CNRS Nantes University US2B US2B
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***  hsTG2  ***

elNémo ID: 2408222113572906941

Job options:

ID        	=	 2408222113572906941
JOBID     	=	 hsTG2
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 25
DQMIN     	=	 -200
DQMAX     	=	 200
DQSTEP    	=	 10
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER hsTG2

data_2Q3Z
# 
_entry.id   2Q3Z 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.381 
_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   2Q3Z         pdb_00002q3z 10.2210/pdb2q3z/pdb 
RCSB  RCSB043119   ?            ?                   
WWPDB D_1000043119 ?            ?                   
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          1kv3 
_pdbx_database_related.details        . 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.entry_id                        2Q3Z 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2007-05-30 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Strop, P.'     1 
'Pinkas, D.M.'  2 
'Brunger, A.T.' 3 
'Khosla, C.'    4 
# 
_citation.id                        primary 
_citation.title                     'Transglutaminase 2 undergoes a large conformational change upon activation' 
_citation.journal_abbrev            'Plos Biol.' 
_citation.journal_volume            5 
_citation.page_first                e327 
_citation.page_last                 e327 
_citation.year                      2007 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           1544-9173 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   18092889 
_citation.pdbx_database_id_DOI      10.1371/journal.pbio.0050327 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Pinkas, D.M.'  1 ? 
primary 'Strop, P.'     2 ? 
primary 'Brunger, A.T.' 3 ? 
primary 'Khosla, C.'    4 ? 
# 
_cell.entry_id           2Q3Z 
_cell.length_a           71.671 
_cell.length_b           71.671 
_cell.length_c           309.010 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         2Q3Z 
_symmetry.space_group_name_H-M             'P 41 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                92 
_symmetry.space_group_name_Hall            ? 
# 
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 'Transglutaminase 2' 77341.602 1   2.3.2.13 ? ? ? 
2 polymer     syn Polypeptide          623.763   1   ?        ? ? ? 
3 non-polymer syn 'SULFATE ION'        96.063    5   ?        ? ? ? 
4 water       nat water                18.015    262 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Tissue transglutaminase, TGase C, TGC, TGC, Transglutaminase-2, TGase- H' 
# 
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  
;MAEELVLERCDLELETNGRDHHTADLCREKLVVRRGQPFWLTLHFEGRNYQASVDSLTFSVVTGPAPSQEAGTKARFPLR
DAVEEGDWTATVVDQQDCTLSLQLTTPANAPIGLYRLSLEASTGYQGSSFVLGHFILLFNAWCPADAVYLDSEEERQEYV
LTQQGFIYQGSAKFIKNIPWNFGQFQDGILDICLILLDVNPKFLKNAGRDCSRRSSPVYVGRVGSGMVNCNDDQGVLLGR
WDNNYGDGVSPMSWIGSVDILRRWKNHGCQRVKYGQCWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNLLIEYFRNEF
GEIQGDKSEMIWNFHCWVESWMTRPDLQPGYEGWQALDPTPQEKSEGTYCCGPVPVRAIKEGDLSTKYDAPFVFAEVNAD
VVDWIQQDDGSVHKSINRSLIVGLKISTKSVGRDEREDITHTYKYPEGSSEEREAFTRANHLNKLAEKEETGMAMRIRVG
QSMNMGSDFDVFAHITNNTAEEYVCRLLLCARTVSYNGILGPECGTKYLLNLTLEPFSEKSVPLCILYEKYRDCLTESNL
IKVRALLVEPVINSYLLAERDLYLENPEIKIRILGEPKQKRKLVAEVSLQNPLPVALEGCTFTVEGAGLTEEQKTVEIPD
PVEAGEEVKVRMDLVPLHMGLHKLVVNFESDKLKAVKGFRNVIIGPA
;
;MAEELVLERCDLELETNGRDHHTADLCREKLVVRRGQPFWLTLHFEGRNYQASVDSLTFSVVTGPAPSQEAGTKARFPLR
DAVEEGDWTATVVDQQDCTLSLQLTTPANAPIGLYRLSLEASTGYQGSSFVLGHFILLFNAWCPADAVYLDSEEERQEYV
LTQQGFIYQGSAKFIKNIPWNFGQFQDGILDICLILLDVNPKFLKNAGRDCSRRSSPVYVGRVGSGMVNCNDDQGVLLGR
WDNNYGDGVSPMSWIGSVDILRRWKNHGCQRVKYGQCWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNLLIEYFRNEF
GEIQGDKSEMIWNFHCWVESWMTRPDLQPGYEGWQALDPTPQEKSEGTYCCGPVPVRAIKEGDLSTKYDAPFVFAEVNAD
VVDWIQQDDGSVHKSINRSLIVGLKISTKSVGRDEREDITHTYKYPEGSSEEREAFTRANHLNKLAEKEETGMAMRIRVG
QSMNMGSDFDVFAHITNNTAEEYVCRLLLCARTVSYNGILGPECGTKYLLNLTLEPFSEKSVPLCILYEKYRDCLTESNL
IKVRALLVEPVINSYLLAERDLYLENPEIKIRILGEPKQKRKLVAEVSLQNPLPVALEGCTFTVEGAGLTEEQKTVEIPD
PVEAGEEVKVRMDLVPLHMGLHKLVVNFESDKLKAVKGFRNVIIGPA
;
A ? 
2 'polypeptide(L)' no yes '(ACE)P(ONL)LPF(NH2)' XPXLPFX X ? 
# 
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   ALA n 
1 3   GLU n 
1 4   GLU n 
1 5   LEU n 
1 6   VAL n 
1 7   LEU n 
1 8   GLU n 
1 9   ARG n 
1 10  CYS n 
1 11  ASP n 
1 12  LEU n 
1 13  GLU n 
1 14  LEU n 
1 15  GLU n 
1 16  THR n 
1 17  ASN n 
1 18  GLY n 
1 19  ARG n 
1 20  ASP n 
1 21  HIS n 
1 22  HIS n 
1 23  THR n 
1 24  ALA n 
1 25  ASP n 
1 26  LEU n 
1 27  CYS n 
1 28  ARG n 
1 29  GLU n 
1 30  LYS n 
1 31  LEU n 
1 32  VAL n 
1 33  VAL n 
1 34  ARG n 
1 35  ARG n 
1 36  GLY n 
1 37  GLN n 
1 38  PRO n 
1 39  PHE n 
1 40  TRP n 
1 41  LEU n 
1 42  THR n 
1 43  LEU n 
1 44  HIS n 
1 45  PHE n 
1 46  GLU n 
1 47  GLY n 
1 48  ARG n 
1 49  ASN n 
1 50  TYR n 
1 51  GLN n 
1 52  ALA n 
1 53  SER n 
1 54  VAL n 
1 55  ASP n 
1 56  SER n 
1 57  LEU n 
1 58  THR n 
1 59  PHE n 
1 60  SER n 
1 61  VAL n 
1 62  VAL n 
1 63  THR n 
1 64  GLY n 
1 65  PRO n 
1 66  ALA n 
1 67  PRO n 
1 68  SER n 
1 69  GLN n 
1 70  GLU n 
1 71  ALA n 
1 72  GLY n 
1 73  THR n 
1 74  LYS n 
1 75  ALA n 
1 76  ARG n 
1 77  PHE n 
1 78  PRO n 
1 79  LEU n 
1 80  ARG n 
1 81  ASP n 
1 82  ALA n 
1 83  VAL n 
1 84  GLU n 
1 85  GLU n 
1 86  GLY n 
1 87  ASP n 
1 88  TRP n 
1 89  THR n 
1 90  ALA n 
1 91  THR n 
1 92  VAL n 
1 93  VAL n 
1 94  ASP n 
1 95  GLN n 
1 96  GLN n 
1 97  ASP n 
1 98  CYS n 
1 99  THR n 
1 100 LEU n 
1 101 SER n 
1 102 LEU n 
1 103 GLN n 
1 104 LEU n 
1 105 THR n 
1 106 THR n 
1 107 PRO n 
1 108 ALA n 
1 109 ASN n 
1 110 ALA n 
1 111 PRO n 
1 112 ILE n 
1 113 GLY n 
1 114 LEU n 
1 115 TYR n 
1 116 ARG n 
1 117 LEU n 
1 118 SER n 
1 119 LEU n 
1 120 GLU n 
1 121 ALA n 
1 122 SER n 
1 123 THR n 
1 124 GLY n 
1 125 TYR n 
1 126 GLN n 
1 127 GLY n 
1 128 SER n 
1 129 SER n 
1 130 PHE n 
1 131 VAL n 
1 132 LEU n 
1 133 GLY n 
1 134 HIS n 
1 135 PHE n 
1 136 ILE n 
1 137 LEU n 
1 138 LEU n 
1 139 PHE n 
1 140 ASN n 
1 141 ALA n 
1 142 TRP n 
1 143 CYS n 
1 144 PRO n 
1 145 ALA n 
1 146 ASP n 
1 147 ALA n 
1 148 VAL n 
1 149 TYR n 
1 150 LEU n 
1 151 ASP n 
1 152 SER n 
1 153 GLU n 
1 154 GLU n 
1 155 GLU n 
1 156 ARG n 
1 157 GLN n 
1 158 GLU n 
1 159 TYR n 
1 160 VAL n 
1 161 LEU n 
1 162 THR n 
1 163 GLN n 
1 164 GLN n 
1 165 GLY n 
1 166 PHE n 
1 167 ILE n 
1 168 TYR n 
1 169 GLN n 
1 170 GLY n 
1 171 SER n 
1 172 ALA n 
1 173 LYS n 
1 174 PHE n 
1 175 ILE n 
1 176 LYS n 
1 177 ASN n 
1 178 ILE n 
1 179 PRO n 
1 180 TRP n 
1 181 ASN n 
1 182 PHE n 
1 183 GLY n 
1 184 GLN n 
1 185 PHE n 
1 186 GLN n 
1 187 ASP n 
1 188 GLY n 
1 189 ILE n 
1 190 LEU n 
1 191 ASP n 
1 192 ILE n 
1 193 CYS n 
1 194 LEU n 
1 195 ILE n 
1 196 LEU n 
1 197 LEU n 
1 198 ASP n 
1 199 VAL n 
1 200 ASN n 
1 201 PRO n 
1 202 LYS n 
1 203 PHE n 
1 204 LEU n 
1 205 LYS n 
1 206 ASN n 
1 207 ALA n 
1 208 GLY n 
1 209 ARG n 
1 210 ASP n 
1 211 CYS n 
1 212 SER n 
1 213 ARG n 
1 214 ARG n 
1 215 SER n 
1 216 SER n 
1 217 PRO n 
1 218 VAL n 
1 219 TYR n 
1 220 VAL n 
1 221 GLY n 
1 222 ARG n 
1 223 VAL n 
1 224 GLY n 
1 225 SER n 
1 226 GLY n 
1 227 MET n 
1 228 VAL n 
1 229 ASN n 
1 230 CYS n 
1 231 ASN n 
1 232 ASP n 
1 233 ASP n 
1 234 GLN n 
1 235 GLY n 
1 236 VAL n 
1 237 LEU n 
1 238 LEU n 
1 239 GLY n 
1 240 ARG n 
1 241 TRP n 
1 242 ASP n 
1 243 ASN n 
1 244 ASN n 
1 245 TYR n 
1 246 GLY n 
1 247 ASP n 
1 248 GLY n 
1 249 VAL n 
1 250 SER n 
1 251 PRO n 
1 252 MET n 
1 253 SER n 
1 254 TRP n 
1 255 ILE n 
1 256 GLY n 
1 257 SER n 
1 258 VAL n 
1 259 ASP n 
1 260 ILE n 
1 261 LEU n 
1 262 ARG n 
1 263 ARG n 
1 264 TRP n 
1 265 LYS n 
1 266 ASN n 
1 267 HIS n 
1 268 GLY n 
1 269 CYS n 
1 270 GLN n 
1 271 ARG n 
1 272 VAL n 
1 273 LYS n 
1 274 TYR n 
1 275 GLY n 
1 276 GLN n 
1 277 CYS n 
1 278 TRP n 
1 279 VAL n 
1 280 PHE n 
1 281 ALA n 
1 282 ALA n 
1 283 VAL n 
1 284 ALA n 
1 285 CYS n 
1 286 THR n 
1 287 VAL n 
1 288 LEU n 
1 289 ARG n 
1 290 CYS n 
1 291 LEU n 
1 292 GLY n 
1 293 ILE n 
1 294 PRO n 
1 295 THR n 
1 296 ARG n 
1 297 VAL n 
1 298 VAL n 
1 299 THR n 
1 300 ASN n 
1 301 TYR n 
1 302 ASN n 
1 303 SER n 
1 304 ALA n 
1 305 HIS n 
1 306 ASP n 
1 307 GLN n 
1 308 ASN n 
1 309 SER n 
1 310 ASN n 
1 311 LEU n 
1 312 LEU n 
1 313 ILE n 
1 314 GLU n 
1 315 TYR n 
1 316 PHE n 
1 317 ARG n 
1 318 ASN n 
1 319 GLU n 
1 320 PHE n 
1 321 GLY n 
1 322 GLU n 
1 323 ILE n 
1 324 GLN n 
1 325 GLY n 
1 326 ASP n 
1 327 LYS n 
1 328 SER n 
1 329 GLU n 
1 330 MET n 
1 331 ILE n 
1 332 TRP n 
1 333 ASN n 
1 334 PHE n 
1 335 HIS n 
1 336 CYS n 
1 337 TRP n 
1 338 VAL n 
1 339 GLU n 
1 340 SER n 
1 341 TRP n 
1 342 MET n 
1 343 THR n 
1 344 ARG n 
1 345 PRO n 
1 346 ASP n 
1 347 LEU n 
1 348 GLN n 
1 349 PRO n 
1 350 GLY n 
1 351 TYR n 
1 352 GLU n 
1 353 GLY n 
1 354 TRP n 
1 355 GLN n 
1 356 ALA n 
1 357 LEU n 
1 358 ASP n 
1 359 PRO n 
1 360 THR n 
1 361 PRO n 
1 362 GLN n 
1 363 GLU n 
1 364 LYS n 
1 365 SER n 
1 366 GLU n 
1 367 GLY n 
1 368 THR n 
1 369 TYR n 
1 370 CYS n 
1 371 CYS n 
1 372 GLY n 
1 373 PRO n 
1 374 VAL n 
1 375 PRO n 
1 376 VAL n 
1 377 ARG n 
1 378 ALA n 
1 379 ILE n 
1 380 LYS n 
1 381 GLU n 
1 382 GLY n 
1 383 ASP n 
1 384 LEU n 
1 385 SER n 
1 386 THR n 
1 387 LYS n 
1 388 TYR n 
1 389 ASP n 
1 390 ALA n 
1 391 PRO n 
1 392 PHE n 
1 393 VAL n 
1 394 PHE n 
1 395 ALA n 
1 396 GLU n 
1 397 VAL n 
1 398 ASN n 
1 399 ALA n 
1 400 ASP n 
1 401 VAL n 
1 402 VAL n 
1 403 ASP n 
1 404 TRP n 
1 405 ILE n 
1 406 GLN n 
1 407 GLN n 
1 408 ASP n 
1 409 ASP n 
1 410 GLY n 
1 411 SER n 
1 412 VAL n 
1 413 HIS n 
1 414 LYS n 
1 415 SER n 
1 416 ILE n 
1 417 ASN n 
1 418 ARG n 
1 419 SER n 
1 420 LEU n 
1 421 ILE n 
1 422 VAL n 
1 423 GLY n 
1 424 LEU n 
1 425 LYS n 
1 426 ILE n 
1 427 SER n 
1 428 THR n 
1 429 LYS n 
1 430 SER n 
1 431 VAL n 
1 432 GLY n 
1 433 ARG n 
1 434 ASP n 
1 435 GLU n 
1 436 ARG n 
1 437 GLU n 
1 438 ASP n 
1 439 ILE n 
1 440 THR n 
1 441 HIS n 
1 442 THR n 
1 443 TYR n 
1 444 LYS n 
1 445 TYR n 
1 446 PRO n 
1 447 GLU n 
1 448 GLY n 
1 449 SER n 
1 450 SER n 
1 451 GLU n 
1 452 GLU n 
1 453 ARG n 
1 454 GLU n 
1 455 ALA n 
1 456 PHE n 
1 457 THR n 
1 458 ARG n 
1 459 ALA n 
1 460 ASN n 
1 461 HIS n 
1 462 LEU n 
1 463 ASN n 
1 464 LYS n 
1 465 LEU n 
1 466 ALA n 
1 467 GLU n 
1 468 LYS n 
1 469 GLU n 
1 470 GLU n 
1 471 THR n 
1 472 GLY n 
1 473 MET n 
1 474 ALA n 
1 475 MET n 
1 476 ARG n 
1 477 ILE n 
1 478 ARG n 
1 479 VAL n 
1 480 GLY n 
1 481 GLN n 
1 482 SER n 
1 483 MET n 
1 484 ASN n 
1 485 MET n 
1 486 GLY n 
1 487 SER n 
1 488 ASP n 
1 489 PHE n 
1 490 ASP n 
1 491 VAL n 
1 492 PHE n 
1 493 ALA n 
1 494 HIS n 
1 495 ILE n 
1 496 THR n 
1 497 ASN n 
1 498 ASN n 
1 499 THR n 
1 500 ALA n 
1 501 GLU n 
1 502 GLU n 
1 503 TYR n 
1 504 VAL n 
1 505 CYS n 
1 506 ARG n 
1 507 LEU n 
1 508 LEU n 
1 509 LEU n 
1 510 CYS n 
1 511 ALA n 
1 512 ARG n 
1 513 THR n 
1 514 VAL n 
1 515 SER n 
1 516 TYR n 
1 517 ASN n 
1 518 GLY n 
1 519 ILE n 
1 520 LEU n 
1 521 GLY n 
1 522 PRO n 
1 523 GLU n 
1 524 CYS n 
1 525 GLY n 
1 526 THR n 
1 527 LYS n 
1 528 TYR n 
1 529 LEU n 
1 530 LEU n 
1 531 ASN n 
1 532 LEU n 
1 533 THR n 
1 534 LEU n 
1 535 GLU n 
1 536 PRO n 
1 537 PHE n 
1 538 SER n 
1 539 GLU n 
1 540 LYS n 
1 541 SER n 
1 542 VAL n 
1 543 PRO n 
1 544 LEU n 
1 545 CYS n 
1 546 ILE n 
1 547 LEU n 
1 548 TYR n 
1 549 GLU n 
1 550 LYS n 
1 551 TYR n 
1 552 ARG n 
1 553 ASP n 
1 554 CYS n 
1 555 LEU n 
1 556 THR n 
1 557 GLU n 
1 558 SER n 
1 559 ASN n 
1 560 LEU n 
1 561 ILE n 
1 562 LYS n 
1 563 VAL n 
1 564 ARG n 
1 565 ALA n 
1 566 LEU n 
1 567 LEU n 
1 568 VAL n 
1 569 GLU n 
1 570 PRO n 
1 571 VAL n 
1 572 ILE n 
1 573 ASN n 
1 574 SER n 
1 575 TYR n 
1 576 LEU n 
1 577 LEU n 
1 578 ALA n 
1 579 GLU n 
1 580 ARG n 
1 581 ASP n 
1 582 LEU n 
1 583 TYR n 
1 584 LEU n 
1 585 GLU n 
1 586 ASN n 
1 587 PRO n 
1 588 GLU n 
1 589 ILE n 
1 590 LYS n 
1 591 ILE n 
1 592 ARG n 
1 593 ILE n 
1 594 LEU n 
1 595 GLY n 
1 596 GLU n 
1 597 PRO n 
1 598 LYS n 
1 599 GLN n 
1 600 LYS n 
1 601 ARG n 
1 602 LYS n 
1 603 LEU n 
1 604 VAL n 
1 605 ALA n 
1 606 GLU n 
1 607 VAL n 
1 608 SER n 
1 609 LEU n 
1 610 GLN n 
1 611 ASN n 
1 612 PRO n 
1 613 LEU n 
1 614 PRO n 
1 615 VAL n 
1 616 ALA n 
1 617 LEU n 
1 618 GLU n 
1 619 GLY n 
1 620 CYS n 
1 621 THR n 
1 622 PHE n 
1 623 THR n 
1 624 VAL n 
1 625 GLU n 
1 626 GLY n 
1 627 ALA n 
1 628 GLY n 
1 629 LEU n 
1 630 THR n 
1 631 GLU n 
1 632 GLU n 
1 633 GLN n 
1 634 LYS n 
1 635 THR n 
1 636 VAL n 
1 637 GLU n 
1 638 ILE n 
1 639 PRO n 
1 640 ASP n 
1 641 PRO n 
1 642 VAL n 
1 643 GLU n 
1 644 ALA n 
1 645 GLY n 
1 646 GLU n 
1 647 GLU n 
1 648 VAL n 
1 649 LYS n 
1 650 VAL n 
1 651 ARG n 
1 652 MET n 
1 653 ASP n 
1 654 LEU n 
1 655 VAL n 
1 656 PRO n 
1 657 LEU n 
1 658 HIS n 
1 659 MET n 
1 660 GLY n 
1 661 LEU n 
1 662 HIS n 
1 663 LYS n 
1 664 LEU n 
1 665 VAL n 
1 666 VAL n 
1 667 ASN n 
1 668 PHE n 
1 669 GLU n 
1 670 SER n 
1 671 ASP n 
1 672 LYS n 
1 673 LEU n 
1 674 LYS n 
1 675 ALA n 
1 676 VAL n 
1 677 LYS n 
1 678 GLY n 
1 679 PHE n 
1 680 ARG n 
1 681 ASN n 
1 682 VAL n 
1 683 ILE n 
1 684 ILE n 
1 685 GLY n 
1 686 PRO n 
1 687 ALA n 
2 1   ACE n 
2 2   PRO n 
2 3   ONL n 
2 4   LEU n 
2 5   PRO n 
2 6   PHE n 
2 7   NH2 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                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     Homo 
_entity_src_gen.pdbx_gene_src_gene                 TGM2 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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                     Escherichia 
_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                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_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                'Chemically synthesized.' 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
_struct_ref.pdbx_db_isoform 
1 UNP TGM2_HUMAN P21980 1 
;MAEELVLERCDLELETNGRDHHTADLCREKLVVRRGQPFWLTLHFEGRNYEASVDSLTFSVVTGPAPSQEAGTKARFPLR
DAVEEGDWTATVVDQQDCTLSLQLTTPANAPIGLYRLSLEASTGYQGSSFVLGHFILLFNAWCPADAVYLDSEEERQEYV
LTQQGFIYQGSAKFIKNIPWNFGQFEDGILDICLILLDVNPKFLKNAGRDCSRRSSPVYVGRVVSGMVNCNDDQGVLLGR
WDNNYGDGVSPMSWIGSVDILRRWKNHGCQRVKYGQCWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNLLIEYFRNEF
GEIQGDKSEMIWNFHCWVESWMTRPDLQPGYEGWQALDPTPQEKSEGTYCCGPVPVRAIKEGDLSTKYDAPFVFAEVNAD
VVDWIQQDDGSVHKSINRSLIVGLKISTKSVGRDEREDITHTYKYPEGSSEEREAFTRANHLNKLAEKEETGMAMRIRVG
QSMNMGSDFDVFAHITNNTAEEYVCRLLLCARTVSYNGILGPECGTKYLLNLNLEPFSEKSVPLCILYEKYRDCLTESNL
IKVRALLVEPVINSYLLAERDLYLENPEIKIRILGEPKQKRKLVAEVSLQNPLPVALEGCTFTVEGAGLTEEQKTVEIPD
PVEAGEEVKVRMDLLPLHMGLHKLVVNFESDKLKAVKGFRNVIIGPA
;
1 ? 
2 PDB 2Q3Z       2Q3Z   2 ? ? ? 
# 
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 2Q3Z A 1 ? 687 ? P21980 1 ? 687 ? 1 687 
2 2 2Q3Z X 1 ? 7   ? 2Q3Z   1 ? 7   ? 1 7   
# 
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 2Q3Z GLN A 51  ? UNP P21980 GLU 51  conflict 51  1 
1 2Q3Z GLN A 186 ? UNP P21980 GLU 186 conflict 186 2 
1 2Q3Z GLY A 224 ? UNP P21980 VAL 224 conflict 224 3 
1 2Q3Z THR A 533 ? UNP P21980 ASN 533 conflict 533 4 
1 2Q3Z VAL A 655 ? UNP P21980 LEU 655 conflict 655 5 
# 
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 
ACE non-polymer         . 'ACETYL GROUP'     ? 'C2 H4 O'        44.053  
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 
CYS 'L-peptide linking' y CYSTEINE           ? 'C3 H7 N O2 S'   121.158 
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 
MET 'L-peptide linking' y METHIONINE         ? 'C5 H11 N O2 S'  149.211 
NH2 non-polymer         . 'AMINO GROUP'      ? 'H2 N'           16.023  
ONL 'L-peptide linking' . 5-OXO-L-NORLEUCINE ? 'C6 H11 N O3'    145.156 
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 
SO4 non-polymer         . 'SULFATE ION'      ? 'O4 S -2'        96.063  
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 
# 
_exptl.crystals_number   1 
_exptl.entry_id          2Q3Z 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.54 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_percent_sol   51.64 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              7.25 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_details    '100 mM HEPES pH 7.25, 1.25M Amm. sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 298K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 315' 
_diffrn_detector.pdbx_collection_date   2006-02-09 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    'Si(111)' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9794 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SSRL BEAMLINE BL11-1' 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.9794 
_diffrn_source.pdbx_synchrotron_site       SSRL 
_diffrn_source.pdbx_synchrotron_beamline   BL11-1 
# 
_reflns.entry_id                     2Q3Z 
_reflns.d_resolution_high            2.000 
_reflns.d_resolution_low             50.000 
_reflns.number_obs                   53209 
_reflns.pdbx_Rmerge_I_obs            0.072 
_reflns.pdbx_netI_over_sigmaI        11.800 
_reflns.pdbx_chi_squared             0.937 
_reflns.pdbx_redundancy              6.300 
_reflns.percent_possible_obs         94.900 
_reflns.observed_criterion_sigma_F   ? 
_reflns.observed_criterion_sigma_I   ? 
_reflns.number_all                   53209 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.R_free_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.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             2.00 
_reflns_shell.d_res_low              2.09 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.Rmerge_I_obs           0.296 
_reflns_shell.meanI_over_sigI_obs    2.38 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.pdbx_chi_squared       0.905 
_reflns_shell.pdbx_redundancy        4.50 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      5332 
_reflns_shell.percent_possible_all   78.20 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 2Q3Z 
_refine.ls_d_res_high                            2.000 
_refine.ls_d_res_low                             25.000 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.ls_percent_reflns_obs                    100.000 
_refine.ls_number_reflns_obs                     53209 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  
;TLS group 1 
1 to 462 
TLS group 2 
467 to 586 
TLS group 3 
587 to 683
;
_refine.ls_R_factor_obs                          0.231 
_refine.ls_R_factor_R_work                       0.228 
_refine.ls_R_factor_R_free                       0.266 
_refine.ls_percent_reflns_R_free                 6.300 
_refine.ls_number_reflns_R_free                  3482 
_refine.B_iso_mean                               39.305 
_refine.aniso_B[1][1]                            1.300 
_refine.aniso_B[2][2]                            1.300 
_refine.aniso_B[3][3]                            -2.600 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.946 
_refine.correlation_coeff_Fo_to_Fc_free          0.914 
_refine.pdbx_overall_ESU_R                       0.200 
_refine.pdbx_overall_ESU_R_Free                  0.177 
_refine.overall_SU_ML                            0.154 
_refine.overall_SU_B                             10.688 
_refine.solvent_model_details                    'BABINET MODEL WITH MASK' 
_refine.pdbx_solvent_vdw_probe_radii             1.200 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_number_reflns_all                     53209 
_refine.ls_R_factor_all                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      1KV3 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_TLS_residual_ADP_flag               'LIKELY RESIDUAL' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        5232 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         25 
_refine_hist.number_atoms_solvent             262 
_refine_hist.number_atoms_total               5519 
_refine_hist.d_res_high                       2.000 
_refine_hist.d_res_low                        25.000 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d         5301 0.012  0.022  ? 'X-RAY DIFFRACTION' ? 
r_bond_other_d           3592 0.002  0.020  ? 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg      7205 1.361  1.967  ? 'X-RAY DIFFRACTION' ? 
r_angle_other_deg        8646 0.862  3.003  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg   649  7.010  5.000  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg   243  32.904 24.074 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg   858  17.398 15.000 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg   36   15.947 15.000 ? 'X-RAY DIFFRACTION' ? 
r_chiral_restr           799  0.085  0.200  ? 'X-RAY DIFFRACTION' ? 
r_gen_planes_refined     5894 0.005  0.020  ? 'X-RAY DIFFRACTION' ? 
r_gen_planes_other       1068 0.001  0.020  ? 'X-RAY DIFFRACTION' ? 
r_nbd_refined            964  0.199  0.200  ? 'X-RAY DIFFRACTION' ? 
r_nbd_other              3808 0.202  0.200  ? 'X-RAY DIFFRACTION' ? 
r_nbtor_refined          2509 0.178  0.200  ? 'X-RAY DIFFRACTION' ? 
r_nbtor_other            3001 0.088  0.200  ? 'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined    274  0.194  0.200  ? 'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other      1    0.019  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined   14   0.100  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other     53   0.137  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined 18   0.164  0.200  ? 'X-RAY DIFFRACTION' ? 
r_mcbond_it              4188 0.865  1.500  ? 'X-RAY DIFFRACTION' ? 
r_mcbond_other           1327 0.156  1.500  ? 'X-RAY DIFFRACTION' ? 
r_mcangle_it             5260 1.049  2.000  ? 'X-RAY DIFFRACTION' ? 
r_scbond_it              2370 1.614  3.000  ? 'X-RAY DIFFRACTION' ? 
r_scangle_it             1945 2.340  4.500  ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.d_res_high                       2.000 
_refine_ls_shell.d_res_low                        2.052 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               100.000 
_refine_ls_shell.number_reflns_R_work             3616 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.278 
_refine_ls_shell.R_factor_R_free                  0.326 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             176 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                3792 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  2Q3Z 
_struct.title                     'Transglutaminase 2 undergoes large conformational change upon activation' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2Q3Z 
_struct_keywords.pdbx_keywords   TRANSFERASE 
_struct_keywords.text            'Transglutaminase 2, tissue transglutaminase, TG2, TRANSFERASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 4 ? 
# 
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  1  GLU A 13  ? HIS A 21  ? GLU A 13  HIS A 21  1 ? 9  
HELX_P HELX_P2  2  THR A 23  ? CYS A 27  ? THR A 23  CYS A 27  5 ? 5  
HELX_P HELX_P3  3  SER A 152 ? VAL A 160 ? SER A 152 VAL A 160 1 ? 9  
HELX_P HELX_P4  4  GLY A 188 ? VAL A 199 ? GLY A 188 VAL A 199 1 ? 12 
HELX_P HELX_P5  5  ASN A 200 ? ASN A 206 ? ASN A 200 ASN A 206 1 ? 7  
HELX_P HELX_P6  6  ASN A 206 ? ARG A 214 ? ASN A 206 ARG A 214 1 ? 9  
HELX_P HELX_P7  7  SER A 216 ? MET A 227 ? SER A 216 MET A 227 1 ? 12 
HELX_P HELX_P8  8  SER A 257 ? HIS A 267 ? SER A 257 HIS A 267 1 ? 11 
HELX_P HELX_P9  9  GLN A 276 ? GLY A 292 ? GLN A 276 GLY A 292 1 ? 17 
HELX_P HELX_P10 10 ASN A 310 ? ASN A 318 ? ASN A 310 ASN A 318 1 ? 9  
HELX_P HELX_P11 11 VAL A 376 ? GLU A 381 ? VAL A 376 GLU A 381 1 ? 6  
HELX_P HELX_P12 12 ASP A 389 ? ASN A 398 ? ASP A 389 ASN A 398 1 ? 10 
HELX_P HELX_P13 13 ILE A 439 ? LYS A 444 ? ILE A 439 LYS A 444 1 ? 6  
HELX_P HELX_P14 14 SER A 449 ? HIS A 461 ? SER A 449 HIS A 461 1 ? 13 
HELX_P HELX_P15 15 LEU A 547 ? ARG A 552 ? LEU A 547 ARG A 552 1 ? 6  
# 
_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 
disulf1 disulf ?    ? A CYS 370 SG ? ? ? 1_555 A CYS 371 SG ? ? A CYS 370 A CYS 371 1_555 ? ? ? ? ? ? ? 2.032 ? ? 
covale1 covale none ? A CYS 277 SG ? ? ? 1_555 B ONL 3   CE ? ? A CYS 277 X ONL 3   1_555 ? ? ? ? ? ? ? 1.629 ? ? 
covale2 covale both ? B ACE 1   C  ? ? ? 1_555 B PRO 2   N  ? ? X ACE 1   X PRO 2   1_555 ? ? ? ? ? ? ? 1.342 ? ? 
covale3 covale both ? B PRO 2   C  ? ? ? 1_555 B ONL 3   N  ? ? X PRO 2   X ONL 3   1_555 ? ? ? ? ? ? ? 1.324 ? ? 
covale4 covale both ? B ONL 3   C  ? ? ? 1_555 B LEU 4   N  ? ? X ONL 3   X LEU 4   1_555 ? ? ? ? ? ? ? 1.322 ? ? 
covale5 covale both ? B PHE 6   C  ? ? ? 1_555 B NH2 7   N  ? ? X PHE 6   X NH2 7   1_555 ? ? ? ? ? ? ? 1.330 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
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 LYS 273 A . ? LYS 273 A TYR 274 A ? TYR 274 A 1 0.48  
2 CYS 370 A . ? CYS 370 A CYS 371 A ? CYS 371 A 1 -4.20 
3 GLY 372 A . ? GLY 372 A PRO 373 A ? PRO 373 A 1 9.13  
4 LYS 387 A . ? LYS 387 A TYR 388 A ? TYR 388 A 1 2.70  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 4 ? 
B ? 5 ? 
C ? 2 ? 
D ? 2 ? 
E ? 6 ? 
F ? 6 ? 
G ? 3 ? 
H ? 3 ? 
I ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? anti-parallel 
A 2 3 ? anti-parallel 
A 3 4 ? anti-parallel 
B 1 2 ? parallel      
B 2 3 ? anti-parallel 
B 3 4 ? anti-parallel 
B 4 5 ? anti-parallel 
C 1 2 ? anti-parallel 
D 1 2 ? parallel      
E 1 2 ? anti-parallel 
E 2 3 ? anti-parallel 
E 3 4 ? anti-parallel 
E 4 5 ? anti-parallel 
E 5 6 ? anti-parallel 
F 1 2 ? anti-parallel 
F 2 3 ? parallel      
F 3 4 ? anti-parallel 
F 4 5 ? anti-parallel 
F 5 6 ? anti-parallel 
G 1 2 ? anti-parallel 
G 2 3 ? anti-parallel 
H 1 2 ? anti-parallel 
H 2 3 ? anti-parallel 
I 1 2 ? anti-parallel 
I 2 3 ? anti-parallel 
I 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 LEU A 7   ? ASP A 11  ? LEU A 7   ASP A 11  
A 2 PHE A 39  ? PHE A 45  ? PHE A 39  PHE A 45  
A 3 THR A 99  ? THR A 105 ? THR A 99  THR A 105 
A 4 THR A 89  ? GLN A 95  ? THR A 89  GLN A 95  
B 1 VAL A 32  ? ARG A 34  ? VAL A 32  ARG A 34  
B 2 GLN A 126 ? LEU A 138 ? GLN A 126 LEU A 138 
B 3 GLY A 113 ? THR A 123 ? GLY A 113 THR A 123 
B 4 ASP A 55  ? THR A 63  ? ASP A 55  THR A 63  
B 5 LYS A 74  ? PRO A 78  ? LYS A 74  PRO A 78  
C 1 GLN A 164 ? GLY A 170 ? GLN A 164 GLY A 170 
C 2 ILE A 175 ? ASN A 181 ? ILE A 175 ASN A 181 
D 1 LEU A 237 ? GLY A 239 ? LEU A 237 GLY A 239 
D 2 VAL A 272 ? GLY A 275 ? VAL A 272 GLY A 275 
E 1 VAL A 374 ? PRO A 375 ? VAL A 374 PRO A 375 
E 2 GLY A 353 ? LEU A 357 ? GLY A 353 LEU A 357 
E 3 PHE A 334 ? MET A 342 ? PHE A 334 MET A 342 
E 4 THR A 295 ? ALA A 304 ? THR A 295 ALA A 304 
E 5 LEU A 420 ? LYS A 429 ? LEU A 420 LYS A 429 
E 6 ARG A 436 ? ASP A 438 ? ARG A 436 ASP A 438 
F 1 SER A 415 ? ILE A 416 ? SER A 415 ILE A 416 
F 2 ASP A 400 ? TRP A 404 ? ASP A 400 TRP A 404 
F 3 SER A 574 ? TYR A 583 ? SER A 574 TYR A 583 
F 4 LEU A 560 ? GLU A 569 ? LEU A 560 GLU A 569 
F 5 TYR A 503 ? VAL A 514 ? TYR A 503 VAL A 514 
F 6 LEU A 520 ? LEU A 534 ? LEU A 520 LEU A 534 
G 1 MET A 473 ? ARG A 478 ? MET A 473 ARG A 478 
G 2 PHE A 489 ? ASN A 497 ? PHE A 489 ASN A 497 
G 3 SER A 538 ? ILE A 546 ? SER A 538 ILE A 546 
H 1 LYS A 590 ? LEU A 594 ? LYS A 590 LEU A 594 
H 2 LEU A 603 ? GLN A 610 ? LEU A 603 GLN A 610 
H 3 GLU A 647 ? LEU A 654 ? GLU A 647 LEU A 654 
I 1 LYS A 634 ? ILE A 638 ? LYS A 634 ILE A 638 
I 2 CYS A 620 ? GLU A 625 ? CYS A 620 GLU A 625 
I 3 HIS A 662 ? GLU A 669 ? HIS A 662 GLU A 669 
I 4 VAL A 676 ? VAL A 682 ? VAL A 676 VAL A 682 
# 
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 
A 1 2 N GLU A 8   ? N GLU A 8   O HIS A 44  ? O HIS A 44  
A 2 3 N LEU A 41  ? N LEU A 41  O LEU A 102 ? O LEU A 102 
A 3 4 O GLN A 103 ? O GLN A 103 N THR A 91  ? N THR A 91  
B 1 2 N VAL A 33  ? N VAL A 33  O ILE A 136 ? O ILE A 136 
B 2 3 O PHE A 130 ? O PHE A 130 N LEU A 119 ? N LEU A 119 
B 3 4 O SER A 118 ? O SER A 118 N SER A 60  ? N SER A 60  
B 4 5 N PHE A 59  ? N PHE A 59  O PHE A 77  ? O PHE A 77  
C 1 2 N GLN A 169 ? N GLN A 169 O LYS A 176 ? O LYS A 176 
D 1 2 N LEU A 238 ? N LEU A 238 O GLY A 275 ? O GLY A 275 
E 1 2 O VAL A 374 ? O VAL A 374 N ALA A 356 ? N ALA A 356 
E 2 3 O GLY A 353 ? O GLY A 353 N MET A 342 ? N MET A 342 
E 3 4 O HIS A 335 ? O HIS A 335 N ASN A 300 ? N ASN A 300 
E 4 5 N SER A 303 ? N SER A 303 O ILE A 421 ? O ILE A 421 
E 5 6 N THR A 428 ? N THR A 428 O GLU A 437 ? O GLU A 437 
F 1 2 O SER A 415 ? O SER A 415 N ASP A 403 ? N ASP A 403 
F 2 3 N ASP A 400 ? N ASP A 400 O TYR A 575 ? O TYR A 575 
F 3 4 O LEU A 582 ? O LEU A 582 N ILE A 561 ? N ILE A 561 
F 4 5 O VAL A 568 ? O VAL A 568 N ARG A 506 ? N ARG A 506 
F 5 6 N CYS A 505 ? N CYS A 505 O LEU A 532 ? O LEU A 532 
G 1 2 N ARG A 476 ? N ARG A 476 O HIS A 494 ? O HIS A 494 
G 2 3 N PHE A 489 ? N PHE A 489 O ILE A 546 ? O ILE A 546 
H 1 2 N ARG A 592 ? N ARG A 592 O GLU A 606 ? O GLU A 606 
H 2 3 N LEU A 603 ? N LEU A 603 O LEU A 654 ? O LEU A 654 
I 1 2 O LYS A 634 ? O LYS A 634 N VAL A 624 ? N VAL A 624 
I 2 3 N GLU A 625 ? N GLU A 625 O VAL A 665 ? O VAL A 665 
I 3 4 N LEU A 664 ? N LEU A 664 O ARG A 680 ? O ARG A 680 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A SO4 688 ? 4 'BINDING SITE FOR RESIDUE SO4 A 688' 
AC2 Software A SO4 689 ? 6 'BINDING SITE FOR RESIDUE SO4 A 689' 
AC3 Software A SO4 690 ? 1 'BINDING SITE FOR RESIDUE SO4 A 690' 
AC4 Software A SO4 691 ? 5 'BINDING SITE FOR RESIDUE SO4 A 691' 
AC5 Software A SO4 692 ? 4 'BINDING SITE FOR RESIDUE SO4 A 692' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4 LYS A 202 ? LYS A 202 . ? 1_555 ? 
2  AC1 4 ARG A 222 ? ARG A 222 . ? 1_555 ? 
3  AC1 4 GLY A 367 ? GLY A 367 . ? 1_555 ? 
4  AC1 4 THR A 368 ? THR A 368 . ? 1_555 ? 
5  AC2 6 LYS A 202 ? LYS A 202 . ? 1_555 ? 
6  AC2 6 ARG A 209 ? ARG A 209 . ? 1_555 ? 
7  AC2 6 TYR A 219 ? TYR A 219 . ? 1_555 ? 
8  AC2 6 HOH H .   ? HOH A 728 . ? 1_555 ? 
9  AC2 6 HOH H .   ? HOH A 931 . ? 1_555 ? 
10 AC2 6 HOH H .   ? HOH A 947 . ? 1_555 ? 
11 AC3 1 ARG A 80  ? ARG A 80  . ? 1_555 ? 
12 AC4 5 ARG A 80  ? ARG A 80  . ? 1_555 ? 
13 AC4 5 ASP A 81  ? ASP A 81  . ? 1_555 ? 
14 AC4 5 ALA A 82  ? ALA A 82  . ? 1_555 ? 
15 AC4 5 HOH H .   ? HOH A 753 . ? 1_555 ? 
16 AC4 5 HOH H .   ? HOH A 873 . ? 5_555 ? 
17 AC5 4 ARG A 478 ? ARG A 478 . ? 1_555 ? 
18 AC5 4 VAL A 479 ? VAL A 479 . ? 1_555 ? 
19 AC5 4 GLY A 480 ? GLY A 480 . ? 1_555 ? 
20 AC5 4 ARG A 580 ? ARG A 580 . ? 1_555 ? 
# 
_atom_sites.entry_id                    2Q3Z 
_atom_sites.fract_transf_matrix[1][1]   0.013953 
_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]   0.013953 
_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]   0.003236 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . MET A 1 1   ? 20.964  -3.135  94.386  1.00 56.60  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 1   ? 19.808  -2.444  95.025  1.00 55.91  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 1   ? 18.795  -2.022  93.961  1.00 55.44  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 1   ? 17.605  -2.293  94.101  1.00 55.74  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 1   ? 20.284  -1.224  95.816  1.00 56.34  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 1   ? 19.286  -0.697  96.847  1.00 56.94  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 1   ? 19.105  -1.692  98.350  1.00 59.44  ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 1   ? 20.810  -2.102  98.761  1.00 57.13  ? 1   MET A CE  1 
ATOM   9    N N   . ALA A 1 2   ? 19.269  -1.368  92.901  1.00 54.85  ? 2   ALA A N   1 
ATOM   10   C CA  . ALA A 1 2   ? 18.386  -0.874  91.840  1.00 53.93  ? 2   ALA A CA  1 
ATOM   11   C C   . ALA A 1 2   ? 17.755  -2.067  91.142  1.00 53.16  ? 2   ALA A C   1 
ATOM   12   O O   . ALA A 1 2   ? 18.439  -3.030  90.799  1.00 53.03  ? 2   ALA A O   1 
ATOM   13   C CB  . ALA A 1 2   ? 19.151  -0.012  90.853  1.00 54.14  ? 2   ALA A CB  1 
ATOM   14   N N   . GLU A 1 3   ? 16.441  -2.028  90.971  1.00 52.09  ? 3   GLU A N   1 
ATOM   15   C CA  . GLU A 1 3   ? 15.748  -3.141  90.328  1.00 51.58  ? 3   GLU A CA  1 
ATOM   16   C C   . GLU A 1 3   ? 15.443  -2.851  88.877  1.00 50.27  ? 3   GLU A C   1 
ATOM   17   O O   . GLU A 1 3   ? 15.351  -1.697  88.481  1.00 49.15  ? 3   GLU A O   1 
ATOM   18   C CB  . GLU A 1 3   ? 14.470  -3.490  91.065  1.00 51.81  ? 3   GLU A CB  1 
ATOM   19   C CG  . GLU A 1 3   ? 14.649  -4.666  92.007  1.00 52.18  ? 3   GLU A CG  1 
ATOM   20   C CD  . GLU A 1 3   ? 13.432  -4.897  92.856  1.00 52.16  ? 3   GLU A CD  1 
ATOM   21   O OE1 . GLU A 1 3   ? 12.972  -3.905  93.475  1.00 53.41  ? 3   GLU A OE1 1 
ATOM   22   O OE2 . GLU A 1 3   ? 12.943  -6.056  92.900  1.00 50.85  ? 3   GLU A OE2 1 
ATOM   23   N N   . GLU A 1 4   ? 15.278  -3.920  88.105  1.00 49.45  ? 4   GLU A N   1 
ATOM   24   C CA  . GLU A 1 4   ? 15.113  -3.814  86.667  1.00 49.21  ? 4   GLU A CA  1 
ATOM   25   C C   . GLU A 1 4   ? 13.824  -3.079  86.293  1.00 47.34  ? 4   GLU A C   1 
ATOM   26   O O   . GLU A 1 4   ? 12.815  -3.111  87.021  1.00 46.51  ? 4   GLU A O   1 
ATOM   27   C CB  . GLU A 1 4   ? 15.133  -5.197  86.016  1.00 49.86  ? 4   GLU A CB  1 
ATOM   28   C CG  . GLU A 1 4   ? 16.410  -5.986  86.255  1.00 51.74  ? 4   GLU A CG  1 
ATOM   29   C CD  . GLU A 1 4   ? 16.286  -7.394  85.725  1.00 52.46  ? 4   GLU A CD  1 
ATOM   30   O OE1 . GLU A 1 4   ? 16.038  -8.309  86.540  1.00 56.47  ? 4   GLU A OE1 1 
ATOM   31   O OE2 . GLU A 1 4   ? 16.397  -7.573  84.491  1.00 56.93  ? 4   GLU A OE2 1 
ATOM   32   N N   . LEU A 1 5   ? 13.889  -2.402  85.157  1.00 45.60  ? 5   LEU A N   1 
ATOM   33   C CA  . LEU A 1 5   ? 12.752  -1.658  84.637  1.00 44.22  ? 5   LEU A CA  1 
ATOM   34   C C   . LEU A 1 5   ? 11.674  -2.624  84.154  1.00 42.88  ? 5   LEU A C   1 
ATOM   35   O O   . LEU A 1 5   ? 11.952  -3.760  83.802  1.00 41.94  ? 5   LEU A O   1 
ATOM   36   C CB  . LEU A 1 5   ? 13.179  -0.746  83.500  1.00 43.74  ? 5   LEU A CB  1 
ATOM   37   C CG  . LEU A 1 5   ? 14.103  0.416   83.854  1.00 42.09  ? 5   LEU A CG  1 
ATOM   38   C CD1 . LEU A 1 5   ? 14.741  1.024   82.587  1.00 41.37  ? 5   LEU A CD1 1 
ATOM   39   C CD2 . LEU A 1 5   ? 13.354  1.459   84.614  1.00 41.00  ? 5   LEU A CD2 1 
ATOM   40   N N   . VAL A 1 6   ? 10.436  -2.163  84.181  1.00 41.87  ? 6   VAL A N   1 
ATOM   41   C CA  . VAL A 1 6   ? 9.316   -2.943  83.695  1.00 41.41  ? 6   VAL A CA  1 
ATOM   42   C C   . VAL A 1 6   ? 8.614   -2.039  82.699  1.00 40.56  ? 6   VAL A C   1 
ATOM   43   O O   . VAL A 1 6   ? 8.149   -0.966  83.043  1.00 40.93  ? 6   VAL A O   1 
ATOM   44   C CB  . VAL A 1 6   ? 8.379   -3.378  84.833  1.00 41.03  ? 6   VAL A CB  1 
ATOM   45   C CG1 . VAL A 1 6   ? 7.173   -4.123  84.290  1.00 40.89  ? 6   VAL A CG1 1 
ATOM   46   C CG2 . VAL A 1 6   ? 9.143   -4.254  85.865  1.00 41.06  ? 6   VAL A CG2 1 
ATOM   47   N N   . LEU A 1 7   ? 8.583   -2.467  81.447  1.00 40.37  ? 7   LEU A N   1 
ATOM   48   C CA  . LEU A 1 7   ? 7.880   -1.745  80.420  1.00 40.41  ? 7   LEU A CA  1 
ATOM   49   C C   . LEU A 1 7   ? 6.399   -1.998  80.569  1.00 39.65  ? 7   LEU A C   1 
ATOM   50   O O   . LEU A 1 7   ? 5.952   -3.139  80.685  1.00 38.37  ? 7   LEU A O   1 
ATOM   51   C CB  . LEU A 1 7   ? 8.353   -2.199  79.047  1.00 40.81  ? 7   LEU A CB  1 
ATOM   52   C CG  . LEU A 1 7   ? 7.809   -1.384  77.875  1.00 40.84  ? 7   LEU A CG  1 
ATOM   53   C CD1 . LEU A 1 7   ? 8.500   -0.027  77.822  1.00 41.93  ? 7   LEU A CD1 1 
ATOM   54   C CD2 . LEU A 1 7   ? 8.035   -2.167  76.627  1.00 42.53  ? 7   LEU A CD2 1 
ATOM   55   N N   . GLU A 1 8   ? 5.642   -0.919  80.605  1.00 40.00  ? 8   GLU A N   1 
ATOM   56   C CA  . GLU A 1 8   ? 4.210   -1.008  80.568  1.00 41.03  ? 8   GLU A CA  1 
ATOM   57   C C   . GLU A 1 8   ? 3.771   -1.157  79.102  1.00 40.62  ? 8   GLU A C   1 
ATOM   58   O O   . GLU A 1 8   ? 3.054   -2.105  78.735  1.00 39.06  ? 8   GLU A O   1 
ATOM   59   C CB  . GLU A 1 8   ? 3.618   0.245   81.159  1.00 41.63  ? 8   GLU A CB  1 
ATOM   60   C CG  . GLU A 1 8   ? 2.153   0.119   81.481  1.00 43.95  ? 8   GLU A CG  1 
ATOM   61   C CD  . GLU A 1 8   ? 1.457   1.414   81.238  1.00 49.76  ? 8   GLU A CD  1 
ATOM   62   O OE1 . GLU A 1 8   ? 2.013   2.454   81.663  1.00 52.75  ? 8   GLU A OE1 1 
ATOM   63   O OE2 . GLU A 1 8   ? 0.377   1.399   80.597  1.00 55.27  ? 8   GLU A OE2 1 
ATOM   64   N N   . ARG A 1 9   ? 4.236   -0.228  78.272  1.00 41.52  ? 9   ARG A N   1 
ATOM   65   C CA  . ARG A 1 9   ? 3.894   -0.231  76.862  1.00 42.70  ? 9   ARG A CA  1 
ATOM   66   C C   . ARG A 1 9   ? 4.787   0.658   76.041  1.00 42.98  ? 9   ARG A C   1 
ATOM   67   O O   . ARG A 1 9   ? 5.378   1.627   76.554  1.00 42.48  ? 9   ARG A O   1 
ATOM   68   C CB  . ARG A 1 9   ? 2.452   0.228   76.680  1.00 42.76  ? 9   ARG A CB  1 
ATOM   69   C CG  . ARG A 1 9   ? 2.225   1.701   76.902  1.00 43.61  ? 9   ARG A CG  1 
ATOM   70   C CD  . ARG A 1 9   ? 0.760   2.006   76.693  1.00 45.45  ? 9   ARG A CD  1 
ATOM   71   N NE  . ARG A 1 9   ? 0.419   3.399   76.980  1.00 48.27  ? 9   ARG A NE  1 
ATOM   72   C CZ  . ARG A 1 9   ? 0.384   4.391   76.092  1.00 48.70  ? 9   ARG A CZ  1 
ATOM   73   N NH1 . ARG A 1 9   ? 0.662   4.184   74.812  1.00 50.75  ? 9   ARG A NH1 1 
ATOM   74   N NH2 . ARG A 1 9   ? 0.052   5.616   76.496  1.00 49.90  ? 9   ARG A NH2 1 
ATOM   75   N N   . CYS A 1 10  ? 4.832   0.356   74.743  1.00 43.50  ? 10  CYS A N   1 
ATOM   76   C CA  . CYS A 1 10  ? 5.578   1.148   73.762  1.00 43.53  ? 10  CYS A CA  1 
ATOM   77   C C   . CYS A 1 10  ? 4.573   1.805   72.781  1.00 43.66  ? 10  CYS A C   1 
ATOM   78   O O   . CYS A 1 10  ? 3.698   1.128   72.230  1.00 43.07  ? 10  CYS A O   1 
ATOM   79   C CB  . CYS A 1 10  ? 6.596   0.266   73.008  1.00 43.29  ? 10  CYS A CB  1 
ATOM   80   S SG  . CYS A 1 10  ? 7.548   1.158   71.734  1.00 47.28  ? 10  CYS A SG  1 
ATOM   81   N N   . ASP A 1 11  ? 4.686   3.123   72.621  1.00 42.56  ? 11  ASP A N   1 
ATOM   82   C CA  . ASP A 1 11  ? 3.831   3.891   71.752  1.00 43.14  ? 11  ASP A CA  1 
ATOM   83   C C   . ASP A 1 11  ? 4.601   4.071   70.445  1.00 43.16  ? 11  ASP A C   1 
ATOM   84   O O   . ASP A 1 11  ? 5.661   4.700   70.415  1.00 41.92  ? 11  ASP A O   1 
ATOM   85   C CB  . ASP A 1 11  ? 3.537   5.259   72.363  1.00 42.70  ? 11  ASP A CB  1 
ATOM   86   C CG  . ASP A 1 11  ? 2.497   6.056   71.576  1.00 43.93  ? 11  ASP A CG  1 
ATOM   87   O OD1 . ASP A 1 11  ? 2.383   5.926   70.331  1.00 43.67  ? 11  ASP A OD1 1 
ATOM   88   O OD2 . ASP A 1 11  ? 1.789   6.853   72.209  1.00 46.29  ? 11  ASP A OD2 1 
ATOM   89   N N   . LEU A 1 12  ? 4.055   3.498   69.377  1.00 44.21  ? 12  LEU A N   1 
ATOM   90   C CA  . LEU A 1 12  ? 4.669   3.507   68.038  1.00 44.04  ? 12  LEU A CA  1 
ATOM   91   C C   . LEU A 1 12  ? 4.589   4.864   67.322  1.00 44.94  ? 12  LEU A C   1 
ATOM   92   O O   . LEU A 1 12  ? 5.150   5.035   66.189  1.00 45.53  ? 12  LEU A O   1 
ATOM   93   C CB  . LEU A 1 12  ? 3.988   2.423   67.172  1.00 44.97  ? 12  LEU A CB  1 
ATOM   94   C CG  . LEU A 1 12  ? 4.123   0.983   67.655  1.00 45.73  ? 12  LEU A CG  1 
ATOM   95   C CD1 . LEU A 1 12  ? 3.088   0.048   66.932  1.00 46.98  ? 12  LEU A CD1 1 
ATOM   96   C CD2 . LEU A 1 12  ? 5.595   0.507   67.545  1.00 47.50  ? 12  LEU A CD2 1 
ATOM   97   N N   . GLU A 1 13  ? 3.890   5.821   67.949  1.00 44.13  ? 13  GLU A N   1 
ATOM   98   C CA  . GLU A 1 13  ? 3.829   7.205   67.490  1.00 44.53  ? 13  GLU A CA  1 
ATOM   99   C C   . GLU A 1 13  ? 3.423   7.252   66.006  1.00 44.89  ? 13  GLU A C   1 
ATOM   100  O O   . GLU A 1 13  ? 4.059   7.917   65.186  1.00 45.00  ? 13  GLU A O   1 
ATOM   101  C CB  . GLU A 1 13  ? 5.164   7.914   67.729  1.00 43.84  ? 13  GLU A CB  1 
ATOM   102  C CG  . GLU A 1 13  ? 5.622   7.959   69.230  1.00 44.83  ? 13  GLU A CG  1 
ATOM   103  C CD  . GLU A 1 13  ? 4.882   9.006   70.034  1.00 47.46  ? 13  GLU A CD  1 
ATOM   104  O OE1 . GLU A 1 13  ? 4.106   9.776   69.434  1.00 45.75  ? 13  GLU A OE1 1 
ATOM   105  O OE2 . GLU A 1 13  ? 5.058   9.058   71.283  1.00 50.21  ? 13  GLU A OE2 1 
ATOM   106  N N   . LEU A 1 14  ? 2.354   6.544   65.679  1.00 45.09  ? 14  LEU A N   1 
ATOM   107  C CA  . LEU A 1 14  ? 1.982   6.358   64.269  1.00 45.72  ? 14  LEU A CA  1 
ATOM   108  C C   . LEU A 1 14  ? 1.683   7.666   63.582  1.00 46.09  ? 14  LEU A C   1 
ATOM   109  O O   . LEU A 1 14  ? 2.011   7.836   62.403  1.00 46.24  ? 14  LEU A O   1 
ATOM   110  C CB  . LEU A 1 14  ? 0.779   5.443   64.163  1.00 45.48  ? 14  LEU A CB  1 
ATOM   111  C CG  . LEU A 1 14  ? 1.030   4.034   64.639  1.00 44.56  ? 14  LEU A CG  1 
ATOM   112  C CD1 . LEU A 1 14  ? -0.217  3.240   64.495  1.00 43.59  ? 14  LEU A CD1 1 
ATOM   113  C CD2 . LEU A 1 14  ? 2.178   3.404   63.894  1.00 44.36  ? 14  LEU A CD2 1 
ATOM   114  N N   . GLU A 1 15  ? 1.078   8.605   64.323  1.00 47.20  ? 15  GLU A N   1 
ATOM   115  C CA  . GLU A 1 15  ? 0.645   9.858   63.737  1.00 47.88  ? 15  GLU A CA  1 
ATOM   116  C C   . GLU A 1 15  ? 1.796   10.764  63.306  1.00 48.32  ? 15  GLU A C   1 
ATOM   117  O O   . GLU A 1 15  ? 1.820   11.252  62.160  1.00 47.81  ? 15  GLU A O   1 
ATOM   118  C CB  . GLU A 1 15  ? -0.283  10.620  64.671  1.00 48.68  ? 15  GLU A CB  1 
ATOM   119  C CG  . GLU A 1 15  ? -1.173  11.582  63.919  1.00 50.11  ? 15  GLU A CG  1 
ATOM   120  C CD  . GLU A 1 15  ? -1.836  12.583  64.819  1.00 51.64  ? 15  GLU A CD  1 
ATOM   121  O OE1 . GLU A 1 15  ? -2.408  12.177  65.856  1.00 56.68  ? 15  GLU A OE1 1 
ATOM   122  O OE2 . GLU A 1 15  ? -1.796  13.788  64.477  1.00 58.28  ? 15  GLU A OE2 1 
ATOM   123  N N   . THR A 1 16  ? 2.750   10.992  64.203  1.00 47.49  ? 16  THR A N   1 
ATOM   124  C CA  . THR A 1 16  ? 3.885   11.860  63.877  1.00 47.63  ? 16  THR A CA  1 
ATOM   125  C C   . THR A 1 16  ? 4.838   11.130  62.932  1.00 47.21  ? 16  THR A C   1 
ATOM   126  O O   . THR A 1 16  ? 5.375   11.726  61.991  1.00 46.72  ? 16  THR A O   1 
ATOM   127  C CB  . THR A 1 16  ? 4.626   12.378  65.148  1.00 48.06  ? 16  THR A CB  1 
ATOM   128  O OG1 . THR A 1 16  ? 5.318   11.299  65.764  1.00 52.65  ? 16  THR A OG1 1 
ATOM   129  C CG2 . THR A 1 16  ? 3.628   12.942  66.140  1.00 46.74  ? 16  THR A CG2 1 
ATOM   130  N N   . ASN A 1 17  ? 5.050   9.849   63.170  1.00 46.15  ? 17  ASN A N   1 
ATOM   131  C CA  . ASN A 1 17  ? 5.884   9.069   62.279  1.00 46.76  ? 17  ASN A CA  1 
ATOM   132  C C   . ASN A 1 17  ? 5.301   9.036   60.839  1.00 46.60  ? 17  ASN A C   1 
ATOM   133  O O   . ASN A 1 17  ? 6.022   9.269   59.897  1.00 47.15  ? 17  ASN A O   1 
ATOM   134  C CB  . ASN A 1 17  ? 6.111   7.653   62.801  1.00 46.04  ? 17  ASN A CB  1 
ATOM   135  C CG  . ASN A 1 17  ? 7.118   7.595   63.950  1.00 45.58  ? 17  ASN A CG  1 
ATOM   136  O OD1 . ASN A 1 17  ? 8.052   8.376   63.998  1.00 42.77  ? 17  ASN A OD1 1 
ATOM   137  N ND2 . ASN A 1 17  ? 6.962   6.625   64.831  1.00 39.71  ? 17  ASN A ND2 1 
ATOM   138  N N   . GLY A 1 18  ? 4.013   8.751   60.689  1.00 47.10  ? 18  GLY A N   1 
ATOM   139  C CA  . GLY A 1 18  ? 3.396   8.704   59.358  1.00 47.10  ? 18  GLY A CA  1 
ATOM   140  C C   . GLY A 1 18  ? 3.606   9.986   58.594  1.00 47.75  ? 18  GLY A C   1 
ATOM   141  O O   . GLY A 1 18  ? 4.030   9.991   57.420  1.00 45.83  ? 18  GLY A O   1 
ATOM   142  N N   . ARG A 1 19  ? 3.306   11.087  59.269  1.00 49.02  ? 19  ARG A N   1 
ATOM   143  C CA  . ARG A 1 19  ? 3.424   12.397  58.683  1.00 50.47  ? 19  ARG A CA  1 
ATOM   144  C C   . ARG A 1 19  ? 4.849   12.584  58.238  1.00 51.04  ? 19  ARG A C   1 
ATOM   145  O O   . ARG A 1 19  ? 5.102   12.847  57.062  1.00 52.12  ? 19  ARG A O   1 
ATOM   146  C CB  . ARG A 1 19  ? 3.001   13.497  59.682  1.00 50.59  ? 19  ARG A CB  1 
ATOM   147  C CG  . ARG A 1 19  ? 2.877   14.907  59.075  1.00 51.10  ? 19  ARG A CG  1 
ATOM   148  C CD  . ARG A 1 19  ? 2.045   15.871  59.985  1.00 54.39  ? 19  ARG A CD  1 
ATOM   149  N NE  . ARG A 1 19  ? 2.368   15.651  61.389  1.00 59.46  ? 19  ARG A NE  1 
ATOM   150  C CZ  . ARG A 1 19  ? 1.543   15.153  62.318  1.00 60.42  ? 19  ARG A CZ  1 
ATOM   151  N NH1 . ARG A 1 19  ? 0.262   14.858  62.064  1.00 60.88  ? 19  ARG A NH1 1 
ATOM   152  N NH2 . ARG A 1 19  ? 2.009   14.979  63.543  1.00 61.10  ? 19  ARG A NH2 1 
ATOM   153  N N   . ASP A 1 20  ? 5.796   12.388  59.147  1.00 50.77  ? 20  ASP A N   1 
ATOM   154  C CA  . ASP A 1 20  ? 7.163   12.807  58.865  1.00 51.01  ? 20  ASP A CA  1 
ATOM   155  C C   . ASP A 1 20  ? 7.815   11.915  57.818  1.00 50.28  ? 20  ASP A C   1 
ATOM   156  O O   . ASP A 1 20  ? 8.683   12.369  57.080  1.00 50.95  ? 20  ASP A O   1 
ATOM   157  C CB  . ASP A 1 20  ? 8.010   12.819  60.133  1.00 51.53  ? 20  ASP A CB  1 
ATOM   158  C CG  . ASP A 1 20  ? 7.832   14.093  60.952  1.00 54.65  ? 20  ASP A CG  1 
ATOM   159  O OD1 . ASP A 1 20  ? 6.765   14.761  60.891  1.00 58.55  ? 20  ASP A OD1 1 
ATOM   160  O OD2 . ASP A 1 20  ? 8.791   14.428  61.672  1.00 60.35  ? 20  ASP A OD2 1 
ATOM   161  N N   . HIS A 1 21  ? 7.385   10.661  57.753  1.00 49.65  ? 21  HIS A N   1 
ATOM   162  C CA  . HIS A 1 21  ? 7.960   9.691   56.820  1.00 49.41  ? 21  HIS A CA  1 
ATOM   163  C C   . HIS A 1 21  ? 7.173   9.582   55.505  1.00 49.49  ? 21  HIS A C   1 
ATOM   164  O O   . HIS A 1 21  ? 7.493   8.750   54.660  1.00 50.10  ? 21  HIS A O   1 
ATOM   165  C CB  . HIS A 1 21  ? 8.104   8.338   57.508  1.00 49.04  ? 21  HIS A CB  1 
ATOM   166  C CG  . HIS A 1 21  ? 9.262   8.315   58.448  1.00 49.03  ? 21  HIS A CG  1 
ATOM   167  N ND1 . HIS A 1 21  ? 10.428  7.650   58.167  1.00 47.01  ? 21  HIS A ND1 1 
ATOM   168  C CD2 . HIS A 1 21  ? 9.493   9.013   59.585  1.00 47.31  ? 21  HIS A CD2 1 
ATOM   169  C CE1 . HIS A 1 21  ? 11.310  7.883   59.116  1.00 46.69  ? 21  HIS A CE1 1 
ATOM   170  N NE2 . HIS A 1 21  ? 10.771  8.714   59.987  1.00 46.43  ? 21  HIS A NE2 1 
ATOM   171  N N   . HIS A 1 22  ? 6.152   10.400  55.351  1.00 48.01  ? 22  HIS A N   1 
ATOM   172  C CA  . HIS A 1 22  ? 5.303   10.349  54.171  1.00 48.28  ? 22  HIS A CA  1 
ATOM   173  C C   . HIS A 1 22  ? 4.704   8.954   54.007  1.00 48.63  ? 22  HIS A C   1 
ATOM   174  O O   . HIS A 1 22  ? 4.635   8.436   52.900  1.00 48.61  ? 22  HIS A O   1 
ATOM   175  C CB  . HIS A 1 22  ? 6.119   10.761  52.948  1.00 46.98  ? 22  HIS A CB  1 
ATOM   176  C CG  . HIS A 1 22  ? 6.907   12.013  53.164  1.00 45.33  ? 22  HIS A CG  1 
ATOM   177  N ND1 . HIS A 1 22  ? 8.228   12.001  53.563  1.00 44.49  ? 22  HIS A ND1 1 
ATOM   178  C CD2 . HIS A 1 22  ? 6.549   13.311  53.088  1.00 43.54  ? 22  HIS A CD2 1 
ATOM   179  C CE1 . HIS A 1 22  ? 8.653   13.242  53.702  1.00 43.75  ? 22  HIS A CE1 1 
ATOM   180  N NE2 . HIS A 1 22  ? 7.651   14.058  53.424  1.00 43.43  ? 22  HIS A NE2 1 
ATOM   181  N N   . THR A 1 23  ? 4.275   8.350   55.123  1.00 49.11  ? 23  THR A N   1 
ATOM   182  C CA  . THR A 1 23  ? 3.767   6.977   55.150  1.00 49.27  ? 23  THR A CA  1 
ATOM   183  C C   . THR A 1 23  ? 2.413   6.924   55.879  1.00 49.26  ? 23  THR A C   1 
ATOM   184  O O   . THR A 1 23  ? 2.001   5.881   56.356  1.00 48.94  ? 23  THR A O   1 
ATOM   185  C CB  . THR A 1 23  ? 4.769   5.985   55.870  1.00 50.00  ? 23  THR A CB  1 
ATOM   186  O OG1 . THR A 1 23  ? 5.098   6.499   57.172  1.00 51.72  ? 23  THR A OG1 1 
ATOM   187  C CG2 . THR A 1 23  ? 6.060   5.817   55.110  1.00 49.85  ? 23  THR A CG2 1 
ATOM   188  N N   . ALA A 1 24  ? 1.730   8.058   55.979  1.00 49.28  ? 24  ALA A N   1 
ATOM   189  C CA  . ALA A 1 24  ? 0.535   8.166   56.817  1.00 49.75  ? 24  ALA A CA  1 
ATOM   190  C C   . ALA A 1 24  ? -0.587  7.223   56.425  1.00 50.10  ? 24  ALA A C   1 
ATOM   191  O O   . ALA A 1 24  ? -1.238  6.646   57.286  1.00 50.21  ? 24  ALA A O   1 
ATOM   192  C CB  . ALA A 1 24  ? 0.031   9.618   56.831  1.00 49.74  ? 24  ALA A CB  1 
ATOM   193  N N   . ASP A 1 25  ? -0.810  7.050   55.123  1.00 50.41  ? 25  ASP A N   1 
ATOM   194  C CA  . ASP A 1 25  ? -1.859  6.141   54.630  1.00 49.88  ? 25  ASP A CA  1 
ATOM   195  C C   . ASP A 1 25  ? -1.526  4.695   54.971  1.00 49.41  ? 25  ASP A C   1 
ATOM   196  O O   . ASP A 1 25  ? -2.412  3.854   55.103  1.00 49.83  ? 25  ASP A O   1 
ATOM   197  C CB  . ASP A 1 25  ? -2.027  6.285   53.113  1.00 50.73  ? 25  ASP A CB  1 
ATOM   198  C CG  . ASP A 1 25  ? -2.529  7.650   52.708  1.00 50.59  ? 25  ASP A CG  1 
ATOM   199  O OD1 . ASP A 1 25  ? -1.823  8.324   51.944  1.00 59.58  ? 25  ASP A OD1 1 
ATOM   200  O OD2 . ASP A 1 25  ? -3.598  8.069   53.155  1.00 53.81  ? 25  ASP A OD2 1 
ATOM   201  N N   . LEU A 1 26  ? -0.245  4.415   55.128  1.00 48.99  ? 26  LEU A N   1 
ATOM   202  C CA  . LEU A 1 26  ? 0.210   3.089   55.485  1.00 49.43  ? 26  LEU A CA  1 
ATOM   203  C C   . LEU A 1 26  ? 0.286   2.835   57.022  1.00 49.62  ? 26  LEU A C   1 
ATOM   204  O O   . LEU A 1 26  ? 0.470   1.686   57.424  1.00 50.07  ? 26  LEU A O   1 
ATOM   205  C CB  . LEU A 1 26  ? 1.583   2.848   54.869  1.00 48.57  ? 26  LEU A CB  1 
ATOM   206  C CG  . LEU A 1 26  ? 1.638   2.814   53.341  1.00 46.92  ? 26  LEU A CG  1 
ATOM   207  C CD1 . LEU A 1 26  ? 3.068   2.966   52.890  1.00 45.47  ? 26  LEU A CD1 1 
ATOM   208  C CD2 . LEU A 1 26  ? 1.007   1.523   52.817  1.00 42.79  ? 26  LEU A CD2 1 
ATOM   209  N N   . CYS A 1 27  ? 0.140   3.883   57.840  1.00 49.63  ? 27  CYS A N   1 
ATOM   210  C CA  . CYS A 1 27  ? 0.300   3.798   59.327  1.00 50.00  ? 27  CYS A CA  1 
ATOM   211  C C   . CYS A 1 27  ? -0.979  3.892   60.133  1.00 50.83  ? 27  CYS A C   1 
ATOM   212  O O   . CYS A 1 27  ? -0.936  4.327   61.278  1.00 51.34  ? 27  CYS A O   1 
ATOM   213  C CB  . CYS A 1 27  ? 1.170   4.940   59.843  1.00 48.25  ? 27  CYS A CB  1 
ATOM   214  S SG  . CYS A 1 27  ? 2.845   4.809   59.475  1.00 46.13  ? 27  CYS A SG  1 
ATOM   215  N N   . ARG A 1 28  ? -2.115  3.513   59.570  1.00 52.32  ? 28  ARG A N   1 
ATOM   216  C CA  . ARG A 1 28  ? -3.360  3.583   60.320  1.00 52.86  ? 28  ARG A CA  1 
ATOM   217  C C   . ARG A 1 28  ? -3.343  2.636   61.516  1.00 53.83  ? 28  ARG A C   1 
ATOM   218  O O   . ARG A 1 28  ? -3.926  2.957   62.556  1.00 53.95  ? 28  ARG A O   1 
ATOM   219  C CB  . ARG A 1 28  ? -4.587  3.280   59.447  1.00 53.34  ? 28  ARG A CB  1 
ATOM   220  C CG  . ARG A 1 28  ? -4.821  4.264   58.309  1.00 54.08  ? 28  ARG A CG  1 
ATOM   221  C CD  . ARG A 1 28  ? -6.195  3.776   57.637  0.00 50.00  ? 28  ARG A CD  1 
ATOM   222  N NE  . ARG A 1 28  ? -7.383  3.541   58.468  0.00 50.00  ? 28  ARG A NE  1 
ATOM   223  C CZ  . ARG A 1 28  ? -8.571  3.168   57.981  0.00 50.00  ? 28  ARG A CZ  1 
ATOM   224  N NH1 . ARG A 1 28  ? -8.732  2.980   56.673  0.00 50.00  ? 28  ARG A NH1 1 
ATOM   225  N NH2 . ARG A 1 28  ? -9.601  2.978   58.804  0.00 50.00  ? 28  ARG A NH2 1 
ATOM   226  N N   . GLU A 1 29  ? -2.643  1.519   61.399  1.00 54.00  ? 29  GLU A N   1 
ATOM   227  C CA  . GLU A 1 29  ? -2.556  0.566   62.476  1.00 53.98  ? 29  GLU A CA  1 
ATOM   228  C C   . GLU A 1 29  ? -1.178  0.073   62.837  1.00 54.06  ? 29  GLU A C   1 
ATOM   229  O O   . GLU A 1 29  ? -0.930  -0.257  63.953  1.00 55.42  ? 29  GLU A O   1 
ATOM   230  C CB  . GLU A 1 29  ? -3.423  -0.613  62.155  1.00 54.56  ? 29  GLU A CB  1 
ATOM   231  C CG  . GLU A 1 29  ? -4.853  -0.224  62.053  1.00 54.78  ? 29  GLU A CG  1 
ATOM   232  C CD  . GLU A 1 29  ? -5.674  -1.329  61.514  1.00 54.58  ? 29  GLU A CD  1 
ATOM   233  O OE1 . GLU A 1 29  ? -6.167  -1.217  60.358  0.00 50.00  ? 29  GLU A OE1 1 
ATOM   234  O OE2 . GLU A 1 29  ? -5.819  -2.317  62.252  0.00 50.00  ? 29  GLU A OE2 1 
ATOM   235  N N   . LYS A 1 30  ? -0.301  -0.013  61.864  1.00 53.11  ? 30  LYS A N   1 
ATOM   236  C CA  . LYS A 1 30  ? 1.040   -0.547  62.058  1.00 52.30  ? 30  LYS A CA  1 
ATOM   237  C C   . LYS A 1 30  ? 2.036   0.526   61.694  1.00 50.95  ? 30  LYS A C   1 
ATOM   238  O O   . LYS A 1 30  ? 1.673   1.478   61.031  1.00 51.25  ? 30  LYS A O   1 
ATOM   239  C CB  . LYS A 1 30  ? 1.253   -1.766  61.167  1.00 52.36  ? 30  LYS A CB  1 
ATOM   240  C CG  . LYS A 1 30  ? 0.328   -2.903  61.488  1.00 54.30  ? 30  LYS A CG  1 
ATOM   241  C CD  . LYS A 1 30  ? 0.679   -4.153  60.698  1.00 54.29  ? 30  LYS A CD  1 
ATOM   242  C CE  . LYS A 1 30  ? -0.466  -5.094  60.159  0.00 50.00  ? 30  LYS A CE  1 
ATOM   243  N NZ  . LYS A 1 30  ? -0.051  -6.319  59.398  0.00 50.00  ? 30  LYS A NZ  1 
ATOM   244  N N   . LEU A 1 31  ? 3.281   0.398   62.151  1.00 48.85  ? 31  LEU A N   1 
ATOM   245  C CA  . LEU A 1 31  ? 4.295   1.428   61.912  1.00 48.30  ? 31  LEU A CA  1 
ATOM   246  C C   . LEU A 1 31  ? 5.065   1.175   60.597  1.00 47.65  ? 31  LEU A C   1 
ATOM   247  O O   . LEU A 1 31  ? 5.693   0.124   60.432  1.00 46.77  ? 31  LEU A O   1 
ATOM   248  C CB  . LEU A 1 31  ? 5.306   1.462   63.066  1.00 47.51  ? 31  LEU A CB  1 
ATOM   249  C CG  . LEU A 1 31  ? 6.426   2.486   62.990  1.00 47.68  ? 31  LEU A CG  1 
ATOM   250  C CD1 . LEU A 1 31  ? 5.849   3.885   62.829  1.00 41.32  ? 31  LEU A CD1 1 
ATOM   251  C CD2 . LEU A 1 31  ? 7.297   2.416   64.265  1.00 48.66  ? 31  LEU A CD2 1 
ATOM   252  N N   . VAL A 1 32  ? 5.052   2.169   59.714  1.00 46.86  ? 32  VAL A N   1 
ATOM   253  C CA  . VAL A 1 32  ? 5.786   2.127   58.440  1.00 46.45  ? 32  VAL A CA  1 
ATOM   254  C C   . VAL A 1 32  ? 6.580   3.392   58.319  1.00 45.27  ? 32  VAL A C   1 
ATOM   255  O O   . VAL A 1 32  ? 6.044   4.499   58.433  1.00 47.42  ? 32  VAL A O   1 
ATOM   256  C CB  . VAL A 1 32  ? 4.826   1.965   57.221  1.00 46.47  ? 32  VAL A CB  1 
ATOM   257  C CG1 . VAL A 1 32  ? 5.632   1.886   55.886  1.00 45.27  ? 32  VAL A CG1 1 
ATOM   258  C CG2 . VAL A 1 32  ? 3.945   0.736   57.417  1.00 44.42  ? 32  VAL A CG2 1 
ATOM   259  N N   . VAL A 1 33  ? 7.887   3.243   58.127  1.00 46.03  ? 33  VAL A N   1 
ATOM   260  C CA  . VAL A 1 33  ? 8.786   4.369   58.104  1.00 45.58  ? 33  VAL A CA  1 
ATOM   261  C C   . VAL A 1 33  ? 9.817   4.181   56.992  1.00 46.13  ? 33  VAL A C   1 
ATOM   262  O O   . VAL A 1 33  ? 9.946   3.115   56.446  1.00 46.44  ? 33  VAL A O   1 
ATOM   263  C CB  . VAL A 1 33  ? 9.571   4.486   59.453  1.00 45.46  ? 33  VAL A CB  1 
ATOM   264  C CG1 . VAL A 1 33  ? 8.642   4.885   60.619  1.00 44.67  ? 33  VAL A CG1 1 
ATOM   265  C CG2 . VAL A 1 33  ? 10.282  3.149   59.754  1.00 46.86  ? 33  VAL A CG2 1 
ATOM   266  N N   . ARG A 1 34  ? 10.593  5.209   56.709  1.00 46.33  ? 34  ARG A N   1 
ATOM   267  C CA  . ARG A 1 34  ? 11.520  5.188   55.577  1.00 47.08  ? 34  ARG A CA  1 
ATOM   268  C C   . ARG A 1 34  ? 12.934  5.323   56.096  1.00 48.40  ? 34  ARG A C   1 
ATOM   269  O O   . ARG A 1 34  ? 13.186  5.954   57.156  1.00 47.83  ? 34  ARG A O   1 
ATOM   270  C CB  . ARG A 1 34  ? 11.177  6.304   54.571  1.00 46.57  ? 34  ARG A CB  1 
ATOM   271  C CG  . ARG A 1 34  ? 9.778   6.164   53.982  1.00 47.60  ? 34  ARG A CG  1 
ATOM   272  C CD  . ARG A 1 34  ? 9.460   7.226   52.922  1.00 46.70  ? 34  ARG A CD  1 
ATOM   273  N NE  . ARG A 1 34  ? 8.054   7.219   52.494  1.00 45.03  ? 34  ARG A NE  1 
ATOM   274  C CZ  . ARG A 1 34  ? 7.541   6.366   51.620  1.00 47.75  ? 34  ARG A CZ  1 
ATOM   275  N NH1 . ARG A 1 34  ? 8.300   5.415   51.074  1.00 50.37  ? 34  ARG A NH1 1 
ATOM   276  N NH2 . ARG A 1 34  ? 6.247   6.452   51.324  1.00 49.49  ? 34  ARG A NH2 1 
ATOM   277  N N   . ARG A 1 35  ? 13.863  4.703   55.382  1.00 48.32  ? 35  ARG A N   1 
ATOM   278  C CA  . ARG A 1 35  ? 15.228  4.574   55.879  1.00 47.88  ? 35  ARG A CA  1 
ATOM   279  C C   . ARG A 1 35  ? 16.007  5.893   55.821  1.00 48.46  ? 35  ARG A C   1 
ATOM   280  O O   . ARG A 1 35  ? 15.652  6.829   55.078  1.00 48.87  ? 35  ARG A O   1 
ATOM   281  C CB  . ARG A 1 35  ? 15.913  3.435   55.111  1.00 48.88  ? 35  ARG A CB  1 
ATOM   282  C CG  . ARG A 1 35  ? 16.006  3.690   53.617  1.00 47.85  ? 35  ARG A CG  1 
ATOM   283  C CD  . ARG A 1 35  ? 16.551  2.502   52.932  1.00 48.75  ? 35  ARG A CD  1 
ATOM   284  N NE  . ARG A 1 35  ? 16.939  2.841   51.572  1.00 48.56  ? 35  ARG A NE  1 
ATOM   285  C CZ  . ARG A 1 35  ? 17.700  2.065   50.809  1.00 47.03  ? 35  ARG A CZ  1 
ATOM   286  N NH1 . ARG A 1 35  ? 18.130  0.919   51.253  1.00 49.23  ? 35  ARG A NH1 1 
ATOM   287  N NH2 . ARG A 1 35  ? 18.037  2.462   49.584  1.00 50.79  ? 35  ARG A NH2 1 
ATOM   288  N N   . GLY A 1 36  ? 17.002  6.010   56.707  1.00 48.25  ? 36  GLY A N   1 
ATOM   289  C CA  . GLY A 1 36  ? 17.914  7.110   56.747  1.00 48.13  ? 36  GLY A CA  1 
ATOM   290  C C   . GLY A 1 36  ? 17.353  8.315   57.464  1.00 48.38  ? 36  GLY A C   1 
ATOM   291  O O   . GLY A 1 36  ? 17.937  9.338   57.402  1.00 49.59  ? 36  GLY A O   1 
ATOM   292  N N   . GLN A 1 37  ? 16.215  8.171   58.140  1.00 48.85  ? 37  GLN A N   1 
ATOM   293  C CA  . GLN A 1 37  ? 15.470  9.309   58.703  1.00 49.07  ? 37  GLN A CA  1 
ATOM   294  C C   . GLN A 1 37  ? 15.008  8.931   60.123  1.00 48.84  ? 37  GLN A C   1 
ATOM   295  O O   . GLN A 1 37  ? 14.472  7.822   60.339  1.00 49.98  ? 37  GLN A O   1 
ATOM   296  C CB  . GLN A 1 37  ? 14.250  9.596   57.863  1.00 48.66  ? 37  GLN A CB  1 
ATOM   297  C CG  . GLN A 1 37  ? 13.394  10.759  58.351  1.00 48.97  ? 37  GLN A CG  1 
ATOM   298  C CD  . GLN A 1 37  ? 12.236  11.037  57.420  1.00 50.68  ? 37  GLN A CD  1 
ATOM   299  O OE1 . GLN A 1 37  ? 12.251  10.605  56.270  1.00 54.51  ? 37  GLN A OE1 1 
ATOM   300  N NE2 . GLN A 1 37  ? 11.219  11.765  57.911  1.00 47.82  ? 37  GLN A NE2 1 
ATOM   301  N N   . PRO A 1 38  ? 15.198  9.837   61.074  1.00 48.46  ? 38  PRO A N   1 
ATOM   302  C CA  . PRO A 1 38  ? 14.755  9.513   62.439  1.00 48.75  ? 38  PRO A CA  1 
ATOM   303  C C   . PRO A 1 38  ? 13.254  9.264   62.553  1.00 48.56  ? 38  PRO A C   1 
ATOM   304  O O   . PRO A 1 38  ? 12.430  9.945   61.917  1.00 48.91  ? 38  PRO A O   1 
ATOM   305  C CB  . PRO A 1 38  ? 15.167  10.737  63.270  1.00 48.49  ? 38  PRO A CB  1 
ATOM   306  C CG  . PRO A 1 38  ? 15.487  11.824  62.305  1.00 49.35  ? 38  PRO A CG  1 
ATOM   307  C CD  . PRO A 1 38  ? 15.789  11.184  60.966  1.00 48.91  ? 38  PRO A CD  1 
ATOM   308  N N   . PHE A 1 39  ? 12.908  8.278   63.357  1.00 48.31  ? 39  PHE A N   1 
ATOM   309  C CA  . PHE A 1 39  ? 11.526  8.088   63.769  1.00 48.33  ? 39  PHE A CA  1 
ATOM   310  C C   . PHE A 1 39  ? 11.462  7.937   65.282  1.00 48.40  ? 39  PHE A C   1 
ATOM   311  O O   . PHE A 1 39  ? 12.501  7.762   65.919  1.00 48.18  ? 39  PHE A O   1 
ATOM   312  C CB  . PHE A 1 39  ? 10.880  6.907   63.047  1.00 47.79  ? 39  PHE A CB  1 
ATOM   313  C CG  . PHE A 1 39  ? 11.463  5.561   63.348  1.00 47.59  ? 39  PHE A CG  1 
ATOM   314  C CD1 . PHE A 1 39  ? 12.581  5.093   62.679  1.00 46.29  ? 39  PHE A CD1 1 
ATOM   315  C CD2 . PHE A 1 39  ? 10.821  4.705   64.224  1.00 48.11  ? 39  PHE A CD2 1 
ATOM   316  C CE1 . PHE A 1 39  ? 13.084  3.826   62.937  1.00 47.26  ? 39  PHE A CE1 1 
ATOM   317  C CE2 . PHE A 1 39  ? 11.317  3.417   64.463  1.00 49.98  ? 39  PHE A CE2 1 
ATOM   318  C CZ  . PHE A 1 39  ? 12.452  2.986   63.809  1.00 49.01  ? 39  PHE A CZ  1 
ATOM   319  N N   . TRP A 1 40  ? 10.256  8.031   65.837  1.00 48.42  ? 40  TRP A N   1 
ATOM   320  C CA  . TRP A 1 40  ? 10.083  8.115   67.297  1.00 47.96  ? 40  TRP A CA  1 
ATOM   321  C C   . TRP A 1 40  ? 9.312   6.930   67.879  1.00 47.59  ? 40  TRP A C   1 
ATOM   322  O O   . TRP A 1 40  ? 8.412   6.387   67.242  1.00 46.36  ? 40  TRP A O   1 
ATOM   323  C CB  . TRP A 1 40  ? 9.471   9.465   67.656  1.00 50.28  ? 40  TRP A CB  1 
ATOM   324  C CG  . TRP A 1 40  ? 10.372  10.514  67.156  1.00 51.81  ? 40  TRP A CG  1 
ATOM   325  C CD1 . TRP A 1 40  ? 11.582  10.860  67.677  1.00 53.96  ? 40  TRP A CD1 1 
ATOM   326  C CD2 . TRP A 1 40  ? 10.222  11.278  65.949  1.00 54.05  ? 40  TRP A CD2 1 
ATOM   327  N NE1 . TRP A 1 40  ? 12.170  11.840  66.906  1.00 53.95  ? 40  TRP A NE1 1 
ATOM   328  C CE2 . TRP A 1 40  ? 11.362  12.104  65.833  1.00 54.39  ? 40  TRP A CE2 1 
ATOM   329  C CE3 . TRP A 1 40  ? 9.208   11.387  64.996  1.00 54.59  ? 40  TRP A CE3 1 
ATOM   330  C CZ2 . TRP A 1 40  ? 11.526  13.015  64.792  1.00 55.19  ? 40  TRP A CZ2 1 
ATOM   331  C CZ3 . TRP A 1 40  ? 9.382   12.271  63.929  1.00 54.51  ? 40  TRP A CZ3 1 
ATOM   332  C CH2 . TRP A 1 40  ? 10.528  13.085  63.847  1.00 54.78  ? 40  TRP A CH2 1 
ATOM   333  N N   . LEU A 1 41  ? 9.711   6.517   69.090  1.00 46.07  ? 41  LEU A N   1 
ATOM   334  C CA  . LEU A 1 41  ? 9.013   5.503   69.872  1.00 45.42  ? 41  LEU A CA  1 
ATOM   335  C C   . LEU A 1 41  ? 9.003   6.060   71.290  1.00 44.42  ? 41  LEU A C   1 
ATOM   336  O O   . LEU A 1 41  ? 10.007  6.655   71.700  1.00 43.16  ? 41  LEU A O   1 
ATOM   337  C CB  . LEU A 1 41  ? 9.798   4.206   69.899  1.00 45.55  ? 41  LEU A CB  1 
ATOM   338  C CG  . LEU A 1 41  ? 10.014  3.474   68.584  1.00 48.42  ? 41  LEU A CG  1 
ATOM   339  C CD1 . LEU A 1 41  ? 10.902  2.243   68.849  1.00 49.96  ? 41  LEU A CD1 1 
ATOM   340  C CD2 . LEU A 1 41  ? 8.678   3.044   67.929  1.00 47.93  ? 41  LEU A CD2 1 
ATOM   341  N N   . THR A 1 42  ? 7.895   5.911   72.011  1.00 43.07  ? 42  THR A N   1 
ATOM   342  C CA  . THR A 1 42  ? 7.803   6.435   73.380  1.00 43.16  ? 42  THR A CA  1 
ATOM   343  C C   . THR A 1 42  ? 7.530   5.296   74.318  1.00 42.62  ? 42  THR A C   1 
ATOM   344  O O   . THR A 1 42  ? 6.511   4.637   74.192  1.00 41.82  ? 42  THR A O   1 
ATOM   345  C CB  . THR A 1 42  ? 6.717   7.502   73.556  1.00 43.08  ? 42  THR A CB  1 
ATOM   346  O OG1 . THR A 1 42  ? 6.995   8.591   72.680  1.00 46.38  ? 42  THR A OG1 1 
ATOM   347  C CG2 . THR A 1 42  ? 6.688   8.016   75.006  1.00 43.01  ? 42  THR A CG2 1 
ATOM   348  N N   . LEU A 1 43  ? 8.471   5.069   75.236  1.00 41.32  ? 43  LEU A N   1 
ATOM   349  C CA  . LEU A 1 43  ? 8.395   3.976   76.196  1.00 41.35  ? 43  LEU A CA  1 
ATOM   350  C C   . LEU A 1 43  ? 7.705   4.500   77.459  1.00 40.19  ? 43  LEU A C   1 
ATOM   351  O O   . LEU A 1 43  ? 7.887   5.650   77.845  1.00 38.99  ? 43  LEU A O   1 
ATOM   352  C CB  . LEU A 1 43  ? 9.794   3.425   76.511  1.00 41.58  ? 43  LEU A CB  1 
ATOM   353  C CG  . LEU A 1 43  ? 10.641  2.833   75.361  1.00 43.03  ? 43  LEU A CG  1 
ATOM   354  C CD1 . LEU A 1 43  ? 11.985  2.269   75.898  1.00 44.00  ? 43  LEU A CD1 1 
ATOM   355  C CD2 . LEU A 1 43  ? 9.880   1.716   74.621  1.00 42.74  ? 43  LEU A CD2 1 
ATOM   356  N N   . HIS A 1 44  ? 6.832   3.668   78.013  1.00 40.23  ? 44  HIS A N   1 
ATOM   357  C CA  . HIS A 1 44  ? 6.126   3.922   79.252  1.00 40.30  ? 44  HIS A CA  1 
ATOM   358  C C   . HIS A 1 44  ? 6.524   2.826   80.214  1.00 40.32  ? 44  HIS A C   1 
ATOM   359  O O   . HIS A 1 44  ? 6.286   1.671   79.931  1.00 40.68  ? 44  HIS A O   1 
ATOM   360  C CB  . HIS A 1 44  ? 4.623   3.836   79.021  1.00 39.66  ? 44  HIS A CB  1 
ATOM   361  C CG  . HIS A 1 44  ? 4.064   4.997   78.279  1.00 38.59  ? 44  HIS A CG  1 
ATOM   362  N ND1 . HIS A 1 44  ? 4.169   5.132   76.907  1.00 40.42  ? 44  HIS A ND1 1 
ATOM   363  C CD2 . HIS A 1 44  ? 3.389   6.081   78.713  1.00 37.35  ? 44  HIS A CD2 1 
ATOM   364  C CE1 . HIS A 1 44  ? 3.583   6.254   76.537  1.00 37.97  ? 44  HIS A CE1 1 
ATOM   365  N NE2 . HIS A 1 44  ? 3.101   6.847   77.614  1.00 40.67  ? 44  HIS A NE2 1 
ATOM   366  N N   . PHE A 1 45  ? 7.138   3.190   81.341  1.00 40.94  ? 45  PHE A N   1 
ATOM   367  C CA  . PHE A 1 45  ? 7.576   2.213   82.328  1.00 40.78  ? 45  PHE A CA  1 
ATOM   368  C C   . PHE A 1 45  ? 6.583   2.148   83.480  1.00 41.00  ? 45  PHE A C   1 
ATOM   369  O O   . PHE A 1 45  ? 5.978   3.159   83.847  1.00 41.26  ? 45  PHE A O   1 
ATOM   370  C CB  . PHE A 1 45  ? 8.986   2.544   82.823  1.00 40.41  ? 45  PHE A CB  1 
ATOM   371  C CG  . PHE A 1 45  ? 10.034  2.424   81.754  1.00 39.72  ? 45  PHE A CG  1 
ATOM   372  C CD1 . PHE A 1 45  ? 10.537  3.542   81.123  1.00 40.69  ? 45  PHE A CD1 1 
ATOM   373  C CD2 . PHE A 1 45  ? 10.501  1.174   81.365  1.00 40.09  ? 45  PHE A CD2 1 
ATOM   374  C CE1 . PHE A 1 45  ? 11.502  3.424   80.120  1.00 39.88  ? 45  PHE A CE1 1 
ATOM   375  C CE2 . PHE A 1 45  ? 11.443  1.044   80.368  1.00 39.87  ? 45  PHE A CE2 1 
ATOM   376  C CZ  . PHE A 1 45  ? 11.967  2.182   79.751  1.00 39.77  ? 45  PHE A CZ  1 
ATOM   377  N N   . GLU A 1 46  ? 6.397   0.939   83.999  1.00 41.44  ? 46  GLU A N   1 
ATOM   378  C CA  . GLU A 1 46  ? 5.590   0.694   85.180  1.00 41.68  ? 46  GLU A CA  1 
ATOM   379  C C   . GLU A 1 46  ? 6.495   0.881   86.390  1.00 41.93  ? 46  GLU A C   1 
ATOM   380  O O   . GLU A 1 46  ? 7.493   0.166   86.551  1.00 41.88  ? 46  GLU A O   1 
ATOM   381  C CB  . GLU A 1 46  ? 5.025   -0.731  85.140  1.00 41.74  ? 46  GLU A CB  1 
ATOM   382  C CG  . GLU A 1 46  ? 3.998   -1.019  86.185  1.00 42.86  ? 46  GLU A CG  1 
ATOM   383  C CD  . GLU A 1 46  ? 2.746   -0.179  86.052  1.00 45.53  ? 46  GLU A CD  1 
ATOM   384  O OE1 . GLU A 1 46  ? 2.411   0.257   84.932  1.00 47.16  ? 46  GLU A OE1 1 
ATOM   385  O OE2 . GLU A 1 46  ? 2.074   0.007   87.088  1.00 50.76  ? 46  GLU A OE2 1 
ATOM   386  N N   . GLY A 1 47  ? 6.143   1.838   87.241  1.00 41.98  ? 47  GLY A N   1 
ATOM   387  C CA  . GLY A 1 47  ? 6.999   2.237   88.345  1.00 41.85  ? 47  GLY A CA  1 
ATOM   388  C C   . GLY A 1 47  ? 8.077   3.227   87.934  1.00 42.16  ? 47  GLY A C   1 
ATOM   389  O O   . GLY A 1 47  ? 7.806   4.245   87.301  1.00 43.11  ? 47  GLY A O   1 
ATOM   390  N N   . ARG A 1 48  ? 9.309   2.910   88.301  1.00 42.01  ? 48  ARG A N   1 
ATOM   391  C CA  . ARG A 1 48  ? 10.483  3.739   88.043  1.00 41.80  ? 48  ARG A CA  1 
ATOM   392  C C   . ARG A 1 48  ? 10.769  3.947   86.541  1.00 41.89  ? 48  ARG A C   1 
ATOM   393  O O   . ARG A 1 48  ? 10.713  2.996   85.782  1.00 42.25  ? 48  ARG A O   1 
ATOM   394  C CB  . ARG A 1 48  ? 11.649  3.023   88.723  1.00 42.01  ? 48  ARG A CB  1 
ATOM   395  C CG  . ARG A 1 48  ? 13.015  3.497   88.418  1.00 41.90  ? 48  ARG A CG  1 
ATOM   396  C CD  . ARG A 1 48  ? 14.013  2.763   89.306  1.00 41.72  ? 48  ARG A CD  1 
ATOM   397  N NE  . ARG A 1 48  ? 14.642  1.620   88.647  1.00 42.23  ? 48  ARG A NE  1 
ATOM   398  C CZ  . ARG A 1 48  ? 15.487  1.713   87.623  1.00 42.06  ? 48  ARG A CZ  1 
ATOM   399  N NH1 . ARG A 1 48  ? 15.787  2.891   87.093  1.00 41.87  ? 48  ARG A NH1 1 
ATOM   400  N NH2 . ARG A 1 48  ? 16.022  0.624   87.108  1.00 42.71  ? 48  ARG A NH2 1 
ATOM   401  N N   . ASN A 1 49  ? 11.072  5.191   86.146  1.00 41.55  ? 49  ASN A N   1 
ATOM   402  C CA  . ASN A 1 49  ? 11.559  5.531   84.808  1.00 41.54  ? 49  ASN A CA  1 
ATOM   403  C C   . ASN A 1 49  ? 13.039  5.154   84.673  1.00 41.37  ? 49  ASN A C   1 
ATOM   404  O O   . ASN A 1 49  ? 13.728  4.809   85.643  1.00 40.59  ? 49  ASN A O   1 
ATOM   405  C CB  . ASN A 1 49  ? 11.370  7.042   84.521  1.00 41.39  ? 49  ASN A CB  1 
ATOM   406  C CG  . ASN A 1 49  ? 11.158  7.378   83.032  1.00 42.15  ? 49  ASN A CG  1 
ATOM   407  O OD1 . ASN A 1 49  ? 11.338  6.543   82.139  1.00 42.80  ? 49  ASN A OD1 1 
ATOM   408  N ND2 . ASN A 1 49  ? 10.782  8.634   82.768  1.00 41.23  ? 49  ASN A ND2 1 
ATOM   409  N N   . TYR A 1 50  ? 13.477  5.157   83.430  1.00 41.49  ? 50  TYR A N   1 
ATOM   410  C CA  . TYR A 1 50  ? 14.853  4.953   83.064  1.00 41.67  ? 50  TYR A CA  1 
ATOM   411  C C   . TYR A 1 50  ? 15.758  5.976   83.741  1.00 41.61  ? 50  TYR A C   1 
ATOM   412  O O   . TYR A 1 50  ? 15.413  7.148   83.823  1.00 41.28  ? 50  TYR A O   1 
ATOM   413  C CB  . TYR A 1 50  ? 14.931  5.090   81.546  1.00 41.46  ? 50  TYR A CB  1 
ATOM   414  C CG  . TYR A 1 50  ? 16.294  5.207   80.926  1.00 41.14  ? 50  TYR A CG  1 
ATOM   415  C CD1 . TYR A 1 50  ? 17.091  4.088   80.721  1.00 41.60  ? 50  TYR A CD1 1 
ATOM   416  C CD2 . TYR A 1 50  ? 16.761  6.430   80.487  1.00 41.21  ? 50  TYR A CD2 1 
ATOM   417  C CE1 . TYR A 1 50  ? 18.345  4.215   80.129  1.00 41.87  ? 50  TYR A CE1 1 
ATOM   418  C CE2 . TYR A 1 50  ? 17.991  6.560   79.894  1.00 41.43  ? 50  TYR A CE2 1 
ATOM   419  C CZ  . TYR A 1 50  ? 18.776  5.450   79.701  1.00 41.42  ? 50  TYR A CZ  1 
ATOM   420  O OH  . TYR A 1 50  ? 20.007  5.615   79.110  1.00 40.91  ? 50  TYR A OH  1 
ATOM   421  N N   . GLN A 1 51  ? 16.915  5.511   84.194  1.00 41.93  ? 51  GLN A N   1 
ATOM   422  C CA  . GLN A 1 51  ? 17.953  6.362   84.748  1.00 42.13  ? 51  GLN A CA  1 
ATOM   423  C C   . GLN A 1 51  ? 19.256  6.002   84.069  1.00 41.48  ? 51  GLN A C   1 
ATOM   424  O O   . GLN A 1 51  ? 19.773  4.904   84.290  1.00 40.54  ? 51  GLN A O   1 
ATOM   425  C CB  . GLN A 1 51  ? 18.114  6.109   86.236  1.00 42.66  ? 51  GLN A CB  1 
ATOM   426  C CG  . GLN A 1 51  ? 16.888  6.369   87.072  1.00 44.43  ? 51  GLN A CG  1 
ATOM   427  C CD  . GLN A 1 51  ? 17.120  5.974   88.521  1.00 44.27  ? 51  GLN A CD  1 
ATOM   428  O OE1 . GLN A 1 51  ? 18.100  6.408   89.137  1.00 47.84  ? 51  GLN A OE1 1 
ATOM   429  N NE2 . GLN A 1 51  ? 16.243  5.128   89.060  1.00 43.06  ? 51  GLN A NE2 1 
ATOM   430  N N   . ALA A 1 52  ? 19.800  6.914   83.262  1.00 40.91  ? 52  ALA A N   1 
ATOM   431  C CA  . ALA A 1 52  ? 20.974  6.579   82.439  1.00 41.25  ? 52  ALA A CA  1 
ATOM   432  C C   . ALA A 1 52  ? 22.173  6.102   83.261  1.00 40.97  ? 52  ALA A C   1 
ATOM   433  O O   . ALA A 1 52  ? 23.006  5.367   82.759  1.00 41.18  ? 52  ALA A O   1 
ATOM   434  C CB  . ALA A 1 52  ? 21.386  7.747   81.558  1.00 41.03  ? 52  ALA A CB  1 
ATOM   435  N N   . SER A 1 53  ? 22.268  6.516   84.518  1.00 41.24  ? 53  SER A N   1 
ATOM   436  C CA  . SER A 1 53  ? 23.426  6.155   85.340  1.00 40.93  ? 53  SER A CA  1 
ATOM   437  C C   . SER A 1 53  ? 23.333  4.732   85.894  1.00 41.01  ? 53  SER A C   1 
ATOM   438  O O   . SER A 1 53  ? 24.335  4.166   86.330  1.00 42.52  ? 53  SER A O   1 
ATOM   439  C CB  . SER A 1 53  ? 23.632  7.169   86.448  1.00 41.22  ? 53  SER A CB  1 
ATOM   440  O OG  . SER A 1 53  ? 22.628  7.088   87.431  1.00 40.76  ? 53  SER A OG  1 
ATOM   441  N N   . VAL A 1 54  ? 22.135  4.159   85.877  1.00 40.66  ? 54  VAL A N   1 
ATOM   442  C CA  . VAL A 1 54  ? 21.893  2.822   86.404  1.00 40.60  ? 54  VAL A CA  1 
ATOM   443  C C   . VAL A 1 54  ? 21.510  1.834   85.282  1.00 40.34  ? 54  VAL A C   1 
ATOM   444  O O   . VAL A 1 54  ? 21.891  0.654   85.320  1.00 40.46  ? 54  VAL A O   1 
ATOM   445  C CB  . VAL A 1 54  ? 20.755  2.887   87.422  1.00 39.94  ? 54  VAL A CB  1 
ATOM   446  C CG1 . VAL A 1 54  ? 20.339  1.508   87.869  1.00 42.81  ? 54  VAL A CG1 1 
ATOM   447  C CG2 . VAL A 1 54  ? 21.162  3.739   88.622  1.00 41.49  ? 54  VAL A CG2 1 
ATOM   448  N N   . ASP A 1 55  ? 20.753  2.307   84.290  1.00 40.15  ? 55  ASP A N   1 
ATOM   449  C CA  . ASP A 1 55  ? 20.125  1.401   83.326  1.00 41.42  ? 55  ASP A CA  1 
ATOM   450  C C   . ASP A 1 55  ? 20.838  1.483   81.991  1.00 42.19  ? 55  ASP A C   1 
ATOM   451  O O   . ASP A 1 55  ? 21.095  2.580   81.519  1.00 42.30  ? 55  ASP A O   1 
ATOM   452  C CB  . ASP A 1 55  ? 18.672  1.802   83.070  1.00 41.22  ? 55  ASP A CB  1 
ATOM   453  C CG  . ASP A 1 55  ? 17.806  1.730   84.300  1.00 41.26  ? 55  ASP A CG  1 
ATOM   454  O OD1 . ASP A 1 55  ? 17.054  2.699   84.532  1.00 40.30  ? 55  ASP A OD1 1 
ATOM   455  O OD2 . ASP A 1 55  ? 17.844  0.700   85.007  1.00 41.34  ? 55  ASP A OD2 1 
ATOM   456  N N   . SER A 1 56  ? 21.103  0.318   81.389  1.00 43.35  ? 56  SER A N   1 
ATOM   457  C CA  . SER A 1 56  ? 21.682  0.199   80.050  1.00 43.98  ? 56  SER A CA  1 
ATOM   458  C C   . SER A 1 56  ? 20.695  -0.502  79.140  1.00 44.37  ? 56  SER A C   1 
ATOM   459  O O   . SER A 1 56  ? 20.391  -1.681  79.329  1.00 45.23  ? 56  SER A O   1 
ATOM   460  C CB  . SER A 1 56  ? 22.966  -0.617  80.071  1.00 44.66  ? 56  SER A CB  1 
ATOM   461  O OG  . SER A 1 56  ? 23.959  0.009   80.867  1.00 46.12  ? 56  SER A OG  1 
ATOM   462  N N   . LEU A 1 57  ? 20.203  0.236   78.152  1.00 44.20  ? 57  LEU A N   1 
ATOM   463  C CA  . LEU A 1 57  ? 19.215  -0.287  77.214  1.00 44.76  ? 57  LEU A CA  1 
ATOM   464  C C   . LEU A 1 57  ? 19.888  -0.576  75.888  1.00 45.09  ? 57  LEU A C   1 
ATOM   465  O O   . LEU A 1 57  ? 20.664  0.241   75.403  1.00 43.59  ? 57  LEU A O   1 
ATOM   466  C CB  . LEU A 1 57  ? 18.072  0.711   76.997  1.00 44.14  ? 57  LEU A CB  1 
ATOM   467  C CG  . LEU A 1 57  ? 16.903  0.619   77.968  1.00 43.51  ? 57  LEU A CG  1 
ATOM   468  C CD1 . LEU A 1 57  ? 17.420  0.630   79.396  1.00 43.93  ? 57  LEU A CD1 1 
ATOM   469  C CD2 . LEU A 1 57  ? 15.920  1.783   77.685  1.00 43.06  ? 57  LEU A CD2 1 
ATOM   470  N N   . THR A 1 58  ? 19.578  -1.738  75.317  1.00 45.96  ? 58  THR A N   1 
ATOM   471  C CA  . THR A 1 58  ? 20.148  -2.148  74.023  1.00 46.99  ? 58  THR A CA  1 
ATOM   472  C C   . THR A 1 58  ? 18.999  -2.631  73.146  1.00 47.29  ? 58  THR A C   1 
ATOM   473  O O   . THR A 1 58  ? 18.103  -3.341  73.624  1.00 48.71  ? 58  THR A O   1 
ATOM   474  C CB  . THR A 1 58  ? 21.228  -3.245  74.203  1.00 47.16  ? 58  THR A CB  1 
ATOM   475  O OG1 . THR A 1 58  ? 22.293  -2.714  74.992  1.00 49.85  ? 58  THR A OG1 1 
ATOM   476  C CG2 . THR A 1 58  ? 21.819  -3.709  72.837  1.00 46.77  ? 58  THR A CG2 1 
ATOM   477  N N   . PHE A 1 59  ? 18.993  -2.191  71.894  1.00 47.96  ? 59  PHE A N   1 
ATOM   478  C CA  . PHE A 1 59  ? 17.961  -2.582  70.930  1.00 47.55  ? 59  PHE A CA  1 
ATOM   479  C C   . PHE A 1 59  ? 18.516  -3.566  69.921  1.00 47.51  ? 59  PHE A C   1 
ATOM   480  O O   . PHE A 1 59  ? 19.702  -3.496  69.582  1.00 47.13  ? 59  PHE A O   1 
ATOM   481  C CB  . PHE A 1 59  ? 17.479  -1.377  70.175  1.00 47.95  ? 59  PHE A CB  1 
ATOM   482  C CG  . PHE A 1 59  ? 16.710  -0.421  71.004  1.00 48.23  ? 59  PHE A CG  1 
ATOM   483  C CD1 . PHE A 1 59  ? 17.341  0.662   71.593  1.00 50.13  ? 59  PHE A CD1 1 
ATOM   484  C CD2 . PHE A 1 59  ? 15.349  -0.589  71.174  1.00 48.78  ? 59  PHE A CD2 1 
ATOM   485  C CE1 . PHE A 1 59  ? 16.629  1.554   72.354  1.00 51.20  ? 59  PHE A CE1 1 
ATOM   486  C CE2 . PHE A 1 59  ? 14.630  0.296   71.913  1.00 51.14  ? 59  PHE A CE2 1 
ATOM   487  C CZ  . PHE A 1 59  ? 15.266  1.374   72.514  1.00 48.67  ? 59  PHE A CZ  1 
ATOM   488  N N   . SER A 1 60  ? 17.657  -4.476  69.461  1.00 47.47  ? 60  SER A N   1 
ATOM   489  C CA  . SER A 1 60  ? 17.983  -5.406  68.372  1.00 47.11  ? 60  SER A CA  1 
ATOM   490  C C   . SER A 1 60  ? 16.871  -5.436  67.347  1.00 47.23  ? 60  SER A C   1 
ATOM   491  O O   . SER A 1 60  ? 15.682  -5.517  67.718  1.00 46.40  ? 60  SER A O   1 
ATOM   492  C CB  . SER A 1 60  ? 18.143  -6.823  68.869  1.00 46.86  ? 60  SER A CB  1 
ATOM   493  O OG  . SER A 1 60  ? 19.183  -6.909  69.807  1.00 50.69  ? 60  SER A OG  1 
ATOM   494  N N   . VAL A 1 61  ? 17.273  -5.387  66.066  1.00 46.21  ? 61  VAL A N   1 
ATOM   495  C CA  . VAL A 1 61  ? 16.344  -5.518  64.941  1.00 46.09  ? 61  VAL A CA  1 
ATOM   496  C C   . VAL A 1 61  ? 16.794  -6.691  64.084  1.00 46.43  ? 61  VAL A C   1 
ATOM   497  O O   . VAL A 1 61  ? 17.976  -6.940  63.946  1.00 45.42  ? 61  VAL A O   1 
ATOM   498  C CB  . VAL A 1 61  ? 16.246  -4.227  64.093  1.00 46.13  ? 61  VAL A CB  1 
ATOM   499  C CG1 . VAL A 1 61  ? 15.630  -3.095  64.882  1.00 44.35  ? 61  VAL A CG1 1 
ATOM   500  C CG2 . VAL A 1 61  ? 17.621  -3.784  63.548  1.00 44.25  ? 61  VAL A CG2 1 
ATOM   501  N N   . VAL A 1 62  ? 15.831  -7.461  63.579  1.00 46.52  ? 62  VAL A N   1 
ATOM   502  C CA  . VAL A 1 62  ? 16.096  -8.464  62.561  1.00 46.54  ? 62  VAL A CA  1 
ATOM   503  C C   . VAL A 1 62  ? 15.048  -8.342  61.427  1.00 47.03  ? 62  VAL A C   1 
ATOM   504  O O   . VAL A 1 62  ? 13.908  -7.942  61.669  1.00 45.23  ? 62  VAL A O   1 
ATOM   505  C CB  . VAL A 1 62  ? 16.033  -9.876  63.132  1.00 46.23  ? 62  VAL A CB  1 
ATOM   506  C CG1 . VAL A 1 62  ? 17.242  -10.182 64.093  1.00 45.40  ? 62  VAL A CG1 1 
ATOM   507  C CG2 . VAL A 1 62  ? 14.695  -10.110 63.848  1.00 45.53  ? 62  VAL A CG2 1 
ATOM   508  N N   . THR A 1 63  ? 15.454  -8.659  60.193  1.00 47.66  ? 63  THR A N   1 
ATOM   509  C CA  . THR A 1 63  ? 14.502  -8.776  59.068  1.00 47.27  ? 63  THR A CA  1 
ATOM   510  C C   . THR A 1 63  ? 14.800  -10.068 58.308  1.00 47.43  ? 63  THR A C   1 
ATOM   511  O O   . THR A 1 63  ? 15.963  -10.476 58.207  1.00 45.89  ? 63  THR A O   1 
ATOM   512  C CB  . THR A 1 63  ? 14.563  -7.540  58.146  1.00 47.13  ? 63  THR A CB  1 
ATOM   513  O OG1 . THR A 1 63  ? 13.471  -7.587  57.201  1.00 46.07  ? 63  THR A OG1 1 
ATOM   514  C CG2 . THR A 1 63  ? 15.932  -7.454  57.427  1.00 47.10  ? 63  THR A CG2 1 
ATOM   515  N N   . GLY A 1 64  ? 13.744  -10.747 57.847  1.00 47.96  ? 64  GLY A N   1 
ATOM   516  C CA  . GLY A 1 64  ? 13.883  -11.956 57.065  1.00 47.58  ? 64  GLY A CA  1 
ATOM   517  C C   . GLY A 1 64  ? 14.037  -13.217 57.879  1.00 48.13  ? 64  GLY A C   1 
ATOM   518  O O   . GLY A 1 64  ? 14.104  -13.170 59.111  1.00 48.47  ? 64  GLY A O   1 
ATOM   519  N N   . PRO A 1 65  ? 14.116  -14.366 57.196  1.00 47.10  ? 65  PRO A N   1 
ATOM   520  C CA  . PRO A 1 65  ? 14.148  -15.664 57.834  1.00 47.25  ? 65  PRO A CA  1 
ATOM   521  C C   . PRO A 1 65  ? 15.538  -16.149 58.260  1.00 47.03  ? 65  PRO A C   1 
ATOM   522  O O   . PRO A 1 65  ? 15.634  -17.196 58.870  1.00 46.24  ? 65  PRO A O   1 
ATOM   523  C CB  . PRO A 1 65  ? 13.586  -16.581 56.743  1.00 47.16  ? 65  PRO A CB  1 
ATOM   524  C CG  . PRO A 1 65  ? 13.921  -15.910 55.485  1.00 45.91  ? 65  PRO A CG  1 
ATOM   525  C CD  . PRO A 1 65  ? 14.145  -14.488 55.727  1.00 47.28  ? 65  PRO A CD  1 
ATOM   526  N N   . ALA A 1 66  ? 16.588  -15.394 57.937  1.00 47.12  ? 66  ALA A N   1 
ATOM   527  C CA  . ALA A 1 66  ? 17.966  -15.794 58.261  1.00 47.02  ? 66  ALA A CA  1 
ATOM   528  C C   . ALA A 1 66  ? 18.793  -14.522 58.430  1.00 47.62  ? 66  ALA A C   1 
ATOM   529  O O   . ALA A 1 66  ? 19.712  -14.251 57.644  1.00 48.61  ? 66  ALA A O   1 
ATOM   530  C CB  . ALA A 1 66  ? 18.521  -16.652 57.161  1.00 46.84  ? 66  ALA A CB  1 
ATOM   531  N N   . PRO A 1 67  ? 18.431  -13.701 59.429  1.00 46.75  ? 67  PRO A N   1 
ATOM   532  C CA  . PRO A 1 67  ? 19.093  -12.432 59.652  1.00 46.72  ? 67  PRO A CA  1 
ATOM   533  C C   . PRO A 1 67  ? 20.550  -12.627 60.068  1.00 46.39  ? 67  PRO A C   1 
ATOM   534  O O   . PRO A 1 67  ? 20.876  -13.604 60.705  1.00 45.92  ? 67  PRO A O   1 
ATOM   535  C CB  . PRO A 1 67  ? 18.267  -11.798 60.773  1.00 46.27  ? 67  PRO A CB  1 
ATOM   536  C CG  . PRO A 1 67  ? 17.611  -12.898 61.438  1.00 47.22  ? 67  PRO A CG  1 
ATOM   537  C CD  . PRO A 1 67  ? 17.361  -13.935 60.406  1.00 47.03  ? 67  PRO A CD  1 
ATOM   538  N N   . SER A 1 68  ? 21.424  -11.728 59.654  1.00 46.62  ? 68  SER A N   1 
ATOM   539  C CA  . SER A 1 68  ? 22.808  -11.744 60.122  1.00 47.20  ? 68  SER A CA  1 
ATOM   540  C C   . SER A 1 68  ? 23.332  -10.313 60.089  1.00 47.09  ? 68  SER A C   1 
ATOM   541  O O   . SER A 1 68  ? 22.871  -9.503  59.295  1.00 46.87  ? 68  SER A O   1 
ATOM   542  C CB  . SER A 1 68  ? 23.682  -12.619 59.229  1.00 47.27  ? 68  SER A CB  1 
ATOM   543  O OG  . SER A 1 68  ? 24.208  -11.835 58.180  1.00 47.76  ? 68  SER A OG  1 
ATOM   544  N N   . GLN A 1 69  ? 24.297  -10.019 60.948  1.00 47.54  ? 69  GLN A N   1 
ATOM   545  C CA  . GLN A 1 69  ? 24.875  -8.690  61.034  1.00 48.30  ? 69  GLN A CA  1 
ATOM   546  C C   . GLN A 1 69  ? 25.738  -8.368  59.818  1.00 47.76  ? 69  GLN A C   1 
ATOM   547  O O   . GLN A 1 69  ? 25.659  -7.267  59.300  1.00 49.17  ? 69  GLN A O   1 
ATOM   548  C CB  . GLN A 1 69  ? 25.646  -8.531  62.355  1.00 48.44  ? 69  GLN A CB  1 
ATOM   549  C CG  . GLN A 1 69  ? 24.692  -8.508  63.567  1.00 49.26  ? 69  GLN A CG  1 
ATOM   550  C CD  . GLN A 1 69  ? 25.296  -7.874  64.820  1.00 51.45  ? 69  GLN A CD  1 
ATOM   551  O OE1 . GLN A 1 69  ? 25.778  -6.733  64.790  1.00 56.71  ? 69  GLN A OE1 1 
ATOM   552  N NE2 . GLN A 1 69  ? 25.254  -8.610  65.929  1.00 52.75  ? 69  GLN A NE2 1 
ATOM   553  N N   . GLU A 1 70  ? 26.487  -9.331  59.347  1.00 48.76  ? 70  GLU A N   1 
ATOM   554  C CA  . GLU A 1 70  ? 27.282  -9.152  58.164  1.00 48.41  ? 70  GLU A CA  1 
ATOM   555  C C   . GLU A 1 70  ? 26.438  -8.876  56.934  1.00 48.63  ? 70  GLU A C   1 
ATOM   556  O O   . GLU A 1 70  ? 26.812  -8.094  56.120  1.00 48.81  ? 70  GLU A O   1 
ATOM   557  C CB  . GLU A 1 70  ? 28.175  -10.347 57.962  1.00 48.99  ? 70  GLU A CB  1 
ATOM   558  C CG  . GLU A 1 70  ? 28.413  -10.708 56.548  1.00 49.70  ? 70  GLU A CG  1 
ATOM   559  C CD  . GLU A 1 70  ? 29.850  -10.976 56.280  0.00 50.00  ? 70  GLU A CD  1 
ATOM   560  O OE1 . GLU A 1 70  ? 30.688  -10.195 56.758  0.00 50.00  ? 70  GLU A OE1 1 
ATOM   561  O OE2 . GLU A 1 70  ? 30.150  -11.976 55.598  0.00 50.00  ? 70  GLU A OE2 1 
ATOM   562  N N   . ALA A 1 71  ? 25.284  -9.504  56.846  1.00 48.18  ? 71  ALA A N   1 
ATOM   563  C CA  . ALA A 1 71  ? 24.298  -9.234  55.775  1.00 46.95  ? 71  ALA A CA  1 
ATOM   564  C C   . ALA A 1 71  ? 23.479  -7.967  55.939  1.00 46.56  ? 71  ALA A C   1 
ATOM   565  O O   . ALA A 1 71  ? 22.733  -7.574  55.028  1.00 45.77  ? 71  ALA A O   1 
ATOM   566  C CB  . ALA A 1 71  ? 23.367  -10.437 55.631  1.00 47.61  ? 71  ALA A CB  1 
ATOM   567  N N   . GLY A 1 72  ? 23.592  -7.290  57.089  1.00 45.23  ? 72  GLY A N   1 
ATOM   568  C CA  . GLY A 1 72  ? 22.845  -6.038  57.297  1.00 44.10  ? 72  GLY A CA  1 
ATOM   569  C C   . GLY A 1 72  ? 21.386  -6.273  57.663  1.00 43.10  ? 72  GLY A C   1 
ATOM   570  O O   . GLY A 1 72  ? 20.602  -5.346  57.744  1.00 42.85  ? 72  GLY A O   1 
ATOM   571  N N   . THR A 1 73  ? 21.005  -7.521  57.846  1.00 43.74  ? 73  THR A N   1 
ATOM   572  C CA  . THR A 1 73  ? 19.622  -7.851  58.160  1.00 44.87  ? 73  THR A CA  1 
ATOM   573  C C   . THR A 1 73  ? 19.411  -8.059  59.672  1.00 45.77  ? 73  THR A C   1 
ATOM   574  O O   . THR A 1 73  ? 18.310  -8.420  60.093  1.00 46.87  ? 73  THR A O   1 
ATOM   575  C CB  . THR A 1 73  ? 19.200  -9.109  57.412  1.00 44.08  ? 73  THR A CB  1 
ATOM   576  O OG1 . THR A 1 73  ? 20.208  -10.093 57.564  1.00 42.69  ? 73  THR A OG1 1 
ATOM   577  C CG2 . THR A 1 73  ? 19.007  -8.778  55.890  1.00 45.16  ? 73  THR A CG2 1 
ATOM   578  N N   . LYS A 1 74  ? 20.491  -7.908  60.452  1.00 46.94  ? 74  LYS A N   1 
ATOM   579  C CA  . LYS A 1 74  ? 20.424  -7.919  61.928  1.00 46.95  ? 74  LYS A CA  1 
ATOM   580  C C   . LYS A 1 74  ? 21.251  -6.751  62.402  1.00 47.14  ? 74  LYS A C   1 
ATOM   581  O O   . LYS A 1 74  ? 22.338  -6.514  61.876  1.00 47.19  ? 74  LYS A O   1 
ATOM   582  C CB  . LYS A 1 74  ? 20.981  -9.225  62.500  1.00 47.82  ? 74  LYS A CB  1 
ATOM   583  C CG  . LYS A 1 74  ? 20.943  -9.330  64.053  1.00 48.06  ? 74  LYS A CG  1 
ATOM   584  C CD  . LYS A 1 74  ? 21.209  -10.746 64.486  1.00 49.14  ? 74  LYS A CD  1 
ATOM   585  C CE  . LYS A 1 74  ? 20.575  -11.073 65.832  1.00 53.08  ? 74  LYS A CE  1 
ATOM   586  N NZ  . LYS A 1 74  ? 21.576  -11.309 66.893  1.00 55.19  ? 74  LYS A NZ  1 
ATOM   587  N N   . ALA A 1 75  ? 20.738  -5.997  63.373  1.00 46.41  ? 75  ALA A N   1 
ATOM   588  C CA  . ALA A 1 75  ? 21.538  -4.939  64.008  1.00 46.30  ? 75  ALA A CA  1 
ATOM   589  C C   . ALA A 1 75  ? 21.229  -4.850  65.520  1.00 46.07  ? 75  ALA A C   1 
ATOM   590  O O   . ALA A 1 75  ? 20.095  -5.087  65.957  1.00 45.11  ? 75  ALA A O   1 
ATOM   591  C CB  . ALA A 1 75  ? 21.315  -3.621  63.346  1.00 45.00  ? 75  ALA A CB  1 
ATOM   592  N N   . ARG A 1 76  ? 22.280  -4.592  66.284  1.00 46.02  ? 76  ARG A N   1 
ATOM   593  C CA  . ARG A 1 76  ? 22.196  -4.388  67.728  1.00 47.36  ? 76  ARG A CA  1 
ATOM   594  C C   . ARG A 1 76  ? 22.799  -3.006  67.994  1.00 47.02  ? 76  ARG A C   1 
ATOM   595  O O   . ARG A 1 76  ? 23.854  -2.658  67.425  1.00 46.68  ? 76  ARG A O   1 
ATOM   596  C CB  . ARG A 1 76  ? 22.978  -5.459  68.462  1.00 47.63  ? 76  ARG A CB  1 
ATOM   597  C CG  . ARG A 1 76  ? 22.514  -6.865  68.172  1.00 50.68  ? 76  ARG A CG  1 
ATOM   598  C CD  . ARG A 1 76  ? 23.505  -7.895  68.684  1.00 53.53  ? 76  ARG A CD  1 
ATOM   599  N NE  . ARG A 1 76  ? 23.433  -8.010  70.136  1.00 59.02  ? 76  ARG A NE  1 
ATOM   600  C CZ  . ARG A 1 76  ? 22.868  -9.027  70.788  1.00 63.42  ? 76  ARG A CZ  1 
ATOM   601  N NH1 . ARG A 1 76  ? 22.326  -10.064 70.123  1.00 65.34  ? 76  ARG A NH1 1 
ATOM   602  N NH2 . ARG A 1 76  ? 22.855  -9.021  72.122  1.00 63.18  ? 76  ARG A NH2 1 
ATOM   603  N N   . PHE A 1 77  ? 22.124  -2.209  68.825  1.00 46.36  ? 77  PHE A N   1 
ATOM   604  C CA  . PHE A 1 77  ? 22.573  -0.845  69.092  1.00 45.83  ? 77  PHE A CA  1 
ATOM   605  C C   . PHE A 1 77  ? 22.073  -0.302  70.461  1.00 45.80  ? 77  PHE A C   1 
ATOM   606  O O   . PHE A 1 77  ? 20.919  -0.549  70.867  1.00 45.32  ? 77  PHE A O   1 
ATOM   607  C CB  . PHE A 1 77  ? 22.200  0.099   67.920  1.00 45.89  ? 77  PHE A CB  1 
ATOM   608  C CG  . PHE A 1 77  ? 20.750  0.066   67.530  1.00 44.49  ? 77  PHE A CG  1 
ATOM   609  C CD1 . PHE A 1 77  ? 19.898  1.090   67.890  1.00 45.51  ? 77  PHE A CD1 1 
ATOM   610  C CD2 . PHE A 1 77  ? 20.244  -0.979  66.772  1.00 45.59  ? 77  PHE A CD2 1 
ATOM   611  C CE1 . PHE A 1 77  ? 18.580  1.081   67.497  1.00 45.59  ? 77  PHE A CE1 1 
ATOM   612  C CE2 . PHE A 1 77  ? 18.934  -1.028  66.414  1.00 46.85  ? 77  PHE A CE2 1 
ATOM   613  C CZ  . PHE A 1 77  ? 18.088  -0.001  66.770  1.00 47.88  ? 77  PHE A CZ  1 
ATOM   614  N N   . PRO A 1 78  ? 22.951  0.416   71.174  1.00 45.76  ? 78  PRO A N   1 
ATOM   615  C CA  . PRO A 1 78  ? 22.598  0.885   72.516  1.00 45.33  ? 78  PRO A CA  1 
ATOM   616  C C   . PRO A 1 78  ? 21.839  2.218   72.474  1.00 45.34  ? 78  PRO A C   1 
ATOM   617  O O   . PRO A 1 78  ? 21.952  3.009   71.495  1.00 44.00  ? 78  PRO A O   1 
ATOM   618  C CB  . PRO A 1 78  ? 23.964  1.044   73.176  1.00 45.58  ? 78  PRO A CB  1 
ATOM   619  C CG  . PRO A 1 78  ? 24.834  1.479   72.063  1.00 46.10  ? 78  PRO A CG  1 
ATOM   620  C CD  . PRO A 1 78  ? 24.311  0.860   70.803  1.00 45.50  ? 78  PRO A CD  1 
ATOM   621  N N   . LEU A 1 79  ? 21.014  2.427   73.497  1.00 44.69  ? 79  LEU A N   1 
ATOM   622  C CA  . LEU A 1 79  ? 20.453  3.746   73.756  1.00 44.08  ? 79  LEU A CA  1 
ATOM   623  C C   . LEU A 1 79  ? 21.556  4.596   74.380  1.00 43.85  ? 79  LEU A C   1 
ATOM   624  O O   . LEU A 1 79  ? 22.056  4.272   75.458  1.00 42.85  ? 79  LEU A O   1 
ATOM   625  C CB  . LEU A 1 79  ? 19.252  3.630   74.711  1.00 44.55  ? 79  LEU A CB  1 
ATOM   626  C CG  . LEU A 1 79  ? 18.540  4.948   75.026  1.00 44.16  ? 79  LEU A CG  1 
ATOM   627  C CD1 . LEU A 1 79  ? 17.878  5.464   73.758  1.00 41.08  ? 79  LEU A CD1 1 
ATOM   628  C CD2 . LEU A 1 79  ? 17.528  4.767   76.152  1.00 42.85  ? 79  LEU A CD2 1 
ATOM   629  N N   . ARG A 1 80  ? 21.967  5.661   73.701  1.00 43.79  ? 80  ARG A N   1 
ATOM   630  C CA  . ARG A 1 80  ? 23.023  6.530   74.192  1.00 43.38  ? 80  ARG A CA  1 
ATOM   631  C C   . ARG A 1 80  ? 22.984  7.892   73.486  1.00 43.12  ? 80  ARG A C   1 
ATOM   632  O O   . ARG A 1 80  ? 22.350  8.036   72.444  1.00 41.26  ? 80  ARG A O   1 
ATOM   633  C CB  . ARG A 1 80  ? 24.393  5.885   73.966  1.00 43.92  ? 80  ARG A CB  1 
ATOM   634  C CG  . ARG A 1 80  ? 24.859  5.889   72.499  1.00 43.81  ? 80  ARG A CG  1 
ATOM   635  C CD  . ARG A 1 80  ? 26.166  5.172   72.324  1.00 44.75  ? 80  ARG A CD  1 
ATOM   636  N NE  . ARG A 1 80  ? 27.270  5.872   72.972  1.00 46.34  ? 80  ARG A NE  1 
ATOM   637  C CZ  . ARG A 1 80  ? 28.537  5.461   72.958  1.00 48.90  ? 80  ARG A CZ  1 
ATOM   638  N NH1 . ARG A 1 80  ? 28.877  4.341   72.332  1.00 49.62  ? 80  ARG A NH1 1 
ATOM   639  N NH2 . ARG A 1 80  ? 29.471  6.163   73.571  1.00 48.02  ? 80  ARG A NH2 1 
ATOM   640  N N   . ASP A 1 81  ? 23.664  8.887   74.050  1.00 42.45  ? 81  ASP A N   1 
ATOM   641  C CA  . ASP A 1 81  ? 23.604  10.239  73.495  1.00 43.15  ? 81  ASP A CA  1 
ATOM   642  C C   . ASP A 1 81  ? 24.374  10.423  72.193  1.00 43.55  ? 81  ASP A C   1 
ATOM   643  O O   . ASP A 1 81  ? 23.937  11.206  71.350  1.00 43.61  ? 81  ASP A O   1 
ATOM   644  C CB  . ASP A 1 81  ? 24.074  11.280  74.509  1.00 42.64  ? 81  ASP A CB  1 
ATOM   645  C CG  . ASP A 1 81  ? 23.091  11.467  75.643  1.00 41.83  ? 81  ASP A CG  1 
ATOM   646  O OD1 . ASP A 1 81  ? 21.899  11.169  75.435  1.00 39.68  ? 81  ASP A OD1 1 
ATOM   647  O OD2 . ASP A 1 81  ? 23.508  11.924  76.727  1.00 40.99  ? 81  ASP A OD2 1 
ATOM   648  N N   . ALA A 1 82  ? 25.530  9.772   72.057  1.00 44.08  ? 82  ALA A N   1 
ATOM   649  C CA  . ALA A 1 82  ? 26.339  9.916   70.845  1.00 44.90  ? 82  ALA A CA  1 
ATOM   650  C C   . ALA A 1 82  ? 25.657  9.200   69.672  1.00 45.00  ? 82  ALA A C   1 
ATOM   651  O O   . ALA A 1 82  ? 25.311  8.018   69.757  1.00 44.44  ? 82  ALA A O   1 
ATOM   652  C CB  . ALA A 1 82  ? 27.769  9.400   71.065  1.00 44.73  ? 82  ALA A CB  1 
ATOM   653  N N   . VAL A 1 83  ? 25.408  9.946   68.604  1.00 45.76  ? 83  VAL A N   1 
ATOM   654  C CA  . VAL A 1 83  ? 24.727  9.395   67.424  1.00 47.23  ? 83  VAL A CA  1 
ATOM   655  C C   . VAL A 1 83  ? 25.684  9.365   66.235  1.00 47.98  ? 83  VAL A C   1 
ATOM   656  O O   . VAL A 1 83  ? 26.075  10.405  65.718  1.00 46.73  ? 83  VAL A O   1 
ATOM   657  C CB  . VAL A 1 83  ? 23.473  10.203  67.053  1.00 47.47  ? 83  VAL A CB  1 
ATOM   658  C CG1 . VAL A 1 83  ? 22.933  9.771   65.672  1.00 46.82  ? 83  VAL A CG1 1 
ATOM   659  C CG2 . VAL A 1 83  ? 22.398  10.040  68.167  1.00 47.28  ? 83  VAL A CG2 1 
ATOM   660  N N   . GLU A 1 84  ? 26.047  8.145   65.827  1.00 49.48  ? 84  GLU A N   1 
ATOM   661  C CA  . GLU A 1 84  ? 26.954  7.928   64.706  1.00 49.50  ? 84  GLU A CA  1 
ATOM   662  C C   . GLU A 1 84  ? 26.157  8.024   63.424  1.00 49.20  ? 84  GLU A C   1 
ATOM   663  O O   . GLU A 1 84  ? 25.238  7.234   63.188  1.00 49.52  ? 84  GLU A O   1 
ATOM   664  C CB  . GLU A 1 84  ? 27.598  6.550   64.822  1.00 50.47  ? 84  GLU A CB  1 
ATOM   665  C CG  . GLU A 1 84  ? 28.593  6.251   63.733  1.00 51.66  ? 84  GLU A CG  1 
ATOM   666  C CD  . GLU A 1 84  ? 29.712  7.223   63.732  1.00 54.43  ? 84  GLU A CD  1 
ATOM   667  O OE1 . GLU A 1 84  ? 30.108  7.670   62.641  1.00 59.54  ? 84  GLU A OE1 1 
ATOM   668  O OE2 . GLU A 1 84  ? 30.193  7.561   64.835  1.00 59.02  ? 84  GLU A OE2 1 
ATOM   669  N N   . GLU A 1 85  ? 26.491  8.998   62.585  1.00 49.30  ? 85  GLU A N   1 
ATOM   670  C CA  . GLU A 1 85  ? 25.719  9.245   61.370  1.00 49.64  ? 85  GLU A CA  1 
ATOM   671  C C   . GLU A 1 85  ? 25.798  8.052   60.420  1.00 49.09  ? 85  GLU A C   1 
ATOM   672  O O   . GLU A 1 85  ? 26.887  7.561   60.122  1.00 49.49  ? 85  GLU A O   1 
ATOM   673  C CB  . GLU A 1 85  ? 26.215  10.510  60.668  1.00 50.28  ? 85  GLU A CB  1 
ATOM   674  C CG  . GLU A 1 85  ? 25.607  11.796  61.205  1.00 51.45  ? 85  GLU A CG  1 
ATOM   675  C CD  . GLU A 1 85  ? 24.153  11.633  61.601  0.00 50.00  ? 85  GLU A CD  1 
ATOM   676  O OE1 . GLU A 1 85  ? 23.362  11.138  60.771  0.00 50.00  ? 85  GLU A OE1 1 
ATOM   677  O OE2 . GLU A 1 85  ? 23.802  11.999  62.742  0.00 50.00  ? 85  GLU A OE2 1 
ATOM   678  N N   . GLY A 1 86  ? 24.645  7.588   59.945  1.00 48.96  ? 86  GLY A N   1 
ATOM   679  C CA  . GLY A 1 86  ? 24.617  6.515   58.951  1.00 48.79  ? 86  GLY A CA  1 
ATOM   680  C C   . GLY A 1 86  ? 24.526  5.133   59.548  1.00 49.16  ? 86  GLY A C   1 
ATOM   681  O O   . GLY A 1 86  ? 24.493  4.138   58.805  1.00 50.12  ? 86  GLY A O   1 
ATOM   682  N N   . ASP A 1 87  ? 24.481  5.058   60.888  1.00 48.15  ? 87  ASP A N   1 
ATOM   683  C CA  . ASP A 1 87  ? 24.256  3.809   61.607  1.00 47.28  ? 87  ASP A CA  1 
ATOM   684  C C   . ASP A 1 87  ? 22.865  3.674   62.199  1.00 45.46  ? 87  ASP A C   1 
ATOM   685  O O   . ASP A 1 87  ? 22.110  4.616   62.282  1.00 44.29  ? 87  ASP A O   1 
ATOM   686  C CB  . ASP A 1 87  ? 25.279  3.693   62.739  1.00 48.24  ? 87  ASP A CB  1 
ATOM   687  C CG  . ASP A 1 87  ? 26.671  3.452   62.221  1.00 50.08  ? 87  ASP A CG  1 
ATOM   688  O OD1 . ASP A 1 87  ? 26.823  3.337   60.984  1.00 52.16  ? 87  ASP A OD1 1 
ATOM   689  O OD2 . ASP A 1 87  ? 27.593  3.331   63.051  1.00 52.17  ? 87  ASP A OD2 1 
ATOM   690  N N   . TRP A 1 88  ? 22.543  2.457   62.594  1.00 46.06  ? 88  TRP A N   1 
ATOM   691  C CA  . TRP A 1 88  ? 21.400  2.162   63.438  1.00 46.17  ? 88  TRP A CA  1 
ATOM   692  C C   . TRP A 1 88  ? 21.714  2.776   64.820  1.00 46.43  ? 88  TRP A C   1 
ATOM   693  O O   . TRP A 1 88  ? 22.720  2.393   65.436  1.00 45.40  ? 88  TRP A O   1 
ATOM   694  C CB  . TRP A 1 88  ? 21.250  0.656   63.624  1.00 45.83  ? 88  TRP A CB  1 
ATOM   695  C CG  . TRP A 1 88  ? 20.683  -0.104  62.449  1.00 46.81  ? 88  TRP A CG  1 
ATOM   696  C CD1 . TRP A 1 88  ? 21.381  -0.765  61.481  1.00 46.60  ? 88  TRP A CD1 1 
ATOM   697  C CD2 . TRP A 1 88  ? 19.307  -0.323  62.171  1.00 46.10  ? 88  TRP A CD2 1 
ATOM   698  N NE1 . TRP A 1 88  ? 20.518  -1.375  60.610  1.00 46.77  ? 88  TRP A NE1 1 
ATOM   699  C CE2 . TRP A 1 88  ? 19.235  -1.119  61.006  1.00 47.35  ? 88  TRP A CE2 1 
ATOM   700  C CE3 . TRP A 1 88  ? 18.128  0.065   62.791  1.00 46.56  ? 88  TRP A CE3 1 
ATOM   701  C CZ2 . TRP A 1 88  ? 18.029  -1.525  60.453  1.00 45.69  ? 88  TRP A CZ2 1 
ATOM   702  C CZ3 . TRP A 1 88  ? 16.909  -0.335  62.232  1.00 47.22  ? 88  TRP A CZ3 1 
ATOM   703  C CH2 . TRP A 1 88  ? 16.873  -1.124  61.061  1.00 46.04  ? 88  TRP A CH2 1 
ATOM   704  N N   . THR A 1 89  ? 20.881  3.711   65.275  1.00 46.78  ? 89  THR A N   1 
ATOM   705  C CA  . THR A 1 89  ? 21.074  4.370   66.599  1.00 46.20  ? 89  THR A CA  1 
ATOM   706  C C   . THR A 1 89  ? 19.758  4.647   67.313  1.00 46.62  ? 89  THR A C   1 
ATOM   707  O O   . THR A 1 89  ? 18.679  4.658   66.719  1.00 47.02  ? 89  THR A O   1 
ATOM   708  C CB  . THR A 1 89  ? 21.813  5.714   66.493  1.00 46.52  ? 89  THR A CB  1 
ATOM   709  O OG1 . THR A 1 89  ? 20.999  6.641   65.773  1.00 46.80  ? 89  THR A OG1 1 
ATOM   710  C CG2 . THR A 1 89  ? 23.196  5.581   65.807  1.00 46.52  ? 89  THR A CG2 1 
ATOM   711  N N   . ALA A 1 90  ? 19.849  4.837   68.632  1.00 45.87  ? 90  ALA A N   1 
ATOM   712  C CA  . ALA A 1 90  ? 18.689  5.183   69.431  1.00 44.49  ? 90  ALA A CA  1 
ATOM   713  C C   . ALA A 1 90  ? 19.182  6.174   70.456  1.00 43.77  ? 90  ALA A C   1 
ATOM   714  O O   . ALA A 1 90  ? 20.230  5.961   71.041  1.00 42.32  ? 90  ALA A O   1 
ATOM   715  C CB  . ALA A 1 90  ? 18.124  3.961   70.077  1.00 44.99  ? 90  ALA A CB  1 
ATOM   716  N N   . THR A 1 91  ? 18.469  7.288   70.610  1.00 43.40  ? 91  THR A N   1 
ATOM   717  C CA  . THR A 1 91  ? 18.818  8.279   71.600  1.00 43.22  ? 91  THR A CA  1 
ATOM   718  C C   . THR A 1 91  ? 17.580  8.857   72.257  1.00 43.45  ? 91  THR A C   1 
ATOM   719  O O   . THR A 1 91  ? 16.520  8.854   71.679  1.00 43.45  ? 91  THR A O   1 
ATOM   720  C CB  . THR A 1 91  ? 19.640  9.424   71.005  1.00 43.94  ? 91  THR A CB  1 
ATOM   721  O OG1 . THR A 1 91  ? 20.395  10.052  72.042  1.00 43.12  ? 91  THR A OG1 1 
ATOM   722  C CG2 . THR A 1 91  ? 18.764  10.465  70.325  1.00 43.08  ? 91  THR A CG2 1 
ATOM   723  N N   . VAL A 1 92  ? 17.759  9.373   73.475  1.00 42.09  ? 92  VAL A N   1 
ATOM   724  C CA  . VAL A 1 92  ? 16.694  10.032  74.224  1.00 40.55  ? 92  VAL A CA  1 
ATOM   725  C C   . VAL A 1 92  ? 16.517  11.450  73.731  1.00 39.39  ? 92  VAL A C   1 
ATOM   726  O O   . VAL A 1 92  ? 17.476  12.217  73.608  1.00 39.01  ? 92  VAL A O   1 
ATOM   727  C CB  . VAL A 1 92  ? 16.981  10.017  75.774  1.00 40.24  ? 92  VAL A CB  1 
ATOM   728  C CG1 . VAL A 1 92  ? 15.868  10.725  76.538  1.00 39.58  ? 92  VAL A CG1 1 
ATOM   729  C CG2 . VAL A 1 92  ? 17.140  8.573   76.282  1.00 38.23  ? 92  VAL A CG2 1 
ATOM   730  N N   . VAL A 1 93  ? 15.274  11.800  73.437  1.00 38.48  ? 93  VAL A N   1 
ATOM   731  C CA  . VAL A 1 93  ? 14.933  13.162  73.094  1.00 38.97  ? 93  VAL A CA  1 
ATOM   732  C C   . VAL A 1 93  ? 13.935  13.819  74.064  1.00 39.49  ? 93  VAL A C   1 
ATOM   733  O O   . VAL A 1 93  ? 13.674  15.010  73.960  1.00 38.53  ? 93  VAL A O   1 
ATOM   734  C CB  . VAL A 1 93  ? 14.441  13.265  71.631  1.00 38.84  ? 93  VAL A CB  1 
ATOM   735  C CG1 . VAL A 1 93  ? 15.600  12.984  70.695  1.00 36.19  ? 93  VAL A CG1 1 
ATOM   736  C CG2 . VAL A 1 93  ? 13.294  12.289  71.344  1.00 39.77  ? 93  VAL A CG2 1 
ATOM   737  N N   . ASP A 1 94  ? 13.354  13.057  74.989  1.00 40.25  ? 94  ASP A N   1 
ATOM   738  C CA  . ASP A 1 94  ? 12.502  13.671  76.012  1.00 41.43  ? 94  ASP A CA  1 
ATOM   739  C C   . ASP A 1 94  ? 12.316  12.666  77.134  1.00 41.47  ? 94  ASP A C   1 
ATOM   740  O O   . ASP A 1 94  ? 12.272  11.475  76.896  1.00 40.90  ? 94  ASP A O   1 
ATOM   741  C CB  . ASP A 1 94  ? 11.149  14.078  75.409  1.00 41.71  ? 94  ASP A CB  1 
ATOM   742  C CG  . ASP A 1 94  ? 10.206  14.691  76.426  1.00 42.36  ? 94  ASP A CG  1 
ATOM   743  O OD1 . ASP A 1 94  ? 10.600  15.575  77.217  1.00 45.46  ? 94  ASP A OD1 1 
ATOM   744  O OD2 . ASP A 1 94  ? 9.035   14.291  76.428  1.00 49.15  ? 94  ASP A OD2 1 
ATOM   745  N N   . GLN A 1 95  ? 12.214  13.145  78.359  1.00 43.16  ? 95  GLN A N   1 
ATOM   746  C CA  . GLN A 1 95  ? 12.028  12.250  79.489  1.00 43.74  ? 95  GLN A CA  1 
ATOM   747  C C   . GLN A 1 95  ? 11.138  12.934  80.500  1.00 44.63  ? 95  GLN A C   1 
ATOM   748  O O   . GLN A 1 95  ? 11.451  14.028  80.977  1.00 43.79  ? 95  GLN A O   1 
ATOM   749  C CB  . GLN A 1 95  ? 13.372  11.841  80.107  1.00 43.75  ? 95  GLN A CB  1 
ATOM   750  C CG  . GLN A 1 95  ? 13.232  10.787  81.202  1.00 44.34  ? 95  GLN A CG  1 
ATOM   751  C CD  . GLN A 1 95  ? 14.546  10.136  81.615  1.00 46.08  ? 95  GLN A CD  1 
ATOM   752  O OE1 . GLN A 1 95  ? 15.628  10.476  81.113  1.00 51.06  ? 95  GLN A OE1 1 
ATOM   753  N NE2 . GLN A 1 95  ? 14.451  9.175   82.537  1.00 48.36  ? 95  GLN A NE2 1 
ATOM   754  N N   . GLN A 1 96  ? 10.010  12.290  80.792  1.00 45.58  ? 96  GLN A N   1 
ATOM   755  C CA  . GLN A 1 96  ? 9.020   12.839  81.705  1.00 46.16  ? 96  GLN A CA  1 
ATOM   756  C C   . GLN A 1 96  ? 8.838   11.841  82.830  1.00 46.78  ? 96  GLN A C   1 
ATOM   757  O O   . GLN A 1 96  ? 9.543   10.818  82.871  1.00 47.93  ? 96  GLN A O   1 
ATOM   758  C CB  . GLN A 1 96  ? 7.709   13.094  80.959  1.00 46.83  ? 96  GLN A CB  1 
ATOM   759  C CG  . GLN A 1 96  ? 7.834   14.018  79.743  1.00 48.16  ? 96  GLN A CG  1 
ATOM   760  C CD  . GLN A 1 96  ? 8.265   15.439  80.104  1.00 50.64  ? 96  GLN A CD  1 
ATOM   761  O OE1 . GLN A 1 96  ? 8.080   15.893  81.230  1.00 54.61  ? 96  GLN A OE1 1 
ATOM   762  N NE2 . GLN A 1 96  ? 8.824   16.149  79.139  1.00 53.70  ? 96  GLN A NE2 1 
ATOM   763  N N   . ASP A 1 97  ? 7.908   12.114  83.744  1.00 46.38  ? 97  ASP A N   1 
ATOM   764  C CA  . ASP A 1 97  ? 7.741   11.270  84.924  1.00 46.24  ? 97  ASP A CA  1 
ATOM   765  C C   . ASP A 1 97  ? 7.889   9.777   84.611  1.00 45.89  ? 97  ASP A C   1 
ATOM   766  O O   . ASP A 1 97  ? 8.812   9.131   85.117  1.00 45.76  ? 97  ASP A O   1 
ATOM   767  C CB  . ASP A 1 97  ? 6.388   11.548  85.609  1.00 46.39  ? 97  ASP A CB  1 
ATOM   768  C CG  . ASP A 1 97  ? 6.309   10.967  87.014  1.00 46.89  ? 97  ASP A CG  1 
ATOM   769  O OD1 . ASP A 1 97  ? 6.286   9.801   86.898  0.00 50.00  ? 97  ASP A OD1 1 
ATOM   770  O OD2 . ASP A 1 97  ? 5.566   11.715  87.695  0.00 50.00  ? 97  ASP A OD2 1 
ATOM   771  N N   . CYS A 1 98  ? 6.982   9.245   83.794  1.00 45.09  ? 98  CYS A N   1 
ATOM   772  C CA  . CYS A 1 98  ? 6.916   7.806   83.500  1.00 45.59  ? 98  CYS A CA  1 
ATOM   773  C C   . CYS A 1 98  ? 7.311   7.444   82.065  1.00 44.25  ? 98  CYS A C   1 
ATOM   774  O O   . CYS A 1 98  ? 7.413   6.255   81.738  1.00 42.86  ? 98  CYS A O   1 
ATOM   775  C CB  . CYS A 1 98  ? 5.494   7.292   83.765  1.00 45.67  ? 98  CYS A CB  1 
ATOM   776  S SG  . CYS A 1 98  ? 4.922   7.655   85.438  1.00 53.95  ? 98  CYS A SG  1 
ATOM   777  N N   . THR A 1 99  ? 7.571   8.465   81.246  1.00 43.66  ? 99  THR A N   1 
ATOM   778  C CA  . THR A 1 99  ? 7.774   8.291   79.804  1.00 43.45  ? 99  THR A CA  1 
ATOM   779  C C   . THR A 1 99  ? 9.205   8.607   79.344  1.00 42.65  ? 99  THR A C   1 
ATOM   780  O O   . THR A 1 99  ? 9.906   9.452   79.913  1.00 40.68  ? 99  THR A O   1 
ATOM   781  C CB  . THR A 1 99  ? 6.772   9.138   78.974  1.00 44.15  ? 99  THR A CB  1 
ATOM   782  O OG1 . THR A 1 99  ? 7.142   10.528  79.014  1.00 44.06  ? 99  THR A OG1 1 
ATOM   783  C CG2 . THR A 1 99  ? 5.351   8.958   79.499  1.00 42.77  ? 99  THR A CG2 1 
ATOM   784  N N   . LEU A 1 100 ? 9.634   7.882   78.320  1.00 41.67  ? 100 LEU A N   1 
ATOM   785  C CA  . LEU A 1 100 ? 10.943  8.080   77.732  1.00 41.95  ? 100 LEU A CA  1 
ATOM   786  C C   . LEU A 1 100 ? 10.730  8.071   76.225  1.00 41.94  ? 100 LEU A C   1 
ATOM   787  O O   . LEU A 1 100 ? 10.351  7.049   75.680  1.00 41.64  ? 100 LEU A O   1 
ATOM   788  C CB  . LEU A 1 100 ? 11.881  6.962   78.151  1.00 41.13  ? 100 LEU A CB  1 
ATOM   789  C CG  . LEU A 1 100 ? 13.357  7.113   77.771  1.00 41.86  ? 100 LEU A CG  1 
ATOM   790  C CD1 . LEU A 1 100 ? 14.038  8.183   78.628  1.00 40.03  ? 100 LEU A CD1 1 
ATOM   791  C CD2 . LEU A 1 100 ? 14.096  5.777   77.910  1.00 39.94  ? 100 LEU A CD2 1 
ATOM   792  N N   . SER A 1 101 ? 10.912  9.218   75.586  1.00 43.15  ? 101 SER A N   1 
ATOM   793  C CA  . SER A 1 101 ? 10.731  9.331   74.139  1.00 44.06  ? 101 SER A CA  1 
ATOM   794  C C   . SER A 1 101 ? 12.080  9.151   73.488  1.00 44.73  ? 101 SER A C   1 
ATOM   795  O O   . SER A 1 101 ? 13.036  9.860   73.814  1.00 44.55  ? 101 SER A O   1 
ATOM   796  C CB  . SER A 1 101 ? 10.168  10.681  73.741  1.00 44.69  ? 101 SER A CB  1 
ATOM   797  O OG  . SER A 1 101 ? 9.140   11.074  74.628  1.00 47.59  ? 101 SER A OG  1 
ATOM   798  N N   . LEU A 1 102 ? 12.131  8.214   72.549  1.00 45.13  ? 102 LEU A N   1 
ATOM   799  C CA  . LEU A 1 102 ? 13.354  7.861   71.857  1.00 45.59  ? 102 LEU A CA  1 
ATOM   800  C C   . LEU A 1 102 ? 13.253  8.217   70.377  1.00 46.23  ? 102 LEU A C   1 
ATOM   801  O O   . LEU A 1 102 ? 12.171  8.133   69.781  1.00 46.09  ? 102 LEU A O   1 
ATOM   802  C CB  . LEU A 1 102 ? 13.575  6.359   71.986  1.00 45.77  ? 102 LEU A CB  1 
ATOM   803  C CG  . LEU A 1 102 ? 13.558  5.837   73.425  1.00 45.59  ? 102 LEU A CG  1 
ATOM   804  C CD1 . LEU A 1 102 ? 13.953  4.405   73.484  1.00 47.75  ? 102 LEU A CD1 1 
ATOM   805  C CD2 . LEU A 1 102 ? 14.501  6.690   74.281  1.00 46.48  ? 102 LEU A CD2 1 
ATOM   806  N N   . GLN A 1 103 ? 14.401  8.588   69.820  1.00 46.11  ? 103 GLN A N   1 
ATOM   807  C CA  . GLN A 1 103 ? 14.600  8.762   68.390  1.00 46.72  ? 103 GLN A CA  1 
ATOM   808  C C   . GLN A 1 103 ? 15.543  7.689   67.828  1.00 47.22  ? 103 GLN A C   1 
ATOM   809  O O   . GLN A 1 103 ? 16.709  7.610   68.209  1.00 47.84  ? 103 GLN A O   1 
ATOM   810  C CB  . GLN A 1 103 ? 15.182  10.143  68.185  1.00 46.28  ? 103 GLN A CB  1 
ATOM   811  C CG  . GLN A 1 103 ? 15.333  10.582  66.761  1.00 47.29  ? 103 GLN A CG  1 
ATOM   812  C CD  . GLN A 1 103 ? 15.589  12.056  66.695  1.00 46.29  ? 103 GLN A CD  1 
ATOM   813  O OE1 . GLN A 1 103 ? 14.692  12.854  66.938  1.00 49.58  ? 103 GLN A OE1 1 
ATOM   814  N NE2 . GLN A 1 103 ? 16.818  12.436  66.379  1.00 48.77  ? 103 GLN A NE2 1 
ATOM   815  N N   . LEU A 1 104 ? 15.023  6.863   66.929  1.00 47.76  ? 104 LEU A N   1 
ATOM   816  C CA  . LEU A 1 104 ? 15.776  5.794   66.292  1.00 48.43  ? 104 LEU A CA  1 
ATOM   817  C C   . LEU A 1 104 ? 16.066  6.213   64.849  1.00 49.07  ? 104 LEU A C   1 
ATOM   818  O O   . LEU A 1 104 ? 15.231  6.860   64.238  1.00 50.41  ? 104 LEU A O   1 
ATOM   819  C CB  . LEU A 1 104 ? 14.996  4.472   66.326  1.00 48.56  ? 104 LEU A CB  1 
ATOM   820  C CG  . LEU A 1 104 ? 15.120  3.616   67.614  1.00 50.42  ? 104 LEU A CG  1 
ATOM   821  C CD1 . LEU A 1 104 ? 14.445  4.302   68.782  1.00 50.65  ? 104 LEU A CD1 1 
ATOM   822  C CD2 . LEU A 1 104 ? 14.512  2.244   67.422  1.00 48.65  ? 104 LEU A CD2 1 
ATOM   823  N N   . THR A 1 105 ? 17.260  5.934   64.340  1.00 49.85  ? 105 THR A N   1 
ATOM   824  C CA  . THR A 1 105 ? 17.545  6.143   62.902  1.00 50.22  ? 105 THR A CA  1 
ATOM   825  C C   . THR A 1 105 ? 18.049  4.829   62.317  1.00 49.63  ? 105 THR A C   1 
ATOM   826  O O   . THR A 1 105 ? 18.650  4.049   63.023  1.00 48.42  ? 105 THR A O   1 
ATOM   827  C CB  . THR A 1 105 ? 18.581  7.247   62.618  1.00 51.13  ? 105 THR A CB  1 
ATOM   828  O OG1 . THR A 1 105 ? 18.317  8.435   63.396  1.00 54.46  ? 105 THR A OG1 1 
ATOM   829  C CG2 . THR A 1 105 ? 18.536  7.645   61.106  1.00 51.47  ? 105 THR A CG2 1 
ATOM   830  N N   . THR A 1 106 ? 17.804  4.594   61.026  1.00 49.91  ? 106 THR A N   1 
ATOM   831  C CA  . THR A 1 106 ? 18.286  3.397   60.323  1.00 49.22  ? 106 THR A CA  1 
ATOM   832  C C   . THR A 1 106 ? 19.279  3.918   59.278  1.00 48.69  ? 106 THR A C   1 
ATOM   833  O O   . THR A 1 106 ? 19.163  5.054   58.892  1.00 47.62  ? 106 THR A O   1 
ATOM   834  C CB  . THR A 1 106 ? 17.182  2.732   59.548  1.00 49.79  ? 106 THR A CB  1 
ATOM   835  O OG1 . THR A 1 106 ? 16.774  3.610   58.494  1.00 52.12  ? 106 THR A OG1 1 
ATOM   836  C CG2 . THR A 1 106 ? 15.951  2.404   60.433  1.00 51.64  ? 106 THR A CG2 1 
ATOM   837  N N   . PRO A 1 107 ? 20.221  3.085   58.807  1.00 47.78  ? 107 PRO A N   1 
ATOM   838  C CA  . PRO A 1 107 ? 21.106  3.488   57.719  1.00 48.45  ? 107 PRO A CA  1 
ATOM   839  C C   . PRO A 1 107 ? 20.308  3.762   56.437  1.00 48.12  ? 107 PRO A C   1 
ATOM   840  O O   . PRO A 1 107 ? 19.269  3.152   56.211  1.00 49.11  ? 107 PRO A O   1 
ATOM   841  C CB  . PRO A 1 107 ? 22.008  2.259   57.529  1.00 48.24  ? 107 PRO A CB  1 
ATOM   842  C CG  . PRO A 1 107 ? 21.898  1.499   58.856  1.00 47.58  ? 107 PRO A CG  1 
ATOM   843  C CD  . PRO A 1 107 ? 20.484  1.698   59.223  1.00 48.24  ? 107 PRO A CD  1 
ATOM   844  N N   . ALA A 1 108 ? 20.769  4.723   55.652  1.00 49.07  ? 108 ALA A N   1 
ATOM   845  C CA  . ALA A 1 108 ? 20.127  5.087   54.399  1.00 49.17  ? 108 ALA A CA  1 
ATOM   846  C C   . ALA A 1 108 ? 20.302  3.966   53.347  1.00 49.41  ? 108 ALA A C   1 
ATOM   847  O O   . ALA A 1 108 ? 19.766  4.078   52.248  1.00 50.51  ? 108 ALA A O   1 
ATOM   848  C CB  . ALA A 1 108 ? 20.686  6.379   53.891  1.00 47.61  ? 108 ALA A CB  1 
ATOM   849  N N   . ASN A 1 109 ? 21.064  2.923   53.667  1.00 49.59  ? 109 ASN A N   1 
ATOM   850  C CA  . ASN A 1 109 ? 21.176  1.750   52.802  1.00 48.90  ? 109 ASN A CA  1 
ATOM   851  C C   . ASN A 1 109 ? 20.746  0.469   53.484  1.00 48.63  ? 109 ASN A C   1 
ATOM   852  O O   . ASN A 1 109 ? 21.138  -0.620  53.052  1.00 47.74  ? 109 ASN A O   1 
ATOM   853  C CB  . ASN A 1 109 ? 22.595  1.621   52.233  1.00 49.57  ? 109 ASN A CB  1 
ATOM   854  C CG  . ASN A 1 109 ? 23.646  1.396   53.300  1.00 52.14  ? 109 ASN A CG  1 
ATOM   855  O OD1 . ASN A 1 109 ? 23.364  1.503   54.505  1.00 53.45  ? 109 ASN A OD1 1 
ATOM   856  N ND2 . ASN A 1 109 ? 24.872  1.056   52.867  1.00 51.08  ? 109 ASN A ND2 1 
ATOM   857  N N   . ALA A 1 110 ? 19.927  0.578   54.540  1.00 47.07  ? 110 ALA A N   1 
ATOM   858  C CA  . ALA A 1 110 ? 19.410  -0.632  55.191  1.00 47.07  ? 110 ALA A CA  1 
ATOM   859  C C   . ALA A 1 110 ? 18.496  -1.396  54.252  1.00 46.36  ? 110 ALA A C   1 
ATOM   860  O O   . ALA A 1 110 ? 17.824  -0.796  53.418  1.00 47.88  ? 110 ALA A O   1 
ATOM   861  C CB  . ALA A 1 110 ? 18.649  -0.308  56.516  1.00 46.07  ? 110 ALA A CB  1 
ATOM   862  N N   . PRO A 1 111 ? 18.468  -2.716  54.388  1.00 45.94  ? 111 PRO A N   1 
ATOM   863  C CA  . PRO A 1 111 ? 17.486  -3.493  53.667  1.00 46.65  ? 111 PRO A CA  1 
ATOM   864  C C   . PRO A 1 111 ? 16.066  -3.086  54.021  1.00 47.26  ? 111 PRO A C   1 
ATOM   865  O O   . PRO A 1 111 ? 15.750  -2.824  55.196  1.00 46.49  ? 111 PRO A O   1 
ATOM   866  C CB  . PRO A 1 111 ? 17.765  -4.916  54.111  1.00 46.37  ? 111 PRO A CB  1 
ATOM   867  C CG  . PRO A 1 111 ? 19.084  -4.901  54.777  1.00 46.58  ? 111 PRO A CG  1 
ATOM   868  C CD  . PRO A 1 111 ? 19.358  -3.546  55.205  1.00 45.15  ? 111 PRO A CD  1 
ATOM   869  N N   . ILE A 1 112 ? 15.202  -3.030  52.998  1.00 46.77  ? 112 ILE A N   1 
ATOM   870  C CA  . ILE A 1 112 ? 13.835  -2.690  53.217  1.00 45.53  ? 112 ILE A CA  1 
ATOM   871  C C   . ILE A 1 112 ? 13.113  -3.960  53.622  1.00 44.71  ? 112 ILE A C   1 
ATOM   872  O O   . ILE A 1 112 ? 13.557  -5.096  53.332  1.00 44.66  ? 112 ILE A O   1 
ATOM   873  C CB  . ILE A 1 112 ? 13.181  -1.968  51.984  1.00 46.58  ? 112 ILE A CB  1 
ATOM   874  C CG1 . ILE A 1 112 ? 13.059  -2.953  50.785  1.00 47.53  ? 112 ILE A CG1 1 
ATOM   875  C CG2 . ILE A 1 112 ? 13.946  -0.647  51.639  1.00 46.72  ? 112 ILE A CG2 1 
ATOM   876  C CD1 . ILE A 1 112 ? 11.714  -2.805  50.001  1.00 46.50  ? 112 ILE A CD1 1 
ATOM   877  N N   . GLY A 1 113 ? 11.979  -3.789  54.288  1.00 44.56  ? 113 GLY A N   1 
ATOM   878  C CA  . GLY A 1 113 ? 11.180  -4.925  54.697  1.00 43.93  ? 113 GLY A CA  1 
ATOM   879  C C   . GLY A 1 113 ? 10.632  -4.799  56.113  1.00 44.77  ? 113 GLY A C   1 
ATOM   880  O O   . GLY A 1 113 ? 10.747  -3.740  56.739  1.00 44.92  ? 113 GLY A O   1 
ATOM   881  N N   . LEU A 1 114 ? 9.969   -5.860  56.545  1.00 44.23  ? 114 LEU A N   1 
ATOM   882  C CA  . LEU A 1 114 ? 9.435   -5.994  57.901  1.00 44.72  ? 114 LEU A CA  1 
ATOM   883  C C   . LEU A 1 114 ? 10.550  -6.328  58.896  1.00 44.99  ? 114 LEU A C   1 
ATOM   884  O O   . LEU A 1 114 ? 11.236  -7.335  58.715  1.00 43.34  ? 114 LEU A O   1 
ATOM   885  C CB  . LEU A 1 114 ? 8.444   -7.142  57.936  1.00 43.94  ? 114 LEU A CB  1 
ATOM   886  C CG  . LEU A 1 114 ? 7.826   -7.472  59.292  1.00 44.03  ? 114 LEU A CG  1 
ATOM   887  C CD1 . LEU A 1 114 ? 7.015   -6.262  59.752  1.00 41.01  ? 114 LEU A CD1 1 
ATOM   888  C CD2 . LEU A 1 114 ? 6.958   -8.713  59.187  1.00 42.17  ? 114 LEU A CD2 1 
ATOM   889  N N   . TYR A 1 115 ? 10.701  -5.480  59.928  1.00 46.27  ? 115 TYR A N   1 
ATOM   890  C CA  . TYR A 1 115 ? 11.651  -5.724  61.039  1.00 45.90  ? 115 TYR A CA  1 
ATOM   891  C C   . TYR A 1 115 ? 10.925  -5.988  62.365  1.00 46.21  ? 115 TYR A C   1 
ATOM   892  O O   . TYR A 1 115 ? 9.868   -5.415  62.613  1.00 44.56  ? 115 TYR A O   1 
ATOM   893  C CB  . TYR A 1 115 ? 12.526  -4.519  61.234  1.00 46.00  ? 115 TYR A CB  1 
ATOM   894  C CG  . TYR A 1 115 ? 13.628  -4.305  60.219  1.00 46.18  ? 115 TYR A CG  1 
ATOM   895  C CD1 . TYR A 1 115 ? 13.374  -3.644  59.016  1.00 49.28  ? 115 TYR A CD1 1 
ATOM   896  C CD2 . TYR A 1 115 ? 14.916  -4.705  60.476  1.00 47.18  ? 115 TYR A CD2 1 
ATOM   897  C CE1 . TYR A 1 115 ? 14.398  -3.392  58.093  1.00 48.55  ? 115 TYR A CE1 1 
ATOM   898  C CE2 . TYR A 1 115 ? 15.952  -4.460  59.572  1.00 48.63  ? 115 TYR A CE2 1 
ATOM   899  C CZ  . TYR A 1 115 ? 15.677  -3.816  58.365  1.00 48.47  ? 115 TYR A CZ  1 
ATOM   900  O OH  . TYR A 1 115 ? 16.693  -3.577  57.458  1.00 48.07  ? 115 TYR A OH  1 
ATOM   901  N N   . ARG A 1 116 ? 11.482  -6.897  63.164  1.00 46.33  ? 116 ARG A N   1 
ATOM   902  C CA  . ARG A 1 116 ? 11.073  -7.085  64.571  1.00 46.88  ? 116 ARG A CA  1 
ATOM   903  C C   . ARG A 1 116 ? 12.060  -6.328  65.445  1.00 46.65  ? 116 ARG A C   1 
ATOM   904  O O   . ARG A 1 116 ? 13.279  -6.541  65.325  1.00 45.60  ? 116 ARG A O   1 
ATOM   905  C CB  . ARG A 1 116 ? 11.067  -8.560  64.944  1.00 47.39  ? 116 ARG A CB  1 
ATOM   906  C CG  . ARG A 1 116 ? 10.535  -8.853  66.336  1.00 47.55  ? 116 ARG A CG  1 
ATOM   907  C CD  . ARG A 1 116 ? 10.726  -10.278 66.629  1.00 50.01  ? 116 ARG A CD  1 
ATOM   908  N NE  . ARG A 1 116 ? 12.138  -10.552 66.884  1.00 54.66  ? 116 ARG A NE  1 
ATOM   909  C CZ  . ARG A 1 116 ? 12.715  -11.741 66.736  1.00 56.60  ? 116 ARG A CZ  1 
ATOM   910  N NH1 . ARG A 1 116 ? 12.015  -12.785 66.285  1.00 58.14  ? 116 ARG A NH1 1 
ATOM   911  N NH2 . ARG A 1 116 ? 14.013  -11.887 67.023  1.00 57.47  ? 116 ARG A NH2 1 
ATOM   912  N N   . LEU A 1 117 ? 11.516  -5.442  66.297  1.00 46.69  ? 117 LEU A N   1 
ATOM   913  C CA  . LEU A 1 117 ? 12.283  -4.625  67.226  1.00 46.01  ? 117 LEU A CA  1 
ATOM   914  C C   . LEU A 1 117 ? 12.173  -5.200  68.646  1.00 45.83  ? 117 LEU A C   1 
ATOM   915  O O   . LEU A 1 117 ? 11.074  -5.362  69.189  1.00 44.37  ? 117 LEU A O   1 
ATOM   916  C CB  . LEU A 1 117 ? 11.759  -3.180  67.216  1.00 45.84  ? 117 LEU A CB  1 
ATOM   917  C CG  . LEU A 1 117 ? 12.445  -2.168  68.145  1.00 46.30  ? 117 LEU A CG  1 
ATOM   918  C CD1 . LEU A 1 117 ? 13.936  -2.000  67.842  1.00 46.02  ? 117 LEU A CD1 1 
ATOM   919  C CD2 . LEU A 1 117 ? 11.749  -0.836  68.037  1.00 44.91  ? 117 LEU A CD2 1 
ATOM   920  N N   . SER A 1 118 ? 13.328  -5.503  69.221  1.00 46.20  ? 118 SER A N   1 
ATOM   921  C CA  . SER A 1 118 ? 13.418  -6.066  70.550  1.00 46.36  ? 118 SER A CA  1 
ATOM   922  C C   . SER A 1 118 ? 14.260  -5.158  71.444  1.00 46.64  ? 118 SER A C   1 
ATOM   923  O O   . SER A 1 118 ? 15.143  -4.436  70.963  1.00 46.69  ? 118 SER A O   1 
ATOM   924  C CB  . SER A 1 118 ? 14.034  -7.456  70.485  1.00 45.64  ? 118 SER A CB  1 
ATOM   925  O OG  . SER A 1 118 ? 13.102  -8.372  69.960  1.00 47.78  ? 118 SER A OG  1 
ATOM   926  N N   . LEU A 1 119 ? 13.996  -5.217  72.754  1.00 46.80  ? 119 LEU A N   1 
ATOM   927  C CA  . LEU A 1 119 ? 14.713  -4.380  73.727  1.00 46.96  ? 119 LEU A CA  1 
ATOM   928  C C   . LEU A 1 119 ? 15.231  -5.250  74.860  1.00 46.82  ? 119 LEU A C   1 
ATOM   929  O O   . LEU A 1 119 ? 14.518  -6.111  75.359  1.00 45.64  ? 119 LEU A O   1 
ATOM   930  C CB  . LEU A 1 119 ? 13.784  -3.296  74.280  1.00 47.29  ? 119 LEU A CB  1 
ATOM   931  C CG  . LEU A 1 119 ? 14.260  -2.446  75.476  1.00 46.98  ? 119 LEU A CG  1 
ATOM   932  C CD1 . LEU A 1 119 ? 15.446  -1.561  75.094  1.00 46.02  ? 119 LEU A CD1 1 
ATOM   933  C CD2 . LEU A 1 119 ? 13.074  -1.599  75.992  1.00 46.50  ? 119 LEU A CD2 1 
ATOM   934  N N   . GLU A 1 120 ? 16.504  -5.064  75.179  1.00 48.11  ? 120 GLU A N   1 
ATOM   935  C CA  . GLU A 1 120 ? 17.100  -5.575  76.409  1.00 48.72  ? 120 GLU A CA  1 
ATOM   936  C C   . GLU A 1 120 ? 17.360  -4.396  77.338  1.00 48.70  ? 120 GLU A C   1 
ATOM   937  O O   . GLU A 1 120 ? 17.968  -3.413  76.943  1.00 47.19  ? 120 GLU A O   1 
ATOM   938  C CB  . GLU A 1 120 ? 18.426  -6.255  76.116  1.00 48.50  ? 120 GLU A CB  1 
ATOM   939  C CG  . GLU A 1 120 ? 18.944  -7.037  77.269  1.00 50.63  ? 120 GLU A CG  1 
ATOM   940  C CD  . GLU A 1 120 ? 20.206  -7.817  76.932  1.00 53.15  ? 120 GLU A CD  1 
ATOM   941  O OE1 . GLU A 1 120 ? 20.579  -7.883  75.725  1.00 60.37  ? 120 GLU A OE1 1 
ATOM   942  O OE2 . GLU A 1 120 ? 20.816  -8.355  77.882  1.00 59.02  ? 120 GLU A OE2 1 
ATOM   943  N N   . ALA A 1 121 ? 16.890  -4.508  78.577  1.00 48.91  ? 121 ALA A N   1 
ATOM   944  C CA  . ALA A 1 121 ? 17.120  -3.486  79.589  1.00 48.93  ? 121 ALA A CA  1 
ATOM   945  C C   . ALA A 1 121 ? 17.939  -4.169  80.678  1.00 48.96  ? 121 ALA A C   1 
ATOM   946  O O   . ALA A 1 121 ? 17.597  -5.274  81.124  1.00 48.29  ? 121 ALA A O   1 
ATOM   947  C CB  . ALA A 1 121 ? 15.802  -2.979  80.138  1.00 49.26  ? 121 ALA A CB  1 
ATOM   948  N N   . SER A 1 122 ? 19.055  -3.549  81.051  1.00 48.90  ? 122 SER A N   1 
ATOM   949  C CA  . SER A 1 122 ? 19.911  -4.111  82.072  1.00 49.22  ? 122 SER A CA  1 
ATOM   950  C C   . SER A 1 122 ? 20.199  -3.114  83.178  1.00 49.44  ? 122 SER A C   1 
ATOM   951  O O   . SER A 1 122 ? 20.667  -2.001  82.916  1.00 47.92  ? 122 SER A O   1 
ATOM   952  C CB  . SER A 1 122 ? 21.218  -4.581  81.478  1.00 49.05  ? 122 SER A CB  1 
ATOM   953  O OG  . SER A 1 122 ? 21.875  -5.373  82.441  1.00 50.80  ? 122 SER A OG  1 
ATOM   954  N N   . THR A 1 123 ? 19.915  -3.543  84.408  1.00 49.99  ? 123 THR A N   1 
ATOM   955  C CA  . THR A 1 123 ? 20.160  -2.755  85.598  1.00 50.73  ? 123 THR A CA  1 
ATOM   956  C C   . THR A 1 123 ? 21.114  -3.541  86.442  1.00 51.47  ? 123 THR A C   1 
ATOM   957  O O   . THR A 1 123 ? 20.755  -4.596  86.995  1.00 50.80  ? 123 THR A O   1 
ATOM   958  C CB  . THR A 1 123 ? 18.865  -2.502  86.373  1.00 50.41  ? 123 THR A CB  1 
ATOM   959  O OG1 . THR A 1 123 ? 17.910  -1.903  85.491  1.00 51.32  ? 123 THR A OG1 1 
ATOM   960  C CG2 . THR A 1 123 ? 19.109  -1.568  87.532  1.00 50.22  ? 123 THR A CG2 1 
ATOM   961  N N   . GLY A 1 124 ? 22.348  -3.045  86.501  1.00 52.91  ? 124 GLY A N   1 
ATOM   962  C CA  . GLY A 1 124 ? 23.376  -3.609  87.359  1.00 53.74  ? 124 GLY A CA  1 
ATOM   963  C C   . GLY A 1 124 ? 23.667  -5.051  87.002  1.00 54.73  ? 124 GLY A C   1 
ATOM   964  O O   . GLY A 1 124 ? 24.069  -5.350  85.869  1.00 55.06  ? 124 GLY A O   1 
ATOM   965  N N   . TYR A 1 125 ? 23.421  -5.942  87.959  1.00 55.36  ? 125 TYR A N   1 
ATOM   966  C CA  . TYR A 1 125 ? 23.750  -7.353  87.809  1.00 56.02  ? 125 TYR A CA  1 
ATOM   967  C C   . TYR A 1 125 ? 22.620  -8.197  87.214  1.00 56.55  ? 125 TYR A C   1 
ATOM   968  O O   . TYR A 1 125 ? 22.566  -9.411  87.483  1.00 57.45  ? 125 TYR A O   1 
ATOM   969  C CB  . TYR A 1 125 ? 24.069  -7.957  89.173  1.00 56.52  ? 125 TYR A CB  1 
ATOM   970  C CG  . TYR A 1 125 ? 25.266  -7.390  89.884  1.00 57.30  ? 125 TYR A CG  1 
ATOM   971  C CD1 . TYR A 1 125 ? 26.557  -7.560  89.374  1.00 57.99  ? 125 TYR A CD1 1 
ATOM   972  C CD2 . TYR A 1 125 ? 25.116  -6.729  91.107  1.00 57.17  ? 125 TYR A CD2 1 
ATOM   973  C CE1 . TYR A 1 125 ? 27.676  -7.056  90.064  1.00 57.79  ? 125 TYR A CE1 1 
ATOM   974  C CE2 . TYR A 1 125 ? 26.206  -6.222  91.790  1.00 57.45  ? 125 TYR A CE2 1 
ATOM   975  C CZ  . TYR A 1 125 ? 27.485  -6.384  91.275  1.00 57.66  ? 125 TYR A CZ  1 
ATOM   976  O OH  . TYR A 1 125 ? 28.554  -5.871  91.988  1.00 57.87  ? 125 TYR A OH  1 
ATOM   977  N N   . GLN A 1 126 ? 21.700  -7.580  86.475  1.00 56.12  ? 126 GLN A N   1 
ATOM   978  C CA  . GLN A 1 126 ? 20.540  -8.298  85.930  1.00 55.93  ? 126 GLN A CA  1 
ATOM   979  C C   . GLN A 1 126 ? 20.082  -7.671  84.633  1.00 55.79  ? 126 GLN A C   1 
ATOM   980  O O   . GLN A 1 126 ? 20.235  -6.461  84.421  1.00 55.56  ? 126 GLN A O   1 
ATOM   981  C CB  . GLN A 1 126 ? 19.354  -8.312  86.915  1.00 55.67  ? 126 GLN A CB  1 
ATOM   982  C CG  . GLN A 1 126 ? 19.632  -8.904  88.320  1.00 55.28  ? 126 GLN A CG  1 
ATOM   983  C CD  . GLN A 1 126 ? 20.009  -10.394 88.345  1.00 54.64  ? 126 GLN A CD  1 
ATOM   984  O OE1 . GLN A 1 126 ? 20.533  -10.894 89.347  1.00 53.20  ? 126 GLN A OE1 1 
ATOM   985  N NE2 . GLN A 1 126 ? 19.743  -11.096 87.262  1.00 54.42  ? 126 GLN A NE2 1 
ATOM   986  N N   . GLY A 1 127 ? 19.493  -8.508  83.781  1.00 56.00  ? 127 GLY A N   1 
ATOM   987  C CA  . GLY A 1 127 ? 19.017  -8.100  82.473  1.00 56.21  ? 127 GLY A CA  1 
ATOM   988  C C   . GLY A 1 127 ? 17.744  -8.816  82.061  1.00 56.49  ? 127 GLY A C   1 
ATOM   989  O O   . GLY A 1 127 ? 17.441  -9.909  82.548  1.00 55.64  ? 127 GLY A O   1 
ATOM   990  N N   . SER A 1 128 ? 16.997  -8.184  81.159  1.00 56.35  ? 128 SER A N   1 
ATOM   991  C CA  . SER A 1 128 ? 15.737  -8.730  80.662  1.00 56.46  ? 128 SER A CA  1 
ATOM   992  C C   . SER A 1 128 ? 15.510  -8.238  79.232  1.00 56.11  ? 128 SER A C   1 
ATOM   993  O O   . SER A 1 128 ? 15.666  -7.039  78.960  1.00 56.30  ? 128 SER A O   1 
ATOM   994  C CB  . SER A 1 128 ? 14.588  -8.269  81.550  1.00 57.16  ? 128 SER A CB  1 
ATOM   995  O OG  . SER A 1 128 ? 14.429  -6.862  81.455  1.00 59.44  ? 128 SER A OG  1 
ATOM   996  N N   . SER A 1 129 ? 15.137  -9.165  78.345  1.00 55.17  ? 129 SER A N   1 
ATOM   997  C CA  . SER A 1 129 ? 15.058  -8.915  76.905  1.00 54.73  ? 129 SER A CA  1 
ATOM   998  C C   . SER A 1 129 ? 13.730  -9.350  76.346  1.00 53.74  ? 129 SER A C   1 
ATOM   999  O O   . SER A 1 129 ? 13.232  -10.405 76.721  1.00 54.26  ? 129 SER A O   1 
ATOM   1000 C CB  . SER A 1 129 ? 16.160  -9.670  76.168  1.00 54.97  ? 129 SER A CB  1 
ATOM   1001 O OG  . SER A 1 129 ? 16.137  -9.332  74.780  1.00 57.61  ? 129 SER A OG  1 
ATOM   1002 N N   . PHE A 1 130 ? 13.176  -8.560  75.421  1.00 52.57  ? 130 PHE A N   1 
ATOM   1003 C CA  . PHE A 1 130 ? 11.836  -8.820  74.896  1.00 51.17  ? 130 PHE A CA  1 
ATOM   1004 C C   . PHE A 1 130 ? 11.451  -7.984  73.671  1.00 49.52  ? 130 PHE A C   1 
ATOM   1005 O O   . PHE A 1 130 ? 12.073  -6.968  73.386  1.00 48.59  ? 130 PHE A O   1 
ATOM   1006 C CB  . PHE A 1 130 ? 10.802  -8.544  75.977  1.00 51.94  ? 130 PHE A CB  1 
ATOM   1007 C CG  . PHE A 1 130 ? 10.818  -7.140  76.452  1.00 51.99  ? 130 PHE A CG  1 
ATOM   1008 C CD1 . PHE A 1 130 ? 11.637  -6.767  77.522  1.00 54.63  ? 130 PHE A CD1 1 
ATOM   1009 C CD2 . PHE A 1 130 ? 10.007  -6.208  75.881  1.00 50.73  ? 130 PHE A CD2 1 
ATOM   1010 C CE1 . PHE A 1 130 ? 11.645  -5.475  77.982  1.00 53.55  ? 130 PHE A CE1 1 
ATOM   1011 C CE2 . PHE A 1 130 ? 10.022  -4.914  76.317  1.00 52.74  ? 130 PHE A CE2 1 
ATOM   1012 C CZ  . PHE A 1 130 ? 10.839  -4.543  77.376  1.00 54.05  ? 130 PHE A CZ  1 
ATOM   1013 N N   . VAL A 1 131 ? 10.362  -8.410  73.026  1.00 47.46  ? 131 VAL A N   1 
ATOM   1014 C CA  . VAL A 1 131 ? 9.897   -7.868  71.753  1.00 46.31  ? 131 VAL A CA  1 
ATOM   1015 C C   . VAL A 1 131 ? 9.080   -6.590  72.005  1.00 45.85  ? 131 VAL A C   1 
ATOM   1016 O O   . VAL A 1 131 ? 8.092   -6.635  72.749  1.00 45.45  ? 131 VAL A O   1 
ATOM   1017 C CB  . VAL A 1 131 ? 9.039   -8.914  70.975  1.00 46.13  ? 131 VAL A CB  1 
ATOM   1018 C CG1 . VAL A 1 131 ? 8.612   -8.358  69.612  1.00 40.24  ? 131 VAL A CG1 1 
ATOM   1019 C CG2 . VAL A 1 131 ? 9.804   -10.221 70.788  1.00 44.06  ? 131 VAL A CG2 1 
ATOM   1020 N N   . LEU A 1 132 ? 9.554   -5.462  71.472  1.00 44.38  ? 132 LEU A N   1 
ATOM   1021 C CA  . LEU A 1 132 ? 8.826   -4.182  71.514  1.00 45.58  ? 132 LEU A CA  1 
ATOM   1022 C C   . LEU A 1 132 ? 7.742   -4.066  70.498  1.00 46.14  ? 132 LEU A C   1 
ATOM   1023 O O   . LEU A 1 132 ? 6.677   -3.524  70.773  1.00 46.20  ? 132 LEU A O   1 
ATOM   1024 C CB  . LEU A 1 132 ? 9.730   -2.995  71.257  1.00 45.45  ? 132 LEU A CB  1 
ATOM   1025 C CG  . LEU A 1 132 ? 10.545  -2.489  72.419  1.00 47.08  ? 132 LEU A CG  1 
ATOM   1026 C CD1 . LEU A 1 132 ? 11.340  -1.306  71.950  1.00 44.46  ? 132 LEU A CD1 1 
ATOM   1027 C CD2 . LEU A 1 132 ? 9.587   -2.149  73.614  1.00 46.06  ? 132 LEU A CD2 1 
ATOM   1028 N N   . GLY A 1 133 ? 8.048   -4.512  69.271  1.00 46.27  ? 133 GLY A N   1 
ATOM   1029 C CA  . GLY A 1 133 ? 7.053   -4.551  68.216  1.00 45.60  ? 133 GLY A CA  1 
ATOM   1030 C C   . GLY A 1 133 ? 7.728   -4.770  66.869  1.00 45.48  ? 133 GLY A C   1 
ATOM   1031 O O   . GLY A 1 133 ? 8.795   -5.374  66.793  1.00 44.14  ? 133 GLY A O   1 
ATOM   1032 N N   . HIS A 1 134 ? 7.101   -4.234  65.831  1.00 45.74  ? 134 HIS A N   1 
ATOM   1033 C CA  . HIS A 1 134 ? 7.578   -4.393  64.456  1.00 45.42  ? 134 HIS A CA  1 
ATOM   1034 C C   . HIS A 1 134 ? 7.438   -3.070  63.779  1.00 45.60  ? 134 HIS A C   1 
ATOM   1035 O O   . HIS A 1 134 ? 6.643   -2.215  64.215  1.00 45.15  ? 134 HIS A O   1 
ATOM   1036 C CB  . HIS A 1 134 ? 6.723   -5.402  63.689  1.00 45.36  ? 134 HIS A CB  1 
ATOM   1037 C CG  . HIS A 1 134 ? 6.868   -6.810  64.157  1.00 45.41  ? 134 HIS A CG  1 
ATOM   1038 N ND1 . HIS A 1 134 ? 7.548   -7.762  63.432  1.00 47.77  ? 134 HIS A ND1 1 
ATOM   1039 C CD2 . HIS A 1 134 ? 6.392   -7.444  65.254  1.00 44.05  ? 134 HIS A CD2 1 
ATOM   1040 C CE1 . HIS A 1 134 ? 7.502   -8.917  64.071  1.00 47.31  ? 134 HIS A CE1 1 
ATOM   1041 N NE2 . HIS A 1 134 ? 6.830   -8.742  65.193  1.00 46.82  ? 134 HIS A NE2 1 
ATOM   1042 N N   . PHE A 1 135 ? 8.194   -2.898  62.693  1.00 45.50  ? 135 PHE A N   1 
ATOM   1043 C CA  . PHE A 1 135 ? 7.969   -1.803  61.763  1.00 45.04  ? 135 PHE A CA  1 
ATOM   1044 C C   . PHE A 1 135 ? 8.377   -2.233  60.361  1.00 44.97  ? 135 PHE A C   1 
ATOM   1045 O O   . PHE A 1 135 ? 9.201   -3.131  60.193  1.00 44.73  ? 135 PHE A O   1 
ATOM   1046 C CB  . PHE A 1 135 ? 8.745   -0.559  62.135  1.00 44.92  ? 135 PHE A CB  1 
ATOM   1047 C CG  . PHE A 1 135 ? 10.228  -0.751  62.231  1.00 46.32  ? 135 PHE A CG  1 
ATOM   1048 C CD1 . PHE A 1 135 ? 11.068  -0.396  61.189  1.00 44.34  ? 135 PHE A CD1 1 
ATOM   1049 C CD2 . PHE A 1 135 ? 10.804  -1.222  63.390  1.00 45.38  ? 135 PHE A CD2 1 
ATOM   1050 C CE1 . PHE A 1 135 ? 12.420  -0.545  61.273  1.00 43.63  ? 135 PHE A CE1 1 
ATOM   1051 C CE2 . PHE A 1 135 ? 12.157  -1.345  63.492  1.00 43.42  ? 135 PHE A CE2 1 
ATOM   1052 C CZ  . PHE A 1 135 ? 12.978  -1.020  62.464  1.00 46.54  ? 135 PHE A CZ  1 
ATOM   1053 N N   . ILE A 1 136 ? 7.808   -1.575  59.374  1.00 45.73  ? 136 ILE A N   1 
ATOM   1054 C CA  . ILE A 1 136 ? 8.211   -1.834  57.965  1.00 45.64  ? 136 ILE A CA  1 
ATOM   1055 C C   . ILE A 1 136 ? 9.020   -0.648  57.527  1.00 44.93  ? 136 ILE A C   1 
ATOM   1056 O O   . ILE A 1 136 ? 8.644   0.496   57.793  1.00 45.82  ? 136 ILE A O   1 
ATOM   1057 C CB  . ILE A 1 136 ? 6.995   -2.122  57.045  1.00 46.51  ? 136 ILE A CB  1 
ATOM   1058 C CG1 . ILE A 1 136 ? 6.298   -3.344  57.548  1.00 45.21  ? 136 ILE A CG1 1 
ATOM   1059 C CG2 . ILE A 1 136 ? 7.478   -2.336  55.579  1.00 47.11  ? 136 ILE A CG2 1 
ATOM   1060 C CD1 . ILE A 1 136 ? 4.987   -3.758  56.832  1.00 44.96  ? 136 ILE A CD1 1 
ATOM   1061 N N   . LEU A 1 137 ? 10.189  -0.933  56.935  1.00 44.01  ? 137 LEU A N   1 
ATOM   1062 C CA  . LEU A 1 137 ? 11.131  0.064   56.526  1.00 44.51  ? 137 LEU A CA  1 
ATOM   1063 C C   . LEU A 1 137 ? 11.164  0.155   54.994  1.00 44.55  ? 137 LEU A C   1 
ATOM   1064 O O   . LEU A 1 137 ? 11.380  -0.850  54.352  1.00 44.74  ? 137 LEU A O   1 
ATOM   1065 C CB  . LEU A 1 137 ? 12.530  -0.348  56.999  1.00 43.54  ? 137 LEU A CB  1 
ATOM   1066 C CG  . LEU A 1 137 ? 13.624  0.714   56.843  1.00 43.70  ? 137 LEU A CG  1 
ATOM   1067 C CD1 . LEU A 1 137 ? 13.309  1.911   57.609  1.00 44.89  ? 137 LEU A CD1 1 
ATOM   1068 C CD2 . LEU A 1 137 ? 14.979  0.113   57.244  1.00 44.36  ? 137 LEU A CD2 1 
ATOM   1069 N N   . LEU A 1 138 ? 11.015  1.354   54.451  1.00 45.80  ? 138 LEU A N   1 
ATOM   1070 C CA  . LEU A 1 138 ? 10.915  1.537   52.978  1.00 45.64  ? 138 LEU A CA  1 
ATOM   1071 C C   . LEU A 1 138 ? 11.979  2.455   52.457  1.00 46.76  ? 138 LEU A C   1 
ATOM   1072 O O   . LEU A 1 138 ? 12.686  3.100   53.227  1.00 45.29  ? 138 LEU A O   1 
ATOM   1073 C CB  . LEU A 1 138 ? 9.531   2.066   52.599  1.00 44.95  ? 138 LEU A CB  1 
ATOM   1074 C CG  . LEU A 1 138 ? 8.340   1.208   53.017  1.00 45.02  ? 138 LEU A CG  1 
ATOM   1075 C CD1 . LEU A 1 138 ? 6.986   1.847   52.678  1.00 47.44  ? 138 LEU A CD1 1 
ATOM   1076 C CD2 . LEU A 1 138 ? 8.462   -0.108  52.361  1.00 43.25  ? 138 LEU A CD2 1 
ATOM   1077 N N   . PHE A 1 139 ? 12.086  2.541   51.119  1.00 46.92  ? 139 PHE A N   1 
ATOM   1078 C CA  . PHE A 1 139 ? 13.056  3.440   50.475  1.00 46.15  ? 139 PHE A CA  1 
ATOM   1079 C C   . PHE A 1 139 ? 12.631  4.857   50.708  1.00 45.92  ? 139 PHE A C   1 
ATOM   1080 O O   . PHE A 1 139 ? 11.446  5.142   50.804  1.00 46.55  ? 139 PHE A O   1 
ATOM   1081 C CB  . PHE A 1 139 ? 13.145  3.201   48.935  1.00 46.18  ? 139 PHE A CB  1 
ATOM   1082 C CG  . PHE A 1 139 ? 13.743  1.870   48.542  1.00 42.80  ? 139 PHE A CG  1 
ATOM   1083 C CD1 . PHE A 1 139 ? 15.120  1.686   48.551  1.00 43.98  ? 139 PHE A CD1 1 
ATOM   1084 C CD2 . PHE A 1 139 ? 12.956  0.846   48.151  1.00 46.08  ? 139 PHE A CD2 1 
ATOM   1085 C CE1 . PHE A 1 139 ? 15.671  0.470   48.195  1.00 44.21  ? 139 PHE A CE1 1 
ATOM   1086 C CE2 . PHE A 1 139 ? 13.492  -0.375  47.762  1.00 44.48  ? 139 PHE A CE2 1 
ATOM   1087 C CZ  . PHE A 1 139 ? 14.844  -0.563  47.789  1.00 44.95  ? 139 PHE A CZ  1 
ATOM   1088 N N   . ASN A 1 140 ? 13.595  5.770   50.748  1.00 46.03  ? 140 ASN A N   1 
ATOM   1089 C CA  . ASN A 1 140 ? 13.319  7.121   51.158  1.00 47.05  ? 140 ASN A CA  1 
ATOM   1090 C C   . ASN A 1 140 ? 13.823  8.137   50.125  1.00 47.47  ? 140 ASN A C   1 
ATOM   1091 O O   . ASN A 1 140 ? 14.985  8.507   50.095  1.00 47.67  ? 140 ASN A O   1 
ATOM   1092 C CB  . ASN A 1 140 ? 13.979  7.380   52.530  1.00 46.41  ? 140 ASN A CB  1 
ATOM   1093 C CG  . ASN A 1 140 ? 13.395  8.564   53.237  1.00 49.13  ? 140 ASN A CG  1 
ATOM   1094 O OD1 . ASN A 1 140 ? 12.699  9.366   52.623  1.00 49.32  ? 140 ASN A OD1 1 
ATOM   1095 N ND2 . ASN A 1 140 ? 13.723  8.728   54.548  1.00 46.58  ? 140 ASN A ND2 1 
ATOM   1096 N N   . ALA A 1 141 ? 12.907  8.586   49.284  1.00 48.32  ? 141 ALA A N   1 
ATOM   1097 C CA  . ALA A 1 141 ? 13.211  9.548   48.244  1.00 48.06  ? 141 ALA A CA  1 
ATOM   1098 C C   . ALA A 1 141 ? 13.433  10.934  48.827  1.00 48.43  ? 141 ALA A C   1 
ATOM   1099 O O   . ALA A 1 141 ? 13.898  11.826  48.133  1.00 47.02  ? 141 ALA A O   1 
ATOM   1100 C CB  . ALA A 1 141 ? 12.093  9.557   47.219  1.00 46.97  ? 141 ALA A CB  1 
ATOM   1101 N N   . TRP A 1 142 ? 13.122  11.111  50.129  1.00 49.39  ? 142 TRP A N   1 
ATOM   1102 C CA  . TRP A 1 142 ? 13.376  12.388  50.806  1.00 48.98  ? 142 TRP A CA  1 
ATOM   1103 C C   . TRP A 1 142 ? 14.747  12.461  51.470  1.00 49.22  ? 142 TRP A C   1 
ATOM   1104 O O   . TRP A 1 142 ? 15.179  13.522  51.892  1.00 48.94  ? 142 TRP A O   1 
ATOM   1105 C CB  . TRP A 1 142 ? 12.292  12.667  51.860  1.00 49.12  ? 142 TRP A CB  1 
ATOM   1106 C CG  . TRP A 1 142 ? 10.938  12.946  51.263  1.00 47.80  ? 142 TRP A CG  1 
ATOM   1107 C CD1 . TRP A 1 142 ? 10.370  14.159  51.098  1.00 47.23  ? 142 TRP A CD1 1 
ATOM   1108 C CD2 . TRP A 1 142 ? 9.996   11.983  50.777  1.00 46.37  ? 142 TRP A CD2 1 
ATOM   1109 N NE1 . TRP A 1 142 ? 9.118   14.020  50.537  1.00 48.82  ? 142 TRP A NE1 1 
ATOM   1110 C CE2 . TRP A 1 142 ? 8.879   12.691  50.314  1.00 46.91  ? 142 TRP A CE2 1 
ATOM   1111 C CE3 . TRP A 1 142 ? 9.994   10.584  50.678  1.00 47.45  ? 142 TRP A CE3 1 
ATOM   1112 C CZ2 . TRP A 1 142 ? 7.764   12.058  49.776  1.00 47.41  ? 142 TRP A CZ2 1 
ATOM   1113 C CZ3 . TRP A 1 142 ? 8.894   9.958   50.140  1.00 48.67  ? 142 TRP A CZ3 1 
ATOM   1114 C CH2 . TRP A 1 142 ? 7.802   10.696  49.674  1.00 47.94  ? 142 TRP A CH2 1 
ATOM   1115 N N   . CYS A 1 143 ? 15.427  11.333  51.577  1.00 49.91  ? 143 CYS A N   1 
ATOM   1116 C CA  . CYS A 1 143 ? 16.696  11.298  52.292  1.00 49.81  ? 143 CYS A CA  1 
ATOM   1117 C C   . CYS A 1 143 ? 17.877  11.493  51.354  1.00 49.57  ? 143 CYS A C   1 
ATOM   1118 O O   . CYS A 1 143 ? 18.081  10.692  50.473  1.00 49.56  ? 143 CYS A O   1 
ATOM   1119 C CB  . CYS A 1 143 ? 16.789  9.960   53.014  1.00 50.02  ? 143 CYS A CB  1 
ATOM   1120 S SG  . CYS A 1 143 ? 18.348  9.643   53.760  1.00 50.64  ? 143 CYS A SG  1 
ATOM   1121 N N   . PRO A 1 144 ? 18.642  12.585  51.503  1.00 49.10  ? 144 PRO A N   1 
ATOM   1122 C CA  . PRO A 1 144 ? 19.752  12.763  50.586  1.00 49.38  ? 144 PRO A CA  1 
ATOM   1123 C C   . PRO A 1 144 ? 20.704  11.598  50.421  1.00 49.43  ? 144 PRO A C   1 
ATOM   1124 O O   . PRO A 1 144 ? 21.325  11.495  49.368  1.00 49.56  ? 144 PRO A O   1 
ATOM   1125 C CB  . PRO A 1 144 ? 20.473  13.990  51.146  1.00 48.71  ? 144 PRO A CB  1 
ATOM   1126 C CG  . PRO A 1 144 ? 19.385  14.770  51.732  1.00 48.66  ? 144 PRO A CG  1 
ATOM   1127 C CD  . PRO A 1 144 ? 18.475  13.770  52.372  1.00 49.83  ? 144 PRO A CD  1 
ATOM   1128 N N   . ALA A 1 145 ? 20.833  10.738  51.432  1.00 48.72  ? 145 ALA A N   1 
ATOM   1129 C CA  . ALA A 1 145 ? 21.819  9.661   51.398  1.00 48.07  ? 145 ALA A CA  1 
ATOM   1130 C C   . ALA A 1 145 ? 21.252  8.387   50.792  1.00 47.60  ? 145 ALA A C   1 
ATOM   1131 O O   . ALA A 1 145 ? 21.995  7.459   50.590  1.00 46.16  ? 145 ALA A O   1 
ATOM   1132 C CB  . ALA A 1 145 ? 22.343  9.363   52.825  1.00 48.13  ? 145 ALA A CB  1 
ATOM   1133 N N   . ASP A 1 146 ? 19.941  8.347   50.565  1.00 46.73  ? 146 ASP A N   1 
ATOM   1134 C CA  . ASP A 1 146 ? 19.282  7.183   49.993  1.00 47.88  ? 146 ASP A CA  1 
ATOM   1135 C C   . ASP A 1 146 ? 19.516  7.188   48.460  1.00 48.12  ? 146 ASP A C   1 
ATOM   1136 O O   . ASP A 1 146 ? 19.519  8.251   47.848  1.00 47.56  ? 146 ASP A O   1 
ATOM   1137 C CB  . ASP A 1 146 ? 17.796  7.215   50.317  1.00 47.70  ? 146 ASP A CB  1 
ATOM   1138 C CG  . ASP A 1 146 ? 17.113  5.927   50.024  1.00 48.20  ? 146 ASP A CG  1 
ATOM   1139 O OD1 . ASP A 1 146 ? 17.417  5.313   48.957  1.00 49.53  ? 146 ASP A OD1 1 
ATOM   1140 O OD2 . ASP A 1 146 ? 16.242  5.493   50.844  1.00 48.84  ? 146 ASP A OD2 1 
ATOM   1141 N N   . ALA A 1 147 ? 19.811  6.000   47.913  1.00 48.13  ? 147 ALA A N   1 
ATOM   1142 C CA  . ALA A 1 147 ? 20.000  5.784   46.461  1.00 47.91  ? 147 ALA A CA  1 
ATOM   1143 C C   . ALA A 1 147 ? 18.828  6.308   45.614  1.00 48.05  ? 147 ALA A C   1 
ATOM   1144 O O   . ALA A 1 147 ? 19.039  6.751   44.469  1.00 47.83  ? 147 ALA A O   1 
ATOM   1145 C CB  . ALA A 1 147 ? 20.253  4.285   46.180  1.00 47.87  ? 147 ALA A CB  1 
ATOM   1146 N N   . VAL A 1 148 ? 17.604  6.277   46.168  1.00 47.95  ? 148 VAL A N   1 
ATOM   1147 C CA  . VAL A 1 148 ? 16.400  6.750   45.476  1.00 47.49  ? 148 VAL A CA  1 
ATOM   1148 C C   . VAL A 1 148 ? 16.100  8.257   45.667  1.00 47.82  ? 148 VAL A C   1 
ATOM   1149 O O   . VAL A 1 148 ? 15.037  8.717   45.291  1.00 47.02  ? 148 VAL A O   1 
ATOM   1150 C CB  . VAL A 1 148 ? 15.158  5.852   45.762  1.00 48.55  ? 148 VAL A CB  1 
ATOM   1151 C CG1 . VAL A 1 148 ? 15.467  4.377   45.400  1.00 47.29  ? 148 VAL A CG1 1 
ATOM   1152 C CG2 . VAL A 1 148 ? 14.655  5.940   47.235  1.00 47.18  ? 148 VAL A CG2 1 
ATOM   1153 N N   . TYR A 1 149 ? 17.019  9.019   46.271  1.00 46.89  ? 149 TYR A N   1 
ATOM   1154 C CA  . TYR A 1 149 ? 16.737  10.408  46.571  1.00 48.13  ? 149 TYR A CA  1 
ATOM   1155 C C   . TYR A 1 149 ? 16.385  11.141  45.287  1.00 48.69  ? 149 TYR A C   1 
ATOM   1156 O O   . TYR A 1 149 ? 17.038  10.922  44.251  1.00 47.60  ? 149 TYR A O   1 
ATOM   1157 C CB  . TYR A 1 149 ? 17.953  11.083  47.193  1.00 47.16  ? 149 TYR A CB  1 
ATOM   1158 C CG  . TYR A 1 149 ? 17.827  12.588  47.475  1.00 46.94  ? 149 TYR A CG  1 
ATOM   1159 C CD1 . TYR A 1 149 ? 16.966  13.074  48.468  1.00 48.77  ? 149 TYR A CD1 1 
ATOM   1160 C CD2 . TYR A 1 149 ? 18.598  13.505  46.789  1.00 47.66  ? 149 TYR A CD2 1 
ATOM   1161 C CE1 . TYR A 1 149 ? 16.878  14.433  48.763  1.00 44.71  ? 149 TYR A CE1 1 
ATOM   1162 C CE2 . TYR A 1 149 ? 18.520  14.880  47.070  1.00 46.99  ? 149 TYR A CE2 1 
ATOM   1163 C CZ  . TYR A 1 149 ? 17.658  15.329  48.071  1.00 46.23  ? 149 TYR A CZ  1 
ATOM   1164 O OH  . TYR A 1 149 ? 17.553  16.687  48.323  1.00 47.52  ? 149 TYR A OH  1 
ATOM   1165 N N   . LEU A 1 150 ? 15.369  11.990  45.408  1.00 49.97  ? 150 LEU A N   1 
ATOM   1166 C CA  . LEU A 1 150 ? 14.888  12.908  44.384  1.00 51.02  ? 150 LEU A CA  1 
ATOM   1167 C C   . LEU A 1 150 ? 14.987  14.267  44.998  1.00 51.30  ? 150 LEU A C   1 
ATOM   1168 O O   . LEU A 1 150 ? 14.433  14.493  46.056  1.00 51.90  ? 150 LEU A O   1 
ATOM   1169 C CB  . LEU A 1 150 ? 13.407  12.632  44.067  1.00 51.65  ? 150 LEU A CB  1 
ATOM   1170 C CG  . LEU A 1 150 ? 12.975  11.885  42.810  1.00 53.93  ? 150 LEU A CG  1 
ATOM   1171 C CD1 . LEU A 1 150 ? 11.465  11.624  42.880  1.00 55.32  ? 150 LEU A CD1 1 
ATOM   1172 C CD2 . LEU A 1 150 ? 13.349  12.696  41.575  1.00 50.20  ? 150 LEU A CD2 1 
ATOM   1173 N N   . ASP A 1 151 ? 15.673  15.198  44.355  1.00 52.06  ? 151 ASP A N   1 
ATOM   1174 C CA  . ASP A 1 151 ? 15.873  16.511  44.946  1.00 52.22  ? 151 ASP A CA  1 
ATOM   1175 C C   . ASP A 1 151 ? 14.678  17.448  44.896  1.00 52.51  ? 151 ASP A C   1 
ATOM   1176 O O   . ASP A 1 151 ? 14.769  18.598  45.349  1.00 53.72  ? 151 ASP A O   1 
ATOM   1177 C CB  . ASP A 1 151 ? 17.101  17.175  44.336  1.00 52.97  ? 151 ASP A CB  1 
ATOM   1178 C CG  . ASP A 1 151 ? 16.962  17.464  42.859  1.00 57.13  ? 151 ASP A CG  1 
ATOM   1179 O OD1 . ASP A 1 151 ? 15.841  17.799  42.399  1.00 63.90  ? 151 ASP A OD1 1 
ATOM   1180 O OD2 . ASP A 1 151 ? 18.007  17.416  42.154  1.00 63.58  ? 151 ASP A OD2 1 
ATOM   1181 N N   . SER A 1 152 ? 13.558  16.979  44.366  1.00 52.07  ? 152 SER A N   1 
ATOM   1182 C CA  . SER A 1 152 ? 12.412  17.840  44.085  1.00 51.31  ? 152 SER A CA  1 
ATOM   1183 C C   . SER A 1 152 ? 11.182  17.312  44.801  1.00 50.31  ? 152 SER A C   1 
ATOM   1184 O O   . SER A 1 152 ? 10.781  16.199  44.561  1.00 49.69  ? 152 SER A O   1 
ATOM   1185 C CB  . SER A 1 152 ? 12.151  17.826  42.566  1.00 51.71  ? 152 SER A CB  1 
ATOM   1186 O OG  . SER A 1 152 ? 10.872  18.337  42.237  1.00 52.82  ? 152 SER A OG  1 
ATOM   1187 N N   . GLU A 1 153 ? 10.566  18.125  45.651  1.00 49.42  ? 153 GLU A N   1 
ATOM   1188 C CA  . GLU A 1 153 ? 9.368   17.703  46.374  1.00 49.85  ? 153 GLU A CA  1 
ATOM   1189 C C   . GLU A 1 153 ? 8.213   17.371  45.426  1.00 49.29  ? 153 GLU A C   1 
ATOM   1190 O O   . GLU A 1 153 ? 7.486   16.428  45.643  1.00 48.13  ? 153 GLU A O   1 
ATOM   1191 C CB  . GLU A 1 153 ? 8.927   18.799  47.380  1.00 49.64  ? 153 GLU A CB  1 
ATOM   1192 C CG  . GLU A 1 153 ? 7.720   18.443  48.288  1.00 49.57  ? 153 GLU A CG  1 
ATOM   1193 C CD  . GLU A 1 153 ? 7.873   17.158  49.102  1.00 51.74  ? 153 GLU A CD  1 
ATOM   1194 O OE1 . GLU A 1 153 ? 6.826   16.608  49.503  1.00 54.27  ? 153 GLU A OE1 1 
ATOM   1195 O OE2 . GLU A 1 153 ? 9.000   16.656  49.325  1.00 50.99  ? 153 GLU A OE2 1 
ATOM   1196 N N   . GLU A 1 154 ? 8.017   18.183  44.398  1.00 50.07  ? 154 GLU A N   1 
ATOM   1197 C CA  . GLU A 1 154 ? 6.895   17.946  43.459  1.00 50.67  ? 154 GLU A CA  1 
ATOM   1198 C C   . GLU A 1 154 ? 7.035   16.603  42.750  1.00 49.39  ? 154 GLU A C   1 
ATOM   1199 O O   . GLU A 1 154 ? 6.050   15.932  42.518  1.00 49.29  ? 154 GLU A O   1 
ATOM   1200 C CB  . GLU A 1 154 ? 6.724   19.091  42.466  1.00 51.42  ? 154 GLU A CB  1 
ATOM   1201 C CG  . GLU A 1 154 ? 7.890   19.219  41.490  1.00 53.95  ? 154 GLU A CG  1 
ATOM   1202 C CD  . GLU A 1 154 ? 7.662   20.261  40.401  1.00 55.25  ? 154 GLU A CD  1 
ATOM   1203 O OE1 . GLU A 1 154 ? 6.688   21.051  40.504  1.00 59.75  ? 154 GLU A OE1 1 
ATOM   1204 O OE2 . GLU A 1 154 ? 8.471   20.264  39.431  1.00 62.56  ? 154 GLU A OE2 1 
ATOM   1205 N N   . GLU A 1 155 ? 8.260   16.181  42.465  1.00 48.97  ? 155 GLU A N   1 
ATOM   1206 C CA  . GLU A 1 155 ? 8.495   14.865  41.857  1.00 48.72  ? 155 GLU A CA  1 
ATOM   1207 C C   . GLU A 1 155 ? 8.332   13.710  42.852  1.00 48.01  ? 155 GLU A C   1 
ATOM   1208 O O   . GLU A 1 155 ? 7.890   12.601  42.520  1.00 47.57  ? 155 GLU A O   1 
ATOM   1209 C CB  . GLU A 1 155 ? 9.878   14.852  41.223  1.00 48.14  ? 155 GLU A CB  1 
ATOM   1210 C CG  . GLU A 1 155 ? 9.998   15.830  40.030  1.00 49.03  ? 155 GLU A CG  1 
ATOM   1211 C CD  . GLU A 1 155 ? 11.296  15.680  39.255  1.00 49.04  ? 155 GLU A CD  1 
ATOM   1212 O OE1 . GLU A 1 155 ? 11.583  16.521  38.423  1.00 53.62  ? 155 GLU A OE1 1 
ATOM   1213 O OE2 . GLU A 1 155 ? 12.037  14.709  39.440  1.00 52.37  ? 155 GLU A OE2 1 
ATOM   1214 N N   . ARG A 1 156 ? 8.722   13.949  44.096  1.00 48.49  ? 156 ARG A N   1 
ATOM   1215 C CA  . ARG A 1 156 ? 8.499   12.940  45.135  1.00 47.97  ? 156 ARG A CA  1 
ATOM   1216 C C   . ARG A 1 156 ? 7.008   12.759  45.303  1.00 46.91  ? 156 ARG A C   1 
ATOM   1217 O O   . ARG A 1 156 ? 6.560   11.651  45.411  1.00 48.11  ? 156 ARG A O   1 
ATOM   1218 C CB  . ARG A 1 156 ? 9.172   13.340  46.444  1.00 48.43  ? 156 ARG A CB  1 
ATOM   1219 C CG  . ARG A 1 156 ? 10.666  13.467  46.299  1.00 47.90  ? 156 ARG A CG  1 
ATOM   1220 C CD  . ARG A 1 156 ? 11.324  13.613  47.638  1.00 49.09  ? 156 ARG A CD  1 
ATOM   1221 N NE  . ARG A 1 156 ? 11.151  14.927  48.168  1.00 49.93  ? 156 ARG A NE  1 
ATOM   1222 C CZ  . ARG A 1 156 ? 12.131  15.781  48.444  1.00 49.58  ? 156 ARG A CZ  1 
ATOM   1223 N NH1 . ARG A 1 156 ? 13.394  15.478  48.212  1.00 51.51  ? 156 ARG A NH1 1 
ATOM   1224 N NH2 . ARG A 1 156 ? 11.832  16.937  48.976  1.00 47.57  ? 156 ARG A NH2 1 
ATOM   1225 N N   . GLN A 1 157 ? 6.230   13.836  45.272  1.00 46.66  ? 157 GLN A N   1 
ATOM   1226 C CA  . GLN A 1 157 ? 4.768   13.702  45.352  1.00 47.02  ? 157 GLN A CA  1 
ATOM   1227 C C   . GLN A 1 157 ? 4.195   12.864  44.190  1.00 47.06  ? 157 GLN A C   1 
ATOM   1228 O O   . GLN A 1 157 ? 3.386   11.939  44.383  1.00 47.59  ? 157 GLN A O   1 
ATOM   1229 C CB  . GLN A 1 157 ? 4.103   15.066  45.390  1.00 47.37  ? 157 GLN A CB  1 
ATOM   1230 C CG  . GLN A 1 157 ? 4.386   15.860  46.635  1.00 50.99  ? 157 GLN A CG  1 
ATOM   1231 C CD  . GLN A 1 157 ? 3.688   15.308  47.881  1.00 55.26  ? 157 GLN A CD  1 
ATOM   1232 O OE1 . GLN A 1 157 ? 2.534   14.868  47.822  1.00 53.89  ? 157 GLN A OE1 1 
ATOM   1233 N NE2 . GLN A 1 157 ? 4.400   15.336  49.020  1.00 58.29  ? 157 GLN A NE2 1 
ATOM   1234 N N   . GLU A 1 158 ? 4.633   13.186  42.978  1.00 46.48  ? 158 GLU A N   1 
ATOM   1235 C CA  . GLU A 1 158 ? 4.165   12.480  41.771  1.00 45.54  ? 158 GLU A CA  1 
ATOM   1236 C C   . GLU A 1 158 ? 4.561   11.028  41.750  1.00 44.98  ? 158 GLU A C   1 
ATOM   1237 O O   . GLU A 1 158 ? 3.719   10.135  41.615  1.00 46.07  ? 158 GLU A O   1 
ATOM   1238 C CB  . GLU A 1 158 ? 4.728   13.158  40.520  1.00 45.20  ? 158 GLU A CB  1 
ATOM   1239 C CG  . GLU A 1 158 ? 4.133   12.618  39.196  1.00 44.32  ? 158 GLU A CG  1 
ATOM   1240 C CD  . GLU A 1 158 ? 2.653   12.869  39.040  1.00 42.64  ? 158 GLU A CD  1 
ATOM   1241 O OE1 . GLU A 1 158 ? 2.179   13.972  39.381  1.00 44.11  ? 158 GLU A OE1 1 
ATOM   1242 O OE2 . GLU A 1 158 ? 1.949   11.978  38.514  1.00 46.52  ? 158 GLU A OE2 1 
ATOM   1243 N N   . TYR A 1 159 ? 5.846   10.778  41.919  1.00 45.04  ? 159 TYR A N   1 
ATOM   1244 C CA  . TYR A 1 159 ? 6.399   9.483   41.591  1.00 45.12  ? 159 TYR A CA  1 
ATOM   1245 C C   . TYR A 1 159 ? 6.408   8.493   42.764  1.00 45.65  ? 159 TYR A C   1 
ATOM   1246 O O   . TYR A 1 159 ? 6.694   7.305   42.571  1.00 45.37  ? 159 TYR A O   1 
ATOM   1247 C CB  . TYR A 1 159 ? 7.794   9.659   41.001  1.00 46.19  ? 159 TYR A CB  1 
ATOM   1248 C CG  . TYR A 1 159 ? 7.880   10.539  39.758  1.00 47.20  ? 159 TYR A CG  1 
ATOM   1249 C CD1 . TYR A 1 159 ? 6.955   10.431  38.704  1.00 48.86  ? 159 TYR A CD1 1 
ATOM   1250 C CD2 . TYR A 1 159 ? 8.906   11.470  39.623  1.00 48.51  ? 159 TYR A CD2 1 
ATOM   1251 C CE1 . TYR A 1 159 ? 7.064   11.249  37.547  1.00 47.52  ? 159 TYR A CE1 1 
ATOM   1252 C CE2 . TYR A 1 159 ? 9.033   12.257  38.475  1.00 48.29  ? 159 TYR A CE2 1 
ATOM   1253 C CZ  . TYR A 1 159 ? 8.101   12.159  37.459  1.00 48.25  ? 159 TYR A CZ  1 
ATOM   1254 O OH  . TYR A 1 159 ? 8.261   12.971  36.355  1.00 46.86  ? 159 TYR A OH  1 
ATOM   1255 N N   . VAL A 1 160 ? 6.102   8.951   43.981  1.00 45.55  ? 160 VAL A N   1 
ATOM   1256 C CA  . VAL A 1 160 ? 6.025   8.019   45.115  1.00 45.06  ? 160 VAL A CA  1 
ATOM   1257 C C   . VAL A 1 160 ? 4.619   7.982   45.688  1.00 45.25  ? 160 VAL A C   1 
ATOM   1258 O O   . VAL A 1 160 ? 4.025   6.890   45.841  1.00 44.64  ? 160 VAL A O   1 
ATOM   1259 C CB  . VAL A 1 160 ? 7.130   8.355   46.229  1.00 46.61  ? 160 VAL A CB  1 
ATOM   1260 C CG1 . VAL A 1 160 ? 7.046   7.392   47.405  1.00 43.51  ? 160 VAL A CG1 1 
ATOM   1261 C CG2 . VAL A 1 160 ? 8.519   8.300   45.620  1.00 45.12  ? 160 VAL A CG2 1 
ATOM   1262 N N   . LEU A 1 161 ? 4.080   9.178   45.950  1.00 44.70  ? 161 LEU A N   1 
ATOM   1263 C CA  . LEU A 1 161 ? 2.893   9.402   46.785  1.00 45.18  ? 161 LEU A CA  1 
ATOM   1264 C C   . LEU A 1 161 ? 1.553   9.448   46.056  1.00 44.70  ? 161 LEU A C   1 
ATOM   1265 O O   . LEU A 1 161 ? 0.521   9.076   46.611  1.00 45.07  ? 161 LEU A O   1 
ATOM   1266 C CB  . LEU A 1 161 ? 3.067   10.706  47.601  1.00 44.86  ? 161 LEU A CB  1 
ATOM   1267 C CG  . LEU A 1 161 ? 4.180   10.676  48.676  1.00 46.51  ? 161 LEU A CG  1 
ATOM   1268 C CD1 . LEU A 1 161 ? 4.193   11.923  49.531  1.00 44.28  ? 161 LEU A CD1 1 
ATOM   1269 C CD2 . LEU A 1 161 ? 4.023   9.453   49.582  1.00 44.87  ? 161 LEU A CD2 1 
ATOM   1270 N N   . THR A 1 162 ? 1.554   9.870   44.799  1.00 44.71  ? 162 THR A N   1 
ATOM   1271 C CA  . THR A 1 162 ? 0.309   10.047  44.058  1.00 43.92  ? 162 THR A CA  1 
ATOM   1272 C C   . THR A 1 162 ? -0.220  8.683   43.631  1.00 43.55  ? 162 THR A C   1 
ATOM   1273 O O   . THR A 1 162 ? 0.511   7.932   43.005  1.00 43.66  ? 162 THR A O   1 
ATOM   1274 C CB  . THR A 1 162 ? 0.553   10.978  42.871  1.00 44.12  ? 162 THR A CB  1 
ATOM   1275 O OG1 . THR A 1 162 ? 1.075   12.208  43.380  1.00 43.32  ? 162 THR A OG1 1 
ATOM   1276 C CG2 . THR A 1 162 ? -0.722  11.253  42.109  1.00 43.91  ? 162 THR A CG2 1 
ATOM   1277 N N   . GLN A 1 163 ? -1.470  8.366   43.979  1.00 43.29  ? 163 GLN A N   1 
ATOM   1278 C CA  . GLN A 1 163 ? -2.005  6.993   43.852  1.00 43.66  ? 163 GLN A CA  1 
ATOM   1279 C C   . GLN A 1 163 ? -2.817  6.743   42.576  1.00 43.58  ? 163 GLN A C   1 
ATOM   1280 O O   . GLN A 1 163 ? -3.265  5.614   42.330  1.00 42.53  ? 163 GLN A O   1 
ATOM   1281 C CB  . GLN A 1 163 ? -2.882  6.656   45.048  1.00 43.75  ? 163 GLN A CB  1 
ATOM   1282 C CG  . GLN A 1 163 ? -2.133  6.665   46.377  1.00 43.29  ? 163 GLN A CG  1 
ATOM   1283 C CD  . GLN A 1 163 ? -2.903  5.898   47.448  1.00 44.24  ? 163 GLN A CD  1 
ATOM   1284 O OE1 . GLN A 1 163 ? -2.955  4.676   47.435  1.00 44.79  ? 163 GLN A OE1 1 
ATOM   1285 N NE2 . GLN A 1 163 ? -3.517  6.623   48.352  1.00 43.45  ? 163 GLN A NE2 1 
ATOM   1286 N N   . GLN A 1 164 ? -3.011  7.800   41.793  1.00 43.35  ? 164 GLN A N   1 
ATOM   1287 C CA  . GLN A 1 164 ? -3.702  7.705   40.504  1.00 42.99  ? 164 GLN A CA  1 
ATOM   1288 C C   . GLN A 1 164 ? -2.876  8.454   39.449  1.00 43.17  ? 164 GLN A C   1 
ATOM   1289 O O   . GLN A 1 164 ? -2.076  9.372   39.746  1.00 43.37  ? 164 GLN A O   1 
ATOM   1290 C CB  . GLN A 1 164 ? -5.091  8.306   40.560  1.00 42.68  ? 164 GLN A CB  1 
ATOM   1291 C CG  . GLN A 1 164 ? -6.095  7.574   41.430  1.00 43.33  ? 164 GLN A CG  1 
ATOM   1292 C CD  . GLN A 1 164 ? -6.072  8.047   42.884  1.00 45.09  ? 164 GLN A CD  1 
ATOM   1293 O OE1 . GLN A 1 164 ? -6.011  9.254   43.152  1.00 47.47  ? 164 GLN A OE1 1 
ATOM   1294 N NE2 . GLN A 1 164 ? -6.145  7.105   43.822  1.00 42.65  ? 164 GLN A NE2 1 
ATOM   1295 N N   . GLY A 1 165 ? -3.057  8.063   38.202  1.00 42.47  ? 165 GLY A N   1 
ATOM   1296 C CA  . GLY A 1 165 ? -2.296  8.703   37.142  1.00 42.33  ? 165 GLY A CA  1 
ATOM   1297 C C   . GLY A 1 165 ? -2.901  8.378   35.811  1.00 41.51  ? 165 GLY A C   1 
ATOM   1298 O O   . GLY A 1 165 ? -4.069  8.035   35.724  1.00 41.48  ? 165 GLY A O   1 
ATOM   1299 N N   . PHE A 1 166 ? -2.102  8.510   34.773  1.00 42.33  ? 166 PHE A N   1 
ATOM   1300 C CA  . PHE A 1 166 ? -2.591  8.279   33.392  1.00 41.73  ? 166 PHE A CA  1 
ATOM   1301 C C   . PHE A 1 166 ? -1.671  7.297   32.704  1.00 41.58  ? 166 PHE A C   1 
ATOM   1302 O O   . PHE A 1 166 ? -0.452  7.341   32.886  1.00 42.47  ? 166 PHE A O   1 
ATOM   1303 C CB  . PHE A 1 166 ? -2.632  9.561   32.596  1.00 41.28  ? 166 PHE A CB  1 
ATOM   1304 C CG  . PHE A 1 166 ? -3.658  10.503  33.051  1.00 41.84  ? 166 PHE A CG  1 
ATOM   1305 C CD1 . PHE A 1 166 ? -3.302  11.661  33.698  1.00 41.54  ? 166 PHE A CD1 1 
ATOM   1306 C CD2 . PHE A 1 166 ? -5.004  10.224  32.856  1.00 40.80  ? 166 PHE A CD2 1 
ATOM   1307 C CE1 . PHE A 1 166 ? -4.275  12.541  34.148  1.00 42.49  ? 166 PHE A CE1 1 
ATOM   1308 C CE2 . PHE A 1 166 ? -5.966  11.096  33.292  1.00 43.31  ? 166 PHE A CE2 1 
ATOM   1309 C CZ  . PHE A 1 166 ? -5.596  12.261  33.946  1.00 42.08  ? 166 PHE A CZ  1 
ATOM   1310 N N   . ILE A 1 167 ? -2.270  6.397   31.935  1.00 41.36  ? 167 ILE A N   1 
ATOM   1311 C CA  . ILE A 1 167 ? -1.530  5.514   31.084  1.00 41.61  ? 167 ILE A CA  1 
ATOM   1312 C C   . ILE A 1 167 ? -1.946  5.843   29.648  1.00 40.82  ? 167 ILE A C   1 
ATOM   1313 O O   . ILE A 1 167 ? -3.108  5.857   29.324  1.00 40.20  ? 167 ILE A O   1 
ATOM   1314 C CB  . ILE A 1 167 ? -1.768  4.054   31.501  1.00 41.49  ? 167 ILE A CB  1 
ATOM   1315 C CG1 . ILE A 1 167 ? -1.100  3.826   32.857  1.00 42.69  ? 167 ILE A CG1 1 
ATOM   1316 C CG2 . ILE A 1 167 ? -1.204  3.090   30.467  1.00 42.54  ? 167 ILE A CG2 1 
ATOM   1317 C CD1 . ILE A 1 167 ? -1.459  2.541   33.481  1.00 43.89  ? 167 ILE A CD1 1 
ATOM   1318 N N   . TYR A 1 168 ? -0.977  6.181   28.807  1.00 41.00  ? 168 TYR A N   1 
ATOM   1319 C CA  . TYR A 1 168 ? -1.307  6.629   27.457  1.00 40.95  ? 168 TYR A CA  1 
ATOM   1320 C C   . TYR A 1 168 ? -1.408  5.425   26.533  1.00 40.14  ? 168 TYR A C   1 
ATOM   1321 O O   . TYR A 1 168 ? -0.563  4.545   26.570  1.00 39.70  ? 168 TYR A O   1 
ATOM   1322 C CB  . TYR A 1 168 ? -0.295  7.674   26.987  1.00 41.42  ? 168 TYR A CB  1 
ATOM   1323 C CG  . TYR A 1 168 ? -0.356  8.852   27.895  1.00 41.05  ? 168 TYR A CG  1 
ATOM   1324 C CD1 . TYR A 1 168 ? 0.487   8.948   28.988  1.00 42.44  ? 168 TYR A CD1 1 
ATOM   1325 C CD2 . TYR A 1 168 ? -1.328  9.827   27.726  1.00 42.99  ? 168 TYR A CD2 1 
ATOM   1326 C CE1 . TYR A 1 168 ? 0.405   10.009  29.863  1.00 40.84  ? 168 TYR A CE1 1 
ATOM   1327 C CE2 . TYR A 1 168 ? -1.420  10.895  28.607  1.00 42.16  ? 168 TYR A CE2 1 
ATOM   1328 C CZ  . TYR A 1 168 ? -0.559  10.976  29.666  1.00 41.07  ? 168 TYR A CZ  1 
ATOM   1329 O OH  . TYR A 1 168 ? -0.622  12.035  30.525  1.00 41.41  ? 168 TYR A OH  1 
ATOM   1330 N N   . GLN A 1 169 ? -2.461  5.400   25.723  1.00 40.03  ? 169 GLN A N   1 
ATOM   1331 C CA  . GLN A 1 169 ? -2.677  4.350   24.747  1.00 39.77  ? 169 GLN A CA  1 
ATOM   1332 C C   . GLN A 1 169 ? -3.180  5.019   23.450  1.00 39.15  ? 169 GLN A C   1 
ATOM   1333 O O   . GLN A 1 169 ? -2.976  6.213   23.248  1.00 37.82  ? 169 GLN A O   1 
ATOM   1334 C CB  . GLN A 1 169 ? -3.764  3.379   25.239  1.00 39.97  ? 169 GLN A CB  1 
ATOM   1335 C CG  . GLN A 1 169 ? -3.541  2.784   26.626  1.00 40.85  ? 169 GLN A CG  1 
ATOM   1336 C CD  . GLN A 1 169 ? -4.703  1.864   27.053  1.00 41.96  ? 169 GLN A CD  1 
ATOM   1337 O OE1 . GLN A 1 169 ? -4.503  0.906   27.780  1.00 50.07  ? 169 GLN A OE1 1 
ATOM   1338 N NE2 . GLN A 1 169 ? -5.906  2.178   26.622  1.00 43.37  ? 169 GLN A NE2 1 
ATOM   1339 N N   . GLY A 1 170 ? -3.838  4.246   22.593  1.00 39.12  ? 170 GLY A N   1 
ATOM   1340 C CA  . GLY A 1 170 ? -4.263  4.714   21.268  1.00 38.66  ? 170 GLY A CA  1 
ATOM   1341 C C   . GLY A 1 170 ? -3.113  4.602   20.281  1.00 38.88  ? 170 GLY A C   1 
ATOM   1342 O O   . GLY A 1 170 ? -2.524  3.530   20.098  1.00 38.94  ? 170 GLY A O   1 
ATOM   1343 N N   . SER A 1 171 ? -2.832  5.703   19.599  1.00 38.76  ? 171 SER A N   1 
ATOM   1344 C CA  . SER A 1 171 ? -1.801  5.764   18.572  1.00 38.97  ? 171 SER A CA  1 
ATOM   1345 C C   . SER A 1 171 ? -1.037  7.069   18.681  1.00 39.37  ? 171 SER A C   1 
ATOM   1346 O O   . SER A 1 171 ? -1.450  7.978   19.390  1.00 39.98  ? 171 SER A O   1 
ATOM   1347 C CB  . SER A 1 171 ? -2.416  5.657   17.164  1.00 38.40  ? 171 SER A CB  1 
ATOM   1348 O OG  . SER A 1 171 ? -3.299  6.753   16.903  1.00 36.88  ? 171 SER A OG  1 
ATOM   1349 N N   . ALA A 1 172 ? 0.058   7.164   17.946  1.00 39.90  ? 172 ALA A N   1 
ATOM   1350 C CA  . ALA A 1 172 ? 0.884   8.352   17.939  1.00 40.75  ? 172 ALA A CA  1 
ATOM   1351 C C   . ALA A 1 172 ? 0.088   9.581   17.514  1.00 41.64  ? 172 ALA A C   1 
ATOM   1352 O O   . ALA A 1 172 ? 0.333   10.684  17.995  1.00 42.28  ? 172 ALA A O   1 
ATOM   1353 C CB  . ALA A 1 172 ? 2.091   8.135   17.016  1.00 40.88  ? 172 ALA A CB  1 
ATOM   1354 N N   . LYS A 1 173 ? -0.881  9.382   16.622  1.00 42.46  ? 173 LYS A N   1 
ATOM   1355 C CA  . LYS A 1 173 ? -1.707  10.473  16.117  1.00 42.42  ? 173 LYS A CA  1 
ATOM   1356 C C   . LYS A 1 173 ? -2.938  10.749  16.963  1.00 41.96  ? 173 LYS A C   1 
ATOM   1357 O O   . LYS A 1 173 ? -3.426  11.873  16.970  1.00 42.06  ? 173 LYS A O   1 
ATOM   1358 C CB  . LYS A 1 173 ? -2.107  10.201  14.664  1.00 43.57  ? 173 LYS A CB  1 
ATOM   1359 C CG  . LYS A 1 173 ? -0.940  10.411  13.700  1.00 46.10  ? 173 LYS A CG  1 
ATOM   1360 C CD  . LYS A 1 173 ? -0.638  11.924  13.484  1.00 49.53  ? 173 LYS A CD  1 
ATOM   1361 C CE  . LYS A 1 173 ? 0.860   12.209  13.286  1.00 49.97  ? 173 LYS A CE  1 
ATOM   1362 N NZ  . LYS A 1 173 ? 1.717   11.616  14.369  1.00 50.33  ? 173 LYS A NZ  1 
ATOM   1363 N N   . PHE A 1 174 ? -3.447  9.719   17.627  1.00 41.22  ? 174 PHE A N   1 
ATOM   1364 C CA  . PHE A 1 174 ? -4.617  9.818   18.485  1.00 41.59  ? 174 PHE A CA  1 
ATOM   1365 C C   . PHE A 1 174 ? -4.292  9.198   19.850  1.00 41.98  ? 174 PHE A C   1 
ATOM   1366 O O   . PHE A 1 174 ? -4.662  8.052   20.161  1.00 41.83  ? 174 PHE A O   1 
ATOM   1367 C CB  . PHE A 1 174 ? -5.802  9.115   17.839  1.00 40.76  ? 174 PHE A CB  1 
ATOM   1368 C CG  . PHE A 1 174 ? -6.332  9.823   16.615  1.00 40.56  ? 174 PHE A CG  1 
ATOM   1369 C CD1 . PHE A 1 174 ? -6.081  9.329   15.347  1.00 41.24  ? 174 PHE A CD1 1 
ATOM   1370 C CD2 . PHE A 1 174 ? -7.066  10.988  16.743  1.00 39.88  ? 174 PHE A CD2 1 
ATOM   1371 C CE1 . PHE A 1 174 ? -6.551  9.980   14.243  1.00 39.26  ? 174 PHE A CE1 1 
ATOM   1372 C CE2 . PHE A 1 174 ? -7.542  11.649  15.652  1.00 39.12  ? 174 PHE A CE2 1 
ATOM   1373 C CZ  . PHE A 1 174 ? -7.293  11.139  14.385  1.00 39.58  ? 174 PHE A CZ  1 
ATOM   1374 N N   . ILE A 1 175 ? -3.569  9.965   20.653  1.00 42.61  ? 175 ILE A N   1 
ATOM   1375 C CA  . ILE A 1 175 ? -3.158  9.517   21.983  1.00 43.33  ? 175 ILE A CA  1 
ATOM   1376 C C   . ILE A 1 175 ? -4.362  9.469   22.941  1.00 44.12  ? 175 ILE A C   1 
ATOM   1377 O O   . ILE A 1 175 ? -5.093  10.440  23.058  1.00 44.50  ? 175 ILE A O   1 
ATOM   1378 C CB  . ILE A 1 175 ? -1.984  10.404  22.480  1.00 43.41  ? 175 ILE A CB  1 
ATOM   1379 C CG1 . ILE A 1 175 ? -0.745  10.082  21.629  1.00 43.73  ? 175 ILE A CG1 1 
ATOM   1380 C CG2 . ILE A 1 175 ? -1.667  10.164  23.960  1.00 42.24  ? 175 ILE A CG2 1 
ATOM   1381 C CD1 . ILE A 1 175 ? 0.497   10.911  21.897  1.00 44.60  ? 175 ILE A CD1 1 
ATOM   1382 N N   . LYS A 1 176 ? -4.589  8.313   23.577  1.00 45.03  ? 176 LYS A N   1 
ATOM   1383 C CA  . LYS A 1 176 ? -5.628  8.144   24.607  1.00 45.57  ? 176 LYS A CA  1 
ATOM   1384 C C   . LYS A 1 176 ? -5.012  8.206   25.998  1.00 45.42  ? 176 LYS A C   1 
ATOM   1385 O O   . LYS A 1 176 ? -4.015  7.543   26.256  1.00 44.89  ? 176 LYS A O   1 
ATOM   1386 C CB  . LYS A 1 176 ? -6.321  6.788   24.472  1.00 45.71  ? 176 LYS A CB  1 
ATOM   1387 C CG  . LYS A 1 176 ? -7.543  6.808   23.625  1.00 47.67  ? 176 LYS A CG  1 
ATOM   1388 C CD  . LYS A 1 176 ? -8.083  5.410   23.337  1.00 48.05  ? 176 LYS A CD  1 
ATOM   1389 C CE  . LYS A 1 176 ? -8.694  4.763   24.575  1.00 49.14  ? 176 LYS A CE  1 
ATOM   1390 N NZ  . LYS A 1 176 ? -9.755  3.786   24.183  1.00 49.12  ? 176 LYS A NZ  1 
ATOM   1391 N N   . ASN A 1 177 ? -5.622  8.965   26.902  1.00 45.81  ? 177 ASN A N   1 
ATOM   1392 C CA  . ASN A 1 177 ? -5.153  9.021   28.295  1.00 45.90  ? 177 ASN A CA  1 
ATOM   1393 C C   . ASN A 1 177 ? -6.114  8.238   29.153  1.00 45.59  ? 177 ASN A C   1 
ATOM   1394 O O   . ASN A 1 177 ? -7.241  8.674   29.369  1.00 46.63  ? 177 ASN A O   1 
ATOM   1395 C CB  . ASN A 1 177 ? -5.090  10.452  28.813  1.00 46.78  ? 177 ASN A CB  1 
ATOM   1396 C CG  . ASN A 1 177 ? -5.043  11.460  27.708  1.00 49.88  ? 177 ASN A CG  1 
ATOM   1397 O OD1 . ASN A 1 177 ? -5.787  12.437  27.724  1.00 54.72  ? 177 ASN A OD1 1 
ATOM   1398 N ND2 . ASN A 1 177 ? -4.175  11.228  26.725  1.00 50.24  ? 177 ASN A ND2 1 
ATOM   1399 N N   . ILE A 1 178 ? -5.689  7.077   29.626  1.00 43.90  ? 178 ILE A N   1 
ATOM   1400 C CA  . ILE A 1 178 ? -6.584  6.234   30.375  1.00 43.08  ? 178 ILE A CA  1 
ATOM   1401 C C   . ILE A 1 178 ? -6.205  6.494   31.845  1.00 41.58  ? 178 ILE A C   1 
ATOM   1402 O O   . ILE A 1 178 ? -5.059  6.327   32.199  1.00 40.40  ? 178 ILE A O   1 
ATOM   1403 C CB  . ILE A 1 178 ? -6.425  4.770   29.913  1.00 42.74  ? 178 ILE A CB  1 
ATOM   1404 C CG1 . ILE A 1 178 ? -7.330  4.492   28.691  1.00 44.56  ? 178 ILE A CG1 1 
ATOM   1405 C CG2 . ILE A 1 178 ? -6.817  3.805   30.957  1.00 44.22  ? 178 ILE A CG2 1 
ATOM   1406 C CD1 . ILE A 1 178 ? -7.308  5.548   27.647  1.00 44.53  ? 178 ILE A CD1 1 
ATOM   1407 N N   . PRO A 1 179 ? -7.152  6.971   32.666  1.00 41.32  ? 179 PRO A N   1 
ATOM   1408 C CA  . PRO A 1 179 ? -6.828  7.179   34.084  1.00 41.91  ? 179 PRO A CA  1 
ATOM   1409 C C   . PRO A 1 179 ? -6.633  5.832   34.767  1.00 41.64  ? 179 PRO A C   1 
ATOM   1410 O O   . PRO A 1 179 ? -7.227  4.835   34.347  1.00 41.24  ? 179 PRO A O   1 
ATOM   1411 C CB  . PRO A 1 179 ? -8.064  7.907   34.616  1.00 41.26  ? 179 PRO A CB  1 
ATOM   1412 C CG  . PRO A 1 179 ? -9.143  7.451   33.774  1.00 41.90  ? 179 PRO A CG  1 
ATOM   1413 C CD  . PRO A 1 179 ? -8.558  7.298   32.403  1.00 41.50  ? 179 PRO A CD  1 
ATOM   1414 N N   . TRP A 1 180 ? -5.828  5.804   35.822  1.00 42.17  ? 180 TRP A N   1 
ATOM   1415 C CA  . TRP A 1 180 ? -5.495  4.549   36.473  1.00 42.49  ? 180 TRP A CA  1 
ATOM   1416 C C   . TRP A 1 180 ? -5.308  4.709   37.977  1.00 42.37  ? 180 TRP A C   1 
ATOM   1417 O O   . TRP A 1 180 ? -4.630  5.622   38.420  1.00 42.12  ? 180 TRP A O   1 
ATOM   1418 C CB  . TRP A 1 180 ? -4.180  4.025   35.913  1.00 42.80  ? 180 TRP A CB  1 
ATOM   1419 C CG  . TRP A 1 180 ? -3.929  2.638   36.284  1.00 43.42  ? 180 TRP A CG  1 
ATOM   1420 C CD1 . TRP A 1 180 ? -3.279  2.193   37.393  1.00 43.63  ? 180 TRP A CD1 1 
ATOM   1421 C CD2 . TRP A 1 180 ? -4.318  1.477   35.545  1.00 43.97  ? 180 TRP A CD2 1 
ATOM   1422 N NE1 . TRP A 1 180 ? -3.235  0.833   37.390  1.00 43.35  ? 180 TRP A NE1 1 
ATOM   1423 C CE2 . TRP A 1 180 ? -3.852  0.361   36.260  1.00 43.97  ? 180 TRP A CE2 1 
ATOM   1424 C CE3 . TRP A 1 180 ? -4.977  1.275   34.322  1.00 44.92  ? 180 TRP A CE3 1 
ATOM   1425 C CZ2 . TRP A 1 180 ? -4.055  -0.950  35.821  1.00 43.62  ? 180 TRP A CZ2 1 
ATOM   1426 C CZ3 . TRP A 1 180 ? -5.177  -0.039  33.877  1.00 44.20  ? 180 TRP A CZ3 1 
ATOM   1427 C CH2 . TRP A 1 180 ? -4.707  -1.132  34.633  1.00 44.01  ? 180 TRP A CH2 1 
ATOM   1428 N N   . ASN A 1 181 ? -5.886  3.793   38.736  1.00 42.15  ? 181 ASN A N   1 
ATOM   1429 C CA  . ASN A 1 181 ? -5.692  3.764   40.192  1.00 42.12  ? 181 ASN A CA  1 
ATOM   1430 C C   . ASN A 1 181 ? -4.557  2.830   40.520  1.00 41.51  ? 181 ASN A C   1 
ATOM   1431 O O   . ASN A 1 181 ? -4.739  1.622   40.569  1.00 41.75  ? 181 ASN A O   1 
ATOM   1432 C CB  . ASN A 1 181 ? -6.984  3.302   40.888  1.00 41.69  ? 181 ASN A CB  1 
ATOM   1433 C CG  . ASN A 1 181 ? -6.840  3.203   42.419  1.00 42.01  ? 181 ASN A CG  1 
ATOM   1434 O OD1 . ASN A 1 181 ? -6.355  4.121   43.058  1.00 41.95  ? 181 ASN A OD1 1 
ATOM   1435 N ND2 . ASN A 1 181 ? -7.287  2.105   42.991  1.00 41.77  ? 181 ASN A ND2 1 
ATOM   1436 N N   . PHE A 1 182 ? -3.379  3.391   40.731  1.00 41.51  ? 182 PHE A N   1 
ATOM   1437 C CA  . PHE A 1 182 ? -2.240  2.633   41.202  1.00 42.77  ? 182 PHE A CA  1 
ATOM   1438 C C   . PHE A 1 182 ? -2.478  2.060   42.599  1.00 43.53  ? 182 PHE A C   1 
ATOM   1439 O O   . PHE A 1 182 ? -2.178  0.890   42.835  1.00 45.66  ? 182 PHE A O   1 
ATOM   1440 C CB  . PHE A 1 182 ? -0.971  3.481   41.173  1.00 43.24  ? 182 PHE A CB  1 
ATOM   1441 C CG  . PHE A 1 182 ? -0.573  3.865   39.784  1.00 42.42  ? 182 PHE A CG  1 
ATOM   1442 C CD1 . PHE A 1 182 ? -0.251  2.874   38.865  1.00 43.69  ? 182 PHE A CD1 1 
ATOM   1443 C CD2 . PHE A 1 182 ? -0.565  5.189   39.388  1.00 42.43  ? 182 PHE A CD2 1 
ATOM   1444 C CE1 . PHE A 1 182 ? 0.080   3.210   37.541  1.00 42.94  ? 182 PHE A CE1 1 
ATOM   1445 C CE2 . PHE A 1 182 ? -0.240  5.527   38.084  1.00 43.58  ? 182 PHE A CE2 1 
ATOM   1446 C CZ  . PHE A 1 182 ? 0.080   4.525   37.170  1.00 43.50  ? 182 PHE A CZ  1 
ATOM   1447 N N   . GLY A 1 183 ? -3.029  2.874   43.491  1.00 43.53  ? 183 GLY A N   1 
ATOM   1448 C CA  . GLY A 1 183 ? -3.537  2.406   44.780  1.00 43.47  ? 183 GLY A CA  1 
ATOM   1449 C C   . GLY A 1 183 ? -2.496  1.857   45.731  1.00 43.39  ? 183 GLY A C   1 
ATOM   1450 O O   . GLY A 1 183 ? -2.824  1.057   46.587  1.00 44.89  ? 183 GLY A O   1 
ATOM   1451 N N   . GLN A 1 184 ? -1.259  2.320   45.609  1.00 43.62  ? 184 GLN A N   1 
ATOM   1452 C CA  . GLN A 1 184 ? -0.125  1.744   46.321  1.00 43.69  ? 184 GLN A CA  1 
ATOM   1453 C C   . GLN A 1 184 ? -0.258  1.746   47.859  1.00 43.99  ? 184 GLN A C   1 
ATOM   1454 O O   . GLN A 1 184 ? 0.403   0.963   48.537  1.00 42.45  ? 184 GLN A O   1 
ATOM   1455 C CB  . GLN A 1 184 ? 1.212   2.390   45.909  1.00 43.91  ? 184 GLN A CB  1 
ATOM   1456 C CG  . GLN A 1 184 ? 1.399   3.876   46.232  1.00 43.32  ? 184 GLN A CG  1 
ATOM   1457 C CD  . GLN A 1 184 ? 1.027   4.797   45.059  1.00 43.36  ? 184 GLN A CD  1 
ATOM   1458 O OE1 . GLN A 1 184 ? 0.124   4.490   44.289  1.00 41.70  ? 184 GLN A OE1 1 
ATOM   1459 N NE2 . GLN A 1 184 ? 1.755   5.915   44.912  1.00 37.93  ? 184 GLN A NE2 1 
ATOM   1460 N N   . PHE A 1 185 ? -1.081  2.636   48.402  1.00 44.79  ? 185 PHE A N   1 
ATOM   1461 C CA  . PHE A 1 185 ? -1.249  2.704   49.877  1.00 45.04  ? 185 PHE A CA  1 
ATOM   1462 C C   . PHE A 1 185 ? -2.591  2.188   50.318  1.00 45.71  ? 185 PHE A C   1 
ATOM   1463 O O   . PHE A 1 185 ? -2.972  2.423   51.463  1.00 46.21  ? 185 PHE A O   1 
ATOM   1464 C CB  . PHE A 1 185 ? -1.054  4.141   50.383  1.00 44.60  ? 185 PHE A CB  1 
ATOM   1465 C CG  . PHE A 1 185 ? 0.208   4.776   49.919  1.00 44.15  ? 185 PHE A CG  1 
ATOM   1466 C CD1 . PHE A 1 185 ? 1.390   4.073   49.877  1.00 46.19  ? 185 PHE A CD1 1 
ATOM   1467 C CD2 . PHE A 1 185 ? 0.219   6.093   49.523  1.00 44.87  ? 185 PHE A CD2 1 
ATOM   1468 C CE1 . PHE A 1 185 ? 2.555   4.679   49.435  1.00 45.58  ? 185 PHE A CE1 1 
ATOM   1469 C CE2 . PHE A 1 185 ? 1.358   6.694   49.105  1.00 44.44  ? 185 PHE A CE2 1 
ATOM   1470 C CZ  . PHE A 1 185 ? 2.533   5.985   49.056  1.00 45.28  ? 185 PHE A CZ  1 
ATOM   1471 N N   . GLN A 1 186 ? -3.324  1.488   49.440  1.00 45.91  ? 186 GLN A N   1 
ATOM   1472 C CA  . GLN A 1 186 ? -4.586  0.883   49.837  1.00 46.50  ? 186 GLN A CA  1 
ATOM   1473 C C   . GLN A 1 186 ? -4.313  -0.258  50.806  1.00 46.48  ? 186 GLN A C   1 
ATOM   1474 O O   . GLN A 1 186 ? -3.236  -0.831  50.814  1.00 45.15  ? 186 GLN A O   1 
ATOM   1475 C CB  . GLN A 1 186 ? -5.393  0.341   48.633  1.00 47.02  ? 186 GLN A CB  1 
ATOM   1476 C CG  . GLN A 1 186 ? -6.043  1.445   47.807  1.00 48.18  ? 186 GLN A CG  1 
ATOM   1477 C CD  . GLN A 1 186 ? -7.268  1.016   47.020  1.00 47.87  ? 186 GLN A CD  1 
ATOM   1478 O OE1 . GLN A 1 186 ? -7.549  1.583   45.984  1.00 50.29  ? 186 GLN A OE1 1 
ATOM   1479 N NE2 . GLN A 1 186 ? -8.031  0.056   47.539  1.00 53.35  ? 186 GLN A NE2 1 
ATOM   1480 N N   . ASP A 1 187 ? -5.320  -0.595  51.587  1.00 47.17  ? 187 ASP A N   1 
ATOM   1481 C CA  . ASP A 1 187 ? -5.203  -1.602  52.640  1.00 47.38  ? 187 ASP A CA  1 
ATOM   1482 C C   . ASP A 1 187 ? -4.770  -2.963  52.059  1.00 47.80  ? 187 ASP A C   1 
ATOM   1483 O O   . ASP A 1 187 ? -5.396  -3.472  51.111  1.00 48.18  ? 187 ASP A O   1 
ATOM   1484 C CB  . ASP A 1 187 ? -6.574  -1.746  53.335  1.00 47.85  ? 187 ASP A CB  1 
ATOM   1485 C CG  . ASP A 1 187 ? -6.510  -2.539  54.627  1.00 48.79  ? 187 ASP A CG  1 
ATOM   1486 O OD1 . ASP A 1 187 ? -5.541  -2.383  55.399  1.00 55.12  ? 187 ASP A OD1 1 
ATOM   1487 O OD2 . ASP A 1 187 ? -7.456  -3.306  54.889  1.00 55.01  ? 187 ASP A OD2 1 
ATOM   1488 N N   . GLY A 1 188 ? -3.700  -3.536  52.599  1.00 47.03  ? 188 GLY A N   1 
ATOM   1489 C CA  . GLY A 1 188 ? -3.273  -4.869  52.182  1.00 46.78  ? 188 GLY A CA  1 
ATOM   1490 C C   . GLY A 1 188 ? -2.193  -4.848  51.113  1.00 46.36  ? 188 GLY A C   1 
ATOM   1491 O O   . GLY A 1 188 ? -1.494  -5.828  50.931  1.00 46.43  ? 188 GLY A O   1 
ATOM   1492 N N   . ILE A 1 189 ? -2.053  -3.738  50.399  1.00 45.79  ? 189 ILE A N   1 
ATOM   1493 C CA  . ILE A 1 189 ? -1.181  -3.706  49.218  1.00 45.52  ? 189 ILE A CA  1 
ATOM   1494 C C   . ILE A 1 189 ? 0.293   -3.813  49.564  1.00 45.58  ? 189 ILE A C   1 
ATOM   1495 O O   . ILE A 1 189 ? 1.017   -4.600  48.957  1.00 45.15  ? 189 ILE A O   1 
ATOM   1496 C CB  . ILE A 1 189 ? -1.449  -2.439  48.349  1.00 44.73  ? 189 ILE A CB  1 
ATOM   1497 C CG1 . ILE A 1 189 ? -2.823  -2.551  47.688  1.00 43.72  ? 189 ILE A CG1 1 
ATOM   1498 C CG2 . ILE A 1 189 ? -0.356  -2.247  47.315  1.00 45.64  ? 189 ILE A CG2 1 
ATOM   1499 C CD1 . ILE A 1 189 ? -3.072  -3.846  46.878  1.00 39.65  ? 189 ILE A CD1 1 
ATOM   1500 N N   . LEU A 1 190 ? 0.736   -3.074  50.577  1.00 46.16  ? 190 LEU A N   1 
ATOM   1501 C CA  . LEU A 1 190 ? 2.118   -3.208  51.058  1.00 46.37  ? 190 LEU A CA  1 
ATOM   1502 C C   . LEU A 1 190 ? 2.476   -4.638  51.492  1.00 46.68  ? 190 LEU A C   1 
ATOM   1503 O O   . LEU A 1 190 ? 3.567   -5.121  51.179  1.00 46.95  ? 190 LEU A O   1 
ATOM   1504 C CB  . LEU A 1 190 ? 2.393   -2.216  52.191  1.00 46.83  ? 190 LEU A CB  1 
ATOM   1505 C CG  . LEU A 1 190 ? 3.732   -2.275  52.943  1.00 47.87  ? 190 LEU A CG  1 
ATOM   1506 C CD1 . LEU A 1 190 ? 4.945   -2.234  51.983  1.00 47.90  ? 190 LEU A CD1 1 
ATOM   1507 C CD2 . LEU A 1 190 ? 3.767   -1.088  53.932  1.00 46.30  ? 190 LEU A CD2 1 
ATOM   1508 N N   . ASP A 1 191 ? 1.588   -5.279  52.245  1.00 46.82  ? 191 ASP A N   1 
ATOM   1509 C CA  . ASP A 1 191 ? 1.762   -6.676  52.653  1.00 46.86  ? 191 ASP A CA  1 
ATOM   1510 C C   . ASP A 1 191 ? 1.875   -7.562  51.412  1.00 46.81  ? 191 ASP A C   1 
ATOM   1511 O O   . ASP A 1 191 ? 2.732   -8.440  51.348  1.00 45.85  ? 191 ASP A O   1 
ATOM   1512 C CB  . ASP A 1 191 ? 0.561   -7.176  53.478  1.00 47.38  ? 191 ASP A CB  1 
ATOM   1513 C CG  . ASP A 1 191 ? 0.504   -6.580  54.893  1.00 49.37  ? 191 ASP A CG  1 
ATOM   1514 O OD1 . ASP A 1 191 ? -0.605  -6.562  55.474  1.00 53.22  ? 191 ASP A OD1 1 
ATOM   1515 O OD2 . ASP A 1 191 ? 1.532   -6.142  55.415  1.00 48.59  ? 191 ASP A OD2 1 
ATOM   1516 N N   . ILE A 1 192 ? 1.005   -7.336  50.425  1.00 46.66  ? 192 ILE A N   1 
ATOM   1517 C CA  . ILE A 1 192 ? 1.083   -8.120  49.179  1.00 46.93  ? 192 ILE A CA  1 
ATOM   1518 C C   . ILE A 1 192 ? 2.439   -7.941  48.483  1.00 46.57  ? 192 ILE A C   1 
ATOM   1519 O O   . ILE A 1 192 ? 3.011   -8.915  47.997  1.00 47.10  ? 192 ILE A O   1 
ATOM   1520 C CB  . ILE A 1 192 ? -0.110  -7.845  48.215  1.00 47.16  ? 192 ILE A CB  1 
ATOM   1521 C CG1 . ILE A 1 192 ? -1.396  -8.390  48.817  1.00 46.93  ? 192 ILE A CG1 1 
ATOM   1522 C CG2 . ILE A 1 192 ? 0.097   -8.535  46.885  1.00 46.93  ? 192 ILE A CG2 1 
ATOM   1523 C CD1 . ILE A 1 192 ? -2.609  -7.943  48.092  1.00 47.49  ? 192 ILE A CD1 1 
ATOM   1524 N N   . CYS A 1 193 ? 2.960   -6.720  48.507  1.00 46.44  ? 193 CYS A N   1 
ATOM   1525 C CA  . CYS A 1 193 ? 4.244   -6.376  47.896  1.00 47.36  ? 193 CYS A CA  1 
ATOM   1526 C C   . CYS A 1 193 ? 5.432   -7.032  48.587  1.00 48.48  ? 193 CYS A C   1 
ATOM   1527 O O   . CYS A 1 193 ? 6.401   -7.438  47.912  1.00 48.55  ? 193 CYS A O   1 
ATOM   1528 C CB  . CYS A 1 193 ? 4.458   -4.884  47.884  1.00 46.36  ? 193 CYS A CB  1 
ATOM   1529 S SG  . CYS A 1 193 ? 3.437   -3.946  46.692  1.00 47.47  ? 193 CYS A SG  1 
ATOM   1530 N N   . LEU A 1 194 ? 5.357   -7.127  49.928  1.00 48.14  ? 194 LEU A N   1 
ATOM   1531 C CA  . LEU A 1 194 ? 6.359   -7.860  50.704  1.00 47.42  ? 194 LEU A CA  1 
ATOM   1532 C C   . LEU A 1 194 ? 6.251   -9.329  50.440  1.00 47.11  ? 194 LEU A C   1 
ATOM   1533 O O   . LEU A 1 194 ? 7.264   -9.988  50.341  1.00 48.61  ? 194 LEU A O   1 
ATOM   1534 C CB  . LEU A 1 194 ? 6.241   -7.557  52.211  1.00 47.68  ? 194 LEU A CB  1 
ATOM   1535 C CG  . LEU A 1 194 ? 6.573   -6.105  52.545  1.00 46.46  ? 194 LEU A CG  1 
ATOM   1536 C CD1 . LEU A 1 194 ? 6.438   -5.838  54.063  1.00 48.64  ? 194 LEU A CD1 1 
ATOM   1537 C CD2 . LEU A 1 194 ? 7.977   -5.768  52.057  1.00 49.72  ? 194 LEU A CD2 1 
ATOM   1538 N N   . ILE A 1 195 ? 5.032   -9.846  50.291  1.00 46.82  ? 195 ILE A N   1 
ATOM   1539 C CA  . ILE A 1 195 ? 4.823   -11.227 49.883  1.00 46.48  ? 195 ILE A CA  1 
ATOM   1540 C C   . ILE A 1 195 ? 5.468   -11.499 48.516  1.00 46.48  ? 195 ILE A C   1 
ATOM   1541 O O   . ILE A 1 195 ? 6.149   -12.507 48.315  1.00 46.22  ? 195 ILE A O   1 
ATOM   1542 C CB  . ILE A 1 195 ? 3.303   -11.633 49.813  1.00 47.00  ? 195 ILE A CB  1 
ATOM   1543 C CG1 . ILE A 1 195 ? 2.700   -11.826 51.212  1.00 47.74  ? 195 ILE A CG1 1 
ATOM   1544 C CG2 . ILE A 1 195 ? 3.149   -12.923 49.055  1.00 45.11  ? 195 ILE A CG2 1 
ATOM   1545 C CD1 . ILE A 1 195 ? 1.199   -11.903 51.233  1.00 47.00  ? 195 ILE A CD1 1 
ATOM   1546 N N   . LEU A 1 196 ? 5.240   -10.608 47.565  1.00 46.30  ? 196 LEU A N   1 
ATOM   1547 C CA  . LEU A 1 196 ? 5.814   -10.785 46.243  1.00 46.61  ? 196 LEU A CA  1 
ATOM   1548 C C   . LEU A 1 196 ? 7.337   -10.974 46.328  1.00 46.53  ? 196 LEU A C   1 
ATOM   1549 O O   . LEU A 1 196 ? 7.874   -11.877 45.692  1.00 46.89  ? 196 LEU A O   1 
ATOM   1550 C CB  . LEU A 1 196 ? 5.398   -9.628  45.335  1.00 46.12  ? 196 LEU A CB  1 
ATOM   1551 C CG  . LEU A 1 196 ? 5.992   -9.476  43.929  1.00 46.93  ? 196 LEU A CG  1 
ATOM   1552 C CD1 . LEU A 1 196 ? 5.141   -8.438  43.179  1.00 48.49  ? 196 LEU A CD1 1 
ATOM   1553 C CD2 . LEU A 1 196 ? 7.459   -8.959  43.996  1.00 49.34  ? 196 LEU A CD2 1 
ATOM   1554 N N   . LEU A 1 197 ? 8.014   -10.178 47.150  1.00 46.81  ? 197 LEU A N   1 
ATOM   1555 C CA  . LEU A 1 197 ? 9.473   -10.313 47.330  1.00 47.18  ? 197 LEU A CA  1 
ATOM   1556 C C   . LEU A 1 197 ? 9.870   -11.642 47.943  1.00 47.89  ? 197 LEU A C   1 
ATOM   1557 O O   . LEU A 1 197 ? 10.887  -12.224 47.548  1.00 48.55  ? 197 LEU A O   1 
ATOM   1558 C CB  . LEU A 1 197 ? 10.064  -9.128  48.124  1.00 47.44  ? 197 LEU A CB  1 
ATOM   1559 C CG  . LEU A 1 197 ? 9.831   -7.719  47.603  1.00 47.73  ? 197 LEU A CG  1 
ATOM   1560 C CD1 . LEU A 1 197 ? 10.382  -6.673  48.539  1.00 46.63  ? 197 LEU A CD1 1 
ATOM   1561 C CD2 . LEU A 1 197 ? 10.429  -7.490  46.190  1.00 49.40  ? 197 LEU A CD2 1 
ATOM   1562 N N   . ASP A 1 198 ? 9.050   -12.146 48.882  1.00 47.84  ? 198 ASP A N   1 
ATOM   1563 C CA  . ASP A 1 198 ? 9.358   -13.364 49.603  1.00 47.25  ? 198 ASP A CA  1 
ATOM   1564 C C   . ASP A 1 198 ? 9.011   -14.631 48.857  1.00 46.83  ? 198 ASP A C   1 
ATOM   1565 O O   . ASP A 1 198 ? 9.338   -15.706 49.345  1.00 46.96  ? 198 ASP A O   1 
ATOM   1566 C CB  . ASP A 1 198 ? 8.648   -13.388 50.964  1.00 48.07  ? 198 ASP A CB  1 
ATOM   1567 C CG  . ASP A 1 198 ? 9.221   -12.369 51.939  1.00 47.91  ? 198 ASP A CG  1 
ATOM   1568 O OD1 . ASP A 1 198 ? 10.384  -11.965 51.780  1.00 45.88  ? 198 ASP A OD1 1 
ATOM   1569 O OD2 . ASP A 1 198 ? 8.524   -12.023 52.908  1.00 52.27  ? 198 ASP A OD2 1 
ATOM   1570 N N   . VAL A 1 199 ? 8.323   -14.533 47.711  1.00 45.82  ? 199 VAL A N   1 
ATOM   1571 C CA  . VAL A 1 199 ? 8.140   -15.685 46.833  1.00 45.01  ? 199 VAL A CA  1 
ATOM   1572 C C   . VAL A 1 199 ? 8.959   -15.579 45.541  1.00 43.98  ? 199 VAL A C   1 
ATOM   1573 O O   . VAL A 1 199 ? 8.784   -16.388 44.637  1.00 42.89  ? 199 VAL A O   1 
ATOM   1574 C CB  . VAL A 1 199 ? 6.627   -15.961 46.473  1.00 45.41  ? 199 VAL A CB  1 
ATOM   1575 C CG1 . VAL A 1 199 ? 5.798   -16.074 47.718  1.00 46.38  ? 199 VAL A CG1 1 
ATOM   1576 C CG2 . VAL A 1 199 ? 6.057   -14.877 45.559  1.00 46.13  ? 199 VAL A CG2 1 
ATOM   1577 N N   . ASN A 1 200 ? 9.844   -14.593 45.441  1.00 43.15  ? 200 ASN A N   1 
ATOM   1578 C CA  . ASN A 1 200 ? 10.611  -14.413 44.220  1.00 43.04  ? 200 ASN A CA  1 
ATOM   1579 C C   . ASN A 1 200 ? 11.667  -15.511 44.207  1.00 43.07  ? 200 ASN A C   1 
ATOM   1580 O O   . ASN A 1 200 ? 12.089  -15.971 45.282  1.00 41.88  ? 200 ASN A O   1 
ATOM   1581 C CB  . ASN A 1 200 ? 11.118  -12.952 44.083  1.00 42.83  ? 200 ASN A CB  1 
ATOM   1582 C CG  . ASN A 1 200 ? 12.613  -12.770 44.380  1.00 43.27  ? 200 ASN A CG  1 
ATOM   1583 O OD1 . ASN A 1 200 ? 13.461  -13.119 43.562  1.00 44.66  ? 200 ASN A OD1 1 
ATOM   1584 N ND2 . ASN A 1 200 ? 12.931  -12.174 45.535  1.00 41.11  ? 200 ASN A ND2 1 
ATOM   1585 N N   . PRO A 1 201 ? 12.001  -16.042 43.004  1.00 42.50  ? 201 PRO A N   1 
ATOM   1586 C CA  . PRO A 1 201 ? 12.952  -17.143 42.883  1.00 42.01  ? 201 PRO A CA  1 
ATOM   1587 C C   . PRO A 1 201 ? 14.331  -16.940 43.537  1.00 41.57  ? 201 PRO A C   1 
ATOM   1588 O O   . PRO A 1 201 ? 14.930  -17.898 43.978  1.00 40.47  ? 201 PRO A O   1 
ATOM   1589 C CB  . PRO A 1 201 ? 13.092  -17.336 41.353  1.00 42.28  ? 201 PRO A CB  1 
ATOM   1590 C CG  . PRO A 1 201 ? 12.459  -16.215 40.733  1.00 42.64  ? 201 PRO A CG  1 
ATOM   1591 C CD  . PRO A 1 201 ? 11.467  -15.646 41.691  1.00 42.73  ? 201 PRO A CD  1 
ATOM   1592 N N   . LYS A 1 202 ? 14.838  -15.716 43.573  1.00 41.92  ? 202 LYS A N   1 
ATOM   1593 C CA  . LYS A 1 202 ? 16.098  -15.441 44.269  1.00 42.82  ? 202 LYS A CA  1 
ATOM   1594 C C   . LYS A 1 202 ? 16.011  -15.647 45.804  1.00 43.45  ? 202 LYS A C   1 
ATOM   1595 O O   . LYS A 1 202 ? 17.001  -15.962 46.433  1.00 43.32  ? 202 LYS A O   1 
ATOM   1596 C CB  . LYS A 1 202 ? 16.541  -14.011 43.986  1.00 42.65  ? 202 LYS A CB  1 
ATOM   1597 C CG  . LYS A 1 202 ? 16.944  -13.796 42.498  1.00 43.20  ? 202 LYS A CG  1 
ATOM   1598 C CD  . LYS A 1 202 ? 17.560  -12.404 42.342  1.00 41.85  ? 202 LYS A CD  1 
ATOM   1599 C CE  . LYS A 1 202 ? 18.309  -12.255 41.004  1.00 43.42  ? 202 LYS A CE  1 
ATOM   1600 N NZ  . LYS A 1 202 ? 19.053  -10.978 40.976  1.00 42.95  ? 202 LYS A NZ  1 
ATOM   1601 N N   . PHE A 1 203 ? 14.830  -15.422 46.373  1.00 44.13  ? 203 PHE A N   1 
ATOM   1602 C CA  . PHE A 1 203 ? 14.552  -15.689 47.794  1.00 43.70  ? 203 PHE A CA  1 
ATOM   1603 C C   . PHE A 1 203 ? 14.503  -17.165 48.027  1.00 44.44  ? 203 PHE A C   1 
ATOM   1604 O O   . PHE A 1 203 ? 15.008  -17.631 49.043  1.00 42.84  ? 203 PHE A O   1 
ATOM   1605 C CB  . PHE A 1 203 ? 13.212  -15.061 48.198  1.00 44.63  ? 203 PHE A CB  1 
ATOM   1606 C CG  . PHE A 1 203 ? 12.866  -15.195 49.681  1.00 43.85  ? 203 PHE A CG  1 
ATOM   1607 C CD1 . PHE A 1 203 ? 13.284  -14.247 50.592  1.00 45.62  ? 203 PHE A CD1 1 
ATOM   1608 C CD2 . PHE A 1 203 ? 12.079  -16.229 50.124  1.00 44.95  ? 203 PHE A CD2 1 
ATOM   1609 C CE1 . PHE A 1 203 ? 12.912  -14.345 51.935  1.00 45.49  ? 203 PHE A CE1 1 
ATOM   1610 C CE2 . PHE A 1 203 ? 11.724  -16.336 51.465  1.00 46.47  ? 203 PHE A CE2 1 
ATOM   1611 C CZ  . PHE A 1 203 ? 12.147  -15.406 52.356  1.00 44.38  ? 203 PHE A CZ  1 
ATOM   1612 N N   . LEU A 1 204 ? 13.927  -17.925 47.094  1.00 44.61  ? 204 LEU A N   1 
ATOM   1613 C CA  . LEU A 1 204 ? 13.933  -19.374 47.247  1.00 45.09  ? 204 LEU A CA  1 
ATOM   1614 C C   . LEU A 1 204 ? 15.347  -19.925 47.119  1.00 45.04  ? 204 LEU A C   1 
ATOM   1615 O O   . LEU A 1 204 ? 15.694  -20.891 47.760  1.00 45.46  ? 204 LEU A O   1 
ATOM   1616 C CB  . LEU A 1 204 ? 12.997  -20.081 46.246  1.00 46.15  ? 204 LEU A CB  1 
ATOM   1617 C CG  . LEU A 1 204 ? 11.628  -19.438 45.989  1.00 48.71  ? 204 LEU A CG  1 
ATOM   1618 C CD1 . LEU A 1 204 ? 10.731  -20.437 45.273  1.00 49.10  ? 204 LEU A CD1 1 
ATOM   1619 C CD2 . LEU A 1 204 ? 10.980  -18.939 47.289  1.00 49.31  ? 204 LEU A CD2 1 
ATOM   1620 N N   . LYS A 1 205 ? 16.160  -19.327 46.266  1.00 45.37  ? 205 LYS A N   1 
ATOM   1621 C CA  . LYS A 1 205 ? 17.520  -19.819 46.035  1.00 45.47  ? 205 LYS A CA  1 
ATOM   1622 C C   . LYS A 1 205 ? 18.422  -19.512 47.244  1.00 44.64  ? 205 LYS A C   1 
ATOM   1623 O O   . LYS A 1 205 ? 19.254  -20.309 47.617  1.00 44.53  ? 205 LYS A O   1 
ATOM   1624 C CB  . LYS A 1 205 ? 18.062  -19.204 44.726  1.00 46.03  ? 205 LYS A CB  1 
ATOM   1625 C CG  . LYS A 1 205 ? 19.587  -19.179 44.538  1.00 46.64  ? 205 LYS A CG  1 
ATOM   1626 C CD  . LYS A 1 205 ? 19.920  -18.981 43.042  1.00 48.60  ? 205 LYS A CD  1 
ATOM   1627 C CE  . LYS A 1 205 ? 21.419  -18.726 42.751  1.00 50.55  ? 205 LYS A CE  1 
ATOM   1628 N NZ  . LYS A 1 205 ? 21.679  -17.265 42.417  1.00 52.25  ? 205 LYS A NZ  1 
ATOM   1629 N N   . ASN A 1 206 ? 18.229  -18.349 47.850  1.00 44.62  ? 206 ASN A N   1 
ATOM   1630 C CA  . ASN A 1 206 ? 19.032  -17.901 48.984  1.00 44.44  ? 206 ASN A CA  1 
ATOM   1631 C C   . ASN A 1 206 ? 18.283  -16.784 49.710  1.00 43.89  ? 206 ASN A C   1 
ATOM   1632 O O   . ASN A 1 206 ? 18.500  -15.632 49.409  1.00 43.58  ? 206 ASN A O   1 
ATOM   1633 C CB  . ASN A 1 206 ? 20.391  -17.356 48.495  1.00 44.44  ? 206 ASN A CB  1 
ATOM   1634 C CG  . ASN A 1 206 ? 21.423  -17.214 49.624  1.00 44.98  ? 206 ASN A CG  1 
ATOM   1635 O OD1 . ASN A 1 206 ? 22.632  -17.310 49.388  1.00 46.06  ? 206 ASN A OD1 1 
ATOM   1636 N ND2 . ASN A 1 206 ? 20.947  -17.039 50.850  1.00 38.30  ? 206 ASN A ND2 1 
ATOM   1637 N N   . ALA A 1 207 ? 17.414  -17.106 50.675  1.00 43.16  ? 207 ALA A N   1 
ATOM   1638 C CA  . ALA A 1 207 ? 16.602  -16.042 51.300  1.00 43.05  ? 207 ALA A CA  1 
ATOM   1639 C C   . ALA A 1 207 ? 17.452  -15.078 52.117  1.00 42.50  ? 207 ALA A C   1 
ATOM   1640 O O   . ALA A 1 207 ? 17.192  -13.899 52.129  1.00 41.78  ? 207 ALA A O   1 
ATOM   1641 C CB  . ALA A 1 207 ? 15.500  -16.628 52.152  1.00 44.10  ? 207 ALA A CB  1 
ATOM   1642 N N   . GLY A 1 208 ? 18.489  -15.555 52.800  1.00 42.78  ? 208 GLY A N   1 
ATOM   1643 C CA  . GLY A 1 208 ? 19.318  -14.598 53.582  1.00 42.71  ? 208 GLY A CA  1 
ATOM   1644 C C   . GLY A 1 208 ? 19.963  -13.546 52.701  1.00 42.19  ? 208 GLY A C   1 
ATOM   1645 O O   . GLY A 1 208 ? 19.954  -12.332 53.007  1.00 41.42  ? 208 GLY A O   1 
ATOM   1646 N N   . ARG A 1 209 ? 20.512  -13.993 51.577  1.00 42.74  ? 209 ARG A N   1 
ATOM   1647 C CA  . ARG A 1 209 ? 21.115  -13.065 50.608  1.00 43.60  ? 209 ARG A CA  1 
ATOM   1648 C C   . ARG A 1 209 ? 20.057  -12.188 49.969  1.00 43.21  ? 209 ARG A C   1 
ATOM   1649 O O   . ARG A 1 209 ? 20.206  -10.953 49.823  1.00 43.99  ? 209 ARG A O   1 
ATOM   1650 C CB  . ARG A 1 209 ? 21.886  -13.862 49.540  1.00 43.73  ? 209 ARG A CB  1 
ATOM   1651 C CG  . ARG A 1 209 ? 22.693  -12.981 48.632  1.00 44.21  ? 209 ARG A CG  1 
ATOM   1652 C CD  . ARG A 1 209 ? 23.135  -13.705 47.382  1.00 47.71  ? 209 ARG A CD  1 
ATOM   1653 N NE  . ARG A 1 209 ? 23.524  -12.710 46.383  1.00 51.19  ? 209 ARG A NE  1 
ATOM   1654 C CZ  . ARG A 1 209 ? 24.723  -12.136 46.307  1.00 53.51  ? 209 ARG A CZ  1 
ATOM   1655 N NH1 . ARG A 1 209 ? 25.691  -12.447 47.163  1.00 53.91  ? 209 ARG A NH1 1 
ATOM   1656 N NH2 . ARG A 1 209 ? 24.964  -11.242 45.360  1.00 53.39  ? 209 ARG A NH2 1 
ATOM   1657 N N   . ASP A 1 210 ? 18.936  -12.786 49.609  1.00 43.90  ? 210 ASP A N   1 
ATOM   1658 C CA  . ASP A 1 210 ? 17.870  -11.981 48.988  1.00 43.11  ? 210 ASP A CA  1 
ATOM   1659 C C   . ASP A 1 210 ? 17.454  -10.813 49.880  1.00 43.58  ? 210 ASP A C   1 
ATOM   1660 O O   . ASP A 1 210 ? 17.303  -9.676  49.416  1.00 42.01  ? 210 ASP A O   1 
ATOM   1661 C CB  . ASP A 1 210 ? 16.659  -12.852 48.622  1.00 43.69  ? 210 ASP A CB  1 
ATOM   1662 C CG  . ASP A 1 210 ? 15.571  -12.060 47.974  1.00 45.21  ? 210 ASP A CG  1 
ATOM   1663 O OD1 . ASP A 1 210 ? 14.688  -11.582 48.701  1.00 47.11  ? 210 ASP A OD1 1 
ATOM   1664 O OD2 . ASP A 1 210 ? 15.649  -11.800 46.740  1.00 46.59  ? 210 ASP A OD2 1 
ATOM   1665 N N   . CYS A 1 211 ? 17.227  -11.081 51.167  1.00 43.15  ? 211 CYS A N   1 
ATOM   1666 C CA  . CYS A 1 211 ? 16.816  -10.010 52.081  1.00 43.38  ? 211 CYS A CA  1 
ATOM   1667 C C   . CYS A 1 211 ? 17.898  -8.972  52.284  1.00 42.14  ? 211 CYS A C   1 
ATOM   1668 O O   . CYS A 1 211 ? 17.604  -7.801  52.389  1.00 44.74  ? 211 CYS A O   1 
ATOM   1669 C CB  . CYS A 1 211 ? 16.391  -10.613 53.435  1.00 43.29  ? 211 CYS A CB  1 
ATOM   1670 S SG  . CYS A 1 211 ? 14.951  -11.645 53.280  1.00 47.49  ? 211 CYS A SG  1 
ATOM   1671 N N   . SER A 1 212 ? 19.149  -9.388  52.259  1.00 42.58  ? 212 SER A N   1 
ATOM   1672 C CA  . SER A 1 212 ? 20.295  -8.471  52.325  1.00 43.25  ? 212 SER A CA  1 
ATOM   1673 C C   . SER A 1 212 ? 20.337  -7.554  51.112  1.00 43.04  ? 212 SER A C   1 
ATOM   1674 O O   . SER A 1 212 ? 20.505  -6.307  51.228  1.00 41.81  ? 212 SER A O   1 
ATOM   1675 C CB  . SER A 1 212 ? 21.602  -9.272  52.375  1.00 43.58  ? 212 SER A CB  1 
ATOM   1676 O OG  . SER A 1 212 ? 22.694  -8.392  52.632  1.00 45.50  ? 212 SER A OG  1 
ATOM   1677 N N   . ARG A 1 213 ? 20.153  -8.151  49.922  1.00 43.62  ? 213 ARG A N   1 
ATOM   1678 C CA  . ARG A 1 213 ? 20.139  -7.353  48.668  1.00 43.67  ? 213 ARG A CA  1 
ATOM   1679 C C   . ARG A 1 213 ? 19.000  -6.365  48.532  1.00 44.46  ? 213 ARG A C   1 
ATOM   1680 O O   . ARG A 1 213 ? 19.014  -5.485  47.655  1.00 44.14  ? 213 ARG A O   1 
ATOM   1681 C CB  . ARG A 1 213 ? 20.139  -8.296  47.457  1.00 43.93  ? 213 ARG A CB  1 
ATOM   1682 C CG  . ARG A 1 213 ? 21.338  -9.177  47.358  1.00 45.60  ? 213 ARG A CG  1 
ATOM   1683 C CD  . ARG A 1 213 ? 22.591  -8.370  47.121  1.00 51.06  ? 213 ARG A CD  1 
ATOM   1684 N NE  . ARG A 1 213 ? 22.645  -7.847  45.753  1.00 54.13  ? 213 ARG A NE  1 
ATOM   1685 C CZ  . ARG A 1 213 ? 22.560  -6.561  45.397  1.00 54.45  ? 213 ARG A CZ  1 
ATOM   1686 N NH1 . ARG A 1 213 ? 22.420  -5.583  46.286  1.00 53.79  ? 213 ARG A NH1 1 
ATOM   1687 N NH2 . ARG A 1 213 ? 22.629  -6.252  44.111  1.00 57.10  ? 213 ARG A NH2 1 
ATOM   1688 N N   . ARG A 1 214 ? 17.972  -6.509  49.356  1.00 45.18  ? 214 ARG A N   1 
ATOM   1689 C CA  . ARG A 1 214 ? 16.894  -5.550  49.386  1.00 44.30  ? 214 ARG A CA  1 
ATOM   1690 C C   . ARG A 1 214 ? 17.342  -4.185  49.931  1.00 44.94  ? 214 ARG A C   1 
ATOM   1691 O O   . ARG A 1 214 ? 16.552  -3.276  49.987  1.00 43.73  ? 214 ARG A O   1 
ATOM   1692 C CB  . ARG A 1 214 ? 15.710  -6.082  50.183  1.00 45.74  ? 214 ARG A CB  1 
ATOM   1693 C CG  . ARG A 1 214 ? 15.086  -7.280  49.595  1.00 44.56  ? 214 ARG A CG  1 
ATOM   1694 C CD  . ARG A 1 214 ? 13.966  -7.786  50.422  1.00 44.70  ? 214 ARG A CD  1 
ATOM   1695 N NE  . ARG A 1 214 ? 13.636  -9.141  50.035  1.00 42.47  ? 214 ARG A NE  1 
ATOM   1696 C CZ  . ARG A 1 214 ? 12.584  -9.822  50.482  1.00 45.52  ? 214 ARG A CZ  1 
ATOM   1697 N NH1 . ARG A 1 214 ? 11.752  -9.293  51.367  1.00 51.26  ? 214 ARG A NH1 1 
ATOM   1698 N NH2 . ARG A 1 214 ? 12.373  -11.040 50.075  1.00 46.64  ? 214 ARG A NH2 1 
ATOM   1699 N N   . SER A 1 215 ? 18.625  -4.006  50.222  1.00 44.92  ? 215 SER A N   1 
ATOM   1700 C CA  . SER A 1 215 ? 19.161  -2.639  50.352  1.00 45.62  ? 215 SER A CA  1 
ATOM   1701 C C   . SER A 1 215 ? 19.109  -1.855  49.057  1.00 46.40  ? 215 SER A C   1 
ATOM   1702 O O   . SER A 1 215 ? 19.109  -0.645  49.079  1.00 45.96  ? 215 SER A O   1 
ATOM   1703 C CB  . SER A 1 215 ? 20.599  -2.644  50.822  1.00 45.66  ? 215 SER A CB  1 
ATOM   1704 O OG  . SER A 1 215 ? 21.381  -3.573  50.085  1.00 48.32  ? 215 SER A OG  1 
ATOM   1705 N N   . SER A 1 216 ? 19.146  -2.555  47.927  1.00 46.71  ? 216 SER A N   1 
ATOM   1706 C CA  . SER A 1 216 ? 19.394  -1.894  46.632  1.00 46.73  ? 216 SER A CA  1 
ATOM   1707 C C   . SER A 1 216 ? 18.107  -1.709  45.867  1.00 46.15  ? 216 SER A C   1 
ATOM   1708 O O   . SER A 1 216 ? 17.377  -2.671  45.648  1.00 45.64  ? 216 SER A O   1 
ATOM   1709 C CB  . SER A 1 216 ? 20.290  -2.799  45.782  1.00 47.93  ? 216 SER A CB  1 
ATOM   1710 O OG  . SER A 1 216 ? 20.327  -2.322  44.455  1.00 47.99  ? 216 SER A OG  1 
ATOM   1711 N N   . PRO A 1 217 ? 17.863  -0.495  45.386  1.00 46.63  ? 217 PRO A N   1 
ATOM   1712 C CA  . PRO A 1 217 ? 16.709  -0.250  44.549  1.00 46.56  ? 217 PRO A CA  1 
ATOM   1713 C C   . PRO A 1 217 ? 16.912  -0.841  43.129  1.00 47.01  ? 217 PRO A C   1 
ATOM   1714 O O   . PRO A 1 217 ? 15.928  -1.023  42.421  1.00 47.46  ? 217 PRO A O   1 
ATOM   1715 C CB  . PRO A 1 217 ? 16.610  1.273   44.568  1.00 47.11  ? 217 PRO A CB  1 
ATOM   1716 C CG  . PRO A 1 217 ? 17.986  1.721   44.716  1.00 46.77  ? 217 PRO A CG  1 
ATOM   1717 C CD  . PRO A 1 217 ? 18.666  0.716   45.562  1.00 45.95  ? 217 PRO A CD  1 
ATOM   1718 N N   . VAL A 1 218 ? 18.157  -1.206  42.776  1.00 46.33  ? 218 VAL A N   1 
ATOM   1719 C CA  . VAL A 1 218 ? 18.469  -1.900  41.521  1.00 45.69  ? 218 VAL A CA  1 
ATOM   1720 C C   . VAL A 1 218 ? 17.968  -3.305  41.670  1.00 45.54  ? 218 VAL A C   1 
ATOM   1721 O O   . VAL A 1 218 ? 17.167  -3.764  40.871  1.00 46.07  ? 218 VAL A O   1 
ATOM   1722 C CB  . VAL A 1 218 ? 19.980  -1.908  41.204  1.00 44.96  ? 218 VAL A CB  1 
ATOM   1723 C CG1 . VAL A 1 218 ? 20.286  -2.821  40.025  1.00 45.38  ? 218 VAL A CG1 1 
ATOM   1724 C CG2 . VAL A 1 218 ? 20.487  -0.515  40.914  1.00 43.37  ? 218 VAL A CG2 1 
ATOM   1725 N N   . TYR A 1 219 ? 18.355  -3.956  42.767  1.00 45.09  ? 219 TYR A N   1 
ATOM   1726 C CA  . TYR A 1 219 ? 17.901  -5.303  43.063  1.00 45.06  ? 219 TYR A CA  1 
ATOM   1727 C C   . TYR A 1 219 ? 16.385  -5.380  43.164  1.00 44.58  ? 219 TYR A C   1 
ATOM   1728 O O   . TYR A 1 219 ? 15.781  -6.301  42.623  1.00 43.91  ? 219 TYR A O   1 
ATOM   1729 C CB  . TYR A 1 219 ? 18.532  -5.825  44.383  1.00 44.04  ? 219 TYR A CB  1 
ATOM   1730 C CG  . TYR A 1 219 ? 18.289  -7.284  44.647  1.00 44.81  ? 219 TYR A CG  1 
ATOM   1731 C CD1 . TYR A 1 219 ? 19.129  -8.250  44.117  1.00 42.12  ? 219 TYR A CD1 1 
ATOM   1732 C CD2 . TYR A 1 219 ? 17.230  -7.712  45.446  1.00 44.34  ? 219 TYR A CD2 1 
ATOM   1733 C CE1 . TYR A 1 219 ? 18.941  -9.566  44.370  1.00 44.89  ? 219 TYR A CE1 1 
ATOM   1734 C CE2 . TYR A 1 219 ? 17.035  -9.062  45.693  1.00 42.56  ? 219 TYR A CE2 1 
ATOM   1735 C CZ  . TYR A 1 219 ? 17.888  -9.980  45.167  1.00 41.45  ? 219 TYR A CZ  1 
ATOM   1736 O OH  . TYR A 1 219 ? 17.721  -11.329 45.374  1.00 43.82  ? 219 TYR A OH  1 
ATOM   1737 N N   . VAL A 1 220 ? 15.782  -4.460  43.902  1.00 44.88  ? 220 VAL A N   1 
ATOM   1738 C CA  . VAL A 1 220 ? 14.352  -4.549  44.206  1.00 45.58  ? 220 VAL A CA  1 
ATOM   1739 C C   . VAL A 1 220 ? 13.485  -4.152  42.985  1.00 46.31  ? 220 VAL A C   1 
ATOM   1740 O O   . VAL A 1 220 ? 12.447  -4.757  42.725  1.00 46.66  ? 220 VAL A O   1 
ATOM   1741 C CB  . VAL A 1 220 ? 13.974  -3.710  45.455  1.00 46.72  ? 220 VAL A CB  1 
ATOM   1742 C CG1 . VAL A 1 220 ? 12.444  -3.695  45.643  1.00 45.90  ? 220 VAL A CG1 1 
ATOM   1743 C CG2 . VAL A 1 220 ? 14.686  -4.308  46.719  1.00 46.16  ? 220 VAL A CG2 1 
ATOM   1744 N N   . GLY A 1 221 ? 13.928  -3.141  42.247  1.00 46.45  ? 221 GLY A N   1 
ATOM   1745 C CA  . GLY A 1 221 ? 13.335  -2.791  40.971  1.00 46.08  ? 221 GLY A CA  1 
ATOM   1746 C C   . GLY A 1 221 ? 13.297  -3.970  40.026  1.00 45.96  ? 221 GLY A C   1 
ATOM   1747 O O   . GLY A 1 221 ? 12.218  -4.323  39.538  1.00 46.08  ? 221 GLY A O   1 
ATOM   1748 N N   . ARG A 1 222 ? 14.451  -4.625  39.854  1.00 45.87  ? 222 ARG A N   1 
ATOM   1749 C CA  . ARG A 1 222 ? 14.594  -5.810  39.006  1.00 45.55  ? 222 ARG A CA  1 
ATOM   1750 C C   . ARG A 1 222 ? 13.656  -6.953  39.366  1.00 46.08  ? 222 ARG A C   1 
ATOM   1751 O O   . ARG A 1 222 ? 13.035  -7.576  38.498  1.00 44.23  ? 222 ARG A O   1 
ATOM   1752 C CB  . ARG A 1 222 ? 16.031  -6.303  39.048  1.00 45.86  ? 222 ARG A CB  1 
ATOM   1753 C CG  . ARG A 1 222 ? 16.326  -7.507  38.155  1.00 45.30  ? 222 ARG A CG  1 
ATOM   1754 C CD  . ARG A 1 222 ? 17.764  -7.553  37.645  1.00 45.35  ? 222 ARG A CD  1 
ATOM   1755 N NE  . ARG A 1 222 ? 18.100  -8.789  36.925  1.00 44.08  ? 222 ARG A NE  1 
ATOM   1756 C CZ  . ARG A 1 222 ? 17.994  -8.991  35.601  1.00 46.35  ? 222 ARG A CZ  1 
ATOM   1757 N NH1 . ARG A 1 222 ? 17.502  -8.066  34.802  1.00 46.11  ? 222 ARG A NH1 1 
ATOM   1758 N NH2 . ARG A 1 222 ? 18.357  -10.156 35.065  1.00 44.88  ? 222 ARG A NH2 1 
ATOM   1759 N N   . VAL A 1 223 ? 13.595  -7.260  40.661  1.00 45.50  ? 223 VAL A N   1 
ATOM   1760 C CA  . VAL A 1 223 ? 12.745  -8.306  41.182  1.00 45.33  ? 223 VAL A CA  1 
ATOM   1761 C C   . VAL A 1 223 ? 11.265  -7.904  41.111  1.00 45.53  ? 223 VAL A C   1 
ATOM   1762 O O   . VAL A 1 223 ? 10.409  -8.704  40.682  1.00 44.83  ? 223 VAL A O   1 
ATOM   1763 C CB  . VAL A 1 223 ? 13.096  -8.586  42.658  1.00 44.80  ? 223 VAL A CB  1 
ATOM   1764 C CG1 . VAL A 1 223 ? 12.022  -9.405  43.274  1.00 44.94  ? 223 VAL A CG1 1 
ATOM   1765 C CG2 . VAL A 1 223 ? 14.456  -9.279  42.762  1.00 44.70  ? 223 VAL A CG2 1 
ATOM   1766 N N   . GLY A 1 224 ? 10.996  -6.679  41.540  1.00 46.00  ? 224 GLY A N   1 
ATOM   1767 C CA  . GLY A 1 224 ? 9.656   -6.118  41.616  1.00 47.24  ? 224 GLY A CA  1 
ATOM   1768 C C   . GLY A 1 224 ? 8.986   -6.099  40.245  1.00 47.67  ? 224 GLY A C   1 
ATOM   1769 O O   . GLY A 1 224 ? 7.968   -6.755  40.048  1.00 48.51  ? 224 GLY A O   1 
ATOM   1770 N N   . SER A 1 225 ? 9.563   -5.362  39.307  1.00 48.07  ? 225 SER A N   1 
ATOM   1771 C CA  . SER A 1 225 ? 9.115   -5.434  37.895  1.00 48.35  ? 225 SER A CA  1 
ATOM   1772 C C   . SER A 1 225 ? 9.133   -6.857  37.356  1.00 48.73  ? 225 SER A C   1 
ATOM   1773 O O   . SER A 1 225 ? 8.143   -7.352  36.746  1.00 48.75  ? 225 SER A O   1 
ATOM   1774 C CB  . SER A 1 225 ? 10.006  -4.521  37.032  1.00 48.43  ? 225 SER A CB  1 
ATOM   1775 O OG  . SER A 1 225 ? 9.474   -4.369  35.722  1.00 49.51  ? 225 SER A OG  1 
ATOM   1776 N N   . GLY A 1 226 ? 10.248  -7.548  37.580  1.00 48.86  ? 226 GLY A N   1 
ATOM   1777 C CA  . GLY A 1 226 ? 10.444  -8.876  37.011  1.00 48.89  ? 226 GLY A CA  1 
ATOM   1778 C C   . GLY A 1 226 ? 9.424   -9.904  37.444  1.00 49.71  ? 226 GLY A C   1 
ATOM   1779 O O   . GLY A 1 226 ? 9.187   -10.909 36.746  1.00 49.31  ? 226 GLY A O   1 
ATOM   1780 N N   . MET A 1 227 ? 8.815   -9.673  38.605  1.00 49.77  ? 227 MET A N   1 
ATOM   1781 C CA  . MET A 1 227 ? 7.865   -10.626 39.180  1.00 50.34  ? 227 MET A CA  1 
ATOM   1782 C C   . MET A 1 227 ? 6.443   -10.448 38.655  1.00 51.05  ? 227 MET A C   1 
ATOM   1783 O O   . MET A 1 227 ? 5.574   -11.276 38.901  1.00 51.13  ? 227 MET A O   1 
ATOM   1784 C CB  . MET A 1 227 ? 7.865   -10.492 40.716  1.00 50.34  ? 227 MET A CB  1 
ATOM   1785 C CG  . MET A 1 227 ? 8.965   -11.330 41.394  1.00 49.14  ? 227 MET A CG  1 
ATOM   1786 S SD  . MET A 1 227 ? 8.680   -13.055 41.219  1.00 50.46  ? 227 MET A SD  1 
ATOM   1787 C CE  . MET A 1 227 ? 7.091   -13.270 42.008  1.00 51.83  ? 227 MET A CE  1 
ATOM   1788 N N   . VAL A 1 228 ? 6.206   -9.367  37.929  1.00 52.26  ? 228 VAL A N   1 
ATOM   1789 C CA  . VAL A 1 228 ? 4.846   -9.021  37.520  1.00 53.81  ? 228 VAL A CA  1 
ATOM   1790 C C   . VAL A 1 228 ? 4.392   -9.946  36.417  1.00 55.02  ? 228 VAL A C   1 
ATOM   1791 O O   . VAL A 1 228 ? 3.261   -10.410 36.419  1.00 54.79  ? 228 VAL A O   1 
ATOM   1792 C CB  . VAL A 1 228 ? 4.724   -7.567  37.056  1.00 52.94  ? 228 VAL A CB  1 
ATOM   1793 C CG1 . VAL A 1 228 ? 3.324   -7.325  36.458  1.00 51.97  ? 228 VAL A CG1 1 
ATOM   1794 C CG2 . VAL A 1 228 ? 4.994   -6.624  38.216  1.00 52.63  ? 228 VAL A CG2 1 
ATOM   1795 N N   . ASN A 1 229 ? 5.288   -10.201 35.476  1.00 57.86  ? 229 ASN A N   1 
ATOM   1796 C CA  . ASN A 1 229 ? 5.041   -11.192 34.448  1.00 59.33  ? 229 ASN A CA  1 
ATOM   1797 C C   . ASN A 1 229 ? 6.201   -12.161 34.398  1.00 62.04  ? 229 ASN A C   1 
ATOM   1798 O O   . ASN A 1 229 ? 7.093   -12.041 33.550  1.00 62.96  ? 229 ASN A O   1 
ATOM   1799 C CB  . ASN A 1 229 ? 4.852   -10.530 33.093  1.00 59.72  ? 229 ASN A CB  1 
ATOM   1800 C CG  . ASN A 1 229 ? 4.238   -11.467 32.078  1.00 59.74  ? 229 ASN A CG  1 
ATOM   1801 O OD1 . ASN A 1 229 ? 3.698   -11.016 31.080  1.00 61.62  ? 229 ASN A OD1 1 
ATOM   1802 N ND2 . ASN A 1 229 ? 4.312   -12.778 32.332  1.00 58.81  ? 229 ASN A ND2 1 
ATOM   1803 N N   . CYS A 1 230 ? 6.165   -13.134 35.297  1.00 64.25  ? 230 CYS A N   1 
ATOM   1804 C CA  . CYS A 1 230 ? 7.328   -13.950 35.564  1.00 65.52  ? 230 CYS A CA  1 
ATOM   1805 C C   . CYS A 1 230 ? 7.134   -15.326 34.952  1.00 66.32  ? 230 CYS A C   1 
ATOM   1806 O O   . CYS A 1 230 ? 6.163   -16.019 35.265  1.00 66.64  ? 230 CYS A O   1 
ATOM   1807 C CB  . CYS A 1 230 ? 7.543   -14.059 37.069  1.00 65.02  ? 230 CYS A CB  1 
ATOM   1808 S SG  . CYS A 1 230 ? 9.116   -14.807 37.560  1.00 66.16  ? 230 CYS A SG  1 
ATOM   1809 N N   . ASN A 1 231 ? 8.075   -15.713 34.092  1.00 67.04  ? 231 ASN A N   1 
ATOM   1810 C CA  . ASN A 1 231 ? 8.132   -17.062 33.509  1.00 67.53  ? 231 ASN A CA  1 
ATOM   1811 C C   . ASN A 1 231 ? 7.777   -18.211 34.476  1.00 67.78  ? 231 ASN A C   1 
ATOM   1812 O O   . ASN A 1 231 ? 7.239   -19.237 34.068  1.00 67.73  ? 231 ASN A O   1 
ATOM   1813 C CB  . ASN A 1 231 ? 9.543   -17.283 32.952  1.00 68.14  ? 231 ASN A CB  1 
ATOM   1814 C CG  . ASN A 1 231 ? 9.559   -18.118 31.698  1.00 68.70  ? 231 ASN A CG  1 
ATOM   1815 O OD1 . ASN A 1 231 ? 10.337  -19.069 31.589  1.00 71.00  ? 231 ASN A OD1 1 
ATOM   1816 N ND2 . ASN A 1 231 ? 8.717   -17.760 30.727  1.00 69.57  ? 231 ASN A ND2 1 
ATOM   1817 N N   . ASP A 1 232 ? 8.091   -18.035 35.753  1.00 68.06  ? 232 ASP A N   1 
ATOM   1818 C CA  . ASP A 1 232 ? 7.702   -18.992 36.790  1.00 67.95  ? 232 ASP A CA  1 
ATOM   1819 C C   . ASP A 1 232 ? 6.214   -18.790 37.114  1.00 67.51  ? 232 ASP A C   1 
ATOM   1820 O O   . ASP A 1 232 ? 5.650   -17.719 36.877  1.00 67.63  ? 232 ASP A O   1 
ATOM   1821 C CB  . ASP A 1 232 ? 8.558   -18.806 38.061  1.00 68.85  ? 232 ASP A CB  1 
ATOM   1822 C CG  . ASP A 1 232 ? 10.006  -18.377 37.757  1.00 70.60  ? 232 ASP A CG  1 
ATOM   1823 O OD1 . ASP A 1 232 ? 10.906  -18.643 38.582  1.00 72.78  ? 232 ASP A OD1 1 
ATOM   1824 O OD2 . ASP A 1 232 ? 10.246  -17.762 36.690  1.00 74.27  ? 232 ASP A OD2 1 
ATOM   1825 N N   . ASP A 1 233 ? 5.576   -19.812 37.672  1.00 66.77  ? 233 ASP A N   1 
ATOM   1826 C CA  . ASP A 1 233 ? 4.123   -19.765 37.861  1.00 65.90  ? 233 ASP A CA  1 
ATOM   1827 C C   . ASP A 1 233 ? 3.664   -18.793 38.942  1.00 64.92  ? 233 ASP A C   1 
ATOM   1828 O O   . ASP A 1 233 ? 2.456   -18.562 39.065  1.00 64.84  ? 233 ASP A O   1 
ATOM   1829 C CB  . ASP A 1 233 ? 3.546   -21.168 38.123  1.00 66.36  ? 233 ASP A CB  1 
ATOM   1830 C CG  . ASP A 1 233 ? 3.930   -21.736 39.489  1.00 67.34  ? 233 ASP A CG  1 
ATOM   1831 O OD1 . ASP A 1 233 ? 3.391   -22.814 39.837  1.00 69.65  ? 233 ASP A OD1 1 
ATOM   1832 O OD2 . ASP A 1 233 ? 4.764   -21.141 40.205  1.00 68.44  ? 233 ASP A OD2 1 
ATOM   1833 N N   . GLN A 1 234 ? 4.612   -18.232 39.712  1.00 63.33  ? 234 GLN A N   1 
ATOM   1834 C CA  . GLN A 1 234 ? 4.278   -17.342 40.832  1.00 62.19  ? 234 GLN A CA  1 
ATOM   1835 C C   . GLN A 1 234 ? 4.244   -15.870 40.467  1.00 60.66  ? 234 GLN A C   1 
ATOM   1836 O O   . GLN A 1 234 ? 4.040   -15.049 41.339  1.00 60.72  ? 234 GLN A O   1 
ATOM   1837 C CB  . GLN A 1 234 ? 5.205   -17.564 42.053  1.00 62.43  ? 234 GLN A CB  1 
ATOM   1838 C CG  . GLN A 1 234 ? 6.602   -16.915 41.975  1.00 63.72  ? 234 GLN A CG  1 
ATOM   1839 C CD  . GLN A 1 234 ? 7.727   -17.914 41.737  1.00 65.71  ? 234 GLN A CD  1 
ATOM   1840 O OE1 . GLN A 1 234 ? 7.620   -18.822 40.898  1.00 66.90  ? 234 GLN A OE1 1 
ATOM   1841 N NE2 . GLN A 1 234 ? 8.820   -17.746 42.475  1.00 66.15  ? 234 GLN A NE2 1 
ATOM   1842 N N   . GLY A 1 235 ? 4.434   -15.527 39.194  1.00 59.05  ? 235 GLY A N   1 
ATOM   1843 C CA  . GLY A 1 235 ? 4.295   -14.131 38.751  1.00 57.52  ? 235 GLY A CA  1 
ATOM   1844 C C   . GLY A 1 235 ? 2.883   -13.566 38.884  1.00 55.89  ? 235 GLY A C   1 
ATOM   1845 O O   . GLY A 1 235 ? 1.924   -14.310 39.072  1.00 55.59  ? 235 GLY A O   1 
ATOM   1846 N N   . VAL A 1 236 ? 2.733   -12.245 38.777  1.00 54.43  ? 236 VAL A N   1 
ATOM   1847 C CA  . VAL A 1 236 ? 1.419   -11.643 39.046  1.00 53.74  ? 236 VAL A CA  1 
ATOM   1848 C C   . VAL A 1 236 ? 0.390   -11.834 37.906  1.00 52.95  ? 236 VAL A C   1 
ATOM   1849 O O   . VAL A 1 236 ? -0.769  -12.158 38.171  1.00 51.81  ? 236 VAL A O   1 
ATOM   1850 C CB  . VAL A 1 236 ? 1.517   -10.167 39.449  1.00 53.16  ? 236 VAL A CB  1 
ATOM   1851 C CG1 . VAL A 1 236 ? 0.133   -9.623  39.744  1.00 52.45  ? 236 VAL A CG1 1 
ATOM   1852 C CG2 . VAL A 1 236 ? 2.418   -10.009 40.666  1.00 52.02  ? 236 VAL A CG2 1 
ATOM   1853 N N   . LEU A 1 237 ? 0.828   -11.674 36.656  1.00 53.06  ? 237 LEU A N   1 
ATOM   1854 C CA  . LEU A 1 237 ? -0.074  -11.664 35.489  1.00 53.24  ? 237 LEU A CA  1 
ATOM   1855 C C   . LEU A 1 237 ? 0.332   -12.650 34.391  1.00 53.64  ? 237 LEU A C   1 
ATOM   1856 O O   . LEU A 1 237 ? 1.512   -12.980 34.265  1.00 54.07  ? 237 LEU A O   1 
ATOM   1857 C CB  . LEU A 1 237 ? -0.102  -10.260 34.895  1.00 52.74  ? 237 LEU A CB  1 
ATOM   1858 C CG  . LEU A 1 237 ? -0.870  -9.197  35.677  1.00 52.88  ? 237 LEU A CG  1 
ATOM   1859 C CD1 . LEU A 1 237 ? -0.401  -7.788  35.306  1.00 51.13  ? 237 LEU A CD1 1 
ATOM   1860 C CD2 . LEU A 1 237 ? -2.372  -9.326  35.453  1.00 52.02  ? 237 LEU A CD2 1 
ATOM   1861 N N   . LEU A 1 238 ? -0.655  -13.113 33.610  1.00 53.66  ? 238 LEU A N   1 
ATOM   1862 C CA  . LEU A 1 238 ? -0.416  -13.862 32.362  1.00 53.88  ? 238 LEU A CA  1 
ATOM   1863 C C   . LEU A 1 238 ? -0.844  -13.050 31.137  1.00 54.06  ? 238 LEU A C   1 
ATOM   1864 O O   . LEU A 1 238 ? -1.960  -12.530 31.089  1.00 53.95  ? 238 LEU A O   1 
ATOM   1865 C CB  . LEU A 1 238 ? -1.178  -15.191 32.362  1.00 53.78  ? 238 LEU A CB  1 
ATOM   1866 C CG  . LEU A 1 238 ? -0.993  -16.094 31.133  1.00 53.90  ? 238 LEU A CG  1 
ATOM   1867 C CD1 . LEU A 1 238 ? 0.458   -16.511 30.945  1.00 53.74  ? 238 LEU A CD1 1 
ATOM   1868 C CD2 . LEU A 1 238 ? -1.877  -17.323 31.238  1.00 53.63  ? 238 LEU A CD2 1 
ATOM   1869 N N   . GLY A 1 239 ? 0.045   -12.953 30.150  1.00 54.36  ? 239 GLY A N   1 
ATOM   1870 C CA  . GLY A 1 239 ? -0.208  -12.147 28.953  1.00 54.72  ? 239 GLY A CA  1 
ATOM   1871 C C   . GLY A 1 239 ? -1.126  -12.879 27.992  1.00 55.18  ? 239 GLY A C   1 
ATOM   1872 O O   . GLY A 1 239 ? -1.206  -14.105 28.049  1.00 54.96  ? 239 GLY A O   1 
ATOM   1873 N N   . ARG A 1 240 ? -1.818  -12.122 27.132  1.00 55.75  ? 240 ARG A N   1 
ATOM   1874 C CA  . ARG A 1 240 ? -2.703  -12.675 26.090  1.00 55.96  ? 240 ARG A CA  1 
ATOM   1875 C C   . ARG A 1 240 ? -3.118  -11.548 25.143  1.00 56.27  ? 240 ARG A C   1 
ATOM   1876 O O   . ARG A 1 240 ? -3.494  -10.466 25.597  1.00 55.99  ? 240 ARG A O   1 
ATOM   1877 C CB  . ARG A 1 240 ? -3.951  -13.329 26.708  1.00 56.16  ? 240 ARG A CB  1 
ATOM   1878 C CG  . ARG A 1 240 ? -4.853  -14.089 25.726  1.00 55.88  ? 240 ARG A CG  1 
ATOM   1879 C CD  . ARG A 1 240 ? -4.884  -15.600 25.973  1.00 56.51  ? 240 ARG A CD  1 
ATOM   1880 N NE  . ARG A 1 240 ? -5.939  -16.234 25.183  1.00 57.37  ? 240 ARG A NE  1 
ATOM   1881 C CZ  . ARG A 1 240 ? -6.218  -17.537 25.161  1.00 56.81  ? 240 ARG A CZ  1 
ATOM   1882 N NH1 . ARG A 1 240 ? -5.544  -18.416 25.897  1.00 56.81  ? 240 ARG A NH1 1 
ATOM   1883 N NH2 . ARG A 1 240 ? -7.201  -17.963 24.393  1.00 57.44  ? 240 ARG A NH2 1 
ATOM   1884 N N   . TRP A 1 241 ? -3.040  -11.808 23.833  1.00 56.93  ? 241 TRP A N   1 
ATOM   1885 C CA  . TRP A 1 241 ? -3.297  -10.786 22.804  1.00 57.41  ? 241 TRP A CA  1 
ATOM   1886 C C   . TRP A 1 241 ? -4.188  -11.263 21.658  1.00 57.68  ? 241 TRP A C   1 
ATOM   1887 O O   . TRP A 1 241 ? -4.161  -10.674 20.583  1.00 57.30  ? 241 TRP A O   1 
ATOM   1888 C CB  . TRP A 1 241 ? -1.976  -10.288 22.206  1.00 57.52  ? 241 TRP A CB  1 
ATOM   1889 C CG  . TRP A 1 241 ? -1.108  -9.561  23.159  1.00 57.83  ? 241 TRP A CG  1 
ATOM   1890 C CD1 . TRP A 1 241 ? -0.990  -8.213  23.293  1.00 57.70  ? 241 TRP A CD1 1 
ATOM   1891 C CD2 . TRP A 1 241 ? -0.217  -10.145 24.112  1.00 57.59  ? 241 TRP A CD2 1 
ATOM   1892 N NE1 . TRP A 1 241 ? -0.079  -7.916  24.274  1.00 58.34  ? 241 TRP A NE1 1 
ATOM   1893 C CE2 . TRP A 1 241 ? 0.409   -9.087  24.795  1.00 58.53  ? 241 TRP A CE2 1 
ATOM   1894 C CE3 . TRP A 1 241 ? 0.103   -11.466 24.465  1.00 57.78  ? 241 TRP A CE3 1 
ATOM   1895 C CZ2 . TRP A 1 241 ? 1.348   -9.304  25.813  1.00 58.06  ? 241 TRP A CZ2 1 
ATOM   1896 C CZ3 . TRP A 1 241 ? 1.038   -11.681 25.473  1.00 57.58  ? 241 TRP A CZ3 1 
ATOM   1897 C CH2 . TRP A 1 241 ? 1.646   -10.606 26.133  1.00 57.95  ? 241 TRP A CH2 1 
ATOM   1898 N N   . ASP A 1 242 ? -4.985  -12.302 21.885  1.00 58.31  ? 242 ASP A N   1 
ATOM   1899 C CA  . ASP A 1 242 ? -5.769  -12.923 20.811  1.00 59.01  ? 242 ASP A CA  1 
ATOM   1900 C C   . ASP A 1 242 ? -7.262  -12.615 20.921  1.00 59.48  ? 242 ASP A C   1 
ATOM   1901 O O   . ASP A 1 242 ? -8.086  -13.359 20.382  1.00 59.04  ? 242 ASP A O   1 
ATOM   1902 C CB  . ASP A 1 242 ? -5.563  -14.443 20.818  1.00 59.08  ? 242 ASP A CB  1 
ATOM   1903 C CG  . ASP A 1 242 ? -6.077  -15.094 22.095  1.00 59.47  ? 242 ASP A CG  1 
ATOM   1904 O OD1 . ASP A 1 242 ? -6.263  -16.324 22.106  1.00 60.25  ? 242 ASP A OD1 1 
ATOM   1905 O OD2 . ASP A 1 242 ? -6.295  -14.370 23.091  1.00 59.69  ? 242 ASP A OD2 1 
ATOM   1906 N N   . ASN A 1 243 ? -7.605  -11.537 21.629  1.00 60.10  ? 243 ASN A N   1 
ATOM   1907 C CA  . ASN A 1 243 ? -9.004  -11.115 21.794  1.00 60.94  ? 243 ASN A CA  1 
ATOM   1908 C C   . ASN A 1 243 ? -9.900  -12.161 22.476  1.00 61.63  ? 243 ASN A C   1 
ATOM   1909 O O   . ASN A 1 243 ? -11.121 -12.056 22.405  1.00 61.73  ? 243 ASN A O   1 
ATOM   1910 C CB  . ASN A 1 243 ? -9.614  -10.705 20.440  1.00 60.77  ? 243 ASN A CB  1 
ATOM   1911 C CG  . ASN A 1 243 ? -10.782 -9.777  20.664  0.00 50.00  ? 243 ASN A CG  1 
ATOM   1912 O OD1 . ASN A 1 243 ? -11.025 -9.231  21.745  0.00 50.00  ? 243 ASN A OD1 1 
ATOM   1913 N ND2 . ASN A 1 243 ? -11.509 -9.557  19.581  0.00 50.00  ? 243 ASN A ND2 1 
ATOM   1914 N N   . ASN A 1 244 ? -9.293  -13.141 23.153  1.00 62.64  ? 244 ASN A N   1 
ATOM   1915 C CA  . ASN A 1 244 ? -10.011 -14.294 23.714  1.00 63.01  ? 244 ASN A CA  1 
ATOM   1916 C C   . ASN A 1 244 ? -9.775  -14.408 25.231  1.00 63.56  ? 244 ASN A C   1 
ATOM   1917 O O   . ASN A 1 244 ? -9.032  -15.277 25.695  1.00 63.49  ? 244 ASN A O   1 
ATOM   1918 C CB  . ASN A 1 244 ? -9.557  -15.566 22.990  1.00 63.13  ? 244 ASN A CB  1 
ATOM   1919 C CG  . ASN A 1 244 ? -10.450 -16.766 23.279  1.00 63.58  ? 244 ASN A CG  1 
ATOM   1920 O OD1 . ASN A 1 244 ? -11.119 -16.833 24.312  1.00 66.32  ? 244 ASN A OD1 1 
ATOM   1921 N ND2 . ASN A 1 244 ? -10.464 -17.726 22.355  1.00 64.82  ? 244 ASN A ND2 1 
ATOM   1922 N N   . TYR A 1 245 ? -10.436 -13.536 25.991  1.00 64.20  ? 245 TYR A N   1 
ATOM   1923 C CA  . TYR A 1 245 ? -10.149 -13.353 27.420  1.00 64.65  ? 245 TYR A CA  1 
ATOM   1924 C C   . TYR A 1 245 ? -11.275 -13.886 28.318  1.00 65.05  ? 245 TYR A C   1 
ATOM   1925 O O   . TYR A 1 245 ? -11.590 -13.305 29.363  1.00 65.18  ? 245 TYR A O   1 
ATOM   1926 C CB  . TYR A 1 245 ? -9.895  -11.869 27.700  1.00 64.99  ? 245 TYR A CB  1 
ATOM   1927 C CG  . TYR A 1 245 ? -9.015  -11.207 26.653  1.00 65.30  ? 245 TYR A CG  1 
ATOM   1928 C CD1 . TYR A 1 245 ? -7.678  -11.577 26.503  1.00 65.83  ? 245 TYR A CD1 1 
ATOM   1929 C CD2 . TYR A 1 245 ? -9.519  -10.217 25.810  1.00 65.42  ? 245 TYR A CD2 1 
ATOM   1930 C CE1 . TYR A 1 245 ? -6.868  -10.982 25.546  1.00 65.38  ? 245 TYR A CE1 1 
ATOM   1931 C CE2 . TYR A 1 245 ? -8.713  -9.615  24.850  1.00 65.33  ? 245 TYR A CE2 1 
ATOM   1932 C CZ  . TYR A 1 245 ? -7.390  -10.005 24.722  1.00 65.51  ? 245 TYR A CZ  1 
ATOM   1933 O OH  . TYR A 1 245 ? -6.584  -9.415  23.773  1.00 65.65  ? 245 TYR A OH  1 
ATOM   1934 N N   . GLY A 1 246 ? -11.863 -15.005 27.913  1.00 65.31  ? 246 GLY A N   1 
ATOM   1935 C CA  . GLY A 1 246 ? -13.021 -15.559 28.603  1.00 65.59  ? 246 GLY A CA  1 
ATOM   1936 C C   . GLY A 1 246 ? -12.685 -16.393 29.824  1.00 65.85  ? 246 GLY A C   1 
ATOM   1937 O O   . GLY A 1 246 ? -13.518 -16.546 30.720  1.00 66.10  ? 246 GLY A O   1 
ATOM   1938 N N   . ASP A 1 247 ? -11.470 -16.930 29.860  1.00 66.00  ? 247 ASP A N   1 
ATOM   1939 C CA  . ASP A 1 247 ? -10.969 -17.613 31.047  1.00 66.11  ? 247 ASP A CA  1 
ATOM   1940 C C   . ASP A 1 247 ? -11.050 -16.714 32.276  0.00 50.00  ? 247 ASP A C   1 
ATOM   1941 O O   . ASP A 1 247 ? -11.180 -17.195 33.402  0.00 50.00  ? 247 ASP A O   1 
ATOM   1942 C CB  . ASP A 1 247 ? -9.528  -18.079 30.829  1.00 66.33  ? 247 ASP A CB  1 
ATOM   1943 C CG  . ASP A 1 247 ? -9.414  -19.136 29.749  1.00 66.28  ? 247 ASP A CG  1 
ATOM   1944 O OD1 . ASP A 1 247 ? -10.416 -19.379 29.044  1.00 66.54  ? 247 ASP A OD1 1 
ATOM   1945 O OD2 . ASP A 1 247 ? -8.322  -19.724 29.603  1.00 66.73  ? 247 ASP A OD2 1 
ATOM   1946 N N   . GLY A 1 248 ? -10.971 -15.407 32.053  1.00 59.89  ? 248 GLY A N   1 
ATOM   1947 C CA  . GLY A 1 248 ? -10.675 -14.467 33.118  1.00 59.87  ? 248 GLY A CA  1 
ATOM   1948 C C   . GLY A 1 248 ? -11.154 -13.064 32.805  1.00 59.87  ? 248 GLY A C   1 
ATOM   1949 O O   . GLY A 1 248 ? -12.334 -12.848 32.527  1.00 59.89  ? 248 GLY A O   1 
ATOM   1950 N N   . VAL A 1 249 ? -10.234 -12.106 32.849  1.00 59.69  ? 249 VAL A N   1 
ATOM   1951 C CA  . VAL A 1 249 ? -10.591 -10.692 32.742  1.00 59.74  ? 249 VAL A CA  1 
ATOM   1952 C C   . VAL A 1 249 ? -9.782  -10.004 31.634  1.00 59.64  ? 249 VAL A C   1 
ATOM   1953 O O   . VAL A 1 249 ? -8.570  -10.225 31.503  1.00 59.53  ? 249 VAL A O   1 
ATOM   1954 C CB  . VAL A 1 249 ? -10.348 -9.964  34.090  1.00 59.83  ? 249 VAL A CB  1 
ATOM   1955 C CG1 . VAL A 1 249 ? -10.514 -8.451  33.938  1.00 60.50  ? 249 VAL A CG1 1 
ATOM   1956 C CG2 . VAL A 1 249 ? -11.287 -10.520 35.171  1.00 59.81  ? 249 VAL A CG2 1 
ATOM   1957 N N   . SER A 1 250 ? -10.464 -9.167  30.850  1.00 59.30  ? 250 SER A N   1 
ATOM   1958 C CA  . SER A 1 250 ? -9.851  -8.485  29.710  1.00 58.96  ? 250 SER A CA  1 
ATOM   1959 C C   . SER A 1 250 ? -8.858  -7.417  30.174  1.00 58.49  ? 250 SER A C   1 
ATOM   1960 O O   . SER A 1 250 ? -9.117  -6.708  31.140  1.00 58.25  ? 250 SER A O   1 
ATOM   1961 C CB  . SER A 1 250 ? -10.931 -7.859  28.809  1.00 59.09  ? 250 SER A CB  1 
ATOM   1962 O OG  . SER A 1 250 ? -10.362 -7.163  27.712  1.00 58.78  ? 250 SER A OG  1 
ATOM   1963 N N   . PRO A 1 251 ? -7.716  -7.296  29.475  1.00 58.23  ? 251 PRO A N   1 
ATOM   1964 C CA  . PRO A 1 251 ? -6.768  -6.221  29.789  1.00 57.97  ? 251 PRO A CA  1 
ATOM   1965 C C   . PRO A 1 251 ? -7.405  -4.823  29.789  1.00 57.72  ? 251 PRO A C   1 
ATOM   1966 O O   . PRO A 1 251 ? -7.013  -3.970  30.585  1.00 57.44  ? 251 PRO A O   1 
ATOM   1967 C CB  . PRO A 1 251 ? -5.723  -6.336  28.670  1.00 58.01  ? 251 PRO A CB  1 
ATOM   1968 C CG  . PRO A 1 251 ? -5.823  -7.762  28.189  1.00 58.26  ? 251 PRO A CG  1 
ATOM   1969 C CD  . PRO A 1 251 ? -7.251  -8.146  28.357  1.00 58.16  ? 251 PRO A CD  1 
ATOM   1970 N N   . MET A 1 252 ? -8.377  -4.604  28.900  1.00 57.58  ? 252 MET A N   1 
ATOM   1971 C CA  . MET A 1 252 ? -9.013  -3.291  28.705  1.00 57.55  ? 252 MET A CA  1 
ATOM   1972 C C   . MET A 1 252 ? -10.034 -2.924  29.789  1.00 57.62  ? 252 MET A C   1 
ATOM   1973 O O   . MET A 1 252 ? -10.544 -1.792  29.827  1.00 57.75  ? 252 MET A O   1 
ATOM   1974 C CB  . MET A 1 252 ? -9.695  -3.246  27.327  1.00 57.58  ? 252 MET A CB  1 
ATOM   1975 C CG  . MET A 1 252 ? -8.726  -3.129  26.144  1.00 57.81  ? 252 MET A CG  1 
ATOM   1976 S SD  . MET A 1 252 ? -7.655  -4.565  25.827  1.00 58.62  ? 252 MET A SD  1 
ATOM   1977 C CE  . MET A 1 252 ? -8.840  -5.752  25.177  1.00 57.97  ? 252 MET A CE  1 
ATOM   1978 N N   . SER A 1 253 ? -10.329 -3.878  30.666  1.00 57.69  ? 253 SER A N   1 
ATOM   1979 C CA  . SER A 1 253 ? -11.332 -3.700  31.720  1.00 57.16  ? 253 SER A CA  1 
ATOM   1980 C C   . SER A 1 253 ? -10.771 -2.980  32.950  1.00 56.76  ? 253 SER A C   1 
ATOM   1981 O O   . SER A 1 253 ? -11.324 -1.968  33.379  1.00 57.25  ? 253 SER A O   1 
ATOM   1982 C CB  . SER A 1 253 ? -11.891 -5.062  32.125  1.00 57.14  ? 253 SER A CB  1 
ATOM   1983 O OG  . SER A 1 253 ? -12.433 -5.731  31.000  1.00 57.93  ? 253 SER A OG  1 
ATOM   1984 N N   . TRP A 1 254 ? -9.691  -3.521  33.515  1.00 56.02  ? 254 TRP A N   1 
ATOM   1985 C CA  . TRP A 1 254 ? -8.978  -2.911  34.648  1.00 55.04  ? 254 TRP A CA  1 
ATOM   1986 C C   . TRP A 1 254 ? -8.948  -1.361  34.618  1.00 54.55  ? 254 TRP A C   1 
ATOM   1987 O O   . TRP A 1 254 ? -8.700  -0.748  33.557  1.00 54.64  ? 254 TRP A O   1 
ATOM   1988 C CB  . TRP A 1 254 ? -7.518  -3.428  34.706  1.00 55.63  ? 254 TRP A CB  1 
ATOM   1989 C CG  . TRP A 1 254 ? -7.359  -4.947  34.604  1.00 55.96  ? 254 TRP A CG  1 
ATOM   1990 C CD1 . TRP A 1 254 ? -6.814  -5.651  33.567  1.00 56.17  ? 254 TRP A CD1 1 
ATOM   1991 C CD2 . TRP A 1 254 ? -7.754  -5.921  35.577  1.00 56.56  ? 254 TRP A CD2 1 
ATOM   1992 N NE1 . TRP A 1 254 ? -6.852  -6.995  33.829  1.00 55.90  ? 254 TRP A NE1 1 
ATOM   1993 C CE2 . TRP A 1 254 ? -7.416  -7.190  35.060  1.00 56.80  ? 254 TRP A CE2 1 
ATOM   1994 C CE3 . TRP A 1 254 ? -8.348  -5.842  36.847  1.00 55.91  ? 254 TRP A CE3 1 
ATOM   1995 C CZ2 . TRP A 1 254 ? -7.666  -8.375  35.764  1.00 56.68  ? 254 TRP A CZ2 1 
ATOM   1996 C CZ3 . TRP A 1 254 ? -8.603  -7.011  37.534  1.00 56.26  ? 254 TRP A CZ3 1 
ATOM   1997 C CH2 . TRP A 1 254 ? -8.260  -8.265  36.995  1.00 56.14  ? 254 TRP A CH2 1 
ATOM   1998 N N   . ILE A 1 255 ? -9.207  -0.736  35.775  1.00 52.96  ? 255 ILE A N   1 
ATOM   1999 C CA  . ILE A 1 255 ? -8.957  0.707   35.971  1.00 51.86  ? 255 ILE A CA  1 
ATOM   2000 C C   . ILE A 1 255 ? -7.994  0.945   37.111  1.00 50.72  ? 255 ILE A C   1 
ATOM   2001 O O   . ILE A 1 255 ? -7.872  2.071   37.604  1.00 50.24  ? 255 ILE A O   1 
ATOM   2002 C CB  . ILE A 1 255 ? -10.250 1.550   36.218  1.00 51.64  ? 255 ILE A CB  1 
ATOM   2003 C CG1 . ILE A 1 255 ? -11.162 0.896   37.254  1.00 51.96  ? 255 ILE A CG1 1 
ATOM   2004 C CG2 . ILE A 1 255 ? -10.978 1.782   34.906  1.00 53.03  ? 255 ILE A CG2 1 
ATOM   2005 C CD1 . ILE A 1 255 ? -12.397 1.729   37.618  1.00 51.77  ? 255 ILE A CD1 1 
ATOM   2006 N N   . GLY A 1 256 ? -7.298  -0.111  37.519  1.00 49.79  ? 256 GLY A N   1 
ATOM   2007 C CA  . GLY A 1 256 ? -6.369  -0.029  38.636  1.00 49.69  ? 256 GLY A CA  1 
ATOM   2008 C C   . GLY A 1 256 ? -5.577  -1.299  38.861  1.00 49.04  ? 256 GLY A C   1 
ATOM   2009 O O   . GLY A 1 256 ? -5.890  -2.353  38.281  1.00 48.66  ? 256 GLY A O   1 
ATOM   2010 N N   . SER A 1 257 ? -4.551  -1.193  39.709  1.00 48.46  ? 257 SER A N   1 
ATOM   2011 C CA  . SER A 1 257 ? -3.634  -2.300  39.992  1.00 48.49  ? 257 SER A CA  1 
ATOM   2012 C C   . SER A 1 257 ? -4.012  -3.103  41.217  1.00 48.44  ? 257 SER A C   1 
ATOM   2013 O O   . SER A 1 257 ? -3.431  -4.164  41.457  1.00 48.61  ? 257 SER A O   1 
ATOM   2014 C CB  . SER A 1 257 ? -2.237  -1.772  40.252  1.00 47.88  ? 257 SER A CB  1 
ATOM   2015 O OG  . SER A 1 257 ? -1.753  -1.054  39.153  1.00 48.40  ? 257 SER A OG  1 
ATOM   2016 N N   . VAL A 1 258 ? -4.966  -2.590  41.984  1.00 48.19  ? 258 VAL A N   1 
ATOM   2017 C CA  . VAL A 1 258 ? -5.254  -3.093  43.315  1.00 48.25  ? 258 VAL A CA  1 
ATOM   2018 C C   . VAL A 1 258 ? -5.972  -4.422  43.250  1.00 48.35  ? 258 VAL A C   1 
ATOM   2019 O O   . VAL A 1 258 ? -5.586  -5.373  43.923  1.00 48.39  ? 258 VAL A O   1 
ATOM   2020 C CB  . VAL A 1 258 ? -6.112  -2.077  44.110  1.00 48.50  ? 258 VAL A CB  1 
ATOM   2021 C CG1 . VAL A 1 258 ? -6.691  -2.710  45.398  1.00 48.73  ? 258 VAL A CG1 1 
ATOM   2022 C CG2 . VAL A 1 258 ? -5.292  -0.858  44.431  1.00 46.51  ? 258 VAL A CG2 1 
ATOM   2023 N N   . ASP A 1 259 ? -7.017  -4.485  42.432  1.00 48.03  ? 259 ASP A N   1 
ATOM   2024 C CA  . ASP A 1 259 ? -7.834  -5.663  42.361  1.00 48.36  ? 259 ASP A CA  1 
ATOM   2025 C C   . ASP A 1 259 ? -7.061  -6.858  41.847  1.00 48.08  ? 259 ASP A C   1 
ATOM   2026 O O   . ASP A 1 259 ? -7.339  -7.987  42.250  1.00 48.92  ? 259 ASP A O   1 
ATOM   2027 C CB  . ASP A 1 259 ? -9.057  -5.437  41.478  1.00 48.75  ? 259 ASP A CB  1 
ATOM   2028 C CG  . ASP A 1 259 ? -10.064 -6.531  41.630  1.00 50.75  ? 259 ASP A CG  1 
ATOM   2029 O OD1 . ASP A 1 259 ? -10.613 -7.009  40.616  1.00 52.93  ? 259 ASP A OD1 1 
ATOM   2030 O OD2 . ASP A 1 259 ? -10.280 -6.955  42.785  1.00 55.41  ? 259 ASP A OD2 1 
ATOM   2031 N N   . ILE A 1 260 ? -6.135  -6.602  40.934  1.00 47.46  ? 260 ILE A N   1 
ATOM   2032 C CA  . ILE A 1 260 ? -5.252  -7.614  40.360  1.00 47.48  ? 260 ILE A CA  1 
ATOM   2033 C C   . ILE A 1 260 ? -4.328  -8.186  41.450  1.00 47.02  ? 260 ILE A C   1 
ATOM   2034 O O   . ILE A 1 260 ? -4.152  -9.400  41.564  1.00 46.12  ? 260 ILE A O   1 
ATOM   2035 C CB  . ILE A 1 260 ? -4.323  -7.001  39.258  1.00 47.63  ? 260 ILE A CB  1 
ATOM   2036 C CG1 . ILE A 1 260 ? -5.136  -6.474  38.066  1.00 47.78  ? 260 ILE A CG1 1 
ATOM   2037 C CG2 . ILE A 1 260 ? -3.301  -8.037  38.765  1.00 47.65  ? 260 ILE A CG2 1 
ATOM   2038 C CD1 . ILE A 1 260 ? -4.370  -5.524  37.133  1.00 47.54  ? 260 ILE A CD1 1 
ATOM   2039 N N   . LEU A 1 261 ? -3.714  -7.274  42.195  1.00 46.73  ? 261 LEU A N   1 
ATOM   2040 C CA  . LEU A 1 261 ? -2.811  -7.637  43.268  1.00 47.49  ? 261 LEU A CA  1 
ATOM   2041 C C   . LEU A 1 261 ? -3.549  -8.480  44.305  1.00 48.10  ? 261 LEU A C   1 
ATOM   2042 O O   . LEU A 1 261 ? -3.028  -9.504  44.734  1.00 48.35  ? 261 LEU A O   1 
ATOM   2043 C CB  . LEU A 1 261 ? -2.196  -6.390  43.882  1.00 47.45  ? 261 LEU A CB  1 
ATOM   2044 C CG  . LEU A 1 261 ? -0.758  -6.004  43.508  1.00 48.27  ? 261 LEU A CG  1 
ATOM   2045 C CD1 . LEU A 1 261 ? -0.162  -6.810  42.419  1.00 45.06  ? 261 LEU A CD1 1 
ATOM   2046 C CD2 . LEU A 1 261 ? -0.609  -4.512  43.259  1.00 46.48  ? 261 LEU A CD2 1 
ATOM   2047 N N   . ARG A 1 262 ? -4.776  -8.084  44.650  1.00 48.54  ? 262 ARG A N   1 
ATOM   2048 C CA  . ARG A 1 262 ? -5.562  -8.805  45.645  1.00 49.38  ? 262 ARG A CA  1 
ATOM   2049 C C   . ARG A 1 262 ? -6.021  -10.146 45.129  1.00 50.14  ? 262 ARG A C   1 
ATOM   2050 O O   . ARG A 1 262 ? -6.058  -11.124 45.866  1.00 50.31  ? 262 ARG A O   1 
ATOM   2051 C CB  . ARG A 1 262 ? -6.747  -7.960  46.101  1.00 49.23  ? 262 ARG A CB  1 
ATOM   2052 C CG  . ARG A 1 262 ? -6.311  -6.687  46.827  1.00 49.53  ? 262 ARG A CG  1 
ATOM   2053 C CD  . ARG A 1 262 ? -7.509  -5.939  47.382  1.00 50.20  ? 262 ARG A CD  1 
ATOM   2054 N NE  . ARG A 1 262 ? -7.116  -4.775  48.169  1.00 50.54  ? 262 ARG A NE  1 
ATOM   2055 C CZ  . ARG A 1 262 ? -7.897  -3.726  48.436  1.00 52.24  ? 262 ARG A CZ  1 
ATOM   2056 N NH1 . ARG A 1 262 ? -9.145  -3.662  47.983  1.00 52.48  ? 262 ARG A NH1 1 
ATOM   2057 N NH2 . ARG A 1 262 ? -7.423  -2.713  49.156  1.00 51.96  ? 262 ARG A NH2 1 
ATOM   2058 N N   . ARG A 1 263 ? -6.387  -10.204 43.853  1.00 50.76  ? 263 ARG A N   1 
ATOM   2059 C CA  . ARG A 1 263 ? -6.701  -11.477 43.231  1.00 51.35  ? 263 ARG A CA  1 
ATOM   2060 C C   . ARG A 1 263 ? -5.504  -12.409 43.329  1.00 51.50  ? 263 ARG A C   1 
ATOM   2061 O O   . ARG A 1 263 ? -5.609  -13.519 43.831  1.00 52.04  ? 263 ARG A O   1 
ATOM   2062 C CB  . ARG A 1 263 ? -7.048  -11.277 41.758  1.00 51.40  ? 263 ARG A CB  1 
ATOM   2063 C CG  . ARG A 1 263 ? -8.467  -10.884 41.488  1.00 52.00  ? 263 ARG A CG  1 
ATOM   2064 C CD  . ARG A 1 263 ? -8.659  -10.712 39.989  1.00 52.80  ? 263 ARG A CD  1 
ATOM   2065 N NE  . ARG A 1 263 ? -9.988  -11.152 39.583  1.00 55.18  ? 263 ARG A NE  1 
ATOM   2066 C CZ  . ARG A 1 263 ? -10.967 -10.357 39.163  1.00 55.65  ? 263 ARG A CZ  1 
ATOM   2067 N NH1 . ARG A 1 263 ? -10.790 -9.044  39.078  1.00 56.55  ? 263 ARG A NH1 1 
ATOM   2068 N NH2 . ARG A 1 263 ? -12.132 -10.885 38.819  1.00 55.07  ? 263 ARG A NH2 1 
ATOM   2069 N N   . TRP A 1 264 ? -4.366  -11.937 42.840  1.00 51.74  ? 264 TRP A N   1 
ATOM   2070 C CA  . TRP A 1 264 ? -3.125  -12.697 42.881  1.00 52.40  ? 264 TRP A CA  1 
ATOM   2071 C C   . TRP A 1 264 ? -2.840  -13.334 44.245  1.00 52.75  ? 264 TRP A C   1 
ATOM   2072 O O   . TRP A 1 264 ? -2.585  -14.524 44.339  1.00 51.66  ? 264 TRP A O   1 
ATOM   2073 C CB  . TRP A 1 264 ? -1.977  -11.782 42.532  1.00 52.20  ? 264 TRP A CB  1 
ATOM   2074 C CG  . TRP A 1 264 ? -0.702  -12.445 42.592  1.00 52.83  ? 264 TRP A CG  1 
ATOM   2075 C CD1 . TRP A 1 264 ? -0.232  -13.372 41.729  1.00 52.91  ? 264 TRP A CD1 1 
ATOM   2076 C CD2 . TRP A 1 264 ? 0.313   -12.250 43.579  1.00 53.05  ? 264 TRP A CD2 1 
ATOM   2077 N NE1 . TRP A 1 264 ? 1.020   -13.778 42.106  1.00 53.78  ? 264 TRP A NE1 1 
ATOM   2078 C CE2 . TRP A 1 264 ? 1.382   -13.102 43.244  1.00 52.95  ? 264 TRP A CE2 1 
ATOM   2079 C CE3 . TRP A 1 264 ? 0.419   -11.442 44.718  1.00 54.22  ? 264 TRP A CE3 1 
ATOM   2080 C CZ2 . TRP A 1 264 ? 2.554   -13.168 43.999  1.00 53.01  ? 264 TRP A CZ2 1 
ATOM   2081 C CZ3 . TRP A 1 264 ? 1.583   -11.511 45.480  1.00 53.20  ? 264 TRP A CZ3 1 
ATOM   2082 C CH2 . TRP A 1 264 ? 2.639   -12.361 45.109  1.00 53.61  ? 264 TRP A CH2 1 
ATOM   2083 N N   . LYS A 1 265 ? -2.862  -12.516 45.290  1.00 53.77  ? 265 LYS A N   1 
ATOM   2084 C CA  . LYS A 1 265 ? -2.636  -13.012 46.654  1.00 54.54  ? 265 LYS A CA  1 
ATOM   2085 C C   . LYS A 1 265 ? -3.589  -14.134 47.024  1.00 55.23  ? 265 LYS A C   1 
ATOM   2086 O O   . LYS A 1 265 ? -3.186  -15.130 47.612  1.00 54.52  ? 265 LYS A O   1 
ATOM   2087 C CB  . LYS A 1 265 ? -2.822  -11.893 47.665  1.00 54.63  ? 265 LYS A CB  1 
ATOM   2088 C CG  . LYS A 1 265 ? -2.565  -12.306 49.116  1.00 54.32  ? 265 LYS A CG  1 
ATOM   2089 C CD  . LYS A 1 265 ? -3.496  -11.574 50.068  1.00 55.10  ? 265 LYS A CD  1 
ATOM   2090 C CE  . LYS A 1 265 ? -3.072  -11.778 51.535  1.00 56.76  ? 265 LYS A CE  1 
ATOM   2091 N NZ  . LYS A 1 265 ? -2.127  -10.681 51.921  1.00 56.78  ? 265 LYS A NZ  1 
ATOM   2092 N N   . ASN A 1 266 ? -4.858  -13.953 46.689  1.00 56.41  ? 266 ASN A N   1 
ATOM   2093 C CA  . ASN A 1 266 ? -5.912  -14.827 47.191  1.00 57.36  ? 266 ASN A CA  1 
ATOM   2094 C C   . ASN A 1 266 ? -5.938  -16.175 46.509  1.00 58.35  ? 266 ASN A C   1 
ATOM   2095 O O   . ASN A 1 266 ? -6.597  -17.101 46.989  1.00 58.00  ? 266 ASN A O   1 
ATOM   2096 C CB  . ASN A 1 266 ? -7.276  -14.154 47.052  1.00 57.40  ? 266 ASN A CB  1 
ATOM   2097 C CG  . ASN A 1 266 ? -7.430  -12.961 47.976  1.00 58.28  ? 266 ASN A CG  1 
ATOM   2098 O OD1 . ASN A 1 266 ? -8.479  -12.776 48.588  1.00 61.08  ? 266 ASN A OD1 1 
ATOM   2099 N ND2 . ASN A 1 266 ? -6.376  -12.154 48.099  1.00 57.24  ? 266 ASN A ND2 1 
ATOM   2100 N N   . HIS A 1 267 ? -5.228  -16.290 45.390  1.00 59.54  ? 267 HIS A N   1 
ATOM   2101 C CA  . HIS A 1 267 ? -5.219  -17.535 44.640  1.00 60.45  ? 267 HIS A CA  1 
ATOM   2102 C C   . HIS A 1 267 ? -3.828  -18.150 44.635  1.00 61.28  ? 267 HIS A C   1 
ATOM   2103 O O   . HIS A 1 267 ? -3.311  -18.528 43.588  1.00 62.01  ? 267 HIS A O   1 
ATOM   2104 C CB  . HIS A 1 267 ? -5.757  -17.270 43.245  1.00 61.04  ? 267 HIS A CB  1 
ATOM   2105 C CG  . HIS A 1 267 ? -7.075  -16.570 43.267  1.00 62.54  ? 267 HIS A CG  1 
ATOM   2106 N ND1 . HIS A 1 267 ? -8.157  -17.061 43.968  1.00 64.02  ? 267 HIS A ND1 1 
ATOM   2107 C CD2 . HIS A 1 267 ? -7.476  -15.394 42.728  1.00 64.05  ? 267 HIS A CD2 1 
ATOM   2108 C CE1 . HIS A 1 267 ? -9.176  -16.232 43.833  1.00 64.64  ? 267 HIS A CE1 1 
ATOM   2109 N NE2 . HIS A 1 267 ? -8.791  -15.215 43.082  1.00 64.90  ? 267 HIS A NE2 1 
ATOM   2110 N N   . GLY A 1 268 ? -3.235  -18.240 45.827  1.00 61.43  ? 268 GLY A N   1 
ATOM   2111 C CA  . GLY A 1 268 ? -1.937  -18.874 46.020  1.00 61.34  ? 268 GLY A CA  1 
ATOM   2112 C C   . GLY A 1 268 ? -0.851  -18.276 45.158  1.00 61.41  ? 268 GLY A C   1 
ATOM   2113 O O   . GLY A 1 268 ? -0.055  -19.004 44.564  1.00 61.72  ? 268 GLY A O   1 
ATOM   2114 N N   . CYS A 1 269 ? -0.827  -16.952 45.069  1.00 61.42  ? 269 CYS A N   1 
ATOM   2115 C CA  . CYS A 1 269 ? 0.148   -16.267 44.234  1.00 61.54  ? 269 CYS A CA  1 
ATOM   2116 C C   . CYS A 1 269 ? 0.195   -16.868 42.810  1.00 61.38  ? 269 CYS A C   1 
ATOM   2117 O O   . CYS A 1 269 ? 1.270   -17.097 42.248  1.00 61.67  ? 269 CYS A O   1 
ATOM   2118 C CB  . CYS A 1 269 ? 1.522   -16.324 44.900  1.00 61.68  ? 269 CYS A CB  1 
ATOM   2119 S SG  . CYS A 1 269 ? 1.548   -15.498 46.503  1.00 65.11  ? 269 CYS A SG  1 
ATOM   2120 N N   . GLN A 1 270 ? -0.977  -17.142 42.244  1.00 60.67  ? 270 GLN A N   1 
ATOM   2121 C CA  . GLN A 1 270 ? -1.052  -17.630 40.875  1.00 60.22  ? 270 GLN A CA  1 
ATOM   2122 C C   . GLN A 1 270 ? -1.382  -16.481 39.945  1.00 59.49  ? 270 GLN A C   1 
ATOM   2123 O O   . GLN A 1 270 ? -2.238  -15.644 40.257  1.00 59.25  ? 270 GLN A O   1 
ATOM   2124 C CB  . GLN A 1 270 ? -2.085  -18.740 40.741  1.00 60.27  ? 270 GLN A CB  1 
ATOM   2125 C CG  . GLN A 1 270 ? -1.647  -20.041 41.377  1.00 60.77  ? 270 GLN A CG  1 
ATOM   2126 C CD  . GLN A 1 270 ? -2.806  -20.951 41.693  1.00 61.09  ? 270 GLN A CD  1 
ATOM   2127 O OE1 . GLN A 1 270 ? -3.714  -21.133 40.881  1.00 63.85  ? 270 GLN A OE1 1 
ATOM   2128 N NE2 . GLN A 1 270 ? -2.783  -21.536 42.881  1.00 63.22  ? 270 GLN A NE2 1 
ATOM   2129 N N   . ARG A 1 271 ? -0.682  -16.455 38.812  1.00 58.63  ? 271 ARG A N   1 
ATOM   2130 C CA  . ARG A 1 271 ? -0.876  -15.441 37.791  1.00 58.51  ? 271 ARG A CA  1 
ATOM   2131 C C   . ARG A 1 271 ? -2.361  -15.192 37.546  1.00 57.67  ? 271 ARG A C   1 
ATOM   2132 O O   . ARG A 1 271 ? -3.164  -16.134 37.489  1.00 57.39  ? 271 ARG A O   1 
ATOM   2133 C CB  . ARG A 1 271 ? -0.259  -15.868 36.462  1.00 58.48  ? 271 ARG A CB  1 
ATOM   2134 C CG  . ARG A 1 271 ? 1.250   -16.000 36.379  1.00 58.85  ? 271 ARG A CG  1 
ATOM   2135 C CD  . ARG A 1 271 ? 1.610   -16.149 34.888  1.00 60.74  ? 271 ARG A CD  1 
ATOM   2136 N NE  . ARG A 1 271 ? 2.956   -16.652 34.611  1.00 61.98  ? 271 ARG A NE  1 
ATOM   2137 C CZ  . ARG A 1 271 ? 3.253   -17.879 34.177  1.00 63.02  ? 271 ARG A CZ  1 
ATOM   2138 N NH1 . ARG A 1 271 ? 2.311   -18.800 33.952  1.00 62.61  ? 271 ARG A NH1 1 
ATOM   2139 N NH2 . ARG A 1 271 ? 4.525   -18.194 33.963  1.00 63.94  ? 271 ARG A NH2 1 
ATOM   2140 N N   . VAL A 1 272 ? -2.695  -13.918 37.388  1.00 56.62  ? 272 VAL A N   1 
ATOM   2141 C CA  . VAL A 1 272 ? -4.038  -13.460 37.088  1.00 56.08  ? 272 VAL A CA  1 
ATOM   2142 C C   . VAL A 1 272 ? -4.138  -13.255 35.575  1.00 55.50  ? 272 VAL A C   1 
ATOM   2143 O O   . VAL A 1 272 ? -3.240  -12.697 34.942  1.00 54.73  ? 272 VAL A O   1 
ATOM   2144 C CB  . VAL A 1 272 ? -4.333  -12.126 37.835  1.00 56.32  ? 272 VAL A CB  1 
ATOM   2145 C CG1 . VAL A 1 272 ? -5.753  -11.633 37.572  1.00 56.50  ? 272 VAL A CG1 1 
ATOM   2146 C CG2 . VAL A 1 272 ? -4.094  -12.290 39.327  1.00 55.40  ? 272 VAL A CG2 1 
ATOM   2147 N N   . LYS A 1 273 ? -5.228  -13.746 35.003  1.00 55.06  ? 273 LYS A N   1 
ATOM   2148 C CA  . LYS A 1 273 ? -5.490  -13.624 33.582  1.00 54.74  ? 273 LYS A CA  1 
ATOM   2149 C C   . LYS A 1 273 ? -6.413  -12.425 33.389  1.00 54.14  ? 273 LYS A C   1 
ATOM   2150 O O   . LYS A 1 273 ? -7.447  -12.348 34.052  1.00 54.40  ? 273 LYS A O   1 
ATOM   2151 C CB  . LYS A 1 273 ? -6.164  -14.888 33.075  1.00 54.59  ? 273 LYS A CB  1 
ATOM   2152 C CG  . LYS A 1 273 ? -5.289  -16.124 33.162  1.00 54.56  ? 273 LYS A CG  1 
ATOM   2153 C CD  . LYS A 1 273 ? -6.073  -17.353 32.817  1.00 54.87  ? 273 LYS A CD  1 
ATOM   2154 C CE  . LYS A 1 273 ? -5.345  -18.613 33.217  1.00 55.16  ? 273 LYS A CE  1 
ATOM   2155 N NZ  . LYS A 1 273 ? -5.888  -19.781 32.483  1.00 54.65  ? 273 LYS A NZ  1 
ATOM   2156 N N   . TYR A 1 274 ? -6.084  -11.485 32.501  1.00 53.15  ? 274 TYR A N   1 
ATOM   2157 C CA  . TYR A 1 274 ? -4.893  -11.493 31.659  1.00 52.12  ? 274 TYR A CA  1 
ATOM   2158 C C   . TYR A 1 274 ? -4.339  -10.088 31.657  1.00 51.67  ? 274 TYR A C   1 
ATOM   2159 O O   . TYR A 1 274 ? -5.060  -9.129  31.918  1.00 51.53  ? 274 TYR A O   1 
ATOM   2160 C CB  . TYR A 1 274 ? -5.238  -11.858 30.212  1.00 52.08  ? 274 TYR A CB  1 
ATOM   2161 C CG  . TYR A 1 274 ? -5.732  -13.280 29.989  1.00 52.57  ? 274 TYR A CG  1 
ATOM   2162 C CD1 . TYR A 1 274 ? -4.842  -14.349 29.997  1.00 52.50  ? 274 TYR A CD1 1 
ATOM   2163 C CD2 . TYR A 1 274 ? -7.082  -13.551 29.731  1.00 52.60  ? 274 TYR A CD2 1 
ATOM   2164 C CE1 . TYR A 1 274 ? -5.271  -15.638 29.776  1.00 52.76  ? 274 TYR A CE1 1 
ATOM   2165 C CE2 . TYR A 1 274 ? -7.524  -14.860 29.500  1.00 52.16  ? 274 TYR A CE2 1 
ATOM   2166 C CZ  . TYR A 1 274 ? -6.605  -15.889 29.519  1.00 51.92  ? 274 TYR A CZ  1 
ATOM   2167 O OH  . TYR A 1 274 ? -6.985  -17.175 29.308  1.00 51.70  ? 274 TYR A OH  1 
ATOM   2168 N N   . GLY A 1 275 ? -3.059  -9.969  31.335  1.00 51.24  ? 275 GLY A N   1 
ATOM   2169 C CA  . GLY A 1 275 ? -2.442  -8.669  31.119  1.00 50.89  ? 275 GLY A CA  1 
ATOM   2170 C C   . GLY A 1 275 ? -2.131  -8.358  29.653  1.00 50.62  ? 275 GLY A C   1 
ATOM   2171 O O   . GLY A 1 275 ? -2.205  -9.223  28.778  1.00 50.29  ? 275 GLY A O   1 
ATOM   2172 N N   . GLN A 1 276 ? -1.809  -7.090  29.408  1.00 50.43  ? 276 GLN A N   1 
ATOM   2173 C CA  . GLN A 1 276 ? -1.131  -6.644  28.191  1.00 50.01  ? 276 GLN A CA  1 
ATOM   2174 C C   . GLN A 1 276 ? -0.121  -5.625  28.641  1.00 49.87  ? 276 GLN A C   1 
ATOM   2175 O O   . GLN A 1 276 ? -0.050  -5.305  29.843  1.00 49.42  ? 276 GLN A O   1 
ATOM   2176 C CB  . GLN A 1 276 ? -2.125  -6.118  27.138  1.00 49.74  ? 276 GLN A CB  1 
ATOM   2177 C CG  . GLN A 1 276 ? -2.712  -7.253  26.326  1.00 48.47  ? 276 GLN A CG  1 
ATOM   2178 C CD  . GLN A 1 276 ? -3.569  -6.820  25.125  1.00 49.95  ? 276 GLN A CD  1 
ATOM   2179 O OE1 . GLN A 1 276 ? -3.628  -5.645  24.771  1.00 51.12  ? 276 GLN A OE1 1 
ATOM   2180 N NE2 . GLN A 1 276 ? -4.232  -7.790  24.496  1.00 47.67  ? 276 GLN A NE2 1 
ATOM   2181 N N   . CYS A 1 277 ? 0.692   -5.115  27.728  1.00 49.29  ? 277 CYS A N   1 
ATOM   2182 C CA  . CYS A 1 277 ? 1.846   -4.374  28.186  1.00 48.91  ? 277 CYS A CA  1 
ATOM   2183 C C   . CYS A 1 277 ? 1.495   -3.345  29.261  1.00 48.91  ? 277 CYS A C   1 
ATOM   2184 O O   . CYS A 1 277 ? 2.195   -3.255  30.286  1.00 49.41  ? 277 CYS A O   1 
ATOM   2185 C CB  . CYS A 1 277 ? 2.568   -3.697  27.020  1.00 49.39  ? 277 CYS A CB  1 
ATOM   2186 S SG  . CYS A 1 277 ? 1.575   -2.470  26.204  1.00 50.74  ? 277 CYS A SG  1 
ATOM   2187 N N   . TRP A 1 278 ? 0.448   -2.542  29.041  1.00 48.19  ? 278 TRP A N   1 
ATOM   2188 C CA  . TRP A 1 278 ? 0.178   -1.429  29.975  1.00 47.06  ? 278 TRP A CA  1 
ATOM   2189 C C   . TRP A 1 278 ? -0.370  -1.948  31.312  1.00 46.45  ? 278 TRP A C   1 
ATOM   2190 O O   . TRP A 1 278 ? -0.309  -1.234  32.306  1.00 45.50  ? 278 TRP A O   1 
ATOM   2191 C CB  . TRP A 1 278 ? -0.800  -0.394  29.400  1.00 46.77  ? 278 TRP A CB  1 
ATOM   2192 C CG  . TRP A 1 278 ? -2.214  -0.854  29.434  1.00 46.06  ? 278 TRP A CG  1 
ATOM   2193 C CD1 . TRP A 1 278 ? -3.143  -0.625  30.422  1.00 46.33  ? 278 TRP A CD1 1 
ATOM   2194 C CD2 . TRP A 1 278 ? -2.854  -1.682  28.468  1.00 45.78  ? 278 TRP A CD2 1 
ATOM   2195 N NE1 . TRP A 1 278 ? -4.335  -1.247  30.096  1.00 45.93  ? 278 TRP A NE1 1 
ATOM   2196 C CE2 . TRP A 1 278 ? -4.173  -1.904  28.909  1.00 44.40  ? 278 TRP A CE2 1 
ATOM   2197 C CE3 . TRP A 1 278 ? -2.445  -2.242  27.257  1.00 45.37  ? 278 TRP A CE3 1 
ATOM   2198 C CZ2 . TRP A 1 278 ? -5.063  -2.659  28.191  1.00 46.02  ? 278 TRP A CZ2 1 
ATOM   2199 C CZ3 . TRP A 1 278 ? -3.309  -3.002  26.577  1.00 46.33  ? 278 TRP A CZ3 1 
ATOM   2200 C CH2 . TRP A 1 278 ? -4.612  -3.209  27.029  1.00 46.48  ? 278 TRP A CH2 1 
ATOM   2201 N N   . VAL A 1 279 ? -0.939  -3.155  31.334  1.00 46.43  ? 279 VAL A N   1 
ATOM   2202 C CA  . VAL A 1 279 ? -1.385  -3.718  32.608  1.00 45.55  ? 279 VAL A CA  1 
ATOM   2203 C C   . VAL A 1 279 ? -0.183  -4.184  33.424  1.00 46.26  ? 279 VAL A C   1 
ATOM   2204 O O   . VAL A 1 279 ? -0.125  -3.940  34.640  1.00 45.94  ? 279 VAL A O   1 
ATOM   2205 C CB  . VAL A 1 279 ? -2.404  -4.850  32.479  1.00 46.08  ? 279 VAL A CB  1 
ATOM   2206 C CG1 . VAL A 1 279 ? -2.986  -5.188  33.877  1.00 44.30  ? 279 VAL A CG1 1 
ATOM   2207 C CG2 . VAL A 1 279 ? -3.525  -4.485  31.505  1.00 46.23  ? 279 VAL A CG2 1 
ATOM   2208 N N   . PHE A 1 280 ? 0.793   -4.826  32.784  1.00 45.54  ? 280 PHE A N   1 
ATOM   2209 C CA  . PHE A 1 280 ? 2.026   -5.176  33.503  1.00 44.91  ? 280 PHE A CA  1 
ATOM   2210 C C   . PHE A 1 280 ? 2.725   -3.955  34.066  1.00 45.22  ? 280 PHE A C   1 
ATOM   2211 O O   . PHE A 1 280 ? 3.175   -3.957  35.224  1.00 43.72  ? 280 PHE A O   1 
ATOM   2212 C CB  . PHE A 1 280 ? 3.037   -5.915  32.617  1.00 45.35  ? 280 PHE A CB  1 
ATOM   2213 C CG  . PHE A 1 280 ? 2.494   -7.101  31.941  1.00 44.36  ? 280 PHE A CG  1 
ATOM   2214 C CD1 . PHE A 1 280 ? 1.942   -8.120  32.651  1.00 46.10  ? 280 PHE A CD1 1 
ATOM   2215 C CD2 . PHE A 1 280 ? 2.562   -7.214  30.572  1.00 47.74  ? 280 PHE A CD2 1 
ATOM   2216 C CE1 . PHE A 1 280 ? 1.433   -9.238  32.004  1.00 47.11  ? 280 PHE A CE1 1 
ATOM   2217 C CE2 . PHE A 1 280 ? 2.058   -8.321  29.935  1.00 45.51  ? 280 PHE A CE2 1 
ATOM   2218 C CZ  . PHE A 1 280 ? 1.487   -9.326  30.657  1.00 46.09  ? 280 PHE A CZ  1 
ATOM   2219 N N   . ALA A 1 281 ? 2.850   -2.925  33.230  1.00 44.50  ? 281 ALA A N   1 
ATOM   2220 C CA  . ALA A 1 281 ? 3.545   -1.714  33.585  1.00 44.44  ? 281 ALA A CA  1 
ATOM   2221 C C   . ALA A 1 281 ? 2.854   -1.044  34.751  1.00 45.00  ? 281 ALA A C   1 
ATOM   2222 O O   . ALA A 1 281 ? 3.514   -0.489  35.652  1.00 45.14  ? 281 ALA A O   1 
ATOM   2223 C CB  . ALA A 1 281 ? 3.587   -0.747  32.374  1.00 44.67  ? 281 ALA A CB  1 
ATOM   2224 N N   . ALA A 1 282 ? 1.528   -1.030  34.688  1.00 44.57  ? 282 ALA A N   1 
ATOM   2225 C CA  . ALA A 1 282 ? 0.694   -0.384  35.696  1.00 44.64  ? 282 ALA A CA  1 
ATOM   2226 C C   . ALA A 1 282 ? 0.871   -1.061  37.071  1.00 44.72  ? 282 ALA A C   1 
ATOM   2227 O O   . ALA A 1 282 ? 0.982   -0.402  38.105  1.00 44.14  ? 282 ALA A O   1 
ATOM   2228 C CB  . ALA A 1 282 ? -0.785  -0.447  35.265  1.00 43.73  ? 282 ALA A CB  1 
ATOM   2229 N N   . VAL A 1 283 ? 0.854   -2.388  37.074  1.00 44.99  ? 283 VAL A N   1 
ATOM   2230 C CA  . VAL A 1 283 ? 1.080   -3.127  38.304  1.00 44.87  ? 283 VAL A CA  1 
ATOM   2231 C C   . VAL A 1 283 ? 2.509   -2.960  38.830  1.00 45.76  ? 283 VAL A C   1 
ATOM   2232 O O   . VAL A 1 283 ? 2.710   -2.851  40.051  1.00 46.44  ? 283 VAL A O   1 
ATOM   2233 C CB  . VAL A 1 283 ? 0.692   -4.591  38.123  1.00 44.64  ? 283 VAL A CB  1 
ATOM   2234 C CG1 . VAL A 1 283 ? 1.030   -5.402  39.373  1.00 44.62  ? 283 VAL A CG1 1 
ATOM   2235 C CG2 . VAL A 1 283 ? -0.789  -4.679  37.808  1.00 42.85  ? 283 VAL A CG2 1 
ATOM   2236 N N   . ALA A 1 284 ? 3.502   -2.928  37.935  1.00 45.12  ? 284 ALA A N   1 
ATOM   2237 C CA  . ALA A 1 284 ? 4.880   -2.637  38.321  1.00 44.95  ? 284 ALA A CA  1 
ATOM   2238 C C   . ALA A 1 284 ? 4.984   -1.277  38.990  1.00 45.35  ? 284 ALA A C   1 
ATOM   2239 O O   . ALA A 1 284 ? 5.655   -1.139  40.018  1.00 44.34  ? 284 ALA A O   1 
ATOM   2240 C CB  . ALA A 1 284 ? 5.849   -2.734  37.139  1.00 44.34  ? 284 ALA A CB  1 
ATOM   2241 N N   . CYS A 1 285 ? 4.275   -0.285  38.466  1.00 45.43  ? 285 CYS A N   1 
ATOM   2242 C CA  . CYS A 1 285 ? 4.301   1.033   39.088  1.00 45.87  ? 285 CYS A CA  1 
ATOM   2243 C C   . CYS A 1 285 ? 3.733   1.016   40.502  1.00 46.93  ? 285 CYS A C   1 
ATOM   2244 O O   . CYS A 1 285 ? 4.296   1.638   41.402  1.00 47.78  ? 285 CYS A O   1 
ATOM   2245 C CB  . CYS A 1 285 ? 3.525   2.038   38.250  1.00 46.44  ? 285 CYS A CB  1 
ATOM   2246 S SG  . CYS A 1 285 ? 3.815   3.725   38.694  1.00 43.00  ? 285 CYS A SG  1 
ATOM   2247 N N   . THR A 1 286 ? 2.609   0.335   40.685  1.00 46.91  ? 286 THR A N   1 
ATOM   2248 C CA  . THR A 1 286 ? 2.022   0.169   42.016  1.00 46.97  ? 286 THR A CA  1 
ATOM   2249 C C   . THR A 1 286 ? 3.029   -0.442  43.006  1.00 47.62  ? 286 THR A C   1 
ATOM   2250 O O   . THR A 1 286 ? 3.306   0.141   44.043  1.00 47.85  ? 286 THR A O   1 
ATOM   2251 C CB  . THR A 1 286 ? 0.792   -0.744  41.940  1.00 47.04  ? 286 THR A CB  1 
ATOM   2252 O OG1 . THR A 1 286 ? -0.235  -0.067  41.213  1.00 43.46  ? 286 THR A OG1 1 
ATOM   2253 C CG2 . THR A 1 286 ? 0.302   -1.132  43.322  1.00 45.85  ? 286 THR A CG2 1 
ATOM   2254 N N   . VAL A 1 287 ? 3.578   -1.598  42.651  1.00 47.35  ? 287 VAL A N   1 
ATOM   2255 C CA  . VAL A 1 287 ? 4.542   -2.314  43.495  1.00 46.53  ? 287 VAL A CA  1 
ATOM   2256 C C   . VAL A 1 287 ? 5.683   -1.391  43.876  1.00 46.51  ? 287 VAL A C   1 
ATOM   2257 O O   . VAL A 1 287 ? 5.971   -1.204  45.063  1.00 45.00  ? 287 VAL A O   1 
ATOM   2258 C CB  . VAL A 1 287 ? 5.059   -3.643  42.816  1.00 46.24  ? 287 VAL A CB  1 
ATOM   2259 C CG1 . VAL A 1 287 ? 6.166   -4.340  43.636  1.00 45.07  ? 287 VAL A CG1 1 
ATOM   2260 C CG2 . VAL A 1 287 ? 3.924   -4.624  42.623  1.00 43.84  ? 287 VAL A CG2 1 
ATOM   2261 N N   . LEU A 1 288 ? 6.305   -0.747  42.899  1.00 46.27  ? 288 LEU A N   1 
ATOM   2262 C CA  . LEU A 1 288 ? 7.548   -0.023  43.169  1.00 46.43  ? 288 LEU A CA  1 
ATOM   2263 C C   . LEU A 1 288 ? 7.304   1.272   43.908  1.00 46.52  ? 288 LEU A C   1 
ATOM   2264 O O   . LEU A 1 288 ? 8.057   1.640   44.817  1.00 46.20  ? 288 LEU A O   1 
ATOM   2265 C CB  . LEU A 1 288 ? 8.326   0.236   41.868  1.00 47.21  ? 288 LEU A CB  1 
ATOM   2266 C CG  . LEU A 1 288 ? 8.738   -1.060  41.173  1.00 46.74  ? 288 LEU A CG  1 
ATOM   2267 C CD1 . LEU A 1 288 ? 9.315   -0.735  39.774  1.00 46.37  ? 288 LEU A CD1 1 
ATOM   2268 C CD2 . LEU A 1 288 ? 9.714   -1.895  42.012  1.00 46.17  ? 288 LEU A CD2 1 
ATOM   2269 N N   . ARG A 1 289 ? 6.232   1.958   43.549  1.00 46.75  ? 289 ARG A N   1 
ATOM   2270 C CA  . ARG A 1 289 ? 5.786   3.129   44.308  1.00 47.06  ? 289 ARG A CA  1 
ATOM   2271 C C   . ARG A 1 289 ? 5.466   2.756   45.800  1.00 47.90  ? 289 ARG A C   1 
ATOM   2272 O O   . ARG A 1 289 ? 5.821   3.491   46.745  1.00 48.85  ? 289 ARG A O   1 
ATOM   2273 C CB  . ARG A 1 289 ? 4.571   3.754   43.636  1.00 46.18  ? 289 ARG A CB  1 
ATOM   2274 C CG  . ARG A 1 289 ? 4.904   4.633   42.406  1.00 46.50  ? 289 ARG A CG  1 
ATOM   2275 C CD  . ARG A 1 289 ? 3.816   5.651   42.102  1.00 46.96  ? 289 ARG A CD  1 
ATOM   2276 N NE  . ARG A 1 289 ? 4.126   6.429   40.887  1.00 45.54  ? 289 ARG A NE  1 
ATOM   2277 C CZ  . ARG A 1 289 ? 3.326   7.300   40.277  1.00 47.34  ? 289 ARG A CZ  1 
ATOM   2278 N NH1 . ARG A 1 289 ? 2.129   7.556   40.744  1.00 45.24  ? 289 ARG A NH1 1 
ATOM   2279 N NH2 . ARG A 1 289 ? 3.729   7.924   39.152  1.00 47.15  ? 289 ARG A NH2 1 
ATOM   2280 N N   . CYS A 1 290 ? 4.822   1.619   46.008  1.00 47.32  ? 290 CYS A N   1 
ATOM   2281 C CA  . CYS A 1 290 ? 4.533   1.155   47.371  1.00 47.03  ? 290 CYS A CA  1 
ATOM   2282 C C   . CYS A 1 290 ? 5.843   1.076   48.196  1.00 46.78  ? 290 CYS A C   1 
ATOM   2283 O O   . CYS A 1 290 ? 5.942   1.618   49.310  1.00 47.46  ? 290 CYS A O   1 
ATOM   2284 C CB  . CYS A 1 290 ? 3.811   -0.162  47.317  1.00 47.26  ? 290 CYS A CB  1 
ATOM   2285 S SG  . CYS A 1 290 ? 3.134   -0.804  48.907  1.00 46.46  ? 290 CYS A SG  1 
ATOM   2286 N N   . LEU A 1 291 ? 6.866   0.490   47.608  1.00 46.31  ? 291 LEU A N   1 
ATOM   2287 C CA  . LEU A 1 291 ? 8.093   0.232   48.311  1.00 45.70  ? 291 LEU A CA  1 
ATOM   2288 C C   . LEU A 1 291 ? 8.943   1.433   48.429  1.00 45.94  ? 291 LEU A C   1 
ATOM   2289 O O   . LEU A 1 291 ? 9.939   1.378   49.132  1.00 46.80  ? 291 LEU A O   1 
ATOM   2290 C CB  . LEU A 1 291 ? 8.858   -0.906  47.685  1.00 45.49  ? 291 LEU A CB  1 
ATOM   2291 C CG  . LEU A 1 291 ? 8.088   -2.206  47.651  1.00 44.11  ? 291 LEU A CG  1 
ATOM   2292 C CD1 . LEU A 1 291 ? 8.932   -3.206  46.886  1.00 45.28  ? 291 LEU A CD1 1 
ATOM   2293 C CD2 . LEU A 1 291 ? 7.771   -2.773  49.078  1.00 43.17  ? 291 LEU A CD2 1 
ATOM   2294 N N   . GLY A 1 292 ? 8.551   2.526   47.775  1.00 45.00  ? 292 GLY A N   1 
ATOM   2295 C CA  . GLY A 1 292 ? 9.250   3.790   47.910  1.00 45.52  ? 292 GLY A CA  1 
ATOM   2296 C C   . GLY A 1 292 ? 10.164  4.197   46.770  1.00 45.44  ? 292 GLY A C   1 
ATOM   2297 O O   . GLY A 1 292 ? 10.858  5.238   46.859  1.00 44.47  ? 292 GLY A O   1 
ATOM   2298 N N   . ILE A 1 293 ? 10.204  3.388   45.706  1.00 46.51  ? 293 ILE A N   1 
ATOM   2299 C CA  . ILE A 1 293 ? 11.064  3.714   44.554  1.00 45.72  ? 293 ILE A CA  1 
ATOM   2300 C C   . ILE A 1 293 ? 10.279  4.617   43.586  1.00 45.72  ? 293 ILE A C   1 
ATOM   2301 O O   . ILE A 1 293 ? 9.245   4.194   43.066  1.00 46.49  ? 293 ILE A O   1 
ATOM   2302 C CB  . ILE A 1 293 ? 11.531  2.478   43.803  1.00 45.74  ? 293 ILE A CB  1 
ATOM   2303 C CG1 . ILE A 1 293 ? 12.307  1.514   44.700  1.00 46.01  ? 293 ILE A CG1 1 
ATOM   2304 C CG2 . ILE A 1 293 ? 12.475  2.939   42.621  1.00 46.80  ? 293 ILE A CG2 1 
ATOM   2305 C CD1 . ILE A 1 293 ? 12.569  0.159   44.110  1.00 44.52  ? 293 ILE A CD1 1 
ATOM   2306 N N   . PRO A 1 294 ? 10.731  5.866   43.365  1.00 46.55  ? 294 PRO A N   1 
ATOM   2307 C CA  . PRO A 1 294 ? 10.008  6.760   42.459  1.00 45.47  ? 294 PRO A CA  1 
ATOM   2308 C C   . PRO A 1 294 ? 9.881   6.090   41.083  1.00 45.28  ? 294 PRO A C   1 
ATOM   2309 O O   . PRO A 1 294 ? 10.901  5.710   40.521  1.00 44.90  ? 294 PRO A O   1 
ATOM   2310 C CB  . PRO A 1 294 ? 10.912  7.965   42.375  1.00 45.61  ? 294 PRO A CB  1 
ATOM   2311 C CG  . PRO A 1 294 ? 11.729  7.895   43.650  1.00 45.71  ? 294 PRO A CG  1 
ATOM   2312 C CD  . PRO A 1 294 ? 11.955  6.510   43.898  1.00 45.93  ? 294 PRO A CD  1 
ATOM   2313 N N   . THR A 1 295 ? 8.650   5.980   40.591  1.00 44.88  ? 295 THR A N   1 
ATOM   2314 C CA  . THR A 1 295 ? 8.319   5.209   39.373  1.00 44.76  ? 295 THR A CA  1 
ATOM   2315 C C   . THR A 1 295 ? 7.224   5.894   38.554  1.00 44.81  ? 295 THR A C   1 
ATOM   2316 O O   . THR A 1 295 ? 6.377   6.604   39.101  1.00 46.16  ? 295 THR A O   1 
ATOM   2317 C CB  . THR A 1 295 ? 7.938   3.791   39.774  1.00 44.85  ? 295 THR A CB  1 
ATOM   2318 O OG1 . THR A 1 295 ? 9.007   3.267   40.558  1.00 45.14  ? 295 THR A OG1 1 
ATOM   2319 C CG2 . THR A 1 295 ? 7.759   2.905   38.552  1.00 44.47  ? 295 THR A CG2 1 
ATOM   2320 N N   . ARG A 1 296 ? 7.312   5.783   37.221  1.00 44.56  ? 296 ARG A N   1 
ATOM   2321 C CA  . ARG A 1 296 ? 6.321   6.379   36.323  1.00 43.29  ? 296 ARG A CA  1 
ATOM   2322 C C   . ARG A 1 296 ? 6.128   5.451   35.104  1.00 42.78  ? 296 ARG A C   1 
ATOM   2323 O O   . ARG A 1 296 ? 7.077   4.848   34.635  1.00 42.63  ? 296 ARG A O   1 
ATOM   2324 C CB  . ARG A 1 296 ? 6.763   7.779   35.881  1.00 43.01  ? 296 ARG A CB  1 
ATOM   2325 C CG  . ARG A 1 296 ? 8.026   7.822   35.058  1.00 43.35  ? 296 ARG A CG  1 
ATOM   2326 C CD  . ARG A 1 296 ? 8.411   9.257   34.752  1.00 43.53  ? 296 ARG A CD  1 
ATOM   2327 N NE  . ARG A 1 296 ? 9.569   9.337   33.871  1.00 43.10  ? 296 ARG A NE  1 
ATOM   2328 C CZ  . ARG A 1 296 ? 10.101  10.481  33.429  1.00 44.49  ? 296 ARG A CZ  1 
ATOM   2329 N NH1 . ARG A 1 296 ? 9.603   11.651  33.787  1.00 42.98  ? 296 ARG A NH1 1 
ATOM   2330 N NH2 . ARG A 1 296 ? 11.145  10.461  32.612  1.00 45.65  ? 296 ARG A NH2 1 
ATOM   2331 N N   . VAL A 1 297 ? 4.881   5.306   34.675  1.00 42.42  ? 297 VAL A N   1 
ATOM   2332 C CA  . VAL A 1 297 ? 4.541   4.512   33.498  1.00 42.06  ? 297 VAL A CA  1 
ATOM   2333 C C   . VAL A 1 297 ? 4.729   5.339   32.236  1.00 41.51  ? 297 VAL A C   1 
ATOM   2334 O O   . VAL A 1 297 ? 4.342   6.508   32.176  1.00 41.46  ? 297 VAL A O   1 
ATOM   2335 C CB  . VAL A 1 297 ? 3.114   3.939   33.567  1.00 41.88  ? 297 VAL A CB  1 
ATOM   2336 C CG1 . VAL A 1 297 ? 2.741   3.210   32.210  1.00 40.45  ? 297 VAL A CG1 1 
ATOM   2337 C CG2 . VAL A 1 297 ? 3.016   2.965   34.741  1.00 41.40  ? 297 VAL A CG2 1 
ATOM   2338 N N   . VAL A 1 298 ? 5.362   4.719   31.245  1.00 42.46  ? 298 VAL A N   1 
ATOM   2339 C CA  . VAL A 1 298 ? 5.707   5.383   29.990  1.00 41.76  ? 298 VAL A CA  1 
ATOM   2340 C C   . VAL A 1 298 ? 5.157   4.545   28.841  1.00 41.37  ? 298 VAL A C   1 
ATOM   2341 O O   . VAL A 1 298 ? 5.141   3.330   28.916  1.00 40.08  ? 298 VAL A O   1 
ATOM   2342 C CB  . VAL A 1 298 ? 7.233   5.561   29.788  1.00 42.34  ? 298 VAL A CB  1 
ATOM   2343 C CG1 . VAL A 1 298 ? 7.859   6.418   30.898  1.00 42.16  ? 298 VAL A CG1 1 
ATOM   2344 C CG2 . VAL A 1 298 ? 7.914   4.264   29.718  1.00 44.00  ? 298 VAL A CG2 1 
ATOM   2345 N N   . THR A 1 299 ? 4.730   5.244   27.789  1.00 41.45  ? 299 THR A N   1 
ATOM   2346 C CA  . THR A 1 299 ? 4.189   4.641   26.588  1.00 41.86  ? 299 THR A CA  1 
ATOM   2347 C C   . THR A 1 299 ? 5.022   5.115   25.400  1.00 41.61  ? 299 THR A C   1 
ATOM   2348 O O   . THR A 1 299 ? 5.262   6.299   25.255  1.00 41.28  ? 299 THR A O   1 
ATOM   2349 C CB  . THR A 1 299 ? 2.735   5.116   26.341  1.00 42.20  ? 299 THR A CB  1 
ATOM   2350 O OG1 . THR A 1 299 ? 1.908   4.687   27.417  1.00 41.64  ? 299 THR A OG1 1 
ATOM   2351 C CG2 . THR A 1 299 ? 2.186   4.536   25.038  1.00 40.94  ? 299 THR A CG2 1 
ATOM   2352 N N   . ASN A 1 300 ? 5.417   4.176   24.546  1.00 42.08  ? 300 ASN A N   1 
ATOM   2353 C CA  . ASN A 1 300 ? 6.076   4.473   23.285  1.00 41.74  ? 300 ASN A CA  1 
ATOM   2354 C C   . ASN A 1 300 ? 5.101   4.099   22.187  1.00 41.62  ? 300 ASN A C   1 
ATOM   2355 O O   . ASN A 1 300 ? 4.392   3.080   22.273  1.00 41.02  ? 300 ASN A O   1 
ATOM   2356 C CB  . ASN A 1 300 ? 7.359   3.649   23.136  1.00 42.01  ? 300 ASN A CB  1 
ATOM   2357 C CG  . ASN A 1 300 ? 7.951   3.700   21.708  1.00 42.88  ? 300 ASN A CG  1 
ATOM   2358 O OD1 . ASN A 1 300 ? 8.365   4.749   21.256  1.00 46.42  ? 300 ASN A OD1 1 
ATOM   2359 N ND2 . ASN A 1 300 ? 8.000   2.576   21.032  1.00 42.42  ? 300 ASN A ND2 1 
ATOM   2360 N N   . TYR A 1 301 ? 5.088   4.906   21.135  1.00 42.25  ? 301 TYR A N   1 
ATOM   2361 C CA  . TYR A 1 301 ? 4.260   4.608   19.969  1.00 42.86  ? 301 TYR A CA  1 
ATOM   2362 C C   . TYR A 1 301 ? 5.084   4.241   18.767  1.00 43.30  ? 301 TYR A C   1 
ATOM   2363 O O   . TYR A 1 301 ? 6.144   4.832   18.527  1.00 42.65  ? 301 TYR A O   1 
ATOM   2364 C CB  . TYR A 1 301 ? 3.426   5.812   19.629  1.00 42.15  ? 301 TYR A CB  1 
ATOM   2365 C CG  . TYR A 1 301 ? 2.461   6.127   20.722  1.00 41.87  ? 301 TYR A CG  1 
ATOM   2366 C CD1 . TYR A 1 301 ? 1.242   5.472   20.797  1.00 40.30  ? 301 TYR A CD1 1 
ATOM   2367 C CD2 . TYR A 1 301 ? 2.747   7.090   21.659  1.00 40.66  ? 301 TYR A CD2 1 
ATOM   2368 C CE1 . TYR A 1 301 ? 0.339   5.750   21.784  1.00 40.55  ? 301 TYR A CE1 1 
ATOM   2369 C CE2 . TYR A 1 301 ? 1.835   7.389   22.673  1.00 42.46  ? 301 TYR A CE2 1 
ATOM   2370 C CZ  . TYR A 1 301 ? 0.639   6.708   22.724  1.00 41.51  ? 301 TYR A CZ  1 
ATOM   2371 O OH  . TYR A 1 301 ? -0.281  6.986   23.689  1.00 41.33  ? 301 TYR A OH  1 
ATOM   2372 N N   . ASN A 1 302 ? 4.567   3.288   17.993  1.00 45.02  ? 302 ASN A N   1 
ATOM   2373 C CA  . ASN A 1 302 ? 5.177   2.910   16.706  1.00 46.53  ? 302 ASN A CA  1 
ATOM   2374 C C   . ASN A 1 302 ? 4.162   3.026   15.573  1.00 47.65  ? 302 ASN A C   1 
ATOM   2375 O O   . ASN A 1 302 ? 2.962   2.884   15.797  1.00 47.57  ? 302 ASN A O   1 
ATOM   2376 C CB  . ASN A 1 302 ? 5.731   1.483   16.765  1.00 45.84  ? 302 ASN A CB  1 
ATOM   2377 C CG  . ASN A 1 302 ? 6.625   1.249   17.981  1.00 45.85  ? 302 ASN A CG  1 
ATOM   2378 O OD1 . ASN A 1 302 ? 7.604   1.960   18.193  1.00 42.26  ? 302 ASN A OD1 1 
ATOM   2379 N ND2 . ASN A 1 302 ? 6.302   0.232   18.757  1.00 43.47  ? 302 ASN A ND2 1 
ATOM   2380 N N   . SER A 1 303 ? 4.640   3.284   14.359  1.00 49.63  ? 303 SER A N   1 
ATOM   2381 C CA  . SER A 1 303 ? 3.743   3.560   13.235  1.00 51.21  ? 303 SER A CA  1 
ATOM   2382 C C   . SER A 1 303 ? 4.177   2.869   11.945  1.00 52.64  ? 303 SER A C   1 
ATOM   2383 O O   . SER A 1 303 ? 5.367   2.855   11.622  1.00 52.47  ? 303 SER A O   1 
ATOM   2384 C CB  . SER A 1 303 ? 3.692   5.063   13.000  1.00 51.82  ? 303 SER A CB  1 
ATOM   2385 O OG  . SER A 1 303 ? 4.967   5.532   12.575  1.00 53.06  ? 303 SER A OG  1 
ATOM   2386 N N   . ALA A 1 304 ? 3.190   2.315   11.227  1.00 54.14  ? 304 ALA A N   1 
ATOM   2387 C CA  . ALA A 1 304 ? 3.379   1.689   9.921   1.00 55.67  ? 304 ALA A CA  1 
ATOM   2388 C C   . ALA A 1 304 ? 2.961   2.642   8.812   1.00 57.09  ? 304 ALA A C   1 
ATOM   2389 O O   . ALA A 1 304 ? 2.302   3.658   9.047   1.00 57.17  ? 304 ALA A O   1 
ATOM   2390 C CB  . ALA A 1 304 ? 2.558   0.416   9.813   1.00 55.56  ? 304 ALA A CB  1 
ATOM   2391 N N   . HIS A 1 305 ? 3.359   2.315   7.594   1.00 58.88  ? 305 HIS A N   1 
ATOM   2392 C CA  . HIS A 1 305 ? 2.814   2.983   6.418   1.00 60.23  ? 305 HIS A CA  1 
ATOM   2393 C C   . HIS A 1 305 ? 2.765   1.931   5.336   1.00 61.31  ? 305 HIS A C   1 
ATOM   2394 O O   . HIS A 1 305 ? 3.783   1.328   5.002   1.00 61.63  ? 305 HIS A O   1 
ATOM   2395 C CB  . HIS A 1 305 ? 3.647   4.214   6.047   1.00 60.89  ? 305 HIS A CB  1 
ATOM   2396 C CG  . HIS A 1 305 ? 3.810   5.168   7.190   1.00 62.48  ? 305 HIS A CG  1 
ATOM   2397 N ND1 . HIS A 1 305 ? 2.822   6.056   7.569   1.00 64.19  ? 305 HIS A ND1 1 
ATOM   2398 C CD2 . HIS A 1 305 ? 4.807   5.311   8.094   1.00 63.60  ? 305 HIS A CD2 1 
ATOM   2399 C CE1 . HIS A 1 305 ? 3.221   6.730   8.634   1.00 63.71  ? 305 HIS A CE1 1 
ATOM   2400 N NE2 . HIS A 1 305 ? 4.423   6.299   8.971   1.00 64.40  ? 305 HIS A NE2 1 
ATOM   2401 N N   . ASP A 1 306 ? 1.558   1.691   4.828   1.00 62.51  ? 306 ASP A N   1 
ATOM   2402 C CA  . ASP A 1 306 ? 1.247   0.470   4.082   1.00 62.80  ? 306 ASP A CA  1 
ATOM   2403 C C   . ASP A 1 306 ? 1.356   0.692   2.577   1.00 63.25  ? 306 ASP A C   1 
ATOM   2404 O O   . ASP A 1 306 ? 0.794   -0.062  1.773   1.00 63.76  ? 306 ASP A O   1 
ATOM   2405 C CB  . ASP A 1 306 ? -0.161  -0.014  4.462   1.00 63.43  ? 306 ASP A CB  1 
ATOM   2406 C CG  . ASP A 1 306 ? -0.309  -0.312  5.960   1.00 64.43  ? 306 ASP A CG  1 
ATOM   2407 O OD1 . ASP A 1 306 ? 0.433   0.266   6.793   1.00 64.55  ? 306 ASP A OD1 1 
ATOM   2408 O OD2 . ASP A 1 306 ? -1.190  -1.130  6.308   1.00 67.01  ? 306 ASP A OD2 1 
ATOM   2409 N N   . SER A 1 309 ? 2.472   -3.120  0.049   1.00 63.41  ? 309 SER A N   1 
ATOM   2410 C CA  . SER A 1 309 ? 2.435   -4.573  0.245   1.00 63.44  ? 309 SER A CA  1 
ATOM   2411 C C   . SER A 1 309 ? 3.422   -5.125  1.288   1.00 63.45  ? 309 SER A C   1 
ATOM   2412 O O   . SER A 1 309 ? 3.509   -6.343  1.455   1.00 63.87  ? 309 SER A O   1 
ATOM   2413 C CB  . SER A 1 309 ? 2.734   -5.275  -1.076  1.00 63.62  ? 309 SER A CB  1 
ATOM   2414 O OG  . SER A 1 309 ? 4.101   -5.649  -1.143  1.00 64.26  ? 309 SER A OG  1 
ATOM   2415 N N   . ASN A 1 310 ? 4.128   -4.242  1.996   1.00 63.08  ? 310 ASN A N   1 
ATOM   2416 C CA  . ASN A 1 310 ? 5.387   -4.569  2.688   1.00 62.63  ? 310 ASN A CA  1 
ATOM   2417 C C   . ASN A 1 310 ? 5.518   -5.975  3.305   1.00 62.25  ? 310 ASN A C   1 
ATOM   2418 O O   . ASN A 1 310 ? 4.656   -6.407  4.078   1.00 62.13  ? 310 ASN A O   1 
ATOM   2419 C CB  . ASN A 1 310 ? 5.663   -3.525  3.779   1.00 62.88  ? 310 ASN A CB  1 
ATOM   2420 C CG  . ASN A 1 310 ? 7.044   -2.904  3.664   1.00 63.28  ? 310 ASN A CG  1 
ATOM   2421 O OD1 . ASN A 1 310 ? 7.809   -2.891  4.625   1.00 64.70  ? 310 ASN A OD1 1 
ATOM   2422 N ND2 . ASN A 1 310 ? 7.364   -2.380  2.490   1.00 64.91  ? 310 ASN A ND2 1 
ATOM   2423 N N   . LEU A 1 311 ? 6.611   -6.664  2.952   1.00 61.49  ? 311 LEU A N   1 
ATOM   2424 C CA  . LEU A 1 311 ? 7.044   -7.894  3.638   1.00 61.01  ? 311 LEU A CA  1 
ATOM   2425 C C   . LEU A 1 311 ? 7.189   -7.693  5.140   1.00 60.69  ? 311 LEU A C   1 
ATOM   2426 O O   . LEU A 1 311 ? 6.887   -8.597  5.912   1.00 60.71  ? 311 LEU A O   1 
ATOM   2427 C CB  . LEU A 1 311 ? 8.398   -8.395  3.106   1.00 60.30  ? 311 LEU A CB  1 
ATOM   2428 C CG  . LEU A 1 311 ? 8.472   -9.758  2.423   1.00 59.65  ? 311 LEU A CG  1 
ATOM   2429 C CD1 . LEU A 1 311 ? 9.893   -10.287 2.490   1.00 58.36  ? 311 LEU A CD1 1 
ATOM   2430 C CD2 . LEU A 1 311 ? 7.516   -10.770 3.024   1.00 58.28  ? 311 LEU A CD2 1 
ATOM   2431 N N   . LEU A 1 312 ? 7.685   -6.524  5.541   1.00 60.60  ? 312 LEU A N   1 
ATOM   2432 C CA  . LEU A 1 312 ? 7.964   -6.239  6.954   1.00 60.68  ? 312 LEU A CA  1 
ATOM   2433 C C   . LEU A 1 312 ? 6.684   -6.272  7.775   1.00 60.68  ? 312 LEU A C   1 
ATOM   2434 O O   . LEU A 1 312 ? 6.653   -6.855  8.861   1.00 60.71  ? 312 LEU A O   1 
ATOM   2435 C CB  . LEU A 1 312 ? 8.639   -4.866  7.132   1.00 60.56  ? 312 LEU A CB  1 
ATOM   2436 C CG  . LEU A 1 312 ? 9.836   -4.749  8.080   1.00 60.54  ? 312 LEU A CG  1 
ATOM   2437 C CD1 . LEU A 1 312 ? 10.030  -3.300  8.513   1.00 60.92  ? 312 LEU A CD1 1 
ATOM   2438 C CD2 . LEU A 1 312 ? 9.682   -5.629  9.304   1.00 61.06  ? 312 LEU A CD2 1 
ATOM   2439 N N   . ILE A 1 313 ? 5.639   -5.630  7.259   1.00 60.63  ? 313 ILE A N   1 
ATOM   2440 C CA  . ILE A 1 313 ? 4.364   -5.552  7.965   1.00 60.63  ? 313 ILE A CA  1 
ATOM   2441 C C   . ILE A 1 313 ? 3.597   -6.877  7.870   1.00 60.47  ? 313 ILE A C   1 
ATOM   2442 O O   . ILE A 1 313 ? 2.807   -7.189  8.755   1.00 60.77  ? 313 ILE A O   1 
ATOM   2443 C CB  . ILE A 1 313 ? 3.492   -4.339  7.492   1.00 60.81  ? 313 ILE A CB  1 
ATOM   2444 C CG1 . ILE A 1 313 ? 4.175   -3.005  7.840   1.00 61.07  ? 313 ILE A CG1 1 
ATOM   2445 C CG2 . ILE A 1 313 ? 2.118   -4.363  8.158   1.00 60.68  ? 313 ILE A CG2 1 
ATOM   2446 C CD1 . ILE A 1 313 ? 4.779   -2.281  6.658   1.00 61.40  ? 313 ILE A CD1 1 
ATOM   2447 N N   . GLU A 1 314 ? 3.845   -7.663  6.826   1.00 59.97  ? 314 GLU A N   1 
ATOM   2448 C CA  . GLU A 1 314 ? 3.277   -9.013  6.729   1.00 59.92  ? 314 GLU A CA  1 
ATOM   2449 C C   . GLU A 1 314 ? 3.857   -9.938  7.789   1.00 59.65  ? 314 GLU A C   1 
ATOM   2450 O O   . GLU A 1 314 ? 3.117   -10.556 8.553   1.00 59.73  ? 314 GLU A O   1 
ATOM   2451 C CB  . GLU A 1 314 ? 3.549   -9.619  5.359   1.00 59.72  ? 314 GLU A CB  1 
ATOM   2452 C CG  . GLU A 1 314 ? 2.641   -9.101  4.274   1.00 60.47  ? 314 GLU A CG  1 
ATOM   2453 C CD  . GLU A 1 314 ? 2.953   -9.712  2.919   1.00 60.13  ? 314 GLU A CD  1 
ATOM   2454 O OE1 . GLU A 1 314 ? 3.347   -10.900 2.864   1.00 60.53  ? 314 GLU A OE1 1 
ATOM   2455 O OE2 . GLU A 1 314 ? 2.799   -9.002  1.910   1.00 61.31  ? 314 GLU A OE2 1 
ATOM   2456 N N   . TYR A 1 315 ? 5.186   -10.039 7.794   1.00 59.34  ? 315 TYR A N   1 
ATOM   2457 C CA  . TYR A 1 315 ? 5.967   -10.775 8.804   1.00 59.15  ? 315 TYR A CA  1 
ATOM   2458 C C   . TYR A 1 315 ? 5.382   -10.624 10.211  1.00 59.03  ? 315 TYR A C   1 
ATOM   2459 O O   . TYR A 1 315 ? 5.201   -11.601 10.935  1.00 59.13  ? 315 TYR A O   1 
ATOM   2460 C CB  . TYR A 1 315 ? 7.409   -10.252 8.759   1.00 58.81  ? 315 TYR A CB  1 
ATOM   2461 C CG  . TYR A 1 315 ? 8.394   -10.818 9.761   1.00 58.75  ? 315 TYR A CG  1 
ATOM   2462 C CD1 . TYR A 1 315 ? 8.699   -10.129 10.933  1.00 58.85  ? 315 TYR A CD1 1 
ATOM   2463 C CD2 . TYR A 1 315 ? 9.067   -12.007 9.509   1.00 58.80  ? 315 TYR A CD2 1 
ATOM   2464 C CE1 . TYR A 1 315 ? 9.623   -10.632 11.847  1.00 58.23  ? 315 TYR A CE1 1 
ATOM   2465 C CE2 . TYR A 1 315 ? 9.991   -12.512 10.410  1.00 58.43  ? 315 TYR A CE2 1 
ATOM   2466 C CZ  . TYR A 1 315 ? 10.260  -11.823 11.577  1.00 58.23  ? 315 TYR A CZ  1 
ATOM   2467 O OH  . TYR A 1 315 ? 11.173  -12.324 12.461  1.00 57.91  ? 315 TYR A OH  1 
ATOM   2468 N N   . PHE A 1 316 ? 5.074   -9.390  10.584  1.00 58.99  ? 316 PHE A N   1 
ATOM   2469 C CA  . PHE A 1 316 ? 4.536   -9.101  11.907  1.00 58.84  ? 316 PHE A CA  1 
ATOM   2470 C C   . PHE A 1 316 ? 3.053   -9.419  12.003  1.00 59.06  ? 316 PHE A C   1 
ATOM   2471 O O   . PHE A 1 316 ? 2.624   -10.077 12.943  1.00 59.01  ? 316 PHE A O   1 
ATOM   2472 C CB  . PHE A 1 316 ? 4.779   -7.642  12.260  1.00 58.25  ? 316 PHE A CB  1 
ATOM   2473 C CG  . PHE A 1 316 ? 6.194   -7.347  12.620  1.00 57.54  ? 316 PHE A CG  1 
ATOM   2474 C CD1 . PHE A 1 316 ? 6.925   -6.419  11.914  1.00 56.18  ? 316 PHE A CD1 1 
ATOM   2475 C CD2 . PHE A 1 316 ? 6.801   -8.009  13.673  1.00 57.70  ? 316 PHE A CD2 1 
ATOM   2476 C CE1 . PHE A 1 316 ? 8.229   -6.148  12.248  1.00 56.18  ? 316 PHE A CE1 1 
ATOM   2477 C CE2 . PHE A 1 316 ? 8.111   -7.742  14.014  1.00 58.04  ? 316 PHE A CE2 1 
ATOM   2478 C CZ  . PHE A 1 316 ? 8.825   -6.808  13.288  1.00 57.47  ? 316 PHE A CZ  1 
ATOM   2479 N N   . ARG A 1 317 ? 2.271   -8.962  11.029  1.00 59.35  ? 317 ARG A N   1 
ATOM   2480 C CA  . ARG A 1 317 ? 0.824   -9.175  11.054  1.00 59.65  ? 317 ARG A CA  1 
ATOM   2481 C C   . ARG A 1 317 ? 0.502   -10.657 11.202  1.00 60.03  ? 317 ARG A C   1 
ATOM   2482 O O   . ARG A 1 317 ? -0.162  -11.067 12.159  1.00 60.53  ? 317 ARG A O   1 
ATOM   2483 C CB  . ARG A 1 317 ? 0.158   -8.621  9.790   1.00 59.55  ? 317 ARG A CB  1 
ATOM   2484 C CG  . ARG A 1 317 ? -1.477  -8.651  9.976   0.00 50.00  ? 317 ARG A CG  1 
ATOM   2485 C CD  . ARG A 1 317 ? -2.164  -10.003 9.638   0.00 50.00  ? 317 ARG A CD  1 
ATOM   2486 N NE  . ARG A 1 317 ? -3.339  -9.847  8.768   0.00 50.00  ? 317 ARG A NE  1 
ATOM   2487 C CZ  . ARG A 1 317 ? -4.059  -10.853 8.264   0.00 50.00  ? 317 ARG A CZ  1 
ATOM   2488 N NH1 . ARG A 1 317 ? -3.754  -12.119 8.539   0.00 50.00  ? 317 ARG A NH1 1 
ATOM   2489 N NH2 . ARG A 1 317 ? -5.102  -10.593 7.483   0.00 50.00  ? 317 ARG A NH2 1 
ATOM   2490 N N   . ASN A 1 318 ? 1.026   -11.455 10.281  1.00 60.11  ? 318 ASN A N   1 
ATOM   2491 C CA  . ASN A 1 318 ? 0.704   -12.877 10.200  1.00 60.09  ? 318 ASN A CA  1 
ATOM   2492 C C   . ASN A 1 318 ? 1.933   -13.721 9.856   1.00 60.12  ? 318 ASN A C   1 
ATOM   2493 O O   . ASN A 1 318 ? 2.141   -14.117 8.712   1.00 59.60  ? 318 ASN A O   1 
ATOM   2494 C CB  . ASN A 1 318 ? -0.460  -13.131 9.214   1.00 60.24  ? 318 ASN A CB  1 
ATOM   2495 C CG  . ASN A 1 318 ? -0.333  -12.355 7.888   1.00 60.70  ? 318 ASN A CG  1 
ATOM   2496 O OD1 . ASN A 1 318 ? -1.223  -12.434 7.030   1.00 62.16  ? 318 ASN A OD1 1 
ATOM   2497 N ND2 . ASN A 1 318 ? 0.763   -11.629 7.709   1.00 60.06  ? 318 ASN A ND2 1 
ATOM   2498 N N   . SER A 1 328 ? 6.966   -13.070 21.617  1.00 68.18  ? 328 SER A N   1 
ATOM   2499 C CA  . SER A 1 328 ? 6.176   -11.838 21.671  1.00 68.03  ? 328 SER A CA  1 
ATOM   2500 C C   . SER A 1 328 ? 6.986   -10.536 21.664  1.00 67.86  ? 328 SER A C   1 
ATOM   2501 O O   . SER A 1 328 ? 6.476   -9.488  22.075  1.00 67.99  ? 328 SER A O   1 
ATOM   2502 C CB  . SER A 1 328 ? 5.229   -11.871 22.875  1.00 68.23  ? 328 SER A CB  1 
ATOM   2503 O OG  . SER A 1 328 ? 4.155   -12.762 22.612  1.00 69.28  ? 328 SER A OG  1 
ATOM   2504 N N   . GLU A 1 329 ? 8.230   -10.588 21.178  1.00 67.49  ? 329 GLU A N   1 
ATOM   2505 C CA  . GLU A 1 329 ? 8.925   -9.372  20.734  1.00 66.85  ? 329 GLU A CA  1 
ATOM   2506 C C   . GLU A 1 329 ? 8.477   -9.045  19.306  1.00 65.59  ? 329 GLU A C   1 
ATOM   2507 O O   . GLU A 1 329 ? 9.159   -9.305  18.312  1.00 65.88  ? 329 GLU A O   1 
ATOM   2508 C CB  . GLU A 1 329 ? 10.447  -9.484  20.855  1.00 66.88  ? 329 GLU A CB  1 
ATOM   2509 C CG  . GLU A 1 329 ? 11.170  -8.216  20.462  1.00 66.64  ? 329 GLU A CG  1 
ATOM   2510 C CD  . GLU A 1 329 ? 12.551  -8.298  20.615  0.00 50.00  ? 329 GLU A CD  1 
ATOM   2511 O OE1 . GLU A 1 329 ? 13.109  -9.343  21.045  0.00 50.00  ? 329 GLU A OE1 1 
ATOM   2512 O OE2 . GLU A 1 329 ? 13.195  -7.256  20.321  0.00 50.00  ? 329 GLU A OE2 1 
ATOM   2513 N N   . MET A 1 330 ? 7.270   -8.508  19.248  1.00 63.98  ? 330 MET A N   1 
ATOM   2514 C CA  . MET A 1 330 ? 6.763   -7.836  18.087  1.00 62.45  ? 330 MET A CA  1 
ATOM   2515 C C   . MET A 1 330 ? 7.113   -6.364  18.217  1.00 60.39  ? 330 MET A C   1 
ATOM   2516 O O   . MET A 1 330 ? 7.767   -5.937  19.179  1.00 60.47  ? 330 MET A O   1 
ATOM   2517 C CB  . MET A 1 330 ? 5.250   -7.971  18.054  1.00 62.69  ? 330 MET A CB  1 
ATOM   2518 C CG  . MET A 1 330 ? 4.645   -7.638  16.707  1.00 61.93  ? 330 MET A CG  1 
ATOM   2519 S SD  . MET A 1 330 ? 3.386   -8.822  16.317  1.00 63.53  ? 330 MET A SD  1 
ATOM   2520 C CE  . MET A 1 330 ? 4.268   -10.385 16.427  1.00 61.45  ? 330 MET A CE  1 
ATOM   2521 N N   . ILE A 1 331 ? 6.691   -5.602  17.223  1.00 57.94  ? 331 ILE A N   1 
ATOM   2522 C CA  . ILE A 1 331 ? 6.669   -4.166  17.305  1.00 55.85  ? 331 ILE A CA  1 
ATOM   2523 C C   . ILE A 1 331 ? 5.181   -3.812  17.228  1.00 54.79  ? 331 ILE A C   1 
ATOM   2524 O O   . ILE A 1 331 ? 4.521   -4.134  16.249  1.00 53.69  ? 331 ILE A O   1 
ATOM   2525 C CB  . ILE A 1 331 ? 7.468   -3.541  16.139  1.00 56.39  ? 331 ILE A CB  1 
ATOM   2526 C CG1 . ILE A 1 331 ? 8.861   -4.170  16.022  1.00 55.69  ? 331 ILE A CG1 1 
ATOM   2527 C CG2 . ILE A 1 331 ? 7.594   -2.030  16.331  1.00 57.03  ? 331 ILE A CG2 1 
ATOM   2528 C CD1 . ILE A 1 331 ? 9.618   -3.724  14.783  1.00 55.69  ? 331 ILE A CD1 1 
ATOM   2529 N N   . TRP A 1 332 ? 4.664   -3.187  18.285  1.00 53.26  ? 332 TRP A N   1 
ATOM   2530 C CA  . TRP A 1 332 ? 3.222   -2.925  18.454  1.00 51.95  ? 332 TRP A CA  1 
ATOM   2531 C C   . TRP A 1 332 ? 2.849   -1.480  18.130  1.00 50.11  ? 332 TRP A C   1 
ATOM   2532 O O   . TRP A 1 332 ? 3.704   -0.609  18.163  1.00 49.77  ? 332 TRP A O   1 
ATOM   2533 C CB  . TRP A 1 332 ? 2.854   -3.080  19.928  1.00 52.83  ? 332 TRP A CB  1 
ATOM   2534 C CG  . TRP A 1 332 ? 3.332   -4.290  20.606  1.00 53.19  ? 332 TRP A CG  1 
ATOM   2535 C CD1 . TRP A 1 332 ? 4.444   -4.415  21.418  1.00 54.00  ? 332 TRP A CD1 1 
ATOM   2536 C CD2 . TRP A 1 332 ? 2.682   -5.549  20.606  1.00 52.89  ? 332 TRP A CD2 1 
ATOM   2537 N NE1 . TRP A 1 332 ? 4.517   -5.708  21.904  1.00 54.53  ? 332 TRP A NE1 1 
ATOM   2538 C CE2 . TRP A 1 332 ? 3.444   -6.419  21.421  1.00 54.06  ? 332 TRP A CE2 1 
ATOM   2539 C CE3 . TRP A 1 332 ? 1.515   -6.028  20.013  1.00 52.96  ? 332 TRP A CE3 1 
ATOM   2540 C CZ2 . TRP A 1 332 ? 3.083   -7.745  21.621  1.00 54.29  ? 332 TRP A CZ2 1 
ATOM   2541 C CZ3 . TRP A 1 332 ? 1.158   -7.340  20.222  1.00 53.39  ? 332 TRP A CZ3 1 
ATOM   2542 C CH2 . TRP A 1 332 ? 1.938   -8.188  21.008  1.00 53.11  ? 332 TRP A CH2 1 
ATOM   2543 N N   . ASN A 1 333 ? 1.554   -1.220  17.956  1.00 48.12  ? 333 ASN A N   1 
ATOM   2544 C CA  . ASN A 1 333 ? 1.053   0.160   17.813  1.00 47.04  ? 333 ASN A CA  1 
ATOM   2545 C C   . ASN A 1 333 ? 1.490   1.070   18.983  1.00 45.13  ? 333 ASN A C   1 
ATOM   2546 O O   . ASN A 1 333 ? 1.964   2.196   18.787  1.00 43.40  ? 333 ASN A O   1 
ATOM   2547 C CB  . ASN A 1 333 ? -0.478  0.191   17.513  1.00 47.59  ? 333 ASN A CB  1 
ATOM   2548 C CG  . ASN A 1 333 ? -1.387  -0.151  18.725  1.00 49.02  ? 333 ASN A CG  1 
ATOM   2549 O OD1 . ASN A 1 333 ? -1.123  -1.073  19.506  1.00 52.51  ? 333 ASN A OD1 1 
ATOM   2550 N ND2 . ASN A 1 333 ? -2.489  0.604   18.859  1.00 49.98  ? 333 ASN A ND2 1 
ATOM   2551 N N   . PHE A 1 334 ? 1.388   0.548   20.195  1.00 43.54  ? 334 PHE A N   1 
ATOM   2552 C CA  . PHE A 1 334 ? 2.087   1.160   21.347  1.00 42.77  ? 334 PHE A CA  1 
ATOM   2553 C C   . PHE A 1 334 ? 2.623   0.100   22.298  1.00 41.44  ? 334 PHE A C   1 
ATOM   2554 O O   . PHE A 1 334 ? 2.167   -1.027  22.311  1.00 39.83  ? 334 PHE A O   1 
ATOM   2555 C CB  . PHE A 1 334 ? 1.205   2.164   22.118  1.00 41.49  ? 334 PHE A CB  1 
ATOM   2556 C CG  . PHE A 1 334 ? 0.086   1.517   22.880  1.00 40.91  ? 334 PHE A CG  1 
ATOM   2557 C CD1 . PHE A 1 334 ? 0.261   1.149   24.194  1.00 40.16  ? 334 PHE A CD1 1 
ATOM   2558 C CD2 . PHE A 1 334 ? -1.134  1.288   22.283  1.00 39.36  ? 334 PHE A CD2 1 
ATOM   2559 C CE1 . PHE A 1 334 ? -0.752  0.532   24.901  1.00 40.82  ? 334 PHE A CE1 1 
ATOM   2560 C CE2 . PHE A 1 334 ? -2.149  0.682   22.977  1.00 41.83  ? 334 PHE A CE2 1 
ATOM   2561 C CZ  . PHE A 1 334 ? -1.956  0.306   24.308  1.00 40.12  ? 334 PHE A CZ  1 
ATOM   2562 N N   . HIS A 1 335 ? 3.604   0.491   23.100  1.00 42.36  ? 335 HIS A N   1 
ATOM   2563 C CA  . HIS A 1 335 ? 4.146   -0.389  24.119  1.00 42.38  ? 335 HIS A CA  1 
ATOM   2564 C C   . HIS A 1 335 ? 4.478   0.413   25.380  1.00 42.45  ? 335 HIS A C   1 
ATOM   2565 O O   . HIS A 1 335 ? 4.926   1.547   25.286  1.00 42.31  ? 335 HIS A O   1 
ATOM   2566 C CB  . HIS A 1 335 ? 5.366   -1.135  23.600  1.00 42.36  ? 335 HIS A CB  1 
ATOM   2567 C CG  . HIS A 1 335 ? 5.986   -2.034  24.612  1.00 43.89  ? 335 HIS A CG  1 
ATOM   2568 N ND1 . HIS A 1 335 ? 5.286   -3.054  25.223  1.00 47.44  ? 335 HIS A ND1 1 
ATOM   2569 C CD2 . HIS A 1 335 ? 7.231   -2.058  25.138  1.00 43.75  ? 335 HIS A CD2 1 
ATOM   2570 C CE1 . HIS A 1 335 ? 6.079   -3.664  26.087  1.00 47.87  ? 335 HIS A CE1 1 
ATOM   2571 N NE2 . HIS A 1 335 ? 7.266   -3.083  26.050  1.00 45.72  ? 335 HIS A NE2 1 
ATOM   2572 N N   . CYS A 1 336 ? 4.256   -0.207  26.547  1.00 42.77  ? 336 CYS A N   1 
ATOM   2573 C CA  . CYS A 1 336 ? 4.348   0.478   27.838  1.00 43.49  ? 336 CYS A CA  1 
ATOM   2574 C C   . CYS A 1 336 ? 5.366   -0.205  28.723  1.00 43.00  ? 336 CYS A C   1 
ATOM   2575 O O   . CYS A 1 336 ? 5.483   -1.410  28.718  1.00 41.76  ? 336 CYS A O   1 
ATOM   2576 C CB  . CYS A 1 336 ? 3.000   0.454   28.571  1.00 43.60  ? 336 CYS A CB  1 
ATOM   2577 S SG  . CYS A 1 336 ? 1.682   1.387   27.759  1.00 44.26  ? 336 CYS A SG  1 
ATOM   2578 N N   . TRP A 1 337 ? 6.101   0.584   29.488  1.00 44.09  ? 337 TRP A N   1 
ATOM   2579 C CA  . TRP A 1 337 ? 6.957   0.025   30.521  1.00 44.32  ? 337 TRP A CA  1 
ATOM   2580 C C   . TRP A 1 337 ? 6.991   1.029   31.655  1.00 44.99  ? 337 TRP A C   1 
ATOM   2581 O O   . TRP A 1 337 ? 6.181   1.944   31.683  1.00 45.17  ? 337 TRP A O   1 
ATOM   2582 C CB  . TRP A 1 337 ? 8.348   -0.344  29.973  1.00 44.93  ? 337 TRP A CB  1 
ATOM   2583 C CG  . TRP A 1 337 ? 9.161   0.759   29.358  1.00 45.22  ? 337 TRP A CG  1 
ATOM   2584 C CD1 . TRP A 1 337 ? 10.053  1.538   29.997  1.00 46.06  ? 337 TRP A CD1 1 
ATOM   2585 C CD2 . TRP A 1 337 ? 9.178   1.177   27.987  1.00 45.02  ? 337 TRP A CD2 1 
ATOM   2586 N NE1 . TRP A 1 337 ? 10.604  2.448   29.146  1.00 47.11  ? 337 TRP A NE1 1 
ATOM   2587 C CE2 . TRP A 1 337 ? 10.101  2.238   27.891  1.00 46.05  ? 337 TRP A CE2 1 
ATOM   2588 C CE3 . TRP A 1 337 ? 8.493   0.776   26.840  1.00 46.34  ? 337 TRP A CE3 1 
ATOM   2589 C CZ2 . TRP A 1 337 ? 10.369  2.899   26.688  1.00 46.83  ? 337 TRP A CZ2 1 
ATOM   2590 C CZ3 . TRP A 1 337 ? 8.779   1.416   25.627  1.00 46.37  ? 337 TRP A CZ3 1 
ATOM   2591 C CH2 . TRP A 1 337 ? 9.709   2.467   25.565  1.00 46.42  ? 337 TRP A CH2 1 
ATOM   2592 N N   . VAL A 1 338 ? 7.883   0.834   32.615  1.00 44.93  ? 338 VAL A N   1 
ATOM   2593 C CA  . VAL A 1 338 ? 8.069   1.839   33.665  1.00 44.00  ? 338 VAL A CA  1 
ATOM   2594 C C   . VAL A 1 338 ? 9.507   2.328   33.702  1.00 43.57  ? 338 VAL A C   1 
ATOM   2595 O O   . VAL A 1 338 ? 10.400  1.704   33.147  1.00 43.55  ? 338 VAL A O   1 
ATOM   2596 C CB  . VAL A 1 338 ? 7.617   1.312   35.072  1.00 43.76  ? 338 VAL A CB  1 
ATOM   2597 C CG1 . VAL A 1 338 ? 6.200   0.761   34.990  1.00 42.58  ? 338 VAL A CG1 1 
ATOM   2598 C CG2 . VAL A 1 338 ? 8.575   0.278   35.603  1.00 42.81  ? 338 VAL A CG2 1 
ATOM   2599 N N   . GLU A 1 339 ? 9.678   3.514   34.282  1.00 43.63  ? 339 GLU A N   1 
ATOM   2600 C CA  . GLU A 1 339 ? 10.970  4.033   34.624  1.00 43.83  ? 339 GLU A CA  1 
ATOM   2601 C C   . GLU A 1 339 ? 10.983  4.232   36.153  1.00 44.35  ? 339 GLU A C   1 
ATOM   2602 O O   . GLU A 1 339 ? 10.007  4.706   36.709  1.00 43.92  ? 339 GLU A O   1 
ATOM   2603 C CB  . GLU A 1 339 ? 11.191  5.376   33.967  1.00 43.92  ? 339 GLU A CB  1 
ATOM   2604 C CG  . GLU A 1 339 ? 11.421  5.263   32.474  1.00 44.63  ? 339 GLU A CG  1 
ATOM   2605 C CD  . GLU A 1 339 ? 11.481  6.583   31.806  1.00 44.50  ? 339 GLU A CD  1 
ATOM   2606 O OE1 . GLU A 1 339 ? 11.229  7.604   32.477  1.00 43.92  ? 339 GLU A OE1 1 
ATOM   2607 O OE2 . GLU A 1 339 ? 11.817  6.600   30.587  1.00 45.49  ? 339 GLU A OE2 1 
ATOM   2608 N N   . SER A 1 340 ? 12.103  3.901   36.782  1.00 45.44  ? 340 SER A N   1 
ATOM   2609 C CA  . SER A 1 340 ? 12.331  4.126   38.250  1.00 46.14  ? 340 SER A CA  1 
ATOM   2610 C C   . SER A 1 340 ? 13.615  4.949   38.495  1.00 46.79  ? 340 SER A C   1 
ATOM   2611 O O   . SER A 1 340 ? 14.628  4.780   37.783  1.00 48.57  ? 340 SER A O   1 
ATOM   2612 C CB  . SER A 1 340 ? 12.429  2.769   38.973  1.00 45.78  ? 340 SER A CB  1 
ATOM   2613 O OG  . SER A 1 340 ? 11.174  2.120   39.023  1.00 44.55  ? 340 SER A OG  1 
ATOM   2614 N N   . TRP A 1 341 ? 13.594  5.797   39.517  1.00 46.77  ? 341 TRP A N   1 
ATOM   2615 C CA  . TRP A 1 341 ? 14.694  6.743   39.778  1.00 46.83  ? 341 TRP A CA  1 
ATOM   2616 C C   . TRP A 1 341 ? 15.668  6.217   40.828  1.00 47.09  ? 341 TRP A C   1 
ATOM   2617 O O   . TRP A 1 341 ? 15.254  5.905   41.945  1.00 47.52  ? 341 TRP A O   1 
ATOM   2618 C CB  . TRP A 1 341 ? 14.112  8.069   40.241  1.00 46.70  ? 341 TRP A CB  1 
ATOM   2619 C CG  . TRP A 1 341 ? 15.130  9.175   40.471  1.00 47.40  ? 341 TRP A CG  1 
ATOM   2620 C CD1 . TRP A 1 341 ? 15.712  9.522   41.689  1.00 46.92  ? 341 TRP A CD1 1 
ATOM   2621 C CD2 . TRP A 1 341 ? 15.682  10.073  39.500  1.00 48.13  ? 341 TRP A CD2 1 
ATOM   2622 N NE1 . TRP A 1 341 ? 16.580  10.571  41.511  1.00 47.09  ? 341 TRP A NE1 1 
ATOM   2623 C CE2 . TRP A 1 341 ? 16.598  10.917  40.181  1.00 47.63  ? 341 TRP A CE2 1 
ATOM   2624 C CE3 . TRP A 1 341 ? 15.501  10.246  38.116  1.00 48.95  ? 341 TRP A CE3 1 
ATOM   2625 C CZ2 . TRP A 1 341 ? 17.303  11.942  39.536  1.00 48.37  ? 341 TRP A CZ2 1 
ATOM   2626 C CZ3 . TRP A 1 341 ? 16.227  11.239  37.463  1.00 46.84  ? 341 TRP A CZ3 1 
ATOM   2627 C CH2 . TRP A 1 341 ? 17.114  12.088  38.176  1.00 48.49  ? 341 TRP A CH2 1 
ATOM   2628 N N   . MET A 1 342 ? 16.954  6.161   40.501  1.00 47.49  ? 342 MET A N   1 
ATOM   2629 C CA  . MET A 1 342 ? 17.949  5.678   41.469  1.00 46.31  ? 342 MET A CA  1 
ATOM   2630 C C   . MET A 1 342 ? 19.336  5.905   40.962  1.00 47.55  ? 342 MET A C   1 
ATOM   2631 O O   . MET A 1 342 ? 19.547  6.030   39.735  1.00 47.85  ? 342 MET A O   1 
ATOM   2632 C CB  . MET A 1 342 ? 17.760  4.170   41.740  1.00 46.51  ? 342 MET A CB  1 
ATOM   2633 C CG  . MET A 1 342 ? 18.029  3.273   40.553  1.00 45.28  ? 342 MET A CG  1 
ATOM   2634 S SD  . MET A 1 342 ? 17.309  1.626   40.583  1.00 44.64  ? 342 MET A SD  1 
ATOM   2635 C CE  . MET A 1 342 ? 15.568  2.071   40.360  1.00 46.33  ? 342 MET A CE  1 
ATOM   2636 N N   . THR A 1 343 ? 20.316  5.913   41.884  1.00 46.97  ? 343 THR A N   1 
ATOM   2637 C CA  . THR A 1 343 ? 21.734  5.922   41.525  1.00 45.88  ? 343 THR A CA  1 
ATOM   2638 C C   . THR A 1 343 ? 22.151  4.548   41.022  1.00 45.77  ? 343 THR A C   1 
ATOM   2639 O O   . THR A 1 343 ? 21.451  3.584   41.212  1.00 45.33  ? 343 THR A O   1 
ATOM   2640 C CB  . THR A 1 343 ? 22.627  6.294   42.731  1.00 46.36  ? 343 THR A CB  1 
ATOM   2641 O OG1 . THR A 1 343 ? 22.425  5.329   43.765  1.00 46.03  ? 343 THR A OG1 1 
ATOM   2642 C CG2 . THR A 1 343 ? 22.301  7.706   43.245  1.00 46.15  ? 343 THR A CG2 1 
ATOM   2643 N N   . ARG A 1 344 ? 23.311  4.460   40.395  1.00 46.08  ? 344 ARG A N   1 
ATOM   2644 C CA  . ARG A 1 344 ? 23.778  3.192   39.812  1.00 45.98  ? 344 ARG A CA  1 
ATOM   2645 C C   . ARG A 1 344 ? 25.235  2.969   40.136  1.00 46.56  ? 344 ARG A C   1 
ATOM   2646 O O   . ARG A 1 344 ? 26.071  2.934   39.224  1.00 46.37  ? 344 ARG A O   1 
ATOM   2647 C CB  . ARG A 1 344 ? 23.570  3.182   38.280  1.00 45.65  ? 344 ARG A CB  1 
ATOM   2648 C CG  . ARG A 1 344 ? 22.120  3.134   37.834  1.00 43.91  ? 344 ARG A CG  1 
ATOM   2649 C CD  . ARG A 1 344 ? 21.387  1.885   38.304  1.00 40.97  ? 344 ARG A CD  1 
ATOM   2650 N NE  . ARG A 1 344 ? 21.951  0.606   37.860  1.00 42.83  ? 344 ARG A NE  1 
ATOM   2651 C CZ  . ARG A 1 344 ? 21.541  -0.113  36.806  1.00 42.78  ? 344 ARG A CZ  1 
ATOM   2652 N NH1 . ARG A 1 344 ? 20.604  0.338   35.963  1.00 40.98  ? 344 ARG A NH1 1 
ATOM   2653 N NH2 . ARG A 1 344 ? 22.109  -1.276  36.558  1.00 44.87  ? 344 ARG A NH2 1 
ATOM   2654 N N   . PRO A 1 345 ? 25.560  2.804   41.454  1.00 47.06  ? 345 PRO A N   1 
ATOM   2655 C CA  . PRO A 1 345 ? 26.934  2.549   41.876  1.00 47.29  ? 345 PRO A CA  1 
ATOM   2656 C C   . PRO A 1 345 ? 27.466  1.226   41.352  1.00 47.55  ? 345 PRO A C   1 
ATOM   2657 O O   . PRO A 1 345 ? 28.662  0.992   41.394  1.00 47.80  ? 345 PRO A O   1 
ATOM   2658 C CB  . PRO A 1 345 ? 26.843  2.530   43.421  1.00 47.84  ? 345 PRO A CB  1 
ATOM   2659 C CG  . PRO A 1 345 ? 25.418  2.178   43.724  1.00 47.44  ? 345 PRO A CG  1 
ATOM   2660 C CD  . PRO A 1 345 ? 24.635  2.829   42.599  1.00 47.08  ? 345 PRO A CD  1 
ATOM   2661 N N   . ASP A 1 346 ? 26.587  0.370   40.849  1.00 48.06  ? 346 ASP A N   1 
ATOM   2662 C CA  . ASP A 1 346 ? 27.004  -0.888  40.209  1.00 47.86  ? 346 ASP A CA  1 
ATOM   2663 C C   . ASP A 1 346 ? 27.471  -0.699  38.746  1.00 48.34  ? 346 ASP A C   1 
ATOM   2664 O O   . ASP A 1 346 ? 27.989  -1.626  38.126  1.00 48.03  ? 346 ASP A O   1 
ATOM   2665 C CB  . ASP A 1 346 ? 25.836  -1.868  40.234  1.00 48.11  ? 346 ASP A CB  1 
ATOM   2666 C CG  . ASP A 1 346 ? 24.687  -1.434  39.340  1.00 47.46  ? 346 ASP A CG  1 
ATOM   2667 O OD1 . ASP A 1 346 ? 24.308  -0.242  39.385  1.00 45.13  ? 346 ASP A OD1 1 
ATOM   2668 O OD2 . ASP A 1 346 ? 24.143  -2.293  38.624  1.00 47.68  ? 346 ASP A OD2 1 
ATOM   2669 N N   . LEU A 1 347 ? 27.277  0.496   38.196  1.00 48.65  ? 347 LEU A N   1 
ATOM   2670 C CA  . LEU A 1 347 ? 27.709  0.804   36.832  1.00 48.65  ? 347 LEU A CA  1 
ATOM   2671 C C   . LEU A 1 347 ? 28.797  1.864   36.859  1.00 50.06  ? 347 LEU A C   1 
ATOM   2672 O O   . LEU A 1 347 ? 29.138  2.410   37.904  1.00 50.24  ? 347 LEU A O   1 
ATOM   2673 C CB  . LEU A 1 347 ? 26.547  1.340   35.978  1.00 47.71  ? 347 LEU A CB  1 
ATOM   2674 C CG  . LEU A 1 347 ? 25.327  0.449   35.863  1.00 46.76  ? 347 LEU A CG  1 
ATOM   2675 C CD1 . LEU A 1 347 ? 24.235  1.181   35.079  1.00 46.00  ? 347 LEU A CD1 1 
ATOM   2676 C CD2 . LEU A 1 347 ? 25.686  -0.875  35.236  1.00 44.98  ? 347 LEU A CD2 1 
ATOM   2677 N N   . GLN A 1 348 ? 29.313  2.178   35.682  1.00 50.93  ? 348 GLN A N   1 
ATOM   2678 C CA  . GLN A 1 348 ? 30.248  3.259   35.555  1.00 51.81  ? 348 GLN A CA  1 
ATOM   2679 C C   . GLN A 1 348 ? 29.550  4.569   35.928  1.00 51.43  ? 348 GLN A C   1 
ATOM   2680 O O   . GLN A 1 348 ? 28.319  4.697   35.820  1.00 51.31  ? 348 GLN A O   1 
ATOM   2681 C CB  . GLN A 1 348 ? 30.828  3.292   34.135  1.00 52.56  ? 348 GLN A CB  1 
ATOM   2682 C CG  . GLN A 1 348 ? 31.638  2.030   33.768  1.00 55.08  ? 348 GLN A CG  1 
ATOM   2683 C CD  . GLN A 1 348 ? 33.127  2.153   34.071  1.00 58.23  ? 348 GLN A CD  1 
ATOM   2684 O OE1 . GLN A 1 348 ? 33.614  1.639   35.090  1.00 61.22  ? 348 GLN A OE1 1 
ATOM   2685 N NE2 . GLN A 1 348 ? 33.861  2.833   33.185  1.00 59.23  ? 348 GLN A NE2 1 
ATOM   2686 N N   . PRO A 1 349 ? 30.333  5.546   36.390  1.00 51.48  ? 349 PRO A N   1 
ATOM   2687 C CA  . PRO A 1 349 ? 29.825  6.841   36.819  1.00 51.11  ? 349 PRO A CA  1 
ATOM   2688 C C   . PRO A 1 349 ? 28.935  7.521   35.786  1.00 50.71  ? 349 PRO A C   1 
ATOM   2689 O O   . PRO A 1 349 ? 29.221  7.458   34.588  1.00 50.99  ? 349 PRO A O   1 
ATOM   2690 C CB  . PRO A 1 349 ? 31.107  7.663   37.003  1.00 51.69  ? 349 PRO A CB  1 
ATOM   2691 C CG  . PRO A 1 349 ? 32.148  6.673   37.319  1.00 51.89  ? 349 PRO A CG  1 
ATOM   2692 C CD  . PRO A 1 349 ? 31.802  5.462   36.517  1.00 51.85  ? 349 PRO A CD  1 
ATOM   2693 N N   . GLY A 1 350 ? 27.869  8.158   36.254  1.00 49.90  ? 350 GLY A N   1 
ATOM   2694 C CA  . GLY A 1 350 ? 27.035  9.028   35.433  1.00 49.66  ? 350 GLY A CA  1 
ATOM   2695 C C   . GLY A 1 350 ? 25.741  8.413   34.943  1.00 49.34  ? 350 GLY A C   1 
ATOM   2696 O O   . GLY A 1 350 ? 25.049  9.013   34.124  1.00 49.23  ? 350 GLY A O   1 
ATOM   2697 N N   . TYR A 1 351 ? 25.410  7.219   35.421  1.00 48.57  ? 351 TYR A N   1 
ATOM   2698 C CA  . TYR A 1 351 ? 24.178  6.548   35.007  1.00 48.57  ? 351 TYR A CA  1 
ATOM   2699 C C   . TYR A 1 351 ? 23.035  6.585   36.029  1.00 48.29  ? 351 TYR A C   1 
ATOM   2700 O O   . TYR A 1 351 ? 22.021  5.911   35.862  1.00 48.27  ? 351 TYR A O   1 
ATOM   2701 C CB  . TYR A 1 351 ? 24.484  5.113   34.577  1.00 49.10  ? 351 TYR A CB  1 
ATOM   2702 C CG  . TYR A 1 351 ? 24.935  5.006   33.133  1.00 49.41  ? 351 TYR A CG  1 
ATOM   2703 C CD1 . TYR A 1 351 ? 24.257  5.681   32.115  1.00 50.68  ? 351 TYR A CD1 1 
ATOM   2704 C CD2 . TYR A 1 351 ? 26.019  4.235   32.789  1.00 49.19  ? 351 TYR A CD2 1 
ATOM   2705 C CE1 . TYR A 1 351 ? 24.661  5.579   30.793  1.00 50.29  ? 351 TYR A CE1 1 
ATOM   2706 C CE2 . TYR A 1 351 ? 26.434  4.129   31.466  1.00 51.17  ? 351 TYR A CE2 1 
ATOM   2707 C CZ  . TYR A 1 351 ? 25.757  4.805   30.483  1.00 50.37  ? 351 TYR A CZ  1 
ATOM   2708 O OH  . TYR A 1 351 ? 26.171  4.686   29.183  1.00 50.69  ? 351 TYR A OH  1 
ATOM   2709 N N   . GLU A 1 352 ? 23.189  7.385   37.079  1.00 47.80  ? 352 GLU A N   1 
ATOM   2710 C CA  . GLU A 1 352 ? 22.089  7.645   37.998  1.00 47.16  ? 352 GLU A CA  1 
ATOM   2711 C C   . GLU A 1 352 ? 20.904  8.296   37.314  1.00 47.25  ? 352 GLU A C   1 
ATOM   2712 O O   . GLU A 1 352 ? 21.068  9.086   36.337  1.00 46.38  ? 352 GLU A O   1 
ATOM   2713 C CB  . GLU A 1 352 ? 22.543  8.536   39.161  1.00 47.56  ? 352 GLU A CB  1 
ATOM   2714 C CG  . GLU A 1 352 ? 23.102  9.901   38.776  1.00 48.39  ? 352 GLU A CG  1 
ATOM   2715 C CD  . GLU A 1 352 ? 24.566  9.882   38.346  1.00 50.35  ? 352 GLU A CD  1 
ATOM   2716 O OE1 . GLU A 1 352 ? 25.080  10.963  38.045  1.00 53.05  ? 352 GLU A OE1 1 
ATOM   2717 O OE2 . GLU A 1 352 ? 25.215  8.815   38.302  1.00 51.96  ? 352 GLU A OE2 1 
ATOM   2718 N N   . GLY A 1 353 ? 19.708  8.000   37.824  1.00 45.80  ? 353 GLY A N   1 
ATOM   2719 C CA  . GLY A 1 353 ? 18.511  8.727   37.414  1.00 45.75  ? 353 GLY A CA  1 
ATOM   2720 C C   . GLY A 1 353 ? 17.451  7.767   36.965  1.00 45.63  ? 353 GLY A C   1 
ATOM   2721 O O   . GLY A 1 353 ? 17.247  6.753   37.606  1.00 44.73  ? 353 GLY A O   1 
ATOM   2722 N N   . TRP A 1 354 ? 16.836  8.006   35.802  1.00 45.21  ? 354 TRP A N   1 
ATOM   2723 C CA  . TRP A 1 354 ? 15.767  7.118   35.352  1.00 45.58  ? 354 TRP A CA  1 
ATOM   2724 C C   . TRP A 1 354 ? 16.335  5.847   34.769  1.00 46.02  ? 354 TRP A C   1 
ATOM   2725 O O   . TRP A 1 354 ? 17.271  5.887   33.943  1.00 46.17  ? 354 TRP A O   1 
ATOM   2726 C CB  . TRP A 1 354 ? 14.853  7.800   34.333  1.00 46.55  ? 354 TRP A CB  1 
ATOM   2727 C CG  . TRP A 1 354 ? 14.014  8.876   34.892  1.00 45.85  ? 354 TRP A CG  1 
ATOM   2728 C CD1 . TRP A 1 354 ? 14.082  10.189  34.592  1.00 46.43  ? 354 TRP A CD1 1 
ATOM   2729 C CD2 . TRP A 1 354 ? 12.930  8.731   35.826  1.00 47.67  ? 354 TRP A CD2 1 
ATOM   2730 N NE1 . TRP A 1 354 ? 13.135  10.883  35.284  1.00 46.59  ? 354 TRP A NE1 1 
ATOM   2731 C CE2 . TRP A 1 354 ? 12.418  10.013  36.060  1.00 46.66  ? 354 TRP A CE2 1 
ATOM   2732 C CE3 . TRP A 1 354 ? 12.387  7.655   36.520  1.00 46.53  ? 354 TRP A CE3 1 
ATOM   2733 C CZ2 . TRP A 1 354 ? 11.361  10.244  36.923  1.00 47.44  ? 354 TRP A CZ2 1 
ATOM   2734 C CZ3 . TRP A 1 354 ? 11.320  7.886   37.398  1.00 47.01  ? 354 TRP A CZ3 1 
ATOM   2735 C CH2 . TRP A 1 354 ? 10.827  9.150   37.591  1.00 47.18  ? 354 TRP A CH2 1 
ATOM   2736 N N   . GLN A 1 355 ? 15.733  4.728   35.191  1.00 45.22  ? 355 GLN A N   1 
ATOM   2737 C CA  . GLN A 1 355 ? 16.084  3.398   34.756  1.00 45.29  ? 355 GLN A CA  1 
ATOM   2738 C C   . GLN A 1 355 ? 14.848  2.742   34.200  1.00 45.94  ? 355 GLN A C   1 
ATOM   2739 O O   . GLN A 1 355 ? 13.813  2.690   34.878  1.00 46.40  ? 355 GLN A O   1 
ATOM   2740 C CB  . GLN A 1 355 ? 16.595  2.553   35.932  1.00 44.76  ? 355 GLN A CB  1 
ATOM   2741 C CG  . GLN A 1 355 ? 17.518  3.309   36.868  1.00 43.38  ? 355 GLN A CG  1 
ATOM   2742 C CD  . GLN A 1 355 ? 18.879  3.568   36.272  1.00 43.00  ? 355 GLN A CD  1 
ATOM   2743 O OE1 . GLN A 1 355 ? 19.482  2.668   35.724  1.00 40.64  ? 355 GLN A OE1 1 
ATOM   2744 N NE2 . GLN A 1 355 ? 19.400  4.795   36.425  1.00 39.00  ? 355 GLN A NE2 1 
ATOM   2745 N N   . ALA A 1 356 ? 14.952  2.246   32.957  1.00 45.23  ? 356 ALA A N   1 
ATOM   2746 C CA  . ALA A 1 356 ? 13.868  1.504   32.320  1.00 45.09  ? 356 ALA A CA  1 
ATOM   2747 C C   . ALA A 1 356 ? 13.713  0.085   32.858  1.00 44.27  ? 356 ALA A C   1 
ATOM   2748 O O   . ALA A 1 356 ? 14.673  -0.677  32.980  1.00 43.99  ? 356 ALA A O   1 
ATOM   2749 C CB  . ALA A 1 356 ? 14.053  1.484   30.726  1.00 44.49  ? 356 ALA A CB  1 
ATOM   2750 N N   . LEU A 1 357 ? 12.471  -0.267  33.179  1.00 44.59  ? 357 LEU A N   1 
ATOM   2751 C CA  . LEU A 1 357 ? 12.118  -1.608  33.604  1.00 45.51  ? 357 LEU A CA  1 
ATOM   2752 C C   . LEU A 1 357 ? 10.930  -2.079  32.766  1.00 45.90  ? 357 LEU A C   1 
ATOM   2753 O O   . LEU A 1 357 ? 9.887   -1.444  32.779  1.00 45.07  ? 357 LEU A O   1 
ATOM   2754 C CB  . LEU A 1 357 ? 11.741  -1.585  35.109  1.00 45.16  ? 357 LEU A CB  1 
ATOM   2755 C CG  . LEU A 1 357 ? 12.897  -1.474  36.126  1.00 45.01  ? 357 LEU A CG  1 
ATOM   2756 C CD1 . LEU A 1 357 ? 12.411  -0.947  37.508  1.00 45.23  ? 357 LEU A CD1 1 
ATOM   2757 C CD2 . LEU A 1 357 ? 13.598  -2.838  36.291  1.00 45.87  ? 357 LEU A CD2 1 
ATOM   2758 N N   . ASP A 1 358 ? 11.069  -3.197  32.069  1.00 48.09  ? 358 ASP A N   1 
ATOM   2759 C CA  . ASP A 1 358 ? 10.013  -3.678  31.182  1.00 49.13  ? 358 ASP A CA  1 
ATOM   2760 C C   . ASP A 1 358 ? 9.492   -5.047  31.630  1.00 49.79  ? 358 ASP A C   1 
ATOM   2761 O O   . ASP A 1 358 ? 10.150  -6.042  31.373  1.00 50.40  ? 358 ASP A O   1 
ATOM   2762 C CB  . ASP A 1 358 ? 10.564  -3.712  29.752  1.00 49.68  ? 358 ASP A CB  1 
ATOM   2763 C CG  . ASP A 1 358 ? 9.466   -3.772  28.683  1.00 49.78  ? 358 ASP A CG  1 
ATOM   2764 O OD1 . ASP A 1 358 ? 8.300   -4.142  28.998  1.00 51.28  ? 358 ASP A OD1 1 
ATOM   2765 O OD2 . ASP A 1 358 ? 9.801   -3.449  27.522  1.00 51.48  ? 358 ASP A OD2 1 
ATOM   2766 N N   . PRO A 1 359 ? 8.325   -5.101  32.332  1.00 51.97  ? 359 PRO A N   1 
ATOM   2767 C CA  . PRO A 1 359 ? 7.702   -6.321  32.910  1.00 53.56  ? 359 PRO A CA  1 
ATOM   2768 C C   . PRO A 1 359 ? 6.866   -7.188  31.960  1.00 56.00  ? 359 PRO A C   1 
ATOM   2769 O O   . PRO A 1 359 ? 6.136   -8.088  32.422  1.00 56.62  ? 359 PRO A O   1 
ATOM   2770 C CB  . PRO A 1 359 ? 6.759   -5.757  33.972  1.00 53.58  ? 359 PRO A CB  1 
ATOM   2771 C CG  . PRO A 1 359 ? 6.331   -4.446  33.410  1.00 53.35  ? 359 PRO A CG  1 
ATOM   2772 C CD  . PRO A 1 359 ? 7.519   -3.902  32.653  1.00 52.20  ? 359 PRO A CD  1 
ATOM   2773 N N   . THR A 1 360 ? 6.966   -6.922  30.664  1.00 57.20  ? 360 THR A N   1 
ATOM   2774 C CA  . THR A 1 360 ? 6.252   -7.679  29.652  1.00 58.74  ? 360 THR A CA  1 
ATOM   2775 C C   . THR A 1 360 ? 6.983   -9.015  29.467  1.00 60.21  ? 360 THR A C   1 
ATOM   2776 O O   . THR A 1 360 ? 8.213   -9.048  29.507  1.00 61.58  ? 360 THR A O   1 
ATOM   2777 C CB  . THR A 1 360 ? 6.113   -6.816  28.353  1.00 58.71  ? 360 THR A CB  1 
ATOM   2778 O OG1 . THR A 1 360 ? 5.209   -5.742  28.638  1.00 58.18  ? 360 THR A OG1 1 
ATOM   2779 C CG2 . THR A 1 360 ? 5.589   -7.636  27.141  1.00 58.56  ? 360 THR A CG2 1 
ATOM   2780 N N   . PRO A 1 361 ? 6.228   -10.116 29.272  1.00 61.95  ? 361 PRO A N   1 
ATOM   2781 C CA  . PRO A 1 361 ? 6.579   -11.536 29.454  1.00 62.69  ? 361 PRO A CA  1 
ATOM   2782 C C   . PRO A 1 361 ? 8.031   -12.058 29.295  1.00 64.01  ? 361 PRO A C   1 
ATOM   2783 O O   . PRO A 1 361 ? 8.689   -12.383 30.310  1.00 65.22  ? 361 PRO A O   1 
ATOM   2784 C CB  . PRO A 1 361 ? 5.672   -12.238 28.441  1.00 62.83  ? 361 PRO A CB  1 
ATOM   2785 C CG  . PRO A 1 361 ? 4.516   -11.355 28.270  1.00 62.09  ? 361 PRO A CG  1 
ATOM   2786 C CD  . PRO A 1 361 ? 4.845   -9.996  28.778  1.00 62.05  ? 361 PRO A CD  1 
ATOM   2787 N N   . GLN A 1 362 ? 8.508   -12.160 28.055  1.00 64.66  ? 362 GLN A N   1 
ATOM   2788 C CA  . GLN A 1 362 ? 9.575   -13.123 27.717  1.00 65.39  ? 362 GLN A CA  1 
ATOM   2789 C C   . GLN A 1 362 ? 10.954  -12.773 28.312  1.00 66.40  ? 362 GLN A C   1 
ATOM   2790 O O   . GLN A 1 362 ? 11.684  -11.926 27.753  1.00 67.35  ? 362 GLN A O   1 
ATOM   2791 C CB  . GLN A 1 362 ? 9.713   -13.232 26.203  1.00 65.08  ? 362 GLN A CB  1 
ATOM   2792 C CG  . GLN A 1 362 ? 8.621   -14.022 25.459  1.00 66.27  ? 362 GLN A CG  1 
ATOM   2793 C CD  . GLN A 1 362 ? 8.768   -13.862 23.957  1.00 66.03  ? 362 GLN A CD  1 
ATOM   2794 O OE1 . GLN A 1 362 ? 9.310   -12.831 23.482  1.00 68.97  ? 362 GLN A OE1 1 
ATOM   2795 N NE2 . GLN A 1 362 ? 8.258   -14.861 23.192  1.00 64.90  ? 362 GLN A NE2 1 
ATOM   2796 N N   . GLU A 1 363 ? 11.281  -13.408 29.446  1.00 67.46  ? 363 GLU A N   1 
ATOM   2797 C CA  . GLU A 1 363 ? 12.673  -13.495 29.961  1.00 67.69  ? 363 GLU A CA  1 
ATOM   2798 C C   . GLU A 1 363 ? 13.311  -14.725 29.287  1.00 68.12  ? 363 GLU A C   1 
ATOM   2799 O O   . GLU A 1 363 ? 12.914  -15.869 29.534  1.00 68.32  ? 363 GLU A O   1 
ATOM   2800 C CB  . GLU A 1 363 ? 12.740  -13.564 31.501  1.00 68.06  ? 363 GLU A CB  1 
ATOM   2801 C CG  . GLU A 1 363 ? 11.443  -14.025 32.199  1.00 69.18  ? 363 GLU A CG  1 
ATOM   2802 C CD  . GLU A 1 363 ? 11.662  -14.582 33.601  1.00 68.84  ? 363 GLU A CD  1 
ATOM   2803 O OE1 . GLU A 1 363 ? 11.408  -13.853 34.592  1.00 69.29  ? 363 GLU A OE1 1 
ATOM   2804 O OE2 . GLU A 1 363 ? 12.059  -15.776 33.696  1.00 70.34  ? 363 GLU A OE2 1 
ATOM   2805 N N   . LYS A 1 364 ? 14.309  -14.466 28.441  1.00 68.43  ? 364 LYS A N   1 
ATOM   2806 C CA  . LYS A 1 364 ? 14.562  -15.296 27.256  1.00 68.47  ? 364 LYS A CA  1 
ATOM   2807 C C   . LYS A 1 364 ? 16.049  -15.501 26.920  1.00 68.50  ? 364 LYS A C   1 
ATOM   2808 O O   . LYS A 1 364 ? 16.471  -16.615 26.579  1.00 67.89  ? 364 LYS A O   1 
ATOM   2809 C CB  . LYS A 1 364 ? 13.818  -14.634 26.081  1.00 68.71  ? 364 LYS A CB  1 
ATOM   2810 C CG  . LYS A 1 364 ? 14.474  -14.684 24.704  1.00 69.21  ? 364 LYS A CG  1 
ATOM   2811 C CD  . LYS A 1 364 ? 14.152  -13.414 23.925  1.00 68.93  ? 364 LYS A CD  1 
ATOM   2812 C CE  . LYS A 1 364 ? 12.640  -13.194 23.758  1.00 69.54  ? 364 LYS A CE  1 
ATOM   2813 N NZ  . LYS A 1 364 ? 12.298  -11.785 23.364  1.00 69.84  ? 364 LYS A NZ  1 
ATOM   2814 N N   . SER A 1 365 ? 16.829  -14.418 27.000  1.00 68.34  ? 365 SER A N   1 
ATOM   2815 C CA  . SER A 1 365 ? 18.257  -14.469 26.671  1.00 67.49  ? 365 SER A CA  1 
ATOM   2816 C C   . SER A 1 365 ? 19.009  -15.146 27.826  1.00 66.93  ? 365 SER A C   1 
ATOM   2817 O O   . SER A 1 365 ? 19.539  -16.258 27.681  1.00 66.92  ? 365 SER A O   1 
ATOM   2818 C CB  . SER A 1 365 ? 18.797  -13.049 26.403  1.00 67.81  ? 365 SER A CB  1 
ATOM   2819 O OG  . SER A 1 365 ? 19.999  -13.084 25.651  1.00 67.73  ? 365 SER A OG  1 
ATOM   2820 N N   . GLU A 1 366 ? 19.014  -14.479 28.977  1.00 65.44  ? 366 GLU A N   1 
ATOM   2821 C CA  . GLU A 1 366 ? 19.701  -14.977 30.157  1.00 64.38  ? 366 GLU A CA  1 
ATOM   2822 C C   . GLU A 1 366 ? 19.161  -14.256 31.390  1.00 63.05  ? 366 GLU A C   1 
ATOM   2823 O O   . GLU A 1 366 ? 18.573  -13.181 31.299  1.00 62.94  ? 366 GLU A O   1 
ATOM   2824 C CB  . GLU A 1 366 ? 21.235  -14.799 30.019  1.00 64.73  ? 366 GLU A CB  1 
ATOM   2825 C CG  . GLU A 1 366 ? 21.999  -14.291 31.299  1.00 65.18  ? 366 GLU A CG  1 
ATOM   2826 C CD  . GLU A 1 366 ? 23.461  -14.741 31.372  1.00 64.63  ? 366 GLU A CD  1 
ATOM   2827 O OE1 . GLU A 1 366 ? 23.863  -15.618 30.584  1.00 62.90  ? 366 GLU A OE1 1 
ATOM   2828 O OE2 . GLU A 1 366 ? 24.205  -14.237 32.249  1.00 66.08  ? 366 GLU A OE2 1 
ATOM   2829 N N   . GLY A 1 367 ? 19.345  -14.875 32.541  1.00 61.34  ? 367 GLY A N   1 
ATOM   2830 C CA  . GLY A 1 367 ? 19.037  -14.226 33.790  1.00 60.03  ? 367 GLY A CA  1 
ATOM   2831 C C   . GLY A 1 367 ? 17.678  -14.613 34.317  1.00 58.70  ? 367 GLY A C   1 
ATOM   2832 O O   . GLY A 1 367 ? 16.853  -15.213 33.618  1.00 58.28  ? 367 GLY A O   1 
ATOM   2833 N N   . THR A 1 368 ? 17.465  -14.245 35.572  1.00 56.67  ? 368 THR A N   1 
ATOM   2834 C CA  . THR A 1 368 ? 16.267  -14.584 36.318  1.00 55.64  ? 368 THR A CA  1 
ATOM   2835 C C   . THR A 1 368 ? 15.102  -13.732 35.849  1.00 54.12  ? 368 THR A C   1 
ATOM   2836 O O   . THR A 1 368 ? 13.949  -14.163 35.875  1.00 53.96  ? 368 THR A O   1 
ATOM   2837 C CB  . THR A 1 368 ? 16.535  -14.339 37.824  1.00 55.47  ? 368 THR A CB  1 
ATOM   2838 O OG1 . THR A 1 368 ? 17.777  -14.968 38.148  1.00 53.86  ? 368 THR A OG1 1 
ATOM   2839 C CG2 . THR A 1 368 ? 15.399  -14.883 38.707  1.00 55.36  ? 368 THR A CG2 1 
ATOM   2840 N N   . TYR A 1 369 ? 15.413  -12.523 35.404  1.00 52.89  ? 369 TYR A N   1 
ATOM   2841 C CA  . TYR A 1 369 ? 14.387  -11.549 35.098  1.00 51.92  ? 369 TYR A CA  1 
ATOM   2842 C C   . TYR A 1 369 ? 14.694  -10.784 33.826  1.00 50.30  ? 369 TYR A C   1 
ATOM   2843 O O   . TYR A 1 369 ? 15.838  -10.679 33.427  1.00 49.12  ? 369 TYR A O   1 
ATOM   2844 C CB  . TYR A 1 369 ? 14.295  -10.517 36.215  1.00 51.57  ? 369 TYR A CB  1 
ATOM   2845 C CG  . TYR A 1 369 ? 13.816  -11.043 37.541  1.00 51.50  ? 369 TYR A CG  1 
ATOM   2846 C CD1 . TYR A 1 369 ? 14.629  -10.989 38.674  1.00 52.02  ? 369 TYR A CD1 1 
ATOM   2847 C CD2 . TYR A 1 369 ? 12.551  -11.568 37.671  1.00 51.24  ? 369 TYR A CD2 1 
ATOM   2848 C CE1 . TYR A 1 369 ? 14.178  -11.480 39.914  1.00 51.00  ? 369 TYR A CE1 1 
ATOM   2849 C CE2 . TYR A 1 369 ? 12.095  -12.068 38.900  1.00 52.51  ? 369 TYR A CE2 1 
ATOM   2850 C CZ  . TYR A 1 369 ? 12.908  -12.011 40.008  1.00 51.08  ? 369 TYR A CZ  1 
ATOM   2851 O OH  . TYR A 1 369 ? 12.425  -12.518 41.184  1.00 50.80  ? 369 TYR A OH  1 
ATOM   2852 N N   . CYS A 1 370 ? 13.649  -10.199 33.259  1.00 49.29  ? 370 CYS A N   1 
ATOM   2853 C CA  . CYS A 1 370 ? 13.779  -9.230  32.182  1.00 49.21  ? 370 CYS A CA  1 
ATOM   2854 C C   . CYS A 1 370 ? 12.625  -8.235  32.301  1.00 48.16  ? 370 CYS A C   1 
ATOM   2855 O O   . CYS A 1 370 ? 11.571  -8.587  32.813  1.00 49.18  ? 370 CYS A O   1 
ATOM   2856 C CB  . CYS A 1 370 ? 13.729  -9.938  30.832  1.00 49.13  ? 370 CYS A CB  1 
ATOM   2857 S SG  . CYS A 1 370 ? 14.677  -9.073  29.516  1.00 48.33  ? 370 CYS A SG  1 
ATOM   2858 N N   . CYS A 1 371 ? 12.789  -6.995  31.869  1.00 47.10  ? 371 CYS A N   1 
ATOM   2859 C CA  . CYS A 1 371 ? 14.034  -6.464  31.355  1.00 46.68  ? 371 CYS A CA  1 
ATOM   2860 C C   . CYS A 1 371 ? 14.363  -5.224  32.126  1.00 46.43  ? 371 CYS A C   1 
ATOM   2861 O O   . CYS A 1 371 ? 13.499  -4.369  32.324  1.00 46.90  ? 371 CYS A O   1 
ATOM   2862 C CB  . CYS A 1 371 ? 13.895  -6.141  29.856  1.00 46.31  ? 371 CYS A CB  1 
ATOM   2863 S SG  . CYS A 1 371 ? 13.491  -7.552  28.875  1.00 46.96  ? 371 CYS A SG  1 
ATOM   2864 N N   . GLY A 1 372 ? 15.612  -5.117  32.567  1.00 46.45  ? 372 GLY A N   1 
ATOM   2865 C CA  . GLY A 1 372 ? 16.079  -3.929  33.303  1.00 46.13  ? 372 GLY A CA  1 
ATOM   2866 C C   . GLY A 1 372 ? 16.365  -4.207  34.794  1.00 45.20  ? 372 GLY A C   1 
ATOM   2867 O O   . GLY A 1 372 ? 16.215  -5.320  35.259  1.00 46.20  ? 372 GLY A O   1 
ATOM   2868 N N   . PRO A 1 373 ? 16.760  -3.184  35.546  1.00 44.73  ? 373 PRO A N   1 
ATOM   2869 C CA  . PRO A 1 373 ? 16.775  -1.793  35.155  1.00 44.13  ? 373 PRO A CA  1 
ATOM   2870 C C   . PRO A 1 373 ? 17.992  -1.446  34.292  1.00 43.48  ? 373 PRO A C   1 
ATOM   2871 O O   . PRO A 1 373 ? 19.090  -1.928  34.555  1.00 41.05  ? 373 PRO A O   1 
ATOM   2872 C CB  . PRO A 1 373 ? 16.866  -1.071  36.488  1.00 44.71  ? 373 PRO A CB  1 
ATOM   2873 C CG  . PRO A 1 373 ? 17.726  -2.003  37.299  1.00 45.25  ? 373 PRO A CG  1 
ATOM   2874 C CD  . PRO A 1 373 ? 17.314  -3.371  36.897  1.00 44.92  ? 373 PRO A CD  1 
ATOM   2875 N N   . VAL A 1 374 ? 17.762  -0.599  33.282  1.00 43.24  ? 374 VAL A N   1 
ATOM   2876 C CA  . VAL A 1 374 ? 18.808  -0.127  32.375  1.00 42.65  ? 374 VAL A CA  1 
ATOM   2877 C C   . VAL A 1 374 ? 18.691  1.375   32.336  1.00 41.88  ? 374 VAL A C   1 
ATOM   2878 O O   . VAL A 1 374 ? 17.594  1.909   32.255  1.00 41.18  ? 374 VAL A O   1 
ATOM   2879 C CB  . VAL A 1 374 ? 18.700  -0.755  30.958  1.00 43.61  ? 374 VAL A CB  1 
ATOM   2880 C CG1 . VAL A 1 374 ? 17.312  -0.439  30.320  1.00 40.75  ? 374 VAL A CG1 1 
ATOM   2881 C CG2 . VAL A 1 374 ? 19.896  -0.283  30.086  1.00 42.73  ? 374 VAL A CG2 1 
ATOM   2882 N N   . PRO A 1 375 ? 19.810  2.077   32.506  1.00 41.84  ? 375 PRO A N   1 
ATOM   2883 C CA  . PRO A 1 375 ? 19.676  3.519   32.487  1.00 42.45  ? 375 PRO A CA  1 
ATOM   2884 C C   . PRO A 1 375 ? 19.072  4.023   31.149  1.00 42.99  ? 375 PRO A C   1 
ATOM   2885 O O   . PRO A 1 375 ? 19.436  3.541   30.083  1.00 44.03  ? 375 PRO A O   1 
ATOM   2886 C CB  . PRO A 1 375 ? 21.114  4.019   32.672  1.00 42.04  ? 375 PRO A CB  1 
ATOM   2887 C CG  . PRO A 1 375 ? 21.894  2.851   33.207  1.00 42.88  ? 375 PRO A CG  1 
ATOM   2888 C CD  . PRO A 1 375 ? 21.194  1.627   32.746  1.00 41.52  ? 375 PRO A CD  1 
ATOM   2889 N N   . VAL A 1 376 ? 18.153  4.964   31.213  1.00 43.91  ? 376 VAL A N   1 
ATOM   2890 C CA  . VAL A 1 376 ? 17.611  5.571   30.007  1.00 43.91  ? 376 VAL A CA  1 
ATOM   2891 C C   . VAL A 1 376 ? 18.739  6.185   29.153  1.00 44.91  ? 376 VAL A C   1 
ATOM   2892 O O   . VAL A 1 376 ? 18.781  6.001   27.940  1.00 45.55  ? 376 VAL A O   1 
ATOM   2893 C CB  . VAL A 1 376 ? 16.468  6.515   30.343  1.00 44.04  ? 376 VAL A CB  1 
ATOM   2894 C CG1 . VAL A 1 376 ? 16.023  7.278   29.090  1.00 42.64  ? 376 VAL A CG1 1 
ATOM   2895 C CG2 . VAL A 1 376 ? 15.278  5.718   30.881  1.00 41.29  ? 376 VAL A CG2 1 
ATOM   2896 N N   . ARG A 1 377 ? 19.695  6.847   29.803  1.00 45.77  ? 377 ARG A N   1 
ATOM   2897 C CA  . ARG A 1 377 ? 20.846  7.407   29.115  1.00 45.15  ? 377 ARG A CA  1 
ATOM   2898 C C   . ARG A 1 377 ? 21.694  6.388   28.344  1.00 45.05  ? 377 ARG A C   1 
ATOM   2899 O O   . ARG A 1 377 ? 22.280  6.741   27.313  1.00 44.03  ? 377 ARG A O   1 
ATOM   2900 C CB  . ARG A 1 377 ? 21.743  8.203   30.066  1.00 45.27  ? 377 ARG A CB  1 
ATOM   2901 C CG  . ARG A 1 377 ? 22.599  9.233   29.323  1.00 47.01  ? 377 ARG A CG  1 
ATOM   2902 C CD  . ARG A 1 377 ? 23.295  10.207  30.255  1.00 49.83  ? 377 ARG A CD  1 
ATOM   2903 N NE  . ARG A 1 377 ? 24.350  9.568   31.053  1.00 53.79  ? 377 ARG A NE  1 
ATOM   2904 C CZ  . ARG A 1 377 ? 25.565  9.244   30.607  1.00 55.09  ? 377 ARG A CZ  1 
ATOM   2905 N NH1 . ARG A 1 377 ? 25.918  9.474   29.351  1.00 55.62  ? 377 ARG A NH1 1 
ATOM   2906 N NH2 . ARG A 1 377 ? 26.443  8.663   31.425  1.00 55.54  ? 377 ARG A NH2 1 
ATOM   2907 N N   . ALA A 1 378 ? 21.779  5.156   28.834  1.00 43.44  ? 378 ALA A N   1 
ATOM   2908 C CA  . ALA A 1 378 ? 22.501  4.107   28.129  1.00 43.57  ? 378 ALA A CA  1 
ATOM   2909 C C   . ALA A 1 378 ? 21.783  3.760   26.832  1.00 43.12  ? 378 ALA A C   1 
ATOM   2910 O O   . ALA A 1 378 ? 22.423  3.509   25.809  1.00 43.90  ? 378 ALA A O   1 
ATOM   2911 C CB  . ALA A 1 378 ? 22.656  2.846   29.006  1.00 41.99  ? 378 ALA A CB  1 
ATOM   2912 N N   . ILE A 1 379 ? 20.452  3.750   26.881  1.00 42.91  ? 379 ILE A N   1 
ATOM   2913 C CA  . ILE A 1 379 ? 19.623  3.551   25.699  1.00 42.99  ? 379 ILE A CA  1 
ATOM   2914 C C   . ILE A 1 379 ? 19.840  4.687   24.658  1.00 43.51  ? 379 ILE A C   1 
ATOM   2915 O O   . ILE A 1 379 ? 20.199  4.435   23.492  1.00 42.44  ? 379 ILE A O   1 
ATOM   2916 C CB  . ILE A 1 379 ? 18.136  3.434   26.079  1.00 43.39  ? 379 ILE A CB  1 
ATOM   2917 C CG1 . ILE A 1 379 ? 17.936  2.268   27.075  1.00 43.70  ? 379 ILE A CG1 1 
ATOM   2918 C CG2 . ILE A 1 379 ? 17.268  3.211   24.843  1.00 43.10  ? 379 ILE A CG2 1 
ATOM   2919 C CD1 . ILE A 1 379 ? 18.644  0.972   26.687  1.00 42.50  ? 379 ILE A CD1 1 
ATOM   2920 N N   . LYS A 1 380 ? 19.672  5.928   25.098  1.00 42.63  ? 380 LYS A N   1 
ATOM   2921 C CA  . LYS A 1 380 ? 19.895  7.070   24.225  1.00 43.20  ? 380 LYS A CA  1 
ATOM   2922 C C   . LYS A 1 380 ? 21.279  7.045   23.591  1.00 43.23  ? 380 LYS A C   1 
ATOM   2923 O O   . LYS A 1 380 ? 21.456  7.407   22.447  1.00 42.48  ? 380 LYS A O   1 
ATOM   2924 C CB  . LYS A 1 380 ? 19.737  8.376   24.985  1.00 42.32  ? 380 LYS A CB  1 
ATOM   2925 C CG  . LYS A 1 380 ? 19.579  9.573   24.064  1.00 42.51  ? 380 LYS A CG  1 
ATOM   2926 C CD  . LYS A 1 380 ? 19.552  10.844  24.859  1.00 43.20  ? 380 LYS A CD  1 
ATOM   2927 C CE  . LYS A 1 380 ? 19.262  12.020  23.995  1.00 42.27  ? 380 LYS A CE  1 
ATOM   2928 N NZ  . LYS A 1 380 ? 18.795  13.164  24.830  1.00 42.73  ? 380 LYS A NZ  1 
ATOM   2929 N N   . GLU A 1 381 ? 22.252  6.608   24.363  1.00 44.17  ? 381 GLU A N   1 
ATOM   2930 C CA  . GLU A 1 381 ? 23.655  6.654   23.975  1.00 45.56  ? 381 GLU A CA  1 
ATOM   2931 C C   . GLU A 1 381 ? 24.083  5.401   23.214  1.00 45.91  ? 381 GLU A C   1 
ATOM   2932 O O   . GLU A 1 381 ? 25.209  5.325   22.731  1.00 46.61  ? 381 GLU A O   1 
ATOM   2933 C CB  . GLU A 1 381 ? 24.486  6.810   25.256  1.00 46.12  ? 381 GLU A CB  1 
ATOM   2934 C CG  . GLU A 1 381 ? 25.510  7.893   25.272  1.00 49.46  ? 381 GLU A CG  1 
ATOM   2935 C CD  . GLU A 1 381 ? 24.994  9.212   24.760  1.00 52.02  ? 381 GLU A CD  1 
ATOM   2936 O OE1 . GLU A 1 381 ? 24.254  9.906   25.487  1.00 52.52  ? 381 GLU A OE1 1 
ATOM   2937 O OE2 . GLU A 1 381 ? 25.360  9.545   23.611  1.00 56.10  ? 381 GLU A OE2 1 
ATOM   2938 N N   . GLY A 1 382 ? 23.186  4.427   23.090  1.00 46.27  ? 382 GLY A N   1 
ATOM   2939 C CA  . GLY A 1 382 ? 23.510  3.158   22.444  1.00 46.63  ? 382 GLY A CA  1 
ATOM   2940 C C   . GLY A 1 382 ? 24.590  2.346   23.149  1.00 47.12  ? 382 GLY A C   1 
ATOM   2941 O O   . GLY A 1 382 ? 25.234  1.509   22.529  1.00 46.05  ? 382 GLY A O   1 
ATOM   2942 N N   . ASP A 1 383 ? 24.765  2.591   24.447  1.00 47.31  ? 383 ASP A N   1 
ATOM   2943 C CA  . ASP A 1 383 ? 25.740  1.888   25.258  1.00 47.61  ? 383 ASP A CA  1 
ATOM   2944 C C   . ASP A 1 383 ? 25.133  0.569   25.749  1.00 47.81  ? 383 ASP A C   1 
ATOM   2945 O O   . ASP A 1 383 ? 24.753  0.450   26.920  1.00 48.58  ? 383 ASP A O   1 
ATOM   2946 C CB  . ASP A 1 383 ? 26.129  2.779   26.449  1.00 47.71  ? 383 ASP A CB  1 
ATOM   2947 C CG  . ASP A 1 383 ? 27.229  2.172   27.309  1.00 48.13  ? 383 ASP A CG  1 
ATOM   2948 O OD1 . ASP A 1 383 ? 27.791  1.134   26.903  1.00 48.50  ? 383 ASP A OD1 1 
ATOM   2949 O OD2 . ASP A 1 383 ? 27.523  2.728   28.399  1.00 50.06  ? 383 ASP A OD2 1 
ATOM   2950 N N   . LEU A 1 384 ? 25.045  -0.414  24.863  1.00 47.40  ? 384 LEU A N   1 
ATOM   2951 C CA  . LEU A 1 384 ? 24.191  -1.590  25.083  1.00 48.09  ? 384 LEU A CA  1 
ATOM   2952 C C   . LEU A 1 384 ? 24.807  -2.720  25.929  1.00 48.41  ? 384 LEU A C   1 
ATOM   2953 O O   . LEU A 1 384 ? 24.175  -3.767  26.127  1.00 48.23  ? 384 LEU A O   1 
ATOM   2954 C CB  . LEU A 1 384 ? 23.696  -2.146  23.731  1.00 47.82  ? 384 LEU A CB  1 
ATOM   2955 C CG  . LEU A 1 384 ? 22.861  -1.168  22.878  1.00 47.90  ? 384 LEU A CG  1 
ATOM   2956 C CD1 . LEU A 1 384 ? 22.195  -1.847  21.714  1.00 45.65  ? 384 LEU A CD1 1 
ATOM   2957 C CD2 . LEU A 1 384 ? 21.817  -0.462  23.714  1.00 47.52  ? 384 LEU A CD2 1 
ATOM   2958 N N   . SER A 1 385 ? 26.025  -2.504  26.420  1.00 48.91  ? 385 SER A N   1 
ATOM   2959 C CA  . SER A 1 385 ? 26.697  -3.455  27.296  1.00 49.09  ? 385 SER A CA  1 
ATOM   2960 C C   . SER A 1 385 ? 26.349  -3.231  28.775  1.00 49.28  ? 385 SER A C   1 
ATOM   2961 O O   . SER A 1 385 ? 26.763  -4.004  29.645  1.00 50.21  ? 385 SER A O   1 
ATOM   2962 C CB  . SER A 1 385 ? 28.213  -3.358  27.099  1.00 49.30  ? 385 SER A CB  1 
ATOM   2963 O OG  . SER A 1 385 ? 28.755  -2.275  27.840  1.00 50.04  ? 385 SER A OG  1 
ATOM   2964 N N   . THR A 1 386 ? 25.599  -2.175  29.047  1.00 49.38  ? 386 THR A N   1 
ATOM   2965 C CA  . THR A 1 386 ? 25.240  -1.768  30.387  1.00 49.47  ? 386 THR A CA  1 
ATOM   2966 C C   . THR A 1 386 ? 24.089  -2.606  30.949  1.00 49.63  ? 386 THR A C   1 
ATOM   2967 O O   . THR A 1 386 ? 23.051  -2.745  30.306  1.00 50.44  ? 386 THR A O   1 
ATOM   2968 C CB  . THR A 1 386 ? 24.778  -0.295  30.386  1.00 49.55  ? 386 THR A CB  1 
ATOM   2969 O OG1 . THR A 1 386 ? 25.698  0.501   29.629  1.00 49.19  ? 386 THR A OG1 1 
ATOM   2970 C CG2 . THR A 1 386 ? 24.699  0.232   31.798  1.00 49.24  ? 386 THR A CG2 1 
ATOM   2971 N N   . LYS A 1 387 ? 24.266  -3.151  32.149  1.00 49.10  ? 387 LYS A N   1 
ATOM   2972 C CA  . LYS A 1 387 ? 23.245  -3.998  32.750  1.00 48.81  ? 387 LYS A CA  1 
ATOM   2973 C C   . LYS A 1 387 ? 22.111  -3.122  33.223  1.00 47.25  ? 387 LYS A C   1 
ATOM   2974 O O   . LYS A 1 387 ? 22.369  -1.997  33.658  1.00 46.29  ? 387 LYS A O   1 
ATOM   2975 C CB  . LYS A 1 387 ? 23.827  -4.811  33.905  1.00 48.81  ? 387 LYS A CB  1 
ATOM   2976 C CG  . LYS A 1 387 ? 24.879  -5.742  33.404  1.00 49.54  ? 387 LYS A CG  1 
ATOM   2977 C CD  . LYS A 1 387 ? 25.516  -6.601  34.476  1.00 51.92  ? 387 LYS A CD  1 
ATOM   2978 C CE  . LYS A 1 387 ? 24.554  -7.650  35.061  1.00 54.63  ? 387 LYS A CE  1 
ATOM   2979 N NZ  . LYS A 1 387 ? 25.122  -9.025  34.953  1.00 55.53  ? 387 LYS A NZ  1 
ATOM   2980 N N   . TYR A 1 388 ? 20.863  -3.604  33.154  1.00 46.82  ? 388 TYR A N   1 
ATOM   2981 C CA  . TYR A 1 388 ? 20.489  -4.976  32.695  1.00 46.39  ? 388 TYR A CA  1 
ATOM   2982 C C   . TYR A 1 388 ? 19.674  -4.914  31.385  1.00 46.38  ? 388 TYR A C   1 
ATOM   2983 O O   . TYR A 1 388 ? 18.812  -4.045  31.243  1.00 45.62  ? 388 TYR A O   1 
ATOM   2984 C CB  . TYR A 1 388 ? 19.620  -5.659  33.751  1.00 46.91  ? 388 TYR A CB  1 
ATOM   2985 C CG  . TYR A 1 388 ? 20.355  -5.969  35.048  1.00 47.95  ? 388 TYR A CG  1 
ATOM   2986 C CD1 . TYR A 1 388 ? 20.869  -7.230  35.292  1.00 47.71  ? 388 TYR A CD1 1 
ATOM   2987 C CD2 . TYR A 1 388 ? 20.552  -4.982  36.008  1.00 49.98  ? 388 TYR A CD2 1 
ATOM   2988 C CE1 . TYR A 1 388 ? 21.555  -7.520  36.462  1.00 48.16  ? 388 TYR A CE1 1 
ATOM   2989 C CE2 . TYR A 1 388 ? 21.236  -5.264  37.198  1.00 49.58  ? 388 TYR A CE2 1 
ATOM   2990 C CZ  . TYR A 1 388 ? 21.729  -6.521  37.405  1.00 48.72  ? 388 TYR A CZ  1 
ATOM   2991 O OH  . TYR A 1 388 ? 22.395  -6.780  38.562  1.00 49.75  ? 388 TYR A OH  1 
ATOM   2992 N N   . ASP A 1 389 ? 19.924  -5.848  30.466  1.00 45.64  ? 389 ASP A N   1 
ATOM   2993 C CA  . ASP A 1 389 ? 19.013  -6.096  29.330  1.00 45.58  ? 389 ASP A CA  1 
ATOM   2994 C C   . ASP A 1 389 ? 18.845  -4.875  28.382  1.00 45.69  ? 389 ASP A C   1 
ATOM   2995 O O   . ASP A 1 389 ? 17.752  -4.615  27.834  1.00 44.76  ? 389 ASP A O   1 
ATOM   2996 C CB  . ASP A 1 389 ? 17.659  -6.535  29.903  1.00 45.19  ? 389 ASP A CB  1 
ATOM   2997 C CG  . ASP A 1 389 ? 17.812  -7.621  30.959  1.00 43.55  ? 389 ASP A CG  1 
ATOM   2998 O OD1 . ASP A 1 389 ? 18.476  -8.596  30.652  1.00 39.93  ? 389 ASP A OD1 1 
ATOM   2999 O OD2 . ASP A 1 389 ? 17.311  -7.479  32.093  1.00 41.48  ? 389 ASP A OD2 1 
ATOM   3000 N N   . ALA A 1 390 ? 19.931  -4.141  28.185  1.00 45.35  ? 390 ALA A N   1 
ATOM   3001 C CA  . ALA A 1 390 ? 19.882  -2.910  27.398  1.00 45.58  ? 390 ALA A CA  1 
ATOM   3002 C C   . ALA A 1 390 ? 19.408  -3.120  25.922  1.00 45.38  ? 390 ALA A C   1 
ATOM   3003 O O   . ALA A 1 390 ? 18.654  -2.300  25.391  1.00 46.12  ? 390 ALA A O   1 
ATOM   3004 C CB  . ALA A 1 390 ? 21.236  -2.202  27.458  1.00 45.56  ? 390 ALA A CB  1 
ATOM   3005 N N   . PRO A 1 391 ? 19.843  -4.204  25.263  1.00 45.41  ? 391 PRO A N   1 
ATOM   3006 C CA  . PRO A 1 391 ? 19.348  -4.430  23.882  1.00 45.73  ? 391 PRO A CA  1 
ATOM   3007 C C   . PRO A 1 391 ? 17.824  -4.531  23.770  1.00 45.93  ? 391 PRO A C   1 
ATOM   3008 O O   . PRO A 1 391 ? 17.245  -4.065  22.795  1.00 44.87  ? 391 PRO A O   1 
ATOM   3009 C CB  . PRO A 1 391 ? 20.018  -5.739  23.500  1.00 45.08  ? 391 PRO A CB  1 
ATOM   3010 C CG  . PRO A 1 391 ? 21.275  -5.723  24.268  1.00 45.41  ? 391 PRO A CG  1 
ATOM   3011 C CD  . PRO A 1 391 ? 20.839  -5.220  25.630  1.00 44.88  ? 391 PRO A CD  1 
ATOM   3012 N N   . PHE A 1 392 ? 17.180  -5.104  24.787  1.00 46.63  ? 392 PHE A N   1 
ATOM   3013 C CA  . PHE A 1 392 ? 15.734  -5.293  24.759  1.00 47.08  ? 392 PHE A CA  1 
ATOM   3014 C C   . PHE A 1 392 ? 14.992  -3.977  24.830  1.00 47.35  ? 392 PHE A C   1 
ATOM   3015 O O   . PHE A 1 392 ? 13.977  -3.815  24.165  1.00 47.67  ? 392 PHE A O   1 
ATOM   3016 C CB  . PHE A 1 392 ? 15.271  -6.201  25.889  1.00 48.85  ? 392 PHE A CB  1 
ATOM   3017 C CG  . PHE A 1 392 ? 15.599  -7.646  25.682  1.00 50.25  ? 392 PHE A CG  1 
ATOM   3018 C CD1 . PHE A 1 392 ? 14.749  -8.464  24.932  1.00 52.09  ? 392 PHE A CD1 1 
ATOM   3019 C CD2 . PHE A 1 392 ? 16.749  -8.199  26.234  1.00 51.45  ? 392 PHE A CD2 1 
ATOM   3020 C CE1 . PHE A 1 392 ? 15.035  -9.812  24.745  1.00 51.83  ? 392 PHE A CE1 1 
ATOM   3021 C CE2 . PHE A 1 392 ? 17.042  -9.537  26.064  1.00 51.32  ? 392 PHE A CE2 1 
ATOM   3022 C CZ  . PHE A 1 392 ? 16.186  -10.356 25.307  1.00 52.08  ? 392 PHE A CZ  1 
ATOM   3023 N N   . VAL A 1 393 ? 15.491  -3.026  25.621  1.00 46.64  ? 393 VAL A N   1 
ATOM   3024 C CA  . VAL A 1 393 ? 14.858  -1.722  25.698  1.00 46.21  ? 393 VAL A CA  1 
ATOM   3025 C C   . VAL A 1 393 ? 15.225  -0.833  24.493  1.00 45.68  ? 393 VAL A C   1 
ATOM   3026 O O   . VAL A 1 393 ? 14.380  -0.117  24.002  1.00 44.50  ? 393 VAL A O   1 
ATOM   3027 C CB  . VAL A 1 393 ? 15.163  -0.979  27.031  1.00 45.86  ? 393 VAL A CB  1 
ATOM   3028 C CG1 . VAL A 1 393 ? 14.322  0.275   27.117  1.00 45.96  ? 393 VAL A CG1 1 
ATOM   3029 C CG2 . VAL A 1 393 ? 14.889  -1.901  28.238  1.00 46.69  ? 393 VAL A CG2 1 
ATOM   3030 N N   . PHE A 1 394 ? 16.482  -0.881  24.053  1.00 45.83  ? 394 PHE A N   1 
ATOM   3031 C CA  . PHE A 1 394 ? 16.918  -0.220  22.809  1.00 45.90  ? 394 PHE A CA  1 
ATOM   3032 C C   . PHE A 1 394 ? 16.007  -0.591  21.627  1.00 45.57  ? 394 PHE A C   1 
ATOM   3033 O O   . PHE A 1 394 ? 15.555  0.284   20.896  1.00 45.98  ? 394 PHE A O   1 
ATOM   3034 C CB  . PHE A 1 394 ? 18.372  -0.581  22.518  1.00 46.30  ? 394 PHE A CB  1 
ATOM   3035 C CG  . PHE A 1 394 ? 19.003  0.230   21.418  1.00 46.54  ? 394 PHE A CG  1 
ATOM   3036 C CD1 . PHE A 1 394 ? 19.561  1.477   21.686  1.00 47.11  ? 394 PHE A CD1 1 
ATOM   3037 C CD2 . PHE A 1 394 ? 19.058  -0.268  20.117  1.00 46.86  ? 394 PHE A CD2 1 
ATOM   3038 C CE1 . PHE A 1 394 ? 20.149  2.223   20.671  1.00 47.58  ? 394 PHE A CE1 1 
ATOM   3039 C CE2 . PHE A 1 394 ? 19.650  0.471   19.095  1.00 47.61  ? 394 PHE A CE2 1 
ATOM   3040 C CZ  . PHE A 1 394 ? 20.196  1.726   19.381  1.00 47.09  ? 394 PHE A CZ  1 
ATOM   3041 N N   . ALA A 1 395 ? 15.731  -1.887  21.476  1.00 44.90  ? 395 ALA A N   1 
ATOM   3042 C CA  . ALA A 1 395 ? 14.883  -2.412  20.414  1.00 45.47  ? 395 ALA A CA  1 
ATOM   3043 C C   . ALA A 1 395 ? 13.451  -1.922  20.436  1.00 45.56  ? 395 ALA A C   1 
ATOM   3044 O O   . ALA A 1 395 ? 12.810  -1.907  19.407  1.00 47.12  ? 395 ALA A O   1 
ATOM   3045 C CB  . ALA A 1 395 ? 14.897  -3.935  20.419  1.00 44.96  ? 395 ALA A CB  1 
ATOM   3046 N N   . GLU A 1 396 ? 12.935  -1.532  21.591  1.00 46.40  ? 396 GLU A N   1 
ATOM   3047 C CA  . GLU A 1 396 ? 11.563  -1.010  21.664  1.00 46.21  ? 396 GLU A CA  1 
ATOM   3048 C C   . GLU A 1 396 ? 11.462  0.416   21.118  1.00 46.11  ? 396 GLU A C   1 
ATOM   3049 O O   . GLU A 1 396 ? 10.381  0.838   20.703  1.00 46.49  ? 396 GLU A O   1 
ATOM   3050 C CB  . GLU A 1 396 ? 11.042  -1.041  23.117  1.00 46.68  ? 396 GLU A CB  1 
ATOM   3051 C CG  . GLU A 1 396 ? 10.788  -2.461  23.688  1.00 49.73  ? 396 GLU A CG  1 
ATOM   3052 C CD  . GLU A 1 396 ? 9.723   -3.256  22.922  1.00 53.87  ? 396 GLU A CD  1 
ATOM   3053 O OE1 . GLU A 1 396 ? 8.701   -2.662  22.520  1.00 57.28  ? 396 GLU A OE1 1 
ATOM   3054 O OE2 . GLU A 1 396 ? 9.894   -4.489  22.726  1.00 57.56  ? 396 GLU A OE2 1 
ATOM   3055 N N   . VAL A 1 397 ? 12.560  1.177   21.173  1.00 44.96  ? 397 VAL A N   1 
ATOM   3056 C CA  . VAL A 1 397 ? 12.545  2.576   20.698  1.00 44.26  ? 397 VAL A CA  1 
ATOM   3057 C C   . VAL A 1 397 ? 13.428  2.818   19.456  1.00 43.67  ? 397 VAL A C   1 
ATOM   3058 O O   . VAL A 1 397 ? 13.540  3.947   18.982  1.00 44.96  ? 397 VAL A O   1 
ATOM   3059 C CB  . VAL A 1 397 ? 12.943  3.583   21.830  1.00 43.84  ? 397 VAL A CB  1 
ATOM   3060 C CG1 . VAL A 1 397 ? 12.049  3.370   23.062  1.00 43.86  ? 397 VAL A CG1 1 
ATOM   3061 C CG2 . VAL A 1 397 ? 14.410  3.453   22.197  1.00 43.21  ? 397 VAL A CG2 1 
ATOM   3062 N N   . ASN A 1 398 ? 14.040  1.762   18.931  1.00 43.07  ? 398 ASN A N   1 
ATOM   3063 C CA  . ASN A 1 398 ? 14.820  1.848   17.706  1.00 42.75  ? 398 ASN A CA  1 
ATOM   3064 C C   . ASN A 1 398 ? 14.533  0.683   16.765  1.00 42.90  ? 398 ASN A C   1 
ATOM   3065 O O   . ASN A 1 398 ? 14.343  -0.456  17.201  1.00 42.33  ? 398 ASN A O   1 
ATOM   3066 C CB  . ASN A 1 398 ? 16.310  1.843   18.017  1.00 42.08  ? 398 ASN A CB  1 
ATOM   3067 C CG  . ASN A 1 398 ? 16.750  3.090   18.717  1.00 43.68  ? 398 ASN A CG  1 
ATOM   3068 O OD1 . ASN A 1 398 ? 16.903  4.138   18.091  1.00 43.09  ? 398 ASN A OD1 1 
ATOM   3069 N ND2 . ASN A 1 398 ? 16.946  2.996   20.031  1.00 40.07  ? 398 ASN A ND2 1 
ATOM   3070 N N   . ALA A 1 399 ? 14.542  0.973   15.468  1.00 42.68  ? 399 ALA A N   1 
ATOM   3071 C CA  . ALA A 1 399 ? 14.472  -0.056  14.447  1.00 42.88  ? 399 ALA A CA  1 
ATOM   3072 C C   . ALA A 1 399 ? 15.090  0.536   13.190  1.00 43.09  ? 399 ALA A C   1 
ATOM   3073 O O   . ALA A 1 399 ? 14.752  1.641   12.793  1.00 43.34  ? 399 ALA A O   1 
ATOM   3074 C CB  . ALA A 1 399 ? 13.052  -0.480  14.196  1.00 42.44  ? 399 ALA A CB  1 
ATOM   3075 N N   . ASP A 1 400 ? 16.026  -0.186  12.599  1.00 43.30  ? 400 ASP A N   1 
ATOM   3076 C CA  . ASP A 1 400 ? 16.747  0.284   11.417  1.00 43.84  ? 400 ASP A CA  1 
ATOM   3077 C C   . ASP A 1 400 ? 16.355  -0.632  10.257  1.00 43.74  ? 400 ASP A C   1 
ATOM   3078 O O   . ASP A 1 400 ? 16.614  -1.839  10.291  1.00 42.79  ? 400 ASP A O   1 
ATOM   3079 C CB  . ASP A 1 400 ? 18.246  0.301   11.764  1.00 44.41  ? 400 ASP A CB  1 
ATOM   3080 C CG  . ASP A 1 400 ? 19.129  -0.136  10.650  1.00 46.49  ? 400 ASP A CG  1 
ATOM   3081 O OD1 . ASP A 1 400 ? 19.222  0.577   9.623   1.00 51.52  ? 400 ASP A OD1 1 
ATOM   3082 O OD2 . ASP A 1 400 ? 19.780  -1.198  10.811  1.00 49.10  ? 400 ASP A OD2 1 
ATOM   3083 N N   . VAL A 1 401 ? 15.695  -0.050  9.249   1.00 44.36  ? 401 VAL A N   1 
ATOM   3084 C CA  . VAL A 1 401 ? 15.144  -0.786  8.109   1.00 44.34  ? 401 VAL A CA  1 
ATOM   3085 C C   . VAL A 1 401 ? 15.643  -0.212  6.789   1.00 44.88  ? 401 VAL A C   1 
ATOM   3086 O O   . VAL A 1 401 ? 15.458  0.973   6.514   1.00 44.49  ? 401 VAL A O   1 
ATOM   3087 C CB  . VAL A 1 401 ? 13.601  -0.754  8.108   1.00 43.96  ? 401 VAL A CB  1 
ATOM   3088 C CG1 . VAL A 1 401 ? 13.058  -1.663  7.000   1.00 45.52  ? 401 VAL A CG1 1 
ATOM   3089 C CG2 . VAL A 1 401 ? 13.046  -1.162  9.501   1.00 44.89  ? 401 VAL A CG2 1 
ATOM   3090 N N   . VAL A 1 402 ? 16.242  -1.076  5.970   1.00 44.87  ? 402 VAL A N   1 
ATOM   3091 C CA  . VAL A 1 402 ? 16.929  -0.684  4.736   1.00 45.69  ? 402 VAL A CA  1 
ATOM   3092 C C   . VAL A 1 402 ? 16.470  -1.548  3.550   1.00 45.53  ? 402 VAL A C   1 
ATOM   3093 O O   . VAL A 1 402 ? 16.411  -2.767  3.671   1.00 44.53  ? 402 VAL A O   1 
ATOM   3094 C CB  . VAL A 1 402 ? 18.443  -0.872  4.931   1.00 45.73  ? 402 VAL A CB  1 
ATOM   3095 C CG1 . VAL A 1 402 ? 19.211  -0.574  3.660   1.00 46.11  ? 402 VAL A CG1 1 
ATOM   3096 C CG2 . VAL A 1 402 ? 18.924  -0.009  6.097   1.00 46.19  ? 402 VAL A CG2 1 
ATOM   3097 N N   . ASP A 1 403 ? 16.137  -0.904  2.425   1.00 46.65  ? 403 ASP A N   1 
ATOM   3098 C CA  . ASP A 1 403 ? 15.779  -1.590  1.166   1.00 47.40  ? 403 ASP A CA  1 
ATOM   3099 C C   . ASP A 1 403 ? 16.942  -1.678  0.200   1.00 48.21  ? 403 ASP A C   1 
ATOM   3100 O O   . ASP A 1 403 ? 17.687  -0.712  0.013   1.00 48.40  ? 403 ASP A O   1 
ATOM   3101 C CB  . ASP A 1 403 ? 14.689  -0.842  0.392   1.00 47.79  ? 403 ASP A CB  1 
ATOM   3102 C CG  . ASP A 1 403 ? 13.323  -0.983  1.004   1.00 49.64  ? 403 ASP A CG  1 
ATOM   3103 O OD1 . ASP A 1 403 ? 13.068  -1.955  1.742   1.00 50.86  ? 403 ASP A OD1 1 
ATOM   3104 O OD2 . ASP A 1 403 ? 12.485  -0.098  0.731   1.00 53.14  ? 403 ASP A OD2 1 
ATOM   3105 N N   . TRP A 1 404 ? 17.054  -2.827  -0.455  1.00 48.84  ? 404 TRP A N   1 
ATOM   3106 C CA  . TRP A 1 404 ? 17.877  -2.957  -1.633  1.00 49.64  ? 404 TRP A CA  1 
ATOM   3107 C C   . TRP A 1 404 ? 16.923  -3.318  -2.754  1.00 49.48  ? 404 TRP A C   1 
ATOM   3108 O O   . TRP A 1 404 ? 16.409  -4.427  -2.787  1.00 48.90  ? 404 TRP A O   1 
ATOM   3109 C CB  . TRP A 1 404 ? 18.942  -4.042  -1.445  1.00 50.54  ? 404 TRP A CB  1 
ATOM   3110 C CG  . TRP A 1 404 ? 19.815  -3.849  -0.205  1.00 51.48  ? 404 TRP A CG  1 
ATOM   3111 C CD1 . TRP A 1 404 ? 19.443  -4.020  1.104   1.00 52.13  ? 404 TRP A CD1 1 
ATOM   3112 C CD2 . TRP A 1 404 ? 21.198  -3.472  -0.180  1.00 51.82  ? 404 TRP A CD2 1 
ATOM   3113 N NE1 . TRP A 1 404 ? 20.506  -3.756  1.941   1.00 52.47  ? 404 TRP A NE1 1 
ATOM   3114 C CE2 . TRP A 1 404 ? 21.596  -3.425  1.175   1.00 52.35  ? 404 TRP A CE2 1 
ATOM   3115 C CE3 . TRP A 1 404 ? 22.140  -3.171  -1.174  1.00 52.35  ? 404 TRP A CE3 1 
ATOM   3116 C CZ2 . TRP A 1 404 ? 22.897  -3.082  1.562   1.00 52.17  ? 404 TRP A CZ2 1 
ATOM   3117 C CZ3 . TRP A 1 404 ? 23.433  -2.830  -0.787  1.00 52.07  ? 404 TRP A CZ3 1 
ATOM   3118 C CH2 . TRP A 1 404 ? 23.797  -2.790  0.567   1.00 51.81  ? 404 TRP A CH2 1 
ATOM   3119 N N   . ILE A 1 405 ? 16.640  -2.352  -3.630  1.00 49.96  ? 405 ILE A N   1 
ATOM   3120 C CA  . ILE A 1 405 ? 15.899  -2.610  -4.889  1.00 50.41  ? 405 ILE A CA  1 
ATOM   3121 C C   . ILE A 1 405 ? 16.854  -2.621  -6.084  1.00 50.33  ? 405 ILE A C   1 
ATOM   3122 O O   . ILE A 1 405 ? 16.676  -3.404  -7.017  1.00 50.54  ? 405 ILE A O   1 
ATOM   3123 C CB  . ILE A 1 405 ? 14.743  -1.598  -5.110  1.00 50.65  ? 405 ILE A CB  1 
ATOM   3124 C CG1 . ILE A 1 405 ? 15.284  -0.189  -5.426  1.00 51.29  ? 405 ILE A CG1 1 
ATOM   3125 C CG2 . ILE A 1 405 ? 13.817  -1.568  -3.869  1.00 50.78  ? 405 ILE A CG2 1 
ATOM   3126 C CD1 . ILE A 1 405 ? 14.313  0.954   -5.042  1.00 51.27  ? 405 ILE A CD1 1 
ATOM   3127 N N   . GLN A 1 406 ? 17.866  -1.752  -6.041  1.00 50.53  ? 406 GLN A N   1 
ATOM   3128 C CA  . GLN A 1 406 ? 19.047  -1.835  -6.918  1.00 50.83  ? 406 GLN A CA  1 
ATOM   3129 C C   . GLN A 1 406 ? 18.732  -1.973  -8.407  1.00 50.65  ? 406 GLN A C   1 
ATOM   3130 O O   . GLN A 1 406 ? 19.584  -2.398  -9.187  1.00 50.82  ? 406 GLN A O   1 
ATOM   3131 C CB  . GLN A 1 406 ? 19.953  -2.995  -6.455  1.00 51.12  ? 406 GLN A CB  1 
ATOM   3132 C CG  . GLN A 1 406 ? 21.447  -2.699  -6.534  1.00 51.23  ? 406 GLN A CG  1 
ATOM   3133 C CD  . GLN A 1 406 ? 21.928  -1.829  -5.383  1.00 51.99  ? 406 GLN A CD  1 
ATOM   3134 O OE1 . GLN A 1 406 ? 23.029  -2.023  -4.870  1.00 53.87  ? 406 GLN A OE1 1 
ATOM   3135 N NE2 . GLN A 1 406 ? 21.102  -0.872  -4.968  1.00 50.50  ? 406 GLN A NE2 1 
ATOM   3136 N N   . LYS A 1 414 ? 20.520  -0.028  -1.869  1.00 59.75  ? 414 LYS A N   1 
ATOM   3137 C CA  . LYS A 1 414 ? 20.713  0.714   -0.617  1.00 59.74  ? 414 LYS A CA  1 
ATOM   3138 C C   . LYS A 1 414 ? 19.714  1.875   -0.468  1.00 59.44  ? 414 LYS A C   1 
ATOM   3139 O O   . LYS A 1 414 ? 19.775  2.847   -1.219  1.00 59.88  ? 414 LYS A O   1 
ATOM   3140 C CB  . LYS A 1 414 ? 22.148  1.254   -0.550  1.00 59.91  ? 414 LYS A CB  1 
ATOM   3141 C CG  . LYS A 1 414 ? 22.687  1.789   -1.891  1.00 60.52  ? 414 LYS A CG  1 
ATOM   3142 C CD  . LYS A 1 414 ? 23.680  2.949   -1.721  1.00 60.56  ? 414 LYS A CD  1 
ATOM   3143 C CE  . LYS A 1 414 ? 23.015  4.205   -1.140  1.00 61.02  ? 414 LYS A CE  1 
ATOM   3144 N NZ  . LYS A 1 414 ? 23.577  5.474   -1.695  1.00 60.85  ? 414 LYS A NZ  1 
ATOM   3145 N N   . SER A 1 415 ? 18.793  1.771   0.488   1.00 58.93  ? 415 SER A N   1 
ATOM   3146 C CA  . SER A 1 415 ? 17.785  2.817   0.699   1.00 58.48  ? 415 SER A CA  1 
ATOM   3147 C C   . SER A 1 415 ? 17.022  2.644   2.011   1.00 58.09  ? 415 SER A C   1 
ATOM   3148 O O   . SER A 1 415 ? 16.527  1.563   2.306   1.00 57.76  ? 415 SER A O   1 
ATOM   3149 C CB  . SER A 1 415 ? 16.793  2.841   -0.469  1.00 58.30  ? 415 SER A CB  1 
ATOM   3150 O OG  . SER A 1 415 ? 15.556  3.423   -0.086  1.00 57.90  ? 415 SER A OG  1 
ATOM   3151 N N   . ILE A 1 416 ? 16.910  3.731   2.775   1.00 57.85  ? 416 ILE A N   1 
ATOM   3152 C CA  . ILE A 1 416 ? 16.184  3.735   4.053   1.00 57.49  ? 416 ILE A CA  1 
ATOM   3153 C C   . ILE A 1 416 ? 14.677  3.573   3.843   1.00 57.07  ? 416 ILE A C   1 
ATOM   3154 O O   . ILE A 1 416 ? 14.069  4.331   3.098   1.00 57.29  ? 416 ILE A O   1 
ATOM   3155 C CB  . ILE A 1 416 ? 16.426  5.045   4.850   1.00 57.54  ? 416 ILE A CB  1 
ATOM   3156 C CG1 . ILE A 1 416 ? 17.815  5.036   5.508   1.00 57.68  ? 416 ILE A CG1 1 
ATOM   3157 C CG2 . ILE A 1 416 ? 15.352  5.221   5.926   1.00 58.01  ? 416 ILE A CG2 1 
ATOM   3158 C CD1 . ILE A 1 416 ? 18.986  5.016   4.523   1.00 57.98  ? 416 ILE A CD1 1 
ATOM   3159 N N   . ASN A 1 417 ? 14.080  2.598   4.521   1.00 56.51  ? 417 ASN A N   1 
ATOM   3160 C CA  . ASN A 1 417 ? 12.673  2.246   4.334   1.00 56.55  ? 417 ASN A CA  1 
ATOM   3161 C C   . ASN A 1 417 ? 11.853  2.725   5.524   1.00 56.41  ? 417 ASN A C   1 
ATOM   3162 O O   . ASN A 1 417 ? 12.086  2.286   6.650   1.00 56.30  ? 417 ASN A O   1 
ATOM   3163 C CB  . ASN A 1 417 ? 12.563  0.723   4.167   1.00 56.39  ? 417 ASN A CB  1 
ATOM   3164 C CG  . ASN A 1 417 ? 11.155  0.252   3.852   1.00 56.15  ? 417 ASN A CG  1 
ATOM   3165 O OD1 . ASN A 1 417 ? 10.311  0.149   4.733   1.00 55.16  ? 417 ASN A OD1 1 
ATOM   3166 N ND2 . ASN A 1 417 ? 10.910  -0.071  2.591   1.00 56.22  ? 417 ASN A ND2 1 
ATOM   3167 N N   . ARG A 1 418 ? 10.908  3.635   5.299   1.00 56.40  ? 418 ARG A N   1 
ATOM   3168 C CA  . ARG A 1 418 ? 10.102  4.155   6.416   1.00 56.59  ? 418 ARG A CA  1 
ATOM   3169 C C   . ARG A 1 418 ? 8.682   3.576   6.431   1.00 56.17  ? 418 ARG A C   1 
ATOM   3170 O O   . ARG A 1 418 ? 7.743   4.223   6.878   1.00 56.41  ? 418 ARG A O   1 
ATOM   3171 C CB  . ARG A 1 418 ? 10.132  5.698   6.469   1.00 57.05  ? 418 ARG A CB  1 
ATOM   3172 C CG  . ARG A 1 418 ? 9.148   6.456   5.560   1.00 59.54  ? 418 ARG A CG  1 
ATOM   3173 C CD  . ARG A 1 418 ? 8.041   7.196   6.338   1.00 61.65  ? 418 ARG A CD  1 
ATOM   3174 N NE  . ARG A 1 418 ? 8.574   8.149   7.318   1.00 63.30  ? 418 ARG A NE  1 
ATOM   3175 C CZ  . ARG A 1 418 ? 7.846   9.059   7.974   1.00 63.46  ? 418 ARG A CZ  1 
ATOM   3176 N NH1 . ARG A 1 418 ? 6.536   9.179   7.765   1.00 64.72  ? 418 ARG A NH1 1 
ATOM   3177 N NH2 . ARG A 1 418 ? 8.437   9.872   8.842   1.00 64.40  ? 418 ARG A NH2 1 
ATOM   3178 N N   . SER A 1 419 ? 8.543   2.332   5.963   1.00 55.43  ? 419 SER A N   1 
ATOM   3179 C CA  . SER A 1 419 ? 7.324   1.549   6.218   1.00 55.05  ? 419 SER A CA  1 
ATOM   3180 C C   . SER A 1 419 ? 7.074   1.330   7.726   1.00 54.15  ? 419 SER A C   1 
ATOM   3181 O O   . SER A 1 419 ? 5.941   1.079   8.138   1.00 53.60  ? 419 SER A O   1 
ATOM   3182 C CB  . SER A 1 419 ? 7.384   0.177   5.542   1.00 54.69  ? 419 SER A CB  1 
ATOM   3183 O OG  . SER A 1 419 ? 7.105   0.282   4.163   1.00 56.39  ? 419 SER A OG  1 
ATOM   3184 N N   . LEU A 1 420 ? 8.135   1.375   8.525   1.00 53.62  ? 420 LEU A N   1 
ATOM   3185 C CA  . LEU A 1 420 ? 8.014   1.205   9.970   1.00 53.11  ? 420 LEU A CA  1 
ATOM   3186 C C   . LEU A 1 420 ? 8.825   2.281   10.665  1.00 52.38  ? 420 LEU A C   1 
ATOM   3187 O O   . LEU A 1 420 ? 10.021  2.406   10.416  1.00 52.19  ? 420 LEU A O   1 
ATOM   3188 C CB  . LEU A 1 420 ? 8.496   -0.196  10.370  1.00 53.46  ? 420 LEU A CB  1 
ATOM   3189 C CG  . LEU A 1 420 ? 8.677   -0.586  11.844  1.00 54.43  ? 420 LEU A CG  1 
ATOM   3190 C CD1 . LEU A 1 420 ? 10.117  -0.343  12.319  1.00 56.37  ? 420 LEU A CD1 1 
ATOM   3191 C CD2 . LEU A 1 420 ? 7.672   0.124   12.764  1.00 54.17  ? 420 LEU A CD2 1 
ATOM   3192 N N   . ILE A 1 421 ? 8.159   3.075   11.506  1.00 51.56  ? 421 ILE A N   1 
ATOM   3193 C CA  . ILE A 1 421 ? 8.837   4.048   12.367  1.00 50.99  ? 421 ILE A CA  1 
ATOM   3194 C C   . ILE A 1 421 ? 8.562   3.689   13.824  1.00 50.28  ? 421 ILE A C   1 
ATOM   3195 O O   . ILE A 1 421 ? 7.414   3.666   14.270  1.00 49.57  ? 421 ILE A O   1 
ATOM   3196 C CB  . ILE A 1 421 ? 8.388   5.493   12.116  1.00 51.04  ? 421 ILE A CB  1 
ATOM   3197 C CG1 . ILE A 1 421 ? 8.463   5.811   10.627  1.00 50.51  ? 421 ILE A CG1 1 
ATOM   3198 C CG2 . ILE A 1 421 ? 9.224   6.485   12.946  1.00 50.80  ? 421 ILE A CG2 1 
ATOM   3199 C CD1 . ILE A 1 421 ? 7.238   5.409   9.940   1.00 51.11  ? 421 ILE A CD1 1 
ATOM   3200 N N   . VAL A 1 422 ? 9.627   3.386   14.545  1.00 49.81  ? 422 VAL A N   1 
ATOM   3201 C CA  . VAL A 1 422 ? 9.523   3.019   15.944  1.00 49.31  ? 422 VAL A CA  1 
ATOM   3202 C C   . VAL A 1 422 ? 10.142  4.134   16.780  1.00 48.84  ? 422 VAL A C   1 
ATOM   3203 O O   . VAL A 1 422 ? 11.132  4.751   16.363  1.00 48.43  ? 422 VAL A O   1 
ATOM   3204 C CB  . VAL A 1 422 ? 10.228  1.686   16.225  1.00 49.82  ? 422 VAL A CB  1 
ATOM   3205 C CG1 . VAL A 1 422 ? 9.660   0.594   15.361  1.00 48.27  ? 422 VAL A CG1 1 
ATOM   3206 C CG2 . VAL A 1 422 ? 11.687  1.807   15.981  1.00 50.41  ? 422 VAL A CG2 1 
ATOM   3207 N N   . GLY A 1 423 ? 9.544   4.394   17.946  1.00 48.40  ? 423 GLY A N   1 
ATOM   3208 C CA  . GLY A 1 423 ? 10.072  5.359   18.892  1.00 47.78  ? 423 GLY A CA  1 
ATOM   3209 C C   . GLY A 1 423 ? 9.492   6.744   18.696  1.00 47.44  ? 423 GLY A C   1 
ATOM   3210 O O   . GLY A 1 423 ? 10.232  7.706   18.551  1.00 49.05  ? 423 GLY A O   1 
ATOM   3211 N N   . LEU A 1 424 ? 8.167   6.848   18.718  1.00 46.12  ? 424 LEU A N   1 
ATOM   3212 C CA  . LEU A 1 424 ? 7.473   8.133   18.577  1.00 44.93  ? 424 LEU A CA  1 
ATOM   3213 C C   . LEU A 1 424 ? 6.707   8.536   19.843  1.00 43.60  ? 424 LEU A C   1 
ATOM   3214 O O   . LEU A 1 424 ? 6.083   7.689   20.479  1.00 42.56  ? 424 LEU A O   1 
ATOM   3215 C CB  . LEU A 1 424 ? 6.434   8.027   17.466  1.00 44.90  ? 424 LEU A CB  1 
ATOM   3216 C CG  . LEU A 1 424 ? 6.916   7.754   16.051  1.00 44.83  ? 424 LEU A CG  1 
ATOM   3217 C CD1 . LEU A 1 424 ? 5.707   7.497   15.149  1.00 45.00  ? 424 LEU A CD1 1 
ATOM   3218 C CD2 . LEU A 1 424 ? 7.727   8.943   15.556  1.00 43.82  ? 424 LEU A CD2 1 
ATOM   3219 N N   . LYS A 1 425 ? 6.715   9.834   20.154  1.00 42.12  ? 425 LYS A N   1 
ATOM   3220 C CA  . LYS A 1 425 ? 5.773   10.419  21.087  1.00 42.36  ? 425 LYS A CA  1 
ATOM   3221 C C   . LYS A 1 425 ? 5.778   9.610   22.404  1.00 42.02  ? 425 LYS A C   1 
ATOM   3222 O O   . LYS A 1 425 ? 4.719   9.225   22.941  1.00 42.13  ? 425 LYS A O   1 
ATOM   3223 C CB  . LYS A 1 425 ? 4.372   10.495  20.457  1.00 42.56  ? 425 LYS A CB  1 
ATOM   3224 C CG  . LYS A 1 425 ? 4.319   11.399  19.213  1.00 43.42  ? 425 LYS A CG  1 
ATOM   3225 C CD  . LYS A 1 425 ? 3.308   12.489  19.342  1.00 44.04  ? 425 LYS A CD  1 
ATOM   3226 C CE  . LYS A 1 425 ? 3.340   13.446  18.134  1.00 45.75  ? 425 LYS A CE  1 
ATOM   3227 N NZ  . LYS A 1 425 ? 1.826   13.777  17.795  0.00 50.00  ? 425 LYS A NZ  1 
ATOM   3228 N N   . ILE A 1 426 ? 6.991   9.360   22.894  1.00 40.55  ? 426 ILE A N   1 
ATOM   3229 C CA  . ILE A 1 426 ? 7.188   8.679   24.158  1.00 40.77  ? 426 ILE A CA  1 
ATOM   3230 C C   . ILE A 1 426 ? 6.669   9.604   25.259  1.00 41.04  ? 426 ILE A C   1 
ATOM   3231 O O   . ILE A 1 426 ? 7.068   10.792  25.333  1.00 40.38  ? 426 ILE A O   1 
ATOM   3232 C CB  . ILE A 1 426 ? 8.647   8.235   24.387  1.00 40.51  ? 426 ILE A CB  1 
ATOM   3233 C CG1 . ILE A 1 426 ? 9.198   7.502   23.160  1.00 40.79  ? 426 ILE A CG1 1 
ATOM   3234 C CG2 . ILE A 1 426 ? 8.759   7.257   25.621  1.00 40.35  ? 426 ILE A CG2 1 
ATOM   3235 C CD1 . ILE A 1 426 ? 10.604  6.969   23.369  1.00 39.71  ? 426 ILE A CD1 1 
ATOM   3236 N N   . SER A 1 427 ? 5.750   9.057   26.078  1.00 40.86  ? 427 SER A N   1 
ATOM   3237 C CA  . SER A 1 427 ? 4.833   9.860   26.861  1.00 40.96  ? 427 SER A CA  1 
ATOM   3238 C C   . SER A 1 427 ? 4.712   9.342   28.283  1.00 41.21  ? 427 SER A C   1 
ATOM   3239 O O   . SER A 1 427 ? 4.750   8.146   28.517  1.00 39.31  ? 427 SER A O   1 
ATOM   3240 C CB  . SER A 1 427 ? 3.430   9.868   26.237  1.00 40.70  ? 427 SER A CB  1 
ATOM   3241 O OG  . SER A 1 427 ? 3.435   10.347  24.902  1.00 40.64  ? 427 SER A OG  1 
ATOM   3242 N N   . THR A 1 428 ? 4.552   10.284  29.214  1.00 42.39  ? 428 THR A N   1 
ATOM   3243 C CA  . THR A 1 428 ? 4.290   9.987   30.631  1.00 41.77  ? 428 THR A CA  1 
ATOM   3244 C C   . THR A 1 428 ? 3.514   11.167  31.244  1.00 42.50  ? 428 THR A C   1 
ATOM   3245 O O   . THR A 1 428 ? 3.523   12.280  30.717  1.00 40.84  ? 428 THR A O   1 
ATOM   3246 C CB  . THR A 1 428 ? 5.622   9.653   31.400  1.00 43.17  ? 428 THR A CB  1 
ATOM   3247 O OG1 . THR A 1 428 ? 5.347   8.904   32.606  1.00 43.93  ? 428 THR A OG1 1 
ATOM   3248 C CG2 . THR A 1 428 ? 6.432   10.900  31.722  1.00 42.67  ? 428 THR A CG2 1 
ATOM   3249 N N   . LYS A 1 429 ? 2.793   10.916  32.332  1.00 42.71  ? 429 LYS A N   1 
ATOM   3250 C CA  . LYS A 1 429 ? 2.028   11.980  32.984  1.00 42.81  ? 429 LYS A CA  1 
ATOM   3251 C C   . LYS A 1 429 ? 2.985   13.052  33.485  1.00 42.74  ? 429 LYS A C   1 
ATOM   3252 O O   . LYS A 1 429 ? 4.055   12.752  34.019  1.00 43.11  ? 429 LYS A O   1 
ATOM   3253 C CB  . LYS A 1 429 ? 1.175   11.419  34.143  1.00 43.32  ? 429 LYS A CB  1 
ATOM   3254 C CG  . LYS A 1 429 ? 0.282   12.461  34.823  1.00 43.37  ? 429 LYS A CG  1 
ATOM   3255 C CD  . LYS A 1 429 ? -0.562  11.888  35.972  1.00 43.06  ? 429 LYS A CD  1 
ATOM   3256 C CE  . LYS A 1 429 ? -1.125  13.014  36.834  1.00 44.65  ? 429 LYS A CE  1 
ATOM   3257 N NZ  . LYS A 1 429 ? -0.032  13.915  37.321  1.00 47.38  ? 429 LYS A NZ  1 
ATOM   3258 N N   . SER A 1 430 ? 2.595   14.306  33.290  1.00 43.06  ? 430 SER A N   1 
ATOM   3259 C CA  . SER A 1 430 ? 3.310   15.440  33.844  1.00 43.93  ? 430 SER A CA  1 
ATOM   3260 C C   . SER A 1 430 ? 3.229   15.487  35.379  1.00 44.30  ? 430 SER A C   1 
ATOM   3261 O O   . SER A 1 430 ? 2.224   15.110  35.969  1.00 45.26  ? 430 SER A O   1 
ATOM   3262 C CB  . SER A 1 430 ? 2.708   16.743  33.340  1.00 43.30  ? 430 SER A CB  1 
ATOM   3263 O OG  . SER A 1 430 ? 2.905   16.884  31.955  1.00 46.04  ? 430 SER A OG  1 
ATOM   3264 N N   . VAL A 1 431 ? 4.258   16.058  35.987  1.00 45.10  ? 431 VAL A N   1 
ATOM   3265 C CA  . VAL A 1 431 ? 4.338   16.223  37.443  1.00 45.33  ? 431 VAL A CA  1 
ATOM   3266 C C   . VAL A 1 431 ? 3.329   17.216  37.981  1.00 45.33  ? 431 VAL A C   1 
ATOM   3267 O O   . VAL A 1 431 ? 3.354   18.399  37.637  1.00 46.01  ? 431 VAL A O   1 
ATOM   3268 C CB  . VAL A 1 431 ? 5.761   16.661  37.847  1.00 46.48  ? 431 VAL A CB  1 
ATOM   3269 C CG1 . VAL A 1 431 ? 5.858   16.936  39.343  1.00 46.64  ? 431 VAL A CG1 1 
ATOM   3270 C CG2 . VAL A 1 431 ? 6.762   15.606  37.426  1.00 43.86  ? 431 VAL A CG2 1 
ATOM   3271 N N   . GLY A 1 432 ? 2.426   16.722  38.825  1.00 45.33  ? 432 GLY A N   1 
ATOM   3272 C CA  . GLY A 1 432 ? 1.459   17.552  39.512  1.00 45.86  ? 432 GLY A CA  1 
ATOM   3273 C C   . GLY A 1 432 ? 0.344   18.077  38.640  1.00 46.22  ? 432 GLY A C   1 
ATOM   3274 O O   . GLY A 1 432 ? -0.407  18.914  39.064  1.00 45.63  ? 432 GLY A O   1 
ATOM   3275 N N   . ARG A 1 433 ? 0.254   17.568  37.416  1.00 46.79  ? 433 ARG A N   1 
ATOM   3276 C CA  . ARG A 1 433 ? -0.738  18.045  36.459  1.00 46.98  ? 433 ARG A CA  1 
ATOM   3277 C C   . ARG A 1 433 ? -1.338  16.889  35.666  1.00 46.25  ? 433 ARG A C   1 
ATOM   3278 O O   . ARG A 1 433 ? -0.677  15.879  35.426  1.00 46.19  ? 433 ARG A O   1 
ATOM   3279 C CB  . ARG A 1 433 ? -0.116  19.069  35.507  1.00 47.30  ? 433 ARG A CB  1 
ATOM   3280 C CG  . ARG A 1 433 ? 0.433   20.306  36.199  1.00 49.45  ? 433 ARG A CG  1 
ATOM   3281 C CD  . ARG A 1 433 ? 1.326   21.109  35.268  1.00 50.55  ? 433 ARG A CD  1 
ATOM   3282 N NE  . ARG A 1 433 ? 0.741   21.252  33.938  1.00 55.80  ? 433 ARG A NE  1 
ATOM   3283 C CZ  . ARG A 1 433 ? 1.392   21.008  32.805  0.00 50.00  ? 433 ARG A CZ  1 
ATOM   3284 N NH1 . ARG A 1 433 ? 2.656   20.607  32.837  0.00 50.00  ? 433 ARG A NH1 1 
ATOM   3285 N NH2 . ARG A 1 433 ? 0.780   21.165  31.639  0.00 50.00  ? 433 ARG A NH2 1 
ATOM   3286 N N   . ASP A 1 434 ? -2.595  17.045  35.263  1.00 46.19  ? 434 ASP A N   1 
ATOM   3287 C CA  . ASP A 1 434 ? -3.241  16.081  34.384  1.00 46.00  ? 434 ASP A CA  1 
ATOM   3288 C C   . ASP A 1 434 ? -2.904  16.438  32.944  1.00 45.59  ? 434 ASP A C   1 
ATOM   3289 O O   . ASP A 1 434 ? -3.774  16.826  32.181  1.00 45.40  ? 434 ASP A O   1 
ATOM   3290 C CB  . ASP A 1 434 ? -4.761  16.108  34.578  1.00 46.05  ? 434 ASP A CB  1 
ATOM   3291 C CG  . ASP A 1 434 ? -5.185  15.664  35.966  1.00 45.65  ? 434 ASP A CG  1 
ATOM   3292 O OD1 . ASP A 1 434 ? -6.346  15.909  36.332  1.00 47.26  ? 434 ASP A OD1 1 
ATOM   3293 O OD2 . ASP A 1 434 ? -4.366  15.066  36.679  1.00 46.45  ? 434 ASP A OD2 1 
ATOM   3294 N N   . GLU A 1 435 ? -1.631  16.329  32.593  1.00 45.34  ? 435 GLU A N   1 
ATOM   3295 C CA  . GLU A 1 435 ? -1.165  16.658  31.253  1.00 45.25  ? 435 GLU A CA  1 
ATOM   3296 C C   . GLU A 1 435 ? -0.108  15.620  30.886  1.00 44.76  ? 435 GLU A C   1 
ATOM   3297 O O   . GLU A 1 435 ? 0.364   14.911  31.762  1.00 45.14  ? 435 GLU A O   1 
ATOM   3298 C CB  . GLU A 1 435 ? -0.591  18.071  31.204  1.00 45.55  ? 435 GLU A CB  1 
ATOM   3299 C CG  . GLU A 1 435 ? -1.603  19.205  31.462  1.00 48.70  ? 435 GLU A CG  1 
ATOM   3300 C CD  . GLU A 1 435 ? -2.508  19.487  30.275  1.00 53.87  ? 435 GLU A CD  1 
ATOM   3301 O OE1 . GLU A 1 435 ? -2.221  18.994  29.159  1.00 56.51  ? 435 GLU A OE1 1 
ATOM   3302 O OE2 . GLU A 1 435 ? -3.513  20.230  30.432  1.00 59.08  ? 435 GLU A OE2 1 
ATOM   3303 N N   . ARG A 1 436 ? 0.201   15.506  29.593  1.00 43.79  ? 436 ARG A N   1 
ATOM   3304 C CA  . ARG A 1 436 ? 1.134   14.494  29.044  1.00 43.88  ? 436 ARG A CA  1 
ATOM   3305 C C   . ARG A 1 436 ? 2.468   15.189  28.863  1.00 42.57  ? 436 ARG A C   1 
ATOM   3306 O O   . ARG A 1 436 ? 2.512   16.308  28.401  1.00 42.98  ? 436 ARG A O   1 
ATOM   3307 C CB  . ARG A 1 436 ? 0.590   13.994  27.678  1.00 43.58  ? 436 ARG A CB  1 
ATOM   3308 C CG  . ARG A 1 436 ? 1.431   12.949  26.868  1.00 44.02  ? 436 ARG A CG  1 
ATOM   3309 C CD  . ARG A 1 436 ? 0.990   12.882  25.342  1.00 46.44  ? 436 ARG A CD  1 
ATOM   3310 N NE  . ARG A 1 436 ? 2.039   13.292  24.360  1.00 47.83  ? 436 ARG A NE  1 
ATOM   3311 C CZ  . ARG A 1 436 ? 1.928   14.263  23.450  1.00 50.91  ? 436 ARG A CZ  1 
ATOM   3312 N NH1 . ARG A 1 436 ? 0.807   14.973  23.315  1.00 52.17  ? 436 ARG A NH1 1 
ATOM   3313 N NH2 . ARG A 1 436 ? 2.951   14.527  22.621  1.00 53.58  ? 436 ARG A NH2 1 
ATOM   3314 N N   . GLU A 1 437 ? 3.539   14.546  29.270  1.00 42.83  ? 437 GLU A N   1 
ATOM   3315 C CA  . GLU A 1 437 ? 4.882   15.045  29.044  1.00 43.28  ? 437 GLU A CA  1 
ATOM   3316 C C   . GLU A 1 437 ? 5.512   14.164  27.985  1.00 42.00  ? 437 GLU A C   1 
ATOM   3317 O O   . GLU A 1 437 ? 5.516   12.966  28.124  1.00 42.11  ? 437 GLU A O   1 
ATOM   3318 C CB  . GLU A 1 437 ? 5.739   14.950  30.313  1.00 41.98  ? 437 GLU A CB  1 
ATOM   3319 C CG  . GLU A 1 437 ? 7.192   15.383  30.061  1.00 43.11  ? 437 GLU A CG  1 
ATOM   3320 C CD  . GLU A 1 437 ? 8.083   15.351  31.292  1.00 46.08  ? 437 GLU A CD  1 
ATOM   3321 O OE1 . GLU A 1 437 ? 7.582   15.056  32.413  1.00 49.10  ? 437 GLU A OE1 1 
ATOM   3322 O OE2 . GLU A 1 437 ? 9.295   15.614  31.129  1.00 48.15  ? 437 GLU A OE2 1 
ATOM   3323 N N   . ASP A 1 438 ? 6.064   14.770  26.948  1.00 42.94  ? 438 ASP A N   1 
ATOM   3324 C CA  . ASP A 1 438 ? 6.771   14.016  25.919  1.00 42.01  ? 438 ASP A CA  1 
ATOM   3325 C C   . ASP A 1 438 ? 8.227   13.866  26.340  1.00 40.91  ? 438 ASP A C   1 
ATOM   3326 O O   . ASP A 1 438 ? 8.958   14.862  26.498  1.00 40.45  ? 438 ASP A O   1 
ATOM   3327 C CB  . ASP A 1 438 ? 6.654   14.752  24.571  1.00 42.82  ? 438 ASP A CB  1 
ATOM   3328 C CG  . ASP A 1 438 ? 7.077   13.892  23.388  1.00 43.89  ? 438 ASP A CG  1 
ATOM   3329 O OD1 . ASP A 1 438 ? 8.256   13.482  23.332  1.00 46.28  ? 438 ASP A OD1 1 
ATOM   3330 O OD2 . ASP A 1 438 ? 6.206   13.620  22.522  1.00 45.41  ? 438 ASP A OD2 1 
ATOM   3331 N N   . ILE A 1 439 ? 8.655   12.624  26.505  1.00 40.13  ? 439 ILE A N   1 
ATOM   3332 C CA  . ILE A 1 439 ? 10.017  12.332  26.926  1.00 40.42  ? 439 ILE A CA  1 
ATOM   3333 C C   . ILE A 1 439 ? 10.805  11.628  25.814  1.00 40.16  ? 439 ILE A C   1 
ATOM   3334 O O   . ILE A 1 439 ? 11.778  10.926  26.070  1.00 42.05  ? 439 ILE A O   1 
ATOM   3335 C CB  . ILE A 1 439 ? 10.032  11.491  28.260  1.00 41.04  ? 439 ILE A CB  1 
ATOM   3336 C CG1 . ILE A 1 439 ? 9.166   10.235  28.144  1.00 39.91  ? 439 ILE A CG1 1 
ATOM   3337 C CG2 . ILE A 1 439 ? 9.487   12.318  29.381  1.00 40.10  ? 439 ILE A CG2 1 
ATOM   3338 C CD1 . ILE A 1 439 ? 9.329   9.269   29.269  1.00 39.16  ? 439 ILE A CD1 1 
ATOM   3339 N N   . THR A 1 440 ? 10.414  11.821  24.564  1.00 40.36  ? 440 THR A N   1 
ATOM   3340 C CA  . THR A 1 440 ? 11.073  11.101  23.469  1.00 40.14  ? 440 THR A CA  1 
ATOM   3341 C C   . THR A 1 440 ? 12.548  11.444  23.458  1.00 39.80  ? 440 THR A C   1 
ATOM   3342 O O   . THR A 1 440 ? 13.414  10.598  23.190  1.00 39.60  ? 440 THR A O   1 
ATOM   3343 C CB  . THR A 1 440 ? 10.458  11.473  22.104  1.00 40.11  ? 440 THR A CB  1 
ATOM   3344 O OG1 . THR A 1 440 ? 9.039   11.337  22.157  1.00 40.36  ? 440 THR A OG1 1 
ATOM   3345 C CG2 . THR A 1 440 ? 11.006  10.563  21.001  1.00 42.08  ? 440 THR A CG2 1 
ATOM   3346 N N   . HIS A 1 441 ? 12.819  12.711  23.740  1.00 39.27  ? 441 HIS A N   1 
ATOM   3347 C CA  . HIS A 1 441 ? 14.176  13.225  23.777  1.00 40.16  ? 441 HIS A CA  1 
ATOM   3348 C C   . HIS A 1 441 ? 15.097  12.508  24.754  1.00 40.60  ? 441 HIS A C   1 
ATOM   3349 O O   . HIS A 1 441 ? 16.307  12.491  24.545  1.00 41.98  ? 441 HIS A O   1 
ATOM   3350 C CB  . HIS A 1 441 ? 14.138  14.722  24.086  1.00 40.12  ? 441 HIS A CB  1 
ATOM   3351 C CG  . HIS A 1 441 ? 13.710  15.037  25.477  1.00 40.24  ? 441 HIS A CG  1 
ATOM   3352 N ND1 . HIS A 1 441 ? 14.600  15.066  26.527  1.00 43.31  ? 441 HIS A ND1 1 
ATOM   3353 C CD2 . HIS A 1 441 ? 12.489  15.300  26.006  1.00 41.36  ? 441 HIS A CD2 1 
ATOM   3354 C CE1 . HIS A 1 441 ? 13.951  15.362  27.639  1.00 42.80  ? 441 HIS A CE1 1 
ATOM   3355 N NE2 . HIS A 1 441 ? 12.669  15.491  27.359  1.00 41.28  ? 441 HIS A NE2 1 
ATOM   3356 N N   . THR A 1 442 ? 14.526  11.881  25.791  1.00 41.05  ? 442 THR A N   1 
ATOM   3357 C CA  . THR A 1 442 ? 15.301  11.146  26.786  1.00 40.83  ? 442 THR A CA  1 
ATOM   3358 C C   . THR A 1 442 ? 15.805  9.807   26.252  1.00 41.60  ? 442 THR A C   1 
ATOM   3359 O O   . THR A 1 442 ? 16.853  9.290   26.699  1.00 40.77  ? 442 THR A O   1 
ATOM   3360 C CB  . THR A 1 442 ? 14.485  10.921  28.127  1.00 41.29  ? 442 THR A CB  1 
ATOM   3361 O OG1 . THR A 1 442 ? 13.425  9.950   27.953  1.00 40.03  ? 442 THR A OG1 1 
ATOM   3362 C CG2 . THR A 1 442 ? 13.929  12.219  28.641  1.00 40.65  ? 442 THR A CG2 1 
ATOM   3363 N N   . TYR A 1 443 ? 15.076  9.247   25.287  1.00 40.94  ? 443 TYR A N   1 
ATOM   3364 C CA  . TYR A 1 443 ? 15.462  7.971   24.680  1.00 41.05  ? 443 TYR A CA  1 
ATOM   3365 C C   . TYR A 1 443 ? 16.230  8.075   23.351  1.00 41.43  ? 443 TYR A C   1 
ATOM   3366 O O   . TYR A 1 443 ? 16.965  7.161   22.987  1.00 40.81  ? 443 TYR A O   1 
ATOM   3367 C CB  . TYR A 1 443 ? 14.216  7.136   24.439  1.00 41.67  ? 443 TYR A CB  1 
ATOM   3368 C CG  . TYR A 1 443 ? 13.747  6.475   25.685  1.00 40.84  ? 443 TYR A CG  1 
ATOM   3369 C CD1 . TYR A 1 443 ? 12.840  7.107   26.508  1.00 41.80  ? 443 TYR A CD1 1 
ATOM   3370 C CD2 . TYR A 1 443 ? 14.226  5.215   26.052  1.00 40.73  ? 443 TYR A CD2 1 
ATOM   3371 C CE1 . TYR A 1 443 ? 12.410  6.512   27.700  1.00 42.21  ? 443 TYR A CE1 1 
ATOM   3372 C CE2 . TYR A 1 443 ? 13.813  4.610   27.215  1.00 42.28  ? 443 TYR A CE2 1 
ATOM   3373 C CZ  . TYR A 1 443 ? 12.900  5.261   28.049  1.00 42.47  ? 443 TYR A CZ  1 
ATOM   3374 O OH  . TYR A 1 443 ? 12.483  4.677   29.244  1.00 43.91  ? 443 TYR A OH  1 
ATOM   3375 N N   . LYS A 1 444 ? 16.056  9.187   22.645  1.00 40.60  ? 444 LYS A N   1 
ATOM   3376 C CA  . LYS A 1 444 ? 16.486  9.292   21.250  1.00 41.49  ? 444 LYS A CA  1 
ATOM   3377 C C   . LYS A 1 444 ? 16.981  10.701  20.907  1.00 40.40  ? 444 LYS A C   1 
ATOM   3378 O O   . LYS A 1 444 ? 16.235  11.655  21.034  1.00 40.17  ? 444 LYS A O   1 
ATOM   3379 C CB  . LYS A 1 444 ? 15.306  8.978   20.331  1.00 40.65  ? 444 LYS A CB  1 
ATOM   3380 C CG  . LYS A 1 444 ? 14.781  7.542   20.374  1.00 43.03  ? 444 LYS A CG  1 
ATOM   3381 C CD  . LYS A 1 444 ? 13.452  7.402   19.617  1.00 42.91  ? 444 LYS A CD  1 
ATOM   3382 C CE  . LYS A 1 444 ? 13.634  7.436   18.088  1.00 42.68  ? 444 LYS A CE  1 
ATOM   3383 N NZ  . LYS A 1 444 ? 14.351  6.248   17.620  1.00 42.74  ? 444 LYS A NZ  1 
ATOM   3384 N N   . TYR A 1 445 ? 18.224  10.810  20.444  1.00 40.57  ? 445 TYR A N   1 
ATOM   3385 C CA  . TYR A 1 445 ? 18.707  12.045  19.840  1.00 41.24  ? 445 TYR A CA  1 
ATOM   3386 C C   . TYR A 1 445 ? 17.917  12.295  18.559  1.00 41.41  ? 445 TYR A C   1 
ATOM   3387 O O   . TYR A 1 445 ? 17.352  11.353  17.995  1.00 40.69  ? 445 TYR A O   1 
ATOM   3388 C CB  . TYR A 1 445 ? 20.202  11.964  19.519  1.00 41.17  ? 445 TYR A CB  1 
ATOM   3389 C CG  . TYR A 1 445 ? 21.091  12.109  20.743  1.00 42.07  ? 445 TYR A CG  1 
ATOM   3390 C CD1 . TYR A 1 445 ? 21.802  11.018  21.251  1.00 38.87  ? 445 TYR A CD1 1 
ATOM   3391 C CD2 . TYR A 1 445 ? 21.232  13.346  21.385  1.00 40.94  ? 445 TYR A CD2 1 
ATOM   3392 C CE1 . TYR A 1 445 ? 22.651  11.153  22.328  1.00 39.98  ? 445 TYR A CE1 1 
ATOM   3393 C CE2 . TYR A 1 445 ? 22.077  13.489  22.494  1.00 41.13  ? 445 TYR A CE2 1 
ATOM   3394 C CZ  . TYR A 1 445 ? 22.771  12.380  22.975  1.00 41.82  ? 445 TYR A CZ  1 
ATOM   3395 O OH  . TYR A 1 445 ? 23.586  12.497  24.086  1.00 40.87  ? 445 TYR A OH  1 
ATOM   3396 N N   . PRO A 1 446 ? 17.837  13.566  18.122  1.00 41.16  ? 446 PRO A N   1 
ATOM   3397 C CA  . PRO A 1 446 ? 17.116  13.876  16.896  1.00 41.37  ? 446 PRO A CA  1 
ATOM   3398 C C   . PRO A 1 446 ? 17.676  13.162  15.667  1.00 42.00  ? 446 PRO A C   1 
ATOM   3399 O O   . PRO A 1 446 ? 18.904  13.024  15.512  1.00 40.68  ? 446 PRO A O   1 
ATOM   3400 C CB  . PRO A 1 446 ? 17.295  15.394  16.751  1.00 41.12  ? 446 PRO A CB  1 
ATOM   3401 C CG  . PRO A 1 446 ? 17.574  15.862  18.134  1.00 41.57  ? 446 PRO A CG  1 
ATOM   3402 C CD  . PRO A 1 446 ? 18.378  14.778  18.754  1.00 41.28  ? 446 PRO A CD  1 
ATOM   3403 N N   . GLU A 1 447 ? 16.759  12.752  14.792  1.00 42.67  ? 447 GLU A N   1 
ATOM   3404 C CA  . GLU A 1 447 ? 17.107  12.004  13.601  1.00 42.54  ? 447 GLU A CA  1 
ATOM   3405 C C   . GLU A 1 447 ? 18.040  12.839  12.723  1.00 41.93  ? 447 GLU A C   1 
ATOM   3406 O O   . GLU A 1 447 ? 17.770  14.007  12.432  1.00 41.39  ? 447 GLU A O   1 
ATOM   3407 C CB  . GLU A 1 447 ? 15.834  11.593  12.842  1.00 43.21  ? 447 GLU A CB  1 
ATOM   3408 C CG  . GLU A 1 447 ? 16.081  10.663  11.628  1.00 44.25  ? 447 GLU A CG  1 
ATOM   3409 C CD  . GLU A 1 447 ? 14.865  10.520  10.707  1.00 46.38  ? 447 GLU A CD  1 
ATOM   3410 O OE1 . GLU A 1 447 ? 13.776  11.059  11.034  1.00 50.84  ? 447 GLU A OE1 1 
ATOM   3411 O OE2 . GLU A 1 447 ? 15.012  9.896   9.622   1.00 51.37  ? 447 GLU A OE2 1 
ATOM   3412 N N   . GLY A 1 448 ? 19.163  12.241  12.353  1.00 41.03  ? 448 GLY A N   1 
ATOM   3413 C CA  . GLY A 1 448 ? 20.146  12.902  11.524  1.00 41.27  ? 448 GLY A CA  1 
ATOM   3414 C C   . GLY A 1 448 ? 21.246  13.655  12.245  1.00 40.95  ? 448 GLY A C   1 
ATOM   3415 O O   . GLY A 1 448 ? 22.190  14.128  11.616  1.00 40.69  ? 448 GLY A O   1 
ATOM   3416 N N   . SER A 1 449 ? 21.132  13.779  13.559  1.00 40.64  ? 449 SER A N   1 
ATOM   3417 C CA  . SER A 1 449 ? 22.147  14.466  14.333  1.00 40.46  ? 449 SER A CA  1 
ATOM   3418 C C   . SER A 1 449 ? 23.353  13.559  14.531  1.00 40.83  ? 449 SER A C   1 
ATOM   3419 O O   . SER A 1 449 ? 23.222  12.320  14.619  1.00 40.99  ? 449 SER A O   1 
ATOM   3420 C CB  . SER A 1 449 ? 21.595  14.853  15.704  1.00 39.70  ? 449 SER A CB  1 
ATOM   3421 O OG  . SER A 1 449 ? 21.310  13.685  16.451  1.00 37.36  ? 449 SER A OG  1 
ATOM   3422 N N   . SER A 1 450 ? 24.510  14.200  14.663  1.00 40.64  ? 450 SER A N   1 
ATOM   3423 C CA  . SER A 1 450 ? 25.768  13.533  14.945  1.00 41.30  ? 450 SER A CA  1 
ATOM   3424 C C   . SER A 1 450 ? 25.717  12.677  16.214  1.00 41.23  ? 450 SER A C   1 
ATOM   3425 O O   . SER A 1 450 ? 26.353  11.633  16.278  1.00 40.17  ? 450 SER A O   1 
ATOM   3426 C CB  . SER A 1 450 ? 26.872  14.582  15.078  1.00 41.00  ? 450 SER A CB  1 
ATOM   3427 O OG  . SER A 1 450 ? 26.859  15.456  13.955  1.00 43.86  ? 450 SER A OG  1 
ATOM   3428 N N   . GLU A 1 451 ? 24.952  13.121  17.209  1.00 41.75  ? 451 GLU A N   1 
ATOM   3429 C CA  . GLU A 1 451 ? 24.788  12.359  18.442  1.00 42.96  ? 451 GLU A CA  1 
ATOM   3430 C C   . GLU A 1 451 ? 23.987  11.079  18.191  1.00 43.41  ? 451 GLU A C   1 
ATOM   3431 O O   . GLU A 1 451 ? 24.265  10.029  18.785  1.00 42.20  ? 451 GLU A O   1 
ATOM   3432 C CB  . GLU A 1 451 ? 24.071  13.191  19.514  1.00 43.33  ? 451 GLU A CB  1 
ATOM   3433 C CG  . GLU A 1 451 ? 24.854  14.378  20.044  1.00 44.75  ? 451 GLU A CG  1 
ATOM   3434 C CD  . GLU A 1 451 ? 24.778  15.611  19.169  1.00 45.73  ? 451 GLU A CD  1 
ATOM   3435 O OE1 . GLU A 1 451 ? 25.379  16.627  19.576  1.00 49.50  ? 451 GLU A OE1 1 
ATOM   3436 O OE2 . GLU A 1 451 ? 24.169  15.577  18.073  1.00 46.85  ? 451 GLU A OE2 1 
ATOM   3437 N N   . GLU A 1 452 ? 22.967  11.195  17.339  1.00 44.00  ? 452 GLU A N   1 
ATOM   3438 C CA  . GLU A 1 452 ? 22.149  10.048  16.942  1.00 44.92  ? 452 GLU A CA  1 
ATOM   3439 C C   . GLU A 1 452 ? 23.010  9.018   16.225  1.00 45.11  ? 452 GLU A C   1 
ATOM   3440 O O   . GLU A 1 452 ? 22.976  7.832   16.532  1.00 43.80  ? 452 GLU A O   1 
ATOM   3441 C CB  . GLU A 1 452 ? 21.004  10.500  16.025  1.00 44.91  ? 452 GLU A CB  1 
ATOM   3442 C CG  . GLU A 1 452 ? 19.855  9.504   15.842  1.00 45.65  ? 452 GLU A CG  1 
ATOM   3443 C CD  . GLU A 1 452 ? 19.853  8.812   14.501  1.00 48.36  ? 452 GLU A CD  1 
ATOM   3444 O OE1 . GLU A 1 452 ? 20.036  9.464   13.448  1.00 44.67  ? 452 GLU A OE1 1 
ATOM   3445 O OE2 . GLU A 1 452 ? 19.669  7.584   14.511  1.00 54.59  ? 452 GLU A OE2 1 
ATOM   3446 N N   . ARG A 1 453 ? 23.809  9.490   15.283  1.00 46.27  ? 453 ARG A N   1 
ATOM   3447 C CA  . ARG A 1 453 ? 24.586  8.585   14.449  1.00 47.46  ? 453 ARG A CA  1 
ATOM   3448 C C   . ARG A 1 453 ? 25.703  7.939   15.258  1.00 47.96  ? 453 ARG A C   1 
ATOM   3449 O O   . ARG A 1 453 ? 26.008  6.768   15.081  1.00 47.46  ? 453 ARG A O   1 
ATOM   3450 C CB  . ARG A 1 453 ? 25.129  9.328   13.235  1.00 47.73  ? 453 ARG A CB  1 
ATOM   3451 C CG  . ARG A 1 453 ? 24.019  10.051  12.471  1.00 47.97  ? 453 ARG A CG  1 
ATOM   3452 C CD  . ARG A 1 453 ? 24.332  10.223  11.009  1.00 48.91  ? 453 ARG A CD  1 
ATOM   3453 N NE  . ARG A 1 453 ? 23.517  11.282  10.416  1.00 50.09  ? 453 ARG A NE  1 
ATOM   3454 C CZ  . ARG A 1 453 ? 23.453  11.552  9.121   1.00 50.63  ? 453 ARG A CZ  1 
ATOM   3455 N NH1 . ARG A 1 453 ? 24.159  10.834  8.253   1.00 52.82  ? 453 ARG A NH1 1 
ATOM   3456 N NH2 . ARG A 1 453 ? 22.682  12.545  8.689   1.00 50.56  ? 453 ARG A NH2 1 
ATOM   3457 N N   . GLU A 1 454 ? 26.283  8.700   16.174  1.00 49.22  ? 454 GLU A N   1 
ATOM   3458 C CA  . GLU A 1 454 ? 27.329  8.182   17.045  1.00 49.97  ? 454 GLU A CA  1 
ATOM   3459 C C   . GLU A 1 454 ? 26.792  7.114   18.024  1.00 50.22  ? 454 GLU A C   1 
ATOM   3460 O O   . GLU A 1 454 ? 27.487  6.150   18.354  1.00 50.60  ? 454 GLU A O   1 
ATOM   3461 C CB  . GLU A 1 454 ? 27.942  9.347   17.810  1.00 50.55  ? 454 GLU A CB  1 
ATOM   3462 C CG  . GLU A 1 454 ? 29.331  9.101   18.369  1.00 51.20  ? 454 GLU A CG  1 
ATOM   3463 C CD  . GLU A 1 454 ? 29.668  10.075  19.488  1.00 51.89  ? 454 GLU A CD  1 
ATOM   3464 O OE1 . GLU A 1 454 ? 28.729  10.559  20.160  1.00 54.73  ? 454 GLU A OE1 1 
ATOM   3465 O OE2 . GLU A 1 454 ? 30.868  10.355  19.694  1.00 56.04  ? 454 GLU A OE2 1 
ATOM   3466 N N   . ALA A 1 455 ? 25.563  7.298   18.489  1.00 50.10  ? 455 ALA A N   1 
ATOM   3467 C CA  . ALA A 1 455 ? 24.904  6.311   19.328  1.00 50.60  ? 455 ALA A CA  1 
ATOM   3468 C C   . ALA A 1 455 ? 24.572  5.058   18.534  1.00 51.17  ? 455 ALA A C   1 
ATOM   3469 O O   . ALA A 1 455 ? 24.679  3.952   19.046  1.00 50.70  ? 455 ALA A O   1 
ATOM   3470 C CB  . ALA A 1 455 ? 23.649  6.883   19.906  1.00 49.86  ? 455 ALA A CB  1 
ATOM   3471 N N   . PHE A 1 456 ? 24.132  5.249   17.288  1.00 52.26  ? 456 PHE A N   1 
ATOM   3472 C CA  . PHE A 1 456 ? 23.772  4.151   16.391  1.00 52.91  ? 456 PHE A CA  1 
ATOM   3473 C C   . PHE A 1 456 ? 25.028  3.303   16.107  1.00 53.32  ? 456 PHE A C   1 
ATOM   3474 O O   . PHE A 1 456 ? 24.951  2.080   16.032  1.00 52.81  ? 456 PHE A O   1 
ATOM   3475 C CB  . PHE A 1 456 ? 23.122  4.739   15.120  1.00 53.82  ? 456 PHE A CB  1 
ATOM   3476 C CG  . PHE A 1 456 ? 22.839  3.737   14.018  1.00 54.02  ? 456 PHE A CG  1 
ATOM   3477 C CD1 . PHE A 1 456 ? 23.808  3.434   13.063  1.00 55.40  ? 456 PHE A CD1 1 
ATOM   3478 C CD2 . PHE A 1 456 ? 21.582  3.157   13.889  1.00 55.99  ? 456 PHE A CD2 1 
ATOM   3479 C CE1 . PHE A 1 456 ? 23.542  2.534   12.024  1.00 55.40  ? 456 PHE A CE1 1 
ATOM   3480 C CE2 . PHE A 1 456 ? 21.308  2.258   12.846  1.00 55.41  ? 456 PHE A CE2 1 
ATOM   3481 C CZ  . PHE A 1 456 ? 22.286  1.950   11.920  1.00 55.15  ? 456 PHE A CZ  1 
ATOM   3482 N N   . THR A 1 457 ? 26.182  3.962   16.020  1.00 54.01  ? 457 THR A N   1 
ATOM   3483 C CA  . THR A 1 457 ? 27.474  3.290   15.861  1.00 54.58  ? 457 THR A CA  1 
ATOM   3484 C C   . THR A 1 457 ? 27.887  2.461   17.081  1.00 55.41  ? 457 THR A C   1 
ATOM   3485 O O   . THR A 1 457 ? 28.413  1.359   16.937  1.00 55.18  ? 457 THR A O   1 
ATOM   3486 C CB  . THR A 1 457 ? 28.593  4.313   15.525  1.00 54.63  ? 457 THR A CB  1 
ATOM   3487 O OG1 . THR A 1 457 ? 28.425  4.770   14.178  1.00 53.81  ? 457 THR A OG1 1 
ATOM   3488 C CG2 . THR A 1 457 ? 29.984  3.697   15.669  1.00 54.21  ? 457 THR A CG2 1 
ATOM   3489 N N   . ARG A 1 458 ? 27.658  2.987   18.280  1.00 56.41  ? 458 ARG A N   1 
ATOM   3490 C CA  . ARG A 1 458 ? 28.019  2.271   19.501  1.00 56.87  ? 458 ARG A CA  1 
ATOM   3491 C C   . ARG A 1 458 ? 27.140  1.023   19.697  1.00 57.00  ? 458 ARG A C   1 
ATOM   3492 O O   . ARG A 1 458 ? 27.616  -0.005  20.195  1.00 56.44  ? 458 ARG A O   1 
ATOM   3493 C CB  . ARG A 1 458 ? 27.925  3.203   20.712  1.00 56.95  ? 458 ARG A CB  1 
ATOM   3494 C CG  . ARG A 1 458 ? 28.640  2.668   21.956  1.00 57.76  ? 458 ARG A CG  1 
ATOM   3495 C CD  . ARG A 1 458 ? 28.543  3.587   23.191  1.00 59.35  ? 458 ARG A CD  1 
ATOM   3496 N NE  . ARG A 1 458 ? 28.449  5.014   22.866  1.00 62.01  ? 458 ARG A NE  1 
ATOM   3497 C CZ  . ARG A 1 458 ? 29.439  5.761   22.369  1.00 63.56  ? 458 ARG A CZ  1 
ATOM   3498 N NH1 . ARG A 1 458 ? 30.642  5.239   22.113  1.00 64.29  ? 458 ARG A NH1 1 
ATOM   3499 N NH2 . ARG A 1 458 ? 29.223  7.051   22.118  1.00 63.60  ? 458 ARG A NH2 1 
ATOM   3500 N N   . ALA A 1 459 ? 25.879  1.121   19.267  1.00 57.36  ? 459 ALA A N   1 
ATOM   3501 C CA  . ALA A 1 459 ? 24.879  0.050   19.411  1.00 57.98  ? 459 ALA A CA  1 
ATOM   3502 C C   . ALA A 1 459 ? 25.056  -1.173  18.479  1.00 58.43  ? 459 ALA A C   1 
ATOM   3503 O O   . ALA A 1 459 ? 24.583  -2.261  18.799  1.00 58.23  ? 459 ALA A O   1 
ATOM   3504 C CB  . ALA A 1 459 ? 23.482  0.621   19.244  1.00 57.49  ? 459 ALA A CB  1 
ATOM   3505 N N   . ASN A 1 460 ? 25.701  -1.004  17.331  1.00 59.41  ? 460 ASN A N   1 
ATOM   3506 C CA  . ASN A 1 460 ? 25.996  -2.157  16.456  1.00 59.97  ? 460 ASN A CA  1 
ATOM   3507 C C   . ASN A 1 460 ? 27.490  -2.324  16.140  1.00 60.66  ? 460 ASN A C   1 
ATOM   3508 O O   . ASN A 1 460 ? 27.872  -3.136  15.278  1.00 60.71  ? 460 ASN A O   1 
ATOM   3509 C CB  . ASN A 1 460 ? 25.138  -2.157  15.174  1.00 60.14  ? 460 ASN A CB  1 
ATOM   3510 C CG  . ASN A 1 460 ? 24.466  -0.825  14.895  1.00 60.87  ? 460 ASN A CG  1 
ATOM   3511 O OD1 . ASN A 1 460 ? 23.521  -0.432  15.583  1.00 63.23  ? 460 ASN A OD1 1 
ATOM   3512 N ND2 . ASN A 1 460 ? 24.928  -0.136  13.853  1.00 62.69  ? 460 ASN A ND2 1 
ATOM   3513 N N   . HIS A 1 461 ? 28.325  -1.582  16.869  1.00 61.22  ? 461 HIS A N   1 
ATOM   3514 C CA  . HIS A 1 461 ? 29.777  -1.677  16.748  1.00 61.54  ? 461 HIS A CA  1 
ATOM   3515 C C   . HIS A 1 461 ? 30.259  -1.323  15.336  1.00 61.72  ? 461 HIS A C   1 
ATOM   3516 O O   . HIS A 1 461 ? 31.409  -1.583  14.970  1.00 61.91  ? 461 HIS A O   1 
ATOM   3517 C CB  . HIS A 1 461 ? 30.244  -3.077  17.171  1.00 62.02  ? 461 HIS A CB  1 
ATOM   3518 C CG  . HIS A 1 461 ? 29.575  -3.581  18.416  1.00 63.23  ? 461 HIS A CG  1 
ATOM   3519 N ND1 . HIS A 1 461 ? 29.453  -2.813  19.556  1.00 64.43  ? 461 HIS A ND1 1 
ATOM   3520 C CD2 . HIS A 1 461 ? 28.991  -4.771  18.701  1.00 64.23  ? 461 HIS A CD2 1 
ATOM   3521 C CE1 . HIS A 1 461 ? 28.828  -3.509  20.490  1.00 64.65  ? 461 HIS A CE1 1 
ATOM   3522 N NE2 . HIS A 1 461 ? 28.535  -4.700  19.997  1.00 64.69  ? 461 HIS A NE2 1 
ATOM   3523 N N   . GLY A 1 472 ? 28.493  -3.116  6.522   1.00 51.89  ? 472 GLY A N   1 
ATOM   3524 C CA  . GLY A 1 472 ? 29.048  -4.218  5.737   1.00 51.75  ? 472 GLY A CA  1 
ATOM   3525 C C   . GLY A 1 472 ? 28.057  -5.284  5.280   1.00 51.67  ? 472 GLY A C   1 
ATOM   3526 O O   . GLY A 1 472 ? 28.295  -5.939  4.259   1.00 51.91  ? 472 GLY A O   1 
ATOM   3527 N N   . MET A 1 473 ? 26.956  -5.473  6.010   1.00 51.59  ? 473 MET A N   1 
ATOM   3528 C CA  . MET A 1 473 ? 25.946  -6.475  5.618   1.00 51.26  ? 473 MET A CA  1 
ATOM   3529 C C   . MET A 1 473 ? 25.117  -6.046  4.389   1.00 50.64  ? 473 MET A C   1 
ATOM   3530 O O   . MET A 1 473 ? 24.699  -4.904  4.309   1.00 50.35  ? 473 MET A O   1 
ATOM   3531 C CB  . MET A 1 473 ? 25.001  -6.771  6.777   1.00 51.78  ? 473 MET A CB  1 
ATOM   3532 C CG  . MET A 1 473 ? 24.046  -7.938  6.501   1.00 53.24  ? 473 MET A CG  1 
ATOM   3533 S SD  . MET A 1 473 ? 24.750  -9.594  6.769   1.00 60.55  ? 473 MET A SD  1 
ATOM   3534 C CE  . MET A 1 473 ? 24.031  -10.002 8.360   1.00 57.67  ? 473 MET A CE  1 
ATOM   3535 N N   . ALA A 1 474 ? 24.868  -6.970  3.456   1.00 49.91  ? 474 ALA A N   1 
ATOM   3536 C CA  . ALA A 1 474 ? 24.050  -6.675  2.261   1.00 49.62  ? 474 ALA A CA  1 
ATOM   3537 C C   . ALA A 1 474 ? 23.257  -7.879  1.753   1.00 49.18  ? 474 ALA A C   1 
ATOM   3538 O O   . ALA A 1 474 ? 23.613  -9.032  2.007   1.00 49.61  ? 474 ALA A O   1 
ATOM   3539 C CB  . ALA A 1 474 ? 24.917  -6.096  1.145   1.00 49.43  ? 474 ALA A CB  1 
ATOM   3540 N N   . MET A 1 475 ? 22.148  -7.606  1.072   1.00 48.40  ? 475 MET A N   1 
ATOM   3541 C CA  . MET A 1 475 ? 21.302  -8.669  0.532   1.00 48.15  ? 475 MET A CA  1 
ATOM   3542 C C   . MET A 1 475 ? 20.722  -8.265  -0.834  1.00 48.33  ? 475 MET A C   1 
ATOM   3543 O O   . MET A 1 475 ? 20.339  -7.114  -1.044  1.00 47.89  ? 475 MET A O   1 
ATOM   3544 C CB  . MET A 1 475 ? 20.171  -9.030  1.492   1.00 47.70  ? 475 MET A CB  1 
ATOM   3545 C CG  . MET A 1 475 ? 19.541  -10.383 1.178   1.00 47.86  ? 475 MET A CG  1 
ATOM   3546 S SD  . MET A 1 475 ? 18.196  -10.949 2.252   1.00 45.90  ? 475 MET A SD  1 
ATOM   3547 C CE  . MET A 1 475 ? 17.339  -9.382  2.446   1.00 44.67  ? 475 MET A CE  1 
ATOM   3548 N N   . ARG A 1 476 ? 20.688  -9.227  -1.753  1.00 48.74  ? 476 ARG A N   1 
ATOM   3549 C CA  . ARG A 1 476 ? 20.021  -9.064  -3.035  1.00 49.10  ? 476 ARG A CA  1 
ATOM   3550 C C   . ARG A 1 476 ? 19.513  -10.412 -3.541  1.00 49.16  ? 476 ARG A C   1 
ATOM   3551 O O   . ARG A 1 476 ? 19.964  -11.476 -3.099  1.00 48.88  ? 476 ARG A O   1 
ATOM   3552 C CB  . ARG A 1 476 ? 20.964  -8.426  -4.047  1.00 49.05  ? 476 ARG A CB  1 
ATOM   3553 C CG  . ARG A 1 476 ? 22.215  -9.221  -4.378  1.00 50.25  ? 476 ARG A CG  1 
ATOM   3554 C CD  . ARG A 1 476 ? 22.966  -8.562  -5.550  1.00 51.92  ? 476 ARG A CD  1 
ATOM   3555 N NE  . ARG A 1 476 ? 24.419  -8.604  -5.358  1.00 54.70  ? 476 ARG A NE  1 
ATOM   3556 C CZ  . ARG A 1 476 ? 25.216  -9.611  -5.712  1.00 55.48  ? 476 ARG A CZ  1 
ATOM   3557 N NH1 . ARG A 1 476 ? 24.727  -10.701 -6.317  1.00 56.61  ? 476 ARG A NH1 1 
ATOM   3558 N NH2 . ARG A 1 476 ? 26.525  -9.521  -5.468  1.00 54.76  ? 476 ARG A NH2 1 
ATOM   3559 N N   . ILE A 1 477 ? 18.569  -10.349 -4.469  1.00 48.85  ? 477 ILE A N   1 
ATOM   3560 C CA  . ILE A 1 477 ? 17.988  -11.533 -5.069  1.00 49.08  ? 477 ILE A CA  1 
ATOM   3561 C C   . ILE A 1 477 ? 18.833  -11.885 -6.302  1.00 49.53  ? 477 ILE A C   1 
ATOM   3562 O O   . ILE A 1 477 ? 19.061  -11.034 -7.169  1.00 48.34  ? 477 ILE A O   1 
ATOM   3563 C CB  . ILE A 1 477 ? 16.522  -11.260 -5.465  1.00 49.17  ? 477 ILE A CB  1 
ATOM   3564 C CG1 . ILE A 1 477 ? 15.759  -10.633 -4.280  1.00 47.45  ? 477 ILE A CG1 1 
ATOM   3565 C CG2 . ILE A 1 477 ? 15.877  -12.523 -6.031  1.00 47.86  ? 477 ILE A CG2 1 
ATOM   3566 C CD1 . ILE A 1 477 ? 15.803  -11.411 -2.969  1.00 46.05  ? 477 ILE A CD1 1 
ATOM   3567 N N   . ARG A 1 478 ? 19.321  -13.121 -6.339  1.00 49.80  ? 478 ARG A N   1 
ATOM   3568 C CA  . ARG A 1 478 ? 20.076  -13.658 -7.456  1.00 50.88  ? 478 ARG A CA  1 
ATOM   3569 C C   . ARG A 1 478 ? 19.264  -14.774 -8.121  1.00 50.84  ? 478 ARG A C   1 
ATOM   3570 O O   . ARG A 1 478 ? 18.365  -15.344 -7.498  1.00 49.45  ? 478 ARG A O   1 
ATOM   3571 C CB  . ARG A 1 478 ? 21.387  -14.270 -6.970  1.00 50.62  ? 478 ARG A CB  1 
ATOM   3572 C CG  . ARG A 1 478 ? 22.586  -13.364 -6.901  1.00 51.81  ? 478 ARG A CG  1 
ATOM   3573 C CD  . ARG A 1 478 ? 23.904  -14.207 -6.987  1.00 54.16  ? 478 ARG A CD  1 
ATOM   3574 N NE  . ARG A 1 478 ? 23.810  -15.523 -6.310  1.00 56.69  ? 478 ARG A NE  1 
ATOM   3575 C CZ  . ARG A 1 478 ? 23.810  -16.718 -6.920  1.00 58.00  ? 478 ARG A CZ  1 
ATOM   3576 N NH1 . ARG A 1 478 ? 23.915  -16.836 -8.241  1.00 57.62  ? 478 ARG A NH1 1 
ATOM   3577 N NH2 . ARG A 1 478 ? 23.717  -17.827 -6.198  1.00 58.69  ? 478 ARG A NH2 1 
ATOM   3578 N N   . VAL A 1 479 ? 19.593  -15.078 -9.381  1.00 51.63  ? 479 VAL A N   1 
ATOM   3579 C CA  . VAL A 1 479 ? 18.999  -16.219 -10.102 1.00 53.03  ? 479 VAL A CA  1 
ATOM   3580 C C   . VAL A 1 479 ? 20.081  -17.118 -10.721 1.00 53.68  ? 479 VAL A C   1 
ATOM   3581 O O   . VAL A 1 479 ? 20.068  -18.335 -10.534 1.00 53.90  ? 479 VAL A O   1 
ATOM   3582 C CB  . VAL A 1 479 ? 18.013  -15.785 -11.212 1.00 53.01  ? 479 VAL A CB  1 
ATOM   3583 C CG1 . VAL A 1 479 ? 17.033  -16.912 -11.505 1.00 54.25  ? 479 VAL A CG1 1 
ATOM   3584 C CG2 . VAL A 1 479 ? 17.265  -14.545 -10.825 1.00 53.99  ? 479 VAL A CG2 1 
ATOM   3585 N N   . GLY A 1 480 ? 21.002  -16.517 -11.470 1.00 54.48  ? 480 GLY A N   1 
ATOM   3586 C CA  . GLY A 1 480 ? 22.174  -17.240 -11.989 1.00 54.96  ? 480 GLY A CA  1 
ATOM   3587 C C   . GLY A 1 480 ? 22.022  -17.960 -13.322 1.00 55.58  ? 480 GLY A C   1 
ATOM   3588 O O   . GLY A 1 480 ? 23.023  -18.436 -13.878 1.00 56.12  ? 480 GLY A O   1 
ATOM   3589 N N   . GLN A 1 481 ? 20.794  -18.073 -13.840 1.00 55.98  ? 481 GLN A N   1 
ATOM   3590 C CA  . GLN A 1 481 ? 20.593  -18.573 -15.212 1.00 55.94  ? 481 GLN A CA  1 
ATOM   3591 C C   . GLN A 1 481 ? 19.296  -18.019 -15.833 1.00 56.02  ? 481 GLN A C   1 
ATOM   3592 O O   . GLN A 1 481 ? 18.604  -17.191 -15.214 1.00 55.59  ? 481 GLN A O   1 
ATOM   3593 C CB  . GLN A 1 481 ? 20.715  -20.118 -15.279 1.00 56.44  ? 481 GLN A CB  1 
ATOM   3594 C CG  . GLN A 1 481 ? 19.435  -20.955 -15.479 1.00 57.45  ? 481 GLN A CG  1 
ATOM   3595 C CD  . GLN A 1 481 ? 18.652  -21.176 -14.217 1.00 59.09  ? 481 GLN A CD  1 
ATOM   3596 O OE1 . GLN A 1 481 ? 18.791  -20.429 -13.236 1.00 62.50  ? 481 GLN A OE1 1 
ATOM   3597 N NE2 . GLN A 1 481 ? 17.811  -22.204 -14.225 1.00 57.66  ? 481 GLN A NE2 1 
ATOM   3598 N N   . SER A 1 482 ? 19.005  -18.425 -17.074 1.00 55.65  ? 482 SER A N   1 
ATOM   3599 C CA  . SER A 1 482 ? 17.791  -17.960 -17.758 1.00 55.29  ? 482 SER A CA  1 
ATOM   3600 C C   . SER A 1 482 ? 16.534  -18.511 -17.070 1.00 55.23  ? 482 SER A C   1 
ATOM   3601 O O   . SER A 1 482 ? 16.555  -19.605 -16.477 1.00 55.58  ? 482 SER A O   1 
ATOM   3602 C CB  . SER A 1 482 ? 17.813  -18.324 -19.256 1.00 55.57  ? 482 SER A CB  1 
ATOM   3603 O OG  . SER A 1 482 ? 17.632  -19.714 -19.473 1.00 54.90  ? 482 SER A OG  1 
ATOM   3604 N N   . MET A 1 483 ? 15.459  -17.724 -17.110 1.00 54.26  ? 483 MET A N   1 
ATOM   3605 C CA  . MET A 1 483 ? 14.196  -18.118 -16.497 1.00 53.64  ? 483 MET A CA  1 
ATOM   3606 C C   . MET A 1 483 ? 13.153  -18.223 -17.567 1.00 52.37  ? 483 MET A C   1 
ATOM   3607 O O   . MET A 1 483 ? 12.874  -17.247 -18.274 1.00 52.80  ? 483 MET A O   1 
ATOM   3608 C CB  . MET A 1 483 ? 13.749  -17.094 -15.477 1.00 53.31  ? 483 MET A CB  1 
ATOM   3609 C CG  . MET A 1 483 ? 14.602  -17.082 -14.244 1.00 53.70  ? 483 MET A CG  1 
ATOM   3610 S SD  . MET A 1 483 ? 14.124  -15.682 -13.268 1.00 54.10  ? 483 MET A SD  1 
ATOM   3611 C CE  . MET A 1 483 ? 14.618  -14.340 -14.350 1.00 50.93  ? 483 MET A CE  1 
ATOM   3612 N N   . ASN A 1 484 ? 12.560  -19.404 -17.662 1.00 50.87  ? 484 ASN A N   1 
ATOM   3613 C CA  . ASN A 1 484 ? 11.732  -19.766 -18.798 1.00 49.12  ? 484 ASN A CA  1 
ATOM   3614 C C   . ASN A 1 484 ? 10.338  -20.126 -18.348 1.00 48.74  ? 484 ASN A C   1 
ATOM   3615 O O   . ASN A 1 484 ? 10.162  -20.796 -17.326 1.00 48.86  ? 484 ASN A O   1 
ATOM   3616 C CB  . ASN A 1 484 ? 12.347  -20.961 -19.508 1.00 49.03  ? 484 ASN A CB  1 
ATOM   3617 C CG  . ASN A 1 484 ? 13.675  -20.638 -20.118 1.00 49.01  ? 484 ASN A CG  1 
ATOM   3618 O OD1 . ASN A 1 484 ? 13.850  -19.576 -20.708 1.00 52.22  ? 484 ASN A OD1 1 
ATOM   3619 N ND2 . ASN A 1 484 ? 14.623  -21.553 -20.001 1.00 48.34  ? 484 ASN A ND2 1 
ATOM   3620 N N   . MET A 1 485 ? 9.349   -19.682 -19.111 1.00 47.68  ? 485 MET A N   1 
ATOM   3621 C CA  . MET A 1 485 ? 7.973   -20.044 -18.854 1.00 46.99  ? 485 MET A CA  1 
ATOM   3622 C C   . MET A 1 485 ? 7.856   -21.549 -19.030 1.00 46.06  ? 485 MET A C   1 
ATOM   3623 O O   . MET A 1 485 ? 8.140   -22.070 -20.100 1.00 44.98  ? 485 MET A O   1 
ATOM   3624 C CB  . MET A 1 485 ? 7.040   -19.311 -19.819 1.00 47.70  ? 485 MET A CB  1 
ATOM   3625 C CG  . MET A 1 485 ? 5.568   -19.673 -19.702 1.00 48.34  ? 485 MET A CG  1 
ATOM   3626 S SD  . MET A 1 485 ? 4.923   -19.140 -18.116 1.00 50.01  ? 485 MET A SD  1 
ATOM   3627 C CE  . MET A 1 485 ? 3.438   -20.148 -18.019 1.00 48.14  ? 485 MET A CE  1 
ATOM   3628 N N   . GLY A 1 486 ? 7.454   -22.237 -17.964 1.00 45.01  ? 486 GLY A N   1 
ATOM   3629 C CA  . GLY A 1 486 ? 7.306   -23.680 -17.994 1.00 44.61  ? 486 GLY A CA  1 
ATOM   3630 C C   . GLY A 1 486 ? 8.348   -24.420 -17.178 1.00 44.37  ? 486 GLY A C   1 
ATOM   3631 O O   . GLY A 1 486 ? 8.188   -25.602 -16.913 1.00 44.00  ? 486 GLY A O   1 
ATOM   3632 N N   . SER A 1 487 ? 9.408   -23.728 -16.767 1.00 44.09  ? 487 SER A N   1 
ATOM   3633 C CA  . SER A 1 487 ? 10.495  -24.359 -16.025 1.00 43.90  ? 487 SER A CA  1 
ATOM   3634 C C   . SER A 1 487 ? 10.336  -24.185 -14.502 1.00 43.13  ? 487 SER A C   1 
ATOM   3635 O O   . SER A 1 487 ? 9.656   -23.274 -14.031 1.00 41.85  ? 487 SER A O   1 
ATOM   3636 C CB  . SER A 1 487 ? 11.849  -23.803 -16.486 1.00 44.11  ? 487 SER A CB  1 
ATOM   3637 O OG  . SER A 1 487 ? 12.100  -22.518 -15.927 1.00 45.71  ? 487 SER A OG  1 
ATOM   3638 N N   . ASP A 1 488 ? 10.928  -25.123 -13.763 1.00 43.07  ? 488 ASP A N   1 
ATOM   3639 C CA  . ASP A 1 488 ? 11.168  -25.002 -12.319 1.00 43.28  ? 488 ASP A CA  1 
ATOM   3640 C C   . ASP A 1 488 ? 12.561  -24.389 -12.181 1.00 43.66  ? 488 ASP A C   1 
ATOM   3641 O O   . ASP A 1 488 ? 13.499  -24.815 -12.879 1.00 43.09  ? 488 ASP A O   1 
ATOM   3642 C CB  . ASP A 1 488 ? 11.198  -26.370 -11.636 1.00 42.86  ? 488 ASP A CB  1 
ATOM   3643 C CG  . ASP A 1 488 ? 9.936   -27.176 -11.838 1.00 41.78  ? 488 ASP A CG  1 
ATOM   3644 O OD1 . ASP A 1 488 ? 8.845   -26.590 -11.846 1.00 40.85  ? 488 ASP A OD1 1 
ATOM   3645 O OD2 . ASP A 1 488 ? 10.035  -28.414 -11.963 1.00 40.19  ? 488 ASP A OD2 1 
ATOM   3646 N N   . PHE A 1 489 ? 12.717  -23.415 -11.287 1.00 43.69  ? 489 PHE A N   1 
ATOM   3647 C CA  . PHE A 1 489 ? 14.016  -22.776 -11.116 1.00 44.07  ? 489 PHE A CA  1 
ATOM   3648 C C   . PHE A 1 489 ? 14.172  -22.277 -9.682  1.00 44.09  ? 489 PHE A C   1 
ATOM   3649 O O   . PHE A 1 489 ? 13.185  -22.040 -8.995  1.00 43.91  ? 489 PHE A O   1 
ATOM   3650 C CB  . PHE A 1 489 ? 14.229  -21.623 -12.136 1.00 44.35  ? 489 PHE A CB  1 
ATOM   3651 C CG  . PHE A 1 489 ? 13.217  -20.526 -12.034 1.00 44.61  ? 489 PHE A CG  1 
ATOM   3652 C CD1 . PHE A 1 489 ? 13.490  -19.382 -11.297 1.00 42.70  ? 489 PHE A CD1 1 
ATOM   3653 C CD2 . PHE A 1 489 ? 11.988  -20.638 -12.673 1.00 45.30  ? 489 PHE A CD2 1 
ATOM   3654 C CE1 . PHE A 1 489 ? 12.556  -18.376 -11.166 1.00 44.95  ? 489 PHE A CE1 1 
ATOM   3655 C CE2 . PHE A 1 489 ? 11.044  -19.613 -12.572 1.00 45.62  ? 489 PHE A CE2 1 
ATOM   3656 C CZ  . PHE A 1 489 ? 11.330  -18.482 -11.804 1.00 46.07  ? 489 PHE A CZ  1 
ATOM   3657 N N   . ASP A 1 490 ? 15.418  -22.128 -9.257  1.00 43.89  ? 490 ASP A N   1 
ATOM   3658 C CA  . ASP A 1 490 ? 15.717  -21.571 -7.948  1.00 44.47  ? 490 ASP A CA  1 
ATOM   3659 C C   . ASP A 1 490 ? 15.991  -20.084 -8.057  1.00 44.16  ? 490 ASP A C   1 
ATOM   3660 O O   . ASP A 1 490 ? 16.621  -19.636 -9.021  1.00 43.42  ? 490 ASP A O   1 
ATOM   3661 C CB  . ASP A 1 490 ? 16.941  -22.245 -7.344  1.00 44.63  ? 490 ASP A CB  1 
ATOM   3662 C CG  . ASP A 1 490 ? 16.676  -23.661 -6.899  1.00 46.36  ? 490 ASP A CG  1 
ATOM   3663 O OD1 . ASP A 1 490 ? 15.520  -24.003 -6.555  1.00 49.14  ? 490 ASP A OD1 1 
ATOM   3664 O OD2 . ASP A 1 490 ? 17.638  -24.443 -6.889  1.00 47.85  ? 490 ASP A OD2 1 
ATOM   3665 N N   . VAL A 1 491 ? 15.506  -19.337 -7.064  1.00 43.98  ? 491 VAL A N   1 
ATOM   3666 C CA  . VAL A 1 491 ? 15.933  -17.966 -6.801  1.00 44.04  ? 491 VAL A CA  1 
ATOM   3667 C C   . VAL A 1 491 ? 16.721  -17.979 -5.486  1.00 44.60  ? 491 VAL A C   1 
ATOM   3668 O O   . VAL A 1 491 ? 16.612  -18.934 -4.696  1.00 43.30  ? 491 VAL A O   1 
ATOM   3669 C CB  . VAL A 1 491 ? 14.757  -16.979 -6.754  1.00 43.88  ? 491 VAL A CB  1 
ATOM   3670 C CG1 . VAL A 1 491 ? 14.021  -16.936 -8.134  1.00 45.80  ? 491 VAL A CG1 1 
ATOM   3671 C CG2 . VAL A 1 491 ? 13.752  -17.322 -5.683  1.00 44.44  ? 491 VAL A CG2 1 
ATOM   3672 N N   . PHE A 1 492 ? 17.548  -16.960 -5.263  1.00 44.30  ? 492 PHE A N   1 
ATOM   3673 C CA  . PHE A 1 492 ? 18.433  -16.957 -4.091  1.00 44.29  ? 492 PHE A CA  1 
ATOM   3674 C C   . PHE A 1 492 ? 18.422  -15.628 -3.368  1.00 44.32  ? 492 PHE A C   1 
ATOM   3675 O O   . PHE A 1 492 ? 18.501  -14.567 -4.010  1.00 44.64  ? 492 PHE A O   1 
ATOM   3676 C CB  . PHE A 1 492 ? 19.883  -17.227 -4.480  1.00 44.45  ? 492 PHE A CB  1 
ATOM   3677 C CG  . PHE A 1 492 ? 20.099  -18.514 -5.186  1.00 44.68  ? 492 PHE A CG  1 
ATOM   3678 C CD1 . PHE A 1 492 ? 20.030  -18.570 -6.573  1.00 43.44  ? 492 PHE A CD1 1 
ATOM   3679 C CD2 . PHE A 1 492 ? 20.398  -19.661 -4.486  1.00 44.66  ? 492 PHE A CD2 1 
ATOM   3680 C CE1 . PHE A 1 492 ? 20.234  -19.753 -7.241  1.00 44.55  ? 492 PHE A CE1 1 
ATOM   3681 C CE2 . PHE A 1 492 ? 20.603  -20.859 -5.144  1.00 44.47  ? 492 PHE A CE2 1 
ATOM   3682 C CZ  . PHE A 1 492 ? 20.529  -20.908 -6.521  1.00 45.04  ? 492 PHE A CZ  1 
ATOM   3683 N N   . ALA A 1 493 ? 18.344  -15.670 -2.037  1.00 43.56  ? 493 ALA A N   1 
ATOM   3684 C CA  . ALA A 1 493 ? 18.679  -14.496 -1.237  1.00 43.71  ? 493 ALA A CA  1 
ATOM   3685 C C   . ALA A 1 493 ? 20.182  -14.583 -1.101  1.00 43.79  ? 493 ALA A C   1 
ATOM   3686 O O   . ALA A 1 493 ? 20.708  -15.498 -0.452  1.00 44.33  ? 493 ALA A O   1 
ATOM   3687 C CB  . ALA A 1 493 ? 18.005  -14.520 0.125   1.00 43.01  ? 493 ALA A CB  1 
ATOM   3688 N N   . HIS A 1 494 ? 20.882  -13.669 -1.749  1.00 43.99  ? 494 HIS A N   1 
ATOM   3689 C CA  . HIS A 1 494 ? 22.329  -13.653 -1.673  1.00 43.91  ? 494 HIS A CA  1 
ATOM   3690 C C   . HIS A 1 494 ? 22.736  -12.660 -0.578  1.00 44.36  ? 494 HIS A C   1 
ATOM   3691 O O   . HIS A 1 494 ? 22.677  -11.444 -0.762  1.00 43.87  ? 494 HIS A O   1 
ATOM   3692 C CB  . HIS A 1 494 ? 22.964  -13.322 -3.013  1.00 43.98  ? 494 HIS A CB  1 
ATOM   3693 C CG  . HIS A 1 494 ? 24.458  -13.324 -2.971  1.00 44.87  ? 494 HIS A CG  1 
ATOM   3694 N ND1 . HIS A 1 494 ? 25.195  -14.462 -2.715  1.00 46.23  ? 494 HIS A ND1 1 
ATOM   3695 C CD2 . HIS A 1 494 ? 25.355  -12.323 -3.136  1.00 46.07  ? 494 HIS A CD2 1 
ATOM   3696 C CE1 . HIS A 1 494 ? 26.479  -14.157 -2.711  1.00 45.94  ? 494 HIS A CE1 1 
ATOM   3697 N NE2 . HIS A 1 494 ? 26.604  -12.868 -2.972  1.00 45.78  ? 494 HIS A NE2 1 
ATOM   3698 N N   . ILE A 1 495 ? 23.109  -13.205 0.576   1.00 44.46  ? 495 ILE A N   1 
ATOM   3699 C CA  . ILE A 1 495 ? 23.430  -12.387 1.748   1.00 44.25  ? 495 ILE A CA  1 
ATOM   3700 C C   . ILE A 1 495 ? 24.941  -12.328 1.896   1.00 44.35  ? 495 ILE A C   1 
ATOM   3701 O O   . ILE A 1 495 ? 25.617  -13.354 1.881   1.00 43.37  ? 495 ILE A O   1 
ATOM   3702 C CB  . ILE A 1 495 ? 22.827  -12.962 3.036   1.00 44.19  ? 495 ILE A CB  1 
ATOM   3703 C CG1 . ILE A 1 495 ? 21.305  -13.076 2.912   1.00 44.10  ? 495 ILE A CG1 1 
ATOM   3704 C CG2 . ILE A 1 495 ? 23.185  -12.061 4.204   1.00 44.20  ? 495 ILE A CG2 1 
ATOM   3705 C CD1 . ILE A 1 495 ? 20.662  -14.094 3.807   1.00 44.04  ? 495 ILE A CD1 1 
ATOM   3706 N N   . THR A 1 496 ? 25.455  -11.108 2.017   1.00 44.59  ? 496 THR A N   1 
ATOM   3707 C CA  . THR A 1 496 ? 26.875  -10.873 2.227   1.00 45.09  ? 496 THR A CA  1 
ATOM   3708 C C   . THR A 1 496 ? 27.070  -10.250 3.604   1.00 45.60  ? 496 THR A C   1 
ATOM   3709 O O   . THR A 1 496 ? 26.371  -9.303  3.956   1.00 45.38  ? 496 THR A O   1 
ATOM   3710 C CB  . THR A 1 496 ? 27.433  -9.938  1.140   1.00 45.00  ? 496 THR A CB  1 
ATOM   3711 O OG1 . THR A 1 496 ? 27.449  -10.643 -0.105  1.00 44.95  ? 496 THR A OG1 1 
ATOM   3712 C CG2 . THR A 1 496 ? 28.846  -9.476  1.486   1.00 44.93  ? 496 THR A CG2 1 
ATOM   3713 N N   . ASN A 1 497 ? 27.993  -10.816 4.382   1.00 46.16  ? 497 ASN A N   1 
ATOM   3714 C CA  . ASN A 1 497 ? 28.407  -10.240 5.648   1.00 46.57  ? 497 ASN A CA  1 
ATOM   3715 C C   . ASN A 1 497 ? 29.868  -9.860  5.547   1.00 46.90  ? 497 ASN A C   1 
ATOM   3716 O O   . ASN A 1 497 ? 30.743  -10.703 5.699   1.00 46.73  ? 497 ASN A O   1 
ATOM   3717 C CB  . ASN A 1 497 ? 28.189  -11.219 6.812   1.00 46.61  ? 497 ASN A CB  1 
ATOM   3718 C CG  . ASN A 1 497 ? 28.655  -10.652 8.151   1.00 46.84  ? 497 ASN A CG  1 
ATOM   3719 O OD1 . ASN A 1 497 ? 28.934  -9.453  8.267   1.00 46.75  ? 497 ASN A OD1 1 
ATOM   3720 N ND2 . ASN A 1 497 ? 28.747  -11.517 9.168   1.00 47.96  ? 497 ASN A ND2 1 
ATOM   3721 N N   . ASN A 1 498 ? 30.119  -8.583  5.280   1.00 47.58  ? 498 ASN A N   1 
ATOM   3722 C CA  . ASN A 1 498 ? 31.481  -8.075  5.179   1.00 47.87  ? 498 ASN A CA  1 
ATOM   3723 C C   . ASN A 1 498 ? 32.021  -7.505  6.495   1.00 48.08  ? 498 ASN A C   1 
ATOM   3724 O O   . ASN A 1 498 ? 32.989  -6.754  6.481   1.00 48.45  ? 498 ASN A O   1 
ATOM   3725 C CB  . ASN A 1 498 ? 31.565  -7.014  4.080   1.00 47.93  ? 498 ASN A CB  1 
ATOM   3726 C CG  . ASN A 1 498 ? 32.994  -6.650  3.736   1.00 48.36  ? 498 ASN A CG  1 
ATOM   3727 O OD1 . ASN A 1 498 ? 33.851  -7.529  3.590   1.00 49.30  ? 498 ASN A OD1 1 
ATOM   3728 N ND2 . ASN A 1 498 ? 33.268  -5.348  3.619   1.00 49.60  ? 498 ASN A ND2 1 
ATOM   3729 N N   . THR A 1 499 ? 31.414  -7.865  7.626   1.00 48.38  ? 499 THR A N   1 
ATOM   3730 C CA  . THR A 1 499 ? 31.879  -7.399  8.935   1.00 48.61  ? 499 THR A CA  1 
ATOM   3731 C C   . THR A 1 499 ? 32.607  -8.506  9.692   1.00 48.85  ? 499 THR A C   1 
ATOM   3732 O O   . THR A 1 499 ? 32.617  -9.666  9.272   1.00 48.61  ? 499 THR A O   1 
ATOM   3733 C CB  . THR A 1 499 ? 30.721  -6.894  9.817   1.00 48.53  ? 499 THR A CB  1 
ATOM   3734 O OG1 . THR A 1 499 ? 30.021  -8.009  10.387  1.00 48.83  ? 499 THR A OG1 1 
ATOM   3735 C CG2 . THR A 1 499 ? 29.762  -6.038  9.007   1.00 48.25  ? 499 THR A CG2 1 
ATOM   3736 N N   . ALA A 1 500 ? 33.204  -8.125  10.821  1.00 49.35  ? 500 ALA A N   1 
ATOM   3737 C CA  . ALA A 1 500 ? 33.974  -9.044  11.651  1.00 49.63  ? 500 ALA A CA  1 
ATOM   3738 C C   . ALA A 1 500 ? 33.104  -9.812  12.637  1.00 49.92  ? 500 ALA A C   1 
ATOM   3739 O O   . ALA A 1 500 ? 33.611  -10.659 13.364  1.00 50.30  ? 500 ALA A O   1 
ATOM   3740 C CB  . ALA A 1 500 ? 35.068  -8.283  12.403  1.00 49.67  ? 500 ALA A CB  1 
ATOM   3741 N N   . GLU A 1 501 ? 31.804  -9.529  12.658  1.00 50.37  ? 501 GLU A N   1 
ATOM   3742 C CA  . GLU A 1 501 ? 30.903  -10.113 13.651  1.00 50.61  ? 501 GLU A CA  1 
ATOM   3743 C C   . GLU A 1 501 ? 29.975  -11.175 13.077  1.00 50.79  ? 501 GLU A C   1 
ATOM   3744 O O   . GLU A 1 501 ? 29.591  -11.118 11.913  1.00 50.75  ? 501 GLU A O   1 
ATOM   3745 C CB  . GLU A 1 501 ? 30.073  -9.014  14.320  1.00 50.82  ? 501 GLU A CB  1 
ATOM   3746 C CG  . GLU A 1 501 ? 30.805  -8.328  15.489  1.00 50.73  ? 501 GLU A CG  1 
ATOM   3747 C CD  . GLU A 1 501 ? 30.310  -6.921  15.764  1.00 51.08  ? 501 GLU A CD  1 
ATOM   3748 O OE1 . GLU A 1 501 ? 29.326  -6.492  15.118  1.00 52.33  ? 501 GLU A OE1 1 
ATOM   3749 O OE2 . GLU A 1 501 ? 30.916  -6.235  16.620  1.00 51.21  ? 501 GLU A OE2 1 
ATOM   3750 N N   . GLU A 1 502 ? 29.646  -12.150 13.924  1.00 51.00  ? 502 GLU A N   1 
ATOM   3751 C CA  . GLU A 1 502 ? 28.647  -13.165 13.629  1.00 50.95  ? 502 GLU A CA  1 
ATOM   3752 C C   . GLU A 1 502 ? 27.273  -12.550 13.777  1.00 50.72  ? 502 GLU A C   1 
ATOM   3753 O O   . GLU A 1 502 ? 27.080  -11.639 14.576  1.00 50.38  ? 502 GLU A O   1 
ATOM   3754 C CB  . GLU A 1 502 ? 28.792  -14.355 14.588  1.00 50.90  ? 502 GLU A CB  1 
ATOM   3755 C CG  . GLU A 1 502 ? 27.952  -15.558 14.194  1.00 51.46  ? 502 GLU A CG  1 
ATOM   3756 C CD  . GLU A 1 502 ? 28.192  -16.762 15.071  1.00 51.49  ? 502 GLU A CD  1 
ATOM   3757 O OE1 . GLU A 1 502 ? 28.091  -16.633 16.310  1.00 53.89  ? 502 GLU A OE1 1 
ATOM   3758 O OE2 . GLU A 1 502 ? 28.479  -17.842 14.521  1.00 53.12  ? 502 GLU A OE2 1 
ATOM   3759 N N   . TYR A 1 503 ? 26.330  -13.042 12.984  1.00 50.94  ? 503 TYR A N   1 
ATOM   3760 C CA  . TYR A 1 503 ? 24.943  -12.590 13.037  1.00 51.00  ? 503 TYR A CA  1 
ATOM   3761 C C   . TYR A 1 503 ? 24.019  -13.783 13.072  1.00 51.02  ? 503 TYR A C   1 
ATOM   3762 O O   . TYR A 1 503 ? 24.237  -14.753 12.354  1.00 51.35  ? 503 TYR A O   1 
ATOM   3763 C CB  . TYR A 1 503 ? 24.604  -11.737 11.817  1.00 52.01  ? 503 TYR A CB  1 
ATOM   3764 C CG  . TYR A 1 503 ? 25.062  -10.303 11.922  1.00 52.34  ? 503 TYR A CG  1 
ATOM   3765 C CD1 . TYR A 1 503 ? 25.945  -9.762  10.991  1.00 52.73  ? 503 TYR A CD1 1 
ATOM   3766 C CD2 . TYR A 1 503 ? 24.617  -9.491  12.960  1.00 53.70  ? 503 TYR A CD2 1 
ATOM   3767 C CE1 . TYR A 1 503 ? 26.372  -8.440  11.094  1.00 53.60  ? 503 TYR A CE1 1 
ATOM   3768 C CE2 . TYR A 1 503 ? 25.043  -8.177  13.081  1.00 52.71  ? 503 TYR A CE2 1 
ATOM   3769 C CZ  . TYR A 1 503 ? 25.916  -7.652  12.142  1.00 53.21  ? 503 TYR A CZ  1 
ATOM   3770 O OH  . TYR A 1 503 ? 26.331  -6.340  12.252  1.00 53.73  ? 503 TYR A OH  1 
ATOM   3771 N N   . VAL A 1 504 ? 22.991  -13.722 13.907  1.00 50.44  ? 504 VAL A N   1 
ATOM   3772 C CA  . VAL A 1 504 ? 21.935  -14.728 13.869  1.00 50.27  ? 504 VAL A CA  1 
ATOM   3773 C C   . VAL A 1 504 ? 20.677  -13.999 13.465  1.00 49.80  ? 504 VAL A C   1 
ATOM   3774 O O   . VAL A 1 504 ? 20.253  -13.042 14.123  1.00 48.99  ? 504 VAL A O   1 
ATOM   3775 C CB  . VAL A 1 504 ? 21.736  -15.450 15.211  1.00 50.54  ? 504 VAL A CB  1 
ATOM   3776 C CG1 . VAL A 1 504 ? 20.818  -16.680 15.017  1.00 50.44  ? 504 VAL A CG1 1 
ATOM   3777 C CG2 . VAL A 1 504 ? 23.072  -15.853 15.774  1.00 50.10  ? 504 VAL A CG2 1 
ATOM   3778 N N   . CYS A 1 505 ? 20.105  -14.436 12.352  1.00 49.00  ? 505 CYS A N   1 
ATOM   3779 C CA  . CYS A 1 505 ? 18.994  -13.750 11.751  1.00 49.25  ? 505 CYS A CA  1 
ATOM   3780 C C   . CYS A 1 505 ? 17.873  -14.685 11.447  1.00 48.72  ? 505 CYS A C   1 
ATOM   3781 O O   . CYS A 1 505 ? 18.045  -15.910 11.386  1.00 49.60  ? 505 CYS A O   1 
ATOM   3782 C CB  . CYS A 1 505 ? 19.412  -13.101 10.444  1.00 49.33  ? 505 CYS A CB  1 
ATOM   3783 S SG  . CYS A 1 505 ? 20.620  -11.872 10.676  1.00 52.49  ? 505 CYS A SG  1 
ATOM   3784 N N   . ARG A 1 506 ? 16.714  -14.071 11.289  1.00 47.78  ? 506 ARG A N   1 
ATOM   3785 C CA  . ARG A 1 506 ? 15.539  -14.729 10.787  1.00 47.43  ? 506 ARG A CA  1 
ATOM   3786 C C   . ARG A 1 506 ? 15.460  -14.281 9.338   1.00 46.36  ? 506 ARG A C   1 
ATOM   3787 O O   . ARG A 1 506 ? 15.762  -13.126 9.025   1.00 45.67  ? 506 ARG A O   1 
ATOM   3788 C CB  . ARG A 1 506 ? 14.312  -14.288 11.568  1.00 47.66  ? 506 ARG A CB  1 
ATOM   3789 C CG  . ARG A 1 506 ? 14.634  -14.053 13.068  1.00 49.17  ? 506 ARG A CG  1 
ATOM   3790 C CD  . ARG A 1 506 ? 13.519  -14.464 13.982  1.00 49.45  ? 506 ARG A CD  1 
ATOM   3791 N NE  . ARG A 1 506 ? 13.836  -14.224 15.393  1.00 49.58  ? 506 ARG A NE  1 
ATOM   3792 C CZ  . ARG A 1 506 ? 14.689  -14.937 16.129  1.00 50.77  ? 506 ARG A CZ  1 
ATOM   3793 N NH1 . ARG A 1 506 ? 15.358  -15.962 15.608  1.00 52.78  ? 506 ARG A NH1 1 
ATOM   3794 N NH2 . ARG A 1 506 ? 14.877  -14.632 17.409  1.00 47.76  ? 506 ARG A NH2 1 
ATOM   3795 N N   . LEU A 1 507 ? 15.090  -15.198 8.468   1.00 45.97  ? 507 LEU A N   1 
ATOM   3796 C CA  . LEU A 1 507 ? 14.950  -14.869 7.032   1.00 45.77  ? 507 LEU A CA  1 
ATOM   3797 C C   . LEU A 1 507 ? 13.583  -15.287 6.543   1.00 45.53  ? 507 LEU A C   1 
ATOM   3798 O O   . LEU A 1 507 ? 13.142  -16.399 6.822   1.00 45.98  ? 507 LEU A O   1 
ATOM   3799 C CB  . LEU A 1 507 ? 16.021  -15.581 6.209   1.00 45.46  ? 507 LEU A CB  1 
ATOM   3800 C CG  . LEU A 1 507 ? 15.983  -15.294 4.678   1.00 45.29  ? 507 LEU A CG  1 
ATOM   3801 C CD1 . LEU A 1 507 ? 16.467  -13.911 4.383   1.00 44.04  ? 507 LEU A CD1 1 
ATOM   3802 C CD2 . LEU A 1 507 ? 16.812  -16.326 3.960   1.00 45.11  ? 507 LEU A CD2 1 
ATOM   3803 N N   . LEU A 1 508 ? 12.913  -14.380 5.827   1.00 46.41  ? 508 LEU A N   1 
ATOM   3804 C CA  . LEU A 1 508 ? 11.700  -14.691 5.119   1.00 46.12  ? 508 LEU A CA  1 
ATOM   3805 C C   . LEU A 1 508 ? 12.038  -14.449 3.657   1.00 45.91  ? 508 LEU A C   1 
ATOM   3806 O O   . LEU A 1 508 ? 12.452  -13.362 3.311   1.00 45.80  ? 508 LEU A O   1 
ATOM   3807 C CB  . LEU A 1 508 ? 10.572  -13.750 5.505   1.00 46.38  ? 508 LEU A CB  1 
ATOM   3808 C CG  . LEU A 1 508 ? 9.129   -14.271 5.430   1.00 46.80  ? 508 LEU A CG  1 
ATOM   3809 C CD1 . LEU A 1 508 ? 8.185   -13.092 5.240   1.00 46.31  ? 508 LEU A CD1 1 
ATOM   3810 C CD2 . LEU A 1 508 ? 8.859   -15.385 4.401   1.00 49.04  ? 508 LEU A CD2 1 
ATOM   3811 N N   . LEU A 1 509 ? 11.877  -15.479 2.841   1.00 45.84  ? 509 LEU A N   1 
ATOM   3812 C CA  . LEU A 1 509 ? 12.122  -15.428 1.402   1.00 46.10  ? 509 LEU A CA  1 
ATOM   3813 C C   . LEU A 1 509 ? 10.896  -16.006 0.726   1.00 45.95  ? 509 LEU A C   1 
ATOM   3814 O O   . LEU A 1 509 ? 10.577  -17.164 0.953   1.00 45.66  ? 509 LEU A O   1 
ATOM   3815 C CB  . LEU A 1 509 ? 13.350  -16.277 1.052   1.00 45.74  ? 509 LEU A CB  1 
ATOM   3816 C CG  . LEU A 1 509 ? 13.756  -16.487 -0.413  1.00 46.15  ? 509 LEU A CG  1 
ATOM   3817 C CD1 . LEU A 1 509 ? 13.997  -15.153 -1.113  1.00 43.56  ? 509 LEU A CD1 1 
ATOM   3818 C CD2 . LEU A 1 509 ? 15.000  -17.420 -0.512  1.00 45.28  ? 509 LEU A CD2 1 
ATOM   3819 N N   . CYS A 1 510 ? 10.213  -15.206 -0.096  1.00 46.15  ? 510 CYS A N   1 
ATOM   3820 C CA  . CYS A 1 510 ? 9.041   -15.702 -0.810  1.00 46.55  ? 510 CYS A CA  1 
ATOM   3821 C C   . CYS A 1 510 ? 8.857   -15.068 -2.179  1.00 45.93  ? 510 CYS A C   1 
ATOM   3822 O O   . CYS A 1 510 ? 9.429   -14.023 -2.486  1.00 45.38  ? 510 CYS A O   1 
ATOM   3823 C CB  . CYS A 1 510 ? 7.788   -15.435 -0.007  1.00 46.40  ? 510 CYS A CB  1 
ATOM   3824 S SG  . CYS A 1 510 ? 7.588   -13.718 0.328   1.00 52.58  ? 510 CYS A SG  1 
ATOM   3825 N N   . ALA A 1 511 ? 7.999   -15.705 -2.967  1.00 46.02  ? 511 ALA A N   1 
ATOM   3826 C CA  . ALA A 1 511 ? 7.684   -15.273 -4.329  1.00 46.52  ? 511 ALA A CA  1 
ATOM   3827 C C   . ALA A 1 511 ? 6.168   -15.224 -4.512  1.00 46.40  ? 511 ALA A C   1 
ATOM   3828 O O   . ALA A 1 511 ? 5.436   -16.085 -4.000  1.00 46.17  ? 511 ALA A O   1 
ATOM   3829 C CB  . ALA A 1 511 ? 8.324   -16.231 -5.334  1.00 45.61  ? 511 ALA A CB  1 
ATOM   3830 N N   . ARG A 1 512 ? 5.713   -14.190 -5.217  1.00 46.77  ? 512 ARG A N   1 
ATOM   3831 C CA  . ARG A 1 512 ? 4.313   -14.031 -5.612  1.00 46.93  ? 512 ARG A CA  1 
ATOM   3832 C C   . ARG A 1 512 ? 4.291   -13.535 -7.047  1.00 46.06  ? 512 ARG A C   1 
ATOM   3833 O O   . ARG A 1 512 ? 5.192   -12.814 -7.480  1.00 44.99  ? 512 ARG A O   1 
ATOM   3834 C CB  . ARG A 1 512 ? 3.581   -13.021 -4.721  1.00 47.05  ? 512 ARG A CB  1 
ATOM   3835 C CG  . ARG A 1 512 ? 3.133   -13.610 -3.388  1.00 49.07  ? 512 ARG A CG  1 
ATOM   3836 C CD  . ARG A 1 512 ? 2.674   -12.572 -2.376  1.00 49.90  ? 512 ARG A CD  1 
ATOM   3837 N NE  . ARG A 1 512 ? 1.317   -12.104 -2.646  1.00 53.15  ? 512 ARG A NE  1 
ATOM   3838 C CZ  . ARG A 1 512 ? 0.590   -11.366 -1.806  1.00 54.04  ? 512 ARG A CZ  1 
ATOM   3839 N NH1 . ARG A 1 512 ? 1.082   -11.002 -0.619  1.00 55.69  ? 512 ARG A NH1 1 
ATOM   3840 N NH2 . ARG A 1 512 ? -0.637  -10.986 -2.148  1.00 53.63  ? 512 ARG A NH2 1 
ATOM   3841 N N   . THR A 1 513 ? 3.254   -13.919 -7.775  1.00 46.05  ? 513 THR A N   1 
ATOM   3842 C CA  . THR A 1 513 ? 3.048   -13.404 -9.125  1.00 46.23  ? 513 THR A CA  1 
ATOM   3843 C C   . THR A 1 513 ? 2.721   -11.925 -9.023  1.00 45.93  ? 513 THR A C   1 
ATOM   3844 O O   . THR A 1 513 ? 2.247   -11.454 -7.985  1.00 45.38  ? 513 THR A O   1 
ATOM   3845 C CB  . THR A 1 513 ? 1.931   -14.164 -9.869  1.00 46.16  ? 513 THR A CB  1 
ATOM   3846 O OG1 . THR A 1 513 ? 0.699   -14.047 -9.147  1.00 47.16  ? 513 THR A OG1 1 
ATOM   3847 C CG2 . THR A 1 513 ? 2.304   -15.648 -10.032 1.00 46.41  ? 513 THR A CG2 1 
ATOM   3848 N N   . VAL A 1 514 ? 2.997   -11.186 -10.096 1.00 46.10  ? 514 VAL A N   1 
ATOM   3849 C CA  . VAL A 1 514 ? 2.659   -9.768  -10.142 1.00 45.96  ? 514 VAL A CA  1 
ATOM   3850 C C   . VAL A 1 514 ? 2.253   -9.356  -11.575 1.00 46.29  ? 514 VAL A C   1 
ATOM   3851 O O   . VAL A 1 514 ? 2.774   -9.894  -12.560 1.00 45.67  ? 514 VAL A O   1 
ATOM   3852 C CB  . VAL A 1 514 ? 3.809   -8.900  -9.532  1.00 45.88  ? 514 VAL A CB  1 
ATOM   3853 C CG1 . VAL A 1 514 ? 5.111   -9.046  -10.322 1.00 45.70  ? 514 VAL A CG1 1 
ATOM   3854 C CG2 . VAL A 1 514 ? 3.390   -7.446  -9.387  1.00 45.62  ? 514 VAL A CG2 1 
ATOM   3855 N N   . SER A 1 515 ? 1.274   -8.457  -11.662 1.00 46.33  ? 515 SER A N   1 
ATOM   3856 C CA  . SER A 1 515 ? 0.810   -7.909  -12.937 1.00 46.93  ? 515 SER A CA  1 
ATOM   3857 C C   . SER A 1 515 ? 1.747   -6.817  -13.413 1.00 47.07  ? 515 SER A C   1 
ATOM   3858 O O   . SER A 1 515 ? 2.528   -6.287  -12.630 1.00 47.09  ? 515 SER A O   1 
ATOM   3859 C CB  . SER A 1 515 ? -0.589  -7.310  -12.789 1.00 47.03  ? 515 SER A CB  1 
ATOM   3860 O OG  . SER A 1 515 ? -1.589  -8.311  -12.751 1.00 48.45  ? 515 SER A OG  1 
ATOM   3861 N N   . TYR A 1 516 ? 1.649   -6.466  -14.697 1.00 48.03  ? 516 TYR A N   1 
ATOM   3862 C CA  . TYR A 1 516 ? 2.426   -5.352  -15.249 1.00 48.20  ? 516 TYR A CA  1 
ATOM   3863 C C   . TYR A 1 516 ? 2.132   -4.028  -14.534 1.00 48.29  ? 516 TYR A C   1 
ATOM   3864 O O   . TYR A 1 516 ? 3.019   -3.190  -14.418 1.00 48.32  ? 516 TYR A O   1 
ATOM   3865 C CB  . TYR A 1 516 ? 2.195   -5.189  -16.766 1.00 49.14  ? 516 TYR A CB  1 
ATOM   3866 C CG  . TYR A 1 516 ? 3.189   -5.925  -17.641 1.00 49.30  ? 516 TYR A CG  1 
ATOM   3867 C CD1 . TYR A 1 516 ? 4.554   -5.866  -17.387 1.00 49.91  ? 516 TYR A CD1 1 
ATOM   3868 C CD2 . TYR A 1 516 ? 2.770   -6.638  -18.748 1.00 50.82  ? 516 TYR A CD2 1 
ATOM   3869 C CE1 . TYR A 1 516 ? 5.465   -6.524  -18.187 1.00 50.03  ? 516 TYR A CE1 1 
ATOM   3870 C CE2 . TYR A 1 516 ? 3.682   -7.307  -19.560 1.00 50.87  ? 516 TYR A CE2 1 
ATOM   3871 C CZ  . TYR A 1 516 ? 5.030   -7.242  -19.270 1.00 50.65  ? 516 TYR A CZ  1 
ATOM   3872 O OH  . TYR A 1 516 ? 5.948   -7.904  -20.058 1.00 51.14  ? 516 TYR A OH  1 
ATOM   3873 N N   . ASN A 1 517 ? 0.895   -3.842  -14.072 1.00 48.16  ? 517 ASN A N   1 
ATOM   3874 C CA  . ASN A 1 517 ? 0.532   -2.648  -13.300 1.00 48.29  ? 517 ASN A CA  1 
ATOM   3875 C C   . ASN A 1 517 ? 0.766   -2.768  -11.775 1.00 48.46  ? 517 ASN A C   1 
ATOM   3876 O O   . ASN A 1 517 ? 0.296   -1.931  -11.007 1.00 48.57  ? 517 ASN A O   1 
ATOM   3877 C CB  . ASN A 1 517 ? -0.906  -2.197  -13.610 1.00 48.39  ? 517 ASN A CB  1 
ATOM   3878 C CG  . ASN A 1 517 ? -1.926  -3.321  -13.527 1.00 48.36  ? 517 ASN A CG  1 
ATOM   3879 O OD1 . ASN A 1 517 ? -1.593  -4.463  -13.216 1.00 49.87  ? 517 ASN A OD1 1 
ATOM   3880 N ND2 . ASN A 1 517 ? -3.188  -2.992  -13.814 1.00 48.19  ? 517 ASN A ND2 1 
ATOM   3881 N N   . GLY A 1 518 ? 1.490   -3.799  -11.346 1.00 48.39  ? 518 GLY A N   1 
ATOM   3882 C CA  . GLY A 1 518 ? 1.977   -3.874  -9.970  1.00 48.82  ? 518 GLY A CA  1 
ATOM   3883 C C   . GLY A 1 518 ? 1.061   -4.550  -8.961  1.00 49.09  ? 518 GLY A C   1 
ATOM   3884 O O   . GLY A 1 518 ? 1.241   -4.383  -7.748  1.00 50.17  ? 518 GLY A O   1 
ATOM   3885 N N   . ILE A 1 519 ? 0.100   -5.333  -9.449  1.00 49.02  ? 519 ILE A N   1 
ATOM   3886 C CA  . ILE A 1 519 ? -0.831  -6.061  -8.584  1.00 48.67  ? 519 ILE A CA  1 
ATOM   3887 C C   . ILE A 1 519 ? -0.233  -7.420  -8.192  1.00 48.66  ? 519 ILE A C   1 
ATOM   3888 O O   . ILE A 1 519 ? 0.006   -8.277  -9.049  1.00 48.63  ? 519 ILE A O   1 
ATOM   3889 C CB  . ILE A 1 519 ? -2.205  -6.268  -9.273  1.00 48.67  ? 519 ILE A CB  1 
ATOM   3890 C CG1 . ILE A 1 519 ? -2.793  -4.930  -9.723  1.00 48.53  ? 519 ILE A CG1 1 
ATOM   3891 C CG2 . ILE A 1 519 ? -3.177  -6.957  -8.333  1.00 48.72  ? 519 ILE A CG2 1 
ATOM   3892 C CD1 . ILE A 1 519 ? -3.966  -5.060  -10.702 1.00 48.48  ? 519 ILE A CD1 1 
ATOM   3893 N N   . LEU A 1 520 ? 0.014   -7.601  -6.894  1.00 48.37  ? 520 LEU A N   1 
ATOM   3894 C CA  . LEU A 1 520 ? 0.502   -8.870  -6.358  1.00 48.18  ? 520 LEU A CA  1 
ATOM   3895 C C   . LEU A 1 520 ? -0.582  -9.948  -6.341  1.00 47.92  ? 520 LEU A C   1 
ATOM   3896 O O   . LEU A 1 520 ? -1.632  -9.765  -5.740  1.00 48.18  ? 520 LEU A O   1 
ATOM   3897 C CB  . LEU A 1 520 ? 1.051   -8.684  -4.934  1.00 48.43  ? 520 LEU A CB  1 
ATOM   3898 C CG  . LEU A 1 520 ? 2.520   -8.264  -4.791  1.00 49.39  ? 520 LEU A CG  1 
ATOM   3899 C CD1 . LEU A 1 520 ? 2.968   -8.266  -3.323  1.00 49.83  ? 520 LEU A CD1 1 
ATOM   3900 C CD2 . LEU A 1 520 ? 3.437   -9.171  -5.600  1.00 49.28  ? 520 LEU A CD2 1 
ATOM   3901 N N   . GLY A 1 521 ? -0.309  -11.075 -6.994  1.00 47.64  ? 521 GLY A N   1 
ATOM   3902 C CA  . GLY A 1 521 ? -1.194  -12.238 -6.974  1.00 47.41  ? 521 GLY A CA  1 
ATOM   3903 C C   . GLY A 1 521 ? -0.760  -13.231 -5.911  1.00 47.19  ? 521 GLY A C   1 
ATOM   3904 O O   . GLY A 1 521 ? 0.040   -12.894 -5.043  1.00 47.28  ? 521 GLY A O   1 
ATOM   3905 N N   . PRO A 1 522 ? -1.285  -14.465 -5.965  1.00 46.98  ? 522 PRO A N   1 
ATOM   3906 C CA  . PRO A 1 522 ? -0.963  -15.495 -4.972  1.00 47.13  ? 522 PRO A CA  1 
ATOM   3907 C C   . PRO A 1 522 ? 0.505   -15.959 -4.899  1.00 47.34  ? 522 PRO A C   1 
ATOM   3908 O O   . PRO A 1 522 ? 1.233   -15.912 -5.889  1.00 47.32  ? 522 PRO A O   1 
ATOM   3909 C CB  . PRO A 1 522 ? -1.861  -16.669 -5.385  1.00 47.03  ? 522 PRO A CB  1 
ATOM   3910 C CG  . PRO A 1 522 ? -2.923  -16.073 -6.222  1.00 46.69  ? 522 PRO A CG  1 
ATOM   3911 C CD  . PRO A 1 522 ? -2.271  -14.950 -6.941  1.00 46.83  ? 522 PRO A CD  1 
ATOM   3912 N N   . GLU A 1 523 ? 0.892   -16.420 -3.710  1.00 47.71  ? 523 GLU A N   1 
ATOM   3913 C CA  . GLU A 1 523 ? 2.214   -16.986 -3.415  1.00 47.35  ? 523 GLU A CA  1 
ATOM   3914 C C   . GLU A 1 523 ? 2.539   -18.197 -4.291  1.00 47.06  ? 523 GLU A C   1 
ATOM   3915 O O   . GLU A 1 523 ? 1.689   -19.054 -4.524  1.00 47.28  ? 523 GLU A O   1 
ATOM   3916 C CB  . GLU A 1 523 ? 2.265   -17.363 -1.929  1.00 47.82  ? 523 GLU A CB  1 
ATOM   3917 C CG  . GLU A 1 523 ? 3.556   -18.054 -1.445  1.00 49.38  ? 523 GLU A CG  1 
ATOM   3918 C CD  . GLU A 1 523 ? 3.420   -19.578 -1.254  1.00 52.02  ? 523 GLU A CD  1 
ATOM   3919 O OE1 . GLU A 1 523 ? 2.408   -20.053 -0.699  1.00 55.07  ? 523 GLU A OE1 1 
ATOM   3920 O OE2 . GLU A 1 523 ? 4.344   -20.314 -1.633  1.00 54.07  ? 523 GLU A OE2 1 
ATOM   3921 N N   . CYS A 1 524 ? 3.764   -18.244 -4.805  1.00 46.75  ? 524 CYS A N   1 
ATOM   3922 C CA  . CYS A 1 524 ? 4.239   -19.406 -5.557  1.00 46.21  ? 524 CYS A CA  1 
ATOM   3923 C C   . CYS A 1 524 ? 5.572   -19.916 -5.003  1.00 46.05  ? 524 CYS A C   1 
ATOM   3924 O O   . CYS A 1 524 ? 6.414   -20.413 -5.752  1.00 46.55  ? 524 CYS A O   1 
ATOM   3925 C CB  . CYS A 1 524 ? 4.362   -19.066 -7.048  1.00 46.14  ? 524 CYS A CB  1 
ATOM   3926 S SG  . CYS A 1 524 ? 5.197   -17.525 -7.394  1.00 46.48  ? 524 CYS A SG  1 
ATOM   3927 N N   . GLY A 1 525 ? 5.759   -19.790 -3.692  1.00 45.18  ? 525 GLY A N   1 
ATOM   3928 C CA  . GLY A 1 525 ? 6.954   -20.322 -3.008  1.00 44.50  ? 525 GLY A CA  1 
ATOM   3929 C C   . GLY A 1 525 ? 7.321   -19.474 -1.803  1.00 44.26  ? 525 GLY A C   1 
ATOM   3930 O O   . GLY A 1 525 ? 7.261   -18.245 -1.871  1.00 43.04  ? 525 GLY A O   1 
ATOM   3931 N N   . THR A 1 526 ? 7.695   -20.130 -0.699  1.00 43.80  ? 526 THR A N   1 
ATOM   3932 C CA  . THR A 1 526 ? 8.021   -19.437 0.551   1.00 43.97  ? 526 THR A CA  1 
ATOM   3933 C C   . THR A 1 526 ? 9.068   -20.244 1.308   1.00 43.85  ? 526 THR A C   1 
ATOM   3934 O O   . THR A 1 526 ? 9.046   -21.466 1.288   1.00 42.29  ? 526 THR A O   1 
ATOM   3935 C CB  . THR A 1 526 ? 6.755   -19.229 1.427   1.00 44.12  ? 526 THR A CB  1 
ATOM   3936 O OG1 . THR A 1 526 ? 5.844   -18.364 0.733   1.00 47.11  ? 526 THR A OG1 1 
ATOM   3937 C CG2 . THR A 1 526 ? 7.095   -18.567 2.765   1.00 44.01  ? 526 THR A CG2 1 
ATOM   3938 N N   . LYS A 1 527 ? 10.021  -19.557 1.922   1.00 44.22  ? 527 LYS A N   1 
ATOM   3939 C CA  . LYS A 1 527 ? 10.976  -20.216 2.819   1.00 45.11  ? 527 LYS A CA  1 
ATOM   3940 C C   . LYS A 1 527 ? 11.196  -19.304 4.021   1.00 45.48  ? 527 LYS A C   1 
ATOM   3941 O O   . LYS A 1 527 ? 11.479  -18.103 3.882   1.00 44.58  ? 527 LYS A O   1 
ATOM   3942 C CB  . LYS A 1 527 ? 12.294  -20.518 2.101   1.00 45.42  ? 527 LYS A CB  1 
ATOM   3943 C CG  . LYS A 1 527 ? 13.411  -21.048 2.992   1.00 44.43  ? 527 LYS A CG  1 
ATOM   3944 C CD  . LYS A 1 527 ? 14.671  -21.285 2.178   1.00 44.94  ? 527 LYS A CD  1 
ATOM   3945 C CE  . LYS A 1 527 ? 15.818  -21.790 3.077   1.00 44.78  ? 527 LYS A CE  1 
ATOM   3946 N NZ  . LYS A 1 527 ? 15.582  -23.164 3.561   1.00 41.91  ? 527 LYS A NZ  1 
ATOM   3947 N N   . TYR A 1 528 ? 10.993  -19.886 5.192   1.00 46.66  ? 528 TYR A N   1 
ATOM   3948 C CA  . TYR A 1 528 ? 11.245  -19.209 6.466   1.00 46.93  ? 528 TYR A CA  1 
ATOM   3949 C C   . TYR A 1 528 ? 12.352  -19.959 7.210   1.00 47.05  ? 528 TYR A C   1 
ATOM   3950 O O   . TYR A 1 528 ? 12.323  -21.188 7.321   1.00 46.80  ? 528 TYR A O   1 
ATOM   3951 C CB  . TYR A 1 528 ? 9.969   -19.127 7.316   1.00 47.66  ? 528 TYR A CB  1 
ATOM   3952 C CG  . TYR A 1 528 ? 10.205  -18.440 8.649   1.00 47.68  ? 528 TYR A CG  1 
ATOM   3953 C CD1 . TYR A 1 528 ? 10.171  -19.153 9.848   1.00 49.05  ? 528 TYR A CD1 1 
ATOM   3954 C CD2 . TYR A 1 528 ? 10.552  -17.110 8.696   1.00 49.76  ? 528 TYR A CD2 1 
ATOM   3955 C CE1 . TYR A 1 528 ? 10.422  -18.530 11.068  1.00 49.93  ? 528 TYR A CE1 1 
ATOM   3956 C CE2 . TYR A 1 528 ? 10.793  -16.466 9.911   1.00 50.22  ? 528 TYR A CE2 1 
ATOM   3957 C CZ  . TYR A 1 528 ? 10.734  -17.183 11.082  1.00 49.76  ? 528 TYR A CZ  1 
ATOM   3958 O OH  . TYR A 1 528 ? 10.978  -16.530 12.271  1.00 51.15  ? 528 TYR A OH  1 
ATOM   3959 N N   . LEU A 1 529 ? 13.326  -19.196 7.696   1.00 47.61  ? 529 LEU A N   1 
ATOM   3960 C CA  . LEU A 1 529 ? 14.430  -19.682 8.518   1.00 48.25  ? 529 LEU A CA  1 
ATOM   3961 C C   . LEU A 1 529 ? 14.505  -18.891 9.838   1.00 48.17  ? 529 LEU A C   1 
ATOM   3962 O O   . LEU A 1 529 ? 14.979  -17.759 9.855   1.00 48.99  ? 529 LEU A O   1 
ATOM   3963 C CB  . LEU A 1 529 ? 15.742  -19.447 7.774   1.00 48.70  ? 529 LEU A CB  1 
ATOM   3964 C CG  . LEU A 1 529 ? 16.364  -20.589 6.976   1.00 51.63  ? 529 LEU A CG  1 
ATOM   3965 C CD1 . LEU A 1 529 ? 17.295  -20.001 5.898   1.00 52.32  ? 529 LEU A CD1 1 
ATOM   3966 C CD2 . LEU A 1 529 ? 17.098  -21.513 7.916   1.00 51.23  ? 529 LEU A CD2 1 
ATOM   3967 N N   . LEU A 1 530 ? 14.057  -19.483 10.934  1.00 48.22  ? 530 LEU A N   1 
ATOM   3968 C CA  . LEU A 1 530 ? 14.186  -18.867 12.260  1.00 47.92  ? 530 LEU A CA  1 
ATOM   3969 C C   . LEU A 1 530 ? 15.639  -18.501 12.609  1.00 47.14  ? 530 LEU A C   1 
ATOM   3970 O O   . LEU A 1 530 ? 15.886  -17.440 13.162  1.00 46.54  ? 530 LEU A O   1 
ATOM   3971 C CB  . LEU A 1 530 ? 13.602  -19.796 13.330  1.00 48.21  ? 530 LEU A CB  1 
ATOM   3972 C CG  . LEU A 1 530 ? 13.154  -19.180 14.672  1.00 49.55  ? 530 LEU A CG  1 
ATOM   3973 C CD1 . LEU A 1 530 ? 14.329  -18.832 15.545  1.00 51.79  ? 530 LEU A CD1 1 
ATOM   3974 C CD2 . LEU A 1 530 ? 12.294  -17.949 14.475  1.00 51.87  ? 530 LEU A CD2 1 
ATOM   3975 N N   . ASN A 1 531 ? 16.566  -19.363 12.215  1.00 47.07  ? 531 ASN A N   1 
ATOM   3976 C CA  . ASN A 1 531 ? 17.948  -19.419 12.682  1.00 47.66  ? 531 ASN A CA  1 
ATOM   3977 C C   . ASN A 1 531 ? 18.984  -19.366 11.566  1.00 47.60  ? 531 ASN A C   1 
ATOM   3978 O O   . ASN A 1 531 ? 19.750  -20.308 11.409  1.00 49.83  ? 531 ASN A O   1 
ATOM   3979 C CB  . ASN A 1 531 ? 18.194  -20.806 13.306  1.00 47.54  ? 531 ASN A CB  1 
ATOM   3980 C CG  . ASN A 1 531 ? 17.505  -21.010 14.615  1.00 48.71  ? 531 ASN A CG  1 
ATOM   3981 O OD1 . ASN A 1 531 ? 17.212  -22.149 14.990  1.00 47.64  ? 531 ASN A OD1 1 
ATOM   3982 N ND2 . ASN A 1 531 ? 17.266  -19.935 15.333  1.00 48.63  ? 531 ASN A ND2 1 
ATOM   3983 N N   . LEU A 1 532 ? 19.034  -18.316 10.779  1.00 48.01  ? 532 LEU A N   1 
ATOM   3984 C CA  . LEU A 1 532 ? 20.099  -18.195 9.796   1.00 47.68  ? 532 LEU A CA  1 
ATOM   3985 C C   . LEU A 1 532 ? 21.322  -17.598 10.481  1.00 47.07  ? 532 LEU A C   1 
ATOM   3986 O O   . LEU A 1 532 ? 21.288  -16.458 10.959  1.00 46.33  ? 532 LEU A O   1 
ATOM   3987 C CB  . LEU A 1 532 ? 19.668  -17.316 8.624   1.00 47.21  ? 532 LEU A CB  1 
ATOM   3988 C CG  . LEU A 1 532 ? 20.162  -17.649 7.211   1.00 48.19  ? 532 LEU A CG  1 
ATOM   3989 C CD1 . LEU A 1 532 ? 20.038  -16.382 6.357   1.00 45.09  ? 532 LEU A CD1 1 
ATOM   3990 C CD2 . LEU A 1 532 ? 21.575  -18.222 7.146   1.00 46.45  ? 532 LEU A CD2 1 
ATOM   3991 N N   . THR A 1 533 ? 22.394  -18.373 10.507  1.00 47.61  ? 533 THR A N   1 
ATOM   3992 C CA  . THR A 1 533 ? 23.657  -17.953 11.099  1.00 47.90  ? 533 THR A CA  1 
ATOM   3993 C C   . THR A 1 533 ? 24.534  -17.404 9.968   1.00 47.90  ? 533 THR A C   1 
ATOM   3994 O O   . THR A 1 533 ? 24.845  -18.114 9.012   1.00 47.67  ? 533 THR A O   1 
ATOM   3995 C CB  . THR A 1 533 ? 24.385  -19.130 11.814  1.00 47.98  ? 533 THR A CB  1 
ATOM   3996 O OG1 . THR A 1 533 ? 23.892  -19.305 13.165  1.00 49.55  ? 533 THR A OG1 1 
ATOM   3997 C CG2 . THR A 1 533 ? 25.902  -18.887 11.884  1.00 48.28  ? 533 THR A CG2 1 
ATOM   3998 N N   . LEU A 1 534 ? 24.927  -16.143 10.085  1.00 47.55  ? 534 LEU A N   1 
ATOM   3999 C CA  . LEU A 1 534 ? 25.883  -15.544 9.163   1.00 47.59  ? 534 LEU A CA  1 
ATOM   4000 C C   . LEU A 1 534 ? 27.259  -15.350 9.817   1.00 47.47  ? 534 LEU A C   1 
ATOM   4001 O O   . LEU A 1 534 ? 27.436  -14.468 10.662  1.00 47.37  ? 534 LEU A O   1 
ATOM   4002 C CB  . LEU A 1 534 ? 25.326  -14.223 8.627   1.00 47.80  ? 534 LEU A CB  1 
ATOM   4003 C CG  . LEU A 1 534 ? 24.312  -14.468 7.495   1.00 47.93  ? 534 LEU A CG  1 
ATOM   4004 C CD1 . LEU A 1 534 ? 23.376  -13.316 7.371   1.00 49.92  ? 534 LEU A CD1 1 
ATOM   4005 C CD2 . LEU A 1 534 ? 25.034  -14.765 6.168   1.00 48.22  ? 534 LEU A CD2 1 
ATOM   4006 N N   . GLU A 1 535 ? 28.222  -16.182 9.413   1.00 47.18  ? 535 GLU A N   1 
ATOM   4007 C CA  . GLU A 1 535 ? 29.583  -16.144 9.951   1.00 46.97  ? 535 GLU A CA  1 
ATOM   4008 C C   . GLU A 1 535 ? 30.275  -14.843 9.533   1.00 46.53  ? 535 GLU A C   1 
ATOM   4009 O O   . GLU A 1 535 ? 29.944  -14.298 8.481   1.00 46.58  ? 535 GLU A O   1 
ATOM   4010 C CB  . GLU A 1 535 ? 30.383  -17.371 9.463   1.00 46.93  ? 535 GLU A CB  1 
ATOM   4011 C CG  . GLU A 1 535 ? 31.861  -17.374 9.863   1.00 47.78  ? 535 GLU A CG  1 
ATOM   4012 C CD  . GLU A 1 535 ? 32.462  -18.778 10.006  1.00 48.06  ? 535 GLU A CD  1 
ATOM   4013 O OE1 . GLU A 1 535 ? 32.285  -19.607 9.082   1.00 50.30  ? 535 GLU A OE1 1 
ATOM   4014 O OE2 . GLU A 1 535 ? 33.119  -19.043 11.041  1.00 48.48  ? 535 GLU A OE2 1 
ATOM   4015 N N   . PRO A 1 536 ? 31.192  -14.306 10.376  1.00 45.89  ? 536 PRO A N   1 
ATOM   4016 C CA  . PRO A 1 536 ? 32.055  -13.195 9.953   1.00 45.51  ? 536 PRO A CA  1 
ATOM   4017 C C   . PRO A 1 536 ? 32.661  -13.348 8.558   1.00 44.98  ? 536 PRO A C   1 
ATOM   4018 O O   . PRO A 1 536 ? 32.964  -14.462 8.130   1.00 44.61  ? 536 PRO A O   1 
ATOM   4019 C CB  . PRO A 1 536 ? 33.181  -13.184 11.004  1.00 45.45  ? 536 PRO A CB  1 
ATOM   4020 C CG  . PRO A 1 536 ? 32.803  -14.171 12.039  1.00 45.74  ? 536 PRO A CG  1 
ATOM   4021 C CD  . PRO A 1 536 ? 31.406  -14.616 11.798  1.00 45.92  ? 536 PRO A CD  1 
ATOM   4022 N N   . PHE A 1 537 ? 32.814  -12.215 7.875   1.00 44.67  ? 537 PHE A N   1 
ATOM   4023 C CA  . PHE A 1 537 ? 33.421  -12.140 6.546   1.00 44.23  ? 537 PHE A CA  1 
ATOM   4024 C C   . PHE A 1 537 ? 33.033  -13.304 5.631   1.00 43.62  ? 537 PHE A C   1 
ATOM   4025 O O   . PHE A 1 537 ? 33.892  -13.963 5.048   1.00 43.09  ? 537 PHE A O   1 
ATOM   4026 C CB  . PHE A 1 537 ? 34.939  -12.025 6.682   1.00 44.27  ? 537 PHE A CB  1 
ATOM   4027 C CG  . PHE A 1 537 ? 35.382  -10.849 7.508   1.00 44.38  ? 537 PHE A CG  1 
ATOM   4028 C CD1 . PHE A 1 537 ? 36.153  -11.033 8.649   1.00 44.57  ? 537 PHE A CD1 1 
ATOM   4029 C CD2 . PHE A 1 537 ? 35.018  -9.556  7.150   1.00 44.40  ? 537 PHE A CD2 1 
ATOM   4030 C CE1 . PHE A 1 537 ? 36.570  -9.947  9.414   1.00 44.56  ? 537 PHE A CE1 1 
ATOM   4031 C CE2 . PHE A 1 537 ? 35.427  -8.465  7.911   1.00 44.30  ? 537 PHE A CE2 1 
ATOM   4032 C CZ  . PHE A 1 537 ? 36.200  -8.662  9.045   1.00 44.50  ? 537 PHE A CZ  1 
ATOM   4033 N N   . SER A 1 538 ? 31.728  -13.538 5.512   1.00 43.44  ? 538 SER A N   1 
ATOM   4034 C CA  . SER A 1 538 ? 31.199  -14.645 4.711   1.00 43.16  ? 538 SER A CA  1 
ATOM   4035 C C   . SER A 1 538 ? 29.997  -14.228 3.864   1.00 42.88  ? 538 SER A C   1 
ATOM   4036 O O   . SER A 1 538 ? 29.457  -13.128 4.031   1.00 42.44  ? 538 SER A O   1 
ATOM   4037 C CB  . SER A 1 538 ? 30.792  -15.799 5.632   1.00 43.25  ? 538 SER A CB  1 
ATOM   4038 O OG  . SER A 1 538 ? 29.515  -15.566 6.209   1.00 44.17  ? 538 SER A OG  1 
ATOM   4039 N N   . GLU A 1 539 ? 29.593  -15.118 2.956   1.00 42.46  ? 539 GLU A N   1 
ATOM   4040 C CA  . GLU A 1 539 ? 28.342  -14.963 2.207   1.00 42.29  ? 539 GLU A CA  1 
ATOM   4041 C C   . GLU A 1 539 ? 27.583  -16.281 2.076   1.00 41.74  ? 539 GLU A C   1 
ATOM   4042 O O   . GLU A 1 539 ? 28.159  -17.354 2.207   1.00 41.14  ? 539 GLU A O   1 
ATOM   4043 C CB  . GLU A 1 539 ? 28.607  -14.399 0.813   1.00 42.28  ? 539 GLU A CB  1 
ATOM   4044 C CG  . GLU A 1 539 ? 29.411  -15.325 -0.083  1.00 42.71  ? 539 GLU A CG  1 
ATOM   4045 C CD  . GLU A 1 539 ? 29.671  -14.733 -1.453  1.00 42.89  ? 539 GLU A CD  1 
ATOM   4046 O OE1 . GLU A 1 539 ? 29.950  -15.511 -2.389  1.00 43.70  ? 539 GLU A OE1 1 
ATOM   4047 O OE2 . GLU A 1 539 ? 29.586  -13.496 -1.594  1.00 44.09  ? 539 GLU A OE2 1 
ATOM   4048 N N   . LYS A 1 540 ? 26.286  -16.169 1.814   1.00 41.58  ? 540 LYS A N   1 
ATOM   4049 C CA  . LYS A 1 540 ? 25.418  -17.320 1.596   1.00 41.73  ? 540 LYS A CA  1 
ATOM   4050 C C   . LYS A 1 540 ? 24.491  -17.012 0.432   1.00 41.03  ? 540 LYS A C   1 
ATOM   4051 O O   . LYS A 1 540 ? 24.056  -15.872 0.270   1.00 41.27  ? 540 LYS A O   1 
ATOM   4052 C CB  . LYS A 1 540 ? 24.536  -17.599 2.824   1.00 41.55  ? 540 LYS A CB  1 
ATOM   4053 C CG  . LYS A 1 540 ? 25.235  -18.270 4.001   1.00 42.83  ? 540 LYS A CG  1 
ATOM   4054 C CD  . LYS A 1 540 ? 24.191  -18.680 5.043   1.00 42.23  ? 540 LYS A CD  1 
ATOM   4055 C CE  . LYS A 1 540 ? 24.641  -19.806 5.889   1.00 41.74  ? 540 LYS A CE  1 
ATOM   4056 N NZ  . LYS A 1 540 ? 25.760  -19.361 6.734   1.00 43.59  ? 540 LYS A NZ  1 
ATOM   4057 N N   . SER A 1 541 ? 24.185  -18.029 -0.363  1.00 41.14  ? 541 SER A N   1 
ATOM   4058 C CA  . SER A 1 541 ? 23.078  -17.953 -1.312  1.00 41.42  ? 541 SER A CA  1 
ATOM   4059 C C   . SER A 1 541 ? 22.007  -18.941 -0.865  1.00 40.91  ? 541 SER A C   1 
ATOM   4060 O O   . SER A 1 541 ? 22.143  -20.133 -1.065  1.00 40.92  ? 541 SER A O   1 
ATOM   4061 C CB  . SER A 1 541 ? 23.539  -18.224 -2.753  1.00 41.84  ? 541 SER A CB  1 
ATOM   4062 O OG  . SER A 1 541 ? 24.680  -17.457 -3.097  1.00 42.45  ? 541 SER A OG  1 
ATOM   4063 N N   . VAL A 1 542 ? 20.963  -18.415 -0.229  1.00 41.39  ? 542 VAL A N   1 
ATOM   4064 C CA  . VAL A 1 542 ? 19.842  -19.202 0.281   1.00 41.63  ? 542 VAL A CA  1 
ATOM   4065 C C   . VAL A 1 542 ? 18.795  -19.355 -0.805  1.00 41.71  ? 542 VAL A C   1 
ATOM   4066 O O   . VAL A 1 542 ? 18.194  -18.357 -1.192  1.00 41.50  ? 542 VAL A O   1 
ATOM   4067 C CB  . VAL A 1 542 ? 19.138  -18.539 1.522   1.00 41.45  ? 542 VAL A CB  1 
ATOM   4068 C CG1 . VAL A 1 542 ? 18.292  -19.590 2.239   1.00 40.56  ? 542 VAL A CG1 1 
ATOM   4069 C CG2 . VAL A 1 542 ? 20.163  -17.901 2.486   1.00 40.39  ? 542 VAL A CG2 1 
ATOM   4070 N N   . PRO A 1 543 ? 18.583  -20.597 -1.287  1.00 42.48  ? 543 PRO A N   1 
ATOM   4071 C CA  . PRO A 1 543 ? 17.677  -20.860 -2.394  1.00 43.30  ? 543 PRO A CA  1 
ATOM   4072 C C   . PRO A 1 543 ? 16.221  -21.043 -1.991  1.00 44.21  ? 543 PRO A C   1 
ATOM   4073 O O   . PRO A 1 543 ? 15.935  -21.541 -0.887  1.00 42.53  ? 543 PRO A O   1 
ATOM   4074 C CB  . PRO A 1 543 ? 18.204  -22.187 -2.980  1.00 43.46  ? 543 PRO A CB  1 
ATOM   4075 C CG  . PRO A 1 543 ? 18.872  -22.884 -1.818  1.00 43.61  ? 543 PRO A CG  1 
ATOM   4076 C CD  . PRO A 1 543 ? 19.248  -21.822 -0.813  1.00 42.09  ? 543 PRO A CD  1 
ATOM   4077 N N   . LEU A 1 544 ? 15.332  -20.683 -2.922  1.00 43.45  ? 544 LEU A N   1 
ATOM   4078 C CA  . LEU A 1 544 ? 13.917  -21.050 -2.876  1.00 43.68  ? 544 LEU A CA  1 
ATOM   4079 C C   . LEU A 1 544 ? 13.531  -21.528 -4.267  1.00 44.03  ? 544 LEU A C   1 
ATOM   4080 O O   . LEU A 1 544 ? 13.757  -20.815 -5.250  1.00 43.26  ? 544 LEU A O   1 
ATOM   4081 C CB  . LEU A 1 544 ? 13.060  -19.835 -2.519  1.00 43.79  ? 544 LEU A CB  1 
ATOM   4082 C CG  . LEU A 1 544 ? 11.538  -19.923 -2.765  1.00 43.78  ? 544 LEU A CG  1 
ATOM   4083 C CD1 . LEU A 1 544 ? 10.904  -20.959 -1.874  1.00 43.84  ? 544 LEU A CD1 1 
ATOM   4084 C CD2 . LEU A 1 544 ? 10.885  -18.571 -2.606  1.00 44.64  ? 544 LEU A CD2 1 
ATOM   4085 N N   . CYS A 1 545 ? 12.932  -22.704 -4.329  1.00 44.10  ? 545 CYS A N   1 
ATOM   4086 C CA  . CYS A 1 545 ? 12.486  -23.314 -5.564  1.00 44.51  ? 545 CYS A CA  1 
ATOM   4087 C C   . CYS A 1 545 ? 11.122  -22.791 -6.016  1.00 44.66  ? 545 CYS A C   1 
ATOM   4088 O O   . CYS A 1 545 ? 10.114  -22.901 -5.292  1.00 44.60  ? 545 CYS A O   1 
ATOM   4089 C CB  . CYS A 1 545 ? 12.402  -24.817 -5.362  1.00 44.61  ? 545 CYS A CB  1 
ATOM   4090 S SG  . CYS A 1 545 ? 12.105  -25.727 -6.870  1.00 45.52  ? 545 CYS A SG  1 
ATOM   4091 N N   . ILE A 1 546 ? 11.110  -22.248 -7.228  1.00 44.76  ? 546 ILE A N   1 
ATOM   4092 C CA  . ILE A 1 546 ? 9.915   -21.742 -7.884  1.00 44.43  ? 546 ILE A CA  1 
ATOM   4093 C C   . ILE A 1 546 ? 9.422   -22.798 -8.865  1.00 44.37  ? 546 ILE A C   1 
ATOM   4094 O O   . ILE A 1 546 ? 10.070  -23.037 -9.875  1.00 43.38  ? 546 ILE A O   1 
ATOM   4095 C CB  . ILE A 1 546 ? 10.245  -20.473 -8.668  1.00 45.27  ? 546 ILE A CB  1 
ATOM   4096 C CG1 . ILE A 1 546 ? 10.913  -19.427 -7.773  1.00 45.16  ? 546 ILE A CG1 1 
ATOM   4097 C CG2 . ILE A 1 546 ? 8.985   -19.902 -9.316  1.00 45.24  ? 546 ILE A CG2 1 
ATOM   4098 C CD1 . ILE A 1 546 ? 10.140  -19.107 -6.498  1.00 47.43  ? 546 ILE A CD1 1 
ATOM   4099 N N   . LEU A 1 547 ? 8.289   -23.428 -8.543  1.00 43.81  ? 547 LEU A N   1 
ATOM   4100 C CA  . LEU A 1 547 ? 7.772   -24.556 -9.288  1.00 44.16  ? 547 LEU A CA  1 
ATOM   4101 C C   . LEU A 1 547 ? 6.745   -24.082 -10.302 1.00 44.39  ? 547 LEU A C   1 
ATOM   4102 O O   . LEU A 1 547 ? 5.965   -23.163 -10.033 1.00 43.99  ? 547 LEU A O   1 
ATOM   4103 C CB  . LEU A 1 547 ? 7.128   -25.573 -8.344  1.00 43.47  ? 547 LEU A CB  1 
ATOM   4104 C CG  . LEU A 1 547 ? 8.043   -26.146 -7.262  1.00 43.26  ? 547 LEU A CG  1 
ATOM   4105 C CD1 . LEU A 1 547 ? 7.284   -27.189 -6.440  1.00 41.32  ? 547 LEU A CD1 1 
ATOM   4106 C CD2 . LEU A 1 547 ? 9.292   -26.772 -7.879  1.00 41.49  ? 547 LEU A CD2 1 
ATOM   4107 N N   . TYR A 1 548 ? 6.762   -24.700 -11.472 1.00 44.78  ? 548 TYR A N   1 
ATOM   4108 C CA  . TYR A 1 548 ? 5.787   -24.378 -12.516 1.00 45.26  ? 548 TYR A CA  1 
ATOM   4109 C C   . TYR A 1 548 ? 4.397   -24.653 -11.993 1.00 45.78  ? 548 TYR A C   1 
ATOM   4110 O O   . TYR A 1 548 ? 3.508   -23.826 -12.119 1.00 46.47  ? 548 TYR A O   1 
ATOM   4111 C CB  . TYR A 1 548 ? 6.025   -25.190 -13.780 1.00 44.85  ? 548 TYR A CB  1 
ATOM   4112 C CG  . TYR A 1 548 ? 4.897   -25.042 -14.760 1.00 44.66  ? 548 TYR A CG  1 
ATOM   4113 C CD1 . TYR A 1 548 ? 4.690   -23.837 -15.424 1.00 44.84  ? 548 TYR A CD1 1 
ATOM   4114 C CD2 . TYR A 1 548 ? 4.006   -26.086 -14.997 1.00 45.05  ? 548 TYR A CD2 1 
ATOM   4115 C CE1 . TYR A 1 548 ? 3.644   -23.682 -16.329 1.00 44.28  ? 548 TYR A CE1 1 
ATOM   4116 C CE2 . TYR A 1 548 ? 2.949   -25.942 -15.907 1.00 44.25  ? 548 TYR A CE2 1 
ATOM   4117 C CZ  . TYR A 1 548 ? 2.774   -24.734 -16.564 1.00 44.53  ? 548 TYR A CZ  1 
ATOM   4118 O OH  . TYR A 1 548 ? 1.736   -24.571 -17.457 1.00 44.15  ? 548 TYR A OH  1 
ATOM   4119 N N   . GLU A 1 549 ? 4.224   -25.815 -11.379 1.00 46.78  ? 549 GLU A N   1 
ATOM   4120 C CA  . GLU A 1 549 ? 2.939   -26.197 -10.818 1.00 47.12  ? 549 GLU A CA  1 
ATOM   4121 C C   . GLU A 1 549 ? 2.397   -25.168 -9.816  1.00 47.36  ? 549 GLU A C   1 
ATOM   4122 O O   . GLU A 1 549 ? 1.185   -25.074 -9.638  1.00 47.25  ? 549 GLU A O   1 
ATOM   4123 C CB  . GLU A 1 549 ? 3.031   -27.584 -10.179 1.00 47.57  ? 549 GLU A CB  1 
ATOM   4124 C CG  . GLU A 1 549 ? 3.317   -28.705 -11.174 1.00 49.25  ? 549 GLU A CG  1 
ATOM   4125 C CD  . GLU A 1 549 ? 2.248   -28.846 -12.254 1.00 51.21  ? 549 GLU A CD  1 
ATOM   4126 O OE1 . GLU A 1 549 ? 1.047   -28.792 -11.910 1.00 53.19  ? 549 GLU A OE1 1 
ATOM   4127 O OE2 . GLU A 1 549 ? 2.607   -29.025 -13.444 1.00 51.59  ? 549 GLU A OE2 1 
ATOM   4128 N N   . LYS A 1 550 ? 3.272   -24.384 -9.181  1.00 47.72  ? 550 LYS A N   1 
ATOM   4129 C CA  . LYS A 1 550 ? 2.817   -23.353 -8.239  1.00 48.05  ? 550 LYS A CA  1 
ATOM   4130 C C   . LYS A 1 550 ? 2.514   -21.991 -8.886  1.00 48.35  ? 550 LYS A C   1 
ATOM   4131 O O   . LYS A 1 550 ? 1.572   -21.319 -8.477  1.00 48.71  ? 550 LYS A O   1 
ATOM   4132 C CB  . LYS A 1 550 ? 3.809   -23.169 -7.089  1.00 47.89  ? 550 LYS A CB  1 
ATOM   4133 C CG  . LYS A 1 550 ? 3.976   -24.373 -6.193  1.00 48.57  ? 550 LYS A CG  1 
ATOM   4134 C CD  . LYS A 1 550 ? 2.680   -24.800 -5.501  1.00 48.72  ? 550 LYS A CD  1 
ATOM   4135 C CE  . LYS A 1 550 ? 2.902   -26.017 -4.603  1.00 48.53  ? 550 LYS A CE  1 
ATOM   4136 N NZ  . LYS A 1 550 ? 1.851   -27.056 -4.812  1.00 48.90  ? 550 LYS A NZ  1 
ATOM   4137 N N   . TYR A 1 551 ? 3.297   -21.559 -9.867  1.00 48.62  ? 551 TYR A N   1 
ATOM   4138 C CA  . TYR A 1 551 ? 2.982   -20.294 -10.542 1.00 48.90  ? 551 TYR A CA  1 
ATOM   4139 C C   . TYR A 1 551 ? 2.076   -20.447 -11.781 1.00 49.67  ? 551 TYR A C   1 
ATOM   4140 O O   . TYR A 1 551 ? 1.477   -19.473 -12.239 1.00 49.77  ? 551 TYR A O   1 
ATOM   4141 C CB  . TYR A 1 551 ? 4.256   -19.510 -10.876 1.00 47.77  ? 551 TYR A CB  1 
ATOM   4142 C CG  . TYR A 1 551 ? 5.151   -20.103 -11.943 1.00 47.13  ? 551 TYR A CG  1 
ATOM   4143 C CD1 . TYR A 1 551 ? 4.811   -20.023 -13.298 1.00 45.75  ? 551 TYR A CD1 1 
ATOM   4144 C CD2 . TYR A 1 551 ? 6.368   -20.688 -11.606 1.00 45.25  ? 551 TYR A CD2 1 
ATOM   4145 C CE1 . TYR A 1 551 ? 5.637   -20.550 -14.276 1.00 45.63  ? 551 TYR A CE1 1 
ATOM   4146 C CE2 . TYR A 1 551 ? 7.200   -21.216 -12.580 1.00 46.60  ? 551 TYR A CE2 1 
ATOM   4147 C CZ  . TYR A 1 551 ? 6.830   -21.143 -13.918 1.00 45.95  ? 551 TYR A CZ  1 
ATOM   4148 O OH  . TYR A 1 551 ? 7.657   -21.665 -14.886 1.00 45.05  ? 551 TYR A OH  1 
ATOM   4149 N N   . ARG A 1 552 ? 1.960   -21.656 -12.317 1.00 50.65  ? 552 ARG A N   1 
ATOM   4150 C CA  . ARG A 1 552 ? 1.225   -21.844 -13.566 1.00 51.44  ? 552 ARG A CA  1 
ATOM   4151 C C   . ARG A 1 552 ? -0.184  -21.240 -13.542 1.00 52.19  ? 552 ARG A C   1 
ATOM   4152 O O   . ARG A 1 552 ? -0.501  -20.391 -14.380 1.00 52.30  ? 552 ARG A O   1 
ATOM   4153 C CB  . ARG A 1 552 ? 1.198   -23.319 -13.982 1.00 51.54  ? 552 ARG A CB  1 
ATOM   4154 C CG  . ARG A 1 552 ? 0.565   -24.280 -12.994 1.00 52.09  ? 552 ARG A CG  1 
ATOM   4155 C CD  . ARG A 1 552 ? -0.814  -24.710 -13.437 1.00 52.85  ? 552 ARG A CD  1 
ATOM   4156 N NE  . ARG A 1 552 ? -0.744  -25.679 -14.535 1.00 53.49  ? 552 ARG A NE  1 
ATOM   4157 C CZ  . ARG A 1 552 ? -0.882  -27.002 -14.414 1.00 52.93  ? 552 ARG A CZ  1 
ATOM   4158 N NH1 . ARG A 1 552 ? -1.111  -27.568 -13.232 1.00 52.79  ? 552 ARG A NH1 1 
ATOM   4159 N NH2 . ARG A 1 552 ? -0.790  -27.772 -15.494 1.00 52.65  ? 552 ARG A NH2 1 
ATOM   4160 N N   . ASP A 1 553 ? -1.014  -21.630 -12.579 1.00 53.05  ? 553 ASP A N   1 
ATOM   4161 C CA  . ASP A 1 553 ? -2.441  -21.279 -12.635 1.00 54.01  ? 553 ASP A CA  1 
ATOM   4162 C C   . ASP A 1 553 ? -2.718  -19.812 -12.299 1.00 54.61  ? 553 ASP A C   1 
ATOM   4163 O O   . ASP A 1 553 ? -3.738  -19.255 -12.729 1.00 54.68  ? 553 ASP A O   1 
ATOM   4164 C CB  . ASP A 1 553 ? -3.289  -22.213 -11.744 1.00 54.24  ? 553 ASP A CB  1 
ATOM   4165 C CG  . ASP A 1 553 ? -3.117  -21.933 -10.252 1.00 55.22  ? 553 ASP A CG  1 
ATOM   4166 O OD1 . ASP A 1 553 ? -1.962  -21.747 -9.791  1.00 56.31  ? 553 ASP A OD1 1 
ATOM   4167 O OD2 . ASP A 1 553 ? -4.147  -21.915 -9.542  1.00 55.76  ? 553 ASP A OD2 1 
ATOM   4168 N N   . CYS A 1 554 ? -1.799  -19.189 -11.565 1.00 55.29  ? 554 CYS A N   1 
ATOM   4169 C CA  . CYS A 1 554 ? -2.045  -17.882 -10.947 1.00 55.77  ? 554 CYS A CA  1 
ATOM   4170 C C   . CYS A 1 554 ? -1.202  -16.739 -11.518 1.00 56.09  ? 554 CYS A C   1 
ATOM   4171 O O   . CYS A 1 554 ? -1.109  -15.681 -10.888 1.00 56.37  ? 554 CYS A O   1 
ATOM   4172 C CB  . CYS A 1 554 ? -1.796  -17.993 -9.434  1.00 56.00  ? 554 CYS A CB  1 
ATOM   4173 S SG  . CYS A 1 554 ? -0.108  -18.522 -8.950  1.00 57.40  ? 554 CYS A SG  1 
ATOM   4174 N N   . LEU A 1 555 ? -0.619  -16.941 -12.706 1.00 56.28  ? 555 LEU A N   1 
ATOM   4175 C CA  . LEU A 1 555 ? 0.395   -16.028 -13.269 1.00 56.32  ? 555 LEU A CA  1 
ATOM   4176 C C   . LEU A 1 555 ? -0.150  -15.235 -14.448 1.00 56.58  ? 555 LEU A C   1 
ATOM   4177 O O   . LEU A 1 555 ? -0.802  -15.798 -15.323 1.00 56.97  ? 555 LEU A O   1 
ATOM   4178 C CB  . LEU A 1 555 ? 1.631   -16.828 -13.718 1.00 56.33  ? 555 LEU A CB  1 
ATOM   4179 C CG  . LEU A 1 555 ? 2.809   -16.129 -14.412 1.00 56.07  ? 555 LEU A CG  1 
ATOM   4180 C CD1 . LEU A 1 555 ? 3.669   -15.358 -13.408 1.00 54.65  ? 555 LEU A CD1 1 
ATOM   4181 C CD2 . LEU A 1 555 ? 3.659   -17.135 -15.188 1.00 55.83  ? 555 LEU A CD2 1 
ATOM   4182 N N   . THR A 1 556 ? 0.149   -13.935 -14.476 1.00 56.78  ? 556 THR A N   1 
ATOM   4183 C CA  . THR A 1 556 ? -0.352  -13.020 -15.520 1.00 56.68  ? 556 THR A CA  1 
ATOM   4184 C C   . THR A 1 556 ? 0.342   -13.206 -16.857 1.00 56.50  ? 556 THR A C   1 
ATOM   4185 O O   . THR A 1 556 ? 1.491   -13.662 -16.914 1.00 56.88  ? 556 THR A O   1 
ATOM   4186 C CB  . THR A 1 556 ? -0.121  -11.546 -15.129 1.00 56.97  ? 556 THR A CB  1 
ATOM   4187 O OG1 . THR A 1 556 ? 1.255   -11.362 -14.746 1.00 57.15  ? 556 THR A OG1 1 
ATOM   4188 C CG2 . THR A 1 556 ? -1.045  -11.144 -13.980 1.00 57.53  ? 556 THR A CG2 1 
ATOM   4189 N N   . GLU A 1 557 ? -0.340  -12.794 -17.926 1.00 56.33  ? 557 GLU A N   1 
ATOM   4190 C CA  . GLU A 1 557 ? 0.243   -12.807 -19.272 1.00 55.77  ? 557 GLU A CA  1 
ATOM   4191 C C   . GLU A 1 557 ? 1.425   -11.812 -19.377 1.00 55.22  ? 557 GLU A C   1 
ATOM   4192 O O   . GLU A 1 557 ? 2.046   -11.665 -20.437 1.00 55.14  ? 557 GLU A O   1 
ATOM   4193 C CB  . GLU A 1 557 ? -0.838  -12.516 -20.330 1.00 56.28  ? 557 GLU A CB  1 
ATOM   4194 C CG  . GLU A 1 557 ? -1.978  -13.567 -20.396 1.00 57.08  ? 557 GLU A CG  1 
ATOM   4195 C CD  . GLU A 1 557 ? -1.743  -14.689 -21.421 1.00 58.13  ? 557 GLU A CD  1 
ATOM   4196 O OE1 . GLU A 1 557 ? -2.641  -14.930 -22.260 1.00 59.36  ? 557 GLU A OE1 1 
ATOM   4197 O OE2 . GLU A 1 557 ? -0.674  -15.335 -21.391 1.00 59.03  ? 557 GLU A OE2 1 
ATOM   4198 N N   . SER A 1 558 ? 1.712   -11.125 -18.271 1.00 54.40  ? 558 SER A N   1 
ATOM   4199 C CA  . SER A 1 558 ? 2.970   -10.397 -18.083 1.00 53.66  ? 558 SER A CA  1 
ATOM   4200 C C   . SER A 1 558 ? 4.149   -11.328 -17.721 1.00 52.85  ? 558 SER A C   1 
ATOM   4201 O O   . SER A 1 558 ? 5.309   -10.932 -17.862 1.00 52.47  ? 558 SER A O   1 
ATOM   4202 C CB  . SER A 1 558 ? 2.803   -9.337  -16.988 1.00 54.02  ? 558 SER A CB  1 
ATOM   4203 O OG  . SER A 1 558 ? 1.571   -8.635  -17.129 1.00 54.20  ? 558 SER A OG  1 
ATOM   4204 N N   . ASN A 1 559 ? 3.857   -12.550 -17.261 1.00 51.51  ? 559 ASN A N   1 
ATOM   4205 C CA  . ASN A 1 559 ? 4.894   -13.535 -16.988 1.00 50.89  ? 559 ASN A CA  1 
ATOM   4206 C C   . ASN A 1 559 ? 5.786   -13.160 -15.790 1.00 49.80  ? 559 ASN A C   1 
ATOM   4207 O O   . ASN A 1 559 ? 6.888   -13.682 -15.671 1.00 49.52  ? 559 ASN A O   1 
ATOM   4208 C CB  . ASN A 1 559 ? 5.787   -13.739 -18.232 1.00 50.91  ? 559 ASN A CB  1 
ATOM   4209 C CG  . ASN A 1 559 ? 5.177   -14.665 -19.264 1.00 52.38  ? 559 ASN A CG  1 
ATOM   4210 O OD1 . ASN A 1 559 ? 3.954   -14.797 -19.375 1.00 54.97  ? 559 ASN A OD1 1 
ATOM   4211 N ND2 . ASN A 1 559 ? 6.038   -15.304 -20.050 1.00 52.97  ? 559 ASN A ND2 1 
ATOM   4212 N N   . LEU A 1 560 ? 5.314   -12.272 -14.911 1.00 48.73  ? 560 LEU A N   1 
ATOM   4213 C CA  . LEU A 1 560 ? 6.164   -11.687 -13.860 1.00 48.65  ? 560 LEU A CA  1 
ATOM   4214 C C   . LEU A 1 560 ? 6.001   -12.354 -12.486 1.00 48.03  ? 560 LEU A C   1 
ATOM   4215 O O   . LEU A 1 560 ? 4.888   -12.655 -12.057 1.00 47.25  ? 560 LEU A O   1 
ATOM   4216 C CB  . LEU A 1 560 ? 5.885   -10.199 -13.708 1.00 48.33  ? 560 LEU A CB  1 
ATOM   4217 C CG  . LEU A 1 560 ? 6.177   -9.323  -14.938 1.00 49.12  ? 560 LEU A CG  1 
ATOM   4218 C CD1 . LEU A 1 560 ? 5.429   -8.012  -14.847 1.00 49.03  ? 560 LEU A CD1 1 
ATOM   4219 C CD2 . LEU A 1 560 ? 7.687   -9.089  -15.075 1.00 48.80  ? 560 LEU A CD2 1 
ATOM   4220 N N   . ILE A 1 561 ? 7.124   -12.560 -11.808 1.00 48.00  ? 561 ILE A N   1 
ATOM   4221 C CA  . ILE A 1 561 ? 7.133   -13.056 -10.422 1.00 48.25  ? 561 ILE A CA  1 
ATOM   4222 C C   . ILE A 1 561 ? 7.972   -12.130 -9.541  1.00 48.46  ? 561 ILE A C   1 
ATOM   4223 O O   . ILE A 1 561 ? 9.143   -11.873 -9.843  1.00 49.03  ? 561 ILE A O   1 
ATOM   4224 C CB  . ILE A 1 561 ? 7.704   -14.455 -10.331 1.00 47.98  ? 561 ILE A CB  1 
ATOM   4225 C CG1 . ILE A 1 561 ? 6.803   -15.438 -11.092 1.00 48.51  ? 561 ILE A CG1 1 
ATOM   4226 C CG2 . ILE A 1 561 ? 7.836   -14.877 -8.876  1.00 47.96  ? 561 ILE A CG2 1 
ATOM   4227 C CD1 . ILE A 1 561 ? 7.233   -16.878 -10.940 1.00 48.76  ? 561 ILE A CD1 1 
ATOM   4228 N N   . LYS A 1 562 ? 7.369   -11.621 -8.466  1.00 47.87  ? 562 LYS A N   1 
ATOM   4229 C CA  . LYS A 1 562 ? 8.096   -10.777 -7.535  1.00 47.68  ? 562 LYS A CA  1 
ATOM   4230 C C   . LYS A 1 562 ? 8.652   -11.670 -6.429  1.00 47.36  ? 562 LYS A C   1 
ATOM   4231 O O   . LYS A 1 562 ? 7.895   -12.360 -5.758  1.00 46.59  ? 562 LYS A O   1 
ATOM   4232 C CB  . LYS A 1 562 ? 7.189   -9.710  -6.936  1.00 48.06  ? 562 LYS A CB  1 
ATOM   4233 C CG  . LYS A 1 562 ? 7.940   -8.702  -6.066  1.00 48.35  ? 562 LYS A CG  1 
ATOM   4234 C CD  . LYS A 1 562 ? 7.030   -7.617  -5.494  1.00 47.87  ? 562 LYS A CD  1 
ATOM   4235 C CE  . LYS A 1 562 ? 6.545   -6.628  -6.538  1.00 47.71  ? 562 LYS A CE  1 
ATOM   4236 N NZ  . LYS A 1 562 ? 7.677   -5.895  -7.131  1.00 47.06  ? 562 LYS A NZ  1 
ATOM   4237 N N   . VAL A 1 563 ? 9.974   -11.670 -6.285  1.00 47.01  ? 563 VAL A N   1 
ATOM   4238 C CA  . VAL A 1 563 ? 10.651  -12.347 -5.174  1.00 46.71  ? 563 VAL A CA  1 
ATOM   4239 C C   . VAL A 1 563 ? 11.032  -11.283 -4.143  1.00 46.37  ? 563 VAL A C   1 
ATOM   4240 O O   . VAL A 1 563 ? 11.558  -10.231 -4.477  1.00 46.45  ? 563 VAL A O   1 
ATOM   4241 C CB  . VAL A 1 563 ? 11.907  -13.103 -5.666  1.00 47.00  ? 563 VAL A CB  1 
ATOM   4242 C CG1 . VAL A 1 563 ? 12.593  -13.817 -4.534  1.00 45.57  ? 563 VAL A CG1 1 
ATOM   4243 C CG2 . VAL A 1 563 ? 11.546  -14.096 -6.824  1.00 46.00  ? 563 VAL A CG2 1 
ATOM   4244 N N   . ARG A 1 564 ? 10.753  -11.570 -2.877  1.00 46.72  ? 564 ARG A N   1 
ATOM   4245 C CA  . ARG A 1 564 ? 10.994  -10.622 -1.801  1.00 46.05  ? 564 ARG A CA  1 
ATOM   4246 C C   . ARG A 1 564 ? 11.657  -11.364 -0.649  1.00 45.61  ? 564 ARG A C   1 
ATOM   4247 O O   . ARG A 1 564 ? 11.238  -12.475 -0.313  1.00 45.28  ? 564 ARG A O   1 
ATOM   4248 C CB  . ARG A 1 564 ? 9.666   -10.044 -1.339  1.00 46.17  ? 564 ARG A CB  1 
ATOM   4249 C CG  . ARG A 1 564 ? 9.114   -8.982  -2.225  1.00 46.52  ? 564 ARG A CG  1 
ATOM   4250 C CD  . ARG A 1 564 ? 7.773   -8.459  -1.732  1.00 46.22  ? 564 ARG A CD  1 
ATOM   4251 N NE  . ARG A 1 564 ? 6.920   -9.576  -1.333  1.00 48.28  ? 564 ARG A NE  1 
ATOM   4252 C CZ  . ARG A 1 564 ? 5.763   -9.450  -0.691  1.00 48.29  ? 564 ARG A CZ  1 
ATOM   4253 N NH1 . ARG A 1 564 ? 5.290   -8.250  -0.403  1.00 49.78  ? 564 ARG A NH1 1 
ATOM   4254 N NH2 . ARG A 1 564 ? 5.071   -10.539 -0.348  1.00 46.48  ? 564 ARG A NH2 1 
ATOM   4255 N N   . ALA A 1 565 ? 12.701  -10.768 -0.077  1.00 45.07  ? 565 ALA A N   1 
ATOM   4256 C CA  . ALA A 1 565 ? 13.384  -11.359 1.095   1.00 45.17  ? 565 ALA A CA  1 
ATOM   4257 C C   . ALA A 1 565 ? 13.391  -10.338 2.236   1.00 44.90  ? 565 ALA A C   1 
ATOM   4258 O O   . ALA A 1 565 ? 13.506  -9.132  1.982   1.00 44.13  ? 565 ALA A O   1 
ATOM   4259 C CB  . ALA A 1 565 ? 14.816  -11.764 0.744   1.00 44.30  ? 565 ALA A CB  1 
ATOM   4260 N N   . LEU A 1 566 ? 13.264  -10.838 3.471   1.00 44.58  ? 566 LEU A N   1 
ATOM   4261 C CA  . LEU A 1 566 ? 13.403  -10.020 4.690   1.00 44.78  ? 566 LEU A CA  1 
ATOM   4262 C C   . LEU A 1 566 ? 14.364  -10.739 5.610   1.00 44.63  ? 566 LEU A C   1 
ATOM   4263 O O   . LEU A 1 566 ? 14.135  -11.891 5.954   1.00 44.76  ? 566 LEU A O   1 
ATOM   4264 C CB  . LEU A 1 566 ? 12.071  -9.848  5.416   1.00 44.80  ? 566 LEU A CB  1 
ATOM   4265 C CG  . LEU A 1 566 ? 12.102  -9.061  6.750   1.00 44.52  ? 566 LEU A CG  1 
ATOM   4266 C CD1 . LEU A 1 566 ? 12.520  -7.614  6.536   1.00 40.60  ? 566 LEU A CD1 1 
ATOM   4267 C CD2 . LEU A 1 566 ? 10.763  -9.139  7.482   1.00 44.04  ? 566 LEU A CD2 1 
ATOM   4268 N N   . LEU A 1 567 ? 15.463  -10.070 5.940   1.00 45.42  ? 567 LEU A N   1 
ATOM   4269 C CA  . LEU A 1 567 ? 16.433  -10.556 6.913   1.00 45.66  ? 567 LEU A CA  1 
ATOM   4270 C C   . LEU A 1 567 ? 16.243  -9.748  8.194   1.00 45.40  ? 567 LEU A C   1 
ATOM   4271 O O   . LEU A 1 567 ? 16.369  -8.529  8.175   1.00 45.55  ? 567 LEU A O   1 
ATOM   4272 C CB  . LEU A 1 567 ? 17.842  -10.343 6.359   1.00 45.66  ? 567 LEU A CB  1 
ATOM   4273 C CG  . LEU A 1 567 ? 19.023  -11.008 7.044   1.00 46.36  ? 567 LEU A CG  1 
ATOM   4274 C CD1 . LEU A 1 567 ? 18.873  -12.481 7.010   1.00 42.22  ? 567 LEU A CD1 1 
ATOM   4275 C CD2 . LEU A 1 567 ? 20.337  -10.559 6.384   1.00 46.46  ? 567 LEU A CD2 1 
ATOM   4276 N N   . VAL A 1 568 ? 15.922  -10.427 9.293   1.00 46.23  ? 568 VAL A N   1 
ATOM   4277 C CA  . VAL A 1 568 ? 15.712  -9.775  10.588  1.00 46.44  ? 568 VAL A CA  1 
ATOM   4278 C C   . VAL A 1 568 ? 16.787  -10.141 11.609  1.00 46.63  ? 568 VAL A C   1 
ATOM   4279 O O   . VAL A 1 568 ? 17.094  -11.322 11.805  1.00 45.52  ? 568 VAL A O   1 
ATOM   4280 C CB  . VAL A 1 568 ? 14.371  -10.180 11.206  1.00 46.93  ? 568 VAL A CB  1 
ATOM   4281 C CG1 . VAL A 1 568 ? 14.112  -9.366  12.499  1.00 46.69  ? 568 VAL A CG1 1 
ATOM   4282 C CG2 . VAL A 1 568 ? 13.240  -9.969  10.207  1.00 47.30  ? 568 VAL A CG2 1 
ATOM   4283 N N   . GLU A 1 569 ? 17.344  -9.120  12.261  1.00 46.86  ? 569 GLU A N   1 
ATOM   4284 C CA  . GLU A 1 569 ? 18.221  -9.334  13.407  1.00 47.15  ? 569 GLU A CA  1 
ATOM   4285 C C   . GLU A 1 569 ? 17.511  -8.732  14.620  1.00 46.58  ? 569 GLU A C   1 
ATOM   4286 O O   . GLU A 1 569 ? 17.571  -7.521  14.856  1.00 46.48  ? 569 GLU A O   1 
ATOM   4287 C CB  . GLU A 1 569 ? 19.628  -8.797  13.117  1.00 47.96  ? 569 GLU A CB  1 
ATOM   4288 C CG  . GLU A 1 569 ? 20.376  -8.066  14.194  1.00 51.26  ? 569 GLU A CG  1 
ATOM   4289 C CD  . GLU A 1 569 ? 20.568  -8.810  15.497  1.00 53.83  ? 569 GLU A CD  1 
ATOM   4290 O OE1 . GLU A 1 569 ? 19.795  -9.729  15.832  1.00 55.47  ? 569 GLU A OE1 1 
ATOM   4291 O OE2 . GLU A 1 569 ? 21.504  -8.423  16.219  1.00 56.72  ? 569 GLU A OE2 1 
ATOM   4292 N N   . PRO A 1 570 ? 16.794  -9.590  15.365  1.00 46.31  ? 570 PRO A N   1 
ATOM   4293 C CA  . PRO A 1 570 ? 15.888  -9.148  16.416  1.00 46.31  ? 570 PRO A CA  1 
ATOM   4294 C C   . PRO A 1 570 ? 16.564  -8.479  17.629  1.00 46.26  ? 570 PRO A C   1 
ATOM   4295 O O   . PRO A 1 570 ? 15.901  -7.695  18.318  1.00 46.48  ? 570 PRO A O   1 
ATOM   4296 C CB  . PRO A 1 570 ? 15.154  -10.436 16.830  1.00 46.50  ? 570 PRO A CB  1 
ATOM   4297 C CG  . PRO A 1 570 ? 15.943  -11.554 16.312  1.00 46.64  ? 570 PRO A CG  1 
ATOM   4298 C CD  . PRO A 1 570 ? 16.815  -11.061 15.219  1.00 46.14  ? 570 PRO A CD  1 
ATOM   4299 N N   . VAL A 1 571 ? 17.849  -8.759  17.876  1.00 45.57  ? 571 VAL A N   1 
ATOM   4300 C CA  . VAL A 1 571 ? 18.550  -8.171  19.030  1.00 44.92  ? 571 VAL A CA  1 
ATOM   4301 C C   . VAL A 1 571 ? 18.717  -6.651  18.921  1.00 44.77  ? 571 VAL A C   1 
ATOM   4302 O O   . VAL A 1 571 ? 18.315  -5.936  19.831  1.00 44.40  ? 571 VAL A O   1 
ATOM   4303 C CB  . VAL A 1 571 ? 19.931  -8.826  19.303  1.00 45.15  ? 571 VAL A CB  1 
ATOM   4304 C CG1 . VAL A 1 571 ? 20.606  -8.165  20.531  1.00 44.38  ? 571 VAL A CG1 1 
ATOM   4305 C CG2 . VAL A 1 571 ? 19.776  -10.325 19.521  1.00 44.61  ? 571 VAL A CG2 1 
ATOM   4306 N N   . ILE A 1 572 ? 19.285  -6.162  17.815  1.00 44.44  ? 572 ILE A N   1 
ATOM   4307 C CA  . ILE A 1 572 ? 19.403  -4.706  17.602  1.00 43.78  ? 572 ILE A CA  1 
ATOM   4308 C C   . ILE A 1 572 ? 18.138  -4.182  16.903  1.00 42.82  ? 572 ILE A C   1 
ATOM   4309 O O   . ILE A 1 572 ? 17.958  -2.974  16.775  1.00 42.48  ? 572 ILE A O   1 
ATOM   4310 C CB  . ILE A 1 572 ? 20.626  -4.242  16.710  1.00 43.97  ? 572 ILE A CB  1 
ATOM   4311 C CG1 . ILE A 1 572 ? 21.715  -5.304  16.538  1.00 45.35  ? 572 ILE A CG1 1 
ATOM   4312 C CG2 . ILE A 1 572 ? 21.242  -2.944  17.289  1.00 44.47  ? 572 ILE A CG2 1 
ATOM   4313 C CD1 . ILE A 1 572 ? 22.040  -5.625  15.051  1.00 45.28  ? 572 ILE A CD1 1 
ATOM   4314 N N   . ASN A 1 573 ? 17.280  -5.089  16.443  1.00 41.58  ? 573 ASN A N   1 
ATOM   4315 C CA  . ASN A 1 573 ? 16.054  -4.718  15.764  1.00 41.17  ? 573 ASN A CA  1 
ATOM   4316 C C   . ASN A 1 573 ? 16.368  -4.062  14.390  1.00 40.74  ? 573 ASN A C   1 
ATOM   4317 O O   . ASN A 1 573 ? 15.894  -2.958  14.076  1.00 39.76  ? 573 ASN A O   1 
ATOM   4318 C CB  . ASN A 1 573 ? 15.224  -3.815  16.663  1.00 40.96  ? 573 ASN A CB  1 
ATOM   4319 C CG  . ASN A 1 573 ? 13.758  -3.850  16.346  1.00 40.74  ? 573 ASN A CG  1 
ATOM   4320 O OD1 . ASN A 1 573 ? 13.052  -2.831  16.576  1.00 42.20  ? 573 ASN A OD1 1 
ATOM   4321 N ND2 . ASN A 1 573 ? 13.274  -5.004  15.854  1.00 39.01  ? 573 ASN A ND2 1 
ATOM   4322 N N   . SER A 1 574 ? 17.181  -4.762  13.589  1.00 40.41  ? 574 SER A N   1 
ATOM   4323 C CA  . SER A 1 574 ? 17.574  -4.263  12.279  1.00 41.14  ? 574 SER A CA  1 
ATOM   4324 C C   . SER A 1 574 ? 17.003  -5.174  11.218  1.00 40.38  ? 574 SER A C   1 
ATOM   4325 O O   . SER A 1 574 ? 16.920  -6.386  11.404  1.00 38.61  ? 574 SER A O   1 
ATOM   4326 C CB  . SER A 1 574 ? 19.093  -4.131  12.153  1.00 41.05  ? 574 SER A CB  1 
ATOM   4327 O OG  . SER A 1 574 ? 19.701  -5.406  12.061  1.00 46.29  ? 574 SER A OG  1 
ATOM   4328 N N   . TYR A 1 575 ? 16.609  -4.567  10.102  1.00 40.81  ? 575 TYR A N   1 
ATOM   4329 C CA  . TYR A 1 575 ? 15.825  -5.232  9.065   1.00 41.66  ? 575 TYR A CA  1 
ATOM   4330 C C   . TYR A 1 575 ? 16.394  -4.903  7.690   1.00 42.06  ? 575 TYR A C   1 
ATOM   4331 O O   . TYR A 1 575 ? 16.606  -3.734  7.370   1.00 40.79  ? 575 TYR A O   1 
ATOM   4332 C CB  . TYR A 1 575 ? 14.366  -4.756  9.135   1.00 42.16  ? 575 TYR A CB  1 
ATOM   4333 C CG  . TYR A 1 575 ? 13.690  -5.144  10.425  1.00 41.96  ? 575 TYR A CG  1 
ATOM   4334 C CD1 . TYR A 1 575 ? 13.733  -4.316  11.530  1.00 40.72  ? 575 TYR A CD1 1 
ATOM   4335 C CD2 . TYR A 1 575 ? 13.052  -6.364  10.544  1.00 41.32  ? 575 TYR A CD2 1 
ATOM   4336 C CE1 . TYR A 1 575 ? 13.132  -4.678  12.710  1.00 41.58  ? 575 TYR A CE1 1 
ATOM   4337 C CE2 . TYR A 1 575 ? 12.455  -6.739  11.737  1.00 43.56  ? 575 TYR A CE2 1 
ATOM   4338 C CZ  . TYR A 1 575 ? 12.504  -5.894  12.817  1.00 41.81  ? 575 TYR A CZ  1 
ATOM   4339 O OH  . TYR A 1 575 ? 11.909  -6.258  13.994  1.00 42.70  ? 575 TYR A OH  1 
ATOM   4340 N N   . LEU A 1 576 ? 16.658  -5.941  6.901   1.00 43.05  ? 576 LEU A N   1 
ATOM   4341 C CA  . LEU A 1 576 ? 17.103  -5.786  5.510   1.00 44.00  ? 576 LEU A CA  1 
ATOM   4342 C C   . LEU A 1 576 ? 16.068  -6.388  4.587   1.00 44.21  ? 576 LEU A C   1 
ATOM   4343 O O   . LEU A 1 576 ? 15.705  -7.551  4.741   1.00 44.85  ? 576 LEU A O   1 
ATOM   4344 C CB  . LEU A 1 576 ? 18.418  -6.521  5.295   1.00 44.32  ? 576 LEU A CB  1 
ATOM   4345 C CG  . LEU A 1 576 ? 19.667  -5.764  5.708   1.00 44.81  ? 576 LEU A CG  1 
ATOM   4346 C CD1 . LEU A 1 576 ? 19.702  -5.591  7.214   1.00 45.46  ? 576 LEU A CD1 1 
ATOM   4347 C CD2 . LEU A 1 576 ? 20.897  -6.509  5.206   1.00 44.94  ? 576 LEU A CD2 1 
ATOM   4348 N N   . LEU A 1 577 ? 15.590  -5.589  3.640   1.00 44.72  ? 577 LEU A N   1 
ATOM   4349 C CA  . LEU A 1 577 ? 14.593  -6.025  2.659   1.00 45.36  ? 577 LEU A CA  1 
ATOM   4350 C C   . LEU A 1 577 ? 15.254  -6.058  1.272   1.00 44.99  ? 577 LEU A C   1 
ATOM   4351 O O   . LEU A 1 577 ? 16.049  -5.184  0.941   1.00 44.96  ? 577 LEU A O   1 
ATOM   4352 C CB  . LEU A 1 577 ? 13.368  -5.077  2.641   1.00 45.74  ? 577 LEU A CB  1 
ATOM   4353 C CG  . LEU A 1 577 ? 12.255  -5.355  3.669   1.00 47.63  ? 577 LEU A CG  1 
ATOM   4354 C CD1 . LEU A 1 577 ? 11.255  -4.204  3.767   1.00 50.18  ? 577 LEU A CD1 1 
ATOM   4355 C CD2 . LEU A 1 577 ? 11.543  -6.642  3.326   1.00 49.66  ? 577 LEU A CD2 1 
ATOM   4356 N N   . ALA A 1 578 ? 14.961  -7.093  0.500   1.00 45.58  ? 578 ALA A N   1 
ATOM   4357 C CA  . ALA A 1 578 ? 15.379  -7.149  -0.915  1.00 45.94  ? 578 ALA A CA  1 
ATOM   4358 C C   . ALA A 1 578 ? 14.188  -7.558  -1.769  1.00 46.25  ? 578 ALA A C   1 
ATOM   4359 O O   . ALA A 1 578 ? 13.438  -8.448  -1.402  1.00 46.17  ? 578 ALA A O   1 
ATOM   4360 C CB  . ALA A 1 578 ? 16.513  -8.144  -1.113  1.00 45.86  ? 578 ALA A CB  1 
ATOM   4361 N N   . GLU A 1 579 ? 14.041  -6.940  -2.931  1.00 46.19  ? 579 GLU A N   1 
ATOM   4362 C CA  . GLU A 1 579 ? 12.951  -7.275  -3.814  1.00 46.17  ? 579 GLU A CA  1 
ATOM   4363 C C   . GLU A 1 579 ? 13.437  -7.184  -5.256  1.00 45.80  ? 579 GLU A C   1 
ATOM   4364 O O   . GLU A 1 579 ? 14.217  -6.312  -5.590  1.00 45.64  ? 579 GLU A O   1 
ATOM   4365 C CB  . GLU A 1 579 ? 11.793  -6.326  -3.535  1.00 46.39  ? 579 GLU A CB  1 
ATOM   4366 C CG  . GLU A 1 579 ? 10.627  -6.370  -4.522  1.00 47.97  ? 579 GLU A CG  1 
ATOM   4367 C CD  . GLU A 1 579 ? 9.748   -5.130  -4.416  1.00 48.10  ? 579 GLU A CD  1 
ATOM   4368 O OE1 . GLU A 1 579 ? 9.618   -4.604  -3.304  1.00 53.60  ? 579 GLU A OE1 1 
ATOM   4369 O OE2 . GLU A 1 579 ? 9.189   -4.671  -5.440  1.00 52.25  ? 579 GLU A OE2 1 
ATOM   4370 N N   . ARG A 1 580 ? 12.982  -8.123  -6.078  1.00 45.61  ? 580 ARG A N   1 
ATOM   4371 C CA  . ARG A 1 580 ? 13.328  -8.178  -7.479  1.00 45.39  ? 580 ARG A CA  1 
ATOM   4372 C C   . ARG A 1 580 ? 12.191  -8.858  -8.227  1.00 44.63  ? 580 ARG A C   1 
ATOM   4373 O O   . ARG A 1 580 ? 11.729  -9.931  -7.835  1.00 44.81  ? 580 ARG A O   1 
ATOM   4374 C CB  . ARG A 1 580 ? 14.608  -8.975  -7.659  1.00 45.51  ? 580 ARG A CB  1 
ATOM   4375 C CG  . ARG A 1 580 ? 15.215  -8.878  -9.045  1.00 46.06  ? 580 ARG A CG  1 
ATOM   4376 C CD  . ARG A 1 580 ? 16.336  -9.900  -9.225  1.00 47.07  ? 580 ARG A CD  1 
ATOM   4377 N NE  . ARG A 1 580 ? 16.831  -9.893  -10.595 1.00 47.42  ? 580 ARG A NE  1 
ATOM   4378 C CZ  . ARG A 1 580 ? 17.871  -10.598 -11.024 1.00 50.37  ? 580 ARG A CZ  1 
ATOM   4379 N NH1 . ARG A 1 580 ? 18.564  -11.372 -10.186 1.00 50.11  ? 580 ARG A NH1 1 
ATOM   4380 N NH2 . ARG A 1 580 ? 18.224  -10.533 -12.310 1.00 50.04  ? 580 ARG A NH2 1 
ATOM   4381 N N   . ASP A 1 581 ? 11.728  -8.210  -9.280  1.00 43.85  ? 581 ASP A N   1 
ATOM   4382 C CA  . ASP A 1 581 ? 10.767  -8.797  -10.195 1.00 43.56  ? 581 ASP A CA  1 
ATOM   4383 C C   . ASP A 1 581 ? 11.514  -9.561  -11.271 1.00 43.41  ? 581 ASP A C   1 
ATOM   4384 O O   . ASP A 1 581 ? 12.490  -9.064  -11.842 1.00 42.12  ? 581 ASP A O   1 
ATOM   4385 C CB  . ASP A 1 581 ? 9.925   -7.716  -10.849 1.00 43.32  ? 581 ASP A CB  1 
ATOM   4386 C CG  . ASP A 1 581 ? 9.164   -6.883  -9.853  1.00 43.10  ? 581 ASP A CG  1 
ATOM   4387 O OD1 . ASP A 1 581 ? 9.086   -5.670  -10.068 1.00 42.43  ? 581 ASP A OD1 1 
ATOM   4388 O OD2 . ASP A 1 581 ? 8.628   -7.436  -8.870  1.00 43.25  ? 581 ASP A OD2 1 
ATOM   4389 N N   . LEU A 1 582 ? 11.045  -10.771 -11.541 1.00 44.02  ? 582 LEU A N   1 
ATOM   4390 C CA  . LEU A 1 582 ? 11.630  -11.624 -12.580 1.00 44.76  ? 582 LEU A CA  1 
ATOM   4391 C C   . LEU A 1 582 ? 10.667  -11.875 -13.761 1.00 45.07  ? 582 LEU A C   1 
ATOM   4392 O O   . LEU A 1 582 ? 9.474   -12.096 -13.557 1.00 45.43  ? 582 LEU A O   1 
ATOM   4393 C CB  . LEU A 1 582 ? 12.036  -12.939 -11.965 1.00 45.21  ? 582 LEU A CB  1 
ATOM   4394 C CG  . LEU A 1 582 ? 12.904  -12.901 -10.693 1.00 45.98  ? 582 LEU A CG  1 
ATOM   4395 C CD1 . LEU A 1 582 ? 12.898  -14.269 -10.067 1.00 44.40  ? 582 LEU A CD1 1 
ATOM   4396 C CD2 . LEU A 1 582 ? 14.314  -12.439 -11.017 1.00 46.40  ? 582 LEU A CD2 1 
ATOM   4397 N N   . TYR A 1 583 ? 11.196  -11.845 -14.990 1.00 44.83  ? 583 TYR A N   1 
ATOM   4398 C CA  . TYR A 1 583 ? 10.405  -12.064 -16.206 1.00 44.53  ? 583 TYR A CA  1 
ATOM   4399 C C   . TYR A 1 583 ? 10.618  -13.491 -16.712 1.00 44.44  ? 583 TYR A C   1 
ATOM   4400 O O   . TYR A 1 583 ? 11.729  -13.856 -17.074 1.00 44.56  ? 583 TYR A O   1 
ATOM   4401 C CB  . TYR A 1 583 ? 10.843  -11.063 -17.277 1.00 45.02  ? 583 TYR A CB  1 
ATOM   4402 C CG  . TYR A 1 583 ? 10.192  -11.218 -18.648 1.00 45.21  ? 583 TYR A CG  1 
ATOM   4403 C CD1 . TYR A 1 583 ? 8.923   -10.711 -18.897 1.00 45.77  ? 583 TYR A CD1 1 
ATOM   4404 C CD2 . TYR A 1 583 ? 10.861  -11.855 -19.697 1.00 44.67  ? 583 TYR A CD2 1 
ATOM   4405 C CE1 . TYR A 1 583 ? 8.333   -10.831 -20.167 1.00 46.72  ? 583 TYR A CE1 1 
ATOM   4406 C CE2 . TYR A 1 583 ? 10.277  -11.984 -20.959 1.00 45.83  ? 583 TYR A CE2 1 
ATOM   4407 C CZ  . TYR A 1 583 ? 9.015   -11.474 -21.182 1.00 46.11  ? 583 TYR A CZ  1 
ATOM   4408 O OH  . TYR A 1 583 ? 8.433   -11.582 -22.428 1.00 47.81  ? 583 TYR A OH  1 
ATOM   4409 N N   . LEU A 1 584 ? 9.566   -14.306 -16.710 1.00 44.18  ? 584 LEU A N   1 
ATOM   4410 C CA  . LEU A 1 584 ? 9.659   -15.678 -17.211 1.00 44.45  ? 584 LEU A CA  1 
ATOM   4411 C C   . LEU A 1 584 ? 9.499   -15.604 -18.725 1.00 44.39  ? 584 LEU A C   1 
ATOM   4412 O O   . LEU A 1 584 ? 8.438   -15.241 -19.236 1.00 44.19  ? 584 LEU A O   1 
ATOM   4413 C CB  . LEU A 1 584 ? 8.586   -16.582 -16.600 1.00 44.24  ? 584 LEU A CB  1 
ATOM   4414 C CG  . LEU A 1 584 ? 8.506   -16.775 -15.071 1.00 45.42  ? 584 LEU A CG  1 
ATOM   4415 C CD1 . LEU A 1 584 ? 8.069   -18.183 -14.789 1.00 44.06  ? 584 LEU A CD1 1 
ATOM   4416 C CD2 . LEU A 1 584 ? 9.797   -16.477 -14.298 1.00 46.83  ? 584 LEU A CD2 1 
ATOM   4417 N N   . GLU A 1 585 ? 10.561  -15.902 -19.453 1.00 44.45  ? 585 GLU A N   1 
ATOM   4418 C CA  . GLU A 1 585 ? 10.553  -15.585 -20.857 1.00 45.23  ? 585 GLU A CA  1 
ATOM   4419 C C   . GLU A 1 585 ? 9.848   -16.674 -21.640 1.00 44.43  ? 585 GLU A C   1 
ATOM   4420 O O   . GLU A 1 585 ? 9.808   -17.833 -21.215 1.00 43.42  ? 585 GLU A O   1 
ATOM   4421 C CB  . GLU A 1 585 ? 11.966  -15.300 -21.349 1.00 45.52  ? 585 GLU A CB  1 
ATOM   4422 C CG  . GLU A 1 585 ? 12.826  -16.507 -21.604 1.00 48.42  ? 585 GLU A CG  1 
ATOM   4423 C CD  . GLU A 1 585 ? 14.319  -16.166 -21.596 1.00 49.53  ? 585 GLU A CD  1 
ATOM   4424 O OE1 . GLU A 1 585 ? 14.663  -15.005 -21.937 1.00 54.42  ? 585 GLU A OE1 1 
ATOM   4425 O OE2 . GLU A 1 585 ? 15.137  -17.062 -21.244 1.00 55.48  ? 585 GLU A OE2 1 
ATOM   4426 N N   . ASN A 1 586 ? 9.230   -16.265 -22.745 1.00 43.66  ? 586 ASN A N   1 
ATOM   4427 C CA  . ASN A 1 586 ? 8.535   -17.171 -23.649 1.00 44.09  ? 586 ASN A CA  1 
ATOM   4428 C C   . ASN A 1 586 ? 9.522   -17.948 -24.497 1.00 43.63  ? 586 ASN A C   1 
ATOM   4429 O O   . ASN A 1 586 ? 10.686  -17.521 -24.682 1.00 43.55  ? 586 ASN A O   1 
ATOM   4430 C CB  . ASN A 1 586 ? 7.604   -16.390 -24.591 1.00 43.55  ? 586 ASN A CB  1 
ATOM   4431 C CG  . ASN A 1 586 ? 6.199   -16.239 -24.049 1.00 44.34  ? 586 ASN A CG  1 
ATOM   4432 O OD1 . ASN A 1 586 ? 5.787   -16.956 -23.145 1.00 47.75  ? 586 ASN A OD1 1 
ATOM   4433 N ND2 . ASN A 1 586 ? 5.448   -15.308 -24.615 1.00 44.80  ? 586 ASN A ND2 1 
ATOM   4434 N N   . PRO A 1 587 ? 9.059   -19.076 -25.060 1.00 43.79  ? 587 PRO A N   1 
ATOM   4435 C CA  . PRO A 1 587 ? 9.939   -19.814 -25.938 1.00 44.46  ? 587 PRO A CA  1 
ATOM   4436 C C   . PRO A 1 587 ? 10.202  -18.997 -27.198 1.00 45.02  ? 587 PRO A C   1 
ATOM   4437 O O   . PRO A 1 587 ? 9.325   -18.258 -27.651 1.00 44.73  ? 587 PRO A O   1 
ATOM   4438 C CB  . PRO A 1 587 ? 9.143   -21.078 -26.237 1.00 44.47  ? 587 PRO A CB  1 
ATOM   4439 C CG  . PRO A 1 587 ? 7.720   -20.656 -26.081 1.00 44.33  ? 587 PRO A CG  1 
ATOM   4440 C CD  . PRO A 1 587 ? 7.727   -19.700 -24.957 1.00 43.57  ? 587 PRO A CD  1 
ATOM   4441 N N   . GLU A 1 588 ? 11.424  -19.079 -27.707 1.00 45.94  ? 588 GLU A N   1 
ATOM   4442 C CA  . GLU A 1 588 ? 11.785  -18.406 -28.933 1.00 46.62  ? 588 GLU A CA  1 
ATOM   4443 C C   . GLU A 1 588 ? 11.096  -19.111 -30.106 1.00 47.03  ? 588 GLU A C   1 
ATOM   4444 O O   . GLU A 1 588 ? 10.947  -20.328 -30.105 1.00 47.42  ? 588 GLU A O   1 
ATOM   4445 C CB  . GLU A 1 588 ? 13.312  -18.405 -29.104 1.00 46.74  ? 588 GLU A CB  1 
ATOM   4446 C CG  . GLU A 1 588 ? 13.796  -17.859 -30.454 1.00 47.15  ? 588 GLU A CG  1 
ATOM   4447 C CD  . GLU A 1 588 ? 15.295  -17.601 -30.491 1.00 47.59  ? 588 GLU A CD  1 
ATOM   4448 O OE1 . GLU A 1 588 ? 16.031  -18.253 -29.726 1.00 48.01  ? 588 GLU A OE1 1 
ATOM   4449 O OE2 . GLU A 1 588 ? 15.732  -16.736 -31.289 1.00 50.28  ? 588 GLU A OE2 1 
ATOM   4450 N N   . ILE A 1 589 ? 10.640  -18.343 -31.086 1.00 48.02  ? 589 ILE A N   1 
ATOM   4451 C CA  . ILE A 1 589 ? 10.193  -18.918 -32.349 1.00 48.19  ? 589 ILE A CA  1 
ATOM   4452 C C   . ILE A 1 589 ? 11.411  -18.920 -33.252 1.00 48.86  ? 589 ILE A C   1 
ATOM   4453 O O   . ILE A 1 589 ? 11.925  -17.863 -33.605 1.00 49.31  ? 589 ILE A O   1 
ATOM   4454 C CB  . ILE A 1 589 ? 9.070   -18.106 -32.984 1.00 48.55  ? 589 ILE A CB  1 
ATOM   4455 C CG1 . ILE A 1 589 ? 7.863   -18.037 -32.045 1.00 48.50  ? 589 ILE A CG1 1 
ATOM   4456 C CG2 . ILE A 1 589 ? 8.651   -18.738 -34.308 1.00 48.53  ? 589 ILE A CG2 1 
ATOM   4457 C CD1 . ILE A 1 589 ? 6.721   -17.243 -32.573 1.00 47.97  ? 589 ILE A CD1 1 
ATOM   4458 N N   . LYS A 1 590 ? 11.926  -20.102 -33.573 1.00 49.70  ? 590 LYS A N   1 
ATOM   4459 C CA  . LYS A 1 590 ? 12.990  -20.202 -34.565 1.00 50.20  ? 590 LYS A CA  1 
ATOM   4460 C C   . LYS A 1 590 ? 12.332  -19.900 -35.910 1.00 50.68  ? 590 LYS A C   1 
ATOM   4461 O O   . LYS A 1 590 ? 11.230  -20.374 -36.184 1.00 50.28  ? 590 LYS A O   1 
ATOM   4462 C CB  . LYS A 1 590 ? 13.628  -21.594 -34.575 1.00 50.17  ? 590 LYS A CB  1 
ATOM   4463 C CG  . LYS A 1 590 ? 15.132  -21.602 -34.869 1.00 50.18  ? 590 LYS A CG  1 
ATOM   4464 C CD  . LYS A 1 590 ? 15.643  -22.970 -34.060 0.00 50.00  ? 590 LYS A CD  1 
ATOM   4465 C CE  . LYS A 1 590 ? 17.090  -23.321 -34.410 0.00 50.00  ? 590 LYS A CE  1 
ATOM   4466 N NZ  . LYS A 1 590 ? 17.182  -24.492 -35.332 0.00 50.00  ? 590 LYS A NZ  1 
ATOM   4467 N N   . ILE A 1 591 ? 12.973  -19.056 -36.709 1.00 51.51  ? 591 ILE A N   1 
ATOM   4468 C CA  . ILE A 1 591 ? 12.472  -18.736 -38.043 1.00 52.10  ? 591 ILE A CA  1 
ATOM   4469 C C   . ILE A 1 591 ? 13.630  -18.902 -39.008 1.00 52.75  ? 591 ILE A C   1 
ATOM   4470 O O   . ILE A 1 591 ? 14.589  -18.130 -38.976 1.00 52.75  ? 591 ILE A O   1 
ATOM   4471 C CB  . ILE A 1 591 ? 11.893  -17.310 -38.129 1.00 52.09  ? 591 ILE A CB  1 
ATOM   4472 C CG1 . ILE A 1 591 ? 10.693  -17.167 -37.195 1.00 51.96  ? 591 ILE A CG1 1 
ATOM   4473 C CG2 . ILE A 1 591 ? 11.463  -16.986 -39.566 1.00 51.61  ? 591 ILE A CG2 1 
ATOM   4474 C CD1 . ILE A 1 591 ? 10.159  -15.754 -37.101 1.00 52.15  ? 591 ILE A CD1 1 
ATOM   4475 N N   . ARG A 1 592 ? 13.550  -19.940 -39.837 1.00 53.40  ? 592 ARG A N   1 
ATOM   4476 C CA  . ARG A 1 592 ? 14.620  -20.264 -40.767 1.00 54.01  ? 592 ARG A CA  1 
ATOM   4477 C C   . ARG A 1 592 ? 14.261  -19.903 -42.210 1.00 54.41  ? 592 ARG A C   1 
ATOM   4478 O O   . ARG A 1 592 ? 13.094  -19.959 -42.617 1.00 54.45  ? 592 ARG A O   1 
ATOM   4479 C CB  . ARG A 1 592 ? 14.987  -21.744 -40.653 1.00 54.32  ? 592 ARG A CB  1 
ATOM   4480 C CG  . ARG A 1 592 ? 15.404  -22.200 -39.249 1.00 55.52  ? 592 ARG A CG  1 
ATOM   4481 C CD  . ARG A 1 592 ? 16.232  -21.159 -38.460 1.00 56.45  ? 592 ARG A CD  1 
ATOM   4482 N NE  . ARG A 1 592 ? 17.272  -20.491 -39.249 1.00 56.96  ? 592 ARG A NE  1 
ATOM   4483 C CZ  . ARG A 1 592 ? 18.287  -19.791 -38.737 1.00 57.24  ? 592 ARG A CZ  1 
ATOM   4484 N NH1 . ARG A 1 592 ? 18.442  -19.663 -37.418 1.00 58.00  ? 592 ARG A NH1 1 
ATOM   4485 N NH2 . ARG A 1 592 ? 19.174  -19.230 -39.554 1.00 57.53  ? 592 ARG A NH2 1 
ATOM   4486 N N   . ILE A 1 593 ? 15.294  -19.552 -42.974 1.00 54.76  ? 593 ILE A N   1 
ATOM   4487 C CA  . ILE A 1 593 ? 15.133  -19.005 -44.318 1.00 54.81  ? 593 ILE A CA  1 
ATOM   4488 C C   . ILE A 1 593 ? 15.708  -19.959 -45.366 1.00 54.89  ? 593 ILE A C   1 
ATOM   4489 O O   . ILE A 1 593 ? 16.875  -19.851 -45.741 1.00 55.00  ? 593 ILE A O   1 
ATOM   4490 C CB  . ILE A 1 593 ? 15.821  -17.620 -44.438 1.00 54.86  ? 593 ILE A CB  1 
ATOM   4491 C CG1 . ILE A 1 593 ? 15.540  -16.760 -43.195 1.00 54.58  ? 593 ILE A CG1 1 
ATOM   4492 C CG2 . ILE A 1 593 ? 15.368  -16.914 -45.710 1.00 54.86  ? 593 ILE A CG2 1 
ATOM   4493 C CD1 . ILE A 1 593 ? 16.574  -16.921 -42.075 1.00 54.29  ? 593 ILE A CD1 1 
ATOM   4494 N N   . LEU A 1 594 ? 14.883  -20.896 -45.830 1.00 54.94  ? 594 LEU A N   1 
ATOM   4495 C CA  . LEU A 1 594 ? 15.289  -21.823 -46.888 1.00 55.08  ? 594 LEU A CA  1 
ATOM   4496 C C   . LEU A 1 594 ? 15.356  -21.080 -48.231 1.00 55.20  ? 594 LEU A C   1 
ATOM   4497 O O   . LEU A 1 594 ? 14.578  -20.151 -48.470 1.00 55.28  ? 594 LEU A O   1 
ATOM   4498 C CB  . LEU A 1 594 ? 14.318  -23.010 -46.994 1.00 55.09  ? 594 LEU A CB  1 
ATOM   4499 C CG  . LEU A 1 594 ? 13.815  -23.703 -45.717 1.00 55.03  ? 594 LEU A CG  1 
ATOM   4500 C CD1 . LEU A 1 594 ? 13.141  -25.026 -46.066 1.00 54.60  ? 594 LEU A CD1 1 
ATOM   4501 C CD2 . LEU A 1 594 ? 14.937  -23.926 -44.714 1.00 55.25  ? 594 LEU A CD2 1 
ATOM   4502 N N   . GLY A 1 595 ? 16.284  -21.488 -49.096 1.00 55.16  ? 595 GLY A N   1 
ATOM   4503 C CA  . GLY A 1 595 ? 16.462  -20.853 -50.404 1.00 55.22  ? 595 GLY A CA  1 
ATOM   4504 C C   . GLY A 1 595 ? 17.451  -19.700 -50.361 1.00 55.28  ? 595 GLY A C   1 
ATOM   4505 O O   . GLY A 1 595 ? 18.078  -19.453 -49.329 1.00 55.29  ? 595 GLY A O   1 
ATOM   4506 N N   . GLU A 1 596 ? 17.574  -18.973 -51.468 1.00 55.36  ? 596 GLU A N   1 
ATOM   4507 C CA  . GLU A 1 596 ? 18.549  -17.887 -51.569 1.00 55.36  ? 596 GLU A CA  1 
ATOM   4508 C C   . GLU A 1 596 ? 18.013  -16.561 -51.025 1.00 55.44  ? 596 GLU A C   1 
ATOM   4509 O O   . GLU A 1 596 ? 16.840  -16.456 -50.668 1.00 55.54  ? 596 GLU A O   1 
ATOM   4510 C CB  . GLU A 1 596 ? 19.010  -17.714 -53.018 1.00 55.26  ? 596 GLU A CB  1 
ATOM   4511 C CG  . GLU A 1 596 ? 20.138  -18.647 -53.427 0.00 50.00  ? 596 GLU A CG  1 
ATOM   4512 C CD  . GLU A 1 596 ? 19.773  -20.109 -53.265 0.00 50.00  ? 596 GLU A CD  1 
ATOM   4513 O OE1 . GLU A 1 596 ? 18.598  -20.399 -52.954 0.00 50.00  ? 596 GLU A OE1 1 
ATOM   4514 O OE2 . GLU A 1 596 ? 20.660  -20.969 -53.449 0.00 50.00  ? 596 GLU A OE2 1 
ATOM   4515 N N   . PRO A 1 597 ? 18.881  -15.553 -50.966 1.00 55.43  ? 597 PRO A N   1 
ATOM   4516 C CA  . PRO A 1 597 ? 18.460  -14.185 -50.659 1.00 55.20  ? 597 PRO A CA  1 
ATOM   4517 C C   . PRO A 1 597 ? 18.592  -13.208 -51.841 1.00 55.09  ? 597 PRO A C   1 
ATOM   4518 O O   . PRO A 1 597 ? 18.508  -11.993 -51.639 1.00 55.14  ? 597 PRO A O   1 
ATOM   4519 C CB  . PRO A 1 597 ? 19.435  -13.793 -49.552 1.00 55.26  ? 597 PRO A CB  1 
ATOM   4520 C CG  . PRO A 1 597 ? 20.731  -14.475 -49.970 1.00 55.47  ? 597 PRO A CG  1 
ATOM   4521 C CD  . PRO A 1 597 ? 20.341  -15.703 -50.791 1.00 55.45  ? 597 PRO A CD  1 
ATOM   4522 N N   . LYS A 1 598 ? 18.791  -13.737 -53.044 1.00 54.82  ? 598 LYS A N   1 
ATOM   4523 C CA  . LYS A 1 598 ? 18.925  -12.903 -54.233 1.00 54.58  ? 598 LYS A CA  1 
ATOM   4524 C C   . LYS A 1 598 ? 17.656  -12.098 -54.494 1.00 54.31  ? 598 LYS A C   1 
ATOM   4525 O O   . LYS A 1 598 ? 16.563  -12.499 -54.093 1.00 54.27  ? 598 LYS A O   1 
ATOM   4526 C CB  . LYS A 1 598 ? 19.263  -13.761 -55.454 1.00 54.50  ? 598 LYS A CB  1 
ATOM   4527 C CG  . LYS A 1 598 ? 20.721  -13.690 -55.878 0.00 50.00  ? 598 LYS A CG  1 
ATOM   4528 C CD  . LYS A 1 598 ? 21.610  -13.246 -54.728 0.00 50.00  ? 598 LYS A CD  1 
ATOM   4529 C CE  . LYS A 1 598 ? 22.729  -12.339 -55.212 0.00 50.00  ? 598 LYS A CE  1 
ATOM   4530 N NZ  . LYS A 1 598 ? 23.992  -12.564 -54.456 0.00 50.00  ? 598 LYS A NZ  1 
ATOM   4531 N N   . GLN A 1 599 ? 17.807  -10.961 -55.166 1.00 54.02  ? 599 GLN A N   1 
ATOM   4532 C CA  . GLN A 1 599 ? 16.752  -9.939  -55.199 1.00 53.72  ? 599 GLN A CA  1 
ATOM   4533 C C   . GLN A 1 599 ? 15.581  -10.271 -56.140 1.00 53.42  ? 599 GLN A C   1 
ATOM   4534 O O   . GLN A 1 599 ? 15.086  -9.385  -56.842 1.00 53.54  ? 599 GLN A O   1 
ATOM   4535 C CB  . GLN A 1 599 ? 17.363  -8.589  -55.618 1.00 53.82  ? 599 GLN A CB  1 
ATOM   4536 C CG  . GLN A 1 599 ? 18.553  -8.115  -54.777 1.00 53.81  ? 599 GLN A CG  1 
ATOM   4537 C CD  . GLN A 1 599 ? 19.530  -7.266  -55.578 1.00 53.72  ? 599 GLN A CD  1 
ATOM   4538 O OE1 . GLN A 1 599 ? 20.194  -7.760  -56.491 1.00 53.63  ? 599 GLN A OE1 1 
ATOM   4539 N NE2 . GLN A 1 599 ? 19.626  -5.987  -55.234 1.00 53.65  ? 599 GLN A NE2 1 
ATOM   4540 N N   . LYS A 1 600 ? 15.133  -11.526 -56.136 1.00 52.88  ? 600 LYS A N   1 
ATOM   4541 C CA  . LYS A 1 600 ? 14.301  -12.050 -57.222 1.00 52.47  ? 600 LYS A CA  1 
ATOM   4542 C C   . LYS A 1 600 ? 13.163  -12.962 -56.746 1.00 51.67  ? 600 LYS A C   1 
ATOM   4543 O O   . LYS A 1 600 ? 12.023  -12.523 -56.598 1.00 51.72  ? 600 LYS A O   1 
ATOM   4544 C CB  . LYS A 1 600 ? 15.163  -12.780 -58.253 1.00 52.32  ? 600 LYS A CB  1 
ATOM   4545 C CG  . LYS A 1 600 ? 16.145  -11.882 -58.988 0.00 50.00  ? 600 LYS A CG  1 
ATOM   4546 C CD  . LYS A 1 600 ? 15.422  -10.892 -59.887 0.00 50.00  ? 600 LYS A CD  1 
ATOM   4547 C CE  . LYS A 1 600 ? 16.403  -9.974  -60.599 0.00 50.00  ? 600 LYS A CE  1 
ATOM   4548 N NZ  . LYS A 1 600 ? 15.711  -9.025  -61.513 0.00 50.00  ? 600 LYS A NZ  1 
ATOM   4549 N N   . ARG A 1 601 ? 13.487  -14.231 -56.510 1.00 50.74  ? 601 ARG A N   1 
ATOM   4550 C CA  . ARG A 1 601 ? 12.575  -15.356 -56.754 1.00 49.73  ? 601 ARG A CA  1 
ATOM   4551 C C   . ARG A 1 601 ? 12.201  -16.211 -55.528 1.00 49.14  ? 601 ARG A C   1 
ATOM   4552 O O   . ARG A 1 601 ? 12.347  -15.768 -54.396 1.00 49.12  ? 601 ARG A O   1 
ATOM   4553 C CB  . ARG A 1 601 ? 13.197  -16.220 -57.857 1.00 49.99  ? 601 ARG A CB  1 
ATOM   4554 C CG  . ARG A 1 601 ? 12.267  -16.525 -59.029 1.00 50.58  ? 601 ARG A CG  1 
ATOM   4555 C CD  . ARG A 1 601 ? 11.941  -15.267 -59.846 1.00 51.10  ? 601 ARG A CD  1 
ATOM   4556 N NE  . ARG A 1 601 ? 10.721  -14.597 -59.389 1.00 51.21  ? 601 ARG A NE  1 
ATOM   4557 C CZ  . ARG A 1 601 ? 9.480   -15.003 -59.662 1.00 51.56  ? 601 ARG A CZ  1 
ATOM   4558 N NH1 . ARG A 1 601 ? 9.263   -16.095 -60.393 1.00 52.05  ? 601 ARG A NH1 1 
ATOM   4559 N NH2 . ARG A 1 601 ? 8.443   -14.315 -59.199 1.00 51.60  ? 601 ARG A NH2 1 
ATOM   4560 N N   . LYS A 1 602 ? 11.727  -17.435 -55.786 1.00 48.36  ? 602 LYS A N   1 
ATOM   4561 C CA  . LYS A 1 602 ? 11.096  -18.323 -54.789 1.00 47.91  ? 602 LYS A CA  1 
ATOM   4562 C C   . LYS A 1 602 ? 11.883  -18.520 -53.491 1.00 47.64  ? 602 LYS A C   1 
ATOM   4563 O O   . LYS A 1 602 ? 13.116  -18.531 -53.495 1.00 47.63  ? 602 LYS A O   1 
ATOM   4564 C CB  . LYS A 1 602 ? 10.829  -19.702 -55.411 1.00 47.70  ? 602 LYS A CB  1 
ATOM   4565 C CG  . LYS A 1 602 ? 9.837   -19.699 -56.574 1.00 47.45  ? 602 LYS A CG  1 
ATOM   4566 C CD  . LYS A 1 602 ? 9.680   -21.089 -57.170 1.00 47.43  ? 602 LYS A CD  1 
ATOM   4567 C CE  . LYS A 1 602 ? 8.709   -21.094 -58.338 1.00 47.10  ? 602 LYS A CE  1 
ATOM   4568 N NZ  . LYS A 1 602 ? 8.491   -22.465 -58.876 1.00 46.73  ? 602 LYS A NZ  1 
ATOM   4569 N N   . LEU A 1 603 ? 11.147  -18.712 -52.394 1.00 47.42  ? 603 LEU A N   1 
ATOM   4570 C CA  . LEU A 1 603 ? 11.721  -18.730 -51.049 1.00 47.42  ? 603 LEU A CA  1 
ATOM   4571 C C   . LEU A 1 603 ? 10.789  -19.452 -50.060 1.00 47.41  ? 603 LEU A C   1 
ATOM   4572 O O   . LEU A 1 603 ? 9.571   -19.250 -50.085 1.00 47.35  ? 603 LEU A O   1 
ATOM   4573 C CB  . LEU A 1 603 ? 11.957  -17.283 -50.588 1.00 47.41  ? 603 LEU A CB  1 
ATOM   4574 C CG  . LEU A 1 603 ? 13.065  -16.968 -49.579 1.00 47.35  ? 603 LEU A CG  1 
ATOM   4575 C CD1 . LEU A 1 603 ? 12.680  -17.443 -48.179 1.00 47.25  ? 603 LEU A CD1 1 
ATOM   4576 C CD2 . LEU A 1 603 ? 14.401  -17.558 -50.020 1.00 47.01  ? 603 LEU A CD2 1 
ATOM   4577 N N   . VAL A 1 604 ? 11.362  -20.282 -49.188 1.00 47.38  ? 604 VAL A N   1 
ATOM   4578 C CA  . VAL A 1 604 ? 10.571  -21.006 -48.184 1.00 47.35  ? 604 VAL A CA  1 
ATOM   4579 C C   . VAL A 1 604 ? 11.022  -20.675 -46.752 1.00 47.23  ? 604 VAL A C   1 
ATOM   4580 O O   . VAL A 1 604 ? 12.219  -20.604 -46.461 1.00 47.02  ? 604 VAL A O   1 
ATOM   4581 C CB  . VAL A 1 604 ? 10.629  -22.536 -48.409 1.00 47.24  ? 604 VAL A CB  1 
ATOM   4582 C CG1 . VAL A 1 604 ? 9.372   -23.195 -47.859 1.00 47.28  ? 604 VAL A CG1 1 
ATOM   4583 C CG2 . VAL A 1 604 ? 10.780  -22.850 -49.879 1.00 47.43  ? 604 VAL A CG2 1 
ATOM   4584 N N   . ALA A 1 605 ? 10.045  -20.475 -45.870 1.00 47.34  ? 605 ALA A N   1 
ATOM   4585 C CA  . ALA A 1 605 ? 10.293  -20.092 -44.477 1.00 47.36  ? 605 ALA A CA  1 
ATOM   4586 C C   . ALA A 1 605 ? 9.919   -21.239 -43.542 1.00 47.35  ? 605 ALA A C   1 
ATOM   4587 O O   . ALA A 1 605 ? 8.765   -21.682 -43.524 1.00 46.91  ? 605 ALA A O   1 
ATOM   4588 C CB  . ALA A 1 605 ? 9.490   -18.856 -44.120 1.00 47.32  ? 605 ALA A CB  1 
ATOM   4589 N N   . GLU A 1 606 ? 10.904  -21.708 -42.777 1.00 47.62  ? 606 GLU A N   1 
ATOM   4590 C CA  . GLU A 1 606 ? 10.701  -22.732 -41.748 1.00 47.75  ? 606 GLU A CA  1 
ATOM   4591 C C   . GLU A 1 606 ? 10.693  -22.088 -40.357 1.00 47.78  ? 606 GLU A C   1 
ATOM   4592 O O   . GLU A 1 606 ? 11.719  -21.576 -39.897 1.00 47.67  ? 606 GLU A O   1 
ATOM   4593 C CB  . GLU A 1 606 ? 11.805  -23.783 -41.834 1.00 47.75  ? 606 GLU A CB  1 
ATOM   4594 C CG  . GLU A 1 606 ? 11.623  -24.970 -40.915 1.00 47.79  ? 606 GLU A CG  1 
ATOM   4595 C CD  . GLU A 1 606 ? 12.635  -26.059 -41.204 1.00 48.04  ? 606 GLU A CD  1 
ATOM   4596 O OE1 . GLU A 1 606 ? 12.219  -27.193 -41.519 1.00 47.36  ? 606 GLU A OE1 1 
ATOM   4597 O OE2 . GLU A 1 606 ? 13.850  -25.770 -41.139 1.00 48.87  ? 606 GLU A OE2 1 
ATOM   4598 N N   . VAL A 1 607 ? 9.531   -22.114 -39.703 1.00 47.65  ? 607 VAL A N   1 
ATOM   4599 C CA  . VAL A 1 607 ? 9.387   -21.588 -38.348 1.00 47.71  ? 607 VAL A CA  1 
ATOM   4600 C C   . VAL A 1 607 ? 9.035   -22.695 -37.344 1.00 47.77  ? 607 VAL A C   1 
ATOM   4601 O O   . VAL A 1 607 ? 8.183   -23.544 -37.620 1.00 47.71  ? 607 VAL A O   1 
ATOM   4602 C CB  . VAL A 1 607 ? 8.325   -20.484 -38.282 1.00 47.81  ? 607 VAL A CB  1 
ATOM   4603 C CG1 . VAL A 1 607 ? 8.385   -19.644 -39.542 1.00 47.87  ? 607 VAL A CG1 1 
ATOM   4604 C CG2 . VAL A 1 607 ? 6.920   -21.074 -38.097 1.00 47.90  ? 607 VAL A CG2 1 
ATOM   4605 N N   . SER A 1 608 ? 9.686   -22.658 -36.177 1.00 47.58  ? 608 SER A N   1 
ATOM   4606 C CA  . SER A 1 608 ? 9.498   -23.671 -35.138 1.00 47.18  ? 608 SER A CA  1 
ATOM   4607 C C   . SER A 1 608 ? 9.480   -23.100 -33.710 1.00 46.92  ? 608 SER A C   1 
ATOM   4608 O O   . SER A 1 608 ? 9.791   -21.931 -33.476 1.00 46.98  ? 608 SER A O   1 
ATOM   4609 C CB  . SER A 1 608 ? 10.596  -24.722 -35.245 1.00 47.43  ? 608 SER A CB  1 
ATOM   4610 O OG  . SER A 1 608 ? 11.847  -24.171 -34.885 1.00 48.54  ? 608 SER A OG  1 
ATOM   4611 N N   . LEU A 1 609 ? 9.120   -23.964 -32.767 1.00 46.26  ? 609 LEU A N   1 
ATOM   4612 C CA  . LEU A 1 609 ? 8.933   -23.610 -31.363 1.00 45.53  ? 609 LEU A CA  1 
ATOM   4613 C C   . LEU A 1 609 ? 8.932   -24.900 -30.535 1.00 44.99  ? 609 LEU A C   1 
ATOM   4614 O O   . LEU A 1 609 ? 8.225   -25.850 -30.874 1.00 44.58  ? 609 LEU A O   1 
ATOM   4615 C CB  . LEU A 1 609 ? 7.599   -22.883 -31.193 1.00 45.59  ? 609 LEU A CB  1 
ATOM   4616 C CG  . LEU A 1 609 ? 7.039   -22.715 -29.776 1.00 45.83  ? 609 LEU A CG  1 
ATOM   4617 C CD1 . LEU A 1 609 ? 6.365   -21.350 -29.595 1.00 44.58  ? 609 LEU A CD1 1 
ATOM   4618 C CD2 . LEU A 1 609 ? 6.075   -23.842 -29.450 1.00 45.50  ? 609 LEU A CD2 1 
ATOM   4619 N N   . GLN A 1 610 ? 9.719   -24.934 -29.465 1.00 44.17  ? 610 GLN A N   1 
ATOM   4620 C CA  . GLN A 1 610 ? 9.701   -26.079 -28.555 1.00 43.90  ? 610 GLN A CA  1 
ATOM   4621 C C   . GLN A 1 610 ? 8.742   -25.780 -27.417 1.00 43.23  ? 610 GLN A C   1 
ATOM   4622 O O   . GLN A 1 610 ? 8.827   -24.718 -26.805 1.00 43.08  ? 610 GLN A O   1 
ATOM   4623 C CB  . GLN A 1 610 ? 11.093  -26.360 -28.006 1.00 43.90  ? 610 GLN A CB  1 
ATOM   4624 C CG  . GLN A 1 610 ? 11.185  -27.663 -27.248 1.00 43.87  ? 610 GLN A CG  1 
ATOM   4625 C CD  . GLN A 1 610 ? 12.295  -27.689 -26.214 1.00 44.44  ? 610 GLN A CD  1 
ATOM   4626 O OE1 . GLN A 1 610 ? 12.988  -28.702 -26.068 1.00 44.34  ? 610 GLN A OE1 1 
ATOM   4627 N NE2 . GLN A 1 610 ? 12.461  -26.589 -25.474 1.00 44.03  ? 610 GLN A NE2 1 
ATOM   4628 N N   . ASN A 1 611 ? 7.821   -26.701 -27.152 1.00 42.57  ? 611 ASN A N   1 
ATOM   4629 C CA  . ASN A 1 611 ? 6.918   -26.580 -26.013 1.00 42.48  ? 611 ASN A CA  1 
ATOM   4630 C C   . ASN A 1 611 ? 7.737   -26.601 -24.712 1.00 42.07  ? 611 ASN A C   1 
ATOM   4631 O O   . ASN A 1 611 ? 8.300   -27.642 -24.357 1.00 41.73  ? 611 ASN A O   1 
ATOM   4632 C CB  . ASN A 1 611 ? 5.904   -27.731 -26.029 1.00 42.50  ? 611 ASN A CB  1 
ATOM   4633 C CG  . ASN A 1 611 ? 4.908   -27.678 -24.873 1.00 42.55  ? 611 ASN A CG  1 
ATOM   4634 O OD1 . ASN A 1 611 ? 4.801   -26.678 -24.166 1.00 43.90  ? 611 ASN A OD1 1 
ATOM   4635 N ND2 . ASN A 1 611 ? 4.167   -28.766 -24.685 1.00 42.42  ? 611 ASN A ND2 1 
ATOM   4636 N N   . PRO A 1 612 ? 7.801   -25.462 -23.993 1.00 41.64  ? 612 PRO A N   1 
ATOM   4637 C CA  . PRO A 1 612 ? 8.669   -25.355 -22.808 1.00 41.57  ? 612 PRO A CA  1 
ATOM   4638 C C   . PRO A 1 612 ? 8.030   -25.930 -21.546 1.00 41.47  ? 612 PRO A C   1 
ATOM   4639 O O   . PRO A 1 612 ? 8.723   -26.185 -20.551 1.00 40.88  ? 612 PRO A O   1 
ATOM   4640 C CB  . PRO A 1 612 ? 8.841   -23.853 -22.650 1.00 41.73  ? 612 PRO A CB  1 
ATOM   4641 C CG  . PRO A 1 612 ? 7.542   -23.290 -23.118 1.00 41.48  ? 612 PRO A CG  1 
ATOM   4642 C CD  . PRO A 1 612 ? 7.037   -24.219 -24.208 1.00 41.74  ? 612 PRO A CD  1 
ATOM   4643 N N   . LEU A 1 613 ? 6.715   -26.129 -21.597 1.00 41.24  ? 613 LEU A N   1 
ATOM   4644 C CA  . LEU A 1 613 ? 5.961   -26.594 -20.457 1.00 41.14  ? 613 LEU A CA  1 
ATOM   4645 C C   . LEU A 1 613 ? 6.197   -28.084 -20.249 1.00 41.32  ? 613 LEU A C   1 
ATOM   4646 O O   . LEU A 1 613 ? 6.623   -28.783 -21.173 1.00 40.96  ? 613 LEU A O   1 
ATOM   4647 C CB  . LEU A 1 613 ? 4.465   -26.343 -20.670 1.00 40.84  ? 613 LEU A CB  1 
ATOM   4648 C CG  . LEU A 1 613 ? 4.004   -24.944 -21.092 1.00 39.91  ? 613 LEU A CG  1 
ATOM   4649 C CD1 . LEU A 1 613 ? 2.512   -24.809 -20.878 1.00 38.78  ? 613 LEU A CD1 1 
ATOM   4650 C CD2 . LEU A 1 613 ? 4.732   -23.827 -20.358 1.00 39.09  ? 613 LEU A CD2 1 
ATOM   4651 N N   . PRO A 1 614 ? 5.927   -28.572 -19.023 1.00 41.59  ? 614 PRO A N   1 
ATOM   4652 C CA  . PRO A 1 614 ? 5.858   -29.992 -18.726 1.00 41.74  ? 614 PRO A CA  1 
ATOM   4653 C C   . PRO A 1 614 ? 4.510   -30.609 -19.116 1.00 41.98  ? 614 PRO A C   1 
ATOM   4654 O O   . PRO A 1 614 ? 4.222   -31.746 -18.735 1.00 41.67  ? 614 PRO A O   1 
ATOM   4655 C CB  . PRO A 1 614 ? 6.031   -30.023 -17.207 1.00 41.85  ? 614 PRO A CB  1 
ATOM   4656 C CG  . PRO A 1 614 ? 5.385   -28.769 -16.758 1.00 41.63  ? 614 PRO A CG  1 
ATOM   4657 C CD  . PRO A 1 614 ? 5.690   -27.755 -17.818 1.00 41.58  ? 614 PRO A CD  1 
ATOM   4658 N N   . VAL A 1 615 ? 3.691   -29.863 -19.856 1.00 42.09  ? 615 VAL A N   1 
ATOM   4659 C CA  . VAL A 1 615 ? 2.382   -30.335 -20.292 1.00 42.45  ? 615 VAL A CA  1 
ATOM   4660 C C   . VAL A 1 615 ? 2.182   -30.058 -21.776 1.00 42.79  ? 615 VAL A C   1 
ATOM   4661 O O   . VAL A 1 615 ? 2.803   -29.153 -22.339 1.00 42.22  ? 615 VAL A O   1 
ATOM   4662 C CB  . VAL A 1 615 ? 1.249   -29.651 -19.513 1.00 42.39  ? 615 VAL A CB  1 
ATOM   4663 C CG1 . VAL A 1 615 ? 1.278   -30.078 -18.053 1.00 42.68  ? 615 VAL A CG1 1 
ATOM   4664 C CG2 . VAL A 1 615 ? 1.346   -28.136 -19.647 1.00 42.36  ? 615 VAL A CG2 1 
ATOM   4665 N N   . ALA A 1 616 ? 1.298   -30.841 -22.393 1.00 43.18  ? 616 ALA A N   1 
ATOM   4666 C CA  . ALA A 1 616 ? 1.043   -30.745 -23.828 1.00 43.53  ? 616 ALA A CA  1 
ATOM   4667 C C   . ALA A 1 616 ? 0.263   -29.485 -24.164 1.00 43.75  ? 616 ALA A C   1 
ATOM   4668 O O   . ALA A 1 616 ? -0.551  -29.009 -23.369 1.00 43.35  ? 616 ALA A O   1 
ATOM   4669 C CB  . ALA A 1 616 ? 0.295   -31.975 -24.330 1.00 43.32  ? 616 ALA A CB  1 
ATOM   4670 N N   . LEU A 1 617 ? 0.518   -28.974 -25.364 1.00 44.39  ? 617 LEU A N   1 
ATOM   4671 C CA  . LEU A 1 617 ? -0.052  -27.716 -25.838 1.00 44.94  ? 617 LEU A CA  1 
ATOM   4672 C C   . LEU A 1 617 ? -1.203  -28.019 -26.794 1.00 45.49  ? 617 LEU A C   1 
ATOM   4673 O O   . LEU A 1 617 ? -1.030  -28.779 -27.749 1.00 45.43  ? 617 LEU A O   1 
ATOM   4674 C CB  . LEU A 1 617 ? 1.040   -26.904 -26.550 1.00 44.86  ? 617 LEU A CB  1 
ATOM   4675 C CG  . LEU A 1 617 ? 1.365   -25.493 -26.055 1.00 44.73  ? 617 LEU A CG  1 
ATOM   4676 C CD1 . LEU A 1 617 ? 1.158   -25.326 -24.564 1.00 44.13  ? 617 LEU A CD1 1 
ATOM   4677 C CD2 . LEU A 1 617 ? 2.800   -25.122 -26.435 1.00 44.75  ? 617 LEU A CD2 1 
ATOM   4678 N N   . GLU A 1 618 ? -2.373  -27.437 -26.525 1.00 46.21  ? 618 GLU A N   1 
ATOM   4679 C CA  . GLU A 1 618 ? -3.575  -27.662 -27.340 1.00 46.72  ? 618 GLU A CA  1 
ATOM   4680 C C   . GLU A 1 618 ? -3.913  -26.428 -28.185 1.00 47.26  ? 618 GLU A C   1 
ATOM   4681 O O   . GLU A 1 618 ? -3.697  -25.289 -27.757 1.00 47.49  ? 618 GLU A O   1 
ATOM   4682 C CB  . GLU A 1 618 ? -4.768  -28.013 -26.448 1.00 46.76  ? 618 GLU A CB  1 
ATOM   4683 C CG  . GLU A 1 618 ? -4.628  -29.323 -25.660 1.00 47.03  ? 618 GLU A CG  1 
ATOM   4684 C CD  . GLU A 1 618 ? -5.307  -30.502 -26.339 1.00 47.14  ? 618 GLU A CD  1 
ATOM   4685 O OE1 . GLU A 1 618 ? -5.128  -30.668 -27.563 1.00 47.30  ? 618 GLU A OE1 1 
ATOM   4686 O OE2 . GLU A 1 618 ? -6.019  -31.265 -25.647 1.00 47.47  ? 618 GLU A OE2 1 
ATOM   4687 N N   . GLY A 1 619 ? -4.436  -26.660 -29.387 1.00 47.73  ? 619 GLY A N   1 
ATOM   4688 C CA  . GLY A 1 619 ? -4.865  -25.579 -30.271 1.00 48.05  ? 619 GLY A CA  1 
ATOM   4689 C C   . GLY A 1 619 ? -3.720  -24.706 -30.744 1.00 48.53  ? 619 GLY A C   1 
ATOM   4690 O O   . GLY A 1 619 ? -3.808  -23.476 -30.693 1.00 48.60  ? 619 GLY A O   1 
ATOM   4691 N N   . CYS A 1 620 ? -2.643  -25.343 -31.197 1.00 49.00  ? 620 CYS A N   1 
ATOM   4692 C CA  . CYS A 1 620 ? -1.486  -24.625 -31.719 1.00 49.40  ? 620 CYS A CA  1 
ATOM   4693 C C   . CYS A 1 620 ? -1.818  -24.078 -33.098 1.00 49.76  ? 620 CYS A C   1 
ATOM   4694 O O   . CYS A 1 620 ? -2.385  -24.786 -33.939 1.00 49.79  ? 620 CYS A O   1 
ATOM   4695 C CB  . CYS A 1 620 ? -0.263  -25.540 -31.831 1.00 49.51  ? 620 CYS A CB  1 
ATOM   4696 S SG  . CYS A 1 620 ? 0.260   -26.333 -30.303 1.00 50.21  ? 620 CYS A SG  1 
ATOM   4697 N N   . THR A 1 621 ? -1.471  -22.814 -33.319 1.00 50.11  ? 621 THR A N   1 
ATOM   4698 C CA  . THR A 1 621 ? -1.636  -22.185 -34.623 1.00 50.18  ? 621 THR A CA  1 
ATOM   4699 C C   . THR A 1 621 ? -0.598  -21.087 -34.800 1.00 50.46  ? 621 THR A C   1 
ATOM   4700 O O   . THR A 1 621 ? -0.447  -20.218 -33.928 1.00 50.86  ? 621 THR A O   1 
ATOM   4701 C CB  . THR A 1 621 ? -3.063  -21.601 -34.814 1.00 50.42  ? 621 THR A CB  1 
ATOM   4702 O OG1 . THR A 1 621 ? -3.501  -20.966 -33.608 1.00 50.71  ? 621 THR A OG1 1 
ATOM   4703 C CG2 . THR A 1 621 ? -4.061  -22.697 -35.190 1.00 50.52  ? 621 THR A CG2 1 
ATOM   4704 N N   . PHE A 1 622 ? 0.145   -21.166 -35.904 1.00 50.22  ? 622 PHE A N   1 
ATOM   4705 C CA  . PHE A 1 622 ? 1.015   -20.087 -36.343 1.00 50.01  ? 622 PHE A CA  1 
ATOM   4706 C C   . PHE A 1 622 ? 0.234   -19.176 -37.284 1.00 49.84  ? 622 PHE A C   1 
ATOM   4707 O O   . PHE A 1 622 ? -0.478  -19.663 -38.156 1.00 49.58  ? 622 PHE A O   1 
ATOM   4708 C CB  . PHE A 1 622 ? 2.228   -20.616 -37.122 1.00 50.37  ? 622 PHE A CB  1 
ATOM   4709 C CG  . PHE A 1 622 ? 3.213   -21.398 -36.293 1.00 50.42  ? 622 PHE A CG  1 
ATOM   4710 C CD1 . PHE A 1 622 ? 4.336   -20.777 -35.752 1.00 50.87  ? 622 PHE A CD1 1 
ATOM   4711 C CD2 . PHE A 1 622 ? 3.044   -22.761 -36.089 1.00 51.08  ? 622 PHE A CD2 1 
ATOM   4712 C CE1 . PHE A 1 622 ? 5.262   -21.504 -34.995 1.00 50.88  ? 622 PHE A CE1 1 
ATOM   4713 C CE2 . PHE A 1 622 ? 3.963   -23.492 -35.341 1.00 50.64  ? 622 PHE A CE2 1 
ATOM   4714 C CZ  . PHE A 1 622 ? 5.075   -22.864 -34.796 1.00 50.85  ? 622 PHE A CZ  1 
ATOM   4715 N N   . THR A 1 623 ? 0.369   -17.865 -37.097 1.00 49.44  ? 623 THR A N   1 
ATOM   4716 C CA  . THR A 1 623 ? 0.001   -16.886 -38.114 1.00 49.09  ? 623 THR A CA  1 
ATOM   4717 C C   . THR A 1 623 ? 1.282   -16.200 -38.540 1.00 48.88  ? 623 THR A C   1 
ATOM   4718 O O   . THR A 1 623 ? 2.115   -15.884 -37.695 1.00 49.01  ? 623 THR A O   1 
ATOM   4719 C CB  . THR A 1 623 ? -0.961  -15.819 -37.587 1.00 49.14  ? 623 THR A CB  1 
ATOM   4720 O OG1 . THR A 1 623 ? -2.087  -16.449 -36.977 1.00 49.29  ? 623 THR A OG1 1 
ATOM   4721 C CG2 . THR A 1 623 ? -1.447  -14.929 -38.726 1.00 49.08  ? 623 THR A CG2 1 
ATOM   4722 N N   . VAL A 1 624 ? 1.444   -15.974 -39.844 1.00 48.35  ? 624 VAL A N   1 
ATOM   4723 C CA  . VAL A 1 624 ? 2.671   -15.383 -40.371 1.00 47.88  ? 624 VAL A CA  1 
ATOM   4724 C C   . VAL A 1 624 ? 2.390   -14.363 -41.462 1.00 47.63  ? 624 VAL A C   1 
ATOM   4725 O O   . VAL A 1 624 ? 1.532   -14.577 -42.326 1.00 47.96  ? 624 VAL A O   1 
ATOM   4726 C CB  . VAL A 1 624 ? 3.613   -16.447 -40.942 1.00 47.34  ? 624 VAL A CB  1 
ATOM   4727 C CG1 . VAL A 1 624 ? 4.885   -15.805 -41.470 1.00 47.60  ? 624 VAL A CG1 1 
ATOM   4728 C CG2 . VAL A 1 624 ? 3.938   -17.489 -39.891 1.00 47.71  ? 624 VAL A CG2 1 
ATOM   4729 N N   . GLU A 1 625 ? 3.128   -13.258 -41.425 1.00 47.55  ? 625 GLU A N   1 
ATOM   4730 C CA  . GLU A 1 625 ? 3.077   -12.270 -42.492 1.00 47.22  ? 625 GLU A CA  1 
ATOM   4731 C C   . GLU A 1 625 ? 4.317   -11.398 -42.514 1.00 46.75  ? 625 GLU A C   1 
ATOM   4732 O O   . GLU A 1 625 ? 5.124   -11.447 -41.603 1.00 46.47  ? 625 GLU A O   1 
ATOM   4733 C CB  . GLU A 1 625 ? 1.823   -11.417 -42.367 1.00 47.51  ? 625 GLU A CB  1 
ATOM   4734 C CG  . GLU A 1 625 ? 1.712   -10.636 -41.094 1.00 47.35  ? 625 GLU A CG  1 
ATOM   4735 C CD  . GLU A 1 625 ? 0.372   -9.977  -40.996 1.00 46.81  ? 625 GLU A CD  1 
ATOM   4736 O OE1 . GLU A 1 625 ? 0.268   -8.768  -41.275 1.00 48.93  ? 625 GLU A OE1 1 
ATOM   4737 O OE2 . GLU A 1 625 ? -0.596  -10.682 -40.683 1.00 47.15  ? 625 GLU A OE2 1 
ATOM   4738 N N   . GLY A 1 626 ? 4.471   -10.614 -43.577 1.00 46.39  ? 626 GLY A N   1 
ATOM   4739 C CA  . GLY A 1 626 ? 5.673   -9.810  -43.756 1.00 46.53  ? 626 GLY A CA  1 
ATOM   4740 C C   . GLY A 1 626 ? 5.814   -9.256  -45.157 1.00 46.63  ? 626 GLY A C   1 
ATOM   4741 O O   . GLY A 1 626 ? 6.401   -9.908  -46.023 1.00 46.55  ? 626 GLY A O   1 
ATOM   4742 N N   . ALA A 1 627 ? 5.287   -8.045  -45.361 1.00 46.38  ? 627 ALA A N   1 
ATOM   4743 C CA  . ALA A 1 627 ? 5.330   -7.347  -46.655 1.00 46.47  ? 627 ALA A CA  1 
ATOM   4744 C C   . ALA A 1 627 ? 6.756   -7.292  -47.211 1.00 46.45  ? 627 ALA A C   1 
ATOM   4745 O O   . ALA A 1 627 ? 7.699   -6.984  -46.487 1.00 45.57  ? 627 ALA A O   1 
ATOM   4746 C CB  . ALA A 1 627 ? 4.766   -5.956  -46.513 1.00 45.80  ? 627 ALA A CB  1 
ATOM   4747 N N   . GLY A 1 628 ? 6.901   -7.598  -48.503 1.00 46.88  ? 628 GLY A N   1 
ATOM   4748 C CA  . GLY A 1 628 ? 8.216   -7.758  -49.133 1.00 47.38  ? 628 GLY A CA  1 
ATOM   4749 C C   . GLY A 1 628 ? 8.679   -9.213  -49.171 1.00 47.94  ? 628 GLY A C   1 
ATOM   4750 O O   . GLY A 1 628 ? 9.668   -9.540  -49.842 1.00 48.04  ? 628 GLY A O   1 
ATOM   4751 N N   . LEU A 1 629 ? 7.967   -10.077 -48.444 1.00 48.47  ? 629 LEU A N   1 
ATOM   4752 C CA  . LEU A 1 629 ? 8.225   -11.519 -48.404 1.00 48.81  ? 629 LEU A CA  1 
ATOM   4753 C C   . LEU A 1 629 ? 6.978   -12.301 -48.810 1.00 49.09  ? 629 LEU A C   1 
ATOM   4754 O O   . LEU A 1 629 ? 7.059   -13.224 -49.615 1.00 48.93  ? 629 LEU A O   1 
ATOM   4755 C CB  . LEU A 1 629 ? 8.685   -11.946 -46.994 1.00 49.01  ? 629 LEU A CB  1 
ATOM   4756 C CG  . LEU A 1 629 ? 10.191  -12.064 -46.705 1.00 49.14  ? 629 LEU A CG  1 
ATOM   4757 C CD1 . LEU A 1 629 ? 11.068  -11.279 -47.687 1.00 48.34  ? 629 LEU A CD1 1 
ATOM   4758 C CD2 . LEU A 1 629 ? 10.510  -11.679 -45.239 1.00 48.66  ? 629 LEU A CD2 1 
ATOM   4759 N N   . THR A 1 630 ? 5.833   -11.941 -48.238 1.00 49.47  ? 630 THR A N   1 
ATOM   4760 C CA  . THR A 1 630 ? 4.561   -12.565 -48.592 1.00 50.03  ? 630 THR A CA  1 
ATOM   4761 C C   . THR A 1 630 ? 3.504   -11.494 -48.769 1.00 50.32  ? 630 THR A C   1 
ATOM   4762 O O   . THR A 1 630 ? 3.624   -10.399 -48.218 1.00 50.27  ? 630 THR A O   1 
ATOM   4763 C CB  . THR A 1 630 ? 4.073   -13.531 -47.504 1.00 50.19  ? 630 THR A CB  1 
ATOM   4764 O OG1 . THR A 1 630 ? 5.196   -14.084 -46.795 1.00 50.94  ? 630 THR A OG1 1 
ATOM   4765 C CG2 . THR A 1 630 ? 3.215   -14.637 -48.120 1.00 49.91  ? 630 THR A CG2 1 
ATOM   4766 N N   . GLU A 1 631 ? 2.478   -11.806 -49.550 1.00 50.74  ? 631 GLU A N   1 
ATOM   4767 C CA  . GLU A 1 631 ? 1.344   -10.901 -49.707 1.00 51.25  ? 631 GLU A CA  1 
ATOM   4768 C C   . GLU A 1 631 ? 0.076   -11.443 -49.060 1.00 51.54  ? 631 GLU A C   1 
ATOM   4769 O O   . GLU A 1 631 ? -0.888  -10.703 -48.874 1.00 51.35  ? 631 GLU A O   1 
ATOM   4770 C CB  . GLU A 1 631 ? 1.105   -10.597 -51.178 1.00 51.33  ? 631 GLU A CB  1 
ATOM   4771 C CG  . GLU A 1 631 ? 2.284   -9.897  -51.838 1.00 51.68  ? 631 GLU A CG  1 
ATOM   4772 C CD  . GLU A 1 631 ? 1.878   -8.624  -52.553 1.00 51.54  ? 631 GLU A CD  1 
ATOM   4773 O OE1 . GLU A 1 631 ? 1.577   -7.629  -51.852 1.00 50.97  ? 631 GLU A OE1 1 
ATOM   4774 O OE2 . GLU A 1 631 ? 1.867   -8.623  -53.805 1.00 50.78  ? 631 GLU A OE2 1 
ATOM   4775 N N   . GLU A 1 632 ? 0.081   -12.729 -48.720 1.00 51.86  ? 632 GLU A N   1 
ATOM   4776 C CA  . GLU A 1 632 ? -1.005  -13.314 -47.961 1.00 52.14  ? 632 GLU A CA  1 
ATOM   4777 C C   . GLU A 1 632 ? -0.508  -13.683 -46.568 1.00 52.46  ? 632 GLU A C   1 
ATOM   4778 O O   . GLU A 1 632 ? 0.596   -14.215 -46.399 1.00 52.53  ? 632 GLU A O   1 
ATOM   4779 C CB  . GLU A 1 632 ? -1.575  -14.552 -48.657 1.00 52.11  ? 632 GLU A CB  1 
ATOM   4780 C CG  . GLU A 1 632 ? -2.916  -14.992 -48.072 1.00 52.20  ? 632 GLU A CG  1 
ATOM   4781 C CD  . GLU A 1 632 ? -3.428  -16.308 -48.638 1.00 52.63  ? 632 GLU A CD  1 
ATOM   4782 O OE1 . GLU A 1 632 ? -3.576  -16.420 -49.878 1.00 52.20  ? 632 GLU A OE1 1 
ATOM   4783 O OE2 . GLU A 1 632 ? -3.705  -17.224 -47.827 1.00 53.56  ? 632 GLU A OE2 1 
ATOM   4784 N N   . GLN A 1 633 ? -1.330  -13.362 -45.574 1.00 52.72  ? 633 GLN A N   1 
ATOM   4785 C CA  . GLN A 1 633 ? -1.144  -13.844 -44.221 1.00 52.56  ? 633 GLN A CA  1 
ATOM   4786 C C   . GLN A 1 633 ? -1.387  -15.345 -44.241 1.00 52.51  ? 633 GLN A C   1 
ATOM   4787 O O   . GLN A 1 633 ? -2.453  -15.796 -44.668 1.00 52.61  ? 633 GLN A O   1 
ATOM   4788 C CB  . GLN A 1 633 ? -2.138  -13.155 -43.289 1.00 52.79  ? 633 GLN A CB  1 
ATOM   4789 C CG  . GLN A 1 633 ? -2.247  -13.731 -41.879 1.00 52.74  ? 633 GLN A CG  1 
ATOM   4790 C CD  . GLN A 1 633 ? -3.314  -13.016 -41.071 1.00 53.10  ? 633 GLN A CD  1 
ATOM   4791 O OE1 . GLN A 1 633 ? -3.063  -11.955 -40.501 1.00 54.58  ? 633 GLN A OE1 1 
ATOM   4792 N NE2 . GLN A 1 633 ? -4.520  -13.584 -41.033 1.00 52.87  ? 633 GLN A NE2 1 
ATOM   4793 N N   . LYS A 1 634 ? -0.400  -16.107 -43.778 1.00 52.44  ? 634 LYS A N   1 
ATOM   4794 C CA  . LYS A 1 634 ? -0.508  -17.559 -43.714 1.00 52.50  ? 634 LYS A CA  1 
ATOM   4795 C C   . LYS A 1 634 ? -0.779  -18.032 -42.289 1.00 52.48  ? 634 LYS A C   1 
ATOM   4796 O O   . LYS A 1 634 ? 0.036   -17.830 -41.389 1.00 52.38  ? 634 LYS A O   1 
ATOM   4797 C CB  . LYS A 1 634 ? 0.765   -18.215 -44.252 1.00 52.56  ? 634 LYS A CB  1 
ATOM   4798 C CG  . LYS A 1 634 ? 1.049   -17.909 -45.714 0.00 50.00  ? 634 LYS A CG  1 
ATOM   4799 C CD  . LYS A 1 634 ? -0.007  -18.518 -46.622 0.00 50.00  ? 634 LYS A CD  1 
ATOM   4800 C CE  . LYS A 1 634 ? 0.313   -18.269 -48.087 0.00 50.00  ? 634 LYS A CE  1 
ATOM   4801 N NZ  . LYS A 1 634 ? -0.740  -18.817 -48.985 0.00 50.00  ? 634 LYS A NZ  1 
ATOM   4802 N N   . THR A 1 635 ? -1.932  -18.662 -42.096 1.00 52.47  ? 635 THR A N   1 
ATOM   4803 C CA  . THR A 1 635 ? -2.304  -19.240 -40.800 1.00 52.48  ? 635 THR A CA  1 
ATOM   4804 C C   . THR A 1 635 ? -2.287  -20.766 -40.882 1.00 52.44  ? 635 THR A C   1 
ATOM   4805 O O   . THR A 1 635 ? -3.112  -21.353 -41.580 1.00 52.00  ? 635 THR A O   1 
ATOM   4806 C CB  . THR A 1 635 ? -3.723  -18.808 -40.366 1.00 52.50  ? 635 THR A CB  1 
ATOM   4807 O OG1 . THR A 1 635 ? -3.711  -17.426 -39.989 1.00 53.09  ? 635 THR A OG1 1 
ATOM   4808 C CG2 . THR A 1 635 ? -4.209  -19.646 -39.185 1.00 52.36  ? 635 THR A CG2 1 
ATOM   4809 N N   . VAL A 1 636 ? -1.355  -21.404 -40.170 1.00 52.48  ? 636 VAL A N   1 
ATOM   4810 C CA  . VAL A 1 636 ? -1.310  -22.872 -40.117 1.00 52.40  ? 636 VAL A CA  1 
ATOM   4811 C C   . VAL A 1 636 ? -2.043  -23.393 -38.882 1.00 52.38  ? 636 VAL A C   1 
ATOM   4812 O O   . VAL A 1 636 ? -2.092  -22.742 -37.837 1.00 52.42  ? 636 VAL A O   1 
ATOM   4813 C CB  . VAL A 1 636 ? 0.134   -23.442 -40.149 1.00 52.32  ? 636 VAL A CB  1 
ATOM   4814 C CG1 . VAL A 1 636 ? 0.957   -22.765 -41.238 1.00 52.01  ? 636 VAL A CG1 1 
ATOM   4815 C CG2 . VAL A 1 636 ? 0.802   -23.294 -38.803 1.00 52.32  ? 636 VAL A CG2 1 
ATOM   4816 N N   . GLU A 1 637 ? -2.613  -24.579 -39.025 1.00 52.27  ? 637 GLU A N   1 
ATOM   4817 C CA  . GLU A 1 637 ? -3.415  -25.189 -37.987 1.00 52.30  ? 637 GLU A CA  1 
ATOM   4818 C C   . GLU A 1 637 ? -2.744  -26.498 -37.608 1.00 52.19  ? 637 GLU A C   1 
ATOM   4819 O O   . GLU A 1 637 ? -2.358  -27.273 -38.482 1.00 52.25  ? 637 GLU A O   1 
ATOM   4820 C CB  . GLU A 1 637 ? -4.818  -25.456 -38.525 1.00 52.40  ? 637 GLU A CB  1 
ATOM   4821 C CG  . GLU A 1 637 ? -5.936  -24.827 -37.719 1.00 52.52  ? 637 GLU A CG  1 
ATOM   4822 C CD  . GLU A 1 637 ? -7.086  -24.398 -38.604 1.00 52.66  ? 637 GLU A CD  1 
ATOM   4823 O OE1 . GLU A 1 637 ? -6.890  -23.437 -39.381 1.00 52.92  ? 637 GLU A OE1 1 
ATOM   4824 O OE2 . GLU A 1 637 ? -8.172  -25.022 -38.528 1.00 52.51  ? 637 GLU A OE2 1 
ATOM   4825 N N   . ILE A 1 638 ? -2.599  -26.734 -36.308 1.00 52.07  ? 638 ILE A N   1 
ATOM   4826 C CA  . ILE A 1 638 ? -1.906  -27.917 -35.807 1.00 51.82  ? 638 ILE A CA  1 
ATOM   4827 C C   . ILE A 1 638 ? -2.872  -28.698 -34.922 1.00 51.59  ? 638 ILE A C   1 
ATOM   4828 O O   . ILE A 1 638 ? -3.032  -28.369 -33.750 1.00 51.78  ? 638 ILE A O   1 
ATOM   4829 C CB  . ILE A 1 638 ? -0.638  -27.525 -35.014 1.00 51.84  ? 638 ILE A CB  1 
ATOM   4830 C CG1 . ILE A 1 638 ? 0.272   -26.621 -35.856 1.00 51.76  ? 638 ILE A CG1 1 
ATOM   4831 C CG2 . ILE A 1 638 ? 0.124   -28.770 -34.572 1.00 52.07  ? 638 ILE A CG2 1 
ATOM   4832 C CD1 . ILE A 1 638 ? 1.267   -25.845 -35.046 1.00 51.65  ? 638 ILE A CD1 1 
ATOM   4833 N N   . PRO A 1 639 ? -3.547  -29.715 -35.487 1.00 51.30  ? 639 PRO A N   1 
ATOM   4834 C CA  . PRO A 1 639 ? -4.474  -30.526 -34.690 1.00 51.12  ? 639 PRO A CA  1 
ATOM   4835 C C   . PRO A 1 639 ? -3.781  -31.481 -33.717 1.00 50.90  ? 639 PRO A C   1 
ATOM   4836 O O   . PRO A 1 639 ? -4.308  -31.731 -32.630 1.00 50.96  ? 639 PRO A O   1 
ATOM   4837 C CB  . PRO A 1 639 ? -5.261  -31.327 -35.745 1.00 51.09  ? 639 PRO A CB  1 
ATOM   4838 C CG  . PRO A 1 639 ? -4.861  -30.775 -37.077 1.00 51.20  ? 639 PRO A CG  1 
ATOM   4839 C CD  . PRO A 1 639 ? -3.513  -30.158 -36.891 1.00 51.33  ? 639 PRO A CD  1 
ATOM   4840 N N   . ASP A 1 640 ? -2.632  -32.027 -34.119 1.00 50.52  ? 640 ASP A N   1 
ATOM   4841 C CA  . ASP A 1 640 ? -1.851  -32.905 -33.248 1.00 50.23  ? 640 ASP A CA  1 
ATOM   4842 C C   . ASP A 1 640 ? -1.227  -32.062 -32.133 1.00 50.00  ? 640 ASP A C   1 
ATOM   4843 O O   . ASP A 1 640 ? -0.382  -31.210 -32.416 1.00 49.69  ? 640 ASP A O   1 
ATOM   4844 C CB  . ASP A 1 640 ? -0.745  -33.627 -34.034 1.00 50.22  ? 640 ASP A CB  1 
ATOM   4845 C CG  . ASP A 1 640 ? -1.275  -34.765 -34.906 1.00 50.06  ? 640 ASP A CG  1 
ATOM   4846 O OD1 . ASP A 1 640 ? -2.375  -35.298 -34.632 1.00 49.42  ? 640 ASP A OD1 1 
ATOM   4847 O OD2 . ASP A 1 640 ? -0.568  -35.138 -35.867 1.00 49.63  ? 640 ASP A OD2 1 
ATOM   4848 N N   . PRO A 1 641 ? -1.633  -32.301 -30.864 1.00 49.69  ? 641 PRO A N   1 
ATOM   4849 C CA  . PRO A 1 641 ? -1.124  -31.478 -29.765 1.00 49.42  ? 641 PRO A CA  1 
ATOM   4850 C C   . PRO A 1 641 ? 0.383   -31.619 -29.589 1.00 49.12  ? 641 PRO A C   1 
ATOM   4851 O O   . PRO A 1 641 ? 0.932   -32.706 -29.780 1.00 48.97  ? 641 PRO A O   1 
ATOM   4852 C CB  . PRO A 1 641 ? -1.857  -32.025 -28.531 1.00 49.45  ? 641 PRO A CB  1 
ATOM   4853 C CG  . PRO A 1 641 ? -2.991  -32.819 -29.055 1.00 49.48  ? 641 PRO A CG  1 
ATOM   4854 C CD  . PRO A 1 641 ? -2.556  -33.343 -30.377 1.00 49.59  ? 641 PRO A CD  1 
ATOM   4855 N N   . VAL A 1 642 ? 1.038   -30.519 -29.238 1.00 48.86  ? 642 VAL A N   1 
ATOM   4856 C CA  . VAL A 1 642 ? 2.478   -30.517 -29.048 1.00 48.69  ? 642 VAL A CA  1 
ATOM   4857 C C   . VAL A 1 642 ? 2.789   -30.961 -27.616 1.00 48.52  ? 642 VAL A C   1 
ATOM   4858 O O   . VAL A 1 642 ? 2.521   -30.232 -26.654 1.00 48.32  ? 642 VAL A O   1 
ATOM   4859 C CB  . VAL A 1 642 ? 3.087   -29.133 -29.343 1.00 48.61  ? 642 VAL A CB  1 
ATOM   4860 C CG1 . VAL A 1 642 ? 4.594   -29.183 -29.217 1.00 48.71  ? 642 VAL A CG1 1 
ATOM   4861 C CG2 . VAL A 1 642 ? 2.691   -28.671 -30.740 1.00 48.68  ? 642 VAL A CG2 1 
ATOM   4862 N N   . GLU A 1 643 ? 3.350   -32.162 -27.487 1.00 48.18  ? 643 GLU A N   1 
ATOM   4863 C CA  . GLU A 1 643 ? 3.671   -32.728 -26.181 1.00 48.13  ? 643 GLU A CA  1 
ATOM   4864 C C   . GLU A 1 643 ? 4.701   -31.843 -25.469 1.00 48.03  ? 643 GLU A C   1 
ATOM   4865 O O   . GLU A 1 643 ? 5.291   -30.947 -26.078 1.00 48.18  ? 643 GLU A O   1 
ATOM   4866 C CB  . GLU A 1 643 ? 4.222   -34.160 -26.308 1.00 47.91  ? 643 GLU A CB  1 
ATOM   4867 C CG  . GLU A 1 643 ? 3.397   -35.136 -27.167 1.00 47.56  ? 643 GLU A CG  1 
ATOM   4868 C CD  . GLU A 1 643 ? 2.062   -35.539 -26.545 1.00 46.50  ? 643 GLU A CD  1 
ATOM   4869 O OE1 . GLU A 1 643 ? 1.307   -36.277 -27.205 1.00 46.01  ? 643 GLU A OE1 1 
ATOM   4870 O OE2 . GLU A 1 643 ? 1.758   -35.128 -25.409 1.00 45.73  ? 643 GLU A OE2 1 
ATOM   4871 N N   . ALA A 1 644 ? 4.903   -32.099 -24.179 1.00 48.02  ? 644 ALA A N   1 
ATOM   4872 C CA  . ALA A 1 644 ? 5.928   -31.415 -23.395 1.00 48.13  ? 644 ALA A CA  1 
ATOM   4873 C C   . ALA A 1 644 ? 7.307   -31.653 -24.004 1.00 48.14  ? 644 ALA A C   1 
ATOM   4874 O O   . ALA A 1 644 ? 7.728   -32.795 -24.178 1.00 48.18  ? 644 ALA A O   1 
ATOM   4875 C CB  . ALA A 1 644 ? 5.899   -31.895 -21.945 1.00 48.02  ? 644 ALA A CB  1 
ATOM   4876 N N   . GLY A 1 645 ? 7.996   -30.571 -24.350 1.00 48.42  ? 645 GLY A N   1 
ATOM   4877 C CA  . GLY A 1 645 ? 9.319   -30.661 -24.965 1.00 48.62  ? 645 GLY A CA  1 
ATOM   4878 C C   . GLY A 1 645 ? 9.318   -30.916 -26.465 1.00 48.81  ? 645 GLY A C   1 
ATOM   4879 O O   . GLY A 1 645 ? 10.357  -30.771 -27.108 1.00 48.84  ? 645 GLY A O   1 
ATOM   4880 N N   . GLU A 1 646 ? 8.170   -31.304 -27.026 1.00 48.92  ? 646 GLU A N   1 
ATOM   4881 C CA  . GLU A 1 646 ? 8.049   -31.504 -28.469 1.00 49.25  ? 646 GLU A CA  1 
ATOM   4882 C C   . GLU A 1 646 ? 8.164   -30.159 -29.162 1.00 49.51  ? 646 GLU A C   1 
ATOM   4883 O O   . GLU A 1 646 ? 7.612   -29.168 -28.689 1.00 49.40  ? 646 GLU A O   1 
ATOM   4884 C CB  . GLU A 1 646 ? 6.702   -32.144 -28.843 1.00 49.28  ? 646 GLU A CB  1 
ATOM   4885 C CG  . GLU A 1 646 ? 6.716   -33.667 -28.946 1.00 49.77  ? 646 GLU A CG  1 
ATOM   4886 C CD  . GLU A 1 646 ? 7.273   -34.187 -30.264 1.00 50.39  ? 646 GLU A CD  1 
ATOM   4887 O OE1 . GLU A 1 646 ? 7.794   -33.382 -31.067 1.00 49.85  ? 646 GLU A OE1 1 
ATOM   4888 O OE2 . GLU A 1 646 ? 7.191   -35.421 -30.490 1.00 51.99  ? 646 GLU A OE2 1 
ATOM   4889 N N   . GLU A 1 647 ? 8.891   -30.122 -30.273 1.00 49.77  ? 647 GLU A N   1 
ATOM   4890 C CA  . GLU A 1 647 ? 8.875   -28.951 -31.126 1.00 50.08  ? 647 GLU A CA  1 
ATOM   4891 C C   . GLU A 1 647 ? 7.838   -29.149 -32.220 1.00 50.10  ? 647 GLU A C   1 
ATOM   4892 O O   . GLU A 1 647 ? 7.484   -30.278 -32.569 1.00 49.92  ? 647 GLU A O   1 
ATOM   4893 C CB  . GLU A 1 647 ? 10.256  -28.661 -31.723 1.00 50.24  ? 647 GLU A CB  1 
ATOM   4894 C CG  . GLU A 1 647 ? 10.653  -29.550 -32.904 1.00 50.48  ? 647 GLU A CG  1 
ATOM   4895 C CD  . GLU A 1 647 ? 11.794  -28.972 -33.721 1.00 50.42  ? 647 GLU A CD  1 
ATOM   4896 O OE1 . GLU A 1 647 ? 12.054  -27.759 -33.604 1.00 49.68  ? 647 GLU A OE1 1 
ATOM   4897 O OE2 . GLU A 1 647 ? 12.426  -29.736 -34.487 1.00 51.40  ? 647 GLU A OE2 1 
ATOM   4898 N N   . VAL A 1 648 ? 7.341   -28.038 -32.735 1.00 50.18  ? 648 VAL A N   1 
ATOM   4899 C CA  . VAL A 1 648 ? 6.474   -28.040 -33.896 1.00 50.46  ? 648 VAL A CA  1 
ATOM   4900 C C   . VAL A 1 648 ? 7.103   -27.115 -34.935 1.00 50.84  ? 648 VAL A C   1 
ATOM   4901 O O   . VAL A 1 648 ? 7.576   -26.024 -34.598 1.00 50.64  ? 648 VAL A O   1 
ATOM   4902 C CB  . VAL A 1 648 ? 5.053   -27.566 -33.556 1.00 50.28  ? 648 VAL A CB  1 
ATOM   4903 C CG1 . VAL A 1 648 ? 5.077   -26.177 -32.922 1.00 50.33  ? 648 VAL A CG1 1 
ATOM   4904 C CG2 . VAL A 1 648 ? 4.191   -27.562 -34.804 1.00 50.23  ? 648 VAL A CG2 1 
ATOM   4905 N N   . LYS A 1 649 ? 7.138   -27.587 -36.183 1.00 51.27  ? 649 LYS A N   1 
ATOM   4906 C CA  . LYS A 1 649 ? 7.605   -26.809 -37.333 1.00 51.48  ? 649 LYS A CA  1 
ATOM   4907 C C   . LYS A 1 649 ? 6.444   -26.587 -38.296 1.00 51.72  ? 649 LYS A C   1 
ATOM   4908 O O   . LYS A 1 649 ? 5.497   -27.376 -38.344 1.00 51.71  ? 649 LYS A O   1 
ATOM   4909 C CB  . LYS A 1 649 ? 8.708   -27.554 -38.097 1.00 51.56  ? 649 LYS A CB  1 
ATOM   4910 C CG  . LYS A 1 649 ? 10.064  -27.643 -37.424 1.00 51.59  ? 649 LYS A CG  1 
ATOM   4911 C CD  . LYS A 1 649 ? 11.057  -28.358 -38.343 1.00 51.62  ? 649 LYS A CD  1 
ATOM   4912 C CE  . LYS A 1 649 ? 12.248  -28.923 -37.589 1.00 51.95  ? 649 LYS A CE  1 
ATOM   4913 N NZ  . LYS A 1 649 ? 12.989  -27.870 -36.838 1.00 51.92  ? 649 LYS A NZ  1 
ATOM   4914 N N   . VAL A 1 650 ? 6.521   -25.501 -39.057 1.00 52.00  ? 650 VAL A N   1 
ATOM   4915 C CA  . VAL A 1 650 ? 5.682   -25.331 -40.236 1.00 52.15  ? 650 VAL A CA  1 
ATOM   4916 C C   . VAL A 1 650 ? 6.519   -24.642 -41.307 1.00 52.42  ? 650 VAL A C   1 
ATOM   4917 O O   . VAL A 1 650 ? 7.363   -23.805 -40.998 1.00 52.37  ? 650 VAL A O   1 
ATOM   4918 C CB  . VAL A 1 650 ? 4.376   -24.538 -39.949 1.00 51.98  ? 650 VAL A CB  1 
ATOM   4919 C CG1 . VAL A 1 650 ? 3.510   -25.265 -38.920 1.00 51.66  ? 650 VAL A CG1 1 
ATOM   4920 C CG2 . VAL A 1 650 ? 4.679   -23.137 -39.492 1.00 51.84  ? 650 VAL A CG2 1 
ATOM   4921 N N   . ARG A 1 651 ? 6.311   -25.040 -42.560 1.00 52.83  ? 651 ARG A N   1 
ATOM   4922 C CA  . ARG A 1 651 ? 7.010   -24.446 -43.696 1.00 53.03  ? 651 ARG A CA  1 
ATOM   4923 C C   . ARG A 1 651 ? 5.978   -23.708 -44.535 1.00 53.05  ? 651 ARG A C   1 
ATOM   4924 O O   . ARG A 1 651 ? 4.874   -24.222 -44.743 1.00 53.14  ? 651 ARG A O   1 
ATOM   4925 C CB  . ARG A 1 651 ? 7.698   -25.538 -44.516 1.00 53.28  ? 651 ARG A CB  1 
ATOM   4926 C CG  . ARG A 1 651 ? 8.706   -26.364 -43.711 1.00 53.52  ? 651 ARG A CG  1 
ATOM   4927 C CD  . ARG A 1 651 ? 8.653   -27.838 -44.064 1.00 53.98  ? 651 ARG A CD  1 
ATOM   4928 N NE  . ARG A 1 651 ? 9.034   -28.688 -42.931 1.00 54.96  ? 651 ARG A NE  1 
ATOM   4929 C CZ  . ARG A 1 651 ? 10.252  -29.188 -42.703 1.00 56.00  ? 651 ARG A CZ  1 
ATOM   4930 N NH1 . ARG A 1 651 ? 11.274  -28.936 -43.523 1.00 56.61  ? 651 ARG A NH1 1 
ATOM   4931 N NH2 . ARG A 1 651 ? 10.456  -29.955 -41.633 1.00 55.96  ? 651 ARG A NH2 1 
ATOM   4932 N N   . MET A 1 652 ? 6.332   -22.518 -45.010 1.00 52.93  ? 652 MET A N   1 
ATOM   4933 C CA  . MET A 1 652 ? 5.424   -21.715 -45.819 1.00 52.83  ? 652 MET A CA  1 
ATOM   4934 C C   . MET A 1 652 ? 6.184   -20.924 -46.879 1.00 52.74  ? 652 MET A C   1 
ATOM   4935 O O   . MET A 1 652 ? 7.316   -20.495 -46.655 1.00 52.73  ? 652 MET A O   1 
ATOM   4936 C CB  . MET A 1 652 ? 4.615   -20.765 -44.933 1.00 53.01  ? 652 MET A CB  1 
ATOM   4937 C CG  . MET A 1 652 ? 3.323   -21.362 -44.401 0.00 50.00  ? 652 MET A CG  1 
ATOM   4938 S SD  . MET A 1 652 ? 1.872   -20.808 -45.317 0.00 50.00  ? 652 MET A SD  1 
ATOM   4939 C CE  . MET A 1 652 ? 1.513   -22.265 -46.295 0.00 50.00  ? 652 MET A CE  1 
ATOM   4940 N N   . ASP A 1 653 ? 5.553   -20.734 -48.033 1.00 52.44  ? 653 ASP A N   1 
ATOM   4941 C CA  . ASP A 1 653 ? 6.228   -20.151 -49.191 1.00 52.24  ? 653 ASP A CA  1 
ATOM   4942 C C   . ASP A 1 653 ? 6.152   -18.626 -49.272 1.00 52.04  ? 653 ASP A C   1 
ATOM   4943 O O   . ASP A 1 653 ? 5.067   -18.033 -49.205 1.00 51.80  ? 653 ASP A O   1 
ATOM   4944 C CB  . ASP A 1 653 ? 5.661   -20.760 -50.465 1.00 52.21  ? 653 ASP A CB  1 
ATOM   4945 C CG  . ASP A 1 653 ? 5.768   -22.264 -50.472 1.00 52.45  ? 653 ASP A CG  1 
ATOM   4946 O OD1 . ASP A 1 653 ? 6.841   -22.774 -50.082 1.00 52.79  ? 653 ASP A OD1 1 
ATOM   4947 O OD2 . ASP A 1 653 ? 4.781   -22.932 -50.847 1.00 52.14  ? 653 ASP A OD2 1 
ATOM   4948 N N   . LEU A 1 654 ? 7.327   -18.016 -49.431 1.00 51.80  ? 654 LEU A N   1 
ATOM   4949 C CA  . LEU A 1 654 ? 7.465   -16.584 -49.660 1.00 51.65  ? 654 LEU A CA  1 
ATOM   4950 C C   . LEU A 1 654 ? 7.829   -16.325 -51.130 1.00 51.57  ? 654 LEU A C   1 
ATOM   4951 O O   . LEU A 1 654 ? 8.180   -17.253 -51.865 1.00 51.50  ? 654 LEU A O   1 
ATOM   4952 C CB  . LEU A 1 654 ? 8.558   -16.008 -48.753 1.00 51.81  ? 654 LEU A CB  1 
ATOM   4953 C CG  . LEU A 1 654 ? 8.755   -16.612 -47.355 1.00 51.28  ? 654 LEU A CG  1 
ATOM   4954 C CD1 . LEU A 1 654 ? 9.922   -15.928 -46.665 1.00 50.54  ? 654 LEU A CD1 1 
ATOM   4955 C CD2 . LEU A 1 654 ? 7.482   -16.516 -46.525 1.00 50.77  ? 654 LEU A CD2 1 
ATOM   4956 N N   . VAL A 1 655 ? 7.733   -15.065 -51.552 1.00 51.31  ? 655 VAL A N   1 
ATOM   4957 C CA  . VAL A 1 655 ? 8.219   -14.632 -52.869 1.00 51.16  ? 655 VAL A CA  1 
ATOM   4958 C C   . VAL A 1 655 ? 8.627   -13.145 -52.840 1.00 51.12  ? 655 VAL A C   1 
ATOM   4959 O O   . VAL A 1 655 ? 7.782   -12.267 -53.020 1.00 51.08  ? 655 VAL A O   1 
ATOM   4960 C CB  . VAL A 1 655 ? 7.180   -14.895 -54.001 1.00 51.14  ? 655 VAL A CB  1 
ATOM   4961 C CG1 . VAL A 1 655 ? 7.640   -16.038 -54.906 1.00 50.67  ? 655 VAL A CG1 1 
ATOM   4962 C CG2 . VAL A 1 655 ? 5.794   -15.165 -53.424 1.00 50.83  ? 655 VAL A CG2 1 
ATOM   4963 N N   . PRO A 1 656 ? 9.924   -12.859 -52.594 1.00 51.05  ? 656 PRO A N   1 
ATOM   4964 C CA  . PRO A 1 656 ? 10.417  -11.479 -52.523 1.00 51.17  ? 656 PRO A CA  1 
ATOM   4965 C C   . PRO A 1 656 ? 10.407  -10.750 -53.866 1.00 51.40  ? 656 PRO A C   1 
ATOM   4966 O O   . PRO A 1 656 ? 9.903   -11.282 -54.858 1.00 51.51  ? 656 PRO A O   1 
ATOM   4967 C CB  . PRO A 1 656 ? 11.853  -11.642 -51.999 1.00 50.97  ? 656 PRO A CB  1 
ATOM   4968 C CG  . PRO A 1 656 ? 12.245  -12.997 -52.374 1.00 50.94  ? 656 PRO A CG  1 
ATOM   4969 C CD  . PRO A 1 656 ? 11.001  -13.831 -52.344 1.00 51.10  ? 656 PRO A CD  1 
ATOM   4970 N N   . LEU A 1 657 ? 10.952  -9.535  -53.893 1.00 51.56  ? 657 LEU A N   1 
ATOM   4971 C CA  . LEU A 1 657 ? 10.925  -8.722  -55.110 1.00 51.58  ? 657 LEU A CA  1 
ATOM   4972 C C   . LEU A 1 657 ? 11.985  -7.608  -55.167 1.00 51.66  ? 657 LEU A C   1 
ATOM   4973 O O   . LEU A 1 657 ? 12.498  -7.317  -56.255 1.00 51.63  ? 657 LEU A O   1 
ATOM   4974 C CB  . LEU A 1 657 ? 9.522   -8.127  -55.283 1.00 51.65  ? 657 LEU A CB  1 
ATOM   4975 C CG  . LEU A 1 657 ? 8.878   -8.275  -56.659 1.00 51.91  ? 657 LEU A CG  1 
ATOM   4976 C CD1 . LEU A 1 657 ? 7.362   -8.163  -56.533 1.00 52.40  ? 657 LEU A CD1 1 
ATOM   4977 C CD2 . LEU A 1 657 ? 9.432   -7.250  -57.656 1.00 52.27  ? 657 LEU A CD2 1 
ATOM   4978 N N   . HIS A 1 658 ? 12.310  -6.985  -54.026 1.00 51.64  ? 658 HIS A N   1 
ATOM   4979 C CA  . HIS A 1 658 ? 13.195  -5.805  -54.023 1.00 51.63  ? 658 HIS A CA  1 
ATOM   4980 C C   . HIS A 1 658 ? 14.383  -5.818  -53.037 1.00 51.60  ? 658 HIS A C   1 
ATOM   4981 O O   . HIS A 1 658 ? 14.384  -6.524  -52.032 1.00 51.62  ? 658 HIS A O   1 
ATOM   4982 C CB  . HIS A 1 658 ? 12.355  -4.524  -53.886 1.00 51.70  ? 658 HIS A CB  1 
ATOM   4983 C CG  . HIS A 1 658 ? 11.754  -4.068  -55.182 1.00 51.60  ? 658 HIS A CG  1 
ATOM   4984 N ND1 . HIS A 1 658 ? 10.413  -4.201  -55.475 1.00 51.66  ? 658 HIS A ND1 1 
ATOM   4985 C CD2 . HIS A 1 658 ? 12.324  -3.516  -56.280 1.00 51.95  ? 658 HIS A CD2 1 
ATOM   4986 C CE1 . HIS A 1 658 ? 10.182  -3.736  -56.690 1.00 51.75  ? 658 HIS A CE1 1 
ATOM   4987 N NE2 . HIS A 1 658 ? 11.324  -3.311  -57.199 1.00 51.70  ? 658 HIS A NE2 1 
ATOM   4988 N N   . MET A 1 659 ? 15.375  -4.987  -53.362 1.00 51.66  ? 659 MET A N   1 
ATOM   4989 C CA  . MET A 1 659 ? 16.759  -5.061  -52.845 1.00 51.66  ? 659 MET A CA  1 
ATOM   4990 C C   . MET A 1 659 ? 16.996  -5.619  -51.442 1.00 50.98  ? 659 MET A C   1 
ATOM   4991 O O   . MET A 1 659 ? 17.750  -6.579  -51.273 1.00 51.14  ? 659 MET A O   1 
ATOM   4992 C CB  . MET A 1 659 ? 17.438  -3.674  -52.921 1.00 51.72  ? 659 MET A CB  1 
ATOM   4993 C CG  . MET A 1 659 ? 16.815  -2.563  -52.036 1.00 52.28  ? 659 MET A CG  1 
ATOM   4994 S SD  . MET A 1 659 ? 18.023  -1.431  -51.286 1.00 52.91  ? 659 MET A SD  1 
ATOM   4995 C CE  . MET A 1 659 ? 18.788  -2.459  -50.030 1.00 52.58  ? 659 MET A CE  1 
ATOM   4996 N N   . GLY A 1 660 ? 16.344  -5.020  -50.451 1.00 50.20  ? 660 GLY A N   1 
ATOM   4997 C CA  . GLY A 1 660 ? 16.897  -4.951  -49.103 1.00 49.31  ? 660 GLY A CA  1 
ATOM   4998 C C   . GLY A 1 660 ? 16.178  -5.753  -48.052 1.00 48.96  ? 660 GLY A C   1 
ATOM   4999 O O   . GLY A 1 660 ? 15.621  -6.814  -48.342 1.00 48.89  ? 660 GLY A O   1 
ATOM   5000 N N   . LEU A 1 661 ? 16.189  -5.220  -46.829 1.00 48.35  ? 661 LEU A N   1 
ATOM   5001 C CA  . LEU A 1 661 ? 15.719  -5.934  -45.644 1.00 47.83  ? 661 LEU A CA  1 
ATOM   5002 C C   . LEU A 1 661 ? 14.198  -6.052  -45.575 1.00 47.28  ? 661 LEU A C   1 
ATOM   5003 O O   . LEU A 1 661 ? 13.478  -5.077  -45.778 1.00 47.44  ? 661 LEU A O   1 
ATOM   5004 C CB  . LEU A 1 661 ? 16.232  -5.253  -44.371 1.00 47.93  ? 661 LEU A CB  1 
ATOM   5005 C CG  . LEU A 1 661 ? 17.632  -5.070  -44.157 0.00 50.00  ? 661 LEU A CG  1 
ATOM   5006 C CD1 . LEU A 1 661 ? 17.920  -4.281  -42.882 0.00 50.00  ? 661 LEU A CD1 1 
ATOM   5007 C CD2 . LEU A 1 661 ? 18.331  -6.426  -44.108 0.00 50.00  ? 661 LEU A CD2 1 
ATOM   5008 N N   . HIS A 1 662 ? 13.735  -7.265  -45.298 1.00 46.39  ? 662 HIS A N   1 
ATOM   5009 C CA  . HIS A 1 662 ? 12.337  -7.539  -45.024 1.00 46.06  ? 662 HIS A CA  1 
ATOM   5010 C C   . HIS A 1 662 ? 12.254  -8.360  -43.746 1.00 45.43  ? 662 HIS A C   1 
ATOM   5011 O O   . HIS A 1 662 ? 13.147  -9.149  -43.447 1.00 45.43  ? 662 HIS A O   1 
ATOM   5012 C CB  . HIS A 1 662 ? 11.703  -8.307  -46.175 1.00 46.29  ? 662 HIS A CB  1 
ATOM   5013 C CG  . HIS A 1 662 ? 11.883  -7.644  -47.502 1.00 46.83  ? 662 HIS A CG  1 
ATOM   5014 N ND1 . HIS A 1 662 ? 12.700  -8.159  -48.485 1.00 47.42  ? 662 HIS A ND1 1 
ATOM   5015 C CD2 . HIS A 1 662 ? 11.384  -6.486  -47.993 1.00 47.32  ? 662 HIS A CD2 1 
ATOM   5016 C CE1 . HIS A 1 662 ? 12.686  -7.355  -49.532 1.00 47.16  ? 662 HIS A CE1 1 
ATOM   5017 N NE2 . HIS A 1 662 ? 11.892  -6.333  -49.262 1.00 47.11  ? 662 HIS A NE2 1 
ATOM   5018 N N   . LYS A 1 663 ? 11.178  -8.167  -43.001 1.00 44.43  ? 663 LYS A N   1 
ATOM   5019 C CA  . LYS A 1 663 ? 11.049  -8.766  -41.697 1.00 44.37  ? 663 LYS A CA  1 
ATOM   5020 C C   . LYS A 1 663 ? 9.834   -9.663  -41.766 1.00 43.99  ? 663 LYS A C   1 
ATOM   5021 O O   . LYS A 1 663 ? 8.727   -9.183  -41.990 1.00 44.09  ? 663 LYS A O   1 
ATOM   5022 C CB  . LYS A 1 663 ? 10.874  -7.660  -40.658 1.00 44.15  ? 663 LYS A CB  1 
ATOM   5023 C CG  . LYS A 1 663 ? 11.429  -7.929  -39.293 1.00 44.23  ? 663 LYS A CG  1 
ATOM   5024 C CD  . LYS A 1 663 ? 11.255  -6.688  -38.394 1.00 43.05  ? 663 LYS A CD  1 
ATOM   5025 C CE  . LYS A 1 663 ? 12.547  -6.292  -37.675 1.00 40.24  ? 663 LYS A CE  1 
ATOM   5026 N NZ  . LYS A 1 663 ? 13.422  -5.393  -38.457 1.00 36.53  ? 663 LYS A NZ  1 
ATOM   5027 N N   . LEU A 1 664 ? 10.051  -10.964 -41.647 1.00 44.03  ? 664 LEU A N   1 
ATOM   5028 C CA  . LEU A 1 664 ? 8.952   -11.908 -41.537 1.00 44.52  ? 664 LEU A CA  1 
ATOM   5029 C C   . LEU A 1 664 ? 8.564   -11.905 -40.081 1.00 44.56  ? 664 LEU A C   1 
ATOM   5030 O O   . LEU A 1 664 ? 9.430   -11.903 -39.228 1.00 44.34  ? 664 LEU A O   1 
ATOM   5031 C CB  . LEU A 1 664 ? 9.389   -13.308 -41.969 1.00 44.34  ? 664 LEU A CB  1 
ATOM   5032 C CG  . LEU A 1 664 ? 8.306   -14.385 -42.051 1.00 44.67  ? 664 LEU A CG  1 
ATOM   5033 C CD1 . LEU A 1 664 ? 7.316   -14.140 -43.228 1.00 43.31  ? 664 LEU A CD1 1 
ATOM   5034 C CD2 . LEU A 1 664 ? 8.976   -15.760 -42.174 1.00 44.27  ? 664 LEU A CD2 1 
ATOM   5035 N N   . VAL A 1 665 ? 7.263   -11.896 -39.818 1.00 45.47  ? 665 VAL A N   1 
ATOM   5036 C CA  . VAL A 1 665 ? 6.702   -11.733 -38.483 1.00 46.04  ? 665 VAL A CA  1 
ATOM   5037 C C   . VAL A 1 665 ? 5.720   -12.872 -38.174 1.00 46.20  ? 665 VAL A C   1 
ATOM   5038 O O   . VAL A 1 665 ? 4.854   -13.194 -38.986 1.00 45.69  ? 665 VAL A O   1 
ATOM   5039 C CB  . VAL A 1 665 ? 5.946   -10.397 -38.376 1.00 46.51  ? 665 VAL A CB  1 
ATOM   5040 C CG1 . VAL A 1 665 ? 5.363   -10.225 -36.973 1.00 46.66  ? 665 VAL A CG1 1 
ATOM   5041 C CG2 . VAL A 1 665 ? 6.856   -9.212  -38.739 1.00 46.73  ? 665 VAL A CG2 1 
ATOM   5042 N N   . VAL A 1 666 ? 5.856   -13.455 -36.983 1.00 46.50  ? 666 VAL A N   1 
ATOM   5043 C CA  . VAL A 1 666 ? 5.115   -14.643 -36.603 1.00 46.53  ? 666 VAL A CA  1 
ATOM   5044 C C   . VAL A 1 666 ? 4.421   -14.471 -35.247 1.00 47.00  ? 666 VAL A C   1 
ATOM   5045 O O   . VAL A 1 666 ? 5.020   -13.936 -34.301 1.00 46.80  ? 666 VAL A O   1 
ATOM   5046 C CB  . VAL A 1 666 ? 6.075   -15.838 -36.512 1.00 46.70  ? 666 VAL A CB  1 
ATOM   5047 C CG1 . VAL A 1 666 ? 5.315   -17.122 -36.181 1.00 46.98  ? 666 VAL A CG1 1 
ATOM   5048 C CG2 . VAL A 1 666 ? 6.875   -15.978 -37.803 1.00 46.30  ? 666 VAL A CG2 1 
ATOM   5049 N N   . ASN A 1 667 ? 3.158   -14.901 -35.178 1.00 47.15  ? 667 ASN A N   1 
ATOM   5050 C CA  . ASN A 1 667 ? 2.433   -15.081 -33.927 1.00 47.31  ? 667 ASN A CA  1 
ATOM   5051 C C   . ASN A 1 667 ? 2.153   -16.570 -33.746 1.00 47.58  ? 667 ASN A C   1 
ATOM   5052 O O   . ASN A 1 667 ? 1.846   -17.271 -34.708 1.00 47.47  ? 667 ASN A O   1 
ATOM   5053 C CB  . ASN A 1 667 ? 1.112   -14.312 -33.931 1.00 47.72  ? 667 ASN A CB  1 
ATOM   5054 C CG  . ASN A 1 667 ? 0.505   -14.154 -32.536 1.00 48.22  ? 667 ASN A CG  1 
ATOM   5055 O OD1 . ASN A 1 667 ? -0.719  -14.184 -32.365 1.00 51.50  ? 667 ASN A OD1 1 
ATOM   5056 N ND2 . ASN A 1 667 ? 1.352   -13.962 -31.544 1.00 48.70  ? 667 ASN A ND2 1 
ATOM   5057 N N   . PHE A 1 668 ? 2.285   -17.043 -32.512 1.00 47.92  ? 668 PHE A N   1 
ATOM   5058 C CA  . PHE A 1 668 ? 1.937   -18.421 -32.128 1.00 47.79  ? 668 PHE A CA  1 
ATOM   5059 C C   . PHE A 1 668 ? 0.961   -18.323 -30.969 1.00 47.80  ? 668 PHE A C   1 
ATOM   5060 O O   . PHE A 1 668 ? 1.234   -17.637 -29.979 1.00 47.58  ? 668 PHE A O   1 
ATOM   5061 C CB  . PHE A 1 668 ? 3.181   -19.204 -31.713 1.00 47.74  ? 668 PHE A CB  1 
ATOM   5062 C CG  . PHE A 1 668 ? 2.890   -20.595 -31.196 1.00 48.21  ? 668 PHE A CG  1 
ATOM   5063 C CD1 . PHE A 1 668 ? 2.834   -21.678 -32.065 1.00 48.53  ? 668 PHE A CD1 1 
ATOM   5064 C CD2 . PHE A 1 668 ? 2.684   -20.823 -29.842 1.00 48.10  ? 668 PHE A CD2 1 
ATOM   5065 C CE1 . PHE A 1 668 ? 2.571   -22.963 -31.594 1.00 48.41  ? 668 PHE A CE1 1 
ATOM   5066 C CE2 . PHE A 1 668 ? 2.411   -22.103 -29.367 1.00 48.33  ? 668 PHE A CE2 1 
ATOM   5067 C CZ  . PHE A 1 668 ? 2.359   -23.173 -30.245 1.00 47.81  ? 668 PHE A CZ  1 
ATOM   5068 N N   . GLU A 1 669 ? -0.184  -18.978 -31.099 1.00 47.70  ? 669 GLU A N   1 
ATOM   5069 C CA  . GLU A 1 669 ? -1.190  -18.924 -30.060 1.00 47.94  ? 669 GLU A CA  1 
ATOM   5070 C C   . GLU A 1 669 ? -1.583  -20.346 -29.635 1.00 47.80  ? 669 GLU A C   1 
ATOM   5071 O O   . GLU A 1 669 ? -1.461  -21.294 -30.416 1.00 47.89  ? 669 GLU A O   1 
ATOM   5072 C CB  . GLU A 1 669 ? -2.388  -18.106 -30.553 1.00 48.00  ? 669 GLU A CB  1 
ATOM   5073 C CG  . GLU A 1 669 ? -3.099  -17.292 -29.458 1.00 48.81  ? 669 GLU A CG  1 
ATOM   5074 C CD  . GLU A 1 669 ? -3.346  -15.840 -29.863 1.00 48.98  ? 669 GLU A CD  1 
ATOM   5075 O OE1 . GLU A 1 669 ? -4.523  -15.425 -29.964 1.00 50.59  ? 669 GLU A OE1 1 
ATOM   5076 O OE2 . GLU A 1 669 ? -2.357  -15.111 -30.080 1.00 51.01  ? 669 GLU A OE2 1 
ATOM   5077 N N   . SER A 1 670 ? -2.021  -20.484 -28.387 1.00 47.55  ? 670 SER A N   1 
ATOM   5078 C CA  . SER A 1 670 ? -2.388  -21.788 -27.820 1.00 47.42  ? 670 SER A CA  1 
ATOM   5079 C C   . SER A 1 670 ? -3.427  -21.645 -26.719 1.00 47.18  ? 670 SER A C   1 
ATOM   5080 O O   . SER A 1 670 ? -3.861  -20.543 -26.396 1.00 46.90  ? 670 SER A O   1 
ATOM   5081 C CB  . SER A 1 670 ? -1.147  -22.492 -27.265 1.00 47.26  ? 670 SER A CB  1 
ATOM   5082 O OG  . SER A 1 670 ? -0.267  -22.869 -28.308 1.00 47.24  ? 670 SER A OG  1 
ATOM   5083 N N   . ASP A 1 671 ? -3.843  -22.772 -26.153 1.00 47.30  ? 671 ASP A N   1 
ATOM   5084 C CA  . ASP A 1 671 ? -4.708  -22.738 -24.982 1.00 47.33  ? 671 ASP A CA  1 
ATOM   5085 C C   . ASP A 1 671 ? -3.905  -22.299 -23.756 1.00 47.32  ? 671 ASP A C   1 
ATOM   5086 O O   . ASP A 1 671 ? -4.397  -21.515 -22.945 1.00 47.42  ? 671 ASP A O   1 
ATOM   5087 C CB  . ASP A 1 671 ? -5.413  -24.088 -24.752 1.00 47.36  ? 671 ASP A CB  1 
ATOM   5088 C CG  . ASP A 1 671 ? -4.459  -25.205 -24.356 1.00 47.39  ? 671 ASP A CG  1 
ATOM   5089 O OD1 . ASP A 1 671 ? -4.854  -26.038 -23.508 1.00 48.18  ? 671 ASP A OD1 1 
ATOM   5090 O OD2 . ASP A 1 671 ? -3.327  -25.259 -24.888 1.00 47.27  ? 671 ASP A OD2 1 
ATOM   5091 N N   . LYS A 1 672 ? -2.663  -22.768 -23.647 1.00 47.24  ? 672 LYS A N   1 
ATOM   5092 C CA  . LYS A 1 672 ? -1.835  -22.494 -22.473 1.00 47.31  ? 672 LYS A CA  1 
ATOM   5093 C C   . LYS A 1 672 ? -0.643  -21.574 -22.756 1.00 47.40  ? 672 LYS A C   1 
ATOM   5094 O O   . LYS A 1 672 ? 0.150   -21.305 -21.857 1.00 47.54  ? 672 LYS A O   1 
ATOM   5095 C CB  . LYS A 1 672 ? -1.332  -23.816 -21.874 1.00 47.33  ? 672 LYS A CB  1 
ATOM   5096 C CG  . LYS A 1 672 ? -2.422  -24.688 -21.260 1.00 46.89  ? 672 LYS A CG  1 
ATOM   5097 C CD  . LYS A 1 672 ? -2.132  -25.983 -20.977 0.00 50.00  ? 672 LYS A CD  1 
ATOM   5098 C CE  . LYS A 1 672 ? -3.311  -26.870 -20.604 0.00 50.00  ? 672 LYS A CE  1 
ATOM   5099 N NZ  . LYS A 1 672 ? -4.125  -26.295 -19.497 0.00 50.00  ? 672 LYS A NZ  1 
ATOM   5100 N N   . LEU A 1 673 ? -0.516  -21.079 -23.984 1.00 47.53  ? 673 LEU A N   1 
ATOM   5101 C CA  . LEU A 1 673 ? 0.678   -20.320 -24.370 1.00 47.56  ? 673 LEU A CA  1 
ATOM   5102 C C   . LEU A 1 673 ? 0.382   -19.363 -25.542 1.00 47.63  ? 673 LEU A C   1 
ATOM   5103 O O   . LEU A 1 673 ? 0.750   -19.613 -26.695 1.00 47.61  ? 673 LEU A O   1 
ATOM   5104 C CB  . LEU A 1 673 ? 1.828   -21.296 -24.682 1.00 47.51  ? 673 LEU A CB  1 
ATOM   5105 C CG  . LEU A 1 673 ? 3.269   -20.828 -24.468 1.00 47.51  ? 673 LEU A CG  1 
ATOM   5106 C CD1 . LEU A 1 673 ? 3.496   -20.359 -23.036 1.00 46.67  ? 673 LEU A CD1 1 
ATOM   5107 C CD2 . LEU A 1 673 ? 4.230   -21.952 -24.809 1.00 47.29  ? 673 LEU A CD2 1 
ATOM   5108 N N   . LYS A 1 674 ? -0.269  -18.249 -25.206 1.00 47.82  ? 674 LYS A N   1 
ATOM   5109 C CA  . LYS A 1 674 ? -0.822  -17.310 -26.186 1.00 47.70  ? 674 LYS A CA  1 
ATOM   5110 C C   . LYS A 1 674 ? 0.117   -16.159 -26.561 1.00 47.92  ? 674 LYS A C   1 
ATOM   5111 O O   . LYS A 1 674 ? 1.031   -15.810 -25.813 1.00 47.89  ? 674 LYS A O   1 
ATOM   5112 C CB  . LYS A 1 674 ? -2.129  -16.708 -25.657 1.00 47.77  ? 674 LYS A CB  1 
ATOM   5113 C CG  . LYS A 1 674 ? -3.267  -17.691 -25.531 1.00 47.66  ? 674 LYS A CG  1 
ATOM   5114 C CD  . LYS A 1 674 ? -4.658  -16.911 -25.647 0.00 50.00  ? 674 LYS A CD  1 
ATOM   5115 C CE  . LYS A 1 674 ? -4.896  -16.438 -24.217 0.00 50.00  ? 674 LYS A CE  1 
ATOM   5116 N NZ  . LYS A 1 674 ? -6.330  -16.105 -23.973 0.00 50.00  ? 674 LYS A NZ  1 
ATOM   5117 N N   . ALA A 1 675 ? -0.144  -15.584 -27.736 1.00 47.77  ? 675 ALA A N   1 
ATOM   5118 C CA  . ALA A 1 675 ? 0.542   -14.406 -28.242 1.00 47.67  ? 675 ALA A CA  1 
ATOM   5119 C C   . ALA A 1 675 ? 2.037   -14.413 -27.975 1.00 47.67  ? 675 ALA A C   1 
ATOM   5120 O O   . ALA A 1 675 ? 2.562   -13.477 -27.377 1.00 48.02  ? 675 ALA A O   1 
ATOM   5121 C CB  . ALA A 1 675 ? -0.104  -13.126 -27.690 1.00 47.40  ? 675 ALA A CB  1 
ATOM   5122 N N   . VAL A 1 676 ? 2.715   -15.470 -28.415 1.00 47.62  ? 676 VAL A N   1 
ATOM   5123 C CA  . VAL A 1 676 ? 4.176   -15.459 -28.461 1.00 47.70  ? 676 VAL A CA  1 
ATOM   5124 C C   . VAL A 1 676 ? 4.599   -15.016 -29.860 1.00 47.83  ? 676 VAL A C   1 
ATOM   5125 O O   . VAL A 1 676 ? 4.135   -15.568 -30.855 1.00 47.98  ? 676 VAL A O   1 
ATOM   5126 C CB  . VAL A 1 676 ? 4.841   -16.803 -28.023 1.00 47.89  ? 676 VAL A CB  1 
ATOM   5127 C CG1 . VAL A 1 676 ? 3.880   -17.981 -28.093 1.00 48.69  ? 676 VAL A CG1 1 
ATOM   5128 C CG2 . VAL A 1 676 ? 6.124   -17.077 -28.794 1.00 47.79  ? 676 VAL A CG2 1 
ATOM   5129 N N   . LYS A 1 677 ? 5.473   -14.009 -29.910 1.00 47.65  ? 677 LYS A N   1 
ATOM   5130 C CA  . LYS A 1 677 ? 5.913   -13.377 -31.155 1.00 47.15  ? 677 LYS A CA  1 
ATOM   5131 C C   . LYS A 1 677 ? 7.366   -13.717 -31.545 1.00 46.92  ? 677 LYS A C   1 
ATOM   5132 O O   . LYS A 1 677 ? 8.194   -14.139 -30.716 1.00 46.39  ? 677 LYS A O   1 
ATOM   5133 C CB  . LYS A 1 677 ? 5.772   -11.860 -31.059 1.00 47.39  ? 677 LYS A CB  1 
ATOM   5134 C CG  . LYS A 1 677 ? 4.516   -11.354 -30.367 1.00 47.32  ? 677 LYS A CG  1 
ATOM   5135 C CD  . LYS A 1 677 ? 3.293   -11.368 -31.252 1.00 46.23  ? 677 LYS A CD  1 
ATOM   5136 C CE  . LYS A 1 677 ? 2.183   -10.521 -30.638 1.00 46.80  ? 677 LYS A CE  1 
ATOM   5137 N NZ  . LYS A 1 677 ? 0.821   -10.775 -31.208 1.00 47.75  ? 677 LYS A NZ  1 
ATOM   5138 N N   . GLY A 1 678 ? 7.648   -13.532 -32.833 1.00 46.46  ? 678 GLY A N   1 
ATOM   5139 C CA  . GLY A 1 678 ? 8.981   -13.757 -33.411 1.00 45.91  ? 678 GLY A CA  1 
ATOM   5140 C C   . GLY A 1 678 ? 9.114   -12.934 -34.688 1.00 45.25  ? 678 GLY A C   1 
ATOM   5141 O O   . GLY A 1 678 ? 8.119   -12.487 -35.247 1.00 44.65  ? 678 GLY A O   1 
ATOM   5142 N N   . PHE A 1 679 ? 10.344  -12.696 -35.121 1.00 45.05  ? 679 PHE A N   1 
ATOM   5143 C CA  . PHE A 1 679 ? 10.587  -12.038 -36.400 1.00 45.48  ? 679 PHE A CA  1 
ATOM   5144 C C   . PHE A 1 679 ? 11.925  -12.520 -36.941 1.00 45.61  ? 679 PHE A C   1 
ATOM   5145 O O   . PHE A 1 679 ? 12.728  -13.059 -36.185 1.00 45.13  ? 679 PHE A O   1 
ATOM   5146 C CB  . PHE A 1 679 ? 10.578  -10.513 -36.263 1.00 44.68  ? 679 PHE A CB  1 
ATOM   5147 C CG  . PHE A 1 679 ? 11.719  -9.967  -35.445 1.00 45.13  ? 679 PHE A CG  1 
ATOM   5148 C CD1 . PHE A 1 679 ? 12.878  -9.501  -36.056 1.00 44.96  ? 679 PHE A CD1 1 
ATOM   5149 C CD2 . PHE A 1 679 ? 11.633  -9.909  -34.064 1.00 45.13  ? 679 PHE A CD2 1 
ATOM   5150 C CE1 . PHE A 1 679 ? 13.927  -8.996  -35.306 1.00 44.14  ? 679 PHE A CE1 1 
ATOM   5151 C CE2 . PHE A 1 679 ? 12.686  -9.401  -33.303 1.00 43.66  ? 679 PHE A CE2 1 
ATOM   5152 C CZ  . PHE A 1 679 ? 13.832  -8.943  -33.931 1.00 43.96  ? 679 PHE A CZ  1 
ATOM   5153 N N   . ARG A 1 680 ? 12.138  -12.358 -38.251 1.00 45.85  ? 680 ARG A N   1 
ATOM   5154 C CA  . ARG A 1 680 ? 13.448  -12.590 -38.864 1.00 45.51  ? 680 ARG A CA  1 
ATOM   5155 C C   . ARG A 1 680 ? 13.691  -11.578 -39.978 1.00 45.00  ? 680 ARG A C   1 
ATOM   5156 O O   . ARG A 1 680 ? 12.815  -11.342 -40.793 1.00 44.34  ? 680 ARG A O   1 
ATOM   5157 C CB  . ARG A 1 680 ? 13.536  -14.024 -39.415 1.00 46.14  ? 680 ARG A CB  1 
ATOM   5158 C CG  . ARG A 1 680 ? 14.886  -14.414 -40.035 1.00 47.26  ? 680 ARG A CG  1 
ATOM   5159 C CD  . ARG A 1 680 ? 15.988  -14.531 -38.993 1.00 51.55  ? 680 ARG A CD  1 
ATOM   5160 N NE  . ARG A 1 680 ? 16.093  -15.888 -38.458 1.00 54.22  ? 680 ARG A NE  1 
ATOM   5161 C CZ  . ARG A 1 680 ? 16.465  -16.196 -37.210 1.00 54.96  ? 680 ARG A CZ  1 
ATOM   5162 N NH1 . ARG A 1 680 ? 16.786  -15.249 -36.325 1.00 54.99  ? 680 ARG A NH1 1 
ATOM   5163 N NH2 . ARG A 1 680 ? 16.515  -17.475 -36.843 1.00 55.26  ? 680 ARG A NH2 1 
ATOM   5164 N N   . ASN A 1 681 ? 14.873  -10.975 -39.981 1.00 44.63  ? 681 ASN A N   1 
ATOM   5165 C CA  . ASN A 1 681 ? 15.325  -10.144 -41.085 1.00 44.87  ? 681 ASN A CA  1 
ATOM   5166 C C   . ASN A 1 681 ? 15.844  -11.027 -42.226 1.00 44.99  ? 681 ASN A C   1 
ATOM   5167 O O   . ASN A 1 681 ? 16.554  -12.004 -41.980 1.00 45.16  ? 681 ASN A O   1 
ATOM   5168 C CB  . ASN A 1 681 ? 16.431  -9.185  -40.625 1.00 44.69  ? 681 ASN A CB  1 
ATOM   5169 C CG  . ASN A 1 681 ? 15.963  -8.222  -39.550 1.00 44.04  ? 681 ASN A CG  1 
ATOM   5170 O OD1 . ASN A 1 681 ? 14.815  -7.809  -39.539 1.00 42.82  ? 681 ASN A OD1 1 
ATOM   5171 N ND2 . ASN A 1 681 ? 16.856  -7.864  -38.639 1.00 43.47  ? 681 ASN A ND2 1 
ATOM   5172 N N   . VAL A 1 682 ? 15.495  -10.682 -43.464 1.00 45.00  ? 682 VAL A N   1 
ATOM   5173 C CA  . VAL A 1 682 ? 15.903  -11.461 -44.636 1.00 44.99  ? 682 VAL A CA  1 
ATOM   5174 C C   . VAL A 1 682 ? 16.465  -10.538 -45.718 1.00 45.14  ? 682 VAL A C   1 
ATOM   5175 O O   . VAL A 1 682 ? 16.004  -9.404  -45.869 1.00 45.12  ? 682 VAL A O   1 
ATOM   5176 C CB  . VAL A 1 682 ? 14.720  -12.268 -45.208 1.00 44.98  ? 682 VAL A CB  1 
ATOM   5177 C CG1 . VAL A 1 682 ? 15.204  -13.250 -46.263 1.00 45.11  ? 682 VAL A CG1 1 
ATOM   5178 C CG2 . VAL A 1 682 ? 13.997  -13.021 -44.107 1.00 45.17  ? 682 VAL A CG2 1 
ATOM   5179 N N   . ILE A 1 683 ? 17.455  -11.042 -46.463 1.00 45.30  ? 683 ILE A N   1 
ATOM   5180 C CA  . ILE A 1 683 ? 18.154  -10.309 -47.546 1.00 45.36  ? 683 ILE A CA  1 
ATOM   5181 C C   . ILE A 1 683 ? 18.980  -9.128  -47.022 1.00 45.44  ? 683 ILE A C   1 
ATOM   5182 O O   . ILE A 1 683 ? 20.040  -8.824  -47.561 1.00 45.29  ? 683 ILE A O   1 
ATOM   5183 C CB  . ILE A 1 683 ? 17.194  -9.820  -48.685 1.00 45.48  ? 683 ILE A CB  1 
ATOM   5184 C CG1 . ILE A 1 683 ? 16.405  -10.990 -49.279 1.00 45.49  ? 683 ILE A CG1 1 
ATOM   5185 C CG2 . ILE A 1 683 ? 17.974  -9.129  -49.797 1.00 45.06  ? 683 ILE A CG2 1 
ATOM   5186 C CD1 . ILE A 1 683 ? 15.515  -10.598 -50.455 1.00 45.35  ? 683 ILE A CD1 1 
HETATM 5187 C C   . ACE B 2 1   ? -6.954  -0.993  23.373  1.00 62.10  ? 1   ACE X C   1 
HETATM 5188 O O   . ACE B 2 1   ? -6.159  -0.727  24.276  1.00 62.99  ? 1   ACE X O   1 
HETATM 5189 C CH3 . ACE B 2 1   ? -8.054  0.017   23.011  1.00 62.49  ? 1   ACE X CH3 1 
ATOM   5190 N N   . PRO B 2 2   ? -6.836  -2.153  22.709  1.00 62.11  ? 2   PRO X N   1 
ATOM   5191 C CA  . PRO B 2 2   ? -5.802  -3.170  22.967  1.00 62.07  ? 2   PRO X CA  1 
ATOM   5192 C C   . PRO B 2 2   ? -4.521  -2.832  22.212  1.00 61.76  ? 2   PRO X C   1 
ATOM   5193 O O   . PRO B 2 2   ? -4.411  -1.795  21.573  1.00 62.03  ? 2   PRO X O   1 
ATOM   5194 C CB  . PRO B 2 2   ? -6.370  -4.489  22.407  1.00 62.10  ? 2   PRO X CB  1 
ATOM   5195 C CG  . PRO B 2 2   ? -7.578  -4.116  21.537  1.00 62.09  ? 2   PRO X CG  1 
ATOM   5196 C CD  . PRO B 2 2   ? -7.699  -2.583  21.596  1.00 62.27  ? 2   PRO X CD  1 
HETATM 5197 N N   . ONL B 2 3   ? -3.566  -3.743  22.314  1.00 61.71  ? 3   ONL X N   1 
HETATM 5198 C CA  . ONL B 2 3   ? -2.276  -3.627  21.651  1.00 61.87  ? 3   ONL X CA  1 
HETATM 5199 C C   . ONL B 2 3   ? -2.373  -4.454  20.348  1.00 62.50  ? 3   ONL X C   1 
HETATM 5200 O O   . ONL B 2 3   ? -2.769  -5.620  20.333  1.00 63.28  ? 3   ONL X O   1 
HETATM 5201 C CB  . ONL B 2 3   ? -1.165  -4.217  22.520  1.00 60.22  ? 3   ONL X CB  1 
HETATM 5202 C CG  . ONL B 2 3   ? -0.528  -3.179  23.426  1.00 57.51  ? 3   ONL X CG  1 
HETATM 5203 C CD  . ONL B 2 3   ? 0.501   -3.832  24.331  1.00 56.87  ? 3   ONL X CD  1 
HETATM 5204 O OD  . ONL B 2 3   ? 0.335   -4.966  24.774  1.00 57.94  ? 3   ONL X OD  1 
HETATM 5205 C CE  . ONL B 2 3   ? 1.747   -3.046  24.690  1.00 55.50  ? 3   ONL X CE  1 
ATOM   5206 N N   . LEU B 2 4   ? -1.982  -3.801  19.267  1.00 63.11  ? 4   LEU X N   1 
ATOM   5207 C CA  . LEU B 2 4   ? -1.996  -4.360  17.925  1.00 63.11  ? 4   LEU X CA  1 
ATOM   5208 C C   . LEU B 2 4   ? -0.627  -4.168  17.290  1.00 62.80  ? 4   LEU X C   1 
ATOM   5209 O O   . LEU B 2 4   ? 0.093   -3.254  17.673  1.00 62.12  ? 4   LEU X O   1 
ATOM   5210 C CB  . LEU B 2 4   ? -2.978  -3.505  17.093  1.00 63.46  ? 4   LEU X CB  1 
ATOM   5211 C CG  . LEU B 2 4   ? -4.279  -3.111  17.819  1.00 63.72  ? 4   LEU X CG  1 
ATOM   5212 C CD1 . LEU B 2 4   ? -4.879  -1.836  17.206  1.00 64.08  ? 4   LEU X CD1 1 
ATOM   5213 C CD2 . LEU B 2 4   ? -5.316  -4.230  17.796  1.00 63.59  ? 4   LEU X CD2 1 
ATOM   5214 N N   . PRO B 2 5   ? -0.198  -4.940  16.281  1.00 65.31  ? 5   PRO X N   1 
ATOM   5215 C CA  . PRO B 2 5   ? 1.098   -4.751  15.591  1.00 65.78  ? 5   PRO X CA  1 
ATOM   5216 C C   . PRO B 2 5   ? 1.090   -3.316  15.020  1.00 67.25  ? 5   PRO X C   1 
ATOM   5217 O O   . PRO B 2 5   ? 0.021   -2.785  14.705  1.00 68.42  ? 5   PRO X O   1 
ATOM   5218 C CB  . PRO B 2 5   ? 1.062   -5.752  14.443  1.00 65.49  ? 5   PRO X CB  1 
ATOM   5219 C CG  . PRO B 2 5   ? -0.425  -6.064  14.265  1.00 65.81  ? 5   PRO X CG  1 
ATOM   5220 C CD  . PRO B 2 5   ? -0.963  -6.047  15.690  1.00 65.39  ? 5   PRO X CD  1 
ATOM   5221 N N   . PHE B 2 6   ? 2.258   -2.682  14.912  1.00 67.79  ? 6   PHE X N   1 
ATOM   5222 C CA  . PHE B 2 6   ? 2.308   -1.299  14.387  1.00 68.84  ? 6   PHE X CA  1 
ATOM   5223 C C   . PHE B 2 6   ? 1.728   -1.305  12.959  1.00 70.66  ? 6   PHE X C   1 
ATOM   5224 O O   . PHE B 2 6   ? 1.867   -2.286  12.228  1.00 70.25  ? 6   PHE X O   1 
ATOM   5225 C CB  . PHE B 2 6   ? 3.728   -0.727  14.414  1.00 70.36  ? 6   PHE X CB  1 
ATOM   5226 C CG  . PHE B 2 6   ? 4.589   -1.370  13.327  1.00 71.37  ? 6   PHE X CG  1 
ATOM   5227 C CD1 . PHE B 2 6   ? 5.388   -2.457  13.632  1.00 71.26  ? 6   PHE X CD1 1 
ATOM   5228 C CD2 . PHE B 2 6   ? 4.561   -0.878  12.026  1.00 71.90  ? 6   PHE X CD2 1 
ATOM   5229 C CE1 . PHE B 2 6   ? 6.168   -3.054  12.643  1.00 71.85  ? 6   PHE X CE1 1 
ATOM   5230 C CE2 . PHE B 2 6   ? 5.332   -1.470  11.025  1.00 71.73  ? 6   PHE X CE2 1 
ATOM   5231 C CZ  . PHE B 2 6   ? 6.138   -2.563  11.337  1.00 71.65  ? 6   PHE X CZ  1 
HETATM 5232 N N   . NH2 B 2 7   ? 1.059   -0.211  12.607  1.00 72.07  ? 7   NH2 X N   1 
HETATM 5233 S S   . SO4 C 3 .   ? 20.216  -12.065 37.488  1.00 50.93  ? 688 SO4 A S   1 
HETATM 5234 O O1  . SO4 C 3 .   ? 21.630  -11.747 37.429  1.00 45.89  ? 688 SO4 A O1  1 
HETATM 5235 O O2  . SO4 C 3 .   ? 19.668  -12.326 36.165  1.00 50.32  ? 688 SO4 A O2  1 
HETATM 5236 O O3  . SO4 C 3 .   ? 19.929  -13.243 38.322  1.00 50.83  ? 688 SO4 A O3  1 
HETATM 5237 O O4  . SO4 C 3 .   ? 19.497  -10.938 38.060  1.00 49.90  ? 688 SO4 A O4  1 
HETATM 5238 S S   . SO4 D 3 .   ? 22.125  -11.861 43.063  1.00 60.69  ? 689 SO4 A S   1 
HETATM 5239 O O1  . SO4 D 3 .   ? 23.512  -12.227 42.771  1.00 58.66  ? 689 SO4 A O1  1 
HETATM 5240 O O2  . SO4 D 3 .   ? 21.229  -12.862 42.479  1.00 59.16  ? 689 SO4 A O2  1 
HETATM 5241 O O3  . SO4 D 3 .   ? 21.881  -11.844 44.513  1.00 60.85  ? 689 SO4 A O3  1 
HETATM 5242 O O4  . SO4 D 3 .   ? 21.889  -10.536 42.506  1.00 56.94  ? 689 SO4 A O4  1 
HETATM 5243 S S   . SO4 E 3 .   ? 32.791  3.745   73.035  1.00 108.49 ? 690 SO4 A S   1 
HETATM 5244 O O1  . SO4 E 3 .   ? 34.054  3.038   72.821  1.00 108.46 ? 690 SO4 A O1  1 
HETATM 5245 O O2  . SO4 E 3 .   ? 32.331  4.273   71.749  1.00 108.15 ? 690 SO4 A O2  1 
HETATM 5246 O O3  . SO4 E 3 .   ? 31.803  2.824   73.599  1.00 107.82 ? 690 SO4 A O3  1 
HETATM 5247 O O4  . SO4 E 3 .   ? 32.988  4.854   73.967  1.00 108.49 ? 690 SO4 A O4  1 
HETATM 5248 S S   . SO4 F 3 .   ? 27.674  8.886   75.271  1.00 49.54  ? 691 SO4 A S   1 
HETATM 5249 O O1  . SO4 F 3 .   ? 28.945  8.207   75.280  1.00 46.52  ? 691 SO4 A O1  1 
HETATM 5250 O O2  . SO4 F 3 .   ? 26.885  8.494   74.102  1.00 49.27  ? 691 SO4 A O2  1 
HETATM 5251 O O3  . SO4 F 3 .   ? 26.829  8.586   76.404  1.00 49.34  ? 691 SO4 A O3  1 
HETATM 5252 O O4  . SO4 F 3 .   ? 27.949  10.318  75.190  1.00 50.07  ? 691 SO4 A O4  1 
HETATM 5253 S S   . SO4 G 3 .   ? 21.647  -12.709 -11.805 1.00 79.62  ? 692 SO4 A S   1 
HETATM 5254 O O1  . SO4 G 3 .   ? 22.843  -13.372 -12.321 1.00 79.96  ? 692 SO4 A O1  1 
HETATM 5255 O O2  . SO4 G 3 .   ? 20.709  -12.463 -12.894 1.00 78.75  ? 692 SO4 A O2  1 
HETATM 5256 O O3  . SO4 G 3 .   ? 21.014  -13.542 -10.789 1.00 78.86  ? 692 SO4 A O3  1 
HETATM 5257 O O4  . SO4 G 3 .   ? 22.032  -11.430 -11.211 1.00 80.37  ? 692 SO4 A O4  1 
HETATM 5258 O O   . HOH H 4 .   ? 4.599   10.419  34.998  1.00 25.68  ? 693 HOH A O   1 
HETATM 5259 O O   . HOH H 4 .   ? 17.130  -12.466 56.675  1.00 27.43  ? 694 HOH A O   1 
HETATM 5260 O O   . HOH H 4 .   ? 20.407  8.741   75.012  1.00 27.79  ? 695 HOH A O   1 
HETATM 5261 O O   . HOH H 4 .   ? 10.691  6.782   48.975  1.00 26.14  ? 696 HOH A O   1 
HETATM 5262 O O   . HOH H 4 .   ? 0.607   9.727   39.138  1.00 30.81  ? 697 HOH A O   1 
HETATM 5263 O O   . HOH H 4 .   ? 20.775  1.608   48.302  1.00 25.71  ? 698 HOH A O   1 
HETATM 5264 O O   . HOH H 4 .   ? 2.869   6.383   36.496  1.00 30.53  ? 699 HOH A O   1 
HETATM 5265 O O   . HOH H 4 .   ? 18.938  9.381   43.708  1.00 31.28  ? 700 HOH A O   1 
HETATM 5266 O O   . HOH H 4 .   ? 23.716  -2.920  59.551  1.00 44.04  ? 701 HOH A O   1 
HETATM 5267 O O   . HOH H 4 .   ? 14.580  5.522   59.358  1.00 27.52  ? 702 HOH A O   1 
HETATM 5268 O O   . HOH H 4 .   ? 2.153   7.997   33.117  1.00 31.66  ? 703 HOH A O   1 
HETATM 5269 O O   . HOH H 4 .   ? 22.661  4.239   69.451  1.00 33.76  ? 704 HOH A O   1 
HETATM 5270 O O   . HOH H 4 .   ? 17.572  -8.431  41.036  1.00 36.59  ? 705 HOH A O   1 
HETATM 5271 O O   . HOH H 4 .   ? 1.910   10.565  54.266  1.00 37.51  ? 706 HOH A O   1 
HETATM 5272 O O   . HOH H 4 .   ? 20.918  3.844   49.855  1.00 29.64  ? 707 HOH A O   1 
HETATM 5273 O O   . HOH H 4 .   ? 0.994   8.269   35.828  1.00 29.81  ? 708 HOH A O   1 
HETATM 5274 O O   . HOH H 4 .   ? 21.832  12.873  71.454  1.00 30.76  ? 709 HOH A O   1 
HETATM 5275 O O   . HOH H 4 .   ? -0.927  -3.680  53.768  1.00 40.65  ? 710 HOH A O   1 
HETATM 5276 O O   . HOH H 4 .   ? 6.102   4.155   49.434  1.00 26.27  ? 711 HOH A O   1 
HETATM 5277 O O   . HOH H 4 .   ? 21.570  9.646   47.295  1.00 34.33  ? 712 HOH A O   1 
HETATM 5278 O O   . HOH H 4 .   ? 11.392  -11.719 54.270  1.00 30.30  ? 713 HOH A O   1 
HETATM 5279 O O   . HOH H 4 .   ? 21.103  1.955   43.586  1.00 25.95  ? 714 HOH A O   1 
HETATM 5280 O O   . HOH H 4 .   ? 22.588  11.455  79.309  1.00 35.23  ? 715 HOH A O   1 
HETATM 5281 O O   . HOH H 4 .   ? 19.683  -12.046 55.701  1.00 32.14  ? 716 HOH A O   1 
HETATM 5282 O O   . HOH H 4 .   ? 20.495  7.805   77.731  1.00 34.82  ? 717 HOH A O   1 
HETATM 5283 O O   . HOH H 4 .   ? 12.196  13.166  32.020  1.00 45.37  ? 718 HOH A O   1 
HETATM 5284 O O   . HOH H 4 .   ? -2.745  13.310  30.120  1.00 33.89  ? 719 HOH A O   1 
HETATM 5285 O O   . HOH H 4 .   ? 28.665  6.486   68.620  1.00 41.22  ? 720 HOH A O   1 
HETATM 5286 O O   . HOH H 4 .   ? 4.523   -3.481  66.758  1.00 31.52  ? 721 HOH A O   1 
HETATM 5287 O O   . HOH H 4 .   ? 22.775  6.960   69.916  1.00 29.92  ? 722 HOH A O   1 
HETATM 5288 O O   . HOH H 4 .   ? 13.045  9.084   30.559  1.00 30.45  ? 723 HOH A O   1 
HETATM 5289 O O   . HOH H 4 .   ? 16.507  -19.847 50.627  1.00 39.28  ? 724 HOH A O   1 
HETATM 5290 O O   . HOH H 4 .   ? 14.377  -8.171  67.395  1.00 40.38  ? 725 HOH A O   1 
HETATM 5291 O O   . HOH H 4 .   ? 21.471  8.182   33.543  1.00 40.85  ? 726 HOH A O   1 
HETATM 5292 O O   . HOH H 4 .   ? 12.692  13.997  34.992  1.00 35.52  ? 727 HOH A O   1 
HETATM 5293 O O   . HOH H 4 .   ? 19.910  -12.797 46.030  1.00 38.23  ? 728 HOH A O   1 
HETATM 5294 O O   . HOH H 4 .   ? 25.147  6.495   40.095  1.00 35.60  ? 729 HOH A O   1 
HETATM 5295 O O   . HOH H 4 .   ? 10.905  -11.292 34.521  1.00 40.27  ? 730 HOH A O   1 
HETATM 5296 O O   . HOH H 4 .   ? 23.040  -16.859 52.591  1.00 41.29  ? 731 HOH A O   1 
HETATM 5297 O O   . HOH H 4 .   ? 8.728   -17.908 49.685  1.00 52.07  ? 732 HOH A O   1 
HETATM 5298 O O   . HOH H 4 .   ? 3.800   16.914  42.230  1.00 35.58  ? 733 HOH A O   1 
HETATM 5299 O O   . HOH H 4 .   ? 24.870  0.249   62.862  1.00 31.51  ? 734 HOH A O   1 
HETATM 5300 O O   . HOH H 4 .   ? 26.454  5.129   37.433  1.00 38.11  ? 735 HOH A O   1 
HETATM 5301 O O   . HOH H 4 .   ? 16.417  -9.614  67.677  1.00 47.50  ? 736 HOH A O   1 
HETATM 5302 O O   . HOH H 4 .   ? 20.793  9.476   56.436  1.00 48.96  ? 737 HOH A O   1 
HETATM 5303 O O   . HOH H 4 .   ? 10.422  -7.823  54.607  1.00 32.31  ? 738 HOH A O   1 
HETATM 5304 O O   . HOH H 4 .   ? 25.923  13.471  71.878  1.00 45.42  ? 739 HOH A O   1 
HETATM 5305 O O   . HOH H 4 .   ? 26.025  12.002  77.540  1.00 46.66  ? 740 HOH A O   1 
HETATM 5306 O O   . HOH H 4 .   ? 7.384   -22.635 -5.729  1.00 40.84  ? 741 HOH A O   1 
HETATM 5307 O O   . HOH H 4 .   ? 18.264  -7.958  -5.916  1.00 51.77  ? 742 HOH A O   1 
HETATM 5308 O O   . HOH H 4 .   ? 10.773  14.764  23.407  1.00 30.37  ? 743 HOH A O   1 
HETATM 5309 O O   . HOH H 4 .   ? 11.015  -24.622 -20.395 1.00 62.77  ? 744 HOH A O   1 
HETATM 5310 O O   . HOH H 4 .   ? 19.377  -18.370 53.015  1.00 34.30  ? 745 HOH A O   1 
HETATM 5311 O O   . HOH H 4 .   ? 14.655  -7.716  53.996  1.00 39.10  ? 746 HOH A O   1 
HETATM 5312 O O   . HOH H 4 .   ? 22.780  -2.549  53.718  1.00 34.89  ? 747 HOH A O   1 
HETATM 5313 O O   . HOH H 4 .   ? 10.166  0.427   85.798  1.00 37.44  ? 748 HOH A O   1 
HETATM 5314 O O   . HOH H 4 .   ? 13.861  12.807  19.936  1.00 46.72  ? 749 HOH A O   1 
HETATM 5315 O O   . HOH H 4 .   ? 25.588  1.517   58.426  1.00 40.01  ? 750 HOH A O   1 
HETATM 5316 O O   . HOH H 4 .   ? 18.695  10.818  65.994  1.00 40.05  ? 751 HOH A O   1 
HETATM 5317 O O   . HOH H 4 .   ? 11.569  12.258  60.850  1.00 33.16  ? 752 HOH A O   1 
HETATM 5318 O O   . HOH H 4 .   ? 24.618  8.175   76.704  1.00 36.16  ? 753 HOH A O   1 
HETATM 5319 O O   . HOH H 4 .   ? -1.094  0.504   59.167  1.00 45.81  ? 754 HOH A O   1 
HETATM 5320 O O   . HOH H 4 .   ? 17.925  4.974   21.361  1.00 35.71  ? 755 HOH A O   1 
HETATM 5321 O O   . HOH H 4 .   ? 12.641  -20.928 41.699  1.00 45.60  ? 756 HOH A O   1 
HETATM 5322 O O   . HOH H 4 .   ? 10.393  10.599  54.238  1.00 27.57  ? 757 HOH A O   1 
HETATM 5323 O O   . HOH H 4 .   ? 22.538  -5.103  28.697  1.00 39.66  ? 758 HOH A O   1 
HETATM 5324 O O   . HOH H 4 .   ? 14.661  -19.442 58.288  1.00 43.07  ? 759 HOH A O   1 
HETATM 5325 O O   . HOH H 4 .   ? 1.208   1.439   73.332  1.00 40.45  ? 760 HOH A O   1 
HETATM 5326 O O   . HOH H 4 .   ? 16.332  14.322  21.328  1.00 35.18  ? 761 HOH A O   1 
HETATM 5327 O O   . HOH H 4 .   ? 17.350  14.091  26.842  1.00 37.38  ? 762 HOH A O   1 
HETATM 5328 O O   . HOH H 4 .   ? 15.398  12.504  55.304  1.00 53.41  ? 763 HOH A O   1 
HETATM 5329 O O   . HOH H 4 .   ? 1.951   5.743   29.792  1.00 29.24  ? 764 HOH A O   1 
HETATM 5330 O O   . HOH H 4 .   ? 14.762  -8.035  92.111  1.00 54.57  ? 765 HOH A O   1 
HETATM 5331 O O   . HOH H 4 .   ? 22.010  -7.721  31.307  1.00 47.58  ? 766 HOH A O   1 
HETATM 5332 O O   . HOH H 4 .   ? 1.969   -3.542  80.625  1.00 30.44  ? 767 HOH A O   1 
HETATM 5333 O O   . HOH H 4 .   ? -2.627  -7.916  52.047  1.00 40.19  ? 768 HOH A O   1 
HETATM 5334 O O   . HOH H 4 .   ? 5.610   -5.942  80.132  1.00 42.68  ? 769 HOH A O   1 
HETATM 5335 O O   . HOH H 4 .   ? 0.691   5.799   68.032  1.00 43.23  ? 770 HOH A O   1 
HETATM 5336 O O   . HOH H 4 .   ? 2.970   -1.062  71.198  1.00 36.75  ? 771 HOH A O   1 
HETATM 5337 O O   . HOH H 4 .   ? 1.275   2.861   69.590  1.00 47.29  ? 772 HOH A O   1 
HETATM 5338 O O   . HOH H 4 .   ? -1.347  17.194  27.724  1.00 36.89  ? 773 HOH A O   1 
HETATM 5339 O O   . HOH H 4 .   ? 24.178  17.094  14.772  1.00 47.85  ? 774 HOH A O   1 
HETATM 5340 O O   . HOH H 4 .   ? 21.434  -3.718  77.672  1.00 44.49  ? 775 HOH A O   1 
HETATM 5341 O O   . HOH H 4 .   ? 19.667  8.230   20.212  1.00 39.89  ? 776 HOH A O   1 
HETATM 5342 O O   . HOH H 4 .   ? 22.633  -1.383  48.611  1.00 37.14  ? 777 HOH A O   1 
HETATM 5343 O O   . HOH H 4 .   ? 1.988   10.159  67.148  1.00 36.78  ? 778 HOH A O   1 
HETATM 5344 O O   . HOH H 4 .   ? 19.085  7.532   32.686  1.00 36.16  ? 779 HOH A O   1 
HETATM 5345 O O   . HOH H 4 .   ? 27.453  2.755   65.506  1.00 41.09  ? 780 HOH A O   1 
HETATM 5346 O O   . HOH H 4 .   ? 21.081  2.997   77.641  1.00 40.83  ? 781 HOH A O   1 
HETATM 5347 O O   . HOH H 4 .   ? 11.691  -6.341  84.039  1.00 38.62  ? 782 HOH A O   1 
HETATM 5348 O O   . HOH H 4 .   ? 25.738  -4.744  55.734  1.00 64.83  ? 783 HOH A O   1 
HETATM 5349 O O   . HOH H 4 .   ? 10.925  -6.198  34.504  1.00 41.06  ? 784 HOH A O   1 
HETATM 5350 O O   . HOH H 4 .   ? 23.052  -9.334  39.172  1.00 48.89  ? 785 HOH A O   1 
HETATM 5351 O O   . HOH H 4 .   ? 13.496  3.871   15.177  1.00 48.40  ? 786 HOH A O   1 
HETATM 5352 O O   . HOH H 4 .   ? -0.076  11.228  60.491  1.00 41.18  ? 787 HOH A O   1 
HETATM 5353 O O   . HOH H 4 .   ? 13.880  13.015  15.353  1.00 44.95  ? 788 HOH A O   1 
HETATM 5354 O O   . HOH H 4 .   ? 7.893   -0.491  21.261  1.00 46.81  ? 789 HOH A O   1 
HETATM 5355 O O   . HOH H 4 .   ? 14.901  8.927   85.814  1.00 46.50  ? 790 HOH A O   1 
HETATM 5356 O O   . HOH H 4 .   ? 25.107  3.733   68.610  1.00 39.52  ? 791 HOH A O   1 
HETATM 5357 O O   . HOH H 4 .   ? 21.914  -17.848 54.963  1.00 37.63  ? 792 HOH A O   1 
HETATM 5358 O O   . HOH H 4 .   ? 15.680  10.028  31.496  1.00 31.60  ? 793 HOH A O   1 
HETATM 5359 O O   . HOH H 4 .   ? 14.422  16.074  20.377  1.00 41.47  ? 794 HOH A O   1 
HETATM 5360 O O   . HOH H 4 .   ? 24.462  -0.300  49.965  1.00 53.82  ? 795 HOH A O   1 
HETATM 5361 O O   . HOH H 4 .   ? 22.832  -1.697  56.253  1.00 39.31  ? 796 HOH A O   1 
HETATM 5362 O O   . HOH H 4 .   ? 19.516  9.971   78.927  1.00 41.38  ? 797 HOH A O   1 
HETATM 5363 O O   . HOH H 4 .   ? 11.290  -7.311  86.692  1.00 40.05  ? 798 HOH A O   1 
HETATM 5364 O O   . HOH H 4 .   ? 0.751   8.666   52.617  1.00 51.36  ? 799 HOH A O   1 
HETATM 5365 O O   . HOH H 4 .   ? 6.203   17.698  26.903  1.00 35.95  ? 800 HOH A O   1 
HETATM 5366 O O   . HOH H 4 .   ? 17.296  -10.288 70.327  1.00 65.52  ? 801 HOH A O   1 
HETATM 5367 O O   . HOH H 4 .   ? 21.132  10.658  44.766  1.00 40.88  ? 802 HOH A O   1 
HETATM 5368 O O   . HOH H 4 .   ? 23.405  8.888   79.011  1.00 49.31  ? 803 HOH A O   1 
HETATM 5369 O O   . HOH H 4 .   ? -2.080  -2.734  58.062  1.00 67.47  ? 804 HOH A O   1 
HETATM 5370 O O   . HOH H 4 .   ? 11.232  -1.243  87.930  1.00 44.22  ? 805 HOH A O   1 
HETATM 5371 O O   . HOH H 4 .   ? 18.417  10.208  28.763  1.00 39.27  ? 806 HOH A O   1 
HETATM 5372 O O   . HOH H 4 .   ? 18.108  15.640  23.234  1.00 37.13  ? 807 HOH A O   1 
HETATM 5373 O O   . HOH H 4 .   ? 0.012   8.410   67.103  1.00 35.26  ? 808 HOH A O   1 
HETATM 5374 O O   . HOH H 4 .   ? 25.129  2.049   66.526  1.00 38.15  ? 809 HOH A O   1 
HETATM 5375 O O   . HOH H 4 .   ? 22.781  -2.858  43.502  1.00 48.44  ? 810 HOH A O   1 
HETATM 5376 O O   . HOH H 4 .   ? 26.270  11.484  80.341  1.00 37.73  ? 811 HOH A O   1 
HETATM 5377 O O   . HOH H 4 .   ? 4.226   -1.993  63.723  1.00 39.37  ? 812 HOH A O   1 
HETATM 5378 O O   . HOH H 4 .   ? 10.878  -9.950  58.091  1.00 41.84  ? 813 HOH A O   1 
HETATM 5379 O O   . HOH H 4 .   ? 5.853   -3.414  73.478  1.00 40.63  ? 814 HOH A O   1 
HETATM 5380 O O   . HOH H 4 .   ? 0.202   8.487   60.247  1.00 40.75  ? 815 HOH A O   1 
HETATM 5381 O O   . HOH H 4 .   ? 11.382  14.778  83.481  1.00 61.77  ? 816 HOH A O   1 
HETATM 5382 O O   . HOH H 4 .   ? 14.123  11.047  17.210  1.00 50.98  ? 817 HOH A O   1 
HETATM 5383 O O   . HOH H 4 .   ? 20.062  -16.482 60.582  1.00 40.52  ? 818 HOH A O   1 
HETATM 5384 O O   . HOH H 4 .   ? 16.676  13.058  34.347  1.00 35.19  ? 819 HOH A O   1 
HETATM 5385 O O   . HOH H 4 .   ? 6.752   13.509  34.274  1.00 35.87  ? 820 HOH A O   1 
HETATM 5386 O O   . HOH H 4 .   ? 24.574  -2.894  64.293  1.00 55.25  ? 821 HOH A O   1 
HETATM 5387 O O   . HOH H 4 .   ? -2.889  15.665  27.642  1.00 47.82  ? 822 HOH A O   1 
HETATM 5388 O O   . HOH H 4 .   ? 7.352   13.973  20.067  1.00 43.74  ? 823 HOH A O   1 
HETATM 5389 O O   . HOH H 4 .   ? 23.874  -1.618  45.723  1.00 48.74  ? 824 HOH A O   1 
HETATM 5390 O O   . HOH H 4 .   ? 9.108   -11.132 74.398  1.00 44.44  ? 825 HOH A O   1 
HETATM 5391 O O   . HOH H 4 .   ? -2.435  -27.834 -31.040 1.00 62.48  ? 826 HOH A O   1 
HETATM 5392 O O   . HOH H 4 .   ? 12.867  -8.993  54.799  1.00 38.44  ? 827 HOH A O   1 
HETATM 5393 O O   . HOH H 4 .   ? 18.392  -17.540 62.467  1.00 57.95  ? 828 HOH A O   1 
HETATM 5394 O O   . HOH H 4 .   ? 8.717   -9.926  33.183  1.00 59.20  ? 829 HOH A O   1 
HETATM 5395 O O   . HOH H 4 .   ? 9.748   -11.483 56.332  1.00 40.35  ? 830 HOH A O   1 
HETATM 5396 O O   . HOH H 4 .   ? 21.404  -18.533 59.444  1.00 46.69  ? 831 HOH A O   1 
HETATM 5397 O O   . HOH H 4 .   ? 15.404  12.673  31.770  1.00 39.45  ? 832 HOH A O   1 
HETATM 5398 O O   . HOH H 4 .   ? 4.192   3.990   86.542  1.00 65.97  ? 833 HOH A O   1 
HETATM 5399 O O   . HOH H 4 .   ? 16.281  4.312   15.381  1.00 69.59  ? 834 HOH A O   1 
HETATM 5400 O O   . HOH H 4 .   ? 11.081  -10.769 61.371  1.00 44.17  ? 835 HOH A O   1 
HETATM 5401 O O   . HOH H 4 .   ? 27.641  2.899   70.105  1.00 38.34  ? 836 HOH A O   1 
HETATM 5402 O O   . HOH H 4 .   ? 25.218  12.945  68.733  1.00 41.19  ? 837 HOH A O   1 
HETATM 5403 O O   . HOH H 4 .   ? 22.149  8.576   60.730  1.00 45.59  ? 838 HOH A O   1 
HETATM 5404 O O   . HOH H 4 .   ? 28.274  -0.490  25.232  1.00 53.75  ? 839 HOH A O   1 
HETATM 5405 O O   . HOH H 4 .   ? 17.463  10.391  34.180  1.00 33.75  ? 840 HOH A O   1 
HETATM 5406 O O   . HOH H 4 .   ? -3.938  -9.669  -6.886  1.00 77.37  ? 841 HOH A O   1 
HETATM 5407 O O   . HOH H 4 .   ? -3.213  -2.917  55.241  1.00 45.82  ? 842 HOH A O   1 
HETATM 5408 O O   . HOH H 4 .   ? -1.807  2.538   79.648  1.00 45.18  ? 843 HOH A O   1 
HETATM 5409 O O   . HOH H 4 .   ? 27.345  -12.001 60.982  1.00 46.02  ? 844 HOH A O   1 
HETATM 5410 O O   . HOH H 4 .   ? 19.719  -7.257  40.783  1.00 38.09  ? 845 HOH A O   1 
HETATM 5411 O O   . HOH H 4 .   ? 10.210  10.979  17.483  1.00 51.39  ? 846 HOH A O   1 
HETATM 5412 O O   . HOH H 4 .   ? 18.077  9.186   83.006  1.00 50.58  ? 847 HOH A O   1 
HETATM 5413 O O   . HOH H 4 .   ? 4.840   15.571  62.470  1.00 54.87  ? 848 HOH A O   1 
HETATM 5414 O O   . HOH H 4 .   ? 11.809  -5.079  88.369  1.00 39.72  ? 849 HOH A O   1 
HETATM 5415 O O   . HOH H 4 .   ? 26.412  -1.231  64.019  1.00 68.05  ? 850 HOH A O   1 
HETATM 5416 O O   . HOH H 4 .   ? 2.298   -7.441  66.241  1.00 46.95  ? 851 HOH A O   1 
HETATM 5417 O O   . HOH H 4 .   ? 26.109  6.135   68.068  1.00 37.34  ? 852 HOH A O   1 
HETATM 5418 O O   . HOH H 4 .   ? 2.907   9.772   37.066  1.00 28.79  ? 853 HOH A O   1 
HETATM 5419 O O   . HOH H 4 .   ? 21.512  -2.862  58.292  1.00 32.29  ? 854 HOH A O   1 
HETATM 5420 O O   . HOH H 4 .   ? 24.598  0.264   56.249  1.00 37.12  ? 855 HOH A O   1 
HETATM 5421 O O   . HOH H 4 .   ? 15.047  -20.161 42.460  1.00 42.18  ? 856 HOH A O   1 
HETATM 5422 O O   . HOH H 4 .   ? 24.209  -4.750  61.427  1.00 49.13  ? 857 HOH A O   1 
HETATM 5423 O O   . HOH H 4 .   ? 14.966  14.257  35.968  1.00 47.63  ? 858 HOH A O   1 
HETATM 5424 O O   . HOH H 4 .   ? 10.827  14.856  35.607  1.00 52.76  ? 859 HOH A O   1 
HETATM 5425 O O   . HOH H 4 .   ? 4.095   -14.510 53.459  1.00 56.88  ? 860 HOH A O   1 
HETATM 5426 O O   . HOH H 4 .   ? 12.543  -7.009  95.333  1.00 45.36  ? 861 HOH A O   1 
HETATM 5427 O O   . HOH H 4 .   ? 0.980   -3.235  57.008  1.00 59.28  ? 862 HOH A O   1 
HETATM 5428 O O   . HOH H 4 .   ? -1.364  -1.013  54.216  1.00 55.65  ? 863 HOH A O   1 
HETATM 5429 O O   . HOH H 4 .   ? 25.178  -12.518 63.563  1.00 45.54  ? 864 HOH A O   1 
HETATM 5430 O O   . HOH H 4 .   ? 3.227   13.197  55.057  1.00 41.56  ? 865 HOH A O   1 
HETATM 5431 O O   . HOH H 4 .   ? 4.764   -2.675  60.988  1.00 42.62  ? 866 HOH A O   1 
HETATM 5432 O O   . HOH H 4 .   ? 6.384   16.917  34.055  1.00 37.05  ? 867 HOH A O   1 
HETATM 5433 O O   . HOH H 4 .   ? 13.351  14.793  68.197  1.00 44.94  ? 868 HOH A O   1 
HETATM 5434 O O   . HOH H 4 .   ? 6.310   12.634  16.188  1.00 54.09  ? 869 HOH A O   1 
HETATM 5435 O O   . HOH H 4 .   ? -5.023  -14.114 -45.227 1.00 86.55  ? 870 HOH A O   1 
HETATM 5436 O O   . HOH H 4 .   ? 8.910   20.959  44.023  1.00 38.92  ? 871 HOH A O   1 
HETATM 5437 O O   . HOH H 4 .   ? 3.108   -9.822  64.950  1.00 47.02  ? 872 HOH A O   1 
HETATM 5438 O O   . HOH H 4 .   ? 8.432   -23.487 3.347   1.00 42.94  ? 873 HOH A O   1 
HETATM 5439 O O   . HOH H 4 .   ? 4.085   -22.057 44.627  1.00 60.10  ? 874 HOH A O   1 
HETATM 5440 O O   . HOH H 4 .   ? 14.022  -11.003 -15.179 1.00 42.09  ? 875 HOH A O   1 
HETATM 5441 O O   . HOH H 4 .   ? 16.185  -2.927  83.661  1.00 38.15  ? 876 HOH A O   1 
HETATM 5442 O O   . HOH H 4 .   ? 0.429   -0.727  55.896  1.00 42.48  ? 877 HOH A O   1 
HETATM 5443 O O   . HOH H 4 .   ? 18.430  -22.766 47.586  1.00 38.44  ? 878 HOH A O   1 
HETATM 5444 O O   . HOH H 4 .   ? -0.413  12.815  58.221  1.00 45.87  ? 879 HOH A O   1 
HETATM 5445 O O   . HOH H 4 .   ? 27.209  -2.929  33.112  1.00 40.76  ? 880 HOH A O   1 
HETATM 5446 O O   . HOH H 4 .   ? 0.314   2.965   11.923  1.00 50.08  ? 881 HOH A O   1 
HETATM 5447 O O   . HOH H 4 .   ? 11.457  -22.767 -29.177 1.00 49.57  ? 882 HOH A O   1 
HETATM 5448 O O   . HOH H 4 .   ? 25.819  -0.567  67.101  1.00 44.31  ? 883 HOH A O   1 
HETATM 5449 O O   . HOH H 4 .   ? 23.830  -12.793 68.303  1.00 75.25  ? 884 HOH A O   1 
HETATM 5450 O O   . HOH H 4 .   ? 23.943  5.434   55.244  1.00 59.94  ? 885 HOH A O   1 
HETATM 5451 O O   . HOH H 4 .   ? 26.854  19.299  21.116  1.00 59.50  ? 886 HOH A O   1 
HETATM 5452 O O   . HOH H 4 .   ? 28.442  21.070  22.265  1.00 48.06  ? 887 HOH A O   1 
HETATM 5453 O O   . HOH H 4 .   ? 10.947  -15.276 -30.797 1.00 42.62  ? 888 HOH A O   1 
HETATM 5454 O O   . HOH H 4 .   ? 20.392  12.075  31.788  1.00 50.74  ? 889 HOH A O   1 
HETATM 5455 O O   . HOH H 4 .   ? -5.556  1.948   22.525  1.00 43.27  ? 890 HOH A O   1 
HETATM 5456 O O   . HOH H 4 .   ? 25.125  -16.546 51.057  1.00 49.67  ? 891 HOH A O   1 
HETATM 5457 O O   . HOH H 4 .   ? 25.966  -14.180 50.370  1.00 56.23  ? 892 HOH A O   1 
HETATM 5458 O O   . HOH H 4 .   ? 14.419  15.983  52.023  1.00 46.39  ? 893 HOH A O   1 
HETATM 5459 O O   . HOH H 4 .   ? 15.111  -8.862  -12.708 1.00 49.32  ? 894 HOH A O   1 
HETATM 5460 O O   . HOH H 4 .   ? 11.499  -5.823  97.212  1.00 45.52  ? 895 HOH A O   1 
HETATM 5461 O O   . HOH H 4 .   ? 24.454  -11.630 65.590  1.00 53.35  ? 896 HOH A O   1 
HETATM 5462 O O   . HOH H 4 .   ? 16.075  9.470   16.282  1.00 53.16  ? 897 HOH A O   1 
HETATM 5463 O O   . HOH H 4 .   ? 24.485  -7.090  29.841  1.00 63.36  ? 898 HOH A O   1 
HETATM 5464 O O   . HOH H 4 .   ? 10.916  -20.018 50.438  1.00 41.40  ? 899 HOH A O   1 
HETATM 5465 O O   . HOH H 4 .   ? 12.172  16.707  53.170  1.00 45.48  ? 900 HOH A O   1 
HETATM 5466 O O   . HOH H 4 .   ? 17.457  14.049  42.276  1.00 51.70  ? 901 HOH A O   1 
HETATM 5467 O O   . HOH H 4 .   ? 26.980  -0.237  54.929  1.00 66.15  ? 902 HOH A O   1 
HETATM 5468 O O   . HOH H 4 .   ? 4.491   19.889  35.600  1.00 55.42  ? 903 HOH A O   1 
HETATM 5469 O O   . HOH H 4 .   ? 19.046  9.064   40.910  1.00 34.35  ? 904 HOH A O   1 
HETATM 5470 O O   . HOH H 4 .   ? 18.948  8.163   66.471  1.00 33.95  ? 905 HOH A O   1 
HETATM 5471 O O   . HOH H 4 .   ? 13.420  -6.912  35.818  1.00 33.75  ? 906 HOH A O   1 
HETATM 5472 O O   . HOH H 4 .   ? 4.510   -2.669  69.571  1.00 35.52  ? 907 HOH A O   1 
HETATM 5473 O O   . HOH H 4 .   ? 11.278  14.709  55.104  1.00 45.91  ? 908 HOH A O   1 
HETATM 5474 O O   . HOH H 4 .   ? 20.034  11.821  77.107  1.00 35.63  ? 909 HOH A O   1 
HETATM 5475 O O   . HOH H 4 .   ? 11.043  -15.197 58.988  1.00 51.13  ? 910 HOH A O   1 
HETATM 5476 O O   . HOH H 4 .   ? 11.473  -4.133  -42.364 1.00 42.10  ? 911 HOH A O   1 
HETATM 5477 O O   . HOH H 4 .   ? 24.646  -1.920  43.887  1.00 59.30  ? 912 HOH A O   1 
HETATM 5478 O O   . HOH H 4 .   ? 14.063  13.675  38.309  1.00 33.14  ? 913 HOH A O   1 
HETATM 5479 O O   . HOH H 4 .   ? -4.066  5.765   14.411  1.00 50.40  ? 914 HOH A O   1 
HETATM 5480 O O   . HOH H 4 .   ? 3.496   13.302  52.638  1.00 50.01  ? 915 HOH A O   1 
HETATM 5481 O O   . HOH H 4 .   ? 13.461  -19.491 50.859  1.00 47.82  ? 916 HOH A O   1 
HETATM 5482 O O   . HOH H 4 .   ? 23.248  8.623   56.206  1.00 66.10  ? 917 HOH A O   1 
HETATM 5483 O O   . HOH H 4 .   ? 7.791   11.704  18.441  1.00 45.53  ? 918 HOH A O   1 
HETATM 5484 O O   . HOH H 4 .   ? 27.983  0.672   30.499  1.00 56.75  ? 919 HOH A O   1 
HETATM 5485 O O   . HOH H 4 .   ? -0.550  -7.945  -19.153 1.00 48.56  ? 920 HOH A O   1 
HETATM 5486 O O   . HOH H 4 .   ? -7.067  -1.525  31.046  1.00 48.53  ? 921 HOH A O   1 
HETATM 5487 O O   . HOH H 4 .   ? 14.231  -14.218 62.537  1.00 50.03  ? 922 HOH A O   1 
HETATM 5488 O O   . HOH H 4 .   ? -2.846  15.935  38.567  1.00 51.43  ? 923 HOH A O   1 
HETATM 5489 O O   . HOH H 4 .   ? 23.403  -0.957  83.828  1.00 41.97  ? 924 HOH A O   1 
HETATM 5490 O O   . HOH H 4 .   ? 22.496  7.228   63.100  1.00 44.69  ? 925 HOH A O   1 
HETATM 5491 O O   . HOH H 4 .   ? -11.084 10.016  30.868  1.00 49.33  ? 926 HOH A O   1 
HETATM 5492 O O   . HOH H 4 .   ? 19.113  11.094  62.738  1.00 50.21  ? 927 HOH A O   1 
HETATM 5493 O O   . HOH H 4 .   ? 19.670  -15.364 45.743  1.00 41.51  ? 928 HOH A O   1 
HETATM 5494 O O   . HOH H 4 .   ? 7.068   -22.863 -0.899  1.00 42.50  ? 929 HOH A O   1 
HETATM 5495 O O   . HOH H 4 .   ? 12.059  -6.940  90.529  1.00 49.41  ? 930 HOH A O   1 
HETATM 5496 O O   . HOH H 4 .   ? 23.174  -8.651  42.557  1.00 48.46  ? 931 HOH A O   1 
HETATM 5497 O O   . HOH H 4 .   ? 12.138  14.443  20.620  1.00 43.77  ? 932 HOH A O   1 
HETATM 5498 O O   . HOH H 4 .   ? 12.550  -12.500 18.196  1.00 54.99  ? 933 HOH A O   1 
HETATM 5499 O O   . HOH H 4 .   ? 10.404  -2.977  -45.285 1.00 44.34  ? 934 HOH A O   1 
HETATM 5500 O O   . HOH H 4 .   ? 1.701   6.231   52.595  1.00 50.20  ? 935 HOH A O   1 
HETATM 5501 O O   . HOH H 4 .   ? -1.467  14.408  39.809  1.00 47.01  ? 936 HOH A O   1 
HETATM 5502 O O   . HOH H 4 .   ? 18.543  -5.979  72.403  1.00 48.72  ? 937 HOH A O   1 
HETATM 5503 O O   . HOH H 4 .   ? 9.531   -13.429 -24.075 1.00 50.39  ? 938 HOH A O   1 
HETATM 5504 O O   . HOH H 4 .   ? -8.528  10.107  30.482  1.00 48.89  ? 939 HOH A O   1 
HETATM 5505 O O   . HOH H 4 .   ? 24.895  -21.502 8.545   1.00 41.72  ? 940 HOH A O   1 
HETATM 5506 O O   . HOH H 4 .   ? 2.970   7.836   74.131  1.00 46.93  ? 941 HOH A O   1 
HETATM 5507 O O   . HOH H 4 .   ? 13.912  7.499   87.838  1.00 52.08  ? 942 HOH A O   1 
HETATM 5508 O O   . HOH H 4 .   ? 2.786   -10.136 -45.826 1.00 48.37  ? 943 HOH A O   1 
HETATM 5509 O O   . HOH H 4 .   ? 11.596  7.092   87.991  1.00 49.90  ? 944 HOH A O   1 
HETATM 5510 O O   . HOH H 4 .   ? 17.956  9.753   31.416  1.00 46.28  ? 945 HOH A O   1 
HETATM 5511 O O   . HOH H 4 .   ? 22.774  -17.634 46.077  1.00 48.71  ? 946 HOH A O   1 
HETATM 5512 O O   . HOH H 4 .   ? 20.285  -15.018 42.760  1.00 49.72  ? 947 HOH A O   1 
HETATM 5513 O O   . HOH H 4 .   ? 4.201   -5.906  66.614  1.00 35.21  ? 948 HOH A O   1 
HETATM 5514 O O   . HOH H 4 .   ? 1.624   -12.004 -45.794 1.00 45.54  ? 949 HOH A O   1 
HETATM 5515 O O   . HOH H 4 .   ? 8.389   11.579  76.990  1.00 39.47  ? 950 HOH A O   1 
HETATM 5516 O O   . HOH H 4 .   ? 9.386   -20.371 -22.066 1.00 44.18  ? 951 HOH A O   1 
HETATM 5517 O O   . HOH H 4 .   ? 12.177  -3.730  -39.958 1.00 39.58  ? 952 HOH A O   1 
HETATM 5518 O O   . HOH H 4 .   ? 21.240  12.278  54.232  1.00 36.89  ? 953 HOH A O   1 
HETATM 5519 O O   . HOH H 4 .   ? 7.523   16.573  52.479  1.00 41.88  ? 954 HOH A O   1 
# 
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   ALA 2   2   2   ALA ALA A . n 
A 1 3   GLU 3   3   3   GLU GLU A . n 
A 1 4   GLU 4   4   4   GLU GLU A . n 
A 1 5   LEU 5   5   5   LEU LEU A . n 
A 1 6   VAL 6   6   6   VAL VAL A . n 
A 1 7   LEU 7   7   7   LEU LEU A . n 
A 1 8   GLU 8   8   8   GLU GLU A . n 
A 1 9   ARG 9   9   9   ARG ARG A . n 
A 1 10  CYS 10  10  10  CYS CYS A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  GLU 13  13  13  GLU GLU A . n 
A 1 14  LEU 14  14  14  LEU LEU A . n 
A 1 15  GLU 15  15  15  GLU GLU A . n 
A 1 16  THR 16  16  16  THR THR A . n 
A 1 17  ASN 17  17  17  ASN ASN A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  ARG 19  19  19  ARG ARG A . n 
A 1 20  ASP 20  20  20  ASP ASP A . n 
A 1 21  HIS 21  21  21  HIS HIS A . n 
A 1 22  HIS 22  22  22  HIS HIS A . n 
A 1 23  THR 23  23  23  THR THR A . n 
A 1 24  ALA 24  24  24  ALA ALA A . n 
A 1 25  ASP 25  25  25  ASP ASP A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  CYS 27  27  27  CYS CYS A . n 
A 1 28  ARG 28  28  28  ARG ARG A . n 
A 1 29  GLU 29  29  29  GLU GLU A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  LEU 31  31  31  LEU LEU A . n 
A 1 32  VAL 32  32  32  VAL VAL A . n 
A 1 33  VAL 33  33  33  VAL VAL A . n 
A 1 34  ARG 34  34  34  ARG ARG A . n 
A 1 35  ARG 35  35  35  ARG ARG A . n 
A 1 36  GLY 36  36  36  GLY GLY A . n 
A 1 37  GLN 37  37  37  GLN GLN A . n 
A 1 38  PRO 38  38  38  PRO PRO A . n 
A 1 39  PHE 39  39  39  PHE PHE A . n 
A 1 40  TRP 40  40  40  TRP TRP A . n 
A 1 41  LEU 41  41  41  LEU LEU A . n 
A 1 42  THR 42  42  42  THR THR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  HIS 44  44  44  HIS HIS A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  GLU 46  46  46  GLU GLU A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  ARG 48  48  48  ARG ARG A . n 
A 1 49  ASN 49  49  49  ASN ASN A . n 
A 1 50  TYR 50  50  50  TYR TYR A . n 
A 1 51  GLN 51  51  51  GLN GLN A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  SER 53  53  53  SER SER A . n 
A 1 54  VAL 54  54  54  VAL VAL A . n 
A 1 55  ASP 55  55  55  ASP ASP A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  PHE 59  59  59  PHE PHE A . n 
A 1 60  SER 60  60  60  SER SER A . n 
A 1 61  VAL 61  61  61  VAL VAL A . n 
A 1 62  VAL 62  62  62  VAL VAL A . n 
A 1 63  THR 63  63  63  THR THR A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  PRO 65  65  65  PRO PRO A . n 
A 1 66  ALA 66  66  66  ALA ALA A . n 
A 1 67  PRO 67  67  67  PRO PRO A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  GLU 70  70  70  GLU GLU A . n 
A 1 71  ALA 71  71  71  ALA ALA A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  THR 73  73  73  THR THR A . n 
A 1 74  LYS 74  74  74  LYS LYS A . n 
A 1 75  ALA 75  75  75  ALA ALA A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  PHE 77  77  77  PHE PHE A . n 
A 1 78  PRO 78  78  78  PRO PRO A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  ARG 80  80  80  ARG ARG A . n 
A 1 81  ASP 81  81  81  ASP ASP A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  VAL 83  83  83  VAL VAL A . n 
A 1 84  GLU 84  84  84  GLU GLU A . n 
A 1 85  GLU 85  85  85  GLU GLU A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  ASP 87  87  87  ASP ASP A . n 
A 1 88  TRP 88  88  88  TRP TRP A . n 
A 1 89  THR 89  89  89  THR THR A . n 
A 1 90  ALA 90  90  90  ALA ALA A . n 
A 1 91  THR 91  91  91  THR THR A . n 
A 1 92  VAL 92  92  92  VAL VAL A . n 
A 1 93  VAL 93  93  93  VAL VAL A . n 
A 1 94  ASP 94  94  94  ASP ASP A . n 
A 1 95  GLN 95  95  95  GLN GLN A . n 
A 1 96  GLN 96  96  96  GLN GLN A . n 
A 1 97  ASP 97  97  97  ASP ASP A . n 
A 1 98  CYS 98  98  98  CYS CYS A . n 
A 1 99  THR 99  99  99  THR THR A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 SER 101 101 101 SER SER A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 PRO 107 107 107 PRO PRO A . n 
A 1 108 ALA 108 108 108 ALA ALA A . n 
A 1 109 ASN 109 109 109 ASN ASN A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 PRO 111 111 111 PRO PRO A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 GLY 113 113 113 GLY GLY A . n 
A 1 114 LEU 114 114 114 LEU LEU A . n 
A 1 115 TYR 115 115 115 TYR TYR A . n 
A 1 116 ARG 116 116 116 ARG ARG A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 SER 118 118 118 SER SER A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 ALA 121 121 121 ALA ALA A . n 
A 1 122 SER 122 122 122 SER SER A . n 
A 1 123 THR 123 123 123 THR THR A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 TYR 125 125 125 TYR TYR A . n 
A 1 126 GLN 126 126 126 GLN GLN A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 SER 129 129 129 SER SER A . n 
A 1 130 PHE 130 130 130 PHE PHE A . n 
A 1 131 VAL 131 131 131 VAL VAL A . n 
A 1 132 LEU 132 132 132 LEU LEU A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 HIS 134 134 134 HIS HIS A . n 
A 1 135 PHE 135 135 135 PHE PHE A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 LEU 137 137 137 LEU LEU A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 PHE 139 139 139 PHE PHE A . n 
A 1 140 ASN 140 140 140 ASN ASN A . n 
A 1 141 ALA 141 141 141 ALA ALA A . n 
A 1 142 TRP 142 142 142 TRP TRP A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 PRO 144 144 144 PRO PRO A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 ASP 146 146 146 ASP ASP A . n 
A 1 147 ALA 147 147 147 ALA ALA A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 TYR 149 149 149 TYR TYR A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 ASP 151 151 151 ASP ASP A . n 
A 1 152 SER 152 152 152 SER SER A . n 
A 1 153 GLU 153 153 153 GLU GLU A . n 
A 1 154 GLU 154 154 154 GLU GLU A . n 
A 1 155 GLU 155 155 155 GLU GLU A . n 
A 1 156 ARG 156 156 156 ARG ARG A . n 
A 1 157 GLN 157 157 157 GLN GLN A . n 
A 1 158 GLU 158 158 158 GLU GLU A . n 
A 1 159 TYR 159 159 159 TYR TYR A . n 
A 1 160 VAL 160 160 160 VAL VAL A . n 
A 1 161 LEU 161 161 161 LEU LEU A . n 
A 1 162 THR 162 162 162 THR THR A . n 
A 1 163 GLN 163 163 163 GLN GLN A . n 
A 1 164 GLN 164 164 164 GLN GLN A . n 
A 1 165 GLY 165 165 165 GLY GLY A . n 
A 1 166 PHE 166 166 166 PHE PHE A . n 
A 1 167 ILE 167 167 167 ILE ILE A . n 
A 1 168 TYR 168 168 168 TYR TYR A . n 
A 1 169 GLN 169 169 169 GLN GLN A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 SER 171 171 171 SER SER A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 LYS 173 173 173 LYS LYS A . n 
A 1 174 PHE 174 174 174 PHE PHE A . n 
A 1 175 ILE 175 175 175 ILE ILE A . n 
A 1 176 LYS 176 176 176 LYS LYS A . n 
A 1 177 ASN 177 177 177 ASN ASN A . n 
A 1 178 ILE 178 178 178 ILE ILE A . n 
A 1 179 PRO 179 179 179 PRO PRO A . n 
A 1 180 TRP 180 180 180 TRP TRP A . n 
A 1 181 ASN 181 181 181 ASN ASN A . n 
A 1 182 PHE 182 182 182 PHE PHE A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 GLN 184 184 184 GLN GLN A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 GLN 186 186 186 GLN GLN A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 GLY 188 188 188 GLY GLY A . n 
A 1 189 ILE 189 189 189 ILE ILE A . n 
A 1 190 LEU 190 190 190 LEU LEU A . n 
A 1 191 ASP 191 191 191 ASP ASP A . n 
A 1 192 ILE 192 192 192 ILE ILE A . n 
A 1 193 CYS 193 193 193 CYS CYS A . n 
A 1 194 LEU 194 194 194 LEU LEU A . n 
A 1 195 ILE 195 195 195 ILE ILE A . n 
A 1 196 LEU 196 196 196 LEU LEU A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 ASP 198 198 198 ASP ASP A . n 
A 1 199 VAL 199 199 199 VAL VAL A . n 
A 1 200 ASN 200 200 200 ASN ASN A . n 
A 1 201 PRO 201 201 201 PRO PRO A . n 
A 1 202 LYS 202 202 202 LYS LYS A . n 
A 1 203 PHE 203 203 203 PHE PHE A . n 
A 1 204 LEU 204 204 204 LEU LEU A . n 
A 1 205 LYS 205 205 205 LYS LYS A . n 
A 1 206 ASN 206 206 206 ASN ASN A . n 
A 1 207 ALA 207 207 207 ALA ALA A . n 
A 1 208 GLY 208 208 208 GLY GLY A . n 
A 1 209 ARG 209 209 209 ARG ARG A . n 
A 1 210 ASP 210 210 210 ASP ASP A . n 
A 1 211 CYS 211 211 211 CYS CYS A . n 
A 1 212 SER 212 212 212 SER SER A . n 
A 1 213 ARG 213 213 213 ARG ARG A . n 
A 1 214 ARG 214 214 214 ARG ARG A . n 
A 1 215 SER 215 215 215 SER SER A . n 
A 1 216 SER 216 216 216 SER SER A . n 
A 1 217 PRO 217 217 217 PRO PRO A . n 
A 1 218 VAL 218 218 218 VAL VAL A . n 
A 1 219 TYR 219 219 219 TYR TYR A . n 
A 1 220 VAL 220 220 220 VAL VAL A . n 
A 1 221 GLY 221 221 221 GLY GLY A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 VAL 223 223 223 VAL VAL A . n 
A 1 224 GLY 224 224 224 GLY GLY A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 GLY 226 226 226 GLY GLY A . n 
A 1 227 MET 227 227 227 MET MET A . n 
A 1 228 VAL 228 228 228 VAL VAL A . n 
A 1 229 ASN 229 229 229 ASN ASN A . n 
A 1 230 CYS 230 230 230 CYS CYS A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 ASP 232 232 232 ASP ASP A . n 
A 1 233 ASP 233 233 233 ASP ASP A . n 
A 1 234 GLN 234 234 234 GLN GLN A . n 
A 1 235 GLY 235 235 235 GLY GLY A . n 
A 1 236 VAL 236 236 236 VAL VAL A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 LEU 238 238 238 LEU LEU A . n 
A 1 239 GLY 239 239 239 GLY GLY A . n 
A 1 240 ARG 240 240 240 ARG ARG A . n 
A 1 241 TRP 241 241 241 TRP TRP A . n 
A 1 242 ASP 242 242 242 ASP ASP A . n 
A 1 243 ASN 243 243 243 ASN ASN A . n 
A 1 244 ASN 244 244 244 ASN ASN A . n 
A 1 245 TYR 245 245 245 TYR TYR A . n 
A 1 246 GLY 246 246 246 GLY GLY A . n 
A 1 247 ASP 247 247 247 ASP ASP A . n 
A 1 248 GLY 248 248 248 GLY GLY A . n 
A 1 249 VAL 249 249 249 VAL VAL A . n 
A 1 250 SER 250 250 250 SER SER A . n 
A 1 251 PRO 251 251 251 PRO PRO A . n 
A 1 252 MET 252 252 252 MET MET A . n 
A 1 253 SER 253 253 253 SER SER A . n 
A 1 254 TRP 254 254 254 TRP TRP A . n 
A 1 255 ILE 255 255 255 ILE ILE A . n 
A 1 256 GLY 256 256 256 GLY GLY A . n 
A 1 257 SER 257 257 257 SER SER A . n 
A 1 258 VAL 258 258 258 VAL VAL A . n 
A 1 259 ASP 259 259 259 ASP ASP A . n 
A 1 260 ILE 260 260 260 ILE ILE A . n 
A 1 261 LEU 261 261 261 LEU LEU A . n 
A 1 262 ARG 262 262 262 ARG ARG A . n 
A 1 263 ARG 263 263 263 ARG ARG A . n 
A 1 264 TRP 264 264 264 TRP TRP A . n 
A 1 265 LYS 265 265 265 LYS LYS A . n 
A 1 266 ASN 266 266 266 ASN ASN A . n 
A 1 267 HIS 267 267 267 HIS HIS A . n 
A 1 268 GLY 268 268 268 GLY GLY A . n 
A 1 269 CYS 269 269 269 CYS CYS A . n 
A 1 270 GLN 270 270 270 GLN GLN A . n 
A 1 271 ARG 271 271 271 ARG ARG A . n 
A 1 272 VAL 272 272 272 VAL VAL A . n 
A 1 273 LYS 273 273 273 LYS LYS A . n 
A 1 274 TYR 274 274 274 TYR TYR A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 GLN 276 276 276 GLN GLN A . n 
A 1 277 CYS 277 277 277 CYS CYS A . n 
A 1 278 TRP 278 278 278 TRP TRP A . n 
A 1 279 VAL 279 279 279 VAL VAL A . n 
A 1 280 PHE 280 280 280 PHE PHE A . n 
A 1 281 ALA 281 281 281 ALA ALA A . n 
A 1 282 ALA 282 282 282 ALA ALA A . n 
A 1 283 VAL 283 283 283 VAL VAL A . n 
A 1 284 ALA 284 284 284 ALA ALA A . n 
A 1 285 CYS 285 285 285 CYS CYS A . n 
A 1 286 THR 286 286 286 THR THR A . n 
A 1 287 VAL 287 287 287 VAL VAL A . n 
A 1 288 LEU 288 288 288 LEU LEU A . n 
A 1 289 ARG 289 289 289 ARG ARG A . n 
A 1 290 CYS 290 290 290 CYS CYS A . n 
A 1 291 LEU 291 291 291 LEU LEU A . n 
A 1 292 GLY 292 292 292 GLY GLY A . n 
A 1 293 ILE 293 293 293 ILE ILE A . n 
A 1 294 PRO 294 294 294 PRO PRO A . n 
A 1 295 THR 295 295 295 THR THR A . n 
A 1 296 ARG 296 296 296 ARG ARG A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 VAL 298 298 298 VAL VAL A . n 
A 1 299 THR 299 299 299 THR THR A . n 
A 1 300 ASN 300 300 300 ASN ASN A . n 
A 1 301 TYR 301 301 301 TYR TYR A . n 
A 1 302 ASN 302 302 302 ASN ASN A . n 
A 1 303 SER 303 303 303 SER SER A . n 
A 1 304 ALA 304 304 304 ALA ALA A . n 
A 1 305 HIS 305 305 305 HIS HIS A . n 
A 1 306 ASP 306 306 306 ASP ASP A . n 
A 1 307 GLN 307 307 ?   ?   ?   A . n 
A 1 308 ASN 308 308 ?   ?   ?   A . n 
A 1 309 SER 309 309 309 SER SER A . n 
A 1 310 ASN 310 310 310 ASN ASN A . n 
A 1 311 LEU 311 311 311 LEU LEU A . n 
A 1 312 LEU 312 312 312 LEU LEU A . n 
A 1 313 ILE 313 313 313 ILE ILE A . n 
A 1 314 GLU 314 314 314 GLU GLU A . n 
A 1 315 TYR 315 315 315 TYR TYR A . n 
A 1 316 PHE 316 316 316 PHE PHE A . n 
A 1 317 ARG 317 317 317 ARG ARG A . n 
A 1 318 ASN 318 318 318 ASN ASN A . n 
A 1 319 GLU 319 319 ?   ?   ?   A . n 
A 1 320 PHE 320 320 ?   ?   ?   A . n 
A 1 321 GLY 321 321 ?   ?   ?   A . n 
A 1 322 GLU 322 322 ?   ?   ?   A . n 
A 1 323 ILE 323 323 ?   ?   ?   A . n 
A 1 324 GLN 324 324 ?   ?   ?   A . n 
A 1 325 GLY 325 325 ?   ?   ?   A . n 
A 1 326 ASP 326 326 ?   ?   ?   A . n 
A 1 327 LYS 327 327 ?   ?   ?   A . n 
A 1 328 SER 328 328 328 SER SER A . n 
A 1 329 GLU 329 329 329 GLU GLU A . n 
A 1 330 MET 330 330 330 MET MET A . n 
A 1 331 ILE 331 331 331 ILE ILE A . n 
A 1 332 TRP 332 332 332 TRP TRP A . n 
A 1 333 ASN 333 333 333 ASN ASN A . n 
A 1 334 PHE 334 334 334 PHE PHE A . n 
A 1 335 HIS 335 335 335 HIS HIS A . n 
A 1 336 CYS 336 336 336 CYS CYS A . n 
A 1 337 TRP 337 337 337 TRP TRP A . n 
A 1 338 VAL 338 338 338 VAL VAL A . n 
A 1 339 GLU 339 339 339 GLU GLU A . n 
A 1 340 SER 340 340 340 SER SER A . n 
A 1 341 TRP 341 341 341 TRP TRP A . n 
A 1 342 MET 342 342 342 MET MET A . n 
A 1 343 THR 343 343 343 THR THR A . n 
A 1 344 ARG 344 344 344 ARG ARG A . n 
A 1 345 PRO 345 345 345 PRO PRO A . n 
A 1 346 ASP 346 346 346 ASP ASP A . n 
A 1 347 LEU 347 347 347 LEU LEU A . n 
A 1 348 GLN 348 348 348 GLN GLN A . n 
A 1 349 PRO 349 349 349 PRO PRO A . n 
A 1 350 GLY 350 350 350 GLY GLY A . n 
A 1 351 TYR 351 351 351 TYR TYR A . n 
A 1 352 GLU 352 352 352 GLU GLU A . n 
A 1 353 GLY 353 353 353 GLY GLY A . n 
A 1 354 TRP 354 354 354 TRP TRP A . n 
A 1 355 GLN 355 355 355 GLN GLN A . n 
A 1 356 ALA 356 356 356 ALA ALA A . n 
A 1 357 LEU 357 357 357 LEU LEU A . n 
A 1 358 ASP 358 358 358 ASP ASP A . n 
A 1 359 PRO 359 359 359 PRO PRO A . n 
A 1 360 THR 360 360 360 THR THR A . n 
A 1 361 PRO 361 361 361 PRO PRO A . n 
A 1 362 GLN 362 362 362 GLN GLN A . n 
A 1 363 GLU 363 363 363 GLU GLU A . n 
A 1 364 LYS 364 364 364 LYS LYS A . n 
A 1 365 SER 365 365 365 SER SER A . n 
A 1 366 GLU 366 366 366 GLU GLU A . n 
A 1 367 GLY 367 367 367 GLY GLY A . n 
A 1 368 THR 368 368 368 THR THR A . n 
A 1 369 TYR 369 369 369 TYR TYR A . n 
A 1 370 CYS 370 370 370 CYS CYS A . n 
A 1 371 CYS 371 371 371 CYS CYS A . n 
A 1 372 GLY 372 372 372 GLY GLY A . n 
A 1 373 PRO 373 373 373 PRO PRO A . n 
A 1 374 VAL 374 374 374 VAL VAL A . n 
A 1 375 PRO 375 375 375 PRO PRO A . n 
A 1 376 VAL 376 376 376 VAL VAL A . n 
A 1 377 ARG 377 377 377 ARG ARG A . n 
A 1 378 ALA 378 378 378 ALA ALA A . n 
A 1 379 ILE 379 379 379 ILE ILE A . n 
A 1 380 LYS 380 380 380 LYS LYS A . n 
A 1 381 GLU 381 381 381 GLU GLU A . n 
A 1 382 GLY 382 382 382 GLY GLY A . n 
A 1 383 ASP 383 383 383 ASP ASP A . n 
A 1 384 LEU 384 384 384 LEU LEU A . n 
A 1 385 SER 385 385 385 SER SER A . n 
A 1 386 THR 386 386 386 THR THR A . n 
A 1 387 LYS 387 387 387 LYS LYS A . n 
A 1 388 TYR 388 388 388 TYR TYR A . n 
A 1 389 ASP 389 389 389 ASP ASP A . n 
A 1 390 ALA 390 390 390 ALA ALA A . n 
A 1 391 PRO 391 391 391 PRO PRO A . n 
A 1 392 PHE 392 392 392 PHE PHE A . n 
A 1 393 VAL 393 393 393 VAL VAL A . n 
A 1 394 PHE 394 394 394 PHE PHE A . n 
A 1 395 ALA 395 395 395 ALA ALA A . n 
A 1 396 GLU 396 396 396 GLU GLU A . n 
A 1 397 VAL 397 397 397 VAL VAL A . n 
A 1 398 ASN 398 398 398 ASN ASN A . n 
A 1 399 ALA 399 399 399 ALA ALA A . n 
A 1 400 ASP 400 400 400 ASP ASP A . n 
A 1 401 VAL 401 401 401 VAL VAL A . n 
A 1 402 VAL 402 402 402 VAL VAL A . n 
A 1 403 ASP 403 403 403 ASP ASP A . n 
A 1 404 TRP 404 404 404 TRP TRP A . n 
A 1 405 ILE 405 405 405 ILE ILE A . n 
A 1 406 GLN 406 406 406 GLN GLN A . n 
A 1 407 GLN 407 407 ?   ?   ?   A . n 
A 1 408 ASP 408 408 ?   ?   ?   A . n 
A 1 409 ASP 409 409 ?   ?   ?   A . n 
A 1 410 GLY 410 410 ?   ?   ?   A . n 
A 1 411 SER 411 411 ?   ?   ?   A . n 
A 1 412 VAL 412 412 ?   ?   ?   A . n 
A 1 413 HIS 413 413 ?   ?   ?   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 ILE 416 416 416 ILE ILE A . n 
A 1 417 ASN 417 417 417 ASN ASN A . n 
A 1 418 ARG 418 418 418 ARG ARG A . n 
A 1 419 SER 419 419 419 SER SER A . n 
A 1 420 LEU 420 420 420 LEU LEU A . n 
A 1 421 ILE 421 421 421 ILE ILE A . n 
A 1 422 VAL 422 422 422 VAL VAL A . n 
A 1 423 GLY 423 423 423 GLY GLY A . n 
A 1 424 LEU 424 424 424 LEU LEU A . n 
A 1 425 LYS 425 425 425 LYS LYS A . n 
A 1 426 ILE 426 426 426 ILE ILE A . n 
A 1 427 SER 427 427 427 SER SER A . n 
A 1 428 THR 428 428 428 THR THR A . n 
A 1 429 LYS 429 429 429 LYS LYS A . n 
A 1 430 SER 430 430 430 SER SER A . n 
A 1 431 VAL 431 431 431 VAL VAL A . n 
A 1 432 GLY 432 432 432 GLY GLY A . n 
A 1 433 ARG 433 433 433 ARG ARG A . n 
A 1 434 ASP 434 434 434 ASP ASP A . n 
A 1 435 GLU 435 435 435 GLU GLU A . n 
A 1 436 ARG 436 436 436 ARG ARG A . n 
A 1 437 GLU 437 437 437 GLU GLU A . n 
A 1 438 ASP 438 438 438 ASP ASP A . n 
A 1 439 ILE 439 439 439 ILE ILE A . n 
A 1 440 THR 440 440 440 THR THR A . n 
A 1 441 HIS 441 441 441 HIS HIS A . n 
A 1 442 THR 442 442 442 THR THR A . n 
A 1 443 TYR 443 443 443 TYR TYR A . n 
A 1 444 LYS 444 444 444 LYS LYS A . n 
A 1 445 TYR 445 445 445 TYR TYR A . n 
A 1 446 PRO 446 446 446 PRO PRO A . n 
A 1 447 GLU 447 447 447 GLU GLU A . n 
A 1 448 GLY 448 448 448 GLY GLY A . n 
A 1 449 SER 449 449 449 SER SER A . n 
A 1 450 SER 450 450 450 SER SER A . n 
A 1 451 GLU 451 451 451 GLU GLU A . n 
A 1 452 GLU 452 452 452 GLU GLU A . n 
A 1 453 ARG 453 453 453 ARG ARG A . n 
A 1 454 GLU 454 454 454 GLU GLU A . n 
A 1 455 ALA 455 455 455 ALA ALA A . n 
A 1 456 PHE 456 456 456 PHE PHE A . n 
A 1 457 THR 457 457 457 THR THR A . n 
A 1 458 ARG 458 458 458 ARG ARG A . n 
A 1 459 ALA 459 459 459 ALA ALA A . n 
A 1 460 ASN 460 460 460 ASN ASN A . n 
A 1 461 HIS 461 461 461 HIS HIS A . n 
A 1 462 LEU 462 462 ?   ?   ?   A . n 
A 1 463 ASN 463 463 ?   ?   ?   A . n 
A 1 464 LYS 464 464 ?   ?   ?   A . n 
A 1 465 LEU 465 465 ?   ?   ?   A . n 
A 1 466 ALA 466 466 ?   ?   ?   A . n 
A 1 467 GLU 467 467 ?   ?   ?   A . n 
A 1 468 LYS 468 468 ?   ?   ?   A . n 
A 1 469 GLU 469 469 ?   ?   ?   A . n 
A 1 470 GLU 470 470 ?   ?   ?   A . n 
A 1 471 THR 471 471 ?   ?   ?   A . n 
A 1 472 GLY 472 472 472 GLY GLY A . n 
A 1 473 MET 473 473 473 MET MET A . n 
A 1 474 ALA 474 474 474 ALA ALA A . n 
A 1 475 MET 475 475 475 MET MET A . n 
A 1 476 ARG 476 476 476 ARG ARG A . n 
A 1 477 ILE 477 477 477 ILE ILE A . n 
A 1 478 ARG 478 478 478 ARG ARG A . n 
A 1 479 VAL 479 479 479 VAL VAL A . n 
A 1 480 GLY 480 480 480 GLY GLY A . n 
A 1 481 GLN 481 481 481 GLN GLN A . n 
A 1 482 SER 482 482 482 SER SER A . n 
A 1 483 MET 483 483 483 MET MET A . n 
A 1 484 ASN 484 484 484 ASN ASN A . n 
A 1 485 MET 485 485 485 MET MET A . n 
A 1 486 GLY 486 486 486 GLY GLY A . n 
A 1 487 SER 487 487 487 SER SER A . n 
A 1 488 ASP 488 488 488 ASP ASP A . n 
A 1 489 PHE 489 489 489 PHE PHE A . n 
A 1 490 ASP 490 490 490 ASP ASP A . n 
A 1 491 VAL 491 491 491 VAL VAL A . n 
A 1 492 PHE 492 492 492 PHE PHE A . n 
A 1 493 ALA 493 493 493 ALA ALA A . n 
A 1 494 HIS 494 494 494 HIS HIS A . n 
A 1 495 ILE 495 495 495 ILE ILE A . n 
A 1 496 THR 496 496 496 THR THR A . n 
A 1 497 ASN 497 497 497 ASN ASN A . n 
A 1 498 ASN 498 498 498 ASN ASN A . n 
A 1 499 THR 499 499 499 THR THR A . n 
A 1 500 ALA 500 500 500 ALA ALA A . n 
A 1 501 GLU 501 501 501 GLU GLU A . n 
A 1 502 GLU 502 502 502 GLU GLU A . n 
A 1 503 TYR 503 503 503 TYR TYR A . n 
A 1 504 VAL 504 504 504 VAL VAL A . n 
A 1 505 CYS 505 505 505 CYS CYS A . n 
A 1 506 ARG 506 506 506 ARG ARG A . n 
A 1 507 LEU 507 507 507 LEU LEU A . n 
A 1 508 LEU 508 508 508 LEU LEU A . n 
A 1 509 LEU 509 509 509 LEU LEU A . n 
A 1 510 CYS 510 510 510 CYS CYS A . n 
A 1 511 ALA 511 511 511 ALA ALA A . n 
A 1 512 ARG 512 512 512 ARG ARG A . n 
A 1 513 THR 513 513 513 THR THR A . n 
A 1 514 VAL 514 514 514 VAL VAL A . n 
A 1 515 SER 515 515 515 SER SER A . n 
A 1 516 TYR 516 516 516 TYR TYR A . n 
A 1 517 ASN 517 517 517 ASN ASN A . n 
A 1 518 GLY 518 518 518 GLY GLY A . n 
A 1 519 ILE 519 519 519 ILE ILE A . n 
A 1 520 LEU 520 520 520 LEU LEU A . n 
A 1 521 GLY 521 521 521 GLY GLY A . n 
A 1 522 PRO 522 522 522 PRO PRO A . n 
A 1 523 GLU 523 523 523 GLU GLU A . n 
A 1 524 CYS 524 524 524 CYS CYS A . n 
A 1 525 GLY 525 525 525 GLY GLY A . n 
A 1 526 THR 526 526 526 THR THR A . n 
A 1 527 LYS 527 527 527 LYS LYS A . n 
A 1 528 TYR 528 528 528 TYR TYR A . n 
A 1 529 LEU 529 529 529 LEU LEU A . n 
A 1 530 LEU 530 530 530 LEU LEU A . n 
A 1 531 ASN 531 531 531 ASN ASN A . n 
A 1 532 LEU 532 532 532 LEU LEU A . n 
A 1 533 THR 533 533 533 THR THR A . n 
A 1 534 LEU 534 534 534 LEU LEU A . n 
A 1 535 GLU 535 535 535 GLU GLU A . n 
A 1 536 PRO 536 536 536 PRO PRO A . n 
A 1 537 PHE 537 537 537 PHE PHE A . n 
A 1 538 SER 538 538 538 SER SER A . n 
A 1 539 GLU 539 539 539 GLU GLU A . n 
A 1 540 LYS 540 540 540 LYS LYS A . n 
A 1 541 SER 541 541 541 SER SER A . n 
A 1 542 VAL 542 542 542 VAL VAL A . n 
A 1 543 PRO 543 543 543 PRO PRO A . n 
A 1 544 LEU 544 544 544 LEU LEU A . n 
A 1 545 CYS 545 545 545 CYS CYS A . n 
A 1 546 ILE 546 546 546 ILE ILE A . n 
A 1 547 LEU 547 547 547 LEU LEU A . n 
A 1 548 TYR 548 548 548 TYR TYR 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 TYR 551 551 551 TYR TYR A . n 
A 1 552 ARG 552 552 552 ARG ARG A . n 
A 1 553 ASP 553 553 553 ASP ASP A . n 
A 1 554 CYS 554 554 554 CYS CYS A . n 
A 1 555 LEU 555 555 555 LEU LEU A . n 
A 1 556 THR 556 556 556 THR THR A . n 
A 1 557 GLU 557 557 557 GLU GLU A . n 
A 1 558 SER 558 558 558 SER SER A . n 
A 1 559 ASN 559 559 559 ASN ASN A . n 
A 1 560 LEU 560 560 560 LEU LEU A . n 
A 1 561 ILE 561 561 561 ILE ILE A . n 
A 1 562 LYS 562 562 562 LYS LYS A . n 
A 1 563 VAL 563 563 563 VAL VAL A . n 
A 1 564 ARG 564 564 564 ARG ARG A . n 
A 1 565 ALA 565 565 565 ALA ALA A . n 
A 1 566 LEU 566 566 566 LEU LEU A . n 
A 1 567 LEU 567 567 567 LEU LEU A . n 
A 1 568 VAL 568 568 568 VAL VAL A . n 
A 1 569 GLU 569 569 569 GLU GLU A . n 
A 1 570 PRO 570 570 570 PRO PRO A . n 
A 1 571 VAL 571 571 571 VAL VAL A . n 
A 1 572 ILE 572 572 572 ILE ILE A . n 
A 1 573 ASN 573 573 573 ASN ASN A . n 
A 1 574 SER 574 574 574 SER SER A . n 
A 1 575 TYR 575 575 575 TYR TYR A . n 
A 1 576 LEU 576 576 576 LEU LEU A . n 
A 1 577 LEU 577 577 577 LEU LEU A . n 
A 1 578 ALA 578 578 578 ALA ALA A . n 
A 1 579 GLU 579 579 579 GLU GLU A . n 
A 1 580 ARG 580 580 580 ARG ARG A . n 
A 1 581 ASP 581 581 581 ASP ASP A . n 
A 1 582 LEU 582 582 582 LEU LEU A . n 
A 1 583 TYR 583 583 583 TYR TYR A . n 
A 1 584 LEU 584 584 584 LEU LEU A . n 
A 1 585 GLU 585 585 585 GLU GLU A . n 
A 1 586 ASN 586 586 586 ASN ASN A . n 
A 1 587 PRO 587 587 587 PRO PRO A . n 
A 1 588 GLU 588 588 588 GLU GLU A . n 
A 1 589 ILE 589 589 589 ILE ILE A . n 
A 1 590 LYS 590 590 590 LYS LYS A . n 
A 1 591 ILE 591 591 591 ILE ILE A . n 
A 1 592 ARG 592 592 592 ARG ARG A . n 
A 1 593 ILE 593 593 593 ILE ILE A . n 
A 1 594 LEU 594 594 594 LEU LEU A . n 
A 1 595 GLY 595 595 595 GLY GLY A . n 
A 1 596 GLU 596 596 596 GLU GLU A . n 
A 1 597 PRO 597 597 597 PRO PRO A . n 
A 1 598 LYS 598 598 598 LYS LYS A . n 
A 1 599 GLN 599 599 599 GLN GLN A . n 
A 1 600 LYS 600 600 600 LYS LYS A . n 
A 1 601 ARG 601 601 601 ARG ARG A . n 
A 1 602 LYS 602 602 602 LYS LYS A . n 
A 1 603 LEU 603 603 603 LEU LEU A . n 
A 1 604 VAL 604 604 604 VAL VAL A . n 
A 1 605 ALA 605 605 605 ALA ALA A . n 
A 1 606 GLU 606 606 606 GLU GLU A . n 
A 1 607 VAL 607 607 607 VAL VAL A . n 
A 1 608 SER 608 608 608 SER SER A . n 
A 1 609 LEU 609 609 609 LEU LEU A . n 
A 1 610 GLN 610 610 610 GLN GLN A . n 
A 1 611 ASN 611 611 611 ASN ASN A . n 
A 1 612 PRO 612 612 612 PRO PRO A . n 
A 1 613 LEU 613 613 613 LEU LEU A . n 
A 1 614 PRO 614 614 614 PRO PRO A . n 
A 1 615 VAL 615 615 615 VAL VAL A . n 
A 1 616 ALA 616 616 616 ALA ALA A . n 
A 1 617 LEU 617 617 617 LEU LEU A . n 
A 1 618 GLU 618 618 618 GLU GLU A . n 
A 1 619 GLY 619 619 619 GLY GLY A . n 
A 1 620 CYS 620 620 620 CYS CYS A . n 
A 1 621 THR 621 621 621 THR THR A . n 
A 1 622 PHE 622 622 622 PHE PHE A . n 
A 1 623 THR 623 623 623 THR THR A . n 
A 1 624 VAL 624 624 624 VAL VAL A . n 
A 1 625 GLU 625 625 625 GLU GLU A . n 
A 1 626 GLY 626 626 626 GLY GLY A . n 
A 1 627 ALA 627 627 627 ALA ALA A . n 
A 1 628 GLY 628 628 628 GLY GLY A . n 
A 1 629 LEU 629 629 629 LEU LEU A . n 
A 1 630 THR 630 630 630 THR THR A . n 
A 1 631 GLU 631 631 631 GLU GLU A . n 
A 1 632 GLU 632 632 632 GLU GLU A . n 
A 1 633 GLN 633 633 633 GLN GLN A . n 
A 1 634 LYS 634 634 634 LYS LYS A . n 
A 1 635 THR 635 635 635 THR THR A . n 
A 1 636 VAL 636 636 636 VAL VAL A . n 
A 1 637 GLU 637 637 637 GLU GLU A . n 
A 1 638 ILE 638 638 638 ILE ILE A . n 
A 1 639 PRO 639 639 639 PRO PRO A . n 
A 1 640 ASP 640 640 640 ASP ASP A . n 
A 1 641 PRO 641 641 641 PRO PRO A . n 
A 1 642 VAL 642 642 642 VAL VAL A . n 
A 1 643 GLU 643 643 643 GLU GLU A . n 
A 1 644 ALA 644 644 644 ALA ALA A . n 
A 1 645 GLY 645 645 645 GLY GLY A . n 
A 1 646 GLU 646 646 646 GLU GLU A . n 
A 1 647 GLU 647 647 647 GLU GLU A . n 
A 1 648 VAL 648 648 648 VAL VAL A . n 
A 1 649 LYS 649 649 649 LYS LYS A . n 
A 1 650 VAL 650 650 650 VAL VAL A . n 
A 1 651 ARG 651 651 651 ARG ARG A . n 
A 1 652 MET 652 652 652 MET MET A . n 
A 1 653 ASP 653 653 653 ASP ASP 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 PRO 656 656 656 PRO PRO A . n 
A 1 657 LEU 657 657 657 LEU LEU A . n 
A 1 658 HIS 658 658 658 HIS HIS A . n 
A 1 659 MET 659 659 659 MET MET A . n 
A 1 660 GLY 660 660 660 GLY GLY A . n 
A 1 661 LEU 661 661 661 LEU LEU A . n 
A 1 662 HIS 662 662 662 HIS HIS A . n 
A 1 663 LYS 663 663 663 LYS LYS A . n 
A 1 664 LEU 664 664 664 LEU LEU A . n 
A 1 665 VAL 665 665 665 VAL VAL A . n 
A 1 666 VAL 666 666 666 VAL VAL A . n 
A 1 667 ASN 667 667 667 ASN ASN A . n 
A 1 668 PHE 668 668 668 PHE PHE A . n 
A 1 669 GLU 669 669 669 GLU GLU A . n 
A 1 670 SER 670 670 670 SER SER A . n 
A 1 671 ASP 671 671 671 ASP ASP A . n 
A 1 672 LYS 672 672 672 LYS LYS A . n 
A 1 673 LEU 673 673 673 LEU LEU A . n 
A 1 674 LYS 674 674 674 LYS LYS A . n 
A 1 675 ALA 675 675 675 ALA ALA A . n 
A 1 676 VAL 676 676 676 VAL VAL A . n 
A 1 677 LYS 677 677 677 LYS LYS A . n 
A 1 678 GLY 678 678 678 GLY GLY A . n 
A 1 679 PHE 679 679 679 PHE PHE A . n 
A 1 680 ARG 680 680 680 ARG ARG A . n 
A 1 681 ASN 681 681 681 ASN ASN A . n 
A 1 682 VAL 682 682 682 VAL VAL A . n 
A 1 683 ILE 683 683 683 ILE ILE A . n 
A 1 684 ILE 684 684 ?   ?   ?   A . n 
A 1 685 GLY 685 685 ?   ?   ?   A . n 
A 1 686 PRO 686 686 ?   ?   ?   A . n 
A 1 687 ALA 687 687 ?   ?   ?   A . n 
B 2 1   ACE 1   1   1   ACE ACE X . n 
B 2 2   PRO 2   2   2   PRO PRO X . n 
B 2 3   ONL 3   3   3   ONL ONL X . n 
B 2 4   LEU 4   4   4   LEU LEU X . n 
B 2 5   PRO 5   5   5   PRO PRO X . n 
B 2 6   PHE 6   6   6   PHE PHE X . n 
B 2 7   NH2 7   7   7   NH2 NH2 X . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 SO4 1   688 301 SO4 SO4 A . 
D 3 SO4 1   689 302 SO4 SO4 A . 
E 3 SO4 1   690 303 SO4 SO4 A . 
F 3 SO4 1   691 304 SO4 SO4 A . 
G 3 SO4 1   692 305 SO4 SO4 A . 
H 4 HOH 1   693 1   HOH HOH A . 
H 4 HOH 2   694 2   HOH HOH A . 
H 4 HOH 3   695 3   HOH HOH A . 
H 4 HOH 4   696 4   HOH HOH A . 
H 4 HOH 5   697 5   HOH HOH A . 
H 4 HOH 6   698 6   HOH HOH A . 
H 4 HOH 7   699 7   HOH HOH A . 
H 4 HOH 8   700 8   HOH HOH A . 
H 4 HOH 9   701 9   HOH HOH A . 
H 4 HOH 10  702 10  HOH HOH A . 
H 4 HOH 11  703 11  HOH HOH A . 
H 4 HOH 12  704 12  HOH HOH A . 
H 4 HOH 13  705 13  HOH HOH A . 
H 4 HOH 14  706 14  HOH HOH A . 
H 4 HOH 15  707 15  HOH HOH A . 
H 4 HOH 16  708 16  HOH HOH A . 
H 4 HOH 17  709 17  HOH HOH A . 
H 4 HOH 18  710 18  HOH HOH A . 
H 4 HOH 19  711 19  HOH HOH A . 
H 4 HOH 20  712 20  HOH HOH A . 
H 4 HOH 21  713 21  HOH HOH A . 
H 4 HOH 22  714 22  HOH HOH A . 
H 4 HOH 23  715 23  HOH HOH A . 
H 4 HOH 24  716 24  HOH HOH A . 
H 4 HOH 25  717 25  HOH HOH A . 
H 4 HOH 26  718 26  HOH HOH A . 
H 4 HOH 27  719 27  HOH HOH A . 
H 4 HOH 28  720 28  HOH HOH A . 
H 4 HOH 29  721 29  HOH HOH A . 
H 4 HOH 30  722 30  HOH HOH A . 
H 4 HOH 31  723 31  HOH HOH A . 
H 4 HOH 32  724 32  HOH HOH A . 
H 4 HOH 33  725 33  HOH HOH A . 
H 4 HOH 34  726 34  HOH HOH A . 
H 4 HOH 35  727 35  HOH HOH A . 
H 4 HOH 36  728 36  HOH HOH A . 
H 4 HOH 37  729 37  HOH HOH A . 
H 4 HOH 38  730 38  HOH HOH A . 
H 4 HOH 39  731 39  HOH HOH A . 
H 4 HOH 40  732 40  HOH HOH A . 
H 4 HOH 41  733 41  HOH HOH A . 
H 4 HOH 42  734 42  HOH HOH A . 
H 4 HOH 43  735 43  HOH HOH A . 
H 4 HOH 44  736 44  HOH HOH A . 
H 4 HOH 45  737 45  HOH HOH A . 
H 4 HOH 46  738 46  HOH HOH A . 
H 4 HOH 47  739 47  HOH HOH A . 
H 4 HOH 48  740 48  HOH HOH A . 
H 4 HOH 49  741 49  HOH HOH A . 
H 4 HOH 50  742 50  HOH HOH A . 
H 4 HOH 51  743 51  HOH HOH A . 
H 4 HOH 52  744 52  HOH HOH A . 
H 4 HOH 53  745 53  HOH HOH A . 
H 4 HOH 54  746 54  HOH HOH A . 
H 4 HOH 55  747 55  HOH HOH A . 
H 4 HOH 56  748 56  HOH HOH A . 
H 4 HOH 57  749 57  HOH HOH A . 
H 4 HOH 58  750 58  HOH HOH A . 
H 4 HOH 59  751 59  HOH HOH A . 
H 4 HOH 60  752 60  HOH HOH A . 
H 4 HOH 61  753 61  HOH HOH A . 
H 4 HOH 62  754 62  HOH HOH A . 
H 4 HOH 63  755 63  HOH HOH A . 
H 4 HOH 64  756 64  HOH HOH A . 
H 4 HOH 65  757 65  HOH HOH A . 
H 4 HOH 66  758 66  HOH HOH A . 
H 4 HOH 67  759 67  HOH HOH A . 
H 4 HOH 68  760 68  HOH HOH A . 
H 4 HOH 69  761 69  HOH HOH A . 
H 4 HOH 70  762 70  HOH HOH A . 
H 4 HOH 71  763 71  HOH HOH A . 
H 4 HOH 72  764 72  HOH HOH A . 
H 4 HOH 73  765 73  HOH HOH A . 
H 4 HOH 74  766 74  HOH HOH A . 
H 4 HOH 75  767 75  HOH HOH A . 
H 4 HOH 76  768 76  HOH HOH A . 
H 4 HOH 77  769 77  HOH HOH A . 
H 4 HOH 78  770 78  HOH HOH A . 
H 4 HOH 79  771 79  HOH HOH A . 
H 4 HOH 80  772 80  HOH HOH A . 
H 4 HOH 81  773 81  HOH HOH A . 
H 4 HOH 82  774 82  HOH HOH A . 
H 4 HOH 83  775 83  HOH HOH A . 
H 4 HOH 84  776 84  HOH HOH A . 
H 4 HOH 85  777 85  HOH HOH A . 
H 4 HOH 86  778 86  HOH HOH A . 
H 4 HOH 87  779 87  HOH HOH A . 
H 4 HOH 88  780 88  HOH HOH A . 
H 4 HOH 89  781 89  HOH HOH A . 
H 4 HOH 90  782 90  HOH HOH A . 
H 4 HOH 91  783 91  HOH HOH A . 
H 4 HOH 92  784 93  HOH HOH A . 
H 4 HOH 93  785 94  HOH HOH A . 
H 4 HOH 94  786 95  HOH HOH A . 
H 4 HOH 95  787 96  HOH HOH A . 
H 4 HOH 96  788 97  HOH HOH A . 
H 4 HOH 97  789 98  HOH HOH A . 
H 4 HOH 98  790 99  HOH HOH A . 
H 4 HOH 99  791 100 HOH HOH A . 
H 4 HOH 100 792 101 HOH HOH A . 
H 4 HOH 101 793 102 HOH HOH A . 
H 4 HOH 102 794 103 HOH HOH A . 
H 4 HOH 103 795 104 HOH HOH A . 
H 4 HOH 104 796 105 HOH HOH A . 
H 4 HOH 105 797 106 HOH HOH A . 
H 4 HOH 106 798 107 HOH HOH A . 
H 4 HOH 107 799 108 HOH HOH A . 
H 4 HOH 108 800 109 HOH HOH A . 
H 4 HOH 109 801 110 HOH HOH A . 
H 4 HOH 110 802 111 HOH HOH A . 
H 4 HOH 111 803 112 HOH HOH A . 
H 4 HOH 112 804 113 HOH HOH A . 
H 4 HOH 113 805 114 HOH HOH A . 
H 4 HOH 114 806 115 HOH HOH A . 
H 4 HOH 115 807 116 HOH HOH A . 
H 4 HOH 116 808 117 HOH HOH A . 
H 4 HOH 117 809 118 HOH HOH A . 
H 4 HOH 118 810 119 HOH HOH A . 
H 4 HOH 119 811 120 HOH HOH A . 
H 4 HOH 120 812 121 HOH HOH A . 
H 4 HOH 121 813 122 HOH HOH A . 
H 4 HOH 122 814 123 HOH HOH A . 
H 4 HOH 123 815 124 HOH HOH A . 
H 4 HOH 124 816 125 HOH HOH A . 
H 4 HOH 125 817 126 HOH HOH A . 
H 4 HOH 126 818 127 HOH HOH A . 
H 4 HOH 127 819 128 HOH HOH A . 
H 4 HOH 128 820 129 HOH HOH A . 
H 4 HOH 129 821 130 HOH HOH A . 
H 4 HOH 130 822 131 HOH HOH A . 
H 4 HOH 131 823 132 HOH HOH A . 
H 4 HOH 132 824 133 HOH HOH A . 
H 4 HOH 133 825 135 HOH HOH A . 
H 4 HOH 134 826 136 HOH HOH A . 
H 4 HOH 135 827 137 HOH HOH A . 
H 4 HOH 136 828 138 HOH HOH A . 
H 4 HOH 137 829 141 HOH HOH A . 
H 4 HOH 138 830 142 HOH HOH A . 
H 4 HOH 139 831 143 HOH HOH A . 
H 4 HOH 140 832 144 HOH HOH A . 
H 4 HOH 141 833 145 HOH HOH A . 
H 4 HOH 142 834 146 HOH HOH A . 
H 4 HOH 143 835 151 HOH HOH A . 
H 4 HOH 144 836 153 HOH HOH A . 
H 4 HOH 145 837 154 HOH HOH A . 
H 4 HOH 146 838 155 HOH HOH A . 
H 4 HOH 147 839 156 HOH HOH A . 
H 4 HOH 148 840 157 HOH HOH A . 
H 4 HOH 149 841 158 HOH HOH A . 
H 4 HOH 150 842 160 HOH HOH A . 
H 4 HOH 151 843 161 HOH HOH A . 
H 4 HOH 152 844 162 HOH HOH A . 
H 4 HOH 153 845 163 HOH HOH A . 
H 4 HOH 154 846 164 HOH HOH A . 
H 4 HOH 155 847 165 HOH HOH A . 
H 4 HOH 156 848 166 HOH HOH A . 
H 4 HOH 157 849 167 HOH HOH A . 
H 4 HOH 158 850 168 HOH HOH A . 
H 4 HOH 159 851 169 HOH HOH A . 
H 4 HOH 160 852 170 HOH HOH A . 
H 4 HOH 161 853 171 HOH HOH A . 
H 4 HOH 162 854 172 HOH HOH A . 
H 4 HOH 163 855 173 HOH HOH A . 
H 4 HOH 164 856 174 HOH HOH A . 
H 4 HOH 165 857 175 HOH HOH A . 
H 4 HOH 166 858 176 HOH HOH A . 
H 4 HOH 167 859 177 HOH HOH A . 
H 4 HOH 168 860 178 HOH HOH A . 
H 4 HOH 169 861 179 HOH HOH A . 
H 4 HOH 170 862 180 HOH HOH A . 
H 4 HOH 171 863 181 HOH HOH A . 
H 4 HOH 172 864 182 HOH HOH A . 
H 4 HOH 173 865 183 HOH HOH A . 
H 4 HOH 174 866 184 HOH HOH A . 
H 4 HOH 175 867 185 HOH HOH A . 
H 4 HOH 176 868 186 HOH HOH A . 
H 4 HOH 177 869 187 HOH HOH A . 
H 4 HOH 178 870 188 HOH HOH A . 
H 4 HOH 179 871 189 HOH HOH A . 
H 4 HOH 180 872 190 HOH HOH A . 
H 4 HOH 181 873 192 HOH HOH A . 
H 4 HOH 182 874 194 HOH HOH A . 
H 4 HOH 183 875 195 HOH HOH A . 
H 4 HOH 184 876 196 HOH HOH A . 
H 4 HOH 185 877 197 HOH HOH A . 
H 4 HOH 186 878 198 HOH HOH A . 
H 4 HOH 187 879 199 HOH HOH A . 
H 4 HOH 188 880 200 HOH HOH A . 
H 4 HOH 189 881 201 HOH HOH A . 
H 4 HOH 190 882 202 HOH HOH A . 
H 4 HOH 191 883 203 HOH HOH A . 
H 4 HOH 192 884 204 HOH HOH A . 
H 4 HOH 193 885 205 HOH HOH A . 
H 4 HOH 194 886 206 HOH HOH A . 
H 4 HOH 195 887 207 HOH HOH A . 
H 4 HOH 196 888 208 HOH HOH A . 
H 4 HOH 197 889 209 HOH HOH A . 
H 4 HOH 198 890 210 HOH HOH A . 
H 4 HOH 199 891 211 HOH HOH A . 
H 4 HOH 200 892 212 HOH HOH A . 
H 4 HOH 201 893 213 HOH HOH A . 
H 4 HOH 202 894 214 HOH HOH A . 
H 4 HOH 203 895 215 HOH HOH A . 
H 4 HOH 204 896 216 HOH HOH A . 
H 4 HOH 205 897 217 HOH HOH A . 
H 4 HOH 206 898 218 HOH HOH A . 
H 4 HOH 207 899 219 HOH HOH A . 
H 4 HOH 208 900 220 HOH HOH A . 
H 4 HOH 209 901 221 HOH HOH A . 
H 4 HOH 210 902 222 HOH HOH A . 
H 4 HOH 211 903 223 HOH HOH A . 
H 4 HOH 212 904 227 HOH HOH A . 
H 4 HOH 213 905 228 HOH HOH A . 
H 4 HOH 214 906 229 HOH HOH A . 
H 4 HOH 215 907 230 HOH HOH A . 
H 4 HOH 216 908 231 HOH HOH A . 
H 4 HOH 217 909 232 HOH HOH A . 
H 4 HOH 218 910 233 HOH HOH A . 
H 4 HOH 219 911 234 HOH HOH A . 
H 4 HOH 220 912 235 HOH HOH A . 
H 4 HOH 221 913 236 HOH HOH A . 
H 4 HOH 222 914 237 HOH HOH A . 
H 4 HOH 223 915 238 HOH HOH A . 
H 4 HOH 224 916 239 HOH HOH A . 
H 4 HOH 225 917 240 HOH HOH A . 
H 4 HOH 226 918 241 HOH HOH A . 
H 4 HOH 227 919 242 HOH HOH A . 
H 4 HOH 228 920 243 HOH HOH A . 
H 4 HOH 229 921 244 HOH HOH A . 
H 4 HOH 230 922 245 HOH HOH A . 
H 4 HOH 231 923 246 HOH HOH A . 
H 4 HOH 232 924 247 HOH HOH A . 
H 4 HOH 233 925 248 HOH HOH A . 
H 4 HOH 234 926 249 HOH HOH A . 
H 4 HOH 235 927 250 HOH HOH A . 
H 4 HOH 236 928 251 HOH HOH A . 
H 4 HOH 237 929 252 HOH HOH A . 
H 4 HOH 238 930 253 HOH HOH A . 
H 4 HOH 239 931 254 HOH HOH A . 
H 4 HOH 240 932 255 HOH HOH A . 
H 4 HOH 241 933 256 HOH HOH A . 
H 4 HOH 242 934 257 HOH HOH A . 
H 4 HOH 243 935 258 HOH HOH A . 
H 4 HOH 244 936 259 HOH HOH A . 
H 4 HOH 245 937 260 HOH HOH A . 
H 4 HOH 246 938 261 HOH HOH A . 
H 4 HOH 247 939 262 HOH HOH A . 
H 4 HOH 248 940 263 HOH HOH A . 
H 4 HOH 249 941 264 HOH HOH A . 
H 4 HOH 250 942 265 HOH HOH A . 
H 4 HOH 251 943 266 HOH HOH A . 
H 4 HOH 252 944 267 HOH HOH A . 
H 4 HOH 253 945 268 HOH HOH A . 
H 4 HOH 254 946 269 HOH HOH A . 
H 4 HOH 255 947 270 HOH HOH A . 
H 4 HOH 256 948 271 HOH HOH A . 
H 4 HOH 257 949 272 HOH HOH A . 
H 4 HOH 258 950 273 HOH HOH A . 
H 4 HOH 259 951 274 HOH HOH A . 
H 4 HOH 260 952 275 HOH HOH A . 
H 4 HOH 261 953 276 HOH HOH A . 
H 4 HOH 262 954 277 HOH HOH A . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA,PQS dimeric    2 
2 software_defined_assembly            PISA     tetrameric 4 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1   A,B,C,D,E,F,G,H 
2 1,2 A,B,C,D,E,F,G,H 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2180  ? 
1 MORE         -68   ? 
1 'SSA (A^2)'  30630 ? 
2 'ABSA (A^2)' 9600  ? 
2 MORE         -160  ? 
2 'SSA (A^2)'  56010 ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z  1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 7_555 y,x,-z 0.0000000000 1.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2007-10-23 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2017-10-18 
4 'Structure model' 1 3 2018-02-14 
5 'Structure model' 1 4 2023-08-30 
6 'Structure model' 1 5 2023-11-15 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1  2 'Structure model' Advisory                    
2  2 'Structure model' 'Derived calculations'      
3  2 'Structure model' 'Version format compliance' 
4  3 'Structure model' Advisory                    
5  3 'Structure model' 'Refinement description'    
6  4 'Structure model' 'Experimental preparation'  
7  5 'Structure model' Advisory                    
8  5 'Structure model' 'Data collection'           
9  5 'Structure model' 'Database references'       
10 5 'Structure model' 'Derived calculations'      
11 5 'Structure model' 'Refinement description'    
12 6 'Structure model' 'Data collection'           
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1  3 'Structure model' pdbx_unobs_or_zero_occ_atoms  
2  3 'Structure model' software                      
3  4 'Structure model' exptl_crystal_grow            
4  5 'Structure model' chem_comp_atom                
5  5 'Structure model' chem_comp_bond                
6  5 'Structure model' database_2                    
7  5 'Structure model' pdbx_initial_refinement_model 
8  5 'Structure model' pdbx_unobs_or_zero_occ_atoms  
9  5 'Structure model' struct_conn                   
10 5 'Structure model' struct_ref_seq_dif            
11 5 'Structure model' struct_site                   
12 6 'Structure model' chem_comp_atom                
13 6 'Structure model' chem_comp_bond                
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  4 'Structure model' '_exptl_crystal_grow.pdbx_details'    
2  4 'Structure model' '_exptl_crystal_grow.temp'            
3  5 'Structure model' '_database_2.pdbx_DOI'                
4  5 'Structure model' '_database_2.pdbx_database_accession' 
5  5 'Structure model' '_struct_conn.pdbx_dist_value'        
6  5 'Structure model' '_struct_conn.pdbx_leaving_atom_flag' 
7  5 'Structure model' '_struct_conn.ptnr1_auth_asym_id'     
8  5 'Structure model' '_struct_conn.ptnr1_auth_comp_id'     
9  5 'Structure model' '_struct_conn.ptnr1_auth_seq_id'      
10 5 'Structure model' '_struct_conn.ptnr1_label_asym_id'    
11 5 'Structure model' '_struct_conn.ptnr1_label_atom_id'    
12 5 'Structure model' '_struct_conn.ptnr1_label_comp_id'    
13 5 'Structure model' '_struct_conn.ptnr1_label_seq_id'     
14 5 'Structure model' '_struct_conn.ptnr2_auth_comp_id'     
15 5 'Structure model' '_struct_conn.ptnr2_auth_seq_id'      
16 5 'Structure model' '_struct_conn.ptnr2_label_atom_id'    
17 5 'Structure model' '_struct_conn.ptnr2_label_comp_id'    
18 5 'Structure model' '_struct_conn.ptnr2_label_seq_id'     
19 5 'Structure model' '_struct_ref_seq_dif.details'         
20 5 'Structure model' '_struct_site.pdbx_auth_asym_id'      
21 5 'Structure model' '_struct_site.pdbx_auth_comp_id'      
22 5 'Structure model' '_struct_site.pdbx_auth_seq_id'       
23 6 'Structure model' '_chem_comp_atom.atom_id'             
24 6 'Structure model' '_chem_comp_bond.atom_id_2'           
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.pdbx_refine_id 
1 ? refined 9.9350  -0.2140  42.7590  -0.1153 -0.3383 -0.2265 -0.0149 -0.0203 0.0000  1.0255 1.0521  4.4242  -0.1156 0.3787 
-0.6471 0.1381  -0.0302 -0.1079 0.0917 -0.0928 0.0395  -0.2095 0.4482  -0.1910 'X-RAY DIFFRACTION' 
2 ? refined 14.5320 -13.9220 -1.8660  0.0607  -0.2398 -0.2056 0.0774  0.0045  0.0484  1.9538 6.0188  8.7493  -0.7329 1.5670 
-0.3107 -0.0725 0.1524  -0.0798 0.1247 0.0971  0.0587  -0.0663 -0.2586 0.0487  'X-RAY DIFFRACTION' 
3 ? refined 7.1070  -19.0930 -38.9520 0.2039  0.0346  0.1565  0.0248  -0.1516 -0.0285 4.6190 13.2923 10.9320 1.3770  1.0017 
-3.4204 0.1757  -0.0190 -0.1567 0.6371 -1.0205 -0.5367 -0.5850 1.1731  -0.2586 'X-RAY DIFFRACTION' 
# 
loop_
_pdbx_refine_tls_group.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.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.selection_details 
1 1 A 1   A 461 ? A 1   A 461 'X-RAY DIFFRACTION' ? 
2 2 A 472 A 586 ? A 472 A 586 'X-RAY DIFFRACTION' ? 
3 3 A 587 A 683 ? A 587 A 683 'X-RAY DIFFRACTION' ? 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
DENZO       .     ?                package 'Zbyszek Otwinowski' zbyszek@mix.swmed.edu    'data reduction'  
http://www.lnls.br/infra/linhasluz/denzo-hkl.htm ?          ? 1 
SCALEPACK   .     ?                package 'Zbyszek Otwinowski' zbyszek@mix.swmed.edu    'data scaling'    
http://www.lnls.br/infra/linhasluz/denzo-hkl.htm ?          ? 2 
REFMAC      .     ?                program 'Murshudov, G.N.'    ccp4@dl.ac.uk            refinement        
http://www.ccp4.ac.uk/main.html                  Fortran_77 ? 3 
PDB_EXTRACT 2.000 'April. 3, 2006' package PDB                  sw-help@rcsb.rutgers.edu 'data extraction' 
http://pdb.rutgers.edu/software/                 C++        ? 4 
Blu-Ice     .     ?                ?       ?                    ?                        'data collection' ? ?          ? 5 
PHASER      .     ?                ?       ?                    ?                        phasing           ? ?          ? 6 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 824 ? ? O A HOH 912 ? ? 2.01 
2 1 O A HOH 810 ? ? O A HOH 912 ? ? 2.12 
3 1 O A HOH 727 ? ? O A HOH 859 ? ? 2.14 
4 1 O A HOH 773 ? ? O A HOH 822 ? ? 2.17 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CG 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_1             329 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_2             329 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.392 
_pdbx_validate_rmsd_bond.bond_target_value         1.515 
_pdbx_validate_rmsd_bond.bond_deviation            -0.123 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.015 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A ASP 97  ? ? CG A ASP 97  ? ? OD1 A ASP 97  ? ? 106.82 118.30 -11.48 0.90 N 
2 1 CB A ASP 97  ? ? CG A ASP 97  ? ? OD2 A ASP 97  ? ? 107.70 118.30 -10.60 0.90 N 
3 1 C  A THR 360 ? ? N  A PRO 361 ? ? CA  A PRO 361 ? ? 129.42 119.30 10.12  1.50 Y 
# 
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 29  ? ? -131.35 -31.87  
2  1 ALA A 66  ? ? -151.57 62.70   
3  1 GLN A 169 ? ? -138.41 -158.87 
4  1 ASN A 206 ? ? -161.70 88.07   
5  1 ARG A 214 ? ? -67.70  4.14    
6  1 ASN A 231 ? ? -39.33  -31.97  
7  1 TRP A 254 ? ? -35.10  135.46  
8  1 ASN A 310 ? ? -35.10  127.57  
9  1 PRO A 361 ? ? -28.50  -74.60  
10 1 GLN A 362 ? ? -69.69  97.88   
11 1 LYS A 364 ? ? -142.91 -43.51  
12 1 VAL A 479 ? ? -128.54 -51.48  
13 1 PHE A 537 ? ? 39.00   51.98   
14 1 GLN A 599 ? ? -76.82  42.15   
15 1 LYS A 600 ? ? -140.20 -82.52  
16 1 ARG A 601 ? ? -119.38 -160.32 
17 1 PRO A 656 ? ? -68.85  -174.24 
18 1 LEU A 657 ? ? -159.11 -35.34  
19 1 LEU A 673 ? ? -155.51 77.34   
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 GLU A 363 ? ? LYS A 364 ? ? -147.69 
2 1 LYS A 600 ? ? ARG A 601 ? ? -146.06 
3 1 MET A 659 ? ? GLY A 660 ? ? -149.45 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ASP 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     97 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.127 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
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 0 A ARG 28  ? CD  ? A ARG 28  CD  
2  1 Y 0 A ARG 28  ? NE  ? A ARG 28  NE  
3  1 Y 0 A ARG 28  ? CZ  ? A ARG 28  CZ  
4  1 Y 0 A ARG 28  ? NH1 ? A ARG 28  NH1 
5  1 Y 0 A ARG 28  ? NH2 ? A ARG 28  NH2 
6  1 Y 0 A GLU 29  ? OE1 ? A GLU 29  OE1 
7  1 Y 0 A GLU 29  ? OE2 ? A GLU 29  OE2 
8  1 Y 0 A LYS 30  ? CE  ? A LYS 30  CE  
9  1 Y 0 A LYS 30  ? NZ  ? A LYS 30  NZ  
10 1 Y 0 A GLU 70  ? CD  ? A GLU 70  CD  
11 1 Y 0 A GLU 70  ? OE1 ? A GLU 70  OE1 
12 1 Y 0 A GLU 70  ? OE2 ? A GLU 70  OE2 
13 1 Y 0 A GLU 85  ? CD  ? A GLU 85  CD  
14 1 Y 0 A GLU 85  ? OE1 ? A GLU 85  OE1 
15 1 Y 0 A GLU 85  ? OE2 ? A GLU 85  OE2 
16 1 Y 0 A ASP 97  ? OD1 ? A ASP 97  OD1 
17 1 Y 0 A ASP 97  ? OD2 ? A ASP 97  OD2 
18 1 Y 0 A ASN 243 ? CG  ? A ASN 243 CG  
19 1 Y 0 A ASN 243 ? OD1 ? A ASN 243 OD1 
20 1 Y 0 A ASN 243 ? ND2 ? A ASN 243 ND2 
21 1 Y 0 A ASP 247 ? C   ? A ASP 247 C   
22 1 Y 0 A ASP 247 ? O   ? A ASP 247 O   
23 1 Y 0 A ARG 317 ? CG  ? A ARG 317 CG  
24 1 Y 0 A ARG 317 ? CD  ? A ARG 317 CD  
25 1 Y 0 A ARG 317 ? NE  ? A ARG 317 NE  
26 1 Y 0 A ARG 317 ? CZ  ? A ARG 317 CZ  
27 1 Y 0 A ARG 317 ? NH1 ? A ARG 317 NH1 
28 1 Y 0 A ARG 317 ? NH2 ? A ARG 317 NH2 
29 1 Y 0 A GLU 329 ? CD  ? A GLU 329 CD  
30 1 Y 0 A GLU 329 ? OE1 ? A GLU 329 OE1 
31 1 Y 0 A GLU 329 ? OE2 ? A GLU 329 OE2 
32 1 Y 0 A LYS 425 ? NZ  ? A LYS 425 NZ  
33 1 Y 0 A ARG 433 ? CZ  ? A ARG 433 CZ  
34 1 Y 0 A ARG 433 ? NH1 ? A ARG 433 NH1 
35 1 Y 0 A ARG 433 ? NH2 ? A ARG 433 NH2 
36 1 Y 0 A LYS 590 ? CD  ? A LYS 590 CD  
37 1 Y 0 A LYS 590 ? CE  ? A LYS 590 CE  
38 1 Y 0 A LYS 590 ? NZ  ? A LYS 590 NZ  
39 1 Y 0 A GLU 596 ? CG  ? A GLU 596 CG  
40 1 Y 0 A GLU 596 ? CD  ? A GLU 596 CD  
41 1 Y 0 A GLU 596 ? OE1 ? A GLU 596 OE1 
42 1 Y 0 A GLU 596 ? OE2 ? A GLU 596 OE2 
43 1 Y 0 A LYS 598 ? CG  ? A LYS 598 CG  
44 1 Y 0 A LYS 598 ? CD  ? A LYS 598 CD  
45 1 Y 0 A LYS 598 ? CE  ? A LYS 598 CE  
46 1 Y 0 A LYS 598 ? NZ  ? A LYS 598 NZ  
47 1 Y 0 A LYS 600 ? CG  ? A LYS 600 CG  
48 1 Y 0 A LYS 600 ? CD  ? A LYS 600 CD  
49 1 Y 0 A LYS 600 ? CE  ? A LYS 600 CE  
50 1 Y 0 A LYS 600 ? NZ  ? A LYS 600 NZ  
51 1 Y 0 A LYS 634 ? CG  ? A LYS 634 CG  
52 1 Y 0 A LYS 634 ? CD  ? A LYS 634 CD  
53 1 Y 0 A LYS 634 ? CE  ? A LYS 634 CE  
54 1 Y 0 A LYS 634 ? NZ  ? A LYS 634 NZ  
55 1 Y 0 A MET 652 ? CG  ? A MET 652 CG  
56 1 Y 0 A MET 652 ? SD  ? A MET 652 SD  
57 1 Y 0 A MET 652 ? CE  ? A MET 652 CE  
58 1 Y 0 A LEU 661 ? CG  ? A LEU 661 CG  
59 1 Y 0 A LEU 661 ? CD1 ? A LEU 661 CD1 
60 1 Y 0 A LEU 661 ? CD2 ? A LEU 661 CD2 
61 1 Y 0 A LYS 672 ? CD  ? A LYS 672 CD  
62 1 Y 0 A LYS 672 ? CE  ? A LYS 672 CE  
63 1 Y 0 A LYS 672 ? NZ  ? A LYS 672 NZ  
64 1 Y 0 A LYS 674 ? CD  ? A LYS 674 CD  
65 1 Y 0 A LYS 674 ? CE  ? A LYS 674 CE  
66 1 Y 0 A LYS 674 ? NZ  ? A LYS 674 NZ  
# 
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 GLN 307 ? A GLN 307 
2  1 Y 1 A ASN 308 ? A ASN 308 
3  1 Y 1 A GLU 319 ? A GLU 319 
4  1 Y 1 A PHE 320 ? A PHE 320 
5  1 Y 1 A GLY 321 ? A GLY 321 
6  1 Y 1 A GLU 322 ? A GLU 322 
7  1 Y 1 A ILE 323 ? A ILE 323 
8  1 Y 1 A GLN 324 ? A GLN 324 
9  1 Y 1 A GLY 325 ? A GLY 325 
10 1 Y 1 A ASP 326 ? A ASP 326 
11 1 Y 1 A LYS 327 ? A LYS 327 
12 1 Y 1 A GLN 407 ? A GLN 407 
13 1 Y 1 A ASP 408 ? A ASP 408 
14 1 Y 1 A ASP 409 ? A ASP 409 
15 1 Y 1 A GLY 410 ? A GLY 410 
16 1 Y 1 A SER 411 ? A SER 411 
17 1 Y 1 A VAL 412 ? A VAL 412 
18 1 Y 1 A HIS 413 ? A HIS 413 
19 1 Y 1 A LEU 462 ? A LEU 462 
20 1 Y 1 A ASN 463 ? A ASN 463 
21 1 Y 1 A LYS 464 ? A LYS 464 
22 1 Y 1 A LEU 465 ? A LEU 465 
23 1 Y 1 A ALA 466 ? A ALA 466 
24 1 Y 1 A GLU 467 ? A GLU 467 
25 1 Y 1 A LYS 468 ? A LYS 468 
26 1 Y 1 A GLU 469 ? A GLU 469 
27 1 Y 1 A GLU 470 ? A GLU 470 
28 1 Y 1 A THR 471 ? A THR 471 
29 1 Y 1 A ILE 684 ? A ILE 684 
30 1 Y 1 A GLY 685 ? A GLY 685 
31 1 Y 1 A PRO 686 ? A PRO 686 
32 1 Y 1 A ALA 687 ? A ALA 687 
# 
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 
ACE C    C N N 1   
ACE O    O N N 2   
ACE CH3  C N N 3   
ACE H    H N N 4   
ACE H1   H N N 5   
ACE H2   H N N 6   
ACE H3   H N N 7   
ALA N    N N N 8   
ALA CA   C N S 9   
ALA C    C N N 10  
ALA O    O N N 11  
ALA CB   C N N 12  
ALA OXT  O N N 13  
ALA H    H N N 14  
ALA H2   H N N 15  
ALA HA   H N N 16  
ALA HB1  H N N 17  
ALA HB2  H N N 18  
ALA HB3  H N N 19  
ALA HXT  H N N 20  
ARG N    N N N 21  
ARG CA   C N S 22  
ARG C    C N N 23  
ARG O    O N N 24  
ARG CB   C N N 25  
ARG CG   C N N 26  
ARG CD   C N N 27  
ARG NE   N N N 28  
ARG CZ   C N N 29  
ARG NH1  N N N 30  
ARG NH2  N N N 31  
ARG OXT  O N N 32  
ARG H    H N N 33  
ARG H2   H N N 34  
ARG HA   H N N 35  
ARG HB2  H N N 36  
ARG HB3  H N N 37  
ARG HG2  H N N 38  
ARG HG3  H N N 39  
ARG HD2  H N N 40  
ARG HD3  H N N 41  
ARG HE   H N N 42  
ARG HH11 H N N 43  
ARG HH12 H N N 44  
ARG HH21 H N N 45  
ARG HH22 H N N 46  
ARG HXT  H N N 47  
ASN N    N N N 48  
ASN CA   C N S 49  
ASN C    C N N 50  
ASN O    O N N 51  
ASN CB   C N N 52  
ASN CG   C N N 53  
ASN OD1  O N N 54  
ASN ND2  N N N 55  
ASN OXT  O N N 56  
ASN H    H N N 57  
ASN H2   H N N 58  
ASN HA   H N N 59  
ASN HB2  H N N 60  
ASN HB3  H N N 61  
ASN HD21 H N N 62  
ASN HD22 H N N 63  
ASN HXT  H N N 64  
ASP N    N N N 65  
ASP CA   C N S 66  
ASP C    C N N 67  
ASP O    O N N 68  
ASP CB   C N N 69  
ASP CG   C N N 70  
ASP OD1  O N N 71  
ASP OD2  O N N 72  
ASP OXT  O N N 73  
ASP H    H N N 74  
ASP H2   H N N 75  
ASP HA   H N N 76  
ASP HB2  H N N 77  
ASP HB3  H N N 78  
ASP HD2  H N N 79  
ASP HXT  H N N 80  
CYS N    N N N 81  
CYS CA   C N R 82  
CYS C    C N N 83  
CYS O    O N N 84  
CYS CB   C N N 85  
CYS SG   S N N 86  
CYS OXT  O N N 87  
CYS H    H N N 88  
CYS H2   H N N 89  
CYS HA   H N N 90  
CYS HB2  H N N 91  
CYS HB3  H N N 92  
CYS HG   H N N 93  
CYS HXT  H N N 94  
GLN N    N N N 95  
GLN CA   C N S 96  
GLN C    C N N 97  
GLN O    O N N 98  
GLN CB   C N N 99  
GLN CG   C N N 100 
GLN CD   C N N 101 
GLN OE1  O N N 102 
GLN NE2  N N N 103 
GLN OXT  O N N 104 
GLN H    H N N 105 
GLN H2   H N N 106 
GLN HA   H N N 107 
GLN HB2  H N N 108 
GLN HB3  H N N 109 
GLN HG2  H N N 110 
GLN HG3  H N N 111 
GLN HE21 H N N 112 
GLN HE22 H N N 113 
GLN HXT  H N N 114 
GLU N    N N N 115 
GLU CA   C N S 116 
GLU C    C N N 117 
GLU O    O N N 118 
GLU CB   C N N 119 
GLU CG   C N N 120 
GLU CD   C N N 121 
GLU OE1  O N N 122 
GLU OE2  O N N 123 
GLU OXT  O N N 124 
GLU H    H N N 125 
GLU H2   H N N 126 
GLU HA   H N N 127 
GLU HB2  H N N 128 
GLU HB3  H N N 129 
GLU HG2  H N N 130 
GLU HG3  H N N 131 
GLU HE2  H N N 132 
GLU HXT  H N N 133 
GLY N    N N N 134 
GLY CA   C N N 135 
GLY C    C N N 136 
GLY O    O N N 137 
GLY OXT  O N N 138 
GLY H    H N N 139 
GLY H2   H N N 140 
GLY HA2  H N N 141 
GLY HA3  H N N 142 
GLY HXT  H N N 143 
HIS N    N N N 144 
HIS CA   C N S 145 
HIS C    C N N 146 
HIS O    O N N 147 
HIS CB   C N N 148 
HIS CG   C Y N 149 
HIS ND1  N Y N 150 
HIS CD2  C Y N 151 
HIS CE1  C Y N 152 
HIS NE2  N Y N 153 
HIS OXT  O N N 154 
HIS H    H N N 155 
HIS H2   H N N 156 
HIS HA   H N N 157 
HIS HB2  H N N 158 
HIS HB3  H N N 159 
HIS HD1  H N N 160 
HIS HD2  H N N 161 
HIS HE1  H N N 162 
HIS HE2  H N N 163 
HIS HXT  H N N 164 
HOH O    O N N 165 
HOH H1   H N N 166 
HOH H2   H N N 167 
ILE N    N N N 168 
ILE CA   C N S 169 
ILE C    C N N 170 
ILE O    O N N 171 
ILE CB   C N S 172 
ILE CG1  C N N 173 
ILE CG2  C N N 174 
ILE CD1  C N N 175 
ILE OXT  O N N 176 
ILE H    H N N 177 
ILE H2   H N N 178 
ILE HA   H N N 179 
ILE HB   H N N 180 
ILE HG12 H N N 181 
ILE HG13 H N N 182 
ILE HG21 H N N 183 
ILE HG22 H N N 184 
ILE HG23 H N N 185 
ILE HD11 H N N 186 
ILE HD12 H N N 187 
ILE HD13 H N N 188 
ILE HXT  H N N 189 
LEU N    N N N 190 
LEU CA   C N S 191 
LEU C    C N N 192 
LEU O    O N N 193 
LEU CB   C N N 194 
LEU CG   C N N 195 
LEU CD1  C N N 196 
LEU CD2  C N N 197 
LEU OXT  O N N 198 
LEU H    H N N 199 
LEU H2   H N N 200 
LEU HA   H N N 201 
LEU HB2  H N N 202 
LEU HB3  H N N 203 
LEU HG   H N N 204 
LEU HD11 H N N 205 
LEU HD12 H N N 206 
LEU HD13 H N N 207 
LEU HD21 H N N 208 
LEU HD22 H N N 209 
LEU HD23 H N N 210 
LEU HXT  H N N 211 
LYS N    N N N 212 
LYS CA   C N S 213 
LYS C    C N N 214 
LYS O    O N N 215 
LYS CB   C N N 216 
LYS CG   C N N 217 
LYS CD   C N N 218 
LYS CE   C N N 219 
LYS NZ   N N N 220 
LYS OXT  O N N 221 
LYS H    H N N 222 
LYS H2   H N N 223 
LYS HA   H N N 224 
LYS HB2  H N N 225 
LYS HB3  H N N 226 
LYS HG2  H N N 227 
LYS HG3  H N N 228 
LYS HD2  H N N 229 
LYS HD3  H N N 230 
LYS HE2  H N N 231 
LYS HE3  H N N 232 
LYS HZ1  H N N 233 
LYS HZ2  H N N 234 
LYS HZ3  H N N 235 
LYS HXT  H N N 236 
MET N    N N N 237 
MET CA   C N S 238 
MET C    C N N 239 
MET O    O N N 240 
MET CB   C N N 241 
MET CG   C N N 242 
MET SD   S N N 243 
MET CE   C N N 244 
MET OXT  O N N 245 
MET H    H N N 246 
MET H2   H N N 247 
MET HA   H N N 248 
MET HB2  H N N 249 
MET HB3  H N N 250 
MET HG2  H N N 251 
MET HG3  H N N 252 
MET HE1  H N N 253 
MET HE2  H N N 254 
MET HE3  H N N 255 
MET HXT  H N N 256 
NH2 N    N N N 257 
NH2 HN1  H N N 258 
NH2 HN2  H N N 259 
ONL N    N N N 260 
ONL CA   C N S 261 
ONL C    C N N 262 
ONL O    O N N 263 
ONL OXT  O N N 264 
ONL CB   C N N 265 
ONL CG   C N N 266 
ONL CD   C N N 267 
ONL OD   O N N 268 
ONL CE   C N N 269 
ONL H    H N N 270 
ONL H2   H N N 271 
ONL HA   H N N 272 
ONL HXT  H N N 273 
ONL HB1  H N N 274 
ONL HB2  H N N 275 
ONL HG1  H N N 276 
ONL HG2  H N N 277 
ONL HE1  H N N 278 
ONL HE2  H N N 279 
ONL HE3  H N N 280 
PHE N    N N N 281 
PHE CA   C N S 282 
PHE C    C N N 283 
PHE O    O N N 284 
PHE CB   C N N 285 
PHE CG   C Y N 286 
PHE CD1  C Y N 287 
PHE CD2  C Y N 288 
PHE CE1  C Y N 289 
PHE CE2  C Y N 290 
PHE CZ   C Y N 291 
PHE OXT  O N N 292 
PHE H    H N N 293 
PHE H2   H N N 294 
PHE HA   H N N 295 
PHE HB2  H N N 296 
PHE HB3  H N N 297 
PHE HD1  H N N 298 
PHE HD2  H N N 299 
PHE HE1  H N N 300 
PHE HE2  H N N 301 
PHE HZ   H N N 302 
PHE HXT  H N N 303 
PRO N    N N N 304 
PRO CA   C N S 305 
PRO C    C N N 306 
PRO O    O N N 307 
PRO CB   C N N 308 
PRO CG   C N N 309 
PRO CD   C N N 310 
PRO OXT  O N N 311 
PRO H    H N N 312 
PRO HA   H N N 313 
PRO HB2  H N N 314 
PRO HB3  H N N 315 
PRO HG2  H N N 316 
PRO HG3  H N N 317 
PRO HD2  H N N 318 
PRO HD3  H N N 319 
PRO HXT  H N N 320 
SER N    N N N 321 
SER CA   C N S 322 
SER C    C N N 323 
SER O    O N N 324 
SER CB   C N N 325 
SER OG   O N N 326 
SER OXT  O N N 327 
SER H    H N N 328 
SER H2   H N N 329 
SER HA   H N N 330 
SER HB2  H N N 331 
SER HB3  H N N 332 
SER HG   H N N 333 
SER HXT  H N N 334 
SO4 S    S N N 335 
SO4 O1   O N N 336 
SO4 O2   O N N 337 
SO4 O3   O N N 338 
SO4 O4   O N N 339 
THR N    N N N 340 
THR CA   C N S 341 
THR C    C N N 342 
THR O    O N N 343 
THR CB   C N R 344 
THR OG1  O N N 345 
THR CG2  C N N 346 
THR OXT  O N N 347 
THR H    H N N 348 
THR H2   H N N 349 
THR HA   H N N 350 
THR HB   H N N 351 
THR HG1  H N N 352 
THR HG21 H N N 353 
THR HG22 H N N 354 
THR HG23 H N N 355 
THR HXT  H N N 356 
TRP N    N N N 357 
TRP CA   C N S 358 
TRP C    C N N 359 
TRP O    O N N 360 
TRP CB   C N N 361 
TRP CG   C Y N 362 
TRP CD1  C Y N 363 
TRP CD2  C Y N 364 
TRP NE1  N Y N 365 
TRP CE2  C Y N 366 
TRP CE3  C Y N 367 
TRP CZ2  C Y N 368 
TRP CZ3  C Y N 369 
TRP CH2  C Y N 370 
TRP OXT  O N N 371 
TRP H    H N N 372 
TRP H2   H N N 373 
TRP HA   H N N 374 
TRP HB2  H N N 375 
TRP HB3  H N N 376 
TRP HD1  H N N 377 
TRP HE1  H N N 378 
TRP HE3  H N N 379 
TRP HZ2  H N N 380 
TRP HZ3  H N N 381 
TRP HH2  H N N 382 
TRP HXT  H N N 383 
TYR N    N N N 384 
TYR CA   C N S 385 
TYR C    C N N 386 
TYR O    O N N 387 
TYR CB   C N N 388 
TYR CG   C Y N 389 
TYR CD1  C Y N 390 
TYR CD2  C Y N 391 
TYR CE1  C Y N 392 
TYR CE2  C Y N 393 
TYR CZ   C Y N 394 
TYR OH   O N N 395 
TYR OXT  O N N 396 
TYR H    H N N 397 
TYR H2   H N N 398 
TYR HA   H N N 399 
TYR HB2  H N N 400 
TYR HB3  H N N 401 
TYR HD1  H N N 402 
TYR HD2  H N N 403 
TYR HE1  H N N 404 
TYR HE2  H N N 405 
TYR HH   H N N 406 
TYR HXT  H N N 407 
VAL N    N N N 408 
VAL CA   C N S 409 
VAL C    C N N 410 
VAL O    O N N 411 
VAL CB   C N N 412 
VAL CG1  C N N 413 
VAL CG2  C N N 414 
VAL OXT  O N N 415 
VAL H    H N N 416 
VAL H2   H N N 417 
VAL HA   H N N 418 
VAL HB   H N N 419 
VAL HG11 H N N 420 
VAL HG12 H N N 421 
VAL HG13 H N N 422 
VAL HG21 H N N 423 
VAL HG22 H N N 424 
VAL HG23 H N N 425 
VAL HXT  H N N 426 
# 
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 
ACE C   O    doub N N 1   
ACE C   CH3  sing N N 2   
ACE C   H    sing N N 3   
ACE CH3 H1   sing N N 4   
ACE CH3 H2   sing N N 5   
ACE CH3 H3   sing N N 6   
ALA N   CA   sing N N 7   
ALA N   H    sing N N 8   
ALA N   H2   sing N N 9   
ALA CA  C    sing N N 10  
ALA CA  CB   sing N N 11  
ALA CA  HA   sing N N 12  
ALA C   O    doub N N 13  
ALA C   OXT  sing N N 14  
ALA CB  HB1  sing N N 15  
ALA CB  HB2  sing N N 16  
ALA CB  HB3  sing N N 17  
ALA OXT HXT  sing N N 18  
ARG N   CA   sing N N 19  
ARG N   H    sing N N 20  
ARG N   H2   sing N N 21  
ARG CA  C    sing N N 22  
ARG CA  CB   sing N N 23  
ARG CA  HA   sing N N 24  
ARG C   O    doub N N 25  
ARG C   OXT  sing N N 26  
ARG CB  CG   sing N N 27  
ARG CB  HB2  sing N N 28  
ARG CB  HB3  sing N N 29  
ARG CG  CD   sing N N 30  
ARG CG  HG2  sing N N 31  
ARG CG  HG3  sing N N 32  
ARG CD  NE   sing N N 33  
ARG CD  HD2  sing N N 34  
ARG CD  HD3  sing N N 35  
ARG NE  CZ   sing N N 36  
ARG NE  HE   sing N N 37  
ARG CZ  NH1  sing N N 38  
ARG CZ  NH2  doub N N 39  
ARG NH1 HH11 sing N N 40  
ARG NH1 HH12 sing N N 41  
ARG NH2 HH21 sing N N 42  
ARG NH2 HH22 sing N N 43  
ARG OXT HXT  sing N N 44  
ASN N   CA   sing N N 45  
ASN N   H    sing N N 46  
ASN N   H2   sing N N 47  
ASN CA  C    sing N N 48  
ASN CA  CB   sing N N 49  
ASN CA  HA   sing N N 50  
ASN C   O    doub N N 51  
ASN C   OXT  sing N N 52  
ASN CB  CG   sing N N 53  
ASN CB  HB2  sing N N 54  
ASN CB  HB3  sing N N 55  
ASN CG  OD1  doub N N 56  
ASN CG  ND2  sing N N 57  
ASN ND2 HD21 sing N N 58  
ASN ND2 HD22 sing N N 59  
ASN OXT HXT  sing N N 60  
ASP N   CA   sing N N 61  
ASP N   H    sing N N 62  
ASP N   H2   sing N N 63  
ASP CA  C    sing N N 64  
ASP CA  CB   sing N N 65  
ASP CA  HA   sing N N 66  
ASP C   O    doub N N 67  
ASP C   OXT  sing N N 68  
ASP CB  CG   sing N N 69  
ASP CB  HB2  sing N N 70  
ASP CB  HB3  sing N N 71  
ASP CG  OD1  doub N N 72  
ASP CG  OD2  sing N N 73  
ASP OD2 HD2  sing N N 74  
ASP OXT HXT  sing N N 75  
CYS N   CA   sing N N 76  
CYS N   H    sing N N 77  
CYS N   H2   sing N N 78  
CYS CA  C    sing N N 79  
CYS CA  CB   sing N N 80  
CYS CA  HA   sing N N 81  
CYS C   O    doub N N 82  
CYS C   OXT  sing N N 83  
CYS CB  SG   sing N N 84  
CYS CB  HB2  sing N N 85  
CYS CB  HB3  sing N N 86  
CYS SG  HG   sing N N 87  
CYS OXT HXT  sing N N 88  
GLN N   CA   sing N N 89  
GLN N   H    sing N N 90  
GLN N   H2   sing N N 91  
GLN CA  C    sing N N 92  
GLN CA  CB   sing N N 93  
GLN CA  HA   sing N N 94  
GLN C   O    doub N N 95  
GLN C   OXT  sing N N 96  
GLN CB  CG   sing N N 97  
GLN CB  HB2  sing N N 98  
GLN CB  HB3  sing N N 99  
GLN CG  CD   sing N N 100 
GLN CG  HG2  sing N N 101 
GLN CG  HG3  sing N N 102 
GLN CD  OE1  doub N N 103 
GLN CD  NE2  sing N N 104 
GLN NE2 HE21 sing N N 105 
GLN NE2 HE22 sing N N 106 
GLN OXT HXT  sing N N 107 
GLU N   CA   sing N N 108 
GLU N   H    sing N N 109 
GLU N   H2   sing N N 110 
GLU CA  C    sing N N 111 
GLU CA  CB   sing N N 112 
GLU CA  HA   sing N N 113 
GLU C   O    doub N N 114 
GLU C   OXT  sing N N 115 
GLU CB  CG   sing N N 116 
GLU CB  HB2  sing N N 117 
GLU CB  HB3  sing N N 118 
GLU CG  CD   sing N N 119 
GLU CG  HG2  sing N N 120 
GLU CG  HG3  sing N N 121 
GLU CD  OE1  doub N N 122 
GLU CD  OE2  sing N N 123 
GLU OE2 HE2  sing N N 124 
GLU OXT HXT  sing N N 125 
GLY N   CA   sing N N 126 
GLY N   H    sing N N 127 
GLY N   H2   sing N N 128 
GLY CA  C    sing N N 129 
GLY CA  HA2  sing N N 130 
GLY CA  HA3  sing N N 131 
GLY C   O    doub N N 132 
GLY C   OXT  sing N N 133 
GLY OXT HXT  sing N N 134 
HIS N   CA   sing N N 135 
HIS N   H    sing N N 136 
HIS N   H2   sing N N 137 
HIS CA  C    sing N N 138 
HIS CA  CB   sing N N 139 
HIS CA  HA   sing N N 140 
HIS C   O    doub N N 141 
HIS C   OXT  sing N N 142 
HIS CB  CG   sing N N 143 
HIS CB  HB2  sing N N 144 
HIS CB  HB3  sing N N 145 
HIS CG  ND1  sing Y N 146 
HIS CG  CD2  doub Y N 147 
HIS ND1 CE1  doub Y N 148 
HIS ND1 HD1  sing N N 149 
HIS CD2 NE2  sing Y N 150 
HIS CD2 HD2  sing N N 151 
HIS CE1 NE2  sing Y N 152 
HIS CE1 HE1  sing N N 153 
HIS NE2 HE2  sing N N 154 
HIS OXT HXT  sing N N 155 
HOH O   H1   sing N N 156 
HOH O   H2   sing N N 157 
ILE N   CA   sing N N 158 
ILE N   H    sing N N 159 
ILE N   H2   sing N N 160 
ILE CA  C    sing N N 161 
ILE CA  CB   sing N N 162 
ILE CA  HA   sing N N 163 
ILE C   O    doub N N 164 
ILE C   OXT  sing N N 165 
ILE CB  CG1  sing N N 166 
ILE CB  CG2  sing N N 167 
ILE CB  HB   sing N N 168 
ILE CG1 CD1  sing N N 169 
ILE CG1 HG12 sing N N 170 
ILE CG1 HG13 sing N N 171 
ILE CG2 HG21 sing N N 172 
ILE CG2 HG22 sing N N 173 
ILE CG2 HG23 sing N N 174 
ILE CD1 HD11 sing N N 175 
ILE CD1 HD12 sing N N 176 
ILE CD1 HD13 sing N N 177 
ILE OXT HXT  sing N N 178 
LEU N   CA   sing N N 179 
LEU N   H    sing N N 180 
LEU N   H2   sing N N 181 
LEU CA  C    sing N N 182 
LEU CA  CB   sing N N 183 
LEU CA  HA   sing N N 184 
LEU C   O    doub N N 185 
LEU C   OXT  sing N N 186 
LEU CB  CG   sing N N 187 
LEU CB  HB2  sing N N 188 
LEU CB  HB3  sing N N 189 
LEU CG  CD1  sing N N 190 
LEU CG  CD2  sing N N 191 
LEU CG  HG   sing N N 192 
LEU CD1 HD11 sing N N 193 
LEU CD1 HD12 sing N N 194 
LEU CD1 HD13 sing N N 195 
LEU CD2 HD21 sing N N 196 
LEU CD2 HD22 sing N N 197 
LEU CD2 HD23 sing N N 198 
LEU OXT HXT  sing N N 199 
LYS N   CA   sing N N 200 
LYS N   H    sing N N 201 
LYS N   H2   sing N N 202 
LYS CA  C    sing N N 203 
LYS CA  CB   sing N N 204 
LYS CA  HA   sing N N 205 
LYS C   O    doub N N 206 
LYS C   OXT  sing N N 207 
LYS CB  CG   sing N N 208 
LYS CB  HB2  sing N N 209 
LYS CB  HB3  sing N N 210 
LYS CG  CD   sing N N 211 
LYS CG  HG2  sing N N 212 
LYS CG  HG3  sing N N 213 
LYS CD  CE   sing N N 214 
LYS CD  HD2  sing N N 215 
LYS CD  HD3  sing N N 216 
LYS CE  NZ   sing N N 217 
LYS CE  HE2  sing N N 218 
LYS CE  HE3  sing N N 219 
LYS NZ  HZ1  sing N N 220 
LYS NZ  HZ2  sing N N 221 
LYS NZ  HZ3  sing N N 222 
LYS OXT HXT  sing N N 223 
MET N   CA   sing N N 224 
MET N   H    sing N N 225 
MET N   H2   sing N N 226 
MET CA  C    sing N N 227 
MET CA  CB   sing N N 228 
MET CA  HA   sing N N 229 
MET C   O    doub N N 230 
MET C   OXT  sing N N 231 
MET CB  CG   sing N N 232 
MET CB  HB2  sing N N 233 
MET CB  HB3  sing N N 234 
MET CG  SD   sing N N 235 
MET CG  HG2  sing N N 236 
MET CG  HG3  sing N N 237 
MET SD  CE   sing N N 238 
MET CE  HE1  sing N N 239 
MET CE  HE2  sing N N 240 
MET CE  HE3  sing N N 241 
MET OXT HXT  sing N N 242 
NH2 N   HN1  sing N N 243 
NH2 N   HN2  sing N N 244 
ONL N   CA   sing N N 245 
ONL N   H    sing N N 246 
ONL N   H2   sing N N 247 
ONL CA  C    sing N N 248 
ONL CA  CB   sing N N 249 
ONL CA  HA   sing N N 250 
ONL C   O    doub N N 251 
ONL C   OXT  sing N N 252 
ONL OXT HXT  sing N N 253 
ONL CB  CG   sing N N 254 
ONL CB  HB1  sing N N 255 
ONL CB  HB2  sing N N 256 
ONL CG  CD   sing N N 257 
ONL CG  HG1  sing N N 258 
ONL CG  HG2  sing N N 259 
ONL CD  OD   doub N N 260 
ONL CD  CE   sing N N 261 
ONL CE  HE1  sing N N 262 
ONL CE  HE2  sing N N 263 
ONL CE  HE3  sing N N 264 
PHE N   CA   sing N N 265 
PHE N   H    sing N N 266 
PHE N   H2   sing N N 267 
PHE CA  C    sing N N 268 
PHE CA  CB   sing N N 269 
PHE CA  HA   sing N N 270 
PHE C   O    doub N N 271 
PHE C   OXT  sing N N 272 
PHE CB  CG   sing N N 273 
PHE CB  HB2  sing N N 274 
PHE CB  HB3  sing N N 275 
PHE CG  CD1  doub Y N 276 
PHE CG  CD2  sing Y N 277 
PHE CD1 CE1  sing Y N 278 
PHE CD1 HD1  sing N N 279 
PHE CD2 CE2  doub Y N 280 
PHE CD2 HD2  sing N N 281 
PHE CE1 CZ   doub Y N 282 
PHE CE1 HE1  sing N N 283 
PHE CE2 CZ   sing Y N 284 
PHE CE2 HE2  sing N N 285 
PHE CZ  HZ   sing N N 286 
PHE OXT HXT  sing N N 287 
PRO N   CA   sing N N 288 
PRO N   CD   sing N N 289 
PRO N   H    sing N N 290 
PRO CA  C    sing N N 291 
PRO CA  CB   sing N N 292 
PRO CA  HA   sing N N 293 
PRO C   O    doub N N 294 
PRO C   OXT  sing N N 295 
PRO CB  CG   sing N N 296 
PRO CB  HB2  sing N N 297 
PRO CB  HB3  sing N N 298 
PRO CG  CD   sing N N 299 
PRO CG  HG2  sing N N 300 
PRO CG  HG3  sing N N 301 
PRO CD  HD2  sing N N 302 
PRO CD  HD3  sing N N 303 
PRO OXT HXT  sing N N 304 
SER N   CA   sing N N 305 
SER N   H    sing N N 306 
SER N   H2   sing N N 307 
SER CA  C    sing N N 308 
SER CA  CB   sing N N 309 
SER CA  HA   sing N N 310 
SER C   O    doub N N 311 
SER C   OXT  sing N N 312 
SER CB  OG   sing N N 313 
SER CB  HB2  sing N N 314 
SER CB  HB3  sing N N 315 
SER OG  HG   sing N N 316 
SER OXT HXT  sing N N 317 
SO4 S   O1   doub N N 318 
SO4 S   O2   doub N N 319 
SO4 S   O3   sing N N 320 
SO4 S   O4   sing N N 321 
THR N   CA   sing N N 322 
THR N   H    sing N N 323 
THR N   H2   sing N N 324 
THR CA  C    sing N N 325 
THR CA  CB   sing N N 326 
THR CA  HA   sing N N 327 
THR C   O    doub N N 328 
THR C   OXT  sing N N 329 
THR CB  OG1  sing N N 330 
THR CB  CG2  sing N N 331 
THR CB  HB   sing N N 332 
THR OG1 HG1  sing N N 333 
THR CG2 HG21 sing N N 334 
THR CG2 HG22 sing N N 335 
THR CG2 HG23 sing N N 336 
THR OXT HXT  sing N N 337 
TRP N   CA   sing N N 338 
TRP N   H    sing N N 339 
TRP N   H2   sing N N 340 
TRP CA  C    sing N N 341 
TRP CA  CB   sing N N 342 
TRP CA  HA   sing N N 343 
TRP C   O    doub N N 344 
TRP C   OXT  sing N N 345 
TRP CB  CG   sing N N 346 
TRP CB  HB2  sing N N 347 
TRP CB  HB3  sing N N 348 
TRP CG  CD1  doub Y N 349 
TRP CG  CD2  sing Y N 350 
TRP CD1 NE1  sing Y N 351 
TRP CD1 HD1  sing N N 352 
TRP CD2 CE2  doub Y N 353 
TRP CD2 CE3  sing Y N 354 
TRP NE1 CE2  sing Y N 355 
TRP NE1 HE1  sing N N 356 
TRP CE2 CZ2  sing Y N 357 
TRP CE3 CZ3  doub Y N 358 
TRP CE3 HE3  sing N N 359 
TRP CZ2 CH2  doub Y N 360 
TRP CZ2 HZ2  sing N N 361 
TRP CZ3 CH2  sing Y N 362 
TRP CZ3 HZ3  sing N N 363 
TRP CH2 HH2  sing N N 364 
TRP OXT HXT  sing N N 365 
TYR N   CA   sing N N 366 
TYR N   H    sing N N 367 
TYR N   H2   sing N N 368 
TYR CA  C    sing N N 369 
TYR CA  CB   sing N N 370 
TYR CA  HA   sing N N 371 
TYR C   O    doub N N 372 
TYR C   OXT  sing N N 373 
TYR CB  CG   sing N N 374 
TYR CB  HB2  sing N N 375 
TYR CB  HB3  sing N N 376 
TYR CG  CD1  doub Y N 377 
TYR CG  CD2  sing Y N 378 
TYR CD1 CE1  sing Y N 379 
TYR CD1 HD1  sing N N 380 
TYR CD2 CE2  doub Y N 381 
TYR CD2 HD2  sing N N 382 
TYR CE1 CZ   doub Y N 383 
TYR CE1 HE1  sing N N 384 
TYR CE2 CZ   sing Y N 385 
TYR CE2 HE2  sing N N 386 
TYR CZ  OH   sing N N 387 
TYR OH  HH   sing N N 388 
TYR OXT HXT  sing N N 389 
VAL N   CA   sing N N 390 
VAL N   H    sing N N 391 
VAL N   H2   sing N N 392 
VAL CA  C    sing N N 393 
VAL CA  CB   sing N N 394 
VAL CA  HA   sing N N 395 
VAL C   O    doub N N 396 
VAL C   OXT  sing N N 397 
VAL CB  CG1  sing N N 398 
VAL CB  CG2  sing N N 399 
VAL CB  HB   sing N N 400 
VAL CG1 HG11 sing N N 401 
VAL CG1 HG12 sing N N 402 
VAL CG1 HG13 sing N N 403 
VAL CG2 HG21 sing N N 404 
VAL CG2 HG22 sing N N 405 
VAL CG2 HG23 sing N N 406 
VAL OXT HXT  sing N N 407 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'SULFATE ION' SO4 
4 water         HOH 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1KV3 
_pdbx_initial_refinement_model.details          ? 
# 



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: April 25th, 2023.