A 254 ? 0.3378 0.2194 0.5783 -0.0401 -0.0397 0.0462  254 TYR A O     
2072 C  CB    . TYR A 254 ? 0.3181 0.2256 0.5799 -0.042  -0.0279 0.0464  254 TYR A CB    
2073 C  CG    . TYR A 254 ? 0.3328 0.2326 0.5828 -0.0423 -0.0318 0.0473  254 TYR A CG    
2074 C  CD1   . TYR A 254 ? 0.3487 0.245  0.5862 -0.0401 -0.0297 0.0441  254 TYR A CD1   
2075 C  CD2   . TYR A 254 ? 0.3454 0.2404 0.5964 -0.0446 -0.0382 0.0515  254 TYR A CD2   
2076 C  CE1   . TYR A 254 ? 0.3676 0.2563 0.594  -0.0399 -0.0334 0.0448  254 TYR A CE1   
2077 C  CE2   . TYR A 254 ? 0.3637 0.2506 0.6033 -0.0447 -0.0424 0.0523  254 TYR A CE2   
2078 C  CZ    . TYR A 254 ? 0.3836 0.2674 0.6107 -0.0422 -0.0398 0.0488  254 TYR A CZ    
2079 O  OH    . TYR A 254 ? 0.4123 0.288  0.6281 -0.0419 -0.0438 0.0494  254 TYR A OH    
2080 N  N     . SER A 255 ? 0.3168 0.2061 0.5796 -0.0428 -0.0413 0.0498  255 SER A N     
2081 C  CA    . SER A 255 ? 0.323  0.2005 0.5807 -0.0437 -0.0495 0.0523  255 SER A CA    
2082 C  C     . SER A 255 ? 0.3286 0.1975 0.5745 -0.0413 -0.0503 0.0496  255 SER A C     
2083 O  O     . SER A 255 ? 0.3406 0.1986 0.5749 -0.0408 -0.0554 0.0502  255 SER A O     
2084 C  CB    . SER A 255 ? 0.3286 0.2073 0.5997 -0.0459 -0.0537 0.056   255 SER A CB    
2085 O  OG    . SER A 255 ? 0.3487 0.2353 0.6307 -0.0453 -0.0494 0.0546  255 SER A OG    
2086 N  N     . GLU A 256 ? 0.3179 0.1918 0.566  -0.0396 -0.0448 0.0464  256 GLU A N     
2087 C  CA    . GLU A 256 ? 0.3249 0.1922 0.5627 -0.0373 -0.0446 0.044   256 GLU A CA    
2088 C  C     . GLU A 256 ? 0.3305 0.1945 0.5545 -0.0354 -0.0427 0.0421  256 GLU A C     
2089 O  O     . GLU A 256 ? 0.3391 0.1931 0.5513 -0.034  -0.0461 0.0421  256 GLU A O     
2090 C  CB    . GLU A 256 ? 0.3431 0.2169 0.5877 -0.0363 -0.0395 0.0415  256 GLU A CB    
2091 C  CG    . GLU A 256 ? 0.3922 0.2649 0.6465 -0.0375 -0.043  0.0433  256 GLU A CG    
2092 C  CD    . GLU A 256 ? 0.4624 0.3433 0.7265 -0.0368 -0.0379 0.041   256 GLU A CD    
2093 O  OE1   . GLU A 256 ? 0.4765 0.3662 0.7439 -0.0361 -0.0318 0.0388  256 GLU A OE1   
2094 O  OE2   . GLU A 256 ? 0.4849 0.363  0.7531 -0.0369 -0.0403 0.0415  256 GLU A OE2   
2095 N  N     . TRP A 257 ? 0.326  0.1979 0.551  -0.0352 -0.0374 0.0405  257 TRP A N     
2096 C  CA    . TRP A 257 ? 0.3374 0.207  0.5502 -0.0333 -0.0355 0.0388  257 TRP A CA    
2097 C  C     . TRP A 257 ? 0.3416 0.2016 0.5454 -0.0337 -0.0417 0.0411  257 TRP A C     
2098 O  O     . TRP A 257 ? 0.3441 0.1963 0.535  -0.0315 -0.0431 0.0402  257 TRP A O     
2099 C  CB    . TRP A 257 ? 0.335  0.2147 0.5515 -0.0334 -0.0294 0.0371  257 TRP A CB    
2100 C  CG    . TRP A 257 ? 0.3403 0.2279 0.5614 -0.0323 -0.0229 0.034   257 TRP A CG    
2101 C  CD1   . TRP A 257 ? 0.3467 0.2443 0.5789 -0.0331 -0.0186 0.0332  257 TRP A CD1   
2102 C  CD2   . TRP A 257 ? 0.3447 0.2309 0.5591 -0.0301 -0.0201 0.0314  257 TRP A CD2   
2103 N  NE1   . TRP A 257 ? 0.3488 0.2504 0.5812 -0.0315 -0.0138 0.03    257 TRP A NE1   
2104 C  CE2   . TRP A 257 ? 0.3507 0.2458 0.5727 -0.0299 -0.0147 0.0291  257 TRP A CE2   
2105 C  CE3   . TRP A 257 ? 0.3576 0.2358 0.5601 -0.0281 -0.0217 0.031   257 TRP A CE3   
2106 C  CZ2   . TRP A 257 ? 0.3589 0.255  0.5777 -0.0282 -0.0112 0.0266  257 TRP A CZ2   
2107 C  CZ3   . TRP A 257 ? 0.3658 0.2458 0.5656 -0.0263 -0.0178 0.0287  257 TRP A CZ3   
2108 C  CH2   . TRP A 257 ? 0.3622 0.251  0.5703 -0.0266 -0.0128 0.0266  257 TRP A CH2   
2109 N  N     . GLU A 258 ? 0.3438 0.2043 0.5546 -0.0363 -0.0456 0.0442  258 GLU A N     
2110 C  CA    . GLU A 258 ? 0.3624 0.2137 0.5662 -0.0372 -0.0525 0.0468  258 GLU A CA    
2111 C  C     . GLU A 258 ? 0.374  0.2122 0.5687 -0.036  -0.0588 0.0475  258 GLU A C     
2112 O  O     . GLU A 258 ? 0.3847 0.2134 0.5664 -0.0346 -0.0624 0.0475  258 GLU A O     
2113 C  CB    . GLU A 258 ? 0.3937 0.249  0.6095 -0.0406 -0.0556 0.0505  258 GLU A CB    
2114 C  CG    . GLU A 258 ? 0.4705 0.3173 0.6799 -0.0419 -0.0625 0.0534  258 GLU A CG    
2115 C  CD    . GLU A 258 ? 0.5641 0.4154 0.7865 -0.0456 -0.0657 0.0577  258 GLU A CD    
2116 O  OE1   . GLU A 258 ? 0.575  0.4297 0.8089 -0.0471 -0.0666 0.0594  258 GLU A OE1   
2117 O  OE2   . GLU A 258 ? 0.6022 0.4538 0.8235 -0.047  -0.0673 0.0596  258 GLU A OE2   
2118 N  N     . SER A 259 ? 0.3698 0.2072 0.5703 -0.0365 -0.0601 0.048   259 SER A N     
2119 C  CA    . SER A 259 ? 0.3802 0.205  0.5716 -0.0353 -0.066  0.0487  259 SER A CA    
2120 C  C     . SER A 259 ? 0.3885 0.2082 0.5654 -0.0316 -0.0632 0.0458  259 SER A C     
2121 O  O     . SER A 259 ? 0.4024 0.21   0.5671 -0.03   -0.0682 0.0463  259 SER A O     
2122 C  CB    . SER A 259 ? 0.3937 0.2194 0.595  -0.0366 -0.0676 0.0498  259 SER A CB    
2123 O  OG    . SER A 259 ? 0.4135 0.2464 0.6187 -0.0353 -0.0611 0.047   259 SER A OG    
2124 N  N     . ILE A 260 ? 0.3771 0.2057 0.555  -0.0302 -0.0554 0.0429  260 ILE A N     
2125 C  CA    . ILE A 260 ? 0.3792 0.2049 0.5449 -0.0267 -0.0519 0.0404  260 ILE A CA    
2126 C  C     . ILE A 260 ? 0.3875 0.2091 0.5423 -0.0252 -0.0528 0.0401  260 ILE A C     
2127 O  O     . ILE A 260 ? 0.3971 0.2091 0.5382 -0.0225 -0.055  0.0398  260 ILE A O     
2128 C  CB    . ILE A 260 ? 0.373  0.2101 0.5453 -0.0261 -0.0439 0.0378  260 ILE A CB    
2129 C  CG1   . ILE A 260 ? 0.3737 0.2137 0.5557 -0.0272 -0.0434 0.0379  260 ILE A CG1   
2130 C  CG2   . ILE A 260 ? 0.3841 0.2195 0.5449 -0.0228 -0.0401 0.0357  260 ILE A CG2   
2131 C  CD1   . ILE A 260 ? 0.3783 0.2296 0.5692 -0.0274 -0.0366 0.0357  260 ILE A CD1   
2132 N  N     . TYR A 261 ? 0.3825 0.2111 0.5433 -0.027  -0.0512 0.0404  261 TYR A N     
2133 C  CA    . TYR A 261 ? 0.3897 0.2157 0.5422 -0.0261 -0.0519 0.0402  261 TYR A CA    
2134 C  C     . TYR A 261 ? 0.4103 0.2228 0.5524 -0.0256 -0.06   0.0421  261 TYR A C     
2135 O  O     . TYR A 261 ? 0.4204 0.2255 0.5488 -0.0225 -0.0607 0.041   261 TYR A O     
2136 C  CB    . TYR A 261 ? 0.3777 0.2137 0.5405 -0.0288 -0.0495 0.0408  261 TYR A CB    
2137 C  CG    . TYR A 261 ? 0.3894 0.2226 0.5443 -0.0283 -0.0509 0.041   261 TYR A CG    
2138 C  CD1   . TYR A 261 ? 0.4066 0.2421 0.554  -0.0257 -0.0462 0.0384  261 TYR A CD1   
2139 C  CD2   . TYR A 261 ? 0.4015 0.229  0.5563 -0.0304 -0.0576 0.044   261 TYR A CD2   
2140 C  CE1   . TYR A 261 ? 0.4228 0.255  0.5626 -0.025  -0.0478 0.0386  261 TYR A CE1   
2141 C  CE2   . TYR A 261 ? 0.4179 0.2419 0.565  -0.0299 -0.0594 0.0442  261 TYR A CE2   
2142 C  CZ    . TYR A 261 ? 0.4322 0.2586 0.5717 -0.0271 -0.0544 0.0414  261 TYR A CZ    
2143 O  OH    . TYR A 261 ? 0.4521 0.275  0.5841 -0.0265 -0.0563 0.0416  261 TYR A OH    
2144 N  N     . ASN A 262 ? 0.4187 0.2274 0.5669 -0.0284 -0.0663 0.0451  262 ASN A N     
2145 C  CA    . ASN A 262 ? 0.4412 0.2361 0.5798 -0.0283 -0.075  0.0471  262 ASN A CA    
2146 C  C     . ASN A 262 ? 0.4625 0.2452 0.5887 -0.0254 -0.0783 0.0465  262 ASN A C     
2147 O  O     . ASN A 262 ? 0.4736 0.2437 0.5912 -0.0251 -0.086  0.0481  262 ASN A O     
2148 C  CB    . ASN A 262 ? 0.453  0.2477 0.6025 -0.0326 -0.0811 0.0509  262 ASN A CB    
2149 C  CG    . ASN A 262 ? 0.5016 0.3003 0.6638 -0.0348 -0.0816 0.0523  262 ASN A CG    
2150 O  OD1   . ASN A 262 ? 0.5208 0.3173 0.6808 -0.0332 -0.0804 0.051   262 ASN A OD1   
2151 N  ND2   . ASN A 262 ? 0.5073 0.312  0.6835 -0.0386 -0.0836 0.0553  262 ASN A ND2   
2152 N  N     . GLY A 263 ? 0.4662 0.2526 0.5914 -0.0232 -0.0726 0.0444  263 GLY A N     
2153 C  CA    . GLY A 263 ? 0.4868 0.263  0.6002 -0.0202 -0.0746 0.0438  263 GLY A CA    
2154 C  C     . GLY A 263 ? 0.5014 0.2716 0.6185 -0.0219 -0.0802 0.0459  263 GLY A C     
2155 O  O     . GLY A 263 ? 0.5106 0.2702 0.6164 -0.0195 -0.0832 0.0458  263 GLY A O     
2156 N  N     . THR A 264 ? 0.503  0.2798 0.6358 -0.0259 -0.0816 0.0477  264 THR A N     
2157 C  CA    . THR A 264 ? 0.5197 0.2914 0.6575 -0.0278 -0.0871 0.0499  264 THR A CA    
2158 C  C     . THR A 264 ? 0.5321 0.3059 0.6699 -0.0261 -0.0828 0.0483  264 THR A C     
2159 O  O     . THR A 264 ? 0.5377 0.3014 0.6683 -0.0251 -0.0871 0.049   264 THR A O     
2160 C  CB    . THR A 264 ? 0.527  0.3066 0.6828 -0.0322 -0.0889 0.0524  264 THR A CB    
2161 O  OG1   . THR A 264 ? 0.5379 0.3158 0.6937 -0.0339 -0.0929 0.0543  264 THR A OG1   
2162 C  CG2   . THR A 264 ? 0.5322 0.306  0.6934 -0.0342 -0.0953 0.0549  264 THR A CG2   
2163 N  N     . TYR A 265 ? 0.5366 0.3227 0.6816 -0.0258 -0.0745 0.0462  265 TYR A N     
2164 C  CA    . TYR A 265 ? 0.5523 0.3417 0.6982 -0.0245 -0.0699 0.0447  265 TYR A CA    
2165 C  C     . TYR A 265 ? 0.5592 0.3555 0.7007 -0.0219 -0.0618 0.0419  265 TYR A C     
2166 O  O     . TYR A 265 ? 0.5582 0.3603 0.7007 -0.022  -0.0589 0.041   265 TYR A O     
2167 C  CB    . TYR A 265 ? 0.5496 0.3488 0.7133 -0.0275 -0.0681 0.0452  265 TYR A CB    
2168 C  CG    . TYR A 265 ? 0.5659 0.3606 0.7372 -0.0304 -0.0755 0.0482  265 TYR A CG    
2169 C  CD1   . TYR A 265 ? 0.5849 0.3687 0.7508 -0.0302 -0.0816 0.0497  265 TYR A CD1   
2170 C  CD2   . TYR A 265 ? 0.5731 0.375  0.7575 -0.0334 -0.0763 0.0498  265 TYR A CD2   
2171 C  CE1   . TYR A 265 ? 0.5953 0.3749 0.7687 -0.033  -0.0888 0.0527  265 TYR A CE1   
2172 C  CE2   . TYR A 265 ? 0.5816 0.3802 0.7742 -0.0361 -0.0831 0.053   265 TYR A CE2   
2173 C  CZ    . TYR A 265 ? 0.5987 0.386  0.7859 -0.036  -0.0896 0.0544  265 TYR A CZ    
2174 O  OH    . TYR A 265 ? 0.6174 0.4011 0.8129 -0.0388 -0.0967 0.0577  265 TYR A OH    
2175 N  N     . ARG A 266 ? 0.5625 0.3585 0.6995 -0.0198 -0.0584 0.0408  266 ARG A N     
2176 C  CA    . ARG A 266 ? 0.5677 0.3716 0.703  -0.0178 -0.0507 0.0386  266 ARG A CA    
2177 C  C     . ARG A 266 ? 0.56   0.3761 0.7109 -0.0201 -0.046  0.0376  266 ARG A C     
2178 O  O     . ARG A 266 ? 0.5533 0.3699 0.7136 -0.0223 -0.0488 0.0387  266 ARG A O     
2179 C  CB    . ARG A 266 ? 0.5943 0.3917 0.7162 -0.0142 -0.0493 0.0383  266 ARG A CB    
2180 C  CG    . ARG A 266 ? 0.6437 0.4399 0.7685 -0.0145 -0.0494 0.039   266 ARG A CG    
2181 C  CD    . ARG A 266 ? 0.6977 0.4865 0.8081 -0.0109 -0.0485 0.0393  266 ARG A CD    
2182 N  NE    . ARG A 266 ? 0.729  0.5197 0.8438 -0.0114 -0.0468 0.0398  266 ARG A NE    
2183 C  CZ    . ARG A 266 ? 0.7537 0.5356 0.8652 -0.0116 -0.0516 0.0414  266 ARG A CZ    
2184 N  NH1   . ARG A 266 ? 0.7448 0.5151 0.8481 -0.0113 -0.0585 0.0427  266 ARG A NH1   
2185 N  NH2   . ARG A 266 ? 0.7549 0.5392 0.8708 -0.0122 -0.0497 0.0419  266 ARG A NH2   
2186 N  N     . ILE A 267 ? 0.561  0.3867 0.7149 -0.0194 -0.0394 0.0356  267 ILE A N     
2187 C  CA    . ILE A 267 ? 0.5647 0.4016 0.7325 -0.0212 -0.035  0.0344  267 ILE A CA    
2188 C  C     . ILE A 267 ? 0.5748 0.4112 0.7471 -0.0216 -0.035  0.0346  267 ILE A C     
2189 O  O     . ILE A 267 ? 0.57   0.4128 0.7547 -0.0236 -0.0339 0.0342  267 ILE A O     
2190 C  CB    . ILE A 267 ? 0.5663 0.412  0.7343 -0.0202 -0.0283 0.0321  267 ILE A CB    
2191 C  CG1   . ILE A 267 ? 0.5684 0.4253 0.7505 -0.0223 -0.0245 0.0307  267 ILE A CG1   
2192 C  CG2   . ILE A 267 ? 0.5753 0.4201 0.7356 -0.0177 -0.0249 0.0314  267 ILE A CG2   
2193 C  CD1   . ILE A 267 ? 0.5794 0.444  0.7619 -0.0218 -0.0195 0.0288  267 ILE A CD1   
2194 N  N     . THR A 268 ? 0.5849 0.4131 0.7468 -0.0197 -0.0366 0.0355  268 THR A N     
2195 C  CA    . THR A 268 ? 0.592  0.4188 0.7567 -0.02   -0.037  0.0361  268 THR A CA    
2196 C  C     . THR A 268 ? 0.5975 0.4153 0.7624 -0.0212 -0.044  0.0382  268 THR A C     
2197 O  O     . THR A 268 ? 0.6007 0.4178 0.7701 -0.022  -0.0449 0.0388  268 THR A O     
2198 C  CB    . THR A 268 ? 0.6134 0.4382 0.7681 -0.0173 -0.0337 0.036   268 THR A CB    
2199 O  OG1   . THR A 268 ? 0.6362 0.4519 0.7761 -0.0147 -0.0359 0.0368  268 THR A OG1   
2200 C  CG2   . THR A 268 ? 0.6117 0.4468 0.7701 -0.0168 -0.0268 0.0341  268 THR A CG2   
2201 N  N     . ASN A 269 ? 0.5986 0.4092 0.7586 -0.0215 -0.0494 0.0396  269 ASN A N     
2202 C  CA    . ASN A 269 ? 0.6082 0.4099 0.7685 -0.0228 -0.0567 0.0418  269 ASN A CA    
2203 C  C     . ASN A 269 ? 0.6004 0.4054 0.7727 -0.0259 -0.0601 0.0428  269 ASN A C     
2204 O  O     . ASN A 269 ? 0.6077 0.4045 0.7788 -0.027  -0.067  0.045   269 ASN A O     
2205 C  CB    . ASN A 269 ? 0.6429 0.4306 0.7862 -0.0205 -0.0617 0.0431  269 ASN A CB    
2206 C  CG    . ASN A 269 ? 0.699  0.4801 0.8347 -0.0201 -0.066  0.0437  269 ASN A CG    
2207 O  OD1   . ASN A 269 ? 0.7108 0.4972 0.8545 -0.0221 -0.0664 0.0438  269 ASN A OD1   
2208 N  ND2   . ASN A 269 ? 0.718  0.487  0.8374 -0.0174 -0.0694 0.0443  269 ASN A ND2   
2209 N  N     . LEU A 270 ? 0.5831 0.4001 0.767  -0.0271 -0.0552 0.0415  270 LEU A N     
2210 C  CA    . LEU A 270 ? 0.5728 0.3949 0.7694 -0.0298 -0.0571 0.0426  270 LEU A CA    
2211 C  C     . LEU A 270 ? 0.5626 0.3834 0.769  -0.0316 -0.061  0.0443  270 LEU A C     
2212 O  O     . LEU A 270 ? 0.5632 0.3864 0.7731 -0.0313 -0.0586 0.0432  270 LEU A O     
2213 C  CB    . LEU A 270 ? 0.5678 0.4032 0.7737 -0.0302 -0.05   0.0405  270 LEU A CB    
2214 C  CG    . LEU A 270 ? 0.582  0.4233 0.7959 -0.032  -0.0502 0.0413  270 LEU A CG    
2215 C  CD1   . LEU A 270 ? 0.5931 0.4279 0.7961 -0.0315 -0.0532 0.0423  270 LEU A CD1   
2216 C  CD2   . LEU A 270 ? 0.5863 0.44   0.8081 -0.0319 -0.0428 0.0389  270 LEU A CD2   
2217 N  N     . PRO A 271 ? 0.5476 0.3637 0.758  -0.0336 -0.0676 0.047   271 PRO A N     
2218 C  CA    . PRO A 271 ? 0.5354 0.3496 0.7551 -0.0353 -0.0719 0.0488  271 PRO A CA    
2219 C  C     . PRO A 271 ? 0.5135 0.3399 0.7496 -0.0363 -0.0673 0.0478  271 PRO A C     
2220 O  O     . PRO A 271 ? 0.5116 0.3375 0.7537 -0.0367 -0.0685 0.0481  271 PRO A O     
2221 C  CB    . PRO A 271 ? 0.5486 0.3566 0.7698 -0.0373 -0.0796 0.0521  271 PRO A CB    
2222 C  CG    . PRO A 271 ? 0.5544 0.3664 0.7737 -0.0374 -0.0775 0.0518  271 PRO A CG    
2223 C  CD    . PRO A 271 ? 0.5406 0.3528 0.7476 -0.0345 -0.0718 0.0488  271 PRO A CD    
2224 N  N     . SER A 272 ? 0.4968 0.3337 0.7396 -0.0365 -0.0619 0.0465  272 SER A N     
2225 C  CA    . SER A 272 ? 0.4852 0.3338 0.7425 -0.037  -0.0569 0.0451  272 SER A CA    
2226 C  C     . SER A 272 ? 0.4757 0.3294 0.731  -0.0351 -0.0502 0.0416  272 SER A C     
2227 O  O     . SER A 272 ? 0.4678 0.3309 0.7336 -0.0351 -0.0457 0.04    272 SER A O     
2228 C  CB    . SER A 272 ? 0.5007 0.358  0.7659 -0.038  -0.0544 0.0456  272 SER A CB    
2229 O  OG    . SER A 272 ? 0.5383 0.3956 0.7932 -0.037  -0.0516 0.0443  272 SER A OG    
2230 N  N     . LEU A 273 ? 0.4749 0.3225 0.7166 -0.0334 -0.0495 0.0406  273 LEU A N     
2231 C  CA    . LEU A 273 ? 0.4716 0.3236 0.7112 -0.0319 -0.0436 0.0377  273 LEU A CA    
2232 C  C     . LEU A 273 ? 0.4615 0.3147 0.7095 -0.0323 -0.044  0.0375  273 LEU A C     
2233 O  O     . LEU A 273 ? 0.4668 0.3126 0.7142 -0.0329 -0.0493 0.0395  273 LEU A O     
2234 C  CB    . LEU A 273 ? 0.482  0.3267 0.7058 -0.03   -0.0435 0.0375  273 LEU A CB    
2235 C  CG    . LEU A 273 ? 0.4967 0.3473 0.7164 -0.0284 -0.0369 0.0349  273 LEU A CG    
2236 C  CD1   . LEU A 273 ? 0.4985 0.3554 0.719  -0.0284 -0.0336 0.0338  273 LEU A CD1   
2237 C  CD2   . LEU A 273 ? 0.5124 0.3556 0.7177 -0.0264 -0.037  0.0353  273 LEU A CD2   
2238 N  N     . GLY A 274 ? 0.4449 0.3071 0.7012 -0.032  -0.0388 0.0351  274 GLY A N     
2239 C  CA    . GLY A 274 ? 0.4364 0.3003 0.7017 -0.0322 -0.039  0.0346  274 GLY A CA    
2240 C  C     . GLY A 274 ? 0.4209 0.2928 0.7011 -0.0329 -0.0379 0.0342  274 GLY A C     
2241 O  O     . GLY A 274 ? 0.4247 0.2998 0.7131 -0.0327 -0.0367 0.0329  274 GLY A O     
2242 N  N     . ARG A 275 ? 0.4002 0.2756 0.6845 -0.0337 -0.0382 0.0353  275 ARG A N     
2243 C  CA    . ARG A 275 ? 0.3818 0.2659 0.6806 -0.0341 -0.0363 0.0352  275 ARG A CA    
2244 C  C     . ARG A 275 ? 0.369  0.2621 0.6724 -0.0326 -0.0295 0.0316  275 ARG A C     
2245 O  O     . ARG A 275 ? 0.3608 0.2607 0.6759 -0.0323 -0.0276 0.0309  275 ARG A O     
2246 C  CB    . ARG A 275 ? 0.3909 0.277  0.6926 -0.0353 -0.0378 0.0376  275 ARG A CB    
2247 C  CG    . ARG A 275 ? 0.4192 0.3071 0.7123 -0.0349 -0.0346 0.0367  275 ARG A CG    
2248 C  CD    . ARG A 275 ? 0.4452 0.3341 0.7415 -0.0364 -0.0372 0.0397  275 ARG A CD    
2249 N  NE    . ARG A 275 ? 0.4712 0.3641 0.7622 -0.0361 -0.0334 0.0387  275 ARG A NE    
2250 C  CZ    . ARG A 275 ? 0.4848 0.3876 0.7816 -0.0355 -0.0274 0.0368  275 ARG A CZ    
2251 N  NH1   . ARG A 275 ? 0.4684 0.3779 0.7758 -0.0347 -0.0243 0.0354  275 ARG A NH1   
2252 N  NH2   . ARG A 275 ? 0.4829 0.3884 0.7741 -0.0354 -0.0246 0.0362  275 ARG A NH2   
2253 N  N     . PHE A 276 ? 0.3648 0.2577 0.6587 -0.0316 -0.0261 0.0293  276 PHE A N     
2254 C  CA    . PHE A 276 ? 0.3607 0.2598 0.6562 -0.0303 -0.0205 0.0258  276 PHE A CA    
2255 C  C     . PHE A 276 ? 0.3678 0.2617 0.653  -0.0298 -0.0204 0.025   276 PHE A C     
2256 O  O     . PHE A 276 ? 0.3791 0.2664 0.6541 -0.03   -0.0228 0.0266  276 PHE A O     
2257 C  CB    . PHE A 276 ? 0.3543 0.261  0.6501 -0.0297 -0.0156 0.0243  276 PHE A CB    
2258 C  CG    . PHE A 276 ? 0.3662 0.2706 0.6512 -0.03   -0.0154 0.025   276 PHE A CG    
2259 C  CD1   . PHE A 276 ? 0.3798 0.2828 0.6551 -0.0291 -0.013  0.0233  276 PHE A CD1   
2260 C  CD2   . PHE A 276 ? 0.3774 0.2815 0.6625 -0.031  -0.0175 0.0274  276 PHE A CD2   
2261 C  CE1   . PHE A 276 ? 0.3921 0.2931 0.6577 -0.0291 -0.0128 0.0239  276 PHE A CE1   
2262 C  CE2   . PHE A 276 ? 0.3895 0.2911 0.6645 -0.0311 -0.0175 0.0279  276 PHE A CE2   
2263 C  CZ    . PHE A 276 ? 0.3909 0.291  0.6561 -0.03   -0.0151 0.0261  276 PHE A CZ    
2264 N  N     . LYS A 277 ? 0.3569 0.2532 0.6449 -0.029  -0.0179 0.0227  277 LYS A N     
2265 C  CA    . LYS A 277 ? 0.354  0.2462 0.6338 -0.0287 -0.0177 0.0223  277 LYS A CA    
2266 C  C     . LYS A 277 ? 0.3429 0.2394 0.6171 -0.0279 -0.0128 0.0201  277 LYS A C     
2267 O  O     . LYS A 277 ? 0.3361 0.2384 0.6126 -0.0275 -0.0098 0.0187  277 LYS A O     
2268 C  CB    . LYS A 277 ? 0.3724 0.2639 0.6586 -0.0287 -0.0185 0.0214  277 LYS A CB    
2269 C  CG    . LYS A 277 ? 0.4211 0.3065 0.7103 -0.0296 -0.0239 0.0239  277 LYS A CG    
2270 C  CD    . LYS A 277 ? 0.4752 0.358  0.7667 -0.0296 -0.0251 0.0235  277 LYS A CD    
2271 C  CE    . LYS A 277 ? 0.5327 0.4066 0.8195 -0.0305 -0.0304 0.0266  277 LYS A CE    
2272 N  NZ    . LYS A 277 ? 0.5673 0.4392 0.8609 -0.0309 -0.0327 0.0265  277 LYS A NZ    
2273 N  N     . PHE A 278 ? 0.3366 0.2302 0.6033 -0.0276 -0.0122 0.0202  278 PHE A N     
2274 C  CA    . PHE A 278 ? 0.3287 0.2264 0.5911 -0.0269 -0.008  0.0183  278 PHE A CA    
2275 C  C     . PHE A 278 ? 0.3115 0.2126 0.5808 -0.0268 -0.0063 0.016   278 PHE A C     
2276 O  O     . PHE A 278 ? 0.3126 0.2104 0.583  -0.0271 -0.0082 0.0168  278 PHE A O     
2277 C  CB    . PHE A 278 ? 0.3326 0.2258 0.5835 -0.0264 -0.008  0.02    278 PHE A CB    
2278 C  CG    . PHE A 278 ? 0.342  0.239  0.5899 -0.0259 -0.0042 0.0185  278 PHE A CG    
2279 C  CD1   . PHE A 278 ? 0.3493 0.2527 0.5993 -0.0256 -0.0007 0.0161  278 PHE A CD1   
2280 C  CD2   . PHE A 278 ? 0.3522 0.2464 0.595  -0.0257 -0.0042 0.0199  278 PHE A CD2   
2281 C  CE1   . PHE A 278 ? 0.3542 0.2609 0.6018 -0.0252 0.0023  0.0149  278 PHE A CE1   
2282 C  CE2   . PHE A 278 ? 0.3569 0.2549 0.5977 -0.0254 -0.001  0.0191  278 PHE A CE2   
2283 C  CZ    . PHE A 278 ? 0.3513 0.2554 0.5946 -0.0252 0.0021  0.0165  278 PHE A CZ    
2284 N  N     . ARG A 279 ? 0.2924 0.1999 0.5669 -0.0262 -0.0032 0.0133  279 ARG A N     
2285 C  CA    . ARG A 279 ? 0.2802 0.191  0.5612 -0.0258 -0.0016 0.0106  279 ARG A CA    
2286 C  C     . ARG A 279 ? 0.259  0.1743 0.5368 -0.0252 0.0023  0.0083  279 ARG A C     
2287 O  O     . ARG A 279 ? 0.2568 0.1768 0.5367 -0.0246 0.0048  0.0065  279 ARG A O     
2288 C  CB    . ARG A 279 ? 0.2996 0.2133 0.5905 -0.0253 -0.0018 0.0094  279 ARG A CB    
2289 C  CG    . ARG A 279 ? 0.3492 0.2586 0.644  -0.026  -0.006  0.0119  279 ARG A CG    
2290 C  CD    . ARG A 279 ? 0.3946 0.3068 0.7005 -0.0252 -0.0063 0.0107  279 ARG A CD    
2291 N  NE    . ARG A 279 ? 0.4349 0.3428 0.745  -0.026  -0.0108 0.0134  279 ARG A NE    
2292 C  CZ    . ARG A 279 ? 0.4537 0.3573 0.7666 -0.0264 -0.0139 0.0139  279 ARG A CZ    
2293 N  NH1   . ARG A 279 ? 0.4346 0.3377 0.7467 -0.0261 -0.0131 0.0122  279 ARG A NH1   
2294 N  NH2   . ARG A 279 ? 0.4551 0.3548 0.7717 -0.0271 -0.0181 0.0164  279 ARG A NH2   
2295 N  N     . LYS A 280 ? 0.2433 0.1572 0.516  -0.0255 0.0026  0.0087  280 LYS A N     
2296 C  CA    . LYS A 280 ? 0.2329 0.1505 0.5023 -0.0252 0.0058  0.007   280 LYS A CA    
2297 C  C     . LYS A 280 ? 0.2193 0.1405 0.4953 -0.0247 0.0072  0.0035  280 LYS A C     
2298 O  O     . LYS A 280 ? 0.2178 0.1373 0.4991 -0.0248 0.0055  0.0028  280 LYS A O     
2299 C  CB    . LYS A 280 ? 0.2451 0.1604 0.5086 -0.0258 0.0055  0.0089  280 LYS A CB    
2300 C  CG    . LYS A 280 ? 0.2711 0.19   0.5331 -0.0257 0.008   0.0074  280 LYS A CG    
2301 C  CD    . LYS A 280 ? 0.2997 0.2215 0.5557 -0.0252 0.0106  0.0071  280 LYS A CD    
2302 C  CE    . LYS A 280 ? 0.3301 0.2554 0.5859 -0.0252 0.0125  0.0055  280 LYS A CE    
2303 N  NZ    . LYS A 280 ? 0.3598 0.2874 0.6091 -0.0248 0.0148  0.0058  280 LYS A NZ    
2304 N  N     . LYS A 281 ? 0.2066 0.1321 0.4816 -0.0239 0.0101  0.0012  281 LYS A N     
2305 C  CA    . LYS A 281 ? 0.2014 0.1298 0.4809 -0.0231 0.0116  -0.0023 281 LYS A CA    
2306 C  C     . LYS A 281 ? 0.2014 0.1299 0.4777 -0.0235 0.0121  -0.003  281 LYS A C     
2307 O  O     . LYS A 281 ? 0.2053 0.1353 0.4758 -0.0238 0.0136  -0.0024 281 LYS A O     
2308 C  CB    . LYS A 281 ? 0.2223 0.1553 0.5018 -0.0219 0.0146  -0.0042 281 LYS A CB    
2309 C  CG    . LYS A 281 ? 0.2699 0.2039 0.5543 -0.0214 0.0144  -0.0035 281 LYS A CG    
2310 C  CD    . LYS A 281 ? 0.3169 0.2558 0.6009 -0.0204 0.0177  -0.005  281 LYS A CD    
2311 C  CE    . LYS A 281 ? 0.3545 0.2955 0.6451 -0.0198 0.0179  -0.0043 281 LYS A CE    
2312 N  NZ    . LYS A 281 ? 0.3809 0.3272 0.6714 -0.0187 0.0216  -0.0057 281 LYS A NZ    
2313 N  N     . ILE A 282 ? 0.1919 0.1187 0.4725 -0.0237 0.0104  -0.0041 282 ILE A N     
2314 C  CA    . ILE A 282 ? 0.1837 0.1105 0.4626 -0.0245 0.0102  -0.0047 282 ILE A CA    
2315 C  C     . ILE A 282 ? 0.1857 0.1134 0.4687 -0.0233 0.0105  -0.0088 282 ILE A C     
2316 O  O     . ILE A 282 ? 0.182  0.1082 0.4706 -0.0225 0.0092  -0.0102 282 ILE A O     
2317 C  CB    . ILE A 282 ? 0.1756 0.0989 0.4548 -0.026  0.0076  -0.0017 282 ILE A CB    
2318 C  CG1   . ILE A 282 ? 0.1792 0.1008 0.4535 -0.0266 0.0073  0.0022  282 ILE A CG1   
2319 C  CG2   . ILE A 282 ? 0.1755 0.0996 0.4535 -0.0269 0.0075  -0.0019 282 ILE A CG2   
2320 C  CD1   . ILE A 282 ? 0.1884 0.1065 0.4629 -0.0278 0.0049  0.0053  282 ILE A CD1   
2321 N  N     . ALA A 283 ? 0.1909 0.1209 0.4707 -0.0231 0.0122  -0.0108 283 ALA A N     
2322 C  CA    . ALA A 283 ? 0.205  0.1352 0.4872 -0.0218 0.0123  -0.0148 283 ALA A CA    
2323 C  C     . ALA A 283 ? 0.225  0.1514 0.5108 -0.0227 0.0089  -0.0149 283 ALA A C     
2324 O  O     . ALA A 283 ? 0.2344 0.1596 0.5192 -0.0246 0.0073  -0.0118 283 ALA A O     
2325 C  CB    . ALA A 283 ? 0.2067 0.1392 0.4837 -0.0217 0.0142  -0.0164 283 ALA A CB    
2326 N  N     . GLU A 284 ? 0.2266 0.1513 0.5166 -0.0212 0.0078  -0.0183 284 GLU A N     
2327 C  CA    . GLU A 284 ? 0.2342 0.1548 0.5281 -0.022  0.0041  -0.0185 284 GLU A CA    
2328 C  C     . GLU A 284 ? 0.2393 0.1591 0.5307 -0.0239 0.0025  -0.0176 284 GLU A C     
2329 O  O     . GLU A 284 ? 0.2465 0.1644 0.5397 -0.026  0       -0.0145 284 GLU A O     
2330 C  CB    . GLU A 284 ? 0.2709 0.1896 0.5686 -0.0195 0.0035  -0.0229 284 GLU A CB    
2331 C  CG    . GLU A 284 ? 0.3454 0.2592 0.6474 -0.0202 -0.0009 -0.0233 284 GLU A CG    
2332 C  CD    . GLU A 284 ? 0.4597 0.371  0.7657 -0.0173 -0.0017 -0.0274 284 GLU A CD    
2333 O  OE1   . GLU A 284 ? 0.4912 0.405  0.7985 -0.0149 0.0011  -0.0289 284 GLU A OE1   
2334 O  OE2   . GLU A 284 ? 0.5    0.407  0.808  -0.0174 -0.0052 -0.029  284 GLU A OE2   
2335 N  N     . LYS A 285 ? 0.2348 0.1567 0.5221 -0.0234 0.0043  -0.0196 285 LYS A N     
2336 C  CA    . LYS A 285 ? 0.2337 0.1554 0.5189 -0.0252 0.0028  -0.0187 285 LYS A CA    
2337 C  C     . LYS A 285 ? 0.2438 0.1673 0.5275 -0.0276 0.0029  -0.0136 285 LYS A C     
2338 O  O     . LYS A 285 ? 0.2508 0.1738 0.5351 -0.0295 0.0009  -0.0117 285 LYS A O     
2339 C  CB    . LYS A 285 ? 0.2474 0.1712 0.5279 -0.024  0.0048  -0.0218 285 LYS A CB    
2340 C  CG    . LYS A 285 ? 0.2991 0.2272 0.5751 -0.0235 0.0088  -0.0208 285 LYS A CG    
2341 C  CD    . LYS A 285 ? 0.3564 0.2862 0.6278 -0.0222 0.0107  -0.024  285 LYS A CD    
2342 C  CE    . LYS A 285 ? 0.4033 0.3372 0.6703 -0.0219 0.0143  -0.0227 285 LYS A CE    
2343 N  NZ    . LYS A 285 ? 0.4377 0.373  0.6998 -0.021  0.016   -0.0254 285 LYS A NZ    
2344 N  N     . SER A 286 ? 0.2445 0.1698 0.5265 -0.0274 0.005   -0.0112 286 SER A N     
2345 C  CA    . SER A 286 ? 0.2505 0.1771 0.5301 -0.029  0.0055  -0.0065 286 SER A CA    
2346 C  C     . SER A 286 ? 0.252  0.1757 0.5351 -0.0304 0.0029  -0.0031 286 SER A C     
2347 O  O     . SER A 286 ? 0.2526 0.1771 0.5341 -0.0318 0.0029  0.0009  286 SER A O     
2348 C  CB    . SER A 286 ? 0.2682 0.1971 0.5435 -0.028  0.0085  -0.0055 286 SER A CB    
2349 O  OG    . SER A 286 ? 0.3015 0.233  0.5736 -0.0268 0.0109  -0.0083 286 SER A OG    
2350 N  N     . LEU A 287 ? 0.2492 0.1697 0.5367 -0.0299 0.0009  -0.0047 287 LEU A N     
2351 C  CA    . LEU A 287 ? 0.2574 0.1747 0.5481 -0.0312 -0.0017 -0.0016 287 LEU A CA    
2352 C  C     . LEU A 287 ? 0.2752 0.1911 0.5685 -0.0334 -0.0046 0.0005  287 LEU A C     
2353 O  O     . LEU A 287 ? 0.2787 0.1941 0.5739 -0.0336 -0.0062 -0.0018 287 LEU A O     
2354 C  CB    . LEU A 287 ? 0.2538 0.1681 0.549  -0.0299 -0.0033 -0.0039 287 LEU A CB    
2355 C  CG    . LEU A 287 ? 0.2632 0.1788 0.5572 -0.0282 -0.001  -0.0047 287 LEU A CG    
2356 C  CD1   . LEU A 287 ? 0.2653 0.1788 0.5649 -0.0267 -0.0024 -0.0073 287 LEU A CD1   
2357 C  CD2   . LEU A 287 ? 0.2707 0.1859 0.5614 -0.0291 -0.0007 -0.0004 287 LEU A CD2   
2358 N  N     . SER A 288 ? 0.2835 0.1986 0.5766 -0.0349 -0.0054 0.0052  288 SER A N     
2359 C  CA    . SER A 288 ? 0.294  0.2082 0.5897 -0.0373 -0.0079 0.0087  288 SER A CA    
2360 C  C     . SER A 288 ? 0.2991 0.2114 0.5941 -0.0382 -0.0085 0.0134  288 SER A C     
2361 O  O     . SER A 288 ? 0.3024 0.2141 0.5944 -0.037  -0.007  0.0137  288 SER A O     
2362 C  CB    . SER A 288 ? 0.3127 0.231  0.6059 -0.0382 -0.0063 0.0105  288 SER A CB    
2363 O  OG    . SER A 288 ? 0.3493 0.2705 0.6371 -0.0377 -0.0029 0.0135  288 SER A OG    
2364 N  N     . GLY A 289 ? 0.2953 0.2065 0.5932 -0.0404 -0.0109 0.0171  289 GLY A N     
2365 C  CA    . GLY A 289 ? 0.2976 0.2068 0.5946 -0.0414 -0.0115 0.0218  289 GLY A CA    
2366 C  C     . GLY A 289 ? 0.2946 0.1998 0.5915 -0.0403 -0.0125 0.0208  289 GLY A C     
2367 O  O     . GLY A 289 ? 0.2996 0.2021 0.6008 -0.0397 -0.0148 0.0171  289 GLY A O     
2368 N  N     . LYS A 290 ? 0.2867 0.1912 0.5783 -0.0397 -0.011  0.0237  290 LYS A N     
2369 C  CA    . LYS A 290 ? 0.2871 0.1876 0.5783 -0.0388 -0.0122 0.0231  290 LYS A CA    
2370 C  C     . LYS A 290 ? 0.2869 0.1889 0.5736 -0.0366 -0.0094 0.0208  290 LYS A C     
2371 O  O     . LYS A 290 ? 0.2871 0.1863 0.5709 -0.0359 -0.0097 0.0218  290 LYS A O     
2372 C  CB    . LYS A 290 ? 0.308  0.2051 0.5963 -0.0398 -0.0133 0.0281  290 LYS A CB    
2373 C  CG    . LYS A 290 ? 0.3472 0.2427 0.6403 -0.0421 -0.0163 0.0309  290 LYS A CG    
2374 C  CD    . LYS A 290 ? 0.3964 0.2901 0.6854 -0.0431 -0.0164 0.0367  290 LYS A CD    
2375 C  CE    . LYS A 290 ? 0.4473 0.3395 0.7418 -0.0457 -0.0196 0.0396  290 LYS A CE    
2376 N  NZ    . LYS A 290 ? 0.4843 0.3761 0.7747 -0.0468 -0.0188 0.0459  290 LYS A NZ    
2377 N  N     . VAL A 291 ? 0.2832 0.1893 0.5693 -0.0357 -0.007  0.0178  291 VAL A N     
2378 C  CA    . VAL A 291 ? 0.2884 0.1966 0.5704 -0.0339 -0.0042 0.0158  291 VAL A CA    
2379 C  C     . VAL A 291 ? 0.2929 0.1988 0.5779 -0.0328 -0.0055 0.0132  291 VAL A C     
2380 O  O     . VAL A 291 ? 0.299  0.2037 0.5803 -0.032  -0.0049 0.0143  291 VAL A O     
2381 C  CB    . VAL A 291 ? 0.2913 0.2042 0.5723 -0.0333 -0.0017 0.0132  291 VAL A CB    
2382 C  CG1   . VAL A 291 ? 0.2969 0.2116 0.5745 -0.0316 0.0008  0.0109  291 VAL A CG1   
2383 C  CG2   . VAL A 291 ? 0.2959 0.2115 0.5735 -0.0343 -0.0001 0.0165  291 VAL A CG2   
2384 N  N     . LYS A 292 ? 0.2876 0.1925 0.5793 -0.0326 -0.0074 0.0101  292 LYS A N     
2385 C  CA    . LYS A 292 ? 0.2932 0.1965 0.5887 -0.0314 -0.0084 0.0079  292 LYS A CA    
2386 C  C     . LYS A 292 ? 0.3073 0.2062 0.6025 -0.0319 -0.0109 0.011   292 LYS A C     
2387 O  O     . LYS A 292 ? 0.3092 0.2076 0.6036 -0.031  -0.0106 0.0109  292 LYS A O     
2388 C  CB    . LYS A 292 ? 0.3064 0.2093 0.609  -0.0307 -0.01   0.004   292 LYS A CB    
2389 C  CG    . LYS A 292 ? 0.3486 0.2506 0.656  -0.029  -0.0107 0.0019  292 LYS A CG    
2390 C  CD    . LYS A 292 ? 0.3975 0.3007 0.71   -0.0272 -0.0104 -0.0029 292 LYS A CD    
2391 C  CE    . LYS A 292 ? 0.4345 0.3382 0.7517 -0.0252 -0.0101 -0.0046 292 LYS A CE    
2392 N  NZ    . LYS A 292 ? 0.459  0.366  0.7727 -0.0247 -0.0072 -0.0038 292 LYS A NZ    
2393 N  N     . GLU A 293 ? 0.3145 0.2103 0.6098 -0.0336 -0.0132 0.0142  293 GLU A N     
2394 C  CA    . GLU A 293 ? 0.3265 0.2174 0.6208 -0.0341 -0.0158 0.0172  293 GLU A CA    
2395 C  C     . GLU A 293 ? 0.3297 0.2201 0.6155 -0.0337 -0.0141 0.0201  293 GLU A C     
2396 O  O     . GLU A 293 ? 0.3298 0.2168 0.6144 -0.0334 -0.0157 0.0211  293 GLU A O     
2397 C  CB    . GLU A 293 ? 0.3577 0.245  0.6544 -0.036  -0.019  0.0199  293 GLU A CB    
2398 C  CG    . GLU A 293 ? 0.4421 0.3238 0.7384 -0.0365 -0.0222 0.0226  293 GLU A CG    
2399 C  CD    . GLU A 293 ? 0.5288 0.4085 0.8282 -0.0353 -0.0237 0.0209  293 GLU A CD    
2400 O  OE1   . GLU A 293 ? 0.5543 0.4312 0.8488 -0.0351 -0.0243 0.0232  293 GLU A OE1   
2401 O  OE2   . GLU A 293 ? 0.5363 0.4171 0.843  -0.0344 -0.0245 0.0173  293 GLU A OE2   
2402 N  N     . PHE A 294 ? 0.3281 0.2218 0.6082 -0.0336 -0.011  0.0211  294 PHE A N     
2403 C  CA    . PHE A 294 ? 0.3319 0.2251 0.6035 -0.0327 -0.0092 0.0233  294 PHE A CA    
2404 C  C     . PHE A 294 ? 0.3292 0.2231 0.6007 -0.0314 -0.0086 0.0208  294 PHE A C     
2405 O  O     . PHE A 294 ? 0.3341 0.2244 0.6017 -0.0309 -0.0098 0.0223  294 PHE A O     
2406 C  CB    . PHE A 294 ? 0.3326 0.2297 0.5988 -0.0326 -0.0058 0.0246  294 PHE A CB    
2407 C  CG    . PHE A 294 ? 0.346  0.2422 0.6031 -0.0312 -0.004  0.0264  294 PHE A CG    
2408 C  CD1   . PHE A 294 ? 0.3612 0.253  0.6118 -0.031  -0.0049 0.0303  294 PHE A CD1   
2409 C  CD2   . PHE A 294 ? 0.3569 0.256  0.6115 -0.03   -0.0018 0.0241  294 PHE A CD2   
2410 C  CE1   . PHE A 294 ? 0.3733 0.2633 0.6148 -0.0295 -0.0035 0.0317  294 PHE A CE1   
2411 C  CE2   . PHE A 294 ? 0.3692 0.2668 0.6152 -0.0287 -0.0006 0.0257  294 PHE A CE2   
2412 C  CZ    . PHE A 294 ? 0.3697 0.2626 0.6091 -0.0283 -0.0015 0.0293  294 PHE A CZ    
2413 N  N     . ASN A 295 ? 0.3207 0.2189 0.5968 -0.0308 -0.007  0.017   295 ASN A N     
2414 C  CA    . ASN A 295 ? 0.3223 0.222  0.5993 -0.0296 -0.0062 0.0148  295 ASN A CA    
2415 C  C     . ASN A 295 ? 0.32   0.2159 0.6014 -0.0296 -0.0094 0.0151  295 ASN A C     
2416 O  O     . ASN A 295 ? 0.3267 0.2214 0.6059 -0.0291 -0.0098 0.0159  295 ASN A O     
2417 C  CB    . ASN A 295 ? 0.3359 0.2407 0.6171 -0.0289 -0.0039 0.0108  295 ASN A CB    
2418 C  CG    . ASN A 295 ? 0.3783 0.286  0.6574 -0.0277 -0.0016 0.0094  295 ASN A CG    
2419 O  OD1   . ASN A 295 ? 0.3913 0.2974 0.6653 -0.0276 -0.0017 0.0115  295 ASN A OD1   
2420 N  ND2   . ASN A 295 ? 0.3867 0.2985 0.6695 -0.0269 0.0004  0.006   295 ASN A ND2   
2421 N  N     . ASN A 296 ? 0.3089 0.2025 0.5963 -0.0303 -0.012  0.015   296 ASN A N     
2422 C  CA    . ASN A 296 ? 0.3069 0.1968 0.5991 -0.0303 -0.0154 0.0155  296 ASN A CA    
2423 C  C     . ASN A 296 ? 0.2975 0.1819 0.5832 -0.031  -0.0177 0.0194  296 ASN A C     
2424 O  O     . ASN A 296 ? 0.2956 0.1776 0.5823 -0.0307 -0.0197 0.02    296 ASN A O     
2425 C  CB    . ASN A 296 ? 0.3314 0.2195 0.6309 -0.0309 -0.0179 0.0146  296 ASN A CB    
2426 C  CG    . ASN A 296 ? 0.3844 0.2766 0.69   -0.0299 -0.0163 0.0105  296 ASN A CG    
2427 O  OD1   . ASN A 296 ? 0.4064 0.2977 0.7155 -0.0305 -0.0177 0.0097  296 ASN A OD1   
2428 N  ND2   . ASN A 296 ? 0.3887 0.2853 0.6955 -0.0284 -0.0136 0.0079  296 ASN A ND2   
2429 N  N     . ILE A 297 ? 0.2909 0.1732 0.5696 -0.0316 -0.0173 0.0222  297 ILE A N     
2430 C  CA    . ILE A 297 ? 0.2927 0.1694 0.5635 -0.0318 -0.0191 0.0259  297 ILE A CA    
2431 C  C     . ILE A 297 ? 0.2957 0.1725 0.5604 -0.0307 -0.0179 0.026   297 ILE A C     
2432 O  O     . ILE A 297 ? 0.3014 0.1733 0.5637 -0.0307 -0.0208 0.0274  297 ILE A O     
2433 C  CB    . ILE A 297 ? 0.2967 0.172  0.5614 -0.0324 -0.0183 0.0289  297 ILE A CB    
2434 C  CG1   . ILE A 297 ? 0.3068 0.1806 0.5777 -0.0339 -0.0206 0.0295  297 ILE A CG1   
2435 C  CG2   . ILE A 297 ? 0.303  0.1726 0.5574 -0.0319 -0.0193 0.0325  297 ILE A CG2   
2436 C  CD1   . ILE A 297 ? 0.3228 0.1975 0.5902 -0.0347 -0.0192 0.0323  297 ILE A CD1   
2437 N  N     . VAL A 298 ? 0.2875 0.1695 0.55   -0.03   -0.0141 0.0243  298 VAL A N     
2438 C  CA    . VAL A 298 ? 0.2898 0.1721 0.5469 -0.029  -0.0131 0.0242  298 VAL A CA    
2439 C  C     . VAL A 298 ? 0.2889 0.1708 0.552  -0.029  -0.0152 0.0229  298 VAL A C     
2440 O  O     . VAL A 298 ? 0.2947 0.1721 0.554  -0.0289 -0.0177 0.0247  298 VAL A O     
2441 C  CB    . VAL A 298 ? 0.2929 0.1812 0.5476 -0.0283 -0.0088 0.0224  298 VAL A CB    
2442 C  CG1   . VAL A 298 ? 0.3028 0.1913 0.5528 -0.0274 -0.0081 0.0222  298 VAL A CG1   
2443 C  CG2   . VAL A 298 ? 0.297  0.1856 0.5455 -0.0282 -0.0068 0.0243  298 VAL A CG2   
2444 N  N     . GLN A 299 ? 0.2767 0.1631 0.5495 -0.029  -0.0145 0.0201  299 GLN A N     
2445 C  CA    . GLN A 299 ? 0.2736 0.1611 0.5536 -0.0288 -0.0159 0.0191  299 GLN A CA    
2446 C  C     . GLN A 299 ? 0.2838 0.1654 0.5667 -0.0295 -0.0207 0.0212  299 GLN A C     
2447 O  O     . GLN A 299 ? 0.2829 0.1645 0.5705 -0.0295 -0.0224 0.0214  299 GLN A O     
2448 C  CB    . GLN A 299 ? 0.2762 0.1698 0.5652 -0.0282 -0.0135 0.0155  299 GLN A CB    
2449 C  CG    . GLN A 299 ? 0.2888 0.1879 0.5746 -0.0275 -0.0091 0.0134  299 GLN A CG    
2450 C  CD    . GLN A 299 ? 0.3062 0.2109 0.5994 -0.0265 -0.0067 0.0098  299 GLN A CD    
2451 O  OE1   . GLN A 299 ? 0.3222 0.228  0.6232 -0.0259 -0.0076 0.0088  299 GLN A OE1   
2452 N  NE2   . GLN A 299 ? 0.2949 0.2034 0.5859 -0.0261 -0.0036 0.0077  299 GLN A NE2   
2453 N  N     . ARG A 300 ? 0.2931 0.1697 0.5732 -0.0302 -0.023  0.0231  300 ARG A N     
2454 C  CA    . ARG A 300 ? 0.3046 0.1747 0.5864 -0.031  -0.0278 0.0254  300 ARG A CA    
2455 C  C     . ARG A 300 ? 0.3189 0.183  0.5917 -0.031  -0.0303 0.0283  300 ARG A C     
2456 O  O     . ARG A 300 ? 0.3221 0.1816 0.5972 -0.0316 -0.0346 0.0298  300 ARG A O     
2457 C  CB    . ARG A 300 ? 0.3226 0.1895 0.6036 -0.0318 -0.0291 0.0266  300 ARG A CB    
2458 C  CG    . ARG A 300 ? 0.3595 0.2199 0.6429 -0.0327 -0.0342 0.0287  300 ARG A CG    
2459 C  CD    . ARG A 300 ? 0.3974 0.2553 0.6801 -0.0335 -0.035  0.0299  300 ARG A CD    
2460 N  NE    . ARG A 300 ? 0.4273 0.2904 0.7183 -0.0336 -0.0332 0.0271  300 ARG A NE    
2461 C  CZ    . ARG A 300 ? 0.4529 0.3169 0.7426 -0.0342 -0.0318 0.0274  300 ARG A CZ    
2462 N  NH1   . ARG A 300 ? 0.4485 0.3095 0.7296 -0.0348 -0.0316 0.0307  300 ARG A NH1   
2463 N  NH2   . ARG A 300 ? 0.4448 0.3127 0.742  -0.0342 -0.0309 0.0247  300 ARG A NH2   
2464 N  N     . TYR A 301 ? 0.3248 0.1886 0.5871 -0.0304 -0.0279 0.029   301 TYR A N     
2465 C  CA    . TYR A 301 ? 0.3362 0.1935 0.5884 -0.03   -0.0303 0.0315  301 TYR A CA    
2466 C  C     . TYR A 301 ? 0.3462 0.2054 0.5932 -0.0292 -0.0284 0.0309  301 TYR A C     
2467 O  O     . TYR A 301 ? 0.3529 0.206  0.5913 -0.0287 -0.0308 0.0329  301 TYR A O     
2468 C  CB    . TYR A 301 ? 0.3378 0.1902 0.5795 -0.0296 -0.03   0.0338  301 TYR A CB    
2469 C  CG    . TYR A 301 ? 0.3449 0.1943 0.59   -0.0306 -0.0322 0.0351  301 TYR A CG    
2470 C  CD1   . TYR A 301 ? 0.356  0.1981 0.6012 -0.0313 -0.0374 0.0371  301 TYR A CD1   
2471 C  CD2   . TYR A 301 ? 0.3531 0.2067 0.6012 -0.031  -0.0295 0.0345  301 TYR A CD2   
2472 C  CE1   . TYR A 301 ? 0.364  0.2031 0.6121 -0.0323 -0.0397 0.0384  301 TYR A CE1   
2473 C  CE2   . TYR A 301 ? 0.3643 0.215  0.6157 -0.0321 -0.0318 0.0359  301 TYR A CE2   
2474 C  CZ    . TYR A 301 ? 0.3777 0.2211 0.6289 -0.0327 -0.0368 0.0378  301 TYR A CZ    
2475 O  OH    . TYR A 301 ? 0.4051 0.2454 0.6593 -0.0338 -0.0392 0.0392  301 TYR A OH    
2476 N  N     . SER A 302 ? 0.3457 0.2127 0.597  -0.0288 -0.0243 0.0284  302 SER A N     
2477 C  CA    . SER A 302 ? 0.3546 0.2237 0.6007 -0.0281 -0.0222 0.0279  302 SER A CA    
2478 C  C     . SER A 302 ? 0.3636 0.233  0.614  -0.0285 -0.0244 0.028   302 SER A C     
2479 O  O     . SER A 302 ? 0.3618 0.2329 0.6223 -0.0293 -0.026  0.0276  302 SER A O     
2480 C  CB    . SER A 302 ? 0.363  0.2402 0.6112 -0.0276 -0.017  0.0252  302 SER A CB    
2481 O  OG    . SER A 302 ? 0.3765 0.2595 0.6359 -0.028  -0.0159 0.0229  302 SER A OG    
2482 N  N     . VAL A 303 ? 0.3731 0.2407 0.6159 -0.028  -0.0244 0.0287  303 VAL A N     
2483 C  CA    . VAL A 303 ? 0.38   0.2486 0.6257 -0.0285 -0.026  0.029   303 VAL A CA    
2484 C  C     . VAL A 303 ? 0.3865 0.2612 0.6297 -0.0278 -0.0214 0.0272  303 VAL A C     
2485 O  O     . VAL A 303 ? 0.3917 0.2661 0.6264 -0.0267 -0.0189 0.0269  303 VAL A O     
2486 C  CB    . VAL A 303 ? 0.3921 0.2514 0.6306 -0.0287 -0.0315 0.0319  303 VAL A CB    
2487 C  CG1   . VAL A 303 ? 0.4006 0.2542 0.6428 -0.0296 -0.0363 0.0336  303 VAL A CG1   
2488 C  CG2   . VAL A 303 ? 0.4018 0.2555 0.6257 -0.0272 -0.0312 0.0327  303 VAL A CG2   
2489 N  N     . GLY A 304 ? 0.3833 0.2641 0.6343 -0.0283 -0.02   0.0262  304 GLY A N     
2490 C  CA    . GLY A 304 ? 0.389  0.276  0.6385 -0.0277 -0.0157 0.0244  304 GLY A CA    
2491 C  C     . GLY A 304 ? 0.3977 0.281  0.6367 -0.0272 -0.0164 0.0256  304 GLY A C     
2492 O  O     . GLY A 304 ? 0.4055 0.2829 0.6415 -0.0277 -0.0208 0.0278  304 GLY A O     
2493 N  N     . LEU A 305 ? 0.3933 0.2797 0.6266 -0.0262 -0.0125 0.0241  305 LEU A N     
2494 C  CA    . LEU A 305 ? 0.3997 0.2831 0.623  -0.0255 -0.0129 0.0249  305 LEU A CA    
2495 C  C     . LEU A 305 ? 0.3963 0.2868 0.623  -0.0258 -0.0098 0.0235  305 LEU A C     
2496 O  O     . LEU A 305 ? 0.3981 0.2943 0.6251 -0.0252 -0.0055 0.0214  305 LEU A O     
2497 C  CB    . LEU A 305 ? 0.4052 0.2862 0.6185 -0.0238 -0.011  0.0248  305 LEU A CB    
2498 C  CG    . LEU A 305 ? 0.4304 0.307  0.6323 -0.0225 -0.0118 0.0258  305 LEU A CG    
2499 C  CD1   . LEU A 305 ? 0.4413 0.3083 0.6375 -0.0225 -0.0174 0.0282  305 LEU A CD1   
2500 C  CD2   . LEU A 305 ? 0.4464 0.3228 0.6403 -0.0206 -0.0087 0.0255  305 LEU A CD2   
2501 N  N     . ALA A 306 ? 0.3853 0.2756 0.6148 -0.0268 -0.0122 0.0248  306 ALA A N     
2502 C  CA    . ALA A 306 ? 0.3777 0.2743 0.6109 -0.0274 -0.0098 0.0241  306 ALA A CA    
2503 C  C     . ALA A 306 ? 0.362  0.267  0.6069 -0.0279 -0.0066 0.0224  306 ALA A C     
2504 O  O     . ALA A 306 ? 0.357  0.2657 0.6088 -0.0288 -0.0067 0.0232  306 ALA A O     
2505 C  CB    . ALA A 306 ? 0.3857 0.2838 0.6104 -0.0263 -0.0068 0.0228  306 ALA A CB    
2506 N  N     . SER A 307 ? 0.3527 0.2606 0.5998 -0.0271 -0.0036 0.0201  307 SER A N     
2507 C  CA    . SER A 307 ? 0.342  0.2568 0.5992 -0.0271 -0.0006 0.018   307 SER A CA    
2508 C  C     . SER A 307 ? 0.3325 0.246  0.5924 -0.0267 -0.0008 0.0169  307 SER A C     
2509 O  O     . SER A 307 ? 0.3368 0.2468 0.5901 -0.0262 -0.0009 0.0168  307 SER A O     
2510 C  CB    . SER A 307 ? 0.3543 0.2755 0.6104 -0.0264 0.0041  0.0155  307 SER A CB    
2511 O  OG    . SER A 307 ? 0.3795 0.3029 0.6347 -0.027  0.0045  0.0165  307 SER A OG    
2512 N  N     . SER A 308 ? 0.3169 0.2332 0.5869 -0.0268 -0.0008 0.0163  308 SER A N     
2513 C  CA    . SER A 308 ? 0.3107 0.2257 0.5842 -0.0265 -0.0013 0.0152  308 SER A CA    
2514 C  C     . SER A 308 ? 0.3021 0.2199 0.5734 -0.0256 0.0023  0.0124  308 SER A C     
2515 O  O     . SER A 308 ? 0.3062 0.2212 0.5763 -0.0256 0.0014  0.0123  308 SER A O     
2516 C  CB    . SER A 308 ? 0.3222 0.2399 0.6072 -0.0264 -0.0019 0.0149  308 SER A CB    
2517 O  OG    . SER A 308 ? 0.3512 0.2762 0.6415 -0.0255 0.0023  0.0124  308 SER A OG    
2518 N  N     . ASP A 309 ? 0.2897 0.213  0.5604 -0.0251 0.006   0.0104  309 ASP A N     
2519 C  CA    . ASP A 309 ? 0.2858 0.2117 0.5547 -0.0244 0.0089  0.0078  309 ASP A CA    
2520 C  C     . ASP A 309 ? 0.2772 0.2028 0.5368 -0.0243 0.0104  0.0079  309 ASP A C     
2521 O  O     . ASP A 309 ? 0.2865 0.2151 0.5451 -0.0239 0.0129  0.0058  309 ASP A O     
2522 C  CB    . ASP A 309 ? 0.3133 0.2452 0.5886 -0.0235 0.012   0.0048  309 ASP A CB    
2523 C  CG    . ASP A 309 ? 0.3947 0.3309 0.6692 -0.0233 0.0145  0.0046  309 ASP A CG    
2524 O  OD1   . ASP A 309 ? 0.4154 0.3501 0.6874 -0.0241 0.0129  0.0072  309 ASP A OD1   
2525 O  OD2   . ASP A 309 ? 0.4274 0.3682 0.7035 -0.0224 0.0177  0.002   309 ASP A OD2   
2526 N  N     . LEU A 310 ? 0.26   0.1817 0.5128 -0.0246 0.0086  0.0104  310 LEU A N     
2527 C  CA    . LEU A 310 ? 0.2521 0.1732 0.4961 -0.0242 0.0099  0.0107  310 LEU A CA    
2528 C  C     . LEU A 310 ? 0.2474 0.1661 0.4894 -0.024  0.0095  0.011   310 LEU A C     
2529 O  O     . LEU A 310 ? 0.2471 0.1629 0.4928 -0.0244 0.0074  0.0117  310 LEU A O     
2530 C  CB    . LEU A 310 ? 0.2507 0.1674 0.4874 -0.0242 0.0077  0.0132  310 LEU A CB    
2531 C  CG    . LEU A 310 ? 0.2575 0.1771 0.4934 -0.0244 0.0088  0.013   310 LEU A CG    
2532 C  CD1   . LEU A 310 ? 0.2656 0.1797 0.4946 -0.0244 0.0057  0.0156  310 LEU A CD1   
2533 C  CD2   . LEU A 310 ? 0.2615 0.1858 0.4946 -0.0238 0.0124  0.0109  310 LEU A CD2   
2534 N  N     . PRO A 311 ? 0.2391 0.1591 0.476  -0.0236 0.0115  0.0107  311 PRO A N     
2535 C  CA    . PRO A 311 ? 0.2384 0.1567 0.4746 -0.0236 0.0113  0.0115  311 PRO A CA    
2536 C  C     . PRO A 311 ? 0.2445 0.1567 0.475  -0.0233 0.0089  0.0146  311 PRO A C     
2537 O  O     . PRO A 311 ? 0.2455 0.1568 0.4736 -0.0231 0.0093  0.0158  311 PRO A O     
2538 C  CB    . PRO A 311 ? 0.2446 0.1666 0.4775 -0.0232 0.0141  0.0106  311 PRO A CB    
2539 C  CG    . PRO A 311 ? 0.2488 0.1718 0.4766 -0.0226 0.0151  0.0105  311 PRO A CG    
2540 C  CD    . PRO A 311 ? 0.2292 0.1525 0.4615 -0.0231 0.0141  0.0097  311 PRO A CD    
2541 N  N     . PHE A 312 ? 0.2477 0.1557 0.4762 -0.0233 0.0064  0.016   312 PHE A N     
2542 C  CA    . PHE A 312 ? 0.2653 0.1665 0.4875 -0.0228 0.0037  0.0188  312 PHE A CA    
2543 C  C     . PHE A 312 ? 0.2845 0.1811 0.5091 -0.0235 -0.0001 0.0199  312 PHE A C     
2544 O  O     . PHE A 312 ? 0.2866 0.1854 0.5164 -0.0241 -0.0006 0.0189  312 PHE A O     
2545 C  CB    . PHE A 312 ? 0.2701 0.1691 0.4816 -0.0213 0.0046  0.0201  312 PHE A CB    
2546 C  CG    . PHE A 312 ? 0.2806 0.1817 0.4904 -0.0211 0.0053  0.019   312 PHE A CG    
2547 C  CD1   . PHE A 312 ? 0.2905 0.188  0.4994 -0.0214 0.0024  0.0199  312 PHE A CD1   
2548 C  CD2   . PHE A 312 ? 0.2895 0.1963 0.499  -0.0208 0.0087  0.0174  312 PHE A CD2   
2549 C  CE1   . PHE A 312 ? 0.2985 0.198  0.5061 -0.0215 0.0029  0.0192  312 PHE A CE1   
2550 C  CE2   . PHE A 312 ? 0.2967 0.2052 0.5044 -0.0207 0.0093  0.0166  312 PHE A CE2   
2551 C  CZ    . PHE A 312 ? 0.2943 0.1993 0.5013 -0.0211 0.0065  0.0175  312 PHE A CZ    
2552 N  N     . GLY A 313 ? 0.2965 0.1868 0.5175 -0.0233 -0.0029 0.0221  313 GLY A N     
2553 C  CA    . GLY A 313 ? 0.3117 0.1964 0.5343 -0.024  -0.0073 0.0236  313 GLY A CA    
2554 C  C     . GLY A 313 ? 0.3305 0.207  0.544  -0.0232 -0.01   0.0263  313 GLY A C     
2555 O  O     . GLY A 313 ? 0.3339 0.2094 0.5397 -0.0219 -0.0081 0.0271  313 GLY A O     
2556 N  N     . VAL A 314 ? 0.3414 0.2119 0.5556 -0.0239 -0.0146 0.0278  314 VAL A N     
2557 C  CA    . VAL A 314 ? 0.3641 0.2257 0.5687 -0.023  -0.0176 0.0304  314 VAL A CA    
2558 C  C     . VAL A 314 ? 0.3779 0.236  0.5866 -0.0239 -0.0204 0.0315  314 VAL A C     
2559 O  O     . VAL A 314 ? 0.3762 0.2357 0.5947 -0.0254 -0.0224 0.031   314 VAL A O     
2560 C  CB    . VAL A 314 ? 0.3816 0.2365 0.5794 -0.0225 -0.0215 0.0316  314 VAL A CB    
2561 C  CG1   . VAL A 314 ? 0.4002 0.2453 0.5859 -0.021  -0.0244 0.034   314 VAL A CG1   
2562 C  CG2   . VAL A 314 ? 0.388  0.2464 0.5823 -0.0217 -0.019  0.0304  314 VAL A CG2   
2563 N  N     . ILE A 315 ? 0.3895 0.2429 0.5906 -0.023  -0.0205 0.0334  315 ILE A N     
2564 C  CA    . ILE A 315 ? 0.4048 0.2531 0.6072 -0.0238 -0.0237 0.0351  315 ILE A CA    
2565 C  C     . ILE A 315 ? 0.4242 0.2623 0.6146 -0.0225 -0.0275 0.0374  315 ILE A C     
2566 O  O     . ILE A 315 ? 0.4305 0.2658 0.6098 -0.0205 -0.0258 0.0385  315 ILE A O     
2567 C  CB    . ILE A 315 ? 0.4087 0.2593 0.6108 -0.0236 -0.0208 0.0359  315 ILE A CB    
2568 C  CG1   . ILE A 315 ? 0.4096 0.2697 0.6222 -0.0247 -0.0171 0.0334  315 ILE A CG1   
2569 C  CG2   . ILE A 315 ? 0.4172 0.2615 0.6195 -0.0245 -0.0245 0.038   315 ILE A CG2   
2570 C  CD1   . ILE A 315 ? 0.4163 0.279  0.6413 -0.0264 -0.0189 0.0318  315 ILE A CD1   
2571 N  N     . ARG A 316 ? 0.4297 0.2624 0.6223 -0.0236 -0.0328 0.0381  316 ARG A N     
2572 C  CA    . ARG A 316 ? 0.4499 0.2718 0.631  -0.0225 -0.0373 0.0402  316 ARG A CA    
2573 C  C     . ARG A 316 ? 0.4643 0.2795 0.6367 -0.0214 -0.0382 0.0424  316 ARG A C     
2574 O  O     . ARG A 316 ? 0.4627 0.2804 0.6412 -0.0225 -0.0373 0.0427  316 ARG A O     
2575 C  CB    . ARG A 316 ? 0.4745 0.2925 0.6617 -0.0243 -0.0432 0.0407  316 ARG A CB    
2576 C  CG    . ARG A 316 ? 0.5172 0.3422 0.7134 -0.0253 -0.0422 0.039   316 ARG A CG    
2577 C  CD    . ARG A 316 ? 0.5664 0.3853 0.7622 -0.0262 -0.0482 0.0404  316 ARG A CD    
2578 N  NE    . ARG A 316 ? 0.6074 0.4286 0.8169 -0.0284 -0.0511 0.0407  316 ARG A NE    
2579 C  CZ    . ARG A 316 ? 0.6403 0.4648 0.8583 -0.0298 -0.0528 0.0408  316 ARG A CZ    
2580 N  NH1   . ARG A 316 ? 0.6363 0.4616 0.8502 -0.0295 -0.0523 0.0407  316 ARG A NH1   
2581 N  NH2   . ARG A 316 ? 0.6386 0.4656 0.8694 -0.0315 -0.0552 0.0413  316 ARG A NH2   
2582 N  N     . LYS A 317 ? 0.4794 0.2857 0.6371 -0.0192 -0.0399 0.044   317 LYS A N     
2583 C  CA    . LYS A 317 ? 0.4981 0.2977 0.646  -0.0178 -0.0404 0.0464  317 LYS A CA    
2584 C  C     . LYS A 317 ? 0.5144 0.3092 0.6673 -0.0198 -0.045  0.0478  317 LYS A C     
2585 O  O     . LYS A 317 ? 0.5202 0.3141 0.6712 -0.0196 -0.0438 0.0494  317 LYS A O     
2586 C  CB    . LYS A 317 ? 0.5225 0.3122 0.6531 -0.0147 -0.042  0.0477  317 LYS A CB    
2587 C  CG    . LYS A 317 ? 0.564  0.3443 0.6906 -0.015  -0.0489 0.048   317 LYS A CG    
2588 C  CD    . LYS A 317 ? 0.613  0.3834 0.7214 -0.0115 -0.0501 0.0489  317 LYS A CD    
2589 C  CE    . LYS A 317 ? 0.6543 0.4147 0.7573 -0.0116 -0.0571 0.0491  317 LYS A CE    
2590 N  NZ    . LYS A 317 ? 0.6848 0.4359 0.7693 -0.0076 -0.0577 0.0496  317 LYS A NZ    
2591 N  N     . GLU A 318 ? 0.5179 0.3107 0.6785 -0.0217 -0.05   0.0474  318 GLU A N     
2592 C  CA    . GLU A 318 ? 0.5265 0.315  0.6934 -0.0237 -0.0549 0.0487  318 GLU A CA    
2593 C  C     . GLU A 318 ? 0.5313 0.3282 0.711  -0.0254 -0.052  0.0478  318 GLU A C     
2594 O  O     . GLU A 318 ? 0.5353 0.3285 0.7174 -0.0265 -0.0549 0.0493  318 GLU A O     
2595 C  CB    . GLU A 318 ? 0.5478 0.3335 0.7212 -0.0254 -0.0606 0.0485  318 GLU A CB    
2596 C  CG    . GLU A 318 ? 0.6071 0.3823 0.7678 -0.0241 -0.0653 0.0497  318 GLU A CG    
2597 C  CD    . GLU A 318 ? 0.6816 0.4599 0.8388 -0.0229 -0.063  0.0483  318 GLU A CD    
2598 O  OE1   . GLU A 318 ? 0.683  0.4723 0.849  -0.0234 -0.0578 0.0463  318 GLU A OE1   
2599 O  OE2   . GLU A 318 ? 0.7229 0.4922 0.8681 -0.0215 -0.0665 0.0492  318 GLU A OE2   
2600 N  N     . SER A 319 ? 0.5305 0.3381 0.718  -0.0257 -0.0467 0.0455  319 SER A N     
2601 C  CA    . SER A 319 ? 0.5349 0.3503 0.734  -0.0271 -0.0439 0.0445  319 SER A CA    
2602 C  C     . SER A 319 ? 0.5381 0.3588 0.7336 -0.026  -0.0381 0.0445  319 SER A C     
2603 O  O     . SER A 319 ? 0.5378 0.3646 0.7422 -0.0272 -0.0359 0.0436  319 SER A O     
2604 C  CB    . SER A 319 ? 0.5518 0.3754 0.7647 -0.0283 -0.0429 0.0417  319 SER A CB    
2605 O  OG    . SER A 319 ? 0.5934 0.421  0.8037 -0.0274 -0.0401 0.0402  319 SER A OG    
2606 N  N     . ARG A 320 ? 0.5381 0.3563 0.7209 -0.0238 -0.0358 0.0455  320 ARG A N     
2607 C  CA    . ARG A 320 ? 0.5385 0.3617 0.7175 -0.0227 -0.0302 0.046   320 ARG A CA    
2608 C  C     . ARG A 320 ? 0.5444 0.3666 0.7239 -0.0234 -0.03   0.0484  320 ARG A C     
2609 O  O     . ARG A 320 ? 0.543  0.3725 0.7286 -0.0241 -0.0264 0.0481  320 ARG A O     
2610 C  CB    . ARG A 320 ? 0.5495 0.3693 0.7142 -0.0197 -0.0283 0.0469  320 ARG A CB    
2611 C  CG    . ARG A 320 ? 0.5707 0.3967 0.7321 -0.0183 -0.0223 0.0476  320 ARG A CG    
2612 C  CD    . ARG A 320 ? 0.5971 0.4208 0.746  -0.0151 -0.0201 0.0479  320 ARG A CD    
2613 N  NE    . ARG A 320 ? 0.6126 0.4419 0.758  -0.0135 -0.0144 0.0491  320 ARG A NE    
2614 C  CZ    . ARG A 320 ? 0.6344 0.4652 0.7721 -0.0108 -0.0112 0.0489  320 ARG A CZ    
2615 N  NH1   . ARG A 320 ? 0.6351 0.4617 0.7671 -0.0095 -0.0132 0.0473  320 ARG A NH1   
2616 N  NH2   . ARG A 320 ? 0.6254 0.4618 0.7612 -0.0094 -0.0061 0.0504  320 ARG A NH2   
2617 N  N     . ASN A 321 ? 0.5481 0.3611 0.7215 -0.0234 -0.0342 0.0509  321 ASN A N     
2618 C  CA    . ASN A 321 ? 0.5537 0.3651 0.7271 -0.0242 -0.0344 0.0535  321 ASN A CA    
2619 C  C     . ASN A 321 ? 0.5424 0.3601 0.7308 -0.0269 -0.0345 0.0522  321 ASN A C     
2620 O  O     . ASN A 321 ? 0.538  0.3603 0.7293 -0.0275 -0.0316 0.0533  321 ASN A O     
2621 C  CB    . ASN A 321 ? 0.585  0.3848 0.7498 -0.0239 -0.0397 0.0561  321 ASN A CB    
2622 C  CG    . ASN A 321 ? 0.647  0.4443 0.8109 -0.0248 -0.0401 0.0592  321 ASN A CG    
2623 O  OD1   . ASN A 321 ? 0.6759 0.4706 0.829  -0.023  -0.0377 0.062   321 ASN A OD1   
2624 N  ND2   . ASN A 321 ? 0.653  0.4511 0.8283 -0.0274 -0.0432 0.0588  321 ASN A ND2   
2625 N  N     . ASP A 322 ? 0.5363 0.3542 0.7344 -0.0283 -0.0379 0.05    322 ASP A N     
2626 C  CA    . ASP A 322 ? 0.5333 0.3564 0.7455 -0.0305 -0.0384 0.0484  322 ASP A CA    
2627 C  C     . ASP A 322 ? 0.5201 0.3535 0.7391 -0.0305 -0.0334 0.0459  322 ASP A C     
2628 O  O     . ASP A 322 ? 0.5193 0.3568 0.7459 -0.0318 -0.0324 0.0455  322 ASP A O     
2629 C  CB    . ASP A 322 ? 0.5596 0.3805 0.78   -0.0315 -0.0431 0.0468  322 ASP A CB    
2630 C  CG    . ASP A 322 ? 0.6329 0.4435 0.8483 -0.0318 -0.049  0.0493  322 ASP A CG    
2631 O  OD1   . ASP A 322 ? 0.6477 0.453  0.855  -0.0316 -0.0496 0.0523  322 ASP A OD1   
2632 O  OD2   . ASP A 322 ? 0.6672 0.4751 0.8869 -0.0323 -0.053  0.0486  322 ASP A OD2   
2633 N  N     . PHE A 323 ? 0.5086 0.3455 0.7242 -0.0292 -0.0304 0.0442  323 PHE A N     
2634 C  CA    . PHE A 323 ? 0.4987 0.3448 0.7195 -0.0291 -0.0257 0.0419  323 PHE A CA    
2635 C  C     . PHE A 323 ? 0.4986 0.3472 0.7155 -0.0289 -0.0223 0.0441  323 PHE A C     
2636 O  O     . PHE A 323 ? 0.4998 0.3537 0.7246 -0.0302 -0.0208 0.0433  323 PHE A O     
2637 C  CB    . PHE A 323 ? 0.4931 0.3415 0.7098 -0.0276 -0.0236 0.0401  323 PHE A CB    
2638 C  CG    . PHE A 323 ? 0.4898 0.3465 0.7079 -0.0271 -0.0185 0.0384  323 PHE A CG    
2639 C  CD1   . PHE A 323 ? 0.4907 0.3542 0.7194 -0.0281 -0.0171 0.0353  323 PHE A CD1   
2640 C  CD2   . PHE A 323 ? 0.4986 0.3561 0.7074 -0.0255 -0.0151 0.0399  323 PHE A CD2   
2641 C  CE1   . PHE A 323 ? 0.4946 0.3651 0.7243 -0.0277 -0.0128 0.0338  323 PHE A CE1   
2642 C  CE2   . PHE A 323 ? 0.5018 0.3668 0.7123 -0.0251 -0.0108 0.0385  323 PHE A CE2   
2643 C  CZ    . PHE A 323 ? 0.4935 0.3648 0.7143 -0.0264 -0.0098 0.0355  323 PHE A CZ    
2644 N  N     . ILE A 324 ? 0.4947 0.3389 0.6995 -0.0273 -0.0214 0.0471  324 ILE A N     
2645 C  CA    . ILE A 324 ? 0.49   0.3364 0.6904 -0.0269 -0.018  0.05    324 ILE A CA    
2646 C  C     . ILE A 324 ? 0.4839 0.3298 0.6905 -0.029  -0.0196 0.052   324 ILE A C     
2647 O  O     . ILE A 324 ? 0.4821 0.3338 0.6929 -0.0298 -0.0169 0.0528  324 ILE A O     
2648 C  CB    . ILE A 324 ? 0.5022 0.3431 0.6879 -0.0242 -0.0169 0.0529  324 ILE A CB    
2649 C  CG1   . ILE A 324 ? 0.5172 0.3594 0.6968 -0.022  -0.0148 0.0509  324 ILE A CG1   
2650 C  CG2   . ILE A 324 ? 0.5077 0.3506 0.6893 -0.0237 -0.0136 0.0567  324 ILE A CG2   
2651 C  CD1   . ILE A 324 ? 0.5279 0.3798 0.713  -0.022  -0.0102 0.0489  324 ILE A CD1   
2652 N  N     . ASN A 325 ? 0.4814 0.3205 0.6891 -0.03   -0.0245 0.0527  325 ASN A N     
2653 C  CA    . ASN A 325 ? 0.4828 0.3205 0.6964 -0.0321 -0.0269 0.0545  325 ASN A CA    
2654 C  C     . ASN A 325 ? 0.4692 0.3139 0.6963 -0.034  -0.0264 0.0518  325 ASN A C     
2655 O  O     . ASN A 325 ? 0.4649 0.3123 0.6961 -0.0354 -0.0256 0.0534  325 ASN A O     
2656 C  CB    . ASN A 325 ? 0.5084 0.3375 0.7216 -0.0328 -0.0326 0.0551  325 ASN A CB    
2657 C  CG    . ASN A 325 ? 0.5719 0.3925 0.7718 -0.0315 -0.034  0.0589  325 ASN A CG    
2658 O  OD1   . ASN A 325 ? 0.5936 0.4148 0.7847 -0.0301 -0.0305 0.0615  325 ASN A OD1   
2659 N  ND2   . ASN A 325 ? 0.5886 0.401  0.7868 -0.0318 -0.0393 0.0592  325 ASN A ND2   
2660 N  N     . ASP A 326 ? 0.459  0.3064 0.6925 -0.0339 -0.0269 0.0477  326 ASP A N     
2661 C  CA    . ASP A 326 ? 0.4529 0.3063 0.6982 -0.0351 -0.0264 0.0445  326 ASP A CA    
2662 C  C     . ASP A 326 ? 0.4458 0.3066 0.6918 -0.035  -0.0218 0.0442  326 ASP A C     
2663 O  O     . ASP A 326 ? 0.4408 0.3048 0.6942 -0.0365 -0.0219 0.0437  326 ASP A O     
2664 C  CB    . ASP A 326 ? 0.4681 0.3226 0.7193 -0.0346 -0.0276 0.0406  326 ASP A CB    
2665 C  CG    . ASP A 326 ? 0.5227 0.3717 0.7789 -0.0353 -0.0327 0.0405  326 ASP A CG    
2666 O  OD1   . ASP A 326 ? 0.5335 0.3778 0.7895 -0.0364 -0.0355 0.043   326 ASP A OD1   
2667 O  OD2   . ASP A 326 ? 0.5492 0.3988 0.8098 -0.0348 -0.0338 0.038   326 ASP A OD2   
2668 N  N     . VAL A 327 ? 0.4435 0.3064 0.6815 -0.0333 -0.0182 0.0446  327 VAL A N     
2669 C  CA    . VAL A 327 ? 0.4454 0.3152 0.6836 -0.0331 -0.014  0.0445  327 VAL A CA    
2670 C  C     . VAL A 327 ? 0.4549 0.3253 0.6923 -0.0342 -0.0132 0.0488  327 VAL A C     
2671 O  O     . VAL A 327 ? 0.4516 0.3272 0.6953 -0.0355 -0.012  0.0487  327 VAL A O     
2672 C  CB    . VAL A 327 ? 0.4499 0.3215 0.6797 -0.0309 -0.0106 0.0441  327 VAL A CB    
2673 C  CG1   . VAL A 327 ? 0.4523 0.3309 0.6821 -0.0306 -0.0063 0.0447  327 VAL A CG1   
2674 C  CG2   . VAL A 327 ? 0.45   0.3221 0.6822 -0.0302 -0.0113 0.0401  327 VAL A CG2   
2675 N  N     . CYS A 328 ? 0.4631 0.3278 0.693  -0.0338 -0.0143 0.0526  328 CYS A N     
2676 C  CA    . CYS A 328 ? 0.4715 0.3364 0.7002 -0.0348 -0.0136 0.0573  328 CYS A CA    
2677 C  C     . CYS A 328 ? 0.4715 0.336  0.7103 -0.0376 -0.017  0.0574  328 CYS A C     
2678 O  O     . CYS A 328 ? 0.4785 0.3467 0.721  -0.0391 -0.0159 0.0599  328 CYS A O     
2679 C  CB    . CYS A 328 ? 0.4937 0.352  0.7109 -0.0333 -0.0139 0.0612  328 CYS A CB    
2680 S  SG    . CYS A 328 ? 0.5753 0.4334 0.7793 -0.0296 -0.0098 0.0616  328 CYS A SG    
2681 N  N     . LYS A 329 ? 0.4638 0.324  0.7073 -0.0383 -0.0211 0.0548  329 LYS A N     
2682 C  CA    . LYS A 329 ? 0.4629 0.3222 0.716  -0.0407 -0.0247 0.0546  329 LYS A CA    
2683 C  C     . LYS A 329 ? 0.4549 0.3207 0.7173 -0.0416 -0.0236 0.0513  329 LYS A C     
2684 O  O     . LYS A 329 ? 0.4529 0.3202 0.721  -0.0435 -0.0246 0.0528  329 LYS A O     
2685 C  CB    . LYS A 329 ? 0.494  0.3468 0.7496 -0.0409 -0.0295 0.0531  329 LYS A CB    
2686 C  CG    . LYS A 329 ? 0.5615 0.4067 0.8082 -0.0407 -0.0315 0.0571  329 LYS A CG    
2687 C  CD    . LYS A 329 ? 0.6274 0.4716 0.8725 -0.0423 -0.0316 0.0623  329 LYS A CD    
2688 C  CE    . LYS A 329 ? 0.6801 0.5232 0.9129 -0.0407 -0.0283 0.0667  329 LYS A CE    
2689 N  NZ    . LYS A 329 ? 0.698  0.5486 0.9312 -0.0409 -0.0236 0.0689  329 LYS A NZ    
2690 N  N     . LEU A 330 ? 0.451  0.3206 0.714  -0.0401 -0.0214 0.0472  330 LEU A N     
2691 C  CA    . LEU A 330 ? 0.45   0.3254 0.7205 -0.0406 -0.0202 0.0438  330 LEU A CA    
2692 C  C     . LEU A 330 ? 0.4517 0.3323 0.7219 -0.0415 -0.0174 0.0465  330 LEU A C     
2693 O  O     . LEU A 330 ? 0.4456 0.3285 0.7231 -0.0432 -0.0186 0.0459  330 LEU A O     
2694 C  CB    . LEU A 330 ? 0.4485 0.3267 0.7181 -0.0387 -0.0181 0.0395  330 LEU A CB    
2695 C  CG    . LEU A 330 ? 0.4565 0.3405 0.7319 -0.0387 -0.0164 0.0357  330 LEU A CG    
2696 C  CD1   . LEU A 330 ? 0.4618 0.3447 0.7467 -0.0399 -0.0197 0.0332  330 LEU A CD1   
2697 C  CD2   . LEU A 330 ? 0.4587 0.3453 0.7318 -0.0368 -0.014  0.0323  330 LEU A CD2   
2698 N  N     . TYR A 331 ? 0.4584 0.3408 0.7203 -0.0403 -0.0138 0.0494  331 TYR A N     
2699 C  CA    . TYR A 331 ? 0.468  0.3561 0.7299 -0.0409 -0.0108 0.0522  331 TYR A CA    
2700 C  C     . TYR A 331 ? 0.4863 0.3734 0.7458 -0.042  -0.0107 0.0584  331 TYR A C     
2701 O  O     . TYR A 331 ? 0.4855 0.3777 0.7442 -0.0423 -0.0077 0.0616  331 TYR A O     
2702 C  CB    . TYR A 331 ? 0.4642 0.3561 0.7195 -0.0386 -0.0065 0.0514  331 TYR A CB    
2703 C  CG    . TYR A 331 ? 0.4642 0.3589 0.7232 -0.0379 -0.0061 0.0458  331 TYR A CG    
2704 C  CD1   . TYR A 331 ? 0.4684 0.3674 0.7349 -0.0392 -0.0063 0.0436  331 TYR A CD1   
2705 C  CD2   . TYR A 331 ? 0.4729 0.3657 0.7274 -0.0359 -0.0055 0.0429  331 TYR A CD2   
2706 C  CE1   . TYR A 331 ? 0.4747 0.3762 0.7437 -0.0384 -0.0056 0.0386  331 TYR A CE1   
2707 C  CE2   . TYR A 331 ? 0.4784 0.3742 0.7361 -0.0353 -0.0048 0.0382  331 TYR A CE2   
2708 C  CZ    . TYR A 331 ? 0.4817 0.3818 0.7464 -0.0365 -0.0047 0.036   331 TYR A CZ    
2709 O  OH    . TYR A 331 ? 0.4886 0.3913 0.7557 -0.0357 -0.0039 0.0314  331 TYR A OH    
2710 N  N     . ASN A 332 ? 0.4985 0.3794 0.7572 -0.0428 -0.0139 0.0603  332 ASN A N     
2711 C  CA    . ASN A 332 ? 0.5145 0.3937 0.7708 -0.044  -0.0142 0.0663  332 ASN A CA    
2712 C  C     . ASN A 332 ? 0.5273 0.408  0.7732 -0.0418 -0.0097 0.0703  332 ASN A C     
2713 O  O     . ASN A 332 ? 0.5268 0.4114 0.7727 -0.0426 -0.0074 0.0751  332 ASN A O     
2714 C  CB    . ASN A 332 ? 0.5295 0.412  0.7949 -0.0471 -0.0157 0.0684  332 ASN A CB    
2715 C  CG    . ASN A 332 ? 0.5858 0.4644 0.8512 -0.049  -0.0181 0.0736  332 ASN A CG    
2716 O  OD1   . ASN A 332 ? 0.6078 0.4796 0.8708 -0.0489 -0.0212 0.0735  332 ASN A OD1   
2717 N  ND2   . ASN A 332 ? 0.5995 0.4823 0.8679 -0.0508 -0.017  0.0786  332 ASN A ND2   
2718 N  N     . ILE A 333 ? 0.5347 0.4123 0.7718 -0.039  -0.0084 0.0685  333 ILE A N     
2719 C  CA    . ILE A 333 ? 0.5502 0.4278 0.776  -0.0363 -0.0045 0.0718  333 ILE A CA    
2720 C  C     . ILE A 333 ? 0.5701 0.4401 0.7889 -0.0361 -0.0065 0.0754  333 ILE A C     
2721 O  O     . ILE A 333 ? 0.5758 0.439  0.7929 -0.0359 -0.0102 0.0732  333 ILE A O     
2722 C  CB    . ILE A 333 ? 0.5557 0.4332 0.7752 -0.0334 -0.0025 0.0681  333 ILE A CB    
2723 C  CG1   . ILE A 333 ? 0.5619 0.4468 0.7885 -0.0338 -0.0007 0.0644  333 ILE A CG1   
2724 C  CG2   . ILE A 333 ? 0.5654 0.442  0.7725 -0.0302 0.0014  0.0714  333 ILE A CG2   
2725 C  CD1   . ILE A 333 ? 0.5812 0.4656 0.8037 -0.0317 0.0002  0.0602  333 ILE A CD1   
2726 N  N     . ASN A 334 ? 0.579  0.4504 0.7947 -0.0363 -0.0043 0.0812  334 ASN A N     
2727 C  CA    . ASN A 334 ? 0.5946 0.4588 0.8034 -0.0362 -0.0062 0.0852  334 ASN A CA    
2728 C  C     . ASN A 334 ? 0.6071 0.4692 0.8018 -0.0325 -0.0022 0.0887  334 ASN A C     
2729 O  O     . ASN A 334 ? 0.6135 0.4673 0.7991 -0.0313 -0.0042 0.0899  334 ASN A O     
2730 C  CB    . ASN A 334 ? 0.606  0.4722 0.8226 -0.0395 -0.0076 0.0896  334 ASN A CB    
2731 C  CG    . ASN A 334 ? 0.643  0.5073 0.871  -0.0428 -0.013  0.0865  334 ASN A CG    
2732 O  OD1   . ASN A 334 ? 0.6607 0.5216 0.8908 -0.0425 -0.016  0.0813  334 ASN A OD1   
2733 N  ND2   . ASN A 334 ? 0.6454 0.5118 0.8812 -0.046  -0.0146 0.0898  334 ASN A ND2   
2734 N  N     . ASP A 335 ? 0.6069 0.4761 0.7995 -0.0306 0.0032  0.0901  335 ASP A N     
2735 C  CA    . ASP A 335 ? 0.6185 0.4868 0.7979 -0.0266 0.0077  0.0933  335 ASP A CA    
2736 C  C     . ASP A 335 ? 0.6352 0.4942 0.8019 -0.0234 0.0061  0.0906  335 ASP A C     
2737 O  O     . ASP A 335 ? 0.6388 0.4974 0.8051 -0.0223 0.0055  0.0858  335 ASP A O     
2738 C  CB    . ASP A 335 ? 0.6282 0.5059 0.809  -0.0249 0.0132  0.0937  335 ASP A CB    
2739 C  CG    . ASP A 335 ? 0.6763 0.5544 0.8449 -0.0209 0.0184  0.0983  335 ASP A CG    
2740 O  OD1   . ASP A 335 ? 0.6869 0.5671 0.8552 -0.0213 0.0204  0.1043  335 ASP A OD1   
2741 O  OD2   . ASP A 335 ? 0.6959 0.572  0.8552 -0.0171 0.0204  0.096   335 ASP A OD2   
2742 N  N     . MET A 336 ? 0.6416 0.4929 0.7977 -0.0219 0.0052  0.0941  336 MET A N     
2743 C  CA    . MET A 336 ? 0.6526 0.4936 0.7955 -0.0189 0.0031  0.0924  336 MET A CA    
2744 C  C     . MET A 336 ? 0.6443 0.4859 0.7772 -0.0145 0.0069  0.0907  336 MET A C     
2745 O  O     . MET A 336 ? 0.6507 0.4858 0.7778 -0.013  0.0041  0.0869  336 MET A O     
2746 C  CB    . MET A 336 ? 0.6794 0.5124 0.8123 -0.0182 0.0018  0.0971  336 MET A CB    
2747 C  CG    . MET A 336 ? 0.7346 0.5713 0.8599 -0.0156 0.0079  0.103   336 MET A CG    
2748 S  SD    . MET A 336 ? 0.8314 0.6798 0.9708 -0.0193 0.0109  0.1082  336 MET A SD    
2749 C  CE    . MET A 336 ? 0.7931 0.6483 0.9232 -0.0146 0.0196  0.1131  336 MET A CE    
2750 N  N     . LYS A 337 ? 0.6297 0.4792 0.7615 -0.0125 0.0129  0.0934  337 LYS A N     
2751 C  CA    . LYS A 337 ? 0.6283 0.4787 0.7512 -0.0082 0.0166  0.0918  337 LYS A CA    
2752 C  C     . LYS A 337 ? 0.6081 0.462  0.7389 -0.0094 0.0152  0.0859  337 LYS A C     
2753 O  O     . LYS A 337 ? 0.6138 0.4627 0.7369 -0.0069 0.0141  0.0826  337 LYS A O     
2754 C  CB    . LYS A 337 ? 0.6572 0.5162 0.7788 -0.0059 0.0235  0.0964  337 LYS A CB    
2755 C  CG    . LYS A 337 ? 0.7207 0.5749 0.8279 -0.002  0.0265  0.1015  337 LYS A CG    
2756 C  CD    . LYS A 337 ? 0.7782 0.6323 0.8732 0.0037  0.0311  0.1011  337 LYS A CD    
2757 C  CE    . LYS A 337 ? 0.826  0.6796 0.9095 0.0079  0.0362  0.107   337 LYS A CE    
2758 N  NZ    . LYS A 337 ? 0.8549 0.7079 0.9262 0.0139  0.0405  0.1063  337 LYS A NZ    
2759 N  N     . ILE A 338 ? 0.5821 0.4441 0.7279 -0.0131 0.0149  0.0848  338 ILE A N     
2760 C  CA    . ILE A 338 ? 0.5643 0.4303 0.7184 -0.0145 0.0138  0.0794  338 ILE A CA    
2761 C  C     . ILE A 338 ? 0.5461 0.404  0.6994 -0.0153 0.0083  0.0751  338 ILE A C     
2762 O  O     . ILE A 338 ? 0.5488 0.4058 0.7    -0.014  0.0078  0.0712  338 ILE A O     
2763 C  CB    . ILE A 338 ? 0.5641 0.4389 0.7337 -0.0185 0.014   0.0794  338 ILE A CB    
2764 C  CG1   . ILE A 338 ? 0.5741 0.458  0.7457 -0.0177 0.0194  0.0835  338 ILE A CG1   
2765 C  CG2   . ILE A 338 ? 0.5654 0.443  0.7434 -0.0201 0.012   0.0736  338 ILE A CG2   
2766 C  CD1   . ILE A 338 ? 0.5824 0.4746 0.7692 -0.0219 0.019   0.0842  338 ILE A CD1   
2767 N  N     . ILE A 339 ? 0.527  0.3793 0.6824 -0.0175 0.004   0.076   339 ILE A N     
2768 C  CA    . ILE A 339 ? 0.5167 0.3615 0.6725 -0.0185 -0.0015 0.0725  339 ILE A CA    
2769 C  C     . ILE A 339 ? 0.5111 0.3472 0.6524 -0.015  -0.0025 0.072   339 ILE A C     
2770 O  O     . ILE A 339 ? 0.5114 0.3444 0.6529 -0.0149 -0.0054 0.0682  339 ILE A O     
2771 C  CB    . ILE A 339 ? 0.5218 0.3627 0.6831 -0.0216 -0.0057 0.0742  339 ILE A CB    
2772 C  CG1   . ILE A 339 ? 0.5251 0.3742 0.7009 -0.0251 -0.0051 0.0744  339 ILE A CG1   
2773 C  CG2   . ILE A 339 ? 0.5309 0.3643 0.6934 -0.0226 -0.0115 0.0709  339 ILE A CG2   
2774 C  CD1   . ILE A 339 ? 0.538  0.3838 0.719  -0.028  -0.0088 0.0768  339 ILE A CD1   
2775 N  N     . LYS A 340 ? 0.505  0.3374 0.6337 -0.0119 -0.0001 0.0758  340 LYS A N     
2776 C  CA    . LYS A 340 ? 0.5097 0.3329 0.6232 -0.0081 -0.0012 0.0753  340 LYS A CA    
2777 C  C     . LYS A 340 ? 0.5014 0.3277 0.6128 -0.0059 0.001   0.072   340 LYS A C     
2778 O  O     . LYS A 340 ? 0.5083 0.3277 0.6138 -0.0047 -0.0023 0.0693  340 LYS A O     
2779 C  CB    . LYS A 340 ? 0.5405 0.3598 0.6405 -0.0047 0.0019  0.0802  340 LYS A CB    
2780 C  CG    . LYS A 340 ? 0.5987 0.4093 0.6942 -0.0058 -0.002  0.083   340 LYS A CG    
2781 C  CD    . LYS A 340 ? 0.6627 0.4694 0.7435 -0.0019 0.0015  0.0879  340 LYS A CD    
2782 C  CE    . LYS A 340 ? 0.7103 0.515  0.7922 -0.004  0.0006  0.0924  340 LYS A CE    
2783 N  NZ    . LYS A 340 ? 0.7337 0.5488 0.8207 -0.0043 0.0067  0.0969  340 LYS A NZ    
2784 N  N     . GLU A 341 ? 0.4859 0.3225 0.6027 -0.0056 0.0062  0.0722  341 GLU A N     
2785 C  CA    . GLU A 341 ? 0.4813 0.3217 0.597  -0.0037 0.0084  0.0692  341 GLU A CA    
2786 C  C     . GLU A 341 ? 0.4733 0.3144 0.5983 -0.0064 0.0047  0.0644  341 GLU A C     
2787 O  O     . GLU A 341 ? 0.4755 0.3133 0.5956 -0.0048 0.0033  0.0616  341 GLU A O     
2788 C  CB    . GLU A 341 ? 0.4959 0.3475 0.6168 -0.0032 0.0144  0.0709  341 GLU A CB    
2789 N  N     . LEU A 342 ? 0.4641 0.3091 0.6021 -0.0104 0.0028  0.0636  342 LEU A N     
2790 C  CA    . LEU A 342 ? 0.4666 0.3129 0.6144 -0.013  -0.0004 0.0594  342 LEU A CA    
2791 C  C     . LEU A 342 ? 0.4843 0.3207 0.6275 -0.013  -0.006  0.058   342 LEU A C     
2792 O  O     . LEU A 342 ? 0.4869 0.3234 0.634  -0.0137 -0.0081 0.0546  342 LEU A O     
2793 C  CB    . LEU A 342 ? 0.4561 0.3077 0.6179 -0.0168 -0.0013 0.0592  342 LEU A CB    
2794 C  CG    . LEU A 342 ? 0.4594 0.3213 0.6293 -0.0178 0.0029  0.0596  342 LEU A CG    
2795 C  CD1   . LEU A 342 ? 0.4625 0.3272 0.6442 -0.0213 0.0011  0.0599  342 LEU A CD1   
2796 C  CD2   . LEU A 342 ? 0.4601 0.3274 0.6339 -0.0176 0.0044  0.0557  342 LEU A CD2   
2797 N  N     . LYS A 343 ? 0.4933 0.3214 0.6289 -0.0123 -0.0086 0.0607  343 LYS A N     
2798 C  CA    . LYS A 343 ? 0.506  0.3242 0.638  -0.0127 -0.0145 0.0598  343 LYS A CA    
2799 C  C     . LYS A 343 ? 0.5231 0.3328 0.6405 -0.0093 -0.016  0.0596  343 LYS A C     
2800 O  O     . LYS A 343 ? 0.5329 0.3327 0.6446 -0.0092 -0.0211 0.06    343 LYS A O     
2801 C  CB    . LYS A 343 ? 0.5256 0.3383 0.6577 -0.0142 -0.0177 0.0626  343 LYS A CB    
2802 C  CG    . LYS A 343 ? 0.5584 0.3769 0.7061 -0.0181 -0.0188 0.0618  343 LYS A CG    
2803 C  CD    . LYS A 343 ? 0.5958 0.4082 0.7431 -0.0196 -0.0222 0.0647  343 LYS A CD    
2804 C  CE    . LYS A 343 ? 0.6121 0.4287 0.7745 -0.0232 -0.0244 0.0636  343 LYS A CE    
2805 N  NZ    . LYS A 343 ? 0.6301 0.4395 0.7918 -0.0247 -0.0287 0.0661  343 LYS A NZ    
2806 N  N     . GLU A 344 ? 0.5241 0.3369 0.6357 -0.0065 -0.0121 0.0588  344 GLU A N     
2807 C  CA    . GLU A 344 ? 0.5376 0.3416 0.6349 -0.0031 -0.0139 0.0583  344 GLU A CA    
2808 C  C     . GLU A 344 ? 0.5388 0.3372 0.6389 -0.0048 -0.02   0.0557  344 GLU A C     
2809 O  O     . GLU A 344 ? 0.5373 0.3422 0.6503 -0.0077 -0.0206 0.0533  344 GLU A O     
2810 C  CB    . GLU A 344 ? 0.567  0.3764 0.6597 -0.0001 -0.0088 0.0575  344 GLU A CB    
2811 C  CG    . GLU A 344 ? 0.6357 0.4355 0.7121 0.0041  -0.0102 0.0574  344 GLU A CG    
2812 C  CD    . GLU A 344 ? 0.7145 0.5191 0.7857 0.0074  -0.0052 0.0568  344 GLU A CD    
2813 O  OE1   . GLU A 344 ? 0.7108 0.5254 0.7878 0.0074  0.0003  0.0578  344 GLU A OE1   
2814 O  OE2   . GLU A 344 ? 0.7576 0.5558 0.8192 0.01    -0.0072 0.0553  344 GLU A OE2   
2815 N  N     . ASP A 345 ? 0.5372 0.3234 0.6256 -0.0032 -0.0249 0.0564  345 ASP A N     
2816 C  CA    . ASP A 345 ? 0.5307 0.311  0.6219 -0.005  -0.0314 0.0546  345 ASP A CA    
2817 C  C     . ASP A 345 ? 0.5076 0.2899 0.5991 -0.0044 -0.0314 0.0519  345 ASP A C     
2818 O  O     . ASP A 345 ? 0.5155 0.2891 0.595  -0.0019 -0.0342 0.0518  345 ASP A O     
2819 C  CB    . ASP A 345 ? 0.575  0.3411 0.6537 -0.0037 -0.0373 0.0564  345 ASP A CB    
2820 C  CG    . ASP A 345 ? 0.6618 0.422  0.7455 -0.0062 -0.0446 0.0553  345 ASP A CG    
2821 O  OD1   . ASP A 345 ? 0.6726 0.4383 0.7713 -0.0099 -0.046  0.0545  345 ASP A OD1   
2822 O  OD2   . ASP A 345 ? 0.7031 0.4531 0.7758 -0.0045 -0.0491 0.0552  345 ASP A OD2   
2823 N  N     . ALA A 346 ? 0.4799 0.2731 0.5847 -0.0066 -0.0287 0.0498  346 ALA A N     
2824 C  CA    . ALA A 346 ? 0.4687 0.265  0.5756 -0.0066 -0.0285 0.0474  346 ALA A CA    
2825 C  C     . ALA A 346 ? 0.4475 0.2544 0.5715 -0.01   -0.0271 0.0453  346 ALA A C     
2826 O  O     . ALA A 346 ? 0.443  0.2562 0.5758 -0.0117 -0.0247 0.0455  346 ALA A O     
2827 C  CB    . ALA A 346 ? 0.4727 0.2719 0.5709 -0.0031 -0.0233 0.0472  346 ALA A CB    
2828 N  N     . ASP A 347 ? 0.4327 0.2415 0.5611 -0.011  -0.0287 0.0433  347 ASP A N     
2829 C  CA    . ASP A 347 ? 0.4163 0.2351 0.5599 -0.0138 -0.0269 0.0411  347 ASP A CA    
2830 C  C     . ASP A 347 ? 0.3997 0.2284 0.5463 -0.0132 -0.0203 0.0402  347 ASP A C     
2831 O  O     . ASP A 347 ? 0.4036 0.2323 0.541  -0.0105 -0.0172 0.0406  347 ASP A O     
2832 C  CB    . ASP A 347 ? 0.4363 0.2552 0.5823 -0.0146 -0.0294 0.0396  347 ASP A CB    
2833 C  CG    . ASP A 347 ? 0.4994 0.3089 0.6435 -0.0155 -0.0363 0.0407  347 ASP A CG    
2834 O  OD1   . ASP A 347 ? 0.5132 0.3187 0.6601 -0.0167 -0.0395 0.042   347 ASP A OD1   
2835 O  OD2   . ASP A 347 ? 0.5249 0.3309 0.6651 -0.0151 -0.039  0.0405  347 ASP A OD2   
2836 N  N     . LEU A 348 ? 0.3767 0.2136 0.536  -0.0155 -0.0183 0.039   348 LEU A N     
2837 C  CA    . LEU A 348 ? 0.3606 0.2066 0.524  -0.0154 -0.0128 0.0383  348 LEU A CA    
2838 C  C     . LEU A 348 ? 0.3441 0.1981 0.518  -0.0171 -0.0113 0.0354  348 LEU A C     
2839 O  O     . LEU A 348 ? 0.3417 0.1968 0.5249 -0.0192 -0.0137 0.0343  348 LEU A O     
2840 C  CB    . LEU A 348 ? 0.3596 0.2072 0.5282 -0.0166 -0.0121 0.0396  348 LEU A CB    
2841 C  CG    . LEU A 348 ? 0.3771 0.2333 0.5503 -0.0168 -0.0072 0.0394  348 LEU A CG    
2842 C  CD1   . LEU A 348 ? 0.3913 0.247  0.5536 -0.014  -0.0038 0.0415  348 LEU A CD1   
2843 C  CD2   . LEU A 348 ? 0.3863 0.2438 0.5671 -0.0188 -0.0078 0.0404  348 LEU A CD2   
2844 N  N     . ILE A 349 ? 0.3317 0.191  0.5038 -0.016  -0.0076 0.0342  349 ILE A N     
2845 C  CA    . ILE A 349 ? 0.3266 0.1935 0.5076 -0.0174 -0.0059 0.0314  349 ILE A CA    
2846 C  C     . ILE A 349 ? 0.3254 0.1997 0.5137 -0.0183 -0.0024 0.0307  349 ILE A C     
2847 O  O     . ILE A 349 ? 0.3328 0.2091 0.5168 -0.0171 0.0007  0.0319  349 ILE A O     
2848 C  CB    . ILE A 349 ? 0.3352 0.2034 0.5105 -0.016  -0.0043 0.0305  349 ILE A CB    
2849 C  CG1   . ILE A 349 ? 0.3542 0.2145 0.5234 -0.0155 -0.0087 0.0311  349 ILE A CG1   
2850 C  CG2   . ILE A 349 ? 0.3356 0.2125 0.5199 -0.0173 -0.0017 0.0278  349 ILE A CG2   
2851 C  CD1   . ILE A 349 ? 0.3745 0.2346 0.537  -0.014  -0.008  0.0305  349 ILE A CD1   
2852 N  N     . VAL A 350 ? 0.3172 0.1953 0.5165 -0.0204 -0.0029 0.0291  350 VAL A N     
2853 C  CA    . VAL A 350 ? 0.3148 0.1992 0.5213 -0.0214 -0.0002 0.0281  350 VAL A CA    
2854 C  C     . VAL A 350 ? 0.3156 0.2071 0.5267 -0.0217 0.0025  0.0253  350 VAL A C     
2855 O  O     . VAL A 350 ? 0.3171 0.2097 0.5326 -0.0223 0.0015  0.0235  350 VAL A O     
2856 C  CB    . VAL A 350 ? 0.3153 0.1988 0.5303 -0.0231 -0.0027 0.0281  350 VAL A CB    
2857 C  CG1   . VAL A 350 ? 0.3185 0.208  0.541  -0.0242 -0.0004 0.0269  350 VAL A CG1   
2858 C  CG2   . VAL A 350 ? 0.3216 0.1978 0.5313 -0.0229 -0.0054 0.0311  350 VAL A CG2   
2859 N  N     . CYS A 351 ? 0.3127 0.2089 0.5226 -0.0212 0.0058  0.0252  351 CYS A N     
2860 C  CA    . CYS A 351 ? 0.3132 0.2158 0.5269 -0.0214 0.0084  0.0225  351 CYS A CA    
2861 C  C     . CYS A 351 ? 0.3065 0.2138 0.5277 -0.0227 0.0096  0.0216  351 CYS A C     
2862 O  O     . CYS A 351 ? 0.3093 0.2167 0.5292 -0.0227 0.0103  0.0238  351 CYS A O     
2863 C  CB    . CYS A 351 ? 0.3259 0.2298 0.5317 -0.0197 0.0108  0.0231  351 CYS A CB    
2864 S  SG    . CYS A 351 ? 0.3668 0.2778 0.5759 -0.02   0.0135  0.02    351 CYS A SG    
2865 N  N     . MET A 352 ? 0.2958 0.2066 0.5246 -0.0237 0.0098  0.0187  352 MET A N     
2866 C  CA    . MET A 352 ? 0.2901 0.2044 0.5258 -0.0248 0.0104  0.0175  352 MET A CA    
2867 C  C     . MET A 352 ? 0.285  0.2047 0.5218 -0.0247 0.0129  0.0149  352 MET A C     
2868 O  O     . MET A 352 ? 0.2902 0.2114 0.5279 -0.0244 0.0134  0.0127  352 MET A O     
2869 C  CB    . MET A 352 ? 0.2939 0.2067 0.5374 -0.0258 0.008   0.016   352 MET A CB    
2870 C  CG    . MET A 352 ? 0.3212 0.2285 0.5638 -0.0261 0.0052  0.0186  352 MET A CG    
2871 S  SD    . MET A 352 ? 0.3973 0.3028 0.6493 -0.027  0.0022  0.0169  352 MET A SD    
2872 C  CE    . MET A 352 ? 0.3744 0.2833 0.6333 -0.028  0.0028  0.0152  352 MET A CE    
2873 N  N     . LEU A 353 ? 0.2726 0.1954 0.5092 -0.025  0.0144  0.0156  353 LEU A N     
2874 C  CA    . LEU A 353 ? 0.2641 0.1916 0.5011 -0.0249 0.0164  0.0134  353 LEU A CA    
2875 C  C     . LEU A 353 ? 0.2502 0.1802 0.4925 -0.0261 0.0163  0.0131  353 LEU A C     
2876 O  O     . LEU A 353 ? 0.2477 0.1769 0.4903 -0.0267 0.0158  0.0159  353 LEU A O     
2877 C  CB    . LEU A 353 ? 0.2704 0.1991 0.5    -0.0236 0.0185  0.0152  353 LEU A CB    
2878 C  CG    . LEU A 353 ? 0.3005 0.2264 0.5238 -0.0223 0.0184  0.0156  353 LEU A CG    
2879 C  CD1   . LEU A 353 ? 0.3129 0.2391 0.5285 -0.0208 0.0201  0.0177  353 LEU A CD1   
2880 C  CD2   . LEU A 353 ? 0.3112 0.2389 0.5361 -0.0224 0.0188  0.0125  353 LEU A CD2   
2881 N  N     . LYS A 354 ? 0.2412 0.174  0.4871 -0.0264 0.0167  0.0098  354 LYS A N     
2882 C  CA    . LYS A 354 ? 0.2399 0.1746 0.4901 -0.0276 0.0162  0.0093  354 LYS A CA    
2883 C  C     . LYS A 354 ? 0.2394 0.1771 0.4864 -0.0276 0.0177  0.0119  354 LYS A C     
2884 O  O     . LYS A 354 ? 0.2396 0.178  0.4891 -0.0287 0.017   0.0143  354 LYS A O     
2885 C  CB    . LYS A 354 ? 0.2556 0.192  0.5093 -0.0276 0.0161  0.005   354 LYS A CB    
2886 C  CG    . LYS A 354 ? 0.2848 0.2216 0.5433 -0.0289 0.0145  0.0043  354 LYS A CG    
2887 C  CD    . LYS A 354 ? 0.3206 0.2572 0.5821 -0.0286 0.0139  -0.0002 354 LYS A CD    
2888 C  CE    . LYS A 354 ? 0.3638 0.2998 0.6298 -0.0298 0.0115  -0.0009 354 LYS A CE    
2889 N  NZ    . LYS A 354 ? 0.3936 0.3323 0.6578 -0.0305 0.012   -0.0007 354 LYS A NZ    
2890 N  N     . GLY A 355 ? 0.237  0.1764 0.4785 -0.0264 0.0197  0.0117  355 GLY A N     
2891 C  CA    . GLY A 355 ? 0.2452 0.1874 0.4832 -0.026  0.0214  0.0142  355 GLY A CA    
2892 C  C     . GLY A 355 ? 0.2514 0.1975 0.4923 -0.0269 0.0216  0.0131  355 GLY A C     
2893 O  O     . GLY A 355 ? 0.2549 0.2037 0.4924 -0.0261 0.0233  0.0133  355 GLY A O     
2894 N  N     . PHE A 356 ? 0.2496 0.1955 0.4966 -0.0284 0.0196  0.012   356 PHE A N     
2895 C  CA    . PHE A 356 ? 0.2563 0.2051 0.5062 -0.0295 0.0191  0.0113  356 PHE A CA    
2896 C  C     . PHE A 356 ? 0.2776 0.2251 0.5311 -0.0302 0.0173  0.007   356 PHE A C     
2897 O  O     . PHE A 356 ? 0.2847 0.2291 0.541  -0.0303 0.0159  0.0054  356 PHE A O     
2898 C  CB    . PHE A 356 ? 0.2448 0.1951 0.4983 -0.0309 0.0183  0.0155  356 PHE A CB    
2899 C  CG    . PHE A 356 ? 0.2413 0.1928 0.4906 -0.0297 0.0205  0.0198  356 PHE A CG    
2900 C  CD1   . PHE A 356 ? 0.2465 0.195  0.4944 -0.0292 0.0204  0.022   356 PHE A CD1   
2901 C  CD2   . PHE A 356 ? 0.244  0.1991 0.4897 -0.0286 0.0227  0.0213  356 PHE A CD2   
2902 C  CE1   . PHE A 356 ? 0.2524 0.2012 0.495  -0.0276 0.0226  0.0255  356 PHE A CE1   
2903 C  CE2   . PHE A 356 ? 0.2505 0.2062 0.4915 -0.0269 0.0249  0.0249  356 PHE A CE2   
2904 C  CZ    . PHE A 356 ? 0.2477 0.2    0.4867 -0.0263 0.0249  0.0269  356 PHE A CZ    
2905 N  N     . LYS A 357 ? 0.2847 0.2342 0.5379 -0.0304 0.0172  0.0051  357 LYS A N     
2906 C  CA    . LYS A 357 ? 0.2963 0.2443 0.5518 -0.0308 0.0155  0.0008  357 LYS A CA    
2907 C  C     . LYS A 357 ? 0.3077 0.2543 0.5691 -0.0327 0.0121  0.0017  357 LYS A C     
2908 O  O     . LYS A 357 ? 0.3127 0.2605 0.5766 -0.0339 0.0115  0.0059  357 LYS A O     
2909 C  CB    . LYS A 357 ? 0.3117 0.2618 0.5633 -0.0302 0.0167  -0.0014 357 LYS A CB    
2910 C  CG    . LYS A 357 ? 0.3504 0.3005 0.5972 -0.0284 0.0191  -0.0037 357 LYS A CG    
2911 C  CD    . LYS A 357 ? 0.4043 0.3569 0.6465 -0.0279 0.0207  -0.0046 357 LYS A CD    
2912 C  CE    . LYS A 357 ? 0.4532 0.4081 0.6922 -0.0276 0.0223  -0.0008 357 LYS A CE    
2913 N  NZ    . LYS A 357 ? 0.482  0.4395 0.7174 -0.0273 0.0232  -0.0012 357 LYS A NZ    
2914 N  N     . PRO A 358 ? 0.3091 0.2531 0.5728 -0.0329 0.0098  -0.0021 358 PRO A N     
2915 C  CA    . PRO A 358 ? 0.31   0.2519 0.5793 -0.0348 0.006   -0.0012 358 PRO A CA    
2916 C  C     . PRO A 358 ? 0.322  0.2668 0.5938 -0.0368 0.0047  0.0029  358 PRO A C     
2917 O  O     . PRO A 358 ? 0.325  0.269  0.602  -0.0386 0.0023  0.0058  358 PRO A O     
2918 C  CB    . PRO A 358 ? 0.3166 0.2555 0.5855 -0.0342 0.0041  -0.0065 358 PRO A CB    
2919 C  CG    . PRO A 358 ? 0.3241 0.2627 0.5892 -0.0319 0.0069  -0.0097 358 PRO A CG    
2920 C  CD    . PRO A 358 ? 0.3054 0.2477 0.5665 -0.0313 0.0104  -0.0071 358 PRO A CD    
2921 N  N     . ARG A 359 ? 0.3254 0.2737 0.5943 -0.0366 0.0063  0.0035  359 ARG A N     
2922 C  CA    . ARG A 359 ? 0.3349 0.2865 0.6069 -0.0384 0.0052  0.0077  359 ARG A CA    
2923 C  C     . ARG A 359 ? 0.3384 0.2941 0.6103 -0.0382 0.008   0.0131  359 ARG A C     
2924 O  O     . ARG A 359 ? 0.3321 0.2913 0.6072 -0.0395 0.0076  0.0172  359 ARG A O     
2925 C  CB    . ARG A 359 ? 0.3576 0.3109 0.6273 -0.0384 0.0049  0.0059  359 ARG A CB    
2926 C  CG    . ARG A 359 ? 0.4087 0.3575 0.6778 -0.0384 0.0019  0.0006  359 ARG A CG    
2927 C  CD    . ARG A 359 ? 0.4662 0.416  0.7322 -0.0384 0.0013  -0.0013 359 ARG A CD    
2928 N  NE    . ARG A 359 ? 0.5296 0.4811 0.789  -0.0362 0.0053  -0.0031 359 ARG A NE    
2929 C  CZ    . ARG A 359 ? 0.575  0.5261 0.8299 -0.0355 0.0053  -0.0064 359 ARG A CZ    
2930 N  NH1   . ARG A 359 ? 0.5768 0.5252 0.8323 -0.0365 0.0016  -0.0084 359 ARG A NH1   
2931 N  NH2   . ARG A 359 ? 0.5739 0.5267 0.8231 -0.0337 0.0089  -0.0076 359 ARG A NH2   
2932 N  N     . GLY A 360 ? 0.3478 0.3027 0.6163 -0.0366 0.0106  0.0133  360 GLY A N     
2933 C  CA    . GLY A 360 ? 0.363  0.3206 0.6298 -0.0359 0.0133  0.018   360 GLY A CA    
2934 C  C     . GLY A 360 ? 0.3826 0.343  0.6431 -0.0339 0.0167  0.0181  360 GLY A C     
2935 O  O     . GLY A 360 ? 0.3886 0.351  0.6466 -0.0327 0.0191  0.0217  360 GLY A O     
2936 N  N     . ASP A 361 ? 0.3886 0.3488 0.6462 -0.0332 0.0168  0.0141  361 ASP A N     
2937 C  CA    . ASP A 361 ? 0.3974 0.3598 0.6489 -0.0314 0.0196  0.0137  361 ASP A CA    
2938 C  C     . ASP A 361 ? 0.4027 0.3626 0.6491 -0.0296 0.0216  0.0126  361 ASP A C     
2939 O  O     . ASP A 361 ? 0.4026 0.3592 0.6498 -0.0297 0.0206  0.0098  361 ASP A O     
2940 C  CB    . ASP A 361 ? 0.4233 0.3864 0.6736 -0.0316 0.0189  0.0102  361 ASP A CB    
2941 C  CG    . ASP A 361 ? 0.491  0.4504 0.7414 -0.0319 0.0171  0.0052  361 ASP A CG    
2942 O  OD1   . ASP A 361 ? 0.5018 0.4586 0.7567 -0.033  0.0147  0.0046  361 ASP A OD1   
2943 O  OD2   . ASP A 361 ? 0.5245 0.4835 0.7703 -0.0307 0.0183  0.0019  361 ASP A OD2   
2944 N  N     . ASP A 362 ? 0.4041 0.3654 0.6455 -0.0279 0.0241  0.0148  362 ASP A N     
2945 C  CA    . ASP A 362 ? 0.4151 0.3735 0.6516 -0.0263 0.0253  0.0143  362 ASP A CA    
2946 C  C     . ASP A 362 ? 0.4176 0.3744 0.651  -0.0257 0.0256  0.0101  362 ASP A C     
2947 O  O     . ASP A 362 ? 0.4206 0.3791 0.6526 -0.0257 0.0259  0.0081  362 ASP A O     
2948 C  CB    . ASP A 362 ? 0.4481 0.4074 0.6794 -0.0244 0.0276  0.0179  362 ASP A CB    
2949 C  CG    . ASP A 362 ? 0.5292 0.4901 0.7549 -0.0228 0.0293  0.0171  362 ASP A CG    
2950 O  OD1   . ASP A 362 ? 0.5383 0.4966 0.7591 -0.0216 0.0297  0.0152  362 ASP A OD1   
2951 O  OD2   . ASP A 362 ? 0.5674 0.5321 0.7939 -0.0227 0.03    0.0186  362 ASP A OD2   
2952 N  N     . ASN A 363 ? 0.4129 0.3664 0.6451 -0.0252 0.0254  0.0091  363 ASN A N     
2953 C  CA    . ASN A 363 ? 0.4133 0.3654 0.6433 -0.0246 0.0258  0.0058  363 ASN A CA    
2954 C  C     . ASN A 363 ? 0.4075 0.3598 0.6308 -0.0231 0.0274  0.0068  363 ASN A C     
2955 O  O     . ASN A 363 ? 0.4153 0.3657 0.6356 -0.0221 0.0277  0.0093  363 ASN A O     
2956 C  CB    . ASN A 363 ? 0.4328 0.3815 0.6648 -0.0246 0.0248  0.0053  363 ASN A CB    
2957 C  CG    . ASN A 363 ? 0.4723 0.4198 0.7107 -0.0258 0.0229  0.0039  363 ASN A CG    
2958 O  OD1   . ASN A 363 ? 0.4849 0.4338 0.7264 -0.0268 0.022   0.0029  363 ASN A OD1   
2959 N  ND2   . ASN A 363 ? 0.4772 0.4218 0.7178 -0.0258 0.0219  0.0038  363 ASN A ND2   
2960 N  N     . ARG A 364 ? 0.3948 0.3489 0.6154 -0.0228 0.0282  0.0049  364 ARG A N     
2961 C  CA    . ARG A 364 ? 0.3887 0.3426 0.6028 -0.0213 0.0294  0.0057  364 ARG A CA    
2962 C  C     . ARG A 364 ? 0.3819 0.3323 0.5932 -0.0207 0.0291  0.0059  364 ARG A C     
2963 O  O     . ARG A 364 ? 0.3854 0.334  0.5919 -0.0194 0.0294  0.0081  364 ARG A O     
2964 C  CB    . ARG A 364 ? 0.398  0.3541 0.6099 -0.0214 0.0301  0.0035  364 ARG A CB    
2965 C  CG    . ARG A 364 ? 0.422  0.3791 0.6281 -0.02   0.0311  0.0052  364 ARG A CG    
2966 C  CD    . ARG A 364 ? 0.4498 0.4096 0.6572 -0.0198 0.0314  0.0076  364 ARG A CD    
2967 N  NE    . ARG A 364 ? 0.4702 0.4326 0.6822 -0.0214 0.0307  0.0061  364 ARG A NE    
2968 C  CZ    . ARG A 364 ? 0.4883 0.4513 0.7062 -0.0227 0.0296  0.0066  364 ARG A CZ    
2969 N  NH1   . ARG A 364 ? 0.4825 0.4441 0.7024 -0.0226 0.0294  0.0089  364 ARG A NH1   
2970 N  NH2   . ARG A 364 ? 0.4824 0.4468 0.7038 -0.024  0.0283  0.005   364 ARG A NH2   
2971 N  N     . PRO A 365 ? 0.3716 0.3209 0.586  -0.0213 0.0285  0.0037  365 PRO A N     
2972 C  CA    . PRO A 365 ? 0.371  0.3172 0.5835 -0.0209 0.0279  0.0043  365 PRO A CA    
2973 C  C     . PRO A 365 ? 0.3722 0.3149 0.5838 -0.0204 0.0268  0.007   365 PRO A C     
2974 O  O     . PRO A 365 ? 0.3778 0.3173 0.5853 -0.0196 0.0261  0.0083  365 PRO A O     
2975 C  CB    . PRO A 365 ? 0.3778 0.3243 0.5956 -0.0217 0.0276  0.0017  365 PRO A CB    
2976 C  CG    . PRO A 365 ? 0.3832 0.3329 0.6029 -0.0222 0.0284  -0.0008 365 PRO A CG    
2977 C  CD    . PRO A 365 ? 0.3628 0.3135 0.5823 -0.0223 0.0283  0.0007  365 PRO A CD    
2978 N  N     . ASP A 366 ? 0.3655 0.3085 0.5808 -0.0209 0.0264  0.008   366 ASP A N     
2979 C  CA    . ASP A 366 ? 0.3646 0.3043 0.579  -0.0206 0.0254  0.0108  366 ASP A CA    
2980 C  C     . ASP A 366 ? 0.3624 0.3007 0.5694 -0.0188 0.0262  0.0136  366 ASP A C     
2981 O  O     . ASP A 366 ? 0.3612 0.2955 0.565  -0.0179 0.0254  0.0158  366 ASP A O     
2982 C  CB    . ASP A 366 ? 0.3704 0.3109 0.5906 -0.0217 0.0248  0.0115  366 ASP A CB    
2983 C  CG    . ASP A 366 ? 0.3914 0.3315 0.6183 -0.023  0.0235  0.0089  366 ASP A CG    
2984 O  OD1   . ASP A 366 ? 0.3912 0.3312 0.6186 -0.0229 0.0235  0.0066  366 ASP A OD1   
2985 O  OD2   . ASP A 366 ? 0.4075 0.3475 0.6391 -0.024  0.0225  0.0094  366 ASP A OD2   
2986 N  N     . ARG A 367 ? 0.3609 0.3021 0.5649 -0.018  0.0278  0.0136  367 ARG A N     
2987 C  CA    . ARG A 367 ? 0.3701 0.3102 0.567  -0.0159 0.0288  0.0161  367 ARG A CA    
2988 C  C     . ARG A 367 ? 0.3846 0.3198 0.575  -0.0146 0.0276  0.0162  367 ARG A C     
2989 O  O     . ARG A 367 ? 0.4    0.332  0.5839 -0.0126 0.0277  0.0184  367 ARG A O     
2990 C  CB    . ARG A 367 ? 0.3774 0.3219 0.5732 -0.0153 0.0304  0.0157  367 ARG A CB    
2991 C  CG    . ARG A 367 ? 0.4002 0.3494 0.6024 -0.0167 0.031   0.0159  367 ARG A CG    
2992 C  CD    . ARG A 367 ? 0.4312 0.3843 0.632  -0.0161 0.0323  0.0157  367 ARG A CD    
2993 N  NE    . ARG A 367 ? 0.4531 0.4105 0.6598 -0.0173 0.0326  0.0168  367 ARG A NE    
2994 C  CZ    . ARG A 367 ? 0.4728 0.434  0.6793 -0.0166 0.0337  0.0183  367 ARG A CZ    
2995 N  NH1   . ARG A 367 ? 0.4685 0.4297 0.6688 -0.0145 0.0349  0.0188  367 ARG A NH1   
2996 N  NH2   . ARG A 367 ? 0.4679 0.4329 0.6806 -0.018  0.0335  0.0195  367 ARG A NH2   
2997 N  N     . GLY A 368 ? 0.3734 0.3077 0.5654 -0.0157 0.0264  0.014   368 GLY A N     
2998 C  CA    . GLY A 368 ? 0.3711 0.3006 0.5578 -0.0149 0.0248  0.0143  368 GLY A CA    
2999 C  C     . GLY A 368 ? 0.3624 0.2876 0.551  -0.0156 0.0225  0.0149  368 GLY A C     
3000 O  O     . GLY A 368 ? 0.3626 0.2831 0.547  -0.0151 0.0205  0.0156  368 GLY A O     
3001 N  N     . ALA A 369 ? 0.3548 0.2809 0.5496 -0.0168 0.0223  0.0149  369 ALA A N     
3002 C  CA    . ALA A 369 ? 0.3556 0.2777 0.5529 -0.0175 0.02    0.0154  369 ALA A CA    
3003 C  C     . ALA A 369 ? 0.3563 0.2722 0.5464 -0.0159 0.0185  0.0182  369 ALA A C     
3004 O  O     . ALA A 369 ? 0.3579 0.269  0.5453 -0.0158 0.016   0.0186  369 ALA A O     
3005 C  CB    . ALA A 369 ? 0.3544 0.2788 0.5597 -0.019  0.0201  0.0147  369 ALA A CB    
3006 N  N     . LEU A 370 ? 0.3527 0.2686 0.5392 -0.0146 0.0199  0.0202  370 LEU A N     
3007 C  CA    . LEU A 370 ? 0.3516 0.2614 0.5299 -0.0126 0.0188  0.0228  370 LEU A CA    
3008 C  C     . LEU A 370 ? 0.3456 0.2516 0.5151 -0.0107 0.018   0.0228  370 LEU A C     
3009 O  O     . LEU A 370 ? 0.348  0.2475 0.513  -0.0102 0.0152  0.0236  370 LEU A O     
3010 C  CB    . LEU A 370 ? 0.3508 0.262  0.5274 -0.0114 0.0209  0.0252  370 LEU A CB    
3011 C  CG    . LEU A 370 ? 0.3617 0.2743 0.5457 -0.0133 0.0207  0.026   370 LEU A CG    
3012 C  CD1   . LEU A 370 ? 0.3694 0.2823 0.5504 -0.0119 0.0224  0.0292  370 LEU A CD1   
3013 C  CD2   . LEU A 370 ? 0.3682 0.2753 0.5538 -0.0144 0.0173  0.0259  370 LEU A CD2   
3014 N  N     . PRO A 371 ? 0.3358 0.2455 0.5034 -0.0099 0.02    0.0219  371 PRO A N     
3015 C  CA    . PRO A 371 ? 0.3334 0.2391 0.4931 -0.0083 0.0187  0.0218  371 PRO A CA    
3016 C  C     . PRO A 371 ? 0.3303 0.2323 0.4913 -0.0099 0.0153  0.0209  371 PRO A C     
3017 O  O     . PRO A 371 ? 0.3422 0.2376 0.4959 -0.0086 0.0127  0.0218  371 PRO A O     
3018 C  CB    . PRO A 371 ? 0.3378 0.2496 0.4987 -0.0082 0.0212  0.0204  371 PRO A CB    
3019 C  CG    . PRO A 371 ? 0.3395 0.2568 0.505  -0.0084 0.024   0.021   371 PRO A CG    
3020 C  CD    . PRO A 371 ? 0.3213 0.2384 0.4936 -0.0104 0.023   0.021   371 PRO A CD    
3021 N  N     . LEU A 372 ? 0.3092 0.2152 0.4796 -0.0125 0.0152  0.0193  372 LEU A N     
3022 C  CA    . LEU A 372 ? 0.3018 0.2053 0.4748 -0.0141 0.0123  0.0188  372 LEU A CA    
3023 C  C     . LEU A 372 ? 0.3083 0.2046 0.4792 -0.0139 0.0089  0.0206  372 LEU A C     
3024 O  O     . LEU A 372 ? 0.3156 0.2066 0.4828 -0.0139 0.0056  0.0214  372 LEU A O     
3025 C  CB    . LEU A 372 ? 0.2908 0.2006 0.4743 -0.0164 0.0136  0.0168  372 LEU A CB    
3026 C  CG    . LEU A 372 ? 0.2975 0.2062 0.4864 -0.0181 0.0112  0.0166  372 LEU A CG    
3027 C  CD1   . LEU A 372 ? 0.3055 0.2129 0.4908 -0.0183 0.0098  0.0168  372 LEU A CD1   
3028 C  CD2   . LEU A 372 ? 0.2953 0.2101 0.494  -0.0197 0.013   0.0146  372 LEU A CD2   
3029 N  N     . VAL A 373 ? 0.304  0.2    0.4768 -0.0138 0.0094  0.0214  373 VAL A N     
3030 C  CA    . VAL A 373 ? 0.3085 0.1976 0.4789 -0.0136 0.0063  0.0232  373 VAL A CA    
3031 C  C     . VAL A 373 ? 0.3197 0.2012 0.4777 -0.011  0.0046  0.0249  373 VAL A C     
3032 O  O     . VAL A 373 ? 0.3224 0.1966 0.4765 -0.0109 0.0007  0.026   373 VAL A O     
3033 C  CB    . VAL A 373 ? 0.3136 0.2044 0.4882 -0.014  0.0076  0.0239  373 VAL A CB    
3034 C  CG1   . VAL A 373 ? 0.3248 0.2079 0.4953 -0.0136 0.0044  0.026   373 VAL A CG1   
3035 C  CG2   . VAL A 373 ? 0.3133 0.2101 0.4995 -0.0165 0.0085  0.022   373 VAL A CG2   
3036 N  N     . ALA A 374 ? 0.3249 0.208  0.4769 -0.0087 0.0076  0.0253  374 ALA A N     
3037 C  CA    . ALA A 374 ? 0.3424 0.2187 0.482  -0.0055 0.0067  0.0267  374 ALA A CA    
3038 C  C     . ALA A 374 ? 0.3587 0.2308 0.4936 -0.0052 0.0037  0.026   374 ALA A C     
3039 O  O     . ALA A 374 ? 0.3708 0.2342 0.4964 -0.0034 0.0005  0.0271  374 ALA A O     
3040 C  CB    . ALA A 374 ? 0.3441 0.2246 0.4801 -0.0031 0.011   0.0271  374 ALA A CB    
3041 N  N     . MET A 375 ? 0.3571 0.2348 0.4979 -0.0071 0.0045  0.0243  375 MET A N     
3042 C  CA    . MET A 375 ? 0.3691 0.2435 0.5066 -0.0073 0.0016  0.024   375 MET A CA    
3043 C  C     . MET A 375 ? 0.3776 0.2465 0.5176 -0.0092 -0.0032 0.0248  375 MET A C     
3044 O  O     . MET A 375 ? 0.3864 0.2479 0.5195 -0.0086 -0.0072 0.0257  375 MET A O     
3045 C  CB    . MET A 375 ? 0.376  0.2583 0.5197 -0.0089 0.0041  0.0222  375 MET A CB    
3046 C  CG    . MET A 375 ? 0.408  0.2941 0.5477 -0.0069 0.0076  0.0216  375 MET A CG    
3047 S  SD    . MET A 375 ? 0.4508 0.346  0.5979 -0.009  0.0103  0.0195  375 MET A SD    
3048 C  CE    . MET A 375 ? 0.3987 0.2889 0.5406 -0.0092 0.0065  0.0198  375 MET A CE    
3049 N  N     . LEU A 376 ? 0.3736 0.2459 0.5233 -0.0116 -0.0031 0.0246  376 LEU A N     
3050 C  CA    . LEU A 376 ? 0.3788 0.2471 0.5328 -0.0136 -0.0074 0.0255  376 LEU A CA    
3051 C  C     . LEU A 376 ? 0.3882 0.2467 0.535  -0.0123 -0.0113 0.0274  376 LEU A C     
3052 O  O     . LEU A 376 ? 0.3949 0.2462 0.5382 -0.0127 -0.0162 0.0286  376 LEU A O     
3053 C  CB    . LEU A 376 ? 0.3738 0.2493 0.5409 -0.0162 -0.0058 0.0246  376 LEU A CB    
3054 C  CG    . LEU A 376 ? 0.3857 0.2694 0.5606 -0.0178 -0.0032 0.0229  376 LEU A CG    
3055 C  CD1   . LEU A 376 ? 0.385  0.2753 0.571  -0.0194 -0.001  0.0216  376 LEU A CD1   
3056 C  CD2   . LEU A 376 ? 0.3965 0.2783 0.5728 -0.0192 -0.0066 0.0238  376 LEU A CD2   
3057 N  N     . ALA A 377 ? 0.386  0.2442 0.5307 -0.011  -0.0093 0.0278  377 ALA A N     
3058 C  CA    . ALA A 377 ? 0.3933 0.2426 0.5315 -0.0099 -0.0126 0.0297  377 ALA A CA    
3059 C  C     . ALA A 377 ? 0.3987 0.2422 0.5234 -0.0061 -0.0118 0.0306  377 ALA A C     
3060 O  O     . ALA A 377 ? 0.4055 0.2416 0.524  -0.0049 -0.014  0.0322  377 ALA A O     
3061 C  CB    . ALA A 377 ? 0.3917 0.2439 0.5381 -0.0115 -0.0118 0.0299  377 ALA A CB    
3062 N  N     . GLY A 378 ? 0.3945 0.2409 0.5144 -0.004  -0.0086 0.0299  378 GLY A N     
3063 C  CA    . GLY A 378 ? 0.407  0.2487 0.5144 0.0001  -0.0071 0.0308  378 GLY A CA    
3064 C  C     . GLY A 378 ? 0.409  0.257  0.5185 0.001   -0.0019 0.0315  378 GLY A C     
3065 O  O     . GLY A 378 ? 0.406  0.257  0.5233 -0.001  -0.0013 0.0319  378 GLY A O     
3066 N  N     . GLU A 379 ? 0.4112 0.2615 0.5147 0.0041  0.0018  0.0316  379 GLU A N     
3067 C  CA    . GLU A 379 ? 0.4142 0.2708 0.5199 0.0051  0.0068  0.0327  379 GLU A CA    
3068 C  C     . GLU A 379 ? 0.429  0.28   0.5289 0.0067  0.0064  0.0351  379 GLU A C     
3069 O  O     . GLU A 379 ? 0.4294 0.2857 0.5345 0.0061  0.0094  0.0364  379 GLU A O     
3070 C  CB    . GLU A 379 ? 0.4317 0.2921 0.5322 0.0083  0.0107  0.0327  379 GLU A CB    
3071 C  CG    . GLU A 379 ? 0.484  0.3355 0.5695 0.013   0.0097  0.0337  379 GLU A CG    
3072 C  CD    . GLU A 379 ? 0.5526 0.4077 0.6333 0.0163  0.0134  0.0335  379 GLU A CD    
3073 O  OE1   . GLU A 379 ? 0.5644 0.4257 0.6513 0.0146  0.0143  0.0318  379 GLU A OE1   
3074 O  OE2   . GLU A 379 ? 0.5766 0.4284 0.6475 0.0207  0.0154  0.0351  379 GLU A OE2   
3075 N  N     . ASN A 380 ? 0.4416 0.2817 0.5309 0.0086  0.0023  0.0358  380 ASN A N     
3076 C  CA    . ASN A 380 ? 0.4606 0.294  0.543  0.0103  0.0015  0.0381  380 ASN A CA    
3077 C  C     . ASN A 380 ? 0.4599 0.2933 0.5514 0.0065  -0.001  0.0386  380 ASN A C     
3078 O  O     . ASN A 380 ? 0.4658 0.2957 0.5537 0.0073  -0.001  0.0406  380 ASN A O     
3079 C  CB    . ASN A 380 ? 0.4989 0.3197 0.5659 0.0138  -0.0025 0.0385  380 ASN A CB    
3080 C  CG    . ASN A 380 ? 0.5738 0.3893 0.6409 0.0121  -0.008  0.0368  380 ASN A CG    
3081 O  OD1   . ASN A 380 ? 0.5991 0.4142 0.6622 0.0135  -0.0082 0.0355  380 ASN A OD1   
3082 N  ND2   . ASN A 380 ? 0.5886 0.4005 0.6611 0.0088  -0.0127 0.0369  380 ASN A ND2   
3083 N  N     . ALA A 381 ? 0.4494 0.2869 0.5525 0.0025  -0.003  0.0368  381 ALA A N     
3084 C  CA    . ALA A 381 ? 0.4493 0.2874 0.5619 -0.0009 -0.0053 0.037   381 ALA A CA    
3085 C  C     . ALA A 381 ? 0.4505 0.2959 0.57   -0.0018 -0.0012 0.038   381 ALA A C     
3086 O  O     . ALA A 381 ? 0.4515 0.3047 0.5737 -0.0012 0.0034  0.0377  381 ALA A O     
3087 C  CB    . ALA A 381 ? 0.4434 0.2857 0.5671 -0.0044 -0.0072 0.0349  381 ALA A CB    
3088 N  N     . GLN A 382 ? 0.4479 0.2905 0.5703 -0.0032 -0.0031 0.0394  382 GLN A N     
3089 C  CA    . GLN A 382 ? 0.4492 0.298  0.5782 -0.0043 0.0002  0.0407  382 GLN A CA    
3090 C  C     . GLN A 382 ? 0.4425 0.3003 0.5861 -0.0078 0.0012  0.0386  382 GLN A C     
3091 O  O     . GLN A 382 ? 0.4467 0.3035 0.5972 -0.0101 -0.002  0.0371  382 GLN A O     
3092 C  CB    . GLN A 382 ? 0.475  0.3173 0.6011 -0.0045 -0.0023 0.0431  382 GLN A CB    
3093 C  CG    . GLN A 382 ? 0.5276 0.3618 0.6382 -0.0006 -0.0022 0.0454  382 GLN A CG    
3094 C  CD    . GLN A 382 ? 0.5888 0.417  0.6962 -0.0007 -0.0041 0.048   382 GLN A CD    
3095 O  OE1   . GLN A 382 ? 0.5939 0.4269 0.7096 -0.0028 -0.0029 0.0492  382 GLN A OE1   
3096 N  NE2   . GLN A 382 ? 0.6124 0.4296 0.7071 0.0017  -0.0075 0.0491  382 GLN A NE2   
3097 N  N     . ILE A 383 ? 0.4299 0.2962 0.578  -0.0078 0.0057  0.0383  383 ILE A N     
3098 C  CA    . ILE A 383 ? 0.4174 0.2919 0.5781 -0.0106 0.0068  0.036   383 ILE A CA    
3099 C  C     . ILE A 383 ? 0.404  0.2833 0.5718 -0.0121 0.0088  0.0374  383 ILE A C     
3100 O  O     . ILE A 383 ? 0.405  0.2867 0.5697 -0.0107 0.0118  0.0396  383 ILE A O     
3101 C  CB    . ILE A 383 ? 0.4222 0.3022 0.5829 -0.0099 0.0095  0.0341  383 ILE A CB    
3102 C  CG1   . ILE A 383 ? 0.4344 0.3091 0.5886 -0.0088 0.007   0.0329  383 ILE A CG1   
3103 C  CG2   . ILE A 383 ? 0.4231 0.3113 0.5956 -0.0125 0.011   0.0317  383 ILE A CG2   
3104 C  CD1   . ILE A 383 ? 0.4482 0.3268 0.5998 -0.0075 0.0094  0.0316  383 ILE A CD1   
3105 N  N     . PHE A 384 ? 0.3882 0.2692 0.566  -0.0149 0.0069  0.0361  384 PHE A N     
3106 C  CA    . PHE A 384 ? 0.3811 0.2662 0.5669 -0.0167 0.0078  0.0369  384 PHE A CA    
3107 C  C     . PHE A 384 ? 0.3692 0.2619 0.5641 -0.0183 0.0094  0.0339  384 PHE A C     
3108 O  O     . PHE A 384 ? 0.3728 0.2657 0.5733 -0.0196 0.0076  0.0312  384 PHE A O     
3109 C  CB    . PHE A 384 ? 0.3795 0.2598 0.5695 -0.0185 0.0038  0.0372  384 PHE A CB    
3110 C  CG    . PHE A 384 ? 0.3834 0.266  0.5809 -0.0205 0.0037  0.0383  384 PHE A CG    
3111 C  CD1   . PHE A 384 ? 0.3874 0.2756 0.5957 -0.0225 0.004   0.0359  384 PHE A CD1   
3112 C  CD2   . PHE A 384 ? 0.3968 0.2752 0.5905 -0.0203 0.0029  0.0418  384 PHE A CD2   
3113 C  CE1   . PHE A 384 ? 0.3934 0.283  0.6086 -0.0244 0.0033  0.0369  384 PHE A CE1   
3114 C  CE2   . PHE A 384 ? 0.4027 0.2828 0.6036 -0.0223 0.0023  0.043   384 PHE A CE2   
3115 C  CZ    . PHE A 384 ? 0.3944 0.2799 0.6062 -0.0244 0.0023  0.0405  384 PHE A CZ    
3116 N  N     . THR A 385 ? 0.3509 0.2497 0.5473 -0.0181 0.0127  0.0344  385 THR A N     
3117 C  CA    . THR A 385 ? 0.3373 0.2428 0.5412 -0.0195 0.0142  0.0316  385 THR A CA    
3118 C  C     . THR A 385 ? 0.32   0.2289 0.5331 -0.0217 0.0138  0.0317  385 THR A C     
3119 O  O     . THR A 385 ? 0.3239 0.2345 0.537  -0.0218 0.0151  0.0347  385 THR A O     
3120 C  CB    . THR A 385 ? 0.3548 0.2646 0.5544 -0.0178 0.0175  0.032   385 THR A CB    
3121 O  OG1   . THR A 385 ? 0.3732 0.2791 0.5641 -0.0157 0.0173  0.0317  385 THR A OG1   
3122 C  CG2   . THR A 385 ? 0.3555 0.2718 0.5618 -0.0191 0.0188  0.0292  385 THR A CG2   
3123 N  N     . PHE A 386 ? 0.3025 0.2124 0.5233 -0.0234 0.0122  0.0287  386 PHE A N     
3124 C  CA    . PHE A 386 ? 0.2963 0.2085 0.5257 -0.0254 0.0113  0.0284  386 PHE A CA    
3125 C  C     . PHE A 386 ? 0.2942 0.2122 0.5286 -0.0261 0.0128  0.0256  386 PHE A C     
3126 O  O     . PHE A 386 ? 0.2974 0.2164 0.5332 -0.0259 0.0129  0.0222  386 PHE A O     
3127 C  CB    . PHE A 386 ? 0.2905 0.1989 0.5251 -0.0265 0.008   0.027   386 PHE A CB    
3128 C  CG    . PHE A 386 ? 0.2918 0.2014 0.535  -0.0284 0.0065  0.0263  386 PHE A CG    
3129 C  CD1   . PHE A 386 ? 0.3005 0.208  0.5449 -0.0295 0.0052  0.0295  386 PHE A CD1   
3130 C  CD2   . PHE A 386 ? 0.2956 0.2079 0.5457 -0.0291 0.0061  0.0224  386 PHE A CD2   
3131 C  CE1   . PHE A 386 ? 0.3034 0.2113 0.5558 -0.0313 0.0032  0.0288  386 PHE A CE1   
3132 C  CE2   . PHE A 386 ? 0.3004 0.2128 0.5579 -0.0306 0.0043  0.0216  386 PHE A CE2   
3133 C  CZ    . PHE A 386 ? 0.2973 0.2074 0.5561 -0.0318 0.0027  0.0248  386 PHE A CZ    
3134 N  N     . ILE A 387 ? 0.2853 0.207  0.5223 -0.0269 0.0139  0.0271  387 ILE A N     
3135 C  CA    . ILE A 387 ? 0.2836 0.2104 0.525  -0.0277 0.0149  0.025   387 ILE A CA    
3136 C  C     . ILE A 387 ? 0.2865 0.2136 0.5362 -0.0298 0.0127  0.0242  387 ILE A C     
3137 O  O     . ILE A 387 ? 0.2903 0.216  0.542  -0.0308 0.0115  0.0272  387 ILE A O     
3138 C  CB    . ILE A 387 ? 0.2867 0.2176 0.5247 -0.027  0.0176  0.0277  387 ILE A CB    
3139 C  CG1   . ILE A 387 ? 0.3023 0.2321 0.5313 -0.0245 0.0197  0.0285  387 ILE A CG1   
3140 C  CG2   . ILE A 387 ? 0.2876 0.2234 0.5298 -0.0279 0.0183  0.0256  387 ILE A CG2   
3141 C  CD1   . ILE A 387 ? 0.3214 0.2507 0.5484 -0.0238 0.0197  0.0248  387 ILE A CD1   
3142 N  N     . TYR A 388 ? 0.2814 0.21   0.5357 -0.0303 0.012   0.0201  388 TYR A N     
3143 C  CA    . TYR A 388 ? 0.2805 0.2085 0.5422 -0.032  0.0095  0.0189  388 TYR A CA    
3144 C  C     . TYR A 388 ? 0.279  0.2104 0.544  -0.0327 0.0095  0.0165  388 TYR A C     
3145 O  O     . TYR A 388 ? 0.2776 0.2079 0.5483 -0.0339 0.0071  0.0149  388 TYR A O     
3146 C  CB    . TYR A 388 ? 0.279  0.2033 0.5438 -0.0318 0.0075  0.016   388 TYR A CB    
3147 C  CG    . TYR A 388 ? 0.2833 0.2083 0.5463 -0.0303 0.0088  0.0124  388 TYR A CG    
3148 C  CD1   . TYR A 388 ? 0.2944 0.2179 0.5525 -0.0291 0.0097  0.0132  388 TYR A CD1   
3149 C  CD2   . TYR A 388 ? 0.2909 0.2178 0.557  -0.0301 0.009   0.0084  388 TYR A CD2   
3150 C  CE1   . TYR A 388 ? 0.3048 0.2293 0.5619 -0.028  0.0108  0.0104  388 TYR A CE1   
3151 C  CE2   . TYR A 388 ? 0.3017 0.2297 0.5663 -0.0287 0.0105  0.0054  388 TYR A CE2   
3152 C  CZ    . TYR A 388 ? 0.3137 0.2407 0.5742 -0.0278 0.0114  0.0066  388 TYR A CZ    
3153 O  OH    . TYR A 388 ? 0.3321 0.2605 0.5916 -0.0267 0.0128  0.0042  388 TYR A OH    
3154 N  N     . GLY A 389 ? 0.2769 0.2118 0.5381 -0.0319 0.0119  0.0162  389 GLY A N     
3155 C  CA    . GLY A 389 ? 0.2789 0.2168 0.5424 -0.0325 0.0119  0.014   389 GLY A CA    
3156 C  C     . GLY A 389 ? 0.2754 0.2155 0.542  -0.0342 0.011   0.0174  389 GLY A C     
3157 O  O     . GLY A 389 ? 0.2747 0.2151 0.541  -0.0347 0.0114  0.0218  389 GLY A O     
3158 N  N     . PRO A 390 ? 0.2716 0.2135 0.5412 -0.0352 0.0099  0.0156  390 PRO A N     
3159 C  CA    . PRO A 390 ? 0.2699 0.214  0.5438 -0.0372 0.0084  0.019   390 PRO A CA    
3160 C  C     . PRO A 390 ? 0.2767 0.2255 0.5479 -0.0368 0.0112  0.023   390 PRO A C     
3161 O  O     . PRO A 390 ? 0.285  0.2359 0.5517 -0.0353 0.0135  0.0216  390 PRO A O     
3162 C  CB    . PRO A 390 ? 0.2763 0.2198 0.5535 -0.0381 0.0059  0.0154  390 PRO A CB    
3163 C  CG    . PRO A 390 ? 0.2851 0.2261 0.5597 -0.0364 0.0063  0.01    390 PRO A CG    
3164 C  CD    . PRO A 390 ? 0.2657 0.2071 0.5352 -0.0346 0.0094  0.0104  390 PRO A CD    
3165 N  N     . LEU A 391 ? 0.2724 0.223  0.5466 -0.0381 0.0109  0.0282  391 LEU A N     
3166 C  CA    . LEU A 391 ? 0.2746 0.2302 0.5471 -0.0375 0.0137  0.0325  391 LEU A CA    
3167 C  C     . LEU A 391 ? 0.2798 0.2391 0.5591 -0.0398 0.0118  0.035   391 LEU A C     
3168 O  O     . LEU A 391 ? 0.2804 0.238  0.5657 -0.0422 0.0084  0.0359  391 LEU A O     
3169 C  CB    . LEU A 391 ? 0.2689 0.2244 0.5393 -0.0368 0.0155  0.0374  391 LEU A CB    
3170 C  CG    . LEU A 391 ? 0.2766 0.2278 0.5408 -0.0349 0.0166  0.036   391 LEU A CG    
3171 C  CD1   . LEU A 391 ? 0.2818 0.2324 0.5438 -0.0343 0.0179  0.0411  391 LEU A CD1   
3172 C  CD2   . LEU A 391 ? 0.2835 0.2354 0.5409 -0.0324 0.0192  0.0336  391 LEU A CD2   
3173 N  N     . ILE A 392 ? 0.2791 0.2432 0.5574 -0.0393 0.0137  0.0364  392 ILE A N     
3174 C  CA    . ILE A 392 ? 0.2847 0.2528 0.5697 -0.0415 0.012   0.0396  392 ILE A CA    
3175 C  C     . ILE A 392 ? 0.2824 0.2536 0.5705 -0.0421 0.0133  0.0465  392 ILE A C     
3176 O  O     . ILE A 392 ? 0.2862 0.2573 0.5691 -0.04   0.0165  0.0484  392 ILE A O     
3177 C  CB    . ILE A 392 ? 0.2972 0.2697 0.5805 -0.0405 0.0136  0.0391  392 ILE A CB    
3178 C  CG1   . ILE A 392 ? 0.3161 0.2915 0.5928 -0.0375 0.0185  0.0413  392 ILE A CG1   
3179 C  CG2   . ILE A 392 ? 0.306  0.2753 0.5867 -0.0403 0.0119  0.0326  392 ILE A CG2   
3180 C  CD1   . ILE A 392 ? 0.3379 0.3178 0.6131 -0.0363 0.0202  0.0414  392 ILE A CD1   
3181 N  N     . LYS A 393 ? 0.2726 0.2461 0.5688 -0.045  0.0106  0.0502  393 LYS A N     
3182 C  CA    . LYS A 393 ? 0.271  0.2478 0.5709 -0.0459 0.0118  0.0572  393 LYS A CA    
3183 C  C     . LYS A 393 ? 0.272  0.2544 0.5676 -0.0431 0.0172  0.0614  393 LYS A C     
3184 O  O     . LYS A 393 ? 0.2767 0.2594 0.5697 -0.0419 0.0198  0.0652  393 LYS A O     
3185 C  CB    . LYS A 393 ? 0.2877 0.2669 0.5977 -0.0496 0.0078  0.0608  393 LYS A CB    
3186 C  CG    . LYS A 393 ? 0.3371 0.32   0.6517 -0.0509 0.0089  0.0684  393 LYS A CG    
3187 C  CD    . LYS A 393 ? 0.3899 0.3677 0.7025 -0.051  0.0084  0.0688  393 LYS A CD    
3188 C  CE    . LYS A 393 ? 0.4364 0.4169 0.7562 -0.0537 0.0073  0.076   393 LYS A CE    
3189 N  NZ    . LYS A 393 ? 0.459  0.4482 0.7818 -0.0533 0.0109  0.0827  393 LYS A NZ    
3190 N  N     . GLY A 394 ? 0.2657 0.2517 0.5597 -0.0418 0.0188  0.0602  394 GLY A N     
3191 C  CA    . GLY A 394 ? 0.2638 0.2548 0.5534 -0.0387 0.0238  0.0635  394 GLY A CA    
3192 C  C     . GLY A 394 ? 0.2642 0.2514 0.5436 -0.0352 0.0271  0.0617  394 GLY A C     
3193 O  O     . GLY A 394 ? 0.2632 0.2529 0.5388 -0.0327 0.031   0.0658  394 GLY A O     
3194 N  N     . ALA A 395 ? 0.2631 0.244  0.5379 -0.0349 0.0254  0.0557  395 ALA A N     
3195 C  CA    . ALA A 395 ? 0.2662 0.2428 0.5316 -0.0319 0.0278  0.0539  395 ALA A CA    
3196 C  C     . ALA A 395 ? 0.2676 0.2413 0.5319 -0.0319 0.028   0.0571  395 ALA A C     
3197 O  O     . ALA A 395 ? 0.2687 0.242  0.5262 -0.0291 0.0312  0.0594  395 ALA A O     
3198 C  CB    . ALA A 395 ? 0.2671 0.2385 0.5292 -0.0317 0.0259  0.0471  395 ALA A CB    
3199 N  N     . ILE A 396 ? 0.2681 0.2398 0.5389 -0.0349 0.0246  0.0576  396 ILE A N     
3200 C  CA    . ILE A 396 ? 0.2804 0.2491 0.5505 -0.0352 0.0244  0.0608  396 ILE A CA    
3201 C  C     . ILE A 396 ? 0.2876 0.2617 0.5589 -0.0347 0.0275  0.0681  396 ILE A C     
3202 O  O     . ILE A 396 ? 0.2895 0.2617 0.5552 -0.0329 0.0297  0.0709  396 ILE A O     
3203 C  CB    . ILE A 396 ? 0.2872 0.2519 0.5638 -0.0385 0.0197  0.0592  396 ILE A CB    
3204 C  CG1   . ILE A 396 ? 0.3037 0.2637 0.5779 -0.0385 0.0192  0.0613  396 ILE A CG1   
3205 C  CG2   . ILE A 396 ? 0.2887 0.2573 0.5752 -0.0419 0.017   0.0618  396 ILE A CG2   
3206 C  CD1   . ILE A 396 ? 0.3276 0.2826 0.5923 -0.0356 0.0208  0.0585  396 ILE A CD1   
3207 N  N     . ASN A 397 ? 0.2905 0.2714 0.5682 -0.0359 0.028   0.0712  397 ASN A N     
3208 C  CA    . ASN A 397 ? 0.296  0.2833 0.576  -0.0352 0.0313  0.0784  397 ASN A CA    
3209 C  C     . ASN A 397 ? 0.3072 0.2955 0.5773 -0.0305 0.0365  0.0794  397 ASN A C     
3210 O  O     . ASN A 397 ? 0.3094 0.2988 0.5762 -0.0287 0.0396  0.0843  397 ASN A O     
3211 C  CB    . ASN A 397 ? 0.3055 0.2998 0.5949 -0.0374 0.0303  0.0808  397 ASN A CB    
3212 C  CG    . ASN A 397 ? 0.346  0.341  0.6459 -0.0419 0.026   0.0835  397 ASN A CG    
3213 O  OD1   . ASN A 397 ? 0.359  0.3506 0.6597 -0.0433 0.0246  0.0855  397 ASN A OD1   
3214 N  ND2   . ASN A 397 ? 0.3571 0.356  0.6651 -0.0444 0.0234  0.0839  397 ASN A ND2   
3215 N  N     . LEU A 398 ? 0.3112 0.2987 0.5761 -0.0283 0.0373  0.0747  398 LEU A N     
3216 C  CA    . LEU A 398 ? 0.3196 0.3071 0.5745 -0.0236 0.0417  0.075   398 LEU A CA    
3217 C  C     . LEU A 398 ? 0.3352 0.3151 0.5805 -0.0216 0.0421  0.0735  398 LEU A C     
3218 O  O     . LEU A 398 ? 0.3365 0.3161 0.574  -0.018  0.0457  0.0761  398 LEU A O     
3219 C  CB    . LEU A 398 ? 0.3188 0.3071 0.5711 -0.0222 0.0419  0.0704  398 LEU A CB    
3220 C  CG    . LEU A 398 ? 0.329  0.3253 0.5845 -0.021  0.0447  0.0738  398 LEU A CG    
3221 C  CD1   . LEU A 398 ? 0.333  0.3346 0.6006 -0.025  0.0421  0.076   398 LEU A CD1   
3222 C  CD2   . LEU A 398 ? 0.3378 0.3337 0.5879 -0.0187 0.0454  0.0694  398 LEU A CD2   
3223 N  N     . ILE A 399 ? 0.3451 0.3188 0.5911 -0.0238 0.0383  0.0697  399 ILE A N     
3224 C  CA    . ILE A 399 ? 0.3684 0.3348 0.6065 -0.0223 0.0379  0.0685  399 ILE A CA    
3225 C  C     . ILE A 399 ? 0.3814 0.3482 0.619  -0.0221 0.0395  0.0748  399 ILE A C     
3226 O  O     . ILE A 399 ? 0.394  0.3572 0.6221 -0.0189 0.0417  0.0762  399 ILE A O     
3227 C  CB    . ILE A 399 ? 0.3794 0.3401 0.6205 -0.0251 0.0333  0.0634  399 ILE A CB    
3228 C  CG1   . ILE A 399 ? 0.3907 0.3497 0.629  -0.0242 0.0325  0.0574  399 ILE A CG1   
3229 C  CG2   . ILE A 399 ? 0.3898 0.3435 0.6263 -0.0248 0.0319  0.0637  399 ILE A CG2   
3230 C  CD1   . ILE A 399 ? 0.4024 0.3587 0.6462 -0.027  0.0286  0.0527  399 ILE A CD1   
3231 N  N     . ASP A 400 ? 0.3746 0.3457 0.6219 -0.0253 0.0384  0.0786  400 ASP A N     
3232 C  CA    . ASP A 400 ? 0.3824 0.3546 0.6302 -0.0255 0.0398  0.085   400 ASP A CA    
3233 C  C     . ASP A 400 ? 0.3901 0.3695 0.6365 -0.0227 0.0452  0.091   400 ASP A C     
3234 O  O     . ASP A 400 ? 0.3941 0.3746 0.6392 -0.022  0.0474  0.0967  400 ASP A O     
3235 C  CB    . ASP A 400 ? 0.4016 0.3752 0.6608 -0.0304 0.036   0.0869  400 ASP A CB    
3236 C  CG    . ASP A 400 ? 0.4525 0.4193 0.7138 -0.0329 0.0309  0.0813  400 ASP A CG    
3237 O  OD1   . ASP A 400 ? 0.4665 0.4268 0.72   -0.031  0.0304  0.0774  400 ASP A OD1   
3238 O  OD2   . ASP A 400 ? 0.469  0.4368 0.7399 -0.0367 0.0271  0.081   400 ASP A OD2   
3239 N  N     . GLN A 401 ? 0.3905 0.375  0.6372 -0.021  0.0473  0.09    401 GLN A N     
3240 C  CA    . GLN A 401 ? 0.3966 0.3884 0.6427 -0.018  0.0524  0.0955  401 GLN A CA    
3241 C  C     . GLN A 401 ? 0.4003 0.3893 0.6332 -0.0123 0.0562  0.0937  401 GLN A C     
3242 O  O     . GLN A 401 ? 0.4041 0.3936 0.6304 -0.0088 0.0603  0.0981  401 GLN A O     
3243 C  CB    . GLN A 401 ? 0.4162 0.4164 0.6733 -0.0203 0.0519  0.0965  401 GLN A CB    
3244 C  CG    . GLN A 401 ? 0.4667 0.4749 0.7233 -0.0167 0.0571  0.1008  401 GLN A CG    
3245 C  CD    . GLN A 401 ? 0.5191 0.5326 0.7824 -0.0178 0.056   0.0988  401 GLN A CD    
3246 O  OE1   . GLN A 401 ? 0.542  0.5546 0.8126 -0.022  0.0513  0.0956  401 GLN A OE1   
3247 N  NE2   . GLN A 401 ? 0.5127 0.5315 0.7734 -0.014  0.0602  0.1006  401 GLN A NE2   
3248 N  N     . ASP A 402 ? 0.3957 0.3814 0.6246 -0.0114 0.0548  0.0875  402 ASP A N     
3249 C  CA    . ASP A 402 ? 0.403  0.3856 0.6202 -0.0064 0.0575  0.0853  402 ASP A CA    
3250 C  C     . ASP A 402 ? 0.4035 0.3807 0.6185 -0.0074 0.0539  0.078   402 ASP A C     
3251 O  O     . ASP A 402 ? 0.4048 0.3858 0.6247 -0.0086 0.0531  0.0756  402 ASP A O     
3252 C  CB    . ASP A 402 ? 0.4235 0.4147 0.643  -0.0039 0.0614  0.0883  402 ASP A CB    
3253 C  CG    . ASP A 402 ? 0.486  0.4752 0.6939 0.0017  0.0648  0.087   402 ASP A CG    
3254 O  OD1   . ASP A 402 ? 0.5088 0.4893 0.7059 0.0038  0.0638  0.0835  402 ASP A OD1   
3255 O  OD2   . ASP A 402 ? 0.4982 0.4943 0.708  0.0041  0.0681  0.0895  402 ASP A OD2   
3256 N  N     . ILE A 403 ? 0.3991 0.3676 0.6069 -0.0071 0.0516  0.0747  403 ILE A N     
3257 C  CA    . ILE A 403 ? 0.398  0.3615 0.6043 -0.0082 0.0482  0.0682  403 ILE A CA    
3258 C  C     . ILE A 403 ? 0.3933 0.3574 0.5934 -0.005  0.05    0.0656  403 ILE A C     
3259 O  O     . ILE A 403 ? 0.394  0.3582 0.5968 -0.0065 0.0479  0.0612  403 ILE A O     
3260 C  CB    . ILE A 403 ? 0.4108 0.3653 0.6117 -0.0086 0.0454  0.0659  403 ILE A CB    
3261 C  CG1   . ILE A 403 ? 0.4242 0.3746 0.6257 -0.0103 0.0418  0.0596  403 ILE A CG1   
3262 C  CG2   . ILE A 403 ? 0.423  0.372  0.6113 -0.0043 0.0475  0.0677  403 ILE A CG2   
3263 C  CD1   . ILE A 403 ? 0.4372 0.3915 0.6497 -0.0143 0.0394  0.0574  403 ILE A CD1   
3264 N  N     . ASN A 404 ? 0.3861 0.3507 0.5781 -0.0004 0.0538  0.0684  404 ASN A N     
3265 C  CA    . ASN A 404 ? 0.3851 0.3499 0.5709 0.0029  0.0553  0.0661  404 ASN A CA    
3266 C  C     . ASN A 404 ? 0.3795 0.3527 0.5737 0.0017  0.0562  0.0662  404 ASN A C     
3267 O  O     . ASN A 404 ? 0.3796 0.3525 0.5713 0.0028  0.0558  0.0629  404 ASN A O     
3268 C  CB    . ASN A 404 ? 0.3959 0.3584 0.5704 0.0084  0.059   0.0689  404 ASN A CB    
3269 C  CG    . ASN A 404 ? 0.4313 0.3837 0.5952 0.01    0.0572  0.0673  404 ASN A CG    
3270 O  OD1   . ASN A 404 ? 0.4387 0.3853 0.6016 0.008   0.0534  0.0629  404 ASN A OD1   
3271 N  ND2   . ASN A 404 ? 0.4477 0.3977 0.6035 0.0137  0.06    0.071   404 ASN A ND2   
3272 N  N     . LYS A 405 ? 0.3703 0.3507 0.5747 -0.0007 0.057   0.0703  405 LYS A N     
3273 C  CA    . LYS A 405 ? 0.3661 0.3544 0.5797 -0.0023 0.0571  0.0708  405 LYS A CA    
3274 C  C     . LYS A 405 ? 0.3625 0.3487 0.581  -0.0063 0.0527  0.0654  405 LYS A C     
3275 O  O     . LYS A 405 ? 0.3674 0.3564 0.5877 -0.0064 0.0523  0.0631  405 LYS A O     
3276 C  CB    . LYS A 405 ? 0.3835 0.3795 0.6072 -0.0042 0.0585  0.0769  405 LYS A CB    
3277 C  CG    . LYS A 405 ? 0.4323 0.4369 0.6643 -0.0049 0.0593  0.0787  405 LYS A CG    
3278 C  CD    . LYS A 405 ? 0.4823 0.495  0.7235 -0.006  0.0614  0.0858  405 LYS A CD    
3279 C  CE    . LYS A 405 ? 0.5246 0.5461 0.7733 -0.0059 0.0626  0.0882  405 LYS A CE    
3280 N  NZ    . LYS A 405 ? 0.5522 0.5797 0.8147 -0.0107 0.0602  0.0918  405 LYS A NZ    
3281 N  N     . LEU A 406 ? 0.3495 0.3308 0.5697 -0.0092 0.0495  0.0632  406 LEU A N     
3282 C  CA    . LEU A 406 ? 0.3439 0.3226 0.5679 -0.0125 0.0456  0.058   406 LEU A CA    
3283 C  C     . LEU A 406 ? 0.3483 0.3221 0.5638 -0.0105 0.0452  0.0531  406 LEU A C     
3284 O  O     . LEU A 406 ? 0.3517 0.3267 0.5692 -0.0115 0.0439  0.0497  406 LEU A O     
3285 C  CB    . LEU A 406 ? 0.3411 0.3155 0.5684 -0.0155 0.0426  0.0574  406 LEU A CB    
3286 C  CG    . LEU A 406 ? 0.3538 0.3253 0.5851 -0.0185 0.0388  0.0521  406 LEU A CG    
3287 C  CD1   . LEU A 406 ? 0.3554 0.3323 0.5951 -0.021  0.0375  0.0515  406 LEU A CD1   
3288 C  CD2   . LEU A 406 ? 0.3618 0.3292 0.5963 -0.0209 0.0361  0.0519  406 LEU A CD2   
3289 N  N     . ALA A 407 ? 0.3457 0.3139 0.5515 -0.0074 0.0463  0.0532  407 ALA A N     
3290 C  CA    . ALA A 407 ? 0.3504 0.3135 0.5476 -0.0053 0.0457  0.0493  407 ALA A CA    
3291 C  C     . ALA A 407 ? 0.3515 0.3185 0.5467 -0.0032 0.0476  0.0488  407 ALA A C     
3292 O  O     . ALA A 407 ? 0.3508 0.3157 0.5432 -0.0031 0.0462  0.0449  407 ALA A O     
3293 C  CB    . ALA A 407 ? 0.357  0.3136 0.544  -0.0021 0.0465  0.0505  407 ALA A CB    
3294 N  N     . LYS A 408 ? 0.3499 0.323  0.5472 -0.0014 0.0506  0.0531  408 LYS A N     
3295 C  CA    . LYS A 408 ? 0.3545 0.3319 0.5507 0.0008  0.0525  0.0532  408 LYS A CA    
3296 C  C     . LYS A 408 ? 0.349  0.3305 0.5532 -0.0026 0.0504  0.0507  408 LYS A C     
3297 O  O     . LYS A 408 ? 0.3518 0.3334 0.553  -0.0014 0.0503  0.0482  408 LYS A O     
3298 C  CB    . LYS A 408 ? 0.3835 0.3669 0.5808 0.0036  0.0565  0.0589  408 LYS A CB    
3299 C  CG    . LYS A 408 ? 0.4462 0.4261 0.6316 0.0092  0.0594  0.06    408 LYS A CG    
3300 C  CD    . LYS A 408 ? 0.4998 0.4869 0.6867 0.0125  0.0639  0.0655  408 LYS A CD    
3301 C  CE    . LYS A 408 ? 0.5539 0.5437 0.7452 0.0116  0.0656  0.0705  408 LYS A CE    
3302 N  NZ    . LYS A 408 ? 0.6025 0.584  0.7864 0.0119  0.0644  0.0696  408 LYS A NZ    
3303 N  N     . ARG A 409 ? 0.3407 0.3249 0.5546 -0.0066 0.0484  0.0511  409 ARG A N     
3304 C  CA    . ARG A 409 ? 0.3422 0.3296 0.5631 -0.0097 0.0461  0.0486  409 ARG A CA    
3305 C  C     . ARG A 409 ? 0.3324 0.3147 0.552  -0.0118 0.043   0.043   409 ARG A C     
3306 O  O     . ARG A 409 ? 0.3284 0.3123 0.5505 -0.0132 0.0416  0.0403  409 ARG A O     
3307 C  CB    . ARG A 409 ? 0.3704 0.3627 0.6023 -0.0131 0.0448  0.0515  409 ARG A CB    
3308 C  CG    . ARG A 409 ? 0.4317 0.4289 0.6673 -0.0122 0.0474  0.0579  409 ARG A CG    
3309 C  CD    . ARG A 409 ? 0.4943 0.4963 0.7417 -0.0162 0.0452  0.0602  409 ARG A CD    
3310 N  NE    . ARG A 409 ? 0.5591 0.5567 0.81   -0.0199 0.0413  0.0569  409 ARG A NE    
3311 C  CZ    . ARG A 409 ? 0.6035 0.6029 0.8632 -0.0236 0.0379  0.0567  409 ARG A CZ    
3312 N  NH1   . ARG A 409 ? 0.5915 0.5973 0.858  -0.0246 0.0378  0.0598  409 ARG A NH1   
3313 N  NH2   . ARG A 409 ? 0.6108 0.6055 0.8726 -0.0263 0.0345  0.0535  409 ARG A NH2   
3314 N  N     . ASN A 410 ? 0.327  0.3037 0.5438 -0.0123 0.0418  0.0414  410 ASN A N     
3315 C  CA    . ASN A 410 ? 0.3311 0.3036 0.5479 -0.0143 0.0391  0.0365  410 ASN A CA    
3316 C  C     . ASN A 410 ? 0.3442 0.3106 0.5521 -0.0122 0.0391  0.0343  410 ASN A C     
3317 O  O     . ASN A 410 ? 0.3534 0.3163 0.5574 -0.0109 0.0397  0.0361  410 ASN A O     
3318 C  CB    . ASN A 410 ? 0.3372 0.3088 0.5609 -0.0174 0.0369  0.0364  410 ASN A CB    
3319 C  CG    . ASN A 410 ? 0.365  0.3331 0.5899 -0.0194 0.0343  0.0315  410 ASN A CG    
3320 O  OD1   . ASN A 410 ? 0.3835 0.3468 0.6047 -0.0189 0.0336  0.0297  410 ASN A OD1   
3321 N  ND2   . ASN A 410 ? 0.3653 0.3357 0.5957 -0.0215 0.0326  0.0294  410 ASN A ND2   
3322 N  N     . GLY A 411 ? 0.341  0.3059 0.5461 -0.0123 0.0383  0.0305  411 GLY A N     
3323 C  CA    . GLY A 411 ? 0.3449 0.3042 0.5423 -0.0107 0.0378  0.0284  411 GLY A CA    
3324 C  C     . GLY A 411 ? 0.3414 0.2957 0.539  -0.0119 0.0359  0.0272  411 GLY A C     
3325 O  O     . GLY A 411 ? 0.3432 0.2924 0.5342 -0.0102 0.0356  0.0273  411 GLY A O     
3326 N  N     . LEU A 412 ? 0.334  0.2892 0.5391 -0.0148 0.0344  0.0262  412 LEU A N     
3327 C  CA    . LEU A 412 ? 0.335  0.2858 0.5413 -0.0159 0.0326  0.0252  412 LEU A CA    
3328 C  C     . LEU A 412 ? 0.3366 0.2855 0.5413 -0.0149 0.0331  0.029   412 LEU A C     
3329 O  O     . LEU A 412 ? 0.3414 0.285  0.5415 -0.014  0.0323  0.0291  412 LEU A O     
3330 C  CB    . LEU A 412 ? 0.3322 0.2843 0.5466 -0.0188 0.0308  0.0228  412 LEU A CB    
3331 C  CG    . LEU A 412 ? 0.3527 0.3005 0.5691 -0.0198 0.0289  0.0218  412 LEU A CG    
3332 C  CD1   . LEU A 412 ? 0.3626 0.3065 0.5743 -0.019  0.0283  0.0197  412 LEU A CD1   
3333 C  CD2   . LEU A 412 ? 0.359  0.3079 0.583  -0.0222 0.0272  0.0197  412 LEU A CD2   
3334 N  N     . TRP A 413 ? 0.3306 0.2836 0.5387 -0.015  0.0345  0.0323  413 TRP A N     
3335 C  CA    . TRP A 413 ? 0.3322 0.2839 0.5384 -0.0139 0.0355  0.0364  413 TRP A CA    
3336 C  C     . TRP A 413 ? 0.3366 0.2852 0.5326 -0.0102 0.0372  0.0378  413 TRP A C     
3337 O  O     . TRP A 413 ? 0.345  0.2887 0.5364 -0.0091 0.0369  0.0393  413 TRP A O     
3338 C  CB    . TRP A 413 ? 0.3259 0.2834 0.5387 -0.015  0.0367  0.0402  413 TRP A CB    
3339 C  CG    . TRP A 413 ? 0.3295 0.2876 0.5512 -0.0185 0.0341  0.0395  413 TRP A CG    
3340 C  CD1   . TRP A 413 ? 0.3386 0.3003 0.5677 -0.021  0.0328  0.0379  413 TRP A CD1   
3341 C  CD2   . TRP A 413 ? 0.3318 0.2859 0.5554 -0.0199 0.0322  0.04    413 TRP A CD2   
3342 N  NE1   . TRP A 413 ? 0.3401 0.3002 0.5755 -0.0237 0.0302  0.0374  413 TRP A NE1   
3343 C  CE2   . TRP A 413 ? 0.3371 0.2927 0.5695 -0.0231 0.0298  0.0387  413 TRP A CE2   
3344 C  CE3   . TRP A 413 ? 0.3412 0.29   0.5596 -0.0187 0.032   0.0414  413 TRP A CE3   
3345 C  CZ2   . TRP A 413 ? 0.3395 0.2919 0.576  -0.025  0.0274  0.0388  413 TRP A CZ2   
3346 C  CZ3   . TRP A 413 ? 0.3468 0.2926 0.5693 -0.0208 0.0296  0.0415  413 TRP A CZ3   
3347 C  CH2   . TRP A 413 ? 0.3423 0.29   0.574  -0.0239 0.0274  0.0402  413 TRP A CH2   
3348 N  N     . LYS A 414 ? 0.3262 0.2766 0.5181 -0.0083 0.0387  0.037   414 LYS A N     
3349 C  CA    . LYS A 414 ? 0.3263 0.2731 0.5078 -0.0044 0.04    0.0378  414 LYS A CA    
3350 C  C     . LYS A 414 ? 0.3204 0.2593 0.4961 -0.0042 0.0375  0.0356  414 LYS A C     
3351 O  O     . LYS A 414 ? 0.3264 0.2602 0.4944 -0.0017 0.0376  0.0372  414 LYS A O     
3352 C  CB    . LYS A 414 ? 0.3519 0.3018 0.5315 -0.0031 0.0411  0.0364  414 LYS A CB    
3353 C  CG    . LYS A 414 ? 0.4045 0.3528 0.5747 0.0014  0.0433  0.0383  414 LYS A CG    
3354 C  CD    . LYS A 414 ? 0.4534 0.4039 0.6217 0.0025  0.0438  0.0364  414 LYS A CD    
3355 C  CE    . LYS A 414 ? 0.5009 0.4585 0.6722 0.004   0.0467  0.0392  414 LYS A CE    
3356 N  NZ    . LYS A 414 ? 0.5285 0.4928 0.7111 0.0005  0.0467  0.0402  414 LYS A NZ    
3357 N  N     . SER A 415 ? 0.3079 0.246  0.4876 -0.0068 0.0351  0.032   415 SER A N     
3358 C  CA    . SER A 415 ? 0.3085 0.2401 0.4848 -0.0071 0.0325  0.0299  415 SER A CA    
3359 C  C     . SER A 415 ? 0.305  0.2325 0.4818 -0.0077 0.0311  0.0316  415 SER A C     
3360 O  O     . SER A 415 ? 0.3098 0.2308 0.4793 -0.0061 0.0298  0.0323  415 SER A O     
3361 C  CB    . SER A 415 ? 0.3211 0.2544 0.5035 -0.0099 0.0309  0.0262  415 SER A CB    
3362 O  OG    . SER A 415 ? 0.3567 0.2848 0.5362 -0.0101 0.0286  0.0245  415 SER A OG    
3363 N  N     . PHE A 416 ? 0.2946 0.2254 0.4794 -0.01   0.0312  0.0326  416 PHE A N     
3364 C  CA    . PHE A 416 ? 0.2931 0.2206 0.4794 -0.0109 0.0298  0.0343  416 PHE A CA    
3365 C  C     . PHE A 416 ? 0.2874 0.2121 0.4663 -0.0082 0.0313  0.0383  416 PHE A C     
3366 O  O     . PHE A 416 ? 0.2918 0.2102 0.4661 -0.0076 0.0295  0.0391  416 PHE A O     
3367 C  CB    . PHE A 416 ? 0.2917 0.2238 0.4883 -0.0138 0.0295  0.0347  416 PHE A CB    
3368 C  CG    . PHE A 416 ? 0.302  0.2357 0.506  -0.0165 0.0278  0.0309  416 PHE A CG    
3369 C  CD1   . PHE A 416 ? 0.319  0.2495 0.5214 -0.0166 0.0261  0.0277  416 PHE A CD1   
3370 C  CD2   . PHE A 416 ? 0.3088 0.247  0.5213 -0.0188 0.0276  0.0306  416 PHE A CD2   
3371 C  CE1   . PHE A 416 ? 0.3292 0.2615 0.5382 -0.0186 0.0249  0.0243  416 PHE A CE1   
3372 C  CE2   . PHE A 416 ? 0.3201 0.2592 0.5385 -0.0207 0.026   0.0269  416 PHE A CE2   
3373 C  CZ    . PHE A 416 ? 0.3242 0.2605 0.5407 -0.0205 0.0249  0.0237  416 PHE A CZ    
3374 N  N     . VAL A 417 ? 0.2774 0.2069 0.4554 -0.0065 0.0344  0.0409  417 VAL A N     
3375 C  CA    . VAL A 417 ? 0.2804 0.2082 0.4515 -0.0036 0.0366  0.0449  417 VAL A CA    
3376 C  C     . VAL A 417 ? 0.2898 0.2107 0.4485 0.0002  0.0364  0.0445  417 VAL A C     
3377 O  O     . VAL A 417 ? 0.2957 0.2113 0.447  0.0023  0.0364  0.0467  417 VAL A O     
3378 C  CB    . VAL A 417 ? 0.2805 0.2162 0.4554 -0.0029 0.0402  0.0482  417 VAL A CB    
3379 C  CG1   . VAL A 417 ? 0.2858 0.2205 0.4538 0.0004  0.043   0.0528  417 VAL A CG1   
3380 C  CG2   . VAL A 417 ? 0.2814 0.2227 0.4685 -0.0068 0.0395  0.0487  417 VAL A CG2   
3381 N  N     . SER A 418 ? 0.2897 0.2102 0.4457 0.0009  0.0358  0.0415  418 SER A N     
3382 C  CA    . SER A 418 ? 0.2985 0.2123 0.4429 0.0044  0.0352  0.041   418 SER A CA    
3383 C  C     . SER A 418 ? 0.3094 0.2145 0.4496 0.0037  0.0311  0.0394  418 SER A C     
3384 O  O     . SER A 418 ? 0.3224 0.2203 0.4518 0.0067  0.0302  0.0401  418 SER A O     
3385 C  CB    . SER A 418 ? 0.3068 0.2231 0.4501 0.0052  0.0357  0.0386  418 SER A CB    
3386 O  OG    . SER A 418 ? 0.3227 0.2468 0.4695 0.0061  0.0392  0.04    418 SER A OG    
3387 N  N     . LEU A 419 ? 0.3016 0.2071 0.4501 -0.0001 0.0285  0.0373  419 LEU A N     
3388 C  CA    . LEU A 419 ? 0.3032 0.2011 0.4489 -0.0009 0.0245  0.0359  419 LEU A CA    
3389 C  C     . LEU A 419 ? 0.3024 0.1974 0.4521 -0.003  0.0223  0.0369  419 LEU A C     
3390 O  O     . LEU A 419 ? 0.3084 0.1964 0.4549 -0.0033 0.0188  0.0362  419 LEU A O     
3391 C  CB    . LEU A 419 ? 0.2998 0.1991 0.45   -0.003  0.0227  0.0324  419 LEU A CB    
3392 C  CG    . LEU A 419 ? 0.3103 0.2093 0.4539 -0.0007 0.0234  0.0314  419 LEU A CG    
3393 C  CD1   . LEU A 419 ? 0.3126 0.2152 0.4622 -0.003  0.0226  0.0284  419 LEU A CD1   
3394 C  CD2   . LEU A 419 ? 0.3206 0.2103 0.4525 0.0021  0.021   0.0321  419 LEU A CD2   
3395 N  N     . SER A 420 ? 0.298  0.1977 0.4544 -0.0045 0.024   0.0386  420 SER A N     
3396 C  CA    . SER A 420 ? 0.3096 0.2065 0.4699 -0.0065 0.0218  0.0397  420 SER A CA    
3397 C  C     . SER A 420 ? 0.335  0.227  0.4871 -0.0042 0.0223  0.0434  420 SER A C     
3398 O  O     . SER A 420 ? 0.3455 0.241  0.4949 -0.0022 0.0259  0.046   420 SER A O     
3399 C  CB    . SER A 420 ? 0.3093 0.2131 0.4814 -0.0095 0.0227  0.0396  420 SER A CB    
3400 O  OG    . SER A 420 ? 0.3241 0.2335 0.5031 -0.0112 0.0231  0.0366  420 SER A OG    
3401 N  N     . ASP A 421 ? 0.3447 0.2292 0.4937 -0.0046 0.0189  0.0438  421 ASP A N     
3402 C  CA    . ASP A 421 ? 0.3607 0.2403 0.5026 -0.0028 0.0191  0.0473  421 ASP A CA    
3403 C  C     . ASP A 421 ? 0.3581 0.2422 0.5093 -0.0055 0.0198  0.0494  421 ASP A C     
3404 O  O     . ASP A 421 ? 0.3592 0.2437 0.507  -0.0042 0.022   0.0531  421 ASP A O     
3405 C  CB    . ASP A 421 ? 0.3996 0.2685 0.5338 -0.0022 0.0147  0.047   421 ASP A CB    
3406 C  CG    . ASP A 421 ? 0.4821 0.3458 0.6057 0.0009  0.0139  0.0457  421 ASP A CG    
3407 O  OD1   . ASP A 421 ? 0.499  0.3634 0.6259 -0.0003 0.0121  0.0427  421 ASP A OD1   
3408 O  OD2   . ASP A 421 ? 0.5156 0.3745 0.6273 0.0047  0.0151  0.0478  421 ASP A OD2   
3409 N  N     . PHE A 422 ? 0.3524 0.2398 0.5151 -0.0092 0.0179  0.0471  422 PHE A N     
3410 C  CA    . PHE A 422 ? 0.3518 0.2431 0.524  -0.012  0.0179  0.0486  422 PHE A CA    
3411 C  C     . PHE A 422 ? 0.3443 0.2431 0.5273 -0.0144 0.0185  0.0458  422 PHE A C     
3412 O  O     . PHE A 422 ? 0.3476 0.2461 0.5333 -0.0152 0.0169  0.0421  422 PHE A O     
3413 C  CB    . PHE A 422 ? 0.3549 0.24   0.5293 -0.0139 0.0136  0.0485  422 PHE A CB    
3414 C  CG    . PHE A 422 ? 0.3745 0.2505 0.5376 -0.0117 0.0118  0.0503  422 PHE A CG    
3415 C  CD1   . PHE A 422 ? 0.3876 0.2613 0.5444 -0.0103 0.0132  0.0545  422 PHE A CD1   
3416 C  CD2   . PHE A 422 ? 0.3917 0.2612 0.5499 -0.011  0.0085  0.0481  422 PHE A CD2   
3417 C  CE1   . PHE A 422 ? 0.4062 0.2707 0.5514 -0.008  0.0113  0.056   422 PHE A CE1   
3418 C  CE2   . PHE A 422 ? 0.4096 0.2698 0.5567 -0.0089 0.0063  0.0497  422 PHE A CE2   
3419 C  CZ    . PHE A 422 ? 0.4097 0.2672 0.5499 -0.0073 0.0077  0.0535  422 PHE A CZ    
3420 N  N     . ILE A 423 ? 0.3343 0.2397 0.5235 -0.0156 0.0208  0.0476  423 ILE A N     
3421 C  CA    . ILE A 423 ? 0.3313 0.2432 0.5304 -0.0178 0.021   0.045   423 ILE A CA    
3422 C  C     . ILE A 423 ? 0.3288 0.2415 0.5369 -0.0209 0.019   0.0459  423 ILE A C     
3423 O  O     . ILE A 423 ? 0.3276 0.2417 0.5364 -0.0212 0.02    0.0498  423 ILE A O     
3424 C  CB    . ILE A 423 ? 0.3352 0.2541 0.5346 -0.0168 0.0247  0.0462  423 ILE A CB    
3425 C  CG1   . ILE A 423 ? 0.3462 0.2641 0.5367 -0.0137 0.0265  0.0452  423 ILE A CG1   
3426 C  CG2   . ILE A 423 ? 0.3368 0.2616 0.5465 -0.0195 0.0243  0.0438  423 ILE A CG2   
3427 C  CD1   . ILE A 423 ? 0.3557 0.2796 0.5448 -0.0119 0.0304  0.0473  423 ILE A CD1   
3428 N  N     . VAL A 424 ? 0.324  0.2358 0.5388 -0.0229 0.0162  0.0424  424 VAL A N     
3429 C  CA    . VAL A 424 ? 0.3256 0.2377 0.5491 -0.0256 0.0139  0.0426  424 VAL A CA    
3430 C  C     . VAL A 424 ? 0.3237 0.2411 0.5556 -0.0274 0.0139  0.0398  424 VAL A C     
3431 O  O     . VAL A 424 ? 0.3276 0.2457 0.5605 -0.0271 0.0137  0.0358  424 VAL A O     
3432 C  CB    . VAL A 424 ? 0.3375 0.2433 0.562  -0.0264 0.0102  0.0412  424 VAL A CB    
3433 C  CG1   . VAL A 424 ? 0.342  0.2479 0.5757 -0.0291 0.0077  0.0413  424 VAL A CG1   
3434 C  CG2   . VAL A 424 ? 0.3496 0.2493 0.565  -0.0247 0.0098  0.0443  424 VAL A CG2   
3435 N  N     . LEU A 425 ? 0.3139 0.2349 0.5517 -0.0291 0.014   0.042   425 LEU A N     
3436 C  CA    . LEU A 425 ? 0.3084 0.2338 0.5538 -0.0308 0.0135  0.0395  425 LEU A CA    
3437 C  C     . LEU A 425 ? 0.3029 0.2263 0.556  -0.0332 0.01    0.039   425 LEU A C     
3438 O  O     . LEU A 425 ? 0.3108 0.2325 0.5648 -0.0342 0.009   0.0427  425 LEU A O     
3439 C  CB    . LEU A 425 ? 0.3102 0.2416 0.557  -0.0311 0.0159  0.0427  425 LEU A CB    
3440 C  CG    . LEU A 425 ? 0.3395 0.2734 0.5787 -0.0285 0.0197  0.0448  425 LEU A CG    
3441 C  CD1   . LEU A 425 ? 0.3419 0.2821 0.5842 -0.029  0.0217  0.0485  425 LEU A CD1   
3442 C  CD2   . LEU A 425 ? 0.3533 0.2872 0.5884 -0.0268 0.0206  0.0405  425 LEU A CD2   
3443 N  N     . ASP A 426 ? 0.2912 0.2147 0.5498 -0.0341 0.0082  0.0345  426 ASP A N     
3444 C  CA    . ASP A 426 ? 0.2883 0.21   0.5547 -0.0363 0.0047  0.0335  426 ASP A CA    
3445 C  C     . ASP A 426 ? 0.2817 0.2069 0.5521 -0.0367 0.0048  0.03    426 ASP A C     
3446 O  O     . ASP A 426 ? 0.2887 0.2129 0.5604 -0.0361 0.0041  0.0254  426 ASP A O     
3447 C  CB    . ASP A 426 ? 0.3079 0.2244 0.5756 -0.036  0.0022  0.0309  426 ASP A CB    
3448 C  CG    . ASP A 426 ? 0.3666 0.2805 0.6419 -0.0379 -0.0016 0.0303  426 ASP A CG    
3449 O  OD1   . ASP A 426 ? 0.3702 0.2863 0.6501 -0.0397 -0.0025 0.0315  426 ASP A OD1   
3450 O  OD2   . ASP A 426 ? 0.4082 0.3179 0.6851 -0.0378 -0.0038 0.0288  426 ASP A OD2   
3451 N  N     . CYS A 427 ? 0.2664 0.196  0.5382 -0.0376 0.0059  0.0325  427 CYS A N     
3452 C  CA    . CYS A 427 ? 0.2587 0.1919 0.5327 -0.0379 0.0062  0.0298  427 CYS A CA    
3453 C  C     . CYS A 427 ? 0.2503 0.1845 0.5315 -0.0404 0.0034  0.0305  427 CYS A C     
3454 O  O     . CYS A 427 ? 0.2506 0.1866 0.5342 -0.0419 0.0031  0.0353  427 CYS A O     
3455 C  CB    . CYS A 427 ? 0.2616 0.1994 0.5306 -0.0366 0.0099  0.0317  427 CYS A CB    
3456 S  SG    . CYS A 427 ? 0.2975 0.2338 0.5572 -0.0335 0.0129  0.0308  427 CYS A SG    
3457 N  N     . PRO A 428 ? 0.2409 0.1748 0.5249 -0.0406 0.0018  0.0259  428 PRO A N     
3458 C  CA    . PRO A 428 ? 0.2393 0.1742 0.5293 -0.0429 -0.0011 0.0265  428 PRO A CA    
3459 C  C     . PRO A 428 ? 0.2447 0.1854 0.5342 -0.0434 0.0011  0.0301  428 PRO A C     
3460 O  O     . PRO A 428 ? 0.2517 0.1951 0.5358 -0.0415 0.0045  0.0297  428 PRO A O     
3461 C  CB    . PRO A 428 ? 0.2453 0.1784 0.5358 -0.0421 -0.0025 0.0202  428 PRO A CB    
3462 C  CG    . PRO A 428 ? 0.2502 0.1811 0.5369 -0.0399 -0.0008 0.0169  428 PRO A CG    
3463 C  CD    . PRO A 428 ? 0.2335 0.1663 0.5151 -0.0388 0.0025  0.0203  428 PRO A CD    
3464 N  N     . ILE A 429 ? 0.2414 0.1839 0.5365 -0.0458 -0.0011 0.0338  429 ILE A N     
3465 C  CA    . ILE A 429 ? 0.2436 0.192  0.5395 -0.0464 0.0007  0.0375  429 ILE A CA    
3466 C  C     . ILE A 429 ? 0.2551 0.2036 0.5557 -0.0481 -0.0028 0.0351  429 ILE A C     
3467 O  O     . ILE A 429 ? 0.261  0.2062 0.5671 -0.0503 -0.0072 0.0348  429 ILE A O     
3468 C  CB    . ILE A 429 ? 0.2384 0.1896 0.5374 -0.0479 0.0012  0.0446  429 ILE A CB    
3469 C  CG1   . ILE A 429 ? 0.2486 0.1983 0.5421 -0.0461 0.004   0.0467  429 ILE A CG1   
3470 C  CG2   . ILE A 429 ? 0.2382 0.1962 0.539  -0.0483 0.0032  0.0487  429 ILE A CG2   
3471 C  CD1   . ILE A 429 ? 0.2677 0.2191 0.5533 -0.043  0.0084  0.0457  429 ILE A CD1   
3472 N  N     . ILE A 430 ? 0.256  0.2074 0.554  -0.0472 -0.0012 0.0331  430 ILE A N     
3473 C  CA    . ILE A 430 ? 0.2668 0.2176 0.5682 -0.0486 -0.0047 0.0305  430 ILE A CA    
3474 C  C     . ILE A 430 ? 0.2796 0.2324 0.589  -0.0519 -0.0081 0.0357  430 ILE A C     
3475 O  O     . ILE A 430 ? 0.2796 0.2378 0.5909 -0.0526 -0.006  0.0415  430 ILE A O     
3476 C  CB    . ILE A 430 ? 0.2736 0.2273 0.5707 -0.0471 -0.0026 0.0279  430 ILE A CB    
3477 C  CG1   . ILE A 430 ? 0.2857 0.2389 0.575  -0.044  0.0016  0.0246  430 ILE A CG1   
3478 C  CG2   . ILE A 430 ? 0.2816 0.2324 0.5804 -0.0481 -0.0066 0.0236  430 ILE A CG2   
3479 C  CD1   . ILE A 430 ? 0.3079 0.2558 0.5954 -0.0429 0.0003  0.0191  430 ILE A CD1   
3480 N  N     . GLY A 431 ? 0.2861 0.2343 0.6    -0.0539 -0.0133 0.0338  431 GLY A N     
3481 C  CA    . GLY A 431 ? 0.2943 0.2434 0.6163 -0.0574 -0.0174 0.0387  431 GLY A CA    
3482 C  C     . GLY A 431 ? 0.3035 0.2504 0.6294 -0.0589 -0.019  0.0422  431 GLY A C     
3483 O  O     . GLY A 431 ? 0.3044 0.2516 0.6375 -0.0621 -0.0228 0.0465  431 GLY A O     
3484 N  N     . GLU A 432 ? 0.3073 0.2519 0.6286 -0.0569 -0.0163 0.0408  432 GLU A N     
3485 C  CA    . GLU A 432 ? 0.3116 0.2535 0.6356 -0.058  -0.0177 0.0437  432 GLU A CA    
3486 C  C     . GLU A 432 ? 0.3157 0.2502 0.6385 -0.057  -0.0204 0.0379  432 GLU A C     
3487 O  O     . GLU A 432 ? 0.3184 0.2508 0.6365 -0.0546 -0.0193 0.032   432 GLU A O     
3488 C  CB    . GLU A 432 ? 0.339  0.2847 0.6595 -0.0568 -0.0127 0.0485  432 GLU A CB    
3489 C  CG    . GLU A 432 ? 0.4084 0.3614 0.7317 -0.0579 -0.0105 0.0551  432 GLU A CG    
3490 C  CD    . GLU A 432 ? 0.4939 0.4498 0.8172 -0.0581 -0.0077 0.0619  432 GLU A CD    
3491 O  OE1   . GLU A 432 ? 0.5179 0.4727 0.8344 -0.0555 -0.0041 0.0613  432 GLU A OE1   
3492 O  OE2   . GLU A 432 ? 0.5147 0.4739 0.8448 -0.0608 -0.0092 0.068   432 GLU A OE2   
3493 N  N     . SER A 433 ? 0.3144 0.245  0.6416 -0.0589 -0.0241 0.0398  433 SER A N     
3494 C  CA    . SER A 433 ? 0.3226 0.246  0.6499 -0.0581 -0.0273 0.0348  433 SER A CA    
3495 C  C     . SER A 433 ? 0.324  0.2456 0.6463 -0.0555 -0.0241 0.0329  433 SER A C     
3496 O  O     . SER A 433 ? 0.3276 0.2446 0.6488 -0.0538 -0.0254 0.0274  433 SER A O     
3497 C  CB    . SER A 433 ? 0.3411 0.2604 0.6753 -0.0612 -0.033  0.0375  433 SER A CB    
3498 O  OG    . SER A 433 ? 0.3665 0.2883 0.7065 -0.0644 -0.036  0.0417  433 SER A OG    
3499 N  N     . TYR A 434 ? 0.3197 0.2447 0.6394 -0.0552 -0.0204 0.0375  434 TYR A N     
3500 C  CA    . TYR A 434 ? 0.3265 0.2491 0.6415 -0.053  -0.0181 0.0364  434 TYR A CA    
3501 C  C     . TYR A 434 ? 0.3305 0.2573 0.6385 -0.0508 -0.0124 0.0377  434 TYR A C     
3502 O  O     . TYR A 434 ? 0.3258 0.2579 0.6328 -0.0508 -0.0099 0.04    434 TYR A O     
3503 C  CB    . TYR A 434 ? 0.3256 0.245  0.6438 -0.0548 -0.0206 0.0405  434 TYR A CB    
3504 C  CG    . TYR A 434 ? 0.3348 0.2484 0.6586 -0.0562 -0.0263 0.0377  434 TYR A CG    
3505 C  CD1   . TYR A 434 ? 0.3512 0.26   0.6741 -0.0542 -0.0275 0.0318  434 TYR A CD1   
3506 C  CD2   . TYR A 434 ? 0.3419 0.2551 0.6723 -0.0594 -0.0306 0.0407  434 TYR A CD2   
3507 C  CE1   . TYR A 434 ? 0.364  0.2673 0.6918 -0.055  -0.0327 0.0288  434 TYR A CE1   
3508 C  CE2   . TYR A 434 ? 0.3549 0.2621 0.69   -0.0605 -0.0362 0.0377  434 TYR A CE2   
3509 C  CZ    . TYR A 434 ? 0.3748 0.2769 0.7083 -0.0581 -0.0372 0.0316  434 TYR A CZ    
3510 O  OH    . TYR A 434 ? 0.3996 0.2954 0.7374 -0.0586 -0.0426 0.0285  434 TYR A OH    
3511 N  N     . ASN A 435 ? 0.3369 0.2613 0.6402 -0.0487 -0.0106 0.0361  435 ASN A N     
3512 C  CA    . ASN A 435 ? 0.3506 0.2777 0.6467 -0.0464 -0.0059 0.0371  435 ASN A CA    
3513 C  C     . ASN A 435 ? 0.3455 0.2751 0.6395 -0.0469 -0.0036 0.0438  435 ASN A C     
3514 O  O     . ASN A 435 ? 0.3505 0.2787 0.648  -0.0488 -0.0057 0.0478  435 ASN A O     
3515 C  CB    . ASN A 435 ? 0.3848 0.3081 0.6769 -0.0442 -0.0053 0.0334  435 ASN A CB    
3516 C  CG    . ASN A 435 ? 0.4514 0.3743 0.7432 -0.0428 -0.0052 0.0272  435 ASN A CG    
3517 O  OD1   . ASN A 435 ? 0.4743 0.3978 0.7697 -0.0436 -0.0069 0.0247  435 ASN A OD1   
3518 N  ND2   . ASN A 435 ? 0.4667 0.3883 0.7542 -0.0406 -0.0034 0.0247  435 ASN A ND2   
3519 N  N     . GLU A 436 ? 0.3333 0.2663 0.621  -0.0448 0.0007  0.0451  436 GLU A N     
3520 C  CA    . GLU A 436 ? 0.3269 0.2619 0.6104 -0.0441 0.0036  0.0508  436 GLU A CA    
3521 C  C     . GLU A 436 ? 0.3181 0.2492 0.5938 -0.0416 0.0052  0.0494  436 GLU A C     
3522 O  O     . GLU A 436 ? 0.3204 0.251  0.5924 -0.0397 0.0064  0.0451  436 GLU A O     
3523 C  CB    . GLU A 436 ? 0.3495 0.291  0.631  -0.0431 0.0074  0.0531  436 GLU A CB    
3524 C  CG    . GLU A 436 ? 0.3865 0.333  0.6753 -0.0456 0.0065  0.0571  436 GLU A CG    
3525 C  CD    . GLU A 436 ? 0.4497 0.3963 0.7424 -0.0478 0.0053  0.0632  436 GLU A CD    
3526 O  OE1   . GLU A 436 ? 0.4559 0.4007 0.7435 -0.0465 0.0072  0.0662  436 GLU A OE1   
3527 O  OE2   . GLU A 436 ? 0.4764 0.4248 0.7772 -0.0508 0.0024  0.0652  436 GLU A OE2   
3528 N  N     . PHE A 437 ? 0.3064 0.2344 0.5792 -0.0415 0.0052  0.0531  437 PHE A N     
3529 C  CA    . PHE A 437 ? 0.3024 0.2261 0.5672 -0.0391 0.0063  0.0522  437 PHE A CA    
3530 C  C     . PHE A 437 ? 0.3027 0.2285 0.56   -0.0371 0.0103  0.0569  437 PHE A C     
3531 O  O     . PHE A 437 ? 0.299  0.2271 0.5577 -0.038  0.0111  0.0622  437 PHE A O     
3532 C  CB    . PHE A 437 ? 0.2969 0.2142 0.5628 -0.04   0.0028  0.0522  437 PHE A CB    
3533 C  CG    . PHE A 437 ? 0.3055 0.218  0.5626 -0.0378 0.0037  0.053   437 PHE A CG    
3534 C  CD1   . PHE A 437 ? 0.3181 0.2282 0.5711 -0.0359 0.0038  0.0488  437 PHE A CD1   
3535 C  CD2   . PHE A 437 ? 0.3165 0.227  0.5691 -0.0376 0.0043  0.0582  437 PHE A CD2   
3536 C  CE1   . PHE A 437 ? 0.3289 0.2341 0.5736 -0.034  0.0041  0.0496  437 PHE A CE1   
3537 C  CE2   . PHE A 437 ? 0.3318 0.2371 0.5755 -0.0355 0.0048  0.0588  437 PHE A CE2   
3538 C  CZ    . PHE A 437 ? 0.3298 0.2323 0.5696 -0.0337 0.0044  0.0545  437 PHE A CZ    
3539 N  N     . ARG A 438 ? 0.302  0.2268 0.5513 -0.0342 0.0126  0.055   438 ARG A N     
3540 C  CA    . ARG A 438 ? 0.3056 0.231  0.5461 -0.0316 0.0163  0.0588  438 ARG A CA    
3541 C  C     . ARG A 438 ? 0.3083 0.2273 0.5399 -0.0292 0.016   0.0568  438 ARG A C     
3542 O  O     . ARG A 438 ? 0.3056 0.2226 0.5373 -0.0289 0.0146  0.052   438 ARG A O     
3543 C  CB    . ARG A 438 ? 0.3192 0.251  0.5583 -0.03   0.02    0.0589  438 ARG A CB    
3544 C  CG    . ARG A 438 ? 0.348  0.2867 0.5956 -0.0322 0.0204  0.0612  438 ARG A CG    
3545 C  CD    . ARG A 438 ? 0.3818 0.3229 0.6312 -0.033  0.0215  0.0678  438 ARG A CD    
3546 N  NE    . ARG A 438 ? 0.406  0.3541 0.6641 -0.0352 0.0217  0.0702  438 ARG A NE    
3547 C  CZ    . ARG A 438 ? 0.4169 0.3654 0.6844 -0.0388 0.0181  0.0706  438 ARG A CZ    
3548 N  NH1   . ARG A 438 ? 0.4109 0.3535 0.6804 -0.0405 0.0143  0.0687  438 ARG A NH1   
3549 N  NH2   . ARG A 438 ? 0.4122 0.3668 0.6873 -0.0408 0.018   0.073   438 ARG A NH2   
3550 N  N     . LEU A 439 ? 0.3144 0.2301 0.5385 -0.0275 0.0171  0.0605  439 LEU A N     
3551 C  CA    . LEU A 439 ? 0.3305 0.2396 0.5447 -0.025  0.0168  0.0593  439 LEU A CA    
3552 C  C     . LEU A 439 ? 0.3455 0.2566 0.5507 -0.0217 0.0211  0.0626  439 LEU A C     
3553 O  O     . LEU A 439 ? 0.3554 0.2675 0.5585 -0.0212 0.023   0.0675  439 LEU A O     
3554 C  CB    . LEU A 439 ? 0.3369 0.2387 0.5489 -0.0256 0.0136  0.0606  439 LEU A CB    
3555 C  CG    . LEU A 439 ? 0.369  0.2633 0.569  -0.0227 0.0132  0.0606  439 LEU A CG    
3556 C  CD1   . LEU A 439 ? 0.3751 0.268  0.5727 -0.0215 0.0125  0.0558  439 LEU A CD1   
3557 C  CD2   . LEU A 439 ? 0.3834 0.2704 0.5824 -0.0238 0.0094  0.0616  439 LEU A CD2   
3558 N  N     . ILE A 440 ? 0.3413 0.2534 0.5417 -0.0194 0.0229  0.0599  440 ILE A N     
3559 C  CA    . ILE A 440 ? 0.3412 0.2553 0.5333 -0.0159 0.0271  0.0625  440 ILE A CA    
3560 C  C     . ILE A 440 ? 0.3464 0.2527 0.5263 -0.0127 0.0265  0.0616  440 ILE A C     
3561 O  O     . ILE A 440 ? 0.345  0.2482 0.5232 -0.0124 0.0246  0.0575  440 ILE A O     
3562 C  CB    . ILE A 440 ? 0.3422 0.2632 0.5376 -0.0154 0.0294  0.0605  440 ILE A CB    
3563 C  CG1   . ILE A 440 ? 0.3469 0.2752 0.5547 -0.0188 0.0292  0.061   440 ILE A CG1   
3564 C  CG2   . ILE A 440 ? 0.3491 0.2721 0.5358 -0.0114 0.0337  0.0631  440 ILE A CG2   
3565 C  CD1   . ILE A 440 ? 0.3594 0.2923 0.5704 -0.0194 0.0313  0.0669  440 ILE A CD1   
3566 N  N     . ILE A 441 ? 0.3523 0.255  0.5233 -0.0102 0.0281  0.0656  441 ILE A N     
3567 C  CA    . ILE A 441 ? 0.3679 0.2622 0.5258 -0.0068 0.0274  0.065   441 ILE A CA    
3568 C  C     . ILE A 441 ? 0.3751 0.2726 0.5267 -0.0031 0.0313  0.0649  441 ILE A C     
3569 O  O     . ILE A 441 ? 0.3812 0.2817 0.5285 -0.0006 0.0354  0.0688  441 ILE A O     
3570 C  CB    . ILE A 441 ? 0.3797 0.2682 0.53   -0.0055 0.0273  0.0692  441 ILE A CB    
3571 C  CG1   . ILE A 441 ? 0.3873 0.2741 0.5458 -0.0096 0.0237  0.07    441 ILE A CG1   
3572 C  CG2   . ILE A 441 ? 0.396  0.2744 0.5322 -0.002  0.0257  0.0682  441 ILE A CG2   
3573 C  CD1   . ILE A 441 ? 0.3998 0.2814 0.5618 -0.0118 0.0186  0.0656  441 ILE A CD1   
3574 N  N     . ASN A 442 ? 0.3732 0.2708 0.5252 -0.003  0.0303  0.0606  442 ASN A N     
3575 C  CA    . ASN A 442 ? 0.3797 0.2807 0.5271 0       0.0335  0.0599  442 ASN A CA    
3576 C  C     . ASN A 442 ? 0.3936 0.2864 0.5268 0.0042  0.033   0.059   442 ASN A C     
3577 O  O     . ASN A 442 ? 0.3966 0.2911 0.5258 0.0067  0.0349  0.0577  442 ASN A O     
3578 C  CB    . ASN A 442 ? 0.3871 0.2932 0.5436 -0.0025 0.0325  0.0558  442 ASN A CB    
3579 C  CG    . ASN A 442 ? 0.4218 0.3338 0.5775 -0.0005 0.0358  0.0553  442 ASN A CG    
3580 O  OD1   . ASN A 442 ? 0.4396 0.3579 0.5973 0.0005  0.0395  0.0584  442 ASN A OD1   
3581 N  ND2   . ASN A 442 ? 0.4207 0.3307 0.574  0       0.0344  0.0514  442 ASN A ND2   
3582 N  N     . LYS A 443 ? 0.4018 0.2853 0.5273 0.005   0.0301  0.0596  443 LYS A N     
3583 C  CA    . LYS A 443 ? 0.4191 0.2932 0.5306 0.0088  0.0286  0.0586  443 LYS A CA    
3584 C  C     . LYS A 443 ? 0.4276 0.3023 0.5286 0.014   0.0329  0.0604  443 LYS A C     
3585 O  O     . LYS A 443 ? 0.4361 0.3082 0.5312 0.0162  0.0323  0.0578  443 LYS A O     
3586 C  CB    . LYS A 443 ? 0.4502 0.3145 0.5548 0.0089  0.0251  0.06    443 LYS A CB    
3587 C  CG    . LYS A 443 ? 0.5057 0.3646 0.6145 0.0056  0.0194  0.0568  443 LYS A CG    
3588 C  CD    . LYS A 443 ? 0.5836 0.4309 0.6824 0.0068  0.0155  0.0579  443 LYS A CD    
3589 C  CE    . LYS A 443 ? 0.6458 0.4884 0.75   0.0034  0.0096  0.0551  443 LYS A CE    
3590 N  NZ    . LYS A 443 ? 0.6702 0.5088 0.7772 0.0011  0.0066  0.0569  443 LYS A NZ    
3591 N  N     . ASN A 444 ? 0.4216 0.2999 0.5206 0.016   0.0372  0.0647  444 ASN A N     
3592 C  CA    . ASN A 444 ? 0.4267 0.3061 0.5161 0.0214  0.0417  0.0667  444 ASN A CA    
3593 C  C     . ASN A 444 ? 0.4205 0.3083 0.5157 0.0217  0.0443  0.0651  444 ASN A C     
3594 O  O     . ASN A 444 ? 0.4251 0.3112 0.5114 0.026   0.046   0.0643  444 ASN A O     
3595 C  CB    . ASN A 444 ? 0.4443 0.3277 0.533  0.023   0.0461  0.0722  444 ASN A CB    
3596 C  CG    . ASN A 444 ? 0.4956 0.3691 0.5694 0.0269  0.046   0.0744  444 ASN A CG    
3597 O  OD1   . ASN A 444 ? 0.5148 0.3773 0.579  0.0279  0.0417  0.0718  444 ASN A OD1   
3598 N  ND2   . ASN A 444 ? 0.5061 0.3833 0.5777 0.029   0.0506  0.0795  444 ASN A ND2   
3599 N  N     . ASN A 445 ? 0.4076 0.3043 0.5174 0.0173  0.0445  0.0645  445 ASN A N     
3600 C  CA    . ASN A 445 ? 0.4018 0.307  0.5185 0.0169  0.0466  0.0632  445 ASN A CA    
3601 C  C     . ASN A 445 ? 0.3941 0.2952 0.5081 0.0168  0.0435  0.0582  445 ASN A C     
3602 O  O     . ASN A 445 ? 0.3987 0.3018 0.5092 0.0195  0.0454  0.0573  445 ASN A O     
3603 C  CB    . ASN A 445 ? 0.4145 0.3286 0.5466 0.012   0.0468  0.0638  445 ASN A CB    
3604 C  CG    . ASN A 445 ? 0.4506 0.3746 0.5896 0.0121  0.0501  0.0643  445 ASN A CG    
3605 O  OD1   . ASN A 445 ? 0.459  0.3859 0.5929 0.0161  0.054   0.0667  445 ASN A OD1   
3606 N  ND2   . ASN A 445 ? 0.4586 0.3878 0.6092 0.0078  0.0484  0.0621  445 ASN A ND2   
3607 N  N     . LYS A 446 ? 0.3818 0.277  0.4973 0.0139  0.0387  0.0554  446 LYS A N     
3608 C  CA    . LYS A 446 ? 0.3751 0.2661 0.4884 0.0134  0.0354  0.0511  446 LYS A CA    
3609 C  C     . LYS A 446 ? 0.381  0.264  0.4793 0.0185  0.0352  0.0509  446 LYS A C     
3610 O  O     . LYS A 446 ? 0.3788 0.2621 0.4744 0.0199  0.0352  0.0487  446 LYS A O     
3611 C  CB    . LYS A 446 ? 0.3795 0.2658 0.4975 0.0095  0.0304  0.0488  446 LYS A CB    
3612 C  CG    . LYS A 446 ? 0.4116 0.2922 0.526  0.0094  0.0267  0.0452  446 LYS A CG    
3613 C  CD    . LYS A 446 ? 0.4471 0.3242 0.5673 0.0056  0.0222  0.0434  446 LYS A CD    
3614 C  CE    . LYS A 446 ? 0.471  0.3422 0.5869 0.0057  0.0184  0.0406  446 LYS A CE    
3615 N  NZ    . LYS A 446 ? 0.4702 0.3394 0.5936 0.0019  0.0143  0.0389  446 LYS A NZ    
3616 N  N     . GLU A 447 ? 0.3854 0.2609 0.4735 0.0212  0.0348  0.0532  447 GLU A N     
3617 C  CA    . GLU A 447 ? 0.3987 0.2651 0.4711 0.0264  0.0343  0.053   447 GLU A CA    
3618 C  C     . GLU A 447 ? 0.4078 0.2792 0.4761 0.0307  0.0391  0.0539  447 GLU A C     
3619 O  O     . GLU A 447 ? 0.4187 0.2854 0.4786 0.0338  0.038   0.0519  447 GLU A O     
3620 C  CB    . GLU A 447 ? 0.4249 0.2832 0.4874 0.0287  0.0337  0.0558  447 GLU A CB    
3621 N  N     . SER A 448 ? 0.3971 0.2783 0.4721 0.0309  0.0441  0.0571  448 SER A N     
3622 C  CA    . SER A 448 ? 0.398  0.2855 0.4712 0.0348  0.049   0.0586  448 SER A CA    
3623 C  C     . SER A 448 ? 0.3904 0.2834 0.4708 0.033   0.0484  0.0554  448 SER A C     
3624 O  O     . SER A 448 ? 0.3936 0.2862 0.4677 0.0368  0.0499  0.0546  448 SER A O     
3625 C  CB    . SER A 448 ? 0.4108 0.308  0.4914 0.0347  0.0541  0.0632  448 SER A CB    
3626 O  OG    . SER A 448 ? 0.4485 0.3406 0.5199 0.0378  0.0557  0.0666  448 SER A OG    
3627 N  N     . ILE A 449 ? 0.3771 0.2749 0.4702 0.0273  0.0463  0.0535  449 ILE A N     
3628 C  CA    . ILE A 449 ? 0.3744 0.2772 0.4743 0.0253  0.0457  0.0505  449 ILE A CA    
3629 C  C     . ILE A 449 ? 0.3938 0.2885 0.4853 0.0266  0.042   0.047   449 ILE A C     
3630 O  O     . ILE A 449 ? 0.3927 0.2897 0.4831 0.0281  0.0427  0.0455  449 ILE A O     
3631 C  CB    . ILE A 449 ? 0.3659 0.2752 0.4805 0.0193  0.0443  0.0494  449 ILE A CB    
3632 C  CG1   . ILE A 449 ? 0.3627 0.2811 0.4861 0.0182  0.048   0.0531  449 ILE A CG1   
3633 C  CG2   . ILE A 449 ? 0.3706 0.2836 0.4907 0.0173  0.0431  0.0459  449 ILE A CG2   
3634 C  CD1   . ILE A 449 ? 0.3676 0.29   0.5036 0.0128  0.0462  0.0525  449 ILE A CD1   
3635 N  N     . LEU A 450 ? 0.4121 0.2969 0.4972 0.0262  0.0378  0.0459  450 LEU A N     
3636 C  CA    . LEU A 450 ? 0.4338 0.3102 0.5109 0.0273  0.0337  0.043   450 LEU A CA    
3637 C  C     . LEU A 450 ? 0.4621 0.3329 0.525  0.0335  0.035   0.0435  450 LEU A C     
3638 O  O     . LEU A 450 ? 0.4703 0.3351 0.5269 0.0346  0.0319  0.0411  450 LEU A O     
3639 C  CB    . LEU A 450 ? 0.4413 0.3089 0.5163 0.025   0.0286  0.042   450 LEU A CB    
3640 C  CG    . LEU A 450 ? 0.4529 0.325  0.5415 0.0191  0.0268  0.041   450 LEU A CG    
3641 C  CD1   . LEU A 450 ? 0.4593 0.3224 0.5454 0.0174  0.0216  0.0403  450 LEU A CD1   
3642 C  CD2   . LEU A 450 ? 0.4561 0.3344 0.5536 0.0161  0.0264  0.0382  450 LEU A CD2   
3643 N  N     . ARG A 451 ? 0.4724 0.3454 0.5306 0.0376  0.0395  0.0466  451 ARG A N     
3644 C  CA    . ARG A 451 ? 0.4916 0.3606 0.537  0.0441  0.0416  0.0473  451 ARG A CA    
3645 C  C     . ARG A 451 ? 0.4949 0.3744 0.5458 0.0457  0.0465  0.0481  451 ARG A C     
3646 O  O     . ARG A 451 ? 0.5037 0.3811 0.5453 0.0511  0.0484  0.0484  451 ARG A O     
3647 C  CB    . ARG A 451 ? 0.5226 0.387  0.5579 0.0485  0.0441  0.0506  451 ARG A CB    
3648 C  CG    . ARG A 451 ? 0.5886 0.4416 0.6163 0.0479  0.0396  0.0504  451 ARG A CG    
3649 C  CD    . ARG A 451 ? 0.6553 0.5029 0.6702 0.0534  0.0423  0.0535  451 ARG A CD    
3650 N  NE    . ARG A 451 ? 0.706  0.5642 0.7275 0.0541  0.0488  0.0576  451 ARG A NE    
3651 C  CZ    . ARG A 451 ? 0.7429 0.6052 0.7723 0.0506  0.0497  0.0601  451 ARG A CZ    
3652 N  NH1   . ARG A 451 ? 0.7363 0.5928 0.7677 0.0464  0.0447  0.0589  451 ARG A NH1   
3653 N  NH2   . ARG A 451 ? 0.7455 0.6176 0.7808 0.0513  0.0554  0.0642  451 ARG A NH2   
3654 N  N     . LYS A 452 ? 0.4872 0.3779 0.5528 0.0414  0.0485  0.0488  452 LYS A N     
3655 C  CA    . LYS A 452 ? 0.4851 0.3862 0.5572 0.0425  0.0527  0.05    452 LYS A CA    
3656 C  C     . LYS A 452 ? 0.4878 0.3886 0.5587 0.0429  0.051   0.0467  452 LYS A C     
3657 O  O     . LYS A 452 ? 0.4898 0.3887 0.5646 0.0389  0.047   0.0436  452 LYS A O     
3658 C  CB    . LYS A 452 ? 0.4902 0.4021 0.5782 0.0373  0.0543  0.0514  452 LYS A CB    
3659 C  CG    . LYS A 452 ? 0.5155 0.4363 0.6079 0.0393  0.0599  0.0561  452 LYS A CG    
3660 C  CD    . LYS A 452 ? 0.5448 0.4694 0.6461 0.0353  0.0603  0.0587  452 LYS A CD    
3661 C  CE    . LYS A 452 ? 0.5598 0.4968 0.6742 0.0332  0.0637  0.0619  452 LYS A CE    
3662 N  NZ    . LYS A 452 ? 0.5563 0.4958 0.68   0.0283  0.0627  0.0636  452 LYS A NZ    
3663 N  N     . THR A 453 ? 0.4867 0.3889 0.5517 0.0481  0.0541  0.0477  453 THR A N     
3664 C  CA    . THR A 453 ? 0.4924 0.3949 0.5559 0.0493  0.053   0.0452  453 THR A CA    
3665 C  C     . THR A 453 ? 0.4915 0.4044 0.5603 0.0518  0.0582  0.0476  453 THR A C     
3666 O  O     . THR A 453 ? 0.4902 0.4065 0.5576 0.0553  0.0626  0.0513  453 THR A O     
3667 C  CB    . THR A 453 ? 0.5163 0.407  0.5639 0.0544  0.0505  0.0434  453 THR A CB    
3668 O  OG1   . THR A 453 ? 0.5342 0.4226 0.5721 0.0607  0.0542  0.0462  453 THR A OG1   
3669 C  CG2   . THR A 453 ? 0.5239 0.4037 0.5662 0.0518  0.0446  0.041   453 THR A CG2   
3670 N  N     . SER A 454 ? 0.4896 0.4077 0.5647 0.0501  0.0576  0.0459  454 SER A N     
3671 C  CA    . SER A 454 ? 0.492  0.4199 0.5726 0.0523  0.062   0.0481  454 SER A CA    
3672 C  C     . SER A 454 ? 0.4976 0.4214 0.566  0.0598  0.0639  0.0486  454 SER A C     
3673 O  O     . SER A 454 ? 0.5067 0.4195 0.5627 0.0626  0.061   0.0464  454 SER A O     
3674 C  CB    . SER A 454 ? 0.5093 0.4437 0.6004 0.0479  0.0604  0.0461  454 SER A CB    
3675 O  OG    . SER A 454 ? 0.551  0.4797 0.6355 0.0491  0.0573  0.0428  454 SER A OG    
3676 N  N     . LYS A 455 ? 0.4901 0.4224 0.5622 0.0632  0.0688  0.0517  455 LYS A N     
3677 C  CA    . LYS A 455 ? 0.4957 0.4261 0.5578 0.0708  0.0716  0.0527  455 LYS A CA    
3678 C  C     . LYS A 455 ? 0.4979 0.4194 0.5504 0.0728  0.0675  0.0485  455 LYS A C     
3679 O  O     . LYS A 455 ? 0.4962 0.4203 0.5551 0.069   0.0648  0.0462  455 LYS A O     
3680 C  CB    . LYS A 455 ? 0.5146 0.458  0.5867 0.0724  0.0767  0.0562  455 LYS A CB    
3681 C  CG    . LYS A 455 ? 0.569  0.512  0.6328 0.0802  0.0798  0.0572  455 LYS A CG    
3682 C  CD    . LYS A 455 ? 0.6144 0.5707 0.6906 0.0804  0.0835  0.0601  455 LYS A CD    
3683 C  CE    . LYS A 455 ? 0.6652 0.6214 0.7339 0.0882  0.0864  0.0607  455 LYS A CE    
3684 N  NZ    . LYS A 455 ? 0.6825 0.6513 0.7638 0.088   0.0892  0.0633  455 LYS A NZ    
3685 N  N     . GLN A 456 ? 0.5002 0.4107 0.5371 0.0784  0.0666  0.0477  456 GLN A N     
3686 C  CA    . GLN A 456 ? 0.5055 0.4063 0.532  0.0809  0.0623  0.044   456 GLN A CA    
3687 C  C     . GLN A 456 ? 0.5002 0.4066 0.5277 0.0849  0.0649  0.0445  456 GLN A C     
3688 O  O     . GLN A 456 ? 0.5038 0.4142 0.5288 0.0907  0.0701  0.0474  456 GLN A O     
3689 C  CB    . GLN A 456 ? 0.5333 0.4207 0.5423 0.0865  0.0609  0.0434  456 GLN A CB    
3690 C  CG    . GLN A 456 ? 0.5776 0.4588 0.5844 0.0832  0.0584  0.0434  456 GLN A CG    
3691 C  CD    . GLN A 456 ? 0.6278 0.5049 0.6388 0.0765  0.0522  0.0401  456 GLN A CD    
3692 O  OE1   . GLN A 456 ? 0.6448 0.516  0.6512 0.0765  0.048   0.0372  456 GLN A OE1   
3693 N  NE2   . GLN A 456 ? 0.6275 0.5079 0.6476 0.0706  0.0515  0.0407  456 GLN A NE2   
3694 N  N     . GLN A 457 ? 0.4904 0.3971 0.5215 0.082   0.0614  0.0417  457 GLN A N     
3695 C  CA    . GLN A 457 ? 0.4866 0.398  0.5189 0.0855  0.063   0.0418  457 GLN A CA    
3696 C  C     . GLN A 457 ? 0.4833 0.3897 0.5143 0.0826  0.0574  0.0379  457 GLN A C     
3697 O  O     . GLN A 457 ? 0.4841 0.3894 0.5201 0.0761  0.0536  0.036   457 GLN A O     
3698 C  CB    . GLN A 457 ? 0.4912 0.4178 0.539  0.0834  0.0676  0.045   457 GLN A CB    
3699 C  CG    . GLN A 457 ? 0.5189 0.4515 0.5802 0.0747  0.0654  0.0441  457 GLN A CG    
3700 C  CD    . GLN A 457 ? 0.5604 0.5067 0.6364 0.0725  0.0689  0.047   457 GLN A CD    
3701 O  OE1   . GLN A 457 ? 0.581  0.5333 0.6673 0.0674  0.0695  0.0484  457 GLN A OE1   
3702 N  NE2   . GLN A 457 ? 0.5585 0.5099 0.636  0.0762  0.0709  0.048   457 GLN A NE2   
3703 N  N     . ASN A 458 ? 0.4789 0.3823 0.503  0.0876  0.057   0.0369  458 ASN A N     
3704 C  CA    . ASN A 458 ? 0.482  0.3811 0.5049 0.0852  0.0518  0.0336  458 ASN A CA    
3705 C  C     . ASN A 458 ? 0.4594 0.3702 0.4974 0.0798  0.0526  0.0341  458 ASN A C     
3706 O  O     . ASN A 458 ? 0.4582 0.3796 0.5044 0.0811  0.0574  0.0369  458 ASN A O     
3707 C  CB    . ASN A 458 ? 0.516  0.4083 0.527  0.0924  0.051   0.0326  458 ASN A CB    
3708 C  CG    . ASN A 458 ? 0.5835 0.4625 0.5778 0.0983  0.0495  0.0318  458 ASN A CG    
3709 O  OD1   . ASN A 458 ? 0.6018 0.4765 0.586  0.1058  0.0509  0.0319  458 ASN A OD1   
3710 N  ND2   . ASN A 458 ? 0.608  0.4798 0.5986 0.0951  0.0464  0.031   458 ASN A ND2   
3711 N  N     . ILE A 459 ? 0.4409 0.3503 0.4828 0.0737  0.0481  0.0315  459 ILE A N     
3712 C  CA    . ILE A 459 ? 0.4242 0.3437 0.4794 0.0686  0.0484  0.0316  459 ILE A CA    
3713 C  C     . ILE A 459 ? 0.4196 0.3362 0.4727 0.0678  0.0446  0.0291  459 ILE A C     
3714 O  O     . ILE A 459 ? 0.4248 0.3317 0.4697 0.0672  0.04    0.0268  459 ILE A O     
3715 C  CB    . ILE A 459 ? 0.4208 0.3444 0.4859 0.0612  0.0478  0.0314  459 ILE A CB    
3716 C  CG1   . ILE A 459 ? 0.4259 0.355  0.4957 0.0619  0.0523  0.0345  459 ILE A CG1   
3717 C  CG2   . ILE A 459 ? 0.4177 0.3492 0.4944 0.0557  0.0468  0.0306  459 ILE A CG2   
3718 C  CD1   . ILE A 459 ? 0.4371 0.367  0.5132 0.056   0.0511  0.0341  459 ILE A CD1   
3719 N  N     . LEU A 460 ? 0.4091 0.334  0.4694 0.068   0.0463  0.03    460 LEU A N     
3720 C  CA    . LEU A 460 ? 0.4148 0.3385 0.4748 0.0668  0.0429  0.028   460 LEU A CA    
3721 C  C     . LEU A 460 ? 0.4085 0.3439 0.4825 0.0623  0.0446  0.0291  460 LEU A C     
3722 O  O     . LEU A 460 ? 0.4042 0.3476 0.4838 0.065   0.0483  0.0317  460 LEU A O     
3723 C  CB    . LEU A 460 ? 0.4236 0.3443 0.4755 0.0741  0.0434  0.0283  460 LEU A CB    
3724 C  CG    . LEU A 460 ? 0.4432 0.3612 0.4933 0.0732  0.0394  0.0263  460 LEU A CG    
3725 C  CD1   . LEU A 460 ? 0.4531 0.3604 0.4956 0.0702  0.0337  0.0234  460 LEU A CD1   
3726 C  CD2   . LEU A 460 ? 0.4555 0.3716 0.4988 0.0807  0.0405  0.0268  460 LEU A CD2   
3727 N  N     . VAL A 461 ? 0.407  0.3434 0.4868 0.0555  0.042   0.0275  461 VAL A N     
3728 C  CA    . VAL A 461 ? 0.4101 0.3564 0.5025 0.051   0.0431  0.0282  461 VAL A CA    
3729 C  C     . VAL A 461 ? 0.4219 0.3714 0.5161 0.052   0.0421  0.028   461 VAL A C     
3730 O  O     . VAL A 461 ? 0.4356 0.3792 0.524  0.0514  0.0384  0.0258  461 VAL A O     
3731 C  CB    . VAL A 461 ? 0.4136 0.3595 0.5106 0.044   0.0406  0.0263  461 VAL A CB    
3732 C  CG1   . VAL A 461 ? 0.4146 0.37   0.5237 0.0395  0.0413  0.0268  461 VAL A CG1   
3733 C  CG2   . VAL A 461 ? 0.4174 0.3606 0.5133 0.0431  0.0415  0.0267  461 VAL A CG2   
3734 N  N     . ASP A 462 ? 0.4147 0.3733 0.5168 0.0536  0.0452  0.0306  462 ASP A N     
3735 C  CA    . ASP A 462 ? 0.4174 0.3795 0.522  0.0547  0.0443  0.0307  462 ASP A CA    
3736 C  C     . ASP A 462 ? 0.4172 0.3804 0.5268 0.0481  0.0408  0.0286  462 ASP A C     
3737 O  O     . ASP A 462 ? 0.4118 0.3794 0.5292 0.0431  0.0411  0.0286  462 ASP A O     
3738 C  CB    . ASP A 462 ? 0.4304 0.4027 0.5438 0.0573  0.0485  0.0345  462 ASP A CB    
3739 C  CG    . ASP A 462 ? 0.4899 0.466  0.606  0.0593  0.0477  0.035   462 ASP A CG    
3740 O  OD1   . ASP A 462 ? 0.5015 0.4712 0.6087 0.0629  0.0458  0.0335  462 ASP A OD1   
3741 O  OD2   . ASP A 462 ? 0.5169 0.5022 0.6441 0.0573  0.0488  0.0372  462 ASP A OD2   
3742 N  N     . PRO A 463 ? 0.4197 0.3787 0.5243 0.0482  0.0374  0.0267  463 PRO A N     
3743 C  CA    . PRO A 463 ? 0.4232 0.3826 0.5313 0.0422  0.034   0.0246  463 PRO A CA    
3744 C  C     . PRO A 463 ? 0.431  0.3997 0.5505 0.039   0.0347  0.0258  463 PRO A C     
3745 O  O     . PRO A 463 ? 0.4325 0.4019 0.5553 0.0338  0.0324  0.0242  463 PRO A O     
3746 C  CB    . PRO A 463 ? 0.4296 0.3823 0.5292 0.0441  0.0305  0.023   463 PRO A CB    
3747 C  CG    . PRO A 463 ? 0.437  0.3833 0.5271 0.0502  0.0313  0.0233  463 PRO A CG    
3748 C  CD    . PRO A 463 ? 0.4156 0.3682 0.5104 0.0538  0.0361  0.0262  463 PRO A CD    
3749 N  N     . THR A 464 ? 0.4327 0.4086 0.5584 0.0421  0.0378  0.0288  464 THR A N     
3750 C  CA    . THR A 464 ? 0.4357 0.4205 0.573  0.0392  0.0382  0.0305  464 THR A CA    
3751 C  C     . THR A 464 ? 0.4373 0.4276 0.5825 0.0373  0.0411  0.0325  464 THR A C     
3752 O  O     . THR A 464 ? 0.4351 0.4272 0.5802 0.0411  0.0446  0.035   464 THR A O     
3753 C  CB    . THR A 464 ? 0.4501 0.4394 0.59   0.0433  0.0389  0.0326  464 THR A CB    
3754 O  OG1   . THR A 464 ? 0.4637 0.4478 0.5974 0.0432  0.0351  0.0303  464 THR A OG1   
3755 C  CG2   . THR A 464 ? 0.4478 0.447  0.6006 0.041   0.0397  0.0353  464 THR A CG2   
3756 N  N     . PRO A 465 ? 0.4417 0.4341 0.593  0.0314  0.0396  0.0315  465 PRO A N     
3757 C  CA    . PRO A 465 ? 0.446  0.4429 0.6048 0.0292  0.0418  0.0332  465 PRO A CA    
3758 C  C     . PRO A 465 ? 0.4503 0.4569 0.6204 0.0295  0.0435  0.0371  465 PRO A C     
3759 O  O     . PRO A 465 ? 0.4524 0.4626 0.6252 0.0312  0.043   0.0384  465 PRO A O     
3760 C  CB    . PRO A 465 ? 0.4543 0.4488 0.6143 0.0231  0.039   0.0302  465 PRO A CB    
3761 C  CG    . PRO A 465 ? 0.4605 0.4542 0.6195 0.0215  0.0358  0.0284  465 PRO A CG    
3762 C  CD    . PRO A 465 ? 0.4404 0.4308 0.5918 0.0266  0.0358  0.0286  465 PRO A CD    
3763 N  N     . ASN A 466 ? 0.4486 0.4594 0.6257 0.0277  0.0454  0.0392  466 ASN A N     
3764 C  CA    . ASN A 466 ? 0.4498 0.4698 0.6387 0.0272  0.047   0.0434  466 ASN A CA    
3765 C  C     . ASN A 466 ? 0.4497 0.4728 0.6452 0.0232  0.0433  0.0427  466 ASN A C     
3766 O  O     . ASN A 466 ? 0.4495 0.4782 0.6507 0.0248  0.0433  0.0454  466 ASN A O     
3767 C  CB    . ASN A 466 ? 0.4638 0.4857 0.6577 0.0247  0.0485  0.0448  466 ASN A CB    
3768 C  CG    . ASN A 466 ? 0.4954 0.5263 0.7023 0.0228  0.0493  0.0491  466 ASN A CG    
3769 O  OD1   . ASN A 466 ? 0.5044 0.5364 0.7177 0.0176  0.0468  0.0484  466 ASN A OD1   
3770 N  ND2   . ASN A 466 ? 0.5012 0.5386 0.7124 0.0269  0.0525  0.0536  466 ASN A ND2   
3771 N  N     . HIS A 467 ? 0.4498 0.4684 0.6434 0.0184  0.04    0.0389  467 HIS A N     
3772 C  CA    . HIS A 467 ? 0.4523 0.4719 0.65   0.0144  0.0361  0.0375  467 HIS A CA    
3773 C  C     . HIS A 467 ? 0.4457 0.4578 0.6357 0.0112  0.0333  0.0325  467 HIS A C     
3774 O  O     . HIS A 467 ? 0.4476 0.4548 0.6318 0.011   0.0342  0.0306  467 HIS A O     
3775 C  CB    . HIS A 467 ? 0.4683 0.4942 0.6779 0.0108  0.0353  0.04    467 HIS A CB    
3776 C  CG    . HIS A 467 ? 0.5166 0.5403 0.7274 0.007   0.0349  0.0385  467 HIS A CG    
3777 N  ND1   . HIS A 467 ? 0.5458 0.5702 0.7573 0.0083  0.0381  0.0402  467 HIS A ND1   
3778 C  CD2   . HIS A 467 ? 0.5373 0.5579 0.7485 0.0023  0.0317  0.0353  467 HIS A CD2   
3779 C  CE1   . HIS A 467 ? 0.5544 0.5762 0.767  0.0043  0.0366  0.0381  467 HIS A CE1   
3780 N  NE2   . HIS A 467 ? 0.5534 0.5729 0.7659 0.0007  0.0328  0.0351  467 HIS A NE2   
3781 N  N     . TYR A 468 ? 0.4351 0.4463 0.625  0.0088  0.0299  0.0308  468 TYR A N     
3782 C  CA    . TYR A 468 ? 0.4345 0.4394 0.6174 0.0059  0.0274  0.0265  468 TYR A CA    
3783 C  C     . TYR A 468 ? 0.4317 0.4366 0.6189 0.001   0.0256  0.0249  468 TYR A C     
3784 O  O     . TYR A 468 ? 0.4256 0.4348 0.6208 -0.001  0.0241  0.0264  468 TYR A O     
3785 C  CB    . TYR A 468 ? 0.4331 0.4361 0.6118 0.0064  0.0247  0.0254  468 TYR A CB    
3786 C  CG    . TYR A 468 ? 0.4406 0.4427 0.6142 0.0116  0.0263  0.0266  468 TYR A CG    
3787 C  CD1   . TYR A 468 ? 0.4539 0.4496 0.6178 0.0134  0.0269  0.0247  468 TYR A CD1   
3788 C  CD2   . TYR A 468 ? 0.4494 0.4569 0.628  0.0149  0.0272  0.03    468 TYR A CD2   
3789 C  CE1   . TYR A 468 ? 0.4672 0.4611 0.6257 0.0184  0.028   0.0257  468 TYR A CE1   
3790 C  CE2   . TYR A 468 ? 0.4628 0.4692 0.6364 0.0202  0.0288  0.0311  468 TYR A CE2   
3791 C  CZ    . TYR A 468 ? 0.4779 0.477  0.6409 0.022   0.0291  0.0288  468 TYR A CZ    
3792 O  OH    . TYR A 468 ? 0.5012 0.4981 0.6584 0.0274  0.0303  0.0296  468 TYR A OH    
3793 N  N     . GLN A 469 ? 0.4365 0.4366 0.6189 -0.0008 0.0258  0.022   469 GLN A N     
3794 C  CA    . GLN A 469 ? 0.4476 0.4471 0.6334 -0.0049 0.0245  0.0202  469 GLN A CA    
3795 C  C     . GLN A 469 ? 0.4504 0.4439 0.6289 -0.0072 0.0232  0.016   469 GLN A C     
3796 O  O     . GLN A 469 ? 0.4533 0.4438 0.6251 -0.0063 0.0224  0.0147  469 GLN A O     
3797 C  CB    . GLN A 469 ? 0.4795 0.4814 0.6707 -0.0049 0.0268  0.0221  469 GLN A CB    
3798 C  CG    . GLN A 469 ? 0.5452 0.5463 0.7329 -0.0011 0.0301  0.0236  469 GLN A CG    
3799 C  CD    . GLN A 469 ? 0.6396 0.6343 0.8188 -0.0012 0.0304  0.0206  469 GLN A CD    
3800 O  OE1   . GLN A 469 ? 0.676  0.667  0.8487 -0.0011 0.029   0.0185  469 GLN A OE1   
3801 N  NE2   . GLN A 469 ? 0.6604 0.6538 0.84   -0.0014 0.032   0.0205  469 GLN A NE2   
3802 N  N     . GLU A 470 ? 0.4489 0.441  0.6289 -0.01   0.023   0.014   470 GLU A N     
3803 C  CA    . GLU A 470 ? 0.4618 0.449  0.6359 -0.0121 0.0222  0.0104  470 GLU A CA    
3804 C  C     . GLU A 470 ? 0.466  0.4494 0.6321 -0.0103 0.0233  0.0095  470 GLU A C     
3805 O  O     . GLU A 470 ? 0.4686 0.4489 0.6293 -0.0114 0.022   0.0074  470 GLU A O     
3806 C  CB    . GLU A 470 ? 0.4982 0.4847 0.6755 -0.0142 0.0228  0.009   470 GLU A CB    
3807 C  CG    . GLU A 470 ? 0.5882 0.5709 0.7612 -0.0166 0.0216  0.0053  470 GLU A CG    
3808 C  CD    . GLU A 470 ? 0.7163 0.6962 0.8871 -0.017  0.0234  0.0036  470 GLU A CD    
3809 O  OE1   . GLU A 470 ? 0.7476 0.7269 0.9211 -0.0189 0.023   0.0019  470 GLU A OE1   
3810 O  OE2   . GLU A 470 ? 0.7447 0.7228 0.9111 -0.0154 0.0248  0.0039  470 GLU A OE2   
3811 N  N     . ASN A 471 ? 0.4648 0.4478 0.6299 -0.0076 0.0255  0.0112  471 ASN A N     
3812 C  CA    . ASN A 471 ? 0.4723 0.451  0.6298 -0.0058 0.026   0.0106  471 ASN A CA    
3813 C  C     . ASN A 471 ? 0.4779 0.4552 0.6303 -0.0046 0.0245  0.0106  471 ASN A C     
3814 O  O     . ASN A 471 ? 0.4844 0.4577 0.6307 -0.0052 0.0235  0.009   471 ASN A O     
3815 C  CB    . ASN A 471 ? 0.4836 0.462  0.6406 -0.0027 0.0282  0.0127  471 ASN A CB    
3816 C  CG    . ASN A 471 ? 0.5206 0.4984 0.6802 -0.0039 0.0296  0.0124  471 ASN A CG    
3817 O  OD1   . ASN A 471 ? 0.5262 0.5074 0.6916 -0.0035 0.0309  0.0143  471 ASN A OD1   
3818 N  ND2   . ASN A 471 ? 0.5333 0.5072 0.6891 -0.0054 0.0292  0.0102  471 ASN A ND2   
3819 N  N     . ASP A 472 ? 0.4759 0.4568 0.6315 -0.0029 0.0241  0.0126  472 ASP A N     
3820 C  CA    . ASP A 472 ? 0.4848 0.4648 0.6363 -0.0015 0.0225  0.0128  472 ASP A CA    
3821 C  C     . ASP A 472 ? 0.488  0.4668 0.6379 -0.0047 0.0198  0.0107  472 ASP A C     
3822 O  O     . ASP A 472 ? 0.4887 0.4642 0.6323 -0.0045 0.0183  0.0098  472 ASP A O     
3823 C  CB    . ASP A 472 ? 0.503  0.4877 0.6594 0.0015  0.0231  0.0158  472 ASP A CB    
3824 C  CG    . ASP A 472 ? 0.5601 0.5454 0.7167 0.005   0.026   0.0179  472 ASP A CG    
3825 O  OD1   . ASP A 472 ? 0.572  0.5527 0.7214 0.0073  0.0265  0.0174  472 ASP A OD1   
3826 O  OD2   . ASP A 472 ? 0.5893 0.5794 0.753  0.0053  0.0277  0.0201  472 ASP A OD2   
3827 N  N     . VAL A 473 ? 0.487  0.468  0.6419 -0.0077 0.0191  0.0098  473 VAL A N     
3828 C  CA    . VAL A 473 ? 0.4919 0.4713 0.6446 -0.0107 0.0167  0.0075  473 VAL A CA    
3829 C  C     . VAL A 473 ? 0.4962 0.471  0.6422 -0.012  0.0171  0.0052  473 VAL A C     
3830 O  O     . VAL A 473 ? 0.5011 0.4733 0.6414 -0.0127 0.0156  0.0042  473 VAL A O     
3831 C  CB    . VAL A 473 ? 0.4973 0.4789 0.6562 -0.0133 0.0157  0.0069  473 VAL A CB    
3832 C  CG1   . VAL A 473 ? 0.507  0.486  0.6621 -0.0162 0.0133  0.0043  473 VAL A CG1   
3833 C  CG2   . VAL A 473 ? 0.4975 0.484  0.6639 -0.0124 0.0149  0.0097  473 VAL A CG2   
3834 N  N     . ASP A 474 ? 0.4944 0.4684 0.6411 -0.0121 0.0192  0.0048  474 ASP A N     
3835 C  CA    . ASP A 474 ? 0.5007 0.471  0.6424 -0.0132 0.0198  0.0031  474 ASP A CA    
3836 C  C     . ASP A 474 ? 0.4955 0.4626 0.6306 -0.0115 0.0193  0.0038  474 ASP A C     
3837 O  O     . ASP A 474 ? 0.4998 0.4642 0.6299 -0.013  0.0184  0.0026  474 ASP A O     
3838 C  CB    . ASP A 474 ? 0.5287 0.4992 0.6735 -0.0132 0.022   0.003   474 ASP A CB    
3839 C  CG    . ASP A 474 ? 0.6075 0.5749 0.7486 -0.0145 0.0226  0.0014  474 ASP A CG    
3840 O  OD1   . ASP A 474 ? 0.6234 0.5904 0.7634 -0.0168 0.0222  -0.0005 474 ASP A OD1   
3841 O  OD2   . ASP A 474 ? 0.6401 0.6053 0.779  -0.0132 0.0234  0.0023  474 ASP A OD2   
3842 N  N     . THR A 475 ? 0.4842 0.4513 0.619  -0.0084 0.0197  0.0058  475 THR A N     
3843 C  CA    . THR A 475 ? 0.4814 0.4447 0.6097 -0.0063 0.0188  0.0065  475 THR A CA    
3844 C  C     . THR A 475 ? 0.4766 0.4389 0.6012 -0.0071 0.0163  0.0061  475 THR A C     
3845 O  O     . THR A 475 ? 0.4793 0.4379 0.5981 -0.0079 0.015   0.0056  475 THR A O     
3846 C  CB    . THR A 475 ? 0.4925 0.4563 0.6214 -0.0023 0.0198  0.0086  475 THR A CB    
3847 O  OG1   . THR A 475 ? 0.5061 0.4698 0.6371 -0.0018 0.0219  0.009   475 THR A OG1   
3848 C  CG2   . THR A 475 ? 0.4983 0.4576 0.62   0.0003  0.0183  0.0093  475 THR A CG2   
3849 N  N     . VAL A 476 ? 0.468  0.4338 0.5963 -0.007  0.0154  0.0066  476 VAL A N     
3850 C  CA    . VAL A 476 ? 0.4702 0.4352 0.5955 -0.0078 0.0129  0.0063  476 VAL A CA    
3851 C  C     . VAL A 476 ? 0.4732 0.4363 0.5953 -0.0114 0.0119  0.0042  476 VAL A C     
3852 O  O     . VAL A 476 ? 0.4835 0.4436 0.5997 -0.0121 0.0103  0.0039  476 VAL A O     
3853 C  CB    . VAL A 476 ? 0.4751 0.4444 0.606  -0.0069 0.012   0.0075  476 VAL A CB    
3854 C  CG1   . VAL A 476 ? 0.4846 0.4531 0.6129 -0.0083 0.009   0.007   476 VAL A CG1   
3855 C  CG2   . VAL A 476 ? 0.4805 0.4514 0.6131 -0.0027 0.013   0.0099  476 VAL A CG2   
3856 N  N     . ILE A 477 ? 0.4623 0.4271 0.5879 -0.0136 0.0131  0.0028  477 ILE A N     
3857 C  CA    . ILE A 477 ? 0.4639 0.4271 0.5863 -0.0167 0.0127  0.0007  477 ILE A CA    
3858 C  C     . ILE A 477 ? 0.4718 0.4317 0.5889 -0.0172 0.0135  0.0005  477 ILE A C     
3859 O  O     . ILE A 477 ? 0.4785 0.4364 0.5905 -0.0187 0.0124  0       477 ILE A O     
3860 C  CB    . ILE A 477 ? 0.4647 0.43   0.592  -0.0183 0.0139  -0.0008 477 ILE A CB    
3861 C  CG1   . ILE A 477 ? 0.4766 0.4443 0.6082 -0.0187 0.012   -0.0006 477 ILE A CG1   
3862 C  CG2   . ILE A 477 ? 0.4719 0.4353 0.5957 -0.0207 0.0145  -0.003  477 ILE A CG2   
3863 C  CD1   . ILE A 477 ? 0.4965 0.4627 0.6239 -0.0199 0.0093  -0.0013 477 ILE A CD1   
3864 N  N     . TYR A 478 ? 0.4662 0.4257 0.5847 -0.0159 0.0152  0.0012  478 TYR A N     
3865 C  CA    . TYR A 478 ? 0.4666 0.4231 0.5812 -0.0164 0.0156  0.0015  478 TYR A CA    
3866 C  C     . TYR A 478 ? 0.471  0.4242 0.5797 -0.0155 0.0133  0.0027  478 TYR A C     
3867 O  O     . TYR A 478 ? 0.4743 0.4254 0.5789 -0.0173 0.0126  0.0027  478 TYR A O     
3868 C  CB    . TYR A 478 ? 0.4662 0.4225 0.5837 -0.0151 0.0173  0.0021  478 TYR A CB    
3869 C  CG    . TYR A 478 ? 0.4822 0.4355 0.5968 -0.016  0.0176  0.0024  478 TYR A CG    
3870 C  CD1   . TYR A 478 ? 0.4947 0.4489 0.6108 -0.0183 0.0191  0.0013  478 TYR A CD1   
3871 C  CD2   . TYR A 478 ? 0.4986 0.4482 0.6092 -0.0144 0.0161  0.004   478 TYR A CD2   
3872 C  CE1   . TYR A 478 ? 0.5093 0.4614 0.6238 -0.0192 0.0193  0.002   478 TYR A CE1   
3873 C  CE2   . TYR A 478 ? 0.5134 0.4602 0.6219 -0.0155 0.0158  0.0046  478 TYR A CE2   
3874 C  CZ    . TYR A 478 ? 0.5259 0.4743 0.6368 -0.018  0.0175  0.0037  478 TYR A CZ    
3875 O  OH    . TYR A 478 ? 0.5496 0.4957 0.6594 -0.0192 0.0171  0.0048  478 TYR A OH    
3876 N  N     . SER A 479 ? 0.4692 0.4221 0.5777 -0.0127 0.0122  0.004   479 SER A N     
3877 C  CA    . SER A 479 ? 0.4761 0.4254 0.5789 -0.0114 0.0097  0.0051  479 SER A CA    
3878 C  C     . SER A 479 ? 0.4791 0.4278 0.5784 -0.0135 0.0076  0.0046  479 SER A C     
3879 O  O     . SER A 479 ? 0.4856 0.4308 0.5795 -0.0144 0.0059  0.0052  479 SER A O     
3880 C  CB    . SER A 479 ? 0.4941 0.4437 0.5977 -0.0076 0.0092  0.0063  479 SER A CB    
3881 O  OG    . SER A 479 ? 0.5268 0.4765 0.6327 -0.0054 0.0111  0.0069  479 SER A OG    
3882 N  N     . ILE A 480 ? 0.4743 0.4261 0.5764 -0.0145 0.0075  0.0037  480 ILE A N     
3883 C  CA    . ILE A 480 ? 0.4793 0.4304 0.5778 -0.0165 0.0054  0.0032  480 ILE A CA    
3884 C  C     . ILE A 480 ? 0.4915 0.4412 0.5864 -0.0196 0.0061  0.0023  480 ILE A C     
3885 O  O     . ILE A 480 ? 0.494  0.441  0.5835 -0.0208 0.0044  0.0029  480 ILE A O     
3886 C  CB    . ILE A 480 ? 0.4766 0.4309 0.5793 -0.0167 0.0048  0.0025  480 ILE A CB    
3887 C  CG1   . ILE A 480 ? 0.4846 0.4403 0.5902 -0.0136 0.0037  0.0041  480 ILE A CG1   
3888 C  CG2   . ILE A 480 ? 0.4812 0.4345 0.5801 -0.0194 0.0029  0.0015  480 ILE A CG2   
3889 C  CD1   . ILE A 480 ? 0.4969 0.4567 0.6088 -0.0137 0.0035  0.004   480 ILE A CD1   
3890 N  N     . PHE A 481 ? 0.4986 0.4503 0.5967 -0.0209 0.0086  0.001   481 PHE A N     
3891 C  CA    . PHE A 481 ? 0.5112 0.4625 0.6066 -0.0235 0.0099  0.0001  481 PHE A CA    
3892 C  C     . PHE A 481 ? 0.5284 0.478  0.6221 -0.024  0.0108  0.0012  481 PHE A C     
3893 O  O     . PHE A 481 ? 0.5287 0.4777 0.6192 -0.0261 0.0114  0.0013  481 PHE A O     
3894 C  CB    . PHE A 481 ? 0.504  0.4578 0.6033 -0.0244 0.012   -0.002  481 PHE A CB    
3895 C  CG    . PHE A 481 ? 0.5074 0.462  0.6069 -0.0248 0.0103  -0.0032 481 PHE A CG    
3896 C  CD1   . PHE A 481 ? 0.5171 0.47   0.6109 -0.0265 0.0088  -0.0038 481 PHE A CD1   
3897 C  CD2   . PHE A 481 ? 0.5125 0.4692 0.6176 -0.0236 0.0098  -0.0032 481 PHE A CD2   
3898 C  CE1   . PHE A 481 ? 0.523  0.476  0.6167 -0.0269 0.0067  -0.0048 481 PHE A CE1   
3899 C  CE2   . PHE A 481 ? 0.5198 0.477  0.6254 -0.0242 0.0076  -0.004  481 PHE A CE2   
3900 C  CZ    . PHE A 481 ? 0.5183 0.4733 0.618  -0.0258 0.0059  -0.0048 481 PHE A CZ    
3901 N  N     . LYS A 482 ? 0.5427 0.4913 0.6383 -0.0222 0.0109  0.0024  482 LYS A N     
3902 C  CA    . LYS A 482 ? 0.5656 0.5122 0.66   -0.0227 0.0112  0.0037  482 LYS A CA    
3903 C  C     . LYS A 482 ? 0.5889 0.5314 0.6783 -0.022  0.0082  0.0056  482 LYS A C     
3904 O  O     . LYS A 482 ? 0.5877 0.5281 0.6748 -0.0235 0.0076  0.007   482 LYS A O     
3905 C  CB    . LYS A 482 ? 0.5894 0.5367 0.6885 -0.0214 0.0131  0.0036  482 LYS A CB    
3906 C  CG    . LYS A 482 ? 0.6514 0.6002 0.7531 -0.0233 0.0155  0.0032  482 LYS A CG    
3907 C  CD    . LYS A 482 ? 0.709  0.6611 0.8126 -0.0248 0.0176  0.0011  482 LYS A CD    
3908 C  CE    . LYS A 482 ? 0.7531 0.7065 0.8585 -0.0264 0.02    0.0009  482 LYS A CE    
3909 N  NZ    . LYS A 482 ? 0.7756 0.7316 0.8818 -0.0274 0.022   -0.0014 482 LYS A NZ    
3910 N  N     . TYR A 483 ? 0.606  0.5472 0.694  -0.0197 0.0061  0.0059  483 TYR A N     
3911 C  CA    . TYR A 483 ? 0.6293 0.5658 0.7122 -0.0185 0.0029  0.0076  483 TYR A CA    
3912 C  C     . TYR A 483 ? 0.6462 0.5815 0.7251 -0.0187 0.0002  0.0079  483 TYR A C     
3913 O  O     . TYR A 483 ? 0.6537 0.5855 0.7278 -0.0197 -0.0023 0.0093  483 TYR A O     
3914 C  CB    . TYR A 483 ? 0.6343 0.5689 0.718  -0.0148 0.0025  0.0081  483 TYR A CB    
3915 C  CG    . TYR A 483 ? 0.6494 0.5839 0.7358 -0.0148 0.0044  0.0082  483 TYR A CG    
3916 C  CD1   . TYR A 483 ? 0.6665 0.5986 0.7514 -0.0169 0.0038  0.0093  483 TYR A CD1   
3917 C  CD2   . TYR A 483 ? 0.6611 0.5983 0.7523 -0.013  0.0068  0.0075  483 TYR A CD2   
3918 C  CE1   . TYR A 483 ? 0.68   0.6122 0.768  -0.0171 0.0054  0.0094  483 TYR A CE1   
3919 C  CE2   . TYR A 483 ? 0.6739 0.6109 0.7678 -0.0131 0.0085  0.0075  483 TYR A CE2   
3920 C  CZ    . TYR A 483 ? 0.6902 0.6247 0.7825 -0.0152 0.0077  0.0084  483 TYR A CZ    
3921 O  OH    . TYR A 483 ? 0.7118 0.646  0.8069 -0.0155 0.009   0.0086  483 TYR A OH    
3922 N  N     . ILE A 484 ? 0.6503 0.5883 0.7313 -0.0178 0.0003  0.0069  484 ILE A N     
3923 C  CA    . ILE A 484 ? 0.6654 0.6021 0.7428 -0.0178 -0.0026 0.0072  484 ILE A CA    
3924 C  C     . ILE A 484 ? 0.6744 0.6113 0.7486 -0.0214 -0.0029 0.0068  484 ILE A C     
3925 O  O     . ILE A 484 ? 0.6814 0.6151 0.7504 -0.0225 -0.0054 0.0081  484 ILE A O     
3926 C  CB    . ILE A 484 ? 0.6747 0.6143 0.7559 -0.0155 -0.0027 0.0066  484 ILE A CB    
3927 C  CG1   . ILE A 484 ? 0.6902 0.6293 0.7735 -0.0115 -0.0023 0.0074  484 ILE A CG1   
3928 C  CG2   . ILE A 484 ? 0.683  0.6213 0.7609 -0.0157 -0.0059 0.007   484 ILE A CG2   
3929 C  CD1   . ILE A 484 ? 0.7053 0.6485 0.794  -0.0092 -0.0016 0.0073  484 ILE A CD1   
3930 N  N     . VAL A 485 ? 0.6737 0.614  0.7506 -0.0231 -0.0005 0.0052  485 VAL A N     
3931 C  CA    . VAL A 485 ? 0.685  0.6255 0.7584 -0.0261 -0.0004 0.0047  485 VAL A CA    
3932 C  C     . VAL A 485 ? 0.6973 0.637  0.7683 -0.0283 0.001   0.0057  485 VAL A C     
3933 O  O     . VAL A 485 ? 0.6947 0.6362 0.7691 -0.0286 0.0039  0.0053  485 VAL A O     
3934 C  CB    . VAL A 485 ? 0.692  0.6357 0.7687 -0.0267 0.0015  0.0024  485 VAL A CB    
3935 C  CG1   . VAL A 485 ? 0.7026 0.6461 0.7748 -0.0294 0.0019  0.0016  485 VAL A CG1   
3936 C  CG2   . VAL A 485 ? 0.6946 0.6394 0.7742 -0.0249 -0.0004 0.002   485 VAL A CG2   
3937 N  N     . PRO A 486 ? 0.7085 0.6455 0.7739 -0.0299 -0.0011 0.0073  486 PRO A N     
3938 C  CA    . PRO A 486 ? 0.7139 0.6505 0.7775 -0.0322 0.0001  0.0089  486 PRO A CA    
3939 C  C     . PRO A 486 ? 0.7201 0.6593 0.7822 -0.0345 0.0029  0.008   486 PRO A C     
3940 O  O     . PRO A 486 ? 0.7249 0.663  0.782  -0.0366 0.0022  0.0093  486 PRO A O     
3941 C  CB    . PRO A 486 ? 0.7262 0.6587 0.7846 -0.0328 -0.0037 0.0113  486 PRO A CB    
3942 C  CG    . PRO A 486 ? 0.7323 0.6635 0.7884 -0.0316 -0.0065 0.0105  486 PRO A CG    
3943 C  CD    . PRO A 486 ? 0.708  0.6423 0.7689 -0.0298 -0.0049 0.008   486 PRO A CD    
3944 N  N     . ASN A 494 ? 0.7928 0.7371 0.8722 -0.0374 0.0112  0.0144  494 ASN A N     
3945 C  CA    . ASN A 494 ? 0.7995 0.7469 0.8825 -0.0391 0.014   0.016   494 ASN A CA    
3946 C  C     . ASN A 494 ? 0.7978 0.7494 0.8859 -0.0382 0.0184  0.0134  494 ASN A C     
3947 O  O     . ASN A 494 ? 0.7968 0.7497 0.89   -0.0384 0.0197  0.0144  494 ASN A O     
3948 C  CB    . ASN A 494 ? 0.8194 0.768  0.899  -0.0418 0.0145  0.0184  494 ASN A CB    
3949 C  CG    . ASN A 494 ? 0.8665 0.8123 0.9451 -0.0436 0.0111  0.0225  494 ASN A CG    
3950 O  OD1   . ASN A 494 ? 0.8851 0.8261 0.9617 -0.0427 0.0069  0.0231  494 ASN A OD1   
3951 N  ND2   . ASN A 494 ? 0.8734 0.822  0.9535 -0.046  0.0128  0.0255  494 ASN A ND2   
3952 N  N     . PRO A 495 ? 0.7924 0.7457 0.8793 -0.0374 0.0205  0.0103  495 PRO A N     
3953 C  CA    . PRO A 495 ? 0.7861 0.7428 0.8777 -0.0366 0.0242  0.008   495 PRO A CA    
3954 C  C     . PRO A 495 ? 0.7841 0.7401 0.8804 -0.0346 0.0237  0.0065  495 PRO A C     
3955 O  O     . PRO A 495 ? 0.7855 0.7392 0.8806 -0.0332 0.0213  0.0057  495 PRO A O     
3956 C  CB    . PRO A 495 ? 0.794  0.7517 0.8816 -0.0364 0.0257  0.0054  495 PRO A CB    
3957 C  CG    . PRO A 495 ? 0.8018 0.7564 0.8844 -0.0364 0.0221  0.0055  495 PRO A CG    
3958 C  CD    . PRO A 495 ? 0.7856 0.7377 0.8669 -0.0372 0.0191  0.0088  495 PRO A CD    
3959 N  N     . PRO A 496 ? 0.7774 0.7356 0.8793 -0.0343 0.0262  0.0062  496 PRO A N     
3960 C  CA    . PRO A 496 ? 0.7723 0.7298 0.8787 -0.0325 0.0258  0.0049  496 PRO A CA    
3961 C  C     . PRO A 496 ? 0.7652 0.7238 0.8726 -0.0312 0.0269  0.0016  496 PRO A C     
3962 O  O     . PRO A 496 ? 0.7682 0.7257 0.8774 -0.0296 0.0256  0.0009  496 PRO A O     
3963 C  CB    . PRO A 496 ? 0.7784 0.738  0.8905 -0.033  0.0279  0.0059  496 PRO A CB    
3964 C  CG    . PRO A 496 ? 0.784  0.7454 0.8948 -0.035  0.0292  0.0082  496 PRO A CG    
3965 C  CD    . PRO A 496 ? 0.7679 0.7295 0.8727 -0.0355 0.0294  0.0072  496 PRO A CD    
3966 N  N     . GLY A 497 ? 0.7526 0.7132 0.8585 -0.0316 0.0291  -0.0002 497 GLY A N     
3967 C  CA    . GLY A 497 ? 0.7451 0.7061 0.8516 -0.0306 0.0297  -0.0034 497 GLY A CA    
3968 C  C     . GLY A 497 ? 0.7315 0.694  0.8444 -0.0296 0.0315  -0.0047 497 GLY A C     
3969 O  O     . GLY A 497 ? 0.7305 0.6945 0.8466 -0.03   0.0334  -0.0038 497 GLY A O     
3970 N  N     . GLY A 498 ? 0.7213 0.6834 0.8365 -0.0285 0.0307  -0.0064 498 GLY A N     
3971 C  CA    . GLY A 498 ? 0.7183 0.6816 0.8396 -0.0277 0.032   -0.0075 498 GLY A CA    
3972 C  C     . GLY A 498 ? 0.7168 0.6794 0.8413 -0.0265 0.0303  -0.0076 498 GLY A C     
3973 O  O     . GLY A 498 ? 0.7211 0.6827 0.8435 -0.0261 0.0282  -0.007  498 GLY A O     
3974 N  N     . ASP A 499 ? 0.7102 0.6736 0.8403 -0.0259 0.0315  -0.0081 499 ASP A N     
3975 C  CA    . ASP A 499 ? 0.7111 0.6744 0.8452 -0.0248 0.0305  -0.008  499 ASP A CA    
3976 C  C     . ASP A 499 ? 0.703  0.6674 0.8427 -0.0246 0.0322  -0.0095 499 ASP A C     
3977 O  O     . ASP A 499 ? 0.7056 0.6708 0.8453 -0.0251 0.0339  -0.0111 499 ASP A O     
3978 C  CB    . ASP A 499 ? 0.7394 0.7013 0.8731 -0.0238 0.0292  -0.0054 499 ASP A CB    
3979 C  CG    . ASP A 499 ? 0.8093 0.7703 0.9442 -0.024  0.0298  -0.0039 499 ASP A CG    
3980 O  OD1   . ASP A 499 ? 0.8178 0.7801 0.9554 -0.0247 0.0316  -0.0047 499 ASP A OD1   
3981 O  OD2   . ASP A 499 ? 0.8461 0.805  0.9795 -0.0232 0.0283  -0.0019 499 ASP A OD2   
3982 N  N     . TRP A 500 ? 0.6901 0.6545 0.8342 -0.0237 0.0318  -0.0088 500 TRP A N     
3983 C  CA    . TRP A 500 ? 0.6824 0.6475 0.8318 -0.0236 0.0331  -0.01   500 TRP A CA    
3984 C  C     . TRP A 500 ? 0.6717 0.6368 0.8227 -0.0238 0.0347  -0.0095 500 TRP A C     
3985 O  O     . TRP A 500 ? 0.6736 0.6396 0.8284 -0.0238 0.036   -0.011  500 TRP A O     
3986 C  CB    . TRP A 500 ? 0.6807 0.6458 0.8342 -0.0227 0.0322  -0.009  500 TRP A CB    
3987 N  N     . SER A 501 ? 0.6578 0.6221 0.8064 -0.024  0.0343  -0.0073 501 SER A N     
3988 C  CA    . SER A 501 ? 0.6465 0.6109 0.7971 -0.0245 0.0353  -0.0062 501 SER A CA    
3989 C  C     . SER A 501 ? 0.6301 0.5963 0.7795 -0.0254 0.0373  -0.0068 501 SER A C     
3990 O  O     . SER A 501 ? 0.6283 0.5956 0.7809 -0.0258 0.0386  -0.0061 501 SER A O     
3991 C  CB    . SER A 501 ? 0.6638 0.626  0.8125 -0.0244 0.0335  -0.0033 501 SER A CB    
3992 O  OG    . SER A 501 ? 0.6921 0.6536 0.8356 -0.025  0.0326  -0.0023 501 SER A OG    
3993 N  N     . GLY A 502 ? 0.6161 0.5827 0.7609 -0.0258 0.0374  -0.0079 502 GLY A N     
3994 C  CA    . GLY A 502 ? 0.6076 0.5759 0.7503 -0.0264 0.0395  -0.0084 502 GLY A CA    
3995 C  C     . GLY A 502 ? 0.5972 0.5651 0.7335 -0.027  0.0388  -0.0086 502 GLY A C     
3996 O  O     . GLY A 502 ? 0.5981 0.5643 0.7315 -0.0271 0.0365  -0.0078 502 GLY A O     
3997 N  N     . LEU A 503 ? 0.5855 0.5548 0.7191 -0.0272 0.041   -0.0098 503 LEU A N     
3998 C  CA    . LEU A 503 ? 0.5807 0.5493 0.7075 -0.0278 0.0406  -0.01   503 LEU A CA    
3999 C  C     . LEU A 503 ? 0.578  0.5484 0.7027 -0.0289 0.0422  -0.0076 503 LEU A C     
4000 O  O     . LEU A 503 ? 0.5762 0.549  0.703  -0.0287 0.0452  -0.0077 503 LEU A O     
4001 C  CB    . LEU A 503 ? 0.5777 0.5459 0.7017 -0.0271 0.0415  -0.0135 503 LEU A CB    
4002 C  CG    . LEU A 503 ? 0.5936 0.5609 0.71   -0.0276 0.0413  -0.0139 503 LEU A CG    
4003 C  CD1   . LEU A 503 ? 0.6042 0.5695 0.7173 -0.0283 0.0379  -0.0128 503 LEU A CD1   
4004 C  CD2   . LEU A 503 ? 0.5999 0.5662 0.7133 -0.0266 0.0424  -0.0175 503 LEU A CD2   
4005 N  N     . SER A 504 ? 0.5746 0.5437 0.6952 -0.03   0.0402  -0.0054 504 SER A N     
4006 C  CA    . SER A 504 ? 0.5742 0.5447 0.6925 -0.0313 0.0412  -0.0028 504 SER A CA    
4007 C  C     . SER A 504 ? 0.5779 0.5476 0.6886 -0.0318 0.0411  -0.0035 504 SER A C     
4008 O  O     . SER A 504 ? 0.5826 0.5498 0.6897 -0.0317 0.0384  -0.0044 504 SER A O     
4009 C  CB    . SER A 504 ? 0.5876 0.5567 0.7067 -0.0324 0.0385  0.0007  504 SER A CB    
4010 O  OG    . SER A 504 ? 0.6104 0.5798 0.736  -0.0321 0.0384  0.0016  504 SER A OG    
4011 N  N     . ILE A 505 ? 0.5728 0.5449 0.6813 -0.0323 0.0441  -0.0028 505 ILE A N     
4012 C  CA    . ILE A 505 ? 0.5787 0.5501 0.6794 -0.0328 0.0444  -0.0031 505 ILE A CA    
4013 C  C     . ILE A 505 ? 0.5856 0.5591 0.6854 -0.0346 0.0454  0.001   505 ILE A C     
4014 O  O     . ILE A 505 ? 0.5808 0.5578 0.6851 -0.0346 0.0484  0.0026  505 ILE A O     
4015 C  CB    . ILE A 505 ? 0.5808 0.5529 0.6787 -0.0313 0.0475  -0.0064 505 ILE A CB    
4016 C  CG1   . ILE A 505 ? 0.5934 0.5632 0.6929 -0.0298 0.0461  -0.0103 505 ILE A CG1   
4017 C  CG2   . ILE A 505 ? 0.5869 0.558  0.6761 -0.0319 0.0479  -0.0064 505 ILE A CG2   
4018 C  CD1   . ILE A 505 ? 0.6117 0.5807 0.7074 -0.0282 0.0482  -0.0141 505 ILE A CD1   
4019 N  N     . ILE A 506 ? 0.5942 0.5657 0.6888 -0.0361 0.0427  0.003   506 ILE A N     
4020 C  CA    . ILE A 506 ? 0.6054 0.5787 0.6992 -0.038  0.0431  0.0073  506 ILE A CA    
4021 C  C     . ILE A 506 ? 0.6143 0.5878 0.7003 -0.0387 0.0446  0.0076  506 ILE A C     
4022 O  O     . ILE A 506 ? 0.6187 0.5896 0.6986 -0.038  0.0436  0.0048  506 ILE A O     
4023 C  CB    . ILE A 506 ? 0.6162 0.5867 0.7109 -0.0395 0.0386  0.0103  506 ILE A CB    
4024 C  CG1   . ILE A 506 ? 0.6362 0.6025 0.7242 -0.0396 0.0348  0.0094  506 ILE A CG1   
4025 C  CG2   . ILE A 506 ? 0.6202 0.5899 0.7216 -0.0387 0.0372  0.0101  506 ILE A CG2   
4026 C  CD1   . ILE A 506 ? 0.6563 0.6202 0.7425 -0.0413 0.031   0.013   506 ILE A CD1   
4027 N  N     . ASP A 507 ? 0.6134 0.5902 0.6996 -0.0402 0.0468  0.0114  507 ASP A N     
4028 C  CA    . ASP A 507 ? 0.6226 0.5998 0.7012 -0.0411 0.0481  0.0127  507 ASP A CA    
4029 C  C     . ASP A 507 ? 0.6278 0.6054 0.7068 -0.044  0.0459  0.0182  507 ASP A C     
4030 O  O     . ASP A 507 ? 0.6291 0.6042 0.7113 -0.0449 0.0418  0.0196  507 ASP A O     
4031 C  CB    . ASP A 507 ? 0.6387 0.6195 0.7155 -0.0396 0.0539  0.0114  507 ASP A CB    
4032 C  CG    . ASP A 507 ? 0.6821 0.6686 0.7665 -0.0395 0.0581  0.0141  507 ASP A CG    
4033 O  OD1   . ASP A 507 ? 0.6861 0.6738 0.7771 -0.0412 0.0562  0.0175  507 ASP A OD1   
4034 O  OD2   . ASP A 507 ? 0.7077 0.6974 0.7914 -0.0377 0.063   0.0128  507 ASP A OD2   
4035 N  N     . ASN A 508 ? 0.6273 0.6076 0.7029 -0.0454 0.0484  0.0213  508 ASN A N     
4036 C  CA    . ASN A 508 ? 0.6329 0.6133 0.709  -0.0484 0.0459  0.0268  508 ASN A CA    
4037 C  C     . ASN A 508 ? 0.6287 0.6136 0.7143 -0.0496 0.0473  0.0309  508 ASN A C     
4038 O  O     . ASN A 508 ? 0.6288 0.6132 0.7163 -0.0521 0.0443  0.0354  508 ASN A O     
4039 C  CB    . ASN A 508 ? 0.6498 0.6308 0.7179 -0.0497 0.0471  0.0289  508 ASN A CB    
4040 C  CG    . ASN A 508 ? 0.6902 0.6654 0.7508 -0.0507 0.0421  0.0284  508 ASN A CG    
4041 O  OD1   . ASN A 508 ? 0.7044 0.6792 0.7602 -0.0529 0.041   0.0318  508 ASN A OD1   
4042 N  ND2   . ASN A 508 ? 0.6986 0.6695 0.7582 -0.0492 0.0388  0.0244  508 ASN A ND2   
4043 N  N     . VAL A 509 ? 0.621  0.6098 0.7126 -0.0477 0.0514  0.0293  509 VAL A N     
4044 C  CA    . VAL A 509 ? 0.6198 0.613  0.721  -0.0488 0.0527  0.0332  509 VAL A CA    
4045 C  C     . VAL A 509 ? 0.6236 0.6164 0.7321 -0.0471 0.0522  0.0306  509 VAL A C     
4046 O  O     . VAL A 509 ? 0.6227 0.6155 0.738  -0.0484 0.0498  0.0336  509 VAL A O     
4047 C  CB    . VAL A 509 ? 0.6241 0.6244 0.7268 -0.0486 0.059   0.0358  509 VAL A CB    
4048 C  CG1   . VAL A 509 ? 0.6324 0.6339 0.7306 -0.0453 0.064   0.0309  509 VAL A CG1   
4049 C  CG2   . VAL A 509 ? 0.6228 0.6284 0.7368 -0.0495 0.0606  0.0397  509 VAL A CG2   
4050 N  N     . HIS A 510 ? 0.6252 0.6171 0.7323 -0.0442 0.0542  0.0252  510 HIS A N     
4051 C  CA    . HIS A 510 ? 0.6252 0.617  0.739  -0.0425 0.0543  0.0226  510 HIS A CA    
4052 C  C     . HIS A 510 ? 0.615  0.6014 0.7263 -0.041  0.0509  0.0182  510 HIS A C     
4053 O  O     . HIS A 510 ? 0.6174 0.6005 0.7214 -0.0407 0.0494  0.0158  510 HIS A O     
4054 C  CB    . HIS A 510 ? 0.6457 0.6421 0.7621 -0.0401 0.0602  0.0204  510 HIS A CB    
4055 C  CG    . HIS A 510 ? 0.6921 0.6951 0.8131 -0.0408 0.0644  0.0247  510 HIS A CG    
4056 N  ND1   . HIS A 510 ? 0.7215 0.7276 0.8371 -0.0404 0.0687  0.0255  510 HIS A ND1   
4057 C  CD2   . HIS A 510 ? 0.7108 0.7178 0.8415 -0.0417 0.0651  0.0283  510 HIS A CD2   
4058 C  CE1   . HIS A 510 ? 0.7287 0.7411 0.8512 -0.041  0.0721  0.0298  510 HIS A CE1   
4059 N  NE2   . HIS A 510 ? 0.7263 0.7395 0.8583 -0.0419 0.0699  0.0317  510 HIS A NE2   
4060 N  N     . GLU A 511 ? 0.601  0.5869 0.7189 -0.0401 0.05    0.0171  511 GLU A N     
4061 C  CA    . GLU A 511 ? 0.5982 0.5803 0.7158 -0.0385 0.0478  0.0131  511 GLU A CA    
4062 C  C     . GLU A 511 ? 0.5914 0.5763 0.7144 -0.0364 0.0514  0.0105  511 GLU A C     
4063 O  O     . GLU A 511 ? 0.5901 0.578  0.7201 -0.0367 0.0529  0.0125  511 GLU A O     
4064 C  CB    . GLU A 511 ? 0.6187 0.5973 0.7392 -0.0392 0.0431  0.0147  511 GLU A CB    
4065 C  CG    . GLU A 511 ? 0.6646 0.64   0.7855 -0.0374 0.0414  0.011   511 GLU A CG    
4066 C  CD    . GLU A 511 ? 0.7235 0.6951 0.8466 -0.0375 0.0373  0.0123  511 GLU A CD    
4067 O  OE1   . GLU A 511 ? 0.7328 0.7032 0.8561 -0.0392 0.0348  0.016   511 GLU A OE1   
4068 O  OE2   . GLU A 511 ? 0.7433 0.713  0.8678 -0.0359 0.0364  0.0098  511 GLU A OE2   
4069 N  N     . PHE A 512 ? 0.5846 0.5684 0.7043 -0.0345 0.0527  0.006   512 PHE A N     
4070 C  CA    . PHE A 512 ? 0.5794 0.5648 0.7031 -0.0323 0.0557  0.0029  512 PHE A CA    
4071 C  C     . PHE A 512 ? 0.568  0.55   0.694  -0.0315 0.0526  0.0003  512 PHE A C     
4072 O  O     . PHE A 512 ? 0.574  0.5525 0.6955 -0.0317 0.0496  -0.0008 512 PHE A O     
4073 C  CB    . PHE A 512 ? 0.5851 0.5709 0.7026 -0.0307 0.0588  -0.0002 512 PHE A CB    
4074 C  CG    . PHE A 512 ? 0.6019 0.5909 0.7156 -0.0314 0.0619  0.0024  512 PHE A CG    
4075 C  CD1   . PHE A 512 ? 0.6124 0.6065 0.7305 -0.0307 0.0664  0.0041  512 PHE A CD1   
4076 C  CD2   . PHE A 512 ? 0.6193 0.6063 0.7251 -0.0327 0.0603  0.0033  512 PHE A CD2   
4077 C  CE1   . PHE A 512 ? 0.6229 0.6205 0.7376 -0.0313 0.0696  0.0069  512 PHE A CE1   
4078 C  CE2   . PHE A 512 ? 0.6304 0.6203 0.7325 -0.0335 0.0631  0.0061  512 PHE A CE2   
4079 C  CZ    . PHE A 512 ? 0.624  0.6193 0.7305 -0.0327 0.0679  0.0079  512 PHE A CZ    
4080 N  N     . ARG A 513 ? 0.5516 0.5346 0.6847 -0.0305 0.0534  -0.0003 513 ARG A N     
4081 C  CA    . ARG A 513 ? 0.5454 0.5254 0.6809 -0.0298 0.0506  -0.0022 513 ARG A CA    
4082 C  C     . ARG A 513 ? 0.535  0.5157 0.675  -0.028  0.0526  -0.0053 513 ARG A C     
4083 O  O     . ARG A 513 ? 0.5313 0.5151 0.6765 -0.0275 0.0553  -0.0046 513 ARG A O     
4084 C  CB    . ARG A 513 ? 0.5589 0.5374 0.698  -0.0311 0.0476  0.001   513 ARG A CB    
4085 C  CG    . ARG A 513 ? 0.597  0.5722 0.7375 -0.0303 0.0447  -0.0004 513 ARG A CG    
4086 C  CD    . ARG A 513 ? 0.6357 0.6083 0.7767 -0.0313 0.0412  0.0026  513 ARG A CD    
4087 N  NE    . ARG A 513 ? 0.6807 0.6504 0.823  -0.0302 0.039   0.0015  513 ARG A NE    
4088 C  CZ    . ARG A 513 ? 0.7274 0.6947 0.8658 -0.0295 0.0371  0.0001  513 ARG A CZ    
4089 N  NH1   . ARG A 513 ? 0.7273 0.6945 0.8602 -0.0298 0.0369  -0.0005 513 ARG A NH1   
4090 N  NH2   . ARG A 513 ? 0.7348 0.7002 0.8751 -0.0283 0.0356  -0.0005 513 ARG A NH2   
4091 N  N     . TRP A 514 ? 0.5288 0.5068 0.6671 -0.027  0.0511  -0.0085 514 TRP A N     
4092 C  CA    . TRP A 514 ? 0.5272 0.505  0.6694 -0.0253 0.0521  -0.0115 514 TRP A CA    
4093 C  C     . TRP A 514 ? 0.533  0.5091 0.6802 -0.0256 0.0494  -0.0108 514 TRP A C     
4094 O  O     . TRP A 514 ? 0.5347 0.5084 0.6796 -0.026  0.0466  -0.0106 514 TRP A O     
4095 C  CB    . TRP A 514 ? 0.5219 0.4973 0.659  -0.0243 0.0516  -0.0153 514 TRP A CB    
4096 C  CG    . TRP A 514 ? 0.5237 0.5    0.6558 -0.0233 0.0546  -0.0171 514 TRP A CG    
4097 C  CD1   . TRP A 514 ? 0.5341 0.5107 0.6668 -0.0213 0.0572  -0.02   514 TRP A CD1   
4098 C  CD2   . TRP A 514 ? 0.5268 0.5031 0.6515 -0.0239 0.0552  -0.0164 514 TRP A CD2   
4099 N  NE1   . TRP A 514 ? 0.5401 0.5169 0.6659 -0.0204 0.0595  -0.0211 514 TRP A NE1   
4100 C  CE2   . TRP A 514 ? 0.537  0.5137 0.6579 -0.0221 0.0584  -0.0188 514 TRP A CE2   
4101 C  CE3   . TRP A 514 ? 0.5369 0.5127 0.6576 -0.0257 0.0533  -0.0138 514 TRP A CE3   
4102 C  CZ2   . TRP A 514 ? 0.5468 0.5235 0.6597 -0.0222 0.0599  -0.0187 514 TRP A CZ2   
4103 C  CZ3   . TRP A 514 ? 0.5495 0.5254 0.6629 -0.026  0.0546  -0.0135 514 TRP A CZ3   
4104 C  CH2   . TRP A 514 ? 0.5505 0.5269 0.66   -0.0243 0.0579  -0.0159 514 TRP A CH2   
4105 N  N     . LEU A 515 ? 0.5346 0.5121 0.6885 -0.0251 0.0504  -0.0103 515 LEU A N     
4106 C  CA    . LEU A 515 ? 0.5436 0.5193 0.702  -0.0252 0.048   -0.0094 515 LEU A CA    
4107 C  C     . LEU A 515 ? 0.5489 0.5238 0.7108 -0.0239 0.0482  -0.0124 515 LEU A C     
4108 O  O     . LEU A 515 ? 0.5502 0.5259 0.7116 -0.0228 0.0503  -0.015  515 LEU A O     
4109 C  CB    . LEU A 515 ? 0.5465 0.5237 0.7103 -0.0259 0.0483  -0.0063 515 LEU A CB    
4110 C  CG    . LEU A 515 ? 0.5672 0.5452 0.7286 -0.0275 0.0478  -0.0029 515 LEU A CG    
4111 C  CD1   . LEU A 515 ? 0.5731 0.5532 0.7409 -0.0282 0.0483  0.0001  515 LEU A CD1   
4112 C  CD2   . LEU A 515 ? 0.5794 0.5539 0.7366 -0.0282 0.0443  -0.0016 515 LEU A CD2   
4113 N  N     . SER A 516 ? 0.5507 0.5237 0.7157 -0.0239 0.046   -0.012  516 SER A N     
4114 C  CA    . SER A 516 ? 0.5585 0.5304 0.7273 -0.023  0.0456  -0.0142 516 SER A CA    
4115 C  C     . SER A 516 ? 0.5659 0.5367 0.7311 -0.0225 0.0453  -0.0173 516 SER A C     
4116 O  O     . SER A 516 ? 0.5707 0.5415 0.7368 -0.0214 0.0466  -0.02   516 SER A O     
4117 C  CB    . SER A 516 ? 0.5727 0.5463 0.7473 -0.0222 0.0477  -0.0147 516 SER A CB    
4118 O  OG    . SER A 516 ? 0.6004 0.575  0.7786 -0.0229 0.0476  -0.0116 516 SER A OG    
4119 N  N     . LEU A 517 ? 0.5641 0.5337 0.7249 -0.0231 0.0433  -0.0168 517 LEU A N     
4120 C  CA    . LEU A 517 ? 0.5676 0.5358 0.7249 -0.0228 0.0424  -0.0194 517 LEU A CA    
4121 C  C     . LEU A 517 ? 0.5679 0.5347 0.7292 -0.0225 0.0406  -0.0207 517 LEU A C     
4122 O  O     . LEU A 517 ? 0.5669 0.5334 0.7305 -0.0229 0.0389  -0.0189 517 LEU A O     
4123 C  CB    . LEU A 517 ? 0.5695 0.537  0.7215 -0.0236 0.0406  -0.0182 517 LEU A CB    
4124 C  CG    . LEU A 517 ? 0.5843 0.5528 0.7317 -0.0242 0.0417  -0.0166 517 LEU A CG    
4125 C  CD1   . LEU A 517 ? 0.5918 0.5591 0.734  -0.0249 0.0395  -0.0159 517 LEU A CD1   
4126 C  CD2   . LEU A 517 ? 0.5913 0.5608 0.7361 -0.0238 0.0444  -0.0184 517 LEU A CD2   
4127 N  N     . PRO A 518 ? 0.5665 0.5322 0.7281 -0.0218 0.0409  -0.0238 518 PRO A N     
4128 C  CA    . PRO A 518 ? 0.5661 0.5302 0.7316 -0.0218 0.0387  -0.0248 518 PRO A CA    
4129 C  C     . PRO A 518 ? 0.5688 0.532  0.7321 -0.0226 0.0359  -0.0243 518 PRO A C     
4130 O  O     . PRO A 518 ? 0.5719 0.5349 0.7298 -0.0229 0.0356  -0.0243 518 PRO A O     
4131 C  CB    . PRO A 518 ? 0.5732 0.5358 0.7382 -0.0206 0.0395  -0.0284 518 PRO A CB    
4132 C  CG    . PRO A 518 ? 0.579  0.5418 0.7374 -0.0201 0.0414  -0.0295 518 PRO A CG    
4133 C  CD    . PRO A 518 ? 0.5597 0.5253 0.7179 -0.0207 0.0431  -0.0263 518 PRO A CD    
4134 N  N     . ARG A 519 ? 0.5628 0.5256 0.7307 -0.023  0.0339  -0.0235 519 ARG A N     
4135 C  CA    . ARG A 519 ? 0.5616 0.5241 0.7292 -0.0237 0.0313  -0.0225 519 ARG A CA    
4136 C  C     . ARG A 519 ? 0.5539 0.5143 0.7176 -0.024  0.0296  -0.0253 519 ARG A C     
4137 O  O     . ARG A 519 ? 0.5519 0.5122 0.7124 -0.0246 0.028   -0.0247 519 ARG A O     
4138 C  CB    . ARG A 519 ? 0.586  0.5489 0.7601 -0.024  0.0299  -0.021  519 ARG A CB    
4139 C  CG    . ARG A 519 ? 0.6486 0.6123 0.8242 -0.0248 0.0274  -0.0192 519 ARG A CG    
4140 C  CD    . ARG A 519 ? 0.7129 0.6767 0.8953 -0.0252 0.0261  -0.0181 519 ARG A CD    
4141 N  NE    . ARG A 519 ? 0.78   0.7414 0.9642 -0.0253 0.0253  -0.021  519 ARG A NE    
4142 C  CZ    . ARG A 519 ? 0.8278 0.7872 1.0121 -0.0259 0.0226  -0.0228 519 ARG A CZ    
4143 N  NH1   . ARG A 519 ? 0.8258 0.7857 1.0095 -0.0268 0.0203  -0.0217 519 ARG A NH1   
4144 N  NH2   . ARG A 519 ? 0.8301 0.7866 1.0154 -0.0257 0.0219  -0.0256 519 ARG A NH2   
4145 N  N     . VAL A 520 ? 0.551  0.5093 0.7144 -0.0233 0.0299  -0.0283 520 VAL A N     
4146 C  CA    . VAL A 520 ? 0.5564 0.5115 0.7151 -0.0232 0.0282  -0.0314 520 VAL A CA    
4147 C  C     . VAL A 520 ? 0.558  0.5116 0.7132 -0.0216 0.0307  -0.0345 520 VAL A C     
4148 O  O     . VAL A 520 ? 0.5561 0.5109 0.7146 -0.0207 0.0332  -0.0345 520 VAL A O     
4149 C  CB    . VAL A 520 ? 0.5653 0.5181 0.7278 -0.0239 0.0244  -0.0321 520 VAL A CB    
4150 C  CG1   . VAL A 520 ? 0.5722 0.5268 0.7379 -0.0254 0.0219  -0.0289 520 VAL A CG1   
4151 C  CG2   . VAL A 520 ? 0.5681 0.5202 0.7365 -0.0234 0.0247  -0.0328 520 VAL A CG2   
4152 N  N     . SER A 521 ? 0.5582 0.5088 0.7065 -0.021  0.0299  -0.0372 521 SER A N     
4153 C  CA    . SER A 521 ? 0.5637 0.5119 0.7075 -0.0191 0.0319  -0.0407 521 SER A CA    
4154 C  C     . SER A 521 ? 0.5656 0.5084 0.7074 -0.0189 0.028   -0.0438 521 SER A C     
4155 O  O     . SER A 521 ? 0.5669 0.5089 0.7121 -0.0205 0.0241  -0.0427 521 SER A O     
4156 C  CB    . SER A 521 ? 0.5827 0.5317 0.7188 -0.0185 0.0345  -0.0409 521 SER A CB    
4157 O  OG    . SER A 521 ? 0.6112 0.5573 0.7408 -0.0192 0.0317  -0.0418 521 SER A OG    
4158 N  N     . GLU A 522 ? 0.5642 0.5033 0.7009 -0.0168 0.0288  -0.0476 522 GLU A N     
4159 C  CA    . GLU A 522 ? 0.5719 0.5049 0.706  -0.0164 0.0246  -0.0508 522 GLU A CA    
4160 C  C     . GLU A 522 ? 0.572  0.5026 0.7023 -0.0183 0.0202  -0.0503 522 GLU A C     
4161 O  O     . GLU A 522 ? 0.5725 0.5006 0.7063 -0.0197 0.0155  -0.0501 522 GLU A O     
4162 C  CB    . GLU A 522 ? 0.6104 0.5394 0.7376 -0.0133 0.0264  -0.0551 522 GLU A CB    
4163 C  CG    . GLU A 522 ? 0.6877 0.6092 0.8116 -0.0127 0.0216  -0.0587 522 GLU A CG    
4164 C  CD    . GLU A 522 ? 0.7942 0.7122 0.9184 -0.01   0.0224  -0.0621 522 GLU A CD    
4165 O  OE1   . GLU A 522 ? 0.8194 0.7412 0.9465 -0.0083 0.0271  -0.0618 522 GLU A OE1   
4166 O  OE2   . GLU A 522 ? 0.8297 0.741  0.9514 -0.0094 0.018   -0.0651 522 GLU A OE2   
4167 N  N     . ASN A 523 ? 0.5662 0.498  0.6901 -0.0184 0.0217  -0.0496 523 ASN A N     
4168 C  CA    . ASN A 523 ? 0.5654 0.4949 0.6853 -0.0201 0.0177  -0.0491 523 ASN A CA    
4169 C  C     . ASN A 523 ? 0.5558 0.4904 0.6781 -0.0219 0.0182  -0.045  523 ASN A C     
4170 O  O     . ASN A 523 ? 0.559  0.4923 0.6787 -0.0233 0.0149  -0.0442 523 ASN A O     
4171 C  CB    . ASN A 523 ? 0.5826 0.5073 0.691  -0.0185 0.0177  -0.0523 523 ASN A CB    
4172 C  CG    . ASN A 523 ? 0.6172 0.536  0.7221 -0.0163 0.0167  -0.0567 523 ASN A CG    
4173 O  OD1   . ASN A 523 ? 0.6328 0.5512 0.7337 -0.0137 0.0208  -0.0589 523 ASN A OD1   
4174 N  ND2   . ASN A 523 ? 0.6212 0.5352 0.7278 -0.0173 0.0111  -0.0578 523 ASN A ND2   
4175 N  N     . GLY A 524 ? 0.5412 0.481  0.6681 -0.0219 0.0219  -0.0425 524 GLY A N     
4176 C  CA    . GLY A 524 ? 0.5322 0.4761 0.6606 -0.0232 0.0225  -0.0388 524 GLY A CA    
4177 C  C     . GLY A 524 ? 0.5153 0.4632 0.6527 -0.0242 0.0224  -0.0355 524 GLY A C     
4178 O  O     . GLY A 524 ? 0.515  0.4632 0.6584 -0.0239 0.0228  -0.0357 524 GLY A O     
4179 N  N     . LYS A 525 ? 0.4986 0.4491 0.6366 -0.0252 0.022   -0.0325 525 LYS A N     
4180 C  CA    . LYS A 525 ? 0.4838 0.4381 0.6288 -0.0257 0.0222  -0.029  525 LYS A CA    
4181 C  C     . LYS A 525 ? 0.4733 0.4302 0.6157 -0.0255 0.0248  -0.0269 525 LYS A C     
4182 O  O     . LYS A 525 ? 0.475  0.4313 0.6114 -0.0258 0.0245  -0.0269 525 LYS A O     
4183 C  CB    . LYS A 525 ? 0.4954 0.45   0.6436 -0.0269 0.0184  -0.0272 525 LYS A CB    
4184 C  CG    . LYS A 525 ? 0.5349 0.4878 0.6885 -0.0274 0.0157  -0.028  525 LYS A CG    
4185 C  CD    . LYS A 525 ? 0.5752 0.5315 0.7367 -0.0282 0.0144  -0.0244 525 LYS A CD    
4186 C  CE    . LYS A 525 ? 0.6073 0.5622 0.7747 -0.0292 0.0111  -0.0245 525 LYS A CE    
4187 N  NZ    . LYS A 525 ? 0.6255 0.5794 0.7929 -0.0305 0.0067  -0.024  525 LYS A NZ    
4188 N  N     . ARG A 526 ? 0.4596 0.4189 0.6063 -0.0251 0.027   -0.025  526 ARG A N     
4189 C  CA    . ARG A 526 ? 0.4532 0.4145 0.598  -0.025  0.0291  -0.0228 526 ARG A CA    
4190 C  C     . ARG A 526 ? 0.4553 0.4174 0.5989 -0.0255 0.0271  -0.0204 526 ARG A C     
4191 O  O     . ARG A 526 ? 0.4549 0.4181 0.6031 -0.0255 0.0257  -0.0187 526 ARG A O     
4192 C  CB    . ARG A 526 ? 0.4524 0.4153 0.6024 -0.0245 0.031   -0.0212 526 ARG A CB    
4193 C  CG    . ARG A 526 ? 0.4679 0.4322 0.6163 -0.0245 0.0325  -0.0189 526 ARG A CG    
4194 C  CD    . ARG A 526 ? 0.4885 0.4537 0.6419 -0.024  0.0338  -0.0175 526 ARG A CD    
4195 N  NE    . ARG A 526 ? 0.5048 0.4704 0.6628 -0.0238 0.0324  -0.0158 526 ARG A NE    
4196 C  CZ    . ARG A 526 ? 0.524  0.4899 0.6871 -0.0235 0.033   -0.0151 526 ARG A CZ    
4197 N  NH1   . ARG A 526 ? 0.519  0.4847 0.6838 -0.0233 0.0347  -0.0161 526 ARG A NH1   
4198 N  NH2   . ARG A 526 ? 0.519  0.4853 0.6855 -0.0232 0.0319  -0.0133 526 ARG A NH2   
4199 N  N     . PRO A 527 ? 0.4555 0.4172 0.5929 -0.0257 0.0272  -0.0201 527 PRO A N     
4200 C  CA    . PRO A 527 ? 0.4549 0.4171 0.591  -0.026  0.0252  -0.0179 527 PRO A CA    
4201 C  C     . PRO A 527 ? 0.4527 0.4167 0.5918 -0.0253 0.0259  -0.015  527 PRO A C     
4202 O  O     . PRO A 527 ? 0.4528 0.4172 0.5934 -0.0249 0.028   -0.0145 527 PRO A O     
4203 C  CB    . PRO A 527 ? 0.4653 0.4262 0.5937 -0.0264 0.0253  -0.0185 527 PRO A CB    
4204 C  CG    . PRO A 527 ? 0.4702 0.4299 0.5958 -0.0264 0.0272  -0.0212 527 PRO A CG    
4205 C  CD    . PRO A 527 ? 0.4501 0.4109 0.5816 -0.0258 0.0291  -0.0215 527 PRO A CD    
4206 N  N     . ASP A 528 ? 0.4497 0.4144 0.5897 -0.025  0.0241  -0.0131 528 ASP A N     
4207 C  CA    . ASP A 528 ? 0.455  0.4206 0.5964 -0.0239 0.0246  -0.0104 528 ASP A CA    
4208 C  C     . ASP A 528 ? 0.4619 0.4264 0.5977 -0.0239 0.0252  -0.0097 528 ASP A C     
4209 O  O     . ASP A 528 ? 0.4637 0.4278 0.5998 -0.0234 0.0265  -0.0084 528 ASP A O     
4210 C  CB    . ASP A 528 ? 0.4717 0.4387 0.6152 -0.0231 0.0227  -0.0085 528 ASP A CB    
4211 C  CG    . ASP A 528 ? 0.5318 0.5006 0.6821 -0.0229 0.0223  -0.008  528 ASP A CG    
4212 O  OD1   . ASP A 528 ? 0.5343 0.503  0.6878 -0.0233 0.0233  -0.0091 528 ASP A OD1   
4213 O  OD2   . ASP A 528 ? 0.5702 0.5406 0.723  -0.0224 0.0208  -0.0064 528 ASP A OD2   
4214 N  N     . HIS A 529 ? 0.4621 0.4255 0.5926 -0.0247 0.0241  -0.0103 529 HIS A N     
4215 C  CA    . HIS A 529 ? 0.4673 0.4296 0.5923 -0.0251 0.0243  -0.0095 529 HIS A CA    
4216 C  C     . HIS A 529 ? 0.463  0.4243 0.5828 -0.0263 0.0244  -0.0113 529 HIS A C     
4217 O  O     . HIS A 529 ? 0.4642 0.4251 0.5833 -0.0267 0.0231  -0.0129 529 HIS A O     
4218 C  CB    . HIS A 529 ? 0.4818 0.4435 0.6046 -0.0243 0.0222  -0.0074 529 HIS A CB    
4219 C  CG    . HIS A 529 ? 0.5092 0.4715 0.6359 -0.0226 0.0222  -0.0056 529 HIS A CG    
4220 N  ND1   . HIS A 529 ? 0.5342 0.4956 0.6609 -0.0219 0.0232  -0.0043 529 HIS A ND1   
4221 C  CD2   . HIS A 529 ? 0.5207 0.4845 0.6512 -0.0214 0.0213  -0.0048 529 HIS A CD2   
4222 C  CE1   . HIS A 529 ? 0.5382 0.5001 0.668  -0.0202 0.023   -0.0029 529 HIS A CE1   
4223 N  NE2   . HIS A 529 ? 0.5345 0.4982 0.6669 -0.0197 0.0221  -0.003  529 HIS A NE2   
4224 N  N     . VAL A 530 ? 0.4554 0.4164 0.5717 -0.027  0.0259  -0.0108 530 VAL A N     
4225 C  CA    . VAL A 530 ? 0.4583 0.4185 0.5688 -0.028  0.0264  -0.0121 530 VAL A CA    
4226 C  C     . VAL A 530 ? 0.466  0.4253 0.5718 -0.0286 0.0255  -0.0098 530 VAL A C     
4227 O  O     . VAL A 530 ? 0.4686 0.4282 0.5757 -0.0286 0.0261  -0.0078 530 VAL A O     
4228 C  CB    . VAL A 530 ? 0.4618 0.4228 0.5726 -0.0281 0.0295  -0.0137 530 VAL A CB    
4229 C  CG1   . VAL A 530 ? 0.4702 0.4302 0.5741 -0.0288 0.0302  -0.0149 530 VAL A CG1   
4230 C  CG2   . VAL A 530 ? 0.4648 0.4261 0.5806 -0.0274 0.03    -0.0159 530 VAL A CG2   
4231 N  N     . ILE A 531 ? 0.4691 0.4269 0.5697 -0.0292 0.0235  -0.0099 531 ILE A N     
4232 C  CA    . ILE A 531 ? 0.4752 0.4319 0.5713 -0.0298 0.0221  -0.0077 531 ILE A CA    
4233 C  C     . ILE A 531 ? 0.4818 0.4379 0.5717 -0.0312 0.0232  -0.008  531 ILE A C     
4234 O  O     . ILE A 531 ? 0.483  0.4383 0.5698 -0.0314 0.0232  -0.0102 531 ILE A O     
4235 C  CB    . ILE A 531 ? 0.4796 0.435  0.5746 -0.0293 0.0186  -0.0072 531 ILE A CB    
4236 C  CG1   . ILE A 531 ? 0.4864 0.4429 0.5877 -0.0277 0.018   -0.0068 531 ILE A CG1   
4237 C  CG2   . ILE A 531 ? 0.4885 0.4421 0.5789 -0.0297 0.0167  -0.0048 531 ILE A CG2   
4238 C  CD1   . ILE A 531 ? 0.5003 0.4571 0.6046 -0.0268 0.019   -0.0051 531 ILE A CD1   
4239 N  N     . GLN A 532 ? 0.4844 0.4407 0.5723 -0.0321 0.0241  -0.0057 532 GLN A N     
4240 C  CA    . GLN A 532 ? 0.4969 0.4531 0.5788 -0.0334 0.0254  -0.0054 532 GLN A CA    
4241 C  C     . GLN A 532 ? 0.5109 0.465  0.5874 -0.0343 0.0224  -0.0035 532 GLN A C     
4242 O  O     . GLN A 532 ? 0.5106 0.4638 0.5882 -0.0344 0.0206  -0.0012 532 GLN A O     
4243 C  CB    . GLN A 532 ? 0.5133 0.4719 0.5971 -0.034  0.0287  -0.0039 532 GLN A CB    
4244 C  CG    . GLN A 532 ? 0.5473 0.5066 0.6253 -0.0349 0.031   -0.0038 532 GLN A CG    
4245 C  CD    . GLN A 532 ? 0.5838 0.5463 0.6646 -0.0353 0.0349  -0.0023 532 GLN A CD    
4246 O  OE1   . GLN A 532 ? 0.5909 0.5549 0.6781 -0.0351 0.0355  -0.0011 532 GLN A OE1   
4247 N  NE2   . GLN A 532 ? 0.5891 0.5528 0.6652 -0.0357 0.0375  -0.0021 532 GLN A NE2   
4248 N  N     . ILE A 533 ? 0.5235 0.476  0.5937 -0.035  0.0217  -0.0046 533 ILE A N     
4249 C  CA    . ILE A 533 ? 0.5428 0.4931 0.6072 -0.036  0.0188  -0.003  533 ILE A CA    
4250 C  C     . ILE A 533 ? 0.5645 0.5149 0.6225 -0.0374 0.0209  -0.0024 533 ILE A C     
4251 O  O     . ILE A 533 ? 0.5662 0.5164 0.6209 -0.0371 0.0225  -0.0047 533 ILE A O     
4252 C  CB    . ILE A 533 ? 0.5455 0.4935 0.6084 -0.0355 0.0152  -0.0045 533 ILE A CB    
4253 C  CG1   . ILE A 533 ? 0.5532 0.5017 0.6226 -0.0339 0.0135  -0.0042 533 ILE A CG1   
4254 C  CG2   . ILE A 533 ? 0.5536 0.499  0.6098 -0.0366 0.0122  -0.0029 533 ILE A CG2   
4255 C  CD1   . ILE A 533 ? 0.5708 0.5184 0.6411 -0.0332 0.0107  -0.0056 533 ILE A CD1   
4256 N  N     . LEU A 534 ? 0.5772 0.5277 0.6333 -0.0389 0.0209  0.0009  534 LEU A N     
4257 C  CA    . LEU A 534 ? 0.5959 0.5474 0.6466 -0.0402 0.0234  0.0022  534 LEU A CA    
4258 C  C     . LEU A 534 ? 0.6159 0.5645 0.6587 -0.0416 0.0207  0.0035  534 LEU A C     
4259 O  O     . LEU A 534 ? 0.6183 0.5672 0.6551 -0.0424 0.0227  0.0037  534 LEU A O     
4260 C  CB    . LEU A 534 ? 0.5957 0.5501 0.6503 -0.0412 0.0257  0.0055  534 LEU A CB    
4261 C  CG    . LEU A 534 ? 0.6087 0.5661 0.6707 -0.04   0.0289  0.0045  534 LEU A CG    
4262 C  CD1   . LEU A 534 ? 0.6103 0.5674 0.6787 -0.0398 0.0268  0.0061  534 LEU A CD1   
4263 C  CD2   . LEU A 534 ? 0.6174 0.5786 0.6799 -0.0407 0.0334  0.006   534 LEU A CD2   
4264 N  N     . ASP A 535 ? 0.6273 0.5732 0.6697 -0.0418 0.0162  0.0044  535 ASP A N     
4265 C  CA    . ASP A 535 ? 0.6485 0.5914 0.6836 -0.0431 0.0131  0.0057  535 ASP A CA    
4266 C  C     . ASP A 535 ? 0.6567 0.5966 0.6884 -0.0424 0.01    0.0031  535 ASP A C     
4267 O  O     . ASP A 535 ? 0.6609 0.598  0.69   -0.0428 0.0059  0.0041  535 ASP A O     
4268 C  CB    . ASP A 535 ? 0.6848 0.6262 0.7207 -0.0441 0.0098  0.0092  535 ASP A CB    
4269 C  CG    . ASP A 535 ? 0.7725 0.7154 0.8077 -0.0461 0.0116  0.0129  535 ASP A CG    
4270 O  OD1   . ASP A 535 ? 0.7863 0.7327 0.8236 -0.0462 0.0161  0.0129  535 ASP A OD1   
4271 O  OD2   . ASP A 535 ? 0.8112 0.7518 0.8441 -0.0475 0.0084  0.0159  535 ASP A OD2   
4272 N  N     . LEU A 536 ? 0.6551 0.5954 0.687  -0.0413 0.0117  -0.0003 536 LEU A N     
4273 C  CA    . LEU A 536 ? 0.662  0.5995 0.6911 -0.0407 0.0085  -0.0027 536 LEU A CA    
4274 C  C     . LEU A 536 ? 0.6751 0.6109 0.6962 -0.0411 0.01    -0.0046 536 LEU A C     
4275 O  O     . LEU A 536 ? 0.6808 0.6133 0.6947 -0.0421 0.0073  -0.0043 536 LEU A O     
4276 C  CB    . LEU A 536 ? 0.658  0.5966 0.6947 -0.039  0.0078  -0.0049 536 LEU A CB    
4277 C  CG    . LEU A 536 ? 0.6761 0.6122 0.7116 -0.0386 0.0045  -0.0073 536 LEU A CG    
4278 C  CD1   . LEU A 536 ? 0.6865 0.6198 0.7183 -0.0393 -0.0002 -0.0058 536 LEU A CD1   
4279 C  CD2   . LEU A 536 ? 0.6795 0.6175 0.7237 -0.0371 0.004   -0.0086 536 LEU A CD2   
4280 N  N     . PHE A 537 ? 0.679  0.6167 0.7009 -0.0403 0.0142  -0.0064 537 PHE A N     
4281 C  CA    . PHE A 537 ? 0.6927 0.6285 0.7065 -0.04   0.0163  -0.0084 537 PHE A CA    
4282 C  C     . PHE A 537 ? 0.6939 0.6327 0.7053 -0.0405 0.0213  -0.0062 537 PHE A C     
4283 O  O     . PHE A 537 ? 0.6936 0.6359 0.711  -0.041  0.023   -0.0036 537 PHE A O     
4284 C  CB    . PHE A 537 ? 0.6965 0.6318 0.7126 -0.0383 0.0172  -0.0123 537 PHE A CB    
4285 C  CG    . PHE A 537 ? 0.7101 0.6435 0.7305 -0.0379 0.0126  -0.014  537 PHE A CG    
4286 C  CD1   . PHE A 537 ? 0.727  0.6561 0.7418 -0.0385 0.0081  -0.0148 537 PHE A CD1   
4287 C  CD2   . PHE A 537 ? 0.7179 0.6538 0.7479 -0.0369 0.0128  -0.0146 537 PHE A CD2   
4288 C  CE1   . PHE A 537 ? 0.7364 0.6644 0.756  -0.0382 0.0038  -0.0159 537 PHE A CE1   
4289 C  CE2   . PHE A 537 ? 0.7269 0.6617 0.7614 -0.0366 0.0088  -0.0157 537 PHE A CE2   
4290 C  CZ    . PHE A 537 ? 0.7291 0.6601 0.7587 -0.0372 0.0044  -0.0162 537 PHE A CZ    
4291 N  N     . GLU A 538 ? 0.6933 0.6306 0.6958 -0.0403 0.0237  -0.0072 538 GLU A N     
4292 C  CA    . GLU A 538 ? 0.6941 0.635  0.6948 -0.0405 0.029   -0.0049 538 GLU A CA    
4293 C  C     . GLU A 538 ? 0.6796 0.625  0.6888 -0.039  0.0333  -0.0057 538 GLU A C     
4294 O  O     . GLU A 538 ? 0.6775 0.6272 0.6906 -0.0396 0.0366  -0.0026 538 GLU A O     
4295 C  CB    . GLU A 538 ? 0.7366 0.675  0.7255 -0.0401 0.031   -0.0057 538 GLU A CB    
4296 C  CG    . GLU A 538 ? 0.8196 0.7567 0.8051 -0.0375 0.034   -0.0099 538 GLU A CG    
4297 C  CD    . GLU A 538 ? 0.9246 0.8638 0.9039 -0.0364 0.04    -0.0092 538 GLU A CD    
4298 O  OE1   . GLU A 538 ? 0.9395 0.8814 0.9168 -0.038  0.042   -0.005  538 GLU A OE1   
4299 O  OE2   . GLU A 538 ? 0.9603 0.8985 0.9368 -0.0338 0.0429  -0.0127 538 GLU A OE2   
4300 N  N     . LYS A 539 ? 0.6669 0.6112 0.6797 -0.0372 0.0328  -0.0095 539 LYS A N     
4301 C  CA    . LYS A 539 ? 0.6561 0.604  0.6772 -0.0358 0.0361  -0.0105 539 LYS A CA    
4302 C  C     . LYS A 539 ? 0.6405 0.5895 0.6713 -0.0363 0.033   -0.0097 539 LYS A C     
4303 O  O     . LYS A 539 ? 0.6438 0.5899 0.6744 -0.0368 0.0284  -0.0102 539 LYS A O     
4304 C  CB    . LYS A 539 ? 0.6764 0.6218 0.6951 -0.0335 0.037   -0.0152 539 LYS A CB    
4305 C  CG    . LYS A 539 ? 0.7203 0.6636 0.7283 -0.0323 0.0397  -0.0168 539 LYS A CG    
4306 C  CD    . LYS A 539 ? 0.7738 0.7132 0.7793 -0.03   0.0392  -0.0217 539 LYS A CD    
4307 C  CE    . LYS A 539 ? 0.8251 0.7613 0.8188 -0.0282 0.0418  -0.0238 539 LYS A CE    
4308 N  NZ    . LYS A 539 ? 0.8525 0.7845 0.8442 -0.0258 0.0412  -0.0288 539 LYS A NZ    
4309 N  N     . PRO A 540 ? 0.6194 0.5723 0.6586 -0.0359 0.0355  -0.0086 540 PRO A N     
4310 C  CA    . PRO A 540 ? 0.6045 0.5579 0.652  -0.036  0.0328  -0.008  540 PRO A CA    
4311 C  C     . PRO A 540 ? 0.5887 0.54   0.6386 -0.0346 0.0307  -0.0117 540 PRO A C     
4312 O  O     . PRO A 540 ? 0.591  0.5417 0.6394 -0.0333 0.0325  -0.0147 540 PRO A O     
4313 C  CB    . PRO A 540 ? 0.6117 0.5695 0.6666 -0.0358 0.0364  -0.0063 540 PRO A CB    
4314 C  CG    . PRO A 540 ? 0.6204 0.5805 0.6714 -0.0359 0.0407  -0.0051 540 PRO A CG    
4315 C  CD    . PRO A 540 ? 0.6075 0.5645 0.6491 -0.0352 0.0409  -0.0077 540 PRO A CD    
4316 N  N     . LEU A 541 ? 0.5694 0.5197 0.6232 -0.0349 0.0269  -0.0112 541 LEU A N     
4317 C  CA    . LEU A 541 ? 0.5568 0.5057 0.614  -0.0338 0.0246  -0.0139 541 LEU A CA    
4318 C  C     . LEU A 541 ? 0.54   0.4917 0.6066 -0.033  0.0258  -0.0137 541 LEU A C     
4319 O  O     . LEU A 541 ? 0.5413 0.4946 0.6117 -0.0334 0.0257  -0.0111 541 LEU A O     
4320 C  CB    . LEU A 541 ? 0.5579 0.5044 0.6138 -0.0344 0.0197  -0.0133 541 LEU A CB    
4321 C  CG    . LEU A 541 ? 0.5706 0.5169 0.6328 -0.0336 0.017   -0.0146 541 LEU A CG    
4322 C  CD1   . LEU A 541 ? 0.5787 0.5228 0.6391 -0.0331 0.0162  -0.0179 541 LEU A CD1   
4323 C  CD2   . LEU A 541 ? 0.5781 0.5236 0.641  -0.0339 0.0131  -0.0128 541 LEU A CD2   
4324 N  N     . LEU A 542 ? 0.525  0.4767 0.595  -0.0319 0.0265  -0.0164 542 LEU A N     
4325 C  CA    . LEU A 542 ? 0.5159 0.4697 0.5945 -0.0311 0.0272  -0.0163 542 LEU A CA    
4326 C  C     . LEU A 542 ? 0.5165 0.4688 0.5981 -0.0307 0.0238  -0.0178 542 LEU A C     
4327 O  O     . LEU A 542 ? 0.5243 0.4745 0.6036 -0.0304 0.0229  -0.0204 542 LEU A O     
4328 C  CB    . LEU A 542 ? 0.5135 0.4688 0.5943 -0.0301 0.031   -0.018  542 LEU A CB    
4329 C  CG    . LEU A 542 ? 0.5307 0.4882 0.6095 -0.0304 0.0347  -0.0163 542 LEU A CG    
4330 C  CD1   . LEU A 542 ? 0.5397 0.4986 0.62   -0.0291 0.0386  -0.0182 542 LEU A CD1   
4331 C  CD2   . LEU A 542 ? 0.5367 0.4964 0.6205 -0.0312 0.0347  -0.0128 542 LEU A CD2   
4332 N  N     . LEU A 543 ? 0.5061 0.4593 0.5921 -0.0307 0.0217  -0.0159 543 LEU A N     
4333 C  CA    . LEU A 543 ? 0.4995 0.4522 0.5894 -0.0303 0.0186  -0.0164 543 LEU A CA    
4334 C  C     . LEU A 543 ? 0.4965 0.4514 0.5947 -0.0294 0.0197  -0.0163 543 LEU A C     
4335 O  O     . LEU A 543 ? 0.4981 0.4546 0.5999 -0.0289 0.0204  -0.0142 543 LEU A O     
4336 C  CB    . LEU A 543 ? 0.4969 0.4492 0.5859 -0.0305 0.0156  -0.0141 543 LEU A CB    
4337 C  CG    . LEU A 543 ? 0.5071 0.4598 0.601  -0.03   0.0126  -0.0139 543 LEU A CG    
4338 C  CD1   . LEU A 543 ? 0.5139 0.4643 0.6052 -0.0307 0.01    -0.016  543 LEU A CD1   
4339 C  CD2   . LEU A 543 ? 0.5124 0.4654 0.6063 -0.0296 0.0104  -0.0114 543 LEU A CD2   
4340 N  N     . SER A 544 ? 0.4896 0.444  0.5905 -0.0291 0.0196  -0.0186 544 SER A N     
4341 C  CA    . SER A 544 ? 0.4883 0.4447 0.5972 -0.0284 0.0205  -0.0185 544 SER A CA    
4342 C  C     . SER A 544 ? 0.4887 0.4459 0.6026 -0.0282 0.0175  -0.0174 544 SER A C     
4343 O  O     . SER A 544 ? 0.4918 0.4474 0.6048 -0.0287 0.0146  -0.0184 544 SER A O     
4344 C  CB    . SER A 544 ? 0.5047 0.4601 0.6142 -0.0281 0.0218  -0.0214 544 SER A CB    
4345 O  OG    . SER A 544 ? 0.5365 0.4919 0.642  -0.0279 0.025   -0.0221 544 SER A OG    
4346 N  N     . ILE A 545 ? 0.48   0.4394 0.5991 -0.0274 0.018   -0.0151 545 ILE A N     
4347 C  CA    . ILE A 545 ? 0.4733 0.4342 0.5974 -0.0269 0.0158  -0.0134 545 ILE A CA    
4348 C  C     . ILE A 545 ? 0.4671 0.4301 0.5989 -0.0263 0.0167  -0.0128 545 ILE A C     
4349 O  O     . ILE A 545 ? 0.4659 0.4296 0.5995 -0.0257 0.0192  -0.0126 545 ILE A O     
4350 C  CB    . ILE A 545 ? 0.4779 0.4396 0.6005 -0.0261 0.0153  -0.0108 545 ILE A CB    
4351 C  CG1   . ILE A 545 ? 0.491  0.4504 0.6057 -0.0268 0.0146  -0.0109 545 ILE A CG1   
4352 C  CG2   . ILE A 545 ? 0.4827 0.4462 0.6099 -0.0252 0.0131  -0.0089 545 ILE A CG2   
4353 C  CD1   . ILE A 545 ? 0.5072 0.4666 0.6201 -0.0259 0.0143  -0.0085 545 ILE A CD1   
4354 N  N     . VAL A 546 ? 0.466  0.43   0.6025 -0.0264 0.0145  -0.0123 546 VAL A N     
4355 C  CA    . VAL A 546 ? 0.4729 0.4393 0.6172 -0.0259 0.015   -0.0111 546 VAL A CA    
4356 C  C     . VAL A 546 ? 0.4773 0.4464 0.6255 -0.025  0.0136  -0.0081 546 VAL A C     
4357 O  O     . VAL A 546 ? 0.4777 0.4467 0.6246 -0.0254 0.011   -0.0076 546 VAL A O     
4358 C  CB    . VAL A 546 ? 0.4863 0.4517 0.634  -0.027  0.0137  -0.0131 546 VAL A CB    
4359 C  CG1   . VAL A 546 ? 0.4987 0.4625 0.6448 -0.0282 0.0099  -0.0139 546 VAL A CG1   
4360 C  CG2   . VAL A 546 ? 0.4899 0.4579 0.6459 -0.0267 0.014   -0.0113 546 VAL A CG2   
4361 N  N     . SER A 547 ? 0.4782 0.4497 0.6306 -0.0235 0.0154  -0.0058 547 SER A N     
4362 C  CA    . SER A 547 ? 0.4864 0.4608 0.6425 -0.0221 0.0148  -0.0028 547 SER A CA    
4363 C  C     . SER A 547 ? 0.4856 0.4631 0.6501 -0.0219 0.0149  -0.0011 547 SER A C     
4364 O  O     . SER A 547 ? 0.4898 0.4672 0.6566 -0.022  0.0167  -0.0015 547 SER A O     
4365 C  CB    . SER A 547 ? 0.514  0.4883 0.667  -0.0199 0.0166  -0.0012 547 SER A CB    
4366 O  OG    . SER A 547 ? 0.5595 0.5332 0.7131 -0.0194 0.0191  -0.0014 547 SER A OG    
4367 N  N     . LYS A 548 ? 0.4771 0.4574 0.6465 -0.0219 0.0129  0.001   548 LYS A N     
4368 C  CA    . LYS A 548 ? 0.4742 0.4581 0.6523 -0.0219 0.0128  0.0034  548 LYS A CA    
4369 C  C     . LYS A 548 ? 0.471  0.4592 0.6529 -0.0199 0.0129  0.0072  548 LYS A C     
4370 O  O     . LYS A 548 ? 0.471  0.4589 0.649  -0.0189 0.0122  0.0074  548 LYS A O     
4371 C  CB    . LYS A 548 ? 0.4949 0.4781 0.6766 -0.0245 0.0096  0.0022  548 LYS A CB    
4372 C  CG    . LYS A 548 ? 0.5471 0.5262 0.7255 -0.0261 0.0096  -0.0015 548 LYS A CG    
4373 C  CD    . LYS A 548 ? 0.5941 0.5738 0.7757 -0.0256 0.0123  -0.0013 548 LYS A CD    
4374 C  CE    . LYS A 548 ? 0.6291 0.6048 0.8067 -0.0265 0.013   -0.005  548 LYS A CE    
4375 N  NZ    . LYS A 548 ? 0.6478 0.6209 0.826  -0.0284 0.0098  -0.0073 548 LYS A NZ    
4376 N  N     . GLU A 549 ? 0.466  0.4584 0.6557 -0.0192 0.0139  0.0102  549 GLU A N     
4377 C  CA    . GLU A 549 ? 0.4673 0.4644 0.6614 -0.017  0.0144  0.0141  549 GLU A CA    
4378 C  C     . GLU A 549 ? 0.4708 0.4701 0.6693 -0.0184 0.0107  0.0152  549 GLU A C     
4379 O  O     . GLU A 549 ? 0.4711 0.4717 0.6683 -0.0168 0.0101  0.0165  549 GLU A O     
4380 C  CB    . GLU A 549 ? 0.4852 0.4864 0.6864 -0.0159 0.0169  0.0173  549 GLU A CB    
4381 C  CG    . GLU A 549 ? 0.5199 0.527  0.7268 -0.0133 0.0179  0.0218  549 GLU A CG    
4382 C  CD    . GLU A 549 ? 0.5527 0.5639 0.7659 -0.012  0.0208  0.0253  549 GLU A CD    
4383 O  OE1   . GLU A 549 ? 0.568  0.5774 0.7816 -0.0133 0.0217  0.0243  549 GLU A OE1   
4384 O  OE2   . GLU A 549 ? 0.5479 0.5643 0.7656 -0.0095 0.0223  0.0293  549 GLU A OE2   
4385 N  N     . LYS A 550 ? 0.4718 0.4709 0.6751 -0.0213 0.0079  0.0147  550 LYS A N     
4386 C  CA    . LYS A 550 ? 0.4794 0.4798 0.6872 -0.0231 0.0037  0.0158  550 LYS A CA    
4387 C  C     . LYS A 550 ? 0.4927 0.4873 0.695  -0.0259 0.0002  0.0117  550 LYS A C     
4388 O  O     . LYS A 550 ? 0.4973 0.488  0.6956 -0.0269 0.001   0.0086  550 LYS A O     
4389 C  CB    . LYS A 550 ? 0.4991 0.5044 0.7183 -0.0243 0.0027  0.0195  550 LYS A CB    
4390 C  CG    . LYS A 550 ? 0.5426 0.5541 0.7675 -0.0214 0.0065  0.024   550 LYS A CG    
4391 C  CD    . LYS A 550 ? 0.5716 0.5877 0.8076 -0.0228 0.0059  0.0276  550 LYS A CD    
4392 C  CE    . LYS A 550 ? 0.5906 0.6128 0.8316 -0.0198 0.0103  0.0321  550 LYS A CE    
4393 N  NZ    . LYS A 550 ? 0.6006 0.6269 0.8423 -0.0167 0.0114  0.0348  550 LYS A NZ    
4394 N  N     . PRO A 551 ? 0.5011 0.4949 0.7033 -0.0272 -0.0039 0.0116  551 PRO A N     
4395 C  CA    . PRO A 551 ? 0.5173 0.505  0.7132 -0.0296 -0.0073 0.0076  551 PRO A CA    
4396 C  C     . PRO A 551 ? 0.5389 0.5244 0.7382 -0.0319 -0.0094 0.0063  551 PRO A C     
4397 O  O     . PRO A 551 ? 0.5467 0.5266 0.7393 -0.033  -0.0102 0.0023  551 PRO A O     
4398 C  CB    . PRO A 551 ? 0.5232 0.5111 0.7197 -0.0303 -0.0115 0.0088  551 PRO A CB    
4399 C  CG    . PRO A 551 ? 0.5193 0.5144 0.7259 -0.029  -0.0111 0.0139  551 PRO A CG    
4400 C  CD    . PRO A 551 ? 0.4945 0.4927 0.7016 -0.0262 -0.0055 0.0152  551 PRO A CD    
4401 N  N     . ASN A 552 ? 0.5461 0.5359 0.7559 -0.0326 -0.0102 0.0098  552 ASN A N     
4402 C  CA    . ASN A 552 ? 0.5618 0.5494 0.7754 -0.0349 -0.0125 0.0088  552 ASN A CA    
4403 C  C     . ASN A 552 ? 0.5743 0.5603 0.7856 -0.0342 -0.0086 0.0068  552 ASN A C     
4404 O  O     . ASN A 552 ? 0.5774 0.5604 0.79   -0.0358 -0.0103 0.0051  552 ASN A O     
4405 C  CB    . ASN A 552 ? 0.5766 0.5689 0.8024 -0.0364 -0.0154 0.0135  552 ASN A CB    
4406 C  CG    . ASN A 552 ? 0.6216 0.6221 0.8554 -0.0345 -0.0128 0.0189  552 ASN A CG    
4407 O  OD1   . ASN A 552 ? 0.6349 0.6377 0.8661 -0.0323 -0.011  0.0198  552 ASN A OD1   
4408 N  ND2   . ASN A 552 ? 0.6286 0.6338 0.8728 -0.0352 -0.0127 0.0228  552 ASN A ND2   
4409 N  N     . ASP A 553 ? 0.5792 0.5667 0.7867 -0.0317 -0.0037 0.0069  553 ASP A N     
4410 C  CA    . ASP A 553 ? 0.591  0.5768 0.7958 -0.031  -0.0002 0.0049  553 ASP A CA    
4411 C  C     . ASP A 553 ? 0.6062 0.5857 0.8014 -0.0315 -0.0004 -0.0002 553 ASP A C     
4412 O  O     . ASP A 553 ? 0.6095 0.5868 0.8032 -0.0314 0.0015  -0.0023 553 ASP A O     
4413 C  CB    . ASP A 553 ? 0.6121 0.6013 0.8161 -0.0282 0.0045  0.0069  553 ASP A CB    
4414 C  CG    . ASP A 553 ? 0.6666 0.6621 0.8795 -0.0272 0.0056  0.012   553 ASP A CG    
4415 O  OD1   . ASP A 553 ? 0.6744 0.672  0.8954 -0.0289 0.0035  0.0141  553 ASP A OD1   
4416 O  OD2   . ASP A 553 ? 0.6932 0.6914 0.9047 -0.0246 0.0085  0.014   553 ASP A OD2   
4417 N  N     . LEU A 554 ? 0.6126 0.5893 0.8016 -0.0319 -0.0025 -0.0021 554 LEU A N     
4418 C  CA    . LEU A 554 ? 0.6268 0.5978 0.8064 -0.0323 -0.0026 -0.0066 554 LEU A CA    
4419 C  C     . LEU A 554 ? 0.6399 0.6069 0.8205 -0.0341 -0.0059 -0.0089 554 LEU A C     
4420 O  O     . LEU A 554 ? 0.6425 0.608  0.825  -0.0356 -0.0106 -0.0086 554 LEU A O     
4421 C  CB    . LEU A 554 ? 0.6288 0.5981 0.802  -0.0323 -0.0045 -0.0072 554 LEU A CB    
4422 C  CG    . LEU A 554 ? 0.6402 0.6121 0.8105 -0.0305 -0.0017 -0.0056 554 LEU A CG    
4423 C  CD1   . LEU A 554 ? 0.6477 0.6181 0.8133 -0.0308 -0.0045 -0.0057 554 LEU A CD1   
4424 C  CD2   . LEU A 554 ? 0.6485 0.6187 0.8126 -0.0294 0.0023  -0.0076 554 LEU A CD2   
4425 N  N     . GLU A 555 ? 0.6461 0.6111 0.8259 -0.0338 -0.0038 -0.0111 555 GLU A N     
4426 C  CA    . GLU A 555 ? 0.6599 0.6207 0.8406 -0.0351 -0.0066 -0.0136 555 GLU A CA    
4427 C  C     . GLU A 555 ? 0.6606 0.6151 0.8331 -0.0357 -0.01   -0.0174 555 GLU A C     
4428 O  O     . GLU A 555 ? 0.6675 0.6206 0.8321 -0.035  -0.0088 -0.0189 555 GLU A O     
4429 C  CB    . GLU A 555 ? 0.7084 0.6684 0.8892 -0.0342 -0.0032 -0.0153 555 GLU A CB    
4430 C  CG    . GLU A 555 ? 0.8131 0.7747 0.9895 -0.0323 0.002   -0.0156 555 GLU A CG    
4431 C  CD    . GLU A 555 ? 0.933  0.8982 1.1155 -0.0316 0.0051  -0.0133 555 GLU A CD    
4432 O  OE1   . GLU A 555 ? 0.9619 0.9298 1.143  -0.0302 0.0084  -0.0118 555 GLU A OE1   
4433 O  OE2   . GLU A 555 ? 0.9638 0.9287 1.152  -0.0323 0.0039  -0.013  555 GLU A OE2   
4434 N  N     . PRO A 556 ? 0.65   0.6002 0.8239 -0.0371 -0.0144 -0.0189 556 PRO A N     
4435 C  CA    . PRO A 556 ? 0.6436 0.5869 0.8087 -0.0375 -0.0178 -0.0227 556 PRO A CA    
4436 C  C     . PRO A 556 ? 0.6307 0.5708 0.7857 -0.0357 -0.0139 -0.0267 556 PRO A C     
4437 O  O     . PRO A 556 ? 0.63   0.5709 0.7858 -0.0345 -0.0101 -0.0277 556 PRO A O     
4438 C  CB    . PRO A 556 ? 0.656  0.5951 0.8249 -0.0389 -0.0226 -0.0237 556 PRO A CB    
4439 C  CG    . PRO A 556 ? 0.6602 0.605  0.8413 -0.04   -0.023  -0.0192 556 PRO A CG    
4440 C  CD    . PRO A 556 ? 0.6399 0.5909 0.823  -0.0384 -0.0167 -0.0172 556 PRO A CD    
4441 N  N     . LYS A 557 ? 0.6172 0.5539 0.763  -0.0354 -0.0148 -0.0286 557 LYS A N     
4442 C  CA    . LYS A 557 ? 0.6112 0.545  0.7468 -0.0338 -0.0113 -0.0321 557 LYS A CA    
4443 C  C     . LYS A 557 ? 0.5955 0.5343 0.7313 -0.0325 -0.0052 -0.0308 557 LYS A C     
4444 O  O     . LYS A 557 ? 0.5981 0.5354 0.7278 -0.0311 -0.0018 -0.0333 557 LYS A O     
4445 C  CB    . LYS A 557 ? 0.6327 0.5608 0.7645 -0.0329 -0.0118 -0.0363 557 LYS A CB    
4446 C  CG    . LYS A 557 ? 0.6801 0.6011 0.8086 -0.0339 -0.0181 -0.0384 557 LYS A CG    
4447 C  CD    . LYS A 557 ? 0.7357 0.6521 0.8649 -0.0333 -0.0193 -0.0414 557 LYS A CD    
4448 C  CE    . LYS A 557 ? 0.781  0.6956 0.9033 -0.0306 -0.0142 -0.045  557 LYS A CE    
4449 N  NZ    . LYS A 557 ? 0.8024 0.7147 0.9284 -0.0299 -0.0144 -0.0469 557 LYS A NZ    
4450 N  N     . ILE A 558 ? 0.5776 0.5224 0.7204 -0.0327 -0.0039 -0.0268 558 ILE A N     
4451 C  CA    . ILE A 558 ? 0.5653 0.5142 0.7082 -0.0315 0.0012  -0.0254 558 ILE A CA    
4452 C  C     . ILE A 558 ? 0.5599 0.5075 0.6935 -0.0309 0.0032  -0.0266 558 ILE A C     
4453 O  O     . ILE A 558 ? 0.5619 0.5101 0.6926 -0.0298 0.0073  -0.0275 558 ILE A O     
4454 C  CB    . ILE A 558 ? 0.5618 0.5164 0.7129 -0.0315 0.002   -0.0211 558 ILE A CB    
4455 C  CG1   . ILE A 558 ? 0.5655 0.5232 0.7168 -0.0301 0.0069  -0.0201 558 ILE A CG1   
4456 C  CG2   . ILE A 558 ? 0.5681 0.5242 0.7189 -0.032  -0.0004 -0.0188 558 ILE A CG2   
4457 C  CD1   . ILE A 558 ? 0.5775 0.5346 0.7308 -0.0296 0.0093  -0.0216 558 ILE A CD1   
4458 N  N     . GLY A 559 ? 0.5508 0.4963 0.6796 -0.0316 0.0002  -0.0267 559 GLY A N     
4459 C  CA    . GLY A 559 ? 0.551  0.4949 0.6705 -0.0312 0.0015  -0.0277 559 GLY A CA    
4460 C  C     . GLY A 559 ? 0.548  0.4879 0.6598 -0.0304 0.0035  -0.0313 559 GLY A C     
4461 O  O     . GLY A 559 ? 0.5507 0.4916 0.658  -0.0295 0.0074  -0.0316 559 GLY A O     
4462 N  N     . VAL A 560 ? 0.5405 0.4759 0.651  -0.0304 0.0009  -0.0341 560 VAL A N     
4463 C  CA    . VAL A 560 ? 0.5397 0.4709 0.6427 -0.0291 0.0027  -0.0379 560 VAL A CA    
4464 C  C     . VAL A 560 ? 0.5256 0.4599 0.6324 -0.0278 0.0077  -0.0381 560 VAL A C     
4465 O  O     . VAL A 560 ? 0.5302 0.4642 0.6315 -0.0264 0.0116  -0.0396 560 VAL A O     
4466 C  CB    . VAL A 560 ? 0.5545 0.4794 0.6554 -0.0293 -0.0021 -0.0408 560 VAL A CB    
4467 C  CG1   . VAL A 560 ? 0.569  0.4893 0.6623 -0.0273 0.0001  -0.045  560 VAL A CG1   
4468 C  CG2   . VAL A 560 ? 0.5603 0.4817 0.6566 -0.0307 -0.0072 -0.0406 560 VAL A CG2   
4469 N  N     . GLN A 561 ? 0.5074 0.4449 0.624  -0.0281 0.0077  -0.0364 561 GLN A N     
4470 C  CA    . GLN A 561 ? 0.4982 0.4385 0.6194 -0.0271 0.0118  -0.0362 561 GLN A CA    
4471 C  C     . GLN A 561 ? 0.4953 0.4397 0.6156 -0.0266 0.0161  -0.0342 561 GLN A C     
4472 O  O     . GLN A 561 ? 0.4984 0.4439 0.6184 -0.0255 0.0198  -0.035  561 GLN A O     
4473 C  CB    . GLN A 561 ? 0.5052 0.4477 0.6366 -0.0278 0.0103  -0.0343 561 GLN A CB    
4474 C  CG    . GLN A 561 ? 0.5331 0.4714 0.6662 -0.0282 0.0063  -0.0365 561 GLN A CG    
4475 C  CD    . GLN A 561 ? 0.5644 0.5053 0.708  -0.0292 0.0046  -0.034  561 GLN A CD    
4476 O  OE1   . GLN A 561 ? 0.571  0.5132 0.7191 -0.0307 0.0013  -0.0315 561 GLN A OE1   
4477 N  NE2   . GLN A 561 ? 0.5672 0.5089 0.7149 -0.0284 0.007   -0.0345 561 GLN A NE2   
4478 N  N     . LEU A 562 ? 0.4861 0.4327 0.6059 -0.0275 0.0153  -0.0315 562 LEU A N     
4479 C  CA    . LEU A 562 ? 0.4806 0.4304 0.5992 -0.0272 0.0187  -0.0294 562 LEU A CA    
4480 C  C     . LEU A 562 ? 0.482  0.4301 0.592  -0.0266 0.0211  -0.0311 562 LEU A C     
4481 O  O     . LEU A 562 ? 0.4891 0.4395 0.5992 -0.026  0.0249  -0.0304 562 LEU A O     
4482 C  CB    . LEU A 562 ? 0.4804 0.4322 0.5997 -0.028  0.0169  -0.0264 562 LEU A CB    
4483 C  CG    . LEU A 562 ? 0.4933 0.4477 0.6211 -0.0283 0.0153  -0.0239 562 LEU A CG    
4484 C  CD1   . LEU A 562 ? 0.5015 0.4576 0.629  -0.0286 0.0137  -0.0212 562 LEU A CD1   
4485 C  CD2   . LEU A 562 ? 0.497  0.4541 0.6304 -0.0275 0.0183  -0.0227 562 LEU A CD2   
4486 N  N     . ILE A 563 ? 0.4751 0.4192 0.5778 -0.0267 0.019   -0.0333 563 ILE A N     
4487 C  CA    . ILE A 563 ? 0.4759 0.4182 0.5696 -0.026  0.0214  -0.0349 563 ILE A CA    
4488 C  C     . ILE A 563 ? 0.4785 0.4202 0.5721 -0.0242 0.0246  -0.0375 563 ILE A C     
4489 O  O     . ILE A 563 ? 0.4816 0.4253 0.573  -0.0234 0.0288  -0.0371 563 ILE A O     
4490 C  CB    . ILE A 563 ? 0.4795 0.417  0.5648 -0.0264 0.018   -0.0366 563 ILE A CB    
4491 C  CG1   . ILE A 563 ? 0.4909 0.4293 0.5769 -0.028  0.0147  -0.0339 563 ILE A CG1   
4492 C  CG2   . ILE A 563 ? 0.485  0.4207 0.5604 -0.0253 0.021   -0.0382 563 ILE A CG2   
4493 C  CD1   . ILE A 563 ? 0.5089 0.4506 0.5937 -0.0284 0.0171  -0.0311 563 ILE A CD1   
4494 N  N     . LYS A 564 ? 0.4729 0.412  0.5697 -0.0238 0.0226  -0.0397 564 LYS A N     
4495 C  CA    . LYS A 564 ? 0.4747 0.4127 0.5719 -0.0219 0.0252  -0.0423 564 LYS A CA    
4496 C  C     . LYS A 564 ? 0.4661 0.4092 0.5705 -0.0214 0.0292  -0.0404 564 LYS A C     
4497 O  O     . LYS A 564 ? 0.4655 0.409  0.5693 -0.0197 0.0327  -0.0419 564 LYS A O     
4498 C  CB    . LYS A 564 ? 0.5017 0.4355 0.6014 -0.0217 0.0213  -0.0448 564 LYS A CB    
4499 C  CG    . LYS A 564 ? 0.5594 0.487  0.6513 -0.022  0.0169  -0.0471 564 LYS A CG    
4500 C  CD    . LYS A 564 ? 0.6179 0.5421 0.6985 -0.0201 0.0192  -0.0499 564 LYS A CD    
4501 C  CE    . LYS A 564 ? 0.6627 0.5813 0.7346 -0.0207 0.0148  -0.0513 564 LYS A CE    
4502 N  NZ    . LYS A 564 ? 0.69   0.6074 0.751  -0.0195 0.0179  -0.0522 564 LYS A NZ    
4503 N  N     . TYR A 565 ? 0.4576 0.4044 0.5685 -0.0228 0.0288  -0.0371 565 TYR A N     
4504 C  CA    . TYR A 565 ? 0.4544 0.4054 0.5715 -0.0226 0.032   -0.035  565 TYR A CA    
4505 C  C     . TYR A 565 ? 0.4587 0.412  0.5715 -0.0223 0.0356  -0.0337 565 TYR A C     
4506 O  O     . TYR A 565 ? 0.4621 0.4176 0.5771 -0.0213 0.0391  -0.0336 565 TYR A O     
4507 C  CB    . TYR A 565 ? 0.4491 0.4026 0.5729 -0.0238 0.0303  -0.0318 565 TYR A CB    
4508 C  CG    . TYR A 565 ? 0.4516 0.4084 0.5819 -0.0235 0.0329  -0.0301 565 TYR A CG    
4509 C  CD1   . TYR A 565 ? 0.4562 0.4128 0.5925 -0.0229 0.033   -0.0311 565 TYR A CD1   
4510 C  CD2   . TYR A 565 ? 0.462  0.4214 0.5923 -0.0238 0.0349  -0.0274 565 TYR A CD2   
4511 C  CE1   . TYR A 565 ? 0.4618 0.4209 0.6038 -0.0226 0.0351  -0.0294 565 TYR A CE1   
4512 C  CE2   . TYR A 565 ? 0.4691 0.4309 0.6051 -0.0236 0.0368  -0.0257 565 TYR A CE2   
4513 C  CZ    . TYR A 565 ? 0.4748 0.4364 0.6166 -0.023  0.037   -0.0268 565 TYR A CZ    
4514 O  OH    . TYR A 565 ? 0.4908 0.4544 0.6381 -0.0228 0.0385  -0.0251 565 TYR A OH    
4515 N  N     . ILE A 566 ? 0.4574 0.4103 0.5645 -0.0233 0.0347  -0.0324 566 ILE A N     
4516 C  CA    . ILE A 566 ? 0.4624 0.4174 0.5651 -0.0233 0.0378  -0.0309 566 ILE A CA    
4517 C  C     . ILE A 566 ? 0.47   0.4237 0.567  -0.0216 0.0408  -0.0336 566 ILE A C     
4518 O  O     . ILE A 566 ? 0.4703 0.4269 0.5678 -0.0209 0.0448  -0.0325 566 ILE A O     
4519 C  CB    . ILE A 566 ? 0.47   0.4244 0.5676 -0.0248 0.0356  -0.029  566 ILE A CB    
4520 C  CG1   . ILE A 566 ? 0.4791 0.4345 0.5822 -0.0259 0.0327  -0.0266 566 ILE A CG1   
4521 C  CG2   . ILE A 566 ? 0.474  0.4305 0.5675 -0.0251 0.0386  -0.0269 566 ILE A CG2   
4522 C  CD1   . ILE A 566 ? 0.4898 0.4487 0.5992 -0.026  0.0344  -0.0238 566 ILE A CD1   
4523 N  N     . GLU A 567 ? 0.4753 0.4245 0.5675 -0.0206 0.0389  -0.037  567 GLU A N     
4524 C  CA    . GLU A 567 ? 0.4858 0.4328 0.5719 -0.0184 0.0415  -0.0401 567 GLU A CA    
4525 C  C     . GLU A 567 ? 0.4827 0.432  0.575  -0.0167 0.0449  -0.0409 567 GLU A C     
4526 O  O     . GLU A 567 ? 0.4844 0.4351 0.5738 -0.0148 0.0491  -0.0416 567 GLU A O     
4527 C  CB    . GLU A 567 ? 0.5212 0.4618 0.6015 -0.0178 0.0377  -0.0438 567 GLU A CB    
4528 C  CG    . GLU A 567 ? 0.5749 0.5125 0.6475 -0.0191 0.0345  -0.0435 567 GLU A CG    
4529 C  CD    . GLU A 567 ? 0.6505 0.5856 0.7117 -0.0177 0.0366  -0.0451 567 GLU A CD    
4530 O  OE1   . GLU A 567 ? 0.672  0.6089 0.7315 -0.0157 0.0415  -0.0457 567 GLU A OE1   
4531 O  OE2   . GLU A 567 ? 0.6644 0.5956 0.7183 -0.0185 0.0334  -0.0456 567 GLU A OE2   
4532 N  N     . TYR A 568 ? 0.4765 0.4266 0.5775 -0.0172 0.0432  -0.0405 568 TYR A N     
4533 C  CA    . TYR A 568 ? 0.4761 0.4283 0.5841 -0.0158 0.0457  -0.041  568 TYR A CA    
4534 C  C     . TYR A 568 ? 0.4631 0.4208 0.5745 -0.016  0.0498  -0.0378 568 TYR A C     
4535 O  O     . TYR A 568 ? 0.4648 0.4242 0.5775 -0.0141 0.0535  -0.0385 568 TYR A O     
4536 C  CB    . TYR A 568 ? 0.4813 0.433  0.5975 -0.0168 0.0425  -0.0407 568 TYR A CB    
4537 C  CG    . TYR A 568 ? 0.4926 0.4475 0.6175 -0.0162 0.0447  -0.0397 568 TYR A CG    
4538 C  CD1   . TYR A 568 ? 0.5056 0.4593 0.6321 -0.0141 0.0464  -0.0424 568 TYR A CD1   
4539 C  CD2   . TYR A 568 ? 0.5041 0.4624 0.6353 -0.0178 0.0446  -0.0361 568 TYR A CD2   
4540 C  CE1   . TYR A 568 ? 0.5172 0.4736 0.6518 -0.0136 0.048   -0.0413 568 TYR A CE1   
4541 C  CE2   . TYR A 568 ? 0.5152 0.4759 0.654  -0.0174 0.0462  -0.0351 568 TYR A CE2   
4542 C  CZ    . TYR A 568 ? 0.5292 0.4891 0.67   -0.0154 0.0478  -0.0376 568 TYR A CZ    
4543 O  OH    . TYR A 568 ? 0.5522 0.5144 0.7008 -0.0151 0.0492  -0.0365 568 TYR A OH    
4544 N  N     . LEU A 569 ? 0.4481 0.4081 0.5611 -0.0181 0.0489  -0.0342 569 LEU A N     
4545 C  CA    . LEU A 569 ? 0.4373 0.402  0.5536 -0.0187 0.052   -0.0308 569 LEU A CA    
4546 C  C     . LEU A 569 ? 0.4451 0.4112 0.5549 -0.0178 0.0557  -0.0306 569 LEU A C     
4547 O  O     . LEU A 569 ? 0.4421 0.412  0.5551 -0.017  0.0594  -0.0292 569 LEU A O     
4548 C  CB    . LEU A 569 ? 0.4269 0.3928 0.5453 -0.021  0.0496  -0.0274 569 LEU A CB    
4549 C  CG    . LEU A 569 ? 0.4301 0.3952 0.5549 -0.0217 0.0465  -0.0269 569 LEU A CG    
4550 C  CD1   . LEU A 569 ? 0.4334 0.399  0.5586 -0.0234 0.0442  -0.0238 569 LEU A CD1   
4551 C  CD2   . LEU A 569 ? 0.4306 0.3977 0.5632 -0.021  0.0482  -0.0265 569 LEU A CD2   
4552 N  N     . PHE A 570 ? 0.456  0.4191 0.5568 -0.0178 0.0546  -0.032  570 PHE A N     
4553 C  CA    . PHE A 570 ? 0.4717 0.4356 0.5649 -0.0168 0.058   -0.032  570 PHE A CA    
4554 C  C     . PHE A 570 ? 0.4847 0.4487 0.5766 -0.0137 0.062   -0.0348 570 PHE A C     
4555 O  O     . PHE A 570 ? 0.4889 0.4555 0.5771 -0.0125 0.0662  -0.0338 570 PHE A O     
4556 C  CB    . PHE A 570 ? 0.4774 0.4372 0.5608 -0.0175 0.0554  -0.0331 570 PHE A CB    
4557 C  CG    . PHE A 570 ? 0.4855 0.4466 0.5674 -0.0201 0.0538  -0.0294 570 PHE A CG    
4558 C  CD1   . PHE A 570 ? 0.4959 0.4608 0.5765 -0.0207 0.057   -0.0262 570 PHE A CD1   
4559 C  CD2   . PHE A 570 ? 0.4952 0.4538 0.577  -0.0218 0.049   -0.0291 570 PHE A CD2   
4560 C  CE1   . PHE A 570 ? 0.5041 0.4696 0.583  -0.0231 0.0552  -0.0229 570 PHE A CE1   
4561 C  CE2   . PHE A 570 ? 0.5039 0.4634 0.5841 -0.0239 0.0475  -0.0259 570 PHE A CE2   
4562 C  CZ    . PHE A 570 ? 0.4997 0.4623 0.5783 -0.0245 0.0504  -0.0229 570 PHE A CZ    
4563 N  N     . ASP A 571 ? 0.4899 0.4512 0.585  -0.0121 0.0607  -0.038  571 ASP A N     
4564 C  CA    . ASP A 571 ? 0.5016 0.4628 0.5965 -0.0088 0.0642  -0.0409 571 ASP A CA    
4565 C  C     . ASP A 571 ? 0.5069 0.4743 0.6105 -0.0082 0.0684  -0.0382 571 ASP A C     
4566 O  O     . ASP A 571 ? 0.5087 0.4772 0.6127 -0.0053 0.0722  -0.0399 571 ASP A O     
4567 C  CB    . ASP A 571 ? 0.5226 0.4788 0.6192 -0.0076 0.0609  -0.0448 571 ASP A CB    
4568 C  CG    . ASP A 571 ? 0.5907 0.54   0.6778 -0.007  0.0575  -0.0485 571 ASP A CG    
4569 O  OD1   . ASP A 571 ? 0.6063 0.5544 0.6847 -0.0072 0.0578  -0.0482 571 ASP A OD1   
4570 O  OD2   . ASP A 571 ? 0.6199 0.5648 0.7083 -0.0063 0.0543  -0.0514 571 ASP A OD2   
4571 N  N     . PHE A 572 ? 0.5068 0.478  0.6176 -0.0109 0.0676  -0.0341 572 PHE A N     
4572 C  CA    . PHE A 572 ? 0.5126 0.4893 0.6321 -0.0108 0.0706  -0.0313 572 PHE A CA    
4573 C  C     . PHE A 572 ? 0.5202 0.5014 0.6407 -0.013  0.072   -0.0264 572 PHE A C     
4574 O  O     . PHE A 572 ? 0.5237 0.5036 0.6402 -0.0153 0.0694  -0.0249 572 PHE A O     
4575 C  CB    . PHE A 572 ? 0.5087 0.4849 0.6373 -0.0117 0.0677  -0.0311 572 PHE A CB    
4576 C  CG    . PHE A 572 ? 0.519  0.4909 0.6475 -0.0098 0.0662  -0.0356 572 PHE A CG    
4577 C  CD1   . PHE A 572 ? 0.53   0.5024 0.6602 -0.0067 0.0693  -0.0379 572 PHE A CD1   
4578 C  CD2   . PHE A 572 ? 0.5316 0.4988 0.6582 -0.0109 0.0615  -0.0374 572 PHE A CD2   
4579 C  CE1   . PHE A 572 ? 0.5437 0.5114 0.6733 -0.0048 0.0674  -0.0421 572 PHE A CE1   
4580 C  CE2   . PHE A 572 ? 0.5422 0.5051 0.6689 -0.0093 0.0596  -0.0412 572 PHE A CE2   
4581 C  CZ    . PHE A 572 ? 0.5422 0.5051 0.6703 -0.0063 0.0624  -0.0436 572 PHE A CZ    
4582 N  N     . THR A 573 ? 0.5207 0.5073 0.6469 -0.0124 0.076   -0.0238 573 THR A N     
4583 C  CA    . THR A 573 ? 0.5291 0.5203 0.6579 -0.0146 0.0771  -0.0186 573 THR A CA    
4584 C  C     . THR A 573 ? 0.5381 0.5284 0.6728 -0.0175 0.0727  -0.0163 573 THR A C     
4585 O  O     . THR A 573 ? 0.5399 0.5296 0.6812 -0.0171 0.0713  -0.0172 573 THR A O     
4586 C  CB    . THR A 573 ? 0.5374 0.5347 0.6724 -0.0131 0.0822  -0.0164 573 THR A CB    
4587 O  OG1   . THR A 573 ? 0.5517 0.5504 0.6796 -0.0108 0.0867  -0.0174 573 THR A OG1   
4588 C  CG2   . THR A 573 ? 0.5358 0.5378 0.6773 -0.0159 0.0822  -0.0106 573 THR A CG2   
4589 N  N     . PRO A 574 ? 0.5395 0.5295 0.6714 -0.0201 0.0704  -0.0133 574 PRO A N     
4590 C  CA    . PRO A 574 ? 0.5436 0.5322 0.6801 -0.0224 0.0662  -0.0111 574 PRO A CA    
4591 C  C     . PRO A 574 ? 0.5504 0.542  0.6969 -0.0226 0.0667  -0.0088 574 PRO A C     
4592 O  O     . PRO A 574 ? 0.5471 0.5431 0.6975 -0.0219 0.0704  -0.007  574 PRO A O     
4593 C  CB    . PRO A 574 ? 0.5526 0.5416 0.6849 -0.0247 0.0649  -0.0076 574 PRO A CB    
4594 C  CG    . PRO A 574 ? 0.559  0.548  0.6828 -0.0239 0.0673  -0.0089 574 PRO A CG    
4595 C  CD    . PRO A 574 ? 0.5351 0.5255 0.6591 -0.0209 0.0715  -0.0118 574 PRO A CD    
4596 N  N     . SER A 575 ? 0.5564 0.5455 0.7071 -0.0234 0.0632  -0.0087 575 SER A N     
4597 C  CA    . SER A 575 ? 0.5654 0.5564 0.7252 -0.0237 0.0631  -0.0066 575 SER A CA    
4598 C  C     . SER A 575 ? 0.579  0.5733 0.7418 -0.0256 0.0635  -0.0016 575 SER A C     
4599 O  O     . SER A 575 ? 0.5741 0.5724 0.7434 -0.0253 0.0659  0.0003  575 SER A O     
4600 C  CB    . SER A 575 ? 0.576  0.5632 0.7382 -0.0243 0.059   -0.0071 575 SER A CB    
4601 O  OG    . SER A 575 ? 0.6034 0.5879 0.7638 -0.0228 0.0585  -0.0113 575 SER A OG    
4602 N  N     . VAL A 576 ? 0.5941 0.5868 0.7523 -0.0276 0.061   0.0006  576 VAL A N     
4603 C  CA    . VAL A 576 ? 0.611  0.6058 0.7713 -0.0298 0.0603  0.0055  576 VAL A CA    
4604 C  C     . VAL A 576 ? 0.6386 0.633  0.7911 -0.0311 0.0601  0.0069  576 VAL A C     
4605 O  O     . VAL A 576 ? 0.6424 0.6341 0.7878 -0.0304 0.0595  0.004   576 VAL A O     
4606 C  CB    . VAL A 576 ? 0.6157 0.6075 0.7798 -0.0313 0.0558  0.0078  576 VAL A CB    
4607 C  CG1   . VAL A 576 ? 0.6175 0.6105 0.7904 -0.0306 0.0562  0.008   576 VAL A CG1   
4608 C  CG2   . VAL A 576 ? 0.624  0.6104 0.7827 -0.0312 0.0522  0.0055  576 VAL A CG2   
4609 N  N     . GLN A 577 ? 0.6554 0.6526 0.8095 -0.033  0.0604  0.0115  577 GLN A N     
4610 C  CA    . GLN A 577 ? 0.6814 0.6784 0.829  -0.0347 0.0598  0.0136  577 GLN A CA    
4611 C  C     . GLN A 577 ? 0.6955 0.6936 0.847  -0.0374 0.0575  0.0192  577 GLN A C     
4612 O  O     . GLN A 577 ? 0.6962 0.6969 0.8559 -0.0379 0.0578  0.0217  577 GLN A O     
4613 C  CB    . GLN A 577 ? 0.711  0.7117 0.8543 -0.0335 0.0648  0.0127  577 GLN A CB    
4614 C  CG    . GLN A 577 ? 0.7685 0.7758 0.9184 -0.0333 0.0692  0.016   577 GLN A CG    
4615 C  CD    . GLN A 577 ? 0.8435 0.854  0.9876 -0.0322 0.0739  0.0157  577 GLN A CD    
4616 O  OE1   . GLN A 577 ? 0.8717 0.8809 1.0105 -0.0296 0.0762  0.0112  577 GLN A OE1   
4617 N  NE2   . GLN A 577 ? 0.852  0.8665 0.9967 -0.0341 0.0754  0.0207  577 GLN A NE2   
4618 N  N     . ARG A 578 ? 0.7051 0.701  0.8508 -0.0393 0.0549  0.0213  578 ARG A N     
4619 C  CA    . ARG A 578 ? 0.7202 0.7164 0.8689 -0.0422 0.0522  0.0268  578 ARG A CA    
4620 C  C     . ARG A 578 ? 0.7364 0.7322 0.8779 -0.0439 0.0515  0.0289  578 ARG A C     
4621 O  O     . ARG A 578 ? 0.7415 0.7347 0.8751 -0.0429 0.0515  0.0257  578 ARG A O     
4622 C  CB    . ARG A 578 ? 0.7375 0.7282 0.888  -0.0429 0.0465  0.0274  578 ARG A CB    
4623 C  CG    . ARG A 578 ? 0.7736 0.7582 0.9164 -0.0424 0.0428  0.0247  578 ARG A CG    
4624 C  CD    . ARG A 578 ? 0.8079 0.7886 0.9478 -0.0447 0.0378  0.0283  578 ARG A CD    
4625 N  NE    . ARG A 578 ? 0.8424 0.817  0.9762 -0.0437 0.034   0.0258  578 ARG A NE    
4626 C  CZ    . ARG A 578 ? 0.8717 0.8415 1.0065 -0.0431 0.0302  0.0256  578 ARG A CZ    
4627 N  NH1   . ARG A 578 ? 0.8681 0.8381 1.0095 -0.0436 0.0292  0.0277  578 ARG A NH1   
4628 N  NH2   . ARG A 578 ? 0.8752 0.8402 1.0044 -0.0418 0.0273  0.0235  578 ARG A NH2   
4629 N  N     . LYS A 579 ? 0.7403 0.7385 0.8846 -0.0465 0.0508  0.0343  579 LYS A N     
4630 C  CA    . LYS A 579 ? 0.7543 0.7517 0.8921 -0.0485 0.0495  0.0369  579 LYS A CA    
4631 C  C     . LYS A 579 ? 0.7693 0.7594 0.9036 -0.0495 0.0429  0.037   579 LYS A C     
4632 O  O     . LYS A 579 ? 0.7741 0.762  0.9134 -0.0505 0.0393  0.0391  579 LYS A O     
4633 C  CB    . LYS A 579 ? 0.7753 0.778  0.9185 -0.0511 0.0509  0.0433  579 LYS A CB    
4634 C  CG    . LYS A 579 ? 0.8275 0.838  0.9764 -0.0497 0.0575  0.0439  579 LYS A CG    
4635 C  CD    . LYS A 579 ? 0.8843 0.8995 1.0438 -0.0518 0.0574  0.0499  579 LYS A CD    
4636 C  CE    . LYS A 579 ? 0.9337 0.9502 1.1018 -0.0502 0.0582  0.0483  579 LYS A CE    
4637 N  NZ    . LYS A 579 ? 0.9679 0.977  1.1346 -0.0497 0.0529  0.045   579 LYS A NZ    
4638 N  N     . ILE A 580 ? 0.7742 0.7603 0.8996 -0.0492 0.0412  0.0346  580 ILE A N     
4639 C  CA    . ILE A 580 ? 0.7845 0.7638 0.9061 -0.0497 0.0351  0.0345  580 ILE A CA    
4640 C  C     . ILE A 580 ? 0.7953 0.773  0.9183 -0.0527 0.031   0.0402  580 ILE A C     
4641 O  O     . ILE A 580 ? 0.8016 0.774  0.9251 -0.0531 0.026   0.0409  580 ILE A O     
4642 C  CB    . ILE A 580 ? 0.7931 0.7692 0.9055 -0.0486 0.0344  0.0312  580 ILE A CB    
4643 C  CG1   . ILE A 580 ? 0.8088 0.778  0.9177 -0.0481 0.0288  0.03    580 ILE A CG1   
4644 C  CG2   . ILE A 580 ? 0.7996 0.7774 0.9066 -0.0504 0.0355  0.0336  580 ILE A CG2   
4645 C  CD1   . ILE A 580 ? 0.825  0.7922 0.9376 -0.046  0.028   0.0272  580 ILE A CD1   
4646 N  N     . ALA A 581 ? 0.7938 0.7761 0.9178 -0.0549 0.0332  0.0443  581 ALA A N     
4647 C  CA    . ALA A 581 ? 0.8016 0.783  0.9275 -0.0582 0.0294  0.0502  581 ALA A CA    
4648 C  C     . ALA A 581 ? 0.8045 0.7874 0.9401 -0.0593 0.0282  0.0534  581 ALA A C     
4649 O  O     . ALA A 581 ? 0.8123 0.7905 0.9491 -0.0611 0.0225  0.0564  581 ALA A O     
4650 C  CB    . ALA A 581 ? 0.8038 0.7901 0.9278 -0.0602 0.0325  0.0538  581 ALA A CB    
4651 N  N     . GLY A 582 ? 0.7963 0.7852 0.9386 -0.0581 0.0333  0.0527  582 GLY A N     
4652 C  CA    . GLY A 582 ? 0.7945 0.7853 0.9468 -0.059  0.0323  0.0558  582 GLY A CA    
4653 C  C     . GLY A 582 ? 0.793  0.779  0.9467 -0.0569 0.0298  0.0519  582 GLY A C     
4654 O  O     . GLY A 582 ? 0.7989 0.7776 0.9488 -0.057  0.0241  0.0515  582 GLY A O     
4655 N  N     . GLY A 583 ? 0.7831 0.773  0.9414 -0.0547 0.0342  0.0491  583 GLY A N     
4656 C  CA    . GLY A 583 ? 0.7829 0.7688 0.9427 -0.0526 0.0325  0.0455  583 GLY A CA    
4657 C  C     . GLY A 583 ? 0.7736 0.7647 0.9417 -0.0512 0.0367  0.0445  583 GLY A C     
4658 O  O     . GLY A 583 ? 0.7682 0.7665 0.9401 -0.0511 0.0419  0.0456  583 GLY A O     
4659 N  N     . ASN A 584 ? 0.7693 0.7569 0.9402 -0.0499 0.0344  0.0424  584 ASN A N     
4660 C  CA    . ASN A 584 ? 0.7639 0.755  0.9423 -0.0483 0.0375  0.0409  584 ASN A CA    
4661 C  C     . ASN A 584 ? 0.752  0.7466 0.9281 -0.0456 0.0432  0.0362  584 ASN A C     
4662 O  O     . ASN A 584 ? 0.747  0.7463 0.9212 -0.0455 0.0474  0.0364  584 ASN A O     
4663 C  CB    . ASN A 584 ? 0.7774 0.7737 0.966  -0.0502 0.0383  0.046   584 ASN A CB    
4664 C  CG    . ASN A 584 ? 0.823  0.8147 1.0142 -0.0528 0.0317  0.0505  584 ASN A CG    
4665 O  OD1   . ASN A 584 ? 0.8405 0.8273 1.0258 -0.0544 0.0274  0.0521  584 ASN A OD1   
4666 N  ND2   . ASN A 584 ? 0.8318 0.8246 1.032  -0.0533 0.0305  0.0526  584 ASN A ND2   
4667 N  N     . TRP A 585 ? 0.7475 0.7391 0.923  -0.0434 0.0429  0.0318  585 TRP A N     
4668 C  CA    . TRP A 585 ? 0.7506 0.7443 0.924  -0.0407 0.0473  0.027   585 TRP A CA    
4669 C  C     . TRP A 585 ? 0.7454 0.7458 0.9268 -0.0398 0.0521  0.0276  585 TRP A C     
4670 O  O     . TRP A 585 ? 0.7451 0.7467 0.9346 -0.0403 0.0512  0.0299  585 TRP A O     
4671 C  CB    . TRP A 585 ? 0.7528 0.7415 0.9246 -0.0389 0.0452  0.0229  585 TRP A CB    
4672 C  CG    . TRP A 585 ? 0.7651 0.7481 0.9286 -0.0389 0.0417  0.0214  585 TRP A CG    
4673 C  CD1   . TRP A 585 ? 0.7796 0.757  0.9413 -0.0394 0.0367  0.0225  585 TRP A CD1   
4674 C  CD2   . TRP A 585 ? 0.7692 0.7515 0.9253 -0.0379 0.0429  0.0182  585 TRP A CD2   
4675 N  NE1   . TRP A 585 ? 0.7865 0.7601 0.9404 -0.0387 0.0351  0.0203  585 TRP A NE1   
4676 C  CE2   . TRP A 585 ? 0.7819 0.7585 0.9326 -0.0379 0.0386  0.0178  585 TRP A CE2   
4677 C  CE3   . TRP A 585 ? 0.776  0.7615 0.9292 -0.0368 0.047   0.0158  585 TRP A CE3   
4678 C  CZ2   . TRP A 585 ? 0.7909 0.7656 0.9344 -0.0372 0.0383  0.0152  585 TRP A CZ2   
4679 C  CZ3   . TRP A 585 ? 0.7887 0.7717 0.9342 -0.0362 0.0464  0.0131  585 TRP A CZ3   
4680 C  CH2   . TRP A 585 ? 0.792  0.7699 0.9332 -0.0365 0.0421  0.013   585 TRP A CH2   
4681 N  N     . GLU A 586 ? 0.7392 0.7437 0.918  -0.0383 0.0572  0.0256  586 GLU A N     
4682 C  CA    . GLU A 586 ? 0.7374 0.7481 0.9224 -0.0366 0.0625  0.0255  586 GLU A CA    
4683 C  C     . GLU A 586 ? 0.7362 0.7456 0.9173 -0.0334 0.0651  0.0194  586 GLU A C     
4684 O  O     . GLU A 586 ? 0.7438 0.7486 0.9172 -0.033  0.0632  0.0162  586 GLU A O     
4685 C  CB    . GLU A 586 ? 0.768  0.7849 0.9526 -0.0373 0.0666  0.0288  586 GLU A CB    
4686 C  CG    . GLU A 586 ? 0.8432 0.8584 1.0218 -0.04   0.0641  0.032   586 GLU A CG    
4687 C  CD    . GLU A 586 ? 0.9322 0.9516 1.1054 -0.0396 0.0687  0.0327  586 GLU A CD    
4688 O  OE1   . GLU A 586 ? 0.955  0.9717 1.1207 -0.0411 0.0667  0.0335  586 GLU A OE1   
4689 O  OE2   . GLU A 586 ? 0.9527 0.9778 1.1289 -0.0375 0.0744  0.0323  586 GLU A OE2   
4690 N  N     . PHE A 587 ? 0.7233 0.7367 0.9099 -0.0311 0.0691  0.0179  587 PHE A N     
4691 C  CA    . PHE A 587 ? 0.7209 0.7328 0.9037 -0.0281 0.0714  0.0122  587 PHE A CA    
4692 C  C     . PHE A 587 ? 0.7224 0.7349 0.896  -0.0272 0.0743  0.0106  587 PHE A C     
4693 O  O     . PHE A 587 ? 0.7194 0.7357 0.892  -0.0282 0.0766  0.014   587 PHE A O     
4694 C  CB    . PHE A 587 ? 0.7144 0.7304 0.905  -0.0257 0.0751  0.0113  587 PHE A CB    
4695 C  CG    . PHE A 587 ? 0.7172 0.7313 0.9155 -0.0258 0.0722  0.0111  587 PHE A CG    
4696 C  CD1   . PHE A 587 ? 0.7299 0.7378 0.9253 -0.026  0.0681  0.0083  587 PHE A CD1   
4697 C  CD2   . PHE A 587 ? 0.7194 0.7379 0.9278 -0.0255 0.0738  0.0136  587 PHE A CD2   
4698 C  CE1   . PHE A 587 ? 0.7356 0.7416 0.9375 -0.026  0.0656  0.0082  587 PHE A CE1   
4699 C  CE2   . PHE A 587 ? 0.7244 0.7408 0.9394 -0.0255 0.071   0.0134  587 PHE A CE2   
4700 C  CZ    . PHE A 587 ? 0.7253 0.7352 0.9367 -0.0258 0.0669  0.0106  587 PHE A CZ    
4701 N  N     . GLY A 588 ? 0.7286 0.737  0.8954 -0.0255 0.074   0.0056  588 GLY A N     
4702 C  CA    . GLY A 588 ? 0.7412 0.749  0.8985 -0.0245 0.0761  0.0034  588 GLY A CA    
4703 C  C     . GLY A 588 ? 0.7466 0.7598 0.9041 -0.0223 0.0821  0.0038  588 GLY A C     
4704 O  O     . GLY A 588 ? 0.746  0.7615 0.9088 -0.0199 0.085   0.0024  588 GLY A O     
4705 N  N     . ASN A 589 ? 0.7496 0.7649 0.9015 -0.0231 0.0841  0.0062  589 ASN A N     
4706 C  CA    . ASN A 589 ? 0.7554 0.7763 0.9071 -0.0211 0.0903  0.0074  589 ASN A CA    
4707 C  C     . ASN A 589 ? 0.7631 0.7814 0.9034 -0.0185 0.0928  0.0031  589 ASN A C     
4708 O  O     . ASN A 589 ? 0.763  0.7829 0.9025 -0.015  0.0971  0.0004  589 ASN A O     
4709 C  CB    . ASN A 589 ? 0.7699 0.7957 0.9241 -0.024  0.091   0.014   589 ASN A CB    
4710 C  CG    . ASN A 589 ? 0.811  0.8442 0.9672 -0.0225 0.0974  0.0168  589 ASN A CG    
4711 O  OD1   . ASN A 589 ? 0.822  0.8602 0.987  -0.0208 0.1007  0.018   589 ASN A OD1   
4712 N  ND2   . ASN A 589 ? 0.8245 0.8587 0.9728 -0.023  0.0995  0.0185  589 ASN A ND2   
4713 N  N     . LYS A 590 ? 0.7678 0.7817 0.8992 -0.0202 0.0897  0.0024  590 LYS A N     
4714 C  CA    . LYS A 590 ? 0.7779 0.7883 0.8975 -0.0182 0.0911  -0.0013 590 LYS A CA    
4715 C  C     . LYS A 590 ? 0.7855 0.7885 0.8999 -0.018  0.0865  -0.0063 590 LYS A C     
4716 O  O     . LYS A 590 ? 0.7888 0.789  0.9058 -0.0203 0.0816  -0.0058 590 LYS A O     
4717 C  CB    . LYS A 590 ? 0.8012 0.8129 0.9141 -0.0203 0.0917  0.0024  590 LYS A CB    
4718 C  CG    . LYS A 590 ? 0.8495 0.8604 0.9651 -0.0246 0.0867  0.0065  590 LYS A CG    
4719 C  CD    . LYS A 590 ? 0.9064 0.9179 1.0149 -0.0266 0.087   0.0099  590 LYS A CD    
4720 C  CE    . LYS A 590 ? 0.9506 0.9615 1.0624 -0.0306 0.0823  0.0144  590 LYS A CE    
4721 N  NZ    . LYS A 590 ? 0.9835 0.9921 1.0861 -0.0326 0.0805  0.016   590 LYS A NZ    
4722 N  N     . SER A 591 ? 0.7865 0.7862 0.8931 -0.015  0.088   -0.0111 591 SER A N     
4723 C  CA    . SER A 591 ? 0.7919 0.7845 0.8932 -0.0146 0.0836  -0.0159 591 SER A CA    
4724 C  C     . SER A 591 ? 0.7944 0.7831 0.8864 -0.0165 0.0806  -0.0157 591 SER A C     
4725 O  O     . SER A 591 ? 0.7973 0.7876 0.883  -0.0167 0.0831  -0.0138 591 SER A O     
4726 C  CB    . SER A 591 ? 0.8095 0.7994 0.9062 -0.0105 0.0861  -0.021  591 SER A CB    
4727 O  OG    . SER A 591 ? 0.8327 0.82   0.9349 -0.0096 0.0837  -0.0242 591 SER A OG    
4728 N  N     . LEU A 592 ? 0.7919 0.7758 0.8831 -0.0179 0.0752  -0.0174 592 LEU A N     
4729 C  CA    . LEU A 592 ? 0.7974 0.7774 0.8803 -0.0197 0.0718  -0.0174 592 LEU A CA    
4730 C  C     . LEU A 592 ? 0.8019 0.7763 0.8754 -0.0176 0.0709  -0.0224 592 LEU A C     
4731 O  O     . LEU A 592 ? 0.805  0.7775 0.8798 -0.0153 0.0712  -0.0261 592 LEU A O     
4732 C  CB    . LEU A 592 ? 0.7988 0.7769 0.8859 -0.0223 0.0664  -0.0161 592 LEU A CB    
4733 C  CG    . LEU A 592 ? 0.8148 0.7959 0.9052 -0.0252 0.0655  -0.0109 592 LEU A CG    
4734 C  CD1   . LEU A 592 ? 0.8179 0.8046 0.9172 -0.0251 0.0689  -0.0079 592 LEU A CD1   
4735 C  CD2   . LEU A 592 ? 0.8203 0.7985 0.9131 -0.027  0.0602  -0.0104 592 LEU A CD2   
4736 N  N     . VAL A 593 ? 0.8003 0.7718 0.8642 -0.0184 0.0696  -0.0223 593 VAL A N     
4737 C  CA    . VAL A 593 ? 0.8075 0.773  0.8614 -0.0166 0.0683  -0.0267 593 VAL A CA    
4738 C  C     . VAL A 593 ? 0.8051 0.7655 0.8561 -0.0186 0.062   -0.0278 593 VAL A C     
4739 O  O     . VAL A 593 ? 0.8086 0.7694 0.8584 -0.0211 0.0599  -0.0248 593 VAL A O     
4740 C  CB    . VAL A 593 ? 0.8234 0.7894 0.8673 -0.0152 0.0725  -0.0262 593 VAL A CB    
4741 C  CG1   . VAL A 593 ? 0.8387 0.7976 0.8703 -0.0141 0.07    -0.0299 593 VAL A CG1   
4742 C  CG2   . VAL A 593 ? 0.8279 0.7982 0.874  -0.012  0.0789  -0.0265 593 VAL A CG2   
4743 N  N     . PRO A 594 ? 0.796  0.7515 0.8463 -0.0175 0.0589  -0.032  594 PRO A N     
4744 C  CA    . PRO A 594 ? 0.7933 0.7444 0.8421 -0.0193 0.0529  -0.0327 594 PRO A CA    
4745 C  C     . PRO A 594 ? 0.7948 0.7425 0.833  -0.0204 0.0508  -0.0323 594 PRO A C     
4746 O  O     . PRO A 594 ? 0.7968 0.7434 0.8358 -0.0227 0.0466  -0.0308 594 PRO A O     
4747 C  CB    . PRO A 594 ? 0.8022 0.7489 0.8519 -0.0177 0.0504  -0.0371 594 PRO A CB    
4748 C  CG    . PRO A 594 ? 0.8079 0.7553 0.8564 -0.0146 0.0551  -0.0393 594 PRO A CG    
4749 C  CD    . PRO A 594 ? 0.7868 0.7408 0.8386 -0.0145 0.0605  -0.0358 594 PRO A CD    
4750 N  N     . ASN A 595 ? 0.7916 0.7377 0.82   -0.0187 0.0539  -0.0335 595 ASN A N     
4751 C  CA    . ASN A 595 ? 0.7969 0.7396 0.8147 -0.0197 0.052   -0.0329 595 ASN A CA    
4752 C  C     . ASN A 595 ? 0.787  0.7337 0.8064 -0.0225 0.0522  -0.0279 595 ASN A C     
4753 O  O     . ASN A 595 ? 0.7926 0.7363 0.8056 -0.0241 0.0491  -0.027  595 ASN A O     
4754 C  CB    . ASN A 595 ? 0.8211 0.7607 0.827  -0.017  0.0553  -0.0353 595 ASN A CB    
4755 C  CG    . ASN A 595 ? 0.8718 0.807  0.866  -0.0182 0.0528  -0.0349 595 ASN A CG    
4756 O  OD1   . ASN A 595 ? 0.8917 0.8218 0.8834 -0.0195 0.047   -0.0362 595 ASN A OD1   
4757 N  ND2   . ASN A 595 ? 0.8802 0.8175 0.8677 -0.0178 0.0571  -0.0326 595 ASN A ND2   
4758 N  N     . ASP A 596 ? 0.7702 0.7231 0.7982 -0.0231 0.0554  -0.0246 596 ASP A N     
4759 C  CA    . ASP A 596 ? 0.7628 0.719  0.793  -0.0259 0.0549  -0.0197 596 ASP A CA    
4760 C  C     . ASP A 596 ? 0.7479 0.7022 0.7824 -0.0281 0.0491  -0.019  596 ASP A C     
4761 O  O     . ASP A 596 ? 0.75   0.7057 0.7852 -0.0303 0.0476  -0.0154 596 ASP A O     
4762 C  CB    . ASP A 596 ? 0.7851 0.7481 0.8244 -0.026  0.0591  -0.0165 596 ASP A CB    
4763 C  CG    . ASP A 596 ? 0.8554 0.8219 0.8921 -0.024  0.0654  -0.0159 596 ASP A CG    
4764 O  OD1   . ASP A 596 ? 0.8758 0.8404 0.9023 -0.0232 0.0671  -0.0165 596 ASP A OD1   
4765 O  OD2   . ASP A 596 ? 0.8779 0.8492 0.9229 -0.0232 0.0688  -0.0147 596 ASP A OD2   
4766 N  N     . PHE A 597 ? 0.7301 0.6815 0.7677 -0.0274 0.0457  -0.0221 597 PHE A N     
4767 C  CA    . PHE A 597 ? 0.7164 0.6668 0.7592 -0.029  0.0408  -0.0213 597 PHE A CA    
4768 C  C     . PHE A 597 ? 0.7028 0.6479 0.7417 -0.0289 0.0362  -0.0243 597 PHE A C     
4769 O  O     . PHE A 597 ? 0.7053 0.6473 0.7401 -0.0273 0.0364  -0.0278 597 PHE A O     
4770 C  CB    . PHE A 597 ? 0.7109 0.6644 0.7648 -0.0286 0.0414  -0.021  597 PHE A CB    
4771 C  CG    . PHE A 597 ? 0.7168 0.6753 0.7757 -0.029  0.0453  -0.0178 597 PHE A CG    
4772 C  CD1   . PHE A 597 ? 0.7243 0.6855 0.7845 -0.0273 0.0501  -0.0186 597 PHE A CD1   
4773 C  CD2   . PHE A 597 ? 0.7261 0.6865 0.7884 -0.0309 0.0439  -0.014  597 PHE A CD2   
4774 C  CE1   . PHE A 597 ? 0.729  0.6951 0.7944 -0.0278 0.0534  -0.0152 597 PHE A CE1   
4775 C  CE2   . PHE A 597 ? 0.7305 0.6952 0.7975 -0.0314 0.0469  -0.0108 597 PHE A CE2   
4776 C  CZ    . PHE A 597 ? 0.7247 0.6924 0.7935 -0.03   0.0516  -0.0113 597 PHE A CZ    
4777 N  N     . ILE A 598 ? 0.6854 0.6296 0.7265 -0.0304 0.0317  -0.0228 598 ILE A N     
4778 C  CA    . ILE A 598 ? 0.6761 0.6163 0.7161 -0.0307 0.0267  -0.0248 598 ILE A CA    
4779 C  C     . ILE A 598 ? 0.6572 0.5993 0.7078 -0.0304 0.0256  -0.025  598 ILE A C     
4780 O  O     . ILE A 598 ? 0.6564 0.6017 0.7131 -0.031  0.0257  -0.0222 598 ILE A O     
4781 C  CB    . ILE A 598 ? 0.6832 0.6218 0.7197 -0.0324 0.0229  -0.0225 598 ILE A CB    
4782 C  CG1   . ILE A 598 ? 0.7013 0.6386 0.7278 -0.033  0.0244  -0.0214 598 ILE A CG1   
4783 C  CG2   . ILE A 598 ? 0.689  0.624  0.7255 -0.0327 0.0176  -0.0242 598 ILE A CG2   
4784 C  CD1   . ILE A 598 ? 0.7255 0.6584 0.7424 -0.032  0.0246  -0.0246 598 ILE A CD1   
4785 N  N     . LEU A 599 ? 0.6394 0.5795 0.692  -0.0293 0.0244  -0.028  599 LEU A N     
4786 C  CA    . LEU A 599 ? 0.6254 0.5675 0.6881 -0.0291 0.0234  -0.0279 599 LEU A CA    
4787 C  C     . LEU A 599 ? 0.6163 0.5562 0.6811 -0.0299 0.0181  -0.0282 599 LEU A C     
4788 O  O     . LEU A 599 ? 0.6214 0.5571 0.6814 -0.0298 0.0154  -0.0306 599 LEU A O     
4789 C  CB    . LEU A 599 ? 0.627  0.569  0.6924 -0.0276 0.0258  -0.0306 599 LEU A CB    
4790 C  CG    . LEU A 599 ? 0.6444 0.5889 0.7087 -0.0264 0.0312  -0.0306 599 LEU A CG    
4791 C  CD1   . LEU A 599 ? 0.6476 0.5913 0.7141 -0.0246 0.033   -0.0337 599 LEU A CD1   
4792 C  CD2   . LEU A 599 ? 0.6506 0.6    0.7213 -0.0272 0.0333  -0.027  599 LEU A CD2   
4793 N  N     . LEU A 600 ? 0.6005 0.5431 0.6723 -0.0305 0.0166  -0.0257 600 LEU A N     
4794 C  CA    . LEU A 600 ? 0.5939 0.5355 0.6694 -0.031  0.012   -0.0254 600 LEU A CA    
4795 C  C     . LEU A 600 ? 0.5787 0.5236 0.6646 -0.0306 0.0122  -0.0243 600 LEU A C     
4796 O  O     . LEU A 600 ? 0.5751 0.523  0.6647 -0.03   0.0154  -0.0231 600 LEU A O     
4797 C  CB    . LEU A 600 ? 0.6001 0.5417 0.6732 -0.0319 0.0094  -0.0229 600 LEU A CB    
4798 C  CG    . LEU A 600 ? 0.6261 0.564  0.689  -0.0327 0.008   -0.0235 600 LEU A CG    
4799 C  CD1   . LEU A 600 ? 0.6323 0.5705 0.6945 -0.0335 0.0052  -0.0209 600 LEU A CD1   
4800 C  CD2   . LEU A 600 ? 0.6394 0.5727 0.6979 -0.0328 0.005   -0.0265 600 LEU A CD2   
4801 N  N     . SER A 601 ? 0.5706 0.5149 0.6611 -0.0308 0.0088  -0.0246 601 SER A N     
4802 C  CA    . SER A 601 ? 0.5671 0.5147 0.6674 -0.0304 0.0089  -0.0233 601 SER A CA    
4803 C  C     . SER A 601 ? 0.5654 0.5146 0.6701 -0.0308 0.0056  -0.0207 601 SER A C     
4804 O  O     . SER A 601 ? 0.5738 0.5209 0.6752 -0.0316 0.0021  -0.0208 601 SER A O     
4805 C  CB    . SER A 601 ? 0.5833 0.5293 0.6869 -0.0303 0.008   -0.0256 601 SER A CB    
4806 O  OG    . SER A 601 ? 0.6106 0.553  0.7117 -0.0312 0.0036  -0.0269 601 SER A OG    
4807 N  N     . ALA A 602 ? 0.5538 0.5068 0.6658 -0.0301 0.0068  -0.0184 602 ALA A N     
4808 C  CA    . ALA A 602 ? 0.5477 0.503  0.6644 -0.0299 0.0043  -0.0157 602 ALA A CA    
4809 C  C     . ALA A 602 ? 0.5379 0.4966 0.6639 -0.0292 0.0049  -0.014  602 ALA A C     
4810 O  O     . ALA A 602 ? 0.5363 0.4963 0.665  -0.0285 0.0079  -0.0142 602 ALA A O     
4811 C  CB    . ALA A 602 ? 0.5507 0.5068 0.6642 -0.0292 0.0052  -0.0136 602 ALA A CB    
4812 N  N     . GLY A 603 ? 0.5335 0.4938 0.6648 -0.0293 0.0019  -0.0123 603 GLY A N     
4813 C  CA    . GLY A 603 ? 0.5366 0.5008 0.6772 -0.0286 0.0024  -0.0102 603 GLY A CA    
4814 C  C     . GLY A 603 ? 0.5402 0.5078 0.684  -0.0273 0.002   -0.0068 603 GLY A C     
4815 O  O     . GLY A 603 ? 0.5438 0.5111 0.6867 -0.0276 -0.0009 -0.006  603 GLY A O     
4816 N  N     . ALA A 604 ? 0.5384 0.5087 0.6853 -0.0255 0.005   -0.005  604 ALA A N     
4817 C  CA    . ALA A 604 ? 0.5437 0.5169 0.693  -0.0236 0.0052  -0.002  604 ALA A CA    
4818 C  C     . ALA A 604 ? 0.5412 0.5188 0.6997 -0.0225 0.0059  0.0007  604 ALA A C     
4819 O  O     . ALA A 604 ? 0.5412 0.5194 0.7029 -0.0227 0.0078  0.0004  604 ALA A O     
4820 C  CB    . ALA A 604 ? 0.5511 0.5231 0.6951 -0.0221 0.0077  -0.0018 604 ALA A CB    
4821 N  N     . PHE A 605 ? 0.5398 0.5206 0.7026 -0.0214 0.0046  0.0034  605 PHE A N     
4822 C  CA    . PHE A 605 ? 0.5451 0.5308 0.7171 -0.0203 0.0053  0.0066  605 PHE A CA    
4823 C  C     . PHE A 605 ? 0.5559 0.5452 0.7307 -0.0179 0.0051  0.0098  605 PHE A C     
4824 O  O     . PHE A 605 ? 0.5598 0.5475 0.7298 -0.0175 0.0035  0.0095  605 PHE A O     
4825 C  CB    . PHE A 605 ? 0.5404 0.527  0.7187 -0.0229 0.0024  0.0065  605 PHE A CB    
4826 C  CG    . PHE A 605 ? 0.5491 0.5338 0.7255 -0.0246 -0.002  0.0057  605 PHE A CG    
4827 C  CD1   . PHE A 605 ? 0.5568 0.5448 0.7378 -0.0239 -0.0041 0.0087  605 PHE A CD1   
4828 C  CD2   . PHE A 605 ? 0.5649 0.5444 0.7348 -0.0267 -0.0039 0.0021  605 PHE A CD2   
4829 C  CE1   . PHE A 605 ? 0.5679 0.5538 0.747  -0.0255 -0.0085 0.008   605 PHE A CE1   
4830 C  CE2   . PHE A 605 ? 0.5767 0.5537 0.7439 -0.0282 -0.0081 0.0013  605 PHE A CE2   
4831 C  CZ    . PHE A 605 ? 0.571  0.5512 0.743  -0.0277 -0.0106 0.0043  605 PHE A CZ    
4832 N  N     . ILE A 606 ? 0.558  0.5524 0.7406 -0.0163 0.0067  0.0131  606 ILE A N     
4833 C  CA    . ILE A 606 ? 0.5676 0.5662 0.754  -0.0136 0.0068  0.0165  606 ILE A CA    
4834 C  C     . ILE A 606 ? 0.5747 0.5771 0.7696 -0.0152 0.0034  0.0187  606 ILE A C     
4835 O  O     . ILE A 606 ? 0.5698 0.5742 0.7714 -0.0171 0.0028  0.0195  606 ILE A O     
4836 C  CB    . ILE A 606 ? 0.5739 0.5756 0.7625 -0.0101 0.011   0.0191  606 ILE A CB    
4837 C  CG1   . ILE A 606 ? 0.5887 0.5859 0.7679 -0.0081 0.0132  0.0172  606 ILE A CG1   
4838 C  CG2   . ILE A 606 ? 0.5799 0.5871 0.7743 -0.0072 0.0112  0.023   606 ILE A CG2   
4839 C  CD1   . ILE A 606 ? 0.6027 0.6013 0.7826 -0.0052 0.017   0.0189  606 ILE A CD1   
4840 N  N     . ASP A 607 ? 0.5858 0.5888 0.7804 -0.0147 0.0009  0.0196  607 ASP A N     
4841 C  CA    . ASP A 607 ? 0.5995 0.6062 0.8026 -0.0162 -0.0028 0.0221  607 ASP A CA    
4842 C  C     . ASP A 607 ? 0.6121 0.623  0.8184 -0.0132 -0.0029 0.0253  607 ASP A C     
4843 O  O     . ASP A 607 ? 0.6172 0.625  0.8166 -0.0121 -0.0039 0.0239  607 ASP A O     
4844 C  CB    . ASP A 607 ? 0.625  0.6267 0.8242 -0.0198 -0.0076 0.0191  607 ASP A CB    
4845 C  CG    . ASP A 607 ? 0.6756 0.6805 0.8835 -0.0215 -0.0121 0.0218  607 ASP A CG    
4846 O  OD1   . ASP A 607 ? 0.681  0.6898 0.8982 -0.0226 -0.0124 0.0242  607 ASP A OD1   
4847 O  OD2   . ASP A 607 ? 0.7    0.7034 0.9055 -0.0218 -0.0155 0.0216  607 ASP A OD2   
4848 N  N     . TYR A 608 ? 0.6161 0.634  0.8332 -0.012  -0.0023 0.0297  608 TYR A N     
4849 C  CA    . TYR A 608 ? 0.6296 0.6523 0.8509 -0.0088 -0.0022 0.0332  608 TYR A CA    
4850 C  C     . TYR A 608 ? 0.6394 0.6638 0.8668 -0.0111 -0.0075 0.0347  608 TYR A C     
4851 O  O     . TYR A 608 ? 0.6334 0.6647 0.872  -0.0106 -0.008  0.0392  608 TYR A O     
4852 C  CB    . TYR A 608 ? 0.6253 0.6551 0.8544 -0.0054 0.0023  0.0375  608 TYR A CB    
4853 C  CG    . TYR A 608 ? 0.6357 0.6631 0.8575 -0.0025 0.0072  0.036   608 TYR A CG    
4854 C  CD1   . TYR A 608 ? 0.6465 0.6714 0.8604 0.0013  0.009   0.0351  608 TYR A CD1   
4855 C  CD2   . TYR A 608 ? 0.6473 0.6743 0.8699 -0.0038 0.0095  0.0355  608 TYR A CD2   
4856 C  CE1   . TYR A 608 ? 0.661  0.683  0.868  0.0039  0.013   0.0338  608 TYR A CE1   
4857 C  CE2   . TYR A 608 ? 0.6614 0.6861 0.8776 -0.0011 0.0137  0.0344  608 TYR A CE2   
4858 C  CZ    . TYR A 608 ? 0.6745 0.6965 0.8827 0.0026  0.0153  0.0335  608 TYR A CZ    
4859 O  OH    . TYR A 608 ? 0.697  0.7158 0.8984 0.0051  0.0188  0.0324  608 TYR A OH    
4860 N  N     . ASP A 609 ? 0.6524 0.6704 0.8723 -0.0136 -0.0115 0.0312  609 ASP A N     
4861 C  CA    . ASP A 609 ? 0.6648 0.6823 0.8876 -0.016  -0.0172 0.0317  609 ASP A CA    
4862 C  C     . ASP A 609 ? 0.6703 0.6909 0.9038 -0.0193 -0.0206 0.0341  609 ASP A C     
4863 O  O     . ASP A 609 ? 0.6686 0.6913 0.9083 -0.0205 -0.025  0.0364  609 ASP A O     
4864 C  CB    . ASP A 609 ? 0.6878 0.7089 0.9132 -0.0129 -0.0178 0.0345  609 ASP A CB    
4865 C  CG    . ASP A 609 ? 0.7615 0.7781 0.9755 -0.0101 -0.0158 0.0319  609 ASP A CG    
4866 O  OD1   . ASP A 609 ? 0.7803 0.7899 0.9838 -0.0119 -0.0162 0.0277  609 ASP A OD1   
4867 O  OD2   . ASP A 609 ? 0.7903 0.8103 1.0059 -0.006  -0.0139 0.0343  609 ASP A OD2   
4868 N  N     . ASN A 610 ? 0.6763 0.6967 0.9118 -0.0209 -0.019  0.0335  610 ASN A N     
4869 C  CA    . ASN A 610 ? 0.686  0.7086 0.9313 -0.0243 -0.0226 0.0356  610 ASN A CA    
4870 C  C     . ASN A 610 ? 0.6993 0.7138 0.9384 -0.0285 -0.0276 0.0313  610 ASN A C     
4871 O  O     . ASN A 610 ? 0.696  0.7106 0.9416 -0.0315 -0.031  0.0323  610 ASN A O     
4872 C  CB    . ASN A 610 ? 0.6985 0.7264 0.9517 -0.0238 -0.0187 0.0383  610 ASN A CB    
4873 C  CG    . ASN A 610 ? 0.7503 0.7766 0.9962 -0.0213 -0.0127 0.0362  610 ASN A CG    
4874 O  OD1   . ASN A 610 ? 0.7654 0.7953 1.011  -0.0173 -0.0083 0.038   610 ASN A OD1   
4875 N  ND2   . ASN A 610 ? 0.7663 0.7869 1.0063 -0.0234 -0.0126 0.0323  610 ASN A ND2   
4876 N  N     . LEU A 611 ? 0.7104 0.7177 0.9367 -0.0286 -0.0282 0.0267  611 LEU A N     
4877 C  CA    . LEU A 611 ? 0.7231 0.7223 0.9417 -0.032  -0.0324 0.0224  611 LEU A CA    
4878 C  C     . LEU A 611 ? 0.7309 0.7268 0.9465 -0.0333 -0.0381 0.0219  611 LEU A C     
4879 O  O     . LEU A 611 ? 0.7309 0.7261 0.941  -0.0315 -0.0374 0.0215  611 LEU A O     
4880 C  CB    . LEU A 611 ? 0.731  0.7244 0.9372 -0.0314 -0.0289 0.0175  611 LEU A CB    
4881 C  CG    . LEU A 611 ? 0.7492 0.7441 0.9568 -0.0307 -0.0241 0.0171  611 LEU A CG    
4882 C  CD1   . LEU A 611 ? 0.7646 0.7542 0.9603 -0.03   -0.0208 0.0127  611 LEU A CD1   
4883 C  CD2   . LEU A 611 ? 0.7541 0.7484 0.9677 -0.0334 -0.0267 0.0172  611 LEU A CD2   
4884 N  N     . THR A 612 ? 0.734  0.7271 0.9527 -0.0366 -0.0441 0.0219  612 THR A N     
4885 C  CA    . THR A 612 ? 0.7452 0.734  0.961  -0.0384 -0.0504 0.0214  612 THR A CA    
4886 C  C     . THR A 612 ? 0.7624 0.7412 0.9634 -0.04   -0.0521 0.0155  612 THR A C     
4887 O  O     . THR A 612 ? 0.7632 0.7392 0.9579 -0.0396 -0.0483 0.0124  612 THR A O     
4888 C  CB    . THR A 612 ? 0.7526 0.7437 0.9802 -0.0412 -0.0564 0.0248  612 THR A CB    
4889 O  OG1   . THR A 612 ? 0.7652 0.7515 0.9913 -0.0437 -0.0581 0.0223  612 THR A OG1   
4890 C  CG2   . THR A 612 ? 0.7485 0.7502 0.9913 -0.0396 -0.0541 0.0309  612 THR A CG2   
4891 N  N     . GLU A 613 ? 0.7735 0.7468 0.9688 -0.0416 -0.0578 0.0142  613 GLU A N     
4892 C  CA    . GLU A 613 ? 0.7913 0.7549 0.9723 -0.043  -0.0596 0.0091  613 GLU A CA    
4893 C  C     . GLU A 613 ? 0.795  0.7543 0.9751 -0.0449 -0.0608 0.0065  613 GLU A C     
4894 O  O     . GLU A 613 ? 0.8016 0.7556 0.9712 -0.0446 -0.0581 0.0023  613 GLU A O     
4895 C  CB    . GLU A 613 ? 0.8286 0.7873 1.0058 -0.0448 -0.0667 0.0089  613 GLU A CB    
4896 C  CG    . GLU A 613 ? 0.8932 0.8528 1.0664 -0.0431 -0.0661 0.0098  613 GLU A CG    
4897 C  CD    . GLU A 613 ? 0.9724 0.9256 1.1395 -0.0451 -0.0732 0.0089  613 GLU A CD    
4898 O  OE1   . GLU A 613 ? 0.9902 0.9357 1.1504 -0.0473 -0.0772 0.0058  613 GLU A OE1   
4899 O  OE2   . GLU A 613 ? 0.9948 0.9502 1.1636 -0.0442 -0.0748 0.0112  613 GLU A OE2   
4900 N  N     . ASN A 614 ? 0.7883 0.7498 0.9794 -0.0467 -0.0649 0.0093  614 ASN A N     
4901 C  CA    . ASN A 614 ? 0.795  0.7525 0.9867 -0.0486 -0.0669 0.0074  614 ASN A CA    
4902 C  C     . ASN A 614 ? 0.7966 0.7572 0.9893 -0.047  -0.06   0.0065  614 ASN A C     
4903 O  O     . ASN A 614 ? 0.802  0.757  0.988  -0.0475 -0.0593 0.0026  614 ASN A O     
4904 C  CB    . ASN A 614 ? 0.8032 0.7636 1.0084 -0.051  -0.0728 0.0116  614 ASN A CB    
4905 C  CG    . ASN A 614 ? 0.8458 0.7983 1.0473 -0.0538 -0.0815 0.0103  614 ASN A CG    
4906 O  OD1   . ASN A 614 ? 0.8641 0.8085 1.0593 -0.0554 -0.0848 0.0067  614 ASN A OD1   
4907 N  ND2   . ASN A 614 ? 0.8523 0.8066 1.0576 -0.0543 -0.0856 0.0132  614 ASN A ND2   
4908 N  N     . ASP A 615 ? 0.7886 0.7579 0.9893 -0.0449 -0.0548 0.0101  615 ASP A N     
4909 C  CA    . ASP A 615 ? 0.7895 0.7621 0.9915 -0.0433 -0.0484 0.0097  615 ASP A CA    
4910 C  C     . ASP A 615 ? 0.7921 0.7597 0.9806 -0.0419 -0.0442 0.0049  615 ASP A C     
4911 O  O     . ASP A 615 ? 0.7961 0.7609 0.9813 -0.042  -0.0419 0.0022  615 ASP A O     
4912 C  CB    . ASP A 615 ? 0.8064 0.7887 1.0181 -0.0409 -0.0439 0.0145  615 ASP A CB    
4913 C  CG    . ASP A 615 ? 0.8602 0.849  1.087  -0.042  -0.0462 0.0198  615 ASP A CG    
4914 O  OD1   . ASP A 615 ? 0.8708 0.8569 1.1014 -0.0448 -0.0507 0.0197  615 ASP A OD1   
4915 O  OD2   . ASP A 615 ? 0.8828 0.8796 1.1176 -0.04   -0.0435 0.0242  615 ASP A OD2   
4916 N  N     . TYR A 616 ? 0.7884 0.7544 0.9691 -0.0408 -0.0436 0.004   616 TYR A N     
4917 C  CA    . TYR A 616 ? 0.7939 0.7554 0.962  -0.0397 -0.0399 -0.0001 616 TYR A CA    
4918 C  C     . TYR A 616 ? 0.791  0.7443 0.9502 -0.0414 -0.0425 -0.0046 616 TYR A C     
4919 O  O     . TYR A 616 ? 0.797  0.7479 0.9502 -0.0407 -0.0387 -0.0076 616 TYR A O     
4920 C  CB    . TYR A 616 ? 0.8003 0.7614 0.9621 -0.0385 -0.0397 0.0002  616 TYR A CB    
4921 C  CG    . TYR A 616 ? 0.8117 0.7794 0.9776 -0.0358 -0.0348 0.003   616 TYR A CG    
4922 C  CD1   . TYR A 616 ? 0.8268 0.7953 0.9894 -0.0341 -0.029  0.0018  616 TYR A CD1   
4923 C  CD2   . TYR A 616 ? 0.8215 0.7943 0.9946 -0.0348 -0.0362 0.0069  616 TYR A CD2   
4924 C  CE1   . TYR A 616 ? 0.8371 0.8107 1.0027 -0.0315 -0.0249 0.0042  616 TYR A CE1   
4925 C  CE2   . TYR A 616 ? 0.8317 0.8099 1.0079 -0.0319 -0.0318 0.0093  616 TYR A CE2   
4926 C  CZ    . TYR A 616 ? 0.8459 0.8241 1.0179 -0.0302 -0.0263 0.0078  616 TYR A CZ    
4927 O  OH    . TYR A 616 ? 0.8653 0.848  1.0395 -0.0272 -0.0223 0.0101  616 TYR A OH    
4928 N  N     . GLU A 617 ? 0.7788 0.7276 0.9375 -0.0435 -0.0492 -0.0049 617 GLU A N     
4929 C  CA    . GLU A 617 ? 0.776  0.7161 0.9259 -0.0449 -0.0525 -0.0091 617 GLU A CA    
4930 C  C     . GLU A 617 ? 0.7573 0.6968 0.911  -0.0452 -0.0513 -0.0104 617 GLU A C     
4931 O  O     . GLU A 617 ? 0.7616 0.6953 0.9064 -0.0449 -0.0502 -0.0146 617 GLU A O     
4932 C  CB    . GLU A 617 ? 0.8125 0.7483 0.9627 -0.0471 -0.0606 -0.0085 617 GLU A CB    
4933 C  CG    . GLU A 617 ? 0.8967 0.822  1.033  -0.0479 -0.064  -0.0132 617 GLU A CG    
4934 C  CD    . GLU A 617 ? 1.0041 0.9245 1.1404 -0.0501 -0.0725 -0.0125 617 GLU A CD    
4935 O  OE1   . GLU A 617 ? 1.0292 0.9406 1.1571 -0.0511 -0.0768 -0.0161 617 GLU A OE1   
4936 O  OE2   . GLU A 617 ? 1.0376 0.9629 1.1823 -0.0507 -0.0751 -0.0084 617 GLU A OE2   
4937 N  N     . LYS A 618 ? 0.7355 0.6812 0.9023 -0.0456 -0.0514 -0.0066 618 LYS A N     
4938 C  CA    . LYS A 618 ? 0.7249 0.6706 0.8965 -0.0461 -0.0504 -0.0073 618 LYS A CA    
4939 C  C     . LYS A 618 ? 0.703  0.6511 0.8718 -0.0439 -0.0429 -0.0087 618 LYS A C     
4940 O  O     . LYS A 618 ? 0.7017 0.646  0.867  -0.0438 -0.0417 -0.0119 618 LYS A O     
4941 C  CB    . LYS A 618 ? 0.7494 0.701  0.936  -0.0475 -0.0531 -0.0023 618 LYS A CB    
4942 C  CG    . LYS A 618 ? 0.8078 0.758  0.9993 -0.0485 -0.0538 -0.0029 618 LYS A CG    
4943 C  CD    . LYS A 618 ? 0.867  0.807  1.0508 -0.0501 -0.0594 -0.0073 618 LYS A CD    
4944 C  CE    . LYS A 618 ? 0.9035 0.8412 1.0902 -0.0506 -0.0594 -0.0086 618 LYS A CE    
4945 N  NZ    . LYS A 618 ? 0.9307 0.8577 1.1086 -0.0516 -0.0648 -0.0132 618 LYS A NZ    
4946 N  N     . ILE A 619 ? 0.6858 0.6396 0.8556 -0.042  -0.038  -0.0067 619 ILE A N     
4947 C  CA    . ILE A 619 ? 0.6781 0.6339 0.845  -0.04   -0.0313 -0.008  619 ILE A CA    
4948 C  C     . ILE A 619 ? 0.6774 0.6265 0.8312 -0.0396 -0.0299 -0.0129 619 ILE A C     
4949 O  O     . ILE A 619 ? 0.6816 0.6293 0.8332 -0.0389 -0.0268 -0.0152 619 ILE A O     
4950 C  CB    . ILE A 619 ? 0.6777 0.6399 0.8472 -0.038  -0.0271 -0.0049 619 ILE A CB    
4951 C  CG1   . ILE A 619 ? 0.6776 0.647  0.8599 -0.0379 -0.0278 0.0002  619 ILE A CG1   
4952 C  CG2   . ILE A 619 ? 0.6849 0.6481 0.8508 -0.0362 -0.0208 -0.0063 619 ILE A CG2   
4953 C  CD1   . ILE A 619 ? 0.6857 0.6605 0.8697 -0.0356 -0.0246 0.0031  619 ILE A CD1   
4954 N  N     . PHE A 620 ? 0.6711 0.6161 0.8165 -0.0399 -0.0324 -0.0143 620 PHE A N     
4955 C  CA    . PHE A 620 ? 0.6755 0.6143 0.8082 -0.0395 -0.0311 -0.0186 620 PHE A CA    
4956 C  C     . PHE A 620 ? 0.6817 0.6143 0.8112 -0.0402 -0.0334 -0.0221 620 PHE A C     
4957 O  O     . PHE A 620 ? 0.6876 0.6174 0.8102 -0.039  -0.03   -0.0253 620 PHE A O     
4958 C  CB    . PHE A 620 ? 0.6748 0.6101 0.7994 -0.04   -0.0342 -0.0191 620 PHE A CB    
4959 C  CG    . PHE A 620 ? 0.6802 0.6194 0.8033 -0.0388 -0.0311 -0.0171 620 PHE A CG    
4960 C  CD1   . PHE A 620 ? 0.6903 0.6314 0.8099 -0.0373 -0.0252 -0.0178 620 PHE A CD1   
4961 C  CD2   . PHE A 620 ? 0.687  0.6275 0.8118 -0.0393 -0.0344 -0.0146 620 PHE A CD2   
4962 C  CE1   . PHE A 620 ? 0.697  0.6409 0.8146 -0.0363 -0.0229 -0.016  620 PHE A CE1   
4963 C  CE2   . PHE A 620 ? 0.6943 0.6378 0.8173 -0.0381 -0.0319 -0.0129 620 PHE A CE2   
4964 C  CZ    . PHE A 620 ? 0.6924 0.6373 0.8116 -0.0367 -0.0263 -0.0136 620 PHE A CZ    
4965 N  N     . GLU A 621 ? 0.6782 0.6086 0.8127 -0.0419 -0.0394 -0.0214 621 GLU A N     
4966 C  CA    . GLU A 621 ? 0.6837 0.6074 0.8153 -0.0425 -0.0425 -0.0247 621 GLU A CA    
4967 C  C     . GLU A 621 ? 0.6698 0.596  0.807  -0.0418 -0.0387 -0.025  621 GLU A C     
4968 O  O     . GLU A 621 ? 0.676  0.5972 0.8071 -0.041  -0.0378 -0.0288 621 GLU A O     
4969 C  CB    . GLU A 621 ? 0.7237 0.6446 0.8605 -0.0449 -0.0505 -0.0232 621 GLU A CB    
4970 C  CG    . GLU A 621 ? 0.8132 0.7238 0.941  -0.0455 -0.0556 -0.0275 621 GLU A CG    
4971 C  CD    . GLU A 621 ? 0.9208 0.8286 1.0552 -0.0469 -0.0599 -0.0276 621 GLU A CD    
4972 O  OE1   . GLU A 621 ? 0.9403 0.8527 1.0824 -0.0464 -0.0564 -0.0265 621 GLU A OE1   
4973 O  OE2   . GLU A 621 ? 0.9589 0.8595 1.0906 -0.0484 -0.0671 -0.0288 621 GLU A OE2   
4974 N  N     . VAL A 622 ? 0.6507 0.5847 0.7994 -0.0419 -0.0365 -0.021  622 VAL A N     
4975 C  CA    . VAL A 622 ? 0.6412 0.578  0.7961 -0.0413 -0.0331 -0.0207 622 VAL A CA    
4976 C  C     . VAL A 622 ? 0.6321 0.5699 0.7811 -0.0391 -0.0263 -0.0228 622 VAL A C     
4977 O  O     . VAL A 622 ? 0.636  0.5709 0.7826 -0.0384 -0.0246 -0.0257 622 VAL A O     
4978 C  CB    . VAL A 622 ? 0.6436 0.5882 0.8121 -0.042  -0.0331 -0.0154 622 VAL A CB    
4979 C  CG1   . VAL A 622 ? 0.648  0.5964 0.822  -0.041  -0.0283 -0.0147 622 VAL A CG1   
4980 C  CG2   . VAL A 622 ? 0.6472 0.5905 0.8231 -0.0444 -0.04   -0.0134 622 VAL A CG2   
4981 N  N     . THR A 623 ? 0.6166 0.5583 0.7635 -0.038  -0.0227 -0.0213 623 THR A N     
4982 C  CA    . THR A 623 ? 0.6108 0.5541 0.7534 -0.0362 -0.0165 -0.0225 623 THR A CA    
4983 C  C     . THR A 623 ? 0.6118 0.55   0.7422 -0.0354 -0.015  -0.0264 623 THR A C     
4984 O  O     . THR A 623 ? 0.6126 0.5505 0.7398 -0.0341 -0.0108 -0.0283 623 THR A O     
4985 C  CB    . THR A 623 ? 0.6164 0.5659 0.7624 -0.0354 -0.0136 -0.019  623 THR A CB    
4986 O  OG1   . THR A 623 ? 0.6284 0.5768 0.7695 -0.0357 -0.0158 -0.0185 623 THR A OG1   
4987 C  CG2   . THR A 623 ? 0.6125 0.5677 0.7703 -0.0357 -0.014  -0.0149 623 THR A CG2   
4988 N  N     . GLY A 624 ? 0.6085 0.5432 0.7322 -0.036  -0.0182 -0.0271 624 GLY A N     
4989 C  CA    . GLY A 624 ? 0.6092 0.5392 0.7206 -0.0352 -0.0168 -0.0303 624 GLY A CA    
4990 C  C     . GLY A 624 ? 0.5969 0.5303 0.7048 -0.0344 -0.0125 -0.029  624 GLY A C     
4991 O  O     . GLY A 624 ? 0.6074 0.5381 0.7059 -0.0337 -0.0103 -0.0311 624 GLY A O     
4992 N  N     . CYS A 625 ? 0.5738 0.5131 0.6889 -0.0344 -0.0114 -0.0253 625 CYS A N     
4993 C  CA    . CYS A 625 ? 0.564  0.5063 0.6764 -0.0336 -0.0079 -0.0237 625 CYS A CA    
4994 C  C     . CYS A 625 ? 0.5573 0.4966 0.6611 -0.0341 -0.0099 -0.0241 625 CYS A C     
4995 O  O     . CYS A 625 ? 0.5598 0.4965 0.663  -0.0351 -0.0147 -0.024  625 CYS A O     
4996 C  CB    . CYS A 625 ? 0.5655 0.5137 0.6871 -0.0331 -0.007  -0.0199 625 CYS A CB    
4997 S  SG    . CYS A 625 ? 0.5948 0.5469 0.7254 -0.0323 -0.0036 -0.019  625 CYS A SG    
4998 N  N     . ASP A 626 ? 0.5512 0.4906 0.6486 -0.0335 -0.0066 -0.0242 626 ASP A N     
4999 C  CA    . ASP A 626 ? 0.5542 0.491  0.6433 -0.034  -0.0083 -0.0241 626 ASP A CA    
5000 C  C     . ASP A 626 ? 0.5479 0.4881 0.6413 -0.0341 -0.0099 -0.0206 626 ASP A C     
5001 O  O     . ASP A 626 ? 0.552  0.4901 0.6411 -0.0348 -0.0131 -0.0201 626 ASP A O     
5002 C  CB    . ASP A 626 ? 0.5769 0.5127 0.6576 -0.0334 -0.0041 -0.0251 626 ASP A CB    
5003 C  CG    . ASP A 626 ? 0.6328 0.5651 0.7079 -0.0329 -0.0024 -0.0286 626 ASP A CG    
5004 O  OD1   . ASP A 626 ? 0.6457 0.5728 0.7134 -0.0333 -0.0051 -0.0308 626 ASP A OD1   
5005 O  OD2   . ASP A 626 ? 0.6589 0.5933 0.7367 -0.032  0.0017  -0.0292 626 ASP A OD2   
5006 N  N     . LEU A 627 ? 0.5343 0.4795 0.6356 -0.0331 -0.0075 -0.0183 627 LEU A N     
5007 C  CA    . LEU A 627 ? 0.527  0.4754 0.6322 -0.0326 -0.0084 -0.0151 627 LEU A CA    
5008 C  C     . LEU A 627 ? 0.5229 0.4761 0.6391 -0.0317 -0.0079 -0.0129 627 LEU A C     
5009 O  O     . LEU A 627 ? 0.5266 0.4811 0.6462 -0.0312 -0.005  -0.0134 627 LEU A O     
5010 C  CB    . LEU A 627 ? 0.5241 0.4733 0.6248 -0.0318 -0.005  -0.0142 627 LEU A CB    
5011 C  CG    . LEU A 627 ? 0.5346 0.4864 0.638  -0.0307 -0.0055 -0.0112 627 LEU A CG    
5012 C  CD1   . LEU A 627 ? 0.5422 0.4922 0.6429 -0.0314 -0.0099 -0.0105 627 LEU A CD1   
5013 C  CD2   . LEU A 627 ? 0.5407 0.4927 0.6402 -0.03   -0.0023 -0.0105 627 LEU A CD2   
5014 N  N     . LEU A 628 ? 0.5132 0.4688 0.6349 -0.0315 -0.0107 -0.0103 628 LEU A N     
5015 C  CA    . LEU A 628 ? 0.5069 0.4676 0.6388 -0.0304 -0.0098 -0.0077 628 LEU A CA    
5016 C  C     . LEU A 628 ? 0.5064 0.4699 0.6392 -0.0285 -0.0087 -0.005  628 LEU A C     
5017 O  O     . LEU A 628 ? 0.5086 0.471  0.6381 -0.0286 -0.0112 -0.0043 628 LEU A O     
5018 C  CB    . LEU A 628 ? 0.5054 0.4673 0.6446 -0.0314 -0.0139 -0.0065 628 LEU A CB    
5019 C  CG    . LEU A 628 ? 0.5263 0.4853 0.6661 -0.0331 -0.0156 -0.0088 628 LEU A CG    
5020 C  CD1   . LEU A 628 ? 0.5326 0.4925 0.6795 -0.0344 -0.0206 -0.0071 628 LEU A CD1   
5021 C  CD2   . LEU A 628 ? 0.5321 0.4927 0.6754 -0.0325 -0.0117 -0.0095 628 LEU A CD2   
5022 N  N     . ILE A 629 ? 0.5022 0.4689 0.6388 -0.0267 -0.0051 -0.0036 629 ILE A N     
5023 C  CA    . ILE A 629 ? 0.5068 0.4755 0.6436 -0.0245 -0.004  -0.0012 629 ILE A CA    
5024 C  C     . ILE A 629 ? 0.5061 0.48   0.6526 -0.0228 -0.0036 0.0018  629 ILE A C     
5025 O  O     . ILE A 629 ? 0.5055 0.4815 0.6562 -0.022  -0.0007 0.0024  629 ILE A O     
5026 C  CB    . ILE A 629 ? 0.5154 0.4826 0.6468 -0.0235 -0.0005 -0.0019 629 ILE A CB    
5027 C  CG1   . ILE A 629 ? 0.5325 0.4953 0.6551 -0.0254 -0.0006 -0.0045 629 ILE A CG1   
5028 C  CG2   . ILE A 629 ? 0.5191 0.4871 0.6494 -0.0212 -0.0001 0.0003  629 ILE A CG2   
5029 C  CD1   . ILE A 629 ? 0.5498 0.5115 0.6687 -0.025  0.0027  -0.0052 629 ILE A CD1   
5030 N  N     . ALA A 630 ? 0.505  0.4809 0.6552 -0.0225 -0.0065 0.0038  630 ALA A N     
5031 C  CA    . ALA A 630 ? 0.5088 0.4903 0.6688 -0.0208 -0.0061 0.0072  630 ALA A CA    
5032 C  C     . ALA A 630 ? 0.5197 0.5028 0.6784 -0.0174 -0.0038 0.0091  630 ALA A C     
5033 O  O     . ALA A 630 ? 0.5237 0.5051 0.6779 -0.0166 -0.0055 0.0092  630 ALA A O     
5034 C  CB    . ALA A 630 ? 0.5059 0.4893 0.6715 -0.0219 -0.0104 0.0088  630 ALA A CB    
5035 N  N     . ILE A 631 ? 0.5238 0.5094 0.6857 -0.0153 -0.0002 0.0104  631 ILE A N     
5036 C  CA    . ILE A 631 ? 0.5385 0.525  0.6987 -0.0117 0.0022  0.012   631 ILE A CA    
5037 C  C     . ILE A 631 ? 0.5544 0.547  0.7235 -0.009  0.0033  0.0157  631 ILE A C     
5038 O  O     . ILE A 631 ? 0.5536 0.5498 0.7302 -0.0098 0.0041  0.017   631 ILE A O     
5039 C  CB    . ILE A 631 ? 0.5405 0.5244 0.6965 -0.0114 0.0055  0.0104  631 ILE A CB    
5040 C  CG1   . ILE A 631 ? 0.5602 0.5387 0.7071 -0.0134 0.0047  0.0074  631 ILE A CG1   
5041 C  CG2   . ILE A 631 ? 0.5409 0.5258 0.6963 -0.0076 0.0083  0.0122  631 ILE A CG2   
5042 C  CD1   . ILE A 631 ? 0.5833 0.5599 0.728  -0.0143 0.0072  0.0057  631 ILE A CD1   
5043 N  N     . LYS A 632 ? 0.5634 0.5572 0.7319 -0.0057 0.0033  0.0176  632 LYS A N     
5044 C  CA    . LYS A 632 ? 0.5768 0.5767 0.7532 -0.0025 0.005   0.0214  632 LYS A CA    
5045 C  C     . LYS A 632 ? 0.5947 0.5937 0.7664 0.0021  0.0069  0.0223  632 LYS A C     
5046 O  O     . LYS A 632 ? 0.6047 0.5993 0.7692 0.0025  0.005   0.0208  632 LYS A O     
5047 C  CB    . LYS A 632 ? 0.6008 0.6054 0.7858 -0.0035 0.002   0.0237  632 LYS A CB    
5048 C  CG    . LYS A 632 ? 0.669  0.6716 0.8504 -0.0034 -0.0016 0.0233  632 LYS A CG    
5049 C  CD    . LYS A 632 ? 0.7411 0.7495 0.9326 -0.0032 -0.004  0.0268  632 LYS A CD    
5050 C  CE    . LYS A 632 ? 0.8019 0.8085 0.9904 -0.0028 -0.0077 0.0267  632 LYS A CE    
5051 N  NZ    . LYS A 632 ? 0.841  0.8414 1.0225 -0.0069 -0.0115 0.0232  632 LYS A NZ    
5052 N  N     . ASN A 633 ? 0.5971 0.5995 0.7721 0.0056  0.0106  0.0246  633 ASN A N     
5053 C  CA    . ASN A 633 ? 0.6086 0.6094 0.7783 0.0105  0.0124  0.0253  633 ASN A CA    
5054 C  C     . ASN A 633 ? 0.6123 0.618  0.7874 0.0139  0.012   0.0285  633 ASN A C     
5055 O  O     . ASN A 633 ? 0.6092 0.6216 0.7944 0.0135  0.0121  0.0313  633 ASN A O     
5056 C  CB    . ASN A 633 ? 0.6186 0.6192 0.787  0.0131  0.0165  0.026   633 ASN A CB    
5057 C  CG    . ASN A 633 ? 0.6384 0.6462 0.8169 0.0137  0.0191  0.0292  633 ASN A CG    
5058 O  OD1   . ASN A 633 ? 0.6434 0.6533 0.8276 0.0099  0.0185  0.0291  633 ASN A OD1   
5059 N  ND2   . ASN A 633 ? 0.6412 0.6528 0.8221 0.0186  0.0218  0.0322  633 ASN A ND2   
5060 N  N     . GLN A 634 ? 0.6169 0.6193 0.7855 0.0171  0.0112  0.028   634 GLN A N     
5061 C  CA    . GLN A 634 ? 0.6232 0.6292 0.7951 0.0214  0.0111  0.0307  634 GLN A CA    
5062 C  C     . GLN A 634 ? 0.6316 0.6366 0.7992 0.0271  0.015   0.0316  634 GLN A C     
5063 O  O     . GLN A 634 ? 0.6379 0.6361 0.7959 0.0276  0.0153  0.0291  634 GLN A O     
5064 C  CB    . GLN A 634 ? 0.6446 0.6459 0.8105 0.0208  0.0069  0.029   634 GLN A CB    
5065 C  CG    . GLN A 634 ? 0.6781 0.6824 0.8466 0.0255  0.0064  0.0314  634 GLN A CG    
5066 C  CD    . GLN A 634 ? 0.7299 0.7289 0.8923 0.0242  0.0018  0.0296  634 GLN A CD    
5067 O  OE1   . GLN A 634 ? 0.7441 0.7447 0.9106 0.0209  -0.0017 0.0298  634 GLN A OE1   
5068 N  NE2   . GLN A 634 ? 0.742  0.7343 0.8942 0.0266  0.0014  0.0278  634 GLN A NE2   
5069 N  N     . ASN A 635 ? 0.6276 0.6394 0.8023 0.0313  0.0181  0.0352  635 ASN A N     
5070 C  CA    . ASN A 635 ? 0.6349 0.6457 0.8052 0.037   0.0222  0.0362  635 ASN A CA    
5071 C  C     . ASN A 635 ? 0.6395 0.6469 0.8031 0.0427  0.0218  0.0361  635 ASN A C     
5072 O  O     . ASN A 635 ? 0.6439 0.6456 0.7984 0.0463  0.0233  0.0349  635 ASN A O     
5073 C  CB    . ASN A 635 ? 0.6428 0.6622 0.8229 0.0391  0.0265  0.0402  635 ASN A CB    
5074 C  CG    . ASN A 635 ? 0.6769 0.6981 0.8619 0.034   0.0271  0.04    635 ASN A CG    
5075 O  OD1   . ASN A 635 ? 0.6923 0.7074 0.8709 0.0308  0.0261  0.0368  635 ASN A OD1   
5076 N  ND2   . ASN A 635 ? 0.6787 0.7084 0.8754 0.0332  0.0286  0.0437  635 ASN A ND2   
5077 N  N     . ASN A 636 ? 0.6379 0.6483 0.8057 0.0434  0.0193  0.0373  636 ASN A N     
5078 C  CA    . ASN A 636 ? 0.6455 0.6524 0.8071 0.0488  0.0184  0.0372  636 ASN A CA    
5079 C  C     . ASN A 636 ? 0.6426 0.6463 0.8022 0.0461  0.013   0.0355  636 ASN A C     
5080 O  O     . ASN A 636 ? 0.637  0.6464 0.8053 0.0449  0.0112  0.0375  636 ASN A O     
5081 C  CB    . ASN A 636 ? 0.6576 0.6719 0.8259 0.0553  0.0221  0.0411  636 ASN A CB    
5082 C  CG    . ASN A 636 ? 0.7012 0.713  0.8628 0.061   0.0266  0.0414  636 ASN A CG    
5083 O  OD1   . ASN A 636 ? 0.7191 0.7217 0.8685 0.0631  0.0256  0.0385  636 ASN A OD1   
5084 N  ND2   . ASN A 636 ? 0.7029 0.7225 0.8721 0.0636  0.0314  0.0449  636 ASN A ND2   
5085 N  N     . PRO A 637 ? 0.6434 0.6377 0.7917 0.0451  0.0102  0.0322  637 PRO A N     
5086 C  CA    . PRO A 637 ? 0.6473 0.6341 0.7852 0.0459  0.0114  0.0298  637 PRO A CA    
5087 C  C     . PRO A 637 ? 0.6483 0.6341 0.7866 0.0397  0.0116  0.0281  637 PRO A C     
5088 O  O     . PRO A 637 ? 0.6499 0.6384 0.7934 0.0345  0.0095  0.0278  637 PRO A O     
5089 C  CB    . PRO A 637 ? 0.6603 0.6386 0.7881 0.0466  0.0072  0.0276  637 PRO A CB    
5090 C  CG    . PRO A 637 ? 0.6641 0.6445 0.7964 0.0424  0.0032  0.0276  637 PRO A CG    
5091 C  CD    . PRO A 637 ? 0.6382 0.6289 0.7836 0.0424  0.005   0.0307  637 PRO A CD    
5092 N  N     . GLN A 638 ? 0.6416 0.6237 0.7746 0.0405  0.014   0.0271  638 GLN A N     
5093 C  CA    . GLN A 638 ? 0.6337 0.6151 0.7674 0.0351  0.0144  0.0256  638 GLN A CA    
5094 C  C     . GLN A 638 ? 0.6257 0.6025 0.7554 0.0295  0.0103  0.0229  638 GLN A C     
5095 O  O     . GLN A 638 ? 0.6331 0.6028 0.7538 0.0299  0.008   0.0212  638 GLN A O     
5096 C  CB    . GLN A 638 ? 0.6539 0.6311 0.7816 0.037   0.0171  0.0248  638 GLN A CB    
5097 C  CG    . GLN A 638 ? 0.6775 0.6601 0.8104 0.0407  0.0218  0.0275  638 GLN A CG    
5098 C  CD    . GLN A 638 ? 0.7241 0.7015 0.8502 0.0418  0.0237  0.0264  638 GLN A CD    
5099 O  OE1   . GLN A 638 ? 0.7408 0.7099 0.8569 0.043   0.0218  0.0245  638 GLN A OE1   
5100 N  NE2   . GLN A 638 ? 0.7266 0.7082 0.8581 0.0412  0.027   0.0278  638 GLN A NE2   
5101 N  N     . LYS A 639 ? 0.6074 0.5882 0.7436 0.0246  0.0094  0.0228  639 LYS A N     
5102 C  CA    . LYS A 639 ? 0.6006 0.5777 0.7333 0.0194  0.0059  0.0204  639 LYS A CA    
5103 C  C     . LYS A 639 ? 0.5834 0.5639 0.722  0.0145  0.0065  0.0198  639 LYS A C     
5104 O  O     . LYS A 639 ? 0.5819 0.5687 0.7294 0.0147  0.008   0.0218  639 LYS A O     
5105 C  CB    . LYS A 639 ? 0.6231 0.6008 0.7567 0.0193  0.0023  0.0209  639 LYS A CB    
5106 C  CG    . LYS A 639 ? 0.6838 0.6546 0.8079 0.0211  -0.0004 0.0199  639 LYS A CG    
5107 C  CD    . LYS A 639 ? 0.7408 0.7127 0.8667 0.0213  -0.0039 0.0207  639 LYS A CD    
5108 C  CE    . LYS A 639 ? 0.7938 0.7599 0.9126 0.0173  -0.0079 0.0187  639 LYS A CE    
5109 N  NZ    . LYS A 639 ? 0.832  0.7909 0.9412 0.0197  -0.0094 0.0179  639 LYS A NZ    
5110 N  N     . TRP A 640 ? 0.5697 0.546  0.7036 0.0103  0.0051  0.0173  640 TRP A N     
5111 C  CA    . TRP A 640 ? 0.557  0.5356 0.6954 0.0058  0.0052  0.0163  640 TRP A CA    
5112 C  C     . TRP A 640 ? 0.5499 0.5282 0.6884 0.0027  0.0014  0.0156  640 TRP A C     
5113 O  O     . TRP A 640 ? 0.5592 0.5326 0.6904 0.0014  -0.0009 0.0141  640 TRP A O     
5114 C  CB    . TRP A 640 ? 0.5544 0.5289 0.6878 0.0033  0.0064  0.0141  640 TRP A CB    
5115 C  CG    . TRP A 640 ? 0.5531 0.5286 0.6883 0.0052  0.0099  0.0147  640 TRP A CG    
5116 C  CD1   . TRP A 640 ? 0.5668 0.5381 0.6961 0.0073  0.0113  0.0144  640 TRP A CD1   
5117 C  CD2   . TRP A 640 ? 0.5466 0.5273 0.6899 0.0049  0.0123  0.0159  640 TRP A CD2   
5118 N  NE1   . TRP A 640 ? 0.568  0.5415 0.7009 0.0085  0.0144  0.0152  640 TRP A NE1   
5119 C  CE2   . TRP A 640 ? 0.5578 0.5373 0.6995 0.007   0.0152  0.0163  640 TRP A CE2   
5120 C  CE3   . TRP A 640 ? 0.5464 0.5325 0.6983 0.003   0.0119  0.017   640 TRP A CE3   
5121 C  CZ2   . TRP A 640 ? 0.5606 0.5441 0.7087 0.0072  0.0179  0.0175  640 TRP A CZ2   
5122 C  CZ3   . TRP A 640 ? 0.5525 0.5425 0.711  0.0031  0.0144  0.0183  640 TRP A CZ3   
5123 C  CH2   . TRP A 640 ? 0.555  0.5439 0.7116 0.0052  0.0175  0.0186  640 TRP A CH2   
5124 N  N     . VAL A 641 ? 0.5319 0.5152 0.6785 0.0017  0.0005  0.017   641 VAL A N     
5125 C  CA    . VAL A 641 ? 0.5254 0.5082 0.6723 -0.0013 -0.0035 0.0163  641 VAL A CA    
5126 C  C     . VAL A 641 ? 0.5262 0.5074 0.6723 -0.0059 -0.004  0.014   641 VAL A C     
5127 O  O     . VAL A 641 ? 0.5247 0.509  0.677  -0.007  -0.0025 0.0143  641 VAL A O     
5128 C  CB    . VAL A 641 ? 0.5216 0.5102 0.6776 -0.0001 -0.005  0.0192  641 VAL A CB    
5129 C  CG1   . VAL A 641 ? 0.5266 0.5136 0.6818 -0.0031 -0.0098 0.0185  641 VAL A CG1   
5130 C  CG2   . VAL A 641 ? 0.5243 0.5149 0.6813 0.0052  -0.0037 0.0216  641 VAL A CG2   
5131 N  N     . ILE A 642 ? 0.5237 0.4997 0.6618 -0.0084 -0.006  0.0116  642 ILE A N     
5132 C  CA    . ILE A 642 ? 0.5214 0.4952 0.6572 -0.0122 -0.0061 0.0091  642 ILE A CA    
5133 C  C     . ILE A 642 ? 0.5198 0.4924 0.6551 -0.015  -0.0102 0.0084  642 ILE A C     
5134 O  O     . ILE A 642 ? 0.522  0.492  0.6524 -0.0152 -0.0129 0.0083  642 ILE A O     
5135 C  CB    . ILE A 642 ? 0.5293 0.4982 0.6562 -0.013  -0.0047 0.0071  642 ILE A CB    
5136 C  CG1   . ILE A 642 ? 0.5398 0.5083 0.6655 -0.0099 -0.0018 0.0081  642 ILE A CG1   
5137 C  CG2   . ILE A 642 ? 0.5367 0.5044 0.6625 -0.0162 -0.0037 0.0048  642 ILE A CG2   
5138 C  CD1   . ILE A 642 ? 0.5528 0.5245 0.6843 -0.0089 0.0016  0.0086  642 ILE A CD1   
5139 N  N     . LYS A 643 ? 0.5136 0.4878 0.6537 -0.0173 -0.0109 0.0077  643 LYS A N     
5140 C  CA    . LYS A 643 ? 0.5205 0.4927 0.6596 -0.0201 -0.015  0.0067  643 LYS A CA    
5141 C  C     . LYS A 643 ? 0.5281 0.4966 0.6621 -0.023  -0.0145 0.0036  643 LYS A C     
5142 O  O     . LYS A 643 ? 0.5275 0.4975 0.6657 -0.0236 -0.0127 0.003   643 LYS A O     
5143 C  CB    . LYS A 643 ? 0.5404 0.5172 0.6898 -0.0203 -0.0173 0.009   643 LYS A CB    
5144 C  CG    . LYS A 643 ? 0.5965 0.5707 0.7449 -0.0231 -0.0224 0.0082  643 LYS A CG    
5145 C  CD    . LYS A 643 ? 0.6511 0.63   0.8106 -0.0235 -0.0252 0.0109  643 LYS A CD    
5146 C  CE    . LYS A 643 ? 0.695  0.6707 0.8533 -0.0262 -0.031  0.0104  643 LYS A CE    
5147 N  NZ    . LYS A 643 ? 0.708  0.6884 0.878  -0.0267 -0.0341 0.0135  643 LYS A NZ    
5148 N  N     . PHE A 644 ? 0.5325 0.4961 0.6572 -0.0245 -0.0159 0.0016  644 PHE A N     
5149 C  CA    . PHE A 644 ? 0.538  0.4978 0.6566 -0.0268 -0.0151 -0.0014 644 PHE A CA    
5150 C  C     . PHE A 644 ? 0.5394 0.4968 0.6572 -0.0291 -0.0192 -0.0027 644 PHE A C     
5151 O  O     . PHE A 644 ? 0.5441 0.4991 0.6579 -0.0298 -0.0227 -0.0025 644 PHE A O     
5152 C  CB    . PHE A 644 ? 0.541  0.4969 0.6496 -0.0272 -0.0141 -0.0025 644 PHE A CB    
5153 C  CG    . PHE A 644 ? 0.5481 0.5051 0.6561 -0.0253 -0.0105 -0.0016 644 PHE A CG    
5154 C  CD1   . PHE A 644 ? 0.5596 0.5171 0.668  -0.0254 -0.0068 -0.0027 644 PHE A CD1   
5155 C  CD2   . PHE A 644 ? 0.5565 0.5134 0.6631 -0.0235 -0.0112 0.0003  644 PHE A CD2   
5156 C  CE1   . PHE A 644 ? 0.5688 0.5266 0.6763 -0.0238 -0.004  -0.0018 644 PHE A CE1   
5157 C  CE2   . PHE A 644 ? 0.5658 0.5228 0.6712 -0.0218 -0.0084 0.0011  644 PHE A CE2   
5158 C  CZ    . PHE A 644 ? 0.5645 0.5218 0.6703 -0.022  -0.005  0.0001  644 PHE A CZ    
5159 N  N     . LYS A 645 ? 0.5342 0.4917 0.6553 -0.0302 -0.0191 -0.004  645 LYS A N     
5160 C  CA    . LYS A 645 ? 0.5398 0.494  0.6596 -0.0324 -0.0233 -0.0055 645 LYS A CA    
5161 C  C     . LYS A 645 ? 0.5484 0.4976 0.6595 -0.0337 -0.0222 -0.0091 645 LYS A C     
5162 O  O     . LYS A 645 ? 0.5495 0.4991 0.6628 -0.0337 -0.0198 -0.0105 645 LYS A O     
5163 C  CB    . LYS A 645 ? 0.5563 0.5139 0.6868 -0.0327 -0.025  -0.0041 645 LYS A CB    
5164 C  CG    . LYS A 645 ? 0.6092 0.5709 0.7479 -0.0321 -0.0279 -0.0006 645 LYS A CG    
5165 C  CD    . LYS A 645 ? 0.6772 0.6353 0.8132 -0.0338 -0.0338 -0.0007 645 LYS A CD    
5166 C  CE    . LYS A 645 ? 0.7335 0.6871 0.8678 -0.0363 -0.0374 -0.003  645 LYS A CE    
5167 N  NZ    . LYS A 645 ? 0.7642 0.714  0.8959 -0.038  -0.0437 -0.003  645 LYS A NZ    
5168 N  N     . PRO A 646 ? 0.5504 0.4949 0.6516 -0.0346 -0.0237 -0.0106 646 PRO A N     
5169 C  CA    . PRO A 646 ? 0.5542 0.4941 0.6467 -0.0355 -0.0223 -0.014  646 PRO A CA    
5170 C  C     . PRO A 646 ? 0.5542 0.4901 0.6459 -0.0369 -0.0261 -0.0161 646 PRO A C     
5171 O  O     . PRO A 646 ? 0.5522 0.487  0.646  -0.0378 -0.0312 -0.0152 646 PRO A O     
5172 C  CB    . PRO A 646 ? 0.5689 0.5056 0.6513 -0.0359 -0.0227 -0.0142 646 PRO A CB    
5173 C  CG    . PRO A 646 ? 0.5727 0.5101 0.6578 -0.036  -0.027  -0.0118 646 PRO A CG    
5174 C  CD    . PRO A 646 ? 0.5467 0.4898 0.6439 -0.0348 -0.0267 -0.0093 646 PRO A CD    
5175 N  N     . LYS A 647 ? 0.5546 0.4882 0.6433 -0.0369 -0.024  -0.019  647 LYS A N     
5176 C  CA    . LYS A 647 ? 0.5627 0.4914 0.6493 -0.038  -0.0278 -0.0214 647 LYS A CA    
5177 C  C     . LYS A 647 ? 0.5716 0.4934 0.6451 -0.0387 -0.0298 -0.0239 647 LYS A C     
5178 O  O     . LYS A 647 ? 0.5746 0.4913 0.6451 -0.0397 -0.0349 -0.0252 647 LYS A O     
5179 C  CB    . LYS A 647 ? 0.5855 0.5141 0.6742 -0.0374 -0.0249 -0.0236 647 LYS A CB    
5180 C  CG    . LYS A 647 ? 0.6376 0.5606 0.7247 -0.0384 -0.0292 -0.0261 647 LYS A CG    
5181 C  CD    . LYS A 647 ? 0.6972 0.6191 0.7843 -0.0375 -0.0261 -0.0288 647 LYS A CD    
5182 C  CE    . LYS A 647 ? 0.7478 0.6685 0.8258 -0.0361 -0.0207 -0.031  647 LYS A CE    
5183 N  NZ    . LYS A 647 ? 0.7761 0.6951 0.8537 -0.0351 -0.0182 -0.0339 647 LYS A NZ    
5184 N  N     . ASN A 648 ? 0.573  0.4944 0.6386 -0.038  -0.0258 -0.0244 648 ASN A N     
5185 C  CA    . ASN A 648 ? 0.586  0.5014 0.6387 -0.0384 -0.0267 -0.0265 648 ASN A CA    
5186 C  C     . ASN A 648 ? 0.5904 0.507  0.6379 -0.0385 -0.0251 -0.0246 648 ASN A C     
5187 O  O     . ASN A 648 ? 0.5882 0.5097 0.642  -0.0381 -0.0237 -0.0218 648 ASN A O     
5188 C  CB    . ASN A 648 ? 0.6063 0.5188 0.6528 -0.0374 -0.0231 -0.0299 648 ASN A CB    
5189 C  CG    . ASN A 648 ? 0.6428 0.5606 0.6938 -0.0362 -0.0167 -0.0294 648 ASN A CG    
5190 O  OD1   . ASN A 648 ? 0.653  0.5746 0.7047 -0.036  -0.0137 -0.0271 648 ASN A OD1   
5191 N  ND2   . ASN A 648 ? 0.649  0.5667 0.703  -0.0354 -0.015  -0.0314 648 ASN A ND2   
5192 N  N     . THR A 649 ? 0.5958 0.5072 0.6312 -0.0389 -0.0256 -0.026  649 THR A N     
5193 C  CA    . THR A 649 ? 0.6032 0.5145 0.6318 -0.0393 -0.0245 -0.0244 649 THR A CA    
5194 C  C     . THR A 649 ? 0.6015 0.5172 0.6309 -0.0385 -0.0184 -0.0231 649 THR A C     
5195 O  O     . THR A 649 ? 0.6013 0.519  0.6307 -0.0388 -0.0181 -0.0205 649 THR A O     
5196 C  CB    . THR A 649 ? 0.6276 0.5318 0.6427 -0.0398 -0.0263 -0.0265 649 THR A CB    
5197 O  OG1   . THR A 649 ? 0.6419 0.5436 0.6522 -0.0388 -0.0234 -0.0297 649 THR A OG1   
5198 C  CG2   . THR A 649 ? 0.6343 0.5337 0.6479 -0.041  -0.0336 -0.0267 649 THR A CG2   
5199 N  N     . ILE A 650 ? 0.5993 0.5164 0.6296 -0.0375 -0.0138 -0.0248 650 ILE A N     
5200 C  CA    . ILE A 650 ? 0.6021 0.5235 0.634  -0.0369 -0.0082 -0.0234 650 ILE A CA    
5201 C  C     . ILE A 650 ? 0.5932 0.5199 0.6361 -0.0365 -0.008  -0.0208 650 ILE A C     
5202 O  O     . ILE A 650 ? 0.5949 0.5239 0.6383 -0.0366 -0.0065 -0.0184 650 ILE A O     
5203 C  CB    . ILE A 650 ? 0.6123 0.534  0.6432 -0.0357 -0.0036 -0.0258 650 ILE A CB    
5204 C  CG1   . ILE A 650 ? 0.6332 0.55   0.6516 -0.0355 -0.0027 -0.0281 650 ILE A CG1   
5205 C  CG2   . ILE A 650 ? 0.6134 0.5405 0.6494 -0.0351 0.0016  -0.0241 650 ILE A CG2   
5206 C  CD1   . ILE A 650 ? 0.6511 0.5687 0.662  -0.0359 0.0008  -0.0263 650 ILE A CD1   
5207 N  N     . ALA A 651 ? 0.5812 0.5094 0.6326 -0.0362 -0.0098 -0.0212 651 ALA A N     
5208 C  CA    . ALA A 651 ? 0.5752 0.5081 0.6367 -0.0355 -0.0096 -0.0187 651 ALA A CA    
5209 C  C     . ALA A 651 ? 0.5727 0.506  0.6344 -0.0359 -0.0129 -0.0162 651 ALA A C     
5210 O  O     . ALA A 651 ? 0.5771 0.5136 0.6429 -0.0351 -0.0116 -0.0139 651 ALA A O     
5211 C  CB    . ALA A 651 ? 0.5746 0.5089 0.6447 -0.0352 -0.0112 -0.0194 651 ALA A CB    
5212 N  N     . GLU A 652 ? 0.5653 0.4947 0.6217 -0.0369 -0.0173 -0.0166 652 GLU A N     
5213 C  CA    . GLU A 652 ? 0.5644 0.4937 0.6206 -0.0372 -0.0207 -0.0142 652 GLU A CA    
5214 C  C     . GLU A 652 ? 0.5563 0.4854 0.6064 -0.0373 -0.0185 -0.0128 652 GLU A C     
5215 O  O     . GLU A 652 ? 0.5531 0.484  0.6061 -0.0367 -0.0194 -0.0103 652 GLU A O     
5216 C  CB    . GLU A 652 ? 0.605  0.5296 0.6563 -0.0384 -0.0261 -0.015  652 GLU A CB    
5217 C  CG    . GLU A 652 ? 0.6855 0.6103 0.7379 -0.0386 -0.0301 -0.0125 652 GLU A CG    
5218 C  CD    . GLU A 652 ? 0.8025 0.7226 0.8508 -0.0399 -0.036  -0.0131 652 GLU A CD    
5219 O  OE1   . GLU A 652 ? 0.8321 0.7499 0.8806 -0.0405 -0.0379 -0.0151 652 GLU A OE1   
5220 O  OE2   . GLU A 652 ? 0.8369 0.7555 0.8819 -0.0404 -0.0389 -0.0115 652 GLU A OE2   
5221 N  N     . LYS A 653 ? 0.5511 0.4782 0.5933 -0.0378 -0.0155 -0.0141 653 LYS A N     
5222 C  CA    . LYS A 653 ? 0.552  0.4793 0.5892 -0.0382 -0.0132 -0.0123 653 LYS A CA    
5223 C  C     . LYS A 653 ? 0.5458 0.4776 0.5902 -0.0371 -0.0099 -0.0106 653 LYS A C     
5224 O  O     . LYS A 653 ? 0.5448 0.477  0.5884 -0.0371 -0.01   -0.0083 653 LYS A O     
5225 C  CB    . LYS A 653 ? 0.5738 0.4987 0.6016 -0.039  -0.0102 -0.0138 653 LYS A CB    
5226 C  CG    . LYS A 653 ? 0.6203 0.5399 0.6386 -0.0401 -0.0137 -0.0149 653 LYS A CG    
5227 C  CD    . LYS A 653 ? 0.6693 0.587  0.6773 -0.0407 -0.0106 -0.0149 653 LYS A CD    
5228 C  CE    . LYS A 653 ? 0.7139 0.6268 0.7123 -0.042  -0.0143 -0.0143 653 LYS A CE    
5229 N  NZ    . LYS A 653 ? 0.7429 0.6509 0.7365 -0.0421 -0.0178 -0.0171 653 LYS A NZ    
5230 N  N     . LEU A 654 ? 0.5403 0.4747 0.5914 -0.0361 -0.0074 -0.0117 654 LEU A N     
5231 C  CA    . LEU A 654 ? 0.5413 0.4796 0.5994 -0.0349 -0.0046 -0.0103 654 LEU A CA    
5232 C  C     . LEU A 654 ? 0.545  0.4848 0.6089 -0.0338 -0.0073 -0.0082 654 LEU A C     
5233 O  O     . LEU A 654 ? 0.5442 0.485  0.6091 -0.0331 -0.0066 -0.0063 654 LEU A O     
5234 C  CB    . LEU A 654 ? 0.538  0.4784 0.6017 -0.0342 -0.0018 -0.0121 654 LEU A CB    
5235 C  CG    . LEU A 654 ? 0.5476 0.4916 0.6189 -0.0329 0.0008  -0.0108 654 LEU A CG    
5236 C  CD1   . LEU A 654 ? 0.5519 0.4964 0.6205 -0.0331 0.0034  -0.0092 654 LEU A CD1   
5237 C  CD2   . LEU A 654 ? 0.5553 0.5008 0.6313 -0.0324 0.0033  -0.0127 654 LEU A CD2   
5238 N  N     . VAL A 655 ? 0.5446 0.4843 0.6119 -0.0336 -0.0107 -0.0086 655 VAL A N     
5239 C  CA    . VAL A 655 ? 0.5484 0.49   0.6215 -0.0323 -0.0133 -0.0066 655 VAL A CA    
5240 C  C     . VAL A 655 ? 0.5606 0.5002 0.6285 -0.0323 -0.0154 -0.0047 655 VAL A C     
5241 O  O     . VAL A 655 ? 0.5599 0.501  0.6309 -0.0307 -0.0151 -0.0028 655 VAL A O     
5242 C  CB    . VAL A 655 ? 0.554  0.4959 0.6316 -0.0325 -0.0168 -0.007  655 VAL A CB    
5243 C  CG1   . VAL A 655 ? 0.5608 0.5045 0.6434 -0.0312 -0.0199 -0.0046 655 VAL A CG1   
5244 C  CG2   . VAL A 655 ? 0.5538 0.4982 0.6384 -0.0322 -0.015  -0.0082 655 VAL A CG2   
5245 N  N     . ASN A 656 ? 0.5706 0.5065 0.6301 -0.0341 -0.0172 -0.0053 656 ASN A N     
5246 C  CA    . ASN A 656 ? 0.581  0.5144 0.6348 -0.0345 -0.0194 -0.0035 656 ASN A CA    
5247 C  C     . ASN A 656 ? 0.5709 0.5047 0.6229 -0.0343 -0.0164 -0.0021 656 ASN A C     
5248 O  O     . ASN A 656 ? 0.5673 0.5003 0.6187 -0.0335 -0.0181 -0.0002 656 ASN A O     
5249 C  CB    . ASN A 656 ? 0.6166 0.5457 0.6611 -0.0367 -0.0216 -0.0044 656 ASN A CB    
5250 C  CG    . ASN A 656 ? 0.6851 0.6126 0.7304 -0.037  -0.026  -0.0052 656 ASN A CG    
5251 O  OD1   . ASN A 656 ? 0.7014 0.6311 0.7541 -0.0358 -0.0284 -0.0042 656 ASN A OD1   
5252 N  ND2   . ASN A 656 ? 0.7078 0.6314 0.7454 -0.0387 -0.0273 -0.0069 656 ASN A ND2   
5253 N  N     . TYR A 657 ? 0.5658 0.5006 0.6172 -0.0348 -0.0123 -0.0031 657 TYR A N     
5254 C  CA    . TYR A 657 ? 0.5688 0.5043 0.6195 -0.0348 -0.0095 -0.0017 657 TYR A CA    
5255 C  C     . TYR A 657 ? 0.5731 0.5107 0.6308 -0.0326 -0.0091 -0.0005 657 TYR A C     
5256 O  O     . TYR A 657 ? 0.5729 0.5094 0.6293 -0.0321 -0.0097 0.0015  657 TYR A O     
5257 C  CB    . TYR A 657 ? 0.5644 0.5012 0.6142 -0.0357 -0.0051 -0.0031 657 TYR A CB    
5258 C  CG    . TYR A 657 ? 0.5681 0.506  0.6182 -0.0359 -0.0022 -0.0014 657 TYR A CG    
5259 C  CD1   . TYR A 657 ? 0.5785 0.5148 0.6223 -0.0376 -0.0019 0.0002  657 TYR A CD1   
5260 C  CD2   . TYR A 657 ? 0.5746 0.5149 0.6314 -0.0345 0.0001  -0.0013 657 TYR A CD2   
5261 C  CE1   . TYR A 657 ? 0.5868 0.5242 0.6316 -0.038  0.0004  0.0021  657 TYR A CE1   
5262 C  CE2   . TYR A 657 ? 0.5838 0.5248 0.6411 -0.0349 0.0023  0.0003  657 TYR A CE2   
5263 C  CZ    . TYR A 657 ? 0.5949 0.5345 0.6464 -0.0367 0.0023  0.0021  657 TYR A CZ    
5264 O  OH    . TYR A 657 ? 0.6109 0.5512 0.6637 -0.0372 0.004   0.0041  657 TYR A OH    
5265 N  N     . ILE A 658 ? 0.5731 0.5135 0.638  -0.0311 -0.0084 -0.0015 658 ILE A N     
5266 C  CA    . ILE A 658 ? 0.5768 0.5194 0.6482 -0.0287 -0.0077 -0.0004 658 ILE A CA    
5267 C  C     . ILE A 658 ? 0.5854 0.5268 0.6567 -0.0271 -0.0112 0.0014  658 ILE A C     
5268 O  O     . ILE A 658 ? 0.5874 0.5282 0.659  -0.0254 -0.0112 0.0028  658 ILE A O     
5269 C  CB    . ILE A 658 ? 0.5775 0.5233 0.6563 -0.0277 -0.0062 -0.0016 658 ILE A CB    
5270 C  CG1   . ILE A 658 ? 0.5888 0.5355 0.6679 -0.0289 -0.0027 -0.0033 658 ILE A CG1   
5271 C  CG2   . ILE A 658 ? 0.5804 0.5285 0.6655 -0.025  -0.0056 -0.0002 658 ILE A CG2   
5272 C  CD1   . ILE A 658 ? 0.6058 0.5547 0.6909 -0.0286 -0.0021 -0.0048 658 ILE A CD1   
5273 N  N     . LYS A 659 ? 0.5889 0.5297 0.6595 -0.0275 -0.0144 0.0011  659 LYS A N     
5274 C  CA    . LYS A 659 ? 0.5992 0.5391 0.6701 -0.0259 -0.018  0.0028  659 LYS A CA    
5275 C  C     . LYS A 659 ? 0.6137 0.5497 0.6775 -0.0264 -0.0195 0.0041  659 LYS A C     
5276 O  O     . LYS A 659 ? 0.6147 0.55   0.6793 -0.0241 -0.0208 0.0056  659 LYS A O     
5277 C  CB    . LYS A 659 ? 0.6183 0.558  0.6896 -0.0268 -0.0214 0.0023  659 LYS A CB    
5278 C  CG    . LYS A 659 ? 0.6599 0.6037 0.74   -0.0257 -0.021  0.0019  659 LYS A CG    
5279 C  CD    . LYS A 659 ? 0.719  0.662  0.7989 -0.0277 -0.0241 0.0009  659 LYS A CD    
5280 C  CE    . LYS A 659 ? 0.7714 0.7139 0.8524 -0.027  -0.0286 0.0024  659 LYS A CE    
5281 N  NZ    . LYS A 659 ? 0.8003 0.7435 0.8851 -0.0282 -0.0315 0.0018  659 LYS A NZ    
5282 N  N     . LEU A 660 ? 0.6233 0.5569 0.6802 -0.0292 -0.0194 0.0037  660 LEU A N     
5283 C  CA    . LEU A 660 ? 0.6411 0.571  0.6913 -0.0302 -0.021  0.0053  660 LEU A CA    
5284 C  C     . LEU A 660 ? 0.6508 0.5806 0.7019 -0.0292 -0.0189 0.0065  660 LEU A C     
5285 O  O     . LEU A 660 ? 0.6561 0.583  0.7044 -0.0286 -0.0211 0.0082  660 LEU A O     
5286 C  CB    . LEU A 660 ? 0.6501 0.5782 0.6933 -0.0334 -0.0206 0.0049  660 LEU A CB    
5287 C  CG    . LEU A 660 ? 0.6738 0.5986 0.711  -0.0348 -0.0247 0.0054  660 LEU A CG    
5288 C  CD1   . LEU A 660 ? 0.6751 0.6008 0.7158 -0.0339 -0.0273 0.0042  660 LEU A CD1   
5289 C  CD2   . LEU A 660 ? 0.6879 0.6109 0.7173 -0.0377 -0.0236 0.0051  660 LEU A CD2   
5290 N  N     . ASN A 661 ? 0.6504 0.583  0.7053 -0.0292 -0.0149 0.0055  661 ASN A N     
5291 C  CA    . ASN A 661 ? 0.6591 0.5914 0.7151 -0.0285 -0.013  0.0066  661 ASN A CA    
5292 C  C     . ASN A 661 ? 0.6631 0.5969 0.725  -0.0251 -0.0124 0.0066  661 ASN A C     
5293 O  O     . ASN A 661 ? 0.6655 0.5993 0.729  -0.0244 -0.0105 0.007   661 ASN A O     
5294 C  CB    . ASN A 661 ? 0.6737 0.6077 0.7298 -0.0305 -0.0092 0.0058  661 ASN A CB    
5295 C  CG    . ASN A 661 ? 0.7151 0.6474 0.7646 -0.0335 -0.0094 0.0067  661 ASN A CG    
5296 O  OD1   . ASN A 661 ? 0.7294 0.6625 0.7765 -0.035  -0.0083 0.0054  661 ASN A OD1   
5297 N  ND2   . ASN A 661 ? 0.7243 0.654  0.7705 -0.0342 -0.0109 0.009   661 ASN A ND2   
5298 N  N     . PHE A 662 ? 0.6635 0.5983 0.7285 -0.0229 -0.0142 0.0065  662 PHE A N     
5299 C  CA    . PHE A 662 ? 0.6695 0.6059 0.7398 -0.0194 -0.0133 0.0068  662 PHE A CA    
5300 C  C     . PHE A 662 ? 0.6808 0.6133 0.7476 -0.0171 -0.0159 0.0085  662 PHE A C     
5301 O  O     . PHE A 662 ? 0.6826 0.615  0.7508 -0.0142 -0.0177 0.0091  662 PHE A O     
5302 C  CB    . PHE A 662 ? 0.6628 0.6028 0.7389 -0.0179 -0.0138 0.0064  662 PHE A CB    
5303 C  CG    . PHE A 662 ? 0.6648 0.6083 0.7477 -0.0154 -0.0109 0.0063  662 PHE A CG    
5304 C  CD1   . PHE A 662 ? 0.6741 0.6175 0.7587 -0.0116 -0.011  0.0076  662 PHE A CD1   
5305 C  CD2   . PHE A 662 ? 0.6712 0.6177 0.7582 -0.0168 -0.008  0.0051  662 PHE A CD2   
5306 C  CE1   . PHE A 662 ? 0.6811 0.6276 0.7714 -0.0093 -0.0081 0.0077  662 PHE A CE1   
5307 C  CE2   . PHE A 662 ? 0.6767 0.6264 0.7699 -0.0146 -0.0054 0.0052  662 PHE A CE2   
5308 C  CZ    . PHE A 662 ? 0.6751 0.6249 0.7699 -0.011  -0.0054 0.0067  662 PHE A CZ    
5309 N  N     . LYS A 663 ? 0.6854 0.6145 0.7475 -0.0186 -0.0162 0.0093  663 LYS A N     
5310 C  CA    . LYS A 663 ? 0.699  0.6232 0.7565 -0.0171 -0.0191 0.0108  663 LYS A CA    
5311 C  C     . LYS A 663 ? 0.7121 0.6345 0.7688 -0.0178 -0.0176 0.0114  663 LYS A C     
5312 O  O     . LYS A 663 ? 0.7117 0.636  0.7691 -0.0207 -0.0151 0.0111  663 LYS A O     
5313 C  CB    . LYS A 663 ? 0.7171 0.638  0.7686 -0.0196 -0.0226 0.0117  663 LYS A CB    
5314 C  CG    . LYS A 663 ? 0.7577 0.6727 0.8038 -0.0189 -0.0263 0.0135  663 LYS A CG    
5315 C  CD    . LYS A 663 ? 0.8036 0.7159 0.8439 -0.0221 -0.0293 0.0147  663 LYS A CD    
5316 C  CE    . LYS A 663 ? 0.8459 0.7521 0.8809 -0.0222 -0.0329 0.0167  663 LYS A CE    
5317 N  NZ    . LYS A 663 ? 0.8689 0.7723 0.8983 -0.0251 -0.0363 0.0181  663 LYS A NZ    
5318 N  N     . SER A 664 ? 0.7195 0.6381 0.7746 -0.0149 -0.0191 0.0123  664 SER A N     
5319 C  CA    . SER A 664 ? 0.7307 0.647  0.785  -0.0154 -0.0183 0.0131  664 SER A CA    
5320 C  C     . SER A 664 ? 0.7371 0.6469 0.7867 -0.013  -0.022  0.0144  664 SER A C     
5321 O  O     . SER A 664 ? 0.7408 0.649  0.7896 -0.0091 -0.0235 0.0141  664 SER A O     
5322 C  CB    . SER A 664 ? 0.7494 0.6693 0.8093 -0.0139 -0.0144 0.0119  664 SER A CB    
5323 O  OG    . SER A 664 ? 0.7842 0.7018 0.8436 -0.0146 -0.0138 0.0127  664 SER A OG    
5324 N  N     . ASN A 665 ? 0.7373 0.6434 0.7841 -0.015  -0.0234 0.0158  665 ASN A N     
5325 C  CA    . ASN A 665 ? 0.7465 0.6454 0.7885 -0.013  -0.0273 0.0171  665 ASN A CA    
5326 C  C     . ASN A 665 ? 0.7482 0.6458 0.7918 -0.0097 -0.0257 0.0165  665 ASN A C     
5327 O  O     . ASN A 665 ? 0.7521 0.6437 0.7916 -0.0064 -0.0286 0.0168  665 ASN A O     
5328 C  CB    . ASN A 665 ? 0.7648 0.6599 0.8032 -0.017  -0.03   0.0193  665 ASN A CB    
5329 C  CG    . ASN A 665 ? 0.804  0.7034 0.8435 -0.0218 -0.0284 0.02    665 ASN A CG    
5330 O  OD1   . ASN A 665 ? 0.8196 0.7182 0.8559 -0.0232 -0.0306 0.0206  665 ASN A OD1   
5331 N  ND2   . ASN A 665 ? 0.8087 0.7124 0.8523 -0.0241 -0.0246 0.0198  665 ASN A ND2   
5332 N  N     . ILE A 666 ? 0.7427 0.6456 0.7918 -0.0105 -0.0213 0.0155  666 ILE A N     
5333 C  CA    . ILE A 666 ? 0.7461 0.6484 0.7971 -0.0079 -0.0195 0.015   666 ILE A CA    
5334 C  C     . ILE A 666 ? 0.7438 0.6505 0.7989 -0.0043 -0.0163 0.0135  666 ILE A C     
5335 O  O     . ILE A 666 ? 0.7475 0.6515 0.801  0       -0.0165 0.0133  666 ILE A O     
5336 C  CB    . ILE A 666 ? 0.7512 0.6557 0.8056 -0.0116 -0.0172 0.0154  666 ILE A CB    
5337 C  CG1   . ILE A 666 ? 0.7662 0.6667 0.8173 -0.0151 -0.0205 0.0176  666 ILE A CG1   
5338 C  CG2   . ILE A 666 ? 0.7567 0.6608 0.8134 -0.0092 -0.0153 0.0149  666 ILE A CG2   
5339 C  CD1   . ILE A 666 ? 0.7801 0.6847 0.8323 -0.0197 -0.0194 0.0182  666 ILE A CD1   
5340 N  N     . PHE A 667 ? 0.7374 0.6507 0.7974 -0.006  -0.0134 0.0125  667 PHE A N     
5341 C  CA    . PHE A 667 ? 0.7398 0.6579 0.8047 -0.0031 -0.0105 0.0115  667 PHE A CA    
5342 C  C     . PHE A 667 ? 0.7535 0.6717 0.8174 -0.0002 -0.0123 0.0116  667 PHE A C     
5343 O  O     . PHE A 667 ? 0.7554 0.6732 0.8173 -0.002  -0.0145 0.0118  667 PHE A O     
5344 C  CB    . PHE A 667 ? 0.7313 0.6561 0.8023 -0.0062 -0.0071 0.0104  667 PHE A CB    
5345 C  CG    . PHE A 667 ? 0.7329 0.662  0.8097 -0.004  -0.0037 0.0097  667 PHE A CG    
5346 C  CD1   . PHE A 667 ? 0.7397 0.6722 0.8198 -0.0013 -0.0031 0.0097  667 PHE A CD1   
5347 C  CD2   . PHE A 667 ? 0.7409 0.671  0.8205 -0.0047 -0.0012 0.0094  667 PHE A CD2   
5348 C  CE1   . PHE A 667 ? 0.7451 0.682  0.831  0.0005  0.0001  0.0095  667 PHE A CE1   
5349 C  CE2   . PHE A 667 ? 0.7477 0.6817 0.8326 -0.0028 0.0019  0.0091  667 PHE A CE2   
5350 C  CZ    . PHE A 667 ? 0.7422 0.6796 0.8303 -0.0003 0.0025  0.0092  667 PHE A CZ    
5351 N  N     . ASP A 668 ? 0.7598 0.6788 0.8253 0.0045  -0.011  0.0116  668 ASP A N     
5352 C  CA    . ASP A 668 ? 0.7709 0.6908 0.8366 0.0081  -0.012  0.0118  668 ASP A CA    
5353 C  C     . ASP A 668 ? 0.773  0.7004 0.8458 0.0064  -0.01   0.0114  668 ASP A C     
5354 O  O     . ASP A 668 ? 0.7696 0.7018 0.8482 0.0079  -0.0068 0.0114  668 ASP A O     
5355 C  CB    . ASP A 668 ? 0.7932 0.7121 0.8586 0.0138  -0.0105 0.0122  668 ASP A CB    
5356 C  CG    . ASP A 668 ? 0.8476 0.7654 0.9112 0.0185  -0.0122 0.0128  668 ASP A CG    
5357 O  OD1   . ASP A 668 ? 0.8585 0.7803 0.9255 0.0177  -0.0128 0.0129  668 ASP A OD1   
5358 O  OD2   . ASP A 668 ? 0.8699 0.7826 0.9285 0.023   -0.0131 0.013   668 ASP A OD2   
5359 N  N     . THR A 669 ? 0.7788 0.7066 0.8508 0.0034  -0.0121 0.0113  669 THR A N     
5360 C  CA    . THR A 669 ? 0.788  0.7219 0.8659 0.0016  -0.011  0.0109  669 THR A CA    
5361 C  C     . THR A 669 ? 0.7955 0.7328 0.8776 0.0055  -0.0111 0.0117  669 THR A C     
5362 O  O     . THR A 669 ? 0.791  0.7336 0.8792 0.0043  -0.0103 0.0116  669 THR A O     
5363 C  CB    . THR A 669 ? 0.8081 0.7409 0.883  -0.0028 -0.0134 0.0104  669 THR A CB    
5364 O  OG1   . THR A 669 ? 0.8244 0.7531 0.8944 -0.0016 -0.0173 0.0112  669 THR A OG1   
5365 C  CG2   . THR A 669 ? 0.8163 0.7468 0.888  -0.0066 -0.0127 0.01    669 THR A CG2   
5366 N  N     . GLY A 670 ? 0.8054 0.7396 0.8846 0.0101  -0.0121 0.0125  670 GLY A N     
5367 C  CA    . GLY A 670 ? 0.8179 0.7553 0.9009 0.0146  -0.0119 0.0136  670 GLY A CA    
5368 C  C     . GLY A 670 ? 0.8254 0.7695 0.9165 0.0165  -0.0078 0.0142  670 GLY A C     
5369 O  O     . GLY A 670 ? 0.8241 0.7728 0.9206 0.0193  -0.0073 0.0155  670 GLY A O     
5370 N  N     . PHE A 671 ? 0.8292 0.7742 0.9216 0.0149  -0.0049 0.0136  671 PHE A N     
5371 C  CA    . PHE A 671 ? 0.8353 0.7865 0.9354 0.016   -0.0011 0.0144  671 PHE A CA    
5372 C  C     . PHE A 671 ? 0.8398 0.7968 0.9472 0.0118  -0.0009 0.0141  671 PHE A C     
5373 O  O     . PHE A 671 ? 0.8346 0.7971 0.9493 0.0122  0.0017  0.015   671 PHE A O     
5374 C  CB    . PHE A 671 ? 0.8367 0.7858 0.935  0.016   0.0014  0.0139  671 PHE A CB    
5375 C  CG    . PHE A 671 ? 0.8431 0.7963 0.9462 0.0198  0.0051  0.0152  671 PHE A CG    
5376 C  CD1   . PHE A 671 ? 0.8541 0.805  0.9537 0.0255  0.0057  0.0162  671 PHE A CD1   
5377 C  CD2   . PHE A 671 ? 0.8514 0.8103 0.962  0.0178  0.0078  0.0155  671 PHE A CD2   
5378 C  CE1   . PHE A 671 ? 0.8615 0.8163 0.9651 0.0291  0.0094  0.0177  671 PHE A CE1   
5379 C  CE2   . PHE A 671 ? 0.858  0.8208 0.973  0.0211  0.0113  0.0171  671 PHE A CE2   
5380 C  CZ    . PHE A 671 ? 0.8565 0.8173 0.9679 0.0268  0.0122  0.0182  671 PHE A CZ    
5381 N  N     . PHE A 672 ? 0.8474 0.8027 0.9524 0.0079  -0.0037 0.0131  672 PHE A N     
5382 C  CA    . PHE A 672 ? 0.8561 0.8153 0.9663 0.004   -0.004  0.0126  672 PHE A CA    
5383 C  C     . PHE A 672 ? 0.8672 0.8273 0.9783 0.0035  -0.0074 0.0131  672 PHE A C     
5384 O  O     . PHE A 672 ? 0.8744 0.8304 0.9798 0.0043  -0.0102 0.0131  672 PHE A O     
5385 C  CB    . PHE A 672 ? 0.8571 0.8135 0.9633 -0.0005 -0.0041 0.0106  672 PHE A CB    
5386 C  CG    . PHE A 672 ? 0.8642 0.8202 0.9706 -0.0009 -0.001  0.01    672 PHE A CG    
5387 C  CD1   . PHE A 672 ? 0.8764 0.8278 0.977  0.0003  -0.0007 0.0099  672 PHE A CD1   
5388 C  CD2   . PHE A 672 ? 0.8719 0.8319 0.9842 -0.0027 0.0013  0.0094  672 PHE A CD2   
5389 C  CE1   . PHE A 672 ? 0.8844 0.8354 0.9855 -0.0002 0.0018  0.0094  672 PHE A CE1   
5390 C  CE2   . PHE A 672 ? 0.8813 0.8409 0.9939 -0.0031 0.004   0.0089  672 PHE A CE2   
5391 C  CZ    . PHE A 672 ? 0.8797 0.8349 0.9868 -0.0019 0.0043  0.0089  672 PHE A CZ    
5392 N  N     . HIS A 673 ? 0.8665 0.8314 0.9846 0.0017  -0.0077 0.0134  673 HIS A N     
5393 C  CA    . HIS A 673 ? 0.8763 0.8418 0.9957 0.0005  -0.0113 0.0139  673 HIS A CA    
5394 C  C     . HIS A 673 ? 0.8839 0.8502 1.0049 -0.0042 -0.0121 0.0124  673 HIS A C     
5395 O  O     . HIS A 673 ? 0.8809 0.8515 1.009  -0.0048 -0.0105 0.0128  673 HIS A O     
5396 C  CB    . HIS A 673 ? 0.8828 0.8539 1.0105 0.0039  -0.0114 0.0164  673 HIS A CB    
5397 C  CG    . HIS A 673 ? 0.9087 0.8808 1.0388 0.0024  -0.0154 0.017   673 HIS A CG    
5398 N  ND1   . HIS A 673 ? 0.9287 0.9051 1.0663 0       -0.0165 0.0176  673 HIS A ND1   
5399 C  CD2   . HIS A 673 ? 0.9251 0.8938 1.0505 0.0029  -0.019  0.0171  673 HIS A CD2   
5400 C  CE1   . HIS A 673 ? 0.9356 0.9111 1.073  -0.0009 -0.0207 0.0181  673 HIS A CE1   
5401 N  NE2   . HIS A 673 ? 0.9367 0.9077 1.0668 0.0008  -0.0222 0.0178  673 HIS A NE2   
5402 N  N     . ILE A 674 ? 0.8927 0.8546 1.0068 -0.0073 -0.0145 0.0108  674 ILE A N     
5403 C  CA    . ILE A 674 ? 0.9051 0.8669 1.0193 -0.0114 -0.0154 0.0092  674 ILE A CA    
5404 C  C     . ILE A 674 ? 0.9162 0.8787 1.0327 -0.0125 -0.0195 0.0098  674 ILE A C     
5405 O  O     . ILE A 674 ? 0.9233 0.8826 1.0346 -0.0129 -0.0226 0.0099  674 ILE A O     
5406 C  CB    . ILE A 674 ? 0.9166 0.8736 1.0222 -0.0142 -0.0148 0.0071  674 ILE A CB    
5407 C  CG1   . ILE A 674 ? 0.9337 0.886  1.0313 -0.0141 -0.0172 0.0074  674 ILE A CG1   
5408 C  CG2   . ILE A 674 ? 0.9224 0.8798 1.0285 -0.0135 -0.0107 0.0066  674 ILE A CG2   
5409 C  CD1   . ILE A 674 ? 0.9548 0.903  1.0445 -0.0173 -0.0168 0.0059  674 ILE A CD1   
5410 N  N     . GLU A 675 ? 0.9141 0.8811 1.0392 -0.0129 -0.0197 0.0107  675 GLU A N     
5411 C  CA    . GLU A 675 ? 0.9194 0.8877 1.0485 -0.014  -0.0239 0.0116  675 GLU A CA    
5412 C  C     . GLU A 675 ? 0.9276 0.8907 1.0491 -0.0178 -0.0271 0.0094  675 GLU A C     
5413 O  O     . GLU A 675 ? 0.9311 0.8922 1.0503 -0.0184 -0.0311 0.0099  675 GLU A O     
5414 C  CB    . GLU A 675 ? 0.9407 0.9145 1.0805 -0.0143 -0.0233 0.0129  675 GLU A CB    
5415 C  CG    . GLU A 675 ? 0.9984 0.9736 1.1433 -0.016  -0.0281 0.014   675 GLU A CG    
5416 C  CD    . GLU A 675 ? 1.0693 1.0496 1.225  -0.0168 -0.0281 0.0156  675 GLU A CD    
5417 O  OE1   . GLU A 675 ? 1.0822 1.0652 1.2414 -0.016  -0.0241 0.0157  675 GLU A OE1   
5418 O  OE2   . GLU A 675 ? 1.088  1.0695 1.2488 -0.0183 -0.0323 0.0169  675 GLU A OE2   
5419 N  N     . GLY A 676 ? 0.9269 0.8877 1.0441 -0.0202 -0.0252 0.007   676 GLY A N     
5420 C  CA    . GLY A 676 ? 0.932  0.8878 1.0411 -0.0235 -0.0272 0.0047  676 GLY A CA    
5421 C  C     . GLY A 676 ? 0.929  0.8838 1.0359 -0.0252 -0.0242 0.0024  676 GLY A C     
5422 O  O     . GLY A 676 ? 0.9226 0.8809 1.0358 -0.0243 -0.0213 0.0026  676 GLY A O     
5423 P  P     . DC  B 1   ? 0.6719 0.6281 0.8505 -0.0181 0.0323  0.0009  1   DC  E P     
5424 O  OP1   . DC  B 1   ? 0.671  0.6265 0.8435 -0.0171 0.0319  0.0019  1   DC  E OP1   
5425 O  OP2   . DC  B 1   ? 0.6718 0.6273 0.8528 -0.0192 0.0324  -0.0002 1   DC  E OP2   
5426 O  "O5'" . DC  B 1   ? 0.6662 0.6258 0.8487 -0.0189 0.0329  -0.0008 1   DC  E "O5'" 
5427 C  "C5'" . DC  B 1   ? 0.6626 0.6241 0.843  -0.0194 0.0331  -0.0022 1   DC  E "C5'" 
5428 C  "C4'" . DC  B 1   ? 0.656  0.6192 0.8403 -0.0206 0.0332  -0.0048 1   DC  E "C4'" 
5429 O  "O4'" . DC  B 1   ? 0.649  0.6128 0.8379 -0.0208 0.0327  -0.0043 1   DC  E "O4'" 
5430 C  "C3'" . DC  B 1   ? 0.6582 0.6207 0.8447 -0.0212 0.0339  -0.0066 1   DC  E "C3'" 
5431 O  "O3'" . DC  B 1   ? 0.6698 0.6327 0.8529 -0.0215 0.0346  -0.0077 1   DC  E "O3'" 
5432 C  "C2'" . DC  B 1   ? 0.6505 0.6139 0.8411 -0.0219 0.0336  -0.0087 1   DC  E "C2'" 
5433 C  "C1'" . DC  B 1   ? 0.6438 0.6076 0.8365 -0.0217 0.0326  -0.0067 1   DC  E "C1'" 
5434 N  N1    . DC  B 1   ? 0.632  0.5948 0.8295 -0.0218 0.0323  -0.0058 1   DC  E N1    
5435 C  C2    . DC  B 1   ? 0.6232 0.5858 0.8253 -0.0226 0.0316  -0.0077 1   DC  E C2    
5436 O  O2    . DC  B 1   ? 0.6198 0.5829 0.8216 -0.0231 0.0313  -0.0101 1   DC  E O2    
5437 N  N3    . DC  B 1   ? 0.6213 0.5828 0.8278 -0.0227 0.0311  -0.0068 1   DC  E N3    
5438 C  C4    . DC  B 1   ? 0.6227 0.5832 0.8286 -0.0221 0.0314  -0.0042 1   DC  E C4    
5439 N  N4    . DC  B 1   ? 0.6225 0.5818 0.8326 -0.0223 0.0308  -0.0033 1   DC  E N4    
5440 C  C5    . DC  B 1   ? 0.6262 0.5866 0.827  -0.0211 0.032   -0.0024 1   DC  E C5    
5441 C  C6    . DC  B 1   ? 0.6303 0.5918 0.8271 -0.021  0.0325  -0.0033 1   DC  E C6    
5442 P  P     . DA  B 2   ? 0.6807 0.6431 0.8653 -0.0218 0.0356  -0.0081 2   DA  E P     
5443 O  OP1   . DA  B 2   ? 0.6847 0.6481 0.8653 -0.0221 0.0364  -0.0085 2   DA  E OP1   
5444 O  OP2   . DA  B 2   ? 0.6818 0.6422 0.8676 -0.0214 0.0348  -0.0057 2   DA  E OP2   
5445 O  "O5'" . DA  B 2   ? 0.6798 0.643  0.8694 -0.0219 0.0362  -0.0106 2   DA  E "O5'" 
5446 C  "C5'" . DA  B 2   ? 0.6798 0.6439 0.8683 -0.0221 0.0367  -0.0133 2   DA  E "C5'" 
5447 C  "C4'" . DA  B 2   ? 0.6791 0.6428 0.8723 -0.0219 0.0366  -0.0155 2   DA  E "C4'" 
5448 O  "O4'" . DA  B 2   ? 0.6755 0.6382 0.8727 -0.0221 0.0352  -0.0142 2   DA  E "O4'" 
5449 C  "C3'" . DA  B 2   ? 0.681  0.645  0.8772 -0.0214 0.0382  -0.0166 2   DA  E "C3'" 
5450 O  "O3'" . DA  B 2   ? 0.6822 0.6464 0.878  -0.0208 0.0391  -0.0198 2   DA  E "O3'" 
5451 C  "C2'" . DA  B 2   ? 0.678  0.6408 0.8796 -0.0214 0.0372  -0.0155 2   DA  E "C2'" 
5452 C  "C1'" . DA  B 2   ? 0.6732 0.635  0.8752 -0.0219 0.0354  -0.0151 2   DA  E "C1'" 
5453 N  N9    . DA  B 2   ? 0.6651 0.6258 0.8703 -0.022  0.0343  -0.0127 2   DA  E N9    
5454 C  C8    . DA  B 2   ? 0.6623 0.6225 0.8657 -0.0219 0.0341  -0.0098 2   DA  E C8    
5455 N  N7    . DA  B 2   ? 0.6583 0.6171 0.8647 -0.0219 0.0331  -0.0081 2   DA  E N7    
5456 C  C5    . DA  B 2   ? 0.6555 0.614  0.8665 -0.0222 0.0326  -0.01   2   DA  E C5    
5457 C  C6    . DA  B 2   ? 0.6505 0.6077 0.8663 -0.0225 0.0314  -0.0094 2   DA  E C6    
5458 N  N6    . DA  B 2   ? 0.649  0.6049 0.8654 -0.0225 0.0307  -0.0066 2   DA  E N6    
5459 N  N1    . DA  B 2   ? 0.6485 0.6053 0.8679 -0.0227 0.0308  -0.0118 2   DA  E N1    
5460 C  C2    . DA  B 2   ? 0.6497 0.6073 0.8675 -0.0225 0.0314  -0.0147 2   DA  E C2    
5461 N  N3    . DA  B 2   ? 0.6538 0.6128 0.867  -0.0222 0.0328  -0.0155 2   DA  E N3    
5462 C  C4    . DA  B 2   ? 0.6583 0.6179 0.8685 -0.0222 0.0333  -0.0129 2   DA  E C4    
5463 P  P     . DT  B 3   ? 0.6796 0.6452 0.876  -0.0199 0.0417  -0.0211 3   DT  E P     
5464 O  OP1   . DT  B 3   ? 0.6828 0.6493 0.8735 -0.0196 0.043   -0.0226 3   DT  E OP1   
5465 O  OP2   . DT  B 3   ? 0.6774 0.6439 0.8769 -0.0202 0.0422  -0.0184 3   DT  E OP2   
5466 O  "O5'" . DT  B 3   ? 0.6734 0.6376 0.8741 -0.0189 0.0415  -0.0239 3   DT  E "O5'" 
5467 C  "C5'" . DT  B 3   ? 0.6698 0.6319 0.8693 -0.0188 0.0398  -0.0262 3   DT  E "C5'" 
5468 C  "C4'" . DT  B 3   ? 0.6664 0.6267 0.8714 -0.0183 0.0387  -0.0275 3   DT  E "C4'" 
5469 O  "O4'" . DT  B 3   ? 0.6647 0.6248 0.874  -0.0193 0.0372  -0.0246 3   DT  E "O4'" 
5470 C  "C3'" . DT  B 3   ? 0.6647 0.6257 0.8726 -0.0166 0.0409  -0.0291 3   DT  E "C3'" 
5471 O  "O3'" . DT  B 3   ? 0.664  0.6225 0.8721 -0.0153 0.0403  -0.0327 3   DT  E "O3'" 
5472 C  "C2'" . DT  B 3   ? 0.6622 0.6234 0.8763 -0.0171 0.0403  -0.0266 3   DT  E "C2'" 
5473 C  "C1'" . DT  B 3   ? 0.6629 0.6224 0.8776 -0.0186 0.0374  -0.025  3   DT  E "C1'" 
5474 N  N1    . DT  B 3   ? 0.6625 0.6222 0.8801 -0.0195 0.0367  -0.0215 3   DT  E N1    
5475 C  C2    . DT  B 3   ? 0.6622 0.62   0.8842 -0.02   0.0348  -0.0207 3   DT  E C2    
5476 O  O2    . DT  B 3   ? 0.6616 0.6177 0.8858 -0.0199 0.0334  -0.0225 3   DT  E O2    
5477 N  N3    . DT  B 3   ? 0.6625 0.62   0.886  -0.0206 0.0342  -0.0175 3   DT  E N3    
5478 C  C4    . DT  B 3   ? 0.6648 0.6234 0.8857 -0.0208 0.0351  -0.0152 3   DT  E C4    
5479 O  O4    . DT  B 3   ? 0.6666 0.6239 0.8884 -0.0212 0.034   -0.0126 3   DT  E O4    
5480 C  C5    . DT  B 3   ? 0.6645 0.6251 0.8813 -0.0205 0.0369  -0.0162 3   DT  E C5    
5481 C  C7    . DT  B 3   ? 0.6638 0.6253 0.8777 -0.0209 0.0375  -0.0137 3   DT  E C7    
5482 C  C6    . DT  B 3   ? 0.6639 0.6252 0.8793 -0.0199 0.0378  -0.0192 3   DT  E C6    
5483 P  P     . DT  B 4   ? 0.6604 0.6193 0.8701 -0.0128 0.0429  -0.0353 4   DT  E P     
5484 O  OP1   . DT  B 4   ? 0.6656 0.6224 0.8695 -0.0112 0.0432  -0.039  4   DT  E OP1   
5485 O  OP2   . DT  B 4   ? 0.6558 0.6187 0.8674 -0.0126 0.0458  -0.0329 4   DT  E OP2   
5486 O  "O5'" . DT  B 4   ? 0.6493 0.6058 0.8657 -0.0125 0.0408  -0.0357 4   DT  E "O5'" 
5487 C  "C5'" . DT  B 4   ? 0.636  0.5887 0.8525 -0.0131 0.0374  -0.0372 4   DT  E "C5'" 
5488 C  "C4'" . DT  B 4   ? 0.6199 0.5711 0.8433 -0.0138 0.0352  -0.0359 4   DT  E "C4'" 
5489 O  "O4'" . DT  B 4   ? 0.6113 0.5647 0.8372 -0.0155 0.0352  -0.0318 4   DT  E "O4'" 
5490 C  "C3'" . DT  B 4   ? 0.6121 0.5628 0.8403 -0.0117 0.0362  -0.0377 4   DT  E "C3'" 
5491 O  "O3'" . DT  B 4   ? 0.6093 0.5563 0.8414 -0.0121 0.0329  -0.0384 4   DT  E "O3'" 
5492 C  "C2'" . DT  B 4   ? 0.6068 0.5609 0.8389 -0.0123 0.0379  -0.0343 4   DT  E "C2'" 
5493 C  "C1'" . DT  B 4   ? 0.6053 0.5589 0.8371 -0.0149 0.0355  -0.0311 4   DT  E "C1'" 
5494 N  N1    . DT  B 4   ? 0.6009 0.5569 0.8337 -0.016  0.0364  -0.0274 4   DT  E N1    
5495 C  C2    . DT  B 4   ? 0.6001 0.555  0.8368 -0.0172 0.0345  -0.0247 4   DT  E C2    
5496 O  O2    . DT  B 4   ? 0.6006 0.5529 0.8401 -0.0177 0.0321  -0.025  4   DT  E O2    
5497 N  N3    . DT  B 4   ? 0.5991 0.5555 0.8358 -0.018  0.0351  -0.0216 4   DT  E N3    
5498 C  C4    . DT  B 4   ? 0.5995 0.5585 0.8333 -0.0178 0.0373  -0.0207 4   DT  E C4    
5499 O  O4    . DT  B 4   ? 0.6025 0.562  0.8365 -0.0186 0.037   -0.0178 4   DT  E O4    
5500 C  C5    . DT  B 4   ? 0.5973 0.5581 0.8278 -0.0166 0.0395  -0.0234 4   DT  E C5    
5501 C  C7    . DT  B 4   ? 0.597  0.5608 0.8243 -0.0165 0.0419  -0.0224 4   DT  E C7    
5502 C  C6    . DT  B 4   ? 0.598  0.5571 0.8279 -0.0157 0.0391  -0.0267 4   DT  E C6    
5503 P  P     . DC  B 5   ? 0.6041 0.5483 0.8394 -0.0095 0.0325  -0.0418 5   DC  E P     
5504 O  OP1   . DC  B 5   ? 0.6076 0.5473 0.839  -0.009  0.03    -0.0452 5   DC  E OP1   
5505 O  OP2   . DC  B 5   ? 0.5997 0.5471 0.836  -0.0071 0.0366  -0.0425 5   DC  E OP2   
5506 O  "O5'" . DC  B 5   ? 0.5948 0.5375 0.8373 -0.011  0.0298  -0.0395 5   DC  E "O5'" 
5507 C  "C5'" . DC  B 5   ? 0.5861 0.5284 0.8293 -0.014  0.0272  -0.0362 5   DC  E "C5'" 
5508 C  "C4'" . DC  B 5   ? 0.578  0.5205 0.8273 -0.015  0.0262  -0.0332 5   DC  E "C4'" 
5509 O  "O4'" . DC  B 5   ? 0.5724 0.5186 0.8213 -0.0155 0.0286  -0.0302 5   DC  E "O4'" 
5510 C  "C3'" . DC  B 5   ? 0.5763 0.517  0.831  -0.0132 0.0258  -0.0349 5   DC  E "C3'" 
5511 O  "O3'" . DC  B 5   ? 0.5775 0.5154 0.8368 -0.0147 0.0224  -0.0333 5   DC  E "O3'" 
5512 C  "C2'" . DC  B 5   ? 0.5706 0.515  0.8275 -0.0124 0.0289  -0.0333 5   DC  E "C2'" 
5513 C  "C1'" . DC  B 5   ? 0.5682 0.5148 0.8224 -0.0147 0.0292  -0.0295 5   DC  E "C1'" 
5514 N  N1    . DC  B 5   ? 0.5626 0.5131 0.8157 -0.0142 0.0323  -0.0282 5   DC  E N1    
5515 C  C2    . DC  B 5   ? 0.5585 0.5099 0.8148 -0.0151 0.0321  -0.0249 5   DC  E C2    
5516 O  O2    . DC  B 5   ? 0.5614 0.5104 0.8209 -0.0162 0.0296  -0.0232 5   DC  E O2    
5517 N  N3    . DC  B 5   ? 0.5514 0.506  0.807  -0.0149 0.0345  -0.0234 5   DC  E N3    
5518 C  C4    . DC  B 5   ? 0.5482 0.5055 0.8002 -0.0138 0.0373  -0.025  5   DC  E C4    
5519 N  N4    . DC  B 5   ? 0.5415 0.502  0.7933 -0.0138 0.0393  -0.0231 5   DC  E N4    
5520 C  C5    . DC  B 5   ? 0.5558 0.5121 0.804  -0.0126 0.0378  -0.0286 5   DC  E C5    
5521 C  C6    . DC  B 5   ? 0.5606 0.5134 0.8095 -0.0129 0.0351  -0.0301 5   DC  E C6    
5522 P  P     . DC  B 6   ? 0.5745 0.509  0.8394 -0.0132 0.0206  -0.0354 6   DC  E P     
5523 O  OP1   . DC  B 6   ? 0.5714 0.5019 0.8383 -0.015  0.0163  -0.0347 6   DC  E OP1   
5524 O  OP2   . DC  B 6   ? 0.5759 0.5104 0.8392 -0.0099 0.0228  -0.0396 6   DC  E OP2   
5525 O  "O5'" . DC  B 6   ? 0.5724 0.5089 0.8423 -0.0134 0.0216  -0.0324 6   DC  E "O5'" 
5526 C  "C5'" . DC  B 6   ? 0.5732 0.5097 0.8441 -0.016  0.02    -0.0282 6   DC  E "C5'" 
5527 C  "C4'" . DC  B 6   ? 0.5711 0.5091 0.8455 -0.016  0.0209  -0.0257 6   DC  E "C4'" 
5528 O  "O4'" . DC  B 6   ? 0.5709 0.5129 0.8425 -0.0153 0.0243  -0.0253 6   DC  E "O4'" 
5529 C  "C3'" . DC  B 6   ? 0.5714 0.5081 0.8522 -0.0142 0.0203  -0.0272 6   DC  E "C3'" 
5530 O  "O3'" . DC  B 6   ? 0.5777 0.5126 0.8624 -0.0157 0.018   -0.024  6   DC  E "O3'" 
5531 C  "C2'" . DC  B 6   ? 0.5661 0.5069 0.8473 -0.0122 0.024   -0.0281 6   DC  E "C2'" 
5532 C  "C1'" . DC  B 6   ? 0.5652 0.5087 0.8416 -0.0139 0.0255  -0.0253 6   DC  E "C1'" 
5533 N  N1    . DC  B 6   ? 0.5595 0.5071 0.8334 -0.0125 0.0292  -0.0262 6   DC  E N1    
5534 C  C2    . DC  B 6   ? 0.5562 0.5066 0.8303 -0.0133 0.0305  -0.0231 6   DC  E C2    
5535 O  O2    . DC  B 6   ? 0.5564 0.5052 0.832  -0.0149 0.0284  -0.02   6   DC  E O2    
5536 N  N3    . DC  B 6   ? 0.5525 0.5068 0.8244 -0.0123 0.0338  -0.0235 6   DC  E N3    
5537 C  C4    . DC  B 6   ? 0.5513 0.5067 0.8206 -0.0104 0.036   -0.027  6   DC  E C4    
5538 N  N4    . DC  B 6   ? 0.5488 0.5082 0.8159 -0.0094 0.0394  -0.0271 6   DC  E N4    
5539 C  C5    . DC  B 6   ? 0.5545 0.5066 0.823  -0.0093 0.0347  -0.0304 6   DC  E C5    
5540 C  C6    . DC  B 6   ? 0.5577 0.506  0.8289 -0.0105 0.0311  -0.0298 6   DC  E C6    
5541 P  P     . DT  B 7   ? 0.5832 0.5157 0.8753 -0.0146 0.016   -0.0247 7   DT  E P     
5542 O  OP1   . DT  B 7   ? 0.5817 0.5098 0.8754 -0.0163 0.0121  -0.0236 7   DT  E OP1   
5543 O  OP2   . DT  B 7   ? 0.5807 0.5143 0.8748 -0.0114 0.018   -0.0287 7   DT  E OP2   
5544 O  "O5'" . DT  B 7   ? 0.5933 0.5274 0.8879 -0.0153 0.0165  -0.0212 7   DT  E "O5'" 
5545 C  "C5'" . DT  B 7   ? 0.6035 0.5374 0.8942 -0.0176 0.0158  -0.0173 7   DT  E "C5'" 
5546 C  "C4'" . DT  B 7   ? 0.6117 0.5473 0.9039 -0.0177 0.0165  -0.0147 7   DT  E "C4'" 
5547 O  "O4'" . DT  B 7   ? 0.6087 0.5487 0.8989 -0.0166 0.02    -0.0157 7   DT  E "O4'" 
5548 C  "C3'" . DT  B 7   ? 0.621  0.5556 0.9209 -0.0169 0.015   -0.0144 7   DT  E "C3'" 
5549 O  "O3'" . DT  B 7   ? 0.6394 0.5725 0.9396 -0.0184 0.0132  -0.0106 7   DT  E "O3'" 
5550 C  "C2'" . DT  B 7   ? 0.6114 0.5504 0.9141 -0.0145 0.0183  -0.0166 7   DT  E "C2'" 
5551 C  "C1'" . DT  B 7   ? 0.6055 0.5476 0.9017 -0.0152 0.0209  -0.0158 7   DT  E "C1'" 
5552 N  N1    . DT  B 7   ? 0.5989 0.5451 0.8945 -0.0131 0.0246  -0.0186 7   DT  E N1    
5553 C  C2    . DT  B 7   ? 0.5979 0.5481 0.8927 -0.013  0.0271  -0.0171 7   DT  E C2    
5554 O  O2    . DT  B 7   ? 0.5991 0.5492 0.8933 -0.0147 0.026   -0.0137 7   DT  E O2    
5555 N  N3    . DT  B 7   ? 0.5951 0.5492 0.8894 -0.0109 0.0307  -0.0197 7   DT  E N3    
5556 C  C4    . DT  B 7   ? 0.5925 0.5463 0.8863 -0.0086 0.032   -0.0238 7   DT  E C4    
5557 O  O4    . DT  B 7   ? 0.5907 0.5479 0.8831 -0.0066 0.0355  -0.0257 7   DT  E O4    
5558 C  C5    . DT  B 7   ? 0.5929 0.5419 0.8876 -0.0088 0.0289  -0.0253 7   DT  E C5    
5559 C  C7    . DT  B 7   ? 0.5935 0.5407 0.8875 -0.0064 0.0293  -0.0298 7   DT  E C7    
5560 C  C6    . DT  B 7   ? 0.5952 0.5409 0.891  -0.0111 0.0254  -0.0226 7   DT  E C6    
5561 P  P     . DC  B 8   ? 0.6556 0.5855 0.9627 -0.0185 0.0099  -0.0091 8   DC  E P     
5562 O  OP1   . DC  B 8   ? 0.6602 0.5858 0.9637 -0.0207 0.007   -0.0058 8   DC  E OP1   
5563 O  OP2   . DC  B 8   ? 0.6523 0.5816 0.9649 -0.0168 0.0096  -0.0124 8   DC  E OP2   
5564 O  "O5'" . DC  B 8   ? 0.666  0.5988 0.977  -0.0179 0.011   -0.0077 8   DC  E "O5'" 
5565 C  "C5'" . DC  B 8   ? 0.6791 0.6123 0.9856 -0.0193 0.0109  -0.0046 8   DC  E "C5'" 
5566 C  "C4'" . DC  B 8   ? 0.6871 0.6249 0.997  -0.0184 0.0132  -0.0043 8   DC  E "C4'" 
5567 O  "O4'" . DC  B 8   ? 0.6903 0.6328 0.9996 -0.0166 0.0172  -0.0075 8   DC  E "O4'" 
5568 C  "C3'" . DC  B 8   ? 0.6864 0.6249 1.0059 -0.0176 0.0118  -0.0034 8   DC  E "C3'" 
5569 O  "O3'" . DC  B 8   ? 0.6876 0.6263 1.0078 -0.0189 0.0104  0.0002  8   DC  E "O3'" 
5570 C  "C2'" . DC  B 8   ? 0.6838 0.6279 1.008  -0.015  0.0157  -0.0065 8   DC  E "C2'" 
5571 C  "C1'" . DC  B 8   ? 0.6862 0.6329 1.0026 -0.015  0.019   -0.0077 8   DC  E "C1'" 
5572 N  N1    . DC  B 8   ? 0.6833 0.6336 1      -0.0125 0.0228  -0.0117 8   DC  E N1    
5573 C  C2    . DC  B 8   ? 0.6761 0.6315 0.9905 -0.0117 0.0266  -0.0121 8   DC  E C2    
5574 O  O2    . DC  B 8   ? 0.6689 0.6256 0.981  -0.0133 0.0267  -0.0092 8   DC  E O2    
5575 N  N3    . DC  B 8   ? 0.6781 0.6361 0.9919 -0.0092 0.03    -0.0158 8   DC  E N3    
5576 C  C4    . DC  B 8   ? 0.6825 0.6381 0.9982 -0.0074 0.0294  -0.019  8   DC  E C4    
5577 N  N4    . DC  B 8   ? 0.683  0.6407 0.9974 -0.0046 0.0326  -0.0227 8   DC  E N4    
5578 C  C5    . DC  B 8   ? 0.6847 0.6353 1.0034 -0.0084 0.0252  -0.0185 8   DC  E C5    
5579 C  C6    . DC  B 8   ? 0.685  0.6333 1.0041 -0.0109 0.0222  -0.0148 8   DC  E C6    
5580 O  "O5'" . DG  C 1   ? 0.6567 0.6614 0.9542 0.0017  0.0684  -0.0155 1   DG  F "O5'" 
5581 C  "C5'" . DG  C 1   ? 0.6564 0.656  0.9576 0.0008  0.064   -0.0161 1   DG  F "C5'" 
5582 C  "C4'" . DG  C 1   ? 0.653  0.6524 0.9596 -0.0027 0.0602  -0.0112 1   DG  F "C4'" 
5583 O  "O4'" . DG  C 1   ? 0.649  0.6443 0.9611 -0.0029 0.0564  -0.0116 1   DG  F "O4'" 
5584 C  "C3'" . DG  C 1   ? 0.6552 0.651  0.9543 -0.0063 0.0571  -0.0096 1   DG  F "C3'" 
5585 O  "O3'" . DG  C 1   ? 0.6554 0.6525 0.959  -0.0091 0.0548  -0.0046 1   DG  F "O3'" 
5586 C  "C2'" . DG  C 1   ? 0.6538 0.6427 0.9501 -0.0069 0.0532  -0.0121 1   DG  F "C2'" 
5587 C  "C1'" . DG  C 1   ? 0.6472 0.6361 0.9533 -0.0056 0.052   -0.0118 1   DG  F "C1'" 
5588 N  N9    . DG  C 1   ? 0.6392 0.6234 0.9443 -0.0041 0.0505  -0.0158 1   DG  F N9    
5589 C  C8    . DG  C 1   ? 0.6372 0.6207 0.9384 -0.0013 0.0528  -0.0203 1   DG  F C8    
5590 N  N7    . DG  C 1   ? 0.6361 0.6146 0.9374 -0.0007 0.0502  -0.0229 1   DG  F N7    
5591 C  C5    . DG  C 1   ? 0.6332 0.6092 0.9388 -0.0033 0.0461  -0.0198 1   DG  F C5    
5592 C  C6    . DG  C 1   ? 0.6293 0.5999 0.9368 -0.004  0.042   -0.0204 1   DG  F C6    
5593 O  O6    . DG  C 1   ? 0.6271 0.5941 0.9335 -0.0027 0.041   -0.0238 1   DG  F O6    
5594 N  N1    . DG  C 1   ? 0.6284 0.5976 0.9393 -0.0067 0.0387  -0.0165 1   DG  F N1    
5595 C  C2    . DG  C 1   ? 0.6288 0.601  0.9411 -0.0084 0.0389  -0.0125 1   DG  F C2    
5596 N  N2    . DG  C 1   ? 0.6291 0.5983 0.9439 -0.0107 0.035   -0.0092 1   DG  F N2    
5597 N  N3    . DG  C 1   ? 0.6298 0.6072 0.9409 -0.0079 0.0426  -0.0118 1   DG  F N3    
5598 C  C4    . DG  C 1   ? 0.6341 0.6133 0.9418 -0.0053 0.0462  -0.0155 1   DG  F C4    
5599 P  P     . DA  C 2   ? 0.6598 0.654  0.9561 -0.0125 0.052   -0.0021 2   DA  F P     
5600 O  OP1   . DA  C 2   ? 0.6585 0.6569 0.9598 -0.0143 0.052   0.0029  2   DA  F OP1   
5601 O  OP2   . DA  C 2   ? 0.6652 0.6579 0.9513 -0.0121 0.0537  -0.0053 2   DA  F OP2   
5602 O  "O5'" . DA  C 2   ? 0.6395 0.6268 0.9357 -0.0143 0.0466  -0.0017 2   DA  F "O5'" 
5603 C  "C5'" . DA  C 2   ? 0.6071 0.5938 0.9117 -0.0152 0.0436  0.0013  2   DA  F "C5'" 
5604 C  "C4'" . DA  C 2   ? 0.5798 0.5593 0.8813 -0.0169 0.0387  0.0017  2   DA  F "C4'" 
5605 O  "O4'" . DA  C 2   ? 0.5701 0.5467 0.8708 -0.0153 0.0386  -0.0022 2   DA  F "O4'" 
5606 C  "C3'" . DA  C 2   ? 0.5642 0.5399 0.8558 -0.0189 0.0368  0.0023  2   DA  F "C3'" 
5607 O  "O3'" . DA  C 2   ? 0.5517 0.5221 0.843  -0.0208 0.0321  0.005   2   DA  F "O3'" 
5608 C  "C2'" . DA  C 2   ? 0.5649 0.5383 0.8502 -0.0177 0.038   -0.0019 2   DA  F "C2'" 
5609 C  "C1'" . DA  C 2   ? 0.5624 0.5345 0.8541 -0.0163 0.0372  -0.0036 2   DA  F "C1'" 
5610 N  N9    . DA  C 2   ? 0.5493 0.5213 0.8389 -0.0143 0.0392  -0.008  2   DA  F N9    
5611 C  C8    . DA  C 2   ? 0.5445 0.5199 0.8311 -0.0125 0.0432  -0.0106 2   DA  F C8    
5612 N  N7    . DA  C 2   ? 0.5405 0.5142 0.8258 -0.0107 0.0438  -0.0145 2   DA  F N7    
5613 C  C5    . DA  C 2   ? 0.5366 0.5058 0.8246 -0.0115 0.0401  -0.0142 2   DA  F C5    
5614 C  C6    . DA  C 2   ? 0.5304 0.4959 0.8187 -0.0107 0.0385  -0.017  2   DA  F C6    
5615 N  N6    . DA  C 2   ? 0.5258 0.491  0.8115 -0.0088 0.0402  -0.0209 2   DA  F N6    
5616 N  N1    . DA  C 2   ? 0.5317 0.4932 0.8228 -0.0121 0.0347  -0.0154 2   DA  F N1    
5617 C  C2    . DA  C 2   ? 0.5341 0.4951 0.827  -0.0139 0.0327  -0.0115 2   DA  F C2    
5618 N  N3    . DA  C 2   ? 0.5367 0.5005 0.8294 -0.0148 0.0336  -0.0088 2   DA  F N3    
5619 C  C4    . DA  C 2   ? 0.5404 0.5085 0.8308 -0.0136 0.0374  -0.0102 2   DA  F C4    
5620 P  P     . DG  C 3   ? 0.5446 0.5109 0.827  -0.0228 0.0294  0.007   3   DG  F P     
5621 O  OP1   . DG  C 3   ? 0.5455 0.5081 0.8307 -0.0245 0.025   0.0108  3   DG  F OP1   
5622 O  OP2   . DG  C 3   ? 0.5455 0.5156 0.8235 -0.0228 0.0325  0.0068  3   DG  F OP2   
5623 O  "O5'" . DG  C 3   ? 0.5305 0.492  0.8061 -0.0224 0.0285  0.0043  3   DG  F "O5'" 
5624 C  "C5'" . DG  C 3   ? 0.5077 0.4653 0.7861 -0.0222 0.026   0.0039  3   DG  F "C5'" 
5625 C  "C4'" . DG  C 3   ? 0.4843 0.4391 0.7567 -0.0218 0.0262  0.0014  3   DG  F "C4'" 
5626 O  "O4'" . DG  C 3   ? 0.4759 0.4339 0.7505 -0.0201 0.0293  -0.0022 3   DG  F "O4'" 
5627 C  "C3'" . DG  C 3   ? 0.4698 0.4233 0.7328 -0.0224 0.0265  0.0015  3   DG  F "C3'" 
5628 O  "O3'" . DG  C 3   ? 0.4574 0.4064 0.716  -0.0226 0.0246  0.0014  3   DG  F "O3'" 
5629 C  "C2'" . DG  C 3   ? 0.469  0.4269 0.7307 -0.0213 0.0304  -0.0016 3   DG  F "C2'" 
5630 C  "C1'" . DG  C 3   ? 0.4706 0.4284 0.7377 -0.02   0.0307  -0.004  3   DG  F "C1'" 
5631 N  N9    . DG  C 3   ? 0.4636 0.425  0.7315 -0.0184 0.034   -0.0074 3   DG  F N9    
5632 C  C8    . DG  C 3   ? 0.4609 0.4265 0.727  -0.0177 0.0373  -0.0083 3   DG  F C8    
5633 N  N7    . DG  C 3   ? 0.4591 0.4264 0.7252 -0.016  0.0396  -0.0118 3   DG  F N7    
5634 C  C5    . DG  C 3   ? 0.4577 0.4215 0.7259 -0.0156 0.0376  -0.0133 3   DG  F C5    
5635 C  C6    . DG  C 3   ? 0.4561 0.4189 0.725  -0.014  0.0382  -0.0169 3   DG  F C6    
5636 O  O6    . DG  C 3   ? 0.4542 0.419  0.7216 -0.0122 0.0408  -0.0199 3   DG  F O6    
5637 N  N1    . DG  C 3   ? 0.4564 0.4153 0.728  -0.0145 0.0351  -0.0169 3   DG  F N1    
5638 C  C2    . DG  C 3   ? 0.4563 0.4124 0.7291 -0.0162 0.0321  -0.0137 3   DG  F C2    
5639 N  N2    . DG  C 3   ? 0.4548 0.4073 0.7299 -0.0166 0.0295  -0.014  3   DG  F N2    
5640 N  N3    . DG  C 3   ? 0.4564 0.413  0.728  -0.0175 0.0316  -0.0105 3   DG  F N3    
5641 C  C4    . DG  C 3   ? 0.4586 0.4191 0.7281 -0.0172 0.0343  -0.0105 3   DG  F C4    
5642 P  P     . DG  C 4   ? 0.4474 0.3916 0.6986 -0.0235 0.0219  0.004   4   DG  F P     
5643 O  OP1   . DG  C 4   ? 0.4502 0.3917 0.7042 -0.0243 0.0188  0.007   4   DG  F OP1   
5644 O  OP2   . DG  C 4   ? 0.4479 0.3937 0.6923 -0.0235 0.0236  0.0036  4   DG  F OP2   
5645 O  "O5'" . DG  C 4   ? 0.431  0.3716 0.6801 -0.0233 0.0207  0.0035  4   DG  F "O5'" 
5646 C  "C5'" . DG  C 4   ? 0.41   0.3484 0.6646 -0.0233 0.0188  0.0037  4   DG  F "C5'" 
5647 C  "C4'" . DG  C 4   ? 0.3907 0.33   0.6471 -0.0228 0.02    0.0012  4   DG  F "C4'" 
5648 O  "O4'" . DG  C 4   ? 0.3778 0.3219 0.637  -0.022  0.0229  -0.0017 4   DG  F "O4'" 
5649 C  "C3'" . DG  C 4   ? 0.388  0.3257 0.6379 -0.0229 0.0201  0.0013  4   DG  F "C3'" 
5650 O  "O3'" . DG  C 4   ? 0.3948 0.3303 0.6475 -0.0231 0.0187  0.0012  4   DG  F "O3'" 
5651 C  "C2'" . DG  C 4   ? 0.3795 0.3216 0.6281 -0.0224 0.0231  -0.0013 4   DG  F "C2'" 
5652 C  "C1'" . DG  C 4   ? 0.3706 0.3153 0.6263 -0.0218 0.0242  -0.0036 4   DG  F "C1'" 
5653 N  N9    . DG  C 4   ? 0.3605 0.3093 0.6153 -0.021  0.0271  -0.0059 4   DG  F N9    
5654 C  C8    . DG  C 4   ? 0.3587 0.3099 0.6105 -0.0211 0.0286  -0.0052 4   DG  F C8    
5655 N  N7    . DG  C 4   ? 0.3582 0.3128 0.6095 -0.0203 0.0313  -0.0077 4   DG  F N7    
5656 C  C5    . DG  C 4   ? 0.3598 0.314  0.6138 -0.0195 0.0313  -0.0103 4   DG  F C5    
5657 C  C6    . DG  C 4   ? 0.3622 0.3183 0.6161 -0.0183 0.0334  -0.0138 4   DG  F C6    
5658 O  O6    . DG  C 4   ? 0.3633 0.3223 0.6146 -0.0176 0.0359  -0.0152 4   DG  F O6    
5659 N  N1    . DG  C 4   ? 0.3595 0.3134 0.6164 -0.0179 0.032   -0.0157 4   DG  F N1    
5660 C  C2    . DG  C 4   ? 0.3574 0.308  0.6173 -0.0187 0.0293  -0.0141 4   DG  F C2    
5661 N  N2    . DG  C 4   ? 0.3566 0.3054 0.6193 -0.0183 0.028   -0.0161 4   DG  F N2    
5662 N  N3    . DG  C 4   ? 0.3578 0.3068 0.6173 -0.0198 0.0276  -0.0108 4   DG  F N3    
5663 C  C4    . DG  C 4   ? 0.3588 0.3095 0.6153 -0.0201 0.0287  -0.0092 4   DG  F C4    
5664 P  P     . DA  C 5   ? 0.4056 0.3403 0.6544 -0.0233 0.0189  0.0013  5   DA  F P     
5665 O  OP1   . DA  C 5   ? 0.4123 0.3429 0.6623 -0.0237 0.0164  0.0033  5   DA  F OP1   
5666 O  OP2   . DA  C 5   ? 0.4072 0.343  0.6489 -0.0231 0.0203  0.0021  5   DA  F OP2   
5667 O  "O5'" . DA  C 5   ? 0.3985 0.3363 0.6518 -0.023  0.0203  -0.0021 5   DA  F "O5'" 
5668 C  "C5'" . DA  C 5   ? 0.3899 0.3272 0.6502 -0.0227 0.0194  -0.0036 5   DA  F "C5'" 
5669 C  "C4'" . DA  C 5   ? 0.3849 0.3233 0.6473 -0.0225 0.0199  -0.0065 5   DA  F "C4'" 
5670 O  "O4'" . DA  C 5   ? 0.3809 0.3227 0.6417 -0.0216 0.0224  -0.0091 5   DA  F "O4'" 
5671 C  "C3'" . DA  C 5   ? 0.3885 0.3258 0.6479 -0.0234 0.0191  -0.0053 5   DA  F "C3'" 
5672 O  "O3'" . DA  C 5   ? 0.3881 0.3243 0.6519 -0.0236 0.0177  -0.007  5   DA  F "O3'" 
5673 C  "C2'" . DA  C 5   ? 0.3864 0.3267 0.6405 -0.0232 0.0213  -0.0062 5   DA  F "C2'" 
5674 C  "C1'" . DA  C 5   ? 0.3835 0.3262 0.6397 -0.0221 0.023   -0.0094 5   DA  F "C1'" 
5675 N  N9    . DA  C 5   ? 0.3831 0.3285 0.6346 -0.0217 0.0252  -0.0097 5   DA  F N9    
5676 C  C8    . DA  C 5   ? 0.3781 0.3237 0.6259 -0.0219 0.0256  -0.0073 5   DA  F C8    
5677 N  N7    . DA  C 5   ? 0.3744 0.3226 0.6186 -0.0216 0.0276  -0.0082 5   DA  F N7    
5678 C  C5    . DA  C 5   ? 0.3759 0.3258 0.6214 -0.021  0.0287  -0.0114 5   DA  F C5    
5679 C  C6    . DA  C 5   ? 0.3734 0.3258 0.616  -0.0203 0.0308  -0.0137 5   DA  F C6    
5680 N  N6    . DA  C 5   ? 0.3722 0.3265 0.6106 -0.0204 0.0323  -0.0129 5   DA  F N6    
5681 N  N1    . DA  C 5   ? 0.3786 0.3312 0.6224 -0.0196 0.0311  -0.0169 5   DA  F N1    
5682 C  C2    . DA  C 5   ? 0.3848 0.335  0.6329 -0.0196 0.0293  -0.0177 5   DA  F C2    
5683 N  N3    . DA  C 5   ? 0.3854 0.3333 0.6369 -0.0204 0.0272  -0.0156 5   DA  F N3    
5684 C  C4    . DA  C 5   ? 0.3833 0.3312 0.6329 -0.021  0.0271  -0.0124 5   DA  F C4    
5685 P  P     . DA  C 6   ? 0.3846 0.3197 0.6476 -0.0249 0.0163  -0.0055 6   DA  F P     
5686 O  OP1   . DA  C 6   ? 0.3834 0.316  0.6522 -0.0253 0.0138  -0.0064 6   DA  F OP1   
5687 O  OP2   . DA  C 6   ? 0.3877 0.3222 0.6461 -0.0255 0.0163  -0.0016 6   DA  F OP2   
5688 O  "O5'" . DA  C 6   ? 0.3781 0.316  0.6385 -0.0247 0.0177  -0.0078 6   DA  F "O5'" 
5689 C  "C5'" . DA  C 6   ? 0.3732 0.3118 0.6356 -0.0237 0.0183  -0.0118 6   DA  F "C5'" 
5690 C  "C4'" . DA  C 6   ? 0.3725 0.3133 0.6307 -0.0235 0.0197  -0.0135 6   DA  F "C4'" 
5691 O  "O4'" . DA  C 6   ? 0.3682 0.3116 0.6222 -0.0228 0.0222  -0.0133 6   DA  F "O4'" 
5692 C  "C3'" . DA  C 6   ? 0.3785 0.3196 0.635  -0.0249 0.0186  -0.0116 6   DA  F "C3'" 
5693 O  "O3'" . DA  C 6   ? 0.3915 0.3314 0.6501 -0.0252 0.0168  -0.0141 6   DA  F "O3'" 
5694 C  "C2'" . DA  C 6   ? 0.3704 0.3145 0.6211 -0.0247 0.0209  -0.011  6   DA  F "C2'" 
5695 C  "C1'" . DA  C 6   ? 0.3617 0.3068 0.6113 -0.0232 0.023   -0.0135 6   DA  F "C1'" 
5696 N  N9    . DA  C 6   ? 0.3481 0.2953 0.5929 -0.023  0.025   -0.012  6   DA  F N9    
5697 C  C8    . DA  C 6   ? 0.3418 0.2886 0.5845 -0.0233 0.025   -0.0087 6   DA  F C8    
5698 N  N7    . DA  C 6   ? 0.3383 0.2867 0.5764 -0.0229 0.0266  -0.0082 6   DA  F N7    
5699 C  C5    . DA  C 6   ? 0.3356 0.286  0.5728 -0.0224 0.0279  -0.0113 6   DA  F C5    
5700 C  C6    . DA  C 6   ? 0.328  0.2806 0.5608 -0.022  0.0298  -0.0122 6   DA  F C6    
5701 N  N6    . DA  C 6   ? 0.3223 0.2754 0.5511 -0.022  0.0305  -0.0101 6   DA  F N6    
5702 N  N1    . DA  C 6   ? 0.3302 0.2838 0.5625 -0.0214 0.0307  -0.0153 6   DA  F N1    
5703 C  C2    . DA  C 6   ? 0.3354 0.2877 0.5711 -0.0212 0.0295  -0.0176 6   DA  F C2    
5704 N  N3    . DA  C 6   ? 0.3385 0.2886 0.5789 -0.0216 0.0276  -0.0171 6   DA  F N3    
5705 C  C4    . DA  C 6   ? 0.3412 0.2906 0.582  -0.0224 0.0269  -0.0137 6   DA  F C4    
5706 P  P     . DT  C 7   ? 0.4008 0.3405 0.6601 -0.0271 0.0146  -0.0121 7   DT  F P     
5707 O  OP1   . DT  C 7   ? 0.4043 0.3407 0.6688 -0.0277 0.0114  -0.0131 7   DT  F OP1   
5708 O  OP2   . DT  C 7   ? 0.4016 0.3432 0.6591 -0.0279 0.0155  -0.0076 7   DT  F OP2   
5709 O  "O5'" . DT  C 7   ? 0.4042 0.3455 0.6598 -0.0267 0.0153  -0.0146 7   DT  F "O5'" 
5710 C  "C5'" . DT  C 7   ? 0.4118 0.3562 0.6625 -0.0264 0.0178  -0.0136 7   DT  F "C5'" 
5711 C  "C4'" . DT  C 7   ? 0.424  0.3689 0.6711 -0.0254 0.0187  -0.0172 7   DT  F "C4'" 
5712 O  "O4'" . DT  C 7   ? 0.421  0.3677 0.6648 -0.0241 0.0217  -0.0178 7   DT  F "O4'" 
5713 C  "C3'" . DT  C 7   ? 0.4436 0.3902 0.6879 -0.0264 0.0183  -0.0164 7   DT  F "C3'" 
5714 O  "O3'" . DT  C 7   ? 0.4734 0.4177 0.7193 -0.027  0.0154  -0.0184 7   DT  F "O3'" 
5715 C  "C2'" . DT  C 7   ? 0.4325 0.3811 0.6711 -0.0252 0.021   -0.018  7   DT  F "C2'" 
5716 C  "C1'" . DT  C 7   ? 0.4191 0.368  0.6578 -0.024  0.0232  -0.0179 7   DT  F "C1'" 
5717 N  N1    . DT  C 7   ? 0.4022 0.3532 0.6384 -0.0242 0.0248  -0.0146 7   DT  F N1    
5718 C  C2    . DT  C 7   ? 0.3977 0.3506 0.6289 -0.0236 0.0268  -0.015  7   DT  F C2    
5719 O  O2    . DT  C 7   ? 0.3982 0.3515 0.6269 -0.023  0.0275  -0.0178 7   DT  F O2    
5720 N  N3    . DT  C 7   ? 0.3928 0.3466 0.6216 -0.0236 0.0278  -0.012  7   DT  F N3    
5721 C  C4    . DT  C 7   ? 0.3868 0.3398 0.6172 -0.0239 0.0272  -0.0088 7   DT  F C4    
5722 O  O4    . DT  C 7   ? 0.3803 0.3336 0.6072 -0.0235 0.028   -0.0065 7   DT  F O4    
5723 C  C5    . DT  C 7   ? 0.3892 0.3404 0.6247 -0.0246 0.0253  -0.0085 7   DT  F C5    
5724 C  C7    . DT  C 7   ? 0.3891 0.3389 0.6261 -0.0249 0.0245  -0.0051 7   DT  F C7    
5725 C  C6    . DT  C 7   ? 0.3936 0.3439 0.632  -0.0248 0.0241  -0.0113 7   DT  F C6    
5726 P  P     . DG  C 8   ? 0.4988 0.444  0.746  -0.029  0.013   -0.0159 8   DG  F P     
5727 O  OP1   . DG  C 8   ? 0.4972 0.4386 0.7475 -0.0298 0.0092  -0.018  8   DG  F OP1   
5728 O  OP2   . DG  C 8   ? 0.4995 0.4474 0.7486 -0.03   0.0138  -0.011  8   DG  F OP2   
5729 O  "O5'" . DG  C 8   ? 0.522  0.4692 0.7634 -0.0285 0.0145  -0.0172 8   DG  F "O5'" 
5730 C  "C5'" . DG  C 8   ? 0.5459 0.4914 0.7833 -0.027  0.0151  -0.0217 8   DG  F "C5'" 
5731 C  "C4'" . DG  C 8   ? 0.5701 0.5179 0.8019 -0.0267 0.0168  -0.0219 8   DG  F "C4'" 
5732 O  "O4'" . DG  C 8   ? 0.5653 0.5161 0.795  -0.026  0.0201  -0.0199 8   DG  F "O4'" 
5733 C  "C3'" . DG  C 8   ? 0.5961 0.5455 0.8284 -0.0284 0.0148  -0.0194 8   DG  F "C3'" 
5734 O  "O3'" . DG  C 8   ? 0.6383 0.587  0.8658 -0.0281 0.0143  -0.0218 8   DG  F "O3'" 
5735 C  "C2'" . DG  C 8   ? 0.5789 0.5322 0.8109 -0.0285 0.0172  -0.0153 8   DG  F "C2'" 
5736 C  "C1'" . DG  C 8   ? 0.5637 0.5174 0.7917 -0.0268 0.0204  -0.017  8   DG  F "C1'" 
5737 N  N9    . DG  C 8   ? 0.5468 0.5024 0.7749 -0.0265 0.0224  -0.0138 8   DG  F N9    
5738 C  C8    . DG  C 8   ? 0.5407 0.4962 0.7729 -0.027  0.022   -0.0109 8   DG  F C8    
5739 N  N7    . DG  C 8   ? 0.534  0.4908 0.7643 -0.0264 0.0238  -0.0084 8   DG  F N7    
5740 C  C5    . DG  C 8   ? 0.5285 0.4865 0.7535 -0.0256 0.0255  -0.0096 8   DG  F C5    
5741 C  C6    . DG  C 8   ? 0.5172 0.4762 0.738  -0.0247 0.0275  -0.008  8   DG  F C6    
5742 O  O6    . DG  C 8   ? 0.5097 0.4685 0.7302 -0.0243 0.0281  -0.0054 8   DG  F O6    
5743 N  N1    . DG  C 8   ? 0.5175 0.4774 0.7337 -0.0243 0.0285  -0.0098 8   DG  F N1    
5744 C  C2    . DG  C 8   ? 0.5207 0.4804 0.736  -0.0245 0.0279  -0.0129 8   DG  F C2    
5745 N  N2    . DG  C 8   ? 0.5185 0.4791 0.7288 -0.024  0.029   -0.0141 8   DG  F N2    
5746 N  N3    . DG  C 8   ? 0.5292 0.4875 0.7479 -0.0251 0.026   -0.0146 8   DG  F N3    
5747 C  C4    . DG  C 8   ? 0.5351 0.4926 0.7588 -0.0257 0.0248  -0.0128 8   DG  F C4    
5748 P  P     . DC  C 9   ? 0.6753 0.6241 0.9036 -0.0299 0.0109  -0.0206 9   DC  F P     
5749 O  OP1   . DC  C 9   ? 0.6813 0.6251 0.9092 -0.03   0.0074  -0.0242 9   DC  F OP1   
5750 O  OP2   . DC  C 9   ? 0.6744 0.6263 0.9082 -0.0315 0.0103  -0.0156 9   DC  F OP2   
5751 O  "O5'" . DC  C 9   ? 0.6981 0.6491 0.92   -0.0292 0.013   -0.0211 9   DC  F "O5'" 
5752 C  "C5'" . DC  C 9   ? 0.7213 0.6716 0.9376 -0.0274 0.0158  -0.0242 9   DC  F "C5'" 
5753 C  "C4'" . DC  C 9   ? 0.7449 0.6982 0.9564 -0.0271 0.0181  -0.023  9   DC  F "C4'" 
5754 O  "O4'" . DC  C 9   ? 0.7462 0.7026 0.9591 -0.0267 0.0207  -0.0199 9   DC  F "O4'" 
5755 C  "C3'" . DC  C 9   ? 0.7637 0.7185 0.9751 -0.0284 0.0159  -0.021  9   DC  F "C3'" 
5756 O  "O3'" . DC  C 9   ? 0.7926 0.7478 0.9976 -0.0278 0.0169  -0.0224 9   DC  F "O3'" 
5757 C  "C2'" . DC  C 9   ? 0.7531 0.7117 0.9684 -0.0289 0.0171  -0.0163 9   DC  F "C2'" 
5758 C  "C1'" . DC  C 9   ? 0.7458 0.7051 0.9589 -0.0274 0.0206  -0.0165 9   DC  F "C1'" 
5759 N  N1    . DC  C 9   ? 0.7357 0.6968 0.9527 -0.0274 0.0216  -0.0129 9   DC  F N1    
5760 C  C2    . DC  C 9   ? 0.728  0.6911 0.9423 -0.0265 0.0242  -0.0108 9   DC  F C2    
5761 O  O2    . DC  C 9   ? 0.724  0.6876 0.9331 -0.0258 0.0254  -0.0118 9   DC  F O2    
5762 N  N3    . DC  C 9   ? 0.7267 0.6907 0.9437 -0.0263 0.0249  -0.0077 9   DC  F N3    
5763 C  C4    . DC  C 9   ? 0.727  0.6903 0.9495 -0.0271 0.0235  -0.0066 9   DC  F C4    
5764 N  N4    . DC  C 9   ? 0.7251 0.689  0.9496 -0.0269 0.0243  -0.0035 9   DC  F N4    
5765 C  C5    . DC  C 9   ? 0.7294 0.6909 0.9553 -0.0283 0.0208  -0.0086 9   DC  F C5    
5766 C  C6    . DC  C 9   ? 0.7331 0.6934 0.956  -0.0283 0.0199  -0.0118 9   DC  F C6    
5767 P  P     . DA  C 10  ? 0.8184 0.7738 1.0218 -0.029  0.0141  -0.0217 10  DA  F P     
5768 O  OP1   . DA  C 10  ? 0.8247 0.7771 1.0208 -0.0282 0.014   -0.0256 10  DA  F OP1   
5769 O  OP2   . DA  C 10  ? 0.8186 0.7735 1.0285 -0.0306 0.0105  -0.0199 10  DA  F OP2   
5770 O  "O5'" . DA  C 10  ? 0.827  0.7869 1.0298 -0.0288 0.0163  -0.0181 10  DA  F "O5'" 
5771 C  "C5'" . DA  C 10  ? 0.8361 0.7975 1.0364 -0.0275 0.02    -0.0176 10  DA  F "C5'" 
5772 C  "C4'" . DA  C 10  ? 0.8419 0.8066 1.0412 -0.0272 0.0213  -0.0143 10  DA  F "C4'" 
5773 O  "O4'" . DA  C 10  ? 0.8382 0.8047 1.0414 -0.0268 0.0227  -0.0113 10  DA  F "O4'" 
5774 C  "C3'" . DA  C 10  ? 0.8496 0.8161 1.0502 -0.0281 0.019   -0.0124 10  DA  F "C3'" 
5775 O  "O3'" . DA  C 10  ? 0.8634 0.8316 1.0594 -0.0273 0.0202  -0.0114 10  DA  F "O3'" 
5776 C  "C2'" . DA  C 10  ? 0.8405 0.8094 1.0481 -0.0286 0.0185  -0.0087 10  DA  F "C2'" 
5777 C  "C1'" . DA  C 10  ? 0.8328 0.802  1.0402 -0.0274 0.0215  -0.0078 10  DA  F "C1'" 
5778 N  N9    . DA  C 10  ? 0.8185 0.7878 1.0319 -0.0279 0.0211  -0.006  10  DA  F N9    
5779 C  C8    . DA  C 10  ? 0.8117 0.7792 1.0296 -0.0292 0.0187  -0.0071 10  DA  F C8    
5780 N  N7    . DA  C 10  ? 0.8054 0.7734 1.0283 -0.0295 0.0188  -0.0048 10  DA  F N7    
5781 C  C5    . DA  C 10  ? 0.804  0.7742 1.0251 -0.0281 0.0216  -0.0022 10  DA  F C5    
5782 C  C6    . DA  C 10  ? 0.7993 0.7706 1.0228 -0.0276 0.023   0.001   10  DA  F C6    
5783 N  N6    . DA  C 10  ? 0.7971 0.7678 1.0261 -0.0285 0.0219  0.0023  10  DA  F N6    
5784 N  N1    . DA  C 10  ? 0.7984 0.7709 1.0181 -0.0259 0.0255  0.0028  10  DA  F N1    
5785 C  C2    . DA  C 10  ? 0.8011 0.7739 1.0154 -0.025  0.0263  0.0016  10  DA  F C2    
5786 N  N3    . DA  C 10  ? 0.8054 0.7776 1.0172 -0.0256 0.0252  -0.0011 10  DA  F N3    
5787 C  C4    . DA  C 10  ? 0.8092 0.7801 1.0245 -0.0271 0.0229  -0.003  10  DA  F C4    
5788 P  P     . DG  C 11  ? 0.8719 0.841  1.0666 -0.028  0.0179  -0.0107 11  DG  F P     
5789 O  OP1   . DG  C 11  ? 0.8753 0.8424 1.0624 -0.0277 0.0183  -0.0135 11  DG  F OP1   
5790 O  OP2   . DG  C 11  ? 0.8698 0.8386 1.0701 -0.0296 0.0144  -0.0103 11  DG  F OP2   
5791 O  "O5'" . DG  C 11  ? 0.8678 0.8409 1.064  -0.027  0.0193  -0.0066 11  DG  F "O5'" 
5792 C  "C5'" . DG  C 11  ? 0.8641 0.8376 1.0574 -0.0255 0.0224  -0.0058 11  DG  F "C5'" 
5793 C  "C4'" . DG  C 11  ? 0.8557 0.8323 1.0523 -0.0244 0.0235  -0.0017 11  DG  F "C4'" 
5794 O  "O4'" . DG  C 11  ? 0.8464 0.8233 1.0484 -0.0247 0.0238  -0.0004 11  DG  F "O4'" 
5795 C  "C3'" . DG  C 11  ? 0.8542 0.8341 1.0537 -0.0245 0.022   0.0009  11  DG  F "C3'" 
5796 O  "O3'" . DG  C 11  ? 0.8623 0.8442 1.0599 -0.0225 0.0239  0.0036  11  DG  F "O3'" 
5797 C  "C2'" . DG  C 11  ? 0.8426 0.8241 1.05   -0.0257 0.0208  0.003   11  DG  F "C2'" 
5798 C  "C1'" . DG  C 11  ? 0.8368 0.8172 1.0445 -0.0249 0.023   0.0032  11  DG  F "C1'" 
5799 N  N9    . DG  C 11  ? 0.8238 0.804  1.0377 -0.0262 0.0219  0.0037  11  DG  F N9    
5800 C  C8    . DG  C 11  ? 0.819  0.7973 1.0357 -0.0282 0.019   0.0016  11  DG  F C8    
5801 N  N7    . DG  C 11  ? 0.8136 0.7916 1.0357 -0.0291 0.0184  0.0026  11  DG  F N7    
5802 C  C5    . DG  C 11  ? 0.8094 0.7894 1.0321 -0.0277 0.0211  0.0056  11  DG  F C5    
5803 C  C6    . DG  C 11  ? 0.8017 0.7823 1.029  -0.0278 0.0218  0.008   11  DG  F C6    
5804 O  O6    . DG  C 11  ? 0.7985 0.778  1.0309 -0.0294 0.0199  0.0081  11  DG  F O6    
5805 N  N1    . DG  C 11  ? 0.8002 0.7822 1.0253 -0.0258 0.0248  0.0106  11  DG  F N1    
5806 C  C2    . DG  C 11  ? 0.8046 0.7872 1.0238 -0.0238 0.0266  0.0108  11  DG  F C2    
5807 N  N2    . DG  C 11  ? 0.8029 0.7862 1.02   -0.0217 0.0291  0.0133  11  DG  F N2    
5808 N  N3    . DG  C 11  ? 0.8118 0.7941 1.0272 -0.0238 0.0259  0.0086  11  DG  F N3    
5809 C  C4    . DG  C 11  ? 0.8152 0.7963 1.0326 -0.0258 0.0233  0.0062  11  DG  F C4    
5810 P  P     . DA  C 12  ? 0.8671 0.8517 1.0641 -0.0217 0.023   0.0055  12  DA  F P     
5811 O  OP1   . DA  C 12  ? 0.8681 0.8507 1.0573 -0.0204 0.0239  0.0041  12  DA  F OP1   
5812 O  OP2   . DA  C 12  ? 0.8661 0.8516 1.0672 -0.0238 0.0199  0.0052  12  DA  F OP2   
5813 O  "O5'" . DA  C 12  ? 0.8658 0.8543 1.067  -0.0198 0.0248  0.0099  12  DA  F "O5'" 
5814 C  "C5'" . DA  C 12  ? 0.8661 0.8534 1.0657 -0.0183 0.0274  0.0107  12  DA  F "C5'" 
5815 C  "C4'" . DA  C 12  ? 0.8607 0.8516 1.0666 -0.0176 0.0285  0.0147  12  DA  F "C4'" 
5816 O  "O4'" . DA  C 12  ? 0.8555 0.8457 1.0664 -0.0198 0.0275  0.0141  12  DA  F "O4'" 
5817 C  "C3'" . DA  C 12  ? 0.8591 0.8551 1.0704 -0.0173 0.0278  0.0181  12  DA  F "C3'" 
5818 O  "O3'" . DA  C 12  ? 0.8678 0.8663 1.0783 -0.0141 0.0305  0.0215  12  DA  F "O3'" 
5819 C  "C2'" . DA  C 12  ? 0.8494 0.8474 1.0692 -0.0198 0.0261  0.0194  12  DA  F "C2'" 
5820 C  "C1'" . DA  C 12  ? 0.8455 0.84   1.0641 -0.0203 0.027   0.0178  12  DA  F "C1'" 
5821 N  N9    . DA  C 12  ? 0.8334 0.8268 1.0573 -0.0232 0.0245  0.0166  12  DA  F N9    
5822 C  C8    . DA  C 12  ? 0.83   0.8219 1.0548 -0.0254 0.0213  0.014   12  DA  F C8    
5823 N  N7    . DA  C 12  ? 0.8249 0.8155 1.0545 -0.0276 0.0192  0.0134  12  DA  F N7    
5824 C  C5    . DA  C 12  ? 0.8207 0.8126 1.0533 -0.0269 0.0212  0.0161  12  DA  F C5    
5825 C  C6    . DA  C 12  ? 0.8155 0.8067 1.0536 -0.0285 0.0202  0.017   12  DA  F C6    
5826 N  N6    . DA  C 12  ? 0.8135 0.8023 1.055  -0.031  0.0167  0.0151  12  DA  F N6    
5827 N  N1    . DA  C 12  ? 0.814  0.8066 1.0534 -0.0273 0.0228  0.0199  12  DA  F N1    
5828 C  C2    . DA  C 12  ? 0.8158 0.81   1.0509 -0.0245 0.026   0.0216  12  DA  F C2    
5829 N  N3    . DA  C 12  ? 0.8191 0.8137 1.0487 -0.0227 0.0271  0.0208  12  DA  F N3    
5830 C  C4    . DA  C 12  ? 0.8237 0.8173 1.0527 -0.0242 0.0245  0.0181  12  DA  F C4    
5831 P  P     . DC  C 13  ? 0.872  0.8765 1.0874 -0.0126 0.0309  0.0256  13  DC  F P     
5832 O  OP1   . DC  C 13  ? 0.8733 0.8773 1.0821 -0.0088 0.0331  0.0263  13  DC  F OP1   
5833 O  OP2   . DC  C 13  ? 0.8711 0.8772 1.0911 -0.0153 0.0275  0.025   13  DC  F OP2   
5834 O  "O5'" . DC  C 13  ? 0.8683 0.8767 1.091  -0.0125 0.0325  0.0298  13  DC  F "O5'" 
5835 C  "C5'" . DC  C 13  ? 0.8679 0.8735 1.0883 -0.0119 0.0344  0.0297  13  DC  F "C5'" 
5836 C  "C4'" . DC  C 13  ? 0.8594 0.8682 1.0882 -0.0135 0.0344  0.0329  13  DC  F "C4'" 
5837 O  "O4'" . DC  C 13  ? 0.8553 0.8619 1.0877 -0.0174 0.0312  0.0303  13  DC  F "O4'" 
5838 C  "C3'" . DC  C 13  ? 0.8531 0.8691 1.0901 -0.0132 0.0349  0.038   13  DC  F "C3'" 
5839 O  "O3'" . DC  C 13  ? 0.8542 0.8729 1.0915 -0.0103 0.0385  0.042   13  DC  F "O3'" 
5840 C  "C2'" . DC  C 13  ? 0.8463 0.8636 1.0922 -0.0174 0.0315  0.0385  13  DC  F "C2'" 
5841 C  "C1'" . DC  C 13  ? 0.8463 0.8571 1.0881 -0.0192 0.0302  0.0339  13  DC  F "C1'" 
5842 N  N1    . DC  C 13  ? 0.8403 0.8492 1.0858 -0.0229 0.0259  0.0313  13  DC  F N1    
5843 C  C2    . DC  C 13  ? 0.8369 0.8451 1.0884 -0.0256 0.0241  0.0319  13  DC  F C2    
5844 O  O2    . DC  C 13  ? 0.8355 0.845  1.0893 -0.0249 0.0261  0.0348  13  DC  F O2    
5845 N  N3    . DC  C 13  ? 0.8357 0.8414 1.0899 -0.0286 0.0199  0.0294  13  DC  F N3    
5846 C  C4    . DC  C 13  ? 0.8381 0.8422 1.089  -0.0291 0.0178  0.0264  13  DC  F C4    
5847 N  N4    . DC  C 13  ? 0.8383 0.8392 1.0909 -0.0318 0.0136  0.0237  13  DC  F N4    
5848 C  C5    . DC  C 13  ? 0.8406 0.8456 1.0855 -0.0266 0.0198  0.0259  13  DC  F C5    
5849 C  C6    . DC  C 13  ? 0.8409 0.8483 1.0836 -0.0236 0.0237  0.0284  13  DC  F C6    
5850 C  "C5'" . DG  D 1   ? 0.8061 0.8048 1.1156 -0.0497 -0.0023 0.0438  1   DG  G "C5'" 
5851 C  "C4'" . DG  D 1   ? 0.8096 0.8102 1.1114 -0.0459 0.004   0.0431  1   DG  G "C4'" 
5852 O  "O4'" . DG  D 1   ? 0.8085 0.8118 1.1065 -0.0442 0.0056  0.0422  1   DG  G "O4'" 
5853 C  "C3'" . DG  D 1   ? 0.8152 0.8093 1.1085 -0.0442 0.0054  0.0372  1   DG  G "C3'" 
5854 O  "O3'" . DG  D 1   ? 0.8155 0.8111 1.106  -0.042  0.0101  0.0394  1   DG  G "O3'" 
5855 C  "C2'" . DG  D 1   ? 0.8163 0.8089 1.1021 -0.0424 0.0063  0.0326  1   DG  G "C2'" 
5856 C  "C1'" . DG  D 1   ? 0.8099 0.8096 1.098  -0.0414 0.0086  0.0373  1   DG  G "C1'" 
5857 N  N9    . DG  D 1   ? 0.8044 0.804  1.0879 -0.0405 0.0083  0.0344  1   DG  G N9    
5858 C  C8    . DG  D 1   ? 0.8037 0.7993 1.0862 -0.0422 0.004   0.0304  1   DG  G C8    
5859 N  N7    . DG  D 1   ? 0.8039 0.7994 1.0805 -0.0407 0.0049  0.0279  1   DG  G N7    
5860 C  C5    . DG  D 1   ? 0.8035 0.8027 1.0769 -0.0378 0.01    0.0299  1   DG  G C5    
5861 C  C6    . DG  D 1   ? 0.8048 0.8053 1.0718 -0.0353 0.0128  0.0289  1   DG  G C6    
5862 O  O6    . DG  D 1   ? 0.8064 0.8054 1.0694 -0.0352 0.0114  0.0258  1   DG  G O6    
5863 N  N1    . DG  D 1   ? 0.8036 0.8072 1.0686 -0.0325 0.0175  0.0317  1   DG  G N1    
5864 C  C2    . DG  D 1   ? 0.8021 0.8074 1.0705 -0.0323 0.0194  0.0352  1   DG  G C2    
5865 N  N2    . DG  D 1   ? 0.8017 0.8092 1.0663 -0.0292 0.0238  0.0374  1   DG  G N2    
5866 N  N3    . DG  D 1   ? 0.8008 0.8052 1.0754 -0.0349 0.0169  0.0365  1   DG  G N3    
5867 C  C4    . DG  D 1   ? 0.8024 0.8038 1.0794 -0.0375 0.0122  0.0337  1   DG  G C4    
5868 P  P     . DT  D 2   ? 0.8167 0.8065 1.0994 -0.0402 0.0121  0.0347  2   DT  G P     
5869 O  OP1   . DT  D 2   ? 0.817  0.8059 1.1032 -0.041  0.0121  0.0375  2   DT  G OP1   
5870 O  OP2   . DT  D 2   ? 0.8199 0.8044 1.0986 -0.0405 0.0095  0.0283  2   DT  G OP2   
5871 O  "O5'" . DT  D 2   ? 0.8058 0.7984 1.0815 -0.0366 0.0173  0.0353  2   DT  G "O5'" 
5872 C  "C5'" . DT  D 2   ? 0.7873 0.785  1.0644 -0.0351 0.0208  0.0411  2   DT  G "C5'" 
5873 C  "C4'" . DT  D 2   ? 0.7705 0.769  1.0393 -0.0314 0.025   0.0405  2   DT  G "C4'" 
5874 O  "O4'" . DT  D 2   ? 0.7634 0.7629 1.0298 -0.0309 0.0245  0.038   2   DT  G "O4'" 
5875 C  "C3'" . DT  D 2   ? 0.7631 0.7559 1.024  -0.0297 0.0265  0.0366  2   DT  G "C3'" 
5876 O  "O3'" . DT  D 2   ? 0.756  0.7499 1.0111 -0.0264 0.0305  0.0389  2   DT  G "O3'" 
5877 C  "C2'" . DT  D 2   ? 0.7635 0.7534 1.02   -0.0297 0.0251  0.0311  2   DT  G "C2'" 
5878 C  "C1'" . DT  D 2   ? 0.7603 0.7552 1.0181 -0.0292 0.0255  0.033   2   DT  G "C1'" 
5879 N  N1    . DT  D 2   ? 0.7541 0.7474 1.0111 -0.0305 0.0227  0.0289  2   DT  G N1    
5880 C  C2    . DT  D 2   ? 0.7488 0.7431 1.0007 -0.0288 0.0239  0.0275  2   DT  G C2    
5881 O  O2    . DT  D 2   ? 0.7429 0.7392 0.9908 -0.0261 0.0271  0.0293  2   DT  G O2    
5882 N  N3    . DT  D 2   ? 0.752  0.7443 1.003  -0.0301 0.0212  0.0238  2   DT  G N3    
5883 C  C4    . DT  D 2   ? 0.755  0.7443 1.0092 -0.0327 0.0174  0.0212  2   DT  G C4    
5884 O  O4    . DT  D 2   ? 0.7575 0.7448 1.0095 -0.0334 0.0152  0.0178  2   DT  G O4    
5885 C  C5    . DT  D 2   ? 0.7541 0.7423 1.0137 -0.0343 0.0161  0.0227  2   DT  G C5    
5886 C  C7    . DT  D 2   ? 0.7537 0.7378 1.0166 -0.0368 0.0118  0.0199  2   DT  G C7    
5887 C  C6    . DT  D 2   ? 0.7535 0.7439 1.0144 -0.0332 0.0188  0.0265  2   DT  G C6    
5888 P  P     . DC  D 3   ? 0.7509 0.7396 0.9994 -0.0247 0.0321  0.0374  3   DC  G P     
5889 O  OP1   . DC  D 3   ? 0.7534 0.7442 1.0013 -0.0229 0.0349  0.0425  3   DC  G OP1   
5890 O  OP2   . DC  D 3   ? 0.7509 0.7348 1.0012 -0.027  0.0291  0.0338  3   DC  G OP2   
5891 O  "O5'" . DC  D 3   ? 0.7361 0.7227 0.9757 -0.0221 0.0337  0.034   3   DC  G "O5'" 
5892 C  "C5'" . DC  D 3   ? 0.7161 0.7062 0.9523 -0.0193 0.0363  0.0364  3   DC  G "C5'" 
5893 C  "C4'" . DC  D 3   ? 0.6971 0.6845 0.9258 -0.0177 0.0367  0.0325  3   DC  G "C4'" 
5894 O  "O4'" . DC  D 3   ? 0.6849 0.6733 0.9162 -0.0197 0.0344  0.0296  3   DC  G "O4'" 
5895 C  "C3'" . DC  D 3   ? 0.6889 0.6702 0.9115 -0.0172 0.0364  0.0291  3   DC  G "C3'" 
5896 O  "O3'" . DC  D 3   ? 0.6823 0.6619 0.8967 -0.0142 0.0381  0.0286  3   DC  G "O3'" 
5897 C  "C2'" . DC  D 3   ? 0.6839 0.6635 0.9085 -0.0197 0.0338  0.0246  3   DC  G "C2'" 
5898 C  "C1'" . DC  D 3   ? 0.6757 0.6594 0.9023 -0.02   0.0334  0.0248  3   DC  G "C1'" 
5899 N  N1    . DC  D 3   ? 0.6579 0.6413 0.8888 -0.0228 0.0305  0.0219  3   DC  G N1    
5900 C  C2    . DC  D 3   ? 0.6505 0.634  0.8788 -0.0229 0.0296  0.019   3   DC  G C2    
5901 O  O2    . DC  D 3   ? 0.6496 0.6333 0.8723 -0.0209 0.0313  0.0189  3   DC  G O2    
5902 N  N3    . DC  D 3   ? 0.6482 0.6308 0.8795 -0.0252 0.0269  0.0163  3   DC  G N3    
5903 C  C4    . DC  D 3   ? 0.6483 0.6301 0.8855 -0.0273 0.0249  0.0164  3   DC  G C4    
5904 N  N4    . DC  D 3   ? 0.647  0.6272 0.8864 -0.0292 0.0219  0.0135  3   DC  G N4    
5905 C  C5    . DC  D 3   ? 0.6499 0.6318 0.8903 -0.0273 0.0256  0.0194  3   DC  G C5    
5906 C  C6    . DC  D 3   ? 0.6528 0.6357 0.89   -0.0251 0.0285  0.0221  3   DC  G C6    
5907 P  P     . DT  D 4   ? 0.6756 0.6489 0.8828 -0.0128 0.0383  0.0269  4   DT  G P     
5908 O  OP1   . DT  D 4   ? 0.6806 0.6531 0.882  -0.0094 0.0406  0.0301  4   DT  G OP1   
5909 O  OP2   . DT  D 4   ? 0.6758 0.6464 0.8869 -0.0152 0.0365  0.0254  4   DT  G OP2   
5910 O  "O5'" . DT  D 4   ? 0.6598 0.6313 0.8624 -0.0127 0.0375  0.023   4   DT  G "O5'" 
5911 C  "C5'" . DT  D 4   ? 0.6409 0.6157 0.843  -0.012  0.0379  0.023   4   DT  G "C5'" 
5912 C  "C4'" . DT  D 4   ? 0.6251 0.5984 0.8255 -0.0134 0.0364  0.0189  4   DT  G "C4'" 
5913 O  "O4'" . DT  D 4   ? 0.6114 0.5866 0.8183 -0.0163 0.0347  0.0173  4   DT  G "O4'" 
5914 C  "C3'" . DT  D 4   ? 0.6223 0.5906 0.8183 -0.0134 0.0357  0.0163  4   DT  G "C3'" 
5915 O  "O3'" . DT  D 4   ? 0.6225 0.5894 0.8125 -0.0124 0.0357  0.0147  4   DT  G "O3'" 
5916 C  "C2'" . DT  D 4   ? 0.6147 0.5827 0.8161 -0.0163 0.0342  0.0136  4   DT  G "C2'" 
5917 C  "C1'" . DT  D 4   ? 0.6046 0.5767 0.8101 -0.0175 0.0336  0.0135  4   DT  G "C1'" 
5918 N  N1    . DT  D 4   ? 0.5871 0.5596 0.7989 -0.02   0.0319  0.012   4   DT  G N1    
5919 C  C2    . DT  D 4   ? 0.5795 0.5522 0.792  -0.0214 0.0306  0.0089  4   DT  G C2    
5920 O  O2    . DT  D 4   ? 0.5789 0.5518 0.7872 -0.0209 0.0308  0.0075  4   DT  G O2    
5921 N  N3    . DT  D 4   ? 0.5748 0.5472 0.7927 -0.0234 0.0288  0.0076  4   DT  G N3    
5922 C  C4    . DT  D 4   ? 0.5719 0.5439 0.795  -0.0243 0.0281  0.0091  4   DT  G C4    
5923 O  O4    . DT  D 4   ? 0.5685 0.5396 0.7959 -0.0261 0.0261  0.0075  4   DT  G O4    
5924 C  C5    . DT  D 4   ? 0.574  0.5461 0.7963 -0.023  0.0297  0.0125  4   DT  G C5    
5925 C  C7    . DT  D 4   ? 0.5713 0.5428 0.7986 -0.0239 0.029   0.0147  4   DT  G C7    
5926 C  C6    . DT  D 4   ? 0.58   0.5522 0.7965 -0.0208 0.0315  0.0137  4   DT  G C6    
5927 P  P     . DG  D 5   ? 0.6215 0.5832 0.8057 -0.0119 0.0351  0.013   5   DG  G P     
5928 O  OP1   . DG  D 5   ? 0.6229 0.5824 0.8    -0.0089 0.0357  0.0148  5   DG  G OP1   
5929 O  OP2   . DG  D 5   ? 0.6203 0.5797 0.8077 -0.0132 0.0344  0.0125  5   DG  G OP2   
5930 O  "O5'" . DG  D 5   ? 0.6161 0.5785 0.8    -0.0135 0.0342  0.0099  5   DG  G "O5'" 
5931 C  "C5'" . DG  D 5   ? 0.6077 0.5731 0.791  -0.0133 0.0344  0.0097  5   DG  G "C5'" 
5932 C  "C4'" . DG  D 5   ? 0.5984 0.5646 0.7828 -0.0153 0.0335  0.0066  5   DG  G "C4'" 
5933 O  "O4'" . DG  D 5   ? 0.592  0.5599 0.7828 -0.0173 0.0329  0.0055  5   DG  G "O4'" 
5934 C  "C3'" . DG  D 5   ? 0.5948 0.5579 0.7762 -0.0159 0.0332  0.0045  5   DG  G "C3'" 
5935 O  "O3'" . DG  D 5   ? 0.5932 0.5569 0.7717 -0.0164 0.0328  0.0028  5   DG  G "O3'" 
5936 C  "C2'" . DG  D 5   ? 0.5909 0.554  0.7778 -0.0177 0.0329  0.0029  5   DG  G "C2'" 
5937 C  "C1'" . DG  D 5   ? 0.587  0.5531 0.7784 -0.0186 0.0325  0.0027  5   DG  G "C1'" 
5938 N  N9    . DG  D 5   ? 0.5778 0.5439 0.7751 -0.0198 0.032   0.0024  5   DG  G N9    
5939 C  C8    . DG  D 5   ? 0.5734 0.5382 0.7729 -0.0194 0.0322  0.0041  5   DG  G C8    
5940 N  N7    . DG  D 5   ? 0.5689 0.5337 0.7737 -0.0208 0.0314  0.0034  5   DG  G N7    
5941 C  C5    . DG  D 5   ? 0.5678 0.5337 0.7738 -0.0219 0.0306  0.0007  5   DG  G C5    
5942 C  C6    . DG  D 5   ? 0.5636 0.5292 0.7742 -0.0234 0.0293  -0.0014 5   DG  G C6    
5943 O  O6    . DG  D 5   ? 0.5608 0.5254 0.7758 -0.0241 0.0285  -0.0012 5   DG  G O6    
5944 N  N1    . DG  D 5   ? 0.5639 0.5301 0.773  -0.0239 0.0287  -0.0039 5   DG  G N1    
5945 C  C2    . DG  D 5   ? 0.5677 0.5348 0.7718 -0.0234 0.0293  -0.0042 5   DG  G C2    
5946 N  N2    . DG  D 5   ? 0.5679 0.5349 0.7707 -0.0241 0.0284  -0.0068 5   DG  G N2    
5947 N  N3    . DG  D 5   ? 0.5717 0.5392 0.7719 -0.0221 0.0305  -0.0022 5   DG  G N3    
5948 C  C4    . DG  D 5   ? 0.5724 0.5391 0.7737 -0.0214 0.0311  0.0001  5   DG  G C4    
5949 MG MG    . MG  E .   ? 2.5404 2.4822 2.6899 -0.0106 0.0276  0.0081  701 MG  A MG    
5950 CL CL    . CL  F .   ? 0.5369 0.4772 0.803  -0.0464 -0.0116 0.0506  702 CL  A CL    
5951 O  O1    . MES G .   ? 0.7923 0.6115 1.023  -0.0363 -0.045  0.0533  703 MES A O1    
5952 C  C2    . MES G .   ? 0.7902 0.6134 1.0216 -0.035  -0.0429 0.0503  703 MES A C2    
5953 C  C3    . MES G .   ? 0.7853 0.6108 1.029  -0.0357 -0.0453 0.047   703 MES A C3    
5954 N  N4    . MES G .   ? 0.7818 0.6126 1.0367 -0.037  -0.0446 0.0453  703 MES A N4    
5955 C  C5    . MES G .   ? 0.784  0.6105 1.038  -0.0384 -0.0469 0.0485  703 MES A C5    
5956 C  C6    . MES G .   ? 0.7879 0.6126 1.0296 -0.0378 -0.0443 0.0521  703 MES A C6    
5957 C  C7    . MES G .   ? 0.7808 0.6134 1.0474 -0.0373 -0.047  0.0423  703 MES A C7    
5958 C  C8    . MES G .   ? 0.7788 0.6189 1.0557 -0.0374 -0.0445 0.039   703 MES A C8    
5959 S  S     . MES G .   ? 0.7772 0.6189 1.0669 -0.0371 -0.0472 0.0357  703 MES A S     
5960 O  O1S   . MES G .   ? 0.7798 0.6174 1.066  -0.0367 -0.0496 0.0369  703 MES A O1S   
5961 O  O2S   . MES G .   ? 0.7757 0.6144 1.0725 -0.0381 -0.0508 0.036   703 MES A O2S   
5962 O  O3S   . MES G .   ? 0.7755 0.6252 1.0702 -0.036  -0.0429 0.032   703 MES A O3S   
5963 O  O     . HOH H .   ? 0.1202 0.0463 0.1802 -0.0239 -0.0103 0.0114  801 HOH A O     
5964 O  O     . HOH H .   ? 0.288  0.2429 0.5308 -0.0301 0.0169  -0.0065 802 HOH A O     
5965 O  O     . HOH H .   ? 0.0991 0.0473 0.3663 -0.021  0.0142  0.0089  803 HOH A O     
5966 O  O     . HOH H .   ? 0.2163 0.1144 0.1963 -0.0442 -0.0276 -0.0169 804 HOH A O     
5967 O  O     . HOH H .   ? 0.1385 0.0509 0.2229 -0.0294 -0.0243 0.0315  805 HOH A O     
5968 O  O     . HOH H .   ? 0.533  0.436  0.7994 -0.0269 -0.0027 0.0142  806 HOH A O     
5969 O  O     . HOH H .   ? 0.131  0.0533 0.2861 -0.0115 0.0208  0.0128  807 HOH A O     
5970 O  O     . HOH H .   ? 0.2677 0.1703 0.2832 -0.0363 -0.0178 -0.0342 808 HOH A O     
5971 O  O     . HOH H .   ? 0.0715 0.0538 0.249  -0.0194 0.0526  -0.0103 809 HOH A O     
5972 O  O     . HOH H .   ? 0.0954 0.128  0.2618 -0.0336 0.0854  0.0305  810 HOH A O     
5973 O  O     . HOH H .   ? 0.1354 0.0854 0.3849 -0.0589 -0.0155 0.0681  811 HOH A O     
5974 O  O     . HOH H .   ? 0.2786 0.219  0.3281 -0.0405 0.0059  0.0093  812 HOH A O     
5975 O  O     . HOH H .   ? 0.2268 0.0704 0.213  0.0754  0.0242  0.0237  813 HOH A O     
5976 O  O     . HOH H .   ? 0.1616 0.0419 0.2624 0.0026  -0.0022 0.0248  814 HOH A O     
5977 O  O     . HOH H .   ? 0.1703 0.1052 0.4622 -0.0347 -0.0056 0.0329  815 HOH A O     
5978 O  O     . HOH H .   ? 0.3315 0.2765 0.393  -0.0096 0.0559  -0.0464 816 HOH A O     
5979 O  O     . HOH H .   ? 0.1743 0.1199 0.3277 -0.0242 0.0238  0.0086  817 HOH A O     
5980 O  O     . HOH H .   ? 0.2667 0.0459 0.2321 0.0159  -0.0856 0.0242  818 HOH A O     
5981 O  O     . HOH H .   ? 0.3149 0.138  0.3468 -0.0244 -0.0691 0.0403  819 HOH A O     
5982 O  O     . HOH H .   ? 0.2298 0.0466 0.2134 0.0256  -0.06   0.0173  820 HOH A O     
5983 O  O     . HOH H .   ? 0.2558 0.1904 0.5991 -0.0669 -0.037  0.0426  821 HOH A O     
5984 O  O     . HOH H .   ? 0.1687 0.0636 0.1856 -0.0391 -0.0323 -0.0337 822 HOH A O     
5985 O  O     . HOH H .   ? 0.0441 0.0387 0.1981 -0.0007 0.0298  -0.004  823 HOH A O     
5986 O  O     . HOH H .   ? 0.1776 0.0575 0.4689 -0.0448 -0.0545 0.0548  824 HOH A O     
5987 O  O     . HOH H .   ? 0.2603 0.2104 0.3579 -0.0198 -0.0317 0.0077  825 HOH A O     
5988 O  O     . HOH H .   ? 0.139  0.0601 0.4426 -0.045  -0.0131 0.0173  826 HOH A O     
5989 O  O     . HOH H .   ? 0.516  0.3158 0.702  -0.0273 -0.0487 0.051   827 HOH A O     
5990 O  O     . HOH H .   ? 0.113  0.0605 0.1737 -0.0389 0.0144  0.006   828 HOH A O     
5991 O  O     . HOH H .   ? 0.1034 0.0462 0.3586 -0.0199 0.023   -0.0231 829 HOH A O     
5992 O  O     . HOH H .   ? 0.255  0.0435 0.3129 -0.0057 -0.0585 0.033   830 HOH A O     
5993 O  O     . HOH H .   ? 0.2457 0.2065 0.4299 -0.0067 0.0389  0.0241  831 HOH A O     
5994 O  O     . HOH H .   ? 0.179  0.0618 0.4825 -0.0514 -0.0288 0.0484  832 HOH A O     
5995 O  O     . HOH H .   ? 0.2563 0.0451 0.3565 -0.0173 -0.0659 0.04    833 HOH A O     
5996 O  O     . HOH H .   ? 0.1448 0.0668 0.3849 -0.0481 -0.0224 0.0531  834 HOH A O     
5997 O  O     . HOH H .   ? 0.1297 0.1006 0.3951 -0.0551 0.0006  0.0635  835 HOH A O     
5998 O  O     . HOH H .   ? 0.1465 0.1303 0.3366 -0.0404 0.0374  0.0283  836 HOH A O     
5999 O  O     . HOH H .   ? 0.1704 0.0992 0.2356 -0.0272 -0.0049 0.0123  837 HOH A O     
6000 O  O     . HOH H .   ? 0.5586 0.435  0.5707 0.0758  0.0374  0.0272  838 HOH A O     
6001 O  O     . HOH H .   ? 0.1961 0.0698 0.2095 0.0685  0.0032  0.0141  839 HOH A O     
6002 O  O     . HOH H .   ? 0.1106 0.1088 0.3847 -0.0482 0.0254  0.0547  840 HOH A O     
6003 O  O     . HOH H .   ? 0.1657 0.0934 0.2237 -0.0192 -0.0268 0.0096  841 HOH A O     
6004 O  O     . HOH H .   ? 0.2411 0.0445 0.2348 -0.006  -0.0782 0.0317  842 HOH A O     
6005 O  O     . HOH H .   ? 0.1342 0.0767 0.3276 -0.0541 -0.0753 0.0014  843 HOH A O     
6006 O  O     . HOH H .   ? 0.1056 0.068  0.2553 -0.0208 0.031   -0.0041 844 HOH A O     
6007 O  O     . HOH H .   ? 0.2347 0.0604 0.2128 0.0607  -0.0324 0.0105  845 HOH A O     
6008 O  O     . HOH I .   ? 0.5466 0.5089 0.7631 -0.0317 0.0113  -0.0123 101 HOH F O     
6009 O  O     . HOH I .   ? 0.3152 0.2591 0.566  -0.0273 0.0188  -0.0021 102 HOH F O     
6010 O  O     . HOH I .   ? 0.0812 0.0525 0.3435 -0.022  0.0367  0.0025  103 HOH F O     
6011 O  O     . HOH I .   ? 0.2124 0.1891 0.4508 -0.0343 0.0101  0.0045  104 HOH F O     
6012 O  O     . HOH J .   ? 0.3473 0.3177 0.5382 -0.0032 0.0445  0.0354  101 HOH G O     
6013 O  O     . HOH J .   ? 0.0774 0.0522 0.2765 -0.0207 0.0298  0.0036  102 HOH G O     
# 
