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***  test_3FXI  ***

elNémo ID: 2403081006492250692

Job options:

ID        	=	 2403081006492250692
JOBID     	=	 test_3FXI
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER test_3FXI

data_3FXI
# 
_entry.id   3FXI 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.380 
_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   3FXI         pdb_00003fxi 10.2210/pdb3fxi/pdb 
RCSB  RCSB051162   ?            ?                   
WWPDB D_1000051162 ?            ?                   
# 
_pdbx_database_status.entry_id                        3FXI 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.recvd_initial_deposition_date   2009-01-21 
_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.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Park, B.S.' 1 
'Song, D.H.' 2 
'Kim, H.M.'  3 
'Lee, J.-O.' 4 
# 
_citation.id                        primary 
_citation.title                     'The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex' 
_citation.journal_abbrev            Nature 
_citation.journal_volume            458 
_citation.page_first                1191 
_citation.page_last                 1195 
_citation.year                      2009 
_citation.journal_id_ASTM           NATUAS 
_citation.country                   UK 
_citation.journal_id_ISSN           0028-0836 
_citation.journal_id_CSD            0006 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   19252480 
_citation.pdbx_database_id_DOI      10.1038/nature07830 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Park, B.S.'  1 ? 
primary 'Song, D.H.'  2 ? 
primary 'Kim, H.M.'   3 ? 
primary 'Choi, B.-S.' 4 ? 
primary 'Lee, H.'     5 ? 
primary 'Lee, J.-O.'  6 ? 
# 
_cell.entry_id           3FXI 
_cell.length_a           91.160 
_cell.length_b           103.500 
_cell.length_c           251.810 
_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                         3FXI 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_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 'Toll-like receptor 4' 68838.328 2 ? ? 'extracellular domain, residues 27-631' ? 
2  polymer     man 'Lymphocyte antigen 96' 16385.941 2 ? ? ?                                       ? 
3  branched    man 
;L-glycero-alpha-D-manno-heptopyranose-(1-7)-L-glycero-alpha-D-manno-heptopyranose-(1-3)-L-glycero-alpha-D-manno-heptopyranose-(1-5)-[3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid-(2-4)]3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid-(2-6)-2-amino-2-deoxy-alpha-D-glucopyranose-(1-6)-2-amino-2-deoxy-alpha-D-glucopyranose
;
1357.181  1 ? ? ?                                       ? 
4  branched    man '2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 424.401   4 ? ? ? ? 
5  branched    man 
;L-glycero-alpha-D-manno-heptopyranose-(1-7)-L-glycero-alpha-D-manno-heptopyranose-(1-3)-L-glycero-alpha-D-manno-heptopyranose-(1-5)-[3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid-(2-4)]3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid-(2-6)-2-amino-2-deoxy-beta-D-glucopyranose-(1-6)-2-amino-2-deoxy-alpha-D-glucopyranose
;
1357.181  1 ? ? ?                                       ? 
6  non-polymer syn '3-HYDROXY-TETRADECANOIC ACID' 244.370   8 ? ? ?                                       ? 
7  non-polymer syn 'LAURIC ACID' 200.318   2 ? ? ?                                       ? 
8  non-polymer syn 'MYRISTIC ACID' 228.371   2 ? ? ?                                       ? 
9  non-polymer syn 'PHOSPHATE ION' 94.971    8 ? ? ?                                       ? 
10 non-polymer man 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   8 ? ? ?                                       ? 
11 non-polymer syn 'MAGNESIUM ION' 24.305    2 ? ? ?                                       ? 
12 water       nat water 18.015    2 ? ? ?                                       ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'TLR4, hToll'                
2 'MD-2, Protein MD-2, ESOP-1' 
# 
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 
;EPCVEVVPNITYQCMELNFYKIPDNLPFSTKNLDLSFNPLRHLGSYSFFSFPELQVLDLSRCEIQTIEDGAYQSLSHLST
LILTGNPIQSLALGAFSGLSSLQKLVAVETNLASLENFPIGHLKTLKELNVAHNLIQSFKLPEYFSNLTNLEHLDLSSNK
IQSIYCTDLRVLHQMPLLNLSLDLSLNPMNFIQPGAFKEIRLHKLTLRNNFDSLNVMKTCIQGLAGLEVHRLVLGEFRNE
GNLEKFDKSALEGLCNLTIEEFRLAYLDYYLDDIIDLFNCLTNVSSFSLVSVTIERVKDFSYNFGWQHLELVNCKFGQFP
TLKLKSLKRLTFTSNKGGNAFSEVDLPSLEFLDLSRNGLSFKGCCSQSDFGTTSLKYLDLSFNGVITMSSNFLGLEQLEH
LDFQHSNLKQMSEFSVFLSLRNLIYLDISHTHTRVAFNGIFNGLSSLEVLKMAGNSFQENFLPDIFTELRNLTFLDLSQC
QLEQLSPTAFNSLSSLQVLNMSHNNFFSLDTFPYKCLNSLQVLDYSLNHIMTSKKQELQHFPSSLAFLNLTQNDFACTCE
HQSFLQWIKDQRQLLVEVERMECATPSDKQGMPVLSLNITCQMNK
;
;EPCVEVVPNITYQCMELNFYKIPDNLPFSTKNLDLSFNPLRHLGSYSFFSFPELQVLDLSRCEIQTIEDGAYQSLSHLST
LILTGNPIQSLALGAFSGLSSLQKLVAVETNLASLENFPIGHLKTLKELNVAHNLIQSFKLPEYFSNLTNLEHLDLSSNK
IQSIYCTDLRVLHQMPLLNLSLDLSLNPMNFIQPGAFKEIRLHKLTLRNNFDSLNVMKTCIQGLAGLEVHRLVLGEFRNE
GNLEKFDKSALEGLCNLTIEEFRLAYLDYYLDDIIDLFNCLTNVSSFSLVSVTIERVKDFSYNFGWQHLELVNCKFGQFP
TLKLKSLKRLTFTSNKGGNAFSEVDLPSLEFLDLSRNGLSFKGCCSQSDFGTTSLKYLDLSFNGVITMSSNFLGLEQLEH
LDFQHSNLKQMSEFSVFLSLRNLIYLDISHTHTRVAFNGIFNGLSSLEVLKMAGNSFQENFLPDIFTELRNLTFLDLSQC
QLEQLSPTAFNSLSSLQVLNMSHNNFFSLDTFPYKCLNSLQVLDYSLNHIMTSKKQELQHFPSSLAFLNLTQNDFACTCE
HQSFLQWIKDQRQLLVEVERMECATPSDKQGMPVLSLNITCQMNK
;
A,B ? 
2 'polypeptide(L)' no no 
;QKQYWVCNSSDASISYTYCDKMQYPISINVNPCIELKGSKGLLHIFYIPRRDLKQLYFNLYITVNTMNLPKRKEVICRGS
DDDYSFCRALKGETVNTTISFSFKGIKFSKGKYKCVVEAISGSPEEMLFCLEFVILHQPNSN
;
;QKQYWVCNSSDASISYTYCDKMQYPISINVNPCIELKGSKGLLHIFYIPRRDLKQLYFNLYITVNTMNLPKRKEVICRGS
DDDYSFCRALKGETVNTTISFSFKGIKFSKGKYKCVVEAISGSPEEMLFCLEFVILHQPNSN
;
C,D ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLU n 
1 2   PRO n 
1 3   CYS n 
1 4   VAL n 
1 5   GLU n 
1 6   VAL n 
1 7   VAL n 
1 8   PRO n 
1 9   ASN n 
1 10  ILE n 
1 11  THR n 
1 12  TYR n 
1 13  GLN n 
1 14  CYS n 
1 15  MET n 
1 16  GLU n 
1 17  LEU n 
1 18  ASN n 
1 19  PHE n 
1 20  TYR n 
1 21  LYS n 
1 22  ILE n 
1 23  PRO n 
1 24  ASP n 
1 25  ASN n 
1 26  LEU n 
1 27  PRO n 
1 28  PHE n 
1 29  SER n 
1 30  THR n 
1 31  LYS n 
1 32  ASN n 
1 33  LEU n 
1 34  ASP n 
1 35  LEU n 
1 36  SER n 
1 37  PHE n 
1 38  ASN n 
1 39  PRO n 
1 40  LEU n 
1 41  ARG n 
1 42  HIS n 
1 43  LEU n 
1 44  GLY n 
1 45  SER n 
1 46  TYR n 
1 47  SER n 
1 48  PHE n 
1 49  PHE n 
1 50  SER n 
1 51  PHE n 
1 52  PRO n 
1 53  GLU n 
1 54  LEU n 
1 55  GLN n 
1 56  VAL n 
1 57  LEU n 
1 58  ASP n 
1 59  LEU n 
1 60  SER n 
1 61  ARG n 
1 62  CYS n 
1 63  GLU n 
1 64  ILE n 
1 65  GLN n 
1 66  THR n 
1 67  ILE n 
1 68  GLU n 
1 69  ASP n 
1 70  GLY n 
1 71  ALA n 
1 72  TYR n 
1 73  GLN n 
1 74  SER n 
1 75  LEU n 
1 76  SER n 
1 77  HIS n 
1 78  LEU n 
1 79  SER n 
1 80  THR n 
1 81  LEU n 
1 82  ILE n 
1 83  LEU n 
1 84  THR n 
1 85  GLY n 
1 86  ASN n 
1 87  PRO n 
1 88  ILE n 
1 89  GLN n 
1 90  SER n 
1 91  LEU n 
1 92  ALA n 
1 93  LEU n 
1 94  GLY n 
1 95  ALA n 
1 96  PHE n 
1 97  SER n 
1 98  GLY n 
1 99  LEU n 
1 100 SER n 
1 101 SER n 
1 102 LEU n 
1 103 GLN n 
1 104 LYS n 
1 105 LEU n 
1 106 VAL n 
1 107 ALA n 
1 108 VAL n 
1 109 GLU n 
1 110 THR n 
1 111 ASN n 
1 112 LEU n 
1 113 ALA n 
1 114 SER n 
1 115 LEU n 
1 116 GLU n 
1 117 ASN n 
1 118 PHE n 
1 119 PRO n 
1 120 ILE n 
1 121 GLY n 
1 122 HIS n 
1 123 LEU n 
1 124 LYS n 
1 125 THR n 
1 126 LEU n 
1 127 LYS n 
1 128 GLU n 
1 129 LEU n 
1 130 ASN n 
1 131 VAL n 
1 132 ALA n 
1 133 HIS n 
1 134 ASN n 
1 135 LEU n 
1 136 ILE n 
1 137 GLN n 
1 138 SER n 
1 139 PHE n 
1 140 LYS n 
1 141 LEU n 
1 142 PRO n 
1 143 GLU n 
1 144 TYR n 
1 145 PHE n 
1 146 SER n 
1 147 ASN n 
1 148 LEU n 
1 149 THR n 
1 150 ASN n 
1 151 LEU n 
1 152 GLU n 
1 153 HIS n 
1 154 LEU n 
1 155 ASP n 
1 156 LEU n 
1 157 SER n 
1 158 SER n 
1 159 ASN n 
1 160 LYS n 
1 161 ILE n 
1 162 GLN n 
1 163 SER n 
1 164 ILE n 
1 165 TYR n 
1 166 CYS n 
1 167 THR n 
1 168 ASP n 
1 169 LEU n 
1 170 ARG n 
1 171 VAL n 
1 172 LEU n 
1 173 HIS n 
1 174 GLN n 
1 175 MET n 
1 176 PRO n 
1 177 LEU n 
1 178 LEU n 
1 179 ASN n 
1 180 LEU n 
1 181 SER n 
1 182 LEU n 
1 183 ASP n 
1 184 LEU n 
1 185 SER n 
1 186 LEU n 
1 187 ASN n 
1 188 PRO n 
1 189 MET n 
1 190 ASN n 
1 191 PHE n 
1 192 ILE n 
1 193 GLN n 
1 194 PRO n 
1 195 GLY n 
1 196 ALA n 
1 197 PHE n 
1 198 LYS n 
1 199 GLU n 
1 200 ILE n 
1 201 ARG n 
1 202 LEU n 
1 203 HIS n 
1 204 LYS n 
1 205 LEU n 
1 206 THR n 
1 207 LEU n 
1 208 ARG n 
1 209 ASN n 
1 210 ASN n 
1 211 PHE n 
1 212 ASP n 
1 213 SER n 
1 214 LEU n 
1 215 ASN n 
1 216 VAL n 
1 217 MET n 
1 218 LYS n 
1 219 THR n 
1 220 CYS n 
1 221 ILE n 
1 222 GLN n 
1 223 GLY n 
1 224 LEU n 
1 225 ALA n 
1 226 GLY n 
1 227 LEU n 
1 228 GLU n 
1 229 VAL n 
1 230 HIS n 
1 231 ARG n 
1 232 LEU n 
1 233 VAL n 
1 234 LEU n 
1 235 GLY n 
1 236 GLU n 
1 237 PHE n 
1 238 ARG n 
1 239 ASN n 
1 240 GLU n 
1 241 GLY n 
1 242 ASN n 
1 243 LEU n 
1 244 GLU n 
1 245 LYS n 
1 246 PHE n 
1 247 ASP n 
1 248 LYS n 
1 249 SER n 
1 250 ALA n 
1 251 LEU n 
1 252 GLU n 
1 253 GLY n 
1 254 LEU n 
1 255 CYS n 
1 256 ASN n 
1 257 LEU n 
1 258 THR n 
1 259 ILE n 
1 260 GLU n 
1 261 GLU n 
1 262 PHE n 
1 263 ARG n 
1 264 LEU n 
1 265 ALA n 
1 266 TYR n 
1 267 LEU n 
1 268 ASP n 
1 269 TYR n 
1 270 TYR n 
1 271 LEU n 
1 272 ASP n 
1 273 ASP n 
1 274 ILE n 
1 275 ILE n 
1 276 ASP n 
1 277 LEU n 
1 278 PHE n 
1 279 ASN n 
1 280 CYS n 
1 281 LEU n 
1 282 THR n 
1 283 ASN n 
1 284 VAL n 
1 285 SER n 
1 286 SER n 
1 287 PHE n 
1 288 SER n 
1 289 LEU n 
1 290 VAL n 
1 291 SER n 
1 292 VAL n 
1 293 THR n 
1 294 ILE n 
1 295 GLU n 
1 296 ARG n 
1 297 VAL n 
1 298 LYS n 
1 299 ASP n 
1 300 PHE n 
1 301 SER n 
1 302 TYR n 
1 303 ASN n 
1 304 PHE n 
1 305 GLY n 
1 306 TRP n 
1 307 GLN n 
1 308 HIS n 
1 309 LEU n 
1 310 GLU n 
1 311 LEU n 
1 312 VAL n 
1 313 ASN n 
1 314 CYS n 
1 315 LYS n 
1 316 PHE n 
1 317 GLY n 
1 318 GLN n 
1 319 PHE n 
1 320 PRO n 
1 321 THR n 
1 322 LEU n 
1 323 LYS n 
1 324 LEU n 
1 325 LYS n 
1 326 SER n 
1 327 LEU n 
1 328 LYS n 
1 329 ARG n 
1 330 LEU n 
1 331 THR n 
1 332 PHE n 
1 333 THR n 
1 334 SER n 
1 335 ASN n 
1 336 LYS n 
1 337 GLY n 
1 338 GLY n 
1 339 ASN n 
1 340 ALA n 
1 341 PHE n 
1 342 SER n 
1 343 GLU n 
1 344 VAL n 
1 345 ASP n 
1 346 LEU n 
1 347 PRO n 
1 348 SER n 
1 349 LEU n 
1 350 GLU n 
1 351 PHE n 
1 352 LEU n 
1 353 ASP n 
1 354 LEU n 
1 355 SER n 
1 356 ARG n 
1 357 ASN n 
1 358 GLY n 
1 359 LEU n 
1 360 SER n 
1 361 PHE n 
1 362 LYS n 
1 363 GLY n 
1 364 CYS n 
1 365 CYS n 
1 366 SER n 
1 367 GLN n 
1 368 SER n 
1 369 ASP n 
1 370 PHE n 
1 371 GLY n 
1 372 THR n 
1 373 THR n 
1 374 SER n 
1 375 LEU n 
1 376 LYS n 
1 377 TYR n 
1 378 LEU n 
1 379 ASP n 
1 380 LEU n 
1 381 SER n 
1 382 PHE n 
1 383 ASN n 
1 384 GLY n 
1 385 VAL n 
1 386 ILE n 
1 387 THR n 
1 388 MET n 
1 389 SER n 
1 390 SER n 
1 391 ASN n 
1 392 PHE n 
1 393 LEU n 
1 394 GLY n 
1 395 LEU n 
1 396 GLU n 
1 397 GLN n 
1 398 LEU n 
1 399 GLU n 
1 400 HIS n 
1 401 LEU n 
1 402 ASP n 
1 403 PHE n 
1 404 GLN n 
1 405 HIS n 
1 406 SER n 
1 407 ASN n 
1 408 LEU n 
1 409 LYS n 
1 410 GLN n 
1 411 MET n 
1 412 SER n 
1 413 GLU n 
1 414 PHE n 
1 415 SER n 
1 416 VAL n 
1 417 PHE n 
1 418 LEU n 
1 419 SER n 
1 420 LEU n 
1 421 ARG n 
1 422 ASN n 
1 423 LEU n 
1 424 ILE n 
1 425 TYR n 
1 426 LEU n 
1 427 ASP n 
1 428 ILE n 
1 429 SER n 
1 430 HIS n 
1 431 THR n 
1 432 HIS n 
1 433 THR n 
1 434 ARG n 
1 435 VAL n 
1 436 ALA n 
1 437 PHE n 
1 438 ASN n 
1 439 GLY n 
1 440 ILE n 
1 441 PHE n 
1 442 ASN n 
1 443 GLY n 
1 444 LEU n 
1 445 SER n 
1 446 SER n 
1 447 LEU n 
1 448 GLU n 
1 449 VAL n 
1 450 LEU n 
1 451 LYS n 
1 452 MET n 
1 453 ALA n 
1 454 GLY n 
1 455 ASN n 
1 456 SER n 
1 457 PHE n 
1 458 GLN n 
1 459 GLU n 
1 460 ASN n 
1 461 PHE n 
1 462 LEU n 
1 463 PRO n 
1 464 ASP n 
1 465 ILE n 
1 466 PHE n 
1 467 THR n 
1 468 GLU n 
1 469 LEU n 
1 470 ARG n 
1 471 ASN n 
1 472 LEU n 
1 473 THR n 
1 474 PHE n 
1 475 LEU n 
1 476 ASP n 
1 477 LEU n 
1 478 SER n 
1 479 GLN n 
1 480 CYS n 
1 481 GLN n 
1 482 LEU n 
1 483 GLU n 
1 484 GLN n 
1 485 LEU n 
1 486 SER n 
1 487 PRO n 
1 488 THR n 
1 489 ALA n 
1 490 PHE n 
1 491 ASN n 
1 492 SER n 
1 493 LEU n 
1 494 SER n 
1 495 SER n 
1 496 LEU n 
1 497 GLN n 
1 498 VAL n 
1 499 LEU n 
1 500 ASN n 
1 501 MET n 
1 502 SER n 
1 503 HIS n 
1 504 ASN n 
1 505 ASN n 
1 506 PHE n 
1 507 PHE n 
1 508 SER n 
1 509 LEU n 
1 510 ASP n 
1 511 THR n 
1 512 PHE n 
1 513 PRO n 
1 514 TYR n 
1 515 LYS n 
1 516 CYS n 
1 517 LEU n 
1 518 ASN n 
1 519 SER n 
1 520 LEU n 
1 521 GLN n 
1 522 VAL n 
1 523 LEU n 
1 524 ASP n 
1 525 TYR n 
1 526 SER n 
1 527 LEU n 
1 528 ASN n 
1 529 HIS n 
1 530 ILE n 
1 531 MET n 
1 532 THR n 
1 533 SER n 
1 534 LYS n 
1 535 LYS n 
1 536 GLN n 
1 537 GLU n 
1 538 LEU n 
1 539 GLN n 
1 540 HIS n 
1 541 PHE n 
1 542 PRO n 
1 543 SER n 
1 544 SER n 
1 545 LEU n 
1 546 ALA n 
1 547 PHE n 
1 548 LEU n 
1 549 ASN n 
1 550 LEU n 
1 551 THR n 
1 552 GLN n 
1 553 ASN n 
1 554 ASP n 
1 555 PHE n 
1 556 ALA n 
1 557 CYS n 
1 558 THR n 
1 559 CYS n 
1 560 GLU n 
1 561 HIS n 
1 562 GLN n 
1 563 SER n 
1 564 PHE n 
1 565 LEU n 
1 566 GLN n 
1 567 TRP n 
1 568 ILE n 
1 569 LYS n 
1 570 ASP n 
1 571 GLN n 
1 572 ARG n 
1 573 GLN n 
1 574 LEU n 
1 575 LEU n 
1 576 VAL n 
1 577 GLU n 
1 578 VAL n 
1 579 GLU n 
1 580 ARG n 
1 581 MET n 
1 582 GLU n 
1 583 CYS n 
1 584 ALA n 
1 585 THR n 
1 586 PRO n 
1 587 SER n 
1 588 ASP n 
1 589 LYS n 
1 590 GLN n 
1 591 GLY n 
1 592 MET n 
1 593 PRO n 
1 594 VAL n 
1 595 LEU n 
1 596 SER n 
1 597 LEU n 
1 598 ASN n 
1 599 ILE n 
1 600 THR n 
1 601 CYS n 
1 602 GLN n 
1 603 MET n 
1 604 ASN n 
1 605 LYS n 
2 1   GLN n 
2 2   LYS n 
2 3   GLN n 
2 4   TYR n 
2 5   TRP n 
2 6   VAL n 
2 7   CYS n 
2 8   ASN n 
2 9   SER n 
2 10  SER n 
2 11  ASP n 
2 12  ALA n 
2 13  SER n 
2 14  ILE n 
2 15  SER n 
2 16  TYR n 
2 17  THR n 
2 18  TYR n 
2 19  CYS n 
2 20  ASP n 
2 21  LYS n 
2 22  MET n 
2 23  GLN n 
2 24  TYR n 
2 25  PRO n 
2 26  ILE n 
2 27  SER n 
2 28  ILE n 
2 29  ASN n 
2 30  VAL n 
2 31  ASN n 
2 32  PRO n 
2 33  CYS n 
2 34  ILE n 
2 35  GLU n 
2 36  LEU n 
2 37  LYS n 
2 38  GLY n 
2 39  SER n 
2 40  LYS n 
2 41  GLY n 
2 42  LEU n 
2 43  LEU n 
2 44  HIS n 
2 45  ILE n 
2 46  PHE n 
2 47  TYR n 
2 48  ILE n 
2 49  PRO n 
2 50  ARG n 
2 51  ARG n 
2 52  ASP n 
2 53  LEU n 
2 54  LYS n 
2 55  GLN n 
2 56  LEU n 
2 57  TYR n 
2 58  PHE n 
2 59  ASN n 
2 60  LEU n 
2 61  TYR n 
2 62  ILE n 
2 63  THR n 
2 64  VAL n 
2 65  ASN n 
2 66  THR n 
2 67  MET n 
2 68  ASN n 
2 69  LEU n 
2 70  PRO n 
2 71  LYS n 
2 72  ARG n 
2 73  LYS n 
2 74  GLU n 
2 75  VAL n 
2 76  ILE n 
2 77  CYS n 
2 78  ARG n 
2 79  GLY n 
2 80  SER n 
2 81  ASP n 
2 82  ASP n 
2 83  ASP n 
2 84  TYR n 
2 85  SER n 
2 86  PHE n 
2 87  CYS n 
2 88  ARG n 
2 89  ALA n 
2 90  LEU n 
2 91  LYS n 
2 92  GLY n 
2 93  GLU n 
2 94  THR n 
2 95  VAL n 
2 96  ASN n 
2 97  THR n 
2 98  THR n 
2 99  ILE n 
2 100 SER n 
2 101 PHE n 
2 102 SER n 
2 103 PHE n 
2 104 LYS n 
2 105 GLY n 
2 106 ILE n 
2 107 LYS n 
2 108 PHE n 
2 109 SER n 
2 110 LYS n 
2 111 GLY n 
2 112 LYS n 
2 113 TYR n 
2 114 LYS n 
2 115 CYS n 
2 116 VAL n 
2 117 VAL n 
2 118 GLU n 
2 119 ALA n 
2 120 ILE n 
2 121 SER n 
2 122 GLY n 
2 123 SER n 
2 124 PRO n 
2 125 GLU n 
2 126 GLU n 
2 127 MET n 
2 128 LEU n 
2 129 PHE n 
2 130 CYS n 
2 131 LEU n 
2 132 GLU n 
2 133 PHE n 
2 134 VAL n 
2 135 ILE n 
2 136 LEU n 
2 137 HIS n 
2 138 GLN n 
2 139 PRO n 
2 140 ASN n 
2 141 SER n 
2 142 ASN n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample ? ? ? human ? TLR4                     ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Trichoplusia ni' 7111 ? ? ? ? ? 
? ? ? ? ? ? 'HIGH FIVE CELLS' ? ? baculovirus ? ? ? pAcGP67A ? ? 
2 1 sample ? ? ? human ? 'ESOP1, LY96, MD-2, MD2' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Trichoplusia ni' 7111 ? ? ? ? ? 
? ? ? ? ? ? 'HIGH FIVE CELLS' ? ? baculovirus ? ? ? pAcGP67A ? ? 
# 
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 TLR4_HUMAN O00206 1 
;EPCVEVVPNITYQCMELNFYKIPDNLPFSTKNLDLSFNPLRHLGSYSFFSFPELQVLDLSRCEIQTIEDGAYQSLSHLST
LILTGNPIQSLALGAFSGLSSLQKLVAVETNLASLENFPIGHLKTLKELNVAHNLIQSFKLPEYFSNLTNLEHLDLSSNK
IQSIYCTDLRVLHQMPLLNLSLDLSLNPMNFIQPGAFKEIRLHKLTLRNNFDSLNVMKTCIQGLAGLEVHRLVLGEFRNE
GNLEKFDKSALEGLCNLTIEEFRLAYLDYYLDDIIDLFNCLTNVSSFSLVSVTIERVKDFSYNFGWQHLELVNCKFGQFP
TLKLKSLKRLTFTSNKGGNAFSEVDLPSLEFLDLSRNGLSFKGCCSQSDFGTTSLKYLDLSFNGVITMSSNFLGLEQLEH
LDFQHSNLKQMSEFSVFLSLRNLIYLDISHTHTRVAFNGIFNGLSSLEVLKMAGNSFQENFLPDIFTELRNLTFLDLSQC
QLEQLSPTAFNSLSSLQVLNMSHNNFFSLDTFPYKCLNSLQVLDYSLNHIMTSKKQELQHFPSSLAFLNLTQNDFACTCE
HQSFLQWIKDQRQLLVEVERMECATPSDKQGMPVLSLNITCQMNK
;
27 ? 
2 UNP LY96_HUMAN Q9Y6Y9 2 
;QKQYWVCNSSDASISYTYCDKMQYPISINVNPCIELKGSKGLLHIFYIPRRDLKQLYFNLYITVNTMNLPKRKEVICRGS
DDDYSFCRALKGETVNTTISFSFKGIKFSKGKYKCVVEAISGSPEEMLFCLEFVILHQPNSN
;
19 ? 
# 
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 3FXI A 1 ? 605 ? O00206 27 ? 631 ? 27 631 
2 1 3FXI B 1 ? 605 ? O00206 27 ? 631 ? 27 631 
3 2 3FXI C 1 ? 142 ? Q9Y6Y9 19 ? 160 ? 19 160 
4 2 3FXI D 1 ? 142 ? Q9Y6Y9 19 ? 160 ? 19 160 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking'           y ALANINE                                           ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking'           y ARGININE                                          ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking'           y ASPARAGINE                                        ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking'           y 'ASPARTIC ACID'                                   ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking'           y CYSTEINE                                          ? 'C3 H7 N O2 S'   121.158 
DAO non-polymer                   . 'LAURIC ACID'                                     ? 'C12 H24 O2'     200.318 
FTT non-polymer                   . '3-HYDROXY-TETRADECANOIC ACID'                    '3-HYDROXY-MYRISTIC ACID' 'C14 H28 O3'     
244.370 
GCS 'D-saccharide, beta linking'  . 2-amino-2-deoxy-beta-D-glucopyranose              
'beta-D-glucosamine; 2-amino-2-deoxy-beta-D-glucose; 2-amino-2-deoxy-D-glucose; 2-amino-2-deoxy-glucose; D-GLUCOSAMINE' 
'C6 H13 N O5'    179.171 
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  
GMH 'D-saccharide, alpha linking' . L-glycero-alpha-D-manno-heptopyranose             
'L-glycero-alpha-D-manno-heptose; L-glycero-D-manno-heptose; L-glycero-manno-heptose; L-GLYCERO-D-MANNO-HEPTOPYRANOSE' 'C7 H14 O7' 
210.182 
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 
KDO 'D-saccharide, alpha linking' . '3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid' 
;3-deoxy-d-manno-oct-2-ulopyranosonic acid; 2-keto-3-deoxy-D-mannooctanoic acid; 3-deoxy-alpha-D-manno-oct-2-ulosonic acid; 3-deoxy-D-manno-oct-2-ulosonic acid; 3-deoxy-manno-oct-2-ulosonic acid
;
'C8 H14 O8'      238.192 
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 
MG  non-polymer                   . 'MAGNESIUM ION'                                   ? 'Mg 2'           24.305  
MYR non-polymer                   . 'MYRISTIC ACID'                                   ? 'C14 H28 O2'     228.371 
NAG 'D-saccharide, beta linking'  . 2-acetamido-2-deoxy-beta-D-glucopyranose          
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
PA1 'D-saccharide, alpha linking' . 2-amino-2-deoxy-alpha-D-glucopyranose             
'alpah-D-glucosamine; 2-amino-2-deoxy-alpha-D-glucose; 2-amino-2-deoxy-D-glucose; 2-amino-2-deoxy-glucose' 'C6 H13 N O5'    
179.171 
PHE 'L-peptide linking'           y PHENYLALANINE                                     ? 'C9 H11 N O2'    165.189 
PO4 non-polymer                   . 'PHOSPHATE ION'                                   ? 'O4 P -3'        94.971  
PRO 'L-peptide linking'           y PROLINE                                           ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking'           y SERINE                                            ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking'           y THREONINE                                         ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking'           y TRYPTOPHAN                                        ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking'           y TYROSINE                                          ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking'           y VALINE                                            ? 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          3FXI 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.pdbx_mosaicity        ? 
_exptl_crystal.pdbx_mosaicity_esd    ? 
_exptl_crystal.density_Matthews      3.51 
_exptl_crystal.density_diffrn        ? 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_meas_temp     ? 
_exptl_crystal.density_percent_sol   64.91 
_exptl_crystal.size_max              ? 
_exptl_crystal.size_mid              ? 
_exptl_crystal.size_min              ? 
_exptl_crystal.size_rad              ? 
_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              7.5 
_exptl_crystal_grow.temp            278 
_exptl_crystal_grow.pdbx_details    
'50mM MgCl2, 0.1M Na-HEPES pH 7.5, 30% PEG MME 550, VAPOR DIFFUSION, HANGING DROP, temperature 278K' 
_exptl_crystal_grow.temp_details    ? 
_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                   MARRESEARCH 
_diffrn_detector.pdbx_collection_date   2008-09-24 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    'SAGITALLY FOCUSED Si(111)' 
_diffrn_radiation.wavelength_id                    1 
_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   0.8726 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ESRF BEAMLINE ID23-2' 
_diffrn_source.pdbx_wavelength_list        0.8726 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       ESRF 
_diffrn_source.pdbx_synchrotron_beamline   ID23-2 
# 
_reflns.entry_id                     3FXI 
_reflns.observed_criterion_sigma_F   0.0 
_reflns.observed_criterion_sigma_I   0.0 
_reflns.d_resolution_high            3.1 
_reflns.d_resolution_low             47.87 
_reflns.number_all                   44174 
_reflns.number_obs                   41586 
_reflns.percent_possible_obs         94.1 
_reflns.pdbx_Rmerge_I_obs            0.101 
_reflns.pdbx_Rsym_value              0.101 
_reflns.pdbx_netI_over_sigmaI        13.59 
_reflns.B_iso_Wilson_estimate        91.7 
_reflns.pdbx_redundancy              4.9 
_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_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             3.1 
_reflns_shell.d_res_low              3.4 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.percent_possible_all   86.5 
_reflns_shell.Rmerge_I_obs           0.481 
_reflns_shell.meanI_over_sigI_obs    3.88 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.pdbx_redundancy        5.0 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 3FXI 
_refine.B_iso_mean                               82.2 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.B_iso_max                                174.67 
_refine.B_iso_min                                35.78 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            1.00 
_refine.ls_d_res_high                            3.1 
_refine.ls_d_res_low                             47.87 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_ls_sigma_I                          0.0 
_refine.ls_number_reflns_all                     44174 
_refine.ls_number_reflns_obs                     41542 
_refine.ls_number_reflns_R_free                  2068 
_refine.ls_percent_reflns_obs                    94.1 
_refine.ls_R_factor_all                          0.241 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_work                       0.241 
_refine.ls_R_factor_R_free                       0.281 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.pdbx_data_cutoff_high_absF               2098397.30 
_refine.pdbx_data_cutoff_low_absF                0.000000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_R_free_error                 0.006 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      'PDB ENTRY 2Z65, 2Z66' 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             anisotropic 
_refine.aniso_B[1][1]                            9.72 
_refine.aniso_B[1][2]                            13.24 
_refine.aniso_B[1][3]                            -22.96 
_refine.aniso_B[2][2]                            0 
_refine.aniso_B[2][3]                            0 
_refine.aniso_B[3][3]                            0 
_refine.details                                  ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_overall_ESU_R                       ? 
_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_overall_phase_error                 ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        3FXI 
_refine_analyze.Luzzati_coordinate_error_obs    0.42 
_refine_analyze.Luzzati_sigma_a_obs             0.67 
_refine_analyze.Luzzati_d_res_low_obs           5.0 
_refine_analyze.Luzzati_coordinate_error_free   0.53 
_refine_analyze.Luzzati_sigma_a_free            0.80 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        11872 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         626 
_refine_hist.number_atoms_solvent             2 
_refine_hist.number_atoms_total               12500 
_refine_hist.d_res_high                       3.1 
_refine_hist.d_res_low                        47.87 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
c_bond_d           0.009 ? ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg        1.6   ? ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d 25.7  ? ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d 0.79  ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   6 
_refine_ls_shell.d_res_high                       3.10 
_refine_ls_shell.d_res_low                        3.29 
_refine_ls_shell.number_reflns_R_work             5872 
_refine_ls_shell.R_factor_R_work                  0.361 
_refine_ls_shell.percent_reflns_obs               85.1 
_refine_ls_shell.R_factor_R_free                  0.391 
_refine_ls_shell.R_factor_R_free_error            0.023 
_refine_ls_shell.percent_reflns_R_free            4.7 
_refine_ls_shell.number_reflns_R_free             289 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.number_reflns_obs                ? 
# 
_struct.entry_id                  3FXI 
_struct.title                     'Crystal structure of the human TLR4-human MD-2-E.coli LPS Ra complex' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            N 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3FXI 
_struct_keywords.text            
;Leucine Rich Repeat, Glycoprotein, Immune response, Inflammatory response, Innate immunity, Membrane, Receptor, Transmembrane, Secreted, IMMUNE SYSTEM
;
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM' 
# 
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 1  ? 
C  N N 2  ? 
D  N N 2  ? 
E  N N 3  ? 
F  N N 4  ? 
G  N N 4  ? 
H  N N 5  ? 
I  N N 4  ? 
J  N N 4  ? 
K  N N 6  ? 
L  N N 6  ? 
M  N N 6  ? 
N  N N 6  ? 
O  N N 7  ? 
P  N N 8  ? 
Q  N N 9  ? 
R  N N 9  ? 
S  N N 9  ? 
T  N N 9  ? 
U  N N 10 ? 
V  N N 10 ? 
W  N N 10 ? 
X  N N 11 ? 
Y  N N 6  ? 
Z  N N 6  ? 
AA N N 6  ? 
BA N N 6  ? 
CA N N 7  ? 
DA N N 8  ? 
EA N N 9  ? 
FA N N 9  ? 
GA N N 9  ? 
HA N N 9  ? 
IA N N 10 ? 
JA N N 10 ? 
KA N N 10 ? 
LA N N 11 ? 
MA N N 10 ? 
NA N N 10 ? 
OA N N 12 ? 
PA N N 12 ? 
# 
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  PRO A 142 ? SER A 146 ? PRO A 168 SER A 172 5 ? 5  
HELX_P HELX_P2  2  TYR A 165 ? ARG A 170 ? TYR A 191 ARG A 196 5 ? 6  
HELX_P HELX_P3  3  VAL A 171 ? MET A 175 ? VAL A 197 MET A 201 5 ? 5  
HELX_P HELX_P4  4  SER A 213 ? LEU A 224 ? SER A 239 LEU A 250 1 ? 12 
HELX_P HELX_P5  5  LEU A 251 ? LEU A 257 ? LEU A 277 LEU A 283 5 ? 7  
HELX_P HELX_P6  6  PHE A 278 ? THR A 282 ? PHE A 304 THR A 308 5 ? 5  
HELX_P HELX_P7  7  GLN A 367 ? GLY A 371 ? GLN A 393 GLY A 397 1 ? 5  
HELX_P HELX_P8  8  GLN A 410 ? PHE A 414 ? GLN A 436 PHE A 440 5 ? 5  
HELX_P HELX_P9  9  PHE A 457 ? PHE A 461 ? PHE A 483 PHE A 487 5 ? 5  
HELX_P HELX_P10 10 ALA A 489 ? LEU A 493 ? ALA A 515 LEU A 519 5 ? 5  
HELX_P HELX_P11 11 PHE A 512 ? LEU A 517 ? PHE A 538 LEU A 543 5 ? 6  
HELX_P HELX_P12 12 THR A 558 ? GLU A 560 ? THR A 584 GLU A 586 5 ? 3  
HELX_P HELX_P13 13 HIS A 561 ? GLN A 571 ? HIS A 587 GLN A 597 1 ? 11 
HELX_P HELX_P14 14 GLU A 577 ? MET A 581 ? GLU A 603 MET A 607 5 ? 5  
HELX_P HELX_P15 15 PRO B 142 ? ASN B 147 ? PRO B 168 ASN B 173 5 ? 6  
HELX_P HELX_P16 16 TYR B 165 ? ARG B 170 ? TYR B 191 ARG B 196 5 ? 6  
HELX_P HELX_P17 17 VAL B 171 ? MET B 175 ? VAL B 197 MET B 201 5 ? 5  
HELX_P HELX_P18 18 SER B 213 ? LEU B 224 ? SER B 239 LEU B 250 1 ? 12 
HELX_P HELX_P19 19 LEU B 251 ? LEU B 257 ? LEU B 277 LEU B 283 5 ? 7  
HELX_P HELX_P20 20 PHE B 278 ? THR B 282 ? PHE B 304 THR B 308 5 ? 5  
HELX_P HELX_P21 21 GLN B 410 ? PHE B 414 ? GLN B 436 PHE B 440 5 ? 5  
HELX_P HELX_P22 22 PHE B 457 ? PHE B 461 ? PHE B 483 PHE B 487 5 ? 5  
HELX_P HELX_P23 23 ALA B 489 ? LEU B 493 ? ALA B 515 LEU B 519 5 ? 5  
HELX_P HELX_P24 24 PHE B 512 ? LEU B 517 ? PHE B 538 LEU B 543 5 ? 6  
HELX_P HELX_P25 25 THR B 558 ? GLU B 560 ? THR B 584 GLU B 586 5 ? 3  
HELX_P HELX_P26 26 HIS B 561 ? GLN B 571 ? HIS B 587 GLN B 597 1 ? 11 
HELX_P HELX_P27 27 GLU B 577 ? MET B 581 ? GLU B 603 MET B 607 5 ? 5  
HELX_P HELX_P28 28 TYR C 84  ? ALA C 89  ? TYR C 102 ALA C 107 5 ? 6  
HELX_P HELX_P29 29 TYR D 84  ? ALA D 89  ? TYR D 102 ALA D 107 5 ? 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 3   SG  ? ? ? 1_555 A  CYS 14  SG ? ? A CYS 29   A CYS 40   1_555 ? ? ? ? ? ? ? 2.047 ? ? 
disulf2  disulf ?    ? A  CYS 255 SG  ? ? ? 1_555 A  CYS 280 SG ? ? A CYS 281  A CYS 306  1_555 ? ? ? ? ? ? ? 2.038 ? ? 
disulf3  disulf ?    ? A  CYS 364 SG  ? ? ? 1_555 A  CYS 365 SG ? ? A CYS 390  A CYS 391  1_555 ? ? ? ? ? ? ? 2.026 ? ? 
disulf4  disulf ?    ? A  CYS 557 SG  ? ? ? 1_555 A  CYS 583 SG ? ? A CYS 583  A CYS 609  1_555 ? ? ? ? ? ? ? 2.032 ? ? 
disulf5  disulf ?    ? A  CYS 559 SG  ? ? ? 1_555 A  CYS 601 SG ? ? A CYS 585  A CYS 627  1_555 ? ? ? ? ? ? ? 2.035 ? ? 
disulf6  disulf ?    ? B  CYS 3   SG  ? ? ? 1_555 B  CYS 14  SG ? ? B CYS 29   B CYS 40   1_555 ? ? ? ? ? ? ? 2.043 ? ? 
disulf7  disulf ?    ? B  CYS 255 SG  ? ? ? 1_555 B  CYS 280 SG ? ? B CYS 281  B CYS 306  1_555 ? ? ? ? ? ? ? 2.049 ? ? 
disulf8  disulf ?    ? B  CYS 364 SG  ? ? ? 1_555 B  CYS 365 SG ? ? B CYS 390  B CYS 391  1_555 ? ? ? ? ? ? ? 2.026 ? ? 
disulf9  disulf ?    ? B  CYS 557 SG  ? ? ? 1_555 B  CYS 583 SG ? ? B CYS 583  B CYS 609  1_555 ? ? ? ? ? ? ? 2.040 ? ? 
disulf10 disulf ?    ? B  CYS 559 SG  ? ? ? 1_555 B  CYS 601 SG ? ? B CYS 585  B CYS 627  1_555 ? ? ? ? ? ? ? 2.037 ? ? 
disulf11 disulf ?    ? C  CYS 7   SG  ? ? ? 1_555 C  CYS 33  SG ? ? C CYS 25   C CYS 51   1_555 ? ? ? ? ? ? ? 2.041 ? ? 
disulf12 disulf ?    ? C  CYS 19  SG  ? ? ? 1_555 C  CYS 130 SG ? ? C CYS 37   C CYS 148  1_555 ? ? ? ? ? ? ? 2.054 ? ? 
disulf13 disulf ?    ? C  CYS 77  SG  ? ? ? 1_555 C  CYS 87  SG ? ? C CYS 95   C CYS 105  1_555 ? ? ? ? ? ? ? 2.023 ? ? 
disulf14 disulf ?    ? D  CYS 7   SG  ? ? ? 1_555 D  CYS 33  SG ? ? D CYS 25   D CYS 51   1_555 ? ? ? ? ? ? ? 2.040 ? ? 
disulf15 disulf ?    ? D  CYS 19  SG  ? ? ? 1_555 D  CYS 130 SG ? ? D CYS 37   D CYS 148  1_555 ? ? ? ? ? ? ? 2.060 ? ? 
disulf16 disulf ?    ? D  CYS 77  SG  ? ? ? 1_555 D  CYS 87  SG ? ? D CYS 95   D CYS 105  1_555 ? ? ? ? ? ? ? 2.033 ? ? 
covale1  covale one  ? A  ASN 147 ND2 ? ? ? 1_555 U  NAG .   C1 ? ? A ASN 173  A NAG 711  1_555 ? ? ? ? ? ? ? 1.460 ? 
N-Glycosylation 
covale2  covale one  ? A  ASN 179 ND2 ? ? ? 1_555 V  NAG .   C1 ? ? A ASN 205  A NAG 721  1_555 ? ? ? ? ? ? ? 1.461 ? 
N-Glycosylation 
covale3  covale one  ? A  ASN 471 ND2 ? ? ? 1_555 W  NAG .   C1 ? ? A ASN 497  A NAG 741  1_555 ? ? ? ? ? ? ? 1.456 ? 
N-Glycosylation 
covale4  covale one  ? A  ASN 500 ND2 ? ? ? 1_555 F  NAG .   C1 ? ? A ASN 526  F NAG 1    1_555 ? ? ? ? ? ? ? 1.456 ? 
N-Glycosylation 
covale5  covale one  ? A  ASN 549 ND2 ? ? ? 1_555 G  NAG .   C1 ? ? A ASN 575  G NAG 1    1_555 ? ? ? ? ? ? ? 1.462 ? 
N-Glycosylation 
covale6  covale one  ? M  FTT .   O3  ? ? ? 1_555 O  DAO .   C1 ? ? A FTT 1005 A DAO 1007 1_555 ? ? ? ? ? ? ? 1.417 ? ? 
covale7  covale one  ? N  FTT .   O3  ? ? ? 1_555 P  MYR .   C1 ? ? A FTT 1006 A MYR 1008 1_555 ? ? ? ? ? ? ? 1.385 ? ? 
covale8  covale one  ? S  PO4 .   P   ? ? ? 1_555 E  GMH .   O4 ? ? A PO4 1017 E GMH 5    1_555 ? ? ? ? ? ? ? 1.490 ? ? 
covale9  covale one  ? T  PO4 .   P   ? ? ? 1_555 E  GMH .   O4 ? ? A PO4 1018 E GMH 4    1_555 ? ? ? ? ? ? ? 1.489 ? ? 
covale10 covale one  ? B  ASN 147 ND2 ? ? ? 1_555 IA NAG .   C1 ? ? B ASN 173  B NAG 811  1_555 ? ? ? ? ? ? ? 1.460 ? 
N-Glycosylation 
covale11 covale one  ? B  ASN 179 ND2 ? ? ? 1_555 JA NAG .   C1 ? ? B ASN 205  B NAG 821  1_555 ? ? ? ? ? ? ? 1.457 ? 
N-Glycosylation 
covale12 covale one  ? B  ASN 471 ND2 ? ? ? 1_555 KA NAG .   C1 ? ? B ASN 497  B NAG 841  1_555 ? ? ? ? ? ? ? 1.483 ? 
N-Glycosylation 
covale13 covale one  ? B  ASN 500 ND2 ? ? ? 1_555 I  NAG .   C1 ? ? B ASN 526  I NAG 1    1_555 ? ? ? ? ? ? ? 1.454 ? 
N-Glycosylation 
covale14 covale one  ? B  ASN 549 ND2 ? ? ? 1_555 J  NAG .   C1 ? ? B ASN 575  J NAG 1    1_555 ? ? ? ? ? ? ? 1.460 ? 
N-Glycosylation 
covale15 covale one  ? AA FTT .   O3  ? ? ? 1_555 CA DAO .   C1 ? ? B FTT 1005 B DAO 1007 1_555 ? ? ? ? ? ? ? 1.413 ? ? 
covale16 covale one  ? BA FTT .   O3  ? ? ? 1_555 DA MYR .   C1 ? ? B FTT 1006 B MYR 1008 1_555 ? ? ? ? ? ? ? 1.385 ? ? 
covale17 covale one  ? GA PO4 .   P   ? ? ? 1_555 H  GMH .   O4 ? ? B PO4 1017 H GMH 5    1_555 ? ? ? ? ? ? ? 1.486 ? ? 
covale18 covale one  ? HA PO4 .   P   ? ? ? 1_555 H  GMH .   O4 ? ? B PO4 1018 H GMH 4    1_555 ? ? ? ? ? ? ? 1.488 ? ? 
covale19 covale one  ? C  ASN 96  ND2 ? ? ? 1_555 MA NAG .   C1 ? ? C ASN 114  C NAG 751  1_555 ? ? ? ? ? ? ? 1.455 ? 
N-Glycosylation 
covale20 covale one  ? D  ASN 96  ND2 ? ? ? 1_555 NA NAG .   C1 ? ? D ASN 114  D NAG 851  1_555 ? ? ? ? ? ? ? 1.451 ? 
N-Glycosylation 
covale21 covale both ? E  PA1 .   O6  ? ? ? 1_555 E  PA1 .   C1 ? ? E PA1 1    E PA1 2    1_555 ? ? ? ? ? ? ? 1.427 ? ? 
covale22 covale both ? E  PA1 .   O6  ? ? ? 1_555 E  KDO .   C2 ? ? E PA1 2    E KDO 3    1_555 ? ? ? ? ? ? ? 1.424 ? ? 
covale23 covale both ? E  KDO .   O5  ? ? ? 1_555 E  GMH .   C1 ? ? E KDO 3    E GMH 4    1_555 ? ? ? ? ? ? ? 1.416 ? ? 
covale24 covale both ? E  KDO .   O4  ? ? ? 1_555 E  KDO .   C2 ? ? E KDO 3    E KDO 7    1_555 ? ? ? ? ? ? ? 1.482 ? ? 
covale25 covale both ? E  GMH .   O3  ? ? ? 1_555 E  GMH .   C1 ? ? E GMH 4    E GMH 5    1_555 ? ? ? ? ? ? ? 1.429 ? ? 
covale26 covale both ? E  GMH .   O7  ? ? ? 1_555 E  GMH .   C1 ? ? E GMH 5    E GMH 6    1_555 ? ? ? ? ? ? ? 1.421 ? ? 
covale27 covale both ? F  NAG .   O4  ? ? ? 1_555 F  NAG .   C1 ? ? F NAG 1    F NAG 2    1_555 ? ? ? ? ? ? ? 1.412 ? ? 
covale28 covale both ? G  NAG .   O4  ? ? ? 1_555 G  NAG .   C1 ? ? G NAG 1    G NAG 2    1_555 ? ? ? ? ? ? ? 1.400 ? ? 
covale29 covale both ? H  PA1 .   O6  ? ? ? 1_555 H  GCS .   C1 ? ? H PA1 1    H GCS 2    1_555 ? ? ? ? ? ? ? 1.427 ? ? 
covale30 covale both ? H  GCS .   O6  ? ? ? 1_555 H  KDO .   C2 ? ? H GCS 2    H KDO 3    1_555 ? ? ? ? ? ? ? 1.423 ? ? 
covale31 covale both ? H  KDO .   O5  ? ? ? 1_555 H  GMH .   C1 ? ? H KDO 3    H GMH 4    1_555 ? ? ? ? ? ? ? 1.421 ? ? 
covale32 covale both ? H  KDO .   O4  ? ? ? 1_555 H  KDO .   C2 ? ? H KDO 3    H KDO 7    1_555 ? ? ? ? ? ? ? 1.485 ? ? 
covale33 covale both ? H  GMH .   O3  ? ? ? 1_555 H  GMH .   C1 ? ? H GMH 4    H GMH 5    1_555 ? ? ? ? ? ? ? 1.429 ? ? 
covale34 covale both ? H  GMH .   O7  ? ? ? 1_555 H  GMH .   C1 ? ? H GMH 5    H GMH 6    1_555 ? ? ? ? ? ? ? 1.420 ? ? 
covale35 covale both ? I  NAG .   O4  ? ? ? 1_555 I  NAG .   C1 ? ? I NAG 1    I NAG 2    1_555 ? ? ? ? ? ? ? 1.385 ? ? 
covale36 covale both ? J  NAG .   O4  ? ? ? 1_555 J  NAG .   C1 ? ? J NAG 1    J NAG 2    1_555 ? ? ? ? ? ? ? 1.399 ? ? 
metalc1  metalc ?    ? OA HOH .   O   ? ? ? 1_555 X  MG  .   MG ? ? A HOH 1    A MG  2001 1_555 ? ? ? ? ? ? ? 2.896 ? ? 
metalc2  metalc ?    ? A  ASP 268 OD2 ? ? ? 1_555 X  MG  .   MG ? ? A ASP 294  A MG  2001 1_555 ? ? ? ? ? ? ? 2.961 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
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 CYS 364 A . ? CYS 390 A CYS 365 A ? CYS 391 A 1 -4.06 
2 CYS 364 B . ? CYS 390 B CYS 365 B ? CYS 391 B 1 -4.06 
3 ASN 31  C . ? ASN 49  C PRO 32  C ? PRO 50  C 1 0.10  
4 ASN 31  D . ? ASN 49  D PRO 32  D ? PRO 50  D 1 -0.25 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 19 ? 
B ? 2  ? 
C ? 2  ? 
D ? 3  ? 
E ? 19 ? 
F ? 2  ? 
G ? 2  ? 
H ? 3  ? 
I ? 6  ? 
J ? 6  ? 
K ? 3  ? 
L ? 6  ? 
M ? 6  ? 
N ? 3  ? 
# 
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  ? parallel      
A 3  4  ? parallel      
A 4  5  ? parallel      
A 5  6  ? parallel      
A 6  7  ? parallel      
A 7  8  ? parallel      
A 8  9  ? parallel      
A 9  10 ? parallel      
A 10 11 ? parallel      
A 11 12 ? parallel      
A 12 13 ? parallel      
A 13 14 ? parallel      
A 14 15 ? parallel      
A 15 16 ? parallel      
A 16 17 ? parallel      
A 17 18 ? parallel      
A 18 19 ? parallel      
B 1  2  ? parallel      
C 1  2  ? parallel      
D 1  2  ? parallel      
D 2  3  ? parallel      
E 1  2  ? anti-parallel 
E 2  3  ? parallel      
E 3  4  ? parallel      
E 4  5  ? parallel      
E 5  6  ? parallel      
E 6  7  ? parallel      
E 7  8  ? parallel      
E 8  9  ? parallel      
E 9  10 ? parallel      
E 10 11 ? parallel      
E 11 12 ? parallel      
E 12 13 ? parallel      
E 13 14 ? parallel      
E 14 15 ? parallel      
E 15 16 ? parallel      
E 16 17 ? parallel      
E 17 18 ? parallel      
E 18 19 ? parallel      
F 1  2  ? parallel      
G 1  2  ? parallel      
H 1  2  ? parallel      
H 2  3  ? parallel      
I 1  2  ? anti-parallel 
I 2  3  ? anti-parallel 
I 3  4  ? anti-parallel 
I 4  5  ? anti-parallel 
I 5  6  ? anti-parallel 
J 1  2  ? anti-parallel 
J 2  3  ? anti-parallel 
J 3  4  ? anti-parallel 
J 4  5  ? anti-parallel 
J 5  6  ? anti-parallel 
K 1  2  ? anti-parallel 
K 2  3  ? anti-parallel 
L 1  2  ? anti-parallel 
L 2  3  ? anti-parallel 
L 3  4  ? anti-parallel 
L 4  5  ? anti-parallel 
L 5  6  ? anti-parallel 
M 1  2  ? anti-parallel 
M 2  3  ? anti-parallel 
M 3  4  ? anti-parallel 
M 4  5  ? anti-parallel 
M 5  6  ? anti-parallel 
N 1  2  ? anti-parallel 
N 2  3  ? 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  VAL A 4   ? VAL A 7   ? VAL A 30  VAL A 33  
A 2  THR A 11  ? GLN A 13  ? THR A 37  GLN A 39  
A 3  ASN A 32  ? ASP A 34  ? ASN A 58  ASP A 60  
A 4  VAL A 56  ? ASP A 58  ? VAL A 82  ASP A 84  
A 5  THR A 80  ? ILE A 82  ? THR A 106 ILE A 108 
A 6  LYS A 104 ? VAL A 106 ? LYS A 130 VAL A 132 
A 7  GLU A 128 ? ASN A 130 ? GLU A 154 ASN A 156 
A 8  HIS A 153 ? ASP A 155 ? HIS A 179 ASP A 181 
A 9  SER A 181 ? ASP A 183 ? SER A 207 ASP A 209 
A 10 ARG A 201 ? ARG A 208 ? ARG A 227 ARG A 234 
A 11 GLU A 228 ? GLY A 235 ? GLU A 254 GLY A 261 
A 12 THR A 258 ? LEU A 267 ? THR A 284 LEU A 293 
A 13 SER A 286 ? VAL A 292 ? SER A 312 VAL A 318 
A 14 HIS A 308 ? VAL A 312 ? HIS A 334 VAL A 338 
A 15 ARG A 329 ? THR A 333 ? ARG A 355 THR A 359 
A 16 PHE A 351 ? ASP A 353 ? PHE A 377 ASP A 379 
A 17 TYR A 377 ? ASP A 379 ? TYR A 403 ASP A 405 
A 18 HIS A 400 ? ASP A 402 ? HIS A 426 ASP A 428 
A 19 TYR A 425 ? ASP A 427 ? TYR A 451 ASP A 453 
B 1  THR A 66  ? ILE A 67  ? THR A 92  ILE A 93  
B 2  SER A 90  ? LEU A 91  ? SER A 116 LEU A 117 
C 1  SER A 163 ? ILE A 164 ? SER A 189 ILE A 190 
C 2  PHE A 191 ? ILE A 192 ? PHE A 217 ILE A 218 
D 1  PHE A 361 ? SER A 366 ? PHE A 387 SER A 392 
D 2  VAL A 385 ? LEU A 393 ? VAL A 411 LEU A 419 
D 3  ASN A 407 ? LYS A 409 ? ASN A 433 LYS A 435 
E 1  VAL B 4   ? VAL B 7   ? VAL B 30  VAL B 33  
E 2  THR B 11  ? GLN B 13  ? THR B 37  GLN B 39  
E 3  ASN B 32  ? ASP B 34  ? ASN B 58  ASP B 60  
E 4  VAL B 56  ? ASP B 58  ? VAL B 82  ASP B 84  
E 5  THR B 80  ? ILE B 82  ? THR B 106 ILE B 108 
E 6  LYS B 104 ? VAL B 106 ? LYS B 130 VAL B 132 
E 7  GLU B 128 ? ASN B 130 ? GLU B 154 ASN B 156 
E 8  HIS B 153 ? ASP B 155 ? HIS B 179 ASP B 181 
E 9  SER B 181 ? ASP B 183 ? SER B 207 ASP B 209 
E 10 ARG B 201 ? ARG B 208 ? ARG B 227 ARG B 234 
E 11 GLU B 228 ? GLY B 235 ? GLU B 254 GLY B 261 
E 12 THR B 258 ? LEU B 267 ? THR B 284 LEU B 293 
E 13 SER B 286 ? VAL B 292 ? SER B 312 VAL B 318 
E 14 HIS B 308 ? VAL B 312 ? HIS B 334 VAL B 338 
E 15 ARG B 329 ? THR B 333 ? ARG B 355 THR B 359 
E 16 PHE B 351 ? ASP B 353 ? PHE B 377 ASP B 379 
E 17 TYR B 377 ? ASP B 379 ? TYR B 403 ASP B 405 
E 18 HIS B 400 ? ASP B 402 ? HIS B 426 ASP B 428 
E 19 TYR B 425 ? ASP B 427 ? TYR B 451 ASP B 453 
F 1  THR B 66  ? ILE B 67  ? THR B 92  ILE B 93  
F 2  SER B 90  ? LEU B 91  ? SER B 116 LEU B 117 
G 1  SER B 163 ? ILE B 164 ? SER B 189 ILE B 190 
G 2  PHE B 191 ? ILE B 192 ? PHE B 217 ILE B 218 
H 1  PHE B 361 ? SER B 366 ? PHE B 387 SER B 392 
H 2  VAL B 385 ? LEU B 393 ? VAL B 411 LEU B 419 
H 3  ASN B 407 ? LYS B 409 ? ASN B 433 LYS B 435 
I 1  TYR C 4   ? ASN C 8   ? TYR C 22  ASN C 26  
I 2  ALA C 12  ? TYR C 18  ? ALA C 30  TYR C 36  
I 3  GLU C 126 ? HIS C 137 ? GLU C 144 HIS C 155 
I 4  GLY C 111 ? SER C 121 ? GLY C 129 SER C 139 
I 5  TYR C 57  ? VAL C 64  ? TYR C 75  VAL C 82  
I 6  MET C 67  ? ASN C 68  ? MET C 85  ASN C 86  
J 1  TYR C 4   ? ASN C 8   ? TYR C 22  ASN C 26  
J 2  ALA C 12  ? TYR C 18  ? ALA C 30  TYR C 36  
J 3  GLU C 126 ? HIS C 137 ? GLU C 144 HIS C 155 
J 4  GLY C 111 ? SER C 121 ? GLY C 129 SER C 139 
J 5  TYR C 57  ? VAL C 64  ? TYR C 75  VAL C 82  
J 6  ARG C 72  ? VAL C 75  ? ARG C 90  VAL C 93  
K 1  SER C 27  ? ASN C 31  ? SER C 45  ASN C 49  
K 2  LEU C 42  ? TYR C 47  ? LEU C 60  TYR C 65  
K 3  VAL C 95  ? SER C 100 ? VAL C 113 SER C 118 
L 1  TYR D 4   ? ASN D 8   ? TYR D 22  ASN D 26  
L 2  ALA D 12  ? TYR D 18  ? ALA D 30  TYR D 36  
L 3  GLU D 126 ? HIS D 137 ? GLU D 144 HIS D 155 
L 4  GLY D 111 ? SER D 121 ? GLY D 129 SER D 139 
L 5  TYR D 57  ? VAL D 64  ? TYR D 75  VAL D 82  
L 6  MET D 67  ? ASN D 68  ? MET D 85  ASN D 86  
M 1  TYR D 4   ? ASN D 8   ? TYR D 22  ASN D 26  
M 2  ALA D 12  ? TYR D 18  ? ALA D 30  TYR D 36  
M 3  GLU D 126 ? HIS D 137 ? GLU D 144 HIS D 155 
M 4  GLY D 111 ? SER D 121 ? GLY D 129 SER D 139 
M 5  TYR D 57  ? VAL D 64  ? TYR D 75  VAL D 82  
M 6  ARG D 72  ? VAL D 75  ? ARG D 90  VAL D 93  
N 1  SER D 27  ? ASN D 31  ? SER D 45  ASN D 49  
N 2  LEU D 42  ? TYR D 47  ? LEU D 60  TYR D 65  
N 3  VAL D 95  ? SER D 100 ? VAL D 113 SER D 118 
# 
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 VAL A 7   ? N VAL A 33  O THR A 11  ? O THR A 37  
A 2  3  N TYR A 12  ? N TYR A 38  O ASN A 32  ? O ASN A 58  
A 3  4  N LEU A 33  ? N LEU A 59  O VAL A 56  ? O VAL A 82  
A 4  5  N LEU A 57  ? N LEU A 83  O THR A 80  ? O THR A 106 
A 5  6  N LEU A 81  ? N LEU A 107 O VAL A 106 ? O VAL A 132 
A 6  7  N LEU A 105 ? N LEU A 131 O ASN A 130 ? O ASN A 156 
A 7  8  N LEU A 129 ? N LEU A 155 O HIS A 153 ? O HIS A 179 
A 8  9  N LEU A 154 ? N LEU A 180 O SER A 181 ? O SER A 207 
A 9  10 N LEU A 182 ? N LEU A 208 O LYS A 204 ? O LYS A 230 
A 10 11 N LEU A 205 ? N LEU A 231 O VAL A 233 ? O VAL A 259 
A 11 12 N LEU A 234 ? N LEU A 260 O ALA A 265 ? O ALA A 291 
A 12 13 N PHE A 262 ? N PHE A 288 O SER A 286 ? O SER A 312 
A 13 14 N PHE A 287 ? N PHE A 313 O HIS A 308 ? O HIS A 334 
A 14 15 N LEU A 309 ? N LEU A 335 O THR A 331 ? O THR A 357 
A 15 16 N PHE A 332 ? N PHE A 358 O ASP A 353 ? O ASP A 379 
A 16 17 N LEU A 352 ? N LEU A 378 O ASP A 379 ? O ASP A 405 
A 17 18 N LEU A 378 ? N LEU A 404 O ASP A 402 ? O ASP A 428 
A 18 19 N LEU A 401 ? N LEU A 427 O ASP A 427 ? O ASP A 453 
B 1  2  N ILE A 67  ? N ILE A 93  O SER A 90  ? O SER A 116 
C 1  2  N ILE A 164 ? N ILE A 190 O PHE A 191 ? O PHE A 217 
D 1  2  N CYS A 364 ? N CYS A 390 O SER A 389 ? O SER A 415 
D 2  3  N ILE A 386 ? N ILE A 412 O ASN A 407 ? O ASN A 433 
E 1  2  N VAL B 7   ? N VAL B 33  O THR B 11  ? O THR B 37  
E 2  3  N TYR B 12  ? N TYR B 38  O ASN B 32  ? O ASN B 58  
E 3  4  N LEU B 33  ? N LEU B 59  O VAL B 56  ? O VAL B 82  
E 4  5  N LEU B 57  ? N LEU B 83  O THR B 80  ? O THR B 106 
E 5  6  N LEU B 81  ? N LEU B 107 O VAL B 106 ? O VAL B 132 
E 6  7  N LEU B 105 ? N LEU B 131 O ASN B 130 ? O ASN B 156 
E 7  8  N LEU B 129 ? N LEU B 155 O HIS B 153 ? O HIS B 179 
E 8  9  N LEU B 154 ? N LEU B 180 O SER B 181 ? O SER B 207 
E 9  10 N LEU B 182 ? N LEU B 208 O LYS B 204 ? O LYS B 230 
E 10 11 N LEU B 205 ? N LEU B 231 O VAL B 233 ? O VAL B 259 
E 11 12 N LEU B 234 ? N LEU B 260 O ALA B 265 ? O ALA B 291 
E 12 13 N PHE B 262 ? N PHE B 288 O SER B 286 ? O SER B 312 
E 13 14 N PHE B 287 ? N PHE B 313 O HIS B 308 ? O HIS B 334 
E 14 15 N LEU B 311 ? N LEU B 337 O THR B 331 ? O THR B 357 
E 15 16 N PHE B 332 ? N PHE B 358 O ASP B 353 ? O ASP B 379 
E 16 17 N LEU B 352 ? N LEU B 378 O ASP B 379 ? O ASP B 405 
E 17 18 N LEU B 378 ? N LEU B 404 O ASP B 402 ? O ASP B 428 
E 18 19 N LEU B 401 ? N LEU B 427 O ASP B 427 ? O ASP B 453 
F 1  2  N ILE B 67  ? N ILE B 93  O SER B 90  ? O SER B 116 
G 1  2  N ILE B 164 ? N ILE B 190 O PHE B 191 ? O PHE B 217 
H 1  2  N CYS B 364 ? N CYS B 390 O SER B 389 ? O SER B 415 
H 2  3  N MET B 388 ? N MET B 414 O LYS B 409 ? O LYS B 435 
I 1  2  N CYS C 7   ? N CYS C 25  O ILE C 14  ? O ILE C 32  
I 2  3  N SER C 15  ? N SER C 33  O VAL C 134 ? O VAL C 152 
I 3  4  O ILE C 135 ? O ILE C 153 N TYR C 113 ? N TYR C 131 
I 4  5  O VAL C 116 ? O VAL C 134 N TYR C 61  ? N TYR C 79  
I 5  6  N VAL C 64  ? N VAL C 82  O MET C 67  ? O MET C 85  
J 1  2  N CYS C 7   ? N CYS C 25  O ILE C 14  ? O ILE C 32  
J 2  3  N SER C 15  ? N SER C 33  O VAL C 134 ? O VAL C 152 
J 3  4  O ILE C 135 ? O ILE C 153 N TYR C 113 ? N TYR C 131 
J 4  5  O VAL C 116 ? O VAL C 134 N TYR C 61  ? N TYR C 79  
J 5  6  N LEU C 60  ? N LEU C 78  O ARG C 72  ? O ARG C 90  
K 1  2  N ASN C 31  ? N ASN C 49  O LEU C 42  ? O LEU C 60  
K 2  3  N LEU C 43  ? N LEU C 61  O ILE C 99  ? O ILE C 117 
L 1  2  N CYS D 7   ? N CYS D 25  O ILE D 14  ? O ILE D 32  
L 2  3  N SER D 15  ? N SER D 33  O VAL D 134 ? O VAL D 152 
L 3  4  O PHE D 129 ? O PHE D 147 N ALA D 119 ? N ALA D 137 
L 4  5  O VAL D 116 ? O VAL D 134 N TYR D 61  ? N TYR D 79  
L 5  6  N VAL D 64  ? N VAL D 82  O MET D 67  ? O MET D 85  
M 1  2  N CYS D 7   ? N CYS D 25  O ILE D 14  ? O ILE D 32  
M 2  3  N SER D 15  ? N SER D 33  O VAL D 134 ? O VAL D 152 
M 3  4  O PHE D 129 ? O PHE D 147 N ALA D 119 ? N ALA D 137 
M 4  5  O VAL D 116 ? O VAL D 134 N TYR D 61  ? N TYR D 79  
M 5  6  N LEU D 60  ? N LEU D 78  O ARG D 72  ? O ARG D 90  
N 1  2  N ASN D 31  ? N ASN D 49  O LEU D 42  ? O LEU D 60  
N 2  3  N LEU D 43  ? N LEU D 61  O ILE D 99  ? O ILE D 117 
# 
_database_PDB_matrix.entry_id          3FXI 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.000000 
_database_PDB_matrix.origx_vector[2]   0.000000 
_database_PDB_matrix.origx_vector[3]   0.000000 
# 
_atom_sites.entry_id                    3FXI 
_atom_sites.fract_transf_matrix[1][1]   0.010970 
_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]   0.009662 
_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]   0.003971 
_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  
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . GLU A  1  1   ? 20.646  27.674  43.260  1.00 116.72 ? 27   GLU A N   1 
ATOM   2     C  CA  . GLU A  1  1   ? 19.751  26.838  42.401  1.00 116.02 ? 27   GLU A CA  1 
ATOM   3     C  C   . GLU A  1  1   ? 20.496  26.310  41.177  1.00 114.77 ? 27   GLU A C   1 
ATOM   4     O  O   . GLU A  1  1   ? 20.032  26.490  40.051  1.00 114.91 ? 27   GLU A O   1 
ATOM   5     C  CB  . GLU A  1  1   ? 18.549  27.657  41.908  1.00 116.16 ? 27   GLU A CB  1 
ATOM   6     C  CG  . GLU A  1  1   ? 17.771  28.389  42.982  1.00 116.64 ? 27   GLU A CG  1 
ATOM   7     C  CD  . GLU A  1  1   ? 16.735  29.310  42.387  1.00 117.36 ? 27   GLU A CD  1 
ATOM   8     O  OE1 . GLU A  1  1   ? 15.853  28.808  41.657  1.00 117.01 ? 27   GLU A OE1 1 
ATOM   9     O  OE2 . GLU A  1  1   ? 16.809  30.532  42.640  1.00 117.72 ? 27   GLU A OE2 1 
ATOM   10    N  N   . PRO A  1  2   ? 21.657  25.656  41.369  1.00 113.02 ? 28   PRO A N   1 
ATOM   11    C  CA  . PRO A  1  2   ? 22.327  25.170  40.161  1.00 111.52 ? 28   PRO A CA  1 
ATOM   12    C  C   . PRO A  1  2   ? 21.456  24.129  39.456  1.00 110.23 ? 28   PRO A C   1 
ATOM   13    O  O   . PRO A  1  2   ? 21.822  23.608  38.406  1.00 110.05 ? 28   PRO A O   1 
ATOM   14    C  CB  . PRO A  1  2   ? 23.650  24.609  40.700  1.00 111.00 ? 28   PRO A CB  1 
ATOM   15    C  CG  . PRO A  1  2   ? 23.303  24.169  42.075  1.00 111.38 ? 28   PRO A CG  1 
ATOM   16    C  CD  . PRO A  1  2   ? 22.403  25.274  42.581  1.00 112.40 ? 28   PRO A CD  1 
ATOM   17    N  N   . CYS A  1  3   ? 20.291  23.856  40.043  1.00 109.12 ? 29   CYS A N   1 
ATOM   18    C  CA  . CYS A  1  3   ? 19.330  22.892  39.511  1.00 108.16 ? 29   CYS A CA  1 
ATOM   19    C  C   . CYS A  1  3   ? 18.803  23.332  38.153  1.00 107.41 ? 29   CYS A C   1 
ATOM   20    O  O   . CYS A  1  3   ? 19.057  24.455  37.711  1.00 107.26 ? 29   CYS A O   1 
ATOM   21    C  CB  . CYS A  1  3   ? 18.124  22.745  40.451  1.00 108.18 ? 29   CYS A CB  1 
ATOM   22    S  SG  . CYS A  1  3   ? 18.428  22.182  42.162  1.00 109.07 ? 29   CYS A SG  1 
ATOM   23    N  N   . VAL A  1  4   ? 18.055  22.441  37.504  1.00 106.14 ? 30   VAL A N   1 
ATOM   24    C  CA  . VAL A  1  4   ? 17.453  22.729  36.209  1.00 104.49 ? 30   VAL A CA  1 
ATOM   25    C  C   . VAL A  1  4   ? 15.951  22.745  36.420  1.00 104.66 ? 30   VAL A C   1 
ATOM   26    O  O   . VAL A  1  4   ? 15.378  21.774  36.902  1.00 104.45 ? 30   VAL A O   1 
ATOM   27    C  CB  . VAL A  1  4   ? 17.795  21.658  35.156  1.00 103.08 ? 30   VAL A CB  1 
ATOM   28    C  CG1 . VAL A  1  4   ? 17.066  21.958  33.870  1.00 102.33 ? 30   VAL A CG1 1 
ATOM   29    C  CG2 . VAL A  1  4   ? 19.286  21.624  34.904  1.00 102.37 ? 30   VAL A CG2 1 
ATOM   30    N  N   . GLU A  1  5   ? 15.329  23.863  36.076  1.00 105.13 ? 31   GLU A N   1 
ATOM   31    C  CA  . GLU A  1  5   ? 13.888  24.042  36.225  1.00 105.72 ? 31   GLU A CA  1 
ATOM   32    C  C   . GLU A  1  5   ? 13.204  23.567  34.942  1.00 106.01 ? 31   GLU A C   1 
ATOM   33    O  O   . GLU A  1  5   ? 13.121  24.313  33.969  1.00 106.78 ? 31   GLU A O   1 
ATOM   34    C  CB  . GLU A  1  5   ? 13.598  25.530  36.475  1.00 106.23 ? 31   GLU A CB  1 
ATOM   35    C  CG  . GLU A  1  5   ? 12.132  25.934  36.566  1.00 107.20 ? 31   GLU A CG  1 
ATOM   36    C  CD  . GLU A  1  5   ? 11.949  27.451  36.587  1.00 107.21 ? 31   GLU A CD  1 
ATOM   37    O  OE1 . GLU A  1  5   ? 12.503  28.107  37.497  1.00 106.22 ? 31   GLU A OE1 1 
ATOM   38    O  OE2 . GLU A  1  5   ? 11.256  27.985  35.690  1.00 107.18 ? 31   GLU A OE2 1 
ATOM   39    N  N   . VAL A  1  6   ? 12.721  22.326  34.936  1.00 106.15 ? 32   VAL A N   1 
ATOM   40    C  CA  . VAL A  1  6   ? 12.065  21.771  33.749  1.00 105.62 ? 32   VAL A CA  1 
ATOM   41    C  C   . VAL A  1  6   ? 10.670  22.353  33.535  1.00 105.97 ? 32   VAL A C   1 
ATOM   42    O  O   . VAL A  1  6   ? 10.343  22.815  32.444  1.00 106.63 ? 32   VAL A O   1 
ATOM   43    C  CB  . VAL A  1  6   ? 11.955  20.237  33.833  1.00 104.66 ? 32   VAL A CB  1 
ATOM   44    C  CG1 . VAL A  1  6   ? 11.384  19.698  32.541  1.00 104.14 ? 32   VAL A CG1 1 
ATOM   45    C  CG2 . VAL A  1  6   ? 13.323  19.630  34.103  1.00 103.42 ? 32   VAL A CG2 1 
ATOM   46    N  N   . VAL A  1  7   ? 9.847   22.311  34.577  1.00 105.71 ? 33   VAL A N   1 
ATOM   47    C  CA  . VAL A  1  7   ? 8.498   22.858  34.516  1.00 105.62 ? 33   VAL A CA  1 
ATOM   48    C  C   . VAL A  1  7   ? 8.378   23.799  35.707  1.00 106.99 ? 33   VAL A C   1 
ATOM   49    O  O   . VAL A  1  7   ? 8.196   23.354  36.842  1.00 107.18 ? 33   VAL A O   1 
ATOM   50    C  CB  . VAL A  1  7   ? 7.444   21.759  34.649  1.00 104.32 ? 33   VAL A CB  1 
ATOM   51    C  CG1 . VAL A  1  7   ? 6.072   22.324  34.356  1.00 103.31 ? 33   VAL A CG1 1 
ATOM   52    C  CG2 . VAL A  1  7   ? 7.771   20.618  33.713  1.00 103.87 ? 33   VAL A CG2 1 
ATOM   53    N  N   . PRO A  1  8   ? 8.464   25.120  35.467  1.00 107.87 ? 34   PRO A N   1 
ATOM   54    C  CA  . PRO A  1  8   ? 8.369   26.095  36.558  1.00 107.66 ? 34   PRO A CA  1 
ATOM   55    C  C   . PRO A  1  8   ? 7.298   25.796  37.602  1.00 108.07 ? 34   PRO A C   1 
ATOM   56    O  O   . PRO A  1  8   ? 6.195   25.358  37.276  1.00 107.55 ? 34   PRO A O   1 
ATOM   57    C  CB  . PRO A  1  8   ? 8.145   27.423  35.823  1.00 107.56 ? 34   PRO A CB  1 
ATOM   58    C  CG  . PRO A  1  8   ? 7.530   27.012  34.518  1.00 108.09 ? 34   PRO A CG  1 
ATOM   59    C  CD  . PRO A  1  8   ? 8.343   25.793  34.161  1.00 108.22 ? 34   PRO A CD  1 
ATOM   60    N  N   . ASN A  1  9   ? 7.649   26.034  38.863  1.00 109.23 ? 35   ASN A N   1 
ATOM   61    C  CA  . ASN A  1  9   ? 6.754   25.801  39.997  1.00 110.45 ? 35   ASN A CA  1 
ATOM   62    C  C   . ASN A  1  9   ? 6.269   24.337  40.066  1.00 109.16 ? 35   ASN A C   1 
ATOM   63    O  O   . ASN A  1  9   ? 5.472   23.995  40.935  1.00 108.65 ? 35   ASN A O   1 
ATOM   64    C  CB  . ASN A  1  9   ? 5.536   26.779  39.953  1.00 113.58 ? 35   ASN A CB  1 
ATOM   65    C  CG  . ASN A  1  9   ? 5.843   28.179  40.567  1.00 117.59 ? 35   ASN A CG  1 
ATOM   66    O  OD1 . ASN A  1  9   ? 6.730   28.291  41.419  1.00 117.54 ? 35   ASN A OD1 1 
ATOM   67    N  ND2 . ASN A  1  9   ? 5.099   29.226  40.173  1.00 122.09 ? 35   ASN A ND2 1 
ATOM   68    N  N   . ILE A  1  10  ? 6.768   23.468  39.182  1.00 107.76 ? 36   ILE A N   1 
ATOM   69    C  CA  . ILE A  1  10  ? 6.318   22.067  39.168  1.00 106.41 ? 36   ILE A CA  1 
ATOM   70    C  C   . ILE A  1  10  ? 7.366   20.930  39.159  1.00 105.49 ? 36   ILE A C   1 
ATOM   71    O  O   . ILE A  1  10  ? 7.290   20.026  39.995  1.00 105.28 ? 36   ILE A O   1 
ATOM   72    C  CB  . ILE A  1  10  ? 5.367   21.810  37.974  1.00 106.65 ? 36   ILE A CB  1 
ATOM   73    C  CG1 . ILE A  1  10  ? 4.290   22.896  37.901  1.00 106.94 ? 36   ILE A CG1 1 
ATOM   74    C  CG2 . ILE A  1  10  ? 4.701   20.450  38.130  1.00 106.77 ? 36   ILE A CG2 1 
ATOM   75    C  CD1 . ILE A  1  10  ? 3.291   22.861  39.037  1.00 106.85 ? 36   ILE A CD1 1 
ATOM   76    N  N   . THR A  1  11  ? 8.317   20.952  38.219  1.00 104.43 ? 37   THR A N   1 
ATOM   77    C  CA  . THR A  1  11  ? 9.342   19.891  38.122  1.00 102.98 ? 37   THR A CA  1 
ATOM   78    C  C   . THR A  1  11  ? 10.807  20.359  38.048  1.00 102.37 ? 37   THR A C   1 
ATOM   79    O  O   . THR A  1  11  ? 11.183  21.109  37.147  1.00 101.20 ? 37   THR A O   1 
ATOM   80    C  CB  . THR A  1  11  ? 9.095   18.985  36.889  1.00 102.72 ? 37   THR A CB  1 
ATOM   81    O  OG1 . THR A  1  11  ? 7.763   18.462  36.930  1.00 102.29 ? 37   THR A OG1 1 
ATOM   82    C  CG2 . THR A  1  11  ? 10.080  17.827  36.874  1.00 101.76 ? 37   THR A CG2 1 
ATOM   83    N  N   . TYR A  1  12  ? 11.630  19.889  38.987  1.00 102.56 ? 38   TYR A N   1 
ATOM   84    C  CA  . TYR A  1  12  ? 13.054  20.243  39.046  1.00 102.75 ? 38   TYR A CA  1 
ATOM   85    C  C   . TYR A  1  12  ? 13.976  19.019  39.069  1.00 102.51 ? 38   TYR A C   1 
ATOM   86    O  O   . TYR A  1  12  ? 13.726  18.057  39.800  1.00 102.00 ? 38   TYR A O   1 
ATOM   87    C  CB  . TYR A  1  12  ? 13.349  21.113  40.287  1.00 102.87 ? 38   TYR A CB  1 
ATOM   88    C  CG  . TYR A  1  12  ? 12.586  22.424  40.317  1.00 103.50 ? 38   TYR A CG  1 
ATOM   89    C  CD1 . TYR A  1  12  ? 11.271  22.480  40.787  1.00 103.60 ? 38   TYR A CD1 1 
ATOM   90    C  CD2 . TYR A  1  12  ? 13.144  23.591  39.786  1.00 103.60 ? 38   TYR A CD2 1 
ATOM   91    C  CE1 . TYR A  1  12  ? 10.531  23.655  40.717  1.00 103.70 ? 38   TYR A CE1 1 
ATOM   92    C  CE2 . TYR A  1  12  ? 12.411  24.770  39.711  1.00 103.32 ? 38   TYR A CE2 1 
ATOM   93    C  CZ  . TYR A  1  12  ? 11.105  24.793  40.174  1.00 103.87 ? 38   TYR A CZ  1 
ATOM   94    O  OH  . TYR A  1  12  ? 10.355  25.940  40.056  1.00 104.67 ? 38   TYR A OH  1 
ATOM   95    N  N   . GLN A  1  13  ? 15.043  19.069  38.271  1.00 102.35 ? 39   GLN A N   1 
ATOM   96    C  CA  . GLN A  1  13  ? 16.012  17.978  38.207  1.00 102.12 ? 39   GLN A CA  1 
ATOM   97    C  C   . GLN A  1  13  ? 17.387  18.437  38.673  1.00 101.21 ? 39   GLN A C   1 
ATOM   98    O  O   . GLN A  1  13  ? 18.154  18.993  37.891  1.00 100.08 ? 39   GLN A O   1 
ATOM   99    C  CB  . GLN A  1  13  ? 16.134  17.430  36.782  1.00 102.76 ? 39   GLN A CB  1 
ATOM   100   C  CG  . GLN A  1  13  ? 17.161  16.310  36.661  1.00 105.10 ? 39   GLN A CG  1 
ATOM   101   C  CD  . GLN A  1  13  ? 17.192  15.676  35.283  1.00 107.06 ? 39   GLN A CD  1 
ATOM   102   O  OE1 . GLN A  1  13  ? 17.508  16.335  34.291  1.00 107.42 ? 39   GLN A OE1 1 
ATOM   103   N  NE2 . GLN A  1  13  ? 16.863  14.388  35.215  1.00 107.74 ? 39   GLN A NE2 1 
ATOM   104   N  N   . CYS A  1  14  ? 17.689  18.205  39.947  1.00 100.72 ? 40   CYS A N   1 
ATOM   105   C  CA  . CYS A  1  14  ? 18.976  18.593  40.514  1.00 100.86 ? 40   CYS A CA  1 
ATOM   106   C  C   . CYS A  1  14  ? 19.867  17.362  40.528  1.00 98.49  ? 40   CYS A C   1 
ATOM   107   O  O   . CYS A  1  14  ? 20.357  16.954  41.578  1.00 98.31  ? 40   CYS A O   1 
ATOM   108   C  CB  . CYS A  1  14  ? 18.811  19.102  41.952  1.00 103.83 ? 40   CYS A CB  1 
ATOM   109   S  SG  . CYS A  1  14  ? 17.515  20.354  42.279  1.00 108.58 ? 40   CYS A SG  1 
ATOM   110   N  N   . MET A  1  15  ? 20.083  16.783  39.353  1.00 96.37  ? 41   MET A N   1 
ATOM   111   C  CA  . MET A  1  15  ? 20.877  15.568  39.232  1.00 93.72  ? 41   MET A CA  1 
ATOM   112   C  C   . MET A  1  15  ? 22.371  15.785  39.087  1.00 91.82  ? 41   MET A C   1 
ATOM   113   O  O   . MET A  1  15  ? 22.815  16.570  38.263  1.00 91.46  ? 41   MET A O   1 
ATOM   114   C  CB  . MET A  1  15  ? 20.367  14.736  38.045  1.00 93.84  ? 41   MET A CB  1 
ATOM   115   C  CG  . MET A  1  15  ? 20.934  13.320  37.958  1.00 92.99  ? 41   MET A CG  1 
ATOM   116   S  SD  . MET A  1  15  ? 20.448  12.488  36.435  1.00 91.06  ? 41   MET A SD  1 
ATOM   117   C  CE  . MET A  1  15  ? 21.929  12.734  35.424  1.00 90.62  ? 41   MET A CE  1 
ATOM   118   N  N   . GLU A  1  16  ? 23.133  15.067  39.902  1.00 90.85  ? 42   GLU A N   1 
ATOM   119   C  CA  . GLU A  1  16  ? 24.587  15.112  39.881  1.00 90.30  ? 42   GLU A CA  1 
ATOM   120   C  C   . GLU A  1  16  ? 25.173  16.518  39.930  1.00 90.35  ? 42   GLU A C   1 
ATOM   121   O  O   . GLU A  1  16  ? 25.801  16.973  38.972  1.00 90.04  ? 42   GLU A O   1 
ATOM   122   C  CB  . GLU A  1  16  ? 25.083  14.374  38.641  1.00 89.91  ? 42   GLU A CB  1 
ATOM   123   C  CG  . GLU A  1  16  ? 26.394  13.644  38.837  1.00 90.37  ? 42   GLU A CG  1 
ATOM   124   C  CD  . GLU A  1  16  ? 26.650  12.606  37.760  1.00 90.72  ? 42   GLU A CD  1 
ATOM   125   O  OE1 . GLU A  1  16  ? 27.728  11.977  37.780  1.00 90.43  ? 42   GLU A OE1 1 
ATOM   126   O  OE2 . GLU A  1  16  ? 25.766  12.419  36.897  1.00 91.10  ? 42   GLU A OE2 1 
ATOM   127   N  N   . LEU A  1  17  ? 24.972  17.194  41.061  1.00 90.14  ? 43   LEU A N   1 
ATOM   128   C  CA  . LEU A  1  17  ? 25.464  18.554  41.263  1.00 89.16  ? 43   LEU A CA  1 
ATOM   129   C  C   . LEU A  1  17  ? 26.171  18.667  42.604  1.00 90.23  ? 43   LEU A C   1 
ATOM   130   O  O   . LEU A  1  17  ? 26.207  19.740  43.208  1.00 91.04  ? 43   LEU A O   1 
ATOM   131   C  CB  . LEU A  1  17  ? 24.306  19.543  41.220  1.00 87.04  ? 43   LEU A CB  1 
ATOM   132   C  CG  . LEU A  1  17  ? 23.489  19.509  39.932  1.00 86.05  ? 43   LEU A CG  1 
ATOM   133   C  CD1 . LEU A  1  17  ? 22.226  20.315  40.104  1.00 85.80  ? 43   LEU A CD1 1 
ATOM   134   C  CD2 . LEU A  1  17  ? 24.320  20.037  38.785  1.00 85.21  ? 43   LEU A CD2 1 
ATOM   135   N  N   . ASN A  1  18  ? 26.728  17.549  43.061  1.00 90.84  ? 44   ASN A N   1 
ATOM   136   C  CA  . ASN A  1  18  ? 27.451  17.485  44.328  1.00 91.39  ? 44   ASN A CA  1 
ATOM   137   C  C   . ASN A  1  18  ? 26.691  17.971  45.551  1.00 91.14  ? 44   ASN A C   1 
ATOM   138   O  O   . ASN A  1  18  ? 27.270  18.606  46.425  1.00 90.63  ? 44   ASN A O   1 
ATOM   139   C  CB  . ASN A  1  18  ? 28.765  18.261  44.240  1.00 91.34  ? 44   ASN A CB  1 
ATOM   140   C  CG  . ASN A  1  18  ? 29.927  17.389  43.840  1.00 91.24  ? 44   ASN A CG  1 
ATOM   141   O  OD1 . ASN A  1  18  ? 30.242  17.256  42.654  1.00 91.26  ? 44   ASN A OD1 1 
ATOM   142   N  ND2 . ASN A  1  18  ? 30.570  16.776  44.831  1.00 91.02  ? 44   ASN A ND2 1 
ATOM   143   N  N   . PHE A  1  19  ? 25.399  17.685  45.618  1.00 91.77  ? 45   PHE A N   1 
ATOM   144   C  CA  . PHE A  1  19  ? 24.623  18.090  46.777  1.00 93.35  ? 45   PHE A CA  1 
ATOM   145   C  C   . PHE A  1  19  ? 24.874  17.107  47.931  1.00 94.62  ? 45   PHE A C   1 
ATOM   146   O  O   . PHE A  1  19  ? 24.670  15.897  47.782  1.00 94.41  ? 45   PHE A O   1 
ATOM   147   C  CB  . PHE A  1  19  ? 23.124  18.125  46.440  1.00 92.60  ? 45   PHE A CB  1 
ATOM   148   C  CG  . PHE A  1  19  ? 22.687  19.348  45.671  1.00 91.67  ? 45   PHE A CG  1 
ATOM   149   C  CD1 . PHE A  1  19  ? 21.339  19.691  45.611  1.00 91.34  ? 45   PHE A CD1 1 
ATOM   150   C  CD2 . PHE A  1  19  ? 23.613  20.150  45.009  1.00 91.42  ? 45   PHE A CD2 1 
ATOM   151   C  CE1 . PHE A  1  19  ? 20.914  20.812  44.908  1.00 91.45  ? 45   PHE A CE1 1 
ATOM   152   C  CE2 . PHE A  1  19  ? 23.198  21.280  44.299  1.00 91.78  ? 45   PHE A CE2 1 
ATOM   153   C  CZ  . PHE A  1  19  ? 21.843  21.613  44.248  1.00 91.48  ? 45   PHE A CZ  1 
ATOM   154   N  N   . TYR A  1  20  ? 25.331  17.629  49.070  1.00 95.62  ? 46   TYR A N   1 
ATOM   155   C  CA  . TYR A  1  20  ? 25.595  16.798  50.245  1.00 96.38  ? 46   TYR A CA  1 
ATOM   156   C  C   . TYR A  1  20  ? 24.388  16.868  51.171  1.00 95.55  ? 46   TYR A C   1 
ATOM   157   O  O   . TYR A  1  20  ? 24.262  16.093  52.126  1.00 94.90  ? 46   TYR A O   1 
ATOM   158   C  CB  . TYR A  1  20  ? 26.864  17.268  50.983  1.00 98.24  ? 46   TYR A CB  1 
ATOM   159   C  CG  . TYR A  1  20  ? 28.162  16.971  50.232  1.00 101.43 ? 46   TYR A CG  1 
ATOM   160   C  CD1 . TYR A  1  20  ? 28.553  17.741  49.125  1.00 102.35 ? 46   TYR A CD1 1 
ATOM   161   C  CD2 . TYR A  1  20  ? 28.985  15.896  50.606  1.00 102.34 ? 46   TYR A CD2 1 
ATOM   162   C  CE1 . TYR A  1  20  ? 29.729  17.448  48.407  1.00 102.49 ? 46   TYR A CE1 1 
ATOM   163   C  CE2 . TYR A  1  20  ? 30.165  15.593  49.894  1.00 102.69 ? 46   TYR A CE2 1 
ATOM   164   C  CZ  . TYR A  1  20  ? 30.528  16.372  48.795  1.00 102.66 ? 46   TYR A CZ  1 
ATOM   165   O  OH  . TYR A  1  20  ? 31.671  16.063  48.083  1.00 101.70 ? 46   TYR A OH  1 
ATOM   166   N  N   . LYS A  1  21  ? 23.499  17.803  50.857  1.00 94.43  ? 47   LYS A N   1 
ATOM   167   C  CA  . LYS A  1  21  ? 22.286  18.025  51.627  1.00 93.81  ? 47   LYS A CA  1 
ATOM   168   C  C   . LYS A  1  21  ? 21.153  18.446  50.687  1.00 92.92  ? 47   LYS A C   1 
ATOM   169   O  O   . LYS A  1  21  ? 21.390  19.121  49.688  1.00 92.99  ? 47   LYS A O   1 
ATOM   170   C  CB  . LYS A  1  21  ? 22.548  19.103  52.686  1.00 94.25  ? 47   LYS A CB  1 
ATOM   171   C  CG  . LYS A  1  21  ? 23.209  20.367  52.147  1.00 95.07  ? 47   LYS A CG  1 
ATOM   172   C  CD  . LYS A  1  21  ? 23.907  21.156  53.250  1.00 95.57  ? 47   LYS A CD  1 
ATOM   173   C  CE  . LYS A  1  21  ? 25.121  20.405  53.823  1.00 96.26  ? 47   LYS A CE  1 
ATOM   174   N  NZ  . LYS A  1  21  ? 26.248  20.206  52.840  1.00 95.92  ? 47   LYS A NZ  1 
ATOM   175   N  N   . ILE A  1  22  ? 19.928  18.034  51.009  1.00 91.56  ? 48   ILE A N   1 
ATOM   176   C  CA  . ILE A  1  22  ? 18.753  18.342  50.194  1.00 90.86  ? 48   ILE A CA  1 
ATOM   177   C  C   . ILE A  1  22  ? 18.583  19.841  49.966  1.00 91.81  ? 48   ILE A C   1 
ATOM   178   O  O   . ILE A  1  22  ? 18.646  20.623  50.907  1.00 91.73  ? 48   ILE A O   1 
ATOM   179   C  CB  . ILE A  1  22  ? 17.458  17.816  50.851  1.00 89.34  ? 48   ILE A CB  1 
ATOM   180   C  CG1 . ILE A  1  22  ? 17.615  16.353  51.248  1.00 88.50  ? 48   ILE A CG1 1 
ATOM   181   C  CG2 . ILE A  1  22  ? 16.299  17.975  49.902  1.00 88.95  ? 48   ILE A CG2 1 
ATOM   182   C  CD1 . ILE A  1  22  ? 18.303  16.160  52.585  1.00 89.31  ? 48   ILE A CD1 1 
ATOM   183   N  N   . PRO A  1  23  ? 18.351  20.265  48.710  1.00 92.89  ? 49   PRO A N   1 
ATOM   184   C  CA  . PRO A  1  23  ? 18.186  21.702  48.484  1.00 94.06  ? 49   PRO A CA  1 
ATOM   185   C  C   . PRO A  1  23  ? 16.972  22.239  49.232  1.00 95.95  ? 49   PRO A C   1 
ATOM   186   O  O   . PRO A  1  23  ? 16.152  21.475  49.745  1.00 96.67  ? 49   PRO A O   1 
ATOM   187   C  CB  . PRO A  1  23  ? 18.044  21.797  46.970  1.00 93.00  ? 49   PRO A CB  1 
ATOM   188   C  CG  . PRO A  1  23  ? 17.352  20.533  46.632  1.00 92.55  ? 49   PRO A CG  1 
ATOM   189   C  CD  . PRO A  1  23  ? 18.096  19.515  47.470  1.00 92.51  ? 49   PRO A CD  1 
ATOM   190   N  N   . ASP A  1  24  ? 16.869  23.559  49.296  1.00 97.76  ? 50   ASP A N   1 
ATOM   191   C  CA  . ASP A  1  24  ? 15.770  24.214  49.991  1.00 99.35  ? 50   ASP A CA  1 
ATOM   192   C  C   . ASP A  1  24  ? 15.338  25.435  49.196  1.00 99.79  ? 50   ASP A C   1 
ATOM   193   O  O   . ASP A  1  24  ? 14.236  25.954  49.373  1.00 100.51 ? 50   ASP A O   1 
ATOM   194   C  CB  . ASP A  1  24  ? 16.231  24.648  51.375  1.00 100.08 ? 50   ASP A CB  1 
ATOM   195   C  CG  . ASP A  1  24  ? 17.453  25.541  51.318  1.00 101.24 ? 50   ASP A CG  1 
ATOM   196   O  OD1 . ASP A  1  24  ? 18.458  25.127  50.701  1.00 101.95 ? 50   ASP A OD1 1 
ATOM   197   O  OD2 . ASP A  1  24  ? 17.420  26.654  51.886  1.00 102.79 ? 50   ASP A OD2 1 
ATOM   198   N  N   . ASN A  1  25  ? 16.220  25.889  48.316  1.00 99.34  ? 51   ASN A N   1 
ATOM   199   C  CA  . ASN A  1  25  ? 15.947  27.048  47.489  1.00 99.32  ? 51   ASN A CA  1 
ATOM   200   C  C   . ASN A  1  25  ? 14.962  26.737  46.367  1.00 99.54  ? 51   ASN A C   1 
ATOM   201   O  O   . ASN A  1  25  ? 14.950  27.426  45.347  1.00 100.36 ? 51   ASN A O   1 
ATOM   202   C  CB  . ASN A  1  25  ? 17.252  27.570  46.893  1.00 100.16 ? 51   ASN A CB  1 
ATOM   203   C  CG  . ASN A  1  25  ? 17.989  26.516  46.092  1.00 101.33 ? 51   ASN A CG  1 
ATOM   204   O  OD1 . ASN A  1  25  ? 19.040  26.786  45.513  1.00 102.39 ? 51   ASN A OD1 1 
ATOM   205   N  ND2 . ASN A  1  25  ? 17.441  25.307  46.054  1.00 102.38 ? 51   ASN A ND2 1 
ATOM   206   N  N   . LEU A  1  26  ? 14.135  25.712  46.557  1.00 99.06  ? 52   LEU A N   1 
ATOM   207   C  CA  . LEU A  1  26  ? 13.158  25.321  45.543  1.00 98.27  ? 52   LEU A CA  1 
ATOM   208   C  C   . LEU A  1  26  ? 11.730  25.507  46.043  1.00 98.13  ? 52   LEU A C   1 
ATOM   209   O  O   . LEU A  1  26  ? 11.456  25.352  47.236  1.00 97.61  ? 52   LEU A O   1 
ATOM   210   C  CB  . LEU A  1  26  ? 13.362  23.856  45.147  1.00 97.61  ? 52   LEU A CB  1 
ATOM   211   C  CG  . LEU A  1  26  ? 14.759  23.430  44.694  1.00 97.00  ? 52   LEU A CG  1 
ATOM   212   C  CD1 . LEU A  1  26  ? 14.799  21.918  44.649  1.00 96.90  ? 52   LEU A CD1 1 
ATOM   213   C  CD2 . LEU A  1  26  ? 15.113  24.038  43.338  1.00 95.97  ? 52   LEU A CD2 1 
ATOM   214   N  N   . PRO A  1  27  ? 10.802  25.838  45.125  1.00 98.15  ? 53   PRO A N   1 
ATOM   215   C  CA  . PRO A  1  27  ? 9.377   26.058  45.414  1.00 98.77  ? 53   PRO A CA  1 
ATOM   216   C  C   . PRO A  1  27  ? 8.714   24.985  46.289  1.00 99.53  ? 53   PRO A C   1 
ATOM   217   O  O   . PRO A  1  27  ? 9.216   23.868  46.400  1.00 99.20  ? 53   PRO A O   1 
ATOM   218   C  CB  . PRO A  1  27  ? 8.765   26.133  44.021  1.00 98.02  ? 53   PRO A CB  1 
ATOM   219   C  CG  . PRO A  1  27  ? 9.845   26.832  43.251  1.00 97.02  ? 53   PRO A CG  1 
ATOM   220   C  CD  . PRO A  1  27  ? 11.088  26.099  43.702  1.00 96.63  ? 53   PRO A CD  1 
ATOM   221   N  N   . PHE A  1  28  ? 7.591   25.340  46.915  1.00 100.78 ? 54   PHE A N   1 
ATOM   222   C  CA  . PHE A  1  28  ? 6.847   24.412  47.770  1.00 101.94 ? 54   PHE A CA  1 
ATOM   223   C  C   . PHE A  1  28  ? 5.856   23.588  46.941  1.00 101.51 ? 54   PHE A C   1 
ATOM   224   O  O   . PHE A  1  28  ? 5.451   22.485  47.327  1.00 101.59 ? 54   PHE A O   1 
ATOM   225   C  CB  . PHE A  1  28  ? 6.078   25.175  48.861  1.00 103.48 ? 54   PHE A CB  1 
ATOM   226   C  CG  . PHE A  1  28  ? 6.965   25.935  49.822  1.00 106.12 ? 54   PHE A CG  1 
ATOM   227   C  CD1 . PHE A  1  28  ? 7.492   27.182  49.473  1.00 106.95 ? 54   PHE A CD1 1 
ATOM   228   C  CD2 . PHE A  1  28  ? 7.284   25.396  51.076  1.00 106.01 ? 54   PHE A CD2 1 
ATOM   229   C  CE1 . PHE A  1  28  ? 8.327   27.883  50.361  1.00 107.41 ? 54   PHE A CE1 1 
ATOM   230   C  CE2 . PHE A  1  28  ? 8.117   26.083  51.971  1.00 105.46 ? 54   PHE A CE2 1 
ATOM   231   C  CZ  . PHE A  1  28  ? 8.640   27.329  51.616  1.00 106.37 ? 54   PHE A CZ  1 
ATOM   232   N  N   . SER A  1  29  ? 5.482   24.143  45.793  1.00 100.50 ? 55   SER A N   1 
ATOM   233   C  CA  . SER A  1  29  ? 4.533   23.527  44.876  1.00 99.21  ? 55   SER A CA  1 
ATOM   234   C  C   . SER A  1  29  ? 5.108   22.330  44.129  1.00 98.51  ? 55   SER A C   1 
ATOM   235   O  O   . SER A  1  29  ? 4.371   21.581  43.484  1.00 99.35  ? 55   SER A O   1 
ATOM   236   C  CB  . SER A  1  29  ? 4.071   24.570  43.864  1.00 99.47  ? 55   SER A CB  1 
ATOM   237   O  OG  . SER A  1  29  ? 5.196   25.142  43.210  1.00 99.26  ? 55   SER A OG  1 
ATOM   238   N  N   . THR A  1  30  ? 6.423   22.167  44.212  1.00 96.70  ? 56   THR A N   1 
ATOM   239   C  CA  . THR A  1  30  ? 7.130   21.079  43.542  1.00 94.42  ? 56   THR A CA  1 
ATOM   240   C  C   . THR A  1  30  ? 6.460   19.709  43.705  1.00 92.25  ? 56   THR A C   1 
ATOM   241   O  O   . THR A  1  30  ? 6.151   19.281  44.819  1.00 91.58  ? 56   THR A O   1 
ATOM   242   C  CB  . THR A  1  30  ? 8.581   21.004  44.048  1.00 94.79  ? 56   THR A CB  1 
ATOM   243   O  OG1 . THR A  1  30  ? 9.187   22.300  43.946  1.00 95.64  ? 56   THR A OG1 1 
ATOM   244   C  CG2 . THR A  1  30  ? 9.380   20.026  43.218  1.00 94.64  ? 56   THR A CG2 1 
ATOM   245   N  N   . LYS A  1  31  ? 6.255   19.025  42.579  1.00 89.79  ? 57   LYS A N   1 
ATOM   246   C  CA  . LYS A  1  31  ? 5.612   17.717  42.567  1.00 86.91  ? 57   LYS A CA  1 
ATOM   247   C  C   . LYS A  1  31  ? 6.567   16.608  42.122  1.00 85.19  ? 57   LYS A C   1 
ATOM   248   O  O   . LYS A  1  31  ? 6.398   15.449  42.498  1.00 84.14  ? 57   LYS A O   1 
ATOM   249   C  CB  . LYS A  1  31  ? 4.388   17.762  41.645  1.00 87.27  ? 57   LYS A CB  1 
ATOM   250   C  CG  . LYS A  1  31  ? 3.385   18.845  42.028  1.00 88.51  ? 57   LYS A CG  1 
ATOM   251   C  CD  . LYS A  1  31  ? 2.322   19.069  40.954  1.00 90.05  ? 57   LYS A CD  1 
ATOM   252   C  CE  . LYS A  1  31  ? 1.285   17.958  40.935  1.00 90.91  ? 57   LYS A CE  1 
ATOM   253   N  NZ  . LYS A  1  31  ? 0.292   18.140  39.832  1.00 91.38  ? 57   LYS A NZ  1 
ATOM   254   N  N   . ASN A  1  32  ? 7.576   16.973  41.334  1.00 83.37  ? 58   ASN A N   1 
ATOM   255   C  CA  . ASN A  1  32  ? 8.555   16.013  40.830  1.00 82.13  ? 58   ASN A CA  1 
ATOM   256   C  C   . ASN A  1  32  ? 9.993   16.488  41.075  1.00 81.34  ? 58   ASN A C   1 
ATOM   257   O  O   . ASN A  1  32  ? 10.433  17.478  40.495  1.00 80.94  ? 58   ASN A O   1 
ATOM   258   C  CB  . ASN A  1  32  ? 8.350   15.804  39.329  1.00 82.65  ? 58   ASN A CB  1 
ATOM   259   C  CG  . ASN A  1  32  ? 6.889   15.604  38.959  1.00 83.65  ? 58   ASN A CG  1 
ATOM   260   O  OD1 . ASN A  1  32  ? 6.243   14.660  39.419  1.00 84.14  ? 58   ASN A OD1 1 
ATOM   261   N  ND2 . ASN A  1  32  ? 6.359   16.493  38.120  1.00 83.18  ? 58   ASN A ND2 1 
ATOM   262   N  N   . LEU A  1  33  ? 10.725  15.767  41.920  1.00 80.19  ? 59   LEU A N   1 
ATOM   263   C  CA  . LEU A  1  33  ? 12.105  16.118  42.241  1.00 78.65  ? 59   LEU A CA  1 
ATOM   264   C  C   . LEU A  1  33  ? 13.062  14.956  42.018  1.00 79.29  ? 59   LEU A C   1 
ATOM   265   O  O   . LEU A  1  33  ? 12.852  13.863  42.554  1.00 78.84  ? 59   LEU A O   1 
ATOM   266   C  CB  . LEU A  1  33  ? 12.206  16.559  43.703  1.00 77.53  ? 59   LEU A CB  1 
ATOM   267   C  CG  . LEU A  1  33  ? 13.607  16.865  44.243  1.00 75.38  ? 59   LEU A CG  1 
ATOM   268   C  CD1 . LEU A  1  33  ? 14.080  18.208  43.734  1.00 74.35  ? 59   LEU A CD1 1 
ATOM   269   C  CD2 . LEU A  1  33  ? 13.577  16.872  45.747  1.00 74.26  ? 59   LEU A CD2 1 
ATOM   270   N  N   . ASP A  1  34  ? 14.113  15.211  41.237  1.00 79.94  ? 60   ASP A N   1 
ATOM   271   C  CA  . ASP A  1  34  ? 15.149  14.221  40.924  1.00 80.36  ? 60   ASP A CA  1 
ATOM   272   C  C   . ASP A  1  34  ? 16.451  14.646  41.616  1.00 80.17  ? 60   ASP A C   1 
ATOM   273   O  O   . ASP A  1  34  ? 17.033  15.681  41.275  1.00 80.68  ? 60   ASP A O   1 
ATOM   274   C  CB  . ASP A  1  34  ? 15.357  14.162  39.401  1.00 81.33  ? 60   ASP A CB  1 
ATOM   275   C  CG  . ASP A  1  34  ? 16.341  13.079  38.966  1.00 82.49  ? 60   ASP A CG  1 
ATOM   276   O  OD1 . ASP A  1  34  ? 17.475  13.047  39.480  1.00 82.98  ? 60   ASP A OD1 1 
ATOM   277   O  OD2 . ASP A  1  34  ? 15.984  12.261  38.087  1.00 84.08  ? 60   ASP A OD2 1 
ATOM   278   N  N   . LEU A  1  35  ? 16.894  13.863  42.596  1.00 79.66  ? 61   LEU A N   1 
ATOM   279   C  CA  . LEU A  1  35  ? 18.130  14.165  43.317  1.00 79.51  ? 61   LEU A CA  1 
ATOM   280   C  C   . LEU A  1  35  ? 19.144  13.056  43.122  1.00 80.07  ? 61   LEU A C   1 
ATOM   281   O  O   . LEU A  1  35  ? 19.937  12.763  44.009  1.00 80.04  ? 61   LEU A O   1 
ATOM   282   C  CB  . LEU A  1  35  ? 17.853  14.350  44.809  1.00 78.69  ? 61   LEU A CB  1 
ATOM   283   C  CG  . LEU A  1  35  ? 17.148  15.646  45.208  1.00 77.97  ? 61   LEU A CG  1 
ATOM   284   C  CD1 . LEU A  1  35  ? 16.927  15.644  46.709  1.00 76.23  ? 61   LEU A CD1 1 
ATOM   285   C  CD2 . LEU A  1  35  ? 17.984  16.849  44.769  1.00 77.18  ? 61   LEU A CD2 1 
ATOM   286   N  N   . SER A  1  36  ? 19.102  12.449  41.943  1.00 81.49  ? 62   SER A N   1 
ATOM   287   C  CA  . SER A  1  36  ? 19.989  11.353  41.581  1.00 82.52  ? 62   SER A CA  1 
ATOM   288   C  C   . SER A  1  36  ? 21.452  11.763  41.480  1.00 82.59  ? 62   SER A C   1 
ATOM   289   O  O   . SER A  1  36  ? 21.776  12.925  41.234  1.00 81.86  ? 62   SER A O   1 
ATOM   290   C  CB  . SER A  1  36  ? 19.560  10.764  40.240  1.00 83.87  ? 62   SER A CB  1 
ATOM   291   O  OG  . SER A  1  36  ? 18.208  10.346  40.273  1.00 86.29  ? 62   SER A OG  1 
ATOM   292   N  N   . PHE A  1  37  ? 22.320  10.774  41.664  1.00 82.49  ? 63   PHE A N   1 
ATOM   293   C  CA  . PHE A  1  37  ? 23.758  10.944  41.590  1.00 81.46  ? 63   PHE A CA  1 
ATOM   294   C  C   . PHE A  1  37  ? 24.324  12.096  42.401  1.00 81.86  ? 63   PHE A C   1 
ATOM   295   O  O   . PHE A  1  37  ? 25.135  12.883  41.908  1.00 82.88  ? 63   PHE A O   1 
ATOM   296   C  CB  . PHE A  1  37  ? 24.184  11.047  40.124  1.00 80.43  ? 63   PHE A CB  1 
ATOM   297   C  CG  . PHE A  1  37  ? 23.912  9.792   39.338  1.00 79.49  ? 63   PHE A CG  1 
ATOM   298   C  CD1 . PHE A  1  37  ? 22.749  9.658   38.591  1.00 78.17  ? 63   PHE A CD1 1 
ATOM   299   C  CD2 . PHE A  1  37  ? 24.787  8.707   39.414  1.00 79.02  ? 63   PHE A CD2 1 
ATOM   300   C  CE1 . PHE A  1  37  ? 22.466  8.470   37.941  1.00 76.82  ? 63   PHE A CE1 1 
ATOM   301   C  CE2 . PHE A  1  37  ? 24.512  7.515   38.767  1.00 76.37  ? 63   PHE A CE2 1 
ATOM   302   C  CZ  . PHE A  1  37  ? 23.350  7.393   38.033  1.00 76.77  ? 63   PHE A CZ  1 
ATOM   303   N  N   . ASN A  1  38  ? 23.880  12.181  43.650  1.00 81.77  ? 64   ASN A N   1 
ATOM   304   C  CA  . ASN A  1  38  ? 24.351  13.193  44.582  1.00 81.58  ? 64   ASN A CA  1 
ATOM   305   C  C   . ASN A  1  38  ? 24.688  12.446  45.864  1.00 81.79  ? 64   ASN A C   1 
ATOM   306   O  O   . ASN A  1  38  ? 23.950  11.552  46.270  1.00 81.67  ? 64   ASN A O   1 
ATOM   307   C  CB  . ASN A  1  38  ? 23.276  14.247  44.843  1.00 80.95  ? 64   ASN A CB  1 
ATOM   308   C  CG  . ASN A  1  38  ? 23.204  15.293  43.745  1.00 80.68  ? 64   ASN A CG  1 
ATOM   309   O  OD1 . ASN A  1  38  ? 24.197  15.961  43.439  1.00 80.60  ? 64   ASN A OD1 1 
ATOM   310   N  ND2 . ASN A  1  38  ? 22.028  15.445  43.148  1.00 80.40  ? 64   ASN A ND2 1 
ATOM   311   N  N   . PRO A  1  39  ? 25.815  12.789  46.507  1.00 82.01  ? 65   PRO A N   1 
ATOM   312   C  CA  . PRO A  1  39  ? 26.222  12.113  47.745  1.00 81.59  ? 65   PRO A CA  1 
ATOM   313   C  C   . PRO A  1  39  ? 25.447  12.568  48.987  1.00 81.21  ? 65   PRO A C   1 
ATOM   314   O  O   . PRO A  1  39  ? 25.922  13.405  49.749  1.00 82.76  ? 65   PRO A O   1 
ATOM   315   C  CB  . PRO A  1  39  ? 27.708  12.443  47.827  1.00 81.44  ? 65   PRO A CB  1 
ATOM   316   C  CG  . PRO A  1  39  ? 27.735  13.857  47.311  1.00 81.58  ? 65   PRO A CG  1 
ATOM   317   C  CD  . PRO A  1  39  ? 26.800  13.818  46.117  1.00 81.95  ? 65   PRO A CD  1 
ATOM   318   N  N   . LEU A  1  40  ? 24.261  12.006  49.198  1.00 79.48  ? 66   LEU A N   1 
ATOM   319   C  CA  . LEU A  1  40  ? 23.450  12.382  50.345  1.00 77.50  ? 66   LEU A CA  1 
ATOM   320   C  C   . LEU A  1  40  ? 24.007  11.592  51.528  1.00 77.55  ? 66   LEU A C   1 
ATOM   321   O  O   . LEU A  1  40  ? 24.395  12.176  52.532  1.00 77.82  ? 66   LEU A O   1 
ATOM   322   C  CB  . LEU A  1  40  ? 21.969  12.314  49.979  1.00 76.63  ? 66   LEU A CB  1 
ATOM   323   C  CG  . LEU A  1  40  ? 21.536  13.213  48.819  1.00 75.93  ? 66   LEU A CG  1 
ATOM   324   C  CD1 . LEU A  1  40  ? 20.048  13.038  48.576  1.00 75.95  ? 66   LEU A CD1 1 
ATOM   325   C  CD2 . LEU A  1  40  ? 21.854  14.662  49.128  1.00 76.58  ? 66   LEU A CD2 1 
ATOM   326   N  N   . ARG A  1  41  ? 24.025  10.272  51.402  1.00 77.90  ? 67   ARG A N   1 
ATOM   327   C  CA  . ARG A  1  41  ? 24.565  9.358   52.412  1.00 79.69  ? 67   ARG A CA  1 
ATOM   328   C  C   . ARG A  1  41  ? 23.941  9.220   53.817  1.00 79.90  ? 67   ARG A C   1 
ATOM   329   O  O   . ARG A  1  41  ? 24.361  8.353   54.583  1.00 78.49  ? 67   ARG A O   1 
ATOM   330   C  CB  . ARG A  1  41  ? 25.980  9.705   52.882  1.00 82.14  ? 67   ARG A CB  1 
ATOM   331   C  CG  . ARG A  1  41  ? 26.913  10.064  51.731  1.00 85.51  ? 67   ARG A CG  1 
ATOM   332   C  CD  . ARG A  1  41  ? 28.345  10.306  52.188  1.00 89.33  ? 67   ARG A CD  1 
ATOM   333   N  NE  . ARG A  1  41  ? 29.025  11.298  51.350  1.00 92.37  ? 67   ARG A NE  1 
ATOM   334   C  CZ  . ARG A  1  41  ? 30.292  11.685  51.511  1.00 93.63  ? 67   ARG A CZ  1 
ATOM   335   N  NH1 . ARG A  1  41  ? 31.029  11.154  52.481  1.00 94.94  ? 67   ARG A NH1 1 
ATOM   336   N  NH2 . ARG A  1  41  ? 30.815  12.620  50.721  1.00 92.54  ? 67   ARG A NH2 1 
ATOM   337   N  N   . HIS A  1  42  ? 22.969  10.063  54.172  1.00 81.56  ? 68   HIS A N   1 
ATOM   338   C  CA  . HIS A  1  42  ? 22.334  10.003  55.505  1.00 82.81  ? 68   HIS A CA  1 
ATOM   339   C  C   . HIS A  1  42  ? 20.967  10.627  55.289  1.00 82.74  ? 68   HIS A C   1 
ATOM   340   O  O   . HIS A  1  42  ? 20.842  11.828  55.064  1.00 83.47  ? 68   HIS A O   1 
ATOM   341   C  CB  . HIS A  1  42  ? 22.992  10.659  56.751  1.00 83.86  ? 68   HIS A CB  1 
ATOM   342   C  CG  . HIS A  1  42  ? 22.356  10.304  58.076  1.00 84.90  ? 68   HIS A CG  1 
ATOM   343   N  ND1 . HIS A  1  42  ? 22.103  9.003   58.462  1.00 86.58  ? 68   HIS A ND1 1 
ATOM   344   C  CD2 . HIS A  1  42  ? 22.030  11.073  59.148  1.00 84.15  ? 68   HIS A CD2 1 
ATOM   345   C  CE1 . HIS A  1  42  ? 21.661  8.986   59.710  1.00 84.12  ? 68   HIS A CE1 1 
ATOM   346   N  NE2 . HIS A  1  42  ? 21.611  10.228  60.150  1.00 81.92  ? 68   HIS A NE2 1 
ATOM   347   N  N   . LEU A  1  43  ? 19.940  9.796   55.358  1.00 82.24  ? 69   LEU A N   1 
ATOM   348   C  CA  . LEU A  1  43  ? 18.581  10.271  55.207  1.00 81.58  ? 69   LEU A CA  1 
ATOM   349   C  C   . LEU A  1  43  ? 18.006  10.290  56.619  1.00 82.35  ? 69   LEU A C   1 
ATOM   350   O  O   . LEU A  1  43  ? 17.631  9.250   57.164  1.00 82.14  ? 69   LEU A O   1 
ATOM   351   C  CB  . LEU A  1  43  ? 17.802  9.315   54.308  1.00 80.07  ? 69   LEU A CB  1 
ATOM   352   C  CG  . LEU A  1  43  ? 17.041  9.957   53.150  1.00 78.98  ? 69   LEU A CG  1 
ATOM   353   C  CD1 . LEU A  1  43  ? 17.951  10.903  52.377  1.00 77.01  ? 69   LEU A CD1 1 
ATOM   354   C  CD2 . LEU A  1  43  ? 16.503  8.864   52.242  1.00 79.09  ? 69   LEU A CD2 1 
ATOM   355   N  N   . GLY A  1  44  ? 17.961  11.476  57.217  1.00 83.33  ? 70   GLY A N   1 
ATOM   356   C  CA  . GLY A  1  44  ? 17.458  11.603  58.575  1.00 85.48  ? 70   GLY A CA  1 
ATOM   357   C  C   . GLY A  1  44  ? 15.995  11.964  58.662  1.00 87.16  ? 70   GLY A C   1 
ATOM   358   O  O   . GLY A  1  44  ? 15.338  12.137  57.637  1.00 88.15  ? 70   GLY A O   1 
ATOM   359   N  N   . SER A  1  45  ? 15.484  12.094  59.884  1.00 88.61  ? 71   SER A N   1 
ATOM   360   C  CA  . SER A  1  45  ? 14.076  12.421  60.106  1.00 90.51  ? 71   SER A CA  1 
ATOM   361   C  C   . SER A  1  45  ? 13.644  13.734  59.467  1.00 91.03  ? 71   SER A C   1 
ATOM   362   O  O   . SER A  1  45  ? 14.356  14.739  59.532  1.00 91.15  ? 71   SER A O   1 
ATOM   363   C  CB  . SER A  1  45  ? 13.782  12.459  61.602  1.00 91.05  ? 71   SER A CB  1 
ATOM   364   O  OG  . SER A  1  45  ? 14.126  11.216  62.192  1.00 93.18  ? 71   SER A OG  1 
ATOM   365   N  N   . TYR A  1  46  ? 12.461  13.714  58.864  1.00 91.44  ? 72   TYR A N   1 
ATOM   366   C  CA  . TYR A  1  46  ? 11.903  14.879  58.184  1.00 91.64  ? 72   TYR A CA  1 
ATOM   367   C  C   . TYR A  1  46  ? 12.907  15.526  57.240  1.00 91.09  ? 72   TYR A C   1 
ATOM   368   O  O   . TYR A  1  46  ? 13.021  16.751  57.209  1.00 90.99  ? 72   TYR A O   1 
ATOM   369   C  CB  . TYR A  1  46  ? 11.402  15.910  59.202  1.00 92.31  ? 72   TYR A CB  1 
ATOM   370   C  CG  . TYR A  1  46  ? 10.201  15.457  60.021  1.00 93.18  ? 72   TYR A CG  1 
ATOM   371   C  CD1 . TYR A  1  46  ? 10.367  14.789  61.240  1.00 93.26  ? 72   TYR A CD1 1 
ATOM   372   C  CD2 . TYR A  1  46  ? 8.898   15.681  59.564  1.00 92.98  ? 72   TYR A CD2 1 
ATOM   373   C  CE1 . TYR A  1  46  ? 9.266   14.358  61.983  1.00 93.56  ? 72   TYR A CE1 1 
ATOM   374   C  CE2 . TYR A  1  46  ? 7.791   15.253  60.296  1.00 93.46  ? 72   TYR A CE2 1 
ATOM   375   C  CZ  . TYR A  1  46  ? 7.977   14.592  61.502  1.00 93.67  ? 72   TYR A CZ  1 
ATOM   376   O  OH  . TYR A  1  46  ? 6.879   14.157  62.217  1.00 92.80  ? 72   TYR A OH  1 
ATOM   377   N  N   . SER A  1  47  ? 13.621  14.696  56.472  1.00 90.36  ? 73   SER A N   1 
ATOM   378   C  CA  . SER A  1  47  ? 14.621  15.169  55.511  1.00 89.14  ? 73   SER A CA  1 
ATOM   379   C  C   . SER A  1  47  ? 13.966  16.003  54.428  1.00 88.55  ? 73   SER A C   1 
ATOM   380   O  O   . SER A  1  47  ? 14.542  16.963  53.926  1.00 87.01  ? 73   SER A O   1 
ATOM   381   C  CB  . SER A  1  47  ? 15.356  13.988  54.871  1.00 88.32  ? 73   SER A CB  1 
ATOM   382   O  OG  . SER A  1  47  ? 16.390  13.493  55.707  1.00 87.14  ? 73   SER A OG  1 
ATOM   383   N  N   . PHE A  1  48  ? 12.753  15.613  54.067  1.00 89.59  ? 74   PHE A N   1 
ATOM   384   C  CA  . PHE A  1  48  ? 12.003  16.333  53.062  1.00 90.39  ? 74   PHE A CA  1 
ATOM   385   C  C   . PHE A  1  48  ? 10.854  16.978  53.785  1.00 91.46  ? 74   PHE A C   1 
ATOM   386   O  O   . PHE A  1  48  ? 10.053  16.282  54.416  1.00 91.93  ? 74   PHE A O   1 
ATOM   387   C  CB  . PHE A  1  48  ? 11.450  15.376  52.001  1.00 89.92  ? 74   PHE A CB  1 
ATOM   388   C  CG  . PHE A  1  48  ? 12.507  14.607  51.270  1.00 87.73  ? 74   PHE A CG  1 
ATOM   389   C  CD1 . PHE A  1  48  ? 13.291  15.222  50.306  1.00 86.62  ? 74   PHE A CD1 1 
ATOM   390   C  CD2 . PHE A  1  48  ? 12.741  13.271  51.577  1.00 87.09  ? 74   PHE A CD2 1 
ATOM   391   C  CE1 . PHE A  1  48  ? 14.301  14.519  49.660  1.00 86.30  ? 74   PHE A CE1 1 
ATOM   392   C  CE2 . PHE A  1  48  ? 13.747  12.559  50.938  1.00 85.72  ? 74   PHE A CE2 1 
ATOM   393   C  CZ  . PHE A  1  48  ? 14.529  13.183  49.976  1.00 85.55  ? 74   PHE A CZ  1 
ATOM   394   N  N   . PHE A  1  49  ? 10.801  18.304  53.723  1.00 92.21  ? 75   PHE A N   1 
ATOM   395   C  CA  . PHE A  1  49  ? 9.720   19.063  54.330  1.00 93.21  ? 75   PHE A CA  1 
ATOM   396   C  C   . PHE A  1  49  ? 9.492   20.272  53.446  1.00 93.82  ? 75   PHE A C   1 
ATOM   397   O  O   . PHE A  1  49  ? 8.396   20.815  53.386  1.00 94.45  ? 75   PHE A O   1 
ATOM   398   C  CB  . PHE A  1  49  ? 10.058  19.478  55.770  1.00 92.57  ? 75   PHE A CB  1 
ATOM   399   C  CG  . PHE A  1  49  ? 11.381  20.175  55.919  1.00 93.91  ? 75   PHE A CG  1 
ATOM   400   C  CD1 . PHE A  1  49  ? 11.597  21.435  55.361  1.00 94.29  ? 75   PHE A CD1 1 
ATOM   401   C  CD2 . PHE A  1  49  ? 12.407  19.580  56.645  1.00 93.75  ? 75   PHE A CD2 1 
ATOM   402   C  CE1 . PHE A  1  49  ? 12.821  22.095  55.527  1.00 93.62  ? 75   PHE A CE1 1 
ATOM   403   C  CE2 . PHE A  1  49  ? 13.631  20.227  56.818  1.00 93.19  ? 75   PHE A CE2 1 
ATOM   404   C  CZ  . PHE A  1  49  ? 13.839  21.489  56.258  1.00 93.16  ? 75   PHE A CZ  1 
ATOM   405   N  N   . SER A  1  50  ? 10.538  20.664  52.726  1.00 94.72  ? 76   SER A N   1 
ATOM   406   C  CA  . SER A  1  50  ? 10.466  21.803  51.821  1.00 95.91  ? 76   SER A CA  1 
ATOM   407   C  C   . SER A  1  50  ? 9.537   21.488  50.647  1.00 95.76  ? 76   SER A C   1 
ATOM   408   O  O   . SER A  1  50  ? 9.195   22.376  49.867  1.00 96.09  ? 76   SER A O   1 
ATOM   409   C  CB  . SER A  1  50  ? 11.864  22.138  51.277  1.00 97.10  ? 76   SER A CB  1 
ATOM   410   O  OG  . SER A  1  50  ? 12.820  22.244  52.317  1.00 98.22  ? 76   SER A OG  1 
ATOM   411   N  N   . PHE A  1  51  ? 9.139   20.221  50.535  1.00 94.99  ? 77   PHE A N   1 
ATOM   412   C  CA  . PHE A  1  51  ? 8.274   19.761  49.452  1.00 94.15  ? 77   PHE A CA  1 
ATOM   413   C  C   . PHE A  1  51  ? 7.128   18.944  50.036  1.00 94.06  ? 77   PHE A C   1 
ATOM   414   O  O   . PHE A  1  51  ? 7.188   17.716  50.084  1.00 94.28  ? 77   PHE A O   1 
ATOM   415   C  CB  . PHE A  1  51  ? 9.100   18.901  48.500  1.00 92.97  ? 77   PHE A CB  1 
ATOM   416   C  CG  . PHE A  1  51  ? 10.508  19.380  48.345  1.00 92.02  ? 77   PHE A CG  1 
ATOM   417   C  CD1 . PHE A  1  51  ? 10.808  20.423  47.477  1.00 92.76  ? 77   PHE A CD1 1 
ATOM   418   C  CD2 . PHE A  1  51  ? 11.521  18.853  49.140  1.00 91.44  ? 77   PHE A CD2 1 
ATOM   419   C  CE1 . PHE A  1  51  ? 12.105  20.946  47.406  1.00 92.96  ? 77   PHE A CE1 1 
ATOM   420   C  CE2 . PHE A  1  51  ? 12.812  19.359  49.083  1.00 91.87  ? 77   PHE A CE2 1 
ATOM   421   C  CZ  . PHE A  1  51  ? 13.111  20.414  48.213  1.00 92.54  ? 77   PHE A CZ  1 
ATOM   422   N  N   . PRO A  1  52  ? 6.067   19.618  50.492  1.00 93.49  ? 78   PRO A N   1 
ATOM   423   C  CA  . PRO A  1  52  ? 4.944   18.881  51.064  1.00 92.84  ? 78   PRO A CA  1 
ATOM   424   C  C   . PRO A  1  52  ? 3.995   18.354  50.005  1.00 92.42  ? 78   PRO A C   1 
ATOM   425   O  O   . PRO A  1  52  ? 3.198   17.456  50.277  1.00 92.96  ? 78   PRO A O   1 
ATOM   426   C  CB  . PRO A  1  52  ? 4.283   19.924  51.944  1.00 92.79  ? 78   PRO A CB  1 
ATOM   427   C  CG  . PRO A  1  52  ? 4.403   21.148  51.093  1.00 92.97  ? 78   PRO A CG  1 
ATOM   428   C  CD  . PRO A  1  52  ? 5.839   21.071  50.581  1.00 93.07  ? 78   PRO A CD  1 
ATOM   429   N  N   . GLU A  1  53  ? 4.085   18.906  48.797  1.00 91.45  ? 79   GLU A N   1 
ATOM   430   C  CA  . GLU A  1  53  ? 3.193   18.492  47.716  1.00 90.85  ? 79   GLU A CA  1 
ATOM   431   C  C   . GLU A  1  53  ? 3.854   17.572  46.675  1.00 89.67  ? 79   GLU A C   1 
ATOM   432   O  O   . GLU A  1  53  ? 3.410   17.520  45.529  1.00 90.72  ? 79   GLU A O   1 
ATOM   433   C  CB  . GLU A  1  53  ? 2.608   19.750  47.041  1.00 91.23  ? 79   GLU A CB  1 
ATOM   434   C  CG  . GLU A  1  53  ? 1.097   19.684  46.708  1.00 91.13  ? 79   GLU A CG  1 
ATOM   435   C  CD  . GLU A  1  53  ? 0.191   19.527  47.943  1.00 91.50  ? 79   GLU A CD  1 
ATOM   436   O  OE1 . GLU A  1  53  ? -1.052  19.558  47.781  1.00 90.20  ? 79   GLU A OE1 1 
ATOM   437   O  OE2 . GLU A  1  53  ? 0.712   19.369  49.074  1.00 92.22  ? 79   GLU A OE2 1 
ATOM   438   N  N   . LEU A  1  54  ? 4.892   16.836  47.085  1.00 88.25  ? 80   LEU A N   1 
ATOM   439   C  CA  . LEU A  1  54  ? 5.626   15.916  46.195  1.00 86.40  ? 80   LEU A CA  1 
ATOM   440   C  C   . LEU A  1  54  ? 4.909   14.619  45.840  1.00 84.30  ? 80   LEU A C   1 
ATOM   441   O  O   . LEU A  1  54  ? 4.310   13.975  46.705  1.00 83.80  ? 80   LEU A O   1 
ATOM   442   C  CB  . LEU A  1  54  ? 6.982   15.529  46.794  1.00 86.32  ? 80   LEU A CB  1 
ATOM   443   C  CG  . LEU A  1  54  ? 8.257   16.215  46.296  1.00 86.25  ? 80   LEU A CG  1 
ATOM   444   C  CD1 . LEU A  1  54  ? 9.449   15.396  46.769  1.00 86.05  ? 80   LEU A CD1 1 
ATOM   445   C  CD2 . LEU A  1  54  ? 8.275   16.307  44.785  1.00 85.89  ? 80   LEU A CD2 1 
ATOM   446   N  N   . GLN A  1  55  ? 5.020   14.231  44.570  1.00 81.62  ? 81   GLN A N   1 
ATOM   447   C  CA  . GLN A  1  55  ? 4.396   13.014  44.068  1.00 79.00  ? 81   GLN A CA  1 
ATOM   448   C  C   . GLN A  1  55  ? 5.435   11.988  43.594  1.00 76.98  ? 81   GLN A C   1 
ATOM   449   O  O   . GLN A  1  55  ? 5.231   10.780  43.738  1.00 75.94  ? 81   GLN A O   1 
ATOM   450   C  CB  . GLN A  1  55  ? 3.455   13.357  42.910  1.00 79.21  ? 81   GLN A CB  1 
ATOM   451   C  CG  . GLN A  1  55  ? 2.515   14.516  43.190  1.00 77.80  ? 81   GLN A CG  1 
ATOM   452   C  CD  . GLN A  1  55  ? 1.436   14.664  42.136  1.00 78.16  ? 81   GLN A CD  1 
ATOM   453   O  OE1 . GLN A  1  55  ? 1.720   14.738  40.939  1.00 77.37  ? 81   GLN A OE1 1 
ATOM   454   N  NE2 . GLN A  1  55  ? 0.183   14.712  42.579  1.00 78.45  ? 81   GLN A NE2 1 
ATOM   455   N  N   . VAL A  1  56  ? 6.542   12.483  43.039  1.00 74.74  ? 82   VAL A N   1 
ATOM   456   C  CA  . VAL A  1  56  ? 7.609   11.635  42.509  1.00 71.68  ? 82   VAL A CA  1 
ATOM   457   C  C   . VAL A  1  56  ? 9.003   12.031  43.015  1.00 70.54  ? 82   VAL A C   1 
ATOM   458   O  O   . VAL A  1  56  ? 9.474   13.137  42.761  1.00 69.42  ? 82   VAL A O   1 
ATOM   459   C  CB  . VAL A  1  56  ? 7.620   11.708  40.966  1.00 71.00  ? 82   VAL A CB  1 
ATOM   460   C  CG1 . VAL A  1  56  ? 8.332   10.500  40.383  1.00 69.83  ? 82   VAL A CG1 1 
ATOM   461   C  CG2 . VAL A  1  56  ? 6.202   11.810  40.452  1.00 70.18  ? 82   VAL A CG2 1 
ATOM   462   N  N   . LEU A  1  57  ? 9.669   11.115  43.710  1.00 69.66  ? 83   LEU A N   1 
ATOM   463   C  CA  . LEU A  1  57  ? 11.005  11.377  44.241  1.00 68.66  ? 83   LEU A CA  1 
ATOM   464   C  C   . LEU A  1  57  ? 12.068  10.371  43.761  1.00 68.74  ? 83   LEU A C   1 
ATOM   465   O  O   . LEU A  1  57  ? 11.959  9.173   44.028  1.00 68.99  ? 83   LEU A O   1 
ATOM   466   C  CB  . LEU A  1  57  ? 10.941  11.363  45.761  1.00 67.27  ? 83   LEU A CB  1 
ATOM   467   C  CG  . LEU A  1  57  ? 12.279  11.513  46.471  1.00 66.79  ? 83   LEU A CG  1 
ATOM   468   C  CD1 . LEU A  1  57  ? 12.928  12.838  46.092  1.00 67.16  ? 83   LEU A CD1 1 
ATOM   469   C  CD2 . LEU A  1  57  ? 12.048  11.433  47.955  1.00 65.98  ? 83   LEU A CD2 1 
ATOM   470   N  N   . ASP A  1  58  ? 13.100  10.866  43.076  1.00 69.01  ? 84   ASP A N   1 
ATOM   471   C  CA  . ASP A  1  58  ? 14.179  10.018  42.546  1.00 69.56  ? 84   ASP A CA  1 
ATOM   472   C  C   . ASP A  1  58  ? 15.497  10.150  43.330  1.00 69.23  ? 84   ASP A C   1 
ATOM   473   O  O   . ASP A  1  58  ? 16.211  11.139  43.200  1.00 69.01  ? 84   ASP A O   1 
ATOM   474   C  CB  . ASP A  1  58  ? 14.431  10.377  41.068  1.00 71.39  ? 84   ASP A CB  1 
ATOM   475   C  CG  . ASP A  1  58  ? 15.133  9.252   40.278  1.00 72.89  ? 84   ASP A CG  1 
ATOM   476   O  OD1 . ASP A  1  58  ? 15.956  8.512   40.865  1.00 72.83  ? 84   ASP A OD1 1 
ATOM   477   O  OD2 . ASP A  1  58  ? 14.876  9.127   39.052  1.00 72.93  ? 84   ASP A OD2 1 
ATOM   478   N  N   . LEU A  1  59  ? 15.826  9.148   44.134  1.00 69.31  ? 85   LEU A N   1 
ATOM   479   C  CA  . LEU A  1  59  ? 17.069  9.170   44.906  1.00 70.95  ? 85   LEU A CA  1 
ATOM   480   C  C   . LEU A  1  59  ? 18.042  8.103   44.405  1.00 72.15  ? 85   LEU A C   1 
ATOM   481   O  O   . LEU A  1  59  ? 18.750  7.466   45.194  1.00 71.54  ? 85   LEU A O   1 
ATOM   482   C  CB  . LEU A  1  59  ? 16.775  8.939   46.386  1.00 71.04  ? 85   LEU A CB  1 
ATOM   483   C  CG  . LEU A  1  59  ? 15.980  10.043  47.081  1.00 71.91  ? 85   LEU A CG  1 
ATOM   484   C  CD1 . LEU A  1  59  ? 15.615  9.586   48.482  1.00 71.47  ? 85   LEU A CD1 1 
ATOM   485   C  CD2 . LEU A  1  59  ? 16.803  11.326  47.121  1.00 71.72  ? 85   LEU A CD2 1 
ATOM   486   N  N   . SER A  1  60  ? 18.068  7.923   43.085  1.00 73.35  ? 86   SER A N   1 
ATOM   487   C  CA  . SER A  1  60  ? 18.924  6.933   42.441  1.00 73.06  ? 86   SER A CA  1 
ATOM   488   C  C   . SER A  1  60  ? 20.399  7.220   42.648  1.00 73.07  ? 86   SER A C   1 
ATOM   489   O  O   . SER A  1  60  ? 20.844  8.358   42.473  1.00 71.64  ? 86   SER A O   1 
ATOM   490   C  CB  . SER A  1  60  ? 18.646  6.876   40.927  1.00 73.03  ? 86   SER A CB  1 
ATOM   491   O  OG  . SER A  1  60  ? 17.415  6.242   40.609  1.00 73.62  ? 86   SER A OG  1 
ATOM   492   N  N   . ARG A  1  61  ? 21.142  6.179   43.025  1.00 73.42  ? 87   ARG A N   1 
ATOM   493   C  CA  . ARG A  1  61  ? 22.592  6.260   43.216  1.00 74.13  ? 87   ARG A CA  1 
ATOM   494   C  C   . ARG A  1  61  ? 23.013  7.481   44.033  1.00 75.24  ? 87   ARG A C   1 
ATOM   495   O  O   . ARG A  1  61  ? 23.744  8.343   43.529  1.00 74.91  ? 87   ARG A O   1 
ATOM   496   C  CB  . ARG A  1  61  ? 23.279  6.320   41.843  1.00 72.91  ? 87   ARG A CB  1 
ATOM   497   C  CG  . ARG A  1  61  ? 24.592  5.590   41.756  1.00 71.25  ? 87   ARG A CG  1 
ATOM   498   C  CD  . ARG A  1  61  ? 24.389  4.092   41.801  1.00 69.03  ? 87   ARG A CD  1 
ATOM   499   N  NE  . ARG A  1  61  ? 25.669  3.389   41.827  1.00 68.38  ? 87   ARG A NE  1 
ATOM   500   C  CZ  . ARG A  1  61  ? 25.807  2.085   41.610  1.00 68.44  ? 87   ARG A CZ  1 
ATOM   501   N  NH1 . ARG A  1  61  ? 24.741  1.339   41.345  1.00 69.38  ? 87   ARG A NH1 1 
ATOM   502   N  NH2 . ARG A  1  61  ? 27.006  1.525   41.660  1.00 66.50  ? 87   ARG A NH2 1 
ATOM   503   N  N   . CYS A  1  62  ? 22.565  7.550   45.286  1.00 75.97  ? 88   CYS A N   1 
ATOM   504   C  CA  . CYS A  1  62  ? 22.886  8.679   46.157  1.00 75.54  ? 88   CYS A CA  1 
ATOM   505   C  C   . CYS A  1  62  ? 23.710  8.274   47.360  1.00 75.00  ? 88   CYS A C   1 
ATOM   506   O  O   . CYS A  1  62  ? 23.702  8.956   48.372  1.00 75.59  ? 88   CYS A O   1 
ATOM   507   C  CB  . CYS A  1  62  ? 21.605  9.363   46.636  1.00 75.72  ? 88   CYS A CB  1 
ATOM   508   S  SG  . CYS A  1  62  ? 20.699  10.244  45.356  1.00 78.56  ? 88   CYS A SG  1 
ATOM   509   N  N   . GLU A  1  63  ? 24.416  7.160   47.247  1.00 75.27  ? 89   GLU A N   1 
ATOM   510   C  CA  . GLU A  1  63  ? 25.248  6.680   48.337  1.00 75.81  ? 89   GLU A CA  1 
ATOM   511   C  C   . GLU A  1  63  ? 24.491  6.576   49.650  1.00 75.86  ? 89   GLU A C   1 
ATOM   512   O  O   . GLU A  1  63  ? 25.109  6.505   50.702  1.00 76.91  ? 89   GLU A O   1 
ATOM   513   C  CB  . GLU A  1  63  ? 26.437  7.613   48.554  1.00 76.77  ? 89   GLU A CB  1 
ATOM   514   C  CG  . GLU A  1  63  ? 27.264  7.913   47.333  1.00 78.15  ? 89   GLU A CG  1 
ATOM   515   C  CD  . GLU A  1  63  ? 28.578  8.576   47.686  1.00 80.12  ? 89   GLU A CD  1 
ATOM   516   O  OE1 . GLU A  1  63  ? 29.247  9.092   46.769  1.00 81.95  ? 89   GLU A OE1 1 
ATOM   517   O  OE2 . GLU A  1  63  ? 28.948  8.577   48.881  1.00 81.96  ? 89   GLU A OE2 1 
ATOM   518   N  N   . ILE A  1  64  ? 23.165  6.575   49.606  1.00 75.62  ? 90   ILE A N   1 
ATOM   519   C  CA  . ILE A  1  64  ? 22.396  6.492   50.845  1.00 75.67  ? 90   ILE A CA  1 
ATOM   520   C  C   . ILE A  1  64  ? 22.736  5.214   51.606  1.00 76.45  ? 90   ILE A C   1 
ATOM   521   O  O   . ILE A  1  64  ? 22.501  4.120   51.127  1.00 76.43  ? 90   ILE A O   1 
ATOM   522   C  CB  . ILE A  1  64  ? 20.880  6.594   50.557  1.00 73.79  ? 90   ILE A CB  1 
ATOM   523   C  CG1 . ILE A  1  64  ? 20.565  8.012   50.057  1.00 72.15  ? 90   ILE A CG1 1 
ATOM   524   C  CG2 . ILE A  1  64  ? 20.076  6.262   51.809  1.00 72.69  ? 90   ILE A CG2 1 
ATOM   525   C  CD1 . ILE A  1  64  ? 19.151  8.227   49.585  1.00 71.98  ? 90   ILE A CD1 1 
ATOM   526   N  N   . GLN A  1  65  ? 23.305  5.372   52.798  1.00 78.63  ? 91   GLN A N   1 
ATOM   527   C  CA  . GLN A  1  65  ? 23.718  4.238   53.616  1.00 81.27  ? 91   GLN A CA  1 
ATOM   528   C  C   . GLN A  1  65  ? 22.748  3.887   54.750  1.00 81.62  ? 91   GLN A C   1 
ATOM   529   O  O   . GLN A  1  65  ? 22.619  2.722   55.136  1.00 80.26  ? 91   GLN A O   1 
ATOM   530   C  CB  . GLN A  1  65  ? 25.096  4.526   54.201  1.00 83.61  ? 91   GLN A CB  1 
ATOM   531   C  CG  . GLN A  1  65  ? 25.862  3.293   54.615  1.00 87.90  ? 91   GLN A CG  1 
ATOM   532   C  CD  . GLN A  1  65  ? 27.176  3.634   55.281  1.00 90.19  ? 91   GLN A CD  1 
ATOM   533   O  OE1 . GLN A  1  65  ? 27.208  4.092   56.433  1.00 91.03  ? 91   GLN A OE1 1 
ATOM   534   N  NE2 . GLN A  1  65  ? 28.273  3.426   54.557  1.00 90.65  ? 91   GLN A NE2 1 
ATOM   535   N  N   . THR A  1  66  ? 22.076  4.900   55.287  1.00 83.00  ? 92   THR A N   1 
ATOM   536   C  CA  . THR A  1  66  ? 21.118  4.696   56.369  1.00 84.12  ? 92   THR A CA  1 
ATOM   537   C  C   . THR A  1  66  ? 19.921  5.648   56.284  1.00 83.86  ? 92   THR A C   1 
ATOM   538   O  O   . THR A  1  66  ? 20.080  6.855   56.117  1.00 83.05  ? 92   THR A O   1 
ATOM   539   C  CB  . THR A  1  66  ? 21.788  4.874   57.771  1.00 84.81  ? 92   THR A CB  1 
ATOM   540   O  OG1 . THR A  1  66  ? 22.446  6.143   57.825  1.00 84.71  ? 92   THR A OG1 1 
ATOM   541   C  CG2 . THR A  1  66  ? 22.807  3.776   58.042  1.00 84.97  ? 92   THR A CG2 1 
ATOM   542   N  N   . ILE A  1  67  ? 18.722  5.083   56.377  1.00 84.51  ? 93   ILE A N   1 
ATOM   543   C  CA  . ILE A  1  67  ? 17.494  5.864   56.365  1.00 85.09  ? 93   ILE A CA  1 
ATOM   544   C  C   . ILE A  1  67  ? 16.901  5.634   57.748  1.00 86.19  ? 93   ILE A C   1 
ATOM   545   O  O   . ILE A  1  67  ? 16.756  4.489   58.186  1.00 85.60  ? 93   ILE A O   1 
ATOM   546   C  CB  . ILE A  1  67  ? 16.493  5.379   55.297  1.00 84.65  ? 93   ILE A CB  1 
ATOM   547   C  CG1 . ILE A  1  67  ? 17.088  5.557   53.897  1.00 85.23  ? 93   ILE A CG1 1 
ATOM   548   C  CG2 . ILE A  1  67  ? 15.218  6.183   55.389  1.00 84.07  ? 93   ILE A CG2 1 
ATOM   549   C  CD1 . ILE A  1  67  ? 16.192  5.075   52.775  1.00 83.02  ? 93   ILE A CD1 1 
ATOM   550   N  N   . GLU A  1  68  ? 16.582  6.725   58.437  1.00 87.21  ? 94   GLU A N   1 
ATOM   551   C  CA  . GLU A  1  68  ? 16.038  6.662   59.791  1.00 88.23  ? 94   GLU A CA  1 
ATOM   552   C  C   . GLU A  1  68  ? 14.515  6.774   59.841  1.00 88.46  ? 94   GLU A C   1 
ATOM   553   O  O   . GLU A  1  68  ? 13.857  6.946   58.815  1.00 88.83  ? 94   GLU A O   1 
ATOM   554   C  CB  . GLU A  1  68  ? 16.670  7.769   60.642  1.00 89.20  ? 94   GLU A CB  1 
ATOM   555   C  CG  . GLU A  1  68  ? 18.192  7.826   60.519  1.00 90.62  ? 94   GLU A CG  1 
ATOM   556   C  CD  . GLU A  1  68  ? 18.828  9.018   61.223  1.00 90.68  ? 94   GLU A CD  1 
ATOM   557   O  OE1 . GLU A  1  68  ? 18.262  10.130  61.135  1.00 91.27  ? 94   GLU A OE1 1 
ATOM   558   O  OE2 . GLU A  1  68  ? 19.907  8.843   61.837  1.00 88.81  ? 94   GLU A OE2 1 
ATOM   559   N  N   . ASP A  1  69  ? 13.965  6.678   61.050  1.00 88.26  ? 95   ASP A N   1 
ATOM   560   C  CA  . ASP A  1  69  ? 12.524  6.767   61.257  1.00 87.61  ? 95   ASP A CA  1 
ATOM   561   C  C   . ASP A  1  69  ? 11.936  8.075   60.752  1.00 86.56  ? 95   ASP A C   1 
ATOM   562   O  O   . ASP A  1  69  ? 12.424  9.156   61.078  1.00 85.29  ? 95   ASP A O   1 
ATOM   563   C  CB  . ASP A  1  69  ? 12.200  6.604   62.740  1.00 88.49  ? 95   ASP A CB  1 
ATOM   564   C  CG  . ASP A  1  69  ? 12.376  5.179   63.217  1.00 89.83  ? 95   ASP A CG  1 
ATOM   565   O  OD1 . ASP A  1  69  ? 11.462  4.362   63.002  1.00 90.63  ? 95   ASP A OD1 1 
ATOM   566   O  OD2 . ASP A  1  69  ? 13.437  4.872   63.794  1.00 91.30  ? 95   ASP A OD2 1 
ATOM   567   N  N   . GLY A  1  70  ? 10.886  7.953   59.945  1.00 86.24  ? 96   GLY A N   1 
ATOM   568   C  CA  . GLY A  1  70  ? 10.204  9.113   59.396  1.00 85.98  ? 96   GLY A CA  1 
ATOM   569   C  C   . GLY A  1  70  ? 11.075  10.079  58.624  1.00 85.36  ? 96   GLY A C   1 
ATOM   570   O  O   . GLY A  1  70  ? 11.200  11.245  58.995  1.00 84.70  ? 96   GLY A O   1 
ATOM   571   N  N   . ALA A  1  71  ? 11.683  9.597   57.547  1.00 84.77  ? 97   ALA A N   1 
ATOM   572   C  CA  . ALA A  1  71  ? 12.536  10.445  56.730  1.00 84.02  ? 97   ALA A CA  1 
ATOM   573   C  C   . ALA A  1  71  ? 11.644  11.162  55.735  1.00 83.90  ? 97   ALA A C   1 
ATOM   574   O  O   . ALA A  1  71  ? 11.928  12.294  55.321  1.00 83.56  ? 97   ALA A O   1 
ATOM   575   C  CB  . ALA A  1  71  ? 13.562  9.609   56.007  1.00 83.80  ? 97   ALA A CB  1 
ATOM   576   N  N   . TYR A  1  72  ? 10.557  10.492  55.360  1.00 83.54  ? 98   TYR A N   1 
ATOM   577   C  CA  . TYR A  1  72  ? 9.604   11.070  54.420  1.00 83.78  ? 98   TYR A CA  1 
ATOM   578   C  C   . TYR A  1  72  ? 8.268   11.284  55.123  1.00 84.56  ? 98   TYR A C   1 
ATOM   579   O  O   . TYR A  1  72  ? 7.208   11.241  54.484  1.00 85.06  ? 98   TYR A O   1 
ATOM   580   C  CB  . TYR A  1  72  ? 9.383   10.151  53.211  1.00 80.56  ? 98   TYR A CB  1 
ATOM   581   C  CG  . TYR A  1  72  ? 10.615  9.446   52.688  1.00 76.21  ? 98   TYR A CG  1 
ATOM   582   C  CD1 . TYR A  1  72  ? 11.000  8.210   53.205  1.00 74.38  ? 98   TYR A CD1 1 
ATOM   583   C  CD2 . TYR A  1  72  ? 11.366  9.989   51.652  1.00 74.13  ? 98   TYR A CD2 1 
ATOM   584   C  CE1 . TYR A  1  72  ? 12.091  7.532   52.698  1.00 72.46  ? 98   TYR A CE1 1 
ATOM   585   C  CE2 . TYR A  1  72  ? 12.462  9.317   51.143  1.00 72.60  ? 98   TYR A CE2 1 
ATOM   586   C  CZ  . TYR A  1  72  ? 12.818  8.092   51.670  1.00 72.50  ? 98   TYR A CZ  1 
ATOM   587   O  OH  . TYR A  1  72  ? 13.911  7.427   51.176  1.00 73.30  ? 98   TYR A OH  1 
ATOM   588   N  N   . GLN A  1  73  ? 8.326   11.527  56.431  1.00 84.27  ? 99   GLN A N   1 
ATOM   589   C  CA  . GLN A  1  73  ? 7.121   11.715  57.227  1.00 83.36  ? 99   GLN A CA  1 
ATOM   590   C  C   . GLN A  1  73  ? 6.096   12.719  56.688  1.00 84.04  ? 99   GLN A C   1 
ATOM   591   O  O   . GLN A  1  73  ? 4.890   12.518  56.842  1.00 83.14  ? 99   GLN A O   1 
ATOM   592   C  CB  . GLN A  1  73  ? 7.500   12.091  58.654  1.00 81.37  ? 99   GLN A CB  1 
ATOM   593   C  CG  . GLN A  1  73  ? 6.319   12.093  59.600  1.00 80.50  ? 99   GLN A CG  1 
ATOM   594   C  CD  . GLN A  1  73  ? 5.576   10.769  59.621  1.00 79.23  ? 99   GLN A CD  1 
ATOM   595   O  OE1 . GLN A  1  73  ? 6.104   9.754   60.072  1.00 77.62  ? 99   GLN A OE1 1 
ATOM   596   N  NE2 . GLN A  1  73  ? 4.340   10.778  59.134  1.00 78.56  ? 99   GLN A NE2 1 
ATOM   597   N  N   . SER A  1  74  ? 6.558   13.782  56.040  1.00 84.59  ? 100  SER A N   1 
ATOM   598   C  CA  . SER A  1  74  ? 5.640   14.788  55.518  1.00 85.25  ? 100  SER A CA  1 
ATOM   599   C  C   . SER A  1  74  ? 5.289   14.687  54.032  1.00 86.43  ? 100  SER A C   1 
ATOM   600   O  O   . SER A  1  74  ? 4.910   15.688  53.420  1.00 87.27  ? 100  SER A O   1 
ATOM   601   C  CB  . SER A  1  74  ? 6.214   16.172  55.793  1.00 85.38  ? 100  SER A CB  1 
ATOM   602   O  OG  . SER A  1  74  ? 7.471   16.317  55.160  1.00 84.75  ? 100  SER A OG  1 
ATOM   603   N  N   . LEU A  1  75  ? 5.402   13.497  53.450  1.00 87.17  ? 101  LEU A N   1 
ATOM   604   C  CA  . LEU A  1  75  ? 5.100   13.321  52.026  1.00 87.86  ? 101  LEU A CA  1 
ATOM   605   C  C   . LEU A  1  75  ? 3.854   12.458  51.806  1.00 88.37  ? 101  LEU A C   1 
ATOM   606   O  O   . LEU A  1  75  ? 3.932   11.326  51.321  1.00 88.96  ? 101  LEU A O   1 
ATOM   607   C  CB  . LEU A  1  75  ? 6.315   12.703  51.328  1.00 87.32  ? 101  LEU A CB  1 
ATOM   608   C  CG  . LEU A  1  75  ? 7.551   13.608  51.248  1.00 86.49  ? 101  LEU A CG  1 
ATOM   609   C  CD1 . LEU A  1  75  ? 8.804   12.793  50.957  1.00 85.22  ? 101  LEU A CD1 1 
ATOM   610   C  CD2 . LEU A  1  75  ? 7.312   14.667  50.175  1.00 86.94  ? 101  LEU A CD2 1 
ATOM   611   N  N   . SER A  1  76  ? 2.699   13.016  52.156  1.00 88.72  ? 102  SER A N   1 
ATOM   612   C  CA  . SER A  1  76  ? 1.431   12.311  52.047  1.00 88.49  ? 102  SER A CA  1 
ATOM   613   C  C   . SER A  1  76  ? 0.967   12.118  50.615  1.00 88.58  ? 102  SER A C   1 
ATOM   614   O  O   . SER A  1  76  ? 0.172   11.221  50.344  1.00 88.54  ? 102  SER A O   1 
ATOM   615   C  CB  . SER A  1  76  ? 0.359   13.069  52.817  1.00 88.91  ? 102  SER A CB  1 
ATOM   616   O  OG  . SER A  1  76  ? 0.084   14.306  52.182  1.00 91.64  ? 102  SER A OG  1 
ATOM   617   N  N   . HIS A  1  77  ? 1.456   12.955  49.704  1.00 88.24  ? 103  HIS A N   1 
ATOM   618   C  CA  . HIS A  1  77  ? 1.049   12.856  48.305  1.00 88.16  ? 103  HIS A CA  1 
ATOM   619   C  C   . HIS A  1  77  ? 2.003   12.029  47.433  1.00 86.05  ? 103  HIS A C   1 
ATOM   620   O  O   . HIS A  1  77  ? 1.656   11.643  46.314  1.00 86.12  ? 103  HIS A O   1 
ATOM   621   C  CB  . HIS A  1  77  ? 0.877   14.264  47.708  1.00 90.95  ? 103  HIS A CB  1 
ATOM   622   C  CG  . HIS A  1  77  ? -0.121  15.117  48.435  1.00 94.04  ? 103  HIS A CG  1 
ATOM   623   N  ND1 . HIS A  1  77  ? -1.379  14.669  48.775  1.00 94.90  ? 103  HIS A ND1 1 
ATOM   624   C  CD2 . HIS A  1  77  ? -0.046  16.397  48.873  1.00 95.15  ? 103  HIS A CD2 1 
ATOM   625   C  CE1 . HIS A  1  77  ? -2.037  15.634  49.394  1.00 94.75  ? 103  HIS A CE1 1 
ATOM   626   N  NE2 . HIS A  1  77  ? -1.252  16.692  49.466  1.00 95.20  ? 103  HIS A NE2 1 
ATOM   627   N  N   . LEU A  1  78  ? 3.196   11.746  47.947  1.00 83.23  ? 104  LEU A N   1 
ATOM   628   C  CA  . LEU A  1  78  ? 4.188   10.975  47.202  1.00 79.98  ? 104  LEU A CA  1 
ATOM   629   C  C   . LEU A  1  78  ? 3.661   9.596   46.814  1.00 78.70  ? 104  LEU A C   1 
ATOM   630   O  O   . LEU A  1  78  ? 3.246   8.819   47.685  1.00 78.97  ? 104  LEU A O   1 
ATOM   631   C  CB  . LEU A  1  78  ? 5.451   10.799  48.034  1.00 78.28  ? 104  LEU A CB  1 
ATOM   632   C  CG  . LEU A  1  78  ? 6.612   10.173  47.272  1.00 76.85  ? 104  LEU A CG  1 
ATOM   633   C  CD1 . LEU A  1  78  ? 7.260   11.214  46.372  1.00 76.67  ? 104  LEU A CD1 1 
ATOM   634   C  CD2 . LEU A  1  78  ? 7.609   9.625   48.253  1.00 76.79  ? 104  LEU A CD2 1 
ATOM   635   N  N   . SER A  1  79  ? 3.707   9.291   45.516  1.00 75.52  ? 105  SER A N   1 
ATOM   636   C  CA  . SER A  1  79  ? 3.226   8.012   45.001  1.00 71.83  ? 105  SER A CA  1 
ATOM   637   C  C   . SER A  1  79  ? 4.356   7.145   44.472  1.00 69.64  ? 105  SER A C   1 
ATOM   638   O  O   . SER A  1  79  ? 4.213   5.930   44.356  1.00 69.78  ? 105  SER A O   1 
ATOM   639   C  CB  . SER A  1  79  ? 2.226   8.256   43.875  1.00 72.62  ? 105  SER A CB  1 
ATOM   640   O  OG  . SER A  1  79  ? 2.822   9.045   42.858  1.00 72.62  ? 105  SER A OG  1 
ATOM   641   N  N   . THR A  1  80  ? 5.473   7.781   44.132  1.00 66.65  ? 106  THR A N   1 
ATOM   642   C  CA  . THR A  1  80  ? 6.634   7.076   43.597  1.00 62.86  ? 106  THR A CA  1 
ATOM   643   C  C   . THR A  1  80  ? 7.943   7.480   44.284  1.00 61.37  ? 106  THR A C   1 
ATOM   644   O  O   . THR A  1  80  ? 8.287   8.664   44.355  1.00 60.24  ? 106  THR A O   1 
ATOM   645   C  CB  . THR A  1  80  ? 6.777   7.330   42.084  1.00 61.78  ? 106  THR A CB  1 
ATOM   646   O  OG1 . THR A  1  80  ? 5.574   6.925   41.421  1.00 59.99  ? 106  THR A OG1 1 
ATOM   647   C  CG2 . THR A  1  80  ? 7.959   6.553   41.515  1.00 59.72  ? 106  THR A CG2 1 
ATOM   648   N  N   . LEU A  1  81  ? 8.657   6.475   44.787  1.00 60.26  ? 107  LEU A N   1 
ATOM   649   C  CA  . LEU A  1  81  ? 9.933   6.651   45.464  1.00 58.76  ? 107  LEU A CA  1 
ATOM   650   C  C   . LEU A  1  81  ? 10.936  5.698   44.825  1.00 58.41  ? 107  LEU A C   1 
ATOM   651   O  O   . LEU A  1  81  ? 10.719  4.483   44.793  1.00 58.94  ? 107  LEU A O   1 
ATOM   652   C  CB  . LEU A  1  81  ? 9.782   6.331   46.947  1.00 58.32  ? 107  LEU A CB  1 
ATOM   653   C  CG  . LEU A  1  81  ? 11.053  6.299   47.797  1.00 56.97  ? 107  LEU A CG  1 
ATOM   654   C  CD1 . LEU A  1  81  ? 11.777  7.610   47.707  1.00 55.96  ? 107  LEU A CD1 1 
ATOM   655   C  CD2 . LEU A  1  81  ? 10.674  5.987   49.229  1.00 57.08  ? 107  LEU A CD2 1 
ATOM   656   N  N   . ILE A  1  82  ? 12.030  6.249   44.315  1.00 57.32  ? 108  ILE A N   1 
ATOM   657   C  CA  . ILE A  1  82  ? 13.048  5.444   43.647  1.00 56.82  ? 108  ILE A CA  1 
ATOM   658   C  C   . ILE A  1  82  ? 14.359  5.498   44.429  1.00 57.75  ? 108  ILE A C   1 
ATOM   659   O  O   . ILE A  1  82  ? 14.929  6.569   44.608  1.00 59.20  ? 108  ILE A O   1 
ATOM   660   C  CB  . ILE A  1  82  ? 13.274  5.973   42.215  1.00 53.94  ? 108  ILE A CB  1 
ATOM   661   C  CG1 . ILE A  1  82  ? 11.926  6.110   41.507  1.00 49.53  ? 108  ILE A CG1 1 
ATOM   662   C  CG2 . ILE A  1  82  ? 14.189  5.035   41.454  1.00 52.69  ? 108  ILE A CG2 1 
ATOM   663   C  CD1 . ILE A  1  82  ? 12.001  6.836   40.217  1.00 46.29  ? 108  ILE A CD1 1 
ATOM   664   N  N   . LEU A  1  83  ? 14.844  4.349   44.886  1.00 57.84  ? 109  LEU A N   1 
ATOM   665   C  CA  . LEU A  1  83  ? 16.082  4.309   45.664  1.00 58.80  ? 109  LEU A CA  1 
ATOM   666   C  C   . LEU A  1  83  ? 17.105  3.416   45.007  1.00 60.11  ? 109  LEU A C   1 
ATOM   667   O  O   . LEU A  1  83  ? 17.972  2.872   45.678  1.00 60.21  ? 109  LEU A O   1 
ATOM   668   C  CB  . LEU A  1  83  ? 15.810  3.785   47.077  1.00 57.06  ? 109  LEU A CB  1 
ATOM   669   C  CG  . LEU A  1  83  ? 14.797  4.546   47.931  1.00 56.37  ? 109  LEU A CG  1 
ATOM   670   C  CD1 . LEU A  1  83  ? 14.548  3.796   49.231  1.00 53.58  ? 109  LEU A CD1 1 
ATOM   671   C  CD2 . LEU A  1  83  ? 15.321  5.941   48.196  1.00 56.30  ? 109  LEU A CD2 1 
ATOM   672   N  N   . THR A  1  84  ? 16.996  3.264   43.694  1.00 62.68  ? 110  THR A N   1 
ATOM   673   C  CA  . THR A  1  84  ? 17.894  2.407   42.922  1.00 64.44  ? 110  THR A CA  1 
ATOM   674   C  C   . THR A  1  84  ? 19.374  2.647   43.177  1.00 65.67  ? 110  THR A C   1 
ATOM   675   O  O   . THR A  1  84  ? 19.831  3.791   43.163  1.00 65.97  ? 110  THR A O   1 
ATOM   676   C  CB  . THR A  1  84  ? 17.654  2.582   41.401  1.00 65.15  ? 110  THR A CB  1 
ATOM   677   O  OG1 . THR A  1  84  ? 16.267  2.386   41.099  1.00 67.13  ? 110  THR A OG1 1 
ATOM   678   C  CG2 . THR A  1  84  ? 18.467  1.581   40.613  1.00 65.22  ? 110  THR A CG2 1 
ATOM   679   N  N   . GLY A  1  85  ? 20.106  1.558   43.418  1.00 66.71  ? 111  GLY A N   1 
ATOM   680   C  CA  . GLY A  1  85  ? 21.549  1.623   43.614  1.00 68.31  ? 111  GLY A CA  1 
ATOM   681   C  C   . GLY A  1  85  ? 22.135  2.287   44.843  1.00 69.17  ? 111  GLY A C   1 
ATOM   682   O  O   . GLY A  1  85  ? 23.189  2.929   44.773  1.00 69.76  ? 111  GLY A O   1 
ATOM   683   N  N   . ASN A  1  86  ? 21.469  2.137   45.976  1.00 68.53  ? 112  ASN A N   1 
ATOM   684   C  CA  . ASN A  1  86  ? 21.984  2.730   47.190  1.00 68.73  ? 112  ASN A CA  1 
ATOM   685   C  C   . ASN A  1  86  ? 22.486  1.642   48.107  1.00 69.87  ? 112  ASN A C   1 
ATOM   686   O  O   . ASN A  1  86  ? 21.824  0.634   48.316  1.00 70.47  ? 112  ASN A O   1 
ATOM   687   C  CB  . ASN A  1  86  ? 20.907  3.558   47.882  1.00 68.41  ? 112  ASN A CB  1 
ATOM   688   C  CG  . ASN A  1  86  ? 20.680  4.882   47.197  1.00 69.41  ? 112  ASN A CG  1 
ATOM   689   O  OD1 . ASN A  1  86  ? 21.605  5.679   47.053  1.00 70.10  ? 112  ASN A OD1 1 
ATOM   690   N  ND2 . ASN A  1  86  ? 19.447  5.128   46.766  1.00 70.69  ? 112  ASN A ND2 1 
ATOM   691   N  N   . PRO A  1  87  ? 23.689  1.820   48.652  1.00 70.88  ? 113  PRO A N   1 
ATOM   692   C  CA  . PRO A  1  87  ? 24.283  0.836   49.563  1.00 72.01  ? 113  PRO A CA  1 
ATOM   693   C  C   . PRO A  1  87  ? 23.673  0.947   50.963  1.00 73.36  ? 113  PRO A C   1 
ATOM   694   O  O   . PRO A  1  87  ? 24.291  1.495   51.877  1.00 74.86  ? 113  PRO A O   1 
ATOM   695   C  CB  . PRO A  1  87  ? 25.753  1.216   49.542  1.00 71.49  ? 113  PRO A CB  1 
ATOM   696   C  CG  . PRO A  1  87  ? 25.694  2.719   49.386  1.00 70.19  ? 113  PRO A CG  1 
ATOM   697   C  CD  . PRO A  1  87  ? 24.646  2.892   48.324  1.00 70.46  ? 113  PRO A CD  1 
ATOM   698   N  N   . ILE A  1  88  ? 22.461  0.434   51.136  1.00 73.68  ? 114  ILE A N   1 
ATOM   699   C  CA  . ILE A  1  88  ? 21.805  0.530   52.428  1.00 74.80  ? 114  ILE A CA  1 
ATOM   700   C  C   . ILE A  1  88  ? 22.339  -0.459  53.456  1.00 77.45  ? 114  ILE A C   1 
ATOM   701   O  O   . ILE A  1  88  ? 22.464  -1.657  53.186  1.00 77.93  ? 114  ILE A O   1 
ATOM   702   C  CB  . ILE A  1  88  ? 20.276  0.398   52.260  1.00 73.62  ? 114  ILE A CB  1 
ATOM   703   C  CG1 . ILE A  1  88  ? 19.731  1.712   51.684  1.00 72.93  ? 114  ILE A CG1 1 
ATOM   704   C  CG2 . ILE A  1  88  ? 19.620  0.051   53.576  1.00 72.98  ? 114  ILE A CG2 1 
ATOM   705   C  CD1 . ILE A  1  88  ? 18.237  1.787   51.551  1.00 71.54  ? 114  ILE A CD1 1 
ATOM   706   N  N   . GLN A  1  89  ? 22.666  0.074   54.635  1.00 79.95  ? 115  GLN A N   1 
ATOM   707   C  CA  . GLN A  1  89  ? 23.205  -0.701  55.753  1.00 81.63  ? 115  GLN A CA  1 
ATOM   708   C  C   . GLN A  1  89  ? 22.186  -0.756  56.882  1.00 81.75  ? 115  GLN A C   1 
ATOM   709   O  O   . GLN A  1  89  ? 21.985  -1.793  57.509  1.00 81.68  ? 115  GLN A O   1 
ATOM   710   C  CB  . GLN A  1  89  ? 24.485  -0.048  56.284  1.00 84.34  ? 115  GLN A CB  1 
ATOM   711   C  CG  . GLN A  1  89  ? 25.663  -0.015  55.308  1.00 87.79  ? 115  GLN A CG  1 
ATOM   712   C  CD  . GLN A  1  89  ? 26.422  -1.326  55.272  1.00 90.23  ? 115  GLN A CD  1 
ATOM   713   O  OE1 . GLN A  1  89  ? 25.832  -2.388  55.037  1.00 91.78  ? 115  GLN A OE1 1 
ATOM   714   N  NE2 . GLN A  1  89  ? 27.735  -1.265  55.502  1.00 90.08  ? 115  GLN A NE2 1 
ATOM   715   N  N   . SER A  1  90  ? 21.545  0.377   57.141  1.00 82.22  ? 116  SER A N   1 
ATOM   716   C  CA  . SER A  1  90  ? 20.556  0.452   58.201  1.00 83.15  ? 116  SER A CA  1 
ATOM   717   C  C   . SER A  1  90  ? 19.263  1.080   57.699  1.00 83.80  ? 116  SER A C   1 
ATOM   718   O  O   . SER A  1  90  ? 19.255  2.207   57.191  1.00 83.30  ? 116  SER A O   1 
ATOM   719   C  CB  . SER A  1  90  ? 21.108  1.258   59.379  1.00 83.03  ? 116  SER A CB  1 
ATOM   720   O  OG  . SER A  1  90  ? 20.309  1.083   60.536  1.00 83.29  ? 116  SER A OG  1 
ATOM   721   N  N   . LEU A  1  91  ? 18.172  0.333   57.858  1.00 84.58  ? 117  LEU A N   1 
ATOM   722   C  CA  . LEU A  1  91  ? 16.846  0.760   57.436  1.00 84.73  ? 117  LEU A CA  1 
ATOM   723   C  C   . LEU A  1  91  ? 15.915  0.768   58.655  1.00 85.09  ? 117  LEU A C   1 
ATOM   724   O  O   . LEU A  1  91  ? 15.450  -0.277  59.106  1.00 85.35  ? 117  LEU A O   1 
ATOM   725   C  CB  . LEU A  1  91  ? 16.331  -0.212  56.367  1.00 84.53  ? 117  LEU A CB  1 
ATOM   726   C  CG  . LEU A  1  91  ? 15.259  0.212   55.362  1.00 84.40  ? 117  LEU A CG  1 
ATOM   727   C  CD1 . LEU A  1  91  ? 15.700  1.440   54.584  1.00 84.27  ? 117  LEU A CD1 1 
ATOM   728   C  CD2 . LEU A  1  91  ? 15.000  -0.945  54.419  1.00 83.87  ? 117  LEU A CD2 1 
ATOM   729   N  N   . ALA A  1  92  ? 15.652  1.958   59.185  1.00 85.64  ? 118  ALA A N   1 
ATOM   730   C  CA  . ALA A  1  92  ? 14.791  2.123   60.359  1.00 86.48  ? 118  ALA A CA  1 
ATOM   731   C  C   . ALA A  1  92  ? 13.416  1.460   60.256  1.00 86.50  ? 118  ALA A C   1 
ATOM   732   O  O   . ALA A  1  92  ? 12.749  1.534   59.223  1.00 86.86  ? 118  ALA A O   1 
ATOM   733   C  CB  . ALA A  1  92  ? 14.621  3.609   60.667  1.00 87.24  ? 118  ALA A CB  1 
ATOM   734   N  N   . LEU A  1  93  ? 12.996  0.842   61.359  1.00 86.11  ? 119  LEU A N   1 
ATOM   735   C  CA  . LEU A  1  93  ? 11.720  0.141   61.454  1.00 85.27  ? 119  LEU A CA  1 
ATOM   736   C  C   . LEU A  1  93  ? 10.553  0.943   60.868  1.00 84.22  ? 119  LEU A C   1 
ATOM   737   O  O   . LEU A  1  93  ? 9.566   0.369   60.398  1.00 84.46  ? 119  LEU A O   1 
ATOM   738   C  CB  . LEU A  1  93  ? 11.452  -0.196  62.921  1.00 85.92  ? 119  LEU A CB  1 
ATOM   739   C  CG  . LEU A  1  93  ? 10.548  -1.377  63.283  1.00 87.84  ? 119  LEU A CG  1 
ATOM   740   C  CD1 . LEU A  1  93  ? 10.679  -1.642  64.781  1.00 87.98  ? 119  LEU A CD1 1 
ATOM   741   C  CD2 . LEU A  1  93  ? 9.088   -1.100  62.903  1.00 89.12  ? 119  LEU A CD2 1 
ATOM   742   N  N   . GLY A  1  94  ? 10.667  2.266   60.891  1.00 82.32  ? 120  GLY A N   1 
ATOM   743   C  CA  . GLY A  1  94  ? 9.605   3.095   60.357  1.00 81.93  ? 120  GLY A CA  1 
ATOM   744   C  C   . GLY A  1  94  ? 10.125  4.141   59.395  1.00 81.63  ? 120  GLY A C   1 
ATOM   745   O  O   . GLY A  1  94  ? 9.753   5.310   59.470  1.00 81.52  ? 120  GLY A O   1 
ATOM   746   N  N   . ALA A  1  95  ? 10.980  3.719   58.475  1.00 81.40  ? 121  ALA A N   1 
ATOM   747   C  CA  . ALA A  1  95  ? 11.557  4.637   57.505  1.00 80.95  ? 121  ALA A CA  1 
ATOM   748   C  C   . ALA A  1  95  ? 10.534  5.133   56.484  1.00 80.80  ? 121  ALA A C   1 
ATOM   749   O  O   . ALA A  1  95  ? 10.562  6.294   56.063  1.00 79.60  ? 121  ALA A O   1 
ATOM   750   C  CB  . ALA A  1  95  ? 12.721  3.961   56.792  1.00 80.51  ? 121  ALA A CB  1 
ATOM   751   N  N   . PHE A  1  96  ? 9.618   4.257   56.102  1.00 81.12  ? 122  PHE A N   1 
ATOM   752   C  CA  . PHE A  1  96  ? 8.621   4.613   55.112  1.00 81.92  ? 122  PHE A CA  1 
ATOM   753   C  C   . PHE A  1  96  ? 7.279   5.083   55.661  1.00 82.97  ? 122  PHE A C   1 
ATOM   754   O  O   . PHE A  1  96  ? 6.250   4.989   54.976  1.00 84.02  ? 122  PHE A O   1 
ATOM   755   C  CB  . PHE A  1  96  ? 8.433   3.432   54.170  1.00 80.81  ? 122  PHE A CB  1 
ATOM   756   C  CG  . PHE A  1  96  ? 9.692   3.040   53.457  1.00 78.12  ? 122  PHE A CG  1 
ATOM   757   C  CD1 . PHE A  1  96  ? 10.335  3.954   52.625  1.00 76.89  ? 122  PHE A CD1 1 
ATOM   758   C  CD2 . PHE A  1  96  ? 10.238  1.767   53.620  1.00 76.22  ? 122  PHE A CD2 1 
ATOM   759   C  CE1 . PHE A  1  96  ? 11.501  3.610   51.963  1.00 76.76  ? 122  PHE A CE1 1 
ATOM   760   C  CE2 . PHE A  1  96  ? 11.404  1.408   52.966  1.00 75.22  ? 122  PHE A CE2 1 
ATOM   761   C  CZ  . PHE A  1  96  ? 12.041  2.330   52.134  1.00 76.35  ? 122  PHE A CZ  1 
ATOM   762   N  N   . SER A  1  97  ? 7.291   5.601   56.887  1.00 82.90  ? 123  SER A N   1 
ATOM   763   C  CA  . SER A  1  97  ? 6.071   6.107   57.502  1.00 82.01  ? 123  SER A CA  1 
ATOM   764   C  C   . SER A  1  97  ? 5.768   7.515   56.977  1.00 80.94  ? 123  SER A C   1 
ATOM   765   O  O   . SER A  1  97  ? 6.665   8.370   56.904  1.00 80.12  ? 123  SER A O   1 
ATOM   766   C  CB  . SER A  1  97  ? 6.217   6.128   59.027  1.00 82.72  ? 123  SER A CB  1 
ATOM   767   O  OG  . SER A  1  97  ? 7.278   6.972   59.430  1.00 83.10  ? 123  SER A OG  1 
ATOM   768   N  N   . GLY A  1  98  ? 4.505   7.734   56.607  1.00 79.59  ? 124  GLY A N   1 
ATOM   769   C  CA  . GLY A  1  98  ? 4.078   9.021   56.082  1.00 78.11  ? 124  GLY A CA  1 
ATOM   770   C  C   . GLY A  1  98  ? 3.648   8.969   54.624  1.00 77.02  ? 124  GLY A C   1 
ATOM   771   O  O   . GLY A  1  98  ? 2.896   9.829   54.168  1.00 77.04  ? 124  GLY A O   1 
ATOM   772   N  N   . LEU A  1  99  ? 4.133   7.963   53.894  1.00 76.40  ? 125  LEU A N   1 
ATOM   773   C  CA  . LEU A  1  99  ? 3.809   7.784   52.477  1.00 75.34  ? 125  LEU A CA  1 
ATOM   774   C  C   . LEU A  1  99  ? 2.480   7.056   52.373  1.00 75.39  ? 125  LEU A C   1 
ATOM   775   O  O   . LEU A  1  99  ? 2.418   5.895   51.965  1.00 74.85  ? 125  LEU A O   1 
ATOM   776   C  CB  . LEU A  1  99  ? 4.891   6.952   51.768  1.00 74.80  ? 125  LEU A CB  1 
ATOM   777   C  CG  . LEU A  1  99  ? 6.368   7.359   51.619  1.00 72.09  ? 125  LEU A CG  1 
ATOM   778   C  CD1 . LEU A  1  99  ? 6.515   8.869   51.687  1.00 71.02  ? 125  LEU A CD1 1 
ATOM   779   C  CD2 . LEU A  1  99  ? 7.190   6.679   52.686  1.00 69.34  ? 125  LEU A CD2 1 
ATOM   780   N  N   . SER A  1  100 ? 1.421   7.758   52.752  1.00 75.78  ? 126  SER A N   1 
ATOM   781   C  CA  . SER A  1  100 ? 0.069   7.221   52.748  1.00 76.10  ? 126  SER A CA  1 
ATOM   782   C  C   . SER A  1  100 ? -0.505  7.084   51.343  1.00 75.76  ? 126  SER A C   1 
ATOM   783   O  O   . SER A  1  100 ? -1.629  6.600   51.171  1.00 75.26  ? 126  SER A O   1 
ATOM   784   C  CB  . SER A  1  100 ? -0.827  8.130   53.584  1.00 77.06  ? 126  SER A CB  1 
ATOM   785   O  OG  . SER A  1  100 ? -0.688  9.482   53.160  1.00 78.01  ? 126  SER A OG  1 
ATOM   786   N  N   . SER A  1  101 ? 0.270   7.505   50.347  1.00 74.64  ? 127  SER A N   1 
ATOM   787   C  CA  . SER A  1  101 ? -0.166  7.440   48.957  1.00 73.80  ? 127  SER A CA  1 
ATOM   788   C  C   . SER A  1  101 ? 0.819   6.740   48.038  1.00 72.89  ? 127  SER A C   1 
ATOM   789   O  O   . SER A  1  101 ? 0.658   6.774   46.817  1.00 73.16  ? 127  SER A O   1 
ATOM   790   C  CB  . SER A  1  101 ? -0.389  8.846   48.420  1.00 74.81  ? 127  SER A CB  1 
ATOM   791   O  OG  . SER A  1  101 ? -1.357  9.522   49.191  1.00 77.26  ? 127  SER A OG  1 
ATOM   792   N  N   . LEU A  1  102 ? 1.837   6.110   48.610  1.00 71.81  ? 128  LEU A N   1 
ATOM   793   C  CA  . LEU A  1  102 ? 2.837   5.440   47.790  1.00 70.31  ? 128  LEU A CA  1 
ATOM   794   C  C   . LEU A  1  102 ? 2.267   4.256   47.017  1.00 69.46  ? 128  LEU A C   1 
ATOM   795   O  O   . LEU A  1  102 ? 1.717   3.319   47.602  1.00 67.71  ? 128  LEU A O   1 
ATOM   796   C  CB  . LEU A  1  102 ? 4.010   4.966   48.648  1.00 68.33  ? 128  LEU A CB  1 
ATOM   797   C  CG  . LEU A  1  102 ? 5.312   4.739   47.884  1.00 66.39  ? 128  LEU A CG  1 
ATOM   798   C  CD1 . LEU A  1  102 ? 5.852   6.083   47.413  1.00 63.43  ? 128  LEU A CD1 1 
ATOM   799   C  CD2 . LEU A  1  102 ? 6.315   4.023   48.778  1.00 65.56  ? 128  LEU A CD2 1 
ATOM   800   N  N   . GLN A  1  103 ? 2.412   4.323   45.694  1.00 68.66  ? 129  GLN A N   1 
ATOM   801   C  CA  . GLN A  1  103 ? 1.940   3.280   44.804  1.00 66.76  ? 129  GLN A CA  1 
ATOM   802   C  C   . GLN A  1  103 ? 3.102   2.475   44.217  1.00 64.72  ? 129  GLN A C   1 
ATOM   803   O  O   . GLN A  1  103 ? 2.996   1.263   44.033  1.00 64.73  ? 129  GLN A O   1 
ATOM   804   C  CB  . GLN A  1  103 ? 1.117   3.899   43.673  1.00 67.97  ? 129  GLN A CB  1 
ATOM   805   C  CG  . GLN A  1  103 ? -0.121  4.612   44.156  1.00 71.78  ? 129  GLN A CG  1 
ATOM   806   C  CD  . GLN A  1  103 ? -1.072  4.938   43.036  1.00 74.07  ? 129  GLN A CD  1 
ATOM   807   O  OE1 . GLN A  1  103 ? -0.776  5.779   42.179  1.00 76.01  ? 129  GLN A OE1 1 
ATOM   808   N  NE2 . GLN A  1  103 ? -2.224  4.264   43.023  1.00 74.75  ? 129  GLN A NE2 1 
ATOM   809   N  N   . LYS A  1  104 ? 4.219   3.150   43.948  1.00 61.49  ? 130  LYS A N   1 
ATOM   810   C  CA  . LYS A  1  104 ? 5.381   2.509   43.349  1.00 57.80  ? 130  LYS A CA  1 
ATOM   811   C  C   . LYS A  1  104 ? 6.633   2.685   44.184  1.00 56.96  ? 130  LYS A C   1 
ATOM   812   O  O   . LYS A  1  104 ? 7.048   3.804   44.449  1.00 56.94  ? 130  LYS A O   1 
ATOM   813   C  CB  . LYS A  1  104 ? 5.594   3.101   41.956  1.00 56.69  ? 130  LYS A CB  1 
ATOM   814   C  CG  . LYS A  1  104 ? 6.750   2.540   41.155  1.00 56.07  ? 130  LYS A CG  1 
ATOM   815   C  CD  . LYS A  1  104 ? 6.795   3.221   39.793  1.00 54.94  ? 130  LYS A CD  1 
ATOM   816   C  CE  . LYS A  1  104 ? 7.915   2.714   38.902  1.00 52.96  ? 130  LYS A CE  1 
ATOM   817   N  NZ  . LYS A  1  104 ? 7.912   3.493   37.641  1.00 52.06  ? 130  LYS A NZ  1 
ATOM   818   N  N   . LEU A  1  105 ? 7.230   1.578   44.607  1.00 56.39  ? 131  LEU A N   1 
ATOM   819   C  CA  . LEU A  1  105 ? 8.457   1.632   45.398  1.00 55.60  ? 131  LEU A CA  1 
ATOM   820   C  C   . LEU A  1  105 ? 9.551   0.883   44.658  1.00 56.59  ? 131  LEU A C   1 
ATOM   821   O  O   . LEU A  1  105 ? 9.437   -0.320  44.423  1.00 57.18  ? 131  LEU A O   1 
ATOM   822   C  CB  . LEU A  1  105 ? 8.247   0.995   46.765  1.00 54.19  ? 131  LEU A CB  1 
ATOM   823   C  CG  . LEU A  1  105 ? 9.493   0.926   47.653  1.00 53.09  ? 131  LEU A CG  1 
ATOM   824   C  CD1 . LEU A  1  105 ? 10.004  2.322   47.932  1.00 52.04  ? 131  LEU A CD1 1 
ATOM   825   C  CD2 . LEU A  1  105 ? 9.173   0.206   48.954  1.00 52.22  ? 131  LEU A CD2 1 
ATOM   826   N  N   . VAL A  1  106 ? 10.613  1.593   44.292  1.00 56.75  ? 132  VAL A N   1 
ATOM   827   C  CA  . VAL A  1  106 ? 11.713  0.980   43.558  1.00 57.15  ? 132  VAL A CA  1 
ATOM   828   C  C   . VAL A  1  106 ? 12.967  0.864   44.424  1.00 58.55  ? 132  VAL A C   1 
ATOM   829   O  O   . VAL A  1  106 ? 13.610  1.867   44.732  1.00 58.59  ? 132  VAL A O   1 
ATOM   830   C  CB  . VAL A  1  106 ? 12.059  1.804   42.306  1.00 55.47  ? 132  VAL A CB  1 
ATOM   831   C  CG1 . VAL A  1  106 ? 12.951  1.006   41.391  1.00 56.08  ? 132  VAL A CG1 1 
ATOM   832   C  CG2 . VAL A  1  106 ? 10.807  2.211   41.588  1.00 53.34  ? 132  VAL A CG2 1 
ATOM   833   N  N   . ALA A  1  107 ? 13.307  -0.363  44.812  1.00 59.46  ? 133  ALA A N   1 
ATOM   834   C  CA  . ALA A  1  107 ? 14.490  -0.613  45.633  1.00 61.05  ? 133  ALA A CA  1 
ATOM   835   C  C   . ALA A  1  107 ? 15.448  -1.606  44.936  1.00 62.26  ? 133  ALA A C   1 
ATOM   836   O  O   . ALA A  1  107 ? 15.905  -2.597  45.537  1.00 62.75  ? 133  ALA A O   1 
ATOM   837   C  CB  . ALA A  1  107 ? 14.061  -1.153  47.001  1.00 59.86  ? 133  ALA A CB  1 
ATOM   838   N  N   . VAL A  1  108 ? 15.750  -1.333  43.666  1.00 61.67  ? 134  VAL A N   1 
ATOM   839   C  CA  . VAL A  1  108 ? 16.631  -2.193  42.887  1.00 61.20  ? 134  VAL A CA  1 
ATOM   840   C  C   . VAL A  1  108 ? 18.066  -1.964  43.304  1.00 62.25  ? 134  VAL A C   1 
ATOM   841   O  O   . VAL A  1  108 ? 18.496  -0.816  43.423  1.00 62.96  ? 134  VAL A O   1 
ATOM   842   C  CB  . VAL A  1  108 ? 16.504  -1.908  41.384  1.00 60.15  ? 134  VAL A CB  1 
ATOM   843   C  CG1 . VAL A  1  108 ? 17.504  -2.740  40.609  1.00 58.62  ? 134  VAL A CG1 1 
ATOM   844   C  CG2 . VAL A  1  108 ? 15.106  -2.218  40.926  1.00 59.40  ? 134  VAL A CG2 1 
ATOM   845   N  N   . GLU A  1  109 ? 18.801  -3.059  43.508  1.00 62.91  ? 135  GLU A N   1 
ATOM   846   C  CA  . GLU A  1  109 ? 20.200  -3.003  43.933  1.00 63.05  ? 135  GLU A CA  1 
ATOM   847   C  C   . GLU A  1  109 ? 20.347  -2.034  45.102  1.00 63.55  ? 135  GLU A C   1 
ATOM   848   O  O   . GLU A  1  109 ? 20.945  -0.968  44.966  1.00 62.75  ? 135  GLU A O   1 
ATOM   849   C  CB  . GLU A  1  109 ? 21.111  -2.587  42.771  1.00 63.38  ? 135  GLU A CB  1 
ATOM   850   C  CG  . GLU A  1  109 ? 22.575  -2.471  43.170  1.00 67.21  ? 135  GLU A CG  1 
ATOM   851   C  CD  . GLU A  1  109 ? 23.557  -2.336  41.987  1.00 68.61  ? 135  GLU A CD  1 
ATOM   852   O  OE1 . GLU A  1  109 ? 23.298  -1.521  41.071  1.00 68.30  ? 135  GLU A OE1 1 
ATOM   853   O  OE2 . GLU A  1  109 ? 24.606  -3.037  41.997  1.00 68.93  ? 135  GLU A OE2 1 
ATOM   854   N  N   . THR A  1  110 ? 19.763  -2.416  46.239  1.00 64.30  ? 136  THR A N   1 
ATOM   855   C  CA  . THR A  1  110 ? 19.802  -1.631  47.472  1.00 65.29  ? 136  THR A CA  1 
ATOM   856   C  C   . THR A  1  110 ? 20.304  -2.497  48.623  1.00 66.33  ? 136  THR A C   1 
ATOM   857   O  O   . THR A  1  110 ? 19.938  -2.292  49.784  1.00 65.90  ? 136  THR A O   1 
ATOM   858   C  CB  . THR A  1  110 ? 18.409  -1.064  47.863  1.00 65.42  ? 136  THR A CB  1 
ATOM   859   O  OG1 . THR A  1  110 ? 17.447  -2.123  47.909  1.00 66.88  ? 136  THR A OG1 1 
ATOM   860   C  CG2 . THR A  1  110 ? 17.957  -0.009  46.874  1.00 65.46  ? 136  THR A CG2 1 
ATOM   861   N  N   . ASN A  1  111 ? 21.125  -3.483  48.281  1.00 67.74  ? 137  ASN A N   1 
ATOM   862   C  CA  . ASN A  1  111 ? 21.719  -4.377  49.263  1.00 69.87  ? 137  ASN A CA  1 
ATOM   863   C  C   . ASN A  1  111 ? 20.702  -5.152  50.094  1.00 70.87  ? 137  ASN A C   1 
ATOM   864   O  O   . ASN A  1  111 ? 21.061  -5.787  51.085  1.00 72.22  ? 137  ASN A O   1 
ATOM   865   C  CB  . ASN A  1  111 ? 22.616  -3.566  50.188  1.00 71.51  ? 137  ASN A CB  1 
ATOM   866   C  CG  . ASN A  1  111 ? 23.797  -4.362  50.696  1.00 74.39  ? 137  ASN A CG  1 
ATOM   867   O  OD1 . ASN A  1  111 ? 24.650  -4.793  49.917  1.00 76.39  ? 137  ASN A OD1 1 
ATOM   868   N  ND2 . ASN A  1  111 ? 23.862  -4.556  52.009  1.00 74.74  ? 137  ASN A ND2 1 
ATOM   869   N  N   . LEU A  1  112 ? 19.436  -5.100  49.691  1.00 71.35  ? 138  LEU A N   1 
ATOM   870   C  CA  . LEU A  1  112 ? 18.358  -5.782  50.403  1.00 71.20  ? 138  LEU A CA  1 
ATOM   871   C  C   . LEU A  1  112 ? 18.598  -7.285  50.445  1.00 71.80  ? 138  LEU A C   1 
ATOM   872   O  O   . LEU A  1  112 ? 18.658  -7.931  49.409  1.00 70.95  ? 138  LEU A O   1 
ATOM   873   C  CB  . LEU A  1  112 ? 17.037  -5.481  49.710  1.00 70.65  ? 138  LEU A CB  1 
ATOM   874   C  CG  . LEU A  1  112 ? 15.793  -5.469  50.581  1.00 70.17  ? 138  LEU A CG  1 
ATOM   875   C  CD1 . LEU A  1  112 ? 14.642  -4.957  49.752  1.00 71.37  ? 138  LEU A CD1 1 
ATOM   876   C  CD2 . LEU A  1  112 ? 15.508  -6.845  51.126  1.00 69.66  ? 138  LEU A CD2 1 
ATOM   877   N  N   . ALA A  1  113 ? 18.725  -7.840  51.646  1.00 73.82  ? 139  ALA A N   1 
ATOM   878   C  CA  . ALA A  1  113 ? 18.994  -9.271  51.804  1.00 75.79  ? 139  ALA A CA  1 
ATOM   879   C  C   . ALA A  1  113 ? 17.789  -10.158 52.130  1.00 77.58  ? 139  ALA A C   1 
ATOM   880   O  O   . ALA A  1  113 ? 17.832  -11.376 51.919  1.00 77.26  ? 139  ALA A O   1 
ATOM   881   C  CB  . ALA A  1  113 ? 20.074  -9.471  52.858  1.00 75.28  ? 139  ALA A CB  1 
ATOM   882   N  N   . SER A  1  114 ? 16.721  -9.562  52.655  1.00 79.58  ? 140  SER A N   1 
ATOM   883   C  CA  . SER A  1  114 ? 15.523  -10.325 52.991  1.00 80.15  ? 140  SER A CA  1 
ATOM   884   C  C   . SER A  1  114 ? 14.273  -9.470  52.929  1.00 80.24  ? 140  SER A C   1 
ATOM   885   O  O   . SER A  1  114 ? 14.253  -8.333  53.393  1.00 79.98  ? 140  SER A O   1 
ATOM   886   C  CB  . SER A  1  114 ? 15.643  -10.930 54.389  1.00 81.14  ? 140  SER A CB  1 
ATOM   887   O  OG  . SER A  1  114 ? 14.514  -11.740 54.685  1.00 83.61  ? 140  SER A OG  1 
ATOM   888   N  N   . LEU A  1  115 ? 13.225  -10.038 52.353  1.00 81.13  ? 141  LEU A N   1 
ATOM   889   C  CA  . LEU A  1  115 ? 11.951  -9.353  52.220  1.00 82.05  ? 141  LEU A CA  1 
ATOM   890   C  C   . LEU A  1  115 ? 11.282  -9.304  53.601  1.00 83.08  ? 141  LEU A C   1 
ATOM   891   O  O   . LEU A  1  115 ? 10.401  -8.479  53.848  1.00 83.22  ? 141  LEU A O   1 
ATOM   892   C  CB  . LEU A  1  115 ? 11.077  -10.128 51.227  1.00 80.63  ? 141  LEU A CB  1 
ATOM   893   C  CG  . LEU A  1  115 ? 10.137  -9.396  50.272  1.00 78.82  ? 141  LEU A CG  1 
ATOM   894   C  CD1 . LEU A  1  115 ? 10.931  -8.413  49.430  1.00 79.71  ? 141  LEU A CD1 1 
ATOM   895   C  CD2 . LEU A  1  115 ? 9.437   -10.408 49.386  1.00 77.08  ? 141  LEU A CD2 1 
ATOM   896   N  N   . GLU A  1  116 ? 11.727  -10.193 54.493  1.00 83.89  ? 142  GLU A N   1 
ATOM   897   C  CA  . GLU A  1  116 ? 11.203  -10.317 55.857  1.00 84.55  ? 142  GLU A CA  1 
ATOM   898   C  C   . GLU A  1  116 ? 11.229  -9.052  56.705  1.00 83.97  ? 142  GLU A C   1 
ATOM   899   O  O   . GLU A  1  116 ? 10.248  -8.710  57.362  1.00 83.70  ? 142  GLU A O   1 
ATOM   900   C  CB  . GLU A  1  116 ? 11.960  -11.413 56.615  1.00 85.84  ? 142  GLU A CB  1 
ATOM   901   C  CG  . GLU A  1  116 ? 11.510  -12.841 56.327  1.00 89.86  ? 142  GLU A CG  1 
ATOM   902   C  CD  . GLU A  1  116 ? 10.070  -13.112 56.764  1.00 92.48  ? 142  GLU A CD  1 
ATOM   903   O  OE1 . GLU A  1  116 ? 9.664   -12.598 57.836  1.00 92.69  ? 142  GLU A OE1 1 
ATOM   904   O  OE2 . GLU A  1  116 ? 9.348   -13.847 56.045  1.00 93.78  ? 142  GLU A OE2 1 
ATOM   905   N  N   . ASN A  1  117 ? 12.351  -8.355  56.711  1.00 84.08  ? 143  ASN A N   1 
ATOM   906   C  CA  . ASN A  1  117 ? 12.446  -7.164  57.531  1.00 84.83  ? 143  ASN A CA  1 
ATOM   907   C  C   . ASN A  1  117 ? 12.244  -5.837  56.821  1.00 84.33  ? 143  ASN A C   1 
ATOM   908   O  O   . ASN A  1  117 ? 12.441  -4.788  57.428  1.00 85.30  ? 143  ASN A O   1 
ATOM   909   C  CB  . ASN A  1  117 ? 13.782  -7.162  58.266  1.00 86.71  ? 143  ASN A CB  1 
ATOM   910   C  CG  . ASN A  1  117 ? 13.971  -8.402  59.126  1.00 88.75  ? 143  ASN A CG  1 
ATOM   911   O  OD1 . ASN A  1  117 ? 13.126  -8.726  59.962  1.00 89.61  ? 143  ASN A OD1 1 
ATOM   912   N  ND2 . ASN A  1  117 ? 15.089  -9.100  58.928  1.00 89.61  ? 143  ASN A ND2 1 
ATOM   913   N  N   . PHE A  1  118 ? 11.843  -5.872  55.553  1.00 83.00  ? 144  PHE A N   1 
ATOM   914   C  CA  . PHE A  1  118 ? 11.604  -4.648  54.781  1.00 81.69  ? 144  PHE A CA  1 
ATOM   915   C  C   . PHE A  1  118 ? 10.338  -3.979  55.373  1.00 81.74  ? 144  PHE A C   1 
ATOM   916   O  O   . PHE A  1  118 ? 9.228   -4.499  55.251  1.00 82.20  ? 144  PHE A O   1 
ATOM   917   C  CB  . PHE A  1  118 ? 11.425  -5.031  53.298  1.00 79.35  ? 144  PHE A CB  1 
ATOM   918   C  CG  . PHE A  1  118 ? 11.798  -3.941  52.324  1.00 76.24  ? 144  PHE A CG  1 
ATOM   919   C  CD1 . PHE A  1  118 ? 12.964  -3.204  52.489  1.00 73.95  ? 144  PHE A CD1 1 
ATOM   920   C  CD2 . PHE A  1  118 ? 10.985  -3.669  51.229  1.00 74.70  ? 144  PHE A CD2 1 
ATOM   921   C  CE1 . PHE A  1  118 ? 13.310  -2.212  51.581  1.00 72.03  ? 144  PHE A CE1 1 
ATOM   922   C  CE2 . PHE A  1  118 ? 11.325  -2.679  50.318  1.00 73.23  ? 144  PHE A CE2 1 
ATOM   923   C  CZ  . PHE A  1  118 ? 12.492  -1.949  50.494  1.00 72.07  ? 144  PHE A CZ  1 
ATOM   924   N  N   . PRO A  1  119 ? 10.495  -2.812  56.024  1.00 81.71  ? 145  PRO A N   1 
ATOM   925   C  CA  . PRO A  1  119 ? 9.387   -2.073  56.653  1.00 81.78  ? 145  PRO A CA  1 
ATOM   926   C  C   . PRO A  1  119 ? 8.361   -1.382  55.753  1.00 81.37  ? 145  PRO A C   1 
ATOM   927   O  O   . PRO A  1  119 ? 8.244   -0.150  55.781  1.00 81.58  ? 145  PRO A O   1 
ATOM   928   C  CB  . PRO A  1  119 ? 10.122  -1.072  57.537  1.00 81.54  ? 145  PRO A CB  1 
ATOM   929   C  CG  . PRO A  1  119 ? 11.283  -0.707  56.665  1.00 82.07  ? 145  PRO A CG  1 
ATOM   930   C  CD  . PRO A  1  119 ? 11.753  -2.049  56.128  1.00 81.24  ? 145  PRO A CD  1 
ATOM   931   N  N   . ILE A  1  120 ? 7.601   -2.168  54.991  1.00 80.37  ? 146  ILE A N   1 
ATOM   932   C  CA  . ILE A  1  120 ? 6.595   -1.616  54.079  1.00 79.55  ? 146  ILE A CA  1 
ATOM   933   C  C   . ILE A  1  120 ? 5.171   -2.113  54.348  1.00 80.05  ? 146  ILE A C   1 
ATOM   934   O  O   . ILE A  1  120 ? 4.210   -1.602  53.750  1.00 79.98  ? 146  ILE A O   1 
ATOM   935   C  CB  . ILE A  1  120 ? 6.928   -1.952  52.605  1.00 77.57  ? 146  ILE A CB  1 
ATOM   936   C  CG1 . ILE A  1  120 ? 7.250   -3.439  52.482  1.00 76.41  ? 146  ILE A CG1 1 
ATOM   937   C  CG2 . ILE A  1  120 ? 8.072   -1.104  52.112  1.00 76.45  ? 146  ILE A CG2 1 
ATOM   938   C  CD1 . ILE A  1  120 ? 7.332   -3.933  51.063  1.00 75.49  ? 146  ILE A CD1 1 
ATOM   939   N  N   . GLY A  1  121 ? 5.053   -3.098  55.242  1.00 79.11  ? 147  GLY A N   1 
ATOM   940   C  CA  . GLY A  1  121 ? 3.769   -3.697  55.578  1.00 77.49  ? 147  GLY A CA  1 
ATOM   941   C  C   . GLY A  1  121 ? 2.564   -2.803  55.838  1.00 77.12  ? 147  GLY A C   1 
ATOM   942   O  O   . GLY A  1  121 ? 1.456   -3.312  55.972  1.00 76.20  ? 147  GLY A O   1 
ATOM   943   N  N   . HIS A  1  122 ? 2.752   -1.488  55.910  1.00 77.18  ? 148  HIS A N   1 
ATOM   944   C  CA  . HIS A  1  122 ? 1.638   -0.585  56.168  1.00 78.17  ? 148  HIS A CA  1 
ATOM   945   C  C   . HIS A  1  122 ? 1.196   0.212   54.946  1.00 78.81  ? 148  HIS A C   1 
ATOM   946   O  O   . HIS A  1  122 ? 0.165   0.891   54.980  1.00 79.42  ? 148  HIS A O   1 
ATOM   947   C  CB  . HIS A  1  122 ? 2.001   0.390   57.281  1.00 78.60  ? 148  HIS A CB  1 
ATOM   948   C  CG  . HIS A  1  122 ? 3.190   1.238   56.967  1.00 79.86  ? 148  HIS A CG  1 
ATOM   949   N  ND1 . HIS A  1  122 ? 4.481   0.776   57.088  1.00 80.52  ? 148  HIS A ND1 1 
ATOM   950   C  CD2 . HIS A  1  122 ? 3.283   2.513   56.516  1.00 80.59  ? 148  HIS A CD2 1 
ATOM   951   C  CE1 . HIS A  1  122 ? 5.322   1.731   56.727  1.00 81.35  ? 148  HIS A CE1 1 
ATOM   952   N  NE2 . HIS A  1  122 ? 4.621   2.793   56.375  1.00 81.28  ? 148  HIS A NE2 1 
ATOM   953   N  N   . LEU A  1  123 ? 1.983   0.140   53.878  1.00 79.27  ? 149  LEU A N   1 
ATOM   954   C  CA  . LEU A  1  123 ? 1.682   0.856   52.641  1.00 79.69  ? 149  LEU A CA  1 
ATOM   955   C  C   . LEU A  1  123 ? 0.602   0.088   51.867  1.00 79.97  ? 149  LEU A C   1 
ATOM   956   O  O   . LEU A  1  123 ? 0.901   -0.683  50.954  1.00 80.69  ? 149  LEU A O   1 
ATOM   957   C  CB  . LEU A  1  123 ? 2.972   0.979   51.817  1.00 79.38  ? 149  LEU A CB  1 
ATOM   958   C  CG  . LEU A  1  123 ? 4.160   1.607   52.561  1.00 79.38  ? 149  LEU A CG  1 
ATOM   959   C  CD1 . LEU A  1  123 ? 5.444   1.296   51.830  1.00 79.06  ? 149  LEU A CD1 1 
ATOM   960   C  CD2 . LEU A  1  123 ? 3.966   3.121   52.698  1.00 80.02  ? 149  LEU A CD2 1 
ATOM   961   N  N   . LYS A  1  124 ? -0.657  0.304   52.238  1.00 79.82  ? 150  LYS A N   1 
ATOM   962   C  CA  . LYS A  1  124 ? -1.775  -0.398  51.612  1.00 79.75  ? 150  LYS A CA  1 
ATOM   963   C  C   . LYS A  1  124 ? -2.015  0.005   50.158  1.00 79.27  ? 150  LYS A C   1 
ATOM   964   O  O   . LYS A  1  124 ? -2.494  -0.800  49.351  1.00 79.83  ? 150  LYS A O   1 
ATOM   965   C  CB  . LYS A  1  124 ? -3.052  -0.174  52.436  1.00 80.50  ? 150  LYS A CB  1 
ATOM   966   C  CG  . LYS A  1  124 ? -3.697  1.190   52.229  1.00 83.47  ? 150  LYS A CG  1 
ATOM   967   C  CD  . LYS A  1  124 ? -4.417  1.698   53.485  1.00 85.65  ? 150  LYS A CD  1 
ATOM   968   C  CE  . LYS A  1  124 ? -3.440  2.267   54.524  1.00 85.93  ? 150  LYS A CE  1 
ATOM   969   N  NZ  . LYS A  1  124 ? -2.648  3.422   53.992  1.00 85.33  ? 150  LYS A NZ  1 
ATOM   970   N  N   . THR A  1  125 ? -1.663  1.241   49.819  1.00 77.21  ? 151  THR A N   1 
ATOM   971   C  CA  . THR A  1  125 ? -1.866  1.742   48.466  1.00 75.26  ? 151  THR A CA  1 
ATOM   972   C  C   . THR A  1  125 ? -0.841  1.246   47.434  1.00 75.22  ? 151  THR A C   1 
ATOM   973   O  O   . THR A  1  125 ? -0.996  1.488   46.229  1.00 75.48  ? 151  THR A O   1 
ATOM   974   C  CB  . THR A  1  125 ? -1.850  3.273   48.465  1.00 73.86  ? 151  THR A CB  1 
ATOM   975   O  OG1 . THR A  1  125 ? -0.599  3.739   48.983  1.00 71.44  ? 151  THR A OG1 1 
ATOM   976   C  CG2 . THR A  1  125 ? -2.976  3.804   49.318  1.00 71.81  ? 151  THR A CG2 1 
ATOM   977   N  N   . LEU A  1  126 ? 0.184   0.542   47.910  1.00 73.82  ? 152  LEU A N   1 
ATOM   978   C  CA  . LEU A  1  126 ? 1.265   0.027   47.067  1.00 72.46  ? 152  LEU A CA  1 
ATOM   979   C  C   . LEU A  1  126 ? 0.793   -0.855  45.916  1.00 72.69  ? 152  LEU A C   1 
ATOM   980   O  O   . LEU A  1  126 ? 0.276   -1.947  46.152  1.00 72.11  ? 152  LEU A O   1 
ATOM   981   C  CB  . LEU A  1  126 ? 2.255   -0.759  47.930  1.00 70.15  ? 152  LEU A CB  1 
ATOM   982   C  CG  . LEU A  1  126 ? 3.661   -1.014  47.385  1.00 68.88  ? 152  LEU A CG  1 
ATOM   983   C  CD1 . LEU A  1  126 ? 4.405   0.303   47.246  1.00 67.77  ? 152  LEU A CD1 1 
ATOM   984   C  CD2 . LEU A  1  126 ? 4.408   -1.947  48.321  1.00 66.77  ? 152  LEU A CD2 1 
ATOM   985   N  N   . LYS A  1  127 ? 0.986   -0.378  44.679  1.00 73.07  ? 153  LYS A N   1 
ATOM   986   C  CA  . LYS A  1  127 ? 0.598   -1.112  43.467  1.00 72.55  ? 153  LYS A CA  1 
ATOM   987   C  C   . LYS A  1  127 ? 1.736   -2.004  42.970  1.00 71.47  ? 153  LYS A C   1 
ATOM   988   O  O   . LYS A  1  127 ? 1.514   -3.178  42.648  1.00 71.82  ? 153  LYS A O   1 
ATOM   989   C  CB  . LYS A  1  127 ? 0.204   -0.150  42.339  1.00 74.07  ? 153  LYS A CB  1 
ATOM   990   C  CG  . LYS A  1  127 ? -1.014  0.720   42.625  1.00 77.88  ? 153  LYS A CG  1 
ATOM   991   C  CD  . LYS A  1  127 ? -1.439  1.512   41.383  1.00 79.88  ? 153  LYS A CD  1 
ATOM   992   C  CE  . LYS A  1  127 ? -2.098  0.604   40.353  1.00 82.05  ? 153  LYS A CE  1 
ATOM   993   N  NZ  . LYS A  1  127 ? -3.314  -0.057  40.924  1.00 83.17  ? 153  LYS A NZ  1 
ATOM   994   N  N   . GLU A  1  128 ? 2.947   -1.445  42.900  1.00 69.44  ? 154  GLU A N   1 
ATOM   995   C  CA  . GLU A  1  128 ? 4.115   -2.199  42.448  1.00 66.27  ? 154  GLU A CA  1 
ATOM   996   C  C   . GLU A  1  128 ? 5.353   -2.027  43.335  1.00 63.16  ? 154  GLU A C   1 
ATOM   997   O  O   . GLU A  1  128 ? 5.694   -0.930  43.765  1.00 62.24  ? 154  GLU A O   1 
ATOM   998   C  CB  . GLU A  1  128 ? 4.437   -1.849  40.989  1.00 67.51  ? 154  GLU A CB  1 
ATOM   999   C  CG  . GLU A  1  128 ? 4.823   -0.404  40.717  1.00 71.17  ? 154  GLU A CG  1 
ATOM   1000  C  CD  . GLU A  1  128 ? 4.930   -0.101  39.217  1.00 73.45  ? 154  GLU A CD  1 
ATOM   1001  O  OE1 . GLU A  1  128 ? 3.889   -0.179  38.530  1.00 73.77  ? 154  GLU A OE1 1 
ATOM   1002  O  OE2 . GLU A  1  128 ? 6.045   0.206   38.724  1.00 73.99  ? 154  GLU A OE2 1 
ATOM   1003  N  N   . LEU A  1  129 ? 6.014   -3.147  43.602  1.00 61.57  ? 155  LEU A N   1 
ATOM   1004  C  CA  . LEU A  1  129 ? 7.209   -3.193  44.442  1.00 59.89  ? 155  LEU A CA  1 
ATOM   1005  C  C   . LEU A  1  129 ? 8.342   -3.885  43.672  1.00 59.83  ? 155  LEU A C   1 
ATOM   1006  O  O   . LEU A  1  129 ? 8.302   -5.090  43.445  1.00 60.19  ? 155  LEU A O   1 
ATOM   1007  C  CB  . LEU A  1  129 ? 6.871   -3.959  45.727  1.00 58.10  ? 155  LEU A CB  1 
ATOM   1008  C  CG  . LEU A  1  129 ? 7.819   -4.075  46.918  1.00 56.38  ? 155  LEU A CG  1 
ATOM   1009  C  CD1 . LEU A  1  129 ? 8.562   -5.364  46.820  1.00 56.76  ? 155  LEU A CD1 1 
ATOM   1010  C  CD2 . LEU A  1  129 ? 8.756   -2.888  46.988  1.00 55.24  ? 155  LEU A CD2 1 
ATOM   1011  N  N   . ASN A  1  130 ? 9.341   -3.106  43.266  1.00 60.18  ? 156  ASN A N   1 
ATOM   1012  C  CA  . ASN A  1  130 ? 10.476  -3.618  42.498  1.00 61.02  ? 156  ASN A CA  1 
ATOM   1013  C  C   . ASN A  1  130 ? 11.726  -3.786  43.359  1.00 61.64  ? 156  ASN A C   1 
ATOM   1014  O  O   . ASN A  1  130 ? 12.342  -2.800  43.777  1.00 61.65  ? 156  ASN A O   1 
ATOM   1015  C  CB  . ASN A  1  130 ? 10.786  -2.663  41.334  1.00 61.18  ? 156  ASN A CB  1 
ATOM   1016  C  CG  . ASN A  1  130 ? 11.853  -3.202  40.399  1.00 61.69  ? 156  ASN A CG  1 
ATOM   1017  O  OD1 . ASN A  1  130 ? 12.208  -2.553  39.411  1.00 61.67  ? 156  ASN A OD1 1 
ATOM   1018  N  ND2 . ASN A  1  130 ? 12.369  -4.395  40.703  1.00 60.20  ? 156  ASN A ND2 1 
ATOM   1019  N  N   . VAL A  1  131 ? 12.101  -5.034  43.620  1.00 61.63  ? 157  VAL A N   1 
ATOM   1020  C  CA  . VAL A  1  131 ? 13.279  -5.315  44.437  1.00 61.69  ? 157  VAL A CA  1 
ATOM   1021  C  C   . VAL A  1  131 ? 14.232  -6.262  43.704  1.00 62.82  ? 157  VAL A C   1 
ATOM   1022  O  O   . VAL A  1  131 ? 14.730  -7.234  44.281  1.00 62.58  ? 157  VAL A O   1 
ATOM   1023  C  CB  . VAL A  1  131 ? 12.878  -5.941  45.806  1.00 60.46  ? 157  VAL A CB  1 
ATOM   1024  C  CG1 . VAL A  1  131 ? 12.222  -4.901  46.682  1.00 59.34  ? 157  VAL A CG1 1 
ATOM   1025  C  CG2 . VAL A  1  131 ? 11.927  -7.107  45.596  1.00 58.59  ? 157  VAL A CG2 1 
ATOM   1026  N  N   . ALA A  1  132 ? 14.480  -5.972  42.428  1.00 62.86  ? 158  ALA A N   1 
ATOM   1027  C  CA  . ALA A  1  132 ? 15.356  -6.801  41.608  1.00 62.79  ? 158  ALA A CA  1 
ATOM   1028  C  C   . ALA A  1  132 ? 16.806  -6.436  41.804  1.00 63.81  ? 158  ALA A C   1 
ATOM   1029  O  O   . ALA A  1  132 ? 17.114  -5.322  42.221  1.00 65.05  ? 158  ALA A O   1 
ATOM   1030  C  CB  . ALA A  1  132 ? 14.994  -6.653  40.152  1.00 61.90  ? 158  ALA A CB  1 
ATOM   1031  N  N   . HIS A  1  133 ? 17.694  -7.380  41.501  1.00 65.02  ? 159  HIS A N   1 
ATOM   1032  C  CA  . HIS A  1  133 ? 19.140  -7.176  41.628  1.00 65.36  ? 159  HIS A CA  1 
ATOM   1033  C  C   . HIS A  1  133 ? 19.517  -7.006  43.107  1.00 65.71  ? 159  HIS A C   1 
ATOM   1034  O  O   . HIS A  1  133 ? 20.184  -6.042  43.489  1.00 66.34  ? 159  HIS A O   1 
ATOM   1035  C  CB  . HIS A  1  133 ? 19.556  -5.939  40.815  1.00 66.12  ? 159  HIS A CB  1 
ATOM   1036  C  CG  . HIS A  1  133 ? 21.012  -5.890  40.466  1.00 67.49  ? 159  HIS A CG  1 
ATOM   1037  N  ND1 . HIS A  1  133 ? 21.575  -4.828  39.788  1.00 68.43  ? 159  HIS A ND1 1 
ATOM   1038  C  CD2 . HIS A  1  133 ? 22.018  -6.765  40.697  1.00 68.33  ? 159  HIS A CD2 1 
ATOM   1039  C  CE1 . HIS A  1  133 ? 22.866  -5.051  39.620  1.00 68.23  ? 159  HIS A CE1 1 
ATOM   1040  N  NE2 . HIS A  1  133 ? 23.160  -6.220  40.163  1.00 68.99  ? 159  HIS A NE2 1 
ATOM   1041  N  N   . ASN A  1  134 ? 19.076  -7.950  43.933  1.00 65.61  ? 160  ASN A N   1 
ATOM   1042  C  CA  . ASN A  1  134 ? 19.342  -7.919  45.362  1.00 65.65  ? 160  ASN A CA  1 
ATOM   1043  C  C   . ASN A  1  134 ? 19.754  -9.302  45.881  1.00 66.68  ? 160  ASN A C   1 
ATOM   1044  O  O   . ASN A  1  134 ? 19.756  -10.278 45.130  1.00 67.61  ? 160  ASN A O   1 
ATOM   1045  C  CB  . ASN A  1  134 ? 18.114  -7.390  46.107  1.00 65.28  ? 160  ASN A CB  1 
ATOM   1046  C  CG  . ASN A  1  134 ? 17.984  -5.870  46.020  1.00 65.85  ? 160  ASN A CG  1 
ATOM   1047  O  OD1 . ASN A  1  134 ? 18.752  -5.145  46.638  1.00 67.17  ? 160  ASN A OD1 1 
ATOM   1048  N  ND2 . ASN A  1  134 ? 17.010  -5.389  45.251  1.00 64.85  ? 160  ASN A ND2 1 
ATOM   1049  N  N   . LEU A  1  135 ? 20.086  -9.383  47.170  1.00 67.39  ? 161  LEU A N   1 
ATOM   1050  C  CA  . LEU A  1  135 ? 20.578  -10.620 47.804  1.00 66.56  ? 161  LEU A CA  1 
ATOM   1051  C  C   . LEU A  1  135 ? 19.562  -11.589 48.424  1.00 66.84  ? 161  LEU A C   1 
ATOM   1052  O  O   . LEU A  1  135 ? 19.917  -12.406 49.276  1.00 66.59  ? 161  LEU A O   1 
ATOM   1053  C  CB  . LEU A  1  135 ? 21.604  -10.230 48.870  1.00 64.38  ? 161  LEU A CB  1 
ATOM   1054  C  CG  . LEU A  1  135 ? 22.539  -9.121  48.387  1.00 62.21  ? 161  LEU A CG  1 
ATOM   1055  C  CD1 . LEU A  1  135 ? 23.157  -8.427  49.568  1.00 62.29  ? 161  LEU A CD1 1 
ATOM   1056  C  CD2 . LEU A  1  135 ? 23.583  -9.696  47.455  1.00 60.82  ? 161  LEU A CD2 1 
ATOM   1057  N  N   . ILE A  1  136 ? 18.312  -11.513 47.988  1.00 67.51  ? 162  ILE A N   1 
ATOM   1058  C  CA  . ILE A  1  136 ? 17.265  -12.367 48.524  1.00 67.24  ? 162  ILE A CA  1 
ATOM   1059  C  C   . ILE A  1  136 ? 17.469  -13.828 48.156  1.00 68.63  ? 162  ILE A C   1 
ATOM   1060  O  O   . ILE A  1  136 ? 17.695  -14.147 46.994  1.00 68.80  ? 162  ILE A O   1 
ATOM   1061  C  CB  . ILE A  1  136 ? 15.891  -11.881 48.032  1.00 65.91  ? 162  ILE A CB  1 
ATOM   1062  C  CG1 . ILE A  1  136 ? 15.634  -10.463 48.569  1.00 63.65  ? 162  ILE A CG1 1 
ATOM   1063  C  CG2 . ILE A  1  136 ? 14.809  -12.866 48.452  1.00 66.12  ? 162  ILE A CG2 1 
ATOM   1064  C  CD1 . ILE A  1  136 ? 14.340  -9.841  48.115  1.00 62.26  ? 162  ILE A CD1 1 
ATOM   1065  N  N   . GLN A  1  137 ? 17.379  -14.710 49.155  1.00 70.83  ? 163  GLN A N   1 
ATOM   1066  C  CA  . GLN A  1  137 ? 17.575  -16.154 48.953  1.00 71.53  ? 163  GLN A CA  1 
ATOM   1067  C  C   . GLN A  1  137 ? 16.333  -17.003 49.084  1.00 72.02  ? 163  GLN A C   1 
ATOM   1068  O  O   . GLN A  1  137 ? 16.290  -18.123 48.570  1.00 71.21  ? 163  GLN A O   1 
ATOM   1069  C  CB  . GLN A  1  137 ? 18.598  -16.699 49.937  1.00 71.41  ? 163  GLN A CB  1 
ATOM   1070  C  CG  . GLN A  1  137 ? 20.019  -16.558 49.489  1.00 72.93  ? 163  GLN A CG  1 
ATOM   1071  C  CD  . GLN A  1  137 ? 20.949  -16.458 50.662  1.00 73.20  ? 163  GLN A CD  1 
ATOM   1072  O  OE1 . GLN A  1  137 ? 20.945  -15.458 51.384  1.00 72.59  ? 163  GLN A OE1 1 
ATOM   1073  N  NE2 . GLN A  1  137 ? 21.750  -17.495 50.873  1.00 73.46  ? 163  GLN A NE2 1 
ATOM   1074  N  N   . SER A  1  138 ? 15.334  -16.472 49.779  1.00 72.98  ? 164  SER A N   1 
ATOM   1075  C  CA  . SER A  1  138 ? 14.093  -17.190 50.005  1.00 74.09  ? 164  SER A CA  1 
ATOM   1076  C  C   . SER A  1  138 ? 12.925  -16.584 49.247  1.00 74.96  ? 164  SER A C   1 
ATOM   1077  O  O   . SER A  1  138 ? 12.885  -15.374 49.031  1.00 74.81  ? 164  SER A O   1 
ATOM   1078  C  CB  . SER A  1  138 ? 13.788  -17.188 51.499  1.00 73.85  ? 164  SER A CB  1 
ATOM   1079  O  OG  . SER A  1  138 ? 12.581  -17.867 51.771  1.00 76.52  ? 164  SER A OG  1 
ATOM   1080  N  N   . PHE A  1  139 ? 11.976  -17.427 48.843  1.00 76.55  ? 165  PHE A N   1 
ATOM   1081  C  CA  . PHE A  1  139 ? 10.789  -16.949 48.135  1.00 78.34  ? 165  PHE A CA  1 
ATOM   1082  C  C   . PHE A  1  139 ? 9.617   -16.812 49.105  1.00 79.94  ? 165  PHE A C   1 
ATOM   1083  O  O   . PHE A  1  139 ? 8.546   -16.339 48.731  1.00 80.57  ? 165  PHE A O   1 
ATOM   1084  C  CB  . PHE A  1  139 ? 10.392  -17.902 47.009  1.00 78.12  ? 165  PHE A CB  1 
ATOM   1085  C  CG  . PHE A  1  139 ? 9.210   -17.430 46.201  1.00 78.20  ? 165  PHE A CG  1 
ATOM   1086  C  CD1 . PHE A  1  139 ? 8.228   -18.329 45.789  1.00 78.89  ? 165  PHE A CD1 1 
ATOM   1087  C  CD2 . PHE A  1  139 ? 9.078   -16.088 45.850  1.00 77.97  ? 165  PHE A CD2 1 
ATOM   1088  C  CE1 . PHE A  1  139 ? 7.129   -17.896 45.037  1.00 78.99  ? 165  PHE A CE1 1 
ATOM   1089  C  CE2 . PHE A  1  139 ? 7.986   -15.644 45.100  1.00 78.26  ? 165  PHE A CE2 1 
ATOM   1090  C  CZ  . PHE A  1  139 ? 7.007   -16.548 44.691  1.00 77.85  ? 165  PHE A CZ  1 
ATOM   1091  N  N   . LYS A  1  140 ? 9.830   -17.220 50.352  1.00 81.42  ? 166  LYS A N   1 
ATOM   1092  C  CA  . LYS A  1  140 ? 8.797   -17.142 51.380  1.00 82.50  ? 166  LYS A CA  1 
ATOM   1093  C  C   . LYS A  1  140 ? 8.349   -15.697 51.589  1.00 82.76  ? 166  LYS A C   1 
ATOM   1094  O  O   . LYS A  1  140 ? 9.046   -14.905 52.220  1.00 81.77  ? 166  LYS A O   1 
ATOM   1095  C  CB  . LYS A  1  140 ? 9.329   -17.731 52.693  1.00 84.21  ? 166  LYS A CB  1 
ATOM   1096  C  CG  . LYS A  1  140 ? 8.321   -17.798 53.848  1.00 85.67  ? 166  LYS A CG  1 
ATOM   1097  C  CD  . LYS A  1  140 ? 8.851   -18.672 54.989  1.00 85.75  ? 166  LYS A CD  1 
ATOM   1098  C  CE  . LYS A  1  140 ? 8.150   -18.350 56.284  1.00 86.19  ? 166  LYS A CE  1 
ATOM   1099  N  NZ  . LYS A  1  140 ? 8.292   -16.892 56.583  1.00 86.57  ? 166  LYS A NZ  1 
ATOM   1100  N  N   . LEU A  1  141 ? 7.178   -15.368 51.042  1.00 83.71  ? 167  LEU A N   1 
ATOM   1101  C  CA  . LEU A  1  141 ? 6.606   -14.025 51.151  1.00 83.21  ? 167  LEU A CA  1 
ATOM   1102  C  C   . LEU A  1  141 ? 6.279   -13.718 52.605  1.00 83.07  ? 167  LEU A C   1 
ATOM   1103  O  O   . LEU A  1  141 ? 5.756   -14.569 53.328  1.00 82.21  ? 167  LEU A O   1 
ATOM   1104  C  CB  . LEU A  1  141 ? 5.341   -13.908 50.296  1.00 82.40  ? 167  LEU A CB  1 
ATOM   1105  C  CG  . LEU A  1  141 ? 5.525   -13.963 48.780  1.00 81.09  ? 167  LEU A CG  1 
ATOM   1106  C  CD1 . LEU A  1  141 ? 4.187   -14.136 48.114  1.00 81.15  ? 167  LEU A CD1 1 
ATOM   1107  C  CD2 . LEU A  1  141 ? 6.194   -12.706 48.299  1.00 81.06  ? 167  LEU A CD2 1 
ATOM   1108  N  N   . PRO A  1  142 ? 6.600   -12.498 53.057  1.00 83.30  ? 168  PRO A N   1 
ATOM   1109  C  CA  . PRO A  1  142 ? 6.332   -12.102 54.440  1.00 83.89  ? 168  PRO A CA  1 
ATOM   1110  C  C   . PRO A  1  142 ? 4.848   -12.107 54.770  1.00 83.79  ? 168  PRO A C   1 
ATOM   1111  O  O   . PRO A  1  142 ? 4.007   -12.093 53.877  1.00 83.70  ? 168  PRO A O   1 
ATOM   1112  C  CB  . PRO A  1  142 ? 6.936   -10.699 54.519  1.00 83.51  ? 168  PRO A CB  1 
ATOM   1113  C  CG  . PRO A  1  142 ? 8.045   -10.754 53.541  1.00 83.35  ? 168  PRO A CG  1 
ATOM   1114  C  CD  . PRO A  1  142 ? 7.394   -11.466 52.374  1.00 83.32  ? 168  PRO A CD  1 
ATOM   1115  N  N   . GLU A  1  143 ? 4.536   -12.122 56.059  1.00 84.07  ? 169  GLU A N   1 
ATOM   1116  C  CA  . GLU A  1  143 ? 3.151   -12.127 56.497  1.00 84.47  ? 169  GLU A CA  1 
ATOM   1117  C  C   . GLU A  1  143 ? 2.480   -10.798 56.217  1.00 83.52  ? 169  GLU A C   1 
ATOM   1118  O  O   . GLU A  1  143 ? 1.299   -10.757 55.896  1.00 82.52  ? 169  GLU A O   1 
ATOM   1119  C  CB  . GLU A  1  143 ? 3.061   -12.426 57.995  1.00 86.75  ? 169  GLU A CB  1 
ATOM   1120  C  CG  . GLU A  1  143 ? 3.236   -13.888 58.371  1.00 90.06  ? 169  GLU A CG  1 
ATOM   1121  C  CD  . GLU A  1  143 ? 2.275   -14.798 57.624  1.00 92.89  ? 169  GLU A CD  1 
ATOM   1122  O  OE1 . GLU A  1  143 ? 2.586   -15.152 56.467  1.00 94.72  ? 169  GLU A OE1 1 
ATOM   1123  O  OE2 . GLU A  1  143 ? 1.205   -15.147 58.177  1.00 94.10  ? 169  GLU A OE2 1 
ATOM   1124  N  N   . TYR A  1  144 ? 3.236   -9.712  56.333  1.00 83.64  ? 170  TYR A N   1 
ATOM   1125  C  CA  . TYR A  1  144 ? 2.673   -8.387  56.113  1.00 84.47  ? 170  TYR A CA  1 
ATOM   1126  C  C   . TYR A  1  144 ? 2.090   -8.193  54.722  1.00 85.34  ? 170  TYR A C   1 
ATOM   1127  O  O   . TYR A  1  144 ? 1.423   -7.193  54.462  1.00 85.62  ? 170  TYR A O   1 
ATOM   1128  C  CB  . TYR A  1  144 ? 3.712   -7.293  56.418  1.00 84.66  ? 170  TYR A CB  1 
ATOM   1129  C  CG  . TYR A  1  144 ? 4.913   -7.238  55.493  1.00 85.59  ? 170  TYR A CG  1 
ATOM   1130  C  CD1 . TYR A  1  144 ? 4.786   -6.820  54.171  1.00 86.19  ? 170  TYR A CD1 1 
ATOM   1131  C  CD2 . TYR A  1  144 ? 6.182   -7.594  55.943  1.00 85.50  ? 170  TYR A CD2 1 
ATOM   1132  C  CE1 . TYR A  1  144 ? 5.889   -6.757  53.323  1.00 85.16  ? 170  TYR A CE1 1 
ATOM   1133  C  CE2 . TYR A  1  144 ? 7.288   -7.533  55.099  1.00 84.56  ? 170  TYR A CE2 1 
ATOM   1134  C  CZ  . TYR A  1  144 ? 7.128   -7.112  53.791  1.00 83.90  ? 170  TYR A CZ  1 
ATOM   1135  O  OH  . TYR A  1  144 ? 8.215   -7.033  52.960  1.00 82.69  ? 170  TYR A OH  1 
ATOM   1136  N  N   . PHE A  1  145 ? 2.323   -9.153  53.830  1.00 86.37  ? 171  PHE A N   1 
ATOM   1137  C  CA  . PHE A  1  145 ? 1.795   -9.059  52.472  1.00 87.44  ? 171  PHE A CA  1 
ATOM   1138  C  C   . PHE A  1  145 ? 0.273   -8.989  52.437  1.00 88.11  ? 171  PHE A C   1 
ATOM   1139  O  O   . PHE A  1  145 ? -0.315  -8.625  51.423  1.00 87.97  ? 171  PHE A O   1 
ATOM   1140  C  CB  . PHE A  1  145 ? 2.293   -10.236 51.634  1.00 88.20  ? 171  PHE A CB  1 
ATOM   1141  C  CG  . PHE A  1  145 ? 3.427   -9.882  50.720  1.00 89.43  ? 171  PHE A CG  1 
ATOM   1142  C  CD1 . PHE A  1  145 ? 4.594   -9.317  51.227  1.00 90.28  ? 171  PHE A CD1 1 
ATOM   1143  C  CD2 . PHE A  1  145 ? 3.311   -10.064 49.345  1.00 89.47  ? 171  PHE A CD2 1 
ATOM   1144  C  CE1 . PHE A  1  145 ? 5.637   -8.928  50.376  1.00 90.15  ? 171  PHE A CE1 1 
ATOM   1145  C  CE2 . PHE A  1  145 ? 4.342   -9.681  48.484  1.00 90.29  ? 171  PHE A CE2 1 
ATOM   1146  C  CZ  . PHE A  1  145 ? 5.510   -9.108  48.999  1.00 90.01  ? 171  PHE A CZ  1 
ATOM   1147  N  N   . SER A  1  146 ? -0.357  -9.339  53.553  1.00 88.58  ? 172  SER A N   1 
ATOM   1148  C  CA  . SER A  1  146 ? -1.802  -9.289  53.656  1.00 88.10  ? 172  SER A CA  1 
ATOM   1149  C  C   . SER A  1  146 ? -2.242  -7.833  53.572  1.00 89.16  ? 172  SER A C   1 
ATOM   1150  O  O   . SER A  1  146 ? -3.043  -7.479  52.713  1.00 89.59  ? 172  SER A O   1 
ATOM   1151  C  CB  . SER A  1  146 ? -2.251  -9.888  54.978  1.00 86.83  ? 172  SER A CB  1 
ATOM   1152  O  OG  . SER A  1  146 ? -1.636  -11.145 55.160  1.00 85.65  ? 172  SER A OG  1 
ATOM   1153  N  N   . ASN A  1  147 ? -1.714  -6.982  54.447  1.00 90.45  ? 173  ASN A N   1 
ATOM   1154  C  CA  . ASN A  1  147 ? -2.093  -5.571  54.429  1.00 92.08  ? 173  ASN A CA  1 
ATOM   1155  C  C   . ASN A  1  147 ? -1.807  -4.927  53.071  1.00 90.87  ? 173  ASN A C   1 
ATOM   1156  O  O   . ASN A  1  147 ? -2.352  -3.869  52.756  1.00 90.98  ? 173  ASN A O   1 
ATOM   1157  C  CB  . ASN A  1  147 ? -1.375  -4.783  55.538  1.00 96.79  ? 173  ASN A CB  1 
ATOM   1158  C  CG  . ASN A  1  147 ? -1.832  -5.179  56.948  1.00 102.35 ? 173  ASN A CG  1 
ATOM   1159  O  OD1 . ASN A  1  147 ? -2.938  -5.705  57.125  1.00 102.49 ? 173  ASN A OD1 1 
ATOM   1160  N  ND2 . ASN A  1  147 ? -0.984  -4.915  57.949  1.00 106.94 ? 173  ASN A ND2 1 
ATOM   1161  N  N   . LEU A  1  148 ? -0.951  -5.560  52.272  1.00 89.54  ? 174  LEU A N   1 
ATOM   1162  C  CA  . LEU A  1  148 ? -0.620  -5.049  50.935  1.00 87.59  ? 174  LEU A CA  1 
ATOM   1163  C  C   . LEU A  1  148 ? -1.679  -5.561  49.961  1.00 86.93  ? 174  LEU A C   1 
ATOM   1164  O  O   . LEU A  1  148 ? -1.428  -6.455  49.160  1.00 86.85  ? 174  LEU A O   1 
ATOM   1165  C  CB  . LEU A  1  148 ? 0.759   -5.548  50.507  1.00 86.22  ? 174  LEU A CB  1 
ATOM   1166  C  CG  . LEU A  1  148 ? 1.980   -4.958  51.200  1.00 84.87  ? 174  LEU A CG  1 
ATOM   1167  C  CD1 . LEU A  1  148 ? 3.241   -5.609  50.666  1.00 84.13  ? 174  LEU A CD1 1 
ATOM   1168  C  CD2 . LEU A  1  148 ? 2.008   -3.464  50.962  1.00 84.87  ? 174  LEU A CD2 1 
ATOM   1169  N  N   . THR A  1  149 ? -2.865  -4.975  50.025  1.00 86.00  ? 175  THR A N   1 
ATOM   1170  C  CA  . THR A  1  149 ? -3.980  -5.419  49.204  1.00 84.80  ? 175  THR A CA  1 
ATOM   1171  C  C   . THR A  1  149 ? -4.125  -4.855  47.786  1.00 82.34  ? 175  THR A C   1 
ATOM   1172  O  O   . THR A  1  149 ? -4.995  -5.290  47.030  1.00 81.41  ? 175  THR A O   1 
ATOM   1173  C  CB  . THR A  1  149 ? -5.293  -5.194  49.978  1.00 85.68  ? 175  THR A CB  1 
ATOM   1174  O  OG1 . THR A  1  149 ? -6.399  -5.629  49.182  1.00 88.42  ? 175  THR A OG1 1 
ATOM   1175  C  CG2 . THR A  1  149 ? -5.457  -3.723  50.335  1.00 85.35  ? 175  THR A CG2 1 
ATOM   1176  N  N   . ASN A  1  150 ? -3.283  -3.900  47.418  1.00 80.47  ? 176  ASN A N   1 
ATOM   1177  C  CA  . ASN A  1  150 ? -3.362  -3.312  46.081  1.00 78.58  ? 176  ASN A CA  1 
ATOM   1178  C  C   . ASN A  1  150 ? -2.135  -3.640  45.240  1.00 76.63  ? 176  ASN A C   1 
ATOM   1179  O  O   . ASN A  1  150 ? -1.921  -3.040  44.184  1.00 76.82  ? 176  ASN A O   1 
ATOM   1180  C  CB  . ASN A  1  150 ? -3.510  -1.792  46.179  1.00 79.10  ? 176  ASN A CB  1 
ATOM   1181  C  CG  . ASN A  1  150 ? -4.874  -1.370  46.659  1.00 79.30  ? 176  ASN A CG  1 
ATOM   1182  O  OD1 . ASN A  1  150 ? -5.419  -1.942  47.605  1.00 79.97  ? 176  ASN A OD1 1 
ATOM   1183  N  ND2 . ASN A  1  150 ? -5.432  -0.352  46.018  1.00 79.29  ? 176  ASN A ND2 1 
ATOM   1184  N  N   . LEU A  1  151 ? -1.338  -4.594  45.706  1.00 73.77  ? 177  LEU A N   1 
ATOM   1185  C  CA  . LEU A  1  151 ? -0.126  -4.982  45.002  1.00 71.82  ? 177  LEU A CA  1 
ATOM   1186  C  C   . LEU A  1  151 ? -0.445  -5.790  43.752  1.00 71.72  ? 177  LEU A C   1 
ATOM   1187  O  O   . LEU A  1  151 ? -1.145  -6.801  43.828  1.00 72.00  ? 177  LEU A O   1 
ATOM   1188  C  CB  . LEU A  1  151 ? 0.772   -5.807  45.925  1.00 69.05  ? 177  LEU A CB  1 
ATOM   1189  C  CG  . LEU A  1  151 ? 2.180   -6.090  45.410  1.00 67.34  ? 177  LEU A CG  1 
ATOM   1190  C  CD1 . LEU A  1  151 ? 2.969   -4.792  45.379  1.00 66.26  ? 177  LEU A CD1 1 
ATOM   1191  C  CD2 . LEU A  1  151 ? 2.861   -7.109  46.294  1.00 64.27  ? 177  LEU A CD2 1 
ATOM   1192  N  N   . GLU A  1  152 ? 0.075   -5.348  42.608  1.00 71.03  ? 178  GLU A N   1 
ATOM   1193  C  CA  . GLU A  1  152 ? -0.151  -6.051  41.350  1.00 71.61  ? 178  GLU A CA  1 
ATOM   1194  C  C   . GLU A  1  152 ? 1.154   -6.457  40.681  1.00 71.32  ? 178  GLU A C   1 
ATOM   1195  O  O   . GLU A  1  152 ? 1.187   -7.384  39.862  1.00 71.11  ? 178  GLU A O   1 
ATOM   1196  C  CB  . GLU A  1  152 ? -0.913  -5.178  40.364  1.00 73.25  ? 178  GLU A CB  1 
ATOM   1197  C  CG  . GLU A  1  152 ? -2.014  -4.354  40.963  1.00 77.88  ? 178  GLU A CG  1 
ATOM   1198  C  CD  . GLU A  1  152 ? -2.948  -3.818  39.902  1.00 80.73  ? 178  GLU A CD  1 
ATOM   1199  O  OE1 . GLU A  1  152 ? -3.779  -4.621  39.405  1.00 82.20  ? 178  GLU A OE1 1 
ATOM   1200  O  OE2 . GLU A  1  152 ? -2.844  -2.612  39.558  1.00 81.84  ? 178  GLU A OE2 1 
ATOM   1201  N  N   . HIS A  1  153 ? 2.228   -5.754  41.023  1.00 69.78  ? 179  HIS A N   1 
ATOM   1202  C  CA  . HIS A  1  153 ? 3.520   -6.032  40.423  1.00 68.06  ? 179  HIS A CA  1 
ATOM   1203  C  C   . HIS A  1  153 ? 4.649   -6.266  41.427  1.00 65.76  ? 179  HIS A C   1 
ATOM   1204  O  O   . HIS A  1  153 ? 4.911   -5.429  42.280  1.00 64.26  ? 179  HIS A O   1 
ATOM   1205  C  CB  . HIS A  1  153 ? 3.876   -4.880  39.496  1.00 70.53  ? 179  HIS A CB  1 
ATOM   1206  C  CG  . HIS A  1  153 ? 2.935   -4.720  38.342  1.00 73.95  ? 179  HIS A CG  1 
ATOM   1207  N  ND1 . HIS A  1  153 ? 3.027   -5.485  37.197  1.00 75.42  ? 179  HIS A ND1 1 
ATOM   1208  C  CD2 . HIS A  1  153 ? 1.888   -3.881  38.149  1.00 75.10  ? 179  HIS A CD2 1 
ATOM   1209  C  CE1 . HIS A  1  153 ? 2.082   -5.122  36.347  1.00 76.16  ? 179  HIS A CE1 1 
ATOM   1210  N  NE2 . HIS A  1  153 ? 1.375   -4.149  36.900  1.00 76.39  ? 179  HIS A NE2 1 
ATOM   1211  N  N   . LEU A  1  154 ? 5.313   -7.416  41.308  1.00 64.26  ? 180  LEU A N   1 
ATOM   1212  C  CA  . LEU A  1  154 ? 6.434   -7.786  42.175  1.00 61.27  ? 180  LEU A CA  1 
ATOM   1213  C  C   . LEU A  1  154 ? 7.601   -8.282  41.320  1.00 61.72  ? 180  LEU A C   1 
ATOM   1214  O  O   . LEU A  1  154 ? 7.489   -9.272  40.588  1.00 61.98  ? 180  LEU A O   1 
ATOM   1215  C  CB  . LEU A  1  154 ? 6.029   -8.891  43.152  1.00 58.40  ? 180  LEU A CB  1 
ATOM   1216  C  CG  . LEU A  1  154 ? 7.127   -9.264  44.146  1.00 56.62  ? 180  LEU A CG  1 
ATOM   1217  C  CD1 . LEU A  1  154 ? 7.371   -8.082  45.038  1.00 55.84  ? 180  LEU A CD1 1 
ATOM   1218  C  CD2 . LEU A  1  154 ? 6.740   -10.473 44.980  1.00 55.33  ? 180  LEU A CD2 1 
ATOM   1219  N  N   . ASP A  1  155 ? 8.721   -7.575  41.410  1.00 62.39  ? 181  ASP A N   1 
ATOM   1220  C  CA  . ASP A  1  155 ? 9.920   -7.920  40.651  1.00 62.29  ? 181  ASP A CA  1 
ATOM   1221  C  C   . ASP A  1  155 ? 10.996  -8.491  41.580  1.00 61.13  ? 181  ASP A C   1 
ATOM   1222  O  O   . ASP A  1  155 ? 11.630  -7.748  42.341  1.00 60.39  ? 181  ASP A O   1 
ATOM   1223  C  CB  . ASP A  1  155 ? 10.472  -6.672  39.944  1.00 63.49  ? 181  ASP A CB  1 
ATOM   1224  C  CG  . ASP A  1  155 ? 11.425  -7.017  38.807  1.00 65.81  ? 181  ASP A CG  1 
ATOM   1225  O  OD1 . ASP A  1  155 ? 12.015  -8.122  38.856  1.00 66.92  ? 181  ASP A OD1 1 
ATOM   1226  O  OD2 . ASP A  1  155 ? 11.595  -6.186  37.876  1.00 66.23  ? 181  ASP A OD2 1 
ATOM   1227  N  N   . LEU A  1  156 ? 11.181  -9.806  41.522  1.00 59.04  ? 182  LEU A N   1 
ATOM   1228  C  CA  . LEU A  1  156 ? 12.187  -10.490 42.328  1.00 57.62  ? 182  LEU A CA  1 
ATOM   1229  C  C   . LEU A  1  156 ? 13.296  -11.033 41.416  1.00 57.71  ? 182  LEU A C   1 
ATOM   1230  O  O   . LEU A  1  156 ? 14.099  -11.887 41.828  1.00 56.19  ? 182  LEU A O   1 
ATOM   1231  C  CB  . LEU A  1  156 ? 11.550  -11.647 43.099  1.00 56.01  ? 182  LEU A CB  1 
ATOM   1232  C  CG  . LEU A  1  156 ? 10.689  -11.316 44.316  1.00 55.11  ? 182  LEU A CG  1 
ATOM   1233  C  CD1 . LEU A  1  156 ? 10.078  -12.580 44.898  1.00 54.58  ? 182  LEU A CD1 1 
ATOM   1234  C  CD2 . LEU A  1  156 ? 11.558  -10.633 45.351  1.00 55.96  ? 182  LEU A CD2 1 
ATOM   1235  N  N   . SER A  1  157 ? 13.339  -10.530 40.181  1.00 57.07  ? 183  SER A N   1 
ATOM   1236  C  CA  . SER A  1  157 ? 14.329  -10.989 39.211  1.00 56.68  ? 183  SER A CA  1 
ATOM   1237  C  C   . SER A  1  157 ? 15.744  -10.581 39.617  1.00 56.41  ? 183  SER A C   1 
ATOM   1238  O  O   . SER A  1  157 ? 15.935  -9.572  40.307  1.00 56.20  ? 183  SER A O   1 
ATOM   1239  C  CB  . SER A  1  157 ? 13.997  -10.459 37.802  1.00 55.23  ? 183  SER A CB  1 
ATOM   1240  O  OG  . SER A  1  157 ? 14.384  -9.102  37.635  1.00 54.16  ? 183  SER A OG  1 
ATOM   1241  N  N   . SER A  1  158 ? 16.719  -11.384 39.187  1.00 54.82  ? 184  SER A N   1 
ATOM   1242  C  CA  . SER A  1  158 ? 18.129  -11.156 39.478  1.00 53.85  ? 184  SER A CA  1 
ATOM   1243  C  C   . SER A  1  158 ? 18.435  -11.146 40.959  1.00 53.50  ? 184  SER A C   1 
ATOM   1244  O  O   . SER A  1  158 ? 19.023  -10.202 41.458  1.00 53.85  ? 184  SER A O   1 
ATOM   1245  C  CB  . SER A  1  158 ? 18.609  -9.838  38.864  1.00 53.08  ? 184  SER A CB  1 
ATOM   1246  O  OG  . SER A  1  158 ? 18.765  -9.936  37.462  1.00 54.50  ? 184  SER A OG  1 
ATOM   1247  N  N   . ASN A  1  159 ? 18.023  -12.187 41.665  1.00 53.73  ? 185  ASN A N   1 
ATOM   1248  C  CA  . ASN A  1  159 ? 18.302  -12.284 43.080  1.00 54.75  ? 185  ASN A CA  1 
ATOM   1249  C  C   . ASN A  1  159 ? 18.977  -13.620 43.320  1.00 57.95  ? 185  ASN A C   1 
ATOM   1250  O  O   . ASN A  1  159 ? 19.564  -14.184 42.396  1.00 59.40  ? 185  ASN A O   1 
ATOM   1251  C  CB  . ASN A  1  159 ? 17.028  -12.151 43.899  1.00 54.13  ? 185  ASN A CB  1 
ATOM   1252  C  CG  . ASN A  1  159 ? 16.641  -10.685 44.160  1.00 54.42  ? 185  ASN A CG  1 
ATOM   1253  O  OD1 . ASN A  1  159 ? 16.197  -9.970  43.259  1.00 54.30  ? 185  ASN A OD1 1 
ATOM   1254  N  ND2 . ASN A  1  159 ? 16.814  -10.241 45.401  1.00 52.45  ? 185  ASN A ND2 1 
ATOM   1255  N  N   . LYS A  1  160 ? 18.903  -14.146 44.537  1.00 60.94  ? 186  LYS A N   1 
ATOM   1256  C  CA  . LYS A  1  160 ? 19.583  -15.412 44.821  1.00 63.38  ? 186  LYS A CA  1 
ATOM   1257  C  C   . LYS A  1  160 ? 18.698  -16.586 45.212  1.00 64.30  ? 186  LYS A C   1 
ATOM   1258  O  O   . LYS A  1  160 ? 19.170  -17.537 45.829  1.00 65.12  ? 186  LYS A O   1 
ATOM   1259  C  CB  . LYS A  1  160 ? 20.651  -15.197 45.901  1.00 63.32  ? 186  LYS A CB  1 
ATOM   1260  C  CG  . LYS A  1  160 ? 21.679  -14.145 45.527  1.00 64.39  ? 186  LYS A CG  1 
ATOM   1261  C  CD  . LYS A  1  160 ? 22.460  -14.560 44.288  1.00 65.82  ? 186  LYS A CD  1 
ATOM   1262  C  CE  . LYS A  1  160 ? 23.301  -13.409 43.737  1.00 66.98  ? 186  LYS A CE  1 
ATOM   1263  N  NZ  . LYS A  1  160 ? 24.192  -12.813 44.774  1.00 68.80  ? 186  LYS A NZ  1 
ATOM   1264  N  N   . ILE A  1  161 ? 17.423  -16.530 44.858  1.00 65.01  ? 187  ILE A N   1 
ATOM   1265  C  CA  . ILE A  1  161 ? 16.532  -17.627 45.187  1.00 65.98  ? 187  ILE A CA  1 
ATOM   1266  C  C   . ILE A  1  161 ? 16.990  -18.877 44.439  1.00 67.91  ? 187  ILE A C   1 
ATOM   1267  O  O   . ILE A  1  161 ? 17.272  -18.819 43.240  1.00 68.07  ? 187  ILE A O   1 
ATOM   1268  C  CB  . ILE A  1  161 ? 15.089  -17.303 44.788  1.00 64.91  ? 187  ILE A CB  1 
ATOM   1269  C  CG1 . ILE A  1  161 ? 14.649  -16.005 45.471  1.00 63.64  ? 187  ILE A CG1 1 
ATOM   1270  C  CG2 . ILE A  1  161 ? 14.176  -18.462 45.162  1.00 63.53  ? 187  ILE A CG2 1 
ATOM   1271  C  CD1 . ILE A  1  161 ? 13.243  -15.585 45.127  1.00 62.32  ? 187  ILE A CD1 1 
ATOM   1272  N  N   . GLN A  1  162 ? 17.066  -20.001 45.150  1.00 70.20  ? 188  GLN A N   1 
ATOM   1273  C  CA  . GLN A  1  162 ? 17.501  -21.266 44.552  1.00 71.52  ? 188  GLN A CA  1 
ATOM   1274  C  C   . GLN A  1  162 ? 16.476  -22.378 44.680  1.00 72.04  ? 188  GLN A C   1 
ATOM   1275  O  O   . GLN A  1  162 ? 16.614  -23.420 44.050  1.00 72.11  ? 188  GLN A O   1 
ATOM   1276  C  CB  . GLN A  1  162 ? 18.805  -21.730 45.185  1.00 72.57  ? 188  GLN A CB  1 
ATOM   1277  C  CG  . GLN A  1  162 ? 19.917  -20.702 45.095  1.00 74.47  ? 188  GLN A CG  1 
ATOM   1278  C  CD  . GLN A  1  162 ? 21.216  -21.188 45.716  1.00 75.36  ? 188  GLN A CD  1 
ATOM   1279  O  OE1 . GLN A  1  162 ? 21.800  -22.178 45.265  1.00 75.07  ? 188  GLN A OE1 1 
ATOM   1280  N  NE2 . GLN A  1  162 ? 21.673  -20.492 46.759  1.00 74.80  ? 188  GLN A NE2 1 
ATOM   1281  N  N   . SER A  1  163 ? 15.450  -22.153 45.492  1.00 73.52  ? 189  SER A N   1 
ATOM   1282  C  CA  . SER A  1  163 ? 14.403  -23.151 45.682  1.00 75.05  ? 189  SER A CA  1 
ATOM   1283  C  C   . SER A  1  163 ? 13.100  -22.600 46.278  1.00 75.58  ? 189  SER A C   1 
ATOM   1284  O  O   . SER A  1  163 ? 13.091  -21.622 47.034  1.00 75.32  ? 189  SER A O   1 
ATOM   1285  C  CB  . SER A  1  163 ? 14.928  -24.281 46.560  1.00 75.63  ? 189  SER A CB  1 
ATOM   1286  O  OG  . SER A  1  163 ? 15.391  -23.769 47.791  1.00 76.72  ? 189  SER A OG  1 
ATOM   1287  N  N   . ILE A  1  164 ? 11.993  -23.242 45.929  1.00 76.15  ? 190  ILE A N   1 
ATOM   1288  C  CA  . ILE A  1  164 ? 10.685  -22.825 46.414  1.00 76.69  ? 190  ILE A CA  1 
ATOM   1289  C  C   . ILE A  1  164 ? 10.018  -23.994 47.139  1.00 77.95  ? 190  ILE A C   1 
ATOM   1290  O  O   . ILE A  1  164 ? 9.765   -25.045 46.538  1.00 76.73  ? 190  ILE A O   1 
ATOM   1291  C  CB  . ILE A  1  164 ? 9.779   -22.371 45.247  1.00 75.81  ? 190  ILE A CB  1 
ATOM   1292  C  CG1 . ILE A  1  164 ? 10.441  -21.220 44.494  1.00 74.51  ? 190  ILE A CG1 1 
ATOM   1293  C  CG2 . ILE A  1  164 ? 8.435   -21.907 45.775  1.00 76.54  ? 190  ILE A CG2 1 
ATOM   1294  C  CD1 . ILE A  1  164 ? 9.738   -20.862 43.215  1.00 73.53  ? 190  ILE A CD1 1 
ATOM   1295  N  N   . TYR A  1  165 ? 9.757   -23.801 48.435  1.00 78.88  ? 191  TYR A N   1 
ATOM   1296  C  CA  . TYR A  1  165 ? 9.124   -24.814 49.271  1.00 79.16  ? 191  TYR A CA  1 
ATOM   1297  C  C   . TYR A  1  165 ? 7.680   -24.429 49.475  1.00 79.64  ? 191  TYR A C   1 
ATOM   1298  O  O   . TYR A  1  165 ? 7.357   -23.250 49.478  1.00 79.66  ? 191  TYR A O   1 
ATOM   1299  C  CB  . TYR A  1  165 ? 9.819   -24.896 50.620  1.00 79.44  ? 191  TYR A CB  1 
ATOM   1300  C  CG  . TYR A  1  165 ? 11.301  -25.178 50.523  1.00 80.59  ? 191  TYR A CG  1 
ATOM   1301  C  CD1 . TYR A  1  165 ? 12.236  -24.246 50.969  1.00 81.19  ? 191  TYR A CD1 1 
ATOM   1302  C  CD2 . TYR A  1  165 ? 11.772  -26.380 49.987  1.00 80.70  ? 191  TYR A CD2 1 
ATOM   1303  C  CE1 . TYR A  1  165 ? 13.606  -24.502 50.887  1.00 81.49  ? 191  TYR A CE1 1 
ATOM   1304  C  CE2 . TYR A  1  165 ? 13.141  -26.647 49.897  1.00 80.82  ? 191  TYR A CE2 1 
ATOM   1305  C  CZ  . TYR A  1  165 ? 14.052  -25.706 50.349  1.00 81.51  ? 191  TYR A CZ  1 
ATOM   1306  O  OH  . TYR A  1  165 ? 15.404  -25.970 50.268  1.00 81.12  ? 191  TYR A OH  1 
ATOM   1307  N  N   . CYS A  1  166 ? 6.816   -25.420 49.662  1.00 80.68  ? 192  CYS A N   1 
ATOM   1308  C  CA  . CYS A  1  166 ? 5.389   -25.172 49.841  1.00 82.24  ? 192  CYS A CA  1 
ATOM   1309  C  C   . CYS A  1  166 ? 5.038   -24.024 50.779  1.00 82.48  ? 192  CYS A C   1 
ATOM   1310  O  O   . CYS A  1  166 ? 4.239   -23.157 50.432  1.00 82.85  ? 192  CYS A O   1 
ATOM   1311  C  CB  . CYS A  1  166 ? 4.688   -26.439 50.331  1.00 82.71  ? 192  CYS A CB  1 
ATOM   1312  S  SG  . CYS A  1  166 ? 4.713   -27.824 49.170  1.00 88.91  ? 192  CYS A SG  1 
ATOM   1313  N  N   . THR A  1  167 ? 5.640   -24.012 51.961  1.00 82.87  ? 193  THR A N   1 
ATOM   1314  C  CA  . THR A  1  167 ? 5.346   -22.987 52.953  1.00 83.58  ? 193  THR A CA  1 
ATOM   1315  C  C   . THR A  1  167 ? 5.586   -21.551 52.499  1.00 85.12  ? 193  THR A C   1 
ATOM   1316  O  O   . THR A  1  167 ? 4.999   -20.618 53.043  1.00 85.66  ? 193  THR A O   1 
ATOM   1317  C  CB  . THR A  1  167 ? 6.145   -23.233 54.230  1.00 82.63  ? 193  THR A CB  1 
ATOM   1318  O  OG1 . THR A  1  167 ? 7.536   -23.010 53.977  1.00 81.75  ? 193  THR A OG1 1 
ATOM   1319  C  CG2 . THR A  1  167 ? 5.940   -24.666 54.697  1.00 82.59  ? 193  THR A CG2 1 
ATOM   1320  N  N   . ASP A  1  168 ? 6.437   -21.379 51.494  1.00 86.79  ? 194  ASP A N   1 
ATOM   1321  C  CA  . ASP A  1  168 ? 6.767   -20.055 50.972  1.00 87.46  ? 194  ASP A CA  1 
ATOM   1322  C  C   . ASP A  1  168 ? 5.538   -19.302 50.448  1.00 87.57  ? 194  ASP A C   1 
ATOM   1323  O  O   . ASP A  1  168 ? 5.417   -18.082 50.620  1.00 86.85  ? 194  ASP A O   1 
ATOM   1324  C  CB  . ASP A  1  168 ? 7.817   -20.185 49.852  1.00 88.63  ? 194  ASP A CB  1 
ATOM   1325  C  CG  . ASP A  1  168 ? 9.141   -20.805 50.337  1.00 89.57  ? 194  ASP A CG  1 
ATOM   1326  O  OD1 . ASP A  1  168 ? 10.027  -21.076 49.491  1.00 89.52  ? 194  ASP A OD1 1 
ATOM   1327  O  OD2 . ASP A  1  168 ? 9.298   -21.014 51.559  1.00 89.66  ? 194  ASP A OD2 1 
ATOM   1328  N  N   . LEU A  1  169 ? 4.622   -20.043 49.833  1.00 87.71  ? 195  LEU A N   1 
ATOM   1329  C  CA  . LEU A  1  169 ? 3.406   -19.475 49.255  1.00 88.66  ? 195  LEU A CA  1 
ATOM   1330  C  C   . LEU A  1  169 ? 2.178   -19.418 50.171  1.00 89.78  ? 195  LEU A C   1 
ATOM   1331  O  O   . LEU A  1  169 ? 1.105   -18.973 49.755  1.00 89.23  ? 195  LEU A O   1 
ATOM   1332  C  CB  . LEU A  1  169 ? 3.051   -20.258 47.999  1.00 87.72  ? 195  LEU A CB  1 
ATOM   1333  C  CG  . LEU A  1  169 ? 4.092   -20.101 46.903  1.00 87.54  ? 195  LEU A CG  1 
ATOM   1334  C  CD1 . LEU A  1  169 ? 3.901   -21.164 45.847  1.00 88.02  ? 195  LEU A CD1 1 
ATOM   1335  C  CD2 . LEU A  1  169 ? 3.972   -18.709 46.316  1.00 86.90  ? 195  LEU A CD2 1 
ATOM   1336  N  N   . ARG A  1  170 ? 2.339   -19.856 51.414  1.00 90.95  ? 196  ARG A N   1 
ATOM   1337  C  CA  . ARG A  1  170 ? 1.237   -19.878 52.365  1.00 91.73  ? 196  ARG A CA  1 
ATOM   1338  C  C   . ARG A  1  170 ? 0.500   -18.550 52.482  1.00 90.77  ? 196  ARG A C   1 
ATOM   1339  O  O   . ARG A  1  170 ? -0.699  -18.529 52.730  1.00 90.51  ? 196  ARG A O   1 
ATOM   1340  C  CB  . ARG A  1  170 ? 1.748   -20.303 53.737  1.00 93.72  ? 196  ARG A CB  1 
ATOM   1341  C  CG  . ARG A  1  170 ? 0.653   -20.629 54.736  1.00 97.63  ? 196  ARG A CG  1 
ATOM   1342  C  CD  . ARG A  1  170 ? 1.243   -20.952 56.102  1.00 101.07 ? 196  ARG A CD  1 
ATOM   1343  N  NE  . ARG A  1  170 ? 2.053   -19.846 56.614  1.00 103.44 ? 196  ARG A NE  1 
ATOM   1344  C  CZ  . ARG A  1  170 ? 1.572   -18.655 56.968  1.00 103.19 ? 196  ARG A CZ  1 
ATOM   1345  N  NH1 . ARG A  1  170 ? 0.273   -18.395 56.878  1.00 102.31 ? 196  ARG A NH1 1 
ATOM   1346  N  NH2 . ARG A  1  170 ? 2.401   -17.717 57.402  1.00 103.30 ? 196  ARG A NH2 1 
ATOM   1347  N  N   . VAL A  1  171 ? 1.211   -17.446 52.298  1.00 90.57  ? 197  VAL A N   1 
ATOM   1348  C  CA  . VAL A  1  171 ? 0.591   -16.126 52.391  1.00 90.00  ? 197  VAL A CA  1 
ATOM   1349  C  C   . VAL A  1  171 ? -0.477  -15.910 51.330  1.00 89.60  ? 197  VAL A C   1 
ATOM   1350  O  O   . VAL A  1  171 ? -1.519  -15.305 51.585  1.00 88.05  ? 197  VAL A O   1 
ATOM   1351  C  CB  . VAL A  1  171 ? 1.613   -15.020 52.192  1.00 90.03  ? 197  VAL A CB  1 
ATOM   1352  C  CG1 . VAL A  1  171 ? 1.020   -13.689 52.642  1.00 89.03  ? 197  VAL A CG1 1 
ATOM   1353  C  CG2 . VAL A  1  171 ? 2.899   -15.371 52.916  1.00 90.66  ? 197  VAL A CG2 1 
ATOM   1354  N  N   . LEU A  1  172 ? -0.189  -16.390 50.127  1.00 89.61  ? 198  LEU A N   1 
ATOM   1355  C  CA  . LEU A  1  172 ? -1.102  -16.249 49.009  1.00 89.36  ? 198  LEU A CA  1 
ATOM   1356  C  C   . LEU A  1  172 ? -2.403  -17.034 49.224  1.00 90.72  ? 198  LEU A C   1 
ATOM   1357  O  O   . LEU A  1  172 ? -3.481  -16.561 48.859  1.00 90.33  ? 198  LEU A O   1 
ATOM   1358  C  CB  . LEU A  1  172 ? -0.396  -16.679 47.717  1.00 86.72  ? 198  LEU A CB  1 
ATOM   1359  C  CG  . LEU A  1  172 ? 0.746   -15.754 47.271  1.00 83.63  ? 198  LEU A CG  1 
ATOM   1360  C  CD1 . LEU A  1  172 ? 1.442   -16.331 46.061  1.00 82.31  ? 198  LEU A CD1 1 
ATOM   1361  C  CD2 . LEU A  1  172 ? 0.195   -14.381 46.953  1.00 82.12  ? 198  LEU A CD2 1 
ATOM   1362  N  N   . HIS A  1  173 ? -2.306  -18.218 49.826  1.00 92.67  ? 199  HIS A N   1 
ATOM   1363  C  CA  . HIS A  1  173 ? -3.489  -19.035 50.101  1.00 94.03  ? 199  HIS A CA  1 
ATOM   1364  C  C   . HIS A  1  173 ? -4.535  -18.238 50.905  1.00 95.25  ? 199  HIS A C   1 
ATOM   1365  O  O   . HIS A  1  173 ? -5.665  -18.685 51.068  1.00 96.07  ? 199  HIS A O   1 
ATOM   1366  C  CB  . HIS A  1  173 ? -3.108  -20.277 50.917  1.00 93.74  ? 199  HIS A CB  1 
ATOM   1367  C  CG  . HIS A  1  173 ? -2.334  -21.311 50.160  1.00 94.11  ? 199  HIS A CG  1 
ATOM   1368  N  ND1 . HIS A  1  173 ? -2.894  -22.084 49.166  1.00 94.26  ? 199  HIS A ND1 1 
ATOM   1369  C  CD2 . HIS A  1  173 ? -1.061  -21.751 50.304  1.00 94.76  ? 199  HIS A CD2 1 
ATOM   1370  C  CE1 . HIS A  1  173 ? -2.000  -22.957 48.734  1.00 94.85  ? 199  HIS A CE1 1 
ATOM   1371  N  NE2 . HIS A  1  173 ? -0.879  -22.775 49.409  1.00 94.17  ? 199  HIS A NE2 1 
ATOM   1372  N  N   . GLN A  1  174 ? -4.162  -17.061 51.402  1.00 96.30  ? 200  GLN A N   1 
ATOM   1373  C  CA  . GLN A  1  174 ? -5.073  -16.251 52.209  1.00 97.18  ? 200  GLN A CA  1 
ATOM   1374  C  C   . GLN A  1  174 ? -5.400  -14.882 51.612  1.00 97.32  ? 200  GLN A C   1 
ATOM   1375  O  O   . GLN A  1  174 ? -5.715  -13.931 52.333  1.00 96.57  ? 200  GLN A O   1 
ATOM   1376  C  CB  . GLN A  1  174 ? -4.488  -16.066 53.611  1.00 98.76  ? 200  GLN A CB  1 
ATOM   1377  C  CG  . GLN A  1  174 ? -4.227  -17.366 54.361  1.00 100.28 ? 200  GLN A CG  1 
ATOM   1378  C  CD  . GLN A  1  174 ? -3.402  -17.148 55.618  1.00 101.57 ? 200  GLN A CD  1 
ATOM   1379  O  OE1 . GLN A  1  174 ? -3.769  -16.352 56.484  1.00 102.60 ? 200  GLN A OE1 1 
ATOM   1380  N  NE2 . GLN A  1  174 ? -2.277  -17.849 55.721  1.00 101.31 ? 200  GLN A NE2 1 
ATOM   1381  N  N   . MET A  1  175 ? -5.312  -14.785 50.294  1.00 97.72  ? 201  MET A N   1 
ATOM   1382  C  CA  . MET A  1  175 ? -5.623  -13.549 49.596  1.00 98.18  ? 201  MET A CA  1 
ATOM   1383  C  C   . MET A  1  175 ? -6.395  -13.948 48.346  1.00 98.71  ? 201  MET A C   1 
ATOM   1384  O  O   . MET A  1  175 ? -5.810  -14.155 47.278  1.00 97.68  ? 201  MET A O   1 
ATOM   1385  C  CB  . MET A  1  175 ? -4.347  -12.805 49.201  1.00 98.13  ? 201  MET A CB  1 
ATOM   1386  C  CG  . MET A  1  175 ? -3.544  -12.241 50.360  1.00 97.74  ? 201  MET A CG  1 
ATOM   1387  S  SD  . MET A  1  175 ? -2.045  -11.379 49.804  1.00 97.67  ? 201  MET A SD  1 
ATOM   1388  C  CE  . MET A  1  175 ? -2.762  -9.929  48.974  1.00 97.63  ? 201  MET A CE  1 
ATOM   1389  N  N   . PRO A  1  176 ? -7.728  -14.085 48.473  1.00 99.41  ? 202  PRO A N   1 
ATOM   1390  C  CA  . PRO A  1  176 ? -8.605  -14.464 47.360  1.00 99.06  ? 202  PRO A CA  1 
ATOM   1391  C  C   . PRO A  1  176 ? -8.318  -13.610 46.131  1.00 98.08  ? 202  PRO A C   1 
ATOM   1392  O  O   . PRO A  1  176 ? -7.672  -14.064 45.185  1.00 98.12  ? 202  PRO A O   1 
ATOM   1393  C  CB  . PRO A  1  176 ? -10.002 -14.226 47.932  1.00 99.35  ? 202  PRO A CB  1 
ATOM   1394  C  CG  . PRO A  1  176 ? -9.819  -14.558 49.380  1.00 98.92  ? 202  PRO A CG  1 
ATOM   1395  C  CD  . PRO A  1  176 ? -8.519  -13.841 49.694  1.00 99.46  ? 202  PRO A CD  1 
ATOM   1396  N  N   . LEU A  1  177 ? -8.805  -12.375 46.146  1.00 96.64  ? 203  LEU A N   1 
ATOM   1397  C  CA  . LEU A  1  177 ? -8.549  -11.464 45.039  1.00 95.65  ? 203  LEU A CA  1 
ATOM   1398  C  C   . LEU A  1  177 ? -7.064  -11.091 45.162  1.00 93.24  ? 203  LEU A C   1 
ATOM   1399  O  O   . LEU A  1  177 ? -6.591  -10.763 46.253  1.00 93.80  ? 203  LEU A O   1 
ATOM   1400  C  CB  . LEU A  1  177 ? -9.444  -10.209 45.151  1.00 97.95  ? 203  LEU A CB  1 
ATOM   1401  C  CG  . LEU A  1  177 ? -10.974 -10.300 44.931  1.00 99.18  ? 203  LEU A CG  1 
ATOM   1402  C  CD1 . LEU A  1  177 ? -11.615 -8.951  45.282  1.00 98.61  ? 203  LEU A CD1 1 
ATOM   1403  C  CD2 . LEU A  1  177 ? -11.305 -10.675 43.465  1.00 98.84  ? 203  LEU A CD2 1 
ATOM   1404  N  N   . LEU A  1  178 ? -6.321  -11.163 44.060  1.00 89.80  ? 204  LEU A N   1 
ATOM   1405  C  CA  . LEU A  1  178 ? -4.899  -10.849 44.105  1.00 86.78  ? 204  LEU A CA  1 
ATOM   1406  C  C   . LEU A  1  178 ? -4.272  -10.946 42.711  1.00 85.50  ? 204  LEU A C   1 
ATOM   1407  O  O   . LEU A  1  178 ? -3.662  -11.952 42.360  1.00 85.66  ? 204  LEU A O   1 
ATOM   1408  C  CB  . LEU A  1  178 ? -4.212  -11.801 45.092  1.00 85.71  ? 204  LEU A CB  1 
ATOM   1409  C  CG  . LEU A  1  178 ? -2.776  -11.569 45.567  1.00 85.43  ? 204  LEU A CG  1 
ATOM   1410  C  CD1 . LEU A  1  178 ? -1.832  -12.404 44.730  1.00 85.28  ? 204  LEU A CD1 1 
ATOM   1411  C  CD2 . LEU A  1  178 ? -2.442  -10.079 45.524  1.00 84.47  ? 204  LEU A CD2 1 
ATOM   1412  N  N   . ASN A  1  179 ? -4.447  -9.883  41.929  1.00 83.86  ? 205  ASN A N   1 
ATOM   1413  C  CA  . ASN A  1  179 ? -3.934  -9.771  40.566  1.00 82.49  ? 205  ASN A CA  1 
ATOM   1414  C  C   . ASN A  1  179 ? -2.406  -9.578  40.644  1.00 81.21  ? 205  ASN A C   1 
ATOM   1415  O  O   . ASN A  1  179 ? -1.913  -8.479  40.404  1.00 83.60  ? 205  ASN A O   1 
ATOM   1416  C  CB  . ASN A  1  179 ? -4.591  -8.543  39.909  1.00 84.70  ? 205  ASN A CB  1 
ATOM   1417  C  CG  . ASN A  1  179 ? -4.789  -8.690  38.406  1.00 88.68  ? 205  ASN A CG  1 
ATOM   1418  O  OD1 . ASN A  1  179 ? -5.467  -9.613  37.955  1.00 88.28  ? 205  ASN A OD1 1 
ATOM   1419  N  ND2 . ASN A  1  179 ? -4.214  -7.767  37.632  1.00 92.86  ? 205  ASN A ND2 1 
ATOM   1420  N  N   . LEU A  1  180 ? -1.652  -10.630 40.957  1.00 76.97  ? 206  LEU A N   1 
ATOM   1421  C  CA  . LEU A  1  180 ? -0.198  -10.494 41.070  1.00 72.80  ? 206  LEU A CA  1 
ATOM   1422  C  C   . LEU A  1  180 ? 0.600   -10.900 39.831  1.00 71.75  ? 206  LEU A C   1 
ATOM   1423  O  O   . LEU A  1  180 ? 0.470   -12.026 39.347  1.00 71.87  ? 206  LEU A O   1 
ATOM   1424  C  CB  . LEU A  1  180 ? 0.304   -11.301 42.272  1.00 71.74  ? 206  LEU A CB  1 
ATOM   1425  C  CG  . LEU A  1  180 ? 1.522   -10.799 43.067  1.00 69.88  ? 206  LEU A CG  1 
ATOM   1426  C  CD1 . LEU A  1  180 ? 2.789   -10.910 42.262  1.00 69.77  ? 206  LEU A CD1 1 
ATOM   1427  C  CD2 . LEU A  1  180 ? 1.294   -9.352  43.471  1.00 69.98  ? 206  LEU A CD2 1 
ATOM   1428  N  N   . SER A  1  181 ? 1.423   -9.973  39.328  1.00 70.08  ? 207  SER A N   1 
ATOM   1429  C  CA  . SER A  1  181 ? 2.303   -10.212 38.167  1.00 68.04  ? 207  SER A CA  1 
ATOM   1430  C  C   . SER A  1  181 ? 3.727   -10.357 38.732  1.00 66.38  ? 207  SER A C   1 
ATOM   1431  O  O   . SER A  1  181 ? 4.329   -9.382  39.190  1.00 65.64  ? 207  SER A O   1 
ATOM   1432  C  CB  . SER A  1  181 ? 2.254   -9.031  37.183  1.00 67.81  ? 207  SER A CB  1 
ATOM   1433  O  OG  . SER A  1  181 ? 0.977   -8.894  36.582  1.00 67.03  ? 207  SER A OG  1 
ATOM   1434  N  N   . LEU A  1  182 ? 4.258   -11.573 38.676  1.00 64.66  ? 208  LEU A N   1 
ATOM   1435  C  CA  . LEU A  1  182 ? 5.566   -11.892 39.236  1.00 63.87  ? 208  LEU A CA  1 
ATOM   1436  C  C   . LEU A  1  182 ? 6.699   -12.198 38.239  1.00 64.77  ? 208  LEU A C   1 
ATOM   1437  O  O   . LEU A  1  182 ? 6.502   -12.933 37.256  1.00 65.15  ? 208  LEU A O   1 
ATOM   1438  C  CB  . LEU A  1  182 ? 5.374   -13.078 40.179  1.00 61.66  ? 208  LEU A CB  1 
ATOM   1439  C  CG  . LEU A  1  182 ? 6.523   -13.734 40.925  1.00 60.93  ? 208  LEU A CG  1 
ATOM   1440  C  CD1 . LEU A  1  182 ? 7.084   -12.791 41.968  1.00 60.16  ? 208  LEU A CD1 1 
ATOM   1441  C  CD2 . LEU A  1  182 ? 5.988   -14.987 41.583  1.00 59.91  ? 208  LEU A CD2 1 
ATOM   1442  N  N   . ASP A  1  183 ? 7.889   -11.645 38.508  1.00 64.40  ? 209  ASP A N   1 
ATOM   1443  C  CA  . ASP A  1  183 ? 9.068   -11.870 37.660  1.00 63.29  ? 209  ASP A CA  1 
ATOM   1444  C  C   . ASP A  1  183 ? 10.164  -12.510 38.496  1.00 62.33  ? 209  ASP A C   1 
ATOM   1445  O  O   . ASP A  1  183 ? 10.639  -11.899 39.448  1.00 62.67  ? 209  ASP A O   1 
ATOM   1446  C  CB  . ASP A  1  183 ? 9.610   -10.552 37.087  1.00 63.91  ? 209  ASP A CB  1 
ATOM   1447  C  CG  . ASP A  1  183 ? 10.558  -10.769 35.898  1.00 65.11  ? 209  ASP A CG  1 
ATOM   1448  O  OD1 . ASP A  1  183 ? 11.240  -11.820 35.869  1.00 65.89  ? 209  ASP A OD1 1 
ATOM   1449  O  OD2 . ASP A  1  183 ? 10.633  -9.896  34.995  1.00 63.76  ? 209  ASP A OD2 1 
ATOM   1450  N  N   . LEU A  1  184 ? 10.563  -13.732 38.133  1.00 61.25  ? 210  LEU A N   1 
ATOM   1451  C  CA  . LEU A  1  184 ? 11.626  -14.465 38.846  1.00 60.28  ? 210  LEU A CA  1 
ATOM   1452  C  C   . LEU A  1  184 ? 12.854  -14.742 37.977  1.00 59.94  ? 210  LEU A C   1 
ATOM   1453  O  O   . LEU A  1  184 ? 13.687  -15.570 38.331  1.00 59.65  ? 210  LEU A O   1 
ATOM   1454  C  CB  . LEU A  1  184 ? 11.102  -15.806 39.381  1.00 58.31  ? 210  LEU A CB  1 
ATOM   1455  C  CG  . LEU A  1  184 ? 10.143  -15.736 40.573  1.00 59.15  ? 210  LEU A CG  1 
ATOM   1456  C  CD1 . LEU A  1  184 ? 9.653   -17.131 40.913  1.00 56.43  ? 210  LEU A CD1 1 
ATOM   1457  C  CD2 . LEU A  1  184 ? 10.839  -15.090 41.772  1.00 57.90  ? 210  LEU A CD2 1 
ATOM   1458  N  N   . SER A  1  185 ? 12.965  -14.040 36.851  1.00 59.55  ? 211  SER A N   1 
ATOM   1459  C  CA  . SER A  1  185 ? 14.070  -14.236 35.919  1.00 58.12  ? 211  SER A CA  1 
ATOM   1460  C  C   . SER A  1  185 ? 15.444  -14.037 36.545  1.00 58.65  ? 211  SER A C   1 
ATOM   1461  O  O   . SER A  1  185 ? 15.603  -13.291 37.511  1.00 59.47  ? 211  SER A O   1 
ATOM   1462  C  CB  . SER A  1  185 ? 13.914  -13.302 34.715  1.00 56.89  ? 211  SER A CB  1 
ATOM   1463  O  OG  . SER A  1  185 ? 12.701  -13.542 34.021  1.00 53.85  ? 211  SER A OG  1 
ATOM   1464  N  N   . LEU A  1  186 ? 16.430  -14.726 35.978  1.00 58.98  ? 212  LEU A N   1 
ATOM   1465  C  CA  . LEU A  1  186 ? 17.821  -14.663 36.425  1.00 58.90  ? 212  LEU A CA  1 
ATOM   1466  C  C   . LEU A  1  186 ? 18.100  -15.083 37.873  1.00 60.57  ? 212  LEU A C   1 
ATOM   1467  O  O   . LEU A  1  186 ? 19.068  -14.640 38.477  1.00 61.97  ? 212  LEU A O   1 
ATOM   1468  C  CB  . LEU A  1  186 ? 18.374  -13.267 36.155  1.00 55.41  ? 212  LEU A CB  1 
ATOM   1469  C  CG  . LEU A  1  186 ? 18.487  -12.966 34.659  1.00 54.62  ? 212  LEU A CG  1 
ATOM   1470  C  CD1 . LEU A  1  186 ? 18.940  -11.545 34.455  1.00 53.76  ? 212  LEU A CD1 1 
ATOM   1471  C  CD2 . LEU A  1  186 ? 19.450  -13.946 33.998  1.00 52.40  ? 212  LEU A CD2 1 
ATOM   1472  N  N   . ASN A  1  187 ? 17.244  -15.932 38.433  1.00 62.43  ? 213  ASN A N   1 
ATOM   1473  C  CA  . ASN A  1  187 ? 17.445  -16.449 39.780  1.00 63.77  ? 213  ASN A CA  1 
ATOM   1474  C  C   . ASN A  1  187 ? 17.919  -17.866 39.511  1.00 66.84  ? 213  ASN A C   1 
ATOM   1475  O  O   . ASN A  1  187 ? 17.309  -18.587 38.721  1.00 67.65  ? 213  ASN A O   1 
ATOM   1476  C  CB  . ASN A  1  187 ? 16.139  -16.457 40.571  1.00 62.50  ? 213  ASN A CB  1 
ATOM   1477  C  CG  . ASN A  1  187 ? 15.908  -15.160 41.341  1.00 63.63  ? 213  ASN A CG  1 
ATOM   1478  O  OD1 . ASN A  1  187 ? 16.550  -14.900 42.356  1.00 63.58  ? 213  ASN A OD1 1 
ATOM   1479  N  ND2 . ASN A  1  187 ? 14.988  -14.339 40.855  1.00 63.84  ? 213  ASN A ND2 1 
ATOM   1480  N  N   . PRO A  1  188 ? 19.032  -18.280 40.138  1.00 69.29  ? 214  PRO A N   1 
ATOM   1481  C  CA  . PRO A  1  188 ? 19.594  -19.625 39.954  1.00 70.35  ? 214  PRO A CA  1 
ATOM   1482  C  C   . PRO A  1  188 ? 18.734  -20.739 40.566  1.00 72.89  ? 214  PRO A C   1 
ATOM   1483  O  O   . PRO A  1  188 ? 19.146  -21.443 41.493  1.00 72.88  ? 214  PRO A O   1 
ATOM   1484  C  CB  . PRO A  1  188 ? 20.958  -19.505 40.610  1.00 69.83  ? 214  PRO A CB  1 
ATOM   1485  C  CG  . PRO A  1  188 ? 20.674  -18.583 41.759  1.00 69.02  ? 214  PRO A CG  1 
ATOM   1486  C  CD  . PRO A  1  188 ? 19.807  -17.516 41.134  1.00 68.94  ? 214  PRO A CD  1 
ATOM   1487  N  N   . MET A  1  189 ? 17.535  -20.890 40.019  1.00 74.89  ? 215  MET A N   1 
ATOM   1488  C  CA  . MET A  1  189 ? 16.578  -21.883 40.477  1.00 76.76  ? 215  MET A CA  1 
ATOM   1489  C  C   . MET A  1  189 ? 17.028  -23.288 40.126  1.00 77.89  ? 215  MET A C   1 
ATOM   1490  O  O   . MET A  1  189 ? 17.687  -23.496 39.105  1.00 79.21  ? 215  MET A O   1 
ATOM   1491  C  CB  . MET A  1  189 ? 15.238  -21.620 39.802  1.00 78.35  ? 215  MET A CB  1 
ATOM   1492  C  CG  . MET A  1  189 ? 14.032  -22.147 40.538  1.00 81.04  ? 215  MET A CG  1 
ATOM   1493  S  SD  . MET A  1  189 ? 13.342  -20.873 41.612  1.00 83.86  ? 215  MET A SD  1 
ATOM   1494  C  CE  . MET A  1  189 ? 12.641  -19.762 40.373  1.00 82.81  ? 215  MET A CE  1 
ATOM   1495  N  N   . ASN A  1  190 ? 16.687  -24.254 40.970  1.00 78.30  ? 216  ASN A N   1 
ATOM   1496  C  CA  . ASN A  1  190 ? 17.022  -25.647 40.674  1.00 80.14  ? 216  ASN A CA  1 
ATOM   1497  C  C   . ASN A  1  190 ? 16.133  -26.631 41.416  1.00 79.54  ? 216  ASN A C   1 
ATOM   1498  O  O   . ASN A  1  190 ? 16.336  -27.840 41.331  1.00 79.05  ? 216  ASN A O   1 
ATOM   1499  C  CB  . ASN A  1  190 ? 18.500  -25.950 40.942  1.00 82.42  ? 216  ASN A CB  1 
ATOM   1500  C  CG  . ASN A  1  190 ? 18.955  -25.460 42.279  1.00 85.29  ? 216  ASN A CG  1 
ATOM   1501  O  OD1 . ASN A  1  190 ? 18.408  -25.852 43.311  1.00 86.81  ? 216  ASN A OD1 1 
ATOM   1502  N  ND2 . ASN A  1  190 ? 19.967  -24.591 42.279  1.00 86.43  ? 216  ASN A ND2 1 
ATOM   1503  N  N   . PHE A  1  191 ? 15.143  -26.103 42.134  1.00 79.16  ? 217  PHE A N   1 
ATOM   1504  C  CA  . PHE A  1  191 ? 14.180  -26.932 42.853  1.00 78.41  ? 217  PHE A CA  1 
ATOM   1505  C  C   . PHE A  1  191 ? 12.932  -26.197 43.336  1.00 78.09  ? 217  PHE A C   1 
ATOM   1506  O  O   . PHE A  1  191 ? 13.007  -25.225 44.099  1.00 77.09  ? 217  PHE A O   1 
ATOM   1507  C  CB  . PHE A  1  191 ? 14.823  -27.635 44.055  1.00 78.29  ? 217  PHE A CB  1 
ATOM   1508  C  CG  . PHE A  1  191 ? 13.855  -28.503 44.848  1.00 78.09  ? 217  PHE A CG  1 
ATOM   1509  C  CD1 . PHE A  1  191 ? 13.277  -29.643 44.273  1.00 78.09  ? 217  PHE A CD1 1 
ATOM   1510  C  CD2 . PHE A  1  191 ? 13.499  -28.164 46.157  1.00 77.62  ? 217  PHE A CD2 1 
ATOM   1511  C  CE1 . PHE A  1  191 ? 12.363  -30.432 44.992  1.00 77.32  ? 217  PHE A CE1 1 
ATOM   1512  C  CE2 . PHE A  1  191 ? 12.591  -28.942 46.885  1.00 76.28  ? 217  PHE A CE2 1 
ATOM   1513  C  CZ  . PHE A  1  191 ? 12.018  -30.079 46.301  1.00 76.72  ? 217  PHE A CZ  1 
ATOM   1514  N  N   . ILE A  1  192 ? 11.783  -26.676 42.869  1.00 77.49  ? 218  ILE A N   1 
ATOM   1515  C  CA  . ILE A  1  192 ? 10.487  -26.153 43.270  1.00 77.09  ? 218  ILE A CA  1 
ATOM   1516  C  C   . ILE A  1  192 ? 9.752   -27.388 43.797  1.00 77.96  ? 218  ILE A C   1 
ATOM   1517  O  O   . ILE A  1  192 ? 9.378   -28.279 43.037  1.00 76.59  ? 218  ILE A O   1 
ATOM   1518  C  CB  . ILE A  1  192 ? 9.734   -25.527 42.085  1.00 75.79  ? 218  ILE A CB  1 
ATOM   1519  C  CG1 . ILE A  1  192 ? 10.457  -24.259 41.623  1.00 75.00  ? 218  ILE A CG1 1 
ATOM   1520  C  CG2 . ILE A  1  192 ? 8.323   -25.174 42.501  1.00 76.15  ? 218  ILE A CG2 1 
ATOM   1521  C  CD1 . ILE A  1  192 ? 9.895   -23.642 40.365  1.00 73.95  ? 218  ILE A CD1 1 
ATOM   1522  N  N   . GLN A  1  193 ? 9.594   -27.440 45.120  1.00 80.46  ? 219  GLN A N   1 
ATOM   1523  C  CA  . GLN A  1  193 ? 8.950   -28.563 45.819  1.00 81.34  ? 219  GLN A CA  1 
ATOM   1524  C  C   . GLN A  1  193 ? 7.573   -28.899 45.270  1.00 80.98  ? 219  GLN A C   1 
ATOM   1525  O  O   . GLN A  1  193 ? 6.665   -28.071 45.317  1.00 81.59  ? 219  GLN A O   1 
ATOM   1526  C  CB  . GLN A  1  193 ? 8.822   -28.246 47.309  1.00 82.57  ? 219  GLN A CB  1 
ATOM   1527  C  CG  . GLN A  1  193 ? 8.573   -29.458 48.178  1.00 83.86  ? 219  GLN A CG  1 
ATOM   1528  C  CD  . GLN A  1  193 ? 7.834   -29.113 49.452  1.00 85.30  ? 219  GLN A CD  1 
ATOM   1529  O  OE1 . GLN A  1  193 ? 8.142   -28.115 50.119  1.00 85.19  ? 219  GLN A OE1 1 
ATOM   1530  N  NE2 . GLN A  1  193 ? 6.851   -29.941 49.804  1.00 86.03  ? 219  GLN A NE2 1 
ATOM   1531  N  N   . PRO A  1  194 ? 7.390   -30.131 44.768  1.00 80.42  ? 220  PRO A N   1 
ATOM   1532  C  CA  . PRO A  1  194 ? 6.102   -30.556 44.209  1.00 80.16  ? 220  PRO A CA  1 
ATOM   1533  C  C   . PRO A  1  194 ? 4.874   -30.131 45.015  1.00 80.37  ? 220  PRO A C   1 
ATOM   1534  O  O   . PRO A  1  194 ? 4.892   -30.102 46.246  1.00 79.14  ? 220  PRO A O   1 
ATOM   1535  C  CB  . PRO A  1  194 ? 6.255   -32.068 44.117  1.00 79.08  ? 220  PRO A CB  1 
ATOM   1536  C  CG  . PRO A  1  194 ? 7.685   -32.213 43.766  1.00 79.20  ? 220  PRO A CG  1 
ATOM   1537  C  CD  . PRO A  1  194 ? 8.369   -31.228 44.702  1.00 80.00  ? 220  PRO A CD  1 
ATOM   1538  N  N   . GLY A  1  195 ? 3.812   -29.791 44.290  1.00 81.42  ? 221  GLY A N   1 
ATOM   1539  C  CA  . GLY A  1  195 ? 2.569   -29.375 44.913  1.00 82.62  ? 221  GLY A CA  1 
ATOM   1540  C  C   . GLY A  1  195 ? 2.626   -28.024 45.600  1.00 83.01  ? 221  GLY A C   1 
ATOM   1541  O  O   . GLY A  1  195 ? 1.662   -27.624 46.262  1.00 83.30  ? 221  GLY A O   1 
ATOM   1542  N  N   . ALA A  1  196 ? 3.740   -27.317 45.443  1.00 82.48  ? 222  ALA A N   1 
ATOM   1543  C  CA  . ALA A  1  196 ? 3.906   -26.011 46.070  1.00 82.16  ? 222  ALA A CA  1 
ATOM   1544  C  C   . ALA A  1  196 ? 2.983   -24.955 45.479  1.00 82.23  ? 222  ALA A C   1 
ATOM   1545  O  O   . ALA A  1  196 ? 2.623   -23.997 46.161  1.00 81.90  ? 222  ALA A O   1 
ATOM   1546  C  CB  . ALA A  1  196 ? 5.353   -25.556 45.955  1.00 81.41  ? 222  ALA A CB  1 
ATOM   1547  N  N   . PHE A  1  197 ? 2.597   -25.125 44.216  1.00 82.36  ? 223  PHE A N   1 
ATOM   1548  C  CA  . PHE A  1  197 ? 1.725   -24.148 43.580  1.00 81.86  ? 223  PHE A CA  1 
ATOM   1549  C  C   . PHE A  1  197 ? 0.261   -24.530 43.471  1.00 83.21  ? 223  PHE A C   1 
ATOM   1550  O  O   . PHE A  1  197 ? -0.523  -23.795 42.866  1.00 83.46  ? 223  PHE A O   1 
ATOM   1551  C  CB  . PHE A  1  197 ? 2.266   -23.766 42.200  1.00 79.51  ? 223  PHE A CB  1 
ATOM   1552  C  CG  . PHE A  1  197 ? 3.413   -22.798 42.259  1.00 76.79  ? 223  PHE A CG  1 
ATOM   1553  C  CD1 . PHE A  1  197 ? 4.722   -23.247 42.385  1.00 74.99  ? 223  PHE A CD1 1 
ATOM   1554  C  CD2 . PHE A  1  197 ? 3.174   -21.429 42.264  1.00 75.58  ? 223  PHE A CD2 1 
ATOM   1555  C  CE1 . PHE A  1  197 ? 5.773   -22.347 42.523  1.00 73.32  ? 223  PHE A CE1 1 
ATOM   1556  C  CE2 . PHE A  1  197 ? 4.218   -20.525 42.401  1.00 73.48  ? 223  PHE A CE2 1 
ATOM   1557  C  CZ  . PHE A  1  197 ? 5.522   -20.985 42.532  1.00 72.13  ? 223  PHE A CZ  1 
ATOM   1558  N  N   . LYS A  1  198 ? -0.113  -25.667 44.057  1.00 84.77  ? 224  LYS A N   1 
ATOM   1559  C  CA  . LYS A  1  198 ? -1.507  -26.111 44.029  1.00 85.05  ? 224  LYS A CA  1 
ATOM   1560  C  C   . LYS A  1  198 ? -2.448  -25.001 44.511  1.00 84.10  ? 224  LYS A C   1 
ATOM   1561  O  O   . LYS A  1  198 ? -2.290  -24.444 45.599  1.00 82.46  ? 224  LYS A O   1 
ATOM   1562  C  CB  . LYS A  1  198 ? -1.702  -27.361 44.898  1.00 86.12  ? 224  LYS A CB  1 
ATOM   1563  C  CG  . LYS A  1  198 ? -1.573  -28.697 44.161  1.00 87.66  ? 224  LYS A CG  1 
ATOM   1564  C  CD  . LYS A  1  198 ? -1.922  -29.865 45.101  1.00 89.01  ? 224  LYS A CD  1 
ATOM   1565  C  CE  . LYS A  1  198 ? -1.860  -31.218 44.397  1.00 88.74  ? 224  LYS A CE  1 
ATOM   1566  N  NZ  . LYS A  1  198 ? -2.077  -32.364 45.331  1.00 88.09  ? 224  LYS A NZ  1 
ATOM   1567  N  N   . GLU A  1  199 ? -3.421  -24.680 43.671  1.00 83.97  ? 225  GLU A N   1 
ATOM   1568  C  CA  . GLU A  1  199 ? -4.402  -23.651 43.970  1.00 83.81  ? 225  GLU A CA  1 
ATOM   1569  C  C   . GLU A  1  199 ? -3.842  -22.264 44.224  1.00 81.64  ? 225  GLU A C   1 
ATOM   1570  O  O   . GLU A  1  199 ? -4.328  -21.522 45.084  1.00 80.72  ? 225  GLU A O   1 
ATOM   1571  C  CB  . GLU A  1  199 ? -5.275  -24.082 45.140  1.00 86.73  ? 225  GLU A CB  1 
ATOM   1572  C  CG  . GLU A  1  199 ? -6.190  -25.241 44.781  1.00 90.51  ? 225  GLU A CG  1 
ATOM   1573  C  CD  . GLU A  1  199 ? -7.321  -25.416 45.760  1.00 92.41  ? 225  GLU A CD  1 
ATOM   1574  O  OE1 . GLU A  1  199 ? -7.039  -25.718 46.945  1.00 93.57  ? 225  GLU A OE1 1 
ATOM   1575  O  OE2 . GLU A  1  199 ? -8.490  -25.246 45.339  1.00 93.73  ? 225  GLU A OE2 1 
ATOM   1576  N  N   . ILE A  1  200 ? -2.815  -21.921 43.460  1.00 79.24  ? 226  ILE A N   1 
ATOM   1577  C  CA  . ILE A  1  200 ? -2.206  -20.610 43.550  1.00 77.19  ? 226  ILE A CA  1 
ATOM   1578  C  C   . ILE A  1  200 ? -2.577  -19.944 42.239  1.00 75.11  ? 226  ILE A C   1 
ATOM   1579  O  O   . ILE A  1  200 ? -2.699  -20.623 41.214  1.00 74.76  ? 226  ILE A O   1 
ATOM   1580  C  CB  . ILE A  1  200 ? -0.675  -20.699 43.648  1.00 77.58  ? 226  ILE A CB  1 
ATOM   1581  C  CG1 . ILE A  1  200 ? -0.273  -21.429 44.927  1.00 78.10  ? 226  ILE A CG1 1 
ATOM   1582  C  CG2 . ILE A  1  200 ? -0.083  -19.301 43.654  1.00 77.69  ? 226  ILE A CG2 1 
ATOM   1583  C  CD1 . ILE A  1  200 ? -0.635  -20.680 46.202  1.00 77.98  ? 226  ILE A CD1 1 
ATOM   1584  N  N   . ARG A  1  201 ? -2.768  -18.631 42.256  1.00 72.79  ? 227  ARG A N   1 
ATOM   1585  C  CA  . ARG A  1  201 ? -3.127  -17.946 41.031  1.00 71.18  ? 227  ARG A CA  1 
ATOM   1586  C  C   . ARG A  1  201 ? -2.391  -16.638 40.786  1.00 68.27  ? 227  ARG A C   1 
ATOM   1587  O  O   . ARG A  1  201 ? -2.509  -15.673 41.538  1.00 67.52  ? 227  ARG A O   1 
ATOM   1588  C  CB  . ARG A  1  201 ? -4.634  -17.709 40.991  1.00 74.08  ? 227  ARG A CB  1 
ATOM   1589  C  CG  . ARG A  1  201 ? -5.111  -16.919 39.783  1.00 79.72  ? 227  ARG A CG  1 
ATOM   1590  C  CD  . ARG A  1  201 ? -6.627  -16.887 39.743  1.00 85.33  ? 227  ARG A CD  1 
ATOM   1591  N  NE  . ARG A  1  201 ? -7.166  -16.425 41.020  1.00 90.43  ? 227  ARG A NE  1 
ATOM   1592  C  CZ  . ARG A  1  201 ? -8.450  -16.484 41.369  1.00 92.57  ? 227  ARG A CZ  1 
ATOM   1593  N  NH1 . ARG A  1  201 ? -9.354  -16.991 40.525  1.00 93.24  ? 227  ARG A NH1 1 
ATOM   1594  N  NH2 . ARG A  1  201 ? -8.825  -16.044 42.571  1.00 92.20  ? 227  ARG A NH2 1 
ATOM   1595  N  N   . LEU A  1  202 ? -1.633  -16.626 39.701  1.00 64.70  ? 228  LEU A N   1 
ATOM   1596  C  CA  . LEU A  1  202 ? -0.874  -15.462 39.302  1.00 61.25  ? 228  LEU A CA  1 
ATOM   1597  C  C   . LEU A  1  202 ? -1.473  -14.907 38.018  1.00 59.85  ? 228  LEU A C   1 
ATOM   1598  O  O   . LEU A  1  202 ? -2.092  -15.644 37.252  1.00 58.70  ? 228  LEU A O   1 
ATOM   1599  C  CB  . LEU A  1  202 ? 0.579   -15.861 39.048  1.00 59.57  ? 228  LEU A CB  1 
ATOM   1600  C  CG  . LEU A  1  202 ? 1.566   -16.066 40.198  1.00 57.82  ? 228  LEU A CG  1 
ATOM   1601  C  CD1 . LEU A  1  202 ? 0.862   -16.063 41.535  1.00 55.72  ? 228  LEU A CD1 1 
ATOM   1602  C  CD2 . LEU A  1  202 ? 2.314   -17.363 39.958  1.00 56.21  ? 228  LEU A CD2 1 
ATOM   1603  N  N   . HIS A  1  203 ? -1.290  -13.612 37.779  1.00 58.63  ? 229  HIS A N   1 
ATOM   1604  C  CA  . HIS A  1  203 ? -1.788  -13.019 36.546  1.00 58.98  ? 229  HIS A CA  1 
ATOM   1605  C  C   . HIS A  1  203 ? -0.727  -13.213 35.450  1.00 58.95  ? 229  HIS A C   1 
ATOM   1606  O  O   . HIS A  1  203 ? -1.049  -13.526 34.298  1.00 59.59  ? 229  HIS A O   1 
ATOM   1607  C  CB  . HIS A  1  203 ? -2.103  -11.534 36.736  1.00 59.21  ? 229  HIS A CB  1 
ATOM   1608  C  CG  . HIS A  1  203 ? -2.673  -10.885 35.512  1.00 61.56  ? 229  HIS A CG  1 
ATOM   1609  N  ND1 . HIS A  1  203 ? -1.909  -10.146 34.634  1.00 62.41  ? 229  HIS A ND1 1 
ATOM   1610  C  CD2 . HIS A  1  203 ? -3.919  -10.924 34.985  1.00 61.93  ? 229  HIS A CD2 1 
ATOM   1611  C  CE1 . HIS A  1  203 ? -2.657  -9.761  33.617  1.00 61.98  ? 229  HIS A CE1 1 
ATOM   1612  N  NE2 . HIS A  1  203 ? -3.881  -10.220 33.806  1.00 62.88  ? 229  HIS A NE2 1 
ATOM   1613  N  N   . LYS A  1  204 ? 0.540   -13.030 35.823  1.00 57.75  ? 230  LYS A N   1 
ATOM   1614  C  CA  . LYS A  1  204 ? 1.664   -13.212 34.899  1.00 56.26  ? 230  LYS A CA  1 
ATOM   1615  C  C   . LYS A  1  204 ? 2.821   -13.827 35.703  1.00 55.19  ? 230  LYS A C   1 
ATOM   1616  O  O   . LYS A  1  204 ? 2.955   -13.569 36.907  1.00 54.81  ? 230  LYS A O   1 
ATOM   1617  C  CB  . LYS A  1  204 ? 2.098   -11.853 34.311  1.00 54.47  ? 230  LYS A CB  1 
ATOM   1618  C  CG  . LYS A  1  204 ? 3.043   -11.901 33.081  1.00 52.27  ? 230  LYS A CG  1 
ATOM   1619  C  CD  . LYS A  1  204 ? 3.459   -10.465 32.685  1.00 53.42  ? 230  LYS A CD  1 
ATOM   1620  C  CE  . LYS A  1  204 ? 4.036   -10.325 31.270  1.00 54.11  ? 230  LYS A CE  1 
ATOM   1621  N  NZ  . LYS A  1  204 ? 5.538   -10.422 31.176  1.00 53.29  ? 230  LYS A NZ  1 
ATOM   1622  N  N   . LEU A  1  205 ? 3.631   -14.654 35.042  1.00 52.56  ? 231  LEU A N   1 
ATOM   1623  C  CA  . LEU A  1  205 ? 4.792   -15.275 35.666  1.00 51.03  ? 231  LEU A CA  1 
ATOM   1624  C  C   . LEU A  1  205 ? 5.855   -15.269 34.586  1.00 51.75  ? 231  LEU A C   1 
ATOM   1625  O  O   . LEU A  1  205 ? 5.601   -15.691 33.457  1.00 52.22  ? 231  LEU A O   1 
ATOM   1626  C  CB  . LEU A  1  205 ? 4.513   -16.725 36.060  1.00 49.57  ? 231  LEU A CB  1 
ATOM   1627  C  CG  . LEU A  1  205 ? 5.253   -17.356 37.255  1.00 48.62  ? 231  LEU A CG  1 
ATOM   1628  C  CD1 . LEU A  1  205 ? 5.272   -18.859 37.059  1.00 47.73  ? 231  LEU A CD1 1 
ATOM   1629  C  CD2 . LEU A  1  205 ? 6.667   -16.844 37.388  1.00 46.33  ? 231  LEU A CD2 1 
ATOM   1630  N  N   . THR A  1  206 ? 7.037   -14.765 34.909  1.00 52.44  ? 232  THR A N   1 
ATOM   1631  C  CA  . THR A  1  206 ? 8.121   -14.754 33.937  1.00 52.42  ? 232  THR A CA  1 
ATOM   1632  C  C   . THR A  1  206 ? 9.289   -15.506 34.564  1.00 52.83  ? 232  THR A C   1 
ATOM   1633  O  O   . THR A  1  206 ? 9.753   -15.165 35.655  1.00 53.22  ? 232  THR A O   1 
ATOM   1634  C  CB  . THR A  1  206 ? 8.569   -13.318 33.582  1.00 52.51  ? 232  THR A CB  1 
ATOM   1635  O  OG1 . THR A  1  206 ? 7.463   -12.571 33.066  1.00 53.28  ? 232  THR A OG1 1 
ATOM   1636  C  CG2 . THR A  1  206 ? 9.648   -13.350 32.525  1.00 51.40  ? 232  THR A CG2 1 
ATOM   1637  N  N   . LEU A  1  207 ? 9.729   -16.552 33.879  1.00 52.07  ? 233  LEU A N   1 
ATOM   1638  C  CA  . LEU A  1  207 ? 10.845  -17.373 34.327  1.00 51.99  ? 233  LEU A CA  1 
ATOM   1639  C  C   . LEU A  1  207 ? 11.834  -17.503 33.176  1.00 53.13  ? 233  LEU A C   1 
ATOM   1640  O  O   . LEU A  1  207 ? 11.851  -18.510 32.448  1.00 52.57  ? 233  LEU A O   1 
ATOM   1641  C  CB  . LEU A  1  207 ? 10.358  -18.759 34.747  1.00 52.19  ? 233  LEU A CB  1 
ATOM   1642  C  CG  . LEU A  1  207 ? 9.520   -18.838 36.024  1.00 53.03  ? 233  LEU A CG  1 
ATOM   1643  C  CD1 . LEU A  1  207 ? 8.997   -20.242 36.207  1.00 52.67  ? 233  LEU A CD1 1 
ATOM   1644  C  CD2 . LEU A  1  207 ? 10.353  -18.426 37.224  1.00 52.91  ? 233  LEU A CD2 1 
ATOM   1645  N  N   . ARG A  1  208 ? 12.635  -16.458 32.994  1.00 54.19  ? 234  ARG A N   1 
ATOM   1646  C  CA  . ARG A  1  208 ? 13.633  -16.433 31.936  1.00 55.46  ? 234  ARG A CA  1 
ATOM   1647  C  C   . ARG A  1  208 ? 15.048  -16.579 32.497  1.00 57.27  ? 234  ARG A C   1 
ATOM   1648  O  O   . ARG A  1  208 ? 15.430  -15.896 33.451  1.00 57.94  ? 234  ARG A O   1 
ATOM   1649  C  CB  . ARG A  1  208 ? 13.509  -15.133 31.135  1.00 54.48  ? 234  ARG A CB  1 
ATOM   1650  C  CG  . ARG A  1  208 ? 12.266  -15.058 30.257  1.00 52.93  ? 234  ARG A CG  1 
ATOM   1651  C  CD  . ARG A  1  208 ? 12.218  -13.760 29.478  1.00 52.41  ? 234  ARG A CD  1 
ATOM   1652  N  NE  . ARG A  1  208 ? 13.172  -13.722 28.374  1.00 51.62  ? 234  ARG A NE  1 
ATOM   1653  C  CZ  . ARG A  1  208 ? 13.569  -12.603 27.781  1.00 50.80  ? 234  ARG A CZ  1 
ATOM   1654  N  NH1 . ARG A  1  208 ? 13.097  -11.428 28.193  1.00 50.03  ? 234  ARG A NH1 1 
ATOM   1655  N  NH2 . ARG A  1  208 ? 14.433  -12.660 26.780  1.00 49.33  ? 234  ARG A NH2 1 
ATOM   1656  N  N   . ASN A  1  209 ? 15.817  -17.481 31.895  1.00 59.25  ? 235  ASN A N   1 
ATOM   1657  C  CA  . ASN A  1  209 ? 17.189  -17.747 32.310  1.00 61.39  ? 235  ASN A CA  1 
ATOM   1658  C  C   . ASN A  1  209 ? 17.270  -18.209 33.748  1.00 62.46  ? 235  ASN A C   1 
ATOM   1659  O  O   . ASN A  1  209 ? 18.144  -17.778 34.499  1.00 64.19  ? 235  ASN A O   1 
ATOM   1660  C  CB  . ASN A  1  209 ? 18.060  -16.504 32.135  1.00 61.25  ? 235  ASN A CB  1 
ATOM   1661  C  CG  . ASN A  1  209 ? 19.175  -16.719 31.138  1.00 62.34  ? 235  ASN A CG  1 
ATOM   1662  O  OD1 . ASN A  1  209 ? 19.997  -15.837 30.907  1.00 63.34  ? 235  ASN A OD1 1 
ATOM   1663  N  ND2 . ASN A  1  209 ? 19.204  -17.900 30.530  1.00 62.83  ? 235  ASN A ND2 1 
ATOM   1664  N  N   . ASN A  1  210 ? 16.371  -19.099 34.135  1.00 63.84  ? 236  ASN A N   1 
ATOM   1665  C  CA  . ASN A  1  210 ? 16.379  -19.583 35.499  1.00 65.83  ? 236  ASN A CA  1 
ATOM   1666  C  C   . ASN A  1  210 ? 17.031  -20.930 35.683  1.00 67.50  ? 236  ASN A C   1 
ATOM   1667  O  O   . ASN A  1  210 ? 17.691  -21.164 36.689  1.00 68.82  ? 236  ASN A O   1 
ATOM   1668  C  CB  . ASN A  1  210 ? 14.961  -19.671 36.034  1.00 66.24  ? 236  ASN A CB  1 
ATOM   1669  C  CG  . ASN A  1  210 ? 14.374  -18.325 36.312  1.00 67.67  ? 236  ASN A CG  1 
ATOM   1670  O  OD1 . ASN A  1  210 ? 14.941  -17.539 37.055  1.00 68.88  ? 236  ASN A OD1 1 
ATOM   1671  N  ND2 . ASN A  1  210 ? 13.226  -18.046 35.721  1.00 68.86  ? 236  ASN A ND2 1 
ATOM   1672  N  N   . PHE A  1  211 ? 16.861  -21.815 34.712  1.00 68.57  ? 237  PHE A N   1 
ATOM   1673  C  CA  . PHE A  1  211 ? 17.385  -23.154 34.858  1.00 68.98  ? 237  PHE A CA  1 
ATOM   1674  C  C   . PHE A  1  211 ? 18.676  -23.440 34.143  1.00 69.50  ? 237  PHE A C   1 
ATOM   1675  O  O   . PHE A  1  211 ? 18.881  -23.010 33.007  1.00 68.11  ? 237  PHE A O   1 
ATOM   1676  C  CB  . PHE A  1  211 ? 16.293  -24.131 34.459  1.00 69.36  ? 237  PHE A CB  1 
ATOM   1677  C  CG  . PHE A  1  211 ? 14.923  -23.669 34.866  1.00 69.49  ? 237  PHE A CG  1 
ATOM   1678  C  CD1 . PHE A  1  211 ? 14.039  -23.150 33.920  1.00 69.40  ? 237  PHE A CD1 1 
ATOM   1679  C  CD2 . PHE A  1  211 ? 14.550  -23.670 36.203  1.00 69.18  ? 237  PHE A CD2 1 
ATOM   1680  C  CE1 . PHE A  1  211 ? 12.801  -22.633 34.295  1.00 69.27  ? 237  PHE A CE1 1 
ATOM   1681  C  CE2 . PHE A  1  211 ? 13.314  -23.154 36.595  1.00 70.67  ? 237  PHE A CE2 1 
ATOM   1682  C  CZ  . PHE A  1  211 ? 12.435  -22.631 35.630  1.00 69.99  ? 237  PHE A CZ  1 
ATOM   1683  N  N   . ASP A  1  212 ? 19.536  -24.180 34.848  1.00 70.64  ? 238  ASP A N   1 
ATOM   1684  C  CA  . ASP A  1  212 ? 20.863  -24.568 34.383  1.00 70.50  ? 238  ASP A CA  1 
ATOM   1685  C  C   . ASP A  1  212 ? 20.846  -25.565 33.229  1.00 68.79  ? 238  ASP A C   1 
ATOM   1686  O  O   . ASP A  1  212 ? 21.378  -25.293 32.159  1.00 68.32  ? 238  ASP A O   1 
ATOM   1687  C  CB  . ASP A  1  212 ? 21.648  -25.136 35.563  1.00 73.04  ? 238  ASP A CB  1 
ATOM   1688  C  CG  . ASP A  1  212 ? 23.106  -25.330 35.245  1.00 77.15  ? 238  ASP A CG  1 
ATOM   1689  O  OD1 . ASP A  1  212 ? 23.710  -24.430 34.613  1.00 78.19  ? 238  ASP A OD1 1 
ATOM   1690  O  OD2 . ASP A  1  212 ? 23.657  -26.381 35.641  1.00 80.65  ? 238  ASP A OD2 1 
ATOM   1691  N  N   . SER A  1  213 ? 20.234  -26.721 33.451  1.00 67.98  ? 239  SER A N   1 
ATOM   1692  C  CA  . SER A  1  213 ? 20.137  -27.757 32.426  1.00 67.00  ? 239  SER A CA  1 
ATOM   1693  C  C   . SER A  1  213 ? 18.680  -27.915 32.000  1.00 66.90  ? 239  SER A C   1 
ATOM   1694  O  O   . SER A  1  213 ? 17.795  -27.262 32.561  1.00 66.35  ? 239  SER A O   1 
ATOM   1695  C  CB  . SER A  1  213 ? 20.627  -29.090 32.985  1.00 67.08  ? 239  SER A CB  1 
ATOM   1696  O  OG  . SER A  1  213 ? 19.749  -29.564 33.993  1.00 66.15  ? 239  SER A OG  1 
ATOM   1697  N  N   . LEU A  1  214 ? 18.433  -28.791 31.024  1.00 66.62  ? 240  LEU A N   1 
ATOM   1698  C  CA  . LEU A  1  214 ? 17.068  -29.037 30.550  1.00 67.00  ? 240  LEU A CA  1 
ATOM   1699  C  C   . LEU A  1  214 ? 16.342  -29.843 31.628  1.00 67.42  ? 240  LEU A C   1 
ATOM   1700  O  O   . LEU A  1  214 ? 15.136  -29.712 31.830  1.00 66.76  ? 240  LEU A O   1 
ATOM   1701  C  CB  . LEU A  1  214 ? 17.079  -29.841 29.242  1.00 65.91  ? 240  LEU A CB  1 
ATOM   1702  C  CG  . LEU A  1  214 ? 15.948  -29.651 28.218  1.00 65.26  ? 240  LEU A CG  1 
ATOM   1703  C  CD1 . LEU A  1  214 ? 15.989  -30.793 27.231  1.00 63.82  ? 240  LEU A CD1 1 
ATOM   1704  C  CD2 . LEU A  1  214 ? 14.590  -29.615 28.891  1.00 64.86  ? 240  LEU A CD2 1 
ATOM   1705  N  N   . ASN A  1  215 ? 17.103  -30.678 32.324  1.00 68.57  ? 241  ASN A N   1 
ATOM   1706  C  CA  . ASN A  1  215 ? 16.564  -31.531 33.372  1.00 68.73  ? 241  ASN A CA  1 
ATOM   1707  C  C   . ASN A  1  215 ? 16.167  -30.722 34.585  1.00 67.69  ? 241  ASN A C   1 
ATOM   1708  O  O   . ASN A  1  215 ? 15.171  -31.030 35.239  1.00 66.93  ? 241  ASN A O   1 
ATOM   1709  C  CB  . ASN A  1  215 ? 17.600  -32.589 33.726  1.00 71.00  ? 241  ASN A CB  1 
ATOM   1710  C  CG  . ASN A  1  215 ? 17.972  -33.437 32.521  1.00 75.45  ? 241  ASN A CG  1 
ATOM   1711  O  OD1 . ASN A  1  215 ? 17.204  -34.319 32.116  1.00 77.30  ? 241  ASN A OD1 1 
ATOM   1712  N  ND2 . ASN A  1  215 ? 19.142  -33.157 31.918  1.00 76.00  ? 241  ASN A ND2 1 
ATOM   1713  N  N   . VAL A  1  216 ? 16.942  -29.686 34.879  1.00 66.61  ? 242  VAL A N   1 
ATOM   1714  C  CA  . VAL A  1  216 ? 16.629  -28.829 36.009  1.00 65.36  ? 242  VAL A CA  1 
ATOM   1715  C  C   . VAL A  1  216 ? 15.368  -28.042 35.668  1.00 64.88  ? 242  VAL A C   1 
ATOM   1716  O  O   . VAL A  1  216 ? 14.528  -27.793 36.541  1.00 64.50  ? 242  VAL A O   1 
ATOM   1717  C  CB  . VAL A  1  216 ? 17.779  -27.845 36.314  1.00 65.30  ? 242  VAL A CB  1 
ATOM   1718  C  CG1 . VAL A  1  216 ? 17.353  -26.834 37.390  1.00 64.37  ? 242  VAL A CG1 1 
ATOM   1719  C  CG2 . VAL A  1  216 ? 18.995  -28.617 36.777  1.00 64.19  ? 242  VAL A CG2 1 
ATOM   1720  N  N   . MET A  1  217 ? 15.227  -27.656 34.401  1.00 63.34  ? 243  MET A N   1 
ATOM   1721  C  CA  . MET A  1  217 ? 14.042  -26.910 33.991  1.00 62.33  ? 243  MET A CA  1 
ATOM   1722  C  C   . MET A  1  217 ? 12.785  -27.767 34.091  1.00 61.37  ? 243  MET A C   1 
ATOM   1723  O  O   . MET A  1  217 ? 11.787  -27.336 34.668  1.00 61.45  ? 243  MET A O   1 
ATOM   1724  C  CB  . MET A  1  217 ? 14.170  -26.387 32.557  1.00 61.87  ? 243  MET A CB  1 
ATOM   1725  C  CG  . MET A  1  217 ? 12.915  -25.666 32.079  1.00 61.48  ? 243  MET A CG  1 
ATOM   1726  S  SD  . MET A  1  217 ? 13.115  -24.837 30.505  1.00 65.05  ? 243  MET A SD  1 
ATOM   1727  C  CE  . MET A  1  217 ? 12.210  -25.886 29.425  1.00 63.88  ? 243  MET A CE  1 
ATOM   1728  N  N   . LYS A  1  218 ? 12.839  -28.974 33.530  1.00 59.92  ? 244  LYS A N   1 
ATOM   1729  C  CA  . LYS A  1  218 ? 11.701  -29.871 33.546  1.00 58.07  ? 244  LYS A CA  1 
ATOM   1730  C  C   . LYS A  1  218 ? 11.283  -30.196 34.967  1.00 58.88  ? 244  LYS A C   1 
ATOM   1731  O  O   . LYS A  1  218 ? 10.098  -30.337 35.255  1.00 59.35  ? 244  LYS A O   1 
ATOM   1732  C  CB  . LYS A  1  218 ? 12.040  -31.136 32.764  1.00 57.24  ? 244  LYS A CB  1 
ATOM   1733  C  CG  . LYS A  1  218 ? 12.213  -30.876 31.280  1.00 58.04  ? 244  LYS A CG  1 
ATOM   1734  C  CD  . LYS A  1  218 ? 12.777  -32.075 30.530  1.00 59.71  ? 244  LYS A CD  1 
ATOM   1735  C  CE  . LYS A  1  218 ? 11.763  -33.208 30.387  1.00 61.10  ? 244  LYS A CE  1 
ATOM   1736  N  NZ  . LYS A  1  218 ? 12.361  -34.408 29.712  1.00 61.86  ? 244  LYS A NZ  1 
ATOM   1737  N  N   . THR A  1  219 ? 12.256  -30.299 35.861  1.00 60.24  ? 245  THR A N   1 
ATOM   1738  C  CA  . THR A  1  219 ? 11.977  -30.594 37.260  1.00 60.95  ? 245  THR A CA  1 
ATOM   1739  C  C   . THR A  1  219 ? 11.199  -29.466 37.914  1.00 62.44  ? 245  THR A C   1 
ATOM   1740  O  O   . THR A  1  219 ? 10.189  -29.709 38.568  1.00 63.24  ? 245  THR A O   1 
ATOM   1741  C  CB  . THR A  1  219 ? 13.272  -30.812 38.039  1.00 60.29  ? 245  THR A CB  1 
ATOM   1742  O  OG1 . THR A  1  219 ? 13.882  -32.021 37.595  1.00 61.18  ? 245  THR A OG1 1 
ATOM   1743  C  CG2 . THR A  1  219 ? 13.005  -30.907 39.522  1.00 59.26  ? 245  THR A CG2 1 
ATOM   1744  N  N   . CYS A  1  220 ? 11.667  -28.234 37.739  1.00 63.90  ? 246  CYS A N   1 
ATOM   1745  C  CA  . CYS A  1  220 ? 10.995  -27.074 38.322  1.00 65.75  ? 246  CYS A CA  1 
ATOM   1746  C  C   . CYS A  1  220 ? 9.588   -26.885 37.782  1.00 66.13  ? 246  CYS A C   1 
ATOM   1747  O  O   . CYS A  1  220 ? 8.659   -26.628 38.538  1.00 66.32  ? 246  CYS A O   1 
ATOM   1748  C  CB  . CYS A  1  220 ? 11.800  -25.800 38.067  1.00 66.96  ? 246  CYS A CB  1 
ATOM   1749  S  SG  . CYS A  1  220 ? 13.374  -25.724 38.941  1.00 67.77  ? 246  CYS A SG  1 
ATOM   1750  N  N   . ILE A  1  221 ? 9.436   -26.999 36.471  1.00 66.91  ? 247  ILE A N   1 
ATOM   1751  C  CA  . ILE A  1  221 ? 8.131   -26.839 35.855  1.00 68.04  ? 247  ILE A CA  1 
ATOM   1752  C  C   . ILE A  1  221 ? 7.133   -27.849 36.429  1.00 69.42  ? 247  ILE A C   1 
ATOM   1753  O  O   . ILE A  1  221 ? 5.923   -27.650 36.346  1.00 70.34  ? 247  ILE A O   1 
ATOM   1754  C  CB  . ILE A  1  221 ? 8.261   -26.947 34.318  1.00 67.24  ? 247  ILE A CB  1 
ATOM   1755  C  CG1 . ILE A  1  221 ? 8.887   -25.657 33.795  1.00 65.49  ? 247  ILE A CG1 1 
ATOM   1756  C  CG2 . ILE A  1  221 ? 6.922   -27.184 33.660  1.00 65.83  ? 247  ILE A CG2 1 
ATOM   1757  C  CD1 . ILE A  1  221 ? 9.165   -25.674 32.326  1.00 67.26  ? 247  ILE A CD1 1 
ATOM   1758  N  N   . GLN A  1  222 ? 7.640   -28.918 37.040  1.00 70.83  ? 248  GLN A N   1 
ATOM   1759  C  CA  . GLN A  1  222 ? 6.780   -29.933 37.652  1.00 70.98  ? 248  GLN A CA  1 
ATOM   1760  C  C   . GLN A  1  222 ? 6.259   -29.452 38.994  1.00 70.24  ? 248  GLN A C   1 
ATOM   1761  O  O   . GLN A  1  222 ? 5.135   -29.766 39.376  1.00 70.98  ? 248  GLN A O   1 
ATOM   1762  C  CB  . GLN A  1  222 ? 7.538   -31.242 37.855  1.00 71.69  ? 248  GLN A CB  1 
ATOM   1763  C  CG  . GLN A  1  222 ? 7.781   -31.998 36.573  1.00 75.95  ? 248  GLN A CG  1 
ATOM   1764  C  CD  . GLN A  1  222 ? 8.380   -33.358 36.821  1.00 77.22  ? 248  GLN A CD  1 
ATOM   1765  O  OE1 . GLN A  1  222 ? 8.732   -34.083 35.886  1.00 77.36  ? 248  GLN A OE1 1 
ATOM   1766  N  NE2 . GLN A  1  222 ? 8.498   -33.717 38.093  1.00 77.77  ? 248  GLN A NE2 1 
ATOM   1767  N  N   . GLY A  1  223 ? 7.084   -28.697 39.713  1.00 69.36  ? 249  GLY A N   1 
ATOM   1768  C  CA  . GLY A  1  223 ? 6.674   -28.176 41.005  1.00 67.50  ? 249  GLY A CA  1 
ATOM   1769  C  C   . GLY A  1  223 ? 5.674   -27.063 40.792  1.00 66.60  ? 249  GLY A C   1 
ATOM   1770  O  O   . GLY A  1  223 ? 4.927   -26.667 41.700  1.00 66.15  ? 249  GLY A O   1 
ATOM   1771  N  N   . LEU A  1  224 ? 5.668   -26.565 39.559  1.00 65.96  ? 250  LEU A N   1 
ATOM   1772  C  CA  . LEU A  1  224 ? 4.781   -25.492 39.146  1.00 65.24  ? 250  LEU A CA  1 
ATOM   1773  C  C   . LEU A  1  224 ? 3.378   -26.059 38.952  1.00 65.31  ? 250  LEU A C   1 
ATOM   1774  O  O   . LEU A  1  224 ? 2.392   -25.317 38.936  1.00 65.84  ? 250  LEU A O   1 
ATOM   1775  C  CB  . LEU A  1  224 ? 5.302   -24.874 37.840  1.00 62.66  ? 250  LEU A CB  1 
ATOM   1776  C  CG  . LEU A  1  224 ? 5.550   -23.364 37.818  1.00 60.97  ? 250  LEU A CG  1 
ATOM   1777  C  CD1 . LEU A  1  224 ? 6.387   -22.937 39.017  1.00 57.79  ? 250  LEU A CD1 1 
ATOM   1778  C  CD2 . LEU A  1  224 ? 6.238   -23.002 36.514  1.00 59.66  ? 250  LEU A CD2 1 
ATOM   1779  N  N   . ALA A  1  225 ? 3.305   -27.383 38.829  1.00 65.19  ? 251  ALA A N   1 
ATOM   1780  C  CA  . ALA A  1  225 ? 2.043   -28.093 38.625  1.00 64.89  ? 251  ALA A CA  1 
ATOM   1781  C  C   . ALA A  1  225 ? 0.896   -27.617 39.521  1.00 64.58  ? 251  ALA A C   1 
ATOM   1782  O  O   . ALA A  1  225 ? 1.049   -27.479 40.742  1.00 65.68  ? 251  ALA A O   1 
ATOM   1783  C  CB  . ALA A  1  225 ? 2.260   -29.600 38.808  1.00 63.91  ? 251  ALA A CB  1 
ATOM   1784  N  N   . GLY A  1  226 ? -0.252  -27.362 38.895  1.00 63.81  ? 252  GLY A N   1 
ATOM   1785  C  CA  . GLY A  1  226 ? -1.426  -26.923 39.625  1.00 63.26  ? 252  GLY A CA  1 
ATOM   1786  C  C   . GLY A  1  226 ? -1.642  -25.431 39.584  1.00 63.22  ? 252  GLY A C   1 
ATOM   1787  O  O   . GLY A  1  226 ? -2.688  -24.923 40.001  1.00 64.18  ? 252  GLY A O   1 
ATOM   1788  N  N   . LEU A  1  227 ? -0.647  -24.720 39.074  1.00 63.00  ? 253  LEU A N   1 
ATOM   1789  C  CA  . LEU A  1  227 ? -0.718  -23.267 38.974  1.00 62.98  ? 253  LEU A CA  1 
ATOM   1790  C  C   . LEU A  1  227 ? -1.721  -22.796 37.942  1.00 63.56  ? 253  LEU A C   1 
ATOM   1791  O  O   . LEU A  1  227 ? -2.020  -23.510 36.987  1.00 64.37  ? 253  LEU A O   1 
ATOM   1792  C  CB  . LEU A  1  227 ? 0.655   -22.693 38.602  1.00 61.21  ? 253  LEU A CB  1 
ATOM   1793  C  CG  . LEU A  1  227 ? 0.740   -21.218 38.187  1.00 59.80  ? 253  LEU A CG  1 
ATOM   1794  C  CD1 . LEU A  1  227 ? 0.529   -20.312 39.400  1.00 59.40  ? 253  LEU A CD1 1 
ATOM   1795  C  CD2 . LEU A  1  227 ? 2.097   -20.945 37.573  1.00 59.35  ? 253  LEU A CD2 1 
ATOM   1796  N  N   . GLU A  1  228 ? -2.240  -21.590 38.148  1.00 64.14  ? 254  GLU A N   1 
ATOM   1797  C  CA  . GLU A  1  228 ? -3.153  -20.986 37.194  1.00 64.31  ? 254  GLU A CA  1 
ATOM   1798  C  C   . GLU A  1  228 ? -2.568  -19.609 36.894  1.00 62.73  ? 254  GLU A C   1 
ATOM   1799  O  O   . GLU A  1  228 ? -2.559  -18.739 37.768  1.00 61.69  ? 254  GLU A O   1 
ATOM   1800  C  CB  . GLU A  1  228 ? -4.569  -20.829 37.758  1.00 66.54  ? 254  GLU A CB  1 
ATOM   1801  C  CG  . GLU A  1  228 ? -5.629  -20.706 36.635  1.00 71.14  ? 254  GLU A CG  1 
ATOM   1802  C  CD  . GLU A  1  228 ? -7.029  -20.340 37.130  1.00 74.20  ? 254  GLU A CD  1 
ATOM   1803  O  OE1 . GLU A  1  228 ? -7.242  -19.163 37.514  1.00 75.40  ? 254  GLU A OE1 1 
ATOM   1804  O  OE2 . GLU A  1  228 ? -7.921  -21.226 37.125  1.00 75.22  ? 254  GLU A OE2 1 
ATOM   1805  N  N   . VAL A  1  229 ? -2.044  -19.434 35.679  1.00 61.01  ? 255  VAL A N   1 
ATOM   1806  C  CA  . VAL A  1  229 ? -1.468  -18.154 35.253  1.00 59.52  ? 255  VAL A CA  1 
ATOM   1807  C  C   . VAL A  1  229 ? -2.195  -17.623 34.033  1.00 57.39  ? 255  VAL A C   1 
ATOM   1808  O  O   . VAL A  1  229 ? -2.564  -18.389 33.142  1.00 59.17  ? 255  VAL A O   1 
ATOM   1809  C  CB  . VAL A  1  229 ? 0.014   -18.280 34.864  1.00 59.86  ? 255  VAL A CB  1 
ATOM   1810  C  CG1 . VAL A  1  229 ? 0.884   -18.136 36.078  1.00 61.31  ? 255  VAL A CG1 1 
ATOM   1811  C  CG2 . VAL A  1  229 ? 0.257   -19.612 34.193  1.00 59.93  ? 255  VAL A CG2 1 
ATOM   1812  N  N   . HIS A  1  230 ? -2.404  -16.317 33.977  1.00 53.84  ? 256  HIS A N   1 
ATOM   1813  C  CA  . HIS A  1  230 ? -3.082  -15.772 32.821  1.00 52.09  ? 256  HIS A CA  1 
ATOM   1814  C  C   . HIS A  1  230 ? -2.097  -15.758 31.661  1.00 50.22  ? 256  HIS A C   1 
ATOM   1815  O  O   . HIS A  1  230 ? -2.405  -16.213 30.564  1.00 51.00  ? 256  HIS A O   1 
ATOM   1816  C  CB  . HIS A  1  230 ? -3.591  -14.357 33.101  1.00 53.33  ? 256  HIS A CB  1 
ATOM   1817  C  CG  . HIS A  1  230 ? -4.175  -13.684 31.901  1.00 55.95  ? 256  HIS A CG  1 
ATOM   1818  N  ND1 . HIS A  1  230 ? -5.249  -14.203 31.205  1.00 57.46  ? 256  HIS A ND1 1 
ATOM   1819  C  CD2 . HIS A  1  230 ? -3.803  -12.564 31.235  1.00 57.00  ? 256  HIS A CD2 1 
ATOM   1820  C  CE1 . HIS A  1  230 ? -5.505  -13.433 30.160  1.00 57.91  ? 256  HIS A CE1 1 
ATOM   1821  N  NE2 . HIS A  1  230 ? -4.641  -12.431 30.154  1.00 57.05  ? 256  HIS A NE2 1 
ATOM   1822  N  N   . ARG A  1  231 ? -0.901  -15.250 31.923  1.00 48.31  ? 257  ARG A N   1 
ATOM   1823  C  CA  . ARG A  1  231 ? 0.150   -15.156 30.916  1.00 46.49  ? 257  ARG A CA  1 
ATOM   1824  C  C   . ARG A  1  231 ? 1.426   -15.751 31.516  1.00 46.15  ? 257  ARG A C   1 
ATOM   1825  O  O   . ARG A  1  231 ? 1.829   -15.349 32.619  1.00 46.40  ? 257  ARG A O   1 
ATOM   1826  C  CB  . ARG A  1  231 ? 0.380   -13.679 30.564  1.00 47.10  ? 257  ARG A CB  1 
ATOM   1827  C  CG  . ARG A  1  231 ? 1.298   -13.425 29.378  1.00 47.19  ? 257  ARG A CG  1 
ATOM   1828  C  CD  . ARG A  1  231 ? 1.606   -11.930 29.182  1.00 46.92  ? 257  ARG A CD  1 
ATOM   1829  N  NE  . ARG A  1  231 ? 2.500   -11.710 28.042  1.00 44.82  ? 257  ARG A NE  1 
ATOM   1830  C  CZ  . ARG A  1  231 ? 2.224   -12.117 26.803  1.00 44.75  ? 257  ARG A CZ  1 
ATOM   1831  N  NH1 . ARG A  1  231 ? 1.080   -12.756 26.554  1.00 41.96  ? 257  ARG A NH1 1 
ATOM   1832  N  NH2 . ARG A  1  231 ? 3.093   -11.910 25.815  1.00 43.37  ? 257  ARG A NH2 1 
ATOM   1833  N  N   . LEU A  1  232 ? 2.050   -16.704 30.814  1.00 43.97  ? 258  LEU A N   1 
ATOM   1834  C  CA  . LEU A  1  232 ? 3.289   -17.332 31.291  1.00 43.15  ? 258  LEU A CA  1 
ATOM   1835  C  C   . LEU A  1  232 ? 4.415   -17.083 30.291  1.00 44.97  ? 258  LEU A C   1 
ATOM   1836  O  O   . LEU A  1  232 ? 4.268   -17.379 29.102  1.00 46.95  ? 258  LEU A O   1 
ATOM   1837  C  CB  . LEU A  1  232 ? 3.094   -18.835 31.485  1.00 41.06  ? 258  LEU A CB  1 
ATOM   1838  C  CG  . LEU A  1  232 ? 4.363   -19.673 31.661  1.00 40.67  ? 258  LEU A CG  1 
ATOM   1839  C  CD1 . LEU A  1  232 ? 5.045   -19.287 32.950  1.00 40.77  ? 258  LEU A CD1 1 
ATOM   1840  C  CD2 . LEU A  1  232 ? 4.033   -21.156 31.658  1.00 39.26  ? 258  LEU A CD2 1 
ATOM   1841  N  N   . VAL A  1  233 ? 5.537   -16.537 30.762  1.00 44.86  ? 259  VAL A N   1 
ATOM   1842  C  CA  . VAL A  1  233 ? 6.664   -16.252 29.873  1.00 43.97  ? 259  VAL A CA  1 
ATOM   1843  C  C   . VAL A  1  233 ? 7.946   -16.994 30.241  1.00 44.79  ? 259  VAL A C   1 
ATOM   1844  O  O   . VAL A  1  233 ? 8.496   -16.799 31.321  1.00 44.82  ? 259  VAL A O   1 
ATOM   1845  C  CB  . VAL A  1  233 ? 6.964   -14.763 29.866  1.00 42.28  ? 259  VAL A CB  1 
ATOM   1846  C  CG1 . VAL A  1  233 ? 7.982   -14.446 28.797  1.00 40.35  ? 259  VAL A CG1 1 
ATOM   1847  C  CG2 . VAL A  1  233 ? 5.690   -14.003 29.654  1.00 41.99  ? 259  VAL A CG2 1 
ATOM   1848  N  N   . LEU A  1  234 ? 8.412   -17.846 29.335  1.00 45.46  ? 260  LEU A N   1 
ATOM   1849  C  CA  . LEU A  1  234 ? 9.632   -18.618 29.540  1.00 46.64  ? 260  LEU A CA  1 
ATOM   1850  C  C   . LEU A  1  234 ? 10.689  -18.145 28.542  1.00 49.29  ? 260  LEU A C   1 
ATOM   1851  O  O   . LEU A  1  234 ? 10.447  -17.211 27.768  1.00 51.20  ? 260  LEU A O   1 
ATOM   1852  C  CB  . LEU A  1  234 ? 9.349   -20.104 29.322  1.00 43.78  ? 260  LEU A CB  1 
ATOM   1853  C  CG  . LEU A  1  234 ? 8.266   -20.707 30.213  1.00 43.36  ? 260  LEU A CG  1 
ATOM   1854  C  CD1 . LEU A  1  234 ? 8.270   -22.217 30.032  1.00 43.77  ? 260  LEU A CD1 1 
ATOM   1855  C  CD2 . LEU A  1  234 ? 8.524   -20.367 31.678  1.00 40.71  ? 260  LEU A CD2 1 
ATOM   1856  N  N   . GLY A  1  235 ? 11.852  -18.791 28.541  1.00 49.40  ? 261  GLY A N   1 
ATOM   1857  C  CA  . GLY A  1  235 ? 12.902  -18.398 27.615  1.00 49.04  ? 261  GLY A CA  1 
ATOM   1858  C  C   . GLY A  1  235 ? 14.156  -17.944 28.339  1.00 49.44  ? 261  GLY A C   1 
ATOM   1859  O  O   . GLY A  1  235 ? 14.260  -18.101 29.545  1.00 49.65  ? 261  GLY A O   1 
ATOM   1860  N  N   . GLU A  1  236 ? 15.106  -17.369 27.609  1.00 50.11  ? 262  GLU A N   1 
ATOM   1861  C  CA  . GLU A  1  236 ? 16.356  -16.906 28.192  1.00 50.29  ? 262  GLU A CA  1 
ATOM   1862  C  C   . GLU A  1  236 ? 16.808  -15.568 27.628  1.00 49.57  ? 262  GLU A C   1 
ATOM   1863  O  O   . GLU A  1  236 ? 16.103  -14.950 26.825  1.00 48.23  ? 262  GLU A O   1 
ATOM   1864  C  CB  . GLU A  1  236 ? 17.439  -17.953 27.948  1.00 52.09  ? 262  GLU A CB  1 
ATOM   1865  C  CG  . GLU A  1  236 ? 17.355  -18.587 26.568  1.00 56.50  ? 262  GLU A CG  1 
ATOM   1866  C  CD  . GLU A  1  236 ? 18.112  -19.905 26.510  1.00 61.23  ? 262  GLU A CD  1 
ATOM   1867  O  OE1 . GLU A  1  236 ? 18.319  -20.490 27.603  1.00 62.46  ? 262  GLU A OE1 1 
ATOM   1868  O  OE2 . GLU A  1  236 ? 18.489  -20.366 25.393  1.00 61.57  ? 262  GLU A OE2 1 
ATOM   1869  N  N   . PHE A  1  237 ? 17.986  -15.124 28.067  1.00 49.01  ? 263  PHE A N   1 
ATOM   1870  C  CA  . PHE A  1  237 ? 18.559  -13.871 27.590  1.00 48.38  ? 263  PHE A CA  1 
ATOM   1871  C  C   . PHE A  1  237 ? 19.734  -14.163 26.684  1.00 48.42  ? 263  PHE A C   1 
ATOM   1872  O  O   . PHE A  1  237 ? 20.543  -15.035 26.971  1.00 49.65  ? 263  PHE A O   1 
ATOM   1873  C  CB  . PHE A  1  237 ? 19.001  -12.989 28.750  1.00 48.61  ? 263  PHE A CB  1 
ATOM   1874  C  CG  . PHE A  1  237 ? 17.861  -12.351 29.477  1.00 50.02  ? 263  PHE A CG  1 
ATOM   1875  C  CD1 . PHE A  1  237 ? 17.349  -12.918 30.639  1.00 50.03  ? 263  PHE A CD1 1 
ATOM   1876  C  CD2 . PHE A  1  237 ? 17.258  -11.207 28.960  1.00 50.42  ? 263  PHE A CD2 1 
ATOM   1877  C  CE1 . PHE A  1  237 ? 16.247  -12.355 31.276  1.00 51.74  ? 263  PHE A CE1 1 
ATOM   1878  C  CE2 . PHE A  1  237 ? 16.161  -10.637 29.583  1.00 51.48  ? 263  PHE A CE2 1 
ATOM   1879  C  CZ  . PHE A  1  237 ? 15.647  -11.210 30.747  1.00 51.75  ? 263  PHE A CZ  1 
ATOM   1880  N  N   . ARG A  1  238 ? 19.803  -13.429 25.581  1.00 49.08  ? 264  ARG A N   1 
ATOM   1881  C  CA  . ARG A  1  238 ? 20.841  -13.578 24.566  1.00 49.18  ? 264  ARG A CA  1 
ATOM   1882  C  C   . ARG A  1  238 ? 22.262  -13.381 25.098  1.00 50.78  ? 264  ARG A C   1 
ATOM   1883  O  O   . ARG A  1  238 ? 23.201  -14.016 24.616  1.00 51.49  ? 264  ARG A O   1 
ATOM   1884  C  CB  . ARG A  1  238 ? 20.567  -12.576 23.445  1.00 47.45  ? 264  ARG A CB  1 
ATOM   1885  C  CG  . ARG A  1  238 ? 21.266  -12.831 22.142  1.00 46.91  ? 264  ARG A CG  1 
ATOM   1886  C  CD  . ARG A  1  238 ? 20.630  -11.946 21.117  1.00 50.48  ? 264  ARG A CD  1 
ATOM   1887  N  NE  . ARG A  1  238 ? 21.300  -11.929 19.825  1.00 54.26  ? 264  ARG A NE  1 
ATOM   1888  C  CZ  . ARG A  1  238 ? 20.951  -11.121 18.822  1.00 56.79  ? 264  ARG A CZ  1 
ATOM   1889  N  NH1 . ARG A  1  238 ? 19.937  -10.267 18.970  1.00 57.53  ? 264  ARG A NH1 1 
ATOM   1890  N  NH2 . ARG A  1  238 ? 21.617  -11.155 17.671  1.00 57.41  ? 264  ARG A NH2 1 
ATOM   1891  N  N   . ASN A  1  239 ? 22.413  -12.507 26.093  1.00 51.65  ? 265  ASN A N   1 
ATOM   1892  C  CA  . ASN A  1  239 ? 23.716  -12.197 26.665  1.00 50.81  ? 265  ASN A CA  1 
ATOM   1893  C  C   . ASN A  1  239 ? 24.008  -12.879 27.988  1.00 51.40  ? 265  ASN A C   1 
ATOM   1894  O  O   . ASN A  1  239 ? 24.773  -12.349 28.792  1.00 51.55  ? 265  ASN A O   1 
ATOM   1895  C  CB  . ASN A  1  239 ? 23.866  -10.678 26.818  1.00 51.19  ? 265  ASN A CB  1 
ATOM   1896  C  CG  . ASN A  1  239 ? 22.873  -10.066 27.814  1.00 52.94  ? 265  ASN A CG  1 
ATOM   1897  O  OD1 . ASN A  1  239 ? 21.720  -10.483 27.919  1.00 53.08  ? 265  ASN A OD1 1 
ATOM   1898  N  ND2 . ASN A  1  239 ? 23.324  -9.043  28.529  1.00 53.93  ? 265  ASN A ND2 1 
ATOM   1899  N  N   . GLU A  1  240 ? 23.404  -14.049 28.204  1.00 52.14  ? 266  GLU A N   1 
ATOM   1900  C  CA  . GLU A  1  240 ? 23.617  -14.825 29.427  1.00 52.61  ? 266  GLU A CA  1 
ATOM   1901  C  C   . GLU A  1  240 ? 23.663  -16.334 29.161  1.00 51.82  ? 266  GLU A C   1 
ATOM   1902  O  O   . GLU A  1  240 ? 23.564  -16.764 28.018  1.00 51.83  ? 266  GLU A O   1 
ATOM   1903  C  CB  . GLU A  1  240 ? 22.535  -14.508 30.451  1.00 53.40  ? 266  GLU A CB  1 
ATOM   1904  C  CG  . GLU A  1  240 ? 23.097  -13.839 31.700  1.00 57.95  ? 266  GLU A CG  1 
ATOM   1905  C  CD  . GLU A  1  240 ? 22.598  -12.413 31.868  1.00 60.24  ? 266  GLU A CD  1 
ATOM   1906  O  OE1 . GLU A  1  240 ? 22.248  -11.789 30.838  1.00 60.90  ? 266  GLU A OE1 1 
ATOM   1907  O  OE2 . GLU A  1  240 ? 22.565  -11.915 33.019  1.00 60.10  ? 266  GLU A OE2 1 
ATOM   1908  N  N   . GLY A  1  241 ? 23.821  -17.129 30.217  1.00 51.87  ? 267  GLY A N   1 
ATOM   1909  C  CA  . GLY A  1  241 ? 23.892  -18.579 30.072  1.00 53.63  ? 267  GLY A CA  1 
ATOM   1910  C  C   . GLY A  1  241 ? 22.644  -19.268 29.548  1.00 55.21  ? 267  GLY A C   1 
ATOM   1911  O  O   . GLY A  1  241 ? 21.593  -19.250 30.192  1.00 56.44  ? 267  GLY A O   1 
ATOM   1912  N  N   . ASN A  1  242 ? 22.775  -19.924 28.400  1.00 55.92  ? 268  ASN A N   1 
ATOM   1913  C  CA  . ASN A  1  242 ? 21.646  -20.581 27.757  1.00 57.54  ? 268  ASN A CA  1 
ATOM   1914  C  C   . ASN A  1  242 ? 21.620  -22.108 27.910  1.00 59.41  ? 268  ASN A C   1 
ATOM   1915  O  O   . ASN A  1  242 ? 22.630  -22.723 28.247  1.00 60.40  ? 268  ASN A O   1 
ATOM   1916  C  CB  . ASN A  1  242 ? 21.659  -20.208 26.268  1.00 58.61  ? 268  ASN A CB  1 
ATOM   1917  C  CG  . ASN A  1  242 ? 21.687  -18.684 26.031  1.00 60.25  ? 268  ASN A CG  1 
ATOM   1918  O  OD1 . ASN A  1  242 ? 22.129  -18.212 24.970  1.00 58.63  ? 268  ASN A OD1 1 
ATOM   1919  N  ND2 . ASN A  1  242 ? 21.199  -17.916 27.010  1.00 59.31  ? 268  ASN A ND2 1 
ATOM   1920  N  N   . LEU A  1  243 ? 20.463  -22.720 27.657  1.00 59.83  ? 269  LEU A N   1 
ATOM   1921  C  CA  . LEU A  1  243 ? 20.313  -24.175 27.744  1.00 59.82  ? 269  LEU A CA  1 
ATOM   1922  C  C   . LEU A  1  243 ? 20.986  -24.783 26.527  1.00 61.74  ? 269  LEU A C   1 
ATOM   1923  O  O   . LEU A  1  243 ? 20.883  -24.237 25.434  1.00 61.83  ? 269  LEU A O   1 
ATOM   1924  C  CB  . LEU A  1  243 ? 18.837  -24.562 27.706  1.00 58.66  ? 269  LEU A CB  1 
ATOM   1925  C  CG  . LEU A  1  243 ? 17.902  -24.028 28.784  1.00 58.12  ? 269  LEU A CG  1 
ATOM   1926  C  CD1 . LEU A  1  243 ? 16.465  -24.394 28.445  1.00 57.63  ? 269  LEU A CD1 1 
ATOM   1927  C  CD2 . LEU A  1  243 ? 18.305  -24.597 30.128  1.00 58.57  ? 269  LEU A CD2 1 
ATOM   1928  N  N   . GLU A  1  244 ? 21.655  -25.916 26.689  1.00 64.48  ? 270  GLU A N   1 
ATOM   1929  C  CA  . GLU A  1  244 ? 22.308  -26.513 25.538  1.00 67.74  ? 270  GLU A CA  1 
ATOM   1930  C  C   . GLU A  1  244 ? 21.366  -27.366 24.702  1.00 68.31  ? 270  GLU A C   1 
ATOM   1931  O  O   . GLU A  1  244 ? 21.693  -27.713 23.570  1.00 69.40  ? 270  GLU A O   1 
ATOM   1932  C  CB  . GLU A  1  244 ? 23.531  -27.338 25.951  1.00 71.32  ? 270  GLU A CB  1 
ATOM   1933  C  CG  . GLU A  1  244 ? 23.235  -28.686 26.594  1.00 76.90  ? 270  GLU A CG  1 
ATOM   1934  C  CD  . GLU A  1  244 ? 24.492  -29.549 26.743  1.00 79.13  ? 270  GLU A CD  1 
ATOM   1935  O  OE1 . GLU A  1  244 ? 25.424  -29.123 27.471  1.00 79.78  ? 270  GLU A OE1 1 
ATOM   1936  O  OE2 . GLU A  1  244 ? 24.542  -30.646 26.126  1.00 79.31  ? 270  GLU A OE2 1 
ATOM   1937  N  N   . LYS A  1  245 ? 20.201  -27.709 25.245  1.00 68.56  ? 271  LYS A N   1 
ATOM   1938  C  CA  . LYS A  1  245 ? 19.232  -28.492 24.481  1.00 68.44  ? 271  LYS A CA  1 
ATOM   1939  C  C   . LYS A  1  245 ? 17.810  -28.119 24.860  1.00 68.55  ? 271  LYS A C   1 
ATOM   1940  O  O   . LYS A  1  245 ? 17.529  -27.709 25.992  1.00 67.74  ? 271  LYS A O   1 
ATOM   1941  C  CB  . LYS A  1  245 ? 19.450  -30.007 24.659  1.00 69.22  ? 271  LYS A CB  1 
ATOM   1942  C  CG  . LYS A  1  245 ? 19.207  -30.568 26.066  1.00 69.65  ? 271  LYS A CG  1 
ATOM   1943  C  CD  . LYS A  1  245 ? 20.509  -30.934 26.790  1.00 68.96  ? 271  LYS A CD  1 
ATOM   1944  C  CE  . LYS A  1  245 ? 21.296  -32.030 26.059  1.00 68.29  ? 271  LYS A CE  1 
ATOM   1945  N  NZ  . LYS A  1  245 ? 20.511  -33.279 25.834  1.00 66.72  ? 271  LYS A NZ  1 
ATOM   1946  N  N   . PHE A  1  246 ? 16.912  -28.254 23.893  1.00 68.44  ? 272  PHE A N   1 
ATOM   1947  C  CA  . PHE A  1  246 ? 15.513  -27.918 24.106  1.00 68.78  ? 272  PHE A CA  1 
ATOM   1948  C  C   . PHE A  1  246 ? 14.696  -28.816 23.190  1.00 69.55  ? 272  PHE A C   1 
ATOM   1949  O  O   . PHE A  1  246 ? 14.140  -28.348 22.195  1.00 70.77  ? 272  PHE A O   1 
ATOM   1950  C  CB  . PHE A  1  246 ? 15.295  -26.442 23.753  1.00 67.20  ? 272  PHE A CB  1 
ATOM   1951  C  CG  . PHE A  1  246 ? 14.097  -25.825 24.401  1.00 66.70  ? 272  PHE A CG  1 
ATOM   1952  C  CD1 . PHE A  1  246 ? 12.837  -25.942 23.823  1.00 66.48  ? 272  PHE A CD1 1 
ATOM   1953  C  CD2 . PHE A  1  246 ? 14.224  -25.144 25.610  1.00 66.02  ? 272  PHE A CD2 1 
ATOM   1954  C  CE1 . PHE A  1  246 ? 11.723  -25.386 24.450  1.00 67.12  ? 272  PHE A CE1 1 
ATOM   1955  C  CE2 . PHE A  1  246 ? 13.116  -24.586 26.245  1.00 64.41  ? 272  PHE A CE2 1 
ATOM   1956  C  CZ  . PHE A  1  246 ? 11.864  -24.704 25.671  1.00 65.44  ? 272  PHE A CZ  1 
ATOM   1957  N  N   . ASP A  1  247 ? 14.639  -30.105 23.528  1.00 70.49  ? 273  ASP A N   1 
ATOM   1958  C  CA  . ASP A  1  247 ? 13.909  -31.096 22.735  1.00 71.26  ? 273  ASP A CA  1 
ATOM   1959  C  C   . ASP A  1  247 ? 12.419  -31.178 23.043  1.00 70.94  ? 273  ASP A C   1 
ATOM   1960  O  O   . ASP A  1  247 ? 11.924  -30.532 23.961  1.00 70.44  ? 273  ASP A O   1 
ATOM   1961  C  CB  . ASP A  1  247 ? 14.532  -32.487 22.899  1.00 73.97  ? 273  ASP A CB  1 
ATOM   1962  C  CG  . ASP A  1  247 ? 14.571  -32.955 24.351  1.00 76.12  ? 273  ASP A CG  1 
ATOM   1963  O  OD1 . ASP A  1  247 ? 13.563  -32.757 25.073  1.00 77.27  ? 273  ASP A OD1 1 
ATOM   1964  O  OD2 . ASP A  1  247 ? 15.608  -33.533 24.759  1.00 75.36  ? 273  ASP A OD2 1 
ATOM   1965  N  N   . LYS A  1  248 ? 11.716  -32.005 22.276  1.00 70.50  ? 274  LYS A N   1 
ATOM   1966  C  CA  . LYS A  1  248 ? 10.274  -32.145 22.414  1.00 70.74  ? 274  LYS A CA  1 
ATOM   1967  C  C   . LYS A  1  248 ? 9.703   -32.435 23.796  1.00 69.94  ? 274  LYS A C   1 
ATOM   1968  O  O   . LYS A  1  248 ? 8.487   -32.542 23.941  1.00 70.35  ? 274  LYS A O   1 
ATOM   1969  C  CB  . LYS A  1  248 ? 9.749   -33.192 21.422  1.00 72.06  ? 274  LYS A CB  1 
ATOM   1970  C  CG  . LYS A  1  248 ? 10.159  -34.635 21.704  1.00 75.02  ? 274  LYS A CG  1 
ATOM   1971  C  CD  . LYS A  1  248 ? 9.649   -35.579 20.600  1.00 77.46  ? 274  LYS A CD  1 
ATOM   1972  C  CE  . LYS A  1  248 ? 10.306  -35.270 19.240  1.00 79.50  ? 274  LYS A CE  1 
ATOM   1973  N  NZ  . LYS A  1  248 ? 9.748   -36.056 18.094  1.00 76.84  ? 274  LYS A NZ  1 
ATOM   1974  N  N   . SER A  1  249 ? 10.543  -32.554 24.814  1.00 68.29  ? 275  SER A N   1 
ATOM   1975  C  CA  . SER A  1  249 ? 10.018  -32.834 26.144  1.00 67.99  ? 275  SER A CA  1 
ATOM   1976  C  C   . SER A  1  249 ? 10.183  -31.665 27.119  1.00 68.03  ? 275  SER A C   1 
ATOM   1977  O  O   . SER A  1  249 ? 9.593   -31.652 28.198  1.00 69.35  ? 275  SER A O   1 
ATOM   1978  C  CB  . SER A  1  249 ? 10.707  -34.061 26.726  1.00 67.16  ? 275  SER A CB  1 
ATOM   1979  O  OG  . SER A  1  249 ? 12.036  -33.730 27.089  1.00 68.52  ? 275  SER A OG  1 
ATOM   1980  N  N   . ALA A  1  250 ? 10.987  -30.682 26.740  1.00 67.33  ? 276  ALA A N   1 
ATOM   1981  C  CA  . ALA A  1  250 ? 11.252  -29.535 27.601  1.00 64.66  ? 276  ALA A CA  1 
ATOM   1982  C  C   . ALA A  1  250 ? 10.006  -28.935 28.229  1.00 63.42  ? 276  ALA A C   1 
ATOM   1983  O  O   . ALA A  1  250 ? 10.026  -28.502 29.380  1.00 62.15  ? 276  ALA A O   1 
ATOM   1984  C  CB  . ALA A  1  250 ? 11.996  -28.467 26.813  1.00 63.98  ? 276  ALA A CB  1 
ATOM   1985  N  N   . LEU A  1  251 ? 8.911   -28.937 27.481  1.00 62.86  ? 277  LEU A N   1 
ATOM   1986  C  CA  . LEU A  1  251 ? 7.684   -28.333 27.968  1.00 63.61  ? 277  LEU A CA  1 
ATOM   1987  C  C   . LEU A  1  251 ? 6.568   -29.268 28.436  1.00 64.90  ? 277  LEU A C   1 
ATOM   1988  O  O   . LEU A  1  251 ? 5.432   -28.821 28.611  1.00 66.45  ? 277  LEU A O   1 
ATOM   1989  C  CB  . LEU A  1  251 ? 7.144   -27.379 26.891  1.00 61.13  ? 277  LEU A CB  1 
ATOM   1990  C  CG  . LEU A  1  251 ? 7.481   -25.880 26.936  1.00 59.47  ? 277  LEU A CG  1 
ATOM   1991  C  CD1 . LEU A  1  251 ? 8.901   -25.621 27.395  1.00 57.48  ? 277  LEU A CD1 1 
ATOM   1992  C  CD2 . LEU A  1  251 ? 7.255   -25.308 25.560  1.00 57.72  ? 277  LEU A CD2 1 
ATOM   1993  N  N   . GLU A  1  252 ? 6.878   -30.544 28.658  1.00 65.39  ? 278  GLU A N   1 
ATOM   1994  C  CA  . GLU A  1  252 ? 5.875   -31.519 29.109  1.00 65.41  ? 278  GLU A CA  1 
ATOM   1995  C  C   . GLU A  1  252 ? 5.037   -31.009 30.270  1.00 65.09  ? 278  GLU A C   1 
ATOM   1996  O  O   . GLU A  1  252 ? 3.813   -31.041 30.223  1.00 65.46  ? 278  GLU A O   1 
ATOM   1997  C  CB  . GLU A  1  252 ? 6.534   -32.804 29.588  1.00 67.11  ? 278  GLU A CB  1 
ATOM   1998  C  CG  . GLU A  1  252 ? 7.112   -33.718 28.541  1.00 70.99  ? 278  GLU A CG  1 
ATOM   1999  C  CD  . GLU A  1  252 ? 8.110   -34.716 29.147  1.00 73.88  ? 278  GLU A CD  1 
ATOM   2000  O  OE1 . GLU A  1  252 ? 8.555   -35.639 28.418  1.00 75.12  ? 278  GLU A OE1 1 
ATOM   2001  O  OE2 . GLU A  1  252 ? 8.451   -34.566 30.352  1.00 72.27  ? 278  GLU A OE2 1 
ATOM   2002  N  N   . GLY A  1  253 ? 5.713   -30.562 31.321  1.00 64.50  ? 279  GLY A N   1 
ATOM   2003  C  CA  . GLY A  1  253 ? 5.034   -30.084 32.512  1.00 64.43  ? 279  GLY A CA  1 
ATOM   2004  C  C   . GLY A  1  253 ? 3.896   -29.086 32.377  1.00 65.15  ? 279  GLY A C   1 
ATOM   2005  O  O   . GLY A  1  253 ? 2.966   -29.113 33.183  1.00 64.05  ? 279  GLY A O   1 
ATOM   2006  N  N   . LEU A  1  254 ? 3.966   -28.206 31.378  1.00 66.25  ? 280  LEU A N   1 
ATOM   2007  C  CA  . LEU A  1  254 ? 2.943   -27.183 31.160  1.00 66.67  ? 280  LEU A CA  1 
ATOM   2008  C  C   . LEU A  1  254 ? 1.543   -27.750 30.984  1.00 67.39  ? 280  LEU A C   1 
ATOM   2009  O  O   . LEU A  1  254 ? 0.544   -27.010 31.035  1.00 66.94  ? 280  LEU A O   1 
ATOM   2010  C  CB  . LEU A  1  254 ? 3.317   -26.336 29.948  1.00 66.64  ? 280  LEU A CB  1 
ATOM   2011  C  CG  . LEU A  1  254 ? 4.204   -25.111 30.183  1.00 66.71  ? 280  LEU A CG  1 
ATOM   2012  C  CD1 . LEU A  1  254 ? 5.225   -25.391 31.248  1.00 66.95  ? 280  LEU A CD1 1 
ATOM   2013  C  CD2 . LEU A  1  254 ? 4.873   -24.716 28.869  1.00 66.82  ? 280  LEU A CD2 1 
ATOM   2014  N  N   . CYS A  1  255 ? 1.480   -29.064 30.777  1.00 67.21  ? 281  CYS A N   1 
ATOM   2015  C  CA  . CYS A  1  255 ? 0.220   -29.766 30.593  1.00 67.35  ? 281  CYS A CA  1 
ATOM   2016  C  C   . CYS A  1  255 ? -0.580  -29.829 31.893  1.00 66.53  ? 281  CYS A C   1 
ATOM   2017  O  O   . CYS A  1  255 ? -1.803  -29.943 31.877  1.00 66.88  ? 281  CYS A O   1 
ATOM   2018  C  CB  . CYS A  1  255 ? 0.496   -31.167 30.054  1.00 69.45  ? 281  CYS A CB  1 
ATOM   2019  S  SG  . CYS A  1  255 ? 0.308   -31.334 28.239  1.00 78.28  ? 281  CYS A SG  1 
ATOM   2020  N  N   . ASN A  1  256 ? 0.125   -29.738 33.019  1.00 66.00  ? 282  ASN A N   1 
ATOM   2021  C  CA  . ASN A  1  256 ? -0.486  -29.755 34.346  1.00 63.83  ? 282  ASN A CA  1 
ATOM   2022  C  C   . ASN A  1  256 ? -0.584  -28.360 34.929  1.00 62.15  ? 282  ASN A C   1 
ATOM   2023  O  O   . ASN A  1  256 ? -0.481  -28.186 36.132  1.00 61.58  ? 282  ASN A O   1 
ATOM   2024  C  CB  . ASN A  1  256 ? 0.329   -30.626 35.296  1.00 64.41  ? 282  ASN A CB  1 
ATOM   2025  C  CG  . ASN A  1  256 ? 0.108   -32.103 35.063  1.00 66.08  ? 282  ASN A CG  1 
ATOM   2026  O  OD1 . ASN A  1  256 ? 0.717   -32.945 35.726  1.00 67.93  ? 282  ASN A OD1 1 
ATOM   2027  N  ND2 . ASN A  1  256 ? -0.772  -32.432 34.119  1.00 66.36  ? 282  ASN A ND2 1 
ATOM   2028  N  N   . LEU A  1  257 ? -0.762  -27.372 34.063  1.00 62.19  ? 283  LEU A N   1 
ATOM   2029  C  CA  . LEU A  1  257 ? -0.884  -25.968 34.449  1.00 62.51  ? 283  LEU A CA  1 
ATOM   2030  C  C   . LEU A  1  257 ? -2.090  -25.434 33.680  1.00 63.53  ? 283  LEU A C   1 
ATOM   2031  O  O   . LEU A  1  257 ? -2.543  -26.039 32.711  1.00 65.78  ? 283  LEU A O   1 
ATOM   2032  C  CB  . LEU A  1  257 ? 0.347   -25.166 33.996  1.00 63.40  ? 283  LEU A CB  1 
ATOM   2033  C  CG  . LEU A  1  257 ? 1.760   -25.180 34.596  1.00 63.14  ? 283  LEU A CG  1 
ATOM   2034  C  CD1 . LEU A  1  257 ? 1.863   -24.128 35.664  1.00 61.91  ? 283  LEU A CD1 1 
ATOM   2035  C  CD2 . LEU A  1  257 ? 2.111   -26.560 35.127  1.00 63.09  ? 283  LEU A CD2 1 
ATOM   2036  N  N   . THR A  1  258 ? -2.610  -24.294 34.094  1.00 62.76  ? 284  THR A N   1 
ATOM   2037  C  CA  . THR A  1  258 ? -3.723  -23.699 33.382  1.00 61.65  ? 284  THR A CA  1 
ATOM   2038  C  C   . THR A  1  258 ? -3.207  -22.357 32.871  1.00 60.32  ? 284  THR A C   1 
ATOM   2039  O  O   . THR A  1  258 ? -3.095  -21.382 33.626  1.00 59.97  ? 284  THR A O   1 
ATOM   2040  C  CB  . THR A  1  258 ? -4.932  -23.509 34.317  1.00 64.21  ? 284  THR A CB  1 
ATOM   2041  O  OG1 . THR A  1  258 ? -5.339  -24.793 34.802  1.00 65.34  ? 284  THR A OG1 1 
ATOM   2042  C  CG2 . THR A  1  258 ? -6.108  -22.854 33.589  1.00 64.79  ? 284  THR A CG2 1 
ATOM   2043  N  N   . ILE A  1  259 ? -2.876  -22.328 31.585  1.00 58.04  ? 285  ILE A N   1 
ATOM   2044  C  CA  . ILE A  1  259 ? -2.336  -21.131 30.941  1.00 56.08  ? 285  ILE A CA  1 
ATOM   2045  C  C   . ILE A  1  259 ? -3.308  -20.529 29.933  1.00 55.06  ? 285  ILE A C   1 
ATOM   2046  O  O   . ILE A  1  259 ? -3.969  -21.253 29.186  1.00 55.77  ? 285  ILE A O   1 
ATOM   2047  C  CB  . ILE A  1  259 ? -1.036  -21.483 30.213  1.00 54.84  ? 285  ILE A CB  1 
ATOM   2048  C  CG1 . ILE A  1  259 ? -0.065  -22.126 31.194  1.00 54.07  ? 285  ILE A CG1 1 
ATOM   2049  C  CG2 . ILE A  1  259 ? -0.447  -20.264 29.580  1.00 52.28  ? 285  ILE A CG2 1 
ATOM   2050  C  CD1 . ILE A  1  259 ? 0.991   -22.933 30.537  1.00 55.38  ? 285  ILE A CD1 1 
ATOM   2051  N  N   . GLU A  1  260 ? -3.397  -19.206 29.912  1.00 53.48  ? 286  GLU A N   1 
ATOM   2052  C  CA  . GLU A  1  260 ? -4.294  -18.536 28.977  1.00 52.95  ? 286  GLU A CA  1 
ATOM   2053  C  C   . GLU A  1  260 ? -3.514  -17.979 27.801  1.00 51.72  ? 286  GLU A C   1 
ATOM   2054  O  O   . GLU A  1  260 ? -3.933  -18.099 26.649  1.00 51.74  ? 286  GLU A O   1 
ATOM   2055  C  CB  . GLU A  1  260 ? -5.059  -17.406 29.660  1.00 53.60  ? 286  GLU A CB  1 
ATOM   2056  C  CG  . GLU A  1  260 ? -6.105  -16.767 28.759  1.00 55.53  ? 286  GLU A CG  1 
ATOM   2057  C  CD  . GLU A  1  260 ? -7.146  -17.763 28.261  1.00 57.23  ? 286  GLU A CD  1 
ATOM   2058  O  OE1 . GLU A  1  260 ? -7.857  -17.449 27.273  1.00 58.46  ? 286  GLU A OE1 1 
ATOM   2059  O  OE2 . GLU A  1  260 ? -7.266  -18.856 28.861  1.00 56.12  ? 286  GLU A OE2 1 
ATOM   2060  N  N   . GLU A  1  261 ? -2.375  -17.364 28.101  1.00 50.15  ? 287  GLU A N   1 
ATOM   2061  C  CA  . GLU A  1  261 ? -1.514  -16.807 27.076  1.00 48.17  ? 287  GLU A CA  1 
ATOM   2062  C  C   . GLU A  1  261 ? -0.091  -17.245 27.369  1.00 45.28  ? 287  GLU A C   1 
ATOM   2063  O  O   . GLU A  1  261 ? 0.377   -17.123 28.498  1.00 43.91  ? 287  GLU A O   1 
ATOM   2064  C  CB  . GLU A  1  261 ? -1.577  -15.285 27.095  1.00 52.13  ? 287  GLU A CB  1 
ATOM   2065  C  CG  . GLU A  1  261 ? -2.958  -14.689 27.275  1.00 56.32  ? 287  GLU A CG  1 
ATOM   2066  C  CD  . GLU A  1  261 ? -2.919  -13.164 27.299  1.00 59.91  ? 287  GLU A CD  1 
ATOM   2067  O  OE1 . GLU A  1  261 ? -1.920  -12.599 27.821  1.00 61.22  ? 287  GLU A OE1 1 
ATOM   2068  O  OE2 . GLU A  1  261 ? -3.885  -12.533 26.805  1.00 60.91  ? 287  GLU A OE2 1 
ATOM   2069  N  N   . PHE A  1  262 ? 0.598   -17.723 26.338  1.00 42.56  ? 288  PHE A N   1 
ATOM   2070  C  CA  . PHE A  1  262 ? 1.972   -18.187 26.465  1.00 41.67  ? 288  PHE A CA  1 
ATOM   2071  C  C   . PHE A  1  262 ? 2.939   -17.416 25.565  1.00 42.24  ? 288  PHE A C   1 
ATOM   2072  O  O   . PHE A  1  262 ? 2.549   -16.929 24.499  1.00 43.62  ? 288  PHE A O   1 
ATOM   2073  C  CB  . PHE A  1  262 ? 2.039   -19.671 26.096  1.00 39.86  ? 288  PHE A CB  1 
ATOM   2074  C  CG  . PHE A  1  262 ? 3.422   -20.247 26.128  1.00 38.25  ? 288  PHE A CG  1 
ATOM   2075  C  CD1 . PHE A  1  262 ? 4.043   -20.532 27.341  1.00 38.69  ? 288  PHE A CD1 1 
ATOM   2076  C  CD2 . PHE A  1  262 ? 4.117   -20.477 24.944  1.00 36.73  ? 288  PHE A CD2 1 
ATOM   2077  C  CE1 . PHE A  1  262 ? 5.344   -21.039 27.370  1.00 38.23  ? 288  PHE A CE1 1 
ATOM   2078  C  CE2 . PHE A  1  262 ? 5.420   -20.983 24.957  1.00 35.77  ? 288  PHE A CE2 1 
ATOM   2079  C  CZ  . PHE A  1  262 ? 6.034   -21.263 26.167  1.00 36.88  ? 288  PHE A CZ  1 
ATOM   2080  N  N   . ARG A  1  263 ? 4.191   -17.292 26.012  1.00 42.62  ? 289  ARG A N   1 
ATOM   2081  C  CA  . ARG A  1  263 ? 5.250   -16.654 25.226  1.00 42.36  ? 289  ARG A CA  1 
ATOM   2082  C  C   . ARG A  1  263 ? 6.638   -17.195 25.557  1.00 43.25  ? 289  ARG A C   1 
ATOM   2083  O  O   . ARG A  1  263 ? 7.054   -17.206 26.717  1.00 44.02  ? 289  ARG A O   1 
ATOM   2084  C  CB  . ARG A  1  263 ? 5.294   -15.138 25.415  1.00 39.64  ? 289  ARG A CB  1 
ATOM   2085  C  CG  . ARG A  1  263 ? 6.517   -14.560 24.728  1.00 38.92  ? 289  ARG A CG  1 
ATOM   2086  C  CD  . ARG A  1  263 ? 6.683   -13.078 24.915  1.00 41.40  ? 289  ARG A CD  1 
ATOM   2087  N  NE  . ARG A  1  263 ? 5.932   -12.330 23.918  1.00 43.12  ? 289  ARG A NE  1 
ATOM   2088  C  CZ  . ARG A  1  263 ? 5.824   -11.006 23.885  1.00 41.76  ? 289  ARG A CZ  1 
ATOM   2089  N  NH1 . ARG A  1  263 ? 6.419   -10.247 24.801  1.00 37.92  ? 289  ARG A NH1 1 
ATOM   2090  N  NH2 . ARG A  1  263 ? 5.114   -10.445 22.917  1.00 43.17  ? 289  ARG A NH2 1 
ATOM   2091  N  N   . LEU A  1  264 ? 7.341   -17.656 24.533  1.00 42.47  ? 290  LEU A N   1 
ATOM   2092  C  CA  . LEU A  1  264 ? 8.705   -18.125 24.696  1.00 41.85  ? 290  LEU A CA  1 
ATOM   2093  C  C   . LEU A  1  264 ? 9.534   -16.959 24.133  1.00 43.24  ? 290  LEU A C   1 
ATOM   2094  O  O   . LEU A  1  264 ? 9.480   -16.656 22.923  1.00 42.31  ? 290  LEU A O   1 
ATOM   2095  C  CB  . LEU A  1  264 ? 8.935   -19.402 23.882  1.00 40.97  ? 290  LEU A CB  1 
ATOM   2096  C  CG  . LEU A  1  264 ? 10.372  -19.897 23.809  1.00 39.29  ? 290  LEU A CG  1 
ATOM   2097  C  CD1 . LEU A  1  264 ? 10.868  -20.159 25.232  1.00 38.68  ? 290  LEU A CD1 1 
ATOM   2098  C  CD2 . LEU A  1  264 ? 10.440  -21.146 22.954  1.00 38.64  ? 290  LEU A CD2 1 
ATOM   2099  N  N   . ALA A  1  265 ? 10.271  -16.288 25.018  1.00 44.17  ? 291  ALA A N   1 
ATOM   2100  C  CA  . ALA A  1  265 ? 11.101  -15.143 24.636  1.00 44.64  ? 291  ALA A CA  1 
ATOM   2101  C  C   . ALA A  1  265 ? 12.601  -15.363 24.532  1.00 45.61  ? 291  ALA A C   1 
ATOM   2102  O  O   . ALA A  1  265 ? 13.321  -15.195 25.508  1.00 45.27  ? 291  ALA A O   1 
ATOM   2103  C  CB  . ALA A  1  265 ? 10.915  -14.011 25.635  1.00 43.72  ? 291  ALA A CB  1 
ATOM   2104  N  N   . TYR A  1  266 ? 13.052  -15.721 23.331  1.00 48.57  ? 292  TYR A N   1 
ATOM   2105  C  CA  . TYR A  1  266 ? 14.463  -15.980 23.011  1.00 51.23  ? 292  TYR A CA  1 
ATOM   2106  C  C   . TYR A  1  266 ? 15.037  -17.316 23.474  1.00 53.09  ? 292  TYR A C   1 
ATOM   2107  O  O   . TYR A  1  266 ? 15.148  -17.588 24.665  1.00 53.43  ? 292  TYR A O   1 
ATOM   2108  C  CB  . TYR A  1  266 ? 15.450  -14.972 23.618  1.00 51.69  ? 292  TYR A CB  1 
ATOM   2109  C  CG  . TYR A  1  266 ? 16.863  -15.240 23.144  1.00 53.33  ? 292  TYR A CG  1 
ATOM   2110  C  CD1 . TYR A  1  266 ? 17.251  -14.920 21.844  1.00 53.67  ? 292  TYR A CD1 1 
ATOM   2111  C  CD2 . TYR A  1  266 ? 17.780  -15.909 23.955  1.00 53.46  ? 292  TYR A CD2 1 
ATOM   2112  C  CE1 . TYR A  1  266 ? 18.508  -15.263 21.364  1.00 53.88  ? 292  TYR A CE1 1 
ATOM   2113  C  CE2 . TYR A  1  266 ? 19.040  -16.258 23.480  1.00 53.41  ? 292  TYR A CE2 1 
ATOM   2114  C  CZ  . TYR A  1  266 ? 19.397  -15.933 22.185  1.00 53.94  ? 292  TYR A CZ  1 
ATOM   2115  O  OH  . TYR A  1  266 ? 20.648  -16.270 21.711  1.00 54.77  ? 292  TYR A OH  1 
ATOM   2116  N  N   . LEU A  1  267 ? 15.433  -18.137 22.514  1.00 54.22  ? 293  LEU A N   1 
ATOM   2117  C  CA  . LEU A  1  267 ? 15.990  -19.442 22.812  1.00 55.42  ? 293  LEU A CA  1 
ATOM   2118  C  C   . LEU A  1  267 ? 17.145  -19.629 21.838  1.00 57.98  ? 293  LEU A C   1 
ATOM   2119  O  O   . LEU A  1  267 ? 16.943  -19.529 20.622  1.00 59.15  ? 293  LEU A O   1 
ATOM   2120  C  CB  . LEU A  1  267 ? 14.846  -20.420 22.508  1.00 54.97  ? 293  LEU A CB  1 
ATOM   2121  C  CG  . LEU A  1  267 ? 14.700  -21.848 23.063  1.00 53.31  ? 293  LEU A CG  1 
ATOM   2122  C  CD1 . LEU A  1  267 ? 15.331  -22.855 22.126  1.00 51.38  ? 293  LEU A CD1 1 
ATOM   2123  C  CD2 . LEU A  1  267 ? 15.291  -21.920 24.468  1.00 53.05  ? 293  LEU A CD2 1 
ATOM   2124  N  N   . ASP A  1  268 ? 18.342  -19.877 22.378  1.00 60.05  ? 294  ASP A N   1 
ATOM   2125  C  CA  . ASP A  1  268 ? 19.568  -20.074 21.593  1.00 60.70  ? 294  ASP A CA  1 
ATOM   2126  C  C   . ASP A  1  268 ? 19.512  -21.327 20.727  1.00 60.62  ? 294  ASP A C   1 
ATOM   2127  O  O   . ASP A  1  268 ? 19.902  -21.306 19.560  1.00 59.90  ? 294  ASP A O   1 
ATOM   2128  C  CB  . ASP A  1  268 ? 20.768  -20.164 22.541  1.00 63.24  ? 294  ASP A CB  1 
ATOM   2129  C  CG  . ASP A  1  268 ? 22.090  -19.815 21.863  1.00 66.34  ? 294  ASP A CG  1 
ATOM   2130  O  OD1 . ASP A  1  268 ? 22.540  -20.558 20.963  1.00 67.27  ? 294  ASP A OD1 1 
ATOM   2131  O  OD2 . ASP A  1  268 ? 22.687  -18.778 22.240  1.00 69.24  ? 294  ASP A OD2 1 
ATOM   2132  N  N   . TYR A  1  269 ? 19.037  -22.416 21.319  1.00 62.62  ? 295  TYR A N   1 
ATOM   2133  C  CA  . TYR A  1  269 ? 18.909  -23.707 20.643  1.00 65.68  ? 295  TYR A CA  1 
ATOM   2134  C  C   . TYR A  1  269 ? 18.016  -23.584 19.396  1.00 67.27  ? 295  TYR A C   1 
ATOM   2135  O  O   . TYR A  1  269 ? 17.009  -22.874 19.419  1.00 68.32  ? 295  TYR A O   1 
ATOM   2136  C  CB  . TYR A  1  269 ? 18.316  -24.712 21.641  1.00 66.29  ? 295  TYR A CB  1 
ATOM   2137  C  CG  . TYR A  1  269 ? 18.198  -26.148 21.169  1.00 69.40  ? 295  TYR A CG  1 
ATOM   2138  C  CD1 . TYR A  1  269 ? 19.295  -27.014 21.191  1.00 70.33  ? 295  TYR A CD1 1 
ATOM   2139  C  CD2 . TYR A  1  269 ? 16.978  -26.646 20.711  1.00 70.21  ? 295  TYR A CD2 1 
ATOM   2140  C  CE1 . TYR A  1  269 ? 19.174  -28.341 20.768  1.00 71.70  ? 295  TYR A CE1 1 
ATOM   2141  C  CE2 . TYR A  1  269 ? 16.849  -27.960 20.287  1.00 71.82  ? 295  TYR A CE2 1 
ATOM   2142  C  CZ  . TYR A  1  269 ? 17.946  -28.807 20.315  1.00 71.99  ? 295  TYR A CZ  1 
ATOM   2143  O  OH  . TYR A  1  269 ? 17.798  -30.112 19.884  1.00 71.65  ? 295  TYR A OH  1 
ATOM   2144  N  N   . TYR A  1  270 ? 18.378  -24.253 18.304  1.00 68.44  ? 296  TYR A N   1 
ATOM   2145  C  CA  . TYR A  1  270 ? 17.562  -24.196 17.089  1.00 70.58  ? 296  TYR A CA  1 
ATOM   2146  C  C   . TYR A  1  270 ? 16.447  -25.223 17.199  1.00 72.49  ? 296  TYR A C   1 
ATOM   2147  O  O   . TYR A  1  270 ? 16.725  -26.416 17.229  1.00 74.25  ? 296  TYR A O   1 
ATOM   2148  C  CB  . TYR A  1  270 ? 18.409  -24.516 15.858  1.00 71.10  ? 296  TYR A CB  1 
ATOM   2149  C  CG  . TYR A  1  270 ? 19.318  -23.401 15.392  1.00 73.69  ? 296  TYR A CG  1 
ATOM   2150  C  CD1 . TYR A  1  270 ? 19.963  -22.563 16.309  1.00 75.35  ? 296  TYR A CD1 1 
ATOM   2151  C  CD2 . TYR A  1  270 ? 19.605  -23.237 14.032  1.00 74.19  ? 296  TYR A CD2 1 
ATOM   2152  C  CE1 . TYR A  1  270 ? 20.884  -21.591 15.883  1.00 76.93  ? 296  TYR A CE1 1 
ATOM   2153  C  CE2 . TYR A  1  270 ? 20.528  -22.272 13.591  1.00 76.12  ? 296  TYR A CE2 1 
ATOM   2154  C  CZ  . TYR A  1  270 ? 21.170  -21.455 14.522  1.00 76.78  ? 296  TYR A CZ  1 
ATOM   2155  O  OH  . TYR A  1  270 ? 22.130  -20.552 14.102  1.00 74.78  ? 296  TYR A OH  1 
ATOM   2156  N  N   . LEU A  1  271 ? 15.196  -24.773 17.255  1.00 74.27  ? 297  LEU A N   1 
ATOM   2157  C  CA  . LEU A  1  271 ? 14.064  -25.688 17.363  1.00 76.30  ? 297  LEU A CA  1 
ATOM   2158  C  C   . LEU A  1  271 ? 14.043  -26.700 16.226  1.00 80.18  ? 297  LEU A C   1 
ATOM   2159  O  O   . LEU A  1  271 ? 14.372  -26.375 15.079  1.00 80.14  ? 297  LEU A O   1 
ATOM   2160  C  CB  . LEU A  1  271 ? 12.741  -24.929 17.352  1.00 74.06  ? 297  LEU A CB  1 
ATOM   2161  C  CG  . LEU A  1  271 ? 12.414  -24.063 18.560  1.00 73.47  ? 297  LEU A CG  1 
ATOM   2162  C  CD1 . LEU A  1  271 ? 11.004  -23.522 18.409  1.00 73.14  ? 297  LEU A CD1 1 
ATOM   2163  C  CD2 . LEU A  1  271 ? 12.548  -24.877 19.835  1.00 73.63  ? 297  LEU A CD2 1 
ATOM   2164  N  N   . ASP A  1  272 ? 13.631  -27.923 16.563  1.00 83.99  ? 298  ASP A N   1 
ATOM   2165  C  CA  . ASP A  1  272 ? 13.539  -29.036 15.619  1.00 87.32  ? 298  ASP A CA  1 
ATOM   2166  C  C   . ASP A  1  272 ? 12.095  -29.199 15.168  1.00 87.84  ? 298  ASP A C   1 
ATOM   2167  O  O   . ASP A  1  272 ? 11.756  -29.007 14.002  1.00 87.79  ? 298  ASP A O   1 
ATOM   2168  C  CB  . ASP A  1  272 ? 13.997  -30.328 16.302  1.00 89.62  ? 298  ASP A CB  1 
ATOM   2169  C  CG  . ASP A  1  272 ? 15.461  -30.281 16.740  1.00 92.55  ? 298  ASP A CG  1 
ATOM   2170  O  OD1 . ASP A  1  272 ? 15.773  -30.870 17.808  1.00 92.62  ? 298  ASP A OD1 1 
ATOM   2171  O  OD2 . ASP A  1  272 ? 16.291  -29.670 16.013  1.00 94.32  ? 298  ASP A OD2 1 
ATOM   2172  N  N   . ASP A  1  273 ? 11.253  -29.565 16.121  1.00 88.90  ? 299  ASP A N   1 
ATOM   2173  C  CA  . ASP A  1  273 ? 9.836   -29.753 15.875  1.00 90.83  ? 299  ASP A CA  1 
ATOM   2174  C  C   . ASP A  1  273 ? 9.039   -28.646 16.561  1.00 90.51  ? 299  ASP A C   1 
ATOM   2175  O  O   . ASP A  1  273 ? 9.519   -28.017 17.507  1.00 90.98  ? 299  ASP A O   1 
ATOM   2176  C  CB  . ASP A  1  273 ? 9.394   -31.126 16.403  1.00 92.12  ? 299  ASP A CB  1 
ATOM   2177  C  CG  . ASP A  1  273 ? 7.891   -31.208 16.646  1.00 92.90  ? 299  ASP A CG  1 
ATOM   2178  O  OD1 . ASP A  1  273 ? 7.435   -30.670 17.678  1.00 92.30  ? 299  ASP A OD1 1 
ATOM   2179  O  OD2 . ASP A  1  273 ? 7.168   -31.793 15.803  1.00 92.08  ? 299  ASP A OD2 1 
ATOM   2180  N  N   . ILE A  1  274 ? 7.822   -28.412 16.091  1.00 89.05  ? 300  ILE A N   1 
ATOM   2181  C  CA  . ILE A  1  274 ? 7.003   -27.381 16.692  1.00 88.85  ? 300  ILE A CA  1 
ATOM   2182  C  C   . ILE A  1  274 ? 5.702   -27.959 17.259  1.00 88.92  ? 300  ILE A C   1 
ATOM   2183  O  O   . ILE A  1  274 ? 5.147   -27.432 18.231  1.00 88.48  ? 300  ILE A O   1 
ATOM   2184  C  CB  . ILE A  1  274 ? 6.686   -26.283 15.662  1.00 88.25  ? 300  ILE A CB  1 
ATOM   2185  C  CG1 . ILE A  1  274 ? 6.006   -25.103 16.343  1.00 87.91  ? 300  ILE A CG1 1 
ATOM   2186  C  CG2 . ILE A  1  274 ? 5.779   -26.832 14.582  1.00 90.39  ? 300  ILE A CG2 1 
ATOM   2187  C  CD1 . ILE A  1  274 ? 5.604   -24.010 15.377  1.00 88.10  ? 300  ILE A CD1 1 
ATOM   2188  N  N   . ILE A  1  275 ? 5.236   -29.060 16.669  1.00 88.48  ? 301  ILE A N   1 
ATOM   2189  C  CA  . ILE A  1  275 ? 3.981   -29.701 17.091  1.00 87.25  ? 301  ILE A CA  1 
ATOM   2190  C  C   . ILE A  1  275 ? 4.055   -30.579 18.357  1.00 85.59  ? 301  ILE A C   1 
ATOM   2191  O  O   . ILE A  1  275 ? 3.134   -30.554 19.185  1.00 85.94  ? 301  ILE A O   1 
ATOM   2192  C  CB  . ILE A  1  275 ? 3.336   -30.488 15.881  1.00 87.70  ? 301  ILE A CB  1 
ATOM   2193  C  CG1 . ILE A  1  275 ? 2.605   -31.746 16.368  1.00 87.92  ? 301  ILE A CG1 1 
ATOM   2194  C  CG2 . ILE A  1  275 ? 4.395   -30.784 14.820  1.00 87.24  ? 301  ILE A CG2 1 
ATOM   2195  C  CD1 . ILE A  1  275 ? 1.276   -31.482 17.074  1.00 89.32  ? 301  ILE A CD1 1 
ATOM   2196  N  N   . ASP A  1  276 ? 5.139   -31.337 18.517  1.00 83.41  ? 302  ASP A N   1 
ATOM   2197  C  CA  . ASP A  1  276 ? 5.324   -32.194 19.698  1.00 80.50  ? 302  ASP A CA  1 
ATOM   2198  C  C   . ASP A  1  276 ? 5.795   -31.332 20.856  1.00 77.39  ? 302  ASP A C   1 
ATOM   2199  O  O   . ASP A  1  276 ? 5.585   -31.645 22.019  1.00 76.93  ? 302  ASP A O   1 
ATOM   2200  C  CB  . ASP A  1  276 ? 6.401   -33.249 19.437  1.00 82.54  ? 302  ASP A CB  1 
ATOM   2201  C  CG  . ASP A  1  276 ? 5.972   -34.307 18.445  1.00 84.84  ? 302  ASP A CG  1 
ATOM   2202  O  OD1 . ASP A  1  276 ? 6.874   -34.930 17.838  1.00 86.20  ? 302  ASP A OD1 1 
ATOM   2203  O  OD2 . ASP A  1  276 ? 4.750   -34.534 18.286  1.00 86.39  ? 302  ASP A OD2 1 
ATOM   2204  N  N   . LEU A  1  277 ? 6.455   -30.243 20.504  1.00 74.94  ? 303  LEU A N   1 
ATOM   2205  C  CA  . LEU A  1  277 ? 7.015   -29.316 21.461  1.00 71.99  ? 303  LEU A CA  1 
ATOM   2206  C  C   . LEU A  1  277 ? 5.983   -28.476 22.196  1.00 70.64  ? 303  LEU A C   1 
ATOM   2207  O  O   . LEU A  1  277 ? 6.068   -28.312 23.409  1.00 70.99  ? 303  LEU A O   1 
ATOM   2208  C  CB  . LEU A  1  277 ? 7.980   -28.391 20.730  1.00 71.10  ? 303  LEU A CB  1 
ATOM   2209  C  CG  . LEU A  1  277 ? 9.159   -27.778 21.474  1.00 71.71  ? 303  LEU A CG  1 
ATOM   2210  C  CD1 . LEU A  1  277 ? 9.783   -26.747 20.540  1.00 72.32  ? 303  LEU A CD1 1 
ATOM   2211  C  CD2 . LEU A  1  277 ? 8.739   -27.142 22.795  1.00 70.36  ? 303  LEU A CD2 1 
ATOM   2212  N  N   . PHE A  1  278 ? 5.007   -27.949 21.465  1.00 68.41  ? 304  PHE A N   1 
ATOM   2213  C  CA  . PHE A  1  278 ? 4.012   -27.084 22.077  1.00 66.77  ? 304  PHE A CA  1 
ATOM   2214  C  C   . PHE A  1  278 ? 2.608   -27.651 22.251  1.00 67.31  ? 304  PHE A C   1 
ATOM   2215  O  O   . PHE A  1  278 ? 1.672   -26.885 22.460  1.00 67.82  ? 304  PHE A O   1 
ATOM   2216  C  CB  . PHE A  1  278 ? 3.895   -25.775 21.273  1.00 63.85  ? 304  PHE A CB  1 
ATOM   2217  C  CG  . PHE A  1  278 ? 5.196   -25.030 21.084  1.00 58.61  ? 304  PHE A CG  1 
ATOM   2218  C  CD1 . PHE A  1  278 ? 5.599   -24.646 19.805  1.00 56.23  ? 304  PHE A CD1 1 
ATOM   2219  C  CD2 . PHE A  1  278 ? 6.006   -24.707 22.165  1.00 55.55  ? 304  PHE A CD2 1 
ATOM   2220  C  CE1 . PHE A  1  278 ? 6.787   -23.963 19.602  1.00 54.12  ? 304  PHE A CE1 1 
ATOM   2221  C  CE2 . PHE A  1  278 ? 7.195   -24.023 21.970  1.00 54.03  ? 304  PHE A CE2 1 
ATOM   2222  C  CZ  . PHE A  1  278 ? 7.588   -23.649 20.686  1.00 54.23  ? 304  PHE A CZ  1 
ATOM   2223  N  N   . ASN A  1  279 ? 2.427   -28.962 22.181  1.00 68.53  ? 305  ASN A N   1 
ATOM   2224  C  CA  . ASN A  1  279 ? 1.069   -29.486 22.311  1.00 70.11  ? 305  ASN A CA  1 
ATOM   2225  C  C   . ASN A  1  279 ? 0.444   -29.358 23.695  1.00 69.97  ? 305  ASN A C   1 
ATOM   2226  O  O   . ASN A  1  279 ? -0.726  -29.685 23.882  1.00 70.04  ? 305  ASN A O   1 
ATOM   2227  C  CB  . ASN A  1  279 ? 0.986   -30.938 21.844  1.00 72.94  ? 305  ASN A CB  1 
ATOM   2228  C  CG  . ASN A  1  279 ? 1.943   -31.853 22.582  1.00 76.13  ? 305  ASN A CG  1 
ATOM   2229  O  OD1 . ASN A  1  279 ? 2.174   -31.701 23.790  1.00 77.66  ? 305  ASN A OD1 1 
ATOM   2230  N  ND2 . ASN A  1  279 ? 2.488   -32.837 21.862  1.00 76.99  ? 305  ASN A ND2 1 
ATOM   2231  N  N   . CYS A  1  280 ? 1.210   -28.887 24.670  1.00 69.89  ? 306  CYS A N   1 
ATOM   2232  C  CA  . CYS A  1  280 ? 0.650   -28.699 25.999  1.00 69.08  ? 306  CYS A CA  1 
ATOM   2233  C  C   . CYS A  1  280 ? 0.044   -27.304 26.102  1.00 67.96  ? 306  CYS A C   1 
ATOM   2234  O  O   . CYS A  1  280 ? -0.689  -27.000 27.043  1.00 66.73  ? 306  CYS A O   1 
ATOM   2235  C  CB  . CYS A  1  280 ? 1.721   -28.897 27.062  1.00 71.75  ? 306  CYS A CB  1 
ATOM   2236  S  SG  . CYS A  1  280 ? 2.036   -30.661 27.393  1.00 77.01  ? 306  CYS A SG  1 
ATOM   2237  N  N   . LEU A  1  281 ? 0.372   -26.461 25.119  1.00 67.45  ? 307  LEU A N   1 
ATOM   2238  C  CA  . LEU A  1  281 ? -0.141  -25.094 25.040  1.00 64.93  ? 307  LEU A CA  1 
ATOM   2239  C  C   . LEU A  1  281 ? -1.168  -25.059 23.934  1.00 64.64  ? 307  LEU A C   1 
ATOM   2240  O  O   . LEU A  1  281 ? -1.461  -24.003 23.396  1.00 65.61  ? 307  LEU A O   1 
ATOM   2241  C  CB  . LEU A  1  281 ? 0.948   -24.073 24.690  1.00 60.69  ? 307  LEU A CB  1 
ATOM   2242  C  CG  . LEU A  1  281 ? 2.088   -23.678 25.619  1.00 58.18  ? 307  LEU A CG  1 
ATOM   2243  C  CD1 . LEU A  1  281 ? 1.630   -23.672 27.050  1.00 57.36  ? 307  LEU A CD1 1 
ATOM   2244  C  CD2 . LEU A  1  281 ? 3.221   -24.635 25.431  1.00 59.05  ? 307  LEU A CD2 1 
ATOM   2245  N  N   . THR A  1  282 ? -1.713  -26.213 23.578  1.00 64.28  ? 308  THR A N   1 
ATOM   2246  C  CA  . THR A  1  282 ? -2.701  -26.237 22.515  1.00 63.74  ? 308  THR A CA  1 
ATOM   2247  C  C   . THR A  1  282 ? -4.010  -25.499 22.882  1.00 65.11  ? 308  THR A C   1 
ATOM   2248  O  O   . THR A  1  282 ? -4.613  -24.821 22.043  1.00 65.05  ? 308  THR A O   1 
ATOM   2249  C  CB  . THR A  1  282 ? -3.015  -27.679 22.108  1.00 61.12  ? 308  THR A CB  1 
ATOM   2250  O  OG1 . THR A  1  282 ? -3.780  -27.671 20.899  1.00 61.81  ? 308  THR A OG1 1 
ATOM   2251  C  CG2 . THR A  1  282 ? -3.795  -28.379 23.198  1.00 57.76  ? 308  THR A CG2 1 
ATOM   2252  N  N   . ASN A  1  283 ? -4.432  -25.614 24.139  1.00 65.39  ? 309  ASN A N   1 
ATOM   2253  C  CA  . ASN A  1  283 ? -5.668  -24.979 24.592  1.00 64.01  ? 309  ASN A CA  1 
ATOM   2254  C  C   . ASN A  1  283 ? -5.475  -23.472 24.782  1.00 61.39  ? 309  ASN A C   1 
ATOM   2255  O  O   . ASN A  1  283 ? -6.435  -22.711 24.884  1.00 60.95  ? 309  ASN A O   1 
ATOM   2256  C  CB  . ASN A  1  283 ? -6.151  -25.626 25.913  1.00 66.80  ? 309  ASN A CB  1 
ATOM   2257  C  CG  . ASN A  1  283 ? -6.548  -27.114 25.755  1.00 68.16  ? 309  ASN A CG  1 
ATOM   2258  O  OD1 . ASN A  1  283 ? -7.214  -27.486 24.783  1.00 67.27  ? 309  ASN A OD1 1 
ATOM   2259  N  ND2 . ASN A  1  283 ? -6.151  -27.957 26.730  1.00 67.82  ? 309  ASN A ND2 1 
ATOM   2260  N  N   . VAL A  1  284 ? -4.225  -23.044 24.829  1.00 58.55  ? 310  VAL A N   1 
ATOM   2261  C  CA  . VAL A  1  284 ? -3.909  -21.632 25.003  1.00 56.21  ? 310  VAL A CA  1 
ATOM   2262  C  C   . VAL A  1  284 ? -4.638  -20.758 23.980  1.00 54.44  ? 310  VAL A C   1 
ATOM   2263  O  O   . VAL A  1  284 ? -4.849  -21.179 22.852  1.00 54.44  ? 310  VAL A O   1 
ATOM   2264  C  CB  . VAL A  1  284 ? -2.386  -21.441 24.891  1.00 55.67  ? 310  VAL A CB  1 
ATOM   2265  C  CG1 . VAL A  1  284 ? -2.046  -20.189 24.100  1.00 54.45  ? 310  VAL A CG1 1 
ATOM   2266  C  CG2 . VAL A  1  284 ? -1.788  -21.394 26.275  1.00 55.16  ? 310  VAL A CG2 1 
ATOM   2267  N  N   . SER A  1  285 ? -5.030  -19.551 24.366  1.00 52.95  ? 311  SER A N   1 
ATOM   2268  C  CA  . SER A  1  285 ? -5.724  -18.675 23.431  1.00 53.11  ? 311  SER A CA  1 
ATOM   2269  C  C   . SER A  1  285 ? -4.779  -17.713 22.701  1.00 52.85  ? 311  SER A C   1 
ATOM   2270  O  O   . SER A  1  285 ? -5.054  -17.307 21.573  1.00 53.87  ? 311  SER A O   1 
ATOM   2271  C  CB  . SER A  1  285 ? -6.797  -17.873 24.150  1.00 54.09  ? 311  SER A CB  1 
ATOM   2272  O  OG  . SER A  1  285 ? -6.210  -16.827 24.896  1.00 56.80  ? 311  SER A OG  1 
ATOM   2273  N  N   . SER A  1  286 ? -3.675  -17.338 23.342  1.00 51.61  ? 312  SER A N   1 
ATOM   2274  C  CA  . SER A  1  286 ? -2.690  -16.459 22.714  1.00 50.32  ? 312  SER A CA  1 
ATOM   2275  C  C   . SER A  1  286 ? -1.306  -17.110 22.751  1.00 49.49  ? 312  SER A C   1 
ATOM   2276  O  O   . SER A  1  286 ? -0.757  -17.342 23.822  1.00 50.31  ? 312  SER A O   1 
ATOM   2277  C  CB  . SER A  1  286 ? -2.642  -15.116 23.435  1.00 51.84  ? 312  SER A CB  1 
ATOM   2278  O  OG  . SER A  1  286 ? -1.636  -14.286 22.878  1.00 52.65  ? 312  SER A OG  1 
ATOM   2279  N  N   . PHE A  1  287 ? -0.744  -17.405 21.587  1.00 47.69  ? 313  PHE A N   1 
ATOM   2280  C  CA  . PHE A  1  287 ? 0.565   -18.031 21.516  1.00 46.16  ? 313  PHE A CA  1 
ATOM   2281  C  C   . PHE A  1  287 ? 1.621   -17.118 20.884  1.00 46.14  ? 313  PHE A C   1 
ATOM   2282  O  O   . PHE A  1  287 ? 1.434   -16.600 19.778  1.00 46.44  ? 313  PHE A O   1 
ATOM   2283  C  CB  . PHE A  1  287 ? 0.478   -19.322 20.716  1.00 45.71  ? 313  PHE A CB  1 
ATOM   2284  C  CG  . PHE A  1  287 ? 1.718   -20.148 20.797  1.00 45.85  ? 313  PHE A CG  1 
ATOM   2285  C  CD1 . PHE A  1  287 ? 1.989   -20.894 21.939  1.00 43.82  ? 313  PHE A CD1 1 
ATOM   2286  C  CD2 . PHE A  1  287 ? 2.639   -20.147 19.754  1.00 44.94  ? 313  PHE A CD2 1 
ATOM   2287  C  CE1 . PHE A  1  287 ? 3.151   -21.623 22.037  1.00 43.75  ? 313  PHE A CE1 1 
ATOM   2288  C  CE2 . PHE A  1  287 ? 3.814   -20.875 19.844  1.00 43.82  ? 313  PHE A CE2 1 
ATOM   2289  C  CZ  . PHE A  1  287 ? 4.073   -21.616 20.985  1.00 45.15  ? 313  PHE A CZ  1 
ATOM   2290  N  N   . SER A  1  288 ? 2.745   -16.943 21.573  1.00 45.17  ? 314  SER A N   1 
ATOM   2291  C  CA  . SER A  1  288 ? 3.814   -16.078 21.071  1.00 45.02  ? 314  SER A CA  1 
ATOM   2292  C  C   . SER A  1  288 ? 5.245   -16.656 21.105  1.00 45.51  ? 314  SER A C   1 
ATOM   2293  O  O   . SER A  1  288 ? 5.654   -17.334 22.063  1.00 45.74  ? 314  SER A O   1 
ATOM   2294  C  CB  . SER A  1  288 ? 3.796   -14.755 21.839  1.00 44.08  ? 314  SER A CB  1 
ATOM   2295  O  OG  . SER A  1  288 ? 4.920   -13.961 21.515  1.00 43.47  ? 314  SER A OG  1 
ATOM   2296  N  N   . LEU A  1  289 ? 5.999   -16.365 20.043  1.00 44.27  ? 315  LEU A N   1 
ATOM   2297  C  CA  . LEU A  1  289 ? 7.392   -16.785 19.921  1.00 42.33  ? 315  LEU A CA  1 
ATOM   2298  C  C   . LEU A  1  289 ? 8.205   -15.579 19.466  1.00 42.36  ? 315  LEU A C   1 
ATOM   2299  O  O   . LEU A  1  289 ? 8.097   -15.164 18.312  1.00 42.50  ? 315  LEU A O   1 
ATOM   2300  C  CB  . LEU A  1  289 ? 7.559   -17.878 18.866  1.00 39.70  ? 315  LEU A CB  1 
ATOM   2301  C  CG  . LEU A  1  289 ? 7.080   -19.297 19.091  1.00 35.93  ? 315  LEU A CG  1 
ATOM   2302  C  CD1 . LEU A  1  289 ? 7.486   -20.089 17.877  1.00 32.02  ? 315  LEU A CD1 1 
ATOM   2303  C  CD2 . LEU A  1  289 ? 7.674   -19.876 20.341  1.00 34.25  ? 315  LEU A CD2 1 
ATOM   2304  N  N   . VAL A  1  290 ? 9.006   -15.007 20.359  1.00 41.67  ? 316  VAL A N   1 
ATOM   2305  C  CA  . VAL A  1  290 ? 9.821   -13.867 19.961  1.00 41.88  ? 316  VAL A CA  1 
ATOM   2306  C  C   . VAL A  1  290 ? 11.294  -14.248 20.029  1.00 40.98  ? 316  VAL A C   1 
ATOM   2307  O  O   . VAL A  1  290 ? 11.754  -14.778 21.032  1.00 39.31  ? 316  VAL A O   1 
ATOM   2308  C  CB  . VAL A  1  290 ? 9.514   -12.589 20.823  1.00 41.61  ? 316  VAL A CB  1 
ATOM   2309  C  CG1 . VAL A  1  290 ? 9.124   -12.973 22.221  1.00 41.80  ? 316  VAL A CG1 1 
ATOM   2310  C  CG2 . VAL A  1  290 ? 10.722  -11.670 20.836  1.00 41.29  ? 316  VAL A CG2 1 
ATOM   2311  N  N   . SER A  1  291 ? 12.008  -13.995 18.930  1.00 41.74  ? 317  SER A N   1 
ATOM   2312  C  CA  . SER A  1  291 ? 13.433  -14.310 18.795  1.00 42.22  ? 317  SER A CA  1 
ATOM   2313  C  C   . SER A  1  291 ? 13.789  -15.776 18.970  1.00 42.16  ? 317  SER A C   1 
ATOM   2314  O  O   . SER A  1  291 ? 14.585  -16.119 19.843  1.00 41.38  ? 317  SER A O   1 
ATOM   2315  C  CB  . SER A  1  291 ? 14.269  -13.501 19.790  1.00 43.06  ? 317  SER A CB  1 
ATOM   2316  O  OG  . SER A  1  291 ? 14.530  -12.197 19.315  1.00 45.05  ? 317  SER A OG  1 
ATOM   2317  N  N   . VAL A  1  292 ? 13.193  -16.644 18.164  1.00 42.74  ? 318  VAL A N   1 
ATOM   2318  C  CA  . VAL A  1  292 ? 13.509  -18.062 18.248  1.00 45.11  ? 318  VAL A CA  1 
ATOM   2319  C  C   . VAL A  1  292 ? 13.657  -18.569 16.819  1.00 46.85  ? 318  VAL A C   1 
ATOM   2320  O  O   . VAL A  1  292 ? 12.885  -18.177 15.941  1.00 44.96  ? 318  VAL A O   1 
ATOM   2321  C  CB  . VAL A  1  292 ? 12.422  -18.884 19.071  1.00 45.10  ? 318  VAL A CB  1 
ATOM   2322  C  CG1 . VAL A  1  292 ? 11.357  -17.961 19.637  1.00 44.14  ? 318  VAL A CG1 1 
ATOM   2323  C  CG2 . VAL A  1  292 ? 11.795  -19.980 18.217  1.00 45.13  ? 318  VAL A CG2 1 
ATOM   2324  N  N   . THR A  1  293 ? 14.676  -19.402 16.584  1.00 49.91  ? 319  THR A N   1 
ATOM   2325  C  CA  . THR A  1  293 ? 14.939  -19.944 15.247  1.00 53.37  ? 319  THR A CA  1 
ATOM   2326  C  C   . THR A  1  293 ? 14.102  -21.193 14.968  1.00 55.01  ? 319  THR A C   1 
ATOM   2327  O  O   . THR A  1  293 ? 14.163  -22.169 15.696  1.00 55.28  ? 319  THR A O   1 
ATOM   2328  C  CB  . THR A  1  293 ? 16.440  -20.282 15.052  1.00 53.48  ? 319  THR A CB  1 
ATOM   2329  O  OG1 . THR A  1  293 ? 17.237  -19.107 15.245  1.00 54.16  ? 319  THR A OG1 1 
ATOM   2330  C  CG2 . THR A  1  293 ? 16.689  -20.779 13.650  1.00 54.52  ? 319  THR A CG2 1 
ATOM   2331  N  N   . ILE A  1  294 ? 13.327  -21.152 13.892  1.00 58.30  ? 320  ILE A N   1 
ATOM   2332  C  CA  . ILE A  1  294 ? 12.444  -22.255 13.534  1.00 61.47  ? 320  ILE A CA  1 
ATOM   2333  C  C   . ILE A  1  294 ? 12.739  -22.834 12.151  1.00 65.15  ? 320  ILE A C   1 
ATOM   2334  O  O   . ILE A  1  294 ? 11.895  -23.496 11.572  1.00 66.86  ? 320  ILE A O   1 
ATOM   2335  C  CB  . ILE A  1  294 ? 10.938  -21.794 13.572  1.00 60.27  ? 320  ILE A CB  1 
ATOM   2336  C  CG1 . ILE A  1  294 ? 10.740  -20.545 12.678  1.00 59.11  ? 320  ILE A CG1 1 
ATOM   2337  C  CG2 . ILE A  1  294 ? 10.513  -21.537 15.008  1.00 57.83  ? 320  ILE A CG2 1 
ATOM   2338  C  CD1 . ILE A  1  294 ? 9.338   -19.979 12.593  1.00 52.82  ? 320  ILE A CD1 1 
ATOM   2339  N  N   . GLU A  1  295 ? 13.924  -22.581 11.615  1.00 69.37  ? 321  GLU A N   1 
ATOM   2340  C  CA  . GLU A  1  295 ? 14.282  -23.095 10.292  1.00 73.10  ? 321  GLU A CA  1 
ATOM   2341  C  C   . GLU A  1  295 ? 14.103  -24.603 10.246  1.00 73.78  ? 321  GLU A C   1 
ATOM   2342  O  O   . GLU A  1  295 ? 13.490  -25.140 9.334   1.00 72.44  ? 321  GLU A O   1 
ATOM   2343  C  CB  . GLU A  1  295 ? 15.745  -22.774 9.963   1.00 76.83  ? 321  GLU A CB  1 
ATOM   2344  C  CG  . GLU A  1  295 ? 16.117  -21.294 10.017  1.00 82.16  ? 321  GLU A CG  1 
ATOM   2345  C  CD  . GLU A  1  295 ? 17.616  -21.035 9.793   1.00 85.34  ? 321  GLU A CD  1 
ATOM   2346  O  OE1 . GLU A  1  295 ? 18.451  -21.413 10.652  1.00 87.24  ? 321  GLU A OE1 1 
ATOM   2347  O  OE2 . GLU A  1  295 ? 17.958  -20.446 8.744   1.00 86.97  ? 321  GLU A OE2 1 
ATOM   2348  N  N   . ARG A  1  296 ? 14.650  -25.271 11.254  1.00 76.53  ? 322  ARG A N   1 
ATOM   2349  C  CA  . ARG A  1  296 ? 14.602  -26.728 11.373  1.00 80.64  ? 322  ARG A CA  1 
ATOM   2350  C  C   . ARG A  1  296 ? 13.226  -27.363 11.555  1.00 80.60  ? 322  ARG A C   1 
ATOM   2351  O  O   . ARG A  1  296 ? 13.143  -28.533 11.931  1.00 80.26  ? 322  ARG A O   1 
ATOM   2352  C  CB  . ARG A  1  296 ? 15.499  -27.194 12.537  1.00 84.43  ? 322  ARG A CB  1 
ATOM   2353  C  CG  . ARG A  1  296 ? 17.006  -27.265 12.229  1.00 89.73  ? 322  ARG A CG  1 
ATOM   2354  C  CD  . ARG A  1  296 ? 17.608  -25.905 11.862  1.00 92.88  ? 322  ARG A CD  1 
ATOM   2355  N  NE  . ARG A  1  296 ? 19.067  -25.964 11.794  1.00 96.09  ? 322  ARG A NE  1 
ATOM   2356  C  CZ  . ARG A  1  296 ? 19.840  -26.385 12.792  1.00 98.56  ? 322  ARG A CZ  1 
ATOM   2357  N  NH1 . ARG A  1  296 ? 19.294  -26.786 13.939  1.00 99.19  ? 322  ARG A NH1 1 
ATOM   2358  N  NH2 . ARG A  1  296 ? 21.164  -26.406 12.650  1.00 100.33 ? 322  ARG A NH2 1 
ATOM   2359  N  N   . VAL A  1  297 ? 12.154  -26.615 11.311  1.00 81.00  ? 323  VAL A N   1 
ATOM   2360  C  CA  . VAL A  1  297 ? 10.813  -27.173 11.469  1.00 80.88  ? 323  VAL A CA  1 
ATOM   2361  C  C   . VAL A  1  297 ? 10.234  -27.439 10.103  1.00 81.69  ? 323  VAL A C   1 
ATOM   2362  O  O   . VAL A  1  297 ? 10.146  -26.534 9.276   1.00 80.51  ? 323  VAL A O   1 
ATOM   2363  C  CB  . VAL A  1  297 ? 9.863   -26.230 12.242  1.00 80.18  ? 323  VAL A CB  1 
ATOM   2364  C  CG1 . VAL A  1  297 ? 8.513   -26.897 12.411  1.00 79.46  ? 323  VAL A CG1 1 
ATOM   2365  C  CG2 . VAL A  1  297 ? 10.444  -25.900 13.608  1.00 80.02  ? 323  VAL A CG2 1 
ATOM   2366  N  N   . LYS A  1  298 ? 9.837   -28.693 9.887   1.00 84.38  ? 324  LYS A N   1 
ATOM   2367  C  CA  . LYS A  1  298 ? 9.287   -29.169 8.611   1.00 86.39  ? 324  LYS A CA  1 
ATOM   2368  C  C   . LYS A  1  298 ? 7.760   -29.073 8.496   1.00 87.36  ? 324  LYS A C   1 
ATOM   2369  O  O   . LYS A  1  298 ? 7.229   -28.911 7.390   1.00 87.68  ? 324  LYS A O   1 
ATOM   2370  C  CB  . LYS A  1  298 ? 9.738   -30.622 8.379   1.00 85.86  ? 324  LYS A CB  1 
ATOM   2371  C  CG  . LYS A  1  298 ? 10.084  -30.976 6.933   1.00 87.40  ? 324  LYS A CG  1 
ATOM   2372  C  CD  . LYS A  1  298 ? 8.850   -31.136 6.057   1.00 89.00  ? 324  LYS A CD  1 
ATOM   2373  C  CE  . LYS A  1  298 ? 9.223   -31.633 4.663   1.00 90.36  ? 324  LYS A CE  1 
ATOM   2374  N  NZ  . LYS A  1  298 ? 8.023   -31.918 3.804   1.00 90.51  ? 324  LYS A NZ  1 
ATOM   2375  N  N   . ASP A  1  299 ? 7.056   -29.164 9.624   1.00 88.01  ? 325  ASP A N   1 
ATOM   2376  C  CA  . ASP A  1  299 ? 5.597   -29.099 9.594   1.00 88.63  ? 325  ASP A CA  1 
ATOM   2377  C  C   . ASP A  1  299 ? 4.982   -28.000 10.459  1.00 89.15  ? 325  ASP A C   1 
ATOM   2378  O  O   . ASP A  1  299 ? 5.107   -28.007 11.685  1.00 89.38  ? 325  ASP A O   1 
ATOM   2379  C  CB  . ASP A  1  299 ? 4.993   -30.455 10.001  1.00 88.00  ? 325  ASP A CB  1 
ATOM   2380  C  CG  . ASP A  1  299 ? 3.533   -30.605 9.569   1.00 88.07  ? 325  ASP A CG  1 
ATOM   2381  O  OD1 . ASP A  1  299 ? 2.679   -29.812 10.016  1.00 87.34  ? 325  ASP A OD1 1 
ATOM   2382  O  OD2 . ASP A  1  299 ? 3.238   -31.516 8.770   1.00 88.18  ? 325  ASP A OD2 1 
ATOM   2383  N  N   . PHE A  1  300 ? 4.312   -27.062 9.798   1.00 89.89  ? 326  PHE A N   1 
ATOM   2384  C  CA  . PHE A  1  300 ? 3.622   -25.955 10.464  1.00 90.27  ? 326  PHE A CA  1 
ATOM   2385  C  C   . PHE A  1  300 ? 2.114   -26.127 10.223  1.00 90.98  ? 326  PHE A C   1 
ATOM   2386  O  O   . PHE A  1  300 ? 1.357   -25.146 10.202  1.00 91.30  ? 326  PHE A O   1 
ATOM   2387  C  CB  . PHE A  1  300 ? 4.071   -24.608 9.881   1.00 88.38  ? 326  PHE A CB  1 
ATOM   2388  C  CG  . PHE A  1  300 ? 5.528   -24.310 10.082  1.00 85.26  ? 326  PHE A CG  1 
ATOM   2389  C  CD1 . PHE A  1  300 ? 6.481   -24.799 9.193   1.00 83.61  ? 326  PHE A CD1 1 
ATOM   2390  C  CD2 . PHE A  1  300 ? 5.943   -23.548 11.167  1.00 82.83  ? 326  PHE A CD2 1 
ATOM   2391  C  CE1 . PHE A  1  300 ? 7.821   -24.531 9.381   1.00 82.35  ? 326  PHE A CE1 1 
ATOM   2392  C  CE2 . PHE A  1  300 ? 7.278   -23.272 11.368  1.00 81.92  ? 326  PHE A CE2 1 
ATOM   2393  C  CZ  . PHE A  1  300 ? 8.226   -23.764 10.474  1.00 82.77  ? 326  PHE A CZ  1 
ATOM   2394  N  N   . SER A  1  301 ? 1.693   -27.384 10.058  1.00 90.87  ? 327  SER A N   1 
ATOM   2395  C  CA  . SER A  1  301 ? 0.302   -27.723 9.771   1.00 89.85  ? 327  SER A CA  1 
ATOM   2396  C  C   . SER A  1  301 ? -0.648  -28.084 10.921  1.00 88.33  ? 327  SER A C   1 
ATOM   2397  O  O   . SER A  1  301 ? -1.859  -28.106 10.716  1.00 88.22  ? 327  SER A O   1 
ATOM   2398  C  CB  . SER A  1  301 ? 0.269   -28.852 8.737   1.00 90.69  ? 327  SER A CB  1 
ATOM   2399  O  OG  . SER A  1  301 ? -1.064  -29.201 8.393   1.00 92.85  ? 327  SER A OG  1 
ATOM   2400  N  N   . TYR A  1  302 ? -0.134  -28.360 12.117  1.00 86.55  ? 328  TYR A N   1 
ATOM   2401  C  CA  . TYR A  1  302 ? -1.026  -28.722 13.214  1.00 84.65  ? 328  TYR A CA  1 
ATOM   2402  C  C   . TYR A  1  302 ? -2.094  -27.676 13.516  1.00 84.19  ? 328  TYR A C   1 
ATOM   2403  O  O   . TYR A  1  302 ? -1.860  -26.468 13.410  1.00 84.40  ? 328  TYR A O   1 
ATOM   2404  C  CB  . TYR A  1  302 ? -0.254  -29.018 14.486  1.00 84.08  ? 328  TYR A CB  1 
ATOM   2405  C  CG  . TYR A  1  302 ? -1.138  -29.684 15.500  1.00 85.39  ? 328  TYR A CG  1 
ATOM   2406  C  CD1 . TYR A  1  302 ? -1.653  -30.954 15.266  1.00 86.47  ? 328  TYR A CD1 1 
ATOM   2407  C  CD2 . TYR A  1  302 ? -1.493  -29.036 16.674  1.00 87.50  ? 328  TYR A CD2 1 
ATOM   2408  C  CE1 . TYR A  1  302 ? -2.504  -31.570 16.172  1.00 88.56  ? 328  TYR A CE1 1 
ATOM   2409  C  CE2 . TYR A  1  302 ? -2.346  -29.635 17.598  1.00 89.99  ? 328  TYR A CE2 1 
ATOM   2410  C  CZ  . TYR A  1  302 ? -2.851  -30.907 17.340  1.00 90.54  ? 328  TYR A CZ  1 
ATOM   2411  O  OH  . TYR A  1  302 ? -3.721  -31.504 18.237  1.00 91.41  ? 328  TYR A OH  1 
ATOM   2412  N  N   . ASN A  1  303 ? -3.269  -28.160 13.910  1.00 83.03  ? 329  ASN A N   1 
ATOM   2413  C  CA  . ASN A  1  303 ? -4.410  -27.300 14.219  1.00 81.18  ? 329  ASN A CA  1 
ATOM   2414  C  C   . ASN A  1  303 ? -4.584  -27.064 15.728  1.00 78.20  ? 329  ASN A C   1 
ATOM   2415  O  O   . ASN A  1  303 ? -5.322  -27.774 16.430  1.00 76.48  ? 329  ASN A O   1 
ATOM   2416  C  CB  . ASN A  1  303 ? -5.683  -27.911 13.591  1.00 83.55  ? 329  ASN A CB  1 
ATOM   2417  C  CG  . ASN A  1  303 ? -6.926  -27.043 13.775  1.00 84.45  ? 329  ASN A CG  1 
ATOM   2418  O  OD1 . ASN A  1  303 ? -6.918  -25.839 13.494  1.00 83.97  ? 329  ASN A OD1 1 
ATOM   2419  N  ND2 . ASN A  1  303 ? -8.010  -27.666 14.232  1.00 84.44  ? 329  ASN A ND2 1 
ATOM   2420  N  N   . PHE A  1  304 ? -3.871  -26.054 16.212  1.00 74.73  ? 330  PHE A N   1 
ATOM   2421  C  CA  . PHE A  1  304 ? -3.920  -25.651 17.607  1.00 72.54  ? 330  PHE A CA  1 
ATOM   2422  C  C   . PHE A  1  304 ? -5.182  -24.794 17.815  1.00 70.76  ? 330  PHE A C   1 
ATOM   2423  O  O   . PHE A  1  304 ? -5.718  -24.221 16.862  1.00 72.45  ? 330  PHE A O   1 
ATOM   2424  C  CB  . PHE A  1  304 ? -2.677  -24.822 17.926  1.00 72.02  ? 330  PHE A CB  1 
ATOM   2425  C  CG  . PHE A  1  304 ? -1.375  -25.584 17.811  1.00 71.16  ? 330  PHE A CG  1 
ATOM   2426  C  CD1 . PHE A  1  304 ? -0.990  -26.489 18.798  1.00 70.98  ? 330  PHE A CD1 1 
ATOM   2427  C  CD2 . PHE A  1  304 ? -0.506  -25.346 16.747  1.00 70.30  ? 330  PHE A CD2 1 
ATOM   2428  C  CE1 . PHE A  1  304 ? 0.238   -27.136 18.736  1.00 69.59  ? 330  PHE A CE1 1 
ATOM   2429  C  CE2 . PHE A  1  304 ? 0.725   -25.988 16.669  1.00 68.71  ? 330  PHE A CE2 1 
ATOM   2430  C  CZ  . PHE A  1  304 ? 1.101   -26.882 17.668  1.00 69.48  ? 330  PHE A CZ  1 
ATOM   2431  N  N   . GLY A  1  305 ? -5.659  -24.687 19.047  1.00 66.75  ? 331  GLY A N   1 
ATOM   2432  C  CA  . GLY A  1  305 ? -6.853  -23.892 19.276  1.00 62.79  ? 331  GLY A CA  1 
ATOM   2433  C  C   . GLY A  1  305 ? -6.568  -22.421 19.485  1.00 60.09  ? 331  GLY A C   1 
ATOM   2434  O  O   . GLY A  1  305 ? -7.444  -21.666 19.927  1.00 59.52  ? 331  GLY A O   1 
ATOM   2435  N  N   . TRP A  1  306 ? -5.339  -22.016 19.171  1.00 57.83  ? 332  TRP A N   1 
ATOM   2436  C  CA  . TRP A  1  306 ? -4.899  -20.628 19.328  1.00 54.79  ? 332  TRP A CA  1 
ATOM   2437  C  C   . TRP A  1  306 ? -5.750  -19.657 18.542  1.00 54.00  ? 332  TRP A C   1 
ATOM   2438  O  O   . TRP A  1  306 ? -6.148  -19.956 17.418  1.00 54.13  ? 332  TRP A O   1 
ATOM   2439  C  CB  . TRP A  1  306 ? -3.467  -20.443 18.835  1.00 52.08  ? 332  TRP A CB  1 
ATOM   2440  C  CG  . TRP A  1  306 ? -2.449  -21.407 19.344  1.00 50.59  ? 332  TRP A CG  1 
ATOM   2441  C  CD1 . TRP A  1  306 ? -2.491  -22.128 20.502  1.00 50.29  ? 332  TRP A CD1 1 
ATOM   2442  C  CD2 . TRP A  1  306 ? -1.184  -21.700 18.738  1.00 49.41  ? 332  TRP A CD2 1 
ATOM   2443  N  NE1 . TRP A  1  306 ? -1.328  -22.848 20.653  1.00 49.27  ? 332  TRP A NE1 1 
ATOM   2444  C  CE2 . TRP A  1  306 ? -0.512  -22.600 19.583  1.00 48.48  ? 332  TRP A CE2 1 
ATOM   2445  C  CE3 . TRP A  1  306 ? -0.556  -21.285 17.560  1.00 49.44  ? 332  TRP A CE3 1 
ATOM   2446  C  CZ2 . TRP A  1  306 ? 0.754   -23.089 19.288  1.00 48.75  ? 332  TRP A CZ2 1 
ATOM   2447  C  CZ3 . TRP A  1  306 ? 0.699   -21.771 17.267  1.00 48.25  ? 332  TRP A CZ3 1 
ATOM   2448  C  CH2 . TRP A  1  306 ? 1.342   -22.661 18.124  1.00 50.11  ? 332  TRP A CH2 1 
ATOM   2449  N  N   . GLN A  1  307 ? -6.000  -18.484 19.119  1.00 54.32  ? 333  GLN A N   1 
ATOM   2450  C  CA  . GLN A  1  307 ? -6.788  -17.443 18.450  1.00 54.95  ? 333  GLN A CA  1 
ATOM   2451  C  C   . GLN A  1  307 ? -5.938  -16.254 18.066  1.00 52.85  ? 333  GLN A C   1 
ATOM   2452  O  O   . GLN A  1  307 ? -6.311  -15.487 17.191  1.00 51.19  ? 333  GLN A O   1 
ATOM   2453  C  CB  . GLN A  1  307 ? -7.914  -16.963 19.334  1.00 56.82  ? 333  GLN A CB  1 
ATOM   2454  C  CG  . GLN A  1  307 ? -8.855  -18.055 19.697  1.00 62.93  ? 333  GLN A CG  1 
ATOM   2455  C  CD  . GLN A  1  307 ? -9.880  -17.568 20.656  1.00 67.48  ? 333  GLN A CD  1 
ATOM   2456  O  OE1 . GLN A  1  307 ? -10.165 -18.230 21.656  1.00 70.63  ? 333  GLN A OE1 1 
ATOM   2457  N  NE2 . GLN A  1  307 ? -10.453 -16.390 20.370  1.00 68.75  ? 333  GLN A NE2 1 
ATOM   2458  N  N   . HIS A  1  308 ? -4.809  -16.100 18.752  1.00 52.13  ? 334  HIS A N   1 
ATOM   2459  C  CA  . HIS A  1  308 ? -3.850  -15.044 18.463  1.00 52.14  ? 334  HIS A CA  1 
ATOM   2460  C  C   . HIS A  1  308 ? -2.450  -15.667 18.386  1.00 50.33  ? 334  HIS A C   1 
ATOM   2461  O  O   . HIS A  1  308 ? -2.004  -16.290 19.343  1.00 50.50  ? 334  HIS A O   1 
ATOM   2462  C  CB  . HIS A  1  308 ? -3.871  -13.967 19.551  1.00 54.34  ? 334  HIS A CB  1 
ATOM   2463  C  CG  . HIS A  1  308 ? -2.777  -12.952 19.405  1.00 58.41  ? 334  HIS A CG  1 
ATOM   2464  N  ND1 . HIS A  1  308 ? -2.033  -12.496 20.476  1.00 59.09  ? 334  HIS A ND1 1 
ATOM   2465  C  CD2 . HIS A  1  308 ? -2.282  -12.322 18.309  1.00 59.16  ? 334  HIS A CD2 1 
ATOM   2466  C  CE1 . HIS A  1  308 ? -1.129  -11.631 20.044  1.00 59.37  ? 334  HIS A CE1 1 
ATOM   2467  N  NE2 . HIS A  1  308 ? -1.259  -11.506 18.734  1.00 59.80  ? 334  HIS A NE2 1 
ATOM   2468  N  N   . LEU A  1  309 ? -1.772  -15.515 17.251  1.00 47.72  ? 335  LEU A N   1 
ATOM   2469  C  CA  . LEU A  1  309 ? -0.431  -16.065 17.089  1.00 47.39  ? 335  LEU A CA  1 
ATOM   2470  C  C   . LEU A  1  309 ? 0.496   -14.936 16.735  1.00 49.18  ? 335  LEU A C   1 
ATOM   2471  O  O   . LEU A  1  309 ? 0.247   -14.209 15.768  1.00 50.29  ? 335  LEU A O   1 
ATOM   2472  C  CB  . LEU A  1  309 ? -0.380  -17.093 15.960  1.00 44.45  ? 335  LEU A CB  1 
ATOM   2473  C  CG  . LEU A  1  309 ? 1.016   -17.609 15.607  1.00 41.42  ? 335  LEU A CG  1 
ATOM   2474  C  CD1 . LEU A  1  309 ? 1.689   -18.230 16.821  1.00 38.65  ? 335  LEU A CD1 1 
ATOM   2475  C  CD2 . LEU A  1  309 ? 0.887   -18.609 14.489  1.00 41.72  ? 335  LEU A CD2 1 
ATOM   2476  N  N   . GLU A  1  310 ? 1.577   -14.799 17.500  1.00 50.95  ? 336  GLU A N   1 
ATOM   2477  C  CA  . GLU A  1  310 ? 2.552   -13.735 17.256  1.00 50.91  ? 336  GLU A CA  1 
ATOM   2478  C  C   . GLU A  1  310 ? 3.992   -14.245 17.116  1.00 49.48  ? 336  GLU A C   1 
ATOM   2479  O  O   . GLU A  1  310 ? 4.574   -14.806 18.050  1.00 49.02  ? 336  GLU A O   1 
ATOM   2480  C  CB  . GLU A  1  310 ? 2.474   -12.687 18.376  1.00 53.17  ? 336  GLU A CB  1 
ATOM   2481  C  CG  . GLU A  1  310 ? 3.583   -11.645 18.345  1.00 56.44  ? 336  GLU A CG  1 
ATOM   2482  C  CD  . GLU A  1  310 ? 3.603   -10.767 19.595  1.00 59.92  ? 336  GLU A CD  1 
ATOM   2483  O  OE1 . GLU A  1  310 ? 3.411   -11.301 20.719  1.00 60.02  ? 336  GLU A OE1 1 
ATOM   2484  O  OE2 . GLU A  1  310 ? 3.827   -9.540  19.451  1.00 62.19  ? 336  GLU A OE2 1 
ATOM   2485  N  N   . LEU A  1  311 ? 4.552   -14.052 15.932  1.00 47.49  ? 337  LEU A N   1 
ATOM   2486  C  CA  . LEU A  1  311 ? 5.921   -14.443 15.654  1.00 46.44  ? 337  LEU A CA  1 
ATOM   2487  C  C   . LEU A  1  311 ? 6.719   -13.183 15.314  1.00 46.07  ? 337  LEU A C   1 
ATOM   2488  O  O   . LEU A  1  311 ? 6.496   -12.591 14.257  1.00 46.27  ? 337  LEU A O   1 
ATOM   2489  C  CB  . LEU A  1  311 ? 5.949   -15.399 14.467  1.00 44.62  ? 337  LEU A CB  1 
ATOM   2490  C  CG  . LEU A  1  311 ? 5.258   -16.728 14.720  1.00 44.74  ? 337  LEU A CG  1 
ATOM   2491  C  CD1 . LEU A  1  311 ? 5.197   -17.557 13.444  1.00 42.52  ? 337  LEU A CD1 1 
ATOM   2492  C  CD2 . LEU A  1  311 ? 6.032   -17.451 15.812  1.00 45.27  ? 337  LEU A CD2 1 
ATOM   2493  N  N   . VAL A  1  312 ? 7.620   -12.752 16.197  1.00 45.44  ? 338  VAL A N   1 
ATOM   2494  C  CA  . VAL A  1  312 ? 8.413   -11.568 15.887  1.00 47.17  ? 338  VAL A CA  1 
ATOM   2495  C  C   . VAL A  1  312 ? 9.886   -11.773 16.143  1.00 47.59  ? 338  VAL A C   1 
ATOM   2496  O  O   . VAL A  1  312 ? 10.282  -12.313 17.171  1.00 45.97  ? 338  VAL A O   1 
ATOM   2497  C  CB  . VAL A  1  312 ? 7.959   -10.303 16.668  1.00 47.16  ? 338  VAL A CB  1 
ATOM   2498  C  CG1 . VAL A  1  312 ? 6.462   -10.143 16.567  1.00 47.63  ? 338  VAL A CG1 1 
ATOM   2499  C  CG2 . VAL A  1  312 ? 8.385   -10.390 18.100  1.00 47.31  ? 338  VAL A CG2 1 
ATOM   2500  N  N   . ASN A  1  313 ? 10.685  -11.333 15.179  1.00 49.92  ? 339  ASN A N   1 
ATOM   2501  C  CA  . ASN A  1  313 ? 12.136  -11.438 15.231  1.00 52.49  ? 339  ASN A CA  1 
ATOM   2502  C  C   . ASN A  1  313 ? 12.660  -12.884 15.261  1.00 51.44  ? 339  ASN A C   1 
ATOM   2503  O  O   . ASN A  1  313 ? 13.603  -13.208 15.978  1.00 50.54  ? 339  ASN A O   1 
ATOM   2504  C  CB  . ASN A  1  313 ? 12.669  -10.666 16.437  1.00 55.54  ? 339  ASN A CB  1 
ATOM   2505  C  CG  . ASN A  1  313 ? 14.145  -10.332 16.299  1.00 61.16  ? 339  ASN A CG  1 
ATOM   2506  O  OD1 . ASN A  1  313 ? 14.787  -9.920  17.265  1.00 64.39  ? 339  ASN A OD1 1 
ATOM   2507  N  ND2 . ASN A  1  313 ? 14.693  -10.504 15.084  1.00 63.56  ? 339  ASN A ND2 1 
ATOM   2508  N  N   . CYS A  1  314 ? 12.059  -13.747 14.462  1.00 51.06  ? 340  CYS A N   1 
ATOM   2509  C  CA  . CYS A  1  314 ? 12.475  -15.132 14.431  1.00 52.54  ? 340  CYS A CA  1 
ATOM   2510  C  C   . CYS A  1  314 ? 13.192  -15.402 13.124  1.00 55.10  ? 340  CYS A C   1 
ATOM   2511  O  O   . CYS A  1  314 ? 12.960  -14.694 12.146  1.00 55.23  ? 340  CYS A O   1 
ATOM   2512  C  CB  . CYS A  1  314 ? 11.247  -16.042 14.538  1.00 51.64  ? 340  CYS A CB  1 
ATOM   2513  S  SG  . CYS A  1  314 ? 10.222  -15.861 16.059  1.00 50.65  ? 340  CYS A SG  1 
ATOM   2514  N  N   . LYS A  1  315 ? 14.073  -16.404 13.105  1.00 57.81  ? 341  LYS A N   1 
ATOM   2515  C  CA  . LYS A  1  315 ? 14.768  -16.778 11.861  1.00 59.66  ? 341  LYS A CA  1 
ATOM   2516  C  C   . LYS A  1  315 ? 13.950  -17.947 11.314  1.00 60.79  ? 341  LYS A C   1 
ATOM   2517  O  O   . LYS A  1  315 ? 13.706  -18.918 12.033  1.00 59.18  ? 341  LYS A O   1 
ATOM   2518  C  CB  . LYS A  1  315 ? 16.205  -17.225 12.132  1.00 59.60  ? 341  LYS A CB  1 
ATOM   2519  C  CG  . LYS A  1  315 ? 17.192  -16.643 11.140  1.00 59.25  ? 341  LYS A CG  1 
ATOM   2520  C  CD  . LYS A  1  315 ? 17.988  -17.689 10.393  1.00 59.34  ? 341  LYS A CD  1 
ATOM   2521  C  CE  . LYS A  1  315 ? 18.890  -17.021 9.365   1.00 60.25  ? 341  LYS A CE  1 
ATOM   2522  N  NZ  . LYS A  1  315 ? 19.783  -17.983 8.639   1.00 63.57  ? 341  LYS A NZ  1 
ATOM   2523  N  N   . PHE A  1  316 ? 13.525  -17.875 10.058  1.00 62.42  ? 342  PHE A N   1 
ATOM   2524  C  CA  . PHE A  1  316 ? 12.681  -18.947 9.559   1.00 66.38  ? 342  PHE A CA  1 
ATOM   2525  C  C   . PHE A  1  316 ? 13.074  -19.667 8.265   1.00 67.37  ? 342  PHE A C   1 
ATOM   2526  O  O   . PHE A  1  316 ? 12.946  -20.896 8.165   1.00 66.90  ? 342  PHE A O   1 
ATOM   2527  C  CB  . PHE A  1  316 ? 11.238  -18.426 9.465   1.00 68.32  ? 342  PHE A CB  1 
ATOM   2528  C  CG  . PHE A  1  316 ? 11.069  -17.215 8.555   1.00 73.08  ? 342  PHE A CG  1 
ATOM   2529  C  CD1 . PHE A  1  316 ? 10.541  -17.355 7.263   1.00 74.69  ? 342  PHE A CD1 1 
ATOM   2530  C  CD2 . PHE A  1  316 ? 11.401  -15.930 8.995   1.00 74.48  ? 342  PHE A CD2 1 
ATOM   2531  C  CE1 . PHE A  1  316 ? 10.341  -16.236 6.417   1.00 73.93  ? 342  PHE A CE1 1 
ATOM   2532  C  CE2 . PHE A  1  316 ? 11.207  -14.800 8.160   1.00 74.93  ? 342  PHE A CE2 1 
ATOM   2533  C  CZ  . PHE A  1  316 ? 10.672  -14.957 6.870   1.00 74.21  ? 342  PHE A CZ  1 
ATOM   2534  N  N   . GLY A  1  317 ? 13.553  -18.921 7.275   1.00 68.22  ? 343  GLY A N   1 
ATOM   2535  C  CA  . GLY A  1  317 ? 13.912  -19.557 6.014   1.00 69.45  ? 343  GLY A CA  1 
ATOM   2536  C  C   . GLY A  1  317 ? 12.705  -19.738 5.098   1.00 68.63  ? 343  GLY A C   1 
ATOM   2537  O  O   . GLY A  1  317 ? 12.346  -18.823 4.343   1.00 68.55  ? 343  GLY A O   1 
ATOM   2538  N  N   . GLN A  1  318 ? 12.071  -20.905 5.149   1.00 67.20  ? 344  GLN A N   1 
ATOM   2539  C  CA  . GLN A  1  318 ? 10.897  -21.130 4.311   1.00 66.27  ? 344  GLN A CA  1 
ATOM   2540  C  C   . GLN A  1  318 ? 9.695   -20.601 5.074   1.00 63.11  ? 344  GLN A C   1 
ATOM   2541  O  O   . GLN A  1  318 ? 9.610   -20.791 6.285   1.00 62.22  ? 344  GLN A O   1 
ATOM   2542  C  CB  . GLN A  1  318 ? 10.708  -22.618 4.049   1.00 71.27  ? 344  GLN A CB  1 
ATOM   2543  C  CG  . GLN A  1  318 ? 9.965   -22.927 2.759   1.00 76.51  ? 344  GLN A CG  1 
ATOM   2544  C  CD  . GLN A  1  318 ? 9.478   -24.367 2.696   1.00 80.26  ? 344  GLN A CD  1 
ATOM   2545  O  OE1 . GLN A  1  318 ? 9.258   -24.914 1.608   1.00 81.71  ? 344  GLN A OE1 1 
ATOM   2546  N  NE2 . GLN A  1  318 ? 9.294   -24.989 3.869   1.00 81.48  ? 344  GLN A NE2 1 
ATOM   2547  N  N   . PHE A  1  319 ? 8.765   -19.952 4.378   1.00 60.12  ? 345  PHE A N   1 
ATOM   2548  C  CA  . PHE A  1  319 ? 7.585   -19.385 5.039   1.00 58.76  ? 345  PHE A CA  1 
ATOM   2549  C  C   . PHE A  1  319 ? 6.689   -20.436 5.686   1.00 57.68  ? 345  PHE A C   1 
ATOM   2550  O  O   . PHE A  1  319 ? 6.277   -21.388 5.036   1.00 57.99  ? 345  PHE A O   1 
ATOM   2551  C  CB  . PHE A  1  319 ? 6.752   -18.566 4.053   1.00 57.65  ? 345  PHE A CB  1 
ATOM   2552  C  CG  . PHE A  1  319 ? 5.804   -17.612 4.720   1.00 56.59  ? 345  PHE A CG  1 
ATOM   2553  C  CD1 . PHE A  1  319 ? 6.279   -16.488 5.378   1.00 56.95  ? 345  PHE A CD1 1 
ATOM   2554  C  CD2 . PHE A  1  319 ? 4.448   -17.846 4.715   1.00 56.26  ? 345  PHE A CD2 1 
ATOM   2555  C  CE1 . PHE A  1  319 ? 5.410   -15.613 6.025   1.00 55.88  ? 345  PHE A CE1 1 
ATOM   2556  C  CE2 . PHE A  1  319 ? 3.577   -16.976 5.359   1.00 56.32  ? 345  PHE A CE2 1 
ATOM   2557  C  CZ  . PHE A  1  319 ? 4.063   -15.856 6.017   1.00 54.80  ? 345  PHE A CZ  1 
ATOM   2558  N  N   . PRO A  1  320 ? 6.357   -20.258 6.974   1.00 56.85  ? 346  PRO A N   1 
ATOM   2559  C  CA  . PRO A  1  320 ? 5.509   -21.202 7.704   1.00 57.94  ? 346  PRO A CA  1 
ATOM   2560  C  C   . PRO A  1  320 ? 4.128   -21.417 7.099   1.00 59.83  ? 346  PRO A C   1 
ATOM   2561  O  O   . PRO A  1  320 ? 3.364   -20.476 6.953   1.00 61.32  ? 346  PRO A O   1 
ATOM   2562  C  CB  . PRO A  1  320 ? 5.458   -20.602 9.111   1.00 56.34  ? 346  PRO A CB  1 
ATOM   2563  C  CG  . PRO A  1  320 ? 5.612   -19.164 8.874   1.00 55.81  ? 346  PRO A CG  1 
ATOM   2564  C  CD  . PRO A  1  320 ? 6.675   -19.091 7.811   1.00 56.23  ? 346  PRO A CD  1 
ATOM   2565  N  N   . THR A  1  321 ? 3.818   -22.663 6.736   1.00 62.30  ? 347  THR A N   1 
ATOM   2566  C  CA  . THR A  1  321 ? 2.504   -22.998 6.150   1.00 63.89  ? 347  THR A CA  1 
ATOM   2567  C  C   . THR A  1  321 ? 1.477   -23.231 7.264   1.00 62.79  ? 347  THR A C   1 
ATOM   2568  O  O   . THR A  1  321 ? 1.168   -24.368 7.627   1.00 62.35  ? 347  THR A O   1 
ATOM   2569  C  CB  . THR A  1  321 ? 2.562   -24.273 5.240   1.00 65.27  ? 347  THR A CB  1 
ATOM   2570  O  OG1 . THR A  1  321 ? 3.471   -25.231 5.810   1.00 67.42  ? 347  THR A OG1 1 
ATOM   2571  C  CG2 . THR A  1  321 ? 2.988   -23.911 3.810   1.00 63.55  ? 347  THR A CG2 1 
ATOM   2572  N  N   . LEU A  1  322 ? 0.961   -22.127 7.788   1.00 61.58  ? 348  LEU A N   1 
ATOM   2573  C  CA  . LEU A  1  322 ? -0.007  -22.125 8.867   1.00 59.34  ? 348  LEU A CA  1 
ATOM   2574  C  C   . LEU A  1  322 ? -1.386  -22.554 8.406   1.00 58.93  ? 348  LEU A C   1 
ATOM   2575  O  O   . LEU A  1  322 ? -1.855  -22.142 7.345   1.00 57.62  ? 348  LEU A O   1 
ATOM   2576  C  CB  . LEU A  1  322 ? -0.088  -20.722 9.457   1.00 59.04  ? 348  LEU A CB  1 
ATOM   2577  C  CG  . LEU A  1  322 ? 1.264   -20.129 9.840   1.00 58.76  ? 348  LEU A CG  1 
ATOM   2578  C  CD1 . LEU A  1  322 ? 1.131   -18.638 9.996   1.00 59.23  ? 348  LEU A CD1 1 
ATOM   2579  C  CD2 . LEU A  1  322 ? 1.760   -20.767 11.113  1.00 57.04  ? 348  LEU A CD2 1 
ATOM   2580  N  N   . LYS A  1  323 ? -2.030  -23.380 9.224   1.00 59.44  ? 349  LYS A N   1 
ATOM   2581  C  CA  . LYS A  1  323 ? -3.368  -23.886 8.930   1.00 59.62  ? 349  LYS A CA  1 
ATOM   2582  C  C   . LYS A  1  323 ? -4.205  -23.910 10.202  1.00 59.25  ? 349  LYS A C   1 
ATOM   2583  O  O   . LYS A  1  323 ? -4.982  -24.835 10.425  1.00 60.96  ? 349  LYS A O   1 
ATOM   2584  C  CB  . LYS A  1  323 ? -3.282  -25.297 8.335   1.00 59.91  ? 349  LYS A CB  1 
ATOM   2585  C  CG  . LYS A  1  323 ? -2.601  -25.364 6.978   1.00 61.77  ? 349  LYS A CG  1 
ATOM   2586  C  CD  . LYS A  1  323 ? -2.457  -26.804 6.472   1.00 62.99  ? 349  LYS A CD  1 
ATOM   2587  C  CE  . LYS A  1  323 ? -1.954  -26.856 5.024   1.00 63.14  ? 349  LYS A CE  1 
ATOM   2588  N  NZ  . LYS A  1  323 ? -2.858  -26.130 4.070   1.00 63.36  ? 349  LYS A NZ  1 
ATOM   2589  N  N   . LEU A  1  324 ? -4.028  -22.894 11.041  1.00 57.88  ? 350  LEU A N   1 
ATOM   2590  C  CA  . LEU A  1  324 ? -4.762  -22.770 12.300  1.00 56.67  ? 350  LEU A CA  1 
ATOM   2591  C  C   . LEU A  1  324 ? -6.183  -22.298 11.998  1.00 57.79  ? 350  LEU A C   1 
ATOM   2592  O  O   . LEU A  1  324 ? -6.395  -21.138 11.642  1.00 58.75  ? 350  LEU A O   1 
ATOM   2593  C  CB  . LEU A  1  324 ? -4.057  -21.754 13.195  1.00 54.76  ? 350  LEU A CB  1 
ATOM   2594  C  CG  . LEU A  1  324 ? -2.565  -22.026 13.410  1.00 52.08  ? 350  LEU A CG  1 
ATOM   2595  C  CD1 . LEU A  1  324 ? -1.822  -20.770 13.808  1.00 49.97  ? 350  LEU A CD1 1 
ATOM   2596  C  CD2 . LEU A  1  324 ? -2.427  -23.088 14.467  1.00 52.76  ? 350  LEU A CD2 1 
ATOM   2597  N  N   . LYS A  1  325 ? -7.157  -23.195 12.157  1.00 58.59  ? 351  LYS A N   1 
ATOM   2598  C  CA  . LYS A  1  325 ? -8.560  -22.886 11.857  1.00 58.04  ? 351  LYS A CA  1 
ATOM   2599  C  C   . LYS A  1  325 ? -9.235  -21.850 12.752  1.00 57.82  ? 351  LYS A C   1 
ATOM   2600  O  O   . LYS A  1  325 ? -10.036 -21.057 12.259  1.00 57.88  ? 351  LYS A O   1 
ATOM   2601  C  CB  . LYS A  1  325 ? -9.401  -24.164 11.889  1.00 57.82  ? 351  LYS A CB  1 
ATOM   2602  C  CG  . LYS A  1  325 ? -8.821  -25.313 11.110  1.00 58.84  ? 351  LYS A CG  1 
ATOM   2603  C  CD  . LYS A  1  325 ? -8.611  -24.935 9.654   1.00 60.90  ? 351  LYS A CD  1 
ATOM   2604  C  CE  . LYS A  1  325 ? -7.940  -26.076 8.896   1.00 62.47  ? 351  LYS A CE  1 
ATOM   2605  N  NZ  . LYS A  1  325 ? -7.606  -25.677 7.500   1.00 63.65  ? 351  LYS A NZ  1 
ATOM   2606  N  N   . SER A  1  326 ? -8.922  -21.853 14.053  1.00 57.21  ? 352  SER A N   1 
ATOM   2607  C  CA  . SER A  1  326 ? -9.555  -20.923 15.001  1.00 55.92  ? 352  SER A CA  1 
ATOM   2608  C  C   . SER A  1  326 ? -8.890  -19.557 15.118  1.00 55.47  ? 352  SER A C   1 
ATOM   2609  O  O   . SER A  1  326 ? -9.480  -18.622 15.682  1.00 54.21  ? 352  SER A O   1 
ATOM   2610  C  CB  . SER A  1  326 ? -9.606  -21.540 16.395  1.00 56.00  ? 352  SER A CB  1 
ATOM   2611  O  OG  . SER A  1  326 ? -10.040 -22.884 16.341  1.00 58.79  ? 352  SER A OG  1 
ATOM   2612  N  N   . LEU A  1  327 ? -7.663  -19.452 14.608  1.00 54.27  ? 353  LEU A N   1 
ATOM   2613  C  CA  . LEU A  1  327 ? -6.908  -18.206 14.660  1.00 52.70  ? 353  LEU A CA  1 
ATOM   2614  C  C   . LEU A  1  327 ? -7.699  -17.021 14.060  1.00 52.65  ? 353  LEU A C   1 
ATOM   2615  O  O   . LEU A  1  327 ? -8.260  -17.124 12.962  1.00 51.08  ? 353  LEU A O   1 
ATOM   2616  C  CB  . LEU A  1  327 ? -5.570  -18.385 13.923  1.00 50.12  ? 353  LEU A CB  1 
ATOM   2617  C  CG  . LEU A  1  327 ? -4.571  -17.227 14.000  1.00 48.69  ? 353  LEU A CG  1 
ATOM   2618  C  CD1 . LEU A  1  327 ? -4.019  -17.172 15.401  1.00 45.42  ? 353  LEU A CD1 1 
ATOM   2619  C  CD2 . LEU A  1  327 ? -3.447  -17.397 12.989  1.00 46.37  ? 353  LEU A CD2 1 
ATOM   2620  N  N   . LYS A  1  328 ? -7.746  -15.909 14.801  1.00 52.75  ? 354  LYS A N   1 
ATOM   2621  C  CA  . LYS A  1  328 ? -8.437  -14.702 14.360  1.00 52.50  ? 354  LYS A CA  1 
ATOM   2622  C  C   . LYS A  1  328 ? -7.484  -13.578 14.028  1.00 51.80  ? 354  LYS A C   1 
ATOM   2623  O  O   . LYS A  1  328 ? -7.747  -12.810 13.113  1.00 51.78  ? 354  LYS A O   1 
ATOM   2624  C  CB  . LYS A  1  328 ? -9.424  -14.209 15.414  1.00 53.66  ? 354  LYS A CB  1 
ATOM   2625  C  CG  . LYS A  1  328 ? -10.733 -14.979 15.434  1.00 58.09  ? 354  LYS A CG  1 
ATOM   2626  C  CD  . LYS A  1  328 ? -11.789 -14.232 16.238  1.00 62.57  ? 354  LYS A CD  1 
ATOM   2627  C  CE  . LYS A  1  328 ? -13.025 -15.083 16.439  1.00 64.85  ? 354  LYS A CE  1 
ATOM   2628  N  NZ  . LYS A  1  328 ? -12.650 -16.386 17.087  1.00 66.80  ? 354  LYS A NZ  1 
ATOM   2629  N  N   . ARG A  1  329 ? -6.388  -13.477 14.776  1.00 52.32  ? 355  ARG A N   1 
ATOM   2630  C  CA  . ARG A  1  329 ? -5.374  -12.442 14.558  1.00 52.77  ? 355  ARG A CA  1 
ATOM   2631  C  C   . ARG A  1  329 ? -3.988  -13.073 14.428  1.00 52.38  ? 355  ARG A C   1 
ATOM   2632  O  O   . ARG A  1  329 ? -3.604  -13.925 15.233  1.00 53.25  ? 355  ARG A O   1 
ATOM   2633  C  CB  . ARG A  1  329 ? -5.333  -11.457 15.731  1.00 55.60  ? 355  ARG A CB  1 
ATOM   2634  C  CG  . ARG A  1  329 ? -6.685  -11.091 16.298  1.00 62.60  ? 355  ARG A CG  1 
ATOM   2635  C  CD  . ARG A  1  329 ? -6.593  -10.181 17.539  1.00 68.41  ? 355  ARG A CD  1 
ATOM   2636  N  NE  . ARG A  1  329 ? -6.284  -8.789  17.197  1.00 73.10  ? 355  ARG A NE  1 
ATOM   2637  C  CZ  . ARG A  1  329 ? -5.055  -8.299  17.042  1.00 75.41  ? 355  ARG A CZ  1 
ATOM   2638  N  NH1 . ARG A  1  329 ? -3.990  -9.087  17.205  1.00 76.25  ? 355  ARG A NH1 1 
ATOM   2639  N  NH2 . ARG A  1  329 ? -4.890  -7.017  16.721  1.00 74.97  ? 355  ARG A NH2 1 
ATOM   2640  N  N   . LEU A  1  330 ? -3.234  -12.652 13.418  1.00 50.99  ? 356  LEU A N   1 
ATOM   2641  C  CA  . LEU A  1  330 ? -1.877  -13.148 13.224  1.00 49.61  ? 356  LEU A CA  1 
ATOM   2642  C  C   . LEU A  1  330 ? -0.904  -11.986 13.076  1.00 50.06  ? 356  LEU A C   1 
ATOM   2643  O  O   . LEU A  1  330 ? -1.077  -11.130 12.199  1.00 50.32  ? 356  LEU A O   1 
ATOM   2644  C  CB  . LEU A  1  330 ? -1.784  -14.023 11.972  1.00 47.26  ? 356  LEU A CB  1 
ATOM   2645  C  CG  . LEU A  1  330 ? -0.363  -14.432 11.555  1.00 44.58  ? 356  LEU A CG  1 
ATOM   2646  C  CD1 . LEU A  1  330 ? 0.223   -15.364 12.604  1.00 41.89  ? 356  LEU A CD1 1 
ATOM   2647  C  CD2 . LEU A  1  330 ? -0.394  -15.082 10.189  1.00 41.10  ? 356  LEU A CD2 1 
ATOM   2648  N  N   . THR A  1  331 ? 0.102   -11.936 13.942  1.00 49.55  ? 357  THR A N   1 
ATOM   2649  C  CA  . THR A  1  331 ? 1.105   -10.885 13.828  1.00 51.21  ? 357  THR A CA  1 
ATOM   2650  C  C   . THR A  1  331 ? 2.441   -11.563 13.516  1.00 51.19  ? 357  THR A C   1 
ATOM   2651  O  O   . THR A  1  331 ? 3.040   -12.183 14.390  1.00 52.68  ? 357  THR A O   1 
ATOM   2652  C  CB  . THR A  1  331 ? 1.240   -10.071 15.121  1.00 51.98  ? 357  THR A CB  1 
ATOM   2653  O  OG1 . THR A  1  331 ? -0.051  -9.589  15.517  1.00 54.03  ? 357  THR A OG1 1 
ATOM   2654  C  CG2 . THR A  1  331 ? 2.177   -8.890  14.893  1.00 50.64  ? 357  THR A CG2 1 
ATOM   2655  N  N   . PHE A  1  332 ? 2.895   -11.447 12.269  1.00 50.40  ? 358  PHE A N   1 
ATOM   2656  C  CA  . PHE A  1  332 ? 4.150   -12.057 11.804  1.00 50.17  ? 358  PHE A CA  1 
ATOM   2657  C  C   . PHE A  1  332 ? 5.056   -10.939 11.315  1.00 50.16  ? 358  PHE A C   1 
ATOM   2658  O  O   . PHE A  1  332 ? 5.112   -10.673 10.112  1.00 49.56  ? 358  PHE A O   1 
ATOM   2659  C  CB  . PHE A  1  332 ? 3.848   -13.002 10.632  1.00 50.07  ? 358  PHE A CB  1 
ATOM   2660  C  CG  . PHE A  1  332 ? 4.999   -13.882 10.226  1.00 49.02  ? 358  PHE A CG  1 
ATOM   2661  C  CD1 . PHE A  1  332 ? 5.298   -15.038 10.943  1.00 48.73  ? 358  PHE A CD1 1 
ATOM   2662  C  CD2 . PHE A  1  332 ? 5.773   -13.562 9.123   1.00 47.96  ? 358  PHE A CD2 1 
ATOM   2663  C  CE1 . PHE A  1  332 ? 6.363   -15.868 10.562  1.00 49.02  ? 358  PHE A CE1 1 
ATOM   2664  C  CE2 . PHE A  1  332 ? 6.838   -14.382 8.737   1.00 48.49  ? 358  PHE A CE2 1 
ATOM   2665  C  CZ  . PHE A  1  332 ? 7.135   -15.538 9.457   1.00 47.72  ? 358  PHE A CZ  1 
ATOM   2666  N  N   . THR A  1  333 ? 5.772   -10.290 12.228  1.00 50.18  ? 359  THR A N   1 
ATOM   2667  C  CA  . THR A  1  333 ? 6.615   -9.172  11.824  1.00 50.68  ? 359  THR A CA  1 
ATOM   2668  C  C   . THR A  1  333 ? 8.085   -9.224  12.211  1.00 51.99  ? 359  THR A C   1 
ATOM   2669  O  O   . THR A  1  333 ? 8.500   -9.970  13.103  1.00 52.99  ? 359  THR A O   1 
ATOM   2670  C  CB  . THR A  1  333 ? 6.059   -7.817  12.357  1.00 49.82  ? 359  THR A CB  1 
ATOM   2671  O  OG1 . THR A  1  333 ? 6.485   -7.613  13.707  1.00 48.49  ? 359  THR A OG1 1 
ATOM   2672  C  CG2 . THR A  1  333 ? 4.555   -7.803  12.322  1.00 50.74  ? 359  THR A CG2 1 
ATOM   2673  N  N   . SER A  1  334 ? 8.861   -8.394  11.522  1.00 52.28  ? 360  SER A N   1 
ATOM   2674  C  CA  . SER A  1  334 ? 10.288  -8.258  11.760  1.00 52.55  ? 360  SER A CA  1 
ATOM   2675  C  C   . SER A  1  334 ? 11.044  -9.565  11.865  1.00 53.73  ? 360  SER A C   1 
ATOM   2676  O  O   . SER A  1  334 ? 11.934  -9.712  12.701  1.00 54.57  ? 360  SER A O   1 
ATOM   2677  C  CB  . SER A  1  334 ? 10.523  -7.438  13.024  1.00 50.84  ? 360  SER A CB  1 
ATOM   2678  O  OG  . SER A  1  334 ? 9.967   -6.149  12.881  1.00 50.99  ? 360  SER A OG  1 
ATOM   2679  N  N   . ASN A  1  335 ? 10.701  -10.513 11.010  1.00 55.13  ? 361  ASN A N   1 
ATOM   2680  C  CA  . ASN A  1  335 ? 11.374  -11.790 11.033  1.00 57.66  ? 361  ASN A CA  1 
ATOM   2681  C  C   . ASN A  1  335 ? 12.496  -11.850 10.019  1.00 59.38  ? 361  ASN A C   1 
ATOM   2682  O  O   . ASN A  1  335 ? 12.311  -11.549 8.851   1.00 60.39  ? 361  ASN A O   1 
ATOM   2683  C  CB  . ASN A  1  335 ? 10.378  -12.911 10.764  1.00 57.63  ? 361  ASN A CB  1 
ATOM   2684  C  CG  . ASN A  1  335 ? 9.315   -13.005 11.824  1.00 57.07  ? 361  ASN A CG  1 
ATOM   2685  O  OD1 . ASN A  1  335 ? 9.610   -13.150 13.013  1.00 54.21  ? 361  ASN A OD1 1 
ATOM   2686  N  ND2 . ASN A  1  335 ? 8.061   -12.925 11.398  1.00 58.31  ? 361  ASN A ND2 1 
ATOM   2687  N  N   . LYS A  1  336 ? 13.671  -12.243 10.486  1.00 62.40  ? 362  LYS A N   1 
ATOM   2688  C  CA  . LYS A  1  336 ? 14.826  -12.362 9.619   1.00 65.07  ? 362  LYS A CA  1 
ATOM   2689  C  C   . LYS A  1  336 ? 14.815  -13.775 9.059   1.00 64.99  ? 362  LYS A C   1 
ATOM   2690  O  O   . LYS A  1  336 ? 15.058  -14.734 9.783   1.00 66.15  ? 362  LYS A O   1 
ATOM   2691  C  CB  . LYS A  1  336 ? 16.117  -12.071 10.414  1.00 65.80  ? 362  LYS A CB  1 
ATOM   2692  C  CG  . LYS A  1  336 ? 16.079  -12.526 11.872  1.00 68.19  ? 362  LYS A CG  1 
ATOM   2693  C  CD  . LYS A  1  336 ? 17.232  -11.945 12.690  1.00 70.64  ? 362  LYS A CD  1 
ATOM   2694  C  CE  . LYS A  1  336 ? 17.268  -12.492 14.137  1.00 71.73  ? 362  LYS A CE  1 
ATOM   2695  N  NZ  . LYS A  1  336 ? 17.642  -13.947 14.237  1.00 71.55  ? 362  LYS A NZ  1 
ATOM   2696  N  N   . GLY A  1  337 ? 14.508  -13.915 7.778   1.00 65.01  ? 363  GLY A N   1 
ATOM   2697  C  CA  . GLY A  1  337 ? 14.484  -15.246 7.208   1.00 67.32  ? 363  GLY A CA  1 
ATOM   2698  C  C   . GLY A  1  337 ? 14.504  -15.293 5.696   1.00 68.79  ? 363  GLY A C   1 
ATOM   2699  O  O   . GLY A  1  337 ? 15.395  -14.752 5.051   1.00 68.14  ? 363  GLY A O   1 
ATOM   2700  N  N   . GLY A  1  338 ? 13.509  -15.966 5.134   1.00 71.14  ? 364  GLY A N   1 
ATOM   2701  C  CA  . GLY A  1  338 ? 13.406  -16.086 3.695   1.00 72.88  ? 364  GLY A CA  1 
ATOM   2702  C  C   . GLY A  1  338 ? 12.929  -14.797 3.066   1.00 73.22  ? 364  GLY A C   1 
ATOM   2703  O  O   . GLY A  1  338 ? 12.993  -13.730 3.683   1.00 73.84  ? 364  GLY A O   1 
ATOM   2704  N  N   . ASN A  1  339 ? 12.455  -14.898 1.833   1.00 72.94  ? 365  ASN A N   1 
ATOM   2705  C  CA  . ASN A  1  339 ? 11.972  -13.733 1.116   1.00 72.66  ? 365  ASN A CA  1 
ATOM   2706  C  C   . ASN A  1  339 ? 10.829  -14.100 0.195   1.00 70.65  ? 365  ASN A C   1 
ATOM   2707  O  O   . ASN A  1  339 ? 10.549  -13.364 -0.757  1.00 72.21  ? 365  ASN A O   1 
ATOM   2708  C  CB  . ASN A  1  339 ? 13.103  -13.083 0.286   1.00 75.29  ? 365  ASN A CB  1 
ATOM   2709  C  CG  . ASN A  1  339 ? 13.675  -14.018 -0.789  1.00 76.71  ? 365  ASN A CG  1 
ATOM   2710  O  OD1 . ASN A  1  339 ? 14.485  -14.902 -0.491  1.00 77.11  ? 365  ASN A OD1 1 
ATOM   2711  N  ND2 . ASN A  1  339 ? 13.249  -13.821 -2.042  1.00 74.82  ? 365  ASN A ND2 1 
ATOM   2712  N  N   . ALA A  1  340 ? 10.178  -15.233 0.458   1.00 66.71  ? 366  ALA A N   1 
ATOM   2713  C  CA  . ALA A  1  340 ? 9.068   -15.652 -0.386  1.00 62.22  ? 366  ALA A CA  1 
ATOM   2714  C  C   . ALA A  1  340 ? 7.890   -16.168 0.405   1.00 59.83  ? 366  ALA A C   1 
ATOM   2715  O  O   . ALA A  1  340 ? 7.987   -17.156 1.121   1.00 59.01  ? 366  ALA A O   1 
ATOM   2716  C  CB  . ALA A  1  340 ? 9.520   -16.690 -1.372  1.00 61.60  ? 366  ALA A CB  1 
ATOM   2717  N  N   . PHE A  1  341 ? 6.775   -15.464 0.260   1.00 57.52  ? 367  PHE A N   1 
ATOM   2718  C  CA  . PHE A  1  341 ? 5.524   -15.793 0.915   1.00 55.09  ? 367  PHE A CA  1 
ATOM   2719  C  C   . PHE A  1  341 ? 4.860   -16.904 0.124   1.00 55.48  ? 367  PHE A C   1 
ATOM   2720  O  O   . PHE A  1  341 ? 5.027   -17.003 -1.089  1.00 55.28  ? 367  PHE A O   1 
ATOM   2721  C  CB  . PHE A  1  341 ? 4.615   -14.556 0.919   1.00 52.73  ? 367  PHE A CB  1 
ATOM   2722  C  CG  . PHE A  1  341 ? 3.188   -14.822 1.359   1.00 49.31  ? 367  PHE A CG  1 
ATOM   2723  C  CD1 . PHE A  1  341 ? 2.856   -14.870 2.712   1.00 47.56  ? 367  PHE A CD1 1 
ATOM   2724  C  CD2 . PHE A  1  341 ? 2.175   -15.025 0.409   1.00 46.97  ? 367  PHE A CD2 1 
ATOM   2725  C  CE1 . PHE A  1  341 ? 1.536   -15.112 3.122   1.00 44.96  ? 367  PHE A CE1 1 
ATOM   2726  C  CE2 . PHE A  1  341 ? 0.863   -15.266 0.799   1.00 45.32  ? 367  PHE A CE2 1 
ATOM   2727  C  CZ  . PHE A  1  341 ? 0.541   -15.312 2.167   1.00 46.52  ? 367  PHE A CZ  1 
ATOM   2728  N  N   . SER A  1  342 ? 4.120   -17.750 0.821   1.00 56.36  ? 368  SER A N   1 
ATOM   2729  C  CA  . SER A  1  342 ? 3.389   -18.821 0.180   1.00 58.22  ? 368  SER A CA  1 
ATOM   2730  C  C   . SER A  1  342 ? 2.042   -18.810 0.883   1.00 59.66  ? 368  SER A C   1 
ATOM   2731  O  O   . SER A  1  342 ? 1.920   -18.279 1.985   1.00 59.17  ? 368  SER A O   1 
ATOM   2732  C  CB  . SER A  1  342 ? 4.099   -20.164 0.374   1.00 59.83  ? 368  SER A CB  1 
ATOM   2733  O  OG  . SER A  1  342 ? 4.128   -20.562 1.737   1.00 61.42  ? 368  SER A OG  1 
ATOM   2734  N  N   . GLU A  1  343 ? 1.032   -19.381 0.242   1.00 61.89  ? 369  GLU A N   1 
ATOM   2735  C  CA  . GLU A  1  343 ? -0.311  -19.419 0.799   1.00 63.36  ? 369  GLU A CA  1 
ATOM   2736  C  C   . GLU A  1  343 ? -0.395  -19.966 2.206   1.00 61.81  ? 369  GLU A C   1 
ATOM   2737  O  O   . GLU A  1  343 ? 0.370   -20.840 2.609   1.00 61.30  ? 369  GLU A O   1 
ATOM   2738  C  CB  . GLU A  1  343 ? -1.231  -20.286 -0.058  1.00 68.41  ? 369  GLU A CB  1 
ATOM   2739  C  CG  . GLU A  1  343 ? -1.171  -20.061 -1.555  1.00 76.71  ? 369  GLU A CG  1 
ATOM   2740  C  CD  . GLU A  1  343 ? -2.163  -20.950 -2.308  1.00 81.20  ? 369  GLU A CD  1 
ATOM   2741  O  OE1 . GLU A  1  343 ? -2.236  -22.168 -1.997  1.00 82.19  ? 369  GLU A OE1 1 
ATOM   2742  O  OE2 . GLU A  1  343 ? -2.864  -20.427 -3.212  1.00 83.74  ? 369  GLU A OE2 1 
ATOM   2743  N  N   . VAL A  1  344 ? -1.357  -19.438 2.946   1.00 60.71  ? 370  VAL A N   1 
ATOM   2744  C  CA  . VAL A  1  344 ? -1.643  -19.910 4.289   1.00 59.50  ? 370  VAL A CA  1 
ATOM   2745  C  C   . VAL A  1  344 ? -3.131  -20.238 4.215   1.00 58.36  ? 370  VAL A C   1 
ATOM   2746  O  O   . VAL A  1  344 ? -3.811  -19.872 3.258   1.00 56.43  ? 370  VAL A O   1 
ATOM   2747  C  CB  . VAL A  1  344 ? -1.391  -18.833 5.373   1.00 59.50  ? 370  VAL A CB  1 
ATOM   2748  C  CG1 . VAL A  1  344 ? 0.084   -18.489 5.422   1.00 58.56  ? 370  VAL A CG1 1 
ATOM   2749  C  CG2 . VAL A  1  344 ? -2.219  -17.597 5.096   1.00 59.05  ? 370  VAL A CG2 1 
ATOM   2750  N  N   . ASP A  1  345 ? -3.646  -20.938 5.207   1.00 58.26  ? 371  ASP A N   1 
ATOM   2751  C  CA  . ASP A  1  345 ? -5.057  -21.280 5.174   1.00 59.14  ? 371  ASP A CA  1 
ATOM   2752  C  C   . ASP A  1  345 ? -5.688  -21.058 6.530   1.00 56.91  ? 371  ASP A C   1 
ATOM   2753  O  O   . ASP A  1  345 ? -5.843  -21.987 7.325   1.00 57.00  ? 371  ASP A O   1 
ATOM   2754  C  CB  . ASP A  1  345 ? -5.230  -22.728 4.732   1.00 63.36  ? 371  ASP A CB  1 
ATOM   2755  C  CG  . ASP A  1  345 ? -6.657  -23.195 4.845   1.00 66.92  ? 371  ASP A CG  1 
ATOM   2756  O  OD1 . ASP A  1  345 ? -7.571  -22.392 4.527   1.00 68.99  ? 371  ASP A OD1 1 
ATOM   2757  O  OD2 . ASP A  1  345 ? -6.858  -24.364 5.244   1.00 68.77  ? 371  ASP A OD2 1 
ATOM   2758  N  N   . LEU A  1  346 ? -6.068  -19.810 6.768   1.00 54.73  ? 372  LEU A N   1 
ATOM   2759  C  CA  . LEU A  1  346 ? -6.639  -19.388 8.037   1.00 53.06  ? 372  LEU A CA  1 
ATOM   2760  C  C   . LEU A  1  346 ? -8.091  -18.922 7.909   1.00 53.45  ? 372  LEU A C   1 
ATOM   2761  O  O   . LEU A  1  346 ? -8.371  -17.720 7.964   1.00 52.37  ? 372  LEU A O   1 
ATOM   2762  C  CB  . LEU A  1  346 ? -5.755  -18.274 8.601   1.00 50.05  ? 372  LEU A CB  1 
ATOM   2763  C  CG  . LEU A  1  346 ? -4.271  -18.675 8.523   1.00 48.06  ? 372  LEU A CG  1 
ATOM   2764  C  CD1 . LEU A  1  346 ? -3.353  -17.566 8.998   1.00 46.82  ? 372  LEU A CD1 1 
ATOM   2765  C  CD2 . LEU A  1  346 ? -4.066  -19.933 9.346   1.00 46.06  ? 372  LEU A CD2 1 
ATOM   2766  N  N   . PRO A  1  347 ? -9.037  -19.884 7.789   1.00 53.91  ? 373  PRO A N   1 
ATOM   2767  C  CA  . PRO A  1  347 ? -10.478 -19.643 7.645   1.00 53.07  ? 373  PRO A CA  1 
ATOM   2768  C  C   . PRO A  1  347 ? -11.109 -18.650 8.611   1.00 53.05  ? 373  PRO A C   1 
ATOM   2769  O  O   . PRO A  1  347 ? -12.094 -18.003 8.262   1.00 53.50  ? 373  PRO A O   1 
ATOM   2770  C  CB  . PRO A  1  347 ? -11.075 -21.039 7.789   1.00 51.92  ? 373  PRO A CB  1 
ATOM   2771  C  CG  . PRO A  1  347 ? -10.104 -21.727 8.696   1.00 52.91  ? 373  PRO A CG  1 
ATOM   2772  C  CD  . PRO A  1  347 ? -8.796  -21.311 8.082   1.00 54.04  ? 373  PRO A CD  1 
ATOM   2773  N  N   . SER A  1  348 ? -10.548 -18.528 9.814   1.00 52.74  ? 374  SER A N   1 
ATOM   2774  C  CA  . SER A  1  348 ? -11.089 -17.612 10.823  1.00 52.10  ? 374  SER A CA  1 
ATOM   2775  C  C   . SER A  1  348 ? -10.370 -16.268 10.942  1.00 51.28  ? 374  SER A C   1 
ATOM   2776  O  O   . SER A  1  348 ? -10.795 -15.401 11.702  1.00 50.25  ? 374  SER A O   1 
ATOM   2777  C  CB  . SER A  1  348 ? -11.085 -18.276 12.206  1.00 51.43  ? 374  SER A CB  1 
ATOM   2778  O  OG  . SER A  1  348 ? -12.039 -19.319 12.296  1.00 50.09  ? 374  SER A OG  1 
ATOM   2779  N  N   . LEU A  1  349 ? -9.298  -16.093 10.183  1.00 51.02  ? 375  LEU A N   1 
ATOM   2780  C  CA  . LEU A  1  349 ? -8.505  -14.876 10.249  1.00 52.67  ? 375  LEU A CA  1 
ATOM   2781  C  C   . LEU A  1  349 ? -9.237  -13.550 9.998   1.00 54.35  ? 375  LEU A C   1 
ATOM   2782  O  O   . LEU A  1  349 ? -9.982  -13.421 9.030   1.00 55.40  ? 375  LEU A O   1 
ATOM   2783  C  CB  . LEU A  1  349 ? -7.340  -14.996 9.272   1.00 51.69  ? 375  LEU A CB  1 
ATOM   2784  C  CG  . LEU A  1  349 ? -6.226  -13.974 9.471   1.00 49.98  ? 375  LEU A CG  1 
ATOM   2785  C  CD1 . LEU A  1  349 ? -5.580  -14.236 10.822  1.00 49.05  ? 375  LEU A CD1 1 
ATOM   2786  C  CD2 . LEU A  1  349 ? -5.214  -14.092 8.345   1.00 49.37  ? 375  LEU A CD2 1 
ATOM   2787  N  N   . GLU A  1  350 ? -9.011  -12.563 10.868  1.00 55.36  ? 376  GLU A N   1 
ATOM   2788  C  CA  . GLU A  1  350 ? -9.622  -11.240 10.712  1.00 56.11  ? 376  GLU A CA  1 
ATOM   2789  C  C   . GLU A  1  350 ? -8.552  -10.142 10.732  1.00 55.14  ? 376  GLU A C   1 
ATOM   2790  O  O   . GLU A  1  350 ? -8.665  -9.139  10.033  1.00 55.03  ? 376  GLU A O   1 
ATOM   2791  C  CB  . GLU A  1  350 ? -10.637 -10.967 11.821  1.00 58.22  ? 376  GLU A CB  1 
ATOM   2792  C  CG  . GLU A  1  350 ? -11.797 -11.924 11.858  1.00 65.96  ? 376  GLU A CG  1 
ATOM   2793  C  CD  . GLU A  1  350 ? -12.784 -11.616 12.988  1.00 71.37  ? 376  GLU A CD  1 
ATOM   2794  O  OE1 . GLU A  1  350 ? -13.417 -12.579 13.505  1.00 72.82  ? 376  GLU A OE1 1 
ATOM   2795  O  OE2 . GLU A  1  350 ? -12.928 -10.419 13.351  1.00 74.04  ? 376  GLU A OE2 1 
ATOM   2796  N  N   . PHE A  1  351 ? -7.516  -10.334 11.537  1.00 53.19  ? 377  PHE A N   1 
ATOM   2797  C  CA  . PHE A  1  351 ? -6.437  -9.361  11.632  1.00 52.41  ? 377  PHE A CA  1 
ATOM   2798  C  C   . PHE A  1  351 ? -5.180  -9.996  11.039  1.00 52.37  ? 377  PHE A C   1 
ATOM   2799  O  O   . PHE A  1  351 ? -4.807  -11.106 11.428  1.00 53.80  ? 377  PHE A O   1 
ATOM   2800  C  CB  . PHE A  1  351 ? -6.179  -8.994  13.091  1.00 53.57  ? 377  PHE A CB  1 
ATOM   2801  C  CG  . PHE A  1  351 ? -5.151  -7.909  13.266  1.00 55.93  ? 377  PHE A CG  1 
ATOM   2802  C  CD1 . PHE A  1  351 ? -5.528  -6.572  13.264  1.00 55.85  ? 377  PHE A CD1 1 
ATOM   2803  C  CD2 . PHE A  1  351 ? -3.794  -8.221  13.387  1.00 56.63  ? 377  PHE A CD2 1 
ATOM   2804  C  CE1 . PHE A  1  351 ? -4.570  -5.564  13.381  1.00 55.43  ? 377  PHE A CE1 1 
ATOM   2805  C  CE2 . PHE A  1  351 ? -2.830  -7.213  13.503  1.00 55.09  ? 377  PHE A CE2 1 
ATOM   2806  C  CZ  . PHE A  1  351 ? -3.223  -5.887  13.497  1.00 54.59  ? 377  PHE A CZ  1 
ATOM   2807  N  N   . LEU A  1  352 ? -4.515  -9.322  10.106  1.00 50.64  ? 378  LEU A N   1 
ATOM   2808  C  CA  . LEU A  1  352 ? -3.329  -9.921  9.518   1.00 49.26  ? 378  LEU A CA  1 
ATOM   2809  C  C   . LEU A  1  352 ? -2.202  -8.940  9.323   1.00 49.06  ? 378  LEU A C   1 
ATOM   2810  O  O   . LEU A  1  352 ? -2.220  -8.142  8.384   1.00 47.86  ? 378  LEU A O   1 
ATOM   2811  C  CB  . LEU A  1  352 ? -3.655  -10.560 8.156   1.00 49.11  ? 378  LEU A CB  1 
ATOM   2812  C  CG  . LEU A  1  352 ? -2.855  -11.779 7.631   1.00 49.09  ? 378  LEU A CG  1 
ATOM   2813  C  CD1 . LEU A  1  352 ? -2.862  -11.722 6.115   1.00 48.07  ? 378  LEU A CD1 1 
ATOM   2814  C  CD2 . LEU A  1  352 ? -1.413  -11.813 8.123   1.00 48.66  ? 378  LEU A CD2 1 
ATOM   2815  N  N   . ASP A  1  353 ? -1.218  -8.997  10.214  1.00 50.00  ? 379  ASP A N   1 
ATOM   2816  C  CA  . ASP A  1  353 ? -0.048  -8.141  10.078  1.00 51.48  ? 379  ASP A CA  1 
ATOM   2817  C  C   . ASP A  1  353 ? 1.110   -9.036  9.668   1.00 50.69  ? 379  ASP A C   1 
ATOM   2818  O  O   . ASP A  1  353 ? 1.489   -9.960  10.388  1.00 49.57  ? 379  ASP A O   1 
ATOM   2819  C  CB  . ASP A  1  353 ? 0.293   -7.412  11.382  1.00 54.17  ? 379  ASP A CB  1 
ATOM   2820  C  CG  . ASP A  1  353 ? 1.526   -6.501  11.237  1.00 56.98  ? 379  ASP A CG  1 
ATOM   2821  O  OD1 . ASP A  1  353 ? 1.743   -5.653  12.140  1.00 58.21  ? 379  ASP A OD1 1 
ATOM   2822  O  OD2 . ASP A  1  353 ? 2.275   -6.639  10.224  1.00 54.95  ? 379  ASP A OD2 1 
ATOM   2823  N  N   . LEU A  1  354 ? 1.661   -8.737  8.500   1.00 49.51  ? 380  LEU A N   1 
ATOM   2824  C  CA  . LEU A  1  354 ? 2.747   -9.495  7.914   1.00 49.00  ? 380  LEU A CA  1 
ATOM   2825  C  C   . LEU A  1  354 ? 3.786   -8.487  7.447   1.00 50.29  ? 380  LEU A C   1 
ATOM   2826  O  O   . LEU A  1  354 ? 4.473   -8.697  6.446   1.00 50.59  ? 380  LEU A O   1 
ATOM   2827  C  CB  . LEU A  1  354 ? 2.193   -10.235 6.717   1.00 47.01  ? 380  LEU A CB  1 
ATOM   2828  C  CG  . LEU A  1  354 ? 2.485   -11.701 6.478   1.00 47.65  ? 380  LEU A CG  1 
ATOM   2829  C  CD1 . LEU A  1  354 ? 1.964   -12.526 7.620   1.00 47.22  ? 380  LEU A CD1 1 
ATOM   2830  C  CD2 . LEU A  1  354 ? 1.802   -12.124 5.183   1.00 49.34  ? 380  LEU A CD2 1 
ATOM   2831  N  N   . SER A  1  355 ? 3.901   -7.390  8.181   1.00 50.47  ? 381  SER A N   1 
ATOM   2832  C  CA  . SER A  1  355 ? 4.820   -6.326  7.807   1.00 50.98  ? 381  SER A CA  1 
ATOM   2833  C  C   . SER A  1  355 ? 6.269   -6.507  8.236   1.00 49.76  ? 381  SER A C   1 
ATOM   2834  O  O   . SER A  1  355 ? 6.562   -7.259  9.160   1.00 50.11  ? 381  SER A O   1 
ATOM   2835  C  CB  . SER A  1  355 ? 4.307   -5.015  8.385   1.00 52.80  ? 381  SER A CB  1 
ATOM   2836  O  OG  . SER A  1  355 ? 4.389   -5.048  9.805   1.00 55.37  ? 381  SER A OG  1 
ATOM   2837  N  N   . ARG A  1  356 ? 7.162   -5.795  7.554   1.00 47.99  ? 382  ARG A N   1 
ATOM   2838  C  CA  . ARG A  1  356 ? 8.591   -5.799  7.862   1.00 46.72  ? 382  ARG A CA  1 
ATOM   2839  C  C   . ARG A  1  356 ? 9.308   -7.136  7.796   1.00 45.52  ? 382  ARG A C   1 
ATOM   2840  O  O   . ARG A  1  356 ? 10.110  -7.446  8.667   1.00 43.86  ? 382  ARG A O   1 
ATOM   2841  C  CB  . ARG A  1  356 ? 8.809   -5.203  9.248   1.00 47.63  ? 382  ARG A CB  1 
ATOM   2842  C  CG  . ARG A  1  356 ? 8.130   -3.861  9.442   1.00 51.77  ? 382  ARG A CG  1 
ATOM   2843  C  CD  . ARG A  1  356 ? 8.439   -3.258  10.805  1.00 54.76  ? 382  ARG A CD  1 
ATOM   2844  N  NE  . ARG A  1  356 ? 8.272   -1.803  10.797  1.00 57.74  ? 382  ARG A NE  1 
ATOM   2845  C  CZ  . ARG A  1  356 ? 7.097   -1.179  10.736  1.00 58.75  ? 382  ARG A CZ  1 
ATOM   2846  N  NH1 . ARG A  1  356 ? 5.963   -1.874  10.680  1.00 58.56  ? 382  ARG A NH1 1 
ATOM   2847  N  NH2 . ARG A  1  356 ? 7.055   0.147   10.731  1.00 58.65  ? 382  ARG A NH2 1 
ATOM   2848  N  N   . ASN A  1  357 ? 9.043   -7.920  6.760   1.00 44.90  ? 383  ASN A N   1 
ATOM   2849  C  CA  . ASN A  1  357 ? 9.680   -9.217  6.640   1.00 44.33  ? 383  ASN A CA  1 
ATOM   2850  C  C   . ASN A  1  357 ? 10.484  -9.328  5.373   1.00 46.29  ? 383  ASN A C   1 
ATOM   2851  O  O   . ASN A  1  357 ? 11.119  -10.359 5.149   1.00 50.64  ? 383  ASN A O   1 
ATOM   2852  C  CB  . ASN A  1  357 ? 8.642   -10.343 6.639   1.00 42.16  ? 383  ASN A CB  1 
ATOM   2853  C  CG  . ASN A  1  357 ? 7.919   -10.488 7.961   1.00 42.57  ? 383  ASN A CG  1 
ATOM   2854  O  OD1 . ASN A  1  357 ? 8.511   -10.836 8.983   1.00 40.26  ? 383  ASN A OD1 1 
ATOM   2855  N  ND2 . ASN A  1  357 ? 6.622   -10.230 7.944   1.00 42.08  ? 383  ASN A ND2 1 
ATOM   2856  N  N   . GLY A  1  358 ? 10.452  -8.299  4.532   1.00 45.15  ? 384  GLY A N   1 
ATOM   2857  C  CA  . GLY A  1  358 ? 11.199  -8.358  3.290   1.00 44.48  ? 384  GLY A CA  1 
ATOM   2858  C  C   . GLY A  1  358 ? 10.622  -9.391  2.349   1.00 45.78  ? 384  GLY A C   1 
ATOM   2859  O  O   . GLY A  1  358 ? 11.259  -9.778  1.376   1.00 47.73  ? 384  GLY A O   1 
ATOM   2860  N  N   . LEU A  1  359 ? 9.405   -9.835  2.637   1.00 47.11  ? 385  LEU A N   1 
ATOM   2861  C  CA  . LEU A  1  359 ? 8.712   -10.840 1.826   1.00 48.43  ? 385  LEU A CA  1 
ATOM   2862  C  C   . LEU A  1  359 ? 8.307   -10.361 0.432   1.00 49.03  ? 385  LEU A C   1 
ATOM   2863  O  O   . LEU A  1  359 ? 8.094   -9.174  0.209   1.00 49.76  ? 385  LEU A O   1 
ATOM   2864  C  CB  . LEU A  1  359 ? 7.451   -11.313 2.552   1.00 48.49  ? 385  LEU A CB  1 
ATOM   2865  C  CG  . LEU A  1  359 ? 7.678   -12.041 3.880   1.00 51.78  ? 385  LEU A CG  1 
ATOM   2866  C  CD1 . LEU A  1  359 ? 6.335   -12.401 4.525   1.00 52.28  ? 385  LEU A CD1 1 
ATOM   2867  C  CD2 . LEU A  1  359 ? 8.508   -13.299 3.630   1.00 52.55  ? 385  LEU A CD2 1 
ATOM   2868  N  N   . SER A  1  360 ? 8.191   -11.301 -0.502  1.00 49.12  ? 386  SER A N   1 
ATOM   2869  C  CA  . SER A  1  360 ? 7.766   -10.995 -1.861  1.00 48.95  ? 386  SER A CA  1 
ATOM   2870  C  C   . SER A  1  360 ? 6.582   -11.875 -2.227  1.00 50.11  ? 386  SER A C   1 
ATOM   2871  O  O   . SER A  1  360 ? 6.635   -13.085 -2.066  1.00 50.03  ? 386  SER A O   1 
ATOM   2872  C  CB  . SER A  1  360 ? 8.899   -11.229 -2.843  1.00 49.12  ? 386  SER A CB  1 
ATOM   2873  O  OG  . SER A  1  360 ? 9.942   -10.289 -2.641  1.00 51.55  ? 386  SER A OG  1 
ATOM   2874  N  N   . PHE A  1  361 ? 5.507   -11.250 -2.701  1.00 51.64  ? 387  PHE A N   1 
ATOM   2875  C  CA  . PHE A  1  361 ? 4.288   -11.948 -3.089  1.00 52.49  ? 387  PHE A CA  1 
ATOM   2876  C  C   . PHE A  1  361 ? 4.228   -11.947 -4.602  1.00 54.86  ? 387  PHE A C   1 
ATOM   2877  O  O   . PHE A  1  361 ? 4.376   -10.895 -5.208  1.00 56.54  ? 387  PHE A O   1 
ATOM   2878  C  CB  . PHE A  1  361 ? 3.090   -11.208 -2.522  1.00 51.98  ? 387  PHE A CB  1 
ATOM   2879  C  CG  . PHE A  1  361 ? 3.115   -11.097 -1.032  1.00 54.17  ? 387  PHE A CG  1 
ATOM   2880  C  CD1 . PHE A  1  361 ? 2.088   -11.634 -0.270  1.00 54.40  ? 387  PHE A CD1 1 
ATOM   2881  C  CD2 . PHE A  1  361 ? 4.187   -10.479 -0.382  1.00 56.21  ? 387  PHE A CD2 1 
ATOM   2882  C  CE1 . PHE A  1  361 ? 2.123   -11.568 1.127   1.00 56.70  ? 387  PHE A CE1 1 
ATOM   2883  C  CE2 . PHE A  1  361 ? 4.245   -10.403 1.019   1.00 57.51  ? 387  PHE A CE2 1 
ATOM   2884  C  CZ  . PHE A  1  361 ? 3.205   -10.950 1.778   1.00 58.19  ? 387  PHE A CZ  1 
ATOM   2885  N  N   . LYS A  1  362 ? 4.010   -13.101 -5.226  1.00 56.51  ? 388  LYS A N   1 
ATOM   2886  C  CA  . LYS A  1  362 ? 3.977   -13.121 -6.680  1.00 59.15  ? 388  LYS A CA  1 
ATOM   2887  C  C   . LYS A  1  362 ? 2.584   -12.922 -7.313  1.00 60.44  ? 388  LYS A C   1 
ATOM   2888  O  O   . LYS A  1  362 ? 2.461   -12.878 -8.543  1.00 62.14  ? 388  LYS A O   1 
ATOM   2889  C  CB  . LYS A  1  362 ? 4.648   -14.398 -7.213  1.00 59.93  ? 388  LYS A CB  1 
ATOM   2890  C  CG  . LYS A  1  362 ? 3.750   -15.636 -7.298  1.00 65.08  ? 388  LYS A CG  1 
ATOM   2891  C  CD  . LYS A  1  362 ? 4.403   -16.770 -8.116  1.00 66.57  ? 388  LYS A CD  1 
ATOM   2892  C  CE  . LYS A  1  362 ? 5.529   -17.463 -7.349  1.00 68.78  ? 388  LYS A CE  1 
ATOM   2893  N  NZ  . LYS A  1  362 ? 5.009   -18.430 -6.325  1.00 69.39  ? 388  LYS A NZ  1 
ATOM   2894  N  N   . GLY A  1  363 ? 1.540   -12.785 -6.496  1.00 60.24  ? 389  GLY A N   1 
ATOM   2895  C  CA  . GLY A  1  363 ? 0.212   -12.556 -7.054  1.00 60.46  ? 389  GLY A CA  1 
ATOM   2896  C  C   . GLY A  1  363 ? -0.780  -11.991 -6.044  1.00 61.88  ? 389  GLY A C   1 
ATOM   2897  O  O   . GLY A  1  363 ? -1.355  -12.797 -5.301  1.00 64.55  ? 389  GLY A O   1 
ATOM   2898  N  N   . CYS A  1  364 ? -1.028  -10.652 -6.010  1.00 64.87  ? 390  CYS A N   1 
ATOM   2899  C  CA  . CYS A  1  364 ? -1.962  -10.162 -5.003  1.00 63.54  ? 390  CYS A CA  1 
ATOM   2900  C  C   . CYS A  1  364 ? -3.230  -9.774  -5.771  1.00 62.34  ? 390  CYS A C   1 
ATOM   2901  O  O   . CYS A  1  364 ? -3.129  -9.455  -6.952  1.00 62.21  ? 390  CYS A O   1 
ATOM   2902  C  CB  . CYS A  1  364 ? -1.347  -8.936  -4.323  1.00 63.07  ? 390  CYS A CB  1 
ATOM   2903  S  SG  . CYS A  1  364 ? -2.040  -8.467  -2.727  1.00 71.68  ? 390  CYS A SG  1 
ATOM   2904  N  N   . CYS A  1  365 ? -4.427  -9.817  -5.178  1.00 60.54  ? 391  CYS A N   1 
ATOM   2905  C  CA  . CYS A  1  365 ? -4.726  -10.287 -3.830  1.00 60.37  ? 391  CYS A CA  1 
ATOM   2906  C  C   . CYS A  1  365 ? -6.024  -11.064 -3.948  1.00 58.85  ? 391  CYS A C   1 
ATOM   2907  O  O   . CYS A  1  365 ? -6.931  -10.652 -4.668  1.00 58.24  ? 391  CYS A O   1 
ATOM   2908  C  CB  . CYS A  1  365 ? -4.951  -9.106  -2.885  1.00 61.95  ? 391  CYS A CB  1 
ATOM   2909  S  SG  . CYS A  1  365 ? -3.860  -7.708  -3.194  1.00 72.33  ? 391  CYS A SG  1 
ATOM   2910  N  N   . SER A  1  366 ? -6.068  -12.212 -3.260  1.00 66.35  ? 392  SER A N   1 
ATOM   2911  C  CA  . SER A  1  366 ? -7.223  -13.095 -3.324  1.00 67.72  ? 392  SER A CA  1 
ATOM   2912  C  C   . SER A  1  366 ? -7.442  -13.793 -1.997  1.00 67.70  ? 392  SER A C   1 
ATOM   2913  O  O   . SER A  1  366 ? -6.590  -13.743 -1.122  1.00 68.52  ? 392  SER A O   1 
ATOM   2914  C  CB  . SER A  1  366 ? -7.008  -14.137 -4.429  1.00 68.38  ? 392  SER A CB  1 
ATOM   2915  O  OG  . SER A  1  366 ? -8.199  -14.846 -4.722  1.00 70.96  ? 392  SER A OG  1 
ATOM   2916  N  N   . GLN A  1  367 ? -8.584  -14.447 -1.848  1.00 68.27  ? 393  GLN A N   1 
ATOM   2917  C  CA  . GLN A  1  367 ? -8.888  -15.130 -0.606  1.00 69.37  ? 393  GLN A CA  1 
ATOM   2918  C  C   . GLN A  1  367 ? -8.110  -16.425 -0.515  1.00 68.96  ? 393  GLN A C   1 
ATOM   2919  O  O   . GLN A  1  367 ? -7.946  -16.985 0.567   1.00 69.27  ? 393  GLN A O   1 
ATOM   2920  C  CB  . GLN A  1  367 ? -10.379 -15.435 -0.518  1.00 71.37  ? 393  GLN A CB  1 
ATOM   2921  C  CG  . GLN A  1  367 ? -10.807 -16.623 -1.338  1.00 73.64  ? 393  GLN A CG  1 
ATOM   2922  C  CD  . GLN A  1  367 ? -11.942 -17.357 -0.680  1.00 75.85  ? 393  GLN A CD  1 
ATOM   2923  O  OE1 . GLN A  1  367 ? -13.104 -16.949 -0.781  1.00 76.59  ? 393  GLN A OE1 1 
ATOM   2924  N  NE2 . GLN A  1  367 ? -11.611 -18.443 0.031   1.00 75.57  ? 393  GLN A NE2 1 
ATOM   2925  N  N   . SER A  1  368 ? -7.637  -16.890 -1.666  1.00 68.57  ? 394  SER A N   1 
ATOM   2926  C  CA  . SER A  1  368 ? -6.874  -18.129 -1.770  1.00 67.99  ? 394  SER A CA  1 
ATOM   2927  C  C   . SER A  1  368 ? -5.441  -17.967 -1.246  1.00 67.20  ? 394  SER A C   1 
ATOM   2928  O  O   . SER A  1  368 ? -4.700  -18.945 -1.094  1.00 66.52  ? 394  SER A O   1 
ATOM   2929  C  CB  . SER A  1  368 ? -6.853  -18.579 -3.227  1.00 68.18  ? 394  SER A CB  1 
ATOM   2930  O  OG  . SER A  1  368 ? -6.405  -17.520 -4.061  1.00 68.53  ? 394  SER A OG  1 
ATOM   2931  N  N   . ASP A  1  369 ? -5.056  -16.727 -0.964  1.00 66.02  ? 395  ASP A N   1 
ATOM   2932  C  CA  . ASP A  1  369 ? -3.725  -16.449 -0.450  1.00 65.07  ? 395  ASP A CA  1 
ATOM   2933  C  C   . ASP A  1  369 ? -3.673  -16.622 1.050   1.00 63.88  ? 395  ASP A C   1 
ATOM   2934  O  O   . ASP A  1  369 ? -2.660  -17.056 1.604   1.00 63.34  ? 395  ASP A O   1 
ATOM   2935  C  CB  . ASP A  1  369 ? -3.306  -15.023 -0.801  1.00 65.86  ? 395  ASP A CB  1 
ATOM   2936  C  CG  . ASP A  1  369 ? -2.993  -14.862 -2.269  1.00 67.91  ? 395  ASP A CG  1 
ATOM   2937  O  OD1 . ASP A  1  369 ? -3.913  -15.014 -3.097  1.00 70.76  ? 395  ASP A OD1 1 
ATOM   2938  O  OD2 . ASP A  1  369 ? -1.822  -14.601 -2.602  1.00 68.66  ? 395  ASP A OD2 1 
ATOM   2939  N  N   . PHE A  1  370 ? -4.786  -16.289 1.697   1.00 62.50  ? 396  PHE A N   1 
ATOM   2940  C  CA  . PHE A  1  370 ? -4.897  -16.366 3.140   1.00 60.38  ? 396  PHE A CA  1 
ATOM   2941  C  C   . PHE A  1  370 ? -5.860  -17.445 3.620   1.00 60.19  ? 396  PHE A C   1 
ATOM   2942  O  O   . PHE A  1  370 ? -5.744  -17.934 4.736   1.00 60.18  ? 396  PHE A O   1 
ATOM   2943  C  CB  . PHE A  1  370 ? -5.291  -14.994 3.647   1.00 57.79  ? 396  PHE A CB  1 
ATOM   2944  C  CG  . PHE A  1  370 ? -4.457  -13.896 3.060   1.00 55.93  ? 396  PHE A CG  1 
ATOM   2945  C  CD1 . PHE A  1  370 ? -5.044  -12.880 2.313   1.00 55.74  ? 396  PHE A CD1 1 
ATOM   2946  C  CD2 . PHE A  1  370 ? -3.081  -13.891 3.234   1.00 54.80  ? 396  PHE A CD2 1 
ATOM   2947  C  CE1 . PHE A  1  370 ? -4.273  -11.877 1.746   1.00 54.86  ? 396  PHE A CE1 1 
ATOM   2948  C  CE2 . PHE A  1  370 ? -2.299  -12.898 2.672   1.00 55.42  ? 396  PHE A CE2 1 
ATOM   2949  C  CZ  . PHE A  1  370 ? -2.895  -11.884 1.924   1.00 55.66  ? 396  PHE A CZ  1 
ATOM   2950  N  N   . GLY A  1  371 ? -6.805  -17.824 2.773   1.00 60.48  ? 397  GLY A N   1 
ATOM   2951  C  CA  . GLY A  1  371 ? -7.739  -18.869 3.144   1.00 60.56  ? 397  GLY A CA  1 
ATOM   2952  C  C   . GLY A  1  371 ? -8.891  -18.366 3.975   1.00 60.72  ? 397  GLY A C   1 
ATOM   2953  O  O   . GLY A  1  371 ? -9.591  -19.143 4.630   1.00 60.39  ? 397  GLY A O   1 
ATOM   2954  N  N   . THR A  1  372 ? -9.102  -17.058 3.930   1.00 61.02  ? 398  THR A N   1 
ATOM   2955  C  CA  . THR A  1  372 ? -10.165 -16.446 4.699   1.00 62.18  ? 398  THR A CA  1 
ATOM   2956  C  C   . THR A  1  372 ? -11.005 -15.493 3.870   1.00 63.14  ? 398  THR A C   1 
ATOM   2957  O  O   . THR A  1  372 ? -10.602 -15.076 2.793   1.00 64.36  ? 398  THR A O   1 
ATOM   2958  C  CB  . THR A  1  372 ? -9.598  -15.645 5.865   1.00 62.61  ? 398  THR A CB  1 
ATOM   2959  O  OG1 . THR A  1  372 ? -10.679 -15.189 6.686   1.00 64.77  ? 398  THR A OG1 1 
ATOM   2960  C  CG2 . THR A  1  372 ? -8.810  -14.438 5.347   1.00 60.25  ? 398  THR A CG2 1 
ATOM   2961  N  N   . THR A  1  373 ? -12.174 -15.145 4.392   1.00 63.63  ? 399  THR A N   1 
ATOM   2962  C  CA  . THR A  1  373 ? -13.079 -14.212 3.729   1.00 63.24  ? 399  THR A CA  1 
ATOM   2963  C  C   . THR A  1  373 ? -13.642 -13.273 4.779   1.00 62.92  ? 399  THR A C   1 
ATOM   2964  O  O   . THR A  1  373 ? -14.724 -12.710 4.607   1.00 63.54  ? 399  THR A O   1 
ATOM   2965  C  CB  . THR A  1  373 ? -14.262 -14.927 3.067   1.00 63.06  ? 399  THR A CB  1 
ATOM   2966  O  OG1 . THR A  1  373 ? -14.856 -15.838 4.006   1.00 63.92  ? 399  THR A OG1 1 
ATOM   2967  C  CG2 . THR A  1  373 ? -13.811 -15.665 1.824   1.00 62.54  ? 399  THR A CG2 1 
ATOM   2968  N  N   . SER A  1  374 ? -12.902 -13.117 5.870   1.00 61.43  ? 400  SER A N   1 
ATOM   2969  C  CA  . SER A  1  374 ? -13.328 -12.264 6.959   1.00 60.35  ? 400  SER A CA  1 
ATOM   2970  C  C   . SER A  1  374 ? -12.265 -11.232 7.268   1.00 60.58  ? 400  SER A C   1 
ATOM   2971  O  O   . SER A  1  374 ? -12.416 -10.436 8.196   1.00 60.61  ? 400  SER A O   1 
ATOM   2972  C  CB  . SER A  1  374 ? -13.580 -13.113 8.195   1.00 59.61  ? 400  SER A CB  1 
ATOM   2973  O  OG  . SER A  1  374 ? -14.350 -14.241 7.851   1.00 59.65  ? 400  SER A OG  1 
ATOM   2974  N  N   . LEU A  1  375 ? -11.182 -11.263 6.500   1.00 60.01  ? 401  LEU A N   1 
ATOM   2975  C  CA  . LEU A  1  375 ? -10.087 -10.331 6.707   1.00 59.44  ? 401  LEU A CA  1 
ATOM   2976  C  C   . LEU A  1  375 ? -10.635 -8.921  6.710   1.00 59.01  ? 401  LEU A C   1 
ATOM   2977  O  O   . LEU A  1  375 ? -11.339 -8.541  5.782   1.00 59.99  ? 401  LEU A O   1 
ATOM   2978  C  CB  . LEU A  1  375 ? -9.056  -10.445 5.583   1.00 60.72  ? 401  LEU A CB  1 
ATOM   2979  C  CG  . LEU A  1  375 ? -7.571  -10.745 5.880   1.00 62.17  ? 401  LEU A CG  1 
ATOM   2980  C  CD1 . LEU A  1  375 ? -6.697  -9.886  4.942   1.00 60.17  ? 401  LEU A CD1 1 
ATOM   2981  C  CD2 . LEU A  1  375 ? -7.223  -10.471 7.336   1.00 60.19  ? 401  LEU A CD2 1 
ATOM   2982  N  N   . LYS A  1  376 ? -10.321 -8.159  7.756   1.00 57.65  ? 402  LYS A N   1 
ATOM   2983  C  CA  . LYS A  1  376 ? -10.754 -6.769  7.870   1.00 55.37  ? 402  LYS A CA  1 
ATOM   2984  C  C   . LYS A  1  376 ? -9.540  -5.861  7.860   1.00 54.08  ? 402  LYS A C   1 
ATOM   2985  O  O   . LYS A  1  376 ? -9.623  -4.717  7.433   1.00 54.23  ? 402  LYS A O   1 
ATOM   2986  C  CB  . LYS A  1  376 ? -11.510 -6.525  9.174   1.00 55.74  ? 402  LYS A CB  1 
ATOM   2987  C  CG  . LYS A  1  376 ? -12.882 -7.107  9.227   1.00 60.63  ? 402  LYS A CG  1 
ATOM   2988  C  CD  . LYS A  1  376 ? -13.565 -6.750  10.533  1.00 66.15  ? 402  LYS A CD  1 
ATOM   2989  C  CE  . LYS A  1  376 ? -14.941 -7.400  10.583  1.00 70.73  ? 402  LYS A CE  1 
ATOM   2990  N  NZ  . LYS A  1  376 ? -14.831 -8.870  10.274  1.00 73.53  ? 402  LYS A NZ  1 
ATOM   2991  N  N   . TYR A  1  377 ? -8.412  -6.384  8.332   1.00 52.49  ? 403  TYR A N   1 
ATOM   2992  C  CA  . TYR A  1  377 ? -7.169  -5.626  8.423   1.00 51.14  ? 403  TYR A CA  1 
ATOM   2993  C  C   . TYR A  1  377 ? -6.050  -6.392  7.712   1.00 51.15  ? 403  TYR A C   1 
ATOM   2994  O  O   . TYR A  1  377 ? -5.896  -7.592  7.917   1.00 53.23  ? 403  TYR A O   1 
ATOM   2995  C  CB  . TYR A  1  377 ? -6.849  -5.434  9.907   1.00 49.73  ? 403  TYR A CB  1 
ATOM   2996  C  CG  . TYR A  1  377 ? -5.624  -4.623  10.225  1.00 50.36  ? 403  TYR A CG  1 
ATOM   2997  C  CD1 . TYR A  1  377 ? -5.722  -3.416  10.903  1.00 48.74  ? 403  TYR A CD1 1 
ATOM   2998  C  CD2 . TYR A  1  377 ? -4.360  -5.111  9.948   1.00 52.08  ? 403  TYR A CD2 1 
ATOM   2999  C  CE1 . TYR A  1  377 ? -4.593  -2.727  11.308  1.00 48.71  ? 403  TYR A CE1 1 
ATOM   3000  C  CE2 . TYR A  1  377 ? -3.222  -4.427  10.349  1.00 52.50  ? 403  TYR A CE2 1 
ATOM   3001  C  CZ  . TYR A  1  377 ? -3.343  -3.243  11.029  1.00 51.12  ? 403  TYR A CZ  1 
ATOM   3002  O  OH  . TYR A  1  377 ? -2.194  -2.604  11.442  1.00 52.45  ? 403  TYR A OH  1 
ATOM   3003  N  N   . LEU A  1  378 ? -5.283  -5.709  6.866   1.00 49.83  ? 404  LEU A N   1 
ATOM   3004  C  CA  . LEU A  1  378 ? -4.187  -6.354  6.138   1.00 48.45  ? 404  LEU A CA  1 
ATOM   3005  C  C   . LEU A  1  378 ? -3.001  -5.403  5.989   1.00 48.95  ? 404  LEU A C   1 
ATOM   3006  O  O   . LEU A  1  378 ? -3.073  -4.403  5.276   1.00 47.49  ? 404  LEU A O   1 
ATOM   3007  C  CB  . LEU A  1  378 ? -4.654  -6.810  4.755   1.00 47.22  ? 404  LEU A CB  1 
ATOM   3008  C  CG  . LEU A  1  378 ? -3.567  -7.334  3.811   1.00 46.94  ? 404  LEU A CG  1 
ATOM   3009  C  CD1 . LEU A  1  378 ? -2.878  -8.548  4.427   1.00 47.10  ? 404  LEU A CD1 1 
ATOM   3010  C  CD2 . LEU A  1  378 ? -4.178  -7.694  2.476   1.00 45.85  ? 404  LEU A CD2 1 
ATOM   3011  N  N   . ASP A  1  379 ? -1.906  -5.744  6.661   1.00 49.16  ? 405  ASP A N   1 
ATOM   3012  C  CA  . ASP A  1  379 ? -0.697  -4.933  6.647   1.00 49.06  ? 405  ASP A CA  1 
ATOM   3013  C  C   . ASP A  1  379 ? 0.488   -5.672  6.003   1.00 48.54  ? 405  ASP A C   1 
ATOM   3014  O  O   . ASP A  1  379 ? 1.117   -6.513  6.636   1.00 50.43  ? 405  ASP A O   1 
ATOM   3015  C  CB  . ASP A  1  379 ? -0.363  -4.537  8.095   1.00 50.39  ? 405  ASP A CB  1 
ATOM   3016  C  CG  . ASP A  1  379 ? 0.806   -3.554  8.205   1.00 53.05  ? 405  ASP A CG  1 
ATOM   3017  O  OD1 . ASP A  1  379 ? 0.987   -3.024  9.334   1.00 53.90  ? 405  ASP A OD1 1 
ATOM   3018  O  OD2 . ASP A  1  379 ? 1.531   -3.314  7.198   1.00 51.56  ? 405  ASP A OD2 1 
ATOM   3019  N  N   . LEU A  1  380 ? 0.788   -5.358  4.746   1.00 45.88  ? 406  LEU A N   1 
ATOM   3020  C  CA  . LEU A  1  380 ? 1.911   -5.966  4.049   1.00 43.67  ? 406  LEU A CA  1 
ATOM   3021  C  C   . LEU A  1  380 ? 2.962   -4.903  3.764   1.00 43.37  ? 406  LEU A C   1 
ATOM   3022  O  O   . LEU A  1  380 ? 3.599   -4.923  2.706   1.00 42.16  ? 406  LEU A O   1 
ATOM   3023  C  CB  . LEU A  1  380 ? 1.464   -6.539  2.723   1.00 43.54  ? 406  LEU A CB  1 
ATOM   3024  C  CG  . LEU A  1  380 ? 0.446   -7.649  2.757   1.00 45.10  ? 406  LEU A CG  1 
ATOM   3025  C  CD1 . LEU A  1  380 ? 0.068   -7.962  1.336   1.00 45.78  ? 406  LEU A CD1 1 
ATOM   3026  C  CD2 . LEU A  1  380 ? 1.025   -8.863  3.446   1.00 45.95  ? 406  LEU A CD2 1 
ATOM   3027  N  N   . SER A  1  381 ? 3.145   -3.968  4.691   1.00 43.31  ? 407  SER A N   1 
ATOM   3028  C  CA  . SER A  1  381 ? 4.113   -2.903  4.471   1.00 43.64  ? 407  SER A CA  1 
ATOM   3029  C  C   . SER A  1  381 ? 5.534   -3.336  4.768   1.00 43.63  ? 407  SER A C   1 
ATOM   3030  O  O   . SER A  1  381 ? 5.759   -4.300  5.484   1.00 44.95  ? 407  SER A O   1 
ATOM   3031  C  CB  . SER A  1  381 ? 3.761   -1.679  5.307   1.00 42.57  ? 407  SER A CB  1 
ATOM   3032  O  OG  . SER A  1  381 ? 3.707   -2.009  6.672   1.00 43.22  ? 407  SER A OG  1 
ATOM   3033  N  N   . PHE A  1  382 ? 6.491   -2.614  4.203   1.00 43.61  ? 408  PHE A N   1 
ATOM   3034  C  CA  . PHE A  1  382 ? 7.909   -2.901  4.375   1.00 43.87  ? 408  PHE A CA  1 
ATOM   3035  C  C   . PHE A  1  382 ? 8.320   -4.300  3.966   1.00 43.88  ? 408  PHE A C   1 
ATOM   3036  O  O   . PHE A  1  382 ? 8.848   -5.052  4.777   1.00 44.08  ? 408  PHE A O   1 
ATOM   3037  C  CB  . PHE A  1  382 ? 8.342   -2.667  5.814   1.00 44.42  ? 408  PHE A CB  1 
ATOM   3038  C  CG  . PHE A  1  382 ? 8.080   -1.283  6.297   1.00 48.55  ? 408  PHE A CG  1 
ATOM   3039  C  CD1 . PHE A  1  382 ? 6.803   -0.920  6.762   1.00 49.71  ? 408  PHE A CD1 1 
ATOM   3040  C  CD2 . PHE A  1  382 ? 9.084   -0.319  6.260   1.00 47.92  ? 408  PHE A CD2 1 
ATOM   3041  C  CE1 . PHE A  1  382 ? 6.534   0.385   7.182   1.00 48.43  ? 408  PHE A CE1 1 
ATOM   3042  C  CE2 . PHE A  1  382 ? 8.834   0.997   6.674   1.00 48.01  ? 408  PHE A CE2 1 
ATOM   3043  C  CZ  . PHE A  1  382 ? 7.556   1.351   7.137   1.00 48.88  ? 408  PHE A CZ  1 
ATOM   3044  N  N   . ASN A  1  383 ? 8.072   -4.647  2.710   1.00 43.16  ? 409  ASN A N   1 
ATOM   3045  C  CA  . ASN A  1  383 ? 8.444   -5.945  2.199   1.00 43.26  ? 409  ASN A CA  1 
ATOM   3046  C  C   . ASN A  1  383 ? 9.094   -5.730  0.854   1.00 45.10  ? 409  ASN A C   1 
ATOM   3047  O  O   . ASN A  1  383 ? 9.413   -4.600  0.496   1.00 48.10  ? 409  ASN A O   1 
ATOM   3048  C  CB  . ASN A  1  383 ? 7.227   -6.841  2.076   1.00 42.38  ? 409  ASN A CB  1 
ATOM   3049  C  CG  . ASN A  1  383 ? 6.694   -7.274  3.426   1.00 44.85  ? 409  ASN A CG  1 
ATOM   3050  O  OD1 . ASN A  1  383 ? 7.401   -7.905  4.207   1.00 46.15  ? 409  ASN A OD1 1 
ATOM   3051  N  ND2 . ASN A  1  383 ? 5.443   -6.939  3.710   1.00 46.77  ? 409  ASN A ND2 1 
ATOM   3052  N  N   . GLY A  1  384 ? 9.324   -6.804  0.113   1.00 45.72  ? 410  GLY A N   1 
ATOM   3053  C  CA  . GLY A  1  384 ? 9.962   -6.656  -1.184  1.00 44.80  ? 410  GLY A CA  1 
ATOM   3054  C  C   . GLY A  1  384 ? 8.957   -6.319  -2.261  1.00 44.52  ? 410  GLY A C   1 
ATOM   3055  O  O   . GLY A  1  384 ? 8.187   -5.381  -2.123  1.00 45.70  ? 410  GLY A O   1 
ATOM   3056  N  N   . VAL A  1  385 ? 8.952   -7.096  -3.331  1.00 43.69  ? 411  VAL A N   1 
ATOM   3057  C  CA  . VAL A  1  385 ? 8.028   -6.861  -4.410  1.00 43.86  ? 411  VAL A CA  1 
ATOM   3058  C  C   . VAL A  1  385 ? 6.675   -7.528  -4.193  1.00 44.03  ? 411  VAL A C   1 
ATOM   3059  O  O   . VAL A  1  385 ? 6.617   -8.647  -3.706  1.00 44.78  ? 411  VAL A O   1 
ATOM   3060  C  CB  . VAL A  1  385 ? 8.620   -7.371  -5.713  1.00 44.26  ? 411  VAL A CB  1 
ATOM   3061  C  CG1 . VAL A  1  385 ? 7.595   -7.284  -6.820  1.00 44.31  ? 411  VAL A CG1 1 
ATOM   3062  C  CG2 . VAL A  1  385 ? 9.853   -6.561  -6.049  1.00 45.46  ? 411  VAL A CG2 1 
ATOM   3063  N  N   . ILE A  1  386 ? 5.595   -6.826  -4.541  1.00 44.17  ? 412  ILE A N   1 
ATOM   3064  C  CA  . ILE A  1  386 ? 4.241   -7.367  -4.427  1.00 44.57  ? 412  ILE A CA  1 
ATOM   3065  C  C   . ILE A  1  386 ? 3.537   -7.141  -5.759  1.00 44.69  ? 412  ILE A C   1 
ATOM   3066  O  O   . ILE A  1  386 ? 3.077   -6.048  -6.042  1.00 45.94  ? 412  ILE A O   1 
ATOM   3067  C  CB  . ILE A  1  386 ? 3.407   -6.680  -3.318  1.00 44.67  ? 412  ILE A CB  1 
ATOM   3068  C  CG1 . ILE A  1  386 ? 4.055   -6.896  -1.954  1.00 45.92  ? 412  ILE A CG1 1 
ATOM   3069  C  CG2 . ILE A  1  386 ? 2.005   -7.275  -3.266  1.00 43.55  ? 412  ILE A CG2 1 
ATOM   3070  C  CD1 . ILE A  1  386 ? 3.264   -6.289  -0.806  1.00 45.65  ? 412  ILE A CD1 1 
ATOM   3071  N  N   . THR A  1  387 ? 3.466   -8.182  -6.577  1.00 45.04  ? 413  THR A N   1 
ATOM   3072  C  CA  . THR A  1  387 ? 2.829   -8.104  -7.882  1.00 45.63  ? 413  THR A CA  1 
ATOM   3073  C  C   . THR A  1  387 ? 1.305   -8.226  -7.785  1.00 47.10  ? 413  THR A C   1 
ATOM   3074  O  O   . THR A  1  387 ? 0.784   -9.187  -7.228  1.00 47.98  ? 413  THR A O   1 
ATOM   3075  C  CB  . THR A  1  387 ? 3.370   -9.214  -8.792  1.00 44.27  ? 413  THR A CB  1 
ATOM   3076  O  OG1 . THR A  1  387 ? 4.797   -9.192  -8.741  1.00 45.16  ? 413  THR A OG1 1 
ATOM   3077  C  CG2 . THR A  1  387 ? 2.926   -9.010  -10.240 1.00 41.67  ? 413  THR A CG2 1 
ATOM   3078  N  N   . MET A  1  388 ? 0.590   -7.247  -8.328  1.00 48.77  ? 414  MET A N   1 
ATOM   3079  C  CA  . MET A  1  388 ? -0.874  -7.262  -8.295  1.00 49.01  ? 414  MET A CA  1 
ATOM   3080  C  C   . MET A  1  388 ? -1.445  -7.995  -9.508  1.00 49.05  ? 414  MET A C   1 
ATOM   3081  O  O   . MET A  1  388 ? -1.169  -7.643  -10.662 1.00 49.27  ? 414  MET A O   1 
ATOM   3082  C  CB  . MET A  1  388 ? -1.414  -5.829  -8.257  1.00 49.57  ? 414  MET A CB  1 
ATOM   3083  C  CG  . MET A  1  388 ? -0.940  -5.005  -7.060  1.00 50.35  ? 414  MET A CG  1 
ATOM   3084  S  SD  . MET A  1  388 ? -1.409  -5.757  -5.486  1.00 52.08  ? 414  MET A SD  1 
ATOM   3085  C  CE  . MET A  1  388 ? -3.165  -5.963  -5.735  1.00 48.11  ? 414  MET A CE  1 
ATOM   3086  N  N   . SER A  1  389 ? -2.258  -9.005  -9.247  1.00 48.71  ? 415  SER A N   1 
ATOM   3087  C  CA  . SER A  1  389 ? -2.836  -9.776  -10.328 1.00 50.25  ? 415  SER A CA  1 
ATOM   3088  C  C   . SER A  1  389 ? -4.244  -10.231 -10.038 1.00 50.93  ? 415  SER A C   1 
ATOM   3089  O  O   . SER A  1  389 ? -4.827  -10.979 -10.823 1.00 52.69  ? 415  SER A O   1 
ATOM   3090  C  CB  . SER A  1  389 ? -1.970  -10.993 -10.616 1.00 51.09  ? 415  SER A CB  1 
ATOM   3091  O  OG  . SER A  1  389 ? -1.703  -11.684 -9.410  1.00 54.70  ? 415  SER A OG  1 
ATOM   3092  N  N   . SER A  1  390 ? -4.786  -9.801  -8.908  1.00 51.65  ? 416  SER A N   1 
ATOM   3093  C  CA  . SER A  1  390 ? -6.150  -10.145 -8.527  1.00 53.76  ? 416  SER A CA  1 
ATOM   3094  C  C   . SER A  1  390 ? -6.685  -9.015  -7.658  1.00 55.02  ? 416  SER A C   1 
ATOM   3095  O  O   . SER A  1  390 ? -6.052  -8.637  -6.670  1.00 55.35  ? 416  SER A O   1 
ATOM   3096  C  CB  . SER A  1  390 ? -6.175  -11.463 -7.757  1.00 53.80  ? 416  SER A CB  1 
ATOM   3097  O  OG  . SER A  1  390 ? -7.513  -11.878 -7.491  1.00 55.43  ? 416  SER A OG  1 
ATOM   3098  N  N   . ASN A  1  391 ? -7.841  -8.462  -8.018  1.00 56.10  ? 417  ASN A N   1 
ATOM   3099  C  CA  . ASN A  1  391 ? -8.396  -7.351  -7.236  1.00 57.87  ? 417  ASN A CA  1 
ATOM   3100  C  C   . ASN A  1  391 ? -9.211  -7.754  -6.003  1.00 57.10  ? 417  ASN A C   1 
ATOM   3101  O  O   . ASN A  1  391 ? -10.404 -7.456  -5.887  1.00 57.32  ? 417  ASN A O   1 
ATOM   3102  C  CB  . ASN A  1  391 ? -9.216  -6.410  -8.132  1.00 59.07  ? 417  ASN A CB  1 
ATOM   3103  C  CG  . ASN A  1  391 ? -9.912  -7.141  -9.247  1.00 61.82  ? 417  ASN A CG  1 
ATOM   3104  O  OD1 . ASN A  1  391 ? -10.254 -8.319  -9.112  1.00 63.24  ? 417  ASN A OD1 1 
ATOM   3105  N  ND2 . ASN A  1  391 ? -10.148 -6.446  -10.354 1.00 62.68  ? 417  ASN A ND2 1 
ATOM   3106  N  N   . PHE A  1  392 ? -8.542  -8.442  -5.088  1.00 54.93  ? 418  PHE A N   1 
ATOM   3107  C  CA  . PHE A  1  392 ? -9.141  -8.865  -3.838  1.00 54.10  ? 418  PHE A CA  1 
ATOM   3108  C  C   . PHE A  1  392 ? -10.449 -9.672  -3.875  1.00 55.74  ? 418  PHE A C   1 
ATOM   3109  O  O   . PHE A  1  392 ? -11.345 -9.449  -3.049  1.00 55.97  ? 418  PHE A O   1 
ATOM   3110  C  CB  . PHE A  1  392 ? -9.330  -7.638  -2.950  1.00 51.57  ? 418  PHE A CB  1 
ATOM   3111  C  CG  . PHE A  1  392 ? -8.049  -6.894  -2.649  1.00 47.78  ? 418  PHE A CG  1 
ATOM   3112  C  CD1 . PHE A  1  392 ? -7.475  -6.056  -3.596  1.00 45.50  ? 418  PHE A CD1 1 
ATOM   3113  C  CD2 . PHE A  1  392 ? -7.429  -7.027  -1.415  1.00 45.68  ? 418  PHE A CD2 1 
ATOM   3114  C  CE1 . PHE A  1  392 ? -6.311  -5.362  -3.322  1.00 44.22  ? 418  PHE A CE1 1 
ATOM   3115  C  CE2 . PHE A  1  392 ? -6.262  -6.337  -1.133  1.00 45.63  ? 418  PHE A CE2 1 
ATOM   3116  C  CZ  . PHE A  1  392 ? -5.700  -5.497  -2.088  1.00 44.68  ? 418  PHE A CZ  1 
ATOM   3117  N  N   . LEU A  1  393 ? -10.559 -10.620 -4.801  1.00 56.26  ? 419  LEU A N   1 
ATOM   3118  C  CA  . LEU A  1  393 ? -11.759 -11.439 -4.872  1.00 56.54  ? 419  LEU A CA  1 
ATOM   3119  C  C   . LEU A  1  393 ? -11.862 -12.228 -3.591  1.00 58.53  ? 419  LEU A C   1 
ATOM   3120  O  O   . LEU A  1  393 ? -11.017 -13.080 -3.334  1.00 58.71  ? 419  LEU A O   1 
ATOM   3121  C  CB  . LEU A  1  393 ? -11.685 -12.439 -6.015  1.00 56.06  ? 419  LEU A CB  1 
ATOM   3122  C  CG  . LEU A  1  393 ? -11.416 -11.954 -7.432  1.00 56.77  ? 419  LEU A CG  1 
ATOM   3123  C  CD1 . LEU A  1  393 ? -11.750 -13.088 -8.389  1.00 55.12  ? 419  LEU A CD1 1 
ATOM   3124  C  CD2 . LEU A  1  393 ? -12.242 -10.718 -7.744  1.00 55.71  ? 419  LEU A CD2 1 
ATOM   3125  N  N   . GLY A  1  394 ? -12.889 -11.952 -2.788  1.00 60.57  ? 420  GLY A N   1 
ATOM   3126  C  CA  . GLY A  1  394 ? -13.068 -12.686 -1.547  1.00 62.61  ? 420  GLY A CA  1 
ATOM   3127  C  C   . GLY A  1  394 ? -12.626 -11.947 -0.300  1.00 64.43  ? 420  GLY A C   1 
ATOM   3128  O  O   . GLY A  1  394 ? -12.758 -12.453 0.818   1.00 66.24  ? 420  GLY A O   1 
ATOM   3129  N  N   . LEU A  1  395 ? -12.097 -10.746 -0.479  1.00 64.64  ? 421  LEU A N   1 
ATOM   3130  C  CA  . LEU A  1  395 ? -11.649 -9.954  0.657   1.00 65.34  ? 421  LEU A CA  1 
ATOM   3131  C  C   . LEU A  1  395 ? -12.433 -8.648  0.658   1.00 66.01  ? 421  LEU A C   1 
ATOM   3132  O  O   . LEU A  1  395 ? -11.877 -7.571  0.894   1.00 65.08  ? 421  LEU A O   1 
ATOM   3133  C  CB  . LEU A  1  395 ? -10.149 -9.676  0.524   1.00 65.11  ? 421  LEU A CB  1 
ATOM   3134  C  CG  . LEU A  1  395 ? -9.243  -10.892 0.321   1.00 62.72  ? 421  LEU A CG  1 
ATOM   3135  C  CD1 . LEU A  1  395 ? -7.829  -10.411 0.061   1.00 61.39  ? 421  LEU A CD1 1 
ATOM   3136  C  CD2 . LEU A  1  395 ? -9.292  -11.799 1.548   1.00 62.31  ? 421  LEU A CD2 1 
ATOM   3137  N  N   . GLU A  1  396 ? -13.729 -8.765  0.380   1.00 67.53  ? 422  GLU A N   1 
ATOM   3138  C  CA  . GLU A  1  396 ? -14.633 -7.623  0.302   1.00 69.35  ? 422  GLU A CA  1 
ATOM   3139  C  C   . GLU A  1  396 ? -14.703 -6.778  1.568   1.00 69.41  ? 422  GLU A C   1 
ATOM   3140  O  O   . GLU A  1  396 ? -14.860 -5.548  1.507   1.00 70.07  ? 422  GLU A O   1 
ATOM   3141  C  CB  . GLU A  1  396 ? -16.040 -8.097  -0.061  1.00 71.46  ? 422  GLU A CB  1 
ATOM   3142  C  CG  . GLU A  1  396 ? -16.242 -8.511  -1.535  1.00 76.27  ? 422  GLU A CG  1 
ATOM   3143  C  CD  . GLU A  1  396 ? -15.615 -9.867  -1.902  1.00 78.63  ? 422  GLU A CD  1 
ATOM   3144  O  OE1 . GLU A  1  396 ? -15.791 -10.843 -1.138  1.00 78.67  ? 422  GLU A OE1 1 
ATOM   3145  O  OE2 . GLU A  1  396 ? -14.965 -9.962  -2.974  1.00 78.81  ? 422  GLU A OE2 1 
ATOM   3146  N  N   . GLN A  1  397 ? -14.559 -7.433  2.714   1.00 68.88  ? 423  GLN A N   1 
ATOM   3147  C  CA  . GLN A  1  397 ? -14.635 -6.754  3.996   1.00 66.73  ? 423  GLN A CA  1 
ATOM   3148  C  C   . GLN A  1  397 ? -13.404 -6.003  4.488   1.00 64.44  ? 423  GLN A C   1 
ATOM   3149  O  O   . GLN A  1  397 ? -13.396 -5.517  5.596   1.00 63.65  ? 423  GLN A O   1 
ATOM   3150  C  CB  . GLN A  1  397 ? -15.063 -7.757  5.044   1.00 68.59  ? 423  GLN A CB  1 
ATOM   3151  C  CG  . GLN A  1  397 ? -16.336 -8.471  4.667   1.00 75.34  ? 423  GLN A CG  1 
ATOM   3152  C  CD  . GLN A  1  397 ? -16.892 -9.304  5.812   1.00 80.01  ? 423  GLN A CD  1 
ATOM   3153  O  OE1 . GLN A  1  397 ? -17.138 -8.786  6.910   1.00 82.24  ? 423  GLN A OE1 1 
ATOM   3154  N  NE2 . GLN A  1  397 ? -17.096 -10.597 5.565   1.00 81.58  ? 423  GLN A NE2 1 
ATOM   3155  N  N   . LEU A  1  398 ? -12.369 -5.887  3.676   1.00 64.19  ? 424  LEU A N   1 
ATOM   3156  C  CA  . LEU A  1  398 ? -11.172 -5.185  4.116   1.00 64.74  ? 424  LEU A CA  1 
ATOM   3157  C  C   . LEU A  1  398 ? -11.456 -3.733  4.429   1.00 65.46  ? 424  LEU A C   1 
ATOM   3158  O  O   . LEU A  1  398 ? -11.874 -2.989  3.549   1.00 67.19  ? 424  LEU A O   1 
ATOM   3159  C  CB  . LEU A  1  398 ? -10.095 -5.218  3.037   1.00 65.40  ? 424  LEU A CB  1 
ATOM   3160  C  CG  . LEU A  1  398 ? -8.943  -6.208  3.113   1.00 64.54  ? 424  LEU A CG  1 
ATOM   3161  C  CD1 . LEU A  1  398 ? -7.903  -5.786  2.088   1.00 63.33  ? 424  LEU A CD1 1 
ATOM   3162  C  CD2 . LEU A  1  398 ? -8.353  -6.218  4.507   1.00 64.51  ? 424  LEU A CD2 1 
ATOM   3163  N  N   . GLU A  1  399 ? -11.203 -3.322  5.668   1.00 65.33  ? 425  GLU A N   1 
ATOM   3164  C  CA  . GLU A  1  399 ? -11.416 -1.935  6.074   1.00 64.85  ? 425  GLU A CA  1 
ATOM   3165  C  C   . GLU A  1  399 ? -10.072 -1.212  6.135   1.00 63.36  ? 425  GLU A C   1 
ATOM   3166  O  O   . GLU A  1  399 ? -10.002 -0.018  5.899   1.00 63.79  ? 425  GLU A O   1 
ATOM   3167  C  CB  . GLU A  1  399 ? -12.088 -1.870  7.450   1.00 67.14  ? 425  GLU A CB  1 
ATOM   3168  C  CG  . GLU A  1  399 ? -13.388 -2.670  7.559   1.00 71.60  ? 425  GLU A CG  1 
ATOM   3169  C  CD  . GLU A  1  399 ? -14.032 -2.576  8.933   1.00 74.83  ? 425  GLU A CD  1 
ATOM   3170  O  OE1 . GLU A  1  399 ? -14.962 -3.365  9.212   1.00 76.79  ? 425  GLU A OE1 1 
ATOM   3171  O  OE2 . GLU A  1  399 ? -13.612 -1.705  9.730   1.00 77.11  ? 425  GLU A OE2 1 
ATOM   3172  N  N   . HIS A  1  400 ? -9.009  -1.950  6.446   1.00 61.39  ? 426  HIS A N   1 
ATOM   3173  C  CA  . HIS A  1  400 ? -7.666  -1.392  6.560   1.00 58.24  ? 426  HIS A CA  1 
ATOM   3174  C  C   . HIS A  1  400 ? -6.686  -2.173  5.666   1.00 56.63  ? 426  HIS A C   1 
ATOM   3175  O  O   . HIS A  1  400 ? -6.679  -3.404  5.680   1.00 56.42  ? 426  HIS A O   1 
ATOM   3176  C  CB  . HIS A  1  400 ? -7.240  -1.464  8.022   1.00 59.55  ? 426  HIS A CB  1 
ATOM   3177  C  CG  . HIS A  1  400 ? -5.980  -0.714  8.336   1.00 62.30  ? 426  HIS A CG  1 
ATOM   3178  N  ND1 . HIS A  1  400 ? -4.745  -1.087  7.848   1.00 63.29  ? 426  HIS A ND1 1 
ATOM   3179  C  CD2 . HIS A  1  400 ? -5.762  0.376   9.112   1.00 61.90  ? 426  HIS A CD2 1 
ATOM   3180  C  CE1 . HIS A  1  400 ? -3.821  -0.263  8.311   1.00 61.85  ? 426  HIS A CE1 1 
ATOM   3181  N  NE2 . HIS A  1  400 ? -4.412  0.633   9.079   1.00 62.00  ? 426  HIS A NE2 1 
ATOM   3182  N  N   . LEU A  1  401 ? -5.868  -1.453  4.894   1.00 53.45  ? 427  LEU A N   1 
ATOM   3183  C  CA  . LEU A  1  401 ? -4.894  -2.064  3.983   1.00 50.55  ? 427  LEU A CA  1 
ATOM   3184  C  C   . LEU A  1  401 ? -3.661  -1.166  3.828   1.00 50.11  ? 427  LEU A C   1 
ATOM   3185  O  O   . LEU A  1  401 ? -3.753  -0.085  3.284   1.00 48.31  ? 427  LEU A O   1 
ATOM   3186  C  CB  . LEU A  1  401 ? -5.550  -2.306  2.622   1.00 47.19  ? 427  LEU A CB  1 
ATOM   3187  C  CG  . LEU A  1  401 ? -4.730  -2.722  1.398   1.00 45.54  ? 427  LEU A CG  1 
ATOM   3188  C  CD1 . LEU A  1  401 ? -3.953  -3.997  1.654   1.00 46.83  ? 427  LEU A CD1 1 
ATOM   3189  C  CD2 . LEU A  1  401 ? -5.671  -2.945  0.250   1.00 42.84  ? 427  LEU A CD2 1 
ATOM   3190  N  N   . ASP A  1  402 ? -2.506  -1.647  4.287   1.00 51.56  ? 428  ASP A N   1 
ATOM   3191  C  CA  . ASP A  1  402 ? -1.249  -0.884  4.256   1.00 52.75  ? 428  ASP A CA  1 
ATOM   3192  C  C   . ASP A  1  402 ? -0.084  -1.533  3.468   1.00 52.76  ? 428  ASP A C   1 
ATOM   3193  O  O   . ASP A  1  402 ? 0.575   -2.443  3.962   1.00 52.76  ? 428  ASP A O   1 
ATOM   3194  C  CB  . ASP A  1  402 ? -0.803  -0.650  5.705   1.00 54.08  ? 428  ASP A CB  1 
ATOM   3195  C  CG  . ASP A  1  402 ? 0.357   0.337   5.825   1.00 55.86  ? 428  ASP A CG  1 
ATOM   3196  O  OD1 . ASP A  1  402 ? 0.939   0.713   4.788   1.00 55.57  ? 428  ASP A OD1 1 
ATOM   3197  O  OD2 . ASP A  1  402 ? 0.692   0.730   6.968   1.00 56.75  ? 428  ASP A OD2 1 
ATOM   3198  N  N   . PHE A  1  403 ? 0.179   -1.050  2.257   1.00 52.06  ? 429  PHE A N   1 
ATOM   3199  C  CA  . PHE A  1  403 ? 1.257   -1.569  1.420   1.00 50.65  ? 429  PHE A CA  1 
ATOM   3200  C  C   . PHE A  1  403 ? 2.493   -0.696  1.517   1.00 51.42  ? 429  PHE A C   1 
ATOM   3201  O  O   . PHE A  1  403 ? 3.458   -0.888  0.783   1.00 51.90  ? 429  PHE A O   1 
ATOM   3202  C  CB  . PHE A  1  403 ? 0.838   -1.574  -0.045  1.00 52.03  ? 429  PHE A CB  1 
ATOM   3203  C  CG  . PHE A  1  403 ? -0.057  -2.701  -0.424  1.00 53.23  ? 429  PHE A CG  1 
ATOM   3204  C  CD1 . PHE A  1  403 ? -1.300  -2.450  -0.986  1.00 53.55  ? 429  PHE A CD1 1 
ATOM   3205  C  CD2 . PHE A  1  403 ? 0.360   -4.012  -0.267  1.00 54.40  ? 429  PHE A CD2 1 
ATOM   3206  C  CE1 . PHE A  1  403 ? -2.119  -3.488  -1.395  1.00 55.44  ? 429  PHE A CE1 1 
ATOM   3207  C  CE2 . PHE A  1  403 ? -0.441  -5.058  -0.667  1.00 56.08  ? 429  PHE A CE2 1 
ATOM   3208  C  CZ  . PHE A  1  403 ? -1.693  -4.795  -1.238  1.00 56.69  ? 429  PHE A CZ  1 
ATOM   3209  N  N   . GLN A  1  404 ? 2.454   0.284   2.404   1.00 51.75  ? 430  GLN A N   1 
ATOM   3210  C  CA  . GLN A  1  404 ? 3.552   1.228   2.580   1.00 51.67  ? 430  GLN A CA  1 
ATOM   3211  C  C   . GLN A  1  404 ? 4.973   0.678   2.488   1.00 51.18  ? 430  GLN A C   1 
ATOM   3212  O  O   . GLN A  1  404 ? 5.308   -0.291  3.149   1.00 52.38  ? 430  GLN A O   1 
ATOM   3213  C  CB  . GLN A  1  404 ? 3.380   1.913   3.921   1.00 52.83  ? 430  GLN A CB  1 
ATOM   3214  C  CG  . GLN A  1  404 ? 4.499   2.834   4.288   1.00 55.26  ? 430  GLN A CG  1 
ATOM   3215  C  CD  . GLN A  1  404 ? 4.355   3.331   5.696   1.00 56.91  ? 430  GLN A CD  1 
ATOM   3216  O  OE1 . GLN A  1  404 ? 5.139   4.166   6.148   1.00 59.51  ? 430  GLN A OE1 1 
ATOM   3217  N  NE2 . GLN A  1  404 ? 3.355   2.814   6.414   1.00 56.13  ? 430  GLN A NE2 1 
ATOM   3218  N  N   . HIS A  1  405 ? 5.805   1.318   1.676   1.00 51.04  ? 431  HIS A N   1 
ATOM   3219  C  CA  . HIS A  1  405 ? 7.214   0.941   1.511   1.00 50.78  ? 431  HIS A CA  1 
ATOM   3220  C  C   . HIS A  1  405 ? 7.541   -0.406  0.912   1.00 48.56  ? 431  HIS A C   1 
ATOM   3221  O  O   . HIS A  1  405 ? 8.616   -0.946  1.143   1.00 47.30  ? 431  HIS A O   1 
ATOM   3222  C  CB  . HIS A  1  405 ? 7.958   1.088   2.840   1.00 52.97  ? 431  HIS A CB  1 
ATOM   3223  C  CG  . HIS A  1  405 ? 8.440   2.481   3.097   1.00 56.47  ? 431  HIS A CG  1 
ATOM   3224  N  ND1 . HIS A  1  405 ? 9.570   3.001   2.498   1.00 55.69  ? 431  HIS A ND1 1 
ATOM   3225  C  CD2 . HIS A  1  405 ? 7.905   3.487   3.830   1.00 57.21  ? 431  HIS A CD2 1 
ATOM   3226  C  CE1 . HIS A  1  405 ? 9.709   4.267   2.850   1.00 56.61  ? 431  HIS A CE1 1 
ATOM   3227  N  NE2 . HIS A  1  405 ? 8.711   4.588   3.657   1.00 58.42  ? 431  HIS A NE2 1 
ATOM   3228  N  N   . SER A  1  406 ? 6.617   -0.938  0.134   1.00 47.80  ? 432  SER A N   1 
ATOM   3229  C  CA  . SER A  1  406 ? 6.830   -2.201  -0.522  1.00 48.47  ? 432  SER A CA  1 
ATOM   3230  C  C   . SER A  1  406 ? 6.724   -1.919  -2.011  1.00 50.73  ? 432  SER A C   1 
ATOM   3231  O  O   . SER A  1  406 ? 5.806   -1.247  -2.454  1.00 51.66  ? 432  SER A O   1 
ATOM   3232  C  CB  . SER A  1  406 ? 5.762   -3.204  -0.092  1.00 46.46  ? 432  SER A CB  1 
ATOM   3233  O  OG  . SER A  1  406 ? 5.858   -3.481  1.287   1.00 44.24  ? 432  SER A OG  1 
ATOM   3234  N  N   . ASN A  1  407 ? 7.681   -2.395  -2.788  1.00 54.48  ? 433  ASN A N   1 
ATOM   3235  C  CA  . ASN A  1  407 ? 7.633   -2.189  -4.224  1.00 57.26  ? 433  ASN A CA  1 
ATOM   3236  C  C   . ASN A  1  407 ? 6.370   -2.867  -4.772  1.00 58.72  ? 433  ASN A C   1 
ATOM   3237  O  O   . ASN A  1  407 ? 6.256   -4.097  -4.753  1.00 59.72  ? 433  ASN A O   1 
ATOM   3238  C  CB  . ASN A  1  407 ? 8.868   -2.815  -4.867  1.00 60.09  ? 433  ASN A CB  1 
ATOM   3239  C  CG  . ASN A  1  407 ? 9.016   -2.440  -6.321  1.00 65.77  ? 433  ASN A CG  1 
ATOM   3240  O  OD1 . ASN A  1  407 ? 8.046   -2.483  -7.099  1.00 66.68  ? 433  ASN A OD1 1 
ATOM   3241  N  ND2 . ASN A  1  407 ? 10.243  -2.069  -6.711  1.00 67.16  ? 433  ASN A ND2 1 
ATOM   3242  N  N   . LEU A  1  408 ? 5.403   -2.077  -5.227  1.00 58.69  ? 434  LEU A N   1 
ATOM   3243  C  CA  . LEU A  1  408 ? 4.170   -2.635  -5.795  1.00 58.25  ? 434  LEU A CA  1 
ATOM   3244  C  C   . LEU A  1  408 ? 4.285   -2.584  -7.318  1.00 58.34  ? 434  LEU A C   1 
ATOM   3245  O  O   . LEU A  1  408 ? 4.841   -1.626  -7.866  1.00 59.19  ? 434  LEU A O   1 
ATOM   3246  C  CB  . LEU A  1  408 ? 2.959   -1.826  -5.329  1.00 58.29  ? 434  LEU A CB  1 
ATOM   3247  C  CG  . LEU A  1  408 ? 2.135   -2.419  -4.182  1.00 59.79  ? 434  LEU A CG  1 
ATOM   3248  C  CD1 . LEU A  1  408 ? 1.240   -1.361  -3.579  1.00 60.67  ? 434  LEU A CD1 1 
ATOM   3249  C  CD2 . LEU A  1  408 ? 1.296   -3.578  -4.705  1.00 61.70  ? 434  LEU A CD2 1 
ATOM   3250  N  N   . LYS A  1  409 ? 3.778   -3.614  -7.995  1.00 56.98  ? 435  LYS A N   1 
ATOM   3251  C  CA  . LYS A  1  409 ? 3.843   -3.675  -9.450  1.00 56.33  ? 435  LYS A CA  1 
ATOM   3252  C  C   . LYS A  1  409 ? 2.511   -4.025  -10.073 1.00 57.13  ? 435  LYS A C   1 
ATOM   3253  O  O   . LYS A  1  409 ? 1.718   -4.757  -9.483  1.00 55.72  ? 435  LYS A O   1 
ATOM   3254  C  CB  . LYS A  1  409 ? 4.884   -4.697  -9.906  1.00 54.69  ? 435  LYS A CB  1 
ATOM   3255  C  CG  . LYS A  1  409 ? 6.304   -4.339  -9.530  1.00 55.55  ? 435  LYS A CG  1 
ATOM   3256  C  CD  . LYS A  1  409 ? 7.292   -5.310  -10.122 1.00 56.04  ? 435  LYS A CD  1 
ATOM   3257  C  CE  . LYS A  1  409 ? 8.698   -4.920  -9.732  1.00 58.27  ? 435  LYS A CE  1 
ATOM   3258  N  NZ  . LYS A  1  409 ? 9.709   -5.892  -10.244 1.00 63.06  ? 435  LYS A NZ  1 
ATOM   3259  N  N   . GLN A  1  410 ? 2.280   -3.495  -11.275 1.00 59.27  ? 436  GLN A N   1 
ATOM   3260  C  CA  . GLN A  1  410 ? 1.045   -3.725  -12.035 1.00 62.36  ? 436  GLN A CA  1 
ATOM   3261  C  C   . GLN A  1  410 ? -0.145  -2.945  -11.475 1.00 64.73  ? 436  GLN A C   1 
ATOM   3262  O  O   . GLN A  1  410 ? -1.299  -3.366  -11.625 1.00 65.48  ? 436  GLN A O   1 
ATOM   3263  C  CB  . GLN A  1  410 ? 0.711   -5.217  -12.068 1.00 60.78  ? 436  GLN A CB  1 
ATOM   3264  C  CG  . GLN A  1  410 ? 1.938   -6.068  -12.238 1.00 62.11  ? 436  GLN A CG  1 
ATOM   3265  C  CD  . GLN A  1  410 ? 1.684   -7.275  -13.076 1.00 62.57  ? 436  GLN A CD  1 
ATOM   3266  O  OE1 . GLN A  1  410 ? 0.780   -8.065  -12.786 1.00 64.93  ? 436  GLN A OE1 1 
ATOM   3267  N  NE2 . GLN A  1  410 ? 2.479   -7.439  -14.130 1.00 61.47  ? 436  GLN A NE2 1 
ATOM   3268  N  N   . MET A  1  411 ? 0.148   -1.810  -10.836 1.00 66.47  ? 437  MET A N   1 
ATOM   3269  C  CA  . MET A  1  411 ? -0.867  -0.944  -10.234 1.00 66.99  ? 437  MET A CA  1 
ATOM   3270  C  C   . MET A  1  411 ? -1.849  -0.347  -11.250 1.00 67.33  ? 437  MET A C   1 
ATOM   3271  O  O   . MET A  1  411 ? -3.074  -0.358  -11.048 1.00 66.20  ? 437  MET A O   1 
ATOM   3272  C  CB  . MET A  1  411 ? -0.171  0.189   -9.486  1.00 68.32  ? 437  MET A CB  1 
ATOM   3273  C  CG  . MET A  1  411 ? 0.242   -0.171  -8.076  1.00 72.34  ? 437  MET A CG  1 
ATOM   3274  S  SD  . MET A  1  411 ? -1.206  -0.242  -6.966  1.00 76.34  ? 437  MET A SD  1 
ATOM   3275  C  CE  . MET A  1  411 ? -1.189  1.405   -6.268  1.00 73.20  ? 437  MET A CE  1 
ATOM   3276  N  N   . SER A  1  412 ? -1.285  0.177   -12.337 1.00 67.23  ? 438  SER A N   1 
ATOM   3277  C  CA  . SER A  1  412 ? -2.048  0.811   -13.408 1.00 66.41  ? 438  SER A CA  1 
ATOM   3278  C  C   . SER A  1  412 ? -2.200  -0.170  -14.559 1.00 66.02  ? 438  SER A C   1 
ATOM   3279  O  O   . SER A  1  412 ? -1.876  0.146   -15.696 1.00 66.71  ? 438  SER A O   1 
ATOM   3280  C  CB  . SER A  1  412 ? -1.303  2.057   -13.911 1.00 66.22  ? 438  SER A CB  1 
ATOM   3281  O  OG  . SER A  1  412 ? -0.719  2.791   -12.838 1.00 67.21  ? 438  SER A OG  1 
ATOM   3282  N  N   . GLU A  1  413 ? -2.705  -1.360  -14.269 1.00 65.36  ? 439  GLU A N   1 
ATOM   3283  C  CA  . GLU A  1  413 ? -2.859  -2.373  -15.300 1.00 64.14  ? 439  GLU A CA  1 
ATOM   3284  C  C   . GLU A  1  413 ? -4.292  -2.883  -15.307 1.00 63.85  ? 439  GLU A C   1 
ATOM   3285  O  O   . GLU A  1  413 ? -4.679  -3.680  -16.168 1.00 64.35  ? 439  GLU A O   1 
ATOM   3286  C  CB  . GLU A  1  413 ? -1.888  -3.507  -15.018 1.00 64.79  ? 439  GLU A CB  1 
ATOM   3287  C  CG  . GLU A  1  413 ? -1.318  -4.156  -16.233 1.00 66.64  ? 439  GLU A CG  1 
ATOM   3288  C  CD  . GLU A  1  413 ? 0.106   -4.581  -15.997 1.00 68.85  ? 439  GLU A CD  1 
ATOM   3289  O  OE1 . GLU A  1  413 ? 0.883   -3.723  -15.521 1.00 69.02  ? 439  GLU A OE1 1 
ATOM   3290  O  OE2 . GLU A  1  413 ? 0.447   -5.754  -16.284 1.00 70.84  ? 439  GLU A OE2 1 
ATOM   3291  N  N   . PHE A  1  414 ? -5.055  -2.426  -14.316 1.00 62.51  ? 440  PHE A N   1 
ATOM   3292  C  CA  . PHE A  1  414 ? -6.470  -2.748  -14.143 1.00 62.10  ? 440  PHE A CA  1 
ATOM   3293  C  C   . PHE A  1  414 ? -6.874  -2.157  -12.795 1.00 61.92  ? 440  PHE A C   1 
ATOM   3294  O  O   . PHE A  1  414 ? -6.058  -1.493  -12.150 1.00 62.53  ? 440  PHE A O   1 
ATOM   3295  C  CB  . PHE A  1  414 ? -6.717  -4.275  -14.210 1.00 61.35  ? 440  PHE A CB  1 
ATOM   3296  C  CG  . PHE A  1  414 ? -6.075  -5.072  -13.098 1.00 62.00  ? 440  PHE A CG  1 
ATOM   3297  C  CD1 . PHE A  1  414 ? -6.786  -5.386  -11.941 1.00 62.35  ? 440  PHE A CD1 1 
ATOM   3298  C  CD2 . PHE A  1  414 ? -4.773  -5.537  -13.218 1.00 62.59  ? 440  PHE A CD2 1 
ATOM   3299  C  CE1 . PHE A  1  414 ? -6.216  -6.154  -10.924 1.00 61.07  ? 440  PHE A CE1 1 
ATOM   3300  C  CE2 . PHE A  1  414 ? -4.186  -6.309  -12.201 1.00 62.16  ? 440  PHE A CE2 1 
ATOM   3301  C  CZ  . PHE A  1  414 ? -4.911  -6.617  -11.055 1.00 61.00  ? 440  PHE A CZ  1 
ATOM   3302  N  N   . SER A  1  415 ? -8.118  -2.357  -12.372 1.00 60.65  ? 441  SER A N   1 
ATOM   3303  C  CA  . SER A  1  415 ? -8.550  -1.825  -11.080 1.00 60.12  ? 441  SER A CA  1 
ATOM   3304  C  C   . SER A  1  415 ? -8.263  -2.841  -9.980  1.00 58.40  ? 441  SER A C   1 
ATOM   3305  O  O   . SER A  1  415 ? -9.094  -3.696  -9.666  1.00 55.71  ? 441  SER A O   1 
ATOM   3306  C  CB  . SER A  1  415 ? -10.042 -1.493  -11.118 1.00 62.73  ? 441  SER A CB  1 
ATOM   3307  O  OG  . SER A  1  415 ? -10.323 -0.524  -12.120 1.00 65.68  ? 441  SER A OG  1 
ATOM   3308  N  N   . VAL A  1  416 ? -7.076  -2.733  -9.395  1.00 58.00  ? 442  VAL A N   1 
ATOM   3309  C  CA  . VAL A  1  416 ? -6.659  -3.661  -8.354  1.00 59.08  ? 442  VAL A CA  1 
ATOM   3310  C  C   . VAL A  1  416 ? -7.515  -3.618  -7.083  1.00 59.18  ? 442  VAL A C   1 
ATOM   3311  O  O   . VAL A  1  416 ? -7.626  -4.617  -6.371  1.00 57.90  ? 442  VAL A O   1 
ATOM   3312  C  CB  . VAL A  1  416 ? -5.177  -3.431  -7.965  1.00 58.88  ? 442  VAL A CB  1 
ATOM   3313  C  CG1 . VAL A  1  416 ? -4.314  -3.439  -9.206  1.00 59.84  ? 442  VAL A CG1 1 
ATOM   3314  C  CG2 . VAL A  1  416 ? -5.018  -2.128  -7.238  1.00 58.48  ? 442  VAL A CG2 1 
ATOM   3315  N  N   . PHE A  1  417 ? -8.130  -2.470  -6.812  1.00 59.76  ? 443  PHE A N   1 
ATOM   3316  C  CA  . PHE A  1  417 ? -8.956  -2.307  -5.622  1.00 60.13  ? 443  PHE A CA  1 
ATOM   3317  C  C   . PHE A  1  417 ? -10.461 -2.385  -5.889  1.00 61.06  ? 443  PHE A C   1 
ATOM   3318  O  O   . PHE A  1  417 ? -11.270 -2.118  -5.007  1.00 62.17  ? 443  PHE A O   1 
ATOM   3319  C  CB  . PHE A  1  417 ? -8.626  -0.969  -4.951  1.00 57.97  ? 443  PHE A CB  1 
ATOM   3320  C  CG  . PHE A  1  417 ? -7.158  -0.773  -4.669  1.00 55.76  ? 443  PHE A CG  1 
ATOM   3321  C  CD1 . PHE A  1  417 ? -6.496  -1.575  -3.757  1.00 55.22  ? 443  PHE A CD1 1 
ATOM   3322  C  CD2 . PHE A  1  417 ? -6.442  0.226   -5.312  1.00 55.26  ? 443  PHE A CD2 1 
ATOM   3323  C  CE1 . PHE A  1  417 ? -5.147  -1.385  -3.490  1.00 54.08  ? 443  PHE A CE1 1 
ATOM   3324  C  CE2 . PHE A  1  417 ? -5.087  0.427   -5.050  1.00 53.88  ? 443  PHE A CE2 1 
ATOM   3325  C  CZ  . PHE A  1  417 ? -4.441  -0.379  -4.139  1.00 53.71  ? 443  PHE A CZ  1 
ATOM   3326  N  N   . LEU A  1  418 ? -10.830 -2.792  -7.093  1.00 62.34  ? 444  LEU A N   1 
ATOM   3327  C  CA  . LEU A  1  418 ? -12.236 -2.880  -7.483  1.00 62.71  ? 444  LEU A CA  1 
ATOM   3328  C  C   . LEU A  1  418 ? -13.218 -3.584  -6.545  1.00 62.35  ? 444  LEU A C   1 
ATOM   3329  O  O   . LEU A  1  418 ? -14.409 -3.318  -6.616  1.00 62.31  ? 444  LEU A O   1 
ATOM   3330  C  CB  . LEU A  1  418 ? -12.353 -3.534  -8.862  1.00 62.97  ? 444  LEU A CB  1 
ATOM   3331  C  CG  . LEU A  1  418 ? -13.542 -3.058  -9.692  1.00 61.30  ? 444  LEU A CG  1 
ATOM   3332  C  CD1 . LEU A  1  418 ? -13.248 -1.627  -10.135 1.00 59.84  ? 444  LEU A CD1 1 
ATOM   3333  C  CD2 . LEU A  1  418 ? -13.765 -3.961  -10.891 1.00 59.44  ? 444  LEU A CD2 1 
ATOM   3334  N  N   . SER A  1  419 ? -12.748 -4.487  -5.689  1.00 63.07  ? 445  SER A N   1 
ATOM   3335  C  CA  . SER A  1  419 ? -13.660 -5.209  -4.794  1.00 63.48  ? 445  SER A CA  1 
ATOM   3336  C  C   . SER A  1  419 ? -13.780 -4.606  -3.408  1.00 64.70  ? 445  SER A C   1 
ATOM   3337  O  O   . SER A  1  419 ? -14.718 -4.927  -2.677  1.00 66.47  ? 445  SER A O   1 
ATOM   3338  C  CB  . SER A  1  419 ? -13.238 -6.683  -4.636  1.00 61.87  ? 445  SER A CB  1 
ATOM   3339  O  OG  . SER A  1  419 ? -13.550 -7.467  -5.777  1.00 59.58  ? 445  SER A OG  1 
ATOM   3340  N  N   . LEU A  1  420 ? -12.837 -3.741  -3.050  1.00 65.20  ? 446  LEU A N   1 
ATOM   3341  C  CA  . LEU A  1  420 ? -12.813 -3.126  -1.726  1.00 66.21  ? 446  LEU A CA  1 
ATOM   3342  C  C   . LEU A  1  420 ? -13.844 -2.025  -1.509  1.00 67.73  ? 446  LEU A C   1 
ATOM   3343  O  O   . LEU A  1  420 ? -13.494 -0.867  -1.270  1.00 68.45  ? 446  LEU A O   1 
ATOM   3344  C  CB  . LEU A  1  420 ? -11.400 -2.600  -1.442  1.00 64.94  ? 446  LEU A CB  1 
ATOM   3345  C  CG  . LEU A  1  420 ? -10.314 -3.595  -0.971  1.00 63.69  ? 446  LEU A CG  1 
ATOM   3346  C  CD1 . LEU A  1  420 ? -10.728 -5.050  -1.240  1.00 61.27  ? 446  LEU A CD1 1 
ATOM   3347  C  CD2 . LEU A  1  420 ? -8.992  -3.251  -1.647  1.00 59.27  ? 446  LEU A CD2 1 
ATOM   3348  N  N   . ARG A  1  421 ? -15.118 -2.401  -1.574  1.00 69.72  ? 447  ARG A N   1 
ATOM   3349  C  CA  . ARG A  1  421 ? -16.213 -1.453  -1.391  1.00 71.73  ? 447  ARG A CA  1 
ATOM   3350  C  C   . ARG A  1  421 ? -16.299 -0.909  0.034   1.00 71.08  ? 447  ARG A C   1 
ATOM   3351  O  O   . ARG A  1  421 ? -16.916 0.127   0.267   1.00 72.54  ? 447  ARG A O   1 
ATOM   3352  C  CB  . ARG A  1  421 ? -17.555 -2.100  -1.773  1.00 74.55  ? 447  ARG A CB  1 
ATOM   3353  C  CG  . ARG A  1  421 ? -17.773 -3.521  -1.237  1.00 80.15  ? 447  ARG A CG  1 
ATOM   3354  C  CD  . ARG A  1  421 ? -19.205 -3.730  -0.742  1.00 85.34  ? 447  ARG A CD  1 
ATOM   3355  N  NE  . ARG A  1  421 ? -20.204 -3.209  -1.681  1.00 91.24  ? 447  ARG A NE  1 
ATOM   3356  C  CZ  . ARG A  1  421 ? -21.438 -2.829  -1.340  1.00 92.76  ? 447  ARG A CZ  1 
ATOM   3357  N  NH1 . ARG A  1  421 ? -21.834 -2.913  -0.070  1.00 93.75  ? 447  ARG A NH1 1 
ATOM   3358  N  NH2 . ARG A  1  421 ? -22.273 -2.350  -2.264  1.00 91.56  ? 447  ARG A NH2 1 
ATOM   3359  N  N   . ASN A  1  422 ? -15.671 -1.592  0.989   1.00 69.29  ? 448  ASN A N   1 
ATOM   3360  C  CA  . ASN A  1  422 ? -15.726 -1.143  2.377   1.00 65.65  ? 448  ASN A CA  1 
ATOM   3361  C  C   . ASN A  1  422 ? -14.415 -0.596  2.916   1.00 64.33  ? 448  ASN A C   1 
ATOM   3362  O  O   . ASN A  1  422 ? -14.362 -0.152  4.060   1.00 63.22  ? 448  ASN A O   1 
ATOM   3363  C  CB  . ASN A  1  422 ? -16.219 -2.284  3.262   1.00 64.04  ? 448  ASN A CB  1 
ATOM   3364  C  CG  . ASN A  1  422 ? -17.525 -2.875  2.761   1.00 64.67  ? 448  ASN A CG  1 
ATOM   3365  O  OD1 . ASN A  1  422 ? -18.453 -2.149  2.401   1.00 63.48  ? 448  ASN A OD1 1 
ATOM   3366  N  ND2 . ASN A  1  422 ? -17.605 -4.197  2.737   1.00 65.68  ? 448  ASN A ND2 1 
ATOM   3367  N  N   . LEU A  1  423 ? -13.366 -0.609  2.095   1.00 63.75  ? 449  LEU A N   1 
ATOM   3368  C  CA  . LEU A  1  423 ? -12.060 -0.128  2.540   1.00 62.70  ? 449  LEU A CA  1 
ATOM   3369  C  C   . LEU A  1  423 ? -12.151 1.311   3.034   1.00 61.78  ? 449  LEU A C   1 
ATOM   3370  O  O   . LEU A  1  423 ? -12.627 2.177   2.320   1.00 63.05  ? 449  LEU A O   1 
ATOM   3371  C  CB  . LEU A  1  423 ? -11.013 -0.231  1.412   1.00 59.96  ? 449  LEU A CB  1 
ATOM   3372  C  CG  . LEU A  1  423 ? -9.573  0.033   1.884   1.00 57.97  ? 449  LEU A CG  1 
ATOM   3373  C  CD1 . LEU A  1  423 ? -9.153  -1.090  2.811   1.00 55.90  ? 449  LEU A CD1 1 
ATOM   3374  C  CD2 . LEU A  1  423 ? -8.621  0.156   0.706   1.00 54.79  ? 449  LEU A CD2 1 
ATOM   3375  N  N   . ILE A  1  424 ? -11.686 1.548   4.256   1.00 60.47  ? 450  ILE A N   1 
ATOM   3376  C  CA  . ILE A  1  424 ? -11.712 2.870   4.861   1.00 59.58  ? 450  ILE A CA  1 
ATOM   3377  C  C   . ILE A  1  424 ? -10.325 3.543   4.904   1.00 60.26  ? 450  ILE A C   1 
ATOM   3378  O  O   . ILE A  1  424 ? -10.212 4.754   4.705   1.00 60.63  ? 450  ILE A O   1 
ATOM   3379  C  CB  . ILE A  1  424 ? -12.308 2.770   6.280   1.00 58.84  ? 450  ILE A CB  1 
ATOM   3380  C  CG1 . ILE A  1  424 ? -13.817 2.539   6.171   1.00 58.70  ? 450  ILE A CG1 1 
ATOM   3381  C  CG2 . ILE A  1  424 ? -11.961 4.002   7.092   1.00 58.42  ? 450  ILE A CG2 1 
ATOM   3382  C  CD1 . ILE A  1  424 ? -14.484 2.063   7.465   1.00 59.91  ? 450  ILE A CD1 1 
ATOM   3383  N  N   . TYR A  1  425 ? -9.279  2.755   5.160   1.00 60.73  ? 451  TYR A N   1 
ATOM   3384  C  CA  . TYR A  1  425 ? -7.896  3.258   5.226   1.00 60.12  ? 451  TYR A CA  1 
ATOM   3385  C  C   . TYR A  1  425 ? -7.046  2.593   4.136   1.00 60.33  ? 451  TYR A C   1 
ATOM   3386  O  O   . TYR A  1  425 ? -7.201  1.396   3.869   1.00 61.38  ? 451  TYR A O   1 
ATOM   3387  C  CB  . TYR A  1  425 ? -7.302  2.968   6.608   1.00 58.68  ? 451  TYR A CB  1 
ATOM   3388  C  CG  . TYR A  1  425 ? -5.906  3.510   6.845   1.00 57.92  ? 451  TYR A CG  1 
ATOM   3389  C  CD1 . TYR A  1  425 ? -4.777  2.759   6.531   1.00 57.96  ? 451  TYR A CD1 1 
ATOM   3390  C  CD2 . TYR A  1  425 ? -5.715  4.776   7.409   1.00 57.16  ? 451  TYR A CD2 1 
ATOM   3391  C  CE1 . TYR A  1  425 ? -3.482  3.261   6.778   1.00 57.72  ? 451  TYR A CE1 1 
ATOM   3392  C  CE2 . TYR A  1  425 ? -4.430  5.286   7.655   1.00 55.55  ? 451  TYR A CE2 1 
ATOM   3393  C  CZ  . TYR A  1  425 ? -3.318  4.526   7.334   1.00 56.08  ? 451  TYR A CZ  1 
ATOM   3394  O  OH  . TYR A  1  425 ? -2.048  5.047   7.513   1.00 54.94  ? 451  TYR A OH  1 
ATOM   3395  N  N   . LEU A  1  426 ? -6.178  3.372   3.490   1.00 58.53  ? 452  LEU A N   1 
ATOM   3396  C  CA  . LEU A  1  426 ? -5.319  2.844   2.429   1.00 58.10  ? 452  LEU A CA  1 
ATOM   3397  C  C   . LEU A  1  426 ? -4.042  3.669   2.289   1.00 58.01  ? 452  LEU A C   1 
ATOM   3398  O  O   . LEU A  1  426 ? -4.082  4.840   1.929   1.00 59.34  ? 452  LEU A O   1 
ATOM   3399  C  CB  . LEU A  1  426 ? -6.053  2.803   1.075   1.00 57.13  ? 452  LEU A CB  1 
ATOM   3400  C  CG  . LEU A  1  426 ? -5.182  2.439   -0.145  1.00 57.56  ? 452  LEU A CG  1 
ATOM   3401  C  CD1 . LEU A  1  426 ? -4.722  0.999   -0.021  1.00 58.13  ? 452  LEU A CD1 1 
ATOM   3402  C  CD2 . LEU A  1  426 ? -5.955  2.621   -1.443  1.00 55.94  ? 452  LEU A CD2 1 
ATOM   3403  N  N   . ASP A  1  427 ? -2.910  3.035   2.572   1.00 57.04  ? 453  ASP A N   1 
ATOM   3404  C  CA  . ASP A  1  427 ? -1.608  3.673   2.498   1.00 55.41  ? 453  ASP A CA  1 
ATOM   3405  C  C   . ASP A  1  427 ? -0.754  2.917   1.467   1.00 55.19  ? 453  ASP A C   1 
ATOM   3406  O  O   . ASP A  1  427 ? -0.488  1.733   1.636   1.00 55.86  ? 453  ASP A O   1 
ATOM   3407  C  CB  . ASP A  1  427 ? -0.942  3.632   3.890   1.00 54.93  ? 453  ASP A CB  1 
ATOM   3408  C  CG  . ASP A  1  427 ? 0.426   4.329   3.928   1.00 55.40  ? 453  ASP A CG  1 
ATOM   3409  O  OD1 . ASP A  1  427 ? 1.075   4.443   2.866   1.00 54.47  ? 453  ASP A OD1 1 
ATOM   3410  O  OD2 . ASP A  1  427 ? 0.876   4.741   5.024   1.00 55.52  ? 453  ASP A OD2 1 
ATOM   3411  N  N   . ILE A  1  428 ? -0.356  3.596   0.395   1.00 54.39  ? 454  ILE A N   1 
ATOM   3412  C  CA  . ILE A  1  428 ? 0.491   3.009   -0.642  1.00 52.37  ? 454  ILE A CA  1 
ATOM   3413  C  C   . ILE A  1  428 ? 1.621   3.993   -0.860  1.00 52.17  ? 454  ILE A C   1 
ATOM   3414  O  O   . ILE A  1  428 ? 2.092   4.186   -1.977  1.00 50.50  ? 454  ILE A O   1 
ATOM   3415  C  CB  . ILE A  1  428 ? -0.247  2.822   -1.991  1.00 51.07  ? 454  ILE A CB  1 
ATOM   3416  C  CG1 . ILE A  1  428 ? -0.797  4.168   -2.472  1.00 52.32  ? 454  ILE A CG1 1 
ATOM   3417  C  CG2 . ILE A  1  428 ? -1.345  1.800   -1.841  1.00 50.31  ? 454  ILE A CG2 1 
ATOM   3418  C  CD1 . ILE A  1  428 ? -1.309  4.183   -3.902  1.00 51.56  ? 454  ILE A CD1 1 
ATOM   3419  N  N   . SER A  1  429 ? 2.043   4.623   0.225   1.00 54.27  ? 455  SER A N   1 
ATOM   3420  C  CA  . SER A  1  429 ? 3.118   5.609   0.166   1.00 58.69  ? 455  SER A CA  1 
ATOM   3421  C  C   . SER A  1  429 ? 4.434   4.931   -0.172  1.00 60.61  ? 455  SER A C   1 
ATOM   3422  O  O   . SER A  1  429 ? 4.719   3.842   0.316   1.00 62.73  ? 455  SER A O   1 
ATOM   3423  C  CB  . SER A  1  429 ? 3.273   6.337   1.513   1.00 58.95  ? 455  SER A CB  1 
ATOM   3424  O  OG  . SER A  1  429 ? 2.042   6.866   1.991   1.00 59.32  ? 455  SER A OG  1 
ATOM   3425  N  N   . HIS A  1  430 ? 5.226   5.572   -1.018  1.00 62.22  ? 456  HIS A N   1 
ATOM   3426  C  CA  . HIS A  1  430 ? 6.528   5.043   -1.401  1.00 64.42  ? 456  HIS A CA  1 
ATOM   3427  C  C   . HIS A  1  430 ? 6.516   3.583   -1.839  1.00 64.57  ? 456  HIS A C   1 
ATOM   3428  O  O   . HIS A  1  430 ? 7.383   2.801   -1.450  1.00 64.22  ? 456  HIS A O   1 
ATOM   3429  C  CB  . HIS A  1  430 ? 7.494   5.200   -0.237  1.00 67.16  ? 456  HIS A CB  1 
ATOM   3430  C  CG  . HIS A  1  430 ? 7.498   6.572   0.358   1.00 70.85  ? 456  HIS A CG  1 
ATOM   3431  N  ND1 . HIS A  1  430 ? 8.467   7.508   0.064   1.00 70.74  ? 456  HIS A ND1 1 
ATOM   3432  C  CD2 . HIS A  1  430 ? 6.654   7.161   1.239   1.00 70.66  ? 456  HIS A CD2 1 
ATOM   3433  C  CE1 . HIS A  1  430 ? 8.222   8.613   0.745   1.00 71.40  ? 456  HIS A CE1 1 
ATOM   3434  N  NE2 . HIS A  1  430 ? 7.129   8.429   1.465   1.00 71.08  ? 456  HIS A NE2 1 
ATOM   3435  N  N   . THR A  1  431 ? 5.533   3.213   -2.647  1.00 64.75  ? 457  THR A N   1 
ATOM   3436  C  CA  . THR A  1  431 ? 5.445   1.850   -3.137  1.00 64.80  ? 457  THR A CA  1 
ATOM   3437  C  C   . THR A  1  431 ? 5.886   1.820   -4.588  1.00 65.41  ? 457  THR A C   1 
ATOM   3438  O  O   . THR A  1  431 ? 5.631   0.855   -5.305  1.00 66.12  ? 457  THR A O   1 
ATOM   3439  C  CB  . THR A  1  431 ? 4.026   1.318   -3.038  1.00 64.78  ? 457  THR A CB  1 
ATOM   3440  O  OG1 . THR A  1  431 ? 3.147   2.128   -3.826  1.00 65.90  ? 457  THR A OG1 1 
ATOM   3441  C  CG2 . THR A  1  431 ? 3.577   1.347   -1.600  1.00 66.41  ? 457  THR A CG2 1 
ATOM   3442  N  N   . HIS A  1  432 ? 6.561   2.889   -5.002  1.00 65.13  ? 458  HIS A N   1 
ATOM   3443  C  CA  . HIS A  1  432 ? 7.057   3.021   -6.357  1.00 64.69  ? 458  HIS A CA  1 
ATOM   3444  C  C   . HIS A  1  432 ? 5.986   2.885   -7.417  1.00 64.53  ? 458  HIS A C   1 
ATOM   3445  O  O   . HIS A  1  432 ? 6.233   2.319   -8.479  1.00 65.54  ? 458  HIS A O   1 
ATOM   3446  C  CB  . HIS A  1  432 ? 8.151   2.007   -6.614  1.00 65.16  ? 458  HIS A CB  1 
ATOM   3447  C  CG  . HIS A  1  432 ? 9.421   2.302   -5.888  1.00 68.08  ? 458  HIS A CG  1 
ATOM   3448  N  ND1 . HIS A  1  432 ? 10.281  1.311   -5.465  1.00 69.86  ? 458  HIS A ND1 1 
ATOM   3449  C  CD2 . HIS A  1  432 ? 9.991   3.475   -5.530  1.00 68.92  ? 458  HIS A CD2 1 
ATOM   3450  C  CE1 . HIS A  1  432 ? 11.328  1.861   -4.877  1.00 70.27  ? 458  HIS A CE1 1 
ATOM   3451  N  NE2 . HIS A  1  432 ? 11.177  3.172   -4.904  1.00 71.12  ? 458  HIS A NE2 1 
ATOM   3452  N  N   . THR A  1  433 ? 4.796   3.405   -7.136  1.00 64.02  ? 459  THR A N   1 
ATOM   3453  C  CA  . THR A  1  433 ? 3.720   3.363   -8.113  1.00 64.92  ? 459  THR A CA  1 
ATOM   3454  C  C   . THR A  1  433 ? 3.933   4.480   -9.144  1.00 66.11  ? 459  THR A C   1 
ATOM   3455  O  O   . THR A  1  433 ? 4.603   5.476   -8.867  1.00 67.35  ? 459  THR A O   1 
ATOM   3456  C  CB  . THR A  1  433 ? 2.346   3.532   -7.432  1.00 63.95  ? 459  THR A CB  1 
ATOM   3457  O  OG1 . THR A  1  433 ? 2.171   2.492   -6.465  1.00 64.94  ? 459  THR A OG1 1 
ATOM   3458  C  CG2 . THR A  1  433 ? 1.215   3.438   -8.442  1.00 63.02  ? 459  THR A CG2 1 
ATOM   3459  N  N   . ARG A  1  434 ? 3.390   4.285   -10.341 1.00 66.84  ? 460  ARG A N   1 
ATOM   3460  C  CA  . ARG A  1  434 ? 3.482   5.247   -11.434 1.00 67.88  ? 460  ARG A CA  1 
ATOM   3461  C  C   . ARG A  1  434 ? 2.072   5.283   -12.014 1.00 67.89  ? 460  ARG A C   1 
ATOM   3462  O  O   . ARG A  1  434 ? 1.791   4.608   -13.004 1.00 68.98  ? 460  ARG A O   1 
ATOM   3463  C  CB  . ARG A  1  434 ? 4.463   4.738   -12.481 1.00 69.90  ? 460  ARG A CB  1 
ATOM   3464  C  CG  . ARG A  1  434 ? 4.477   5.511   -13.774 1.00 73.80  ? 460  ARG A CG  1 
ATOM   3465  C  CD  . ARG A  1  434 ? 5.159   6.839   -13.606 1.00 78.32  ? 460  ARG A CD  1 
ATOM   3466  N  NE  . ARG A  1  434 ? 6.175   7.059   -14.635 1.00 84.27  ? 460  ARG A NE  1 
ATOM   3467  C  CZ  . ARG A  1  434 ? 5.943   7.063   -15.952 1.00 87.71  ? 460  ARG A CZ  1 
ATOM   3468  N  NH1 . ARG A  1  434 ? 4.717   6.857   -16.433 1.00 88.06  ? 460  ARG A NH1 1 
ATOM   3469  N  NH2 . ARG A  1  434 ? 6.947   7.280   -16.802 1.00 88.81  ? 460  ARG A NH2 1 
ATOM   3470  N  N   . VAL A  1  435 ? 1.183   6.050   -11.386 1.00 66.51  ? 461  VAL A N   1 
ATOM   3471  C  CA  . VAL A  1  435 ? -0.204  6.125   -11.828 1.00 64.10  ? 461  VAL A CA  1 
ATOM   3472  C  C   . VAL A  1  435 ? -0.307  6.425   -13.312 1.00 63.60  ? 461  VAL A C   1 
ATOM   3473  O  O   . VAL A  1  435 ? 0.268   7.398   -13.806 1.00 63.37  ? 461  VAL A O   1 
ATOM   3474  C  CB  . VAL A  1  435 ? -0.966  7.186   -11.040 1.00 63.68  ? 461  VAL A CB  1 
ATOM   3475  C  CG1 . VAL A  1  435 ? -2.470  6.919   -11.133 1.00 63.27  ? 461  VAL A CG1 1 
ATOM   3476  C  CG2 . VAL A  1  435 ? -0.496  7.181   -9.601  1.00 61.87  ? 461  VAL A CG2 1 
ATOM   3477  N  N   . ALA A  1  436 ? -1.030  5.572   -14.028 1.00 62.66  ? 462  ALA A N   1 
ATOM   3478  C  CA  . ALA A  1  436 ? -1.194  5.747   -15.463 1.00 62.15  ? 462  ALA A CA  1 
ATOM   3479  C  C   . ALA A  1  436 ? -2.476  5.094   -15.926 1.00 62.66  ? 462  ALA A C   1 
ATOM   3480  O  O   . ALA A  1  436 ? -2.544  4.548   -17.024 1.00 63.64  ? 462  ALA A O   1 
ATOM   3481  C  CB  . ALA A  1  436 ? -0.016  5.158   -16.203 1.00 60.47  ? 462  ALA A CB  1 
ATOM   3482  N  N   . PHE A  1  437 ? -3.488  5.150   -15.073 1.00 62.82  ? 463  PHE A N   1 
ATOM   3483  C  CA  . PHE A  1  437 ? -4.795  4.597   -15.389 1.00 63.80  ? 463  PHE A CA  1 
ATOM   3484  C  C   . PHE A  1  437 ? -5.809  5.314   -14.517 1.00 66.04  ? 463  PHE A C   1 
ATOM   3485  O  O   . PHE A  1  437 ? -5.786  5.208   -13.289 1.00 66.22  ? 463  PHE A O   1 
ATOM   3486  C  CB  . PHE A  1  437 ? -4.838  3.096   -15.121 1.00 61.57  ? 463  PHE A CB  1 
ATOM   3487  C  CG  . PHE A  1  437 ? -6.187  2.474   -15.371 1.00 61.13  ? 463  PHE A CG  1 
ATOM   3488  C  CD1 . PHE A  1  437 ? -6.839  2.651   -16.585 1.00 60.98  ? 463  PHE A CD1 1 
ATOM   3489  C  CD2 . PHE A  1  437 ? -6.796  1.682   -14.402 1.00 61.18  ? 463  PHE A CD2 1 
ATOM   3490  C  CE1 . PHE A  1  437 ? -8.079  2.041   -16.828 1.00 61.01  ? 463  PHE A CE1 1 
ATOM   3491  C  CE2 . PHE A  1  437 ? -8.035  1.067   -14.632 1.00 60.23  ? 463  PHE A CE2 1 
ATOM   3492  C  CZ  . PHE A  1  437 ? -8.677  1.245   -15.846 1.00 60.62  ? 463  PHE A CZ  1 
ATOM   3493  N  N   . ASN A  1  438 ? -6.705  6.051   -15.160 1.00 68.58  ? 464  ASN A N   1 
ATOM   3494  C  CA  . ASN A  1  438 ? -7.715  6.813   -14.442 1.00 70.46  ? 464  ASN A CA  1 
ATOM   3495  C  C   . ASN A  1  438 ? -8.786  5.964   -13.760 1.00 70.64  ? 464  ASN A C   1 
ATOM   3496  O  O   . ASN A  1  438 ? -9.810  6.476   -13.307 1.00 71.93  ? 464  ASN A O   1 
ATOM   3497  C  CB  . ASN A  1  438 ? -8.328  7.840   -15.396 1.00 71.22  ? 464  ASN A CB  1 
ATOM   3498  C  CG  . ASN A  1  438 ? -7.396  9.021   -15.643 1.00 72.33  ? 464  ASN A CG  1 
ATOM   3499  O  OD1 . ASN A  1  438 ? -6.226  8.854   -15.994 1.00 72.76  ? 464  ASN A OD1 1 
ATOM   3500  N  ND2 . ASN A  1  438 ? -7.914  10.223  -15.451 1.00 74.65  ? 464  ASN A ND2 1 
ATOM   3501  N  N   . GLY A  1  439 ? -8.528  4.663   -13.670 1.00 70.30  ? 465  GLY A N   1 
ATOM   3502  C  CA  . GLY A  1  439 ? -9.453  3.755   -13.004 1.00 68.32  ? 465  GLY A CA  1 
ATOM   3503  C  C   . GLY A  1  439 ? -8.718  3.095   -11.846 1.00 66.61  ? 465  GLY A C   1 
ATOM   3504  O  O   . GLY A  1  439 ? -9.195  2.137   -11.228 1.00 64.61  ? 465  GLY A O   1 
ATOM   3505  N  N   . ILE A  1  440 ? -7.545  3.646   -11.543 1.00 64.89  ? 466  ILE A N   1 
ATOM   3506  C  CA  . ILE A  1  440 ? -6.696  3.121   -10.495 1.00 63.48  ? 466  ILE A CA  1 
ATOM   3507  C  C   . ILE A  1  440 ? -7.380  2.959   -9.149  1.00 64.30  ? 466  ILE A C   1 
ATOM   3508  O  O   . ILE A  1  440 ? -7.038  2.046   -8.399  1.00 65.25  ? 466  ILE A O   1 
ATOM   3509  C  CB  . ILE A  1  440 ? -5.437  3.985   -10.339 1.00 61.18  ? 466  ILE A CB  1 
ATOM   3510  C  CG1 . ILE A  1  440 ? -4.495  3.359   -9.320  1.00 59.47  ? 466  ILE A CG1 1 
ATOM   3511  C  CG2 . ILE A  1  440 ? -5.817  5.374   -9.921  1.00 61.02  ? 466  ILE A CG2 1 
ATOM   3512  C  CD1 . ILE A  1  440 ? -3.106  3.932   -9.377  1.00 59.64  ? 466  ILE A CD1 1 
ATOM   3513  N  N   . PHE A  1  441 ? -8.360  3.808   -8.849  1.00 64.65  ? 467  PHE A N   1 
ATOM   3514  C  CA  . PHE A  1  441 ? -9.039  3.715   -7.560  1.00 64.15  ? 467  PHE A CA  1 
ATOM   3515  C  C   . PHE A  1  441 ? -10.513 3.316   -7.589  1.00 63.46  ? 467  PHE A C   1 
ATOM   3516  O  O   . PHE A  1  441 ? -11.208 3.432   -6.583  1.00 62.74  ? 467  PHE A O   1 
ATOM   3517  C  CB  . PHE A  1  441 ? -8.878  5.034   -6.796  1.00 64.89  ? 467  PHE A CB  1 
ATOM   3518  C  CG  . PHE A  1  441 ? -7.447  5.371   -6.432  1.00 66.17  ? 467  PHE A CG  1 
ATOM   3519  C  CD1 . PHE A  1  441 ? -6.834  6.524   -6.928  1.00 66.23  ? 467  PHE A CD1 1 
ATOM   3520  C  CD2 . PHE A  1  441 ? -6.721  4.550   -5.574  1.00 67.27  ? 467  PHE A CD2 1 
ATOM   3521  C  CE1 . PHE A  1  441 ? -5.515  6.863   -6.569  1.00 66.16  ? 467  PHE A CE1 1 
ATOM   3522  C  CE2 . PHE A  1  441 ? -5.403  4.875   -5.207  1.00 68.04  ? 467  PHE A CE2 1 
ATOM   3523  C  CZ  . PHE A  1  441 ? -4.796  6.038   -5.708  1.00 67.03  ? 467  PHE A CZ  1 
ATOM   3524  N  N   . ASN A  1  442 ? -10.990 2.819   -8.720  1.00 64.47  ? 468  ASN A N   1 
ATOM   3525  C  CA  . ASN A  1  442 ? -12.394 2.422   -8.807  1.00 67.18  ? 468  ASN A CA  1 
ATOM   3526  C  C   . ASN A  1  442 ? -12.782 1.306   -7.836  1.00 67.58  ? 468  ASN A C   1 
ATOM   3527  O  O   . ASN A  1  442 ? -12.178 0.232   -7.814  1.00 67.93  ? 468  ASN A O   1 
ATOM   3528  C  CB  . ASN A  1  442 ? -12.761 1.978   -10.226 1.00 69.50  ? 468  ASN A CB  1 
ATOM   3529  C  CG  . ASN A  1  442 ? -12.648 3.098   -11.248 1.00 71.31  ? 468  ASN A CG  1 
ATOM   3530  O  OD1 . ASN A  1  442 ? -13.099 2.949   -12.387 1.00 73.01  ? 468  ASN A OD1 1 
ATOM   3531  N  ND2 . ASN A  1  442 ? -12.035 4.214   -10.858 1.00 70.32  ? 468  ASN A ND2 1 
ATOM   3532  N  N   . GLY A  1  443 ? -13.820 1.563   -7.052  1.00 68.14  ? 469  GLY A N   1 
ATOM   3533  C  CA  . GLY A  1  443 ? -14.286 0.593   -6.084  1.00 67.63  ? 469  GLY A CA  1 
ATOM   3534  C  C   . GLY A  1  443 ? -14.169 1.144   -4.675  1.00 67.73  ? 469  GLY A C   1 
ATOM   3535  O  O   . GLY A  1  443 ? -14.944 0.781   -3.782  1.00 67.36  ? 469  GLY A O   1 
ATOM   3536  N  N   . LEU A  1  444 ? -13.210 2.045   -4.486  1.00 67.74  ? 470  LEU A N   1 
ATOM   3537  C  CA  . LEU A  1  444 ? -12.963 2.645   -3.180  1.00 69.50  ? 470  LEU A CA  1 
ATOM   3538  C  C   . LEU A  1  444 ? -13.966 3.722   -2.731  1.00 71.48  ? 470  LEU A C   1 
ATOM   3539  O  O   . LEU A  1  444 ? -13.586 4.867   -2.455  1.00 72.19  ? 470  LEU A O   1 
ATOM   3540  C  CB  . LEU A  1  444 ? -11.550 3.219   -3.156  1.00 67.12  ? 470  LEU A CB  1 
ATOM   3541  C  CG  . LEU A  1  444 ? -10.450 2.208   -3.458  1.00 64.76  ? 470  LEU A CG  1 
ATOM   3542  C  CD1 . LEU A  1  444 ? -9.109  2.909   -3.362  1.00 63.37  ? 470  LEU A CD1 1 
ATOM   3543  C  CD2 . LEU A  1  444 ? -10.535 1.039   -2.481  1.00 63.47  ? 470  LEU A CD2 1 
ATOM   3544  N  N   . SER A  1  445 ? -15.238 3.336   -2.635  1.00 72.95  ? 471  SER A N   1 
ATOM   3545  C  CA  . SER A  1  445 ? -16.314 4.233   -2.216  1.00 73.58  ? 471  SER A CA  1 
ATOM   3546  C  C   . SER A  1  445 ? -16.115 4.754   -0.790  1.00 74.41  ? 471  SER A C   1 
ATOM   3547  O  O   . SER A  1  445 ? -15.844 5.941   -0.569  1.00 76.19  ? 471  SER A O   1 
ATOM   3548  C  CB  . SER A  1  445 ? -17.645 3.492   -2.285  1.00 72.98  ? 471  SER A CB  1 
ATOM   3549  O  OG  . SER A  1  445 ? -17.720 2.750   -3.484  1.00 74.97  ? 471  SER A OG  1 
ATOM   3550  N  N   . SER A  1  446 ? -16.251 3.848   0.171   1.00 72.85  ? 472  SER A N   1 
ATOM   3551  C  CA  . SER A  1  446 ? -16.124 4.169   1.582   1.00 71.23  ? 472  SER A CA  1 
ATOM   3552  C  C   . SER A  1  446 ? -14.797 4.802   2.001   1.00 70.35  ? 472  SER A C   1 
ATOM   3553  O  O   . SER A  1  446 ? -14.697 5.369   3.090   1.00 69.74  ? 472  SER A O   1 
ATOM   3554  C  CB  . SER A  1  446 ? -16.359 2.894   2.390   1.00 72.33  ? 472  SER A CB  1 
ATOM   3555  O  OG  . SER A  1  446 ? -17.576 2.277   2.005   1.00 73.00  ? 472  SER A OG  1 
ATOM   3556  N  N   . LEU A  1  447 ? -13.788 4.717   1.138   1.00 70.12  ? 473  LEU A N   1 
ATOM   3557  C  CA  . LEU A  1  447 ? -12.465 5.242   1.465   1.00 70.76  ? 473  LEU A CA  1 
ATOM   3558  C  C   . LEU A  1  447 ? -12.506 6.586   2.174   1.00 70.96  ? 473  LEU A C   1 
ATOM   3559  O  O   . LEU A  1  447 ? -13.185 7.500   1.714   1.00 73.59  ? 473  LEU A O   1 
ATOM   3560  C  CB  . LEU A  1  447 ? -11.604 5.358   0.200   1.00 70.30  ? 473  LEU A CB  1 
ATOM   3561  C  CG  . LEU A  1  447 ? -10.085 5.501   0.422   1.00 70.04  ? 473  LEU A CG  1 
ATOM   3562  C  CD1 . LEU A  1  447 ? -9.534  4.239   1.079   1.00 69.59  ? 473  LEU A CD1 1 
ATOM   3563  C  CD2 . LEU A  1  447 ? -9.392  5.724   -0.894  1.00 69.44  ? 473  LEU A CD2 1 
ATOM   3564  N  N   . GLU A  1  448 ? -11.780 6.701   3.286   1.00 70.02  ? 474  GLU A N   1 
ATOM   3565  C  CA  . GLU A  1  448 ? -11.718 7.947   4.039   1.00 69.68  ? 474  GLU A CA  1 
ATOM   3566  C  C   . GLU A  1  448 ? -10.303 8.511   4.153   1.00 68.93  ? 474  GLU A C   1 
ATOM   3567  O  O   . GLU A  1  448 ? -10.119 9.718   4.261   1.00 68.60  ? 474  GLU A O   1 
ATOM   3568  C  CB  . GLU A  1  448 ? -12.325 7.745   5.414   1.00 70.39  ? 474  GLU A CB  1 
ATOM   3569  C  CG  . GLU A  1  448 ? -13.819 7.611   5.332   1.00 73.78  ? 474  GLU A CG  1 
ATOM   3570  C  CD  . GLU A  1  448 ? -14.438 7.158   6.630   1.00 77.07  ? 474  GLU A CD  1 
ATOM   3571  O  OE1 . GLU A  1  448 ? -14.078 7.720   7.699   1.00 78.29  ? 474  GLU A OE1 1 
ATOM   3572  O  OE2 . GLU A  1  448 ? -15.293 6.245   6.576   1.00 77.19  ? 474  GLU A OE2 1 
ATOM   3573  N  N   . VAL A  1  449 ? -9.303  7.638   4.138   1.00 67.84  ? 475  VAL A N   1 
ATOM   3574  C  CA  . VAL A  1  449 ? -7.920  8.083   4.202   1.00 65.75  ? 475  VAL A CA  1 
ATOM   3575  C  C   . VAL A  1  449 ? -7.237  7.501   2.974   1.00 65.13  ? 475  VAL A C   1 
ATOM   3576  O  O   . VAL A  1  449 ? -7.628  6.451   2.483   1.00 64.41  ? 475  VAL A O   1 
ATOM   3577  C  CB  . VAL A  1  449 ? -7.221  7.600   5.481   1.00 64.93  ? 475  VAL A CB  1 
ATOM   3578  C  CG1 . VAL A  1  449 ? -5.810  8.186   5.562   1.00 63.86  ? 475  VAL A CG1 1 
ATOM   3579  C  CG2 . VAL A  1  449 ? -8.024  8.026   6.682   1.00 63.52  ? 475  VAL A CG2 1 
ATOM   3580  N  N   . LEU A  1  450 ? -6.227  8.192   2.473   1.00 64.66  ? 476  LEU A N   1 
ATOM   3581  C  CA  . LEU A  1  450 ? -5.527  7.743   1.279   1.00 64.31  ? 476  LEU A CA  1 
ATOM   3582  C  C   . LEU A  1  450 ? -4.119  8.333   1.287   1.00 64.11  ? 476  LEU A C   1 
ATOM   3583  O  O   . LEU A  1  450 ? -3.925  9.497   0.963   1.00 65.31  ? 476  LEU A O   1 
ATOM   3584  C  CB  . LEU A  1  450 ? -6.299  8.217   0.034   1.00 63.94  ? 476  LEU A CB  1 
ATOM   3585  C  CG  . LEU A  1  450 ? -5.924  7.810   -1.403  1.00 64.63  ? 476  LEU A CG  1 
ATOM   3586  C  CD1 . LEU A  1  450 ? -4.466  8.160   -1.729  1.00 64.27  ? 476  LEU A CD1 1 
ATOM   3587  C  CD2 . LEU A  1  450 ? -6.159  6.333   -1.553  1.00 64.89  ? 476  LEU A CD2 1 
ATOM   3588  N  N   . LYS A  1  451 ? -3.132  7.540   1.664   1.00 63.82  ? 477  LYS A N   1 
ATOM   3589  C  CA  . LYS A  1  451 ? -1.774  8.049   1.687   1.00 65.09  ? 477  LYS A CA  1 
ATOM   3590  C  C   . LYS A  1  451 ? -0.987  7.516   0.499   1.00 65.26  ? 477  LYS A C   1 
ATOM   3591  O  O   . LYS A  1  451 ? -0.591  6.362   0.482   1.00 65.32  ? 477  LYS A O   1 
ATOM   3592  C  CB  . LYS A  1  451 ? -1.056  7.650   2.986   1.00 65.24  ? 477  LYS A CB  1 
ATOM   3593  C  CG  . LYS A  1  451 ? -1.761  8.012   4.280   1.00 64.66  ? 477  LYS A CG  1 
ATOM   3594  C  CD  . LYS A  1  451 ? -0.801  7.839   5.447   1.00 65.05  ? 477  LYS A CD  1 
ATOM   3595  C  CE  . LYS A  1  451 ? -1.500  7.943   6.792   1.00 66.52  ? 477  LYS A CE  1 
ATOM   3596  N  NZ  . LYS A  1  451 ? -0.572  7.640   7.926   1.00 66.33  ? 477  LYS A NZ  1 
ATOM   3597  N  N   . MET A  1  452 ? -0.762  8.345   -0.506  1.00 66.21  ? 478  MET A N   1 
ATOM   3598  C  CA  . MET A  1  452 ? 0.005   7.880   -1.641  1.00 66.46  ? 478  MET A CA  1 
ATOM   3599  C  C   . MET A  1  452 ? 1.202   8.771   -1.895  1.00 66.01  ? 478  MET A C   1 
ATOM   3600  O  O   . MET A  1  452 ? 1.526   9.082   -3.041  1.00 66.84  ? 478  MET A O   1 
ATOM   3601  C  CB  . MET A  1  452 ? -0.878  7.768   -2.893  1.00 67.87  ? 478  MET A CB  1 
ATOM   3602  C  CG  . MET A  1  452 ? -1.503  9.042   -3.426  1.00 69.40  ? 478  MET A CG  1 
ATOM   3603  S  SD  . MET A  1  452 ? -2.554  8.632   -4.875  1.00 72.93  ? 478  MET A SD  1 
ATOM   3604  C  CE  . MET A  1  452 ? -1.307  8.377   -6.098  1.00 69.41  ? 478  MET A CE  1 
ATOM   3605  N  N   . ALA A  1  453 ? 1.863   9.167   -0.812  1.00 64.12  ? 479  ALA A N   1 
ATOM   3606  C  CA  . ALA A  1  453 ? 3.038   10.012  -0.916  1.00 64.78  ? 479  ALA A CA  1 
ATOM   3607  C  C   . ALA A  1  453 ? 4.186   9.251   -1.579  1.00 66.04  ? 479  ALA A C   1 
ATOM   3608  O  O   . ALA A  1  453 ? 4.070   8.061   -1.840  1.00 66.95  ? 479  ALA A O   1 
ATOM   3609  C  CB  . ALA A  1  453 ? 3.454   10.475  0.452   1.00 63.26  ? 479  ALA A CB  1 
ATOM   3610  N  N   . GLY A  1  454 ? 5.280   9.960   -1.862  1.00 67.27  ? 480  GLY A N   1 
ATOM   3611  C  CA  . GLY A  1  454 ? 6.468   9.370   -2.465  1.00 67.24  ? 480  GLY A CA  1 
ATOM   3612  C  C   . GLY A  1  454 ? 6.432   8.730   -3.850  1.00 67.80  ? 480  GLY A C   1 
ATOM   3613  O  O   . GLY A  1  454 ? 7.466   8.242   -4.319  1.00 67.44  ? 480  GLY A O   1 
ATOM   3614  N  N   . ASN A  1  455 ? 5.284   8.727   -4.522  1.00 67.64  ? 481  ASN A N   1 
ATOM   3615  C  CA  . ASN A  1  455 ? 5.222   8.094   -5.837  1.00 68.10  ? 481  ASN A CA  1 
ATOM   3616  C  C   . ASN A  1  455 ? 5.457   9.016   -7.027  1.00 68.90  ? 481  ASN A C   1 
ATOM   3617  O  O   . ASN A  1  455 ? 6.407   9.813   -7.034  1.00 68.28  ? 481  ASN A O   1 
ATOM   3618  C  CB  . ASN A  1  455 ? 3.896   7.351   -5.997  1.00 66.63  ? 481  ASN A CB  1 
ATOM   3619  C  CG  . ASN A  1  455 ? 3.757   6.215   -5.009  1.00 66.70  ? 481  ASN A CG  1 
ATOM   3620  O  OD1 . ASN A  1  455 ? 4.663   5.402   -4.856  1.00 65.27  ? 481  ASN A OD1 1 
ATOM   3621  N  ND2 . ASN A  1  455 ? 2.624   6.154   -4.328  1.00 67.42  ? 481  ASN A ND2 1 
ATOM   3622  N  N   . SER A  1  456 ? 4.606   8.879   -8.044  1.00 69.80  ? 482  SER A N   1 
ATOM   3623  C  CA  . SER A  1  456 ? 4.704   9.690   -9.259  1.00 70.40  ? 482  SER A CA  1 
ATOM   3624  C  C   . SER A  1  456 ? 3.533   9.439   -10.200 1.00 70.25  ? 482  SER A C   1 
ATOM   3625  O  O   . SER A  1  456 ? 2.839   8.422   -10.111 1.00 69.05  ? 482  SER A O   1 
ATOM   3626  C  CB  . SER A  1  456 ? 5.981   9.376   -10.022 1.00 70.01  ? 482  SER A CB  1 
ATOM   3627  O  OG  . SER A  1  456 ? 5.789   8.221   -10.819 1.00 70.96  ? 482  SER A OG  1 
ATOM   3628  N  N   . PHE A  1  457 ? 3.328   10.377  -11.115 1.00 71.09  ? 483  PHE A N   1 
ATOM   3629  C  CA  . PHE A  1  457 ? 2.252   10.254  -12.072 1.00 70.92  ? 483  PHE A CA  1 
ATOM   3630  C  C   . PHE A  1  457 ? 2.787   10.368  -13.473 1.00 73.12  ? 483  PHE A C   1 
ATOM   3631  O  O   . PHE A  1  457 ? 3.873   10.915  -13.698 1.00 71.76  ? 483  PHE A O   1 
ATOM   3632  C  CB  . PHE A  1  457 ? 1.194   11.328  -11.848 1.00 66.98  ? 483  PHE A CB  1 
ATOM   3633  C  CG  . PHE A  1  457 ? 0.441   11.176  -10.562 1.00 64.48  ? 483  PHE A CG  1 
ATOM   3634  C  CD1 . PHE A  1  457 ? 1.042   11.485  -9.346  1.00 62.81  ? 483  PHE A CD1 1 
ATOM   3635  C  CD2 . PHE A  1  457 ? -0.881  10.745  -10.567 1.00 63.53  ? 483  PHE A CD2 1 
ATOM   3636  C  CE1 . PHE A  1  457 ? 0.330   11.370  -8.148  1.00 62.21  ? 483  PHE A CE1 1 
ATOM   3637  C  CE2 . PHE A  1  457 ? -1.609  10.624  -9.378  1.00 62.16  ? 483  PHE A CE2 1 
ATOM   3638  C  CZ  . PHE A  1  457 ? -1.002  10.938  -8.167  1.00 61.69  ? 483  PHE A CZ  1 
ATOM   3639  N  N   . GLN A  1  458 ? 2.012   9.829   -14.407 1.00 76.70  ? 484  GLN A N   1 
ATOM   3640  C  CA  . GLN A  1  458 ? 2.359   9.857   -15.817 1.00 79.79  ? 484  GLN A CA  1 
ATOM   3641  C  C   . GLN A  1  458 ? 2.286   11.311  -16.262 1.00 81.33  ? 484  GLN A C   1 
ATOM   3642  O  O   . GLN A  1  458 ? 1.262   11.981  -16.066 1.00 81.12  ? 484  GLN A O   1 
ATOM   3643  C  CB  . GLN A  1  458 ? 1.364   9.003   -16.617 1.00 79.77  ? 484  GLN A CB  1 
ATOM   3644  C  CG  . GLN A  1  458 ? 1.644   8.948   -18.110 1.00 79.37  ? 484  GLN A CG  1 
ATOM   3645  C  CD  . GLN A  1  458 ? 0.632   8.097   -18.849 1.00 80.45  ? 484  GLN A CD  1 
ATOM   3646  O  OE1 . GLN A  1  458 ? -0.578  8.201   -18.619 1.00 80.07  ? 484  GLN A OE1 1 
ATOM   3647  N  NE2 . GLN A  1  458 ? 1.121   7.251   -19.752 1.00 80.76  ? 484  GLN A NE2 1 
ATOM   3648  N  N   . GLU A  1  459 ? 3.387   11.799  -16.824 1.00 82.56  ? 485  GLU A N   1 
ATOM   3649  C  CA  . GLU A  1  459 ? 3.464   13.168  -17.308 1.00 84.25  ? 485  GLU A CA  1 
ATOM   3650  C  C   . GLU A  1  459 ? 3.485   14.191  -16.174 1.00 83.55  ? 485  GLU A C   1 
ATOM   3651  O  O   . GLU A  1  459 ? 3.537   15.391  -16.411 1.00 85.25  ? 485  GLU A O   1 
ATOM   3652  C  CB  . GLU A  1  459 ? 2.285   13.438  -18.252 1.00 86.84  ? 485  GLU A CB  1 
ATOM   3653  C  CG  . GLU A  1  459 ? 2.665   14.114  -19.557 1.00 91.08  ? 485  GLU A CG  1 
ATOM   3654  C  CD  . GLU A  1  459 ? 3.963   13.582  -20.134 1.00 94.11  ? 485  GLU A CD  1 
ATOM   3655  O  OE1 . GLU A  1  459 ? 5.039   14.014  -19.658 1.00 94.69  ? 485  GLU A OE1 1 
ATOM   3656  O  OE2 . GLU A  1  459 ? 3.908   12.717  -21.044 1.00 96.16  ? 485  GLU A OE2 1 
ATOM   3657  N  N   . ASN A  1  460 ? 3.446   13.717  -14.939 1.00 82.46  ? 486  ASN A N   1 
ATOM   3658  C  CA  . ASN A  1  460 ? 3.460   14.609  -13.788 1.00 80.72  ? 486  ASN A CA  1 
ATOM   3659  C  C   . ASN A  1  460 ? 2.204   15.459  -13.700 1.00 79.01  ? 486  ASN A C   1 
ATOM   3660  O  O   . ASN A  1  460 ? 2.172   16.472  -13.024 1.00 77.47  ? 486  ASN A O   1 
ATOM   3661  C  CB  . ASN A  1  460 ? 4.708   15.482  -13.830 1.00 80.27  ? 486  ASN A CB  1 
ATOM   3662  C  CG  . ASN A  1  460 ? 5.975   14.666  -13.672 1.00 81.14  ? 486  ASN A CG  1 
ATOM   3663  O  OD1 . ASN A  1  460 ? 7.086   15.185  -13.769 1.00 80.95  ? 486  ASN A OD1 1 
ATOM   3664  N  ND2 . ASN A  1  460 ? 5.810   13.371  -13.418 1.00 82.00  ? 486  ASN A ND2 1 
ATOM   3665  N  N   . PHE A  1  461 ? 1.164   15.016  -14.387 1.00 79.13  ? 487  PHE A N   1 
ATOM   3666  C  CA  . PHE A  1  461 ? -0.116  15.701  -14.389 1.00 80.58  ? 487  PHE A CA  1 
ATOM   3667  C  C   . PHE A  1  461 ? -1.064  14.865  -13.525 1.00 80.78  ? 487  PHE A C   1 
ATOM   3668  O  O   . PHE A  1  461 ? -1.167  13.657  -13.706 1.00 81.14  ? 487  PHE A O   1 
ATOM   3669  C  CB  . PHE A  1  461 ? -0.618  15.835  -15.842 1.00 79.27  ? 487  PHE A CB  1 
ATOM   3670  C  CG  . PHE A  1  461 ? -2.087  16.148  -15.967 1.00 79.34  ? 487  PHE A CG  1 
ATOM   3671  C  CD1 . PHE A  1  461 ? -3.033  15.121  -16.013 1.00 79.82  ? 487  PHE A CD1 1 
ATOM   3672  C  CD2 . PHE A  1  461 ? -2.528  17.465  -16.052 1.00 79.97  ? 487  PHE A CD2 1 
ATOM   3673  C  CE1 . PHE A  1  461 ? -4.408  15.391  -16.143 1.00 80.15  ? 487  PHE A CE1 1 
ATOM   3674  C  CE2 . PHE A  1  461 ? -3.903  17.757  -16.182 1.00 81.76  ? 487  PHE A CE2 1 
ATOM   3675  C  CZ  . PHE A  1  461 ? -4.847  16.710  -16.230 1.00 81.25  ? 487  PHE A CZ  1 
ATOM   3676  N  N   . LEU A  1  462 ? -1.734  15.503  -12.571 1.00 80.47  ? 488  LEU A N   1 
ATOM   3677  C  CA  . LEU A  1  462 ? -2.644  14.791  -11.689 1.00 81.11  ? 488  LEU A CA  1 
ATOM   3678  C  C   . LEU A  1  462 ? -4.040  14.662  -12.286 1.00 81.33  ? 488  LEU A C   1 
ATOM   3679  O  O   . LEU A  1  462 ? -4.787  15.625  -12.316 1.00 81.68  ? 488  LEU A O   1 
ATOM   3680  C  CB  . LEU A  1  462 ? -2.721  15.511  -10.342 1.00 82.39  ? 488  LEU A CB  1 
ATOM   3681  C  CG  . LEU A  1  462 ? -3.766  15.024  -9.333  1.00 84.12  ? 488  LEU A CG  1 
ATOM   3682  C  CD1 . LEU A  1  462 ? -3.559  13.551  -9.006  1.00 84.75  ? 488  LEU A CD1 1 
ATOM   3683  C  CD2 . LEU A  1  462 ? -3.655  15.859  -8.071  1.00 86.53  ? 488  LEU A CD2 1 
ATOM   3684  N  N   . PRO A  1  463 ? -4.411  13.460  -12.761 1.00 81.67  ? 489  PRO A N   1 
ATOM   3685  C  CA  . PRO A  1  463 ? -5.727  13.198  -13.364 1.00 81.15  ? 489  PRO A CA  1 
ATOM   3686  C  C   . PRO A  1  463 ? -6.944  13.177  -12.431 1.00 81.02  ? 489  PRO A C   1 
ATOM   3687  O  O   . PRO A  1  463 ? -6.843  13.397  -11.223 1.00 79.81  ? 489  PRO A O   1 
ATOM   3688  C  CB  . PRO A  1  463 ? -5.532  11.839  -14.045 1.00 80.98  ? 489  PRO A CB  1 
ATOM   3689  C  CG  . PRO A  1  463 ? -4.052  11.771  -14.303 1.00 80.65  ? 489  PRO A CG  1 
ATOM   3690  C  CD  . PRO A  1  463 ? -3.498  12.335  -13.022 1.00 81.24  ? 489  PRO A CD  1 
ATOM   3691  N  N   . ASP A  1  464 ? -8.095  12.888  -13.034 1.00 81.87  ? 490  ASP A N   1 
ATOM   3692  C  CA  . ASP A  1  464 ? -9.389  12.809  -12.351 1.00 83.51  ? 490  ASP A CA  1 
ATOM   3693  C  C   . ASP A  1  464 ? -9.661  11.398  -11.836 1.00 82.70  ? 490  ASP A C   1 
ATOM   3694  O  O   . ASP A  1  464 ? -10.587 10.723  -12.286 1.00 82.09  ? 490  ASP A O   1 
ATOM   3695  C  CB  . ASP A  1  464 ? -10.501 13.208  -13.326 1.00 86.82  ? 490  ASP A CB  1 
ATOM   3696  C  CG  . ASP A  1  464 ? -10.973 14.635  -13.126 1.00 89.34  ? 490  ASP A CG  1 
ATOM   3697  O  OD1 . ASP A  1  464 ? -11.629 14.897  -12.087 1.00 91.45  ? 490  ASP A OD1 1 
ATOM   3698  O  OD2 . ASP A  1  464 ? -10.687 15.487  -14.001 1.00 89.29  ? 490  ASP A OD2 1 
ATOM   3699  N  N   . ILE A  1  465 ? -8.866  10.971  -10.871 1.00 81.86  ? 491  ILE A N   1 
ATOM   3700  C  CA  . ILE A  1  465 ? -8.983  9.630   -10.320 1.00 81.04  ? 491  ILE A CA  1 
ATOM   3701  C  C   . ILE A  1  465 ? -9.705  9.538   -8.980  1.00 81.04  ? 491  ILE A C   1 
ATOM   3702  O  O   . ILE A  1  465 ? -9.925  8.446   -8.470  1.00 80.39  ? 491  ILE A O   1 
ATOM   3703  C  CB  . ILE A  1  465 ? -7.590  9.043   -10.163 1.00 80.01  ? 491  ILE A CB  1 
ATOM   3704  C  CG1 . ILE A  1  465 ? -6.713  10.048  -9.399  1.00 79.39  ? 491  ILE A CG1 1 
ATOM   3705  C  CG2 . ILE A  1  465 ? -7.015  8.735   -11.530 1.00 79.79  ? 491  ILE A CG2 1 
ATOM   3706  C  CD1 . ILE A  1  465 ? -5.239  9.703   -9.351  1.00 78.68  ? 491  ILE A CD1 1 
ATOM   3707  N  N   . PHE A  1  466 ? -10.093 10.679  -8.428  1.00 81.31  ? 492  PHE A N   1 
ATOM   3708  C  CA  . PHE A  1  466 ? -10.740 10.706  -7.129  1.00 81.80  ? 492  PHE A CA  1 
ATOM   3709  C  C   . PHE A  1  466 ? -12.255 10.871  -7.169  1.00 83.40  ? 492  PHE A C   1 
ATOM   3710  O  O   . PHE A  1  466 ? -12.921 10.910  -6.127  1.00 83.30  ? 492  PHE A O   1 
ATOM   3711  C  CB  . PHE A  1  466 ? -10.110 11.825  -6.311  1.00 78.86  ? 492  PHE A CB  1 
ATOM   3712  C  CG  . PHE A  1  466 ? -8.615  11.772  -6.288  1.00 76.56  ? 492  PHE A CG  1 
ATOM   3713  C  CD1 . PHE A  1  466 ? -7.957  10.739  -5.634  1.00 76.47  ? 492  PHE A CD1 1 
ATOM   3714  C  CD2 . PHE A  1  466 ? -7.865  12.753  -6.912  1.00 76.23  ? 492  PHE A CD2 1 
ATOM   3715  C  CE1 . PHE A  1  466 ? -6.564  10.689  -5.598  1.00 77.18  ? 492  PHE A CE1 1 
ATOM   3716  C  CE2 . PHE A  1  466 ? -6.473  12.717  -6.885  1.00 76.80  ? 492  PHE A CE2 1 
ATOM   3717  C  CZ  . PHE A  1  466 ? -5.819  11.682  -6.226  1.00 77.58  ? 492  PHE A CZ  1 
ATOM   3718  N  N   . THR A  1  467 ? -12.791 10.935  -8.382  1.00 85.29  ? 493  THR A N   1 
ATOM   3719  C  CA  . THR A  1  467 ? -14.224 11.133  -8.605  1.00 87.01  ? 493  THR A CA  1 
ATOM   3720  C  C   . THR A  1  467 ? -15.207 10.137  -7.962  1.00 86.70  ? 493  THR A C   1 
ATOM   3721  O  O   . THR A  1  467 ? -16.417 10.374  -7.958  1.00 86.10  ? 493  THR A O   1 
ATOM   3722  C  CB  . THR A  1  467 ? -14.521 11.239  -10.143 1.00 87.57  ? 493  THR A CB  1 
ATOM   3723  O  OG1 . THR A  1  467 ? -13.975 10.102  -10.823 1.00 86.08  ? 493  THR A OG1 1 
ATOM   3724  C  CG2 . THR A  1  467 ? -13.894 12.523  -10.731 1.00 87.32  ? 493  THR A CG2 1 
ATOM   3725  N  N   . GLU A  1  468 ? -14.702 9.037   -7.412  1.00 87.02  ? 494  GLU A N   1 
ATOM   3726  C  CA  . GLU A  1  468 ? -15.575 8.049   -6.784  1.00 87.55  ? 494  GLU A CA  1 
ATOM   3727  C  C   . GLU A  1  468 ? -15.386 8.032   -5.258  1.00 87.71  ? 494  GLU A C   1 
ATOM   3728  O  O   . GLU A  1  468 ? -16.253 7.552   -4.517  1.00 86.74  ? 494  GLU A O   1 
ATOM   3729  C  CB  . GLU A  1  468 ? -15.291 6.656   -7.370  1.00 88.50  ? 494  GLU A CB  1 
ATOM   3730  C  CG  . GLU A  1  468 ? -16.461 5.660   -7.231  1.00 90.80  ? 494  GLU A CG  1 
ATOM   3731  C  CD  . GLU A  1  468 ? -16.165 4.259   -7.798  1.00 91.21  ? 494  GLU A CD  1 
ATOM   3732  O  OE1 . GLU A  1  468 ? -15.581 4.158   -8.904  1.00 89.92  ? 494  GLU A OE1 1 
ATOM   3733  O  OE2 . GLU A  1  468 ? -16.540 3.257   -7.139  1.00 90.79  ? 494  GLU A OE2 1 
ATOM   3734  N  N   . LEU A  1  469 ? -14.257 8.575   -4.801  1.00 88.19  ? 495  LEU A N   1 
ATOM   3735  C  CA  . LEU A  1  469 ? -13.912 8.622   -3.378  1.00 89.06  ? 495  LEU A CA  1 
ATOM   3736  C  C   . LEU A  1  469 ? -14.658 9.736   -2.647  1.00 90.60  ? 495  LEU A C   1 
ATOM   3737  O  O   . LEU A  1  469 ? -14.088 10.801  -2.384  1.00 91.56  ? 495  LEU A O   1 
ATOM   3738  C  CB  . LEU A  1  469 ? -12.404 8.845   -3.216  1.00 87.28  ? 495  LEU A CB  1 
ATOM   3739  C  CG  . LEU A  1  469 ? -11.439 8.037   -4.091  1.00 85.03  ? 495  LEU A CG  1 
ATOM   3740  C  CD1 . LEU A  1  469 ? -10.007 8.343   -3.682  1.00 84.42  ? 495  LEU A CD1 1 
ATOM   3741  C  CD2 . LEU A  1  469 ? -11.716 6.560   -3.952  1.00 82.85  ? 495  LEU A CD2 1 
ATOM   3742  N  N   . ARG A  1  470 ? -15.918 9.481   -2.298  1.00 91.79  ? 496  ARG A N   1 
ATOM   3743  C  CA  . ARG A  1  470 ? -16.746 10.477  -1.620  1.00 92.19  ? 496  ARG A CA  1 
ATOM   3744  C  C   . ARG A  1  470 ? -16.378 10.847  -0.182  1.00 91.41  ? 496  ARG A C   1 
ATOM   3745  O  O   . ARG A  1  470 ? -15.939 11.978  0.070   1.00 91.65  ? 496  ARG A O   1 
ATOM   3746  C  CB  . ARG A  1  470 ? -18.216 10.058  -1.683  1.00 94.15  ? 496  ARG A CB  1 
ATOM   3747  C  CG  . ARG A  1  470 ? -18.935 10.592  -2.920  1.00 97.83  ? 496  ARG A CG  1 
ATOM   3748  C  CD  . ARG A  1  470 ? -18.946 12.124  -2.904  1.00 101.32 ? 496  ARG A CD  1 
ATOM   3749  N  NE  . ARG A  1  470 ? -19.495 12.729  -4.118  1.00 104.30 ? 496  ARG A NE  1 
ATOM   3750  C  CZ  . ARG A  1  470 ? -18.942 12.635  -5.325  1.00 106.40 ? 496  ARG A CZ  1 
ATOM   3751  N  NH1 . ARG A  1  470 ? -17.816 11.950  -5.490  1.00 107.54 ? 496  ARG A NH1 1 
ATOM   3752  N  NH2 . ARG A  1  470 ? -19.500 13.244  -6.368  1.00 107.04 ? 496  ARG A NH2 1 
ATOM   3753  N  N   . ASN A  1  471 ? -16.559 9.909   0.750   1.00 89.38  ? 497  ASN A N   1 
ATOM   3754  C  CA  . ASN A  1  471 ? -16.269 10.152  2.169   1.00 86.99  ? 497  ASN A CA  1 
ATOM   3755  C  C   . ASN A  1  471 ? -14.793 10.482  2.421   1.00 84.10  ? 497  ASN A C   1 
ATOM   3756  O  O   . ASN A  1  471 ? -14.385 10.686  3.561   1.00 83.24  ? 497  ASN A O   1 
ATOM   3757  C  CB  . ASN A  1  471 ? -16.671 8.934   3.024   1.00 88.75  ? 497  ASN A CB  1 
ATOM   3758  C  CG  . ASN A  1  471 ? -18.069 8.411   2.707   1.00 91.14  ? 497  ASN A CG  1 
ATOM   3759  O  OD1 . ASN A  1  471 ? -18.371 8.088   1.556   1.00 90.26  ? 497  ASN A OD1 1 
ATOM   3760  N  ND2 . ASN A  1  471 ? -18.916 8.307   3.730   1.00 94.87  ? 497  ASN A ND2 1 
ATOM   3761  N  N   . LEU A  1  472 ? -14.005 10.546  1.355   1.00 81.46  ? 498  LEU A N   1 
ATOM   3762  C  CA  . LEU A  1  472 ? -12.581 10.836  1.459   1.00 80.80  ? 498  LEU A CA  1 
ATOM   3763  C  C   . LEU A  1  472 ? -12.310 12.086  2.324   1.00 80.57  ? 498  LEU A C   1 
ATOM   3764  O  O   . LEU A  1  472 ? -12.609 13.200  1.907   1.00 82.56  ? 498  LEU A O   1 
ATOM   3765  C  CB  . LEU A  1  472 ? -12.011 11.002  0.036   1.00 79.86  ? 498  LEU A CB  1 
ATOM   3766  C  CG  . LEU A  1  472 ? -10.616 10.482  -0.373  1.00 79.75  ? 498  LEU A CG  1 
ATOM   3767  C  CD1 . LEU A  1  472 ? -9.567  11.592  -0.294  1.00 79.38  ? 498  LEU A CD1 1 
ATOM   3768  C  CD2 . LEU A  1  472 ? -10.235 9.293   0.508   1.00 79.21  ? 498  LEU A CD2 1 
ATOM   3769  N  N   . THR A  1  473 ? -11.739 11.898  3.518   1.00 78.94  ? 499  THR A N   1 
ATOM   3770  C  CA  . THR A  1  473 ? -11.439 13.010  4.431   1.00 77.23  ? 499  THR A CA  1 
ATOM   3771  C  C   . THR A  1  473 ? -9.955  13.396  4.560   1.00 77.07  ? 499  THR A C   1 
ATOM   3772  O  O   . THR A  1  473 ? -9.639  14.478  5.039   1.00 77.37  ? 499  THR A O   1 
ATOM   3773  C  CB  . THR A  1  473 ? -11.939 12.727  5.865   1.00 77.08  ? 499  THR A CB  1 
ATOM   3774  O  OG1 . THR A  1  473 ? -10.915 12.043  6.600   1.00 77.64  ? 499  THR A OG1 1 
ATOM   3775  C  CG2 . THR A  1  473 ? -13.206 11.880  5.847   1.00 75.91  ? 499  THR A CG2 1 
ATOM   3776  N  N   . PHE A  1  474 ? -9.045  12.509  4.170   1.00 77.61  ? 500  PHE A N   1 
ATOM   3777  C  CA  . PHE A  1  474 ? -7.604  12.790  4.247   1.00 76.94  ? 500  PHE A CA  1 
ATOM   3778  C  C   . PHE A  1  474 ? -6.974  12.376  2.918   1.00 76.80  ? 500  PHE A C   1 
ATOM   3779  O  O   . PHE A  1  474 ? -7.454  11.448  2.269   1.00 77.92  ? 500  PHE A O   1 
ATOM   3780  C  CB  . PHE A  1  474 ? -6.966  11.987  5.382   1.00 76.38  ? 500  PHE A CB  1 
ATOM   3781  C  CG  . PHE A  1  474 ? -5.600  12.483  5.794   1.00 76.08  ? 500  PHE A CG  1 
ATOM   3782  C  CD1 . PHE A  1  474 ? -5.447  13.256  6.942   1.00 75.17  ? 500  PHE A CD1 1 
ATOM   3783  C  CD2 . PHE A  1  474 ? -4.465  12.146  5.058   1.00 76.20  ? 500  PHE A CD2 1 
ATOM   3784  C  CE1 . PHE A  1  474 ? -4.185  13.685  7.354   1.00 75.34  ? 500  PHE A CE1 1 
ATOM   3785  C  CE2 . PHE A  1  474 ? -3.190  12.571  5.459   1.00 76.01  ? 500  PHE A CE2 1 
ATOM   3786  C  CZ  . PHE A  1  474 ? -3.050  13.340  6.612   1.00 75.61  ? 500  PHE A CZ  1 
ATOM   3787  N  N   . LEU A  1  475 ? -5.904  13.048  2.505   1.00 75.08  ? 501  LEU A N   1 
ATOM   3788  C  CA  . LEU A  1  475 ? -5.276  12.701  1.236   1.00 73.53  ? 501  LEU A CA  1 
ATOM   3789  C  C   . LEU A  1  475 ? -3.877  13.269  1.096   1.00 73.21  ? 501  LEU A C   1 
ATOM   3790  O  O   . LEU A  1  475 ? -3.699  14.434  0.743   1.00 73.12  ? 501  LEU A O   1 
ATOM   3791  C  CB  . LEU A  1  475 ? -6.155  13.169  0.069   1.00 73.72  ? 501  LEU A CB  1 
ATOM   3792  C  CG  . LEU A  1  475 ? -5.621  13.125  -1.370  1.00 75.51  ? 501  LEU A CG  1 
ATOM   3793  C  CD1 . LEU A  1  475 ? -5.245  11.716  -1.773  1.00 76.64  ? 501  LEU A CD1 1 
ATOM   3794  C  CD2 . LEU A  1  475 ? -6.685  13.652  -2.310  1.00 75.27  ? 501  LEU A CD2 1 
ATOM   3795  N  N   . ASP A  1  476 ? -2.884  12.434  1.386   1.00 73.19  ? 502  ASP A N   1 
ATOM   3796  C  CA  . ASP A  1  476 ? -1.490  12.837  1.272   1.00 73.24  ? 502  ASP A CA  1 
ATOM   3797  C  C   . ASP A  1  476 ? -1.168  12.628  -0.205  1.00 73.58  ? 502  ASP A C   1 
ATOM   3798  O  O   . ASP A  1  476 ? -1.601  11.635  -0.794  1.00 74.56  ? 502  ASP A O   1 
ATOM   3799  C  CB  . ASP A  1  476 ? -0.586  11.949  2.143   1.00 72.27  ? 502  ASP A CB  1 
ATOM   3800  C  CG  . ASP A  1  476 ? 0.847   12.461  2.217   1.00 73.12  ? 502  ASP A CG  1 
ATOM   3801  O  OD1 . ASP A  1  476 ? 1.313   13.063  1.223   1.00 72.64  ? 502  ASP A OD1 1 
ATOM   3802  O  OD2 . ASP A  1  476 ? 1.516   12.251  3.259   1.00 72.72  ? 502  ASP A OD2 1 
ATOM   3803  N  N   . LEU A  1  477 ? -0.434  13.569  -0.798  1.00 73.30  ? 503  LEU A N   1 
ATOM   3804  C  CA  . LEU A  1  477 ? -0.047  13.499  -2.207  1.00 71.26  ? 503  LEU A CA  1 
ATOM   3805  C  C   . LEU A  1  477 ? 1.302   14.169  -2.352  1.00 70.28  ? 503  LEU A C   1 
ATOM   3806  O  O   . LEU A  1  477 ? 1.618   14.713  -3.405  1.00 69.51  ? 503  LEU A O   1 
ATOM   3807  C  CB  . LEU A  1  477 ? -1.073  14.222  -3.090  1.00 70.70  ? 503  LEU A CB  1 
ATOM   3808  C  CG  . LEU A  1  477 ? -2.218  13.394  -3.690  1.00 70.95  ? 503  LEU A CG  1 
ATOM   3809  C  CD1 . LEU A  1  477 ? -3.404  14.258  -4.061  1.00 72.29  ? 503  LEU A CD1 1 
ATOM   3810  C  CD2 . LEU A  1  477 ? -1.699  12.686  -4.911  1.00 72.40  ? 503  LEU A CD2 1 
ATOM   3811  N  N   . SER A  1  478 ? 2.095   14.134  -1.287  1.00 69.78  ? 504  SER A N   1 
ATOM   3812  C  CA  . SER A  1  478 ? 3.402   14.763  -1.317  1.00 70.59  ? 504  SER A CA  1 
ATOM   3813  C  C   . SER A  1  478 ? 4.444   13.936  -2.044  1.00 71.43  ? 504  SER A C   1 
ATOM   3814  O  O   . SER A  1  478 ? 4.196   12.808  -2.433  1.00 71.63  ? 504  SER A O   1 
ATOM   3815  C  CB  . SER A  1  478 ? 3.882   15.062  0.101   1.00 70.73  ? 504  SER A CB  1 
ATOM   3816  O  OG  . SER A  1  478 ? 4.135   13.879  0.827   1.00 72.03  ? 504  SER A OG  1 
ATOM   3817  N  N   . GLN A  1  479 ? 5.609   14.530  -2.243  1.00 73.54  ? 505  GLN A N   1 
ATOM   3818  C  CA  . GLN A  1  479 ? 6.730   13.888  -2.918  1.00 74.70  ? 505  GLN A CA  1 
ATOM   3819  C  C   . GLN A  1  479 ? 6.406   13.145  -4.223  1.00 75.55  ? 505  GLN A C   1 
ATOM   3820  O  O   . GLN A  1  479 ? 7.199   12.323  -4.675  1.00 76.14  ? 505  GLN A O   1 
ATOM   3821  C  CB  . GLN A  1  479 ? 7.435   12.960  -1.929  1.00 73.71  ? 505  GLN A CB  1 
ATOM   3822  C  CG  . GLN A  1  479 ? 7.656   13.634  -0.588  1.00 75.55  ? 505  GLN A CG  1 
ATOM   3823  C  CD  . GLN A  1  479 ? 8.655   12.918  0.294   1.00 77.55  ? 505  GLN A CD  1 
ATOM   3824  O  OE1 . GLN A  1  479 ? 9.779   12.632  -0.126  1.00 79.11  ? 505  GLN A OE1 1 
ATOM   3825  N  NE2 . GLN A  1  479 ? 8.261   12.642  1.535   1.00 75.49  ? 505  GLN A NE2 1 
ATOM   3826  N  N   . CYS A  1  480 ? 5.266   13.447  -4.842  1.00 76.03  ? 506  CYS A N   1 
ATOM   3827  C  CA  . CYS A  1  480 ? 4.892   12.785  -6.092  1.00 77.68  ? 506  CYS A CA  1 
ATOM   3828  C  C   . CYS A  1  480 ? 5.345   13.481  -7.381  1.00 79.12  ? 506  CYS A C   1 
ATOM   3829  O  O   . CYS A  1  480 ? 4.773   13.235  -8.463  1.00 78.80  ? 506  CYS A O   1 
ATOM   3830  C  CB  . CYS A  1  480 ? 3.383   12.582  -6.150  1.00 77.80  ? 506  CYS A CB  1 
ATOM   3831  S  SG  . CYS A  1  480 ? 2.786   11.479  -4.882  1.00 80.41  ? 506  CYS A SG  1 
ATOM   3832  N  N   . GLN A  1  481 ? 6.357   14.346  -7.268  1.00 79.67  ? 507  GLN A N   1 
ATOM   3833  C  CA  . GLN A  1  481 ? 6.894   15.062  -8.426  1.00 80.40  ? 507  GLN A CA  1 
ATOM   3834  C  C   . GLN A  1  481 ? 5.824   15.722  -9.324  1.00 81.29  ? 507  GLN A C   1 
ATOM   3835  O  O   . GLN A  1  481 ? 6.056   15.955  -10.519 1.00 81.16  ? 507  GLN A O   1 
ATOM   3836  C  CB  . GLN A  1  481 ? 7.737   14.103  -9.265  1.00 80.53  ? 507  GLN A CB  1 
ATOM   3837  C  CG  . GLN A  1  481 ? 8.952   13.537  -8.558  1.00 79.56  ? 507  GLN A CG  1 
ATOM   3838  C  CD  . GLN A  1  481 ? 9.616   12.431  -9.355  1.00 79.04  ? 507  GLN A CD  1 
ATOM   3839  O  OE1 . GLN A  1  481 ? 9.737   11.301  -8.895  1.00 77.97  ? 507  GLN A OE1 1 
ATOM   3840  N  NE2 . GLN A  1  481 ? 10.050  12.756  -10.559 1.00 81.12  ? 507  GLN A NE2 1 
ATOM   3841  N  N   . LEU A  1  482 ? 4.660   16.013  -8.746  1.00 81.81  ? 508  LEU A N   1 
ATOM   3842  C  CA  . LEU A  1  482 ? 3.562   16.647  -9.465  1.00 82.59  ? 508  LEU A CA  1 
ATOM   3843  C  C   . LEU A  1  482 ? 3.939   18.044  -9.938  1.00 84.44  ? 508  LEU A C   1 
ATOM   3844  O  O   . LEU A  1  482 ? 4.579   18.786  -9.197  1.00 86.03  ? 508  LEU A O   1 
ATOM   3845  C  CB  . LEU A  1  482 ? 2.329   16.741  -8.564  1.00 80.30  ? 508  LEU A CB  1 
ATOM   3846  C  CG  . LEU A  1  482 ? 1.382   15.540  -8.542  1.00 80.16  ? 508  LEU A CG  1 
ATOM   3847  C  CD1 . LEU A  1  482 ? 0.260   15.792  -7.549  1.00 79.44  ? 508  LEU A CD1 1 
ATOM   3848  C  CD2 . LEU A  1  482 ? 0.800   15.315  -9.931  1.00 80.23  ? 508  LEU A CD2 1 
ATOM   3849  N  N   . GLU A  1  483 ? 3.544   18.389  -11.167 1.00 86.27  ? 509  GLU A N   1 
ATOM   3850  C  CA  . GLU A  1  483 ? 3.815   19.704  -11.764 1.00 86.46  ? 509  GLU A CA  1 
ATOM   3851  C  C   . GLU A  1  483 ? 2.515   20.375  -12.195 1.00 86.27  ? 509  GLU A C   1 
ATOM   3852  O  O   . GLU A  1  483 ? 2.162   21.426  -11.684 1.00 87.05  ? 509  GLU A O   1 
ATOM   3853  C  CB  . GLU A  1  483 ? 4.758   19.561  -12.961 1.00 86.78  ? 509  GLU A CB  1 
ATOM   3854  C  CG  . GLU A  1  483 ? 6.224   19.333  -12.578 1.00 88.66  ? 509  GLU A CG  1 
ATOM   3855  C  CD  . GLU A  1  483 ? 7.130   19.100  -13.787 1.00 90.63  ? 509  GLU A CD  1 
ATOM   3856  O  OE1 . GLU A  1  483 ? 8.370   19.110  -13.618 1.00 91.37  ? 509  GLU A OE1 1 
ATOM   3857  O  OE2 . GLU A  1  483 ? 6.603   18.907  -14.907 1.00 90.83  ? 509  GLU A OE2 1 
ATOM   3858  N  N   . GLN A  1  484 ? 1.802   19.759  -13.128 1.00 87.29  ? 510  GLN A N   1 
ATOM   3859  C  CA  . GLN A  1  484 ? 0.529   20.305  -13.601 1.00 88.99  ? 510  GLN A CA  1 
ATOM   3860  C  C   . GLN A  1  484 ? -0.571  19.827  -12.663 1.00 88.06  ? 510  GLN A C   1 
ATOM   3861  O  O   . GLN A  1  484 ? -0.287  19.210  -11.639 1.00 88.82  ? 510  GLN A O   1 
ATOM   3862  C  CB  . GLN A  1  484 ? 0.209   19.833  -15.031 1.00 91.91  ? 510  GLN A CB  1 
ATOM   3863  C  CG  . GLN A  1  484 ? 1.278   20.123  -16.092 1.00 95.87  ? 510  GLN A CG  1 
ATOM   3864  C  CD  . GLN A  1  484 ? 1.874   21.521  -15.975 1.00 97.67  ? 510  GLN A CD  1 
ATOM   3865  O  OE1 . GLN A  1  484 ? 1.168   22.489  -15.682 1.00 97.71  ? 510  GLN A OE1 1 
ATOM   3866  N  NE2 . GLN A  1  484 ? 3.181   21.629  -16.212 1.00 98.36  ? 510  GLN A NE2 1 
ATOM   3867  N  N   . LEU A  1  485 ? -1.825  20.088  -13.022 1.00 86.71  ? 511  LEU A N   1 
ATOM   3868  C  CA  . LEU A  1  485 ? -2.945  19.691  -12.182 1.00 85.30  ? 511  LEU A CA  1 
ATOM   3869  C  C   . LEU A  1  485 ? -4.284  19.829  -12.914 1.00 84.84  ? 511  LEU A C   1 
ATOM   3870  O  O   . LEU A  1  485 ? -4.561  20.847  -13.533 1.00 84.28  ? 511  LEU A O   1 
ATOM   3871  C  CB  . LEU A  1  485 ? -2.945  20.554  -10.916 1.00 84.92  ? 511  LEU A CB  1 
ATOM   3872  C  CG  . LEU A  1  485 ? -3.609  20.046  -9.634  1.00 85.29  ? 511  LEU A CG  1 
ATOM   3873  C  CD1 . LEU A  1  485 ? -3.195  20.933  -8.479  1.00 85.49  ? 511  LEU A CD1 1 
ATOM   3874  C  CD2 . LEU A  1  485 ? -5.116  20.029  -9.779  1.00 86.48  ? 511  LEU A CD2 1 
ATOM   3875  N  N   . SER A  1  486 ? -5.102  18.787  -12.860 1.00 85.44  ? 512  SER A N   1 
ATOM   3876  C  CA  . SER A  1  486 ? -6.409  18.816  -13.493 1.00 86.52  ? 512  SER A CA  1 
ATOM   3877  C  C   . SER A  1  486 ? -7.316  19.647  -12.602 1.00 88.89  ? 512  SER A C   1 
ATOM   3878  O  O   . SER A  1  486 ? -7.443  19.386  -11.397 1.00 89.06  ? 512  SER A O   1 
ATOM   3879  C  CB  . SER A  1  486 ? -6.982  17.409  -13.616 1.00 86.29  ? 512  SER A CB  1 
ATOM   3880  O  OG  . SER A  1  486 ? -8.384  17.448  -13.831 1.00 85.54  ? 512  SER A OG  1 
ATOM   3881  N  N   . PRO A  1  487 ? -7.976  20.655  -13.181 1.00 90.08  ? 513  PRO A N   1 
ATOM   3882  C  CA  . PRO A  1  487 ? -8.869  21.516  -12.408 1.00 91.37  ? 513  PRO A CA  1 
ATOM   3883  C  C   . PRO A  1  487 ? -10.103 20.807  -11.854 1.00 93.10  ? 513  PRO A C   1 
ATOM   3884  O  O   . PRO A  1  487 ? -10.718 21.290  -10.895 1.00 94.55  ? 513  PRO A O   1 
ATOM   3885  C  CB  . PRO A  1  487 ? -9.225  22.604  -13.409 1.00 90.79  ? 513  PRO A CB  1 
ATOM   3886  C  CG  . PRO A  1  487 ? -9.273  21.839  -14.690 1.00 89.44  ? 513  PRO A CG  1 
ATOM   3887  C  CD  . PRO A  1  487 ? -8.015  21.012  -14.608 1.00 89.85  ? 513  PRO A CD  1 
ATOM   3888  N  N   . THR A  1  488 ? -10.462 19.664  -12.441 1.00 93.79  ? 514  THR A N   1 
ATOM   3889  C  CA  . THR A  1  488 ? -11.644 18.918  -11.995 1.00 94.23  ? 514  THR A CA  1 
ATOM   3890  C  C   . THR A  1  488 ? -11.354 17.826  -10.955 1.00 94.94  ? 514  THR A C   1 
ATOM   3891  O  O   . THR A  1  488 ? -12.276 17.199  -10.431 1.00 95.58  ? 514  THR A O   1 
ATOM   3892  C  CB  . THR A  1  488 ? -12.358 18.261  -13.184 1.00 93.93  ? 514  THR A CB  1 
ATOM   3893  O  OG1 . THR A  1  488 ? -12.131 19.039  -14.367 1.00 94.27  ? 514  THR A OG1 1 
ATOM   3894  C  CG2 . THR A  1  488 ? -13.859 18.169  -12.914 1.00 93.20  ? 514  THR A CG2 1 
ATOM   3895  N  N   . ALA A  1  489 ? -10.074 17.607  -10.663 1.00 95.46  ? 515  ALA A N   1 
ATOM   3896  C  CA  . ALA A  1  489 ? -9.630  16.597  -9.701  1.00 95.36  ? 515  ALA A CA  1 
ATOM   3897  C  C   . ALA A  1  489 ? -10.473 16.481  -8.423  1.00 95.67  ? 515  ALA A C   1 
ATOM   3898  O  O   . ALA A  1  489 ? -11.411 15.678  -8.345  1.00 95.99  ? 515  ALA A O   1 
ATOM   3899  C  CB  . ALA A  1  489 ? -8.174  16.859  -9.330  1.00 94.39  ? 515  ALA A CB  1 
ATOM   3900  N  N   . PHE A  1  490 ? -10.117 17.284  -7.426  1.00 95.55  ? 516  PHE A N   1 
ATOM   3901  C  CA  . PHE A  1  490 ? -10.772 17.289  -6.126  1.00 96.40  ? 516  PHE A CA  1 
ATOM   3902  C  C   . PHE A  1  490 ? -12.259 17.659  -6.097  1.00 97.56  ? 516  PHE A C   1 
ATOM   3903  O  O   . PHE A  1  490 ? -12.914 17.489  -5.067  1.00 97.30  ? 516  PHE A O   1 
ATOM   3904  C  CB  . PHE A  1  490 ? -10.005 18.237  -5.202  1.00 95.31  ? 516  PHE A CB  1 
ATOM   3905  C  CG  . PHE A  1  490 ? -8.508  18.156  -5.352  1.00 94.01  ? 516  PHE A CG  1 
ATOM   3906  C  CD1 . PHE A  1  490 ? -7.747  19.320  -5.440  1.00 93.42  ? 516  PHE A CD1 1 
ATOM   3907  C  CD2 . PHE A  1  490 ? -7.855  16.925  -5.378  1.00 93.96  ? 516  PHE A CD2 1 
ATOM   3908  C  CE1 . PHE A  1  490 ? -6.355  19.267  -5.547  1.00 93.85  ? 516  PHE A CE1 1 
ATOM   3909  C  CE2 . PHE A  1  490 ? -6.458  16.854  -5.485  1.00 94.51  ? 516  PHE A CE2 1 
ATOM   3910  C  CZ  . PHE A  1  490 ? -5.704  18.031  -5.571  1.00 94.53  ? 516  PHE A CZ  1 
ATOM   3911  N  N   . ASN A  1  491 ? -12.793 18.140  -7.218  1.00 99.26  ? 517  ASN A N   1 
ATOM   3912  C  CA  . ASN A  1  491 ? -14.196 18.581  -7.309  1.00 101.74 ? 517  ASN A CA  1 
ATOM   3913  C  C   . ASN A  1  491 ? -15.347 17.746  -6.730  1.00 101.50 ? 517  ASN A C   1 
ATOM   3914  O  O   . ASN A  1  491 ? -16.486 18.225  -6.667  1.00 101.66 ? 517  ASN A O   1 
ATOM   3915  C  CB  . ASN A  1  491 ? -14.531 18.927  -8.760  1.00 104.17 ? 517  ASN A CB  1 
ATOM   3916  C  CG  . ASN A  1  491 ? -13.909 20.245  -9.200  1.00 107.81 ? 517  ASN A CG  1 
ATOM   3917  O  OD1 . ASN A  1  491 ? -13.901 20.572  -10.391 1.00 109.12 ? 517  ASN A OD1 1 
ATOM   3918  N  ND2 . ASN A  1  491 ? -13.387 21.015  -8.235  1.00 108.97 ? 517  ASN A ND2 1 
ATOM   3919  N  N   . SER A  1  492 ? -15.076 16.520  -6.306  1.00 100.20 ? 518  SER A N   1 
ATOM   3920  C  CA  . SER A  1  492 ? -16.136 15.696  -5.741  1.00 98.44  ? 518  SER A CA  1 
ATOM   3921  C  C   . SER A  1  492 ? -15.865 15.380  -4.272  1.00 97.38  ? 518  SER A C   1 
ATOM   3922  O  O   . SER A  1  492 ? -16.704 14.787  -3.587  1.00 96.71  ? 518  SER A O   1 
ATOM   3923  C  CB  . SER A  1  492 ? -16.285 14.405  -6.553  1.00 98.39  ? 518  SER A CB  1 
ATOM   3924  O  OG  . SER A  1  492 ? -15.021 13.872  -6.914  1.00 97.98  ? 518  SER A OG  1 
ATOM   3925  N  N   . LEU A  1  493 ? -14.692 15.805  -3.800  1.00 96.19  ? 519  LEU A N   1 
ATOM   3926  C  CA  . LEU A  1  493 ? -14.258 15.588  -2.418  1.00 95.60  ? 519  LEU A CA  1 
ATOM   3927  C  C   . LEU A  1  493 ? -14.834 16.637  -1.461  1.00 94.81  ? 519  LEU A C   1 
ATOM   3928  O  O   . LEU A  1  493 ? -14.117 17.506  -0.958  1.00 94.91  ? 519  LEU A O   1 
ATOM   3929  C  CB  . LEU A  1  493 ? -12.729 15.613  -2.351  1.00 95.52  ? 519  LEU A CB  1 
ATOM   3930  C  CG  . LEU A  1  493 ? -11.996 14.792  -3.423  1.00 94.96  ? 519  LEU A CG  1 
ATOM   3931  C  CD1 . LEU A  1  493 ? -10.483 15.020  -3.315  1.00 93.42  ? 519  LEU A CD1 1 
ATOM   3932  C  CD2 . LEU A  1  493 ? -12.349 13.314  -3.268  1.00 94.69  ? 519  LEU A CD2 1 
ATOM   3933  N  N   . SER A  1  494 ? -16.136 16.543  -1.214  1.00 93.65  ? 520  SER A N   1 
ATOM   3934  C  CA  . SER A  1  494 ? -16.827 17.471  -0.335  1.00 91.74  ? 520  SER A CA  1 
ATOM   3935  C  C   . SER A  1  494 ? -16.383 17.350  1.126   1.00 91.21  ? 520  SER A C   1 
ATOM   3936  O  O   . SER A  1  494 ? -16.172 18.367  1.807   1.00 91.69  ? 520  SER A O   1 
ATOM   3937  C  CB  . SER A  1  494 ? -18.339 17.250  -0.447  1.00 90.57  ? 520  SER A CB  1 
ATOM   3938  O  OG  . SER A  1  494 ? -18.672 15.881  -0.322  1.00 88.13  ? 520  SER A OG  1 
ATOM   3939  N  N   . SER A  1  495 ? -16.220 16.113  1.597   1.00 89.30  ? 521  SER A N   1 
ATOM   3940  C  CA  . SER A  1  495 ? -15.816 15.870  2.982   1.00 86.74  ? 521  SER A CA  1 
ATOM   3941  C  C   . SER A  1  495 ? -14.317 16.020  3.250   1.00 85.17  ? 521  SER A C   1 
ATOM   3942  O  O   . SER A  1  495 ? -13.886 16.033  4.408   1.00 84.20  ? 521  SER A O   1 
ATOM   3943  C  CB  . SER A  1  495 ? -16.285 14.479  3.431   1.00 85.20  ? 521  SER A CB  1 
ATOM   3944  O  OG  . SER A  1  495 ? -17.702 14.404  3.483   1.00 83.30  ? 521  SER A OG  1 
ATOM   3945  N  N   . LEU A  1  496 ? -13.527 16.148  2.187   1.00 83.26  ? 522  LEU A N   1 
ATOM   3946  C  CA  . LEU A  1  496 ? -12.084 16.289  2.339   1.00 81.66  ? 522  LEU A CA  1 
ATOM   3947  C  C   . LEU A  1  496 ? -11.733 17.432  3.301   1.00 79.97  ? 522  LEU A C   1 
ATOM   3948  O  O   . LEU A  1  496 ? -12.199 18.554  3.123   1.00 81.02  ? 522  LEU A O   1 
ATOM   3949  C  CB  . LEU A  1  496 ? -11.437 16.538  0.974   1.00 81.85  ? 522  LEU A CB  1 
ATOM   3950  C  CG  . LEU A  1  496 ? -9.917  16.351  0.974   1.00 83.73  ? 522  LEU A CG  1 
ATOM   3951  C  CD1 . LEU A  1  496 ? -9.618  14.856  1.123   1.00 82.64  ? 522  LEU A CD1 1 
ATOM   3952  C  CD2 . LEU A  1  496 ? -9.291  16.918  -0.300  1.00 82.08  ? 522  LEU A CD2 1 
ATOM   3953  N  N   . GLN A  1  497 ? -10.911 17.132  4.307   1.00 77.81  ? 523  GLN A N   1 
ATOM   3954  C  CA  . GLN A  1  497 ? -10.487 18.103  5.316   1.00 75.73  ? 523  GLN A CA  1 
ATOM   3955  C  C   . GLN A  1  497 ? -9.006  18.470  5.174   1.00 76.70  ? 523  GLN A C   1 
ATOM   3956  O  O   . GLN A  1  497 ? -8.656  19.649  5.137   1.00 77.26  ? 523  GLN A O   1 
ATOM   3957  C  CB  . GLN A  1  497 ? -10.738 17.549  6.719   1.00 73.34  ? 523  GLN A CB  1 
ATOM   3958  C  CG  . GLN A  1  497 ? -12.145 17.041  6.930   1.00 71.69  ? 523  GLN A CG  1 
ATOM   3959  C  CD  . GLN A  1  497 ? -12.363 16.488  8.324   1.00 71.51  ? 523  GLN A CD  1 
ATOM   3960  O  OE1 . GLN A  1  497 ? -13.440 15.977  8.640   1.00 69.92  ? 523  GLN A OE1 1 
ATOM   3961  N  NE2 . GLN A  1  497 ? -11.341 16.592  9.172   1.00 71.87  ? 523  GLN A NE2 1 
ATOM   3962  N  N   . VAL A  1  498 ? -8.128  17.470  5.124   1.00 77.05  ? 524  VAL A N   1 
ATOM   3963  C  CA  . VAL A  1  498 ? -6.700  17.747  4.962   1.00 76.51  ? 524  VAL A CA  1 
ATOM   3964  C  C   . VAL A  1  498 ? -6.326  17.409  3.517   1.00 76.96  ? 524  VAL A C   1 
ATOM   3965  O  O   . VAL A  1  498 ? -7.046  16.682  2.834   1.00 77.21  ? 524  VAL A O   1 
ATOM   3966  C  CB  . VAL A  1  498 ? -5.829  16.901  5.920   1.00 75.38  ? 524  VAL A CB  1 
ATOM   3967  C  CG1 . VAL A  1  498 ? -4.428  17.507  6.028   1.00 73.23  ? 524  VAL A CG1 1 
ATOM   3968  C  CG2 . VAL A  1  498 ? -6.483  16.825  7.276   1.00 75.54  ? 524  VAL A CG2 1 
ATOM   3969  N  N   . LEU A  1  499 ? -5.215  17.958  3.048   1.00 75.91  ? 525  LEU A N   1 
ATOM   3970  C  CA  . LEU A  1  499 ? -4.766  17.702  1.692   1.00 75.69  ? 525  LEU A CA  1 
ATOM   3971  C  C   . LEU A  1  499 ? -3.303  18.122  1.563   1.00 75.49  ? 525  LEU A C   1 
ATOM   3972  O  O   . LEU A  1  499 ? -2.989  19.288  1.334   1.00 75.36  ? 525  LEU A O   1 
ATOM   3973  C  CB  . LEU A  1  499 ? -5.657  18.454  0.697   1.00 76.08  ? 525  LEU A CB  1 
ATOM   3974  C  CG  . LEU A  1  499 ? -5.251  18.507  -0.783  1.00 77.50  ? 525  LEU A CG  1 
ATOM   3975  C  CD1 . LEU A  1  499 ? -4.838  17.130  -1.294  1.00 77.66  ? 525  LEU A CD1 1 
ATOM   3976  C  CD2 . LEU A  1  499 ? -6.424  19.045  -1.585  1.00 76.98  ? 525  LEU A CD2 1 
ATOM   3977  N  N   . ASN A  1  500 ? -2.411  17.151  1.724   1.00 75.25  ? 526  ASN A N   1 
ATOM   3978  C  CA  . ASN A  1  500 ? -0.977  17.384  1.649   1.00 74.66  ? 526  ASN A CA  1 
ATOM   3979  C  C   . ASN A  1  500 ? -0.589  17.404  0.178   1.00 75.27  ? 526  ASN A C   1 
ATOM   3980  O  O   . ASN A  1  500 ? -1.048  16.567  -0.595  1.00 75.35  ? 526  ASN A O   1 
ATOM   3981  C  CB  . ASN A  1  500 ? -0.225  16.261  2.373   1.00 72.96  ? 526  ASN A CB  1 
ATOM   3982  C  CG  . ASN A  1  500 ? 1.176   16.668  2.815   1.00 73.39  ? 526  ASN A CG  1 
ATOM   3983  O  OD1 . ASN A  1  500 ? 1.886   17.370  2.092   1.00 72.85  ? 526  ASN A OD1 1 
ATOM   3984  N  ND2 . ASN A  1  500 ? 1.569   16.196  4.001   1.00 73.99  ? 526  ASN A ND2 1 
ATOM   3985  N  N   . MET A  1  501 ? 0.227   18.386  -0.201  1.00 75.86  ? 527  MET A N   1 
ATOM   3986  C  CA  . MET A  1  501 ? 0.716   18.542  -1.570  1.00 74.87  ? 527  MET A CA  1 
ATOM   3987  C  C   . MET A  1  501 ? 2.128   19.045  -1.396  1.00 74.31  ? 527  MET A C   1 
ATOM   3988  O  O   . MET A  1  501 ? 2.691   19.686  -2.279  1.00 73.59  ? 527  MET A O   1 
ATOM   3989  C  CB  . MET A  1  501 ? -0.089  19.583  -2.343  1.00 74.55  ? 527  MET A CB  1 
ATOM   3990  C  CG  . MET A  1  501 ? -1.558  19.254  -2.553  1.00 76.80  ? 527  MET A CG  1 
ATOM   3991  S  SD  . MET A  1  501 ? -1.920  18.084  -3.895  1.00 79.43  ? 527  MET A SD  1 
ATOM   3992  C  CE  . MET A  1  501 ? -1.180  18.877  -5.316  1.00 78.27  ? 527  MET A CE  1 
ATOM   3993  N  N   . SER A  1  502 ? 2.688   18.748  -0.232  1.00 74.34  ? 528  SER A N   1 
ATOM   3994  C  CA  . SER A  1  502 ? 4.036   19.163  0.103   1.00 76.33  ? 528  SER A CA  1 
ATOM   3995  C  C   . SER A  1  502 ? 5.110   18.627  -0.835  1.00 77.41  ? 528  SER A C   1 
ATOM   3996  O  O   . SER A  1  502 ? 4.836   17.884  -1.767  1.00 76.36  ? 528  SER A O   1 
ATOM   3997  C  CB  . SER A  1  502 ? 4.357   18.739  1.532   1.00 75.85  ? 528  SER A CB  1 
ATOM   3998  O  OG  . SER A  1  502 ? 5.743   18.865  1.784   1.00 77.83  ? 528  SER A OG  1 
ATOM   3999  N  N   . HIS A  1  503 ? 6.340   19.033  -0.564  1.00 80.12  ? 529  HIS A N   1 
ATOM   4000  C  CA  . HIS A  1  503 ? 7.516   18.642  -1.318  1.00 84.40  ? 529  HIS A CA  1 
ATOM   4001  C  C   . HIS A  1  503 ? 7.318   18.100  -2.749  1.00 86.36  ? 529  HIS A C   1 
ATOM   4002  O  O   . HIS A  1  503 ? 7.877   17.070  -3.115  1.00 88.04  ? 529  HIS A O   1 
ATOM   4003  C  CB  . HIS A  1  503 ? 8.321   17.660  -0.469  1.00 85.50  ? 529  HIS A CB  1 
ATOM   4004  C  CG  . HIS A  1  503 ? 9.769   17.595  -0.833  1.00 88.14  ? 529  HIS A CG  1 
ATOM   4005  N  ND1 . HIS A  1  503 ? 10.724  17.093  0.023   1.00 89.61  ? 529  HIS A ND1 1 
ATOM   4006  C  CD2 . HIS A  1  503 ? 10.423  17.938  -1.968  1.00 89.13  ? 529  HIS A CD2 1 
ATOM   4007  C  CE1 . HIS A  1  503 ? 11.905  17.126  -0.570  1.00 91.03  ? 529  HIS A CE1 1 
ATOM   4008  N  NE2 . HIS A  1  503 ? 11.748  17.634  -1.779  1.00 91.30  ? 529  HIS A NE2 1 
ATOM   4009  N  N   . ASN A  1  504 ? 6.529   18.807  -3.556  1.00 88.15  ? 530  ASN A N   1 
ATOM   4010  C  CA  . ASN A  1  504 ? 6.295   18.430  -4.951  1.00 89.05  ? 530  ASN A CA  1 
ATOM   4011  C  C   . ASN A  1  504 ? 7.135   19.318  -5.872  1.00 90.56  ? 530  ASN A C   1 
ATOM   4012  O  O   . ASN A  1  504 ? 8.180   19.848  -5.469  1.00 90.20  ? 530  ASN A O   1 
ATOM   4013  C  CB  . ASN A  1  504 ? 4.820   18.592  -5.322  1.00 89.04  ? 530  ASN A CB  1 
ATOM   4014  C  CG  . ASN A  1  504 ? 4.055   17.292  -5.248  1.00 89.41  ? 530  ASN A CG  1 
ATOM   4015  O  OD1 . ASN A  1  504 ? 4.467   16.291  -5.818  1.00 89.68  ? 530  ASN A OD1 1 
ATOM   4016  N  ND2 . ASN A  1  504 ? 2.926   17.305  -4.553  1.00 90.84  ? 530  ASN A ND2 1 
ATOM   4017  N  N   . ASN A  1  505 ? 6.685   19.465  -7.114  1.00 92.19  ? 531  ASN A N   1 
ATOM   4018  C  CA  . ASN A  1  505 ? 7.388   20.296  -8.075  1.00 94.54  ? 531  ASN A CA  1 
ATOM   4019  C  C   . ASN A  1  505 ? 6.481   21.292  -8.784  1.00 96.59  ? 531  ASN A C   1 
ATOM   4020  O  O   . ASN A  1  505 ? 6.522   21.422  -10.013 1.00 96.66  ? 531  ASN A O   1 
ATOM   4021  C  CB  . ASN A  1  505 ? 8.127   19.436  -9.098  1.00 93.43  ? 531  ASN A CB  1 
ATOM   4022  C  CG  . ASN A  1  505 ? 9.397   18.833  -8.531  1.00 93.31  ? 531  ASN A CG  1 
ATOM   4023  O  OD1 . ASN A  1  505 ? 10.180  19.519  -7.866  1.00 92.57  ? 531  ASN A OD1 1 
ATOM   4024  N  ND2 . ASN A  1  505 ? 9.616   17.550  -8.799  1.00 92.51  ? 531  ASN A ND2 1 
ATOM   4025  N  N   . PHE A  1  506 ? 5.654   21.980  -8.000  1.00 98.72  ? 532  PHE A N   1 
ATOM   4026  C  CA  . PHE A  1  506 ? 4.766   22.997  -8.531  1.00 101.27 ? 532  PHE A CA  1 
ATOM   4027  C  C   . PHE A  1  506 ? 5.550   24.300  -8.579  1.00 103.83 ? 532  PHE A C   1 
ATOM   4028  O  O   . PHE A  1  506 ? 6.402   24.543  -7.721  1.00 103.46 ? 532  PHE A O   1 
ATOM   4029  C  CB  . PHE A  1  506 ? 3.561   23.193  -7.622  1.00 100.57 ? 532  PHE A CB  1 
ATOM   4030  C  CG  . PHE A  1  506 ? 2.493   22.171  -7.801  1.00 101.34 ? 532  PHE A CG  1 
ATOM   4031  C  CD1 . PHE A  1  506 ? 2.656   20.883  -7.313  1.00 101.41 ? 532  PHE A CD1 1 
ATOM   4032  C  CD2 . PHE A  1  506 ? 1.303   22.504  -8.443  1.00 102.03 ? 532  PHE A CD2 1 
ATOM   4033  C  CE1 . PHE A  1  506 ? 1.639   19.932  -7.460  1.00 101.89 ? 532  PHE A CE1 1 
ATOM   4034  C  CE2 . PHE A  1  506 ? 0.281   21.565  -8.597  1.00 102.08 ? 532  PHE A CE2 1 
ATOM   4035  C  CZ  . PHE A  1  506 ? 0.449   20.273  -8.102  1.00 101.55 ? 532  PHE A CZ  1 
ATOM   4036  N  N   . PHE A  1  507 ? 5.271   25.124  -9.590  1.00 106.71 ? 533  PHE A N   1 
ATOM   4037  C  CA  . PHE A  1  507 ? 5.930   26.423  -9.743  1.00 108.11 ? 533  PHE A CA  1 
ATOM   4038  C  C   . PHE A  1  507 ? 4.906   27.550  -9.632  1.00 108.65 ? 533  PHE A C   1 
ATOM   4039  O  O   . PHE A  1  507 ? 5.250   28.684  -9.303  1.00 108.29 ? 533  PHE A O   1 
ATOM   4040  C  CB  . PHE A  1  507 ? 6.650   26.528  -11.098 1.00 108.06 ? 533  PHE A CB  1 
ATOM   4041  C  CG  . PHE A  1  507 ? 8.119   26.185  -11.044 1.00 109.03 ? 533  PHE A CG  1 
ATOM   4042  C  CD1 . PHE A  1  507 ? 8.546   24.861  -11.061 1.00 109.78 ? 533  PHE A CD1 1 
ATOM   4043  C  CD2 . PHE A  1  507 ? 9.080   27.197  -10.977 1.00 109.44 ? 533  PHE A CD2 1 
ATOM   4044  C  CE1 . PHE A  1  507 ? 9.913   24.542  -11.012 1.00 110.41 ? 533  PHE A CE1 1 
ATOM   4045  C  CE2 . PHE A  1  507 ? 10.448  26.897  -10.926 1.00 109.68 ? 533  PHE A CE2 1 
ATOM   4046  C  CZ  . PHE A  1  507 ? 10.870  25.568  -10.944 1.00 110.14 ? 533  PHE A CZ  1 
ATOM   4047  N  N   . SER A  1  508 ? 3.640   27.223  -9.880  1.00 109.78 ? 534  SER A N   1 
ATOM   4048  C  CA  . SER A  1  508 ? 2.573   28.215  -9.838  1.00 110.75 ? 534  SER A CA  1 
ATOM   4049  C  C   . SER A  1  508 ? 1.329   27.844  -9.018  1.00 111.10 ? 534  SER A C   1 
ATOM   4050  O  O   . SER A  1  508 ? 0.422   27.180  -9.524  1.00 111.43 ? 534  SER A O   1 
ATOM   4051  C  CB  . SER A  1  508 ? 2.140   28.546  -11.272 1.00 111.21 ? 534  SER A CB  1 
ATOM   4052  O  OG  . SER A  1  508 ? 1.696   27.382  -11.951 1.00 111.34 ? 534  SER A OG  1 
ATOM   4053  N  N   . LEU A  1  509 ? 1.272   28.296  -7.768  1.00 111.25 ? 535  LEU A N   1 
ATOM   4054  C  CA  . LEU A  1  509 ? 0.122   28.024  -6.910  1.00 111.46 ? 535  LEU A CA  1 
ATOM   4055  C  C   . LEU A  1  509 ? -1.159  28.541  -7.558  1.00 112.17 ? 535  LEU A C   1 
ATOM   4056  O  O   . LEU A  1  509 ? -1.197  29.656  -8.068  1.00 112.49 ? 535  LEU A O   1 
ATOM   4057  C  CB  . LEU A  1  509 ? 0.316   28.687  -5.541  1.00 110.67 ? 535  LEU A CB  1 
ATOM   4058  C  CG  . LEU A  1  509 ? -0.875  28.815  -4.578  1.00 110.31 ? 535  LEU A CG  1 
ATOM   4059  C  CD1 . LEU A  1  509 ? -1.550  27.477  -4.356  1.00 110.21 ? 535  LEU A CD1 1 
ATOM   4060  C  CD2 . LEU A  1  509 ? -0.382  29.377  -3.258  1.00 110.07 ? 535  LEU A CD2 1 
ATOM   4061  N  N   . ASP A  1  510 ? -2.201  27.716  -7.547  1.00 113.39 ? 536  ASP A N   1 
ATOM   4062  C  CA  . ASP A  1  510 ? -3.486  28.094  -8.128  1.00 114.75 ? 536  ASP A CA  1 
ATOM   4063  C  C   . ASP A  1  510 ? -4.534  28.120  -7.026  1.00 114.67 ? 536  ASP A C   1 
ATOM   4064  O  O   . ASP A  1  510 ? -4.199  28.010  -5.848  1.00 114.99 ? 536  ASP A O   1 
ATOM   4065  C  CB  . ASP A  1  510 ? -3.906  27.097  -9.205  1.00 116.04 ? 536  ASP A CB  1 
ATOM   4066  C  CG  . ASP A  1  510 ? -4.971  27.657  -10.127 1.00 117.86 ? 536  ASP A CG  1 
ATOM   4067  O  OD1 . ASP A  1  510 ? -4.633  28.558  -10.927 1.00 118.14 ? 536  ASP A OD1 1 
ATOM   4068  O  OD2 . ASP A  1  510 ? -6.140  27.206  -10.047 1.00 118.57 ? 536  ASP A OD2 1 
ATOM   4069  N  N   . THR A  1  511 ? -5.799  28.257  -7.404  1.00 114.91 ? 537  THR A N   1 
ATOM   4070  C  CA  . THR A  1  511 ? -6.876  28.307  -6.424  1.00 116.26 ? 537  THR A CA  1 
ATOM   4071  C  C   . THR A  1  511 ? -8.222  27.842  -6.956  1.00 116.10 ? 537  THR A C   1 
ATOM   4072  O  O   . THR A  1  511 ? -9.188  27.737  -6.197  1.00 115.78 ? 537  THR A O   1 
ATOM   4073  C  CB  . THR A  1  511 ? -7.075  29.743  -5.874  1.00 117.37 ? 537  THR A CB  1 
ATOM   4074  O  OG1 . THR A  1  511 ? -7.159  30.670  -6.965  1.00 117.94 ? 537  THR A OG1 1 
ATOM   4075  C  CG2 . THR A  1  511 ? -5.927  30.135  -4.958  1.00 118.93 ? 537  THR A CG2 1 
ATOM   4076  N  N   . PHE A  1  512 ? -8.295  27.563  -8.254  1.00 116.07 ? 538  PHE A N   1 
ATOM   4077  C  CA  . PHE A  1  512 ? -9.557  27.138  -8.849  1.00 115.85 ? 538  PHE A CA  1 
ATOM   4078  C  C   . PHE A  1  512 ? -10.040 25.737  -8.459  1.00 115.18 ? 538  PHE A C   1 
ATOM   4079  O  O   . PHE A  1  512 ? -11.197 25.562  -8.071  1.00 115.19 ? 538  PHE A O   1 
ATOM   4080  C  CB  . PHE A  1  512 ? -9.495  27.242  -10.378 1.00 115.68 ? 538  PHE A CB  1 
ATOM   4081  C  CG  . PHE A  1  512 ? -10.772 26.821  -11.062 1.00 116.82 ? 538  PHE A CG  1 
ATOM   4082  C  CD1 . PHE A  1  512 ? -12.000 27.391  -10.705 1.00 116.93 ? 538  PHE A CD1 1 
ATOM   4083  C  CD2 . PHE A  1  512 ? -10.752 25.842  -12.051 1.00 116.80 ? 538  PHE A CD2 1 
ATOM   4084  C  CE1 . PHE A  1  512 ? -13.190 26.982  -11.322 1.00 116.59 ? 538  PHE A CE1 1 
ATOM   4085  C  CE2 . PHE A  1  512 ? -11.934 25.424  -12.674 1.00 116.82 ? 538  PHE A CE2 1 
ATOM   4086  C  CZ  . PHE A  1  512 ? -13.156 25.996  -12.311 1.00 116.72 ? 538  PHE A CZ  1 
ATOM   4087  N  N   . PRO A  1  513 ? -9.162  24.722  -8.548  1.00 114.18 ? 539  PRO A N   1 
ATOM   4088  C  CA  . PRO A  1  513 ? -9.575  23.361  -8.193  1.00 113.02 ? 539  PRO A CA  1 
ATOM   4089  C  C   . PRO A  1  513 ? -10.193 23.203  -6.797  1.00 112.58 ? 539  PRO A C   1 
ATOM   4090  O  O   . PRO A  1  513 ? -11.123 22.416  -6.612  1.00 112.44 ? 539  PRO A O   1 
ATOM   4091  C  CB  . PRO A  1  513 ? -8.286  22.562  -8.366  1.00 112.76 ? 539  PRO A CB  1 
ATOM   4092  C  CG  . PRO A  1  513 ? -7.210  23.574  -8.098  1.00 112.35 ? 539  PRO A CG  1 
ATOM   4093  C  CD  . PRO A  1  513 ? -7.716  24.771  -8.837  1.00 113.30 ? 539  PRO A CD  1 
ATOM   4094  N  N   . TYR A  1  514 ? -9.687  23.966  -5.832  1.00 112.08 ? 540  TYR A N   1 
ATOM   4095  C  CA  . TYR A  1  514 ? -10.160 23.915  -4.451  1.00 111.68 ? 540  TYR A CA  1 
ATOM   4096  C  C   . TYR A  1  514 ? -11.489 24.626  -4.181  1.00 111.29 ? 540  TYR A C   1 
ATOM   4097  O  O   . TYR A  1  514 ? -11.960 24.665  -3.044  1.00 111.21 ? 540  TYR A O   1 
ATOM   4098  C  CB  . TYR A  1  514 ? -9.076  24.487  -3.539  1.00 111.78 ? 540  TYR A CB  1 
ATOM   4099  C  CG  . TYR A  1  514 ? -7.696  23.966  -3.876  1.00 111.82 ? 540  TYR A CG  1 
ATOM   4100  C  CD1 . TYR A  1  514 ? -6.860  24.653  -4.757  1.00 111.55 ? 540  TYR A CD1 1 
ATOM   4101  C  CD2 . TYR A  1  514 ? -7.237  22.764  -3.333  1.00 112.44 ? 540  TYR A CD2 1 
ATOM   4102  C  CE1 . TYR A  1  514 ? -5.598  24.156  -5.088  1.00 112.03 ? 540  TYR A CE1 1 
ATOM   4103  C  CE2 . TYR A  1  514 ? -5.982  22.254  -3.656  1.00 112.17 ? 540  TYR A CE2 1 
ATOM   4104  C  CZ  . TYR A  1  514 ? -5.166  22.950  -4.532  1.00 112.16 ? 540  TYR A CZ  1 
ATOM   4105  O  OH  . TYR A  1  514 ? -3.925  22.430  -4.844  1.00 110.35 ? 540  TYR A OH  1 
ATOM   4106  N  N   . LYS A  1  515 ? -12.088 25.173  -5.231  1.00 111.11 ? 541  LYS A N   1 
ATOM   4107  C  CA  . LYS A  1  515 ? -13.352 25.895  -5.130  1.00 110.45 ? 541  LYS A CA  1 
ATOM   4108  C  C   . LYS A  1  515 ? -14.453 25.149  -4.383  1.00 109.51 ? 541  LYS A C   1 
ATOM   4109  O  O   . LYS A  1  515 ? -15.164 25.740  -3.576  1.00 109.39 ? 541  LYS A O   1 
ATOM   4110  C  CB  . LYS A  1  515 ? -13.868 26.241  -6.527  1.00 111.80 ? 541  LYS A CB  1 
ATOM   4111  C  CG  . LYS A  1  515 ? -14.197 25.009  -7.377  1.00 114.27 ? 541  LYS A CG  1 
ATOM   4112  C  CD  . LYS A  1  515 ? -14.853 25.374  -8.715  1.00 115.42 ? 541  LYS A CD  1 
ATOM   4113  C  CE  . LYS A  1  515 ? -15.140 24.131  -9.562  1.00 114.71 ? 541  LYS A CE  1 
ATOM   4114  N  NZ  . LYS A  1  515 ? -15.744 24.464  -10.882 1.00 113.55 ? 541  LYS A NZ  1 
ATOM   4115  N  N   . CYS A  1  516 ? -14.590 23.854  -4.647  1.00 108.30 ? 542  CYS A N   1 
ATOM   4116  C  CA  . CYS A  1  516 ? -15.647 23.067  -4.021  1.00 107.17 ? 542  CYS A CA  1 
ATOM   4117  C  C   . CYS A  1  516 ? -15.276 22.225  -2.795  1.00 106.43 ? 542  CYS A C   1 
ATOM   4118  O  O   . CYS A  1  516 ? -16.051 21.359  -2.384  1.00 106.37 ? 542  CYS A O   1 
ATOM   4119  C  CB  . CYS A  1  516 ? -16.294 22.164  -5.076  1.00 106.96 ? 542  CYS A CB  1 
ATOM   4120  S  SG  . CYS A  1  516 ? -16.952 23.042  -6.530  1.00 107.72 ? 542  CYS A SG  1 
ATOM   4121  N  N   . LEU A  1  517 ? -14.113 22.471  -2.199  1.00 105.32 ? 543  LEU A N   1 
ATOM   4122  C  CA  . LEU A  1  517 ? -13.707 21.695  -1.026  1.00 104.32 ? 543  LEU A CA  1 
ATOM   4123  C  C   . LEU A  1  517 ? -14.348 22.211  0.267   1.00 103.60 ? 543  LEU A C   1 
ATOM   4124  O  O   . LEU A  1  517 ? -13.671 22.725  1.161   1.00 103.79 ? 543  LEU A O   1 
ATOM   4125  C  CB  . LEU A  1  517 ? -12.177 21.687  -0.904  1.00 104.70 ? 543  LEU A CB  1 
ATOM   4126  C  CG  . LEU A  1  517 ? -11.420 20.921  -2.003  1.00 104.13 ? 543  LEU A CG  1 
ATOM   4127  C  CD1 . LEU A  1  517 ? -9.926  21.072  -1.784  1.00 103.79 ? 543  LEU A CD1 1 
ATOM   4128  C  CD2 . LEU A  1  517 ? -11.809 19.447  -1.991  1.00 103.36 ? 543  LEU A CD2 1 
ATOM   4129  N  N   . ASN A  1  518 ? -15.666 22.052  0.347   1.00 102.23 ? 544  ASN A N   1 
ATOM   4130  C  CA  . ASN A  1  518 ? -16.471 22.485  1.487   1.00 100.77 ? 544  ASN A CA  1 
ATOM   4131  C  C   . ASN A  1  518 ? -15.782 22.373  2.830   1.00 99.12  ? 544  ASN A C   1 
ATOM   4132  O  O   . ASN A  1  518 ? -15.530 23.378  3.496   1.00 99.03  ? 544  ASN A O   1 
ATOM   4133  C  CB  . ASN A  1  518 ? -17.763 21.670  1.568   1.00 102.19 ? 544  ASN A CB  1 
ATOM   4134  C  CG  . ASN A  1  518 ? -18.660 21.866  0.366   1.00 103.85 ? 544  ASN A CG  1 
ATOM   4135  O  OD1 . ASN A  1  518 ? -18.230 21.709  -0.779  1.00 104.13 ? 544  ASN A OD1 1 
ATOM   4136  N  ND2 . ASN A  1  518 ? -19.924 22.202  0.621   1.00 104.73 ? 544  ASN A ND2 1 
ATOM   4137  N  N   . SER A  1  519 ? -15.493 21.136  3.225   1.00 96.70  ? 545  SER A N   1 
ATOM   4138  C  CA  . SER A  1  519 ? -14.879 20.863  4.515   1.00 94.15  ? 545  SER A CA  1 
ATOM   4139  C  C   . SER A  1  519 ? -13.382 21.112  4.605   1.00 92.93  ? 545  SER A C   1 
ATOM   4140  O  O   . SER A  1  519 ? -12.825 21.085  5.703   1.00 93.23  ? 545  SER A O   1 
ATOM   4141  C  CB  . SER A  1  519 ? -15.171 19.418  4.936   1.00 93.30  ? 545  SER A CB  1 
ATOM   4142  O  OG  . SER A  1  519 ? -16.562 19.173  5.029   1.00 91.54  ? 545  SER A OG  1 
ATOM   4143  N  N   . LEU A  1  520 ? -12.725 21.370  3.478   1.00 91.16  ? 546  LEU A N   1 
ATOM   4144  C  CA  . LEU A  1  520 ? -11.281 21.587  3.510   1.00 90.35  ? 546  LEU A CA  1 
ATOM   4145  C  C   . LEU A  1  520 ? -10.809 22.521  4.634   1.00 89.59  ? 546  LEU A C   1 
ATOM   4146  O  O   . LEU A  1  520 ? -11.143 23.704  4.645   1.00 90.95  ? 546  LEU A O   1 
ATOM   4147  C  CB  . LEU A  1  520 ? -10.776 22.127  2.174   1.00 89.37  ? 546  LEU A CB  1 
ATOM   4148  C  CG  . LEU A  1  520 ? -9.250  22.227  2.181   1.00 89.96  ? 546  LEU A CG  1 
ATOM   4149  C  CD1 . LEU A  1  520 ? -8.659  20.826  2.221   1.00 89.71  ? 546  LEU A CD1 1 
ATOM   4150  C  CD2 . LEU A  1  520 ? -8.766  22.982  0.962   1.00 89.44  ? 546  LEU A CD2 1 
ATOM   4151  N  N   . GLN A  1  521 ? -10.021 21.985  5.565   1.00 88.15  ? 547  GLN A N   1 
ATOM   4152  C  CA  . GLN A  1  521 ? -9.502  22.763  6.680   1.00 86.84  ? 547  GLN A CA  1 
ATOM   4153  C  C   . GLN A  1  521 ? -8.014  23.028  6.537   1.00 86.75  ? 547  GLN A C   1 
ATOM   4154  O  O   . GLN A  1  521 ? -7.553  24.140  6.797   1.00 86.50  ? 547  GLN A O   1 
ATOM   4155  C  CB  . GLN A  1  521 ? -9.748  22.035  7.999   1.00 87.30  ? 547  GLN A CB  1 
ATOM   4156  C  CG  . GLN A  1  521 ? -11.191 21.649  8.244   1.00 87.76  ? 547  GLN A CG  1 
ATOM   4157  C  CD  . GLN A  1  521 ? -11.399 21.041  9.617   1.00 88.26  ? 547  GLN A CD  1 
ATOM   4158  O  OE1 . GLN A  1  521 ? -12.487 20.550  9.930   1.00 87.72  ? 547  GLN A OE1 1 
ATOM   4159  N  NE2 . GLN A  1  521 ? -10.352 21.077  10.451  1.00 88.13  ? 547  GLN A NE2 1 
ATOM   4160  N  N   . VAL A  1  522 ? -7.261  22.004  6.138   1.00 86.68  ? 548  VAL A N   1 
ATOM   4161  C  CA  . VAL A  1  522 ? -5.815  22.149  5.974   1.00 86.13  ? 548  VAL A CA  1 
ATOM   4162  C  C   . VAL A  1  522 ? -5.397  21.986  4.517   1.00 85.59  ? 548  VAL A C   1 
ATOM   4163  O  O   . VAL A  1  522 ? -6.066  21.320  3.733   1.00 84.18  ? 548  VAL A O   1 
ATOM   4164  C  CB  . VAL A  1  522 ? -5.027  21.116  6.831   1.00 85.32  ? 548  VAL A CB  1 
ATOM   4165  C  CG1 . VAL A  1  522 ? -3.558  21.534  6.934   1.00 84.17  ? 548  VAL A CG1 1 
ATOM   4166  C  CG2 . VAL A  1  522 ? -5.649  20.997  8.209   1.00 85.22  ? 548  VAL A CG2 1 
ATOM   4167  N  N   . LEU A  1  523 ? -4.285  22.611  4.158   1.00 86.11  ? 549  LEU A N   1 
ATOM   4168  C  CA  . LEU A  1  523 ? -3.773  22.515  2.805   1.00 86.99  ? 549  LEU A CA  1 
ATOM   4169  C  C   . LEU A  1  523 ? -2.280  22.833  2.757   1.00 87.72  ? 549  LEU A C   1 
ATOM   4170  O  O   . LEU A  1  523 ? -1.884  23.966  2.486   1.00 88.66  ? 549  LEU A O   1 
ATOM   4171  C  CB  . LEU A  1  523 ? -4.521  23.465  1.873   1.00 87.38  ? 549  LEU A CB  1 
ATOM   4172  C  CG  . LEU A  1  523 ? -4.281  23.139  0.394   1.00 88.27  ? 549  LEU A CG  1 
ATOM   4173  C  CD1 . LEU A  1  523 ? -5.476  22.347  -0.090  1.00 88.93  ? 549  LEU A CD1 1 
ATOM   4174  C  CD2 . LEU A  1  523 ? -4.094  24.388  -0.452  1.00 86.73  ? 549  LEU A CD2 1 
ATOM   4175  N  N   . ASP A  1  524 ? -1.452  21.828  3.017   1.00 87.78  ? 550  ASP A N   1 
ATOM   4176  C  CA  . ASP A  1  524 ? -0.012  22.021  2.983   1.00 87.33  ? 550  ASP A CA  1 
ATOM   4177  C  C   . ASP A  1  524 ? 0.388   22.200  1.518   1.00 86.73  ? 550  ASP A C   1 
ATOM   4178  O  O   . ASP A  1  524 ? -0.207  21.581  0.635   1.00 85.88  ? 550  ASP A O   1 
ATOM   4179  C  CB  . ASP A  1  524 ? 0.685   20.803  3.605   1.00 86.89  ? 550  ASP A CB  1 
ATOM   4180  C  CG  . ASP A  1  524 ? 2.158   21.044  3.879   1.00 88.03  ? 550  ASP A CG  1 
ATOM   4181  O  OD1 . ASP A  1  524 ? 2.721   20.344  4.753   1.00 88.45  ? 550  ASP A OD1 1 
ATOM   4182  O  OD2 . ASP A  1  524 ? 2.757   21.926  3.220   1.00 88.77  ? 550  ASP A OD2 1 
ATOM   4183  N  N   . TYR A  1  525 ? 1.369   23.070  1.270   1.00 86.43  ? 551  TYR A N   1 
ATOM   4184  C  CA  . TYR A  1  525 ? 1.869   23.343  -0.079  1.00 85.72  ? 551  TYR A CA  1 
ATOM   4185  C  C   . TYR A  1  525 ? 3.346   23.700  0.025   1.00 86.23  ? 551  TYR A C   1 
ATOM   4186  O  O   . TYR A  1  525 ? 3.934   24.230  -0.916  1.00 85.66  ? 551  TYR A O   1 
ATOM   4187  C  CB  . TYR A  1  525 ? 1.112   24.520  -0.711  1.00 84.08  ? 551  TYR A CB  1 
ATOM   4188  C  CG  . TYR A  1  525 ? 0.361   24.188  -1.987  1.00 82.90  ? 551  TYR A CG  1 
ATOM   4189  C  CD1 . TYR A  1  525 ? -1.019  23.948  -1.972  1.00 82.22  ? 551  TYR A CD1 1 
ATOM   4190  C  CD2 . TYR A  1  525 ? 1.030   24.096  -3.207  1.00 82.09  ? 551  TYR A CD2 1 
ATOM   4191  C  CE1 . TYR A  1  525 ? -1.709  23.625  -3.135  1.00 80.50  ? 551  TYR A CE1 1 
ATOM   4192  C  CE2 . TYR A  1  525 ? 0.347   23.769  -4.379  1.00 81.32  ? 551  TYR A CE2 1 
ATOM   4193  C  CZ  . TYR A  1  525 ? -1.023  23.533  -4.335  1.00 80.68  ? 551  TYR A CZ  1 
ATOM   4194  O  OH  . TYR A  1  525 ? -1.703  23.185  -5.483  1.00 79.75  ? 551  TYR A OH  1 
ATOM   4195  N  N   . SER A  1  526 ? 3.931   23.398  1.181   1.00 87.79  ? 552  SER A N   1 
ATOM   4196  C  CA  . SER A  1  526 ? 5.329   23.696  1.465   1.00 90.74  ? 552  SER A CA  1 
ATOM   4197  C  C   . SER A  1  526 ? 6.353   22.983  0.594   1.00 93.54  ? 552  SER A C   1 
ATOM   4198  O  O   . SER A  1  526 ? 6.005   22.218  -0.299  1.00 93.98  ? 552  SER A O   1 
ATOM   4199  C  CB  . SER A  1  526 ? 5.627   23.392  2.929   1.00 90.66  ? 552  SER A CB  1 
ATOM   4200  O  OG  . SER A  1  526 ? 5.397   22.025  3.222   1.00 91.06  ? 552  SER A OG  1 
ATOM   4201  N  N   . LEU A  1  527 ? 7.625   23.249  0.875   1.00 96.72  ? 553  LEU A N   1 
ATOM   4202  C  CA  . LEU A  1  527 ? 8.749   22.668  0.148   1.00 100.14 ? 553  LEU A CA  1 
ATOM   4203  C  C   . LEU A  1  527 ? 8.605   22.497  -1.371  1.00 102.90 ? 553  LEU A C   1 
ATOM   4204  O  O   . LEU A  1  527 ? 9.213   21.598  -1.951  1.00 103.24 ? 553  LEU A O   1 
ATOM   4205  C  CB  . LEU A  1  527 ? 9.139   21.330  0.774   1.00 99.60  ? 553  LEU A CB  1 
ATOM   4206  C  CG  . LEU A  1  527 ? 10.335  21.334  1.723   1.00 99.27  ? 553  LEU A CG  1 
ATOM   4207  C  CD1 . LEU A  1  527 ? 10.589  19.913  2.191   1.00 100.38 ? 553  LEU A CD1 1 
ATOM   4208  C  CD2 . LEU A  1  527 ? 11.571  21.870  1.017   1.00 99.46  ? 553  LEU A CD2 1 
ATOM   4209  N  N   . ASN A  1  528 ? 7.814   23.349  -2.017  1.00 106.47 ? 554  ASN A N   1 
ATOM   4210  C  CA  . ASN A  1  528 ? 7.657   23.280  -3.472  1.00 110.65 ? 554  ASN A CA  1 
ATOM   4211  C  C   . ASN A  1  528 ? 8.620   24.264  -4.137  1.00 114.38 ? 554  ASN A C   1 
ATOM   4212  O  O   . ASN A  1  528 ? 9.670   24.606  -3.576  1.00 114.41 ? 554  ASN A O   1 
ATOM   4213  C  CB  . ASN A  1  528 ? 6.224   23.628  -3.904  1.00 109.79 ? 554  ASN A CB  1 
ATOM   4214  C  CG  . ASN A  1  528 ? 5.267   22.466  -3.764  1.00 109.10 ? 554  ASN A CG  1 
ATOM   4215  O  OD1 . ASN A  1  528 ? 4.194   22.455  -4.366  1.00 108.72 ? 554  ASN A OD1 1 
ATOM   4216  N  ND2 . ASN A  1  528 ? 5.643   21.487  -2.959  1.00 109.78 ? 554  ASN A ND2 1 
ATOM   4217  N  N   . HIS A  1  529 ? 8.250   24.716  -5.332  1.00 118.20 ? 555  HIS A N   1 
ATOM   4218  C  CA  . HIS A  1  529 ? 9.052   25.671  -6.083  1.00 121.90 ? 555  HIS A CA  1 
ATOM   4219  C  C   . HIS A  1  529 ? 8.129   26.756  -6.640  1.00 123.98 ? 555  HIS A C   1 
ATOM   4220  O  O   . HIS A  1  529 ? 8.350   27.270  -7.738  1.00 124.27 ? 555  HIS A O   1 
ATOM   4221  C  CB  . HIS A  1  529 ? 9.803   24.955  -7.216  1.00 122.92 ? 555  HIS A CB  1 
ATOM   4222  C  CG  . HIS A  1  529 ? 10.886  24.031  -6.739  1.00 124.67 ? 555  HIS A CG  1 
ATOM   4223  N  ND1 . HIS A  1  529 ? 12.001  24.474  -6.057  1.00 124.90 ? 555  HIS A ND1 1 
ATOM   4224  C  CD2 . HIS A  1  529 ? 11.021  22.686  -6.841  1.00 125.61 ? 555  HIS A CD2 1 
ATOM   4225  C  CE1 . HIS A  1  529 ? 12.773  23.444  -5.760  1.00 125.33 ? 555  HIS A CE1 1 
ATOM   4226  N  NE2 . HIS A  1  529 ? 12.202  22.346  -6.225  1.00 125.88 ? 555  HIS A NE2 1 
ATOM   4227  N  N   . ILE A  1  530 ? 7.099   27.100  -5.858  1.00 126.24 ? 556  ILE A N   1 
ATOM   4228  C  CA  . ILE A  1  530 ? 6.107   28.114  -6.235  1.00 128.59 ? 556  ILE A CA  1 
ATOM   4229  C  C   . ILE A  1  530 ? 6.669   29.532  -6.134  1.00 130.49 ? 556  ILE A C   1 
ATOM   4230  O  O   . ILE A  1  530 ? 7.604   29.792  -5.375  1.00 130.99 ? 556  ILE A O   1 
ATOM   4231  C  CB  . ILE A  1  530 ? 4.845   28.053  -5.330  1.00 127.94 ? 556  ILE A CB  1 
ATOM   4232  C  CG1 . ILE A  1  530 ? 4.284   26.632  -5.293  1.00 128.32 ? 556  ILE A CG1 1 
ATOM   4233  C  CG2 . ILE A  1  530 ? 3.766   28.996  -5.862  1.00 127.48 ? 556  ILE A CG2 1 
ATOM   4234  C  CD1 . ILE A  1  530 ? 3.085   26.475  -4.379  1.00 127.80 ? 556  ILE A CD1 1 
ATOM   4235  N  N   . MET A  1  531 ? 6.081   30.442  -6.907  1.00 132.21 ? 557  MET A N   1 
ATOM   4236  C  CA  . MET A  1  531 ? 6.486   31.840  -6.926  1.00 133.63 ? 557  MET A CA  1 
ATOM   4237  C  C   . MET A  1  531 ? 5.499   32.638  -7.764  1.00 134.83 ? 557  MET A C   1 
ATOM   4238  O  O   . MET A  1  531 ? 5.197   33.790  -7.459  1.00 134.76 ? 557  MET A O   1 
ATOM   4239  C  CB  . MET A  1  531 ? 7.891   31.979  -7.517  1.00 133.71 ? 557  MET A CB  1 
ATOM   4240  C  CG  . MET A  1  531 ? 8.045   31.398  -8.910  1.00 134.18 ? 557  MET A CG  1 
ATOM   4241  S  SD  . MET A  1  531 ? 9.718   31.587  -9.550  1.00 134.94 ? 557  MET A SD  1 
ATOM   4242  C  CE  . MET A  1  531 ? 10.492  30.062  -8.980  1.00 136.45 ? 557  MET A CE  1 
ATOM   4243  N  N   . THR A  1  532 ? 4.989   32.002  -8.813  1.00 136.74 ? 558  THR A N   1 
ATOM   4244  C  CA  . THR A  1  532 ? 4.041   32.628  -9.734  1.00 138.37 ? 558  THR A CA  1 
ATOM   4245  C  C   . THR A  1  532 ? 2.579   32.437  -9.300  1.00 139.63 ? 558  THR A C   1 
ATOM   4246  O  O   . THR A  1  532 ? 2.294   32.175  -8.130  1.00 139.99 ? 558  THR A O   1 
ATOM   4247  C  CB  . THR A  1  532 ? 4.221   32.048  -11.161 1.00 138.26 ? 558  THR A CB  1 
ATOM   4248  O  OG1 . THR A  1  532 ? 5.607   31.760  -11.387 1.00 137.91 ? 558  THR A OG1 1 
ATOM   4249  C  CG2 . THR A  1  532 ? 3.754   33.046  -12.215 1.00 138.11 ? 558  THR A CG2 1 
ATOM   4250  N  N   . SER A  1  533 ? 1.669   32.578  -10.261 1.00 140.98 ? 559  SER A N   1 
ATOM   4251  C  CA  . SER A  1  533 ? 0.227   32.435  -10.050 1.00 142.64 ? 559  SER A CA  1 
ATOM   4252  C  C   . SER A  1  533 ? -0.421  32.712  -11.404 1.00 144.00 ? 559  SER A C   1 
ATOM   4253  O  O   . SER A  1  533 ? -0.832  33.837  -11.686 1.00 144.54 ? 559  SER A O   1 
ATOM   4254  C  CB  . SER A  1  533 ? -0.269  33.448  -9.017  1.00 142.33 ? 559  SER A CB  1 
ATOM   4255  O  OG  . SER A  1  533 ? -1.679  33.399  -8.885  1.00 141.77 ? 559  SER A OG  1 
ATOM   4256  N  N   . LYS A  1  534 ? -0.510  31.677  -12.234 1.00 145.42 ? 560  LYS A N   1 
ATOM   4257  C  CA  . LYS A  1  534 ? -1.061  31.787  -13.585 1.00 146.77 ? 560  LYS A CA  1 
ATOM   4258  C  C   . LYS A  1  534 ? -2.549  32.139  -13.728 1.00 147.84 ? 560  LYS A C   1 
ATOM   4259  O  O   . LYS A  1  534 ? -3.135  31.966  -14.798 1.00 147.59 ? 560  LYS A O   1 
ATOM   4260  C  CB  . LYS A  1  534 ? -0.726  30.499  -14.347 1.00 146.26 ? 560  LYS A CB  1 
ATOM   4261  C  CG  . LYS A  1  534 ? 0.783   30.256  -14.414 1.00 146.07 ? 560  LYS A CG  1 
ATOM   4262  C  CD  . LYS A  1  534 ? 1.155   28.848  -14.856 1.00 145.99 ? 560  LYS A CD  1 
ATOM   4263  C  CE  . LYS A  1  534 ? 2.670   28.653  -14.823 1.00 145.43 ? 560  LYS A CE  1 
ATOM   4264  N  NZ  . LYS A  1  534 ? 3.098   27.277  -15.201 1.00 144.80 ? 560  LYS A NZ  1 
ATOM   4265  N  N   . LYS A  1  535 ? -3.144  32.650  -12.652 1.00 149.66 ? 561  LYS A N   1 
ATOM   4266  C  CA  . LYS A  1  535 ? -4.550  33.070  -12.626 1.00 151.18 ? 561  LYS A CA  1 
ATOM   4267  C  C   . LYS A  1  535 ? -4.880  33.736  -11.290 1.00 152.35 ? 561  LYS A C   1 
ATOM   4268  O  O   . LYS A  1  535 ? -4.975  33.075  -10.257 1.00 152.61 ? 561  LYS A O   1 
ATOM   4269  C  CB  . LYS A  1  535 ? -5.490  31.883  -12.867 1.00 150.52 ? 561  LYS A CB  1 
ATOM   4270  C  CG  . LYS A  1  535 ? -6.136  31.893  -14.247 1.00 150.01 ? 561  LYS A CG  1 
ATOM   4271  C  CD  . LYS A  1  535 ? -7.030  33.118  -14.426 1.00 149.34 ? 561  LYS A CD  1 
ATOM   4272  C  CE  . LYS A  1  535 ? -7.421  33.333  -15.887 1.00 148.94 ? 561  LYS A CE  1 
ATOM   4273  N  NZ  . LYS A  1  535 ? -8.174  32.192  -16.478 1.00 148.64 ? 561  LYS A NZ  1 
ATOM   4274  N  N   . GLN A  1  536 ? -5.050  35.055  -11.323 1.00 154.00 ? 562  GLN A N   1 
ATOM   4275  C  CA  . GLN A  1  536 ? -5.347  35.837  -10.121 1.00 155.75 ? 562  GLN A CA  1 
ATOM   4276  C  C   . GLN A  1  536 ? -6.759  35.675  -9.550  1.00 156.27 ? 562  GLN A C   1 
ATOM   4277  O  O   . GLN A  1  536 ? -7.376  36.651  -9.109  1.00 156.23 ? 562  GLN A O   1 
ATOM   4278  C  CB  . GLN A  1  536 ? -5.074  37.324  -10.385 1.00 156.49 ? 562  GLN A CB  1 
ATOM   4279  C  CG  . GLN A  1  536 ? -3.686  37.802  -9.967  1.00 157.42 ? 562  GLN A CG  1 
ATOM   4280  C  CD  . GLN A  1  536 ? -2.561  36.995  -10.593 1.00 157.88 ? 562  GLN A CD  1 
ATOM   4281  O  OE1 . GLN A  1  536 ? -2.420  36.943  -11.815 1.00 157.59 ? 562  GLN A OE1 1 
ATOM   4282  N  NE2 . GLN A  1  536 ? -1.749  36.364  -9.750  1.00 158.17 ? 562  GLN A NE2 1 
ATOM   4283  N  N   . GLU A  1  537 ? -7.264  34.444  -9.562  1.00 156.56 ? 563  GLU A N   1 
ATOM   4284  C  CA  . GLU A  1  537 ? -8.588  34.143  -9.020  1.00 156.16 ? 563  GLU A CA  1 
ATOM   4285  C  C   . GLU A  1  537 ? -8.336  33.584  -7.619  1.00 155.29 ? 563  GLU A C   1 
ATOM   4286  O  O   . GLU A  1  537 ? -9.001  32.653  -7.155  1.00 155.32 ? 563  GLU A O   1 
ATOM   4287  C  CB  . GLU A  1  537 ? -9.301  33.109  -9.903  1.00 156.52 ? 563  GLU A CB  1 
ATOM   4288  C  CG  . GLU A  1  537 ? -10.709 32.761  -9.438  1.00 156.87 ? 563  GLU A CG  1 
ATOM   4289  C  CD  . GLU A  1  537 ? -11.604 33.983  -9.311  1.00 156.97 ? 563  GLU A CD  1 
ATOM   4290  O  OE1 . GLU A  1  537 ? -12.689 33.855  -8.708  1.00 157.25 ? 563  GLU A OE1 1 
ATOM   4291  O  OE2 . GLU A  1  537 ? -11.231 35.065  -9.815  1.00 156.64 ? 563  GLU A OE2 1 
ATOM   4292  N  N   . LEU A  1  538 ? -7.360  34.200  -6.962  1.00 153.85 ? 564  LEU A N   1 
ATOM   4293  C  CA  . LEU A  1  538 ? -6.901  33.827  -5.631  1.00 152.52 ? 564  LEU A CA  1 
ATOM   4294  C  C   . LEU A  1  538 ? -7.929  33.916  -4.497  1.00 151.96 ? 564  LEU A C   1 
ATOM   4295  O  O   . LEU A  1  538 ? -7.558  33.830  -3.324  1.00 151.79 ? 564  LEU A O   1 
ATOM   4296  C  CB  . LEU A  1  538 ? -5.677  34.679  -5.286  1.00 152.19 ? 564  LEU A CB  1 
ATOM   4297  C  CG  . LEU A  1  538 ? -4.614  34.732  -6.391  1.00 151.80 ? 564  LEU A CG  1 
ATOM   4298  C  CD1 . LEU A  1  538 ? -3.638  35.863  -6.132  1.00 151.91 ? 564  LEU A CD1 1 
ATOM   4299  C  CD2 . LEU A  1  538 ? -3.893  33.403  -6.466  1.00 151.79 ? 564  LEU A CD2 1 
ATOM   4300  N  N   . GLN A  1  539 ? -9.208  34.078  -4.828  1.00 150.94 ? 565  GLN A N   1 
ATOM   4301  C  CA  . GLN A  1  539 ? -10.231 34.173  -3.785  1.00 150.11 ? 565  GLN A CA  1 
ATOM   4302  C  C   . GLN A  1  539 ? -10.915 32.837  -3.512  1.00 148.78 ? 565  GLN A C   1 
ATOM   4303  O  O   . GLN A  1  539 ? -11.469 32.625  -2.430  1.00 148.38 ? 565  GLN A O   1 
ATOM   4304  C  CB  . GLN A  1  539 ? -11.297 35.216  -4.158  1.00 150.80 ? 565  GLN A CB  1 
ATOM   4305  C  CG  . GLN A  1  539 ? -12.180 34.832  -5.346  1.00 151.56 ? 565  GLN A CG  1 
ATOM   4306  C  CD  . GLN A  1  539 ? -13.673 34.894  -5.021  1.00 151.66 ? 565  GLN A CD  1 
ATOM   4307  O  OE1 . GLN A  1  539 ? -14.182 35.920  -4.564  1.00 151.78 ? 565  GLN A OE1 1 
ATOM   4308  N  NE2 . GLN A  1  539 ? -14.380 33.793  -5.269  1.00 151.52 ? 565  GLN A NE2 1 
ATOM   4309  N  N   . HIS A  1  540 ? -10.865 31.940  -4.493  1.00 147.04 ? 566  HIS A N   1 
ATOM   4310  C  CA  . HIS A  1  540 ? -11.503 30.633  -4.383  1.00 145.35 ? 566  HIS A CA  1 
ATOM   4311  C  C   . HIS A  1  540 ? -10.904 29.611  -3.402  1.00 143.44 ? 566  HIS A C   1 
ATOM   4312  O  O   . HIS A  1  540 ? -10.538 28.503  -3.801  1.00 143.79 ? 566  HIS A O   1 
ATOM   4313  C  CB  . HIS A  1  540 ? -11.620 29.993  -5.777  1.00 146.54 ? 566  HIS A CB  1 
ATOM   4314  C  CG  . HIS A  1  540 ? -12.872 30.363  -6.515  1.00 147.50 ? 566  HIS A CG  1 
ATOM   4315  N  ND1 . HIS A  1  540 ? -14.132 30.155  -5.993  1.00 147.72 ? 566  HIS A ND1 1 
ATOM   4316  C  CD2 . HIS A  1  540 ? -13.060 30.903  -7.743  1.00 147.41 ? 566  HIS A CD2 1 
ATOM   4317  C  CE1 . HIS A  1  540 ? -15.041 30.551  -6.866  1.00 147.32 ? 566  HIS A CE1 1 
ATOM   4318  N  NE2 . HIS A  1  540 ? -14.417 31.009  -7.936  1.00 147.51 ? 566  HIS A NE2 1 
ATOM   4319  N  N   . PHE A  1  541 ? -10.813 29.986  -2.124  1.00 140.25 ? 567  PHE A N   1 
ATOM   4320  C  CA  . PHE A  1  541 ? -10.315 29.098  -1.065  1.00 136.62 ? 567  PHE A CA  1 
ATOM   4321  C  C   . PHE A  1  541 ? -11.506 28.865  -0.126  1.00 134.33 ? 567  PHE A C   1 
ATOM   4322  O  O   . PHE A  1  541 ? -12.000 29.802  0.495   1.00 134.39 ? 567  PHE A O   1 
ATOM   4323  C  CB  . PHE A  1  541 ? -9.165  29.754  -0.280  1.00 135.71 ? 567  PHE A CB  1 
ATOM   4324  C  CG  . PHE A  1  541 ? -7.775  29.363  -0.747  1.00 134.04 ? 567  PHE A CG  1 
ATOM   4325  C  CD1 . PHE A  1  541 ? -6.654  29.986  -0.201  1.00 133.12 ? 567  PHE A CD1 1 
ATOM   4326  C  CD2 . PHE A  1  541 ? -7.586  28.383  -1.722  1.00 133.13 ? 567  PHE A CD2 1 
ATOM   4327  C  CE1 . PHE A  1  541 ? -5.367  29.642  -0.614  1.00 132.64 ? 567  PHE A CE1 1 
ATOM   4328  C  CE2 . PHE A  1  541 ? -6.299  28.028  -2.146  1.00 132.33 ? 567  PHE A CE2 1 
ATOM   4329  C  CZ  . PHE A  1  541 ? -5.186  28.661  -1.591  1.00 132.49 ? 567  PHE A CZ  1 
ATOM   4330  N  N   . PRO A  1  542 ? -11.976 27.612  -0.012  1.00 131.93 ? 568  PRO A N   1 
ATOM   4331  C  CA  . PRO A  1  542 ? -13.109 27.234  0.839   1.00 129.80 ? 568  PRO A CA  1 
ATOM   4332  C  C   . PRO A  1  542 ? -13.323 28.070  2.099   1.00 127.52 ? 568  PRO A C   1 
ATOM   4333  O  O   . PRO A  1  542 ? -12.374 28.501  2.752   1.00 127.54 ? 568  PRO A O   1 
ATOM   4334  C  CB  . PRO A  1  542 ? -12.824 25.770  1.147   1.00 130.57 ? 568  PRO A CB  1 
ATOM   4335  C  CG  . PRO A  1  542 ? -12.279 25.296  -0.154  1.00 130.99 ? 568  PRO A CG  1 
ATOM   4336  C  CD  . PRO A  1  542 ? -11.313 26.408  -0.546  1.00 131.64 ? 568  PRO A CD  1 
ATOM   4337  N  N   . SER A  1  543 ? -14.592 28.276  2.434   1.00 124.63 ? 569  SER A N   1 
ATOM   4338  C  CA  . SER A  1  543 ? -14.989 29.067  3.593   1.00 121.85 ? 569  SER A CA  1 
ATOM   4339  C  C   . SER A  1  543 ? -14.548 28.508  4.940   1.00 120.29 ? 569  SER A C   1 
ATOM   4340  O  O   . SER A  1  543 ? -14.468 29.252  5.921   1.00 120.10 ? 569  SER A O   1 
ATOM   4341  C  CB  . SER A  1  543 ? -16.503 29.242  3.589   1.00 121.60 ? 569  SER A CB  1 
ATOM   4342  O  OG  . SER A  1  543 ? -16.922 29.897  2.405   1.00 120.83 ? 569  SER A OG  1 
ATOM   4343  N  N   . SER A  1  544 ? -14.261 27.209  4.992   1.00 117.96 ? 570  SER A N   1 
ATOM   4344  C  CA  . SER A  1  544 ? -13.832 26.582  6.241   1.00 115.07 ? 570  SER A CA  1 
ATOM   4345  C  C   . SER A  1  544 ? -12.312 26.507  6.369   1.00 112.77 ? 570  SER A C   1 
ATOM   4346  O  O   . SER A  1  544 ? -11.791 26.330  7.471   1.00 112.74 ? 570  SER A O   1 
ATOM   4347  C  CB  . SER A  1  544 ? -14.420 25.179  6.355   1.00 114.93 ? 570  SER A CB  1 
ATOM   4348  O  OG  . SER A  1  544 ? -14.025 24.395  5.247   1.00 115.27 ? 570  SER A OG  1 
ATOM   4349  N  N   . LEU A  1  545 ? -11.610 26.644  5.246   1.00 109.61 ? 571  LEU A N   1 
ATOM   4350  C  CA  . LEU A  1  545 ? -10.150 26.593  5.223   1.00 107.61 ? 571  LEU A CA  1 
ATOM   4351  C  C   . LEU A  1  545 ? -9.499  27.424  6.332   1.00 106.77 ? 571  LEU A C   1 
ATOM   4352  O  O   . LEU A  1  545 ? -9.466  28.650  6.255   1.00 107.68 ? 571  LEU A O   1 
ATOM   4353  C  CB  . LEU A  1  545 ? -9.647  27.074  3.861   1.00 106.99 ? 571  LEU A CB  1 
ATOM   4354  C  CG  . LEU A  1  545 ? -8.135  27.204  3.656   1.00 107.09 ? 571  LEU A CG  1 
ATOM   4355  C  CD1 . LEU A  1  545 ? -7.469  25.848  3.804   1.00 107.43 ? 571  LEU A CD1 1 
ATOM   4356  C  CD2 . LEU A  1  545 ? -7.858  27.778  2.280   1.00 106.37 ? 571  LEU A CD2 1 
ATOM   4357  N  N   . ALA A  1  546 ? -8.977  26.758  7.359   1.00 104.93 ? 572  ALA A N   1 
ATOM   4358  C  CA  . ALA A  1  546 ? -8.334  27.453  8.463   1.00 102.90 ? 572  ALA A CA  1 
ATOM   4359  C  C   . ALA A  1  546 ? -6.850  27.595  8.199   1.00 102.01 ? 572  ALA A C   1 
ATOM   4360  O  O   . ALA A  1  546 ? -6.364  28.696  7.980   1.00 102.22 ? 572  ALA A O   1 
ATOM   4361  C  CB  . ALA A  1  546 ? -8.564  26.709  9.772   1.00 102.93 ? 572  ALA A CB  1 
ATOM   4362  N  N   . PHE A  1  547 ? -6.129  26.480  8.207   1.00 101.47 ? 573  PHE A N   1 
ATOM   4363  C  CA  . PHE A  1  547 ? -4.686  26.507  7.974   1.00 101.03 ? 573  PHE A CA  1 
ATOM   4364  C  C   . PHE A  1  547 ? -4.312  26.408  6.495   1.00 100.73 ? 573  PHE A C   1 
ATOM   4365  O  O   . PHE A  1  547 ? -5.068  25.869  5.692   1.00 100.52 ? 573  PHE A O   1 
ATOM   4366  C  CB  . PHE A  1  547 ? -4.008  25.378  8.747   1.00 100.35 ? 573  PHE A CB  1 
ATOM   4367  C  CG  . PHE A  1  547 ? -4.200  25.465  10.233  1.00 100.84 ? 573  PHE A CG  1 
ATOM   4368  C  CD1 . PHE A  1  547 ? -5.442  25.186  10.806  1.00 99.92  ? 573  PHE A CD1 1 
ATOM   4369  C  CD2 . PHE A  1  547 ? -3.139  25.832  11.065  1.00 101.42 ? 573  PHE A CD2 1 
ATOM   4370  C  CE1 . PHE A  1  547 ? -5.629  25.269  12.182  1.00 99.84  ? 573  PHE A CE1 1 
ATOM   4371  C  CE2 . PHE A  1  547 ? -3.308  25.919  12.448  1.00 101.22 ? 573  PHE A CE2 1 
ATOM   4372  C  CZ  . PHE A  1  547 ? -4.561  25.635  13.010  1.00 101.06 ? 573  PHE A CZ  1 
ATOM   4373  N  N   . LEU A  1  548 ? -3.142  26.940  6.145   1.00 100.08 ? 574  LEU A N   1 
ATOM   4374  C  CA  . LEU A  1  548 ? -2.654  26.905  4.773   1.00 98.78  ? 574  LEU A CA  1 
ATOM   4375  C  C   . LEU A  1  548 ? -1.150  27.103  4.741   1.00 99.06  ? 574  LEU A C   1 
ATOM   4376  O  O   . LEU A  1  548 ? -0.667  28.200  4.479   1.00 99.16  ? 574  LEU A O   1 
ATOM   4377  C  CB  . LEU A  1  548 ? -3.314  27.989  3.933   1.00 98.27  ? 574  LEU A CB  1 
ATOM   4378  C  CG  . LEU A  1  548 ? -3.105  27.802  2.429   1.00 98.35  ? 574  LEU A CG  1 
ATOM   4379  C  CD1 . LEU A  1  548 ? -4.454  27.514  1.806   1.00 98.79  ? 574  LEU A CD1 1 
ATOM   4380  C  CD2 . LEU A  1  548 ? -2.465  29.030  1.790   1.00 97.76  ? 574  LEU A CD2 1 
ATOM   4381  N  N   . ASN A  1  549 ? -0.415  26.032  5.010   1.00 99.78  ? 575  ASN A N   1 
ATOM   4382  C  CA  . ASN A  1  549 ? 1.037   26.070  5.013   1.00 100.60 ? 575  ASN A CA  1 
ATOM   4383  C  C   . ASN A  1  549 ? 1.487   26.456  3.602   1.00 100.63 ? 575  ASN A C   1 
ATOM   4384  O  O   . ASN A  1  549 ? 0.856   26.068  2.620   1.00 100.61 ? 575  ASN A O   1 
ATOM   4385  C  CB  . ASN A  1  549 ? 1.575   24.683  5.385   1.00 101.94 ? 575  ASN A CB  1 
ATOM   4386  C  CG  . ASN A  1  549 ? 3.027   24.713  5.851   1.00 104.82 ? 575  ASN A CG  1 
ATOM   4387  O  OD1 . ASN A  1  549 ? 3.866   25.355  5.210   1.00 105.66 ? 575  ASN A OD1 1 
ATOM   4388  N  ND2 . ASN A  1  549 ? 3.331   24.018  6.952   1.00 107.17 ? 575  ASN A ND2 1 
ATOM   4389  N  N   . LEU A  1  550 ? 2.557   27.241  3.513   1.00 100.46 ? 576  LEU A N   1 
ATOM   4390  C  CA  . LEU A  1  550 ? 3.121   27.678  2.236   1.00 100.44 ? 576  LEU A CA  1 
ATOM   4391  C  C   . LEU A  1  550 ? 4.594   27.935  2.513   1.00 100.76 ? 576  LEU A C   1 
ATOM   4392  O  O   . LEU A  1  550 ? 5.317   28.516  1.703   1.00 99.85  ? 576  LEU A O   1 
ATOM   4393  C  CB  . LEU A  1  550 ? 2.452   28.965  1.743   1.00 100.87 ? 576  LEU A CB  1 
ATOM   4394  C  CG  . LEU A  1  550 ? 1.030   28.917  1.163   1.00 101.43 ? 576  LEU A CG  1 
ATOM   4395  C  CD1 . LEU A  1  550 ? 0.521   30.328  0.940   1.00 101.36 ? 576  LEU A CD1 1 
ATOM   4396  C  CD2 . LEU A  1  550 ? 1.019   28.156  -0.147  1.00 100.92 ? 576  LEU A CD2 1 
ATOM   4397  N  N   . THR A  1  551 ? 5.028   27.467  3.674   1.00 101.91 ? 577  THR A N   1 
ATOM   4398  C  CA  . THR A  1  551 ? 6.394   27.642  4.118   1.00 104.43 ? 577  THR A CA  1 
ATOM   4399  C  C   . THR A  1  551 ? 7.444   27.063  3.188   1.00 106.87 ? 577  THR A C   1 
ATOM   4400  O  O   . THR A  1  551 ? 7.204   26.080  2.497   1.00 106.91 ? 577  THR A O   1 
ATOM   4401  C  CB  . THR A  1  551 ? 6.583   27.024  5.499   1.00 103.67 ? 577  THR A CB  1 
ATOM   4402  O  OG1 . THR A  1  551 ? 6.409   25.608  5.415   1.00 103.32 ? 577  THR A OG1 1 
ATOM   4403  C  CG2 . THR A  1  551 ? 5.561   27.576  6.463   1.00 103.62 ? 577  THR A CG2 1 
ATOM   4404  N  N   . GLN A  1  552 ? 8.611   27.698  3.185   1.00 110.17 ? 578  GLN A N   1 
ATOM   4405  C  CA  . GLN A  1  552 ? 9.741   27.266  2.378   1.00 113.51 ? 578  GLN A CA  1 
ATOM   4406  C  C   . GLN A  1  552 ? 9.408   27.070  0.904   1.00 115.60 ? 578  GLN A C   1 
ATOM   4407  O  O   . GLN A  1  552 ? 8.817   26.067  0.521   1.00 116.07 ? 578  GLN A O   1 
ATOM   4408  C  CB  . GLN A  1  552 ? 10.305  25.976  2.970   1.00 113.92 ? 578  GLN A CB  1 
ATOM   4409  C  CG  . GLN A  1  552 ? 11.645  25.554  2.414   1.00 114.77 ? 578  GLN A CG  1 
ATOM   4410  C  CD  . GLN A  1  552 ? 12.308  24.511  3.290   1.00 115.66 ? 578  GLN A CD  1 
ATOM   4411  O  OE1 . GLN A  1  552 ? 13.362  23.969  2.946   1.00 116.62 ? 578  GLN A OE1 1 
ATOM   4412  N  NE2 . GLN A  1  552 ? 11.695  24.230  4.440   1.00 115.07 ? 578  GLN A NE2 1 
ATOM   4413  N  N   . ASN A  1  553 ? 9.798   28.041  0.088   1.00 118.41 ? 579  ASN A N   1 
ATOM   4414  C  CA  . ASN A  1  553 ? 9.569   27.998  -1.351  1.00 121.66 ? 579  ASN A CA  1 
ATOM   4415  C  C   . ASN A  1  553 ? 10.606  28.860  -2.046  1.00 124.69 ? 579  ASN A C   1 
ATOM   4416  O  O   . ASN A  1  553 ? 11.623  29.221  -1.459  1.00 124.27 ? 579  ASN A O   1 
ATOM   4417  C  CB  . ASN A  1  553 ? 8.171   28.514  -1.691  1.00 120.84 ? 579  ASN A CB  1 
ATOM   4418  C  CG  . ASN A  1  553 ? 7.121   27.431  -1.639  1.00 120.33 ? 579  ASN A CG  1 
ATOM   4419  O  OD1 . ASN A  1  553 ? 6.770   26.836  -2.660  1.00 119.56 ? 579  ASN A OD1 1 
ATOM   4420  N  ND2 . ASN A  1  553 ? 6.614   27.162  -0.440  1.00 120.56 ? 579  ASN A ND2 1 
ATOM   4421  N  N   . ASP A  1  554 ? 10.344  29.186  -3.304  1.00 129.03 ? 580  ASP A N   1 
ATOM   4422  C  CA  . ASP A  1  554 ? 11.263  30.012  -4.069  1.00 133.93 ? 580  ASP A CA  1 
ATOM   4423  C  C   . ASP A  1  554 ? 10.494  31.186  -4.667  1.00 136.52 ? 580  ASP A C   1 
ATOM   4424  O  O   . ASP A  1  554 ? 10.447  31.368  -5.887  1.00 137.11 ? 580  ASP A O   1 
ATOM   4425  C  CB  . ASP A  1  554 ? 11.937  29.169  -5.156  1.00 134.88 ? 580  ASP A CB  1 
ATOM   4426  C  CG  . ASP A  1  554 ? 12.792  28.048  -4.573  1.00 136.07 ? 580  ASP A CG  1 
ATOM   4427  O  OD1 . ASP A  1  554 ? 13.749  28.355  -3.821  1.00 136.32 ? 580  ASP A OD1 1 
ATOM   4428  O  OD2 . ASP A  1  554 ? 12.507  26.861  -4.858  1.00 136.29 ? 580  ASP A OD2 1 
ATOM   4429  N  N   . PHE A  1  555 ? 9.889   31.973  -3.779  1.00 139.12 ? 581  PHE A N   1 
ATOM   4430  C  CA  . PHE A  1  555 ? 9.097   33.137  -4.162  1.00 141.50 ? 581  PHE A CA  1 
ATOM   4431  C  C   . PHE A  1  555 ? 9.873   34.107  -5.039  1.00 144.29 ? 581  PHE A C   1 
ATOM   4432  O  O   . PHE A  1  555 ? 11.106  34.080  -5.079  1.00 144.41 ? 581  PHE A O   1 
ATOM   4433  C  CB  . PHE A  1  555 ? 8.622   33.896  -2.922  1.00 139.64 ? 581  PHE A CB  1 
ATOM   4434  C  CG  . PHE A  1  555 ? 7.973   33.035  -1.883  1.00 138.02 ? 581  PHE A CG  1 
ATOM   4435  C  CD1 . PHE A  1  555 ? 8.747   32.338  -0.958  1.00 137.60 ? 581  PHE A CD1 1 
ATOM   4436  C  CD2 . PHE A  1  555 ? 6.587   32.941  -1.812  1.00 136.67 ? 581  PHE A CD2 1 
ATOM   4437  C  CE1 . PHE A  1  555 ? 8.146   31.557  0.033   1.00 136.95 ? 581  PHE A CE1 1 
ATOM   4438  C  CE2 . PHE A  1  555 ? 5.973   32.168  -0.831  1.00 136.03 ? 581  PHE A CE2 1 
ATOM   4439  C  CZ  . PHE A  1  555 ? 6.754   31.472  0.099   1.00 136.17 ? 581  PHE A CZ  1 
ATOM   4440  N  N   . ALA A  1  556 ? 9.129   34.969  -5.729  1.00 147.44 ? 582  ALA A N   1 
ATOM   4441  C  CA  . ALA A  1  556 ? 9.700   35.995  -6.602  1.00 150.57 ? 582  ALA A CA  1 
ATOM   4442  C  C   . ALA A  1  556 ? 9.445   37.360  -5.954  1.00 152.51 ? 582  ALA A C   1 
ATOM   4443  O  O   . ALA A  1  556 ? 8.354   37.919  -6.078  1.00 152.89 ? 582  ALA A O   1 
ATOM   4444  C  CB  . ALA A  1  556 ? 9.045   35.937  -7.989  1.00 149.82 ? 582  ALA A CB  1 
ATOM   4445  N  N   . CYS A  1  557 ? 10.447  37.885  -5.252  1.00 154.76 ? 583  CYS A N   1 
ATOM   4446  C  CA  . CYS A  1  557 ? 10.313  39.170  -4.573  1.00 156.56 ? 583  CYS A CA  1 
ATOM   4447  C  C   . CYS A  1  557 ? 10.838  40.353  -5.391  1.00 157.96 ? 583  CYS A C   1 
ATOM   4448  O  O   . CYS A  1  557 ? 11.732  41.080  -4.959  1.00 158.18 ? 583  CYS A O   1 
ATOM   4449  C  CB  . CYS A  1  557 ? 11.002  39.114  -3.196  1.00 156.72 ? 583  CYS A CB  1 
ATOM   4450  S  SG  . CYS A  1  557 ? 10.266  37.898  -2.046  1.00 156.66 ? 583  CYS A SG  1 
ATOM   4451  N  N   . THR A  1  558 ? 10.278  40.516  -6.586  1.00 159.80 ? 584  THR A N   1 
ATOM   4452  C  CA  . THR A  1  558 ? 10.614  41.614  -7.491  1.00 161.89 ? 584  THR A CA  1 
ATOM   4453  C  C   . THR A  1  558 ? 9.248   42.163  -7.893  1.00 163.78 ? 584  THR A C   1 
ATOM   4454  O  O   . THR A  1  558 ? 8.280   41.404  -7.941  1.00 163.64 ? 584  THR A O   1 
ATOM   4455  C  CB  . THR A  1  558 ? 11.351  41.120  -8.753  1.00 161.40 ? 584  THR A CB  1 
ATOM   4456  O  OG1 . THR A  1  558 ? 10.464  40.327  -9.553  1.00 160.87 ? 584  THR A OG1 1 
ATOM   4457  C  CG2 . THR A  1  558 ? 12.566  40.293  -8.368  1.00 161.19 ? 584  THR A CG2 1 
ATOM   4458  N  N   . CYS A  1  559 ? 9.148   43.461  -8.180  1.00 166.19 ? 585  CYS A N   1 
ATOM   4459  C  CA  . CYS A  1  559 ? 7.845   44.030  -8.528  1.00 168.35 ? 585  CYS A CA  1 
ATOM   4460  C  C   . CYS A  1  559 ? 7.108   43.229  -9.605  1.00 168.47 ? 585  CYS A C   1 
ATOM   4461  O  O   . CYS A  1  559 ? 5.890   43.337  -9.738  1.00 168.59 ? 585  CYS A O   1 
ATOM   4462  C  CB  . CYS A  1  559 ? 7.954   45.512  -8.961  1.00 170.07 ? 585  CYS A CB  1 
ATOM   4463  S  SG  . CYS A  1  559 ? 6.296   46.239  -9.239  1.00 173.14 ? 585  CYS A SG  1 
ATOM   4464  N  N   . GLU A  1  560 ? 7.844   42.415  -10.355 1.00 168.46 ? 586  GLU A N   1 
ATOM   4465  C  CA  . GLU A  1  560 ? 7.255   41.601  -11.415 1.00 168.35 ? 586  GLU A CA  1 
ATOM   4466  C  C   . GLU A  1  560 ? 6.011   40.847  -10.943 1.00 168.09 ? 586  GLU A C   1 
ATOM   4467  O  O   . GLU A  1  560 ? 5.065   40.644  -11.709 1.00 167.66 ? 586  GLU A O   1 
ATOM   4468  C  CB  . GLU A  1  560 ? 8.291   40.604  -11.933 1.00 168.63 ? 586  GLU A CB  1 
ATOM   4469  C  CG  . GLU A  1  560 ? 7.802   39.732  -13.071 1.00 168.80 ? 586  GLU A CG  1 
ATOM   4470  C  CD  . GLU A  1  560 ? 8.818   38.681  -13.461 1.00 168.81 ? 586  GLU A CD  1 
ATOM   4471  O  OE1 . GLU A  1  560 ? 9.195   37.872  -12.587 1.00 168.89 ? 586  GLU A OE1 1 
ATOM   4472  O  OE2 . GLU A  1  560 ? 9.240   38.665  -14.635 1.00 168.57 ? 586  GLU A OE2 1 
ATOM   4473  N  N   . HIS A  1  561 ? 6.017   40.436  -9.677  1.00 167.94 ? 587  HIS A N   1 
ATOM   4474  C  CA  . HIS A  1  561 ? 4.902   39.699  -9.097  1.00 167.64 ? 587  HIS A CA  1 
ATOM   4475  C  C   . HIS A  1  561 ? 4.351   40.396  -7.857  1.00 167.21 ? 587  HIS A C   1 
ATOM   4476  O  O   . HIS A  1  561 ? 4.213   39.794  -6.794  1.00 166.94 ? 587  HIS A O   1 
ATOM   4477  C  CB  . HIS A  1  561 ? 5.350   38.276  -8.754  1.00 168.00 ? 587  HIS A CB  1 
ATOM   4478  C  CG  . HIS A  1  561 ? 5.708   37.453  -9.954  1.00 168.19 ? 587  HIS A CG  1 
ATOM   4479  N  ND1 . HIS A  1  561 ? 4.774   37.052  -10.888 1.00 168.30 ? 587  HIS A ND1 1 
ATOM   4480  C  CD2 . HIS A  1  561 ? 6.900   36.985  -10.394 1.00 167.98 ? 587  HIS A CD2 1 
ATOM   4481  C  CE1 . HIS A  1  561 ? 5.376   36.376  -11.849 1.00 168.23 ? 587  HIS A CE1 1 
ATOM   4482  N  NE2 . HIS A  1  561 ? 6.668   36.322  -11.574 1.00 168.17 ? 587  HIS A NE2 1 
ATOM   4483  N  N   . GLN A  1  562 ? 4.038   41.676  -8.009  1.00 167.12 ? 588  GLN A N   1 
ATOM   4484  C  CA  . GLN A  1  562 ? 3.490   42.479  -6.925  1.00 166.74 ? 588  GLN A CA  1 
ATOM   4485  C  C   . GLN A  1  562 ? 2.067   42.016  -6.651  1.00 166.24 ? 588  GLN A C   1 
ATOM   4486  O  O   . GLN A  1  562 ? 1.607   42.016  -5.511  1.00 166.17 ? 588  GLN A O   1 
ATOM   4487  C  CB  . GLN A  1  562 ? 3.488   43.959  -7.334  1.00 167.13 ? 588  GLN A CB  1 
ATOM   4488  C  CG  . GLN A  1  562 ? 2.848   44.914  -6.336  1.00 167.53 ? 588  GLN A CG  1 
ATOM   4489  C  CD  . GLN A  1  562 ? 2.679   46.316  -6.902  1.00 167.84 ? 588  GLN A CD  1 
ATOM   4490  O  OE1 . GLN A  1  562 ? 2.037   46.503  -7.935  1.00 168.09 ? 588  GLN A OE1 1 
ATOM   4491  N  NE2 . GLN A  1  562 ? 3.255   47.307  -6.227  1.00 168.11 ? 588  GLN A NE2 1 
ATOM   4492  N  N   . SER A  1  563 ? 1.383   41.609  -7.714  1.00 165.66 ? 589  SER A N   1 
ATOM   4493  C  CA  . SER A  1  563 ? -0.001  41.160  -7.631  1.00 164.92 ? 589  SER A CA  1 
ATOM   4494  C  C   . SER A  1  563 ? -0.194  39.923  -6.758  1.00 164.32 ? 589  SER A C   1 
ATOM   4495  O  O   . SER A  1  563 ? -1.164  39.835  -6.007  1.00 164.19 ? 589  SER A O   1 
ATOM   4496  C  CB  . SER A  1  563 ? -0.536  40.892  -9.042  1.00 164.73 ? 589  SER A CB  1 
ATOM   4497  O  OG  . SER A  1  563 ? -1.908  40.544  -9.017  1.00 164.65 ? 589  SER A OG  1 
ATOM   4498  N  N   . PHE A  1  564 ? 0.731   38.973  -6.858  1.00 163.69 ? 590  PHE A N   1 
ATOM   4499  C  CA  . PHE A  1  564 ? 0.656   37.736  -6.084  1.00 162.93 ? 590  PHE A CA  1 
ATOM   4500  C  C   . PHE A  1  564 ? 1.334   37.833  -4.712  1.00 162.15 ? 590  PHE A C   1 
ATOM   4501  O  O   . PHE A  1  564 ? 0.817   37.315  -3.722  1.00 162.02 ? 590  PHE A O   1 
ATOM   4502  C  CB  . PHE A  1  564 ? 1.271   36.589  -6.895  1.00 163.04 ? 590  PHE A CB  1 
ATOM   4503  C  CG  . PHE A  1  564 ? 1.278   35.262  -6.179  1.00 162.86 ? 590  PHE A CG  1 
ATOM   4504  C  CD1 . PHE A  1  564 ? 0.089   34.676  -5.750  1.00 162.87 ? 590  PHE A CD1 1 
ATOM   4505  C  CD2 . PHE A  1  564 ? 2.476   34.589  -5.955  1.00 162.36 ? 590  PHE A CD2 1 
ATOM   4506  C  CE1 . PHE A  1  564 ? 0.092   33.441  -5.104  1.00 162.53 ? 590  PHE A CE1 1 
ATOM   4507  C  CE2 . PHE A  1  564 ? 2.493   33.354  -5.310  1.00 162.29 ? 590  PHE A CE2 1 
ATOM   4508  C  CZ  . PHE A  1  564 ? 1.298   32.777  -4.885  1.00 162.54 ? 590  PHE A CZ  1 
ATOM   4509  N  N   . LEU A  1  565 ? 2.481   38.502  -4.650  1.00 161.18 ? 591  LEU A N   1 
ATOM   4510  C  CA  . LEU A  1  565 ? 3.211   38.650  -3.390  1.00 160.10 ? 591  LEU A CA  1 
ATOM   4511  C  C   . LEU A  1  565 ? 2.380   39.438  -2.380  1.00 160.11 ? 591  LEU A C   1 
ATOM   4512  O  O   . LEU A  1  565 ? 2.611   39.361  -1.171  1.00 159.87 ? 591  LEU A O   1 
ATOM   4513  C  CB  . LEU A  1  565 ? 4.553   39.350  -3.639  1.00 159.10 ? 591  LEU A CB  1 
ATOM   4514  C  CG  . LEU A  1  565 ? 5.607   39.324  -2.526  1.00 158.42 ? 591  LEU A CG  1 
ATOM   4515  C  CD1 . LEU A  1  565 ? 6.983   39.469  -3.152  1.00 158.27 ? 591  LEU A CD1 1 
ATOM   4516  C  CD2 . LEU A  1  565 ? 5.351   40.422  -1.501  1.00 158.28 ? 591  LEU A CD2 1 
ATOM   4517  N  N   . GLN A  1  566 ? 1.407   40.188  -2.893  1.00 160.31 ? 592  GLN A N   1 
ATOM   4518  C  CA  . GLN A  1  566 ? 0.516   40.997  -2.065  1.00 160.19 ? 592  GLN A CA  1 
ATOM   4519  C  C   . GLN A  1  566 ? -0.578  40.116  -1.461  1.00 160.03 ? 592  GLN A C   1 
ATOM   4520  O  O   . GLN A  1  566 ? -0.880  40.211  -0.273  1.00 160.20 ? 592  GLN A O   1 
ATOM   4521  C  CB  . GLN A  1  566 ? -0.111  42.115  -2.911  1.00 160.24 ? 592  GLN A CB  1 
ATOM   4522  C  CG  . GLN A  1  566 ? -1.175  42.945  -2.201  1.00 159.78 ? 592  GLN A CG  1 
ATOM   4523  C  CD  . GLN A  1  566 ? -0.628  43.790  -1.062  1.00 159.47 ? 592  GLN A CD  1 
ATOM   4524  O  OE1 . GLN A  1  566 ? -1.391  44.372  -0.292  1.00 158.98 ? 592  GLN A OE1 1 
ATOM   4525  N  NE2 . GLN A  1  566 ? 0.697   43.865  -0.954  1.00 159.31 ? 592  GLN A NE2 1 
ATOM   4526  N  N   . TRP A  1  567 ? -1.164  39.255  -2.287  1.00 159.69 ? 593  TRP A N   1 
ATOM   4527  C  CA  . TRP A  1  567 ? -2.220  38.344  -1.851  1.00 159.19 ? 593  TRP A CA  1 
ATOM   4528  C  C   . TRP A  1  567 ? -1.792  37.522  -0.636  1.00 158.63 ? 593  TRP A C   1 
ATOM   4529  O  O   . TRP A  1  567 ? -2.619  37.136  0.190   1.00 158.08 ? 593  TRP A O   1 
ATOM   4530  C  CB  . TRP A  1  567 ? -2.590  37.409  -3.000  1.00 160.07 ? 593  TRP A CB  1 
ATOM   4531  C  CG  . TRP A  1  567 ? -3.581  36.364  -2.628  1.00 160.75 ? 593  TRP A CG  1 
ATOM   4532  C  CD1 . TRP A  1  567 ? -4.914  36.538  -2.403  1.00 160.74 ? 593  TRP A CD1 1 
ATOM   4533  C  CD2 . TRP A  1  567 ? -3.314  34.973  -2.423  1.00 161.22 ? 593  TRP A CD2 1 
ATOM   4534  N  NE1 . TRP A  1  567 ? -5.495  35.338  -2.069  1.00 161.01 ? 593  TRP A NE1 1 
ATOM   4535  C  CE2 . TRP A  1  567 ? -4.535  34.362  -2.074  1.00 161.18 ? 593  TRP A CE2 1 
ATOM   4536  C  CE3 . TRP A  1  567 ? -2.160  34.184  -2.499  1.00 161.64 ? 593  TRP A CE3 1 
ATOM   4537  C  CZ2 . TRP A  1  567 ? -4.634  32.993  -1.800  1.00 161.53 ? 593  TRP A CZ2 1 
ATOM   4538  C  CZ3 . TRP A  1  567 ? -2.259  32.824  -2.227  1.00 161.81 ? 593  TRP A CZ3 1 
ATOM   4539  C  CH2 . TRP A  1  567 ? -3.486  32.245  -1.883  1.00 161.80 ? 593  TRP A CH2 1 
ATOM   4540  N  N   . ILE A  1  568 ? -0.493  37.256  -0.543  1.00 158.34 ? 594  ILE A N   1 
ATOM   4541  C  CA  . ILE A  1  568 ? 0.075   36.495  0.564   1.00 157.97 ? 594  ILE A CA  1 
ATOM   4542  C  C   . ILE A  1  568 ? -0.112  37.293  1.851   1.00 158.14 ? 594  ILE A C   1 
ATOM   4543  O  O   . ILE A  1  568 ? -0.509  36.752  2.884   1.00 158.26 ? 594  ILE A O   1 
ATOM   4544  C  CB  . ILE A  1  568 ? 1.586   36.239  0.337   1.00 157.48 ? 594  ILE A CB  1 
ATOM   4545  C  CG1 . ILE A  1  568 ? 1.802   35.500  -0.988  1.00 157.19 ? 594  ILE A CG1 1 
ATOM   4546  C  CG2 . ILE A  1  568 ? 2.162   35.439  1.486   1.00 157.45 ? 594  ILE A CG2 1 
ATOM   4547  C  CD1 . ILE A  1  568 ? 1.115   34.155  -1.078  1.00 156.62 ? 594  ILE A CD1 1 
ATOM   4548  N  N   . LYS A  1  569 ? 0.174   38.589  1.774   1.00 158.22 ? 595  LYS A N   1 
ATOM   4549  C  CA  . LYS A  1  569 ? 0.033   39.484  2.916   1.00 157.89 ? 595  LYS A CA  1 
ATOM   4550  C  C   . LYS A  1  569 ? -1.448  39.613  3.268   1.00 157.61 ? 595  LYS A C   1 
ATOM   4551  O  O   . LYS A  1  569 ? -1.839  39.451  4.424   1.00 157.33 ? 595  LYS A O   1 
ATOM   4552  C  CB  . LYS A  1  569 ? 0.582   40.874  2.577   1.00 158.08 ? 595  LYS A CB  1 
ATOM   4553  C  CG  . LYS A  1  569 ? 2.041   40.934  2.128   1.00 158.54 ? 595  LYS A CG  1 
ATOM   4554  C  CD  . LYS A  1  569 ? 2.351   42.313  1.540   1.00 159.00 ? 595  LYS A CD  1 
ATOM   4555  C  CE  . LYS A  1  569 ? 3.808   42.467  1.132   1.00 159.32 ? 595  LYS A CE  1 
ATOM   4556  N  NZ  . LYS A  1  569 ? 4.715   42.559  2.308   1.00 159.31 ? 595  LYS A NZ  1 
ATOM   4557  N  N   . ASP A  1  570 ? -2.258  39.900  2.250   1.00 157.50 ? 596  ASP A N   1 
ATOM   4558  C  CA  . ASP A  1  570 ? -3.701  40.089  2.399   1.00 157.24 ? 596  ASP A CA  1 
ATOM   4559  C  C   . ASP A  1  570 ? -4.406  39.099  3.316   1.00 156.66 ? 596  ASP A C   1 
ATOM   4560  O  O   . ASP A  1  570 ? -5.370  39.459  3.992   1.00 157.07 ? 596  ASP A O   1 
ATOM   4561  C  CB  . ASP A  1  570 ? -4.393  40.068  1.029   1.00 157.79 ? 596  ASP A CB  1 
ATOM   4562  C  CG  . ASP A  1  570 ? -4.003  41.247  0.154   1.00 158.19 ? 596  ASP A CG  1 
ATOM   4563  O  OD1 . ASP A  1  570 ? -4.049  42.400  0.640   1.00 157.98 ? 596  ASP A OD1 1 
ATOM   4564  O  OD2 . ASP A  1  570 ? -3.659  41.017  -1.026  1.00 158.55 ? 596  ASP A OD2 1 
ATOM   4565  N  N   . GLN A  1  571 ? -3.953  37.850  3.326   1.00 155.44 ? 597  GLN A N   1 
ATOM   4566  C  CA  . GLN A  1  571 ? -4.573  36.854  4.189   1.00 153.72 ? 597  GLN A CA  1 
ATOM   4567  C  C   . GLN A  1  571 ? -3.558  36.050  4.978   1.00 152.17 ? 597  GLN A C   1 
ATOM   4568  O  O   . GLN A  1  571 ? -3.416  34.847  4.781   1.00 151.99 ? 597  GLN A O   1 
ATOM   4569  C  CB  . GLN A  1  571 ? -5.474  35.916  3.379   1.00 153.84 ? 597  GLN A CB  1 
ATOM   4570  C  CG  . GLN A  1  571 ? -4.942  35.533  2.016   1.00 154.18 ? 597  GLN A CG  1 
ATOM   4571  C  CD  . GLN A  1  571 ? -5.897  34.627  1.273   1.00 154.72 ? 597  GLN A CD  1 
ATOM   4572  O  OE1 . GLN A  1  571 ? -6.024  33.446  1.591   1.00 155.35 ? 597  GLN A OE1 1 
ATOM   4573  N  NE2 . GLN A  1  571 ? -6.592  35.183  0.287   1.00 155.25 ? 597  GLN A NE2 1 
ATOM   4574  N  N   . ARG A  1  572 ? -2.850  36.734  5.870   1.00 150.38 ? 598  ARG A N   1 
ATOM   4575  C  CA  . ARG A  1  572 ? -1.862  36.088  6.714   1.00 148.58 ? 598  ARG A CA  1 
ATOM   4576  C  C   . ARG A  1  572 ? -2.580  35.548  7.942   1.00 146.67 ? 598  ARG A C   1 
ATOM   4577  O  O   . ARG A  1  572 ? -1.965  35.246  8.962   1.00 146.05 ? 598  ARG A O   1 
ATOM   4578  C  CB  . ARG A  1  572 ? -0.761  37.077  7.110   1.00 149.38 ? 598  ARG A CB  1 
ATOM   4579  C  CG  . ARG A  1  572 ? -1.232  38.298  7.874   1.00 150.53 ? 598  ARG A CG  1 
ATOM   4580  C  CD  . ARG A  1  572 ? -0.079  39.275  8.056   1.00 151.86 ? 598  ARG A CD  1 
ATOM   4581  N  NE  . ARG A  1  572 ? 1.073   38.639  8.695   1.00 153.30 ? 598  ARG A NE  1 
ATOM   4582  C  CZ  . ARG A  1  572 ? 2.302   39.152  8.715   1.00 153.55 ? 598  ARG A CZ  1 
ATOM   4583  N  NH1 . ARG A  1  572 ? 2.549   40.317  8.129   1.00 153.56 ? 598  ARG A NH1 1 
ATOM   4584  N  NH2 . ARG A  1  572 ? 3.287   38.496  9.318   1.00 153.10 ? 598  ARG A NH2 1 
ATOM   4585  N  N   . GLN A  1  573 ? -3.899  35.436  7.825   1.00 144.88 ? 599  GLN A N   1 
ATOM   4586  C  CA  . GLN A  1  573 ? -4.723  34.911  8.897   1.00 143.82 ? 599  GLN A CA  1 
ATOM   4587  C  C   . GLN A  1  573 ? -5.071  33.467  8.598   1.00 142.66 ? 599  GLN A C   1 
ATOM   4588  O  O   . GLN A  1  573 ? -5.917  32.871  9.264   1.00 142.44 ? 599  GLN A O   1 
ATOM   4589  C  CB  . GLN A  1  573 ? -6.004  35.725  9.053   1.00 144.96 ? 599  GLN A CB  1 
ATOM   4590  C  CG  . GLN A  1  573 ? -5.844  36.932  9.962   1.00 146.86 ? 599  GLN A CG  1 
ATOM   4591  C  CD  . GLN A  1  573 ? -5.269  36.564  11.327  1.00 147.59 ? 599  GLN A CD  1 
ATOM   4592  O  OE1 . GLN A  1  573 ? -5.765  35.655  11.998  1.00 147.95 ? 599  GLN A OE1 1 
ATOM   4593  N  NE2 . GLN A  1  573 ? -4.223  37.275  11.743  1.00 147.39 ? 599  GLN A NE2 1 
ATOM   4594  N  N   . LEU A  1  574 ? -4.417  32.919  7.577   1.00 141.16 ? 600  LEU A N   1 
ATOM   4595  C  CA  . LEU A  1  574 ? -4.610  31.529  7.160   1.00 139.12 ? 600  LEU A CA  1 
ATOM   4596  C  C   . LEU A  1  574 ? -3.258  30.819  7.148   1.00 138.26 ? 600  LEU A C   1 
ATOM   4597  O  O   . LEU A  1  574 ? -3.180  29.621  7.386   1.00 138.49 ? 600  LEU A O   1 
ATOM   4598  C  CB  . LEU A  1  574 ? -5.228  31.460  5.758   1.00 137.78 ? 600  LEU A CB  1 
ATOM   4599  C  CG  . LEU A  1  574 ? -6.671  31.934  5.566   1.00 137.27 ? 600  LEU A CG  1 
ATOM   4600  C  CD1 . LEU A  1  574 ? -7.041  31.841  4.105   1.00 136.61 ? 600  LEU A CD1 1 
ATOM   4601  C  CD2 . LEU A  1  574 ? -7.613  31.086  6.394   1.00 137.13 ? 600  LEU A CD2 1 
ATOM   4602  N  N   . LEU A  1  575 ? -2.199  31.574  6.878   1.00 137.32 ? 601  LEU A N   1 
ATOM   4603  C  CA  . LEU A  1  575 ? -0.847  31.033  6.823   1.00 136.72 ? 601  LEU A CA  1 
ATOM   4604  C  C   . LEU A  1  575 ? -0.358  30.351  8.093   1.00 136.63 ? 601  LEU A C   1 
ATOM   4605  O  O   . LEU A  1  575 ? -1.116  30.122  9.030   1.00 136.60 ? 601  LEU A O   1 
ATOM   4606  C  CB  . LEU A  1  575 ? 0.137   32.137  6.454   1.00 136.67 ? 601  LEU A CB  1 
ATOM   4607  C  CG  . LEU A  1  575 ? 0.256   32.465  4.967   1.00 136.78 ? 601  LEU A CG  1 
ATOM   4608  C  CD1 . LEU A  1  575 ? 1.046   33.751  4.783   1.00 137.31 ? 601  LEU A CD1 1 
ATOM   4609  C  CD2 . LEU A  1  575 ? 0.939   31.307  4.253   1.00 137.20 ? 601  LEU A CD2 1 
ATOM   4610  N  N   . VAL A  1  576 ? 0.929   30.022  8.097   1.00 136.72 ? 602  VAL A N   1 
ATOM   4611  C  CA  . VAL A  1  576 ? 1.568   29.369  9.228   1.00 136.94 ? 602  VAL A CA  1 
ATOM   4612  C  C   . VAL A  1  576 ? 2.946   29.992  9.470   1.00 137.98 ? 602  VAL A C   1 
ATOM   4613  O  O   . VAL A  1  576 ? 3.122   31.196  9.283   1.00 138.00 ? 602  VAL A O   1 
ATOM   4614  C  CB  . VAL A  1  576 ? 1.714   27.861  8.975   1.00 135.90 ? 602  VAL A CB  1 
ATOM   4615  C  CG1 . VAL A  1  576 ? 0.343   27.204  8.941   1.00 134.82 ? 602  VAL A CG1 1 
ATOM   4616  C  CG2 . VAL A  1  576 ? 2.428   27.631  7.664   1.00 135.57 ? 602  VAL A CG2 1 
ATOM   4617  N  N   . GLU A  1  577 ? 3.914   29.179  9.881   1.00 139.08 ? 603  GLU A N   1 
ATOM   4618  C  CA  . GLU A  1  577 ? 5.272   29.652  10.155  1.00 141.05 ? 603  GLU A CA  1 
ATOM   4619  C  C   . GLU A  1  577 ? 5.781   30.660  9.124   1.00 142.29 ? 603  GLU A C   1 
ATOM   4620  O  O   . GLU A  1  577 ? 6.296   30.271  8.077   1.00 142.65 ? 603  GLU A O   1 
ATOM   4621  C  CB  . GLU A  1  577 ? 6.224   28.465  10.191  1.00 141.38 ? 603  GLU A CB  1 
ATOM   4622  C  CG  . GLU A  1  577 ? 5.806   27.368  11.142  1.00 142.59 ? 603  GLU A CG  1 
ATOM   4623  C  CD  . GLU A  1  577 ? 6.479   26.048  10.823  1.00 143.44 ? 603  GLU A CD  1 
ATOM   4624  O  OE1 . GLU A  1  577 ? 6.156   25.452  9.772   1.00 143.35 ? 603  GLU A OE1 1 
ATOM   4625  O  OE2 . GLU A  1  577 ? 7.339   25.612  11.614  1.00 144.11 ? 603  GLU A OE2 1 
ATOM   4626  N  N   . VAL A  1  578 ? 5.665   31.950  9.430   1.00 143.46 ? 604  VAL A N   1 
ATOM   4627  C  CA  . VAL A  1  578 ? 6.105   32.994  8.506   1.00 144.62 ? 604  VAL A CA  1 
ATOM   4628  C  C   . VAL A  1  578 ? 7.621   33.249  8.498   1.00 145.79 ? 604  VAL A C   1 
ATOM   4629  O  O   . VAL A  1  578 ? 8.150   33.771  7.516   1.00 146.39 ? 604  VAL A O   1 
ATOM   4630  C  CB  . VAL A  1  578 ? 5.359   34.327  8.786   1.00 144.36 ? 604  VAL A CB  1 
ATOM   4631  C  CG1 . VAL A  1  578 ? 5.788   35.401  7.788   1.00 143.98 ? 604  VAL A CG1 1 
ATOM   4632  C  CG2 . VAL A  1  578 ? 3.856   34.103  8.699   1.00 143.14 ? 604  VAL A CG2 1 
ATOM   4633  N  N   . GLU A  1  579 ? 8.322   32.883  9.572   1.00 146.86 ? 605  GLU A N   1 
ATOM   4634  C  CA  . GLU A  1  579 ? 9.776   33.086  9.632   1.00 148.07 ? 605  GLU A CA  1 
ATOM   4635  C  C   . GLU A  1  579 ? 10.530  32.070  8.771   1.00 148.47 ? 605  GLU A C   1 
ATOM   4636  O  O   . GLU A  1  579 ? 11.760  31.970  8.838   1.00 147.92 ? 605  GLU A O   1 
ATOM   4637  C  CB  . GLU A  1  579 ? 10.291  33.005  11.081  1.00 148.78 ? 605  GLU A CB  1 
ATOM   4638  C  CG  . GLU A  1  579 ? 10.119  31.651  11.766  1.00 149.65 ? 605  GLU A CG  1 
ATOM   4639  C  CD  . GLU A  1  579 ? 8.699   31.409  12.250  1.00 150.23 ? 605  GLU A CD  1 
ATOM   4640  O  OE1 . GLU A  1  579 ? 8.222   32.192  13.098  1.00 150.37 ? 605  GLU A OE1 1 
ATOM   4641  O  OE2 . GLU A  1  579 ? 8.059   30.441  11.787  1.00 150.59 ? 605  GLU A OE2 1 
ATOM   4642  N  N   . ARG A  1  580 ? 9.778   31.322  7.967   1.00 149.13 ? 606  ARG A N   1 
ATOM   4643  C  CA  . ARG A  1  580 ? 10.341  30.308  7.078   1.00 149.41 ? 606  ARG A CA  1 
ATOM   4644  C  C   . ARG A  1  580 ? 9.846   30.498  5.646   1.00 148.90 ? 606  ARG A C   1 
ATOM   4645  O  O   . ARG A  1  580 ? 9.955   29.592  4.818   1.00 148.39 ? 606  ARG A O   1 
ATOM   4646  C  CB  . ARG A  1  580 ? 9.967   28.899  7.559   1.00 150.05 ? 606  ARG A CB  1 
ATOM   4647  C  CG  . ARG A  1  580 ? 10.737  28.397  8.783   1.00 150.40 ? 606  ARG A CG  1 
ATOM   4648  C  CD  . ARG A  1  580 ? 10.310  26.978  9.135   1.00 150.47 ? 606  ARG A CD  1 
ATOM   4649  N  NE  . ARG A  1  580 ? 10.369  26.099  7.967   1.00 150.80 ? 606  ARG A NE  1 
ATOM   4650  C  CZ  . ARG A  1  580 ? 9.862   24.871  7.919   1.00 150.53 ? 606  ARG A CZ  1 
ATOM   4651  N  NH1 . ARG A  1  580 ? 9.252   24.360  8.980   1.00 150.21 ? 606  ARG A NH1 1 
ATOM   4652  N  NH2 . ARG A  1  580 ? 9.952   24.159  6.801   1.00 150.09 ? 606  ARG A NH2 1 
ATOM   4653  N  N   . MET A  1  581 ? 9.294   31.673  5.363   1.00 148.47 ? 607  MET A N   1 
ATOM   4654  C  CA  . MET A  1  581 ? 8.798   31.979  4.030   1.00 148.76 ? 607  MET A CA  1 
ATOM   4655  C  C   . MET A  1  581 ? 9.741   32.945  3.314   1.00 150.01 ? 607  MET A C   1 
ATOM   4656  O  O   . MET A  1  581 ? 9.310   33.781  2.521   1.00 150.42 ? 607  MET A O   1 
ATOM   4657  C  CB  . MET A  1  581 ? 7.396   32.583  4.110   1.00 147.17 ? 607  MET A CB  1 
ATOM   4658  C  CG  . MET A  1  581 ? 6.316   31.594  4.502   1.00 145.89 ? 607  MET A CG  1 
ATOM   4659  S  SD  . MET A  1  581 ? 4.653   32.318  4.516   1.00 143.84 ? 607  MET A SD  1 
ATOM   4660  C  CE  . MET A  1  581 ? 4.170   32.109  2.795   1.00 144.78 ? 607  MET A CE  1 
ATOM   4661  N  N   . GLU A  1  582 ? 11.032  32.809  3.598   1.00 151.22 ? 608  GLU A N   1 
ATOM   4662  C  CA  . GLU A  1  582 ? 12.078  33.645  3.011   1.00 152.14 ? 608  GLU A CA  1 
ATOM   4663  C  C   . GLU A  1  582 ? 11.992  33.787  1.486   1.00 153.11 ? 608  GLU A C   1 
ATOM   4664  O  O   . GLU A  1  582 ? 11.515  32.890  0.788   1.00 152.68 ? 608  GLU A O   1 
ATOM   4665  C  CB  . GLU A  1  582 ? 13.449  33.082  3.409   1.00 151.67 ? 608  GLU A CB  1 
ATOM   4666  C  CG  . GLU A  1  582 ? 13.750  33.203  4.900   1.00 151.22 ? 608  GLU A CG  1 
ATOM   4667  C  CD  . GLU A  1  582 ? 14.780  32.201  5.392   1.00 151.04 ? 608  GLU A CD  1 
ATOM   4668  O  OE1 . GLU A  1  582 ? 14.402  31.043  5.666   1.00 150.39 ? 608  GLU A OE1 1 
ATOM   4669  O  OE2 . GLU A  1  582 ? 15.968  32.571  5.499   1.00 151.03 ? 608  GLU A OE2 1 
ATOM   4670  N  N   . CYS A  1  583 ? 12.451  34.929  0.977   1.00 154.55 ? 609  CYS A N   1 
ATOM   4671  C  CA  . CYS A  1  583 ? 12.444  35.188  -0.461  1.00 155.81 ? 609  CYS A CA  1 
ATOM   4672  C  C   . CYS A  1  583 ? 13.501  34.310  -1.123  1.00 156.23 ? 609  CYS A C   1 
ATOM   4673  O  O   . CYS A  1  583 ? 14.204  33.554  -0.452  1.00 155.58 ? 609  CYS A O   1 
ATOM   4674  C  CB  . CYS A  1  583 ? 12.760  36.663  -0.763  1.00 156.44 ? 609  CYS A CB  1 
ATOM   4675  S  SG  . CYS A  1  583 ? 11.463  37.903  -0.404  1.00 156.22 ? 609  CYS A SG  1 
ATOM   4676  N  N   . ALA A  1  584 ? 13.621  34.423  -2.441  1.00 156.96 ? 610  ALA A N   1 
ATOM   4677  C  CA  . ALA A  1  584 ? 14.596  33.629  -3.162  1.00 157.77 ? 610  ALA A CA  1 
ATOM   4678  C  C   . ALA A  1  584 ? 15.200  34.318  -4.382  1.00 158.58 ? 610  ALA A C   1 
ATOM   4679  O  O   . ALA A  1  584 ? 16.383  34.134  -4.666  1.00 158.51 ? 610  ALA A O   1 
ATOM   4680  C  CB  . ALA A  1  584 ? 13.968  32.302  -3.574  1.00 157.73 ? 610  ALA A CB  1 
ATOM   4681  N  N   . THR A  1  585 ? 14.410  35.123  -5.091  1.00 159.64 ? 611  THR A N   1 
ATOM   4682  C  CA  . THR A  1  585 ? 14.903  35.785  -6.303  1.00 160.87 ? 611  THR A CA  1 
ATOM   4683  C  C   . THR A  1  585 ? 15.879  36.970  -6.184  1.00 161.71 ? 611  THR A C   1 
ATOM   4684  O  O   . THR A  1  585 ? 16.860  37.033  -6.928  1.00 162.21 ? 611  THR A O   1 
ATOM   4685  C  CB  . THR A  1  585 ? 13.732  36.201  -7.223  1.00 160.59 ? 611  THR A CB  1 
ATOM   4686  O  OG1 . THR A  1  585 ? 12.745  36.902  -6.461  1.00 161.08 ? 611  THR A OG1 1 
ATOM   4687  C  CG2 . THR A  1  585 ? 13.103  34.974  -7.862  1.00 160.34 ? 611  THR A CG2 1 
ATOM   4688  N  N   . PRO A  1  586 ? 15.627  37.930  -5.277  1.00 161.81 ? 612  PRO A N   1 
ATOM   4689  C  CA  . PRO A  1  586 ? 16.593  39.034  -5.205  1.00 161.80 ? 612  PRO A CA  1 
ATOM   4690  C  C   . PRO A  1  586 ? 17.938  38.554  -4.651  1.00 162.11 ? 612  PRO A C   1 
ATOM   4691  O  O   . PRO A  1  586 ? 18.045  38.239  -3.466  1.00 161.89 ? 612  PRO A O   1 
ATOM   4692  C  CB  . PRO A  1  586 ? 15.908  40.033  -4.275  1.00 161.56 ? 612  PRO A CB  1 
ATOM   4693  C  CG  . PRO A  1  586 ? 14.456  39.762  -4.497  1.00 161.64 ? 612  PRO A CG  1 
ATOM   4694  C  CD  . PRO A  1  586 ? 14.413  38.252  -4.512  1.00 161.78 ? 612  PRO A CD  1 
ATOM   4695  N  N   . SER A  1  587 ? 18.963  38.502  -5.502  1.00 162.64 ? 613  SER A N   1 
ATOM   4696  C  CA  . SER A  1  587 ? 20.288  38.050  -5.072  1.00 163.08 ? 613  SER A CA  1 
ATOM   4697  C  C   . SER A  1  587 ? 20.844  38.962  -3.985  1.00 164.05 ? 613  SER A C   1 
ATOM   4698  O  O   . SER A  1  587 ? 21.892  38.677  -3.398  1.00 164.03 ? 613  SER A O   1 
ATOM   4699  C  CB  . SER A  1  587 ? 21.264  38.006  -6.259  1.00 162.16 ? 613  SER A CB  1 
ATOM   4700  O  OG  . SER A  1  587 ? 21.591  39.303  -6.720  1.00 160.93 ? 613  SER A OG  1 
ATOM   4701  N  N   . ASP A  1  588 ? 20.124  40.053  -3.724  1.00 165.20 ? 614  ASP A N   1 
ATOM   4702  C  CA  . ASP A  1  588 ? 20.499  41.037  -2.709  1.00 165.92 ? 614  ASP A CA  1 
ATOM   4703  C  C   . ASP A  1  588 ? 19.473  41.036  -1.569  1.00 165.72 ? 614  ASP A C   1 
ATOM   4704  O  O   . ASP A  1  588 ? 19.806  41.338  -0.419  1.00 165.52 ? 614  ASP A O   1 
ATOM   4705  C  CB  . ASP A  1  588 ? 20.582  42.443  -3.329  1.00 166.65 ? 614  ASP A CB  1 
ATOM   4706  C  CG  . ASP A  1  588 ? 21.715  42.584  -4.352  1.00 167.39 ? 614  ASP A CG  1 
ATOM   4707  O  OD1 . ASP A  1  588 ? 22.898  42.503  -3.957  1.00 167.83 ? 614  ASP A OD1 1 
ATOM   4708  O  OD2 . ASP A  1  588 ? 21.421  42.778  -5.553  1.00 167.33 ? 614  ASP A OD2 1 
ATOM   4709  N  N   . LYS A  1  589 ? 18.226  40.699  -1.895  1.00 165.45 ? 615  LYS A N   1 
ATOM   4710  C  CA  . LYS A  1  589 ? 17.158  40.651  -0.899  1.00 165.07 ? 615  LYS A CA  1 
ATOM   4711  C  C   . LYS A  1  589 ? 16.556  39.245  -0.809  1.00 164.69 ? 615  LYS A C   1 
ATOM   4712  O  O   . LYS A  1  589 ? 15.499  38.974  -1.373  1.00 164.45 ? 615  LYS A O   1 
ATOM   4713  C  CB  . LYS A  1  589 ? 16.062  41.672  -1.239  1.00 164.78 ? 615  LYS A CB  1 
ATOM   4714  C  CG  . LYS A  1  589 ? 16.544  43.127  -1.332  1.00 164.52 ? 615  LYS A CG  1 
ATOM   4715  C  CD  . LYS A  1  589 ? 17.232  43.600  -0.053  1.00 164.20 ? 615  LYS A CD  1 
ATOM   4716  C  CE  . LYS A  1  589 ? 16.296  43.595  1.144   1.00 164.05 ? 615  LYS A CE  1 
ATOM   4717  N  NZ  . LYS A  1  589 ? 15.150  44.527  0.961   1.00 163.98 ? 615  LYS A NZ  1 
ATOM   4718  N  N   . GLN A  1  590 ? 17.247  38.363  -0.088  1.00 164.35 ? 616  GLN A N   1 
ATOM   4719  C  CA  . GLN A  1  590 ? 16.827  36.976  0.105   1.00 163.81 ? 616  GLN A CA  1 
ATOM   4720  C  C   . GLN A  1  590 ? 16.946  36.590  1.576   1.00 163.55 ? 616  GLN A C   1 
ATOM   4721  O  O   . GLN A  1  590 ? 18.021  36.689  2.164   1.00 163.39 ? 616  GLN A O   1 
ATOM   4722  C  CB  . GLN A  1  590 ? 17.711  36.045  -0.728  1.00 164.04 ? 616  GLN A CB  1 
ATOM   4723  C  CG  . GLN A  1  590 ? 17.513  34.556  -0.448  1.00 163.25 ? 616  GLN A CG  1 
ATOM   4724  C  CD  . GLN A  1  590 ? 18.626  33.707  -1.034  1.00 162.61 ? 616  GLN A CD  1 
ATOM   4725  O  OE1 . GLN A  1  590 ? 18.870  33.721  -2.242  1.00 162.23 ? 616  GLN A OE1 1 
ATOM   4726  N  NE2 . GLN A  1  590 ? 19.311  32.964  -0.176  1.00 161.88 ? 616  GLN A NE2 1 
ATOM   4727  N  N   . GLY A  1  591 ? 15.841  36.146  2.167   1.00 163.65 ? 617  GLY A N   1 
ATOM   4728  C  CA  . GLY A  1  591 ? 15.863  35.750  3.565   1.00 163.95 ? 617  GLY A CA  1 
ATOM   4729  C  C   . GLY A  1  591 ? 14.970  36.611  4.440   1.00 164.07 ? 617  GLY A C   1 
ATOM   4730  O  O   . GLY A  1  591 ? 14.840  36.375  5.641   1.00 163.63 ? 617  GLY A O   1 
ATOM   4731  N  N   . MET A  1  592 ? 14.355  37.618  3.829   1.00 164.44 ? 618  MET A N   1 
ATOM   4732  C  CA  . MET A  1  592 ? 13.468  38.532  4.537   1.00 164.86 ? 618  MET A CA  1 
ATOM   4733  C  C   . MET A  1  592 ? 12.040  38.023  4.361   1.00 165.51 ? 618  MET A C   1 
ATOM   4734  O  O   . MET A  1  592 ? 11.638  37.653  3.257   1.00 165.40 ? 618  MET A O   1 
ATOM   4735  C  CB  . MET A  1  592 ? 13.613  39.941  3.953   1.00 164.41 ? 618  MET A CB  1 
ATOM   4736  C  CG  . MET A  1  592 ? 12.995  41.062  4.778   1.00 163.48 ? 618  MET A CG  1 
ATOM   4737  S  SD  . MET A  1  592 ? 13.309  42.678  4.023   1.00 162.20 ? 618  MET A SD  1 
ATOM   4738  C  CE  . MET A  1  592 ? 15.063  42.852  4.327   1.00 161.79 ? 618  MET A CE  1 
ATOM   4739  N  N   . PRO A  1  593 ? 11.251  37.995  5.447   1.00 166.43 ? 619  PRO A N   1 
ATOM   4740  C  CA  . PRO A  1  593 ? 9.867   37.514  5.358   1.00 167.30 ? 619  PRO A CA  1 
ATOM   4741  C  C   . PRO A  1  593 ? 9.035   38.215  4.281   1.00 168.06 ? 619  PRO A C   1 
ATOM   4742  O  O   . PRO A  1  593 ? 8.978   39.442  4.228   1.00 168.21 ? 619  PRO A O   1 
ATOM   4743  C  CB  . PRO A  1  593 ? 9.330   37.744  6.773   1.00 166.96 ? 619  PRO A CB  1 
ATOM   4744  C  CG  . PRO A  1  593 ? 10.148  38.902  7.267   1.00 166.74 ? 619  PRO A CG  1 
ATOM   4745  C  CD  . PRO A  1  593 ? 11.528  38.550  6.783   1.00 166.55 ? 619  PRO A CD  1 
ATOM   4746  N  N   . VAL A  1  594 ? 8.396   37.419  3.426   1.00 169.01 ? 620  VAL A N   1 
ATOM   4747  C  CA  . VAL A  1  594 ? 7.571   37.940  2.341   1.00 170.10 ? 620  VAL A CA  1 
ATOM   4748  C  C   . VAL A  1  594 ? 6.437   38.825  2.855   1.00 171.28 ? 620  VAL A C   1 
ATOM   4749  O  O   . VAL A  1  594 ? 5.955   39.710  2.143   1.00 171.55 ? 620  VAL A O   1 
ATOM   4750  C  CB  . VAL A  1  594 ? 6.985   36.790  1.492   1.00 169.60 ? 620  VAL A CB  1 
ATOM   4751  C  CG1 . VAL A  1  594 ? 6.042   37.341  0.435   1.00 170.01 ? 620  VAL A CG1 1 
ATOM   4752  C  CG2 . VAL A  1  594 ? 8.111   36.018  0.830   1.00 169.39 ? 620  VAL A CG2 1 
ATOM   4753  N  N   . LEU A  1  595 ? 6.013   38.587  4.093   1.00 172.34 ? 621  LEU A N   1 
ATOM   4754  C  CA  . LEU A  1  595 ? 4.948   39.386  4.689   1.00 173.40 ? 621  LEU A CA  1 
ATOM   4755  C  C   . LEU A  1  595 ? 5.543   40.674  5.264   1.00 174.16 ? 621  LEU A C   1 
ATOM   4756  O  O   . LEU A  1  595 ? 5.004   41.246  6.213   1.00 174.25 ? 621  LEU A O   1 
ATOM   4757  C  CB  . LEU A  1  595 ? 4.238   38.598  5.799   1.00 173.29 ? 621  LEU A CB  1 
ATOM   4758  C  CG  . LEU A  1  595 ? 3.531   37.293  5.411   1.00 173.41 ? 621  LEU A CG  1 
ATOM   4759  C  CD1 . LEU A  1  595 ? 2.844   36.701  6.632   1.00 173.28 ? 621  LEU A CD1 1 
ATOM   4760  C  CD2 . LEU A  1  595 ? 2.510   37.561  4.313   1.00 173.41 ? 621  LEU A CD2 1 
ATOM   4761  N  N   . SER A  1  596 ? 6.653   41.121  4.673   1.00 175.00 ? 622  SER A N   1 
ATOM   4762  C  CA  . SER A  1  596 ? 7.356   42.332  5.104   1.00 175.49 ? 622  SER A CA  1 
ATOM   4763  C  C   . SER A  1  596 ? 8.268   42.887  4.002   1.00 175.98 ? 622  SER A C   1 
ATOM   4764  O  O   . SER A  1  596 ? 9.495   42.820  4.118   1.00 175.76 ? 622  SER A O   1 
ATOM   4765  C  CB  . SER A  1  596 ? 8.213   42.034  6.340   1.00 175.39 ? 622  SER A CB  1 
ATOM   4766  O  OG  . SER A  1  596 ? 7.443   41.478  7.387   1.00 175.36 ? 622  SER A OG  1 
ATOM   4767  N  N   . LEU A  1  597 ? 7.677   43.437  2.942   1.00 176.58 ? 623  LEU A N   1 
ATOM   4768  C  CA  . LEU A  1  597 ? 8.465   43.985  1.836   1.00 177.30 ? 623  LEU A CA  1 
ATOM   4769  C  C   . LEU A  1  597 ? 8.048   45.371  1.349   1.00 177.55 ? 623  LEU A C   1 
ATOM   4770  O  O   . LEU A  1  597 ? 6.857   45.690  1.286   1.00 177.40 ? 623  LEU A O   1 
ATOM   4771  C  CB  . LEU A  1  597 ? 8.439   43.033  0.636   1.00 177.46 ? 623  LEU A CB  1 
ATOM   4772  C  CG  . LEU A  1  597 ? 9.523   41.958  0.504   1.00 177.38 ? 623  LEU A CG  1 
ATOM   4773  C  CD1 . LEU A  1  597 ? 10.897  42.606  0.583   1.00 176.80 ? 623  LEU A CD1 1 
ATOM   4774  C  CD2 . LEU A  1  597 ? 9.356   40.919  1.593   1.00 177.70 ? 623  LEU A CD2 1 
ATOM   4775  N  N   . ASN A  1  598 ? 9.047   46.184  0.999   1.00 177.82 ? 624  ASN A N   1 
ATOM   4776  C  CA  . ASN A  1  598 ? 8.817   47.527  0.473   1.00 177.97 ? 624  ASN A CA  1 
ATOM   4777  C  C   . ASN A  1  598 ? 8.306   47.365  -0.958  1.00 177.91 ? 624  ASN A C   1 
ATOM   4778  O  O   . ASN A  1  598 ? 9.097   47.241  -1.897  1.00 177.83 ? 624  ASN A O   1 
ATOM   4779  C  CB  . ASN A  1  598 ? 10.122  48.340  0.455   1.00 177.89 ? 624  ASN A CB  1 
ATOM   4780  C  CG  . ASN A  1  598 ? 10.616  48.699  1.846   1.00 177.75 ? 624  ASN A CG  1 
ATOM   4781  O  OD1 . ASN A  1  598 ? 9.960   49.437  2.582   1.00 177.62 ? 624  ASN A OD1 1 
ATOM   4782  N  ND2 . ASN A  1  598 ? 11.782  48.180  2.210   1.00 177.49 ? 624  ASN A ND2 1 
ATOM   4783  N  N   . ILE A  1  599 ? 6.985   47.357  -1.113  1.00 177.78 ? 625  ILE A N   1 
ATOM   4784  C  CA  . ILE A  1  599 ? 6.358   47.193  -2.420  1.00 177.22 ? 625  ILE A CA  1 
ATOM   4785  C  C   . ILE A  1  599 ? 6.524   48.447  -3.283  1.00 176.97 ? 625  ILE A C   1 
ATOM   4786  O  O   . ILE A  1  599 ? 5.544   49.003  -3.785  1.00 177.05 ? 625  ILE A O   1 
ATOM   4787  C  CB  . ILE A  1  599 ? 4.850   46.873  -2.263  1.00 176.76 ? 625  ILE A CB  1 
ATOM   4788  C  CG1 . ILE A  1  599 ? 4.635   45.885  -1.112  1.00 176.43 ? 625  ILE A CG1 1 
ATOM   4789  C  CG2 . ILE A  1  599 ? 4.309   46.280  -3.552  1.00 176.59 ? 625  ILE A CG2 1 
ATOM   4790  C  CD1 . ILE A  1  599 ? 5.324   44.545  -1.292  1.00 176.15 ? 625  ILE A CD1 1 
ATOM   4791  N  N   . THR A  1  600 ? 7.774   48.880  -3.454  1.00 176.46 ? 626  THR A N   1 
ATOM   4792  C  CA  . THR A  1  600 ? 8.093   50.071  -4.242  1.00 175.68 ? 626  THR A CA  1 
ATOM   4793  C  C   . THR A  1  600 ? 8.356   49.751  -5.717  1.00 175.50 ? 626  THR A C   1 
ATOM   4794  O  O   . THR A  1  600 ? 9.354   49.112  -6.054  1.00 175.34 ? 626  THR A O   1 
ATOM   4795  C  CB  . THR A  1  600 ? 9.339   50.802  -3.669  1.00 175.37 ? 626  THR A CB  1 
ATOM   4796  O  OG1 . THR A  1  600 ? 10.480  49.938  -3.745  1.00 174.94 ? 626  THR A OG1 1 
ATOM   4797  C  CG2 . THR A  1  600 ? 9.109   51.202  -2.217  1.00 174.76 ? 626  THR A CG2 1 
ATOM   4798  N  N   . CYS A  1  601 ? 7.455   50.203  -6.587  1.00 175.08 ? 627  CYS A N   1 
ATOM   4799  C  CA  . CYS A  1  601 ? 7.579   49.983  -8.027  1.00 174.65 ? 627  CYS A CA  1 
ATOM   4800  C  C   . CYS A  1  601 ? 7.660   51.311  -8.777  1.00 174.31 ? 627  CYS A C   1 
ATOM   4801  O  O   . CYS A  1  601 ? 6.734   51.594  -9.570  1.00 173.81 ? 627  CYS A O   1 
ATOM   4802  C  CB  . CYS A  1  601 ? 6.379   49.206  -8.562  1.00 174.55 ? 627  CYS A CB  1 
ATOM   4803  S  SG  . CYS A  1  601 ? 5.998   47.613  -7.768  1.00 174.49 ? 627  CYS A SG  1 
ATOM   4804  N  N   . GLU B  1  1   ? 2.042   1.519   -63.280 1.00 117.02 ? 27   GLU B N   1 
ATOM   4805  C  CA  . GLU B  1  1   ? 2.930   1.169   -62.123 1.00 117.08 ? 27   GLU B CA  1 
ATOM   4806  C  C   . GLU B  1  1   ? 2.183   1.289   -60.793 1.00 115.97 ? 27   GLU B C   1 
ATOM   4807  O  O   . GLU B  1  1   ? 2.650   1.978   -59.880 1.00 116.03 ? 27   GLU B O   1 
ATOM   4808  C  CB  . GLU B  1  1   ? 4.150   2.106   -62.062 1.00 117.94 ? 27   GLU B CB  1 
ATOM   4809  C  CG  . GLU B  1  1   ? 4.942   2.253   -63.351 1.00 118.52 ? 27   GLU B CG  1 
ATOM   4810  C  CD  . GLU B  1  1   ? 5.991   3.344   -63.243 1.00 119.02 ? 27   GLU B CD  1 
ATOM   4811  O  OE1 . GLU B  1  1   ? 6.869   3.229   -62.362 1.00 119.18 ? 27   GLU B OE1 1 
ATOM   4812  O  OE2 . GLU B  1  1   ? 5.929   4.318   -64.027 1.00 119.25 ? 27   GLU B OE2 1 
ATOM   4813  N  N   . PRO B  1  2   ? 1.010   0.636   -60.661 1.00 114.42 ? 28   PRO B N   1 
ATOM   4814  C  CA  . PRO B  1  2   ? 0.338   0.779   -59.366 1.00 112.61 ? 28   PRO B CA  1 
ATOM   4815  C  C   . PRO B  1  2   ? 1.204   0.178   -58.248 1.00 111.77 ? 28   PRO B C   1 
ATOM   4816  O  O   . PRO B  1  2   ? 0.827   0.206   -57.079 1.00 111.49 ? 28   PRO B O   1 
ATOM   4817  C  CB  . PRO B  1  2   ? -0.987  0.040   -59.581 1.00 111.88 ? 28   PRO B CB  1 
ATOM   4818  C  CG  . PRO B  1  2   ? -0.637  -1.008  -60.594 1.00 112.14 ? 28   PRO B CG  1 
ATOM   4819  C  CD  . PRO B  1  2   ? 0.262   -0.266  -61.557 1.00 113.34 ? 28   PRO B CD  1 
ATOM   4820  N  N   . CYS B  1  3   ? 2.373   -0.346  -58.631 1.00 110.60 ? 29   CYS B N   1 
ATOM   4821  C  CA  . CYS B  1  3   ? 3.325   -0.968  -57.708 1.00 108.55 ? 29   CYS B CA  1 
ATOM   4822  C  C   . CYS B  1  3   ? 3.859   0.042   -56.713 1.00 107.13 ? 29   CYS B C   1 
ATOM   4823  O  O   . CYS B  1  3   ? 3.616   1.240   -56.836 1.00 106.60 ? 29   CYS B O   1 
ATOM   4824  C  CB  . CYS B  1  3   ? 4.529   -1.548  -58.461 1.00 108.45 ? 29   CYS B CB  1 
ATOM   4825  S  SG  . CYS B  1  3   ? 4.230   -2.842  -59.715 1.00 110.42 ? 29   CYS B SG  1 
ATOM   4826  N  N   . VAL B  1  4   ? 4.595   -0.460  -55.727 1.00 106.09 ? 30   VAL B N   1 
ATOM   4827  C  CA  . VAL B  1  4   ? 5.205   0.387   -54.713 1.00 104.79 ? 30   VAL B CA  1 
ATOM   4828  C  C   . VAL B  1  4   ? 6.714   0.302   -54.906 1.00 104.88 ? 30   VAL B C   1 
ATOM   4829  O  O   . VAL B  1  4   ? 7.294   -0.781  -54.868 1.00 105.26 ? 30   VAL B O   1 
ATOM   4830  C  CB  . VAL B  1  4   ? 4.857   -0.078  -53.286 1.00 103.51 ? 30   VAL B CB  1 
ATOM   4831  C  CG1 . VAL B  1  4   ? 5.583   0.788   -52.273 1.00 102.77 ? 30   VAL B CG1 1 
ATOM   4832  C  CG2 . VAL B  1  4   ? 3.365   0.008   -53.058 1.00 102.23 ? 30   VAL B CG2 1 
ATOM   4833  N  N   . GLU B  1  5   ? 7.340   1.449   -55.123 1.00 104.61 ? 31   GLU B N   1 
ATOM   4834  C  CA  . GLU B  1  5   ? 8.778   1.520   -55.323 1.00 105.06 ? 31   GLU B CA  1 
ATOM   4835  C  C   . GLU B  1  5   ? 9.454   1.692   -53.959 1.00 105.11 ? 31   GLU B C   1 
ATOM   4836  O  O   . GLU B  1  5   ? 9.532   2.806   -53.435 1.00 104.98 ? 31   GLU B O   1 
ATOM   4837  C  CB  . GLU B  1  5   ? 9.091   2.708   -56.246 1.00 106.20 ? 31   GLU B CB  1 
ATOM   4838  C  CG  . GLU B  1  5   ? 10.565  3.014   -56.503 1.00 107.01 ? 31   GLU B CG  1 
ATOM   4839  C  CD  . GLU B  1  5   ? 10.758  4.346   -57.219 1.00 106.96 ? 31   GLU B CD  1 
ATOM   4840  O  OE1 . GLU B  1  5   ? 10.220  4.504   -58.334 1.00 106.98 ? 31   GLU B OE1 1 
ATOM   4841  O  OE2 . GLU B  1  5   ? 11.443  5.232   -56.664 1.00 107.08 ? 31   GLU B OE2 1 
ATOM   4842  N  N   . VAL B  1  6   ? 9.935   0.592   -53.383 1.00 104.69 ? 32   VAL B N   1 
ATOM   4843  C  CA  . VAL B  1  6   ? 10.589  0.645   -52.074 1.00 104.62 ? 32   VAL B CA  1 
ATOM   4844  C  C   . VAL B  1  6   ? 11.990  1.250   -52.152 1.00 105.00 ? 32   VAL B C   1 
ATOM   4845  O  O   . VAL B  1  6   ? 12.320  2.167   -51.404 1.00 105.29 ? 32   VAL B O   1 
ATOM   4846  C  CB  . VAL B  1  6   ? 10.693  -0.753  -51.443 1.00 104.01 ? 32   VAL B CB  1 
ATOM   4847  C  CG1 . VAL B  1  6   ? 11.266  -0.641  -50.046 1.00 102.80 ? 32   VAL B CG1 1 
ATOM   4848  C  CG2 . VAL B  1  6   ? 9.325   -1.410  -51.413 1.00 103.03 ? 32   VAL B CG2 1 
ATOM   4849  N  N   . VAL B  1  7   ? 12.812  0.723   -53.050 1.00 105.04 ? 33   VAL B N   1 
ATOM   4850  C  CA  . VAL B  1  7   ? 14.165  1.224   -53.244 1.00 105.39 ? 33   VAL B CA  1 
ATOM   4851  C  C   . VAL B  1  7   ? 14.289  1.505   -54.736 1.00 106.53 ? 33   VAL B C   1 
ATOM   4852  O  O   . VAL B  1  7   ? 14.452  0.577   -55.530 1.00 107.44 ? 33   VAL B O   1 
ATOM   4853  C  CB  . VAL B  1  7   ? 15.217  0.175   -52.848 1.00 104.42 ? 33   VAL B CB  1 
ATOM   4854  C  CG1 . VAL B  1  7   ? 16.596  0.799   -52.848 1.00 103.73 ? 33   VAL B CG1 1 
ATOM   4855  C  CG2 . VAL B  1  7   ? 14.888  -0.399  -51.493 1.00 103.98 ? 33   VAL B CG2 1 
ATOM   4856  N  N   . PRO B  1  8   ? 14.222  2.787   -55.140 1.00 106.45 ? 34   PRO B N   1 
ATOM   4857  C  CA  . PRO B  1  8   ? 14.323  3.142   -56.559 1.00 106.24 ? 34   PRO B CA  1 
ATOM   4858  C  C   . PRO B  1  8   ? 15.390  2.383   -57.341 1.00 107.10 ? 34   PRO B C   1 
ATOM   4859  O  O   . PRO B  1  8   ? 16.497  2.147   -56.847 1.00 106.29 ? 34   PRO B O   1 
ATOM   4860  C  CB  . PRO B  1  8   ? 14.567  4.650   -56.523 1.00 106.01 ? 34   PRO B CB  1 
ATOM   4861  C  CG  . PRO B  1  8   ? 15.187  4.876   -55.174 1.00 105.32 ? 34   PRO B CG  1 
ATOM   4862  C  CD  . PRO B  1  8   ? 14.365  3.984   -54.298 1.00 105.55 ? 34   PRO B CD  1 
ATOM   4863  N  N   . ASN B  1  9   ? 15.032  2.001   -58.566 1.00 108.47 ? 35   ASN B N   1 
ATOM   4864  C  CA  . ASN B  1  9   ? 15.915  1.259   -59.463 1.00 109.63 ? 35   ASN B CA  1 
ATOM   4865  C  C   . ASN B  1  9   ? 16.392  -0.071  -58.854 1.00 108.90 ? 35   ASN B C   1 
ATOM   4866  O  O   . ASN B  1  9   ? 17.186  -0.777  -59.471 1.00 109.16 ? 35   ASN B O   1 
ATOM   4867  C  CB  . ASN B  1  9   ? 17.138  2.134   -59.879 1.00 112.30 ? 35   ASN B CB  1 
ATOM   4868  C  CG  . ASN B  1  9   ? 16.826  3.114   -61.046 1.00 114.92 ? 35   ASN B CG  1 
ATOM   4869  O  OD1 . ASN B  1  9   ? 15.948  2.825   -61.867 1.00 114.85 ? 35   ASN B OD1 1 
ATOM   4870  N  ND2 . ASN B  1  9   ? 17.548  4.244   -61.140 1.00 116.60 ? 35   ASN B ND2 1 
ATOM   4871  N  N   . ILE B  1  10  ? 15.894  -0.431  -57.666 1.00 108.29 ? 36   ILE B N   1 
ATOM   4872  C  CA  . ILE B  1  10  ? 16.331  -1.669  -56.996 1.00 106.87 ? 36   ILE B CA  1 
ATOM   4873  C  C   . ILE B  1  10  ? 15.277  -2.671  -56.469 1.00 105.58 ? 36   ILE B C   1 
ATOM   4874  O  O   . ILE B  1  10  ? 15.347  -3.859  -56.796 1.00 104.65 ? 36   ILE B O   1 
ATOM   4875  C  CB  . ILE B  1  10  ? 17.277  -1.346  -55.808 1.00 106.72 ? 36   ILE B CB  1 
ATOM   4876  C  CG1 . ILE B  1  10  ? 18.362  -0.357  -56.244 1.00 107.07 ? 36   ILE B CG1 1 
ATOM   4877  C  CG2 . ILE B  1  10  ? 17.929  -2.624  -55.309 1.00 106.58 ? 36   ILE B CG2 1 
ATOM   4878  C  CD1 . ILE B  1  10  ? 19.368  -0.923  -57.236 1.00 107.57 ? 36   ILE B CD1 1 
ATOM   4879  N  N   . THR B  1  11  ? 14.328  -2.209  -55.649 1.00 104.12 ? 37   THR B N   1 
ATOM   4880  C  CA  . THR B  1  11  ? 13.297  -3.091  -55.081 1.00 103.06 ? 37   THR B CA  1 
ATOM   4881  C  C   . THR B  1  11  ? 11.839  -2.626  -55.242 1.00 102.67 ? 37   THR B C   1 
ATOM   4882  O  O   . THR B  1  11  ? 11.475  -1.533  -54.802 1.00 102.19 ? 37   THR B O   1 
ATOM   4883  C  CB  . THR B  1  11  ? 13.534  -3.320  -53.567 1.00 102.91 ? 37   THR B CB  1 
ATOM   4884  O  OG1 . THR B  1  11  ? 14.861  -3.815  -53.356 1.00 102.44 ? 37   THR B OG1 1 
ATOM   4885  C  CG2 . THR B  1  11  ? 12.541  -4.334  -53.018 1.00 102.37 ? 37   THR B CG2 1 
ATOM   4886  N  N   . TYR B  1  12  ? 11.006  -3.473  -55.848 1.00 102.69 ? 38   TYR B N   1 
ATOM   4887  C  CA  . TYR B  1  12  ? 9.585   -3.168  -56.063 1.00 102.99 ? 38   TYR B CA  1 
ATOM   4888  C  C   . TYR B  1  12  ? 8.654   -4.259  -55.521 1.00 102.97 ? 38   TYR B C   1 
ATOM   4889  O  O   . TYR B  1  12  ? 8.903   -5.453  -55.713 1.00 102.83 ? 38   TYR B O   1 
ATOM   4890  C  CB  . TYR B  1  12  ? 9.292   -2.962  -57.563 1.00 103.73 ? 38   TYR B CB  1 
ATOM   4891  C  CG  . TYR B  1  12  ? 10.065  -1.823  -58.194 1.00 104.20 ? 38   TYR B CG  1 
ATOM   4892  C  CD1 . TYR B  1  12  ? 11.383  -2.002  -58.623 1.00 104.47 ? 38   TYR B CD1 1 
ATOM   4893  C  CD2 . TYR B  1  12  ? 9.512   -0.543  -58.280 1.00 104.06 ? 38   TYR B CD2 1 
ATOM   4894  C  CE1 . TYR B  1  12  ? 12.131  -0.939  -59.106 1.00 104.90 ? 38   TYR B CE1 1 
ATOM   4895  C  CE2 . TYR B  1  12  ? 10.254  0.526   -58.761 1.00 104.32 ? 38   TYR B CE2 1 
ATOM   4896  C  CZ  . TYR B  1  12  ? 11.563  0.323   -59.165 1.00 105.17 ? 38   TYR B CZ  1 
ATOM   4897  O  OH  . TYR B  1  12  ? 12.331  1.391   -59.581 1.00 106.40 ? 38   TYR B OH  1 
ATOM   4898  N  N   . GLN B  1  13  ? 7.582   -3.838  -54.847 1.00 102.91 ? 39   GLN B N   1 
ATOM   4899  C  CA  . GLN B  1  13  ? 6.598   -4.764  -54.287 1.00 102.35 ? 39   GLN B CA  1 
ATOM   4900  C  C   . GLN B  1  13  ? 5.233   -4.552  -54.914 1.00 101.34 ? 39   GLN B C   1 
ATOM   4901  O  O   . GLN B  1  13  ? 4.479   -3.678  -54.495 1.00 100.46 ? 39   GLN B O   1 
ATOM   4902  C  CB  . GLN B  1  13  ? 6.467   -4.588  -52.772 1.00 103.54 ? 39   GLN B CB  1 
ATOM   4903  C  CG  . GLN B  1  13  ? 5.441   -5.525  -52.142 1.00 104.68 ? 39   GLN B CG  1 
ATOM   4904  C  CD  . GLN B  1  13  ? 5.409   -5.443  -50.627 1.00 105.91 ? 39   GLN B CD  1 
ATOM   4905  O  OE1 . GLN B  1  13  ? 5.089   -4.399  -50.060 1.00 106.81 ? 39   GLN B OE1 1 
ATOM   4906  N  NE2 . GLN B  1  13  ? 5.744   -6.549  -49.963 1.00 104.90 ? 39   GLN B NE2 1 
ATOM   4907  N  N   . CYS B  1  14  ? 4.923   -5.351  -55.924 1.00 100.88 ? 40   CYS B N   1 
ATOM   4908  C  CA  . CYS B  1  14  ? 3.638   -5.250  -56.600 1.00 101.33 ? 40   CYS B CA  1 
ATOM   4909  C  C   . CYS B  1  14  ? 2.736   -6.351  -56.044 1.00 99.73  ? 40   CYS B C   1 
ATOM   4910  O  O   . CYS B  1  14  ? 2.232   -7.201  -56.786 1.00 99.43  ? 40   CYS B O   1 
ATOM   4911  C  CB  . CYS B  1  14  ? 3.804   -5.453  -58.106 1.00 104.31 ? 40   CYS B CB  1 
ATOM   4912  S  SG  . CYS B  1  14  ? 5.126   -4.506  -58.939 1.00 109.40 ? 40   CYS B SG  1 
ATOM   4913  N  N   . MET B  1  15  ? 2.528   -6.325  -54.733 1.00 97.54  ? 41   MET B N   1 
ATOM   4914  C  CA  . MET B  1  15  ? 1.724   -7.343  -54.068 1.00 94.84  ? 41   MET B CA  1 
ATOM   4915  C  C   . MET B  1  15  ? 0.231   -7.061  -54.041 1.00 93.40  ? 41   MET B C   1 
ATOM   4916  O  O   . MET B  1  15  ? -0.204  -5.975  -53.668 1.00 92.62  ? 41   MET B O   1 
ATOM   4917  C  CB  . MET B  1  15  ? 2.225   -7.539  -52.630 1.00 94.28  ? 41   MET B CB  1 
ATOM   4918  C  CG  . MET B  1  15  ? 1.645   -8.750  -51.901 1.00 92.30  ? 41   MET B CG  1 
ATOM   4919  S  SD  . MET B  1  15  ? 2.132   -8.807  -50.156 1.00 90.16  ? 41   MET B SD  1 
ATOM   4920  C  CE  . MET B  1  15  ? 0.662   -8.083  -49.366 1.00 90.40  ? 41   MET B CE  1 
ATOM   4921  N  N   . GLU B  1  16  ? -0.542  -8.061  -54.446 1.00 92.40  ? 42   GLU B N   1 
ATOM   4922  C  CA  . GLU B  1  16  ? -1.999  -7.988  -54.449 1.00 91.71  ? 42   GLU B CA  1 
ATOM   4923  C  C   . GLU B  1  16  ? -2.576  -6.756  -55.142 1.00 90.80  ? 42   GLU B C   1 
ATOM   4924  O  O   . GLU B  1  16  ? -3.198  -5.903  -54.503 1.00 89.35  ? 42   GLU B O   1 
ATOM   4925  C  CB  . GLU B  1  16  ? -2.502  -8.062  -53.007 1.00 92.35  ? 42   GLU B CB  1 
ATOM   4926  C  CG  . GLU B  1  16  ? -3.830  -8.786  -52.844 1.00 92.91  ? 42   GLU B CG  1 
ATOM   4927  C  CD  . GLU B  1  16  ? -4.090  -9.206  -51.408 1.00 92.89  ? 42   GLU B CD  1 
ATOM   4928  O  OE1 . GLU B  1  16  ? -5.174  -9.765  -51.138 1.00 92.43  ? 42   GLU B OE1 1 
ATOM   4929  O  OE2 . GLU B  1  16  ? -3.207  -8.978  -50.551 1.00 93.79  ? 42   GLU B OE2 1 
ATOM   4930  N  N   . LEU B  1  17  ? -2.369  -6.685  -56.456 1.00 90.28  ? 43   LEU B N   1 
ATOM   4931  C  CA  . LEU B  1  17  ? -2.854  -5.578  -57.274 1.00 89.41  ? 43   LEU B CA  1 
ATOM   4932  C  C   . LEU B  1  17  ? -3.563  -6.103  -58.520 1.00 90.01  ? 43   LEU B C   1 
ATOM   4933  O  O   . LEU B  1  17  ? -3.600  -5.441  -59.555 1.00 89.99  ? 43   LEU B O   1 
ATOM   4934  C  CB  . LEU B  1  17  ? -1.686  -4.688  -57.688 1.00 87.37  ? 43   LEU B CB  1 
ATOM   4935  C  CG  . LEU B  1  17  ? -0.874  -4.127  -56.530 1.00 86.50  ? 43   LEU B CG  1 
ATOM   4936  C  CD1 . LEU B  1  17  ? 0.389   -3.498  -57.062 1.00 86.71  ? 43   LEU B CD1 1 
ATOM   4937  C  CD2 . LEU B  1  17  ? -1.700  -3.121  -55.764 1.00 86.53  ? 43   LEU B CD2 1 
ATOM   4938  N  N   . ASN B  1  18  ? -4.119  -7.304  -58.407 1.00 91.14  ? 44   ASN B N   1 
ATOM   4939  C  CA  . ASN B  1  18  ? -4.842  -7.940  -59.499 1.00 91.89  ? 44   ASN B CA  1 
ATOM   4940  C  C   . ASN B  1  18  ? -4.082  -8.074  -60.801 1.00 92.63  ? 44   ASN B C   1 
ATOM   4941  O  O   . ASN B  1  18  ? -4.658  -7.886  -61.870 1.00 93.66  ? 44   ASN B O   1 
ATOM   4942  C  CB  . ASN B  1  18  ? -6.151  -7.204  -59.782 1.00 92.24  ? 44   ASN B CB  1 
ATOM   4943  C  CG  . ASN B  1  18  ? -7.316  -7.784  -59.020 1.00 92.25  ? 44   ASN B CG  1 
ATOM   4944  O  OD1 . ASN B  1  18  ? -7.625  -7.354  -57.906 1.00 92.66  ? 44   ASN B OD1 1 
ATOM   4945  N  ND2 . ASN B  1  18  ? -7.968  -8.782  -59.616 1.00 91.81  ? 44   ASN B ND2 1 
ATOM   4946  N  N   . PHE B  1  19  ? -2.795  -8.388  -60.724 1.00 93.12  ? 45   PHE B N   1 
ATOM   4947  C  CA  . PHE B  1  19  ? -2.010  -8.568  -61.941 1.00 93.89  ? 45   PHE B CA  1 
ATOM   4948  C  C   . PHE B  1  19  ? -2.272  -9.967  -62.503 1.00 94.45  ? 45   PHE B C   1 
ATOM   4949  O  O   . PHE B  1  19  ? -2.061  -10.964 -61.807 1.00 94.61  ? 45   PHE B O   1 
ATOM   4950  C  CB  . PHE B  1  19  ? -0.509  -8.396  -61.661 1.00 92.82  ? 45   PHE B CB  1 
ATOM   4951  C  CG  . PHE B  1  19  ? -0.061  -6.959  -61.541 1.00 92.49  ? 45   PHE B CG  1 
ATOM   4952  C  CD1 . PHE B  1  19  ? 1.289   -6.638  -61.633 1.00 92.08  ? 45   PHE B CD1 1 
ATOM   4953  C  CD2 . PHE B  1  19  ? -0.982  -5.927  -61.334 1.00 92.92  ? 45   PHE B CD2 1 
ATOM   4954  C  CE1 . PHE B  1  19  ? 1.725   -5.311  -61.520 1.00 92.52  ? 45   PHE B CE1 1 
ATOM   4955  C  CE2 . PHE B  1  19  ? -0.558  -4.584  -61.218 1.00 92.33  ? 45   PHE B CE2 1 
ATOM   4956  C  CZ  . PHE B  1  19  ? 0.800   -4.276  -61.312 1.00 92.32  ? 45   PHE B CZ  1 
ATOM   4957  N  N   . TYR B  1  20  ? -2.745  -10.034 -63.750 1.00 94.97  ? 46   TYR B N   1 
ATOM   4958  C  CA  . TYR B  1  20  ? -3.017  -11.311 -64.404 1.00 95.48  ? 46   TYR B CA  1 
ATOM   4959  C  C   . TYR B  1  20  ? -1.815  -11.698 -65.249 1.00 95.05  ? 46   TYR B C   1 
ATOM   4960  O  O   . TYR B  1  20  ? -1.701  -12.831 -65.714 1.00 93.93  ? 46   TYR B O   1 
ATOM   4961  C  CB  . TYR B  1  20  ? -4.277  -11.217 -65.281 1.00 96.78  ? 46   TYR B CB  1 
ATOM   4962  C  CG  . TYR B  1  20  ? -5.573  -11.118 -64.488 1.00 99.56  ? 46   TYR B CG  1 
ATOM   4963  C  CD1 . TYR B  1  20  ? -5.956  -9.920  -63.878 1.00 100.08 ? 46   TYR B CD1 1 
ATOM   4964  C  CD2 . TYR B  1  20  ? -6.402  -12.238 -64.314 1.00 100.90 ? 46   TYR B CD2 1 
ATOM   4965  C  CE1 . TYR B  1  20  ? -7.126  -9.838  -63.112 1.00 101.22 ? 46   TYR B CE1 1 
ATOM   4966  C  CE2 . TYR B  1  20  ? -7.576  -12.167 -63.549 1.00 101.36 ? 46   TYR B CE2 1 
ATOM   4967  C  CZ  . TYR B  1  20  ? -7.931  -10.963 -62.950 1.00 101.71 ? 46   TYR B CZ  1 
ATOM   4968  O  OH  . TYR B  1  20  ? -9.080  -10.887 -62.183 1.00 101.48 ? 46   TYR B OH  1 
ATOM   4969  N  N   . LYS B  1  21  ? -0.916  -10.732 -65.422 1.00 95.51  ? 47   LYS B N   1 
ATOM   4970  C  CA  . LYS B  1  21  ? 0.310   -10.894 -66.203 1.00 95.12  ? 47   LYS B CA  1 
ATOM   4971  C  C   . LYS B  1  21  ? 1.451   -10.094 -65.559 1.00 94.19  ? 47   LYS B C   1 
ATOM   4972  O  O   . LYS B  1  21  ? 1.223   -9.018  -64.991 1.00 93.74  ? 47   LYS B O   1 
ATOM   4973  C  CB  . LYS B  1  21  ? 0.064   -10.421 -67.642 1.00 95.98  ? 47   LYS B CB  1 
ATOM   4974  C  CG  . LYS B  1  21  ? -0.593  -9.032  -67.742 1.00 96.96  ? 47   LYS B CG  1 
ATOM   4975  C  CD  . LYS B  1  21  ? -1.290  -8.820  -69.090 1.00 98.04  ? 47   LYS B CD  1 
ATOM   4976  C  CE  . LYS B  1  21  ? -2.515  -9.738  -69.269 1.00 98.10  ? 47   LYS B CE  1 
ATOM   4977  N  NZ  . LYS B  1  21  ? -3.627  -9.453  -68.306 1.00 97.33  ? 47   LYS B NZ  1 
ATOM   4978  N  N   . ILE B  1  22  ? 2.669   -10.625 -65.645 1.00 92.76  ? 48   ILE B N   1 
ATOM   4979  C  CA  . ILE B  1  22  ? 3.844   -9.978  -65.059 1.00 91.45  ? 48   ILE B CA  1 
ATOM   4980  C  C   . ILE B  1  22  ? 4.028   -8.544  -65.556 1.00 91.42  ? 48   ILE B C   1 
ATOM   4981  O  O   . ILE B  1  22  ? 3.959   -8.283  -66.747 1.00 90.50  ? 48   ILE B O   1 
ATOM   4982  C  CB  . ILE B  1  22  ? 5.135   -10.764 -65.383 1.00 90.34  ? 48   ILE B CB  1 
ATOM   4983  C  CG1 . ILE B  1  22  ? 4.956   -12.249 -65.062 1.00 89.32  ? 48   ILE B CG1 1 
ATOM   4984  C  CG2 . ILE B  1  22  ? 6.298   -10.188 -64.605 1.00 89.10  ? 48   ILE B CG2 1 
ATOM   4985  C  CD1 . ILE B  1  22  ? 4.246   -13.032 -66.158 1.00 88.85  ? 48   ILE B CD1 1 
ATOM   4986  N  N   . PRO B  1  23  ? 4.275   -7.596  -64.644 1.00 92.59  ? 49   PRO B N   1 
ATOM   4987  C  CA  . PRO B  1  23  ? 4.453   -6.222  -65.109 1.00 94.41  ? 49   PRO B CA  1 
ATOM   4988  C  C   . PRO B  1  23  ? 5.672   -6.101  -66.018 1.00 96.60  ? 49   PRO B C   1 
ATOM   4989  O  O   . PRO B  1  23  ? 6.488   -7.019  -66.114 1.00 96.87  ? 49   PRO B O   1 
ATOM   4990  C  CB  . PRO B  1  23  ? 4.603   -5.436  -63.809 1.00 94.04  ? 49   PRO B CB  1 
ATOM   4991  C  CG  . PRO B  1  23  ? 5.282   -6.416  -62.918 1.00 93.01  ? 49   PRO B CG  1 
ATOM   4992  C  CD  . PRO B  1  23  ? 4.533   -7.695  -63.197 1.00 92.85  ? 49   PRO B CD  1 
ATOM   4993  N  N   . ASP B  1  24  ? 5.789   -4.958  -66.682 1.00 98.63  ? 50   ASP B N   1 
ATOM   4994  C  CA  . ASP B  1  24  ? 6.893   -4.711  -67.602 1.00 99.68  ? 50   ASP B CA  1 
ATOM   4995  C  C   . ASP B  1  24  ? 7.336   -3.261  -67.461 1.00 99.30  ? 50   ASP B C   1 
ATOM   4996  O  O   . ASP B  1  24  ? 8.439   -2.887  -67.850 1.00 98.96  ? 50   ASP B O   1 
ATOM   4997  C  CB  . ASP B  1  24  ? 6.432   -4.975  -69.037 1.00 100.93 ? 50   ASP B CB  1 
ATOM   4998  C  CG  . ASP B  1  24  ? 5.217   -4.140  -69.420 1.00 102.18 ? 50   ASP B CG  1 
ATOM   4999  O  OD1 . ASP B  1  24  ? 4.198   -4.189  -68.689 1.00 103.74 ? 50   ASP B OD1 1 
ATOM   5000  O  OD2 . ASP B  1  24  ? 5.273   -3.434  -70.451 1.00 102.54 ? 50   ASP B OD2 1 
ATOM   5001  N  N   . ASN B  1  25  ? 6.459   -2.446  -66.893 1.00 98.97  ? 51   ASN B N   1 
ATOM   5002  C  CA  . ASN B  1  25  ? 6.745   -1.037  -66.702 1.00 99.67  ? 51   ASN B CA  1 
ATOM   5003  C  C   . ASN B  1  25  ? 7.739   -0.790  -65.573 1.00 98.99  ? 51   ASN B C   1 
ATOM   5004  O  O   . ASN B  1  25  ? 7.787   0.306   -65.006 1.00 98.47  ? 51   ASN B O   1 
ATOM   5005  C  CB  . ASN B  1  25  ? 5.444   -0.281  -66.420 1.00 101.30 ? 51   ASN B CB  1 
ATOM   5006  C  CG  . ASN B  1  25  ? 4.695   -0.831  -65.222 1.00 102.67 ? 51   ASN B CG  1 
ATOM   5007  O  OD1 . ASN B  1  25  ? 3.654   -0.298  -64.837 1.00 103.90 ? 51   ASN B OD1 1 
ATOM   5008  N  ND2 . ASN B  1  25  ? 5.216   -1.907  -64.627 1.00 103.48 ? 51   ASN B ND2 1 
ATOM   5009  N  N   . LEU B  1  26  ? 8.536   -1.804  -65.256 1.00 98.41  ? 52   LEU B N   1 
ATOM   5010  C  CA  . LEU B  1  26  ? 9.515   -1.690  -64.179 1.00 98.05  ? 52   LEU B CA  1 
ATOM   5011  C  C   . LEU B  1  26  ? 10.945  -1.771  -64.703 1.00 97.71  ? 52   LEU B C   1 
ATOM   5012  O  O   . LEU B  1  26  ? 11.218  -2.470  -65.683 1.00 97.15  ? 52   LEU B O   1 
ATOM   5013  C  CB  . LEU B  1  26  ? 9.294   -2.801  -63.148 1.00 97.99  ? 52   LEU B CB  1 
ATOM   5014  C  CG  . LEU B  1  26  ? 7.893   -2.963  -62.558 1.00 97.18  ? 52   LEU B CG  1 
ATOM   5015  C  CD1 . LEU B  1  26  ? 7.841   -4.270  -61.804 1.00 97.29  ? 52   LEU B CD1 1 
ATOM   5016  C  CD2 . LEU B  1  26  ? 7.552   -1.797  -61.644 1.00 97.50  ? 52   LEU B CD2 1 
ATOM   5017  N  N   . PRO B  1  27  ? 11.878  -1.059  -64.044 1.00 97.61  ? 53   PRO B N   1 
ATOM   5018  C  CA  . PRO B  1  27  ? 13.303  -1.009  -64.397 1.00 98.51  ? 53   PRO B CA  1 
ATOM   5019  C  C   . PRO B  1  27  ? 13.957  -2.371  -64.668 1.00 99.82  ? 53   PRO B C   1 
ATOM   5020  O  O   . PRO B  1  27  ? 13.446  -3.407  -64.248 1.00 100.83 ? 53   PRO B O   1 
ATOM   5021  C  CB  . PRO B  1  27  ? 13.917  -0.296  -63.200 1.00 97.45  ? 53   PRO B CB  1 
ATOM   5022  C  CG  . PRO B  1  27  ? 12.850  0.681   -62.839 1.00 96.82  ? 53   PRO B CG  1 
ATOM   5023  C  CD  . PRO B  1  27  ? 11.600  -0.171  -62.900 1.00 96.55  ? 53   PRO B CD  1 
ATOM   5024  N  N   . PHE B  1  28  ? 15.083  -2.357  -65.382 1.00 100.70 ? 54   PHE B N   1 
ATOM   5025  C  CA  . PHE B  1  28  ? 15.817  -3.581  -65.705 1.00 101.52 ? 54   PHE B CA  1 
ATOM   5026  C  C   . PHE B  1  28  ? 16.794  -3.926  -64.590 1.00 100.56 ? 54   PHE B C   1 
ATOM   5027  O  O   . PHE B  1  28  ? 17.176  -5.081  -64.411 1.00 101.31 ? 54   PHE B O   1 
ATOM   5028  C  CB  . PHE B  1  28  ? 16.591  -3.417  -67.019 1.00 104.18 ? 54   PHE B CB  1 
ATOM   5029  C  CG  . PHE B  1  28  ? 15.703  -3.180  -68.229 1.00 108.91 ? 54   PHE B CG  1 
ATOM   5030  C  CD1 . PHE B  1  28  ? 15.189  -1.903  -68.508 1.00 109.76 ? 54   PHE B CD1 1 
ATOM   5031  C  CD2 . PHE B  1  28  ? 15.370  -4.241  -69.090 1.00 110.07 ? 54   PHE B CD2 1 
ATOM   5032  C  CE1 . PHE B  1  28  ? 14.352  -1.684  -69.624 1.00 109.06 ? 54   PHE B CE1 1 
ATOM   5033  C  CE2 . PHE B  1  28  ? 14.533  -4.039  -70.210 1.00 109.00 ? 54   PHE B CE2 1 
ATOM   5034  C  CZ  . PHE B  1  28  ? 14.027  -2.756  -70.477 1.00 109.17 ? 54   PHE B CZ  1 
ATOM   5035  N  N   . SER B  1  29  ? 17.181  -2.905  -63.838 1.00 99.22  ? 55   SER B N   1 
ATOM   5036  C  CA  . SER B  1  29  ? 18.124  -3.038  -62.735 1.00 98.13  ? 55   SER B CA  1 
ATOM   5037  C  C   . SER B  1  29  ? 17.539  -3.735  -61.510 1.00 97.85  ? 55   SER B C   1 
ATOM   5038  O  O   . SER B  1  29  ? 18.267  -4.083  -60.579 1.00 98.34  ? 55   SER B O   1 
ATOM   5039  C  CB  . SER B  1  29  ? 18.609  -1.653  -62.323 1.00 97.81  ? 55   SER B CB  1 
ATOM   5040  O  OG  . SER B  1  29  ? 17.504  -0.823  -62.012 1.00 97.39  ? 55   SER B OG  1 
ATOM   5041  N  N   . THR B  1  30  ? 16.224  -3.917  -61.513 1.00 96.90  ? 56   THR B N   1 
ATOM   5042  C  CA  . THR B  1  30  ? 15.508  -4.556  -60.409 1.00 95.00  ? 56   THR B CA  1 
ATOM   5043  C  C   . THR B  1  30  ? 16.161  -5.853  -59.914 1.00 93.46  ? 56   THR B C   1 
ATOM   5044  O  O   . THR B  1  30  ? 16.459  -6.762  -60.704 1.00 93.50  ? 56   THR B O   1 
ATOM   5045  C  CB  . THR B  1  30  ? 14.058  -4.845  -60.826 1.00 95.40  ? 56   THR B CB  1 
ATOM   5046  O  OG1 . THR B  1  30  ? 13.476  -3.647  -61.353 1.00 95.62  ? 56   THR B OG1 1 
ATOM   5047  C  CG2 . THR B  1  30  ? 13.238  -5.310  -59.639 1.00 95.52  ? 56   THR B CG2 1 
ATOM   5048  N  N   . LYS B  1  31  ? 16.364  -5.929  -58.596 1.00 91.09  ? 57   LYS B N   1 
ATOM   5049  C  CA  . LYS B  1  31  ? 16.989  -7.090  -57.963 1.00 87.97  ? 57   LYS B CA  1 
ATOM   5050  C  C   . LYS B  1  31  ? 16.029  -7.868  -57.054 1.00 85.50  ? 57   LYS B C   1 
ATOM   5051  O  O   . LYS B  1  31  ? 16.205  -9.070  -56.844 1.00 84.06  ? 57   LYS B O   1 
ATOM   5052  C  CB  . LYS B  1  31  ? 18.216  -6.631  -57.165 1.00 87.62  ? 57   LYS B CB  1 
ATOM   5053  C  CG  . LYS B  1  31  ? 19.225  -5.855  -58.002 1.00 88.20  ? 57   LYS B CG  1 
ATOM   5054  C  CD  . LYS B  1  31  ? 20.297  -5.174  -57.157 1.00 87.57  ? 57   LYS B CD  1 
ATOM   5055  C  CE  . LYS B  1  31  ? 21.329  -6.160  -56.635 1.00 87.76  ? 57   LYS B CE  1 
ATOM   5056  N  NZ  . LYS B  1  31  ? 22.331  -5.483  -55.764 1.00 87.23  ? 57   LYS B NZ  1 
ATOM   5057  N  N   . ASN B  1  32  ? 15.018  -7.178  -56.529 1.00 83.44  ? 58   ASN B N   1 
ATOM   5058  C  CA  . ASN B  1  32  ? 14.026  -7.786  -55.638 1.00 81.44  ? 58   ASN B CA  1 
ATOM   5059  C  C   . ASN B  1  32  ? 12.599  -7.473  -56.082 1.00 79.71  ? 58   ASN B C   1 
ATOM   5060  O  O   . ASN B  1  32  ? 12.169  -6.326  -56.033 1.00 79.35  ? 58   ASN B O   1 
ATOM   5061  C  CB  . ASN B  1  32  ? 14.215  -7.268  -54.215 1.00 82.57  ? 58   ASN B CB  1 
ATOM   5062  C  CG  . ASN B  1  32  ? 15.661  -7.285  -53.779 1.00 84.53  ? 58   ASN B CG  1 
ATOM   5063  O  OD1 . ASN B  1  32  ? 16.300  -8.341  -53.745 1.00 87.34  ? 58   ASN B OD1 1 
ATOM   5064  N  ND2 . ASN B  1  32  ? 16.191  -6.114  -53.435 1.00 83.93  ? 58   ASN B ND2 1 
ATOM   5065  N  N   . LEU B  1  33  ? 11.861  -8.495  -56.495 1.00 78.26  ? 59   LEU B N   1 
ATOM   5066  C  CA  . LEU B  1  33  ? 10.487  -8.311  -56.955 1.00 77.13  ? 59   LEU B CA  1 
ATOM   5067  C  C   . LEU B  1  33  ? 9.524   -9.220  -56.213 1.00 76.88  ? 59   LEU B C   1 
ATOM   5068  O  O   . LEU B  1  33  ? 9.730   -10.430 -56.148 1.00 76.59  ? 59   LEU B O   1 
ATOM   5069  C  CB  . LEU B  1  33  ? 10.390  -8.600  -58.460 1.00 75.96  ? 59   LEU B CB  1 
ATOM   5070  C  CG  . LEU B  1  33  ? 9.004   -8.566  -59.099 1.00 73.89  ? 59   LEU B CG  1 
ATOM   5071  C  CD1 . LEU B  1  33  ? 8.565   -7.136  -59.271 1.00 74.52  ? 59   LEU B CD1 1 
ATOM   5072  C  CD2 . LEU B  1  33  ? 9.034   -9.254  -60.431 1.00 73.13  ? 59   LEU B CD2 1 
ATOM   5073  N  N   . ASP B  1  34  ? 8.471   -8.624  -55.666 1.00 77.59  ? 60   ASP B N   1 
ATOM   5074  C  CA  . ASP B  1  34  ? 7.434   -9.354  -54.930 1.00 79.07  ? 60   ASP B CA  1 
ATOM   5075  C  C   . ASP B  1  34  ? 6.132   -9.290  -55.740 1.00 78.84  ? 60   ASP B C   1 
ATOM   5076  O  O   . ASP B  1  34  ? 5.564   -8.213  -55.913 1.00 79.38  ? 60   ASP B O   1 
ATOM   5077  C  CB  . ASP B  1  34  ? 7.226   -8.702  -53.548 1.00 80.54  ? 60   ASP B CB  1 
ATOM   5078  C  CG  . ASP B  1  34  ? 6.218   -9.451  -52.667 1.00 80.85  ? 60   ASP B CG  1 
ATOM   5079  O  OD1 . ASP B  1  34  ? 5.075   -9.701  -53.106 1.00 80.75  ? 60   ASP B OD1 1 
ATOM   5080  O  OD2 . ASP B  1  34  ? 6.568   -9.781  -51.515 1.00 81.85  ? 60   ASP B OD2 1 
ATOM   5081  N  N   . LEU B  1  35  ? 5.674   -10.433 -56.246 1.00 78.79  ? 61   LEU B N   1 
ATOM   5082  C  CA  . LEU B  1  35  ? 4.438   -10.487 -57.028 1.00 79.41  ? 61   LEU B CA  1 
ATOM   5083  C  C   . LEU B  1  35  ? 3.420   -11.383 -56.346 1.00 80.28  ? 61   LEU B C   1 
ATOM   5084  O  O   . LEU B  1  35  ? 2.627   -12.064 -57.004 1.00 79.68  ? 61   LEU B O   1 
ATOM   5085  C  CB  . LEU B  1  35  ? 4.699   -11.015 -58.440 1.00 78.39  ? 61   LEU B CB  1 
ATOM   5086  C  CG  . LEU B  1  35  ? 5.402   -10.066 -59.404 1.00 77.57  ? 61   LEU B CG  1 
ATOM   5087  C  CD1 . LEU B  1  35  ? 5.591   -10.760 -60.730 1.00 77.30  ? 61   LEU B CD1 1 
ATOM   5088  C  CD2 . LEU B  1  35  ? 4.586   -8.801  -59.573 1.00 76.42  ? 61   LEU B CD2 1 
ATOM   5089  N  N   . SER B  1  36  ? 3.453   -11.364 -55.017 1.00 81.95  ? 62   SER B N   1 
ATOM   5090  C  CA  . SER B  1  36  ? 2.558   -12.163 -54.187 1.00 82.64  ? 62   SER B CA  1 
ATOM   5091  C  C   . SER B  1  36  ? 1.100   -11.740 -54.297 1.00 82.62  ? 62   SER B C   1 
ATOM   5092  O  O   . SER B  1  36  ? 0.787   -10.592 -54.623 1.00 82.70  ? 62   SER B O   1 
ATOM   5093  C  CB  . SER B  1  36  ? 2.975   -12.068 -52.720 1.00 83.28  ? 62   SER B CB  1 
ATOM   5094  O  OG  . SER B  1  36  ? 4.316   -12.482 -52.536 1.00 84.74  ? 62   SER B OG  1 
ATOM   5095  N  N   . PHE B  1  37  ? 0.225   -12.692 -53.999 1.00 82.12  ? 63   PHE B N   1 
ATOM   5096  C  CA  . PHE B  1  37  ? -1.214  -12.493 -54.023 1.00 81.96  ? 63   PHE B CA  1 
ATOM   5097  C  C   . PHE B  1  37  ? -1.773  -11.851 -55.281 1.00 82.54  ? 63   PHE B C   1 
ATOM   5098  O  O   . PHE B  1  37  ? -2.582  -10.928 -55.212 1.00 83.63  ? 63   PHE B O   1 
ATOM   5099  C  CB  . PHE B  1  37  ? -1.648  -11.710 -52.778 1.00 80.84  ? 63   PHE B CB  1 
ATOM   5100  C  CG  . PHE B  1  37  ? -1.392  -12.451 -51.495 1.00 79.76  ? 63   PHE B CG  1 
ATOM   5101  C  CD1 . PHE B  1  37  ? -0.235  -12.223 -50.761 1.00 79.31  ? 63   PHE B CD1 1 
ATOM   5102  C  CD2 . PHE B  1  37  ? -2.274  -13.445 -51.069 1.00 78.71  ? 63   PHE B CD2 1 
ATOM   5103  C  CE1 . PHE B  1  37  ? 0.045   -12.980 -49.630 1.00 79.49  ? 63   PHE B CE1 1 
ATOM   5104  C  CE2 . PHE B  1  37  ? -2.007  -14.209 -49.944 1.00 77.36  ? 63   PHE B CE2 1 
ATOM   5105  C  CZ  . PHE B  1  37  ? -0.848  -13.979 -49.221 1.00 78.71  ? 63   PHE B CZ  1 
ATOM   5106  N  N   . ASN B  1  38  ? -1.323  -12.349 -56.429 1.00 82.46  ? 64   ASN B N   1 
ATOM   5107  C  CA  . ASN B  1  38  ? -1.791  -11.878 -57.729 1.00 81.99  ? 64   ASN B CA  1 
ATOM   5108  C  C   . ASN B  1  38  ? -2.134  -13.135 -58.511 1.00 82.14  ? 64   ASN B C   1 
ATOM   5109  O  O   . ASN B  1  38  ? -1.400  -14.121 -58.448 1.00 82.29  ? 64   ASN B O   1 
ATOM   5110  C  CB  . ASN B  1  38  ? -0.710  -11.069 -58.449 1.00 81.30  ? 64   ASN B CB  1 
ATOM   5111  C  CG  . ASN B  1  38  ? -0.631  -9.637  -57.948 1.00 81.39  ? 64   ASN B CG  1 
ATOM   5112  O  OD1 . ASN B  1  38  ? -1.621  -8.912  -57.981 1.00 81.73  ? 64   ASN B OD1 1 
ATOM   5113  N  ND2 . ASN B  1  38  ? 0.545   -9.225  -57.477 1.00 80.91  ? 64   ASN B ND2 1 
ATOM   5114  N  N   . PRO B  1  39  ? -3.262  -13.125 -59.248 1.00 82.06  ? 65   PRO B N   1 
ATOM   5115  C  CA  . PRO B  1  39  ? -3.683  -14.296 -60.029 1.00 81.39  ? 65   PRO B CA  1 
ATOM   5116  C  C   . PRO B  1  39  ? -2.908  -14.490 -61.338 1.00 81.09  ? 65   PRO B C   1 
ATOM   5117  O  O   . PRO B  1  39  ? -3.389  -14.114 -62.405 1.00 82.50  ? 65   PRO B O   1 
ATOM   5118  C  CB  . PRO B  1  39  ? -5.162  -14.018 -60.264 1.00 80.89  ? 65   PRO B CB  1 
ATOM   5119  C  CG  . PRO B  1  39  ? -5.168  -12.522 -60.480 1.00 80.62  ? 65   PRO B CG  1 
ATOM   5120  C  CD  . PRO B  1  39  ? -4.222  -12.011 -59.405 1.00 81.85  ? 65   PRO B CD  1 
ATOM   5121  N  N   . LEU B  1  40  ? -1.720  -15.086 -61.262 1.00 79.36  ? 66   LEU B N   1 
ATOM   5122  C  CA  . LEU B  1  40  ? -0.905  -15.294 -62.455 1.00 78.24  ? 66   LEU B CA  1 
ATOM   5123  C  C   . LEU B  1  40  ? -1.466  -16.542 -63.134 1.00 78.43  ? 66   LEU B C   1 
ATOM   5124  O  O   . LEU B  1  40  ? -1.855  -16.500 -64.293 1.00 78.19  ? 66   LEU B O   1 
ATOM   5125  C  CB  . LEU B  1  40  ? 0.575   -15.185 -62.099 1.00 77.83  ? 66   LEU B CB  1 
ATOM   5126  C  CG  . LEU B  1  40  ? 1.015   -13.853 -61.473 1.00 76.35  ? 66   LEU B CG  1 
ATOM   5127  C  CD1 . LEU B  1  40  ? 2.501   -13.891 -61.162 1.00 75.92  ? 66   LEU B CD1 1 
ATOM   5128  C  CD2 . LEU B  1  40  ? 0.699   -12.714 -62.415 1.00 75.46  ? 66   LEU B CD2 1 
ATOM   5129  N  N   . ARG B  1  41  ? -1.482  -17.648 -62.408 1.00 79.41  ? 67   ARG B N   1 
ATOM   5130  C  CA  . ARG B  1  41  ? -2.041  -18.915 -62.874 1.00 80.53  ? 67   ARG B CA  1 
ATOM   5131  C  C   . ARG B  1  41  ? -1.415  -19.683 -64.039 1.00 80.88  ? 67   ARG B C   1 
ATOM   5132  O  O   . ARG B  1  41  ? -1.828  -20.807 -64.315 1.00 81.12  ? 67   ARG B O   1 
ATOM   5133  C  CB  . ARG B  1  41  ? -3.447  -18.810 -63.470 1.00 81.54  ? 67   ARG B CB  1 
ATOM   5134  C  CG  . ARG B  1  41  ? -4.390  -17.963 -62.618 1.00 85.50  ? 67   ARG B CG  1 
ATOM   5135  C  CD  . ARG B  1  41  ? -5.817  -17.946 -63.151 1.00 89.23  ? 67   ARG B CD  1 
ATOM   5136  N  NE  . ARG B  1  41  ? -6.481  -16.673 -62.864 1.00 93.02  ? 67   ARG B NE  1 
ATOM   5137  C  CZ  . ARG B  1  41  ? -7.739  -16.392 -63.190 1.00 93.71  ? 67   ARG B CZ  1 
ATOM   5138  N  NH1 . ARG B  1  41  ? -8.481  -17.302 -63.811 1.00 93.07  ? 67   ARG B NH1 1 
ATOM   5139  N  NH2 . ARG B  1  41  ? -8.249  -15.190 -62.920 1.00 93.59  ? 67   ARG B NH2 1 
ATOM   5140  N  N   . HIS B  1  42  ? -0.447  -19.097 -64.739 1.00 82.24  ? 68   HIS B N   1 
ATOM   5141  C  CA  . HIS B  1  42  ? 0.175   -19.781 -65.882 1.00 84.11  ? 68   HIS B CA  1 
ATOM   5142  C  C   . HIS B  1  42  ? 1.546   -19.160 -65.988 1.00 84.06  ? 68   HIS B C   1 
ATOM   5143  O  O   . HIS B  1  42  ? 1.684   -17.998 -66.371 1.00 84.36  ? 68   HIS B O   1 
ATOM   5144  C  CB  . HIS B  1  42  ? -0.474  -19.778 -67.287 1.00 86.23  ? 68   HIS B CB  1 
ATOM   5145  C  CG  . HIS B  1  42  ? 0.161   -20.725 -68.273 1.00 87.85  ? 68   HIS B CG  1 
ATOM   5146  N  ND1 . HIS B  1  42  ? 0.407   -22.057 -67.991 1.00 88.30  ? 68   HIS B ND1 1 
ATOM   5147  C  CD2 . HIS B  1  42  ? 0.499   -20.554 -69.577 1.00 88.60  ? 68   HIS B CD2 1 
ATOM   5148  C  CE1 . HIS B  1  42  ? 0.859   -22.662 -69.075 1.00 87.96  ? 68   HIS B CE1 1 
ATOM   5149  N  NE2 . HIS B  1  42  ? 0.924   -21.774 -70.052 1.00 89.57  ? 68   HIS B NE2 1 
ATOM   5150  N  N   . LEU B  1  43  ? 2.560   -19.946 -65.652 1.00 83.90  ? 69   LEU B N   1 
ATOM   5151  C  CA  . LEU B  1  43  ? 3.932   -19.483 -65.747 1.00 83.30  ? 69   LEU B CA  1 
ATOM   5152  C  C   . LEU B  1  43  ? 4.509   -20.130 -67.007 1.00 84.41  ? 69   LEU B C   1 
ATOM   5153  O  O   . LEU B  1  43  ? 4.879   -21.310 -67.001 1.00 83.45  ? 69   LEU B O   1 
ATOM   5154  C  CB  . LEU B  1  43  ? 4.711   -19.907 -64.505 1.00 81.15  ? 69   LEU B CB  1 
ATOM   5155  C  CG  . LEU B  1  43  ? 5.484   -18.798 -63.784 1.00 79.02  ? 69   LEU B CG  1 
ATOM   5156  C  CD1 . LEU B  1  43  ? 4.594   -17.589 -63.552 1.00 76.47  ? 69   LEU B CD1 1 
ATOM   5157  C  CD2 . LEU B  1  43  ? 6.022   -19.346 -62.468 1.00 78.08  ? 69   LEU B CD2 1 
ATOM   5158  N  N   . GLY B  1  44  ? 4.558   -19.354 -68.090 1.00 86.13  ? 70   GLY B N   1 
ATOM   5159  C  CA  . GLY B  1  44  ? 5.069   -19.861 -69.355 1.00 88.11  ? 70   GLY B CA  1 
ATOM   5160  C  C   . GLY B  1  44  ? 6.540   -19.583 -69.595 1.00 89.25  ? 70   GLY B C   1 
ATOM   5161  O  O   . GLY B  1  44  ? 7.204   -18.955 -68.774 1.00 89.48  ? 70   GLY B O   1 
ATOM   5162  N  N   . SER B  1  45  ? 7.050   -20.049 -70.730 1.00 90.70  ? 71   SER B N   1 
ATOM   5163  C  CA  . SER B  1  45  ? 8.460   -19.866 -71.076 1.00 91.58  ? 71   SER B CA  1 
ATOM   5164  C  C   . SER B  1  45  ? 8.901   -18.408 -71.120 1.00 91.62  ? 71   SER B C   1 
ATOM   5165  O  O   . SER B  1  45  ? 8.196   -17.540 -71.637 1.00 91.15  ? 71   SER B O   1 
ATOM   5166  C  CB  . SER B  1  45  ? 8.757   -20.530 -72.414 1.00 91.55  ? 71   SER B CB  1 
ATOM   5167  O  OG  . SER B  1  45  ? 8.387   -21.898 -72.372 1.00 93.94  ? 71   SER B OG  1 
ATOM   5168  N  N   . TYR B  1  46  ? 10.086  -18.156 -70.576 1.00 92.45  ? 72   TYR B N   1 
ATOM   5169  C  CA  . TYR B  1  46  ? 10.653  -16.815 -70.525 1.00 92.99  ? 72   TYR B CA  1 
ATOM   5170  C  C   . TYR B  1  46  ? 9.656   -15.790 -69.993 1.00 92.95  ? 72   TYR B C   1 
ATOM   5171  O  O   . TYR B  1  46  ? 9.546   -14.690 -70.539 1.00 92.13  ? 72   TYR B O   1 
ATOM   5172  C  CB  . TYR B  1  46  ? 11.147  -16.385 -71.909 1.00 93.49  ? 72   TYR B CB  1 
ATOM   5173  C  CG  . TYR B  1  46  ? 12.339  -17.176 -72.419 1.00 94.84  ? 72   TYR B CG  1 
ATOM   5174  C  CD1 . TYR B  1  46  ? 12.163  -18.338 -73.181 1.00 94.81  ? 72   TYR B CD1 1 
ATOM   5175  C  CD2 . TYR B  1  46  ? 13.646  -16.776 -72.118 1.00 95.42  ? 72   TYR B CD2 1 
ATOM   5176  C  CE1 . TYR B  1  46  ? 13.261  -19.085 -73.629 1.00 95.87  ? 72   TYR B CE1 1 
ATOM   5177  C  CE2 . TYR B  1  46  ? 14.750  -17.516 -72.558 1.00 96.04  ? 72   TYR B CE2 1 
ATOM   5178  C  CZ  . TYR B  1  46  ? 14.553  -18.671 -73.313 1.00 96.58  ? 72   TYR B CZ  1 
ATOM   5179  O  OH  . TYR B  1  46  ? 15.641  -19.421 -73.735 1.00 96.93  ? 72   TYR B OH  1 
ATOM   5180  N  N   . SER B  1  47  ? 8.940   -16.159 -68.926 1.00 92.92  ? 73   SER B N   1 
ATOM   5181  C  CA  . SER B  1  47  ? 7.950   -15.286 -68.293 1.00 91.43  ? 73   SER B CA  1 
ATOM   5182  C  C   . SER B  1  47  ? 8.623   -14.056 -67.716 1.00 90.75  ? 73   SER B C   1 
ATOM   5183  O  O   . SER B  1  47  ? 8.064   -12.962 -67.729 1.00 90.55  ? 73   SER B O   1 
ATOM   5184  C  CB  . SER B  1  47  ? 7.205   -16.028 -67.179 1.00 91.15  ? 73   SER B CB  1 
ATOM   5185  O  OG  . SER B  1  47  ? 6.158   -16.833 -67.699 1.00 91.58  ? 73   SER B OG  1 
ATOM   5186  N  N   . PHE B  1  48  ? 9.828   -14.247 -67.202 1.00 90.52  ? 74   PHE B N   1 
ATOM   5187  C  CA  . PHE B  1  48  ? 10.588  -13.144 -66.643 1.00 91.18  ? 74   PHE B CA  1 
ATOM   5188  C  C   . PHE B  1  48  ? 11.746  -12.917 -67.576 1.00 92.10  ? 74   PHE B C   1 
ATOM   5189  O  O   . PHE B  1  48  ? 12.547  -13.826 -67.807 1.00 92.48  ? 74   PHE B O   1 
ATOM   5190  C  CB  . PHE B  1  48  ? 11.134  -13.497 -65.262 1.00 90.05  ? 74   PHE B CB  1 
ATOM   5191  C  CG  . PHE B  1  48  ? 10.074  -13.833 -64.261 1.00 89.49  ? 74   PHE B CG  1 
ATOM   5192  C  CD1 . PHE B  1  48  ? 9.299   -12.829 -63.687 1.00 88.55  ? 74   PHE B CD1 1 
ATOM   5193  C  CD2 . PHE B  1  48  ? 9.823   -15.164 -63.919 1.00 89.58  ? 74   PHE B CD2 1 
ATOM   5194  C  CE1 . PHE B  1  48  ? 8.288   -13.140 -62.791 1.00 87.62  ? 74   PHE B CE1 1 
ATOM   5195  C  CE2 . PHE B  1  48  ? 8.813   -15.488 -63.022 1.00 88.40  ? 74   PHE B CE2 1 
ATOM   5196  C  CZ  . PHE B  1  48  ? 8.040   -14.473 -62.455 1.00 88.07  ? 74   PHE B CZ  1 
ATOM   5197  N  N   . PHE B  1  49  ? 11.809  -11.719 -68.139 1.00 93.11  ? 75   PHE B N   1 
ATOM   5198  C  CA  . PHE B  1  49  ? 12.893  -11.335 -69.031 1.00 94.06  ? 75   PHE B CA  1 
ATOM   5199  C  C   . PHE B  1  49  ? 13.118  -9.850  -68.813 1.00 94.49  ? 75   PHE B C   1 
ATOM   5200  O  O   . PHE B  1  49  ? 14.208  -9.336  -69.032 1.00 94.99  ? 75   PHE B O   1 
ATOM   5201  C  CB  . PHE B  1  49  ? 12.557  -11.640 -70.504 1.00 93.56  ? 75   PHE B CB  1 
ATOM   5202  C  CG  . PHE B  1  49  ? 11.240  -11.074 -70.974 1.00 94.70  ? 75   PHE B CG  1 
ATOM   5203  C  CD1 . PHE B  1  49  ? 11.035  -9.690  -71.072 1.00 94.09  ? 75   PHE B CD1 1 
ATOM   5204  C  CD2 . PHE B  1  49  ? 10.201  -11.931 -71.336 1.00 95.49  ? 75   PHE B CD2 1 
ATOM   5205  C  CE1 . PHE B  1  49  ? 9.815   -9.168  -71.524 1.00 92.97  ? 75   PHE B CE1 1 
ATOM   5206  C  CE2 . PHE B  1  49  ? 8.974   -11.423 -71.790 1.00 95.60  ? 75   PHE B CE2 1 
ATOM   5207  C  CZ  . PHE B  1  49  ? 8.782   -10.033 -71.885 1.00 94.26  ? 75   PHE B CZ  1 
ATOM   5208  N  N   . SER B  1  50  ? 12.078  -9.168  -68.353 1.00 94.88  ? 76   SER B N   1 
ATOM   5209  C  CA  . SER B  1  50  ? 12.157  -7.739  -68.086 1.00 95.77  ? 76   SER B CA  1 
ATOM   5210  C  C   . SER B  1  50  ? 13.084  -7.477  -66.897 1.00 95.82  ? 76   SER B C   1 
ATOM   5211  O  O   . SER B  1  50  ? 13.432  -6.327  -66.608 1.00 95.63  ? 76   SER B O   1 
ATOM   5212  C  CB  . SER B  1  50  ? 10.762  -7.186  -67.764 1.00 96.97  ? 76   SER B CB  1 
ATOM   5213  O  OG  . SER B  1  50  ? 9.807   -7.566  -68.743 1.00 97.73  ? 76   SER B OG  1 
ATOM   5214  N  N   . PHE B  1  51  ? 13.475  -8.552  -66.209 1.00 95.60  ? 77   PHE B N   1 
ATOM   5215  C  CA  . PHE B  1  51  ? 14.340  -8.468  -65.025 1.00 94.44  ? 77   PHE B CA  1 
ATOM   5216  C  C   . PHE B  1  51  ? 15.474  -9.475  -65.158 1.00 93.49  ? 77   PHE B C   1 
ATOM   5217  O  O   . PHE B  1  51  ? 15.395  -10.582 -64.634 1.00 93.30  ? 77   PHE B O   1 
ATOM   5218  C  CB  . PHE B  1  51  ? 13.506  -8.783  -63.784 1.00 93.66  ? 77   PHE B CB  1 
ATOM   5219  C  CG  . PHE B  1  51  ? 12.099  -8.271  -63.873 1.00 92.18  ? 77   PHE B CG  1 
ATOM   5220  C  CD1 . PHE B  1  51  ? 11.813  -6.935  -63.602 1.00 91.78  ? 77   PHE B CD1 1 
ATOM   5221  C  CD2 . PHE B  1  51  ? 11.079  -9.101  -64.323 1.00 91.76  ? 77   PHE B CD2 1 
ATOM   5222  C  CE1 . PHE B  1  51  ? 10.535  -6.432  -63.785 1.00 91.86  ? 77   PHE B CE1 1 
ATOM   5223  C  CE2 . PHE B  1  51  ? 9.798   -8.615  -64.513 1.00 92.21  ? 77   PHE B CE2 1 
ATOM   5224  C  CZ  . PHE B  1  51  ? 9.518   -7.272  -64.245 1.00 92.52  ? 77   PHE B CZ  1 
ATOM   5225  N  N   . PRO B  1  52  ? 16.545  -9.100  -65.865 1.00 92.66  ? 78   PRO B N   1 
ATOM   5226  C  CA  . PRO B  1  52  ? 17.655  -10.029 -66.031 1.00 91.80  ? 78   PRO B CA  1 
ATOM   5227  C  C   . PRO B  1  52  ? 18.599  -10.009 -64.848 1.00 91.30  ? 78   PRO B C   1 
ATOM   5228  O  O   . PRO B  1  52  ? 19.388  -10.937 -64.667 1.00 92.05  ? 78   PRO B O   1 
ATOM   5229  C  CB  . PRO B  1  52  ? 18.321  -9.522  -67.297 1.00 92.09  ? 78   PRO B CB  1 
ATOM   5230  C  CG  . PRO B  1  52  ? 18.220  -8.041  -67.118 1.00 92.32  ? 78   PRO B CG  1 
ATOM   5231  C  CD  . PRO B  1  52  ? 16.789  -7.854  -66.619 1.00 92.65  ? 78   PRO B CD  1 
ATOM   5232  N  N   . GLU B  1  53  ? 18.514  -8.959  -64.033 1.00 90.09  ? 79   GLU B N   1 
ATOM   5233  C  CA  . GLU B  1  53  ? 19.408  -8.827  -62.887 1.00 88.97  ? 79   GLU B CA  1 
ATOM   5234  C  C   . GLU B  1  53  ? 18.747  -9.142  -61.533 1.00 88.26  ? 79   GLU B C   1 
ATOM   5235  O  O   . GLU B  1  53  ? 19.193  -8.656  -60.491 1.00 87.47  ? 79   GLU B O   1 
ATOM   5236  C  CB  . GLU B  1  53  ? 20.021  -7.413  -62.892 1.00 87.53  ? 79   GLU B CB  1 
ATOM   5237  C  CG  . GLU B  1  53  ? 21.546  -7.337  -62.592 1.00 86.44  ? 79   GLU B CG  1 
ATOM   5238  C  CD  . GLU B  1  53  ? 22.452  -8.088  -63.608 1.00 84.31  ? 79   GLU B CD  1 
ATOM   5239  O  OE1 . GLU B  1  53  ? 23.690  -8.025  -63.489 1.00 79.98  ? 79   GLU B OE1 1 
ATOM   5240  O  OE2 . GLU B  1  53  ? 21.943  -8.749  -64.525 1.00 83.20  ? 79   GLU B OE2 1 
ATOM   5241  N  N   . LEU B  1  54  ? 17.708  -9.982  -61.557 1.00 87.71  ? 80   LEU B N   1 
ATOM   5242  C  CA  . LEU B  1  54  ? 16.963  -10.381 -60.347 1.00 85.74  ? 80   LEU B CA  1 
ATOM   5243  C  C   . LEU B  1  54  ? 17.664  -11.375 -59.425 1.00 83.89  ? 80   LEU B C   1 
ATOM   5244  O  O   . LEU B  1  54  ? 18.240  -12.369 -59.877 1.00 83.87  ? 80   LEU B O   1 
ATOM   5245  C  CB  . LEU B  1  54  ? 15.600  -10.988 -60.714 1.00 86.28  ? 80   LEU B CB  1 
ATOM   5246  C  CG  . LEU B  1  54  ? 14.331  -10.134 -60.618 1.00 86.43  ? 80   LEU B CG  1 
ATOM   5247  C  CD1 . LEU B  1  54  ? 13.111  -11.052 -60.676 1.00 86.89  ? 80   LEU B CD1 1 
ATOM   5248  C  CD2 . LEU B  1  54  ? 14.327  -9.339  -59.322 1.00 85.56  ? 80   LEU B CD2 1 
ATOM   5249  N  N   . GLN B  1  55  ? 17.559  -11.116 -58.124 1.00 81.47  ? 81   GLN B N   1 
ATOM   5250  C  CA  . GLN B  1  55  ? 18.166  -11.958 -57.104 1.00 78.99  ? 81   GLN B CA  1 
ATOM   5251  C  C   . GLN B  1  55  ? 17.124  -12.631 -56.209 1.00 77.47  ? 81   GLN B C   1 
ATOM   5252  O  O   . GLN B  1  55  ? 17.320  -13.766 -55.766 1.00 77.65  ? 81   GLN B O   1 
ATOM   5253  C  CB  . GLN B  1  55  ? 19.100  -11.124 -56.232 1.00 78.15  ? 81   GLN B CB  1 
ATOM   5254  C  CG  . GLN B  1  55  ? 20.059  -10.271 -57.020 1.00 78.80  ? 81   GLN B CG  1 
ATOM   5255  C  CD  . GLN B  1  55  ? 21.131  -9.647  -56.157 1.00 78.96  ? 81   GLN B CD  1 
ATOM   5256  O  OE1 . GLN B  1  55  ? 20.837  -9.033  -55.136 1.00 77.66  ? 81   GLN B OE1 1 
ATOM   5257  N  NE2 . GLN B  1  55  ? 22.385  -9.792  -56.569 1.00 79.78  ? 81   GLN B NE2 1 
ATOM   5258  N  N   . VAL B  1  56  ? 16.021  -11.931 -55.949 1.00 75.07  ? 82   VAL B N   1 
ATOM   5259  C  CA  . VAL B  1  56  ? 14.947  -12.442 -55.088 1.00 71.81  ? 82   VAL B CA  1 
ATOM   5260  C  C   . VAL B  1  56  ? 13.550  -12.328 -55.710 1.00 70.62  ? 82   VAL B C   1 
ATOM   5261  O  O   . VAL B  1  56  ? 13.073  -11.222 -55.961 1.00 70.64  ? 82   VAL B O   1 
ATOM   5262  C  CB  . VAL B  1  56  ? 14.920  -11.670 -53.765 1.00 70.68  ? 82   VAL B CB  1 
ATOM   5263  C  CG1 . VAL B  1  56  ? 14.203  -12.472 -52.721 1.00 69.06  ? 82   VAL B CG1 1 
ATOM   5264  C  CG2 . VAL B  1  56  ? 16.329  -11.342 -53.328 1.00 69.73  ? 82   VAL B CG2 1 
ATOM   5265  N  N   . LEU B  1  57  ? 12.885  -13.463 -55.925 1.00 69.29  ? 83   LEU B N   1 
ATOM   5266  C  CA  . LEU B  1  57  ? 11.546  -13.469 -56.518 1.00 68.86  ? 83   LEU B CA  1 
ATOM   5267  C  C   . LEU B  1  57  ? 10.476  -14.113 -55.631 1.00 69.23  ? 83   LEU B C   1 
ATOM   5268  O  O   . LEU B  1  57  ? 10.573  -15.291 -55.302 1.00 69.43  ? 83   LEU B O   1 
ATOM   5269  C  CB  . LEU B  1  57  ? 11.586  -14.189 -57.861 1.00 67.46  ? 83   LEU B CB  1 
ATOM   5270  C  CG  . LEU B  1  57  ? 10.251  -14.346 -58.577 1.00 66.61  ? 83   LEU B CG  1 
ATOM   5271  C  CD1 . LEU B  1  57  ? 9.642   -12.986 -58.865 1.00 65.39  ? 83   LEU B CD1 1 
ATOM   5272  C  CD2 . LEU B  1  57  ? 10.480  -15.112 -59.855 1.00 67.55  ? 83   LEU B CD2 1 
ATOM   5273  N  N   . ASP B  1  58  ? 9.452   -13.341 -55.265 1.00 69.93  ? 84   ASP B N   1 
ATOM   5274  C  CA  . ASP B  1  58  ? 8.360   -13.833 -54.407 1.00 70.67  ? 84   ASP B CA  1 
ATOM   5275  C  C   . ASP B  1  58  ? 7.030   -14.062 -55.166 1.00 70.32  ? 84   ASP B C   1 
ATOM   5276  O  O   . ASP B  1  58  ? 6.323   -13.109 -55.517 1.00 68.52  ? 84   ASP B O   1 
ATOM   5277  C  CB  . ASP B  1  58  ? 8.121   -12.830 -53.263 1.00 72.24  ? 84   ASP B CB  1 
ATOM   5278  C  CG  . ASP B  1  58  ? 7.416   -13.453 -52.048 1.00 73.32  ? 84   ASP B CG  1 
ATOM   5279  O  OD1 . ASP B  1  58  ? 6.585   -14.373 -52.225 1.00 75.13  ? 84   ASP B OD1 1 
ATOM   5280  O  OD2 . ASP B  1  58  ? 7.675   -13.000 -50.909 1.00 72.49  ? 84   ASP B OD2 1 
ATOM   5281  N  N   . LEU B  1  59  ? 6.691   -15.325 -55.405 1.00 70.45  ? 85   LEU B N   1 
ATOM   5282  C  CA  . LEU B  1  59  ? 5.455   -15.663 -56.103 1.00 71.87  ? 85   LEU B CA  1 
ATOM   5283  C  C   . LEU B  1  59  ? 4.490   -16.371 -55.165 1.00 72.66  ? 85   LEU B C   1 
ATOM   5284  O  O   . LEU B  1  59  ? 3.785   -17.300 -55.562 1.00 72.95  ? 85   LEU B O   1 
ATOM   5285  C  CB  . LEU B  1  59  ? 5.750   -16.553 -57.311 1.00 71.89  ? 85   LEU B CB  1 
ATOM   5286  C  CG  . LEU B  1  59  ? 6.555   -15.902 -58.437 1.00 71.82  ? 85   LEU B CG  1 
ATOM   5287  C  CD1 . LEU B  1  59  ? 6.917   -16.955 -59.466 1.00 72.77  ? 85   LEU B CD1 1 
ATOM   5288  C  CD2 . LEU B  1  59  ? 5.746   -14.781 -59.067 1.00 71.49  ? 85   LEU B CD2 1 
ATOM   5289  N  N   . SER B  1  60  ? 4.465   -15.919 -53.916 1.00 73.31  ? 86   SER B N   1 
ATOM   5290  C  CA  . SER B  1  60  ? 3.595   -16.494 -52.896 1.00 74.12  ? 86   SER B CA  1 
ATOM   5291  C  C   . SER B  1  60  ? 2.111   -16.322 -53.217 1.00 74.72  ? 86   SER B C   1 
ATOM   5292  O  O   . SER B  1  60  ? 1.666   -15.225 -53.589 1.00 74.51  ? 86   SER B O   1 
ATOM   5293  C  CB  . SER B  1  60  ? 3.877   -15.847 -51.528 1.00 73.78  ? 86   SER B CB  1 
ATOM   5294  O  OG  . SER B  1  60  ? 5.080   -16.313 -50.945 1.00 73.74  ? 86   SER B OG  1 
ATOM   5295  N  N   . ARG B  1  61  ? 1.360   -17.413 -53.073 1.00 74.34  ? 87   ARG B N   1 
ATOM   5296  C  CA  . ARG B  1  61  ? -0.088  -17.411 -53.287 1.00 74.52  ? 87   ARG B CA  1 
ATOM   5297  C  C   . ARG B  1  61  ? -0.503  -16.719 -54.583 1.00 75.72  ? 87   ARG B C   1 
ATOM   5298  O  O   . ARG B  1  61  ? -1.243  -15.735 -54.544 1.00 76.73  ? 87   ARG B O   1 
ATOM   5299  C  CB  . ARG B  1  61  ? -0.774  -16.708 -52.105 1.00 72.19  ? 87   ARG B CB  1 
ATOM   5300  C  CG  . ARG B  1  61  ? -2.100  -17.295 -51.701 1.00 69.63  ? 87   ARG B CG  1 
ATOM   5301  C  CD  . ARG B  1  61  ? -1.911  -18.657 -51.067 1.00 67.36  ? 87   ARG B CD  1 
ATOM   5302  N  NE  . ARG B  1  61  ? -3.187  -19.291 -50.763 1.00 65.87  ? 87   ARG B NE  1 
ATOM   5303  C  CZ  . ARG B  1  61  ? -3.327  -20.341 -49.960 1.00 66.50  ? 87   ARG B CZ  1 
ATOM   5304  N  NH1 . ARG B  1  61  ? -2.270  -20.885 -49.371 1.00 66.81  ? 87   ARG B NH1 1 
ATOM   5305  N  NH2 . ARG B  1  61  ? -4.531  -20.844 -49.739 1.00 67.78  ? 87   ARG B NH2 1 
ATOM   5306  N  N   . CYS B  1  62  ? -0.044  -17.232 -55.722 1.00 76.30  ? 88   CYS B N   1 
ATOM   5307  C  CA  . CYS B  1  62  ? -0.367  -16.629 -57.014 1.00 77.15  ? 88   CYS B CA  1 
ATOM   5308  C  C   . CYS B  1  62  ? -1.196  -17.531 -57.904 1.00 77.11  ? 88   CYS B C   1 
ATOM   5309  O  O   . CYS B  1  62  ? -1.191  -17.389 -59.124 1.00 76.90  ? 88   CYS B O   1 
ATOM   5310  C  CB  . CYS B  1  62  ? 0.911   -16.238 -57.752 1.00 78.49  ? 88   CYS B CB  1 
ATOM   5311  S  SG  . CYS B  1  62  ? 1.785   -14.815 -57.048 1.00 82.67  ? 88   CYS B SG  1 
ATOM   5312  N  N   . GLU B  1  63  ? -1.911  -18.461 -57.292 1.00 77.86  ? 89   GLU B N   1 
ATOM   5313  C  CA  . GLU B  1  63  ? -2.753  -19.376 -58.047 1.00 77.44  ? 89   GLU B CA  1 
ATOM   5314  C  C   . GLU B  1  63  ? -2.002  -20.084 -59.160 1.00 76.99  ? 89   GLU B C   1 
ATOM   5315  O  O   . GLU B  1  63  ? -2.623  -20.638 -60.057 1.00 76.70  ? 89   GLU B O   1 
ATOM   5316  C  CB  . GLU B  1  63  ? -3.927  -18.636 -58.679 1.00 77.93  ? 89   GLU B CB  1 
ATOM   5317  C  CG  . GLU B  1  63  ? -4.769  -17.826 -57.726 1.00 80.76  ? 89   GLU B CG  1 
ATOM   5318  C  CD  . GLU B  1  63  ? -6.085  -17.380 -58.358 1.00 82.64  ? 89   GLU B CD  1 
ATOM   5319  O  OE1 . GLU B  1  63  ? -6.753  -16.487 -57.785 1.00 84.15  ? 89   GLU B OE1 1 
ATOM   5320  O  OE2 . GLU B  1  63  ? -6.459  -17.933 -59.419 1.00 82.45  ? 89   GLU B OE2 1 
ATOM   5321  N  N   . ILE B  1  64  ? -0.674  -20.067 -59.122 1.00 77.75  ? 90   ILE B N   1 
ATOM   5322  C  CA  . ILE B  1  64  ? 0.099   -20.739 -60.169 1.00 77.61  ? 90   ILE B CA  1 
ATOM   5323  C  C   . ILE B  1  64  ? -0.236  -22.237 -60.237 1.00 79.00  ? 90   ILE B C   1 
ATOM   5324  O  O   . ILE B  1  64  ? 0.030   -22.998 -59.307 1.00 78.04  ? 90   ILE B O   1 
ATOM   5325  C  CB  . ILE B  1  64  ? 1.609   -20.519 -59.957 1.00 75.35  ? 90   ILE B CB  1 
ATOM   5326  C  CG1 . ILE B  1  64  ? 1.926   -19.037 -60.183 1.00 73.48  ? 90   ILE B CG1 1 
ATOM   5327  C  CG2 . ILE B  1  64  ? 2.411   -21.415 -60.886 1.00 73.67  ? 90   ILE B CG2 1 
ATOM   5328  C  CD1 . ILE B  1  64  ? 3.336   -18.632 -59.834 1.00 74.02  ? 90   ILE B CD1 1 
ATOM   5329  N  N   . GLN B  1  65  ? -0.828  -22.642 -61.358 1.00 80.91  ? 91   GLN B N   1 
ATOM   5330  C  CA  . GLN B  1  65  ? -1.250  -24.022 -61.558 1.00 83.77  ? 91   GLN B CA  1 
ATOM   5331  C  C   . GLN B  1  65  ? -0.293  -24.868 -62.397 1.00 84.37  ? 91   GLN B C   1 
ATOM   5332  O  O   . GLN B  1  65  ? -0.189  -26.083 -62.196 1.00 83.28  ? 91   GLN B O   1 
ATOM   5333  C  CB  . GLN B  1  65  ? -2.633  -24.025 -62.204 1.00 85.67  ? 91   GLN B CB  1 
ATOM   5334  C  CG  . GLN B  1  65  ? -3.407  -25.309 -62.009 1.00 89.05  ? 91   GLN B CG  1 
ATOM   5335  C  CD  . GLN B  1  65  ? -4.722  -25.300 -62.754 1.00 91.40  ? 91   GLN B CD  1 
ATOM   5336  O  OE1 . GLN B  1  65  ? -4.757  -25.429 -63.981 1.00 92.26  ? 91   GLN B OE1 1 
ATOM   5337  N  NE2 . GLN B  1  65  ? -5.814  -25.133 -62.019 1.00 92.51  ? 91   GLN B NE2 1 
ATOM   5338  N  N   . THR B  1  66  ? 0.391   -24.226 -63.339 1.00 85.60  ? 92   THR B N   1 
ATOM   5339  C  CA  . THR B  1  66  ? 1.341   -24.917 -64.208 1.00 86.32  ? 92   THR B CA  1 
ATOM   5340  C  C   . THR B  1  66  ? 2.539   -24.043 -64.578 1.00 86.68  ? 92   THR B C   1 
ATOM   5341  O  O   . THR B  1  66  ? 2.386   -22.887 -64.994 1.00 85.65  ? 92   THR B O   1 
ATOM   5342  C  CB  . THR B  1  66  ? 0.671   -25.394 -65.529 1.00 86.85  ? 92   THR B CB  1 
ATOM   5343  O  OG1 . THR B  1  66  ? 0.043   -24.281 -66.181 1.00 87.58  ? 92   THR B OG1 1 
ATOM   5344  C  CG2 . THR B  1  66  ? -0.375  -26.470 -65.250 1.00 86.74  ? 92   THR B CG2 1 
ATOM   5345  N  N   . ILE B  1  67  ? 3.733   -24.601 -64.397 1.00 87.54  ? 93   ILE B N   1 
ATOM   5346  C  CA  . ILE B  1  67  ? 4.973   -23.908 -64.744 1.00 88.00  ? 93   ILE B CA  1 
ATOM   5347  C  C   . ILE B  1  67  ? 5.561   -24.751 -65.858 1.00 88.68  ? 93   ILE B C   1 
ATOM   5348  O  O   . ILE B  1  67  ? 5.678   -25.975 -65.723 1.00 88.42  ? 93   ILE B O   1 
ATOM   5349  C  CB  . ILE B  1  67  ? 5.976   -23.848 -63.570 1.00 87.10  ? 93   ILE B CB  1 
ATOM   5350  C  CG1 . ILE B  1  67  ? 5.392   -23.024 -62.417 1.00 87.08  ? 93   ILE B CG1 1 
ATOM   5351  C  CG2 . ILE B  1  67  ? 7.262   -23.197 -64.032 1.00 86.21  ? 93   ILE B CG2 1 
ATOM   5352  C  CD1 . ILE B  1  67  ? 6.282   -22.946 -61.200 1.00 86.17  ? 93   ILE B CD1 1 
ATOM   5353  N  N   . GLU B  1  68  ? 5.910   -24.094 -66.961 1.00 89.41  ? 94   GLU B N   1 
ATOM   5354  C  CA  . GLU B  1  68  ? 6.453   -24.778 -68.130 1.00 90.23  ? 94   GLU B CA  1 
ATOM   5355  C  C   . GLU B  1  68  ? 7.975   -24.719 -68.219 1.00 89.69  ? 94   GLU B C   1 
ATOM   5356  O  O   . GLU B  1  68  ? 8.635   -24.093 -67.389 1.00 89.35  ? 94   GLU B O   1 
ATOM   5357  C  CB  . GLU B  1  68  ? 5.836   -24.181 -69.393 1.00 91.20  ? 94   GLU B CB  1 
ATOM   5358  C  CG  . GLU B  1  68  ? 4.324   -24.067 -69.310 1.00 93.56  ? 94   GLU B CG  1 
ATOM   5359  C  CD  . GLU B  1  68  ? 3.711   -23.353 -70.498 1.00 94.49  ? 94   GLU B CD  1 
ATOM   5360  O  OE1 . GLU B  1  68  ? 4.269   -22.310 -70.915 1.00 93.96  ? 94   GLU B OE1 1 
ATOM   5361  O  OE2 . GLU B  1  68  ? 2.663   -23.832 -70.997 1.00 95.25  ? 94   GLU B OE2 1 
ATOM   5362  N  N   . ASP B  1  69  ? 8.523   -25.390 -69.229 1.00 89.26  ? 95   ASP B N   1 
ATOM   5363  C  CA  . ASP B  1  69  ? 9.962   -25.431 -69.443 1.00 88.56  ? 95   ASP B CA  1 
ATOM   5364  C  C   . ASP B  1  69  ? 10.562  -24.046 -69.593 1.00 88.05  ? 95   ASP B C   1 
ATOM   5365  O  O   . ASP B  1  69  ? 10.071  -23.223 -70.367 1.00 88.17  ? 95   ASP B O   1 
ATOM   5366  C  CB  . ASP B  1  69  ? 10.284  -26.264 -70.683 1.00 89.49  ? 95   ASP B CB  1 
ATOM   5367  C  CG  . ASP B  1  69  ? 10.080  -27.747 -70.450 1.00 91.83  ? 95   ASP B CG  1 
ATOM   5368  O  OD1 . ASP B  1  69  ? 10.992  -28.385 -69.887 1.00 92.86  ? 95   ASP B OD1 1 
ATOM   5369  O  OD2 . ASP B  1  69  ? 9.002   -28.275 -70.804 1.00 93.71  ? 95   ASP B OD2 1 
ATOM   5370  N  N   . GLY B  1  70  ? 11.626  -23.796 -68.836 1.00 87.13  ? 96   GLY B N   1 
ATOM   5371  C  CA  . GLY B  1  70  ? 12.305  -22.515 -68.890 1.00 86.05  ? 96   GLY B CA  1 
ATOM   5372  C  C   . GLY B  1  70  ? 11.430  -21.296 -68.669 1.00 85.73  ? 96   GLY B C   1 
ATOM   5373  O  O   . GLY B  1  70  ? 11.311  -20.441 -69.545 1.00 85.85  ? 96   GLY B O   1 
ATOM   5374  N  N   . ALA B  1  71  ? 10.816  -21.208 -67.494 1.00 85.29  ? 97   ALA B N   1 
ATOM   5375  C  CA  . ALA B  1  71  ? 9.975   -20.067 -67.171 1.00 84.01  ? 97   ALA B CA  1 
ATOM   5376  C  C   . ALA B  1  71  ? 10.877  -18.968 -66.623 1.00 83.83  ? 97   ALA B C   1 
ATOM   5377  O  O   . ALA B  1  71  ? 10.607  -17.775 -66.793 1.00 83.41  ? 97   ALA B O   1 
ATOM   5378  C  CB  . ALA B  1  71  ? 8.940   -20.462 -66.143 1.00 83.86  ? 97   ALA B CB  1 
ATOM   5379  N  N   . TYR B  1  72  ? 11.955  -19.384 -65.962 1.00 83.83  ? 98   TYR B N   1 
ATOM   5380  C  CA  . TYR B  1  72  ? 12.915  -18.438 -65.395 1.00 83.68  ? 98   TYR B CA  1 
ATOM   5381  C  C   . TYR B  1  72  ? 14.246  -18.581 -66.119 1.00 84.44  ? 98   TYR B C   1 
ATOM   5382  O  O   . TYR B  1  72  ? 15.301  -18.318 -65.544 1.00 84.84  ? 98   TYR B O   1 
ATOM   5383  C  CB  . TYR B  1  72  ? 13.148  -18.707 -63.899 1.00 80.87  ? 98   TYR B CB  1 
ATOM   5384  C  CG  . TYR B  1  72  ? 11.924  -19.083 -63.090 1.00 76.73  ? 98   TYR B CG  1 
ATOM   5385  C  CD1 . TYR B  1  72  ? 11.537  -20.418 -62.962 1.00 75.21  ? 98   TYR B CD1 1 
ATOM   5386  C  CD2 . TYR B  1  72  ? 11.170  -18.113 -62.431 1.00 73.66  ? 98   TYR B CD2 1 
ATOM   5387  C  CE1 . TYR B  1  72  ? 10.438  -20.776 -62.194 1.00 73.13  ? 98   TYR B CE1 1 
ATOM   5388  C  CE2 . TYR B  1  72  ? 10.069  -18.462 -61.669 1.00 72.29  ? 98   TYR B CE2 1 
ATOM   5389  C  CZ  . TYR B  1  72  ? 9.707   -19.794 -61.553 1.00 72.49  ? 98   TYR B CZ  1 
ATOM   5390  O  OH  . TYR B  1  72  ? 8.603   -20.151 -60.807 1.00 71.93  ? 98   TYR B OH  1 
ATOM   5391  N  N   . GLN B  1  73  ? 14.191  -18.984 -67.384 1.00 85.11  ? 99   GLN B N   1 
ATOM   5392  C  CA  . GLN B  1  73  ? 15.399  -19.198 -68.171 1.00 84.61  ? 99   GLN B CA  1 
ATOM   5393  C  C   . GLN B  1  73  ? 16.431  -18.068 -68.158 1.00 83.92  ? 99   GLN B C   1 
ATOM   5394  O  O   . GLN B  1  73  ? 17.633  -18.329 -68.222 1.00 83.73  ? 99   GLN B O   1 
ATOM   5395  C  CB  . GLN B  1  73  ? 15.028  -19.529 -69.619 1.00 83.84  ? 99   GLN B CB  1 
ATOM   5396  C  CG  . GLN B  1  73  ? 16.220  -19.990 -70.455 1.00 83.32  ? 99   GLN B CG  1 
ATOM   5397  C  CD  . GLN B  1  73  ? 16.958  -21.180 -69.840 1.00 82.54  ? 99   GLN B CD  1 
ATOM   5398  O  OE1 . GLN B  1  73  ? 16.415  -22.288 -69.746 1.00 81.31  ? 99   GLN B OE1 1 
ATOM   5399  N  NE2 . GLN B  1  73  ? 18.203  -20.949 -69.416 1.00 80.38  ? 99   GLN B NE2 1 
ATOM   5400  N  N   . SER B  1  74  ? 15.978  -16.827 -68.053 1.00 83.18  ? 100  SER B N   1 
ATOM   5401  C  CA  . SER B  1  74  ? 16.909  -15.709 -68.077 1.00 83.60  ? 100  SER B CA  1 
ATOM   5402  C  C   . SER B  1  74  ? 17.269  -15.102 -66.729 1.00 84.41  ? 100  SER B C   1 
ATOM   5403  O  O   . SER B  1  74  ? 17.664  -13.940 -66.662 1.00 84.07  ? 100  SER B O   1 
ATOM   5404  C  CB  . SER B  1  74  ? 16.352  -14.610 -68.974 1.00 83.89  ? 100  SER B CB  1 
ATOM   5405  O  OG  . SER B  1  74  ? 15.101  -14.159 -68.488 1.00 83.77  ? 100  SER B OG  1 
ATOM   5406  N  N   . LEU B  1  75  ? 17.150  -15.876 -65.658 1.00 86.21  ? 101  LEU B N   1 
ATOM   5407  C  CA  . LEU B  1  75  ? 17.454  -15.373 -64.310 1.00 87.15  ? 101  LEU B CA  1 
ATOM   5408  C  C   . LEU B  1  75  ? 18.686  -16.053 -63.710 1.00 88.20  ? 101  LEU B C   1 
ATOM   5409  O  O   . LEU B  1  75  ? 18.592  -16.833 -62.760 1.00 88.51  ? 101  LEU B O   1 
ATOM   5410  C  CB  . LEU B  1  75  ? 16.237  -15.589 -63.407 1.00 86.90  ? 101  LEU B CB  1 
ATOM   5411  C  CG  . LEU B  1  75  ? 15.005  -14.746 -63.750 1.00 86.48  ? 101  LEU B CG  1 
ATOM   5412  C  CD1 . LEU B  1  75  ? 13.749  -15.333 -63.121 1.00 85.77  ? 101  LEU B CD1 1 
ATOM   5413  C  CD2 . LEU B  1  75  ? 15.250  -13.317 -63.286 1.00 85.83  ? 101  LEU B CD2 1 
ATOM   5414  N  N   . SER B  1  76  ? 19.846  -15.737 -64.275 1.00 89.32  ? 102  SER B N   1 
ATOM   5415  C  CA  . SER B  1  76  ? 21.111  -16.322 -63.846 1.00 89.08  ? 102  SER B CA  1 
ATOM   5416  C  C   . SER B  1  76  ? 21.575  -15.833 -62.484 1.00 88.34  ? 102  SER B C   1 
ATOM   5417  O  O   . SER B  1  76  ? 22.359  -16.509 -61.824 1.00 88.27  ? 102  SER B O   1 
ATOM   5418  C  CB  . SER B  1  76  ? 22.200  -16.011 -64.870 1.00 89.86  ? 102  SER B CB  1 
ATOM   5419  O  OG  . SER B  1  76  ? 22.494  -14.621 -64.881 1.00 89.69  ? 102  SER B OG  1 
ATOM   5420  N  N   . HIS B  1  77  ? 21.101  -14.664 -62.067 1.00 87.67  ? 103  HIS B N   1 
ATOM   5421  C  CA  . HIS B  1  77  ? 21.511  -14.103 -60.780 1.00 87.75  ? 103  HIS B CA  1 
ATOM   5422  C  C   . HIS B  1  77  ? 20.542  -14.420 -59.622 1.00 86.17  ? 103  HIS B C   1 
ATOM   5423  O  O   . HIS B  1  77  ? 20.883  -14.253 -58.446 1.00 85.61  ? 103  HIS B O   1 
ATOM   5424  C  CB  . HIS B  1  77  ? 21.697  -12.575 -60.901 1.00 90.27  ? 103  HIS B CB  1 
ATOM   5425  C  CG  . HIS B  1  77  ? 22.695  -12.153 -61.943 1.00 93.57  ? 103  HIS B CG  1 
ATOM   5426  N  ND1 . HIS B  1  77  ? 23.955  -12.706 -62.039 1.00 95.08  ? 103  HIS B ND1 1 
ATOM   5427  C  CD2 . HIS B  1  77  ? 22.623  -11.216 -62.922 1.00 94.93  ? 103  HIS B CD2 1 
ATOM   5428  C  CE1 . HIS B  1  77  ? 24.612  -12.132 -63.033 1.00 95.79  ? 103  HIS B CE1 1 
ATOM   5429  N  NE2 . HIS B  1  77  ? 23.826  -11.222 -63.586 1.00 94.82  ? 103  HIS B NE2 1 
ATOM   5430  N  N   . LEU B  1  78  ? 19.340  -14.882 -59.954 1.00 83.26  ? 104  LEU B N   1 
ATOM   5431  C  CA  . LEU B  1  78  ? 18.345  -15.210 -58.938 1.00 79.51  ? 104  LEU B CA  1 
ATOM   5432  C  C   . LEU B  1  78  ? 18.862  -16.258 -57.964 1.00 78.19  ? 104  LEU B C   1 
ATOM   5433  O  O   . LEU B  1  78  ? 19.266  -17.349 -58.375 1.00 79.03  ? 104  LEU B O   1 
ATOM   5434  C  CB  . LEU B  1  78  ? 17.084  -15.747 -59.595 1.00 78.78  ? 104  LEU B CB  1 
ATOM   5435  C  CG  . LEU B  1  78  ? 15.920  -15.958 -58.633 1.00 77.46  ? 104  LEU B CG  1 
ATOM   5436  C  CD1 . LEU B  1  78  ? 15.287  -14.613 -58.325 1.00 76.55  ? 104  LEU B CD1 1 
ATOM   5437  C  CD2 . LEU B  1  78  ? 14.903  -16.907 -59.253 1.00 77.31  ? 104  LEU B CD2 1 
ATOM   5438  N  N   . SER B  1  79  ? 18.816  -15.933 -56.676 1.00 75.97  ? 105  SER B N   1 
ATOM   5439  C  CA  . SER B  1  79  ? 19.278  -16.836 -55.612 1.00 73.35  ? 105  SER B CA  1 
ATOM   5440  C  C   . SER B  1  79  ? 18.141  -17.353 -54.719 1.00 70.77  ? 105  SER B C   1 
ATOM   5441  O  O   . SER B  1  79  ? 18.289  -18.366 -54.027 1.00 69.87  ? 105  SER B O   1 
ATOM   5442  C  CB  . SER B  1  79  ? 20.293  -16.113 -54.728 1.00 74.26  ? 105  SER B CB  1 
ATOM   5443  O  OG  . SER B  1  79  ? 19.706  -14.944 -54.175 1.00 72.26  ? 105  SER B OG  1 
ATOM   5444  N  N   . THR B  1  80  ? 17.020  -16.635 -54.728 1.00 67.16  ? 106  THR B N   1 
ATOM   5445  C  CA  . THR B  1  80  ? 15.856  -16.994 -53.931 1.00 62.66  ? 106  THR B CA  1 
ATOM   5446  C  C   . THR B  1  80  ? 14.561  -16.958 -54.741 1.00 61.72  ? 106  THR B C   1 
ATOM   5447  O  O   . THR B  1  80  ? 14.234  -15.955 -55.380 1.00 61.32  ? 106  THR B O   1 
ATOM   5448  C  CB  . THR B  1  80  ? 15.713  -16.050 -52.741 1.00 60.41  ? 106  THR B CB  1 
ATOM   5449  O  OG1 . THR B  1  80  ? 16.898  -16.126 -51.951 1.00 59.25  ? 106  THR B OG1 1 
ATOM   5450  C  CG2 . THR B  1  80  ? 14.525  -16.424 -51.890 1.00 58.93  ? 106  THR B CG2 1 
ATOM   5451  N  N   . LEU B  1  81  ? 13.839  -18.074 -54.708 1.00 60.58  ? 107  LEU B N   1 
ATOM   5452  C  CA  . LEU B  1  81  ? 12.568  -18.222 -55.407 1.00 59.67  ? 107  LEU B CA  1 
ATOM   5453  C  C   . LEU B  1  81  ? 11.566  -18.772 -54.400 1.00 59.30  ? 107  LEU B C   1 
ATOM   5454  O  O   . LEU B  1  81  ? 11.785  -19.831 -53.813 1.00 59.45  ? 107  LEU B O   1 
ATOM   5455  C  CB  . LEU B  1  81  ? 12.717  -19.188 -56.585 1.00 59.23  ? 107  LEU B CB  1 
ATOM   5456  C  CG  . LEU B  1  81  ? 11.462  -19.587 -57.349 1.00 57.70  ? 107  LEU B CG  1 
ATOM   5457  C  CD1 . LEU B  1  81  ? 10.765  -18.363 -57.890 1.00 56.64  ? 107  LEU B CD1 1 
ATOM   5458  C  CD2 . LEU B  1  81  ? 11.858  -20.523 -58.465 1.00 58.07  ? 107  LEU B CD2 1 
ATOM   5459  N  N   . ILE B  1  82  ? 10.476  -18.039 -54.201 1.00 58.82  ? 108  ILE B N   1 
ATOM   5460  C  CA  . ILE B  1  82  ? 9.443   -18.418 -53.246 1.00 58.38  ? 108  ILE B CA  1 
ATOM   5461  C  C   . ILE B  1  82  ? 8.134   -18.715 -53.979 1.00 60.06  ? 108  ILE B C   1 
ATOM   5462  O  O   . ILE B  1  82  ? 7.582   -17.845 -54.656 1.00 62.11  ? 108  ILE B O   1 
ATOM   5463  C  CB  . ILE B  1  82  ? 9.225   -17.274 -52.244 1.00 56.67  ? 108  ILE B CB  1 
ATOM   5464  C  CG1 . ILE B  1  82  ? 10.573  -16.836 -51.670 1.00 55.42  ? 108  ILE B CG1 1 
ATOM   5465  C  CG2 . ILE B  1  82  ? 8.325   -17.725 -51.125 1.00 56.15  ? 108  ILE B CG2 1 
ATOM   5466  C  CD1 . ILE B  1  82  ? 10.520  -15.555 -50.910 1.00 53.47  ? 108  ILE B CD1 1 
ATOM   5467  N  N   . LEU B  1  83  ? 7.637   -19.939 -53.853 1.00 60.15  ? 109  LEU B N   1 
ATOM   5468  C  CA  . LEU B  1  83  ? 6.403   -20.325 -54.529 1.00 61.08  ? 109  LEU B CA  1 
ATOM   5469  C  C   . LEU B  1  83  ? 5.368   -20.804 -53.525 1.00 63.21  ? 109  LEU B C   1 
ATOM   5470  O  O   . LEU B  1  83  ? 4.483   -21.587 -53.873 1.00 63.56  ? 109  LEU B O   1 
ATOM   5471  C  CB  . LEU B  1  83  ? 6.682   -21.450 -55.531 1.00 58.84  ? 109  LEU B CB  1 
ATOM   5472  C  CG  . LEU B  1  83  ? 7.711   -21.185 -56.629 1.00 57.98  ? 109  LEU B CG  1 
ATOM   5473  C  CD1 . LEU B  1  83  ? 7.953   -22.459 -57.428 1.00 55.53  ? 109  LEU B CD1 1 
ATOM   5474  C  CD2 . LEU B  1  83  ? 7.220   -20.049 -57.527 1.00 57.34  ? 109  LEU B CD2 1 
ATOM   5475  N  N   . THR B  1  84  ? 5.489   -20.338 -52.283 1.00 64.45  ? 110  THR B N   1 
ATOM   5476  C  CA  . THR B  1  84  ? 4.575   -20.725 -51.208 1.00 65.08  ? 110  THR B CA  1 
ATOM   5477  C  C   . THR B  1  84  ? 3.085   -20.615 -51.569 1.00 66.18  ? 110  THR B C   1 
ATOM   5478  O  O   . THR B  1  84  ? 2.627   -19.604 -52.123 1.00 65.29  ? 110  THR B O   1 
ATOM   5479  C  CB  . THR B  1  84  ? 4.810   -19.862 -49.947 1.00 64.55  ? 110  THR B CB  1 
ATOM   5480  O  OG1 . THR B  1  84  ? 6.190   -19.901 -49.597 1.00 65.16  ? 110  THR B OG1 1 
ATOM   5481  C  CG2 . THR B  1  84  ? 4.003   -20.378 -48.781 1.00 64.01  ? 110  THR B CG2 1 
ATOM   5482  N  N   . GLY B  1  85  ? 2.341   -21.671 -51.259 1.00 66.55  ? 111  GLY B N   1 
ATOM   5483  C  CA  . GLY B  1  85  ? 0.906   -21.681 -51.486 1.00 68.35  ? 111  GLY B CA  1 
ATOM   5484  C  C   . GLY B  1  85  ? 0.337   -21.665 -52.893 1.00 69.50  ? 111  GLY B C   1 
ATOM   5485  O  O   . GLY B  1  85  ? -0.708  -21.052 -53.142 1.00 69.84  ? 111  GLY B O   1 
ATOM   5486  N  N   . ASN B  1  86  ? 1.001   -22.336 -53.820 1.00 70.22  ? 112  ASN B N   1 
ATOM   5487  C  CA  . ASN B  1  86  ? 0.498   -22.383 -55.175 1.00 70.82  ? 112  ASN B CA  1 
ATOM   5488  C  C   . ASN B  1  86  ? -0.011  -23.770 -55.486 1.00 72.25  ? 112  ASN B C   1 
ATOM   5489  O  O   . ASN B  1  86  ? 0.653   -24.769 -55.196 1.00 71.84  ? 112  ASN B O   1 
ATOM   5490  C  CB  . ASN B  1  86  ? 1.579   -21.980 -56.170 1.00 68.79  ? 112  ASN B CB  1 
ATOM   5491  C  CG  . ASN B  1  86  ? 1.813   -20.486 -56.181 1.00 68.96  ? 112  ASN B CG  1 
ATOM   5492  O  OD1 . ASN B  1  86  ? 0.897   -19.704 -56.441 1.00 67.95  ? 112  ASN B OD1 1 
ATOM   5493  N  ND2 . ASN B  1  86  ? 3.039   -20.078 -55.886 1.00 69.25  ? 112  ASN B ND2 1 
ATOM   5494  N  N   . PRO B  1  87  ? -1.229  -23.851 -56.049 1.00 73.65  ? 113  PRO B N   1 
ATOM   5495  C  CA  . PRO B  1  87  ? -1.842  -25.136 -56.406 1.00 74.23  ? 113  PRO B CA  1 
ATOM   5496  C  C   . PRO B  1  87  ? -1.234  -25.690 -57.691 1.00 75.47  ? 113  PRO B C   1 
ATOM   5497  O  O   . PRO B  1  87  ? -1.842  -25.613 -58.759 1.00 76.54  ? 113  PRO B O   1 
ATOM   5498  C  CB  . PRO B  1  87  ? -3.311  -24.770 -56.570 1.00 73.58  ? 113  PRO B CB  1 
ATOM   5499  C  CG  . PRO B  1  87  ? -3.236  -23.370 -57.114 1.00 72.21  ? 113  PRO B CG  1 
ATOM   5500  C  CD  . PRO B  1  87  ? -2.178  -22.736 -56.251 1.00 72.33  ? 113  PRO B CD  1 
ATOM   5501  N  N   . ILE B  1  88  ? -0.033  -26.244 -57.593 1.00 76.24  ? 114  ILE B N   1 
ATOM   5502  C  CA  . ILE B  1  88  ? 0.625   -26.771 -58.775 1.00 77.41  ? 114  ILE B CA  1 
ATOM   5503  C  C   . ILE B  1  88  ? 0.082   -28.126 -59.230 1.00 79.55  ? 114  ILE B C   1 
ATOM   5504  O  O   . ILE B  1  88  ? -0.047  -29.066 -58.437 1.00 79.68  ? 114  ILE B O   1 
ATOM   5505  C  CB  . ILE B  1  88  ? 2.157   -26.824 -58.556 1.00 75.55  ? 114  ILE B CB  1 
ATOM   5506  C  CG1 . ILE B  1  88  ? 2.722   -25.406 -58.679 1.00 74.55  ? 114  ILE B CG1 1 
ATOM   5507  C  CG2 . ILE B  1  88  ? 2.816   -27.753 -59.560 1.00 74.81  ? 114  ILE B CG2 1 
ATOM   5508  C  CD1 . ILE B  1  88  ? 4.217   -25.311 -58.554 1.00 73.84  ? 114  ILE B CD1 1 
ATOM   5509  N  N   . GLN B  1  89  ? -0.257  -28.188 -60.518 1.00 81.59  ? 115  GLN B N   1 
ATOM   5510  C  CA  . GLN B  1  89  ? -0.794  -29.388 -61.152 1.00 83.76  ? 115  GLN B CA  1 
ATOM   5511  C  C   . GLN B  1  89  ? 0.239   -29.974 -62.106 1.00 83.57  ? 115  GLN B C   1 
ATOM   5512  O  O   . GLN B  1  89  ? 0.448   -31.183 -62.145 1.00 82.66  ? 115  GLN B O   1 
ATOM   5513  C  CB  . GLN B  1  89  ? -2.059  -29.045 -61.949 1.00 86.71  ? 115  GLN B CB  1 
ATOM   5514  C  CG  . GLN B  1  89  ? -3.243  -28.566 -61.123 1.00 90.75  ? 115  GLN B CG  1 
ATOM   5515  C  CD  . GLN B  1  89  ? -4.003  -29.709 -60.477 1.00 93.03  ? 115  GLN B CD  1 
ATOM   5516  O  OE1 . GLN B  1  89  ? -3.421  -30.532 -59.759 1.00 94.18  ? 115  GLN B OE1 1 
ATOM   5517  N  NE2 . GLN B  1  89  ? -5.317  -29.765 -60.727 1.00 92.92  ? 115  GLN B NE2 1 
ATOM   5518  N  N   . SER B  1  90  ? 0.879   -29.104 -62.879 1.00 84.48  ? 116  SER B N   1 
ATOM   5519  C  CA  . SER B  1  90  ? 1.880   -29.536 -63.850 1.00 85.13  ? 116  SER B CA  1 
ATOM   5520  C  C   . SER B  1  90  ? 3.178   -28.751 -63.699 1.00 85.07  ? 116  SER B C   1 
ATOM   5521  O  O   . SER B  1  90  ? 3.197   -27.516 -63.783 1.00 83.98  ? 116  SER B O   1 
ATOM   5522  C  CB  . SER B  1  90  ? 1.332   -29.378 -65.281 1.00 86.08  ? 116  SER B CB  1 
ATOM   5523  O  OG  . SER B  1  90  ? 2.158   -30.023 -66.240 1.00 85.18  ? 116  SER B OG  1 
ATOM   5524  N  N   . LEU B  1  91  ? 4.259   -29.495 -63.489 1.00 85.28  ? 117  LEU B N   1 
ATOM   5525  C  CA  . LEU B  1  91  ? 5.585   -28.923 -63.306 1.00 86.45  ? 117  LEU B CA  1 
ATOM   5526  C  C   . LEU B  1  91  ? 6.517   -29.492 -64.373 1.00 87.32  ? 117  LEU B C   1 
ATOM   5527  O  O   . LEU B  1  91  ? 6.975   -30.636 -64.259 1.00 87.58  ? 117  LEU B O   1 
ATOM   5528  C  CB  . LEU B  1  91  ? 6.095   -29.285 -61.907 1.00 86.49  ? 117  LEU B CB  1 
ATOM   5529  C  CG  . LEU B  1  91  ? 7.171   -28.451 -61.206 1.00 85.66  ? 117  LEU B CG  1 
ATOM   5530  C  CD1 . LEU B  1  91  ? 6.730   -27.001 -61.090 1.00 84.76  ? 117  LEU B CD1 1 
ATOM   5531  C  CD2 . LEU B  1  91  ? 7.420   -29.027 -59.823 1.00 84.50  ? 117  LEU B CD2 1 
ATOM   5532  N  N   . ALA B  1  92  ? 6.795   -28.686 -65.401 1.00 88.15  ? 118  ALA B N   1 
ATOM   5533  C  CA  . ALA B  1  92  ? 7.655   -29.094 -66.522 1.00 88.09  ? 118  ALA B CA  1 
ATOM   5534  C  C   . ALA B  1  92  ? 9.019   -29.646 -66.112 1.00 87.85  ? 118  ALA B C   1 
ATOM   5535  O  O   . ALA B  1  92  ? 9.676   -29.115 -65.218 1.00 88.02  ? 118  ALA B O   1 
ATOM   5536  C  CB  . ALA B  1  92  ? 7.840   -27.928 -67.489 1.00 87.81  ? 118  ALA B CB  1 
ATOM   5537  N  N   . LEU B  1  93  ? 9.432   -30.712 -66.793 1.00 87.26  ? 119  LEU B N   1 
ATOM   5538  C  CA  . LEU B  1  93  ? 10.703  -31.387 -66.542 1.00 86.19  ? 119  LEU B CA  1 
ATOM   5539  C  C   . LEU B  1  93  ? 11.881  -30.418 -66.400 1.00 85.06  ? 119  LEU B C   1 
ATOM   5540  O  O   . LEU B  1  93  ? 12.861  -30.722 -65.725 1.00 85.15  ? 119  LEU B O   1 
ATOM   5541  C  CB  . LEU B  1  93  ? 10.976  -32.380 -67.677 1.00 87.27  ? 119  LEU B CB  1 
ATOM   5542  C  CG  . LEU B  1  93  ? 11.865  -33.608 -67.448 1.00 87.62  ? 119  LEU B CG  1 
ATOM   5543  C  CD1 . LEU B  1  93  ? 11.731  -34.537 -68.658 1.00 88.37  ? 119  LEU B CD1 1 
ATOM   5544  C  CD2 . LEU B  1  93  ? 13.315  -33.204 -67.236 1.00 87.48  ? 119  LEU B CD2 1 
ATOM   5545  N  N   . GLY B  1  94  ? 11.786  -29.257 -67.037 1.00 83.41  ? 120  GLY B N   1 
ATOM   5546  C  CA  . GLY B  1  94  ? 12.861  -28.284 -66.945 1.00 82.23  ? 120  GLY B CA  1 
ATOM   5547  C  C   . GLY B  1  94  ? 12.349  -26.903 -66.587 1.00 82.11  ? 120  GLY B C   1 
ATOM   5548  O  O   . GLY B  1  94  ? 12.718  -25.904 -67.202 1.00 81.43  ? 120  GLY B O   1 
ATOM   5549  N  N   . ALA B  1  95  ? 11.492  -26.845 -65.578 1.00 82.42  ? 121  ALA B N   1 
ATOM   5550  C  CA  . ALA B  1  95  ? 10.909  -25.580 -65.148 1.00 82.31  ? 121  ALA B CA  1 
ATOM   5551  C  C   . ALA B  1  95  ? 11.927  -24.677 -64.471 1.00 81.75  ? 121  ALA B C   1 
ATOM   5552  O  O   . ALA B  1  95  ? 11.888  -23.457 -64.630 1.00 80.61  ? 121  ALA B O   1 
ATOM   5553  C  CB  . ALA B  1  95  ? 9.739   -25.842 -64.208 1.00 82.31  ? 121  ALA B CB  1 
ATOM   5554  N  N   . PHE B  1  96  ? 12.845  -25.284 -63.725 1.00 82.08  ? 122  PHE B N   1 
ATOM   5555  C  CA  . PHE B  1  96  ? 13.852  -24.520 -63.003 1.00 81.58  ? 122  PHE B CA  1 
ATOM   5556  C  C   . PHE B  1  96  ? 15.195  -24.369 -63.704 1.00 81.95  ? 122  PHE B C   1 
ATOM   5557  O  O   . PHE B  1  96  ? 16.224  -24.152 -63.061 1.00 81.62  ? 122  PHE B O   1 
ATOM   5558  C  CB  . PHE B  1  96  ? 14.036  -25.127 -61.621 1.00 79.60  ? 122  PHE B CB  1 
ATOM   5559  C  CG  . PHE B  1  96  ? 12.787  -25.120 -60.805 1.00 78.32  ? 122  PHE B CG  1 
ATOM   5560  C  CD1 . PHE B  1  96  ? 12.159  -23.918 -60.491 1.00 77.19  ? 122  PHE B CD1 1 
ATOM   5561  C  CD2 . PHE B  1  96  ? 12.224  -26.314 -60.366 1.00 78.00  ? 122  PHE B CD2 1 
ATOM   5562  C  CE1 . PHE B  1  96  ? 10.981  -23.897 -59.751 1.00 77.31  ? 122  PHE B CE1 1 
ATOM   5563  C  CE2 . PHE B  1  96  ? 11.046  -26.311 -59.624 1.00 78.15  ? 122  PHE B CE2 1 
ATOM   5564  C  CZ  . PHE B  1  96  ? 10.419  -25.094 -59.312 1.00 78.05  ? 122  PHE B CZ  1 
ATOM   5565  N  N   . SER B  1  97  ? 15.178  -24.463 -65.029 1.00 82.40  ? 123  SER B N   1 
ATOM   5566  C  CA  . SER B  1  97  ? 16.394  -24.317 -65.809 1.00 82.54  ? 123  SER B CA  1 
ATOM   5567  C  C   . SER B  1  97  ? 16.709  -22.825 -65.996 1.00 82.04  ? 123  SER B C   1 
ATOM   5568  O  O   . SER B  1  97  ? 15.823  -22.026 -66.332 1.00 81.40  ? 123  SER B O   1 
ATOM   5569  C  CB  . SER B  1  97  ? 16.233  -25.005 -67.172 1.00 83.47  ? 123  SER B CB  1 
ATOM   5570  O  OG  . SER B  1  97  ? 15.167  -24.436 -67.916 1.00 84.25  ? 123  SER B OG  1 
ATOM   5571  N  N   . GLY B  1  98  ? 17.973  -22.464 -65.770 1.00 81.17  ? 124  GLY B N   1 
ATOM   5572  C  CA  . GLY B  1  98  ? 18.406  -21.083 -65.908 1.00 78.66  ? 124  GLY B CA  1 
ATOM   5573  C  C   . GLY B  1  98  ? 18.853  -20.470 -64.593 1.00 77.49  ? 124  GLY B C   1 
ATOM   5574  O  O   . GLY B  1  98  ? 19.634  -19.515 -64.588 1.00 76.89  ? 124  GLY B O   1 
ATOM   5575  N  N   . LEU B  1  99  ? 18.351  -21.014 -63.481 1.00 76.38  ? 125  LEU B N   1 
ATOM   5576  C  CA  . LEU B  1  99  ? 18.687  -20.527 -62.139 1.00 75.03  ? 125  LEU B CA  1 
ATOM   5577  C  C   . LEU B  1  99  ? 20.023  -21.130 -61.700 1.00 74.88  ? 125  LEU B C   1 
ATOM   5578  O  O   . LEU B  1  99  ? 20.095  -21.951 -60.789 1.00 73.95  ? 125  LEU B O   1 
ATOM   5579  C  CB  . LEU B  1  99  ? 17.596  -20.912 -61.130 1.00 73.27  ? 125  LEU B CB  1 
ATOM   5580  C  CG  . LEU B  1  99  ? 16.128  -20.464 -61.193 1.00 70.60  ? 125  LEU B CG  1 
ATOM   5581  C  CD1 . LEU B  1  99  ? 15.997  -19.164 -61.944 1.00 69.49  ? 125  LEU B CD1 1 
ATOM   5582  C  CD2 . LEU B  1  99  ? 15.292  -21.544 -61.837 1.00 70.27  ? 125  LEU B CD2 1 
ATOM   5583  N  N   . SER B  1  100 ? 21.082  -20.712 -62.371 1.00 75.50  ? 126  SER B N   1 
ATOM   5584  C  CA  . SER B  1  100 ? 22.425  -21.194 -62.104 1.00 74.95  ? 126  SER B CA  1 
ATOM   5585  C  C   . SER B  1  100 ? 22.996  -20.669 -60.794 1.00 73.97  ? 126  SER B C   1 
ATOM   5586  O  O   . SER B  1  100 ? 24.110  -21.027 -60.418 1.00 73.07  ? 126  SER B O   1 
ATOM   5587  C  CB  . SER B  1  100 ? 23.334  -20.783 -63.269 1.00 75.91  ? 126  SER B CB  1 
ATOM   5588  O  OG  . SER B  1  100 ? 23.223  -19.387 -63.539 1.00 75.56  ? 126  SER B OG  1 
ATOM   5589  N  N   . SER B  1  101 ? 22.228  -19.828 -60.105 1.00 73.50  ? 127  SER B N   1 
ATOM   5590  C  CA  . SER B  1  101 ? 22.671  -19.229 -58.839 1.00 72.72  ? 127  SER B CA  1 
ATOM   5591  C  C   . SER B  1  101 ? 21.683  -19.412 -57.697 1.00 71.50  ? 127  SER B C   1 
ATOM   5592  O  O   . SER B  1  101 ? 21.838  -18.817 -56.634 1.00 70.53  ? 127  SER B O   1 
ATOM   5593  C  CB  . SER B  1  101 ? 22.904  -17.727 -59.020 1.00 72.34  ? 127  SER B CB  1 
ATOM   5594  O  OG  . SER B  1  101 ? 23.893  -17.497 -59.999 1.00 73.80  ? 127  SER B OG  1 
ATOM   5595  N  N   . LEU B  1  102 ? 20.663  -20.228 -57.914 1.00 71.06  ? 128  LEU B N   1 
ATOM   5596  C  CA  . LEU B  1  102 ? 19.654  -20.419 -56.880 1.00 69.58  ? 128  LEU B CA  1 
ATOM   5597  C  C   . LEU B  1  102 ? 20.219  -21.099 -55.653 1.00 69.14  ? 128  LEU B C   1 
ATOM   5598  O  O   . LEU B  1  102 ? 20.767  -22.197 -55.733 1.00 69.10  ? 128  LEU B O   1 
ATOM   5599  C  CB  . LEU B  1  102 ? 18.468  -21.235 -57.407 1.00 67.70  ? 128  LEU B CB  1 
ATOM   5600  C  CG  . LEU B  1  102 ? 17.155  -21.068 -56.641 1.00 64.13  ? 128  LEU B CG  1 
ATOM   5601  C  CD1 . LEU B  1  102 ? 16.631  -19.665 -56.851 1.00 61.33  ? 128  LEU B CD1 1 
ATOM   5602  C  CD2 . LEU B  1  102 ? 16.151  -22.094 -57.116 1.00 63.91  ? 128  LEU B CD2 1 
ATOM   5603  N  N   . GLN B  1  103 ? 20.072  -20.425 -54.515 1.00 68.76  ? 129  GLN B N   1 
ATOM   5604  C  CA  . GLN B  1  103 ? 20.534  -20.943 -53.234 1.00 68.00  ? 129  GLN B CA  1 
ATOM   5605  C  C   . GLN B  1  103 ? 19.366  -21.378 -52.334 1.00 66.01  ? 129  GLN B C   1 
ATOM   5606  O  O   . GLN B  1  103 ? 19.462  -22.365 -51.601 1.00 64.85  ? 129  GLN B O   1 
ATOM   5607  C  CB  . GLN B  1  103 ? 21.365  -19.880 -52.518 1.00 68.40  ? 129  GLN B CB  1 
ATOM   5608  C  CG  . GLN B  1  103 ? 22.605  -19.497 -53.270 1.00 71.68  ? 129  GLN B CG  1 
ATOM   5609  C  CD  . GLN B  1  103 ? 23.564  -18.690 -52.437 1.00 73.29  ? 129  GLN B CD  1 
ATOM   5610  O  OE1 . GLN B  1  103 ? 23.280  -17.548 -52.070 1.00 74.33  ? 129  GLN B OE1 1 
ATOM   5611  N  NE2 . GLN B  1  103 ? 24.713  -19.283 -52.125 1.00 74.30  ? 129  GLN B NE2 1 
ATOM   5612  N  N   . LYS B  1  104 ? 18.263  -20.639 -52.413 1.00 63.14  ? 130  LYS B N   1 
ATOM   5613  C  CA  . LYS B  1  104 ? 17.094  -20.918 -51.603 1.00 60.30  ? 130  LYS B CA  1 
ATOM   5614  C  C   . LYS B  1  104 ? 15.824  -21.141 -52.427 1.00 60.17  ? 130  LYS B C   1 
ATOM   5615  O  O   . LYS B  1  104 ? 15.378  -20.252 -53.158 1.00 60.12  ? 130  LYS B O   1 
ATOM   5616  C  CB  . LYS B  1  104 ? 16.893  -19.756 -50.641 1.00 58.01  ? 130  LYS B CB  1 
ATOM   5617  C  CG  . LYS B  1  104 ? 15.715  -19.875 -49.695 1.00 57.39  ? 130  LYS B CG  1 
ATOM   5618  C  CD  . LYS B  1  104 ? 15.671  -18.635 -48.812 1.00 57.26  ? 130  LYS B CD  1 
ATOM   5619  C  CE  . LYS B  1  104 ? 14.555  -18.656 -47.790 1.00 56.66  ? 130  LYS B CE  1 
ATOM   5620  N  NZ  . LYS B  1  104 ? 14.582  -17.387 -47.001 1.00 55.22  ? 130  LYS B NZ  1 
ATOM   5621  N  N   . LEU B  1  105 ? 15.239  -22.331 -52.308 1.00 59.56  ? 131  LEU B N   1 
ATOM   5622  C  CA  . LEU B  1  105 ? 14.001  -22.647 -53.027 1.00 58.90  ? 131  LEU B CA  1 
ATOM   5623  C  C   . LEU B  1  105 ? 12.893  -22.957 -52.021 1.00 59.00  ? 131  LEU B C   1 
ATOM   5624  O  O   . LEU B  1  105 ? 13.000  -23.911 -51.255 1.00 59.42  ? 131  LEU B O   1 
ATOM   5625  C  CB  . LEU B  1  105 ? 14.209  -23.849 -53.943 1.00 56.62  ? 131  LEU B CB  1 
ATOM   5626  C  CG  . LEU B  1  105 ? 12.959  -24.302 -54.689 1.00 54.99  ? 131  LEU B CG  1 
ATOM   5627  C  CD1 . LEU B  1  105 ? 12.429  -23.173 -55.561 1.00 52.91  ? 131  LEU B CD1 1 
ATOM   5628  C  CD2 . LEU B  1  105 ? 13.301  -25.534 -55.526 1.00 55.54  ? 131  LEU B CD2 1 
ATOM   5629  N  N   . VAL B  1  106 ? 11.836  -22.150 -52.022 1.00 58.51  ? 132  VAL B N   1 
ATOM   5630  C  CA  . VAL B  1  106 ? 10.731  -22.338 -51.090 1.00 57.75  ? 132  VAL B CA  1 
ATOM   5631  C  C   . VAL B  1  106 ? 9.476   -22.836 -51.803 1.00 59.19  ? 132  VAL B C   1 
ATOM   5632  O  O   . VAL B  1  106 ? 8.836   -22.086 -52.538 1.00 60.03  ? 132  VAL B O   1 
ATOM   5633  C  CB  . VAL B  1  106 ? 10.386  -21.017 -50.382 1.00 56.01  ? 132  VAL B CB  1 
ATOM   5634  C  CG1 . VAL B  1  106 ? 9.503   -21.283 -49.200 1.00 54.81  ? 132  VAL B CG1 1 
ATOM   5635  C  CG2 . VAL B  1  106 ? 11.644  -20.315 -49.953 1.00 55.30  ? 132  VAL B CG2 1 
ATOM   5636  N  N   . ALA B  1  107 ? 9.129   -24.102 -51.589 1.00 60.01  ? 133  ALA B N   1 
ATOM   5637  C  CA  . ALA B  1  107 ? 7.945   -24.691 -52.210 1.00 60.64  ? 133  ALA B CA  1 
ATOM   5638  C  C   . ALA B  1  107 ? 6.981   -25.232 -51.138 1.00 62.09  ? 133  ALA B C   1 
ATOM   5639  O  O   . ALA B  1  107 ? 6.501   -26.371 -51.230 1.00 62.28  ? 133  ALA B O   1 
ATOM   5640  C  CB  . ALA B  1  107 ? 8.360   -25.807 -53.163 1.00 58.33  ? 133  ALA B CB  1 
ATOM   5641  N  N   . VAL B  1  108 ? 6.696   -24.407 -50.130 1.00 62.25  ? 134  VAL B N   1 
ATOM   5642  C  CA  . VAL B  1  108 ? 5.805   -24.803 -49.046 1.00 62.65  ? 134  VAL B CA  1 
ATOM   5643  C  C   . VAL B  1  108 ? 4.375   -24.769 -49.536 1.00 64.14  ? 134  VAL B C   1 
ATOM   5644  O  O   . VAL B  1  108 ? 3.969   -23.801 -50.191 1.00 65.24  ? 134  VAL B O   1 
ATOM   5645  C  CB  . VAL B  1  108 ? 5.934   -23.860 -47.848 1.00 61.92  ? 134  VAL B CB  1 
ATOM   5646  C  CG1 . VAL B  1  108 ? 4.913   -24.223 -46.783 1.00 60.30  ? 134  VAL B CG1 1 
ATOM   5647  C  CG2 . VAL B  1  108 ? 7.335   -23.952 -47.285 1.00 61.71  ? 134  VAL B CG2 1 
ATOM   5648  N  N   . GLU B  1  109 ? 3.620   -25.821 -49.206 1.00 65.04  ? 135  GLU B N   1 
ATOM   5649  C  CA  . GLU B  1  109 ? 2.221   -25.960 -49.608 1.00 64.80  ? 135  GLU B CA  1 
ATOM   5650  C  C   . GLU B  1  109 ? 2.080   -25.643 -51.094 1.00 65.28  ? 135  GLU B C   1 
ATOM   5651  O  O   . GLU B  1  109 ? 1.481   -24.632 -51.472 1.00 64.49  ? 135  GLU B O   1 
ATOM   5652  C  CB  . GLU B  1  109 ? 1.312   -25.042 -48.774 1.00 64.78  ? 135  GLU B CB  1 
ATOM   5653  C  CG  . GLU B  1  109 ? -0.158  -25.119 -49.170 1.00 67.39  ? 135  GLU B CG  1 
ATOM   5654  C  CD  . GLU B  1  109 ? -1.123  -24.458 -48.177 1.00 68.01  ? 135  GLU B CD  1 
ATOM   5655  O  OE1 . GLU B  1  109 ? -0.862  -23.312 -47.749 1.00 68.88  ? 135  GLU B OE1 1 
ATOM   5656  O  OE2 . GLU B  1  109 ? -2.162  -25.083 -47.843 1.00 66.95  ? 135  GLU B OE2 1 
ATOM   5657  N  N   . THR B  1  110 ? 2.665   -26.512 -51.923 1.00 66.42  ? 136  THR B N   1 
ATOM   5658  C  CA  . THR B  1  110 ? 2.627   -26.382 -53.381 1.00 67.23  ? 136  THR B CA  1 
ATOM   5659  C  C   . THR B  1  110 ? 2.114   -27.676 -53.998 1.00 68.85  ? 136  THR B C   1 
ATOM   5660  O  O   . THR B  1  110 ? 2.460   -28.026 -55.129 1.00 69.99  ? 136  THR B O   1 
ATOM   5661  C  CB  . THR B  1  110 ? 4.022   -26.078 -53.994 1.00 66.29  ? 136  THR B CB  1 
ATOM   5662  O  OG1 . THR B  1  110 ? 4.977   -27.047 -53.549 1.00 66.57  ? 136  THR B OG1 1 
ATOM   5663  C  CG2 . THR B  1  110 ? 4.487   -24.695 -53.599 1.00 66.72  ? 136  THR B CG2 1 
ATOM   5664  N  N   . ASN B  1  111 ? 1.305   -28.396 -53.231 1.00 70.26  ? 137  ASN B N   1 
ATOM   5665  C  CA  . ASN B  1  111 ? 0.689   -29.636 -53.690 1.00 72.30  ? 137  ASN B CA  1 
ATOM   5666  C  C   . ASN B  1  111 ? 1.696   -30.717 -54.076 1.00 72.66  ? 137  ASN B C   1 
ATOM   5667  O  O   . ASN B  1  111 ? 1.330   -31.742 -54.657 1.00 73.54  ? 137  ASN B O   1 
ATOM   5668  C  CB  . ASN B  1  111 ? -0.216  -29.329 -54.883 1.00 73.75  ? 137  ASN B CB  1 
ATOM   5669  C  CG  . ASN B  1  111 ? -1.404  -30.248 -54.959 1.00 74.90  ? 137  ASN B CG  1 
ATOM   5670  O  OD1 . ASN B  1  111 ? -2.254  -30.253 -54.062 1.00 74.79  ? 137  ASN B OD1 1 
ATOM   5671  N  ND2 . ASN B  1  111 ? -1.479  -31.036 -56.035 1.00 75.97  ? 137  ASN B ND2 1 
ATOM   5672  N  N   . LEU B  1  112 ? 2.961   -30.488 -53.745 1.00 72.36  ? 138  LEU B N   1 
ATOM   5673  C  CA  . LEU B  1  112 ? 4.019   -31.432 -54.059 1.00 72.53  ? 138  LEU B CA  1 
ATOM   5674  C  C   . LEU B  1  112 ? 3.764   -32.782 -53.386 1.00 73.18  ? 138  LEU B C   1 
ATOM   5675  O  O   . LEU B  1  112 ? 3.701   -32.873 -52.158 1.00 72.62  ? 138  LEU B O   1 
ATOM   5676  C  CB  . LEU B  1  112 ? 5.346   -30.848 -53.597 1.00 72.71  ? 138  LEU B CB  1 
ATOM   5677  C  CG  . LEU B  1  112 ? 6.595   -31.250 -54.375 1.00 72.83  ? 138  LEU B CG  1 
ATOM   5678  C  CD1 . LEU B  1  112 ? 7.764   -30.425 -53.867 1.00 72.43  ? 138  LEU B CD1 1 
ATOM   5679  C  CD2 . LEU B  1  112 ? 6.859   -32.741 -54.216 1.00 72.91  ? 138  LEU B CD2 1 
ATOM   5680  N  N   . ALA B  1  113 ? 3.631   -33.832 -54.193 1.00 74.29  ? 139  ALA B N   1 
ATOM   5681  C  CA  . ALA B  1  113 ? 3.351   -35.168 -53.662 1.00 76.36  ? 139  ALA B CA  1 
ATOM   5682  C  C   . ALA B  1  113 ? 4.556   -36.105 -53.531 1.00 77.62  ? 139  ALA B C   1 
ATOM   5683  O  O   . ALA B  1  113 ? 4.509   -37.073 -52.768 1.00 77.78  ? 139  ALA B O   1 
ATOM   5684  C  CB  . ALA B  1  113 ? 2.263   -35.835 -54.503 1.00 75.72  ? 139  ALA B CB  1 
ATOM   5685  N  N   . SER B  1  114 ? 5.627   -35.835 -54.272 1.00 79.00  ? 140  SER B N   1 
ATOM   5686  C  CA  . SER B  1  114 ? 6.814   -36.681 -54.202 1.00 80.29  ? 140  SER B CA  1 
ATOM   5687  C  C   . SER B  1  114 ? 8.075   -35.913 -54.552 1.00 80.57  ? 140  SER B C   1 
ATOM   5688  O  O   . SER B  1  114 ? 8.107   -35.134 -55.500 1.00 81.21  ? 140  SER B O   1 
ATOM   5689  C  CB  . SER B  1  114 ? 6.677   -37.886 -55.141 1.00 81.59  ? 140  SER B CB  1 
ATOM   5690  O  OG  . SER B  1  114 ? 7.787   -38.767 -55.009 1.00 82.94  ? 140  SER B OG  1 
ATOM   5691  N  N   . LEU B  1  115 ? 9.118   -36.146 -53.775 1.00 80.96  ? 141  LEU B N   1 
ATOM   5692  C  CA  . LEU B  1  115 ? 10.394  -35.491 -53.980 1.00 81.70  ? 141  LEU B CA  1 
ATOM   5693  C  C   . LEU B  1  115 ? 11.058  -36.093 -55.223 1.00 82.83  ? 141  LEU B C   1 
ATOM   5694  O  O   . LEU B  1  115 ? 11.946  -35.486 -55.820 1.00 82.96  ? 141  LEU B O   1 
ATOM   5695  C  CB  . LEU B  1  115 ? 11.265  -35.728 -52.742 1.00 81.03  ? 141  LEU B CB  1 
ATOM   5696  C  CG  . LEU B  1  115 ? 12.212  -34.646 -52.234 1.00 79.48  ? 141  LEU B CG  1 
ATOM   5697  C  CD1 . LEU B  1  115 ? 11.444  -33.369 -51.951 1.00 79.29  ? 141  LEU B CD1 1 
ATOM   5698  C  CD2 . LEU B  1  115 ? 12.895  -35.152 -50.976 1.00 78.23  ? 141  LEU B CD2 1 
ATOM   5699  N  N   . GLU B  1  116 ? 10.604  -37.288 -55.604 1.00 84.21  ? 142  GLU B N   1 
ATOM   5700  C  CA  . GLU B  1  116 ? 11.133  -38.039 -56.747 1.00 84.30  ? 142  GLU B CA  1 
ATOM   5701  C  C   . GLU B  1  116 ? 11.126  -37.322 -58.077 1.00 83.21  ? 142  GLU B C   1 
ATOM   5702  O  O   . GLU B  1  116 ? 12.114  -37.331 -58.798 1.00 82.84  ? 142  GLU B O   1 
ATOM   5703  C  CB  . GLU B  1  116 ? 10.369  -39.358 -56.912 1.00 86.57  ? 142  GLU B CB  1 
ATOM   5704  C  CG  . GLU B  1  116 ? 10.798  -40.490 -55.977 1.00 89.82  ? 142  GLU B CG  1 
ATOM   5705  C  CD  . GLU B  1  116 ? 12.230  -40.946 -56.234 1.00 91.81  ? 142  GLU B CD  1 
ATOM   5706  O  OE1 . GLU B  1  116 ? 12.629  -40.997 -57.424 1.00 92.06  ? 142  GLU B OE1 1 
ATOM   5707  O  OE2 . GLU B  1  116 ? 12.942  -41.263 -55.249 1.00 92.10  ? 142  GLU B OE2 1 
ATOM   5708  N  N   . ASN B  1  117 ? 10.010  -36.701 -58.414 1.00 83.43  ? 143  ASN B N   1 
ATOM   5709  C  CA  . ASN B  1  117 ? 9.920   -36.026 -59.695 1.00 84.26  ? 143  ASN B CA  1 
ATOM   5710  C  C   . ASN B  1  117 ? 10.129  -34.518 -59.684 1.00 83.49  ? 143  ASN B C   1 
ATOM   5711  O  O   . ASN B  1  117 ? 9.945   -33.867 -60.706 1.00 84.13  ? 143  ASN B O   1 
ATOM   5712  C  CB  . ASN B  1  117 ? 8.582   -36.366 -60.358 1.00 86.42  ? 143  ASN B CB  1 
ATOM   5713  C  CG  . ASN B  1  117 ? 8.379   -37.873 -60.529 1.00 87.83  ? 143  ASN B CG  1 
ATOM   5714  O  OD1 . ASN B  1  117 ? 9.214   -38.558 -61.124 1.00 88.29  ? 143  ASN B OD1 1 
ATOM   5715  N  ND2 . ASN B  1  117 ? 7.265   -38.388 -60.012 1.00 87.78  ? 143  ASN B ND2 1 
ATOM   5716  N  N   . PHE B  1  118 ? 10.519  -33.962 -58.542 1.00 82.67  ? 144  PHE B N   1 
ATOM   5717  C  CA  . PHE B  1  118 ? 10.773  -32.523 -58.427 1.00 81.37  ? 144  PHE B CA  1 
ATOM   5718  C  C   . PHE B  1  118 ? 12.046  -32.214 -59.260 1.00 82.12  ? 144  PHE B C   1 
ATOM   5719  O  O   . PHE B  1  118 ? 13.153  -32.619 -58.900 1.00 83.19  ? 144  PHE B O   1 
ATOM   5720  C  CB  . PHE B  1  118 ? 10.963  -32.174 -56.942 1.00 78.40  ? 144  PHE B CB  1 
ATOM   5721  C  CG  . PHE B  1  118 ? 10.603  -30.756 -56.589 1.00 76.08  ? 144  PHE B CG  1 
ATOM   5722  C  CD1 . PHE B  1  118 ? 9.442   -30.168 -57.083 1.00 74.80  ? 144  PHE B CD1 1 
ATOM   5723  C  CD2 . PHE B  1  118 ? 11.417  -30.011 -55.743 1.00 75.18  ? 144  PHE B CD2 1 
ATOM   5724  C  CE1 . PHE B  1  118 ? 9.099   -28.856 -56.741 1.00 72.85  ? 144  PHE B CE1 1 
ATOM   5725  C  CE2 . PHE B  1  118 ? 11.083  -28.702 -55.395 1.00 73.66  ? 144  PHE B CE2 1 
ATOM   5726  C  CZ  . PHE B  1  118 ? 9.921   -28.123 -55.896 1.00 72.45  ? 144  PHE B CZ  1 
ATOM   5727  N  N   . PRO B  1  119 ? 11.899  -31.489 -60.387 1.00 81.97  ? 145  PRO B N   1 
ATOM   5728  C  CA  . PRO B  1  119 ? 13.010  -31.133 -61.287 1.00 81.92  ? 145  PRO B CA  1 
ATOM   5729  C  C   . PRO B  1  119 ? 14.044  -30.112 -60.809 1.00 81.58  ? 145  PRO B C   1 
ATOM   5730  O  O   . PRO B  1  119 ? 14.169  -29.037 -61.400 1.00 82.07  ? 145  PRO B O   1 
ATOM   5731  C  CB  . PRO B  1  119 ? 12.283  -30.647 -62.529 1.00 81.69  ? 145  PRO B CB  1 
ATOM   5732  C  CG  . PRO B  1  119 ? 11.133  -29.898 -61.920 1.00 81.82  ? 145  PRO B CG  1 
ATOM   5733  C  CD  . PRO B  1  119 ? 10.649  -30.848 -60.836 1.00 81.40  ? 145  PRO B CD  1 
ATOM   5734  N  N   . ILE B  1  120 ? 14.804  -30.462 -59.775 1.00 80.56  ? 146  ILE B N   1 
ATOM   5735  C  CA  . ILE B  1  120 ? 15.817  -29.559 -59.216 1.00 79.92  ? 146  ILE B CA  1 
ATOM   5736  C  C   . ILE B  1  120 ? 17.234  -30.146 -59.207 1.00 79.73  ? 146  ILE B C   1 
ATOM   5737  O  O   . ILE B  1  120 ? 18.196  -29.441 -58.876 1.00 79.19  ? 146  ILE B O   1 
ATOM   5738  C  CB  . ILE B  1  120 ? 15.480  -29.171 -57.745 1.00 79.82  ? 146  ILE B CB  1 
ATOM   5739  C  CG1 . ILE B  1  120 ? 15.160  -30.437 -56.940 1.00 78.76  ? 146  ILE B CG1 1 
ATOM   5740  C  CG2 . ILE B  1  120 ? 14.330  -28.169 -57.702 1.00 78.41  ? 146  ILE B CG2 1 
ATOM   5741  C  CD1 . ILE B  1  120 ? 15.060  -30.206 -55.465 1.00 78.06  ? 146  ILE B CD1 1 
ATOM   5742  N  N   . GLY B  1  121 ? 17.345  -31.427 -59.561 1.00 78.69  ? 147  GLY B N   1 
ATOM   5743  C  CA  . GLY B  1  121 ? 18.625  -32.122 -59.559 1.00 76.74  ? 147  GLY B CA  1 
ATOM   5744  C  C   . GLY B  1  121 ? 19.842  -31.469 -60.191 1.00 76.27  ? 147  GLY B C   1 
ATOM   5745  O  O   . GLY B  1  121 ? 20.946  -31.991 -60.065 1.00 74.72  ? 147  GLY B O   1 
ATOM   5746  N  N   . HIS B  1  122 ? 19.661  -30.340 -60.867 1.00 77.28  ? 148  HIS B N   1 
ATOM   5747  C  CA  . HIS B  1  122 ? 20.779  -29.656 -61.513 1.00 78.17  ? 148  HIS B CA  1 
ATOM   5748  C  C   . HIS B  1  122 ? 21.224  -28.380 -60.802 1.00 78.34  ? 148  HIS B C   1 
ATOM   5749  O  O   . HIS B  1  122 ? 22.256  -27.799 -61.140 1.00 78.63  ? 148  HIS B O   1 
ATOM   5750  C  CB  . HIS B  1  122 ? 20.421  -29.308 -62.954 1.00 78.30  ? 148  HIS B CB  1 
ATOM   5751  C  CG  . HIS B  1  122 ? 19.236  -28.406 -63.078 1.00 78.96  ? 148  HIS B CG  1 
ATOM   5752  N  ND1 . HIS B  1  122 ? 17.940  -28.863 -62.975 1.00 80.37  ? 148  HIS B ND1 1 
ATOM   5753  C  CD2 . HIS B  1  122 ? 19.152  -27.071 -63.280 1.00 78.93  ? 148  HIS B CD2 1 
ATOM   5754  C  CE1 . HIS B  1  122 ? 17.107  -27.846 -63.111 1.00 80.57  ? 148  HIS B CE1 1 
ATOM   5755  N  NE2 . HIS B  1  122 ? 17.818  -26.747 -63.297 1.00 80.28  ? 148  HIS B NE2 1 
ATOM   5756  N  N   . LEU B  1  123 ? 20.440  -27.942 -59.823 1.00 78.57  ? 149  LEU B N   1 
ATOM   5757  C  CA  . LEU B  1  123 ? 20.754  -26.739 -59.061 1.00 78.44  ? 149  LEU B CA  1 
ATOM   5758  C  C   . LEU B  1  123 ? 21.814  -27.078 -58.008 1.00 78.92  ? 149  LEU B C   1 
ATOM   5759  O  O   . LEU B  1  123 ? 21.497  -27.337 -56.849 1.00 79.02  ? 149  LEU B O   1 
ATOM   5760  C  CB  . LEU B  1  123 ? 19.477  -26.227 -58.402 1.00 78.55  ? 149  LEU B CB  1 
ATOM   5761  C  CG  . LEU B  1  123 ? 18.286  -26.016 -59.349 1.00 77.94  ? 149  LEU B CG  1 
ATOM   5762  C  CD1 . LEU B  1  123 ? 16.996  -25.938 -58.556 1.00 78.45  ? 149  LEU B CD1 1 
ATOM   5763  C  CD2 . LEU B  1  123 ? 18.488  -24.757 -60.166 1.00 76.80  ? 149  LEU B CD2 1 
ATOM   5764  N  N   . LYS B  1  124 ? 23.078  -27.068 -58.425 1.00 79.43  ? 150  LYS B N   1 
ATOM   5765  C  CA  . LYS B  1  124 ? 24.194  -27.414 -57.544 1.00 78.90  ? 150  LYS B CA  1 
ATOM   5766  C  C   . LYS B  1  124 ? 24.446  -26.384 -56.450 1.00 77.58  ? 150  LYS B C   1 
ATOM   5767  O  O   . LYS B  1  124 ? 24.937  -26.726 -55.370 1.00 77.27  ? 150  LYS B O   1 
ATOM   5768  C  CB  . LYS B  1  124 ? 25.475  -27.610 -58.370 1.00 80.63  ? 150  LYS B CB  1 
ATOM   5769  C  CG  . LYS B  1  124 ? 26.146  -26.310 -58.817 1.00 83.25  ? 150  LYS B CG  1 
ATOM   5770  C  CD  . LYS B  1  124 ? 26.875  -26.439 -60.163 1.00 85.92  ? 150  LYS B CD  1 
ATOM   5771  C  CE  . LYS B  1  124 ? 25.898  -26.422 -61.360 1.00 87.69  ? 150  LYS B CE  1 
ATOM   5772  N  NZ  . LYS B  1  124 ? 25.061  -25.173 -61.441 1.00 88.43  ? 150  LYS B NZ  1 
ATOM   5773  N  N   . THR B  1  125 ? 24.105  -25.130 -56.724 1.00 75.64  ? 151  THR B N   1 
ATOM   5774  C  CA  . THR B  1  125 ? 24.316  -24.058 -55.752 1.00 75.63  ? 151  THR B CA  1 
ATOM   5775  C  C   . THR B  1  125 ? 23.287  -23.987 -54.615 1.00 75.21  ? 151  THR B C   1 
ATOM   5776  O  O   . THR B  1  125 ? 23.441  -23.196 -53.678 1.00 74.37  ? 151  THR B O   1 
ATOM   5777  C  CB  . THR B  1  125 ? 24.329  -22.694 -56.446 1.00 74.95  ? 151  THR B CB  1 
ATOM   5778  O  OG1 . THR B  1  125 ? 23.077  -22.486 -57.109 1.00 75.31  ? 151  THR B OG1 1 
ATOM   5779  C  CG2 . THR B  1  125 ? 25.456  -22.626 -57.451 1.00 74.33  ? 151  THR B CG2 1 
ATOM   5780  N  N   . LEU B  1  126 ? 22.252  -24.820 -54.707 1.00 74.46  ? 152  LEU B N   1 
ATOM   5781  C  CA  . LEU B  1  126 ? 21.160  -24.869 -53.733 1.00 71.79  ? 152  LEU B CA  1 
ATOM   5782  C  C   . LEU B  1  126 ? 21.639  -25.120 -52.308 1.00 71.48  ? 152  LEU B C   1 
ATOM   5783  O  O   . LEU B  1  126 ? 22.164  -26.192 -52.013 1.00 71.92  ? 152  LEU B O   1 
ATOM   5784  C  CB  . LEU B  1  126 ? 20.168  -25.965 -54.142 1.00 70.16  ? 152  LEU B CB  1 
ATOM   5785  C  CG  . LEU B  1  126 ? 18.764  -25.933 -53.545 1.00 69.22  ? 152  LEU B CG  1 
ATOM   5786  C  CD1 . LEU B  1  126 ? 18.042  -24.673 -54.013 1.00 67.50  ? 152  LEU B CD1 1 
ATOM   5787  C  CD2 . LEU B  1  126 ? 18.005  -27.191 -53.961 1.00 67.83  ? 152  LEU B CD2 1 
ATOM   5788  N  N   . LYS B  1  127 ? 21.444  -24.132 -51.432 1.00 70.87  ? 153  LYS B N   1 
ATOM   5789  C  CA  . LYS B  1  127 ? 21.835  -24.234 -50.027 1.00 70.33  ? 153  LYS B CA  1 
ATOM   5790  C  C   . LYS B  1  127 ? 20.690  -24.774 -49.175 1.00 69.61  ? 153  LYS B C   1 
ATOM   5791  O  O   . LYS B  1  127 ? 20.892  -25.646 -48.330 1.00 70.28  ? 153  LYS B O   1 
ATOM   5792  C  CB  . LYS B  1  127 ? 22.242  -22.873 -49.471 1.00 71.92  ? 153  LYS B CB  1 
ATOM   5793  C  CG  . LYS B  1  127 ? 23.453  -22.248 -50.116 1.00 76.47  ? 153  LYS B CG  1 
ATOM   5794  C  CD  . LYS B  1  127 ? 23.868  -20.982 -49.374 1.00 79.38  ? 153  LYS B CD  1 
ATOM   5795  C  CE  . LYS B  1  127 ? 24.518  -21.323 -48.039 1.00 82.03  ? 153  LYS B CE  1 
ATOM   5796  N  NZ  . LYS B  1  127 ? 25.746  -22.171 -48.240 1.00 83.86  ? 153  LYS B NZ  1 
ATOM   5797  N  N   . GLU B  1  128 ? 19.488  -24.243 -49.385 1.00 68.37  ? 154  GLU B N   1 
ATOM   5798  C  CA  . GLU B  1  128 ? 18.319  -24.689 -48.633 1.00 66.08  ? 154  GLU B CA  1 
ATOM   5799  C  C   . GLU B  1  128 ? 17.063  -24.945 -49.482 1.00 63.35  ? 154  GLU B C   1 
ATOM   5800  O  O   . GLU B  1  128 ? 16.712  -24.174 -50.369 1.00 62.39  ? 154  GLU B O   1 
ATOM   5801  C  CB  . GLU B  1  128 ? 18.023  -23.697 -47.506 1.00 68.18  ? 154  GLU B CB  1 
ATOM   5802  C  CG  . GLU B  1  128 ? 17.620  -22.288 -47.938 1.00 70.24  ? 154  GLU B CG  1 
ATOM   5803  C  CD  . GLU B  1  128 ? 17.504  -21.338 -46.737 1.00 71.95  ? 154  GLU B CD  1 
ATOM   5804  O  OE1 . GLU B  1  128 ? 18.550  -21.106 -46.082 1.00 72.80  ? 154  GLU B OE1 1 
ATOM   5805  O  OE2 . GLU B  1  128 ? 16.384  -20.837 -46.447 1.00 69.50  ? 154  GLU B OE2 1 
ATOM   5806  N  N   . LEU B  1  129 ? 16.398  -26.053 -49.192 1.00 61.78  ? 155  LEU B N   1 
ATOM   5807  C  CA  . LEU B  1  129 ? 15.205  -26.466 -49.912 1.00 60.79  ? 155  LEU B CA  1 
ATOM   5808  C  C   . LEU B  1  129 ? 14.076  -26.717 -48.913 1.00 60.87  ? 155  LEU B C   1 
ATOM   5809  O  O   . LEU B  1  129 ? 14.111  -27.685 -48.152 1.00 60.91  ? 155  LEU B O   1 
ATOM   5810  C  CB  . LEU B  1  129 ? 15.537  -27.736 -50.707 1.00 60.44  ? 155  LEU B CB  1 
ATOM   5811  C  CG  . LEU B  1  129 ? 14.583  -28.390 -51.709 1.00 59.51  ? 155  LEU B CG  1 
ATOM   5812  C  CD1 . LEU B  1  129 ? 13.823  -29.482 -51.009 1.00 59.76  ? 155  LEU B CD1 1 
ATOM   5813  C  CD2 . LEU B  1  129 ? 13.659  -27.354 -52.341 1.00 58.11  ? 155  LEU B CD2 1 
ATOM   5814  N  N   . ASN B  1  130 ? 13.082  -25.827 -48.919 1.00 60.63  ? 156  ASN B N   1 
ATOM   5815  C  CA  . ASN B  1  130 ? 11.932  -25.909 -48.015 1.00 60.40  ? 156  ASN B CA  1 
ATOM   5816  C  C   . ASN B  1  130 ? 10.670  -26.443 -48.703 1.00 61.05  ? 156  ASN B C   1 
ATOM   5817  O  O   . ASN B  1  130 ? 10.042  -25.745 -49.504 1.00 60.77  ? 156  ASN B O   1 
ATOM   5818  C  CB  . ASN B  1  130 ? 11.633  -24.528 -47.432 1.00 59.92  ? 156  ASN B CB  1 
ATOM   5819  C  CG  . ASN B  1  130 ? 10.562  -24.566 -46.348 1.00 61.44  ? 156  ASN B CG  1 
ATOM   5820  O  OD1 . ASN B  1  130 ? 10.216  -23.536 -45.767 1.00 59.41  ? 156  ASN B OD1 1 
ATOM   5821  N  ND2 . ASN B  1  130 ? 10.033  -25.756 -46.074 1.00 60.94  ? 156  ASN B ND2 1 
ATOM   5822  N  N   . VAL B  1  131 ? 10.294  -27.675 -48.376 1.00 60.90  ? 157  VAL B N   1 
ATOM   5823  C  CA  . VAL B  1  131 ? 9.117   -28.293 -48.967 1.00 60.59  ? 157  VAL B CA  1 
ATOM   5824  C  C   . VAL B  1  131 ? 8.174   -28.788 -47.878 1.00 61.19  ? 157  VAL B C   1 
ATOM   5825  O  O   . VAL B  1  131 ? 7.695   -29.923 -47.933 1.00 60.69  ? 157  VAL B O   1 
ATOM   5826  C  CB  . VAL B  1  131 ? 9.514   -29.470 -49.882 1.00 60.02  ? 157  VAL B CB  1 
ATOM   5827  C  CG1 . VAL B  1  131 ? 10.197  -28.932 -51.124 1.00 57.98  ? 157  VAL B CG1 1 
ATOM   5828  C  CG2 . VAL B  1  131 ? 10.443  -30.433 -49.140 1.00 59.32  ? 157  VAL B CG2 1 
ATOM   5829  N  N   . ALA B  1  132 ? 7.912   -27.928 -46.894 1.00 61.81  ? 158  ALA B N   1 
ATOM   5830  C  CA  . ALA B  1  132 ? 7.033   -28.265 -45.778 1.00 62.77  ? 158  ALA B CA  1 
ATOM   5831  C  C   . ALA B  1  132 ? 5.580   -28.010 -46.125 1.00 63.81  ? 158  ALA B C   1 
ATOM   5832  O  O   . ALA B  1  132 ? 5.277   -27.201 -47.006 1.00 63.16  ? 158  ALA B O   1 
ATOM   5833  C  CB  . ALA B  1  132 ? 7.412   -27.459 -44.557 1.00 61.99  ? 158  ALA B CB  1 
ATOM   5834  N  N   . HIS B  1  133 ? 4.688   -28.706 -45.423 1.00 64.93  ? 159  HIS B N   1 
ATOM   5835  C  CA  . HIS B  1  133 ? 3.248   -28.576 -45.639 1.00 65.45  ? 159  HIS B CA  1 
ATOM   5836  C  C   . HIS B  1  133 ? 2.875   -29.113 -47.027 1.00 64.81  ? 159  HIS B C   1 
ATOM   5837  O  O   . HIS B  1  133 ? 2.215   -28.434 -47.812 1.00 64.28  ? 159  HIS B O   1 
ATOM   5838  C  CB  . HIS B  1  133 ? 2.839   -27.106 -45.506 1.00 66.01  ? 159  HIS B CB  1 
ATOM   5839  C  CG  . HIS B  1  133 ? 1.387   -26.894 -45.214 1.00 68.27  ? 159  HIS B CG  1 
ATOM   5840  N  ND1 . HIS B  1  133 ? 0.829   -25.636 -45.106 1.00 69.84  ? 159  HIS B ND1 1 
ATOM   5841  C  CD2 . HIS B  1  133 ? 0.378   -27.771 -45.004 1.00 69.36  ? 159  HIS B CD2 1 
ATOM   5842  C  CE1 . HIS B  1  133 ? -0.461  -25.748 -44.843 1.00 69.14  ? 159  HIS B CE1 1 
ATOM   5843  N  NE2 . HIS B  1  133 ? -0.761  -27.033 -44.776 1.00 70.08  ? 159  HIS B NE2 1 
ATOM   5844  N  N   . ASN B  1  134 ? 3.309   -30.337 -47.315 1.00 63.80  ? 160  ASN B N   1 
ATOM   5845  C  CA  . ASN B  1  134 ? 3.033   -30.979 -48.586 1.00 64.96  ? 160  ASN B CA  1 
ATOM   5846  C  C   . ASN B  1  134 ? 2.614   -32.441 -48.416 1.00 66.67  ? 160  ASN B C   1 
ATOM   5847  O  O   . ASN B  1  134 ? 2.612   -32.966 -47.301 1.00 68.96  ? 160  ASN B O   1 
ATOM   5848  C  CB  . ASN B  1  134 ? 4.245   -30.862 -49.495 1.00 65.79  ? 160  ASN B CB  1 
ATOM   5849  C  CG  . ASN B  1  134 ? 4.377   -29.474 -50.112 1.00 67.36  ? 160  ASN B CG  1 
ATOM   5850  O  OD1 . ASN B  1  134 ? 3.593   -29.092 -50.985 1.00 67.93  ? 160  ASN B OD1 1 
ATOM   5851  N  ND2 . ASN B  1  134 ? 5.366   -28.713 -49.657 1.00 67.32  ? 160  ASN B ND2 1 
ATOM   5852  N  N   . LEU B  1  135 ? 2.288   -33.104 -49.524 1.00 66.77  ? 161  LEU B N   1 
ATOM   5853  C  CA  . LEU B  1  135 ? 1.780   -34.479 -49.495 1.00 67.32  ? 161  LEU B CA  1 
ATOM   5854  C  C   . LEU B  1  135 ? 2.780   -35.635 -49.587 1.00 68.24  ? 161  LEU B C   1 
ATOM   5855  O  O   . LEU B  1  135 ? 2.411   -36.761 -49.952 1.00 69.37  ? 161  LEU B O   1 
ATOM   5856  C  CB  . LEU B  1  135 ? 0.749   -34.618 -50.613 1.00 66.60  ? 161  LEU B CB  1 
ATOM   5857  C  CG  . LEU B  1  135 ? -0.175  -33.405 -50.714 1.00 65.06  ? 161  LEU B CG  1 
ATOM   5858  C  CD1 . LEU B  1  135 ? -0.808  -33.338 -52.091 1.00 65.84  ? 161  LEU B CD1 1 
ATOM   5859  C  CD2 . LEU B  1  135 ? -1.211  -33.482 -49.624 1.00 64.29  ? 161  LEU B CD2 1 
ATOM   5860  N  N   . ILE B  1  136 ? 4.035   -35.373 -49.253 1.00 67.71  ? 162  ILE B N   1 
ATOM   5861  C  CA  . ILE B  1  136 ? 5.063   -36.402 -49.324 1.00 67.42  ? 162  ILE B CA  1 
ATOM   5862  C  C   . ILE B  1  136 ? 4.836   -37.534 -48.326 1.00 68.53  ? 162  ILE B C   1 
ATOM   5863  O  O   . ILE B  1  136 ? 4.587   -37.287 -47.149 1.00 68.67  ? 162  ILE B O   1 
ATOM   5864  C  CB  . ILE B  1  136 ? 6.440   -35.760 -49.111 1.00 66.57  ? 162  ILE B CB  1 
ATOM   5865  C  CG1 . ILE B  1  136 ? 6.694   -34.769 -50.247 1.00 64.38  ? 162  ILE B CG1 1 
ATOM   5866  C  CG2 . ILE B  1  136 ? 7.526   -36.823 -49.017 1.00 66.03  ? 162  ILE B CG2 1 
ATOM   5867  C  CD1 . ILE B  1  136 ? 7.993   -34.027 -50.127 1.00 64.92  ? 162  ILE B CD1 1 
ATOM   5868  N  N   . GLN B  1  137 ? 4.923   -38.775 -48.803 1.00 69.86  ? 163  GLN B N   1 
ATOM   5869  C  CA  . GLN B  1  137 ? 4.708   -39.951 -47.952 1.00 71.77  ? 163  GLN B CA  1 
ATOM   5870  C  C   . GLN B  1  137 ? 5.949   -40.783 -47.674 1.00 72.46  ? 163  GLN B C   1 
ATOM   5871  O  O   . GLN B  1  137 ? 5.990   -41.558 -46.713 1.00 71.43  ? 163  GLN B O   1 
ATOM   5872  C  CB  . GLN B  1  137 ? 3.676   -40.869 -48.580 1.00 72.53  ? 163  GLN B CB  1 
ATOM   5873  C  CG  . GLN B  1  137 ? 2.261   -40.537 -48.231 1.00 75.62  ? 163  GLN B CG  1 
ATOM   5874  C  CD  . GLN B  1  137 ? 1.315   -40.985 -49.314 1.00 77.49  ? 163  GLN B CD  1 
ATOM   5875  O  OE1 . GLN B  1  137 ? 1.337   -40.443 -50.429 1.00 77.55  ? 163  GLN B OE1 1 
ATOM   5876  N  NE2 . GLN B  1  137 ? 0.487   -41.989 -49.009 1.00 76.69  ? 163  GLN B NE2 1 
ATOM   5877  N  N   . SER B  1  138 ? 6.957   -40.630 -48.523 1.00 73.81  ? 164  SER B N   1 
ATOM   5878  C  CA  . SER B  1  138 ? 8.187   -41.389 -48.375 1.00 75.11  ? 164  SER B CA  1 
ATOM   5879  C  C   . SER B  1  138 ? 9.358   -40.506 -47.989 1.00 76.03  ? 164  SER B C   1 
ATOM   5880  O  O   . SER B  1  138 ? 9.406   -39.332 -48.362 1.00 74.69  ? 164  SER B O   1 
ATOM   5881  C  CB  . SER B  1  138 ? 8.500   -42.105 -49.686 1.00 75.17  ? 164  SER B CB  1 
ATOM   5882  O  OG  . SER B  1  138 ? 9.693   -42.858 -49.584 1.00 76.06  ? 164  SER B OG  1 
ATOM   5883  N  N   . PHE B  1  139 ? 10.299  -41.080 -47.241 1.00 78.27  ? 165  PHE B N   1 
ATOM   5884  C  CA  . PHE B  1  139 ? 11.495  -40.344 -46.825 1.00 80.58  ? 165  PHE B CA  1 
ATOM   5885  C  C   . PHE B  1  139 ? 12.667  -40.676 -47.755 1.00 81.79  ? 165  PHE B C   1 
ATOM   5886  O  O   . PHE B  1  139 ? 13.747  -40.091 -47.656 1.00 82.19  ? 165  PHE B O   1 
ATOM   5887  C  CB  . PHE B  1  139 ? 11.888  -40.687 -45.381 1.00 80.01  ? 165  PHE B CB  1 
ATOM   5888  C  CG  . PHE B  1  139 ? 13.069  -39.895 -44.872 1.00 80.23  ? 165  PHE B CG  1 
ATOM   5889  C  CD1 . PHE B  1  139 ? 14.053  -40.508 -44.096 1.00 80.27  ? 165  PHE B CD1 1 
ATOM   5890  C  CD2 . PHE B  1  139 ? 13.204  -38.537 -45.177 1.00 80.49  ? 165  PHE B CD2 1 
ATOM   5891  C  CE1 . PHE B  1  139 ? 15.155  -39.787 -43.631 1.00 79.49  ? 165  PHE B CE1 1 
ATOM   5892  C  CE2 . PHE B  1  139 ? 14.308  -37.802 -44.715 1.00 80.61  ? 165  PHE B CE2 1 
ATOM   5893  C  CZ  . PHE B  1  139 ? 15.284  -38.431 -43.940 1.00 79.41  ? 165  PHE B CZ  1 
ATOM   5894  N  N   . LYS B  1  140 ? 12.446  -41.622 -48.661 1.00 83.24  ? 166  LYS B N   1 
ATOM   5895  C  CA  . LYS B  1  140 ? 13.478  -42.039 -49.603 1.00 84.14  ? 166  LYS B CA  1 
ATOM   5896  C  C   . LYS B  1  140 ? 13.942  -40.853 -50.456 1.00 84.12  ? 166  LYS B C   1 
ATOM   5897  O  O   . LYS B  1  140 ? 13.248  -40.427 -51.386 1.00 82.96  ? 166  LYS B O   1 
ATOM   5898  C  CB  . LYS B  1  140 ? 12.939  -43.181 -50.485 1.00 85.22  ? 166  LYS B CB  1 
ATOM   5899  C  CG  . LYS B  1  140 ? 13.949  -43.801 -51.452 1.00 86.94  ? 166  LYS B CG  1 
ATOM   5900  C  CD  . LYS B  1  140 ? 13.395  -45.074 -52.088 1.00 86.95  ? 166  LYS B CD  1 
ATOM   5901  C  CE  . LYS B  1  140 ? 14.105  -45.392 -53.399 1.00 86.73  ? 166  LYS B CE  1 
ATOM   5902  N  NZ  . LYS B  1  140 ? 13.979  -44.256 -54.360 1.00 84.91  ? 166  LYS B NZ  1 
ATOM   5903  N  N   . LEU B  1  141 ? 15.118  -40.324 -50.119 1.00 84.87  ? 167  LEU B N   1 
ATOM   5904  C  CA  . LEU B  1  141 ? 15.704  -39.187 -50.837 1.00 85.09  ? 167  LEU B CA  1 
ATOM   5905  C  C   . LEU B  1  141 ? 16.027  -39.581 -52.270 1.00 84.72  ? 167  LEU B C   1 
ATOM   5906  O  O   . LEU B  1  141 ? 16.551  -40.664 -52.515 1.00 85.71  ? 167  LEU B O   1 
ATOM   5907  C  CB  . LEU B  1  141 ? 16.978  -38.712 -50.134 1.00 84.93  ? 167  LEU B CB  1 
ATOM   5908  C  CG  . LEU B  1  141 ? 16.790  -38.045 -48.763 1.00 84.98  ? 167  LEU B CG  1 
ATOM   5909  C  CD1 . LEU B  1  141 ? 18.125  -37.912 -48.069 1.00 83.92  ? 167  LEU B CD1 1 
ATOM   5910  C  CD2 . LEU B  1  141 ? 16.127  -36.677 -48.936 1.00 83.88  ? 167  LEU B CD2 1 
ATOM   5911  N  N   . PRO B  1  142 ? 15.710  -38.707 -53.237 1.00 83.99  ? 168  PRO B N   1 
ATOM   5912  C  CA  . PRO B  1  142 ? 15.981  -39.011 -54.642 1.00 84.17  ? 168  PRO B CA  1 
ATOM   5913  C  C   . PRO B  1  142 ? 17.464  -39.188 -54.933 1.00 84.36  ? 168  PRO B C   1 
ATOM   5914  O  O   . PRO B  1  142 ? 18.313  -38.765 -54.151 1.00 83.40  ? 168  PRO B O   1 
ATOM   5915  C  CB  . PRO B  1  142 ? 15.384  -37.811 -55.373 1.00 83.47  ? 168  PRO B CB  1 
ATOM   5916  C  CG  . PRO B  1  142 ? 14.279  -37.383 -54.484 1.00 83.05  ? 168  PRO B CG  1 
ATOM   5917  C  CD  . PRO B  1  142 ? 14.928  -37.467 -53.123 1.00 83.51  ? 168  PRO B CD  1 
ATOM   5918  N  N   . GLU B  1  143 ? 17.771  -39.812 -56.066 1.00 85.30  ? 169  GLU B N   1 
ATOM   5919  C  CA  . GLU B  1  143 ? 19.156  -40.034 -56.453 1.00 85.75  ? 169  GLU B CA  1 
ATOM   5920  C  C   . GLU B  1  143 ? 19.838  -38.728 -56.824 1.00 85.06  ? 169  GLU B C   1 
ATOM   5921  O  O   . GLU B  1  143 ? 21.022  -38.548 -56.555 1.00 84.47  ? 169  GLU B O   1 
ATOM   5922  C  CB  . GLU B  1  143 ? 19.241  -40.994 -57.641 1.00 87.45  ? 169  GLU B CB  1 
ATOM   5923  C  CG  . GLU B  1  143 ? 19.049  -42.459 -57.292 1.00 90.40  ? 169  GLU B CG  1 
ATOM   5924  C  CD  . GLU B  1  143 ? 19.997  -42.930 -56.193 1.00 92.46  ? 169  GLU B CD  1 
ATOM   5925  O  OE1 . GLU B  1  143 ? 19.688  -42.709 -55.000 1.00 92.79  ? 169  GLU B OE1 1 
ATOM   5926  O  OE2 . GLU B  1  143 ? 21.059  -43.515 -56.521 1.00 93.77  ? 169  GLU B OE2 1 
ATOM   5927  N  N   . TYR B  1  144 ? 19.089  -37.815 -57.433 1.00 85.03  ? 170  TYR B N   1 
ATOM   5928  C  CA  . TYR B  1  144 ? 19.663  -36.544 -57.843 1.00 85.49  ? 170  TYR B CA  1 
ATOM   5929  C  C   . TYR B  1  144 ? 20.253  -35.732 -56.696 1.00 85.92  ? 170  TYR B C   1 
ATOM   5930  O  O   . TYR B  1  144 ? 20.929  -34.734 -56.921 1.00 85.26  ? 170  TYR B O   1 
ATOM   5931  C  CB  . TYR B  1  144 ? 18.632  -35.715 -58.624 1.00 85.19  ? 170  TYR B CB  1 
ATOM   5932  C  CG  . TYR B  1  144 ? 17.442  -35.220 -57.833 1.00 85.81  ? 170  TYR B CG  1 
ATOM   5933  C  CD1 . TYR B  1  144 ? 17.581  -34.226 -56.858 1.00 86.39  ? 170  TYR B CD1 1 
ATOM   5934  C  CD2 . TYR B  1  144 ? 16.168  -35.728 -58.077 1.00 85.60  ? 170  TYR B CD2 1 
ATOM   5935  C  CE1 . TYR B  1  144 ? 16.482  -33.750 -56.152 1.00 85.69  ? 170  TYR B CE1 1 
ATOM   5936  C  CE2 . TYR B  1  144 ? 15.066  -35.259 -57.374 1.00 85.85  ? 170  TYR B CE2 1 
ATOM   5937  C  CZ  . TYR B  1  144 ? 15.232  -34.269 -56.414 1.00 85.53  ? 170  TYR B CZ  1 
ATOM   5938  O  OH  . TYR B  1  144 ? 14.138  -33.796 -55.729 1.00 85.50  ? 170  TYR B OH  1 
ATOM   5939  N  N   . PHE B  1  145 ? 20.013  -36.165 -55.463 1.00 87.24  ? 171  PHE B N   1 
ATOM   5940  C  CA  . PHE B  1  145 ? 20.554  -35.453 -54.309 1.00 88.80  ? 171  PHE B CA  1 
ATOM   5941  C  C   . PHE B  1  145 ? 22.080  -35.385 -54.308 1.00 89.39  ? 171  PHE B C   1 
ATOM   5942  O  O   . PHE B  1  145 ? 22.676  -34.584 -53.587 1.00 89.37  ? 171  PHE B O   1 
ATOM   5943  C  CB  . PHE B  1  145 ? 20.057  -36.089 -53.012 1.00 89.15  ? 171  PHE B CB  1 
ATOM   5944  C  CG  . PHE B  1  145 ? 18.924  -35.337 -52.374 1.00 90.35  ? 171  PHE B CG  1 
ATOM   5945  C  CD1 . PHE B  1  145 ? 17.759  -35.059 -53.094 1.00 90.89  ? 171  PHE B CD1 1 
ATOM   5946  C  CD2 . PHE B  1  145 ? 19.034  -34.868 -51.070 1.00 89.71  ? 171  PHE B CD2 1 
ATOM   5947  C  CE1 . PHE B  1  145 ? 16.717  -34.321 -52.519 1.00 90.95  ? 171  PHE B CE1 1 
ATOM   5948  C  CE2 . PHE B  1  145 ? 18.003  -34.131 -50.482 1.00 90.44  ? 171  PHE B CE2 1 
ATOM   5949  C  CZ  . PHE B  1  145 ? 16.841  -33.852 -51.207 1.00 90.74  ? 171  PHE B CZ  1 
ATOM   5950  N  N   . SER B  1  146 ? 22.706  -36.224 -55.125 1.00 89.60  ? 172  SER B N   1 
ATOM   5951  C  CA  . SER B  1  146 ? 24.153  -36.234 -55.230 1.00 88.81  ? 172  SER B CA  1 
ATOM   5952  C  C   . SER B  1  146 ? 24.609  -34.913 -55.837 1.00 89.74  ? 172  SER B C   1 
ATOM   5953  O  O   . SER B  1  146 ? 25.420  -34.217 -55.251 1.00 90.04  ? 172  SER B O   1 
ATOM   5954  C  CB  . SER B  1  146 ? 24.603  -37.386 -56.115 1.00 87.92  ? 172  SER B CB  1 
ATOM   5955  O  OG  . SER B  1  146 ? 23.951  -38.581 -55.733 1.00 87.59  ? 172  SER B OG  1 
ATOM   5956  N  N   . ASN B  1  147 ? 24.088  -34.559 -57.009 1.00 91.40  ? 173  ASN B N   1 
ATOM   5957  C  CA  . ASN B  1  147 ? 24.487  -33.307 -57.649 1.00 92.58  ? 173  ASN B CA  1 
ATOM   5958  C  C   . ASN B  1  147 ? 24.208  -32.112 -56.737 1.00 91.40  ? 173  ASN B C   1 
ATOM   5959  O  O   . ASN B  1  147 ? 24.773  -31.032 -56.938 1.00 91.52  ? 173  ASN B O   1 
ATOM   5960  C  CB  . ASN B  1  147 ? 23.771  -33.101 -59.002 1.00 96.95  ? 173  ASN B CB  1 
ATOM   5961  C  CG  . ASN B  1  147 ? 24.206  -34.107 -60.075 1.00 101.70 ? 173  ASN B CG  1 
ATOM   5962  O  OD1 . ASN B  1  147 ? 25.304  -34.673 -60.002 1.00 101.99 ? 173  ASN B OD1 1 
ATOM   5963  N  ND2 . ASN B  1  147 ? 23.332  -34.319 -61.066 1.00 105.69 ? 173  ASN B ND2 1 
ATOM   5964  N  N   . LEU B  1  148 ? 23.335  -32.300 -55.745 1.00 89.54  ? 174  LEU B N   1 
ATOM   5965  C  CA  . LEU B  1  148 ? 23.004  -31.228 -54.795 1.00 88.00  ? 174  LEU B CA  1 
ATOM   5966  C  C   . LEU B  1  148 ? 24.053  -31.234 -53.686 1.00 86.91  ? 174  LEU B C   1 
ATOM   5967  O  O   . LEU B  1  148 ? 23.786  -31.637 -52.555 1.00 85.95  ? 174  LEU B O   1 
ATOM   5968  C  CB  . LEU B  1  148 ? 21.616  -31.454 -54.191 1.00 86.66  ? 174  LEU B CB  1 
ATOM   5969  C  CG  . LEU B  1  148 ? 20.399  -31.213 -55.076 1.00 85.62  ? 174  LEU B CG  1 
ATOM   5970  C  CD1 . LEU B  1  148 ? 19.134  -31.519 -54.294 1.00 85.30  ? 174  LEU B CD1 1 
ATOM   5971  C  CD2 . LEU B  1  148 ? 20.391  -29.770 -55.552 1.00 85.09  ? 174  LEU B CD2 1 
ATOM   5972  N  N   . THR B  1  149 ? 25.245  -30.760 -54.018 1.00 86.12  ? 175  THR B N   1 
ATOM   5973  C  CA  . THR B  1  149 ? 26.356  -30.777 -53.082 1.00 85.15  ? 175  THR B CA  1 
ATOM   5974  C  C   . THR B  1  149 ? 26.501  -29.622 -52.088 1.00 83.53  ? 175  THR B C   1 
ATOM   5975  O  O   . THR B  1  149 ? 27.347  -29.673 -51.198 1.00 82.07  ? 175  THR B O   1 
ATOM   5976  C  CB  . THR B  1  149 ? 27.668  -30.932 -53.864 1.00 85.79  ? 175  THR B CB  1 
ATOM   5977  O  OG1 . THR B  1  149 ? 28.763  -30.976 -52.948 1.00 89.27  ? 175  THR B OG1 1 
ATOM   5978  C  CG2 . THR B  1  149 ? 27.855  -29.768 -54.845 1.00 85.97  ? 175  THR B CG2 1 
ATOM   5979  N  N   . ASN B  1  150 ? 25.680  -28.587 -52.222 1.00 82.25  ? 176  ASN B N   1 
ATOM   5980  C  CA  . ASN B  1  150 ? 25.760  -27.441 -51.318 1.00 79.89  ? 176  ASN B CA  1 
ATOM   5981  C  C   . ASN B  1  150 ? 24.528  -27.331 -50.425 1.00 77.61  ? 176  ASN B C   1 
ATOM   5982  O  O   . ASN B  1  150 ? 24.315  -26.304 -49.768 1.00 77.52  ? 176  ASN B O   1 
ATOM   5983  C  CB  . ASN B  1  150 ? 25.920  -26.146 -52.120 1.00 81.06  ? 176  ASN B CB  1 
ATOM   5984  C  CG  . ASN B  1  150 ? 27.293  -26.004 -52.728 1.00 81.45  ? 176  ASN B CG  1 
ATOM   5985  O  OD1 . ASN B  1  150 ? 27.822  -26.943 -53.326 1.00 82.28  ? 176  ASN B OD1 1 
ATOM   5986  N  ND2 . ASN B  1  150 ? 27.877  -24.817 -52.592 1.00 81.39  ? 176  ASN B ND2 1 
ATOM   5987  N  N   . LEU B  1  151 ? 23.729  -28.390 -50.389 1.00 74.33  ? 177  LEU B N   1 
ATOM   5988  C  CA  . LEU B  1  151 ? 22.519  -28.384 -49.578 1.00 71.85  ? 177  LEU B CA  1 
ATOM   5989  C  C   . LEU B  1  151 ? 22.831  -28.524 -48.089 1.00 71.00  ? 177  LEU B C   1 
ATOM   5990  O  O   . LEU B  1  151 ? 23.519  -29.458 -47.679 1.00 71.14  ? 177  LEU B O   1 
ATOM   5991  C  CB  . LEU B  1  151 ? 21.593  -29.519 -50.014 1.00 69.96  ? 177  LEU B CB  1 
ATOM   5992  C  CG  . LEU B  1  151 ? 20.185  -29.511 -49.422 1.00 67.43  ? 177  LEU B CG  1 
ATOM   5993  C  CD1 . LEU B  1  151 ? 19.405  -28.355 -50.017 1.00 65.55  ? 177  LEU B CD1 1 
ATOM   5994  C  CD2 . LEU B  1  151 ? 19.495  -30.833 -49.715 1.00 65.69  ? 177  LEU B CD2 1 
ATOM   5995  N  N   . GLU B  1  152 ? 22.321  -27.596 -47.282 1.00 70.06  ? 178  GLU B N   1 
ATOM   5996  C  CA  . GLU B  1  152 ? 22.541  -27.639 -45.840 1.00 69.95  ? 178  GLU B CA  1 
ATOM   5997  C  C   . GLU B  1  152 ? 21.233  -27.671 -45.064 1.00 68.84  ? 178  GLU B C   1 
ATOM   5998  O  O   . GLU B  1  152 ? 21.190  -28.104 -43.916 1.00 68.00  ? 178  GLU B O   1 
ATOM   5999  C  CB  . GLU B  1  152 ? 23.319  -26.420 -45.371 1.00 72.12  ? 178  GLU B CB  1 
ATOM   6000  C  CG  . GLU B  1  152 ? 24.424  -25.968 -46.291 1.00 76.17  ? 178  GLU B CG  1 
ATOM   6001  C  CD  . GLU B  1  152 ? 25.364  -25.009 -45.594 1.00 77.97  ? 178  GLU B CD  1 
ATOM   6002  O  OE1 . GLU B  1  152 ? 26.178  -25.501 -44.776 1.00 79.37  ? 178  GLU B OE1 1 
ATOM   6003  O  OE2 . GLU B  1  152 ? 25.274  -23.780 -45.846 1.00 78.07  ? 178  GLU B OE2 1 
ATOM   6004  N  N   . HIS B  1  153 ? 20.163  -27.210 -45.694 1.00 67.92  ? 179  HIS B N   1 
ATOM   6005  C  CA  . HIS B  1  153 ? 18.874  -27.162 -45.035 1.00 66.75  ? 179  HIS B CA  1 
ATOM   6006  C  C   . HIS B  1  153 ? 17.739  -27.835 -45.810 1.00 65.02  ? 179  HIS B C   1 
ATOM   6007  O  O   . HIS B  1  153 ? 17.457  -27.486 -46.951 1.00 65.35  ? 179  HIS B O   1 
ATOM   6008  C  CB  . HIS B  1  153 ? 18.525  -25.701 -44.763 1.00 69.05  ? 179  HIS B CB  1 
ATOM   6009  C  CG  . HIS B  1  153 ? 19.460  -25.023 -43.807 1.00 73.16  ? 179  HIS B CG  1 
ATOM   6010  N  ND1 . HIS B  1  153 ? 19.361  -25.169 -42.438 1.00 74.55  ? 179  HIS B ND1 1 
ATOM   6011  C  CD2 . HIS B  1  153 ? 20.518  -24.204 -44.021 1.00 74.06  ? 179  HIS B CD2 1 
ATOM   6012  C  CE1 . HIS B  1  153 ? 20.318  -24.470 -41.849 1.00 74.25  ? 179  HIS B CE1 1 
ATOM   6013  N  NE2 . HIS B  1  153 ? 21.034  -23.875 -42.787 1.00 74.33  ? 179  HIS B NE2 1 
ATOM   6014  N  N   . LEU B  1  154 ? 17.085  -28.801 -45.176 1.00 62.63  ? 180  LEU B N   1 
ATOM   6015  C  CA  . LEU B  1  154 ? 15.961  -29.497 -45.783 1.00 61.12  ? 180  LEU B CA  1 
ATOM   6016  C  C   . LEU B  1  154 ? 14.784  -29.507 -44.808 1.00 61.93  ? 180  LEU B C   1 
ATOM   6017  O  O   . LEU B  1  154 ? 14.893  -30.031 -43.693 1.00 62.33  ? 180  LEU B O   1 
ATOM   6018  C  CB  . LEU B  1  154 ? 16.334  -30.940 -46.136 1.00 58.50  ? 180  LEU B CB  1 
ATOM   6019  C  CG  . LEU B  1  154 ? 15.226  -31.721 -46.859 1.00 55.88  ? 180  LEU B CG  1 
ATOM   6020  C  CD1 . LEU B  1  154 ? 14.979  -31.090 -48.204 1.00 54.84  ? 180  LEU B CD1 1 
ATOM   6021  C  CD2 . LEU B  1  154 ? 15.602  -33.168 -47.035 1.00 54.75  ? 180  LEU B CD2 1 
ATOM   6022  N  N   . ASP B  1  155 ? 13.662  -28.919 -45.228 1.00 61.95  ? 181  ASP B N   1 
ATOM   6023  C  CA  . ASP B  1  155 ? 12.456  -28.863 -44.405 1.00 60.67  ? 181  ASP B CA  1 
ATOM   6024  C  C   . ASP B  1  155 ? 11.376  -29.796 -44.959 1.00 59.60  ? 181  ASP B C   1 
ATOM   6025  O  O   . ASP B  1  155 ? 10.763  -29.501 -45.979 1.00 59.50  ? 181  ASP B O   1 
ATOM   6026  C  CB  . ASP B  1  155 ? 11.915  -27.432 -44.366 1.00 61.44  ? 181  ASP B CB  1 
ATOM   6027  C  CG  . ASP B  1  155 ? 10.973  -27.195 -43.195 1.00 64.16  ? 181  ASP B CG  1 
ATOM   6028  O  OD1 . ASP B  1  155 ? 10.372  -28.182 -42.713 1.00 66.28  ? 181  ASP B OD1 1 
ATOM   6029  O  OD2 . ASP B  1  155 ? 10.826  -26.025 -42.759 1.00 64.43  ? 181  ASP B OD2 1 
ATOM   6030  N  N   . LEU B  1  156 ? 11.164  -30.928 -44.290 1.00 58.99  ? 182  LEU B N   1 
ATOM   6031  C  CA  . LEU B  1  156 ? 10.149  -31.910 -44.685 1.00 58.36  ? 182  LEU B CA  1 
ATOM   6032  C  C   . LEU B  1  156 ? 9.047   -31.956 -43.623 1.00 58.60  ? 182  LEU B C   1 
ATOM   6033  O  O   . LEU B  1  156 ? 8.240   -32.889 -43.585 1.00 58.67  ? 182  LEU B O   1 
ATOM   6034  C  CB  . LEU B  1  156 ? 10.765  -33.311 -44.828 1.00 56.65  ? 182  LEU B CB  1 
ATOM   6035  C  CG  . LEU B  1  156 ? 11.635  -33.594 -46.052 1.00 57.23  ? 182  LEU B CG  1 
ATOM   6036  C  CD1 . LEU B  1  156 ? 12.235  -34.997 -45.961 1.00 56.68  ? 182  LEU B CD1 1 
ATOM   6037  C  CD2 . LEU B  1  156 ? 10.790  -33.443 -47.300 1.00 56.67  ? 182  LEU B CD2 1 
ATOM   6038  N  N   . SER B  1  157 ? 9.014   -30.945 -42.759 1.00 58.75  ? 183  SER B N   1 
ATOM   6039  C  CA  . SER B  1  157 ? 8.020   -30.892 -41.691 1.00 58.61  ? 183  SER B CA  1 
ATOM   6040  C  C   . SER B  1  157 ? 6.605   -30.693 -42.245 1.00 58.78  ? 183  SER B C   1 
ATOM   6041  O  O   . SER B  1  157 ? 6.416   -30.092 -43.321 1.00 57.78  ? 183  SER B O   1 
ATOM   6042  C  CB  . SER B  1  157 ? 8.357   -29.771 -40.693 1.00 58.01  ? 183  SER B CB  1 
ATOM   6043  O  OG  . SER B  1  157 ? 8.021   -28.487 -41.189 1.00 57.42  ? 183  SER B OG  1 
ATOM   6044  N  N   . SER B  1  158 ? 5.624   -31.205 -41.496 1.00 57.58  ? 184  SER B N   1 
ATOM   6045  C  CA  . SER B  1  158 ? 4.216   -31.120 -41.863 1.00 56.94  ? 184  SER B CA  1 
ATOM   6046  C  C   . SER B  1  158 ? 3.911   -31.796 -43.188 1.00 57.42  ? 184  SER B C   1 
ATOM   6047  O  O   . SER B  1  158 ? 3.336   -31.187 -44.090 1.00 56.70  ? 184  SER B O   1 
ATOM   6048  C  CB  . SER B  1  158 ? 3.751   -29.668 -41.932 1.00 56.00  ? 184  SER B CB  1 
ATOM   6049  O  OG  . SER B  1  158 ? 3.622   -29.110 -40.643 1.00 55.73  ? 184  SER B OG  1 
ATOM   6050  N  N   . ASN B  1  159 ? 4.306   -33.054 -43.314 1.00 58.21  ? 185  ASN B N   1 
ATOM   6051  C  CA  . ASN B  1  159 ? 4.033   -33.801 -44.529 1.00 59.49  ? 185  ASN B CA  1 
ATOM   6052  C  C   . ASN B  1  159 ? 3.338   -35.098 -44.120 1.00 62.01  ? 185  ASN B C   1 
ATOM   6053  O  O   . ASN B  1  159 ? 2.756   -35.166 -43.034 1.00 63.53  ? 185  ASN B O   1 
ATOM   6054  C  CB  . ASN B  1  159 ? 5.328   -34.074 -45.302 1.00 58.13  ? 185  ASN B CB  1 
ATOM   6055  C  CG  . ASN B  1  159 ? 5.716   -32.917 -46.221 1.00 57.23  ? 185  ASN B CG  1 
ATOM   6056  O  OD1 . ASN B  1  159 ? 6.167   -31.864 -45.774 1.00 56.89  ? 185  ASN B OD1 1 
ATOM   6057  N  ND2 . ASN B  1  159 ? 5.521   -33.110 -47.513 1.00 57.56  ? 185  ASN B ND2 1 
ATOM   6058  N  N   . LYS B  1  160 ? 3.394   -36.125 -44.963 1.00 63.74  ? 186  LYS B N   1 
ATOM   6059  C  CA  . LYS B  1  160 ? 2.712   -37.365 -44.639 1.00 64.34  ? 186  LYS B CA  1 
ATOM   6060  C  C   . LYS B  1  160 ? 3.597   -38.577 -44.447 1.00 65.62  ? 186  LYS B C   1 
ATOM   6061  O  O   . LYS B  1  160 ? 3.131   -39.703 -44.588 1.00 68.16  ? 186  LYS B O   1 
ATOM   6062  C  CB  . LYS B  1  160 ? 1.656   -37.660 -45.703 1.00 63.94  ? 186  LYS B CB  1 
ATOM   6063  C  CG  . LYS B  1  160 ? 0.646   -36.533 -45.859 1.00 65.06  ? 186  LYS B CG  1 
ATOM   6064  C  CD  . LYS B  1  160 ? -0.145  -36.325 -44.568 1.00 66.54  ? 186  LYS B CD  1 
ATOM   6065  C  CE  . LYS B  1  160 ? -0.973  -35.053 -44.613 1.00 66.88  ? 186  LYS B CE  1 
ATOM   6066  N  NZ  . LYS B  1  160 ? -1.863  -35.014 -45.805 1.00 68.82  ? 186  LYS B NZ  1 
ATOM   6067  N  N   . ILE B  1  161 ? 4.864   -38.370 -44.119 1.00 66.19  ? 187  ILE B N   1 
ATOM   6068  C  CA  . ILE B  1  161 ? 5.748   -39.507 -43.903 1.00 67.35  ? 187  ILE B CA  1 
ATOM   6069  C  C   . ILE B  1  161 ? 5.277   -40.267 -42.660 1.00 69.44  ? 187  ILE B C   1 
ATOM   6070  O  O   . ILE B  1  161 ? 4.994   -39.651 -41.628 1.00 68.87  ? 187  ILE B O   1 
ATOM   6071  C  CB  . ILE B  1  161 ? 7.200   -39.052 -43.696 1.00 65.50  ? 187  ILE B CB  1 
ATOM   6072  C  CG1 . ILE B  1  161 ? 7.653   -38.234 -44.903 1.00 64.34  ? 187  ILE B CG1 1 
ATOM   6073  C  CG2 . ILE B  1  161 ? 8.101   -40.260 -43.508 1.00 64.69  ? 187  ILE B CG2 1 
ATOM   6074  C  CD1 . ILE B  1  161 ? 9.061   -37.731 -44.773 1.00 64.41  ? 187  ILE B CD1 1 
ATOM   6075  N  N   . GLN B  1  162 ? 5.196   -41.597 -42.767 1.00 71.18  ? 188  GLN B N   1 
ATOM   6076  C  CA  . GLN B  1  162 ? 4.749   -42.443 -41.661 1.00 71.90  ? 188  GLN B CA  1 
ATOM   6077  C  C   . GLN B  1  162 ? 5.768   -43.490 -41.248 1.00 72.46  ? 188  GLN B C   1 
ATOM   6078  O  O   . GLN B  1  162 ? 5.630   -44.120 -40.194 1.00 71.23  ? 188  GLN B O   1 
ATOM   6079  C  CB  . GLN B  1  162 ? 3.442   -43.136 -42.029 1.00 72.89  ? 188  GLN B CB  1 
ATOM   6080  C  CG  . GLN B  1  162 ? 2.344   -42.170 -42.436 1.00 73.83  ? 188  GLN B CG  1 
ATOM   6081  C  CD  . GLN B  1  162 ? 1.032   -42.862 -42.739 1.00 73.76  ? 188  GLN B CD  1 
ATOM   6082  O  OE1 . GLN B  1  162 ? 0.439   -43.505 -41.861 1.00 72.35  ? 188  GLN B OE1 1 
ATOM   6083  N  NE2 . GLN B  1  162 ? 0.565   -42.732 -43.987 1.00 72.64  ? 188  GLN B NE2 1 
ATOM   6084  N  N   . SER B  1  163 ? 6.791   -43.674 -42.080 1.00 74.29  ? 189  SER B N   1 
ATOM   6085  C  CA  . SER B  1  163 ? 7.831   -44.653 -41.785 1.00 75.97  ? 189  SER B CA  1 
ATOM   6086  C  C   . SER B  1  163 ? 9.128   -44.442 -42.553 1.00 75.71  ? 189  SER B C   1 
ATOM   6087  O  O   . SER B  1  163 ? 9.135   -43.901 -43.663 1.00 75.32  ? 189  SER B O   1 
ATOM   6088  C  CB  . SER B  1  163 ? 7.309   -46.069 -42.059 1.00 77.45  ? 189  SER B CB  1 
ATOM   6089  O  OG  . SER B  1  163 ? 6.870   -46.195 -43.404 1.00 77.90  ? 189  SER B OG  1 
ATOM   6090  N  N   . ILE B  1  164 ? 10.228  -44.875 -41.944 1.00 76.20  ? 190  ILE B N   1 
ATOM   6091  C  CA  . ILE B  1  164 ? 11.544  -44.748 -42.557 1.00 77.64  ? 190  ILE B CA  1 
ATOM   6092  C  C   . ILE B  1  164 ? 12.200  -46.127 -42.660 1.00 78.89  ? 190  ILE B C   1 
ATOM   6093  O  O   . ILE B  1  164 ? 12.454  -46.781 -41.640 1.00 79.02  ? 190  ILE B O   1 
ATOM   6094  C  CB  . ILE B  1  164 ? 12.461  -43.809 -41.728 1.00 76.59  ? 190  ILE B CB  1 
ATOM   6095  C  CG1 . ILE B  1  164 ? 11.816  -42.428 -41.606 1.00 75.29  ? 190  ILE B CG1 1 
ATOM   6096  C  CG2 . ILE B  1  164 ? 13.820  -43.658 -42.403 1.00 75.92  ? 190  ILE B CG2 1 
ATOM   6097  C  CD1 . ILE B  1  164 ? 12.536  -41.517 -40.661 1.00 73.26  ? 190  ILE B CD1 1 
ATOM   6098  N  N   . TYR B  1  165 ? 12.459  -46.559 -43.896 1.00 79.42  ? 191  TYR B N   1 
ATOM   6099  C  CA  . TYR B  1  165 ? 13.088  -47.847 -44.159 1.00 79.62  ? 191  TYR B CA  1 
ATOM   6100  C  C   . TYR B  1  165 ? 14.536  -47.601 -44.523 1.00 80.02  ? 191  TYR B C   1 
ATOM   6101  O  O   . TYR B  1  165 ? 14.867  -46.564 -45.086 1.00 79.45  ? 191  TYR B O   1 
ATOM   6102  C  CB  . TYR B  1  165 ? 12.387  -48.554 -45.316 1.00 79.79  ? 191  TYR B CB  1 
ATOM   6103  C  CG  . TYR B  1  165 ? 10.906  -48.740 -45.110 1.00 81.05  ? 191  TYR B CG  1 
ATOM   6104  C  CD1 . TYR B  1  165 ? 9.979   -48.093 -45.939 1.00 81.76  ? 191  TYR B CD1 1 
ATOM   6105  C  CD2 . TYR B  1  165 ? 10.423  -49.556 -44.086 1.00 80.48  ? 191  TYR B CD2 1 
ATOM   6106  C  CE1 . TYR B  1  165 ? 8.606   -48.258 -45.752 1.00 81.91  ? 191  TYR B CE1 1 
ATOM   6107  C  CE2 . TYR B  1  165 ? 9.053   -49.728 -43.890 1.00 81.69  ? 191  TYR B CE2 1 
ATOM   6108  C  CZ  . TYR B  1  165 ? 8.153   -49.077 -44.726 1.00 82.33  ? 191  TYR B CZ  1 
ATOM   6109  O  OH  . TYR B  1  165 ? 6.796   -49.251 -44.533 1.00 83.25  ? 191  TYR B OH  1 
ATOM   6110  N  N   . CYS B  1  166 ? 15.392  -48.565 -44.214 1.00 81.09  ? 192  CYS B N   1 
ATOM   6111  C  CA  . CYS B  1  166 ? 16.819  -48.451 -44.490 1.00 82.81  ? 192  CYS B CA  1 
ATOM   6112  C  C   . CYS B  1  166 ? 17.187  -47.890 -45.869 1.00 83.34  ? 192  CYS B C   1 
ATOM   6113  O  O   . CYS B  1  166 ? 18.018  -46.991 -45.980 1.00 83.54  ? 192  CYS B O   1 
ATOM   6114  C  CB  . CYS B  1  166 ? 17.494  -49.816 -44.311 1.00 84.07  ? 192  CYS B CB  1 
ATOM   6115  S  SG  . CYS B  1  166 ? 17.432  -50.526 -42.620 1.00 85.90  ? 192  CYS B SG  1 
ATOM   6116  N  N   . THR B  1  167 ? 16.575  -48.419 -46.919 1.00 84.27  ? 193  THR B N   1 
ATOM   6117  C  CA  . THR B  1  167 ? 16.879  -47.979 -48.276 1.00 84.60  ? 193  THR B CA  1 
ATOM   6118  C  C   . THR B  1  167 ? 16.650  -46.490 -48.542 1.00 85.77  ? 193  THR B C   1 
ATOM   6119  O  O   . THR B  1  167 ? 17.248  -45.922 -49.457 1.00 85.41  ? 193  THR B O   1 
ATOM   6120  C  CB  . THR B  1  167 ? 16.069  -48.800 -49.294 1.00 84.03  ? 193  THR B CB  1 
ATOM   6121  O  OG1 . THR B  1  167 ? 14.674  -48.484 -49.183 1.00 83.79  ? 193  THR B OG1 1 
ATOM   6122  C  CG2 . THR B  1  167 ? 16.264  -50.279 -49.030 1.00 83.28  ? 193  THR B CG2 1 
ATOM   6123  N  N   . ASP B  1  168 ? 15.792  -45.862 -47.741 1.00 87.06  ? 194  ASP B N   1 
ATOM   6124  C  CA  . ASP B  1  168 ? 15.476  -44.440 -47.890 1.00 87.67  ? 194  ASP B CA  1 
ATOM   6125  C  C   . ASP B  1  168 ? 16.710  -43.531 -47.769 1.00 87.48  ? 194  ASP B C   1 
ATOM   6126  O  O   . ASP B  1  168 ? 16.834  -42.522 -48.476 1.00 85.99  ? 194  ASP B O   1 
ATOM   6127  C  CB  . ASP B  1  168 ? 14.437  -44.033 -46.838 1.00 88.76  ? 194  ASP B CB  1 
ATOM   6128  C  CG  . ASP B  1  168 ? 13.129  -44.802 -46.975 1.00 90.90  ? 194  ASP B CG  1 
ATOM   6129  O  OD1 . ASP B  1  168 ? 12.238  -44.638 -46.105 1.00 92.03  ? 194  ASP B OD1 1 
ATOM   6130  O  OD2 . ASP B  1  168 ? 12.990  -45.567 -47.957 1.00 91.75  ? 194  ASP B OD2 1 
ATOM   6131  N  N   . LEU B  1  169 ? 17.623  -43.914 -46.879 1.00 87.85  ? 195  LEU B N   1 
ATOM   6132  C  CA  . LEU B  1  169 ? 18.846  -43.160 -46.620 1.00 88.99  ? 195  LEU B CA  1 
ATOM   6133  C  C   . LEU B  1  169 ? 20.069  -43.547 -47.458 1.00 90.52  ? 195  LEU B C   1 
ATOM   6134  O  O   . LEU B  1  169 ? 21.144  -42.965 -47.302 1.00 91.07  ? 195  LEU B O   1 
ATOM   6135  C  CB  . LEU B  1  169 ? 19.194  -43.291 -45.144 1.00 87.76  ? 195  LEU B CB  1 
ATOM   6136  C  CG  . LEU B  1  169 ? 18.162  -42.627 -44.247 1.00 87.71  ? 195  LEU B CG  1 
ATOM   6137  C  CD1 . LEU B  1  169 ? 18.348  -43.083 -42.823 1.00 87.82  ? 195  LEU B CD1 1 
ATOM   6138  C  CD2 . LEU B  1  169 ? 18.293  -41.115 -44.373 1.00 87.70  ? 195  LEU B CD2 1 
ATOM   6139  N  N   . ARG B  1  170 ? 19.906  -44.517 -48.352 1.00 91.78  ? 196  ARG B N   1 
ATOM   6140  C  CA  . ARG B  1  170 ? 21.010  -44.984 -49.184 1.00 92.01  ? 196  ARG B CA  1 
ATOM   6141  C  C   . ARG B  1  170 ? 21.756  -43.864 -49.904 1.00 90.93  ? 196  ARG B C   1 
ATOM   6142  O  O   . ARG B  1  170 ? 22.953  -43.972 -50.149 1.00 90.85  ? 196  ARG B O   1 
ATOM   6143  C  CB  . ARG B  1  170 ? 20.495  -46.001 -50.203 1.00 94.30  ? 196  ARG B CB  1 
ATOM   6144  C  CG  . ARG B  1  170 ? 21.589  -46.757 -50.938 1.00 97.77  ? 196  ARG B CG  1 
ATOM   6145  C  CD  . ARG B  1  170 ? 20.992  -47.674 -52.000 1.00 100.82 ? 196  ARG B CD  1 
ATOM   6146  N  NE  . ARG B  1  170 ? 20.185  -46.924 -52.960 1.00 102.78 ? 196  ARG B NE  1 
ATOM   6147  C  CZ  . ARG B  1  170 ? 20.671  -46.035 -53.825 1.00 104.05 ? 196  ARG B CZ  1 
ATOM   6148  N  NH1 . ARG B  1  170 ? 21.973  -45.771 -53.873 1.00 103.61 ? 196  ARG B NH1 1 
ATOM   6149  N  NH2 . ARG B  1  170 ? 19.843  -45.398 -54.641 1.00 104.70 ? 196  ARG B NH2 1 
ATOM   6150  N  N   . VAL B  1  171 ? 21.055  -42.790 -50.240 1.00 89.95  ? 197  VAL B N   1 
ATOM   6151  C  CA  . VAL B  1  171 ? 21.684  -41.678 -50.943 1.00 89.61  ? 197  VAL B CA  1 
ATOM   6152  C  C   . VAL B  1  171 ? 22.760  -41.020 -50.103 1.00 89.27  ? 197  VAL B C   1 
ATOM   6153  O  O   . VAL B  1  171 ? 23.819  -40.640 -50.602 1.00 88.28  ? 197  VAL B O   1 
ATOM   6154  C  CB  . VAL B  1  171 ? 20.674  -40.593 -51.281 1.00 89.60  ? 197  VAL B CB  1 
ATOM   6155  C  CG1 . VAL B  1  171 ? 21.279  -39.632 -52.305 1.00 89.13  ? 197  VAL B CG1 1 
ATOM   6156  C  CG2 . VAL B  1  171 ? 19.385  -41.226 -51.766 1.00 90.09  ? 197  VAL B CG2 1 
ATOM   6157  N  N   . LEU B  1  172 ? 22.466  -40.876 -48.817 1.00 89.82  ? 198  LEU B N   1 
ATOM   6158  C  CA  . LEU B  1  172 ? 23.387  -40.246 -47.885 1.00 89.80  ? 198  LEU B CA  1 
ATOM   6159  C  C   . LEU B  1  172 ? 24.678  -41.047 -47.711 1.00 91.26  ? 198  LEU B C   1 
ATOM   6160  O  O   . LEU B  1  172 ? 25.758  -40.465 -47.606 1.00 91.35  ? 198  LEU B O   1 
ATOM   6161  C  CB  . LEU B  1  172 ? 22.682  -40.018 -46.539 1.00 87.24  ? 198  LEU B CB  1 
ATOM   6162  C  CG  . LEU B  1  172 ? 21.549  -38.976 -46.568 1.00 85.32  ? 198  LEU B CG  1 
ATOM   6163  C  CD1 . LEU B  1  172 ? 20.852  -38.924 -45.226 1.00 83.63  ? 198  LEU B CD1 1 
ATOM   6164  C  CD2 . LEU B  1  172 ? 22.106  -37.606 -46.916 1.00 83.69  ? 198  LEU B CD2 1 
ATOM   6165  N  N   . HIS B  1  173 ? 24.573  -42.373 -47.694 1.00 93.41  ? 199  HIS B N   1 
ATOM   6166  C  CA  . HIS B  1  173 ? 25.751  -43.233 -47.553 1.00 94.97  ? 199  HIS B CA  1 
ATOM   6167  C  C   . HIS B  1  173 ? 26.799  -42.904 -48.635 1.00 96.24  ? 199  HIS B C   1 
ATOM   6168  O  O   . HIS B  1  173 ? 27.931  -43.378 -48.568 1.00 96.95  ? 199  HIS B O   1 
ATOM   6169  C  CB  . HIS B  1  173 ? 25.362  -44.713 -47.695 1.00 94.61  ? 199  HIS B CB  1 
ATOM   6170  C  CG  . HIS B  1  173 ? 24.577  -45.268 -46.546 1.00 95.69  ? 199  HIS B CG  1 
ATOM   6171  N  ND1 . HIS B  1  173 ? 25.130  -45.495 -45.305 1.00 96.00  ? 199  HIS B ND1 1 
ATOM   6172  C  CD2 . HIS B  1  173 ? 23.299  -45.717 -46.475 1.00 96.20  ? 199  HIS B CD2 1 
ATOM   6173  C  CE1 . HIS B  1  173 ? 24.229  -46.065 -44.521 1.00 95.56  ? 199  HIS B CE1 1 
ATOM   6174  N  NE2 . HIS B  1  173 ? 23.110  -46.211 -45.207 1.00 94.94  ? 199  HIS B NE2 1 
ATOM   6175  N  N   . GLN B  1  174 ? 26.424  -42.097 -49.625 1.00 96.79  ? 200  GLN B N   1 
ATOM   6176  C  CA  . GLN B  1  174 ? 27.337  -41.756 -50.715 1.00 97.50  ? 200  GLN B CA  1 
ATOM   6177  C  C   . GLN B  1  174 ? 27.673  -40.269 -50.822 1.00 97.30  ? 200  GLN B C   1 
ATOM   6178  O  O   . GLN B  1  174 ? 27.972  -39.759 -51.901 1.00 96.59  ? 200  GLN B O   1 
ATOM   6179  C  CB  . GLN B  1  174 ? 26.749  -42.240 -52.040 1.00 98.89  ? 200  GLN B CB  1 
ATOM   6180  C  CG  . GLN B  1  174 ? 26.496  -43.738 -52.102 1.00 100.21 ? 200  GLN B CG  1 
ATOM   6181  C  CD  . GLN B  1  174 ? 25.673  -44.117 -53.319 1.00 101.83 ? 200  GLN B CD  1 
ATOM   6182  O  OE1 . GLN B  1  174 ? 26.057  -43.823 -54.452 1.00 102.73 ? 200  GLN B OE1 1 
ATOM   6183  N  NE2 . GLN B  1  174 ? 24.535  -44.770 -53.092 1.00 102.71 ? 200  GLN B NE2 1 
ATOM   6184  N  N   . MET B  1  175 ? 27.608  -39.573 -49.699 1.00 97.39  ? 201  MET B N   1 
ATOM   6185  C  CA  . MET B  1  175 ? 27.931  -38.159 -49.659 1.00 97.41  ? 201  MET B CA  1 
ATOM   6186  C  C   . MET B  1  175 ? 28.699  -37.935 -48.372 1.00 97.98  ? 201  MET B C   1 
ATOM   6187  O  O   . MET B  1  175 ? 28.112  -37.604 -47.340 1.00 97.30  ? 201  MET B O   1 
ATOM   6188  C  CB  . MET B  1  175 ? 26.667  -37.308 -49.648 1.00 97.55  ? 201  MET B CB  1 
ATOM   6189  C  CG  . MET B  1  175 ? 25.865  -37.324 -50.935 1.00 97.78  ? 201  MET B CG  1 
ATOM   6190  S  SD  . MET B  1  175 ? 24.381  -36.274 -50.802 1.00 96.78  ? 201  MET B SD  1 
ATOM   6191  C  CE  . MET B  1  175 ? 25.117  -34.632 -50.772 1.00 95.85  ? 201  MET B CE  1 
ATOM   6192  N  N   . PRO B  1  176 ? 30.027  -38.137 -48.410 1.00 98.69  ? 202  PRO B N   1 
ATOM   6193  C  CA  . PRO B  1  176 ? 30.904  -37.960 -47.245 1.00 98.48  ? 202  PRO B CA  1 
ATOM   6194  C  C   . PRO B  1  176 ? 30.622  -36.627 -46.553 1.00 97.78  ? 202  PRO B C   1 
ATOM   6195  O  O   . PRO B  1  176 ? 29.968  -36.591 -45.509 1.00 98.43  ? 202  PRO B O   1 
ATOM   6196  C  CB  . PRO B  1  176 ? 32.301  -38.022 -47.858 1.00 98.99  ? 202  PRO B CB  1 
ATOM   6197  C  CG  . PRO B  1  176 ? 32.109  -38.988 -48.995 1.00 99.10  ? 202  PRO B CG  1 
ATOM   6198  C  CD  . PRO B  1  176 ? 30.811  -38.501 -49.605 1.00 98.76  ? 202  PRO B CD  1 
ATOM   6199  N  N   . LEU B  1  177 ? 31.123  -35.537 -47.133 1.00 96.04  ? 203  LEU B N   1 
ATOM   6200  C  CA  . LEU B  1  177 ? 30.880  -34.206 -46.584 1.00 93.74  ? 203  LEU B CA  1 
ATOM   6201  C  C   . LEU B  1  177 ? 29.403  -33.922 -46.870 1.00 91.13  ? 203  LEU B C   1 
ATOM   6202  O  O   . LEU B  1  177 ? 28.936  -34.132 -47.985 1.00 91.05  ? 203  LEU B O   1 
ATOM   6203  C  CB  . LEU B  1  177 ? 31.783  -33.160 -47.270 1.00 94.53  ? 203  LEU B CB  1 
ATOM   6204  C  CG  . LEU B  1  177 ? 33.309  -33.163 -47.039 1.00 94.96  ? 203  LEU B CG  1 
ATOM   6205  C  CD1 . LEU B  1  177 ? 33.949  -32.139 -47.966 1.00 94.08  ? 203  LEU B CD1 1 
ATOM   6206  C  CD2 . LEU B  1  177 ? 33.655  -32.834 -45.574 1.00 95.03  ? 203  LEU B CD2 1 
ATOM   6207  N  N   . LEU B  1  178 ? 28.661  -33.471 -45.865 1.00 88.28  ? 204  LEU B N   1 
ATOM   6208  C  CA  . LEU B  1  178 ? 27.243  -33.205 -46.059 1.00 85.65  ? 204  LEU B CA  1 
ATOM   6209  C  C   . LEU B  1  178 ? 26.622  -32.640 -44.786 1.00 84.41  ? 204  LEU B C   1 
ATOM   6210  O  O   . LEU B  1  178 ? 26.007  -33.365 -44.009 1.00 85.15  ? 204  LEU B O   1 
ATOM   6211  C  CB  . LEU B  1  178 ? 26.544  -34.505 -46.488 1.00 84.65  ? 204  LEU B CB  1 
ATOM   6212  C  CG  . LEU B  1  178 ? 25.106  -34.514 -47.008 1.00 83.59  ? 204  LEU B CG  1 
ATOM   6213  C  CD1 . LEU B  1  178 ? 24.159  -34.848 -45.876 1.00 83.11  ? 204  LEU B CD1 1 
ATOM   6214  C  CD2 . LEU B  1  178 ? 24.780  -33.181 -47.658 1.00 82.46  ? 204  LEU B CD2 1 
ATOM   6215  N  N   . ASN B  1  179 ? 26.799  -31.337 -44.587 1.00 82.73  ? 205  ASN B N   1 
ATOM   6216  C  CA  . ASN B  1  179 ? 26.290  -30.594 -43.427 1.00 81.12  ? 205  ASN B CA  1 
ATOM   6217  C  C   . ASN B  1  179 ? 24.765  -30.434 -43.586 1.00 79.71  ? 205  ASN B C   1 
ATOM   6218  O  O   . ASN B  1  179 ? 24.286  -29.339 -43.883 1.00 80.96  ? 205  ASN B O   1 
ATOM   6219  C  CB  . ASN B  1  179 ? 26.959  -29.206 -43.409 1.00 82.72  ? 205  ASN B CB  1 
ATOM   6220  C  CG  . ASN B  1  179 ? 27.149  -28.647 -42.020 1.00 85.01  ? 205  ASN B CG  1 
ATOM   6221  O  OD1 . ASN B  1  179 ? 27.825  -29.258 -41.196 1.00 83.72  ? 205  ASN B OD1 1 
ATOM   6222  N  ND2 . ASN B  1  179 ? 26.549  -27.481 -41.768 1.00 89.27  ? 205  ASN B ND2 1 
ATOM   6223  N  N   . LEU B  1  180 ? 23.999  -31.507 -43.380 1.00 75.97  ? 206  LEU B N   1 
ATOM   6224  C  CA  . LEU B  1  180 ? 22.542  -31.438 -43.539 1.00 71.13  ? 206  LEU B CA  1 
ATOM   6225  C  C   . LEU B  1  180 ? 21.745  -31.219 -42.244 1.00 69.03  ? 206  LEU B C   1 
ATOM   6226  O  O   . LEU B  1  180 ? 21.881  -31.983 -41.284 1.00 67.55  ? 206  LEU B O   1 
ATOM   6227  C  CB  . LEU B  1  180 ? 22.044  -32.709 -44.237 1.00 70.69  ? 206  LEU B CB  1 
ATOM   6228  C  CG  . LEU B  1  180 ? 20.835  -32.624 -45.179 1.00 69.24  ? 206  LEU B CG  1 
ATOM   6229  C  CD1 . LEU B  1  180 ? 19.560  -32.330 -44.425 1.00 69.70  ? 206  LEU B CD1 1 
ATOM   6230  C  CD2 . LEU B  1  180 ? 21.090  -31.549 -46.203 1.00 69.97  ? 206  LEU B CD2 1 
ATOM   6231  N  N   . SER B  1  181 ? 20.921  -30.164 -42.236 1.00 66.92  ? 207  SER B N   1 
ATOM   6232  C  CA  . SER B  1  181 ? 20.049  -29.817 -41.101 1.00 64.06  ? 207  SER B CA  1 
ATOM   6233  C  C   . SER B  1  181 ? 18.632  -30.192 -41.534 1.00 63.07  ? 207  SER B C   1 
ATOM   6234  O  O   . SER B  1  181 ? 18.038  -29.530 -42.389 1.00 63.17  ? 207  SER B O   1 
ATOM   6235  C  CB  . SER B  1  181 ? 20.108  -28.317 -40.795 1.00 62.95  ? 207  SER B CB  1 
ATOM   6236  O  OG  . SER B  1  181 ? 21.379  -27.925 -40.306 1.00 61.57  ? 207  SER B OG  1 
ATOM   6237  N  N   . LEU B  1  182 ? 18.095  -31.246 -40.925 1.00 61.62  ? 208  LEU B N   1 
ATOM   6238  C  CA  . LEU B  1  182 ? 16.780  -31.777 -41.270 1.00 60.50  ? 208  LEU B CA  1 
ATOM   6239  C  C   . LEU B  1  182 ? 15.642  -31.578 -40.253 1.00 60.57  ? 208  LEU B C   1 
ATOM   6240  O  O   . LEU B  1  182 ? 15.826  -31.782 -39.048 1.00 59.45  ? 208  LEU B O   1 
ATOM   6241  C  CB  . LEU B  1  182 ? 16.959  -33.270 -41.570 1.00 59.61  ? 208  LEU B CB  1 
ATOM   6242  C  CG  . LEU B  1  182 ? 15.796  -34.191 -41.927 1.00 60.25  ? 208  LEU B CG  1 
ATOM   6243  C  CD1 . LEU B  1  182 ? 15.219  -33.842 -43.293 1.00 59.72  ? 208  LEU B CD1 1 
ATOM   6244  C  CD2 . LEU B  1  182 ? 16.313  -35.609 -41.920 1.00 58.18  ? 208  LEU B CD2 1 
ATOM   6245  N  N   . ASP B  1  183 ? 14.469  -31.181 -40.754 1.00 60.97  ? 209  ASP B N   1 
ATOM   6246  C  CA  . ASP B  1  183 ? 13.282  -30.987 -39.915 1.00 61.76  ? 209  ASP B CA  1 
ATOM   6247  C  C   . ASP B  1  183 ? 12.164  -31.939 -40.356 1.00 61.14  ? 209  ASP B C   1 
ATOM   6248  O  O   . ASP B  1  183 ? 11.686  -31.840 -41.481 1.00 60.03  ? 209  ASP B O   1 
ATOM   6249  C  CB  . ASP B  1  183 ? 12.755  -29.554 -40.011 1.00 62.69  ? 209  ASP B CB  1 
ATOM   6250  C  CG  . ASP B  1  183 ? 11.829  -29.197 -38.846 1.00 65.11  ? 209  ASP B CG  1 
ATOM   6251  O  OD1 . ASP B  1  183 ? 11.167  -30.112 -38.308 1.00 66.66  ? 209  ASP B OD1 1 
ATOM   6252  O  OD2 . ASP B  1  183 ? 11.752  -28.006 -38.462 1.00 65.36  ? 209  ASP B OD2 1 
ATOM   6253  N  N   . LEU B  1  184 ? 11.754  -32.846 -39.463 1.00 60.65  ? 210  LEU B N   1 
ATOM   6254  C  CA  . LEU B  1  184 ? 10.693  -33.816 -39.752 1.00 59.01  ? 210  LEU B CA  1 
ATOM   6255  C  C   . LEU B  1  184 ? 9.477   -33.653 -38.850 1.00 58.62  ? 210  LEU B C   1 
ATOM   6256  O  O   . LEU B  1  184 ? 8.643   -34.547 -38.771 1.00 58.90  ? 210  LEU B O   1 
ATOM   6257  C  CB  . LEU B  1  184 ? 11.216  -35.247 -39.614 1.00 57.23  ? 210  LEU B CB  1 
ATOM   6258  C  CG  . LEU B  1  184 ? 12.168  -35.731 -40.704 1.00 56.93  ? 210  LEU B CG  1 
ATOM   6259  C  CD1 . LEU B  1  184 ? 12.651  -37.123 -40.358 1.00 56.26  ? 210  LEU B CD1 1 
ATOM   6260  C  CD2 . LEU B  1  184 ? 11.458  -35.722 -42.055 1.00 55.40  ? 210  LEU B CD2 1 
ATOM   6261  N  N   . SER B  1  185 ? 9.369   -32.506 -38.187 1.00 59.08  ? 211  SER B N   1 
ATOM   6262  C  CA  . SER B  1  185 ? 8.254   -32.228 -37.279 1.00 59.37  ? 211  SER B CA  1 
ATOM   6263  C  C   . SER B  1  185 ? 6.875   -32.319 -37.929 1.00 59.92  ? 211  SER B C   1 
ATOM   6264  O  O   . SER B  1  185 ? 6.711   -32.061 -39.125 1.00 59.89  ? 211  SER B O   1 
ATOM   6265  C  CB  . SER B  1  185 ? 8.417   -30.841 -36.651 1.00 58.26  ? 211  SER B CB  1 
ATOM   6266  O  OG  . SER B  1  185 ? 9.628   -30.743 -35.917 1.00 57.45  ? 211  SER B OG  1 
ATOM   6267  N  N   . LEU B  1  186 ? 5.890   -32.681 -37.113 1.00 59.75  ? 212  LEU B N   1 
ATOM   6268  C  CA  . LEU B  1  186 ? 4.507   -32.816 -37.545 1.00 60.12  ? 212  LEU B CA  1 
ATOM   6269  C  C   . LEU B  1  186 ? 4.234   -33.853 -38.636 1.00 62.37  ? 212  LEU B C   1 
ATOM   6270  O  O   . LEU B  1  186 ? 3.282   -33.728 -39.400 1.00 64.16  ? 212  LEU B O   1 
ATOM   6271  C  CB  . LEU B  1  186 ? 3.955   -31.450 -37.952 1.00 56.47  ? 212  LEU B CB  1 
ATOM   6272  C  CG  . LEU B  1  186 ? 3.845   -30.487 -36.763 1.00 55.67  ? 212  LEU B CG  1 
ATOM   6273  C  CD1 . LEU B  1  186 ? 3.378   -29.143 -37.247 1.00 55.22  ? 212  LEU B CD1 1 
ATOM   6274  C  CD2 . LEU B  1  186 ? 2.888   -31.028 -35.711 1.00 52.58  ? 212  LEU B CD2 1 
ATOM   6275  N  N   . ASN B  1  187 ? 5.081   -34.871 -38.722 1.00 63.65  ? 213  ASN B N   1 
ATOM   6276  C  CA  . ASN B  1  187 ? 4.862   -35.948 -39.667 1.00 66.06  ? 213  ASN B CA  1 
ATOM   6277  C  C   . ASN B  1  187 ? 4.370   -37.082 -38.776 1.00 69.02  ? 213  ASN B C   1 
ATOM   6278  O  O   . ASN B  1  187 ? 4.982   -37.376 -37.748 1.00 69.41  ? 213  ASN B O   1 
ATOM   6279  C  CB  . ASN B  1  187 ? 6.160   -36.330 -40.353 1.00 66.73  ? 213  ASN B CB  1 
ATOM   6280  C  CG  . ASN B  1  187 ? 6.385   -35.547 -41.635 1.00 69.72  ? 213  ASN B CG  1 
ATOM   6281  O  OD1 . ASN B  1  187 ? 5.723   -35.789 -42.653 1.00 70.06  ? 213  ASN B OD1 1 
ATOM   6282  N  ND2 . ASN B  1  187 ? 7.313   -34.592 -41.593 1.00 70.22  ? 213  ASN B ND2 1 
ATOM   6283  N  N   . PRO B  1  188 ? 3.244   -37.723 -39.141 1.00 70.28  ? 214  PRO B N   1 
ATOM   6284  C  CA  . PRO B  1  188 ? 2.672   -38.825 -38.356 1.00 71.04  ? 214  PRO B CA  1 
ATOM   6285  C  C   . PRO B  1  188 ? 3.523   -40.105 -38.372 1.00 73.26  ? 214  PRO B C   1 
ATOM   6286  O  O   . PRO B  1  188 ? 3.112   -41.163 -38.868 1.00 73.11  ? 214  PRO B O   1 
ATOM   6287  C  CB  . PRO B  1  188 ? 1.307   -39.005 -39.001 1.00 70.24  ? 214  PRO B CB  1 
ATOM   6288  C  CG  . PRO B  1  188 ? 1.614   -38.740 -40.442 1.00 69.78  ? 214  PRO B CG  1 
ATOM   6289  C  CD  . PRO B  1  188 ? 2.479   -37.512 -40.384 1.00 69.19  ? 214  PRO B CD  1 
ATOM   6290  N  N   . MET B  1  189 ? 4.717   -39.994 -37.809 1.00 75.16  ? 215  MET B N   1 
ATOM   6291  C  CA  . MET B  1  189 ? 5.666   -41.094 -37.757 1.00 78.11  ? 215  MET B CA  1 
ATOM   6292  C  C   . MET B  1  189 ? 5.200   -42.170 -36.792 1.00 79.12  ? 215  MET B C   1 
ATOM   6293  O  O   . MET B  1  189 ? 4.527   -41.867 -35.804 1.00 79.45  ? 215  MET B O   1 
ATOM   6294  C  CB  . MET B  1  189 ? 7.018   -40.566 -37.283 1.00 79.90  ? 215  MET B CB  1 
ATOM   6295  C  CG  . MET B  1  189 ? 8.206   -41.399 -37.691 1.00 82.67  ? 215  MET B CG  1 
ATOM   6296  S  SD  . MET B  1  189 ? 8.861   -40.806 -39.251 1.00 86.24  ? 215  MET B SD  1 
ATOM   6297  C  CE  . MET B  1  189 ? 9.616   -39.227 -38.653 1.00 85.66  ? 215  MET B CE  1 
ATOM   6298  N  N   . ASN B  1  190 ? 5.549   -43.422 -37.078 1.00 80.20  ? 216  ASN B N   1 
ATOM   6299  C  CA  . ASN B  1  190 ? 5.197   -44.520 -36.179 1.00 81.80  ? 216  ASN B CA  1 
ATOM   6300  C  C   . ASN B  1  190 ? 6.078   -45.735 -36.381 1.00 81.31  ? 216  ASN B C   1 
ATOM   6301  O  O   . ASN B  1  190 ? 5.875   -46.765 -35.737 1.00 81.23  ? 216  ASN B O   1 
ATOM   6302  C  CB  . ASN B  1  190 ? 3.710   -44.908 -36.287 1.00 84.33  ? 216  ASN B CB  1 
ATOM   6303  C  CG  . ASN B  1  190 ? 3.256   -45.090 -37.710 1.00 86.75  ? 216  ASN B CG  1 
ATOM   6304  O  OD1 . ASN B  1  190 ? 3.798   -45.922 -38.442 1.00 88.00  ? 216  ASN B OD1 1 
ATOM   6305  N  ND2 . ASN B  1  190 ? 2.255   -44.304 -38.120 1.00 87.43  ? 216  ASN B ND2 1 
ATOM   6306  N  N   . PHE B  1  191 ? 7.057   -45.612 -37.277 1.00 80.93  ? 217  PHE B N   1 
ATOM   6307  C  CA  . PHE B  1  191 ? 8.013   -46.696 -37.523 1.00 81.07  ? 217  PHE B CA  1 
ATOM   6308  C  C   . PHE B  1  191 ? 9.274   -46.284 -38.285 1.00 80.81  ? 217  PHE B C   1 
ATOM   6309  O  O   . PHE B  1  191 ? 9.208   -45.762 -39.409 1.00 81.29  ? 217  PHE B O   1 
ATOM   6310  C  CB  . PHE B  1  191 ? 7.362   -47.877 -38.264 1.00 80.75  ? 217  PHE B CB  1 
ATOM   6311  C  CG  . PHE B  1  191 ? 8.322   -49.019 -38.558 1.00 79.63  ? 217  PHE B CG  1 
ATOM   6312  C  CD1 . PHE B  1  191 ? 8.897   -49.757 -37.521 1.00 79.34  ? 217  PHE B CD1 1 
ATOM   6313  C  CD2 . PHE B  1  191 ? 8.675   -49.331 -39.873 1.00 79.27  ? 217  PHE B CD2 1 
ATOM   6314  C  CE1 . PHE B  1  191 ? 9.811   -50.796 -37.787 1.00 79.05  ? 217  PHE B CE1 1 
ATOM   6315  C  CE2 . PHE B  1  191 ? 9.586   -50.366 -40.153 1.00 78.95  ? 217  PHE B CE2 1 
ATOM   6316  C  CZ  . PHE B  1  191 ? 10.156  -51.099 -39.107 1.00 78.74  ? 217  PHE B CZ  1 
ATOM   6317  N  N   . ILE B  1  192 ? 10.420  -46.520 -37.652 1.00 79.12  ? 218  ILE B N   1 
ATOM   6318  C  CA  . ILE B  1  192 ? 11.716  -46.242 -38.252 1.00 78.81  ? 218  ILE B CA  1 
ATOM   6319  C  C   . ILE B  1  192 ? 12.438  -47.582 -38.155 1.00 79.66  ? 218  ILE B C   1 
ATOM   6320  O  O   . ILE B  1  192 ? 12.816  -48.019 -37.067 1.00 79.74  ? 218  ILE B O   1 
ATOM   6321  C  CB  . ILE B  1  192 ? 12.490  -45.132 -37.481 1.00 77.64  ? 218  ILE B CB  1 
ATOM   6322  C  CG1 . ILE B  1  192 ? 11.791  -43.778 -37.669 1.00 76.36  ? 218  ILE B CG1 1 
ATOM   6323  C  CG2 . ILE B  1  192 ? 13.911  -45.029 -37.997 1.00 75.82  ? 218  ILE B CG2 1 
ATOM   6324  C  CD1 . ILE B  1  192 ? 12.368  -42.659 -36.838 1.00 73.32  ? 218  ILE B CD1 1 
ATOM   6325  N  N   . GLN B  1  193 ? 12.593  -48.240 -39.302 1.00 80.50  ? 219  GLN B N   1 
ATOM   6326  C  CA  . GLN B  1  193 ? 13.230  -49.553 -39.388 1.00 81.22  ? 219  GLN B CA  1 
ATOM   6327  C  C   . GLN B  1  193 ? 14.602  -49.601 -38.731 1.00 80.59  ? 219  GLN B C   1 
ATOM   6328  O  O   . GLN B  1  193 ? 15.504  -48.885 -39.144 1.00 80.87  ? 219  GLN B O   1 
ATOM   6329  C  CB  . GLN B  1  193 ? 13.372  -49.960 -40.852 1.00 83.00  ? 219  GLN B CB  1 
ATOM   6330  C  CG  . GLN B  1  193 ? 13.598  -51.457 -41.056 1.00 85.93  ? 219  GLN B CG  1 
ATOM   6331  C  CD  . GLN B  1  193 ? 14.346  -51.766 -42.336 1.00 86.52  ? 219  GLN B CD  1 
ATOM   6332  O  OE1 . GLN B  1  193 ? 14.051  -51.205 -43.398 1.00 86.97  ? 219  GLN B OE1 1 
ATOM   6333  N  NE2 . GLN B  1  193 ? 15.317  -52.665 -42.245 1.00 86.44  ? 219  GLN B NE2 1 
ATOM   6334  N  N   . PRO B  1  194 ? 14.787  -50.467 -37.714 1.00 80.24  ? 220  PRO B N   1 
ATOM   6335  C  CA  . PRO B  1  194 ? 16.070  -50.592 -37.010 1.00 80.26  ? 220  PRO B CA  1 
ATOM   6336  C  C   . PRO B  1  194 ? 17.303  -50.620 -37.913 1.00 81.32  ? 220  PRO B C   1 
ATOM   6337  O  O   . PRO B  1  194 ? 17.286  -51.194 -39.009 1.00 81.45  ? 220  PRO B O   1 
ATOM   6338  C  CB  . PRO B  1  194 ? 15.905  -51.887 -36.221 1.00 79.80  ? 220  PRO B CB  1 
ATOM   6339  C  CG  . PRO B  1  194 ? 14.469  -51.862 -35.867 1.00 80.61  ? 220  PRO B CG  1 
ATOM   6340  C  CD  . PRO B  1  194 ? 13.804  -51.419 -37.162 1.00 80.45  ? 220  PRO B CD  1 
ATOM   6341  N  N   . GLY B  1  195 ? 18.374  -49.989 -37.438 1.00 81.83  ? 221  GLY B N   1 
ATOM   6342  C  CA  . GLY B  1  195 ? 19.616  -49.939 -38.190 1.00 81.68  ? 221  GLY B CA  1 
ATOM   6343  C  C   . GLY B  1  195 ? 19.571  -49.055 -39.423 1.00 81.50  ? 221  GLY B C   1 
ATOM   6344  O  O   . GLY B  1  195 ? 20.529  -49.015 -40.195 1.00 81.32  ? 221  GLY B O   1 
ATOM   6345  N  N   . ALA B  1  196 ? 18.468  -48.334 -39.607 1.00 81.45  ? 222  ALA B N   1 
ATOM   6346  C  CA  . ALA B  1  196 ? 18.308  -47.461 -40.765 1.00 81.48  ? 222  ALA B CA  1 
ATOM   6347  C  C   . ALA B  1  196 ? 19.232  -46.254 -40.728 1.00 81.33  ? 222  ALA B C   1 
ATOM   6348  O  O   . ALA B  1  196 ? 19.588  -45.709 -41.770 1.00 80.87  ? 222  ALA B O   1 
ATOM   6349  C  CB  . ALA B  1  196 ? 16.859  -46.999 -40.880 1.00 81.33  ? 222  ALA B CB  1 
ATOM   6350  N  N   . PHE B  1  197 ? 19.621  -45.831 -39.531 1.00 81.42  ? 223  PHE B N   1 
ATOM   6351  C  CA  . PHE B  1  197 ? 20.497  -44.679 -39.423 1.00 81.24  ? 223  PHE B CA  1 
ATOM   6352  C  C   . PHE B  1  197 ? 21.955  -44.990 -39.156 1.00 82.71  ? 223  PHE B C   1 
ATOM   6353  O  O   . PHE B  1  197 ? 22.753  -44.073 -38.977 1.00 83.60  ? 223  PHE B O   1 
ATOM   6354  C  CB  . PHE B  1  197 ? 19.961  -43.698 -38.374 1.00 78.19  ? 223  PHE B CB  1 
ATOM   6355  C  CG  . PHE B  1  197 ? 18.826  -42.858 -38.875 1.00 74.89  ? 223  PHE B CG  1 
ATOM   6356  C  CD1 . PHE B  1  197 ? 17.520  -43.308 -38.797 1.00 73.16  ? 223  PHE B CD1 1 
ATOM   6357  C  CD2 . PHE B  1  197 ? 19.078  -41.655 -39.512 1.00 73.69  ? 223  PHE B CD2 1 
ATOM   6358  C  CE1 . PHE B  1  197 ? 16.482  -42.576 -39.354 1.00 71.70  ? 223  PHE B CE1 1 
ATOM   6359  C  CE2 . PHE B  1  197 ? 18.046  -40.920 -40.071 1.00 71.88  ? 223  PHE B CE2 1 
ATOM   6360  C  CZ  . PHE B  1  197 ? 16.743  -41.382 -39.992 1.00 70.56  ? 223  PHE B CZ  1 
ATOM   6361  N  N   . LYS B  1  198 ? 22.310  -46.271 -39.140 1.00 84.09  ? 224  LYS B N   1 
ATOM   6362  C  CA  . LYS B  1  198 ? 23.699  -46.658 -38.906 1.00 85.35  ? 224  LYS B CA  1 
ATOM   6363  C  C   . LYS B  1  198 ? 24.653  -45.902 -39.837 1.00 84.72  ? 224  LYS B C   1 
ATOM   6364  O  O   . LYS B  1  198 ? 24.496  -45.911 -41.058 1.00 84.47  ? 224  LYS B O   1 
ATOM   6365  C  CB  . LYS B  1  198 ? 23.890  -48.172 -39.099 1.00 86.81  ? 224  LYS B CB  1 
ATOM   6366  C  CG  . LYS B  1  198 ? 23.754  -49.014 -37.832 1.00 88.66  ? 224  LYS B CG  1 
ATOM   6367  C  CD  . LYS B  1  198 ? 24.086  -50.479 -38.131 1.00 90.71  ? 224  LYS B CD  1 
ATOM   6368  C  CE  . LYS B  1  198 ? 23.999  -51.359 -36.882 1.00 92.62  ? 224  LYS B CE  1 
ATOM   6369  N  NZ  . LYS B  1  198 ? 24.236  -52.813 -37.183 1.00 91.57  ? 224  LYS B NZ  1 
ATOM   6370  N  N   . GLU B  1  199 ? 25.641  -45.247 -39.240 1.00 84.01  ? 225  GLU B N   1 
ATOM   6371  C  CA  . GLU B  1  199 ? 26.635  -44.478 -39.979 1.00 83.20  ? 225  GLU B CA  1 
ATOM   6372  C  C   . GLU B  1  199 ? 26.090  -43.359 -40.857 1.00 80.69  ? 225  GLU B C   1 
ATOM   6373  O  O   . GLU B  1  199 ? 26.594  -43.102 -41.953 1.00 79.00  ? 225  GLU B O   1 
ATOM   6374  C  CB  . GLU B  1  199 ? 27.504  -45.411 -40.807 1.00 85.75  ? 225  GLU B CB  1 
ATOM   6375  C  CG  . GLU B  1  199 ? 28.395  -46.283 -39.952 1.00 89.48  ? 225  GLU B CG  1 
ATOM   6376  C  CD  . GLU B  1  199 ? 29.526  -46.892 -40.746 1.00 92.66  ? 225  GLU B CD  1 
ATOM   6377  O  OE1 . GLU B  1  199 ? 29.244  -47.716 -41.649 1.00 93.95  ? 225  GLU B OE1 1 
ATOM   6378  O  OE2 . GLU B  1  199 ? 30.697  -46.542 -40.470 1.00 94.05  ? 225  GLU B OE2 1 
ATOM   6379  N  N   . ILE B  1  200 ? 25.056  -42.695 -40.354 1.00 78.34  ? 226  ILE B N   1 
ATOM   6380  C  CA  . ILE B  1  200 ? 24.452  -41.562 -41.038 1.00 75.35  ? 226  ILE B CA  1 
ATOM   6381  C  C   . ILE B  1  200 ? 24.830  -40.364 -40.173 1.00 73.34  ? 226  ILE B C   1 
ATOM   6382  O  O   . ILE B  1  200 ? 24.931  -40.484 -38.947 1.00 71.91  ? 226  ILE B O   1 
ATOM   6383  C  CB  . ILE B  1  200 ? 22.920  -41.681 -41.088 1.00 74.79  ? 226  ILE B CB  1 
ATOM   6384  C  CG1 . ILE B  1  200 ? 22.523  -42.918 -41.884 1.00 74.62  ? 226  ILE B CG1 1 
ATOM   6385  C  CG2 . ILE B  1  200 ? 22.324  -40.436 -41.715 1.00 74.09  ? 226  ILE B CG2 1 
ATOM   6386  C  CD1 . ILE B  1  200 ? 22.904  -42.849 -43.341 1.00 74.86  ? 226  ILE B CD1 1 
ATOM   6387  N  N   . ARG B  1  201 ? 25.055  -39.219 -40.798 1.00 70.68  ? 227  ARG B N   1 
ATOM   6388  C  CA  . ARG B  1  201 ? 25.420  -38.047 -40.029 1.00 69.42  ? 227  ARG B CA  1 
ATOM   6389  C  C   . ARG B  1  201 ? 24.695  -36.763 -40.424 1.00 67.01  ? 227  ARG B C   1 
ATOM   6390  O  O   . ARG B  1  201 ? 24.814  -36.256 -41.541 1.00 65.83  ? 227  ARG B O   1 
ATOM   6391  C  CB  . ARG B  1  201 ? 26.924  -37.833 -40.091 1.00 72.03  ? 227  ARG B CB  1 
ATOM   6392  C  CG  . ARG B  1  201 ? 27.404  -36.595 -39.371 1.00 76.90  ? 227  ARG B CG  1 
ATOM   6393  C  CD  . ARG B  1  201 ? 28.919  -36.545 -39.365 1.00 82.13  ? 227  ARG B CD  1 
ATOM   6394  N  NE  . ARG B  1  201 ? 29.455  -36.727 -40.710 1.00 87.51  ? 227  ARG B NE  1 
ATOM   6395  C  CZ  . ARG B  1  201 ? 30.738  -36.939 -40.987 1.00 90.04  ? 227  ARG B CZ  1 
ATOM   6396  N  NH1 . ARG B  1  201 ? 31.636  -36.998 -40.003 1.00 90.55  ? 227  ARG B NH1 1 
ATOM   6397  N  NH2 . ARG B  1  201 ? 31.119  -37.098 -42.253 1.00 90.47  ? 227  ARG B NH2 1 
ATOM   6398  N  N   . LEU B  1  202 ? 23.938  -36.243 -39.471 1.00 63.96  ? 228  LEU B N   1 
ATOM   6399  C  CA  . LEU B  1  202 ? 23.179  -35.024 -39.656 1.00 60.28  ? 228  LEU B CA  1 
ATOM   6400  C  C   . LEU B  1  202 ? 23.778  -33.937 -38.773 1.00 59.26  ? 228  LEU B C   1 
ATOM   6401  O  O   . LEU B  1  202 ? 24.377  -34.229 -37.734 1.00 58.79  ? 228  LEU B O   1 
ATOM   6402  C  CB  . LEU B  1  202 ? 21.728  -35.266 -39.238 1.00 58.38  ? 228  LEU B CB  1 
ATOM   6403  C  CG  . LEU B  1  202 ? 20.730  -35.956 -40.169 1.00 57.07  ? 228  LEU B CG  1 
ATOM   6404  C  CD1 . LEU B  1  202 ? 21.409  -36.598 -41.359 1.00 57.28  ? 228  LEU B CD1 1 
ATOM   6405  C  CD2 . LEU B  1  202 ? 19.973  -36.967 -39.358 1.00 55.79  ? 228  LEU B CD2 1 
ATOM   6406  N  N   . HIS B  1  203 ? 23.622  -32.682 -39.175 1.00 57.83  ? 229  HIS B N   1 
ATOM   6407  C  CA  . HIS B  1  203 ? 24.133  -31.598 -38.351 1.00 57.20  ? 229  HIS B CA  1 
ATOM   6408  C  C   . HIS B  1  203 ? 23.082  -31.250 -37.289 1.00 55.98  ? 229  HIS B C   1 
ATOM   6409  O  O   . HIS B  1  203 ? 23.416  -30.994 -36.136 1.00 54.69  ? 229  HIS B O   1 
ATOM   6410  C  CB  . HIS B  1  203 ? 24.455  -30.371 -39.200 1.00 58.23  ? 229  HIS B CB  1 
ATOM   6411  C  CG  . HIS B  1  203 ? 25.031  -29.240 -38.409 1.00 60.42  ? 229  HIS B CG  1 
ATOM   6412  N  ND1 . HIS B  1  203 ? 24.275  -28.167 -37.983 1.00 61.06  ? 229  HIS B ND1 1 
ATOM   6413  C  CD2 . HIS B  1  203 ? 26.275  -29.048 -37.909 1.00 60.38  ? 229  HIS B CD2 1 
ATOM   6414  C  CE1 . HIS B  1  203 ? 25.029  -27.364 -37.253 1.00 60.76  ? 229  HIS B CE1 1 
ATOM   6415  N  NE2 . HIS B  1  203 ? 26.247  -27.876 -37.193 1.00 60.82  ? 229  HIS B NE2 1 
ATOM   6416  N  N   . LYS B  1  204 ? 21.812  -31.260 -37.696 1.00 54.65  ? 230  LYS B N   1 
ATOM   6417  C  CA  . LYS B  1  204 ? 20.693  -30.980 -36.801 1.00 52.85  ? 230  LYS B CA  1 
ATOM   6418  C  C   . LYS B  1  204 ? 19.528  -31.882 -37.238 1.00 51.69  ? 230  LYS B C   1 
ATOM   6419  O  O   . LYS B  1  204 ? 19.395  -32.207 -38.413 1.00 50.30  ? 230  LYS B O   1 
ATOM   6420  C  CB  . LYS B  1  204 ? 20.284  -29.492 -36.905 1.00 52.89  ? 230  LYS B CB  1 
ATOM   6421  C  CG  . LYS B  1  204 ? 19.340  -28.934 -35.794 1.00 50.32  ? 230  LYS B CG  1 
ATOM   6422  C  CD  . LYS B  1  204 ? 18.906  -27.489 -36.126 1.00 49.21  ? 230  LYS B CD  1 
ATOM   6423  C  CE  . LYS B  1  204 ? 18.352  -26.710 -34.934 1.00 48.78  ? 230  LYS B CE  1 
ATOM   6424  N  NZ  . LYS B  1  204 ? 16.862  -26.716 -34.792 1.00 49.31  ? 230  LYS B NZ  1 
ATOM   6425  N  N   . LEU B  1  205 ? 18.708  -32.297 -36.278 1.00 50.53  ? 231  LEU B N   1 
ATOM   6426  C  CA  . LEU B  1  205 ? 17.539  -33.117 -36.546 1.00 50.48  ? 231  LEU B CA  1 
ATOM   6427  C  C   . LEU B  1  205 ? 16.474  -32.592 -35.593 1.00 51.60  ? 231  LEU B C   1 
ATOM   6428  O  O   . LEU B  1  205 ? 16.724  -32.454 -34.392 1.00 50.92  ? 231  LEU B O   1 
ATOM   6429  C  CB  . LEU B  1  205 ? 17.789  -34.592 -36.217 1.00 49.07  ? 231  LEU B CB  1 
ATOM   6430  C  CG  . LEU B  1  205 ? 17.051  -35.713 -36.983 1.00 48.22  ? 231  LEU B CG  1 
ATOM   6431  C  CD1 . LEU B  1  205 ? 17.017  -36.958 -36.094 1.00 46.46  ? 231  LEU B CD1 1 
ATOM   6432  C  CD2 . LEU B  1  205 ? 15.642  -35.321 -37.369 1.00 47.07  ? 231  LEU B CD2 1 
ATOM   6433  N  N   . THR B  1  206 ? 15.297  -32.274 -36.125 1.00 52.23  ? 232  THR B N   1 
ATOM   6434  C  CA  . THR B  1  206 ? 14.201  -31.810 -35.284 1.00 51.78  ? 232  THR B CA  1 
ATOM   6435  C  C   . THR B  1  206 ? 13.022  -32.753 -35.501 1.00 51.63  ? 232  THR B C   1 
ATOM   6436  O  O   . THR B  1  206 ? 12.559  -32.936 -36.627 1.00 50.46  ? 232  THR B O   1 
ATOM   6437  C  CB  . THR B  1  206 ? 13.770  -30.382 -35.637 1.00 52.61  ? 232  THR B CB  1 
ATOM   6438  O  OG1 . THR B  1  206 ? 14.895  -29.502 -35.531 1.00 52.42  ? 232  THR B OG1 1 
ATOM   6439  C  CG2 . THR B  1  206 ? 12.680  -29.912 -34.690 1.00 52.29  ? 232  THR B CG2 1 
ATOM   6440  N  N   . LEU B  1  207 ? 12.570  -33.365 -34.409 1.00 51.60  ? 233  LEU B N   1 
ATOM   6441  C  CA  . LEU B  1  207 ? 11.451  -34.295 -34.414 1.00 51.47  ? 233  LEU B CA  1 
ATOM   6442  C  C   . LEU B  1  207 ? 10.469  -33.860 -33.329 1.00 53.23  ? 233  LEU B C   1 
ATOM   6443  O  O   . LEU B  1  207 ? 10.453  -34.404 -32.213 1.00 53.69  ? 233  LEU B O   1 
ATOM   6444  C  CB  . LEU B  1  207 ? 11.937  -35.720 -34.131 1.00 50.67  ? 233  LEU B CB  1 
ATOM   6445  C  CG  . LEU B  1  207 ? 12.791  -36.386 -35.209 1.00 50.36  ? 233  LEU B CG  1 
ATOM   6446  C  CD1 . LEU B  1  207 ? 13.301  -37.717 -34.708 1.00 50.09  ? 233  LEU B CD1 1 
ATOM   6447  C  CD2 . LEU B  1  207 ? 11.974  -36.571 -36.479 1.00 51.59  ? 233  LEU B CD2 1 
ATOM   6448  N  N   . ARG B  1  208 ? 9.665   -32.854 -33.657 1.00 53.62  ? 234  ARG B N   1 
ATOM   6449  C  CA  . ARG B  1  208 ? 8.678   -32.339 -32.727 1.00 54.76  ? 234  ARG B CA  1 
ATOM   6450  C  C   . ARG B  1  208 ? 7.267   -32.715 -33.167 1.00 56.43  ? 234  ARG B C   1 
ATOM   6451  O  O   . ARG B  1  208 ? 6.904   -32.557 -34.335 1.00 55.74  ? 234  ARG B O   1 
ATOM   6452  C  CB  . ARG B  1  208 ? 8.808   -30.818 -32.605 1.00 54.15  ? 234  ARG B CB  1 
ATOM   6453  C  CG  . ARG B  1  208 ? 10.061  -30.356 -31.869 1.00 53.23  ? 234  ARG B CG  1 
ATOM   6454  C  CD  . ARG B  1  208 ? 10.138  -28.837 -31.783 1.00 52.44  ? 234  ARG B CD  1 
ATOM   6455  N  NE  . ARG B  1  208 ? 9.210   -28.275 -30.807 1.00 50.99  ? 234  ARG B NE  1 
ATOM   6456  C  CZ  . ARG B  1  208 ? 8.822   -27.006 -30.805 1.00 50.23  ? 234  ARG B CZ  1 
ATOM   6457  N  NH1 . ARG B  1  208 ? 9.287   -26.174 -31.729 1.00 49.50  ? 234  ARG B NH1 1 
ATOM   6458  N  NH2 . ARG B  1  208 ? 7.961   -26.575 -29.893 1.00 49.18  ? 234  ARG B NH2 1 
ATOM   6459  N  N   . ASN B  1  209 ? 6.484   -33.225 -32.219 1.00 58.53  ? 235  ASN B N   1 
ATOM   6460  C  CA  . ASN B  1  209 ? 5.106   -33.638 -32.465 1.00 60.58  ? 235  ASN B CA  1 
ATOM   6461  C  C   . ASN B  1  209 ? 5.017   -34.712 -33.516 1.00 61.94  ? 235  ASN B C   1 
ATOM   6462  O  O   . ASN B  1  209 ? 4.146   -34.669 -34.381 1.00 62.16  ? 235  ASN B O   1 
ATOM   6463  C  CB  . ASN B  1  209 ? 4.255   -32.449 -32.897 1.00 60.24  ? 235  ASN B CB  1 
ATOM   6464  C  CG  . ASN B  1  209 ? 3.177   -32.134 -31.905 1.00 61.44  ? 235  ASN B CG  1 
ATOM   6465  O  OD1 . ASN B  1  209 ? 2.384   -31.225 -32.109 1.00 63.16  ? 235  ASN B OD1 1 
ATOM   6466  N  ND2 . ASN B  1  209 ? 3.137   -32.889 -30.816 1.00 62.10  ? 235  ASN B ND2 1 
ATOM   6467  N  N   . ASN B  1  210 ? 5.907   -35.692 -33.434 1.00 63.66  ? 236  ASN B N   1 
ATOM   6468  C  CA  . ASN B  1  210 ? 5.910   -36.761 -34.412 1.00 65.68  ? 236  ASN B CA  1 
ATOM   6469  C  C   . ASN B  1  210 ? 5.242   -38.026 -33.949 1.00 67.39  ? 236  ASN B C   1 
ATOM   6470  O  O   . ASN B  1  210 ? 4.553   -38.685 -34.726 1.00 69.85  ? 236  ASN B O   1 
ATOM   6471  C  CB  . ASN B  1  210 ? 7.337   -37.093 -34.831 1.00 65.13  ? 236  ASN B CB  1 
ATOM   6472  C  CG  . ASN B  1  210 ? 7.934   -36.037 -35.717 1.00 66.68  ? 236  ASN B CG  1 
ATOM   6473  O  OD1 . ASN B  1  210 ? 7.371   -35.684 -36.756 1.00 69.23  ? 236  ASN B OD1 1 
ATOM   6474  N  ND2 . ASN B  1  210 ? 9.083   -35.525 -35.322 1.00 65.79  ? 236  ASN B ND2 1 
ATOM   6475  N  N   . PHE B  1  211 ? 5.419   -38.364 -32.683 1.00 67.84  ? 237  PHE B N   1 
ATOM   6476  C  CA  . PHE B  1  211 ? 4.869   -39.607 -32.196 1.00 69.36  ? 237  PHE B CA  1 
ATOM   6477  C  C   . PHE B  1  211 ? 3.560   -39.525 -31.443 1.00 70.68  ? 237  PHE B C   1 
ATOM   6478  O  O   . PHE B  1  211 ? 3.336   -38.619 -30.643 1.00 71.68  ? 237  PHE B O   1 
ATOM   6479  C  CB  . PHE B  1  211 ? 5.947   -40.293 -31.377 1.00 69.79  ? 237  PHE B CB  1 
ATOM   6480  C  CG  . PHE B  1  211 ? 7.322   -40.092 -31.949 1.00 70.49  ? 237  PHE B CG  1 
ATOM   6481  C  CD1 . PHE B  1  211 ? 8.221   -39.213 -31.344 1.00 70.48  ? 237  PHE B CD1 1 
ATOM   6482  C  CD2 . PHE B  1  211 ? 7.690   -40.717 -33.141 1.00 69.98  ? 237  PHE B CD2 1 
ATOM   6483  C  CE1 . PHE B  1  211 ? 9.471   -38.953 -31.908 1.00 70.05  ? 237  PHE B CE1 1 
ATOM   6484  C  CE2 . PHE B  1  211 ? 8.933   -40.471 -33.721 1.00 70.66  ? 237  PHE B CE2 1 
ATOM   6485  C  CZ  . PHE B  1  211 ? 9.830   -39.577 -33.099 1.00 71.03  ? 237  PHE B CZ  1 
ATOM   6486  N  N   . ASP B  1  212 ? 2.698   -40.498 -31.725 1.00 71.52  ? 238  ASP B N   1 
ATOM   6487  C  CA  . ASP B  1  212 ? 1.370   -40.608 -31.132 1.00 70.91  ? 238  ASP B CA  1 
ATOM   6488  C  C   . ASP B  1  212 ? 1.396   -40.955 -29.647 1.00 68.31  ? 238  ASP B C   1 
ATOM   6489  O  O   . ASP B  1  212 ? 0.882   -40.208 -28.827 1.00 67.41  ? 238  ASP B O   1 
ATOM   6490  C  CB  . ASP B  1  212 ? 0.570   -41.655 -31.914 1.00 74.68  ? 238  ASP B CB  1 
ATOM   6491  C  CG  . ASP B  1  212 ? -0.899  -41.670 -31.542 1.00 78.13  ? 238  ASP B CG  1 
ATOM   6492  O  OD1 . ASP B  1  212 ? -1.505  -40.579 -31.412 1.00 78.97  ? 238  ASP B OD1 1 
ATOM   6493  O  OD2 . ASP B  1  212 ? -1.453  -42.782 -31.401 1.00 81.35  ? 238  ASP B OD2 1 
ATOM   6494  N  N   . SER B  1  213 ? 1.998   -42.088 -29.308 1.00 66.64  ? 239  SER B N   1 
ATOM   6495  C  CA  . SER B  1  213 ? 2.090   -42.529 -27.922 1.00 65.85  ? 239  SER B CA  1 
ATOM   6496  C  C   . SER B  1  213 ? 3.533   -42.460 -27.457 1.00 64.97  ? 239  SER B C   1 
ATOM   6497  O  O   . SER B  1  213 ? 4.408   -42.078 -28.229 1.00 64.26  ? 239  SER B O   1 
ATOM   6498  C  CB  . SER B  1  213 ? 1.596   -43.972 -27.798 1.00 66.10  ? 239  SER B CB  1 
ATOM   6499  O  OG  . SER B  1  213 ? 2.457   -44.869 -28.474 1.00 64.03  ? 239  SER B OG  1 
ATOM   6500  N  N   . LEU B  1  214 ? 3.778   -42.829 -26.201 1.00 64.64  ? 240  LEU B N   1 
ATOM   6501  C  CA  . LEU B  1  214 ? 5.140   -42.822 -25.667 1.00 66.20  ? 240  LEU B CA  1 
ATOM   6502  C  C   . LEU B  1  214 ? 5.854   -44.036 -26.245 1.00 67.61  ? 240  LEU B C   1 
ATOM   6503  O  O   . LEU B  1  214 ? 7.056   -44.014 -26.513 1.00 67.47  ? 240  LEU B O   1 
ATOM   6504  C  CB  . LEU B  1  214 ? 5.138   -42.931 -24.138 1.00 65.67  ? 240  LEU B CB  1 
ATOM   6505  C  CG  . LEU B  1  214 ? 6.270   -42.283 -23.317 1.00 64.41  ? 240  LEU B CG  1 
ATOM   6506  C  CD1 . LEU B  1  214 ? 6.228   -42.829 -21.896 1.00 63.02  ? 240  LEU B CD1 1 
ATOM   6507  C  CD2 . LEU B  1  214 ? 7.623   -42.556 -23.930 1.00 63.34  ? 240  LEU B CD2 1 
ATOM   6508  N  N   . ASN B  1  215 ? 5.086   -45.095 -26.453 1.00 69.31  ? 241  ASN B N   1 
ATOM   6509  C  CA  . ASN B  1  215 ? 5.620   -46.338 -26.988 1.00 69.98  ? 241  ASN B CA  1 
ATOM   6510  C  C   . ASN B  1  215 ? 6.019   -46.180 -28.438 1.00 68.25  ? 241  ASN B C   1 
ATOM   6511  O  O   . ASN B  1  215 ? 7.019   -46.743 -28.877 1.00 68.11  ? 241  ASN B O   1 
ATOM   6512  C  CB  . ASN B  1  215 ? 4.578   -47.438 -26.814 1.00 73.45  ? 241  ASN B CB  1 
ATOM   6513  C  CG  . ASN B  1  215 ? 4.199   -47.633 -25.348 1.00 78.46  ? 241  ASN B CG  1 
ATOM   6514  O  OD1 . ASN B  1  215 ? 4.961   -48.243 -24.574 1.00 79.18  ? 241  ASN B OD1 1 
ATOM   6515  N  ND2 . ASN B  1  215 ? 3.036   -47.086 -24.944 1.00 79.00  ? 241  ASN B ND2 1 
ATOM   6516  N  N   . VAL B  1  216 ? 5.240   -45.408 -29.181 1.00 66.75  ? 242  VAL B N   1 
ATOM   6517  C  CA  . VAL B  1  216 ? 5.562   -45.177 -30.575 1.00 65.65  ? 242  VAL B CA  1 
ATOM   6518  C  C   . VAL B  1  216 ? 6.836   -44.339 -30.628 1.00 65.70  ? 242  VAL B C   1 
ATOM   6519  O  O   . VAL B  1  216 ? 7.687   -44.539 -31.507 1.00 66.43  ? 242  VAL B O   1 
ATOM   6520  C  CB  . VAL B  1  216 ? 4.425   -44.437 -31.307 1.00 64.87  ? 242  VAL B CB  1 
ATOM   6521  C  CG1 . VAL B  1  216 ? 4.863   -44.059 -32.725 1.00 64.16  ? 242  VAL B CG1 1 
ATOM   6522  C  CG2 . VAL B  1  216 ? 3.198   -45.319 -31.369 1.00 65.07  ? 242  VAL B CG2 1 
ATOM   6523  N  N   . MET B  1  217 ? 6.983   -43.411 -29.683 1.00 63.97  ? 243  MET B N   1 
ATOM   6524  C  CA  . MET B  1  217 ? 8.170   -42.575 -29.674 1.00 61.85  ? 243  MET B CA  1 
ATOM   6525  C  C   . MET B  1  217 ? 9.402   -43.402 -29.368 1.00 60.68  ? 243  MET B C   1 
ATOM   6526  O  O   . MET B  1  217 ? 10.388  -43.349 -30.101 1.00 61.21  ? 243  MET B O   1 
ATOM   6527  C  CB  . MET B  1  217 ? 8.050   -41.439 -28.660 1.00 61.51  ? 243  MET B CB  1 
ATOM   6528  C  CG  . MET B  1  217 ? 9.308   -40.567 -28.599 1.00 61.66  ? 243  MET B CG  1 
ATOM   6529  S  SD  . MET B  1  217 ? 9.128   -39.101 -27.585 1.00 62.93  ? 243  MET B SD  1 
ATOM   6530  C  CE  . MET B  1  217 ? 10.006  -39.551 -26.134 1.00 64.36  ? 243  MET B CE  1 
ATOM   6531  N  N   . LYS B  1  218 ? 9.341   -44.177 -28.295 1.00 59.41  ? 244  LYS B N   1 
ATOM   6532  C  CA  . LYS B  1  218 ? 10.473  -45.002 -27.903 1.00 59.48  ? 244  LYS B CA  1 
ATOM   6533  C  C   . LYS B  1  218 ? 10.893  -45.959 -29.015 1.00 60.67  ? 244  LYS B C   1 
ATOM   6534  O  O   . LYS B  1  218 ? 12.078  -46.250 -29.193 1.00 60.49  ? 244  LYS B O   1 
ATOM   6535  C  CB  . LYS B  1  218 ? 10.135  -45.765 -26.617 1.00 57.20  ? 244  LYS B CB  1 
ATOM   6536  C  CG  . LYS B  1  218 ? 9.970   -44.841 -25.422 1.00 56.46  ? 244  LYS B CG  1 
ATOM   6537  C  CD  . LYS B  1  218 ? 9.407   -45.536 -24.212 1.00 57.26  ? 244  LYS B CD  1 
ATOM   6538  C  CE  . LYS B  1  218 ? 10.408  -46.470 -23.559 1.00 58.79  ? 244  LYS B CE  1 
ATOM   6539  N  NZ  . LYS B  1  218 ? 9.786   -47.201 -22.400 1.00 59.03  ? 244  LYS B NZ  1 
ATOM   6540  N  N   . THR B  1  219 ? 9.917   -46.437 -29.772 1.00 62.20  ? 245  THR B N   1 
ATOM   6541  C  CA  . THR B  1  219 ? 10.191  -47.349 -30.868 1.00 63.34  ? 245  THR B CA  1 
ATOM   6542  C  C   . THR B  1  219 ? 10.982  -46.650 -31.965 1.00 64.42  ? 245  THR B C   1 
ATOM   6543  O  O   . THR B  1  219 ? 11.992  -47.166 -32.432 1.00 64.89  ? 245  THR B O   1 
ATOM   6544  C  CB  . THR B  1  219 ? 8.882   -47.894 -31.465 1.00 63.02  ? 245  THR B CB  1 
ATOM   6545  O  OG1 . THR B  1  219 ? 8.250   -48.740 -30.505 1.00 63.08  ? 245  THR B OG1 1 
ATOM   6546  C  CG2 . THR B  1  219 ? 9.152   -48.686 -32.733 1.00 61.98  ? 245  THR B CG2 1 
ATOM   6547  N  N   . CYS B  1  220 ? 10.522  -45.476 -32.378 1.00 65.53  ? 246  CYS B N   1 
ATOM   6548  C  CA  . CYS B  1  220 ? 11.209  -44.737 -33.429 1.00 67.18  ? 246  CYS B CA  1 
ATOM   6549  C  C   . CYS B  1  220 ? 12.619  -44.341 -33.037 1.00 67.89  ? 246  CYS B C   1 
ATOM   6550  O  O   . CYS B  1  220 ? 13.549  -44.489 -33.823 1.00 68.38  ? 246  CYS B O   1 
ATOM   6551  C  CB  . CYS B  1  220 ? 10.431  -43.481 -33.799 1.00 67.63  ? 246  CYS B CB  1 
ATOM   6552  S  SG  . CYS B  1  220 ? 8.874   -43.809 -34.574 1.00 69.57  ? 246  CYS B SG  1 
ATOM   6553  N  N   . ILE B  1  221 ? 12.772  -43.818 -31.827 1.00 68.48  ? 247  ILE B N   1 
ATOM   6554  C  CA  . ILE B  1  221 ? 14.082  -43.411 -31.348 1.00 69.46  ? 247  ILE B CA  1 
ATOM   6555  C  C   . ILE B  1  221 ? 15.074  -44.584 -31.365 1.00 72.22  ? 247  ILE B C   1 
ATOM   6556  O  O   . ILE B  1  221 ? 16.296  -44.380 -31.337 1.00 73.56  ? 247  ILE B O   1 
ATOM   6557  C  CB  . ILE B  1  221 ? 13.960  -42.797 -29.943 1.00 67.37  ? 247  ILE B CB  1 
ATOM   6558  C  CG1 . ILE B  1  221 ? 13.353  -41.404 -30.081 1.00 65.77  ? 247  ILE B CG1 1 
ATOM   6559  C  CG2 . ILE B  1  221 ? 15.307  -42.737 -29.245 1.00 65.54  ? 247  ILE B CG2 1 
ATOM   6560  C  CD1 . ILE B  1  221 ? 13.060  -40.730 -28.777 1.00 65.84  ? 247  ILE B CD1 1 
ATOM   6561  N  N   . GLN B  1  222 ? 14.550  -45.810 -31.432 1.00 73.44  ? 248  GLN B N   1 
ATOM   6562  C  CA  . GLN B  1  222 ? 15.400  -47.003 -31.498 1.00 72.86  ? 248  GLN B CA  1 
ATOM   6563  C  C   . GLN B  1  222 ? 15.918  -47.207 -32.916 1.00 71.44  ? 248  GLN B C   1 
ATOM   6564  O  O   . GLN B  1  222 ? 17.040  -47.672 -33.110 1.00 72.06  ? 248  GLN B O   1 
ATOM   6565  C  CB  . GLN B  1  222 ? 14.638  -48.248 -31.062 1.00 73.91  ? 248  GLN B CB  1 
ATOM   6566  C  CG  . GLN B  1  222 ? 14.395  -48.321 -29.578 1.00 77.23  ? 248  GLN B CG  1 
ATOM   6567  C  CD  . GLN B  1  222 ? 13.776  -49.640 -29.166 1.00 79.12  ? 248  GLN B CD  1 
ATOM   6568  O  OE1 . GLN B  1  222 ? 13.409  -49.830 -28.003 1.00 79.45  ? 248  GLN B OE1 1 
ATOM   6569  N  NE2 . GLN B  1  222 ? 13.662  -50.568 -30.120 1.00 79.06  ? 248  GLN B NE2 1 
ATOM   6570  N  N   . GLY B  1  223 ? 15.095  -46.868 -33.902 1.00 69.42  ? 249  GLY B N   1 
ATOM   6571  C  CA  . GLY B  1  223 ? 15.510  -47.011 -35.285 1.00 68.08  ? 249  GLY B CA  1 
ATOM   6572  C  C   . GLY B  1  223 ? 16.528  -45.936 -35.599 1.00 67.22  ? 249  GLY B C   1 
ATOM   6573  O  O   . GLY B  1  223 ? 17.294  -46.024 -36.561 1.00 67.77  ? 249  GLY B O   1 
ATOM   6574  N  N   . LEU B  1  224 ? 16.528  -44.911 -34.755 1.00 66.26  ? 250  LEU B N   1 
ATOM   6575  C  CA  . LEU B  1  224 ? 17.430  -43.779 -34.885 1.00 64.52  ? 250  LEU B CA  1 
ATOM   6576  C  C   . LEU B  1  224 ? 18.832  -44.200 -34.449 1.00 64.17  ? 250  LEU B C   1 
ATOM   6577  O  O   . LEU B  1  224 ? 19.819  -43.543 -34.782 1.00 62.86  ? 250  LEU B O   1 
ATOM   6578  C  CB  . LEU B  1  224 ? 16.918  -42.626 -34.012 1.00 62.37  ? 250  LEU B CB  1 
ATOM   6579  C  CG  . LEU B  1  224 ? 16.688  -41.277 -34.689 1.00 61.77  ? 250  LEU B CG  1 
ATOM   6580  C  CD1 . LEU B  1  224 ? 15.853  -41.450 -35.946 1.00 59.06  ? 250  LEU B CD1 1 
ATOM   6581  C  CD2 . LEU B  1  224 ? 16.014  -40.341 -33.699 1.00 60.10  ? 250  LEU B CD2 1 
ATOM   6582  N  N   . ALA B  1  225 ? 18.900  -45.312 -33.714 1.00 64.24  ? 251  ALA B N   1 
ATOM   6583  C  CA  . ALA B  1  225 ? 20.158  -45.866 -33.201 1.00 65.02  ? 251  ALA B CA  1 
ATOM   6584  C  C   . ALA B  1  225 ? 21.319  -45.892 -34.202 1.00 64.94  ? 251  ALA B C   1 
ATOM   6585  O  O   . ALA B  1  225 ? 21.178  -46.377 -35.339 1.00 65.33  ? 251  ALA B O   1 
ATOM   6586  C  CB  . ALA B  1  225 ? 19.917  -47.275 -32.651 1.00 64.62  ? 251  ALA B CB  1 
ATOM   6587  N  N   . GLY B  1  226 ? 22.466  -45.376 -33.757 1.00 63.33  ? 252  GLY B N   1 
ATOM   6588  C  CA  . GLY B  1  226 ? 23.648  -45.338 -34.594 1.00 63.12  ? 252  GLY B CA  1 
ATOM   6589  C  C   . GLY B  1  226 ? 23.879  -43.999 -35.258 1.00 63.19  ? 252  GLY B C   1 
ATOM   6590  O  O   . GLY B  1  226 ? 24.929  -43.770 -35.862 1.00 63.72  ? 252  GLY B O   1 
ATOM   6591  N  N   . LEU B  1  227 ? 22.891  -43.115 -35.149 1.00 63.50  ? 253  LEU B N   1 
ATOM   6592  C  CA  . LEU B  1  227 ? 22.967  -41.779 -35.744 1.00 63.43  ? 253  LEU B CA  1 
ATOM   6593  C  C   . LEU B  1  227 ? 23.980  -40.897 -35.045 1.00 63.90  ? 253  LEU B C   1 
ATOM   6594  O  O   . LEU B  1  227 ? 24.291  -41.104 -33.863 1.00 64.57  ? 253  LEU B O   1 
ATOM   6595  C  CB  . LEU B  1  227 ? 21.601  -41.080 -35.673 1.00 61.83  ? 253  LEU B CB  1 
ATOM   6596  C  CG  . LEU B  1  227 ? 21.530  -39.578 -35.989 1.00 58.61  ? 253  LEU B CG  1 
ATOM   6597  C  CD1 . LEU B  1  227 ? 21.776  -39.336 -37.462 1.00 59.39  ? 253  LEU B CD1 1 
ATOM   6598  C  CD2 . LEU B  1  227 ? 20.165  -39.047 -35.608 1.00 58.33  ? 253  LEU B CD2 1 
ATOM   6599  N  N   . GLU B  1  228 ? 24.500  -39.922 -35.788 1.00 63.80  ? 254  GLU B N   1 
ATOM   6600  C  CA  . GLU B  1  228 ? 25.422  -38.943 -35.227 1.00 63.07  ? 254  GLU B CA  1 
ATOM   6601  C  C   . GLU B  1  228 ? 24.862  -37.575 -35.598 1.00 61.71  ? 254  GLU B C   1 
ATOM   6602  O  O   . GLU B  1  228 ? 24.884  -37.187 -36.767 1.00 61.84  ? 254  GLU B O   1 
ATOM   6603  C  CB  . GLU B  1  228 ? 26.838  -39.082 -35.795 1.00 65.14  ? 254  GLU B CB  1 
ATOM   6604  C  CG  . GLU B  1  228 ? 27.899  -38.469 -34.856 1.00 69.62  ? 254  GLU B CG  1 
ATOM   6605  C  CD  . GLU B  1  228 ? 29.311  -38.377 -35.448 1.00 71.46  ? 254  GLU B CD  1 
ATOM   6606  O  OE1 . GLU B  1  228 ? 29.531  -37.532 -36.342 1.00 72.79  ? 254  GLU B OE1 1 
ATOM   6607  O  OE2 . GLU B  1  228 ? 30.196  -39.153 -35.016 1.00 72.99  ? 254  GLU B OE2 1 
ATOM   6608  N  N   . VAL B  1  229 ? 24.334  -36.861 -34.607 1.00 60.07  ? 255  VAL B N   1 
ATOM   6609  C  CA  . VAL B  1  229 ? 23.777  -35.526 -34.828 1.00 59.04  ? 255  VAL B CA  1 
ATOM   6610  C  C   . VAL B  1  229 ? 24.508  -34.513 -33.985 1.00 57.29  ? 255  VAL B C   1 
ATOM   6611  O  O   . VAL B  1  229 ? 24.880  -34.793 -32.848 1.00 56.75  ? 255  VAL B O   1 
ATOM   6612  C  CB  . VAL B  1  229 ? 22.295  -35.433 -34.437 1.00 60.06  ? 255  VAL B CB  1 
ATOM   6613  C  CG1 . VAL B  1  229 ? 21.430  -35.867 -35.592 1.00 61.90  ? 255  VAL B CG1 1 
ATOM   6614  C  CG2 . VAL B  1  229 ? 22.026  -36.292 -33.193 1.00 60.91  ? 255  VAL B CG2 1 
ATOM   6615  N  N   . HIS B  1  230 ? 24.722  -33.329 -34.534 1.00 54.97  ? 256  HIS B N   1 
ATOM   6616  C  CA  . HIS B  1  230 ? 25.401  -32.314 -33.762 1.00 53.38  ? 256  HIS B CA  1 
ATOM   6617  C  C   . HIS B  1  230 ? 24.419  -31.753 -32.733 1.00 51.63  ? 256  HIS B C   1 
ATOM   6618  O  O   . HIS B  1  230 ? 24.724  -31.651 -31.549 1.00 50.78  ? 256  HIS B O   1 
ATOM   6619  C  CB  . HIS B  1  230 ? 25.897  -31.191 -34.672 1.00 55.02  ? 256  HIS B CB  1 
ATOM   6620  C  CG  . HIS B  1  230 ? 26.502  -30.043 -33.923 1.00 56.44  ? 256  HIS B CG  1 
ATOM   6621  N  ND1 . HIS B  1  230 ? 27.570  -30.197 -33.067 1.00 57.20  ? 256  HIS B ND1 1 
ATOM   6622  C  CD2 . HIS B  1  230 ? 26.151  -28.737 -33.858 1.00 56.77  ? 256  HIS B CD2 1 
ATOM   6623  C  CE1 . HIS B  1  230 ? 27.851  -29.034 -32.503 1.00 56.99  ? 256  HIS B CE1 1 
ATOM   6624  N  NE2 . HIS B  1  230 ? 27.004  -28.133 -32.966 1.00 56.76  ? 256  HIS B NE2 1 
ATOM   6625  N  N   . ARG B  1  231 ? 23.224  -31.412 -33.206 1.00 49.88  ? 257  ARG B N   1 
ATOM   6626  C  CA  . ARG B  1  231 ? 22.165  -30.844 -32.374 1.00 47.64  ? 257  ARG B CA  1 
ATOM   6627  C  C   . ARG B  1  231 ? 20.883  -31.644 -32.626 1.00 47.04  ? 257  ARG B C   1 
ATOM   6628  O  O   . ARG B  1  231 ? 20.470  -31.800 -33.777 1.00 48.54  ? 257  ARG B O   1 
ATOM   6629  C  CB  . ARG B  1  231 ? 21.944  -29.374 -32.771 1.00 46.14  ? 257  ARG B CB  1 
ATOM   6630  C  CG  . ARG B  1  231 ? 21.045  -28.600 -31.851 1.00 44.11  ? 257  ARG B CG  1 
ATOM   6631  C  CD  . ARG B  1  231 ? 20.747  -27.190 -32.352 1.00 43.46  ? 257  ARG B CD  1 
ATOM   6632  N  NE  . ARG B  1  231 ? 19.839  -26.479 -31.445 1.00 42.14  ? 257  ARG B NE  1 
ATOM   6633  C  CZ  . ARG B  1  231 ? 20.111  -26.264 -30.160 1.00 42.44  ? 257  ARG B CZ  1 
ATOM   6634  N  NH1 . ARG B  1  231 ? 21.260  -26.698 -29.642 1.00 40.90  ? 257  ARG B NH1 1 
ATOM   6635  N  NH2 . ARG B  1  231 ? 19.234  -25.640 -29.387 1.00 39.75  ? 257  ARG B NH2 1 
ATOM   6636  N  N   . LEU B  1  232 ? 20.259  -32.154 -31.565 1.00 44.56  ? 258  LEU B N   1 
ATOM   6637  C  CA  . LEU B  1  232 ? 19.018  -32.918 -31.705 1.00 43.55  ? 258  LEU B CA  1 
ATOM   6638  C  C   . LEU B  1  232 ? 17.897  -32.216 -30.943 1.00 44.68  ? 258  LEU B C   1 
ATOM   6639  O  O   . LEU B  1  232 ? 18.036  -31.926 -29.749 1.00 45.88  ? 258  LEU B O   1 
ATOM   6640  C  CB  . LEU B  1  232 ? 19.188  -34.348 -31.169 1.00 41.46  ? 258  LEU B CB  1 
ATOM   6641  C  CG  . LEU B  1  232 ? 17.907  -35.180 -30.947 1.00 40.34  ? 258  LEU B CG  1 
ATOM   6642  C  CD1 . LEU B  1  232 ? 17.242  -35.445 -32.281 1.00 38.81  ? 258  LEU B CD1 1 
ATOM   6643  C  CD2 . LEU B  1  232 ? 18.223  -36.492 -30.252 1.00 36.20  ? 258  LEU B CD2 1 
ATOM   6644  N  N   . VAL B  1  233 ? 16.785  -31.943 -31.625 1.00 44.33  ? 259  VAL B N   1 
ATOM   6645  C  CA  . VAL B  1  233 ? 15.658  -31.270 -30.984 1.00 44.81  ? 259  VAL B CA  1 
ATOM   6646  C  C   . VAL B  1  233 ? 14.370  -32.087 -30.955 1.00 45.28  ? 259  VAL B C   1 
ATOM   6647  O  O   . VAL B  1  233 ? 13.811  -32.402 -32.001 1.00 44.15  ? 259  VAL B O   1 
ATOM   6648  C  CB  . VAL B  1  233 ? 15.359  -29.951 -31.678 1.00 44.59  ? 259  VAL B CB  1 
ATOM   6649  C  CG1 . VAL B  1  233 ? 14.341  -29.169 -30.891 1.00 44.27  ? 259  VAL B CG1 1 
ATOM   6650  C  CG2 . VAL B  1  233 ? 16.628  -29.172 -31.837 1.00 45.25  ? 259  VAL B CG2 1 
ATOM   6651  N  N   . LEU B  1  234 ? 13.908  -32.408 -29.745 1.00 47.05  ? 260  LEU B N   1 
ATOM   6652  C  CA  . LEU B  1  234 ? 12.680  -33.176 -29.527 1.00 48.43  ? 260  LEU B CA  1 
ATOM   6653  C  C   . LEU B  1  234 ? 11.626  -32.292 -28.857 1.00 49.93  ? 260  LEU B C   1 
ATOM   6654  O  O   . LEU B  1  234 ? 11.884  -31.123 -28.590 1.00 50.85  ? 260  LEU B O   1 
ATOM   6655  C  CB  . LEU B  1  234 ? 12.961  -34.396 -28.648 1.00 45.13  ? 260  LEU B CB  1 
ATOM   6656  C  CG  . LEU B  1  234 ? 14.018  -35.360 -29.185 1.00 45.20  ? 260  LEU B CG  1 
ATOM   6657  C  CD1 . LEU B  1  234 ? 13.999  -36.616 -28.325 1.00 44.68  ? 260  LEU B CD1 1 
ATOM   6658  C  CD2 . LEU B  1  234 ? 13.750  -35.700 -30.653 1.00 42.62  ? 260  LEU B CD2 1 
ATOM   6659  N  N   . GLY B  1  235 ? 10.447  -32.844 -28.578 1.00 50.25  ? 261  GLY B N   1 
ATOM   6660  C  CA  . GLY B  1  235 ? 9.398   -32.055 -27.955 1.00 49.95  ? 261  GLY B CA  1 
ATOM   6661  C  C   . GLY B  1  235 ? 8.159   -31.985 -28.828 1.00 50.77  ? 261  GLY B C   1 
ATOM   6662  O  O   . GLY B  1  235 ? 8.074   -32.684 -29.834 1.00 52.07  ? 261  GLY B O   1 
ATOM   6663  N  N   . GLU B  1  236 ? 7.207   -31.136 -28.456 1.00 50.33  ? 262  GLU B N   1 
ATOM   6664  C  CA  . GLU B  1  236 ? 5.958   -30.985 -29.198 1.00 51.03  ? 262  GLU B CA  1 
ATOM   6665  C  C   . GLU B  1  236 ? 5.503   -29.535 -29.320 1.00 50.57  ? 262  GLU B C   1 
ATOM   6666  O  O   . GLU B  1  236 ? 6.193   -28.609 -28.885 1.00 51.08  ? 262  GLU B O   1 
ATOM   6667  C  CB  . GLU B  1  236 ? 4.866   -31.786 -28.503 1.00 53.63  ? 262  GLU B CB  1 
ATOM   6668  C  CG  . GLU B  1  236 ? 4.977   -31.747 -26.983 1.00 57.62  ? 262  GLU B CG  1 
ATOM   6669  C  CD  . GLU B  1  236 ? 4.191   -32.866 -26.306 1.00 61.70  ? 262  GLU B CD  1 
ATOM   6670  O  OE1 . GLU B  1  236 ? 3.982   -33.909 -26.974 1.00 62.82  ? 262  GLU B OE1 1 
ATOM   6671  O  OE2 . GLU B  1  236 ? 3.799   -32.721 -25.112 1.00 61.95  ? 262  GLU B OE2 1 
ATOM   6672  N  N   . PHE B  1  237 ? 4.336   -29.338 -29.920 1.00 48.63  ? 263  PHE B N   1 
ATOM   6673  C  CA  . PHE B  1  237 ? 3.793   -28.001 -30.070 1.00 47.96  ? 263  PHE B CA  1 
ATOM   6674  C  C   . PHE B  1  237 ? 2.609   -27.815 -29.147 1.00 48.09  ? 263  PHE B C   1 
ATOM   6675  O  O   . PHE B  1  237 ? 1.780   -28.702 -29.005 1.00 49.95  ? 263  PHE B O   1 
ATOM   6676  C  CB  . PHE B  1  237 ? 3.373   -27.748 -31.513 1.00 49.78  ? 263  PHE B CB  1 
ATOM   6677  C  CG  . PHE B  1  237 ? 4.524   -27.530 -32.437 1.00 50.95  ? 263  PHE B CG  1 
ATOM   6678  C  CD1 . PHE B  1  237 ? 5.018   -28.573 -33.213 1.00 52.15  ? 263  PHE B CD1 1 
ATOM   6679  C  CD2 . PHE B  1  237 ? 5.145   -26.287 -32.495 1.00 50.45  ? 263  PHE B CD2 1 
ATOM   6680  C  CE1 . PHE B  1  237 ? 6.121   -28.385 -34.036 1.00 52.36  ? 263  PHE B CE1 1 
ATOM   6681  C  CE2 . PHE B  1  237 ? 6.239   -26.081 -33.303 1.00 51.37  ? 263  PHE B CE2 1 
ATOM   6682  C  CZ  . PHE B  1  237 ? 6.735   -27.132 -34.082 1.00 53.24  ? 263  PHE B CZ  1 
ATOM   6683  N  N   . ARG B  1  238 ? 2.544   -26.647 -28.525 1.00 47.80  ? 264  ARG B N   1 
ATOM   6684  C  CA  . ARG B  1  238 ? 1.506   -26.301 -27.567 1.00 47.92  ? 264  ARG B CA  1 
ATOM   6685  C  C   . ARG B  1  238 ? 0.104   -26.356 -28.122 1.00 47.98  ? 264  ARG B C   1 
ATOM   6686  O  O   . ARG B  1  238 ? -0.835  -26.657 -27.401 1.00 48.85  ? 264  ARG B O   1 
ATOM   6687  C  CB  . ARG B  1  238 ? 1.788   -24.907 -27.030 1.00 48.03  ? 264  ARG B CB  1 
ATOM   6688  C  CG  . ARG B  1  238 ? 1.130   -24.542 -25.728 1.00 49.41  ? 264  ARG B CG  1 
ATOM   6689  C  CD  . ARG B  1  238 ? 1.773   -23.265 -25.236 1.00 52.32  ? 264  ARG B CD  1 
ATOM   6690  N  NE  . ARG B  1  238 ? 1.106   -22.664 -24.089 1.00 56.55  ? 264  ARG B NE  1 
ATOM   6691  C  CZ  . ARG B  1  238 ? 1.454   -21.490 -23.563 1.00 58.85  ? 264  ARG B CZ  1 
ATOM   6692  N  NH1 . ARG B  1  238 ? 2.467   -20.799 -24.083 1.00 59.92  ? 264  ARG B NH1 1 
ATOM   6693  N  NH2 . ARG B  1  238 ? 0.780   -20.990 -22.529 1.00 58.91  ? 264  ARG B NH2 1 
ATOM   6694  N  N   . ASN B  1  239 ? -0.036  -26.058 -29.407 1.00 49.37  ? 265  ASN B N   1 
ATOM   6695  C  CA  . ASN B  1  239 ? -1.348  -26.046 -30.060 1.00 49.94  ? 265  ASN B CA  1 
ATOM   6696  C  C   . ASN B  1  239 ? -1.662  -27.273 -30.917 1.00 49.55  ? 265  ASN B C   1 
ATOM   6697  O  O   . ASN B  1  239 ? -2.430  -27.186 -31.864 1.00 48.60  ? 265  ASN B O   1 
ATOM   6698  C  CB  . ASN B  1  239 ? -1.492  -24.769 -30.906 1.00 51.30  ? 265  ASN B CB  1 
ATOM   6699  C  CG  . ASN B  1  239 ? -0.479  -24.690 -32.060 1.00 51.95  ? 265  ASN B CG  1 
ATOM   6700  O  OD1 . ASN B  1  239 ? 0.675   -25.115 -31.940 1.00 51.32  ? 265  ASN B OD1 1 
ATOM   6701  N  ND2 . ASN B  1  239 ? -0.909  -24.111 -33.171 1.00 52.49  ? 265  ASN B ND2 1 
ATOM   6702  N  N   . GLU B  1  240 ? -1.070  -28.409 -30.570 1.00 50.53  ? 266  GLU B N   1 
ATOM   6703  C  CA  . GLU B  1  240 ? -1.298  -29.655 -31.287 1.00 52.38  ? 266  GLU B CA  1 
ATOM   6704  C  C   . GLU B  1  240 ? -1.355  -30.870 -30.348 1.00 53.03  ? 266  GLU B C   1 
ATOM   6705  O  O   . GLU B  1  240 ? -1.264  -30.726 -29.127 1.00 54.11  ? 266  GLU B O   1 
ATOM   6706  C  CB  . GLU B  1  240 ? -0.219  -29.865 -32.338 1.00 52.67  ? 266  GLU B CB  1 
ATOM   6707  C  CG  . GLU B  1  240 ? -0.768  -29.854 -33.743 1.00 58.26  ? 266  GLU B CG  1 
ATOM   6708  C  CD  . GLU B  1  240 ? -0.266  -28.671 -34.533 1.00 62.14  ? 266  GLU B CD  1 
ATOM   6709  O  OE1 . GLU B  1  240 ? 0.084   -27.661 -33.884 1.00 64.97  ? 266  GLU B OE1 1 
ATOM   6710  O  OE2 . GLU B  1  240 ? -0.226  -28.740 -35.789 1.00 63.66  ? 266  GLU B OE2 1 
ATOM   6711  N  N   . GLY B  1  241 ? -1.509  -32.062 -30.918 1.00 53.01  ? 267  GLY B N   1 
ATOM   6712  C  CA  . GLY B  1  241 ? -1.597  -33.274 -30.112 1.00 54.29  ? 267  GLY B CA  1 
ATOM   6713  C  C   . GLY B  1  241 ? -0.357  -33.646 -29.320 1.00 55.31  ? 267  GLY B C   1 
ATOM   6714  O  O   . GLY B  1  241 ? 0.692   -33.932 -29.894 1.00 56.83  ? 267  GLY B O   1 
ATOM   6715  N  N   . ASN B  1  242 ? -0.492  -33.695 -28.000 1.00 55.63  ? 268  ASN B N   1 
ATOM   6716  C  CA  . ASN B  1  242 ? 0.632   -33.997 -27.118 1.00 57.25  ? 268  ASN B CA  1 
ATOM   6717  C  C   . ASN B  1  242 ? 0.654   -35.424 -26.554 1.00 58.21  ? 268  ASN B C   1 
ATOM   6718  O  O   . ASN B  1  242 ? -0.342  -36.131 -26.610 1.00 60.54  ? 268  ASN B O   1 
ATOM   6719  C  CB  . ASN B  1  242 ? 0.632   -32.975 -25.969 1.00 58.13  ? 268  ASN B CB  1 
ATOM   6720  C  CG  . ASN B  1  242 ? 0.633   -31.513 -26.469 1.00 59.84  ? 268  ASN B CG  1 
ATOM   6721  O  OD1 . ASN B  1  242 ? 0.213   -30.593 -25.753 1.00 59.12  ? 268  ASN B OD1 1 
ATOM   6722  N  ND2 . ASN B  1  242 ? 1.117   -31.301 -27.694 1.00 59.11  ? 268  ASN B ND2 1 
ATOM   6723  N  N   . LEU B  1  243 ? 1.796   -35.843 -26.019 1.00 58.38  ? 269  LEU B N   1 
ATOM   6724  C  CA  . LEU B  1  243 ? 1.939   -37.170 -25.431 1.00 59.19  ? 269  LEU B CA  1 
ATOM   6725  C  C   . LEU B  1  243 ? 1.268   -37.148 -24.078 1.00 61.00  ? 269  LEU B C   1 
ATOM   6726  O  O   . LEU B  1  243 ? 1.380   -36.163 -23.360 1.00 61.47  ? 269  LEU B O   1 
ATOM   6727  C  CB  . LEU B  1  243 ? 3.414   -37.510 -25.218 1.00 58.48  ? 269  LEU B CB  1 
ATOM   6728  C  CG  . LEU B  1  243 ? 4.347   -37.568 -26.425 1.00 58.41  ? 269  LEU B CG  1 
ATOM   6729  C  CD1 . LEU B  1  243 ? 5.767   -37.758 -25.935 1.00 58.75  ? 269  LEU B CD1 1 
ATOM   6730  C  CD2 . LEU B  1  243 ? 3.950   -38.701 -27.355 1.00 58.17  ? 269  LEU B CD2 1 
ATOM   6731  N  N   . GLU B  1  244 ? 0.593   -38.227 -23.703 1.00 64.41  ? 270  GLU B N   1 
ATOM   6732  C  CA  . GLU B  1  244 ? -0.065  -38.226 -22.407 1.00 68.61  ? 270  GLU B CA  1 
ATOM   6733  C  C   . GLU B  1  244 ? 0.870   -38.606 -21.270 1.00 69.02  ? 270  GLU B C   1 
ATOM   6734  O  O   . GLU B  1  244 ? 0.544   -38.389 -20.108 1.00 70.67  ? 270  GLU B O   1 
ATOM   6735  C  CB  . GLU B  1  244 ? -1.301  -39.133 -22.400 1.00 71.59  ? 270  GLU B CB  1 
ATOM   6736  C  CG  . GLU B  1  244 ? -1.020  -40.619 -22.327 1.00 76.65  ? 270  GLU B CG  1 
ATOM   6737  C  CD  . GLU B  1  244 ? -2.285  -41.425 -22.063 1.00 79.44  ? 270  GLU B CD  1 
ATOM   6738  O  OE1 . GLU B  1  244 ? -3.219  -41.367 -22.906 1.00 79.87  ? 270  GLU B OE1 1 
ATOM   6739  O  OE2 . GLU B  1  244 ? -2.339  -42.112 -21.011 1.00 80.73  ? 270  GLU B OE2 1 
ATOM   6740  N  N   . LYS B  1  245 ? 2.022   -39.181 -21.589 1.00 69.48  ? 271  LYS B N   1 
ATOM   6741  C  CA  . LYS B  1  245 ? 2.983   -39.519 -20.542 1.00 70.71  ? 271  LYS B CA  1 
ATOM   6742  C  C   . LYS B  1  245 ? 4.415   -39.377 -21.043 1.00 71.30  ? 271  LYS B C   1 
ATOM   6743  O  O   . LYS B  1  245 ? 4.700   -39.557 -22.234 1.00 70.98  ? 271  LYS B O   1 
ATOM   6744  C  CB  . LYS B  1  245 ? 2.755   -40.934 -19.984 1.00 70.81  ? 271  LYS B CB  1 
ATOM   6745  C  CG  . LYS B  1  245 ? 2.989   -42.072 -20.963 1.00 71.65  ? 271  LYS B CG  1 
ATOM   6746  C  CD  . LYS B  1  245 ? 1.683   -42.716 -21.445 1.00 71.61  ? 271  LYS B CD  1 
ATOM   6747  C  CE  . LYS B  1  245 ? 0.893   -43.349 -20.286 1.00 71.70  ? 271  LYS B CE  1 
ATOM   6748  N  NZ  . LYS B  1  245 ? 1.682   -44.339 -19.488 1.00 69.66  ? 271  LYS B NZ  1 
ATOM   6749  N  N   . PHE B  1  246 ? 5.315   -39.044 -20.123 1.00 71.25  ? 272  PHE B N   1 
ATOM   6750  C  CA  . PHE B  1  246 ? 6.717   -38.855 -20.462 1.00 71.31  ? 272  PHE B CA  1 
ATOM   6751  C  C   . PHE B  1  246 ? 7.534   -39.237 -19.232 1.00 72.12  ? 272  PHE B C   1 
ATOM   6752  O  O   . PHE B  1  246 ? 8.116   -38.373 -18.575 1.00 72.77  ? 272  PHE B O   1 
ATOM   6753  C  CB  . PHE B  1  246 ? 6.944   -37.386 -20.835 1.00 69.38  ? 272  PHE B CB  1 
ATOM   6754  C  CG  . PHE B  1  246 ? 8.145   -37.152 -21.694 1.00 67.43  ? 272  PHE B CG  1 
ATOM   6755  C  CD1 . PHE B  1  246 ? 9.403   -37.005 -21.128 1.00 66.47  ? 272  PHE B CD1 1 
ATOM   6756  C  CD2 . PHE B  1  246 ? 8.015   -37.100 -23.084 1.00 66.71  ? 272  PHE B CD2 1 
ATOM   6757  C  CE1 . PHE B  1  246 ? 10.521  -36.814 -21.936 1.00 67.10  ? 272  PHE B CE1 1 
ATOM   6758  C  CE2 . PHE B  1  246 ? 9.121   -36.910 -23.903 1.00 65.58  ? 272  PHE B CE2 1 
ATOM   6759  C  CZ  . PHE B  1  246 ? 10.383  -36.765 -23.334 1.00 66.55  ? 272  PHE B CZ  1 
ATOM   6760  N  N   . ASP B  1  247 ? 7.564   -40.535 -18.924 1.00 72.61  ? 273  ASP B N   1 
ATOM   6761  C  CA  . ASP B  1  247 ? 8.286   -41.043 -17.758 1.00 72.51  ? 273  ASP B CA  1 
ATOM   6762  C  C   . ASP B  1  247 ? 9.769   -41.273 -18.001 1.00 71.20  ? 273  ASP B C   1 
ATOM   6763  O  O   . ASP B  1  247 ? 10.255  -41.132 -19.116 1.00 70.73  ? 273  ASP B O   1 
ATOM   6764  C  CB  . ASP B  1  247 ? 7.657   -42.342 -17.262 1.00 75.33  ? 273  ASP B CB  1 
ATOM   6765  C  CG  . ASP B  1  247 ? 7.622   -43.419 -18.333 1.00 77.94  ? 273  ASP B CG  1 
ATOM   6766  O  OD1 . ASP B  1  247 ? 8.633   -43.591 -19.057 1.00 78.82  ? 273  ASP B OD1 1 
ATOM   6767  O  OD2 . ASP B  1  247 ? 6.580   -44.101 -18.441 1.00 80.25  ? 273  ASP B OD2 1 
ATOM   6768  N  N   . LYS B  1  248 ? 10.471  -41.665 -16.944 1.00 69.91  ? 274  LYS B N   1 
ATOM   6769  C  CA  . LYS B  1  248 ? 11.911  -41.865 -16.997 1.00 68.63  ? 274  LYS B CA  1 
ATOM   6770  C  C   . LYS B  1  248 ? 12.477  -42.762 -18.080 1.00 66.89  ? 274  LYS B C   1 
ATOM   6771  O  O   . LYS B  1  248 ? 13.685  -42.931 -18.158 1.00 66.91  ? 274  LYS B O   1 
ATOM   6772  C  CB  . LYS B  1  248 ? 12.426  -42.334 -15.629 1.00 70.06  ? 274  LYS B CB  1 
ATOM   6773  C  CG  . LYS B  1  248 ? 11.978  -43.718 -15.201 1.00 73.58  ? 274  LYS B CG  1 
ATOM   6774  C  CD  . LYS B  1  248 ? 12.477  -44.040 -13.786 1.00 76.77  ? 274  LYS B CD  1 
ATOM   6775  C  CE  . LYS B  1  248 ? 11.832  -43.125 -12.730 1.00 78.21  ? 274  LYS B CE  1 
ATOM   6776  N  NZ  . LYS B  1  248 ? 12.389  -43.297 -11.351 1.00 76.14  ? 274  LYS B NZ  1 
ATOM   6777  N  N   . SER B  1  249 ? 11.637  -43.332 -18.929 1.00 65.85  ? 275  SER B N   1 
ATOM   6778  C  CA  . SER B  1  249 ? 12.163  -44.203 -19.971 1.00 65.04  ? 275  SER B CA  1 
ATOM   6779  C  C   . SER B  1  249 ? 12.004  -43.626 -21.373 1.00 65.72  ? 275  SER B C   1 
ATOM   6780  O  O   . SER B  1  249 ? 12.606  -44.116 -22.327 1.00 66.99  ? 275  SER B O   1 
ATOM   6781  C  CB  . SER B  1  249 ? 11.466  -45.552 -19.926 1.00 63.66  ? 275  SER B CB  1 
ATOM   6782  O  OG  . SER B  1  249 ? 10.150  -45.427 -20.428 1.00 62.33  ? 275  SER B OG  1 
ATOM   6783  N  N   . ALA B  1  250 ? 11.191  -42.585 -21.500 1.00 65.32  ? 276  ALA B N   1 
ATOM   6784  C  CA  . ALA B  1  250 ? 10.934  -41.961 -22.795 1.00 63.14  ? 276  ALA B CA  1 
ATOM   6785  C  C   . ALA B  1  250 ? 12.183  -41.702 -23.641 1.00 61.80  ? 276  ALA B C   1 
ATOM   6786  O  O   . ALA B  1  250 ? 12.138  -41.790 -24.866 1.00 58.19  ? 276  ALA B O   1 
ATOM   6787  C  CB  . ALA B  1  250 ? 10.175  -40.662 -22.584 1.00 63.48  ? 276  ALA B CB  1 
ATOM   6788  N  N   . LEU B  1  251 ? 13.296  -41.402 -22.978 1.00 62.10  ? 277  LEU B N   1 
ATOM   6789  C  CA  . LEU B  1  251 ? 14.535  -41.083 -23.683 1.00 62.99  ? 277  LEU B CA  1 
ATOM   6790  C  C   . LEU B  1  251 ? 15.646  -42.132 -23.647 1.00 64.03  ? 277  LEU B C   1 
ATOM   6791  O  O   . LEU B  1  251 ? 16.781  -41.823 -23.987 1.00 65.01  ? 277  LEU B O   1 
ATOM   6792  C  CB  . LEU B  1  251 ? 15.077  -39.740 -23.167 1.00 59.78  ? 277  LEU B CB  1 
ATOM   6793  C  CG  . LEU B  1  251 ? 14.755  -38.434 -23.912 1.00 57.36  ? 277  LEU B CG  1 
ATOM   6794  C  CD1 . LEU B  1  251 ? 13.345  -38.415 -24.426 1.00 56.34  ? 277  LEU B CD1 1 
ATOM   6795  C  CD2 . LEU B  1  251 ? 14.977  -37.274 -22.977 1.00 55.97  ? 277  LEU B CD2 1 
ATOM   6796  N  N   . GLU B  1  252 ? 15.324  -43.361 -23.252 1.00 65.17  ? 278  GLU B N   1 
ATOM   6797  C  CA  . GLU B  1  252 ? 16.320  -44.436 -23.189 1.00 65.53  ? 278  GLU B CA  1 
ATOM   6798  C  C   . GLU B  1  252 ? 17.155  -44.521 -24.449 1.00 65.15  ? 278  GLU B C   1 
ATOM   6799  O  O   . GLU B  1  252 ? 18.377  -44.549 -24.390 1.00 63.81  ? 278  GLU B O   1 
ATOM   6800  C  CB  . GLU B  1  252 ? 15.657  -45.798 -23.023 1.00 68.07  ? 278  GLU B CB  1 
ATOM   6801  C  CG  . GLU B  1  252 ? 15.071  -46.124 -21.673 1.00 72.87  ? 278  GLU B CG  1 
ATOM   6802  C  CD  . GLU B  1  252 ? 14.082  -47.297 -21.757 1.00 76.21  ? 278  GLU B CD  1 
ATOM   6803  O  OE1 . GLU B  1  252 ? 13.647  -47.783 -20.679 1.00 78.69  ? 278  GLU B OE1 1 
ATOM   6804  O  OE2 . GLU B  1  252 ? 13.730  -47.717 -22.894 1.00 73.32  ? 278  GLU B OE2 1 
ATOM   6805  N  N   . GLY B  1  253 ? 16.475  -44.585 -25.590 1.00 65.44  ? 279  GLY B N   1 
ATOM   6806  C  CA  . GLY B  1  253 ? 17.149  -44.724 -26.873 1.00 66.93  ? 279  GLY B CA  1 
ATOM   6807  C  C   . GLY B  1  253 ? 18.308  -43.804 -27.217 1.00 66.92  ? 279  GLY B C   1 
ATOM   6808  O  O   . GLY B  1  253 ? 19.246  -44.209 -27.907 1.00 66.72  ? 279  GLY B O   1 
ATOM   6809  N  N   . LEU B  1  254 ? 18.241  -42.564 -26.757 1.00 67.48  ? 280  LEU B N   1 
ATOM   6810  C  CA  . LEU B  1  254 ? 19.280  -41.583 -27.033 1.00 67.02  ? 280  LEU B CA  1 
ATOM   6811  C  C   . LEU B  1  254 ? 20.672  -42.033 -26.601 1.00 67.51  ? 280  LEU B C   1 
ATOM   6812  O  O   . LEU B  1  254 ? 21.682  -41.435 -26.990 1.00 67.95  ? 280  LEU B O   1 
ATOM   6813  C  CB  . LEU B  1  254 ? 18.922  -40.257 -26.353 1.00 66.47  ? 280  LEU B CB  1 
ATOM   6814  C  CG  . LEU B  1  254 ? 18.029  -39.283 -27.123 1.00 65.47  ? 280  LEU B CG  1 
ATOM   6815  C  CD1 . LEU B  1  254 ? 17.001  -40.029 -27.932 1.00 66.00  ? 280  LEU B CD1 1 
ATOM   6816  C  CD2 . LEU B  1  254 ? 17.368  -38.336 -26.143 1.00 65.33  ? 280  LEU B CD2 1 
ATOM   6817  N  N   . CYS B  1  255 ? 20.722  -43.084 -25.793 1.00 67.29  ? 281  CYS B N   1 
ATOM   6818  C  CA  . CYS B  1  255 ? 21.989  -43.622 -25.307 1.00 67.59  ? 281  CYS B CA  1 
ATOM   6819  C  C   . CYS B  1  255 ? 22.783  -44.301 -26.431 1.00 66.45  ? 281  CYS B C   1 
ATOM   6820  O  O   . CYS B  1  255 ? 24.006  -44.426 -26.353 1.00 65.62  ? 281  CYS B O   1 
ATOM   6821  C  CB  . CYS B  1  255 ? 21.721  -44.611 -24.171 1.00 69.59  ? 281  CYS B CB  1 
ATOM   6822  S  SG  . CYS B  1  255 ? 21.877  -43.934 -22.472 1.00 75.76  ? 281  CYS B SG  1 
ATOM   6823  N  N   . ASN B  1  256 ? 22.075  -44.721 -27.477 1.00 65.41  ? 282  ASN B N   1 
ATOM   6824  C  CA  . ASN B  1  256 ? 22.680  -45.369 -28.634 1.00 63.82  ? 282  ASN B CA  1 
ATOM   6825  C  C   . ASN B  1  256 ? 22.784  -44.393 -29.794 1.00 63.55  ? 282  ASN B C   1 
ATOM   6826  O  O   . ASN B  1  256 ? 22.681  -44.782 -30.955 1.00 64.55  ? 282  ASN B O   1 
ATOM   6827  C  CB  . ASN B  1  256 ? 21.850  -46.577 -29.075 1.00 64.19  ? 282  ASN B CB  1 
ATOM   6828  C  CG  . ASN B  1  256 ? 22.054  -47.782 -28.188 1.00 65.58  ? 282  ASN B CG  1 
ATOM   6829  O  OD1 . ASN B  1  256 ? 21.429  -48.824 -28.394 1.00 66.28  ? 282  ASN B OD1 1 
ATOM   6830  N  ND2 . ASN B  1  256 ? 22.935  -47.655 -27.198 1.00 65.58  ? 282  ASN B ND2 1 
ATOM   6831  N  N   . LEU B  1  257 ? 22.968  -43.120 -29.471 1.00 63.40  ? 283  LEU B N   1 
ATOM   6832  C  CA  . LEU B  1  257 ? 23.097  -42.061 -30.471 1.00 62.77  ? 283  LEU B CA  1 
ATOM   6833  C  C   . LEU B  1  257 ? 24.304  -41.247 -30.040 1.00 62.36  ? 283  LEU B C   1 
ATOM   6834  O  O   . LEU B  1  257 ? 24.733  -41.337 -28.889 1.00 62.51  ? 283  LEU B O   1 
ATOM   6835  C  CB  . LEU B  1  257 ? 21.881  -41.126 -30.448 1.00 62.91  ? 283  LEU B CB  1 
ATOM   6836  C  CG  . LEU B  1  257 ? 20.474  -41.422 -30.978 1.00 62.38  ? 283  LEU B CG  1 
ATOM   6837  C  CD1 . LEU B  1  257 ? 20.388  -40.984 -32.419 1.00 62.76  ? 283  LEU B CD1 1 
ATOM   6838  C  CD2 . LEU B  1  257 ? 20.123  -42.885 -30.803 1.00 62.35  ? 283  LEU B CD2 1 
ATOM   6839  N  N   . THR B  1  258 ? 24.847  -40.446 -30.947 1.00 61.77  ? 284  THR B N   1 
ATOM   6840  C  CA  . THR B  1  258 ? 25.975  -39.594 -30.598 1.00 61.12  ? 284  THR B CA  1 
ATOM   6841  C  C   . THR B  1  258 ? 25.476  -38.170 -30.754 1.00 59.93  ? 284  THR B C   1 
ATOM   6842  O  O   . THR B  1  258 ? 25.364  -37.661 -31.872 1.00 59.92  ? 284  THR B O   1 
ATOM   6843  C  CB  . THR B  1  258 ? 27.178  -39.844 -31.514 1.00 62.85  ? 284  THR B CB  1 
ATOM   6844  O  OG1 . THR B  1  258 ? 27.594  -41.210 -31.386 1.00 65.88  ? 284  THR B OG1 1 
ATOM   6845  C  CG2 . THR B  1  258 ? 28.342  -38.942 -31.128 1.00 62.91  ? 284  THR B CG2 1 
ATOM   6846  N  N   . ILE B  1  259 ? 25.160  -37.542 -29.621 1.00 58.41  ? 285  ILE B N   1 
ATOM   6847  C  CA  . ILE B  1  259 ? 24.619  -36.183 -29.602 1.00 56.32  ? 285  ILE B CA  1 
ATOM   6848  C  C   . ILE B  1  259 ? 25.592  -35.184 -28.991 1.00 54.79  ? 285  ILE B C   1 
ATOM   6849  O  O   . ILE B  1  259 ? 26.240  -35.481 -27.995 1.00 55.80  ? 285  ILE B O   1 
ATOM   6850  C  CB  . ILE B  1  259 ? 23.322  -36.154 -28.796 1.00 54.67  ? 285  ILE B CB  1 
ATOM   6851  C  CG1 . ILE B  1  259 ? 22.342  -37.159 -29.383 1.00 53.65  ? 285  ILE B CG1 1 
ATOM   6852  C  CG2 . ILE B  1  259 ? 22.734  -34.765 -28.798 1.00 53.03  ? 285  ILE B CG2 1 
ATOM   6853  C  CD1 . ILE B  1  259 ? 21.295  -37.565 -28.406 1.00 55.29  ? 285  ILE B CD1 1 
ATOM   6854  N  N   . GLU B  1  260 ? 25.693  -34.002 -29.586 1.00 53.05  ? 286  GLU B N   1 
ATOM   6855  C  CA  . GLU B  1  260 ? 26.595  -32.982 -29.070 1.00 52.64  ? 286  GLU B CA  1 
ATOM   6856  C  C   . GLU B  1  260 ? 25.822  -31.934 -28.291 1.00 51.01  ? 286  GLU B C   1 
ATOM   6857  O  O   . GLU B  1  260 ? 26.247  -31.495 -27.226 1.00 49.60  ? 286  GLU B O   1 
ATOM   6858  C  CB  . GLU B  1  260 ? 27.366  -32.301 -30.206 1.00 54.71  ? 286  GLU B CB  1 
ATOM   6859  C  CG  . GLU B  1  260 ? 28.413  -31.309 -29.712 1.00 57.22  ? 286  GLU B CG  1 
ATOM   6860  C  CD  . GLU B  1  260 ? 29.463  -31.968 -28.821 1.00 60.71  ? 286  GLU B CD  1 
ATOM   6861  O  OE1 . GLU B  1  260 ? 30.199  -31.246 -28.100 1.00 60.88  ? 286  GLU B OE1 1 
ATOM   6862  O  OE2 . GLU B  1  260 ? 29.559  -33.221 -28.849 1.00 62.01  ? 286  GLU B OE2 1 
ATOM   6863  N  N   . GLU B  1  261 ? 24.683  -31.531 -28.839 1.00 50.08  ? 287  GLU B N   1 
ATOM   6864  C  CA  . GLU B  1  261 ? 23.835  -30.544 -28.193 1.00 48.34  ? 287  GLU B CA  1 
ATOM   6865  C  C   . GLU B  1  261 ? 22.415  -31.064 -28.270 1.00 46.42  ? 287  GLU B C   1 
ATOM   6866  O  O   . GLU B  1  261 ? 21.962  -31.503 -29.328 1.00 44.29  ? 287  GLU B O   1 
ATOM   6867  C  CB  . GLU B  1  261 ? 23.905  -29.200 -28.914 1.00 50.87  ? 287  GLU B CB  1 
ATOM   6868  C  CG  . GLU B  1  261 ? 25.294  -28.763 -29.327 1.00 54.88  ? 287  GLU B CG  1 
ATOM   6869  C  CD  . GLU B  1  261 ? 25.282  -27.440 -30.078 1.00 56.67  ? 287  GLU B CD  1 
ATOM   6870  O  OE1 . GLU B  1  261 ? 24.300  -27.187 -30.816 1.00 58.45  ? 287  GLU B OE1 1 
ATOM   6871  O  OE2 . GLU B  1  261 ? 26.257  -26.665 -29.937 1.00 56.87  ? 287  GLU B OE2 1 
ATOM   6872  N  N   . PHE B  1  262 ? 21.717  -30.997 -27.141 1.00 45.03  ? 288  PHE B N   1 
ATOM   6873  C  CA  . PHE B  1  262 ? 20.330  -31.454 -27.044 1.00 43.63  ? 288  PHE B CA  1 
ATOM   6874  C  C   . PHE B  1  262 ? 19.369  -30.341 -26.583 1.00 43.94  ? 288  PHE B C   1 
ATOM   6875  O  O   . PHE B  1  262 ? 19.752  -29.419 -25.844 1.00 43.80  ? 288  PHE B O   1 
ATOM   6876  C  CB  . PHE B  1  262 ? 20.250  -32.609 -26.048 1.00 41.11  ? 288  PHE B CB  1 
ATOM   6877  C  CG  . PHE B  1  262 ? 18.861  -33.112 -25.804 1.00 39.48  ? 288  PHE B CG  1 
ATOM   6878  C  CD1 . PHE B  1  262 ? 18.230  -33.915 -26.747 1.00 39.45  ? 288  PHE B CD1 1 
ATOM   6879  C  CD2 . PHE B  1  262 ? 18.172  -32.761 -24.643 1.00 37.89  ? 288  PHE B CD2 1 
ATOM   6880  C  CE1 . PHE B  1  262 ? 16.928  -34.369 -26.538 1.00 38.42  ? 288  PHE B CE1 1 
ATOM   6881  C  CE2 . PHE B  1  262 ? 16.873  -33.203 -24.421 1.00 38.09  ? 288  PHE B CE2 1 
ATOM   6882  C  CZ  . PHE B  1  262 ? 16.245  -34.007 -25.367 1.00 38.30  ? 288  PHE B CZ  1 
ATOM   6883  N  N   . ARG B  1  263 ? 18.120  -30.433 -27.033 1.00 43.78  ? 289  ARG B N   1 
ATOM   6884  C  CA  . ARG B  1  263 ? 17.082  -29.494 -26.619 1.00 43.67  ? 289  ARG B CA  1 
ATOM   6885  C  C   . ARG B  1  263 ? 15.690  -30.110 -26.660 1.00 44.62  ? 289  ARG B C   1 
ATOM   6886  O  O   . ARG B  1  263 ? 15.261  -30.649 -27.693 1.00 46.23  ? 289  ARG B O   1 
ATOM   6887  C  CB  . ARG B  1  263 ? 17.041  -28.235 -27.489 1.00 42.99  ? 289  ARG B CB  1 
ATOM   6888  C  CG  . ARG B  1  263 ? 15.801  -27.375 -27.167 1.00 39.35  ? 289  ARG B CG  1 
ATOM   6889  C  CD  . ARG B  1  263 ? 15.660  -26.149 -28.037 1.00 39.30  ? 289  ARG B CD  1 
ATOM   6890  N  NE  . ARG B  1  263 ? 16.429  -25.041 -27.495 1.00 40.64  ? 289  ARG B NE  1 
ATOM   6891  C  CZ  . ARG B  1  263 ? 16.549  -23.857 -28.077 1.00 40.35  ? 289  ARG B CZ  1 
ATOM   6892  N  NH1 . ARG B  1  263 ? 15.956  -23.608 -29.237 1.00 38.36  ? 289  ARG B NH1 1 
ATOM   6893  N  NH2 . ARG B  1  263 ? 17.259  -22.916 -27.484 1.00 42.38  ? 289  ARG B NH2 1 
ATOM   6894  N  N   . LEU B  1  264 ? 14.995  -30.038 -25.530 1.00 42.08  ? 290  LEU B N   1 
ATOM   6895  C  CA  . LEU B  1  264 ? 13.625  -30.503 -25.463 1.00 40.84  ? 290  LEU B CA  1 
ATOM   6896  C  C   . LEU B  1  264 ? 12.784  -29.204 -25.540 1.00 40.84  ? 290  LEU B C   1 
ATOM   6897  O  O   . LEU B  1  264 ? 12.816  -28.383 -24.632 1.00 40.62  ? 290  LEU B O   1 
ATOM   6898  C  CB  . LEU B  1  264 ? 13.379  -31.254 -24.152 1.00 38.19  ? 290  LEU B CB  1 
ATOM   6899  C  CG  . LEU B  1  264 ? 11.929  -31.672 -23.881 1.00 38.46  ? 290  LEU B CG  1 
ATOM   6900  C  CD1 . LEU B  1  264 ? 11.386  -32.549 -25.010 1.00 38.83  ? 290  LEU B CD1 1 
ATOM   6901  C  CD2 . LEU B  1  264 ? 11.867  -32.406 -22.572 1.00 38.05  ? 290  LEU B CD2 1 
ATOM   6902  N  N   . ALA B  1  265 ? 12.064  -29.009 -26.643 1.00 40.80  ? 291  ALA B N   1 
ATOM   6903  C  CA  . ALA B  1  265 ? 11.249  -27.815 -26.843 1.00 41.91  ? 291  ALA B CA  1 
ATOM   6904  C  C   . ALA B  1  265 ? 9.742   -27.938 -26.649 1.00 44.27  ? 291  ALA B C   1 
ATOM   6905  O  O   . ALA B  1  265 ? 9.008   -28.228 -27.603 1.00 44.95  ? 291  ALA B O   1 
ATOM   6906  C  CB  . ALA B  1  265 ? 11.455  -27.284 -28.260 1.00 41.21  ? 291  ALA B CB  1 
ATOM   6907  N  N   . TYR B  1  266 ? 9.290   -27.681 -25.422 1.00 45.49  ? 292  TYR B N   1 
ATOM   6908  C  CA  . TYR B  1  266 ? 7.874   -27.753 -25.035 1.00 48.87  ? 292  TYR B CA  1 
ATOM   6909  C  C   . TYR B  1  266 ? 7.285   -29.151 -24.804 1.00 50.24  ? 292  TYR B C   1 
ATOM   6910  O  O   . TYR B  1  266 ? 7.185   -29.958 -25.727 1.00 53.26  ? 292  TYR B O   1 
ATOM   6911  C  CB  . TYR B  1  266 ? 6.905   -27.133 -26.048 1.00 48.54  ? 292  TYR B CB  1 
ATOM   6912  C  CG  . TYR B  1  266 ? 5.490   -27.139 -25.505 1.00 51.93  ? 292  TYR B CG  1 
ATOM   6913  C  CD1 . TYR B  1  266 ? 5.105   -26.252 -24.500 1.00 52.55  ? 292  TYR B CD1 1 
ATOM   6914  C  CD2 . TYR B  1  266 ? 4.566   -28.100 -25.910 1.00 53.48  ? 292  TYR B CD2 1 
ATOM   6915  C  CE1 . TYR B  1  266 ? 3.845   -26.324 -23.906 1.00 53.61  ? 292  TYR B CE1 1 
ATOM   6916  C  CE2 . TYR B  1  266 ? 3.299   -28.181 -25.318 1.00 54.17  ? 292  TYR B CE2 1 
ATOM   6917  C  CZ  . TYR B  1  266 ? 2.949   -27.288 -24.317 1.00 54.88  ? 292  TYR B CZ  1 
ATOM   6918  O  OH  . TYR B  1  266 ? 1.703   -27.348 -23.724 1.00 56.44  ? 292  TYR B OH  1 
ATOM   6919  N  N   . LEU B  1  267 ? 6.873   -29.432 -23.575 1.00 49.89  ? 293  LEU B N   1 
ATOM   6920  C  CA  . LEU B  1  267 ? 6.312   -30.728 -23.242 1.00 52.40  ? 293  LEU B CA  1 
ATOM   6921  C  C   . LEU B  1  267 ? 5.163   -30.440 -22.311 1.00 55.09  ? 293  LEU B C   1 
ATOM   6922  O  O   . LEU B  1  267 ? 5.367   -29.791 -21.286 1.00 56.80  ? 293  LEU B O   1 
ATOM   6923  C  CB  . LEU B  1  267 ? 7.443   -31.477 -22.511 1.00 52.65  ? 293  LEU B CB  1 
ATOM   6924  C  CG  . LEU B  1  267 ? 7.591   -33.005 -22.347 1.00 51.38  ? 293  LEU B CG  1 
ATOM   6925  C  CD1 . LEU B  1  267 ? 6.965   -33.458 -21.062 1.00 48.54  ? 293  LEU B CD1 1 
ATOM   6926  C  CD2 . LEU B  1  267 ? 7.004   -33.720 -23.554 1.00 52.17  ? 293  LEU B CD2 1 
ATOM   6927  N  N   . ASP B  1  268 ? 3.966   -30.902 -22.677 1.00 57.17  ? 294  ASP B N   1 
ATOM   6928  C  CA  . ASP B  1  268 ? 2.742   -30.689 -21.892 1.00 59.15  ? 294  ASP B CA  1 
ATOM   6929  C  C   . ASP B  1  268 ? 2.786   -31.401 -20.544 1.00 59.90  ? 294  ASP B C   1 
ATOM   6930  O  O   . ASP B  1  268 ? 2.398   -30.834 -19.519 1.00 59.43  ? 294  ASP B O   1 
ATOM   6931  C  CB  . ASP B  1  268 ? 1.535   -31.186 -22.695 1.00 61.68  ? 294  ASP B CB  1 
ATOM   6932  C  CG  . ASP B  1  268 ? 0.213   -30.560 -22.249 1.00 62.81  ? 294  ASP B CG  1 
ATOM   6933  O  OD1 . ASP B  1  268 ? -0.226  -30.786 -21.099 1.00 62.84  ? 294  ASP B OD1 1 
ATOM   6934  O  OD2 . ASP B  1  268 ? -0.397  -29.840 -23.067 1.00 64.41  ? 294  ASP B OD2 1 
ATOM   6935  N  N   . TYR B  1  269 ? 3.250   -32.647 -20.563 1.00 62.07  ? 295  TYR B N   1 
ATOM   6936  C  CA  . TYR B  1  269 ? 3.367   -33.481 -19.364 1.00 64.69  ? 295  TYR B CA  1 
ATOM   6937  C  C   . TYR B  1  269 ? 4.264   -32.801 -18.314 1.00 65.08  ? 295  TYR B C   1 
ATOM   6938  O  O   . TYR B  1  269 ? 5.269   -32.185 -18.656 1.00 65.18  ? 295  TYR B O   1 
ATOM   6939  C  CB  . TYR B  1  269 ? 3.943   -34.847 -19.785 1.00 66.38  ? 295  TYR B CB  1 
ATOM   6940  C  CG  . TYR B  1  269 ? 4.052   -35.909 -18.701 1.00 69.47  ? 295  TYR B CG  1 
ATOM   6941  C  CD1 . TYR B  1  269 ? 2.936   -36.661 -18.299 1.00 70.45  ? 295  TYR B CD1 1 
ATOM   6942  C  CD2 . TYR B  1  269 ? 5.281   -36.166 -18.076 1.00 69.61  ? 295  TYR B CD2 1 
ATOM   6943  C  CE1 . TYR B  1  269 ? 3.047   -37.641 -17.296 1.00 71.16  ? 295  TYR B CE1 1 
ATOM   6944  C  CE2 . TYR B  1  269 ? 5.402   -37.135 -17.077 1.00 70.25  ? 295  TYR B CE2 1 
ATOM   6945  C  CZ  . TYR B  1  269 ? 4.286   -37.866 -16.689 1.00 71.18  ? 295  TYR B CZ  1 
ATOM   6946  O  OH  . TYR B  1  269 ? 4.420   -38.789 -15.674 1.00 70.19  ? 295  TYR B OH  1 
ATOM   6947  N  N   . TYR B  1  270 ? 3.902   -32.890 -17.040 1.00 66.76  ? 296  TYR B N   1 
ATOM   6948  C  CA  . TYR B  1  270 ? 4.717   -32.278 -15.986 1.00 69.93  ? 296  TYR B CA  1 
ATOM   6949  C  C   . TYR B  1  270 ? 5.819   -33.250 -15.594 1.00 72.27  ? 296  TYR B C   1 
ATOM   6950  O  O   . TYR B  1  270 ? 5.530   -34.310 -15.048 1.00 74.57  ? 296  TYR B O   1 
ATOM   6951  C  CB  . TYR B  1  270 ? 3.868   -31.974 -14.747 1.00 69.94  ? 296  TYR B CB  1 
ATOM   6952  C  CG  . TYR B  1  270 ? 2.971   -30.763 -14.858 1.00 71.81  ? 296  TYR B CG  1 
ATOM   6953  C  CD1 . TYR B  1  270 ? 2.323   -30.448 -16.059 1.00 73.05  ? 296  TYR B CD1 1 
ATOM   6954  C  CD2 . TYR B  1  270 ? 2.692   -29.983 -13.735 1.00 71.83  ? 296  TYR B CD2 1 
ATOM   6955  C  CE1 . TYR B  1  270 ? 1.409   -29.396 -16.135 1.00 74.67  ? 296  TYR B CE1 1 
ATOM   6956  C  CE2 . TYR B  1  270 ? 1.778   -28.926 -13.795 1.00 74.14  ? 296  TYR B CE2 1 
ATOM   6957  C  CZ  . TYR B  1  270 ? 1.132   -28.639 -14.998 1.00 75.14  ? 296  TYR B CZ  1 
ATOM   6958  O  OH  . TYR B  1  270 ? 0.168   -27.645 -15.051 1.00 73.86  ? 296  TYR B OH  1 
ATOM   6959  N  N   . LEU B  1  271 ? 7.075   -32.900 -15.860 1.00 74.13  ? 297  LEU B N   1 
ATOM   6960  C  CA  . LEU B  1  271 ? 8.190   -33.781 -15.521 1.00 75.40  ? 297  LEU B CA  1 
ATOM   6961  C  C   . LEU B  1  271 ? 8.202   -34.136 -14.050 1.00 78.51  ? 297  LEU B C   1 
ATOM   6962  O  O   . LEU B  1  271 ? 7.872   -33.312 -13.189 1.00 77.96  ? 297  LEU B O   1 
ATOM   6963  C  CB  . LEU B  1  271 ? 9.528   -33.142 -15.864 1.00 74.34  ? 297  LEU B CB  1 
ATOM   6964  C  CG  . LEU B  1  271 ? 9.855   -32.909 -17.325 1.00 73.68  ? 297  LEU B CG  1 
ATOM   6965  C  CD1 . LEU B  1  271 ? 11.271  -32.375 -17.427 1.00 73.94  ? 297  LEU B CD1 1 
ATOM   6966  C  CD2 . LEU B  1  271 ? 9.705   -34.206 -18.084 1.00 73.41  ? 297  LEU B CD2 1 
ATOM   6967  N  N   . ASP B  1  272 ? 8.619   -35.369 -13.778 1.00 82.87  ? 298  ASP B N   1 
ATOM   6968  C  CA  . ASP B  1  272 ? 8.694   -35.916 -12.421 1.00 87.12  ? 298  ASP B CA  1 
ATOM   6969  C  C   . ASP B  1  272 ? 10.137  -35.863 -11.937 1.00 88.00  ? 298  ASP B C   1 
ATOM   6970  O  O   . ASP B  1  272 ? 10.472  -35.165 -10.982 1.00 88.17  ? 298  ASP B O   1 
ATOM   6971  C  CB  . ASP B  1  272 ? 8.211   -37.379 -12.420 1.00 88.97  ? 298  ASP B CB  1 
ATOM   6972  C  CG  . ASP B  1  272 ? 6.745   -37.524 -12.845 1.00 92.03  ? 298  ASP B CG  1 
ATOM   6973  O  OD1 . ASP B  1  272 ? 6.421   -38.525 -13.528 1.00 92.14  ? 298  ASP B OD1 1 
ATOM   6974  O  OD2 . ASP B  1  272 ? 5.919   -36.647 -12.486 1.00 93.94  ? 298  ASP B OD2 1 
ATOM   6975  N  N   . ASP B  1  273 ? 10.983  -36.624 -12.612 1.00 89.36  ? 299  ASP B N   1 
ATOM   6976  C  CA  . ASP B  1  273 ? 12.395  -36.690 -12.286 1.00 90.73  ? 299  ASP B CA  1 
ATOM   6977  C  C   . ASP B  1  273 ? 13.189  -36.038 -13.404 1.00 90.71  ? 299  ASP B C   1 
ATOM   6978  O  O   . ASP B  1  273 ? 12.708  -35.918 -14.529 1.00 91.43  ? 299  ASP B O   1 
ATOM   6979  C  CB  . ASP B  1  273 ? 12.818  -38.155 -12.121 1.00 92.78  ? 299  ASP B CB  1 
ATOM   6980  C  CG  . ASP B  1  273 ? 14.314  -38.362 -12.306 1.00 93.86  ? 299  ASP B CG  1 
ATOM   6981  O  OD1 . ASP B  1  273 ? 14.767  -38.401 -13.474 1.00 93.16  ? 299  ASP B OD1 1 
ATOM   6982  O  OD2 . ASP B  1  273 ? 15.036  -38.478 -11.287 1.00 93.57  ? 299  ASP B OD2 1 
ATOM   6983  N  N   . ILE B  1  274 ? 14.405  -35.614 -13.098 1.00 89.96  ? 300  ILE B N   1 
ATOM   6984  C  CA  . ILE B  1  274 ? 15.231  -34.991 -14.108 1.00 89.46  ? 300  ILE B CA  1 
ATOM   6985  C  C   . ILE B  1  274 ? 16.530  -35.785 -14.347 1.00 89.44  ? 300  ILE B C   1 
ATOM   6986  O  O   . ILE B  1  274 ? 17.076  -35.778 -15.455 1.00 89.70  ? 300  ILE B O   1 
ATOM   6987  C  CB  . ILE B  1  274 ? 15.554  -33.545 -13.704 1.00 88.90  ? 300  ILE B CB  1 
ATOM   6988  C  CG1 . ILE B  1  274 ? 16.256  -32.829 -14.847 1.00 89.54  ? 300  ILE B CG1 1 
ATOM   6989  C  CG2 . ILE B  1  274 ? 16.443  -33.532 -12.485 1.00 90.90  ? 300  ILE B CG2 1 
ATOM   6990  C  CD1 . ILE B  1  274 ? 16.670  -31.426 -14.500 1.00 89.80  ? 300  ILE B CD1 1 
ATOM   6991  N  N   . ILE B  1  275 ? 16.998  -36.495 -13.319 1.00 88.74  ? 301  ILE B N   1 
ATOM   6992  C  CA  . ILE B  1  275 ? 18.245  -37.270 -13.399 1.00 87.79  ? 301  ILE B CA  1 
ATOM   6993  C  C   . ILE B  1  275 ? 18.160  -38.637 -14.109 1.00 86.21  ? 301  ILE B C   1 
ATOM   6994  O  O   . ILE B  1  275 ? 19.085  -39.021 -14.839 1.00 86.01  ? 301  ILE B O   1 
ATOM   6995  C  CB  . ILE B  1  275 ? 18.889  -37.416 -11.958 1.00 88.99  ? 301  ILE B CB  1 
ATOM   6996  C  CG1 . ILE B  1  275 ? 19.605  -38.767 -11.789 1.00 90.07  ? 301  ILE B CG1 1 
ATOM   6997  C  CG2 . ILE B  1  275 ? 17.821  -37.184 -10.887 1.00 88.90  ? 301  ILE B CG2 1 
ATOM   6998  C  CD1 . ILE B  1  275 ? 20.944  -38.897 -12.531 1.00 90.53  ? 301  ILE B CD1 1 
ATOM   6999  N  N   . ASP B  1  276 ? 17.065  -39.366 -13.902 1.00 83.76  ? 302  ASP B N   1 
ATOM   7000  C  CA  . ASP B  1  276 ? 16.877  -40.670 -14.546 1.00 81.29  ? 302  ASP B CA  1 
ATOM   7001  C  C   . ASP B  1  276 ? 16.416  -40.434 -15.985 1.00 77.86  ? 302  ASP B C   1 
ATOM   7002  O  O   . ASP B  1  276 ? 16.649  -41.238 -16.888 1.00 76.68  ? 302  ASP B O   1 
ATOM   7003  C  CB  . ASP B  1  276 ? 15.792  -41.483 -13.822 1.00 83.22  ? 302  ASP B CB  1 
ATOM   7004  C  CG  . ASP B  1  276 ? 16.221  -41.968 -12.444 1.00 83.96  ? 302  ASP B CG  1 
ATOM   7005  O  OD1 . ASP B  1  276 ? 15.323  -42.234 -11.609 1.00 84.86  ? 302  ASP B OD1 1 
ATOM   7006  O  OD2 . ASP B  1  276 ? 17.436  -42.097 -12.195 1.00 83.81  ? 302  ASP B OD2 1 
ATOM   7007  N  N   . LEU B  1  277 ? 15.758  -39.303 -16.173 1.00 73.70  ? 303  LEU B N   1 
ATOM   7008  C  CA  . LEU B  1  277 ? 15.207  -38.931 -17.455 1.00 70.90  ? 303  LEU B CA  1 
ATOM   7009  C  C   . LEU B  1  277 ? 16.242  -38.546 -18.491 1.00 69.07  ? 303  LEU B C   1 
ATOM   7010  O  O   . LEU B  1  277 ? 16.161  -38.967 -19.632 1.00 69.51  ? 303  LEU B O   1 
ATOM   7011  C  CB  . LEU B  1  277 ? 14.242  -37.764 -17.253 1.00 70.73  ? 303  LEU B CB  1 
ATOM   7012  C  CG  . LEU B  1  277 ? 13.057  -37.555 -18.194 1.00 69.43  ? 303  LEU B CG  1 
ATOM   7013  C  CD1 . LEU B  1  277 ? 12.443  -36.220 -17.850 1.00 69.87  ? 303  LEU B CD1 1 
ATOM   7014  C  CD2 . LEU B  1  277 ? 13.480  -37.587 -19.645 1.00 67.51  ? 303  LEU B CD2 1 
ATOM   7015  N  N   . PHE B  1  278 ? 17.219  -37.745 -18.096 1.00 67.52  ? 304  PHE B N   1 
ATOM   7016  C  CA  . PHE B  1  278 ? 18.218  -37.280 -19.038 1.00 65.58  ? 304  PHE B CA  1 
ATOM   7017  C  C   . PHE B  1  278 ? 19.619  -37.866 -18.915 1.00 67.15  ? 304  PHE B C   1 
ATOM   7018  O  O   . PHE B  1  278 ? 20.565  -37.281 -19.439 1.00 68.28  ? 304  PHE B O   1 
ATOM   7019  C  CB  . PHE B  1  278 ? 18.338  -35.762 -18.924 1.00 62.93  ? 304  PHE B CB  1 
ATOM   7020  C  CG  . PHE B  1  278 ? 17.034  -35.011 -19.083 1.00 59.62  ? 304  PHE B CG  1 
ATOM   7021  C  CD1 . PHE B  1  278 ? 16.636  -34.073 -18.120 1.00 56.83  ? 304  PHE B CD1 1 
ATOM   7022  C  CD2 . PHE B  1  278 ? 16.236  -35.194 -20.210 1.00 58.01  ? 304  PHE B CD2 1 
ATOM   7023  C  CE1 . PHE B  1  278 ? 15.473  -33.330 -18.278 1.00 54.98  ? 304  PHE B CE1 1 
ATOM   7024  C  CE2 . PHE B  1  278 ? 15.066  -34.453 -20.379 1.00 57.06  ? 304  PHE B CE2 1 
ATOM   7025  C  CZ  . PHE B  1  278 ? 14.682  -33.517 -19.408 1.00 56.07  ? 304  PHE B CZ  1 
ATOM   7026  N  N   . ASN B  1  279 ? 19.790  -39.004 -18.249 1.00 68.77  ? 305  ASN B N   1 
ATOM   7027  C  CA  . ASN B  1  279 ? 21.145  -39.531 -18.106 1.00 69.22  ? 305  ASN B CA  1 
ATOM   7028  C  C   . ASN B  1  279 ? 21.762  -40.056 -19.395 1.00 68.78  ? 305  ASN B C   1 
ATOM   7029  O  O   . ASN B  1  279 ? 22.925  -40.432 -19.411 1.00 68.99  ? 305  ASN B O   1 
ATOM   7030  C  CB  . ASN B  1  279 ? 21.218  -40.602 -17.014 1.00 71.31  ? 305  ASN B CB  1 
ATOM   7031  C  CG  . ASN B  1  279 ? 20.253  -41.727 -17.240 1.00 75.22  ? 305  ASN B CG  1 
ATOM   7032  O  OD1 . ASN B  1  279 ? 20.010  -42.144 -18.381 1.00 78.57  ? 305  ASN B OD1 1 
ATOM   7033  N  ND2 . ASN B  1  279 ? 19.698  -42.248 -16.152 1.00 77.21  ? 305  ASN B ND2 1 
ATOM   7034  N  N   . CYS B  1  280 ? 20.996  -40.087 -20.477 1.00 68.65  ? 306  CYS B N   1 
ATOM   7035  C  CA  . CYS B  1  280 ? 21.548  -40.543 -21.747 1.00 68.38  ? 306  CYS B CA  1 
ATOM   7036  C  C   . CYS B  1  280 ? 22.164  -39.366 -22.493 1.00 66.87  ? 306  CYS B C   1 
ATOM   7037  O  O   . CYS B  1  280 ? 22.897  -39.536 -23.470 1.00 65.75  ? 306  CYS B O   1 
ATOM   7038  C  CB  . CYS B  1  280 ? 20.466  -41.217 -22.592 1.00 70.33  ? 306  CYS B CB  1 
ATOM   7039  S  SG  . CYS B  1  280 ? 20.143  -42.929 -22.046 1.00 75.18  ? 306  CYS B SG  1 
ATOM   7040  N  N   . LEU B  1  281 ? 21.854  -38.165 -22.012 1.00 66.46  ? 307  LEU B N   1 
ATOM   7041  C  CA  . LEU B  1  281 ? 22.384  -36.931 -22.578 1.00 64.97  ? 307  LEU B CA  1 
ATOM   7042  C  C   . LEU B  1  281 ? 23.420  -36.391 -21.611 1.00 65.69  ? 307  LEU B C   1 
ATOM   7043  O  O   . LEU B  1  281 ? 23.732  -35.209 -21.640 1.00 68.20  ? 307  LEU B O   1 
ATOM   7044  C  CB  . LEU B  1  281 ? 21.305  -35.854 -22.738 1.00 61.32  ? 307  LEU B CB  1 
ATOM   7045  C  CG  . LEU B  1  281 ? 20.161  -35.952 -23.737 1.00 59.33  ? 307  LEU B CG  1 
ATOM   7046  C  CD1 . LEU B  1  281 ? 20.614  -36.645 -24.999 1.00 58.54  ? 307  LEU B CD1 1 
ATOM   7047  C  CD2 . LEU B  1  281 ? 19.036  -36.697 -23.113 1.00 58.91  ? 307  LEU B CD2 1 
ATOM   7048  N  N   . THR B  1  282 ? 23.943  -37.238 -20.737 1.00 64.82  ? 308  THR B N   1 
ATOM   7049  C  CA  . THR B  1  282 ? 24.933  -36.767 -19.785 1.00 63.46  ? 308  THR B CA  1 
ATOM   7050  C  C   . THR B  1  282 ? 26.247  -36.307 -20.450 1.00 64.01  ? 308  THR B C   1 
ATOM   7051  O  O   . THR B  1  282 ? 26.860  -35.336 -20.022 1.00 62.79  ? 308  THR B O   1 
ATOM   7052  C  CB  . THR B  1  282 ? 25.241  -37.853 -18.759 1.00 61.67  ? 308  THR B CB  1 
ATOM   7053  O  OG1 . THR B  1  282 ? 26.015  -37.282 -17.703 1.00 61.97  ? 308  THR B OG1 1 
ATOM   7054  C  CG2 . THR B  1  282 ? 26.009  -39.002 -19.398 1.00 59.23  ? 308  THR B CG2 1 
ATOM   7055  N  N   . ASN B  1  283 ? 26.667  -36.997 -21.507 1.00 65.35  ? 309  ASN B N   1 
ATOM   7056  C  CA  . ASN B  1  283 ? 27.912  -36.662 -22.203 1.00 64.88  ? 309  ASN B CA  1 
ATOM   7057  C  C   . ASN B  1  283 ? 27.737  -35.415 -23.075 1.00 62.92  ? 309  ASN B C   1 
ATOM   7058  O  O   . ASN B  1  283 ? 28.705  -34.796 -23.500 1.00 63.51  ? 309  ASN B O   1 
ATOM   7059  C  CB  . ASN B  1  283 ? 28.382  -37.855 -23.074 1.00 67.96  ? 309  ASN B CB  1 
ATOM   7060  C  CG  . ASN B  1  283 ? 28.776  -39.115 -22.240 1.00 70.32  ? 309  ASN B CG  1 
ATOM   7061  O  OD1 . ASN B  1  283 ? 29.463  -39.006 -21.213 1.00 70.36  ? 309  ASN B OD1 1 
ATOM   7062  N  ND2 . ASN B  1  283 ? 28.353  -40.309 -22.704 1.00 69.48  ? 309  ASN B ND2 1 
ATOM   7063  N  N   . VAL B  1  284 ? 26.490  -35.046 -23.335 1.00 60.71  ? 310  VAL B N   1 
ATOM   7064  C  CA  . VAL B  1  284 ? 26.175  -33.876 -24.151 1.00 57.06  ? 310  VAL B CA  1 
ATOM   7065  C  C   . VAL B  1  284 ? 26.906  -32.634 -23.639 1.00 56.14  ? 310  VAL B C   1 
ATOM   7066  O  O   . VAL B  1  284 ? 27.098  -32.489 -22.434 1.00 57.46  ? 310  VAL B O   1 
ATOM   7067  C  CB  . VAL B  1  284 ? 24.661  -33.650 -24.127 1.00 55.58  ? 310  VAL B CB  1 
ATOM   7068  C  CG1 . VAL B  1  284 ? 24.338  -32.187 -24.007 1.00 55.32  ? 310  VAL B CG1 1 
ATOM   7069  C  CG2 . VAL B  1  284 ? 24.050  -34.251 -25.363 1.00 54.81  ? 310  VAL B CG2 1 
ATOM   7070  N  N   . SER B  1  285 ? 27.316  -31.740 -24.535 1.00 54.22  ? 311  SER B N   1 
ATOM   7071  C  CA  . SER B  1  285 ? 28.021  -30.531 -24.098 1.00 53.29  ? 311  SER B CA  1 
ATOM   7072  C  C   . SER B  1  285 ? 27.088  -29.329 -23.877 1.00 52.62  ? 311  SER B C   1 
ATOM   7073  O  O   . SER B  1  285 ? 27.369  -28.453 -23.061 1.00 53.29  ? 311  SER B O   1 
ATOM   7074  C  CB  . SER B  1  285 ? 29.102  -30.148 -25.101 1.00 52.19  ? 311  SER B CB  1 
ATOM   7075  O  OG  . SER B  1  285 ? 28.523  -29.584 -26.256 1.00 53.44  ? 311  SER B OG  1 
ATOM   7076  N  N   . SER B  1  286 ? 25.984  -29.287 -24.608 1.00 51.56  ? 312  SER B N   1 
ATOM   7077  C  CA  . SER B  1  286 ? 25.017  -28.207 -24.477 1.00 49.90  ? 312  SER B CA  1 
ATOM   7078  C  C   . SER B  1  286 ? 23.630  -28.789 -24.231 1.00 49.78  ? 312  SER B C   1 
ATOM   7079  O  O   . SER B  1  286 ? 23.066  -29.466 -25.096 1.00 50.37  ? 312  SER B O   1 
ATOM   7080  C  CB  . SER B  1  286 ? 24.993  -27.360 -25.750 1.00 51.39  ? 312  SER B CB  1 
ATOM   7081  O  OG  . SER B  1  286 ? 23.941  -26.411 -25.715 1.00 51.99  ? 312  SER B OG  1 
ATOM   7082  N  N   . PHE B  1  287 ? 23.079  -28.525 -23.051 1.00 48.50  ? 313  PHE B N   1 
ATOM   7083  C  CA  . PHE B  1  287 ? 21.757  -29.029 -22.695 1.00 46.99  ? 313  PHE B CA  1 
ATOM   7084  C  C   . PHE B  1  287 ? 20.696  -27.923 -22.583 1.00 45.82  ? 313  PHE B C   1 
ATOM   7085  O  O   . PHE B  1  287 ? 20.882  -26.941 -21.861 1.00 45.49  ? 313  PHE B O   1 
ATOM   7086  C  CB  . PHE B  1  287 ? 21.837  -29.787 -21.374 1.00 46.58  ? 313  PHE B CB  1 
ATOM   7087  C  CG  . PHE B  1  287 ? 20.598  -30.557 -21.060 1.00 47.48  ? 313  PHE B CG  1 
ATOM   7088  C  CD1 . PHE B  1  287 ? 20.306  -31.735 -21.738 1.00 48.63  ? 313  PHE B CD1 1 
ATOM   7089  C  CD2 . PHE B  1  287 ? 19.675  -30.066 -20.160 1.00 47.84  ? 313  PHE B CD2 1 
ATOM   7090  C  CE1 . PHE B  1  287 ? 19.110  -32.416 -21.515 1.00 46.89  ? 313  PHE B CE1 1 
ATOM   7091  C  CE2 . PHE B  1  287 ? 18.472  -30.739 -19.929 1.00 47.71  ? 313  PHE B CE2 1 
ATOM   7092  C  CZ  . PHE B  1  287 ? 18.189  -31.911 -20.613 1.00 46.81  ? 313  PHE B CZ  1 
ATOM   7093  N  N   . SER B  1  288 ? 19.575  -28.091 -23.274 1.00 44.95  ? 314  SER B N   1 
ATOM   7094  C  CA  . SER B  1  288 ? 18.514  -27.076 -23.244 1.00 45.18  ? 314  SER B CA  1 
ATOM   7095  C  C   . SER B  1  288 ? 17.077  -27.567 -23.016 1.00 45.14  ? 314  SER B C   1 
ATOM   7096  O  O   . SER B  1  288 ? 16.638  -28.574 -23.583 1.00 46.96  ? 314  SER B O   1 
ATOM   7097  C  CB  . SER B  1  288 ? 18.541  -26.257 -24.549 1.00 44.90  ? 314  SER B CB  1 
ATOM   7098  O  OG  . SER B  1  288 ? 17.412  -25.409 -24.666 1.00 41.46  ? 314  SER B OG  1 
ATOM   7099  N  N   . LEU B  1  289 ? 16.342  -26.820 -22.198 1.00 43.20  ? 315  LEU B N   1 
ATOM   7100  C  CA  . LEU B  1  289 ? 14.940  -27.113 -21.909 1.00 41.92  ? 315  LEU B CA  1 
ATOM   7101  C  C   . LEU B  1  289 ? 14.139  -25.835 -22.078 1.00 41.11  ? 315  LEU B C   1 
ATOM   7102  O  O   . LEU B  1  289 ? 14.257  -24.933 -21.267 1.00 43.04  ? 315  LEU B O   1 
ATOM   7103  C  CB  . LEU B  1  289 ? 14.747  -27.577 -20.467 1.00 40.17  ? 315  LEU B CB  1 
ATOM   7104  C  CG  . LEU B  1  289 ? 15.228  -28.945 -19.999 1.00 39.51  ? 315  LEU B CG  1 
ATOM   7105  C  CD1 . LEU B  1  289 ? 14.851  -29.087 -18.542 1.00 35.27  ? 315  LEU B CD1 1 
ATOM   7106  C  CD2 . LEU B  1  289 ? 14.606  -30.061 -20.836 1.00 38.72  ? 315  LEU B CD2 1 
ATOM   7107  N  N   . VAL B  1  290 ? 13.342  -25.733 -23.126 1.00 40.02  ? 316  VAL B N   1 
ATOM   7108  C  CA  . VAL B  1  290 ? 12.531  -24.541 -23.294 1.00 40.85  ? 316  VAL B CA  1 
ATOM   7109  C  C   . VAL B  1  290 ? 11.047  -24.895 -23.173 1.00 42.04  ? 316  VAL B C   1 
ATOM   7110  O  O   . VAL B  1  290 ? 10.553  -25.833 -23.818 1.00 41.72  ? 316  VAL B O   1 
ATOM   7111  C  CB  . VAL B  1  290 ? 12.821  -23.804 -24.654 1.00 40.92  ? 316  VAL B CB  1 
ATOM   7112  C  CG1 . VAL B  1  290 ? 13.204  -24.784 -25.725 1.00 41.87  ? 316  VAL B CG1 1 
ATOM   7113  C  CG2 . VAL B  1  290 ? 11.596  -23.004 -25.097 1.00 39.07  ? 316  VAL B CG2 1 
ATOM   7114  N  N   . SER B  1  291 ? 10.350  -24.146 -22.319 1.00 42.07  ? 317  SER B N   1 
ATOM   7115  C  CA  . SER B  1  291 ? 8.928   -24.339 -22.063 1.00 41.95  ? 317  SER B CA  1 
ATOM   7116  C  C   . SER B  1  291 ? 8.574   -25.713 -21.546 1.00 42.53  ? 317  SER B C   1 
ATOM   7117  O  O   . SER B  1  291 ? 7.789   -26.410 -22.170 1.00 44.00  ? 317  SER B O   1 
ATOM   7118  C  CB  . SER B  1  291 ? 8.107   -24.084 -23.324 1.00 41.67  ? 317  SER B CB  1 
ATOM   7119  O  OG  . SER B  1  291 ? 7.829   -22.715 -23.492 1.00 42.35  ? 317  SER B OG  1 
ATOM   7120  N  N   . VAL B  1  292 ? 9.153   -26.121 -20.426 1.00 42.54  ? 318  VAL B N   1 
ATOM   7121  C  CA  . VAL B  1  292 ? 8.815   -27.417 -19.856 1.00 44.73  ? 318  VAL B CA  1 
ATOM   7122  C  C   . VAL B  1  292 ? 8.668   -27.200 -18.348 1.00 47.14  ? 318  VAL B C   1 
ATOM   7123  O  O   . VAL B  1  292 ? 9.457   -26.472 -17.742 1.00 45.55  ? 318  VAL B O   1 
ATOM   7124  C  CB  . VAL B  1  292 ? 9.884   -28.551 -20.213 1.00 43.83  ? 318  VAL B CB  1 
ATOM   7125  C  CG1 . VAL B  1  292 ? 10.965  -28.005 -21.120 1.00 42.41  ? 318  VAL B CG1 1 
ATOM   7126  C  CG2 . VAL B  1  292 ? 10.491  -29.156 -18.958 1.00 44.18  ? 318  VAL B CG2 1 
ATOM   7127  N  N   . THR B  1  293 ? 7.634   -27.804 -17.756 1.00 50.64  ? 319  THR B N   1 
ATOM   7128  C  CA  . THR B  1  293 ? 7.369   -27.654 -16.323 1.00 53.01  ? 319  THR B CA  1 
ATOM   7129  C  C   . THR B  1  293 ? 8.199   -28.638 -15.513 1.00 55.39  ? 319  THR B C   1 
ATOM   7130  O  O   . THR B  1  293 ? 8.138   -29.837 -15.743 1.00 55.82  ? 319  THR B O   1 
ATOM   7131  C  CB  . THR B  1  293 ? 5.865   -27.864 -15.997 1.00 51.75  ? 319  THR B CB  1 
ATOM   7132  O  OG1 . THR B  1  293 ? 5.075   -26.926 -16.734 1.00 50.03  ? 319  THR B OG1 1 
ATOM   7133  C  CG2 . THR B  1  293 ? 5.604   -27.643 -14.534 1.00 52.96  ? 319  THR B CG2 1 
ATOM   7134  N  N   . ILE B  1  294 ? 8.972   -28.119 -14.566 1.00 59.54  ? 320  ILE B N   1 
ATOM   7135  C  CA  . ILE B  1  294 ? 9.849   -28.941 -13.727 1.00 64.22  ? 320  ILE B CA  1 
ATOM   7136  C  C   . ILE B  1  294 ? 9.550   -28.810 -12.233 1.00 67.52  ? 320  ILE B C   1 
ATOM   7137  O  O   . ILE B  1  294 ? 10.400  -29.134 -11.413 1.00 69.60  ? 320  ILE B O   1 
ATOM   7138  C  CB  . ILE B  1  294 ? 11.364  -28.566 -13.947 1.00 63.93  ? 320  ILE B CB  1 
ATOM   7139  C  CG1 . ILE B  1  294 ? 11.566  -27.036 -13.728 1.00 63.26  ? 320  ILE B CG1 1 
ATOM   7140  C  CG2 . ILE B  1  294 ? 11.816  -29.031 -15.335 1.00 62.33  ? 320  ILE B CG2 1 
ATOM   7141  C  CD1 . ILE B  1  294 ? 12.985  -26.473 -13.909 1.00 57.71  ? 320  ILE B CD1 1 
ATOM   7142  N  N   . GLU B  1  295 ? 8.364   -28.330 -11.875 1.00 70.60  ? 321  GLU B N   1 
ATOM   7143  C  CA  . GLU B  1  295 ? 7.999   -28.175 -10.465 1.00 74.07  ? 321  GLU B CA  1 
ATOM   7144  C  C   . GLU B  1  295 ? 8.182   -29.488 -9.714  1.00 74.61  ? 321  GLU B C   1 
ATOM   7145  O  O   . GLU B  1  295 ? 8.812   -29.533 -8.663  1.00 71.95  ? 321  GLU B O   1 
ATOM   7146  C  CB  . GLU B  1  295 ? 6.535   -27.748 -10.340 1.00 77.59  ? 321  GLU B CB  1 
ATOM   7147  C  CG  . GLU B  1  295 ? 6.180   -26.463 -11.082 1.00 84.00  ? 321  GLU B CG  1 
ATOM   7148  C  CD  . GLU B  1  295 ? 4.689   -26.123 -11.007 1.00 87.56  ? 321  GLU B CD  1 
ATOM   7149  O  OE1 . GLU B  1  295 ? 3.860   -26.868 -11.586 1.00 88.43  ? 321  GLU B OE1 1 
ATOM   7150  O  OE2 . GLU B  1  295 ? 4.348   -25.105 -10.358 1.00 90.46  ? 321  GLU B OE2 1 
ATOM   7151  N  N   . ARG B  1  296 ? 7.613   -30.547 -10.281 1.00 77.80  ? 322  ARG B N   1 
ATOM   7152  C  CA  . ARG B  1  296 ? 7.649   -31.896 -9.718  1.00 80.78  ? 322  ARG B CA  1 
ATOM   7153  C  C   . ARG B  1  296 ? 9.026   -32.549 -9.587  1.00 80.90  ? 322  ARG B C   1 
ATOM   7154  O  O   . ARG B  1  296 ? 9.112   -33.757 -9.366  1.00 80.75  ? 322  ARG B O   1 
ATOM   7155  C  CB  . ARG B  1  296 ? 6.752   -32.831 -10.547 1.00 83.74  ? 322  ARG B CB  1 
ATOM   7156  C  CG  . ARG B  1  296 ? 5.249   -32.737 -10.257 1.00 88.33  ? 322  ARG B CG  1 
ATOM   7157  C  CD  . ARG B  1  296 ? 4.659   -31.361 -10.565 1.00 91.61  ? 322  ARG B CD  1 
ATOM   7158  N  NE  . ARG B  1  296 ? 3.198   -31.372 -10.482 1.00 95.04  ? 322  ARG B NE  1 
ATOM   7159  C  CZ  . ARG B  1  296 ? 2.420   -32.203 -11.173 1.00 97.08  ? 322  ARG B CZ  1 
ATOM   7160  N  NH1 . ARG B  1  296 ? 2.963   -33.092 -12.000 1.00 97.97  ? 322  ARG B NH1 1 
ATOM   7161  N  NH2 . ARG B  1  296 ? 1.097   -32.149 -11.043 1.00 98.23  ? 322  ARG B NH2 1 
ATOM   7162  N  N   . VAL B  1  297 ? 10.102  -31.779 -9.726  1.00 81.25  ? 323  VAL B N   1 
ATOM   7163  C  CA  . VAL B  1  297 ? 11.436  -32.356 -9.605  1.00 81.26  ? 323  VAL B CA  1 
ATOM   7164  C  C   . VAL B  1  297 ? 12.016  -31.962 -8.269  1.00 81.75  ? 323  VAL B C   1 
ATOM   7165  O  O   . VAL B  1  297 ? 12.119  -30.778 -7.955  1.00 80.01  ? 323  VAL B O   1 
ATOM   7166  C  CB  . VAL B  1  297 ? 12.389  -31.889 -10.735 1.00 81.38  ? 323  VAL B CB  1 
ATOM   7167  C  CG1 . VAL B  1  297 ? 13.748  -32.565 -10.575 1.00 80.95  ? 323  VAL B CG1 1 
ATOM   7168  C  CG2 . VAL B  1  297 ? 11.803  -32.229 -12.106 1.00 80.21  ? 323  VAL B CG2 1 
ATOM   7169  N  N   . LYS B  1  298 ? 12.395  -32.978 -7.495  1.00 84.04  ? 324  LYS B N   1 
ATOM   7170  C  CA  . LYS B  1  298 ? 12.946  -32.810 -6.152  1.00 86.16  ? 324  LYS B CA  1 
ATOM   7171  C  C   . LYS B  1  298 ? 14.484  -32.684 -6.090  1.00 87.18  ? 324  LYS B C   1 
ATOM   7172  O  O   . LYS B  1  298 ? 15.025  -32.026 -5.190  1.00 87.09  ? 324  LYS B O   1 
ATOM   7173  C  CB  . LYS B  1  298 ? 12.475  -33.983 -5.277  1.00 86.07  ? 324  LYS B CB  1 
ATOM   7174  C  CG  . LYS B  1  298 ? 12.134  -33.629 -3.826  1.00 88.00  ? 324  LYS B CG  1 
ATOM   7175  C  CD  . LYS B  1  298 ? 13.375  -33.400 -2.958  1.00 89.07  ? 324  LYS B CD  1 
ATOM   7176  C  CE  . LYS B  1  298 ? 12.993  -33.173 -1.493  1.00 89.35  ? 324  LYS B CE  1 
ATOM   7177  N  NZ  . LYS B  1  298 ? 14.193  -33.027 -0.613  1.00 89.84  ? 324  LYS B NZ  1 
ATOM   7178  N  N   . ASP B  1  299 ? 15.188  -33.297 -7.040  1.00 87.81  ? 325  ASP B N   1 
ATOM   7179  C  CA  . ASP B  1  299 ? 16.648  -33.244 -7.040  1.00 88.03  ? 325  ASP B CA  1 
ATOM   7180  C  C   . ASP B  1  299 ? 17.272  -32.690 -8.312  1.00 88.73  ? 325  ASP B C   1 
ATOM   7181  O  O   . ASP B  1  299 ? 17.156  -33.286 -9.388  1.00 88.67  ? 325  ASP B O   1 
ATOM   7182  C  CB  . ASP B  1  299 ? 17.237  -34.639 -6.772  1.00 86.96  ? 325  ASP B CB  1 
ATOM   7183  C  CG  . ASP B  1  299 ? 18.696  -34.588 -6.325  1.00 86.33  ? 325  ASP B CG  1 
ATOM   7184  O  OD1 . ASP B  1  299 ? 19.548  -34.077 -7.070  1.00 85.04  ? 325  ASP B OD1 1 
ATOM   7185  O  OD2 . ASP B  1  299 ? 18.996  -35.060 -5.213  1.00 87.87  ? 325  ASP B OD2 1 
ATOM   7186  N  N   . PHE B  1  300 ? 17.949  -31.552 -8.165  1.00 89.77  ? 326  PHE B N   1 
ATOM   7187  C  CA  . PHE B  1  300 ? 18.652  -30.891 -9.270  1.00 90.07  ? 326  PHE B CA  1 
ATOM   7188  C  C   . PHE B  1  300 ? 20.163  -30.944 -8.982  1.00 90.07  ? 326  PHE B C   1 
ATOM   7189  O  O   . PHE B  1  300 ? 20.940  -30.087 -9.427  1.00 89.65  ? 326  PHE B O   1 
ATOM   7190  C  CB  . PHE B  1  300 ? 18.210  -29.422 -9.386  1.00 89.18  ? 326  PHE B CB  1 
ATOM   7191  C  CG  . PHE B  1  300 ? 16.750  -29.242 -9.703  1.00 86.59  ? 326  PHE B CG  1 
ATOM   7192  C  CD1 . PHE B  1  300 ? 15.792  -29.265 -8.688  1.00 85.29  ? 326  PHE B CD1 1 
ATOM   7193  C  CD2 . PHE B  1  300 ? 16.338  -29.057 -11.021 1.00 83.95  ? 326  PHE B CD2 1 
ATOM   7194  C  CE1 . PHE B  1  300 ? 14.450  -29.106 -8.985  1.00 83.57  ? 326  PHE B CE1 1 
ATOM   7195  C  CE2 . PHE B  1  300 ? 15.003  -28.897 -11.329 1.00 82.87  ? 326  PHE B CE2 1 
ATOM   7196  C  CZ  . PHE B  1  300 ? 14.050  -28.920 -10.311 1.00 83.45  ? 326  PHE B CZ  1 
ATOM   7197  N  N   . SER B  1  301 ? 20.563  -31.976 -8.243  1.00 89.89  ? 327  SER B N   1 
ATOM   7198  C  CA  . SER B  1  301 ? 21.946  -32.152 -7.830  1.00 89.40  ? 327  SER B CA  1 
ATOM   7199  C  C   . SER B  1  301 ? 22.883  -33.018 -8.671  1.00 87.91  ? 327  SER B C   1 
ATOM   7200  O  O   . SER B  1  301 ? 24.090  -32.990 -8.448  1.00 88.06  ? 327  SER B O   1 
ATOM   7201  C  CB  . SER B  1  301 ? 21.968  -32.662 -6.389  1.00 90.47  ? 327  SER B CB  1 
ATOM   7202  O  OG  . SER B  1  301 ? 23.298  -32.847 -5.939  1.00 94.33  ? 327  SER B OG  1 
ATOM   7203  N  N   . TYR B  1  302 ? 22.364  -33.782 -9.628  1.00 86.03  ? 328  TYR B N   1 
ATOM   7204  C  CA  . TYR B  1  302 ? 23.249  -34.630 -10.418 1.00 84.77  ? 328  TYR B CA  1 
ATOM   7205  C  C   . TYR B  1  302 ? 24.323  -33.863 -11.181 1.00 83.83  ? 328  TYR B C   1 
ATOM   7206  O  O   . TYR B  1  302 ? 24.088  -32.765 -11.678 1.00 83.23  ? 328  TYR B O   1 
ATOM   7207  C  CB  . TYR B  1  302 ? 22.471  -35.489 -11.401 1.00 84.94  ? 328  TYR B CB  1 
ATOM   7208  C  CG  . TYR B  1  302 ? 23.348  -36.572 -11.984 1.00 86.44  ? 328  TYR B CG  1 
ATOM   7209  C  CD1 . TYR B  1  302 ? 23.854  -37.594 -11.181 1.00 86.50  ? 328  TYR B CD1 1 
ATOM   7210  C  CD2 . TYR B  1  302 ? 23.714  -36.550 -13.322 1.00 87.63  ? 328  TYR B CD2 1 
ATOM   7211  C  CE1 . TYR B  1  302 ? 24.705  -38.565 -11.697 1.00 87.12  ? 328  TYR B CE1 1 
ATOM   7212  C  CE2 . TYR B  1  302 ? 24.570  -37.516 -13.853 1.00 88.23  ? 328  TYR B CE2 1 
ATOM   7213  C  CZ  . TYR B  1  302 ? 25.064  -38.520 -13.033 1.00 87.85  ? 328  TYR B CZ  1 
ATOM   7214  O  OH  . TYR B  1  302 ? 25.931  -39.462 -13.547 1.00 88.22  ? 328  TYR B OH  1 
ATOM   7215  N  N   . ASN B  1  303 ? 25.506  -34.467 -11.269 1.00 83.04  ? 329  ASN B N   1 
ATOM   7216  C  CA  . ASN B  1  303 ? 26.658  -33.866 -11.937 1.00 81.32  ? 329  ASN B CA  1 
ATOM   7217  C  C   . ASN B  1  303 ? 26.837  -34.358 -13.387 1.00 79.13  ? 329  ASN B C   1 
ATOM   7218  O  O   . ASN B  1  303 ? 27.575  -35.320 -13.676 1.00 78.66  ? 329  ASN B O   1 
ATOM   7219  C  CB  . ASN B  1  303 ? 27.924  -34.129 -11.093 1.00 83.49  ? 329  ASN B CB  1 
ATOM   7220  C  CG  . ASN B  1  303 ? 29.175  -33.468 -11.666 1.00 85.32  ? 329  ASN B CG  1 
ATOM   7221  O  OD1 . ASN B  1  303 ? 29.176  -32.275 -11.991 1.00 85.68  ? 329  ASN B OD1 1 
ATOM   7222  N  ND2 . ASN B  1  303 ? 30.255  -34.245 -11.779 1.00 85.21  ? 329  ASN B ND2 1 
ATOM   7223  N  N   . PHE B  1  304 ? 26.132  -33.685 -14.290 1.00 75.63  ? 330  PHE B N   1 
ATOM   7224  C  CA  . PHE B  1  304 ? 26.186  -33.983 -15.712 1.00 72.44  ? 330  PHE B CA  1 
ATOM   7225  C  C   . PHE B  1  304 ? 27.458  -33.330 -16.273 1.00 70.06  ? 330  PHE B C   1 
ATOM   7226  O  O   . PHE B  1  304 ? 27.992  -32.385 -15.683 1.00 70.82  ? 330  PHE B O   1 
ATOM   7227  C  CB  . PHE B  1  304 ? 24.950  -33.394 -16.399 1.00 73.40  ? 330  PHE B CB  1 
ATOM   7228  C  CG  . PHE B  1  304 ? 23.628  -34.001 -15.951 1.00 74.26  ? 330  PHE B CG  1 
ATOM   7229  C  CD1 . PHE B  1  304 ? 23.232  -35.267 -16.401 1.00 73.55  ? 330  PHE B CD1 1 
ATOM   7230  C  CD2 . PHE B  1  304 ? 22.762  -33.287 -15.114 1.00 74.19  ? 330  PHE B CD2 1 
ATOM   7231  C  CE1 . PHE B  1  304 ? 21.994  -35.808 -16.041 1.00 71.66  ? 330  PHE B CE1 1 
ATOM   7232  C  CE2 . PHE B  1  304 ? 21.514  -33.822 -14.744 1.00 73.34  ? 330  PHE B CE2 1 
ATOM   7233  C  CZ  . PHE B  1  304 ? 21.134  -35.086 -15.212 1.00 72.24  ? 330  PHE B CZ  1 
ATOM   7234  N  N   . GLY B  1  305 ? 27.944  -33.817 -17.407 1.00 66.73  ? 331  GLY B N   1 
ATOM   7235  C  CA  . GLY B  1  305 ? 29.146  -33.234 -17.975 1.00 61.93  ? 331  GLY B CA  1 
ATOM   7236  C  C   . GLY B  1  305 ? 28.851  -32.036 -18.851 1.00 59.49  ? 331  GLY B C   1 
ATOM   7237  O  O   . GLY B  1  305 ? 29.715  -31.586 -19.592 1.00 60.51  ? 331  GLY B O   1 
ATOM   7238  N  N   . TRP B  1  306 ? 27.626  -31.521 -18.770 1.00 57.11  ? 332  TRP B N   1 
ATOM   7239  C  CA  . TRP B  1  306 ? 27.197  -30.367 -19.561 1.00 54.28  ? 332  TRP B CA  1 
ATOM   7240  C  C   . TRP B  1  306 ? 28.060  -29.138 -19.321 1.00 53.70  ? 332  TRP B C   1 
ATOM   7241  O  O   . TRP B  1  306 ? 28.457  -28.878 -18.186 1.00 53.38  ? 332  TRP B O   1 
ATOM   7242  C  CB  . TRP B  1  306 ? 25.767  -29.973 -19.207 1.00 52.22  ? 332  TRP B CB  1 
ATOM   7243  C  CG  . TRP B  1  306 ? 24.760  -31.061 -19.192 1.00 50.57  ? 332  TRP B CG  1 
ATOM   7244  C  CD1 . TRP B  1  306 ? 24.800  -32.236 -19.877 1.00 50.78  ? 332  TRP B CD1 1 
ATOM   7245  C  CD2 . TRP B  1  306 ? 23.487  -31.020 -18.540 1.00 50.80  ? 332  TRP B CD2 1 
ATOM   7246  N  NE1 . TRP B  1  306 ? 23.621  -32.926 -19.698 1.00 49.59  ? 332  TRP B NE1 1 
ATOM   7247  C  CE2 . TRP B  1  306 ? 22.801  -32.198 -18.881 1.00 50.23  ? 332  TRP B CE2 1 
ATOM   7248  C  CE3 . TRP B  1  306 ? 22.858  -30.095 -17.702 1.00 51.78  ? 332  TRP B CE3 1 
ATOM   7249  C  CZ2 . TRP B  1  306 ? 21.519  -32.475 -18.414 1.00 50.44  ? 332  TRP B CZ2 1 
ATOM   7250  C  CZ3 . TRP B  1  306 ? 21.587  -30.371 -17.237 1.00 50.73  ? 332  TRP B CZ3 1 
ATOM   7251  C  CH2 . TRP B  1  306 ? 20.932  -31.551 -17.594 1.00 51.65  ? 332  TRP B CH2 1 
ATOM   7252  N  N   . GLN B  1  307 ? 28.318  -28.368 -20.376 1.00 53.56  ? 333  GLN B N   1 
ATOM   7253  C  CA  . GLN B  1  307 ? 29.114  -27.148 -20.256 1.00 54.87  ? 333  GLN B CA  1 
ATOM   7254  C  C   . GLN B  1  307 ? 28.268  -25.914 -20.462 1.00 53.38  ? 333  GLN B C   1 
ATOM   7255  O  O   . GLN B  1  307 ? 28.632  -24.826 -20.028 1.00 52.82  ? 333  GLN B O   1 
ATOM   7256  C  CB  . GLN B  1  307 ? 30.244  -27.137 -21.259 1.00 57.19  ? 333  GLN B CB  1 
ATOM   7257  C  CG  . GLN B  1  307 ? 31.185  -28.267 -21.076 1.00 62.43  ? 333  GLN B CG  1 
ATOM   7258  C  CD  . GLN B  1  307 ? 32.197  -28.290 -22.167 1.00 66.52  ? 333  GLN B CD  1 
ATOM   7259  O  OE1 . GLN B  1  307 ? 32.455  -29.341 -22.772 1.00 69.09  ? 333  GLN B OE1 1 
ATOM   7260  N  NE2 . GLN B  1  307 ? 32.790  -27.123 -22.443 1.00 66.38  ? 333  GLN B NE2 1 
ATOM   7261  N  N   . HIS B  1  308 ? 27.148  -26.087 -21.150 1.00 52.60  ? 334  HIS B N   1 
ATOM   7262  C  CA  . HIS B  1  308 ? 26.200  -25.004 -21.386 1.00 52.12  ? 334  HIS B CA  1 
ATOM   7263  C  C   . HIS B  1  308 ? 24.797  -25.523 -21.038 1.00 50.60  ? 334  HIS B C   1 
ATOM   7264  O  O   . HIS B  1  308 ? 24.347  -26.523 -21.589 1.00 50.74  ? 334  HIS B O   1 
ATOM   7265  C  CB  . HIS B  1  308 ? 26.231  -24.562 -22.849 1.00 52.86  ? 334  HIS B CB  1 
ATOM   7266  C  CG  . HIS B  1  308 ? 25.154  -23.586 -23.200 1.00 56.39  ? 334  HIS B CG  1 
ATOM   7267  N  ND1 . HIS B  1  308 ? 24.446  -23.648 -24.383 1.00 57.41  ? 334  HIS B ND1 1 
ATOM   7268  C  CD2 . HIS B  1  308 ? 24.649  -22.531 -22.516 1.00 58.17  ? 334  HIS B CD2 1 
ATOM   7269  C  CE1 . HIS B  1  308 ? 23.548  -22.678 -24.408 1.00 58.87  ? 334  HIS B CE1 1 
ATOM   7270  N  NE2 . HIS B  1  308 ? 23.650  -21.985 -23.287 1.00 59.49  ? 334  HIS B NE2 1 
ATOM   7271  N  N   . LEU B  1  309 ? 24.120  -24.861 -20.105 1.00 49.86  ? 335  LEU B N   1 
ATOM   7272  C  CA  . LEU B  1  309 ? 22.761  -25.252 -19.707 1.00 48.01  ? 335  LEU B CA  1 
ATOM   7273  C  C   . LEU B  1  309 ? 21.837  -24.078 -19.929 1.00 47.79  ? 335  LEU B C   1 
ATOM   7274  O  O   . LEU B  1  309 ? 22.099  -22.984 -19.429 1.00 47.40  ? 335  LEU B O   1 
ATOM   7275  C  CB  . LEU B  1  309 ? 22.702  -25.640 -18.231 1.00 45.84  ? 335  LEU B CB  1 
ATOM   7276  C  CG  . LEU B  1  309 ? 21.300  -25.914 -17.669 1.00 44.97  ? 335  LEU B CG  1 
ATOM   7277  C  CD1 . LEU B  1  309 ? 20.629  -27.010 -18.456 1.00 42.54  ? 335  LEU B CD1 1 
ATOM   7278  C  CD2 . LEU B  1  309 ? 21.408  -26.310 -16.200 1.00 42.36  ? 335  LEU B CD2 1 
ATOM   7279  N  N   . GLU B  1  310 ? 20.755  -24.304 -20.665 1.00 47.52  ? 336  GLU B N   1 
ATOM   7280  C  CA  . GLU B  1  310 ? 19.815  -23.231 -20.952 1.00 48.85  ? 336  GLU B CA  1 
ATOM   7281  C  C   . GLU B  1  310 ? 18.380  -23.588 -20.595 1.00 48.46  ? 336  GLU B C   1 
ATOM   7282  O  O   . GLU B  1  310 ? 17.801  -24.514 -21.158 1.00 50.01  ? 336  GLU B O   1 
ATOM   7283  C  CB  . GLU B  1  310 ? 19.904  -22.834 -22.432 1.00 49.90  ? 336  GLU B CB  1 
ATOM   7284  C  CG  . GLU B  1  310 ? 18.810  -21.880 -22.897 1.00 53.75  ? 336  GLU B CG  1 
ATOM   7285  C  CD  . GLU B  1  310 ? 18.806  -21.671 -24.418 1.00 57.14  ? 336  GLU B CD  1 
ATOM   7286  O  OE1 . GLU B  1  310 ? 19.002  -22.662 -25.161 1.00 58.27  ? 336  GLU B OE1 1 
ATOM   7287  O  OE2 . GLU B  1  310 ? 18.592  -20.522 -24.878 1.00 59.06  ? 336  GLU B OE2 1 
ATOM   7288  N  N   . LEU B  1  311 ? 17.811  -22.845 -19.656 1.00 46.86  ? 337  LEU B N   1 
ATOM   7289  C  CA  . LEU B  1  311 ? 16.442  -23.063 -19.228 1.00 46.37  ? 337  LEU B CA  1 
ATOM   7290  C  C   . LEU B  1  311 ? 15.665  -21.786 -19.496 1.00 46.97  ? 337  LEU B C   1 
ATOM   7291  O  O   . LEU B  1  311 ? 15.891  -20.783 -18.822 1.00 48.03  ? 337  LEU B O   1 
ATOM   7292  C  CB  . LEU B  1  311 ? 16.406  -23.374 -17.733 1.00 45.91  ? 337  LEU B CB  1 
ATOM   7293  C  CG  . LEU B  1  311 ? 17.095  -24.678 -17.340 1.00 46.62  ? 337  LEU B CG  1 
ATOM   7294  C  CD1 . LEU B  1  311 ? 17.180  -24.818 -15.818 1.00 44.57  ? 337  LEU B CD1 1 
ATOM   7295  C  CD2 . LEU B  1  311 ? 16.307  -25.827 -17.971 1.00 45.07  ? 337  LEU B CD2 1 
ATOM   7296  N  N   . VAL B  1  312 ? 14.768  -21.794 -20.481 1.00 47.05  ? 338  VAL B N   1 
ATOM   7297  C  CA  . VAL B  1  312 ? 13.981  -20.593 -20.753 1.00 47.20  ? 338  VAL B CA  1 
ATOM   7298  C  C   . VAL B  1  312 ? 12.511  -20.899 -20.871 1.00 48.14  ? 338  VAL B C   1 
ATOM   7299  O  O   . VAL B  1  312 ? 12.113  -21.881 -21.492 1.00 48.85  ? 338  VAL B O   1 
ATOM   7300  C  CB  . VAL B  1  312 ? 14.436  -19.860 -22.036 1.00 45.70  ? 338  VAL B CB  1 
ATOM   7301  C  CG1 . VAL B  1  312 ? 15.929  -19.695 -22.019 1.00 46.91  ? 338  VAL B CG1 1 
ATOM   7302  C  CG2 . VAL B  1  312 ? 14.007  -20.609 -23.267 1.00 44.44  ? 338  VAL B CG2 1 
ATOM   7303  N  N   . ASN B  1  313 ? 11.711  -20.044 -20.253 1.00 49.20  ? 339  ASN B N   1 
ATOM   7304  C  CA  . ASN B  1  313 ? 10.258  -20.162 -20.256 1.00 51.50  ? 339  ASN B CA  1 
ATOM   7305  C  C   . ASN B  1  313 ? 9.711   -21.442 -19.606 1.00 51.65  ? 339  ASN B C   1 
ATOM   7306  O  O   . ASN B  1  313 ? 8.748   -22.037 -20.093 1.00 51.92  ? 339  ASN B O   1 
ATOM   7307  C  CB  . ASN B  1  313 ? 9.721   -20.029 -21.684 1.00 52.54  ? 339  ASN B CB  1 
ATOM   7308  C  CG  . ASN B  1  313 ? 8.255   -19.637 -21.716 1.00 56.29  ? 339  ASN B CG  1 
ATOM   7309  O  OD1 . ASN B  1  313 ? 7.604   -19.698 -22.757 1.00 59.94  ? 339  ASN B OD1 1 
ATOM   7310  N  ND2 . ASN B  1  313 ? 7.725   -19.221 -20.568 1.00 58.94  ? 339  ASN B ND2 1 
ATOM   7311  N  N   . CYS B  1  314 ? 10.311  -21.851 -18.495 1.00 51.55  ? 340  CYS B N   1 
ATOM   7312  C  CA  . CYS B  1  314 ? 9.886   -23.054 -17.801 1.00 51.89  ? 340  CYS B CA  1 
ATOM   7313  C  C   . CYS B  1  314 ? 9.171   -22.685 -16.522 1.00 54.25  ? 340  CYS B C   1 
ATOM   7314  O  O   . CYS B  1  314 ? 9.420   -21.615 -15.978 1.00 55.75  ? 340  CYS B O   1 
ATOM   7315  C  CB  . CYS B  1  314 ? 11.103  -23.903 -17.460 1.00 48.97  ? 340  CYS B CB  1 
ATOM   7316  S  SG  . CYS B  1  314 ? 12.033  -24.384 -18.884 1.00 48.70  ? 340  CYS B SG  1 
ATOM   7317  N  N   . LYS B  1  315 ? 8.272   -23.549 -16.051 1.00 56.39  ? 341  LYS B N   1 
ATOM   7318  C  CA  . LYS B  1  315 ? 7.572   -23.295 -14.792 1.00 58.04  ? 341  LYS B CA  1 
ATOM   7319  C  C   . LYS B  1  315 ? 8.375   -24.083 -13.774 1.00 59.73  ? 341  LYS B C   1 
ATOM   7320  O  O   . LYS B  1  315 ? 8.600   -25.269 -13.970 1.00 59.69  ? 341  LYS B O   1 
ATOM   7321  C  CB  . LYS B  1  315 ? 6.134   -23.807 -14.839 1.00 57.69  ? 341  LYS B CB  1 
ATOM   7322  C  CG  . LYS B  1  315 ? 5.136   -22.831 -14.235 1.00 58.20  ? 341  LYS B CG  1 
ATOM   7323  C  CD  . LYS B  1  315 ? 4.367   -23.398 -13.051 1.00 57.10  ? 341  LYS B CD  1 
ATOM   7324  C  CE  . LYS B  1  315 ? 3.457   -22.326 -12.470 1.00 57.37  ? 341  LYS B CE  1 
ATOM   7325  N  NZ  . LYS B  1  315 ? 2.574   -22.812 -11.368 1.00 59.08  ? 341  LYS B NZ  1 
ATOM   7326  N  N   . PHE B  1  316 ? 8.812   -23.447 -12.692 1.00 62.20  ? 342  PHE B N   1 
ATOM   7327  C  CA  . PHE B  1  316 ? 9.642   -24.173 -11.748 1.00 65.93  ? 342  PHE B CA  1 
ATOM   7328  C  C   . PHE B  1  316 ? 9.240   -24.205 -10.270 1.00 66.40  ? 342  PHE B C   1 
ATOM   7329  O  O   . PHE B  1  316 ? 9.346   -25.249 -9.613  1.00 66.35  ? 342  PHE B O   1 
ATOM   7330  C  CB  . PHE B  1  316 ? 11.100  -23.687 -11.899 1.00 68.22  ? 342  PHE B CB  1 
ATOM   7331  C  CG  . PHE B  1  316 ? 11.294  -22.198 -11.659 1.00 72.13  ? 342  PHE B CG  1 
ATOM   7332  C  CD1 . PHE B  1  316 ? 11.812  -21.737 -10.442 1.00 73.22  ? 342  PHE B CD1 1 
ATOM   7333  C  CD2 . PHE B  1  316 ? 10.973  -21.260 -12.647 1.00 72.76  ? 342  PHE B CD2 1 
ATOM   7334  C  CE1 . PHE B  1  316 ? 12.012  -20.363 -10.212 1.00 74.15  ? 342  PHE B CE1 1 
ATOM   7335  C  CE2 . PHE B  1  316 ? 11.168  -19.885 -12.430 1.00 73.97  ? 342  PHE B CE2 1 
ATOM   7336  C  CZ  . PHE B  1  316 ? 11.690  -19.433 -11.211 1.00 74.62  ? 342  PHE B CZ  1 
ATOM   7337  N  N   . GLY B  1  317 ? 8.775   -23.083 -9.737  1.00 66.99  ? 343  GLY B N   1 
ATOM   7338  C  CA  . GLY B  1  317 ? 8.419   -23.060 -8.323  1.00 68.72  ? 343  GLY B CA  1 
ATOM   7339  C  C   . GLY B  1  317 ? 9.628   -22.798 -7.428  1.00 68.32  ? 343  GLY B C   1 
ATOM   7340  O  O   . GLY B  1  317 ? 9.996   -21.641 -7.198  1.00 68.53  ? 343  GLY B O   1 
ATOM   7341  N  N   . GLN B  1  318 ? 10.245  -23.859 -6.911  1.00 67.21  ? 344  GLN B N   1 
ATOM   7342  C  CA  . GLN B  1  318 ? 11.425  -23.696 -6.067  1.00 65.85  ? 344  GLN B CA  1 
ATOM   7343  C  C   . GLN B  1  318 ? 12.625  -23.580 -6.994  1.00 63.25  ? 344  GLN B C   1 
ATOM   7344  O  O   . GLN B  1  318 ? 12.690  -24.288 -7.996  1.00 62.88  ? 344  GLN B O   1 
ATOM   7345  C  CB  . GLN B  1  318 ? 11.607  -24.902 -5.162  1.00 69.56  ? 344  GLN B CB  1 
ATOM   7346  C  CG  . GLN B  1  318 ? 12.328  -24.574 -3.866  1.00 76.00  ? 344  GLN B CG  1 
ATOM   7347  C  CD  . GLN B  1  318 ? 12.815  -25.805 -3.132  1.00 79.29  ? 344  GLN B CD  1 
ATOM   7348  O  OE1 . GLN B  1  318 ? 13.025  -25.770 -1.909  1.00 79.79  ? 344  GLN B OE1 1 
ATOM   7349  N  NE2 . GLN B  1  318 ? 13.017  -26.905 -3.876  1.00 80.55  ? 344  GLN B NE2 1 
ATOM   7350  N  N   . PHE B  1  319 ? 13.572  -22.702 -6.668  1.00 60.43  ? 345  PHE B N   1 
ATOM   7351  C  CA  . PHE B  1  319 ? 14.750  -22.504 -7.519  1.00 58.68  ? 345  PHE B CA  1 
ATOM   7352  C  C   . PHE B  1  319 ? 15.637  -23.741 -7.602  1.00 58.40  ? 345  PHE B C   1 
ATOM   7353  O  O   . PHE B  1  319 ? 16.031  -24.295 -6.571  1.00 58.49  ? 345  PHE B O   1 
ATOM   7354  C  CB  . PHE B  1  319 ? 15.594  -21.330 -7.025  1.00 57.24  ? 345  PHE B CB  1 
ATOM   7355  C  CG  . PHE B  1  319 ? 16.555  -20.806 -8.055  1.00 55.50  ? 345  PHE B CG  1 
ATOM   7356  C  CD1 . PHE B  1  319 ? 16.090  -20.105 -9.155  1.00 55.83  ? 345  PHE B CD1 1 
ATOM   7357  C  CD2 . PHE B  1  319 ? 17.917  -21.025 -7.937  1.00 54.62  ? 345  PHE B CD2 1 
ATOM   7358  C  CE1 . PHE B  1  319 ? 16.967  -19.628 -10.127 1.00 55.24  ? 345  PHE B CE1 1 
ATOM   7359  C  CE2 . PHE B  1  319 ? 18.805  -20.554 -8.905  1.00 53.89  ? 345  PHE B CE2 1 
ATOM   7360  C  CZ  . PHE B  1  319 ? 18.327  -19.854 -10.002 1.00 53.57  ? 345  PHE B CZ  1 
ATOM   7361  N  N   . PRO B  1  320 ? 15.990  -24.171 -8.832  1.00 57.83  ? 346  PRO B N   1 
ATOM   7362  C  CA  . PRO B  1  320 ? 16.830  -25.354 -9.035  1.00 58.11  ? 346  PRO B CA  1 
ATOM   7363  C  C   . PRO B  1  320 ? 18.210  -25.278 -8.402  1.00 59.74  ? 346  PRO B C   1 
ATOM   7364  O  O   . PRO B  1  320 ? 18.991  -24.398 -8.731  1.00 60.33  ? 346  PRO B O   1 
ATOM   7365  C  CB  . PRO B  1  320 ? 16.876  -25.482 -10.555 1.00 56.30  ? 346  PRO B CB  1 
ATOM   7366  C  CG  . PRO B  1  320 ? 16.743  -24.084 -11.017 1.00 55.35  ? 346  PRO B CG  1 
ATOM   7367  C  CD  . PRO B  1  320 ? 15.684  -23.521 -10.119 1.00 55.50  ? 346  PRO B CD  1 
ATOM   7368  N  N   . THR B  1  321 ? 18.496  -26.207 -7.491  1.00 62.12  ? 347  THR B N   1 
ATOM   7369  C  CA  . THR B  1  321 ? 19.799  -26.259 -6.812  1.00 64.09  ? 347  THR B CA  1 
ATOM   7370  C  C   . THR B  1  321 ? 20.815  -26.985 -7.681  1.00 63.22  ? 347  THR B C   1 
ATOM   7371  O  O   . THR B  1  321 ? 21.118  -28.161 -7.468  1.00 63.78  ? 347  THR B O   1 
ATOM   7372  C  CB  . THR B  1  321 ? 19.732  -26.983 -5.429  1.00 65.41  ? 347  THR B CB  1 
ATOM   7373  O  OG1 . THR B  1  321 ? 18.835  -28.104 -5.506  1.00 66.75  ? 347  THR B OG1 1 
ATOM   7374  C  CG2 . THR B  1  321 ? 19.272  -26.005 -4.335  1.00 65.77  ? 347  THR B CG2 1 
ATOM   7375  N  N   . LEU B  1  322 ? 21.328  -26.251 -8.662  1.00 61.41  ? 348  LEU B N   1 
ATOM   7376  C  CA  . LEU B  1  322 ? 22.296  -26.753 -9.613  1.00 59.34  ? 348  LEU B CA  1 
ATOM   7377  C  C   . LEU B  1  322 ? 23.673  -26.965 -9.002  1.00 58.66  ? 348  LEU B C   1 
ATOM   7378  O  O   . LEU B  1  322 ? 24.156  -26.126 -8.247  1.00 57.85  ? 348  LEU B O   1 
ATOM   7379  C  CB  . LEU B  1  322 ? 22.392  -25.762 -10.761 1.00 58.36  ? 348  LEU B CB  1 
ATOM   7380  C  CG  . LEU B  1  322 ? 21.044  -25.435 -11.396 1.00 56.30  ? 348  LEU B CG  1 
ATOM   7381  C  CD1 . LEU B  1  322 ? 21.156  -24.193 -12.220 1.00 56.77  ? 348  LEU B CD1 1 
ATOM   7382  C  CD2 . LEU B  1  322 ? 20.599  -26.597 -12.253 1.00 55.67  ? 348  LEU B CD2 1 
ATOM   7383  N  N   . LYS B  1  323 ? 24.299  -28.089 -9.342  1.00 58.96  ? 349  LYS B N   1 
ATOM   7384  C  CA  . LYS B  1  323 ? 25.637  -28.415 -8.848  1.00 59.34  ? 349  LYS B CA  1 
ATOM   7385  C  C   . LYS B  1  323 ? 26.479  -29.044 -9.957  1.00 58.57  ? 349  LYS B C   1 
ATOM   7386  O  O   . LYS B  1  323 ? 27.234  -29.984 -9.727  1.00 58.04  ? 349  LYS B O   1 
ATOM   7387  C  CB  . LYS B  1  323 ? 25.538  -29.377 -7.664  1.00 60.37  ? 349  LYS B CB  1 
ATOM   7388  C  CG  . LYS B  1  323 ? 24.861  -28.780 -6.440  1.00 60.32  ? 349  LYS B CG  1 
ATOM   7389  C  CD  . LYS B  1  323 ? 24.727  -29.809 -5.328  1.00 62.13  ? 349  LYS B CD  1 
ATOM   7390  C  CE  . LYS B  1  323 ? 24.251  -29.179 -4.013  1.00 63.95  ? 349  LYS B CE  1 
ATOM   7391  N  NZ  . LYS B  1  323 ? 25.166  -28.095 -3.498  1.00 62.94  ? 349  LYS B NZ  1 
ATOM   7392  N  N   . LEU B  1  324 ? 26.324  -28.517 -11.166 1.00 58.42  ? 350  LEU B N   1 
ATOM   7393  C  CA  . LEU B  1  324 ? 27.050  -28.990 -12.341 1.00 57.20  ? 350  LEU B CA  1 
ATOM   7394  C  C   . LEU B  1  324 ? 28.476  -28.452 -12.284 1.00 57.44  ? 350  LEU B C   1 
ATOM   7395  O  O   . LEU B  1  324 ? 28.692  -27.256 -12.493 1.00 59.42  ? 350  LEU B O   1 
ATOM   7396  C  CB  . LEU B  1  324 ? 26.342  -28.488 -13.603 1.00 54.10  ? 350  LEU B CB  1 
ATOM   7397  C  CG  . LEU B  1  324 ? 24.852  -28.835 -13.636 1.00 49.49  ? 350  LEU B CG  1 
ATOM   7398  C  CD1 . LEU B  1  324 ? 24.118  -27.903 -14.553 1.00 50.58  ? 350  LEU B CD1 1 
ATOM   7399  C  CD2 . LEU B  1  324 ? 24.685  -30.255 -14.083 1.00 49.48  ? 350  LEU B CD2 1 
ATOM   7400  N  N   . LYS B  1  325 ? 29.444  -29.332 -12.021 1.00 56.70  ? 351  LYS B N   1 
ATOM   7401  C  CA  . LYS B  1  325 ? 30.844  -28.931 -11.897 1.00 55.82  ? 351  LYS B CA  1 
ATOM   7402  C  C   . LYS B  1  325 ? 31.523  -28.443 -13.177 1.00 56.31  ? 351  LYS B C   1 
ATOM   7403  O  O   . LYS B  1  325 ? 32.329  -27.514 -13.123 1.00 57.55  ? 351  LYS B O   1 
ATOM   7404  C  CB  . LYS B  1  325 ? 31.678  -30.075 -11.326 1.00 55.80  ? 351  LYS B CB  1 
ATOM   7405  C  CG  . LYS B  1  325 ? 31.109  -30.718 -10.089 1.00 57.57  ? 351  LYS B CG  1 
ATOM   7406  C  CD  . LYS B  1  325 ? 30.906  -29.716 -8.982  1.00 59.28  ? 351  LYS B CD  1 
ATOM   7407  C  CE  . LYS B  1  325 ? 30.198  -30.371 -7.808  1.00 60.99  ? 351  LYS B CE  1 
ATOM   7408  N  NZ  . LYS B  1  325 ? 29.872  -29.376 -6.761  1.00 63.97  ? 351  LYS B NZ  1 
ATOM   7409  N  N   . SER B  1  326 ? 31.207  -29.047 -14.322 1.00 55.12  ? 352  SER B N   1 
ATOM   7410  C  CA  . SER B  1  326 ? 31.845  -28.663 -15.582 1.00 54.39  ? 352  SER B CA  1 
ATOM   7411  C  C   . SER B  1  326 ? 31.200  -27.503 -16.324 1.00 53.93  ? 352  SER B C   1 
ATOM   7412  O  O   . SER B  1  326 ? 31.794  -26.957 -17.258 1.00 54.17  ? 352  SER B O   1 
ATOM   7413  C  CB  . SER B  1  326 ? 31.902  -29.858 -16.532 1.00 56.21  ? 352  SER B CB  1 
ATOM   7414  O  OG  . SER B  1  326 ? 32.322  -31.041 -15.878 1.00 59.89  ? 352  SER B OG  1 
ATOM   7415  N  N   . LEU B  1  327 ? 29.984  -27.144 -15.919 1.00 53.69  ? 353  LEU B N   1 
ATOM   7416  C  CA  . LEU B  1  327 ? 29.231  -26.057 -16.546 1.00 52.06  ? 353  LEU B CA  1 
ATOM   7417  C  C   . LEU B  1  327 ? 30.023  -24.741 -16.572 1.00 52.38  ? 353  LEU B C   1 
ATOM   7418  O  O   . LEU B  1  327 ? 30.568  -24.315 -15.552 1.00 52.07  ? 353  LEU B O   1 
ATOM   7419  C  CB  . LEU B  1  327 ? 27.891  -25.864 -15.807 1.00 48.22  ? 353  LEU B CB  1 
ATOM   7420  C  CG  . LEU B  1  327 ? 26.898  -24.870 -16.423 1.00 46.14  ? 353  LEU B CG  1 
ATOM   7421  C  CD1 . LEU B  1  327 ? 26.377  -25.444 -17.697 1.00 45.81  ? 353  LEU B CD1 1 
ATOM   7422  C  CD2 . LEU B  1  327 ? 25.746  -24.565 -15.490 1.00 43.13  ? 353  LEU B CD2 1 
ATOM   7423  N  N   . LYS B  1  328 ? 30.085  -24.112 -17.746 1.00 52.94  ? 354  LYS B N   1 
ATOM   7424  C  CA  . LYS B  1  328 ? 30.789  -22.842 -17.909 1.00 54.32  ? 354  LYS B CA  1 
ATOM   7425  C  C   . LYS B  1  328 ? 29.838  -21.675 -18.140 1.00 54.66  ? 354  LYS B C   1 
ATOM   7426  O  O   . LYS B  1  328 ? 30.106  -20.558 -17.689 1.00 55.51  ? 354  LYS B O   1 
ATOM   7427  C  CB  . LYS B  1  328 ? 31.785  -22.898 -19.068 1.00 54.40  ? 354  LYS B CB  1 
ATOM   7428  C  CG  . LYS B  1  328 ? 33.081  -23.575 -18.732 1.00 57.67  ? 354  LYS B CG  1 
ATOM   7429  C  CD  . LYS B  1  328 ? 34.123  -23.309 -19.810 1.00 62.07  ? 354  LYS B CD  1 
ATOM   7430  C  CE  . LYS B  1  328 ? 35.364  -24.165 -19.584 1.00 67.07  ? 354  LYS B CE  1 
ATOM   7431  N  NZ  . LYS B  1  328 ? 35.003  -25.637 -19.514 1.00 69.74  ? 354  LYS B NZ  1 
ATOM   7432  N  N   . ARG B  1  329 ? 28.742  -21.928 -18.858 1.00 54.17  ? 355  ARG B N   1 
ATOM   7433  C  CA  . ARG B  1  329 ? 27.740  -20.896 -19.150 1.00 53.60  ? 355  ARG B CA  1 
ATOM   7434  C  C   . ARG B  1  329 ? 26.355  -21.395 -18.757 1.00 51.52  ? 355  ARG B C   1 
ATOM   7435  O  O   . ARG B  1  329 ? 25.979  -22.519 -19.094 1.00 49.47  ? 355  ARG B O   1 
ATOM   7436  C  CB  . ARG B  1  329 ? 27.708  -20.556 -20.649 1.00 56.20  ? 355  ARG B CB  1 
ATOM   7437  C  CG  . ARG B  1  329 ? 29.069  -20.511 -21.322 1.00 63.24  ? 355  ARG B CG  1 
ATOM   7438  C  CD  . ARG B  1  329 ? 28.999  -20.289 -22.842 1.00 67.29  ? 355  ARG B CD  1 
ATOM   7439  N  NE  . ARG B  1  329 ? 28.693  -18.901 -23.184 1.00 72.24  ? 355  ARG B NE  1 
ATOM   7440  C  CZ  . ARG B  1  329 ? 27.464  -18.395 -23.273 1.00 74.77  ? 355  ARG B CZ  1 
ATOM   7441  N  NH1 . ARG B  1  329 ? 26.399  -19.158 -23.052 1.00 75.05  ? 355  ARG B NH1 1 
ATOM   7442  N  NH2 . ARG B  1  329 ? 27.297  -17.113 -23.578 1.00 75.78  ? 355  ARG B NH2 1 
ATOM   7443  N  N   . LEU B  1  330 ? 25.600  -20.549 -18.060 1.00 49.71  ? 356  LEU B N   1 
ATOM   7444  C  CA  . LEU B  1  330 ? 24.244  -20.890 -17.646 1.00 48.12  ? 356  LEU B CA  1 
ATOM   7445  C  C   . LEU B  1  330 ? 23.276  -19.798 -18.051 1.00 48.80  ? 356  LEU B C   1 
ATOM   7446  O  O   . LEU B  1  330 ? 23.443  -18.651 -17.654 1.00 51.93  ? 356  LEU B O   1 
ATOM   7447  C  CB  . LEU B  1  330 ? 24.157  -21.061 -16.130 1.00 45.80  ? 356  LEU B CB  1 
ATOM   7448  C  CG  . LEU B  1  330 ? 22.735  -21.210 -15.567 1.00 44.50  ? 356  LEU B CG  1 
ATOM   7449  C  CD1 . LEU B  1  330 ? 22.150  -22.519 -16.054 1.00 42.62  ? 356  LEU B CD1 1 
ATOM   7450  C  CD2 . LEU B  1  330 ? 22.746  -21.153 -14.043 1.00 41.05  ? 356  LEU B CD2 1 
ATOM   7451  N  N   . THR B  1  331 ? 22.268  -20.133 -18.843 1.00 48.02  ? 357  THR B N   1 
ATOM   7452  C  CA  . THR B  1  331 ? 21.285  -19.129 -19.225 1.00 49.03  ? 357  THR B CA  1 
ATOM   7453  C  C   . THR B  1  331 ? 19.950  -19.577 -18.647 1.00 49.94  ? 357  THR B C   1 
ATOM   7454  O  O   . THR B  1  331 ? 19.347  -20.528 -19.135 1.00 51.82  ? 357  THR B O   1 
ATOM   7455  C  CB  . THR B  1  331 ? 21.152  -18.993 -20.746 1.00 48.82  ? 357  THR B CB  1 
ATOM   7456  O  OG1 . THR B  1  331 ? 22.431  -18.694 -21.318 1.00 51.09  ? 357  THR B OG1 1 
ATOM   7457  C  CG2 . THR B  1  331 ? 20.193  -17.867 -21.088 1.00 47.91  ? 357  THR B CG2 1 
ATOM   7458  N  N   . PHE B  1  332 ? 19.505  -18.895 -17.597 1.00 49.85  ? 358  PHE B N   1 
ATOM   7459  C  CA  . PHE B  1  332 ? 18.252  -19.207 -16.910 1.00 49.92  ? 358  PHE B CA  1 
ATOM   7460  C  C   . PHE B  1  332 ? 17.359  -17.979 -17.009 1.00 49.69  ? 358  PHE B C   1 
ATOM   7461  O  O   . PHE B  1  332 ? 17.306  -17.185 -16.071 1.00 50.49  ? 358  PHE B O   1 
ATOM   7462  C  CB  . PHE B  1  332 ? 18.553  -19.509 -15.433 1.00 49.48  ? 358  PHE B CB  1 
ATOM   7463  C  CG  . PHE B  1  332 ? 17.391  -20.075 -14.663 1.00 51.19  ? 358  PHE B CG  1 
ATOM   7464  C  CD1 . PHE B  1  332 ? 17.063  -21.428 -14.769 1.00 51.28  ? 358  PHE B CD1 1 
ATOM   7465  C  CD2 . PHE B  1  332 ? 16.629  -19.265 -13.824 1.00 50.94  ? 358  PHE B CD2 1 
ATOM   7466  C  CE1 . PHE B  1  332 ? 15.992  -21.977 -14.046 1.00 50.90  ? 358  PHE B CE1 1 
ATOM   7467  C  CE2 . PHE B  1  332 ? 15.549  -19.802 -13.094 1.00 50.99  ? 358  PHE B CE2 1 
ATOM   7468  C  CZ  . PHE B  1  332 ? 15.229  -21.167 -13.207 1.00 50.20  ? 358  PHE B CZ  1 
ATOM   7469  N  N   . THR B  1  333 ? 16.656  -17.814 -18.126 1.00 50.16  ? 359  THR B N   1 
ATOM   7470  C  CA  . THR B  1  333 ? 15.807  -16.628 -18.289 1.00 52.51  ? 359  THR B CA  1 
ATOM   7471  C  C   . THR B  1  333 ? 14.326  -16.834 -18.614 1.00 52.82  ? 359  THR B C   1 
ATOM   7472  O  O   . THR B  1  333 ? 13.899  -17.905 -19.066 1.00 53.33  ? 359  THR B O   1 
ATOM   7473  C  CB  . THR B  1  333 ? 16.376  -15.670 -19.372 1.00 53.00  ? 359  THR B CB  1 
ATOM   7474  O  OG1 . THR B  1  333 ? 15.929  -16.077 -20.668 1.00 52.29  ? 359  THR B OG1 1 
ATOM   7475  C  CG2 . THR B  1  333 ? 17.892  -15.708 -19.360 1.00 54.81  ? 359  THR B CG2 1 
ATOM   7476  N  N   . SER B  1  334 ? 13.560  -15.772 -18.380 1.00 51.61  ? 360  SER B N   1 
ATOM   7477  C  CA  . SER B  1  334 ? 12.133  -15.750 -18.649 1.00 51.89  ? 360  SER B CA  1 
ATOM   7478  C  C   . SER B  1  334 ? 11.355  -16.946 -18.127 1.00 52.98  ? 360  SER B C   1 
ATOM   7479  O  O   . SER B  1  334 ? 10.435  -17.432 -18.772 1.00 54.43  ? 360  SER B O   1 
ATOM   7480  C  CB  . SER B  1  334 ? 11.903  -15.604 -20.147 1.00 49.99  ? 360  SER B CB  1 
ATOM   7481  O  OG  . SER B  1  334 ? 12.499  -14.410 -20.603 1.00 49.53  ? 360  SER B OG  1 
ATOM   7482  N  N   . ASN B  1  335 ? 11.706  -17.407 -16.944 1.00 54.32  ? 361  ASN B N   1 
ATOM   7483  C  CA  . ASN B  1  335 ? 11.013  -18.540 -16.376 1.00 57.47  ? 361  ASN B CA  1 
ATOM   7484  C  C   . ASN B  1  335 ? 9.882   -18.104 -15.461 1.00 60.20  ? 361  ASN B C   1 
ATOM   7485  O  O   . ASN B  1  335 ? 10.065  -17.279 -14.565 1.00 61.69  ? 361  ASN B O   1 
ATOM   7486  C  CB  . ASN B  1  335 ? 11.994  -19.421 -15.603 1.00 56.63  ? 361  ASN B CB  1 
ATOM   7487  C  CG  . ASN B  1  335 ? 13.063  -20.011 -16.491 1.00 57.21  ? 361  ASN B CG  1 
ATOM   7488  O  OD1 . ASN B  1  335 ? 12.762  -20.678 -17.479 1.00 57.15  ? 361  ASN B OD1 1 
ATOM   7489  N  ND2 . ASN B  1  335 ? 14.322  -19.767 -16.150 1.00 57.79  ? 361  ASN B ND2 1 
ATOM   7490  N  N   . LYS B  1  336 ? 8.703   -18.657 -15.692 1.00 62.82  ? 362  LYS B N   1 
ATOM   7491  C  CA  . LYS B  1  336 ? 7.552   -18.341 -14.859 1.00 64.94  ? 362  LYS B CA  1 
ATOM   7492  C  C   . LYS B  1  336 ? 7.544   -19.329 -13.711 1.00 65.45  ? 362  LYS B C   1 
ATOM   7493  O  O   . LYS B  1  336 ? 7.282   -20.503 -13.909 1.00 66.65  ? 362  LYS B O   1 
ATOM   7494  C  CB  . LYS B  1  336 ? 6.270   -18.454 -15.691 1.00 66.50  ? 362  LYS B CB  1 
ATOM   7495  C  CG  . LYS B  1  336 ? 6.319   -19.512 -16.800 1.00 69.40  ? 362  LYS B CG  1 
ATOM   7496  C  CD  . LYS B  1  336 ? 5.151   -19.364 -17.797 1.00 71.45  ? 362  LYS B CD  1 
ATOM   7497  C  CE  . LYS B  1  336 ? 5.077   -20.527 -18.809 1.00 73.19  ? 362  LYS B CE  1 
ATOM   7498  N  NZ  . LYS B  1  336 ? 4.665   -21.862 -18.221 1.00 74.09  ? 362  LYS B NZ  1 
ATOM   7499  N  N   . GLY B  1  337 ? 7.857   -18.874 -12.509 1.00 66.18  ? 363  GLY B N   1 
ATOM   7500  C  CA  . GLY B  1  337 ? 7.873   -19.801 -11.395 1.00 67.39  ? 363  GLY B CA  1 
ATOM   7501  C  C   . GLY B  1  337 ? 7.874   -19.148 -10.033 1.00 68.60  ? 363  GLY B C   1 
ATOM   7502  O  O   . GLY B  1  337 ? 6.986   -18.369 -9.708  1.00 69.10  ? 363  GLY B O   1 
ATOM   7503  N  N   . GLY B  1  338 ? 8.876   -19.477 -9.228  1.00 70.38  ? 364  GLY B N   1 
ATOM   7504  C  CA  . GLY B  1  338 ? 8.974   -18.913 -7.898  1.00 73.00  ? 364  GLY B CA  1 
ATOM   7505  C  C   . GLY B  1  338 ? 9.460   -17.479 -7.935  1.00 74.07  ? 364  GLY B C   1 
ATOM   7506  O  O   . GLY B  1  338 ? 9.415   -16.812 -8.982  1.00 74.20  ? 364  GLY B O   1 
ATOM   7507  N  N   . ASN B  1  339 ? 9.922   -17.001 -6.783  1.00 74.46  ? 365  ASN B N   1 
ATOM   7508  C  CA  . ASN B  1  339 ? 10.423  -15.635 -6.675  1.00 74.49  ? 365  ASN B CA  1 
ATOM   7509  C  C   . ASN B  1  339 ? 11.573  -15.540 -5.688  1.00 71.33  ? 365  ASN B C   1 
ATOM   7510  O  O   . ASN B  1  339 ? 11.872  -14.458 -5.190  1.00 72.62  ? 365  ASN B O   1 
ATOM   7511  C  CB  . ASN B  1  339 ? 9.303   -14.661 -6.243  1.00 76.83  ? 365  ASN B CB  1 
ATOM   7512  C  CG  . ASN B  1  339 ? 8.719   -14.993 -4.862  1.00 78.29  ? 365  ASN B CG  1 
ATOM   7513  O  OD1 . ASN B  1  339 ? 7.901   -15.910 -4.719  1.00 78.55  ? 365  ASN B OD1 1 
ATOM   7514  N  ND2 . ASN B  1  339 ? 9.143   -14.246 -3.843  1.00 76.55  ? 365  ASN B ND2 1 
ATOM   7515  N  N   . ALA B  1  340 ? 12.213  -16.666 -5.399  1.00 67.10  ? 366  ALA B N   1 
ATOM   7516  C  CA  . ALA B  1  340 ? 13.317  -16.654 -4.461  1.00 62.16  ? 366  ALA B CA  1 
ATOM   7517  C  C   . ALA B  1  340 ? 14.489  -17.502 -4.918  1.00 59.90  ? 366  ALA B C   1 
ATOM   7518  O  O   . ALA B  1  340 ? 14.387  -18.715 -5.094  1.00 58.78  ? 366  ALA B O   1 
ATOM   7519  C  CB  . ALA B  1  340 ? 12.844  -17.101 -3.108  1.00 62.20  ? 366  ALA B CB  1 
ATOM   7520  N  N   . PHE B  1  341 ? 15.607  -16.824 -5.114  1.00 57.98  ? 367  PHE B N   1 
ATOM   7521  C  CA  . PHE B  1  341 ? 16.856  -17.427 -5.533  1.00 55.86  ? 367  PHE B CA  1 
ATOM   7522  C  C   . PHE B  1  341 ? 17.501  -18.062 -4.316  1.00 56.21  ? 367  PHE B C   1 
ATOM   7523  O  O   . PHE B  1  341 ? 17.323  -17.598 -3.195  1.00 56.01  ? 367  PHE B O   1 
ATOM   7524  C  CB  . PHE B  1  341 ? 17.782  -16.335 -6.095  1.00 52.47  ? 367  PHE B CB  1 
ATOM   7525  C  CG  . PHE B  1  341 ? 19.198  -16.793 -6.356  1.00 49.52  ? 367  PHE B CG  1 
ATOM   7526  C  CD1 . PHE B  1  341 ? 19.525  -17.488 -7.527  1.00 48.51  ? 367  PHE B CD1 1 
ATOM   7527  C  CD2 . PHE B  1  341 ? 20.211  -16.519 -5.438  1.00 46.33  ? 367  PHE B CD2 1 
ATOM   7528  C  CE1 . PHE B  1  341 ? 20.838  -17.900 -7.775  1.00 44.24  ? 367  PHE B CE1 1 
ATOM   7529  C  CE2 . PHE B  1  341 ? 21.517  -16.925 -5.673  1.00 44.16  ? 367  PHE B CE2 1 
ATOM   7530  C  CZ  . PHE B  1  341 ? 21.832  -17.618 -6.850  1.00 45.01  ? 367  PHE B CZ  1 
ATOM   7531  N  N   . SER B  1  342 ? 18.230  -19.145 -4.537  1.00 57.97  ? 368  SER B N   1 
ATOM   7532  C  CA  . SER B  1  342 ? 18.949  -19.805 -3.459  1.00 60.02  ? 368  SER B CA  1 
ATOM   7533  C  C   . SER B  1  342 ? 20.299  -20.128 -4.083  1.00 60.91  ? 368  SER B C   1 
ATOM   7534  O  O   . SER B  1  342 ? 20.422  -20.134 -5.313  1.00 60.34  ? 368  SER B O   1 
ATOM   7535  C  CB  . SER B  1  342 ? 18.225  -21.072 -2.993  1.00 60.32  ? 368  SER B CB  1 
ATOM   7536  O  OG  . SER B  1  342 ? 18.145  -22.048 -4.017  1.00 63.28  ? 368  SER B OG  1 
ATOM   7537  N  N   . GLU B  1  343 ? 21.306  -20.365 -3.245  1.00 62.11  ? 369  GLU B N   1 
ATOM   7538  C  CA  . GLU B  1  343 ? 22.659  -20.656 -3.717  1.00 63.27  ? 369  GLU B CA  1 
ATOM   7539  C  C   . GLU B  1  343 ? 22.749  -21.793 -4.709  1.00 61.37  ? 369  GLU B C   1 
ATOM   7540  O  O   . GLU B  1  343 ? 21.982  -22.751 -4.659  1.00 62.11  ? 369  GLU B O   1 
ATOM   7541  C  CB  . GLU B  1  343 ? 23.575  -21.028 -2.558  1.00 67.95  ? 369  GLU B CB  1 
ATOM   7542  C  CG  . GLU B  1  343 ? 23.505  -20.120 -1.333  1.00 76.36  ? 369  GLU B CG  1 
ATOM   7543  C  CD  . GLU B  1  343 ? 24.487  -20.558 -0.241  1.00 80.26  ? 369  GLU B CD  1 
ATOM   7544  O  OE1 . GLU B  1  343 ? 24.555  -21.778 0.047   1.00 82.24  ? 369  GLU B OE1 1 
ATOM   7545  O  OE2 . GLU B  1  343 ? 25.183  -19.687 0.333   1.00 82.34  ? 369  GLU B OE2 1 
ATOM   7546  N  N   . VAL B  1  344 ? 23.706  -21.672 -5.614  1.00 59.12  ? 370  VAL B N   1 
ATOM   7547  C  CA  . VAL B  1  344 ? 23.972  -22.710 -6.588  1.00 57.99  ? 370  VAL B CA  1 
ATOM   7548  C  C   . VAL B  1  344 ? 25.443  -22.978 -6.369  1.00 57.78  ? 370  VAL B C   1 
ATOM   7549  O  O   . VAL B  1  344 ? 26.122  -22.203 -5.703  1.00 58.23  ? 370  VAL B O   1 
ATOM   7550  C  CB  . VAL B  1  344 ? 23.732  -22.251 -8.051  1.00 57.90  ? 370  VAL B CB  1 
ATOM   7551  C  CG1 . VAL B  1  344 ? 22.269  -21.951 -8.259  1.00 57.47  ? 370  VAL B CG1 1 
ATOM   7552  C  CG2 . VAL B  1  344 ? 24.569  -21.033 -8.379  1.00 56.20  ? 370  VAL B CG2 1 
ATOM   7553  N  N   . ASP B  1  345 ? 25.951  -24.072 -6.904  1.00 57.59  ? 371  ASP B N   1 
ATOM   7554  C  CA  . ASP B  1  345 ? 27.358  -24.362 -6.718  1.00 58.32  ? 371  ASP B CA  1 
ATOM   7555  C  C   . ASP B  1  345 ? 27.990  -24.805 -8.018  1.00 57.50  ? 371  ASP B C   1 
ATOM   7556  O  O   . ASP B  1  345 ? 28.145  -26.006 -8.273  1.00 58.01  ? 371  ASP B O   1 
ATOM   7557  C  CB  . ASP B  1  345 ? 27.531  -25.430 -5.653  1.00 61.98  ? 371  ASP B CB  1 
ATOM   7558  C  CG  . ASP B  1  345 ? 28.950  -25.901 -5.550  1.00 66.34  ? 371  ASP B CG  1 
ATOM   7559  O  OD1 . ASP B  1  345 ? 29.868  -25.056 -5.650  1.00 68.94  ? 371  ASP B OD1 1 
ATOM   7560  O  OD2 . ASP B  1  345 ? 29.149  -27.115 -5.362  1.00 71.52  ? 371  ASP B OD2 1 
ATOM   7561  N  N   . LEU B  1  346 ? 28.370  -23.814 -8.824  1.00 54.89  ? 372  LEU B N   1 
ATOM   7562  C  CA  . LEU B  1  346 ? 28.952  -24.044 -10.139 1.00 52.45  ? 372  LEU B CA  1 
ATOM   7563  C  C   . LEU B  1  346 ? 30.404  -23.587 -10.231 1.00 52.53  ? 372  LEU B C   1 
ATOM   7564  O  O   . LEU B  1  346 ? 30.690  -22.551 -10.813 1.00 53.01  ? 372  LEU B O   1 
ATOM   7565  C  CB  . LEU B  1  346 ? 28.081  -23.322 -11.165 1.00 48.80  ? 372  LEU B CB  1 
ATOM   7566  C  CG  . LEU B  1  346 ? 26.590  -23.634 -10.919 1.00 46.00  ? 372  LEU B CG  1 
ATOM   7567  C  CD1 . LEU B  1  346 ? 25.694  -22.893 -11.870 1.00 44.39  ? 372  LEU B CD1 1 
ATOM   7568  C  CD2 . LEU B  1  346 ? 26.361  -25.103 -11.059 1.00 42.73  ? 372  LEU B CD2 1 
ATOM   7569  N  N   . PRO B  1  347 ? 31.343  -24.386 -9.678  1.00 52.96  ? 373  PRO B N   1 
ATOM   7570  C  CA  . PRO B  1  347 ? 32.786  -24.109 -9.662  1.00 52.53  ? 373  PRO B CA  1 
ATOM   7571  C  C   . PRO B  1  347 ? 33.423  -23.669 -10.972 1.00 52.98  ? 373  PRO B C   1 
ATOM   7572  O  O   . PRO B  1  347 ? 34.402  -22.916 -10.948 1.00 54.90  ? 373  PRO B O   1 
ATOM   7573  C  CB  . PRO B  1  347 ? 33.385  -25.419 -9.151  1.00 50.25  ? 373  PRO B CB  1 
ATOM   7574  C  CG  . PRO B  1  347 ? 32.404  -26.426 -9.596  1.00 51.24  ? 373  PRO B CG  1 
ATOM   7575  C  CD  . PRO B  1  347 ? 31.103  -25.776 -9.251  1.00 52.11  ? 373  PRO B CD  1 
ATOM   7576  N  N   . SER B  1  348 ? 32.876  -24.125 -12.103 1.00 52.31  ? 374  SER B N   1 
ATOM   7577  C  CA  . SER B  1  348 ? 33.426  -23.778 -13.416 1.00 50.23  ? 374  SER B CA  1 
ATOM   7578  C  C   . SER B  1  348 ? 32.719  -22.654 -14.151 1.00 49.54  ? 374  SER B C   1 
ATOM   7579  O  O   . SER B  1  348 ? 33.132  -22.271 -15.230 1.00 49.82  ? 374  SER B O   1 
ATOM   7580  C  CB  . SER B  1  348 ? 33.433  -25.002 -14.327 1.00 49.87  ? 374  SER B CB  1 
ATOM   7581  O  OG  . SER B  1  348 ? 34.362  -25.974 -13.875 1.00 49.10  ? 374  SER B OG  1 
ATOM   7582  N  N   . LEU B  1  349 ? 31.663  -22.120 -13.560 1.00 49.56  ? 375  LEU B N   1 
ATOM   7583  C  CA  . LEU B  1  349 ? 30.867  -21.074 -14.183 1.00 50.26  ? 375  LEU B CA  1 
ATOM   7584  C  C   . LEU B  1  349 ? 31.607  -19.795 -14.577 1.00 51.54  ? 375  LEU B C   1 
ATOM   7585  O  O   . LEU B  1  349 ? 32.347  -19.241 -13.776 1.00 52.43  ? 375  LEU B O   1 
ATOM   7586  C  CB  . LEU B  1  349 ? 29.706  -20.721 -13.251 1.00 48.02  ? 375  LEU B CB  1 
ATOM   7587  C  CG  . LEU B  1  349 ? 28.580  -19.928 -13.896 1.00 47.61  ? 375  LEU B CG  1 
ATOM   7588  C  CD1 . LEU B  1  349 ? 27.954  -20.776 -14.978 1.00 46.05  ? 375  LEU B CD1 1 
ATOM   7589  C  CD2 . LEU B  1  349 ? 27.568  -19.520 -12.850 1.00 45.18  ? 375  LEU B CD2 1 
ATOM   7590  N  N   . GLU B  1  350 ? 31.395  -19.331 -15.810 1.00 52.03  ? 376  GLU B N   1 
ATOM   7591  C  CA  . GLU B  1  350 ? 32.007  -18.098 -16.287 1.00 54.24  ? 376  GLU B CA  1 
ATOM   7592  C  C   . GLU B  1  350 ? 30.954  -17.128 -16.831 1.00 53.94  ? 376  GLU B C   1 
ATOM   7593  O  O   . GLU B  1  350 ? 31.097  -15.910 -16.713 1.00 55.09  ? 376  GLU B O   1 
ATOM   7594  C  CB  . GLU B  1  350 ? 33.030  -18.374 -17.387 1.00 58.84  ? 376  GLU B CB  1 
ATOM   7595  C  CG  . GLU B  1  350 ? 34.211  -19.244 -16.962 1.00 65.62  ? 376  GLU B CG  1 
ATOM   7596  C  CD  . GLU B  1  350 ? 35.197  -19.506 -18.100 1.00 68.55  ? 376  GLU B CD  1 
ATOM   7597  O  OE1 . GLU B  1  350 ? 35.824  -20.593 -18.096 1.00 68.35  ? 376  GLU B OE1 1 
ATOM   7598  O  OE2 . GLU B  1  350 ? 35.337  -18.625 -18.989 1.00 70.31  ? 376  GLU B OE2 1 
ATOM   7599  N  N   . PHE B  1  351 ? 29.907  -17.662 -17.441 1.00 52.02  ? 377  PHE B N   1 
ATOM   7600  C  CA  . PHE B  1  351 ? 28.846  -16.829 -17.986 1.00 50.96  ? 377  PHE B CA  1 
ATOM   7601  C  C   . PHE B  1  351 ? 27.593  -17.112 -17.159 1.00 50.59  ? 377  PHE B C   1 
ATOM   7602  O  O   . PHE B  1  351 ? 27.214  -18.275 -16.997 1.00 50.13  ? 377  PHE B O   1 
ATOM   7603  C  CB  . PHE B  1  351 ? 28.595  -17.184 -19.449 1.00 51.65  ? 377  PHE B CB  1 
ATOM   7604  C  CG  . PHE B  1  351 ? 27.589  -16.298 -20.121 1.00 54.90  ? 377  PHE B CG  1 
ATOM   7605  C  CD1 . PHE B  1  351 ? 27.982  -15.115 -20.747 1.00 57.06  ? 377  PHE B CD1 1 
ATOM   7606  C  CD2 . PHE B  1  351 ? 26.233  -16.615 -20.091 1.00 56.72  ? 377  PHE B CD2 1 
ATOM   7607  C  CE1 . PHE B  1  351 ? 27.029  -14.252 -21.333 1.00 57.28  ? 377  PHE B CE1 1 
ATOM   7608  C  CE2 . PHE B  1  351 ? 25.272  -15.762 -20.672 1.00 58.20  ? 377  PHE B CE2 1 
ATOM   7609  C  CZ  . PHE B  1  351 ? 25.671  -14.579 -21.293 1.00 57.10  ? 377  PHE B CZ  1 
ATOM   7610  N  N   . LEU B  1  352 ? 26.947  -16.074 -16.635 1.00 49.55  ? 378  LEU B N   1 
ATOM   7611  C  CA  . LEU B  1  352 ? 25.755  -16.301 -15.831 1.00 49.24  ? 378  LEU B CA  1 
ATOM   7612  C  C   . LEU B  1  352 ? 24.628  -15.333 -16.125 1.00 49.92  ? 378  LEU B C   1 
ATOM   7613  O  O   . LEU B  1  352 ? 24.659  -14.198 -15.656 1.00 49.07  ? 378  LEU B O   1 
ATOM   7614  C  CB  . LEU B  1  352 ? 26.081  -16.214 -14.335 1.00 48.21  ? 378  LEU B CB  1 
ATOM   7615  C  CG  . LEU B  1  352 ? 25.266  -17.048 -13.323 1.00 50.05  ? 378  LEU B CG  1 
ATOM   7616  C  CD1 . LEU B  1  352 ? 25.278  -16.314 -11.991 1.00 47.07  ? 378  LEU B CD1 1 
ATOM   7617  C  CD2 . LEU B  1  352 ? 23.817  -17.285 -13.785 1.00 48.98  ? 378  LEU B CD2 1 
ATOM   7618  N  N   . ASP B  1  353 ? 23.640  -15.782 -16.906 1.00 50.43  ? 379  ASP B N   1 
ATOM   7619  C  CA  . ASP B  1  353 ? 22.472  -14.956 -17.207 1.00 51.29  ? 379  ASP B CA  1 
ATOM   7620  C  C   . ASP B  1  353 ? 21.311  -15.544 -16.423 1.00 50.59  ? 379  ASP B C   1 
ATOM   7621  O  O   . ASP B  1  353 ? 20.940  -16.691 -16.632 1.00 51.07  ? 379  ASP B O   1 
ATOM   7622  C  CB  . ASP B  1  353 ? 22.123  -14.938 -18.694 1.00 52.60  ? 379  ASP B CB  1 
ATOM   7623  C  CG  . ASP B  1  353 ? 20.911  -14.028 -18.996 1.00 54.84  ? 379  ASP B CG  1 
ATOM   7624  O  OD1 . ASP B  1  353 ? 20.690  -13.684 -20.191 1.00 53.29  ? 379  ASP B OD1 1 
ATOM   7625  O  OD2 . ASP B  1  353 ? 20.176  -13.667 -18.030 1.00 52.25  ? 379  ASP B OD2 1 
ATOM   7626  N  N   . LEU B  1  354 ? 20.749  -14.733 -15.532 1.00 49.19  ? 380  LEU B N   1 
ATOM   7627  C  CA  . LEU B  1  354 ? 19.666  -15.126 -14.653 1.00 47.53  ? 380  LEU B CA  1 
ATOM   7628  C  C   . LEU B  1  354 ? 18.644  -13.998 -14.723 1.00 48.81  ? 380  LEU B C   1 
ATOM   7629  O  O   . LEU B  1  354 ? 17.966  -13.687 -13.744 1.00 48.94  ? 380  LEU B O   1 
ATOM   7630  C  CB  . LEU B  1  354 ? 20.219  -15.225 -13.238 1.00 45.38  ? 380  LEU B CB  1 
ATOM   7631  C  CG  . LEU B  1  354 ? 19.913  -16.415 -12.344 1.00 45.67  ? 380  LEU B CG  1 
ATOM   7632  C  CD1 . LEU B  1  354 ? 20.426  -17.688 -12.964 1.00 46.00  ? 380  LEU B CD1 1 
ATOM   7633  C  CD2 . LEU B  1  354 ? 20.580  -16.184 -11.012 1.00 46.50  ? 380  LEU B CD2 1 
ATOM   7634  N  N   . SER B  1  355 ? 18.533  -13.384 -15.893 1.00 48.77  ? 381  SER B N   1 
ATOM   7635  C  CA  . SER B  1  355 ? 17.632  -12.255 -16.058 1.00 50.11  ? 381  SER B CA  1 
ATOM   7636  C  C   . SER B  1  355 ? 16.183  -12.604 -16.344 1.00 50.59  ? 381  SER B C   1 
ATOM   7637  O  O   . SER B  1  355 ? 15.887  -13.711 -16.800 1.00 51.71  ? 381  SER B O   1 
ATOM   7638  C  CB  . SER B  1  355 ? 18.142  -11.357 -17.182 1.00 51.06  ? 381  SER B CB  1 
ATOM   7639  O  OG  . SER B  1  355 ? 18.042  -12.013 -18.436 1.00 53.39  ? 381  SER B OG  1 
ATOM   7640  N  N   . ARG B  1  356 ? 15.293  -11.640 -16.079 1.00 49.23  ? 382  ARG B N   1 
ATOM   7641  C  CA  . ARG B  1  356 ? 13.854  -11.764 -16.335 1.00 47.55  ? 382  ARG B CA  1 
ATOM   7642  C  C   . ARG B  1  356 ? 13.119  -12.921 -15.645 1.00 46.70  ? 382  ARG B C   1 
ATOM   7643  O  O   . ARG B  1  356 ? 12.291  -13.580 -16.263 1.00 46.34  ? 382  ARG B O   1 
ATOM   7644  C  CB  . ARG B  1  356 ? 13.628  -11.867 -17.838 1.00 47.63  ? 382  ARG B CB  1 
ATOM   7645  C  CG  . ARG B  1  356 ? 14.329  -10.788 -18.639 1.00 50.09  ? 382  ARG B CG  1 
ATOM   7646  C  CD  . ARG B  1  356 ? 14.034  -10.914 -20.117 1.00 52.59  ? 382  ARG B CD  1 
ATOM   7647  N  NE  . ARG B  1  356 ? 14.209  -9.640  -20.807 1.00 56.69  ? 382  ARG B NE  1 
ATOM   7648  C  CZ  . ARG B  1  356 ? 15.386  -9.066  -21.037 1.00 58.81  ? 382  ARG B CZ  1 
ATOM   7649  N  NH1 . ARG B  1  356 ? 16.505  -9.665  -20.629 1.00 59.72  ? 382  ARG B NH1 1 
ATOM   7650  N  NH2 . ARG B  1  356 ? 15.443  -7.896  -21.673 1.00 59.53  ? 382  ARG B NH2 1 
ATOM   7651  N  N   . ASN B  1  357 ? 13.403  -13.160 -14.373 1.00 44.96  ? 383  ASN B N   1 
ATOM   7652  C  CA  . ASN B  1  357 ? 12.749  -14.233 -13.670 1.00 44.34  ? 383  ASN B CA  1 
ATOM   7653  C  C   . ASN B  1  357 ? 11.932  -13.732 -12.511 1.00 46.30  ? 383  ASN B C   1 
ATOM   7654  O  O   . ASN B  1  357 ? 11.272  -14.531 -11.850 1.00 51.19  ? 383  ASN B O   1 
ATOM   7655  C  CB  . ASN B  1  357 ? 13.774  -15.218 -13.133 1.00 43.74  ? 383  ASN B CB  1 
ATOM   7656  C  CG  . ASN B  1  357 ? 14.482  -15.970 -14.221 1.00 43.93  ? 383  ASN B CG  1 
ATOM   7657  O  OD1 . ASN B  1  357 ? 13.867  -16.737 -14.970 1.00 42.03  ? 383  ASN B OD1 1 
ATOM   7658  N  ND2 . ASN B  1  357 ? 15.790  -15.761 -14.322 1.00 42.84  ? 383  ASN B ND2 1 
ATOM   7659  N  N   . GLY B  1  358 ? 11.977  -12.432 -12.242 1.00 45.43  ? 384  GLY B N   1 
ATOM   7660  C  CA  . GLY B  1  358 ? 11.241  -11.890 -11.113 1.00 43.82  ? 384  GLY B CA  1 
ATOM   7661  C  C   . GLY B  1  358 ? 11.826  -12.385 -9.800  1.00 45.20  ? 384  GLY B C   1 
ATOM   7662  O  O   . GLY B  1  358 ? 11.188  -12.290 -8.753  1.00 47.70  ? 384  GLY B O   1 
ATOM   7663  N  N   . LEU B  1  359 ? 13.047  -12.907 -9.853  1.00 44.70  ? 385  LEU B N   1 
ATOM   7664  C  CA  . LEU B  1  359 ? 13.725  -13.430 -8.680  1.00 46.51  ? 385  LEU B CA  1 
ATOM   7665  C  C   . LEU B  1  359 ? 14.135  -12.373 -7.647  1.00 48.23  ? 385  LEU B C   1 
ATOM   7666  O  O   . LEU B  1  359 ? 14.364  -11.216 -7.991  1.00 49.80  ? 385  LEU B O   1 
ATOM   7667  C  CB  . LEU B  1  359 ? 14.968  -14.182 -9.130  1.00 47.83  ? 385  LEU B CB  1 
ATOM   7668  C  CG  . LEU B  1  359 ? 14.730  -15.452 -9.943  1.00 51.13  ? 385  LEU B CG  1 
ATOM   7669  C  CD1 . LEU B  1  359 ? 16.071  -16.081 -10.307 1.00 52.11  ? 385  LEU B CD1 1 
ATOM   7670  C  CD2 . LEU B  1  359 ? 13.892  -16.441 -9.124  1.00 53.77  ? 385  LEU B CD2 1 
ATOM   7671  N  N   . SER B  1  360 ? 14.247  -12.775 -6.381  1.00 48.26  ? 386  SER B N   1 
ATOM   7672  C  CA  . SER B  1  360 ? 14.673  -11.872 -5.322  1.00 47.22  ? 386  SER B CA  1 
ATOM   7673  C  C   . SER B  1  360 ? 15.846  -12.489 -4.584  1.00 47.85  ? 386  SER B C   1 
ATOM   7674  O  O   . SER B  1  360 ? 15.779  -13.621 -4.148  1.00 47.31  ? 386  SER B O   1 
ATOM   7675  C  CB  . SER B  1  360 ? 13.534  -11.607 -4.341  1.00 47.52  ? 386  SER B CB  1 
ATOM   7676  O  OG  . SER B  1  360 ? 12.510  -10.836 -4.948  1.00 51.63  ? 386  SER B OG  1 
ATOM   7677  N  N   . PHE B  1  361 ? 16.929  -11.732 -4.460  1.00 50.28  ? 387  PHE B N   1 
ATOM   7678  C  CA  . PHE B  1  361 ? 18.138  -12.176 -3.776  1.00 52.03  ? 387  PHE B CA  1 
ATOM   7679  C  C   . PHE B  1  361 ? 18.207  -11.464 -2.443  1.00 54.45  ? 387  PHE B C   1 
ATOM   7680  O  O   . PHE B  1  361 ? 18.091  -10.247 -2.409  1.00 55.83  ? 387  PHE B O   1 
ATOM   7681  C  CB  . PHE B  1  361 ? 19.354  -11.805 -4.613  1.00 52.85  ? 387  PHE B CB  1 
ATOM   7682  C  CG  . PHE B  1  361 ? 19.329  -12.395 -5.989  1.00 56.13  ? 387  PHE B CG  1 
ATOM   7683  C  CD1 . PHE B  1  361 ? 20.357  -13.234 -6.413  1.00 56.36  ? 387  PHE B CD1 1 
ATOM   7684  C  CD2 . PHE B  1  361 ? 18.249  -12.149 -6.851  1.00 56.69  ? 387  PHE B CD2 1 
ATOM   7685  C  CE1 . PHE B  1  361 ? 20.313  -13.828 -7.678  1.00 57.36  ? 387  PHE B CE1 1 
ATOM   7686  C  CE2 . PHE B  1  361 ? 18.187  -12.739 -8.121  1.00 57.53  ? 387  PHE B CE2 1 
ATOM   7687  C  CZ  . PHE B  1  361 ? 19.221  -13.582 -8.539  1.00 57.75  ? 387  PHE B CZ  1 
ATOM   7688  N  N   . LYS B  1  362 ? 18.409  -12.192 -1.347  1.00 56.99  ? 388  LYS B N   1 
ATOM   7689  C  CA  . LYS B  1  362 ? 18.446  -11.540 -0.046  1.00 58.72  ? 388  LYS B CA  1 
ATOM   7690  C  C   . LYS B  1  362 ? 19.823  -11.121 0.430   1.00 60.66  ? 388  LYS B C   1 
ATOM   7691  O  O   . LYS B  1  362 ? 19.938  -10.518 1.495   1.00 65.07  ? 388  LYS B O   1 
ATOM   7692  C  CB  . LYS B  1  362 ? 17.772  -12.409 1.025   1.00 60.97  ? 388  LYS B CB  1 
ATOM   7693  C  CG  . LYS B  1  362 ? 18.663  -13.487 1.671   1.00 65.70  ? 388  LYS B CG  1 
ATOM   7694  C  CD  . LYS B  1  362 ? 18.000  -14.111 2.923   1.00 68.44  ? 388  LYS B CD  1 
ATOM   7695  C  CE  . LYS B  1  362 ? 16.840  -15.067 2.577   1.00 70.38  ? 388  LYS B CE  1 
ATOM   7696  N  NZ  . LYS B  1  362 ? 17.316  -16.404 2.117   1.00 71.02  ? 388  LYS B NZ  1 
ATOM   7697  N  N   . GLY B  1  363 ? 20.867  -11.415 -0.335  1.00 60.27  ? 389  GLY B N   1 
ATOM   7698  C  CA  . GLY B  1  363 ? 22.203  -11.019 0.095   1.00 60.80  ? 389  GLY B CA  1 
ATOM   7699  C  C   . GLY B  1  363 ? 23.173  -11.117 -1.052  1.00 61.03  ? 389  GLY B C   1 
ATOM   7700  O  O   . GLY B  1  363 ? 23.776  -12.138 -1.298  1.00 62.21  ? 389  GLY B O   1 
ATOM   7701  N  N   . CYS B  1  364 ? 23.370  -10.035 -1.748  1.00 64.87  ? 390  CYS B N   1 
ATOM   7702  C  CA  . CYS B  1  364 ? 24.227  -10.098 -2.926  1.00 63.54  ? 390  CYS B CA  1 
ATOM   7703  C  C   . CYS B  1  364 ? 25.496  -9.381  -2.452  1.00 62.34  ? 390  CYS B C   1 
ATOM   7704  O  O   . CYS B  1  364 ? 25.399  -8.538  -1.565  1.00 62.21  ? 390  CYS B O   1 
ATOM   7705  C  CB  . CYS B  1  364 ? 23.593  -9.351  -4.102  1.00 63.07  ? 390  CYS B CB  1 
ATOM   7706  S  SG  . CYS B  1  364 ? 24.270  -9.695  -5.736  1.00 71.68  ? 390  CYS B SG  1 
ATOM   7707  N  N   . CYS B  1  365 ? 26.689  -9.693  -2.966  1.00 60.54  ? 391  CYS B N   1 
ATOM   7708  C  CA  . CYS B  1  365 ? 26.984  -10.748 -3.929  1.00 60.37  ? 391  CYS B CA  1 
ATOM   7709  C  C   . CYS B  1  365 ? 28.294  -11.364 -3.469  1.00 58.85  ? 391  CYS B C   1 
ATOM   7710  O  O   . CYS B  1  365 ? 29.200  -10.652 -3.045  1.00 58.24  ? 391  CYS B O   1 
ATOM   7711  C  CB  . CYS B  1  365 ? 27.189  -10.159 -5.326  1.00 61.95  ? 391  CYS B CB  1 
ATOM   7712  S  SG  . CYS B  1  365 ? 26.083  -8.792  -5.710  1.00 72.33  ? 391  CYS B SG  1 
ATOM   7713  N  N   . SER B  1  366 ? 28.414  -12.656 -3.497  1.00 68.03  ? 392  SER B N   1 
ATOM   7714  C  CA  . SER B  1  366 ? 29.635  -13.235 -3.007  1.00 68.05  ? 392  SER B CA  1 
ATOM   7715  C  C   . SER B  1  366 ? 29.862  -14.437 -3.869  1.00 68.33  ? 392  SER B C   1 
ATOM   7716  O  O   . SER B  1  366 ? 29.024  -14.762 -4.706  1.00 68.62  ? 392  SER B O   1 
ATOM   7717  C  CB  . SER B  1  366 ? 29.440  -13.633 -1.542  1.00 68.25  ? 392  SER B CB  1 
ATOM   7718  O  OG  . SER B  1  366 ? 30.631  -14.132 -0.963  1.00 69.67  ? 392  SER B OG  1 
ATOM   7719  N  N   . GLN B  1  367 ? 30.983  -15.109 -3.669  1.00 69.12  ? 393  GLN B N   1 
ATOM   7720  C  CA  . GLN B  1  367 ? 31.284  -16.288 -4.459  1.00 69.74  ? 393  GLN B CA  1 
ATOM   7721  C  C   . GLN B  1  367 ? 30.489  -17.468 -3.934  1.00 68.66  ? 393  GLN B C   1 
ATOM   7722  O  O   . GLN B  1  367 ? 30.289  -18.454 -4.630  1.00 68.35  ? 393  GLN B O   1 
ATOM   7723  C  CB  . GLN B  1  367 ? 32.766  -16.607 -4.390  1.00 70.48  ? 393  GLN B CB  1 
ATOM   7724  C  CG  . GLN B  1  367 ? 33.161  -17.282 -3.120  1.00 73.33  ? 393  GLN B CG  1 
ATOM   7725  C  CD  . GLN B  1  367 ? 34.293  -18.243 -3.354  1.00 75.78  ? 393  GLN B CD  1 
ATOM   7726  O  OE1 . GLN B  1  367 ? 35.455  -17.836 -3.434  1.00 77.65  ? 393  GLN B OE1 1 
ATOM   7727  N  NE2 . GLN B  1  367 ? 33.965  -19.531 -3.491  1.00 75.74  ? 393  GLN B NE2 1 
ATOM   7728  N  N   . SER B  1  368 ? 30.040  -17.348 -2.693  1.00 68.57  ? 394  SER B N   1 
ATOM   7729  C  CA  . SER B  1  368 ? 29.254  -18.386 -2.034  1.00 68.34  ? 394  SER B CA  1 
ATOM   7730  C  C   . SER B  1  368 ? 27.813  -18.465 -2.579  1.00 67.38  ? 394  SER B C   1 
ATOM   7731  O  O   . SER B  1  368 ? 27.059  -19.380 -2.252  1.00 65.93  ? 394  SER B O   1 
ATOM   7732  C  CB  . SER B  1  368 ? 29.238  -18.113 -0.524  1.00 68.35  ? 394  SER B CB  1 
ATOM   7733  O  OG  . SER B  1  368 ? 28.839  -16.776 -0.255  1.00 70.29  ? 394  SER B OG  1 
ATOM   7734  N  N   . ASP B  1  369 ? 27.439  -17.502 -3.414  1.00 67.30  ? 395  ASP B N   1 
ATOM   7735  C  CA  . ASP B  1  369 ? 26.105  -17.473 -3.994  1.00 66.32  ? 395  ASP B CA  1 
ATOM   7736  C  C   . ASP B  1  369 ? 26.055  -18.308 -5.251  1.00 64.64  ? 395  ASP B C   1 
ATOM   7737  O  O   . ASP B  1  369 ? 25.033  -18.918 -5.562  1.00 64.80  ? 395  ASP B O   1 
ATOM   7738  C  CB  . ASP B  1  369 ? 25.706  -16.043 -4.340  1.00 67.44  ? 395  ASP B CB  1 
ATOM   7739  C  CG  . ASP B  1  369 ? 25.386  -15.230 -3.118  1.00 70.36  ? 395  ASP B CG  1 
ATOM   7740  O  OD1 . ASP B  1  369 ? 26.304  -14.990 -2.308  1.00 73.00  ? 395  ASP B OD1 1 
ATOM   7741  O  OD2 . ASP B  1  369 ? 24.209  -14.842 -2.954  1.00 72.91  ? 395  ASP B OD2 1 
ATOM   7742  N  N   . PHE B  1  370 ? 27.176  -18.344 -5.957  1.00 62.04  ? 396  PHE B N   1 
ATOM   7743  C  CA  . PHE B  1  370 ? 27.264  -19.070 -7.198  1.00 60.08  ? 396  PHE B CA  1 
ATOM   7744  C  C   . PHE B  1  370 ? 28.206  -20.249 -7.134  1.00 59.91  ? 396  PHE B C   1 
ATOM   7745  O  O   . PHE B  1  370 ? 28.081  -21.192 -7.909  1.00 59.92  ? 396  PHE B O   1 
ATOM   7746  C  CB  . PHE B  1  370 ? 27.667  -18.089 -8.281  1.00 58.50  ? 396  PHE B CB  1 
ATOM   7747  C  CG  . PHE B  1  370 ? 26.837  -16.830 -8.272  1.00 57.31  ? 396  PHE B CG  1 
ATOM   7748  C  CD1 . PHE B  1  370 ? 27.429  -15.589 -8.068  1.00 57.49  ? 396  PHE B CD1 1 
ATOM   7749  C  CD2 . PHE B  1  370 ? 25.458  -16.891 -8.446  1.00 56.01  ? 396  PHE B CD2 1 
ATOM   7750  C  CE1 . PHE B  1  370 ? 26.666  -14.433 -8.040  1.00 56.11  ? 396  PHE B CE1 1 
ATOM   7751  C  CE2 . PHE B  1  370 ? 24.685  -15.743 -8.421  1.00 55.60  ? 396  PHE B CE2 1 
ATOM   7752  C  CZ  . PHE B  1  370 ? 25.289  -14.509 -8.217  1.00 56.01  ? 396  PHE B CZ  1 
ATOM   7753  N  N   . GLY B  1  371 ? 29.144  -20.200 -6.199  1.00 60.65  ? 397  GLY B N   1 
ATOM   7754  C  CA  . GLY B  1  371 ? 30.083  -21.299 -6.033  1.00 61.12  ? 397  GLY B CA  1 
ATOM   7755  C  C   . GLY B  1  371 ? 31.234  -21.262 -7.011  1.00 61.20  ? 397  GLY B C   1 
ATOM   7756  O  O   . GLY B  1  371 ? 31.922  -22.261 -7.220  1.00 60.74  ? 397  GLY B O   1 
ATOM   7757  N  N   . THR B  1  372 ? 31.453  -20.092 -7.594  1.00 61.64  ? 398  THR B N   1 
ATOM   7758  C  CA  . THR B  1  372 ? 32.517  -19.923 -8.557  1.00 62.73  ? 398  THR B CA  1 
ATOM   7759  C  C   . THR B  1  372 ? 33.363  -18.695 -8.252  1.00 64.79  ? 398  THR B C   1 
ATOM   7760  O  O   . THR B  1  372 ? 32.956  -17.816 -7.487  1.00 66.35  ? 398  THR B O   1 
ATOM   7761  C  CB  . THR B  1  372 ? 31.950  -19.750 -9.960  1.00 61.58  ? 398  THR B CB  1 
ATOM   7762  O  OG1 . THR B  1  372 ? 33.026  -19.738 -10.900 1.00 63.29  ? 398  THR B OG1 1 
ATOM   7763  C  CG2 . THR B  1  372 ? 31.184  -18.441 -10.062 1.00 60.34  ? 398  THR B CG2 1 
ATOM   7764  N  N   . THR B  1  373 ? 34.543  -18.641 -8.866  1.00 65.12  ? 399  THR B N   1 
ATOM   7765  C  CA  . THR B  1  373 ? 35.463  -17.511 -8.718  1.00 64.89  ? 399  THR B CA  1 
ATOM   7766  C  C   . THR B  1  373 ? 36.031  -17.178 -10.085 1.00 63.77  ? 399  THR B C   1 
ATOM   7767  O  O   . THR B  1  373 ? 37.114  -16.607 -10.194 1.00 64.90  ? 399  THR B O   1 
ATOM   7768  C  CB  . THR B  1  373 ? 36.640  -17.838 -7.799  1.00 64.83  ? 399  THR B CB  1 
ATOM   7769  O  OG1 . THR B  1  373 ? 37.225  -19.083 -8.203  1.00 66.38  ? 399  THR B OG1 1 
ATOM   7770  C  CG2 . THR B  1  373 ? 36.177  -17.909 -6.361  1.00 65.33  ? 399  THR B CG2 1 
ATOM   7771  N  N   . SER B  1  374 ? 35.289  -17.542 -11.125 1.00 61.40  ? 400  SER B N   1 
ATOM   7772  C  CA  . SER B  1  374 ? 35.725  -17.294 -12.479 1.00 59.29  ? 400  SER B CA  1 
ATOM   7773  C  C   . SER B  1  374 ? 34.666  -16.511 -13.217 1.00 59.40  ? 400  SER B C   1 
ATOM   7774  O  O   . SER B  1  374 ? 34.832  -16.213 -14.400 1.00 61.07  ? 400  SER B O   1 
ATOM   7775  C  CB  . SER B  1  374 ? 35.956  -18.612 -13.191 1.00 58.61  ? 400  SER B CB  1 
ATOM   7776  O  OG  . SER B  1  374 ? 36.683  -19.487 -12.358 1.00 59.59  ? 400  SER B OG  1 
ATOM   7777  N  N   . LEU B  1  375 ? 33.575  -16.189 -12.526 1.00 57.40  ? 401  LEU B N   1 
ATOM   7778  C  CA  . LEU B  1  375 ? 32.497  -15.438 -13.144 1.00 56.52  ? 401  LEU B CA  1 
ATOM   7779  C  C   . LEU B  1  375 ? 33.061  -14.196 -13.819 1.00 55.58  ? 401  LEU B C   1 
ATOM   7780  O  O   . LEU B  1  375 ? 33.772  -13.433 -13.183 1.00 55.79  ? 401  LEU B O   1 
ATOM   7781  C  CB  . LEU B  1  375 ? 31.468  -15.006 -12.093 1.00 57.59  ? 401  LEU B CB  1 
ATOM   7782  C  CG  . LEU B  1  375 ? 29.981  -15.395 -12.223 1.00 59.30  ? 401  LEU B CG  1 
ATOM   7783  C  CD1 . LEU B  1  375 ? 29.121  -14.220 -11.784 1.00 58.17  ? 401  LEU B CD1 1 
ATOM   7784  C  CD2 . LEU B  1  375 ? 29.627  -15.780 -13.655 1.00 58.60  ? 401  LEU B CD2 1 
ATOM   7785  N  N   . LYS B  1  376 ? 32.760  -14.016 -15.105 1.00 54.53  ? 402  LYS B N   1 
ATOM   7786  C  CA  . LYS B  1  376 ? 33.197  -12.842 -15.858 1.00 54.46  ? 402  LYS B CA  1 
ATOM   7787  C  C   . LYS B  1  376 ? 31.985  -12.012 -16.287 1.00 53.73  ? 402  LYS B C   1 
ATOM   7788  O  O   . LYS B  1  376 ? 32.076  -10.788 -16.458 1.00 53.61  ? 402  LYS B O   1 
ATOM   7789  C  CB  . LYS B  1  376 ? 33.954  -13.238 -17.112 1.00 55.78  ? 402  LYS B CB  1 
ATOM   7790  C  CG  . LYS B  1  376 ? 35.313  -13.782 -16.878 1.00 60.88  ? 402  LYS B CG  1 
ATOM   7791  C  CD  . LYS B  1  376 ? 35.996  -14.080 -18.209 1.00 66.55  ? 402  LYS B CD  1 
ATOM   7792  C  CE  . LYS B  1  376 ? 37.373  -14.690 -17.959 1.00 71.13  ? 402  LYS B CE  1 
ATOM   7793  N  NZ  . LYS B  1  376 ? 37.268  -15.832 -16.981 1.00 73.52  ? 402  LYS B NZ  1 
ATOM   7794  N  N   . TYR B  1  377 ? 30.850  -12.688 -16.445 1.00 51.76  ? 403  TYR B N   1 
ATOM   7795  C  CA  . TYR B  1  377 ? 29.611  -12.044 -16.877 1.00 50.33  ? 403  TYR B CA  1 
ATOM   7796  C  C   . TYR B  1  377 ? 28.489  -12.392 -15.892 1.00 49.64  ? 403  TYR B C   1 
ATOM   7797  O  O   . TYR B  1  377 ? 28.338  -13.549 -15.517 1.00 51.20  ? 403  TYR B O   1 
ATOM   7798  C  CB  . TYR B  1  377 ? 29.300  -12.545 -18.283 1.00 49.36  ? 403  TYR B CB  1 
ATOM   7799  C  CG  . TYR B  1  377 ? 28.079  -11.990 -18.944 1.00 48.24  ? 403  TYR B CG  1 
ATOM   7800  C  CD1 . TYR B  1  377 ? 28.183  -11.242 -20.101 1.00 47.20  ? 403  TYR B CD1 1 
ATOM   7801  C  CD2 . TYR B  1  377 ? 26.815  -12.288 -18.470 1.00 49.23  ? 403  TYR B CD2 1 
ATOM   7802  C  CE1 . TYR B  1  377 ? 27.062  -10.812 -20.776 1.00 47.15  ? 403  TYR B CE1 1 
ATOM   7803  C  CE2 . TYR B  1  377 ? 25.688  -11.859 -19.140 1.00 50.01  ? 403  TYR B CE2 1 
ATOM   7804  C  CZ  . TYR B  1  377 ? 25.819  -11.125 -20.291 1.00 48.28  ? 403  TYR B CZ  1 
ATOM   7805  O  OH  . TYR B  1  377 ? 24.690  -10.727 -20.953 1.00 50.67  ? 403  TYR B OH  1 
ATOM   7806  N  N   . LEU B  1  378 ? 27.724  -11.392 -15.456 1.00 47.80  ? 404  LEU B N   1 
ATOM   7807  C  CA  . LEU B  1  378 ? 26.631  -11.606 -14.511 1.00 45.31  ? 404  LEU B CA  1 
ATOM   7808  C  C   . LEU B  1  378 ? 25.465  -10.675 -14.828 1.00 46.65  ? 404  LEU B C   1 
ATOM   7809  O  O   . LEU B  1  378 ? 25.568  -9.462  -14.677 1.00 47.51  ? 404  LEU B O   1 
ATOM   7810  C  CB  . LEU B  1  378 ? 27.111  -11.365 -13.090 1.00 43.06  ? 404  LEU B CB  1 
ATOM   7811  C  CG  . LEU B  1  378 ? 26.041  -11.397 -12.008 1.00 44.09  ? 404  LEU B CG  1 
ATOM   7812  C  CD1 . LEU B  1  378 ? 25.343  -12.732 -11.982 1.00 45.35  ? 404  LEU B CD1 1 
ATOM   7813  C  CD2 . LEU B  1  378 ? 26.687  -11.127 -10.680 1.00 44.58  ? 404  LEU B CD2 1 
ATOM   7814  N  N   . ASP B  1  379 ? 24.350  -11.260 -15.260 1.00 47.52  ? 405  ASP B N   1 
ATOM   7815  C  CA  . ASP B  1  379 ? 23.156  -10.514 -15.641 1.00 45.70  ? 405  ASP B CA  1 
ATOM   7816  C  C   . ASP B  1  379 ? 21.972  -10.852 -14.744 1.00 44.29  ? 405  ASP B C   1 
ATOM   7817  O  O   . ASP B  1  379 ? 21.328  -11.866 -14.927 1.00 46.16  ? 405  ASP B O   1 
ATOM   7818  C  CB  . ASP B  1  379 ? 22.825  -10.854 -17.099 1.00 48.03  ? 405  ASP B CB  1 
ATOM   7819  C  CG  . ASP B  1  379 ? 21.670  -10.038 -17.664 1.00 52.40  ? 405  ASP B CG  1 
ATOM   7820  O  OD1 . ASP B  1  379 ? 21.473  -10.078 -18.910 1.00 52.99  ? 405  ASP B OD1 1 
ATOM   7821  O  OD2 . ASP B  1  379 ? 20.956  -9.368  -16.878 1.00 53.21  ? 405  ASP B OD2 1 
ATOM   7822  N  N   . LEU B  1  380 ? 21.691  -10.001 -13.772 1.00 42.84  ? 406  LEU B N   1 
ATOM   7823  C  CA  . LEU B  1  380 ? 20.568  -10.200 -12.871 1.00 42.75  ? 406  LEU B CA  1 
ATOM   7824  C  C   . LEU B  1  380 ? 19.525  -9.128  -13.109 1.00 42.99  ? 406  LEU B C   1 
ATOM   7825  O  O   . LEU B  1  380 ? 18.887  -8.676  -12.163 1.00 44.53  ? 406  LEU B O   1 
ATOM   7826  C  CB  . LEU B  1  380 ? 21.012  -10.088 -11.426 1.00 42.19  ? 406  LEU B CB  1 
ATOM   7827  C  CG  . LEU B  1  380 ? 22.012  -11.115 -10.937 1.00 42.54  ? 406  LEU B CG  1 
ATOM   7828  C  CD1 . LEU B  1  380 ? 22.373  -10.753 -9.537  1.00 43.42  ? 406  LEU B CD1 1 
ATOM   7829  C  CD2 . LEU B  1  380 ? 21.426  -12.509 -10.990 1.00 44.56  ? 406  LEU B CD2 1 
ATOM   7830  N  N   . SER B  1  381 ? 19.344  -8.714  -14.356 1.00 42.84  ? 407  SER B N   1 
ATOM   7831  C  CA  . SER B  1  381 ? 18.381  -7.663  -14.640 1.00 43.65  ? 407  SER B CA  1 
ATOM   7832  C  C   . SER B  1  381 ? 16.957  -8.175  -14.690 1.00 44.34  ? 407  SER B C   1 
ATOM   7833  O  O   . SER B  1  381 ? 16.728  -9.366  -14.864 1.00 46.21  ? 407  SER B O   1 
ATOM   7834  C  CB  . SER B  1  381 ? 18.727  -6.974  -15.962 1.00 43.80  ? 407  SER B CB  1 
ATOM   7835  O  OG  . SER B  1  381 ? 18.729  -7.898  -17.034 1.00 45.48  ? 407  SER B OG  1 
ATOM   7836  N  N   . PHE B  1  382 ? 16.002  -7.263  -14.537 1.00 44.58  ? 408  PHE B N   1 
ATOM   7837  C  CA  . PHE B  1  382 ? 14.571  -7.581  -14.574 1.00 44.24  ? 408  PHE B CA  1 
ATOM   7838  C  C   . PHE B  1  382 ? 14.148  -8.634  -13.586 1.00 43.68  ? 408  PHE B C   1 
ATOM   7839  O  O   . PHE B  1  382 ? 13.627  -9.667  -13.975 1.00 43.22  ? 408  PHE B O   1 
ATOM   7840  C  CB  . PHE B  1  382 ? 14.144  -8.044  -15.963 1.00 45.17  ? 408  PHE B CB  1 
ATOM   7841  C  CG  . PHE B  1  382 ? 14.427  -7.049  -17.039 1.00 46.73  ? 408  PHE B CG  1 
ATOM   7842  C  CD1 . PHE B  1  382 ? 15.691  -6.980  -17.630 1.00 45.91  ? 408  PHE B CD1 1 
ATOM   7843  C  CD2 . PHE B  1  382 ? 13.431  -6.166  -17.459 1.00 46.69  ? 408  PHE B CD2 1 
ATOM   7844  C  CE1 . PHE B  1  382 ? 15.961  -6.043  -18.628 1.00 47.23  ? 408  PHE B CE1 1 
ATOM   7845  C  CE2 . PHE B  1  382 ? 13.683  -5.223  -18.456 1.00 46.92  ? 408  PHE B CE2 1 
ATOM   7846  C  CZ  . PHE B  1  382 ? 14.952  -5.157  -19.047 1.00 46.77  ? 408  PHE B CZ  1 
ATOM   7847  N  N   . ASN B  1  383 ? 14.384  -8.369  -12.313 1.00 42.49  ? 409  ASN B N   1 
ATOM   7848  C  CA  . ASN B  1  383 ? 14.006  -9.281  -11.266 1.00 41.82  ? 409  ASN B CA  1 
ATOM   7849  C  C   . ASN B  1  383 ? 13.372  -8.459  -10.175 1.00 43.22  ? 409  ASN B C   1 
ATOM   7850  O  O   . ASN B  1  383 ? 13.076  -7.292  -10.376 1.00 45.98  ? 409  ASN B O   1 
ATOM   7851  C  CB  . ASN B  1  383 ? 15.227  -10.012 -10.747 1.00 43.73  ? 409  ASN B CB  1 
ATOM   7852  C  CG  . ASN B  1  383 ? 15.758  -11.041 -11.741 1.00 47.07  ? 409  ASN B CG  1 
ATOM   7853  O  OD1 . ASN B  1  383 ? 15.042  -11.969 -12.136 1.00 49.65  ? 409  ASN B OD1 1 
ATOM   7854  N  ND2 . ASN B  1  383 ? 17.020  -10.888 -12.142 1.00 45.94  ? 409  ASN B ND2 1 
ATOM   7855  N  N   . GLY B  1  384 ? 13.147  -9.059  -9.018  1.00 44.06  ? 410  GLY B N   1 
ATOM   7856  C  CA  . GLY B  1  384 ? 12.519  -8.327  -7.932  1.00 44.71  ? 410  GLY B CA  1 
ATOM   7857  C  C   . GLY B  1  384 ? 13.530  -7.547  -7.124  1.00 45.43  ? 410  GLY B C   1 
ATOM   7858  O  O   . GLY B  1  384 ? 14.331  -6.799  -7.668  1.00 47.49  ? 410  GLY B O   1 
ATOM   7859  N  N   . VAL B  1  385 ? 13.515  -7.730  -5.817  1.00 44.14  ? 411  VAL B N   1 
ATOM   7860  C  CA  . VAL B  1  385 ? 14.437  -7.017  -4.976  1.00 44.30  ? 411  VAL B CA  1 
ATOM   7861  C  C   . VAL B  1  385 ? 15.765  -7.737  -4.868  1.00 45.34  ? 411  VAL B C   1 
ATOM   7862  O  O   . VAL B  1  385 ? 15.790  -8.960  -4.797  1.00 45.83  ? 411  VAL B O   1 
ATOM   7863  C  CB  . VAL B  1  385 ? 13.854  -6.867  -3.582  1.00 44.20  ? 411  VAL B CB  1 
ATOM   7864  C  CG1 . VAL B  1  385 ? 14.887  -6.289  -2.648  1.00 44.61  ? 411  VAL B CG1 1 
ATOM   7865  C  CG2 . VAL B  1  385 ? 12.634  -5.980  -3.643  1.00 46.01  ? 411  VAL B CG2 1 
ATOM   7866  N  N   . ILE B  1  386 ? 16.861  -6.972  -4.871  1.00 45.21  ? 412  ILE B N   1 
ATOM   7867  C  CA  . ILE B  1  386 ? 18.217  -7.511  -4.716  1.00 44.10  ? 412  ILE B CA  1 
ATOM   7868  C  C   . ILE B  1  386 ? 18.920  -6.704  -3.635  1.00 44.26  ? 412  ILE B C   1 
ATOM   7869  O  O   . ILE B  1  386 ? 19.398  -5.612  -3.883  1.00 46.58  ? 412  ILE B O   1 
ATOM   7870  C  CB  . ILE B  1  386 ? 19.054  -7.403  -6.007  1.00 42.76  ? 412  ILE B CB  1 
ATOM   7871  C  CG1 . ILE B  1  386 ? 18.391  -8.194  -7.129  1.00 45.03  ? 412  ILE B CG1 1 
ATOM   7872  C  CG2 . ILE B  1  386 ? 20.454  -7.951  -5.778  1.00 40.92  ? 412  ILE B CG2 1 
ATOM   7873  C  CD1 . ILE B  1  386 ? 19.203  -8.205  -8.426  1.00 45.54  ? 412  ILE B CD1 1 
ATOM   7874  N  N   . THR B  1  387 ? 18.982  -7.251  -2.433  1.00 44.70  ? 413  THR B N   1 
ATOM   7875  C  CA  . THR B  1  387 ? 19.622  -6.581  -1.309  1.00 45.72  ? 413  THR B CA  1 
ATOM   7876  C  C   . THR B  1  387 ? 21.147  -6.731  -1.337  1.00 47.78  ? 413  THR B C   1 
ATOM   7877  O  O   . THR B  1  387 ? 21.653  -7.848  -1.363  1.00 49.33  ? 413  THR B O   1 
ATOM   7878  C  CB  . THR B  1  387 ? 19.089  -7.160  0.003   1.00 44.04  ? 413  THR B CB  1 
ATOM   7879  O  OG1 . THR B  1  387 ? 17.660  -7.150  -0.044  1.00 43.34  ? 413  THR B OG1 1 
ATOM   7880  C  CG2 . THR B  1  387 ? 19.564  -6.348  1.197   1.00 43.14  ? 413  THR B CG2 1 
ATOM   7881  N  N   . MET B  1  388 ? 21.877  -5.612  -1.326  1.00 48.53  ? 414  MET B N   1 
ATOM   7882  C  CA  . MET B  1  388 ? 23.343  -5.647  -1.334  1.00 48.17  ? 414  MET B CA  1 
ATOM   7883  C  C   . MET B  1  388 ? 23.908  -5.747  0.078   1.00 48.10  ? 414  MET B C   1 
ATOM   7884  O  O   . MET B  1  388 ? 23.616  -4.907  0.944   1.00 47.65  ? 414  MET B O   1 
ATOM   7885  C  CB  . MET B  1  388 ? 23.889  -4.400  -2.008  1.00 48.70  ? 414  MET B CB  1 
ATOM   7886  C  CG  . MET B  1  388 ? 23.423  -4.219  -3.435  1.00 52.57  ? 414  MET B CG  1 
ATOM   7887  S  SD  . MET B  1  388 ? 23.851  -5.605  -4.502  1.00 58.03  ? 414  MET B SD  1 
ATOM   7888  C  CE  . MET B  1  388 ? 25.662  -5.705  -4.237  1.00 53.12  ? 414  MET B CE  1 
ATOM   7889  N  N   . SER B  1  389 ? 24.722  -6.771  0.312   1.00 47.12  ? 415  SER B N   1 
ATOM   7890  C  CA  . SER B  1  389 ? 25.284  -6.965  1.631   1.00 48.50  ? 415  SER B CA  1 
ATOM   7891  C  C   . SER B  1  389 ? 26.686  -7.506  1.600   1.00 49.22  ? 415  SER B C   1 
ATOM   7892  O  O   . SER B  1  389 ? 27.262  -7.791  2.647   1.00 50.17  ? 415  SER B O   1 
ATOM   7893  C  CB  . SER B  1  389 ? 24.403  -7.904  2.438   1.00 49.98  ? 415  SER B CB  1 
ATOM   7894  O  OG  . SER B  1  389 ? 24.124  -9.084  1.710   1.00 51.50  ? 415  SER B OG  1 
ATOM   7895  N  N   . SER B  1  390 ? 27.231  -7.663  0.400   1.00 49.83  ? 416  SER B N   1 
ATOM   7896  C  CA  . SER B  1  390 ? 28.598  -8.152  0.220   1.00 51.38  ? 416  SER B CA  1 
ATOM   7897  C  C   . SER B  1  390 ? 29.146  -7.568  -1.080  1.00 52.71  ? 416  SER B C   1 
ATOM   7898  O  O   . SER B  1  390 ? 28.522  -7.710  -2.137  1.00 53.06  ? 416  SER B O   1 
ATOM   7899  C  CB  . SER B  1  390 ? 28.621  -9.679  0.166   1.00 51.14  ? 416  SER B CB  1 
ATOM   7900  O  OG  . SER B  1  390 ? 29.955  -10.162 0.106   1.00 52.03  ? 416  SER B OG  1 
ATOM   7901  N  N   . ASN B  1  391 ? 30.301  -6.909  -1.018  1.00 54.45  ? 417  ASN B N   1 
ATOM   7902  C  CA  . ASN B  1  391 ? 30.863  -6.290  -2.221  1.00 56.00  ? 417  ASN B CA  1 
ATOM   7903  C  C   . ASN B  1  391 ? 31.674  -7.222  -3.123  1.00 56.21  ? 417  ASN B C   1 
ATOM   7904  O  O   . ASN B  1  391 ? 32.865  -7.010  -3.373  1.00 56.84  ? 417  ASN B O   1 
ATOM   7905  C  CB  . ASN B  1  391 ? 31.687  -5.046  -1.856  1.00 56.40  ? 417  ASN B CB  1 
ATOM   7906  C  CG  . ASN B  1  391 ? 32.368  -5.178  -0.526  1.00 58.18  ? 417  ASN B CG  1 
ATOM   7907  O  OD1 . ASN B  1  391 ? 32.708  -6.281  -0.094  1.00 61.22  ? 417  ASN B OD1 1 
ATOM   7908  N  ND2 . ASN B  1  391 ? 32.591  -4.054  0.134   1.00 59.53  ? 417  ASN B ND2 1 
ATOM   7909  N  N   . PHE B  1  392 ? 31.000  -8.256  -3.612  1.00 54.52  ? 418  PHE B N   1 
ATOM   7910  C  CA  . PHE B  1  392 ? 31.585  -9.223  -4.519  1.00 52.57  ? 418  PHE B CA  1 
ATOM   7911  C  C   . PHE B  1  392 ? 32.872  -9.931  -4.105  1.00 53.80  ? 418  PHE B C   1 
ATOM   7912  O  O   . PHE B  1  392 ? 33.762  -10.114 -4.933  1.00 53.11  ? 418  PHE B O   1 
ATOM   7913  C  CB  . PHE B  1  392 ? 31.788  -8.564  -5.877  1.00 49.92  ? 418  PHE B CB  1 
ATOM   7914  C  CG  . PHE B  1  392 ? 30.524  -8.033  -6.482  1.00 47.92  ? 418  PHE B CG  1 
ATOM   7915  C  CD1 . PHE B  1  392 ? 29.959  -6.848  -6.024  1.00 47.09  ? 418  PHE B CD1 1 
ATOM   7916  C  CD2 . PHE B  1  392 ? 29.897  -8.717  -7.511  1.00 46.64  ? 418  PHE B CD2 1 
ATOM   7917  C  CE1 . PHE B  1  392 ? 28.781  -6.354  -6.584  1.00 46.17  ? 418  PHE B CE1 1 
ATOM   7918  C  CE2 . PHE B  1  392 ? 28.725  -8.238  -8.078  1.00 45.45  ? 418  PHE B CE2 1 
ATOM   7919  C  CZ  . PHE B  1  392 ? 28.164  -7.050  -7.616  1.00 45.39  ? 418  PHE B CZ  1 
ATOM   7920  N  N   . LEU B  1  393 ? 32.971  -10.346 -2.844  1.00 54.60  ? 419  LEU B N   1 
ATOM   7921  C  CA  . LEU B  1  393 ? 34.168  -11.051 -2.397  1.00 55.95  ? 419  LEU B CA  1 
ATOM   7922  C  C   . LEU B  1  393 ? 34.268  -12.342 -3.173  1.00 56.37  ? 419  LEU B C   1 
ATOM   7923  O  O   . LEU B  1  393 ? 33.407  -13.193 -3.039  1.00 57.44  ? 419  LEU B O   1 
ATOM   7924  C  CB  . LEU B  1  393 ? 34.084  -11.400 -0.913  1.00 56.80  ? 419  LEU B CB  1 
ATOM   7925  C  CG  . LEU B  1  393 ? 33.814  -10.303 0.118   1.00 58.83  ? 419  LEU B CG  1 
ATOM   7926  C  CD1 . LEU B  1  393 ? 34.151  -10.852 1.516   1.00 57.00  ? 419  LEU B CD1 1 
ATOM   7927  C  CD2 . LEU B  1  393 ? 34.650  -9.058  -0.188  1.00 59.49  ? 419  LEU B CD2 1 
ATOM   7928  N  N   . GLY B  1  394 ? 35.307  -12.493 -3.983  1.00 57.64  ? 420  GLY B N   1 
ATOM   7929  C  CA  . GLY B  1  394 ? 35.464  -13.721 -4.736  1.00 59.10  ? 420  GLY B CA  1 
ATOM   7930  C  C   . GLY B  1  394 ? 35.030  -13.638 -6.185  1.00 61.30  ? 420  GLY B C   1 
ATOM   7931  O  O   . GLY B  1  394 ? 35.157  -14.613 -6.922  1.00 62.97  ? 420  GLY B O   1 
ATOM   7932  N  N   . LEU B  1  395 ? 34.520  -12.485 -6.605  1.00 62.30  ? 421  LEU B N   1 
ATOM   7933  C  CA  . LEU B  1  395 ? 34.075  -12.305 -7.983  1.00 63.35  ? 421  LEU B CA  1 
ATOM   7934  C  C   . LEU B  1  395 ? 34.861  -11.160 -8.593  1.00 65.04  ? 421  LEU B C   1 
ATOM   7935  O  O   . LEU B  1  395 ? 34.310  -10.339 -9.332  1.00 65.53  ? 421  LEU B O   1 
ATOM   7936  C  CB  . LEU B  1  395 ? 32.582  -11.981 -8.021  1.00 62.86  ? 421  LEU B CB  1 
ATOM   7937  C  CG  . LEU B  1  395 ? 31.669  -12.952 -7.267  1.00 62.97  ? 421  LEU B CG  1 
ATOM   7938  C  CD1 . LEU B  1  395 ? 30.266  -12.398 -7.251  1.00 63.12  ? 421  LEU B CD1 1 
ATOM   7939  C  CD2 . LEU B  1  395 ? 31.699  -14.326 -7.923  1.00 62.97  ? 421  LEU B CD2 1 
ATOM   7940  N  N   . GLU B  1  396 ? 36.151  -11.119 -8.264  1.00 66.79  ? 422  GLU B N   1 
ATOM   7941  C  CA  . GLU B  1  396 ? 37.067  -10.083 -8.729  1.00 68.57  ? 422  GLU B CA  1 
ATOM   7942  C  C   . GLU B  1  396 ? 37.145  -9.932  -10.247 1.00 68.96  ? 422  GLU B C   1 
ATOM   7943  O  O   . GLU B  1  396 ? 37.336  -8.825  -10.768 1.00 69.57  ? 422  GLU B O   1 
ATOM   7944  C  CB  . GLU B  1  396 ? 38.466  -10.360 -8.187  1.00 70.24  ? 422  GLU B CB  1 
ATOM   7945  C  CG  . GLU B  1  396 ? 38.682  -10.050 -6.698  1.00 75.25  ? 422  GLU B CG  1 
ATOM   7946  C  CD  . GLU B  1  396 ? 38.064  -11.068 -5.742  1.00 77.53  ? 422  GLU B CD  1 
ATOM   7947  O  OE1 . GLU B  1  396 ? 38.236  -12.288 -5.974  1.00 77.08  ? 422  GLU B OE1 1 
ATOM   7948  O  OE2 . GLU B  1  396 ? 37.431  -10.638 -4.741  1.00 78.09  ? 422  GLU B OE2 1 
ATOM   7949  N  N   . GLN B  1  397 ? 36.971  -11.041 -10.954 1.00 68.36  ? 423  GLN B N   1 
ATOM   7950  C  CA  . GLN B  1  397 ? 37.067  -11.040 -12.401 1.00 67.32  ? 423  GLN B CA  1 
ATOM   7951  C  C   . GLN B  1  397 ? 35.854  -10.582 -13.197 1.00 65.20  ? 423  GLN B C   1 
ATOM   7952  O  O   . GLN B  1  397 ? 35.856  -10.643 -14.419 1.00 64.46  ? 423  GLN B O   1 
ATOM   7953  C  CB  . GLN B  1  397 ? 37.490  -12.426 -12.853 1.00 69.90  ? 423  GLN B CB  1 
ATOM   7954  C  CG  . GLN B  1  397 ? 38.765  -12.882 -12.183 1.00 74.88  ? 423  GLN B CG  1 
ATOM   7955  C  CD  . GLN B  1  397 ? 39.302  -14.141 -12.807 1.00 79.65  ? 423  GLN B CD  1 
ATOM   7956  O  OE1 . GLN B  1  397 ? 39.533  -14.195 -14.021 1.00 82.29  ? 423  GLN B OE1 1 
ATOM   7957  N  NE2 . GLN B  1  397 ? 39.510  -15.169 -11.986 1.00 81.53  ? 423  GLN B NE2 1 
ATOM   7958  N  N   . LEU B  1  398 ? 34.822  -10.108 -12.524 1.00 64.12  ? 424  LEU B N   1 
ATOM   7959  C  CA  . LEU B  1  398 ? 33.636  -9.672  -13.242 1.00 64.46  ? 424  LEU B CA  1 
ATOM   7960  C  C   . LEU B  1  398 ? 33.932  -8.546  -14.201 1.00 65.21  ? 424  LEU B C   1 
ATOM   7961  O  O   . LEU B  1  398 ? 34.353  -7.480  -13.764 1.00 66.71  ? 424  LEU B O   1 
ATOM   7962  C  CB  . LEU B  1  398 ? 32.563  -9.179  -12.281 1.00 64.49  ? 424  LEU B CB  1 
ATOM   7963  C  CG  . LEU B  1  398 ? 31.404  -10.088 -11.898 1.00 64.39  ? 424  LEU B CG  1 
ATOM   7964  C  CD1 . LEU B  1  398 ? 30.363  -9.243  -11.174 1.00 64.77  ? 424  LEU B CD1 1 
ATOM   7965  C  CD2 . LEU B  1  398 ? 30.797  -10.717 -13.133 1.00 62.37  ? 424  LEU B CD2 1 
ATOM   7966  N  N   . GLU B  1  399 ? 33.698  -8.768  -15.496 1.00 65.66  ? 425  GLU B N   1 
ATOM   7967  C  CA  . GLU B  1  399 ? 33.909  -7.727  -16.502 1.00 65.58  ? 425  GLU B CA  1 
ATOM   7968  C  C   . GLU B  1  399 ? 32.561  -7.097  -16.900 1.00 64.65  ? 425  GLU B C   1 
ATOM   7969  O  O   . GLU B  1  399 ? 32.496  -5.919  -17.249 1.00 65.43  ? 425  GLU B O   1 
ATOM   7970  C  CB  . GLU B  1  399 ? 34.579  -8.310  -17.745 1.00 68.06  ? 425  GLU B CB  1 
ATOM   7971  C  CG  . GLU B  1  399 ? 35.870  -9.079  -17.466 1.00 73.16  ? 425  GLU B CG  1 
ATOM   7972  C  CD  . GLU B  1  399 ? 36.529  -9.633  -18.747 1.00 76.04  ? 425  GLU B CD  1 
ATOM   7973  O  OE1 . GLU B  1  399 ? 37.463  -10.471 -18.629 1.00 76.56  ? 425  GLU B OE1 1 
ATOM   7974  O  OE2 . GLU B  1  399 ? 36.115  -9.232  -19.867 1.00 75.87  ? 425  GLU B OE2 1 
ATOM   7975  N  N   . HIS B  1  400 ? 31.488  -7.881  -16.824 1.00 61.77  ? 426  HIS B N   1 
ATOM   7976  C  CA  . HIS B  1  400 ? 30.151  -7.420  -17.188 1.00 58.92  ? 426  HIS B CA  1 
ATOM   7977  C  C   . HIS B  1  400 ? 29.168  -7.688  -16.031 1.00 57.79  ? 426  HIS B C   1 
ATOM   7978  O  O   . HIS B  1  400 ? 29.168  -8.773  -15.462 1.00 59.38  ? 426  HIS B O   1 
ATOM   7979  C  CB  . HIS B  1  400 ? 29.723  -8.167  -18.447 1.00 58.45  ? 426  HIS B CB  1 
ATOM   7980  C  CG  . HIS B  1  400 ? 28.472  -7.643  -19.079 1.00 59.92  ? 426  HIS B CG  1 
ATOM   7981  N  ND1 . HIS B  1  400 ? 27.235  -7.743  -18.480 1.00 60.91  ? 426  HIS B ND1 1 
ATOM   7982  C  CD2 . HIS B  1  400 ? 28.263  -7.048  -20.277 1.00 60.02  ? 426  HIS B CD2 1 
ATOM   7983  C  CE1 . HIS B  1  400 ? 26.316  -7.237  -19.284 1.00 60.12  ? 426  HIS B CE1 1 
ATOM   7984  N  NE2 . HIS B  1  400 ? 26.914  -6.810  -20.381 1.00 60.52  ? 426  HIS B NE2 1 
ATOM   7985  N  N   . LEU B  1  401 ? 28.337  -6.705  -15.689 1.00 54.08  ? 427  LEU B N   1 
ATOM   7986  C  CA  . LEU B  1  401 ? 27.365  -6.830  -14.597 1.00 49.89  ? 427  LEU B CA  1 
ATOM   7987  C  C   . LEU B  1  401 ? 26.151  -5.939  -14.890 1.00 50.91  ? 427  LEU B C   1 
ATOM   7988  O  O   . LEU B  1  401 ? 26.269  -4.720  -14.949 1.00 52.12  ? 427  LEU B O   1 
ATOM   7989  C  CB  . LEU B  1  401 ? 28.028  -6.427  -13.276 1.00 46.48  ? 427  LEU B CB  1 
ATOM   7990  C  CG  . LEU B  1  401 ? 27.219  -6.199  -12.001 1.00 43.14  ? 427  LEU B CG  1 
ATOM   7991  C  CD1 . LEU B  1  401 ? 26.440  -7.421  -11.648 1.00 43.44  ? 427  LEU B CD1 1 
ATOM   7992  C  CD2 . LEU B  1  401 ? 28.158  -5.875  -10.889 1.00 40.30  ? 427  LEU B CD2 1 
ATOM   7993  N  N   . ASP B  1  402 ? 24.981  -6.554  -15.054 1.00 51.28  ? 428  ASP B N   1 
ATOM   7994  C  CA  . ASP B  1  402 ? 23.750  -5.837  -15.398 1.00 50.49  ? 428  ASP B CA  1 
ATOM   7995  C  C   . ASP B  1  402 ? 22.595  -6.021  -14.410 1.00 49.75  ? 428  ASP B C   1 
ATOM   7996  O  O   . ASP B  1  402 ? 21.929  -7.034  -14.430 1.00 51.17  ? 428  ASP B O   1 
ATOM   7997  C  CB  . ASP B  1  402 ? 23.311  -6.302  -16.794 1.00 52.86  ? 428  ASP B CB  1 
ATOM   7998  C  CG  . ASP B  1  402 ? 22.170  -5.482  -17.371 1.00 55.88  ? 428  ASP B CG  1 
ATOM   7999  O  OD1 . ASP B  1  402 ? 21.570  -4.671  -16.627 1.00 57.59  ? 428  ASP B OD1 1 
ATOM   8000  O  OD2 . ASP B  1  402 ? 21.874  -5.661  -18.576 1.00 54.86  ? 428  ASP B OD2 1 
ATOM   8001  N  N   . PHE B  1  403 ? 22.346  -5.034  -13.558 1.00 50.00  ? 429  PHE B N   1 
ATOM   8002  C  CA  . PHE B  1  403 ? 21.257  -5.090  -12.577 1.00 49.42  ? 429  PHE B CA  1 
ATOM   8003  C  C   . PHE B  1  403 ? 20.023  -4.354  -13.072 1.00 49.74  ? 429  PHE B C   1 
ATOM   8004  O  O   . PHE B  1  403 ? 19.044  -4.207  -12.344 1.00 49.61  ? 429  PHE B O   1 
ATOM   8005  C  CB  . PHE B  1  403 ? 21.676  -4.433  -11.273 1.00 48.83  ? 429  PHE B CB  1 
ATOM   8006  C  CG  . PHE B  1  403 ? 22.560  -5.269  -10.432 1.00 50.93  ? 429  PHE B CG  1 
ATOM   8007  C  CD1 . PHE B  1  403 ? 23.808  -4.809  -10.055 1.00 53.23  ? 429  PHE B CD1 1 
ATOM   8008  C  CD2 . PHE B  1  403 ? 22.124  -6.488  -9.952  1.00 52.46  ? 429  PHE B CD2 1 
ATOM   8009  C  CE1 . PHE B  1  403 ? 24.614  -5.554  -9.196  1.00 54.85  ? 429  PHE B CE1 1 
ATOM   8010  C  CE2 . PHE B  1  403 ? 22.915  -7.241  -9.097  1.00 53.56  ? 429  PHE B CE2 1 
ATOM   8011  C  CZ  . PHE B  1  403 ? 24.164  -6.774  -8.712  1.00 53.59  ? 429  PHE B CZ  1 
ATOM   8012  N  N   . GLN B  1  404 ? 20.080  -3.882  -14.306 1.00 49.88  ? 430  GLN B N   1 
ATOM   8013  C  CA  . GLN B  1  404 ? 18.988  -3.129  -14.903 1.00 51.04  ? 430  GLN B CA  1 
ATOM   8014  C  C   . GLN B  1  404 ? 17.558  -3.564  -14.554 1.00 51.63  ? 430  GLN B C   1 
ATOM   8015  O  O   . GLN B  1  404 ? 17.222  -4.741  -14.659 1.00 53.86  ? 430  GLN B O   1 
ATOM   8016  C  CB  . GLN B  1  404 ? 19.160  -3.161  -16.413 1.00 51.84  ? 430  GLN B CB  1 
ATOM   8017  C  CG  . GLN B  1  404 ? 18.050  -2.505  -17.178 1.00 53.49  ? 430  GLN B CG  1 
ATOM   8018  C  CD  . GLN B  1  404 ? 18.183  -2.743  -18.657 1.00 53.75  ? 430  GLN B CD  1 
ATOM   8019  O  OE1 . GLN B  1  404 ? 17.401  -2.224  -19.447 1.00 55.50  ? 430  GLN B OE1 1 
ATOM   8020  N  NE2 . GLN B  1  404 ? 19.177  -3.536  -19.044 1.00 51.99  ? 430  GLN B NE2 1 
ATOM   8021  N  N   . HIS B  1  405 ? 16.721  -2.605  -14.160 1.00 50.76  ? 431  HIS B N   1 
ATOM   8022  C  CA  . HIS B  1  405 ? 15.314  -2.850  -13.832 1.00 49.99  ? 431  HIS B CA  1 
ATOM   8023  C  C   . HIS B  1  405 ? 14.987  -3.769  -12.675 1.00 49.24  ? 431  HIS B C   1 
ATOM   8024  O  O   . HIS B  1  405 ? 13.917  -4.363  -12.633 1.00 49.69  ? 431  HIS B O   1 
ATOM   8025  C  CB  . HIS B  1  405 ? 14.579  -3.336  -15.067 1.00 50.02  ? 431  HIS B CB  1 
ATOM   8026  C  CG  . HIS B  1  405 ? 14.122  -2.227  -15.950 1.00 52.51  ? 431  HIS B CG  1 
ATOM   8027  N  ND1 . HIS B  1  405 ? 13.003  -1.475  -15.666 1.00 52.67  ? 431  HIS B ND1 1 
ATOM   8028  C  CD2 . HIS B  1  405 ? 14.661  -1.703  -17.075 1.00 51.91  ? 431  HIS B CD2 1 
ATOM   8029  C  CE1 . HIS B  1  405 ? 12.874  -0.532  -16.582 1.00 53.86  ? 431  HIS B CE1 1 
ATOM   8030  N  NE2 . HIS B  1  405 ? 13.867  -0.648  -17.446 1.00 53.80  ? 431  HIS B NE2 1 
ATOM   8031  N  N   . SER B  1  406 ? 15.903  -3.881  -11.731 1.00 48.35  ? 432  SER B N   1 
ATOM   8032  C  CA  . SER B  1  406 ? 15.673  -4.722  -10.578 1.00 49.17  ? 432  SER B CA  1 
ATOM   8033  C  C   . SER B  1  406 ? 15.789  -3.808  -9.382  1.00 50.66  ? 432  SER B C   1 
ATOM   8034  O  O   . SER B  1  406 ? 16.746  -3.057  -9.280  1.00 53.20  ? 432  SER B O   1 
ATOM   8035  C  CB  . SER B  1  406 ? 16.736  -5.820  -10.500 1.00 47.80  ? 432  SER B CB  1 
ATOM   8036  O  OG  . SER B  1  406 ? 16.653  -6.675  -11.629 1.00 46.32  ? 432  SER B OG  1 
ATOM   8037  N  N   . ASN B  1  407 ? 14.825  -3.851  -8.476  1.00 51.99  ? 433  ASN B N   1 
ATOM   8038  C  CA  . ASN B  1  407 ? 14.889  -2.997  -7.306  1.00 53.00  ? 433  ASN B CA  1 
ATOM   8039  C  C   . ASN B  1  407 ? 16.102  -3.370  -6.459  1.00 53.82  ? 433  ASN B C   1 
ATOM   8040  O  O   . ASN B  1  407 ? 16.119  -4.423  -5.825  1.00 54.17  ? 433  ASN B O   1 
ATOM   8041  C  CB  . ASN B  1  407 ? 13.606  -3.148  -6.498  1.00 55.05  ? 433  ASN B CB  1 
ATOM   8042  C  CG  . ASN B  1  407 ? 13.477  -2.108  -5.392  1.00 59.75  ? 433  ASN B CG  1 
ATOM   8043  O  OD1 . ASN B  1  407 ? 12.429  -2.016  -4.743  1.00 61.65  ? 433  ASN B OD1 1 
ATOM   8044  N  ND2 . ASN B  1  407 ? 14.536  -1.324  -5.165  1.00 60.86  ? 433  ASN B ND2 1 
ATOM   8045  N  N   . LEU B  1  408 ? 17.121  -2.511  -6.473  1.00 55.46  ? 434  LEU B N   1 
ATOM   8046  C  CA  . LEU B  1  408 ? 18.344  -2.711  -5.688  1.00 55.45  ? 434  LEU B CA  1 
ATOM   8047  C  C   . LEU B  1  408 ? 18.225  -1.935  -4.371  1.00 57.16  ? 434  LEU B C   1 
ATOM   8048  O  O   . LEU B  1  408 ? 17.684  -0.821  -4.340  1.00 58.30  ? 434  LEU B O   1 
ATOM   8049  C  CB  . LEU B  1  408 ? 19.558  -2.209  -6.456  1.00 55.85  ? 434  LEU B CB  1 
ATOM   8050  C  CG  . LEU B  1  408 ? 20.372  -3.256  -7.207  1.00 58.87  ? 434  LEU B CG  1 
ATOM   8051  C  CD1 . LEU B  1  408 ? 21.303  -2.597  -8.228  1.00 60.17  ? 434  LEU B CD1 1 
ATOM   8052  C  CD2 . LEU B  1  408 ? 21.183  -4.041  -6.202  1.00 60.46  ? 434  LEU B CD2 1 
ATOM   8053  N  N   . LYS B  1  409 ? 18.716  -2.525  -3.282  1.00 57.03  ? 435  LYS B N   1 
ATOM   8054  C  CA  . LYS B  1  409 ? 18.653  -1.894  -1.964  1.00 54.97  ? 435  LYS B CA  1 
ATOM   8055  C  C   . LYS B  1  409 ? 19.987  -1.931  -1.250  1.00 55.44  ? 435  LYS B C   1 
ATOM   8056  O  O   . LYS B  1  409 ? 20.769  -2.859  -1.430  1.00 54.56  ? 435  LYS B O   1 
ATOM   8057  C  CB  . LYS B  1  409 ? 17.609  -2.576  -1.090  1.00 52.73  ? 435  LYS B CB  1 
ATOM   8058  C  CG  . LYS B  1  409 ? 16.206  -2.454  -1.612  1.00 53.56  ? 435  LYS B CG  1 
ATOM   8059  C  CD  . LYS B  1  409 ? 15.198  -3.045  -0.653  1.00 54.01  ? 435  LYS B CD  1 
ATOM   8060  C  CE  . LYS B  1  409 ? 13.800  -2.880  -1.199  1.00 56.20  ? 435  LYS B CE  1 
ATOM   8061  N  NZ  . LYS B  1  409 ? 12.788  -3.457  -0.281  1.00 60.93  ? 435  LYS B NZ  1 
ATOM   8062  N  N   . GLN B  1  410 ? 20.231  -0.911  -0.431  1.00 57.42  ? 436  GLN B N   1 
ATOM   8063  C  CA  . GLN B  1  410 ? 21.473  -0.777  0.338   1.00 59.44  ? 436  GLN B CA  1 
ATOM   8064  C  C   . GLN B  1  410 ? 22.663  -0.349  -0.513  1.00 60.32  ? 436  GLN B C   1 
ATOM   8065  O  O   . GLN B  1  410 ? 23.801  -0.638  -0.176  1.00 59.49  ? 436  GLN B O   1 
ATOM   8066  C  CB  . GLN B  1  410 ? 21.800  -2.093  1.043   1.00 58.87  ? 436  GLN B CB  1 
ATOM   8067  C  CG  . GLN B  1  410 ? 20.570  -2.760  1.603   1.00 60.06  ? 436  GLN B CG  1 
ATOM   8068  C  CD  . GLN B  1  410 ? 20.826  -3.420  2.914   1.00 59.55  ? 436  GLN B CD  1 
ATOM   8069  O  OE1 . GLN B  1  410 ? 21.733  -4.248  3.035   1.00 60.62  ? 436  GLN B OE1 1 
ATOM   8070  N  NE2 . GLN B  1  410 ? 20.027  -3.068  3.919   1.00 59.66  ? 436  GLN B NE2 1 
ATOM   8071  N  N   . MET B  1  411 ? 22.384  0.356   -1.603  1.00 62.46  ? 437  MET B N   1 
ATOM   8072  C  CA  . MET B  1  411 ? 23.404  0.823   -2.532  1.00 64.75  ? 437  MET B CA  1 
ATOM   8073  C  C   . MET B  1  411 ? 24.395  1.803   -1.915  1.00 65.05  ? 437  MET B C   1 
ATOM   8074  O  O   . MET B  1  411 ? 25.614  1.672   -2.092  1.00 64.23  ? 437  MET B O   1 
ATOM   8075  C  CB  . MET B  1  411 ? 22.714  1.481   -3.729  1.00 68.54  ? 437  MET B CB  1 
ATOM   8076  C  CG  . MET B  1  411 ? 22.266  0.513   -4.808  1.00 72.41  ? 437  MET B CG  1 
ATOM   8077  S  SD  . MET B  1  411 ? 23.690  -0.118  -5.736  1.00 77.94  ? 437  MET B SD  1 
ATOM   8078  C  CE  . MET B  1  411 ? 23.746  1.073   -7.121  1.00 75.24  ? 437  MET B CE  1 
ATOM   8079  N  N   . SER B  1  412 ? 23.848  2.790   -1.203  1.00 65.46  ? 438  SER B N   1 
ATOM   8080  C  CA  . SER B  1  412 ? 24.620  3.853   -0.549  1.00 62.95  ? 438  SER B CA  1 
ATOM   8081  C  C   . SER B  1  412 ? 24.774  3.522   0.923   1.00 62.07  ? 438  SER B C   1 
ATOM   8082  O  O   . SER B  1  412 ? 24.474  4.336   1.778   1.00 63.10  ? 438  SER B O   1 
ATOM   8083  C  CB  . SER B  1  412 ? 23.872  5.188   -0.689  1.00 62.22  ? 438  SER B CB  1 
ATOM   8084  O  OG  . SER B  1  412 ? 23.280  5.335   -1.976  1.00 61.22  ? 438  SER B OG  1 
ATOM   8085  N  N   . GLU B  1  413 ? 25.250  2.326   1.220   1.00 60.92  ? 439  GLU B N   1 
ATOM   8086  C  CA  . GLU B  1  413 ? 25.384  1.904   2.598   1.00 60.27  ? 439  GLU B CA  1 
ATOM   8087  C  C   . GLU B  1  413 ? 26.803  1.446   2.848   1.00 60.42  ? 439  GLU B C   1 
ATOM   8088  O  O   . GLU B  1  413 ? 27.176  1.138   3.975   1.00 61.70  ? 439  GLU B O   1 
ATOM   8089  C  CB  . GLU B  1  413 ? 24.407  0.773   2.864   1.00 60.04  ? 439  GLU B CB  1 
ATOM   8090  C  CG  . GLU B  1  413 ? 23.837  0.757   4.245   1.00 63.97  ? 439  GLU B CG  1 
ATOM   8091  C  CD  . GLU B  1  413 ? 22.386  0.290   4.244   1.00 66.21  ? 439  GLU B CD  1 
ATOM   8092  O  OE1 . GLU B  1  413 ? 21.596  0.836   3.436   1.00 66.54  ? 439  GLU B OE1 1 
ATOM   8093  O  OE2 . GLU B  1  413 ? 22.030  -0.606  5.048   1.00 67.20  ? 439  GLU B OE2 1 
ATOM   8094  N  N   . PHE B  1  414 ? 27.572  1.388   1.767   1.00 59.81  ? 440  PHE B N   1 
ATOM   8095  C  CA  . PHE B  1  414 ? 28.985  1.006   1.770   1.00 60.18  ? 440  PHE B CA  1 
ATOM   8096  C  C   . PHE B  1  414 ? 29.393  0.901   0.298   1.00 60.51  ? 440  PHE B C   1 
ATOM   8097  O  O   . PHE B  1  414 ? 28.582  1.215   -0.582  1.00 61.12  ? 440  PHE B O   1 
ATOM   8098  C  CB  . PHE B  1  414 ? 29.223  -0.313  2.544   1.00 59.25  ? 440  PHE B CB  1 
ATOM   8099  C  CG  . PHE B  1  414 ? 28.580  -1.526  1.933   1.00 61.94  ? 440  PHE B CG  1 
ATOM   8100  C  CD1 . PHE B  1  414 ? 29.294  -2.354  1.065   1.00 63.28  ? 440  PHE B CD1 1 
ATOM   8101  C  CD2 . PHE B  1  414 ? 27.264  -1.862  2.242   1.00 61.58  ? 440  PHE B CD2 1 
ATOM   8102  C  CE1 . PHE B  1  414 ? 28.705  -3.508  0.511   1.00 62.32  ? 440  PHE B CE1 1 
ATOM   8103  C  CE2 . PHE B  1  414 ? 26.669  -3.005  1.697   1.00 61.51  ? 440  PHE B CE2 1 
ATOM   8104  C  CZ  . PHE B  1  414 ? 27.393  -3.831  0.829   1.00 60.92  ? 440  PHE B CZ  1 
ATOM   8105  N  N   . SER B  1  415 ? 30.635  0.508   0.016   1.00 60.06  ? 441  SER B N   1 
ATOM   8106  C  CA  . SER B  1  415 ? 31.078  0.387   -1.376  1.00 60.05  ? 441  SER B CA  1 
ATOM   8107  C  C   . SER B  1  415 ? 30.776  -1.011  -1.882  1.00 59.46  ? 441  SER B C   1 
ATOM   8108  O  O   . SER B  1  415 ? 31.595  -1.917  -1.757  1.00 58.51  ? 441  SER B O   1 
ATOM   8109  C  CB  . SER B  1  415 ? 32.571  0.668   -1.485  1.00 61.16  ? 441  SER B CB  1 
ATOM   8110  O  OG  . SER B  1  415 ? 32.854  1.998   -1.079  1.00 65.11  ? 441  SER B OG  1 
ATOM   8111  N  N   . VAL B  1  416 ? 29.589  -1.179  -2.457  1.00 59.34  ? 442  VAL B N   1 
ATOM   8112  C  CA  . VAL B  1  416 ? 29.159  -2.484  -2.938  1.00 59.36  ? 442  VAL B CA  1 
ATOM   8113  C  C   . VAL B  1  416 ? 30.009  -3.042  -4.076  1.00 60.01  ? 442  VAL B C   1 
ATOM   8114  O  O   . VAL B  1  416 ? 30.106  -4.256  -4.241  1.00 59.70  ? 442  VAL B O   1 
ATOM   8115  C  CB  . VAL B  1  416 ? 27.682  -2.452  -3.387  1.00 59.27  ? 442  VAL B CB  1 
ATOM   8116  C  CG1 . VAL B  1  416 ? 26.821  -1.863  -2.298  1.00 59.55  ? 442  VAL B CG1 1 
ATOM   8117  C  CG2 . VAL B  1  416 ? 27.534  -1.656  -4.642  1.00 60.87  ? 442  VAL B CG2 1 
ATOM   8118  N  N   . PHE B  1  417 ? 30.634  -2.159  -4.852  1.00 60.38  ? 443  PHE B N   1 
ATOM   8119  C  CA  . PHE B  1  417 ? 31.462  -2.587  -5.975  1.00 59.37  ? 443  PHE B CA  1 
ATOM   8120  C  C   . PHE B  1  417 ? 32.967  -2.542  -5.690  1.00 59.96  ? 443  PHE B C   1 
ATOM   8121  O  O   . PHE B  1  417 ? 33.789  -2.687  -6.599  1.00 60.28  ? 443  PHE B O   1 
ATOM   8122  C  CB  . PHE B  1  417 ? 31.142  -1.725  -7.195  1.00 56.28  ? 443  PHE B CB  1 
ATOM   8123  C  CG  . PHE B  1  417 ? 29.681  -1.673  -7.533  1.00 54.71  ? 443  PHE B CG  1 
ATOM   8124  C  CD1 . PHE B  1  417 ? 29.008  -2.804  -7.952  1.00 53.10  ? 443  PHE B CD1 1 
ATOM   8125  C  CD2 . PHE B  1  417 ? 28.972  -0.484  -7.426  1.00 56.34  ? 443  PHE B CD2 1 
ATOM   8126  C  CE1 . PHE B  1  417 ? 27.658  -2.754  -8.262  1.00 51.66  ? 443  PHE B CE1 1 
ATOM   8127  C  CE2 . PHE B  1  417 ? 27.603  -0.423  -7.737  1.00 54.03  ? 443  PHE B CE2 1 
ATOM   8128  C  CZ  . PHE B  1  417 ? 26.955  -1.558  -8.154  1.00 52.26  ? 443  PHE B CZ  1 
ATOM   8129  N  N   . LEU B  1  418 ? 33.328  -2.380  -4.426  1.00 60.46  ? 444  LEU B N   1 
ATOM   8130  C  CA  . LEU B  1  418 ? 34.733  -2.277  -4.049  1.00 61.45  ? 444  LEU B CA  1 
ATOM   8131  C  C   . LEU B  1  418 ? 35.707  -3.327  -4.563  1.00 61.52  ? 444  LEU B C   1 
ATOM   8132  O  O   . LEU B  1  418 ? 36.895  -3.049  -4.652  1.00 63.22  ? 444  LEU B O   1 
ATOM   8133  C  CB  . LEU B  1  418 ? 34.874  -2.214  -2.524  1.00 61.48  ? 444  LEU B CB  1 
ATOM   8134  C  CG  . LEU B  1  418 ? 36.065  -1.392  -2.023  1.00 60.44  ? 444  LEU B CG  1 
ATOM   8135  C  CD1 . LEU B  1  418 ? 35.788  0.099   -2.278  1.00 58.03  ? 444  LEU B CD1 1 
ATOM   8136  C  CD2 . LEU B  1  418 ? 36.288  -1.649  -0.546  1.00 61.09  ? 444  LEU B CD2 1 
ATOM   8137  N  N   . SER B  1  419 ? 35.233  -4.526  -4.888  1.00 61.33  ? 445  SER B N   1 
ATOM   8138  C  CA  . SER B  1  419 ? 36.136  -5.583  -5.346  1.00 60.38  ? 445  SER B CA  1 
ATOM   8139  C  C   . SER B  1  419 ? 36.266  -5.695  -6.854  1.00 62.17  ? 445  SER B C   1 
ATOM   8140  O  O   . SER B  1  419 ? 37.203  -6.324  -7.352  1.00 62.62  ? 445  SER B O   1 
ATOM   8141  C  CB  . SER B  1  419 ? 35.690  -6.942  -4.804  1.00 58.05  ? 445  SER B CB  1 
ATOM   8142  O  OG  . SER B  1  419 ? 36.005  -7.100  -3.440  1.00 55.07  ? 445  SER B OG  1 
ATOM   8143  N  N   . LEU B  1  420 ? 35.333  -5.088  -7.575  1.00 63.07  ? 446  LEU B N   1 
ATOM   8144  C  CA  . LEU B  1  420 ? 35.317  -5.165  -9.032  1.00 65.12  ? 446  LEU B CA  1 
ATOM   8145  C  C   . LEU B  1  420 ? 36.363  -4.299  -9.736  1.00 66.95  ? 446  LEU B C   1 
ATOM   8146  O  O   . LEU B  1  420 ? 36.031  -3.371  -10.480 1.00 68.08  ? 446  LEU B O   1 
ATOM   8147  C  CB  . LEU B  1  420 ? 33.908  -4.827  -9.535  1.00 63.60  ? 446  LEU B CB  1 
ATOM   8148  C  CG  . LEU B  1  420 ? 32.819  -5.907  -9.487  1.00 61.32  ? 446  LEU B CG  1 
ATOM   8149  C  CD1 . LEU B  1  420 ? 33.216  -7.064  -8.577  1.00 58.59  ? 446  LEU B CD1 1 
ATOM   8150  C  CD2 . LEU B  1  420 ? 31.520  -5.259  -9.045  1.00 59.68  ? 446  LEU B CD2 1 
ATOM   8151  N  N   . ARG B  1  421 ? 37.631  -4.616  -9.504  1.00 69.17  ? 447  ARG B N   1 
ATOM   8152  C  CA  . ARG B  1  421 ? 38.729  -3.866  -10.104 1.00 70.77  ? 447  ARG B CA  1 
ATOM   8153  C  C   . ARG B  1  421 ? 38.814  -4.044  -11.616 1.00 69.93  ? 447  ARG B C   1 
ATOM   8154  O  O   . ARG B  1  421 ? 39.452  -3.239  -12.303 1.00 70.36  ? 447  ARG B O   1 
ATOM   8155  C  CB  . ARG B  1  421 ? 40.068  -4.274  -9.469  1.00 73.67  ? 447  ARG B CB  1 
ATOM   8156  C  CG  . ARG B  1  421 ? 40.264  -5.784  -9.273  1.00 78.47  ? 447  ARG B CG  1 
ATOM   8157  C  CD  . ARG B  1  421 ? 41.690  -6.212  -9.598  1.00 84.27  ? 447  ARG B CD  1 
ATOM   8158  N  NE  . ARG B  1  421 ? 42.696  -5.313  -9.018  1.00 90.89  ? 447  ARG B NE  1 
ATOM   8159  C  CZ  . ARG B  1  421 ? 43.933  -5.139  -9.498  1.00 92.35  ? 447  ARG B CZ  1 
ATOM   8160  N  NH1 . ARG B  1  421 ? 44.339  -5.802  -10.582 1.00 92.71  ? 447  ARG B NH1 1 
ATOM   8161  N  NH2 . ARG B  1  421 ? 44.769  -4.293  -8.897  1.00 91.17  ? 447  ARG B NH2 1 
ATOM   8162  N  N   . ASN B  1  422 ? 38.160  -5.081  -12.139 1.00 67.85  ? 448  ASN B N   1 
ATOM   8163  C  CA  . ASN B  1  422 ? 38.215  -5.345  -13.573 1.00 64.26  ? 448  ASN B CA  1 
ATOM   8164  C  C   . ASN B  1  422 ? 36.911  -5.101  -14.309 1.00 61.77  ? 448  ASN B C   1 
ATOM   8165  O  O   . ASN B  1  422 ? 36.860  -5.237  -15.525 1.00 60.80  ? 448  ASN B O   1 
ATOM   8166  C  CB  . ASN B  1  422 ? 38.695  -6.781  -13.819 1.00 62.61  ? 448  ASN B CB  1 
ATOM   8167  C  CG  . ASN B  1  422 ? 40.013  -7.081  -13.116 1.00 62.29  ? 448  ASN B CG  1 
ATOM   8168  O  OD1 . ASN B  1  422 ? 40.951  -6.289  -13.169 1.00 63.52  ? 448  ASN B OD1 1 
ATOM   8169  N  ND2 . ASN B  1  422 ? 40.091  -8.228  -12.463 1.00 60.85  ? 448  ASN B ND2 1 
ATOM   8170  N  N   . LEU B  1  423 ? 35.865  -4.722  -13.582 1.00 60.77  ? 449  LEU B N   1 
ATOM   8171  C  CA  . LEU B  1  423 ? 34.566  -4.478  -14.210 1.00 60.85  ? 449  LEU B CA  1 
ATOM   8172  C  C   . LEU B  1  423 ? 34.670  -3.432  -15.316 1.00 61.05  ? 449  LEU B C   1 
ATOM   8173  O  O   . LEU B  1  423 ? 35.172  -2.339  -15.089 1.00 62.94  ? 449  LEU B O   1 
ATOM   8174  C  CB  . LEU B  1  423 ? 33.522  -4.018  -13.175 1.00 58.39  ? 449  LEU B CB  1 
ATOM   8175  C  CG  . LEU B  1  423 ? 32.090  -3.985  -13.728 1.00 56.90  ? 449  LEU B CG  1 
ATOM   8176  C  CD1 . LEU B  1  423 ? 31.638  -5.411  -14.021 1.00 55.23  ? 449  LEU B CD1 1 
ATOM   8177  C  CD2 . LEU B  1  423 ? 31.142  -3.322  -12.746 1.00 55.57  ? 449  LEU B CD2 1 
ATOM   8178  N  N   . ILE B  1  424 ? 34.186  -3.777  -16.507 1.00 60.72  ? 450  ILE B N   1 
ATOM   8179  C  CA  . ILE B  1  424 ? 34.227  -2.885  -17.664 1.00 60.07  ? 450  ILE B CA  1 
ATOM   8180  C  C   . ILE B  1  424 ? 32.847  -2.308  -18.028 1.00 60.18  ? 450  ILE B C   1 
ATOM   8181  O  O   . ILE B  1  424 ? 32.736  -1.152  -18.444 1.00 60.20  ? 450  ILE B O   1 
ATOM   8182  C  CB  . ILE B  1  424 ? 34.830  -3.631  -18.883 1.00 59.97  ? 450  ILE B CB  1 
ATOM   8183  C  CG1 . ILE B  1  424 ? 36.339  -3.809  -18.679 1.00 60.70  ? 450  ILE B CG1 1 
ATOM   8184  C  CG2 . ILE B  1  424 ? 34.518  -2.890  -20.160 1.00 58.02  ? 450  ILE B CG2 1 
ATOM   8185  C  CD1 . ILE B  1  424 ? 36.994  -4.843  -19.596 1.00 60.91  ? 450  ILE B CD1 1 
ATOM   8186  N  N   . TYR B  1  425 ? 31.800  -3.116  -17.871 1.00 59.42  ? 451  TYR B N   1 
ATOM   8187  C  CA  . TYR B  1  425 ? 30.432  -2.689  -18.167 1.00 57.92  ? 451  TYR B CA  1 
ATOM   8188  C  C   . TYR B  1  425 ? 29.585  -2.752  -16.893 1.00 57.46  ? 451  TYR B C   1 
ATOM   8189  O  O   . TYR B  1  425 ? 29.725  -3.682  -16.109 1.00 58.79  ? 451  TYR B O   1 
ATOM   8190  C  CB  . TYR B  1  425 ? 29.834  -3.599  -19.249 1.00 57.20  ? 451  TYR B CB  1 
ATOM   8191  C  CG  . TYR B  1  425 ? 28.441  -3.219  -19.727 1.00 56.52  ? 451  TYR B CG  1 
ATOM   8192  C  CD1 . TYR B  1  425 ? 27.303  -3.729  -19.111 1.00 55.75  ? 451  TYR B CD1 1 
ATOM   8193  C  CD2 . TYR B  1  425 ? 28.264  -2.347  -20.804 1.00 56.23  ? 451  TYR B CD2 1 
ATOM   8194  C  CE1 . TYR B  1  425 ? 26.020  -3.375  -19.560 1.00 56.24  ? 451  TYR B CE1 1 
ATOM   8195  C  CE2 . TYR B  1  425 ? 26.989  -1.990  -21.259 1.00 55.04  ? 451  TYR B CE2 1 
ATOM   8196  C  CZ  . TYR B  1  425 ? 25.874  -2.500  -20.633 1.00 55.48  ? 451  TYR B CZ  1 
ATOM   8197  O  OH  . TYR B  1  425 ? 24.616  -2.103  -21.047 1.00 54.72  ? 451  TYR B OH  1 
ATOM   8198  N  N   . LEU B  1  426 ? 28.733  -1.755  -16.677 1.00 56.02  ? 452  LEU B N   1 
ATOM   8199  C  CA  . LEU B  1  426 ? 27.866  -1.727  -15.498 1.00 55.76  ? 452  LEU B CA  1 
ATOM   8200  C  C   . LEU B  1  426 ? 26.589  -0.928  -15.761 1.00 55.32  ? 452  LEU B C   1 
ATOM   8201  O  O   . LEU B  1  426 ? 26.629  0.274   -15.991 1.00 55.40  ? 452  LEU B O   1 
ATOM   8202  C  CB  . LEU B  1  426 ? 28.602  -1.137  -14.284 1.00 56.78  ? 452  LEU B CB  1 
ATOM   8203  C  CG  . LEU B  1  426 ? 27.731  -0.898  -13.035 1.00 57.19  ? 452  LEU B CG  1 
ATOM   8204  C  CD1 . LEU B  1  426 ? 27.275  -2.225  -12.467 1.00 58.08  ? 452  LEU B CD1 1 
ATOM   8205  C  CD2 . LEU B  1  426 ? 28.509  -0.141  -11.986 1.00 55.94  ? 452  LEU B CD2 1 
ATOM   8206  N  N   . ASP B  1  427 ? 25.455  -1.613  -15.721 1.00 54.82  ? 453  ASP B N   1 
ATOM   8207  C  CA  . ASP B  1  427 ? 24.162  -0.995  -15.966 1.00 54.55  ? 453  ASP B CA  1 
ATOM   8208  C  C   . ASP B  1  427 ? 23.307  -1.170  -14.709 1.00 55.81  ? 453  ASP B C   1 
ATOM   8209  O  O   . ASP B  1  427 ? 23.028  -2.292  -14.308 1.00 58.10  ? 453  ASP B O   1 
ATOM   8210  C  CB  . ASP B  1  427 ? 23.501  -1.686  -17.170 1.00 53.35  ? 453  ASP B CB  1 
ATOM   8211  C  CG  . ASP B  1  427 ? 22.146  -1.099  -17.533 1.00 55.17  ? 453  ASP B CG  1 
ATOM   8212  O  OD1 . ASP B  1  427 ? 21.500  -0.482  -16.659 1.00 55.08  ? 453  ASP B OD1 1 
ATOM   8213  O  OD2 . ASP B  1  427 ? 21.709  -1.270  -18.698 1.00 55.74  ? 453  ASP B OD2 1 
ATOM   8214  N  N   . ILE B  1  428 ? 22.919  -0.067  -14.075 1.00 55.71  ? 454  ILE B N   1 
ATOM   8215  C  CA  . ILE B  1  428 ? 22.068  -0.103  -12.883 1.00 53.35  ? 454  ILE B CA  1 
ATOM   8216  C  C   . ILE B  1  428 ? 20.927  0.860   -13.137 1.00 53.29  ? 454  ILE B C   1 
ATOM   8217  O  O   . ILE B  1  428 ? 20.434  1.510   -12.225 1.00 52.29  ? 454  ILE B O   1 
ATOM   8218  C  CB  . ILE B  1  428 ? 22.809  0.354   -11.606 1.00 52.71  ? 454  ILE B CB  1 
ATOM   8219  C  CG1 . ILE B  1  428 ? 23.358  1.777   -11.802 1.00 51.90  ? 454  ILE B CG1 1 
ATOM   8220  C  CG2 . ILE B  1  428 ? 23.907  -0.644  -11.265 1.00 50.73  ? 454  ILE B CG2 1 
ATOM   8221  C  CD1 . ILE B  1  428 ? 23.876  2.440   -10.537 1.00 50.12  ? 454  ILE B CD1 1 
ATOM   8222  N  N   . SER B  1  429 ? 20.531  0.952   -14.400 1.00 54.46  ? 455  SER B N   1 
ATOM   8223  C  CA  . SER B  1  429 ? 19.456  1.836   -14.808 1.00 57.73  ? 455  SER B CA  1 
ATOM   8224  C  C   . SER B  1  429 ? 18.149  1.397   -14.177 1.00 60.36  ? 455  SER B C   1 
ATOM   8225  O  O   . SER B  1  429 ? 17.875  0.207   -14.070 1.00 62.39  ? 455  SER B O   1 
ATOM   8226  C  CB  . SER B  1  429 ? 19.294  1.823   -16.330 1.00 56.65  ? 455  SER B CB  1 
ATOM   8227  O  OG  . SER B  1  429 ? 20.528  2.054   -16.981 1.00 58.43  ? 455  SER B OG  1 
ATOM   8228  N  N   . HIS B  1  430 ? 17.347  2.365   -13.757 1.00 62.76  ? 456  HIS B N   1 
ATOM   8229  C  CA  . HIS B  1  430 ? 16.041  2.095   -13.168 1.00 64.61  ? 456  HIS B CA  1 
ATOM   8230  C  C   . HIS B  1  430 ? 16.049  1.010   -12.109 1.00 64.34  ? 456  HIS B C   1 
ATOM   8231  O  O   . HIS B  1  430 ? 15.179  0.137   -12.102 1.00 64.48  ? 456  HIS B O   1 
ATOM   8232  C  CB  . HIS B  1  430 ? 15.058  1.707   -14.269 1.00 66.08  ? 456  HIS B CB  1 
ATOM   8233  C  CG  . HIS B  1  430 ? 15.063  2.645   -15.436 1.00 69.56  ? 456  HIS B CG  1 
ATOM   8234  N  ND1 . HIS B  1  430 ? 14.110  3.624   -15.608 1.00 69.90  ? 456  HIS B ND1 1 
ATOM   8235  C  CD2 . HIS B  1  430 ? 15.905  2.743   -16.493 1.00 70.24  ? 456  HIS B CD2 1 
ATOM   8236  C  CE1 . HIS B  1  430 ? 14.358  4.282   -16.728 1.00 70.74  ? 456  HIS B CE1 1 
ATOM   8237  N  NE2 . HIS B  1  430 ? 15.440  3.768   -17.282 1.00 71.72  ? 456  HIS B NE2 1 
ATOM   8238  N  N   . THR B  1  431 ? 17.031  1.061   -11.219 1.00 64.01  ? 457  THR B N   1 
ATOM   8239  C  CA  . THR B  1  431 ? 17.110  0.090   -10.142 1.00 64.11  ? 457  THR B CA  1 
ATOM   8240  C  C   . THR B  1  431 ? 16.675  0.737   -8.841  1.00 64.73  ? 457  THR B C   1 
ATOM   8241  O  O   . THR B  1  431 ? 16.930  0.217   -7.757  1.00 65.05  ? 457  THR B O   1 
ATOM   8242  C  CB  . THR B  1  431 ? 18.519  -0.442  -9.986  1.00 63.75  ? 457  THR B CB  1 
ATOM   8243  O  OG1 . THR B  1  431 ? 19.408  0.625   -9.650  1.00 63.00  ? 457  THR B OG1 1 
ATOM   8244  C  CG2 . THR B  1  431 ? 18.961  -1.062  -11.282 1.00 66.46  ? 457  THR B CG2 1 
ATOM   8245  N  N   . HIS B  1  432 ? 16.009  1.881   -8.970  1.00 65.69  ? 458  HIS B N   1 
ATOM   8246  C  CA  . HIS B  1  432 ? 15.509  2.628   -7.827  1.00 64.61  ? 458  HIS B CA  1 
ATOM   8247  C  C   . HIS B  1  432 ? 16.579  2.990   -6.826  1.00 62.74  ? 458  HIS B C   1 
ATOM   8248  O  O   . HIS B  1  432 ? 16.337  2.969   -5.628  1.00 61.88  ? 458  HIS B O   1 
ATOM   8249  C  CB  . HIS B  1  432 ? 14.407  1.838   -7.130  1.00 66.97  ? 458  HIS B CB  1 
ATOM   8250  C  CG  . HIS B  1  432 ? 13.138  1.769   -7.911  1.00 69.73  ? 458  HIS B CG  1 
ATOM   8251  N  ND1 . HIS B  1  432 ? 12.270  0.699   -7.827  1.00 70.30  ? 458  HIS B ND1 1 
ATOM   8252  C  CD2 . HIS B  1  432 ? 12.576  2.645   -8.778  1.00 70.78  ? 458  HIS B CD2 1 
ATOM   8253  C  CE1 . HIS B  1  432 ? 11.231  0.919   -8.609  1.00 71.40  ? 458  HIS B CE1 1 
ATOM   8254  N  NE2 . HIS B  1  432 ? 11.391  2.094   -9.197  1.00 72.56  ? 458  HIS B NE2 1 
ATOM   8255  N  N   . THR B  1  433 ? 17.767  3.315   -7.315  1.00 62.57  ? 459  THR B N   1 
ATOM   8256  C  CA  . THR B  1  433 ? 18.844  3.719   -6.428  1.00 63.83  ? 459  THR B CA  1 
ATOM   8257  C  C   . THR B  1  433 ? 18.662  5.190   -6.048  1.00 65.45  ? 459  THR B C   1 
ATOM   8258  O  O   . THR B  1  433 ? 18.034  5.963   -6.767  1.00 66.42  ? 459  THR B O   1 
ATOM   8259  C  CB  . THR B  1  433 ? 20.200  3.539   -7.094  1.00 62.59  ? 459  THR B CB  1 
ATOM   8260  O  OG1 . THR B  1  433 ? 20.347  2.172   -7.469  1.00 64.57  ? 459  THR B OG1 1 
ATOM   8261  C  CG2 . THR B  1  433 ? 21.316  3.899   -6.149  1.00 61.93  ? 459  THR B CG2 1 
ATOM   8262  N  N   . ARG B  1  434 ? 19.199  5.562   -4.895  1.00 66.56  ? 460  ARG B N   1 
ATOM   8263  C  CA  . ARG B  1  434 ? 19.124  6.923   -4.379  1.00 67.20  ? 460  ARG B CA  1 
ATOM   8264  C  C   . ARG B  1  434 ? 20.524  7.204   -3.879  1.00 66.33  ? 460  ARG B C   1 
ATOM   8265  O  O   . ARG B  1  434 ? 20.789  7.059   -2.689  1.00 66.71  ? 460  ARG B O   1 
ATOM   8266  C  CB  . ARG B  1  434 ? 18.147  6.968   -3.209  1.00 70.89  ? 460  ARG B CB  1 
ATOM   8267  C  CG  . ARG B  1  434 ? 18.138  8.260   -2.412  1.00 74.91  ? 460  ARG B CG  1 
ATOM   8268  C  CD  . ARG B  1  434 ? 17.463  9.368   -3.183  1.00 79.72  ? 460  ARG B CD  1 
ATOM   8269  N  NE  . ARG B  1  434 ? 16.445  10.052  -2.386  1.00 85.31  ? 460  ARG B NE  1 
ATOM   8270  C  CZ  . ARG B  1  434 ? 16.670  10.658  -1.218  1.00 88.68  ? 460  ARG B CZ  1 
ATOM   8271  N  NH1 . ARG B  1  434 ? 17.892  10.673  -0.683  1.00 88.29  ? 460  ARG B NH1 1 
ATOM   8272  N  NH2 . ARG B  1  434 ? 15.665  11.263  -0.584  1.00 89.98  ? 460  ARG B NH2 1 
ATOM   8273  N  N   . VAL B  1  435 ? 21.419  7.584   -4.786  1.00 64.86  ? 461  VAL B N   1 
ATOM   8274  C  CA  . VAL B  1  435 ? 22.810  7.842   -4.428  1.00 62.64  ? 461  VAL B CA  1 
ATOM   8275  C  C   . VAL B  1  435 ? 22.923  8.803   -3.257  1.00 62.11  ? 461  VAL B C   1 
ATOM   8276  O  O   . VAL B  1  435 ? 22.376  9.900   -3.296  1.00 63.04  ? 461  VAL B O   1 
ATOM   8277  C  CB  . VAL B  1  435 ? 23.576  8.410   -5.614  1.00 62.03  ? 461  VAL B CB  1 
ATOM   8278  C  CG1 . VAL B  1  435 ? 25.070  8.199   -5.418  1.00 61.23  ? 461  VAL B CG1 1 
ATOM   8279  C  CG2 . VAL B  1  435 ? 23.096  7.748   -6.886  1.00 61.45  ? 461  VAL B CG2 1 
ATOM   8280  N  N   . ALA B  1  436 ? 23.628  8.380   -2.212  1.00 60.60  ? 462  ALA B N   1 
ATOM   8281  C  CA  . ALA B  1  436 ? 23.797  9.191   -1.016  1.00 59.02  ? 462  ALA B CA  1 
ATOM   8282  C  C   . ALA B  1  436 ? 25.073  8.824   -0.303  1.00 59.95  ? 462  ALA B C   1 
ATOM   8283  O  O   . ALA B  1  436 ? 25.135  8.843   0.924   1.00 60.96  ? 462  ALA B O   1 
ATOM   8284  C  CB  . ALA B  1  436 ? 22.629  9.004   -0.089  1.00 57.09  ? 462  ALA B CB  1 
ATOM   8285  N  N   . PHE B  1  437 ? 26.086  8.467   -1.079  1.00 60.52  ? 463  PHE B N   1 
ATOM   8286  C  CA  . PHE B  1  437 ? 27.389  8.116   -0.542  1.00 62.75  ? 463  PHE B CA  1 
ATOM   8287  C  C   . PHE B  1  437 ? 28.394  8.343   -1.657  1.00 65.31  ? 463  PHE B C   1 
ATOM   8288  O  O   . PHE B  1  437 ? 28.343  7.706   -2.707  1.00 66.04  ? 463  PHE B O   1 
ATOM   8289  C  CB  . PHE B  1  437 ? 27.425  6.661   -0.082  1.00 61.12  ? 463  PHE B CB  1 
ATOM   8290  C  CG  . PHE B  1  437 ? 28.774  6.216   0.420   1.00 60.56  ? 463  PHE B CG  1 
ATOM   8291  C  CD1 . PHE B  1  437 ? 29.438  6.935   1.403   1.00 60.44  ? 463  PHE B CD1 1 
ATOM   8292  C  CD2 . PHE B  1  437 ? 29.360  5.046   -0.056  1.00 59.67  ? 463  PHE B CD2 1 
ATOM   8293  C  CE1 . PHE B  1  437 ? 30.670  6.495   1.904   1.00 60.59  ? 463  PHE B CE1 1 
ATOM   8294  C  CE2 . PHE B  1  437 ? 30.594  4.594   0.436   1.00 58.48  ? 463  PHE B CE2 1 
ATOM   8295  C  CZ  . PHE B  1  437 ? 31.249  5.312   1.420   1.00 58.94  ? 463  PHE B CZ  1 
ATOM   8296  N  N   . ASN B  1  438 ? 29.311  9.266   -1.425  1.00 68.05  ? 464  ASN B N   1 
ATOM   8297  C  CA  . ASN B  1  438 ? 30.309  9.601   -2.420  1.00 69.95  ? 464  ASN B CA  1 
ATOM   8298  C  C   . ASN B  1  438 ? 31.367  8.522   -2.622  1.00 70.41  ? 464  ASN B C   1 
ATOM   8299  O  O   . ASN B  1  438 ? 32.401  8.751   -3.259  1.00 71.69  ? 464  ASN B O   1 
ATOM   8300  C  CB  . ASN B  1  438 ? 30.936  10.950  -2.055  1.00 72.17  ? 464  ASN B CB  1 
ATOM   8301  C  CG  . ASN B  1  438 ? 30.018  12.123  -2.389  1.00 72.92  ? 464  ASN B CG  1 
ATOM   8302  O  OD1 . ASN B  1  438 ? 28.846  12.154  -1.996  1.00 72.73  ? 464  ASN B OD1 1 
ATOM   8303  N  ND2 . ASN B  1  438 ? 30.551  13.092  -3.121  1.00 74.14  ? 464  ASN B ND2 1 
ATOM   8304  N  N   . GLY B  1  439 ? 31.100  7.338   -2.084  1.00 69.50  ? 465  GLY B N   1 
ATOM   8305  C  CA  . GLY B  1  439 ? 32.025  6.228   -2.254  1.00 67.83  ? 465  GLY B CA  1 
ATOM   8306  C  C   . GLY B  1  439 ? 31.297  5.104   -2.968  1.00 65.34  ? 465  GLY B C   1 
ATOM   8307  O  O   . GLY B  1  439 ? 31.778  3.974   -3.066  1.00 64.06  ? 465  GLY B O   1 
ATOM   8308  N  N   . ILE B  1  440 ? 30.124  5.447   -3.489  1.00 63.72  ? 466  ILE B N   1 
ATOM   8309  C  CA  . ILE B  1  440 ? 29.271  4.506   -4.176  1.00 62.79  ? 466  ILE B CA  1 
ATOM   8310  C  C   . ILE B  1  440 ? 29.948  3.719   -5.296  1.00 64.09  ? 466  ILE B C   1 
ATOM   8311  O  O   . ILE B  1  440 ? 29.595  2.557   -5.528  1.00 65.18  ? 466  ILE B O   1 
ATOM   8312  C  CB  . ILE B  1  440 ? 27.999  5.219   -4.709  1.00 60.26  ? 466  ILE B CB  1 
ATOM   8313  C  CG1 . ILE B  1  440 ? 27.062  4.208   -5.352  1.00 59.95  ? 466  ILE B CG1 1 
ATOM   8314  C  CG2 . ILE B  1  440 ? 28.358  6.272   -5.715  1.00 59.50  ? 466  ILE B CG2 1 
ATOM   8315  C  CD1 . ILE B  1  440 ? 25.688  4.752   -5.588  1.00 60.15  ? 466  ILE B CD1 1 
ATOM   8316  N  N   . PHE B  1  441 ? 30.936  4.316   -5.962  1.00 64.15  ? 467  PHE B N   1 
ATOM   8317  C  CA  . PHE B  1  441 ? 31.608  3.633   -7.065  1.00 63.49  ? 467  PHE B CA  1 
ATOM   8318  C  C   . PHE B  1  441 ? 33.082  3.287   -6.853  1.00 63.65  ? 467  PHE B C   1 
ATOM   8319  O  O   . PHE B  1  441 ? 33.782  2.921   -7.801  1.00 62.44  ? 467  PHE B O   1 
ATOM   8320  C  CB  . PHE B  1  441 ? 31.460  4.457   -8.345  1.00 62.95  ? 467  PHE B CB  1 
ATOM   8321  C  CG  . PHE B  1  441 ? 30.029  4.589   -8.831  1.00 63.37  ? 467  PHE B CG  1 
ATOM   8322  C  CD1 . PHE B  1  441 ? 29.435  5.843   -8.955  1.00 64.15  ? 467  PHE B CD1 1 
ATOM   8323  C  CD2 . PHE B  1  441 ? 29.292  3.467   -9.210  1.00 62.93  ? 467  PHE B CD2 1 
ATOM   8324  C  CE1 . PHE B  1  441 ? 28.126  5.981   -9.446  1.00 64.47  ? 467  PHE B CE1 1 
ATOM   8325  C  CE2 . PHE B  1  441 ? 27.983  3.595   -9.703  1.00 62.71  ? 467  PHE B CE2 1 
ATOM   8326  C  CZ  . PHE B  1  441 ? 27.401  4.853   -9.827  1.00 63.57  ? 467  PHE B CZ  1 
ATOM   8327  N  N   . ASN B  1  442 ? 33.556  3.370   -5.616  1.00 65.43  ? 468  ASN B N   1 
ATOM   8328  C  CA  . ASN B  1  442 ? 34.963  3.063   -5.346  1.00 67.18  ? 468  ASN B CA  1 
ATOM   8329  C  C   . ASN B  1  442 ? 35.342  1.631   -5.696  1.00 66.45  ? 468  ASN B C   1 
ATOM   8330  O  O   . ASN B  1  442 ? 34.731  0.685   -5.222  1.00 67.30  ? 468  ASN B O   1 
ATOM   8331  C  CB  . ASN B  1  442 ? 35.318  3.314   -3.871  1.00 68.36  ? 468  ASN B CB  1 
ATOM   8332  C  CG  . ASN B  1  442 ? 35.209  4.773   -3.477  1.00 69.20  ? 468  ASN B CG  1 
ATOM   8333  O  OD1 . ASN B  1  442 ? 35.666  5.160   -2.404  1.00 70.75  ? 468  ASN B OD1 1 
ATOM   8334  N  ND2 . ASN B  1  442 ? 34.596  5.588   -4.335  1.00 69.28  ? 468  ASN B ND2 1 
ATOM   8335  N  N   . GLY B  1  443 ? 36.374  1.484   -6.513  1.00 66.35  ? 469  GLY B N   1 
ATOM   8336  C  CA  . GLY B  1  443 ? 36.830  0.168   -6.901  1.00 66.26  ? 469  GLY B CA  1 
ATOM   8337  C  C   . GLY B  1  443 ? 36.708  -0.008  -8.395  1.00 66.79  ? 469  GLY B C   1 
ATOM   8338  O  O   . GLY B  1  443 ? 37.465  -0.766  -9.007  1.00 66.64  ? 469  GLY B O   1 
ATOM   8339  N  N   . LEU B  1  444 ? 35.765  0.718   -8.986  1.00 66.82  ? 470  LEU B N   1 
ATOM   8340  C  CA  . LEU B  1  444 ? 35.515  0.636   -10.420 1.00 68.76  ? 470  LEU B CA  1 
ATOM   8341  C  C   . LEU B  1  444 ? 36.530  1.368   -11.312 1.00 70.30  ? 470  LEU B C   1 
ATOM   8342  O  O   . LEU B  1  444 ? 36.170  2.281   -12.066 1.00 69.90  ? 470  LEU B O   1 
ATOM   8343  C  CB  . LEU B  1  444 ? 34.106  1.152   -10.712 1.00 66.53  ? 470  LEU B CB  1 
ATOM   8344  C  CG  . LEU B  1  444 ? 32.995  0.404   -9.988  1.00 63.71  ? 470  LEU B CG  1 
ATOM   8345  C  CD1 . LEU B  1  444 ? 31.663  0.991   -10.385 1.00 61.41  ? 470  LEU B CD1 1 
ATOM   8346  C  CD2 . LEU B  1  444 ? 33.075  -1.078  -10.328 1.00 62.27  ? 470  LEU B CD2 1 
ATOM   8347  N  N   . SER B  1  445 ? 37.789  0.948   -11.232 1.00 71.41  ? 471  SER B N   1 
ATOM   8348  C  CA  . SER B  1  445 ? 38.868  1.544   -12.016 1.00 73.05  ? 471  SER B CA  1 
ATOM   8349  C  C   . SER B  1  445 ? 38.686  1.353   -13.521 1.00 74.68  ? 471  SER B C   1 
ATOM   8350  O  O   . SER B  1  445 ? 38.456  2.310   -14.278 1.00 75.80  ? 471  SER B O   1 
ATOM   8351  C  CB  . SER B  1  445 ? 40.191  0.923   -11.609 1.00 71.68  ? 471  SER B CB  1 
ATOM   8352  O  OG  . SER B  1  445 ? 40.270  0.879   -10.201 1.00 74.73  ? 471  SER B OG  1 
ATOM   8353  N  N   . SER B  1  446 ? 38.793  0.100   -13.943 1.00 74.65  ? 472  SER B N   1 
ATOM   8354  C  CA  . SER B  1  446 ? 38.674  -0.271  -15.346 1.00 72.91  ? 472  SER B CA  1 
ATOM   8355  C  C   . SER B  1  446 ? 37.352  0.115   -16.016 1.00 71.47  ? 472  SER B C   1 
ATOM   8356  O  O   . SER B  1  446 ? 37.257  0.122   -17.244 1.00 70.75  ? 472  SER B O   1 
ATOM   8357  C  CB  . SER B  1  446 ? 38.898  -1.780  -15.476 1.00 73.71  ? 472  SER B CB  1 
ATOM   8358  O  OG  . SER B  1  446 ? 40.113  -2.174  -14.849 1.00 74.13  ? 472  SER B OG  1 
ATOM   8359  N  N   . LEU B  1  447 ? 36.341  0.446   -15.217 1.00 70.46  ? 473  LEU B N   1 
ATOM   8360  C  CA  . LEU B  1  447 ? 35.025  0.783   -15.758 1.00 70.00  ? 473  LEU B CA  1 
ATOM   8361  C  C   . LEU B  1  447 ? 35.078  1.653   -17.009 1.00 69.83  ? 473  LEU B C   1 
ATOM   8362  O  O   . LEU B  1  447 ? 35.764  2.663   -17.031 1.00 72.02  ? 473  LEU B O   1 
ATOM   8363  C  CB  . LEU B  1  447 ? 34.165  1.469   -14.688 1.00 68.36  ? 473  LEU B CB  1 
ATOM   8364  C  CG  . LEU B  1  447 ? 32.644  1.506   -14.945 1.00 68.15  ? 473  LEU B CG  1 
ATOM   8365  C  CD1 . LEU B  1  447 ? 32.073  0.105   -14.950 1.00 67.85  ? 473  LEU B CD1 1 
ATOM   8366  C  CD2 . LEU B  1  447 ? 31.952  2.318   -13.875 1.00 66.98  ? 473  LEU B CD2 1 
ATOM   8367  N  N   . GLU B  1  448 ? 34.352  1.250   -18.049 1.00 69.35  ? 474  GLU B N   1 
ATOM   8368  C  CA  . GLU B  1  448 ? 34.302  2.001   -19.300 1.00 69.19  ? 474  GLU B CA  1 
ATOM   8369  C  C   . GLU B  1  448 ? 32.897  2.452   -19.671 1.00 68.53  ? 474  GLU B C   1 
ATOM   8370  O  O   . GLU B  1  448 ? 32.721  3.471   -20.340 1.00 68.10  ? 474  GLU B O   1 
ATOM   8371  C  CB  . GLU B  1  448 ? 34.898  1.179   -20.426 1.00 70.58  ? 474  GLU B CB  1 
ATOM   8372  C  CG  . GLU B  1  448 ? 36.393  1.074   -20.288 1.00 74.56  ? 474  GLU B CG  1 
ATOM   8373  C  CD  . GLU B  1  448 ? 36.996  0.050   -21.212 1.00 76.42  ? 474  GLU B CD  1 
ATOM   8374  O  OE1 . GLU B  1  448 ? 36.634  0.043   -22.408 1.00 76.40  ? 474  GLU B OE1 1 
ATOM   8375  O  OE2 . GLU B  1  448 ? 37.845  -0.737  -20.733 1.00 77.48  ? 474  GLU B OE2 1 
ATOM   8376  N  N   . VAL B  1  449 ? 31.895  1.686   -19.252 1.00 67.77  ? 475  VAL B N   1 
ATOM   8377  C  CA  . VAL B  1  449 ? 30.506  2.054   -19.507 1.00 66.12  ? 475  VAL B CA  1 
ATOM   8378  C  C   . VAL B  1  449 ? 29.804  2.120   -18.156 1.00 64.65  ? 475  VAL B C   1 
ATOM   8379  O  O   . VAL B  1  449 ? 30.155  1.389   -17.232 1.00 64.16  ? 475  VAL B O   1 
ATOM   8380  C  CB  . VAL B  1  449 ? 29.802  1.035   -20.413 1.00 66.17  ? 475  VAL B CB  1 
ATOM   8381  C  CG1 . VAL B  1  449 ? 28.394  1.528   -20.744 1.00 65.57  ? 475  VAL B CG1 1 
ATOM   8382  C  CG2 . VAL B  1  449 ? 30.613  0.837   -21.686 1.00 65.13  ? 475  VAL B CG2 1 
ATOM   8383  N  N   . LEU B  1  450 ? 28.825  3.003   -18.040 1.00 63.25  ? 476  LEU B N   1 
ATOM   8384  C  CA  . LEU B  1  450 ? 28.109  3.170   -16.788 1.00 63.93  ? 476  LEU B CA  1 
ATOM   8385  C  C   . LEU B  1  450 ? 26.715  3.701   -17.086 1.00 63.88  ? 476  LEU B C   1 
ATOM   8386  O  O   . LEU B  1  450 ? 26.549  4.879   -17.386 1.00 63.38  ? 476  LEU B O   1 
ATOM   8387  C  CB  . LEU B  1  450 ? 28.869  4.161   -15.894 1.00 63.59  ? 476  LEU B CB  1 
ATOM   8388  C  CG  . LEU B  1  450 ? 28.491  4.443   -14.429 1.00 64.48  ? 476  LEU B CG  1 
ATOM   8389  C  CD1 . LEU B  1  450 ? 27.035  4.887   -14.293 1.00 63.55  ? 476  LEU B CD1 1 
ATOM   8390  C  CD2 . LEU B  1  450 ? 28.729  3.200   -13.621 1.00 65.96  ? 476  LEU B CD2 1 
ATOM   8391  N  N   . LYS B  1  451 ? 25.712  2.834   -17.024 1.00 64.74  ? 477  LYS B N   1 
ATOM   8392  C  CA  . LYS B  1  451 ? 24.350  3.274   -17.288 1.00 65.71  ? 477  LYS B CA  1 
ATOM   8393  C  C   . LYS B  1  451 ? 23.562  3.354   -15.991 1.00 66.24  ? 477  LYS B C   1 
ATOM   8394  O  O   . LYS B  1  451 ? 23.157  2.338   -15.441 1.00 67.56  ? 477  LYS B O   1 
ATOM   8395  C  CB  . LYS B  1  451 ? 23.638  2.317   -18.246 1.00 64.93  ? 477  LYS B CB  1 
ATOM   8396  C  CG  . LYS B  1  451 ? 24.348  2.055   -19.561 1.00 65.13  ? 477  LYS B CG  1 
ATOM   8397  C  CD  . LYS B  1  451 ? 23.387  1.373   -20.532 1.00 66.82  ? 477  LYS B CD  1 
ATOM   8398  C  CE  . LYS B  1  451 ? 24.089  0.817   -21.768 1.00 66.98  ? 477  LYS B CE  1 
ATOM   8399  N  NZ  . LYS B  1  451 ? 23.163  0.017   -22.622 1.00 66.51  ? 477  LYS B NZ  1 
ATOM   8400  N  N   . MET B  1  452 ? 23.347  4.555   -15.486 1.00 66.43  ? 478  MET B N   1 
ATOM   8401  C  CA  . MET B  1  452 ? 22.589  4.671   -14.262 1.00 66.43  ? 478  MET B CA  1 
ATOM   8402  C  C   . MET B  1  452 ? 21.388  5.581   -14.441 1.00 65.81  ? 478  MET B C   1 
ATOM   8403  O  O   . MET B  1  452 ? 21.044  6.361   -13.559 1.00 65.67  ? 478  MET B O   1 
ATOM   8404  C  CB  . MET B  1  452 ? 23.491  5.146   -13.113 1.00 68.21  ? 478  MET B CB  1 
ATOM   8405  C  CG  . MET B  1  452 ? 24.105  6.531   -13.235 1.00 68.53  ? 478  MET B CG  1 
ATOM   8406  S  SD  . MET B  1  452 ? 25.130  6.854   -11.774 1.00 72.21  ? 478  MET B SD  1 
ATOM   8407  C  CE  . MET B  1  452 ? 23.896  7.160   -10.544 1.00 68.79  ? 478  MET B CE  1 
ATOM   8408  N  N   . ALA B  1  453 ? 20.751  5.469   -15.599 1.00 64.57  ? 479  ALA B N   1 
ATOM   8409  C  CA  . ALA B  1  453 ? 19.574  6.265   -15.897 1.00 65.44  ? 479  ALA B CA  1 
ATOM   8410  C  C   . ALA B  1  453 ? 18.427  5.908   -14.953 1.00 66.72  ? 479  ALA B C   1 
ATOM   8411  O  O   . ALA B  1  453 ? 18.535  4.981   -14.163 1.00 68.30  ? 479  ALA B O   1 
ATOM   8412  C  CB  . ALA B  1  453 ? 19.145  6.028   -17.322 1.00 63.95  ? 479  ALA B CB  1 
ATOM   8413  N  N   . GLY B  1  454 ? 17.342  6.673   -15.032 1.00 68.23  ? 480  GLY B N   1 
ATOM   8414  C  CA  . GLY B  1  454 ? 16.151  6.437   -14.226 1.00 68.06  ? 480  GLY B CA  1 
ATOM   8415  C  C   . GLY B  1  454 ? 16.180  6.514   -12.708 1.00 68.75  ? 480  GLY B C   1 
ATOM   8416  O  O   . GLY B  1  454 ? 15.146  6.309   -12.078 1.00 70.11  ? 480  GLY B O   1 
ATOM   8417  N  N   . ASN B  1  455 ? 17.323  6.816   -12.103 1.00 68.75  ? 481  ASN B N   1 
ATOM   8418  C  CA  . ASN B  1  455 ? 17.380  6.863   -10.647 1.00 68.75  ? 481  ASN B CA  1 
ATOM   8419  C  C   . ASN B  1  455 ? 17.165  8.231   -10.030 1.00 69.30  ? 481  ASN B C   1 
ATOM   8420  O  O   . ASN B  1  455 ? 16.241  8.959   -10.405 1.00 69.01  ? 481  ASN B O   1 
ATOM   8421  C  CB  . ASN B  1  455 ? 18.703  6.277   -10.163 1.00 67.83  ? 481  ASN B CB  1 
ATOM   8422  C  CG  . ASN B  1  455 ? 18.838  4.811   -10.517 1.00 68.43  ? 481  ASN B CG  1 
ATOM   8423  O  OD1 . ASN B  1  455 ? 17.910  4.020   -10.293 1.00 68.44  ? 481  ASN B OD1 1 
ATOM   8424  N  ND2 . ASN B  1  455 ? 19.985  4.436   -11.074 1.00 67.46  ? 481  ASN B ND2 1 
ATOM   8425  N  N   . SER B  1  456 ? 18.013  8.561   -9.060  1.00 70.40  ? 482  SER B N   1 
ATOM   8426  C  CA  . SER B  1  456 ? 17.930  9.842   -8.368  1.00 71.82  ? 482  SER B CA  1 
ATOM   8427  C  C   . SER B  1  456 ? 19.104  10.048  -7.419  1.00 71.86  ? 482  SER B C   1 
ATOM   8428  O  O   . SER B  1  456 ? 19.796  9.097   -7.038  1.00 71.08  ? 482  SER B O   1 
ATOM   8429  C  CB  . SER B  1  456 ? 16.638  9.941   -7.554  1.00 72.40  ? 482  SER B CB  1 
ATOM   8430  O  OG  . SER B  1  456 ? 16.792  9.280   -6.307  1.00 73.39  ? 482  SER B OG  1 
ATOM   8431  N  N   . PHE B  1  457 ? 19.319  11.305  -7.044  1.00 72.33  ? 483  PHE B N   1 
ATOM   8432  C  CA  . PHE B  1  457 ? 20.389  11.641  -6.129  1.00 72.10  ? 483  PHE B CA  1 
ATOM   8433  C  C   . PHE B  1  457 ? 19.856  12.391  -4.924  1.00 73.67  ? 483  PHE B C   1 
ATOM   8434  O  O   . PHE B  1  457 ? 18.765  12.967  -4.949  1.00 72.62  ? 483  PHE B O   1 
ATOM   8435  C  CB  . PHE B  1  457 ? 21.452  12.485  -6.823  1.00 68.34  ? 483  PHE B CB  1 
ATOM   8436  C  CG  . PHE B  1  457 ? 22.208  11.752  -7.889  1.00 66.04  ? 483  PHE B CG  1 
ATOM   8437  C  CD1 . PHE B  1  457 ? 21.605  11.452  -9.109  1.00 64.17  ? 483  PHE B CD1 1 
ATOM   8438  C  CD2 . PHE B  1  457 ? 23.533  11.378  -7.682  1.00 64.44  ? 483  PHE B CD2 1 
ATOM   8439  C  CE1 . PHE B  1  457 ? 22.312  10.794  -10.110 1.00 62.95  ? 483  PHE B CE1 1 
ATOM   8440  C  CE2 . PHE B  1  457 ? 24.255  10.720  -8.669  1.00 63.08  ? 483  PHE B CE2 1 
ATOM   8441  C  CZ  . PHE B  1  457 ? 23.644  10.426  -9.889  1.00 63.34  ? 483  PHE B CZ  1 
ATOM   8442  N  N   . GLN B  1  458 ? 20.643  12.356  -3.859  1.00 76.72  ? 484  GLN B N   1 
ATOM   8443  C  CA  . GLN B  1  458 ? 20.297  13.029  -2.627  1.00 79.65  ? 484  GLN B CA  1 
ATOM   8444  C  C   . GLN B  1  458 ? 20.379  14.524  -2.910  1.00 81.94  ? 484  GLN B C   1 
ATOM   8445  O  O   . GLN B  1  458 ? 21.411  15.020  -3.385  1.00 81.12  ? 484  GLN B O   1 
ATOM   8446  C  CB  . GLN B  1  458 ? 21.287  12.637  -1.518  1.00 78.97  ? 484  GLN B CB  1 
ATOM   8447  C  CG  . GLN B  1  458 ? 21.011  13.280  -0.170  1.00 79.33  ? 484  GLN B CG  1 
ATOM   8448  C  CD  . GLN B  1  458 ? 22.005  12.846  0.894   1.00 80.71  ? 484  GLN B CD  1 
ATOM   8449  O  OE1 . GLN B  1  458 ? 23.215  12.821  0.657   1.00 80.13  ? 484  GLN B OE1 1 
ATOM   8450  N  NE2 . GLN B  1  458 ? 21.498  12.513  2.082   1.00 81.07  ? 484  GLN B NE2 1 
ATOM   8451  N  N   . GLU B  1  459 ? 19.278  15.226  -2.647  1.00 83.71  ? 485  GLU B N   1 
ATOM   8452  C  CA  . GLU B  1  459 ? 19.219  16.665  -2.847  1.00 85.22  ? 485  GLU B CA  1 
ATOM   8453  C  C   . GLU B  1  459 ? 19.216  17.044  -4.327  1.00 84.85  ? 485  GLU B C   1 
ATOM   8454  O  O   . GLU B  1  459 ? 19.191  18.219  -4.678  1.00 86.19  ? 485  GLU B O   1 
ATOM   8455  C  CB  . GLU B  1  459 ? 20.401  17.327  -2.128  1.00 87.08  ? 485  GLU B CB  1 
ATOM   8456  C  CG  . GLU B  1  459 ? 20.025  18.534  -1.286  1.00 91.06  ? 485  GLU B CG  1 
ATOM   8457  C  CD  . GLU B  1  459 ? 18.721  18.338  -0.523  1.00 93.56  ? 485  GLU B CD  1 
ATOM   8458  O  OE1 . GLU B  1  459 ? 17.638  18.494  -1.141  1.00 94.35  ? 485  GLU B OE1 1 
ATOM   8459  O  OE2 . GLU B  1  459 ? 18.782  18.010  0.687   1.00 94.38  ? 485  GLU B OE2 1 
ATOM   8460  N  N   . ASN B  1  460 ? 19.237  16.046  -5.197  1.00 83.41  ? 486  ASN B N   1 
ATOM   8461  C  CA  . ASN B  1  460 ? 19.224  16.304  -6.624  1.00 81.97  ? 486  ASN B CA  1 
ATOM   8462  C  C   . ASN B  1  460 ? 20.486  17.009  -7.086  1.00 80.96  ? 486  ASN B C   1 
ATOM   8463  O  O   . ASN B  1  460 ? 20.524  17.604  -8.150  1.00 81.88  ? 486  ASN B O   1 
ATOM   8464  C  CB  . ASN B  1  460 ? 17.981  17.113  -6.987  1.00 81.32  ? 486  ASN B CB  1 
ATOM   8465  C  CG  . ASN B  1  460 ? 16.704  16.328  -6.754  1.00 82.66  ? 486  ASN B CG  1 
ATOM   8466  O  OD1 . ASN B  1  460 ? 15.603  16.849  -6.906  1.00 84.26  ? 486  ASN B OD1 1 
ATOM   8467  N  ND2 . ASN B  1  460 ? 16.849  15.056  -6.389  1.00 83.33  ? 486  ASN B ND2 1 
ATOM   8468  N  N   . PHE B  1  461 ? 21.527  16.929  -6.276  1.00 79.97  ? 487  PHE B N   1 
ATOM   8469  C  CA  . PHE B  1  461 ? 22.806  17.531  -6.609  1.00 80.28  ? 487  PHE B CA  1 
ATOM   8470  C  C   . PHE B  1  461 ? 23.743  16.377  -6.977  1.00 80.81  ? 487  PHE B C   1 
ATOM   8471  O  O   . PHE B  1  461 ? 23.837  15.395  -6.246  1.00 81.97  ? 487  PHE B O   1 
ATOM   8472  C  CB  . PHE B  1  461 ? 23.314  18.319  -5.395  1.00 80.01  ? 487  PHE B CB  1 
ATOM   8473  C  CG  . PHE B  1  461 ? 24.792  18.634  -5.428  1.00 80.44  ? 487  PHE B CG  1 
ATOM   8474  C  CD1 . PHE B  1  461 ? 25.729  17.733  -4.905  1.00 80.39  ? 487  PHE B CD1 1 
ATOM   8475  C  CD2 . PHE B  1  461 ? 25.250  19.840  -5.961  1.00 81.01  ? 487  PHE B CD2 1 
ATOM   8476  C  CE1 . PHE B  1  461 ? 27.106  18.022  -4.907  1.00 80.02  ? 487  PHE B CE1 1 
ATOM   8477  C  CE2 . PHE B  1  461 ? 26.626  20.144  -5.973  1.00 81.22  ? 487  PHE B CE2 1 
ATOM   8478  C  CZ  . PHE B  1  461 ? 27.558  19.226  -5.438  1.00 80.46  ? 487  PHE B CZ  1 
ATOM   8479  N  N   . LEU B  1  462 ? 24.417  16.482  -8.117  1.00 81.32  ? 488  LEU B N   1 
ATOM   8480  C  CA  . LEU B  1  462 ? 25.326  15.426  -8.574  1.00 81.50  ? 488  LEU B CA  1 
ATOM   8481  C  C   . LEU B  1  462 ? 26.728  15.565  -7.992  1.00 80.51  ? 488  LEU B C   1 
ATOM   8482  O  O   . LEU B  1  462 ? 27.495  16.402  -8.435  1.00 79.20  ? 488  LEU B O   1 
ATOM   8483  C  CB  . LEU B  1  462 ? 25.408  15.445  -10.097 1.00 82.95  ? 488  LEU B CB  1 
ATOM   8484  C  CG  . LEU B  1  462 ? 26.453  14.545  -10.748 1.00 85.01  ? 488  LEU B CG  1 
ATOM   8485  C  CD1 . LEU B  1  462 ? 26.230  13.095  -10.360 1.00 87.02  ? 488  LEU B CD1 1 
ATOM   8486  C  CD2 . LEU B  1  462 ? 26.346  14.705  -12.253 1.00 86.92  ? 488  LEU B CD2 1 
ATOM   8487  N  N   . PRO B  1  463 ? 27.079  14.727  -7.002  1.00 81.12  ? 489  PRO B N   1 
ATOM   8488  C  CA  . PRO B  1  463 ? 28.394  14.756  -6.344  1.00 81.20  ? 489  PRO B CA  1 
ATOM   8489  C  C   . PRO B  1  463 ? 29.608  14.301  -7.147  1.00 80.98  ? 489  PRO B C   1 
ATOM   8490  O  O   . PRO B  1  463 ? 29.507  13.927  -8.308  1.00 79.64  ? 489  PRO B O   1 
ATOM   8491  C  CB  . PRO B  1  463 ? 28.186  13.875  -5.103  1.00 81.72  ? 489  PRO B CB  1 
ATOM   8492  C  CG  . PRO B  1  463 ? 26.696  13.954  -4.850  1.00 81.35  ? 489  PRO B CG  1 
ATOM   8493  C  CD  . PRO B  1  463 ? 26.151  13.859  -6.254  1.00 81.47  ? 489  PRO B CD  1 
ATOM   8494  N  N   . ASP B  1  464 ? 30.758  14.333  -6.479  1.00 82.47  ? 490  ASP B N   1 
ATOM   8495  C  CA  . ASP B  1  464 ? 32.054  13.935  -7.041  1.00 84.74  ? 490  ASP B CA  1 
ATOM   8496  C  C   . ASP B  1  464 ? 32.320  12.441  -6.844  1.00 84.34  ? 490  ASP B C   1 
ATOM   8497  O  O   . ASP B  1  464 ? 33.264  12.049  -6.138  1.00 83.68  ? 490  ASP B O   1 
ATOM   8498  C  CB  . ASP B  1  464 ? 33.170  14.725  -6.355  1.00 86.94  ? 490  ASP B CB  1 
ATOM   8499  C  CG  . ASP B  1  464 ? 33.665  15.879  -7.194  1.00 88.63  ? 490  ASP B CG  1 
ATOM   8500  O  OD1 . ASP B  1  464 ? 34.336  15.620  -8.220  1.00 89.24  ? 490  ASP B OD1 1 
ATOM   8501  O  OD2 . ASP B  1  464 ? 33.377  17.040  -6.826  1.00 89.75  ? 490  ASP B OD2 1 
ATOM   8502  N  N   . ILE B  1  465 ? 31.508  11.616  -7.495  1.00 83.43  ? 491  ILE B N   1 
ATOM   8503  C  CA  . ILE B  1  465 ? 31.604  10.165  -7.369  1.00 81.58  ? 491  ILE B CA  1 
ATOM   8504  C  C   . ILE B  1  465 ? 32.321  9.443   -8.506  1.00 81.58  ? 491  ILE B C   1 
ATOM   8505  O  O   . ILE B  1  465 ? 32.528  8.234   -8.439  1.00 80.80  ? 491  ILE B O   1 
ATOM   8506  C  CB  . ILE B  1  465 ? 30.204  9.591   -7.244  1.00 80.41  ? 491  ILE B CB  1 
ATOM   8507  C  CG1 . ILE B  1  465 ? 29.338  10.136  -8.388  1.00 78.36  ? 491  ILE B CG1 1 
ATOM   8508  C  CG2 . ILE B  1  465 ? 29.617  9.960   -5.882  1.00 80.60  ? 491  ILE B CG2 1 
ATOM   8509  C  CD1 . ILE B  1  465 ? 27.864  9.820   -8.271  1.00 77.36  ? 491  ILE B CD1 1 
ATOM   8510  N  N   . PHE B  1  466 ? 32.712  10.186  -9.536  1.00 81.91  ? 492  PHE B N   1 
ATOM   8511  C  CA  . PHE B  1  466 ? 33.372  9.610   -10.704 1.00 80.74  ? 492  PHE B CA  1 
ATOM   8512  C  C   . PHE B  1  466 ? 34.889  9.782   -10.737 1.00 82.15  ? 492  PHE B C   1 
ATOM   8513  O  O   . PHE B  1  466 ? 35.551  9.340   -11.671 1.00 82.12  ? 492  PHE B O   1 
ATOM   8514  C  CB  . PHE B  1  466 ? 32.755  10.231  -11.953 1.00 76.50  ? 492  PHE B CB  1 
ATOM   8515  C  CG  . PHE B  1  466 ? 31.259  10.192  -11.965 1.00 74.33  ? 492  PHE B CG  1 
ATOM   8516  C  CD1 . PHE B  1  466 ? 30.587  8.988   -12.070 1.00 73.54  ? 492  PHE B CD1 1 
ATOM   8517  C  CD2 . PHE B  1  466 ? 30.519  11.359  -11.871 1.00 75.45  ? 492  PHE B CD2 1 
ATOM   8518  C  CE1 . PHE B  1  466 ? 29.196  8.944   -12.082 1.00 74.46  ? 492  PHE B CE1 1 
ATOM   8519  C  CE2 . PHE B  1  466 ? 29.118  11.331  -11.881 1.00 75.97  ? 492  PHE B CE2 1 
ATOM   8520  C  CZ  . PHE B  1  466 ? 28.456  10.118  -11.989 1.00 75.32  ? 492  PHE B CZ  1 
ATOM   8521  N  N   . THR B  1  467 ? 35.431  10.403  -9.699  1.00 84.25  ? 493  THR B N   1 
ATOM   8522  C  CA  . THR B  1  467 ? 36.861  10.678  -9.601  1.00 85.80  ? 493  THR B CA  1 
ATOM   8523  C  C   . THR B  1  467 ? 37.832  9.489   -9.701  1.00 85.91  ? 493  THR B C   1 
ATOM   8524  O  O   . THR B  1  467 ? 39.040  9.685   -9.802  1.00 86.01  ? 493  THR B O   1 
ATOM   8525  C  CB  . THR B  1  467 ? 37.153  11.482  -8.295  1.00 87.43  ? 493  THR B CB  1 
ATOM   8526  O  OG1 . THR B  1  467 ? 36.597  10.796  -7.158  1.00 88.97  ? 493  THR B OG1 1 
ATOM   8527  C  CG2 . THR B  1  467 ? 36.537  12.891  -8.382  1.00 87.09  ? 493  THR B CG2 1 
ATOM   8528  N  N   . GLU B  1  468 ? 37.320  8.261   -9.680  1.00 86.74  ? 494  GLU B N   1 
ATOM   8529  C  CA  . GLU B  1  468 ? 38.188  7.082   -9.762  1.00 87.09  ? 494  GLU B CA  1 
ATOM   8530  C  C   . GLU B  1  468 ? 37.998  6.354   -11.098 1.00 86.22  ? 494  GLU B C   1 
ATOM   8531  O  O   . GLU B  1  468 ? 38.861  5.588   -11.525 1.00 84.52  ? 494  GLU B O   1 
ATOM   8532  C  CB  . GLU B  1  468 ? 37.897  6.121   -8.588  1.00 88.75  ? 494  GLU B CB  1 
ATOM   8533  C  CG  . GLU B  1  468 ? 39.067  5.161   -8.238  1.00 91.22  ? 494  GLU B CG  1 
ATOM   8534  C  CD  . GLU B  1  468 ? 38.755  4.169   -7.099  1.00 91.39  ? 494  GLU B CD  1 
ATOM   8535  O  OE1 . GLU B  1  468 ? 38.165  4.584   -6.072  1.00 92.34  ? 494  GLU B OE1 1 
ATOM   8536  O  OE2 . GLU B  1  468 ? 39.121  2.977   -7.223  1.00 89.35  ? 494  GLU B OE2 1 
ATOM   8537  N  N   . LEU B  1  469 ? 36.869  6.621   -11.752 1.00 86.12  ? 495  LEU B N   1 
ATOM   8538  C  CA  . LEU B  1  469 ? 36.518  6.008   -13.033 1.00 86.68  ? 495  LEU B CA  1 
ATOM   8539  C  C   . LEU B  1  469 ? 37.273  6.636   -14.204 1.00 87.97  ? 495  LEU B C   1 
ATOM   8540  O  O   . LEU B  1  469 ? 36.715  7.443   -14.947 1.00 87.75  ? 495  LEU B O   1 
ATOM   8541  C  CB  . LEU B  1  469 ? 35.015  6.158   -13.279 1.00 85.48  ? 495  LEU B CB  1 
ATOM   8542  C  CG  . LEU B  1  469 ? 34.048  5.868   -12.126 1.00 84.22  ? 495  LEU B CG  1 
ATOM   8543  C  CD1 . LEU B  1  469 ? 32.617  5.941   -12.640 1.00 83.34  ? 495  LEU B CD1 1 
ATOM   8544  C  CD2 . LEU B  1  469 ? 34.327  4.499   -11.540 1.00 83.80  ? 495  LEU B CD2 1 
ATOM   8545  N  N   . ARG B  1  470 ? 38.533  6.247   -14.381 1.00 89.60  ? 496  ARG B N   1 
ATOM   8546  C  CA  . ARG B  1  470 ? 39.369  6.806   -15.446 1.00 91.17  ? 496  ARG B CA  1 
ATOM   8547  C  C   . ARG B  1  470 ? 39.004  6.479   -16.901 1.00 90.28  ? 496  ARG B C   1 
ATOM   8548  O  O   . ARG B  1  470 ? 38.583  7.364   -17.653 1.00 90.40  ? 496  ARG B O   1 
ATOM   8549  C  CB  . ARG B  1  470 ? 40.842  6.451   -15.189 1.00 93.33  ? 496  ARG B CB  1 
ATOM   8550  C  CG  . ARG B  1  470 ? 41.576  7.490   -14.336 1.00 97.51  ? 496  ARG B CG  1 
ATOM   8551  C  CD  . ARG B  1  470 ? 41.593  8.845   -15.048 1.00 100.92 ? 496  ARG B CD  1 
ATOM   8552  N  NE  . ARG B  1  470 ? 42.145  9.939   -14.246 1.00 104.14 ? 496  ARG B NE  1 
ATOM   8553  C  CZ  . ARG B  1  470 ? 41.588  10.421  -13.136 1.00 105.47 ? 496  ARG B CZ  1 
ATOM   8554  N  NH1 . ARG B  1  470 ? 40.457  9.903   -12.678 1.00 106.08 ? 496  ARG B NH1 1 
ATOM   8555  N  NH2 . ARG B  1  470 ? 42.148  11.439  -12.491 1.00 105.74 ? 496  ARG B NH2 1 
ATOM   8556  N  N   . ASN B  1  471 ? 39.174  5.218   -17.294 1.00 88.75  ? 497  ASN B N   1 
ATOM   8557  C  CA  . ASN B  1  471 ? 38.884  4.776   -18.657 1.00 85.75  ? 497  ASN B CA  1 
ATOM   8558  C  C   . ASN B  1  471 ? 37.405  4.952   -19.032 1.00 83.24  ? 497  ASN B C   1 
ATOM   8559  O  O   . ASN B  1  471 ? 36.992  4.599   -20.130 1.00 82.02  ? 497  ASN B O   1 
ATOM   8560  C  CB  . ASN B  1  471 ? 39.283  3.299   -18.840 1.00 87.32  ? 497  ASN B CB  1 
ATOM   8561  C  CG  . ASN B  1  471 ? 40.688  2.979   -18.316 1.00 88.06  ? 497  ASN B CG  1 
ATOM   8562  O  OD1 . ASN B  1  471 ? 40.993  3.215   -17.148 1.00 89.43  ? 497  ASN B OD1 1 
ATOM   8563  N  ND2 . ASN B  1  471 ? 41.535  2.412   -19.170 1.00 88.20  ? 497  ASN B ND2 1 
ATOM   8564  N  N   . LEU B  1  472 ? 36.617  5.505   -18.118 1.00 81.14  ? 498  LEU B N   1 
ATOM   8565  C  CA  . LEU B  1  472 ? 35.187  5.724   -18.346 1.00 80.02  ? 498  LEU B CA  1 
ATOM   8566  C  C   . LEU B  1  472 ? 34.915  6.439   -19.690 1.00 78.64  ? 498  LEU B C   1 
ATOM   8567  O  O   . LEU B  1  472 ? 35.208  7.622   -19.833 1.00 79.00  ? 498  LEU B O   1 
ATOM   8568  C  CB  . LEU B  1  472 ? 34.622  6.539   -17.167 1.00 79.99  ? 498  LEU B CB  1 
ATOM   8569  C  CG  . LEU B  1  472 ? 33.222  6.299   -16.571 1.00 79.54  ? 498  LEU B CG  1 
ATOM   8570  C  CD1 . LEU B  1  472 ? 32.192  7.264   -17.160 1.00 77.56  ? 498  LEU B CD1 1 
ATOM   8571  C  CD2 . LEU B  1  472 ? 32.829  4.844   -16.791 1.00 78.88  ? 498  LEU B CD2 1 
ATOM   8572  N  N   . THR B  1  473 ? 34.342  5.721   -20.661 1.00 77.12  ? 499  THR B N   1 
ATOM   8573  C  CA  . THR B  1  473 ? 34.052  6.283   -21.989 1.00 75.65  ? 499  THR B CA  1 
ATOM   8574  C  C   . THR B  1  473 ? 32.583  6.570   -22.303 1.00 74.56  ? 499  THR B C   1 
ATOM   8575  O  O   . THR B  1  473 ? 32.284  7.287   -23.253 1.00 73.06  ? 499  THR B O   1 
ATOM   8576  C  CB  . THR B  1  473 ? 34.556  5.369   -23.124 1.00 75.99  ? 499  THR B CB  1 
ATOM   8577  O  OG1 . THR B  1  473 ? 33.531  4.428   -23.461 1.00 76.08  ? 499  THR B OG1 1 
ATOM   8578  C  CG2 . THR B  1  473 ? 35.820  4.615   -22.705 1.00 74.78  ? 499  THR B CG2 1 
ATOM   8579  N  N   . PHE B  1  474 ? 31.669  5.984   -21.538 1.00 75.05  ? 500  PHE B N   1 
ATOM   8580  C  CA  . PHE B  1  474 ? 30.232  6.207   -21.738 1.00 75.49  ? 500  PHE B CA  1 
ATOM   8581  C  C   . PHE B  1  474 ? 29.595  6.466   -20.370 1.00 75.04  ? 500  PHE B C   1 
ATOM   8582  O  O   . PHE B  1  474 ? 30.059  5.927   -19.365 1.00 76.65  ? 500  PHE B O   1 
ATOM   8583  C  CB  . PHE B  1  474 ? 29.586  4.973   -22.370 1.00 75.20  ? 500  PHE B CB  1 
ATOM   8584  C  CG  . PHE B  1  474 ? 28.225  5.227   -22.965 1.00 74.86  ? 500  PHE B CG  1 
ATOM   8585  C  CD1 . PHE B  1  474 ? 28.075  5.383   -24.338 1.00 74.83  ? 500  PHE B CD1 1 
ATOM   8586  C  CD2 . PHE B  1  474 ? 27.090  5.286   -22.158 1.00 75.12  ? 500  PHE B CD2 1 
ATOM   8587  C  CE1 . PHE B  1  474 ? 26.811  5.585   -24.903 1.00 74.89  ? 500  PHE B CE1 1 
ATOM   8588  C  CE2 . PHE B  1  474 ? 25.816  5.491   -22.712 1.00 74.26  ? 500  PHE B CE2 1 
ATOM   8589  C  CZ  . PHE B  1  474 ? 25.676  5.640   -24.085 1.00 74.29  ? 500  PHE B CZ  1 
ATOM   8590  N  N   . LEU B  1  475 ? 28.544  7.280   -20.317 1.00 72.42  ? 501  LEU B N   1 
ATOM   8591  C  CA  . LEU B  1  475 ? 27.907  7.557   -19.040 1.00 71.14  ? 501  LEU B CA  1 
ATOM   8592  C  C   . LEU B  1  475 ? 26.515  8.127   -19.194 1.00 71.28  ? 501  LEU B C   1 
ATOM   8593  O  O   . LEU B  1  475 ? 26.354  9.317   -19.466 1.00 71.19  ? 501  LEU B O   1 
ATOM   8594  C  CB  . LEU B  1  475 ? 28.773  8.515   -18.211 1.00 71.74  ? 501  LEU B CB  1 
ATOM   8595  C  CG  . LEU B  1  475 ? 28.241  9.151   -16.911 1.00 71.89  ? 501  LEU B CG  1 
ATOM   8596  C  CD1 . LEU B  1  475 ? 27.864  8.101   -15.897 1.00 71.89  ? 501  LEU B CD1 1 
ATOM   8597  C  CD2 . LEU B  1  475 ? 29.302  10.052  -16.326 1.00 72.68  ? 501  LEU B CD2 1 
ATOM   8598  N  N   . ASP B  1  476 ? 25.513  7.263   -19.030 1.00 71.25  ? 502  ASP B N   1 
ATOM   8599  C  CA  . ASP B  1  476 ? 24.117  7.677   -19.122 1.00 71.05  ? 502  ASP B CA  1 
ATOM   8600  C  C   . ASP B  1  476 ? 23.780  8.170   -17.729 1.00 71.39  ? 502  ASP B C   1 
ATOM   8601  O  O   . ASP B  1  476 ? 24.164  7.545   -16.747 1.00 72.03  ? 502  ASP B O   1 
ATOM   8602  C  CB  . ASP B  1  476 ? 23.208  6.497   -19.482 1.00 70.32  ? 502  ASP B CB  1 
ATOM   8603  C  CG  . ASP B  1  476 ? 21.782  6.932   -19.799 1.00 71.18  ? 502  ASP B CG  1 
ATOM   8604  O  OD1 . ASP B  1  476 ? 21.317  7.941   -19.214 1.00 70.39  ? 502  ASP B OD1 1 
ATOM   8605  O  OD2 . ASP B  1  476 ? 21.117  6.261   -20.622 1.00 70.09  ? 502  ASP B OD2 1 
ATOM   8606  N  N   . LEU B  1  477 ? 23.079  9.296   -17.647 1.00 71.88  ? 503  LEU B N   1 
ATOM   8607  C  CA  . LEU B  1  477 ? 22.693  9.895   -16.373 1.00 71.45  ? 503  LEU B CA  1 
ATOM   8608  C  C   . LEU B  1  477 ? 21.346  10.555  -16.561 1.00 71.02  ? 503  LEU B C   1 
ATOM   8609  O  O   . LEU B  1  477 ? 21.018  11.513  -15.866 1.00 71.84  ? 503  LEU B O   1 
ATOM   8610  C  CB  . LEU B  1  477 ? 23.727  10.950  -15.934 1.00 71.30  ? 503  LEU B CB  1 
ATOM   8611  C  CG  . LEU B  1  477 ? 24.866  10.510  -15.007 1.00 73.41  ? 503  LEU B CG  1 
ATOM   8612  C  CD1 . LEU B  1  477 ? 26.062  11.451  -15.094 1.00 72.85  ? 503  LEU B CD1 1 
ATOM   8613  C  CD2 . LEU B  1  477 ? 24.324  10.448  -13.588 1.00 74.85  ? 503  LEU B CD2 1 
ATOM   8614  N  N   . SER B  1  478 ? 20.563  10.045  -17.505 1.00 70.20  ? 504  SER B N   1 
ATOM   8615  C  CA  . SER B  1  478 ? 19.257  10.627  -17.765 1.00 70.89  ? 504  SER B CA  1 
ATOM   8616  C  C   . SER B  1  478 ? 18.203  10.249  -16.732 1.00 71.03  ? 504  SER B C   1 
ATOM   8617  O  O   . SER B  1  478 ? 18.436  9.430   -15.856 1.00 70.22  ? 504  SER B O   1 
ATOM   8618  C  CB  . SER B  1  478 ? 18.779  10.247  -19.166 1.00 70.32  ? 504  SER B CB  1 
ATOM   8619  O  OG  . SER B  1  478 ? 18.573  8.858   -19.283 1.00 70.80  ? 504  SER B OG  1 
ATOM   8620  N  N   . GLN B  1  479 ? 17.047  10.886  -16.833 1.00 72.93  ? 505  GLN B N   1 
ATOM   8621  C  CA  . GLN B  1  479 ? 15.929  10.643  -15.933 1.00 75.43  ? 505  GLN B CA  1 
ATOM   8622  C  C   . GLN B  1  479 ? 16.249  10.581  -14.428 1.00 76.78  ? 505  GLN B C   1 
ATOM   8623  O  O   . GLN B  1  479 ? 15.454  10.051  -13.645 1.00 78.25  ? 505  GLN B O   1 
ATOM   8624  C  CB  . GLN B  1  479 ? 15.210  9.370   -16.376 1.00 75.45  ? 505  GLN B CB  1 
ATOM   8625  C  CG  . GLN B  1  479 ? 14.982  9.340   -17.872 1.00 78.41  ? 505  GLN B CG  1 
ATOM   8626  C  CD  . GLN B  1  479 ? 13.971  8.304   -18.302 1.00 79.67  ? 505  GLN B CD  1 
ATOM   8627  O  OE1 . GLN B  1  479 ? 12.855  8.265   -17.780 1.00 81.03  ? 505  GLN B OE1 1 
ATOM   8628  N  NE2 . GLN B  1  479 ? 14.347  7.467   -19.272 1.00 78.64  ? 505  GLN B NE2 1 
ATOM   8629  N  N   . CYS B  1  480 ? 17.389  11.132  -14.011 1.00 77.64  ? 506  CYS B N   1 
ATOM   8630  C  CA  . CYS B  1  480 ? 17.763  11.129  -12.592 1.00 77.99  ? 506  CYS B CA  1 
ATOM   8631  C  C   . CYS B  1  480 ? 17.328  12.338  -11.758 1.00 78.47  ? 506  CYS B C   1 
ATOM   8632  O  O   . CYS B  1  480 ? 17.918  12.609  -10.715 1.00 78.32  ? 506  CYS B O   1 
ATOM   8633  C  CB  . CYS B  1  480 ? 19.263  10.980  -12.448 1.00 77.59  ? 506  CYS B CB  1 
ATOM   8634  S  SG  . CYS B  1  480 ? 19.832  9.442   -13.087 1.00 80.56  ? 506  CYS B SG  1 
ATOM   8635  N  N   . GLN B  1  481 ? 16.305  13.058  -12.209 1.00 79.07  ? 507  GLN B N   1 
ATOM   8636  C  CA  . GLN B  1  481 ? 15.791  14.221  -11.481 1.00 79.55  ? 507  GLN B CA  1 
ATOM   8637  C  C   . GLN B  1  481 ? 16.859  15.258  -11.071 1.00 80.38  ? 507  GLN B C   1 
ATOM   8638  O  O   . GLN B  1  481 ? 16.598  16.107  -10.211 1.00 79.39  ? 507  GLN B O   1 
ATOM   8639  C  CB  . GLN B  1  481 ? 15.024  13.754  -10.230 1.00 78.69  ? 507  GLN B CB  1 
ATOM   8640  C  CG  . GLN B  1  481 ? 13.993  12.653  -10.487 1.00 75.86  ? 507  GLN B CG  1 
ATOM   8641  C  CD  . GLN B  1  481 ? 13.045  12.423  -9.314  1.00 73.68  ? 507  GLN B CD  1 
ATOM   8642  O  OE1 . GLN B  1  481 ? 12.227  13.276  -8.983  1.00 70.50  ? 507  GLN B OE1 1 
ATOM   8643  N  NE2 . GLN B  1  481 ? 13.156  11.266  -8.688  1.00 73.98  ? 507  GLN B NE2 1 
ATOM   8644  N  N   . LEU B  1  482 ? 18.042  15.189  -11.689 1.00 80.72  ? 508  LEU B N   1 
ATOM   8645  C  CA  . LEU B  1  482 ? 19.135  16.112  -11.395 1.00 80.51  ? 508  LEU B CA  1 
ATOM   8646  C  C   . LEU B  1  482 ? 18.758  17.567  -11.643 1.00 82.76  ? 508  LEU B C   1 
ATOM   8647  O  O   . LEU B  1  482 ? 18.117  17.892  -12.644 1.00 82.78  ? 508  LEU B O   1 
ATOM   8648  C  CB  . LEU B  1  482 ? 20.358  15.769  -12.237 1.00 77.96  ? 508  LEU B CB  1 
ATOM   8649  C  CG  . LEU B  1  482 ? 21.277  14.678  -11.708 1.00 78.19  ? 508  LEU B CG  1 
ATOM   8650  C  CD1 . LEU B  1  482 ? 22.393  14.426  -12.694 1.00 77.97  ? 508  LEU B CD1 1 
ATOM   8651  C  CD2 . LEU B  1  482 ? 21.858  15.103  -10.373 1.00 79.42  ? 508  LEU B CD2 1 
ATOM   8652  N  N   . GLU B  1  483 ? 19.165  18.439  -10.720 1.00 85.06  ? 509  GLU B N   1 
ATOM   8653  C  CA  . GLU B  1  483 ? 18.903  19.879  -10.800 1.00 86.14  ? 509  GLU B CA  1 
ATOM   8654  C  C   . GLU B  1  483 ? 20.213  20.672  -10.735 1.00 86.06  ? 509  GLU B C   1 
ATOM   8655  O  O   . GLU B  1  483 ? 20.564  21.386  -11.672 1.00 85.37  ? 509  GLU B O   1 
ATOM   8656  C  CB  . GLU B  1  483 ? 17.962  20.307  -9.663  1.00 86.73  ? 509  GLU B CB  1 
ATOM   8657  C  CG  . GLU B  1  483 ? 16.487  19.947  -9.906  1.00 88.88  ? 509  GLU B CG  1 
ATOM   8658  C  CD  . GLU B  1  483 ? 15.576  20.293  -8.727  1.00 90.11  ? 509  GLU B CD  1 
ATOM   8659  O  OE1 . GLU B  1  483 ? 14.332  20.239  -8.887  1.00 88.85  ? 509  GLU B OE1 1 
ATOM   8660  O  OE2 . GLU B  1  483 ? 16.104  20.608  -7.638  1.00 91.81  ? 509  GLU B OE2 1 
ATOM   8661  N  N   . GLN B  1  484 ? 20.932  20.536  -9.626  1.00 87.45  ? 510  GLN B N   1 
ATOM   8662  C  CA  . GLN B  1  484 ? 22.208  21.225  -9.446  1.00 88.64  ? 510  GLN B CA  1 
ATOM   8663  C  C   . GLN B  1  484 ? 23.300  20.348  -10.049 1.00 87.47  ? 510  GLN B C   1 
ATOM   8664  O  O   . GLN B  1  484 ? 23.005  19.338  -10.680 1.00 86.54  ? 510  GLN B O   1 
ATOM   8665  C  CB  . GLN B  1  484 ? 22.516  21.468  -7.954  1.00 91.98  ? 510  GLN B CB  1 
ATOM   8666  C  CG  . GLN B  1  484 ? 21.441  22.228  -7.149  1.00 95.54  ? 510  GLN B CG  1 
ATOM   8667  C  CD  . GLN B  1  484 ? 20.856  23.416  -7.909  1.00 98.14  ? 510  GLN B CD  1 
ATOM   8668  O  OE1 . GLN B  1  484 ? 21.572  24.121  -8.631  1.00 98.86  ? 510  GLN B OE1 1 
ATOM   8669  N  NE2 . GLN B  1  484 ? 19.549  23.643  -7.748  1.00 97.88  ? 510  GLN B NE2 1 
ATOM   8670  N  N   . LEU B  1  485 ? 24.557  20.727  -9.842  1.00 86.78  ? 511  LEU B N   1 
ATOM   8671  C  CA  . LEU B  1  485 ? 25.669  19.975  -10.404 1.00 86.00  ? 511  LEU B CA  1 
ATOM   8672  C  C   . LEU B  1  485 ? 27.008  20.430  -9.833  1.00 85.92  ? 511  LEU B C   1 
ATOM   8673  O  O   . LEU B  1  485 ? 27.297  21.620  -9.767  1.00 86.43  ? 511  LEU B O   1 
ATOM   8674  C  CB  . LEU B  1  485 ? 25.663  20.153  -11.923 1.00 85.11  ? 511  LEU B CB  1 
ATOM   8675  C  CG  . LEU B  1  485 ? 26.348  19.123  -12.816 1.00 84.90  ? 511  LEU B CG  1 
ATOM   8676  C  CD1 . LEU B  1  485 ? 25.940  19.361  -14.258 1.00 84.83  ? 511  LEU B CD1 1 
ATOM   8677  C  CD2 . LEU B  1  485 ? 27.849  19.207  -12.656 1.00 84.37  ? 511  LEU B CD2 1 
ATOM   8678  N  N   . SER B  1  486 ? 27.822  19.474  -9.409  1.00 86.13  ? 512  SER B N   1 
ATOM   8679  C  CA  . SER B  1  486 ? 29.132  19.787  -8.864  1.00 86.81  ? 512  SER B CA  1 
ATOM   8680  C  C   . SER B  1  486 ? 30.044  20.115  -10.030 1.00 88.12  ? 512  SER B C   1 
ATOM   8681  O  O   . SER B  1  486 ? 30.154  19.347  -10.974 1.00 87.73  ? 512  SER B O   1 
ATOM   8682  C  CB  . SER B  1  486 ? 29.696  18.593  -8.090  1.00 85.97  ? 512  SER B CB  1 
ATOM   8683  O  OG  . SER B  1  486 ? 31.103  18.690  -7.947  1.00 82.96  ? 512  SER B OG  1 
ATOM   8684  N  N   . PRO B  1  487 ? 30.709  21.269  -9.981  1.00 89.91  ? 513  PRO B N   1 
ATOM   8685  C  CA  . PRO B  1  487 ? 31.607  21.664  -11.063 1.00 90.89  ? 513  PRO B CA  1 
ATOM   8686  C  C   . PRO B  1  487 ? 32.838  20.772  -11.207 1.00 91.70  ? 513  PRO B C   1 
ATOM   8687  O  O   . PRO B  1  487 ? 33.460  20.741  -12.267 1.00 92.34  ? 513  PRO B O   1 
ATOM   8688  C  CB  . PRO B  1  487 ? 31.972  23.092  -10.686 1.00 91.27  ? 513  PRO B CB  1 
ATOM   8689  C  CG  . PRO B  1  487 ? 32.010  23.020  -9.190  1.00 91.35  ? 513  PRO B CG  1 
ATOM   8690  C  CD  . PRO B  1  487 ? 30.738  22.260  -8.890  1.00 90.83  ? 513  PRO B CD  1 
ATOM   8691  N  N   . THR B  1  488 ? 33.187  20.035  -10.158 1.00 92.36  ? 514  THR B N   1 
ATOM   8692  C  CA  . THR B  1  488 ? 34.367  19.169  -10.213 1.00 93.83  ? 514  THR B CA  1 
ATOM   8693  C  C   . THR B  1  488 ? 34.068  17.718  -10.631 1.00 94.77  ? 514  THR B C   1 
ATOM   8694  O  O   . THR B  1  488 ? 34.988  16.916  -10.805 1.00 95.46  ? 514  THR B O   1 
ATOM   8695  C  CB  . THR B  1  488 ? 35.073  19.133  -8.849  1.00 94.57  ? 514  THR B CB  1 
ATOM   8696  O  OG1 . THR B  1  488 ? 34.863  20.378  -8.170  1.00 95.74  ? 514  THR B OG1 1 
ATOM   8697  C  CG2 . THR B  1  488 ? 36.569  18.902  -9.029  1.00 93.85  ? 514  THR B CG2 1 
ATOM   8698  N  N   . ALA B  1  489 ? 32.786  17.394  -10.790 1.00 94.69  ? 515  ALA B N   1 
ATOM   8699  C  CA  . ALA B  1  489 ? 32.335  16.055  -11.169 1.00 93.50  ? 515  ALA B CA  1 
ATOM   8700  C  C   . ALA B  1  489 ? 33.164  15.343  -12.232 1.00 93.32  ? 515  ALA B C   1 
ATOM   8701  O  O   . ALA B  1  489 ? 34.079  14.581  -11.926 1.00 93.41  ? 515  ALA B O   1 
ATOM   8702  C  CB  . ALA B  1  489 ? 30.885  16.118  -11.615 1.00 92.29  ? 515  ALA B CB  1 
ATOM   8703  N  N   . PHE B  1  490 ? 32.825  15.599  -13.487 1.00 93.95  ? 516  PHE B N   1 
ATOM   8704  C  CA  . PHE B  1  490 ? 33.475  14.984  -14.644 1.00 95.38  ? 516  PHE B CA  1 
ATOM   8705  C  C   . PHE B  1  490 ? 34.967  15.300  -14.846 1.00 96.48  ? 516  PHE B C   1 
ATOM   8706  O  O   . PHE B  1  490 ? 35.623  14.682  -15.676 1.00 95.69  ? 516  PHE B O   1 
ATOM   8707  C  CB  . PHE B  1  490 ? 32.711  15.380  -15.916 1.00 94.42  ? 516  PHE B CB  1 
ATOM   8708  C  CG  . PHE B  1  490 ? 31.208  15.387  -15.756 1.00 93.95  ? 516  PHE B CG  1 
ATOM   8709  C  CD1 . PHE B  1  490 ? 30.456  16.469  -16.209 1.00 93.42  ? 516  PHE B CD1 1 
ATOM   8710  C  CD2 . PHE B  1  490 ? 30.541  14.311  -15.174 1.00 93.61  ? 516  PHE B CD2 1 
ATOM   8711  C  CE1 . PHE B  1  490 ? 29.059  16.485  -16.085 1.00 93.51  ? 516  PHE B CE1 1 
ATOM   8712  C  CE2 . PHE B  1  490 ? 29.142  14.314  -15.044 1.00 94.10  ? 516  PHE B CE2 1 
ATOM   8713  C  CZ  . PHE B  1  490 ? 28.396  15.407  -15.503 1.00 93.39  ? 516  PHE B CZ  1 
ATOM   8714  N  N   . ASN B  1  491 ? 35.502  16.244  -14.083 1.00 98.82  ? 517  ASN B N   1 
ATOM   8715  C  CA  . ASN B  1  491 ? 36.901  16.672  -14.212 1.00 100.45 ? 517  ASN B CA  1 
ATOM   8716  C  C   . ASN B  1  491 ? 38.029  15.648  -14.339 1.00 99.86  ? 517  ASN B C   1 
ATOM   8717  O  O   . ASN B  1  491 ? 39.165  16.028  -14.624 1.00 100.18 ? 517  ASN B O   1 
ATOM   8718  C  CB  . ASN B  1  491 ? 37.247  17.635  -13.070 1.00 102.95 ? 517  ASN B CB  1 
ATOM   8719  C  CG  . ASN B  1  491 ? 36.620  19.000  -13.259 1.00 105.69 ? 517  ASN B CG  1 
ATOM   8720  O  OD1 . ASN B  1  491 ? 36.603  19.821  -12.337 1.00 106.00 ? 517  ASN B OD1 1 
ATOM   8721  N  ND2 . ASN B  1  491 ? 36.103  19.254  -14.466 1.00 106.51 ? 517  ASN B ND2 1 
ATOM   8722  N  N   . SER B  1  492 ? 37.748  14.370  -14.129 1.00 98.52  ? 518  SER B N   1 
ATOM   8723  C  CA  . SER B  1  492 ? 38.803  13.366  -14.232 1.00 96.86  ? 518  SER B CA  1 
ATOM   8724  C  C   . SER B  1  492 ? 38.547  12.416  -15.391 1.00 95.76  ? 518  SER B C   1 
ATOM   8725  O  O   . SER B  1  492 ? 39.394  11.586  -15.734 1.00 94.09  ? 518  SER B O   1 
ATOM   8726  C  CB  . SER B  1  492 ? 38.931  12.588  -12.906 1.00 97.45  ? 518  SER B CB  1 
ATOM   8727  O  OG  . SER B  1  492 ? 37.665  12.295  -12.330 1.00 96.98  ? 518  SER B OG  1 
ATOM   8728  N  N   . LEU B  1  493 ? 37.372  12.569  -15.999 1.00 95.14  ? 519  LEU B N   1 
ATOM   8729  C  CA  . LEU B  1  493 ? 36.930  11.732  -17.118 1.00 94.24  ? 519  LEU B CA  1 
ATOM   8730  C  C   . LEU B  1  493 ? 37.507  12.206  -18.448 1.00 92.95  ? 519  LEU B C   1 
ATOM   8731  O  O   . LEU B  1  493 ? 36.792  12.747  -19.303 1.00 92.02  ? 519  LEU B O   1 
ATOM   8732  C  CB  . LEU B  1  493 ? 35.398  11.733  -17.193 1.00 93.90  ? 519  LEU B CB  1 
ATOM   8733  C  CG  . LEU B  1  493 ? 34.651  11.506  -15.874 1.00 93.30  ? 519  LEU B CG  1 
ATOM   8734  C  CD1 . LEU B  1  493 ? 33.149  11.665  -16.080 1.00 92.17  ? 519  LEU B CD1 1 
ATOM   8735  C  CD2 . LEU B  1  493 ? 34.999  10.130  -15.332 1.00 93.18  ? 519  LEU B CD2 1 
ATOM   8736  N  N   . SER B  1  494 ? 38.806  11.989  -18.618 1.00 91.92  ? 520  SER B N   1 
ATOM   8737  C  CA  . SER B  1  494 ? 39.498  12.401  -19.829 1.00 90.60  ? 520  SER B CA  1 
ATOM   8738  C  C   . SER B  1  494 ? 39.052  11.620  -21.061 1.00 90.12  ? 520  SER B C   1 
ATOM   8739  O  O   . SER B  1  494 ? 38.843  12.207  -22.124 1.00 91.31  ? 520  SER B O   1 
ATOM   8740  C  CB  . SER B  1  494 ? 41.008  12.255  -19.632 1.00 89.69  ? 520  SER B CB  1 
ATOM   8741  O  OG  . SER B  1  494 ? 41.320  10.969  -19.125 1.00 89.10  ? 520  SER B OG  1 
ATOM   8742  N  N   . SER B  1  495 ? 38.890  10.306  -20.921 1.00 87.88  ? 521  SER B N   1 
ATOM   8743  C  CA  . SER B  1  495 ? 38.479  9.471   -22.050 1.00 84.15  ? 521  SER B CA  1 
ATOM   8744  C  C   . SER B  1  495 ? 36.983  9.497   -22.355 1.00 82.67  ? 521  SER B C   1 
ATOM   8745  O  O   . SER B  1  495 ? 36.549  8.989   -23.380 1.00 81.10  ? 521  SER B O   1 
ATOM   8746  C  CB  . SER B  1  495 ? 38.919  8.025   -21.823 1.00 83.05  ? 521  SER B CB  1 
ATOM   8747  O  OG  . SER B  1  495 ? 40.328  7.926   -21.809 1.00 82.18  ? 521  SER B OG  1 
ATOM   8748  N  N   . LEU B  1  496 ? 36.195  10.098  -21.474 1.00 81.97  ? 522  LEU B N   1 
ATOM   8749  C  CA  . LEU B  1  496 ? 34.753  10.150  -21.676 1.00 81.28  ? 522  LEU B CA  1 
ATOM   8750  C  C   . LEU B  1  496 ? 34.409  10.709  -23.050 1.00 79.99  ? 522  LEU B C   1 
ATOM   8751  O  O   . LEU B  1  496 ? 34.883  11.783  -23.410 1.00 80.79  ? 522  LEU B O   1 
ATOM   8752  C  CB  . LEU B  1  496 ? 34.087  11.011  -20.597 1.00 81.98  ? 522  LEU B CB  1 
ATOM   8753  C  CG  . LEU B  1  496 ? 32.561  10.860  -20.535 1.00 81.85  ? 522  LEU B CG  1 
ATOM   8754  C  CD1 . LEU B  1  496 ? 32.243  9.486   -19.951 1.00 81.10  ? 522  LEU B CD1 1 
ATOM   8755  C  CD2 . LEU B  1  496 ? 31.931  11.967  -19.692 1.00 82.35  ? 522  LEU B CD2 1 
ATOM   8756  N  N   . GLN B  1  497 ? 33.582  9.974   -23.799 1.00 78.53  ? 523  GLN B N   1 
ATOM   8757  C  CA  . GLN B  1  497 ? 33.144  10.367  -25.145 1.00 77.26  ? 523  GLN B CA  1 
ATOM   8758  C  C   . GLN B  1  497 ? 31.670  10.783  -25.202 1.00 77.75  ? 523  GLN B C   1 
ATOM   8759  O  O   . GLN B  1  497 ? 31.335  11.849  -25.723 1.00 78.46  ? 523  GLN B O   1 
ATOM   8760  C  CB  . GLN B  1  497 ? 33.380  9.225   -26.133 1.00 74.16  ? 523  GLN B CB  1 
ATOM   8761  C  CG  . GLN B  1  497 ? 34.785  8.674   -26.088 1.00 72.27  ? 523  GLN B CG  1 
ATOM   8762  C  CD  . GLN B  1  497 ? 35.000  7.552   -27.082 1.00 71.52  ? 523  GLN B CD  1 
ATOM   8763  O  OE1 . GLN B  1  497 ? 36.070  6.931   -27.124 1.00 70.66  ? 523  GLN B OE1 1 
ATOM   8764  N  NE2 . GLN B  1  497 ? 33.982  7.281   -27.887 1.00 69.47  ? 523  GLN B NE2 1 
ATOM   8765  N  N   . VAL B  1  498 ? 30.783  9.938   -24.692 1.00 78.08  ? 524  VAL B N   1 
ATOM   8766  C  CA  . VAL B  1  498 ? 29.364  10.281  -24.684 1.00 77.56  ? 524  VAL B CA  1 
ATOM   8767  C  C   . VAL B  1  498 ? 28.983  10.654  -23.248 1.00 77.75  ? 524  VAL B C   1 
ATOM   8768  O  O   . VAL B  1  498 ? 29.687  10.300  -22.293 1.00 78.58  ? 524  VAL B O   1 
ATOM   8769  C  CB  . VAL B  1  498 ? 28.484  9.102   -25.146 1.00 76.49  ? 524  VAL B CB  1 
ATOM   8770  C  CG1 . VAL B  1  498 ? 27.093  9.599   -25.518 1.00 73.88  ? 524  VAL B CG1 1 
ATOM   8771  C  CG2 . VAL B  1  498 ? 29.128  8.415   -26.320 1.00 76.08  ? 524  VAL B CG2 1 
ATOM   8772  N  N   . LEU B  1  499 ? 27.887  11.385  -23.099 1.00 75.81  ? 525  LEU B N   1 
ATOM   8773  C  CA  . LEU B  1  499 ? 27.439  11.780  -21.778 1.00 75.98  ? 525  LEU B CA  1 
ATOM   8774  C  C   . LEU B  1  499 ? 25.991  12.224  -21.873 1.00 75.62  ? 525  LEU B C   1 
ATOM   8775  O  O   . LEU B  1  499 ? 25.697  13.361  -22.239 1.00 74.92  ? 525  LEU B O   1 
ATOM   8776  C  CB  . LEU B  1  499 ? 28.336  12.903  -21.225 1.00 77.29  ? 525  LEU B CB  1 
ATOM   8777  C  CG  . LEU B  1  499 ? 27.943  13.641  -19.934 1.00 77.38  ? 525  LEU B CG  1 
ATOM   8778  C  CD1 . LEU B  1  499 ? 27.521  12.674  -18.847 1.00 77.77  ? 525  LEU B CD1 1 
ATOM   8779  C  CD2 . LEU B  1  499 ? 29.124  14.470  -19.479 1.00 77.19  ? 525  LEU B CD2 1 
ATOM   8780  N  N   . ASN B  1  500 ? 25.091  11.301  -21.552 1.00 75.58  ? 526  ASN B N   1 
ATOM   8781  C  CA  . ASN B  1  500 ? 23.659  11.560  -21.599 1.00 75.88  ? 526  ASN B CA  1 
ATOM   8782  C  C   . ASN B  1  500 ? 23.257  12.263  -20.303 1.00 76.83  ? 526  ASN B C   1 
ATOM   8783  O  O   . ASN B  1  500 ? 23.693  11.869  -19.220 1.00 77.94  ? 526  ASN B O   1 
ATOM   8784  C  CB  . ASN B  1  500 ? 22.897  10.239  -21.731 1.00 75.45  ? 526  ASN B CB  1 
ATOM   8785  C  CG  . ASN B  1  500 ? 21.490  10.420  -22.288 1.00 77.36  ? 526  ASN B CG  1 
ATOM   8786  O  OD1 . ASN B  1  500 ? 20.799  11.393  -21.956 1.00 76.86  ? 526  ASN B OD1 1 
ATOM   8787  N  ND2 . ASN B  1  500 ? 21.062  9.470   -23.125 1.00 78.35  ? 526  ASN B ND2 1 
ATOM   8788  N  N   . MET B  1  501 ? 22.449  13.313  -20.424 1.00 76.22  ? 527  MET B N   1 
ATOM   8789  C  CA  . MET B  1  501 ? 21.970  14.078  -19.276 1.00 75.04  ? 527  MET B CA  1 
ATOM   8790  C  C   . MET B  1  501 ? 20.559  14.448  -19.661 1.00 74.64  ? 527  MET B C   1 
ATOM   8791  O  O   . MET B  1  501 ? 19.985  15.409  -19.162 1.00 74.43  ? 527  MET B O   1 
ATOM   8792  C  CB  . MET B  1  501 ? 22.788  15.356  -19.069 1.00 74.30  ? 527  MET B CB  1 
ATOM   8793  C  CG  . MET B  1  501 ? 24.264  15.156  -18.745 1.00 75.66  ? 527  MET B CG  1 
ATOM   8794  S  SD  . MET B  1  501 ? 24.631  14.737  -17.017 1.00 79.28  ? 527  MET B SD  1 
ATOM   8795  C  CE  . MET B  1  501 ? 23.869  16.095  -16.125 1.00 77.97  ? 527  MET B CE  1 
ATOM   8796  N  N   . SER B  1  502 ? 20.011  13.664  -20.572 1.00 74.62  ? 528  SER B N   1 
ATOM   8797  C  CA  . SER B  1  502 ? 18.667  13.893  -21.058 1.00 76.39  ? 528  SER B CA  1 
ATOM   8798  C  C   . SER B  1  502 ? 17.600  13.866  -19.967 1.00 77.68  ? 528  SER B C   1 
ATOM   8799  O  O   . SER B  1  502 ? 17.878  13.660  -18.792 1.00 75.69  ? 528  SER B O   1 
ATOM   8800  C  CB  . SER B  1  502 ? 18.332  12.862  -22.139 1.00 75.03  ? 528  SER B CB  1 
ATOM   8801  O  OG  . SER B  1  502 ? 16.945  12.863  -22.424 1.00 75.14  ? 528  SER B OG  1 
ATOM   8802  N  N   . HIS B  1  503 ? 16.368  14.080  -20.399 1.00 81.73  ? 529  HIS B N   1 
ATOM   8803  C  CA  . HIS B  1  503 ? 15.182  14.095  -19.552 1.00 86.45  ? 529  HIS B CA  1 
ATOM   8804  C  C   . HIS B  1  503 ? 15.371  14.293  -18.037 1.00 88.39  ? 529  HIS B C   1 
ATOM   8805  O  O   . HIS B  1  503 ? 14.789  13.562  -17.232 1.00 89.59  ? 529  HIS B O   1 
ATOM   8806  C  CB  . HIS B  1  503 ? 14.366  12.829  -19.834 1.00 86.85  ? 529  HIS B CB  1 
ATOM   8807  C  CG  . HIS B  1  503 ? 12.916  12.962  -19.494 1.00 89.12  ? 529  HIS B CG  1 
ATOM   8808  N  ND1 . HIS B  1  503 ? 11.948  12.141  -20.035 1.00 91.08  ? 529  HIS B ND1 1 
ATOM   8809  C  CD2 . HIS B  1  503 ? 12.267  13.807  -18.656 1.00 89.59  ? 529  HIS B CD2 1 
ATOM   8810  C  CE1 . HIS B  1  503 ? 10.766  12.474  -19.545 1.00 91.90  ? 529  HIS B CE1 1 
ATOM   8811  N  NE2 . HIS B  1  503 ? 10.932  13.482  -18.705 1.00 91.47  ? 529  HIS B NE2 1 
ATOM   8812  N  N   . ASN B  1  504 ? 16.167  15.293  -17.656 1.00 89.66  ? 530  ASN B N   1 
ATOM   8813  C  CA  . ASN B  1  504 ? 16.405  15.611  -16.247 1.00 90.19  ? 530  ASN B CA  1 
ATOM   8814  C  C   . ASN B  1  504 ? 15.574  16.830  -15.844 1.00 91.38  ? 530  ASN B C   1 
ATOM   8815  O  O   . ASN B  1  504 ? 14.543  17.129  -16.457 1.00 90.41  ? 530  ASN B O   1 
ATOM   8816  C  CB  . ASN B  1  504 ? 17.887  15.911  -16.003 1.00 88.85  ? 530  ASN B CB  1 
ATOM   8817  C  CG  . ASN B  1  504 ? 18.648  14.714  -15.473 1.00 87.83  ? 530  ASN B CG  1 
ATOM   8818  O  OD1 . ASN B  1  504 ? 18.244  14.097  -14.495 1.00 88.32  ? 530  ASN B OD1 1 
ATOM   8819  N  ND2 . ASN B  1  504 ? 19.764  14.394  -16.105 1.00 86.70  ? 530  ASN B ND2 1 
ATOM   8820  N  N   . ASN B  1  505 ? 16.022  17.526  -14.804 1.00 93.57  ? 531  ASN B N   1 
ATOM   8821  C  CA  . ASN B  1  505 ? 15.331  18.717  -14.339 1.00 96.19  ? 531  ASN B CA  1 
ATOM   8822  C  C   . ASN B  1  505 ? 16.252  19.918  -14.165 1.00 98.69  ? 531  ASN B C   1 
ATOM   8823  O  O   . ASN B  1  505 ? 16.222  20.594  -13.133 1.00 99.69  ? 531  ASN B O   1 
ATOM   8824  C  CB  . ASN B  1  505 ? 14.584  18.443  -13.036 1.00 94.97  ? 531  ASN B CB  1 
ATOM   8825  C  CG  . ASN B  1  505 ? 13.306  17.670  -13.262 1.00 95.03  ? 531  ASN B CG  1 
ATOM   8826  O  OD1 . ASN B  1  505 ? 12.526  17.983  -14.170 1.00 93.78  ? 531  ASN B OD1 1 
ATOM   8827  N  ND2 . ASN B  1  505 ? 13.073  16.657  -12.429 1.00 95.21  ? 531  ASN B ND2 1 
ATOM   8828  N  N   . PHE B  1  506 ? 17.083  20.165  -15.176 1.00 100.78 ? 532  PHE B N   1 
ATOM   8829  C  CA  . PHE B  1  506 ? 17.985  21.306  -15.181 1.00 101.87 ? 532  PHE B CA  1 
ATOM   8830  C  C   . PHE B  1  506 ? 17.213  22.493  -15.752 1.00 103.60 ? 532  PHE B C   1 
ATOM   8831  O  O   . PHE B  1  506 ? 16.372  22.323  -16.641 1.00 102.63 ? 532  PHE B O   1 
ATOM   8832  C  CB  . PHE B  1  506 ? 19.192  21.045  -16.080 1.00 101.49 ? 532  PHE B CB  1 
ATOM   8833  C  CG  . PHE B  1  506 ? 20.253  20.205  -15.453 1.00 101.30 ? 532  PHE B CG  1 
ATOM   8834  C  CD1 . PHE B  1  506 ? 20.071  18.842  -15.280 1.00 101.34 ? 532  PHE B CD1 1 
ATOM   8835  C  CD2 . PHE B  1  506 ? 21.449  20.783  -15.044 1.00 101.62 ? 532  PHE B CD2 1 
ATOM   8836  C  CE1 . PHE B  1  506 ? 21.076  18.062  -14.707 1.00 102.46 ? 532  PHE B CE1 1 
ATOM   8837  C  CE2 . PHE B  1  506 ? 22.461  20.019  -14.471 1.00 101.85 ? 532  PHE B CE2 1 
ATOM   8838  C  CZ  . PHE B  1  506 ? 22.280  18.654  -14.299 1.00 101.92 ? 532  PHE B CZ  1 
ATOM   8839  N  N   . PHE B  1  507 ? 17.495  23.685  -15.229 1.00 106.15 ? 533  PHE B N   1 
ATOM   8840  C  CA  . PHE B  1  507 ? 16.854  24.913  -15.698 1.00 108.05 ? 533  PHE B CA  1 
ATOM   8841  C  C   . PHE B  1  507 ? 17.884  25.855  -16.329 1.00 108.86 ? 533  PHE B C   1 
ATOM   8842  O  O   . PHE B  1  507 ? 17.541  26.706  -17.153 1.00 108.56 ? 533  PHE B O   1 
ATOM   8843  C  CB  . PHE B  1  507 ? 16.141  25.634  -14.544 1.00 107.41 ? 533  PHE B CB  1 
ATOM   8844  C  CG  . PHE B  1  507 ? 14.668  25.318  -14.435 1.00 108.83 ? 533  PHE B CG  1 
ATOM   8845  C  CD1 . PHE B  1  507 ? 14.228  24.156  -13.800 1.00 109.38 ? 533  PHE B CD1 1 
ATOM   8846  C  CD2 . PHE B  1  507 ? 13.716  26.187  -14.974 1.00 109.75 ? 533  PHE B CD2 1 
ATOM   8847  C  CE1 . PHE B  1  507 ? 12.859  23.863  -13.702 1.00 110.06 ? 533  PHE B CE1 1 
ATOM   8848  C  CE2 . PHE B  1  507 ? 12.345  25.908  -14.885 1.00 110.26 ? 533  PHE B CE2 1 
ATOM   8849  C  CZ  . PHE B  1  507 ? 11.913  24.742  -14.247 1.00 110.23 ? 533  PHE B CZ  1 
ATOM   8850  N  N   . SER B  1  508 ? 19.149  25.673  -15.961 1.00 109.80 ? 534  SER B N   1 
ATOM   8851  C  CA  . SER B  1  508 ? 20.217  26.525  -16.464 1.00 110.39 ? 534  SER B CA  1 
ATOM   8852  C  C   . SER B  1  508 ? 21.446  25.801  -17.005 1.00 110.49 ? 534  SER B C   1 
ATOM   8853  O  O   . SER B  1  508 ? 22.334  25.436  -16.242 1.00 110.52 ? 534  SER B O   1 
ATOM   8854  C  CB  . SER B  1  508 ? 20.667  27.471  -15.352 1.00 111.45 ? 534  SER B CB  1 
ATOM   8855  O  OG  . SER B  1  508 ? 21.113  26.736  -14.218 1.00 112.25 ? 534  SER B OG  1 
ATOM   8856  N  N   . LEU B  1  509 ? 21.511  25.621  -18.319 1.00 110.95 ? 535  LEU B N   1 
ATOM   8857  C  CA  . LEU B  1  509 ? 22.664  24.967  -18.937 1.00 111.89 ? 535  LEU B CA  1 
ATOM   8858  C  C   . LEU B  1  509 ? 23.960  25.724  -18.602 1.00 112.34 ? 535  LEU B C   1 
ATOM   8859  O  O   . LEU B  1  509 ? 24.012  26.949  -18.661 1.00 111.94 ? 535  LEU B O   1 
ATOM   8860  C  CB  . LEU B  1  509 ? 22.470  24.884  -20.462 1.00 111.59 ? 535  LEU B CB  1 
ATOM   8861  C  CG  . LEU B  1  509 ? 23.659  24.552  -21.380 1.00 110.58 ? 535  LEU B CG  1 
ATOM   8862  C  CD1 . LEU B  1  509 ? 24.330  23.263  -20.957 1.00 110.21 ? 535  LEU B CD1 1 
ATOM   8863  C  CD2 . LEU B  1  509 ? 23.167  24.442  -22.809 1.00 109.92 ? 535  LEU B CD2 1 
ATOM   8864  N  N   . ASP B  1  510 ? 24.999  24.981  -18.238 1.00 113.63 ? 536  ASP B N   1 
ATOM   8865  C  CA  . ASP B  1  510 ? 26.282  25.579  -17.897 1.00 114.60 ? 536  ASP B CA  1 
ATOM   8866  C  C   . ASP B  1  510 ? 27.323  25.077  -18.883 1.00 114.86 ? 536  ASP B C   1 
ATOM   8867  O  O   . ASP B  1  510 ? 26.977  24.438  -19.875 1.00 115.33 ? 536  ASP B O   1 
ATOM   8868  C  CB  . ASP B  1  510 ? 26.692  25.188  -16.477 1.00 115.44 ? 536  ASP B CB  1 
ATOM   8869  C  CG  . ASP B  1  510 ? 27.762  26.094  -15.915 1.00 116.42 ? 536  ASP B CG  1 
ATOM   8870  O  OD1 . ASP B  1  510 ? 27.447  27.270  -15.628 1.00 116.56 ? 536  ASP B OD1 1 
ATOM   8871  O  OD2 . ASP B  1  510 ? 28.918  25.644  -15.767 1.00 117.37 ? 536  ASP B OD2 1 
ATOM   8872  N  N   . THR B  1  511 ? 28.594  25.352  -18.608 1.00 115.40 ? 537  THR B N   1 
ATOM   8873  C  CA  . THR B  1  511 ? 29.672  24.923  -19.498 1.00 116.43 ? 537  THR B CA  1 
ATOM   8874  C  C   . THR B  1  511 ? 31.018  24.744  -18.807 1.00 116.12 ? 537  THR B C   1 
ATOM   8875  O  O   . THR B  1  511 ? 31.981  24.287  -19.421 1.00 115.83 ? 537  THR B O   1 
ATOM   8876  C  CB  . THR B  1  511 ? 29.882  25.930  -20.652 1.00 117.22 ? 537  THR B CB  1 
ATOM   8877  O  OG1 . THR B  1  511 ? 29.980  27.255  -20.116 1.00 118.44 ? 537  THR B OG1 1 
ATOM   8878  C  CG2 . THR B  1  511 ? 28.730  25.868  -21.643 1.00 118.31 ? 537  THR B CG2 1 
ATOM   8879  N  N   . PHE B  1  512 ? 31.094  25.101  -17.533 1.00 115.98 ? 538  PHE B N   1 
ATOM   8880  C  CA  . PHE B  1  512 ? 32.355  24.988  -16.819 1.00 115.84 ? 538  PHE B CA  1 
ATOM   8881  C  C   . PHE B  1  512 ? 32.819  23.566  -16.523 1.00 115.29 ? 538  PHE B C   1 
ATOM   8882  O  O   . PHE B  1  512 ? 33.972  23.221  -16.794 1.00 114.60 ? 538  PHE B O   1 
ATOM   8883  C  CB  . PHE B  1  512 ? 32.301  25.786  -15.507 1.00 116.21 ? 538  PHE B CB  1 
ATOM   8884  C  CG  . PHE B  1  512 ? 33.573  25.705  -14.697 1.00 116.75 ? 538  PHE B CG  1 
ATOM   8885  C  CD1 . PHE B  1  512 ? 34.806  26.025  -15.273 1.00 116.34 ? 538  PHE B CD1 1 
ATOM   8886  C  CD2 . PHE B  1  512 ? 33.540  25.296  -13.362 1.00 116.47 ? 538  PHE B CD2 1 
ATOM   8887  C  CE1 . PHE B  1  512 ? 35.986  25.936  -14.535 1.00 116.14 ? 538  PHE B CE1 1 
ATOM   8888  C  CE2 . PHE B  1  512 ? 34.715  25.202  -12.610 1.00 116.53 ? 538  PHE B CE2 1 
ATOM   8889  C  CZ  . PHE B  1  512 ? 35.943  25.522  -13.198 1.00 116.59 ? 538  PHE B CZ  1 
ATOM   8890  N  N   . PRO B  1  513 ? 31.931  22.715  -15.971 1.00 114.82 ? 539  PRO B N   1 
ATOM   8891  C  CA  . PRO B  1  513 ? 32.330  21.337  -15.653 1.00 114.29 ? 539  PRO B CA  1 
ATOM   8892  C  C   . PRO B  1  513 ? 32.944  20.533  -16.811 1.00 113.79 ? 539  PRO B C   1 
ATOM   8893  O  O   . PRO B  1  513 ? 33.870  19.739  -16.603 1.00 113.51 ? 539  PRO B O   1 
ATOM   8894  C  CB  . PRO B  1  513 ? 31.034  20.723  -15.117 1.00 113.85 ? 539  PRO B CB  1 
ATOM   8895  C  CG  . PRO B  1  513 ? 29.967  21.502  -15.833 1.00 113.09 ? 539  PRO B CG  1 
ATOM   8896  C  CD  . PRO B  1  513 ? 30.485  22.905  -15.749 1.00 113.66 ? 539  PRO B CD  1 
ATOM   8897  N  N   . TYR B  1  514 ? 32.441  20.763  -18.022 1.00 113.00 ? 540  TYR B N   1 
ATOM   8898  C  CA  . TYR B  1  514 ? 32.903  20.063  -19.219 1.00 111.71 ? 540  TYR B CA  1 
ATOM   8899  C  C   . TYR B  1  514 ? 34.236  20.556  -19.776 1.00 111.55 ? 540  TYR B C   1 
ATOM   8900  O  O   . TYR B  1  514 ? 34.718  20.053  -20.787 1.00 110.54 ? 540  TYR B O   1 
ATOM   8901  C  CB  . TYR B  1  514 ? 31.827  20.159  -20.299 1.00 110.56 ? 540  TYR B CB  1 
ATOM   8902  C  CG  . TYR B  1  514 ? 30.438  19.875  -19.771 1.00 111.04 ? 540  TYR B CG  1 
ATOM   8903  C  CD1 . TYR B  1  514 ? 29.609  20.907  -19.315 1.00 111.38 ? 540  TYR B CD1 1 
ATOM   8904  C  CD2 . TYR B  1  514 ? 29.962  18.572  -19.690 1.00 111.54 ? 540  TYR B CD2 1 
ATOM   8905  C  CE1 . TYR B  1  514 ? 28.338  20.640  -18.794 1.00 111.23 ? 540  TYR B CE1 1 
ATOM   8906  C  CE2 . TYR B  1  514 ? 28.697  18.294  -19.170 1.00 111.76 ? 540  TYR B CE2 1 
ATOM   8907  C  CZ  . TYR B  1  514 ? 27.891  19.330  -18.723 1.00 111.49 ? 540  TYR B CZ  1 
ATOM   8908  O  OH  . TYR B  1  514 ? 26.647  19.046  -18.203 1.00 110.30 ? 540  TYR B OH  1 
ATOM   8909  N  N   . LYS B  1  515 ? 34.831  21.528  -19.098 1.00 112.31 ? 541  LYS B N   1 
ATOM   8910  C  CA  . LYS B  1  515 ? 36.106  22.109  -19.513 1.00 112.19 ? 541  LYS B CA  1 
ATOM   8911  C  C   . LYS B  1  515 ? 37.201  21.090  -19.836 1.00 110.60 ? 541  LYS B C   1 
ATOM   8912  O  O   . LYS B  1  515 ? 37.909  21.226  -20.831 1.00 110.13 ? 541  LYS B O   1 
ATOM   8913  C  CB  . LYS B  1  515 ? 36.629  23.062  -18.422 1.00 113.89 ? 541  LYS B CB  1 
ATOM   8914  C  CG  . LYS B  1  515 ? 36.943  22.376  -17.082 1.00 114.96 ? 541  LYS B CG  1 
ATOM   8915  C  CD  . LYS B  1  515 ? 37.592  23.325  -16.071 1.00 115.79 ? 541  LYS B CD  1 
ATOM   8916  C  CE  . LYS B  1  515 ? 37.874  22.621  -14.740 1.00 115.65 ? 541  LYS B CE  1 
ATOM   8917  N  NZ  . LYS B  1  515 ? 38.482  23.520  -13.708 1.00 115.06 ? 541  LYS B NZ  1 
ATOM   8918  N  N   . CYS B  1  516 ? 37.335  20.068  -19.002 1.00 109.00 ? 542  CYS B N   1 
ATOM   8919  C  CA  . CYS B  1  516 ? 38.393  19.085  -19.194 1.00 107.73 ? 542  CYS B CA  1 
ATOM   8920  C  C   . CYS B  1  516 ? 38.011  17.772  -19.877 1.00 106.50 ? 542  CYS B C   1 
ATOM   8921  O  O   . CYS B  1  516 ? 38.781  16.805  -19.828 1.00 105.33 ? 542  CYS B O   1 
ATOM   8922  C  CB  . CYS B  1  516 ? 39.048  18.782  -17.841 1.00 108.69 ? 542  CYS B CB  1 
ATOM   8923  S  SG  . CYS B  1  516 ? 39.751  20.236  -17.005 1.00 109.29 ? 542  CYS B SG  1 
ATOM   8924  N  N   . LEU B  1  517 ? 36.845  17.726  -20.520 1.00 104.91 ? 543  LEU B N   1 
ATOM   8925  C  CA  . LEU B  1  517 ? 36.417  16.498  -21.196 1.00 103.46 ? 543  LEU B CA  1 
ATOM   8926  C  C   . LEU B  1  517 ? 37.060  16.346  -22.579 1.00 102.47 ? 543  LEU B C   1 
ATOM   8927  O  O   . LEU B  1  517 ? 36.383  16.373  -23.607 1.00 101.57 ? 543  LEU B O   1 
ATOM   8928  C  CB  . LEU B  1  517 ? 34.886  16.455  -21.307 1.00 102.48 ? 543  LEU B CB  1 
ATOM   8929  C  CG  . LEU B  1  517 ? 34.129  16.292  -19.982 1.00 102.19 ? 543  LEU B CG  1 
ATOM   8930  C  CD1 . LEU B  1  517 ? 32.643  16.356  -20.245 1.00 101.83 ? 543  LEU B CD1 1 
ATOM   8931  C  CD2 . LEU B  1  517 ? 34.494  14.973  -19.306 1.00 101.68 ? 543  LEU B CD2 1 
ATOM   8932  N  N   . ASN B  1  518 ? 38.381  16.175  -22.575 1.00 101.49 ? 544  ASN B N   1 
ATOM   8933  C  CA  . ASN B  1  518 ? 39.184  16.017  -23.786 1.00 100.20 ? 544  ASN B CA  1 
ATOM   8934  C  C   . ASN B  1  518 ? 38.492  15.294  -24.925 1.00 98.99  ? 544  ASN B C   1 
ATOM   8935  O  O   . ASN B  1  518 ? 38.251  15.873  -25.978 1.00 99.46  ? 544  ASN B O   1 
ATOM   8936  C  CB  . ASN B  1  518 ? 40.470  15.249  -23.480 1.00 102.09 ? 544  ASN B CB  1 
ATOM   8937  C  CG  . ASN B  1  518 ? 41.364  15.963  -22.495 1.00 104.50 ? 544  ASN B CG  1 
ATOM   8938  O  OD1 . ASN B  1  518 ? 40.926  16.356  -21.406 1.00 105.82 ? 544  ASN B OD1 1 
ATOM   8939  N  ND2 . ASN B  1  518 ? 42.636  16.121  -22.863 1.00 105.03 ? 544  ASN B ND2 1 
ATOM   8940  N  N   . SER B  1  519 ? 38.199  14.015  -24.710 1.00 96.85  ? 545  SER B N   1 
ATOM   8941  C  CA  . SER B  1  519 ? 37.580  13.176  -25.726 1.00 92.93  ? 545  SER B CA  1 
ATOM   8942  C  C   . SER B  1  519 ? 36.084  13.368  -25.925 1.00 91.51  ? 545  SER B C   1 
ATOM   8943  O  O   . SER B  1  519 ? 35.526  12.846  -26.887 1.00 90.04  ? 545  SER B O   1 
ATOM   8944  C  CB  . SER B  1  519 ? 37.858  11.699  -25.416 1.00 91.90  ? 545  SER B CB  1 
ATOM   8945  O  OG  . SER B  1  519 ? 39.247  11.433  -25.370 1.00 89.67  ? 545  SER B OG  1 
ATOM   8946  N  N   . LEU B  1  520 ? 35.430  14.117  -25.043 1.00 90.45  ? 546  LEU B N   1 
ATOM   8947  C  CA  . LEU B  1  520 ? 33.985  14.304  -25.172 1.00 90.05  ? 546  LEU B CA  1 
ATOM   8948  C  C   . LEU B  1  520 ? 33.525  14.610  -26.593 1.00 89.31  ? 546  LEU B C   1 
ATOM   8949  O  O   . LEU B  1  520 ? 33.869  15.646  -27.148 1.00 90.66  ? 546  LEU B O   1 
ATOM   8950  C  CB  . LEU B  1  520 ? 33.486  15.414  -24.253 1.00 90.91  ? 546  LEU B CB  1 
ATOM   8951  C  CG  . LEU B  1  520 ? 31.955  15.521  -24.326 1.00 91.62  ? 546  LEU B CG  1 
ATOM   8952  C  CD1 . LEU B  1  520 ? 31.334  14.275  -23.703 1.00 92.64  ? 546  LEU B CD1 1 
ATOM   8953  C  CD2 . LEU B  1  520 ? 31.470  16.755  -23.599 1.00 92.68  ? 546  LEU B CD2 1 
ATOM   8954  N  N   . GLN B  1  521 ? 32.733  13.710  -27.170 1.00 88.07  ? 547  GLN B N   1 
ATOM   8955  C  CA  . GLN B  1  521 ? 32.214  13.885  -28.524 1.00 86.94  ? 547  GLN B CA  1 
ATOM   8956  C  C   . GLN B  1  521 ? 30.720  14.176  -28.533 1.00 86.93  ? 547  GLN B C   1 
ATOM   8957  O  O   . GLN B  1  521 ? 30.257  15.006  -29.309 1.00 86.82  ? 547  GLN B O   1 
ATOM   8958  C  CB  . GLN B  1  521 ? 32.459  12.644  -29.361 1.00 85.98  ? 547  GLN B CB  1 
ATOM   8959  C  CG  . GLN B  1  521 ? 33.891  12.183  -29.381 1.00 86.64  ? 547  GLN B CG  1 
ATOM   8960  C  CD  . GLN B  1  521 ? 34.097  11.005  -30.323 1.00 88.23  ? 547  GLN B CD  1 
ATOM   8961  O  OE1 . GLN B  1  521 ? 35.180  10.419  -30.372 1.00 88.08  ? 547  GLN B OE1 1 
ATOM   8962  N  NE2 . GLN B  1  521 ? 33.054  10.655  -31.083 1.00 87.36  ? 547  GLN B NE2 1 
ATOM   8963  N  N   . VAL B  1  522 ? 29.961  13.487  -27.686 1.00 87.54  ? 548  VAL B N   1 
ATOM   8964  C  CA  . VAL B  1  522 ? 28.514  13.707  -27.620 1.00 87.36  ? 548  VAL B CA  1 
ATOM   8965  C  C   . VAL B  1  522 ? 28.086  14.224  -26.257 1.00 87.25  ? 548  VAL B C   1 
ATOM   8966  O  O   . VAL B  1  522 ? 28.745  13.965  -25.249 1.00 86.89  ? 548  VAL B O   1 
ATOM   8967  C  CB  . VAL B  1  522 ? 27.719  12.417  -27.905 1.00 87.05  ? 548  VAL B CB  1 
ATOM   8968  C  CG1 . VAL B  1  522 ? 26.258  12.761  -28.196 1.00 84.36  ? 548  VAL B CG1 1 
ATOM   8969  C  CG2 . VAL B  1  522 ? 28.343  11.668  -29.065 1.00 87.03  ? 548  VAL B CG2 1 
ATOM   8970  N  N   . LEU B  1  523 ? 26.982  14.961  -26.235 1.00 87.01  ? 549  LEU B N   1 
ATOM   8971  C  CA  . LEU B  1  523 ? 26.474  15.516  -24.991 1.00 88.69  ? 549  LEU B CA  1 
ATOM   8972  C  C   . LEU B  1  523 ? 24.997  15.848  -25.105 1.00 88.65  ? 549  LEU B C   1 
ATOM   8973  O  O   . LEU B  1  523 ? 24.624  16.981  -25.399 1.00 88.80  ? 549  LEU B O   1 
ATOM   8974  C  CB  . LEU B  1  523 ? 27.236  16.788  -24.600 1.00 89.80  ? 549  LEU B CB  1 
ATOM   8975  C  CG  . LEU B  1  523 ? 26.995  17.186  -23.138 1.00 90.96  ? 549  LEU B CG  1 
ATOM   8976  C  CD1 . LEU B  1  523 ? 28.191  16.688  -22.336 1.00 91.86  ? 549  LEU B CD1 1 
ATOM   8977  C  CD2 . LEU B  1  523 ? 26.817  18.695  -22.967 1.00 90.48  ? 549  LEU B CD2 1 
ATOM   8978  N  N   . ASP B  1  524 ? 24.155  14.853  -24.876 1.00 88.39  ? 550  ASP B N   1 
ATOM   8979  C  CA  . ASP B  1  524 ? 22.719  15.059  -24.944 1.00 87.34  ? 550  ASP B CA  1 
ATOM   8980  C  C   . ASP B  1  524 ? 22.324  15.896  -23.722 1.00 87.14  ? 550  ASP B C   1 
ATOM   8981  O  O   . ASP B  1  524 ? 22.915  15.761  -22.651 1.00 87.30  ? 550  ASP B O   1 
ATOM   8982  C  CB  . ASP B  1  524 ? 22.016  13.695  -24.944 1.00 87.48  ? 550  ASP B CB  1 
ATOM   8983  C  CG  . ASP B  1  524 ? 20.543  13.789  -25.283 1.00 87.86  ? 550  ASP B CG  1 
ATOM   8984  O  OD1 . ASP B  1  524 ? 19.965  12.769  -25.740 1.00 86.71  ? 550  ASP B OD1 1 
ATOM   8985  O  OD2 . ASP B  1  524 ? 19.962  14.880  -25.086 1.00 88.27  ? 550  ASP B OD2 1 
ATOM   8986  N  N   . TYR B  1  525 ? 21.347  16.781  -23.901 1.00 86.80  ? 551  TYR B N   1 
ATOM   8987  C  CA  . TYR B  1  525 ? 20.865  17.649  -22.825 1.00 86.46  ? 551  TYR B CA  1 
ATOM   8988  C  C   . TYR B  1  525 ? 19.392  17.931  -23.083 1.00 87.20  ? 551  TYR B C   1 
ATOM   8989  O  O   . TYR B  1  525 ? 18.809  18.841  -22.491 1.00 86.74  ? 551  TYR B O   1 
ATOM   8990  C  CB  . TYR B  1  525 ? 21.641  18.977  -22.808 1.00 84.67  ? 551  TYR B CB  1 
ATOM   8991  C  CG  . TYR B  1  525 ? 22.391  19.267  -21.519 1.00 82.49  ? 551  TYR B CG  1 
ATOM   8992  C  CD1 . TYR B  1  525 ? 23.772  19.043  -21.422 1.00 80.71  ? 551  TYR B CD1 1 
ATOM   8993  C  CD2 . TYR B  1  525 ? 21.714  19.739  -20.390 1.00 81.47  ? 551  TYR B CD2 1 
ATOM   8994  C  CE1 . TYR B  1  525 ? 24.458  19.275  -20.237 1.00 79.10  ? 551  TYR B CE1 1 
ATOM   8995  C  CE2 . TYR B  1  525 ? 22.389  19.973  -19.195 1.00 80.42  ? 551  TYR B CE2 1 
ATOM   8996  C  CZ  . TYR B  1  525 ? 23.762  19.735  -19.127 1.00 79.94  ? 551  TYR B CZ  1 
ATOM   8997  O  OH  . TYR B  1  525 ? 24.432  19.924  -17.936 1.00 79.24  ? 551  TYR B OH  1 
ATOM   8998  N  N   . SER B  1  526 ? 18.807  17.134  -23.973 1.00 88.76  ? 552  SER B N   1 
ATOM   8999  C  CA  . SER B  1  526 ? 17.407  17.273  -24.366 1.00 92.20  ? 552  SER B CA  1 
ATOM   9000  C  C   . SER B  1  526 ? 16.372  17.068  -23.263 1.00 94.27  ? 552  SER B C   1 
ATOM   9001  O  O   . SER B  1  526 ? 16.708  16.811  -22.112 1.00 94.88  ? 552  SER B O   1 
ATOM   9002  C  CB  . SER B  1  526 ? 17.097  16.317  -25.514 1.00 92.18  ? 552  SER B CB  1 
ATOM   9003  O  OG  . SER B  1  526 ? 17.296  14.971  -25.125 1.00 93.36  ? 552  SER B OG  1 
ATOM   9004  N  N   . LEU B  1  527 ? 15.105  17.181  -23.642 1.00 96.98  ? 553  LEU B N   1 
ATOM   9005  C  CA  . LEU B  1  527 ? 13.978  17.022  -22.730 1.00 100.52 ? 553  LEU B CA  1 
ATOM   9006  C  C   . LEU B  1  527 ? 14.130  17.573  -21.307 1.00 103.12 ? 553  LEU B C   1 
ATOM   9007  O  O   . LEU B  1  527 ? 13.523  17.050  -20.373 1.00 103.33 ? 553  LEU B O   1 
ATOM   9008  C  CB  . LEU B  1  527 ? 13.557  15.551  -22.657 1.00 100.57 ? 553  LEU B CB  1 
ATOM   9009  C  CG  . LEU B  1  527 ? 12.361  15.112  -23.514 1.00 100.67 ? 553  LEU B CG  1 
ATOM   9010  C  CD1 . LEU B  1  527 ? 12.091  13.628  -23.273 1.00 101.67 ? 553  LEU B CD1 1 
ATOM   9011  C  CD2 . LEU B  1  527 ? 11.130  15.929  -23.154 1.00 99.81  ? 553  LEU B CD2 1 
ATOM   9012  N  N   . ASN B  1  528 ? 14.927  18.624  -21.133 1.00 106.56 ? 554  ASN B N   1 
ATOM   9013  C  CA  . ASN B  1  528 ? 15.089  19.232  -19.814 1.00 110.25 ? 554  ASN B CA  1 
ATOM   9014  C  C   . ASN B  1  528 ? 14.135  20.418  -19.686 1.00 113.49 ? 554  ASN B C   1 
ATOM   9015  O  O   . ASN B  1  528 ? 13.086  20.473  -20.341 1.00 112.62 ? 554  ASN B O   1 
ATOM   9016  C  CB  . ASN B  1  528 ? 16.526  19.727  -19.596 1.00 109.42 ? 554  ASN B CB  1 
ATOM   9017  C  CG  . ASN B  1  528 ? 17.471  18.625  -19.179 1.00 108.95 ? 554  ASN B CG  1 
ATOM   9018  O  OD1 . ASN B  1  528 ? 18.557  18.883  -18.658 1.00 108.15 ? 554  ASN B OD1 1 
ATOM   9019  N  ND2 . ASN B  1  528 ? 17.068  17.389  -19.409 1.00 110.34 ? 554  ASN B ND2 1 
ATOM   9020  N  N   . HIS B  1  529 ? 14.510  21.366  -18.832 1.00 117.78 ? 555  HIS B N   1 
ATOM   9021  C  CA  . HIS B  1  529 ? 13.719  22.567  -18.610 1.00 122.13 ? 555  HIS B CA  1 
ATOM   9022  C  C   . HIS B  1  529 ? 14.657  23.782  -18.615 1.00 124.27 ? 555  HIS B C   1 
ATOM   9023  O  O   . HIS B  1  529 ? 14.441  24.759  -17.893 1.00 124.22 ? 555  HIS B O   1 
ATOM   9024  C  CB  . HIS B  1  529 ? 12.963  22.462  -17.276 1.00 123.58 ? 555  HIS B CB  1 
ATOM   9025  C  CG  . HIS B  1  529 ? 11.870  21.432  -17.274 1.00 125.48 ? 555  HIS B CG  1 
ATOM   9026  N  ND1 . HIS B  1  529 ? 10.761  21.517  -18.089 1.00 126.21 ? 555  HIS B ND1 1 
ATOM   9027  C  CD2 . HIS B  1  529 ? 11.722  20.291  -16.559 1.00 126.77 ? 555  HIS B CD2 1 
ATOM   9028  C  CE1 . HIS B  1  529 ? 9.978   20.474  -17.878 1.00 126.80 ? 555  HIS B CE1 1 
ATOM   9029  N  NE2 . HIS B  1  529 ? 10.537  19.714  -16.954 1.00 127.49 ? 555  HIS B NE2 1 
ATOM   9030  N  N   . ILE B  1  530 ? 15.693  23.707  -19.454 1.00 126.70 ? 556  ILE B N   1 
ATOM   9031  C  CA  . ILE B  1  530 ? 16.688  24.777  -19.592 1.00 128.98 ? 556  ILE B CA  1 
ATOM   9032  C  C   . ILE B  1  530 ? 16.137  25.989  -20.347 1.00 130.92 ? 556  ILE B C   1 
ATOM   9033  O  O   . ILE B  1  530 ? 15.211  25.871  -21.158 1.00 130.99 ? 556  ILE B O   1 
ATOM   9034  C  CB  . ILE B  1  530 ? 17.949  24.296  -20.362 1.00 128.24 ? 556  ILE B CB  1 
ATOM   9035  C  CG1 . ILE B  1  530 ? 18.497  23.015  -19.742 1.00 128.23 ? 556  ILE B CG1 1 
ATOM   9036  C  CG2 . ILE B  1  530 ? 19.032  25.364  -20.312 1.00 127.47 ? 556  ILE B CG2 1 
ATOM   9037  C  CD1 . ILE B  1  530 ? 19.686  22.444  -20.494 1.00 128.14 ? 556  ILE B CD1 1 
ATOM   9038  N  N   . MET B  1  531 ? 16.728  27.151  -20.076 1.00 132.88 ? 557  MET B N   1 
ATOM   9039  C  CA  . MET B  1  531 ? 16.340  28.404  -20.719 1.00 134.66 ? 557  MET B CA  1 
ATOM   9040  C  C   . MET B  1  531 ? 17.337  29.489  -20.345 1.00 135.15 ? 557  MET B C   1 
ATOM   9041  O  O   . MET B  1  531 ? 17.652  30.364  -21.145 1.00 134.59 ? 557  MET B O   1 
ATOM   9042  C  CB  . MET B  1  531 ? 14.939  28.821  -20.269 1.00 135.64 ? 557  MET B CB  1 
ATOM   9043  C  CG  . MET B  1  531 ? 14.780  28.962  -18.762 1.00 137.07 ? 557  MET B CG  1 
ATOM   9044  S  SD  . MET B  1  531 ? 13.097  29.437  -18.280 1.00 138.80 ? 557  MET B SD  1 
ATOM   9045  C  CE  . MET B  1  531 ? 12.309  27.818  -18.091 1.00 139.28 ? 557  MET B CE  1 
ATOM   9046  N  N   . THR B  1  532 ? 17.844  29.400  -19.121 1.00 136.64 ? 558  THR B N   1 
ATOM   9047  C  CA  . THR B  1  532 ? 18.795  30.370  -18.595 1.00 138.27 ? 558  THR B CA  1 
ATOM   9048  C  C   . THR B  1  532 ? 20.251  29.993  -18.898 1.00 139.77 ? 558  THR B C   1 
ATOM   9049  O  O   . THR B  1  532 ? 20.532  29.234  -19.828 1.00 139.47 ? 558  THR B O   1 
ATOM   9050  C  CB  . THR B  1  532 ? 18.614  30.514  -17.063 1.00 137.64 ? 558  THR B CB  1 
ATOM   9051  O  OG1 . THR B  1  532 ? 17.225  30.381  -16.738 1.00 136.37 ? 558  THR B OG1 1 
ATOM   9052  C  CG2 . THR B  1  532 ? 19.094  31.881  -16.588 1.00 137.45 ? 558  THR B CG2 1 
ATOM   9053  N  N   . SER B  1  533 ? 21.161  30.542  -18.098 1.00 141.59 ? 559  SER B N   1 
ATOM   9054  C  CA  . SER B  1  533 ? 22.600  30.313  -18.219 1.00 143.51 ? 559  SER B CA  1 
ATOM   9055  C  C   . SER B  1  533 ? 23.255  31.180  -17.144 1.00 144.64 ? 559  SER B C   1 
ATOM   9056  O  O   . SER B  1  533 ? 23.671  32.307  -17.415 1.00 145.28 ? 559  SER B O   1 
ATOM   9057  C  CB  . SER B  1  533 ? 23.097  30.733  -19.609 1.00 143.61 ? 559  SER B CB  1 
ATOM   9058  O  OG  . SER B  1  533 ? 24.507  30.616  -19.711 1.00 144.06 ? 559  SER B OG  1 
ATOM   9059  N  N   . LYS B  1  534 ? 23.335  30.647  -15.927 1.00 145.78 ? 560  LYS B N   1 
ATOM   9060  C  CA  . LYS B  1  534 ? 23.891  31.369  -14.781 1.00 147.21 ? 560  LYS B CA  1 
ATOM   9061  C  C   . LYS B  1  534 ? 25.385  31.732  -14.813 1.00 148.51 ? 560  LYS B C   1 
ATOM   9062  O  O   . LYS B  1  534 ? 25.973  32.061  -13.778 1.00 148.48 ? 560  LYS B O   1 
ATOM   9063  C  CB  . LYS B  1  534 ? 23.544  30.593  -13.508 1.00 146.55 ? 560  LYS B CB  1 
ATOM   9064  C  CG  . LYS B  1  534 ? 22.036  30.425  -13.340 1.00 146.25 ? 560  LYS B CG  1 
ATOM   9065  C  CD  . LYS B  1  534 ? 21.659  29.385  -12.295 1.00 145.81 ? 560  LYS B CD  1 
ATOM   9066  C  CE  . LYS B  1  534 ? 20.141  29.210  -12.234 1.00 145.08 ? 560  LYS B CE  1 
ATOM   9067  N  NZ  . LYS B  1  534 ? 19.701  28.162  -11.266 1.00 143.89 ? 560  LYS B NZ  1 
ATOM   9068  N  N   . LYS B  1  535 ? 25.983  31.678  -16.003 1.00 150.21 ? 561  LYS B N   1 
ATOM   9069  C  CA  . LYS B  1  535 ? 27.392  32.027  -16.219 1.00 151.68 ? 561  LYS B CA  1 
ATOM   9070  C  C   . LYS B  1  535 ? 27.726  31.998  -17.715 1.00 152.66 ? 561  LYS B C   1 
ATOM   9071  O  O   . LYS B  1  535 ? 27.812  30.930  -18.324 1.00 152.71 ? 561  LYS B O   1 
ATOM   9072  C  CB  . LYS B  1  535 ? 28.326  31.079  -15.448 1.00 150.89 ? 561  LYS B CB  1 
ATOM   9073  C  CG  . LYS B  1  535 ? 28.976  31.724  -14.222 1.00 150.23 ? 561  LYS B CG  1 
ATOM   9074  C  CD  . LYS B  1  535 ? 29.878  32.892  -14.628 1.00 149.57 ? 561  LYS B CD  1 
ATOM   9075  C  CE  . LYS B  1  535 ? 30.270  33.757  -13.435 1.00 148.67 ? 561  LYS B CE  1 
ATOM   9076  N  NZ  . LYS B  1  535 ? 31.018  33.015  -12.387 1.00 148.09 ? 561  LYS B NZ  1 
ATOM   9077  N  N   . GLN B  1  536 ? 27.907  33.184  -18.298 1.00 153.93 ? 562  GLN B N   1 
ATOM   9078  C  CA  . GLN B  1  536 ? 28.214  33.323  -19.723 1.00 155.18 ? 562  GLN B CA  1 
ATOM   9079  C  C   . GLN B  1  536 ? 29.624  32.904  -20.143 1.00 155.50 ? 562  GLN B C   1 
ATOM   9080  O  O   . GLN B  1  536 ? 30.250  33.562  -20.978 1.00 155.33 ? 562  GLN B O   1 
ATOM   9081  C  CB  . GLN B  1  536 ? 27.958  34.762  -20.175 1.00 155.47 ? 562  GLN B CB  1 
ATOM   9082  C  CG  . GLN B  1  536 ? 26.578  34.991  -20.780 1.00 156.95 ? 562  GLN B CG  1 
ATOM   9083  C  CD  . GLN B  1  536 ? 25.443  34.571  -19.862 1.00 157.77 ? 562  GLN B CD  1 
ATOM   9084  O  OE1 . GLN B  1  536 ? 25.304  35.084  -18.750 1.00 158.04 ? 562  GLN B OE1 1 
ATOM   9085  N  NE2 . GLN B  1  536 ? 24.618  33.637  -20.329 1.00 157.79 ? 562  GLN B NE2 1 
ATOM   9086  N  N   . GLU B  1  537 ? 30.118  31.812  -19.563 1.00 155.82 ? 563  GLU B N   1 
ATOM   9087  C  CA  . GLU B  1  537 ? 31.438  31.283  -19.896 1.00 155.48 ? 563  GLU B CA  1 
ATOM   9088  C  C   . GLU B  1  537 ? 31.177  30.139  -20.872 1.00 154.93 ? 563  GLU B C   1 
ATOM   9089  O  O   . GLU B  1  537 ? 31.823  29.089  -20.834 1.00 155.11 ? 563  GLU B O   1 
ATOM   9090  C  CB  . GLU B  1  537 ? 32.139  30.769  -18.631 1.00 155.95 ? 563  GLU B CB  1 
ATOM   9091  C  CG  . GLU B  1  537 ? 33.541  30.237  -18.878 1.00 156.67 ? 563  GLU B CG  1 
ATOM   9092  C  CD  . GLU B  1  537 ? 34.446  31.252  -19.559 1.00 157.06 ? 563  GLU B CD  1 
ATOM   9093  O  OE1 . GLU B  1  537 ? 35.527  30.851  -20.040 1.00 156.99 ? 563  GLU B OE1 1 
ATOM   9094  O  OE2 . GLU B  1  537 ? 34.082  32.448  -19.611 1.00 157.06 ? 563  GLU B OE2 1 
ATOM   9095  N  N   . LEU B  1  538 ? 30.212  30.385  -21.751 1.00 153.90 ? 564  LEU B N   1 
ATOM   9096  C  CA  . LEU B  1  538 ? 29.748  29.441  -22.759 1.00 152.62 ? 564  LEU B CA  1 
ATOM   9097  C  C   . LEU B  1  538 ? 30.771  28.988  -23.806 1.00 151.57 ? 564  LEU B C   1 
ATOM   9098  O  O   . LEU B  1  538 ? 30.402  28.372  -24.806 1.00 151.33 ? 564  LEU B O   1 
ATOM   9099  C  CB  . LEU B  1  538 ? 28.523  30.046  -23.458 1.00 152.69 ? 564  LEU B CB  1 
ATOM   9100  C  CG  . LEU B  1  538 ? 27.456  30.613  -22.511 1.00 152.57 ? 564  LEU B CG  1 
ATOM   9101  C  CD1 . LEU B  1  538 ? 26.486  31.501  -23.271 1.00 152.31 ? 564  LEU B CD1 1 
ATOM   9102  C  CD2 . LEU B  1  538 ? 26.724  29.471  -21.829 1.00 152.49 ? 564  LEU B CD2 1 
ATOM   9103  N  N   . GLN B  1  539 ? 32.048  29.274  -23.585 1.00 150.43 ? 565  GLN B N   1 
ATOM   9104  C  CA  . GLN B  1  539 ? 33.064  28.865  -24.548 1.00 149.61 ? 565  GLN B CA  1 
ATOM   9105  C  C   . GLN B  1  539 ? 33.732  27.547  -24.171 1.00 148.71 ? 565  GLN B C   1 
ATOM   9106  O  O   . GLN B  1  539 ? 34.271  26.855  -25.036 1.00 148.20 ? 565  GLN B O   1 
ATOM   9107  C  CB  . GLN B  1  539 ? 34.142  29.945  -24.696 1.00 150.51 ? 565  GLN B CB  1 
ATOM   9108  C  CG  . GLN B  1  539 ? 35.032  30.141  -23.465 1.00 151.28 ? 565  GLN B CG  1 
ATOM   9109  C  CD  . GLN B  1  539 ? 36.521  30.025  -23.777 1.00 151.19 ? 565  GLN B CD  1 
ATOM   9110  O  OE1 . GLN B  1  539 ? 37.042  30.715  -24.657 1.00 151.23 ? 565  GLN B OE1 1 
ATOM   9111  N  NE2 . GLN B  1  539 ? 37.210  29.152  -23.050 1.00 150.80 ? 565  GLN B NE2 1 
ATOM   9112  N  N   . HIS B  1  540 ? 33.682  27.203  -22.884 1.00 147.54 ? 566  HIS B N   1 
ATOM   9113  C  CA  . HIS B  1  540 ? 34.308  25.983  -22.370 1.00 145.95 ? 566  HIS B CA  1 
ATOM   9114  C  C   . HIS B  1  540 ? 33.703  24.622  -22.762 1.00 144.20 ? 566  HIS B C   1 
ATOM   9115  O  O   . HIS B  1  540 ? 33.350  23.826  -21.884 1.00 144.61 ? 566  HIS B O   1 
ATOM   9116  C  CB  . HIS B  1  540 ? 34.421  26.064  -20.837 1.00 146.80 ? 566  HIS B CB  1 
ATOM   9117  C  CG  . HIS B  1  540 ? 35.679  26.726  -20.355 1.00 147.82 ? 566  HIS B CG  1 
ATOM   9118  N  ND1 . HIS B  1  540 ? 36.937  26.297  -20.725 1.00 147.91 ? 566  HIS B ND1 1 
ATOM   9119  C  CD2 . HIS B  1  540 ? 35.873  27.772  -19.516 1.00 147.99 ? 566  HIS B CD2 1 
ATOM   9120  C  CE1 . HIS B  1  540 ? 37.850  27.048  -20.136 1.00 147.62 ? 566  HIS B CE1 1 
ATOM   9121  N  NE2 . HIS B  1  540 ? 37.231  27.951  -19.397 1.00 148.02 ? 566  HIS B NE2 1 
ATOM   9122  N  N   . PHE B  1  541 ? 33.595  24.363  -24.072 1.00 141.18 ? 567  PHE B N   1 
ATOM   9123  C  CA  . PHE B  1  541 ? 33.089  23.088  -24.615 1.00 137.19 ? 567  PHE B CA  1 
ATOM   9124  C  C   . PHE B  1  541 ? 34.263  22.430  -25.340 1.00 134.93 ? 567  PHE B C   1 
ATOM   9125  O  O   . PHE B  1  541 ? 34.740  22.952  -26.342 1.00 134.58 ? 567  PHE B O   1 
ATOM   9126  C  CB  . PHE B  1  541 ? 31.948  23.318  -25.616 1.00 135.64 ? 567  PHE B CB  1 
ATOM   9127  C  CG  . PHE B  1  541 ? 30.561  23.203  -25.018 1.00 134.31 ? 567  PHE B CG  1 
ATOM   9128  C  CD1 . PHE B  1  541 ? 29.441  23.509  -25.788 1.00 133.54 ? 567  PHE B CD1 1 
ATOM   9129  C  CD2 . PHE B  1  541 ? 30.367  22.789  -23.698 1.00 133.59 ? 567  PHE B CD2 1 
ATOM   9130  C  CE1 . PHE B  1  541 ? 28.150  23.409  -25.258 1.00 132.60 ? 567  PHE B CE1 1 
ATOM   9131  C  CE2 . PHE B  1  541 ? 29.074  22.686  -23.158 1.00 132.92 ? 567  PHE B CE2 1 
ATOM   9132  C  CZ  . PHE B  1  541 ? 27.963  22.997  -23.942 1.00 132.12 ? 567  PHE B CZ  1 
ATOM   9133  N  N   . PRO B  1  542 ? 34.731  21.270  -24.851 1.00 132.91 ? 568  PRO B N   1 
ATOM   9134  C  CA  . PRO B  1  542 ? 35.856  20.525  -25.426 1.00 130.69 ? 568  PRO B CA  1 
ATOM   9135  C  C   . PRO B  1  542 ? 36.073  20.684  -26.920 1.00 128.55 ? 568  PRO B C   1 
ATOM   9136  O  O   . PRO B  1  542 ? 35.121  20.794  -27.693 1.00 127.79 ? 568  PRO B O   1 
ATOM   9137  C  CB  . PRO B  1  542 ? 35.554  19.092  -25.017 1.00 131.56 ? 568  PRO B CB  1 
ATOM   9138  C  CG  . PRO B  1  542 ? 35.012  19.284  -23.640 1.00 132.56 ? 568  PRO B CG  1 
ATOM   9139  C  CD  . PRO B  1  542 ? 34.053  20.458  -23.824 1.00 133.05 ? 568  PRO B CD  1 
ATOM   9140  N  N   . SER B  1  543 ? 37.348  20.687  -27.303 1.00 126.36 ? 569  SER B N   1 
ATOM   9141  C  CA  . SER B  1  543 ? 37.765  20.855  -28.692 1.00 123.85 ? 569  SER B CA  1 
ATOM   9142  C  C   . SER B  1  543 ? 37.314  19.741  -29.636 1.00 121.95 ? 569  SER B C   1 
ATOM   9143  O  O   . SER B  1  543 ? 37.227  19.948  -30.849 1.00 121.51 ? 569  SER B O   1 
ATOM   9144  C  CB  . SER B  1  543 ? 39.287  21.002  -28.756 1.00 123.86 ? 569  SER B CB  1 
ATOM   9145  O  OG  . SER B  1  543 ? 39.719  22.140  -28.023 1.00 123.55 ? 569  SER B OG  1 
ATOM   9146  N  N   . SER B  1  544 ? 37.016  18.568  -29.084 1.00 119.64 ? 570  SER B N   1 
ATOM   9147  C  CA  . SER B  1  544 ? 36.574  17.434  -29.897 1.00 116.23 ? 570  SER B CA  1 
ATOM   9148  C  C   . SER B  1  544 ? 35.050  17.321  -29.985 1.00 113.61 ? 570  SER B C   1 
ATOM   9149  O  O   . SER B  1  544 ? 34.516  16.653  -30.869 1.00 111.94 ? 570  SER B O   1 
ATOM   9150  C  CB  . SER B  1  544 ? 37.152  16.131  -29.335 1.00 116.23 ? 570  SER B CB  1 
ATOM   9151  O  OG  . SER B  1  544 ? 36.751  15.934  -27.991 1.00 116.11 ? 570  SER B OG  1 
ATOM   9152  N  N   . LEU B  1  545 ? 34.360  17.983  -29.063 1.00 111.48 ? 571  LEU B N   1 
ATOM   9153  C  CA  . LEU B  1  545 ? 32.903  17.964  -29.018 1.00 109.66 ? 571  LEU B CA  1 
ATOM   9154  C  C   . LEU B  1  545 ? 32.263  18.194  -30.385 1.00 108.31 ? 571  LEU B C   1 
ATOM   9155  O  O   . LEU B  1  545 ? 32.243  19.317  -30.886 1.00 108.40 ? 571  LEU B O   1 
ATOM   9156  C  CB  . LEU B  1  545 ? 32.402  19.025  -28.033 1.00 110.21 ? 571  LEU B CB  1 
ATOM   9157  C  CG  . LEU B  1  545 ? 30.889  19.253  -27.914 1.00 110.35 ? 571  LEU B CG  1 
ATOM   9158  C  CD1 . LEU B  1  545 ? 30.209  17.988  -27.424 1.00 110.26 ? 571  LEU B CD1 1 
ATOM   9159  C  CD2 . LEU B  1  545 ? 30.629  20.410  -26.951 1.00 110.84 ? 571  LEU B CD2 1 
ATOM   9160  N  N   . ALA B  1  546 ? 31.738  17.129  -30.982 1.00 106.88 ? 572  ALA B N   1 
ATOM   9161  C  CA  . ALA B  1  546 ? 31.084  17.228  -32.284 1.00 105.34 ? 572  ALA B CA  1 
ATOM   9162  C  C   . ALA B  1  546 ? 29.588  17.499  -32.128 1.00 104.43 ? 572  ALA B C   1 
ATOM   9163  O  O   . ALA B  1  546 ? 29.115  18.588  -32.450 1.00 104.54 ? 572  ALA B O   1 
ATOM   9164  C  CB  . ALA B  1  546 ? 31.305  15.948  -33.088 1.00 104.17 ? 572  ALA B CB  1 
ATOM   9165  N  N   . PHE B  1  547 ? 28.850  16.514  -31.626 1.00 103.85 ? 573  PHE B N   1 
ATOM   9166  C  CA  . PHE B  1  547 ? 27.404  16.655  -31.437 1.00 102.58 ? 573  PHE B CA  1 
ATOM   9167  C  C   . PHE B  1  547 ? 27.035  17.258  -30.085 1.00 102.18 ? 573  PHE B C   1 
ATOM   9168  O  O   . PHE B  1  547 ? 27.797  17.148  -29.123 1.00 102.51 ? 573  PHE B O   1 
ATOM   9169  C  CB  . PHE B  1  547 ? 26.720  15.297  -31.579 1.00 101.80 ? 573  PHE B CB  1 
ATOM   9170  C  CG  . PHE B  1  547 ? 26.915  14.667  -32.921 1.00 101.43 ? 573  PHE B CG  1 
ATOM   9171  C  CD1 . PHE B  1  547 ? 28.152  14.141  -33.287 1.00 100.53 ? 573  PHE B CD1 1 
ATOM   9172  C  CD2 . PHE B  1  547 ? 25.861  14.609  -33.827 1.00 101.41 ? 573  PHE B CD2 1 
ATOM   9173  C  CE1 . PHE B  1  547 ? 28.341  13.574  -34.540 1.00 100.82 ? 573  PHE B CE1 1 
ATOM   9174  C  CE2 . PHE B  1  547 ? 26.031  14.045  -35.088 1.00 101.41 ? 573  PHE B CE2 1 
ATOM   9175  C  CZ  . PHE B  1  547 ? 27.275  13.520  -35.450 1.00 101.73 ? 573  PHE B CZ  1 
ATOM   9176  N  N   . LEU B  1  548 ? 25.864  17.893  -30.023 1.00 101.02 ? 574  LEU B N   1 
ATOM   9177  C  CA  . LEU B  1  548 ? 25.388  18.512  -28.787 1.00 100.91 ? 574  LEU B CA  1 
ATOM   9178  C  C   . LEU B  1  548 ? 23.894  18.720  -28.845 1.00 100.45 ? 574  LEU B C   1 
ATOM   9179  O  O   . LEU B  1  548 ? 23.414  19.820  -29.102 1.00 99.87  ? 574  LEU B O   1 
ATOM   9180  C  CB  . LEU B  1  548 ? 26.066  19.865  -28.535 1.00 101.58 ? 574  LEU B CB  1 
ATOM   9181  C  CG  . LEU B  1  548 ? 25.870  20.407  -27.109 1.00 102.09 ? 574  LEU B CG  1 
ATOM   9182  C  CD1 . LEU B  1  548 ? 27.227  20.437  -26.411 1.00 101.40 ? 574  LEU B CD1 1 
ATOM   9183  C  CD2 . LEU B  1  548 ? 25.231  21.790  -27.123 1.00 100.84 ? 574  LEU B CD2 1 
ATOM   9184  N  N   . ASN B  1  549 ? 23.159  17.651  -28.596 1.00 101.54 ? 575  ASN B N   1 
ATOM   9185  C  CA  . ASN B  1  549 ? 21.703  17.695  -28.612 1.00 102.86 ? 575  ASN B CA  1 
ATOM   9186  C  C   . ASN B  1  549 ? 21.265  18.702  -27.541 1.00 102.80 ? 575  ASN B C   1 
ATOM   9187  O  O   . ASN B  1  549 ? 21.909  18.822  -26.501 1.00 103.12 ? 575  ASN B O   1 
ATOM   9188  C  CB  . ASN B  1  549 ? 21.146  16.282  -28.308 1.00 103.60 ? 575  ASN B CB  1 
ATOM   9189  C  CG  . ASN B  1  549 ? 19.679  16.115  -28.721 1.00 104.92 ? 575  ASN B CG  1 
ATOM   9190  O  OD1 . ASN B  1  549 ? 18.866  16.986  -28.398 1.00 104.34 ? 575  ASN B OD1 1 
ATOM   9191  N  ND2 . ASN B  1  549 ? 19.325  15.030  -29.427 1.00 106.30 ? 575  ASN B ND2 1 
ATOM   9192  N  N   . LEU B  1  550 ? 20.193  19.438  -27.819 1.00 102.36 ? 576  LEU B N   1 
ATOM   9193  C  CA  . LEU B  1  550 ? 19.643  20.425  -26.886 1.00 102.39 ? 576  LEU B CA  1 
ATOM   9194  C  C   . LEU B  1  550 ? 18.174  20.539  -27.240 1.00 102.50 ? 576  LEU B C   1 
ATOM   9195  O  O   . LEU B  1  550 ? 17.459  21.426  -26.778 1.00 101.48 ? 576  LEU B O   1 
ATOM   9196  C  CB  . LEU B  1  550 ? 20.326  21.794  -27.051 1.00 102.55 ? 576  LEU B CB  1 
ATOM   9197  C  CG  . LEU B  1  550 ? 21.761  21.996  -26.526 1.00 102.82 ? 576  LEU B CG  1 
ATOM   9198  C  CD1 . LEU B  1  550 ? 22.292  23.332  -26.992 1.00 102.87 ? 576  LEU B CD1 1 
ATOM   9199  C  CD2 . LEU B  1  550 ? 21.778  21.937  -25.007 1.00 102.59 ? 576  LEU B CD2 1 
ATOM   9200  N  N   . THR B  1  551 ? 17.735  19.599  -28.065 1.00 103.92 ? 577  THR B N   1 
ATOM   9201  C  CA  . THR B  1  551 ? 16.364  19.560  -28.539 1.00 105.93 ? 577  THR B CA  1 
ATOM   9202  C  C   . THR B  1  551 ? 15.312  19.495  -27.445 1.00 107.31 ? 577  THR B C   1 
ATOM   9203  O  O   . THR B  1  551 ? 15.543  18.975  -26.365 1.00 107.32 ? 577  THR B O   1 
ATOM   9204  C  CB  . THR B  1  551 ? 16.158  18.371  -29.497 1.00 105.30 ? 577  THR B CB  1 
ATOM   9205  O  OG1 . THR B  1  551 ? 16.312  17.142  -28.779 1.00 104.81 ? 577  THR B OG1 1 
ATOM   9206  C  CG2 . THR B  1  551 ? 17.188  18.419  -30.609 1.00 105.30 ? 577  THR B CG2 1 
ATOM   9207  N  N   . GLN B  1  552 ? 14.152  20.052  -27.749 1.00 110.01 ? 578  GLN B N   1 
ATOM   9208  C  CA  . GLN B  1  552 ? 13.027  20.053  -26.837 1.00 113.32 ? 578  GLN B CA  1 
ATOM   9209  C  C   . GLN B  1  552 ? 13.373  20.556  -25.443 1.00 115.50 ? 578  GLN B C   1 
ATOM   9210  O  O   . GLN B  1  552 ? 13.969  19.847  -24.642 1.00 115.46 ? 578  GLN B O   1 
ATOM   9211  C  CB  . GLN B  1  552 ? 12.446  18.642  -26.770 1.00 113.33 ? 578  GLN B CB  1 
ATOM   9212  C  CG  . GLN B  1  552 ? 11.095  18.542  -26.095 1.00 113.25 ? 578  GLN B CG  1 
ATOM   9213  C  CD  . GLN B  1  552 ? 10.427  17.213  -26.379 1.00 113.47 ? 578  GLN B CD  1 
ATOM   9214  O  OE1 . GLN B  1  552 ? 9.374   16.902  -25.823 1.00 113.29 ? 578  GLN B OE1 1 
ATOM   9215  N  NE2 . GLN B  1  552 ? 11.039  16.419  -27.258 1.00 112.30 ? 578  GLN B NE2 1 
ATOM   9216  N  N   . ASN B  1  553 ? 12.988  21.796  -25.171 1.00 119.08 ? 579  ASN B N   1 
ATOM   9217  C  CA  . ASN B  1  553 ? 13.216  22.433  -23.880 1.00 122.67 ? 579  ASN B CA  1 
ATOM   9218  C  C   . ASN B  1  553 ? 12.181  23.532  -23.660 1.00 125.80 ? 579  ASN B C   1 
ATOM   9219  O  O   . ASN B  1  553 ? 11.156  23.588  -24.341 1.00 125.36 ? 579  ASN B O   1 
ATOM   9220  C  CB  . ASN B  1  553 ? 14.621  23.035  -23.818 1.00 121.71 ? 579  ASN B CB  1 
ATOM   9221  C  CG  . ASN B  1  553 ? 15.660  22.041  -23.360 1.00 121.29 ? 579  ASN B CG  1 
ATOM   9222  O  OD1 . ASN B  1  553 ? 16.012  21.988  -22.181 1.00 120.77 ? 579  ASN B OD1 1 
ATOM   9223  N  ND2 . ASN B  1  553 ? 16.150  21.233  -24.293 1.00 121.22 ? 579  ASN B ND2 1 
ATOM   9224  N  N   . ASP B  1  554 ? 12.454  24.405  -22.700 1.00 129.91 ? 580  ASP B N   1 
ATOM   9225  C  CA  . ASP B  1  554 ? 11.544  25.498  -22.409 1.00 134.39 ? 580  ASP B CA  1 
ATOM   9226  C  C   . ASP B  1  554 ? 12.322  26.812  -22.422 1.00 136.78 ? 580  ASP B C   1 
ATOM   9227  O  O   . ASP B  1  554 ? 12.370  27.541  -21.430 1.00 137.08 ? 580  ASP B O   1 
ATOM   9228  C  CB  . ASP B  1  554 ? 10.861  25.258  -21.059 1.00 135.72 ? 580  ASP B CB  1 
ATOM   9229  C  CG  . ASP B  1  554 ? 9.996   23.999  -21.062 1.00 137.17 ? 580  ASP B CG  1 
ATOM   9230  O  OD1 . ASP B  1  554 ? 9.049   23.921  -21.882 1.00 137.44 ? 580  ASP B OD1 1 
ATOM   9231  O  OD2 . ASP B  1  554 ? 10.264  23.086  -20.248 1.00 137.87 ? 580  ASP B OD2 1 
ATOM   9232  N  N   . PHE B  1  555 ? 12.936  27.091  -23.570 1.00 139.47 ? 581  PHE B N   1 
ATOM   9233  C  CA  . PHE B  1  555 ? 13.732  28.294  -23.772 1.00 141.53 ? 581  PHE B CA  1 
ATOM   9234  C  C   . PHE B  1  555 ? 12.962  29.569  -23.447 1.00 143.84 ? 581  PHE B C   1 
ATOM   9235  O  O   . PHE B  1  555 ? 11.729  29.577  -23.404 1.00 143.65 ? 581  PHE B O   1 
ATOM   9236  C  CB  . PHE B  1  555 ? 14.210  28.382  -25.227 1.00 140.14 ? 581  PHE B CB  1 
ATOM   9237  C  CG  . PHE B  1  555 ? 14.853  27.124  -25.746 1.00 138.76 ? 581  PHE B CG  1 
ATOM   9238  C  CD1 . PHE B  1  555 ? 14.073  26.086  -26.256 1.00 137.84 ? 581  PHE B CD1 1 
ATOM   9239  C  CD2 . PHE B  1  555 ? 16.240  26.989  -25.751 1.00 137.52 ? 581  PHE B CD2 1 
ATOM   9240  C  CE1 . PHE B  1  555 ? 14.666  24.933  -26.770 1.00 136.75 ? 581  PHE B CE1 1 
ATOM   9241  C  CE2 . PHE B  1  555 ? 16.844  25.843  -26.261 1.00 136.48 ? 581  PHE B CE2 1 
ATOM   9242  C  CZ  . PHE B  1  555 ? 16.056  24.809  -26.773 1.00 136.35 ? 581  PHE B CZ  1 
ATOM   9243  N  N   . ALA B  1  556 ? 13.714  30.645  -23.227 1.00 146.85 ? 582  ALA B N   1 
ATOM   9244  C  CA  . ALA B  1  556 ? 13.150  31.958  -22.931 1.00 149.90 ? 582  ALA B CA  1 
ATOM   9245  C  C   . ALA B  1  556 ? 13.415  32.858  -24.140 1.00 152.53 ? 582  ALA B C   1 
ATOM   9246  O  O   . ALA B  1  556 ? 14.514  33.403  -24.288 1.00 152.84 ? 582  ALA B O   1 
ATOM   9247  C  CB  . ALA B  1  556 ? 13.810  32.542  -21.687 1.00 148.90 ? 582  ALA B CB  1 
ATOM   9248  N  N   . CYS B  1  557 ? 12.413  33.001  -25.008 1.00 155.48 ? 583  CYS B N   1 
ATOM   9249  C  CA  . CYS B  1  557 ? 12.552  33.818  -26.211 1.00 158.23 ? 583  CYS B CA  1 
ATOM   9250  C  C   . CYS B  1  557 ? 12.033  35.252  -26.043 1.00 159.80 ? 583  CYS B C   1 
ATOM   9251  O  O   . CYS B  1  557 ? 11.133  35.695  -26.763 1.00 159.82 ? 583  CYS B O   1 
ATOM   9252  C  CB  . CYS B  1  557 ? 11.860  33.131  -27.405 1.00 158.85 ? 583  CYS B CB  1 
ATOM   9253  S  SG  . CYS B  1  557 ? 12.584  31.512  -27.857 1.00 160.24 ? 583  CYS B SG  1 
ATOM   9254  N  N   . THR B  1  558 ? 12.614  35.957  -25.073 1.00 161.65 ? 584  THR B N   1 
ATOM   9255  C  CA  . THR B  1  558 ? 12.300  37.355  -24.774 1.00 162.97 ? 584  THR B CA  1 
ATOM   9256  C  C   . THR B  1  558 ? 13.677  38.019  -24.670 1.00 164.64 ? 584  THR B C   1 
ATOM   9257  O  O   . THR B  1  558 ? 14.642  37.361  -24.274 1.00 164.61 ? 584  THR B O   1 
ATOM   9258  C  CB  . THR B  1  558 ? 11.555  37.503  -23.425 1.00 162.09 ? 584  THR B CB  1 
ATOM   9259  O  OG1 . THR B  1  558 ? 12.436  37.160  -22.346 1.00 161.06 ? 584  THR B OG1 1 
ATOM   9260  C  CG2 . THR B  1  558 ? 10.327  36.598  -23.388 1.00 161.28 ? 584  THR B CG2 1 
ATOM   9261  N  N   . CYS B  1  559 ? 13.787  39.301  -25.016 1.00 166.44 ? 585  CYS B N   1 
ATOM   9262  C  CA  . CYS B  1  559 ? 15.095  39.954  -24.971 1.00 168.32 ? 585  CYS B CA  1 
ATOM   9263  C  C   . CYS B  1  559 ? 15.830  39.735  -23.644 1.00 168.52 ? 585  CYS B C   1 
ATOM   9264  O  O   . CYS B  1  559 ? 17.053  39.879  -23.572 1.00 168.75 ? 585  CYS B O   1 
ATOM   9265  C  CB  . CYS B  1  559 ? 14.993  41.467  -25.268 1.00 169.72 ? 585  CYS B CB  1 
ATOM   9266  S  SG  . CYS B  1  559 ? 16.659  42.224  -25.352 1.00 172.82 ? 585  CYS B SG  1 
ATOM   9267  N  N   . GLU B  1  560 ? 15.088  39.373  -22.601 1.00 168.39 ? 586  GLU B N   1 
ATOM   9268  C  CA  . GLU B  1  560 ? 15.670  39.137  -21.282 1.00 168.17 ? 586  GLU B CA  1 
ATOM   9269  C  C   . GLU B  1  560 ? 16.906  38.243  -21.346 1.00 168.12 ? 586  GLU B C   1 
ATOM   9270  O  O   . GLU B  1  560 ? 17.852  38.413  -20.572 1.00 167.45 ? 586  GLU B O   1 
ATOM   9271  C  CB  . GLU B  1  560 ? 14.626  38.503  -20.364 1.00 168.09 ? 586  GLU B CB  1 
ATOM   9272  C  CG  . GLU B  1  560 ? 15.112  38.257  -18.954 1.00 168.52 ? 586  GLU B CG  1 
ATOM   9273  C  CD  . GLU B  1  560 ? 14.091  37.516  -18.122 1.00 168.88 ? 586  GLU B CD  1 
ATOM   9274  O  OE1 . GLU B  1  560 ? 13.709  36.397  -18.520 1.00 169.16 ? 586  GLU B OE1 1 
ATOM   9275  O  OE2 . GLU B  1  560 ? 13.668  38.049  -17.074 1.00 168.83 ? 586  GLU B OE2 1 
ATOM   9276  N  N   . HIS B  1  561 ? 16.889  37.294  -22.275 1.00 168.48 ? 587  HIS B N   1 
ATOM   9277  C  CA  . HIS B  1  561 ? 17.995  36.358  -22.445 1.00 168.70 ? 587  HIS B CA  1 
ATOM   9278  C  C   . HIS B  1  561 ? 18.548  36.394  -23.866 1.00 168.64 ? 587  HIS B C   1 
ATOM   9279  O  O   . HIS B  1  561 ? 18.669  35.363  -24.530 1.00 168.73 ? 587  HIS B O   1 
ATOM   9280  C  CB  . HIS B  1  561 ? 17.532  34.939  -22.090 1.00 168.88 ? 587  HIS B CB  1 
ATOM   9281  C  CG  . HIS B  1  561 ? 17.168  34.770  -20.646 1.00 169.03 ? 587  HIS B CG  1 
ATOM   9282  N  ND1 . HIS B  1  561 ? 18.098  34.845  -19.633 1.00 168.94 ? 587  HIS B ND1 1 
ATOM   9283  C  CD2 . HIS B  1  561 ? 15.970  34.566  -20.046 1.00 168.71 ? 587  HIS B CD2 1 
ATOM   9284  C  CE1 . HIS B  1  561 ? 17.490  34.695  -18.468 1.00 168.87 ? 587  HIS B CE1 1 
ATOM   9285  N  NE2 . HIS B  1  561 ? 16.200  34.525  -18.692 1.00 168.74 ? 587  HIS B NE2 1 
ATOM   9286  N  N   . GLN B  1  562 ? 18.875  37.599  -24.323 1.00 168.33 ? 588  GLN B N   1 
ATOM   9287  C  CA  . GLN B  1  562 ? 19.426  37.802  -25.657 1.00 167.83 ? 588  GLN B CA  1 
ATOM   9288  C  C   . GLN B  1  562 ? 20.849  37.251  -25.685 1.00 167.17 ? 588  GLN B C   1 
ATOM   9289  O  O   . GLN B  1  562 ? 21.307  36.716  -26.699 1.00 166.71 ? 588  GLN B O   1 
ATOM   9290  C  CB  . GLN B  1  562 ? 19.439  39.299  -25.983 1.00 168.34 ? 588  GLN B CB  1 
ATOM   9291  C  CG  . GLN B  1  562 ? 20.087  39.670  -27.312 1.00 168.95 ? 588  GLN B CG  1 
ATOM   9292  C  CD  . GLN B  1  562 ? 20.283  41.172  -27.460 1.00 169.27 ? 588  GLN B CD  1 
ATOM   9293  O  OE1 . GLN B  1  562 ? 20.935  41.807  -26.629 1.00 169.34 ? 588  GLN B OE1 1 
ATOM   9294  N  NE2 . GLN B  1  562 ? 19.720  41.747  -28.520 1.00 169.47 ? 588  GLN B NE2 1 
ATOM   9295  N  N   . SER B  1  563 ? 21.535  37.379  -24.553 1.00 166.41 ? 589  SER B N   1 
ATOM   9296  C  CA  . SER B  1  563 ? 22.915  36.926  -24.412 1.00 165.65 ? 589  SER B CA  1 
ATOM   9297  C  C   . SER B  1  563 ? 23.102  35.419  -24.607 1.00 165.37 ? 589  SER B C   1 
ATOM   9298  O  O   . SER B  1  563 ? 24.074  34.980  -25.226 1.00 165.23 ? 589  SER B O   1 
ATOM   9299  C  CB  . SER B  1  563 ? 23.451  37.342  -23.040 1.00 165.18 ? 589  SER B CB  1 
ATOM   9300  O  OG  . SER B  1  563 ? 24.816  36.997  -22.902 1.00 164.81 ? 589  SER B OG  1 
ATOM   9301  N  N   . PHE B  1  564 ? 22.168  34.633  -24.080 1.00 164.83 ? 590  PHE B N   1 
ATOM   9302  C  CA  . PHE B  1  564 ? 22.228  33.175  -24.187 1.00 163.90 ? 590  PHE B CA  1 
ATOM   9303  C  C   . PHE B  1  564 ? 21.548  32.634  -25.459 1.00 162.89 ? 590  PHE B C   1 
ATOM   9304  O  O   . PHE B  1  564 ? 22.067  31.715  -26.101 1.00 162.78 ? 590  PHE B O   1 
ATOM   9305  C  CB  . PHE B  1  564 ? 21.601  32.548  -22.930 1.00 163.94 ? 590  PHE B CB  1 
ATOM   9306  C  CG  . PHE B  1  564 ? 21.582  31.042  -22.937 1.00 164.01 ? 590  PHE B CG  1 
ATOM   9307  C  CD1 . PHE B  1  564 ? 22.766  30.313  -23.051 1.00 163.98 ? 590  PHE B CD1 1 
ATOM   9308  C  CD2 . PHE B  1  564 ? 20.376  30.353  -22.820 1.00 163.60 ? 590  PHE B CD2 1 
ATOM   9309  C  CE1 . PHE B  1  564 ? 22.748  28.917  -23.053 1.00 163.69 ? 590  PHE B CE1 1 
ATOM   9310  C  CE2 . PHE B  1  564 ? 20.342  28.965  -22.822 1.00 163.51 ? 590  PHE B CE2 1 
ATOM   9311  C  CZ  . PHE B  1  564 ? 21.532  28.241  -22.936 1.00 163.78 ? 590  PHE B CZ  1 
ATOM   9312  N  N   . LEU B  1  565 ? 20.401  33.207  -25.825 1.00 161.44 ? 591  LEU B N   1 
ATOM   9313  C  CA  . LEU B  1  565 ? 19.668  32.764  -27.010 1.00 160.22 ? 591  LEU B CA  1 
ATOM   9314  C  C   . LEU B  1  565 ? 20.502  32.987  -28.265 1.00 160.25 ? 591  LEU B C   1 
ATOM   9315  O  O   . LEU B  1  565 ? 20.271  32.363  -29.301 1.00 160.11 ? 591  LEU B O   1 
ATOM   9316  C  CB  . LEU B  1  565 ? 18.335  33.514  -27.116 1.00 159.17 ? 591  LEU B CB  1 
ATOM   9317  C  CG  . LEU B  1  565 ? 17.273  32.978  -28.084 1.00 158.76 ? 591  LEU B CG  1 
ATOM   9318  C  CD1 . LEU B  1  565 ? 15.898  33.407  -27.601 1.00 157.80 ? 591  LEU B CD1 1 
ATOM   9319  C  CD2 . LEU B  1  565 ? 17.538  33.471  -29.504 1.00 158.42 ? 591  LEU B CD2 1 
ATOM   9320  N  N   . GLN B  1  566 ? 21.481  33.881  -28.155 1.00 160.54 ? 592  GLN B N   1 
ATOM   9321  C  CA  . GLN B  1  566 ? 22.377  34.199  -29.263 1.00 160.79 ? 592  GLN B CA  1 
ATOM   9322  C  C   . GLN B  1  566 ? 23.460  33.120  -29.384 1.00 160.84 ? 592  GLN B C   1 
ATOM   9323  O  O   . GLN B  1  566 ? 23.753  32.641  -30.481 1.00 161.01 ? 592  GLN B O   1 
ATOM   9324  C  CB  . GLN B  1  566 ? 23.021  35.574  -29.031 1.00 160.69 ? 592  GLN B CB  1 
ATOM   9325  C  CG  . GLN B  1  566 ? 24.093  35.968  -30.044 1.00 160.38 ? 592  GLN B CG  1 
ATOM   9326  C  CD  . GLN B  1  566 ? 23.556  36.188  -31.447 1.00 160.02 ? 592  GLN B CD  1 
ATOM   9327  O  OE1 . GLN B  1  566 ? 24.325  36.336  -32.395 1.00 159.80 ? 592  GLN B OE1 1 
ATOM   9328  N  NE2 . GLN B  1  566 ? 22.234  36.218  -31.584 1.00 159.78 ? 592  GLN B NE2 1 
ATOM   9329  N  N   . TRP B  1  567 ? 24.041  32.740  -28.247 1.00 160.57 ? 593  TRP B N   1 
ATOM   9330  C  CA  . TRP B  1  567 ? 25.089  31.722  -28.203 1.00 160.09 ? 593  TRP B CA  1 
ATOM   9331  C  C   . TRP B  1  567 ? 24.654  30.434  -28.899 1.00 159.48 ? 593  TRP B C   1 
ATOM   9332  O  O   . TRP B  1  567 ? 25.478  29.698  -29.447 1.00 158.92 ? 593  TRP B O   1 
ATOM   9333  C  CB  . TRP B  1  567 ? 25.451  31.428  -26.751 1.00 160.51 ? 593  TRP B CB  1 
ATOM   9334  C  CG  . TRP B  1  567 ? 26.431  30.324  -26.600 1.00 161.40 ? 593  TRP B CG  1 
ATOM   9335  C  CD1 . TRP B  1  567 ? 27.767  30.362  -26.884 1.00 161.39 ? 593  TRP B CD1 1 
ATOM   9336  C  CD2 . TRP B  1  567 ? 26.155  29.001  -26.135 1.00 162.08 ? 593  TRP B CD2 1 
ATOM   9337  N  NE1 . TRP B  1  567 ? 28.340  29.139  -26.622 1.00 161.74 ? 593  TRP B NE1 1 
ATOM   9338  C  CE2 . TRP B  1  567 ? 27.371  28.286  -26.160 1.00 162.10 ? 593  TRP B CE2 1 
ATOM   9339  C  CE3 . TRP B  1  567 ? 24.994  28.350  -25.699 1.00 162.47 ? 593  TRP B CE3 1 
ATOM   9340  C  CZ2 . TRP B  1  567 ? 27.458  26.944  -25.761 1.00 162.26 ? 593  TRP B CZ2 1 
ATOM   9341  C  CZ3 . TRP B  1  567 ? 25.082  27.016  -25.305 1.00 162.63 ? 593  TRP B CZ3 1 
ATOM   9342  C  CH2 . TRP B  1  567 ? 26.307  26.330  -25.339 1.00 162.58 ? 593  TRP B CH2 1 
ATOM   9343  N  N   . ILE B  1  568 ? 23.352  30.169  -28.865 1.00 159.14 ? 594  ILE B N   1 
ATOM   9344  C  CA  . ILE B  1  568 ? 22.775  28.988  -29.497 1.00 158.96 ? 594  ILE B CA  1 
ATOM   9345  C  C   . ILE B  1  568 ? 22.968  29.094  -31.011 1.00 159.08 ? 594  ILE B C   1 
ATOM   9346  O  O   . ILE B  1  568 ? 23.362  28.129  -31.674 1.00 159.15 ? 594  ILE B O   1 
ATOM   9347  C  CB  . ILE B  1  568 ? 21.260  28.885  -29.184 1.00 158.48 ? 594  ILE B CB  1 
ATOM   9348  C  CG1 . ILE B  1  568 ? 21.048  28.846  -27.668 1.00 158.23 ? 594  ILE B CG1 1 
ATOM   9349  C  CG2 . ILE B  1  568 ? 20.665  27.656  -29.842 1.00 158.55 ? 594  ILE B CG2 1 
ATOM   9350  C  CD1 . ILE B  1  568 ? 21.738  27.692  -26.964 1.00 157.39 ? 594  ILE B CD1 1 
ATOM   9351  N  N   . LYS B  1  569 ? 22.690  30.280  -31.544 1.00 158.89 ? 595  LYS B N   1 
ATOM   9352  C  CA  . LYS B  1  569 ? 22.838  30.543  -32.970 1.00 158.55 ? 595  LYS B CA  1 
ATOM   9353  C  C   . LYS B  1  569 ? 24.320  30.480  -33.338 1.00 158.19 ? 595  LYS B C   1 
ATOM   9354  O  O   . LYS B  1  569 ? 24.705  29.796  -34.286 1.00 158.00 ? 595  LYS B O   1 
ATOM   9355  C  CB  . LYS B  1  569 ? 22.304  31.938  -33.318 1.00 158.78 ? 595  LYS B CB  1 
ATOM   9356  C  CG  . LYS B  1  569 ? 20.849  32.214  -32.954 1.00 159.07 ? 595  LYS B CG  1 
ATOM   9357  C  CD  . LYS B  1  569 ? 20.557  33.714  -33.064 1.00 159.05 ? 595  LYS B CD  1 
ATOM   9358  C  CE  . LYS B  1  569 ? 19.100  34.052  -32.785 1.00 159.17 ? 595  LYS B CE  1 
ATOM   9359  N  NZ  . LYS B  1  569 ? 18.204  33.593  -33.881 1.00 159.01 ? 595  LYS B NZ  1 
ATOM   9360  N  N   . ASP B  1  570 ? 25.135  31.201  -32.567 1.00 157.89 ? 596  ASP B N   1 
ATOM   9361  C  CA  . ASP B  1  570 ? 26.583  31.288  -32.778 1.00 157.61 ? 596  ASP B CA  1 
ATOM   9362  C  C   . ASP B  1  570 ? 27.279  29.976  -33.135 1.00 157.32 ? 596  ASP B C   1 
ATOM   9363  O  O   . ASP B  1  570 ? 28.240  29.976  -33.908 1.00 157.56 ? 596  ASP B O   1 
ATOM   9364  C  CB  . ASP B  1  570 ? 27.274  31.898  -31.551 1.00 157.59 ? 596  ASP B CB  1 
ATOM   9365  C  CG  . ASP B  1  570 ? 26.900  33.353  -31.327 1.00 157.66 ? 596  ASP B CG  1 
ATOM   9366  O  OD1 . ASP B  1  570 ? 26.957  34.148  -32.292 1.00 157.40 ? 596  ASP B OD1 1 
ATOM   9367  O  OD2 . ASP B  1  570 ? 26.562  33.706  -30.179 1.00 157.49 ? 596  ASP B OD2 1 
ATOM   9368  N  N   . GLN B  1  571 ? 26.819  28.867  -32.566 1.00 156.48 ? 597  GLN B N   1 
ATOM   9369  C  CA  . GLN B  1  571 ? 27.424  27.573  -32.866 1.00 154.85 ? 597  GLN B CA  1 
ATOM   9370  C  C   . GLN B  1  571 ? 26.394  26.504  -33.191 1.00 153.49 ? 597  GLN B C   1 
ATOM   9371  O  O   . GLN B  1  571 ? 26.232  25.534  -32.454 1.00 153.38 ? 597  GLN B O   1 
ATOM   9372  C  CB  . GLN B  1  571 ? 28.320  27.109  -31.711 1.00 154.83 ? 597  GLN B CB  1 
ATOM   9373  C  CG  . GLN B  1  571 ? 27.788  27.407  -30.323 1.00 154.83 ? 597  GLN B CG  1 
ATOM   9374  C  CD  . GLN B  1  571 ? 28.742  26.944  -29.240 1.00 154.66 ? 597  GLN B CD  1 
ATOM   9375  O  OE1 . GLN B  1  571 ? 28.866  25.751  -28.979 1.00 154.64 ? 597  GLN B OE1 1 
ATOM   9376  N  NE2 . GLN B  1  571 ? 29.434  27.889  -28.614 1.00 154.55 ? 597  GLN B NE2 1 
ATOM   9377  N  N   . ARG B  1  572 ? 25.695  26.699  -34.304 1.00 151.69 ? 598  ARG B N   1 
ATOM   9378  C  CA  . ARG B  1  572 ? 24.695  25.747  -34.749 1.00 149.62 ? 598  ARG B CA  1 
ATOM   9379  C  C   . ARG B  1  572 ? 25.408  24.694  -35.587 1.00 147.74 ? 598  ARG B C   1 
ATOM   9380  O  O   . ARG B  1  572 ? 24.790  23.964  -36.360 1.00 147.03 ? 598  ARG B O   1 
ATOM   9381  C  CB  . ARG B  1  572 ? 23.606  26.450  -35.565 1.00 150.47 ? 598  ARG B CB  1 
ATOM   9382  C  CG  . ARG B  1  572 ? 24.088  27.182  -36.810 1.00 151.26 ? 598  ARG B CG  1 
ATOM   9383  C  CD  . ARG B  1  572 ? 22.944  27.972  -37.426 1.00 151.75 ? 598  ARG B CD  1 
ATOM   9384  N  NE  . ARG B  1  572 ? 21.788  27.121  -37.696 1.00 152.88 ? 598  ARG B NE  1 
ATOM   9385  C  CZ  . ARG B  1  572 ? 20.566  27.575  -37.962 1.00 153.16 ? 598  ARG B CZ  1 
ATOM   9386  N  NH1 . ARG B  1  572 ? 20.333  28.879  -37.993 1.00 153.01 ? 598  ARG B NH1 1 
ATOM   9387  N  NH2 . ARG B  1  572 ? 19.574  26.724  -38.193 1.00 153.24 ? 598  ARG B NH2 1 
ATOM   9388  N  N   . GLN B  1  573 ? 26.724  24.638  -35.428 1.00 145.93 ? 599  GLN B N   1 
ATOM   9389  C  CA  . GLN B  1  573 ? 27.538  23.666  -36.137 1.00 144.91 ? 599  GLN B CA  1 
ATOM   9390  C  C   . GLN B  1  573 ? 27.874  22.520  -35.196 1.00 143.90 ? 599  GLN B C   1 
ATOM   9391  O  O   . GLN B  1  573 ? 28.712  21.671  -35.502 1.00 143.78 ? 599  GLN B O   1 
ATOM   9392  C  CB  . GLN B  1  573 ? 28.825  24.307  -36.650 1.00 145.91 ? 599  GLN B CB  1 
ATOM   9393  C  CG  . GLN B  1  573 ? 28.676  24.957  -38.014 1.00 147.22 ? 599  GLN B CG  1 
ATOM   9394  C  CD  . GLN B  1  573 ? 28.097  24.006  -39.048 1.00 147.63 ? 599  GLN B CD  1 
ATOM   9395  O  OE1 . GLN B  1  573 ? 28.591  22.890  -39.231 1.00 147.53 ? 599  GLN B OE1 1 
ATOM   9396  N  NE2 . GLN B  1  573 ? 27.047  24.448  -39.737 1.00 147.59 ? 599  GLN B NE2 1 
ATOM   9397  N  N   . LEU B  1  574 ? 27.216  22.517  -34.041 1.00 142.28 ? 600  LEU B N   1 
ATOM   9398  C  CA  . LEU B  1  574 ? 27.406  21.479  -33.037 1.00 140.06 ? 600  LEU B CA  1 
ATOM   9399  C  C   . LEU B  1  574 ? 26.052  20.865  -32.704 1.00 139.21 ? 600  LEU B C   1 
ATOM   9400  O  O   . LEU B  1  574 ? 25.960  19.686  -32.369 1.00 139.54 ? 600  LEU B O   1 
ATOM   9401  C  CB  . LEU B  1  574 ? 28.030  22.061  -31.764 1.00 139.22 ? 600  LEU B CB  1 
ATOM   9402  C  CG  . LEU B  1  574 ? 29.476  22.557  -31.825 1.00 138.53 ? 600  LEU B CG  1 
ATOM   9403  C  CD1 . LEU B  1  574 ? 29.854  23.176  -30.487 1.00 138.71 ? 600  LEU B CD1 1 
ATOM   9404  C  CD2 . LEU B  1  574 ? 30.407  21.405  -32.159 1.00 137.41 ? 600  LEU B CD2 1 
ATOM   9405  N  N   . LEU B  1  575 ? 25.002  21.672  -32.811 1.00 138.26 ? 601  LEU B N   1 
ATOM   9406  C  CA  . LEU B  1  575 ? 23.641  21.230  -32.511 1.00 137.95 ? 601  LEU B CA  1 
ATOM   9407  C  C   . LEU B  1  575 ? 23.145  20.037  -33.316 1.00 137.66 ? 601  LEU B C   1 
ATOM   9408  O  O   . LEU B  1  575 ? 23.905  19.386  -34.031 1.00 137.31 ? 601  LEU B O   1 
ATOM   9409  C  CB  . LEU B  1  575 ? 22.661  22.391  -32.692 1.00 137.49 ? 601  LEU B CB  1 
ATOM   9410  C  CG  . LEU B  1  575 ? 22.544  23.375  -31.527 1.00 137.16 ? 601  LEU B CG  1 
ATOM   9411  C  CD1 . LEU B  1  575 ? 21.776  24.606  -31.967 1.00 136.95 ? 601  LEU B CD1 1 
ATOM   9412  C  CD2 . LEU B  1  575 ? 21.854  22.691  -30.356 1.00 136.88 ? 601  LEU B CD2 1 
ATOM   9413  N  N   . VAL B  1  576 ? 21.853  19.763  -33.176 1.00 137.54 ? 602  VAL B N   1 
ATOM   9414  C  CA  . VAL B  1  576 ? 21.203  18.661  -33.872 1.00 137.76 ? 602  VAL B CA  1 
ATOM   9415  C  C   . VAL B  1  576 ? 19.833  19.116  -34.373 1.00 138.52 ? 602  VAL B C   1 
ATOM   9416  O  O   . VAL B  1  576 ? 19.671  20.272  -34.759 1.00 138.28 ? 602  VAL B O   1 
ATOM   9417  C  CB  . VAL B  1  576 ? 21.044  17.446  -32.942 1.00 137.11 ? 602  VAL B CB  1 
ATOM   9418  C  CG1 . VAL B  1  576 ? 22.413  16.865  -32.606 1.00 136.30 ? 602  VAL B CG1 1 
ATOM   9419  C  CG2 . VAL B  1  576 ? 20.332  17.864  -31.674 1.00 136.81 ? 602  VAL B CG2 1 
ATOM   9420  N  N   . GLU B  1  577 ? 18.856  18.214  -34.367 1.00 139.79 ? 603  GLU B N   1 
ATOM   9421  C  CA  . GLU B  1  577 ? 17.498  18.518  -34.829 1.00 141.49 ? 603  GLU B CA  1 
ATOM   9422  C  C   . GLU B  1  577 ? 17.000  19.895  -34.380 1.00 142.37 ? 603  GLU B C   1 
ATOM   9423  O  O   . GLU B  1  577 ? 16.493  20.042  -33.268 1.00 142.49 ? 603  GLU B O   1 
ATOM   9424  C  CB  . GLU B  1  577 ? 16.536  17.453  -34.315 1.00 141.80 ? 603  GLU B CB  1 
ATOM   9425  C  CG  . GLU B  1  577 ? 16.940  16.039  -34.652 1.00 142.34 ? 603  GLU B CG  1 
ATOM   9426  C  CD  . GLU B  1  577 ? 16.253  15.027  -33.760 1.00 143.14 ? 603  GLU B CD  1 
ATOM   9427  O  OE1 . GLU B  1  577 ? 16.571  14.982  -32.551 1.00 143.62 ? 603  GLU B OE1 1 
ATOM   9428  O  OE2 . GLU B  1  577 ? 15.389  14.281  -34.263 1.00 143.71 ? 603  GLU B OE2 1 
ATOM   9429  N  N   . VAL B  1  578 ? 17.115  20.891  -35.254 1.00 143.22 ? 604  VAL B N   1 
ATOM   9430  C  CA  . VAL B  1  578 ? 16.690  22.246  -34.919 1.00 144.13 ? 604  VAL B CA  1 
ATOM   9431  C  C   . VAL B  1  578 ? 15.180  22.491  -35.033 1.00 145.35 ? 604  VAL B C   1 
ATOM   9432  O  O   . VAL B  1  578 ? 14.654  23.409  -34.401 1.00 145.49 ? 604  VAL B O   1 
ATOM   9433  C  CB  . VAL B  1  578 ? 17.447  23.287  -35.782 1.00 143.81 ? 604  VAL B CB  1 
ATOM   9434  C  CG1 . VAL B  1  578 ? 17.028  24.701  -35.399 1.00 143.73 ? 604  VAL B CG1 1 
ATOM   9435  C  CG2 . VAL B  1  578 ? 18.946  23.118  -35.593 1.00 143.25 ? 604  VAL B CG2 1 
ATOM   9436  N  N   . GLU B  1  579 ? 14.479  21.675  -35.819 1.00 146.50 ? 605  GLU B N   1 
ATOM   9437  C  CA  . GLU B  1  579 ? 13.031  21.843  -35.971 1.00 147.84 ? 605  GLU B CA  1 
ATOM   9438  C  C   . GLU B  1  579 ? 12.271  21.357  -34.735 1.00 148.43 ? 605  GLU B C   1 
ATOM   9439  O  O   . GLU B  1  579 ? 11.041  21.260  -34.739 1.00 148.12 ? 605  GLU B O   1 
ATOM   9440  C  CB  . GLU B  1  579 ? 12.513  21.098  -37.212 1.00 148.11 ? 605  GLU B CB  1 
ATOM   9441  C  CG  . GLU B  1  579 ? 12.667  19.584  -37.188 1.00 148.81 ? 605  GLU B CG  1 
ATOM   9442  C  CD  . GLU B  1  579 ? 14.078  19.131  -37.508 1.00 149.54 ? 605  GLU B CD  1 
ATOM   9443  O  OE1 . GLU B  1  579 ? 14.555  19.423  -38.623 1.00 150.07 ? 605  GLU B OE1 1 
ATOM   9444  O  OE2 . GLU B  1  579 ? 14.710  18.485  -36.646 1.00 150.19 ? 605  GLU B OE2 1 
ATOM   9445  N  N   . ARG B  1  580 ? 13.019  21.054  -33.678 1.00 149.09 ? 606  ARG B N   1 
ATOM   9446  C  CA  . ARG B  1  580 ? 12.440  20.577  -32.430 1.00 149.64 ? 606  ARG B CA  1 
ATOM   9447  C  C   . ARG B  1  580 ? 12.936  21.407  -31.252 1.00 149.66 ? 606  ARG B C   1 
ATOM   9448  O  O   . ARG B  1  580 ? 12.821  20.988  -30.100 1.00 149.99 ? 606  ARG B O   1 
ATOM   9449  C  CB  . ARG B  1  580 ? 12.803  19.105  -32.198 1.00 150.16 ? 606  ARG B CB  1 
ATOM   9450  C  CG  . ARG B  1  580 ? 12.020  18.098  -33.042 1.00 150.59 ? 606  ARG B CG  1 
ATOM   9451  C  CD  . ARG B  1  580 ? 12.441  16.674  -32.694 1.00 150.80 ? 606  ARG B CD  1 
ATOM   9452  N  NE  . ARG B  1  580 ? 12.375  16.439  -31.253 1.00 151.36 ? 606  ARG B NE  1 
ATOM   9453  C  CZ  . ARG B  1  580 ? 12.867  15.367  -30.642 1.00 151.34 ? 606  ARG B CZ  1 
ATOM   9454  N  NH1 . ARG B  1  580 ? 13.466  14.413  -31.343 1.00 151.13 ? 606  ARG B NH1 1 
ATOM   9455  N  NH2 . ARG B  1  580 ? 12.772  15.259  -29.321 1.00 151.13 ? 606  ARG B NH2 1 
ATOM   9456  N  N   . MET B  1  581 ? 13.499  22.576  -31.543 1.00 149.38 ? 607  MET B N   1 
ATOM   9457  C  CA  . MET B  1  581 ? 14.001  23.462  -30.495 1.00 149.27 ? 607  MET B CA  1 
ATOM   9458  C  C   . MET B  1  581 ? 13.069  24.655  -30.308 1.00 149.99 ? 607  MET B C   1 
ATOM   9459  O  O   . MET B  1  581 ? 13.507  25.757  -29.988 1.00 150.00 ? 607  MET B O   1 
ATOM   9460  C  CB  . MET B  1  581 ? 15.412  23.949  -30.833 1.00 147.99 ? 607  MET B CB  1 
ATOM   9461  C  CG  . MET B  1  581 ? 16.480  22.882  -30.720 1.00 146.98 ? 607  MET B CG  1 
ATOM   9462  S  SD  . MET B  1  581 ? 18.134  23.513  -31.046 1.00 146.46 ? 607  MET B SD  1 
ATOM   9463  C  CE  . MET B  1  581 ? 18.616  24.103  -29.420 1.00 145.88 ? 607  MET B CE  1 
ATOM   9464  N  N   . GLU B  1  582 ? 11.778  24.413  -30.508 1.00 151.12 ? 608  GLU B N   1 
ATOM   9465  C  CA  . GLU B  1  582 ? 10.741  25.434  -30.378 1.00 152.51 ? 608  GLU B CA  1 
ATOM   9466  C  C   . GLU B  1  582 ? 10.836  26.268  -29.094 1.00 153.88 ? 608  GLU B C   1 
ATOM   9467  O  O   . GLU B  1  582 ? 11.316  25.795  -28.062 1.00 153.92 ? 608  GLU B O   1 
ATOM   9468  C  CB  . GLU B  1  582 ? 9.365   24.762  -30.466 1.00 151.90 ? 608  GLU B CB  1 
ATOM   9469  C  CG  . GLU B  1  582 ? 9.058   24.183  -31.847 1.00 151.74 ? 608  GLU B CG  1 
ATOM   9470  C  CD  . GLU B  1  582 ? 8.018   23.075  -31.818 1.00 151.39 ? 608  GLU B CD  1 
ATOM   9471  O  OE1 . GLU B  1  582 ? 8.388   21.918  -31.517 1.00 151.23 ? 608  GLU B OE1 1 
ATOM   9472  O  OE2 . GLU B  1  582 ? 6.831   23.359  -32.097 1.00 150.91 ? 608  GLU B OE2 1 
ATOM   9473  N  N   . CYS B  1  583 ? 10.379  27.517  -29.171 1.00 155.73 ? 609  CYS B N   1 
ATOM   9474  C  CA  . CYS B  1  583 ? 10.391  28.419  -28.019 1.00 157.12 ? 609  CYS B CA  1 
ATOM   9475  C  C   . CYS B  1  583 ? 9.335   27.961  -27.026 1.00 157.37 ? 609  CYS B C   1 
ATOM   9476  O  O   . CYS B  1  583 ? 8.620   26.988  -27.272 1.00 156.81 ? 609  CYS B O   1 
ATOM   9477  C  CB  . CYS B  1  583 ? 10.077  29.864  -28.437 1.00 158.16 ? 609  CYS B CB  1 
ATOM   9478  S  SG  . CYS B  1  583 ? 11.381  30.775  -29.330 1.00 159.65 ? 609  CYS B SG  1 
ATOM   9479  N  N   . ALA B  1  584 ? 9.226   28.674  -25.909 1.00 157.84 ? 610  ALA B N   1 
ATOM   9480  C  CA  . ALA B  1  584 ? 8.247   28.311  -24.900 1.00 158.53 ? 610  ALA B CA  1 
ATOM   9481  C  C   . ALA B  1  584 ? 7.651   29.488  -24.138 1.00 159.21 ? 610  ALA B C   1 
ATOM   9482  O  O   . ALA B  1  584 ? 6.472   29.458  -23.793 1.00 159.15 ? 610  ALA B O   1 
ATOM   9483  C  CB  . ALA B  1  584 ? 8.861   27.324  -23.918 1.00 158.37 ? 610  ALA B CB  1 
ATOM   9484  N  N   . THR B  1  585 ? 8.448   30.528  -23.888 1.00 160.11 ? 611  THR B N   1 
ATOM   9485  C  CA  . THR B  1  585 ? 7.967   31.680  -23.121 1.00 161.09 ? 611  THR B CA  1 
ATOM   9486  C  C   . THR B  1  585 ? 7.000   32.681  -23.782 1.00 162.11 ? 611  THR B C   1 
ATOM   9487  O  O   . THR B  1  585 ? 6.020   33.093  -23.154 1.00 162.49 ? 611  THR B O   1 
ATOM   9488  C  CB  . THR B  1  585 ? 9.148   32.463  -22.508 1.00 160.63 ? 611  THR B CB  1 
ATOM   9489  O  OG1 . THR B  1  585 ? 10.136  32.720  -23.513 1.00 160.57 ? 611  THR B OG1 1 
ATOM   9490  C  CG2 . THR B  1  585 ? 9.768   31.671  -21.375 1.00 160.33 ? 611  THR B CG2 1 
ATOM   9491  N  N   . PRO B  1  586 ? 7.260   33.107  -25.034 1.00 162.47 ? 612  PRO B N   1 
ATOM   9492  C  CA  . PRO B  1  586 ? 6.299   34.058  -25.614 1.00 162.38 ? 612  PRO B CA  1 
ATOM   9493  C  C   . PRO B  1  586 ? 4.941   33.392  -25.888 1.00 162.48 ? 612  PRO B C   1 
ATOM   9494  O  O   . PRO B  1  586 ? 4.829   32.559  -26.789 1.00 162.24 ? 612  PRO B O   1 
ATOM   9495  C  CB  . PRO B  1  586 ? 6.994   34.509  -26.900 1.00 162.18 ? 612  PRO B CB  1 
ATOM   9496  C  CG  . PRO B  1  586 ? 8.456   34.352  -26.573 1.00 161.90 ? 612  PRO B CG  1 
ATOM   9497  C  CD  . PRO B  1  586 ? 8.477   33.026  -25.861 1.00 162.17 ? 612  PRO B CD  1 
ATOM   9498  N  N   . SER B  1  587 ? 3.915   33.754  -25.114 1.00 162.63 ? 613  SER B N   1 
ATOM   9499  C  CA  . SER B  1  587 ? 2.585   33.163  -25.288 1.00 163.15 ? 613  SER B CA  1 
ATOM   9500  C  C   . SER B  1  587 ? 2.033   33.471  -26.676 1.00 164.07 ? 613  SER B C   1 
ATOM   9501  O  O   . SER B  1  587 ? 0.977   32.962  -27.066 1.00 163.81 ? 613  SER B O   1 
ATOM   9502  C  CB  . SER B  1  587 ? 1.612   33.680  -24.220 1.00 162.16 ? 613  SER B CB  1 
ATOM   9503  O  OG  . SER B  1  587 ? 1.299   35.044  -24.416 1.00 160.98 ? 613  SER B OG  1 
ATOM   9504  N  N   . ASP B  1  588 ? 2.763   34.306  -27.411 1.00 165.30 ? 614  ASP B N   1 
ATOM   9505  C  CA  . ASP B  1  588 ? 2.394   34.705  -28.770 1.00 166.32 ? 614  ASP B CA  1 
ATOM   9506  C  C   . ASP B  1  588 ? 3.424   34.164  -29.778 1.00 166.50 ? 614  ASP B C   1 
ATOM   9507  O  O   . ASP B  1  588 ? 3.094   33.898  -30.937 1.00 166.51 ? 614  ASP B O   1 
ATOM   9508  C  CB  . ASP B  1  588 ? 2.323   36.242  -28.875 1.00 166.81 ? 614  ASP B CB  1 
ATOM   9509  C  CG  . ASP B  1  588 ? 1.195   36.848  -28.039 1.00 166.91 ? 614  ASP B CG  1 
ATOM   9510  O  OD1 . ASP B  1  588 ? 0.012   36.604  -28.357 1.00 166.78 ? 614  ASP B OD1 1 
ATOM   9511  O  OD2 . ASP B  1  588 ? 1.493   37.571  -27.064 1.00 167.03 ? 614  ASP B OD2 1 
ATOM   9512  N  N   . LYS B  1  589 ? 4.669   34.006  -29.328 1.00 166.37 ? 615  LYS B N   1 
ATOM   9513  C  CA  . LYS B  1  589 ? 5.742   33.493  -30.181 1.00 165.81 ? 615  LYS B CA  1 
ATOM   9514  C  C   . LYS B  1  589 ? 6.335   32.198  -29.607 1.00 165.35 ? 615  LYS B C   1 
ATOM   9515  O  O   . LYS B  1  589 ? 7.399   32.202  -28.984 1.00 165.04 ? 615  LYS B O   1 
ATOM   9516  C  CB  . LYS B  1  589 ? 6.845   34.549  -30.346 1.00 165.66 ? 615  LYS B CB  1 
ATOM   9517  C  CG  . LYS B  1  589 ? 6.370   35.881  -30.936 1.00 165.53 ? 615  LYS B CG  1 
ATOM   9518  C  CD  . LYS B  1  589 ? 5.677   35.707  -32.290 1.00 165.44 ? 615  LYS B CD  1 
ATOM   9519  C  CE  . LYS B  1  589 ? 6.615   35.141  -33.350 1.00 165.62 ? 615  LYS B CE  1 
ATOM   9520  N  NZ  . LYS B  1  589 ? 7.777   36.034  -33.627 1.00 165.87 ? 615  LYS B NZ  1 
ATOM   9521  N  N   . GLN B  1  590 ? 5.628   31.094  -29.831 1.00 164.92 ? 616  GLN B N   1 
ATOM   9522  C  CA  . GLN B  1  590 ? 6.037   29.775  -29.357 1.00 164.48 ? 616  GLN B CA  1 
ATOM   9523  C  C   . GLN B  1  590 ? 5.914   28.749  -30.485 1.00 164.34 ? 616  GLN B C   1 
ATOM   9524  O  O   . GLN B  1  590 ? 4.836   28.570  -31.055 1.00 164.28 ? 616  GLN B O   1 
ATOM   9525  C  CB  . GLN B  1  590 ? 5.145   29.349  -28.185 1.00 164.22 ? 616  GLN B CB  1 
ATOM   9526  C  CG  . GLN B  1  590 ? 5.327   27.901  -27.739 1.00 163.55 ? 616  GLN B CG  1 
ATOM   9527  C  CD  . GLN B  1  590 ? 4.206   27.428  -26.831 1.00 163.02 ? 616  GLN B CD  1 
ATOM   9528  O  OE1 . GLN B  1  590 ? 3.970   28.004  -25.773 1.00 162.81 ? 616  GLN B OE1 1 
ATOM   9529  N  NE2 . GLN B  1  590 ? 3.507   26.376  -27.246 1.00 162.37 ? 616  GLN B NE2 1 
ATOM   9530  N  N   . GLY B  1  591 ? 7.014   28.075  -30.802 1.00 163.95 ? 617  GLY B N   1 
ATOM   9531  C  CA  . GLY B  1  591 ? 6.978   27.074  -31.853 1.00 163.82 ? 617  GLY B CA  1 
ATOM   9532  C  C   . GLY B  1  591 ? 7.875   27.424  -33.020 1.00 163.81 ? 617  GLY B C   1 
ATOM   9533  O  O   . GLY B  1  591 ? 7.999   26.656  -33.974 1.00 163.28 ? 617  GLY B O   1 
ATOM   9534  N  N   . MET B  1  592 ? 8.500   28.592  -32.939 1.00 164.25 ? 618  MET B N   1 
ATOM   9535  C  CA  . MET B  1  592 ? 9.397   29.063  -33.984 1.00 165.18 ? 618  MET B CA  1 
ATOM   9536  C  C   . MET B  1  592 ? 10.823  28.683  -33.589 1.00 165.86 ? 618  MET B C   1 
ATOM   9537  O  O   . MET B  1  592 ? 11.227  28.877  -32.443 1.00 165.42 ? 618  MET B O   1 
ATOM   9538  C  CB  . MET B  1  592 ? 9.269   30.585  -34.127 1.00 164.80 ? 618  MET B CB  1 
ATOM   9539  C  CG  . MET B  1  592 ? 9.893   31.179  -35.383 1.00 163.86 ? 618  MET B CG  1 
ATOM   9540  S  SD  . MET B  1  592 ? 9.604   32.955  -35.474 1.00 162.30 ? 618  MET B SD  1 
ATOM   9541  C  CE  . MET B  1  592 ? 7.845   32.989  -35.826 1.00 161.69 ? 618  MET B CE  1 
ATOM   9542  N  N   . PRO B  1  593 ? 11.608  28.142  -34.540 1.00 166.88 ? 619  PRO B N   1 
ATOM   9543  C  CA  . PRO B  1  593 ? 12.988  27.747  -34.238 1.00 167.67 ? 619  PRO B CA  1 
ATOM   9544  C  C   . PRO B  1  593 ? 13.824  28.856  -33.610 1.00 168.38 ? 619  PRO B C   1 
ATOM   9545  O  O   . PRO B  1  593 ? 13.892  29.963  -34.133 1.00 168.52 ? 619  PRO B O   1 
ATOM   9546  C  CB  . PRO B  1  593 ? 13.526  27.291  -35.599 1.00 167.33 ? 619  PRO B CB  1 
ATOM   9547  C  CG  . PRO B  1  593 ? 12.719  28.097  -36.575 1.00 166.94 ? 619  PRO B CG  1 
ATOM   9548  C  CD  . PRO B  1  593 ? 11.334  28.019  -35.985 1.00 166.88 ? 619  PRO B CD  1 
ATOM   9549  N  N   . VAL B  1  594 ? 14.453  28.545  -32.481 1.00 169.60 ? 620  VAL B N   1 
ATOM   9550  C  CA  . VAL B  1  594 ? 15.286  29.505  -31.764 1.00 171.20 ? 620  VAL B CA  1 
ATOM   9551  C  C   . VAL B  1  594 ? 16.429  30.033  -32.630 1.00 172.47 ? 620  VAL B C   1 
ATOM   9552  O  O   . VAL B  1  594 ? 16.925  31.142  -32.408 1.00 173.10 ? 620  VAL B O   1 
ATOM   9553  C  CB  . VAL B  1  594 ? 15.866  28.877  -30.472 1.00 171.03 ? 620  VAL B CB  1 
ATOM   9554  C  CG1 . VAL B  1  594 ? 16.827  29.845  -29.789 1.00 170.77 ? 620  VAL B CG1 1 
ATOM   9555  C  CG2 . VAL B  1  594 ? 14.730  28.518  -29.527 1.00 171.00 ? 620  VAL B CG2 1 
ATOM   9556  N  N   . LEU B  1  595 ? 16.847  29.246  -33.618 1.00 173.30 ? 621  LEU B N   1 
ATOM   9557  C  CA  . LEU B  1  595 ? 17.920  29.669  -34.514 1.00 174.15 ? 621  LEU B CA  1 
ATOM   9558  C  C   . LEU B  1  595 ? 17.337  30.545  -35.626 1.00 174.95 ? 621  LEU B C   1 
ATOM   9559  O  O   . LEU B  1  595 ? 17.876  30.599  -36.733 1.00 174.99 ? 621  LEU B O   1 
ATOM   9560  C  CB  . LEU B  1  595 ? 18.626  28.450  -35.123 1.00 173.87 ? 621  LEU B CB  1 
ATOM   9561  C  CG  . LEU B  1  595 ? 19.324  27.478  -34.165 1.00 173.59 ? 621  LEU B CG  1 
ATOM   9562  C  CD1 . LEU B  1  595 ? 20.008  26.380  -34.971 1.00 173.52 ? 621  LEU B CD1 1 
ATOM   9563  C  CD2 . LEU B  1  595 ? 20.342  28.219  -33.313 1.00 173.20 ? 621  LEU B CD2 1 
ATOM   9564  N  N   . SER B  1  596 ? 16.237  31.231  -35.313 1.00 175.75 ? 622  SER B N   1 
ATOM   9565  C  CA  . SER B  1  596 ? 15.543  32.109  -36.262 1.00 176.03 ? 622  SER B CA  1 
ATOM   9566  C  C   . SER B  1  596 ? 14.635  33.121  -35.546 1.00 176.43 ? 622  SER B C   1 
ATOM   9567  O  O   . SER B  1  596 ? 13.405  33.023  -35.629 1.00 176.18 ? 622  SER B O   1 
ATOM   9568  C  CB  . SER B  1  596 ? 14.686  31.273  -37.220 1.00 175.90 ? 622  SER B CB  1 
ATOM   9569  O  OG  . SER B  1  596 ? 15.452  30.279  -37.877 1.00 175.61 ? 622  SER B OG  1 
ATOM   9570  N  N   . LEU B  1  597 ? 15.233  34.093  -34.857 1.00 177.00 ? 623  LEU B N   1 
ATOM   9571  C  CA  . LEU B  1  597 ? 14.455  35.101  -34.133 1.00 177.56 ? 623  LEU B CA  1 
ATOM   9572  C  C   . LEU B  1  597 ? 14.887  36.554  -34.347 1.00 177.84 ? 623  LEU B C   1 
ATOM   9573  O  O   . LEU B  1  597 ? 16.080  36.857  -34.438 1.00 177.75 ? 623  LEU B O   1 
ATOM   9574  C  CB  . LEU B  1  597 ? 14.477  34.815  -32.625 1.00 177.38 ? 623  LEU B CB  1 
ATOM   9575  C  CG  . LEU B  1  597 ? 13.388  33.934  -32.007 1.00 177.27 ? 623  LEU B CG  1 
ATOM   9576  C  CD1 . LEU B  1  597 ? 12.016  34.482  -32.386 1.00 177.14 ? 623  LEU B CD1 1 
ATOM   9577  C  CD2 . LEU B  1  597 ? 13.540  32.505  -32.485 1.00 177.63 ? 623  LEU B CD2 1 
ATOM   9578  N  N   . ASN B  1  598 ? 13.896  37.444  -34.416 1.00 177.99 ? 624  ASN B N   1 
ATOM   9579  C  CA  . ASN B  1  598 ? 14.136  38.876  -34.577 1.00 178.09 ? 624  ASN B CA  1 
ATOM   9580  C  C   . ASN B  1  598 ? 14.648  39.388  -33.233 1.00 178.01 ? 624  ASN B C   1 
ATOM   9581  O  O   . ASN B  1  598 ? 13.856  39.717  -32.347 1.00 178.04 ? 624  ASN B O   1 
ATOM   9582  C  CB  . ASN B  1  598 ? 12.839  39.610  -34.935 1.00 178.15 ? 624  ASN B CB  1 
ATOM   9583  C  CG  . ASN B  1  598 ? 12.341  39.283  -36.333 1.00 178.09 ? 624  ASN B CG  1 
ATOM   9584  O  OD1 . ASN B  1  598 ? 13.000  39.590  -37.327 1.00 177.97 ? 624  ASN B OD1 1 
ATOM   9585  N  ND2 . ASN B  1  598 ? 11.171  38.664  -36.413 1.00 177.94 ? 624  ASN B ND2 1 
ATOM   9586  N  N   . ILE B  1  599 ? 15.969  39.448  -33.088 1.00 177.84 ? 625  ILE B N   1 
ATOM   9587  C  CA  . ILE B  1  599 ? 16.597  39.900  -31.849 1.00 177.48 ? 625  ILE B CA  1 
ATOM   9588  C  C   . ILE B  1  599 ? 16.446  41.417  -31.666 1.00 177.23 ? 625  ILE B C   1 
ATOM   9589  O  O   . ILE B  1  599 ? 17.435  42.133  -31.471 1.00 177.27 ? 625  ILE B O   1 
ATOM   9590  C  CB  . ILE B  1  599 ? 18.102  39.528  -31.833 1.00 177.15 ? 625  ILE B CB  1 
ATOM   9591  C  CG1 . ILE B  1  599 ? 18.302  38.113  -32.394 1.00 176.66 ? 625  ILE B CG1 1 
ATOM   9592  C  CG2 . ILE B  1  599 ? 18.637  39.595  -30.414 1.00 177.03 ? 625  ILE B CG2 1 
ATOM   9593  C  CD1 . ILE B  1  599 ? 17.604  37.018  -31.609 1.00 176.24 ? 625  ILE B CD1 1 
ATOM   9594  N  N   . THR B  1  600 ? 15.201  41.892  -31.723 1.00 176.73 ? 626  THR B N   1 
ATOM   9595  C  CA  . THR B  1  600 ? 14.893  43.313  -31.577 1.00 175.72 ? 626  THR B CA  1 
ATOM   9596  C  C   . THR B  1  600 ? 14.628  43.717  -30.123 1.00 175.49 ? 626  THR B C   1 
ATOM   9597  O  O   . THR B  1  600 ? 13.624  43.316  -29.534 1.00 175.19 ? 626  THR B O   1 
ATOM   9598  C  CB  . THR B  1  600 ? 13.655  43.704  -32.424 1.00 175.27 ? 626  THR B CB  1 
ATOM   9599  O  OG1 . THR B  1  600 ? 12.505  42.986  -31.959 1.00 174.70 ? 626  THR B OG1 1 
ATOM   9600  C  CG2 . THR B  1  600 ? 13.886  43.375  -33.896 1.00 174.66 ? 626  THR B CG2 1 
ATOM   9601  N  N   . CYS B  1  601 ? 15.534  44.512  -29.554 1.00 175.14 ? 627  CYS B N   1 
ATOM   9602  C  CA  . CYS B  1  601 ? 15.409  44.984  -28.176 1.00 174.63 ? 627  CYS B CA  1 
ATOM   9603  C  C   . CYS B  1  601 ? 15.346  46.508  -28.133 1.00 174.67 ? 627  CYS B C   1 
ATOM   9604  O  O   . CYS B  1  601 ? 16.281  47.109  -27.564 1.00 174.57 ? 627  CYS B O   1 
ATOM   9605  C  CB  . CYS B  1  601 ? 16.602  44.537  -27.336 1.00 174.09 ? 627  CYS B CB  1 
ATOM   9606  S  SG  . CYS B  1  601 ? 16.970  42.754  -27.294 1.00 173.98 ? 627  CYS B SG  1 
ATOM   9607  N  N   . GLN C  2  1   ? 38.493  15.287  27.001  1.00 104.09 ? 19   GLN C N   1 
ATOM   9608  C  CA  . GLN C  2  1   ? 39.351  15.412  25.785  1.00 104.55 ? 19   GLN C CA  1 
ATOM   9609  C  C   . GLN C  2  1   ? 40.256  14.190  25.597  1.00 103.68 ? 19   GLN C C   1 
ATOM   9610  O  O   . GLN C  2  1   ? 40.708  13.895  24.484  1.00 103.59 ? 19   GLN C O   1 
ATOM   9611  C  CB  . GLN C  2  1   ? 40.210  16.681  25.881  1.00 106.28 ? 19   GLN C CB  1 
ATOM   9612  C  CG  . GLN C  2  1   ? 41.129  16.908  24.682  1.00 107.40 ? 19   GLN C CG  1 
ATOM   9613  C  CD  . GLN C  2  1   ? 40.444  16.580  23.365  1.00 107.87 ? 19   GLN C CD  1 
ATOM   9614  O  OE1 . GLN C  2  1   ? 39.348  17.064  23.084  1.00 107.57 ? 19   GLN C OE1 1 
ATOM   9615  N  NE2 . GLN C  2  1   ? 41.093  15.753  22.549  1.00 108.15 ? 19   GLN C NE2 1 
ATOM   9616  N  N   . LYS C  2  2   ? 40.511  13.481  26.692  1.00 102.04 ? 20   LYS C N   1 
ATOM   9617  C  CA  . LYS C  2  2   ? 41.361  12.303  26.660  1.00 100.41 ? 20   LYS C CA  1 
ATOM   9618  C  C   . LYS C  2  2   ? 40.854  11.249  25.679  1.00 99.46  ? 20   LYS C C   1 
ATOM   9619  O  O   . LYS C  2  2   ? 39.651  10.992  25.583  1.00 99.21  ? 20   LYS C O   1 
ATOM   9620  C  CB  . LYS C  2  2   ? 41.456  11.690  28.063  1.00 101.00 ? 20   LYS C CB  1 
ATOM   9621  C  CG  . LYS C  2  2   ? 42.353  10.457  28.148  1.00 102.62 ? 20   LYS C CG  1 
ATOM   9622  C  CD  . LYS C  2  2   ? 42.224  9.708   29.482  1.00 103.10 ? 20   LYS C CD  1 
ATOM   9623  C  CE  . LYS C  2  2   ? 43.051  8.417   29.463  1.00 102.97 ? 20   LYS C CE  1 
ATOM   9624  N  NZ  . LYS C  2  2   ? 42.882  7.576   30.675  1.00 102.63 ? 20   LYS C NZ  1 
ATOM   9625  N  N   . GLN C  2  3   ? 41.783  10.656  24.938  1.00 97.71  ? 21   GLN C N   1 
ATOM   9626  C  CA  . GLN C  2  3   ? 41.445  9.600   24.001  1.00 95.75  ? 21   GLN C CA  1 
ATOM   9627  C  C   . GLN C  2  3   ? 41.657  8.278   24.728  1.00 94.31  ? 21   GLN C C   1 
ATOM   9628  O  O   . GLN C  2  3   ? 42.704  8.070   25.342  1.00 94.36  ? 21   GLN C O   1 
ATOM   9629  C  CB  . GLN C  2  3   ? 42.349  9.643   22.775  1.00 96.50  ? 21   GLN C CB  1 
ATOM   9630  C  CG  . GLN C  2  3   ? 41.808  10.454  21.623  1.00 99.33  ? 21   GLN C CG  1 
ATOM   9631  C  CD  . GLN C  2  3   ? 42.260  9.893   20.278  1.00 101.87 ? 21   GLN C CD  1 
ATOM   9632  O  OE1 . GLN C  2  3   ? 43.462  9.760   20.020  1.00 101.59 ? 21   GLN C OE1 1 
ATOM   9633  N  NE2 . GLN C  2  3   ? 41.296  9.555   19.417  1.00 102.19 ? 21   GLN C NE2 1 
ATOM   9634  N  N   . TYR C  2  4   ? 40.664  7.393   24.673  1.00 92.02  ? 22   TYR C N   1 
ATOM   9635  C  CA  . TYR C  2  4   ? 40.773  6.094   25.324  1.00 88.97  ? 22   TYR C CA  1 
ATOM   9636  C  C   . TYR C  2  4   ? 41.087  5.018   24.292  1.00 87.07  ? 22   TYR C C   1 
ATOM   9637  O  O   . TYR C  2  4   ? 40.502  4.991   23.209  1.00 86.45  ? 22   TYR C O   1 
ATOM   9638  C  CB  . TYR C  2  4   ? 39.477  5.769   26.061  1.00 89.00  ? 22   TYR C CB  1 
ATOM   9639  C  CG  . TYR C  2  4   ? 39.061  6.837   27.056  1.00 89.23  ? 22   TYR C CG  1 
ATOM   9640  C  CD1 . TYR C  2  4   ? 38.440  8.020   26.627  1.00 88.44  ? 22   TYR C CD1 1 
ATOM   9641  C  CD2 . TYR C  2  4   ? 39.303  6.676   28.425  1.00 88.58  ? 22   TYR C CD2 1 
ATOM   9642  C  CE1 . TYR C  2  4   ? 38.071  9.013   27.538  1.00 88.13  ? 22   TYR C CE1 1 
ATOM   9643  C  CE2 . TYR C  2  4   ? 38.940  7.663   29.340  1.00 88.06  ? 22   TYR C CE2 1 
ATOM   9644  C  CZ  . TYR C  2  4   ? 38.327  8.825   28.893  1.00 87.89  ? 22   TYR C CZ  1 
ATOM   9645  O  OH  . TYR C  2  4   ? 37.974  9.803   29.799  1.00 87.22  ? 22   TYR C OH  1 
ATOM   9646  N  N   . TRP C  2  5   ? 42.016  4.133   24.634  1.00 85.53  ? 23   TRP C N   1 
ATOM   9647  C  CA  . TRP C  2  5   ? 42.441  3.072   23.725  1.00 84.54  ? 23   TRP C CA  1 
ATOM   9648  C  C   . TRP C  2  5   ? 41.772  1.727   23.997  1.00 83.95  ? 23   TRP C C   1 
ATOM   9649  O  O   . TRP C  2  5   ? 42.003  1.093   25.030  1.00 83.84  ? 23   TRP C O   1 
ATOM   9650  C  CB  . TRP C  2  5   ? 43.959  2.909   23.812  1.00 83.80  ? 23   TRP C CB  1 
ATOM   9651  C  CG  . TRP C  2  5   ? 44.560  1.935   22.840  1.00 82.86  ? 23   TRP C CG  1 
ATOM   9652  C  CD1 . TRP C  2  5   ? 44.590  2.043   21.477  1.00 82.71  ? 23   TRP C CD1 1 
ATOM   9653  C  CD2 . TRP C  2  5   ? 45.267  0.729   23.163  1.00 82.53  ? 23   TRP C CD2 1 
ATOM   9654  N  NE1 . TRP C  2  5   ? 45.278  0.979   20.936  1.00 82.32  ? 23   TRP C NE1 1 
ATOM   9655  C  CE2 . TRP C  2  5   ? 45.703  0.162   21.952  1.00 82.49  ? 23   TRP C CE2 1 
ATOM   9656  C  CE3 . TRP C  2  5   ? 45.572  0.075   24.362  1.00 82.37  ? 23   TRP C CE3 1 
ATOM   9657  C  CZ2 . TRP C  2  5   ? 46.432  -1.033  21.908  1.00 82.24  ? 23   TRP C CZ2 1 
ATOM   9658  C  CZ3 . TRP C  2  5   ? 46.298  -1.117  24.311  1.00 81.55  ? 23   TRP C CZ3 1 
ATOM   9659  C  CH2 . TRP C  2  5   ? 46.716  -1.652  23.097  1.00 81.36  ? 23   TRP C CH2 1 
ATOM   9660  N  N   . VAL C  2  6   ? 40.943  1.287   23.063  1.00 82.40  ? 24   VAL C N   1 
ATOM   9661  C  CA  . VAL C  2  6   ? 40.286  0.016   23.234  1.00 81.28  ? 24   VAL C CA  1 
ATOM   9662  C  C   . VAL C  2  6   ? 41.299  -1.081  22.915  1.00 80.43  ? 24   VAL C C   1 
ATOM   9663  O  O   . VAL C  2  6   ? 41.762  -1.764  23.826  1.00 80.91  ? 24   VAL C O   1 
ATOM   9664  C  CB  . VAL C  2  6   ? 39.051  -0.098  22.324  1.00 82.09  ? 24   VAL C CB  1 
ATOM   9665  C  CG1 . VAL C  2  6   ? 38.267  -1.370  22.669  1.00 82.44  ? 24   VAL C CG1 1 
ATOM   9666  C  CG2 . VAL C  2  6   ? 38.166  1.139   22.500  1.00 81.11  ? 24   VAL C CG2 1 
ATOM   9667  N  N   . CYS C  2  7   ? 41.661  -1.244  21.640  1.00 79.19  ? 25   CYS C N   1 
ATOM   9668  C  CA  . CYS C  2  7   ? 42.640  -2.270  21.263  1.00 78.33  ? 25   CYS C CA  1 
ATOM   9669  C  C   . CYS C  2  7   ? 43.161  -2.179  19.836  1.00 77.82  ? 25   CYS C C   1 
ATOM   9670  O  O   . CYS C  2  7   ? 42.718  -1.352  19.045  1.00 76.79  ? 25   CYS C O   1 
ATOM   9671  C  CB  . CYS C  2  7   ? 42.059  -3.675  21.462  1.00 78.54  ? 25   CYS C CB  1 
ATOM   9672  S  SG  . CYS C  2  7   ? 40.586  -4.084  20.451  1.00 81.60  ? 25   CYS C SG  1 
ATOM   9673  N  N   . ASN C  2  8   ? 44.116  -3.060  19.536  1.00 78.80  ? 26   ASN C N   1 
ATOM   9674  C  CA  . ASN C  2  8   ? 44.736  -3.182  18.215  1.00 79.53  ? 26   ASN C CA  1 
ATOM   9675  C  C   . ASN C  2  8   ? 44.756  -4.663  17.799  1.00 79.40  ? 26   ASN C C   1 
ATOM   9676  O  O   . ASN C  2  8   ? 44.995  -5.555  18.624  1.00 78.81  ? 26   ASN C O   1 
ATOM   9677  C  CB  . ASN C  2  8   ? 46.182  -2.672  18.236  1.00 80.20  ? 26   ASN C CB  1 
ATOM   9678  C  CG  . ASN C  2  8   ? 46.277  -1.167  18.336  1.00 80.87  ? 26   ASN C CG  1 
ATOM   9679  O  OD1 . ASN C  2  8   ? 47.376  -0.607  18.390  1.00 81.14  ? 26   ASN C OD1 1 
ATOM   9680  N  ND2 . ASN C  2  8   ? 45.129  -0.498  18.357  1.00 81.81  ? 26   ASN C ND2 1 
ATOM   9681  N  N   . SER C  2  9   ? 44.499  -4.917  16.520  1.00 78.99  ? 27   SER C N   1 
ATOM   9682  C  CA  . SER C  2  9   ? 44.511  -6.276  15.988  1.00 78.69  ? 27   SER C CA  1 
ATOM   9683  C  C   . SER C  2  9   ? 45.627  -6.331  14.959  1.00 78.00  ? 27   SER C C   1 
ATOM   9684  O  O   . SER C  2  9   ? 46.758  -5.948  15.244  1.00 79.15  ? 27   SER C O   1 
ATOM   9685  C  CB  . SER C  2  9   ? 43.172  -6.601  15.325  1.00 78.36  ? 27   SER C CB  1 
ATOM   9686  O  OG  . SER C  2  9   ? 42.847  -5.624  14.353  1.00 77.70  ? 27   SER C OG  1 
ATOM   9687  N  N   . SER C  2  10  ? 45.313  -6.811  13.768  1.00 76.73  ? 28   SER C N   1 
ATOM   9688  C  CA  . SER C  2  10  ? 46.294  -6.871  12.702  1.00 76.10  ? 28   SER C CA  1 
ATOM   9689  C  C   . SER C  2  10  ? 45.678  -6.125  11.531  1.00 75.87  ? 28   SER C C   1 
ATOM   9690  O  O   . SER C  2  10  ? 46.324  -5.850  10.528  1.00 75.00  ? 28   SER C O   1 
ATOM   9691  C  CB  . SER C  2  10  ? 46.580  -8.320  12.339  1.00 75.31  ? 28   SER C CB  1 
ATOM   9692  O  OG  . SER C  2  10  ? 45.377  -9.053  12.257  1.00 77.07  ? 28   SER C OG  1 
ATOM   9693  N  N   . ASP C  2  11  ? 44.408  -5.784  11.705  1.00 76.36  ? 29   ASP C N   1 
ATOM   9694  C  CA  . ASP C  2  11  ? 43.621  -5.071  10.716  1.00 76.23  ? 29   ASP C CA  1 
ATOM   9695  C  C   . ASP C  2  11  ? 43.395  -3.658  11.175  1.00 74.76  ? 29   ASP C C   1 
ATOM   9696  O  O   . ASP C  2  11  ? 43.431  -2.723  10.379  1.00 72.64  ? 29   ASP C O   1 
ATOM   9697  C  CB  . ASP C  2  11  ? 42.250  -5.727  10.571  1.00 79.93  ? 29   ASP C CB  1 
ATOM   9698  C  CG  . ASP C  2  11  ? 42.191  -6.724  9.444   1.00 84.26  ? 29   ASP C CG  1 
ATOM   9699  O  OD1 . ASP C  2  11  ? 43.063  -7.623  9.380   1.00 86.53  ? 29   ASP C OD1 1 
ATOM   9700  O  OD2 . ASP C  2  11  ? 41.252  -6.606  8.625   1.00 86.33  ? 29   ASP C OD2 1 
ATOM   9701  N  N   . ALA C  2  12  ? 43.159  -3.510  12.474  1.00 74.45  ? 30   ALA C N   1 
ATOM   9702  C  CA  . ALA C  2  12  ? 42.847  -2.194  13.006  1.00 74.17  ? 30   ALA C CA  1 
ATOM   9703  C  C   . ALA C  2  12  ? 43.327  -1.786  14.388  1.00 73.29  ? 30   ALA C C   1 
ATOM   9704  O  O   . ALA C  2  12  ? 43.878  -2.577  15.161  1.00 72.58  ? 30   ALA C O   1 
ATOM   9705  C  CB  . ALA C  2  12  ? 41.350  -1.982  12.940  1.00 74.58  ? 30   ALA C CB  1 
ATOM   9706  N  N   . SER C  2  13  ? 43.068  -0.508  14.662  1.00 72.35  ? 31   SER C N   1 
ATOM   9707  C  CA  . SER C  2  13  ? 43.393  0.170   15.904  1.00 72.08  ? 31   SER C CA  1 
ATOM   9708  C  C   . SER C  2  13  ? 42.117  0.938   16.266  1.00 72.44  ? 31   SER C C   1 
ATOM   9709  O  O   . SER C  2  13  ? 41.669  1.807   15.510  1.00 72.76  ? 31   SER C O   1 
ATOM   9710  C  CB  . SER C  2  13  ? 44.558  1.137   15.674  1.00 71.89  ? 31   SER C CB  1 
ATOM   9711  O  OG  . SER C  2  13  ? 44.934  1.811   16.865  1.00 71.47  ? 31   SER C OG  1 
ATOM   9712  N  N   . ILE C  2  14  ? 41.535  0.617   17.419  1.00 71.98  ? 32   ILE C N   1 
ATOM   9713  C  CA  . ILE C  2  14  ? 40.288  1.241   17.856  1.00 71.23  ? 32   ILE C CA  1 
ATOM   9714  C  C   . ILE C  2  14  ? 40.413  2.097   19.121  1.00 71.11  ? 32   ILE C C   1 
ATOM   9715  O  O   . ILE C  2  14  ? 40.957  1.661   20.139  1.00 71.50  ? 32   ILE C O   1 
ATOM   9716  C  CB  . ILE C  2  14  ? 39.222  0.142   18.087  1.00 71.69  ? 32   ILE C CB  1 
ATOM   9717  C  CG1 . ILE C  2  14  ? 39.036  -0.660  16.806  1.00 71.16  ? 32   ILE C CG1 1 
ATOM   9718  C  CG2 . ILE C  2  14  ? 37.891  0.740   18.463  1.00 70.65  ? 32   ILE C CG2 1 
ATOM   9719  C  CD1 . ILE C  2  14  ? 38.277  -1.924  17.005  1.00 71.52  ? 32   ILE C CD1 1 
ATOM   9720  N  N   . SER C  2  15  ? 39.897  3.320   19.047  1.00 71.11  ? 33   SER C N   1 
ATOM   9721  C  CA  . SER C  2  15  ? 39.925  4.259   20.170  1.00 70.23  ? 33   SER C CA  1 
ATOM   9722  C  C   . SER C  2  15  ? 38.656  5.118   20.142  1.00 69.28  ? 33   SER C C   1 
ATOM   9723  O  O   . SER C  2  15  ? 37.954  5.170   19.128  1.00 68.86  ? 33   SER C O   1 
ATOM   9724  C  CB  . SER C  2  15  ? 41.153  5.170   20.073  1.00 71.02  ? 33   SER C CB  1 
ATOM   9725  O  OG  . SER C  2  15  ? 41.081  5.998   18.916  1.00 70.40  ? 33   SER C OG  1 
ATOM   9726  N  N   . TYR C  2  16  ? 38.363  5.788   21.254  1.00 67.98  ? 34   TYR C N   1 
ATOM   9727  C  CA  . TYR C  2  16  ? 37.177  6.645   21.333  1.00 67.41  ? 34   TYR C CA  1 
ATOM   9728  C  C   . TYR C  2  16  ? 37.339  7.855   22.256  1.00 67.80  ? 34   TYR C C   1 
ATOM   9729  O  O   . TYR C  2  16  ? 38.194  7.880   23.147  1.00 67.49  ? 34   TYR C O   1 
ATOM   9730  C  CB  . TYR C  2  16  ? 35.946  5.827   21.783  1.00 64.87  ? 34   TYR C CB  1 
ATOM   9731  C  CG  . TYR C  2  16  ? 35.947  5.358   23.240  1.00 61.77  ? 34   TYR C CG  1 
ATOM   9732  C  CD1 . TYR C  2  16  ? 35.370  6.129   24.251  1.00 59.56  ? 34   TYR C CD1 1 
ATOM   9733  C  CD2 . TYR C  2  16  ? 36.542  4.145   23.603  1.00 60.81  ? 34   TYR C CD2 1 
ATOM   9734  C  CE1 . TYR C  2  16  ? 35.384  5.708   25.582  1.00 58.66  ? 34   TYR C CE1 1 
ATOM   9735  C  CE2 . TYR C  2  16  ? 36.564  3.715   24.929  1.00 59.44  ? 34   TYR C CE2 1 
ATOM   9736  C  CZ  . TYR C  2  16  ? 35.983  4.497   25.917  1.00 59.41  ? 34   TYR C CZ  1 
ATOM   9737  O  OH  . TYR C  2  16  ? 36.000  4.041   27.229  1.00 57.15  ? 34   TYR C OH  1 
ATOM   9738  N  N   . THR C  2  17  ? 36.503  8.861   22.014  1.00 68.21  ? 35   THR C N   1 
ATOM   9739  C  CA  . THR C  2  17  ? 36.476  10.078  22.813  1.00 68.72  ? 35   THR C CA  1 
ATOM   9740  C  C   . THR C  2  17  ? 34.990  10.283  23.107  1.00 70.22  ? 35   THR C C   1 
ATOM   9741  O  O   . THR C  2  17  ? 34.175  9.412   22.799  1.00 71.12  ? 35   THR C O   1 
ATOM   9742  C  CB  . THR C  2  17  ? 37.023  11.282  22.023  1.00 67.62  ? 35   THR C CB  1 
ATOM   9743  O  OG1 . THR C  2  17  ? 36.066  11.692  21.042  1.00 66.81  ? 35   THR C OG1 1 
ATOM   9744  C  CG2 . THR C  2  17  ? 38.315  10.903  21.316  1.00 67.27  ? 35   THR C CG2 1 
ATOM   9745  N  N   . TYR C  2  18  ? 34.622  11.406  23.707  1.00 70.51  ? 36   TYR C N   1 
ATOM   9746  C  CA  . TYR C  2  18  ? 33.214  11.652  23.981  1.00 69.81  ? 36   TYR C CA  1 
ATOM   9747  C  C   . TYR C  2  18  ? 32.761  12.757  23.052  1.00 71.16  ? 36   TYR C C   1 
ATOM   9748  O  O   . TYR C  2  18  ? 33.579  13.530  22.576  1.00 71.54  ? 36   TYR C O   1 
ATOM   9749  C  CB  . TYR C  2  18  ? 33.004  12.074  25.441  1.00 68.03  ? 36   TYR C CB  1 
ATOM   9750  C  CG  . TYR C  2  18  ? 33.186  10.961  26.467  1.00 67.02  ? 36   TYR C CG  1 
ATOM   9751  C  CD1 . TYR C  2  18  ? 34.456  10.470  26.797  1.00 65.80  ? 36   TYR C CD1 1 
ATOM   9752  C  CD2 . TYR C  2  18  ? 32.080  10.395  27.109  1.00 66.10  ? 36   TYR C CD2 1 
ATOM   9753  C  CE1 . TYR C  2  18  ? 34.615  9.448   27.741  1.00 64.51  ? 36   TYR C CE1 1 
ATOM   9754  C  CE2 . TYR C  2  18  ? 32.231  9.367   28.052  1.00 64.76  ? 36   TYR C CE2 1 
ATOM   9755  C  CZ  . TYR C  2  18  ? 33.498  8.901   28.358  1.00 65.17  ? 36   TYR C CZ  1 
ATOM   9756  O  OH  . TYR C  2  18  ? 33.645  7.871   29.258  1.00 65.34  ? 36   TYR C OH  1 
ATOM   9757  N  N   . CYS C  2  19  ? 31.468  12.803  22.757  1.00 73.83  ? 37   CYS C N   1 
ATOM   9758  C  CA  . CYS C  2  19  ? 30.907  13.851  21.906  1.00 77.14  ? 37   CYS C CA  1 
ATOM   9759  C  C   . CYS C  2  19  ? 29.699  14.452  22.594  1.00 78.23  ? 37   CYS C C   1 
ATOM   9760  O  O   . CYS C  2  19  ? 28.851  15.060  21.949  1.00 78.88  ? 37   CYS C O   1 
ATOM   9761  C  CB  . CYS C  2  19  ? 30.497  13.347  20.502  1.00 78.31  ? 37   CYS C CB  1 
ATOM   9762  S  SG  . CYS C  2  19  ? 29.841  11.646  20.326  1.00 85.93  ? 37   CYS C SG  1 
ATOM   9763  N  N   . ASP C  2  20  ? 29.619  14.275  23.907  1.00 80.05  ? 38   ASP C N   1 
ATOM   9764  C  CA  . ASP C  2  20  ? 28.510  14.833  24.671  1.00 82.90  ? 38   ASP C CA  1 
ATOM   9765  C  C   . ASP C  2  20  ? 29.042  15.674  25.828  1.00 84.31  ? 38   ASP C C   1 
ATOM   9766  O  O   . ASP C  2  20  ? 30.207  15.544  26.217  1.00 84.45  ? 38   ASP C O   1 
ATOM   9767  C  CB  . ASP C  2  20  ? 27.586  13.719  25.195  1.00 82.86  ? 38   ASP C CB  1 
ATOM   9768  C  CG  . ASP C  2  20  ? 28.273  12.793  26.192  1.00 83.91  ? 38   ASP C CG  1 
ATOM   9769  O  OD1 . ASP C  2  20  ? 29.523  12.762  26.222  1.00 84.39  ? 38   ASP C OD1 1 
ATOM   9770  O  OD2 . ASP C  2  20  ? 27.558  12.079  26.937  1.00 82.64  ? 38   ASP C OD2 1 
ATOM   9771  N  N   . LYS C  2  21  ? 28.187  16.545  26.358  1.00 85.68  ? 39   LYS C N   1 
ATOM   9772  C  CA  . LYS C  2  21  ? 28.555  17.420  27.466  1.00 86.77  ? 39   LYS C CA  1 
ATOM   9773  C  C   . LYS C  2  21  ? 29.015  16.616  28.696  1.00 87.19  ? 39   LYS C C   1 
ATOM   9774  O  O   . LYS C  2  21  ? 30.199  16.642  29.045  1.00 86.44  ? 39   LYS C O   1 
ATOM   9775  C  CB  . LYS C  2  21  ? 27.368  18.325  27.822  1.00 87.99  ? 39   LYS C CB  1 
ATOM   9776  C  CG  . LYS C  2  21  ? 26.878  19.256  26.685  1.00 88.51  ? 39   LYS C CG  1 
ATOM   9777  C  CD  . LYS C  2  21  ? 25.730  18.656  25.843  1.00 89.18  ? 39   LYS C CD  1 
ATOM   9778  C  CE  . LYS C  2  21  ? 26.221  18.022  24.532  1.00 89.37  ? 39   LYS C CE  1 
ATOM   9779  N  NZ  . LYS C  2  21  ? 25.105  17.579  23.636  1.00 87.09  ? 39   LYS C NZ  1 
ATOM   9780  N  N   . MET C  2  22  ? 28.083  15.912  29.346  1.00 87.28  ? 40   MET C N   1 
ATOM   9781  C  CA  . MET C  2  22  ? 28.399  15.079  30.518  1.00 87.51  ? 40   MET C CA  1 
ATOM   9782  C  C   . MET C  2  22  ? 29.238  13.904  30.032  1.00 85.80  ? 40   MET C C   1 
ATOM   9783  O  O   . MET C  2  22  ? 28.863  13.238  29.075  1.00 87.14  ? 40   MET C O   1 
ATOM   9784  C  CB  . MET C  2  22  ? 27.116  14.542  31.155  1.00 90.06  ? 40   MET C CB  1 
ATOM   9785  C  CG  . MET C  2  22  ? 26.363  15.525  32.048  1.00 94.90  ? 40   MET C CG  1 
ATOM   9786  S  SD  . MET C  2  22  ? 25.851  17.079  31.258  1.00 100.35 ? 40   MET C SD  1 
ATOM   9787  C  CE  . MET C  2  22  ? 26.916  18.322  32.192  1.00 99.21  ? 40   MET C CE  1 
ATOM   9788  N  N   . GLN C  2  23  ? 30.359  13.621  30.679  1.00 83.00  ? 41   GLN C N   1 
ATOM   9789  C  CA  . GLN C  2  23  ? 31.187  12.527  30.197  1.00 81.00  ? 41   GLN C CA  1 
ATOM   9790  C  C   . GLN C  2  23  ? 31.263  11.319  31.108  1.00 79.76  ? 41   GLN C C   1 
ATOM   9791  O  O   . GLN C  2  23  ? 32.347  10.884  31.497  1.00 79.77  ? 41   GLN C O   1 
ATOM   9792  C  CB  . GLN C  2  23  ? 32.589  13.046  29.896  1.00 82.00  ? 41   GLN C CB  1 
ATOM   9793  C  CG  . GLN C  2  23  ? 32.625  14.094  28.793  1.00 82.90  ? 41   GLN C CG  1 
ATOM   9794  C  CD  . GLN C  2  23  ? 33.981  14.755  28.663  1.00 83.27  ? 41   GLN C CD  1 
ATOM   9795  O  OE1 . GLN C  2  23  ? 34.978  14.111  28.324  1.00 82.43  ? 41   GLN C OE1 1 
ATOM   9796  N  NE2 . GLN C  2  23  ? 34.027  16.051  28.943  1.00 84.04  ? 41   GLN C NE2 1 
ATOM   9797  N  N   . TYR C  2  24  ? 30.098  10.772  31.429  1.00 78.27  ? 42   TYR C N   1 
ATOM   9798  C  CA  . TYR C  2  24  ? 29.997  9.596   32.287  1.00 75.98  ? 42   TYR C CA  1 
ATOM   9799  C  C   . TYR C  2  24  ? 30.924  8.483   31.779  1.00 73.88  ? 42   TYR C C   1 
ATOM   9800  O  O   . TYR C  2  24  ? 30.870  8.095   30.605  1.00 73.60  ? 42   TYR C O   1 
ATOM   9801  C  CB  . TYR C  2  24  ? 28.547  9.106   32.310  1.00 76.07  ? 42   TYR C CB  1 
ATOM   9802  C  CG  . TYR C  2  24  ? 27.510  10.187  32.565  1.00 75.45  ? 42   TYR C CG  1 
ATOM   9803  C  CD1 . TYR C  2  24  ? 26.594  10.549  31.576  1.00 75.65  ? 42   TYR C CD1 1 
ATOM   9804  C  CD2 . TYR C  2  24  ? 27.401  10.797  33.811  1.00 75.33  ? 42   TYR C CD2 1 
ATOM   9805  C  CE1 . TYR C  2  24  ? 25.590  11.480  31.825  1.00 75.95  ? 42   TYR C CE1 1 
ATOM   9806  C  CE2 . TYR C  2  24  ? 26.402  11.730  34.071  1.00 76.02  ? 42   TYR C CE2 1 
ATOM   9807  C  CZ  . TYR C  2  24  ? 25.494  12.065  33.074  1.00 76.42  ? 42   TYR C CZ  1 
ATOM   9808  O  OH  . TYR C  2  24  ? 24.463  12.949  33.337  1.00 77.32  ? 42   TYR C OH  1 
ATOM   9809  N  N   . PRO C  2  25  ? 31.778  7.949   32.663  1.00 72.21  ? 43   PRO C N   1 
ATOM   9810  C  CA  . PRO C  2  25  ? 32.736  6.879   32.334  1.00 71.92  ? 43   PRO C CA  1 
ATOM   9811  C  C   . PRO C  2  25  ? 32.165  5.508   31.930  1.00 71.02  ? 43   PRO C C   1 
ATOM   9812  O  O   . PRO C  2  25  ? 31.137  5.077   32.453  1.00 70.73  ? 43   PRO C O   1 
ATOM   9813  C  CB  . PRO C  2  25  ? 33.591  6.793   33.597  1.00 71.30  ? 43   PRO C CB  1 
ATOM   9814  C  CG  . PRO C  2  25  ? 32.622  7.157   34.678  1.00 71.40  ? 43   PRO C CG  1 
ATOM   9815  C  CD  . PRO C  2  25  ? 31.885  8.336   34.082  1.00 70.83  ? 43   PRO C CD  1 
ATOM   9816  N  N   . ILE C  2  26  ? 32.839  4.833   30.994  1.00 69.86  ? 44   ILE C N   1 
ATOM   9817  C  CA  . ILE C  2  26  ? 32.424  3.504   30.535  1.00 68.65  ? 44   ILE C CA  1 
ATOM   9818  C  C   . ILE C  2  26  ? 33.626  2.604   30.425  1.00 68.09  ? 44   ILE C C   1 
ATOM   9819  O  O   . ILE C  2  26  ? 34.718  3.067   30.111  1.00 70.37  ? 44   ILE C O   1 
ATOM   9820  C  CB  . ILE C  2  26  ? 31.837  3.473   29.121  1.00 68.41  ? 44   ILE C CB  1 
ATOM   9821  C  CG1 . ILE C  2  26  ? 31.293  4.826   28.725  1.00 71.59  ? 44   ILE C CG1 1 
ATOM   9822  C  CG2 . ILE C  2  26  ? 30.726  2.445   29.057  1.00 67.44  ? 44   ILE C CG2 1 
ATOM   9823  C  CD1 . ILE C  2  26  ? 30.761  4.822   27.315  1.00 74.08  ? 44   ILE C CD1 1 
ATOM   9824  N  N   . SER C  2  27  ? 33.411  1.314   30.656  1.00 66.36  ? 45   SER C N   1 
ATOM   9825  C  CA  . SER C  2  27  ? 34.463  0.316   30.538  1.00 64.44  ? 45   SER C CA  1 
ATOM   9826  C  C   . SER C  2  27  ? 34.153  -0.500  29.279  1.00 63.38  ? 45   SER C C   1 
ATOM   9827  O  O   . SER C  2  27  ? 33.081  -1.069  29.159  1.00 64.62  ? 45   SER C O   1 
ATOM   9828  C  CB  . SER C  2  27  ? 34.472  -0.570  31.771  1.00 63.59  ? 45   SER C CB  1 
ATOM   9829  O  OG  . SER C  2  27  ? 35.406  -1.615  31.612  1.00 65.20  ? 45   SER C OG  1 
ATOM   9830  N  N   . ILE C  2  28  ? 35.082  -0.550  28.334  1.00 62.81  ? 46   ILE C N   1 
ATOM   9831  C  CA  . ILE C  2  28  ? 34.852  -1.263  27.084  1.00 62.64  ? 46   ILE C CA  1 
ATOM   9832  C  C   . ILE C  2  28  ? 35.988  -2.186  26.681  1.00 63.73  ? 46   ILE C C   1 
ATOM   9833  O  O   . ILE C  2  28  ? 37.060  -1.726  26.315  1.00 63.46  ? 46   ILE C O   1 
ATOM   9834  C  CB  . ILE C  2  28  ? 34.641  -0.268  25.948  1.00 62.04  ? 46   ILE C CB  1 
ATOM   9835  C  CG1 . ILE C  2  28  ? 33.471  0.647   26.278  1.00 61.85  ? 46   ILE C CG1 1 
ATOM   9836  C  CG2 . ILE C  2  28  ? 34.390  -1.000  24.656  1.00 62.56  ? 46   ILE C CG2 1 
ATOM   9837  C  CD1 . ILE C  2  28  ? 33.308  1.780   25.306  1.00 62.03  ? 46   ILE C CD1 1 
ATOM   9838  N  N   . ASN C  2  29  ? 35.744  -3.491  26.724  1.00 66.07  ? 47   ASN C N   1 
ATOM   9839  C  CA  . ASN C  2  29  ? 36.756  -4.478  26.350  1.00 67.97  ? 47   ASN C CA  1 
ATOM   9840  C  C   . ASN C  2  29  ? 36.288  -5.351  25.200  1.00 68.42  ? 47   ASN C C   1 
ATOM   9841  O  O   . ASN C  2  29  ? 35.125  -5.748  25.133  1.00 69.85  ? 47   ASN C O   1 
ATOM   9842  C  CB  . ASN C  2  29  ? 37.104  -5.361  27.543  1.00 69.69  ? 47   ASN C CB  1 
ATOM   9843  C  CG  . ASN C  2  29  ? 37.589  -4.555  28.730  1.00 73.01  ? 47   ASN C CG  1 
ATOM   9844  O  OD1 . ASN C  2  29  ? 36.802  -3.873  29.402  1.00 73.92  ? 47   ASN C OD1 1 
ATOM   9845  N  ND2 . ASN C  2  29  ? 38.897  -4.618  28.990  1.00 72.81  ? 47   ASN C ND2 1 
ATOM   9846  N  N   . VAL C  2  30  ? 37.201  -5.648  24.290  1.00 67.83  ? 48   VAL C N   1 
ATOM   9847  C  CA  . VAL C  2  30  ? 36.874  -6.455  23.136  1.00 67.21  ? 48   VAL C CA  1 
ATOM   9848  C  C   . VAL C  2  30  ? 37.867  -7.611  23.065  1.00 67.71  ? 48   VAL C C   1 
ATOM   9849  O  O   . VAL C  2  30  ? 39.072  -7.385  22.903  1.00 67.87  ? 48   VAL C O   1 
ATOM   9850  C  CB  . VAL C  2  30  ? 36.948  -5.581  21.858  1.00 67.48  ? 48   VAL C CB  1 
ATOM   9851  C  CG1 . VAL C  2  30  ? 36.439  -6.343  20.655  1.00 67.84  ? 48   VAL C CG1 1 
ATOM   9852  C  CG2 . VAL C  2  30  ? 36.136  -4.312  22.054  1.00 66.28  ? 48   VAL C CG2 1 
ATOM   9853  N  N   . ASN C  2  31  ? 37.368  -8.845  23.193  1.00 67.66  ? 49   ASN C N   1 
ATOM   9854  C  CA  . ASN C  2  31  ? 38.239  -10.026 23.148  1.00 67.38  ? 49   ASN C CA  1 
ATOM   9855  C  C   . ASN C  2  31  ? 37.787  -11.165 22.263  1.00 66.15  ? 49   ASN C C   1 
ATOM   9856  O  O   . ASN C  2  31  ? 36.778  -11.802 22.541  1.00 66.13  ? 49   ASN C O   1 
ATOM   9857  C  CB  . ASN C  2  31  ? 38.456  -10.567 24.555  1.00 68.29  ? 49   ASN C CB  1 
ATOM   9858  C  CG  . ASN C  2  31  ? 39.212  -9.597  25.424  1.00 69.41  ? 49   ASN C CG  1 
ATOM   9859  O  OD1 . ASN C  2  31  ? 38.616  -8.774  26.120  1.00 70.18  ? 49   ASN C OD1 1 
ATOM   9860  N  ND2 . ASN C  2  31  ? 40.541  -9.665  25.366  1.00 69.07  ? 49   ASN C ND2 1 
ATOM   9861  N  N   . PRO C  2  32  ? 38.549  -11.461 21.196  1.00 65.83  ? 50   PRO C N   1 
ATOM   9862  C  CA  . PRO C  2  32  ? 39.792  -10.806 20.773  1.00 66.77  ? 50   PRO C CA  1 
ATOM   9863  C  C   . PRO C  2  32  ? 39.491  -9.486  20.078  1.00 67.57  ? 50   PRO C C   1 
ATOM   9864  O  O   . PRO C  2  32  ? 38.333  -9.166  19.837  1.00 67.73  ? 50   PRO C O   1 
ATOM   9865  C  CB  . PRO C  2  32  ? 40.404  -11.825 19.822  1.00 66.43  ? 50   PRO C CB  1 
ATOM   9866  C  CG  . PRO C  2  32  ? 39.198  -12.387 19.156  1.00 67.03  ? 50   PRO C CG  1 
ATOM   9867  C  CD  . PRO C  2  32  ? 38.242  -12.596 20.310  1.00 66.15  ? 50   PRO C CD  1 
ATOM   9868  N  N   . CYS C  2  33  ? 40.518  -8.723  19.735  1.00 68.99  ? 51   CYS C N   1 
ATOM   9869  C  CA  . CYS C  2  33  ? 40.270  -7.440  19.094  1.00 72.11  ? 51   CYS C CA  1 
ATOM   9870  C  C   . CYS C  2  33  ? 39.677  -7.582  17.699  1.00 72.40  ? 51   CYS C C   1 
ATOM   9871  O  O   . CYS C  2  33  ? 40.041  -8.482  16.943  1.00 73.00  ? 51   CYS C O   1 
ATOM   9872  C  CB  . CYS C  2  33  ? 41.553  -6.602  19.032  1.00 74.25  ? 51   CYS C CB  1 
ATOM   9873  S  SG  . CYS C  2  33  ? 41.282  -4.827  18.682  1.00 75.83  ? 51   CYS C SG  1 
ATOM   9874  N  N   . ILE C  2  34  ? 38.764  -6.674  17.374  1.00 72.01  ? 52   ILE C N   1 
ATOM   9875  C  CA  . ILE C  2  34  ? 38.095  -6.654  16.089  1.00 72.22  ? 52   ILE C CA  1 
ATOM   9876  C  C   . ILE C  2  34  ? 39.065  -6.707  14.922  1.00 74.26  ? 52   ILE C C   1 
ATOM   9877  O  O   . ILE C  2  34  ? 40.134  -6.110  14.957  1.00 74.50  ? 52   ILE C O   1 
ATOM   9878  C  CB  . ILE C  2  34  ? 37.285  -5.377  15.917  1.00 71.07  ? 52   ILE C CB  1 
ATOM   9879  C  CG1 . ILE C  2  34  ? 36.291  -5.228  17.063  1.00 70.75  ? 52   ILE C CG1 1 
ATOM   9880  C  CG2 . ILE C  2  34  ? 36.563  -5.396  14.587  1.00 71.40  ? 52   ILE C CG2 1 
ATOM   9881  C  CD1 . ILE C  2  34  ? 35.171  -6.201  17.030  1.00 70.67  ? 52   ILE C CD1 1 
ATOM   9882  N  N   . GLU C  2  35  ? 38.675  -7.437  13.886  1.00 76.69  ? 53   GLU C N   1 
ATOM   9883  C  CA  . GLU C  2  35  ? 39.449  -7.534  12.663  1.00 78.27  ? 53   GLU C CA  1 
ATOM   9884  C  C   . GLU C  2  35  ? 38.435  -7.277  11.567  1.00 77.31  ? 53   GLU C C   1 
ATOM   9885  O  O   . GLU C  2  35  ? 37.467  -8.025  11.417  1.00 77.83  ? 53   GLU C O   1 
ATOM   9886  C  CB  . GLU C  2  35  ? 40.079  -8.915  12.512  1.00 81.59  ? 53   GLU C CB  1 
ATOM   9887  C  CG  . GLU C  2  35  ? 41.515  -8.968  13.008  1.00 87.83  ? 53   GLU C CG  1 
ATOM   9888  C  CD  . GLU C  2  35  ? 42.150  -10.343 12.860  1.00 91.64  ? 53   GLU C CD  1 
ATOM   9889  O  OE1 . GLU C  2  35  ? 41.718  -11.277 13.575  1.00 94.00  ? 53   GLU C OE1 1 
ATOM   9890  O  OE2 . GLU C  2  35  ? 43.079  -10.487 12.028  1.00 93.73  ? 53   GLU C OE2 1 
ATOM   9891  N  N   . LEU C  2  36  ? 38.632  -6.199  10.821  1.00 75.64  ? 54   LEU C N   1 
ATOM   9892  C  CA  . LEU C  2  36  ? 37.691  -5.856  9.772   1.00 74.57  ? 54   LEU C CA  1 
ATOM   9893  C  C   . LEU C  2  36  ? 37.582  -6.879  8.655   1.00 74.26  ? 54   LEU C C   1 
ATOM   9894  O  O   . LEU C  2  36  ? 36.687  -6.790  7.831   1.00 74.11  ? 54   LEU C O   1 
ATOM   9895  C  CB  . LEU C  2  36  ? 38.023  -4.475  9.212   1.00 73.34  ? 54   LEU C CB  1 
ATOM   9896  C  CG  . LEU C  2  36  ? 37.330  -3.348  9.980   1.00 71.05  ? 54   LEU C CG  1 
ATOM   9897  C  CD1 . LEU C  2  36  ? 37.658  -3.455  11.449  1.00 69.45  ? 54   LEU C CD1 1 
ATOM   9898  C  CD2 . LEU C  2  36  ? 37.743  -2.012  9.416   1.00 69.97  ? 54   LEU C CD2 1 
ATOM   9899  N  N   . LYS C  2  37  ? 38.496  -7.842  8.623   1.00 74.51  ? 55   LYS C N   1 
ATOM   9900  C  CA  . LYS C  2  37  ? 38.448  -8.888  7.609   1.00 74.76  ? 55   LYS C CA  1 
ATOM   9901  C  C   . LYS C  2  37  ? 37.433  -9.937  8.058   1.00 74.29  ? 55   LYS C C   1 
ATOM   9902  O  O   . LYS C  2  37  ? 37.144  -10.891 7.345   1.00 74.31  ? 55   LYS C O   1 
ATOM   9903  C  CB  . LYS C  2  37  ? 39.833  -9.527  7.423   1.00 76.55  ? 55   LYS C CB  1 
ATOM   9904  C  CG  . LYS C  2  37  ? 40.541  -9.956  8.710   1.00 79.44  ? 55   LYS C CG  1 
ATOM   9905  C  CD  . LYS C  2  37  ? 40.149  -11.353 9.193   1.00 81.63  ? 55   LYS C CD  1 
ATOM   9906  C  CE  . LYS C  2  37  ? 40.678  -12.424 8.253   1.00 83.78  ? 55   LYS C CE  1 
ATOM   9907  N  NZ  . LYS C  2  37  ? 42.160  -12.325 8.073   1.00 84.94  ? 55   LYS C NZ  1 
ATOM   9908  N  N   . GLY C  2  38  ? 36.885  -9.740  9.251   1.00 73.78  ? 56   GLY C N   1 
ATOM   9909  C  CA  . GLY C  2  38  ? 35.914  -10.670 9.793   1.00 71.68  ? 56   GLY C CA  1 
ATOM   9910  C  C   . GLY C  2  38  ? 36.430  -11.223 11.099  1.00 70.81  ? 56   GLY C C   1 
ATOM   9911  O  O   . GLY C  2  38  ? 37.550  -11.726 11.157  1.00 70.72  ? 56   GLY C O   1 
ATOM   9912  N  N   . SER C  2  39  ? 35.620  -11.121 12.150  1.00 70.55  ? 57   SER C N   1 
ATOM   9913  C  CA  . SER C  2  39  ? 35.990  -11.615 13.477  1.00 69.88  ? 57   SER C CA  1 
ATOM   9914  C  C   . SER C  2  39  ? 34.766  -11.927 14.334  1.00 68.55  ? 57   SER C C   1 
ATOM   9915  O  O   . SER C  2  39  ? 33.638  -11.601 13.978  1.00 67.27  ? 57   SER C O   1 
ATOM   9916  C  CB  . SER C  2  39  ? 36.870  -10.584 14.209  1.00 69.86  ? 57   SER C CB  1 
ATOM   9917  O  OG  . SER C  2  39  ? 36.174  -9.373  14.449  1.00 68.62  ? 57   SER C OG  1 
ATOM   9918  N  N   . LYS C  2  40  ? 35.000  -12.579 15.462  1.00 67.68  ? 58   LYS C N   1 
ATOM   9919  C  CA  . LYS C  2  40  ? 33.921  -12.898 16.373  1.00 67.54  ? 58   LYS C CA  1 
ATOM   9920  C  C   . LYS C  2  40  ? 34.503  -13.064 17.767  1.00 66.75  ? 58   LYS C C   1 
ATOM   9921  O  O   . LYS C  2  40  ? 35.396  -13.876 17.981  1.00 68.23  ? 58   LYS C O   1 
ATOM   9922  C  CB  . LYS C  2  40  ? 33.177  -14.157 15.914  1.00 69.14  ? 58   LYS C CB  1 
ATOM   9923  C  CG  . LYS C  2  40  ? 33.924  -15.477 16.035  1.00 71.82  ? 58   LYS C CG  1 
ATOM   9924  C  CD  . LYS C  2  40  ? 33.504  -16.236 17.289  1.00 74.70  ? 58   LYS C CD  1 
ATOM   9925  C  CE  . LYS C  2  40  ? 33.825  -17.727 17.199  1.00 76.56  ? 58   LYS C CE  1 
ATOM   9926  N  NZ  . LYS C  2  40  ? 35.271  -18.020 16.921  1.00 79.15  ? 58   LYS C NZ  1 
ATOM   9927  N  N   . GLY C  2  41  ? 34.008  -12.266 18.706  1.00 64.61  ? 59   GLY C N   1 
ATOM   9928  C  CA  . GLY C  2  41  ? 34.499  -12.329 20.068  1.00 62.84  ? 59   GLY C CA  1 
ATOM   9929  C  C   . GLY C  2  41  ? 33.470  -11.860 21.079  1.00 61.76  ? 59   GLY C C   1 
ATOM   9930  O  O   . GLY C  2  41  ? 32.281  -11.800 20.763  1.00 61.92  ? 59   GLY C O   1 
ATOM   9931  N  N   . LEU C  2  42  ? 33.928  -11.543 22.293  1.00 59.81  ? 60   LEU C N   1 
ATOM   9932  C  CA  . LEU C  2  42  ? 33.064  -11.073 23.370  1.00 58.11  ? 60   LEU C CA  1 
ATOM   9933  C  C   . LEU C  2  42  ? 33.358  -9.618  23.686  1.00 58.75  ? 60   LEU C C   1 
ATOM   9934  O  O   . LEU C  2  42  ? 34.521  -9.230  23.800  1.00 59.13  ? 60   LEU C O   1 
ATOM   9935  C  CB  . LEU C  2  42  ? 33.291  -11.886 24.638  1.00 55.75  ? 60   LEU C CB  1 
ATOM   9936  C  CG  . LEU C  2  42  ? 33.132  -13.396 24.581  1.00 54.07  ? 60   LEU C CG  1 
ATOM   9937  C  CD1 . LEU C  2  42  ? 33.430  -13.943 25.953  1.00 54.51  ? 60   LEU C CD1 1 
ATOM   9938  C  CD2 . LEU C  2  42  ? 31.739  -13.784 24.144  1.00 53.35  ? 60   LEU C CD2 1 
ATOM   9939  N  N   . LEU C  2  43  ? 32.297  -8.827  23.826  1.00 58.37  ? 61   LEU C N   1 
ATOM   9940  C  CA  . LEU C  2  43  ? 32.394  -7.407  24.140  1.00 58.71  ? 61   LEU C CA  1 
ATOM   9941  C  C   . LEU C  2  43  ? 31.925  -7.194  25.573  1.00 60.05  ? 61   LEU C C   1 
ATOM   9942  O  O   . LEU C  2  43  ? 30.728  -7.235  25.846  1.00 59.99  ? 61   LEU C O   1 
ATOM   9943  C  CB  . LEU C  2  43  ? 31.504  -6.604  23.196  1.00 58.03  ? 61   LEU C CB  1 
ATOM   9944  C  CG  . LEU C  2  43  ? 31.128  -5.196  23.652  1.00 59.04  ? 61   LEU C CG  1 
ATOM   9945  C  CD1 . LEU C  2  43  ? 32.372  -4.313  23.660  1.00 61.02  ? 61   LEU C CD1 1 
ATOM   9946  C  CD2 . LEU C  2  43  ? 30.080  -4.623  22.735  1.00 58.18  ? 61   LEU C CD2 1 
ATOM   9947  N  N   . HIS C  2  44  ? 32.859  -6.974  26.490  1.00 61.52  ? 62   HIS C N   1 
ATOM   9948  C  CA  . HIS C  2  44  ? 32.494  -6.770  27.881  1.00 63.25  ? 62   HIS C CA  1 
ATOM   9949  C  C   . HIS C  2  44  ? 32.346  -5.297  28.218  1.00 61.41  ? 62   HIS C C   1 
ATOM   9950  O  O   . HIS C  2  44  ? 33.243  -4.515  27.972  1.00 61.90  ? 62   HIS C O   1 
ATOM   9951  C  CB  . HIS C  2  44  ? 33.531  -7.418  28.803  1.00 68.18  ? 62   HIS C CB  1 
ATOM   9952  C  CG  . HIS C  2  44  ? 33.206  -7.285  30.265  1.00 75.91  ? 62   HIS C CG  1 
ATOM   9953  N  ND1 . HIS C  2  44  ? 33.303  -6.088  30.951  1.00 77.99  ? 62   HIS C ND1 1 
ATOM   9954  C  CD2 . HIS C  2  44  ? 32.759  -8.196  31.167  1.00 77.73  ? 62   HIS C CD2 1 
ATOM   9955  C  CE1 . HIS C  2  44  ? 32.930  -6.268  32.207  1.00 78.56  ? 62   HIS C CE1 1 
ATOM   9956  N  NE2 . HIS C  2  44  ? 32.595  -7.537  32.365  1.00 78.75  ? 62   HIS C NE2 1 
ATOM   9957  N  N   . ILE C  2  45  ? 31.205  -4.927  28.784  1.00 59.98  ? 63   ILE C N   1 
ATOM   9958  C  CA  . ILE C  2  45  ? 30.950  -3.545  29.155  1.00 59.10  ? 63   ILE C CA  1 
ATOM   9959  C  C   . ILE C  2  45  ? 30.568  -3.448  30.616  1.00 59.42  ? 63   ILE C C   1 
ATOM   9960  O  O   . ILE C  2  45  ? 29.981  -4.373  31.169  1.00 60.08  ? 63   ILE C O   1 
ATOM   9961  C  CB  . ILE C  2  45  ? 29.800  -2.947  28.339  1.00 58.81  ? 63   ILE C CB  1 
ATOM   9962  C  CG1 . ILE C  2  45  ? 30.170  -2.935  26.860  1.00 59.30  ? 63   ILE C CG1 1 
ATOM   9963  C  CG2 . ILE C  2  45  ? 29.499  -1.540  28.818  1.00 58.03  ? 63   ILE C CG2 1 
ATOM   9964  C  CD1 . ILE C  2  45  ? 28.998  -2.671  25.956  1.00 59.63  ? 63   ILE C CD1 1 
ATOM   9965  N  N   . PHE C  2  46  ? 30.931  -2.328  31.236  1.00 59.73  ? 64   PHE C N   1 
ATOM   9966  C  CA  . PHE C  2  46  ? 30.609  -2.043  32.632  1.00 59.55  ? 64   PHE C CA  1 
ATOM   9967  C  C   . PHE C  2  46  ? 30.190  -0.606  32.586  1.00 59.69  ? 64   PHE C C   1 
ATOM   9968  O  O   . PHE C  2  46  ? 30.949  0.234   32.131  1.00 60.24  ? 64   PHE C O   1 
ATOM   9969  C  CB  . PHE C  2  46  ? 31.814  -2.156  33.542  1.00 59.26  ? 64   PHE C CB  1 
ATOM   9970  C  CG  . PHE C  2  46  ? 31.490  -1.913  34.980  1.00 61.62  ? 64   PHE C CG  1 
ATOM   9971  C  CD1 . PHE C  2  46  ? 31.057  -2.958  35.799  1.00 62.26  ? 64   PHE C CD1 1 
ATOM   9972  C  CD2 . PHE C  2  46  ? 31.585  -0.625  35.518  1.00 63.03  ? 64   PHE C CD2 1 
ATOM   9973  C  CE1 . PHE C  2  46  ? 30.722  -2.731  37.142  1.00 62.52  ? 64   PHE C CE1 1 
ATOM   9974  C  CE2 . PHE C  2  46  ? 31.256  -0.378  36.859  1.00 62.82  ? 64   PHE C CE2 1 
ATOM   9975  C  CZ  . PHE C  2  46  ? 30.821  -1.436  37.675  1.00 62.60  ? 64   PHE C CZ  1 
ATOM   9976  N  N   . TYR C  2  47  ? 28.984  -0.323  33.050  1.00 60.58  ? 65   TYR C N   1 
ATOM   9977  C  CA  . TYR C  2  47  ? 28.445  1.027   33.002  1.00 62.21  ? 65   TYR C CA  1 
ATOM   9978  C  C   . TYR C  2  47  ? 27.426  1.134   34.093  1.00 62.66  ? 65   TYR C C   1 
ATOM   9979  O  O   . TYR C  2  47  ? 26.958  0.134   34.622  1.00 64.13  ? 65   TYR C O   1 
ATOM   9980  C  CB  . TYR C  2  47  ? 27.746  1.258   31.654  1.00 62.51  ? 65   TYR C CB  1 
ATOM   9981  C  CG  . TYR C  2  47  ? 27.408  2.691   31.288  1.00 62.42  ? 65   TYR C CG  1 
ATOM   9982  C  CD1 . TYR C  2  47  ? 28.392  3.671   31.258  1.00 64.71  ? 65   TYR C CD1 1 
ATOM   9983  C  CD2 . TYR C  2  47  ? 26.129  3.039   30.879  1.00 62.23  ? 65   TYR C CD2 1 
ATOM   9984  C  CE1 . TYR C  2  47  ? 28.117  4.974   30.820  1.00 65.95  ? 65   TYR C CE1 1 
ATOM   9985  C  CE2 . TYR C  2  47  ? 25.833  4.336   30.437  1.00 64.54  ? 65   TYR C CE2 1 
ATOM   9986  C  CZ  . TYR C  2  47  ? 26.833  5.305   30.408  1.00 65.67  ? 65   TYR C CZ  1 
ATOM   9987  O  OH  . TYR C  2  47  ? 26.567  6.605   29.994  1.00 64.68  ? 65   TYR C OH  1 
ATOM   9988  N  N   . ILE C  2  48  ? 27.069  2.365   34.405  1.00 63.82  ? 66   ILE C N   1 
ATOM   9989  C  CA  . ILE C  2  48  ? 26.081  2.666   35.423  1.00 65.03  ? 66   ILE C CA  1 
ATOM   9990  C  C   . ILE C  2  48  ? 25.387  3.859   34.770  1.00 62.94  ? 66   ILE C C   1 
ATOM   9991  O  O   . ILE C  2  48  ? 25.819  4.995   34.914  1.00 61.84  ? 66   ILE C O   1 
ATOM   9992  C  CB  . ILE C  2  48  ? 26.809  3.013   36.746  1.00 64.96  ? 66   ILE C CB  1 
ATOM   9993  C  CG1 . ILE C  2  48  ? 25.832  3.555   37.771  1.00 67.18  ? 66   ILE C CG1 1 
ATOM   9994  C  CG2 . ILE C  2  48  ? 27.936  4.006   36.481  1.00 68.29  ? 66   ILE C CG2 1 
ATOM   9995  C  CD1 . ILE C  2  48  ? 26.521  3.950   39.068  1.00 70.56  ? 66   ILE C CD1 1 
ATOM   9996  N  N   . PRO C  2  49  ? 24.317  3.594   33.994  1.00 63.25  ? 67   PRO C N   1 
ATOM   9997  C  CA  . PRO C  2  49  ? 23.534  4.606   33.270  1.00 66.32  ? 67   PRO C CA  1 
ATOM   9998  C  C   . PRO C  2  49  ? 22.960  5.726   34.133  1.00 67.35  ? 67   PRO C C   1 
ATOM   9999  O  O   . PRO C  2  49  ? 23.000  5.639   35.359  1.00 68.24  ? 67   PRO C O   1 
ATOM   10000 C  CB  . PRO C  2  49  ? 22.456  3.772   32.586  1.00 63.22  ? 67   PRO C CB  1 
ATOM   10001 C  CG  . PRO C  2  49  ? 22.227  2.686   33.557  1.00 62.43  ? 67   PRO C CG  1 
ATOM   10002 C  CD  . PRO C  2  49  ? 23.626  2.292   33.948  1.00 63.64  ? 67   PRO C CD  1 
ATOM   10003 N  N   . ARG C  2  50  ? 22.448  6.780   33.493  1.00 68.07  ? 68   ARG C N   1 
ATOM   10004 C  CA  . ARG C  2  50  ? 21.859  7.914   34.206  1.00 69.74  ? 68   ARG C CA  1 
ATOM   10005 C  C   . ARG C  2  50  ? 20.414  8.013   33.742  1.00 70.93  ? 68   ARG C C   1 
ATOM   10006 O  O   . ARG C  2  50  ? 19.701  8.976   34.039  1.00 71.42  ? 68   ARG C O   1 
ATOM   10007 C  CB  . ARG C  2  50  ? 22.603  9.215   33.881  1.00 69.97  ? 68   ARG C CB  1 
ATOM   10008 C  CG  . ARG C  2  50  ? 24.127  9.101   33.895  1.00 70.80  ? 68   ARG C CG  1 
ATOM   10009 C  CD  . ARG C  2  50  ? 24.772  9.139   35.280  1.00 70.52  ? 68   ARG C CD  1 
ATOM   10010 N  NE  . ARG C  2  50  ? 25.954  8.269   35.350  1.00 71.95  ? 68   ARG C NE  1 
ATOM   10011 C  CZ  . ARG C  2  50  ? 26.969  8.427   36.193  1.00 72.01  ? 68   ARG C CZ  1 
ATOM   10012 N  NH1 . ARG C  2  50  ? 26.972  9.439   37.046  1.00 72.34  ? 68   ARG C NH1 1 
ATOM   10013 N  NH2 . ARG C  2  50  ? 27.969  7.552   36.206  1.00 72.58  ? 68   ARG C NH2 1 
ATOM   10014 N  N   . ARG C  2  51  ? 20.008  7.000   32.985  1.00 72.16  ? 69   ARG C N   1 
ATOM   10015 C  CA  . ARG C  2  51  ? 18.652  6.875   32.462  1.00 72.46  ? 69   ARG C CA  1 
ATOM   10016 C  C   . ARG C  2  51  ? 18.376  5.390   32.391  1.00 70.75  ? 69   ARG C C   1 
ATOM   10017 O  O   . ARG C  2  51  ? 19.255  4.587   32.671  1.00 70.79  ? 69   ARG C O   1 
ATOM   10018 C  CB  . ARG C  2  51  ? 18.542  7.480   31.064  1.00 74.09  ? 69   ARG C CB  1 
ATOM   10019 C  CG  . ARG C  2  51  ? 18.431  8.998   31.050  1.00 79.23  ? 69   ARG C CG  1 
ATOM   10020 C  CD  . ARG C  2  51  ? 18.251  9.523   29.619  1.00 83.34  ? 69   ARG C CD  1 
ATOM   10021 N  NE  . ARG C  2  51  ? 16.901  10.018  29.328  1.00 87.93  ? 69   ARG C NE  1 
ATOM   10022 C  CZ  . ARG C  2  51  ? 15.779  9.302   29.443  1.00 90.97  ? 69   ARG C CZ  1 
ATOM   10023 N  NH1 . ARG C  2  51  ? 15.823  8.037   29.853  1.00 92.99  ? 69   ARG C NH1 1 
ATOM   10024 N  NH2 . ARG C  2  51  ? 14.602  9.846   29.139  1.00 90.74  ? 69   ARG C NH2 1 
ATOM   10025 N  N   . ASP C  2  52  ? 17.155  5.019   32.036  1.00 69.45  ? 70   ASP C N   1 
ATOM   10026 C  CA  . ASP C  2  52  ? 16.814  3.607   31.924  1.00 67.98  ? 70   ASP C CA  1 
ATOM   10027 C  C   . ASP C  2  52  ? 17.188  3.118   30.525  1.00 66.97  ? 70   ASP C C   1 
ATOM   10028 O  O   . ASP C  2  52  ? 16.997  3.843   29.545  1.00 67.48  ? 70   ASP C O   1 
ATOM   10029 C  CB  . ASP C  2  52  ? 15.321  3.410   32.163  1.00 67.76  ? 70   ASP C CB  1 
ATOM   10030 C  CG  . ASP C  2  52  ? 14.919  3.713   33.586  1.00 68.55  ? 70   ASP C CG  1 
ATOM   10031 O  OD1 . ASP C  2  52  ? 15.755  4.265   34.328  1.00 70.33  ? 70   ASP C OD1 1 
ATOM   10032 O  OD2 . ASP C  2  52  ? 13.769  3.407   33.964  1.00 68.54  ? 70   ASP C OD2 1 
ATOM   10033 N  N   . LEU C  2  53  ? 17.720  1.902   30.419  1.00 63.74  ? 71   LEU C N   1 
ATOM   10034 C  CA  . LEU C  2  53  ? 18.101  1.383   29.113  1.00 61.05  ? 71   LEU C CA  1 
ATOM   10035 C  C   . LEU C  2  53  ? 16.896  0.921   28.287  1.00 60.80  ? 71   LEU C C   1 
ATOM   10036 O  O   . LEU C  2  53  ? 17.029  0.458   27.160  1.00 59.65  ? 71   LEU C O   1 
ATOM   10037 C  CB  . LEU C  2  53  ? 19.118  0.265   29.285  1.00 58.46  ? 71   LEU C CB  1 
ATOM   10038 C  CG  . LEU C  2  53  ? 20.394  0.731   29.971  1.00 56.32  ? 71   LEU C CG  1 
ATOM   10039 C  CD1 . LEU C  2  53  ? 21.433  -0.356  29.871  1.00 56.01  ? 71   LEU C CD1 1 
ATOM   10040 C  CD2 . LEU C  2  53  ? 20.901  1.998   29.330  1.00 55.04  ? 71   LEU C CD2 1 
ATOM   10041 N  N   . LYS C  2  54  ? 15.716  1.083   28.869  1.00 61.96  ? 72   LYS C N   1 
ATOM   10042 C  CA  . LYS C  2  54  ? 14.432  0.748   28.259  1.00 62.98  ? 72   LYS C CA  1 
ATOM   10043 C  C   . LYS C  2  54  ? 14.379  1.252   26.810  1.00 62.63  ? 72   LYS C C   1 
ATOM   10044 O  O   . LYS C  2  54  ? 14.483  2.444   26.569  1.00 62.58  ? 72   LYS C O   1 
ATOM   10045 C  CB  . LYS C  2  54  ? 13.336  1.407   29.109  1.00 64.24  ? 72   LYS C CB  1 
ATOM   10046 C  CG  . LYS C  2  54  ? 11.913  1.276   28.641  1.00 67.42  ? 72   LYS C CG  1 
ATOM   10047 C  CD  . LYS C  2  54  ? 11.001  2.022   29.613  1.00 71.12  ? 72   LYS C CD  1 
ATOM   10048 C  CE  . LYS C  2  54  ? 9.516   1.924   29.213  1.00 74.22  ? 72   LYS C CE  1 
ATOM   10049 N  NZ  . LYS C  2  54  ? 8.590   2.636   30.168  1.00 74.88  ? 72   LYS C NZ  1 
ATOM   10050 N  N   . GLN C  2  55  ? 14.227  0.345   25.848  1.00 63.10  ? 73   GLN C N   1 
ATOM   10051 C  CA  . GLN C  2  55  ? 14.162  0.713   24.431  1.00 62.97  ? 73   GLN C CA  1 
ATOM   10052 C  C   . GLN C  2  55  ? 15.374  1.466   23.897  1.00 62.78  ? 73   GLN C C   1 
ATOM   10053 O  O   . GLN C  2  55  ? 15.214  2.478   23.207  1.00 62.80  ? 73   GLN C O   1 
ATOM   10054 C  CB  . GLN C  2  55  ? 12.911  1.536   24.155  1.00 63.38  ? 73   GLN C CB  1 
ATOM   10055 C  CG  . GLN C  2  55  ? 11.633  0.743   24.372  1.00 67.38  ? 73   GLN C CG  1 
ATOM   10056 C  CD  . GLN C  2  55  ? 10.413  1.623   24.509  1.00 69.03  ? 73   GLN C CD  1 
ATOM   10057 O  OE1 . GLN C  2  55  ? 9.984   2.270   23.551  1.00 68.98  ? 73   GLN C OE1 1 
ATOM   10058 N  NE2 . GLN C  2  55  ? 9.845   1.659   25.716  1.00 70.71  ? 73   GLN C NE2 1 
ATOM   10059 N  N   . LEU C  2  56  ? 16.573  0.958   24.204  1.00 61.58  ? 74   LEU C N   1 
ATOM   10060 C  CA  . LEU C  2  56  ? 17.848  1.542   23.770  1.00 59.97  ? 74   LEU C CA  1 
ATOM   10061 C  C   . LEU C  2  56  ? 17.970  1.485   22.247  1.00 60.35  ? 74   LEU C C   1 
ATOM   10062 O  O   . LEU C  2  56  ? 17.256  0.741   21.590  1.00 60.74  ? 74   LEU C O   1 
ATOM   10063 C  CB  . LEU C  2  56  ? 19.008  0.745   24.377  1.00 57.36  ? 74   LEU C CB  1 
ATOM   10064 C  CG  . LEU C  2  56  ? 20.331  1.390   24.797  1.00 57.99  ? 74   LEU C CG  1 
ATOM   10065 C  CD1 . LEU C  2  56  ? 21.343  0.288   25.059  1.00 56.85  ? 74   LEU C CD1 1 
ATOM   10066 C  CD2 . LEU C  2  56  ? 20.856  2.317   23.736  1.00 58.67  ? 74   LEU C CD2 1 
ATOM   10067 N  N   . TYR C  2  57  ? 18.854  2.296   21.685  1.00 61.46  ? 75   TYR C N   1 
ATOM   10068 C  CA  . TYR C  2  57  ? 19.120  2.283   20.250  1.00 62.33  ? 75   TYR C CA  1 
ATOM   10069 C  C   . TYR C  2  57  ? 20.219  3.276   19.940  1.00 62.27  ? 75   TYR C C   1 
ATOM   10070 O  O   . TYR C  2  57  ? 20.311  4.325   20.576  1.00 63.67  ? 75   TYR C O   1 
ATOM   10071 C  CB  . TYR C  2  57  ? 17.857  2.551   19.402  1.00 63.06  ? 75   TYR C CB  1 
ATOM   10072 C  CG  . TYR C  2  57  ? 17.382  3.989   19.208  1.00 64.51  ? 75   TYR C CG  1 
ATOM   10073 C  CD1 . TYR C  2  57  ? 16.527  4.596   20.125  1.00 64.85  ? 75   TYR C CD1 1 
ATOM   10074 C  CD2 . TYR C  2  57  ? 17.711  4.700   18.049  1.00 64.15  ? 75   TYR C CD2 1 
ATOM   10075 C  CE1 . TYR C  2  57  ? 16.008  5.859   19.891  1.00 66.04  ? 75   TYR C CE1 1 
ATOM   10076 C  CE2 . TYR C  2  57  ? 17.198  5.957   17.809  1.00 65.01  ? 75   TYR C CE2 1 
ATOM   10077 C  CZ  . TYR C  2  57  ? 16.346  6.533   18.734  1.00 66.40  ? 75   TYR C CZ  1 
ATOM   10078 O  OH  . TYR C  2  57  ? 15.831  7.793   18.517  1.00 68.53  ? 75   TYR C OH  1 
ATOM   10079 N  N   . PHE C  2  58  ? 21.085  2.917   19.003  1.00 61.13  ? 76   PHE C N   1 
ATOM   10080 C  CA  . PHE C  2  58  ? 22.185  3.781   18.624  1.00 61.25  ? 76   PHE C CA  1 
ATOM   10081 C  C   . PHE C  2  58  ? 21.848  4.485   17.316  1.00 61.52  ? 76   PHE C C   1 
ATOM   10082 O  O   . PHE C  2  58  ? 21.079  3.969   16.514  1.00 62.26  ? 76   PHE C O   1 
ATOM   10083 C  CB  . PHE C  2  58  ? 23.452  2.954   18.422  1.00 59.58  ? 76   PHE C CB  1 
ATOM   10084 C  CG  . PHE C  2  58  ? 23.889  2.189   19.635  1.00 60.57  ? 76   PHE C CG  1 
ATOM   10085 C  CD1 . PHE C  2  58  ? 24.399  0.901   19.506  1.00 61.15  ? 76   PHE C CD1 1 
ATOM   10086 C  CD2 . PHE C  2  58  ? 23.852  2.761   20.895  1.00 61.80  ? 76   PHE C CD2 1 
ATOM   10087 C  CE1 . PHE C  2  58  ? 24.869  0.193   20.606  1.00 60.49  ? 76   PHE C CE1 1 
ATOM   10088 C  CE2 . PHE C  2  58  ? 24.323  2.058   22.008  1.00 62.46  ? 76   PHE C CE2 1 
ATOM   10089 C  CZ  . PHE C  2  58  ? 24.833  0.768   21.858  1.00 61.41  ? 76   PHE C CZ  1 
ATOM   10090 N  N   . ASN C  2  59  ? 22.380  5.685   17.127  1.00 61.07  ? 77   ASN C N   1 
ATOM   10091 C  CA  . ASN C  2  59  ? 22.206  6.394   15.876  1.00 59.32  ? 77   ASN C CA  1 
ATOM   10092 C  C   . ASN C  2  59  ? 23.650  6.373   15.432  1.00 58.72  ? 77   ASN C C   1 
ATOM   10093 O  O   . ASN C  2  59  ? 24.528  6.783   16.183  1.00 58.70  ? 77   ASN C O   1 
ATOM   10094 C  CB  . ASN C  2  59  ? 21.709  7.819   16.091  1.00 58.15  ? 77   ASN C CB  1 
ATOM   10095 C  CG  . ASN C  2  59  ? 20.208  7.928   15.965  1.00 58.36  ? 77   ASN C CG  1 
ATOM   10096 O  OD1 . ASN C  2  59  ? 19.629  7.509   14.966  1.00 58.04  ? 77   ASN C OD1 1 
ATOM   10097 N  ND2 . ASN C  2  59  ? 19.568  8.503   16.973  1.00 60.19  ? 77   ASN C ND2 1 
ATOM   10098 N  N   . LEU C  2  60  ? 23.921  5.847   14.251  1.00 58.00  ? 78   LEU C N   1 
ATOM   10099 C  CA  . LEU C  2  60  ? 25.301  5.774   13.834  1.00 59.20  ? 78   LEU C CA  1 
ATOM   10100 C  C   . LEU C  2  60  ? 25.652  6.710   12.698  1.00 60.46  ? 78   LEU C C   1 
ATOM   10101 O  O   . LEU C  2  60  ? 24.980  6.733   11.663  1.00 60.76  ? 78   LEU C O   1 
ATOM   10102 C  CB  . LEU C  2  60  ? 25.657  4.338   13.451  1.00 58.49  ? 78   LEU C CB  1 
ATOM   10103 C  CG  . LEU C  2  60  ? 25.441  3.220   14.466  1.00 57.88  ? 78   LEU C CG  1 
ATOM   10104 C  CD1 . LEU C  2  60  ? 25.897  1.924   13.845  1.00 57.45  ? 78   LEU C CD1 1 
ATOM   10105 C  CD2 . LEU C  2  60  ? 26.213  3.483   15.741  1.00 57.86  ? 78   LEU C CD2 1 
ATOM   10106 N  N   . TYR C  2  61  ? 26.714  7.484   12.906  1.00 60.78  ? 79   TYR C N   1 
ATOM   10107 C  CA  . TYR C  2  61  ? 27.187  8.417   11.900  1.00 62.60  ? 79   TYR C CA  1 
ATOM   10108 C  C   . TYR C  2  61  ? 28.599  7.990   11.493  1.00 65.97  ? 79   TYR C C   1 
ATOM   10109 O  O   . TYR C  2  61  ? 29.602  8.404   12.105  1.00 68.04  ? 79   TYR C O   1 
ATOM   10110 C  CB  . TYR C  2  61  ? 27.163  9.841   12.456  1.00 59.51  ? 79   TYR C CB  1 
ATOM   10111 C  CG  . TYR C  2  61  ? 25.801  10.256  12.994  1.00 57.61  ? 79   TYR C CG  1 
ATOM   10112 C  CD1 . TYR C  2  61  ? 25.511  10.177  14.367  1.00 57.16  ? 79   TYR C CD1 1 
ATOM   10113 C  CD2 . TYR C  2  61  ? 24.786  10.697  12.133  1.00 55.18  ? 79   TYR C CD2 1 
ATOM   10114 C  CE1 . TYR C  2  61  ? 24.249  10.526  14.863  1.00 54.42  ? 79   TYR C CE1 1 
ATOM   10115 C  CE2 . TYR C  2  61  ? 23.527  11.044  12.623  1.00 53.40  ? 79   TYR C CE2 1 
ATOM   10116 C  CZ  . TYR C  2  61  ? 23.267  10.953  13.985  1.00 54.07  ? 79   TYR C CZ  1 
ATOM   10117 O  OH  . TYR C  2  61  ? 22.019  11.265  14.474  1.00 54.07  ? 79   TYR C OH  1 
ATOM   10118 N  N   . ILE C  2  62  ? 28.666  7.152   10.454  1.00 67.95  ? 80   ILE C N   1 
ATOM   10119 C  CA  . ILE C  2  62  ? 29.940  6.626   9.966   1.00 68.63  ? 80   ILE C CA  1 
ATOM   10120 C  C   . ILE C  2  62  ? 30.576  7.569   8.955   1.00 69.59  ? 80   ILE C C   1 
ATOM   10121 O  O   . ILE C  2  62  ? 29.889  8.336   8.276   1.00 68.07  ? 80   ILE C O   1 
ATOM   10122 C  CB  . ILE C  2  62  ? 29.776  5.213   9.307   1.00 68.05  ? 80   ILE C CB  1 
ATOM   10123 C  CG1 . ILE C  2  62  ? 28.763  4.366   10.075  1.00 65.98  ? 80   ILE C CG1 1 
ATOM   10124 C  CG2 . ILE C  2  62  ? 31.101  4.477   9.315   1.00 68.38  ? 80   ILE C CG2 1 
ATOM   10125 C  CD1 . ILE C  2  62  ? 27.336  4.722   9.741   1.00 65.26  ? 80   ILE C CD1 1 
ATOM   10126 N  N   . THR C  2  63  ? 31.900  7.495   8.872   1.00 72.01  ? 81   THR C N   1 
ATOM   10127 C  CA  . THR C  2  63  ? 32.683  8.321   7.966   1.00 73.78  ? 81   THR C CA  1 
ATOM   10128 C  C   . THR C  2  63  ? 33.911  7.564   7.449   1.00 74.93  ? 81   THR C C   1 
ATOM   10129 O  O   . THR C  2  63  ? 34.731  7.052   8.228   1.00 74.33  ? 81   THR C O   1 
ATOM   10130 C  CB  . THR C  2  63  ? 33.148  9.622   8.665   1.00 74.06  ? 81   THR C CB  1 
ATOM   10131 O  OG1 . THR C  2  63  ? 32.004  10.388  9.061   1.00 74.96  ? 81   THR C OG1 1 
ATOM   10132 C  CG2 . THR C  2  63  ? 33.990  10.459  7.732   1.00 75.64  ? 81   THR C CG2 1 
ATOM   10133 N  N   . VAL C  2  64  ? 34.012  7.501   6.121   1.00 76.31  ? 82   VAL C N   1 
ATOM   10134 C  CA  . VAL C  2  64  ? 35.116  6.832   5.428   1.00 76.69  ? 82   VAL C CA  1 
ATOM   10135 C  C   . VAL C  2  64  ? 36.015  7.888   4.776   1.00 77.39  ? 82   VAL C C   1 
ATOM   10136 O  O   . VAL C  2  64  ? 35.605  8.525   3.803   1.00 78.16  ? 82   VAL C O   1 
ATOM   10137 C  CB  . VAL C  2  64  ? 34.598  5.914   4.296   1.00 75.95  ? 82   VAL C CB  1 
ATOM   10138 C  CG1 . VAL C  2  64  ? 35.677  4.929   3.893   1.00 74.21  ? 82   VAL C CG1 1 
ATOM   10139 C  CG2 . VAL C  2  64  ? 33.334  5.207   4.724   1.00 76.29  ? 82   VAL C CG2 1 
ATOM   10140 N  N   . ASN C  2  65  ? 37.224  8.069   5.299   1.00 77.02  ? 83   ASN C N   1 
ATOM   10141 C  CA  . ASN C  2  65  ? 38.162  9.042   4.746   1.00 77.25  ? 83   ASN C CA  1 
ATOM   10142 C  C   . ASN C  2  65  ? 37.450  10.283  4.202   1.00 78.44  ? 83   ASN C C   1 
ATOM   10143 O  O   . ASN C  2  65  ? 37.457  10.510  2.993   1.00 78.90  ? 83   ASN C O   1 
ATOM   10144 C  CB  . ASN C  2  65  ? 38.994  8.414   3.618   1.00 74.35  ? 83   ASN C CB  1 
ATOM   10145 C  CG  . ASN C  2  65  ? 39.719  7.153   4.048   1.00 73.66  ? 83   ASN C CG  1 
ATOM   10146 O  OD1 . ASN C  2  65  ? 40.365  7.119   5.095   1.00 73.30  ? 83   ASN C OD1 1 
ATOM   10147 N  ND2 . ASN C  2  65  ? 39.631  6.109   3.230   1.00 72.65  ? 83   ASN C ND2 1 
ATOM   10148 N  N   . THR C  2  66  ? 36.831  11.062  5.095   1.00 79.60  ? 84   THR C N   1 
ATOM   10149 C  CA  . THR C  2  66  ? 36.114  12.299  4.733   1.00 81.76  ? 84   THR C CA  1 
ATOM   10150 C  C   . THR C  2  66  ? 34.703  12.082  4.166   1.00 82.00  ? 84   THR C C   1 
ATOM   10151 O  O   . THR C  2  66  ? 33.875  13.003  4.176   1.00 82.12  ? 84   THR C O   1 
ATOM   10152 C  CB  . THR C  2  66  ? 36.931  13.175  3.701   1.00 83.27  ? 84   THR C CB  1 
ATOM   10153 O  OG1 . THR C  2  66  ? 36.838  14.554  4.074   1.00 85.74  ? 84   THR C OG1 1 
ATOM   10154 C  CG2 . THR C  2  66  ? 36.372  13.049  2.270   1.00 83.28  ? 84   THR C CG2 1 
ATOM   10155 N  N   . MET C  2  67  ? 34.436  10.874  3.670   1.00 81.59  ? 85   MET C N   1 
ATOM   10156 C  CA  . MET C  2  67  ? 33.134  10.546  3.093   1.00 79.69  ? 85   MET C CA  1 
ATOM   10157 C  C   . MET C  2  67  ? 32.093  10.232  4.163   1.00 78.40  ? 85   MET C C   1 
ATOM   10158 O  O   . MET C  2  67  ? 32.397  9.630   5.193   1.00 78.02  ? 85   MET C O   1 
ATOM   10159 C  CB  . MET C  2  67  ? 33.264  9.360   2.136   1.00 79.82  ? 85   MET C CB  1 
ATOM   10160 C  CG  . MET C  2  67  ? 33.315  9.738   0.666   1.00 79.50  ? 85   MET C CG  1 
ATOM   10161 S  SD  . MET C  2  67  ? 34.720  8.982   -0.150  1.00 81.42  ? 85   MET C SD  1 
ATOM   10162 C  CE  . MET C  2  67  ? 34.310  7.257   -0.071  1.00 79.33  ? 85   MET C CE  1 
ATOM   10163 N  N   . ASN C  2  68  ? 30.857  10.642  3.911   1.00 77.43  ? 86   ASN C N   1 
ATOM   10164 C  CA  . ASN C  2  68  ? 29.774  10.416  4.858   1.00 76.75  ? 86   ASN C CA  1 
ATOM   10165 C  C   . ASN C  2  68  ? 28.698  9.453   4.365   1.00 74.93  ? 86   ASN C C   1 
ATOM   10166 O  O   . ASN C  2  68  ? 28.199  9.566   3.246   1.00 75.82  ? 86   ASN C O   1 
ATOM   10167 C  CB  . ASN C  2  68  ? 29.140  11.757  5.245   1.00 78.86  ? 86   ASN C CB  1 
ATOM   10168 C  CG  . ASN C  2  68  ? 29.695  12.309  6.554   1.00 82.13  ? 86   ASN C CG  1 
ATOM   10169 O  OD1 . ASN C  2  68  ? 30.901  12.229  6.822   1.00 83.51  ? 86   ASN C OD1 1 
ATOM   10170 N  ND2 . ASN C  2  68  ? 28.814  12.882  7.373   1.00 83.53  ? 86   ASN C ND2 1 
ATOM   10171 N  N   . LEU C  2  69  ? 28.352  8.497   5.221   1.00 72.04  ? 87   LEU C N   1 
ATOM   10172 C  CA  . LEU C  2  69  ? 27.335  7.500   4.923   1.00 67.70  ? 87   LEU C CA  1 
ATOM   10173 C  C   . LEU C  2  69  ? 26.074  7.961   5.618   1.00 65.90  ? 87   LEU C C   1 
ATOM   10174 O  O   . LEU C  2  69  ? 26.143  8.670   6.617   1.00 66.04  ? 87   LEU C O   1 
ATOM   10175 C  CB  . LEU C  2  69  ? 27.748  6.150   5.497   1.00 65.43  ? 87   LEU C CB  1 
ATOM   10176 C  CG  . LEU C  2  69  ? 28.904  5.417   4.830   1.00 64.43  ? 87   LEU C CG  1 
ATOM   10177 C  CD1 . LEU C  2  69  ? 29.710  4.642   5.855   1.00 64.19  ? 87   LEU C CD1 1 
ATOM   10178 C  CD2 . LEU C  2  69  ? 28.340  4.508   3.763   1.00 63.70  ? 87   LEU C CD2 1 
ATOM   10179 N  N   . PRO C  2  70  ? 24.904  7.583   5.093   1.00 64.12  ? 88   PRO C N   1 
ATOM   10180 C  CA  . PRO C  2  70  ? 23.641  7.983   5.717   1.00 63.10  ? 88   PRO C CA  1 
ATOM   10181 C  C   . PRO C  2  70  ? 23.582  7.566   7.195   1.00 62.39  ? 88   PRO C C   1 
ATOM   10182 O  O   . PRO C  2  70  ? 24.407  6.775   7.675   1.00 62.12  ? 88   PRO C O   1 
ATOM   10183 C  CB  . PRO C  2  70  ? 22.608  7.266   4.866   1.00 63.25  ? 88   PRO C CB  1 
ATOM   10184 C  CG  . PRO C  2  70  ? 23.225  7.326   3.507   1.00 63.02  ? 88   PRO C CG  1 
ATOM   10185 C  CD  . PRO C  2  70  ? 24.671  6.967   3.778   1.00 63.03  ? 88   PRO C CD  1 
ATOM   10186 N  N   . LYS C  2  71  ? 22.614  8.107   7.923   1.00 61.28  ? 89   LYS C N   1 
ATOM   10187 C  CA  . LYS C  2  71  ? 22.480  7.769   9.328   1.00 60.72  ? 89   LYS C CA  1 
ATOM   10188 C  C   . LYS C  2  71  ? 22.065  6.321   9.384   1.00 60.65  ? 89   LYS C C   1 
ATOM   10189 O  O   . LYS C  2  71  ? 21.505  5.805   8.428   1.00 60.80  ? 89   LYS C O   1 
ATOM   10190 C  CB  . LYS C  2  71  ? 21.402  8.618   10.006  1.00 60.57  ? 89   LYS C CB  1 
ATOM   10191 C  CG  . LYS C  2  71  ? 21.249  8.303   11.484  1.00 61.20  ? 89   LYS C CG  1 
ATOM   10192 C  CD  . LYS C  2  71  ? 20.360  9.290   12.220  1.00 62.72  ? 89   LYS C CD  1 
ATOM   10193 C  CE  . LYS C  2  71  ? 18.888  9.057   11.961  1.00 62.63  ? 89   LYS C CE  1 
ATOM   10194 N  NZ  . LYS C  2  71  ? 18.092  9.939   12.859  1.00 62.84  ? 89   LYS C NZ  1 
ATOM   10195 N  N   . ARG C  2  72  ? 22.357  5.661   10.495  1.00 60.02  ? 90   ARG C N   1 
ATOM   10196 C  CA  . ARG C  2  72  ? 21.966  4.274   10.675  1.00 58.97  ? 90   ARG C CA  1 
ATOM   10197 C  C   . ARG C  2  72  ? 21.297  4.174   12.021  1.00 59.41  ? 90   ARG C C   1 
ATOM   10198 O  O   . ARG C  2  72  ? 21.833  4.664   13.014  1.00 61.17  ? 90   ARG C O   1 
ATOM   10199 C  CB  . ARG C  2  72  ? 23.176  3.339   10.681  1.00 57.95  ? 90   ARG C CB  1 
ATOM   10200 C  CG  . ARG C  2  72  ? 23.831  3.130   9.343   1.00 60.90  ? 90   ARG C CG  1 
ATOM   10201 C  CD  . ARG C  2  72  ? 24.907  2.063   9.434   1.00 60.97  ? 90   ARG C CD  1 
ATOM   10202 N  NE  . ARG C  2  72  ? 24.341  0.725   9.601   1.00 63.18  ? 90   ARG C NE  1 
ATOM   10203 C  CZ  . ARG C  2  72  ? 23.936  -0.051  8.600   1.00 63.18  ? 90   ARG C CZ  1 
ATOM   10204 N  NH1 . ARG C  2  72  ? 24.029  0.369   7.344   1.00 63.15  ? 90   ARG C NH1 1 
ATOM   10205 N  NH2 . ARG C  2  72  ? 23.455  -1.257  8.857   1.00 62.99  ? 90   ARG C NH2 1 
ATOM   10206 N  N   . LYS C  2  73  ? 20.113  3.575   12.059  1.00 58.46  ? 91   LYS C N   1 
ATOM   10207 C  CA  . LYS C  2  73  ? 19.439  3.377   13.330  1.00 57.27  ? 91   LYS C CA  1 
ATOM   10208 C  C   . LYS C  2  73  ? 19.552  1.893   13.643  1.00 57.23  ? 91   LYS C C   1 
ATOM   10209 O  O   . LYS C  2  73  ? 19.048  1.058   12.903  1.00 57.71  ? 91   LYS C O   1 
ATOM   10210 C  CB  . LYS C  2  73  ? 17.977  3.782   13.254  1.00 55.21  ? 91   LYS C CB  1 
ATOM   10211 C  CG  . LYS C  2  73  ? 17.257  3.599   14.566  1.00 55.05  ? 91   LYS C CG  1 
ATOM   10212 C  CD  . LYS C  2  73  ? 15.846  4.155   14.522  1.00 56.39  ? 91   LYS C CD  1 
ATOM   10213 C  CE  . LYS C  2  73  ? 15.134  3.958   15.854  1.00 56.74  ? 91   LYS C CE  1 
ATOM   10214 N  NZ  . LYS C  2  73  ? 13.897  4.765   15.941  1.00 57.62  ? 91   LYS C NZ  1 
ATOM   10215 N  N   . GLU C  2  74  ? 20.261  1.565   14.712  1.00 57.10  ? 92   GLU C N   1 
ATOM   10216 C  CA  . GLU C  2  74  ? 20.427  0.183   15.126  1.00 58.75  ? 92   GLU C CA  1 
ATOM   10217 C  C   . GLU C  2  74  ? 19.725  0.051   16.473  1.00 58.80  ? 92   GLU C C   1 
ATOM   10218 O  O   . GLU C  2  74  ? 20.082  0.719   17.442  1.00 59.84  ? 92   GLU C O   1 
ATOM   10219 C  CB  . GLU C  2  74  ? 21.912  -0.169  15.279  1.00 60.82  ? 92   GLU C CB  1 
ATOM   10220 C  CG  . GLU C  2  74  ? 22.709  -0.212  13.978  1.00 65.26  ? 92   GLU C CG  1 
ATOM   10221 C  CD  . GLU C  2  74  ? 22.080  -1.118  12.919  1.00 68.76  ? 92   GLU C CD  1 
ATOM   10222 O  OE1 . GLU C  2  74  ? 21.600  -2.228  13.267  1.00 69.50  ? 92   GLU C OE1 1 
ATOM   10223 O  OE2 . GLU C  2  74  ? 22.078  -0.719  11.732  1.00 70.14  ? 92   GLU C OE2 1 
ATOM   10224 N  N   . VAL C  2  75  ? 18.725  -0.816  16.533  1.00 57.90  ? 93   VAL C N   1 
ATOM   10225 C  CA  . VAL C  2  75  ? 17.966  -0.998  17.757  1.00 55.34  ? 93   VAL C CA  1 
ATOM   10226 C  C   . VAL C  2  75  ? 18.445  -2.131  18.655  1.00 55.76  ? 93   VAL C C   1 
ATOM   10227 O  O   . VAL C  2  75  ? 18.611  -3.252  18.209  1.00 57.16  ? 93   VAL C O   1 
ATOM   10228 C  CB  . VAL C  2  75  ? 16.488  -1.264  17.438  1.00 52.54  ? 93   VAL C CB  1 
ATOM   10229 C  CG1 . VAL C  2  75  ? 15.657  -1.120  18.696  1.00 51.34  ? 93   VAL C CG1 1 
ATOM   10230 C  CG2 . VAL C  2  75  ? 16.019  -0.339  16.351  1.00 49.43  ? 93   VAL C CG2 1 
ATOM   10231 N  N   . ILE C  2  76  ? 18.673  -1.826  19.922  1.00 56.29  ? 94   ILE C N   1 
ATOM   10232 C  CA  . ILE C  2  76  ? 19.056  -2.831  20.904  1.00 57.20  ? 94   ILE C CA  1 
ATOM   10233 C  C   . ILE C  2  76  ? 17.851  -2.667  21.805  1.00 59.31  ? 94   ILE C C   1 
ATOM   10234 O  O   . ILE C  2  76  ? 17.593  -1.562  22.248  1.00 62.30  ? 94   ILE C O   1 
ATOM   10235 C  CB  . ILE C  2  76  ? 20.286  -2.409  21.713  1.00 56.92  ? 94   ILE C CB  1 
ATOM   10236 C  CG1 . ILE C  2  76  ? 21.175  -1.475  20.881  1.00 55.28  ? 94   ILE C CG1 1 
ATOM   10237 C  CG2 . ILE C  2  76  ? 20.996  -3.646  22.245  1.00 54.75  ? 94   ILE C CG2 1 
ATOM   10238 C  CD1 . ILE C  2  76  ? 21.642  -2.038  19.573  1.00 55.96  ? 94   ILE C CD1 1 
ATOM   10239 N  N   . CYS C  2  77  ? 17.096  -3.720  22.073  1.00 60.85  ? 95   CYS C N   1 
ATOM   10240 C  CA  . CYS C  2  77  ? 15.895  -3.593  22.919  1.00 62.99  ? 95   CYS C CA  1 
ATOM   10241 C  C   . CYS C  2  77  ? 14.710  -2.925  22.216  1.00 64.18  ? 95   CYS C C   1 
ATOM   10242 O  O   . CYS C  2  77  ? 14.698  -1.709  22.035  1.00 63.73  ? 95   CYS C O   1 
ATOM   10243 C  CB  . CYS C  2  77  ? 16.143  -2.755  24.185  1.00 62.06  ? 95   CYS C CB  1 
ATOM   10244 S  SG  . CYS C  2  77  ? 17.673  -3.002  25.127  1.00 64.39  ? 95   CYS C SG  1 
ATOM   10245 N  N   . ARG C  2  78  ? 13.709  -3.708  21.830  1.00 66.67  ? 96   ARG C N   1 
ATOM   10246 C  CA  . ARG C  2  78  ? 12.522  -3.133  21.209  1.00 68.37  ? 96   ARG C CA  1 
ATOM   10247 C  C   . ARG C  2  78  ? 11.590  -2.638  22.323  1.00 69.03  ? 96   ARG C C   1 
ATOM   10248 O  O   . ARG C  2  78  ? 10.823  -1.701  22.118  1.00 70.75  ? 96   ARG C O   1 
ATOM   10249 C  CB  . ARG C  2  78  ? 11.815  -4.157  20.303  1.00 69.49  ? 96   ARG C CB  1 
ATOM   10250 C  CG  . ARG C  2  78  ? 12.146  -5.625  20.597  1.00 73.35  ? 96   ARG C CG  1 
ATOM   10251 C  CD  . ARG C  2  78  ? 11.491  -6.583  19.598  1.00 74.69  ? 96   ARG C CD  1 
ATOM   10252 N  NE  . ARG C  2  78  ? 10.044  -6.716  19.792  1.00 76.47  ? 96   ARG C NE  1 
ATOM   10253 C  CZ  . ARG C  2  78  ? 9.478   -7.335  20.829  1.00 77.50  ? 96   ARG C CZ  1 
ATOM   10254 N  NH1 . ARG C  2  78  ? 10.245  -7.879  21.775  1.00 75.97  ? 96   ARG C NH1 1 
ATOM   10255 N  NH2 . ARG C  2  78  ? 8.145   -7.420  20.919  1.00 76.61  ? 96   ARG C NH2 1 
ATOM   10256 N  N   . GLY C  2  79  ? 11.662  -3.254  23.506  1.00 68.69  ? 97   GLY C N   1 
ATOM   10257 C  CA  . GLY C  2  79  ? 10.832  -2.798  24.613  1.00 69.22  ? 97   GLY C CA  1 
ATOM   10258 C  C   . GLY C  2  79  ? 9.981   -3.796  25.396  1.00 69.84  ? 97   GLY C C   1 
ATOM   10259 O  O   . GLY C  2  79  ? 9.451   -3.463  26.457  1.00 70.09  ? 97   GLY C O   1 
ATOM   10260 N  N   . SER C  2  80  ? 9.830   -5.014  24.900  1.00 69.18  ? 98   SER C N   1 
ATOM   10261 C  CA  . SER C  2  80  ? 9.019   -5.996  25.611  1.00 69.19  ? 98   SER C CA  1 
ATOM   10262 C  C   . SER C  2  80  ? 9.652   -7.389  25.531  1.00 68.95  ? 98   SER C C   1 
ATOM   10263 O  O   . SER C  2  80  ? 9.803   -7.957  24.439  1.00 70.12  ? 98   SER C O   1 
ATOM   10264 C  CB  . SER C  2  80  ? 7.601   -6.011  25.024  1.00 69.67  ? 98   SER C CB  1 
ATOM   10265 O  OG  . SER C  2  80  ? 6.797   -7.023  25.615  1.00 71.15  ? 98   SER C OG  1 
ATOM   10266 N  N   . ASP C  2  81  ? 10.021  -7.940  26.685  1.00 66.21  ? 99   ASP C N   1 
ATOM   10267 C  CA  . ASP C  2  81  ? 10.651  -9.256  26.728  1.00 64.33  ? 99   ASP C CA  1 
ATOM   10268 C  C   . ASP C  2  81  ? 11.794  -9.267  25.706  1.00 62.21  ? 99   ASP C C   1 
ATOM   10269 O  O   . ASP C  2  81  ? 11.815  -10.063 24.776  1.00 61.30  ? 99   ASP C O   1 
ATOM   10270 C  CB  . ASP C  2  81  ? 9.606   -10.334 26.417  1.00 64.60  ? 99   ASP C CB  1 
ATOM   10271 C  CG  . ASP C  2  81  ? 8.618   -10.545 27.569  1.00 66.51  ? 99   ASP C CG  1 
ATOM   10272 O  OD1 . ASP C  2  81  ? 7.418   -10.763 27.298  1.00 68.50  ? 99   ASP C OD1 1 
ATOM   10273 O  OD2 . ASP C  2  81  ? 9.036   -10.515 28.751  1.00 66.74  ? 99   ASP C OD2 1 
ATOM   10274 N  N   . ASP C  2  82  ? 12.752  -8.368  25.911  1.00 60.91  ? 100  ASP C N   1 
ATOM   10275 C  CA  . ASP C  2  82  ? 13.887  -8.207  25.009  1.00 59.75  ? 100  ASP C CA  1 
ATOM   10276 C  C   . ASP C  2  82  ? 14.937  -9.300  25.064  1.00 58.48  ? 100  ASP C C   1 
ATOM   10277 O  O   . ASP C  2  82  ? 14.995  -10.081 26.009  1.00 58.72  ? 100  ASP C O   1 
ATOM   10278 C  CB  . ASP C  2  82  ? 14.559  -6.854  25.254  1.00 62.00  ? 100  ASP C CB  1 
ATOM   10279 C  CG  . ASP C  2  82  ? 13.687  -5.678  24.833  1.00 63.13  ? 100  ASP C CG  1 
ATOM   10280 O  OD1 . ASP C  2  82  ? 13.256  -5.677  23.657  1.00 62.96  ? 100  ASP C OD1 1 
ATOM   10281 O  OD2 . ASP C  2  82  ? 13.447  -4.760  25.666  1.00 62.70  ? 100  ASP C OD2 1 
ATOM   10282 N  N   . ASP C  2  83  ? 15.780  -9.332  24.038  1.00 56.73  ? 101  ASP C N   1 
ATOM   10283 C  CA  . ASP C  2  83  ? 16.836  -10.325 23.923  1.00 54.26  ? 101  ASP C CA  1 
ATOM   10284 C  C   . ASP C  2  83  ? 17.886  -10.169 24.999  1.00 53.70  ? 101  ASP C C   1 
ATOM   10285 O  O   . ASP C  2  83  ? 18.242  -11.138 25.652  1.00 53.12  ? 101  ASP C O   1 
ATOM   10286 C  CB  . ASP C  2  83  ? 17.511  -10.221 22.555  1.00 53.81  ? 101  ASP C CB  1 
ATOM   10287 C  CG  . ASP C  2  83  ? 16.624  -10.691 21.413  1.00 55.24  ? 101  ASP C CG  1 
ATOM   10288 O  OD1 . ASP C  2  83  ? 15.376  -10.710 21.571  1.00 56.37  ? 101  ASP C OD1 1 
ATOM   10289 O  OD2 . ASP C  2  83  ? 17.183  -11.025 20.343  1.00 53.83  ? 101  ASP C OD2 1 
ATOM   10290 N  N   . TYR C  2  84  ? 18.385  -8.946  25.174  1.00 54.13  ? 102  TYR C N   1 
ATOM   10291 C  CA  . TYR C  2  84  ? 19.432  -8.668  26.166  1.00 53.31  ? 102  TYR C CA  1 
ATOM   10292 C  C   . TYR C  2  84  ? 18.885  -8.407  27.566  1.00 53.94  ? 102  TYR C C   1 
ATOM   10293 O  O   . TYR C  2  84  ? 17.810  -7.827  27.725  1.00 54.71  ? 102  TYR C O   1 
ATOM   10294 C  CB  . TYR C  2  84  ? 20.298  -7.498  25.693  1.00 50.30  ? 102  TYR C CB  1 
ATOM   10295 C  CG  . TYR C  2  84  ? 21.087  -7.829  24.448  1.00 50.71  ? 102  TYR C CG  1 
ATOM   10296 C  CD1 . TYR C  2  84  ? 21.098  -6.973  23.351  1.00 50.26  ? 102  TYR C CD1 1 
ATOM   10297 C  CD2 . TYR C  2  84  ? 21.796  -9.027  24.351  1.00 51.31  ? 102  TYR C CD2 1 
ATOM   10298 C  CE1 . TYR C  2  84  ? 21.793  -7.301  22.180  1.00 49.65  ? 102  TYR C CE1 1 
ATOM   10299 C  CE2 . TYR C  2  84  ? 22.497  -9.371  23.190  1.00 51.26  ? 102  TYR C CE2 1 
ATOM   10300 C  CZ  . TYR C  2  84  ? 22.492  -8.502  22.107  1.00 51.16  ? 102  TYR C CZ  1 
ATOM   10301 O  OH  . TYR C  2  84  ? 23.205  -8.841  20.971  1.00 52.56  ? 102  TYR C OH  1 
ATOM   10302 N  N   . SER C  2  85  ? 19.624  -8.839  28.584  1.00 53.59  ? 103  SER C N   1 
ATOM   10303 C  CA  . SER C  2  85  ? 19.182  -8.666  29.957  1.00 53.94  ? 103  SER C CA  1 
ATOM   10304 C  C   . SER C  2  85  ? 19.383  -7.250  30.458  1.00 54.55  ? 103  SER C C   1 
ATOM   10305 O  O   . SER C  2  85  ? 18.707  -6.817  31.384  1.00 54.66  ? 103  SER C O   1 
ATOM   10306 C  CB  . SER C  2  85  ? 19.933  -9.622  30.868  1.00 54.83  ? 103  SER C CB  1 
ATOM   10307 O  OG  . SER C  2  85  ? 21.284  -9.233  30.990  1.00 55.48  ? 103  SER C OG  1 
ATOM   10308 N  N   . PHE C  2  86  ? 20.311  -6.524  29.854  1.00 55.39  ? 104  PHE C N   1 
ATOM   10309 C  CA  . PHE C  2  86  ? 20.567  -5.164  30.296  1.00 56.97  ? 104  PHE C CA  1 
ATOM   10310 C  C   . PHE C  2  86  ? 19.502  -4.143  29.879  1.00 57.02  ? 104  PHE C C   1 
ATOM   10311 O  O   . PHE C  2  86  ? 19.537  -2.996  30.310  1.00 57.76  ? 104  PHE C O   1 
ATOM   10312 C  CB  . PHE C  2  86  ? 21.964  -4.726  29.840  1.00 57.48  ? 104  PHE C CB  1 
ATOM   10313 C  CG  . PHE C  2  86  ? 22.148  -4.714  28.354  1.00 58.05  ? 104  PHE C CG  1 
ATOM   10314 C  CD1 . PHE C  2  86  ? 21.619  -3.691  27.582  1.00 58.58  ? 104  PHE C CD1 1 
ATOM   10315 C  CD2 . PHE C  2  86  ? 22.867  -5.719  27.733  1.00 58.50  ? 104  PHE C CD2 1 
ATOM   10316 C  CE1 . PHE C  2  86  ? 21.807  -3.664  26.208  1.00 59.90  ? 104  PHE C CE1 1 
ATOM   10317 C  CE2 . PHE C  2  86  ? 23.065  -5.709  26.367  1.00 59.48  ? 104  PHE C CE2 1 
ATOM   10318 C  CZ  . PHE C  2  86  ? 22.532  -4.676  25.597  1.00 60.69  ? 104  PHE C CZ  1 
ATOM   10319 N  N   . CYS C  2  87  ? 18.547  -4.557  29.059  1.00 56.51  ? 105  CYS C N   1 
ATOM   10320 C  CA  . CYS C  2  87  ? 17.483  -3.654  28.643  1.00 57.63  ? 105  CYS C CA  1 
ATOM   10321 C  C   . CYS C  2  87  ? 16.635  -3.299  29.856  1.00 57.71  ? 105  CYS C C   1 
ATOM   10322 O  O   . CYS C  2  87  ? 16.099  -2.195  29.963  1.00 57.70  ? 105  CYS C O   1 
ATOM   10323 C  CB  . CYS C  2  87  ? 16.586  -4.321  27.616  1.00 59.14  ? 105  CYS C CB  1 
ATOM   10324 S  SG  . CYS C  2  87  ? 17.420  -4.777  26.065  1.00 63.98  ? 105  CYS C SG  1 
ATOM   10325 N  N   . ARG C  2  88  ? 16.508  -4.260  30.762  1.00 57.36  ? 106  ARG C N   1 
ATOM   10326 C  CA  . ARG C  2  88  ? 15.733  -4.097  31.981  1.00 56.48  ? 106  ARG C CA  1 
ATOM   10327 C  C   . ARG C  2  88  ? 16.378  -3.134  32.972  1.00 56.60  ? 106  ARG C C   1 
ATOM   10328 O  O   . ARG C  2  88  ? 15.740  -2.710  33.925  1.00 58.06  ? 106  ARG C O   1 
ATOM   10329 C  CB  . ARG C  2  88  ? 15.553  -5.459  32.654  1.00 56.24  ? 106  ARG C CB  1 
ATOM   10330 C  CG  . ARG C  2  88  ? 14.470  -6.328  32.072  1.00 56.19  ? 106  ARG C CG  1 
ATOM   10331 C  CD  . ARG C  2  88  ? 14.666  -7.787  32.461  1.00 56.97  ? 106  ARG C CD  1 
ATOM   10332 N  NE  . ARG C  2  88  ? 14.975  -7.959  33.876  1.00 58.46  ? 106  ARG C NE  1 
ATOM   10333 C  CZ  . ARG C  2  88  ? 16.110  -8.498  34.323  1.00 60.97  ? 106  ARG C CZ  1 
ATOM   10334 N  NH1 . ARG C  2  88  ? 17.027  -8.916  33.451  1.00 60.96  ? 106  ARG C NH1 1 
ATOM   10335 N  NH2 . ARG C  2  88  ? 16.342  -8.607  35.634  1.00 59.30  ? 106  ARG C NH2 1 
ATOM   10336 N  N   . ALA C  2  89  ? 17.639  -2.789  32.753  1.00 56.67  ? 107  ALA C N   1 
ATOM   10337 C  CA  . ALA C  2  89  ? 18.360  -1.889  33.660  1.00 56.54  ? 107  ALA C CA  1 
ATOM   10338 C  C   . ALA C  2  89  ? 17.706  -0.527  33.918  1.00 56.46  ? 107  ALA C C   1 
ATOM   10339 O  O   . ALA C  2  89  ? 17.209  0.126   32.997  1.00 56.95  ? 107  ALA C O   1 
ATOM   10340 C  CB  . ALA C  2  89  ? 19.777  -1.682  33.154  1.00 55.94  ? 107  ALA C CB  1 
ATOM   10341 N  N   . LEU C  2  90  ? 17.732  -0.102  35.181  1.00 56.65  ? 108  LEU C N   1 
ATOM   10342 C  CA  . LEU C  2  90  ? 17.164  1.181   35.602  1.00 57.21  ? 108  LEU C CA  1 
ATOM   10343 C  C   . LEU C  2  90  ? 18.208  2.290   35.758  1.00 58.16  ? 108  LEU C C   1 
ATOM   10344 O  O   . LEU C  2  90  ? 19.413  2.035   35.731  1.00 56.45  ? 108  LEU C O   1 
ATOM   10345 C  CB  . LEU C  2  90  ? 16.433  1.015   36.925  1.00 56.37  ? 108  LEU C CB  1 
ATOM   10346 C  CG  . LEU C  2  90  ? 15.255  0.054   36.896  1.00 54.72  ? 108  LEU C CG  1 
ATOM   10347 C  CD1 . LEU C  2  90  ? 14.673  -0.091  38.295  1.00 54.18  ? 108  LEU C CD1 1 
ATOM   10348 C  CD2 . LEU C  2  90  ? 14.217  0.587   35.931  1.00 54.85  ? 108  LEU C CD2 1 
ATOM   10349 N  N   . LYS C  2  91  ? 17.724  3.511   35.971  1.00 60.26  ? 109  LYS C N   1 
ATOM   10350 C  CA  . LYS C  2  91  ? 18.580  4.689   36.098  1.00 62.82  ? 109  LYS C CA  1 
ATOM   10351 C  C   . LYS C  2  91  ? 19.898  4.550   36.869  1.00 64.75  ? 109  LYS C C   1 
ATOM   10352 O  O   . LYS C  2  91  ? 20.940  4.943   36.357  1.00 66.87  ? 109  LYS C O   1 
ATOM   10353 C  CB  . LYS C  2  91  ? 17.795  5.867   36.681  1.00 61.41  ? 109  LYS C CB  1 
ATOM   10354 C  CG  . LYS C  2  91  ? 18.573  7.174   36.639  1.00 59.38  ? 109  LYS C CG  1 
ATOM   10355 C  CD  . LYS C  2  91  ? 18.045  8.179   37.647  1.00 58.86  ? 109  LYS C CD  1 
ATOM   10356 C  CE  . LYS C  2  91  ? 17.165  9.224   37.015  1.00 56.96  ? 109  LYS C CE  1 
ATOM   10357 N  NZ  . LYS C  2  91  ? 17.968  10.058  36.098  1.00 58.32  ? 109  LYS C NZ  1 
ATOM   10358 N  N   . GLY C  2  92  ? 19.888  4.016   38.084  1.00 65.35  ? 110  GLY C N   1 
ATOM   10359 C  CA  . GLY C  2  92  ? 21.157  3.918   38.791  1.00 65.82  ? 110  GLY C CA  1 
ATOM   10360 C  C   . GLY C  2  92  ? 21.708  2.519   38.987  1.00 66.60  ? 110  GLY C C   1 
ATOM   10361 O  O   . GLY C  2  92  ? 22.575  2.309   39.840  1.00 66.43  ? 110  GLY C O   1 
ATOM   10362 N  N   . GLU C  2  93  ? 21.226  1.573   38.183  1.00 66.54  ? 111  GLU C N   1 
ATOM   10363 C  CA  . GLU C  2  93  ? 21.628  0.174   38.285  1.00 66.57  ? 111  GLU C CA  1 
ATOM   10364 C  C   . GLU C  2  93  ? 22.976  -0.155  37.646  1.00 66.26  ? 111  GLU C C   1 
ATOM   10365 O  O   . GLU C  2  93  ? 23.298  0.312   36.558  1.00 66.37  ? 111  GLU C O   1 
ATOM   10366 C  CB  . GLU C  2  93  ? 20.526  -0.699  37.666  1.00 67.51  ? 111  GLU C CB  1 
ATOM   10367 C  CG  . GLU C  2  93  ? 20.560  -2.190  38.011  1.00 67.42  ? 111  GLU C CG  1 
ATOM   10368 C  CD  . GLU C  2  93  ? 19.337  -2.932  37.480  1.00 67.77  ? 111  GLU C CD  1 
ATOM   10369 O  OE1 . GLU C  2  93  ? 19.236  -4.149  37.704  1.00 68.41  ? 111  GLU C OE1 1 
ATOM   10370 O  OE2 . GLU C  2  93  ? 18.466  -2.305  36.837  1.00 66.70  ? 111  GLU C OE2 1 
ATOM   10371 N  N   . THR C  2  94  ? 23.757  -0.978  38.333  1.00 66.73  ? 112  THR C N   1 
ATOM   10372 C  CA  . THR C  2  94  ? 25.055  -1.399  37.827  1.00 67.11  ? 112  THR C CA  1 
ATOM   10373 C  C   . THR C  2  94  ? 24.857  -2.400  36.704  1.00 68.39  ? 112  THR C C   1 
ATOM   10374 O  O   . THR C  2  94  ? 24.161  -3.412  36.872  1.00 69.69  ? 112  THR C O   1 
ATOM   10375 C  CB  . THR C  2  94  ? 25.886  -2.084  38.910  1.00 67.14  ? 112  THR C CB  1 
ATOM   10376 O  OG1 . THR C  2  94  ? 26.093  -1.175  40.004  1.00 68.08  ? 112  THR C OG1 1 
ATOM   10377 C  CG2 . THR C  2  94  ? 27.216  -2.532  38.345  1.00 63.90  ? 112  THR C CG2 1 
ATOM   10378 N  N   . VAL C  2  95  ? 25.479  -2.109  35.565  1.00 68.47  ? 113  VAL C N   1 
ATOM   10379 C  CA  . VAL C  2  95  ? 25.398  -2.959  34.384  1.00 67.92  ? 113  VAL C CA  1 
ATOM   10380 C  C   . VAL C  2  95  ? 26.767  -3.577  34.077  1.00 69.04  ? 113  VAL C C   1 
ATOM   10381 O  O   . VAL C  2  95  ? 27.613  -2.919  33.486  1.00 70.01  ? 113  VAL C O   1 
ATOM   10382 C  CB  . VAL C  2  95  ? 24.953  -2.134  33.178  1.00 66.26  ? 113  VAL C CB  1 
ATOM   10383 C  CG1 . VAL C  2  95  ? 24.650  -3.038  32.007  1.00 65.62  ? 113  VAL C CG1 1 
ATOM   10384 C  CG2 . VAL C  2  95  ? 23.752  -1.303  33.552  1.00 65.71  ? 113  VAL C CG2 1 
ATOM   10385 N  N   . ASN C  2  96  ? 26.992  -4.821  34.498  1.00 69.84  ? 114  ASN C N   1 
ATOM   10386 C  CA  . ASN C  2  96  ? 28.256  -5.528  34.245  1.00 70.68  ? 114  ASN C CA  1 
ATOM   10387 C  C   . ASN C  2  96  ? 27.865  -6.718  33.383  1.00 69.29  ? 114  ASN C C   1 
ATOM   10388 O  O   . ASN C  2  96  ? 27.478  -7.765  33.899  1.00 68.71  ? 114  ASN C O   1 
ATOM   10389 C  CB  . ASN C  2  96  ? 28.863  -6.032  35.559  1.00 75.59  ? 114  ASN C CB  1 
ATOM   10390 C  CG  . ASN C  2  96  ? 30.235  -6.664  35.381  1.00 79.97  ? 114  ASN C CG  1 
ATOM   10391 O  OD1 . ASN C  2  96  ? 30.590  -7.110  34.290  1.00 80.17  ? 114  ASN C OD1 1 
ATOM   10392 N  ND2 . ASN C  2  96  ? 30.996  -6.701  36.473  1.00 85.22  ? 114  ASN C ND2 1 
ATOM   10393 N  N   . THR C  2  97  ? 27.972  -6.559  32.070  1.00 68.13  ? 115  THR C N   1 
ATOM   10394 C  CA  . THR C  2  97  ? 27.566  -7.616  31.152  1.00 66.43  ? 115  THR C CA  1 
ATOM   10395 C  C   . THR C  2  97  ? 28.587  -7.957  30.069  1.00 64.59  ? 115  THR C C   1 
ATOM   10396 O  O   . THR C  2  97  ? 29.544  -7.219  29.846  1.00 63.63  ? 115  THR C O   1 
ATOM   10397 C  CB  . THR C  2  97  ? 26.230  -7.232  30.466  1.00 66.40  ? 115  THR C CB  1 
ATOM   10398 O  OG1 . THR C  2  97  ? 25.745  -8.341  29.704  1.00 68.26  ? 115  THR C OG1 1 
ATOM   10399 C  CG2 . THR C  2  97  ? 26.433  -6.049  29.533  1.00 64.60  ? 115  THR C CG2 1 
ATOM   10400 N  N   . THR C  2  98  ? 28.366  -9.095  29.413  1.00 63.04  ? 116  THR C N   1 
ATOM   10401 C  CA  . THR C  2  98  ? 29.216  -9.570  28.328  1.00 61.07  ? 116  THR C CA  1 
ATOM   10402 C  C   . THR C  2  98  ? 28.328  -9.914  27.149  1.00 60.30  ? 116  THR C C   1 
ATOM   10403 O  O   . THR C  2  98  ? 27.531  -10.847 27.219  1.00 61.34  ? 116  THR C O   1 
ATOM   10404 C  CB  . THR C  2  98  ? 29.998  -10.837 28.708  1.00 59.85  ? 116  THR C CB  1 
ATOM   10405 O  OG1 . THR C  2  98  ? 30.905  -10.541 29.774  1.00 59.97  ? 116  THR C OG1 1 
ATOM   10406 C  CG2 . THR C  2  98  ? 30.786  -11.343 27.513  1.00 59.15  ? 116  THR C CG2 1 
ATOM   10407 N  N   . ILE C  2  99  ? 28.475  -9.155  26.072  1.00 58.18  ? 117  ILE C N   1 
ATOM   10408 C  CA  . ILE C  2  99  ? 27.698  -9.350  24.855  1.00 56.81  ? 117  ILE C CA  1 
ATOM   10409 C  C   . ILE C  2  99  ? 28.565  -10.028 23.787  1.00 58.55  ? 117  ILE C C   1 
ATOM   10410 O  O   . ILE C  2  99  ? 29.715  -9.634  23.575  1.00 60.02  ? 117  ILE C O   1 
ATOM   10411 C  CB  . ILE C  2  99  ? 27.242  -7.994  24.344  1.00 54.22  ? 117  ILE C CB  1 
ATOM   10412 C  CG1 . ILE C  2  99  ? 26.451  -7.301  25.448  1.00 54.22  ? 117  ILE C CG1 1 
ATOM   10413 C  CG2 . ILE C  2  99  ? 26.447  -8.144  23.068  1.00 52.52  ? 117  ILE C CG2 1 
ATOM   10414 C  CD1 . ILE C  2  99  ? 26.421  -5.803  25.340  1.00 54.99  ? 117  ILE C CD1 1 
ATOM   10415 N  N   . SER C  2  100 ? 28.041  -11.049 23.120  1.00 58.40  ? 118  SER C N   1 
ATOM   10416 C  CA  . SER C  2  100 ? 28.831  -11.714 22.085  1.00 57.67  ? 118  SER C CA  1 
ATOM   10417 C  C   . SER C  2  100 ? 28.540  -11.101 20.726  1.00 56.85  ? 118  SER C C   1 
ATOM   10418 O  O   . SER C  2  100 ? 27.430  -10.643 20.473  1.00 57.26  ? 118  SER C O   1 
ATOM   10419 C  CB  . SER C  2  100 ? 28.529  -13.218 22.052  1.00 57.73  ? 118  SER C CB  1 
ATOM   10420 O  OG  . SER C  2  100 ? 27.143  -13.480 22.184  1.00 57.79  ? 118  SER C OG  1 
ATOM   10421 N  N   . PHE C  2  101 ? 29.540  -11.082 19.852  1.00 56.49  ? 119  PHE C N   1 
ATOM   10422 C  CA  . PHE C  2  101 ? 29.352  -10.533 18.512  1.00 57.58  ? 119  PHE C CA  1 
ATOM   10423 C  C   . PHE C  2  101 ? 30.046  -11.394 17.459  1.00 58.27  ? 119  PHE C C   1 
ATOM   10424 O  O   . PHE C  2  101 ? 30.823  -12.293 17.791  1.00 57.80  ? 119  PHE C O   1 
ATOM   10425 C  CB  . PHE C  2  101 ? 29.859  -9.083  18.447  1.00 56.52  ? 119  PHE C CB  1 
ATOM   10426 C  CG  . PHE C  2  101 ? 31.345  -8.938  18.631  1.00 55.60  ? 119  PHE C CG  1 
ATOM   10427 C  CD1 . PHE C  2  101 ? 32.210  -9.083  17.557  1.00 55.06  ? 119  PHE C CD1 1 
ATOM   10428 C  CD2 . PHE C  2  101 ? 31.877  -8.661  19.882  1.00 55.71  ? 119  PHE C CD2 1 
ATOM   10429 C  CE1 . PHE C  2  101 ? 33.574  -8.960  17.727  1.00 54.22  ? 119  PHE C CE1 1 
ATOM   10430 C  CE2 . PHE C  2  101 ? 33.239  -8.535  20.065  1.00 54.64  ? 119  PHE C CE2 1 
ATOM   10431 C  CZ  . PHE C  2  101 ? 34.092  -8.684  18.984  1.00 55.51  ? 119  PHE C CZ  1 
ATOM   10432 N  N   . SER C  2  102 ? 29.746  -11.120 16.191  1.00 58.69  ? 120  SER C N   1 
ATOM   10433 C  CA  . SER C  2  102 ? 30.323  -11.863 15.072  1.00 59.51  ? 120  SER C CA  1 
ATOM   10434 C  C   . SER C  2  102 ? 29.947  -11.191 13.757  1.00 60.31  ? 120  SER C C   1 
ATOM   10435 O  O   . SER C  2  102 ? 28.886  -10.592 13.661  1.00 61.01  ? 120  SER C O   1 
ATOM   10436 C  CB  . SER C  2  102 ? 29.798  -13.299 15.084  1.00 59.17  ? 120  SER C CB  1 
ATOM   10437 O  OG  . SER C  2  102 ? 29.862  -13.886 13.794  1.00 61.03  ? 120  SER C OG  1 
ATOM   10438 N  N   . PHE C  2  103 ? 30.821  -11.256 12.755  1.00 61.01  ? 121  PHE C N   1 
ATOM   10439 C  CA  . PHE C  2  103 ? 30.516  -10.665 11.452  1.00 63.47  ? 121  PHE C CA  1 
ATOM   10440 C  C   . PHE C  2  103 ? 31.526  -11.077 10.405  1.00 65.49  ? 121  PHE C C   1 
ATOM   10441 O  O   . PHE C  2  103 ? 32.599  -11.573 10.743  1.00 65.73  ? 121  PHE C O   1 
ATOM   10442 C  CB  . PHE C  2  103 ? 30.435  -9.132  11.531  1.00 62.46  ? 121  PHE C CB  1 
ATOM   10443 C  CG  . PHE C  2  103 ? 31.744  -8.455  11.833  1.00 62.63  ? 121  PHE C CG  1 
ATOM   10444 C  CD1 . PHE C  2  103 ? 32.635  -8.137  10.817  1.00 60.96  ? 121  PHE C CD1 1 
ATOM   10445 C  CD2 . PHE C  2  103 ? 32.084  -8.128  13.144  1.00 63.10  ? 121  PHE C CD2 1 
ATOM   10446 C  CE1 . PHE C  2  103 ? 33.846  -7.507  11.102  1.00 61.17  ? 121  PHE C CE1 1 
ATOM   10447 C  CE2 . PHE C  2  103 ? 33.299  -7.496  13.439  1.00 62.25  ? 121  PHE C CE2 1 
ATOM   10448 C  CZ  . PHE C  2  103 ? 34.181  -7.183  12.419  1.00 61.15  ? 121  PHE C CZ  1 
ATOM   10449 N  N   . LYS C  2  104 ? 31.166  -10.891 9.136   1.00 68.04  ? 122  LYS C N   1 
ATOM   10450 C  CA  . LYS C  2  104 ? 32.034  -11.241 8.015   1.00 70.46  ? 122  LYS C CA  1 
ATOM   10451 C  C   . LYS C  2  104 ? 31.356  -10.853 6.713   1.00 71.62  ? 122  LYS C C   1 
ATOM   10452 O  O   . LYS C  2  104 ? 30.180  -10.499 6.712   1.00 73.62  ? 122  LYS C O   1 
ATOM   10453 C  CB  . LYS C  2  104 ? 32.305  -12.749 7.995   1.00 71.25  ? 122  LYS C CB  1 
ATOM   10454 C  CG  . LYS C  2  104 ? 31.070  -13.608 7.695   1.00 72.53  ? 122  LYS C CG  1 
ATOM   10455 C  CD  . LYS C  2  104 ? 31.409  -15.120 7.620   1.00 74.84  ? 122  LYS C CD  1 
ATOM   10456 C  CE  . LYS C  2  104 ? 32.105  -15.516 6.312   1.00 76.51  ? 122  LYS C CE  1 
ATOM   10457 N  NZ  . LYS C  2  104 ? 32.434  -16.973 6.237   1.00 75.49  ? 122  LYS C NZ  1 
ATOM   10458 N  N   . GLY C  2  105 ? 32.094  -10.907 5.608   1.00 71.86  ? 123  GLY C N   1 
ATOM   10459 C  CA  . GLY C  2  105 ? 31.489  -10.602 4.325   1.00 72.05  ? 123  GLY C CA  1 
ATOM   10460 C  C   . GLY C  2  105 ? 31.716  -9.262  3.645   1.00 72.81  ? 123  GLY C C   1 
ATOM   10461 O  O   . GLY C  2  105 ? 31.316  -9.110  2.494   1.00 73.60  ? 123  GLY C O   1 
ATOM   10462 N  N   . ILE C  2  106 ? 32.331  -8.284  4.308   1.00 72.78  ? 124  ILE C N   1 
ATOM   10463 C  CA  . ILE C  2  106 ? 32.563  -7.006  3.639   1.00 70.78  ? 124  ILE C CA  1 
ATOM   10464 C  C   . ILE C  2  106 ? 34.006  -6.529  3.617   1.00 70.09  ? 124  ILE C C   1 
ATOM   10465 O  O   . ILE C  2  106 ? 34.725  -6.613  4.609   1.00 68.22  ? 124  ILE C O   1 
ATOM   10466 C  CB  . ILE C  2  106 ? 31.658  -5.892  4.217   1.00 70.75  ? 124  ILE C CB  1 
ATOM   10467 C  CG1 . ILE C  2  106 ? 30.207  -6.163  3.810   1.00 71.93  ? 124  ILE C CG1 1 
ATOM   10468 C  CG2 . ILE C  2  106 ? 32.080  -4.525  3.686   1.00 69.18  ? 124  ILE C CG2 1 
ATOM   10469 C  CD1 . ILE C  2  106 ? 29.196  -5.094  4.242   1.00 73.27  ? 124  ILE C CD1 1 
ATOM   10470 N  N   . LYS C  2  107 ? 34.417  -6.050  2.447   1.00 69.67  ? 125  LYS C N   1 
ATOM   10471 C  CA  . LYS C  2  107 ? 35.757  -5.527  2.218   1.00 69.81  ? 125  LYS C CA  1 
ATOM   10472 C  C   . LYS C  2  107 ? 35.693  -4.022  2.431   1.00 71.13  ? 125  LYS C C   1 
ATOM   10473 O  O   . LYS C  2  107 ? 34.802  -3.355  1.896   1.00 71.03  ? 125  LYS C O   1 
ATOM   10474 C  CB  . LYS C  2  107 ? 36.184  -5.806  0.778   1.00 68.75  ? 125  LYS C CB  1 
ATOM   10475 C  CG  . LYS C  2  107 ? 37.525  -5.212  0.357   1.00 68.57  ? 125  LYS C CG  1 
ATOM   10476 C  CD  . LYS C  2  107 ? 37.452  -4.726  -1.101  1.00 68.56  ? 125  LYS C CD  1 
ATOM   10477 C  CE  . LYS C  2  107 ? 38.826  -4.436  -1.723  1.00 67.68  ? 125  LYS C CE  1 
ATOM   10478 N  NZ  . LYS C  2  107 ? 39.622  -5.667  -2.013  1.00 66.17  ? 125  LYS C NZ  1 
ATOM   10479 N  N   . PHE C  2  108 ? 36.627  -3.494  3.223   1.00 71.82  ? 126  PHE C N   1 
ATOM   10480 C  CA  . PHE C  2  108 ? 36.682  -2.059  3.494   1.00 71.22  ? 126  PHE C CA  1 
ATOM   10481 C  C   . PHE C  2  108 ? 37.921  -1.425  2.873   1.00 71.26  ? 126  PHE C C   1 
ATOM   10482 O  O   . PHE C  2  108 ? 38.954  -2.078  2.734   1.00 71.38  ? 126  PHE C O   1 
ATOM   10483 C  CB  . PHE C  2  108 ? 36.721  -1.796  4.996   1.00 70.00  ? 126  PHE C CB  1 
ATOM   10484 C  CG  . PHE C  2  108 ? 35.641  -2.472  5.759   1.00 68.41  ? 126  PHE C CG  1 
ATOM   10485 C  CD1 . PHE C  2  108 ? 35.751  -3.811  6.096   1.00 68.14  ? 126  PHE C CD1 1 
ATOM   10486 C  CD2 . PHE C  2  108 ? 34.500  -1.773  6.127   1.00 68.61  ? 126  PHE C CD2 1 
ATOM   10487 C  CE1 . PHE C  2  108 ? 34.737  -4.452  6.800   1.00 68.38  ? 126  PHE C CE1 1 
ATOM   10488 C  CE2 . PHE C  2  108 ? 33.478  -2.397  6.829   1.00 68.95  ? 126  PHE C CE2 1 
ATOM   10489 C  CZ  . PHE C  2  108 ? 33.595  -3.744  7.166   1.00 68.43  ? 126  PHE C CZ  1 
ATOM   10490 N  N   . SER C  2  109 ? 37.821  -0.150  2.511   1.00 71.78  ? 127  SER C N   1 
ATOM   10491 C  CA  . SER C  2  109 ? 38.968  0.551   1.944   1.00 72.19  ? 127  SER C CA  1 
ATOM   10492 C  C   . SER C  2  109 ? 39.999  0.661   3.066   1.00 72.62  ? 127  SER C C   1 
ATOM   10493 O  O   . SER C  2  109 ? 39.736  0.297   4.213   1.00 72.27  ? 127  SER C O   1 
ATOM   10494 C  CB  . SER C  2  109 ? 38.594  1.975   1.490   1.00 71.56  ? 127  SER C CB  1 
ATOM   10495 O  OG  . SER C  2  109 ? 37.442  2.005   0.663   1.00 70.50  ? 127  SER C OG  1 
ATOM   10496 N  N   . LYS C  2  110 ? 41.177  1.163   2.718   1.00 73.13  ? 128  LYS C N   1 
ATOM   10497 C  CA  . LYS C  2  110 ? 42.249  1.371   3.679   1.00 72.41  ? 128  LYS C CA  1 
ATOM   10498 C  C   . LYS C  2  110 ? 42.044  2.812   4.142   1.00 71.45  ? 128  LYS C C   1 
ATOM   10499 O  O   . LYS C  2  110 ? 41.571  3.657   3.377   1.00 70.52  ? 128  LYS C O   1 
ATOM   10500 C  CB  . LYS C  2  110 ? 43.589  1.220   2.977   1.00 73.89  ? 128  LYS C CB  1 
ATOM   10501 C  CG  . LYS C  2  110 ? 44.795  1.585   3.803   1.00 78.82  ? 128  LYS C CG  1 
ATOM   10502 C  CD  . LYS C  2  110 ? 46.054  1.572   2.919   1.00 82.45  ? 128  LYS C CD  1 
ATOM   10503 C  CE  . LYS C  2  110 ? 47.329  1.952   3.685   1.00 82.97  ? 128  LYS C CE  1 
ATOM   10504 N  NZ  . LYS C  2  110 ? 48.534  1.952   2.798   1.00 82.64  ? 128  LYS C NZ  1 
ATOM   10505 N  N   . GLY C  2  111 ? 42.353  3.108   5.393   1.00 70.05  ? 129  GLY C N   1 
ATOM   10506 C  CA  . GLY C  2  111 ? 42.152  4.475   5.816   1.00 69.93  ? 129  GLY C CA  1 
ATOM   10507 C  C   . GLY C  2  111 ? 41.681  4.682   7.236   1.00 70.69  ? 129  GLY C C   1 
ATOM   10508 O  O   . GLY C  2  111 ? 41.827  3.809   8.095   1.00 69.76  ? 129  GLY C O   1 
ATOM   10509 N  N   . LYS C  2  112 ? 41.115  5.863   7.471   1.00 71.83  ? 130  LYS C N   1 
ATOM   10510 C  CA  . LYS C  2  112 ? 40.617  6.252   8.784   1.00 73.35  ? 130  LYS C CA  1 
ATOM   10511 C  C   . LYS C  2  112 ? 39.093  6.275   8.825   1.00 72.76  ? 130  LYS C C   1 
ATOM   10512 O  O   . LYS C  2  112 ? 38.453  6.985   8.042   1.00 72.37  ? 130  LYS C O   1 
ATOM   10513 C  CB  . LYS C  2  112 ? 41.174  7.639   9.173   1.00 74.10  ? 130  LYS C CB  1 
ATOM   10514 C  CG  . LYS C  2  112 ? 40.591  8.242   10.456  1.00 75.13  ? 130  LYS C CG  1 
ATOM   10515 C  CD  . LYS C  2  112 ? 41.410  9.428   10.966  1.00 78.75  ? 130  LYS C CD  1 
ATOM   10516 C  CE  . LYS C  2  112 ? 42.732  8.964   11.619  1.00 81.43  ? 130  LYS C CE  1 
ATOM   10517 N  NZ  . LYS C  2  112 ? 43.591  10.071  12.179  1.00 81.78  ? 130  LYS C NZ  1 
ATOM   10518 N  N   . TYR C  2  113 ? 38.525  5.478   9.731   1.00 71.56  ? 131  TYR C N   1 
ATOM   10519 C  CA  . TYR C  2  113 ? 37.084  5.416   9.911   1.00 69.85  ? 131  TYR C CA  1 
ATOM   10520 C  C   . TYR C  2  113 ? 36.720  6.042   11.237  1.00 70.64  ? 131  TYR C C   1 
ATOM   10521 O  O   . TYR C  2  113 ? 37.393  5.810   12.251  1.00 70.19  ? 131  TYR C O   1 
ATOM   10522 C  CB  . TYR C  2  113 ? 36.590  3.969   9.906   1.00 67.56  ? 131  TYR C CB  1 
ATOM   10523 C  CG  . TYR C  2  113 ? 36.662  3.291   8.562   1.00 65.79  ? 131  TYR C CG  1 
ATOM   10524 C  CD1 . TYR C  2  113 ? 37.771  2.527   8.202   1.00 63.96  ? 131  TYR C CD1 1 
ATOM   10525 C  CD2 . TYR C  2  113 ? 35.631  3.441   7.631   1.00 64.70  ? 131  TYR C CD2 1 
ATOM   10526 C  CE1 . TYR C  2  113 ? 37.856  1.935   6.955   1.00 62.20  ? 131  TYR C CE1 1 
ATOM   10527 C  CE2 . TYR C  2  113 ? 35.707  2.854   6.382   1.00 62.09  ? 131  TYR C CE2 1 
ATOM   10528 C  CZ  . TYR C  2  113 ? 36.823  2.106   6.049   1.00 62.25  ? 131  TYR C CZ  1 
ATOM   10529 O  OH  . TYR C  2  113 ? 36.928  1.554   4.795   1.00 61.08  ? 131  TYR C OH  1 
ATOM   10530 N  N   . LYS C  2  114 ? 35.670  6.856   11.230  1.00 71.28  ? 132  LYS C N   1 
ATOM   10531 C  CA  . LYS C  2  114 ? 35.204  7.464   12.461  1.00 73.01  ? 132  LYS C CA  1 
ATOM   10532 C  C   . LYS C  2  114 ? 33.692  7.205   12.533  1.00 72.55  ? 132  LYS C C   1 
ATOM   10533 O  O   . LYS C  2  114 ? 32.953  7.408   11.568  1.00 72.49  ? 132  LYS C O   1 
ATOM   10534 C  CB  . LYS C  2  114 ? 35.576  8.967   12.509  1.00 76.02  ? 132  LYS C CB  1 
ATOM   10535 C  CG  . LYS C  2  114 ? 34.596  9.975   11.894  1.00 80.78  ? 132  LYS C CG  1 
ATOM   10536 C  CD  . LYS C  2  114 ? 33.518  10.398  12.904  1.00 83.56  ? 132  LYS C CD  1 
ATOM   10537 C  CE  . LYS C  2  114 ? 32.596  11.489  12.349  1.00 85.39  ? 132  LYS C CE  1 
ATOM   10538 N  NZ  . LYS C  2  114 ? 33.299  12.799  12.222  1.00 86.80  ? 132  LYS C NZ  1 
ATOM   10539 N  N   . CYS C  2  115 ? 33.243  6.700   13.674  1.00 71.95  ? 133  CYS C N   1 
ATOM   10540 C  CA  . CYS C  2  115 ? 31.836  6.384   13.858  1.00 70.83  ? 133  CYS C CA  1 
ATOM   10541 C  C   . CYS C  2  115 ? 31.266  7.006   15.119  1.00 68.59  ? 133  CYS C C   1 
ATOM   10542 O  O   . CYS C  2  115 ? 31.641  6.623   16.227  1.00 68.56  ? 133  CYS C O   1 
ATOM   10543 C  CB  . CYS C  2  115 ? 31.650  4.862   13.912  1.00 72.33  ? 133  CYS C CB  1 
ATOM   10544 S  SG  . CYS C  2  115 ? 29.946  4.305   14.195  1.00 75.69  ? 133  CYS C SG  1 
ATOM   10545 N  N   . VAL C  2  116 ? 30.370  7.972   14.949  1.00 65.85  ? 134  VAL C N   1 
ATOM   10546 C  CA  . VAL C  2  116 ? 29.736  8.608   16.091  1.00 64.33  ? 134  VAL C CA  1 
ATOM   10547 C  C   . VAL C  2  116 ? 28.576  7.711   16.463  1.00 64.84  ? 134  VAL C C   1 
ATOM   10548 O  O   . VAL C  2  116 ? 27.712  7.423   15.630  1.00 65.77  ? 134  VAL C O   1 
ATOM   10549 C  CB  . VAL C  2  116 ? 29.200  10.003  15.746  1.00 62.60  ? 134  VAL C CB  1 
ATOM   10550 C  CG1 . VAL C  2  116 ? 28.315  10.516  16.866  1.00 60.23  ? 134  VAL C CG1 1 
ATOM   10551 C  CG2 . VAL C  2  116 ? 30.355  10.942  15.521  1.00 62.88  ? 134  VAL C CG2 1 
ATOM   10552 N  N   . VAL C  2  117 ? 28.578  7.248   17.706  1.00 63.90  ? 135  VAL C N   1 
ATOM   10553 C  CA  . VAL C  2  117 ? 27.538  6.371   18.200  1.00 63.38  ? 135  VAL C CA  1 
ATOM   10554 C  C   . VAL C  2  117 ? 26.782  7.071   19.324  1.00 63.90  ? 135  VAL C C   1 
ATOM   10555 O  O   . VAL C  2  117 ? 27.197  7.097   20.478  1.00 63.84  ? 135  VAL C O   1 
ATOM   10556 C  CB  . VAL C  2  117 ? 28.150  5.026   18.668  1.00 63.56  ? 135  VAL C CB  1 
ATOM   10557 C  CG1 . VAL C  2  117 ? 29.412  5.282   19.457  1.00 64.38  ? 135  VAL C CG1 1 
ATOM   10558 C  CG2 . VAL C  2  117 ? 27.154  4.245   19.502  1.00 64.83  ? 135  VAL C CG2 1 
ATOM   10559 N  N   . GLU C  2  118 ? 25.673  7.678   18.946  1.00 64.82  ? 136  GLU C N   1 
ATOM   10560 C  CA  . GLU C  2  118 ? 24.813  8.392   19.866  1.00 65.97  ? 136  GLU C CA  1 
ATOM   10561 C  C   . GLU C  2  118 ? 23.802  7.376   20.372  1.00 66.33  ? 136  GLU C C   1 
ATOM   10562 O  O   . GLU C  2  118 ? 23.025  6.832   19.596  1.00 65.78  ? 136  GLU C O   1 
ATOM   10563 C  CB  . GLU C  2  118 ? 24.124  9.534   19.106  1.00 67.45  ? 136  GLU C CB  1 
ATOM   10564 C  CG  . GLU C  2  118 ? 22.795  10.033  19.669  1.00 70.40  ? 136  GLU C CG  1 
ATOM   10565 C  CD  . GLU C  2  118 ? 22.165  11.124  18.797  1.00 72.13  ? 136  GLU C CD  1 
ATOM   10566 O  OE1 . GLU C  2  118 ? 22.098  10.947  17.558  1.00 72.71  ? 136  GLU C OE1 1 
ATOM   10567 O  OE2 . GLU C  2  118 ? 21.728  12.156  19.350  1.00 73.49  ? 136  GLU C OE2 1 
ATOM   10568 N  N   . ALA C  2  119 ? 23.834  7.104   21.671  1.00 66.87  ? 137  ALA C N   1 
ATOM   10569 C  CA  . ALA C  2  119 ? 22.913  6.151   22.279  1.00 66.79  ? 137  ALA C CA  1 
ATOM   10570 C  C   . ALA C  2  119 ? 21.670  6.880   22.789  1.00 67.06  ? 137  ALA C C   1 
ATOM   10571 O  O   . ALA C  2  119 ? 21.763  7.998   23.283  1.00 67.53  ? 137  ALA C O   1 
ATOM   10572 C  CB  . ALA C  2  119 ? 23.605  5.422   23.415  1.00 66.13  ? 137  ALA C CB  1 
ATOM   10573 N  N   . ILE C  2  120 ? 20.508  6.248   22.662  1.00 67.03  ? 138  ILE C N   1 
ATOM   10574 C  CA  . ILE C  2  120 ? 19.254  6.856   23.098  1.00 67.52  ? 138  ILE C CA  1 
ATOM   10575 C  C   . ILE C  2  120 ? 18.328  5.821   23.749  1.00 69.78  ? 138  ILE C C   1 
ATOM   10576 O  O   . ILE C  2  120 ? 18.206  4.699   23.266  1.00 70.57  ? 138  ILE C O   1 
ATOM   10577 C  CB  . ILE C  2  120 ? 18.534  7.496   21.904  1.00 65.62  ? 138  ILE C CB  1 
ATOM   10578 C  CG1 . ILE C  2  120 ? 19.448  8.533   21.258  1.00 65.02  ? 138  ILE C CG1 1 
ATOM   10579 C  CG2 . ILE C  2  120 ? 17.231  8.126   22.352  1.00 64.55  ? 138  ILE C CG2 1 
ATOM   10580 C  CD1 . ILE C  2  120 ? 18.916  9.077   19.962  1.00 65.88  ? 138  ILE C CD1 1 
ATOM   10581 N  N   . SER C  2  121 ? 17.675  6.204   24.844  1.00 72.06  ? 139  SER C N   1 
ATOM   10582 C  CA  . SER C  2  121 ? 16.773  5.306   25.553  1.00 73.52  ? 139  SER C CA  1 
ATOM   10583 C  C   . SER C  2  121 ? 15.838  6.048   26.495  1.00 75.64  ? 139  SER C C   1 
ATOM   10584 O  O   . SER C  2  121 ? 15.926  7.256   26.660  1.00 75.81  ? 139  SER C O   1 
ATOM   10585 C  CB  . SER C  2  121 ? 17.571  4.304   26.367  1.00 73.10  ? 139  SER C CB  1 
ATOM   10586 O  OG  . SER C  2  121 ? 18.222  4.965   27.431  1.00 73.99  ? 139  SER C OG  1 
ATOM   10587 N  N   . GLY C  2  122 ? 14.949  5.298   27.130  1.00 78.69  ? 140  GLY C N   1 
ATOM   10588 C  CA  . GLY C  2  122 ? 14.001  5.890   28.051  1.00 82.52  ? 140  GLY C CA  1 
ATOM   10589 C  C   . GLY C  2  122 ? 12.630  5.999   27.417  1.00 85.87  ? 140  GLY C C   1 
ATOM   10590 O  O   . GLY C  2  122 ? 12.507  5.943   26.191  1.00 85.63  ? 140  GLY C O   1 
ATOM   10591 N  N   . SER C  2  123 ? 11.595  6.141   28.246  1.00 89.09  ? 141  SER C N   1 
ATOM   10592 C  CA  . SER C  2  123 ? 10.223  6.276   27.751  1.00 90.95  ? 141  SER C CA  1 
ATOM   10593 C  C   . SER C  2  123 ? 10.085  7.535   26.901  1.00 91.84  ? 141  SER C C   1 
ATOM   10594 O  O   . SER C  2  123 ? 9.635   7.461   25.757  1.00 91.93  ? 141  SER C O   1 
ATOM   10595 C  CB  . SER C  2  123 ? 9.224   6.302   28.913  1.00 91.44  ? 141  SER C CB  1 
ATOM   10596 O  OG  . SER C  2  123 ? 9.777   6.923   30.063  1.00 92.40  ? 141  SER C OG  1 
ATOM   10597 N  N   . PRO C  2  124 ? 10.467  8.710   27.439  1.00 92.41  ? 142  PRO C N   1 
ATOM   10598 C  CA  . PRO C  2  124 ? 10.332  9.905   26.595  1.00 93.12  ? 142  PRO C CA  1 
ATOM   10599 C  C   . PRO C  2  124 ? 11.556  9.961   25.671  1.00 93.62  ? 142  PRO C C   1 
ATOM   10600 O  O   . PRO C  2  124 ? 11.643  10.793  24.766  1.00 94.82  ? 142  PRO C O   1 
ATOM   10601 C  CB  . PRO C  2  124 ? 10.322  11.057  27.611  1.00 92.95  ? 142  PRO C CB  1 
ATOM   10602 C  CG  . PRO C  2  124 ? 10.151  10.376  28.976  1.00 92.67  ? 142  PRO C CG  1 
ATOM   10603 C  CD  . PRO C  2  124 ? 10.881  9.086   28.800  1.00 91.82  ? 142  PRO C CD  1 
ATOM   10604 N  N   . GLU C  2  125 ? 12.488  9.045   25.928  1.00 92.75  ? 143  GLU C N   1 
ATOM   10605 C  CA  . GLU C  2  125 ? 13.746  8.901   25.196  1.00 91.10  ? 143  GLU C CA  1 
ATOM   10606 C  C   . GLU C  2  125 ? 14.570  10.177  24.986  1.00 89.98  ? 143  GLU C C   1 
ATOM   10607 O  O   . GLU C  2  125 ? 14.167  11.105  24.282  1.00 89.60  ? 143  GLU C O   1 
ATOM   10608 C  CB  . GLU C  2  125 ? 13.517  8.188   23.852  1.00 90.37  ? 143  GLU C CB  1 
ATOM   10609 C  CG  . GLU C  2  125 ? 12.859  8.999   22.750  1.00 89.38  ? 143  GLU C CG  1 
ATOM   10610 C  CD  . GLU C  2  125 ? 13.064  8.363   21.381  1.00 89.58  ? 143  GLU C CD  1 
ATOM   10611 O  OE1 . GLU C  2  125 ? 12.667  7.188   21.204  1.00 90.30  ? 143  GLU C OE1 1 
ATOM   10612 O  OE2 . GLU C  2  125 ? 13.627  9.031   20.485  1.00 87.38  ? 143  GLU C OE2 1 
ATOM   10613 N  N   . GLU C  2  126 ? 15.739  10.190  25.617  1.00 88.56  ? 144  GLU C N   1 
ATOM   10614 C  CA  . GLU C  2  126 ? 16.672  11.294  25.544  1.00 87.30  ? 144  GLU C CA  1 
ATOM   10615 C  C   . GLU C  2  126 ? 18.027  10.638  25.433  1.00 84.27  ? 144  GLU C C   1 
ATOM   10616 O  O   . GLU C  2  126 ? 18.158  9.469   25.744  1.00 83.22  ? 144  GLU C O   1 
ATOM   10617 C  CB  . GLU C  2  126 ? 16.584  12.120  26.815  1.00 91.59  ? 144  GLU C CB  1 
ATOM   10618 C  CG  . GLU C  2  126 ? 15.153  12.458  27.194  1.00 98.49  ? 144  GLU C CG  1 
ATOM   10619 C  CD  . GLU C  2  126 ? 15.055  13.424  28.364  1.00 102.76 ? 144  GLU C CD  1 
ATOM   10620 O  OE1 . GLU C  2  126 ? 15.556  13.087  29.469  1.00 104.31 ? 144  GLU C OE1 1 
ATOM   10621 O  OE2 . GLU C  2  126 ? 14.476  14.524  28.167  1.00 104.57 ? 144  GLU C OE2 1 
ATOM   10622 N  N   . MET C  2  127 ? 19.037  11.380  25.002  1.00 82.22  ? 145  MET C N   1 
ATOM   10623 C  CA  . MET C  2  127 ? 20.363  10.803  24.843  1.00 80.25  ? 145  MET C CA  1 
ATOM   10624 C  C   . MET C  2  127 ? 20.951  10.217  26.119  1.00 78.41  ? 145  MET C C   1 
ATOM   10625 O  O   . MET C  2  127 ? 20.837  10.798  27.190  1.00 77.78  ? 145  MET C O   1 
ATOM   10626 C  CB  . MET C  2  127 ? 21.328  11.838  24.293  1.00 82.19  ? 145  MET C CB  1 
ATOM   10627 C  CG  . MET C  2  127 ? 22.650  11.230  23.903  1.00 85.99  ? 145  MET C CG  1 
ATOM   10628 S  SD  . MET C  2  127 ? 23.993  12.417  23.908  1.00 90.09  ? 145  MET C SD  1 
ATOM   10629 C  CE  . MET C  2  127 ? 24.408  12.409  25.696  1.00 88.17  ? 145  MET C CE  1 
ATOM   10630 N  N   . LEU C  2  128 ? 21.589  9.058   25.985  1.00 76.83  ? 146  LEU C N   1 
ATOM   10631 C  CA  . LEU C  2  128 ? 22.208  8.367   27.112  1.00 75.39  ? 146  LEU C CA  1 
ATOM   10632 C  C   . LEU C  2  128 ? 23.683  8.776   27.157  1.00 75.05  ? 146  LEU C C   1 
ATOM   10633 O  O   . LEU C  2  128 ? 24.190  9.215   28.196  1.00 75.88  ? 146  LEU C O   1 
ATOM   10634 C  CB  . LEU C  2  128 ? 22.092  6.853   26.927  1.00 74.05  ? 146  LEU C CB  1 
ATOM   10635 C  CG  . LEU C  2  128 ? 21.958  5.948   28.159  1.00 74.16  ? 146  LEU C CG  1 
ATOM   10636 C  CD1 . LEU C  2  128 ? 22.441  4.554   27.795  1.00 73.11  ? 146  LEU C CD1 1 
ATOM   10637 C  CD2 . LEU C  2  128 ? 22.778  6.476   29.329  1.00 76.51  ? 146  LEU C CD2 1 
ATOM   10638 N  N   . PHE C  2  129 ? 24.370  8.608   26.029  1.00 73.12  ? 147  PHE C N   1 
ATOM   10639 C  CA  . PHE C  2  129 ? 25.768  8.993   25.903  1.00 71.63  ? 147  PHE C CA  1 
ATOM   10640 C  C   . PHE C  2  129 ? 26.122  9.098   24.425  1.00 72.13  ? 147  PHE C C   1 
ATOM   10641 O  O   . PHE C  2  129 ? 25.412  8.578   23.567  1.00 71.52  ? 147  PHE C O   1 
ATOM   10642 C  CB  . PHE C  2  129 ? 26.691  7.989   26.613  1.00 69.44  ? 147  PHE C CB  1 
ATOM   10643 C  CG  . PHE C  2  129 ? 26.690  6.614   26.009  1.00 68.85  ? 147  PHE C CG  1 
ATOM   10644 C  CD1 . PHE C  2  129 ? 27.282  6.373   24.765  1.00 69.08  ? 147  PHE C CD1 1 
ATOM   10645 C  CD2 . PHE C  2  129 ? 26.102  5.557   26.681  1.00 68.20  ? 147  PHE C CD2 1 
ATOM   10646 C  CE1 . PHE C  2  129 ? 27.274  5.097   24.200  1.00 67.60  ? 147  PHE C CE1 1 
ATOM   10647 C  CE2 . PHE C  2  129 ? 26.091  4.284   26.129  1.00 67.85  ? 147  PHE C CE2 1 
ATOM   10648 C  CZ  . PHE C  2  129 ? 26.681  4.052   24.883  1.00 66.56  ? 147  PHE C CZ  1 
ATOM   10649 N  N   . CYS C  2  130 ? 27.207  9.801   24.131  1.00 73.12  ? 148  CYS C N   1 
ATOM   10650 C  CA  . CYS C  2  130 ? 27.662  9.967   22.761  1.00 73.99  ? 148  CYS C CA  1 
ATOM   10651 C  C   . CYS C  2  130 ? 29.147  9.657   22.781  1.00 73.57  ? 148  CYS C C   1 
ATOM   10652 O  O   . CYS C  2  130 ? 29.874  10.164  23.629  1.00 73.98  ? 148  CYS C O   1 
ATOM   10653 C  CB  . CYS C  2  130 ? 27.441  11.407  22.293  1.00 75.44  ? 148  CYS C CB  1 
ATOM   10654 S  SG  . CYS C  2  130 ? 27.797  11.706  20.521  1.00 82.09  ? 148  CYS C SG  1 
ATOM   10655 N  N   . LEU C  2  131 ? 29.597  8.813   21.859  1.00 73.21  ? 149  LEU C N   1 
ATOM   10656 C  CA  . LEU C  2  131 ? 31.007  8.446   21.772  1.00 72.42  ? 149  LEU C CA  1 
ATOM   10657 C  C   . LEU C  2  131 ? 31.432  8.548   20.319  1.00 73.52  ? 149  LEU C C   1 
ATOM   10658 O  O   . LEU C  2  131 ? 30.640  8.264   19.424  1.00 73.60  ? 149  LEU C O   1 
ATOM   10659 C  CB  . LEU C  2  131 ? 31.207  7.006   22.236  1.00 69.63  ? 149  LEU C CB  1 
ATOM   10660 C  CG  . LEU C  2  131 ? 30.956  6.681   23.699  1.00 67.17  ? 149  LEU C CG  1 
ATOM   10661 C  CD1 . LEU C  2  131 ? 31.041  5.187   23.913  1.00 67.16  ? 149  LEU C CD1 1 
ATOM   10662 C  CD2 . LEU C  2  131 ? 31.993  7.392   24.532  1.00 67.40  ? 149  LEU C CD2 1 
ATOM   10663 N  N   . GLU C  2  132 ? 32.669  8.966   20.075  1.00 74.91  ? 150  GLU C N   1 
ATOM   10664 C  CA  . GLU C  2  132 ? 33.163  9.045   18.707  1.00 75.54  ? 150  GLU C CA  1 
ATOM   10665 C  C   . GLU C  2  132 ? 34.308  8.047   18.585  1.00 74.05  ? 150  GLU C C   1 
ATOM   10666 O  O   . GLU C  2  132 ? 35.372  8.220   19.189  1.00 73.94  ? 150  GLU C O   1 
ATOM   10667 C  CB  . GLU C  2  132 ? 33.656  10.448  18.362  1.00 78.64  ? 150  GLU C CB  1 
ATOM   10668 C  CG  . GLU C  2  132 ? 33.885  10.636  16.863  1.00 85.05  ? 150  GLU C CG  1 
ATOM   10669 C  CD  . GLU C  2  132 ? 34.744  11.852  16.518  1.00 89.36  ? 150  GLU C CD  1 
ATOM   10670 O  OE1 . GLU C  2  132 ? 35.918  11.908  16.976  1.00 89.86  ? 150  GLU C OE1 1 
ATOM   10671 O  OE2 . GLU C  2  132 ? 34.244  12.743  15.780  1.00 91.08  ? 150  GLU C OE2 1 
ATOM   10672 N  N   . PHE C  2  133 ? 34.069  6.990   17.813  1.00 72.15  ? 151  PHE C N   1 
ATOM   10673 C  CA  . PHE C  2  133 ? 35.053  5.933   17.611  1.00 70.29  ? 151  PHE C CA  1 
ATOM   10674 C  C   . PHE C  2  133 ? 35.969  6.170   16.427  1.00 70.63  ? 151  PHE C C   1 
ATOM   10675 O  O   . PHE C  2  133 ? 35.517  6.459   15.323  1.00 70.78  ? 151  PHE C O   1 
ATOM   10676 C  CB  . PHE C  2  133 ? 34.362  4.577   17.422  1.00 66.12  ? 151  PHE C CB  1 
ATOM   10677 C  CG  . PHE C  2  133 ? 33.856  3.959   18.700  1.00 61.49  ? 151  PHE C CG  1 
ATOM   10678 C  CD1 . PHE C  2  133 ? 32.618  4.318   19.232  1.00 58.76  ? 151  PHE C CD1 1 
ATOM   10679 C  CD2 . PHE C  2  133 ? 34.620  3.008   19.368  1.00 58.27  ? 151  PHE C CD2 1 
ATOM   10680 C  CE1 . PHE C  2  133 ? 32.160  3.741   20.404  1.00 56.45  ? 151  PHE C CE1 1 
ATOM   10681 C  CE2 . PHE C  2  133 ? 34.168  2.430   20.540  1.00 55.28  ? 151  PHE C CE2 1 
ATOM   10682 C  CZ  . PHE C  2  133 ? 32.933  2.792   21.059  1.00 55.73  ? 151  PHE C CZ  1 
ATOM   10683 N  N   . VAL C  2  134 ? 37.266  6.043   16.664  1.00 71.39  ? 152  VAL C N   1 
ATOM   10684 C  CA  . VAL C  2  134 ? 38.246  6.222   15.610  1.00 72.97  ? 152  VAL C CA  1 
ATOM   10685 C  C   . VAL C  2  134 ? 38.909  4.878   15.419  1.00 73.14  ? 152  VAL C C   1 
ATOM   10686 O  O   . VAL C  2  134 ? 39.585  4.360   16.315  1.00 73.01  ? 152  VAL C O   1 
ATOM   10687 C  CB  . VAL C  2  134 ? 39.302  7.269   15.990  1.00 74.64  ? 152  VAL C CB  1 
ATOM   10688 C  CG1 . VAL C  2  134 ? 40.433  7.266   14.969  1.00 75.42  ? 152  VAL C CG1 1 
ATOM   10689 C  CG2 . VAL C  2  134 ? 38.648  8.651   16.058  1.00 75.90  ? 152  VAL C CG2 1 
ATOM   10690 N  N   . ILE C  2  135 ? 38.708  4.310   14.240  1.00 73.05  ? 153  ILE C N   1 
ATOM   10691 C  CA  . ILE C  2  135 ? 39.264  3.008   13.933  1.00 72.84  ? 153  ILE C CA  1 
ATOM   10692 C  C   . ILE C  2  135 ? 40.113  3.055   12.656  1.00 72.76  ? 153  ILE C C   1 
ATOM   10693 O  O   . ILE C  2  135 ? 39.621  3.384   11.574  1.00 72.61  ? 153  ILE C O   1 
ATOM   10694 C  CB  . ILE C  2  135 ? 38.098  1.995   13.846  1.00 73.16  ? 153  ILE C CB  1 
ATOM   10695 C  CG1 . ILE C  2  135 ? 38.551  0.681   13.244  1.00 73.30  ? 153  ILE C CG1 1 
ATOM   10696 C  CG2 . ILE C  2  135 ? 36.943  2.596   13.078  1.00 72.71  ? 153  ILE C CG2 1 
ATOM   10697 C  CD1 . ILE C  2  135 ? 37.473  -0.363  13.354  1.00 74.87  ? 153  ILE C CD1 1 
ATOM   10698 N  N   . LEU C  2  136 ? 41.405  2.770   12.804  1.00 72.36  ? 154  LEU C N   1 
ATOM   10699 C  CA  . LEU C  2  136 ? 42.328  2.789   11.674  1.00 73.37  ? 154  LEU C CA  1 
ATOM   10700 C  C   . LEU C  2  136 ? 42.382  1.403   11.063  1.00 74.53  ? 154  LEU C C   1 
ATOM   10701 O  O   . LEU C  2  136 ? 42.496  0.414   11.776  1.00 74.06  ? 154  LEU C O   1 
ATOM   10702 C  CB  . LEU C  2  136 ? 43.746  3.204   12.107  1.00 72.79  ? 154  LEU C CB  1 
ATOM   10703 C  CG  . LEU C  2  136 ? 44.041  4.558   12.767  1.00 72.18  ? 154  LEU C CG  1 
ATOM   10704 C  CD1 . LEU C  2  136 ? 43.264  5.676   12.078  1.00 71.64  ? 154  LEU C CD1 1 
ATOM   10705 C  CD2 . LEU C  2  136 ? 43.672  4.489   14.243  1.00 74.43  ? 154  LEU C CD2 1 
ATOM   10706 N  N   . HIS C  2  137 ? 42.319  1.337   9.738   1.00 76.42  ? 155  HIS C N   1 
ATOM   10707 C  CA  . HIS C  2  137 ? 42.341  0.062   9.045   1.00 77.97  ? 155  HIS C CA  1 
ATOM   10708 C  C   . HIS C  2  137 ? 43.477  -0.082  8.034   1.00 80.69  ? 155  HIS C C   1 
ATOM   10709 O  O   . HIS C  2  137 ? 43.655  0.753   7.140   1.00 80.00  ? 155  HIS C O   1 
ATOM   10710 C  CB  . HIS C  2  137 ? 40.994  -0.146  8.345   1.00 76.28  ? 155  HIS C CB  1 
ATOM   10711 C  CG  . HIS C  2  137 ? 40.890  -1.432  7.583   1.00 75.97  ? 155  HIS C CG  1 
ATOM   10712 N  ND1 . HIS C  2  137 ? 41.088  -2.666  8.169   1.00 76.18  ? 155  HIS C ND1 1 
ATOM   10713 C  CD2 . HIS C  2  137 ? 40.601  -1.676  6.284   1.00 74.59  ? 155  HIS C CD2 1 
ATOM   10714 C  CE1 . HIS C  2  137 ? 40.929  -3.612  7.262   1.00 74.82  ? 155  HIS C CE1 1 
ATOM   10715 N  NE2 . HIS C  2  137 ? 40.632  -3.037  6.109   1.00 74.75  ? 155  HIS C NE2 1 
ATOM   10716 N  N   . GLN C  2  138 ? 44.243  -1.155  8.195   1.00 84.85  ? 156  GLN C N   1 
ATOM   10717 C  CA  . GLN C  2  138 ? 45.344  -1.483  7.297   1.00 90.76  ? 156  GLN C CA  1 
ATOM   10718 C  C   . GLN C  2  138 ? 45.098  -2.920  6.800   1.00 94.17  ? 156  GLN C C   1 
ATOM   10719 O  O   . GLN C  2  138 ? 45.384  -3.886  7.506   1.00 94.48  ? 156  GLN C O   1 
ATOM   10720 C  CB  . GLN C  2  138 ? 46.686  -1.398  8.037   1.00 91.61  ? 156  GLN C CB  1 
ATOM   10721 C  CG  . GLN C  2  138 ? 47.891  -1.815  7.192   1.00 93.89  ? 156  GLN C CG  1 
ATOM   10722 C  CD  . GLN C  2  138 ? 47.989  -1.036  5.877   1.00 95.95  ? 156  GLN C CD  1 
ATOM   10723 O  OE1 . GLN C  2  138 ? 48.132  0.193   5.875   1.00 96.54  ? 156  GLN C OE1 1 
ATOM   10724 N  NE2 . GLN C  2  138 ? 47.909  -1.752  4.754   1.00 95.55  ? 156  GLN C NE2 1 
ATOM   10725 N  N   . PRO C  2  139 ? 44.557  -3.072  5.577   1.00 97.12  ? 157  PRO C N   1 
ATOM   10726 C  CA  . PRO C  2  139 ? 44.267  -4.387  4.994   1.00 100.06 ? 157  PRO C CA  1 
ATOM   10727 C  C   . PRO C  2  139 ? 45.459  -5.316  4.747   1.00 103.13 ? 157  PRO C C   1 
ATOM   10728 O  O   . PRO C  2  139 ? 46.548  -5.112  5.290   1.00 103.42 ? 157  PRO C O   1 
ATOM   10729 C  CB  . PRO C  2  139 ? 43.532  -4.030  3.702   1.00 99.93  ? 157  PRO C CB  1 
ATOM   10730 C  CG  . PRO C  2  139 ? 44.161  -2.738  3.309   1.00 98.94  ? 157  PRO C CG  1 
ATOM   10731 C  CD  . PRO C  2  139 ? 44.208  -1.998  4.628   1.00 97.93  ? 157  PRO C CD  1 
ATOM   10732 N  N   . ASN C  2  140 ? 45.223  -6.341  3.925   1.00 106.63 ? 158  ASN C N   1 
ATOM   10733 C  CA  . ASN C  2  140 ? 46.225  -7.350  3.560   1.00 109.46 ? 158  ASN C CA  1 
ATOM   10734 C  C   . ASN C  2  140 ? 46.714  -8.202  4.740   1.00 110.65 ? 158  ASN C C   1 
ATOM   10735 O  O   . ASN C  2  140 ? 46.475  -9.437  4.710   1.00 111.07 ? 158  ASN C O   1 
ATOM   10736 C  CB  . ASN C  2  140 ? 47.427  -6.690  2.866   1.00 110.05 ? 158  ASN C CB  1 
ATOM   10737 C  CG  . ASN C  2  140 ? 48.556  -7.674  2.587   1.00 110.73 ? 158  ASN C CG  1 
ATOM   10738 O  OD1 . ASN C  2  140 ? 48.397  -8.614  1.804   1.00 111.26 ? 158  ASN C OD1 1 
ATOM   10739 N  ND2 . ASN C  2  140 ? 49.701  -7.464  3.234   1.00 110.23 ? 158  ASN C ND2 1 
ATOM   10740 N  N   . GLN D  2  1   ? -15.875 -1.741  -43.153 1.00 103.86 ? 19   GLN D N   1 
ATOM   10741 C  CA  . GLN D  2  1   ? -16.742 -1.052  -42.142 1.00 105.02 ? 19   GLN D CA  1 
ATOM   10742 C  C   . GLN D  2  1   ? -17.660 -2.028  -41.406 1.00 104.07 ? 19   GLN D C   1 
ATOM   10743 O  O   . GLN D  2  1   ? -18.121 -1.761  -40.289 1.00 102.82 ? 19   GLN D O   1 
ATOM   10744 C  CB  . GLN D  2  1   ? -17.598 0.029   -42.821 1.00 107.09 ? 19   GLN D CB  1 
ATOM   10745 C  CG  . GLN D  2  1   ? -18.508 0.785   -41.860 1.00 108.28 ? 19   GLN D CG  1 
ATOM   10746 C  CD  . GLN D  2  1   ? -17.817 1.104   -40.539 1.00 109.26 ? 19   GLN D CD  1 
ATOM   10747 O  OE1 . GLN D  2  1   ? -16.712 1.657   -40.514 1.00 108.89 ? 19   GLN D OE1 1 
ATOM   10748 N  NE2 . GLN D  2  1   ? -18.463 0.742   -39.432 1.00 108.86 ? 19   GLN D NE2 1 
ATOM   10749 N  N   . LYS D  2  2   ? -17.924 -3.161  -42.048 1.00 103.42 ? 20   LYS D N   1 
ATOM   10750 C  CA  . LYS D  2  2   ? -18.786 -4.190  -41.479 1.00 101.99 ? 20   LYS D CA  1 
ATOM   10751 C  C   . LYS D  2  2   ? -18.283 -4.680  -40.116 1.00 100.41 ? 20   LYS D C   1 
ATOM   10752 O  O   . LYS D  2  2   ? -17.085 -4.885  -39.911 1.00 100.05 ? 20   LYS D O   1 
ATOM   10753 C  CB  . LYS D  2  2   ? -18.887 -5.380  -42.449 1.00 102.18 ? 20   LYS D CB  1 
ATOM   10754 C  CG  . LYS D  2  2   ? -19.800 -6.497  -41.971 1.00 103.11 ? 20   LYS D CG  1 
ATOM   10755 C  CD  . LYS D  2  2   ? -19.664 -7.773  -42.802 1.00 103.64 ? 20   LYS D CD  1 
ATOM   10756 C  CE  . LYS D  2  2   ? -20.499 -8.907  -42.187 1.00 104.64 ? 20   LYS D CE  1 
ATOM   10757 N  NZ  . LYS D  2  2   ? -20.349 -10.230 -42.864 1.00 103.60 ? 20   LYS D NZ  1 
ATOM   10758 N  N   . GLN D  2  3   ? -19.210 -4.849  -39.182 1.00 98.44  ? 21   GLN D N   1 
ATOM   10759 C  CA  . GLN D  2  3   ? -18.872 -5.353  -37.864 1.00 96.66  ? 21   GLN D CA  1 
ATOM   10760 C  C   . GLN D  2  3   ? -19.103 -6.854  -37.900 1.00 95.04  ? 21   GLN D C   1 
ATOM   10761 O  O   . GLN D  2  3   ? -20.151 -7.309  -38.358 1.00 94.49  ? 21   GLN D O   1 
ATOM   10762 C  CB  . GLN D  2  3   ? -19.767 -4.740  -36.793 1.00 97.44  ? 21   GLN D CB  1 
ATOM   10763 C  CG  . GLN D  2  3   ? -19.219 -3.493  -36.152 1.00 98.64  ? 21   GLN D CG  1 
ATOM   10764 C  CD  . GLN D  2  3   ? -19.674 -3.372  -34.717 1.00 99.69  ? 21   GLN D CD  1 
ATOM   10765 O  OE1 . GLN D  2  3   ? -20.872 -3.347  -34.433 1.00 99.10  ? 21   GLN D OE1 1 
ATOM   10766 N  NE2 . GLN D  2  3   ? -18.714 -3.309  -33.797 1.00 100.49 ? 21   GLN D NE2 1 
ATOM   10767 N  N   . TYR D  2  4   ? -18.127 -7.624  -37.427 1.00 92.91  ? 22   TYR D N   1 
ATOM   10768 C  CA  . TYR D  2  4   ? -18.252 -9.078  -37.416 1.00 89.95  ? 22   TYR D CA  1 
ATOM   10769 C  C   . TYR D  2  4   ? -18.576 -9.548  -36.005 1.00 88.20  ? 22   TYR D C   1 
ATOM   10770 O  O   . TYR D  2  4   ? -17.987 -9.078  -35.038 1.00 88.87  ? 22   TYR D O   1 
ATOM   10771 C  CB  . TYR D  2  4   ? -16.956 -9.721  -37.915 1.00 89.53  ? 22   TYR D CB  1 
ATOM   10772 C  CG  . TYR D  2  4   ? -16.527 -9.241  -39.290 1.00 89.28  ? 22   TYR D CG  1 
ATOM   10773 C  CD1 . TYR D  2  4   ? -15.900 -8.001  -39.458 1.00 89.49  ? 22   TYR D CD1 1 
ATOM   10774 C  CD2 . TYR D  2  4   ? -16.769 -10.013 -40.426 1.00 88.28  ? 22   TYR D CD2 1 
ATOM   10775 C  CE1 . TYR D  2  4   ? -15.526 -7.546  -40.729 1.00 89.25  ? 22   TYR D CE1 1 
ATOM   10776 C  CE2 . TYR D  2  4   ? -16.401 -9.568  -41.693 1.00 87.86  ? 22   TYR D CE2 1 
ATOM   10777 C  CZ  . TYR D  2  4   ? -15.783 -8.340  -41.843 1.00 88.42  ? 22   TYR D CZ  1 
ATOM   10778 O  OH  . TYR D  2  4   ? -15.424 -7.899  -43.099 1.00 87.03  ? 22   TYR D OH  1 
ATOM   10779 N  N   . TRP D  2  5   ? -19.516 -10.475 -35.891 1.00 86.09  ? 23   TRP D N   1 
ATOM   10780 C  CA  . TRP D  2  5   ? -19.941 -10.980 -34.594 1.00 84.60  ? 23   TRP D CA  1 
ATOM   10781 C  C   . TRP D  2  5   ? -19.277 -12.296 -34.217 1.00 84.21  ? 23   TRP D C   1 
ATOM   10782 O  O   . TRP D  2  5   ? -19.501 -13.323 -34.860 1.00 84.84  ? 23   TRP D O   1 
ATOM   10783 C  CB  . TRP D  2  5   ? -21.457 -11.156 -34.605 1.00 83.64  ? 23   TRP D CB  1 
ATOM   10784 C  CG  . TRP D  2  5   ? -22.066 -11.559 -33.303 1.00 83.77  ? 23   TRP D CG  1 
ATOM   10785 C  CD1 . TRP D  2  5   ? -22.102 -10.826 -32.152 1.00 84.54  ? 23   TRP D CD1 1 
ATOM   10786 C  CD2 . TRP D  2  5   ? -22.784 -12.771 -33.029 1.00 83.80  ? 23   TRP D CD2 1 
ATOM   10787 N  NE1 . TRP D  2  5   ? -22.805 -11.504 -31.181 1.00 84.33  ? 23   TRP D NE1 1 
ATOM   10788 C  CE2 . TRP D  2  5   ? -23.234 -12.700 -31.694 1.00 84.06  ? 23   TRP D CE2 1 
ATOM   10789 C  CE3 . TRP D  2  5   ? -23.091 -13.909 -33.783 1.00 83.73  ? 23   TRP D CE3 1 
ATOM   10790 C  CZ2 . TRP D  2  5   ? -23.978 -13.727 -31.098 1.00 84.05  ? 23   TRP D CZ2 1 
ATOM   10791 C  CZ3 . TRP D  2  5   ? -23.833 -14.933 -33.187 1.00 83.75  ? 23   TRP D CZ3 1 
ATOM   10792 C  CH2 . TRP D  2  5   ? -24.266 -14.832 -31.860 1.00 84.36  ? 23   TRP D CH2 1 
ATOM   10793 N  N   . VAL D  2  6   ? -18.453 -12.274 -33.176 1.00 83.29  ? 24   VAL D N   1 
ATOM   10794 C  CA  . VAL D  2  6   ? -17.805 -13.497 -32.736 1.00 81.72  ? 24   VAL D CA  1 
ATOM   10795 C  C   . VAL D  2  6   ? -18.826 -14.317 -31.941 1.00 81.12  ? 24   VAL D C   1 
ATOM   10796 O  O   . VAL D  2  6   ? -19.298 -15.341 -32.429 1.00 81.59  ? 24   VAL D O   1 
ATOM   10797 C  CB  . VAL D  2  6   ? -16.570 -13.193 -31.876 1.00 81.62  ? 24   VAL D CB  1 
ATOM   10798 C  CG1 . VAL D  2  6   ? -15.798 -14.480 -31.602 1.00 80.96  ? 24   VAL D CG1 1 
ATOM   10799 C  CG2 . VAL D  2  6   ? -15.688 -12.181 -32.588 1.00 81.24  ? 24   VAL D CG2 1 
ATOM   10800 N  N   . CYS D  2  7   ? -19.189 -13.864 -30.738 1.00 79.76  ? 25   CYS D N   1 
ATOM   10801 C  CA  . CYS D  2  7   ? -20.171 -14.586 -29.924 1.00 79.38  ? 25   CYS D CA  1 
ATOM   10802 C  C   . CYS D  2  7   ? -20.689 -13.840 -28.700 1.00 79.92  ? 25   CYS D C   1 
ATOM   10803 O  O   . CYS D  2  7   ? -20.225 -12.742 -28.377 1.00 80.47  ? 25   CYS D O   1 
ATOM   10804 C  CB  . CYS D  2  7   ? -19.596 -15.919 -29.449 1.00 78.77  ? 25   CYS D CB  1 
ATOM   10805 S  SG  . CYS D  2  7   ? -18.112 -15.815 -28.367 1.00 80.19  ? 25   CYS D SG  1 
ATOM   10806 N  N   . ASN D  2  8   ? -21.652 -14.467 -28.022 1.00 79.59  ? 26   ASN D N   1 
ATOM   10807 C  CA  . ASN D  2  8   ? -22.258 -13.941 -26.799 1.00 79.55  ? 26   ASN D CA  1 
ATOM   10808 C  C   . ASN D  2  8   ? -22.292 -15.055 -25.756 1.00 78.71  ? 26   ASN D C   1 
ATOM   10809 O  O   . ASN D  2  8   ? -22.534 -16.217 -26.079 1.00 78.87  ? 26   ASN D O   1 
ATOM   10810 C  CB  . ASN D  2  8   ? -23.703 -13.475 -27.040 1.00 81.94  ? 26   ASN D CB  1 
ATOM   10811 C  CG  . ASN D  2  8   ? -23.791 -12.175 -27.827 1.00 83.74  ? 26   ASN D CG  1 
ATOM   10812 O  OD1 . ASN D  2  8   ? -24.894 -11.703 -28.152 1.00 84.42  ? 26   ASN D OD1 1 
ATOM   10813 N  ND2 . ASN D  2  8   ? -22.639 -11.587 -28.134 1.00 83.78  ? 26   ASN D ND2 1 
ATOM   10814 N  N   . SER D  2  9   ? -22.042 -14.699 -24.505 1.00 78.84  ? 27   SER D N   1 
ATOM   10815 C  CA  . SER D  2  9   ? -22.079 -15.670 -23.411 1.00 79.18  ? 27   SER D CA  1 
ATOM   10816 C  C   . SER D  2  9   ? -23.198 -15.229 -22.469 1.00 78.81  ? 27   SER D C   1 
ATOM   10817 O  O   . SER D  2  9   ? -24.339 -15.017 -22.893 1.00 79.66  ? 27   SER D O   1 
ATOM   10818 C  CB  . SER D  2  9   ? -20.744 -15.679 -22.663 1.00 78.97  ? 27   SER D CB  1 
ATOM   10819 O  OG  . SER D  2  9   ? -20.400 -14.368 -22.236 1.00 79.62  ? 27   SER D OG  1 
ATOM   10820 N  N   . SER D  2  10  ? -22.873 -15.090 -21.193 1.00 77.52  ? 28   SER D N   1 
ATOM   10821 C  CA  . SER D  2  10  ? -23.849 -14.638 -20.218 1.00 76.70  ? 28   SER D CA  1 
ATOM   10822 C  C   . SER D  2  10  ? -23.223 -13.431 -19.526 1.00 76.92  ? 28   SER D C   1 
ATOM   10823 O  O   . SER D  2  10  ? -23.864 -12.695 -18.780 1.00 76.85  ? 28   SER D O   1 
ATOM   10824 C  CB  . SER D  2  10  ? -24.137 -15.756 -19.224 1.00 75.56  ? 28   SER D CB  1 
ATOM   10825 O  OG  . SER D  2  10  ? -22.936 -16.364 -18.801 1.00 73.34  ? 28   SER D OG  1 
ATOM   10826 N  N   . ASP D  2  11  ? -21.952 -13.232 -19.831 1.00 77.74  ? 29   ASP D N   1 
ATOM   10827 C  CA  . ASP D  2  11  ? -21.151 -12.153 -19.286 1.00 77.88  ? 29   ASP D CA  1 
ATOM   10828 C  C   . ASP D  2  11  ? -20.900 -11.117 -20.355 1.00 77.24  ? 29   ASP D C   1 
ATOM   10829 O  O   . ASP D  2  11  ? -20.883 -9.915  -20.075 1.00 76.66  ? 29   ASP D O   1 
ATOM   10830 C  CB  . ASP D  2  11  ? -19.789 -12.693 -18.843 1.00 80.85  ? 29   ASP D CB  1 
ATOM   10831 C  CG  . ASP D  2  11  ? -19.747 -13.054 -17.377 1.00 84.21  ? 29   ASP D CG  1 
ATOM   10832 O  OD1 . ASP D  2  11  ? -20.642 -13.794 -16.898 1.00 85.05  ? 29   ASP D OD1 1 
ATOM   10833 O  OD2 . ASP D  2  11  ? -18.800 -12.590 -16.704 1.00 85.71  ? 29   ASP D OD2 1 
ATOM   10834 N  N   . ALA D  2  12  ? -20.705 -11.584 -21.587 1.00 75.75  ? 30   ALA D N   1 
ATOM   10835 C  CA  . ALA D  2  12  ? -20.384 -10.663 -22.656 1.00 74.18  ? 30   ALA D CA  1 
ATOM   10836 C  C   . ALA D  2  12  ? -20.868 -10.940 -24.071 1.00 73.54  ? 30   ALA D C   1 
ATOM   10837 O  O   . ALA D  2  12  ? -21.437 -11.985 -24.386 1.00 72.79  ? 30   ALA D O   1 
ATOM   10838 C  CB  . ALA D  2  12  ? -18.878 -10.461 -22.678 1.00 74.78  ? 30   ALA D CB  1 
ATOM   10839 N  N   . SER D  2  13  ? -20.604 -9.941  -24.908 1.00 73.16  ? 31   SER D N   1 
ATOM   10840 C  CA  . SER D  2  13  ? -20.920 -9.923  -26.325 1.00 73.07  ? 31   SER D CA  1 
ATOM   10841 C  C   . SER D  2  13  ? -19.630 -9.414  -27.003 1.00 73.97  ? 31   SER D C   1 
ATOM   10842 O  O   . SER D  2  13  ? -19.168 -8.293  -26.739 1.00 73.75  ? 31   SER D O   1 
ATOM   10843 C  CB  . SER D  2  13  ? -22.078 -8.965  -26.572 1.00 72.05  ? 31   SER D CB  1 
ATOM   10844 O  OG  . SER D  2  13  ? -22.416 -8.906  -27.943 1.00 72.02  ? 31   SER D OG  1 
ATOM   10845 N  N   . ILE D  2  14  ? -19.054 -10.246 -27.869 1.00 74.09  ? 32   ILE D N   1 
ATOM   10846 C  CA  . ILE D  2  14  ? -17.799 -9.920  -28.545 1.00 73.92  ? 32   ILE D CA  1 
ATOM   10847 C  C   . ILE D  2  14  ? -17.913 -9.737  -30.065 1.00 73.98  ? 32   ILE D C   1 
ATOM   10848 O  O   . ILE D  2  14  ? -18.459 -10.592 -30.773 1.00 74.72  ? 32   ILE D O   1 
ATOM   10849 C  CB  . ILE D  2  14  ? -16.755 -11.021 -28.242 1.00 73.51  ? 32   ILE D CB  1 
ATOM   10850 C  CG1 . ILE D  2  14  ? -16.587 -11.155 -26.733 1.00 73.37  ? 32   ILE D CG1 1 
ATOM   10851 C  CG2 . ILE D  2  14  ? -15.418 -10.677 -28.850 1.00 73.58  ? 32   ILE D CG2 1 
ATOM   10852 C  CD1 . ILE D  2  14  ? -15.839 -12.379 -26.320 1.00 73.39  ? 32   ILE D CD1 1 
ATOM   10853 N  N   . SER D  2  15  ? -17.387 -8.617  -30.556 1.00 72.70  ? 33   SER D N   1 
ATOM   10854 C  CA  . SER D  2  15  ? -17.410 -8.316  -31.983 1.00 71.46  ? 33   SER D CA  1 
ATOM   10855 C  C   . SER D  2  15  ? -16.133 -7.550  -32.350 1.00 70.15  ? 33   SER D C   1 
ATOM   10856 O  O   . SER D  2  15  ? -15.437 -7.048  -31.469 1.00 69.67  ? 33   SER D O   1 
ATOM   10857 C  CB  . SER D  2  15  ? -18.646 -7.472  -32.329 1.00 71.58  ? 33   SER D CB  1 
ATOM   10858 O  OG  . SER D  2  15  ? -18.585 -6.192  -31.718 1.00 72.88  ? 33   SER D OG  1 
ATOM   10859 N  N   . TYR D  2  16  ? -15.829 -7.467  -33.647 1.00 69.35  ? 34   TYR D N   1 
ATOM   10860 C  CA  . TYR D  2  16  ? -14.640 -6.756  -34.119 1.00 68.30  ? 34   TYR D CA  1 
ATOM   10861 C  C   . TYR D  2  16  ? -14.812 -6.103  -35.497 1.00 69.27  ? 34   TYR D C   1 
ATOM   10862 O  O   . TYR D  2  16  ? -15.704 -6.453  -36.283 1.00 68.11  ? 34   TYR D O   1 
ATOM   10863 C  CB  . TYR D  2  16  ? -13.412 -7.702  -34.144 1.00 65.90  ? 34   TYR D CB  1 
ATOM   10864 C  CG  . TYR D  2  16  ? -13.425 -8.793  -35.212 1.00 63.41  ? 34   TYR D CG  1 
ATOM   10865 C  CD1 . TYR D  2  16  ? -12.862 -8.574  -36.469 1.00 62.74  ? 34   TYR D CD1 1 
ATOM   10866 C  CD2 . TYR D  2  16  ? -14.013 -10.037 -34.964 1.00 63.00  ? 34   TYR D CD2 1 
ATOM   10867 C  CE1 . TYR D  2  16  ? -12.884 -9.561  -37.454 1.00 62.19  ? 34   TYR D CE1 1 
ATOM   10868 C  CE2 . TYR D  2  16  ? -14.044 -11.028 -35.938 1.00 61.76  ? 34   TYR D CE2 1 
ATOM   10869 C  CZ  . TYR D  2  16  ? -13.478 -10.786 -37.183 1.00 62.71  ? 34   TYR D CZ  1 
ATOM   10870 O  OH  . TYR D  2  16  ? -13.501 -11.779 -38.147 1.00 63.66  ? 34   TYR D OH  1 
ATOM   10871 N  N   . THR D  2  17  ? -13.946 -5.131  -35.763 1.00 70.20  ? 35   THR D N   1 
ATOM   10872 C  CA  . THR D  2  17  ? -13.916 -4.418  -37.035 1.00 70.05  ? 35   THR D CA  1 
ATOM   10873 C  C   . THR D  2  17  ? -12.428 -4.393  -37.393 1.00 71.07  ? 35   THR D C   1 
ATOM   10874 O  O   . THR D  2  17  ? -11.619 -5.036  -36.705 1.00 71.21  ? 35   THR D O   1 
ATOM   10875 C  CB  . THR D  2  17  ? -14.449 -2.966  -36.881 1.00 68.71  ? 35   THR D CB  1 
ATOM   10876 O  OG1 . THR D  2  17  ? -13.498 -2.159  -36.171 1.00 66.85  ? 35   THR D OG1 1 
ATOM   10877 C  CG2 . THR D  2  17  ? -15.756 -2.972  -36.103 1.00 67.52  ? 35   THR D CG2 1 
ATOM   10878 N  N   . TYR D  2  18  ? -12.056 -3.681  -38.456 1.00 70.65  ? 36   TYR D N   1 
ATOM   10879 C  CA  . TYR D  2  18  ? -10.650 -3.589  -38.816 1.00 70.14  ? 36   TYR D CA  1 
ATOM   10880 C  C   . TYR D  2  18  ? -10.176 -2.181  -38.509 1.00 72.30  ? 36   TYR D C   1 
ATOM   10881 O  O   . TYR D  2  18  ? -10.982 -1.256  -38.472 1.00 72.42  ? 36   TYR D O   1 
ATOM   10882 C  CB  . TYR D  2  18  ? -10.444 -3.899  -40.294 1.00 67.52  ? 36   TYR D CB  1 
ATOM   10883 C  CG  . TYR D  2  18  ? -10.627 -5.357  -40.673 1.00 66.92  ? 36   TYR D CG  1 
ATOM   10884 C  CD1 . TYR D  2  18  ? -11.895 -5.937  -40.734 1.00 66.36  ? 36   TYR D CD1 1 
ATOM   10885 C  CD2 . TYR D  2  18  ? -9.524  -6.160  -40.978 1.00 66.35  ? 36   TYR D CD2 1 
ATOM   10886 C  CE1 . TYR D  2  18  ? -12.057 -7.287  -41.090 1.00 65.61  ? 36   TYR D CE1 1 
ATOM   10887 C  CE2 . TYR D  2  18  ? -9.674  -7.507  -41.333 1.00 65.74  ? 36   TYR D CE2 1 
ATOM   10888 C  CZ  . TYR D  2  18  ? -10.940 -8.065  -41.385 1.00 65.92  ? 36   TYR D CZ  1 
ATOM   10889 O  OH  . TYR D  2  18  ? -11.078 -9.405  -41.702 1.00 64.92  ? 36   TYR D OH  1 
ATOM   10890 N  N   . CYS D  2  19  ? -8.883  -2.028  -38.242 1.00 74.77  ? 37   CYS D N   1 
ATOM   10891 C  CA  . CYS D  2  19  ? -8.301  -0.718  -37.968 1.00 78.24  ? 37   CYS D CA  1 
ATOM   10892 C  C   . CYS D  2  19  ? -7.082  -0.500  -38.853 1.00 79.57  ? 37   CYS D C   1 
ATOM   10893 O  O   . CYS D  2  19  ? -6.220  0.335   -38.558 1.00 80.07  ? 37   CYS D O   1 
ATOM   10894 C  CB  . CYS D  2  19  ? -7.902  -0.547  -36.488 1.00 78.71  ? 37   CYS D CB  1 
ATOM   10895 S  SG  . CYS D  2  19  ? -7.273  -2.009  -35.578 1.00 86.72  ? 37   CYS D SG  1 
ATOM   10896 N  N   . ASP D  2  20  ? -7.011  -1.259  -39.941 1.00 81.27  ? 38   ASP D N   1 
ATOM   10897 C  CA  . ASP D  2  20  ? -5.897  -1.132  -40.870 1.00 83.41  ? 38   ASP D CA  1 
ATOM   10898 C  C   . ASP D  2  20  ? -6.425  -0.927  -42.279 1.00 84.59  ? 38   ASP D C   1 
ATOM   10899 O  O   . ASP D  2  20  ? -7.586  -1.218  -42.570 1.00 84.79  ? 38   ASP D O   1 
ATOM   10900 C  CB  . ASP D  2  20  ? -4.988  -2.372  -40.809 1.00 83.64  ? 38   ASP D CB  1 
ATOM   10901 C  CG  . ASP D  2  20  ? -5.683  -3.650  -41.272 1.00 84.45  ? 38   ASP D CG  1 
ATOM   10902 O  OD1 . ASP D  2  20  ? -6.929  -3.676  -41.292 1.00 85.67  ? 38   ASP D OD1 1 
ATOM   10903 O  OD2 . ASP D  2  20  ? -4.976  -4.632  -41.605 1.00 82.97  ? 38   ASP D OD2 1 
ATOM   10904 N  N   . LYS D  2  21  ? -5.567  -0.405  -43.147 1.00 86.29  ? 39   LYS D N   1 
ATOM   10905 C  CA  . LYS D  2  21  ? -5.930  -0.149  -44.537 1.00 87.67  ? 39   LYS D CA  1 
ATOM   10906 C  C   . LYS D  2  21  ? -6.410  -1.434  -45.241 1.00 87.86  ? 39   LYS D C   1 
ATOM   10907 O  O   . LYS D  2  21  ? -7.598  -1.578  -45.532 1.00 87.04  ? 39   LYS D O   1 
ATOM   10908 C  CB  . LYS D  2  21  ? -4.733  0.464   -45.277 1.00 88.34  ? 39   LYS D CB  1 
ATOM   10909 C  CG  . LYS D  2  21  ? -4.224  1.806   -44.701 1.00 89.99  ? 39   LYS D CG  1 
ATOM   10910 C  CD  . LYS D  2  21  ? -3.086  1.647   -43.661 1.00 90.33  ? 39   LYS D CD  1 
ATOM   10911 C  CE  . LYS D  2  21  ? -3.586  1.725   -42.212 1.00 89.49  ? 39   LYS D CE  1 
ATOM   10912 N  NZ  . LYS D  2  21  ? -2.473  1.729   -41.220 1.00 87.33  ? 39   LYS D NZ  1 
ATOM   10913 N  N   . MET D  2  22  ? -5.487  -2.359  -45.511 1.00 88.24  ? 40   MET D N   1 
ATOM   10914 C  CA  . MET D  2  22  ? -5.816  -3.638  -46.157 1.00 88.07  ? 40   MET D CA  1 
ATOM   10915 C  C   . MET D  2  22  ? -6.662  -4.443  -45.176 1.00 86.75  ? 40   MET D C   1 
ATOM   10916 O  O   . MET D  2  22  ? -6.294  -4.580  -44.012 1.00 88.20  ? 40   MET D O   1 
ATOM   10917 C  CB  . MET D  2  22  ? -4.532  -4.418  -46.472 1.00 91.02  ? 40   MET D CB  1 
ATOM   10918 C  CG  . MET D  2  22  ? -3.766  -3.967  -47.723 1.00 96.03  ? 40   MET D CG  1 
ATOM   10919 S  SD  . MET D  2  22  ? -3.221  -2.222  -47.770 1.00 103.00 ? 40   MET D SD  1 
ATOM   10920 C  CE  . MET D  2  22  ? -4.279  -1.562  -49.160 1.00 99.71  ? 40   MET D CE  1 
ATOM   10921 N  N   . GLN D  2  23  ? -7.782  -4.995  -45.619 1.00 84.09  ? 41   GLN D N   1 
ATOM   10922 C  CA  . GLN D  2  23  ? -8.613  -5.737  -44.677 1.00 81.89  ? 41   GLN D CA  1 
ATOM   10923 C  C   . GLN D  2  23  ? -8.701  -7.230  -44.926 1.00 79.96  ? 41   GLN D C   1 
ATOM   10924 O  O   . GLN D  2  23  ? -9.785  -7.785  -45.073 1.00 79.43  ? 41   GLN D O   1 
ATOM   10925 C  CB  . GLN D  2  23  ? -10.013 -5.133  -44.634 1.00 82.59  ? 41   GLN D CB  1 
ATOM   10926 C  CG  . GLN D  2  23  ? -10.024 -3.686  -44.163 1.00 84.27  ? 41   GLN D CG  1 
ATOM   10927 C  CD  . GLN D  2  23  ? -11.371 -3.028  -44.360 1.00 85.72  ? 41   GLN D CD  1 
ATOM   10928 O  OE1 . GLN D  2  23  ? -12.370 -3.441  -43.769 1.00 86.50  ? 41   GLN D OE1 1 
ATOM   10929 N  NE2 . GLN D  2  23  ? -11.408 -1.998  -45.206 1.00 87.58  ? 41   GLN D NE2 1 
ATOM   10930 N  N   . TYR D  2  24  ? -7.542  -7.873  -44.949 1.00 78.62  ? 42   TYR D N   1 
ATOM   10931 C  CA  . TYR D  2  24  ? -7.446  -9.310  -45.169 1.00 76.39  ? 42   TYR D CA  1 
ATOM   10932 C  C   . TYR D  2  24  ? -8.375  -10.052 -44.207 1.00 75.24  ? 42   TYR D C   1 
ATOM   10933 O  O   . TYR D  2  24  ? -8.310  -9.862  -42.989 1.00 75.61  ? 42   TYR D O   1 
ATOM   10934 C  CB  . TYR D  2  24  ? -6.002  -9.763  -44.952 1.00 76.53  ? 42   TYR D CB  1 
ATOM   10935 C  CG  . TYR D  2  24  ? -4.941  -8.941  -45.684 1.00 76.06  ? 42   TYR D CG  1 
ATOM   10936 C  CD1 . TYR D  2  24  ? -4.023  -8.154  -44.976 1.00 76.01  ? 42   TYR D CD1 1 
ATOM   10937 C  CD2 . TYR D  2  24  ? -4.817  -8.997  -47.072 1.00 74.35  ? 42   TYR D CD2 1 
ATOM   10938 C  CE1 . TYR D  2  24  ? -3.008  -7.457  -45.630 1.00 74.89  ? 42   TYR D CE1 1 
ATOM   10939 C  CE2 . TYR D  2  24  ? -3.808  -8.302  -47.731 1.00 74.80  ? 42   TYR D CE2 1 
ATOM   10940 C  CZ  . TYR D  2  24  ? -2.903  -7.537  -47.005 1.00 75.34  ? 42   TYR D CZ  1 
ATOM   10941 O  OH  . TYR D  2  24  ? -1.867  -6.889  -47.653 1.00 76.33  ? 42   TYR D OH  1 
ATOM   10942 N  N   . PRO D  2  25  ? -9.245  -10.919 -44.741 1.00 73.57  ? 43   PRO D N   1 
ATOM   10943 C  CA  . PRO D  2  25  ? -10.210 -11.703 -43.956 1.00 72.85  ? 43   PRO D CA  1 
ATOM   10944 C  C   . PRO D  2  25  ? -9.646  -12.724 -42.964 1.00 72.52  ? 43   PRO D C   1 
ATOM   10945 O  O   . PRO D  2  25  ? -8.606  -13.330 -43.214 1.00 72.40  ? 43   PRO D O   1 
ATOM   10946 C  CB  . PRO D  2  25  ? -11.060 -12.368 -45.035 1.00 71.76  ? 43   PRO D CB  1 
ATOM   10947 C  CG  . PRO D  2  25  ? -10.088 -12.570 -46.144 1.00 70.94  ? 43   PRO D CG  1 
ATOM   10948 C  CD  . PRO D  2  25  ? -9.344  -11.251 -46.173 1.00 71.92  ? 43   PRO D CD  1 
ATOM   10949 N  N   . ILE D  2  26  ? -10.337 -12.900 -41.836 1.00 72.57  ? 44   ILE D N   1 
ATOM   10950 C  CA  . ILE D  2  26  ? -9.930  -13.875 -40.813 1.00 71.47  ? 44   ILE D CA  1 
ATOM   10951 C  C   . ILE D  2  26  ? -11.149 -14.618 -40.304 1.00 70.22  ? 44   ILE D C   1 
ATOM   10952 O  O   . ILE D  2  26  ? -12.252 -14.072 -40.267 1.00 71.53  ? 44   ILE D O   1 
ATOM   10953 C  CB  . ILE D  2  26  ? -9.319  -13.240 -39.540 1.00 71.63  ? 44   ILE D CB  1 
ATOM   10954 C  CG1 . ILE D  2  26  ? -8.737  -11.864 -39.830 1.00 73.97  ? 44   ILE D CG1 1 
ATOM   10955 C  CG2 . ILE D  2  26  ? -8.230  -14.138 -38.996 1.00 69.77  ? 44   ILE D CG2 1 
ATOM   10956 C  CD1 . ILE D  2  26  ? -8.221  -11.185 -38.576 1.00 75.89  ? 44   ILE D CD1 1 
ATOM   10957 N  N   . SER D  2  27  ? -10.934 -15.861 -39.900 1.00 68.27  ? 45   SER D N   1 
ATOM   10958 C  CA  . SER D  2  27  ? -11.993 -16.685 -39.337 1.00 67.08  ? 45   SER D CA  1 
ATOM   10959 C  C   . SER D  2  27  ? -11.682 -16.828 -37.830 1.00 66.85  ? 45   SER D C   1 
ATOM   10960 O  O   . SER D  2  27  ? -10.611 -17.305 -37.452 1.00 66.86  ? 45   SER D O   1 
ATOM   10961 C  CB  . SER D  2  27  ? -12.007 -18.045 -40.023 1.00 66.03  ? 45   SER D CB  1 
ATOM   10962 O  OG  . SER D  2  27  ? -12.927 -18.911 -39.395 1.00 67.15  ? 45   SER D OG  1 
ATOM   10963 N  N   . ILE D  2  28  ? -12.613 -16.413 -36.973 1.00 66.20  ? 46   ILE D N   1 
ATOM   10964 C  CA  . ILE D  2  28  ? -12.385 -16.458 -35.529 1.00 64.74  ? 46   ILE D CA  1 
ATOM   10965 C  C   . ILE D  2  28  ? -13.521 -17.070 -34.734 1.00 64.55  ? 46   ILE D C   1 
ATOM   10966 O  O   . ILE D  2  28  ? -14.579 -16.468 -34.608 1.00 63.75  ? 46   ILE D O   1 
ATOM   10967 C  CB  . ILE D  2  28  ? -12.157 -15.044 -34.996 1.00 63.46  ? 46   ILE D CB  1 
ATOM   10968 C  CG1 . ILE D  2  28  ? -10.989 -14.399 -35.736 1.00 61.27  ? 46   ILE D CG1 1 
ATOM   10969 C  CG2 . ILE D  2  28  ? -11.929 -15.085 -33.508 1.00 63.62  ? 46   ILE D CG2 1 
ATOM   10970 C  CD1 . ILE D  2  28  ? -10.831 -12.952 -35.420 1.00 61.42  ? 46   ILE D CD1 1 
ATOM   10971 N  N   . ASN D  2  29  ? -13.289 -18.256 -34.176 1.00 66.71  ? 47   ASN D N   1 
ATOM   10972 C  CA  . ASN D  2  29  ? -14.313 -18.954 -33.391 1.00 69.05  ? 47   ASN D CA  1 
ATOM   10973 C  C   . ASN D  2  29  ? -13.868 -19.208 -31.968 1.00 68.74  ? 47   ASN D C   1 
ATOM   10974 O  O   . ASN D  2  29  ? -12.723 -19.560 -31.720 1.00 70.16  ? 47   ASN D O   1 
ATOM   10975 C  CB  . ASN D  2  29  ? -14.687 -20.284 -34.042 1.00 71.31  ? 47   ASN D CB  1 
ATOM   10976 C  CG  . ASN D  2  29  ? -15.171 -20.109 -35.471 1.00 74.96  ? 47   ASN D CG  1 
ATOM   10977 O  OD1 . ASN D  2  29  ? -14.380 -19.825 -36.386 1.00 77.35  ? 47   ASN D OD1 1 
ATOM   10978 N  ND2 . ASN D  2  29  ? -16.473 -20.258 -35.671 1.00 75.27  ? 47   ASN D ND2 1 
ATOM   10979 N  N   . VAL D  2  30  ? -14.786 -19.037 -31.032 1.00 68.17  ? 48   VAL D N   1 
ATOM   10980 C  CA  . VAL D  2  30  ? -14.471 -19.209 -29.630 1.00 67.98  ? 48   VAL D CA  1 
ATOM   10981 C  C   . VAL D  2  30  ? -15.471 -20.194 -29.020 1.00 67.76  ? 48   VAL D C   1 
ATOM   10982 O  O   . VAL D  2  30  ? -16.666 -19.913 -28.968 1.00 67.90  ? 48   VAL D O   1 
ATOM   10983 C  CB  . VAL D  2  30  ? -14.540 -17.832 -28.906 1.00 67.94  ? 48   VAL D CB  1 
ATOM   10984 C  CG1 . VAL D  2  30  ? -14.032 -17.956 -27.491 1.00 69.40  ? 48   VAL D CG1 1 
ATOM   10985 C  CG2 . VAL D  2  30  ? -13.713 -16.800 -29.661 1.00 67.10  ? 48   VAL D CG2 1 
ATOM   10986 N  N   . ASN D  2  31  ? -14.985 -21.350 -28.567 1.00 67.37  ? 49   ASN D N   1 
ATOM   10987 C  CA  . ASN D  2  31  ? -15.860 -22.369 -27.983 1.00 66.73  ? 49   ASN D CA  1 
ATOM   10988 C  C   . ASN D  2  31  ? -15.409 -22.974 -26.657 1.00 66.09  ? 49   ASN D C   1 
ATOM   10989 O  O   . ASN D  2  31  ? -14.401 -23.681 -26.598 1.00 65.17  ? 49   ASN D O   1 
ATOM   10990 C  CB  . ASN D  2  31  ? -16.073 -23.500 -28.979 1.00 66.59  ? 49   ASN D CB  1 
ATOM   10991 C  CG  . ASN D  2  31  ? -16.805 -23.049 -30.200 1.00 67.58  ? 49   ASN D CG  1 
ATOM   10992 O  OD1 . ASN D  2  31  ? -16.195 -22.690 -31.210 1.00 68.34  ? 49   ASN D OD1 1 
ATOM   10993 N  ND2 . ASN D  2  31  ? -18.131 -23.038 -30.116 1.00 68.20  ? 49   ASN D ND2 1 
ATOM   10994 N  N   . PRO D  2  32  ? -16.173 -22.729 -25.574 1.00 65.75  ? 50   PRO D N   1 
ATOM   10995 C  CA  . PRO D  2  32  ? -17.406 -21.932 -25.514 1.00 65.65  ? 50   PRO D CA  1 
ATOM   10996 C  C   . PRO D  2  32  ? -17.088 -20.443 -25.528 1.00 66.27  ? 50   PRO D C   1 
ATOM   10997 O  O   . PRO D  2  32  ? -15.927 -20.062 -25.485 1.00 66.17  ? 50   PRO D O   1 
ATOM   10998 C  CB  . PRO D  2  32  ? -18.026 -22.377 -24.203 1.00 64.20  ? 50   PRO D CB  1 
ATOM   10999 C  CG  . PRO D  2  32  ? -16.827 -22.586 -23.353 1.00 64.50  ? 50   PRO D CG  1 
ATOM   11000 C  CD  . PRO D  2  32  ? -15.882 -23.328 -24.261 1.00 64.61  ? 50   PRO D CD  1 
ATOM   11001 N  N   . CYS D  2  33  ? -18.106 -19.597 -25.574 1.00 67.98  ? 51   CYS D N   1 
ATOM   11002 C  CA  . CYS D  2  33  ? -17.847 -18.169 -25.602 1.00 71.03  ? 51   CYS D CA  1 
ATOM   11003 C  C   . CYS D  2  33  ? -17.263 -17.653 -24.297 1.00 71.65  ? 51   CYS D C   1 
ATOM   11004 O  O   . CYS D  2  33  ? -17.633 -18.091 -23.208 1.00 71.51  ? 51   CYS D O   1 
ATOM   11005 C  CB  . CYS D  2  33  ? -19.113 -17.386 -25.939 1.00 73.23  ? 51   CYS D CB  1 
ATOM   11006 S  SG  . CYS D  2  33  ? -18.820 -15.650 -26.461 1.00 78.09  ? 51   CYS D SG  1 
ATOM   11007 N  N   . ILE D  2  34  ? -16.339 -16.709 -24.432 1.00 72.75  ? 52   ILE D N   1 
ATOM   11008 C  CA  . ILE D  2  34  ? -15.664 -16.096 -23.302 1.00 73.63  ? 52   ILE D CA  1 
ATOM   11009 C  C   . ILE D  2  34  ? -16.623 -15.596 -22.244 1.00 75.40  ? 52   ILE D C   1 
ATOM   11010 O  O   . ILE D  2  34  ? -17.687 -15.067 -22.556 1.00 76.45  ? 52   ILE D O   1 
ATOM   11011 C  CB  . ILE D  2  34  ? -14.840 -14.881 -23.745 1.00 72.27  ? 52   ILE D CB  1 
ATOM   11012 C  CG1 . ILE D  2  34  ? -13.843 -15.292 -24.822 1.00 72.51  ? 52   ILE D CG1 1 
ATOM   11013 C  CG2 . ILE D  2  34  ? -14.125 -14.275 -22.561 1.00 72.01  ? 52   ILE D CG2 1 
ATOM   11014 C  CD1 . ILE D  2  34  ? -12.718 -16.154 -24.329 1.00 71.60  ? 52   ILE D CD1 1 
ATOM   11015 N  N   . GLU D  2  35  ? -16.235 -15.775 -20.989 1.00 77.19  ? 53   GLU D N   1 
ATOM   11016 C  CA  . GLU D  2  35  ? -17.011 -15.282 -19.861 1.00 79.57  ? 53   GLU D CA  1 
ATOM   11017 C  C   . GLU D  2  35  ? -15.989 -14.553 -19.004 1.00 78.57  ? 53   GLU D C   1 
ATOM   11018 O  O   . GLU D  2  35  ? -15.024 -15.156 -18.530 1.00 77.95  ? 53   GLU D O   1 
ATOM   11019 C  CB  . GLU D  2  35  ? -17.660 -16.428 -19.085 1.00 82.50  ? 53   GLU D CB  1 
ATOM   11020 C  CG  . GLU D  2  35  ? -19.096 -16.688 -19.506 1.00 87.54  ? 53   GLU D CG  1 
ATOM   11021 C  CD  . GLU D  2  35  ? -19.744 -17.834 -18.746 1.00 90.75  ? 53   GLU D CD  1 
ATOM   11022 O  OE1 . GLU D  2  35  ? -19.328 -18.997 -18.948 1.00 92.97  ? 53   GLU D OE1 1 
ATOM   11023 O  OE2 . GLU D  2  35  ? -20.672 -17.574 -17.945 1.00 93.21  ? 53   GLU D OE2 1 
ATOM   11024 N  N   . LEU D  2  36  ? -16.180 -13.249 -18.833 1.00 77.28  ? 54   LEU D N   1 
ATOM   11025 C  CA  . LEU D  2  36  ? -15.230 -12.455 -18.063 1.00 75.44  ? 54   LEU D CA  1 
ATOM   11026 C  C   . LEU D  2  36  ? -15.126 -12.839 -16.590 1.00 74.64  ? 54   LEU D C   1 
ATOM   11027 O  O   . LEU D  2  36  ? -14.236 -12.372 -15.883 1.00 72.45  ? 54   LEU D O   1 
ATOM   11028 C  CB  . LEU D  2  36  ? -15.552 -10.968 -18.218 1.00 73.79  ? 54   LEU D CB  1 
ATOM   11029 C  CG  . LEU D  2  36  ? -14.850 -10.337 -19.424 1.00 72.09  ? 54   LEU D CG  1 
ATOM   11030 C  CD1 . LEU D  2  36  ? -15.190 -11.109 -20.677 1.00 72.06  ? 54   LEU D CD1 1 
ATOM   11031 C  CD2 . LEU D  2  36  ? -15.256 -8.892  -19.563 1.00 71.18  ? 54   LEU D CD2 1 
ATOM   11032 N  N   . LYS D  2  37  ? -16.034 -13.690 -16.129 1.00 74.66  ? 55   LYS D N   1 
ATOM   11033 C  CA  . LYS D  2  37  ? -16.003 -14.139 -14.748 1.00 73.99  ? 55   LYS D CA  1 
ATOM   11034 C  C   . LYS D  2  37  ? -15.003 -15.280 -14.665 1.00 72.26  ? 55   LYS D C   1 
ATOM   11035 O  O   . LYS D  2  37  ? -14.712 -15.795 -13.599 1.00 72.17  ? 55   LYS D O   1 
ATOM   11036 C  CB  . LYS D  2  37  ? -17.399 -14.599 -14.299 1.00 76.20  ? 55   LYS D CB  1 
ATOM   11037 C  CG  . LYS D  2  37  ? -18.119 -15.569 -15.254 1.00 80.23  ? 55   LYS D CG  1 
ATOM   11038 C  CD  . LYS D  2  37  ? -17.752 -17.047 -15.032 1.00 82.90  ? 55   LYS D CD  1 
ATOM   11039 C  CE  . LYS D  2  37  ? -18.278 -17.568 -13.690 1.00 84.49  ? 55   LYS D CE  1 
ATOM   11040 N  NZ  . LYS D  2  37  ? -19.755 -17.398 -13.566 1.00 85.30  ? 55   LYS D NZ  1 
ATOM   11041 N  N   . GLY D  2  38  ? -14.469 -15.664 -15.810 1.00 70.98  ? 56   GLY D N   1 
ATOM   11042 C  CA  . GLY D  2  38  ? -13.512 -16.745 -15.843 1.00 70.58  ? 56   GLY D CA  1 
ATOM   11043 C  C   . GLY D  2  38  ? -14.026 -17.835 -16.753 1.00 70.90  ? 56   GLY D C   1 
ATOM   11044 O  O   . GLY D  2  38  ? -15.148 -18.312 -16.573 1.00 71.95  ? 56   GLY D O   1 
ATOM   11045 N  N   . SER D  2  39  ? -13.215 -18.230 -17.733 1.00 70.61  ? 57   SER D N   1 
ATOM   11046 C  CA  . SER D  2  39  ? -13.597 -19.277 -18.680 1.00 71.14  ? 57   SER D CA  1 
ATOM   11047 C  C   . SER D  2  39  ? -12.378 -19.957 -19.301 1.00 71.04  ? 57   SER D C   1 
ATOM   11048 O  O   . SER D  2  39  ? -11.252 -19.495 -19.142 1.00 71.19  ? 57   SER D O   1 
ATOM   11049 C  CB  . SER D  2  39  ? -14.470 -18.695 -19.795 1.00 70.80  ? 57   SER D CB  1 
ATOM   11050 O  OG  . SER D  2  39  ? -13.747 -17.749 -20.560 1.00 70.53  ? 57   SER D OG  1 
ATOM   11051 N  N   . LYS D  2  40  ? -12.612 -21.069 -19.990 1.00 70.60  ? 58   LYS D N   1 
ATOM   11052 C  CA  . LYS D  2  40  ? -11.540 -21.799 -20.645 1.00 70.33  ? 58   LYS D CA  1 
ATOM   11053 C  C   . LYS D  2  40  ? -12.136 -22.591 -21.800 1.00 70.52  ? 58   LYS D C   1 
ATOM   11054 O  O   . LYS D  2  40  ? -13.045 -23.405 -21.603 1.00 72.35  ? 58   LYS D O   1 
ATOM   11055 C  CB  . LYS D  2  40  ? -10.804 -22.714 -19.652 1.00 69.89  ? 58   LYS D CB  1 
ATOM   11056 C  CG  . LYS D  2  40  ? -11.561 -23.919 -19.145 1.00 71.95  ? 58   LYS D CG  1 
ATOM   11057 C  CD  . LYS D  2  40  ? -11.164 -25.174 -19.907 1.00 74.91  ? 58   LYS D CD  1 
ATOM   11058 C  CE  . LYS D  2  40  ? -11.503 -26.449 -19.128 1.00 77.07  ? 58   LYS D CE  1 
ATOM   11059 N  NZ  . LYS D  2  40  ? -12.952 -26.588 -18.752 1.00 79.22  ? 58   LYS D NZ  1 
ATOM   11060 N  N   . GLY D  2  41  ? -11.638 -22.321 -23.006 1.00 68.28  ? 59   GLY D N   1 
ATOM   11061 C  CA  . GLY D  2  41  ? -12.132 -23.000 -24.188 1.00 65.61  ? 59   GLY D CA  1 
ATOM   11062 C  C   . GLY D  2  41  ? -11.105 -23.065 -25.295 1.00 63.83  ? 59   GLY D C   1 
ATOM   11063 O  O   . GLY D  2  41  ? -9.921  -22.875 -25.035 1.00 64.70  ? 59   GLY D O   1 
ATOM   11064 N  N   . LEU D  2  42  ? -11.558 -23.340 -26.521 1.00 61.53  ? 60   LEU D N   1 
ATOM   11065 C  CA  . LEU D  2  42  ? -10.678 -23.431 -27.687 1.00 59.00  ? 60   LEU D CA  1 
ATOM   11066 C  C   . LEU D  2  42  ? -10.957 -22.288 -28.638 1.00 59.29  ? 60   LEU D C   1 
ATOM   11067 O  O   . LEU D  2  42  ? -12.109 -21.982 -28.925 1.00 59.56  ? 60   LEU D O   1 
ATOM   11068 C  CB  . LEU D  2  42  ? -10.900 -24.735 -28.440 1.00 57.00  ? 60   LEU D CB  1 
ATOM   11069 C  CG  . LEU D  2  42  ? -10.764 -26.050 -27.678 1.00 57.23  ? 60   LEU D CG  1 
ATOM   11070 C  CD1 . LEU D  2  42  ? -11.095 -27.178 -28.620 1.00 56.78  ? 60   LEU D CD1 1 
ATOM   11071 C  CD2 . LEU D  2  42  ? -9.362  -26.218 -27.129 1.00 56.10  ? 60   LEU D CD2 1 
ATOM   11072 N  N   . LEU D  2  43  ? -9.890  -21.658 -29.119 1.00 59.90  ? 61   LEU D N   1 
ATOM   11073 C  CA  . LEU D  2  43  ? -9.974  -20.549 -30.064 1.00 59.88  ? 61   LEU D CA  1 
ATOM   11074 C  C   . LEU D  2  43  ? -9.506  -21.035 -31.436 1.00 60.53  ? 61   LEU D C   1 
ATOM   11075 O  O   . LEU D  2  43  ? -8.311  -21.213 -31.654 1.00 59.88  ? 61   LEU D O   1 
ATOM   11076 C  CB  . LEU D  2  43  ? -9.071  -19.406 -29.603 1.00 59.62  ? 61   LEU D CB  1 
ATOM   11077 C  CG  . LEU D  2  43  ? -8.693  -18.351 -30.651 1.00 59.93  ? 61   LEU D CG  1 
ATOM   11078 C  CD1 . LEU D  2  43  ? -9.924  -17.562 -31.074 1.00 59.99  ? 61   LEU D CD1 1 
ATOM   11079 C  CD2 . LEU D  2  43  ? -7.640  -17.417 -30.073 1.00 58.32  ? 61   LEU D CD2 1 
ATOM   11080 N  N   . HIS D  2  44  ? -10.440 -21.260 -32.354 1.00 62.08  ? 62   HIS D N   1 
ATOM   11081 C  CA  . HIS D  2  44  ? -10.082 -21.730 -33.684 1.00 64.48  ? 62   HIS D CA  1 
ATOM   11082 C  C   . HIS D  2  44  ? -9.931  -20.593 -34.682 1.00 63.14  ? 62   HIS D C   1 
ATOM   11083 O  O   . HIS D  2  44  ? -10.841 -19.796 -34.863 1.00 63.68  ? 62   HIS D O   1 
ATOM   11084 C  CB  . HIS D  2  44  ? -11.121 -22.721 -34.195 1.00 70.16  ? 62   HIS D CB  1 
ATOM   11085 C  CG  . HIS D  2  44  ? -10.796 -23.292 -35.544 1.00 77.92  ? 62   HIS D CG  1 
ATOM   11086 N  ND1 . HIS D  2  44  ? -10.896 -22.558 -36.709 1.00 80.90  ? 62   HIS D ND1 1 
ATOM   11087 C  CD2 . HIS D  2  44  ? -10.357 -24.523 -35.910 1.00 79.07  ? 62   HIS D CD2 1 
ATOM   11088 C  CE1 . HIS D  2  44  ? -10.534 -23.312 -37.735 1.00 81.96  ? 62   HIS D CE1 1 
ATOM   11089 N  NE2 . HIS D  2  44  ? -10.203 -24.509 -37.278 1.00 81.15  ? 62   HIS D NE2 1 
ATOM   11090 N  N   . ILE D  2  45  ? -8.776  -20.532 -35.335 1.00 61.59  ? 63   ILE D N   1 
ATOM   11091 C  CA  . ILE D  2  45  ? -8.505  -19.487 -36.306 1.00 60.68  ? 63   ILE D CA  1 
ATOM   11092 C  C   . ILE D  2  45  ? -8.124  -20.079 -37.640 1.00 60.89  ? 63   ILE D C   1 
ATOM   11093 O  O   . ILE D  2  45  ? -7.520  -21.146 -37.699 1.00 61.28  ? 63   ILE D O   1 
ATOM   11094 C  CB  . ILE D  2  45  ? -7.337  -18.587 -35.856 1.00 59.63  ? 63   ILE D CB  1 
ATOM   11095 C  CG1 . ILE D  2  45  ? -7.687  -17.899 -34.545 1.00 59.04  ? 63   ILE D CG1 1 
ATOM   11096 C  CG2 . ILE D  2  45  ? -7.035  -17.547 -36.922 1.00 58.03  ? 63   ILE D CG2 1 
ATOM   11097 C  CD1 . ILE D  2  45  ? -6.514  -17.259 -33.891 1.00 58.39  ? 63   ILE D CD1 1 
ATOM   11098 N  N   . PHE D  2  46  ? -8.502  -19.384 -38.706 1.00 60.56  ? 64   PHE D N   1 
ATOM   11099 C  CA  . PHE D  2  46  ? -8.178  -19.780 -40.066 1.00 60.45  ? 64   PHE D CA  1 
ATOM   11100 C  C   . PHE D  2  46  ? -7.744  -18.477 -40.699 1.00 60.89  ? 64   PHE D C   1 
ATOM   11101 O  O   . PHE D  2  46  ? -8.505  -17.509 -40.710 1.00 60.12  ? 64   PHE D O   1 
ATOM   11102 C  CB  . PHE D  2  46  ? -9.391  -20.312 -40.812 1.00 59.87  ? 64   PHE D CB  1 
ATOM   11103 C  CG  . PHE D  2  46  ? -9.075  -20.760 -42.207 1.00 62.60  ? 64   PHE D CG  1 
ATOM   11104 C  CD1 . PHE D  2  46  ? -8.636  -22.063 -42.449 1.00 62.91  ? 64   PHE D CD1 1 
ATOM   11105 C  CD2 . PHE D  2  46  ? -9.174  -19.868 -43.286 1.00 63.37  ? 64   PHE D CD2 1 
ATOM   11106 C  CE1 . PHE D  2  46  ? -8.297  -22.477 -43.746 1.00 62.71  ? 64   PHE D CE1 1 
ATOM   11107 C  CE2 . PHE D  2  46  ? -8.838  -20.266 -44.589 1.00 62.16  ? 64   PHE D CE2 1 
ATOM   11108 C  CZ  . PHE D  2  46  ? -8.399  -21.574 -44.819 1.00 62.00  ? 64   PHE D CZ  1 
ATOM   11109 N  N   . TYR D  2  47  ? -6.526  -18.455 -41.224 1.00 61.36  ? 65   TYR D N   1 
ATOM   11110 C  CA  . TYR D  2  47  ? -5.975  -17.249 -41.818 1.00 61.77  ? 65   TYR D CA  1 
ATOM   11111 C  C   . TYR D  2  47  ? -4.951  -17.681 -42.833 1.00 63.39  ? 65   TYR D C   1 
ATOM   11112 O  O   . TYR D  2  47  ? -4.490  -18.817 -42.835 1.00 62.95  ? 65   TYR D O   1 
ATOM   11113 C  CB  . TYR D  2  47  ? -5.275  -16.412 -40.733 1.00 62.97  ? 65   TYR D CB  1 
ATOM   11114 C  CG  . TYR D  2  47  ? -4.922  -14.973 -41.085 1.00 62.85  ? 65   TYR D CG  1 
ATOM   11115 C  CD1 . TYR D  2  47  ? -5.906  -14.075 -41.496 1.00 63.59  ? 65   TYR D CD1 1 
ATOM   11116 C  CD2 . TYR D  2  47  ? -3.626  -14.486 -40.898 1.00 61.70  ? 65   TYR D CD2 1 
ATOM   11117 C  CE1 . TYR D  2  47  ? -5.619  -12.733 -41.705 1.00 64.36  ? 65   TYR D CE1 1 
ATOM   11118 C  CE2 . TYR D  2  47  ? -3.326  -13.145 -41.103 1.00 63.54  ? 65   TYR D CE2 1 
ATOM   11119 C  CZ  . TYR D  2  47  ? -4.330  -12.265 -41.509 1.00 64.93  ? 65   TYR D CZ  1 
ATOM   11120 O  OH  . TYR D  2  47  ? -4.077  -10.919 -41.737 1.00 65.80  ? 65   TYR D OH  1 
ATOM   11121 N  N   . ILE D  2  48  ? -4.586  -16.735 -43.681 1.00 64.83  ? 66   ILE D N   1 
ATOM   11122 C  CA  . ILE D  2  48  ? -3.600  -16.941 -44.722 1.00 64.50  ? 66   ILE D CA  1 
ATOM   11123 C  C   . ILE D  2  48  ? -2.897  -15.582 -44.691 1.00 65.02  ? 66   ILE D C   1 
ATOM   11124 O  O   . ILE D  2  48  ? -3.331  -14.633 -45.338 1.00 64.39  ? 66   ILE D O   1 
ATOM   11125 C  CB  . ILE D  2  48  ? -4.327  -17.231 -46.057 1.00 66.44  ? 66   ILE D CB  1 
ATOM   11126 C  CG1 . ILE D  2  48  ? -3.345  -17.252 -47.217 1.00 67.48  ? 66   ILE D CG1 1 
ATOM   11127 C  CG2 . ILE D  2  48  ? -5.437  -16.202 -46.284 1.00 68.32  ? 66   ILE D CG2 1 
ATOM   11128 C  CD1 . ILE D  2  48  ? -4.049  -17.469 -48.554 1.00 68.95  ? 66   ILE D CD1 1 
ATOM   11129 N  N   . PRO D  2  49  ? -1.818  -15.470 -43.891 1.00 65.29  ? 67   PRO D N   1 
ATOM   11130 C  CA  . PRO D  2  49  ? -1.030  -14.245 -43.722 1.00 64.37  ? 67   PRO D CA  1 
ATOM   11131 C  C   . PRO D  2  49  ? -0.447  -13.657 -45.005 1.00 66.43  ? 67   PRO D C   1 
ATOM   11132 O  O   . PRO D  2  49  ? -0.476  -14.290 -46.052 1.00 66.29  ? 67   PRO D O   1 
ATOM   11133 C  CB  . PRO D  2  49  ? 0.043   -14.673 -42.722 1.00 64.51  ? 67   PRO D CB  1 
ATOM   11134 C  CG  . PRO D  2  49  ? 0.274   -16.092 -43.086 1.00 63.24  ? 67   PRO D CG  1 
ATOM   11135 C  CD  . PRO D  2  49  ? -1.138  -16.605 -43.241 1.00 64.08  ? 67   PRO D CD  1 
ATOM   11136 N  N   . ARG D  2  50  ? 0.063   -12.432 -44.924 1.00 68.61  ? 68   ARG D N   1 
ATOM   11137 C  CA  . ARG D  2  50  ? 0.666   -11.771 -46.081 1.00 69.86  ? 68   ARG D CA  1 
ATOM   11138 C  C   . ARG D  2  50  ? 2.121   -11.489 -45.714 1.00 71.19  ? 68   ARG D C   1 
ATOM   11139 O  O   . ARG D  2  50  ? 2.847   -10.799 -46.433 1.00 72.10  ? 68   ARG D O   1 
ATOM   11140 C  CB  . ARG D  2  50  ? -0.069  -10.462 -46.385 1.00 70.54  ? 68   ARG D CB  1 
ATOM   11141 C  CG  . ARG D  2  50  ? -1.589  -10.567 -46.321 1.00 70.92  ? 68   ARG D CG  1 
ATOM   11142 C  CD  . ARG D  2  50  ? -2.229  -11.151 -47.578 1.00 70.82  ? 68   ARG D CD  1 
ATOM   11143 N  NE  . ARG D  2  50  ? -3.415  -11.950 -47.248 1.00 72.27  ? 68   ARG D NE  1 
ATOM   11144 C  CZ  . ARG D  2  50  ? -4.426  -12.200 -48.080 1.00 73.43  ? 68   ARG D CZ  1 
ATOM   11145 N  NH1 . ARG D  2  50  ? -4.423  -11.703 -49.313 1.00 74.42  ? 68   ARG D NH1 1 
ATOM   11146 N  NH2 . ARG D  2  50  ? -5.431  -12.978 -47.693 1.00 73.98  ? 68   ARG D NH2 1 
ATOM   11147 N  N   . ARG D  2  51  ? 2.518   -12.028 -44.567 1.00 72.08  ? 69   ARG D N   1 
ATOM   11148 C  CA  . ARG D  2  51  ? 3.869   -11.900 -44.039 1.00 73.14  ? 69   ARG D CA  1 
ATOM   11149 C  C   . ARG D  2  51  ? 4.139   -13.193 -43.289 1.00 72.04  ? 69   ARG D C   1 
ATOM   11150 O  O   . ARG D  2  51  ? 3.257   -14.043 -43.187 1.00 71.89  ? 69   ARG D O   1 
ATOM   11151 C  CB  . ARG D  2  51  ? 3.985   -10.710 -43.079 1.00 74.36  ? 69   ARG D CB  1 
ATOM   11152 C  CG  . ARG D  2  51  ? 4.122   -9.365  -43.769 1.00 79.52  ? 69   ARG D CG  1 
ATOM   11153 C  CD  . ARG D  2  51  ? 4.307   -8.249  -42.750 1.00 84.17  ? 69   ARG D CD  1 
ATOM   11154 N  NE  . ARG D  2  51  ? 5.664   -7.694  -42.723 1.00 89.21  ? 69   ARG D NE  1 
ATOM   11155 C  CZ  . ARG D  2  51  ? 6.776   -8.396  -42.495 1.00 90.90  ? 69   ARG D CZ  1 
ATOM   11156 N  NH1 . ARG D  2  51  ? 6.706   -9.703  -42.276 1.00 92.11  ? 69   ARG D NH1 1 
ATOM   11157 N  NH2 . ARG D  2  51  ? 7.963   -7.790  -42.471 1.00 91.29  ? 69   ARG D NH2 1 
ATOM   11158 N  N   . ASP D  2  52  ? 5.352   -13.354 -42.774 1.00 70.25  ? 70   ASP D N   1 
ATOM   11159 C  CA  . ASP D  2  52  ? 5.683   -14.554 -42.025 1.00 68.33  ? 70   ASP D CA  1 
ATOM   11160 C  C   . ASP D  2  52  ? 5.303   -14.326 -40.573 1.00 66.52  ? 70   ASP D C   1 
ATOM   11161 O  O   . ASP D  2  52  ? 5.476   -13.224 -40.053 1.00 66.05  ? 70   ASP D O   1 
ATOM   11162 C  CB  . ASP D  2  52  ? 7.175   -14.838 -42.143 1.00 70.01  ? 70   ASP D CB  1 
ATOM   11163 C  CG  . ASP D  2  52  ? 7.585   -15.214 -43.559 1.00 71.18  ? 70   ASP D CG  1 
ATOM   11164 O  OD1 . ASP D  2  52  ? 6.745   -15.061 -44.480 1.00 71.43  ? 70   ASP D OD1 1 
ATOM   11165 O  OD2 . ASP D  2  52  ? 8.748   -15.655 -43.740 1.00 70.67  ? 70   ASP D OD2 1 
ATOM   11166 N  N   . LEU D  2  53  ? 4.785   -15.357 -39.915 1.00 64.29  ? 71   LEU D N   1 
ATOM   11167 C  CA  . LEU D  2  53  ? 4.389   -15.208 -38.520 1.00 62.48  ? 71   LEU D CA  1 
ATOM   11168 C  C   . LEU D  2  53  ? 5.583   -15.257 -37.570 1.00 61.74  ? 71   LEU D C   1 
ATOM   11169 O  O   . LEU D  2  53  ? 5.439   -15.174 -36.356 1.00 61.24  ? 71   LEU D O   1 
ATOM   11170 C  CB  . LEU D  2  53  ? 3.344   -16.266 -38.156 1.00 60.90  ? 71   LEU D CB  1 
ATOM   11171 C  CG  . LEU D  2  53  ? 2.069   -16.169 -38.999 1.00 58.86  ? 71   LEU D CG  1 
ATOM   11172 C  CD1 . LEU D  2  53  ? 1.022   -17.089 -38.417 1.00 59.27  ? 71   LEU D CD1 1 
ATOM   11173 C  CD2 . LEU D  2  53  ? 1.556   -14.743 -39.018 1.00 56.95  ? 71   LEU D CD2 1 
ATOM   11174 N  N   . LYS D  2  54  ? 6.766   -15.381 -38.159 1.00 62.11  ? 72   LYS D N   1 
ATOM   11175 C  CA  . LYS D  2  54  ? 8.046   -15.409 -37.455 1.00 62.92  ? 72   LYS D CA  1 
ATOM   11176 C  C   . LYS D  2  54  ? 8.105   -14.290 -36.405 1.00 62.77  ? 72   LYS D C   1 
ATOM   11177 O  O   . LYS D  2  54  ? 8.006   -13.114 -36.739 1.00 62.24  ? 72   LYS D O   1 
ATOM   11178 C  CB  . LYS D  2  54  ? 9.145   -15.230 -38.510 1.00 65.27  ? 72   LYS D CB  1 
ATOM   11179 C  CG  . LYS D  2  54  ? 10.572  -15.154 -38.030 1.00 68.68  ? 72   LYS D CG  1 
ATOM   11180 C  CD  . LYS D  2  54  ? 11.487  -14.961 -39.244 1.00 72.43  ? 72   LYS D CD  1 
ATOM   11181 C  CE  . LYS D  2  54  ? 12.972  -14.846 -38.853 1.00 75.54  ? 72   LYS D CE  1 
ATOM   11182 N  NZ  . LYS D  2  54  ? 13.885  -14.643 -40.036 1.00 75.48  ? 72   LYS D NZ  1 
ATOM   11183 N  N   . GLN D  2  55  ? 8.252   -14.651 -35.135 1.00 63.40  ? 73   GLN D N   1 
ATOM   11184 C  CA  . GLN D  2  55  ? 8.314   -13.658 -34.054 1.00 64.64  ? 73   GLN D CA  1 
ATOM   11185 C  C   . GLN D  2  55  ? 7.096   -12.719 -33.942 1.00 64.31  ? 73   GLN D C   1 
ATOM   11186 O  O   . GLN D  2  55  ? 7.244   -11.496 -33.816 1.00 64.29  ? 73   GLN D O   1 
ATOM   11187 C  CB  . GLN D  2  55  ? 9.584   -12.817 -34.197 1.00 65.60  ? 73   GLN D CB  1 
ATOM   11188 C  CG  . GLN D  2  55  ? 10.856  -13.616 -34.014 1.00 68.40  ? 73   GLN D CG  1 
ATOM   11189 C  CD  . GLN D  2  55  ? 12.075  -12.907 -34.567 1.00 70.29  ? 73   GLN D CD  1 
ATOM   11190 O  OE1 . GLN D  2  55  ? 12.515  -11.888 -34.029 1.00 70.79  ? 73   GLN D OE1 1 
ATOM   11191 N  NE2 . GLN D  2  55  ? 12.633  -13.448 -35.653 1.00 71.30  ? 73   GLN D NE2 1 
ATOM   11192 N  N   . LEU D  2  56  ? 5.900   -13.304 -33.967 1.00 62.45  ? 74   LEU D N   1 
ATOM   11193 C  CA  . LEU D  2  56  ? 4.644   -12.568 -33.866 1.00 61.01  ? 74   LEU D CA  1 
ATOM   11194 C  C   . LEU D  2  56  ? 4.517   -11.924 -32.482 1.00 61.29  ? 74   LEU D C   1 
ATOM   11195 O  O   . LEU D  2  56  ? 5.196   -12.308 -31.539 1.00 61.21  ? 74   LEU D O   1 
ATOM   11196 C  CB  . LEU D  2  56  ? 3.480   -13.546 -34.057 1.00 59.73  ? 74   LEU D CB  1 
ATOM   11197 C  CG  . LEU D  2  56  ? 2.154   -13.156 -34.723 1.00 59.47  ? 74   LEU D CG  1 
ATOM   11198 C  CD1 . LEU D  2  56  ? 1.132   -14.254 -34.444 1.00 59.07  ? 74   LEU D CD1 1 
ATOM   11199 C  CD2 . LEU D  2  56  ? 1.638   -11.837 -34.202 1.00 58.55  ? 74   LEU D CD2 1 
ATOM   11200 N  N   . TYR D  2  57  ? 3.659   -10.921 -32.376 1.00 62.06  ? 75   TYR D N   1 
ATOM   11201 C  CA  . TYR D  2  57  ? 3.384   -10.270 -31.100 1.00 62.72  ? 75   TYR D CA  1 
ATOM   11202 C  C   . TYR D  2  57  ? 2.305   -9.220  -31.290 1.00 62.92  ? 75   TYR D C   1 
ATOM   11203 O  O   . TYR D  2  57  ? 2.244   -8.555  -32.322 1.00 64.09  ? 75   TYR D O   1 
ATOM   11204 C  CB  . TYR D  2  57  ? 4.647   -9.659  -30.459 1.00 63.24  ? 75   TYR D CB  1 
ATOM   11205 C  CG  . TYR D  2  57  ? 5.123   -8.308  -30.956 1.00 64.17  ? 75   TYR D CG  1 
ATOM   11206 C  CD1 . TYR D  2  57  ? 5.982   -8.207  -32.046 1.00 66.01  ? 75   TYR D CD1 1 
ATOM   11207 C  CD2 . TYR D  2  57  ? 4.797   -7.139  -30.271 1.00 64.21  ? 75   TYR D CD2 1 
ATOM   11208 C  CE1 . TYR D  2  57  ? 6.517   -6.973  -32.437 1.00 67.36  ? 75   TYR D CE1 1 
ATOM   11209 C  CE2 . TYR D  2  57  ? 5.321   -5.909  -30.654 1.00 65.83  ? 75   TYR D CE2 1 
ATOM   11210 C  CZ  . TYR D  2  57  ? 6.184   -5.833  -31.737 1.00 66.47  ? 75   TYR D CZ  1 
ATOM   11211 O  OH  . TYR D  2  57  ? 6.722   -4.632  -32.128 1.00 66.96  ? 75   TYR D OH  1 
ATOM   11212 N  N   . PHE D  2  58  ? 1.427   -9.107  -30.305 1.00 62.09  ? 76   PHE D N   1 
ATOM   11213 C  CA  . PHE D  2  58  ? 0.338   -8.161  -30.369 1.00 61.02  ? 76   PHE D CA  1 
ATOM   11214 C  C   . PHE D  2  58  ? 0.678   -6.949  -29.532 1.00 61.51  ? 76   PHE D C   1 
ATOM   11215 O  O   . PHE D  2  58  ? 1.418   -7.046  -28.565 1.00 62.85  ? 76   PHE D O   1 
ATOM   11216 C  CB  . PHE D  2  58  ? -0.933  -8.794  -29.804 1.00 60.33  ? 76   PHE D CB  1 
ATOM   11217 C  CG  . PHE D  2  58  ? -1.385  -10.030 -30.527 1.00 61.47  ? 76   PHE D CG  1 
ATOM   11218 C  CD1 . PHE D  2  58  ? -1.888  -11.111 -29.811 1.00 62.44  ? 76   PHE D CD1 1 
ATOM   11219 C  CD2 . PHE D  2  58  ? -1.356  -10.105 -31.916 1.00 61.87  ? 76   PHE D CD2 1 
ATOM   11220 C  CE1 . PHE D  2  58  ? -2.355  -12.256 -30.464 1.00 62.76  ? 76   PHE D CE1 1 
ATOM   11221 C  CE2 . PHE D  2  58  ? -1.822  -11.246 -32.583 1.00 62.61  ? 76   PHE D CE2 1 
ATOM   11222 C  CZ  . PHE D  2  58  ? -2.325  -12.323 -31.853 1.00 63.07  ? 76   PHE D CZ  1 
ATOM   11223 N  N   . ASN D  2  59  ? 0.172   -5.793  -29.927 1.00 62.03  ? 77   ASN D N   1 
ATOM   11224 C  CA  . ASN D  2  59  ? 0.348   -4.582  -29.138 1.00 61.13  ? 77   ASN D CA  1 
ATOM   11225 C  C   . ASN D  2  59  ? -1.097  -4.384  -28.734 1.00 60.73  ? 77   ASN D C   1 
ATOM   11226 O  O   . ASN D  2  59  ? -1.977  -4.369  -29.592 1.00 60.57  ? 77   ASN D O   1 
ATOM   11227 C  CB  . ASN D  2  59  ? 0.859   -3.417  -29.982 1.00 60.04  ? 77   ASN D CB  1 
ATOM   11228 C  CG  . ASN D  2  59  ? 2.363   -3.287  -29.918 1.00 60.65  ? 77   ASN D CG  1 
ATOM   11229 O  OD1 . ASN D  2  59  ? 2.946   -3.244  -28.838 1.00 61.33  ? 77   ASN D OD1 1 
ATOM   11230 N  ND2 . ASN D  2  59  ? 3.004   -3.228  -31.073 1.00 62.62  ? 77   ASN D ND2 1 
ATOM   11231 N  N   . LEU D  2  60  ? -1.367  -4.282  -27.442 1.00 59.75  ? 78   LEU D N   1 
ATOM   11232 C  CA  . LEU D  2  60  ? -2.748  -4.146  -27.042 1.00 60.59  ? 78   LEU D CA  1 
ATOM   11233 C  C   . LEU D  2  60  ? -3.083  -2.793  -26.464 1.00 61.29  ? 78   LEU D C   1 
ATOM   11234 O  O   . LEU D  2  60  ? -2.422  -2.307  -25.545 1.00 60.91  ? 78   LEU D O   1 
ATOM   11235 C  CB  . LEU D  2  60  ? -3.120  -5.240  -26.041 1.00 60.53  ? 78   LEU D CB  1 
ATOM   11236 C  CG  . LEU D  2  60  ? -2.912  -6.708  -26.426 1.00 61.47  ? 78   LEU D CG  1 
ATOM   11237 C  CD1 . LEU D  2  60  ? -3.352  -7.581  -25.261 1.00 61.52  ? 78   LEU D CD1 1 
ATOM   11238 C  CD2 . LEU D  2  60  ? -3.694  -7.068  -27.680 1.00 60.41  ? 78   LEU D CD2 1 
ATOM   11239 N  N   . TYR D  2  61  ? -4.131  -2.195  -27.019 1.00 62.63  ? 79   TYR D N   1 
ATOM   11240 C  CA  . TYR D  2  61  ? -4.614  -0.901  -26.567 1.00 64.38  ? 79   TYR D CA  1 
ATOM   11241 C  C   . TYR D  2  61  ? -6.041  -1.090  -26.014 1.00 66.44  ? 79   TYR D C   1 
ATOM   11242 O  O   . TYR D  2  61  ? -7.045  -0.985  -26.739 1.00 67.31  ? 79   TYR D O   1 
ATOM   11243 C  CB  . TYR D  2  61  ? -4.579  0.109   -27.727 1.00 60.65  ? 79   TYR D CB  1 
ATOM   11244 C  CG  . TYR D  2  61  ? -3.220  0.219   -28.392 1.00 59.06  ? 79   TYR D CG  1 
ATOM   11245 C  CD1 . TYR D  2  61  ? -2.931  -0.494  -29.563 1.00 60.11  ? 79   TYR D CD1 1 
ATOM   11246 C  CD2 . TYR D  2  61  ? -2.206  0.996   -27.834 1.00 57.31  ? 79   TYR D CD2 1 
ATOM   11247 C  CE1 . TYR D  2  61  ? -1.660  -0.437  -30.161 1.00 58.00  ? 79   TYR D CE1 1 
ATOM   11248 C  CE2 . TYR D  2  61  ? -0.936  1.058   -28.419 1.00 57.03  ? 79   TYR D CE2 1 
ATOM   11249 C  CZ  . TYR D  2  61  ? -0.670  0.338   -29.577 1.00 57.49  ? 79   TYR D CZ  1 
ATOM   11250 O  OH  . TYR D  2  61  ? 0.598   0.354   -30.122 1.00 58.41  ? 79   TYR D OH  1 
ATOM   11251 N  N   . ILE D  2  62  ? -6.112  -1.376  -24.717 1.00 67.63  ? 80   ILE D N   1 
ATOM   11252 C  CA  . ILE D  2  62  ? -7.387  -1.597  -24.057 1.00 69.96  ? 80   ILE D CA  1 
ATOM   11253 C  C   . ILE D  2  62  ? -8.013  -0.274  -23.600 1.00 72.48  ? 80   ILE D C   1 
ATOM   11254 O  O   . ILE D  2  62  ? -7.313  0.722   -23.346 1.00 72.04  ? 80   ILE D O   1 
ATOM   11255 C  CB  . ILE D  2  62  ? -7.237  -2.531  -22.811 1.00 69.28  ? 80   ILE D CB  1 
ATOM   11256 C  CG1 . ILE D  2  62  ? -6.221  -3.634  -23.082 1.00 67.53  ? 80   ILE D CG1 1 
ATOM   11257 C  CG2 . ILE D  2  62  ? -8.568  -3.169  -22.468 1.00 68.59  ? 80   ILE D CG2 1 
ATOM   11258 C  CD1 . ILE D  2  62  ? -4.805  -3.154  -22.930 1.00 67.38  ? 80   ILE D CD1 1 
ATOM   11259 N  N   . THR D  2  63  ? -9.341  -0.284  -23.491 1.00 75.26  ? 81   THR D N   1 
ATOM   11260 C  CA  . THR D  2  63  ? -10.115 0.878   -23.069 1.00 76.77  ? 81   THR D CA  1 
ATOM   11261 C  C   . THR D  2  63  ? -11.353 0.470   -22.249 1.00 77.09  ? 81   THR D C   1 
ATOM   11262 O  O   . THR D  2  63  ? -12.190 -0.324  -22.697 1.00 77.15  ? 81   THR D O   1 
ATOM   11263 C  CB  . THR D  2  63  ? -10.565 1.706   -24.295 1.00 77.50  ? 81   THR D CB  1 
ATOM   11264 O  OG1 . THR D  2  63  ? -9.412  2.155   -25.021 1.00 78.54  ? 81   THR D OG1 1 
ATOM   11265 C  CG2 . THR D  2  63  ? -11.378 2.912   -23.850 1.00 78.76  ? 81   THR D CG2 1 
ATOM   11266 N  N   . VAL D  2  64  ? -11.444 1.024   -21.042 1.00 77.52  ? 82   VAL D N   1 
ATOM   11267 C  CA  . VAL D  2  64  ? -12.550 0.762   -20.119 1.00 77.27  ? 82   VAL D CA  1 
ATOM   11268 C  C   . VAL D  2  64  ? -13.428 2.020   -20.033 1.00 78.14  ? 82   VAL D C   1 
ATOM   11269 O  O   . VAL D  2  64  ? -13.003 3.036   -19.461 1.00 78.58  ? 82   VAL D O   1 
ATOM   11270 C  CB  . VAL D  2  64  ? -12.032 0.462   -18.681 1.00 75.74  ? 82   VAL D CB  1 
ATOM   11271 C  CG1 . VAL D  2  64  ? -13.108 -0.204  -17.873 1.00 73.86  ? 82   VAL D CG1 1 
ATOM   11272 C  CG2 . VAL D  2  64  ? -10.786 -0.385  -18.725 1.00 75.02  ? 82   VAL D CG2 1 
ATOM   11273 N  N   . ASN D  2  65  ? -14.633 1.957   -20.597 1.00 77.72  ? 83   ASN D N   1 
ATOM   11274 C  CA  . ASN D  2  65  ? -15.565 3.085   -20.553 1.00 76.90  ? 83   ASN D CA  1 
ATOM   11275 C  C   . ASN D  2  65  ? -14.827 4.428   -20.629 1.00 78.11  ? 83   ASN D C   1 
ATOM   11276 O  O   . ASN D  2  65  ? -14.799 5.177   -19.648 1.00 77.12  ? 83   ASN D O   1 
ATOM   11277 C  CB  . ASN D  2  65  ? -16.407 3.049   -19.261 1.00 73.48  ? 83   ASN D CB  1 
ATOM   11278 C  CG  . ASN D  2  65  ? -17.161 1.728   -19.063 1.00 71.04  ? 83   ASN D CG  1 
ATOM   11279 O  OD1 . ASN D  2  65  ? -17.826 1.233   -19.969 1.00 68.78  ? 83   ASN D OD1 1 
ATOM   11280 N  ND2 . ASN D  2  65  ? -17.070 1.170   -17.861 1.00 69.63  ? 83   ASN D ND2 1 
ATOM   11281 N  N   . THR D  2  66  ? -14.220 4.707   -21.786 1.00 79.21  ? 84   THR D N   1 
ATOM   11282 C  CA  . THR D  2  66  ? -13.491 5.953   -22.033 1.00 80.00  ? 84   THR D CA  1 
ATOM   11283 C  C   . THR D  2  66  ? -12.089 6.003   -21.419 1.00 80.55  ? 84   THR D C   1 
ATOM   11284 O  O   . THR D  2  66  ? -11.248 6.802   -21.844 1.00 81.18  ? 84   THR D O   1 
ATOM   11285 C  CB  . THR D  2  66  ? -14.301 7.193   -21.538 1.00 80.96  ? 84   THR D CB  1 
ATOM   11286 O  OG1 . THR D  2  66  ? -14.214 8.240   -22.512 1.00 82.47  ? 84   THR D OG1 1 
ATOM   11287 C  CG2 . THR D  2  66  ? -13.746 7.730   -20.208 1.00 81.74  ? 84   THR D CG2 1 
ATOM   11288 N  N   . MET D  2  67  ? -11.836 5.159   -20.422 1.00 80.13  ? 85   MET D N   1 
ATOM   11289 C  CA  . MET D  2  67  ? -10.530 5.131   -19.770 1.00 79.40  ? 85   MET D CA  1 
ATOM   11290 C  C   . MET D  2  67  ? -9.488  4.356   -20.572 1.00 78.58  ? 85   MET D C   1 
ATOM   11291 O  O   . MET D  2  67  ? -9.802  3.355   -21.217 1.00 78.06  ? 85   MET D O   1 
ATOM   11292 C  CB  . MET D  2  67  ? -10.652 4.529   -18.374 1.00 79.91  ? 85   MET D CB  1 
ATOM   11293 C  CG  . MET D  2  67  ? -10.699 5.542   -17.249 1.00 81.05  ? 85   MET D CG  1 
ATOM   11294 S  SD  . MET D  2  67  ? -12.144 5.249   -16.220 1.00 83.25  ? 85   MET D SD  1 
ATOM   11295 C  CE  . MET D  2  67  ? -11.733 3.710   -15.441 1.00 82.70  ? 85   MET D CE  1 
ATOM   11296 N  N   . ASN D  2  68  ? -8.242  4.818   -20.526 1.00 77.54  ? 86   ASN D N   1 
ATOM   11297 C  CA  . ASN D  2  68  ? -7.166  4.164   -21.264 1.00 76.47  ? 86   ASN D CA  1 
ATOM   11298 C  C   . ASN D  2  68  ? -6.092  3.544   -20.382 1.00 74.67  ? 86   ASN D C   1 
ATOM   11299 O  O   . ASN D  2  68  ? -5.581  4.181   -19.457 1.00 75.47  ? 86   ASN D O   1 
ATOM   11300 C  CB  . ASN D  2  68  ? -6.522  5.152   -22.238 1.00 77.38  ? 86   ASN D CB  1 
ATOM   11301 C  CG  . ASN D  2  68  ? -7.084  5.031   -23.641 1.00 78.54  ? 86   ASN D CG  1 
ATOM   11302 O  OD1 . ASN D  2  68  ? -8.292  4.841   -23.830 1.00 77.29  ? 86   ASN D OD1 1 
ATOM   11303 N  ND2 . ASN D  2  68  ? -6.209  5.146   -24.637 1.00 80.08  ? 86   ASN D ND2 1 
ATOM   11304 N  N   . LEU D  2  69  ? -5.762  2.291   -20.687 1.00 71.97  ? 87   LEU D N   1 
ATOM   11305 C  CA  . LEU D  2  69  ? -4.749  1.531   -19.964 1.00 67.27  ? 87   LEU D CA  1 
ATOM   11306 C  C   . LEU D  2  69  ? -3.490  1.603   -20.786 1.00 64.77  ? 87   LEU D C   1 
ATOM   11307 O  O   . LEU D  2  69  ? -3.553  1.762   -21.991 1.00 64.60  ? 87   LEU D O   1 
ATOM   11308 C  CB  . LEU D  2  69  ? -5.171  0.070   -19.851 1.00 67.35  ? 87   LEU D CB  1 
ATOM   11309 C  CG  . LEU D  2  69  ? -6.348  -0.266  -18.930 1.00 68.21  ? 87   LEU D CG  1 
ATOM   11310 C  CD1 . LEU D  2  69  ? -7.177  -1.425  -19.483 1.00 66.59  ? 87   LEU D CD1 1 
ATOM   11311 C  CD2 . LEU D  2  69  ? -5.789  -0.586  -17.546 1.00 68.12  ? 87   LEU D CD2 1 
ATOM   11312 N  N   . PRO D  2  70  ? -2.326  1.499   -20.146 1.00 63.28  ? 88   PRO D N   1 
ATOM   11313 C  CA  . PRO D  2  70  ? -1.062  1.553   -20.879 1.00 62.59  ? 88   PRO D CA  1 
ATOM   11314 C  C   . PRO D  2  70  ? -1.010  0.508   -21.996 1.00 62.53  ? 88   PRO D C   1 
ATOM   11315 O  O   . PRO D  2  70  ? -1.847  -0.400  -22.057 1.00 63.99  ? 88   PRO D O   1 
ATOM   11316 C  CB  . PRO D  2  70  ? -0.035  1.285   -19.789 1.00 62.45  ? 88   PRO D CB  1 
ATOM   11317 C  CG  . PRO D  2  70  ? -0.638  1.968   -18.616 1.00 62.76  ? 88   PRO D CG  1 
ATOM   11318 C  CD  . PRO D  2  70  ? -2.092  1.542   -18.695 1.00 63.33  ? 88   PRO D CD  1 
ATOM   11319 N  N   . LYS D  2  71  ? -0.040  0.639   -22.893 1.00 61.47  ? 89   LYS D N   1 
ATOM   11320 C  CA  . LYS D  2  71  ? 0.089   -0.321  -23.977 1.00 60.25  ? 89   LYS D CA  1 
ATOM   11321 C  C   . LYS D  2  71  ? 0.489   -1.642  -23.360 1.00 60.18  ? 89   LYS D C   1 
ATOM   11322 O  O   . LYS D  2  71  ? 1.059   -1.671  -22.279 1.00 61.63  ? 89   LYS D O   1 
ATOM   11323 C  CB  . LYS D  2  71  ? 1.170   0.111   -24.969 1.00 59.62  ? 89   LYS D CB  1 
ATOM   11324 C  CG  . LYS D  2  71  ? 1.294   -0.849  -26.137 1.00 61.33  ? 89   LYS D CG  1 
ATOM   11325 C  CD  . LYS D  2  71  ? 2.205   -0.339  -27.241 1.00 63.78  ? 89   LYS D CD  1 
ATOM   11326 C  CE  . LYS D  2  71  ? 3.685   -0.453  -26.885 1.00 65.22  ? 89   LYS D CE  1 
ATOM   11327 N  NZ  . LYS D  2  71  ? 4.514   -0.082  -28.072 1.00 66.79  ? 89   LYS D NZ  1 
ATOM   11328 N  N   . ARG D  2  72  ? 0.170   -2.735  -24.029 1.00 59.57  ? 90   ARG D N   1 
ATOM   11329 C  CA  . ARG D  2  72  ? 0.556   -4.043  -23.545 1.00 58.76  ? 90   ARG D CA  1 
ATOM   11330 C  C   . ARG D  2  72  ? 1.225   -4.768  -24.698 1.00 60.31  ? 90   ARG D C   1 
ATOM   11331 O  O   . ARG D  2  72  ? 0.696   -4.787  -25.816 1.00 61.65  ? 90   ARG D O   1 
ATOM   11332 C  CB  . ARG D  2  72  ? -0.654  -4.856  -23.110 1.00 57.05  ? 90   ARG D CB  1 
ATOM   11333 C  CG  . ARG D  2  72  ? -1.280  -4.411  -21.827 1.00 59.98  ? 90   ARG D CG  1 
ATOM   11334 C  CD  . ARG D  2  72  ? -2.360  -5.396  -21.410 1.00 61.08  ? 90   ARG D CD  1 
ATOM   11335 N  NE  . ARG D  2  72  ? -1.806  -6.671  -20.954 1.00 62.66  ? 90   ARG D NE  1 
ATOM   11336 C  CZ  . ARG D  2  72  ? -1.410  -6.910  -19.708 1.00 62.34  ? 90   ARG D CZ  1 
ATOM   11337 N  NH1 . ARG D  2  72  ? -1.506  -5.959  -18.783 1.00 62.97  ? 90   ARG D NH1 1 
ATOM   11338 N  NH2 . ARG D  2  72  ? -0.928  -8.099  -19.386 1.00 59.53  ? 90   ARG D NH2 1 
ATOM   11339 N  N   . LYS D  2  73  ? 2.399   -5.337  -24.451 1.00 59.73  ? 91   LYS D N   1 
ATOM   11340 C  CA  . LYS D  2  73  ? 3.066   -6.103  -25.485 1.00 57.91  ? 91   LYS D CA  1 
ATOM   11341 C  C   . LYS D  2  73  ? 2.941   -7.559  -25.056 1.00 57.55  ? 91   LYS D C   1 
ATOM   11342 O  O   . LYS D  2  73  ? 3.437   -7.955  -24.006 1.00 58.09  ? 91   LYS D O   1 
ATOM   11343 C  CB  . LYS D  2  73  ? 4.537   -5.709  -25.610 1.00 57.36  ? 91   LYS D CB  1 
ATOM   11344 C  CG  . LYS D  2  73  ? 5.275   -6.510  -26.668 1.00 56.56  ? 91   LYS D CG  1 
ATOM   11345 C  CD  . LYS D  2  73  ? 6.693   -6.022  -26.861 1.00 57.38  ? 91   LYS D CD  1 
ATOM   11346 C  CE  . LYS D  2  73  ? 7.395   -6.824  -27.950 1.00 58.69  ? 91   LYS D CE  1 
ATOM   11347 N  NZ  . LYS D  2  73  ? 8.642   -6.170  -28.457 1.00 59.12  ? 91   LYS D NZ  1 
ATOM   11348 N  N   . GLU D  2  74  ? 2.227   -8.343  -25.849 1.00 57.06  ? 92   GLU D N   1 
ATOM   11349 C  CA  . GLU D  2  74  ? 2.055   -9.757  -25.570 1.00 57.20  ? 92   GLU D CA  1 
ATOM   11350 C  C   . GLU D  2  74  ? 2.764   -10.499 -26.690 1.00 56.01  ? 92   GLU D C   1 
ATOM   11351 O  O   . GLU D  2  74  ? 2.415   -10.339 -27.855 1.00 55.13  ? 92   GLU D O   1 
ATOM   11352 C  CB  . GLU D  2  74  ? 0.571   -10.125 -25.550 1.00 59.77  ? 92   GLU D CB  1 
ATOM   11353 C  CG  . GLU D  2  74  ? -0.222  -9.549  -24.390 1.00 64.76  ? 92   GLU D CG  1 
ATOM   11354 C  CD  . GLU D  2  74  ? 0.399   -9.858  -23.021 1.00 69.59  ? 92   GLU D CD  1 
ATOM   11355 O  OE1 . GLU D  2  74  ? 0.858   -11.008 -22.803 1.00 71.50  ? 92   GLU D OE1 1 
ATOM   11356 O  OE2 . GLU D  2  74  ? 0.415   -8.951  -22.155 1.00 70.77  ? 92   GLU D OE2 1 
ATOM   11357 N  N   . VAL D  2  75  ? 3.761   -11.305 -26.342 1.00 55.26  ? 93   VAL D N   1 
ATOM   11358 C  CA  . VAL D  2  75  ? 4.520   -12.044 -27.348 1.00 54.48  ? 93   VAL D CA  1 
ATOM   11359 C  C   . VAL D  2  75  ? 4.032   -13.463 -27.615 1.00 55.47  ? 93   VAL D C   1 
ATOM   11360 O  O   . VAL D  2  75  ? 3.837   -14.243 -26.695 1.00 56.70  ? 93   VAL D O   1 
ATOM   11361 C  CB  . VAL D  2  75  ? 5.993   -12.140 -26.962 1.00 51.03  ? 93   VAL D CB  1 
ATOM   11362 C  CG1 . VAL D  2  75  ? 6.807   -12.592 -28.144 1.00 48.45  ? 93   VAL D CG1 1 
ATOM   11363 C  CG2 . VAL D  2  75  ? 6.461   -10.814 -26.449 1.00 50.57  ? 93   VAL D CG2 1 
ATOM   11364 N  N   . ILE D  2  76  ? 3.820   -13.784 -28.883 1.00 56.14  ? 94   ILE D N   1 
ATOM   11365 C  CA  . ILE D  2  76  ? 3.411   -15.123 -29.282 1.00 57.93  ? 94   ILE D CA  1 
ATOM   11366 C  C   . ILE D  2  76  ? 4.601   -15.402 -30.156 1.00 60.29  ? 94   ILE D C   1 
ATOM   11367 O  O   . ILE D  2  76  ? 4.852   -14.618 -31.060 1.00 63.58  ? 94   ILE D O   1 
ATOM   11368 C  CB  . ILE D  2  76  ? 2.171   -15.118 -30.202 1.00 57.80  ? 94   ILE D CB  1 
ATOM   11369 C  CG1 . ILE D  2  76  ? 1.268   -13.914 -29.901 1.00 56.78  ? 94   ILE D CG1 1 
ATOM   11370 C  CG2 . ILE D  2  76  ? 1.442   -16.440 -30.088 1.00 56.16  ? 94   ILE D CG2 1 
ATOM   11371 C  CD1 . ILE D  2  76  ? 0.795   -13.807 -28.480 1.00 55.18  ? 94   ILE D CD1 1 
ATOM   11372 N  N   . CYS D  2  77  ? 5.352   -16.467 -29.905 1.00 61.16  ? 95   CYS D N   1 
ATOM   11373 C  CA  . CYS D  2  77  ? 6.549   -16.756 -30.724 1.00 63.78  ? 95   CYS D CA  1 
ATOM   11374 C  C   . CYS D  2  77  ? 7.760   -15.847 -30.422 1.00 64.58  ? 95   CYS D C   1 
ATOM   11375 O  O   . CYS D  2  77  ? 7.809   -14.690 -30.868 1.00 62.36  ? 95   CYS D O   1 
ATOM   11376 C  CB  . CYS D  2  77  ? 6.289   -16.599 -32.238 1.00 63.78  ? 95   CYS D CB  1 
ATOM   11377 S  SG  . CYS D  2  77  ? 4.736   -17.235 -32.968 1.00 65.29  ? 95   CYS D SG  1 
ATOM   11378 N  N   . ARG D  2  78  ? 8.735   -16.360 -29.675 1.00 66.21  ? 96   ARG D N   1 
ATOM   11379 C  CA  . ARG D  2  78  ? 9.931   -15.583 -29.393 1.00 67.67  ? 96   ARG D CA  1 
ATOM   11380 C  C   . ARG D  2  78  ? 10.871  -15.673 -30.611 1.00 68.85  ? 96   ARG D C   1 
ATOM   11381 O  O   . ARG D  2  78  ? 11.653  -14.756 -30.864 1.00 69.82  ? 96   ARG D O   1 
ATOM   11382 C  CB  . ARG D  2  78  ? 10.621  -16.074 -28.108 1.00 68.29  ? 96   ARG D CB  1 
ATOM   11383 C  CG  . ARG D  2  78  ? 10.278  -17.504 -27.693 1.00 72.95  ? 96   ARG D CG  1 
ATOM   11384 C  CD  . ARG D  2  78  ? 10.930  -17.908 -26.362 1.00 74.59  ? 96   ARG D CD  1 
ATOM   11385 N  NE  . ARG D  2  78  ? 12.378  -18.131 -26.468 1.00 76.96  ? 96   ARG D NE  1 
ATOM   11386 C  CZ  . ARG D  2  78  ? 12.936  -19.158 -27.107 1.00 77.25  ? 96   ARG D CZ  1 
ATOM   11387 N  NH1 . ARG D  2  78  ? 12.164  -20.062 -27.707 1.00 76.53  ? 96   ARG D NH1 1 
ATOM   11388 N  NH2 . ARG D  2  78  ? 14.263  -19.289 -27.132 1.00 75.93  ? 96   ARG D NH2 1 
ATOM   11389 N  N   . GLY D  2  79  ? 10.794  -16.768 -31.369 1.00 68.77  ? 97   GLY D N   1 
ATOM   11390 C  CA  . GLY D  2  79  ? 11.627  -16.874 -32.557 1.00 69.25  ? 97   GLY D CA  1 
ATOM   11391 C  C   . GLY D  2  79  ? 12.466  -18.120 -32.791 1.00 70.00  ? 97   GLY D C   1 
ATOM   11392 O  O   . GLY D  2  79  ? 12.998  -18.301 -33.892 1.00 70.33  ? 97   GLY D O   1 
ATOM   11393 N  N   . SER D  2  80  ? 12.612  -18.975 -31.785 1.00 69.79  ? 98   SER D N   1 
ATOM   11394 C  CA  . SER D  2  80  ? 13.412  -20.190 -31.957 1.00 70.30  ? 98   SER D CA  1 
ATOM   11395 C  C   . SER D  2  80  ? 12.775  -21.387 -31.242 1.00 70.56  ? 98   SER D C   1 
ATOM   11396 O  O   . SER D  2  80  ? 12.648  -21.389 -30.008 1.00 72.14  ? 98   SER D O   1 
ATOM   11397 C  CB  . SER D  2  80  ? 14.823  -19.957 -31.421 1.00 69.91  ? 98   SER D CB  1 
ATOM   11398 O  OG  . SER D  2  80  ? 15.602  -21.138 -31.495 1.00 70.83  ? 98   SER D OG  1 
ATOM   11399 N  N   . ASP D  2  81  ? 12.376  -22.400 -32.013 1.00 68.10  ? 99   ASP D N   1 
ATOM   11400 C  CA  . ASP D  2  81  ? 11.739  -23.584 -31.442 1.00 65.22  ? 99   ASP D CA  1 
ATOM   11401 C  C   . ASP D  2  81  ? 10.591  -23.101 -30.535 1.00 63.51  ? 99   ASP D C   1 
ATOM   11402 O  O   . ASP D  2  81  ? 10.561  -23.365 -29.334 1.00 62.37  ? 99   ASP D O   1 
ATOM   11403 C  CB  . ASP D  2  81  ? 12.780  -24.399 -30.654 1.00 65.53  ? 99   ASP D CB  1 
ATOM   11404 C  CG  . ASP D  2  81  ? 13.753  -25.163 -31.563 1.00 67.26  ? 99   ASP D CG  1 
ATOM   11405 O  OD1 . ASP D  2  81  ? 14.952  -25.261 -31.211 1.00 68.44  ? 99   ASP D OD1 1 
ATOM   11406 O  OD2 . ASP D  2  81  ? 13.325  -25.680 -32.621 1.00 67.66  ? 99   ASP D OD2 1 
ATOM   11407 N  N   . ASP D  2  82  ? 9.641   -22.392 -31.138 1.00 61.28  ? 100  ASP D N   1 
ATOM   11408 C  CA  . ASP D  2  82  ? 8.511   -21.825 -30.417 1.00 60.00  ? 100  ASP D CA  1 
ATOM   11409 C  C   . ASP D  2  82  ? 7.461   -22.810 -29.958 1.00 59.07  ? 100  ASP D C   1 
ATOM   11410 O  O   . ASP D  2  82  ? 7.400   -23.942 -30.429 1.00 60.30  ? 100  ASP D O   1 
ATOM   11411 C  CB  . ASP D  2  82  ? 7.848   -20.740 -31.269 1.00 61.01  ? 100  ASP D CB  1 
ATOM   11412 C  CG  . ASP D  2  82  ? 8.736   -19.521 -31.444 1.00 62.56  ? 100  ASP D CG  1 
ATOM   11413 O  OD1 . ASP D  2  82  ? 9.202   -18.999 -30.408 1.00 64.16  ? 100  ASP D OD1 1 
ATOM   11414 O  OD2 . ASP D  2  82  ? 8.971   -19.084 -32.596 1.00 60.50  ? 100  ASP D OD2 1 
ATOM   11415 N  N   . ASP D  2  83  ? 6.624   -22.350 -29.036 1.00 57.52  ? 101  ASP D N   1 
ATOM   11416 C  CA  . ASP D  2  83  ? 5.549   -23.159 -28.474 1.00 55.81  ? 101  ASP D CA  1 
ATOM   11417 C  C   . ASP D  2  83  ? 4.484   -23.513 -29.509 1.00 55.58  ? 101  ASP D C   1 
ATOM   11418 O  O   . ASP D  2  83  ? 4.100   -24.672 -29.640 1.00 57.27  ? 101  ASP D O   1 
ATOM   11419 C  CB  . ASP D  2  83  ? 4.879   -22.416 -27.311 1.00 54.12  ? 101  ASP D CB  1 
ATOM   11420 C  CG  . ASP D  2  83  ? 5.763   -22.329 -26.065 1.00 54.86  ? 101  ASP D CG  1 
ATOM   11421 O  OD1 . ASP D  2  83  ? 7.001   -22.457 -26.181 1.00 54.64  ? 101  ASP D OD1 1 
ATOM   11422 O  OD2 . ASP D  2  83  ? 5.210   -22.122 -24.957 1.00 53.09  ? 101  ASP D OD2 1 
ATOM   11423 N  N   . TYR D  2  84  ? 4.001   -22.515 -30.241 1.00 54.90  ? 102  TYR D N   1 
ATOM   11424 C  CA  . TYR D  2  84  ? 2.957   -22.738 -31.237 1.00 53.68  ? 102  TYR D CA  1 
ATOM   11425 C  C   . TYR D  2  84  ? 3.516   -23.156 -32.589 1.00 53.78  ? 102  TYR D C   1 
ATOM   11426 O  O   . TYR D  2  84  ? 4.591   -22.727 -32.993 1.00 55.14  ? 102  TYR D O   1 
ATOM   11427 C  CB  . TYR D  2  84  ? 2.097   -21.469 -31.375 1.00 52.68  ? 102  TYR D CB  1 
ATOM   11428 C  CG  . TYR D  2  84  ? 1.300   -21.161 -30.125 1.00 51.43  ? 102  TYR D CG  1 
ATOM   11429 C  CD1 . TYR D  2  84  ? 1.278   -19.882 -29.571 1.00 50.06  ? 102  TYR D CD1 1 
ATOM   11430 C  CD2 . TYR D  2  84  ? 0.607   -22.171 -29.465 1.00 51.84  ? 102  TYR D CD2 1 
ATOM   11431 C  CE1 . TYR D  2  84  ? 0.586   -19.621 -28.381 1.00 49.40  ? 102  TYR D CE1 1 
ATOM   11432 C  CE2 . TYR D  2  84  ? -0.078  -21.928 -28.279 1.00 52.13  ? 102  TYR D CE2 1 
ATOM   11433 C  CZ  . TYR D  2  84  ? -0.090  -20.652 -27.737 1.00 51.54  ? 102  TYR D CZ  1 
ATOM   11434 O  OH  . TYR D  2  84  ? -0.781  -20.432 -26.552 1.00 52.80  ? 102  TYR D OH  1 
ATOM   11435 N  N   . SER D  2  85  ? 2.779   -24.005 -33.288 1.00 53.74  ? 103  SER D N   1 
ATOM   11436 C  CA  . SER D  2  85  ? 3.220   -24.483 -34.587 1.00 53.79  ? 103  SER D CA  1 
ATOM   11437 C  C   . SER D  2  85  ? 3.029   -23.447 -35.694 1.00 54.12  ? 103  SER D C   1 
ATOM   11438 O  O   . SER D  2  85  ? 3.703   -23.503 -36.723 1.00 52.22  ? 103  SER D O   1 
ATOM   11439 C  CB  . SER D  2  85  ? 2.464   -25.755 -34.961 1.00 53.01  ? 103  SER D CB  1 
ATOM   11440 O  OG  . SER D  2  85  ? 1.114   -25.459 -35.274 1.00 54.26  ? 103  SER D OG  1 
ATOM   11441 N  N   . PHE D  2  86  ? 2.117   -22.502 -35.491 1.00 55.46  ? 104  PHE D N   1 
ATOM   11442 C  CA  . PHE D  2  86  ? 1.859   -21.512 -36.525 1.00 57.41  ? 104  PHE D CA  1 
ATOM   11443 C  C   . PHE D  2  86  ? 2.925   -20.427 -36.627 1.00 58.27  ? 104  PHE D C   1 
ATOM   11444 O  O   . PHE D  2  86  ? 2.899   -19.604 -37.547 1.00 58.40  ? 104  PHE D O   1 
ATOM   11445 C  CB  . PHE D  2  86  ? 0.476   -20.898 -36.340 1.00 57.69  ? 104  PHE D CB  1 
ATOM   11446 C  CG  . PHE D  2  86  ? 0.294   -20.202 -35.036 1.00 60.12  ? 104  PHE D CG  1 
ATOM   11447 C  CD1 . PHE D  2  86  ? 0.811   -18.929 -34.834 1.00 60.30  ? 104  PHE D CD1 1 
ATOM   11448 C  CD2 . PHE D  2  86  ? -0.418  -20.815 -34.008 1.00 61.66  ? 104  PHE D CD2 1 
ATOM   11449 C  CE1 . PHE D  2  86  ? 0.619   -18.257 -33.624 1.00 60.21  ? 104  PHE D CE1 1 
ATOM   11450 C  CE2 . PHE D  2  86  ? -0.618  -20.161 -32.798 1.00 61.46  ? 104  PHE D CE2 1 
ATOM   11451 C  CZ  . PHE D  2  86  ? -0.095  -18.872 -32.604 1.00 60.74  ? 104  PHE D CZ  1 
ATOM   11452 N  N   . CYS D  2  87  ? 3.873   -20.431 -35.698 1.00 58.23  ? 105  CYS D N   1 
ATOM   11453 C  CA  . CYS D  2  87  ? 4.952   -19.451 -35.747 1.00 59.09  ? 105  CYS D CA  1 
ATOM   11454 C  C   . CYS D  2  87  ? 5.793   -19.708 -36.985 1.00 58.99  ? 105  CYS D C   1 
ATOM   11455 O  O   . CYS D  2  87  ? 6.317   -18.786 -37.592 1.00 59.94  ? 105  CYS D O   1 
ATOM   11456 C  CB  . CYS D  2  87  ? 5.849   -19.579 -34.530 1.00 60.32  ? 105  CYS D CB  1 
ATOM   11457 S  SG  . CYS D  2  87  ? 5.007   -19.250 -32.956 1.00 66.12  ? 105  CYS D SG  1 
ATOM   11458 N  N   . ARG D  2  88  ? 5.919   -20.981 -37.343 1.00 59.07  ? 106  ARG D N   1 
ATOM   11459 C  CA  . ARG D  2  88  ? 6.688   -21.411 -38.505 1.00 58.33  ? 106  ARG D CA  1 
ATOM   11460 C  C   . ARG D  2  88  ? 6.047   -21.013 -39.837 1.00 58.45  ? 106  ARG D C   1 
ATOM   11461 O  O   . ARG D  2  88  ? 6.686   -21.089 -40.882 1.00 61.04  ? 106  ARG D O   1 
ATOM   11462 C  CB  . ARG D  2  88  ? 6.853   -22.934 -38.472 1.00 58.15  ? 106  ARG D CB  1 
ATOM   11463 C  CG  . ARG D  2  88  ? 7.923   -23.452 -37.524 1.00 58.69  ? 106  ARG D CG  1 
ATOM   11464 C  CD  . ARG D  2  88  ? 7.710   -24.936 -37.187 1.00 57.37  ? 106  ARG D CD  1 
ATOM   11465 N  NE  . ARG D  2  88  ? 7.405   -25.734 -38.369 1.00 57.44  ? 106  ARG D NE  1 
ATOM   11466 C  CZ  . ARG D  2  88  ? 6.274   -26.411 -38.523 1.00 58.49  ? 106  ARG D CZ  1 
ATOM   11467 N  NH1 . ARG D  2  88  ? 5.370   -26.375 -37.554 1.00 58.36  ? 106  ARG D NH1 1 
ATOM   11468 N  NH2 . ARG D  2  88  ? 6.032   -27.093 -39.645 1.00 56.97  ? 106  ARG D NH2 1 
ATOM   11469 N  N   . ALA D  2  89  ? 4.789   -20.593 -39.808 1.00 57.06  ? 107  ALA D N   1 
ATOM   11470 C  CA  . ALA D  2  89  ? 4.082   -20.209 -41.029 1.00 55.69  ? 107  ALA D CA  1 
ATOM   11471 C  C   . ALA D  2  89  ? 4.750   -19.119 -41.882 1.00 55.41  ? 107  ALA D C   1 
ATOM   11472 O  O   . ALA D  2  89  ? 5.251   -18.111 -41.365 1.00 53.78  ? 107  ALA D O   1 
ATOM   11473 C  CB  . ALA D  2  89  ? 2.667   -19.786 -40.674 1.00 56.27  ? 107  ALA D CB  1 
ATOM   11474 N  N   . LEU D  2  90  ? 4.727   -19.330 -43.198 1.00 55.42  ? 108  LEU D N   1 
ATOM   11475 C  CA  . LEU D  2  90  ? 5.311   -18.393 -44.161 1.00 56.03  ? 108  LEU D CA  1 
ATOM   11476 C  C   . LEU D  2  90  ? 4.274   -17.483 -44.814 1.00 57.59  ? 108  LEU D C   1 
ATOM   11477 O  O   . LEU D  2  90  ? 3.064   -17.698 -44.684 1.00 57.47  ? 108  LEU D O   1 
ATOM   11478 C  CB  . LEU D  2  90  ? 6.043   -19.147 -45.264 1.00 54.23  ? 108  LEU D CB  1 
ATOM   11479 C  CG  . LEU D  2  90  ? 7.203   -20.000 -44.802 1.00 52.12  ? 108  LEU D CG  1 
ATOM   11480 C  CD1 . LEU D  2  90  ? 7.790   -20.761 -45.976 1.00 52.01  ? 108  LEU D CD1 1 
ATOM   11481 C  CD2 . LEU D  2  90  ? 8.226   -19.096 -44.188 1.00 52.69  ? 108  LEU D CD2 1 
ATOM   11482 N  N   . LYS D  2  91  ? 4.767   -16.497 -45.558 1.00 59.80  ? 109  LYS D N   1 
ATOM   11483 C  CA  . LYS D  2  91  ? 3.919   -15.514 -46.224 1.00 62.55  ? 109  LYS D CA  1 
ATOM   11484 C  C   . LYS D  2  91  ? 2.608   -15.991 -46.853 1.00 65.59  ? 109  LYS D C   1 
ATOM   11485 O  O   . LYS D  2  91  ? 1.569   -15.386 -46.596 1.00 68.80  ? 109  LYS D O   1 
ATOM   11486 C  CB  . LYS D  2  91  ? 4.706   -14.745 -47.283 1.00 60.97  ? 109  LYS D CB  1 
ATOM   11487 C  CG  . LYS D  2  91  ? 3.926   -13.581 -47.865 1.00 59.43  ? 109  LYS D CG  1 
ATOM   11488 C  CD  . LYS D  2  91  ? 4.465   -13.162 -49.225 1.00 60.63  ? 109  LYS D CD  1 
ATOM   11489 C  CE  . LYS D  2  91  ? 5.367   -11.934 -49.133 1.00 60.17  ? 109  LYS D CE  1 
ATOM   11490 N  NZ  . LYS D  2  91  ? 4.597   -10.733 -48.693 1.00 59.67  ? 109  LYS D NZ  1 
ATOM   11491 N  N   . GLY D  2  92  ? 2.612   -17.042 -47.669 1.00 65.71  ? 110  GLY D N   1 
ATOM   11492 C  CA  . GLY D  2  92  ? 1.337   -17.441 -48.259 1.00 66.38  ? 110  GLY D CA  1 
ATOM   11493 C  C   . GLY D  2  92  ? 0.762   -18.760 -47.780 1.00 67.17  ? 110  GLY D C   1 
ATOM   11494 O  O   . GLY D  2  92  ? -0.116  -19.334 -48.415 1.00 66.59  ? 110  GLY D O   1 
ATOM   11495 N  N   . GLU D  2  93  ? 1.247   -19.232 -46.641 1.00 68.25  ? 111  GLU D N   1 
ATOM   11496 C  CA  . GLU D  2  93  ? 0.824   -20.513 -46.080 1.00 68.31  ? 111  GLU D CA  1 
ATOM   11497 C  C   . GLU D  2  93  ? -0.521  -20.497 -45.364 1.00 68.27  ? 111  GLU D C   1 
ATOM   11498 O  O   . GLU D  2  93  ? -0.841  -19.572 -44.615 1.00 69.73  ? 111  GLU D O   1 
ATOM   11499 C  CB  . GLU D  2  93  ? 1.914   -21.014 -45.121 1.00 68.73  ? 111  GLU D CB  1 
ATOM   11500 C  CG  . GLU D  2  93  ? 1.866   -22.492 -44.757 1.00 67.77  ? 111  GLU D CG  1 
ATOM   11501 C  CD  . GLU D  2  93  ? 3.077   -22.913 -43.931 1.00 69.33  ? 111  GLU D CD  1 
ATOM   11502 O  OE1 . GLU D  2  93  ? 3.154   -24.102 -43.559 1.00 69.98  ? 111  GLU D OE1 1 
ATOM   11503 O  OE2 . GLU D  2  93  ? 3.954   -22.061 -43.648 1.00 69.03  ? 111  GLU D OE2 1 
ATOM   11504 N  N   . THR D  2  94  ? -1.307  -21.542 -45.595 1.00 68.13  ? 112  THR D N   1 
ATOM   11505 C  CA  . THR D  2  94  ? -2.612  -21.667 -44.958 1.00 67.28  ? 112  THR D CA  1 
ATOM   11506 C  C   . THR D  2  94  ? -2.420  -22.019 -43.487 1.00 68.25  ? 112  THR D C   1 
ATOM   11507 O  O   . THR D  2  94  ? -1.727  -22.987 -43.146 1.00 68.64  ? 112  THR D O   1 
ATOM   11508 C  CB  . THR D  2  94  ? -3.450  -22.777 -45.603 1.00 64.94  ? 112  THR D CB  1 
ATOM   11509 O  OG1 . THR D  2  94  ? -3.650  -22.485 -46.989 1.00 63.74  ? 112  THR D OG1 1 
ATOM   11510 C  CG2 . THR D  2  94  ? -4.778  -22.893 -44.912 1.00 63.00  ? 112  THR D CG2 1 
ATOM   11511 N  N   . VAL D  2  95  ? -3.047  -21.231 -42.623 1.00 68.64  ? 113  VAL D N   1 
ATOM   11512 C  CA  . VAL D  2  95  ? -2.969  -21.433 -41.183 1.00 68.33  ? 113  VAL D CA  1 
ATOM   11513 C  C   . VAL D  2  95  ? -4.341  -21.818 -40.632 1.00 69.13  ? 113  VAL D C   1 
ATOM   11514 O  O   . VAL D  2  95  ? -5.183  -20.958 -40.419 1.00 69.40  ? 113  VAL D O   1 
ATOM   11515 C  CB  . VAL D  2  95  ? -2.518  -20.144 -40.496 1.00 67.47  ? 113  VAL D CB  1 
ATOM   11516 C  CG1 . VAL D  2  95  ? -2.226  -20.405 -39.036 1.00 66.13  ? 113  VAL D CG1 1 
ATOM   11517 C  CG2 . VAL D  2  95  ? -1.318  -19.578 -41.223 1.00 66.88  ? 113  VAL D CG2 1 
ATOM   11518 N  N   . ASN D  2  96  ? -4.572  -23.110 -40.425 1.00 71.12  ? 114  ASN D N   1 
ATOM   11519 C  CA  . ASN D  2  96  ? -5.844  -23.607 -39.873 1.00 72.16  ? 114  ASN D CA  1 
ATOM   11520 C  C   . ASN D  2  96  ? -5.459  -24.263 -38.551 1.00 70.09  ? 114  ASN D C   1 
ATOM   11521 O  O   . ASN D  2  96  ? -5.062  -25.430 -38.517 1.00 69.73  ? 114  ASN D O   1 
ATOM   11522 C  CB  . ASN D  2  96  ? -6.470  -24.656 -40.806 1.00 76.44  ? 114  ASN D CB  1 
ATOM   11523 C  CG  . ASN D  2  96  ? -7.842  -25.126 -40.340 1.00 80.04  ? 114  ASN D CG  1 
ATOM   11524 O  OD1 . ASN D  2  96  ? -8.195  -25.020 -39.168 1.00 79.55  ? 114  ASN D OD1 1 
ATOM   11525 N  ND2 . ASN D  2  96  ? -8.615  -25.673 -41.269 1.00 84.88  ? 114  ASN D ND2 1 
ATOM   11526 N  N   . THR D  2  97  ? -5.575  -23.511 -37.465 1.00 68.15  ? 115  THR D N   1 
ATOM   11527 C  CA  . THR D  2  97  ? -5.181  -24.027 -36.167 1.00 67.22  ? 115  THR D CA  1 
ATOM   11528 C  C   . THR D  2  97  ? -6.207  -23.820 -35.047 1.00 66.08  ? 115  THR D C   1 
ATOM   11529 O  O   . THR D  2  97  ? -7.173  -23.073 -35.198 1.00 65.26  ? 115  THR D O   1 
ATOM   11530 C  CB  . THR D  2  97  ? -3.833  -23.400 -35.741 1.00 66.81  ? 115  THR D CB  1 
ATOM   11531 O  OG1 . THR D  2  97  ? -3.358  -24.051 -34.557 1.00 68.13  ? 115  THR D OG1 1 
ATOM   11532 C  CG2 . THR D  2  97  ? -4.005  -21.911 -35.467 1.00 65.43  ? 115  THR D CG2 1 
ATOM   11533 N  N   . THR D  2  98  ? -5.980  -24.508 -33.927 1.00 64.45  ? 116  THR D N   1 
ATOM   11534 C  CA  . THR D  2  98  ? -6.835  -24.422 -32.746 1.00 61.79  ? 116  THR D CA  1 
ATOM   11535 C  C   . THR D  2  98  ? -5.941  -24.190 -31.542 1.00 60.33  ? 116  THR D C   1 
ATOM   11536 O  O   . THR D  2  98  ? -5.128  -25.038 -31.176 1.00 60.35  ? 116  THR D O   1 
ATOM   11537 C  CB  . THR D  2  98  ? -7.634  -25.717 -32.505 1.00 61.30  ? 116  THR D CB  1 
ATOM   11538 O  OG1 . THR D  2  98  ? -8.548  -25.919 -33.587 1.00 62.61  ? 116  THR D OG1 1 
ATOM   11539 C  CG2 . THR D  2  98  ? -8.413  -25.628 -31.207 1.00 59.06  ? 116  THR D CG2 1 
ATOM   11540 N  N   . ILE D  2  99  ? -6.103  -23.028 -30.932 1.00 58.30  ? 117  ILE D N   1 
ATOM   11541 C  CA  . ILE D  2  99  ? -5.322  -22.634 -29.771 1.00 57.21  ? 117  ILE D CA  1 
ATOM   11542 C  C   . ILE D  2  99  ? -6.183  -22.721 -28.517 1.00 58.35  ? 117  ILE D C   1 
ATOM   11543 O  O   . ILE D  2  99  ? -7.311  -22.232 -28.506 1.00 60.43  ? 117  ILE D O   1 
ATOM   11544 C  CB  . ILE D  2  99  ? -4.855  -21.200 -29.961 1.00 54.70  ? 117  ILE D CB  1 
ATOM   11545 C  CG1 . ILE D  2  99  ? -4.057  -21.121 -31.259 1.00 54.85  ? 117  ILE D CG1 1 
ATOM   11546 C  CG2 . ILE D  2  99  ? -4.058  -20.745 -28.776 1.00 52.56  ? 117  ILE D CG2 1 
ATOM   11547 C  CD1 . ILE D  2  99  ? -4.043  -19.754 -31.882 1.00 56.15  ? 117  ILE D CD1 1 
ATOM   11548 N  N   . SER D  2  100 ? -5.675  -23.339 -27.458 1.00 58.31  ? 118  SER D N   1 
ATOM   11549 C  CA  . SER D  2  100 ? -6.462  -23.434 -26.229 1.00 57.93  ? 118  SER D CA  1 
ATOM   11550 C  C   . SER D  2  100 ? -6.154  -22.265 -25.311 1.00 57.60  ? 118  SER D C   1 
ATOM   11551 O  O   . SER D  2  100 ? -5.041  -21.748 -25.305 1.00 58.30  ? 118  SER D O   1 
ATOM   11552 C  CB  . SER D  2  100 ? -6.177  -24.750 -25.501 1.00 58.74  ? 118  SER D CB  1 
ATOM   11553 O  OG  . SER D  2  100 ? -4.785  -25.059 -25.493 1.00 61.08  ? 118  SER D OG  1 
ATOM   11554 N  N   . PHE D  2  101 ? -7.147  -21.839 -24.544 1.00 57.29  ? 119  PHE D N   1 
ATOM   11555 C  CA  . PHE D  2  101 ? -6.957  -20.736 -23.620 1.00 57.48  ? 119  PHE D CA  1 
ATOM   11556 C  C   . PHE D  2  101 ? -7.660  -21.002 -22.287 1.00 57.66  ? 119  PHE D C   1 
ATOM   11557 O  O   . PHE D  2  101 ? -8.431  -21.948 -22.160 1.00 57.06  ? 119  PHE D O   1 
ATOM   11558 C  CB  . PHE D  2  101 ? -7.453  -19.430 -24.252 1.00 56.22  ? 119  PHE D CB  1 
ATOM   11559 C  CG  . PHE D  2  101 ? -8.938  -19.382 -24.480 1.00 55.34  ? 119  PHE D CG  1 
ATOM   11560 C  CD1 . PHE D  2  101 ? -9.797  -18.994 -23.470 1.00 54.71  ? 119  PHE D CD1 1 
ATOM   11561 C  CD2 . PHE D  2  101 ? -9.472  -19.726 -25.711 1.00 55.90  ? 119  PHE D CD2 1 
ATOM   11562 C  CE1 . PHE D  2  101 ? -11.159 -18.959 -23.677 1.00 55.08  ? 119  PHE D CE1 1 
ATOM   11563 C  CE2 . PHE D  2  101 ? -10.837 -19.695 -25.930 1.00 55.19  ? 119  PHE D CE2 1 
ATOM   11564 C  CZ  . PHE D  2  101 ? -11.682 -19.310 -24.914 1.00 55.08  ? 119  PHE D CZ  1 
ATOM   11565 N  N   . SER D  2  102 ? -7.375  -20.166 -21.294 1.00 58.53  ? 120  SER D N   1 
ATOM   11566 C  CA  . SER D  2  102 ? -7.960  -20.300 -19.961 1.00 59.09  ? 120  SER D CA  1 
ATOM   11567 C  C   . SER D  2  102 ? -7.567  -19.098 -19.112 1.00 59.84  ? 120  SER D C   1 
ATOM   11568 O  O   . SER D  2  102 ? -6.503  -18.531 -19.313 1.00 60.97  ? 120  SER D O   1 
ATOM   11569 C  CB  . SER D  2  102 ? -7.450  -21.585 -19.302 1.00 59.73  ? 120  SER D CB  1 
ATOM   11570 O  OG  . SER D  2  102 ? -7.506  -21.500 -17.892 1.00 61.54  ? 120  SER D OG  1 
ATOM   11571 N  N   . PHE D  2  103 ? -8.426  -18.687 -18.187 1.00 61.30  ? 121  PHE D N   1 
ATOM   11572 C  CA  . PHE D  2  103 ? -8.114  -17.558 -17.308 1.00 63.44  ? 121  PHE D CA  1 
ATOM   11573 C  C   . PHE D  2  103 ? -9.126  -17.417 -16.189 1.00 65.87  ? 121  PHE D C   1 
ATOM   11574 O  O   . PHE D  2  103 ? -10.212 -18.001 -16.247 1.00 66.72  ? 121  PHE D O   1 
ATOM   11575 C  CB  . PHE D  2  103 ? -8.023  -16.244 -18.096 1.00 61.68  ? 121  PHE D CB  1 
ATOM   11576 C  CG  . PHE D  2  103 ? -9.321  -15.784 -18.681 1.00 60.56  ? 121  PHE D CG  1 
ATOM   11577 C  CD1 . PHE D  2  103 ? -10.198 -15.009 -17.934 1.00 59.80  ? 121  PHE D CD1 1 
ATOM   11578 C  CD2 . PHE D  2  103 ? -9.665  -16.116 -19.989 1.00 61.12  ? 121  PHE D CD2 1 
ATOM   11579 C  CE1 . PHE D  2  103 ? -11.406 -14.568 -18.480 1.00 60.64  ? 121  PHE D CE1 1 
ATOM   11580 C  CE2 . PHE D  2  103 ? -10.869 -15.686 -20.550 1.00 61.51  ? 121  PHE D CE2 1 
ATOM   11581 C  CZ  . PHE D  2  103 ? -11.746 -14.906 -19.791 1.00 61.51  ? 121  PHE D CZ  1 
ATOM   11582 N  N   . LYS D  2  104 ? -8.765  -16.650 -15.168 1.00 68.17  ? 122  LYS D N   1 
ATOM   11583 C  CA  . LYS D  2  104 ? -9.642  -16.437 -14.020 1.00 71.60  ? 122  LYS D CA  1 
ATOM   11584 C  C   . LYS D  2  104 ? -8.942  -15.502 -13.051 1.00 72.84  ? 122  LYS D C   1 
ATOM   11585 O  O   . LYS D  2  104 ? -7.762  -15.195 -13.222 1.00 73.81  ? 122  LYS D O   1 
ATOM   11586 C  CB  . LYS D  2  104 ? -9.936  -17.768 -13.299 1.00 72.26  ? 122  LYS D CB  1 
ATOM   11587 C  CG  . LYS D  2  104 ? -8.709  -18.408 -12.622 1.00 74.93  ? 122  LYS D CG  1 
ATOM   11588 C  CD  . LYS D  2  104 ? -9.042  -19.706 -11.858 1.00 77.33  ? 122  LYS D CD  1 
ATOM   11589 C  CE  . LYS D  2  104 ? -9.736  -19.445 -10.511 1.00 78.92  ? 122  LYS D CE  1 
ATOM   11590 N  NZ  . LYS D  2  104 ? -10.067 -20.713 -9.764  1.00 77.96  ? 122  LYS D NZ  1 
ATOM   11591 N  N   . GLY D  2  105 ? -9.672  -15.029 -12.047 1.00 73.31  ? 123  GLY D N   1 
ATOM   11592 C  CA  . GLY D  2  105 ? -9.052  -14.176 -11.054 1.00 73.26  ? 123  GLY D CA  1 
ATOM   11593 C  C   . GLY D  2  105 ? -9.265  -12.677 -11.072 1.00 73.28  ? 123  GLY D C   1 
ATOM   11594 O  O   . GLY D  2  105 ? -8.830  -12.010 -10.132 1.00 73.63  ? 123  GLY D O   1 
ATOM   11595 N  N   . ILE D  2  106 ? -9.900  -12.122 -12.101 1.00 72.46  ? 124  ILE D N   1 
ATOM   11596 C  CA  . ILE D  2  106 ? -10.107 -10.676 -12.093 1.00 72.16  ? 124  ILE D CA  1 
ATOM   11597 C  C   . ILE D  2  106 ? -11.538 -10.221 -12.300 1.00 71.91  ? 124  ILE D C   1 
ATOM   11598 O  O   . ILE D  2  106 ? -12.258 -10.745 -13.146 1.00 72.84  ? 124  ILE D O   1 
ATOM   11599 C  CB  . ILE D  2  106 ? -9.189  -9.956  -13.105 1.00 72.21  ? 124  ILE D CB  1 
ATOM   11600 C  CG1 . ILE D  2  106 ? -7.741  -10.021 -12.607 1.00 73.34  ? 124  ILE D CG1 1 
ATOM   11601 C  CG2 . ILE D  2  106 ? -9.610  -8.495  -13.255 1.00 70.11  ? 124  ILE D CG2 1 
ATOM   11602 C  CD1 . ILE D  2  106 ? -6.716  -9.301  -13.491 1.00 74.52  ? 124  ILE D CD1 1 
ATOM   11603 N  N   . LYS D  2  107 ? -11.938 -9.244  -11.492 1.00 71.78  ? 125  LYS D N   1 
ATOM   11604 C  CA  . LYS D  2  107 ? -13.274 -8.658  -11.539 1.00 71.74  ? 125  LYS D CA  1 
ATOM   11605 C  C   . LYS D  2  107 ? -13.208 -7.427  -12.428 1.00 71.99  ? 125  LYS D C   1 
ATOM   11606 O  O   . LYS D  2  107 ? -12.317 -6.589  -12.258 1.00 72.42  ? 125  LYS D O   1 
ATOM   11607 C  CB  . LYS D  2  107 ? -13.709 -8.237  -10.131 1.00 71.14  ? 125  LYS D CB  1 
ATOM   11608 C  CG  . LYS D  2  107 ? -15.051 -7.517  -10.029 1.00 70.80  ? 125  LYS D CG  1 
ATOM   11609 C  CD  . LYS D  2  107 ? -14.964 -6.422  -8.959  1.00 71.85  ? 125  LYS D CD  1 
ATOM   11610 C  CE  . LYS D  2  107 ? -16.327 -5.857  -8.559  1.00 72.59  ? 125  LYS D CE  1 
ATOM   11611 N  NZ  . LYS D  2  107 ? -17.141 -6.803  -7.717  1.00 72.65  ? 125  LYS D NZ  1 
ATOM   11612 N  N   . PHE D  2  108 ? -14.139 -7.323  -13.378 1.00 71.79  ? 126  PHE D N   1 
ATOM   11613 C  CA  . PHE D  2  108 ? -14.179 -6.178  -14.285 1.00 71.03  ? 126  PHE D CA  1 
ATOM   11614 C  C   . PHE D  2  108 ? -15.414 -5.330  -14.039 1.00 71.31  ? 126  PHE D C   1 
ATOM   11615 O  O   . PHE D  2  108 ? -16.456 -5.847  -13.624 1.00 70.82  ? 126  PHE D O   1 
ATOM   11616 C  CB  . PHE D  2  108 ? -14.209 -6.637  -15.736 1.00 70.33  ? 126  PHE D CB  1 
ATOM   11617 C  CG  . PHE D  2  108 ? -13.130 -7.604  -16.090 1.00 69.12  ? 126  PHE D CG  1 
ATOM   11618 C  CD1 . PHE D  2  108 ? -13.248 -8.954  -15.756 1.00 68.92  ? 126  PHE D CD1 1 
ATOM   11619 C  CD2 . PHE D  2  108 ? -11.986 -7.169  -16.751 1.00 67.85  ? 126  PHE D CD2 1 
ATOM   11620 C  CE1 . PHE D  2  108 ? -12.236 -9.861  -16.074 1.00 67.90  ? 126  PHE D CE1 1 
ATOM   11621 C  CE2 . PHE D  2  108 ? -10.970 -8.061  -17.073 1.00 67.46  ? 126  PHE D CE2 1 
ATOM   11622 C  CZ  . PHE D  2  108 ? -11.095 -9.416  -16.735 1.00 67.18  ? 126  PHE D CZ  1 
ATOM   11623 N  N   . SER D  2  109 ? -15.297 -4.029  -14.299 1.00 71.56  ? 127  SER D N   1 
ATOM   11624 C  CA  . SER D  2  109 ? -16.435 -3.132  -14.132 1.00 71.45  ? 127  SER D CA  1 
ATOM   11625 C  C   . SER D  2  109 ? -17.472 -3.548  -15.173 1.00 72.16  ? 127  SER D C   1 
ATOM   11626 O  O   . SER D  2  109 ? -17.214 -4.408  -16.024 1.00 71.09  ? 127  SER D O   1 
ATOM   11627 C  CB  . SER D  2  109 ? -16.047 -1.671  -14.394 1.00 70.49  ? 127  SER D CB  1 
ATOM   11628 O  OG  . SER D  2  109 ? -14.890 -1.286  -13.689 1.00 70.22  ? 127  SER D OG  1 
ATOM   11629 N  N   . LYS D  2  110 ? -18.646 -2.935  -15.094 1.00 72.80  ? 128  LYS D N   1 
ATOM   11630 C  CA  . LYS D  2  110 ? -19.713 -3.201  -16.039 1.00 72.87  ? 128  LYS D CA  1 
ATOM   11631 C  C   . LYS D  2  110 ? -19.498 -2.144  -17.123 1.00 71.93  ? 128  LYS D C   1 
ATOM   11632 O  O   . LYS D  2  110 ? -19.023 -1.045  -16.825 1.00 72.19  ? 128  LYS D O   1 
ATOM   11633 C  CB  . LYS D  2  110 ? -21.056 -3.008  -15.340 1.00 74.57  ? 128  LYS D CB  1 
ATOM   11634 C  CG  . LYS D  2  110 ? -22.272 -3.054  -16.248 1.00 79.14  ? 128  LYS D CG  1 
ATOM   11635 C  CD  . LYS D  2  110 ? -23.528 -2.620  -15.473 1.00 80.63  ? 128  LYS D CD  1 
ATOM   11636 C  CE  . LYS D  2  110 ? -24.786 -2.635  -16.336 1.00 80.17  ? 128  LYS D CE  1 
ATOM   11637 N  NZ  . LYS D  2  110 ? -25.989 -2.261  -15.538 1.00 80.10  ? 128  LYS D NZ  1 
ATOM   11638 N  N   . GLY D  2  111 ? -19.802 -2.456  -18.376 1.00 69.63  ? 129  GLY D N   1 
ATOM   11639 C  CA  . GLY D  2  111 ? -19.598 -1.440  -19.385 1.00 69.69  ? 129  GLY D CA  1 
ATOM   11640 C  C   . GLY D  2  111 ? -19.142 -1.912  -20.743 1.00 70.61  ? 129  GLY D C   1 
ATOM   11641 O  O   . GLY D  2  111 ? -19.326 -3.074  -21.096 1.00 71.14  ? 129  GLY D O   1 
ATOM   11642 N  N   . LYS D  2  112 ? -18.557 -0.992  -21.507 1.00 71.45  ? 130  LYS D N   1 
ATOM   11643 C  CA  . LYS D  2  112 ? -18.069 -1.280  -22.851 1.00 73.19  ? 130  LYS D CA  1 
ATOM   11644 C  C   . LYS D  2  112 ? -16.541 -1.284  -22.897 1.00 73.65  ? 130  LYS D C   1 
ATOM   11645 O  O   . LYS D  2  112 ? -15.887 -0.297  -22.531 1.00 74.49  ? 130  LYS D O   1 
ATOM   11646 C  CB  . LYS D  2  112 ? -18.626 -0.241  -23.846 1.00 73.95  ? 130  LYS D CB  1 
ATOM   11647 C  CG  . LYS D  2  112 ? -18.029 -0.294  -25.263 1.00 75.57  ? 130  LYS D CG  1 
ATOM   11648 C  CD  . LYS D  2  112 ? -18.820 0.546   -26.272 1.00 76.60  ? 130  LYS D CD  1 
ATOM   11649 C  CE  . LYS D  2  112 ? -20.150 -0.145  -26.632 1.00 79.49  ? 130  LYS D CE  1 
ATOM   11650 N  NZ  . LYS D  2  112 ? -20.997 0.593   -27.629 1.00 78.87  ? 130  LYS D NZ  1 
ATOM   11651 N  N   . TYR D  2  113 ? -15.980 -2.413  -23.327 1.00 73.04  ? 131  TYR D N   1 
ATOM   11652 C  CA  . TYR D  2  113 ? -14.535 -2.549  -23.454 1.00 71.26  ? 131  TYR D CA  1 
ATOM   11653 C  C   . TYR D  2  113 ? -14.165 -2.602  -24.921 1.00 71.15  ? 131  TYR D C   1 
ATOM   11654 O  O   . TYR D  2  113 ? -14.838 -3.250  -25.719 1.00 70.24  ? 131  TYR D O   1 
ATOM   11655 C  CB  . TYR D  2  113 ? -14.033 -3.821  -22.767 1.00 68.77  ? 131  TYR D CB  1 
ATOM   11656 C  CG  . TYR D  2  113 ? -14.120 -3.781  -21.264 1.00 67.31  ? 131  TYR D CG  1 
ATOM   11657 C  CD1 . TYR D  2  113 ? -15.238 -4.295  -20.591 1.00 65.84  ? 131  TYR D CD1 1 
ATOM   11658 C  CD2 . TYR D  2  113 ? -13.093 -3.211  -20.507 1.00 65.43  ? 131  TYR D CD2 1 
ATOM   11659 C  CE1 . TYR D  2  113 ? -15.328 -4.241  -19.204 1.00 63.85  ? 131  TYR D CE1 1 
ATOM   11660 C  CE2 . TYR D  2  113 ? -13.174 -3.153  -19.125 1.00 63.85  ? 131  TYR D CE2 1 
ATOM   11661 C  CZ  . TYR D  2  113 ? -14.292 -3.666  -18.477 1.00 63.87  ? 131  TYR D CZ  1 
ATOM   11662 O  OH  . TYR D  2  113 ? -14.380 -3.583  -17.105 1.00 63.65  ? 131  TYR D OH  1 
ATOM   11663 N  N   . LYS D  2  114 ? -13.106 -1.897  -25.282 1.00 72.04  ? 132  LYS D N   1 
ATOM   11664 C  CA  . LYS D  2  114 ? -12.654 -1.935  -26.651 1.00 74.23  ? 132  LYS D CA  1 
ATOM   11665 C  C   . LYS D  2  114 ? -11.151 -2.206  -26.583 1.00 74.36  ? 132  LYS D C   1 
ATOM   11666 O  O   . LYS D  2  114 ? -10.420 -1.569  -25.812 1.00 74.61  ? 132  LYS D O   1 
ATOM   11667 C  CB  . LYS D  2  114 ? -13.004 -0.620  -27.389 1.00 76.64  ? 132  LYS D CB  1 
ATOM   11668 C  CG  . LYS D  2  114 ? -12.001 0.532   -27.289 1.00 81.33  ? 132  LYS D CG  1 
ATOM   11669 C  CD  . LYS D  2  114 ? -10.908 0.424   -28.360 1.00 84.42  ? 132  LYS D CD  1 
ATOM   11670 C  CE  . LYS D  2  114 ? -9.986  1.652   -28.373 1.00 86.86  ? 132  LYS D CE  1 
ATOM   11671 N  NZ  . LYS D  2  114 ? -10.663 2.908   -28.864 1.00 88.35  ? 132  LYS D NZ  1 
ATOM   11672 N  N   . CYS D  2  115 ? -10.707 -3.197  -27.355 1.00 73.42  ? 133  CYS D N   1 
ATOM   11673 C  CA  . CYS D  2  115 ? -9.300  -3.575  -27.385 1.00 72.55  ? 133  CYS D CA  1 
ATOM   11674 C  C   . CYS D  2  115 ? -8.719  -3.616  -28.791 1.00 70.17  ? 133  CYS D C   1 
ATOM   11675 O  O   . CYS D  2  115 ? -9.095  -4.464  -29.604 1.00 69.62  ? 133  CYS D O   1 
ATOM   11676 C  CB  . CYS D  2  115 ? -9.106  -4.947  -26.737 1.00 73.73  ? 133  CYS D CB  1 
ATOM   11677 S  SG  . CYS D  2  115 ? -7.371  -5.506  -26.752 1.00 78.36  ? 133  CYS D SG  1 
ATOM   11678 N  N   . VAL D  2  116 ? -7.807  -2.692  -29.077 1.00 67.25  ? 134  VAL D N   1 
ATOM   11679 C  CA  . VAL D  2  116 ? -7.167  -2.666  -30.377 1.00 64.82  ? 134  VAL D CA  1 
ATOM   11680 C  C   . VAL D  2  116 ? -6.021  -3.643  -30.275 1.00 63.99  ? 134  VAL D C   1 
ATOM   11681 O  O   . VAL D  2  116 ? -5.165  -3.517  -29.402 1.00 62.92  ? 134  VAL D O   1 
ATOM   11682 C  CB  . VAL D  2  116 ? -6.623  -1.274  -30.723 1.00 64.05  ? 134  VAL D CB  1 
ATOM   11683 C  CG1 . VAL D  2  116 ? -5.751  -1.343  -31.964 1.00 61.67  ? 134  VAL D CG1 1 
ATOM   11684 C  CG2 . VAL D  2  116 ? -7.774  -0.334  -30.953 1.00 62.99  ? 134  VAL D CG2 1 
ATOM   11685 N  N   . VAL D  2  117 ? -6.033  -4.633  -31.158 1.00 63.78  ? 135  VAL D N   1 
ATOM   11686 C  CA  . VAL D  2  117 ? -5.004  -5.651  -31.192 1.00 63.97  ? 135  VAL D CA  1 
ATOM   11687 C  C   . VAL D  2  117 ? -4.244  -5.565  -32.506 1.00 64.33  ? 135  VAL D C   1 
ATOM   11688 O  O   . VAL D  2  117 ? -4.666  -6.094  -33.528 1.00 63.54  ? 135  VAL D O   1 
ATOM   11689 C  CB  . VAL D  2  117 ? -5.625  -7.058  -30.989 1.00 63.66  ? 135  VAL D CB  1 
ATOM   11690 C  CG1 . VAL D  2  117 ? -6.886  -7.178  -31.788 1.00 64.87  ? 135  VAL D CG1 1 
ATOM   11691 C  CG2 . VAL D  2  117 ? -4.642  -8.145  -31.380 1.00 63.96  ? 135  VAL D CG2 1 
ATOM   11692 N  N   . GLU D  2  118 ? -3.125  -4.850  -32.454 1.00 66.40  ? 136  GLU D N   1 
ATOM   11693 C  CA  . GLU D  2  118 ? -2.239  -4.641  -33.593 1.00 67.63  ? 136  GLU D CA  1 
ATOM   11694 C  C   . GLU D  2  118 ? -1.236  -5.790  -33.584 1.00 67.47  ? 136  GLU D C   1 
ATOM   11695 O  O   . GLU D  2  118 ? -0.455  -5.922  -32.646 1.00 67.89  ? 136  GLU D O   1 
ATOM   11696 C  CB  . GLU D  2  118 ? -1.533  -3.285  -33.432 1.00 68.38  ? 136  GLU D CB  1 
ATOM   11697 C  CG  . GLU D  2  118 ? -0.230  -3.109  -34.195 1.00 71.07  ? 136  GLU D CG  1 
ATOM   11698 C  CD  . GLU D  2  118 ? 0.415   -1.755  -33.920 1.00 73.46  ? 136  GLU D CD  1 
ATOM   11699 O  OE1 . GLU D  2  118 ? 0.486   -1.358  -32.736 1.00 74.26  ? 136  GLU D OE1 1 
ATOM   11700 O  OE2 . GLU D  2  118 ? 0.860   -1.087  -34.882 1.00 75.00  ? 136  GLU D OE2 1 
ATOM   11701 N  N   . ALA D  2  119 ? -1.284  -6.636  -34.612 1.00 67.24  ? 137  ALA D N   1 
ATOM   11702 C  CA  . ALA D  2  119 ? -0.376  -7.775  -34.712 1.00 67.34  ? 137  ALA D CA  1 
ATOM   11703 C  C   . ALA D  2  119 ? 0.870   -7.384  -35.496 1.00 67.71  ? 137  ALA D C   1 
ATOM   11704 O  O   . ALA D  2  119 ? 0.785   -6.637  -36.467 1.00 68.52  ? 137  ALA D O   1 
ATOM   11705 C  CB  . ALA D  2  119 ? -1.072  -8.937  -35.387 1.00 66.40  ? 137  ALA D CB  1 
ATOM   11706 N  N   . ILE D  2  120 ? 2.026   -7.888  -35.075 1.00 68.16  ? 138  ILE D N   1 
ATOM   11707 C  CA  . ILE D  2  120 ? 3.289   -7.564  -35.738 1.00 68.68  ? 138  ILE D CA  1 
ATOM   11708 C  C   . ILE D  2  120 ? 4.197   -8.791  -35.831 1.00 70.30  ? 138  ILE D C   1 
ATOM   11709 O  O   . ILE D  2  120 ? 4.298   -9.573  -34.881 1.00 70.33  ? 138  ILE D O   1 
ATOM   11710 C  CB  . ILE D  2  120 ? 4.023   -6.436  -34.980 1.00 67.52  ? 138  ILE D CB  1 
ATOM   11711 C  CG1 . ILE D  2  120 ? 3.131   -5.192  -34.925 1.00 66.54  ? 138  ILE D CG1 1 
ATOM   11712 C  CG2 . ILE D  2  120 ? 5.340   -6.119  -35.660 1.00 66.00  ? 138  ILE D CG2 1 
ATOM   11713 C  CD1 . ILE D  2  120 ? 3.643   -4.121  -34.002 1.00 67.48  ? 138  ILE D CD1 1 
ATOM   11714 N  N   . SER D  2  121 ? 4.853   -8.952  -36.978 1.00 71.79  ? 139  SER D N   1 
ATOM   11715 C  CA  . SER D  2  121 ? 5.740   -10.085 -37.195 1.00 74.61  ? 139  SER D CA  1 
ATOM   11716 C  C   . SER D  2  121 ? 6.682   -9.878  -38.369 1.00 76.82  ? 139  SER D C   1 
ATOM   11717 O  O   . SER D  2  121 ? 6.595   -8.880  -39.084 1.00 75.97  ? 139  SER D O   1 
ATOM   11718 C  CB  . SER D  2  121 ? 4.926   -11.350 -37.448 1.00 74.95  ? 139  SER D CB  1 
ATOM   11719 O  OG  . SER D  2  121 ? 4.274   -11.281 -38.702 1.00 73.75  ? 139  SER D OG  1 
ATOM   11720 N  N   . GLY D  2  122 ? 7.566   -10.852 -38.571 1.00 79.54  ? 140  GLY D N   1 
ATOM   11721 C  CA  . GLY D  2  122 ? 8.525   -10.783 -39.655 1.00 83.39  ? 140  GLY D CA  1 
ATOM   11722 C  C   . GLY D  2  122 ? 9.898   -10.402 -39.141 1.00 86.45  ? 140  GLY D C   1 
ATOM   11723 O  O   . GLY D  2  122 ? 10.027  -9.900  -38.015 1.00 85.62  ? 140  GLY D O   1 
ATOM   11724 N  N   . SER D  2  123 ? 10.927  -10.647 -39.955 1.00 89.25  ? 141  SER D N   1 
ATOM   11725 C  CA  . SER D  2  123 ? 12.301  -10.313 -39.577 1.00 90.60  ? 141  SER D CA  1 
ATOM   11726 C  C   . SER D  2  123 ? 12.464  -8.804  -39.412 1.00 91.06  ? 141  SER D C   1 
ATOM   11727 O  O   . SER D  2  123 ? 12.946  -8.350  -38.375 1.00 91.15  ? 141  SER D O   1 
ATOM   11728 C  CB  . SER D  2  123 ? 13.296  -10.862 -40.610 1.00 90.86  ? 141  SER D CB  1 
ATOM   11729 O  OG  . SER D  2  123 ? 12.747  -10.856 -41.917 1.00 91.34  ? 141  SER D OG  1 
ATOM   11730 N  N   . PRO D  2  124 ? 12.070  -8.007  -40.425 1.00 91.24  ? 142  PRO D N   1 
ATOM   11731 C  CA  . PRO D  2  124 ? 12.225  -6.563  -40.238 1.00 91.85  ? 142  PRO D CA  1 
ATOM   11732 C  C   . PRO D  2  124 ? 11.004  -6.067  -39.445 1.00 92.51  ? 142  PRO D C   1 
ATOM   11733 O  O   . PRO D  2  124 ? 10.933  -4.912  -39.010 1.00 93.20  ? 142  PRO D O   1 
ATOM   11734 C  CB  . PRO D  2  124 ? 12.248  -6.020  -41.672 1.00 91.59  ? 142  PRO D CB  1 
ATOM   11735 C  CG  . PRO D  2  124 ? 12.415  -7.252  -42.549 1.00 91.20  ? 142  PRO D CG  1 
ATOM   11736 C  CD  . PRO D  2  124 ? 11.657  -8.300  -41.803 1.00 90.83  ? 142  PRO D CD  1 
ATOM   11737 N  N   . GLU D  2  125 ? 10.056  -6.986  -39.259 1.00 91.45  ? 143  GLU D N   1 
ATOM   11738 C  CA  . GLU D  2  125 ? 8.802   -6.766  -38.540 1.00 89.84  ? 143  GLU D CA  1 
ATOM   11739 C  C   . GLU D  2  125 ? 8.000   -5.534  -38.947 1.00 89.28  ? 143  GLU D C   1 
ATOM   11740 O  O   . GLU D  2  125 ? 8.416   -4.396  -38.755 1.00 89.14  ? 143  GLU D O   1 
ATOM   11741 C  CB  . GLU D  2  125 ? 9.020   -6.775  -37.015 1.00 88.43  ? 143  GLU D CB  1 
ATOM   11742 C  CG  . GLU D  2  125 ? 9.698   -5.566  -36.405 1.00 87.39  ? 143  GLU D CG  1 
ATOM   11743 C  CD  . GLU D  2  125 ? 9.485   -5.505  -34.898 1.00 88.06  ? 143  GLU D CD  1 
ATOM   11744 O  OE1 . GLU D  2  125 ? 9.866   -6.466  -34.201 1.00 88.22  ? 143  GLU D OE1 1 
ATOM   11745 O  OE2 . GLU D  2  125 ? 8.926   -4.501  -34.406 1.00 87.79  ? 143  GLU D OE2 1 
ATOM   11746 N  N   . GLU D  2  126 ? 6.832   -5.799  -39.518 1.00 88.53  ? 144  GLU D N   1 
ATOM   11747 C  CA  . GLU D  2  126 ? 5.908   -4.778  -39.973 1.00 87.85  ? 144  GLU D CA  1 
ATOM   11748 C  C   . GLU D  2  126 ? 4.543   -5.299  -39.575 1.00 85.89  ? 144  GLU D C   1 
ATOM   11749 O  O   . GLU D  2  126 ? 4.401   -6.484  -39.301 1.00 86.27  ? 144  GLU D O   1 
ATOM   11750 C  CB  . GLU D  2  126 ? 5.997   -4.634  -41.480 1.00 90.86  ? 144  GLU D CB  1 
ATOM   11751 C  CG  . GLU D  2  126 ? 7.430   -4.527  -41.957 1.00 97.45  ? 144  GLU D CG  1 
ATOM   11752 C  CD  . GLU D  2  126 ? 7.536   -4.222  -43.438 1.00 101.56 ? 144  GLU D CD  1 
ATOM   11753 O  OE1 . GLU D  2  126 ? 7.045   -5.034  -44.260 1.00 103.45 ? 144  GLU D OE1 1 
ATOM   11754 O  OE2 . GLU D  2  126 ? 8.113   -3.164  -43.781 1.00 103.80 ? 144  GLU D OE2 1 
ATOM   11755 N  N   . MET D  2  127 ? 3.536   -4.437  -39.549 1.00 83.29  ? 145  MET D N   1 
ATOM   11756 C  CA  . MET D  2  127 ? 2.209   -4.863  -39.131 1.00 80.55  ? 145  MET D CA  1 
ATOM   11757 C  C   . MET D  2  127 ? 1.628   -5.972  -39.980 1.00 78.25  ? 145  MET D C   1 
ATOM   11758 O  O   . MET D  2  127 ? 1.770   -5.965  -41.193 1.00 78.26  ? 145  MET D O   1 
ATOM   11759 C  CB  . MET D  2  127 ? 1.246   -3.693  -39.135 1.00 82.22  ? 145  MET D CB  1 
ATOM   11760 C  CG  . MET D  2  127 ? -0.063  -4.045  -38.476 1.00 85.31  ? 145  MET D CG  1 
ATOM   11761 S  SD  . MET D  2  127 ? -1.415  -3.011  -39.020 1.00 90.23  ? 145  MET D SD  1 
ATOM   11762 C  CE  . MET D  2  127 ? -1.799  -3.811  -40.633 1.00 87.60  ? 145  MET D CE  1 
ATOM   11763 N  N   . LEU D  2  128 ? 0.969   -6.924  -39.324 1.00 76.11  ? 146  LEU D N   1 
ATOM   11764 C  CA  . LEU D  2  128 ? 0.349   -8.057  -40.004 1.00 74.53  ? 146  LEU D CA  1 
ATOM   11765 C  C   . LEU D  2  128 ? -1.122  -7.700  -40.249 1.00 74.20  ? 146  LEU D C   1 
ATOM   11766 O  O   . LEU D  2  128 ? -1.615  -7.789  -41.379 1.00 74.64  ? 146  LEU D O   1 
ATOM   11767 C  CB  . LEU D  2  128 ? 0.445   -9.316  -39.130 1.00 73.59  ? 146  LEU D CB  1 
ATOM   11768 C  CG  . LEU D  2  128 ? 0.572   -10.693 -39.793 1.00 73.24  ? 146  LEU D CG  1 
ATOM   11769 C  CD1 . LEU D  2  128 ? 0.085   -11.744 -38.806 1.00 72.32  ? 146  LEU D CD1 1 
ATOM   11770 C  CD2 . LEU D  2  128 ? -0.248  -10.764 -41.077 1.00 75.02  ? 146  LEU D CD2 1 
ATOM   11771 N  N   . PHE D  2  129 ? -1.816  -7.317  -39.178 1.00 73.01  ? 147  PHE D N   1 
ATOM   11772 C  CA  . PHE D  2  129 ? -3.213  -6.907  -39.240 1.00 71.21  ? 147  PHE D CA  1 
ATOM   11773 C  C   . PHE D  2  129 ? -3.564  -6.132  -37.981 1.00 71.59  ? 147  PHE D C   1 
ATOM   11774 O  O   . PHE D  2  129 ? -2.856  -6.199  -36.979 1.00 71.64  ? 147  PHE D O   1 
ATOM   11775 C  CB  . PHE D  2  129 ? -4.141  -8.113  -39.388 1.00 69.83  ? 147  PHE D CB  1 
ATOM   11776 C  CG  . PHE D  2  129 ? -4.138  -9.051  -38.205 1.00 69.67  ? 147  PHE D CG  1 
ATOM   11777 C  CD1 . PHE D  2  129 ? -4.737  -8.685  -36.996 1.00 68.81  ? 147  PHE D CD1 1 
ATOM   11778 C  CD2 . PHE D  2  129 ? -3.556  -10.316 -38.308 1.00 68.96  ? 147  PHE D CD2 1 
ATOM   11779 C  CE1 . PHE D  2  129 ? -4.755  -9.563  -35.904 1.00 67.29  ? 147  PHE D CE1 1 
ATOM   11780 C  CE2 . PHE D  2  129 ? -3.569  -11.199 -37.228 1.00 67.93  ? 147  PHE D CE2 1 
ATOM   11781 C  CZ  . PHE D  2  129 ? -4.172  -10.822 -36.019 1.00 66.70  ? 147  PHE D CZ  1 
ATOM   11782 N  N   . CYS D  2  130 ? -4.646  -5.375  -38.047 1.00 72.26  ? 148  CYS D N   1 
ATOM   11783 C  CA  . CYS D  2  130 ? -5.096  -4.594  -36.913 1.00 73.34  ? 148  CYS D CA  1 
ATOM   11784 C  C   . CYS D  2  130 ? -6.586  -4.851  -36.788 1.00 71.70  ? 148  CYS D C   1 
ATOM   11785 O  O   . CYS D  2  130 ? -7.307  -4.772  -37.772 1.00 71.02  ? 148  CYS D O   1 
ATOM   11786 C  CB  . CYS D  2  130 ? -4.842  -3.105  -37.152 1.00 76.55  ? 148  CYS D CB  1 
ATOM   11787 S  SG  . CYS D  2  130 ? -5.217  -2.041  -35.708 1.00 83.82  ? 148  CYS D SG  1 
ATOM   11788 N  N   . LEU D  2  131 ? -7.040  -5.173  -35.584 1.00 71.06  ? 149  LEU D N   1 
ATOM   11789 C  CA  . LEU D  2  131 ? -8.451  -5.432  -35.342 1.00 71.53  ? 149  LEU D CA  1 
ATOM   11790 C  C   . LEU D  2  131 ? -8.873  -4.666  -34.107 1.00 73.72  ? 149  LEU D C   1 
ATOM   11791 O  O   . LEU D  2  131 ? -8.080  -4.512  -33.174 1.00 74.70  ? 149  LEU D O   1 
ATOM   11792 C  CB  . LEU D  2  131 ? -8.681  -6.913  -35.082 1.00 69.69  ? 149  LEU D CB  1 
ATOM   11793 C  CG  . LEU D  2  131 ? -8.429  -7.895  -36.216 1.00 68.71  ? 149  LEU D CG  1 
ATOM   11794 C  CD1 . LEU D  2  131 ? -8.546  -9.309  -35.688 1.00 68.50  ? 149  LEU D CD1 1 
ATOM   11795 C  CD2 . LEU D  2  131 ? -9.432  -7.655  -37.311 1.00 67.85  ? 149  LEU D CD2 1 
ATOM   11796 N  N   . GLU D  2  132 ? -10.108 -4.170  -34.094 1.00 75.73  ? 150  GLU D N   1 
ATOM   11797 C  CA  . GLU D  2  132 ? -10.608 -3.457  -32.917 1.00 76.80  ? 150  GLU D CA  1 
ATOM   11798 C  C   . GLU D  2  132 ? -11.759 -4.271  -32.331 1.00 74.81  ? 150  GLU D C   1 
ATOM   11799 O  O   . GLU D  2  132 ? -12.828 -4.388  -32.939 1.00 74.12  ? 150  GLU D O   1 
ATOM   11800 C  CB  . GLU D  2  132 ? -11.093 -2.045  -33.263 1.00 79.10  ? 150  GLU D CB  1 
ATOM   11801 C  CG  . GLU D  2  132 ? -11.302 -1.186  -32.020 1.00 84.95  ? 150  GLU D CG  1 
ATOM   11802 C  CD  . GLU D  2  132 ? -12.142 0.054   -32.277 1.00 89.25  ? 150  GLU D CD  1 
ATOM   11803 O  OE1 . GLU D  2  132 ? -13.317 -0.108  -32.689 1.00 91.57  ? 150  GLU D OE1 1 
ATOM   11804 O  OE2 . GLU D  2  132 ? -11.633 1.184   -32.069 1.00 90.76  ? 150  GLU D OE2 1 
ATOM   11805 N  N   . PHE D  2  133 ? -11.517 -4.853  -31.158 1.00 72.89  ? 151  PHE D N   1 
ATOM   11806 C  CA  . PHE D  2  133 ? -12.511 -5.681  -30.487 1.00 71.49  ? 151  PHE D CA  1 
ATOM   11807 C  C   . PHE D  2  133 ? -13.414 -4.911  -29.552 1.00 71.84  ? 151  PHE D C   1 
ATOM   11808 O  O   . PHE D  2  133 ? -12.950 -4.155  -28.706 1.00 72.47  ? 151  PHE D O   1 
ATOM   11809 C  CB  . PHE D  2  133 ? -11.839 -6.803  -29.694 1.00 67.66  ? 151  PHE D CB  1 
ATOM   11810 C  CG  . PHE D  2  133 ? -11.345 -7.940  -30.539 1.00 64.32  ? 151  PHE D CG  1 
ATOM   11811 C  CD1 . PHE D  2  133 ? -10.108 -7.867  -31.192 1.00 63.08  ? 151  PHE D CD1 1 
ATOM   11812 C  CD2 . PHE D  2  133 ? -12.123 -9.091  -30.683 1.00 61.74  ? 151  PHE D CD2 1 
ATOM   11813 C  CE1 . PHE D  2  133 ? -9.650  -8.930  -31.983 1.00 62.97  ? 151  PHE D CE1 1 
ATOM   11814 C  CE2 . PHE D  2  133 ? -11.682 -10.161 -31.468 1.00 62.08  ? 151  PHE D CE2 1 
ATOM   11815 C  CZ  . PHE D  2  133 ? -10.439 -10.086 -32.122 1.00 63.04  ? 151  PHE D CZ  1 
ATOM   11816 N  N   . VAL D  2  134 ? -14.713 -5.118  -29.711 1.00 72.88  ? 152  VAL D N   1 
ATOM   11817 C  CA  . VAL D  2  134 ? -15.700 -4.466  -28.863 1.00 74.44  ? 152  VAL D CA  1 
ATOM   11818 C  C   . VAL D  2  134 ? -16.379 -5.574  -28.065 1.00 74.70  ? 152  VAL D C   1 
ATOM   11819 O  O   . VAL D  2  134 ? -17.044 -6.463  -28.620 1.00 74.43  ? 152  VAL D O   1 
ATOM   11820 C  CB  . VAL D  2  134 ? -16.748 -3.685  -29.699 1.00 74.98  ? 152  VAL D CB  1 
ATOM   11821 C  CG1 . VAL D  2  134 ? -17.889 -3.202  -28.794 1.00 74.88  ? 152  VAL D CG1 1 
ATOM   11822 C  CG2 . VAL D  2  134 ? -16.076 -2.511  -30.397 1.00 74.14  ? 152  VAL D CG2 1 
ATOM   11823 N  N   . ILE D  2  135 ? -16.190 -5.519  -26.755 1.00 74.24  ? 153  ILE D N   1 
ATOM   11824 C  CA  . ILE D  2  135 ? -16.746 -6.524  -25.876 1.00 73.49  ? 153  ILE D CA  1 
ATOM   11825 C  C   . ILE D  2  135 ? -17.588 -5.882  -24.771 1.00 72.76  ? 153  ILE D C   1 
ATOM   11826 O  O   . ILE D  2  135 ? -17.095 -5.097  -23.959 1.00 71.33  ? 153  ILE D O   1 
ATOM   11827 C  CB  . ILE D  2  135 ? -15.582 -7.395  -25.331 1.00 73.68  ? 153  ILE D CB  1 
ATOM   11828 C  CG1 . ILE D  2  135 ? -16.045 -8.280  -24.186 1.00 73.14  ? 153  ILE D CG1 1 
ATOM   11829 C  CG2 . ILE D  2  135 ? -14.414 -6.512  -24.938 1.00 72.58  ? 153  ILE D CG2 1 
ATOM   11830 C  CD1 . ILE D  2  135 ? -14.986 -9.269  -23.792 1.00 73.88  ? 153  ILE D CD1 1 
ATOM   11831 N  N   . LEU D  2  136 ? -18.881 -6.193  -24.783 1.00 72.62  ? 154  LEU D N   1 
ATOM   11832 C  CA  . LEU D  2  136 ? -19.806 -5.646  -23.799 1.00 73.50  ? 154  LEU D CA  1 
ATOM   11833 C  C   . LEU D  2  136 ? -19.871 -6.587  -22.610 1.00 74.14  ? 154  LEU D C   1 
ATOM   11834 O  O   . LEU D  2  136 ? -20.005 -7.792  -22.781 1.00 73.99  ? 154  LEU D O   1 
ATOM   11835 C  CB  . LEU D  2  136 ? -21.214 -5.486  -24.393 1.00 73.58  ? 154  LEU D CB  1 
ATOM   11836 C  CG  . LEU D  2  136 ? -21.492 -4.587  -25.612 1.00 74.19  ? 154  LEU D CG  1 
ATOM   11837 C  CD1 . LEU D  2  136 ? -20.692 -3.271  -25.510 1.00 74.06  ? 154  LEU D CD1 1 
ATOM   11838 C  CD2 . LEU D  2  136 ? -21.131 -5.332  -26.889 1.00 74.15  ? 154  LEU D CD2 1 
ATOM   11839 N  N   . HIS D  2  137 ? -19.803 -6.031  -21.406 1.00 75.50  ? 155  HIS D N   1 
ATOM   11840 C  CA  . HIS D  2  137 ? -19.839 -6.836  -20.197 1.00 78.15  ? 155  HIS D CA  1 
ATOM   11841 C  C   . HIS D  2  137 ? -20.972 -6.481  -19.231 1.00 81.70  ? 155  HIS D C   1 
ATOM   11842 O  O   . HIS D  2  137 ? -21.144 -5.322  -18.830 1.00 81.16  ? 155  HIS D O   1 
ATOM   11843 C  CB  . HIS D  2  137 ? -18.492 -6.723  -19.480 1.00 76.93  ? 155  HIS D CB  1 
ATOM   11844 C  CG  . HIS D  2  137 ? -18.416 -7.501  -18.203 1.00 76.33  ? 155  HIS D CG  1 
ATOM   11845 N  ND1 . HIS D  2  137 ? -18.634 -8.860  -18.145 1.00 75.88  ? 155  HIS D ND1 1 
ATOM   11846 C  CD2 . HIS D  2  137 ? -18.125 -7.112  -16.938 1.00 75.46  ? 155  HIS D CD2 1 
ATOM   11847 C  CE1 . HIS D  2  137 ? -18.481 -9.276  -16.901 1.00 74.56  ? 155  HIS D CE1 1 
ATOM   11848 N  NE2 . HIS D  2  137 ? -18.171 -8.236  -16.149 1.00 74.82  ? 155  HIS D NE2 1 
ATOM   11849 N  N   . GLN D  2  138 ? -21.744 -7.501  -18.871 1.00 86.06  ? 156  GLN D N   1 
ATOM   11850 C  CA  . GLN D  2  138 ? -22.848 -7.358  -17.932 1.00 91.21  ? 156  GLN D CA  1 
ATOM   11851 C  C   . GLN D  2  138 ? -22.617 -8.398  -16.833 1.00 94.88  ? 156  GLN D C   1 
ATOM   11852 O  O   . GLN D  2  138 ? -22.925 -9.577  -17.019 1.00 95.65  ? 156  GLN D O   1 
ATOM   11853 C  CB  . GLN D  2  138 ? -24.185 -7.616  -18.633 1.00 91.68  ? 156  GLN D CB  1 
ATOM   11854 C  CG  . GLN D  2  138 ? -25.392 -7.590  -17.695 1.00 93.84  ? 156  GLN D CG  1 
ATOM   11855 C  CD  . GLN D  2  138 ? -25.491 -6.292  -16.892 1.00 95.86  ? 156  GLN D CD  1 
ATOM   11856 O  OE1 . GLN D  2  138 ? -25.633 -5.203  -17.463 1.00 96.66  ? 156  GLN D OE1 1 
ATOM   11857 N  NE2 . GLN D  2  138 ? -25.410 -6.403  -15.562 1.00 95.11  ? 156  GLN D NE2 1 
ATOM   11858 N  N   . PRO D  2  139 ? -22.068 -7.972  -15.674 1.00 98.26  ? 157  PRO D N   1 
ATOM   11859 C  CA  . PRO D  2  139 ? -21.787 -8.870  -14.543 1.00 101.00 ? 157  PRO D CA  1 
ATOM   11860 C  C   . PRO D  2  139 ? -22.984 -9.577  -13.898 1.00 103.82 ? 157  PRO D C   1 
ATOM   11861 O  O   . PRO D  2  139 ? -24.072 -9.653  -14.485 1.00 104.07 ? 157  PRO D O   1 
ATOM   11862 C  CB  . PRO D  2  139 ? -21.051 -7.961  -13.558 1.00 100.29 ? 157  PRO D CB  1 
ATOM   11863 C  CG  . PRO D  2  139 ? -21.658 -6.624  -13.825 1.00 99.76  ? 157  PRO D CG  1 
ATOM   11864 C  CD  . PRO D  2  139 ? -21.698 -6.584  -15.336 1.00 98.50  ? 157  PRO D CD  1 
ATOM   11865 N  N   . ASN D  2  140 ? -22.757 -10.102 -12.690 1.00 106.91 ? 158  ASN D N   1 
ATOM   11866 C  CA  . ASN D  2  140 ? -23.768 -10.822 -11.902 1.00 109.78 ? 158  ASN D CA  1 
ATOM   11867 C  C   . ASN D  2  140 ? -24.263 -12.114 -12.572 1.00 111.17 ? 158  ASN D C   1 
ATOM   11868 O  O   . ASN D  2  140 ? -24.043 -13.197 -11.976 1.00 111.75 ? 158  ASN D O   1 
ATOM   11869 C  CB  . ASN D  2  140 ? -24.964 -9.903  -11.594 1.00 110.35 ? 158  ASN D CB  1 
ATOM   11870 C  CG  . ASN D  2  140 ? -26.100 -10.632 -10.883 1.00 110.44 ? 158  ASN D CG  1 
ATOM   11871 O  OD1 . ASN D  2  140 ? -25.946 -11.087 -9.752  1.00 110.76 ? 158  ASN D OD1 1 
ATOM   11872 N  ND2 . ASN D  2  140 ? -27.246 -10.750 -11.555 1.00 110.04 ? 158  ASN D ND2 1 
HETATM 11873 C  C1  . PA1 E  3  .   ? 23.778  -10.778 8.188   1.00 80.45  ? 1    PA1 E C1  1 
HETATM 11874 O  O1  . PA1 E  3  .   ? 23.915  -11.358 6.885   1.00 82.40  ? 1    PA1 E O1  1 
HETATM 11875 C  C2  . PA1 E  3  .   ? 24.671  -9.536  8.447   1.00 80.80  ? 1    PA1 E C2  1 
HETATM 11876 N  N2  . PA1 E  3  .   ? 24.625  -8.426  7.445   1.00 84.12  ? 1    PA1 E N2  1 
HETATM 11877 C  C3  . PA1 E  3  .   ? 26.126  -10.038 8.445   1.00 78.06  ? 1    PA1 E C3  1 
HETATM 11878 O  O3  . PA1 E  3  .   ? 27.029  -8.973  8.716   1.00 78.74  ? 1    PA1 E O3  1 
HETATM 11879 C  C4  . PA1 E  3  .   ? 26.471  -11.168 9.429   1.00 76.42  ? 1    PA1 E C4  1 
HETATM 11880 O  O4  . PA1 E  3  .   ? 27.692  -11.800 9.079   1.00 76.11  ? 1    PA1 E O4  1 
HETATM 11881 C  C5  . PA1 E  3  .   ? 25.402  -12.240 9.403   1.00 75.74  ? 1    PA1 E C5  1 
HETATM 11882 O  O5  . PA1 E  3  .   ? 24.083  -11.658 9.313   1.00 78.42  ? 1    PA1 E O5  1 
HETATM 11883 C  C6  . PA1 E  3  .   ? 25.508  -13.074 10.681  1.00 72.87  ? 1    PA1 E C6  1 
HETATM 11884 O  O6  . PA1 E  3  .   ? 25.190  -12.394 11.891  1.00 69.86  ? 1    PA1 E O6  1 
HETATM 11885 C  C1  . PA1 E  3  .   ? 25.754  -12.616 13.183  1.00 69.49  ? 2    PA1 E C1  1 
HETATM 11886 C  C2  . PA1 E  3  .   ? 25.496  -11.517 14.229  1.00 68.65  ? 2    PA1 E C2  1 
HETATM 11887 N  N2  . PA1 E  3  .   ? 26.020  -10.315 13.568  1.00 69.28  ? 2    PA1 E N2  1 
HETATM 11888 C  C3  . PA1 E  3  .   ? 26.128  -11.883 15.600  1.00 68.94  ? 2    PA1 E C3  1 
HETATM 11889 O  O3  . PA1 E  3  .   ? 25.892  -10.808 16.498  1.00 67.58  ? 2    PA1 E O3  1 
HETATM 11890 C  C4  . PA1 E  3  .   ? 25.386  -13.166 16.016  1.00 70.23  ? 2    PA1 E C4  1 
HETATM 11891 O  O4  . PA1 E  3  .   ? 25.823  -13.599 17.286  1.00 69.35  ? 2    PA1 E O4  1 
HETATM 11892 C  C5  . PA1 E  3  .   ? 25.730  -14.280 15.007  1.00 72.35  ? 2    PA1 E C5  1 
HETATM 11893 O  O5  . PA1 E  3  .   ? 25.291  -13.846 13.732  1.00 69.92  ? 2    PA1 E O5  1 
HETATM 11894 C  C6  . PA1 E  3  .   ? 25.089  -15.619 15.314  1.00 78.78  ? 2    PA1 E C6  1 
HETATM 11895 O  O6  . PA1 E  3  .   ? 25.470  -16.568 14.310  1.00 87.25  ? 2    PA1 E O6  1 
HETATM 11896 C  C1  . KDO E  3  .   ? 25.546  -18.664 15.195  1.00 94.70  ? 3    KDO E C1  1 
HETATM 11897 O  O1A . KDO E  3  .   ? 26.719  -18.792 15.602  1.00 96.42  ? 3    KDO E O1A 1 
HETATM 11898 O  O1B . KDO E  3  .   ? 24.545  -19.114 15.818  1.00 95.53  ? 3    KDO E O1B 1 
HETATM 11899 C  C2  . KDO E  3  .   ? 25.304  -17.918 13.889  1.00 93.28  ? 3    KDO E C2  1 
HETATM 11900 C  C3  . KDO E  3  .   ? 26.216  -18.552 12.829  1.00 95.86  ? 3    KDO E C3  1 
HETATM 11901 C  C4  . KDO E  3  .   ? 26.004  -17.807 11.500  1.00 100.74 ? 3    KDO E C4  1 
HETATM 11902 O  O4  . KDO E  3  .   ? 26.826  -18.394 10.436  1.00 104.42 ? 3    KDO E O4  1 
HETATM 11903 C  C5  . KDO E  3  .   ? 24.486  -17.810 11.117  1.00 101.61 ? 3    KDO E C5  1 
HETATM 11904 O  O5  . KDO E  3  .   ? 24.014  -19.102 10.745  1.00 107.68 ? 3    KDO E O5  1 
HETATM 11905 C  C6  . KDO E  3  .   ? 23.668  -17.143 12.291  1.00 98.14  ? 3    KDO E C6  1 
HETATM 11906 O  O6  . KDO E  3  .   ? 23.923  -17.827 13.523  1.00 96.05  ? 3    KDO E O6  1 
HETATM 11907 C  C7  . KDO E  3  .   ? 22.129  -17.108 12.068  1.00 96.39  ? 3    KDO E C7  1 
HETATM 11908 O  O7  . KDO E  3  .   ? 21.827  -16.419 10.876  1.00 94.13  ? 3    KDO E O7  1 
HETATM 11909 C  C8  . KDO E  3  .   ? 21.368  -16.434 13.235  1.00 96.52  ? 3    KDO E C8  1 
HETATM 11910 O  O8  . KDO E  3  .   ? 20.000  -16.825 13.378  1.00 95.98  ? 3    KDO E O8  1 
HETATM 11911 C  C1  . GMH E  3  .   ? 23.356  -19.645 9.615   1.00 116.77 ? 4    GMH E C1  1 
HETATM 11912 C  C2  . GMH E  3  .   ? 23.729  -21.128 9.574   1.00 119.02 ? 4    GMH E C2  1 
HETATM 11913 C  C3  . GMH E  3  .   ? 24.909  -21.391 8.631   1.00 122.26 ? 4    GMH E C3  1 
HETATM 11914 C  C4  . GMH E  3  .   ? 24.706  -20.801 7.239   1.00 123.48 ? 4    GMH E C4  1 
HETATM 11915 C  C5  . GMH E  3  .   ? 24.487  -19.271 7.404   1.00 123.80 ? 4    GMH E C5  1 
HETATM 11916 C  C6  . GMH E  3  .   ? 24.288  -18.602 6.037   1.00 126.08 ? 4    GMH E C6  1 
HETATM 11917 C  C7  . GMH E  3  .   ? 24.052  -17.090 6.104   1.00 126.90 ? 4    GMH E C7  1 
HETATM 11918 O  O2  . GMH E  3  .   ? 22.582  -21.849 9.183   1.00 119.45 ? 4    GMH E O2  1 
HETATM 11919 O  O3  . GMH E  3  .   ? 25.135  -22.816 8.604   1.00 124.49 ? 4    GMH E O3  1 
HETATM 11920 O  O4  . GMH E  3  .   ? 25.821  -21.028 6.381   1.00 125.70 ? 4    GMH E O4  1 
HETATM 11921 O  O5  . GMH E  3  .   ? 23.353  -19.091 8.280   1.00 121.81 ? 4    GMH E O5  1 
HETATM 11922 O  O6  . GMH E  3  .   ? 23.188  -19.198 5.346   1.00 127.07 ? 4    GMH E O6  1 
HETATM 11923 O  O7  . GMH E  3  .   ? 23.879  -16.554 4.802   1.00 127.76 ? 4    GMH E O7  1 
HETATM 11924 C  C1  . GMH E  3  .   ? 26.255  -23.366 9.301   1.00 128.77 ? 5    GMH E C1  1 
HETATM 11925 C  C2  . GMH E  3  .   ? 26.628  -24.754 8.750   1.00 129.76 ? 5    GMH E C2  1 
HETATM 11926 C  C3  . GMH E  3  .   ? 25.901  -25.877 9.503   1.00 130.48 ? 5    GMH E C3  1 
HETATM 11927 C  C4  . GMH E  3  .   ? 26.103  -25.799 11.024  1.00 131.36 ? 5    GMH E C4  1 
HETATM 11928 C  C5  . GMH E  3  .   ? 25.528  -24.425 11.485  1.00 131.37 ? 5    GMH E C5  1 
HETATM 11929 C  C6  . GMH E  3  .   ? 25.658  -24.220 13.022  1.00 131.61 ? 5    GMH E C6  1 
HETATM 11930 C  C7  . GMH E  3  .   ? 25.050  -22.864 13.496  1.00 131.63 ? 5    GMH E C7  1 
HETATM 11931 O  O2  . GMH E  3  .   ? 28.045  -24.910 8.846   1.00 128.59 ? 5    GMH E O2  1 
HETATM 11932 O  O3  . GMH E  3  .   ? 26.356  -27.108 8.945   1.00 130.60 ? 5    GMH E O3  1 
HETATM 11933 O  O4  . GMH E  3  .   ? 25.422  -26.837 11.727  1.00 131.26 ? 5    GMH E O4  1 
HETATM 11934 O  O5  . GMH E  3  .   ? 26.236  -23.395 10.741  1.00 131.35 ? 5    GMH E O5  1 
HETATM 11935 O  O6  . GMH E  3  .   ? 27.035  -24.244 13.383  1.00 130.98 ? 5    GMH E O6  1 
HETATM 11936 O  O7  . GMH E  3  .   ? 25.102  -22.543 14.913  1.00 131.25 ? 5    GMH E O7  1 
HETATM 11937 C  C1  . GMH E  3  .   ? 25.340  -23.515 15.922  1.00 132.86 ? 6    GMH E C1  1 
HETATM 11938 C  C2  . GMH E  3  .   ? 24.406  -23.351 17.140  1.00 133.64 ? 6    GMH E C2  1 
HETATM 11939 C  C3  . GMH E  3  .   ? 24.771  -22.141 18.014  1.00 134.51 ? 6    GMH E C3  1 
HETATM 11940 C  C4  . GMH E  3  .   ? 26.247  -22.088 18.417  1.00 134.38 ? 6    GMH E C4  1 
HETATM 11941 C  C5  . GMH E  3  .   ? 27.034  -22.016 17.078  1.00 133.38 ? 6    GMH E C5  1 
HETATM 11942 C  C6  . GMH E  3  .   ? 28.532  -21.919 17.319  1.00 133.40 ? 6    GMH E C6  1 
HETATM 11943 C  C7  . GMH E  3  .   ? 29.339  -21.836 16.026  1.00 132.75 ? 6    GMH E C7  1 
HETATM 11944 O  O2  . GMH E  3  .   ? 24.433  -24.543 17.913  1.00 133.08 ? 6    GMH E O2  1 
HETATM 11945 O  O3  . GMH E  3  .   ? 23.874  -22.166 19.131  1.00 134.60 ? 6    GMH E O3  1 
HETATM 11946 O  O4  . GMH E  3  .   ? 26.557  -20.947 19.225  1.00 134.25 ? 6    GMH E O4  1 
HETATM 11947 O  O5  . GMH E  3  .   ? 26.695  -23.193 16.292  1.00 133.38 ? 6    GMH E O5  1 
HETATM 11948 O  O6  . GMH E  3  .   ? 28.987  -23.052 18.061  1.00 132.96 ? 6    GMH E O6  1 
HETATM 11949 O  O7  . GMH E  3  .   ? 30.716  -21.741 16.310  1.00 132.53 ? 6    GMH E O7  1 
HETATM 11950 C  C1  . KDO E  3  .   ? 27.989  -16.441 9.813   1.00 111.83 ? 7    KDO E C1  1 
HETATM 11951 O  O1A . KDO E  3  .   ? 27.364  -16.295 8.723   1.00 113.08 ? 7    KDO E O1A 1 
HETATM 11952 O  O1B . KDO E  3  .   ? 28.452  -15.478 10.478  1.00 111.01 ? 7    KDO E O1B 1 
HETATM 11953 C  C2  . KDO E  3  .   ? 28.206  -17.859 10.360  1.00 109.82 ? 7    KDO E C2  1 
HETATM 11954 C  C3  . KDO E  3  .   ? 28.522  -18.791 9.173   1.00 110.52 ? 7    KDO E C3  1 
HETATM 11955 C  C4  . KDO E  3  .   ? 28.810  -20.203 9.683   1.00 110.64 ? 7    KDO E C4  1 
HETATM 11956 O  O4  . KDO E  3  .   ? 29.101  -21.083 8.600   1.00 109.71 ? 7    KDO E O4  1 
HETATM 11957 C  C5  . KDO E  3  .   ? 29.994  -20.116 10.673  1.00 110.11 ? 7    KDO E C5  1 
HETATM 11958 O  O5  . KDO E  3  .   ? 31.182  -19.730 9.996   1.00 109.86 ? 7    KDO E O5  1 
HETATM 11959 C  C6  . KDO E  3  .   ? 29.650  -19.121 11.820  1.00 110.58 ? 7    KDO E C6  1 
HETATM 11960 O  O6  . KDO E  3  .   ? 29.316  -17.835 11.271  1.00 110.82 ? 7    KDO E O6  1 
HETATM 11961 C  C7  . KDO E  3  .   ? 30.812  -18.981 12.798  1.00 111.49 ? 7    KDO E C7  1 
HETATM 11962 O  O7  . KDO E  3  .   ? 31.125  -20.263 13.344  1.00 110.87 ? 7    KDO E O7  1 
HETATM 11963 C  C8  . KDO E  3  .   ? 30.439  -18.007 13.921  1.00 111.93 ? 7    KDO E C8  1 
HETATM 11964 O  O8  . KDO E  3  .   ? 31.507  -17.851 14.834  1.00 112.93 ? 7    KDO E O8  1 
HETATM 11965 C  C1  . NAG F  4  .   ? 2.840   16.580  4.599   1.00 75.76  ? 1    NAG F C1  1 
HETATM 11966 C  C2  . NAG F  4  .   ? 2.718   16.600  6.130   1.00 77.24  ? 1    NAG F C2  1 
HETATM 11967 C  C3  . NAG F  4  .   ? 4.061   16.948  6.797   1.00 77.00  ? 1    NAG F C3  1 
HETATM 11968 C  C4  . NAG F  4  .   ? 5.182   16.030  6.300   1.00 77.36  ? 1    NAG F C4  1 
HETATM 11969 C  C5  . NAG F  4  .   ? 5.178   16.068  4.754   1.00 76.20  ? 1    NAG F C5  1 
HETATM 11970 C  C6  . NAG F  4  .   ? 6.211   15.169  4.103   1.00 76.12  ? 1    NAG F C6  1 
HETATM 11971 C  C7  . NAG F  4  .   ? 0.472   17.186  6.755   1.00 82.44  ? 1    NAG F C7  1 
HETATM 11972 C  C8  . NAG F  4  .   ? -0.488  18.224  7.324   1.00 82.22  ? 1    NAG F C8  1 
HETATM 11973 N  N2  . NAG F  4  .   ? 1.725   17.571  6.537   1.00 80.13  ? 1    NAG F N2  1 
HETATM 11974 O  O3  . NAG F  4  .   ? 3.933   16.804  8.199   1.00 78.79  ? 1    NAG F O3  1 
HETATM 11975 O  O4  . NAG F  4  .   ? 6.472   16.478  6.820   1.00 80.03  ? 1    NAG F O4  1 
HETATM 11976 O  O5  . NAG F  4  .   ? 3.882   15.672  4.231   1.00 75.32  ? 1    NAG F O5  1 
HETATM 11977 O  O6  . NAG F  4  .   ? 5.813   14.772  2.794   1.00 75.33  ? 1    NAG F O6  1 
HETATM 11978 O  O7  . NAG F  4  .   ? 0.076   16.037  6.513   1.00 84.59  ? 1    NAG F O7  1 
HETATM 11979 C  C1  . NAG F  4  .   ? 6.870   16.162  8.137   1.00 83.72  ? 2    NAG F C1  1 
HETATM 11980 C  C2  . NAG F  4  .   ? 8.428   15.972  8.187   1.00 84.62  ? 2    NAG F C2  1 
HETATM 11981 C  C3  . NAG F  4  .   ? 9.032   16.099  9.604   1.00 85.90  ? 2    NAG F C3  1 
HETATM 11982 C  C4  . NAG F  4  .   ? 8.494   17.305  10.353  1.00 87.40  ? 2    NAG F C4  1 
HETATM 11983 C  C5  . NAG F  4  .   ? 6.962   17.176  10.355  1.00 87.43  ? 2    NAG F C5  1 
HETATM 11984 C  C6  . NAG F  4  .   ? 6.266   18.272  11.161  1.00 87.77  ? 2    NAG F C6  1 
HETATM 11985 C  C7  . NAG F  4  .   ? 8.179   14.079  6.683   1.00 86.12  ? 2    NAG F C7  1 
HETATM 11986 C  C8  . NAG F  4  .   ? 7.115   13.034  7.002   1.00 84.91  ? 2    NAG F C8  1 
HETATM 11987 N  N2  . NAG F  4  .   ? 8.795   14.648  7.715   1.00 85.63  ? 2    NAG F N2  1 
HETATM 11988 O  O3  . NAG F  4  .   ? 10.443  16.177  9.509   1.00 86.24  ? 2    NAG F O3  1 
HETATM 11989 O  O4  . NAG F  4  .   ? 9.020   17.319  11.683  1.00 85.97  ? 2    NAG F O4  1 
HETATM 11990 O  O5  . NAG F  4  .   ? 6.461   17.257  8.989   1.00 86.29  ? 2    NAG F O5  1 
HETATM 11991 O  O6  . NAG F  4  .   ? 6.158   19.492  10.427  1.00 86.36  ? 2    NAG F O6  1 
HETATM 11992 O  O7  . NAG F  4  .   ? 8.446   14.355  5.509   1.00 85.92  ? 2    NAG F O7  1 
HETATM 11993 C  C1  . NAG G  4  .   ? 2.572   22.826  7.326   1.00 109.39 ? 1    NAG G C1  1 
HETATM 11994 C  C2  . NAG G  4  .   ? 3.503   21.818  8.039   1.00 110.65 ? 1    NAG G C2  1 
HETATM 11995 C  C3  . NAG G  4  .   ? 2.721   20.625  8.661   1.00 112.01 ? 1    NAG G C3  1 
HETATM 11996 C  C4  . NAG G  4  .   ? 1.463   21.098  9.446   1.00 113.43 ? 1    NAG G C4  1 
HETATM 11997 C  C5  . NAG G  4  .   ? 0.653   22.047  8.556   1.00 112.17 ? 1    NAG G C5  1 
HETATM 11998 C  C6  . NAG G  4  .   ? -0.585  22.591  9.241   1.00 111.91 ? 1    NAG G C6  1 
HETATM 11999 C  C7  . NAG G  4  .   ? 5.791   21.565  7.318   1.00 108.79 ? 1    NAG G C7  1 
HETATM 12000 C  C8  . NAG G  4  .   ? 6.385   22.824  6.706   1.00 108.33 ? 1    NAG G C8  1 
HETATM 12001 N  N2  . NAG G  4  .   ? 4.500   21.317  7.105   1.00 109.34 ? 1    NAG G N2  1 
HETATM 12002 O  O3  . NAG G  4  .   ? 3.586   19.922  9.545   1.00 111.99 ? 1    NAG G O3  1 
HETATM 12003 O  O4  . NAG G  4  .   ? 0.632   19.967  9.839   1.00 115.68 ? 1    NAG G O4  1 
HETATM 12004 O  O5  . NAG G  4  .   ? 1.465   23.180  8.179   1.00 110.80 ? 1    NAG G O5  1 
HETATM 12005 O  O6  . NAG G  4  .   ? -0.254  23.305  10.427  1.00 111.51 ? 1    NAG G O6  1 
HETATM 12006 O  O7  . NAG G  4  .   ? 6.510   20.825  7.994   1.00 108.33 ? 1    NAG G O7  1 
HETATM 12007 C  C1  . NAG G  4  .   ? 0.809   19.417  11.114  1.00 117.58 ? 2    NAG G C1  1 
HETATM 12008 C  C2  . NAG G  4  .   ? -0.567  18.981  11.684  1.00 117.85 ? 2    NAG G C2  1 
HETATM 12009 C  C3  . NAG G  4  .   ? -0.462  17.937  12.835  1.00 118.71 ? 2    NAG G C3  1 
HETATM 12010 C  C4  . NAG G  4  .   ? 0.610   16.867  12.574  1.00 118.90 ? 2    NAG G C4  1 
HETATM 12011 C  C5  . NAG G  4  .   ? 1.903   17.575  12.217  1.00 118.35 ? 2    NAG G C5  1 
HETATM 12012 C  C6  . NAG G  4  .   ? 3.060   16.619  12.020  1.00 117.56 ? 2    NAG G C6  1 
HETATM 12013 C  C7  . NAG G  4  .   ? -2.431  20.528  11.763  1.00 118.31 ? 2    NAG G C7  1 
HETATM 12014 C  C8  . NAG G  4  .   ? -3.645  20.193  12.624  1.00 118.18 ? 2    NAG G C8  1 
HETATM 12015 N  N2  . NAG G  4  .   ? -1.232  20.161  12.211  1.00 118.09 ? 2    NAG G N2  1 
HETATM 12016 O  O3  . NAG G  4  .   ? -1.720  17.299  13.010  1.00 119.11 ? 2    NAG G O3  1 
HETATM 12017 O  O4  . NAG G  4  .   ? 0.792   16.050  13.726  1.00 118.89 ? 2    NAG G O4  1 
HETATM 12018 O  O5  . NAG G  4  .   ? 1.715   18.300  10.986  1.00 118.80 ? 2    NAG G O5  1 
HETATM 12019 O  O6  . NAG G  4  .   ? 3.922   16.636  13.142  1.00 116.62 ? 2    NAG G O6  1 
HETATM 12020 O  O7  . NAG G  4  .   ? -2.586  21.128  10.700  1.00 118.16 ? 2    NAG G O7  1 
HETATM 12021 C  C1  . PA1 H  5  .   ? -1.361  -16.210 -14.352 1.00 79.39  ? 1    PA1 H C1  1 
HETATM 12022 O  O1  . PA1 H  5  .   ? -1.499  -16.121 -12.938 1.00 81.14  ? 1    PA1 H O1  1 
HETATM 12023 C  C2  . PA1 H  5  .   ? -2.243  -15.225 -15.165 1.00 79.86  ? 1    PA1 H C2  1 
HETATM 12024 N  N2  . PA1 H  5  .   ? -2.186  -13.789 -14.797 1.00 83.21  ? 1    PA1 H N2  1 
HETATM 12025 C  C3  . PA1 H  5  .   ? -3.702  -15.649 -14.938 1.00 78.00  ? 1    PA1 H C3  1 
HETATM 12026 O  O3  . PA1 H  5  .   ? -4.593  -14.822 -15.674 1.00 77.54  ? 1    PA1 H O3  1 
HETATM 12027 C  C4  . PA1 H  5  .   ? -4.054  -17.102 -15.293 1.00 76.48  ? 1    PA1 H C4  1 
HETATM 12028 O  O4  . PA1 H  5  .   ? -5.297  -17.482 -14.719 1.00 76.47  ? 1    PA1 H O4  1 
HETATM 12029 C  C5  . PA1 H  5  .   ? -2.997  -18.051 -14.756 1.00 76.04  ? 1    PA1 H C5  1 
HETATM 12030 O  O5  . PA1 H  5  .   ? -1.673  -17.505 -14.934 1.00 77.86  ? 1    PA1 H O5  1 
HETATM 12031 C  C6  . PA1 H  5  .   ? -3.101  -19.388 -15.495 1.00 74.08  ? 1    PA1 H C6  1 
HETATM 12032 O  O6  . PA1 H  5  .   ? -2.801  -19.345 -16.889 1.00 71.53  ? 1    PA1 H O6  1 
HETATM 12033 C  C1  . GCS H  5  .   ? -3.365  -20.140 -17.931 1.00 70.47  ? 2    GCS H C1  1 
HETATM 12034 C  C2  . GCS H  5  .   ? -3.096  -19.656 -19.362 1.00 69.62  ? 2    GCS H C2  1 
HETATM 12035 C  C3  . GCS H  5  .   ? -3.734  -20.616 -20.417 1.00 69.52  ? 2    GCS H C3  1 
HETATM 12036 C  C4  . GCS H  5  .   ? -3.008  -21.950 -20.195 1.00 71.62  ? 2    GCS H C4  1 
HETATM 12037 C  C5  . GCS H  5  .   ? -3.360  -22.462 -18.776 1.00 73.93  ? 2    GCS H C5  1 
HETATM 12038 C  C6  . GCS H  5  .   ? -2.734  -23.804 -18.424 1.00 79.74  ? 2    GCS H C6  1 
HETATM 12039 N  N2  . GCS H  5  .   ? -3.608  -18.276 -19.334 1.00 69.46  ? 2    GCS H N2  1 
HETATM 12040 O  O3  . GCS H  5  .   ? -3.502  -20.087 -21.712 1.00 67.12  ? 2    GCS H O3  1 
HETATM 12041 O  O4  . GCS H  5  .   ? -3.452  -22.920 -21.119 1.00 71.75  ? 2    GCS H O4  1 
HETATM 12042 O  O5  . GCS H  5  .   ? -2.914  -21.486 -17.841 1.00 71.95  ? 2    GCS H O5  1 
HETATM 12043 O  O6  . GCS H  5  .   ? -3.110  -24.169 -17.096 1.00 88.40  ? 2    GCS H O6  1 
HETATM 12044 C  C1  . KDO H  5  .   ? -3.215  -26.436 -16.914 1.00 96.63  ? 3    KDO H C1  1 
HETATM 12045 O  O1A . KDO H  5  .   ? -2.214  -27.137 -17.263 1.00 97.67  ? 3    KDO H O1A 1 
HETATM 12046 O  O1B . KDO H  5  .   ? -4.404  -26.725 -17.218 1.00 96.98  ? 3    KDO H O1B 1 
HETATM 12047 C  C2  . KDO H  5  .   ? -2.956  -25.166 -16.093 1.00 94.86  ? 3    KDO H C2  1 
HETATM 12048 C  C3  . KDO H  5  .   ? -3.874  -25.231 -14.857 1.00 97.13  ? 3    KDO H C3  1 
HETATM 12049 C  C4  . KDO H  5  .   ? -3.652  -23.955 -14.028 1.00 101.51 ? 3    KDO H C4  1 
HETATM 12050 O  O4  . KDO H  5  .   ? -4.482  -23.974 -12.815 1.00 105.15 ? 3    KDO H O4  1 
HETATM 12051 C  C5  . KDO H  5  .   ? -2.134  -23.793 -13.687 1.00 102.27 ? 3    KDO H C5  1 
HETATM 12052 O  O5  . KDO H  5  .   ? -1.667  -24.770 -12.759 1.00 107.81 ? 3    KDO H O5  1 
HETATM 12053 C  C6  . KDO H  5  .   ? -1.315  -23.752 -15.034 1.00 98.70  ? 3    KDO H C6  1 
HETATM 12054 O  O6  . KDO H  5  .   ? -1.574  -24.924 -15.805 1.00 96.50  ? 3    KDO H O6  1 
HETATM 12055 C  C7  . KDO H  5  .   ? 0.226   -23.630 -14.848 1.00 97.63  ? 3    KDO H C7  1 
HETATM 12056 O  O7  . KDO H  5  .   ? 0.541   -22.461 -14.110 1.00 95.41  ? 3    KDO H O7  1 
HETATM 12057 C  C8  . KDO H  5  .   ? 0.990   -23.585 -16.189 1.00 97.22  ? 3    KDO H C8  1 
HETATM 12058 O  O8  . KDO H  5  .   ? 2.353   -24.004 -16.122 1.00 96.44  ? 3    KDO H O8  1 
HETATM 12059 C  C1  . GMH H  5  .   ? -1.015  -24.731 -11.497 1.00 116.44 ? 4    GMH H C1  1 
HETATM 12060 C  C2  . GMH H  5  .   ? -1.405  -26.023 -10.771 1.00 119.09 ? 4    GMH H C2  1 
HETATM 12061 C  C3  . GMH H  5  .   ? -2.588  -25.808 -9.819  1.00 122.60 ? 4    GMH H C3  1 
HETATM 12062 C  C4  . GMH H  5  .   ? -2.380  -24.637 -8.858  1.00 123.89 ? 4    GMH H C4  1 
HETATM 12063 C  C5  . GMH H  5  .   ? -2.145  -23.363 -9.716  1.00 123.81 ? 4    GMH H C5  1 
HETATM 12064 C  C6  . GMH H  5  .   ? -1.938  -22.132 -8.819  1.00 125.87 ? 4    GMH H C6  1 
HETATM 12065 C  C7  . GMH H  5  .   ? -1.681  -20.829 -9.582  1.00 126.02 ? 4    GMH H C7  1 
HETATM 12066 O  O2  . GMH H  5  .   ? -0.266  -26.499 -10.088 1.00 119.19 ? 4    GMH H O2  1 
HETATM 12067 O  O3  . GMH H  5  .   ? -2.825  -27.064 -9.139  1.00 125.45 ? 4    GMH H O3  1 
HETATM 12068 O  O4  . GMH H  5  .   ? -3.498  -24.426 -7.998  1.00 125.56 ? 4    GMH H O4  1 
HETATM 12069 O  O5  . GMH H  5  .   ? -1.010  -23.622 -10.576 1.00 121.30 ? 4    GMH H O5  1 
HETATM 12070 O  O6  . GMH H  5  .   ? -0.849  -22.347 -7.921  1.00 127.13 ? 4    GMH H O6  1 
HETATM 12071 O  O7  . GMH H  5  .   ? -1.507  -19.754 -8.678  1.00 126.22 ? 4    GMH H O7  1 
HETATM 12072 C  C1  . GMH H  5  .   ? -3.958  -27.859 -9.495  1.00 129.06 ? 5    GMH H C1  1 
HETATM 12073 C  C2  . GMH H  5  .   ? -4.344  -28.827 -8.364  1.00 130.02 ? 5    GMH H C2  1 
HETATM 12074 C  C3  . GMH H  5  .   ? -3.622  -30.172 -8.505  1.00 130.56 ? 5    GMH H C3  1 
HETATM 12075 C  C4  . GMH H  5  .   ? -3.825  -30.808 -9.890  1.00 131.35 ? 5    GMH H C4  1 
HETATM 12076 C  C5  . GMH H  5  .   ? -3.240  -29.813 -10.933 1.00 131.10 ? 5    GMH H C5  1 
HETATM 12077 C  C6  . GMH H  5  .   ? -3.374  -30.347 -12.389 1.00 131.55 ? 5    GMH H C6  1 
HETATM 12078 C  C7  . GMH H  5  .   ? -2.756  -29.372 -13.444 1.00 131.51 ? 5    GMH H C7  1 
HETATM 12079 O  O2  . GMH H  5  .   ? -5.763  -29.007 -8.386  1.00 128.97 ? 5    GMH H O2  1 
HETATM 12080 O  O3  . GMH H  5  .   ? -4.086  -30.998 -7.435  1.00 130.56 ? 5    GMH H O3  1 
HETATM 12081 O  O4  . GMH H  5  .   ? -3.147  -32.053 -10.023 1.00 130.84 ? 5    GMH H O4  1 
HETATM 12082 O  O5  . GMH H  5  .   ? -3.943  -28.558 -10.753 1.00 131.09 ? 5    GMH H O5  1 
HETATM 12083 O  O6  . GMH H  5  .   ? -4.755  -30.526 -12.697 1.00 131.32 ? 5    GMH H O6  1 
HETATM 12084 O  O7  . GMH H  5  .   ? -2.810  -29.744 -14.851 1.00 130.22 ? 5    GMH H O7  1 
HETATM 12085 C  C1  . GMH H  5  .   ? -3.055  -31.071 -15.293 1.00 132.15 ? 6    GMH H C1  1 
HETATM 12086 C  C2  . GMH H  5  .   ? -2.124  -31.498 -16.444 1.00 132.93 ? 6    GMH H C2  1 
HETATM 12087 C  C3  . GMH H  5  .   ? -2.483  -30.837 -17.779 1.00 134.14 ? 6    GMH H C3  1 
HETATM 12088 C  C4  . GMH H  5  .   ? -3.960  -30.967 -18.162 1.00 133.97 ? 6    GMH H C4  1 
HETATM 12089 C  C5  . GMH H  5  .   ? -4.738  -30.273 -17.013 1.00 133.15 ? 6    GMH H C5  1 
HETATM 12090 C  C6  . GMH H  5  .   ? -6.233  -30.285 -17.279 1.00 133.45 ? 6    GMH H C6  1 
HETATM 12091 C  C7  . GMH H  5  .   ? -7.036  -29.599 -16.177 1.00 133.13 ? 6    GMH H C7  1 
HETATM 12092 O  O2  . GMH H  5  .   ? -2.160  -32.912 -16.568 1.00 132.72 ? 6    GMH H O2  1 
HETATM 12093 O  O3  . GMH H  5  .   ? -1.588  -31.387 -18.751 1.00 134.09 ? 6    GMH H O3  1 
HETATM 12094 O  O4  . GMH H  5  .   ? -4.269  -30.329 -19.409 1.00 133.34 ? 6    GMH H O4  1 
HETATM 12095 O  O5  . GMH H  5  .   ? -4.406  -30.949 -15.770 1.00 132.39 ? 6    GMH H O5  1 
HETATM 12096 O  O6  . GMH H  5  .   ? -6.697  -31.630 -17.410 1.00 133.05 ? 6    GMH H O6  1 
HETATM 12097 O  O7  . GMH H  5  .   ? -8.411  -29.630 -16.474 1.00 132.86 ? 6    GMH H O7  1 
HETATM 12098 C  C1  . KDO H  5  .   ? -5.625  -21.944 -13.182 1.00 111.42 ? 7    KDO H C1  1 
HETATM 12099 O  O1A . KDO H  5  .   ? -6.088  -21.398 -14.216 1.00 110.40 ? 7    KDO H O1A 1 
HETATM 12100 O  O1B . KDO H  5  .   ? -4.991  -21.310 -12.290 1.00 112.29 ? 7    KDO H O1B 1 
HETATM 12101 C  C2  . KDO H  5  .   ? -5.860  -23.454 -13.003 1.00 109.75 ? 7    KDO H C2  1 
HETATM 12102 C  C3  . KDO H  5  .   ? -6.175  -23.724 -11.515 1.00 110.19 ? 7    KDO H C3  1 
HETATM 12103 C  C4  . KDO H  5  .   ? -6.479  -25.203 -11.312 1.00 110.25 ? 7    KDO H C4  1 
HETATM 12104 O  O4  . KDO H  5  .   ? -6.767  -25.470 -9.946  1.00 109.85 ? 7    KDO H O4  1 
HETATM 12105 C  C5  . KDO H  5  .   ? -7.671  -25.574 -12.229 1.00 110.37 ? 7    KDO H C5  1 
HETATM 12106 O  O5  . KDO H  5  .   ? -8.853  -24.897 -11.812 1.00 109.74 ? 7    KDO H O5  1 
HETATM 12107 C  C6  . KDO H  5  .   ? -7.325  -25.236 -13.708 1.00 110.82 ? 7    KDO H C6  1 
HETATM 12108 O  O6  . KDO H  5  .   ? -6.975  -23.843 -13.824 1.00 110.81 ? 7    KDO H O6  1 
HETATM 12109 C  C7  . KDO H  5  .   ? -8.491  -25.555 -14.643 1.00 111.36 ? 7    KDO H C7  1 
HETATM 12110 O  O7  . KDO H  5  .   ? -8.813  -26.941 -14.539 1.00 110.87 ? 7    KDO H O7  1 
HETATM 12111 C  C8  . KDO H  5  .   ? -8.119  -25.215 -16.087 1.00 112.05 ? 7    KDO H C8  1 
HETATM 12112 O  O8  . KDO H  5  .   ? -9.196  -25.494 -16.962 1.00 112.57 ? 7    KDO H O8  1 
HETATM 12113 C  C1  . NAG I  4  .   ? 19.729  9.538   -23.702 1.00 79.47  ? 1    NAG I C1  1 
HETATM 12114 C  C2  . NAG I  4  .   ? 19.723  8.866   -25.075 1.00 79.35  ? 1    NAG I C2  1 
HETATM 12115 C  C3  . NAG I  4  .   ? 18.325  8.928   -25.694 1.00 80.75  ? 1    NAG I C3  1 
HETATM 12116 C  C4  . NAG I  4  .   ? 17.242  8.428   -24.724 1.00 82.54  ? 1    NAG I C4  1 
HETATM 12117 C  C5  . NAG I  4  .   ? 17.417  9.022   -23.314 1.00 82.21  ? 1    NAG I C5  1 
HETATM 12118 C  C6  . NAG I  4  .   ? 16.545  8.290   -22.314 1.00 82.41  ? 1    NAG I C6  1 
HETATM 12119 C  C7  . NAG I  4  .   ? 21.713  8.860   -26.422 1.00 79.72  ? 1    NAG I C7  1 
HETATM 12120 C  C8  . NAG I  4  .   ? 22.801  9.660   -27.137 1.00 79.26  ? 1    NAG I C8  1 
HETATM 12121 N  N2  . NAG I  4  .   ? 20.659  9.525   -25.959 1.00 78.83  ? 1    NAG I N2  1 
HETATM 12122 O  O3  . NAG I  4  .   ? 18.293  8.130   -26.868 1.00 79.68  ? 1    NAG I O3  1 
HETATM 12123 O  O4  . NAG I  4  .   ? 15.947  8.824   -25.216 1.00 86.77  ? 1    NAG I O4  1 
HETATM 12124 O  O5  . NAG I  4  .   ? 18.779  8.893   -22.847 1.00 80.71  ? 1    NAG I O5  1 
HETATM 12125 O  O6  . NAG I  4  .   ? 16.083  9.162   -21.298 1.00 84.12  ? 1    NAG I O6  1 
HETATM 12126 O  O7  . NAG I  4  .   ? 21.842  7.642   -26.283 1.00 80.18  ? 1    NAG I O7  1 
HETATM 12127 C  C1  . NAG I  4  .   ? 15.286  7.991   -26.103 1.00 91.70  ? 2    NAG I C1  1 
HETATM 12128 C  C2  . NAG I  4  .   ? 13.772  8.255   -26.006 1.00 94.52  ? 2    NAG I C2  1 
HETATM 12129 C  C3  . NAG I  4  .   ? 13.049  7.373   -27.039 1.00 94.71  ? 2    NAG I C3  1 
HETATM 12130 C  C4  . NAG I  4  .   ? 13.561  7.769   -28.428 1.00 95.10  ? 2    NAG I C4  1 
HETATM 12131 C  C5  . NAG I  4  .   ? 15.081  7.522   -28.468 1.00 95.34  ? 2    NAG I C5  1 
HETATM 12132 C  C6  . NAG I  4  .   ? 15.703  7.896   -29.801 1.00 96.01  ? 2    NAG I C6  1 
HETATM 12133 C  C7  . NAG I  4  .   ? 12.751  9.032   -23.944 1.00 98.98  ? 2    NAG I C7  1 
HETATM 12134 C  C8  . NAG I  4  .   ? 13.714  9.936   -23.183 1.00 99.38  ? 2    NAG I C8  1 
HETATM 12135 N  N2  . NAG I  4  .   ? 13.275  8.023   -24.654 1.00 97.30  ? 2    NAG I N2  1 
HETATM 12136 O  O3  . NAG I  4  .   ? 11.646  7.574   -26.960 1.00 94.92  ? 2    NAG I O3  1 
HETATM 12137 O  O4  . NAG I  4  .   ? 12.900  7.020   -29.448 1.00 94.22  ? 2    NAG I O4  1 
HETATM 12138 O  O5  . NAG I  4  .   ? 15.751  8.297   -27.435 1.00 92.88  ? 2    NAG I O5  1 
HETATM 12139 O  O6  . NAG I  4  .   ? 16.087  6.734   -30.526 1.00 96.99  ? 2    NAG I O6  1 
HETATM 12140 O  O7  . NAG I  4  .   ? 11.535  9.260   -23.881 1.00 99.17  ? 2    NAG I O7  1 
HETATM 12141 C  C1  . NAG J  4  .   ? 19.987  13.736  -29.294 1.00 107.05 ? 1    NAG J C1  1 
HETATM 12142 C  C2  . NAG J  4  .   ? 18.935  12.618  -29.169 1.00 106.88 ? 1    NAG J C2  1 
HETATM 12143 C  C3  . NAG J  4  .   ? 19.603  11.237  -29.114 1.00 108.11 ? 1    NAG J C3  1 
HETATM 12144 C  C4  . NAG J  4  .   ? 20.576  11.029  -30.296 1.00 109.23 ? 1    NAG J C4  1 
HETATM 12145 C  C5  . NAG J  4  .   ? 21.526  12.237  -30.366 1.00 109.56 ? 1    NAG J C5  1 
HETATM 12146 C  C6  . NAG J  4  .   ? 22.456  12.195  -31.558 1.00 111.32 ? 1    NAG J C6  1 
HETATM 12147 C  C7  . NAG J  4  .   ? 16.794  12.805  -28.126 1.00 103.83 ? 1    NAG J C7  1 
HETATM 12148 C  C8  . NAG J  4  .   ? 15.993  11.794  -27.328 1.00 102.63 ? 1    NAG J C8  1 
HETATM 12149 N  N2  . NAG J  4  .   ? 18.114  12.803  -27.991 1.00 104.55 ? 1    NAG J N2  1 
HETATM 12150 O  O3  . NAG J  4  .   ? 18.600  10.236  -29.142 1.00 109.50 ? 1    NAG J O3  1 
HETATM 12151 O  O4  . NAG J  4  .   ? 21.360  9.827   -30.078 1.00 109.69 ? 1    NAG J O4  1 
HETATM 12152 O  O5  . NAG J  4  .   ? 20.787  13.478  -30.456 1.00 107.99 ? 1    NAG J O5  1 
HETATM 12153 O  O6  . NAG J  4  .   ? 23.045  13.469  -31.785 1.00 113.39 ? 1    NAG J O6  1 
HETATM 12154 O  O7  . NAG J  4  .   ? 16.213  13.579  -28.890 1.00 103.72 ? 1    NAG J O7  1 
HETATM 12155 C  C1  . NAG J  4  .   ? 21.162  8.705   -30.890 1.00 110.44 ? 2    NAG J C1  1 
HETATM 12156 C  C2  . NAG J  4  .   ? 22.514  7.984   -31.093 1.00 110.60 ? 2    NAG J C2  1 
HETATM 12157 C  C3  . NAG J  4  .   ? 22.350  6.621   -31.795 1.00 110.61 ? 2    NAG J C3  1 
HETATM 12158 C  C4  . NAG J  4  .   ? 21.275  5.775   -31.111 1.00 111.24 ? 2    NAG J C4  1 
HETATM 12159 C  C5  . NAG J  4  .   ? 19.981  6.593   -30.956 1.00 111.35 ? 2    NAG J C5  1 
HETATM 12160 C  C6  . NAG J  4  .   ? 18.922  5.823   -30.184 1.00 111.30 ? 2    NAG J C6  1 
HETATM 12161 C  C7  . NAG J  4  .   ? 24.559  9.210   -31.372 1.00 111.37 ? 2    NAG J C7  1 
HETATM 12162 C  C8  . NAG J  4  .   ? 25.820  8.542   -31.910 1.00 111.16 ? 2    NAG J C8  1 
HETATM 12163 N  N2  . NAG J  4  .   ? 23.394  8.824   -31.878 1.00 110.84 ? 2    NAG J N2  1 
HETATM 12164 O  O3  . NAG J  4  .   ? 23.590  5.924   -31.771 1.00 109.15 ? 2    NAG J O3  1 
HETATM 12165 O  O4  . NAG J  4  .   ? 21.024  4.610   -31.890 1.00 111.18 ? 2    NAG J O4  1 
HETATM 12166 O  O5  . NAG J  4  .   ? 20.237  7.824   -30.222 1.00 111.14 ? 2    NAG J O5  1 
HETATM 12167 O  O6  . NAG J  4  .   ? 19.253  5.724   -28.803 1.00 110.36 ? 2    NAG J O6  1 
HETATM 12168 O  O7  . NAG J  4  .   ? 24.645  10.071  -30.493 1.00 112.10 ? 2    NAG J O7  1 
HETATM 12169 C  C1  . FTT K  6  .   ? 24.098  -7.192  7.323   1.00 86.36  ? 1003 FTT A C1  1 
HETATM 12170 C  C2  . FTT K  6  .   ? 24.361  -6.415  6.020   1.00 87.21  ? 1003 FTT A C2  1 
HETATM 12171 C  C3  . FTT K  6  .   ? 24.439  -4.907  6.291   1.00 89.48  ? 1003 FTT A C3  1 
HETATM 12172 C  C4  . FTT K  6  .   ? 25.586  -4.100  5.666   1.00 91.01  ? 1003 FTT A C4  1 
HETATM 12173 C  C5  . FTT K  6  .   ? 26.683  -3.587  6.603   1.00 93.48  ? 1003 FTT A C5  1 
HETATM 12174 C  C6  . FTT K  6  .   ? 27.029  -2.095  6.489   1.00 95.72  ? 1003 FTT A C6  1 
HETATM 12175 C  C7  . FTT K  6  .   ? 28.161  -1.726  7.463   1.00 98.14  ? 1003 FTT A C7  1 
HETATM 12176 C  C8  . FTT K  6  .   ? 28.661  -0.283  7.325   1.00 98.98  ? 1003 FTT A C8  1 
HETATM 12177 C  C9  . FTT K  6  .   ? 29.919  -0.254  6.492   1.00 100.68 ? 1003 FTT A C9  1 
HETATM 12178 C  C10 . FTT K  6  .   ? 30.584  1.084   6.213   1.00 103.59 ? 1003 FTT A C10 1 
HETATM 12179 C  C11 . FTT K  6  .   ? 31.661  0.656   5.226   1.00 106.65 ? 1003 FTT A C11 1 
HETATM 12180 C  C12 . FTT K  6  .   ? 32.554  1.675   4.531   1.00 108.00 ? 1003 FTT A C12 1 
HETATM 12181 C  C13 . FTT K  6  .   ? 33.420  0.859   3.549   1.00 110.31 ? 1003 FTT A C13 1 
HETATM 12182 C  C14 . FTT K  6  .   ? 34.359  1.686   2.676   1.00 110.24 ? 1003 FTT A C14 1 
HETATM 12183 O  O2  . FTT K  6  .   ? 23.426  -6.732  8.262   1.00 88.17  ? 1003 FTT A O2  1 
HETATM 12184 O  O3  . FTT K  6  .   ? 23.204  -4.340  5.865   1.00 88.61  ? 1003 FTT A O3  1 
HETATM 12185 C  C1  . FTT L  6  .   ? 27.952  -8.216  7.942   1.00 78.17  ? 1004 FTT A C1  1 
HETATM 12186 C  C2  . FTT L  6  .   ? 28.747  -7.148  8.692   1.00 77.47  ? 1004 FTT A C2  1 
HETATM 12187 C  C3  . FTT L  6  .   ? 29.769  -6.285  7.970   1.00 77.08  ? 1004 FTT A C3  1 
HETATM 12188 C  C4  . FTT L  6  .   ? 30.428  -5.349  8.966   1.00 77.22  ? 1004 FTT A C4  1 
HETATM 12189 C  C5  . FTT L  6  .   ? 30.437  -4.947  10.433  1.00 77.41  ? 1004 FTT A C5  1 
HETATM 12190 C  C6  . FTT L  6  .   ? 31.493  -3.889  10.625  1.00 77.71  ? 1004 FTT A C6  1 
HETATM 12191 C  C7  . FTT L  6  .   ? 32.349  -4.221  11.830  1.00 78.72  ? 1004 FTT A C7  1 
HETATM 12192 C  C8  . FTT L  6  .   ? 32.076  -3.210  12.908  1.00 80.18  ? 1004 FTT A C8  1 
HETATM 12193 C  C9  . FTT L  6  .   ? 33.288  -2.834  13.739  1.00 80.93  ? 1004 FTT A C9  1 
HETATM 12194 C  C10 . FTT L  6  .   ? 32.635  -1.722  14.505  1.00 82.11  ? 1004 FTT A C10 1 
HETATM 12195 C  C11 . FTT L  6  .   ? 33.383  -0.898  15.517  1.00 83.94  ? 1004 FTT A C11 1 
HETATM 12196 C  C12 . FTT L  6  .   ? 32.281  0.114   15.819  1.00 84.11  ? 1004 FTT A C12 1 
HETATM 12197 C  C13 . FTT L  6  .   ? 32.602  1.228   16.789  1.00 83.97  ? 1004 FTT A C13 1 
HETATM 12198 C  C14 . FTT L  6  .   ? 31.361  2.105   16.859  1.00 83.66  ? 1004 FTT A C14 1 
HETATM 12199 O  O2  . FTT L  6  .   ? 28.044  -8.486  6.741   1.00 78.65  ? 1004 FTT A O2  1 
HETATM 12200 O  O3  . FTT L  6  .   ? 30.738  -7.152  7.377   1.00 78.00  ? 1004 FTT A O3  1 
HETATM 12201 C  C1  . FTT M  6  .   ? 25.433  -9.267  12.952  1.00 69.61  ? 1005 FTT A C1  1 
HETATM 12202 C  C2  . FTT M  6  .   ? 26.326  -8.182  12.324  1.00 69.11  ? 1005 FTT A C2  1 
HETATM 12203 C  C3  . FTT M  6  .   ? 26.474  -6.812  12.965  1.00 69.01  ? 1005 FTT A C3  1 
HETATM 12204 C  C4  . FTT M  6  .   ? 27.859  -6.709  13.542  1.00 68.97  ? 1005 FTT A C4  1 
HETATM 12205 C  C5  . FTT M  6  .   ? 27.750  -6.022  14.891  1.00 70.61  ? 1005 FTT A C5  1 
HETATM 12206 C  C6  . FTT M  6  .   ? 29.105  -5.417  15.226  1.00 70.43  ? 1005 FTT A C6  1 
HETATM 12207 C  C7  . FTT M  6  .   ? 29.611  -5.962  16.534  1.00 71.97  ? 1005 FTT A C7  1 
HETATM 12208 C  C8  . FTT M  6  .   ? 30.917  -5.325  16.917  1.00 73.47  ? 1005 FTT A C8  1 
HETATM 12209 C  C9  . FTT M  6  .   ? 30.726  -4.332  18.039  1.00 75.47  ? 1005 FTT A C9  1 
HETATM 12210 C  C10 . FTT M  6  .   ? 32.075  -3.749  18.357  1.00 77.86  ? 1005 FTT A C10 1 
HETATM 12211 C  C11 . FTT M  6  .   ? 32.051  -2.703  19.440  1.00 78.65  ? 1005 FTT A C11 1 
HETATM 12212 C  C12 . FTT M  6  .   ? 33.494  -2.279  19.575  1.00 80.34  ? 1005 FTT A C12 1 
HETATM 12213 C  C13 . FTT M  6  .   ? 33.678  -1.229  20.634  1.00 81.50  ? 1005 FTT A C13 1 
HETATM 12214 C  C14 . FTT M  6  .   ? 35.162  -0.915  20.687  1.00 83.86  ? 1005 FTT A C14 1 
HETATM 12215 O  O2  . FTT M  6  .   ? 24.196  -9.206  12.873  1.00 69.75  ? 1005 FTT A O2  1 
HETATM 12216 O  O3  . FTT M  6  .   ? 26.163  -5.871  11.955  1.00 69.41  ? 1005 FTT A O3  1 
HETATM 12217 C  C1  . FTT N  6  .   ? 25.512  -9.608  17.131  1.00 69.17  ? 1006 FTT A C1  1 
HETATM 12218 C  C2  . FTT N  6  .   ? 26.443  -8.522  17.679  1.00 67.85  ? 1006 FTT A C2  1 
HETATM 12219 C  C3  . FTT N  6  .   ? 25.657  -7.362  18.294  1.00 65.67  ? 1006 FTT A C3  1 
HETATM 12220 C  C4  . FTT N  6  .   ? 26.630  -6.290  18.804  1.00 63.43  ? 1006 FTT A C4  1 
HETATM 12221 C  C5  . FTT N  6  .   ? 25.978  -5.044  19.394  1.00 61.47  ? 1006 FTT A C5  1 
HETATM 12222 C  C6  . FTT N  6  .   ? 25.825  -5.047  20.895  1.00 58.59  ? 1006 FTT A C6  1 
HETATM 12223 C  C7  . FTT N  6  .   ? 26.363  -3.911  21.735  1.00 57.28  ? 1006 FTT A C7  1 
HETATM 12224 C  C8  . FTT N  6  .   ? 25.369  -3.543  22.814  1.00 55.68  ? 1006 FTT A C8  1 
HETATM 12225 C  C9  . FTT N  6  .   ? 25.925  -2.426  23.665  1.00 56.41  ? 1006 FTT A C9  1 
HETATM 12226 C  C10 . FTT N  6  .   ? 24.945  -2.092  24.760  1.00 56.92  ? 1006 FTT A C10 1 
HETATM 12227 C  C11 . FTT N  6  .   ? 25.596  -1.014  25.586  1.00 57.81  ? 1006 FTT A C11 1 
HETATM 12228 C  C12 . FTT N  6  .   ? 24.680  -0.657  26.716  1.00 58.45  ? 1006 FTT A C12 1 
HETATM 12229 C  C13 . FTT N  6  .   ? 25.366  0.406   27.531  1.00 59.60  ? 1006 FTT A C13 1 
HETATM 12230 C  C14 . FTT N  6  .   ? 24.464  0.793   28.681  1.00 62.55  ? 1006 FTT A C14 1 
HETATM 12231 O  O2  . FTT N  6  .   ? 24.288  -9.467  17.215  1.00 72.32  ? 1006 FTT A O2  1 
HETATM 12232 O  O3  . FTT N  6  .   ? 24.817  -6.568  17.504  1.00 65.36  ? 1006 FTT A O3  1 
HETATM 12233 O  O1  . DAO O  7  .   ? 23.827  -5.248  11.854  1.00 74.22  ? 1007 DAO A O1  1 
HETATM 12234 C  C1  . DAO O  7  .   ? 25.025  -5.108  11.593  1.00 72.70  ? 1007 DAO A C1  1 
HETATM 12235 C  C2  . DAO O  7  .   ? 25.187  -3.873  10.719  1.00 73.32  ? 1007 DAO A C2  1 
HETATM 12236 C  C3  . DAO O  7  .   ? 26.521  -3.148  10.752  1.00 72.70  ? 1007 DAO A C3  1 
HETATM 12237 C  C4  . DAO O  7  .   ? 26.279  -1.777  11.370  1.00 71.22  ? 1007 DAO A C4  1 
HETATM 12238 C  C5  . DAO O  7  .   ? 27.199  -1.521  12.553  1.00 71.51  ? 1007 DAO A C5  1 
HETATM 12239 C  C6  . DAO O  7  .   ? 28.645  -1.372  12.114  1.00 70.92  ? 1007 DAO A C6  1 
HETATM 12240 C  C7  . DAO O  7  .   ? 29.126  0.067   12.164  1.00 72.87  ? 1007 DAO A C7  1 
HETATM 12241 C  C8  . DAO O  7  .   ? 30.530  -0.034  11.623  1.00 74.04  ? 1007 DAO A C8  1 
HETATM 12242 C  C9  . DAO O  7  .   ? 31.399  1.198   11.437  1.00 73.38  ? 1007 DAO A C9  1 
HETATM 12243 C  C10 . DAO O  7  .   ? 32.588  0.493   10.807  1.00 74.66  ? 1007 DAO A C10 1 
HETATM 12244 C  C11 . DAO O  7  .   ? 33.768  1.315   10.360  1.00 76.10  ? 1007 DAO A C11 1 
HETATM 12245 C  C12 . DAO O  7  .   ? 34.786  0.351   9.750   1.00 75.71  ? 1007 DAO A C12 1 
HETATM 12246 C  C1  . MYR P  8  .   ? 23.643  -6.190  16.874  1.00 66.38  ? 1008 MYR A C1  1 
HETATM 12247 O  O1  . MYR P  8  .   ? 22.482  -6.392  17.173  1.00 67.96  ? 1008 MYR A O1  1 
HETATM 12248 C  C2  . MYR P  8  .   ? 23.738  -5.372  15.588  1.00 67.62  ? 1008 MYR A C2  1 
HETATM 12249 C  C3  . MYR P  8  .   ? 23.594  -3.871  15.819  1.00 70.16  ? 1008 MYR A C3  1 
HETATM 12250 C  C4  . MYR P  8  .   ? 24.967  -3.232  15.776  1.00 71.25  ? 1008 MYR A C4  1 
HETATM 12251 C  C5  . MYR P  8  .   ? 25.307  -2.140  16.772  1.00 71.57  ? 1008 MYR A C5  1 
HETATM 12252 C  C6  . MYR P  8  .   ? 26.734  -1.731  16.460  1.00 74.38  ? 1008 MYR A C6  1 
HETATM 12253 C  C7  . MYR P  8  .   ? 27.069  -0.357  17.006  1.00 76.00  ? 1008 MYR A C7  1 
HETATM 12254 C  C8  . MYR P  8  .   ? 28.382  -0.380  17.777  1.00 78.06  ? 1008 MYR A C8  1 
HETATM 12255 C  C9  . MYR P  8  .   ? 28.136  -0.048  19.235  1.00 79.31  ? 1008 MYR A C9  1 
HETATM 12256 C  C10 . MYR P  8  .   ? 29.363  -0.041  20.131  1.00 79.21  ? 1008 MYR A C10 1 
HETATM 12257 C  C11 . MYR P  8  .   ? 28.800  0.294   21.495  1.00 78.57  ? 1008 MYR A C11 1 
HETATM 12258 C  C12 . MYR P  8  .   ? 29.799  0.351   22.622  1.00 77.84  ? 1008 MYR A C12 1 
HETATM 12259 C  C13 . MYR P  8  .   ? 28.989  0.648   23.871  1.00 78.58  ? 1008 MYR A C13 1 
HETATM 12260 C  C14 . MYR P  8  .   ? 29.868  0.708   25.105  1.00 79.66  ? 1008 MYR A C14 1 
HETATM 12261 P  P   . PO4 Q  9  .   ? 25.073  -13.807 18.532  1.00 68.51  ? 1010 PO4 A P   1 
HETATM 12262 O  O2  . PO4 Q  9  .   ? 26.016  -14.277 19.573  1.00 67.53  ? 1010 PO4 A O2  1 
HETATM 12263 O  O3  . PO4 Q  9  .   ? 24.455  -12.529 18.955  1.00 66.52  ? 1010 PO4 A O3  1 
HETATM 12264 O  O4  . PO4 Q  9  .   ? 24.030  -14.822 18.298  1.00 66.08  ? 1010 PO4 A O4  1 
HETATM 12265 P  P   . PO4 R  9  .   ? 23.161  -12.545 6.368   1.00 84.58  ? 1011 PO4 A P   1 
HETATM 12266 O  O2  . PO4 R  9  .   ? 24.128  -13.609 5.992   1.00 82.05  ? 1011 PO4 A O2  1 
HETATM 12267 O  O3  . PO4 R  9  .   ? 22.231  -13.067 7.405   1.00 81.95  ? 1011 PO4 A O3  1 
HETATM 12268 O  O4  . PO4 R  9  .   ? 22.385  -12.121 5.163   1.00 82.89  ? 1011 PO4 A O4  1 
HETATM 12269 P  P   . PO4 S  9  .   ? 25.568  -27.797 12.857  1.00 131.61 ? 1017 PO4 A P   1 
HETATM 12270 O  O2  . PO4 S  9  .   ? 26.884  -27.588 13.517  1.00 130.51 ? 1017 PO4 A O2  1 
HETATM 12271 O  O3  . PO4 S  9  .   ? 24.476  -27.580 13.843  1.00 129.90 ? 1017 PO4 A O3  1 
HETATM 12272 O  O4  . PO4 S  9  .   ? 25.493  -29.185 12.342  1.00 131.69 ? 1017 PO4 A O4  1 
HETATM 12273 P  P   . PO4 T  9  .   ? 26.356  -21.652 5.139   1.00 127.51 ? 1018 PO4 A P   1 
HETATM 12274 O  O2  . PO4 T  9  .   ? 27.826  -21.847 5.272   1.00 126.37 ? 1018 PO4 A O2  1 
HETATM 12275 O  O3  . PO4 T  9  .   ? 25.701  -22.969 4.922   1.00 126.28 ? 1018 PO4 A O3  1 
HETATM 12276 O  O4  . PO4 T  9  .   ? 26.077  -20.765 3.975   1.00 126.31 ? 1018 PO4 A O4  1 
HETATM 12277 C  C1  . NAG U  10 .   ? -1.384  -4.052  59.057  1.00 111.63 ? 711  NAG A C1  1 
HETATM 12278 C  C2  . NAG U  10 .   ? -0.738  -4.542  60.381  1.00 113.66 ? 711  NAG A C2  1 
HETATM 12279 C  C3  . NAG U  10 .   ? -1.011  -3.551  61.552  1.00 114.77 ? 711  NAG A C3  1 
HETATM 12280 C  C4  . NAG U  10 .   ? -0.748  -2.081  61.146  1.00 114.29 ? 711  NAG A C4  1 
HETATM 12281 C  C5  . NAG U  10 .   ? -1.473  -1.759  59.833  1.00 113.84 ? 711  NAG A C5  1 
HETATM 12282 C  C6  . NAG U  10 .   ? -1.210  -0.335  59.360  1.00 112.79 ? 711  NAG A C6  1 
HETATM 12283 C  C7  . NAG U  10 .   ? -0.473  -6.806  61.218  1.00 114.42 ? 711  NAG A C7  1 
HETATM 12284 C  C8  . NAG U  10 .   ? -0.449  -6.994  62.732  1.00 112.98 ? 711  NAG A C8  1 
HETATM 12285 N  N2  . NAG U  10 .   ? -1.270  -5.856  60.722  1.00 114.38 ? 711  NAG A N2  1 
HETATM 12286 O  O3  . NAG U  10 .   ? -0.189  -3.886  62.668  1.00 115.11 ? 711  NAG A O3  1 
HETATM 12287 O  O4  . NAG U  10 .   ? -1.201  -1.199  62.168  1.00 114.03 ? 711  NAG A O4  1 
HETATM 12288 O  O5  . NAG U  10 .   ? -1.032  -2.670  58.791  1.00 113.25 ? 711  NAG A O5  1 
HETATM 12289 O  O6  . NAG U  10 .   ? -1.642  -0.129  58.020  1.00 111.66 ? 711  NAG A O6  1 
HETATM 12290 O  O7  . NAG U  10 .   ? 0.229   -7.531  60.504  1.00 113.75 ? 711  NAG A O7  1 
HETATM 12291 C  C1  . NAG V  10 .   ? -5.006  -6.990  36.682  1.00 98.08  ? 721  NAG A C1  1 
HETATM 12292 C  C2  . NAG V  10 .   ? -4.095  -6.410  35.588  1.00 99.95  ? 721  NAG A C2  1 
HETATM 12293 C  C3  . NAG V  10 .   ? -4.897  -5.545  34.600  1.00 101.29 ? 721  NAG A C3  1 
HETATM 12294 C  C4  . NAG V  10 .   ? -6.076  -6.350  34.039  1.00 102.39 ? 721  NAG A C4  1 
HETATM 12295 C  C5  . NAG V  10 .   ? -6.891  -7.029  35.174  1.00 102.26 ? 721  NAG A C5  1 
HETATM 12296 C  C6  . NAG V  10 .   ? -7.915  -8.004  34.628  1.00 102.15 ? 721  NAG A C6  1 
HETATM 12297 C  C7  . NAG V  10 .   ? -1.802  -6.107  36.185  1.00 102.26 ? 721  NAG A C7  1 
HETATM 12298 C  C8  . NAG V  10 .   ? -0.888  -5.644  35.058  1.00 102.43 ? 721  NAG A C8  1 
HETATM 12299 N  N2  . NAG V  10 .   ? -3.040  -5.627  36.190  1.00 100.68 ? 721  NAG A N2  1 
HETATM 12300 O  O3  . NAG V  10 .   ? -4.060  -5.131  33.521  1.00 100.10 ? 721  NAG A O3  1 
HETATM 12301 O  O4  . NAG V  10 .   ? -6.921  -5.479  33.292  1.00 103.04 ? 721  NAG A O4  1 
HETATM 12302 O  O5  . NAG V  10 .   ? -6.031  -7.793  36.065  1.00 100.17 ? 721  NAG A O5  1 
HETATM 12303 O  O6  . NAG V  10 .   ? -8.242  -8.996  35.593  1.00 103.55 ? 721  NAG A O6  1 
HETATM 12304 O  O7  . NAG V  10 .   ? -1.385  -6.911  37.036  1.00 101.97 ? 721  NAG A O7  1 
HETATM 12305 C  C1  . NAG W  10 .   ? -19.559 7.031   4.012   1.00 99.89  ? 741  NAG A C1  1 
HETATM 12306 C  C2  . NAG W  10 .   ? -20.702 7.204   5.049   1.00 102.51 ? 741  NAG A C2  1 
HETATM 12307 C  C3  . NAG W  10 .   ? -21.432 5.852   5.289   1.00 103.82 ? 741  NAG A C3  1 
HETATM 12308 C  C4  . NAG W  10 .   ? -21.778 5.128   3.968   1.00 103.19 ? 741  NAG A C4  1 
HETATM 12309 C  C5  . NAG W  10 .   ? -20.568 5.097   3.014   1.00 101.86 ? 741  NAG A C5  1 
HETATM 12310 C  C6  . NAG W  10 .   ? -20.914 4.527   1.654   1.00 101.06 ? 741  NAG A C6  1 
HETATM 12311 C  C7  . NAG W  10 .   ? -20.858 8.429   7.144   1.00 103.79 ? 741  NAG A C7  1 
HETATM 12312 C  C8  . NAG W  10 .   ? -21.561 7.721   8.296   1.00 102.82 ? 741  NAG A C8  1 
HETATM 12313 N  N2  . NAG W  10 .   ? -20.138 7.682   6.305   1.00 103.57 ? 741  NAG A N2  1 
HETATM 12314 O  O3  . NAG W  10 .   ? -22.627 6.065   6.037   1.00 104.44 ? 741  NAG A O3  1 
HETATM 12315 O  O4  . NAG W  10 .   ? -22.189 3.794   4.254   1.00 103.81 ? 741  NAG A O4  1 
HETATM 12316 O  O5  . NAG W  10 .   ? -20.059 6.432   2.801   1.00 100.61 ? 741  NAG A O5  1 
HETATM 12317 O  O6  . NAG W  10 .   ? -21.286 3.162   1.756   1.00 101.21 ? 741  NAG A O6  1 
HETATM 12318 O  O7  . NAG W  10 .   ? -20.956 9.654   7.029   1.00 103.91 ? 741  NAG A O7  1 
HETATM 12319 MG MG  . MG  X  11 .   ? 24.541  -17.851 20.125  1.00 72.74  ? 2001 MG  A MG  1 
HETATM 12320 C  C1  . FTT Y  6  .   ? -1.645  -12.647 -15.261 1.00 85.97  ? 1003 FTT B C1  1 
HETATM 12321 C  C2  . FTT Y  6  .   ? -1.900  -11.335 -14.468 1.00 87.19  ? 1003 FTT B C2  1 
HETATM 12322 C  C3  . FTT Y  6  .   ? -1.973  -10.108 -15.399 1.00 88.31  ? 1003 FTT B C3  1 
HETATM 12323 C  C4  . FTT Y  6  .   ? -3.113  -9.100  -15.215 1.00 88.84  ? 1003 FTT B C4  1 
HETATM 12324 C  C5  . FTT Y  6  .   ? -4.205  -9.074  -16.284 1.00 91.76  ? 1003 FTT B C5  1 
HETATM 12325 C  C6  . FTT Y  6  .   ? -4.518  -7.704  -16.899 1.00 93.69  ? 1003 FTT B C6  1 
HETATM 12326 C  C7  . FTT Y  6  .   ? -5.648  -7.821  -17.929 1.00 96.38  ? 1003 FTT B C7  1 
HETATM 12327 C  C8  . FTT Y  6  .   ? -6.132  -6.472  -18.473 1.00 98.50  ? 1003 FTT B C8  1 
HETATM 12328 C  C9  . FTT Y  6  .   ? -7.403  -6.045  -17.759 1.00 101.65 ? 1003 FTT B C9  1 
HETATM 12329 C  C10 . FTT Y  6  .   ? -8.070  -4.727  -18.132 1.00 103.75 ? 1003 FTT B C10 1 
HETATM 12330 C  C11 . FTT Y  6  .   ? -9.146  -4.654  -17.064 1.00 106.65 ? 1003 FTT B C11 1 
HETATM 12331 C  C12 . FTT Y  6  .   ? -10.023 -3.422  -16.921 1.00 108.79 ? 1003 FTT B C12 1 
HETATM 12332 C  C13 . FTT Y  6  .   ? -10.896 -3.679  -15.676 1.00 111.23 ? 1003 FTT B C13 1 
HETATM 12333 C  C14 . FTT Y  6  .   ? -11.825 -2.525  -15.297 1.00 111.12 ? 1003 FTT B C14 1 
HETATM 12334 O  O2  . FTT Y  6  .   ? -0.970  -12.690 -16.297 1.00 86.55  ? 1003 FTT B O2  1 
HETATM 12335 O  O3  . FTT Y  6  .   ? -0.746  -9.407  -15.274 1.00 87.31  ? 1003 FTT B O3  1 
HETATM 12336 C  C1  . FTT Z  6  .   ? -5.514  -13.798 -15.343 1.00 76.31  ? 1004 FTT B C1  1 
HETATM 12337 C  C2  . FTT Z  6  .   ? -6.298  -13.194 -16.502 1.00 76.29  ? 1004 FTT B C2  1 
HETATM 12338 C  C3  . FTT Z  6  .   ? -7.319  -12.093 -16.263 1.00 76.48  ? 1004 FTT B C3  1 
HETATM 12339 C  C4  . FTT Z  6  .   ? -7.974  -11.712 -17.579 1.00 76.64  ? 1004 FTT B C4  1 
HETATM 12340 C  C5  . FTT Z  6  .   ? -7.987  -12.024 -19.063 1.00 76.22  ? 1004 FTT B C5  1 
HETATM 12341 C  C6  . FTT Z  6  .   ? -9.031  -11.160 -19.720 1.00 75.99  ? 1004 FTT B C6  1 
HETATM 12342 C  C7  . FTT Z  6  .   ? -9.898  -11.999 -20.635 1.00 77.60  ? 1004 FTT B C7  1 
HETATM 12343 C  C8  . FTT Z  6  .   ? -9.613  -11.618 -22.062 1.00 79.12  ? 1004 FTT B C8  1 
HETATM 12344 C  C9  . FTT Z  6  .   ? -10.821 -11.684 -22.983 1.00 80.58  ? 1004 FTT B C9  1 
HETATM 12345 C  C10 . FTT Z  6  .   ? -10.170 -11.047 -24.177 1.00 82.77  ? 1004 FTT B C10 1 
HETATM 12346 C  C11 . FTT Z  6  .   ? -10.910 -10.785 -25.461 1.00 83.65  ? 1004 FTT B C11 1 
HETATM 12347 C  C12 . FTT Z  6  .   ? -9.794  -10.044 -26.184 1.00 83.43  ? 1004 FTT B C12 1 
HETATM 12348 C  C13 . FTT Z  6  .   ? -10.110 -9.525  -27.558 1.00 84.20  ? 1004 FTT B C13 1 
HETATM 12349 C  C14 . FTT Z  6  .   ? -8.862  -8.786  -28.024 1.00 85.10  ? 1004 FTT B C14 1 
HETATM 12350 O  O2  . FTT Z  6  .   ? -5.617  -13.492 -14.162 1.00 76.74  ? 1004 FTT B O2  1 
HETATM 12351 O  O3  . FTT Z  6  .   ? -8.289  -12.586 -15.349 1.00 77.62  ? 1004 FTT B O3  1 
HETATM 12352 C  C1  . FTT AA 6  .   ? -3.013  -17.074 -19.283 1.00 68.66  ? 1005 FTT B C1  1 
HETATM 12353 C  C2  . FTT AA 6  .   ? -3.890  -15.818 -19.235 1.00 68.74  ? 1005 FTT B C2  1 
HETATM 12354 C  C3  . FTT AA 6  .   ? -4.026  -14.895 -20.437 1.00 68.58  ? 1005 FTT B C3  1 
HETATM 12355 C  C4  . FTT AA 6  .   ? -5.415  -15.057 -21.005 1.00 68.35  ? 1005 FTT B C4  1 
HETATM 12356 C  C5  . FTT AA 6  .   ? -5.296  -15.067 -22.514 1.00 69.47  ? 1005 FTT B C5  1 
HETATM 12357 C  C6  . FTT AA 6  .   ? -6.640  -14.679 -23.096 1.00 70.57  ? 1005 FTT B C6  1 
HETATM 12358 C  C7  . FTT AA 6  .   ? -7.167  -15.779 -23.981 1.00 72.68  ? 1005 FTT B C7  1 
HETATM 12359 C  C8  . FTT AA 6  .   ? -8.473  -15.395 -24.624 1.00 74.18  ? 1005 FTT B C8  1 
HETATM 12360 C  C9  . FTT AA 6  .   ? -8.276  -15.030 -26.077 1.00 76.27  ? 1005 FTT B C9  1 
HETATM 12361 C  C10 . FTT AA 6  .   ? -9.623  -14.662 -26.637 1.00 79.18  ? 1005 FTT B C10 1 
HETATM 12362 C  C11 . FTT AA 6  .   ? -9.593  -14.225 -28.086 1.00 80.39  ? 1005 FTT B C11 1 
HETATM 12363 C  C12 . FTT AA 6  .   ? -11.034 -13.890 -28.416 1.00 81.75  ? 1005 FTT B C12 1 
HETATM 12364 C  C13 . FTT AA 6  .   ? -11.204 -13.437 -29.841 1.00 81.78  ? 1005 FTT B C13 1 
HETATM 12365 C  C14 . FTT AA 6  .   ? -12.685 -13.179 -30.031 1.00 83.58  ? 1005 FTT B C14 1 
HETATM 12366 O  O2  . FTT AA 6  .   ? -1.772  -17.002 -19.248 1.00 68.11  ? 1005 FTT B O2  1 
HETATM 12367 O  O3  . FTT AA 6  .   ? -3.705  -13.593 -19.966 1.00 68.76  ? 1005 FTT B O3  1 
HETATM 12368 C  C1  . FTT BA 6  .   ? -3.106  -19.312 -22.822 1.00 68.88  ? 1006 FTT B C1  1 
HETATM 12369 C  C2  . FTT BA 6  .   ? -4.028  -18.585 -23.804 1.00 66.78  ? 1006 FTT B C2  1 
HETATM 12370 C  C3  . FTT BA 6  .   ? -3.238  -17.850 -24.887 1.00 64.01  ? 1006 FTT B C3  1 
HETATM 12371 C  C4  . FTT BA 6  .   ? -4.194  -17.133 -25.846 1.00 61.83  ? 1006 FTT B C4  1 
HETATM 12372 C  C5  . FTT BA 6  .   ? -3.529  -16.316 -26.945 1.00 60.52  ? 1006 FTT B C5  1 
HETATM 12373 C  C6  . FTT BA 6  .   ? -3.397  -17.019 -28.267 1.00 59.36  ? 1006 FTT B C6  1 
HETATM 12374 C  C7  . FTT BA 6  .   ? -3.942  -16.415 -29.547 1.00 58.69  ? 1006 FTT B C7  1 
HETATM 12375 C  C8  . FTT BA 6  .   ? -2.946  -16.591 -30.677 1.00 56.90  ? 1006 FTT B C8  1 
HETATM 12376 C  C9  . FTT BA 6  .   ? -3.499  -16.006 -31.953 1.00 56.99  ? 1006 FTT B C9  1 
HETATM 12377 C  C10 . FTT BA 6  .   ? -2.509  -16.227 -33.067 1.00 57.40  ? 1006 FTT B C10 1 
HETATM 12378 C  C11 . FTT BA 6  .   ? -3.157  -15.648 -34.297 1.00 58.48  ? 1006 FTT B C11 1 
HETATM 12379 C  C12 . FTT BA 6  .   ? -2.240  -15.851 -35.464 1.00 61.20  ? 1006 FTT B C12 1 
HETATM 12380 C  C13 . FTT BA 6  .   ? -2.913  -15.280 -36.689 1.00 61.49  ? 1006 FTT B C13 1 
HETATM 12381 C  C14 . FTT BA 6  .   ? -1.997  -15.481 -37.883 1.00 64.24  ? 1006 FTT B C14 1 
HETATM 12382 O  O2  . FTT BA 6  .   ? -1.881  -19.231 -22.946 1.00 72.62  ? 1006 FTT B O2  1 
HETATM 12383 O  O3  . FTT BA 6  .   ? -2.396  -16.786 -24.556 1.00 63.42  ? 1006 FTT B O3  1 
HETATM 12384 O  O1  . DAO CA 7  .   ? -1.386  -12.982 -20.226 1.00 73.69  ? 1007 DAO B O1  1 
HETATM 12385 C  C1  . DAO CA 7  .   ? -2.575  -12.746 -20.020 1.00 71.10  ? 1007 DAO B C1  1 
HETATM 12386 C  C2  . DAO CA 7  .   ? -2.735  -11.256 -19.801 1.00 71.27  ? 1007 DAO B C2  1 
HETATM 12387 C  C3  . DAO CA 7  .   ? -4.058  -10.622 -20.172 1.00 70.09  ? 1007 DAO B C3  1 
HETATM 12388 C  C4  . DAO CA 7  .   ? -3.797  -9.703  -21.354 1.00 70.59  ? 1007 DAO B C4  1 
HETATM 12389 C  C5  . DAO CA 7  .   ? -4.712  -10.007 -22.530 1.00 71.31  ? 1007 DAO B C5  1 
HETATM 12390 C  C6  . DAO CA 7  .   ? -6.149  -9.651  -22.212 1.00 71.98  ? 1007 DAO B C6  1 
HETATM 12391 C  C7  . DAO CA 7  .   ? -6.608  -8.376  -22.894 1.00 73.77  ? 1007 DAO B C7  1 
HETATM 12392 C  C8  . DAO CA 7  .   ? -8.013  -8.209  -22.367 1.00 74.65  ? 1007 DAO B C8  1 
HETATM 12393 C  C9  . DAO CA 7  .   ? -8.867  -7.034  -22.789 1.00 74.49  ? 1007 DAO B C9  1 
HETATM 12394 C  C10 . DAO CA 7  .   ? -10.079 -7.363  -21.931 1.00 76.65  ? 1007 DAO B C10 1 
HETATM 12395 C  C11 . DAO CA 7  .   ? -11.267 -6.422  -21.938 1.00 77.01  ? 1007 DAO B C11 1 
HETATM 12396 C  C12 . DAO CA 7  .   ? -12.292 -6.993  -20.965 1.00 76.27  ? 1007 DAO B C12 1 
HETATM 12397 C  C1  . MYR DA 8  .   ? -1.220  -16.182 -24.144 1.00 65.40  ? 1008 MYR B C1  1 
HETATM 12398 O  O1  . MYR DA 8  .   ? -0.057  -16.532 -24.267 1.00 69.08  ? 1008 MYR B O1  1 
HETATM 12399 C  C2  . MYR DA 8  .   ? -1.300  -14.854 -23.415 1.00 65.50  ? 1008 MYR B C2  1 
HETATM 12400 C  C3  . MYR DA 8  .   ? -1.134  -13.654 -24.334 1.00 67.74  ? 1008 MYR B C3  1 
HETATM 12401 C  C4  . MYR DA 8  .   ? -2.496  -13.053 -24.596 1.00 69.06  ? 1008 MYR B C4  1 
HETATM 12402 C  C5  . MYR DA 8  .   ? -2.827  -12.544 -25.975 1.00 69.68  ? 1008 MYR B C5  1 
HETATM 12403 C  C6  . MYR DA 8  .   ? -4.248  -12.026 -25.886 1.00 73.21  ? 1008 MYR B C6  1 
HETATM 12404 C  C7  . MYR DA 8  .   ? -4.580  -11.063 -27.006 1.00 74.82  ? 1008 MYR B C7  1 
HETATM 12405 C  C8  . MYR DA 8  .   ? -5.891  -11.442 -27.678 1.00 76.14  ? 1008 MYR B C8  1 
HETATM 12406 C  C9  . MYR DA 8  .   ? -5.641  -11.812 -29.124 1.00 77.23  ? 1008 MYR B C9  1 
HETATM 12407 C  C10 . MYR DA 8  .   ? -6.864  -12.203 -29.928 1.00 78.31  ? 1008 MYR B C10 1 
HETATM 12408 C  C11 . MYR DA 8  .   ? -6.305  -12.534 -31.293 1.00 78.29  ? 1008 MYR B C11 1 
HETATM 12409 C  C12 . MYR DA 8  .   ? -7.310  -13.006 -32.313 1.00 77.50  ? 1008 MYR B C12 1 
HETATM 12410 C  C13 . MYR DA 8  .   ? -6.505  -13.331 -33.558 1.00 78.07  ? 1008 MYR B C13 1 
HETATM 12411 C  C14 . MYR DA 8  .   ? -7.380  -13.861 -34.676 1.00 78.28  ? 1008 MYR B C14 1 
HETATM 12412 P  P   . PO4 EA 9  .   ? -2.714  -23.706 -22.133 1.00 73.05  ? 1010 PO4 B P   1 
HETATM 12413 O  O2  . PO4 EA 9  .   ? -3.669  -24.600 -22.831 1.00 69.30  ? 1010 PO4 B O2  1 
HETATM 12414 O  O3  . PO4 EA 9  .   ? -2.079  -22.770 -23.101 1.00 69.70  ? 1010 PO4 B O3  1 
HETATM 12415 O  O4  . PO4 EA 9  .   ? -1.680  -24.527 -21.455 1.00 69.46  ? 1010 PO4 B O4  1 
HETATM 12416 P  P   . PO4 FA 9  .   ? -0.744  -16.939 -11.938 1.00 83.38  ? 1011 PO4 B P   1 
HETATM 12417 O  O2  . PO4 FA 9  .   ? -1.708  -17.712 -11.118 1.00 82.84  ? 1011 PO4 B O2  1 
HETATM 12418 O  O3  . PO4 FA 9  .   ? 0.177   -17.873 -12.610 1.00 81.57  ? 1011 PO4 B O3  1 
HETATM 12419 O  O4  . PO4 FA 9  .   ? 0.039   -16.021 -11.059 1.00 83.08  ? 1011 PO4 B O4  1 
HETATM 12420 P  P   . PO4 GA 9  .   ? -3.304  -33.422 -10.578 1.00 130.55 ? 1017 PO4 B P   1 
HETATM 12421 O  O2  . PO4 GA 9  .   ? -4.625  -33.534 -11.258 1.00 129.86 ? 1017 PO4 B O2  1 
HETATM 12422 O  O3  . PO4 GA 9  .   ? -2.210  -33.684 -11.553 1.00 129.64 ? 1017 PO4 B O3  1 
HETATM 12423 O  O4  . PO4 GA 9  .   ? -3.232  -34.415 -9.480  1.00 130.42 ? 1017 PO4 B O4  1 
HETATM 12424 P  P   . PO4 HA 9  .   ? -4.043  -24.405 -6.614  1.00 126.90 ? 1018 PO4 B P   1 
HETATM 12425 O  O2  . PO4 HA 9  .   ? -5.514  -24.633 -6.658  1.00 125.75 ? 1018 PO4 B O2  1 
HETATM 12426 O  O3  . PO4 HA 9  .   ? -3.400  -25.478 -5.808  1.00 125.48 ? 1018 PO4 B O3  1 
HETATM 12427 O  O4  . PO4 HA 9  .   ? -3.763  -23.081 -5.994  1.00 126.00 ? 1018 PO4 B O4  1 
HETATM 12428 C  C1  . NAG IA 10 .   ? 23.713  -34.232 -62.473 1.00 108.73 ? 811  NAG B C1  1 
HETATM 12429 C  C2  . NAG IA 10 .   ? 22.636  -34.945 -63.335 1.00 109.81 ? 811  NAG B C2  1 
HETATM 12430 C  C3  . NAG IA 10 .   ? 22.886  -34.765 -64.849 1.00 110.44 ? 811  NAG B C3  1 
HETATM 12431 C  C4  . NAG IA 10 .   ? 23.131  -33.286 -65.190 1.00 110.57 ? 811  NAG B C4  1 
HETATM 12432 C  C5  . NAG IA 10 .   ? 24.235  -32.738 -64.284 1.00 110.53 ? 811  NAG B C5  1 
HETATM 12433 C  C6  . NAG IA 10 .   ? 24.558  -31.287 -64.557 1.00 111.26 ? 811  NAG B C6  1 
HETATM 12434 C  C7  . NAG IA 10 .   ? 22.089  -36.780 -61.873 1.00 109.99 ? 811  NAG B C7  1 
HETATM 12435 C  C8  . NAG IA 10 .   ? 23.039  -37.458 -60.895 1.00 109.72 ? 811  NAG B C8  1 
HETATM 12436 N  N2  . NAG IA 10 .   ? 22.606  -36.363 -63.027 1.00 110.08 ? 811  NAG B N2  1 
HETATM 12437 O  O3  . NAG IA 10 .   ? 21.761  -35.251 -65.577 1.00 109.74 ? 811  NAG B O3  1 
HETATM 12438 O  O4  . NAG IA 10 .   ? 23.514  -33.150 -66.554 1.00 110.19 ? 811  NAG B O4  1 
HETATM 12439 O  O5  . NAG IA 10 .   ? 23.845  -32.856 -62.893 1.00 109.80 ? 811  NAG B O5  1 
HETATM 12440 O  O6  . NAG IA 10 .   ? 25.691  -31.171 -65.404 1.00 111.44 ? 811  NAG B O6  1 
HETATM 12441 O  O7  . NAG IA 10 .   ? 20.900  -36.625 -61.576 1.00 109.11 ? 811  NAG B O7  1 
HETATM 12442 C  C1  . NAG JA 10 .   ? 27.296  -26.321 -41.299 1.00 92.50  ? 821  NAG B C1  1 
HETATM 12443 C  C2  . NAG JA 10 .   ? 26.304  -25.256 -40.777 1.00 93.86  ? 821  NAG B C2  1 
HETATM 12444 C  C3  . NAG JA 10 .   ? 27.032  -24.067 -40.096 1.00 95.26  ? 821  NAG B C3  1 
HETATM 12445 C  C4  . NAG JA 10 .   ? 28.036  -24.580 -39.060 1.00 95.86  ? 821  NAG B C4  1 
HETATM 12446 C  C5  . NAG JA 10 .   ? 28.981  -25.594 -39.733 1.00 96.48  ? 821  NAG B C5  1 
HETATM 12447 C  C6  . NAG JA 10 .   ? 29.993  -26.178 -38.755 1.00 97.37  ? 821  NAG B C6  1 
HETATM 12448 C  C7  . NAG JA 10 .   ? 24.650  -23.779 -41.739 1.00 98.55  ? 821  NAG B C7  1 
HETATM 12449 C  C8  . NAG JA 10 .   ? 25.051  -22.402 -42.252 1.00 98.93  ? 821  NAG B C8  1 
HETATM 12450 N  N2  . NAG JA 10 .   ? 25.523  -24.771 -41.896 1.00 96.26  ? 821  NAG B N2  1 
HETATM 12451 O  O3  . NAG JA 10 .   ? 26.086  -23.216 -39.449 1.00 94.65  ? 821  NAG B O3  1 
HETATM 12452 O  O4  . NAG JA 10 .   ? 28.774  -23.488 -38.523 1.00 94.49  ? 821  NAG B O4  1 
HETATM 12453 O  O5  . NAG JA 10 .   ? 28.218  -26.704 -40.266 1.00 95.20  ? 821  NAG B O5  1 
HETATM 12454 O  O6  . NAG JA 10 .   ? 29.899  -27.599 -38.675 1.00 97.45  ? 821  NAG B O6  1 
HETATM 12455 O  O7  . NAG JA 10 .   ? 23.548  -23.936 -41.208 1.00 100.22 ? 821  NAG B O7  1 
HETATM 12456 C  C1  . NAG KA 10 .   ? 42.283  1.133   -19.110 1.00 87.85  ? 841  NAG B C1  1 
HETATM 12457 C  C2  . NAG KA 10 .   ? 43.606  1.172   -19.898 1.00 88.50  ? 841  NAG B C2  1 
HETATM 12458 C  C3  . NAG KA 10 .   ? 44.531  0.021   -19.479 1.00 89.24  ? 841  NAG B C3  1 
HETATM 12459 C  C4  . NAG KA 10 .   ? 44.735  -0.015  -17.947 1.00 89.68  ? 841  NAG B C4  1 
HETATM 12460 C  C5  . NAG KA 10 .   ? 43.355  0.024   -17.269 1.00 89.01  ? 841  NAG B C5  1 
HETATM 12461 C  C6  . NAG KA 10 .   ? 43.434  0.105   -15.761 1.00 88.89  ? 841  NAG B C6  1 
HETATM 12462 C  C7  . NAG KA 10 .   ? 43.906  2.025   -22.109 1.00 91.26  ? 841  NAG B C7  1 
HETATM 12463 C  C8  . NAG KA 10 .   ? 44.819  1.565   -23.229 1.00 90.45  ? 841  NAG B C8  1 
HETATM 12464 N  N2  . NAG KA 10 .   ? 43.366  1.102   -21.324 1.00 90.01  ? 841  NAG B N2  1 
HETATM 12465 O  O3  . NAG KA 10 .   ? 45.785  0.177   -20.122 1.00 88.42  ? 841  NAG B O3  1 
HETATM 12466 O  O4  . NAG KA 10 .   ? 45.408  -1.245  -17.573 1.00 90.84  ? 841  NAG B O4  1 
HETATM 12467 O  O5  . NAG KA 10 .   ? 42.589  1.171   -17.709 1.00 87.87  ? 841  NAG B O5  1 
HETATM 12468 O  O6  . NAG KA 10 .   ? 42.185  0.499   -15.209 1.00 89.30  ? 841  NAG B O6  1 
HETATM 12469 O  O7  . NAG KA 10 .   ? 43.707  3.230   -21.939 1.00 91.64  ? 841  NAG B O7  1 
HETATM 12470 MG MG  . MG  LA 11 .   ? -2.247  -27.957 -21.630 1.00 83.19  ? 2001 MG  B MG  1 
HETATM 12471 C  C1  . NAG MA 10 .   ? 31.940  -7.782  36.711  1.00 91.10  ? 751  NAG C C1  1 
HETATM 12472 C  C2  . NAG MA 10 .   ? 32.597  -7.588  38.102  1.00 93.93  ? 751  NAG C C2  1 
HETATM 12473 C  C3  . NAG MA 10 .   ? 33.356  -8.826  38.627  1.00 95.36  ? 751  NAG C C3  1 
HETATM 12474 C  C4  . NAG MA 10 .   ? 32.745  -10.176 38.233  1.00 95.74  ? 751  NAG C C4  1 
HETATM 12475 C  C5  . NAG MA 10 .   ? 32.199  -10.151 36.800  1.00 95.42  ? 751  NAG C C5  1 
HETATM 12476 C  C6  . NAG MA 10 .   ? 31.429  -11.420 36.472  1.00 96.32  ? 751  NAG C C6  1 
HETATM 12477 C  C7  . NAG MA 10 .   ? 33.199  -5.263  37.704  1.00 95.56  ? 751  NAG C C7  1 
HETATM 12478 C  C8  . NAG MA 10 .   ? 33.741  -4.741  36.375  1.00 94.79  ? 751  NAG C C8  1 
HETATM 12479 N  N2  . NAG MA 10 .   ? 33.557  -6.497  38.053  1.00 95.06  ? 751  NAG C N2  1 
HETATM 12480 O  O3  . NAG MA 10 .   ? 33.419  -8.757  40.045  1.00 96.63  ? 751  NAG C O3  1 
HETATM 12481 O  O4  . NAG MA 10 .   ? 33.751  -11.177 38.344  1.00 95.78  ? 751  NAG C O4  1 
HETATM 12482 O  O5  . NAG MA 10 .   ? 31.279  -9.049  36.649  1.00 93.49  ? 751  NAG C O5  1 
HETATM 12483 O  O6  . NAG MA 10 .   ? 30.410  -11.671 37.435  1.00 96.93  ? 751  NAG C O6  1 
HETATM 12484 O  O7  . NAG MA 10 .   ? 32.476  -4.546  38.410  1.00 94.50  ? 751  NAG C O7  1 
HETATM 12485 C  C1  . NAG NA 10 .   ? -9.668  -26.591 -40.878 1.00 88.68  ? 851  NAG D C1  1 
HETATM 12486 C  C2  . NAG NA 10 .   ? -10.529 -26.935 -42.111 1.00 89.07  ? 851  NAG D C2  1 
HETATM 12487 C  C3  . NAG NA 10 .   ? -11.506 -28.103 -41.864 1.00 91.06  ? 851  NAG D C3  1 
HETATM 12488 C  C4  . NAG NA 10 .   ? -10.912 -29.243 -41.005 1.00 93.30  ? 851  NAG D C4  1 
HETATM 12489 C  C5  . NAG NA 10 .   ? -10.148 -28.666 -39.803 1.00 93.68  ? 851  NAG D C5  1 
HETATM 12490 C  C6  . NAG NA 10 .   ? -9.485  -29.722 -38.921 1.00 92.68  ? 851  NAG D C6  1 
HETATM 12491 C  C7  . NAG NA 10 .   ? -11.256 -25.228 -43.661 1.00 86.38  ? 851  NAG D C7  1 
HETATM 12492 C  C8  . NAG NA 10 .   ? -12.511 -25.331 -44.515 1.00 85.80  ? 851  NAG D C8  1 
HETATM 12493 N  N2  . NAG NA 10 .   ? -11.311 -25.758 -42.444 1.00 87.72  ? 851  NAG D N2  1 
HETATM 12494 O  O3  . NAG NA 10 .   ? -11.913 -28.627 -43.118 1.00 90.12  ? 851  NAG D O3  1 
HETATM 12495 O  O4  . NAG NA 10 .   ? -11.964 -30.089 -40.543 1.00 94.60  ? 851  NAG D O4  1 
HETATM 12496 O  O5  . NAG NA 10 .   ? -9.117  -27.771 -40.275 1.00 91.90  ? 851  NAG D O5  1 
HETATM 12497 O  O6  . NAG NA 10 .   ? -8.658  -30.602 -39.674 1.00 91.27  ? 851  NAG D O6  1 
HETATM 12498 O  O7  . NAG NA 10 .   ? -10.249 -24.667 -44.106 1.00 84.19  ? 851  NAG D O7  1 
HETATM 12499 O  O   . HOH OA 12 .   ? 24.451  -16.386 22.621  1.00 41.22  ? 1    HOH A O   1 
HETATM 12500 O  O   . HOH PA 12 .   ? -1.837  -27.393 -24.672 1.00 48.08  ? 2    HOH B O   1 
# 
_database_PDB_caveat.id     1 
_database_PDB_caveat.text   'PA1 E 2 HAS WRONG CHIRALITY AT ATOM C1' 
# 
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   GLU 1   27  27  GLU GLU A . n 
A 1 2   PRO 2   28  28  PRO PRO A . n 
A 1 3   CYS 3   29  29  CYS CYS A . n 
A 1 4   VAL 4   30  30  VAL VAL A . n 
A 1 5   GLU 5   31  31  GLU GLU A . n 
A 1 6   VAL 6   32  32  VAL VAL A . n 
A 1 7   VAL 7   33  33  VAL VAL A . n 
A 1 8   PRO 8   34  34  PRO PRO A . n 
A 1 9   ASN 9   35  35  ASN ASN A . n 
A 1 10  ILE 10  36  36  ILE ILE A . n 
A 1 11  THR 11  37  37  THR THR A . n 
A 1 12  TYR 12  38  38  TYR TYR A . n 
A 1 13  GLN 13  39  39  GLN GLN A . n 
A 1 14  CYS 14  40  40  CYS CYS A . n 
A 1 15  MET 15  41  41  MET MET A . n 
A 1 16  GLU 16  42  42  GLU GLU A . n 
A 1 17  LEU 17  43  43  LEU LEU A . n 
A 1 18  ASN 18  44  44  ASN ASN A . n 
A 1 19  PHE 19  45  45  PHE PHE A . n 
A 1 20  TYR 20  46  46  TYR TYR A . n 
A 1 21  LYS 21  47  47  LYS LYS A . n 
A 1 22  ILE 22  48  48  ILE ILE A . n 
A 1 23  PRO 23  49  49  PRO PRO A . n 
A 1 24  ASP 24  50  50  ASP ASP A . n 
A 1 25  ASN 25  51  51  ASN ASN A . n 
A 1 26  LEU 26  52  52  LEU LEU A . n 
A 1 27  PRO 27  53  53  PRO PRO A . n 
A 1 28  PHE 28  54  54  PHE PHE A . n 
A 1 29  SER 29  55  55  SER SER A . n 
A 1 30  THR 30  56  56  THR THR A . n 
A 1 31  LYS 31  57  57  LYS LYS A . n 
A 1 32  ASN 32  58  58  ASN ASN A . n 
A 1 33  LEU 33  59  59  LEU LEU A . n 
A 1 34  ASP 34  60  60  ASP ASP A . n 
A 1 35  LEU 35  61  61  LEU LEU A . n 
A 1 36  SER 36  62  62  SER SER A . n 
A 1 37  PHE 37  63  63  PHE PHE A . n 
A 1 38  ASN 38  64  64  ASN ASN A . n 
A 1 39  PRO 39  65  65  PRO PRO A . n 
A 1 40  LEU 40  66  66  LEU LEU A . n 
A 1 41  ARG 41  67  67  ARG ARG A . n 
A 1 42  HIS 42  68  68  HIS HIS A . n 
A 1 43  LEU 43  69  69  LEU LEU A . n 
A 1 44  GLY 44  70  70  GLY GLY A . n 
A 1 45  SER 45  71  71  SER SER A . n 
A 1 46  TYR 46  72  72  TYR TYR A . n 
A 1 47  SER 47  73  73  SER SER A . n 
A 1 48  PHE 48  74  74  PHE PHE A . n 
A 1 49  PHE 49  75  75  PHE PHE A . n 
A 1 50  SER 50  76  76  SER SER A . n 
A 1 51  PHE 51  77  77  PHE PHE A . n 
A 1 52  PRO 52  78  78  PRO PRO A . n 
A 1 53  GLU 53  79  79  GLU GLU A . n 
A 1 54  LEU 54  80  80  LEU LEU A . n 
A 1 55  GLN 55  81  81  GLN GLN A . n 
A 1 56  VAL 56  82  82  VAL VAL A . n 
A 1 57  LEU 57  83  83  LEU LEU A . n 
A 1 58  ASP 58  84  84  ASP ASP A . n 
A 1 59  LEU 59  85  85  LEU LEU A . n 
A 1 60  SER 60  86  86  SER SER A . n 
A 1 61  ARG 61  87  87  ARG ARG A . n 
A 1 62  CYS 62  88  88  CYS CYS A . n 
A 1 63  GLU 63  89  89  GLU GLU A . n 
A 1 64  ILE 64  90  90  ILE ILE A . n 
A 1 65  GLN 65  91  91  GLN GLN A . n 
A 1 66  THR 66  92  92  THR THR A . n 
A 1 67  ILE 67  93  93  ILE ILE A . n 
A 1 68  GLU 68  94  94  GLU GLU A . n 
A 1 69  ASP 69  95  95  ASP ASP A . n 
A 1 70  GLY 70  96  96  GLY GLY A . n 
A 1 71  ALA 71  97  97  ALA ALA A . n 
A 1 72  TYR 72  98  98  TYR TYR A . n 
A 1 73  GLN 73  99  99  GLN GLN A . n 
A 1 74  SER 74  100 100 SER SER A . n 
A 1 75  LEU 75  101 101 LEU LEU A . n 
A 1 76  SER 76  102 102 SER SER A . n 
A 1 77  HIS 77  103 103 HIS HIS A . n 
A 1 78  LEU 78  104 104 LEU LEU A . n 
A 1 79  SER 79  105 105 SER SER A . n 
A 1 80  THR 80  106 106 THR THR A . n 
A 1 81  LEU 81  107 107 LEU LEU A . n 
A 1 82  ILE 82  108 108 ILE ILE A . n 
A 1 83  LEU 83  109 109 LEU LEU A . n 
A 1 84  THR 84  110 110 THR THR A . n 
A 1 85  GLY 85  111 111 GLY GLY A . n 
A 1 86  ASN 86  112 112 ASN ASN A . n 
A 1 87  PRO 87  113 113 PRO PRO A . n 
A 1 88  ILE 88  114 114 ILE ILE A . n 
A 1 89  GLN 89  115 115 GLN GLN A . n 
A 1 90  SER 90  116 116 SER SER A . n 
A 1 91  LEU 91  117 117 LEU LEU A . n 
A 1 92  ALA 92  118 118 ALA ALA A . n 
A 1 93  LEU 93  119 119 LEU LEU A . n 
A 1 94  GLY 94  120 120 GLY GLY A . n 
A 1 95  ALA 95  121 121 ALA ALA A . n 
A 1 96  PHE 96  122 122 PHE PHE A . n 
A 1 97  SER 97  123 123 SER SER A . n 
A 1 98  GLY 98  124 124 GLY GLY A . n 
A 1 99  LEU 99  125 125 LEU LEU A . n 
A 1 100 SER 100 126 126 SER SER A . n 
A 1 101 SER 101 127 127 SER SER A . n 
A 1 102 LEU 102 128 128 LEU LEU A . n 
A 1 103 GLN 103 129 129 GLN GLN A . n 
A 1 104 LYS 104 130 130 LYS LYS A . n 
A 1 105 LEU 105 131 131 LEU LEU A . n 
A 1 106 VAL 106 132 132 VAL VAL A . n 
A 1 107 ALA 107 133 133 ALA ALA A . n 
A 1 108 VAL 108 134 134 VAL VAL A . n 
A 1 109 GLU 109 135 135 GLU GLU A . n 
A 1 110 THR 110 136 136 THR THR A . n 
A 1 111 ASN 111 137 137 ASN ASN A . n 
A 1 112 LEU 112 138 138 LEU LEU A . n 
A 1 113 ALA 113 139 139 ALA ALA A . n 
A 1 114 SER 114 140 140 SER SER A . n 
A 1 115 LEU 115 141 141 LEU LEU A . n 
A 1 116 GLU 116 142 142 GLU GLU A . n 
A 1 117 ASN 117 143 143 ASN ASN A . n 
A 1 118 PHE 118 144 144 PHE PHE A . n 
A 1 119 PRO 119 145 145 PRO PRO A . n 
A 1 120 ILE 120 146 146 ILE ILE A . n 
A 1 121 GLY 121 147 147 GLY GLY A . n 
A 1 122 HIS 122 148 148 HIS HIS A . n 
A 1 123 LEU 123 149 149 LEU LEU A . n 
A 1 124 LYS 124 150 150 LYS LYS A . n 
A 1 125 THR 125 151 151 THR THR A . n 
A 1 126 LEU 126 152 152 LEU LEU A . n 
A 1 127 LYS 127 153 153 LYS LYS A . n 
A 1 128 GLU 128 154 154 GLU GLU A . n 
A 1 129 LEU 129 155 155 LEU LEU A . n 
A 1 130 ASN 130 156 156 ASN ASN A . n 
A 1 131 VAL 131 157 157 VAL VAL A . n 
A 1 132 ALA 132 158 158 ALA ALA A . n 
A 1 133 HIS 133 159 159 HIS HIS A . n 
A 1 134 ASN 134 160 160 ASN ASN A . n 
A 1 135 LEU 135 161 161 LEU LEU A . n 
A 1 136 ILE 136 162 162 ILE ILE A . n 
A 1 137 GLN 137 163 163 GLN GLN A . n 
A 1 138 SER 138 164 164 SER SER A . n 
A 1 139 PHE 139 165 165 PHE PHE A . n 
A 1 140 LYS 140 166 166 LYS LYS A . n 
A 1 141 LEU 141 167 167 LEU LEU A . n 
A 1 142 PRO 142 168 168 PRO PRO A . n 
A 1 143 GLU 143 169 169 GLU GLU A . n 
A 1 144 TYR 144 170 170 TYR TYR A . n 
A 1 145 PHE 145 171 171 PHE PHE A . n 
A 1 146 SER 146 172 172 SER SER A . n 
A 1 147 ASN 147 173 173 ASN ASN A . n 
A 1 148 LEU 148 174 174 LEU LEU A . n 
A 1 149 THR 149 175 175 THR THR A . n 
A 1 150 ASN 150 176 176 ASN ASN A . n 
A 1 151 LEU 151 177 177 LEU LEU A . n 
A 1 152 GLU 152 178 178 GLU GLU A . n 
A 1 153 HIS 153 179 179 HIS HIS A . n 
A 1 154 LEU 154 180 180 LEU LEU A . n 
A 1 155 ASP 155 181 181 ASP ASP A . n 
A 1 156 LEU 156 182 182 LEU LEU A . n 
A 1 157 SER 157 183 183 SER SER A . n 
A 1 158 SER 158 184 184 SER SER A . n 
A 1 159 ASN 159 185 185 ASN ASN A . n 
A 1 160 LYS 160 186 186 LYS LYS A . n 
A 1 161 ILE 161 187 187 ILE ILE A . n 
A 1 162 GLN 162 188 188 GLN GLN A . n 
A 1 163 SER 163 189 189 SER SER A . n 
A 1 164 ILE 164 190 190 ILE ILE A . n 
A 1 165 TYR 165 191 191 TYR TYR A . n 
A 1 166 CYS 166 192 192 CYS CYS A . n 
A 1 167 THR 167 193 193 THR THR A . n 
A 1 168 ASP 168 194 194 ASP ASP A . n 
A 1 169 LEU 169 195 195 LEU LEU A . n 
A 1 170 ARG 170 196 196 ARG ARG A . n 
A 1 171 VAL 171 197 197 VAL VAL A . n 
A 1 172 LEU 172 198 198 LEU LEU A . n 
A 1 173 HIS 173 199 199 HIS HIS A . n 
A 1 174 GLN 174 200 200 GLN GLN A . n 
A 1 175 MET 175 201 201 MET MET A . n 
A 1 176 PRO 176 202 202 PRO PRO A . n 
A 1 177 LEU 177 203 203 LEU LEU A . n 
A 1 178 LEU 178 204 204 LEU LEU A . n 
A 1 179 ASN 179 205 205 ASN ASN A . n 
A 1 180 LEU 180 206 206 LEU LEU A . n 
A 1 181 SER 181 207 207 SER SER A . n 
A 1 182 LEU 182 208 208 LEU LEU A . n 
A 1 183 ASP 183 209 209 ASP ASP A . n 
A 1 184 LEU 184 210 210 LEU LEU A . n 
A 1 185 SER 185 211 211 SER SER A . n 
A 1 186 LEU 186 212 212 LEU LEU A . n 
A 1 187 ASN 187 213 213 ASN ASN A . n 
A 1 188 PRO 188 214 214 PRO PRO A . n 
A 1 189 MET 189 215 215 MET MET A . n 
A 1 190 ASN 190 216 216 ASN ASN A . n 
A 1 191 PHE 191 217 217 PHE PHE A . n 
A 1 192 ILE 192 218 218 ILE ILE A . n 
A 1 193 GLN 193 219 219 GLN GLN A . n 
A 1 194 PRO 194 220 220 PRO PRO A . n 
A 1 195 GLY 195 221 221 GLY GLY A . n 
A 1 196 ALA 196 222 222 ALA ALA A . n 
A 1 197 PHE 197 223 223 PHE PHE A . n 
A 1 198 LYS 198 224 224 LYS LYS A . n 
A 1 199 GLU 199 225 225 GLU GLU A . n 
A 1 200 ILE 200 226 226 ILE ILE A . n 
A 1 201 ARG 201 227 227 ARG ARG A . n 
A 1 202 LEU 202 228 228 LEU LEU A . n 
A 1 203 HIS 203 229 229 HIS HIS A . n 
A 1 204 LYS 204 230 230 LYS LYS A . n 
A 1 205 LEU 205 231 231 LEU LEU A . n 
A 1 206 THR 206 232 232 THR THR A . n 
A 1 207 LEU 207 233 233 LEU LEU A . n 
A 1 208 ARG 208 234 234 ARG ARG A . n 
A 1 209 ASN 209 235 235 ASN ASN A . n 
A 1 210 ASN 210 236 236 ASN ASN A . n 
A 1 211 PHE 211 237 237 PHE PHE A . n 
A 1 212 ASP 212 238 238 ASP ASP A . n 
A 1 213 SER 213 239 239 SER SER A . n 
A 1 214 LEU 214 240 240 LEU LEU A . n 
A 1 215 ASN 215 241 241 ASN ASN A . n 
A 1 216 VAL 216 242 242 VAL VAL A . n 
A 1 217 MET 217 243 243 MET MET A . n 
A 1 218 LYS 218 244 244 LYS LYS A . n 
A 1 219 THR 219 245 245 THR THR A . n 
A 1 220 CYS 220 246 246 CYS CYS A . n 
A 1 221 ILE 221 247 247 ILE ILE A . n 
A 1 222 GLN 222 248 248 GLN GLN A . n 
A 1 223 GLY 223 249 249 GLY GLY A . n 
A 1 224 LEU 224 250 250 LEU LEU A . n 
A 1 225 ALA 225 251 251 ALA ALA A . n 
A 1 226 GLY 226 252 252 GLY GLY A . n 
A 1 227 LEU 227 253 253 LEU LEU A . n 
A 1 228 GLU 228 254 254 GLU GLU A . n 
A 1 229 VAL 229 255 255 VAL VAL A . n 
A 1 230 HIS 230 256 256 HIS HIS A . n 
A 1 231 ARG 231 257 257 ARG ARG A . n 
A 1 232 LEU 232 258 258 LEU LEU A . n 
A 1 233 VAL 233 259 259 VAL VAL A . n 
A 1 234 LEU 234 260 260 LEU LEU A . n 
A 1 235 GLY 235 261 261 GLY GLY A . n 
A 1 236 GLU 236 262 262 GLU GLU A . n 
A 1 237 PHE 237 263 263 PHE PHE A . n 
A 1 238 ARG 238 264 264 ARG ARG A . n 
A 1 239 ASN 239 265 265 ASN ASN A . n 
A 1 240 GLU 240 266 266 GLU GLU A . n 
A 1 241 GLY 241 267 267 GLY GLY A . n 
A 1 242 ASN 242 268 268 ASN ASN A . n 
A 1 243 LEU 243 269 269 LEU LEU A . n 
A 1 244 GLU 244 270 270 GLU GLU A . n 
A 1 245 LYS 245 271 271 LYS LYS A . n 
A 1 246 PHE 246 272 272 PHE PHE A . n 
A 1 247 ASP 247 273 273 ASP ASP A . n 
A 1 248 LYS 248 274 274 LYS LYS A . n 
A 1 249 SER 249 275 275 SER SER A . n 
A 1 250 ALA 250 276 276 ALA ALA A . n 
A 1 251 LEU 251 277 277 LEU LEU A . n 
A 1 252 GLU 252 278 278 GLU GLU A . n 
A 1 253 GLY 253 279 279 GLY GLY A . n 
A 1 254 LEU 254 280 280 LEU LEU A . n 
A 1 255 CYS 255 281 281 CYS CYS A . n 
A 1 256 ASN 256 282 282 ASN ASN A . n 
A 1 257 LEU 257 283 283 LEU LEU A . n 
A 1 258 THR 258 284 284 THR THR A . n 
A 1 259 ILE 259 285 285 ILE ILE A . n 
A 1 260 GLU 260 286 286 GLU GLU A . n 
A 1 261 GLU 261 287 287 GLU GLU A . n 
A 1 262 PHE 262 288 288 PHE PHE A . n 
A 1 263 ARG 263 289 289 ARG ARG A . n 
A 1 264 LEU 264 290 290 LEU LEU A . n 
A 1 265 ALA 265 291 291 ALA ALA A . n 
A 1 266 TYR 266 292 292 TYR TYR A . n 
A 1 267 LEU 267 293 293 LEU LEU A . n 
A 1 268 ASP 268 294 294 ASP ASP A . n 
A 1 269 TYR 269 295 295 TYR TYR A . n 
A 1 270 TYR 270 296 296 TYR TYR A . n 
A 1 271 LEU 271 297 297 LEU LEU A . n 
A 1 272 ASP 272 298 298 ASP ASP A . n 
A 1 273 ASP 273 299 299 ASP ASP A . n 
A 1 274 ILE 274 300 300 ILE ILE A . n 
A 1 275 ILE 275 301 301 ILE ILE A . n 
A 1 276 ASP 276 302 302 ASP ASP A . n 
A 1 277 LEU 277 303 303 LEU LEU A . n 
A 1 278 PHE 278 304 304 PHE PHE A . n 
A 1 279 ASN 279 305 305 ASN ASN A . n 
A 1 280 CYS 280 306 306 CYS CYS A . n 
A 1 281 LEU 281 307 307 LEU LEU A . n 
A 1 282 THR 282 308 308 THR THR A . n 
A 1 283 ASN 283 309 309 ASN ASN A . n 
A 1 284 VAL 284 310 310 VAL VAL A . n 
A 1 285 SER 285 311 311 SER SER A . n 
A 1 286 SER 286 312 312 SER SER A . n 
A 1 287 PHE 287 313 313 PHE PHE A . n 
A 1 288 SER 288 314 314 SER SER A . n 
A 1 289 LEU 289 315 315 LEU LEU A . n 
A 1 290 VAL 290 316 316 VAL VAL A . n 
A 1 291 SER 291 317 317 SER SER A . n 
A 1 292 VAL 292 318 318 VAL VAL A . n 
A 1 293 THR 293 319 319 THR THR A . n 
A 1 294 ILE 294 320 320 ILE ILE A . n 
A 1 295 GLU 295 321 321 GLU GLU A . n 
A 1 296 ARG 296 322 322 ARG ARG A . n 
A 1 297 VAL 297 323 323 VAL VAL A . n 
A 1 298 LYS 298 324 324 LYS LYS A . n 
A 1 299 ASP 299 325 325 ASP ASP A . n 
A 1 300 PHE 300 326 326 PHE PHE A . n 
A 1 301 SER 301 327 327 SER SER A . n 
A 1 302 TYR 302 328 328 TYR TYR A . n 
A 1 303 ASN 303 329 329 ASN ASN A . n 
A 1 304 PHE 304 330 330 PHE PHE A . n 
A 1 305 GLY 305 331 331 GLY GLY A . n 
A 1 306 TRP 306 332 332 TRP TRP A . n 
A 1 307 GLN 307 333 333 GLN GLN A . n 
A 1 308 HIS 308 334 334 HIS HIS A . n 
A 1 309 LEU 309 335 335 LEU LEU A . n 
A 1 310 GLU 310 336 336 GLU GLU A . n 
A 1 311 LEU 311 337 337 LEU LEU A . n 
A 1 312 VAL 312 338 338 VAL VAL A . n 
A 1 313 ASN 313 339 339 ASN ASN A . n 
A 1 314 CYS 314 340 340 CYS CYS A . n 
A 1 315 LYS 315 341 341 LYS LYS A . n 
A 1 316 PHE 316 342 342 PHE PHE A . n 
A 1 317 GLY 317 343 343 GLY GLY A . n 
A 1 318 GLN 318 344 344 GLN GLN A . n 
A 1 319 PHE 319 345 345 PHE PHE A . n 
A 1 320 PRO 320 346 346 PRO PRO A . n 
A 1 321 THR 321 347 347 THR THR A . n 
A 1 322 LEU 322 348 348 LEU LEU A . n 
A 1 323 LYS 323 349 349 LYS LYS A . n 
A 1 324 LEU 324 350 350 LEU LEU A . n 
A 1 325 LYS 325 351 351 LYS LYS A . n 
A 1 326 SER 326 352 352 SER SER A . n 
A 1 327 LEU 327 353 353 LEU LEU A . n 
A 1 328 LYS 328 354 354 LYS LYS A . n 
A 1 329 ARG 329 355 355 ARG ARG A . n 
A 1 330 LEU 330 356 356 LEU LEU A . n 
A 1 331 THR 331 357 357 THR THR A . n 
A 1 332 PHE 332 358 358 PHE PHE A . n 
A 1 333 THR 333 359 359 THR THR A . n 
A 1 334 SER 334 360 360 SER SER A . n 
A 1 335 ASN 335 361 361 ASN ASN A . n 
A 1 336 LYS 336 362 362 LYS LYS A . n 
A 1 337 GLY 337 363 363 GLY GLY A . n 
A 1 338 GLY 338 364 364 GLY GLY A . n 
A 1 339 ASN 339 365 365 ASN ASN A . n 
A 1 340 ALA 340 366 366 ALA ALA A . n 
A 1 341 PHE 341 367 367 PHE PHE A . n 
A 1 342 SER 342 368 368 SER SER A . n 
A 1 343 GLU 343 369 369 GLU GLU A . n 
A 1 344 VAL 344 370 370 VAL VAL A . n 
A 1 345 ASP 345 371 371 ASP ASP A . n 
A 1 346 LEU 346 372 372 LEU LEU A . n 
A 1 347 PRO 347 373 373 PRO PRO A . n 
A 1 348 SER 348 374 374 SER SER A . n 
A 1 349 LEU 349 375 375 LEU LEU A . n 
A 1 350 GLU 350 376 376 GLU GLU A . n 
A 1 351 PHE 351 377 377 PHE PHE A . n 
A 1 352 LEU 352 378 378 LEU LEU A . n 
A 1 353 ASP 353 379 379 ASP ASP A . n 
A 1 354 LEU 354 380 380 LEU LEU A . n 
A 1 355 SER 355 381 381 SER SER A . n 
A 1 356 ARG 356 382 382 ARG ARG A . n 
A 1 357 ASN 357 383 383 ASN ASN A . n 
A 1 358 GLY 358 384 384 GLY GLY A . n 
A 1 359 LEU 359 385 385 LEU LEU A . n 
A 1 360 SER 360 386 386 SER SER A . n 
A 1 361 PHE 361 387 387 PHE PHE A . n 
A 1 362 LYS 362 388 388 LYS LYS A . n 
A 1 363 GLY 363 389 389 GLY GLY A . n 
A 1 364 CYS 364 390 390 CYS CYS A . n 
A 1 365 CYS 365 391 391 CYS CYS A . n 
A 1 366 SER 366 392 392 SER SER A . n 
A 1 367 GLN 367 393 393 GLN GLN A . n 
A 1 368 SER 368 394 394 SER SER A . n 
A 1 369 ASP 369 395 395 ASP ASP A . n 
A 1 370 PHE 370 396 396 PHE PHE A . n 
A 1 371 GLY 371 397 397 GLY GLY A . n 
A 1 372 THR 372 398 398 THR THR A . n 
A 1 373 THR 373 399 399 THR THR A . n 
A 1 374 SER 374 400 400 SER SER A . n 
A 1 375 LEU 375 401 401 LEU LEU A . n 
A 1 376 LYS 376 402 402 LYS LYS A . n 
A 1 377 TYR 377 403 403 TYR TYR A . n 
A 1 378 LEU 378 404 404 LEU LEU A . n 
A 1 379 ASP 379 405 405 ASP ASP A . n 
A 1 380 LEU 380 406 406 LEU LEU A . n 
A 1 381 SER 381 407 407 SER SER A . n 
A 1 382 PHE 382 408 408 PHE PHE A . n 
A 1 383 ASN 383 409 409 ASN ASN A . n 
A 1 384 GLY 384 410 410 GLY GLY A . n 
A 1 385 VAL 385 411 411 VAL VAL A . n 
A 1 386 ILE 386 412 412 ILE ILE A . n 
A 1 387 THR 387 413 413 THR THR A . n 
A 1 388 MET 388 414 414 MET MET A . n 
A 1 389 SER 389 415 415 SER SER A . n 
A 1 390 SER 390 416 416 SER SER A . n 
A 1 391 ASN 391 417 417 ASN ASN A . n 
A 1 392 PHE 392 418 418 PHE PHE A . n 
A 1 393 LEU 393 419 419 LEU LEU A . n 
A 1 394 GLY 394 420 420 GLY GLY A . n 
A 1 395 LEU 395 421 421 LEU LEU A . n 
A 1 396 GLU 396 422 422 GLU GLU A . n 
A 1 397 GLN 397 423 423 GLN GLN A . n 
A 1 398 LEU 398 424 424 LEU LEU A . n 
A 1 399 GLU 399 425 425 GLU GLU A . n 
A 1 400 HIS 400 426 426 HIS HIS A . n 
A 1 401 LEU 401 427 427 LEU LEU A . n 
A 1 402 ASP 402 428 428 ASP ASP A . n 
A 1 403 PHE 403 429 429 PHE PHE A . n 
A 1 404 GLN 404 430 430 GLN GLN A . n 
A 1 405 HIS 405 431 431 HIS HIS A . n 
A 1 406 SER 406 432 432 SER SER A . n 
A 1 407 ASN 407 433 433 ASN ASN A . n 
A 1 408 LEU 408 434 434 LEU LEU A . n 
A 1 409 LYS 409 435 435 LYS LYS A . n 
A 1 410 GLN 410 436 436 GLN GLN A . n 
A 1 411 MET 411 437 437 MET MET A . n 
A 1 412 SER 412 438 438 SER SER A . n 
A 1 413 GLU 413 439 439 GLU GLU A . n 
A 1 414 PHE 414 440 440 PHE PHE A . n 
A 1 415 SER 415 441 441 SER SER A . n 
A 1 416 VAL 416 442 442 VAL VAL A . n 
A 1 417 PHE 417 443 443 PHE PHE A . n 
A 1 418 LEU 418 444 444 LEU LEU A . n 
A 1 419 SER 419 445 445 SER SER A . n 
A 1 420 LEU 420 446 446 LEU LEU A . n 
A 1 421 ARG 421 447 447 ARG ARG A . n 
A 1 422 ASN 422 448 448 ASN ASN A . n 
A 1 423 LEU 423 449 449 LEU LEU A . n 
A 1 424 ILE 424 450 450 ILE ILE A . n 
A 1 425 TYR 425 451 451 TYR TYR A . n 
A 1 426 LEU 426 452 452 LEU LEU A . n 
A 1 427 ASP 427 453 453 ASP ASP A . n 
A 1 428 ILE 428 454 454 ILE ILE A . n 
A 1 429 SER 429 455 455 SER SER A . n 
A 1 430 HIS 430 456 456 HIS HIS A . n 
A 1 431 THR 431 457 457 THR THR A . n 
A 1 432 HIS 432 458 458 HIS HIS A . n 
A 1 433 THR 433 459 459 THR THR A . n 
A 1 434 ARG 434 460 460 ARG ARG A . n 
A 1 435 VAL 435 461 461 VAL VAL A . n 
A 1 436 ALA 436 462 462 ALA ALA A . n 
A 1 437 PHE 437 463 463 PHE PHE A . n 
A 1 438 ASN 438 464 464 ASN ASN A . n 
A 1 439 GLY 439 465 465 GLY GLY A . n 
A 1 440 ILE 440 466 466 ILE ILE A . n 
A 1 441 PHE 441 467 467 PHE PHE A . n 
A 1 442 ASN 442 468 468 ASN ASN A . n 
A 1 443 GLY 443 469 469 GLY GLY A . n 
A 1 444 LEU 444 470 470 LEU LEU A . n 
A 1 445 SER 445 471 471 SER SER A . n 
A 1 446 SER 446 472 472 SER SER A . n 
A 1 447 LEU 447 473 473 LEU LEU A . n 
A 1 448 GLU 448 474 474 GLU GLU A . n 
A 1 449 VAL 449 475 475 VAL VAL A . n 
A 1 450 LEU 450 476 476 LEU LEU A . n 
A 1 451 LYS 451 477 477 LYS LYS A . n 
A 1 452 MET 452 478 478 MET MET A . n 
A 1 453 ALA 453 479 479 ALA ALA A . n 
A 1 454 GLY 454 480 480 GLY GLY A . n 
A 1 455 ASN 455 481 481 ASN ASN A . n 
A 1 456 SER 456 482 482 SER SER A . n 
A 1 457 PHE 457 483 483 PHE PHE A . n 
A 1 458 GLN 458 484 484 GLN GLN A . n 
A 1 459 GLU 459 485 485 GLU GLU A . n 
A 1 460 ASN 460 486 486 ASN ASN A . n 
A 1 461 PHE 461 487 487 PHE PHE A . n 
A 1 462 LEU 462 488 488 LEU LEU A . n 
A 1 463 PRO 463 489 489 PRO PRO A . n 
A 1 464 ASP 464 490 490 ASP ASP A . n 
A 1 465 ILE 465 491 491 ILE ILE A . n 
A 1 466 PHE 466 492 492 PHE PHE A . n 
A 1 467 THR 467 493 493 THR THR A . n 
A 1 468 GLU 468 494 494 GLU GLU A . n 
A 1 469 LEU 469 495 495 LEU LEU A . n 
A 1 470 ARG 470 496 496 ARG ARG A . n 
A 1 471 ASN 471 497 497 ASN ASN A . n 
A 1 472 LEU 472 498 498 LEU LEU A . n 
A 1 473 THR 473 499 499 THR THR A . n 
A 1 474 PHE 474 500 500 PHE PHE A . n 
A 1 475 LEU 475 501 501 LEU LEU A . n 
A 1 476 ASP 476 502 502 ASP ASP A . n 
A 1 477 LEU 477 503 503 LEU LEU A . n 
A 1 478 SER 478 504 504 SER SER A . n 
A 1 479 GLN 479 505 505 GLN GLN A . n 
A 1 480 CYS 480 506 506 CYS CYS A . n 
A 1 481 GLN 481 507 507 GLN GLN A . n 
A 1 482 LEU 482 508 508 LEU LEU A . n 
A 1 483 GLU 483 509 509 GLU GLU A . n 
A 1 484 GLN 484 510 510 GLN GLN A . n 
A 1 485 LEU 485 511 511 LEU LEU A . n 
A 1 486 SER 486 512 512 SER SER A . n 
A 1 487 PRO 487 513 513 PRO PRO A . n 
A 1 488 THR 488 514 514 THR THR A . n 
A 1 489 ALA 489 515 515 ALA ALA A . n 
A 1 490 PHE 490 516 516 PHE PHE A . n 
A 1 491 ASN 491 517 517 ASN ASN A . n 
A 1 492 SER 492 518 518 SER SER A . n 
A 1 493 LEU 493 519 519 LEU LEU A . n 
A 1 494 SER 494 520 520 SER SER A . n 
A 1 495 SER 495 521 521 SER SER A . n 
A 1 496 LEU 496 522 522 LEU LEU A . n 
A 1 497 GLN 497 523 523 GLN GLN A . n 
A 1 498 VAL 498 524 524 VAL VAL A . n 
A 1 499 LEU 499 525 525 LEU LEU A . n 
A 1 500 ASN 500 526 526 ASN ASN A . n 
A 1 501 MET 501 527 527 MET MET A . n 
A 1 502 SER 502 528 528 SER SER A . n 
A 1 503 HIS 503 529 529 HIS HIS A . n 
A 1 504 ASN 504 530 530 ASN ASN A . n 
A 1 505 ASN 505 531 531 ASN ASN A . n 
A 1 506 PHE 506 532 532 PHE PHE A . n 
A 1 507 PHE 507 533 533 PHE PHE A . n 
A 1 508 SER 508 534 534 SER SER A . n 
A 1 509 LEU 509 535 535 LEU LEU A . n 
A 1 510 ASP 510 536 536 ASP ASP A . n 
A 1 511 THR 511 537 537 THR THR A . n 
A 1 512 PHE 512 538 538 PHE PHE A . n 
A 1 513 PRO 513 539 539 PRO PRO A . n 
A 1 514 TYR 514 540 540 TYR TYR A . n 
A 1 515 LYS 515 541 541 LYS LYS A . n 
A 1 516 CYS 516 542 542 CYS CYS A . n 
A 1 517 LEU 517 543 543 LEU LEU A . n 
A 1 518 ASN 518 544 544 ASN ASN A . n 
A 1 519 SER 519 545 545 SER SER A . n 
A 1 520 LEU 520 546 546 LEU LEU A . n 
A 1 521 GLN 521 547 547 GLN GLN A . n 
A 1 522 VAL 522 548 548 VAL VAL A . n 
A 1 523 LEU 523 549 549 LEU LEU A . n 
A 1 524 ASP 524 550 550 ASP ASP A . n 
A 1 525 TYR 525 551 551 TYR TYR A . n 
A 1 526 SER 526 552 552 SER SER A . n 
A 1 527 LEU 527 553 553 LEU LEU A . n 
A 1 528 ASN 528 554 554 ASN ASN A . n 
A 1 529 HIS 529 555 555 HIS HIS A . n 
A 1 530 ILE 530 556 556 ILE ILE A . n 
A 1 531 MET 531 557 557 MET MET A . n 
A 1 532 THR 532 558 558 THR THR A . n 
A 1 533 SER 533 559 559 SER SER A . n 
A 1 534 LYS 534 560 560 LYS LYS A . n 
A 1 535 LYS 535 561 561 LYS LYS A . n 
A 1 536 GLN 536 562 562 GLN GLN A . n 
A 1 537 GLU 537 563 563 GLU GLU A . n 
A 1 538 LEU 538 564 564 LEU LEU A . n 
A 1 539 GLN 539 565 565 GLN GLN A . n 
A 1 540 HIS 540 566 566 HIS HIS A . n 
A 1 541 PHE 541 567 567 PHE PHE A . n 
A 1 542 PRO 542 568 568 PRO PRO A . n 
A 1 543 SER 543 569 569 SER SER A . n 
A 1 544 SER 544 570 570 SER SER A . n 
A 1 545 LEU 545 571 571 LEU LEU A . n 
A 1 546 ALA 546 572 572 ALA ALA A . n 
A 1 547 PHE 547 573 573 PHE PHE A . n 
A 1 548 LEU 548 574 574 LEU LEU A . n 
A 1 549 ASN 549 575 575 ASN ASN A . n 
A 1 550 LEU 550 576 576 LEU LEU A . n 
A 1 551 THR 551 577 577 THR THR A . n 
A 1 552 GLN 552 578 578 GLN GLN A . n 
A 1 553 ASN 553 579 579 ASN ASN A . n 
A 1 554 ASP 554 580 580 ASP ASP A . n 
A 1 555 PHE 555 581 581 PHE PHE A . n 
A 1 556 ALA 556 582 582 ALA ALA A . n 
A 1 557 CYS 557 583 583 CYS CYS A . n 
A 1 558 THR 558 584 584 THR THR A . n 
A 1 559 CYS 559 585 585 CYS CYS A . n 
A 1 560 GLU 560 586 586 GLU GLU A . n 
A 1 561 HIS 561 587 587 HIS HIS A . n 
A 1 562 GLN 562 588 588 GLN GLN A . n 
A 1 563 SER 563 589 589 SER SER A . n 
A 1 564 PHE 564 590 590 PHE PHE A . n 
A 1 565 LEU 565 591 591 LEU LEU A . n 
A 1 566 GLN 566 592 592 GLN GLN A . n 
A 1 567 TRP 567 593 593 TRP TRP A . n 
A 1 568 ILE 568 594 594 ILE ILE A . n 
A 1 569 LYS 569 595 595 LYS LYS A . n 
A 1 570 ASP 570 596 596 ASP ASP A . n 
A 1 571 GLN 571 597 597 GLN GLN A . n 
A 1 572 ARG 572 598 598 ARG ARG A . n 
A 1 573 GLN 573 599 599 GLN GLN A . n 
A 1 574 LEU 574 600 600 LEU LEU A . n 
A 1 575 LEU 575 601 601 LEU LEU A . n 
A 1 576 VAL 576 602 602 VAL VAL A . n 
A 1 577 GLU 577 603 603 GLU GLU A . n 
A 1 578 VAL 578 604 604 VAL VAL A . n 
A 1 579 GLU 579 605 605 GLU GLU A . n 
A 1 580 ARG 580 606 606 ARG ARG A . n 
A 1 581 MET 581 607 607 MET MET A . n 
A 1 582 GLU 582 608 608 GLU GLU A . n 
A 1 583 CYS 583 609 609 CYS CYS A . n 
A 1 584 ALA 584 610 610 ALA ALA A . n 
A 1 585 THR 585 611 611 THR THR A . n 
A 1 586 PRO 586 612 612 PRO PRO A . n 
A 1 587 SER 587 613 613 SER SER A . n 
A 1 588 ASP 588 614 614 ASP ASP A . n 
A 1 589 LYS 589 615 615 LYS LYS A . n 
A 1 590 GLN 590 616 616 GLN GLN A . n 
A 1 591 GLY 591 617 617 GLY GLY A . n 
A 1 592 MET 592 618 618 MET MET A . n 
A 1 593 PRO 593 619 619 PRO PRO A . n 
A 1 594 VAL 594 620 620 VAL VAL A . n 
A 1 595 LEU 595 621 621 LEU LEU A . n 
A 1 596 SER 596 622 622 SER SER A . n 
A 1 597 LEU 597 623 623 LEU LEU A . n 
A 1 598 ASN 598 624 624 ASN ASN A . n 
A 1 599 ILE 599 625 625 ILE ILE A . n 
A 1 600 THR 600 626 626 THR THR A . n 
A 1 601 CYS 601 627 627 CYS CYS A . n 
A 1 602 GLN 602 628 ?   ?   ?   A . n 
A 1 603 MET 603 629 ?   ?   ?   A . n 
A 1 604 ASN 604 630 ?   ?   ?   A . n 
A 1 605 LYS 605 631 ?   ?   ?   A . n 
B 1 1   GLU 1   27  27  GLU GLU B . n 
B 1 2   PRO 2   28  28  PRO PRO B . n 
B 1 3   CYS 3   29  29  CYS CYS B . n 
B 1 4   VAL 4   30  30  VAL VAL B . n 
B 1 5   GLU 5   31  31  GLU GLU B . n 
B 1 6   VAL 6   32  32  VAL VAL B . n 
B 1 7   VAL 7   33  33  VAL VAL B . n 
B 1 8   PRO 8   34  34  PRO PRO B . n 
B 1 9   ASN 9   35  35  ASN ASN B . n 
B 1 10  ILE 10  36  36  ILE ILE B . n 
B 1 11  THR 11  37  37  THR THR B . n 
B 1 12  TYR 12  38  38  TYR TYR B . n 
B 1 13  GLN 13  39  39  GLN GLN B . n 
B 1 14  CYS 14  40  40  CYS CYS B . n 
B 1 15  MET 15  41  41  MET MET B . n 
B 1 16  GLU 16  42  42  GLU GLU B . n 
B 1 17  LEU 17  43  43  LEU LEU B . n 
B 1 18  ASN 18  44  44  ASN ASN B . n 
B 1 19  PHE 19  45  45  PHE PHE B . n 
B 1 20  TYR 20  46  46  TYR TYR B . n 
B 1 21  LYS 21  47  47  LYS LYS B . n 
B 1 22  ILE 22  48  48  ILE ILE B . n 
B 1 23  PRO 23  49  49  PRO PRO B . n 
B 1 24  ASP 24  50  50  ASP ASP B . n 
B 1 25  ASN 25  51  51  ASN ASN B . n 
B 1 26  LEU 26  52  52  LEU LEU B . n 
B 1 27  PRO 27  53  53  PRO PRO B . n 
B 1 28  PHE 28  54  54  PHE PHE B . n 
B 1 29  SER 29  55  55  SER SER B . n 
B 1 30  THR 30  56  56  THR THR B . n 
B 1 31  LYS 31  57  57  LYS LYS B . n 
B 1 32  ASN 32  58  58  ASN ASN B . n 
B 1 33  LEU 33  59  59  LEU LEU B . n 
B 1 34  ASP 34  60  60  ASP ASP B . n 
B 1 35  LEU 35  61  61  LEU LEU B . n 
B 1 36  SER 36  62  62  SER SER B . n 
B 1 37  PHE 37  63  63  PHE PHE B . n 
B 1 38  ASN 38  64  64  ASN ASN B . n 
B 1 39  PRO 39  65  65  PRO PRO B . n 
B 1 40  LEU 40  66  66  LEU LEU B . n 
B 1 41  ARG 41  67  67  ARG ARG B . n 
B 1 42  HIS 42  68  68  HIS HIS B . n 
B 1 43  LEU 43  69  69  LEU LEU B . n 
B 1 44  GLY 44  70  70  GLY GLY B . n 
B 1 45  SER 45  71  71  SER SER B . n 
B 1 46  TYR 46  72  72  TYR TYR B . n 
B 1 47  SER 47  73  73  SER SER B . n 
B 1 48  PHE 48  74  74  PHE PHE B . n 
B 1 49  PHE 49  75  75  PHE PHE B . n 
B 1 50  SER 50  76  76  SER SER B . n 
B 1 51  PHE 51  77  77  PHE PHE B . n 
B 1 52  PRO 52  78  78  PRO PRO B . n 
B 1 53  GLU 53  79  79  GLU GLU B . n 
B 1 54  LEU 54  80  80  LEU LEU B . n 
B 1 55  GLN 55  81  81  GLN GLN B . n 
B 1 56  VAL 56  82  82  VAL VAL B . n 
B 1 57  LEU 57  83  83  LEU LEU B . n 
B 1 58  ASP 58  84  84  ASP ASP B . n 
B 1 59  LEU 59  85  85  LEU LEU B . n 
B 1 60  SER 60  86  86  SER SER B . n 
B 1 61  ARG 61  87  87  ARG ARG B . n 
B 1 62  CYS 62  88  88  CYS CYS B . n 
B 1 63  GLU 63  89  89  GLU GLU B . n 
B 1 64  ILE 64  90  90  ILE ILE B . n 
B 1 65  GLN 65  91  91  GLN GLN B . n 
B 1 66  THR 66  92  92  THR THR B . n 
B 1 67  ILE 67  93  93  ILE ILE B . n 
B 1 68  GLU 68  94  94  GLU GLU B . n 
B 1 69  ASP 69  95  95  ASP ASP B . n 
B 1 70  GLY 70  96  96  GLY GLY B . n 
B 1 71  ALA 71  97  97  ALA ALA B . n 
B 1 72  TYR 72  98  98  TYR TYR B . n 
B 1 73  GLN 73  99  99  GLN GLN B . n 
B 1 74  SER 74  100 100 SER SER B . n 
B 1 75  LEU 75  101 101 LEU LEU B . n 
B 1 76  SER 76  102 102 SER SER B . n 
B 1 77  HIS 77  103 103 HIS HIS B . n 
B 1 78  LEU 78  104 104 LEU LEU B . n 
B 1 79  SER 79  105 105 SER SER B . n 
B 1 80  THR 80  106 106 THR THR B . n 
B 1 81  LEU 81  107 107 LEU LEU B . n 
B 1 82  ILE 82  108 108 ILE ILE B . n 
B 1 83  LEU 83  109 109 LEU LEU B . n 
B 1 84  THR 84  110 110 THR THR B . n 
B 1 85  GLY 85  111 111 GLY GLY B . n 
B 1 86  ASN 86  112 112 ASN ASN B . n 
B 1 87  PRO 87  113 113 PRO PRO B . n 
B 1 88  ILE 88  114 114 ILE ILE B . n 
B 1 89  GLN 89  115 115 GLN GLN B . n 
B 1 90  SER 90  116 116 SER SER B . n 
B 1 91  LEU 91  117 117 LEU LEU B . n 
B 1 92  ALA 92  118 118 ALA ALA B . n 
B 1 93  LEU 93  119 119 LEU LEU B . n 
B 1 94  GLY 94  120 120 GLY GLY B . n 
B 1 95  ALA 95  121 121 ALA ALA B . n 
B 1 96  PHE 96  122 122 PHE PHE B . n 
B 1 97  SER 97  123 123 SER SER B . n 
B 1 98  GLY 98  124 124 GLY GLY B . n 
B 1 99  LEU 99  125 125 LEU LEU B . n 
B 1 100 SER 100 126 126 SER SER B . n 
B 1 101 SER 101 127 127 SER SER B . n 
B 1 102 LEU 102 128 128 LEU LEU B . n 
B 1 103 GLN 103 129 129 GLN GLN B . n 
B 1 104 LYS 104 130 130 LYS LYS B . n 
B 1 105 LEU 105 131 131 LEU LEU B . n 
B 1 106 VAL 106 132 132 VAL VAL B . n 
B 1 107 ALA 107 133 133 ALA ALA B . n 
B 1 108 VAL 108 134 134 VAL VAL B . n 
B 1 109 GLU 109 135 135 GLU GLU B . n 
B 1 110 THR 110 136 136 THR THR B . n 
B 1 111 ASN 111 137 137 ASN ASN B . n 
B 1 112 LEU 112 138 138 LEU LEU B . n 
B 1 113 ALA 113 139 139 ALA ALA B . n 
B 1 114 SER 114 140 140 SER SER B . n 
B 1 115 LEU 115 141 141 LEU LEU B . n 
B 1 116 GLU 116 142 142 GLU GLU B . n 
B 1 117 ASN 117 143 143 ASN ASN B . n 
B 1 118 PHE 118 144 144 PHE PHE B . n 
B 1 119 PRO 119 145 145 PRO PRO B . n 
B 1 120 ILE 120 146 146 ILE ILE B . n 
B 1 121 GLY 121 147 147 GLY GLY B . n 
B 1 122 HIS 122 148 148 HIS HIS B . n 
B 1 123 LEU 123 149 149 LEU LEU B . n 
B 1 124 LYS 124 150 150 LYS LYS B . n 
B 1 125 THR 125 151 151 THR THR B . n 
B 1 126 LEU 126 152 152 LEU LEU B . n 
B 1 127 LYS 127 153 153 LYS LYS B . n 
B 1 128 GLU 128 154 154 GLU GLU B . n 
B 1 129 LEU 129 155 155 LEU LEU B . n 
B 1 130 ASN 130 156 156 ASN ASN B . n 
B 1 131 VAL 131 157 157 VAL VAL B . n 
B 1 132 ALA 132 158 158 ALA ALA B . n 
B 1 133 HIS 133 159 159 HIS HIS B . n 
B 1 134 ASN 134 160 160 ASN ASN B . n 
B 1 135 LEU 135 161 161 LEU LEU B . n 
B 1 136 ILE 136 162 162 ILE ILE B . n 
B 1 137 GLN 137 163 163 GLN GLN B . n 
B 1 138 SER 138 164 164 SER SER B . n 
B 1 139 PHE 139 165 165 PHE PHE B . n 
B 1 140 LYS 140 166 166 LYS LYS B . n 
B 1 141 LEU 141 167 167 LEU LEU B . n 
B 1 142 PRO 142 168 168 PRO PRO B . n 
B 1 143 GLU 143 169 169 GLU GLU B . n 
B 1 144 TYR 144 170 170 TYR TYR B . n 
B 1 145 PHE 145 171 171 PHE PHE B . n 
B 1 146 SER 146 172 172 SER SER B . n 
B 1 147 ASN 147 173 173 ASN ASN B . n 
B 1 148 LEU 148 174 174 LEU LEU B . n 
B 1 149 THR 149 175 175 THR THR B . n 
B 1 150 ASN 150 176 176 ASN ASN B . n 
B 1 151 LEU 151 177 177 LEU LEU B . n 
B 1 152 GLU 152 178 178 GLU GLU B . n 
B 1 153 HIS 153 179 179 HIS HIS B . n 
B 1 154 LEU 154 180 180 LEU LEU B . n 
B 1 155 ASP 155 181 181 ASP ASP B . n 
B 1 156 LEU 156 182 182 LEU LEU B . n 
B 1 157 SER 157 183 183 SER SER B . n 
B 1 158 SER 158 184 184 SER SER B . n 
B 1 159 ASN 159 185 185 ASN ASN B . n 
B 1 160 LYS 160 186 186 LYS LYS B . n 
B 1 161 ILE 161 187 187 ILE ILE B . n 
B 1 162 GLN 162 188 188 GLN GLN B . n 
B 1 163 SER 163 189 189 SER SER B . n 
B 1 164 ILE 164 190 190 ILE ILE B . n 
B 1 165 TYR 165 191 191 TYR TYR B . n 
B 1 166 CYS 166 192 192 CYS CYS B . n 
B 1 167 THR 167 193 193 THR THR B . n 
B 1 168 ASP 168 194 194 ASP ASP B . n 
B 1 169 LEU 169 195 195 LEU LEU B . n 
B 1 170 ARG 170 196 196 ARG ARG B . n 
B 1 171 VAL 171 197 197 VAL VAL B . n 
B 1 172 LEU 172 198 198 LEU LEU B . n 
B 1 173 HIS 173 199 199 HIS HIS B . n 
B 1 174 GLN 174 200 200 GLN GLN B . n 
B 1 175 MET 175 201 201 MET MET B . n 
B 1 176 PRO 176 202 202 PRO PRO B . n 
B 1 177 LEU 177 203 203 LEU LEU B . n 
B 1 178 LEU 178 204 204 LEU LEU B . n 
B 1 179 ASN 179 205 205 ASN ASN B . n 
B 1 180 LEU 180 206 206 LEU LEU B . n 
B 1 181 SER 181 207 207 SER SER B . n 
B 1 182 LEU 182 208 208 LEU LEU B . n 
B 1 183 ASP 183 209 209 ASP ASP B . n 
B 1 184 LEU 184 210 210 LEU LEU B . n 
B 1 185 SER 185 211 211 SER SER B . n 
B 1 186 LEU 186 212 212 LEU LEU B . n 
B 1 187 ASN 187 213 213 ASN ASN B . n 
B 1 188 PRO 188 214 214 PRO PRO B . n 
B 1 189 MET 189 215 215 MET MET B . n 
B 1 190 ASN 190 216 216 ASN ASN B . n 
B 1 191 PHE 191 217 217 PHE PHE B . n 
B 1 192 ILE 192 218 218 ILE ILE B . n 
B 1 193 GLN 193 219 219 GLN GLN B . n 
B 1 194 PRO 194 220 220 PRO PRO B . n 
B 1 195 GLY 195 221 221 GLY GLY B . n 
B 1 196 ALA 196 222 222 ALA ALA B . n 
B 1 197 PHE 197 223 223 PHE PHE B . n 
B 1 198 LYS 198 224 224 LYS LYS B . n 
B 1 199 GLU 199 225 225 GLU GLU B . n 
B 1 200 ILE 200 226 226 ILE ILE B . n 
B 1 201 ARG 201 227 227 ARG ARG B . n 
B 1 202 LEU 202 228 228 LEU LEU B . n 
B 1 203 HIS 203 229 229 HIS HIS B . n 
B 1 204 LYS 204 230 230 LYS LYS B . n 
B 1 205 LEU 205 231 231 LEU LEU B . n 
B 1 206 THR 206 232 232 THR THR B . n 
B 1 207 LEU 207 233 233 LEU LEU B . n 
B 1 208 ARG 208 234 234 ARG ARG B . n 
B 1 209 ASN 209 235 235 ASN ASN B . n 
B 1 210 ASN 210 236 236 ASN ASN B . n 
B 1 211 PHE 211 237 237 PHE PHE B . n 
B 1 212 ASP 212 238 238 ASP ASP B . n 
B 1 213 SER 213 239 239 SER SER B . n 
B 1 214 LEU 214 240 240 LEU LEU B . n 
B 1 215 ASN 215 241 241 ASN ASN B . n 
B 1 216 VAL 216 242 242 VAL VAL B . n 
B 1 217 MET 217 243 243 MET MET B . n 
B 1 218 LYS 218 244 244 LYS LYS B . n 
B 1 219 THR 219 245 245 THR THR B . n 
B 1 220 CYS 220 246 246 CYS CYS B . n 
B 1 221 ILE 221 247 247 ILE ILE B . n 
B 1 222 GLN 222 248 248 GLN GLN B . n 
B 1 223 GLY 223 249 249 GLY GLY B . n 
B 1 224 LEU 224 250 250 LEU LEU B . n 
B 1 225 ALA 225 251 251 ALA ALA B . n 
B 1 226 GLY 226 252 252 GLY GLY B . n 
B 1 227 LEU 227 253 253 LEU LEU B . n 
B 1 228 GLU 228 254 254 GLU GLU B . n 
B 1 229 VAL 229 255 255 VAL VAL B . n 
B 1 230 HIS 230 256 256 HIS HIS B . n 
B 1 231 ARG 231 257 257 ARG ARG B . n 
B 1 232 LEU 232 258 258 LEU LEU B . n 
B 1 233 VAL 233 259 259 VAL VAL B . n 
B 1 234 LEU 234 260 260 LEU LEU B . n 
B 1 235 GLY 235 261 261 GLY GLY B . n 
B 1 236 GLU 236 262 262 GLU GLU B . n 
B 1 237 PHE 237 263 263 PHE PHE B . n 
B 1 238 ARG 238 264 264 ARG ARG B . n 
B 1 239 ASN 239 265 265 ASN ASN B . n 
B 1 240 GLU 240 266 266 GLU GLU B . n 
B 1 241 GLY 241 267 267 GLY GLY B . n 
B 1 242 ASN 242 268 268 ASN ASN B . n 
B 1 243 LEU 243 269 269 LEU LEU B . n 
B 1 244 GLU 244 270 270 GLU GLU B . n 
B 1 245 LYS 245 271 271 LYS LYS B . n 
B 1 246 PHE 246 272 272 PHE PHE B . n 
B 1 247 ASP 247 273 273 ASP ASP B . n 
B 1 248 LYS 248 274 274 LYS LYS B . n 
B 1 249 SER 249 275 275 SER SER B . n 
B 1 250 ALA 250 276 276 ALA ALA B . n 
B 1 251 LEU 251 277 277 LEU LEU B . n 
B 1 252 GLU 252 278 278 GLU GLU B . n 
B 1 253 GLY 253 279 279 GLY GLY B . n 
B 1 254 LEU 254 280 280 LEU LEU B . n 
B 1 255 CYS 255 281 281 CYS CYS B . n 
B 1 256 ASN 256 282 282 ASN ASN B . n 
B 1 257 LEU 257 283 283 LEU LEU B . n 
B 1 258 THR 258 284 284 THR THR B . n 
B 1 259 ILE 259 285 285 ILE ILE B . n 
B 1 260 GLU 260 286 286 GLU GLU B . n 
B 1 261 GLU 261 287 287 GLU GLU B . n 
B 1 262 PHE 262 288 288 PHE PHE B . n 
B 1 263 ARG 263 289 289 ARG ARG B . n 
B 1 264 LEU 264 290 290 LEU LEU B . n 
B 1 265 ALA 265 291 291 ALA ALA B . n 
B 1 266 TYR 266 292 292 TYR TYR B . n 
B 1 267 LEU 267 293 293 LEU LEU B . n 
B 1 268 ASP 268 294 294 ASP ASP B . n 
B 1 269 TYR 269 295 295 TYR TYR B . n 
B 1 270 TYR 270 296 296 TYR TYR B . n 
B 1 271 LEU 271 297 297 LEU LEU B . n 
B 1 272 ASP 272 298 298 ASP ASP B . n 
B 1 273 ASP 273 299 299 ASP ASP B . n 
B 1 274 ILE 274 300 300 ILE ILE B . n 
B 1 275 ILE 275 301 301 ILE ILE B . n 
B 1 276 ASP 276 302 302 ASP ASP B . n 
B 1 277 LEU 277 303 303 LEU LEU B . n 
B 1 278 PHE 278 304 304 PHE PHE B . n 
B 1 279 ASN 279 305 305 ASN ASN B . n 
B 1 280 CYS 280 306 306 CYS CYS B . n 
B 1 281 LEU 281 307 307 LEU LEU B . n 
B 1 282 THR 282 308 308 THR THR B . n 
B 1 283 ASN 283 309 309 ASN ASN B . n 
B 1 284 VAL 284 310 310 VAL VAL B . n 
B 1 285 SER 285 311 311 SER SER B . n 
B 1 286 SER 286 312 312 SER SER B . n 
B 1 287 PHE 287 313 313 PHE PHE B . n 
B 1 288 SER 288 314 314 SER SER B . n 
B 1 289 LEU 289 315 315 LEU LEU B . n 
B 1 290 VAL 290 316 316 VAL VAL B . n 
B 1 291 SER 291 317 317 SER SER B . n 
B 1 292 VAL 292 318 318 VAL VAL B . n 
B 1 293 THR 293 319 319 THR THR B . n 
B 1 294 ILE 294 320 320 ILE ILE B . n 
B 1 295 GLU 295 321 321 GLU GLU B . n 
B 1 296 ARG 296 322 322 ARG ARG B . n 
B 1 297 VAL 297 323 323 VAL VAL B . n 
B 1 298 LYS 298 324 324 LYS LYS B . n 
B 1 299 ASP 299 325 325 ASP ASP B . n 
B 1 300 PHE 300 326 326 PHE PHE B . n 
B 1 301 SER 301 327 327 SER SER B . n 
B 1 302 TYR 302 328 328 TYR TYR B . n 
B 1 303 ASN 303 329 329 ASN ASN B . n 
B 1 304 PHE 304 330 330 PHE PHE B . n 
B 1 305 GLY 305 331 331 GLY GLY B . n 
B 1 306 TRP 306 332 332 TRP TRP B . n 
B 1 307 GLN 307 333 333 GLN GLN B . n 
B 1 308 HIS 308 334 334 HIS HIS B . n 
B 1 309 LEU 309 335 335 LEU LEU B . n 
B 1 310 GLU 310 336 336 GLU GLU B . n 
B 1 311 LEU 311 337 337 LEU LEU B . n 
B 1 312 VAL 312 338 338 VAL VAL B . n 
B 1 313 ASN 313 339 339 ASN ASN B . n 
B 1 314 CYS 314 340 340 CYS CYS B . n 
B 1 315 LYS 315 341 341 LYS LYS B . n 
B 1 316 PHE 316 342 342 PHE PHE B . n 
B 1 317 GLY 317 343 343 GLY GLY B . n 
B 1 318 GLN 318 344 344 GLN GLN B . n 
B 1 319 PHE 319 345 345 PHE PHE B . n 
B 1 320 PRO 320 346 346 PRO PRO B . n 
B 1 321 THR 321 347 347 THR THR B . n 
B 1 322 LEU 322 348 348 LEU LEU B . n 
B 1 323 LYS 323 349 349 LYS LYS B . n 
B 1 324 LEU 324 350 350 LEU LEU B . n 
B 1 325 LYS 325 351 351 LYS LYS B . n 
B 1 326 SER 326 352 352 SER SER B . n 
B 1 327 LEU 327 353 353 LEU LEU B . n 
B 1 328 LYS 328 354 354 LYS LYS B . n 
B 1 329 ARG 329 355 355 ARG ARG B . n 
B 1 330 LEU 330 356 356 LEU LEU B . n 
B 1 331 THR 331 357 357 THR THR B . n 
B 1 332 PHE 332 358 358 PHE PHE B . n 
B 1 333 THR 333 359 359 THR THR B . n 
B 1 334 SER 334 360 360 SER SER B . n 
B 1 335 ASN 335 361 361 ASN ASN B . n 
B 1 336 LYS 336 362 362 LYS LYS B . n 
B 1 337 GLY 337 363 363 GLY GLY B . n 
B 1 338 GLY 338 364 364 GLY GLY B . n 
B 1 339 ASN 339 365 365 ASN ASN B . n 
B 1 340 ALA 340 366 366 ALA ALA B . n 
B 1 341 PHE 341 367 367 PHE PHE B . n 
B 1 342 SER 342 368 368 SER SER B . n 
B 1 343 GLU 343 369 369 GLU GLU B . n 
B 1 344 VAL 344 370 370 VAL VAL B . n 
B 1 345 ASP 345 371 371 ASP ASP B . n 
B 1 346 LEU 346 372 372 LEU LEU B . n 
B 1 347 PRO 347 373 373 PRO PRO B . n 
B 1 348 SER 348 374 374 SER SER B . n 
B 1 349 LEU 349 375 375 LEU LEU B . n 
B 1 350 GLU 350 376 376 GLU GLU B . n 
B 1 351 PHE 351 377 377 PHE PHE B . n 
B 1 352 LEU 352 378 378 LEU LEU B . n 
B 1 353 ASP 353 379 379 ASP ASP B . n 
B 1 354 LEU 354 380 380 LEU LEU B . n 
B 1 355 SER 355 381 381 SER SER B . n 
B 1 356 ARG 356 382 382 ARG ARG B . n 
B 1 357 ASN 357 383 383 ASN ASN B . n 
B 1 358 GLY 358 384 384 GLY GLY B . n 
B 1 359 LEU 359 385 385 LEU LEU B . n 
B 1 360 SER 360 386 386 SER SER B . n 
B 1 361 PHE 361 387 387 PHE PHE B . n 
B 1 362 LYS 362 388 388 LYS LYS B . n 
B 1 363 GLY 363 389 389 GLY GLY B . n 
B 1 364 CYS 364 390 390 CYS CYS B . n 
B 1 365 CYS 365 391 391 CYS CYS B . n 
B 1 366 SER 366 392 392 SER SER B . n 
B 1 367 GLN 367 393 393 GLN GLN B . n 
B 1 368 SER 368 394 394 SER SER B . n 
B 1 369 ASP 369 395 395 ASP ASP B . n 
B 1 370 PHE 370 396 396 PHE PHE B . n 
B 1 371 GLY 371 397 397 GLY GLY B . n 
B 1 372 THR 372 398 398 THR THR B . n 
B 1 373 THR 373 399 399 THR THR B . n 
B 1 374 SER 374 400 400 SER SER B . n 
B 1 375 LEU 375 401 401 LEU LEU B . n 
B 1 376 LYS 376 402 402 LYS LYS B . n 
B 1 377 TYR 377 403 403 TYR TYR B . n 
B 1 378 LEU 378 404 404 LEU LEU B . n 
B 1 379 ASP 379 405 405 ASP ASP B . n 
B 1 380 LEU 380 406 406 LEU LEU B . n 
B 1 381 SER 381 407 407 SER SER B . n 
B 1 382 PHE 382 408 408 PHE PHE B . n 
B 1 383 ASN 383 409 409 ASN ASN B . n 
B 1 384 GLY 384 410 410 GLY GLY B . n 
B 1 385 VAL 385 411 411 VAL VAL B . n 
B 1 386 ILE 386 412 412 ILE ILE B . n 
B 1 387 THR 387 413 413 THR THR B . n 
B 1 388 MET 388 414 414 MET MET B . n 
B 1 389 SER 389 415 415 SER SER B . n 
B 1 390 SER 390 416 416 SER SER B . n 
B 1 391 ASN 391 417 417 ASN ASN B . n 
B 1 392 PHE 392 418 418 PHE PHE B . n 
B 1 393 LEU 393 419 419 LEU LEU B . n 
B 1 394 GLY 394 420 420 GLY GLY B . n 
B 1 395 LEU 395 421 421 LEU LEU B . n 
B 1 396 GLU 396 422 422 GLU GLU B . n 
B 1 397 GLN 397 423 423 GLN GLN B . n 
B 1 398 LEU 398 424 424 LEU LEU B . n 
B 1 399 GLU 399 425 425 GLU GLU B . n 
B 1 400 HIS 400 426 426 HIS HIS B . n 
B 1 401 LEU 401 427 427 LEU LEU B . n 
B 1 402 ASP 402 428 428 ASP ASP B . n 
B 1 403 PHE 403 429 429 PHE PHE B . n 
B 1 404 GLN 404 430 430 GLN GLN B . n 
B 1 405 HIS 405 431 431 HIS HIS B . n 
B 1 406 SER 406 432 432 SER SER B . n 
B 1 407 ASN 407 433 433 ASN ASN B . n 
B 1 408 LEU 408 434 434 LEU LEU B . n 
B 1 409 LYS 409 435 435 LYS LYS B . n 
B 1 410 GLN 410 436 436 GLN GLN B . n 
B 1 411 MET 411 437 437 MET MET B . n 
B 1 412 SER 412 438 438 SER SER B . n 
B 1 413 GLU 413 439 439 GLU GLU B . n 
B 1 414 PHE 414 440 440 PHE PHE B . n 
B 1 415 SER 415 441 441 SER SER B . n 
B 1 416 VAL 416 442 442 VAL VAL B . n 
B 1 417 PHE 417 443 443 PHE PHE B . n 
B 1 418 LEU 418 444 444 LEU LEU B . n 
B 1 419 SER 419 445 445 SER SER B . n 
B 1 420 LEU 420 446 446 LEU LEU B . n 
B 1 421 ARG 421 447 447 ARG ARG B . n 
B 1 422 ASN 422 448 448 ASN ASN B . n 
B 1 423 LEU 423 449 449 LEU LEU B . n 
B 1 424 ILE 424 450 450 ILE ILE B . n 
B 1 425 TYR 425 451 451 TYR TYR B . n 
B 1 426 LEU 426 452 452 LEU LEU B . n 
B 1 427 ASP 427 453 453 ASP ASP B . n 
B 1 428 ILE 428 454 454 ILE ILE B . n 
B 1 429 SER 429 455 455 SER SER B . n 
B 1 430 HIS 430 456 456 HIS HIS B . n 
B 1 431 THR 431 457 457 THR THR B . n 
B 1 432 HIS 432 458 458 HIS HIS B . n 
B 1 433 THR 433 459 459 THR THR B . n 
B 1 434 ARG 434 460 460 ARG ARG B . n 
B 1 435 VAL 435 461 461 VAL VAL B . n 
B 1 436 ALA 436 462 462 ALA ALA B . n 
B 1 437 PHE 437 463 463 PHE PHE B . n 
B 1 438 ASN 438 464 464 ASN ASN B . n 
B 1 439 GLY 439 465 465 GLY GLY B . n 
B 1 440 ILE 440 466 466 ILE ILE B . n 
B 1 441 PHE 441 467 467 PHE PHE B . n 
B 1 442 ASN 442 468 468 ASN ASN B . n 
B 1 443 GLY 443 469 469 GLY GLY B . n 
B 1 444 LEU 444 470 470 LEU LEU B . n 
B 1 445 SER 445 471 471 SER SER B . n 
B 1 446 SER 446 472 472 SER SER B . n 
B 1 447 LEU 447 473 473 LEU LEU B . n 
B 1 448 GLU 448 474 474 GLU GLU B . n 
B 1 449 VAL 449 475 475 VAL VAL B . n 
B 1 450 LEU 450 476 476 LEU LEU B . n 
B 1 451 LYS 451 477 477 LYS LYS B . n 
B 1 452 MET 452 478 478 MET MET B . n 
B 1 453 ALA 453 479 479 ALA ALA B . n 
B 1 454 GLY 454 480 480 GLY GLY B . n 
B 1 455 ASN 455 481 481 ASN ASN B . n 
B 1 456 SER 456 482 482 SER SER B . n 
B 1 457 PHE 457 483 483 PHE PHE B . n 
B 1 458 GLN 458 484 484 GLN GLN B . n 
B 1 459 GLU 459 485 485 GLU GLU B . n 
B 1 460 ASN 460 486 486 ASN ASN B . n 
B 1 461 PHE 461 487 487 PHE PHE B . n 
B 1 462 LEU 462 488 488 LEU LEU B . n 
B 1 463 PRO 463 489 489 PRO PRO B . n 
B 1 464 ASP 464 490 490 ASP ASP B . n 
B 1 465 ILE 465 491 491 ILE ILE B . n 
B 1 466 PHE 466 492 492 PHE PHE B . n 
B 1 467 THR 467 493 493 THR THR B . n 
B 1 468 GLU 468 494 494 GLU GLU B . n 
B 1 469 LEU 469 495 495 LEU LEU B . n 
B 1 470 ARG 470 496 496 ARG ARG B . n 
B 1 471 ASN 471 497 497 ASN ASN B . n 
B 1 472 LEU 472 498 498 LEU LEU B . n 
B 1 473 THR 473 499 499 THR THR B . n 
B 1 474 PHE 474 500 500 PHE PHE B . n 
B 1 475 LEU 475 501 501 LEU LEU B . n 
B 1 476 ASP 476 502 502 ASP ASP B . n 
B 1 477 LEU 477 503 503 LEU LEU B . n 
B 1 478 SER 478 504 504 SER SER B . n 
B 1 479 GLN 479 505 505 GLN GLN B . n 
B 1 480 CYS 480 506 506 CYS CYS B . n 
B 1 481 GLN 481 507 507 GLN GLN B . n 
B 1 482 LEU 482 508 508 LEU LEU B . n 
B 1 483 GLU 483 509 509 GLU GLU B . n 
B 1 484 GLN 484 510 510 GLN GLN B . n 
B 1 485 LEU 485 511 511 LEU LEU B . n 
B 1 486 SER 486 512 512 SER SER B . n 
B 1 487 PRO 487 513 513 PRO PRO B . n 
B 1 488 THR 488 514 514 THR THR B . n 
B 1 489 ALA 489 515 515 ALA ALA B . n 
B 1 490 PHE 490 516 516 PHE PHE B . n 
B 1 491 ASN 491 517 517 ASN ASN B . n 
B 1 492 SER 492 518 518 SER SER B . n 
B 1 493 LEU 493 519 519 LEU LEU B . n 
B 1 494 SER 494 520 520 SER SER B . n 
B 1 495 SER 495 521 521 SER SER B . n 
B 1 496 LEU 496 522 522 LEU LEU B . n 
B 1 497 GLN 497 523 523 GLN GLN B . n 
B 1 498 VAL 498 524 524 VAL VAL B . n 
B 1 499 LEU 499 525 525 LEU LEU B . n 
B 1 500 ASN 500 526 526 ASN ASN B . n 
B 1 501 MET 501 527 527 MET MET B . n 
B 1 502 SER 502 528 528 SER SER B . n 
B 1 503 HIS 503 529 529 HIS HIS B . n 
B 1 504 ASN 504 530 530 ASN ASN B . n 
B 1 505 ASN 505 531 531 ASN ASN B . n 
B 1 506 PHE 506 532 532 PHE PHE B . n 
B 1 507 PHE 507 533 533 PHE PHE B . n 
B 1 508 SER 508 534 534 SER SER B . n 
B 1 509 LEU 509 535 535 LEU LEU B . n 
B 1 510 ASP 510 536 536 ASP ASP B . n 
B 1 511 THR 511 537 537 THR THR B . n 
B 1 512 PHE 512 538 538 PHE PHE B . n 
B 1 513 PRO 513 539 539 PRO PRO B . n 
B 1 514 TYR 514 540 540 TYR TYR B . n 
B 1 515 LYS 515 541 541 LYS LYS B . n 
B 1 516 CYS 516 542 542 CYS CYS B . n 
B 1 517 LEU 517 543 543 LEU LEU B . n 
B 1 518 ASN 518 544 544 ASN ASN B . n 
B 1 519 SER 519 545 545 SER SER B . n 
B 1 520 LEU 520 546 546 LEU LEU B . n 
B 1 521 GLN 521 547 547 GLN GLN B . n 
B 1 522 VAL 522 548 548 VAL VAL B . n 
B 1 523 LEU 523 549 549 LEU LEU B . n 
B 1 524 ASP 524 550 550 ASP ASP B . n 
B 1 525 TYR 525 551 551 TYR TYR B . n 
B 1 526 SER 526 552 552 SER SER B . n 
B 1 527 LEU 527 553 553 LEU LEU B . n 
B 1 528 ASN 528 554 554 ASN ASN B . n 
B 1 529 HIS 529 555 555 HIS HIS B . n 
B 1 530 ILE 530 556 556 ILE ILE B . n 
B 1 531 MET 531 557 557 MET MET B . n 
B 1 532 THR 532 558 558 THR THR B . n 
B 1 533 SER 533 559 559 SER SER B . n 
B 1 534 LYS 534 560 560 LYS LYS B . n 
B 1 535 LYS 535 561 561 LYS LYS B . n 
B 1 536 GLN 536 562 562 GLN GLN B . n 
B 1 537 GLU 537 563 563 GLU GLU B . n 
B 1 538 LEU 538 564 564 LEU LEU B . n 
B 1 539 GLN 539 565 565 GLN GLN B . n 
B 1 540 HIS 540 566 566 HIS HIS B . n 
B 1 541 PHE 541 567 567 PHE PHE B . n 
B 1 542 PRO 542 568 568 PRO PRO B . n 
B 1 543 SER 543 569 569 SER SER B . n 
B 1 544 SER 544 570 570 SER SER B . n 
B 1 545 LEU 545 571 571 LEU LEU B . n 
B 1 546 ALA 546 572 572 ALA ALA B . n 
B 1 547 PHE 547 573 573 PHE PHE B . n 
B 1 548 LEU 548 574 574 LEU LEU B . n 
B 1 549 ASN 549 575 575 ASN ASN B . n 
B 1 550 LEU 550 576 576 LEU LEU B . n 
B 1 551 THR 551 577 577 THR THR B . n 
B 1 552 GLN 552 578 578 GLN GLN B . n 
B 1 553 ASN 553 579 579 ASN ASN B . n 
B 1 554 ASP 554 580 580 ASP ASP B . n 
B 1 555 PHE 555 581 581 PHE PHE B . n 
B 1 556 ALA 556 582 582 ALA ALA B . n 
B 1 557 CYS 557 583 583 CYS CYS B . n 
B 1 558 THR 558 584 584 THR THR B . n 
B 1 559 CYS 559 585 585 CYS CYS B . n 
B 1 560 GLU 560 586 586 GLU GLU B . n 
B 1 561 HIS 561 587 587 HIS HIS B . n 
B 1 562 GLN 562 588 588 GLN GLN B . n 
B 1 563 SER 563 589 589 SER SER B . n 
B 1 564 PHE 564 590 590 PHE PHE B . n 
B 1 565 LEU 565 591 591 LEU LEU B . n 
B 1 566 GLN 566 592 592 GLN GLN B . n 
B 1 567 TRP 567 593 593 TRP TRP B . n 
B 1 568 ILE 568 594 594 ILE ILE B . n 
B 1 569 LYS 569 595 595 LYS LYS B . n 
B 1 570 ASP 570 596 596 ASP ASP B . n 
B 1 571 GLN 571 597 597 GLN GLN B . n 
B 1 572 ARG 572 598 598 ARG ARG B . n 
B 1 573 GLN 573 599 599 GLN GLN B . n 
B 1 574 LEU 574 600 600 LEU LEU B . n 
B 1 575 LEU 575 601 601 LEU LEU B . n 
B 1 576 VAL 576 602 602 VAL VAL B . n 
B 1 577 GLU 577 603 603 GLU GLU B . n 
B 1 578 VAL 578 604 604 VAL VAL B . n 
B 1 579 GLU 579 605 605 GLU GLU B . n 
B 1 580 ARG 580 606 606 ARG ARG B . n 
B 1 581 MET 581 607 607 MET MET B . n 
B 1 582 GLU 582 608 608 GLU GLU B . n 
B 1 583 CYS 583 609 609 CYS CYS B . n 
B 1 584 ALA 584 610 610 ALA ALA B . n 
B 1 585 THR 585 611 611 THR THR B . n 
B 1 586 PRO 586 612 612 PRO PRO B . n 
B 1 587 SER 587 613 613 SER SER B . n 
B 1 588 ASP 588 614 614 ASP ASP B . n 
B 1 589 LYS 589 615 615 LYS LYS B . n 
B 1 590 GLN 590 616 616 GLN GLN B . n 
B 1 591 GLY 591 617 617 GLY GLY B . n 
B 1 592 MET 592 618 618 MET MET B . n 
B 1 593 PRO 593 619 619 PRO PRO B . n 
B 1 594 VAL 594 620 620 VAL VAL B . n 
B 1 595 LEU 595 621 621 LEU LEU B . n 
B 1 596 SER 596 622 622 SER SER B . n 
B 1 597 LEU 597 623 623 LEU LEU B . n 
B 1 598 ASN 598 624 624 ASN ASN B . n 
B 1 599 ILE 599 625 625 ILE ILE B . n 
B 1 600 THR 600 626 626 THR THR B . n 
B 1 601 CYS 601 627 627 CYS CYS B . n 
B 1 602 GLN 602 628 ?   ?   ?   B . n 
B 1 603 MET 603 629 ?   ?   ?   B . n 
B 1 604 ASN 604 630 ?   ?   ?   B . n 
B 1 605 LYS 605 631 ?   ?   ?   B . n 
C 2 1   GLN 1   19  19  GLN GLN C . n 
C 2 2   LYS 2   20  20  LYS LYS C . n 
C 2 3   GLN 3   21  21  GLN GLN C . n 
C 2 4   TYR 4   22  22  TYR TYR C . n 
C 2 5   TRP 5   23  23  TRP TRP C . n 
C 2 6   VAL 6   24  24  VAL VAL C . n 
C 2 7   CYS 7   25  25  CYS CYS C . n 
C 2 8   ASN 8   26  26  ASN ASN C . n 
C 2 9   SER 9   27  27  SER SER C . n 
C 2 10  SER 10  28  28  SER SER C . n 
C 2 11  ASP 11  29  29  ASP ASP C . n 
C 2 12  ALA 12  30  30  ALA ALA C . n 
C 2 13  SER 13  31  31  SER SER C . n 
C 2 14  ILE 14  32  32  ILE ILE C . n 
C 2 15  SER 15  33  33  SER SER C . n 
C 2 16  TYR 16  34  34  TYR TYR C . n 
C 2 17  THR 17  35  35  THR THR C . n 
C 2 18  TYR 18  36  36  TYR TYR C . n 
C 2 19  CYS 19  37  37  CYS CYS C . n 
C 2 20  ASP 20  38  38  ASP ASP C . n 
C 2 21  LYS 21  39  39  LYS LYS C . n 
C 2 22  MET 22  40  40  MET MET C . n 
C 2 23  GLN 23  41  41  GLN GLN C . n 
C 2 24  TYR 24  42  42  TYR TYR C . n 
C 2 25  PRO 25  43  43  PRO PRO C . n 
C 2 26  ILE 26  44  44  ILE ILE C . n 
C 2 27  SER 27  45  45  SER SER C . n 
C 2 28  ILE 28  46  46  ILE ILE C . n 
C 2 29  ASN 29  47  47  ASN ASN C . n 
C 2 30  VAL 30  48  48  VAL VAL C . n 
C 2 31  ASN 31  49  49  ASN ASN C . n 
C 2 32  PRO 32  50  50  PRO PRO C . n 
C 2 33  CYS 33  51  51  CYS CYS C . n 
C 2 34  ILE 34  52  52  ILE ILE C . n 
C 2 35  GLU 35  53  53  GLU GLU C . n 
C 2 36  LEU 36  54  54  LEU LEU C . n 
C 2 37  LYS 37  55  55  LYS LYS C . n 
C 2 38  GLY 38  56  56  GLY GLY C . n 
C 2 39  SER 39  57  57  SER SER C . n 
C 2 40  LYS 40  58  58  LYS LYS C . n 
C 2 41  GLY 41  59  59  GLY GLY C . n 
C 2 42  LEU 42  60  60  LEU LEU C . n 
C 2 43  LEU 43  61  61  LEU LEU C . n 
C 2 44  HIS 44  62  62  HIS HIS C . n 
C 2 45  ILE 45  63  63  ILE ILE C . n 
C 2 46  PHE 46  64  64  PHE PHE C . n 
C 2 47  TYR 47  65  65  TYR TYR C . n 
C 2 48  ILE 48  66  66  ILE ILE C . n 
C 2 49  PRO 49  67  67  PRO PRO C . n 
C 2 50  ARG 50  68  68  ARG ARG C . n 
C 2 51  ARG 51  69  69  ARG ARG C . n 
C 2 52  ASP 52  70  70  ASP ASP C . n 
C 2 53  LEU 53  71  71  LEU LEU C . n 
C 2 54  LYS 54  72  72  LYS LYS C . n 
C 2 55  GLN 55  73  73  GLN GLN C . n 
C 2 56  LEU 56  74  74  LEU LEU C . n 
C 2 57  TYR 57  75  75  TYR TYR C . n 
C 2 58  PHE 58  76  76  PHE PHE C . n 
C 2 59  ASN 59  77  77  ASN ASN C . n 
C 2 60  LEU 60  78  78  LEU LEU C . n 
C 2 61  TYR 61  79  79  TYR TYR C . n 
C 2 62  ILE 62  80  80  ILE ILE C . n 
C 2 63  THR 63  81  81  THR THR C . n 
C 2 64  VAL 64  82  82  VAL VAL C . n 
C 2 65  ASN 65  83  83  ASN ASN C . n 
C 2 66  THR 66  84  84  THR THR C . n 
C 2 67  MET 67  85  85  MET MET C . n 
C 2 68  ASN 68  86  86  ASN ASN C . n 
C 2 69  LEU 69  87  87  LEU LEU C . n 
C 2 70  PRO 70  88  88  PRO PRO C . n 
C 2 71  LYS 71  89  89  LYS LYS C . n 
C 2 72  ARG 72  90  90  ARG ARG C . n 
C 2 73  LYS 73  91  91  LYS LYS C . n 
C 2 74  GLU 74  92  92  GLU GLU C . n 
C 2 75  VAL 75  93  93  VAL VAL C . n 
C 2 76  ILE 76  94  94  ILE ILE C . n 
C 2 77  CYS 77  95  95  CYS CYS C . n 
C 2 78  ARG 78  96  96  ARG ARG C . n 
C 2 79  GLY 79  97  97  GLY GLY C . n 
C 2 80  SER 80  98  98  SER SER C . n 
C 2 81  ASP 81  99  99  ASP ASP C . n 
C 2 82  ASP 82  100 100 ASP ASP C . n 
C 2 83  ASP 83  101 101 ASP ASP C . n 
C 2 84  TYR 84  102 102 TYR TYR C . n 
C 2 85  SER 85  103 103 SER SER C . n 
C 2 86  PHE 86  104 104 PHE PHE C . n 
C 2 87  CYS 87  105 105 CYS CYS C . n 
C 2 88  ARG 88  106 106 ARG ARG C . n 
C 2 89  ALA 89  107 107 ALA ALA C . n 
C 2 90  LEU 90  108 108 LEU LEU C . n 
C 2 91  LYS 91  109 109 LYS LYS C . n 
C 2 92  GLY 92  110 110 GLY GLY C . n 
C 2 93  GLU 93  111 111 GLU GLU C . n 
C 2 94  THR 94  112 112 THR THR C . n 
C 2 95  VAL 95  113 113 VAL VAL C . n 
C 2 96  ASN 96  114 114 ASN ASN C . n 
C 2 97  THR 97  115 115 THR THR C . n 
C 2 98  THR 98  116 116 THR THR C . n 
C 2 99  ILE 99  117 117 ILE ILE C . n 
C 2 100 SER 100 118 118 SER SER C . n 
C 2 101 PHE 101 119 119 PHE PHE C . n 
C 2 102 SER 102 120 120 SER SER C . n 
C 2 103 PHE 103 121 121 PHE PHE C . n 
C 2 104 LYS 104 122 122 LYS LYS C . n 
C 2 105 GLY 105 123 123 GLY GLY C . n 
C 2 106 ILE 106 124 124 ILE ILE C . n 
C 2 107 LYS 107 125 125 LYS LYS C . n 
C 2 108 PHE 108 126 126 PHE PHE C . n 
C 2 109 SER 109 127 127 SER SER C . n 
C 2 110 LYS 110 128 128 LYS LYS C . n 
C 2 111 GLY 111 129 129 GLY GLY C . n 
C 2 112 LYS 112 130 130 LYS LYS C . n 
C 2 113 TYR 113 131 131 TYR TYR C . n 
C 2 114 LYS 114 132 132 LYS LYS C . n 
C 2 115 CYS 115 133 133 CYS CYS C . n 
C 2 116 VAL 116 134 134 VAL VAL C . n 
C 2 117 VAL 117 135 135 VAL VAL C . n 
C 2 118 GLU 118 136 136 GLU GLU C . n 
C 2 119 ALA 119 137 137 ALA ALA C . n 
C 2 120 ILE 120 138 138 ILE ILE C . n 
C 2 121 SER 121 139 139 SER SER C . n 
C 2 122 GLY 122 140 140 GLY GLY C . n 
C 2 123 SER 123 141 141 SER SER C . n 
C 2 124 PRO 124 142 142 PRO PRO C . n 
C 2 125 GLU 125 143 143 GLU GLU C . n 
C 2 126 GLU 126 144 144 GLU GLU C . n 
C 2 127 MET 127 145 145 MET MET C . n 
C 2 128 LEU 128 146 146 LEU LEU C . n 
C 2 129 PHE 129 147 147 PHE PHE C . n 
C 2 130 CYS 130 148 148 CYS CYS C . n 
C 2 131 LEU 131 149 149 LEU LEU C . n 
C 2 132 GLU 132 150 150 GLU GLU C . n 
C 2 133 PHE 133 151 151 PHE PHE C . n 
C 2 134 VAL 134 152 152 VAL VAL C . n 
C 2 135 ILE 135 153 153 ILE ILE C . n 
C 2 136 LEU 136 154 154 LEU LEU C . n 
C 2 137 HIS 137 155 155 HIS HIS C . n 
C 2 138 GLN 138 156 156 GLN GLN C . n 
C 2 139 PRO 139 157 157 PRO PRO C . n 
C 2 140 ASN 140 158 158 ASN ASN C . n 
C 2 141 SER 141 159 ?   ?   ?   C . n 
C 2 142 ASN 142 160 ?   ?   ?   C . n 
D 2 1   GLN 1   19  19  GLN GLN D . n 
D 2 2   LYS 2   20  20  LYS LYS D . n 
D 2 3   GLN 3   21  21  GLN GLN D . n 
D 2 4   TYR 4   22  22  TYR TYR D . n 
D 2 5   TRP 5   23  23  TRP TRP D . n 
D 2 6   VAL 6   24  24  VAL VAL D . n 
D 2 7   CYS 7   25  25  CYS CYS D . n 
D 2 8   ASN 8   26  26  ASN ASN D . n 
D 2 9   SER 9   27  27  SER SER D . n 
D 2 10  SER 10  28  28  SER SER D . n 
D 2 11  ASP 11  29  29  ASP ASP D . n 
D 2 12  ALA 12  30  30  ALA ALA D . n 
D 2 13  SER 13  31  31  SER SER D . n 
D 2 14  ILE 14  32  32  ILE ILE D . n 
D 2 15  SER 15  33  33  SER SER D . n 
D 2 16  TYR 16  34  34  TYR TYR D . n 
D 2 17  THR 17  35  35  THR THR D . n 
D 2 18  TYR 18  36  36  TYR TYR D . n 
D 2 19  CYS 19  37  37  CYS CYS D . n 
D 2 20  ASP 20  38  38  ASP ASP D . n 
D 2 21  LYS 21  39  39  LYS LYS D . n 
D 2 22  MET 22  40  40  MET MET D . n 
D 2 23  GLN 23  41  41  GLN GLN D . n 
D 2 24  TYR 24  42  42  TYR TYR D . n 
D 2 25  PRO 25  43  43  PRO PRO D . n 
D 2 26  ILE 26  44  44  ILE ILE D . n 
D 2 27  SER 27  45  45  SER SER D . n 
D 2 28  ILE 28  46  46  ILE ILE D . n 
D 2 29  ASN 29  47  47  ASN ASN D . n 
D 2 30  VAL 30  48  48  VAL VAL D . n 
D 2 31  ASN 31  49  49  ASN ASN D . n 
D 2 32  PRO 32  50  50  PRO PRO D . n 
D 2 33  CYS 33  51  51  CYS CYS D . n 
D 2 34  ILE 34  52  52  ILE ILE D . n 
D 2 35  GLU 35  53  53  GLU GLU D . n 
D 2 36  LEU 36  54  54  LEU LEU D . n 
D 2 37  LYS 37  55  55  LYS LYS D . n 
D 2 38  GLY 38  56  56  GLY GLY D . n 
D 2 39  SER 39  57  57  SER SER D . n 
D 2 40  LYS 40  58  58  LYS LYS D . n 
D 2 41  GLY 41  59  59  GLY GLY D . n 
D 2 42  LEU 42  60  60  LEU LEU D . n 
D 2 43  LEU 43  61  61  LEU LEU D . n 
D 2 44  HIS 44  62  62  HIS HIS D . n 
D 2 45  ILE 45  63  63  ILE ILE D . n 
D 2 46  PHE 46  64  64  PHE PHE D . n 
D 2 47  TYR 47  65  65  TYR TYR D . n 
D 2 48  ILE 48  66  66  ILE ILE D . n 
D 2 49  PRO 49  67  67  PRO PRO D . n 
D 2 50  ARG 50  68  68  ARG ARG D . n 
D 2 51  ARG 51  69  69  ARG ARG D . n 
D 2 52  ASP 52  70  70  ASP ASP D . n 
D 2 53  LEU 53  71  71  LEU LEU D . n 
D 2 54  LYS 54  72  72  LYS LYS D . n 
D 2 55  GLN 55  73  73  GLN GLN D . n 
D 2 56  LEU 56  74  74  LEU LEU D . n 
D 2 57  TYR 57  75  75  TYR TYR D . n 
D 2 58  PHE 58  76  76  PHE PHE D . n 
D 2 59  ASN 59  77  77  ASN ASN D . n 
D 2 60  LEU 60  78  78  LEU LEU D . n 
D 2 61  TYR 61  79  79  TYR TYR D . n 
D 2 62  ILE 62  80  80  ILE ILE D . n 
D 2 63  THR 63  81  81  THR THR D . n 
D 2 64  VAL 64  82  82  VAL VAL D . n 
D 2 65  ASN 65  83  83  ASN ASN D . n 
D 2 66  THR 66  84  84  THR THR D . n 
D 2 67  MET 67  85  85  MET MET D . n 
D 2 68  ASN 68  86  86  ASN ASN D . n 
D 2 69  LEU 69  87  87  LEU LEU D . n 
D 2 70  PRO 70  88  88  PRO PRO D . n 
D 2 71  LYS 71  89  89  LYS LYS D . n 
D 2 72  ARG 72  90  90  ARG ARG D . n 
D 2 73  LYS 73  91  91  LYS LYS D . n 
D 2 74  GLU 74  92  92  GLU GLU D . n 
D 2 75  VAL 75  93  93  VAL VAL D . n 
D 2 76  ILE 76  94  94  ILE ILE D . n 
D 2 77  CYS 77  95  95  CYS CYS D . n 
D 2 78  ARG 78  96  96  ARG ARG D . n 
D 2 79  GLY 79  97  97  GLY GLY D . n 
D 2 80  SER 80  98  98  SER SER D . n 
D 2 81  ASP 81  99  99  ASP ASP D . n 
D 2 82  ASP 82  100 100 ASP ASP D . n 
D 2 83  ASP 83  101 101 ASP ASP D . n 
D 2 84  TYR 84  102 102 TYR TYR D . n 
D 2 85  SER 85  103 103 SER SER D . n 
D 2 86  PHE 86  104 104 PHE PHE D . n 
D 2 87  CYS 87  105 105 CYS CYS D . n 
D 2 88  ARG 88  106 106 ARG ARG D . n 
D 2 89  ALA 89  107 107 ALA ALA D . n 
D 2 90  LEU 90  108 108 LEU LEU D . n 
D 2 91  LYS 91  109 109 LYS LYS D . n 
D 2 92  GLY 92  110 110 GLY GLY D . n 
D 2 93  GLU 93  111 111 GLU GLU D . n 
D 2 94  THR 94  112 112 THR THR D . n 
D 2 95  VAL 95  113 113 VAL VAL D . n 
D 2 96  ASN 96  114 114 ASN ASN D . n 
D 2 97  THR 97  115 115 THR THR D . n 
D 2 98  THR 98  116 116 THR THR D . n 
D 2 99  ILE 99  117 117 ILE ILE D . n 
D 2 100 SER 100 118 118 SER SER D . n 
D 2 101 PHE 101 119 119 PHE PHE D . n 
D 2 102 SER 102 120 120 SER SER D . n 
D 2 103 PHE 103 121 121 PHE PHE D . n 
D 2 104 LYS 104 122 122 LYS LYS D . n 
D 2 105 GLY 105 123 123 GLY GLY D . n 
D 2 106 ILE 106 124 124 ILE ILE D . n 
D 2 107 LYS 107 125 125 LYS LYS D . n 
D 2 108 PHE 108 126 126 PHE PHE D . n 
D 2 109 SER 109 127 127 SER SER D . n 
D 2 110 LYS 110 128 128 LYS LYS D . n 
D 2 111 GLY 111 129 129 GLY GLY D . n 
D 2 112 LYS 112 130 130 LYS LYS D . n 
D 2 113 TYR 113 131 131 TYR TYR D . n 
D 2 114 LYS 114 132 132 LYS LYS D . n 
D 2 115 CYS 115 133 133 CYS CYS D . n 
D 2 116 VAL 116 134 134 VAL VAL D . n 
D 2 117 VAL 117 135 135 VAL VAL D . n 
D 2 118 GLU 118 136 136 GLU GLU D . n 
D 2 119 ALA 119 137 137 ALA ALA D . n 
D 2 120 ILE 120 138 138 ILE ILE D . n 
D 2 121 SER 121 139 139 SER SER D . n 
D 2 122 GLY 122 140 140 GLY GLY D . n 
D 2 123 SER 123 141 141 SER SER D . n 
D 2 124 PRO 124 142 142 PRO PRO D . n 
D 2 125 GLU 125 143 143 GLU GLU D . n 
D 2 126 GLU 126 144 144 GLU GLU D . n 
D 2 127 MET 127 145 145 MET MET D . n 
D 2 128 LEU 128 146 146 LEU LEU D . n 
D 2 129 PHE 129 147 147 PHE PHE D . n 
D 2 130 CYS 130 148 148 CYS CYS D . n 
D 2 131 LEU 131 149 149 LEU LEU D . n 
D 2 132 GLU 132 150 150 GLU GLU D . n 
D 2 133 PHE 133 151 151 PHE PHE D . n 
D 2 134 VAL 134 152 152 VAL VAL D . n 
D 2 135 ILE 135 153 153 ILE ILE D . n 
D 2 136 LEU 136 154 154 LEU LEU D . n 
D 2 137 HIS 137 155 155 HIS HIS D . n 
D 2 138 GLN 138 156 156 GLN GLN D . n 
D 2 139 PRO 139 157 157 PRO PRO D . n 
D 2 140 ASN 140 158 158 ASN ASN D . n 
D 2 141 SER 141 159 ?   ?   ?   D . n 
D 2 142 ASN 142 160 ?   ?   ?   D . 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 
K  6  FTT 1 1003 1003 FTT FTT A . 
L  6  FTT 1 1004 1004 FTT FTT A . 
M  6  FTT 1 1005 1005 FTT FTT A . 
N  6  FTT 1 1006 1006 FTT FTT A . 
O  7  DAO 1 1007 1007 DAO DAO A . 
P  8  MYR 1 1008 1008 MYR MYR A . 
Q  9  PO4 1 1010 1010 PO4 PO4 A . 
R  9  PO4 1 1011 1011 PO4 PO4 A . 
S  9  PO4 1 1017 1017 PO4 PO4 A . 
T  9  PO4 1 1018 1018 PO4 PO4 A . 
U  10 NAG 1 711  711  NAG NAG A . 
V  10 NAG 1 721  721  NAG NAG A . 
W  10 NAG 1 741  741  NAG NAG A . 
X  11 MG  1 2001 2001 MG  MG  A . 
Y  6  FTT 1 1003 1003 FTT FTT B . 
Z  6  FTT 1 1004 1004 FTT FTT B . 
AA 6  FTT 1 1005 1005 FTT FTT B . 
BA 6  FTT 1 1006 1006 FTT FTT B . 
CA 7  DAO 1 1007 1007 DAO DAO B . 
DA 8  MYR 1 1008 1008 MYR MYR B . 
EA 9  PO4 1 1010 1010 PO4 PO4 B . 
FA 9  PO4 1 1011 1011 PO4 PO4 B . 
GA 9  PO4 1 1017 1017 PO4 PO4 B . 
HA 9  PO4 1 1018 1018 PO4 PO4 B . 
IA 10 NAG 1 811  811  NAG NAG B . 
JA 10 NAG 1 821  821  NAG NAG B . 
KA 10 NAG 1 841  841  NAG NAG B . 
LA 11 MG  1 2001 2001 MG  MG  B . 
MA 10 NAG 1 751  751  NAG NAG C . 
NA 10 NAG 1 851  851  NAG NAG D . 
OA 12 HOH 1 1    1    HOH HOH A . 
PA 12 HOH 1 2    2    HOH HOH B . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1  A ASN 147 A ASN 173 ? ASN 'GLYCOSYLATION SITE' 
2  A ASN 179 A ASN 205 ? ASN 'GLYCOSYLATION SITE' 
3  A ASN 471 A ASN 497 ? ASN 'GLYCOSYLATION SITE' 
4  A ASN 500 A ASN 526 ? ASN 'GLYCOSYLATION SITE' 
5  A ASN 549 A ASN 575 ? ASN 'GLYCOSYLATION SITE' 
6  B ASN 147 B ASN 173 ? ASN 'GLYCOSYLATION SITE' 
7  B ASN 179 B ASN 205 ? ASN 'GLYCOSYLATION SITE' 
8  B ASN 471 B ASN 497 ? ASN 'GLYCOSYLATION SITE' 
9  B ASN 500 B ASN 526 ? ASN 'GLYCOSYLATION SITE' 
10 B ASN 549 B ASN 575 ? ASN 'GLYCOSYLATION SITE' 
11 C ASN 96  C ASN 114 ? ASN 'GLYCOSYLATION SITE' 
12 D ASN 96  D ASN 114 ? ASN 'GLYCOSYLATION SITE' 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      
A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,JA,KA,LA,MA,NA,OA,PA 
# 
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)' 27360 ? 
1 MORE         142   ? 
1 'SSA (A^2)'  61520 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
_pdbx_struct_conn_angle.id                    1 
_pdbx_struct_conn_angle.ptnr1_label_atom_id   O 
_pdbx_struct_conn_angle.ptnr1_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr1_label_asym_id   OA 
_pdbx_struct_conn_angle.ptnr1_label_comp_id   HOH 
_pdbx_struct_conn_angle.ptnr1_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id    HOH 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id     1 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr1_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr2_label_atom_id   MG 
_pdbx_struct_conn_angle.ptnr2_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr2_label_asym_id   X 
_pdbx_struct_conn_angle.ptnr2_label_comp_id   MG 
_pdbx_struct_conn_angle.ptnr2_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id    MG 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id     2001 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr2_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr3_label_atom_id   OD2 
_pdbx_struct_conn_angle.ptnr3_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr3_label_asym_id   A 
_pdbx_struct_conn_angle.ptnr3_label_comp_id   ASP 
_pdbx_struct_conn_angle.ptnr3_label_seq_id    268 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id    ASP 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id     294 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr3_symmetry        1_555 
_pdbx_struct_conn_angle.value                 61.5 
_pdbx_struct_conn_angle.value_esd             ? 
# 
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 2009-03-03 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2012-06-20 
4 'Structure model' 1 3 2020-07-01 
5 'Structure model' 2 0 2020-07-29 
6 'Structure model' 2 1 2023-11-01 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ?                          ? 
2 5 'Structure model' repository Remediation       'Carbohydrate remediation' ? 
# 
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' 'Non-polymer description'   
2  2 'Structure model' 'Version format compliance' 
3  3 'Structure model' 'Non-polymer description'   
4  4 'Structure model' Advisory                    
5  4 'Structure model' 'Data collection'           
6  4 'Structure model' 'Derived calculations'      
7  5 'Structure model' Advisory                    
8  5 'Structure model' 'Atomic model'              
9  5 'Structure model' 'Data collection'           
10 5 'Structure model' 'Derived calculations'      
11 5 'Structure model' 'Structure summary'         
12 6 'Structure model' 'Data collection'           
13 6 'Structure model' 'Database references'       
14 6 'Structure model' 'Refinement description'    
15 6 'Structure model' 'Structure summary'         
# 
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  4 'Structure model' chem_comp                     
2  4 'Structure model' database_PDB_caveat           
3  4 'Structure model' pdbx_unobs_or_zero_occ_atoms  
4  4 'Structure model' pdbx_validate_close_contact   
5  4 'Structure model' struct_conn                   
6  5 'Structure model' atom_site                     
7  5 'Structure model' chem_comp                     
8  5 'Structure model' database_PDB_caveat           
9  5 'Structure model' entity                        
10 5 'Structure model' pdbx_branch_scheme            
11 5 'Structure model' pdbx_chem_comp_identifier     
12 5 'Structure model' pdbx_entity_branch            
13 5 'Structure model' pdbx_entity_branch_descriptor 
14 5 'Structure model' pdbx_entity_branch_link       
15 5 'Structure model' pdbx_entity_branch_list       
16 5 'Structure model' pdbx_entity_nonpoly           
17 5 'Structure model' pdbx_nonpoly_scheme           
18 5 'Structure model' pdbx_struct_assembly_gen      
19 5 'Structure model' pdbx_struct_conn_angle        
20 5 'Structure model' pdbx_unobs_or_zero_occ_atoms  
21 5 'Structure model' pdbx_validate_chiral          
22 5 'Structure model' pdbx_validate_close_contact   
23 5 'Structure model' struct_asym                   
24 5 'Structure model' struct_conn                   
25 5 'Structure model' struct_site                   
26 5 'Structure model' struct_site_gen               
27 6 'Structure model' chem_comp                     
28 6 'Structure model' chem_comp_atom                
29 6 'Structure model' chem_comp_bond                
30 6 'Structure model' database_2                    
31 6 'Structure model' pdbx_initial_refinement_model 
# 
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' '_chem_comp.type'                             
2  5 'Structure model' '_atom_site.B_iso_or_equiv'                   
3  5 'Structure model' '_atom_site.Cartn_x'                          
4  5 'Structure model' '_atom_site.Cartn_y'                          
5  5 'Structure model' '_atom_site.Cartn_z'                          
6  5 'Structure model' '_atom_site.auth_asym_id'                     
7  5 'Structure model' '_atom_site.auth_atom_id'                     
8  5 'Structure model' '_atom_site.auth_comp_id'                     
9  5 'Structure model' '_atom_site.auth_seq_id'                      
10 5 'Structure model' '_atom_site.label_asym_id'                    
11 5 'Structure model' '_atom_site.label_atom_id'                    
12 5 'Structure model' '_atom_site.label_comp_id'                    
13 5 'Structure model' '_atom_site.label_entity_id'                  
14 5 'Structure model' '_atom_site.type_symbol'                      
15 5 'Structure model' '_chem_comp.name'                             
16 5 'Structure model' '_chem_comp.type'                             
17 5 'Structure model' '_database_PDB_caveat.text'                   
18 5 'Structure model' '_pdbx_struct_assembly_gen.asym_id_list'      
19 5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
20 5 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_asym_id' 
21 5 'Structure model' '_pdbx_unobs_or_zero_occ_atoms.label_asym_id' 
22 5 'Structure model' '_pdbx_validate_chiral.auth_asym_id'          
23 5 'Structure model' '_pdbx_validate_chiral.auth_seq_id'           
24 5 'Structure model' '_pdbx_validate_close_contact.auth_asym_id_1' 
25 5 'Structure model' '_pdbx_validate_close_contact.auth_asym_id_2' 
26 5 'Structure model' '_pdbx_validate_close_contact.auth_seq_id_1'  
27 5 'Structure model' '_pdbx_validate_close_contact.auth_seq_id_2'  
28 5 'Structure model' '_struct_conn.pdbx_dist_value'                
29 5 'Structure model' '_struct_conn.pdbx_leaving_atom_flag'         
30 5 'Structure model' '_struct_conn.pdbx_role'                      
31 5 'Structure model' '_struct_conn.ptnr1_auth_asym_id'             
32 5 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
33 5 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
34 5 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
35 5 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
36 5 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
37 5 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
38 5 'Structure model' '_struct_conn.ptnr2_auth_asym_id'             
39 5 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
40 5 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
41 5 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
42 5 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
43 5 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
44 6 'Structure model' '_chem_comp.pdbx_synonyms'                    
45 6 'Structure model' '_database_2.pdbx_DOI'                        
46 6 'Structure model' '_database_2.pdbx_database_accession'         
# 
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 
CNS         .     ?               package 'Axel T. Brunger' axel.brunger@yale.edu refinement        http://cns-online.org/ 
Fortran_77 ? 1 
PDB_EXTRACT 3.006 'June 11, 2008' package PDB               help@deposit.rcsb.org 'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/ C++        ? 2 
DNA         .     ?               ?       ?                 ?                     'data collection' ? ?          ? 3 
XDS         .     ?               ?       ?                 ?                     'data reduction'  ? ?          ? 4 
XDS         .     ?               ?       ?                 ?                     'data scaling'    ? ?          ? 5 
PHASER      .     ?               ?       ?                 ?                     phasing           ? ?          ? 6 
# 
_pdbx_entry_details.entry_id                 3FXI 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.nonpolymer_details       
;RESIDUES FROM 1001 TO 1018 IN THE CHAINS A AND B ARE E.COLI 
LIPOPOLYSACCHARIDES
;
_pdbx_entry_details.sequence_details         ? 
_pdbx_entry_details.has_ligand_of_interest   ? 
# 
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 N2  H GCS 2   ? ? C1 B FTT 1005 ? ? 1.34 
2  1 N2  H PA1 1   ? ? C1 B FTT 1003 ? ? 1.35 
3  1 N2  E PA1 1   ? ? C1 A FTT 1003 ? ? 1.35 
4  1 N2  E PA1 2   ? ? C1 A FTT 1005 ? ? 1.35 
5  1 O3  E PA1 2   ? ? C1 A FTT 1006 ? ? 1.41 
6  1 O3  H GCS 2   ? ? C1 B FTT 1006 ? ? 1.41 
7  1 O3  H PA1 1   ? ? C1 B FTT 1004 ? ? 1.42 
8  1 O3  E PA1 1   ? ? C1 A FTT 1004 ? ? 1.42 
9  1 O4  E PA1 2   ? ? P  A PO4 1010 ? ? 1.47 
10 1 O4  H GCS 2   ? ? P  B PO4 1010 ? ? 1.48 
11 1 O1  H PA1 1   ? ? P  B PO4 1011 ? ? 1.50 
12 1 O1  E PA1 1   ? ? P  A PO4 1011 ? ? 1.50 
13 1 O6  H GCS 2   ? ? O6 H KDO 3    ? ? 2.14 
14 1 O6  E PA1 2   ? ? O6 E KDO 3    ? ? 2.14 
15 1 O4  H KDO 3   ? ? C3 H KDO 7    ? ? 2.15 
16 1 O4  E KDO 3   ? ? C3 E KDO 7    ? ? 2.15 
17 1 ND2 B ASN 497 ? ? O5 B NAG 841  ? ? 2.19 
# 
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 ARG 67 ? ? CA A ARG 67 ? ? C  A ARG 67 ? ? 96.57  110.40 -13.83 2.00 N 
2 1 N  A HIS 68 ? ? CA A HIS 68 ? ? CB A HIS 68 ? ? 121.61 110.60 11.01  1.80 N 
3 1 CB B ARG 67 ? ? CA B ARG 67 ? ? C  B ARG 67 ? ? 96.54  110.40 -13.86 2.00 N 
4 1 N  B HIS 68 ? ? CA B HIS 68 ? ? CB B HIS 68 ? ? 121.84 110.60 11.24  1.80 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1   1 ASN A 35  ? ? 57.61   4.33    
2   1 ILE A 36  ? ? -130.25 -53.10  
3   1 CYS A 40  ? ? -98.71  58.16   
4   1 ASP A 50  ? ? -141.11 -18.88  
5   1 ASN A 51  ? ? -74.48  24.33   
6   1 PRO A 53  ? ? -47.10  159.39  
7   1 ARG A 67  ? ? 64.42   -7.37   
8   1 PHE A 75  ? ? -146.66 -25.33  
9   1 GLU A 89  ? ? 52.29   17.24   
10  1 LEU A 101 ? ? -112.58 69.77   
11  1 ASN A 137 ? ? 59.33   10.82   
12  1 LYS A 166 ? ? -59.90  103.15  
13  1 TYR A 170 ? ? -59.52  -9.15   
14  1 ASN A 185 ? ? -126.33 -156.45 
15  1 PRO A 202 ? ? -49.01  -77.13  
16  1 LEU A 204 ? ? -177.66 81.24   
17  1 PRO A 214 ? ? -69.43  64.29   
18  1 ASN A 216 ? ? -157.87 4.52    
19  1 PHE A 272 ? ? -150.51 71.40   
20  1 LYS A 274 ? ? -52.08  -0.31   
21  1 TYR A 292 ? ? 76.91   116.49  
22  1 ASP A 298 ? ? -99.69  -65.56  
23  1 ARG A 322 ? ? -64.46  14.11   
24  1 ASN A 365 ? ? -147.01 20.25   
25  1 LEU A 372 ? ? -115.47 76.97   
26  1 GLN A 430 ? ? -38.85  129.44  
27  1 SER A 438 ? ? -100.36 53.65   
28  1 PHE A 440 ? ? 172.88  -177.51 
29  1 ALA A 462 ? ? -154.62 34.95   
30  1 ASN A 464 ? ? -69.78  13.08   
31  1 ASN A 481 ? ? -93.38  -134.59 
32  1 ASN A 497 ? ? -61.63  2.07    
33  1 LEU A 498 ? ? -49.97  109.98  
34  1 LEU A 501 ? ? -163.72 97.81   
35  1 LEU A 503 ? ? -148.19 28.54   
36  1 GLN A 505 ? ? 46.10   18.97   
37  1 GLN A 507 ? ? 48.11   24.26   
38  1 GLU A 509 ? ? -123.56 -62.29  
39  1 ALA A 515 ? ? -40.75  -87.93  
40  1 ASN A 517 ? ? -45.62  -9.32   
41  1 LEU A 525 ? ? -164.07 95.54   
42  1 MET A 527 ? ? -143.78 23.60   
43  1 HIS A 529 ? ? 19.96   48.42   
44  1 ASN A 530 ? ? -102.15 -155.28 
45  1 THR A 537 ? ? -153.74 -5.77   
46  1 LEU A 549 ? ? -158.09 84.97   
47  1 TYR A 551 ? ? -148.99 14.96   
48  1 SER A 552 ? ? -63.72  -179.11 
49  1 LEU A 553 ? ? 38.50   28.72   
50  1 ASN A 554 ? ? -95.44  -153.67 
51  1 MET A 557 ? ? -172.37 -34.70  
52  1 THR A 558 ? ? -89.48  -158.97 
53  1 SER A 559 ? ? 178.66  85.47   
54  1 LYS A 560 ? ? -65.34  16.72   
55  1 LYS A 561 ? ? -174.44 107.52  
56  1 GLN A 562 ? ? -72.40  39.89   
57  1 GLU A 563 ? ? -98.90  38.99   
58  1 LEU A 564 ? ? -61.29  12.30   
59  1 HIS A 566 ? ? -69.64  57.51   
60  1 PRO A 568 ? ? -30.13  143.89  
61  1 LEU A 571 ? ? -45.59  105.45  
62  1 ALA A 572 ? ? -91.65  -68.03  
63  1 LEU A 574 ? ? -159.38 80.47   
64  1 LEU A 576 ? ? -153.32 12.74   
65  1 GLN A 578 ? ? 52.22   102.31  
66  1 CYS A 583 ? ? -95.26  57.56   
67  1 CYS A 585 ? ? -49.69  -19.58  
68  1 LEU A 601 ? ? -58.26  -171.36 
69  1 VAL A 602 ? ? -138.10 -144.46 
70  1 GLU A 603 ? ? -41.45  96.70   
71  1 GLU A 608 ? ? -48.57  150.05  
72  1 ALA A 610 ? ? -146.90 -35.18  
73  1 SER A 622 ? ? -159.87 70.45   
74  1 PRO B 28  ? ? -63.14  0.18    
75  1 ASN B 35  ? ? 58.01   4.49    
76  1 ILE B 36  ? ? -129.59 -53.59  
77  1 CYS B 40  ? ? -99.79  58.24   
78  1 ASP B 50  ? ? -141.50 -18.88  
79  1 ASN B 51  ? ? -74.13  22.86   
80  1 PRO B 53  ? ? -47.18  159.46  
81  1 ARG B 67  ? ? 65.67   -8.41   
82  1 PHE B 75  ? ? -147.03 -24.83  
83  1 GLU B 89  ? ? 52.76   16.17   
84  1 LEU B 101 ? ? -112.95 69.80   
85  1 LYS B 166 ? ? -59.20  103.36  
86  1 TYR B 170 ? ? -59.18  -9.37   
87  1 ASN B 185 ? ? -126.93 -157.61 
88  1 PRO B 202 ? ? -48.20  -77.54  
89  1 LEU B 204 ? ? -177.51 81.56   
90  1 PRO B 214 ? ? -68.64  64.38   
91  1 ASN B 216 ? ? -158.90 2.93    
92  1 LYS B 274 ? ? -52.54  -0.34   
93  1 TYR B 292 ? ? 77.40   116.01  
94  1 ASP B 298 ? ? -100.82 -64.74  
95  1 ARG B 322 ? ? -63.23  13.42   
96  1 ASN B 365 ? ? -145.87 19.99   
97  1 LEU B 372 ? ? -114.45 77.54   
98  1 GLN B 430 ? ? -36.96  130.61  
99  1 SER B 438 ? ? -99.69  52.37   
100 1 PHE B 440 ? ? 172.59  -177.26 
101 1 ALA B 462 ? ? -153.74 34.31   
102 1 ASN B 481 ? ? -94.04  -135.00 
103 1 PRO B 489 ? ? -69.91  -178.89 
104 1 THR B 493 ? ? -56.63  -9.37   
105 1 ASN B 497 ? ? -62.06  2.12    
106 1 LEU B 498 ? ? -50.07  109.80  
107 1 LEU B 501 ? ? -162.19 100.13  
108 1 LEU B 503 ? ? -146.37 27.10   
109 1 GLN B 505 ? ? 45.98   19.67   
110 1 GLN B 507 ? ? 51.04   16.66   
111 1 GLU B 509 ? ? -123.77 -61.48  
112 1 ALA B 515 ? ? -40.61  -87.00  
113 1 ASN B 517 ? ? -45.48  -10.04  
114 1 LEU B 525 ? ? -163.17 96.99   
115 1 MET B 527 ? ? -143.58 22.59   
116 1 SER B 528 ? ? -58.68  179.72  
117 1 HIS B 529 ? ? 19.01   48.08   
118 1 ASN B 530 ? ? -102.17 -156.13 
119 1 ASP B 536 ? ? -117.84 -169.94 
120 1 THR B 537 ? ? -154.13 -5.71   
121 1 LEU B 549 ? ? -158.54 84.84   
122 1 TYR B 551 ? ? -149.69 14.85   
123 1 SER B 552 ? ? -62.62  -179.16 
124 1 LEU B 553 ? ? 37.82   29.43   
125 1 ASN B 554 ? ? -95.75  -153.95 
126 1 MET B 557 ? ? -171.68 -34.08  
127 1 THR B 558 ? ? -89.27  -158.09 
128 1 SER B 559 ? ? 177.66  85.00   
129 1 LYS B 560 ? ? -65.42  16.83   
130 1 LYS B 561 ? ? -174.16 107.49  
131 1 GLN B 562 ? ? -72.18  39.89   
132 1 GLU B 563 ? ? -99.35  39.44   
133 1 LEU B 564 ? ? -61.97  12.46   
134 1 HIS B 566 ? ? -69.39  56.46   
135 1 PRO B 568 ? ? -29.01  144.23  
136 1 LEU B 571 ? ? -46.44  105.29  
137 1 ALA B 572 ? ? -90.77  -68.88  
138 1 LEU B 574 ? ? -160.16 79.61   
139 1 LEU B 576 ? ? -153.98 11.77   
140 1 GLN B 578 ? ? 51.05   102.76  
141 1 CYS B 583 ? ? -95.38  58.51   
142 1 CYS B 585 ? ? -49.72  -19.89  
143 1 LEU B 601 ? ? -57.69  -170.84 
144 1 VAL B 602 ? ? -138.77 -145.00 
145 1 GLU B 603 ? ? -41.20  97.25   
146 1 GLU B 608 ? ? -47.95  150.53  
147 1 ALA B 610 ? ? -146.70 -34.87  
148 1 SER B 622 ? ? -160.35 70.20   
149 1 VAL C 24  ? ? -77.37  -71.12  
150 1 SER C 27  ? ? -116.69 -128.75 
151 1 GLN C 41  ? ? -112.27 56.10   
152 1 TYR C 75  ? ? -177.42 142.42  
153 1 ASN C 83  ? ? 34.43   66.38   
154 1 THR C 84  ? ? 79.84   -20.57  
155 1 CYS C 95  ? ? 74.80   105.02  
156 1 SER C 120 ? ? -171.88 147.51  
157 1 GLU C 143 ? ? 49.06   114.07  
158 1 PRO C 157 ? ? -62.69  -163.83 
159 1 VAL D 24  ? ? -78.00  -70.61  
160 1 SER D 27  ? ? -117.04 -127.03 
161 1 LYS D 39  ? ? -57.40  -71.17  
162 1 GLN D 41  ? ? -112.97 56.84   
163 1 TYR D 75  ? ? -176.73 141.98  
164 1 ASN D 83  ? ? 34.87   67.62   
165 1 THR D 84  ? ? 78.37   -20.29  
166 1 CYS D 95  ? ? 75.11   102.05  
167 1 SER D 120 ? ? -173.12 148.42  
168 1 GLU D 143 ? ? 49.84   113.83  
169 1 PRO D 157 ? ? -62.04  -163.64 
# 
_pdbx_validate_chiral.id              1 
_pdbx_validate_chiral.PDB_model_num   1 
_pdbx_validate_chiral.auth_atom_id    C1 
_pdbx_validate_chiral.label_alt_id    ? 
_pdbx_validate_chiral.auth_asym_id    E 
_pdbx_validate_chiral.auth_comp_id    PA1 
_pdbx_validate_chiral.auth_seq_id     2 
_pdbx_validate_chiral.PDB_ins_code    ? 
_pdbx_validate_chiral.details         'WRONG HAND' 
_pdbx_validate_chiral.omega           . 
# 
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 N 1 A FTT 1003 ? O1 ? K  FTT 1 O1 
2  1 N 1 A FTT 1004 ? O1 ? L  FTT 1 O1 
3  1 N 1 A FTT 1005 ? O1 ? M  FTT 1 O1 
4  1 N 1 A FTT 1006 ? O1 ? N  FTT 1 O1 
5  1 N 1 A PO4 1010 ? O1 ? Q  PO4 1 O1 
6  1 N 1 A PO4 1011 ? O1 ? R  PO4 1 O1 
7  1 N 1 B FTT 1003 ? O1 ? Y  FTT 1 O1 
8  1 N 1 B FTT 1004 ? O1 ? Z  FTT 1 O1 
9  1 N 1 B FTT 1005 ? O1 ? AA FTT 1 O1 
10 1 N 1 B FTT 1006 ? O1 ? BA FTT 1 O1 
11 1 N 1 B PO4 1010 ? O1 ? EA PO4 1 O1 
12 1 N 1 B PO4 1011 ? O1 ? FA PO4 1 O1 
# 
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 628 ? A GLN 602 
2  1 Y 1 A MET 629 ? A MET 603 
3  1 Y 1 A ASN 630 ? A ASN 604 
4  1 Y 1 A LYS 631 ? A LYS 605 
5  1 Y 1 B GLN 628 ? B GLN 602 
6  1 Y 1 B MET 629 ? B MET 603 
7  1 Y 1 B ASN 630 ? B ASN 604 
8  1 Y 1 B LYS 631 ? B LYS 605 
9  1 Y 1 C SER 159 ? C SER 141 
10 1 Y 1 C ASN 160 ? C ASN 142 
11 1 Y 1 D SER 159 ? D SER 141 
12 1 Y 1 D ASN 160 ? D ASN 142 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
DAO O1   O  N N 88  
DAO O2   O  N N 89  
DAO C1   C  N N 90  
DAO C2   C  N N 91  
DAO C3   C  N N 92  
DAO C4   C  N N 93  
DAO C5   C  N N 94  
DAO C6   C  N N 95  
DAO C7   C  N N 96  
DAO C8   C  N N 97  
DAO C9   C  N N 98  
DAO C10  C  N N 99  
DAO C11  C  N N 100 
DAO C12  C  N N 101 
DAO HO2  H  N N 102 
DAO H21  H  N N 103 
DAO H22  H  N N 104 
DAO H31  H  N N 105 
DAO H32  H  N N 106 
DAO H41  H  N N 107 
DAO H42  H  N N 108 
DAO H51  H  N N 109 
DAO H52  H  N N 110 
DAO H61  H  N N 111 
DAO H62  H  N N 112 
DAO H71  H  N N 113 
DAO H72  H  N N 114 
DAO H81  H  N N 115 
DAO H82  H  N N 116 
DAO H91  H  N N 117 
DAO H92  H  N N 118 
DAO H101 H  N N 119 
DAO H102 H  N N 120 
DAO H111 H  N N 121 
DAO H112 H  N N 122 
DAO H121 H  N N 123 
DAO H122 H  N N 124 
DAO H123 H  N N 125 
FTT C1   C  N N 126 
FTT C2   C  N N 127 
FTT C3   C  N R 128 
FTT C4   C  N N 129 
FTT C5   C  N N 130 
FTT C6   C  N N 131 
FTT C7   C  N N 132 
FTT C8   C  N N 133 
FTT C9   C  N N 134 
FTT C10  C  N N 135 
FTT C11  C  N N 136 
FTT C12  C  N N 137 
FTT C13  C  N N 138 
FTT C14  C  N N 139 
FTT O2   O  N N 140 
FTT O3   O  N N 141 
FTT O1   O  N N 142 
FTT H21  H  N N 143 
FTT H22  H  N N 144 
FTT H3   H  N N 145 
FTT H41  H  N N 146 
FTT H42  H  N N 147 
FTT H51  H  N N 148 
FTT H52  H  N N 149 
FTT H61  H  N N 150 
FTT H62  H  N N 151 
FTT H71  H  N N 152 
FTT H72  H  N N 153 
FTT H81  H  N N 154 
FTT H82  H  N N 155 
FTT H91  H  N N 156 
FTT H92  H  N N 157 
FTT H101 H  N N 158 
FTT H102 H  N N 159 
FTT H111 H  N N 160 
FTT H112 H  N N 161 
FTT H121 H  N N 162 
FTT H122 H  N N 163 
FTT H131 H  N N 164 
FTT H132 H  N N 165 
FTT H141 H  N N 166 
FTT H142 H  N N 167 
FTT H143 H  N N 168 
FTT HO3  H  N N 169 
FTT HO1  H  N N 170 
GCS C1   C  N R 171 
GCS C2   C  N R 172 
GCS C3   C  N R 173 
GCS C4   C  N S 174 
GCS C5   C  N R 175 
GCS C6   C  N N 176 
GCS N2   N  N N 177 
GCS O1   O  N N 178 
GCS O3   O  N N 179 
GCS O4   O  N N 180 
GCS O5   O  N N 181 
GCS O6   O  N N 182 
GCS H1   H  N N 183 
GCS H2   H  N N 184 
GCS H3   H  N N 185 
GCS H4   H  N N 186 
GCS H5   H  N N 187 
GCS H61  H  N N 188 
GCS H62  H  N N 189 
GCS HN21 H  N N 190 
GCS HN22 H  N N 191 
GCS HO1  H  N N 192 
GCS HO3  H  N N 193 
GCS HO4  H  N N 194 
GCS HO6  H  N N 195 
GLN N    N  N N 196 
GLN CA   C  N S 197 
GLN C    C  N N 198 
GLN O    O  N N 199 
GLN CB   C  N N 200 
GLN CG   C  N N 201 
GLN CD   C  N N 202 
GLN OE1  O  N N 203 
GLN NE2  N  N N 204 
GLN OXT  O  N N 205 
GLN H    H  N N 206 
GLN H2   H  N N 207 
GLN HA   H  N N 208 
GLN HB2  H  N N 209 
GLN HB3  H  N N 210 
GLN HG2  H  N N 211 
GLN HG3  H  N N 212 
GLN HE21 H  N N 213 
GLN HE22 H  N N 214 
GLN HXT  H  N N 215 
GLU N    N  N N 216 
GLU CA   C  N S 217 
GLU C    C  N N 218 
GLU O    O  N N 219 
GLU CB   C  N N 220 
GLU CG   C  N N 221 
GLU CD   C  N N 222 
GLU OE1  O  N N 223 
GLU OE2  O  N N 224 
GLU OXT  O  N N 225 
GLU H    H  N N 226 
GLU H2   H  N N 227 
GLU HA   H  N N 228 
GLU HB2  H  N N 229 
GLU HB3  H  N N 230 
GLU HG2  H  N N 231 
GLU HG3  H  N N 232 
GLU HE2  H  N N 233 
GLU HXT  H  N N 234 
GLY N    N  N N 235 
GLY CA   C  N N 236 
GLY C    C  N N 237 
GLY O    O  N N 238 
GLY OXT  O  N N 239 
GLY H    H  N N 240 
GLY H2   H  N N 241 
GLY HA2  H  N N 242 
GLY HA3  H  N N 243 
GLY HXT  H  N N 244 
GMH C1   C  N S 245 
GMH C2   C  N S 246 
GMH C3   C  N S 247 
GMH C4   C  N S 248 
GMH C5   C  N R 249 
GMH C6   C  N S 250 
GMH C7   C  N N 251 
GMH O1   O  N N 252 
GMH O2   O  N N 253 
GMH O3   O  N N 254 
GMH O4   O  N N 255 
GMH O5   O  N N 256 
GMH O6   O  N N 257 
GMH O7   O  N N 258 
GMH H1   H  N N 259 
GMH H2   H  N N 260 
GMH H3   H  N N 261 
GMH H4   H  N N 262 
GMH H5   H  N N 263 
GMH H6   H  N N 264 
GMH H71  H  N N 265 
GMH H72  H  N N 266 
GMH HO1  H  N N 267 
GMH HO2  H  N N 268 
GMH HO3  H  N N 269 
GMH HO4  H  N N 270 
GMH HO6  H  N N 271 
GMH HO7  H  N N 272 
HIS N    N  N N 273 
HIS CA   C  N S 274 
HIS C    C  N N 275 
HIS O    O  N N 276 
HIS CB   C  N N 277 
HIS CG   C  Y N 278 
HIS ND1  N  Y N 279 
HIS CD2  C  Y N 280 
HIS CE1  C  Y N 281 
HIS NE2  N  Y N 282 
HIS OXT  O  N N 283 
HIS H    H  N N 284 
HIS H2   H  N N 285 
HIS HA   H  N N 286 
HIS HB2  H  N N 287 
HIS HB3  H  N N 288 
HIS HD1  H  N N 289 
HIS HD2  H  N N 290 
HIS HE1  H  N N 291 
HIS HE2  H  N N 292 
HIS HXT  H  N N 293 
HOH O    O  N N 294 
HOH H1   H  N N 295 
HOH H2   H  N N 296 
ILE N    N  N N 297 
ILE CA   C  N S 298 
ILE C    C  N N 299 
ILE O    O  N N 300 
ILE CB   C  N S 301 
ILE CG1  C  N N 302 
ILE CG2  C  N N 303 
ILE CD1  C  N N 304 
ILE OXT  O  N N 305 
ILE H    H  N N 306 
ILE H2   H  N N 307 
ILE HA   H  N N 308 
ILE HB   H  N N 309 
ILE HG12 H  N N 310 
ILE HG13 H  N N 311 
ILE HG21 H  N N 312 
ILE HG22 H  N N 313 
ILE HG23 H  N N 314 
ILE HD11 H  N N 315 
ILE HD12 H  N N 316 
ILE HD13 H  N N 317 
ILE HXT  H  N N 318 
KDO C1   C  N N 319 
KDO O1A  O  N N 320 
KDO O1B  O  N N 321 
KDO C2   C  N R 322 
KDO O2   O  N N 323 
KDO C3   C  N N 324 
KDO C4   C  N R 325 
KDO O4   O  N N 326 
KDO C5   C  N R 327 
KDO O5   O  N N 328 
KDO C6   C  N R 329 
KDO O6   O  N N 330 
KDO C7   C  N R 331 
KDO O7   O  N N 332 
KDO C8   C  N N 333 
KDO O8   O  N N 334 
KDO HO1B H  N N 335 
KDO HO2  H  N N 336 
KDO H31  H  N N 337 
KDO H32  H  N N 338 
KDO H4   H  N N 339 
KDO HO4  H  N N 340 
KDO H5   H  N N 341 
KDO HO5  H  N N 342 
KDO H6   H  N N 343 
KDO H7   H  N N 344 
KDO HO7  H  N N 345 
KDO H81  H  N N 346 
KDO H82  H  N N 347 
KDO HO8  H  N N 348 
LEU N    N  N N 349 
LEU CA   C  N S 350 
LEU C    C  N N 351 
LEU O    O  N N 352 
LEU CB   C  N N 353 
LEU CG   C  N N 354 
LEU CD1  C  N N 355 
LEU CD2  C  N N 356 
LEU OXT  O  N N 357 
LEU H    H  N N 358 
LEU H2   H  N N 359 
LEU HA   H  N N 360 
LEU HB2  H  N N 361 
LEU HB3  H  N N 362 
LEU HG   H  N N 363 
LEU HD11 H  N N 364 
LEU HD12 H  N N 365 
LEU HD13 H  N N 366 
LEU HD21 H  N N 367 
LEU HD22 H  N N 368 
LEU HD23 H  N N 369 
LEU HXT  H  N N 370 
LYS N    N  N N 371 
LYS CA   C  N S 372 
LYS C    C  N N 373 
LYS O    O  N N 374 
LYS CB   C  N N 375 
LYS CG   C  N N 376 
LYS CD   C  N N 377 
LYS CE   C  N N 378 
LYS NZ   N  N N 379 
LYS OXT  O  N N 380 
LYS H    H  N N 381 
LYS H2   H  N N 382 
LYS HA   H  N N 383 
LYS HB2  H  N N 384 
LYS HB3  H  N N 385 
LYS HG2  H  N N 386 
LYS HG3  H  N N 387 
LYS HD2  H  N N 388 
LYS HD3  H  N N 389 
LYS HE2  H  N N 390 
LYS HE3  H  N N 391 
LYS HZ1  H  N N 392 
LYS HZ2  H  N N 393 
LYS HZ3  H  N N 394 
LYS HXT  H  N N 395 
MET N    N  N N 396 
MET CA   C  N S 397 
MET C    C  N N 398 
MET O    O  N N 399 
MET CB   C  N N 400 
MET CG   C  N N 401 
MET SD   S  N N 402 
MET CE   C  N N 403 
MET OXT  O  N N 404 
MET H    H  N N 405 
MET H2   H  N N 406 
MET HA   H  N N 407 
MET HB2  H  N N 408 
MET HB3  H  N N 409 
MET HG2  H  N N 410 
MET HG3  H  N N 411 
MET HE1  H  N N 412 
MET HE2  H  N N 413 
MET HE3  H  N N 414 
MET HXT  H  N N 415 
MG  MG   MG N N 416 
MYR C1   C  N N 417 
MYR O1   O  N N 418 
MYR O2   O  N N 419 
MYR C2   C  N N 420 
MYR C3   C  N N 421 
MYR C4   C  N N 422 
MYR C5   C  N N 423 
MYR C6   C  N N 424 
MYR C7   C  N N 425 
MYR C8   C  N N 426 
MYR C9   C  N N 427 
MYR C10  C  N N 428 
MYR C11  C  N N 429 
MYR C12  C  N N 430 
MYR C13  C  N N 431 
MYR C14  C  N N 432 
MYR HO2  H  N N 433 
MYR H21  H  N N 434 
MYR H22  H  N N 435 
MYR H31  H  N N 436 
MYR H32  H  N N 437 
MYR H41  H  N N 438 
MYR H42  H  N N 439 
MYR H51  H  N N 440 
MYR H52  H  N N 441 
MYR H61  H  N N 442 
MYR H62  H  N N 443 
MYR H71  H  N N 444 
MYR H72  H  N N 445 
MYR H81  H  N N 446 
MYR H82  H  N N 447 
MYR H91  H  N N 448 
MYR H92  H  N N 449 
MYR H101 H  N N 450 
MYR H102 H  N N 451 
MYR H111 H  N N 452 
MYR H112 H  N N 453 
MYR H121 H  N N 454 
MYR H122 H  N N 455 
MYR H131 H  N N 456 
MYR H132 H  N N 457 
MYR H141 H  N N 458 
MYR H142 H  N N 459 
MYR H143 H  N N 460 
NAG C1   C  N R 461 
NAG C2   C  N R 462 
NAG C3   C  N R 463 
NAG C4   C  N S 464 
NAG C5   C  N R 465 
NAG C6   C  N N 466 
NAG C7   C  N N 467 
NAG C8   C  N N 468 
NAG N2   N  N N 469 
NAG O1   O  N N 470 
NAG O3   O  N N 471 
NAG O4   O  N N 472 
NAG O5   O  N N 473 
NAG O6   O  N N 474 
NAG O7   O  N N 475 
NAG H1   H  N N 476 
NAG H2   H  N N 477 
NAG H3   H  N N 478 
NAG H4   H  N N 479 
NAG H5   H  N N 480 
NAG H61  H  N N 481 
NAG H62  H  N N 482 
NAG H81  H  N N 483 
NAG H82  H  N N 484 
NAG H83  H  N N 485 
NAG HN2  H  N N 486 
NAG HO1  H  N N 487 
NAG HO3  H  N N 488 
NAG HO4  H  N N 489 
NAG HO6  H  N N 490 
PA1 C1   C  N S 491 
PA1 O1   O  N N 492 
PA1 C2   C  N R 493 
PA1 N2   N  N N 494 
PA1 C3   C  N R 495 
PA1 O3   O  N N 496 
PA1 C4   C  N S 497 
PA1 O4   O  N N 498 
PA1 C5   C  N R 499 
PA1 O5   O  N N 500 
PA1 C6   C  N N 501 
PA1 O6   O  N N 502 
PA1 H1   H  N N 503 
PA1 HO1  H  N N 504 
PA1 H2   H  N N 505 
PA1 HN21 H  N N 506 
PA1 HN22 H  N N 507 
PA1 H3   H  N N 508 
PA1 HO3  H  N N 509 
PA1 H4   H  N N 510 
PA1 HO4  H  N N 511 
PA1 H5   H  N N 512 
PA1 H61  H  N N 513 
PA1 H62  H  N N 514 
PA1 HO6  H  N N 515 
PHE N    N  N N 516 
PHE CA   C  N S 517 
PHE C    C  N N 518 
PHE O    O  N N 519 
PHE CB   C  N N 520 
PHE CG   C  Y N 521 
PHE CD1  C  Y N 522 
PHE CD2  C  Y N 523 
PHE CE1  C  Y N 524 
PHE CE2  C  Y N 525 
PHE CZ   C  Y N 526 
PHE OXT  O  N N 527 
PHE H    H  N N 528 
PHE H2   H  N N 529 
PHE HA   H  N N 530 
PHE HB2  H  N N 531 
PHE HB3  H  N N 532 
PHE HD1  H  N N 533 
PHE HD2  H  N N 534 
PHE HE1  H  N N 535 
PHE HE2  H  N N 536 
PHE HZ   H  N N 537 
PHE HXT  H  N N 538 
PO4 P    P  N N 539 
PO4 O1   O  N N 540 
PO4 O2   O  N N 541 
PO4 O3   O  N N 542 
PO4 O4   O  N N 543 
PRO N    N  N N 544 
PRO CA   C  N S 545 
PRO C    C  N N 546 
PRO O    O  N N 547 
PRO CB   C  N N 548 
PRO CG   C  N N 549 
PRO CD   C  N N 550 
PRO OXT  O  N N 551 
PRO H    H  N N 552 
PRO HA   H  N N 553 
PRO HB2  H  N N 554 
PRO HB3  H  N N 555 
PRO HG2  H  N N 556 
PRO HG3  H  N N 557 
PRO HD2  H  N N 558 
PRO HD3  H  N N 559 
PRO HXT  H  N N 560 
SER N    N  N N 561 
SER CA   C  N S 562 
SER C    C  N N 563 
SER O    O  N N 564 
SER CB   C  N N 565 
SER OG   O  N N 566 
SER OXT  O  N N 567 
SER H    H  N N 568 
SER H2   H  N N 569 
SER HA   H  N N 570 
SER HB2  H  N N 571 
SER HB3  H  N N 572 
SER HG   H  N N 573 
SER HXT  H  N N 574 
THR N    N  N N 575 
THR CA   C  N S 576 
THR C    C  N N 577 
THR O    O  N N 578 
THR CB   C  N R 579 
THR OG1  O  N N 580 
THR CG2  C  N N 581 
THR OXT  O  N N 582 
THR H    H  N N 583 
THR H2   H  N N 584 
THR HA   H  N N 585 
THR HB   H  N N 586 
THR HG1  H  N N 587 
THR HG21 H  N N 588 
THR HG22 H  N N 589 
THR HG23 H  N N 590 
THR HXT  H  N N 591 
TRP N    N  N N 592 
TRP CA   C  N S 593 
TRP C    C  N N 594 
TRP O    O  N N 595 
TRP CB   C  N N 596 
TRP CG   C  Y N 597 
TRP CD1  C  Y N 598 
TRP CD2  C  Y N 599 
TRP NE1  N  Y N 600 
TRP CE2  C  Y N 601 
TRP CE3  C  Y N 602 
TRP CZ2  C  Y N 603 
TRP CZ3  C  Y N 604 
TRP CH2  C  Y N 605 
TRP OXT  O  N N 606 
TRP H    H  N N 607 
TRP H2   H  N N 608 
TRP HA   H  N N 609 
TRP HB2  H  N N 610 
TRP HB3  H  N N 611 
TRP HD1  H  N N 612 
TRP HE1  H  N N 613 
TRP HE3  H  N N 614 
TRP HZ2  H  N N 615 
TRP HZ3  H  N N 616 
TRP HH2  H  N N 617 
TRP HXT  H  N N 618 
TYR N    N  N N 619 
TYR CA   C  N S 620 
TYR C    C  N N 621 
TYR O    O  N N 622 
TYR CB   C  N N 623 
TYR CG   C  Y N 624 
TYR CD1  C  Y N 625 
TYR CD2  C  Y N 626 
TYR CE1  C  Y N 627 
TYR CE2  C  Y N 628 
TYR CZ   C  Y N 629 
TYR OH   O  N N 630 
TYR OXT  O  N N 631 
TYR H    H  N N 632 
TYR H2   H  N N 633 
TYR HA   H  N N 634 
TYR HB2  H  N N 635 
TYR HB3  H  N N 636 
TYR HD1  H  N N 637 
TYR HD2  H  N N 638 
TYR HE1  H  N N 639 
TYR HE2  H  N N 640 
TYR HH   H  N N 641 
TYR HXT  H  N N 642 
VAL N    N  N N 643 
VAL CA   C  N S 644 
VAL C    C  N N 645 
VAL O    O  N N 646 
VAL CB   C  N N 647 
VAL CG1  C  N N 648 
VAL CG2  C  N N 649 
VAL OXT  O  N N 650 
VAL H    H  N N 651 
VAL H2   H  N N 652 
VAL HA   H  N N 653 
VAL HB   H  N N 654 
VAL HG11 H  N N 655 
VAL HG12 H  N N 656 
VAL HG13 H  N N 657 
VAL HG21 H  N N 658 
VAL HG22 H  N N 659 
VAL HG23 H  N N 660 
VAL HXT  H  N N 661 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
DAO O1  C1   doub N N 83  
DAO O2  C1   sing N N 84  
DAO O2  HO2  sing N N 85  
DAO C1  C2   sing N N 86  
DAO C2  C3   sing N N 87  
DAO C2  H21  sing N N 88  
DAO C2  H22  sing N N 89  
DAO C3  C4   sing N N 90  
DAO C3  H31  sing N N 91  
DAO C3  H32  sing N N 92  
DAO C4  C5   sing N N 93  
DAO C4  H41  sing N N 94  
DAO C4  H42  sing N N 95  
DAO C5  C6   sing N N 96  
DAO C5  H51  sing N N 97  
DAO C5  H52  sing N N 98  
DAO C6  C7   sing N N 99  
DAO C6  H61  sing N N 100 
DAO C6  H62  sing N N 101 
DAO C7  C8   sing N N 102 
DAO C7  H71  sing N N 103 
DAO C7  H72  sing N N 104 
DAO C8  C9   sing N N 105 
DAO C8  H81  sing N N 106 
DAO C8  H82  sing N N 107 
DAO C9  C10  sing N N 108 
DAO C9  H91  sing N N 109 
DAO C9  H92  sing N N 110 
DAO C10 C11  sing N N 111 
DAO C10 H101 sing N N 112 
DAO C10 H102 sing N N 113 
DAO C11 C12  sing N N 114 
DAO C11 H111 sing N N 115 
DAO C11 H112 sing N N 116 
DAO C12 H121 sing N N 117 
DAO C12 H122 sing N N 118 
DAO C12 H123 sing N N 119 
FTT C1  C2   sing N N 120 
FTT C1  O2   doub N N 121 
FTT C1  O1   sing N N 122 
FTT C2  C3   sing N N 123 
FTT C2  H21  sing N N 124 
FTT C2  H22  sing N N 125 
FTT C3  C4   sing N N 126 
FTT C3  O3   sing N N 127 
FTT C3  H3   sing N N 128 
FTT C4  C5   sing N N 129 
FTT C4  H41  sing N N 130 
FTT C4  H42  sing N N 131 
FTT C5  C6   sing N N 132 
FTT C5  H51  sing N N 133 
FTT C5  H52  sing N N 134 
FTT C6  C7   sing N N 135 
FTT C6  H61  sing N N 136 
FTT C6  H62  sing N N 137 
FTT C7  C8   sing N N 138 
FTT C7  H71  sing N N 139 
FTT C7  H72  sing N N 140 
FTT C8  C9   sing N N 141 
FTT C8  H81  sing N N 142 
FTT C8  H82  sing N N 143 
FTT C9  C10  sing N N 144 
FTT C9  H91  sing N N 145 
FTT C9  H92  sing N N 146 
FTT C10 C11  sing N N 147 
FTT C10 H101 sing N N 148 
FTT C10 H102 sing N N 149 
FTT C11 C12  sing N N 150 
FTT C11 H111 sing N N 151 
FTT C11 H112 sing N N 152 
FTT C12 C13  sing N N 153 
FTT C12 H121 sing N N 154 
FTT C12 H122 sing N N 155 
FTT C13 C14  sing N N 156 
FTT C13 H131 sing N N 157 
FTT C13 H132 sing N N 158 
FTT C14 H141 sing N N 159 
FTT C14 H142 sing N N 160 
FTT C14 H143 sing N N 161 
FTT O3  HO3  sing N N 162 
FTT O1  HO1  sing N N 163 
GCS C1  C2   sing N N 164 
GCS C1  O1   sing N N 165 
GCS C1  O5   sing N N 166 
GCS C1  H1   sing N N 167 
GCS C2  C3   sing N N 168 
GCS C2  N2   sing N N 169 
GCS C2  H2   sing N N 170 
GCS C3  C4   sing N N 171 
GCS C3  O3   sing N N 172 
GCS C3  H3   sing N N 173 
GCS C4  C5   sing N N 174 
GCS C4  O4   sing N N 175 
GCS C4  H4   sing N N 176 
GCS C5  C6   sing N N 177 
GCS C5  O5   sing N N 178 
GCS C5  H5   sing N N 179 
GCS C6  O6   sing N N 180 
GCS C6  H61  sing N N 181 
GCS C6  H62  sing N N 182 
GCS N2  HN21 sing N N 183 
GCS N2  HN22 sing N N 184 
GCS O1  HO1  sing N N 185 
GCS O3  HO3  sing N N 186 
GCS O4  HO4  sing N N 187 
GCS O6  HO6  sing N N 188 
GLN N   CA   sing N N 189 
GLN N   H    sing N N 190 
GLN N   H2   sing N N 191 
GLN CA  C    sing N N 192 
GLN CA  CB   sing N N 193 
GLN CA  HA   sing N N 194 
GLN C   O    doub N N 195 
GLN C   OXT  sing N N 196 
GLN CB  CG   sing N N 197 
GLN CB  HB2  sing N N 198 
GLN CB  HB3  sing N N 199 
GLN CG  CD   sing N N 200 
GLN CG  HG2  sing N N 201 
GLN CG  HG3  sing N N 202 
GLN CD  OE1  doub N N 203 
GLN CD  NE2  sing N N 204 
GLN NE2 HE21 sing N N 205 
GLN NE2 HE22 sing N N 206 
GLN OXT HXT  sing N N 207 
GLU N   CA   sing N N 208 
GLU N   H    sing N N 209 
GLU N   H2   sing N N 210 
GLU CA  C    sing N N 211 
GLU CA  CB   sing N N 212 
GLU CA  HA   sing N N 213 
GLU C   O    doub N N 214 
GLU C   OXT  sing N N 215 
GLU CB  CG   sing N N 216 
GLU CB  HB2  sing N N 217 
GLU CB  HB3  sing N N 218 
GLU CG  CD   sing N N 219 
GLU CG  HG2  sing N N 220 
GLU CG  HG3  sing N N 221 
GLU CD  OE1  doub N N 222 
GLU CD  OE2  sing N N 223 
GLU OE2 HE2  sing N N 224 
GLU OXT HXT  sing N N 225 
GLY N   CA   sing N N 226 
GLY N   H    sing N N 227 
GLY N   H2   sing N N 228 
GLY CA  C    sing N N 229 
GLY CA  HA2  sing N N 230 
GLY CA  HA3  sing N N 231 
GLY C   O    doub N N 232 
GLY C   OXT  sing N N 233 
GLY OXT HXT  sing N N 234 
GMH C1  C2   sing N N 235 
GMH C1  O1   sing N N 236 
GMH C1  O5   sing N N 237 
GMH C1  H1   sing N N 238 
GMH C2  C3   sing N N 239 
GMH C2  O2   sing N N 240 
GMH C2  H2   sing N N 241 
GMH C3  C4   sing N N 242 
GMH C3  O3   sing N N 243 
GMH C3  H3   sing N N 244 
GMH C4  C5   sing N N 245 
GMH C4  O4   sing N N 246 
GMH C4  H4   sing N N 247 
GMH C5  C6   sing N N 248 
GMH C5  O5   sing N N 249 
GMH C5  H5   sing N N 250 
GMH C6  C7   sing N N 251 
GMH C6  O6   sing N N 252 
GMH C6  H6   sing N N 253 
GMH C7  O7   sing N N 254 
GMH C7  H71  sing N N 255 
GMH C7  H72  sing N N 256 
GMH O1  HO1  sing N N 257 
GMH O2  HO2  sing N N 258 
GMH O3  HO3  sing N N 259 
GMH O4  HO4  sing N N 260 
GMH O6  HO6  sing N N 261 
GMH O7  HO7  sing N N 262 
HIS N   CA   sing N N 263 
HIS N   H    sing N N 264 
HIS N   H2   sing N N 265 
HIS CA  C    sing N N 266 
HIS CA  CB   sing N N 267 
HIS CA  HA   sing N N 268 
HIS C   O    doub N N 269 
HIS C   OXT  sing N N 270 
HIS CB  CG   sing N N 271 
HIS CB  HB2  sing N N 272 
HIS CB  HB3  sing N N 273 
HIS CG  ND1  sing Y N 274 
HIS CG  CD2  doub Y N 275 
HIS ND1 CE1  doub Y N 276 
HIS ND1 HD1  sing N N 277 
HIS CD2 NE2  sing Y N 278 
HIS CD2 HD2  sing N N 279 
HIS CE1 NE2  sing Y N 280 
HIS CE1 HE1  sing N N 281 
HIS NE2 HE2  sing N N 282 
HIS OXT HXT  sing N N 283 
HOH O   H1   sing N N 284 
HOH O   H2   sing N N 285 
ILE N   CA   sing N N 286 
ILE N   H    sing N N 287 
ILE N   H2   sing N N 288 
ILE CA  C    sing N N 289 
ILE CA  CB   sing N N 290 
ILE CA  HA   sing N N 291 
ILE C   O    doub N N 292 
ILE C   OXT  sing N N 293 
ILE CB  CG1  sing N N 294 
ILE CB  CG2  sing N N 295 
ILE CB  HB   sing N N 296 
ILE CG1 CD1  sing N N 297 
ILE CG1 HG12 sing N N 298 
ILE CG1 HG13 sing N N 299 
ILE CG2 HG21 sing N N 300 
ILE CG2 HG22 sing N N 301 
ILE CG2 HG23 sing N N 302 
ILE CD1 HD11 sing N N 303 
ILE CD1 HD12 sing N N 304 
ILE CD1 HD13 sing N N 305 
ILE OXT HXT  sing N N 306 
KDO C1  O1A  doub N N 307 
KDO C1  O1B  sing N N 308 
KDO C1  C2   sing N N 309 
KDO O1B HO1B sing N N 310 
KDO C2  O2   sing N N 311 
KDO C2  C3   sing N N 312 
KDO C2  O6   sing N N 313 
KDO O2  HO2  sing N N 314 
KDO C3  C4   sing N N 315 
KDO C3  H31  sing N N 316 
KDO C3  H32  sing N N 317 
KDO C4  O4   sing N N 318 
KDO C4  C5   sing N N 319 
KDO C4  H4   sing N N 320 
KDO O4  HO4  sing N N 321 
KDO C5  O5   sing N N 322 
KDO C5  C6   sing N N 323 
KDO C5  H5   sing N N 324 
KDO O5  HO5  sing N N 325 
KDO C6  O6   sing N N 326 
KDO C6  C7   sing N N 327 
KDO C6  H6   sing N N 328 
KDO C7  O7   sing N N 329 
KDO C7  C8   sing N N 330 
KDO C7  H7   sing N N 331 
KDO O7  HO7  sing N N 332 
KDO C8  O8   sing N N 333 
KDO C8  H81  sing N N 334 
KDO C8  H82  sing N N 335 
KDO O8  HO8  sing N N 336 
LEU N   CA   sing N N 337 
LEU N   H    sing N N 338 
LEU N   H2   sing N N 339 
LEU CA  C    sing N N 340 
LEU CA  CB   sing N N 341 
LEU CA  HA   sing N N 342 
LEU C   O    doub N N 343 
LEU C   OXT  sing N N 344 
LEU CB  CG   sing N N 345 
LEU CB  HB2  sing N N 346 
LEU CB  HB3  sing N N 347 
LEU CG  CD1  sing N N 348 
LEU CG  CD2  sing N N 349 
LEU CG  HG   sing N N 350 
LEU CD1 HD11 sing N N 351 
LEU CD1 HD12 sing N N 352 
LEU CD1 HD13 sing N N 353 
LEU CD2 HD21 sing N N 354 
LEU CD2 HD22 sing N N 355 
LEU CD2 HD23 sing N N 356 
LEU OXT HXT  sing N N 357 
LYS N   CA   sing N N 358 
LYS N   H    sing N N 359 
LYS N   H2   sing N N 360 
LYS CA  C    sing N N 361 
LYS CA  CB   sing N N 362 
LYS CA  HA   sing N N 363 
LYS C   O    doub N N 364 
LYS C   OXT  sing N N 365 
LYS CB  CG   sing N N 366 
LYS CB  HB2  sing N N 367 
LYS CB  HB3  sing N N 368 
LYS CG  CD   sing N N 369 
LYS CG  HG2  sing N N 370 
LYS CG  HG3  sing N N 371 
LYS CD  CE   sing N N 372 
LYS CD  HD2  sing N N 373 
LYS CD  HD3  sing N N 374 
LYS CE  NZ   sing N N 375 
LYS CE  HE2  sing N N 376 
LYS CE  HE3  sing N N 377 
LYS NZ  HZ1  sing N N 378 
LYS NZ  HZ2  sing N N 379 
LYS NZ  HZ3  sing N N 380 
LYS OXT HXT  sing N N 381 
MET N   CA   sing N N 382 
MET N   H    sing N N 383 
MET N   H2   sing N N 384 
MET CA  C    sing N N 385 
MET CA  CB   sing N N 386 
MET CA  HA   sing N N 387 
MET C   O    doub N N 388 
MET C   OXT  sing N N 389 
MET CB  CG   sing N N 390 
MET CB  HB2  sing N N 391 
MET CB  HB3  sing N N 392 
MET CG  SD   sing N N 393 
MET CG  HG2  sing N N 394 
MET CG  HG3  sing N N 395 
MET SD  CE   sing N N 396 
MET CE  HE1  sing N N 397 
MET CE  HE2  sing N N 398 
MET CE  HE3  sing N N 399 
MET OXT HXT  sing N N 400 
MYR C1  O1   doub N N 401 
MYR C1  O2   sing N N 402 
MYR C1  C2   sing N N 403 
MYR O2  HO2  sing N N 404 
MYR C2  C3   sing N N 405 
MYR C2  H21  sing N N 406 
MYR C2  H22  sing N N 407 
MYR C3  C4   sing N N 408 
MYR C3  H31  sing N N 409 
MYR C3  H32  sing N N 410 
MYR C4  C5   sing N N 411 
MYR C4  H41  sing N N 412 
MYR C4  H42  sing N N 413 
MYR C5  C6   sing N N 414 
MYR C5  H51  sing N N 415 
MYR C5  H52  sing N N 416 
MYR C6  C7   sing N N 417 
MYR C6  H61  sing N N 418 
MYR C6  H62  sing N N 419 
MYR C7  C8   sing N N 420 
MYR C7  H71  sing N N 421 
MYR C7  H72  sing N N 422 
MYR C8  C9   sing N N 423 
MYR C8  H81  sing N N 424 
MYR C8  H82  sing N N 425 
MYR C9  C10  sing N N 426 
MYR C9  H91  sing N N 427 
MYR C9  H92  sing N N 428 
MYR C10 C11  sing N N 429 
MYR C10 H101 sing N N 430 
MYR C10 H102 sing N N 431 
MYR C11 C12  sing N N 432 
MYR C11 H111 sing N N 433 
MYR C11 H112 sing N N 434 
MYR C12 C13  sing N N 435 
MYR C12 H121 sing N N 436 
MYR C12 H122 sing N N 437 
MYR C13 C14  sing N N 438 
MYR C13 H131 sing N N 439 
MYR C13 H132 sing N N 440 
MYR C14 H141 sing N N 441 
MYR C14 H142 sing N N 442 
MYR C14 H143 sing N N 443 
NAG C1  C2   sing N N 444 
NAG C1  O1   sing N N 445 
NAG C1  O5   sing N N 446 
NAG C1  H1   sing N N 447 
NAG C2  C3   sing N N 448 
NAG C2  N2   sing N N 449 
NAG C2  H2   sing N N 450 
NAG C3  C4   sing N N 451 
NAG C3  O3   sing N N 452 
NAG C3  H3   sing N N 453 
NAG C4  C5   sing N N 454 
NAG C4  O4   sing N N 455 
NAG C4  H4   sing N N 456 
NAG C5  C6   sing N N 457 
NAG C5  O5   sing N N 458 
NAG C5  H5   sing N N 459 
NAG C6  O6   sing N N 460 
NAG C6  H61  sing N N 461 
NAG C6  H62  sing N N 462 
NAG C7  C8   sing N N 463 
NAG C7  N2   sing N N 464 
NAG C7  O7   doub N N 465 
NAG C8  H81  sing N N 466 
NAG C8  H82  sing N N 467 
NAG C8  H83  sing N N 468 
NAG N2  HN2  sing N N 469 
NAG O1  HO1  sing N N 470 
NAG O3  HO3  sing N N 471 
NAG O4  HO4  sing N N 472 
NAG O6  HO6  sing N N 473 
PA1 C1  O1   sing N N 474 
PA1 C1  C2   sing N N 475 
PA1 C1  O5   sing N N 476 
PA1 C1  H1   sing N N 477 
PA1 O1  HO1  sing N N 478 
PA1 C2  N2   sing N N 479 
PA1 C2  C3   sing N N 480 
PA1 C2  H2   sing N N 481 
PA1 N2  HN21 sing N N 482 
PA1 N2  HN22 sing N N 483 
PA1 C3  O3   sing N N 484 
PA1 C3  C4   sing N N 485 
PA1 C3  H3   sing N N 486 
PA1 O3  HO3  sing N N 487 
PA1 C4  O4   sing N N 488 
PA1 C4  C5   sing N N 489 
PA1 C4  H4   sing N N 490 
PA1 O4  HO4  sing N N 491 
PA1 C5  O5   sing N N 492 
PA1 C5  C6   sing N N 493 
PA1 C5  H5   sing N N 494 
PA1 C6  O6   sing N N 495 
PA1 C6  H61  sing N N 496 
PA1 C6  H62  sing N N 497 
PA1 O6  HO6  sing N N 498 
PHE N   CA   sing N N 499 
PHE N   H    sing N N 500 
PHE N   H2   sing N N 501 
PHE CA  C    sing N N 502 
PHE CA  CB   sing N N 503 
PHE CA  HA   sing N N 504 
PHE C   O    doub N N 505 
PHE C   OXT  sing N N 506 
PHE CB  CG   sing N N 507 
PHE CB  HB2  sing N N 508 
PHE CB  HB3  sing N N 509 
PHE CG  CD1  doub Y N 510 
PHE CG  CD2  sing Y N 511 
PHE CD1 CE1  sing Y N 512 
PHE CD1 HD1  sing N N 513 
PHE CD2 CE2  doub Y N 514 
PHE CD2 HD2  sing N N 515 
PHE CE1 CZ   doub Y N 516 
PHE CE1 HE1  sing N N 517 
PHE CE2 CZ   sing Y N 518 
PHE CE2 HE2  sing N N 519 
PHE CZ  HZ   sing N N 520 
PHE OXT HXT  sing N N 521 
PO4 P   O1   doub N N 522 
PO4 P   O2   sing N N 523 
PO4 P   O3   sing N N 524 
PO4 P   O4   sing N N 525 
PRO N   CA   sing N N 526 
PRO N   CD   sing N N 527 
PRO N   H    sing N N 528 
PRO CA  C    sing N N 529 
PRO CA  CB   sing N N 530 
PRO CA  HA   sing N N 531 
PRO C   O    doub N N 532 
PRO C   OXT  sing N N 533 
PRO CB  CG   sing N N 534 
PRO CB  HB2  sing N N 535 
PRO CB  HB3  sing N N 536 
PRO CG  CD   sing N N 537 
PRO CG  HG2  sing N N 538 
PRO CG  HG3  sing N N 539 
PRO CD  HD2  sing N N 540 
PRO CD  HD3  sing N N 541 
PRO OXT HXT  sing N N 542 
SER N   CA   sing N N 543 
SER N   H    sing N N 544 
SER N   H2   sing N N 545 
SER CA  C    sing N N 546 
SER CA  CB   sing N N 547 
SER CA  HA   sing N N 548 
SER C   O    doub N N 549 
SER C   OXT  sing N N 550 
SER CB  OG   sing N N 551 
SER CB  HB2  sing N N 552 
SER CB  HB3  sing N N 553 
SER OG  HG   sing N N 554 
SER OXT HXT  sing N N 555 
THR N   CA   sing N N 556 
THR N   H    sing N N 557 
THR N   H2   sing N N 558 
THR CA  C    sing N N 559 
THR CA  CB   sing N N 560 
THR CA  HA   sing N N 561 
THR C   O    doub N N 562 
THR C   OXT  sing N N 563 
THR CB  OG1  sing N N 564 
THR CB  CG2  sing N N 565 
THR CB  HB   sing N N 566 
THR OG1 HG1  sing N N 567 
THR CG2 HG21 sing N N 568 
THR CG2 HG22 sing N N 569 
THR CG2 HG23 sing N N 570 
THR OXT HXT  sing N N 571 
TRP N   CA   sing N N 572 
TRP N   H    sing N N 573 
TRP N   H2   sing N N 574 
TRP CA  C    sing N N 575 
TRP CA  CB   sing N N 576 
TRP CA  HA   sing N N 577 
TRP C   O    doub N N 578 
TRP C   OXT  sing N N 579 
TRP CB  CG   sing N N 580 
TRP CB  HB2  sing N N 581 
TRP CB  HB3  sing N N 582 
TRP CG  CD1  doub Y N 583 
TRP CG  CD2  sing Y N 584 
TRP CD1 NE1  sing Y N 585 
TRP CD1 HD1  sing N N 586 
TRP CD2 CE2  doub Y N 587 
TRP CD2 CE3  sing Y N 588 
TRP NE1 CE2  sing Y N 589 
TRP NE1 HE1  sing N N 590 
TRP CE2 CZ2  sing Y N 591 
TRP CE3 CZ3  doub Y N 592 
TRP CE3 HE3  sing N N 593 
TRP CZ2 CH2  doub Y N 594 
TRP CZ2 HZ2  sing N N 595 
TRP CZ3 CH2  sing Y N 596 
TRP CZ3 HZ3  sing N N 597 
TRP CH2 HH2  sing N N 598 
TRP OXT HXT  sing N N 599 
TYR N   CA   sing N N 600 
TYR N   H    sing N N 601 
TYR N   H2   sing N N 602 
TYR CA  C    sing N N 603 
TYR CA  CB   sing N N 604 
TYR CA  HA   sing N N 605 
TYR C   O    doub N N 606 
TYR C   OXT  sing N N 607 
TYR CB  CG   sing N N 608 
TYR CB  HB2  sing N N 609 
TYR CB  HB3  sing N N 610 
TYR CG  CD1  doub Y N 611 
TYR CG  CD2  sing Y N 612 
TYR CD1 CE1  sing Y N 613 
TYR CD1 HD1  sing N N 614 
TYR CD2 CE2  doub Y N 615 
TYR CD2 HD2  sing N N 616 
TYR CE1 CZ   doub Y N 617 
TYR CE1 HE1  sing N N 618 
TYR CE2 CZ   sing Y N 619 
TYR CE2 HE2  sing N N 620 
TYR CZ  OH   sing N N 621 
TYR OH  HH   sing N N 622 
TYR OXT HXT  sing N N 623 
VAL N   CA   sing N N 624 
VAL N   H    sing N N 625 
VAL N   H2   sing N N 626 
VAL CA  C    sing N N 627 
VAL CA  CB   sing N N 628 
VAL CA  HA   sing N N 629 
VAL C   O    doub N N 630 
VAL C   OXT  sing N N 631 
VAL CB  CG1  sing N N 632 
VAL CB  CG2  sing N N 633 
VAL CB  HB   sing N N 634 
VAL CG1 HG11 sing N N 635 
VAL CG1 HG12 sing N N 636 
VAL CG1 HG13 sing N N 637 
VAL CG2 HG21 sing N N 638 
VAL CG2 HG22 sing N N 639 
VAL CG2 HG23 sing N N 640 
VAL OXT HXT  sing N N 641 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
E 3 PA1 1 E PA1 1 A PA1 1002 n 
E 3 PA1 2 E PA1 2 A PA1 1001 n 
E 3 KDO 3 E KDO 3 A KDO 1012 n 
E 3 GMH 4 E GMH 4 A GMH 1014 n 
E 3 GMH 5 E GMH 5 A GMH 1015 n 
E 3 GMH 6 E GMH 6 A GMH 1016 n 
E 3 KDO 7 E KDO 7 A KDO 1013 n 
F 4 NAG 1 F NAG 1 A NAG 731  n 
F 4 NAG 2 F NAG 2 A NAG 732  n 
G 4 NAG 1 G NAG 1 A NAG 761  n 
G 4 NAG 2 G NAG 2 A NAG 762  n 
H 5 PA1 1 H PA1 1 B PA1 1002 n 
H 5 GCS 2 H GCS 2 B GCS 1001 n 
H 5 KDO 3 H KDO 3 B KDO 1012 n 
H 5 GMH 4 H GMH 4 B GMH 1014 n 
H 5 GMH 5 H GMH 5 B GMH 1015 n 
H 5 GMH 6 H GMH 6 B GMH 1016 n 
H 5 KDO 7 H KDO 7 B KDO 1013 n 
I 4 NAG 1 I NAG 1 B NAG 831  n 
I 4 NAG 2 I NAG 2 B NAG 832  n 
J 4 NAG 1 J NAG 1 B NAG 861  n 
J 4 NAG 2 J NAG 2 B NAG 862  n 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
GCS 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNb                        
GCS 'COMMON NAME'                         GMML     1.0 b-D-glucopyranosamine          
GCS 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpN                      
GCS 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcN                           
GMH 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 LDmanHep                       
GMH 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 L-gro-a-D-manHepp              
KDO 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DKdopa                         
KDO 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Kdop                       
KDO 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Kdo                            
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
PA1 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNa                        
PA1 'COMMON NAME'                         GMML     1.0 a-D-glucopyranosamine          
PA1 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-GlcpN                      
PA1 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcN                           
# 
loop_
_pdbx_entity_branch.entity_id 
_pdbx_entity_branch.type 
3 oligosaccharide 
4 oligosaccharide 
5 oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 3 'LDmanHep1-7LDmanHep1-3LDmanHep1-5[DKdopa2-4]DKdopa2-6DGlcpNa1-6DGlcpNa1-ROH' 'Glycam Condensed Sequence' GMML       1.0   
2 3 'WURCS=2.0/3,7,6/[a2122h-1a_1-5_2*N][Aad1122h-2a_2-6][a11221h-1a_1-5]/1-1-2-2-3-3-3/a6-b1_b6-c2_c4-d2_c5-e1_e3-f1_f7-g1' WURCS 
PDB2Glycan 1.1.0 
3 3 '[][a-D-GlcpN]{[(6+1)][b-D-GlcpN]{[(6+2)][a-D-Kdop]{[(4+2)][a-D-Kdop]{}[(5+1)][a-D-Manp]{[(3+1)][a-D-Manp]{}}}}}' LINUCS 
PDB-CARE   ?     
4 4 DGlcpNAcb1-4DGlcpNAcb1- 'Glycam Condensed Sequence' GMML       1.0   
5 4 'WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1' WURCS                       PDB2Glycan 1.1.0 
6 4 '[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}' LINUCS                      PDB-CARE   ?     
7 5 'LDmanHep1-7LDmanHep1-3LDmanHep1-5[DKdopa2-4]DKdopa2-6DGlcpNb1-6DGlcpNa1-ROH' 'Glycam Condensed Sequence' GMML       1.0   
8 5 
;WURCS=2.0/4,7,6/[a2122h-1a_1-5_2*N][a2122h-1b_1-5_2*N][Aad1122h-2a_2-6][a11221h-1a_1-5]/1-2-3-3-4-4-4/a6-b1_b6-c2_c4-d2_c5-e1_e3-f1_f7-g1
;
WURCS                       PDB2Glycan 1.1.0 
9 5 '[][a-D-GlcpN]{[(6+1)][b-D-GlcpN]{[(6+2)][a-D-Kdop]{[(4+2)][a-D-Kdop]{}[(5+1)][a-D-Manp]{[(3+1)][a-D-Manp]{}}}}}' LINUCS 
PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1  3 2 PA1 C1 O1 1 PA1 O6 HO6 sing ? 
2  3 3 KDO C2 O2 2 PA1 O6 HO6 sing ? 
3  3 4 GMH C1 O1 3 KDO O5 HO5 sing ? 
4  3 5 GMH C1 O1 4 GMH O3 HO3 sing ? 
5  3 6 GMH C1 O1 5 GMH O7 HO7 sing ? 
6  3 7 KDO C2 O2 3 KDO O4 HO4 sing ? 
7  4 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
8  5 2 GCS C1 O1 1 PA1 O6 HO6 sing ? 
9  5 3 KDO C2 O2 2 GCS O6 HO6 sing ? 
10 5 4 GMH C1 O1 3 KDO O5 HO5 sing ? 
11 5 5 GMH C1 O1 4 GMH O3 HO3 sing ? 
12 5 6 GMH C1 O1 5 GMH O7 HO7 sing ? 
13 5 7 KDO C2 O2 3 KDO O4 HO4 sing ? 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
3 PA1 1 n 
3 PA1 2 n 
3 KDO 3 n 
3 GMH 4 n 
3 GMH 5 n 
3 GMH 6 n 
3 KDO 7 n 
4 NAG 1 n 
4 NAG 2 n 
5 PA1 1 n 
5 GCS 2 n 
5 KDO 3 n 
5 GMH 4 n 
5 GMH 5 n 
5 GMH 6 n 
5 KDO 7 n 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
6  '3-HYDROXY-TETRADECANOIC ACID'           FTT 
7  'LAURIC ACID'                            DAO 
8  'MYRISTIC ACID'                          MYR 
9  'PHOSPHATE ION'                          PO4 
10 2-acetamido-2-deoxy-beta-D-glucopyranose NAG 
11 'MAGNESIUM ION'                          MG  
12 water                                    HOH 
# 
loop_
_pdbx_initial_refinement_model.id 
_pdbx_initial_refinement_model.entity_id_list 
_pdbx_initial_refinement_model.type 
_pdbx_initial_refinement_model.source_name 
_pdbx_initial_refinement_model.accession_code 
_pdbx_initial_refinement_model.details 
1 ? 'experimental model' PDB 2Z65 'PDB ENTRY 2Z65, 2Z66' 
2 ? 'experimental model' PDB 2Z66 'PDB ENTRY 2Z65, 2Z66' 
# 



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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.