data_9MGQ
# 
_entry.id   9MGQ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9MGQ         pdb_00009mgq 10.2210/pdb9mgq/pdb 
WWPDB D_1000290936 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-05 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9MGQ 
_pdbx_database_status.recvd_initial_deposition_date   2024-12-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              dwhittington@tangotx.com 
_pdbx_contact_author.name_first         Douglas 
_pdbx_contact_author.name_last          Whittington 
_pdbx_contact_author.name_mi            A 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5946-8543 
# 
_audit_author.name               'Whittington, D.A.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0002-5946-8543 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            68 
_citation.language                  ? 
_citation.page_first                4217 
_citation.page_last                 4236 
_citation.title                     'MTA-Cooperative PRMT5 Inhibitors: Mechanism Switching Through Structure-Based Design.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c01998 
_citation.pdbx_database_id_PubMed   39919252 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Cottrell, K.M.'    1  0009-0008-6511-0696 
primary 'Whittington, D.A.' 2  0000-0002-5946-8543 
primary 'Briggs, K.J.'      3  ?                   
primary 'Jahic, H.'         4  ?                   
primary 'Ali, J.A.'         5  ?                   
primary 'Amor, A.J.'        6  ?                   
primary 'Gotur, D.'         7  ?                   
primary 'Tonini, M.R.'      8  ?                   
primary 'Zhang, W.'         9  ?                   
primary 'Huang, A.'         10 ?                   
primary 'Maxwell, J.P.'     11 0000-0002-5969-6490 
# 
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 'Protein arginine N-methyltransferase 5'                                                                        
73763.625 1   2.1.1.320 ? 'FULL LENGTH' 'N-terminal Flag tag'  
2 polymer     man 'Methylosome protein 50'                                                                                        
37862.406 1   ?         ? ?             'N-terminal His-8 tag' 
3 non-polymer syn SINEFUNGIN                                                                                                      
381.387   1   ?         ? ?             ?                      
4 non-polymer syn '2-(cyclobutylamino)-N-{(2R)-2-hydroxy-2-[(3S)-1,2,3,4-tetrahydroisoquinolin-3-yl]ethyl}pyridine-4-carboxamide' 
366.457   1   ?         ? ?             ?                      
5 non-polymer syn 1,2-ETHANEDIOL                                                                                                  
62.068    19  ?         ? ?             ?                      
6 non-polymer syn 'SULFATE ION'                                                                                                   
96.063    8   ?         ? ?             ?                      
7 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                                                                         
106.120   3   ?         ? ?             ?                      
8 water       nat water                                                                                                           
18.015    369 ?         ? ?             ?                      
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 
;72 kDa ICln-binding protein,Histone-arginine N-methyltransferase PRMT5,Jak-binding protein 1,Shk1 kinase-binding protein 1 homolog,SKB1Hs
;
2 'MEP-50,Androgen receptor cofactor p44,WD repeat-containing protein 77,p44/Mep50' 
# 
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 
;MDYKDDDDKAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFIQEPAKNRPGPQTRSDLL
LSGRDWNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELNFGAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFW
MRVPLVAPEDLRDDIIENAPTTHTEEYSGEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILP
TSIFLTNKKGFPVLSKMHQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPL
QPLMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKDTNVQVLMVLGAGRGPLVNASLRAAKQADRRIKLYAVE
KNPNAVVTLENWQFEEWGSQVTVVSSDMREWVAPEKADIIVSELLGSFADNELSPECLDGAQHFLKDDGVSIPGEYTSFL
APISSSKLYNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSAPQPCFTFSHPNRDPMIDNNRYCTLEFPVEVNTVLHGFA
GYFETVLYQDITLSIRPETHSPGMFSWFPILFPIKQPITVREGQTICVRFWRCSNSKKVWYEWAVTAPVCSAIHNPTGRS
YTIGL
;
;MDYKDDDDKAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFIQEPAKNRPGPQTRSDLL
LSGRDWNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELNFGAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFW
MRVPLVAPEDLRDDIIENAPTTHTEEYSGEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILP
TSIFLTNKKGFPVLSKMHQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPL
QPLMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKDTNVQVLMVLGAGRGPLVNASLRAAKQADRRIKLYAVE
KNPNAVVTLENWQFEEWGSQVTVVSSDMREWVAPEKADIIVSELLGSFADNELSPECLDGAQHFLKDDGVSIPGEYTSFL
APISSSKLYNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSAPQPCFTFSHPNRDPMIDNNRYCTLEFPVEVNTVLHGFA
GYFETVLYQDITLSIRPETHSPGMFSWFPILFPIKQPITVREGQTICVRFWRCSNSKKVWYEWAVTAPVCSAIHNPTGRS
YTIGL
;
A ? 
2 'polypeptide(L)' no no 
;MHHHHHHHHRKETPPPLVPPAAREWNLPPNAPACMERQLEAARYRSDGALLLGASSLSGRCWAGSLWLFKDPCAAPNEGF
CSAGVQTEAGVADLTWVGERGILVASDSGAVELWELDENETLIVSKFCKYEHDDIVSTVSVLSSGTQAVSGSKDICIKVW
DLAQQVVLSSYRAHAAQVTCVAASPHKDSVFLSCSEDNRILLWDTRCPKPASQIGCSAPGYLPTSLAWHPQQSEVFVFGD
ENGTVSLVDTKSTSCVLSSAVHSQCVTGLVFSPHSVPFLASLSEDCSLAVLDSSLSELFRSQAHRDFVRDATWSPLNHSL
LTTVGWDHQVVHHVVPTEPLPAPGPASVTE
;
;MHHHHHHHHRKETPPPLVPPAAREWNLPPNAPACMERQLEAARYRSDGALLLGASSLSGRCWAGSLWLFKDPCAAPNEGF
CSAGVQTEAGVADLTWVGERGILVASDSGAVELWELDENETLIVSKFCKYEHDDIVSTVSVLSSGTQAVSGSKDICIKVW
DLAQQVVLSSYRAHAAQVTCVAASPHKDSVFLSCSEDNRILLWDTRCPKPASQIGCSAPGYLPTSLAWHPQQSEVFVFGD
ENGTVSLVDTKSTSCVLSSAVHSQCVTGLVFSPHSVPFLASLSEDCSLAVLDSSLSELFRSQAHRDFVRDATWSPLNHSL
LTTVGWDHQVVHHVVPTEPLPAPGPASVTE
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 SINEFUNGIN                                                                                                      SFG   
4 '2-(cyclobutylamino)-N-{(2R)-2-hydroxy-2-[(3S)-1,2,3,4-tetrahydroisoquinolin-3-yl]ethyl}pyridine-4-carboxamide' A1BLG 
5 1,2-ETHANEDIOL                                                                                                  EDO   
6 'SULFATE ION'                                                                                                   SO4   
7 'DI(HYDROXYETHYL)ETHER'                                                                                         PEG   
8 water                                                                                                           HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ASP n 
1 3   TYR n 
1 4   LYS n 
1 5   ASP n 
1 6   ASP n 
1 7   ASP n 
1 8   ASP n 
1 9   LYS n 
1 10  ALA n 
1 11  ALA n 
1 12  MET n 
1 13  ALA n 
1 14  VAL n 
1 15  GLY n 
1 16  GLY n 
1 17  ALA n 
1 18  GLY n 
1 19  GLY n 
1 20  SER n 
1 21  ARG n 
1 22  VAL n 
1 23  SER n 
1 24  SER n 
1 25  GLY n 
1 26  ARG n 
1 27  ASP n 
1 28  LEU n 
1 29  ASN n 
1 30  CYS n 
1 31  VAL n 
1 32  PRO n 
1 33  GLU n 
1 34  ILE n 
1 35  ALA n 
1 36  ASP n 
1 37  THR n 
1 38  LEU n 
1 39  GLY n 
1 40  ALA n 
1 41  VAL n 
1 42  ALA n 
1 43  LYS n 
1 44  GLN n 
1 45  GLY n 
1 46  PHE n 
1 47  ASP n 
1 48  PHE n 
1 49  LEU n 
1 50  CYS n 
1 51  MET n 
1 52  PRO n 
1 53  VAL n 
1 54  PHE n 
1 55  HIS n 
1 56  PRO n 
1 57  ARG n 
1 58  PHE n 
1 59  LYS n 
1 60  ARG n 
1 61  GLU n 
1 62  PHE n 
1 63  ILE n 
1 64  GLN n 
1 65  GLU n 
1 66  PRO n 
1 67  ALA n 
1 68  LYS n 
1 69  ASN n 
1 70  ARG n 
1 71  PRO n 
1 72  GLY n 
1 73  PRO n 
1 74  GLN n 
1 75  THR n 
1 76  ARG n 
1 77  SER n 
1 78  ASP n 
1 79  LEU n 
1 80  LEU n 
1 81  LEU n 
1 82  SER n 
1 83  GLY n 
1 84  ARG n 
1 85  ASP n 
1 86  TRP n 
1 87  ASN n 
1 88  THR n 
1 89  LEU n 
1 90  ILE n 
1 91  VAL n 
1 92  GLY n 
1 93  LYS n 
1 94  LEU n 
1 95  SER n 
1 96  PRO n 
1 97  TRP n 
1 98  ILE n 
1 99  ARG n 
1 100 PRO n 
1 101 ASP n 
1 102 SER n 
1 103 LYS n 
1 104 VAL n 
1 105 GLU n 
1 106 LYS n 
1 107 ILE n 
1 108 ARG n 
1 109 ARG n 
1 110 ASN n 
1 111 SER n 
1 112 GLU n 
1 113 ALA n 
1 114 ALA n 
1 115 MET n 
1 116 LEU n 
1 117 GLN n 
1 118 GLU n 
1 119 LEU n 
1 120 ASN n 
1 121 PHE n 
1 122 GLY n 
1 123 ALA n 
1 124 TYR n 
1 125 LEU n 
1 126 GLY n 
1 127 LEU n 
1 128 PRO n 
1 129 ALA n 
1 130 PHE n 
1 131 LEU n 
1 132 LEU n 
1 133 PRO n 
1 134 LEU n 
1 135 ASN n 
1 136 GLN n 
1 137 GLU n 
1 138 ASP n 
1 139 ASN n 
1 140 THR n 
1 141 ASN n 
1 142 LEU n 
1 143 ALA n 
1 144 ARG n 
1 145 VAL n 
1 146 LEU n 
1 147 THR n 
1 148 ASN n 
1 149 HIS n 
1 150 ILE n 
1 151 HIS n 
1 152 THR n 
1 153 GLY n 
1 154 HIS n 
1 155 HIS n 
1 156 SER n 
1 157 SER n 
1 158 MET n 
1 159 PHE n 
1 160 TRP n 
1 161 MET n 
1 162 ARG n 
1 163 VAL n 
1 164 PRO n 
1 165 LEU n 
1 166 VAL n 
1 167 ALA n 
1 168 PRO n 
1 169 GLU n 
1 170 ASP n 
1 171 LEU n 
1 172 ARG n 
1 173 ASP n 
1 174 ASP n 
1 175 ILE n 
1 176 ILE n 
1 177 GLU n 
1 178 ASN n 
1 179 ALA n 
1 180 PRO n 
1 181 THR n 
1 182 THR n 
1 183 HIS n 
1 184 THR n 
1 185 GLU n 
1 186 GLU n 
1 187 TYR n 
1 188 SER n 
1 189 GLY n 
1 190 GLU n 
1 191 GLU n 
1 192 LYS n 
1 193 THR n 
1 194 TRP n 
1 195 MET n 
1 196 TRP n 
1 197 TRP n 
1 198 HIS n 
1 199 ASN n 
1 200 PHE n 
1 201 ARG n 
1 202 THR n 
1 203 LEU n 
1 204 CYS n 
1 205 ASP n 
1 206 TYR n 
1 207 SER n 
1 208 LYS n 
1 209 ARG n 
1 210 ILE n 
1 211 ALA n 
1 212 VAL n 
1 213 ALA n 
1 214 LEU n 
1 215 GLU n 
1 216 ILE n 
1 217 GLY n 
1 218 ALA n 
1 219 ASP n 
1 220 LEU n 
1 221 PRO n 
1 222 SER n 
1 223 ASN n 
1 224 HIS n 
1 225 VAL n 
1 226 ILE n 
1 227 ASP n 
1 228 ARG n 
1 229 TRP n 
1 230 LEU n 
1 231 GLY n 
1 232 GLU n 
1 233 PRO n 
1 234 ILE n 
1 235 LYS n 
1 236 ALA n 
1 237 ALA n 
1 238 ILE n 
1 239 LEU n 
1 240 PRO n 
1 241 THR n 
1 242 SER n 
1 243 ILE n 
1 244 PHE n 
1 245 LEU n 
1 246 THR n 
1 247 ASN n 
1 248 LYS n 
1 249 LYS n 
1 250 GLY n 
1 251 PHE n 
1 252 PRO n 
1 253 VAL n 
1 254 LEU n 
1 255 SER n 
1 256 LYS n 
1 257 MET n 
1 258 HIS n 
1 259 GLN n 
1 260 ARG n 
1 261 LEU n 
1 262 ILE n 
1 263 PHE n 
1 264 ARG n 
1 265 LEU n 
1 266 LEU n 
1 267 LYS n 
1 268 LEU n 
1 269 GLU n 
1 270 VAL n 
1 271 GLN n 
1 272 PHE n 
1 273 ILE n 
1 274 ILE n 
1 275 THR n 
1 276 GLY n 
1 277 THR n 
1 278 ASN n 
1 279 HIS n 
1 280 HIS n 
1 281 SER n 
1 282 GLU n 
1 283 LYS n 
1 284 GLU n 
1 285 PHE n 
1 286 CYS n 
1 287 SER n 
1 288 TYR n 
1 289 LEU n 
1 290 GLN n 
1 291 TYR n 
1 292 LEU n 
1 293 GLU n 
1 294 TYR n 
1 295 LEU n 
1 296 SER n 
1 297 GLN n 
1 298 ASN n 
1 299 ARG n 
1 300 PRO n 
1 301 PRO n 
1 302 PRO n 
1 303 ASN n 
1 304 ALA n 
1 305 TYR n 
1 306 GLU n 
1 307 LEU n 
1 308 PHE n 
1 309 ALA n 
1 310 LYS n 
1 311 GLY n 
1 312 TYR n 
1 313 GLU n 
1 314 ASP n 
1 315 TYR n 
1 316 LEU n 
1 317 GLN n 
1 318 SER n 
1 319 PRO n 
1 320 LEU n 
1 321 GLN n 
1 322 PRO n 
1 323 LEU n 
1 324 MET n 
1 325 ASP n 
1 326 ASN n 
1 327 LEU n 
1 328 GLU n 
1 329 SER n 
1 330 GLN n 
1 331 THR n 
1 332 TYR n 
1 333 GLU n 
1 334 VAL n 
1 335 PHE n 
1 336 GLU n 
1 337 LYS n 
1 338 ASP n 
1 339 PRO n 
1 340 ILE n 
1 341 LYS n 
1 342 TYR n 
1 343 SER n 
1 344 GLN n 
1 345 TYR n 
1 346 GLN n 
1 347 GLN n 
1 348 ALA n 
1 349 ILE n 
1 350 TYR n 
1 351 LYS n 
1 352 CYS n 
1 353 LEU n 
1 354 LEU n 
1 355 ASP n 
1 356 ARG n 
1 357 VAL n 
1 358 PRO n 
1 359 GLU n 
1 360 GLU n 
1 361 GLU n 
1 362 LYS n 
1 363 ASP n 
1 364 THR n 
1 365 ASN n 
1 366 VAL n 
1 367 GLN n 
1 368 VAL n 
1 369 LEU n 
1 370 MET n 
1 371 VAL n 
1 372 LEU n 
1 373 GLY n 
1 374 ALA n 
1 375 GLY n 
1 376 ARG n 
1 377 GLY n 
1 378 PRO n 
1 379 LEU n 
1 380 VAL n 
1 381 ASN n 
1 382 ALA n 
1 383 SER n 
1 384 LEU n 
1 385 ARG n 
1 386 ALA n 
1 387 ALA n 
1 388 LYS n 
1 389 GLN n 
1 390 ALA n 
1 391 ASP n 
1 392 ARG n 
1 393 ARG n 
1 394 ILE n 
1 395 LYS n 
1 396 LEU n 
1 397 TYR n 
1 398 ALA n 
1 399 VAL n 
1 400 GLU n 
1 401 LYS n 
1 402 ASN n 
1 403 PRO n 
1 404 ASN n 
1 405 ALA n 
1 406 VAL n 
1 407 VAL n 
1 408 THR n 
1 409 LEU n 
1 410 GLU n 
1 411 ASN n 
1 412 TRP n 
1 413 GLN n 
1 414 PHE n 
1 415 GLU n 
1 416 GLU n 
1 417 TRP n 
1 418 GLY n 
1 419 SER n 
1 420 GLN n 
1 421 VAL n 
1 422 THR n 
1 423 VAL n 
1 424 VAL n 
1 425 SER n 
1 426 SER n 
1 427 ASP n 
1 428 MET n 
1 429 ARG n 
1 430 GLU n 
1 431 TRP n 
1 432 VAL n 
1 433 ALA n 
1 434 PRO n 
1 435 GLU n 
1 436 LYS n 
1 437 ALA n 
1 438 ASP n 
1 439 ILE n 
1 440 ILE n 
1 441 VAL n 
1 442 SER n 
1 443 GLU n 
1 444 LEU n 
1 445 LEU n 
1 446 GLY n 
1 447 SER n 
1 448 PHE n 
1 449 ALA n 
1 450 ASP n 
1 451 ASN n 
1 452 GLU n 
1 453 LEU n 
1 454 SER n 
1 455 PRO n 
1 456 GLU n 
1 457 CYS n 
1 458 LEU n 
1 459 ASP n 
1 460 GLY n 
1 461 ALA n 
1 462 GLN n 
1 463 HIS n 
1 464 PHE n 
1 465 LEU n 
1 466 LYS n 
1 467 ASP n 
1 468 ASP n 
1 469 GLY n 
1 470 VAL n 
1 471 SER n 
1 472 ILE n 
1 473 PRO n 
1 474 GLY n 
1 475 GLU n 
1 476 TYR n 
1 477 THR n 
1 478 SER n 
1 479 PHE n 
1 480 LEU n 
1 481 ALA n 
1 482 PRO n 
1 483 ILE n 
1 484 SER n 
1 485 SER n 
1 486 SER n 
1 487 LYS n 
1 488 LEU n 
1 489 TYR n 
1 490 ASN n 
1 491 GLU n 
1 492 VAL n 
1 493 ARG n 
1 494 ALA n 
1 495 CYS n 
1 496 ARG n 
1 497 GLU n 
1 498 LYS n 
1 499 ASP n 
1 500 ARG n 
1 501 ASP n 
1 502 PRO n 
1 503 GLU n 
1 504 ALA n 
1 505 GLN n 
1 506 PHE n 
1 507 GLU n 
1 508 MET n 
1 509 PRO n 
1 510 TYR n 
1 511 VAL n 
1 512 VAL n 
1 513 ARG n 
1 514 LEU n 
1 515 HIS n 
1 516 ASN n 
1 517 PHE n 
1 518 HIS n 
1 519 GLN n 
1 520 LEU n 
1 521 SER n 
1 522 ALA n 
1 523 PRO n 
1 524 GLN n 
1 525 PRO n 
1 526 CYS n 
1 527 PHE n 
1 528 THR n 
1 529 PHE n 
1 530 SER n 
1 531 HIS n 
1 532 PRO n 
1 533 ASN n 
1 534 ARG n 
1 535 ASP n 
1 536 PRO n 
1 537 MET n 
1 538 ILE n 
1 539 ASP n 
1 540 ASN n 
1 541 ASN n 
1 542 ARG n 
1 543 TYR n 
1 544 CYS n 
1 545 THR n 
1 546 LEU n 
1 547 GLU n 
1 548 PHE n 
1 549 PRO n 
1 550 VAL n 
1 551 GLU n 
1 552 VAL n 
1 553 ASN n 
1 554 THR n 
1 555 VAL n 
1 556 LEU n 
1 557 HIS n 
1 558 GLY n 
1 559 PHE n 
1 560 ALA n 
1 561 GLY n 
1 562 TYR n 
1 563 PHE n 
1 564 GLU n 
1 565 THR n 
1 566 VAL n 
1 567 LEU n 
1 568 TYR n 
1 569 GLN n 
1 570 ASP n 
1 571 ILE n 
1 572 THR n 
1 573 LEU n 
1 574 SER n 
1 575 ILE n 
1 576 ARG n 
1 577 PRO n 
1 578 GLU n 
1 579 THR n 
1 580 HIS n 
1 581 SER n 
1 582 PRO n 
1 583 GLY n 
1 584 MET n 
1 585 PHE n 
1 586 SER n 
1 587 TRP n 
1 588 PHE n 
1 589 PRO n 
1 590 ILE n 
1 591 LEU n 
1 592 PHE n 
1 593 PRO n 
1 594 ILE n 
1 595 LYS n 
1 596 GLN n 
1 597 PRO n 
1 598 ILE n 
1 599 THR n 
1 600 VAL n 
1 601 ARG n 
1 602 GLU n 
1 603 GLY n 
1 604 GLN n 
1 605 THR n 
1 606 ILE n 
1 607 CYS n 
1 608 VAL n 
1 609 ARG n 
1 610 PHE n 
1 611 TRP n 
1 612 ARG n 
1 613 CYS n 
1 614 SER n 
1 615 ASN n 
1 616 SER n 
1 617 LYS n 
1 618 LYS n 
1 619 VAL n 
1 620 TRP n 
1 621 TYR n 
1 622 GLU n 
1 623 TRP n 
1 624 ALA n 
1 625 VAL n 
1 626 THR n 
1 627 ALA n 
1 628 PRO n 
1 629 VAL n 
1 630 CYS n 
1 631 SER n 
1 632 ALA n 
1 633 ILE n 
1 634 HIS n 
1 635 ASN n 
1 636 PRO n 
1 637 THR n 
1 638 GLY n 
1 639 ARG n 
1 640 SER n 
1 641 TYR n 
1 642 THR n 
1 643 ILE n 
1 644 GLY n 
1 645 LEU n 
2 1   MET n 
2 2   HIS n 
2 3   HIS n 
2 4   HIS n 
2 5   HIS n 
2 6   HIS n 
2 7   HIS n 
2 8   HIS n 
2 9   HIS n 
2 10  ARG n 
2 11  LYS n 
2 12  GLU n 
2 13  THR n 
2 14  PRO n 
2 15  PRO n 
2 16  PRO n 
2 17  LEU n 
2 18  VAL n 
2 19  PRO n 
2 20  PRO n 
2 21  ALA n 
2 22  ALA n 
2 23  ARG n 
2 24  GLU n 
2 25  TRP n 
2 26  ASN n 
2 27  LEU n 
2 28  PRO n 
2 29  PRO n 
2 30  ASN n 
2 31  ALA n 
2 32  PRO n 
2 33  ALA n 
2 34  CYS n 
2 35  MET n 
2 36  GLU n 
2 37  ARG n 
2 38  GLN n 
2 39  LEU n 
2 40  GLU n 
2 41  ALA n 
2 42  ALA n 
2 43  ARG n 
2 44  TYR n 
2 45  ARG n 
2 46  SER n 
2 47  ASP n 
2 48  GLY n 
2 49  ALA n 
2 50  LEU n 
2 51  LEU n 
2 52  LEU n 
2 53  GLY n 
2 54  ALA n 
2 55  SER n 
2 56  SER n 
2 57  LEU n 
2 58  SER n 
2 59  GLY n 
2 60  ARG n 
2 61  CYS n 
2 62  TRP n 
2 63  ALA n 
2 64  GLY n 
2 65  SER n 
2 66  LEU n 
2 67  TRP n 
2 68  LEU n 
2 69  PHE n 
2 70  LYS n 
2 71  ASP n 
2 72  PRO n 
2 73  CYS n 
2 74  ALA n 
2 75  ALA n 
2 76  PRO n 
2 77  ASN n 
2 78  GLU n 
2 79  GLY n 
2 80  PHE n 
2 81  CYS n 
2 82  SER n 
2 83  ALA n 
2 84  GLY n 
2 85  VAL n 
2 86  GLN n 
2 87  THR n 
2 88  GLU n 
2 89  ALA n 
2 90  GLY n 
2 91  VAL n 
2 92  ALA n 
2 93  ASP n 
2 94  LEU n 
2 95  THR n 
2 96  TRP n 
2 97  VAL n 
2 98  GLY n 
2 99  GLU n 
2 100 ARG n 
2 101 GLY n 
2 102 ILE n 
2 103 LEU n 
2 104 VAL n 
2 105 ALA n 
2 106 SER n 
2 107 ASP n 
2 108 SER n 
2 109 GLY n 
2 110 ALA n 
2 111 VAL n 
2 112 GLU n 
2 113 LEU n 
2 114 TRP n 
2 115 GLU n 
2 116 LEU n 
2 117 ASP n 
2 118 GLU n 
2 119 ASN n 
2 120 GLU n 
2 121 THR n 
2 122 LEU n 
2 123 ILE n 
2 124 VAL n 
2 125 SER n 
2 126 LYS n 
2 127 PHE n 
2 128 CYS n 
2 129 LYS n 
2 130 TYR n 
2 131 GLU n 
2 132 HIS n 
2 133 ASP n 
2 134 ASP n 
2 135 ILE n 
2 136 VAL n 
2 137 SER n 
2 138 THR n 
2 139 VAL n 
2 140 SER n 
2 141 VAL n 
2 142 LEU n 
2 143 SER n 
2 144 SER n 
2 145 GLY n 
2 146 THR n 
2 147 GLN n 
2 148 ALA n 
2 149 VAL n 
2 150 SER n 
2 151 GLY n 
2 152 SER n 
2 153 LYS n 
2 154 ASP n 
2 155 ILE n 
2 156 CYS n 
2 157 ILE n 
2 158 LYS n 
2 159 VAL n 
2 160 TRP n 
2 161 ASP n 
2 162 LEU n 
2 163 ALA n 
2 164 GLN n 
2 165 GLN n 
2 166 VAL n 
2 167 VAL n 
2 168 LEU n 
2 169 SER n 
2 170 SER n 
2 171 TYR n 
2 172 ARG n 
2 173 ALA n 
2 174 HIS n 
2 175 ALA n 
2 176 ALA n 
2 177 GLN n 
2 178 VAL n 
2 179 THR n 
2 180 CYS n 
2 181 VAL n 
2 182 ALA n 
2 183 ALA n 
2 184 SER n 
2 185 PRO n 
2 186 HIS n 
2 187 LYS n 
2 188 ASP n 
2 189 SER n 
2 190 VAL n 
2 191 PHE n 
2 192 LEU n 
2 193 SER n 
2 194 CYS n 
2 195 SER n 
2 196 GLU n 
2 197 ASP n 
2 198 ASN n 
2 199 ARG n 
2 200 ILE n 
2 201 LEU n 
2 202 LEU n 
2 203 TRP n 
2 204 ASP n 
2 205 THR n 
2 206 ARG n 
2 207 CYS n 
2 208 PRO n 
2 209 LYS n 
2 210 PRO n 
2 211 ALA n 
2 212 SER n 
2 213 GLN n 
2 214 ILE n 
2 215 GLY n 
2 216 CYS n 
2 217 SER n 
2 218 ALA n 
2 219 PRO n 
2 220 GLY n 
2 221 TYR n 
2 222 LEU n 
2 223 PRO n 
2 224 THR n 
2 225 SER n 
2 226 LEU n 
2 227 ALA n 
2 228 TRP n 
2 229 HIS n 
2 230 PRO n 
2 231 GLN n 
2 232 GLN n 
2 233 SER n 
2 234 GLU n 
2 235 VAL n 
2 236 PHE n 
2 237 VAL n 
2 238 PHE n 
2 239 GLY n 
2 240 ASP n 
2 241 GLU n 
2 242 ASN n 
2 243 GLY n 
2 244 THR n 
2 245 VAL n 
2 246 SER n 
2 247 LEU n 
2 248 VAL n 
2 249 ASP n 
2 250 THR n 
2 251 LYS n 
2 252 SER n 
2 253 THR n 
2 254 SER n 
2 255 CYS n 
2 256 VAL n 
2 257 LEU n 
2 258 SER n 
2 259 SER n 
2 260 ALA n 
2 261 VAL n 
2 262 HIS n 
2 263 SER n 
2 264 GLN n 
2 265 CYS n 
2 266 VAL n 
2 267 THR n 
2 268 GLY n 
2 269 LEU n 
2 270 VAL n 
2 271 PHE n 
2 272 SER n 
2 273 PRO n 
2 274 HIS n 
2 275 SER n 
2 276 VAL n 
2 277 PRO n 
2 278 PHE n 
2 279 LEU n 
2 280 ALA n 
2 281 SER n 
2 282 LEU n 
2 283 SER n 
2 284 GLU n 
2 285 ASP n 
2 286 CYS n 
2 287 SER n 
2 288 LEU n 
2 289 ALA n 
2 290 VAL n 
2 291 LEU n 
2 292 ASP n 
2 293 SER n 
2 294 SER n 
2 295 LEU n 
2 296 SER n 
2 297 GLU n 
2 298 LEU n 
2 299 PHE n 
2 300 ARG n 
2 301 SER n 
2 302 GLN n 
2 303 ALA n 
2 304 HIS n 
2 305 ARG n 
2 306 ASP n 
2 307 PHE n 
2 308 VAL n 
2 309 ARG n 
2 310 ASP n 
2 311 ALA n 
2 312 THR n 
2 313 TRP n 
2 314 SER n 
2 315 PRO n 
2 316 LEU n 
2 317 ASN n 
2 318 HIS n 
2 319 SER n 
2 320 LEU n 
2 321 LEU n 
2 322 THR n 
2 323 THR n 
2 324 VAL n 
2 325 GLY n 
2 326 TRP n 
2 327 ASP n 
2 328 HIS n 
2 329 GLN n 
2 330 VAL n 
2 331 VAL n 
2 332 HIS n 
2 333 HIS n 
2 334 VAL n 
2 335 VAL n 
2 336 PRO n 
2 337 THR n 
2 338 GLU n 
2 339 PRO n 
2 340 LEU n 
2 341 PRO n 
2 342 ALA n 
2 343 PRO n 
2 344 GLY n 
2 345 PRO n 
2 346 ALA n 
2 347 SER n 
2 348 VAL n 
2 349 THR n 
2 350 GLU 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 'Biological sequence' 1 645 human ? 'PRMT5, HRMT1L5, IBP72, JBP1, SKB1'       ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? 
? ? ? 'Trichoplusia ni' 7111 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 350 human ? 'WDR77, MEP50, WD45, HKMT1069, Nbla10071' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? 
? ? ? 'Trichoplusia ni' 7111 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1BLG non-polymer         . 
'2-(cyclobutylamino)-N-{(2R)-2-hydroxy-2-[(3S)-1,2,3,4-tetrahydroisoquinolin-3-yl]ethyl}pyridine-4-carboxamide' ?                  
'C21 H26 N4 O2'  366.457 
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 
EDO   non-polymer         . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL'  'C2 H6 O2'       62.068  
GLN   'L-peptide linking' y GLUTAMINE ?                  'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ?                  'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE ?                  'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE ?                  'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER ?                  'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE ?                  'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE ?                  'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE ?                  'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE ?                  'C5 H11 N O2 S'  149.211 
PEG   non-polymer         . 'DI(HYDROXYETHYL)ETHER' ?                  'C4 H10 O3'      106.120 
PHE   'L-peptide linking' y PHENYLALANINE ?                  'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE ?                  'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE ?                  'C3 H7 N O3'     105.093 
SFG   non-polymer         . SINEFUNGIN ADENOSYL-ORNITHINE 'C15 H23 N7 O5'  381.387 
SO4   non-polymer         . 'SULFATE ION' ?                  'O4 S -2'        96.063  
THR   'L-peptide linking' y THREONINE ?                  'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ?                  'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE ?                  'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE ?                  'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -7  ?   ?   ?   A . n 
A 1 2   ASP 2   -6  ?   ?   ?   A . n 
A 1 3   TYR 3   -5  ?   ?   ?   A . n 
A 1 4   LYS 4   -4  ?   ?   ?   A . n 
A 1 5   ASP 5   -3  ?   ?   ?   A . n 
A 1 6   ASP 6   -2  ?   ?   ?   A . n 
A 1 7   ASP 7   -1  ?   ?   ?   A . n 
A 1 8   ASP 8   0   ?   ?   ?   A . n 
A 1 9   LYS 9   1   ?   ?   ?   A . n 
A 1 10  ALA 10  2   ?   ?   ?   A . n 
A 1 11  ALA 11  3   ?   ?   ?   A . n 
A 1 12  MET 12  4   ?   ?   ?   A . n 
A 1 13  ALA 13  5   ?   ?   ?   A . n 
A 1 14  VAL 14  6   ?   ?   ?   A . n 
A 1 15  GLY 15  7   ?   ?   ?   A . n 
A 1 16  GLY 16  8   ?   ?   ?   A . n 
A 1 17  ALA 17  9   ?   ?   ?   A . n 
A 1 18  GLY 18  10  ?   ?   ?   A . n 
A 1 19  GLY 19  11  ?   ?   ?   A . n 
A 1 20  SER 20  12  ?   ?   ?   A . n 
A 1 21  ARG 21  13  ?   ?   ?   A . n 
A 1 22  VAL 22  14  14  VAL VAL A . n 
A 1 23  SER 23  15  15  SER SER A . n 
A 1 24  SER 24  16  16  SER SER A . n 
A 1 25  GLY 25  17  17  GLY GLY A . n 
A 1 26  ARG 26  18  18  ARG ARG A . n 
A 1 27  ASP 27  19  19  ASP ASP A . n 
A 1 28  LEU 28  20  20  LEU LEU A . n 
A 1 29  ASN 29  21  21  ASN ASN A . n 
A 1 30  CYS 30  22  22  CYS CYS A . n 
A 1 31  VAL 31  23  23  VAL VAL A . n 
A 1 32  PRO 32  24  24  PRO PRO A . n 
A 1 33  GLU 33  25  25  GLU GLU A . n 
A 1 34  ILE 34  26  26  ILE ILE A . n 
A 1 35  ALA 35  27  27  ALA ALA A . n 
A 1 36  ASP 36  28  28  ASP ASP A . n 
A 1 37  THR 37  29  29  THR THR A . n 
A 1 38  LEU 38  30  30  LEU LEU A . n 
A 1 39  GLY 39  31  31  GLY GLY A . n 
A 1 40  ALA 40  32  32  ALA ALA A . n 
A 1 41  VAL 41  33  33  VAL VAL A . n 
A 1 42  ALA 42  34  34  ALA ALA A . n 
A 1 43  LYS 43  35  35  LYS LYS A . n 
A 1 44  GLN 44  36  36  GLN GLN A . n 
A 1 45  GLY 45  37  37  GLY GLY A . n 
A 1 46  PHE 46  38  38  PHE PHE A . n 
A 1 47  ASP 47  39  39  ASP ASP A . n 
A 1 48  PHE 48  40  40  PHE PHE A . n 
A 1 49  LEU 49  41  41  LEU LEU A . n 
A 1 50  CYS 50  42  42  CYS CYS A . n 
A 1 51  MET 51  43  43  MET MET A . n 
A 1 52  PRO 52  44  44  PRO PRO A . n 
A 1 53  VAL 53  45  45  VAL VAL A . n 
A 1 54  PHE 54  46  46  PHE PHE A . n 
A 1 55  HIS 55  47  47  HIS HIS A . n 
A 1 56  PRO 56  48  48  PRO PRO A . n 
A 1 57  ARG 57  49  49  ARG ARG A . n 
A 1 58  PHE 58  50  50  PHE PHE A . n 
A 1 59  LYS 59  51  51  LYS LYS A . n 
A 1 60  ARG 60  52  52  ARG ARG A . n 
A 1 61  GLU 61  53  53  GLU GLU A . n 
A 1 62  PHE 62  54  54  PHE PHE A . n 
A 1 63  ILE 63  55  55  ILE ILE A . n 
A 1 64  GLN 64  56  56  GLN GLN A . n 
A 1 65  GLU 65  57  57  GLU GLU A . n 
A 1 66  PRO 66  58  58  PRO PRO A . n 
A 1 67  ALA 67  59  59  ALA ALA A . n 
A 1 68  LYS 68  60  60  LYS LYS A . n 
A 1 69  ASN 69  61  61  ASN ASN A . n 
A 1 70  ARG 70  62  62  ARG ARG A . n 
A 1 71  PRO 71  63  63  PRO PRO A . n 
A 1 72  GLY 72  64  64  GLY GLY A . n 
A 1 73  PRO 73  65  65  PRO PRO A . n 
A 1 74  GLN 74  66  66  GLN GLN A . n 
A 1 75  THR 75  67  67  THR THR A . n 
A 1 76  ARG 76  68  68  ARG ARG A . n 
A 1 77  SER 77  69  69  SER SER A . n 
A 1 78  ASP 78  70  70  ASP ASP A . n 
A 1 79  LEU 79  71  71  LEU LEU A . n 
A 1 80  LEU 80  72  72  LEU LEU A . n 
A 1 81  LEU 81  73  73  LEU LEU A . n 
A 1 82  SER 82  74  74  SER SER A . n 
A 1 83  GLY 83  75  75  GLY GLY A . n 
A 1 84  ARG 84  76  76  ARG ARG A . n 
A 1 85  ASP 85  77  77  ASP ASP A . n 
A 1 86  TRP 86  78  78  TRP TRP A . n 
A 1 87  ASN 87  79  79  ASN ASN A . n 
A 1 88  THR 88  80  80  THR THR A . n 
A 1 89  LEU 89  81  81  LEU LEU A . n 
A 1 90  ILE 90  82  82  ILE ILE A . n 
A 1 91  VAL 91  83  83  VAL VAL A . n 
A 1 92  GLY 92  84  84  GLY GLY A . n 
A 1 93  LYS 93  85  85  LYS LYS A . n 
A 1 94  LEU 94  86  86  LEU LEU A . n 
A 1 95  SER 95  87  87  SER SER A . n 
A 1 96  PRO 96  88  88  PRO PRO A . n 
A 1 97  TRP 97  89  89  TRP TRP A . n 
A 1 98  ILE 98  90  90  ILE ILE A . n 
A 1 99  ARG 99  91  91  ARG ARG A . n 
A 1 100 PRO 100 92  92  PRO PRO A . n 
A 1 101 ASP 101 93  93  ASP ASP A . n 
A 1 102 SER 102 94  94  SER SER A . n 
A 1 103 LYS 103 95  95  LYS LYS A . n 
A 1 104 VAL 104 96  96  VAL VAL A . n 
A 1 105 GLU 105 97  97  GLU GLU A . n 
A 1 106 LYS 106 98  98  LYS LYS A . n 
A 1 107 ILE 107 99  99  ILE ILE A . n 
A 1 108 ARG 108 100 100 ARG ARG A . n 
A 1 109 ARG 109 101 101 ARG ARG A . n 
A 1 110 ASN 110 102 102 ASN ASN A . n 
A 1 111 SER 111 103 103 SER SER A . n 
A 1 112 GLU 112 104 104 GLU GLU A . n 
A 1 113 ALA 113 105 105 ALA ALA A . n 
A 1 114 ALA 114 106 106 ALA ALA A . n 
A 1 115 MET 115 107 107 MET MET A . n 
A 1 116 LEU 116 108 108 LEU LEU A . n 
A 1 117 GLN 117 109 109 GLN GLN A . n 
A 1 118 GLU 118 110 110 GLU GLU A . n 
A 1 119 LEU 119 111 111 LEU LEU A . n 
A 1 120 ASN 120 112 112 ASN ASN A . n 
A 1 121 PHE 121 113 113 PHE PHE A . n 
A 1 122 GLY 122 114 114 GLY GLY A . n 
A 1 123 ALA 123 115 115 ALA ALA A . n 
A 1 124 TYR 124 116 116 TYR TYR A . n 
A 1 125 LEU 125 117 117 LEU LEU A . n 
A 1 126 GLY 126 118 118 GLY GLY A . n 
A 1 127 LEU 127 119 119 LEU LEU A . n 
A 1 128 PRO 128 120 120 PRO PRO A . n 
A 1 129 ALA 129 121 121 ALA ALA A . n 
A 1 130 PHE 130 122 122 PHE PHE A . n 
A 1 131 LEU 131 123 123 LEU LEU A . n 
A 1 132 LEU 132 124 124 LEU LEU A . n 
A 1 133 PRO 133 125 125 PRO PRO A . n 
A 1 134 LEU 134 126 126 LEU LEU A . n 
A 1 135 ASN 135 127 127 ASN ASN A . n 
A 1 136 GLN 136 128 128 GLN GLN A . n 
A 1 137 GLU 137 129 129 GLU GLU A . n 
A 1 138 ASP 138 130 130 ASP ASP A . n 
A 1 139 ASN 139 131 131 ASN ASN A . n 
A 1 140 THR 140 132 132 THR THR A . n 
A 1 141 ASN 141 133 133 ASN ASN A . n 
A 1 142 LEU 142 134 134 LEU LEU A . n 
A 1 143 ALA 143 135 135 ALA ALA A . n 
A 1 144 ARG 144 136 136 ARG ARG A . n 
A 1 145 VAL 145 137 137 VAL VAL A . n 
A 1 146 LEU 146 138 138 LEU LEU A . n 
A 1 147 THR 147 139 139 THR THR A . n 
A 1 148 ASN 148 140 140 ASN ASN A . n 
A 1 149 HIS 149 141 141 HIS HIS A . n 
A 1 150 ILE 150 142 142 ILE ILE A . n 
A 1 151 HIS 151 143 143 HIS HIS A . n 
A 1 152 THR 152 144 144 THR THR A . n 
A 1 153 GLY 153 145 145 GLY GLY A . n 
A 1 154 HIS 154 146 146 HIS HIS A . n 
A 1 155 HIS 155 147 147 HIS HIS A . n 
A 1 156 SER 156 148 148 SER SER A . n 
A 1 157 SER 157 149 149 SER SER A . n 
A 1 158 MET 158 150 150 MET MET A . n 
A 1 159 PHE 159 151 151 PHE PHE A . n 
A 1 160 TRP 160 152 152 TRP TRP A . n 
A 1 161 MET 161 153 153 MET MET A . n 
A 1 162 ARG 162 154 154 ARG ARG A . n 
A 1 163 VAL 163 155 155 VAL VAL A . n 
A 1 164 PRO 164 156 156 PRO PRO A . n 
A 1 165 LEU 165 157 157 LEU LEU A . n 
A 1 166 VAL 166 158 158 VAL VAL A . n 
A 1 167 ALA 167 159 159 ALA ALA A . n 
A 1 168 PRO 168 160 160 PRO PRO A . n 
A 1 169 GLU 169 161 161 GLU GLU A . n 
A 1 170 ASP 170 162 162 ASP ASP A . n 
A 1 171 LEU 171 163 163 LEU LEU A . n 
A 1 172 ARG 172 164 164 ARG ARG A . n 
A 1 173 ASP 173 165 165 ASP ASP A . n 
A 1 174 ASP 174 166 166 ASP ASP A . n 
A 1 175 ILE 175 167 167 ILE ILE A . n 
A 1 176 ILE 176 168 168 ILE ILE A . n 
A 1 177 GLU 177 169 169 GLU GLU A . n 
A 1 178 ASN 178 170 170 ASN ASN A . n 
A 1 179 ALA 179 171 171 ALA ALA A . n 
A 1 180 PRO 180 172 172 PRO PRO A . n 
A 1 181 THR 181 173 173 THR THR A . n 
A 1 182 THR 182 174 174 THR THR A . n 
A 1 183 HIS 183 175 175 HIS HIS A . n 
A 1 184 THR 184 176 176 THR THR A . n 
A 1 185 GLU 185 177 177 GLU GLU A . n 
A 1 186 GLU 186 178 178 GLU GLU A . n 
A 1 187 TYR 187 179 179 TYR TYR A . n 
A 1 188 SER 188 180 180 SER SER A . n 
A 1 189 GLY 189 181 181 GLY GLY A . n 
A 1 190 GLU 190 182 182 GLU GLU A . n 
A 1 191 GLU 191 183 183 GLU GLU A . n 
A 1 192 LYS 192 184 184 LYS LYS A . n 
A 1 193 THR 193 185 185 THR THR A . n 
A 1 194 TRP 194 186 186 TRP TRP A . n 
A 1 195 MET 195 187 187 MET MET A . n 
A 1 196 TRP 196 188 188 TRP TRP A . n 
A 1 197 TRP 197 189 189 TRP TRP A . n 
A 1 198 HIS 198 190 190 HIS HIS A . n 
A 1 199 ASN 199 191 191 ASN ASN A . n 
A 1 200 PHE 200 192 192 PHE PHE A . n 
A 1 201 ARG 201 193 193 ARG ARG A . n 
A 1 202 THR 202 194 194 THR THR A . n 
A 1 203 LEU 203 195 195 LEU LEU A . n 
A 1 204 CYS 204 196 196 CYS CYS A . n 
A 1 205 ASP 205 197 197 ASP ASP A . n 
A 1 206 TYR 206 198 198 TYR TYR A . n 
A 1 207 SER 207 199 199 SER SER A . n 
A 1 208 LYS 208 200 200 LYS LYS A . n 
A 1 209 ARG 209 201 201 ARG ARG A . n 
A 1 210 ILE 210 202 202 ILE ILE A . n 
A 1 211 ALA 211 203 203 ALA ALA A . n 
A 1 212 VAL 212 204 204 VAL VAL A . n 
A 1 213 ALA 213 205 205 ALA ALA A . n 
A 1 214 LEU 214 206 206 LEU LEU A . n 
A 1 215 GLU 215 207 207 GLU GLU A . n 
A 1 216 ILE 216 208 208 ILE ILE A . n 
A 1 217 GLY 217 209 209 GLY GLY A . n 
A 1 218 ALA 218 210 210 ALA ALA A . n 
A 1 219 ASP 219 211 211 ASP ASP A . n 
A 1 220 LEU 220 212 212 LEU LEU A . n 
A 1 221 PRO 221 213 213 PRO PRO A . n 
A 1 222 SER 222 214 214 SER SER A . n 
A 1 223 ASN 223 215 215 ASN ASN A . n 
A 1 224 HIS 224 216 216 HIS HIS A . n 
A 1 225 VAL 225 217 217 VAL VAL A . n 
A 1 226 ILE 226 218 218 ILE ILE A . n 
A 1 227 ASP 227 219 219 ASP ASP A . n 
A 1 228 ARG 228 220 220 ARG ARG A . n 
A 1 229 TRP 229 221 221 TRP TRP A . n 
A 1 230 LEU 230 222 222 LEU LEU A . n 
A 1 231 GLY 231 223 223 GLY GLY A . n 
A 1 232 GLU 232 224 224 GLU GLU A . n 
A 1 233 PRO 233 225 225 PRO PRO A . n 
A 1 234 ILE 234 226 226 ILE ILE A . n 
A 1 235 LYS 235 227 227 LYS LYS A . n 
A 1 236 ALA 236 228 228 ALA ALA A . n 
A 1 237 ALA 237 229 229 ALA ALA A . n 
A 1 238 ILE 238 230 230 ILE ILE A . n 
A 1 239 LEU 239 231 231 LEU LEU A . n 
A 1 240 PRO 240 232 232 PRO PRO A . n 
A 1 241 THR 241 233 233 THR THR A . n 
A 1 242 SER 242 234 234 SER SER A . n 
A 1 243 ILE 243 235 235 ILE ILE A . n 
A 1 244 PHE 244 236 236 PHE PHE A . n 
A 1 245 LEU 245 237 237 LEU LEU A . n 
A 1 246 THR 246 238 238 THR THR A . n 
A 1 247 ASN 247 239 239 ASN ASN A . n 
A 1 248 LYS 248 240 240 LYS LYS A . n 
A 1 249 LYS 249 241 241 LYS LYS A . n 
A 1 250 GLY 250 242 242 GLY GLY A . n 
A 1 251 PHE 251 243 243 PHE PHE A . n 
A 1 252 PRO 252 244 244 PRO PRO A . n 
A 1 253 VAL 253 245 245 VAL VAL A . n 
A 1 254 LEU 254 246 246 LEU LEU A . n 
A 1 255 SER 255 247 247 SER SER A . n 
A 1 256 LYS 256 248 248 LYS LYS A . n 
A 1 257 MET 257 249 249 MET MET A . n 
A 1 258 HIS 258 250 250 HIS HIS A . n 
A 1 259 GLN 259 251 251 GLN GLN A . n 
A 1 260 ARG 260 252 252 ARG ARG A . n 
A 1 261 LEU 261 253 253 LEU LEU A . n 
A 1 262 ILE 262 254 254 ILE ILE A . n 
A 1 263 PHE 263 255 255 PHE PHE A . n 
A 1 264 ARG 264 256 256 ARG ARG A . n 
A 1 265 LEU 265 257 257 LEU LEU A . n 
A 1 266 LEU 266 258 258 LEU LEU A . n 
A 1 267 LYS 267 259 259 LYS LYS A . n 
A 1 268 LEU 268 260 260 LEU LEU A . n 
A 1 269 GLU 269 261 261 GLU GLU A . n 
A 1 270 VAL 270 262 262 VAL VAL A . n 
A 1 271 GLN 271 263 263 GLN GLN A . n 
A 1 272 PHE 272 264 264 PHE PHE A . n 
A 1 273 ILE 273 265 265 ILE ILE A . n 
A 1 274 ILE 274 266 266 ILE ILE A . n 
A 1 275 THR 275 267 267 THR THR A . n 
A 1 276 GLY 276 268 268 GLY GLY A . n 
A 1 277 THR 277 269 269 THR THR A . n 
A 1 278 ASN 278 270 270 ASN ASN A . n 
A 1 279 HIS 279 271 271 HIS HIS A . n 
A 1 280 HIS 280 272 272 HIS HIS A . n 
A 1 281 SER 281 273 273 SER SER A . n 
A 1 282 GLU 282 274 274 GLU GLU A . n 
A 1 283 LYS 283 275 275 LYS LYS A . n 
A 1 284 GLU 284 276 276 GLU GLU A . n 
A 1 285 PHE 285 277 277 PHE PHE A . n 
A 1 286 CYS 286 278 278 CYS CYS A . n 
A 1 287 SER 287 279 279 SER SER A . n 
A 1 288 TYR 288 280 280 TYR TYR A . n 
A 1 289 LEU 289 281 281 LEU LEU A . n 
A 1 290 GLN 290 282 282 GLN GLN A . n 
A 1 291 TYR 291 283 283 TYR TYR A . n 
A 1 292 LEU 292 284 284 LEU LEU A . n 
A 1 293 GLU 293 285 285 GLU GLU A . n 
A 1 294 TYR 294 286 286 TYR TYR A . n 
A 1 295 LEU 295 287 287 LEU LEU A . n 
A 1 296 SER 296 288 288 SER SER A . n 
A 1 297 GLN 297 289 289 GLN GLN A . n 
A 1 298 ASN 298 290 290 ASN ASN A . n 
A 1 299 ARG 299 291 291 ARG ARG A . n 
A 1 300 PRO 300 292 292 PRO PRO A . n 
A 1 301 PRO 301 293 293 PRO PRO A . n 
A 1 302 PRO 302 294 294 PRO PRO A . n 
A 1 303 ASN 303 295 295 ASN ASN A . n 
A 1 304 ALA 304 296 296 ALA ALA A . n 
A 1 305 TYR 305 297 297 TYR TYR A . n 
A 1 306 GLU 306 298 298 GLU GLU A . n 
A 1 307 LEU 307 299 299 LEU LEU A . n 
A 1 308 PHE 308 300 300 PHE PHE A . n 
A 1 309 ALA 309 301 301 ALA ALA A . n 
A 1 310 LYS 310 302 302 LYS LYS A . n 
A 1 311 GLY 311 303 303 GLY GLY A . n 
A 1 312 TYR 312 304 304 TYR TYR A . n 
A 1 313 GLU 313 305 305 GLU GLU A . n 
A 1 314 ASP 314 306 306 ASP ASP A . n 
A 1 315 TYR 315 307 307 TYR TYR A . n 
A 1 316 LEU 316 308 308 LEU LEU A . n 
A 1 317 GLN 317 309 309 GLN GLN A . n 
A 1 318 SER 318 310 310 SER SER A . n 
A 1 319 PRO 319 311 311 PRO PRO A . n 
A 1 320 LEU 320 312 312 LEU LEU A . n 
A 1 321 GLN 321 313 313 GLN GLN A . n 
A 1 322 PRO 322 314 314 PRO PRO A . n 
A 1 323 LEU 323 315 315 LEU LEU A . n 
A 1 324 MET 324 316 316 MET MET A . n 
A 1 325 ASP 325 317 317 ASP ASP A . n 
A 1 326 ASN 326 318 318 ASN ASN A . n 
A 1 327 LEU 327 319 319 LEU LEU A . n 
A 1 328 GLU 328 320 320 GLU GLU A . n 
A 1 329 SER 329 321 321 SER SER A . n 
A 1 330 GLN 330 322 322 GLN GLN A . n 
A 1 331 THR 331 323 323 THR THR A . n 
A 1 332 TYR 332 324 324 TYR TYR A . n 
A 1 333 GLU 333 325 325 GLU GLU A . n 
A 1 334 VAL 334 326 326 VAL VAL A . n 
A 1 335 PHE 335 327 327 PHE PHE A . n 
A 1 336 GLU 336 328 328 GLU GLU A . n 
A 1 337 LYS 337 329 329 LYS LYS A . n 
A 1 338 ASP 338 330 330 ASP ASP A . n 
A 1 339 PRO 339 331 331 PRO PRO A . n 
A 1 340 ILE 340 332 332 ILE ILE A . n 
A 1 341 LYS 341 333 333 LYS LYS A . n 
A 1 342 TYR 342 334 334 TYR TYR A . n 
A 1 343 SER 343 335 335 SER SER A . n 
A 1 344 GLN 344 336 336 GLN GLN A . n 
A 1 345 TYR 345 337 337 TYR TYR A . n 
A 1 346 GLN 346 338 338 GLN GLN A . n 
A 1 347 GLN 347 339 339 GLN GLN A . n 
A 1 348 ALA 348 340 340 ALA ALA A . n 
A 1 349 ILE 349 341 341 ILE ILE A . n 
A 1 350 TYR 350 342 342 TYR TYR A . n 
A 1 351 LYS 351 343 343 LYS LYS A . n 
A 1 352 CYS 352 344 344 CYS CYS A . n 
A 1 353 LEU 353 345 345 LEU LEU A . n 
A 1 354 LEU 354 346 346 LEU LEU A . n 
A 1 355 ASP 355 347 347 ASP ASP A . n 
A 1 356 ARG 356 348 348 ARG ARG A . n 
A 1 357 VAL 357 349 349 VAL VAL A . n 
A 1 358 PRO 358 350 350 PRO PRO A . n 
A 1 359 GLU 359 351 351 GLU GLU A . n 
A 1 360 GLU 360 352 352 GLU GLU A . n 
A 1 361 GLU 361 353 353 GLU GLU A . n 
A 1 362 LYS 362 354 354 LYS LYS A . n 
A 1 363 ASP 363 355 355 ASP ASP A . n 
A 1 364 THR 364 356 356 THR THR A . n 
A 1 365 ASN 365 357 357 ASN ASN A . n 
A 1 366 VAL 366 358 358 VAL VAL A . n 
A 1 367 GLN 367 359 359 GLN GLN A . n 
A 1 368 VAL 368 360 360 VAL VAL A . n 
A 1 369 LEU 369 361 361 LEU LEU A . n 
A 1 370 MET 370 362 362 MET MET A . n 
A 1 371 VAL 371 363 363 VAL VAL A . n 
A 1 372 LEU 372 364 364 LEU LEU A . n 
A 1 373 GLY 373 365 365 GLY GLY A . n 
A 1 374 ALA 374 366 366 ALA ALA A . n 
A 1 375 GLY 375 367 367 GLY GLY A . n 
A 1 376 ARG 376 368 368 ARG ARG A . n 
A 1 377 GLY 377 369 369 GLY GLY A . n 
A 1 378 PRO 378 370 370 PRO PRO A . n 
A 1 379 LEU 379 371 371 LEU LEU A . n 
A 1 380 VAL 380 372 372 VAL VAL A . n 
A 1 381 ASN 381 373 373 ASN ASN A . n 
A 1 382 ALA 382 374 374 ALA ALA A . n 
A 1 383 SER 383 375 375 SER SER A . n 
A 1 384 LEU 384 376 376 LEU LEU A . n 
A 1 385 ARG 385 377 377 ARG ARG A . n 
A 1 386 ALA 386 378 378 ALA ALA A . n 
A 1 387 ALA 387 379 379 ALA ALA A . n 
A 1 388 LYS 388 380 380 LYS LYS A . n 
A 1 389 GLN 389 381 381 GLN GLN A . n 
A 1 390 ALA 390 382 382 ALA ALA A . n 
A 1 391 ASP 391 383 383 ASP ASP A . n 
A 1 392 ARG 392 384 384 ARG ARG A . n 
A 1 393 ARG 393 385 385 ARG ARG A . n 
A 1 394 ILE 394 386 386 ILE ILE A . n 
A 1 395 LYS 395 387 387 LYS LYS A . n 
A 1 396 LEU 396 388 388 LEU LEU A . n 
A 1 397 TYR 397 389 389 TYR TYR A . n 
A 1 398 ALA 398 390 390 ALA ALA A . n 
A 1 399 VAL 399 391 391 VAL VAL A . n 
A 1 400 GLU 400 392 392 GLU GLU A . n 
A 1 401 LYS 401 393 393 LYS LYS A . n 
A 1 402 ASN 402 394 394 ASN ASN A . n 
A 1 403 PRO 403 395 395 PRO PRO A . n 
A 1 404 ASN 404 396 396 ASN ASN A . n 
A 1 405 ALA 405 397 397 ALA ALA A . n 
A 1 406 VAL 406 398 398 VAL VAL A . n 
A 1 407 VAL 407 399 399 VAL VAL A . n 
A 1 408 THR 408 400 400 THR THR A . n 
A 1 409 LEU 409 401 401 LEU LEU A . n 
A 1 410 GLU 410 402 402 GLU GLU A . n 
A 1 411 ASN 411 403 403 ASN ASN A . n 
A 1 412 TRP 412 404 404 TRP TRP A . n 
A 1 413 GLN 413 405 405 GLN GLN A . n 
A 1 414 PHE 414 406 406 PHE PHE A . n 
A 1 415 GLU 415 407 407 GLU GLU A . n 
A 1 416 GLU 416 408 408 GLU GLU A . n 
A 1 417 TRP 417 409 409 TRP TRP A . n 
A 1 418 GLY 418 410 410 GLY GLY A . n 
A 1 419 SER 419 411 411 SER SER A . n 
A 1 420 GLN 420 412 412 GLN GLN A . n 
A 1 421 VAL 421 413 413 VAL VAL A . n 
A 1 422 THR 422 414 414 THR THR A . n 
A 1 423 VAL 423 415 415 VAL VAL A . n 
A 1 424 VAL 424 416 416 VAL VAL A . n 
A 1 425 SER 425 417 417 SER SER A . n 
A 1 426 SER 426 418 418 SER SER A . n 
A 1 427 ASP 427 419 419 ASP ASP A . n 
A 1 428 MET 428 420 420 MET MET A . n 
A 1 429 ARG 429 421 421 ARG ARG A . n 
A 1 430 GLU 430 422 422 GLU GLU A . n 
A 1 431 TRP 431 423 423 TRP TRP A . n 
A 1 432 VAL 432 424 424 VAL VAL A . n 
A 1 433 ALA 433 425 425 ALA ALA A . n 
A 1 434 PRO 434 426 426 PRO PRO A . n 
A 1 435 GLU 435 427 427 GLU GLU A . n 
A 1 436 LYS 436 428 428 LYS LYS A . n 
A 1 437 ALA 437 429 429 ALA ALA A . n 
A 1 438 ASP 438 430 430 ASP ASP A . n 
A 1 439 ILE 439 431 431 ILE ILE A . n 
A 1 440 ILE 440 432 432 ILE ILE A . n 
A 1 441 VAL 441 433 433 VAL VAL A . n 
A 1 442 SER 442 434 434 SER SER A . n 
A 1 443 GLU 443 435 435 GLU GLU A . n 
A 1 444 LEU 444 436 436 LEU LEU A . n 
A 1 445 LEU 445 437 437 LEU LEU A . n 
A 1 446 GLY 446 438 438 GLY GLY A . n 
A 1 447 SER 447 439 439 SER SER A . n 
A 1 448 PHE 448 440 440 PHE PHE A . n 
A 1 449 ALA 449 441 441 ALA ALA A . n 
A 1 450 ASP 450 442 442 ASP ASP A . n 
A 1 451 ASN 451 443 443 ASN ASN A . n 
A 1 452 GLU 452 444 444 GLU GLU A . n 
A 1 453 LEU 453 445 445 LEU LEU A . n 
A 1 454 SER 454 446 446 SER SER A . n 
A 1 455 PRO 455 447 447 PRO PRO A . n 
A 1 456 GLU 456 448 448 GLU GLU A . n 
A 1 457 CYS 457 449 449 CYS CYS A . n 
A 1 458 LEU 458 450 450 LEU LEU A . n 
A 1 459 ASP 459 451 451 ASP ASP A . n 
A 1 460 GLY 460 452 452 GLY GLY A . n 
A 1 461 ALA 461 453 453 ALA ALA A . n 
A 1 462 GLN 462 454 454 GLN GLN A . n 
A 1 463 HIS 463 455 455 HIS HIS A . n 
A 1 464 PHE 464 456 456 PHE PHE A . n 
A 1 465 LEU 465 457 457 LEU LEU A . n 
A 1 466 LYS 466 458 458 LYS LYS A . n 
A 1 467 ASP 467 459 459 ASP ASP A . n 
A 1 468 ASP 468 460 460 ASP ASP A . n 
A 1 469 GLY 469 461 461 GLY GLY A . n 
A 1 470 VAL 470 462 462 VAL VAL A . n 
A 1 471 SER 471 463 463 SER SER A . n 
A 1 472 ILE 472 464 464 ILE ILE A . n 
A 1 473 PRO 473 465 465 PRO PRO A . n 
A 1 474 GLY 474 466 466 GLY GLY A . n 
A 1 475 GLU 475 467 467 GLU GLU A . n 
A 1 476 TYR 476 468 468 TYR TYR A . n 
A 1 477 THR 477 469 469 THR THR A . n 
A 1 478 SER 478 470 470 SER SER A . n 
A 1 479 PHE 479 471 471 PHE PHE A . n 
A 1 480 LEU 480 472 472 LEU LEU A . n 
A 1 481 ALA 481 473 473 ALA ALA A . n 
A 1 482 PRO 482 474 474 PRO PRO A . n 
A 1 483 ILE 483 475 475 ILE ILE A . n 
A 1 484 SER 484 476 476 SER SER A . n 
A 1 485 SER 485 477 477 SER SER A . n 
A 1 486 SER 486 478 478 SER SER A . n 
A 1 487 LYS 487 479 479 LYS LYS A . n 
A 1 488 LEU 488 480 480 LEU LEU A . n 
A 1 489 TYR 489 481 481 TYR TYR A . n 
A 1 490 ASN 490 482 482 ASN ASN A . n 
A 1 491 GLU 491 483 483 GLU GLU A . n 
A 1 492 VAL 492 484 484 VAL VAL A . n 
A 1 493 ARG 493 485 485 ARG ARG A . n 
A 1 494 ALA 494 486 486 ALA ALA A . n 
A 1 495 CYS 495 487 487 CYS CYS A . n 
A 1 496 ARG 496 488 488 ARG ARG A . n 
A 1 497 GLU 497 489 489 GLU GLU A . n 
A 1 498 LYS 498 490 490 LYS LYS A . n 
A 1 499 ASP 499 491 491 ASP ASP A . n 
A 1 500 ARG 500 492 492 ARG ARG A . n 
A 1 501 ASP 501 493 493 ASP ASP A . n 
A 1 502 PRO 502 494 494 PRO PRO A . n 
A 1 503 GLU 503 495 495 GLU GLU A . n 
A 1 504 ALA 504 496 496 ALA ALA A . n 
A 1 505 GLN 505 497 497 GLN GLN A . n 
A 1 506 PHE 506 498 498 PHE PHE A . n 
A 1 507 GLU 507 499 499 GLU GLU A . n 
A 1 508 MET 508 500 500 MET MET A . n 
A 1 509 PRO 509 501 501 PRO PRO A . n 
A 1 510 TYR 510 502 502 TYR TYR A . n 
A 1 511 VAL 511 503 503 VAL VAL A . n 
A 1 512 VAL 512 504 504 VAL VAL A . n 
A 1 513 ARG 513 505 505 ARG ARG A . n 
A 1 514 LEU 514 506 506 LEU LEU A . n 
A 1 515 HIS 515 507 507 HIS HIS A . n 
A 1 516 ASN 516 508 508 ASN ASN A . n 
A 1 517 PHE 517 509 509 PHE PHE A . n 
A 1 518 HIS 518 510 510 HIS HIS A . n 
A 1 519 GLN 519 511 511 GLN GLN A . n 
A 1 520 LEU 520 512 512 LEU LEU A . n 
A 1 521 SER 521 513 513 SER SER A . n 
A 1 522 ALA 522 514 514 ALA ALA A . n 
A 1 523 PRO 523 515 515 PRO PRO A . n 
A 1 524 GLN 524 516 516 GLN GLN A . n 
A 1 525 PRO 525 517 517 PRO PRO A . n 
A 1 526 CYS 526 518 518 CYS CYS A . n 
A 1 527 PHE 527 519 519 PHE PHE A . n 
A 1 528 THR 528 520 520 THR THR A . n 
A 1 529 PHE 529 521 521 PHE PHE A . n 
A 1 530 SER 530 522 522 SER SER A . n 
A 1 531 HIS 531 523 523 HIS HIS A . n 
A 1 532 PRO 532 524 524 PRO PRO A . n 
A 1 533 ASN 533 525 525 ASN ASN A . n 
A 1 534 ARG 534 526 526 ARG ARG A . n 
A 1 535 ASP 535 527 527 ASP ASP A . n 
A 1 536 PRO 536 528 528 PRO PRO A . n 
A 1 537 MET 537 529 529 MET MET A . n 
A 1 538 ILE 538 530 530 ILE ILE A . n 
A 1 539 ASP 539 531 531 ASP ASP A . n 
A 1 540 ASN 540 532 532 ASN ASN A . n 
A 1 541 ASN 541 533 533 ASN ASN A . n 
A 1 542 ARG 542 534 534 ARG ARG A . n 
A 1 543 TYR 543 535 535 TYR TYR A . n 
A 1 544 CYS 544 536 536 CYS CYS A . n 
A 1 545 THR 545 537 537 THR THR A . n 
A 1 546 LEU 546 538 538 LEU LEU A . n 
A 1 547 GLU 547 539 539 GLU GLU A . n 
A 1 548 PHE 548 540 540 PHE PHE A . n 
A 1 549 PRO 549 541 541 PRO PRO A . n 
A 1 550 VAL 550 542 542 VAL VAL A . n 
A 1 551 GLU 551 543 543 GLU GLU A . n 
A 1 552 VAL 552 544 544 VAL VAL A . n 
A 1 553 ASN 553 545 545 ASN ASN A . n 
A 1 554 THR 554 546 546 THR THR A . n 
A 1 555 VAL 555 547 547 VAL VAL A . n 
A 1 556 LEU 556 548 548 LEU LEU A . n 
A 1 557 HIS 557 549 549 HIS HIS A . n 
A 1 558 GLY 558 550 550 GLY GLY A . n 
A 1 559 PHE 559 551 551 PHE PHE A . n 
A 1 560 ALA 560 552 552 ALA ALA A . n 
A 1 561 GLY 561 553 553 GLY GLY A . n 
A 1 562 TYR 562 554 554 TYR TYR A . n 
A 1 563 PHE 563 555 555 PHE PHE A . n 
A 1 564 GLU 564 556 556 GLU GLU A . n 
A 1 565 THR 565 557 557 THR THR A . n 
A 1 566 VAL 566 558 558 VAL VAL A . n 
A 1 567 LEU 567 559 559 LEU LEU A . n 
A 1 568 TYR 568 560 560 TYR TYR A . n 
A 1 569 GLN 569 561 561 GLN GLN A . n 
A 1 570 ASP 570 562 562 ASP ASP A . n 
A 1 571 ILE 571 563 563 ILE ILE A . n 
A 1 572 THR 572 564 564 THR THR A . n 
A 1 573 LEU 573 565 565 LEU LEU A . n 
A 1 574 SER 574 566 566 SER SER A . n 
A 1 575 ILE 575 567 567 ILE ILE A . n 
A 1 576 ARG 576 568 568 ARG ARG A . n 
A 1 577 PRO 577 569 569 PRO PRO A . n 
A 1 578 GLU 578 570 570 GLU GLU A . n 
A 1 579 THR 579 571 571 THR THR A . n 
A 1 580 HIS 580 572 572 HIS HIS A . n 
A 1 581 SER 581 573 573 SER SER A . n 
A 1 582 PRO 582 574 574 PRO PRO A . n 
A 1 583 GLY 583 575 575 GLY GLY A . n 
A 1 584 MET 584 576 576 MET MET A . n 
A 1 585 PHE 585 577 577 PHE PHE A . n 
A 1 586 SER 586 578 578 SER SER A . n 
A 1 587 TRP 587 579 579 TRP TRP A . n 
A 1 588 PHE 588 580 580 PHE PHE A . n 
A 1 589 PRO 589 581 581 PRO PRO A . n 
A 1 590 ILE 590 582 582 ILE ILE A . n 
A 1 591 LEU 591 583 583 LEU LEU A . n 
A 1 592 PHE 592 584 584 PHE PHE A . n 
A 1 593 PRO 593 585 585 PRO PRO A . n 
A 1 594 ILE 594 586 586 ILE ILE A . n 
A 1 595 LYS 595 587 587 LYS LYS A . n 
A 1 596 GLN 596 588 588 GLN GLN A . n 
A 1 597 PRO 597 589 589 PRO PRO A . n 
A 1 598 ILE 598 590 590 ILE ILE A . n 
A 1 599 THR 599 591 591 THR THR A . n 
A 1 600 VAL 600 592 592 VAL VAL A . n 
A 1 601 ARG 601 593 593 ARG ARG A . n 
A 1 602 GLU 602 594 594 GLU GLU A . n 
A 1 603 GLY 603 595 595 GLY GLY A . n 
A 1 604 GLN 604 596 596 GLN GLN A . n 
A 1 605 THR 605 597 597 THR THR A . n 
A 1 606 ILE 606 598 598 ILE ILE A . n 
A 1 607 CYS 607 599 599 CYS CYS A . n 
A 1 608 VAL 608 600 600 VAL VAL A . n 
A 1 609 ARG 609 601 601 ARG ARG A . n 
A 1 610 PHE 610 602 602 PHE PHE A . n 
A 1 611 TRP 611 603 603 TRP TRP A . n 
A 1 612 ARG 612 604 604 ARG ARG A . n 
A 1 613 CYS 613 605 605 CYS CYS A . n 
A 1 614 SER 614 606 606 SER SER A . n 
A 1 615 ASN 615 607 607 ASN ASN A . n 
A 1 616 SER 616 608 608 SER SER A . n 
A 1 617 LYS 617 609 609 LYS LYS A . n 
A 1 618 LYS 618 610 610 LYS LYS A . n 
A 1 619 VAL 619 611 611 VAL VAL A . n 
A 1 620 TRP 620 612 612 TRP TRP A . n 
A 1 621 TYR 621 613 613 TYR TYR A . n 
A 1 622 GLU 622 614 614 GLU GLU A . n 
A 1 623 TRP 623 615 615 TRP TRP A . n 
A 1 624 ALA 624 616 616 ALA ALA A . n 
A 1 625 VAL 625 617 617 VAL VAL A . n 
A 1 626 THR 626 618 618 THR THR A . n 
A 1 627 ALA 627 619 619 ALA ALA A . n 
A 1 628 PRO 628 620 620 PRO PRO A . n 
A 1 629 VAL 629 621 621 VAL VAL A . n 
A 1 630 CYS 630 622 622 CYS CYS A . n 
A 1 631 SER 631 623 623 SER SER A . n 
A 1 632 ALA 632 624 624 ALA ALA A . n 
A 1 633 ILE 633 625 625 ILE ILE A . n 
A 1 634 HIS 634 626 626 HIS HIS A . n 
A 1 635 ASN 635 627 627 ASN ASN A . n 
A 1 636 PRO 636 628 628 PRO PRO A . n 
A 1 637 THR 637 629 629 THR THR A . n 
A 1 638 GLY 638 630 630 GLY GLY A . n 
A 1 639 ARG 639 631 631 ARG ARG A . n 
A 1 640 SER 640 632 632 SER SER A . n 
A 1 641 TYR 641 633 633 TYR TYR A . n 
A 1 642 THR 642 634 634 THR THR A . n 
A 1 643 ILE 643 635 635 ILE ILE A . n 
A 1 644 GLY 644 636 636 GLY GLY A . n 
A 1 645 LEU 645 637 637 LEU LEU A . n 
B 2 1   MET 1   -7  ?   ?   ?   B . n 
B 2 2   HIS 2   -6  ?   ?   ?   B . n 
B 2 3   HIS 3   -5  ?   ?   ?   B . n 
B 2 4   HIS 4   -4  ?   ?   ?   B . n 
B 2 5   HIS 5   -3  ?   ?   ?   B . n 
B 2 6   HIS 6   -2  ?   ?   ?   B . n 
B 2 7   HIS 7   -1  ?   ?   ?   B . n 
B 2 8   HIS 8   0   ?   ?   ?   B . n 
B 2 9   HIS 9   1   ?   ?   ?   B . n 
B 2 10  ARG 10  2   ?   ?   ?   B . n 
B 2 11  LYS 11  3   ?   ?   ?   B . n 
B 2 12  GLU 12  4   ?   ?   ?   B . n 
B 2 13  THR 13  5   ?   ?   ?   B . n 
B 2 14  PRO 14  6   ?   ?   ?   B . n 
B 2 15  PRO 15  7   ?   ?   ?   B . n 
B 2 16  PRO 16  8   ?   ?   ?   B . n 
B 2 17  LEU 17  9   ?   ?   ?   B . n 
B 2 18  VAL 18  10  ?   ?   ?   B . n 
B 2 19  PRO 19  11  ?   ?   ?   B . n 
B 2 20  PRO 20  12  ?   ?   ?   B . n 
B 2 21  ALA 21  13  ?   ?   ?   B . n 
B 2 22  ALA 22  14  ?   ?   ?   B . n 
B 2 23  ARG 23  15  ?   ?   ?   B . n 
B 2 24  GLU 24  16  ?   ?   ?   B . n 
B 2 25  TRP 25  17  ?   ?   ?   B . n 
B 2 26  ASN 26  18  ?   ?   ?   B . n 
B 2 27  LEU 27  19  ?   ?   ?   B . n 
B 2 28  PRO 28  20  20  PRO PRO B . n 
B 2 29  PRO 29  21  21  PRO PRO B . n 
B 2 30  ASN 30  22  22  ASN ASN B . n 
B 2 31  ALA 31  23  23  ALA ALA B . n 
B 2 32  PRO 32  24  24  PRO PRO B . n 
B 2 33  ALA 33  25  25  ALA ALA B . n 
B 2 34  CYS 34  26  26  CYS CYS B . n 
B 2 35  MET 35  27  27  MET MET B . n 
B 2 36  GLU 36  28  28  GLU GLU B . n 
B 2 37  ARG 37  29  29  ARG ARG B . n 
B 2 38  GLN 38  30  30  GLN GLN B . n 
B 2 39  LEU 39  31  31  LEU LEU B . n 
B 2 40  GLU 40  32  32  GLU GLU B . n 
B 2 41  ALA 41  33  33  ALA ALA B . n 
B 2 42  ALA 42  34  34  ALA ALA B . n 
B 2 43  ARG 43  35  35  ARG ARG B . n 
B 2 44  TYR 44  36  36  TYR TYR B . n 
B 2 45  ARG 45  37  37  ARG ARG B . n 
B 2 46  SER 46  38  38  SER SER B . n 
B 2 47  ASP 47  39  39  ASP ASP B . n 
B 2 48  GLY 48  40  40  GLY GLY B . n 
B 2 49  ALA 49  41  41  ALA ALA B . n 
B 2 50  LEU 50  42  42  LEU LEU B . n 
B 2 51  LEU 51  43  43  LEU LEU B . n 
B 2 52  LEU 52  44  44  LEU LEU B . n 
B 2 53  GLY 53  45  45  GLY GLY B . n 
B 2 54  ALA 54  46  46  ALA ALA B . n 
B 2 55  SER 55  47  47  SER SER B . n 
B 2 56  SER 56  48  48  SER SER B . n 
B 2 57  LEU 57  49  49  LEU LEU B . n 
B 2 58  SER 58  50  50  SER SER B . n 
B 2 59  GLY 59  51  51  GLY GLY B . n 
B 2 60  ARG 60  52  52  ARG ARG B . n 
B 2 61  CYS 61  53  53  CYS CYS B . n 
B 2 62  TRP 62  54  54  TRP TRP B . n 
B 2 63  ALA 63  55  55  ALA ALA B . n 
B 2 64  GLY 64  56  56  GLY GLY B . n 
B 2 65  SER 65  57  57  SER SER B . n 
B 2 66  LEU 66  58  58  LEU LEU B . n 
B 2 67  TRP 67  59  59  TRP TRP B . n 
B 2 68  LEU 68  60  60  LEU LEU B . n 
B 2 69  PHE 69  61  61  PHE PHE B . n 
B 2 70  LYS 70  62  62  LYS LYS B . n 
B 2 71  ASP 71  63  63  ASP ASP B . n 
B 2 72  PRO 72  64  64  PRO PRO B . n 
B 2 73  CYS 73  65  65  CYS CYS B . n 
B 2 74  ALA 74  66  66  ALA ALA B . n 
B 2 75  ALA 75  67  67  ALA ALA B . n 
B 2 76  PRO 76  68  68  PRO PRO B . n 
B 2 77  ASN 77  69  69  ASN ASN B . n 
B 2 78  GLU 78  70  70  GLU GLU B . n 
B 2 79  GLY 79  71  71  GLY GLY B . n 
B 2 80  PHE 80  72  72  PHE PHE B . n 
B 2 81  CYS 81  73  73  CYS CYS B . n 
B 2 82  SER 82  74  74  SER SER B . n 
B 2 83  ALA 83  75  75  ALA ALA B . n 
B 2 84  GLY 84  76  76  GLY GLY B . n 
B 2 85  VAL 85  77  77  VAL VAL B . n 
B 2 86  GLN 86  78  78  GLN GLN B . n 
B 2 87  THR 87  79  79  THR THR B . n 
B 2 88  GLU 88  80  80  GLU GLU B . n 
B 2 89  ALA 89  81  81  ALA ALA B . n 
B 2 90  GLY 90  82  82  GLY GLY B . n 
B 2 91  VAL 91  83  83  VAL VAL B . n 
B 2 92  ALA 92  84  84  ALA ALA B . n 
B 2 93  ASP 93  85  85  ASP ASP B . n 
B 2 94  LEU 94  86  86  LEU LEU B . n 
B 2 95  THR 95  87  87  THR THR B . n 
B 2 96  TRP 96  88  88  TRP TRP B . n 
B 2 97  VAL 97  89  89  VAL VAL B . n 
B 2 98  GLY 98  90  90  GLY GLY B . n 
B 2 99  GLU 99  91  91  GLU GLU B . n 
B 2 100 ARG 100 92  92  ARG ARG B . n 
B 2 101 GLY 101 93  93  GLY GLY B . n 
B 2 102 ILE 102 94  94  ILE ILE B . n 
B 2 103 LEU 103 95  95  LEU LEU B . n 
B 2 104 VAL 104 96  96  VAL VAL B . n 
B 2 105 ALA 105 97  97  ALA ALA B . n 
B 2 106 SER 106 98  98  SER SER B . n 
B 2 107 ASP 107 99  99  ASP ASP B . n 
B 2 108 SER 108 100 100 SER SER B . n 
B 2 109 GLY 109 101 101 GLY GLY B . n 
B 2 110 ALA 110 102 102 ALA ALA B . n 
B 2 111 VAL 111 103 103 VAL VAL B . n 
B 2 112 GLU 112 104 104 GLU GLU B . n 
B 2 113 LEU 113 105 105 LEU LEU B . n 
B 2 114 TRP 114 106 106 TRP TRP B . n 
B 2 115 GLU 115 107 107 GLU GLU B . n 
B 2 116 LEU 116 108 108 LEU LEU B . n 
B 2 117 ASP 117 109 109 ASP ASP B . n 
B 2 118 GLU 118 110 110 GLU GLU B . n 
B 2 119 ASN 119 111 111 ASN ASN B . n 
B 2 120 GLU 120 112 112 GLU GLU B . n 
B 2 121 THR 121 113 113 THR THR B . n 
B 2 122 LEU 122 114 114 LEU LEU B . n 
B 2 123 ILE 123 115 115 ILE ILE B . n 
B 2 124 VAL 124 116 116 VAL VAL B . n 
B 2 125 SER 125 117 117 SER SER B . n 
B 2 126 LYS 126 118 118 LYS LYS B . n 
B 2 127 PHE 127 119 119 PHE PHE B . n 
B 2 128 CYS 128 120 120 CYS CYS B . n 
B 2 129 LYS 129 121 121 LYS LYS B . n 
B 2 130 TYR 130 122 122 TYR TYR B . n 
B 2 131 GLU 131 123 123 GLU GLU B . n 
B 2 132 HIS 132 124 124 HIS HIS B . n 
B 2 133 ASP 133 125 125 ASP ASP B . n 
B 2 134 ASP 134 126 126 ASP ASP B . n 
B 2 135 ILE 135 127 127 ILE ILE B . n 
B 2 136 VAL 136 128 128 VAL VAL B . n 
B 2 137 SER 137 129 129 SER SER B . n 
B 2 138 THR 138 130 130 THR THR B . n 
B 2 139 VAL 139 131 131 VAL VAL B . n 
B 2 140 SER 140 132 132 SER SER B . n 
B 2 141 VAL 141 133 133 VAL VAL B . n 
B 2 142 LEU 142 134 134 LEU LEU B . n 
B 2 143 SER 143 135 135 SER SER B . n 
B 2 144 SER 144 136 136 SER SER B . n 
B 2 145 GLY 145 137 137 GLY GLY B . n 
B 2 146 THR 146 138 138 THR THR B . n 
B 2 147 GLN 147 139 139 GLN GLN B . n 
B 2 148 ALA 148 140 140 ALA ALA B . n 
B 2 149 VAL 149 141 141 VAL VAL B . n 
B 2 150 SER 150 142 142 SER SER B . n 
B 2 151 GLY 151 143 143 GLY GLY B . n 
B 2 152 SER 152 144 144 SER SER B . n 
B 2 153 LYS 153 145 145 LYS LYS B . n 
B 2 154 ASP 154 146 146 ASP ASP B . n 
B 2 155 ILE 155 147 147 ILE ILE B . n 
B 2 156 CYS 156 148 148 CYS CYS B . n 
B 2 157 ILE 157 149 149 ILE ILE B . n 
B 2 158 LYS 158 150 150 LYS LYS B . n 
B 2 159 VAL 159 151 151 VAL VAL B . n 
B 2 160 TRP 160 152 152 TRP TRP B . n 
B 2 161 ASP 161 153 153 ASP ASP B . n 
B 2 162 LEU 162 154 154 LEU LEU B . n 
B 2 163 ALA 163 155 155 ALA ALA B . n 
B 2 164 GLN 164 156 156 GLN GLN B . n 
B 2 165 GLN 165 157 157 GLN GLN B . n 
B 2 166 VAL 166 158 158 VAL VAL B . n 
B 2 167 VAL 167 159 159 VAL VAL B . n 
B 2 168 LEU 168 160 160 LEU LEU B . n 
B 2 169 SER 169 161 161 SER SER B . n 
B 2 170 SER 170 162 162 SER SER B . n 
B 2 171 TYR 171 163 163 TYR TYR B . n 
B 2 172 ARG 172 164 164 ARG ARG B . n 
B 2 173 ALA 173 165 165 ALA ALA B . n 
B 2 174 HIS 174 166 166 HIS HIS B . n 
B 2 175 ALA 175 167 167 ALA ALA B . n 
B 2 176 ALA 176 168 168 ALA ALA B . n 
B 2 177 GLN 177 169 169 GLN GLN B . n 
B 2 178 VAL 178 170 170 VAL VAL B . n 
B 2 179 THR 179 171 171 THR THR B . n 
B 2 180 CYS 180 172 172 CYS CYS B . n 
B 2 181 VAL 181 173 173 VAL VAL B . n 
B 2 182 ALA 182 174 174 ALA ALA B . n 
B 2 183 ALA 183 175 175 ALA ALA B . n 
B 2 184 SER 184 176 176 SER SER B . n 
B 2 185 PRO 185 177 177 PRO PRO B . n 
B 2 186 HIS 186 178 178 HIS HIS B . n 
B 2 187 LYS 187 179 179 LYS LYS B . n 
B 2 188 ASP 188 180 180 ASP ASP B . n 
B 2 189 SER 189 181 181 SER SER B . n 
B 2 190 VAL 190 182 182 VAL VAL B . n 
B 2 191 PHE 191 183 183 PHE PHE B . n 
B 2 192 LEU 192 184 184 LEU LEU B . n 
B 2 193 SER 193 185 185 SER SER B . n 
B 2 194 CYS 194 186 186 CYS CYS B . n 
B 2 195 SER 195 187 187 SER SER B . n 
B 2 196 GLU 196 188 188 GLU GLU B . n 
B 2 197 ASP 197 189 189 ASP ASP B . n 
B 2 198 ASN 198 190 190 ASN ASN B . n 
B 2 199 ARG 199 191 191 ARG ARG B . n 
B 2 200 ILE 200 192 192 ILE ILE B . n 
B 2 201 LEU 201 193 193 LEU LEU B . n 
B 2 202 LEU 202 194 194 LEU LEU B . n 
B 2 203 TRP 203 195 195 TRP TRP B . n 
B 2 204 ASP 204 196 196 ASP ASP B . n 
B 2 205 THR 205 197 197 THR THR B . n 
B 2 206 ARG 206 198 198 ARG ARG B . n 
B 2 207 CYS 207 199 199 CYS CYS B . n 
B 2 208 PRO 208 200 200 PRO PRO B . n 
B 2 209 LYS 209 201 201 LYS LYS B . n 
B 2 210 PRO 210 202 202 PRO PRO B . n 
B 2 211 ALA 211 203 203 ALA ALA B . n 
B 2 212 SER 212 204 204 SER SER B . n 
B 2 213 GLN 213 205 205 GLN GLN B . n 
B 2 214 ILE 214 206 206 ILE ILE B . n 
B 2 215 GLY 215 207 ?   ?   ?   B . n 
B 2 216 CYS 216 208 ?   ?   ?   B . n 
B 2 217 SER 217 209 ?   ?   ?   B . n 
B 2 218 ALA 218 210 210 ALA ALA B . n 
B 2 219 PRO 219 211 211 PRO PRO B . n 
B 2 220 GLY 220 212 212 GLY GLY B . n 
B 2 221 TYR 221 213 213 TYR TYR B . n 
B 2 222 LEU 222 214 214 LEU LEU B . n 
B 2 223 PRO 223 215 215 PRO PRO B . n 
B 2 224 THR 224 216 216 THR THR B . n 
B 2 225 SER 225 217 217 SER SER B . n 
B 2 226 LEU 226 218 218 LEU LEU B . n 
B 2 227 ALA 227 219 219 ALA ALA B . n 
B 2 228 TRP 228 220 220 TRP TRP B . n 
B 2 229 HIS 229 221 221 HIS HIS B . n 
B 2 230 PRO 230 222 222 PRO PRO B . n 
B 2 231 GLN 231 223 223 GLN GLN B . n 
B 2 232 GLN 232 224 224 GLN GLN B . n 
B 2 233 SER 233 225 225 SER SER B . n 
B 2 234 GLU 234 226 226 GLU GLU B . n 
B 2 235 VAL 235 227 227 VAL VAL B . n 
B 2 236 PHE 236 228 228 PHE PHE B . n 
B 2 237 VAL 237 229 229 VAL VAL B . n 
B 2 238 PHE 238 230 230 PHE PHE B . n 
B 2 239 GLY 239 231 231 GLY GLY B . n 
B 2 240 ASP 240 232 232 ASP ASP B . n 
B 2 241 GLU 241 233 233 GLU GLU B . n 
B 2 242 ASN 242 234 234 ASN ASN B . n 
B 2 243 GLY 243 235 235 GLY GLY B . n 
B 2 244 THR 244 236 236 THR THR B . n 
B 2 245 VAL 245 237 237 VAL VAL B . n 
B 2 246 SER 246 238 238 SER SER B . n 
B 2 247 LEU 247 239 239 LEU LEU B . n 
B 2 248 VAL 248 240 240 VAL VAL B . n 
B 2 249 ASP 249 241 241 ASP ASP B . n 
B 2 250 THR 250 242 242 THR THR B . n 
B 2 251 LYS 251 243 243 LYS LYS B . n 
B 2 252 SER 252 244 244 SER SER B . n 
B 2 253 THR 253 245 245 THR THR B . n 
B 2 254 SER 254 246 246 SER SER B . n 
B 2 255 CYS 255 247 247 CYS CYS B . n 
B 2 256 VAL 256 248 248 VAL VAL B . n 
B 2 257 LEU 257 249 249 LEU LEU B . n 
B 2 258 SER 258 250 250 SER SER B . n 
B 2 259 SER 259 251 251 SER SER B . n 
B 2 260 ALA 260 252 252 ALA ALA B . n 
B 2 261 VAL 261 253 253 VAL VAL B . n 
B 2 262 HIS 262 254 254 HIS HIS B . n 
B 2 263 SER 263 255 255 SER SER B . n 
B 2 264 GLN 264 256 256 GLN GLN B . n 
B 2 265 CYS 265 257 257 CYS CYS B . n 
B 2 266 VAL 266 258 258 VAL VAL B . n 
B 2 267 THR 267 259 259 THR THR B . n 
B 2 268 GLY 268 260 260 GLY GLY B . n 
B 2 269 LEU 269 261 261 LEU LEU B . n 
B 2 270 VAL 270 262 262 VAL VAL B . n 
B 2 271 PHE 271 263 263 PHE PHE B . n 
B 2 272 SER 272 264 264 SER SER B . n 
B 2 273 PRO 273 265 265 PRO PRO B . n 
B 2 274 HIS 274 266 266 HIS HIS B . n 
B 2 275 SER 275 267 267 SER SER B . n 
B 2 276 VAL 276 268 268 VAL VAL B . n 
B 2 277 PRO 277 269 269 PRO PRO B . n 
B 2 278 PHE 278 270 270 PHE PHE B . n 
B 2 279 LEU 279 271 271 LEU LEU B . n 
B 2 280 ALA 280 272 272 ALA ALA B . n 
B 2 281 SER 281 273 273 SER SER B . n 
B 2 282 LEU 282 274 274 LEU LEU B . n 
B 2 283 SER 283 275 275 SER SER B . n 
B 2 284 GLU 284 276 276 GLU GLU B . n 
B 2 285 ASP 285 277 277 ASP ASP B . n 
B 2 286 CYS 286 278 278 CYS CYS B . n 
B 2 287 SER 287 279 279 SER SER B . n 
B 2 288 LEU 288 280 280 LEU LEU B . n 
B 2 289 ALA 289 281 281 ALA ALA B . n 
B 2 290 VAL 290 282 282 VAL VAL B . n 
B 2 291 LEU 291 283 283 LEU LEU B . n 
B 2 292 ASP 292 284 284 ASP ASP B . n 
B 2 293 SER 293 285 285 SER SER B . n 
B 2 294 SER 294 286 286 SER SER B . n 
B 2 295 LEU 295 287 287 LEU LEU B . n 
B 2 296 SER 296 288 288 SER SER B . n 
B 2 297 GLU 297 289 289 GLU GLU B . n 
B 2 298 LEU 298 290 290 LEU LEU B . n 
B 2 299 PHE 299 291 291 PHE PHE B . n 
B 2 300 ARG 300 292 292 ARG ARG B . n 
B 2 301 SER 301 293 293 SER SER B . n 
B 2 302 GLN 302 294 294 GLN GLN B . n 
B 2 303 ALA 303 295 295 ALA ALA B . n 
B 2 304 HIS 304 296 296 HIS HIS B . n 
B 2 305 ARG 305 297 297 ARG ARG B . n 
B 2 306 ASP 306 298 298 ASP ASP B . n 
B 2 307 PHE 307 299 299 PHE PHE B . n 
B 2 308 VAL 308 300 300 VAL VAL B . n 
B 2 309 ARG 309 301 301 ARG ARG B . n 
B 2 310 ASP 310 302 302 ASP ASP B . n 
B 2 311 ALA 311 303 303 ALA ALA B . n 
B 2 312 THR 312 304 304 THR THR B . n 
B 2 313 TRP 313 305 305 TRP TRP B . n 
B 2 314 SER 314 306 306 SER SER B . n 
B 2 315 PRO 315 307 307 PRO PRO B . n 
B 2 316 LEU 316 308 308 LEU LEU B . n 
B 2 317 ASN 317 309 309 ASN ASN B . n 
B 2 318 HIS 318 310 310 HIS HIS B . n 
B 2 319 SER 319 311 311 SER SER B . n 
B 2 320 LEU 320 312 312 LEU LEU B . n 
B 2 321 LEU 321 313 313 LEU LEU B . n 
B 2 322 THR 322 314 314 THR THR B . n 
B 2 323 THR 323 315 315 THR THR B . n 
B 2 324 VAL 324 316 316 VAL VAL B . n 
B 2 325 GLY 325 317 317 GLY GLY B . n 
B 2 326 TRP 326 318 318 TRP TRP B . n 
B 2 327 ASP 327 319 319 ASP ASP B . n 
B 2 328 HIS 328 320 320 HIS HIS B . n 
B 2 329 GLN 329 321 321 GLN GLN B . n 
B 2 330 VAL 330 322 322 VAL VAL B . n 
B 2 331 VAL 331 323 323 VAL VAL B . n 
B 2 332 HIS 332 324 324 HIS HIS B . n 
B 2 333 HIS 333 325 325 HIS HIS B . n 
B 2 334 VAL 334 326 326 VAL VAL B . n 
B 2 335 VAL 335 327 327 VAL VAL B . n 
B 2 336 PRO 336 328 328 PRO PRO B . n 
B 2 337 THR 337 329 ?   ?   ?   B . n 
B 2 338 GLU 338 330 ?   ?   ?   B . n 
B 2 339 PRO 339 331 ?   ?   ?   B . n 
B 2 340 LEU 340 332 ?   ?   ?   B . n 
B 2 341 PRO 341 333 ?   ?   ?   B . n 
B 2 342 ALA 342 334 ?   ?   ?   B . n 
B 2 343 PRO 343 335 ?   ?   ?   B . n 
B 2 344 GLY 344 336 ?   ?   ?   B . n 
B 2 345 PRO 345 337 ?   ?   ?   B . n 
B 2 346 ALA 346 338 ?   ?   ?   B . n 
B 2 347 SER 347 339 ?   ?   ?   B . n 
B 2 348 VAL 348 340 ?   ?   ?   B . n 
B 2 349 THR 349 341 ?   ?   ?   B . n 
B 2 350 GLU 350 342 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BLG 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BLG 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C  3 SFG   1   701  1   SFG   SFG A . 
D  4 A1BLG 1   702  1   A1BLG 123 A . 
E  5 EDO   1   703  2   EDO   EDO A . 
F  5 EDO   1   704  3   EDO   EDO A . 
G  5 EDO   1   705  4   EDO   EDO A . 
H  5 EDO   1   706  5   EDO   EDO A . 
I  5 EDO   1   707  7   EDO   EDO A . 
J  5 EDO   1   708  8   EDO   EDO A . 
K  5 EDO   1   709  9   EDO   EDO A . 
L  5 EDO   1   710  10  EDO   EDO A . 
M  5 EDO   1   711  11  EDO   EDO A . 
N  5 EDO   1   712  12  EDO   EDO A . 
O  5 EDO   1   713  13  EDO   EDO A . 
P  5 EDO   1   714  14  EDO   EDO A . 
Q  5 EDO   1   715  16  EDO   EDO A . 
R  5 EDO   1   716  17  EDO   EDO A . 
S  5 EDO   1   717  19  EDO   EDO A . 
T  5 EDO   1   718  20  EDO   EDO A . 
U  5 EDO   1   719  21  EDO   EDO A . 
V  6 SO4   1   720  1   SO4   SO4 A . 
W  6 SO4   1   721  2   SO4   SO4 A . 
X  6 SO4   1   722  4   SO4   SO4 A . 
Y  6 SO4   1   723  5   SO4   SO4 A . 
Z  6 SO4   1   724  6   SO4   SO4 A . 
AA 6 SO4   1   725  7   SO4   SO4 A . 
BA 6 SO4   1   726  8   SO4   SO4 A . 
CA 7 PEG   1   727  1   PEG   PEG A . 
DA 7 PEG   1   728  2   PEG   PEG A . 
EA 7 PEG   1   729  3   PEG   PEG A . 
FA 5 EDO   1   401  6   EDO   EDO B . 
GA 5 EDO   1   402  15  EDO   EDO B . 
HA 6 SO4   1   403  3   SO4   SO4 B . 
IA 8 HOH   1   801  138 HOH   HOH A . 
IA 8 HOH   2   802  13  HOH   HOH A . 
IA 8 HOH   3   803  50  HOH   HOH A . 
IA 8 HOH   4   804  266 HOH   HOH A . 
IA 8 HOH   5   805  90  HOH   HOH A . 
IA 8 HOH   6   806  53  HOH   HOH A . 
IA 8 HOH   7   807  315 HOH   HOH A . 
IA 8 HOH   8   808  116 HOH   HOH A . 
IA 8 HOH   9   809  166 HOH   HOH A . 
IA 8 HOH   10  810  48  HOH   HOH A . 
IA 8 HOH   11  811  136 HOH   HOH A . 
IA 8 HOH   12  812  43  HOH   HOH A . 
IA 8 HOH   13  813  229 HOH   HOH A . 
IA 8 HOH   14  814  294 HOH   HOH A . 
IA 8 HOH   15  815  59  HOH   HOH A . 
IA 8 HOH   16  816  6   HOH   HOH A . 
IA 8 HOH   17  817  132 HOH   HOH A . 
IA 8 HOH   18  818  10  HOH   HOH A . 
IA 8 HOH   19  819  23  HOH   HOH A . 
IA 8 HOH   20  820  243 HOH   HOH A . 
IA 8 HOH   21  821  246 HOH   HOH A . 
IA 8 HOH   22  822  3   HOH   HOH A . 
IA 8 HOH   23  823  321 HOH   HOH A . 
IA 8 HOH   24  824  180 HOH   HOH A . 
IA 8 HOH   25  825  221 HOH   HOH A . 
IA 8 HOH   26  826  96  HOH   HOH A . 
IA 8 HOH   27  827  17  HOH   HOH A . 
IA 8 HOH   28  828  316 HOH   HOH A . 
IA 8 HOH   29  829  9   HOH   HOH A . 
IA 8 HOH   30  830  1   HOH   HOH A . 
IA 8 HOH   31  831  55  HOH   HOH A . 
IA 8 HOH   32  832  76  HOH   HOH A . 
IA 8 HOH   33  833  309 HOH   HOH A . 
IA 8 HOH   34  834  285 HOH   HOH A . 
IA 8 HOH   35  835  24  HOH   HOH A . 
IA 8 HOH   36  836  253 HOH   HOH A . 
IA 8 HOH   37  837  61  HOH   HOH A . 
IA 8 HOH   38  838  128 HOH   HOH A . 
IA 8 HOH   39  839  84  HOH   HOH A . 
IA 8 HOH   40  840  105 HOH   HOH A . 
IA 8 HOH   41  841  145 HOH   HOH A . 
IA 8 HOH   42  842  29  HOH   HOH A . 
IA 8 HOH   43  843  42  HOH   HOH A . 
IA 8 HOH   44  844  244 HOH   HOH A . 
IA 8 HOH   45  845  344 HOH   HOH A . 
IA 8 HOH   46  846  72  HOH   HOH A . 
IA 8 HOH   47  847  118 HOH   HOH A . 
IA 8 HOH   48  848  179 HOH   HOH A . 
IA 8 HOH   49  849  36  HOH   HOH A . 
IA 8 HOH   50  850  130 HOH   HOH A . 
IA 8 HOH   51  851  181 HOH   HOH A . 
IA 8 HOH   52  852  268 HOH   HOH A . 
IA 8 HOH   53  853  377 HOH   HOH A . 
IA 8 HOH   54  854  187 HOH   HOH A . 
IA 8 HOH   55  855  349 HOH   HOH A . 
IA 8 HOH   56  856  94  HOH   HOH A . 
IA 8 HOH   57  857  353 HOH   HOH A . 
IA 8 HOH   58  858  310 HOH   HOH A . 
IA 8 HOH   59  859  250 HOH   HOH A . 
IA 8 HOH   60  860  119 HOH   HOH A . 
IA 8 HOH   61  861  167 HOH   HOH A . 
IA 8 HOH   62  862  7   HOH   HOH A . 
IA 8 HOH   63  863  359 HOH   HOH A . 
IA 8 HOH   64  864  240 HOH   HOH A . 
IA 8 HOH   65  865  169 HOH   HOH A . 
IA 8 HOH   66  866  47  HOH   HOH A . 
IA 8 HOH   67  867  79  HOH   HOH A . 
IA 8 HOH   68  868  270 HOH   HOH A . 
IA 8 HOH   69  869  251 HOH   HOH A . 
IA 8 HOH   70  870  257 HOH   HOH A . 
IA 8 HOH   71  871  121 HOH   HOH A . 
IA 8 HOH   72  872  15  HOH   HOH A . 
IA 8 HOH   73  873  49  HOH   HOH A . 
IA 8 HOH   74  874  217 HOH   HOH A . 
IA 8 HOH   75  875  242 HOH   HOH A . 
IA 8 HOH   76  876  269 HOH   HOH A . 
IA 8 HOH   77  877  39  HOH   HOH A . 
IA 8 HOH   78  878  157 HOH   HOH A . 
IA 8 HOH   79  879  161 HOH   HOH A . 
IA 8 HOH   80  880  317 HOH   HOH A . 
IA 8 HOH   81  881  21  HOH   HOH A . 
IA 8 HOH   82  882  234 HOH   HOH A . 
IA 8 HOH   83  883  366 HOH   HOH A . 
IA 8 HOH   84  884  341 HOH   HOH A . 
IA 8 HOH   85  885  100 HOH   HOH A . 
IA 8 HOH   86  886  245 HOH   HOH A . 
IA 8 HOH   87  887  32  HOH   HOH A . 
IA 8 HOH   88  888  106 HOH   HOH A . 
IA 8 HOH   89  889  71  HOH   HOH A . 
IA 8 HOH   90  890  78  HOH   HOH A . 
IA 8 HOH   91  891  20  HOH   HOH A . 
IA 8 HOH   92  892  260 HOH   HOH A . 
IA 8 HOH   93  893  104 HOH   HOH A . 
IA 8 HOH   94  894  361 HOH   HOH A . 
IA 8 HOH   95  895  162 HOH   HOH A . 
IA 8 HOH   96  896  18  HOH   HOH A . 
IA 8 HOH   97  897  126 HOH   HOH A . 
IA 8 HOH   98  898  214 HOH   HOH A . 
IA 8 HOH   99  899  381 HOH   HOH A . 
IA 8 HOH   100 900  182 HOH   HOH A . 
IA 8 HOH   101 901  291 HOH   HOH A . 
IA 8 HOH   102 902  343 HOH   HOH A . 
IA 8 HOH   103 903  331 HOH   HOH A . 
IA 8 HOH   104 904  378 HOH   HOH A . 
IA 8 HOH   105 905  26  HOH   HOH A . 
IA 8 HOH   106 906  185 HOH   HOH A . 
IA 8 HOH   107 907  201 HOH   HOH A . 
IA 8 HOH   108 908  62  HOH   HOH A . 
IA 8 HOH   109 909  264 HOH   HOH A . 
IA 8 HOH   110 910  286 HOH   HOH A . 
IA 8 HOH   111 911  56  HOH   HOH A . 
IA 8 HOH   112 912  33  HOH   HOH A . 
IA 8 HOH   113 913  64  HOH   HOH A . 
IA 8 HOH   114 914  323 HOH   HOH A . 
IA 8 HOH   115 915  156 HOH   HOH A . 
IA 8 HOH   116 916  30  HOH   HOH A . 
IA 8 HOH   117 917  122 HOH   HOH A . 
IA 8 HOH   118 918  279 HOH   HOH A . 
IA 8 HOH   119 919  177 HOH   HOH A . 
IA 8 HOH   120 920  5   HOH   HOH A . 
IA 8 HOH   121 921  68  HOH   HOH A . 
IA 8 HOH   122 922  267 HOH   HOH A . 
IA 8 HOH   123 923  282 HOH   HOH A . 
IA 8 HOH   124 924  222 HOH   HOH A . 
IA 8 HOH   125 925  189 HOH   HOH A . 
IA 8 HOH   126 926  131 HOH   HOH A . 
IA 8 HOH   127 927  37  HOH   HOH A . 
IA 8 HOH   128 928  8   HOH   HOH A . 
IA 8 HOH   129 929  186 HOH   HOH A . 
IA 8 HOH   130 930  197 HOH   HOH A . 
IA 8 HOH   131 931  144 HOH   HOH A . 
IA 8 HOH   132 932  370 HOH   HOH A . 
IA 8 HOH   133 933  25  HOH   HOH A . 
IA 8 HOH   134 934  356 HOH   HOH A . 
IA 8 HOH   135 935  280 HOH   HOH A . 
IA 8 HOH   136 936  19  HOH   HOH A . 
IA 8 HOH   137 937  88  HOH   HOH A . 
IA 8 HOH   138 938  54  HOH   HOH A . 
IA 8 HOH   139 939  249 HOH   HOH A . 
IA 8 HOH   140 940  296 HOH   HOH A . 
IA 8 HOH   141 941  149 HOH   HOH A . 
IA 8 HOH   142 942  120 HOH   HOH A . 
IA 8 HOH   143 943  63  HOH   HOH A . 
IA 8 HOH   144 944  176 HOH   HOH A . 
IA 8 HOH   145 945  124 HOH   HOH A . 
IA 8 HOH   146 946  150 HOH   HOH A . 
IA 8 HOH   147 947  45  HOH   HOH A . 
IA 8 HOH   148 948  345 HOH   HOH A . 
IA 8 HOH   149 949  86  HOH   HOH A . 
IA 8 HOH   150 950  293 HOH   HOH A . 
IA 8 HOH   151 951  65  HOH   HOH A . 
IA 8 HOH   152 952  67  HOH   HOH A . 
IA 8 HOH   153 953  83  HOH   HOH A . 
IA 8 HOH   154 954  112 HOH   HOH A . 
IA 8 HOH   155 955  12  HOH   HOH A . 
IA 8 HOH   156 956  252 HOH   HOH A . 
IA 8 HOH   157 957  142 HOH   HOH A . 
IA 8 HOH   158 958  215 HOH   HOH A . 
IA 8 HOH   159 959  16  HOH   HOH A . 
IA 8 HOH   160 960  261 HOH   HOH A . 
IA 8 HOH   161 961  129 HOH   HOH A . 
IA 8 HOH   162 962  95  HOH   HOH A . 
IA 8 HOH   163 963  109 HOH   HOH A . 
IA 8 HOH   164 964  192 HOH   HOH A . 
IA 8 HOH   165 965  170 HOH   HOH A . 
IA 8 HOH   166 966  224 HOH   HOH A . 
IA 8 HOH   167 967  40  HOH   HOH A . 
IA 8 HOH   168 968  339 HOH   HOH A . 
IA 8 HOH   169 969  101 HOH   HOH A . 
IA 8 HOH   170 970  211 HOH   HOH A . 
IA 8 HOH   171 971  115 HOH   HOH A . 
IA 8 HOH   172 972  172 HOH   HOH A . 
IA 8 HOH   173 973  328 HOH   HOH A . 
IA 8 HOH   174 974  318 HOH   HOH A . 
IA 8 HOH   175 975  148 HOH   HOH A . 
IA 8 HOH   176 976  379 HOH   HOH A . 
IA 8 HOH   177 977  160 HOH   HOH A . 
IA 8 HOH   178 978  85  HOH   HOH A . 
IA 8 HOH   179 979  183 HOH   HOH A . 
IA 8 HOH   180 980  14  HOH   HOH A . 
IA 8 HOH   181 981  292 HOH   HOH A . 
IA 8 HOH   182 982  230 HOH   HOH A . 
IA 8 HOH   183 983  288 HOH   HOH A . 
IA 8 HOH   184 984  382 HOH   HOH A . 
IA 8 HOH   185 985  165 HOH   HOH A . 
IA 8 HOH   186 986  87  HOH   HOH A . 
IA 8 HOH   187 987  247 HOH   HOH A . 
IA 8 HOH   188 988  372 HOH   HOH A . 
IA 8 HOH   189 989  99  HOH   HOH A . 
IA 8 HOH   190 990  52  HOH   HOH A . 
IA 8 HOH   191 991  127 HOH   HOH A . 
IA 8 HOH   192 992  38  HOH   HOH A . 
IA 8 HOH   193 993  193 HOH   HOH A . 
IA 8 HOH   194 994  239 HOH   HOH A . 
IA 8 HOH   195 995  35  HOH   HOH A . 
IA 8 HOH   196 996  46  HOH   HOH A . 
IA 8 HOH   197 997  355 HOH   HOH A . 
IA 8 HOH   198 998  218 HOH   HOH A . 
IA 8 HOH   199 999  351 HOH   HOH A . 
IA 8 HOH   200 1000 301 HOH   HOH A . 
IA 8 HOH   201 1001 284 HOH   HOH A . 
IA 8 HOH   202 1002 380 HOH   HOH A . 
IA 8 HOH   203 1003 216 HOH   HOH A . 
IA 8 HOH   204 1004 28  HOH   HOH A . 
IA 8 HOH   205 1005 265 HOH   HOH A . 
IA 8 HOH   206 1006 41  HOH   HOH A . 
IA 8 HOH   207 1007 346 HOH   HOH A . 
IA 8 HOH   208 1008 302 HOH   HOH A . 
IA 8 HOH   209 1009 298 HOH   HOH A . 
IA 8 HOH   210 1010 307 HOH   HOH A . 
IA 8 HOH   211 1011 139 HOH   HOH A . 
IA 8 HOH   212 1012 363 HOH   HOH A . 
IA 8 HOH   213 1013 275 HOH   HOH A . 
IA 8 HOH   214 1014 263 HOH   HOH A . 
IA 8 HOH   215 1015 365 HOH   HOH A . 
IA 8 HOH   216 1016 175 HOH   HOH A . 
IA 8 HOH   217 1017 395 HOH   HOH A . 
IA 8 HOH   218 1018 147 HOH   HOH A . 
IA 8 HOH   219 1019 108 HOH   HOH A . 
IA 8 HOH   220 1020 376 HOH   HOH A . 
IA 8 HOH   221 1021 256 HOH   HOH A . 
IA 8 HOH   222 1022 2   HOH   HOH A . 
IA 8 HOH   223 1023 287 HOH   HOH A . 
IA 8 HOH   224 1024 281 HOH   HOH A . 
IA 8 HOH   225 1025 97  HOH   HOH A . 
IA 8 HOH   226 1026 290 HOH   HOH A . 
IA 8 HOH   227 1027 322 HOH   HOH A . 
IA 8 HOH   228 1028 98  HOH   HOH A . 
IA 8 HOH   229 1029 254 HOH   HOH A . 
IA 8 HOH   230 1030 362 HOH   HOH A . 
IA 8 HOH   231 1031 272 HOH   HOH A . 
IA 8 HOH   232 1032 364 HOH   HOH A . 
IA 8 HOH   233 1033 44  HOH   HOH A . 
IA 8 HOH   234 1034 202 HOH   HOH A . 
IA 8 HOH   235 1035 89  HOH   HOH A . 
IA 8 HOH   236 1036 103 HOH   HOH A . 
IA 8 HOH   237 1037 92  HOH   HOH A . 
IA 8 HOH   238 1038 143 HOH   HOH A . 
IA 8 HOH   239 1039 58  HOH   HOH A . 
IA 8 HOH   240 1040 173 HOH   HOH A . 
IA 8 HOH   241 1041 73  HOH   HOH A . 
IA 8 HOH   242 1042 200 HOH   HOH A . 
IA 8 HOH   243 1043 203 HOH   HOH A . 
IA 8 HOH   244 1044 137 HOH   HOH A . 
IA 8 HOH   245 1045 354 HOH   HOH A . 
IA 8 HOH   246 1046 233 HOH   HOH A . 
IA 8 HOH   247 1047 135 HOH   HOH A . 
IA 8 HOH   248 1048 371 HOH   HOH A . 
IA 8 HOH   249 1049 340 HOH   HOH A . 
IA 8 HOH   250 1050 111 HOH   HOH A . 
IA 8 HOH   251 1051 305 HOH   HOH A . 
IA 8 HOH   252 1052 273 HOH   HOH A . 
IA 8 HOH   253 1053 134 HOH   HOH A . 
IA 8 HOH   254 1054 357 HOH   HOH A . 
IA 8 HOH   255 1055 332 HOH   HOH A . 
IA 8 HOH   256 1056 374 HOH   HOH A . 
IA 8 HOH   257 1057 368 HOH   HOH A . 
IA 8 HOH   258 1058 375 HOH   HOH A . 
IA 8 HOH   259 1059 373 HOH   HOH A . 
IA 8 HOH   260 1060 174 HOH   HOH A . 
IA 8 HOH   261 1061 271 HOH   HOH A . 
IA 8 HOH   262 1062 141 HOH   HOH A . 
IA 8 HOH   263 1063 338 HOH   HOH A . 
IA 8 HOH   264 1064 369 HOH   HOH A . 
IA 8 HOH   265 1065 228 HOH   HOH A . 
IA 8 HOH   266 1066 358 HOH   HOH A . 
IA 8 HOH   267 1067 342 HOH   HOH A . 
IA 8 HOH   268 1068 125 HOH   HOH A . 
IA 8 HOH   269 1069 102 HOH   HOH A . 
IA 8 HOH   270 1070 329 HOH   HOH A . 
IA 8 HOH   271 1071 350 HOH   HOH A . 
IA 8 HOH   272 1072 107 HOH   HOH A . 
IA 8 HOH   273 1073 232 HOH   HOH A . 
IA 8 HOH   274 1074 238 HOH   HOH A . 
IA 8 HOH   275 1075 276 HOH   HOH A . 
IA 8 HOH   276 1076 336 HOH   HOH A . 
IA 8 HOH   277 1077 299 HOH   HOH A . 
IA 8 HOH   278 1078 300 HOH   HOH A . 
IA 8 HOH   279 1079 304 HOH   HOH A . 
IA 8 HOH   280 1080 237 HOH   HOH A . 
IA 8 HOH   281 1081 334 HOH   HOH A . 
JA 8 HOH   1   501  22  HOH   HOH B . 
JA 8 HOH   2   502  133 HOH   HOH B . 
JA 8 HOH   3   503  385 HOH   HOH B . 
JA 8 HOH   4   504  66  HOH   HOH B . 
JA 8 HOH   5   505  31  HOH   HOH B . 
JA 8 HOH   6   506  81  HOH   HOH B . 
JA 8 HOH   7   507  396 HOH   HOH B . 
JA 8 HOH   8   508  311 HOH   HOH B . 
JA 8 HOH   9   509  51  HOH   HOH B . 
JA 8 HOH   10  510  295 HOH   HOH B . 
JA 8 HOH   11  511  312 HOH   HOH B . 
JA 8 HOH   12  512  278 HOH   HOH B . 
JA 8 HOH   13  513  258 HOH   HOH B . 
JA 8 HOH   14  514  153 HOH   HOH B . 
JA 8 HOH   15  515  77  HOH   HOH B . 
JA 8 HOH   16  516  255 HOH   HOH B . 
JA 8 HOH   17  517  207 HOH   HOH B . 
JA 8 HOH   18  518  152 HOH   HOH B . 
JA 8 HOH   19  519  324 HOH   HOH B . 
JA 8 HOH   20  520  314 HOH   HOH B . 
JA 8 HOH   21  521  205 HOH   HOH B . 
JA 8 HOH   22  522  163 HOH   HOH B . 
JA 8 HOH   23  523  327 HOH   HOH B . 
JA 8 HOH   24  524  347 HOH   HOH B . 
JA 8 HOH   25  525  248 HOH   HOH B . 
JA 8 HOH   26  526  386 HOH   HOH B . 
JA 8 HOH   27  527  151 HOH   HOH B . 
JA 8 HOH   28  528  325 HOH   HOH B . 
JA 8 HOH   29  529  196 HOH   HOH B . 
JA 8 HOH   30  530  241 HOH   HOH B . 
JA 8 HOH   31  531  333 HOH   HOH B . 
JA 8 HOH   32  532  195 HOH   HOH B . 
JA 8 HOH   33  533  330 HOH   HOH B . 
JA 8 HOH   34  534  383 HOH   HOH B . 
JA 8 HOH   35  535  75  HOH   HOH B . 
JA 8 HOH   36  536  27  HOH   HOH B . 
JA 8 HOH   37  537  387 HOH   HOH B . 
JA 8 HOH   38  538  155 HOH   HOH B . 
JA 8 HOH   39  539  199 HOH   HOH B . 
JA 8 HOH   40  540  57  HOH   HOH B . 
JA 8 HOH   41  541  297 HOH   HOH B . 
JA 8 HOH   42  542  184 HOH   HOH B . 
JA 8 HOH   43  543  262 HOH   HOH B . 
JA 8 HOH   44  544  306 HOH   HOH B . 
JA 8 HOH   45  545  391 HOH   HOH B . 
JA 8 HOH   46  546  60  HOH   HOH B . 
JA 8 HOH   47  547  390 HOH   HOH B . 
JA 8 HOH   48  548  158 HOH   HOH B . 
JA 8 HOH   49  549  397 HOH   HOH B . 
JA 8 HOH   50  550  226 HOH   HOH B . 
JA 8 HOH   51  551  394 HOH   HOH B . 
JA 8 HOH   52  552  69  HOH   HOH B . 
JA 8 HOH   53  553  277 HOH   HOH B . 
JA 8 HOH   54  554  206 HOH   HOH B . 
JA 8 HOH   55  555  320 HOH   HOH B . 
JA 8 HOH   56  556  117 HOH   HOH B . 
JA 8 HOH   57  557  388 HOH   HOH B . 
JA 8 HOH   58  558  389 HOH   HOH B . 
JA 8 HOH   59  559  70  HOH   HOH B . 
JA 8 HOH   60  560  289 HOH   HOH B . 
JA 8 HOH   61  561  164 HOH   HOH B . 
JA 8 HOH   62  562  74  HOH   HOH B . 
JA 8 HOH   63  563  208 HOH   HOH B . 
JA 8 HOH   64  564  313 HOH   HOH B . 
JA 8 HOH   65  565  213 HOH   HOH B . 
JA 8 HOH   66  566  348 HOH   HOH B . 
JA 8 HOH   67  567  219 HOH   HOH B . 
JA 8 HOH   68  568  337 HOH   HOH B . 
JA 8 HOH   69  569  393 HOH   HOH B . 
JA 8 HOH   70  570  227 HOH   HOH B . 
JA 8 HOH   71  571  188 HOH   HOH B . 
JA 8 HOH   72  572  198 HOH   HOH B . 
JA 8 HOH   73  573  283 HOH   HOH B . 
JA 8 HOH   74  574  274 HOH   HOH B . 
JA 8 HOH   75  575  303 HOH   HOH B . 
JA 8 HOH   76  576  159 HOH   HOH B . 
JA 8 HOH   77  577  335 HOH   HOH B . 
JA 8 HOH   78  578  326 HOH   HOH B . 
JA 8 HOH   79  579  190 HOH   HOH B . 
JA 8 HOH   80  580  204 HOH   HOH B . 
JA 8 HOH   81  581  319 HOH   HOH B . 
JA 8 HOH   82  582  80  HOH   HOH B . 
JA 8 HOH   83  583  231 HOH   HOH B . 
JA 8 HOH   84  584  384 HOH   HOH B . 
JA 8 HOH   85  585  194 HOH   HOH B . 
JA 8 HOH   86  586  236 HOH   HOH B . 
JA 8 HOH   87  587  191 HOH   HOH B . 
JA 8 HOH   88  588  392 HOH   HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER    ? ? ? 2.11.6 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? .      2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? STARANISO ? ? ? .      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? .      4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9MGQ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     101.660 
_cell.length_a_esd                 ? 
_cell.length_b                     137.700 
_cell.length_b_esd                 ? 
_cell.length_c                     178.000 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9MGQ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9MGQ 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.79 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.92 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '25% PEG 3350, 0.1 M Bis-Tris (pH 5.5), 0.2 M ammonium sulfate' 
_exptl_crystal_grow.pdbx_pH_range   5.5 
_exptl_crystal_grow.temp            283 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2018-04-10 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ALBA BEAMLINE XALOC' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   XALOC 
_diffrn_source.pdbx_synchrotron_site       ALBA 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9MGQ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.85 
_reflns.d_resolution_low                               108.91 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     74746 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           94.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.041 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.095 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
5.02 108.91 ? 39.6 ? ? ? ? 5563 ? ? ? ? ? ? ? ? ? ? ? ?   ? ? ? ? 0.016 ? 1 1 0.999 ? ? 99.3 ? 0.037 ? ? ? ? ? ? ? ? ? 
1.85 1.88   ? 1.5  ? ? ? ? 142  ? ? ? ? ? ? ? ? ? ? ? 6.7 ? ? ? ? 0.668 ? 2 1 0.057 ? ? ?    ? 1.595 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.89890 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.00000 
_refine.aniso_B[2][2]                            0.10540 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            0.79350 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               37.61 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.943 
_refine.correlation_coeff_Fo_to_Fc_free          0.914 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9MGQ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.85 
_refine.ls_d_res_low                             37.00 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     74731 
_refine.ls_number_reflns_R_free                  3690 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    70.3 
_refine.ls_percent_reflns_R_free                 4.940 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.202 
_refine.ls_R_factor_R_free                       0.242 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.199 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.164 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.163 
_refine.pdbx_overall_SU_R_Blow_DPI               0.178 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.179 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_analyze.entry_id                        9MGQ 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.28 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.85 
_refine_hist.d_res_low                        37.00 
_refine_hist.number_atoms_solvent             369 
_refine_hist.number_atoms_total               7924 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        7364 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         191 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008 ? 7941  ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 1.01  ? 10921 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 2668  ? t_dihedral_angle_d        2.00  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? 187   ? t_trig_c_planes           2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1146  ? t_gen_planes              5.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 7941  ? t_it                      20.00 HARMONIC     
'X-RAY DIFFRACTION' ? 3.09  ? ?     ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 17.44 ? ?     ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 981   ? t_chiral_improper_torsion 5.00  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? 9158  ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.85 
_refine_ls_shell.d_res_low                        1.90 
_refine_ls_shell.number_reflns_all                291 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             ? 
_refine_ls_shell.number_reflns_R_work             277 
_refine_ls_shell.percent_reflns_obs               3.73 
_refine_ls_shell.percent_reflns_R_free            4.81 
_refine_ls_shell.R_factor_all                     0.215 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            0.000 
_refine_ls_shell.R_factor_R_work                  0.215 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.224 
# 
_struct.entry_id                     9MGQ 
_struct.title                        'Crystal structure of PRMT5:MEP50 in complex with sinefungin and compound 47' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9MGQ 
_struct_keywords.text            'methyltransferase, inhibitor, MTAP-null, TRANSFERASE, TRANSFERASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   TRANSFERASE/INHIBITOR 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 2 ? 
C  N N 3 ? 
D  N N 4 ? 
E  N N 5 ? 
F  N N 5 ? 
G  N N 5 ? 
H  N N 5 ? 
I  N N 5 ? 
J  N N 5 ? 
K  N N 5 ? 
L  N N 5 ? 
M  N N 5 ? 
N  N N 5 ? 
O  N N 5 ? 
P  N N 5 ? 
Q  N N 5 ? 
R  N N 5 ? 
S  N N 5 ? 
T  N N 5 ? 
U  N N 5 ? 
V  N N 6 ? 
W  N N 6 ? 
X  N N 6 ? 
Y  N N 6 ? 
Z  N N 6 ? 
AA N N 6 ? 
BA N N 6 ? 
CA N N 7 ? 
DA N N 7 ? 
EA N N 7 ? 
FA N N 5 ? 
GA N N 5 ? 
HA N N 6 ? 
IA N N 8 ? 
JA N N 8 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP ANM5_HUMAN  O14744 ? 1 
;AAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFIQEPAKNRPGPQTRSDLLLSGRDWNTL
IVGKLSPWIRPDSKVEKIRRNSEAAMLQELNFGAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPE
DLRDDIIENAPTTHTEEYSGEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILPTSIFLTNKK
GFPVLSKMHQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPLQPLMDNLES
QTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKDTNVQVLMVLGAGRGPLVNASLRAAKQADRRIKLYAVEKNPNAVVTL
ENWQFEEWGSQVTVVSSDMREWVAPEKADIIVSELLGSFADNELSPECLDGAQHFLKDDGVSIPGEYTSFLAPISSSKLY
NEVRACREKDRDPEAQFEMPYVVRLHNFHQLSAPQPCFTFSHPNRDPMIDNNRYCTLEFPVEVNTVLHGFAGYFETVLYQ
DITLSIRPETHSPGMFSWFPILFPIKQPITVREGQTICVRFWRCSNSKKVWYEWAVTAPVCSAIHNPTGRSYTIGL
;
2 
2 UNP MEP50_HUMAN Q9BQA1 ? 2 
;RKETPPPLVPPAAREWNLPPNAPACMERQLEAARYRSDGALLLGASSLSGRCWAGSLWLFKDPCAAPNEGFCSAGVQTEA
GVADLTWVGERGILVASDSGAVELWELDENETLIVSKFCKYEHDDIVSTVSVLSSGTQAVSGSKDICIKVWDLAQQVVLS
SYRAHAAQVTCVAASPHKDSVFLSCSEDNRILLWDTRCPKPASQIGCSAPGYLPTSLAWHPQQSEVFVFGDENGTVSLVD
TKSTSCVLSSAVHSQCVTGLVFSPHSVPFLASLSEDCSLAVLDSSLSELFRSQAHRDFVRDATWSPLNHSLLTTVGWDHQ
VVHHVVPTEPLPAPGPASVTE
;
2 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9MGQ A 10 ? 645 ? O14744 2 ? 637 ? 2 637 
2 2 9MGQ B 10 ? 350 ? Q9BQA1 2 ? 342 ? 2 342 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9MGQ MET A 1 ? UNP O14744 ? ? 'initiating methionine' -7 1  
1 9MGQ ASP A 2 ? UNP O14744 ? ? 'expression tag'        -6 2  
1 9MGQ TYR A 3 ? UNP O14744 ? ? 'expression tag'        -5 3  
1 9MGQ LYS A 4 ? UNP O14744 ? ? 'expression tag'        -4 4  
1 9MGQ ASP A 5 ? UNP O14744 ? ? 'expression tag'        -3 5  
1 9MGQ ASP A 6 ? UNP O14744 ? ? 'expression tag'        -2 6  
1 9MGQ ASP A 7 ? UNP O14744 ? ? 'expression tag'        -1 7  
1 9MGQ ASP A 8 ? UNP O14744 ? ? 'expression tag'        0  8  
1 9MGQ LYS A 9 ? UNP O14744 ? ? 'expression tag'        1  9  
2 9MGQ MET B 1 ? UNP Q9BQA1 ? ? 'initiating methionine' -7 10 
2 9MGQ HIS B 2 ? UNP Q9BQA1 ? ? 'expression tag'        -6 11 
2 9MGQ HIS B 3 ? UNP Q9BQA1 ? ? 'expression tag'        -5 12 
2 9MGQ HIS B 4 ? UNP Q9BQA1 ? ? 'expression tag'        -4 13 
2 9MGQ HIS B 5 ? UNP Q9BQA1 ? ? 'expression tag'        -3 14 
2 9MGQ HIS B 6 ? UNP Q9BQA1 ? ? 'expression tag'        -2 15 
2 9MGQ HIS B 7 ? UNP Q9BQA1 ? ? 'expression tag'        -1 16 
2 9MGQ HIS B 8 ? UNP Q9BQA1 ? ? 'expression tag'        0  17 
2 9MGQ HIS B 9 ? UNP Q9BQA1 ? ? 'expression tag'        1  18 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   octameric 
_pdbx_struct_assembly.oligomeric_count     8 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,D,E,F,G,H,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 
1 2 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 
1 3 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 
1 4 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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000    0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 2_545 -x,-y-1,z -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 
0.0000000000 -137.7000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
3 'crystal symmetry operation' 3_555 -x,y,-z   -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000    0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
4 'crystal symmetry operation' 4_545 x,-y-1,-z 1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 
0.0000000000 -137.7000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLU A 33  ? GLN A 44  ? GLU A 25  GLN A 36  1 ? 12 
HELX_P HELX_P2  AA2 PRO A 66  ? ARG A 70  ? PRO A 58  ARG A 62  5 ? 5  
HELX_P HELX_P3  AA3 SER A 77  ? LEU A 81  ? SER A 69  LEU A 73  5 ? 5  
HELX_P HELX_P4  AA4 SER A 82  ? LEU A 89  ? SER A 74  LEU A 81  1 ? 8  
HELX_P HELX_P5  AA5 VAL A 104 ? GLY A 126 ? VAL A 96  GLY A 118 1 ? 23 
HELX_P HELX_P6  AA6 ASN A 139 ? HIS A 151 ? ASN A 131 HIS A 143 1 ? 13 
HELX_P HELX_P7  AA7 ALA A 167 ? ARG A 172 ? ALA A 159 ARG A 164 1 ? 6  
HELX_P HELX_P8  AA8 SER A 188 ? GLU A 190 ? SER A 180 GLU A 182 5 ? 3  
HELX_P HELX_P9  AA9 GLU A 191 ? CYS A 204 ? GLU A 183 CYS A 196 1 ? 14 
HELX_P HELX_P10 AB1 SER A 222 ? ARG A 228 ? SER A 214 ARG A 220 1 ? 7  
HELX_P HELX_P11 AB2 SER A 242 ? PHE A 244 ? SER A 234 PHE A 236 5 ? 3  
HELX_P HELX_P12 AB3 SER A 255 ? LEU A 268 ? SER A 247 LEU A 260 1 ? 14 
HELX_P HELX_P13 AB4 CYS A 286 ? ASN A 298 ? CYS A 278 ASN A 290 1 ? 13 
HELX_P HELX_P14 AB5 ASN A 303 ? LYS A 310 ? ASN A 295 LYS A 302 1 ? 8  
HELX_P HELX_P15 AB6 GLU A 328 ? GLU A 336 ? GLU A 320 GLU A 328 1 ? 9  
HELX_P HELX_P16 AB7 ILE A 340 ? VAL A 357 ? ILE A 332 VAL A 349 1 ? 18 
HELX_P HELX_P17 AB8 PRO A 358 ? LYS A 362 ? PRO A 350 LYS A 354 5 ? 5  
HELX_P HELX_P18 AB9 GLY A 377 ? ASP A 391 ? GLY A 369 ASP A 383 1 ? 15 
HELX_P HELX_P19 AC1 ASN A 402 ? GLU A 416 ? ASN A 394 GLU A 408 1 ? 15 
HELX_P HELX_P20 AC2 TRP A 417 ? SER A 419 ? TRP A 409 SER A 411 5 ? 3  
HELX_P HELX_P21 AC3 LEU A 453 ? GLY A 460 ? LEU A 445 GLY A 452 1 ? 8  
HELX_P HELX_P22 AC4 ALA A 461 ? HIS A 463 ? ALA A 453 HIS A 455 5 ? 3  
HELX_P HELX_P23 AC5 SER A 485 ? ALA A 494 ? SER A 477 ALA A 486 1 ? 10 
HELX_P HELX_P24 AC6 GLU A 503 ? GLU A 507 ? GLU A 495 GLU A 499 5 ? 5  
HELX_P HELX_P25 AC7 ARG A 576 ? HIS A 580 ? ARG A 568 HIS A 572 5 ? 5  
HELX_P HELX_P26 AC8 ASN A 635 ? ARG A 639 ? ASN A 627 ARG A 631 5 ? 5  
HELX_P HELX_P27 AC9 ASP B 71  ? ALA B 75  ? ASP B 63  ALA B 67  5 ? 5  
HELX_P HELX_P28 AD1 ASN B 77  ? CYS B 81  ? ASN B 69  CYS B 73  5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLU 65  A . ? GLU 57  A PRO 66  A ? PRO 58  A 1 6.63  
2 GLY 72  A . ? GLY 64  A PRO 73  A ? PRO 65  A 1 0.89  
3 ILE 472 A . ? ILE 464 A PRO 473 A ? PRO 465 A 1 5.08  
4 HIS 531 A . ? HIS 523 A PRO 532 A ? PRO 524 A 1 -2.90 
5 ALA 627 A . ? ALA 619 A PRO 628 A ? PRO 620 A 1 1.54  
6 ALA 75  B . ? ALA 67  B PRO 76  B ? PRO 68  B 1 3.91  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9 ? 
AA2 ? 2 ? 
AA3 ? 5 ? 
AA4 ? 5 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 4 ? 
AA8 ? 4 ? 
AA9 ? 4 ? 
AB1 ? 4 ? 
AB2 ? 4 ? 
AB3 ? 4 ? 
AB4 ? 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 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
AA1 8 9 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 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 
AA1 1 SER A 24  ? ASP A 27  ? SER A 16  ASP A 19  
AA1 2 PHE A 48  ? PRO A 52  ? PHE A 40  PRO A 44  
AA1 3 ILE A 90  ? LYS A 93  ? ILE A 82  LYS A 85  
AA1 4 ALA A 129 ? PRO A 133 ? ALA A 121 PRO A 125 
AA1 5 MET A 158 ? PRO A 164 ? MET A 150 PRO A 156 
AA1 6 ILE A 210 ? GLU A 215 ? ILE A 202 GLU A 207 
AA1 7 ILE A 234 ? PRO A 240 ? ILE A 226 PRO A 232 
AA1 8 GLN A 271 ? THR A 275 ? GLN A 263 THR A 267 
AA1 9 SER A 24  ? ASP A 27  ? SER A 16  ASP A 19  
AA2 1 LEU A 245 ? THR A 246 ? LEU A 237 THR A 238 
AA2 2 PRO A 252 ? VAL A 253 ? PRO A 244 VAL A 245 
AA3 1 VAL A 421 ? SER A 425 ? VAL A 413 SER A 417 
AA3 2 ARG A 393 ? GLU A 400 ? ARG A 385 GLU A 392 
AA3 3 VAL A 366 ? LEU A 372 ? VAL A 358 LEU A 364 
AA3 4 ALA A 437 ? VAL A 441 ? ALA A 429 VAL A 433 
AA3 5 LEU A 465 ? ILE A 472 ? LEU A 457 ILE A 464 
AA4 1 TYR A 510 ? VAL A 511 ? TYR A 502 VAL A 503 
AA4 2 ILE A 590 ? VAL A 600 ? ILE A 582 VAL A 592 
AA4 3 THR A 554 ? TYR A 568 ? THR A 546 TYR A 560 
AA4 4 GLU A 475 ? SER A 484 ? GLU A 467 SER A 476 
AA4 5 GLN A 524 ? SER A 530 ? GLN A 516 SER A 522 
AA5 1 HIS A 518 ? GLN A 519 ? HIS A 510 GLN A 511 
AA5 2 GLU A 475 ? SER A 484 ? GLU A 467 SER A 476 
AA5 3 THR A 554 ? TYR A 568 ? THR A 546 TYR A 560 
AA5 4 ILE A 571 ? SER A 574 ? ILE A 563 SER A 566 
AA6 1 ARG A 542 ? PRO A 549 ? ARG A 534 PRO A 541 
AA6 2 THR A 605 ? SER A 614 ? THR A 597 SER A 606 
AA6 3 LYS A 618 ? ALA A 627 ? LYS A 610 ALA A 619 
AA6 4 ILE A 643 ? GLY A 644 ? ILE A 635 GLY A 636 
AA7 1 GLN B 38  ? TYR B 44  ? GLN B 30  TYR B 36  
AA7 2 LEU B 50  ? SER B 55  ? LEU B 42  SER B 47  
AA7 3 GLY B 64  ? PHE B 69  ? GLY B 56  PHE B 61  
AA7 4 ALA B 83  ? THR B 87  ? ALA B 75  THR B 79  
AA8 1 VAL B 91  ? VAL B 97  ? VAL B 83  VAL B 89  
AA8 2 GLY B 101 ? SER B 106 ? GLY B 93  SER B 98  
AA8 3 ALA B 110 ? LEU B 116 ? ALA B 102 LEU B 108 
AA8 4 ILE B 123 ? TYR B 130 ? ILE B 115 TYR B 122 
AA9 1 VAL B 136 ? VAL B 141 ? VAL B 128 VAL B 133 
AA9 2 GLN B 147 ? SER B 152 ? GLN B 139 SER B 144 
AA9 3 ILE B 157 ? ASP B 161 ? ILE B 149 ASP B 153 
AA9 4 VAL B 166 ? TYR B 171 ? VAL B 158 TYR B 163 
AB1 1 VAL B 178 ? ALA B 183 ? VAL B 170 ALA B 175 
AB1 2 VAL B 190 ? SER B 195 ? VAL B 182 SER B 187 
AB1 3 ILE B 200 ? ASP B 204 ? ILE B 192 ASP B 196 
AB1 4 ALA B 211 ? GLN B 213 ? ALA B 203 GLN B 205 
AB2 1 PRO B 223 ? TRP B 228 ? PRO B 215 TRP B 220 
AB2 2 VAL B 235 ? ASP B 240 ? VAL B 227 ASP B 232 
AB2 3 THR B 244 ? ASP B 249 ? THR B 236 ASP B 241 
AB2 4 SER B 254 ? ALA B 260 ? SER B 246 ALA B 252 
AB3 1 VAL B 266 ? PHE B 271 ? VAL B 258 PHE B 263 
AB3 2 LEU B 279 ? SER B 283 ? LEU B 271 SER B 275 
AB3 3 LEU B 288 ? LEU B 291 ? LEU B 280 LEU B 283 
AB3 4 GLU B 297 ? SER B 301 ? GLU B 289 SER B 293 
AB4 1 VAL B 308 ? TRP B 313 ? VAL B 300 TRP B 305 
AB4 2 LEU B 320 ? GLY B 325 ? LEU B 312 GLY B 317 
AB4 3 VAL B 330 ? VAL B 334 ? VAL B 322 VAL B 326 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ARG A 26  ? N ARG A 18  O CYS A 50  ? O CYS A 42  
AA1 2 3 N LEU A 49  ? N LEU A 41  O VAL A 91  ? O VAL A 83  
AA1 3 4 N GLY A 92  ? N GLY A 84  O LEU A 131 ? O LEU A 123 
AA1 4 5 N LEU A 132 ? N LEU A 124 O ARG A 162 ? O ARG A 154 
AA1 5 6 N PHE A 159 ? N PHE A 151 O ALA A 211 ? O ALA A 203 
AA1 6 7 N LEU A 214 ? N LEU A 206 O ILE A 238 ? O ILE A 230 
AA1 7 8 N LEU A 239 ? N LEU A 231 O ILE A 273 ? O ILE A 265 
AA1 8 9 O ILE A 274 ? O ILE A 266 N ASP A 27  ? N ASP A 19  
AA2 1 2 N LEU A 245 ? N LEU A 237 O VAL A 253 ? O VAL A 245 
AA3 1 2 O THR A 422 ? O THR A 414 N ALA A 398 ? N ALA A 390 
AA3 2 3 O TYR A 397 ? O TYR A 389 N VAL A 371 ? N VAL A 363 
AA3 3 4 N MET A 370 ? N MET A 362 O VAL A 441 ? O VAL A 433 
AA3 4 5 N ILE A 440 ? N ILE A 432 O ILE A 472 ? O ILE A 464 
AA4 1 2 N TYR A 510 ? N TYR A 502 O LEU A 591 ? O LEU A 583 
AA4 2 3 O ILE A 598 ? O ILE A 590 N LEU A 556 ? N LEU A 548 
AA4 3 4 O GLU A 564 ? O GLU A 556 N THR A 477 ? N THR A 469 
AA4 4 5 N SER A 478 ? N SER A 470 O CYS A 526 ? O CYS A 518 
AA5 1 2 O HIS A 518 ? O HIS A 510 N SER A 484 ? N SER A 476 
AA5 2 3 N THR A 477 ? N THR A 469 O GLU A 564 ? O GLU A 556 
AA5 3 4 N TYR A 568 ? N TYR A 560 O ILE A 571 ? O ILE A 563 
AA6 1 2 N PHE A 548 ? N PHE A 540 O ILE A 606 ? O ILE A 598 
AA6 2 3 N CYS A 613 ? N CYS A 605 O TRP A 620 ? O TRP A 612 
AA6 3 4 N VAL A 619 ? N VAL A 611 O ILE A 643 ? O ILE A 635 
AA7 1 2 N GLN B 38  ? N GLN B 30  O SER B 55  ? O SER B 47  
AA7 2 3 N LEU B 50  ? N LEU B 42  O PHE B 69  ? O PHE B 61  
AA7 3 4 N LEU B 68  ? N LEU B 60  O ALA B 83  ? O ALA B 75  
AA8 1 2 N THR B 95  ? N THR B 87  O LEU B 103 ? O LEU B 95  
AA8 2 3 N VAL B 104 ? N VAL B 96  O GLU B 112 ? O GLU B 104 
AA8 3 4 N GLU B 115 ? N GLU B 107 O VAL B 124 ? O VAL B 116 
AA9 1 2 N SER B 140 ? N SER B 132 O VAL B 149 ? O VAL B 141 
AA9 2 3 N ALA B 148 ? N ALA B 140 O TRP B 160 ? O TRP B 152 
AA9 3 4 N ILE B 157 ? N ILE B 149 O TYR B 171 ? O TYR B 163 
AB1 1 2 N ALA B 182 ? N ALA B 174 O LEU B 192 ? O LEU B 184 
AB1 2 3 N PHE B 191 ? N PHE B 183 O TRP B 203 ? O TRP B 195 
AB1 3 4 N LEU B 202 ? N LEU B 194 O SER B 212 ? O SER B 204 
AB2 1 2 N THR B 224 ? N THR B 216 O GLY B 239 ? O GLY B 231 
AB2 2 3 N PHE B 236 ? N PHE B 228 O VAL B 248 ? O VAL B 240 
AB2 3 4 N LEU B 247 ? N LEU B 239 O LEU B 257 ? O LEU B 249 
AB3 1 2 N VAL B 270 ? N VAL B 262 O ALA B 280 ? O ALA B 272 
AB3 2 3 N LEU B 279 ? N LEU B 271 O LEU B 291 ? O LEU B 283 
AB3 3 4 N VAL B 290 ? N VAL B 282 O LEU B 298 ? O LEU B 290 
AB4 1 2 N THR B 312 ? N THR B 304 O THR B 322 ? O THR B 314 
AB4 2 3 N LEU B 321 ? N LEU B 313 O HIS B 333 ? O HIS B 325 
# 
_pdbx_entry_details.entry_id                   9MGQ 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 GLU A 408 ? ? -121.93 -55.87  
2  1 ALA A 441 ? ? 69.44   -70.20  
3  1 SER A 477 ? ? -167.23 102.01  
4  1 HIS A 507 ? ? -133.41 -59.57  
5  1 CYS A 518 ? ? -109.73 -77.07  
6  1 TYR A 560 ? ? -160.44 117.71  
7  1 GLN A 561 ? ? 53.70   -105.86 
8  1 ASN B 22  ? ? 68.71   -17.09  
9  1 TRP B 54  ? ? -107.66 74.99   
10 1 ALA B 55  ? ? -118.02 -163.54 
11 1 PRO B 68  ? ? -97.91  30.32   
12 1 ILE B 147 ? ? 78.05   -10.46  
13 1 ARG B 164 ? ? -113.95 75.69   
14 1 THR B 197 ? ? -68.93  1.72    
15 1 CYS B 257 ? ? -36.69  129.19  
# 
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 MET -7  ? A MET 1   
2  1 Y 1 A ASP -6  ? A ASP 2   
3  1 Y 1 A TYR -5  ? A TYR 3   
4  1 Y 1 A LYS -4  ? A LYS 4   
5  1 Y 1 A ASP -3  ? A ASP 5   
6  1 Y 1 A ASP -2  ? A ASP 6   
7  1 Y 1 A ASP -1  ? A ASP 7   
8  1 Y 1 A ASP 0   ? A ASP 8   
9  1 Y 1 A LYS 1   ? A LYS 9   
10 1 Y 1 A ALA 2   ? A ALA 10  
11 1 Y 1 A ALA 3   ? A ALA 11  
12 1 Y 1 A MET 4   ? A MET 12  
13 1 Y 1 A ALA 5   ? A ALA 13  
14 1 Y 1 A VAL 6   ? A VAL 14  
15 1 Y 1 A GLY 7   ? A GLY 15  
16 1 Y 1 A GLY 8   ? A GLY 16  
17 1 Y 1 A ALA 9   ? A ALA 17  
18 1 Y 1 A GLY 10  ? A GLY 18  
19 1 Y 1 A GLY 11  ? A GLY 19  
20 1 Y 1 A SER 12  ? A SER 20  
21 1 Y 1 A ARG 13  ? A ARG 21  
22 1 Y 1 B MET -7  ? B MET 1   
23 1 Y 1 B HIS -6  ? B HIS 2   
24 1 Y 1 B HIS -5  ? B HIS 3   
25 1 Y 1 B HIS -4  ? B HIS 4   
26 1 Y 1 B HIS -3  ? B HIS 5   
27 1 Y 1 B HIS -2  ? B HIS 6   
28 1 Y 1 B HIS -1  ? B HIS 7   
29 1 Y 1 B HIS 0   ? B HIS 8   
30 1 Y 1 B HIS 1   ? B HIS 9   
31 1 Y 1 B ARG 2   ? B ARG 10  
32 1 Y 1 B LYS 3   ? B LYS 11  
33 1 Y 1 B GLU 4   ? B GLU 12  
34 1 Y 1 B THR 5   ? B THR 13  
35 1 Y 1 B PRO 6   ? B PRO 14  
36 1 Y 1 B PRO 7   ? B PRO 15  
37 1 Y 1 B PRO 8   ? B PRO 16  
38 1 Y 1 B LEU 9   ? B LEU 17  
39 1 Y 1 B VAL 10  ? B VAL 18  
40 1 Y 1 B PRO 11  ? B PRO 19  
41 1 Y 1 B PRO 12  ? B PRO 20  
42 1 Y 1 B ALA 13  ? B ALA 21  
43 1 Y 1 B ALA 14  ? B ALA 22  
44 1 Y 1 B ARG 15  ? B ARG 23  
45 1 Y 1 B GLU 16  ? B GLU 24  
46 1 Y 1 B TRP 17  ? B TRP 25  
47 1 Y 1 B ASN 18  ? B ASN 26  
48 1 Y 1 B LEU 19  ? B LEU 27  
49 1 Y 1 B GLY 207 ? B GLY 215 
50 1 Y 1 B CYS 208 ? B CYS 216 
51 1 Y 1 B SER 209 ? B SER 217 
52 1 Y 1 B THR 329 ? B THR 337 
53 1 Y 1 B GLU 330 ? B GLU 338 
54 1 Y 1 B PRO 331 ? B PRO 339 
55 1 Y 1 B LEU 332 ? B LEU 340 
56 1 Y 1 B PRO 333 ? B PRO 341 
57 1 Y 1 B ALA 334 ? B ALA 342 
58 1 Y 1 B PRO 335 ? B PRO 343 
59 1 Y 1 B GLY 336 ? B GLY 344 
60 1 Y 1 B PRO 337 ? B PRO 345 
61 1 Y 1 B ALA 338 ? B ALA 346 
62 1 Y 1 B SER 339 ? B SER 347 
63 1 Y 1 B VAL 340 ? B VAL 348 
64 1 Y 1 B THR 341 ? B THR 349 
65 1 Y 1 B GLU 342 ? B GLU 350 
# 
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 
A1BLG C1     C N N 1   
A1BLG C2     C N N 2   
A1BLG C3     C Y N 3   
A1BLG C4     C Y N 4   
A1BLG C5     C Y N 5   
A1BLG C6     C Y N 6   
A1BLG C7     C N N 7   
A1BLG N1     N Y N 8   
A1BLG N2     N N N 9   
A1BLG N3     N N N 10  
A1BLG C8     C N N 11  
A1BLG O1     O N N 12  
A1BLG C11    C Y N 13  
A1BLG C10    C N N 14  
A1BLG C9     C N N 15  
A1BLG N      N N N 16  
A1BLG C      C N R 17  
A1BLG O      O N N 18  
A1BLG C12    C N S 19  
A1BLG C20    C N N 20  
A1BLG C19    C Y N 21  
A1BLG C14    C Y N 22  
A1BLG C13    C N N 23  
A1BLG C18    C Y N 24  
A1BLG C17    C Y N 25  
A1BLG C16    C Y N 26  
A1BLG C15    C Y N 27  
A1BLG H4     H N N 28  
A1BLG H3     H N N 29  
A1BLG H6     H N N 30  
A1BLG H7     H N N 31  
A1BLG H9     H N N 32  
A1BLG H8     H N N 33  
A1BLG H25    H N N 34  
A1BLG H11    H N N 35  
A1BLG H10    H N N 36  
A1BLG H16    H N N 37  
A1BLG H14    H N N 38  
A1BLG H15    H N N 39  
A1BLG H13    H N N 40  
A1BLG H12    H N N 41  
A1BLG H5     H N N 42  
A1BLG H      H N N 43  
A1BLG H2     H N N 44  
A1BLG H1     H N N 45  
A1BLG H23    H N N 46  
A1BLG H24    H N N 47  
A1BLG H17    H N N 48  
A1BLG H18    H N N 49  
A1BLG H22    H N N 50  
A1BLG H21    H N N 51  
A1BLG H20    H N N 52  
A1BLG H19    H N N 53  
ALA   N      N N N 54  
ALA   CA     C N S 55  
ALA   C      C N N 56  
ALA   O      O N N 57  
ALA   CB     C N N 58  
ALA   OXT    O N N 59  
ALA   H      H N N 60  
ALA   H2     H N N 61  
ALA   HA     H N N 62  
ALA   HB1    H N N 63  
ALA   HB2    H N N 64  
ALA   HB3    H N N 65  
ALA   HXT    H N N 66  
ARG   N      N N N 67  
ARG   CA     C N S 68  
ARG   C      C N N 69  
ARG   O      O N N 70  
ARG   CB     C N N 71  
ARG   CG     C N N 72  
ARG   CD     C N N 73  
ARG   NE     N N N 74  
ARG   CZ     C N N 75  
ARG   NH1    N N N 76  
ARG   NH2    N N N 77  
ARG   OXT    O N N 78  
ARG   H      H N N 79  
ARG   H2     H N N 80  
ARG   HA     H N N 81  
ARG   HB2    H N N 82  
ARG   HB3    H N N 83  
ARG   HG2    H N N 84  
ARG   HG3    H N N 85  
ARG   HD2    H N N 86  
ARG   HD3    H N N 87  
ARG   HE     H N N 88  
ARG   HH11   H N N 89  
ARG   HH12   H N N 90  
ARG   HH21   H N N 91  
ARG   HH22   H N N 92  
ARG   HXT    H N N 93  
ASN   N      N N N 94  
ASN   CA     C N S 95  
ASN   C      C N N 96  
ASN   O      O N N 97  
ASN   CB     C N N 98  
ASN   CG     C N N 99  
ASN   OD1    O N N 100 
ASN   ND2    N N N 101 
ASN   OXT    O N N 102 
ASN   H      H N N 103 
ASN   H2     H N N 104 
ASN   HA     H N N 105 
ASN   HB2    H N N 106 
ASN   HB3    H N N 107 
ASN   HD21   H N N 108 
ASN   HD22   H N N 109 
ASN   HXT    H N N 110 
ASP   N      N N N 111 
ASP   CA     C N S 112 
ASP   C      C N N 113 
ASP   O      O N N 114 
ASP   CB     C N N 115 
ASP   CG     C N N 116 
ASP   OD1    O N N 117 
ASP   OD2    O N N 118 
ASP   OXT    O N N 119 
ASP   H      H N N 120 
ASP   H2     H N N 121 
ASP   HA     H N N 122 
ASP   HB2    H N N 123 
ASP   HB3    H N N 124 
ASP   HD2    H N N 125 
ASP   HXT    H N N 126 
CYS   N      N N N 127 
CYS   CA     C N R 128 
CYS   C      C N N 129 
CYS   O      O N N 130 
CYS   CB     C N N 131 
CYS   SG     S N N 132 
CYS   OXT    O N N 133 
CYS   H      H N N 134 
CYS   H2     H N N 135 
CYS   HA     H N N 136 
CYS   HB2    H N N 137 
CYS   HB3    H N N 138 
CYS   HG     H N N 139 
CYS   HXT    H N N 140 
EDO   C1     C N N 141 
EDO   O1     O N N 142 
EDO   C2     C N N 143 
EDO   O2     O N N 144 
EDO   H11    H N N 145 
EDO   H12    H N N 146 
EDO   HO1    H N N 147 
EDO   H21    H N N 148 
EDO   H22    H N N 149 
EDO   HO2    H N N 150 
GLN   N      N N N 151 
GLN   CA     C N S 152 
GLN   C      C N N 153 
GLN   O      O N N 154 
GLN   CB     C N N 155 
GLN   CG     C N N 156 
GLN   CD     C N N 157 
GLN   OE1    O N N 158 
GLN   NE2    N N N 159 
GLN   OXT    O N N 160 
GLN   H      H N N 161 
GLN   H2     H N N 162 
GLN   HA     H N N 163 
GLN   HB2    H N N 164 
GLN   HB3    H N N 165 
GLN   HG2    H N N 166 
GLN   HG3    H N N 167 
GLN   HE21   H N N 168 
GLN   HE22   H N N 169 
GLN   HXT    H N N 170 
GLU   N      N N N 171 
GLU   CA     C N S 172 
GLU   C      C N N 173 
GLU   O      O N N 174 
GLU   CB     C N N 175 
GLU   CG     C N N 176 
GLU   CD     C N N 177 
GLU   OE1    O N N 178 
GLU   OE2    O N N 179 
GLU   OXT    O N N 180 
GLU   H      H N N 181 
GLU   H2     H N N 182 
GLU   HA     H N N 183 
GLU   HB2    H N N 184 
GLU   HB3    H N N 185 
GLU   HG2    H N N 186 
GLU   HG3    H N N 187 
GLU   HE2    H N N 188 
GLU   HXT    H N N 189 
GLY   N      N N N 190 
GLY   CA     C N N 191 
GLY   C      C N N 192 
GLY   O      O N N 193 
GLY   OXT    O N N 194 
GLY   H      H N N 195 
GLY   H2     H N N 196 
GLY   HA2    H N N 197 
GLY   HA3    H N N 198 
GLY   HXT    H N N 199 
HIS   N      N N N 200 
HIS   CA     C N S 201 
HIS   C      C N N 202 
HIS   O      O N N 203 
HIS   CB     C N N 204 
HIS   CG     C Y N 205 
HIS   ND1    N Y N 206 
HIS   CD2    C Y N 207 
HIS   CE1    C Y N 208 
HIS   NE2    N Y N 209 
HIS   OXT    O N N 210 
HIS   H      H N N 211 
HIS   H2     H N N 212 
HIS   HA     H N N 213 
HIS   HB2    H N N 214 
HIS   HB3    H N N 215 
HIS   HD1    H N N 216 
HIS   HD2    H N N 217 
HIS   HE1    H N N 218 
HIS   HE2    H N N 219 
HIS   HXT    H N N 220 
HOH   O      O N N 221 
HOH   H1     H N N 222 
HOH   H2     H N N 223 
ILE   N      N N N 224 
ILE   CA     C N S 225 
ILE   C      C N N 226 
ILE   O      O N N 227 
ILE   CB     C N S 228 
ILE   CG1    C N N 229 
ILE   CG2    C N N 230 
ILE   CD1    C N N 231 
ILE   OXT    O N N 232 
ILE   H      H N N 233 
ILE   H2     H N N 234 
ILE   HA     H N N 235 
ILE   HB     H N N 236 
ILE   HG12   H N N 237 
ILE   HG13   H N N 238 
ILE   HG21   H N N 239 
ILE   HG22   H N N 240 
ILE   HG23   H N N 241 
ILE   HD11   H N N 242 
ILE   HD12   H N N 243 
ILE   HD13   H N N 244 
ILE   HXT    H N N 245 
LEU   N      N N N 246 
LEU   CA     C N S 247 
LEU   C      C N N 248 
LEU   O      O N N 249 
LEU   CB     C N N 250 
LEU   CG     C N N 251 
LEU   CD1    C N N 252 
LEU   CD2    C N N 253 
LEU   OXT    O N N 254 
LEU   H      H N N 255 
LEU   H2     H N N 256 
LEU   HA     H N N 257 
LEU   HB2    H N N 258 
LEU   HB3    H N N 259 
LEU   HG     H N N 260 
LEU   HD11   H N N 261 
LEU   HD12   H N N 262 
LEU   HD13   H N N 263 
LEU   HD21   H N N 264 
LEU   HD22   H N N 265 
LEU   HD23   H N N 266 
LEU   HXT    H N N 267 
LYS   N      N N N 268 
LYS   CA     C N S 269 
LYS   C      C N N 270 
LYS   O      O N N 271 
LYS   CB     C N N 272 
LYS   CG     C N N 273 
LYS   CD     C N N 274 
LYS   CE     C N N 275 
LYS   NZ     N N N 276 
LYS   OXT    O N N 277 
LYS   H      H N N 278 
LYS   H2     H N N 279 
LYS   HA     H N N 280 
LYS   HB2    H N N 281 
LYS   HB3    H N N 282 
LYS   HG2    H N N 283 
LYS   HG3    H N N 284 
LYS   HD2    H N N 285 
LYS   HD3    H N N 286 
LYS   HE2    H N N 287 
LYS   HE3    H N N 288 
LYS   HZ1    H N N 289 
LYS   HZ2    H N N 290 
LYS   HZ3    H N N 291 
LYS   HXT    H N N 292 
MET   N      N N N 293 
MET   CA     C N S 294 
MET   C      C N N 295 
MET   O      O N N 296 
MET   CB     C N N 297 
MET   CG     C N N 298 
MET   SD     S N N 299 
MET   CE     C N N 300 
MET   OXT    O N N 301 
MET   H      H N N 302 
MET   H2     H N N 303 
MET   HA     H N N 304 
MET   HB2    H N N 305 
MET   HB3    H N N 306 
MET   HG2    H N N 307 
MET   HG3    H N N 308 
MET   HE1    H N N 309 
MET   HE2    H N N 310 
MET   HE3    H N N 311 
MET   HXT    H N N 312 
PEG   C1     C N N 313 
PEG   O1     O N N 314 
PEG   C2     C N N 315 
PEG   O2     O N N 316 
PEG   C3     C N N 317 
PEG   C4     C N N 318 
PEG   O4     O N N 319 
PEG   H11    H N N 320 
PEG   H12    H N N 321 
PEG   HO1    H N N 322 
PEG   H21    H N N 323 
PEG   H22    H N N 324 
PEG   H31    H N N 325 
PEG   H32    H N N 326 
PEG   H41    H N N 327 
PEG   H42    H N N 328 
PEG   HO4    H N N 329 
PHE   N      N N N 330 
PHE   CA     C N S 331 
PHE   C      C N N 332 
PHE   O      O N N 333 
PHE   CB     C N N 334 
PHE   CG     C Y N 335 
PHE   CD1    C Y N 336 
PHE   CD2    C Y N 337 
PHE   CE1    C Y N 338 
PHE   CE2    C Y N 339 
PHE   CZ     C Y N 340 
PHE   OXT    O N N 341 
PHE   H      H N N 342 
PHE   H2     H N N 343 
PHE   HA     H N N 344 
PHE   HB2    H N N 345 
PHE   HB3    H N N 346 
PHE   HD1    H N N 347 
PHE   HD2    H N N 348 
PHE   HE1    H N N 349 
PHE   HE2    H N N 350 
PHE   HZ     H N N 351 
PHE   HXT    H N N 352 
PRO   N      N N N 353 
PRO   CA     C N S 354 
PRO   C      C N N 355 
PRO   O      O N N 356 
PRO   CB     C N N 357 
PRO   CG     C N N 358 
PRO   CD     C N N 359 
PRO   OXT    O N N 360 
PRO   H      H N N 361 
PRO   HA     H N N 362 
PRO   HB2    H N N 363 
PRO   HB3    H N N 364 
PRO   HG2    H N N 365 
PRO   HG3    H N N 366 
PRO   HD2    H N N 367 
PRO   HD3    H N N 368 
PRO   HXT    H N N 369 
SER   N      N N N 370 
SER   CA     C N S 371 
SER   C      C N N 372 
SER   O      O N N 373 
SER   CB     C N N 374 
SER   OG     O N N 375 
SER   OXT    O N N 376 
SER   H      H N N 377 
SER   H2     H N N 378 
SER   HA     H N N 379 
SER   HB2    H N N 380 
SER   HB3    H N N 381 
SER   HG     H N N 382 
SER   HXT    H N N 383 
SFG   N      N N N 384 
SFG   CA     C N S 385 
SFG   C      C N N 386 
SFG   O      O N N 387 
SFG   OXT    O N N 388 
SFG   CB     C N N 389 
SFG   CG     C N N 390 
SFG   CD     C N S 391 
SFG   NE     N N N 392 
SFG   "C5'"  C N N 393 
SFG   "C4'"  C N R 394 
SFG   "O4'"  O N N 395 
SFG   "C3'"  C N S 396 
SFG   "O3'"  O N N 397 
SFG   "C2'"  C N R 398 
SFG   "O2'"  O N N 399 
SFG   "C1'"  C N R 400 
SFG   N9     N Y N 401 
SFG   C8     C Y N 402 
SFG   N7     N Y N 403 
SFG   C5     C Y N 404 
SFG   C6     C Y N 405 
SFG   N6     N N N 406 
SFG   N1     N Y N 407 
SFG   C2     C Y N 408 
SFG   N3     N Y N 409 
SFG   C4     C Y N 410 
SFG   HN1    H N N 411 
SFG   HN2    H N N 412 
SFG   HA     H N N 413 
SFG   HXT    H N N 414 
SFG   HB1    H N N 415 
SFG   HB2    H N N 416 
SFG   HG1    H N N 417 
SFG   HG2    H N N 418 
SFG   HD     H N N 419 
SFG   HNE1   H N N 420 
SFG   HNE2   H N N 421 
SFG   "H5'1" H N N 422 
SFG   "H5'2" H N N 423 
SFG   "H4'"  H N N 424 
SFG   "H3'"  H N N 425 
SFG   "HO3'" H N N 426 
SFG   "H2'"  H N N 427 
SFG   "HO2'" H N N 428 
SFG   "H1'"  H N N 429 
SFG   H8     H N N 430 
SFG   HN61   H N N 431 
SFG   HN62   H N N 432 
SFG   H2     H N N 433 
SO4   S      S N N 434 
SO4   O1     O N N 435 
SO4   O2     O N N 436 
SO4   O3     O N N 437 
SO4   O4     O N N 438 
THR   N      N N N 439 
THR   CA     C N S 440 
THR   C      C N N 441 
THR   O      O N N 442 
THR   CB     C N R 443 
THR   OG1    O N N 444 
THR   CG2    C N N 445 
THR   OXT    O N N 446 
THR   H      H N N 447 
THR   H2     H N N 448 
THR   HA     H N N 449 
THR   HB     H N N 450 
THR   HG1    H N N 451 
THR   HG21   H N N 452 
THR   HG22   H N N 453 
THR   HG23   H N N 454 
THR   HXT    H N N 455 
TRP   N      N N N 456 
TRP   CA     C N S 457 
TRP   C      C N N 458 
TRP   O      O N N 459 
TRP   CB     C N N 460 
TRP   CG     C Y N 461 
TRP   CD1    C Y N 462 
TRP   CD2    C Y N 463 
TRP   NE1    N Y N 464 
TRP   CE2    C Y N 465 
TRP   CE3    C Y N 466 
TRP   CZ2    C Y N 467 
TRP   CZ3    C Y N 468 
TRP   CH2    C Y N 469 
TRP   OXT    O N N 470 
TRP   H      H N N 471 
TRP   H2     H N N 472 
TRP   HA     H N N 473 
TRP   HB2    H N N 474 
TRP   HB3    H N N 475 
TRP   HD1    H N N 476 
TRP   HE1    H N N 477 
TRP   HE3    H N N 478 
TRP   HZ2    H N N 479 
TRP   HZ3    H N N 480 
TRP   HH2    H N N 481 
TRP   HXT    H N N 482 
TYR   N      N N N 483 
TYR   CA     C N S 484 
TYR   C      C N N 485 
TYR   O      O N N 486 
TYR   CB     C N N 487 
TYR   CG     C Y N 488 
TYR   CD1    C Y N 489 
TYR   CD2    C Y N 490 
TYR   CE1    C Y N 491 
TYR   CE2    C Y N 492 
TYR   CZ     C Y N 493 
TYR   OH     O N N 494 
TYR   OXT    O N N 495 
TYR   H      H N N 496 
TYR   H2     H N N 497 
TYR   HA     H N N 498 
TYR   HB2    H N N 499 
TYR   HB3    H N N 500 
TYR   HD1    H N N 501 
TYR   HD2    H N N 502 
TYR   HE1    H N N 503 
TYR   HE2    H N N 504 
TYR   HH     H N N 505 
TYR   HXT    H N N 506 
VAL   N      N N N 507 
VAL   CA     C N S 508 
VAL   C      C N N 509 
VAL   O      O N N 510 
VAL   CB     C N N 511 
VAL   CG1    C N N 512 
VAL   CG2    C N N 513 
VAL   OXT    O N N 514 
VAL   H      H N N 515 
VAL   H2     H N N 516 
VAL   HA     H N N 517 
VAL   HB     H N N 518 
VAL   HG11   H N N 519 
VAL   HG12   H N N 520 
VAL   HG13   H N N 521 
VAL   HG21   H N N 522 
VAL   HG22   H N N 523 
VAL   HG23   H N N 524 
VAL   HXT    H N N 525 
# 
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 
A1BLG O1    C2     doub N N 1   
A1BLG C10   C7     sing N N 2   
A1BLG C10   C9     sing N N 3   
A1BLG N2    C7     sing N N 4   
A1BLG N2    C6     sing N N 5   
A1BLG C11   C6     doub Y N 6   
A1BLG C11   C3     sing Y N 7   
A1BLG C2    C3     sing N N 8   
A1BLG C2    N      sing N N 9   
A1BLG O     C      sing N N 10  
A1BLG C7    C8     sing N N 11  
A1BLG C6    N1     sing Y N 12  
A1BLG C     C1     sing N N 13  
A1BLG C     C12    sing N N 14  
A1BLG C3    C4     doub Y N 15  
A1BLG N3    C20    sing N N 16  
A1BLG N3    C12    sing N N 17  
A1BLG C9    C8     sing N N 18  
A1BLG C1    N      sing N N 19  
A1BLG C20   C19    sing N N 20  
A1BLG C12   C13    sing N N 21  
A1BLG N1    C5     doub Y N 22  
A1BLG C4    C5     sing Y N 23  
A1BLG C19   C18    doub Y N 24  
A1BLG C19   C14    sing Y N 25  
A1BLG C13   C14    sing N N 26  
A1BLG C18   C17    sing Y N 27  
A1BLG C14   C15    doub Y N 28  
A1BLG C17   C16    doub Y N 29  
A1BLG C15   C16    sing Y N 30  
A1BLG C1    H4     sing N N 31  
A1BLG C1    H3     sing N N 32  
A1BLG C4    H6     sing N N 33  
A1BLG C5    H7     sing N N 34  
A1BLG C7    H9     sing N N 35  
A1BLG N2    H8     sing N N 36  
A1BLG N3    H25    sing N N 37  
A1BLG C8    H11    sing N N 38  
A1BLG C8    H10    sing N N 39  
A1BLG C11   H16    sing N N 40  
A1BLG C10   H14    sing N N 41  
A1BLG C10   H15    sing N N 42  
A1BLG C9    H13    sing N N 43  
A1BLG C9    H12    sing N N 44  
A1BLG N     H5     sing N N 45  
A1BLG C     H      sing N N 46  
A1BLG O     H2     sing N N 47  
A1BLG C12   H1     sing N N 48  
A1BLG C20   H23    sing N N 49  
A1BLG C20   H24    sing N N 50  
A1BLG C13   H17    sing N N 51  
A1BLG C13   H18    sing N N 52  
A1BLG C18   H22    sing N N 53  
A1BLG C17   H21    sing N N 54  
A1BLG C16   H20    sing N N 55  
A1BLG C15   H19    sing N N 56  
ALA   N     CA     sing N N 57  
ALA   N     H      sing N N 58  
ALA   N     H2     sing N N 59  
ALA   CA    C      sing N N 60  
ALA   CA    CB     sing N N 61  
ALA   CA    HA     sing N N 62  
ALA   C     O      doub N N 63  
ALA   C     OXT    sing N N 64  
ALA   CB    HB1    sing N N 65  
ALA   CB    HB2    sing N N 66  
ALA   CB    HB3    sing N N 67  
ALA   OXT   HXT    sing N N 68  
ARG   N     CA     sing N N 69  
ARG   N     H      sing N N 70  
ARG   N     H2     sing N N 71  
ARG   CA    C      sing N N 72  
ARG   CA    CB     sing N N 73  
ARG   CA    HA     sing N N 74  
ARG   C     O      doub N N 75  
ARG   C     OXT    sing N N 76  
ARG   CB    CG     sing N N 77  
ARG   CB    HB2    sing N N 78  
ARG   CB    HB3    sing N N 79  
ARG   CG    CD     sing N N 80  
ARG   CG    HG2    sing N N 81  
ARG   CG    HG3    sing N N 82  
ARG   CD    NE     sing N N 83  
ARG   CD    HD2    sing N N 84  
ARG   CD    HD3    sing N N 85  
ARG   NE    CZ     sing N N 86  
ARG   NE    HE     sing N N 87  
ARG   CZ    NH1    sing N N 88  
ARG   CZ    NH2    doub N N 89  
ARG   NH1   HH11   sing N N 90  
ARG   NH1   HH12   sing N N 91  
ARG   NH2   HH21   sing N N 92  
ARG   NH2   HH22   sing N N 93  
ARG   OXT   HXT    sing N N 94  
ASN   N     CA     sing N N 95  
ASN   N     H      sing N N 96  
ASN   N     H2     sing N N 97  
ASN   CA    C      sing N N 98  
ASN   CA    CB     sing N N 99  
ASN   CA    HA     sing N N 100 
ASN   C     O      doub N N 101 
ASN   C     OXT    sing N N 102 
ASN   CB    CG     sing N N 103 
ASN   CB    HB2    sing N N 104 
ASN   CB    HB3    sing N N 105 
ASN   CG    OD1    doub N N 106 
ASN   CG    ND2    sing N N 107 
ASN   ND2   HD21   sing N N 108 
ASN   ND2   HD22   sing N N 109 
ASN   OXT   HXT    sing N N 110 
ASP   N     CA     sing N N 111 
ASP   N     H      sing N N 112 
ASP   N     H2     sing N N 113 
ASP   CA    C      sing N N 114 
ASP   CA    CB     sing N N 115 
ASP   CA    HA     sing N N 116 
ASP   C     O      doub N N 117 
ASP   C     OXT    sing N N 118 
ASP   CB    CG     sing N N 119 
ASP   CB    HB2    sing N N 120 
ASP   CB    HB3    sing N N 121 
ASP   CG    OD1    doub N N 122 
ASP   CG    OD2    sing N N 123 
ASP   OD2   HD2    sing N N 124 
ASP   OXT   HXT    sing N N 125 
CYS   N     CA     sing N N 126 
CYS   N     H      sing N N 127 
CYS   N     H2     sing N N 128 
CYS   CA    C      sing N N 129 
CYS   CA    CB     sing N N 130 
CYS   CA    HA     sing N N 131 
CYS   C     O      doub N N 132 
CYS   C     OXT    sing N N 133 
CYS   CB    SG     sing N N 134 
CYS   CB    HB2    sing N N 135 
CYS   CB    HB3    sing N N 136 
CYS   SG    HG     sing N N 137 
CYS   OXT   HXT    sing N N 138 
EDO   C1    O1     sing N N 139 
EDO   C1    C2     sing N N 140 
EDO   C1    H11    sing N N 141 
EDO   C1    H12    sing N N 142 
EDO   O1    HO1    sing N N 143 
EDO   C2    O2     sing N N 144 
EDO   C2    H21    sing N N 145 
EDO   C2    H22    sing N N 146 
EDO   O2    HO2    sing N N 147 
GLN   N     CA     sing N N 148 
GLN   N     H      sing N N 149 
GLN   N     H2     sing N N 150 
GLN   CA    C      sing N N 151 
GLN   CA    CB     sing N N 152 
GLN   CA    HA     sing N N 153 
GLN   C     O      doub N N 154 
GLN   C     OXT    sing N N 155 
GLN   CB    CG     sing N N 156 
GLN   CB    HB2    sing N N 157 
GLN   CB    HB3    sing N N 158 
GLN   CG    CD     sing N N 159 
GLN   CG    HG2    sing N N 160 
GLN   CG    HG3    sing N N 161 
GLN   CD    OE1    doub N N 162 
GLN   CD    NE2    sing N N 163 
GLN   NE2   HE21   sing N N 164 
GLN   NE2   HE22   sing N N 165 
GLN   OXT   HXT    sing N N 166 
GLU   N     CA     sing N N 167 
GLU   N     H      sing N N 168 
GLU   N     H2     sing N N 169 
GLU   CA    C      sing N N 170 
GLU   CA    CB     sing N N 171 
GLU   CA    HA     sing N N 172 
GLU   C     O      doub N N 173 
GLU   C     OXT    sing N N 174 
GLU   CB    CG     sing N N 175 
GLU   CB    HB2    sing N N 176 
GLU   CB    HB3    sing N N 177 
GLU   CG    CD     sing N N 178 
GLU   CG    HG2    sing N N 179 
GLU   CG    HG3    sing N N 180 
GLU   CD    OE1    doub N N 181 
GLU   CD    OE2    sing N N 182 
GLU   OE2   HE2    sing N N 183 
GLU   OXT   HXT    sing N N 184 
GLY   N     CA     sing N N 185 
GLY   N     H      sing N N 186 
GLY   N     H2     sing N N 187 
GLY   CA    C      sing N N 188 
GLY   CA    HA2    sing N N 189 
GLY   CA    HA3    sing N N 190 
GLY   C     O      doub N N 191 
GLY   C     OXT    sing N N 192 
GLY   OXT   HXT    sing N N 193 
HIS   N     CA     sing N N 194 
HIS   N     H      sing N N 195 
HIS   N     H2     sing N N 196 
HIS   CA    C      sing N N 197 
HIS   CA    CB     sing N N 198 
HIS   CA    HA     sing N N 199 
HIS   C     O      doub N N 200 
HIS   C     OXT    sing N N 201 
HIS   CB    CG     sing N N 202 
HIS   CB    HB2    sing N N 203 
HIS   CB    HB3    sing N N 204 
HIS   CG    ND1    sing Y N 205 
HIS   CG    CD2    doub Y N 206 
HIS   ND1   CE1    doub Y N 207 
HIS   ND1   HD1    sing N N 208 
HIS   CD2   NE2    sing Y N 209 
HIS   CD2   HD2    sing N N 210 
HIS   CE1   NE2    sing Y N 211 
HIS   CE1   HE1    sing N N 212 
HIS   NE2   HE2    sing N N 213 
HIS   OXT   HXT    sing N N 214 
HOH   O     H1     sing N N 215 
HOH   O     H2     sing N N 216 
ILE   N     CA     sing N N 217 
ILE   N     H      sing N N 218 
ILE   N     H2     sing N N 219 
ILE   CA    C      sing N N 220 
ILE   CA    CB     sing N N 221 
ILE   CA    HA     sing N N 222 
ILE   C     O      doub N N 223 
ILE   C     OXT    sing N N 224 
ILE   CB    CG1    sing N N 225 
ILE   CB    CG2    sing N N 226 
ILE   CB    HB     sing N N 227 
ILE   CG1   CD1    sing N N 228 
ILE   CG1   HG12   sing N N 229 
ILE   CG1   HG13   sing N N 230 
ILE   CG2   HG21   sing N N 231 
ILE   CG2   HG22   sing N N 232 
ILE   CG2   HG23   sing N N 233 
ILE   CD1   HD11   sing N N 234 
ILE   CD1   HD12   sing N N 235 
ILE   CD1   HD13   sing N N 236 
ILE   OXT   HXT    sing N N 237 
LEU   N     CA     sing N N 238 
LEU   N     H      sing N N 239 
LEU   N     H2     sing N N 240 
LEU   CA    C      sing N N 241 
LEU   CA    CB     sing N N 242 
LEU   CA    HA     sing N N 243 
LEU   C     O      doub N N 244 
LEU   C     OXT    sing N N 245 
LEU   CB    CG     sing N N 246 
LEU   CB    HB2    sing N N 247 
LEU   CB    HB3    sing N N 248 
LEU   CG    CD1    sing N N 249 
LEU   CG    CD2    sing N N 250 
LEU   CG    HG     sing N N 251 
LEU   CD1   HD11   sing N N 252 
LEU   CD1   HD12   sing N N 253 
LEU   CD1   HD13   sing N N 254 
LEU   CD2   HD21   sing N N 255 
LEU   CD2   HD22   sing N N 256 
LEU   CD2   HD23   sing N N 257 
LEU   OXT   HXT    sing N N 258 
LYS   N     CA     sing N N 259 
LYS   N     H      sing N N 260 
LYS   N     H2     sing N N 261 
LYS   CA    C      sing N N 262 
LYS   CA    CB     sing N N 263 
LYS   CA    HA     sing N N 264 
LYS   C     O      doub N N 265 
LYS   C     OXT    sing N N 266 
LYS   CB    CG     sing N N 267 
LYS   CB    HB2    sing N N 268 
LYS   CB    HB3    sing N N 269 
LYS   CG    CD     sing N N 270 
LYS   CG    HG2    sing N N 271 
LYS   CG    HG3    sing N N 272 
LYS   CD    CE     sing N N 273 
LYS   CD    HD2    sing N N 274 
LYS   CD    HD3    sing N N 275 
LYS   CE    NZ     sing N N 276 
LYS   CE    HE2    sing N N 277 
LYS   CE    HE3    sing N N 278 
LYS   NZ    HZ1    sing N N 279 
LYS   NZ    HZ2    sing N N 280 
LYS   NZ    HZ3    sing N N 281 
LYS   OXT   HXT    sing N N 282 
MET   N     CA     sing N N 283 
MET   N     H      sing N N 284 
MET   N     H2     sing N N 285 
MET   CA    C      sing N N 286 
MET   CA    CB     sing N N 287 
MET   CA    HA     sing N N 288 
MET   C     O      doub N N 289 
MET   C     OXT    sing N N 290 
MET   CB    CG     sing N N 291 
MET   CB    HB2    sing N N 292 
MET   CB    HB3    sing N N 293 
MET   CG    SD     sing N N 294 
MET   CG    HG2    sing N N 295 
MET   CG    HG3    sing N N 296 
MET   SD    CE     sing N N 297 
MET   CE    HE1    sing N N 298 
MET   CE    HE2    sing N N 299 
MET   CE    HE3    sing N N 300 
MET   OXT   HXT    sing N N 301 
PEG   C1    O1     sing N N 302 
PEG   C1    C2     sing N N 303 
PEG   C1    H11    sing N N 304 
PEG   C1    H12    sing N N 305 
PEG   O1    HO1    sing N N 306 
PEG   C2    O2     sing N N 307 
PEG   C2    H21    sing N N 308 
PEG   C2    H22    sing N N 309 
PEG   O2    C3     sing N N 310 
PEG   C3    C4     sing N N 311 
PEG   C3    H31    sing N N 312 
PEG   C3    H32    sing N N 313 
PEG   C4    O4     sing N N 314 
PEG   C4    H41    sing N N 315 
PEG   C4    H42    sing N N 316 
PEG   O4    HO4    sing N N 317 
PHE   N     CA     sing N N 318 
PHE   N     H      sing N N 319 
PHE   N     H2     sing N N 320 
PHE   CA    C      sing N N 321 
PHE   CA    CB     sing N N 322 
PHE   CA    HA     sing N N 323 
PHE   C     O      doub N N 324 
PHE   C     OXT    sing N N 325 
PHE   CB    CG     sing N N 326 
PHE   CB    HB2    sing N N 327 
PHE   CB    HB3    sing N N 328 
PHE   CG    CD1    doub Y N 329 
PHE   CG    CD2    sing Y N 330 
PHE   CD1   CE1    sing Y N 331 
PHE   CD1   HD1    sing N N 332 
PHE   CD2   CE2    doub Y N 333 
PHE   CD2   HD2    sing N N 334 
PHE   CE1   CZ     doub Y N 335 
PHE   CE1   HE1    sing N N 336 
PHE   CE2   CZ     sing Y N 337 
PHE   CE2   HE2    sing N N 338 
PHE   CZ    HZ     sing N N 339 
PHE   OXT   HXT    sing N N 340 
PRO   N     CA     sing N N 341 
PRO   N     CD     sing N N 342 
PRO   N     H      sing N N 343 
PRO   CA    C      sing N N 344 
PRO   CA    CB     sing N N 345 
PRO   CA    HA     sing N N 346 
PRO   C     O      doub N N 347 
PRO   C     OXT    sing N N 348 
PRO   CB    CG     sing N N 349 
PRO   CB    HB2    sing N N 350 
PRO   CB    HB3    sing N N 351 
PRO   CG    CD     sing N N 352 
PRO   CG    HG2    sing N N 353 
PRO   CG    HG3    sing N N 354 
PRO   CD    HD2    sing N N 355 
PRO   CD    HD3    sing N N 356 
PRO   OXT   HXT    sing N N 357 
SER   N     CA     sing N N 358 
SER   N     H      sing N N 359 
SER   N     H2     sing N N 360 
SER   CA    C      sing N N 361 
SER   CA    CB     sing N N 362 
SER   CA    HA     sing N N 363 
SER   C     O      doub N N 364 
SER   C     OXT    sing N N 365 
SER   CB    OG     sing N N 366 
SER   CB    HB2    sing N N 367 
SER   CB    HB3    sing N N 368 
SER   OG    HG     sing N N 369 
SER   OXT   HXT    sing N N 370 
SFG   N     CA     sing N N 371 
SFG   N     HN1    sing N N 372 
SFG   N     HN2    sing N N 373 
SFG   CA    C      sing N N 374 
SFG   CA    CB     sing N N 375 
SFG   CA    HA     sing N N 376 
SFG   C     O      doub N N 377 
SFG   C     OXT    sing N N 378 
SFG   OXT   HXT    sing N N 379 
SFG   CB    CG     sing N N 380 
SFG   CB    HB1    sing N N 381 
SFG   CB    HB2    sing N N 382 
SFG   CG    CD     sing N N 383 
SFG   CG    HG1    sing N N 384 
SFG   CG    HG2    sing N N 385 
SFG   CD    NE     sing N N 386 
SFG   CD    "C5'"  sing N N 387 
SFG   CD    HD     sing N N 388 
SFG   NE    HNE1   sing N N 389 
SFG   NE    HNE2   sing N N 390 
SFG   "C5'" "C4'"  sing N N 391 
SFG   "C5'" "H5'1" sing N N 392 
SFG   "C5'" "H5'2" sing N N 393 
SFG   "C4'" "O4'"  sing N N 394 
SFG   "C4'" "C3'"  sing N N 395 
SFG   "C4'" "H4'"  sing N N 396 
SFG   "O4'" "C1'"  sing N N 397 
SFG   "C3'" "O3'"  sing N N 398 
SFG   "C3'" "C2'"  sing N N 399 
SFG   "C3'" "H3'"  sing N N 400 
SFG   "O3'" "HO3'" sing N N 401 
SFG   "C2'" "O2'"  sing N N 402 
SFG   "C2'" "C1'"  sing N N 403 
SFG   "C2'" "H2'"  sing N N 404 
SFG   "O2'" "HO2'" sing N N 405 
SFG   "C1'" N9     sing N N 406 
SFG   "C1'" "H1'"  sing N N 407 
SFG   N9    C8     sing Y N 408 
SFG   N9    C4     sing Y N 409 
SFG   C8    N7     doub Y N 410 
SFG   C8    H8     sing N N 411 
SFG   N7    C5     sing Y N 412 
SFG   C5    C6     sing Y N 413 
SFG   C5    C4     doub Y N 414 
SFG   C6    N6     sing N N 415 
SFG   C6    N1     doub Y N 416 
SFG   N6    HN61   sing N N 417 
SFG   N6    HN62   sing N N 418 
SFG   N1    C2     sing Y N 419 
SFG   C2    N3     doub Y N 420 
SFG   C2    H2     sing N N 421 
SFG   N3    C4     sing Y N 422 
SO4   S     O1     doub N N 423 
SO4   S     O2     doub N N 424 
SO4   S     O3     sing N N 425 
SO4   S     O4     sing N N 426 
THR   N     CA     sing N N 427 
THR   N     H      sing N N 428 
THR   N     H2     sing N N 429 
THR   CA    C      sing N N 430 
THR   CA    CB     sing N N 431 
THR   CA    HA     sing N N 432 
THR   C     O      doub N N 433 
THR   C     OXT    sing N N 434 
THR   CB    OG1    sing N N 435 
THR   CB    CG2    sing N N 436 
THR   CB    HB     sing N N 437 
THR   OG1   HG1    sing N N 438 
THR   CG2   HG21   sing N N 439 
THR   CG2   HG22   sing N N 440 
THR   CG2   HG23   sing N N 441 
THR   OXT   HXT    sing N N 442 
TRP   N     CA     sing N N 443 
TRP   N     H      sing N N 444 
TRP   N     H2     sing N N 445 
TRP   CA    C      sing N N 446 
TRP   CA    CB     sing N N 447 
TRP   CA    HA     sing N N 448 
TRP   C     O      doub N N 449 
TRP   C     OXT    sing N N 450 
TRP   CB    CG     sing N N 451 
TRP   CB    HB2    sing N N 452 
TRP   CB    HB3    sing N N 453 
TRP   CG    CD1    doub Y N 454 
TRP   CG    CD2    sing Y N 455 
TRP   CD1   NE1    sing Y N 456 
TRP   CD1   HD1    sing N N 457 
TRP   CD2   CE2    doub Y N 458 
TRP   CD2   CE3    sing Y N 459 
TRP   NE1   CE2    sing Y N 460 
TRP   NE1   HE1    sing N N 461 
TRP   CE2   CZ2    sing Y N 462 
TRP   CE3   CZ3    doub Y N 463 
TRP   CE3   HE3    sing N N 464 
TRP   CZ2   CH2    doub Y N 465 
TRP   CZ2   HZ2    sing N N 466 
TRP   CZ3   CH2    sing Y N 467 
TRP   CZ3   HZ3    sing N N 468 
TRP   CH2   HH2    sing N N 469 
TRP   OXT   HXT    sing N N 470 
TYR   N     CA     sing N N 471 
TYR   N     H      sing N N 472 
TYR   N     H2     sing N N 473 
TYR   CA    C      sing N N 474 
TYR   CA    CB     sing N N 475 
TYR   CA    HA     sing N N 476 
TYR   C     O      doub N N 477 
TYR   C     OXT    sing N N 478 
TYR   CB    CG     sing N N 479 
TYR   CB    HB2    sing N N 480 
TYR   CB    HB3    sing N N 481 
TYR   CG    CD1    doub Y N 482 
TYR   CG    CD2    sing Y N 483 
TYR   CD1   CE1    sing Y N 484 
TYR   CD1   HD1    sing N N 485 
TYR   CD2   CE2    doub Y N 486 
TYR   CD2   HD2    sing N N 487 
TYR   CE1   CZ     doub Y N 488 
TYR   CE1   HE1    sing N N 489 
TYR   CE2   CZ     sing Y N 490 
TYR   CE2   HE2    sing N N 491 
TYR   CZ    OH     sing N N 492 
TYR   OH    HH     sing N N 493 
TYR   OXT   HXT    sing N N 494 
VAL   N     CA     sing N N 495 
VAL   N     H      sing N N 496 
VAL   N     H2     sing N N 497 
VAL   CA    C      sing N N 498 
VAL   CA    CB     sing N N 499 
VAL   CA    HA     sing N N 500 
VAL   C     O      doub N N 501 
VAL   C     OXT    sing N N 502 
VAL   CB    CG1    sing N N 503 
VAL   CB    CG2    sing N N 504 
VAL   CB    HB     sing N N 505 
VAL   CG1   HG11   sing N N 506 
VAL   CG1   HG12   sing N N 507 
VAL   CG1   HG13   sing N N 508 
VAL   CG2   HG21   sing N N 509 
VAL   CG2   HG22   sing N N 510 
VAL   CG2   HG23   sing N N 511 
VAL   OXT   HXT    sing N N 512 
# 
_pdbx_audit_support.funding_organization   'Other private' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4X60 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9MGQ 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.009837 
_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]   0.007262 
_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]   0.005618 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N      . VAL   A  1 22  ? 39.038 -70.946  -19.602 1.00 49.58  ? 14   VAL   A N      1 
ATOM   2    C CA     . VAL   A  1 22  ? 38.207 -71.916  -20.318 1.00 49.13  ? 14   VAL   A CA     1 
ATOM   3    C C      . VAL   A  1 22  ? 38.008 -73.194  -19.501 1.00 49.64  ? 14   VAL   A C      1 
ATOM   4    O O      . VAL   A  1 22  ? 38.962 -73.949  -19.278 1.00 49.40  ? 14   VAL   A O      1 
ATOM   5    C CB     . VAL   A  1 22  ? 38.712 -72.201  -21.770 1.00 53.86  ? 14   VAL   A CB     1 
ATOM   6    C CG1    . VAL   A  1 22  ? 38.095 -73.470  -22.365 1.00 53.93  ? 14   VAL   A CG1    1 
ATOM   7    C CG2    . VAL   A  1 22  ? 38.428 -71.020  -22.677 1.00 53.86  ? 14   VAL   A CG2    1 
ATOM   8    N N      . SER   A  1 23  ? 36.759 -73.424  -19.056 1.00 43.46  ? 15   SER   A N      1 
ATOM   9    C CA     . SER   A  1 23  ? 36.370 -74.640  -18.348 1.00 41.93  ? 15   SER   A CA     1 
ATOM   10   C C      . SER   A  1 23  ? 36.051 -75.634  -19.458 1.00 42.71  ? 15   SER   A C      1 
ATOM   11   O O      . SER   A  1 23  ? 35.176 -75.379  -20.295 1.00 41.39  ? 15   SER   A O      1 
ATOM   12   C CB     . SER   A  1 23  ? 35.162 -74.400  -17.451 1.00 45.57  ? 15   SER   A CB     1 
ATOM   13   O OG     . SER   A  1 23  ? 34.944 -75.547  -16.647 1.00 55.87  ? 15   SER   A OG     1 
ATOM   14   N N      . SER   A  1 24  ? 36.840 -76.709  -19.535 1.00 37.70  ? 16   SER   A N      1 
ATOM   15   C CA     . SER   A  1 24  ? 36.717 -77.665  -20.625 1.00 36.94  ? 16   SER   A CA     1 
ATOM   16   C C      . SER   A  1 24  ? 36.528 -79.111  -20.202 1.00 36.32  ? 16   SER   A C      1 
ATOM   17   O O      . SER   A  1 24  ? 37.034 -79.539  -19.168 1.00 35.93  ? 16   SER   A O      1 
ATOM   18   C CB     . SER   A  1 24  ? 37.914 -77.543  -21.555 1.00 43.23  ? 16   SER   A CB     1 
ATOM   19   O OG     . SER   A  1 24  ? 39.112 -77.846  -20.854 1.00 58.97  ? 16   SER   A OG     1 
ATOM   20   N N      . GLY   A  1 25  ? 35.804 -79.849  -21.031 1.00 29.84  ? 17   GLY   A N      1 
ATOM   21   C CA     . GLY   A  1 25  ? 35.513 -81.253  -20.803 1.00 28.32  ? 17   GLY   A CA     1 
ATOM   22   C C      . GLY   A  1 25  ? 35.785 -82.123  -22.004 1.00 29.82  ? 17   GLY   A C      1 
ATOM   23   O O      . GLY   A  1 25  ? 35.825 -81.647  -23.144 1.00 28.85  ? 17   GLY   A O      1 
ATOM   24   N N      . ARG   A  1 26  ? 36.021 -83.397  -21.735 1.00 26.28  ? 18   ARG   A N      1 
ATOM   25   C CA     . ARG   A  1 26  ? 36.262 -84.409  -22.741 1.00 26.41  ? 18   ARG   A CA     1 
ATOM   26   C C      . ARG   A  1 26  ? 35.062 -85.322  -22.760 1.00 30.05  ? 18   ARG   A C      1 
ATOM   27   O O      . ARG   A  1 26  ? 34.654 -85.820  -21.710 1.00 30.23  ? 18   ARG   A O      1 
ATOM   28   C CB     . ARG   A  1 26  ? 37.531 -85.229  -22.395 1.00 26.88  ? 18   ARG   A CB     1 
ATOM   29   C CG     . ARG   A  1 26  ? 37.869 -86.341  -23.391 1.00 30.45  ? 18   ARG   A CG     1 
ATOM   30   C CD     . ARG   A  1 26  ? 38.442 -85.781  -24.688 1.00 39.78  ? 18   ARG   A CD     1 
ATOM   31   N NE     . ARG   A  1 26  ? 38.861 -86.842  -25.602 1.00 42.45  ? 18   ARG   A NE     1 
ATOM   32   C CZ     . ARG   A  1 26  ? 38.184 -87.222  -26.679 1.00 52.15  ? 18   ARG   A CZ     1 
ATOM   33   N NH1    . ARG   A  1 26  ? 37.053 -86.612  -27.012 1.00 37.18  ? 18   ARG   A NH1    1 
ATOM   34   N NH2    . ARG   A  1 26  ? 38.650 -88.191  -27.454 1.00 40.35  ? 18   ARG   A NH2    1 
ATOM   35   N N      . ASP   A  1 27  ? 34.521 -85.573  -23.949 1.00 25.84  ? 19   ASP   A N      1 
ATOM   36   C CA     . ASP   A  1 27  ? 33.416 -86.503  -24.112 1.00 25.18  ? 19   ASP   A CA     1 
ATOM   37   C C      . ASP   A  1 27  ? 33.997 -87.835  -24.583 1.00 29.81  ? 19   ASP   A C      1 
ATOM   38   O O      . ASP   A  1 27  ? 34.772 -87.860  -25.540 1.00 30.66  ? 19   ASP   A O      1 
ATOM   39   C CB     . ASP   A  1 27  ? 32.395 -85.972  -25.137 1.00 26.44  ? 19   ASP   A CB     1 
ATOM   40   C CG     . ASP   A  1 27  ? 31.180 -86.864  -25.302 1.00 36.76  ? 19   ASP   A CG     1 
ATOM   41   O OD1    . ASP   A  1 27  ? 30.731 -87.446  -24.292 1.00 38.44  ? 19   ASP   A OD1    1 
ATOM   42   O OD2    . ASP   A  1 27  ? 30.674 -86.977  -26.441 1.00 39.27  ? 19   ASP   A OD2    1 
ATOM   43   N N      . LEU   A  1 28  ? 33.639 -88.932  -23.914 1.00 26.30  ? 20   LEU   A N      1 
ATOM   44   C CA     . LEU   A  1 28  ? 34.106 -90.270  -24.289 1.00 26.70  ? 20   LEU   A CA     1 
ATOM   45   C C      . LEU   A  1 28  ? 32.970 -91.289  -24.201 1.00 31.71  ? 20   LEU   A C      1 
ATOM   46   O O      . LEU   A  1 28  ? 32.164 -91.243  -23.263 1.00 30.92  ? 20   LEU   A O      1 
ATOM   47   C CB     . LEU   A  1 28  ? 35.293 -90.720  -23.405 1.00 26.58  ? 20   LEU   A CB     1 
ATOM   48   C CG     . LEU   A  1 28  ? 36.654 -90.018  -23.621 1.00 31.79  ? 20   LEU   A CG     1 
ATOM   49   C CD1    . LEU   A  1 28  ? 37.696 -90.523  -22.621 1.00 31.98  ? 20   LEU   A CD1    1 
ATOM   50   C CD2    . LEU   A  1 28  ? 37.198 -90.254  -25.026 1.00 34.80  ? 20   LEU   A CD2    1 
ATOM   51   N N      . ASN   A  1 29  ? 32.894 -92.196  -25.181 1.00 28.40  ? 21   ASN   A N      1 
ATOM   52   C CA     . ASN   A  1 29  ? 31.892 -93.258  -25.156 1.00 28.70  ? 21   ASN   A CA     1 
ATOM   53   C C      . ASN   A  1 29  ? 32.531 -94.627  -24.885 1.00 33.75  ? 21   ASN   A C      1 
ATOM   54   O O      . ASN   A  1 29  ? 31.847 -95.658  -24.907 1.00 33.91  ? 21   ASN   A O      1 
ATOM   55   C CB     . ASN   A  1 29  ? 31.011 -93.246  -26.406 1.00 29.44  ? 21   ASN   A CB     1 
ATOM   56   C CG     . ASN   A  1 29  ? 29.544 -93.448  -26.094 1.00 50.63  ? 21   ASN   A CG     1 
ATOM   57   O OD1    . ASN   A  1 29  ? 29.030 -93.042  -25.032 1.00 43.30  ? 21   ASN   A OD1    1 
ATOM   58   N ND2    . ASN   A  1 29  ? 28.831 -94.072  -27.019 1.00 42.87  ? 21   ASN   A ND2    1 
ATOM   59   N N      . CYS   A  1 30  ? 33.852 -94.624  -24.603 1.00 29.64  ? 22   CYS   A N      1 
ATOM   60   C CA     . CYS   A  1 30  ? 34.617 -95.824  -24.278 1.00 28.73  ? 22   CYS   A CA     1 
ATOM   61   C C      . CYS   A  1 30  ? 35.517 -95.542  -23.095 1.00 31.38  ? 22   CYS   A C      1 
ATOM   62   O O      . CYS   A  1 30  ? 36.399 -94.688  -23.183 1.00 31.15  ? 22   CYS   A O      1 
ATOM   63   C CB     . CYS   A  1 30  ? 35.411 -96.322  -25.480 1.00 28.91  ? 22   CYS   A CB     1 
ATOM   64   S SG     . CYS   A  1 30  ? 36.480 -97.737  -25.111 1.00 32.64  ? 22   CYS   A SG     1 
ATOM   65   N N      . VAL   A  1 31  ? 35.270 -96.237  -21.975 1.00 27.91  ? 23   VAL   A N      1 
ATOM   66   C CA     . VAL   A  1 31  ? 36.010 -96.054  -20.724 1.00 28.16  ? 23   VAL   A CA     1 
ATOM   67   C C      . VAL   A  1 31  ? 36.347 -97.445  -20.163 1.00 32.91  ? 23   VAL   A C      1 
ATOM   68   O O      . VAL   A  1 31  ? 35.569 -97.988  -19.368 1.00 31.82  ? 23   VAL   A O      1 
ATOM   69   C CB     . VAL   A  1 31  ? 35.258 -95.150  -19.685 1.00 31.58  ? 23   VAL   A CB     1 
ATOM   70   C CG1    . VAL   A  1 31  ? 36.151 -94.808  -18.493 1.00 31.02  ? 23   VAL   A CG1    1 
ATOM   71   C CG2    . VAL   A  1 31  ? 34.715 -93.872  -20.319 1.00 31.55  ? 23   VAL   A CG2    1 
ATOM   72   N N      . PRO   A  1 32  ? 37.470 -98.068  -20.614 1.00 30.18  ? 24   PRO   A N      1 
ATOM   73   C CA     . PRO   A  1 32  ? 37.811 -99.418  -20.120 1.00 29.52  ? 24   PRO   A CA     1 
ATOM   74   C C      . PRO   A  1 32  ? 38.073 -99.459  -18.609 1.00 33.35  ? 24   PRO   A C      1 
ATOM   75   O O      . PRO   A  1 32  ? 37.523 -100.318 -17.926 1.00 32.93  ? 24   PRO   A O      1 
ATOM   76   C CB     . PRO   A  1 32  ? 39.047 -99.801  -20.949 1.00 31.05  ? 24   PRO   A CB     1 
ATOM   77   C CG     . PRO   A  1 32  ? 39.013 -98.880  -22.146 1.00 35.20  ? 24   PRO   A CG     1 
ATOM   78   C CD     . PRO   A  1 32  ? 38.463 -97.599  -21.603 1.00 31.03  ? 24   PRO   A CD     1 
ATOM   79   N N      . GLU   A  1 33  ? 38.892 -98.525  -18.105 1.00 31.47  ? 25   GLU   A N      1 
ATOM   80   C CA     . GLU   A  1 33  ? 39.242 -98.357  -16.689 1.00 32.84  ? 25   GLU   A CA     1 
ATOM   81   C C      . GLU   A  1 33  ? 38.980 -96.890  -16.346 1.00 36.77  ? 25   GLU   A C      1 
ATOM   82   O O      . GLU   A  1 33  ? 39.570 -96.003  -16.971 1.00 35.64  ? 25   GLU   A O      1 
ATOM   83   C CB     . GLU   A  1 33  ? 40.723 -98.710  -16.449 1.00 34.71  ? 25   GLU   A CB     1 
ATOM   84   C CG     . GLU   A  1 33  ? 41.067 -99.001  -15.001 1.00 49.40  ? 25   GLU   A CG     1 
ATOM   85   C CD     . GLU   A  1 33  ? 40.843 -100.440 -14.588 1.00 82.74  ? 25   GLU   A CD     1 
ATOM   86   O OE1    . GLU   A  1 33  ? 41.610 -101.317 -15.046 1.00 82.55  ? 25   GLU   A OE1    1 
ATOM   87   O OE2    . GLU   A  1 33  ? 39.914 -100.686 -13.786 1.00 84.39  ? 25   GLU   A OE2    1 
ATOM   88   N N      . ILE   A  1 34  ? 38.089 -96.634  -15.372 1.00 34.43  ? 26   ILE   A N      1 
ATOM   89   C CA     . ILE   A  1 34  ? 37.689 -95.272  -15.002 1.00 35.24  ? 26   ILE   A CA     1 
ATOM   90   C C      . ILE   A  1 34  ? 38.859 -94.432  -14.431 1.00 41.00  ? 26   ILE   A C      1 
ATOM   91   O O      . ILE   A  1 34  ? 38.999 -93.284  -14.844 1.00 40.75  ? 26   ILE   A O      1 
ATOM   92   C CB     . ILE   A  1 34  ? 36.420 -95.248  -14.099 1.00 38.80  ? 26   ILE   A CB     1 
ATOM   93   C CG1    . ILE   A  1 34  ? 35.751 -93.859  -14.106 1.00 39.65  ? 26   ILE   A CG1    1 
ATOM   94   C CG2    . ILE   A  1 34  ? 36.671 -95.765  -12.671 1.00 40.64  ? 26   ILE   A CG2    1 
ATOM   95   C CD1    . ILE   A  1 34  ? 34.360 -93.836  -13.529 1.00 48.54  ? 26   ILE   A CD1    1 
ATOM   96   N N      . ALA   A  1 35  ? 39.700 -94.988  -13.536 1.00 39.82  ? 27   ALA   A N      1 
ATOM   97   C CA     . ALA   A  1 35  ? 40.820 -94.241  -12.942 1.00 40.80  ? 27   ALA   A CA     1 
ATOM   98   C C      . ALA   A  1 35  ? 41.917 -93.898  -13.946 1.00 44.35  ? 27   ALA   A C      1 
ATOM   99   O O      . ALA   A  1 35  ? 42.423 -92.775  -13.917 1.00 43.76  ? 27   ALA   A O      1 
ATOM   100  C CB     . ALA   A  1 35  ? 41.397 -94.988  -11.749 1.00 41.95  ? 27   ALA   A CB     1 
ATOM   101  N N      . ASP   A  1 36  ? 42.257 -94.844  -14.853 1.00 41.12  ? 28   ASP   A N      1 
ATOM   102  C CA     . ASP   A  1 36  ? 43.261 -94.649  -15.909 1.00 41.03  ? 28   ASP   A CA     1 
ATOM   103  C C      . ASP   A  1 36  ? 42.821 -93.571  -16.903 1.00 43.32  ? 28   ASP   A C      1 
ATOM   104  O O      . ASP   A  1 36  ? 43.610 -92.686  -17.241 1.00 42.64  ? 28   ASP   A O      1 
ATOM   105  C CB     . ASP   A  1 36  ? 43.550 -95.971  -16.649 1.00 43.50  ? 28   ASP   A CB     1 
ATOM   106  C CG     . ASP   A  1 36  ? 44.214 -97.054  -15.808 1.00 60.81  ? 28   ASP   A CG     1 
ATOM   107  O OD1    . ASP   A  1 36  ? 44.839 -96.713  -14.772 1.00 63.10  ? 28   ASP   A OD1    1 
ATOM   108  O OD2    . ASP   A  1 36  ? 44.147 -98.239  -16.206 1.00 67.07  ? 28   ASP   A OD2    1 
ATOM   109  N N      . THR   A  1 37  ? 41.547 -93.628  -17.329 1.00 38.99  ? 29   THR   A N      1 
ATOM   110  C CA     . THR   A  1 37  ? 40.939 -92.700  -18.280 1.00 38.19  ? 29   THR   A CA     1 
ATOM   111  C C      . THR   A  1 37  ? 40.867 -91.282  -17.711 1.00 41.01  ? 29   THR   A C      1 
ATOM   112  O O      . THR   A  1 37  ? 41.264 -90.336  -18.396 1.00 41.08  ? 29   THR   A O      1 
ATOM   113  C CB     . THR   A  1 37  ? 39.593 -93.256  -18.755 1.00 42.86  ? 29   THR   A CB     1 
ATOM   114  O OG1    . THR   A  1 37  ? 39.821 -94.515  -19.391 1.00 40.86  ? 29   THR   A OG1    1 
ATOM   115  C CG2    . THR   A  1 37  ? 38.878 -92.330  -19.713 1.00 40.31  ? 29   THR   A CG2    1 
ATOM   116  N N      . LEU   A  1 38  ? 40.387 -91.138  -16.466 1.00 37.00  ? 30   LEU   A N      1 
ATOM   117  C CA     . LEU   A  1 38  ? 40.289 -89.836  -15.804 1.00 36.73  ? 30   LEU   A CA     1 
ATOM   118  C C      . LEU   A  1 38  ? 41.668 -89.191  -15.666 1.00 40.20  ? 30   LEU   A C      1 
ATOM   119  O O      . LEU   A  1 38  ? 41.821 -88.012  -15.984 1.00 38.99  ? 30   LEU   A O      1 
ATOM   120  C CB     . LEU   A  1 38  ? 39.571 -89.959  -14.445 1.00 36.97  ? 30   LEU   A CB     1 
ATOM   121  C CG     . LEU   A  1 38  ? 39.106 -88.654  -13.784 1.00 41.68  ? 30   LEU   A CG     1 
ATOM   122  C CD1    . LEU   A  1 38  ? 38.090 -87.918  -14.642 1.00 41.82  ? 30   LEU   A CD1    1 
ATOM   123  C CD2    . LEU   A  1 38  ? 38.530 -88.916  -12.415 1.00 44.15  ? 30   LEU   A CD2    1 
ATOM   124  N N      . GLY   A  1 39  ? 42.662 -89.990  -15.265 1.00 37.92  ? 31   GLY   A N      1 
ATOM   125  C CA     . GLY   A  1 39  ? 44.052 -89.557  -15.149 1.00 37.73  ? 31   GLY   A CA     1 
ATOM   126  C C      . GLY   A  1 39  ? 44.613 -89.093  -16.480 1.00 42.17  ? 31   GLY   A C      1 
ATOM   127  O O      . GLY   A  1 39  ? 45.289 -88.062  -16.542 1.00 42.03  ? 31   GLY   A O      1 
ATOM   128  N N      . ALA   A  1 40  ? 44.287 -89.832  -17.569 1.00 38.96  ? 32   ALA   A N      1 
ATOM   129  C CA     . ALA   A  1 40  ? 44.706 -89.507  -18.933 1.00 38.94  ? 32   ALA   A CA     1 
ATOM   130  C C      . ALA   A  1 40  ? 44.087 -88.191  -19.433 1.00 43.98  ? 32   ALA   A C      1 
ATOM   131  O O      . ALA   A  1 40  ? 44.807 -87.383  -20.025 1.00 43.93  ? 32   ALA   A O      1 
ATOM   132  C CB     . ALA   A  1 40  ? 44.365 -90.647  -19.877 1.00 39.53  ? 32   ALA   A CB     1 
ATOM   133  N N      . VAL   A  1 41  ? 42.773 -87.956  -19.168 1.00 40.86  ? 33   VAL   A N      1 
ATOM   134  C CA     . VAL   A  1 41  ? 42.090 -86.726  -19.601 1.00 40.41  ? 33   VAL   A CA     1 
ATOM   135  C C      . VAL   A  1 41  ? 42.559 -85.518  -18.766 1.00 44.35  ? 33   VAL   A C      1 
ATOM   136  O O      . VAL   A  1 41  ? 42.724 -84.433  -19.327 1.00 43.38  ? 33   VAL   A O      1 
ATOM   137  C CB     . VAL   A  1 41  ? 40.533 -86.820  -19.719 1.00 44.48  ? 33   VAL   A CB     1 
ATOM   138  C CG1    . VAL   A  1 41  ? 40.108 -87.956  -20.651 1.00 44.05  ? 33   VAL   A CG1    1 
ATOM   139  C CG2    . VAL   A  1 41  ? 39.841 -86.947  -18.364 1.00 44.51  ? 33   VAL   A CG2    1 
ATOM   140  N N      . ALA   A  1 42  ? 42.809 -85.713  -17.446 1.00 41.64  ? 34   ALA   A N      1 
ATOM   141  C CA     . ALA   A  1 42  ? 43.298 -84.654  -16.556 1.00 42.03  ? 34   ALA   A CA     1 
ATOM   142  C C      . ALA   A  1 42  ? 44.694 -84.202  -16.987 1.00 47.64  ? 34   ALA   A C      1 
ATOM   143  O O      . ALA   A  1 42  ? 44.961 -82.999  -17.005 1.00 47.20  ? 34   ALA   A O      1 
ATOM   144  C CB     . ALA   A  1 42  ? 43.314 -85.136  -15.113 1.00 42.77  ? 34   ALA   A CB     1 
ATOM   145  N N      . LYS   A  1 43  ? 45.559 -85.167  -17.398 1.00 45.71  ? 35   LYS   A N      1 
ATOM   146  C CA     . LYS   A  1 43  ? 46.918 -84.920  -17.903 1.00 45.87  ? 35   LYS   A CA     1 
ATOM   147  C C      . LYS   A  1 43  ? 46.864 -84.039  -19.168 1.00 49.64  ? 35   LYS   A C      1 
ATOM   148  O O      . LYS   A  1 43  ? 47.711 -83.157  -19.333 1.00 50.42  ? 35   LYS   A O      1 
ATOM   149  C CB     . LYS   A  1 43  ? 47.633 -86.253  -18.200 1.00 48.61  ? 35   LYS   A CB     1 
ATOM   150  C CG     . LYS   A  1 43  ? 49.154 -86.155  -18.268 1.00 68.77  ? 35   LYS   A CG     1 
ATOM   151  C CD     . LYS   A  1 43  ? 49.806 -86.432  -16.914 1.00 81.47  ? 35   LYS   A CD     1 
ATOM   152  C CE     . LYS   A  1 43  ? 51.311 -86.320  -16.961 1.00 93.20  ? 35   LYS   A CE     1 
ATOM   153  N NZ     . LYS   A  1 43  ? 51.920 -86.531  -15.620 1.00 102.12 ? 35   LYS   A NZ     1 
ATOM   154  N N      . GLN   A  1 44  ? 45.838 -84.257  -20.028 1.00 43.97  ? 36   GLN   A N      1 
ATOM   155  C CA     . GLN   A  1 44  ? 45.596 -83.495  -21.264 1.00 42.47  ? 36   GLN   A CA     1 
ATOM   156  C C      . GLN   A  1 44  ? 45.122 -82.051  -20.994 1.00 44.84  ? 36   GLN   A C      1 
ATOM   157  O O      . GLN   A  1 44  ? 45.157 -81.215  -21.895 1.00 44.49  ? 36   GLN   A O      1 
ATOM   158  C CB     . GLN   A  1 44  ? 44.604 -84.236  -22.181 1.00 43.35  ? 36   GLN   A CB     1 
ATOM   159  C CG     . GLN   A  1 44  ? 45.162 -85.505  -22.817 1.00 48.30  ? 36   GLN   A CG     1 
ATOM   160  C CD     . GLN   A  1 44  ? 44.110 -86.404  -23.437 1.00 66.42  ? 36   GLN   A CD     1 
ATOM   161  O OE1    . GLN   A  1 44  ? 42.916 -86.360  -23.108 1.00 61.33  ? 36   GLN   A OE1    1 
ATOM   162  N NE2    . GLN   A  1 44  ? 44.548 -87.300  -24.308 1.00 58.67  ? 36   GLN   A NE2    1 
ATOM   163  N N      . GLY   A  1 45  ? 44.687 -81.778  -19.766 1.00 41.02  ? 37   GLY   A N      1 
ATOM   164  C CA     . GLY   A  1 45  ? 44.246 -80.450  -19.346 1.00 40.12  ? 37   GLY   A CA     1 
ATOM   165  C C      . GLY   A  1 45  ? 42.752 -80.241  -19.210 1.00 41.42  ? 37   GLY   A C      1 
ATOM   166  O O      . GLY   A  1 45  ? 42.316 -79.104  -19.009 1.00 40.54  ? 37   GLY   A O      1 
ATOM   167  N N      . PHE   A  1 46  ? 41.952 -81.321  -19.337 1.00 36.25  ? 38   PHE   A N      1 
ATOM   168  C CA     . PHE   A  1 46  ? 40.496 -81.250  -19.199 1.00 34.61  ? 38   PHE   A CA     1 
ATOM   169  C C      . PHE   A  1 46  ? 40.087 -81.171  -17.724 1.00 37.91  ? 38   PHE   A C      1 
ATOM   170  O O      . PHE   A  1 46  ? 40.662 -81.859  -16.881 1.00 37.01  ? 38   PHE   A O      1 
ATOM   171  C CB     . PHE   A  1 46  ? 39.815 -82.443  -19.881 1.00 35.49  ? 38   PHE   A CB     1 
ATOM   172  C CG     . PHE   A  1 46  ? 40.001 -82.497  -21.377 1.00 36.34  ? 38   PHE   A CG     1 
ATOM   173  C CD1    . PHE   A  1 46  ? 39.137 -81.818  -22.226 1.00 38.45  ? 38   PHE   A CD1    1 
ATOM   174  C CD2    . PHE   A  1 46  ? 41.035 -83.239  -21.941 1.00 37.71  ? 38   PHE   A CD2    1 
ATOM   175  C CE1    . PHE   A  1 46  ? 39.293 -81.892  -23.614 1.00 39.04  ? 38   PHE   A CE1    1 
ATOM   176  C CE2    . PHE   A  1 46  ? 41.207 -83.292  -23.328 1.00 39.84  ? 38   PHE   A CE2    1 
ATOM   177  C CZ     . PHE   A  1 46  ? 40.339 -82.614  -24.155 1.00 37.90  ? 38   PHE   A CZ     1 
ATOM   178  N N      . ASP   A  1 47  ? 39.078 -80.336  -17.428 1.00 34.24  ? 39   ASP   A N      1 
ATOM   179  C CA     . ASP   A  1 47  ? 38.527 -80.124  -16.086 1.00 33.35  ? 39   ASP   A CA     1 
ATOM   180  C C      . ASP   A  1 47  ? 37.475 -81.168  -15.727 1.00 33.96  ? 39   ASP   A C      1 
ATOM   181  O O      . ASP   A  1 47  ? 37.207 -81.377  -14.543 1.00 34.32  ? 39   ASP   A O      1 
ATOM   182  C CB     . ASP   A  1 47  ? 37.942 -78.707  -15.955 1.00 35.63  ? 39   ASP   A CB     1 
ATOM   183  C CG     . ASP   A  1 47  ? 38.955 -77.610  -16.202 1.00 52.14  ? 39   ASP   A CG     1 
ATOM   184  O OD1    . ASP   A  1 47  ? 39.998 -77.596  -15.508 1.00 54.30  ? 39   ASP   A OD1    1 
ATOM   185  O OD2    . ASP   A  1 47  ? 38.719 -76.779  -17.104 1.00 59.80  ? 39   ASP   A OD2    1 
ATOM   186  N N      . PHE   A  1 48  ? 36.877 -81.820  -16.738 1.00 26.72  ? 40   PHE   A N      1 
ATOM   187  C CA     . PHE   A  1 48  ? 35.860 -82.856  -16.523 1.00 24.93  ? 40   PHE   A CA     1 
ATOM   188  C C      . PHE   A  1 48  ? 35.770 -83.837  -17.673 1.00 26.13  ? 40   PHE   A C      1 
ATOM   189  O O      . PHE   A  1 48  ? 36.295 -83.595  -18.760 1.00 24.51  ? 40   PHE   A O      1 
ATOM   190  C CB     . PHE   A  1 48  ? 34.469 -82.259  -16.181 1.00 26.00  ? 40   PHE   A CB     1 
ATOM   191  C CG     . PHE   A  1 48  ? 33.808 -81.447  -17.269 1.00 26.67  ? 40   PHE   A CG     1 
ATOM   192  C CD1    . PHE   A  1 48  ? 34.080 -80.093  -17.411 1.00 29.23  ? 40   PHE   A CD1    1 
ATOM   193  C CD2    . PHE   A  1 48  ? 32.854 -82.022  -18.105 1.00 27.54  ? 40   PHE   A CD2    1 
ATOM   194  C CE1    . PHE   A  1 48  ? 33.444 -79.335  -18.403 1.00 30.20  ? 40   PHE   A CE1    1 
ATOM   195  C CE2    . PHE   A  1 48  ? 32.214 -81.265  -19.089 1.00 29.71  ? 40   PHE   A CE2    1 
ATOM   196  C CZ     . PHE   A  1 48  ? 32.516 -79.929  -19.235 1.00 28.49  ? 40   PHE   A CZ     1 
ATOM   197  N N      . LEU   A  1 49  ? 35.090 -84.944  -17.417 1.00 23.24  ? 41   LEU   A N      1 
ATOM   198  C CA     . LEU   A  1 49  ? 34.898 -86.022  -18.359 1.00 23.71  ? 41   LEU   A CA     1 
ATOM   199  C C      . LEU   A  1 49  ? 33.417 -86.383  -18.458 1.00 29.87  ? 41   LEU   A C      1 
ATOM   200  O O      . LEU   A  1 49  ? 32.782 -86.655  -17.438 1.00 30.02  ? 41   LEU   A O      1 
ATOM   201  C CB     . LEU   A  1 49  ? 35.728 -87.245  -17.886 1.00 23.44  ? 41   LEU   A CB     1 
ATOM   202  C CG     . LEU   A  1 49  ? 35.529 -88.594  -18.597 1.00 27.78  ? 41   LEU   A CG     1 
ATOM   203  C CD1    . LEU   A  1 49  ? 35.974 -88.541  -20.061 1.00 27.24  ? 41   LEU   A CD1    1 
ATOM   204  C CD2    . LEU   A  1 49  ? 36.232 -89.715  -17.842 1.00 29.90  ? 41   LEU   A CD2    1 
ATOM   205  N N      . CYS   A  1 50  ? 32.882 -86.394  -19.690 1.00 26.79  ? 42   CYS   A N      1 
ATOM   206  C CA     . CYS   A  1 50  ? 31.525 -86.838  -19.973 1.00 27.36  ? 42   CYS   A CA     1 
ATOM   207  C C      . CYS   A  1 50  ? 31.663 -88.304  -20.343 1.00 30.95  ? 42   CYS   A C      1 
ATOM   208  O O      . CYS   A  1 50  ? 32.368 -88.641  -21.290 1.00 30.65  ? 42   CYS   A O      1 
ATOM   209  C CB     . CYS   A  1 50  ? 30.889 -86.031  -21.100 1.00 28.12  ? 42   CYS   A CB     1 
ATOM   210  S SG     . CYS   A  1 50  ? 30.964 -84.245  -20.850 1.00 32.71  ? 42   CYS   A SG     1 
ATOM   211  N N      . MET   A  1 51  ? 31.030 -89.177  -19.575 1.00 27.89  ? 43   MET   A N      1 
ATOM   212  C CA     . MET   A  1 51  ? 31.153 -90.609  -19.801 1.00 27.89  ? 43   MET   A CA     1 
ATOM   213  C C      . MET   A  1 51  ? 29.883 -91.384  -19.475 1.00 29.82  ? 43   MET   A C      1 
ATOM   214  O O      . MET   A  1 51  ? 29.066 -90.914  -18.681 1.00 27.34  ? 43   MET   A O      1 
ATOM   215  C CB     . MET   A  1 51  ? 32.349 -91.177  -19.004 1.00 30.54  ? 43   MET   A CB     1 
ATOM   216  C CG     . MET   A  1 51  ? 32.378 -90.761  -17.555 1.00 34.91  ? 43   MET   A CG     1 
ATOM   217  S SD     . MET   A  1 51  ? 33.222 -91.967  -16.512 1.00 40.05  ? 43   MET   A SD     1 
ATOM   218  C CE     . MET   A  1 51  ? 31.813 -92.506  -15.479 1.00 36.96  ? 43   MET   A CE     1 
ATOM   219  N N      . PRO   A  1 52  ? 29.718 -92.599  -20.042 1.00 27.02  ? 44   PRO   A N      1 
ATOM   220  C CA     . PRO   A  1 52  ? 28.549 -93.413  -19.682 1.00 27.25  ? 44   PRO   A CA     1 
ATOM   221  C C      . PRO   A  1 52  ? 28.676 -93.919  -18.234 1.00 31.32  ? 44   PRO   A C      1 
ATOM   222  O O      . PRO   A  1 52  ? 29.790 -94.152  -17.766 1.00 30.36  ? 44   PRO   A O      1 
ATOM   223  C CB     . PRO   A  1 52  ? 28.608 -94.578  -20.683 1.00 28.82  ? 44   PRO   A CB     1 
ATOM   224  C CG     . PRO   A  1 52  ? 29.646 -94.208  -21.696 1.00 32.73  ? 44   PRO   A CG     1 
ATOM   225  C CD     . PRO   A  1 52  ? 30.592 -93.315  -20.997 1.00 28.49  ? 44   PRO   A CD     1 
ATOM   226  N N      . VAL   A  1 53  ? 27.546 -94.047  -17.522 1.00 28.00  ? 45   VAL   A N      1 
ATOM   227  C CA     . VAL   A  1 53  ? 27.524 -94.531  -16.134 1.00 28.25  ? 45   VAL   A CA     1 
ATOM   228  C C      . VAL   A  1 53  ? 27.288 -96.039  -16.096 1.00 30.45  ? 45   VAL   A C      1 
ATOM   229  O O      . VAL   A  1 53  ? 27.618 -96.690  -15.111 1.00 30.76  ? 45   VAL   A O      1 
ATOM   230  C CB     . VAL   A  1 53  ? 26.571 -93.739  -15.187 1.00 33.09  ? 45   VAL   A CB     1 
ATOM   231  C CG1    . VAL   A  1 53  ? 27.118 -92.337  -14.933 1.00 33.79  ? 45   VAL   A CG1    1 
ATOM   232  C CG2    . VAL   A  1 53  ? 25.142 -93.678  -15.729 1.00 32.56  ? 45   VAL   A CG2    1 
ATOM   233  N N      . PHE   A  1 54  ? 26.711 -96.575  -17.178 1.00 25.84  ? 46   PHE   A N      1 
ATOM   234  C CA     . PHE   A  1 54  ? 26.478 -97.991  -17.437 1.00 24.86  ? 46   PHE   A CA     1 
ATOM   235  C C      . PHE   A  1 54  ? 27.164 -98.224  -18.772 1.00 27.52  ? 46   PHE   A C      1 
ATOM   236  O O      . PHE   A  1 54  ? 27.354 -97.254  -19.501 1.00 28.13  ? 46   PHE   A O      1 
ATOM   237  C CB     . PHE   A  1 54  ? 24.971 -98.278  -17.571 1.00 26.34  ? 46   PHE   A CB     1 
ATOM   238  C CG     . PHE   A  1 54  ? 24.231 -98.322  -16.258 1.00 27.53  ? 46   PHE   A CG     1 
ATOM   239  C CD1    . PHE   A  1 54  ? 23.957 -97.154  -15.553 1.00 30.15  ? 46   PHE   A CD1    1 
ATOM   240  C CD2    . PHE   A  1 54  ? 23.790 -99.527  -15.732 1.00 29.25  ? 46   PHE   A CD2    1 
ATOM   241  C CE1    . PHE   A  1 54  ? 23.299 -97.199  -14.324 1.00 30.38  ? 46   PHE   A CE1    1 
ATOM   242  C CE2    . PHE   A  1 54  ? 23.102 -99.566  -14.520 1.00 31.90  ? 46   PHE   A CE2    1 
ATOM   243  C CZ     . PHE   A  1 54  ? 22.870 -98.402  -13.819 1.00 29.54  ? 46   PHE   A CZ     1 
ATOM   244  N N      . HIS   A  1 55  ? 27.547 -99.470  -19.109 1.00 22.95  ? 47   HIS   A N      1 
ATOM   245  C CA     . HIS   A  1 55  ? 28.185 -99.699  -20.408 1.00 22.47  ? 47   HIS   A CA     1 
ATOM   246  C C      . HIS   A  1 55  ? 27.194 -99.326  -21.534 1.00 23.39  ? 47   HIS   A C      1 
ATOM   247  O O      . HIS   A  1 55  ? 26.053 -99.797  -21.524 1.00 21.51  ? 47   HIS   A O      1 
ATOM   248  C CB     . HIS   A  1 55  ? 28.720 -101.138 -20.567 1.00 23.35  ? 47   HIS   A CB     1 
ATOM   249  C CG     . HIS   A  1 55  ? 29.611 -101.304 -21.761 1.00 26.83  ? 47   HIS   A CG     1 
ATOM   250  N ND1    . HIS   A  1 55  ? 29.108 -101.259 -23.050 1.00 28.84  ? 47   HIS   A ND1    1 
ATOM   251  C CD2    . HIS   A  1 55  ? 30.948 -101.497 -21.822 1.00 28.63  ? 47   HIS   A CD2    1 
ATOM   252  C CE1    . HIS   A  1 55  ? 30.152 -101.400 -23.850 1.00 28.08  ? 47   HIS   A CE1    1 
ATOM   253  N NE2    . HIS   A  1 55  ? 31.278 -101.569 -23.156 1.00 28.37  ? 47   HIS   A NE2    1 
ATOM   254  N N      . PRO   A  1 56  ? 27.608 -98.458  -22.481 1.00 21.21  ? 48   PRO   A N      1 
ATOM   255  C CA     . PRO   A  1 56  ? 26.668 -97.999  -23.529 1.00 21.46  ? 48   PRO   A CA     1 
ATOM   256  C C      . PRO   A  1 56  ? 25.979 -99.093  -24.355 1.00 25.91  ? 48   PRO   A C      1 
ATOM   257  O O      . PRO   A  1 56  ? 24.853 -98.878  -24.799 1.00 24.76  ? 48   PRO   A O      1 
ATOM   258  C CB     . PRO   A  1 56  ? 27.505 -97.064  -24.411 1.00 23.50  ? 48   PRO   A CB     1 
ATOM   259  C CG     . PRO   A  1 56  ? 28.887 -97.145  -23.924 1.00 27.64  ? 48   PRO   A CG     1 
ATOM   260  C CD     . PRO   A  1 56  ? 28.917 -97.776  -22.580 1.00 22.96  ? 48   PRO   A CD     1 
ATOM   261  N N      . ARG   A  1 57  ? 26.620 -100.266 -24.526 1.00 23.85  ? 49   ARG   A N      1 
ATOM   262  C CA     . ARG   A  1 57  ? 26.044 -101.391 -25.277 1.00 24.23  ? 49   ARG   A CA     1 
ATOM   263  C C      . ARG   A  1 57  ? 25.316 -102.393 -24.376 1.00 28.42  ? 49   ARG   A C      1 
ATOM   264  O O      . ARG   A  1 57  ? 24.718 -103.338 -24.885 1.00 28.65  ? 49   ARG   A O      1 
ATOM   265  C CB     . ARG   A  1 57  ? 27.136 -102.128 -26.078 1.00 23.31  ? 49   ARG   A CB     1 
ATOM   266  C CG     . ARG   A  1 57  ? 27.584 -101.413 -27.347 1.00 29.44  ? 49   ARG   A CG     1 
ATOM   267  C CD     . ARG   A  1 57  ? 28.425 -102.328 -28.225 1.00 34.39  ? 49   ARG   A CD     1 
ATOM   268  N NE     . ARG   A  1 57  ? 29.729 -102.617 -27.623 1.00 31.15  ? 49   ARG   A NE     1 
ATOM   269  C CZ     . ARG   A  1 57  ? 30.112 -103.806 -27.167 1.00 40.66  ? 49   ARG   A CZ     1 
ATOM   270  N NH1    . ARG   A  1 57  ? 29.301 -104.853 -27.258 1.00 25.60  ? 49   ARG   A NH1    1 
ATOM   271  N NH2    . ARG   A  1 57  ? 31.310 -103.958 -26.619 1.00 28.04  ? 49   ARG   A NH2    1 
ATOM   272  N N      . PHE   A  1 58  ? 25.375 -102.205 -23.049 1.00 25.55  ? 50   PHE   A N      1 
ATOM   273  C CA     . PHE   A  1 58  ? 24.777 -103.145 -22.097 1.00 26.19  ? 50   PHE   A CA     1 
ATOM   274  C C      . PHE   A  1 58  ? 23.265 -102.957 -21.916 1.00 28.96  ? 50   PHE   A C      1 
ATOM   275  O O      . PHE   A  1 58  ? 22.812 -102.540 -20.848 1.00 28.99  ? 50   PHE   A O      1 
ATOM   276  C CB     . PHE   A  1 58  ? 25.539 -103.098 -20.754 1.00 28.64  ? 50   PHE   A CB     1 
ATOM   277  C CG     . PHE   A  1 58  ? 25.238 -104.175 -19.738 1.00 30.90  ? 50   PHE   A CG     1 
ATOM   278  C CD1    . PHE   A  1 58  ? 25.384 -105.524 -20.060 1.00 34.78  ? 50   PHE   A CD1    1 
ATOM   279  C CD2    . PHE   A  1 58  ? 24.890 -103.841 -18.432 1.00 33.97  ? 50   PHE   A CD2    1 
ATOM   280  C CE1    . PHE   A  1 58  ? 25.172 -106.518 -19.099 1.00 35.69  ? 50   PHE   A CE1    1 
ATOM   281  C CE2    . PHE   A  1 58  ? 24.656 -104.838 -17.475 1.00 36.67  ? 50   PHE   A CE2    1 
ATOM   282  C CZ     . PHE   A  1 58  ? 24.811 -106.166 -17.813 1.00 34.92  ? 50   PHE   A CZ     1 
ATOM   283  N N      . LYS   A  1 59  ? 22.485 -103.289 -22.969 1.00 25.80  ? 51   LYS   A N      1 
ATOM   284  C CA     . LYS   A  1 59  ? 21.015 -103.242 -22.980 1.00 25.14  ? 51   LYS   A CA     1 
ATOM   285  C C      . LYS   A  1 59  ? 20.486 -104.133 -21.867 1.00 29.05  ? 51   LYS   A C      1 
ATOM   286  O O      . LYS   A  1 59  ? 20.984 -105.252 -21.689 1.00 27.91  ? 51   LYS   A O      1 
ATOM   287  C CB     . LYS   A  1 59  ? 20.444 -103.715 -24.331 1.00 26.84  ? 51   LYS   A CB     1 
ATOM   288  C CG     . LYS   A  1 59  ? 20.659 -102.727 -25.475 1.00 43.62  ? 51   LYS   A CG     1 
ATOM   289  C CD     . LYS   A  1 59  ? 20.118 -103.233 -26.815 1.00 53.65  ? 51   LYS   A CD     1 
ATOM   290  C CE     . LYS   A  1 59  ? 18.664 -102.882 -27.053 1.00 59.81  ? 51   LYS   A CE     1 
ATOM   291  N NZ     . LYS   A  1 59  ? 18.277 -103.075 -28.478 1.00 65.65  ? 51   LYS   A NZ     1 
ATOM   292  N N      . ARG   A  1 60  ? 19.498 -103.624 -21.109 1.00 25.57  ? 52   ARG   A N      1 
ATOM   293  C CA     . ARG   A  1 60  ? 18.899 -104.296 -19.949 1.00 25.23  ? 52   ARG   A CA     1 
ATOM   294  C C      . ARG   A  1 60  ? 17.395 -104.511 -20.104 1.00 29.70  ? 52   ARG   A C      1 
ATOM   295  O O      . ARG   A  1 60  ? 16.696 -103.659 -20.652 1.00 28.69  ? 52   ARG   A O      1 
ATOM   296  C CB     . ARG   A  1 60  ? 19.226 -103.525 -18.653 1.00 24.13  ? 52   ARG   A CB     1 
ATOM   297  C CG     . ARG   A  1 60  ? 20.725 -103.567 -18.330 1.00 29.45  ? 52   ARG   A CG     1 
ATOM   298  C CD     . ARG   A  1 60  ? 21.188 -102.683 -17.187 1.00 31.53  ? 52   ARG   A CD     1 
ATOM   299  N NE     . ARG   A  1 60  ? 20.725 -101.296 -17.285 1.00 29.41  ? 52   ARG   A NE     1 
ATOM   300  C CZ     . ARG   A  1 60  ? 21.326 -100.330 -17.972 1.00 35.65  ? 52   ARG   A CZ     1 
ATOM   301  N NH1    . ARG   A  1 60  ? 22.419 -100.588 -18.682 1.00 22.83  ? 52   ARG   A NH1    1 
ATOM   302  N NH2    . ARG   A  1 60  ? 20.836 -99.097  -17.959 1.00 23.40  ? 52   ARG   A NH2    1 
ATOM   303  N N      . GLU   A  1 61  ? 16.912 -105.670 -19.650 1.00 27.14  ? 53   GLU   A N      1 
ATOM   304  C CA     . GLU   A  1 61  ? 15.499 -106.055 -19.708 1.00 27.30  ? 53   GLU   A CA     1 
ATOM   305  C C      . GLU   A  1 61  ? 14.875 -105.882 -18.323 1.00 32.28  ? 53   GLU   A C      1 
ATOM   306  O O      . GLU   A  1 61  ? 15.482 -106.253 -17.313 1.00 32.42  ? 53   GLU   A O      1 
ATOM   307  C CB     . GLU   A  1 61  ? 15.351 -107.499 -20.218 1.00 28.39  ? 53   GLU   A CB     1 
ATOM   308  C CG     . GLU   A  1 61  ? 13.921 -107.998 -20.390 1.00 34.85  ? 53   GLU   A CG     1 
ATOM   309  C CD     . GLU   A  1 61  ? 12.997 -107.162 -21.258 1.00 54.05  ? 53   GLU   A CD     1 
ATOM   310  O OE1    . GLU   A  1 61  ? 13.441 -106.700 -22.335 1.00 55.24  ? 53   GLU   A OE1    1 
ATOM   311  O OE2    . GLU   A  1 61  ? 11.817 -106.993 -20.874 1.00 42.31  ? 53   GLU   A OE2    1 
ATOM   312  N N      . PHE   A  1 62  ? 13.664 -105.326 -18.275 1.00 29.23  ? 54   PHE   A N      1 
ATOM   313  C CA     . PHE   A  1 62  ? 13.017 -105.053 -16.994 1.00 29.46  ? 54   PHE   A CA     1 
ATOM   314  C C      . PHE   A  1 62  ? 11.762 -105.846 -16.751 1.00 37.08  ? 54   PHE   A C      1 
ATOM   315  O O      . PHE   A  1 62  ? 11.391 -106.018 -15.590 1.00 37.15  ? 54   PHE   A O      1 
ATOM   316  C CB     . PHE   A  1 62  ? 12.749 -103.539 -16.845 1.00 30.25  ? 54   PHE   A CB     1 
ATOM   317  C CG     . PHE   A  1 62  ? 14.017 -102.728 -16.716 1.00 30.78  ? 54   PHE   A CG     1 
ATOM   318  C CD1    . PHE   A  1 62  ? 14.717 -102.316 -17.844 1.00 32.75  ? 54   PHE   A CD1    1 
ATOM   319  C CD2    . PHE   A  1 62  ? 14.521 -102.391 -15.465 1.00 32.44  ? 54   PHE   A CD2    1 
ATOM   320  C CE1    . PHE   A  1 62  ? 15.905 -101.595 -17.723 1.00 33.46  ? 54   PHE   A CE1    1 
ATOM   321  C CE2    . PHE   A  1 62  ? 15.701 -101.651 -15.345 1.00 34.60  ? 54   PHE   A CE2    1 
ATOM   322  C CZ     . PHE   A  1 62  ? 16.384 -101.260 -16.473 1.00 32.45  ? 54   PHE   A CZ     1 
ATOM   323  N N      . ILE   A  1 63  ? 11.116 -106.347 -17.818 1.00 36.65  ? 55   ILE   A N      1 
ATOM   324  C CA     . ILE   A  1 63  ? 9.844  -107.047 -17.682 1.00 37.80  ? 55   ILE   A CA     1 
ATOM   325  C C      . ILE   A  1 63  ? 9.899  -108.557 -18.026 1.00 42.62  ? 55   ILE   A C      1 
ATOM   326  O O      . ILE   A  1 63  ? 9.437  -109.349 -17.198 1.00 42.03  ? 55   ILE   A O      1 
ATOM   327  C CB     . ILE   A  1 63  ? 8.740  -106.272 -18.483 1.00 41.50  ? 55   ILE   A CB     1 
ATOM   328  C CG1    . ILE   A  1 63  ? 8.317  -104.965 -17.740 1.00 42.51  ? 55   ILE   A CG1    1 
ATOM   329  C CG2    . ILE   A  1 63  ? 7.508  -107.114 -18.859 1.00 42.26  ? 55   ILE   A CG2    1 
ATOM   330  C CD1    . ILE   A  1 63  ? 7.891  -105.078 -16.200 1.00 48.29  ? 55   ILE   A CD1    1 
ATOM   331  N N      . GLN   A  1 64  ? 10.418 -108.972 -19.204 1.00 39.34  ? 56   GLN   A N      1 
ATOM   332  C CA     . GLN   A  1 64  ? 10.321 -110.405 -19.498 1.00 39.27  ? 56   GLN   A CA     1 
ATOM   333  C C      . GLN   A  1 64  ? 11.551 -111.241 -19.115 1.00 41.84  ? 56   GLN   A C      1 
ATOM   334  O O      . GLN   A  1 64  ? 12.699 -110.828 -19.268 1.00 40.56  ? 56   GLN   A O      1 
ATOM   335  C CB     . GLN   A  1 64  ? 9.883  -110.702 -20.949 1.00 40.88  ? 56   GLN   A CB     1 
ATOM   336  C CG     . GLN   A  1 64  ? 10.730 -110.128 -22.071 1.00 66.09  ? 56   GLN   A CG     1 
ATOM   337  C CD     . GLN   A  1 64  ? 10.081 -110.427 -23.404 1.00 93.21  ? 56   GLN   A CD     1 
ATOM   338  O OE1    . GLN   A  1 64  ? 9.163  -109.727 -23.851 1.00 91.28  ? 56   GLN   A OE1    1 
ATOM   339  N NE2    . GLN   A  1 64  ? 10.524 -111.489 -24.062 1.00 84.97  ? 56   GLN   A NE2    1 
ATOM   340  N N      . GLU   A  1 65  ? 11.256 -112.441 -18.591 1.00 38.50  ? 57   GLU   A N      1 
ATOM   341  C CA     . GLU   A  1 65  ? 12.217 -113.467 -18.191 1.00 38.11  ? 57   GLU   A CA     1 
ATOM   342  C C      . GLU   A  1 65  ? 12.657 -114.185 -19.477 1.00 41.10  ? 57   GLU   A C      1 
ATOM   343  O O      . GLU   A  1 65  ? 11.872 -114.234 -20.427 1.00 40.73  ? 57   GLU   A O      1 
ATOM   344  C CB     . GLU   A  1 65  ? 11.557 -114.468 -17.226 1.00 39.47  ? 57   GLU   A CB     1 
ATOM   345  C CG     . GLU   A  1 65  ? 11.298 -113.904 -15.837 1.00 52.15  ? 57   GLU   A CG     1 
ATOM   346  C CD     . GLU   A  1 65  ? 10.496 -114.794 -14.905 1.00 81.90  ? 57   GLU   A CD     1 
ATOM   347  O OE1    . GLU   A  1 65  ? 9.410  -115.265 -15.316 1.00 83.34  ? 57   GLU   A OE1    1 
ATOM   348  O OE2    . GLU   A  1 65  ? 10.933 -114.982 -13.746 1.00 77.22  ? 57   GLU   A OE2    1 
ATOM   349  N N      . PRO   A  1 66  ? 13.904 -114.691 -19.583 1.00 36.40  ? 58   PRO   A N      1 
ATOM   350  C CA     . PRO   A  1 66  ? 14.944 -114.780 -18.546 1.00 35.60  ? 58   PRO   A CA     1 
ATOM   351  C C      . PRO   A  1 66  ? 15.888 -113.588 -18.419 1.00 37.36  ? 58   PRO   A C      1 
ATOM   352  O O      . PRO   A  1 66  ? 16.522 -113.453 -17.367 1.00 36.13  ? 58   PRO   A O      1 
ATOM   353  C CB     . PRO   A  1 66  ? 15.689 -116.057 -18.942 1.00 37.56  ? 58   PRO   A CB     1 
ATOM   354  C CG     . PRO   A  1 66  ? 15.621 -116.057 -20.452 1.00 42.05  ? 58   PRO   A CG     1 
ATOM   355  C CD     . PRO   A  1 66  ? 14.311 -115.398 -20.815 1.00 37.71  ? 58   PRO   A CD     1 
ATOM   356  N N      . ALA   A  1 67  ? 16.000 -112.736 -19.466 1.00 32.82  ? 59   ALA   A N      1 
ATOM   357  C CA     . ALA   A  1 67  ? 16.916 -111.579 -19.480 1.00 31.92  ? 59   ALA   A CA     1 
ATOM   358  C C      . ALA   A  1 67  ? 16.726 -110.590 -18.311 1.00 33.61  ? 59   ALA   A C      1 
ATOM   359  O O      . ALA   A  1 67  ? 17.703 -109.964 -17.894 1.00 32.77  ? 59   ALA   A O      1 
ATOM   360  C CB     . ALA   A  1 67  ? 16.848 -110.852 -20.812 1.00 32.30  ? 59   ALA   A CB     1 
ATOM   361  N N      . LYS   A  1 68  ? 15.493 -110.481 -17.772 1.00 29.06  ? 60   LYS   A N      1 
ATOM   362  C CA     . LYS   A  1 68  ? 15.146 -109.632 -16.620 1.00 29.42  ? 60   LYS   A CA     1 
ATOM   363  C C      . LYS   A  1 68  ? 15.957 -110.074 -15.376 1.00 33.52  ? 60   LYS   A C      1 
ATOM   364  O O      . LYS   A  1 68  ? 16.383 -109.229 -14.587 1.00 32.72  ? 60   LYS   A O      1 
ATOM   365  C CB     . LYS   A  1 68  ? 13.626 -109.747 -16.340 1.00 32.08  ? 60   LYS   A CB     1 
ATOM   366  C CG     . LYS   A  1 68  ? 13.102 -108.965 -15.140 1.00 49.53  ? 60   LYS   A CG     1 
ATOM   367  C CD     . LYS   A  1 68  ? 11.774 -109.547 -14.645 1.00 60.37  ? 60   LYS   A CD     1 
ATOM   368  C CE     . LYS   A  1 68  ? 11.248 -108.864 -13.403 1.00 71.96  ? 60   LYS   A CE     1 
ATOM   369  N NZ     . LYS   A  1 68  ? 12.050 -109.200 -12.197 1.00 83.03  ? 60   LYS   A NZ     1 
ATOM   370  N N      . ASN   A  1 69  ? 16.190 -111.396 -15.229 1.00 30.35  ? 61   ASN   A N      1 
ATOM   371  C CA     . ASN   A  1 69  ? 16.915 -111.955 -14.085 1.00 31.06  ? 61   ASN   A CA     1 
ATOM   372  C C      . ASN   A  1 69  ? 18.427 -112.081 -14.311 1.00 35.44  ? 61   ASN   A C      1 
ATOM   373  O O      . ASN   A  1 69  ? 19.083 -112.886 -13.646 1.00 36.04  ? 61   ASN   A O      1 
ATOM   374  C CB     . ASN   A  1 69  ? 16.285 -113.276 -13.644 1.00 32.24  ? 61   ASN   A CB     1 
ATOM   375  C CG     . ASN   A  1 69  ? 14.879 -113.090 -13.122 1.00 50.84  ? 61   ASN   A CG     1 
ATOM   376  O OD1    . ASN   A  1 69  ? 14.592 -112.171 -12.344 1.00 42.98  ? 61   ASN   A OD1    1 
ATOM   377  N ND2    . ASN   A  1 69  ? 13.962 -113.926 -13.573 1.00 42.42  ? 61   ASN   A ND2    1 
ATOM   378  N N      . ARG   A  1 70  ? 18.991 -111.220 -15.185 1.00 31.11  ? 62   ARG   A N      1 
ATOM   379  C CA     . ARG   A  1 70  ? 20.423 -111.192 -15.462 1.00 30.98  ? 62   ARG   A CA     1 
ATOM   380  C C      . ARG   A  1 70  ? 21.199 -110.921 -14.163 1.00 37.00  ? 62   ARG   A C      1 
ATOM   381  O O      . ARG   A  1 70  ? 20.958 -109.896 -13.516 1.00 36.01  ? 62   ARG   A O      1 
ATOM   382  C CB     . ARG   A  1 70  ? 20.765 -110.142 -16.535 1.00 29.49  ? 62   ARG   A CB     1 
ATOM   383  C CG     . ARG   A  1 70  ? 22.256 -110.034 -16.846 1.00 27.41  ? 62   ARG   A CG     1 
ATOM   384  C CD     . ARG   A  1 70  ? 22.555 -108.909 -17.818 1.00 29.36  ? 62   ARG   A CD     1 
ATOM   385  N NE     . ARG   A  1 70  ? 21.815 -109.062 -19.071 1.00 26.68  ? 62   ARG   A NE     1 
ATOM   386  C CZ     . ARG   A  1 70  ? 21.475 -108.060 -19.869 1.00 39.24  ? 62   ARG   A CZ     1 
ATOM   387  N NH1    . ARG   A  1 70  ? 21.795 -106.808 -19.551 1.00 26.45  ? 62   ARG   A NH1    1 
ATOM   388  N NH2    . ARG   A  1 70  ? 20.785 -108.294 -20.976 1.00 27.91  ? 62   ARG   A NH2    1 
ATOM   389  N N      . PRO   A  1 71  ? 22.119 -111.833 -13.757 1.00 34.79  ? 63   PRO   A N      1 
ATOM   390  C CA     . PRO   A  1 71  ? 22.872 -111.598 -12.517 1.00 34.30  ? 63   PRO   A CA     1 
ATOM   391  C C      . PRO   A  1 71  ? 23.742 -110.358 -12.621 1.00 37.13  ? 63   PRO   A C      1 
ATOM   392  O O      . PRO   A  1 71  ? 24.227 -110.019 -13.711 1.00 36.07  ? 63   PRO   A O      1 
ATOM   393  C CB     . PRO   A  1 71  ? 23.692 -112.879 -12.339 1.00 36.31  ? 63   PRO   A CB     1 
ATOM   394  C CG     . PRO   A  1 71  ? 23.788 -113.468 -13.698 1.00 41.35  ? 63   PRO   A CG     1 
ATOM   395  C CD     . PRO   A  1 71  ? 22.513 -113.106 -14.399 1.00 36.83  ? 63   PRO   A CD     1 
ATOM   396  N N      . GLY   A  1 72  ? 23.872 -109.666 -11.495 1.00 32.58  ? 64   GLY   A N      1 
ATOM   397  C CA     . GLY   A  1 72  ? 24.652 -108.441 -11.383 1.00 31.92  ? 64   GLY   A CA     1 
ATOM   398  C C      . GLY   A  1 72  ? 26.146 -108.676 -11.282 1.00 35.98  ? 64   GLY   A C      1 
ATOM   399  O O      . GLY   A  1 72  ? 26.590 -109.826 -11.347 1.00 36.61  ? 64   GLY   A O      1 
ATOM   400  N N      . PRO   A  1 73  ? 26.971 -107.617 -11.126 1.00 32.24  ? 65   PRO   A N      1 
ATOM   401  C CA     . PRO   A  1 73  ? 26.599 -106.185 -11.017 1.00 31.93  ? 65   PRO   A CA     1 
ATOM   402  C C      . PRO   A  1 73  ? 26.062 -105.587 -12.321 1.00 35.81  ? 65   PRO   A C      1 
ATOM   403  O O      . PRO   A  1 73  ? 26.370 -106.095 -13.398 1.00 36.10  ? 65   PRO   A O      1 
ATOM   404  C CB     . PRO   A  1 73  ? 27.894 -105.526 -10.534 1.00 33.49  ? 65   PRO   A CB     1 
ATOM   405  C CG     . PRO   A  1 73  ? 28.992 -106.415 -11.066 1.00 37.78  ? 65   PRO   A CG     1 
ATOM   406  C CD     . PRO   A  1 73  ? 28.433 -107.812 -11.017 1.00 33.20  ? 65   PRO   A CD     1 
ATOM   407  N N      . GLN   A  1 74  ? 25.222 -104.547 -12.225 1.00 31.07  ? 66   GLN   A N      1 
ATOM   408  C CA     . GLN   A  1 74  ? 24.634 -103.905 -13.410 1.00 29.75  ? 66   GLN   A CA     1 
ATOM   409  C C      . GLN   A  1 74  ? 25.563 -102.865 -14.030 1.00 30.57  ? 66   GLN   A C      1 
ATOM   410  O O      . GLN   A  1 74  ? 25.419 -102.534 -15.204 1.00 29.45  ? 66   GLN   A O      1 
ATOM   411  C CB     . GLN   A  1 74  ? 23.245 -103.317 -13.101 1.00 30.92  ? 66   GLN   A CB     1 
ATOM   412  C CG     . GLN   A  1 74  ? 22.191 -104.350 -12.688 1.00 40.30  ? 66   GLN   A CG     1 
ATOM   413  C CD     . GLN   A  1 74  ? 21.984 -105.482 -13.676 1.00 57.77  ? 66   GLN   A CD     1 
ATOM   414  O OE1    . GLN   A  1 74  ? 21.897 -105.288 -14.897 1.00 50.29  ? 66   GLN   A OE1    1 
ATOM   415  N NE2    . GLN   A  1 74  ? 21.862 -106.697 -13.155 1.00 50.80  ? 66   GLN   A NE2    1 
ATOM   416  N N      . THR   A  1 75  ? 26.524 -102.359 -13.238 1.00 26.33  ? 67   THR   A N      1 
ATOM   417  C CA     . THR   A  1 75  ? 27.548 -101.399 -13.666 1.00 26.00  ? 67   THR   A CA     1 
ATOM   418  C C      . THR   A  1 75  ? 28.751 -101.453 -12.714 1.00 31.41  ? 67   THR   A C      1 
ATOM   419  O O      . THR   A  1 75  ? 28.792 -102.312 -11.837 1.00 31.33  ? 67   THR   A O      1 
ATOM   420  C CB     . THR   A  1 75  ? 26.974 -99.983  -13.887 1.00 30.95  ? 67   THR   A CB     1 
ATOM   421  O OG1    . THR   A  1 75  ? 28.016 -99.163  -14.406 1.00 31.20  ? 67   THR   A OG1    1 
ATOM   422  C CG2    . THR   A  1 75  ? 26.380 -99.355  -12.614 1.00 27.73  ? 67   THR   A CG2    1 
ATOM   423  N N      . ARG   A  1 76  ? 29.742 -100.574 -12.907 1.00 29.42  ? 68   ARG   A N      1 
ATOM   424  C CA     . ARG   A  1 76  ? 30.884 -100.548 -12.020 1.00 29.76  ? 68   ARG   A CA     1 
ATOM   425  C C      . ARG   A  1 76  ? 30.591 -99.731  -10.758 1.00 33.71  ? 68   ARG   A C      1 
ATOM   426  O O      . ARG   A  1 76  ? 29.678 -98.902  -10.738 1.00 33.83  ? 68   ARG   A O      1 
ATOM   427  C CB     . ARG   A  1 76  ? 32.183 -100.143 -12.721 1.00 29.64  ? 68   ARG   A CB     1 
ATOM   428  C CG     . ARG   A  1 76  ? 32.238 -98.791  -13.354 1.00 35.17  ? 68   ARG   A CG     1 
ATOM   429  C CD     . ARG   A  1 76  ? 33.576 -98.705  -14.038 1.00 39.24  ? 68   ARG   A CD     1 
ATOM   430  N NE     . ARG   A  1 76  ? 33.529 -97.782  -15.154 1.00 47.33  ? 68   ARG   A NE     1 
ATOM   431  C CZ     . ARG   A  1 76  ? 34.119 -97.981  -16.323 1.00 53.98  ? 68   ARG   A CZ     1 
ATOM   432  N NH1    . ARG   A  1 76  ? 34.832 -99.082  -16.539 1.00 33.39  ? 68   ARG   A NH1    1 
ATOM   433  N NH2    . ARG   A  1 76  ? 34.007 -97.083  -17.284 1.00 43.50  ? 68   ARG   A NH2    1 
ATOM   434  N N      . SER   A  1 77  ? 31.348 -100.024 -9.693  1.00 28.84  ? 69   SER   A N      1 
ATOM   435  C CA     . SER   A  1 77  ? 31.178 -99.477  -8.356  1.00 27.64  ? 69   SER   A CA     1 
ATOM   436  C C      . SER   A  1 77  ? 31.514 -98.006  -8.185  1.00 29.64  ? 69   SER   A C      1 
ATOM   437  O O      . SER   A  1 77  ? 32.459 -97.483  -8.785  1.00 28.82  ? 69   SER   A O      1 
ATOM   438  C CB     . SER   A  1 77  ? 31.977 -100.308 -7.353  1.00 29.93  ? 69   SER   A CB     1 
ATOM   439  O OG     . SER   A  1 77  ? 31.696 -99.920  -6.020  1.00 39.65  ? 69   SER   A OG     1 
ATOM   440  N N      . ASP   A  1 78  ? 30.746 -97.361  -7.285  1.00 26.27  ? 70   ASP   A N      1 
ATOM   441  C CA     . ASP   A  1 78  ? 30.912 -95.985  -6.813  1.00 26.31  ? 70   ASP   A CA     1 
ATOM   442  C C      . ASP   A  1 78  ? 32.245 -95.848  -6.057  1.00 30.50  ? 70   ASP   A C      1 
ATOM   443  O O      . ASP   A  1 78  ? 32.785 -94.745  -5.968  1.00 30.22  ? 70   ASP   A O      1 
ATOM   444  C CB     . ASP   A  1 78  ? 29.748 -95.609  -5.865  1.00 27.71  ? 70   ASP   A CB     1 
ATOM   445  C CG     . ASP   A  1 78  ? 29.552 -96.498  -4.636  1.00 36.00  ? 70   ASP   A CG     1 
ATOM   446  O OD1    . ASP   A  1 78  ? 29.958 -97.680  -4.679  1.00 36.79  ? 70   ASP   A OD1    1 
ATOM   447  O OD2    . ASP   A  1 78  ? 28.939 -96.030  -3.662  1.00 37.55  ? 70   ASP   A OD2    1 
ATOM   448  N N      . LEU   A  1 79  ? 32.781 -96.974  -5.530  1.00 27.65  ? 71   LEU   A N      1 
ATOM   449  C CA     . LEU   A  1 79  ? 34.043 -97.000  -4.779  1.00 28.35  ? 71   LEU   A CA     1 
ATOM   450  C C      . LEU   A  1 79  ? 35.275 -96.726  -5.630  1.00 32.43  ? 71   LEU   A C      1 
ATOM   451  O O      . LEU   A  1 79  ? 36.339 -96.438  -5.081  1.00 31.86  ? 71   LEU   A O      1 
ATOM   452  C CB     . LEU   A  1 79  ? 34.218 -98.329  -4.026  1.00 28.39  ? 71   LEU   A CB     1 
ATOM   453  C CG     . LEU   A  1 79  ? 33.272 -98.586  -2.854  1.00 33.33  ? 71   LEU   A CG     1 
ATOM   454  C CD1    . LEU   A  1 79  ? 33.473 -99.970  -2.330  1.00 33.92  ? 71   LEU   A CD1    1 
ATOM   455  C CD2    . LEU   A  1 79  ? 33.494 -97.592  -1.719  1.00 33.87  ? 71   LEU   A CD2    1 
ATOM   456  N N      . LEU   A  1 80  ? 35.138 -96.810  -6.964  1.00 29.92  ? 72   LEU   A N      1 
ATOM   457  C CA     . LEU   A  1 80  ? 36.242 -96.593  -7.912  1.00 29.47  ? 72   LEU   A CA     1 
ATOM   458  C C      . LEU   A  1 80  ? 36.751 -95.158  -7.949  1.00 32.39  ? 72   LEU   A C      1 
ATOM   459  O O      . LEU   A  1 80  ? 37.878 -94.920  -8.389  1.00 31.87  ? 72   LEU   A O      1 
ATOM   460  C CB     . LEU   A  1 80  ? 35.873 -97.088  -9.317  1.00 29.42  ? 72   LEU   A CB     1 
ATOM   461  C CG     . LEU   A  1 80  ? 35.731 -98.603  -9.461  1.00 34.02  ? 72   LEU   A CG     1 
ATOM   462  C CD1    . LEU   A  1 80  ? 35.115 -98.952  -10.779 1.00 34.13  ? 72   LEU   A CD1    1 
ATOM   463  C CD2    . LEU   A  1 80  ? 37.075 -99.318  -9.320  1.00 36.53  ? 72   LEU   A CD2    1 
ATOM   464  N N      . LEU   A  1 81  ? 35.943 -94.210  -7.444  1.00 28.65  ? 73   LEU   A N      1 
ATOM   465  C CA     . LEU   A  1 81  ? 36.302 -92.798  -7.350  1.00 27.59  ? 73   LEU   A CA     1 
ATOM   466  C C      . LEU   A  1 81  ? 35.874 -92.236  -6.008  1.00 30.16  ? 73   LEU   A C      1 
ATOM   467  O O      . LEU   A  1 81  ? 34.904 -92.719  -5.412  1.00 29.44  ? 73   LEU   A O      1 
ATOM   468  C CB     . LEU   A  1 81  ? 35.639 -91.973  -8.479  1.00 27.63  ? 73   LEU   A CB     1 
ATOM   469  C CG     . LEU   A  1 81  ? 36.098 -92.169  -9.928  1.00 32.53  ? 73   LEU   A CG     1 
ATOM   470  C CD1    . LEU   A  1 81  ? 35.249 -91.302  -10.880 1.00 32.19  ? 73   LEU   A CD1    1 
ATOM   471  C CD2    . LEU   A  1 81  ? 37.582 -91.832  -10.102 1.00 34.95  ? 73   LEU   A CD2    1 
ATOM   472  N N      . SER   A  1 82  ? 36.563 -91.181  -5.554  1.00 27.07  ? 74   SER   A N      1 
ATOM   473  C CA     . SER   A  1 82  ? 36.219 -90.477  -4.321  1.00 27.25  ? 74   SER   A CA     1 
ATOM   474  C C      . SER   A  1 82  ? 34.948 -89.645  -4.562  1.00 33.57  ? 74   SER   A C      1 
ATOM   475  O O      . SER   A  1 82  ? 34.621 -89.347  -5.716  1.00 33.64  ? 74   SER   A O      1 
ATOM   476  C CB     . SER   A  1 82  ? 37.362 -89.566  -3.888  1.00 28.25  ? 74   SER   A CB     1 
ATOM   477  O OG     . SER   A  1 82  ? 37.494 -88.456  -4.759  1.00 35.54  ? 74   SER   A OG     1 
ATOM   478  N N      . GLY   A  1 83  ? 34.263 -89.273  -3.479  1.00 31.06  ? 75   GLY   A N      1 
ATOM   479  C CA     . GLY   A  1 83  ? 33.054 -88.458  -3.526  1.00 30.85  ? 75   GLY   A CA     1 
ATOM   480  C C      . GLY   A  1 83  ? 33.271 -87.154  -4.263  1.00 35.77  ? 75   GLY   A C      1 
ATOM   481  O O      . GLY   A  1 83  ? 32.449 -86.769  -5.096  1.00 35.76  ? 75   GLY   A O      1 
ATOM   482  N N      . ARG   A  1 84  ? 34.422 -86.501  -3.997  1.00 32.88  ? 76   ARG   A N      1 
ATOM   483  C CA     . ARG   A  1 84  ? 34.852 -85.245  -4.621  1.00 32.84  ? 76   ARG   A CA     1 
ATOM   484  C C      . ARG   A  1 84  ? 34.926 -85.383  -6.150  1.00 35.50  ? 76   ARG   A C      1 
ATOM   485  O O      . ARG   A  1 84  ? 34.447 -84.494  -6.855  1.00 35.88  ? 76   ARG   A O      1 
ATOM   486  C CB     . ARG   A  1 84  ? 36.195 -84.784  -4.014  1.00 34.23  ? 76   ARG   A CB     1 
ATOM   487  C CG     . ARG   A  1 84  ? 36.807 -83.531  -4.646  1.00 47.44  ? 76   ARG   A CG     1 
ATOM   488  C CD     . ARG   A  1 84  ? 36.857 -82.365  -3.683  1.00 62.05  ? 76   ARG   A CD     1 
ATOM   489  N NE     . ARG   A  1 84  ? 37.762 -81.316  -4.155  1.00 76.16  ? 76   ARG   A NE     1 
ATOM   490  C CZ     . ARG   A  1 84  ? 37.387 -80.256  -4.866  1.00 91.80  ? 76   ARG   A CZ     1 
ATOM   491  N NH1    . ARG   A  1 84  ? 36.112 -80.084  -5.195  1.00 78.71  ? 76   ARG   A NH1    1 
ATOM   492  N NH2    . ARG   A  1 84  ? 38.283 -79.356  -5.248  1.00 79.48  ? 76   ARG   A NH2    1 
ATOM   493  N N      . ASP   A  1 85  ? 35.503 -86.500  -6.650  1.00 30.55  ? 77   ASP   A N      1 
ATOM   494  C CA     . ASP   A  1 85  ? 35.647 -86.782  -8.078  1.00 29.66  ? 77   ASP   A CA     1 
ATOM   495  C C      . ASP   A  1 85  ? 34.293 -86.942  -8.778  1.00 30.98  ? 77   ASP   A C      1 
ATOM   496  O O      . ASP   A  1 85  ? 34.102 -86.366  -9.853  1.00 29.69  ? 77   ASP   A O      1 
ATOM   497  C CB     . ASP   A  1 85  ? 36.543 -88.012  -8.322  1.00 31.54  ? 77   ASP   A CB     1 
ATOM   498  C CG     . ASP   A  1 85  ? 38.009 -87.841  -7.960  1.00 43.23  ? 77   ASP   A CG     1 
ATOM   499  O OD1    . ASP   A  1 85  ? 38.441 -86.687  -7.746  1.00 45.01  ? 77   ASP   A OD1    1 
ATOM   500  O OD2    . ASP   A  1 85  ? 38.726 -88.864  -7.888  1.00 49.81  ? 77   ASP   A OD2    1 
ATOM   501  N N      . TRP   A  1 86  ? 33.357 -87.707  -8.169  1.00 25.34  ? 78   TRP   A N      1 
ATOM   502  C CA     . TRP   A  1 86  ? 32.014 -87.897  -8.730  1.00 24.31  ? 78   TRP   A CA     1 
ATOM   503  C C      . TRP   A  1 86  ? 31.255 -86.561  -8.791  1.00 27.63  ? 78   TRP   A C      1 
ATOM   504  O O      . TRP   A  1 86  ? 30.605 -86.277  -9.797  1.00 25.62  ? 78   TRP   A O      1 
ATOM   505  C CB     . TRP   A  1 86  ? 31.196 -88.897  -7.911  1.00 22.62  ? 78   TRP   A CB     1 
ATOM   506  C CG     . TRP   A  1 86  ? 31.664 -90.319  -7.960  1.00 23.82  ? 78   TRP   A CG     1 
ATOM   507  C CD1    . TRP   A  1 86  ? 32.071 -91.079  -6.903  1.00 26.56  ? 78   TRP   A CD1    1 
ATOM   508  C CD2    . TRP   A  1 86  ? 31.642 -91.195  -9.099  1.00 23.83  ? 78   TRP   A CD2    1 
ATOM   509  N NE1    . TRP   A  1 86  ? 32.328 -92.365  -7.314  1.00 25.58  ? 78   TRP   A NE1    1 
ATOM   510  C CE2    . TRP   A  1 86  ? 32.084 -92.463  -8.659  1.00 27.33  ? 78   TRP   A CE2    1 
ATOM   511  C CE3    . TRP   A  1 86  ? 31.311 -91.026  -10.458 1.00 24.98  ? 78   TRP   A CE3    1 
ATOM   512  C CZ2    . TRP   A  1 86  ? 32.227 -93.550  -9.531  1.00 26.51  ? 78   TRP   A CZ2    1 
ATOM   513  C CZ3    . TRP   A  1 86  ? 31.453 -92.104  -11.320 1.00 26.41  ? 78   TRP   A CZ3    1 
ATOM   514  C CH2    . TRP   A  1 86  ? 31.894 -93.350  -10.854 1.00 27.01  ? 78   TRP   A CH2    1 
ATOM   515  N N      . ASN   A  1 87  ? 31.370 -85.737  -7.723  1.00 24.20  ? 79   ASN   A N      1 
ATOM   516  C CA     . ASN   A  1 87  ? 30.701 -84.436  -7.627  1.00 24.28  ? 79   ASN   A CA     1 
ATOM   517  C C      . ASN   A  1 87  ? 31.246 -83.342  -8.542  1.00 28.15  ? 79   ASN   A C      1 
ATOM   518  O O      . ASN   A  1 87  ? 30.512 -82.400  -8.850  1.00 26.88  ? 79   ASN   A O      1 
ATOM   519  C CB     . ASN   A  1 87  ? 30.758 -83.913  -6.187  1.00 25.07  ? 79   ASN   A CB     1 
ATOM   520  C CG     . ASN   A  1 87  ? 30.030 -84.716  -5.143  1.00 32.36  ? 79   ASN   A CG     1 
ATOM   521  O OD1    . ASN   A  1 87  ? 30.279 -84.549  -3.962  1.00 27.17  ? 79   ASN   A OD1    1 
ATOM   522  N ND2    . ASN   A  1 87  ? 29.100 -85.566  -5.523  1.00 25.33  ? 79   ASN   A ND2    1 
ATOM   523  N N      . THR   A  1 88  ? 32.538 -83.404  -8.907  1.00 26.17  ? 80   THR   A N      1 
ATOM   524  C CA     . THR   A  1 88  ? 33.153 -82.327  -9.692  1.00 26.73  ? 80   THR   A CA     1 
ATOM   525  C C      . THR   A  1 88  ? 33.716 -82.706  -11.075 1.00 32.40  ? 80   THR   A C      1 
ATOM   526  O O      . THR   A  1 88  ? 33.779 -81.846  -11.954 1.00 34.05  ? 80   THR   A O      1 
ATOM   527  C CB     . THR   A  1 88  ? 34.273 -81.658  -8.869  1.00 35.65  ? 80   THR   A CB     1 
ATOM   528  O OG1    . THR   A  1 88  ? 35.292 -82.616  -8.581  1.00 36.11  ? 80   THR   A OG1    1 
ATOM   529  C CG2    . THR   A  1 88  ? 33.768 -81.016  -7.575  1.00 34.06  ? 80   THR   A CG2    1 
ATOM   530  N N      . LEU   A  1 89  ? 34.186 -83.938  -11.255 1.00 28.96  ? 81   LEU   A N      1 
ATOM   531  C CA     . LEU   A  1 89  ? 34.855 -84.299  -12.507 1.00 28.73  ? 81   LEU   A CA     1 
ATOM   532  C C      . LEU   A  1 89  ? 34.034 -85.142  -13.490 1.00 31.38  ? 81   LEU   A C      1 
ATOM   533  O O      . LEU   A  1 89  ? 34.469 -85.303  -14.626 1.00 32.67  ? 81   LEU   A O      1 
ATOM   534  C CB     . LEU   A  1 89  ? 36.197 -85.014  -12.211 1.00 28.63  ? 81   LEU   A CB     1 
ATOM   535  C CG     . LEU   A  1 89  ? 37.151 -84.409  -11.172 1.00 33.23  ? 81   LEU   A CG     1 
ATOM   536  C CD1    . LEU   A  1 89  ? 38.274 -85.372  -10.872 1.00 34.09  ? 81   LEU   A CD1    1 
ATOM   537  C CD2    . LEU   A  1 89  ? 37.736 -83.088  -11.636 1.00 34.71  ? 81   LEU   A CD2    1 
ATOM   538  N N      . ILE   A  1 90  ? 32.893 -85.701  -13.076 1.00 25.45  ? 82   ILE   A N      1 
ATOM   539  C CA     . ILE   A  1 90  ? 32.148 -86.597  -13.954 1.00 24.37  ? 82   ILE   A CA     1 
ATOM   540  C C      . ILE   A  1 90  ? 30.772 -86.073  -14.385 1.00 28.69  ? 82   ILE   A C      1 
ATOM   541  O O      . ILE   A  1 90  ? 29.907 -85.795  -13.549 1.00 28.95  ? 82   ILE   A O      1 
ATOM   542  C CB     . ILE   A  1 90  ? 32.040 -88.013  -13.310 1.00 26.83  ? 82   ILE   A CB     1 
ATOM   543  C CG1    . ILE   A  1 90  ? 33.437 -88.610  -12.925 1.00 26.95  ? 82   ILE   A CG1    1 
ATOM   544  C CG2    . ILE   A  1 90  ? 31.217 -88.996  -14.176 1.00 25.59  ? 82   ILE   A CG2    1 
ATOM   545  C CD1    . ILE   A  1 90  ? 34.533 -88.727  -14.096 1.00 29.75  ? 82   ILE   A CD1    1 
ATOM   546  N N      . VAL   A  1 91  ? 30.572 -85.984  -15.702 1.00 23.77  ? 83   VAL   A N      1 
ATOM   547  C CA     . VAL   A  1 91  ? 29.284 -85.649  -16.298 1.00 22.91  ? 83   VAL   A CA     1 
ATOM   548  C C      . VAL   A  1 91  ? 28.768 -86.972  -16.874 1.00 26.35  ? 83   VAL   A C      1 
ATOM   549  O O      . VAL   A  1 91  ? 29.470 -87.634  -17.636 1.00 25.60  ? 83   VAL   A O      1 
ATOM   550  C CB     . VAL   A  1 91  ? 29.325 -84.484  -17.325 1.00 25.71  ? 83   VAL   A CB     1 
ATOM   551  C CG1    . VAL   A  1 91  ? 28.022 -84.396  -18.124 1.00 25.20  ? 83   VAL   A CG1    1 
ATOM   552  C CG2    . VAL   A  1 91  ? 29.603 -83.157  -16.625 1.00 25.31  ? 83   VAL   A CG2    1 
ATOM   553  N N      . GLY   A  1 92  ? 27.600 -87.397  -16.411 1.00 22.49  ? 84   GLY   A N      1 
ATOM   554  C CA     . GLY   A  1 92  ? 27.010 -88.649  -16.858 1.00 22.63  ? 84   GLY   A CA     1 
ATOM   555  C C      . GLY   A  1 92  ? 26.371 -88.533  -18.225 1.00 25.98  ? 84   GLY   A C      1 
ATOM   556  O O      . GLY   A  1 92  ? 26.044 -87.432  -18.683 1.00 25.40  ? 84   GLY   A O      1 
ATOM   557  N N      . LYS   A  1 93  ? 26.204 -89.661  -18.890 1.00 22.08  ? 85   LYS   A N      1 
ATOM   558  C CA     . LYS   A  1 93  ? 25.582 -89.690  -20.214 1.00 22.17  ? 85   LYS   A CA     1 
ATOM   559  C C      . LYS   A  1 93  ? 24.547 -90.794  -20.264 1.00 25.35  ? 85   LYS   A C      1 
ATOM   560  O O      . LYS   A  1 93  ? 24.816 -91.908  -19.818 1.00 26.23  ? 85   LYS   A O      1 
ATOM   561  C CB     . LYS   A  1 93  ? 26.634 -89.942  -21.292 1.00 24.68  ? 85   LYS   A CB     1 
ATOM   562  C CG     . LYS   A  1 93  ? 27.463 -88.730  -21.663 1.00 35.89  ? 85   LYS   A CG     1 
ATOM   563  C CD     . LYS   A  1 93  ? 28.742 -89.143  -22.383 1.00 41.50  ? 85   LYS   A CD     1 
ATOM   564  C CE     . LYS   A  1 93  ? 28.487 -89.749  -23.739 1.00 44.60  ? 85   LYS   A CE     1 
ATOM   565  N NZ     . LYS   A  1 93  ? 29.745 -90.041  -24.462 1.00 50.94  ? 85   LYS   A NZ     1 
ATOM   566  N N      . LEU   A  1 94  ? 23.369 -90.492  -20.797 1.00 21.52  ? 86   LEU   A N      1 
ATOM   567  C CA     . LEU   A  1 94  ? 22.319 -91.491  -20.950 1.00 21.93  ? 86   LEU   A CA     1 
ATOM   568  C C      . LEU   A  1 94  ? 22.752 -92.475  -22.057 1.00 25.18  ? 86   LEU   A C      1 
ATOM   569  O O      . LEU   A  1 94  ? 23.317 -92.046  -23.071 1.00 25.01  ? 86   LEU   A O      1 
ATOM   570  C CB     . LEU   A  1 94  ? 20.990 -90.817  -21.326 1.00 22.21  ? 86   LEU   A CB     1 
ATOM   571  C CG     . LEU   A  1 94  ? 19.740 -91.721  -21.339 1.00 27.07  ? 86   LEU   A CG     1 
ATOM   572  C CD1    . LEU   A  1 94  ? 19.198 -91.941  -19.935 1.00 27.10  ? 86   LEU   A CD1    1 
ATOM   573  C CD2    . LEU   A  1 94  ? 18.670 -91.146  -22.241 1.00 29.52  ? 86   LEU   A CD2    1 
ATOM   574  N N      . SER   A  1 95  ? 22.510 -93.780  -21.844 1.00 20.39  ? 87   SER   A N      1 
ATOM   575  C CA     . SER   A  1 95  ? 22.861 -94.825  -22.807 1.00 20.76  ? 87   SER   A CA     1 
ATOM   576  C C      . SER   A  1 95  ? 22.172 -94.620  -24.180 1.00 25.53  ? 87   SER   A C      1 
ATOM   577  O O      . SER   A  1 95  ? 21.006 -94.222  -24.202 1.00 23.79  ? 87   SER   A O      1 
ATOM   578  C CB     . SER   A  1 95  ? 22.547 -96.197  -22.239 1.00 21.86  ? 87   SER   A CB     1 
ATOM   579  O OG     . SER   A  1 95  ? 23.456 -96.475  -21.191 1.00 30.14  ? 87   SER   A OG     1 
ATOM   580  N N      . PRO   A  1 96  ? 22.871 -94.867  -25.322 1.00 24.50  ? 88   PRO   A N      1 
ATOM   581  C CA     . PRO   A  1 96  ? 22.254 -94.593  -26.640 1.00 24.05  ? 88   PRO   A CA     1 
ATOM   582  C C      . PRO   A  1 96  ? 21.057 -95.463  -27.013 1.00 26.21  ? 88   PRO   A C      1 
ATOM   583  O O      . PRO   A  1 96  ? 20.236 -95.022  -27.810 1.00 25.55  ? 88   PRO   A O      1 
ATOM   584  C CB     . PRO   A  1 96  ? 23.412 -94.756  -27.631 1.00 26.04  ? 88   PRO   A CB     1 
ATOM   585  C CG     . PRO   A  1 96  ? 24.409 -95.584  -26.930 1.00 30.62  ? 88   PRO   A CG     1 
ATOM   586  C CD     . PRO   A  1 96  ? 24.281 -95.289  -25.467 1.00 26.16  ? 88   PRO   A CD     1 
ATOM   587  N N      . TRP   A  1 97  ? 20.931 -96.667  -26.426 1.00 21.99  ? 89   TRP   A N      1 
ATOM   588  C CA     . TRP   A  1 97  ? 19.808 -97.566  -26.707 1.00 21.03  ? 89   TRP   A CA     1 
ATOM   589  C C      . TRP   A  1 97  ? 18.512 -97.126  -26.008 1.00 24.13  ? 89   TRP   A C      1 
ATOM   590  O O      . TRP   A  1 97  ? 17.449 -97.648  -26.344 1.00 23.99  ? 89   TRP   A O      1 
ATOM   591  C CB     . TRP   A  1 97  ? 20.159 -99.022  -26.329 1.00 19.93  ? 89   TRP   A CB     1 
ATOM   592  C CG     . TRP   A  1 97  ? 20.443 -99.227  -24.860 1.00 20.90  ? 89   TRP   A CG     1 
ATOM   593  C CD1    . TRP   A  1 97  ? 21.654 -99.132  -24.239 1.00 23.65  ? 89   TRP   A CD1    1 
ATOM   594  C CD2    . TRP   A  1 97  ? 19.496 -99.588  -23.841 1.00 20.75  ? 89   TRP   A CD2    1 
ATOM   595  N NE1    . TRP   A  1 97  ? 21.527 -99.434  -22.904 1.00 23.06  ? 89   TRP   A NE1    1 
ATOM   596  C CE2    . TRP   A  1 97  ? 20.211 -99.707  -22.628 1.00 24.64  ? 89   TRP   A CE2    1 
ATOM   597  C CE3    . TRP   A  1 97  ? 18.109 -99.832  -23.837 1.00 22.09  ? 89   TRP   A CE3    1 
ATOM   598  C CZ2    . TRP   A  1 97  ? 19.579 -100.011 -21.410 1.00 24.02  ? 89   TRP   A CZ2    1 
ATOM   599  C CZ3    . TRP   A  1 97  ? 17.488 -100.164 -22.636 1.00 23.69  ? 89   TRP   A CZ3    1 
ATOM   600  C CH2    . TRP   A  1 97  ? 18.227 -100.291 -21.450 1.00 24.27  ? 89   TRP   A CH2    1 
ATOM   601  N N      . ILE   A  1 98  ? 18.592 -96.200  -25.018 1.00 19.56  ? 90   ILE   A N      1 
ATOM   602  C CA     . ILE   A  1 98  ? 17.401 -95.745  -24.298 1.00 19.28  ? 90   ILE   A CA     1 
ATOM   603  C C      . ILE   A  1 98  ? 16.552 -94.861  -25.226 1.00 20.48  ? 90   ILE   A C      1 
ATOM   604  O O      . ILE   A  1 98  ? 16.983 -93.771  -25.605 1.00 19.16  ? 90   ILE   A O      1 
ATOM   605  C CB     . ILE   A  1 98  ? 17.772 -95.095  -22.932 1.00 22.66  ? 90   ILE   A CB     1 
ATOM   606  C CG1    . ILE   A  1 98  ? 18.383 -96.160  -21.983 1.00 23.18  ? 90   ILE   A CG1    1 
ATOM   607  C CG2    . ILE   A  1 98  ? 16.556 -94.389  -22.277 1.00 23.49  ? 90   ILE   A CG2    1 
ATOM   608  C CD1    . ILE   A  1 98  ? 19.139 -95.606  -20.795 1.00 23.30  ? 90   ILE   A CD1    1 
ATOM   609  N N      . ARG   A  1 99  ? 15.378 -95.364  -25.636 1.00 16.64  ? 91   ARG   A N      1 
ATOM   610  C CA     . ARG   A  1 99  ? 14.486 -94.648  -26.573 1.00 16.58  ? 91   ARG   A CA     1 
ATOM   611  C C      . ARG   A  1 99  ? 13.055 -94.609  -26.015 1.00 20.37  ? 91   ARG   A C      1 
ATOM   612  O O      . ARG   A  1 99  ? 12.215 -95.429  -26.401 1.00 18.66  ? 91   ARG   A O      1 
ATOM   613  C CB     . ARG   A  1 99  ? 14.534 -95.280  -27.989 1.00 18.35  ? 91   ARG   A CB     1 
ATOM   614  C CG     . ARG   A  1 99  ? 15.928 -95.290  -28.656 1.00 30.75  ? 91   ARG   A CG     1 
ATOM   615  C CD     . ARG   A  1 99  ? 16.273 -94.009  -29.420 1.00 36.81  ? 91   ARG   A CD     1 
ATOM   616  N NE     . ARG   A  1 99  ? 16.552 -92.872  -28.535 1.00 39.15  ? 91   ARG   A NE     1 
ATOM   617  C CZ     . ARG   A  1 99  ? 16.420 -91.593  -28.880 1.00 51.45  ? 91   ARG   A CZ     1 
ATOM   618  N NH1    . ARG   A  1 99  ? 16.023 -91.264  -30.106 1.00 38.44  ? 91   ARG   A NH1    1 
ATOM   619  N NH2    . ARG   A  1 99  ? 16.697 -90.632  -28.007 1.00 36.48  ? 91   ARG   A NH2    1 
ATOM   620  N N      . PRO   A  1 100 ? 12.761 -93.664  -25.082 1.00 18.55  ? 92   PRO   A N      1 
ATOM   621  C CA     . PRO   A  1 100 ? 11.417 -93.625  -24.472 1.00 18.44  ? 92   PRO   A CA     1 
ATOM   622  C C      . PRO   A  1 100 ? 10.301 -93.259  -25.437 1.00 22.65  ? 92   PRO   A C      1 
ATOM   623  O O      . PRO   A  1 100 ? 9.138  -93.505  -25.139 1.00 21.58  ? 92   PRO   A O      1 
ATOM   624  C CB     . PRO   A  1 100 ? 11.564 -92.595  -23.347 1.00 20.45  ? 92   PRO   A CB     1 
ATOM   625  C CG     . PRO   A  1 100 ? 13.033 -92.403  -23.167 1.00 25.07  ? 92   PRO   A CG     1 
ATOM   626  C CD     . PRO   A  1 100 ? 13.636 -92.627  -24.502 1.00 20.33  ? 92   PRO   A CD     1 
ATOM   627  N N      . ASP   A  1 101 ? 10.652 -92.686  -26.596 1.00 21.44  ? 93   ASP   A N      1 
ATOM   628  C CA     . ASP   A  1 101 ? 9.668  -92.304  -27.610 1.00 21.62  ? 93   ASP   A CA     1 
ATOM   629  C C      . ASP   A  1 101 ? 9.641  -93.253  -28.827 1.00 26.01  ? 93   ASP   A C      1 
ATOM   630  O O      . ASP   A  1 101 ? 9.122  -92.890  -29.880 1.00 27.04  ? 93   ASP   A O      1 
ATOM   631  C CB     . ASP   A  1 101 ? 9.858  -90.837  -28.010 1.00 22.77  ? 93   ASP   A CB     1 
ATOM   632  C CG     . ASP   A  1 101 ? 9.412  -89.926  -26.883 1.00 24.96  ? 93   ASP   A CG     1 
ATOM   633  O OD1    . ASP   A  1 101 ? 8.190  -89.705  -26.752 1.00 23.35  ? 93   ASP   A OD1    1 
ATOM   634  O OD2    . ASP   A  1 101 ? 10.278 -89.487  -26.099 1.00 24.63  ? 93   ASP   A OD2    1 
ATOM   635  N N      . SER   A  1 102 ? 10.123 -94.491  -28.651 1.00 23.41  ? 94   SER   A N      1 
ATOM   636  C CA     . SER   A  1 102 ? 10.118 -95.548  -29.679 1.00 23.54  ? 94   SER   A CA     1 
ATOM   637  C C      . SER   A  1 102 ? 8.687  -95.870  -30.154 1.00 28.64  ? 94   SER   A C      1 
ATOM   638  O O      . SER   A  1 102 ? 7.741  -95.665  -29.406 1.00 28.15  ? 94   SER   A O      1 
ATOM   639  C CB     . SER   A  1 102 ? 10.752 -96.814  -29.111 1.00 25.97  ? 94   SER   A CB     1 
ATOM   640  O OG     . SER   A  1 102 ? 10.622 -97.924  -29.988 1.00 32.47  ? 94   SER   A OG     1 
ATOM   641  N N      . LYS   A  1 103 ? 8.530  -96.425  -31.365 1.00 27.14  ? 95   LYS   A N      1 
ATOM   642  C CA     . LYS   A  1 103 ? 7.203  -96.818  -31.873 1.00 27.90  ? 95   LYS   A CA     1 
ATOM   643  C C      . LYS   A  1 103 ? 6.791  -98.173  -31.285 1.00 32.53  ? 95   LYS   A C      1 
ATOM   644  O O      . LYS   A  1 103 ? 5.620  -98.567  -31.353 1.00 33.23  ? 95   LYS   A O      1 
ATOM   645  C CB     . LYS   A  1 103 ? 7.194  -96.876  -33.417 1.00 31.58  ? 95   LYS   A CB     1 
ATOM   646  C CG     . LYS   A  1 103 ? 7.349  -95.518  -34.103 1.00 48.74  ? 95   LYS   A CG     1 
ATOM   647  C CD     . LYS   A  1 103 ? 6.020  -94.792  -34.280 1.00 61.10  ? 95   LYS   A CD     1 
ATOM   648  C CE     . LYS   A  1 103 ? 6.226  -93.394  -34.807 1.00 77.30  ? 95   LYS   A CE     1 
ATOM   649  N NZ     . LYS   A  1 103 ? 4.934  -92.688  -35.002 1.00 91.23  ? 95   LYS   A NZ     1 
ATOM   650  N N      . VAL   A  1 104 ? 7.759  -98.883  -30.703 1.00 28.43  ? 96   VAL   A N      1 
ATOM   651  C CA     . VAL   A  1 104 ? 7.541  -100.197 -30.104 1.00 28.37  ? 96   VAL   A CA     1 
ATOM   652  C C      . VAL   A  1 104 ? 7.238  -100.033 -28.605 1.00 33.10  ? 96   VAL   A C      1 
ATOM   653  O O      . VAL   A  1 104 ? 8.079  -99.502  -27.873 1.00 32.64  ? 96   VAL   A O      1 
ATOM   654  C CB     . VAL   A  1 104 ? 8.765  -101.112 -30.348 1.00 31.50  ? 96   VAL   A CB     1 
ATOM   655  C CG1    . VAL   A  1 104 ? 8.616  -102.422 -29.609 1.00 31.07  ? 96   VAL   A CG1    1 
ATOM   656  C CG2    . VAL   A  1 104 ? 9.001  -101.356 -31.833 1.00 31.18  ? 96   VAL   A CG2    1 
ATOM   657  N N      . GLU   A  1 105 ? 6.057  -100.514 -28.154 1.00 30.61  ? 97   GLU   A N      1 
ATOM   658  C CA     . GLU   A  1 105 ? 5.628  -100.438 -26.750 1.00 30.94  ? 97   GLU   A CA     1 
ATOM   659  C C      . GLU   A  1 105 ? 6.663  -101.021 -25.775 1.00 33.23  ? 97   GLU   A C      1 
ATOM   660  O O      . GLU   A  1 105 ? 6.990  -100.355 -24.790 1.00 32.52  ? 97   GLU   A O      1 
ATOM   661  C CB     . GLU   A  1 105 ? 4.241  -101.074 -26.532 1.00 32.57  ? 97   GLU   A CB     1 
ATOM   662  C CG     . GLU   A  1 105 ? 3.654  -100.752 -25.160 1.00 44.53  ? 97   GLU   A CG     1 
ATOM   663  C CD     . GLU   A  1 105 ? 2.609  -101.710 -24.623 1.00 65.14  ? 97   GLU   A CD     1 
ATOM   664  O OE1    . GLU   A  1 105 ? 2.959  -102.878 -24.336 1.00 66.42  ? 97   GLU   A OE1    1 
ATOM   665  O OE2    . GLU   A  1 105 ? 1.453  -101.271 -24.423 1.00 58.21  ? 97   GLU   A OE2    1 
ATOM   666  N N      . LYS   A  1 106 ? 7.205  -102.223 -26.072 1.00 28.75  ? 98   LYS   A N      1 
ATOM   667  C CA     . LYS   A  1 106 ? 8.210  -102.900 -25.234 1.00 28.83  ? 98   LYS   A CA     1 
ATOM   668  C C      . LYS   A  1 106 ? 9.489  -102.078 -25.082 1.00 31.33  ? 98   LYS   A C      1 
ATOM   669  O O      . LYS   A  1 106 ? 10.071 -102.051 -23.991 1.00 31.23  ? 98   LYS   A O      1 
ATOM   670  C CB     . LYS   A  1 106 ? 8.534  -104.312 -25.752 1.00 31.39  ? 98   LYS   A CB     1 
ATOM   671  C CG     . LYS   A  1 106 ? 7.388  -105.304 -25.591 1.00 44.02  ? 98   LYS   A CG     1 
ATOM   672  C CD     . LYS   A  1 106 ? 7.872  -106.742 -25.702 1.00 51.31  ? 98   LYS   A CD     1 
ATOM   673  C CE     . LYS   A  1 106 ? 6.747  -107.704 -25.982 1.00 54.19  ? 98   LYS   A CE     1 
ATOM   674  N NZ     . LYS   A  1 106 ? 7.216  -109.112 -25.960 1.00 58.73  ? 98   LYS   A NZ     1 
ATOM   675  N N      . ILE   A  1 107 ? 9.908  -101.392 -26.162 1.00 26.28  ? 99   ILE   A N      1 
ATOM   676  C CA     . ILE   A  1 107 ? 11.090 -100.529 -26.133 1.00 24.94  ? 99   ILE   A CA     1 
ATOM   677  C C      . ILE   A  1 107 ? 10.798 -99.270  -25.293 1.00 28.30  ? 99   ILE   A C      1 
ATOM   678  O O      . ILE   A  1 107 ? 11.661 -98.875  -24.514 1.00 27.38  ? 99   ILE   A O      1 
ATOM   679  C CB     . ILE   A  1 107 ? 11.676 -100.237 -27.543 1.00 27.26  ? 99   ILE   A CB     1 
ATOM   680  C CG1    . ILE   A  1 107 ? 12.092 -101.568 -28.255 1.00 27.15  ? 99   ILE   A CG1    1 
ATOM   681  C CG2    . ILE   A  1 107 ? 12.867 -99.259  -27.460 1.00 25.74  ? 99   ILE   A CG2    1 
ATOM   682  C CD1    . ILE   A  1 107 ? 12.504 -101.435 -29.761 1.00 31.20  ? 99   ILE   A CD1    1 
ATOM   683  N N      . ARG   A  1 108 ? 9.590  -98.669  -25.419 1.00 25.16  ? 100  ARG   A N      1 
ATOM   684  C CA     . ARG   A  1 108 ? 9.206  -97.496  -24.620 1.00 25.50  ? 100  ARG   A CA     1 
ATOM   685  C C      . ARG   A  1 108 ? 9.235  -97.807  -23.114 1.00 27.24  ? 100  ARG   A C      1 
ATOM   686  O O      . ARG   A  1 108 ? 9.786  -97.022  -22.347 1.00 25.91  ? 100  ARG   A O      1 
ATOM   687  C CB     . ARG   A  1 108 ? 7.811  -96.980  -24.995 1.00 25.88  ? 100  ARG   A CB     1 
ATOM   688  C CG     . ARG   A  1 108 ? 7.731  -96.272  -26.328 1.00 30.24  ? 100  ARG   A CG     1 
ATOM   689  C CD     . ARG   A  1 108 ? 6.480  -95.413  -26.422 1.00 36.08  ? 100  ARG   A CD     1 
ATOM   690  N NE     . ARG   A  1 108 ? 5.246  -96.179  -26.217 1.00 45.09  ? 100  ARG   A NE     1 
ATOM   691  C CZ     . ARG   A  1 108 ? 4.537  -96.753  -27.186 1.00 54.65  ? 100  ARG   A CZ     1 
ATOM   692  N NH1    . ARG   A  1 108 ? 4.936  -96.669  -28.449 1.00 35.63  ? 100  ARG   A NH1    1 
ATOM   693  N NH2    . ARG   A  1 108 ? 3.427  -97.420  -26.898 1.00 43.51  ? 100  ARG   A NH2    1 
ATOM   694  N N      . ARG   A  1 109 ? 8.663  -98.957  -22.706 1.00 24.06  ? 101  ARG   A N      1 
ATOM   695  C CA     . ARG   A  1 109 ? 8.593  -99.386  -21.305 1.00 23.73  ? 101  ARG   A CA     1 
ATOM   696  C C      . ARG   A  1 109 ? 9.977  -99.688  -20.705 1.00 27.15  ? 101  ARG   A C      1 
ATOM   697  O O      . ARG   A  1 109 ? 10.286 -99.156  -19.639 1.00 26.19  ? 101  ARG   A O      1 
ATOM   698  C CB     . ARG   A  1 109 ? 7.613  -100.559 -21.127 1.00 26.79  ? 101  ARG   A CB     1 
ATOM   699  C CG     . ARG   A  1 109 ? 6.140  -100.170 -21.294 1.00 41.00  ? 101  ARG   A CG     1 
ATOM   700  C CD     . ARG   A  1 109 ? 5.228  -101.251 -20.734 1.00 56.20  ? 101  ARG   A CD     1 
ATOM   701  N NE     . ARG   A  1 109 ? 3.818  -101.059 -21.092 1.00 65.64  ? 101  ARG   A NE     1 
ATOM   702  C CZ     . ARG   A  1 109 ? 2.939  -100.375 -20.364 1.00 82.27  ? 101  ARG   A CZ     1 
ATOM   703  N NH1    . ARG   A  1 109 ? 3.314  -99.791  -19.231 1.00 76.39  ? 101  ARG   A NH1    1 
ATOM   704  N NH2    . ARG   A  1 109 ? 1.679  -100.267 -20.764 1.00 66.02  ? 101  ARG   A NH2    1 
ATOM   705  N N      . ASN   A  1 110 ? 10.823 -100.494 -21.396 1.00 23.99  ? 102  ASN   A N      1 
ATOM   706  C CA     . ASN   A  1 110 ? 12.195 -100.801 -20.935 1.00 24.08  ? 102  ASN   A CA     1 
ATOM   707  C C      . ASN   A  1 110 ? 13.049 -99.532  -20.877 1.00 25.49  ? 102  ASN   A C      1 
ATOM   708  O O      . ASN   A  1 110 ? 13.875 -99.392  -19.977 1.00 24.61  ? 102  ASN   A O      1 
ATOM   709  C CB     . ASN   A  1 110 ? 12.901 -101.813 -21.867 1.00 23.69  ? 102  ASN   A CB     1 
ATOM   710  C CG     . ASN   A  1 110 ? 12.607 -103.258 -21.581 1.00 43.17  ? 102  ASN   A CG     1 
ATOM   711  O OD1    . ASN   A  1 110 ? 12.632 -103.709 -20.432 1.00 28.55  ? 102  ASN   A OD1    1 
ATOM   712  N ND2    . ASN   A  1 110 ? 12.352 -104.033 -22.640 1.00 41.29  ? 102  ASN   A ND2    1 
ATOM   713  N N      . SER   A  1 111 ? 12.863 -98.628  -21.860 1.00 20.72  ? 103  SER   A N      1 
ATOM   714  C CA     . SER   A  1 111 ? 13.620 -97.385  -21.935 1.00 19.40  ? 103  SER   A CA     1 
ATOM   715  C C      . SER   A  1 111 ? 13.284 -96.444  -20.810 1.00 21.66  ? 103  SER   A C      1 
ATOM   716  O O      . SER   A  1 111 ? 14.194 -95.790  -20.330 1.00 21.79  ? 103  SER   A O      1 
ATOM   717  C CB     . SER   A  1 111 ? 13.441 -96.717  -23.285 1.00 20.97  ? 103  SER   A CB     1 
ATOM   718  O OG     . SER   A  1 111 ? 14.053 -97.501  -24.296 1.00 26.31  ? 103  SER   A OG     1 
ATOM   719  N N      . GLU   A  1 112 ? 11.992 -96.385  -20.384 1.00 18.63  ? 104  GLU   A N      1 
ATOM   720  C CA     A GLU   A  1 112 ? 11.544 -95.558  -19.262 0.50 19.19  ? 104  GLU   A CA     1 
ATOM   721  C CA     B GLU   A  1 112 ? 11.551 -95.548  -19.264 0.50 18.77  ? 104  GLU   A CA     1 
ATOM   722  C C      . GLU   A  1 112 ? 12.205 -96.083  -17.985 1.00 23.13  ? 104  GLU   A C      1 
ATOM   723  O O      . GLU   A  1 112 ? 12.791 -95.304  -17.228 1.00 22.21  ? 104  GLU   A O      1 
ATOM   724  C CB     A GLU   A  1 112 ? 10.015 -95.632  -19.105 0.50 20.68  ? 104  GLU   A CB     1 
ATOM   725  C CB     B GLU   A  1 112 ? 10.004 -95.526  -19.137 0.50 19.91  ? 104  GLU   A CB     1 
ATOM   726  C CG     A GLU   A  1 112 ? 9.223  -94.865  -20.145 0.50 30.10  ? 104  GLU   A CG     1 
ATOM   727  C CG     B GLU   A  1 112 ? 9.494  -94.965  -17.809 0.50 24.95  ? 104  GLU   A CG     1 
ATOM   728  C CD     A GLU   A  1 112 ? 7.728  -95.112  -20.090 0.50 45.02  ? 104  GLU   A CD     1 
ATOM   729  C CD     B GLU   A  1 112 ? 8.002  -94.776  -17.605 0.50 38.81  ? 104  GLU   A CD     1 
ATOM   730  O OE1    A GLU   A  1 112 ? 7.144  -95.427  -21.151 0.50 19.13  ? 104  GLU   A OE1    1 
ATOM   731  O OE1    B GLU   A  1 112 ? 7.636  -94.071  -16.638 0.50 24.61  ? 104  GLU   A OE1    1 
ATOM   732  O OE2    A GLU   A  1 112 ? 7.139  -94.993  -18.991 0.50 48.45  ? 104  GLU   A OE2    1 
ATOM   733  O OE2    B GLU   A  1 112 ? 7.198  -95.361  -18.367 0.50 37.76  ? 104  GLU   A OE2    1 
ATOM   734  N N      . ALA   A  1 113 ? 12.117 -97.424  -17.755 1.00 20.35  ? 105  ALA   A N      1 
ATOM   735  C CA     . ALA   A  1 113 ? 12.704 -98.078  -16.585 1.00 19.92  ? 105  ALA   A CA     1 
ATOM   736  C C      . ALA   A  1 113 ? 14.219 -97.879  -16.554 1.00 24.65  ? 105  ALA   A C      1 
ATOM   737  O O      . ALA   A  1 113 ? 14.746 -97.523  -15.502 1.00 25.77  ? 105  ALA   A O      1 
ATOM   738  C CB     . ALA   A  1 113 ? 12.351 -99.560  -16.563 1.00 20.50  ? 105  ALA   A CB     1 
ATOM   739  N N      . ALA   A  1 114 ? 14.904 -98.015  -17.715 1.00 21.18  ? 106  ALA   A N      1 
ATOM   740  C CA     . ALA   A  1 114 ? 16.357 -97.816  -17.818 1.00 20.38  ? 106  ALA   A CA     1 
ATOM   741  C C      . ALA   A  1 114 ? 16.768 -96.376  -17.631 1.00 22.08  ? 106  ALA   A C      1 
ATOM   742  O O      . ALA   A  1 114 ? 17.840 -96.115  -17.089 1.00 20.69  ? 106  ALA   A O      1 
ATOM   743  C CB     . ALA   A  1 114 ? 16.863 -98.312  -19.156 1.00 20.90  ? 106  ALA   A CB     1 
ATOM   744  N N      . MET   A  1 115 ? 15.963 -95.435  -18.148 1.00 20.17  ? 107  MET   A N      1 
ATOM   745  C CA     . MET   A  1 115 ? 16.266 -94.008  -18.030 1.00 19.78  ? 107  MET   A CA     1 
ATOM   746  C C      . MET   A  1 115 ? 16.185 -93.580  -16.555 1.00 22.42  ? 107  MET   A C      1 
ATOM   747  O O      . MET   A  1 115 ? 17.086 -92.896  -16.064 1.00 21.90  ? 107  MET   A O      1 
ATOM   748  C CB     . MET   A  1 115 ? 15.328 -93.183  -18.921 1.00 21.41  ? 107  MET   A CB     1 
ATOM   749  C CG     . MET   A  1 115 ? 15.531 -91.690  -18.786 1.00 24.06  ? 107  MET   A CG     1 
ATOM   750  S SD     . MET   A  1 115 ? 14.443 -90.811  -19.908 1.00 26.04  ? 107  MET   A SD     1 
ATOM   751  C CE     . MET   A  1 115 ? 14.503 -89.157  -19.191 1.00 22.55  ? 107  MET   A CE     1 
ATOM   752  N N      . LEU   A  1 116 ? 15.139 -94.043  -15.842 1.00 18.88  ? 108  LEU   A N      1 
ATOM   753  C CA     . LEU   A  1 116 ? 14.964 -93.783  -14.412 1.00 19.03  ? 108  LEU   A CA     1 
ATOM   754  C C      . LEU   A  1 116 ? 16.113 -94.381  -13.609 1.00 21.01  ? 108  LEU   A C      1 
ATOM   755  O O      . LEU   A  1 116 ? 16.629 -93.739  -12.705 1.00 20.04  ? 108  LEU   A O      1 
ATOM   756  C CB     . LEU   A  1 116 ? 13.607 -94.322  -13.914 1.00 19.32  ? 108  LEU   A CB     1 
ATOM   757  C CG     . LEU   A  1 116 ? 12.381 -93.484  -14.321 1.00 24.43  ? 108  LEU   A CG     1 
ATOM   758  C CD1    . LEU   A  1 116 ? 11.087 -94.174  -13.928 1.00 24.48  ? 108  LEU   A CD1    1 
ATOM   759  C CD2    . LEU   A  1 116 ? 12.434 -92.055  -13.723 1.00 26.59  ? 108  LEU   A CD2    1 
ATOM   760  N N      . GLN   A  1 117 ? 16.570 -95.568  -14.003 1.00 18.48  ? 109  GLN   A N      1 
ATOM   761  C CA     . GLN   A  1 117 ? 17.680 -96.267  -13.361 1.00 18.86  ? 109  GLN   A CA     1 
ATOM   762  C C      . GLN   A  1 117 ? 18.991 -95.501  -13.500 1.00 23.83  ? 109  GLN   A C      1 
ATOM   763  O O      . GLN   A  1 117 ? 19.700 -95.336  -12.510 1.00 23.46  ? 109  GLN   A O      1 
ATOM   764  C CB     . GLN   A  1 117 ? 17.791 -97.663  -13.978 1.00 20.57  ? 109  GLN   A CB     1 
ATOM   765  C CG     . GLN   A  1 117 ? 19.105 -98.398  -13.741 1.00 29.78  ? 109  GLN   A CG     1 
ATOM   766  C CD     . GLN   A  1 117 ? 19.106 -99.662  -14.562 1.00 35.55  ? 109  GLN   A CD     1 
ATOM   767  O OE1    . GLN   A  1 117 ? 19.160 -99.622  -15.778 1.00 31.29  ? 109  GLN   A OE1    1 
ATOM   768  N NE2    . GLN   A  1 117 ? 18.918 -100.800 -13.940 1.00 24.98  ? 109  GLN   A NE2    1 
ATOM   769  N N      . GLU   A  1 118 ? 19.307 -95.022  -14.720 1.00 21.36  ? 110  GLU   A N      1 
ATOM   770  C CA     . GLU   A  1 118 ? 20.549 -94.291  -14.969 1.00 21.44  ? 110  GLU   A CA     1 
ATOM   771  C C      . GLU   A  1 118 ? 20.531 -92.932  -14.301 1.00 25.18  ? 110  GLU   A C      1 
ATOM   772  O O      . GLU   A  1 118 ? 21.545 -92.509  -13.750 1.00 24.24  ? 110  GLU   A O      1 
ATOM   773  C CB     . GLU   A  1 118 ? 20.848 -94.182  -16.474 1.00 22.79  ? 110  GLU   A CB     1 
ATOM   774  C CG     . GLU   A  1 118 ? 21.027 -95.541  -17.136 1.00 28.85  ? 110  GLU   A CG     1 
ATOM   775  C CD     . GLU   A  1 118 ? 21.751 -95.596  -18.470 1.00 42.46  ? 110  GLU   A CD     1 
ATOM   776  O OE1    . GLU   A  1 118 ? 22.106 -94.529  -19.023 1.00 30.77  ? 110  GLU   A OE1    1 
ATOM   777  O OE2    . GLU   A  1 118 ? 21.939 -96.724  -18.978 1.00 27.92  ? 110  GLU   A OE2    1 
ATOM   778  N N      . LEU   A  1 119 ? 19.375 -92.246  -14.342 1.00 22.42  ? 111  LEU   A N      1 
ATOM   779  C CA     . LEU   A  1 119 ? 19.206 -90.942  -13.701 1.00 20.82  ? 111  LEU   A CA     1 
ATOM   780  C C      . LEU   A  1 119 ? 19.337 -91.095  -12.183 1.00 22.67  ? 111  LEU   A C      1 
ATOM   781  O O      . LEU   A  1 119 ? 20.033 -90.306  -11.548 1.00 21.06  ? 111  LEU   A O      1 
ATOM   782  C CB     . LEU   A  1 119 ? 17.853 -90.306  -14.075 1.00 20.38  ? 111  LEU   A CB     1 
ATOM   783  C CG     . LEU   A  1 119 ? 17.711 -89.747  -15.508 1.00 23.52  ? 111  LEU   A CG     1 
ATOM   784  C CD1    . LEU   A  1 119 ? 16.258 -89.381  -15.808 1.00 23.22  ? 111  LEU   A CD1    1 
ATOM   785  C CD2    . LEU   A  1 119 ? 18.655 -88.561  -15.766 1.00 22.05  ? 111  LEU   A CD2    1 
ATOM   786  N N      . ASN   A  1 120 ? 18.739 -92.149  -11.611 1.00 19.51  ? 112  ASN   A N      1 
ATOM   787  C CA     . ASN   A  1 120 ? 18.858 -92.332  -10.169 1.00 19.91  ? 112  ASN   A CA     1 
ATOM   788  C C      . ASN   A  1 120 ? 20.256 -92.763  -9.734  1.00 23.97  ? 112  ASN   A C      1 
ATOM   789  O O      . ASN   A  1 120 ? 20.698 -92.347  -8.658  1.00 23.01  ? 112  ASN   A O      1 
ATOM   790  C CB     . ASN   A  1 120 ? 17.790 -93.229  -9.625  1.00 20.43  ? 112  ASN   A CB     1 
ATOM   791  C CG     . ASN   A  1 120 ? 16.446 -92.578  -9.606  1.00 32.79  ? 112  ASN   A CG     1 
ATOM   792  O OD1    . ASN   A  1 120 ? 16.296 -91.447  -9.172  1.00 34.67  ? 112  ASN   A OD1    1 
ATOM   793  N ND2    . ASN   A  1 120 ? 15.434 -93.288  -10.038 1.00 28.98  ? 112  ASN   A ND2    1 
ATOM   794  N N      . PHE   A  1 121 ? 20.990 -93.494  -10.607 1.00 20.35  ? 113  PHE   A N      1 
ATOM   795  C CA     . PHE   A  1 121 ? 22.376 -93.845  -10.319 1.00 19.92  ? 113  PHE   A CA     1 
ATOM   796  C C      . PHE   A  1 121 ? 23.243 -92.596  -10.334 1.00 23.08  ? 113  PHE   A C      1 
ATOM   797  O O      . PHE   A  1 121 ? 24.111 -92.473  -9.494  1.00 23.64  ? 113  PHE   A O      1 
ATOM   798  C CB     . PHE   A  1 121 ? 22.929 -94.949  -11.241 1.00 21.97  ? 113  PHE   A CB     1 
ATOM   799  C CG     . PHE   A  1 121 ? 24.208 -95.560  -10.709 1.00 24.14  ? 113  PHE   A CG     1 
ATOM   800  C CD1    . PHE   A  1 121 ? 24.201 -96.332  -9.549  1.00 27.29  ? 113  PHE   A CD1    1 
ATOM   801  C CD2    . PHE   A  1 121 ? 25.413 -95.387  -11.378 1.00 26.89  ? 113  PHE   A CD2    1 
ATOM   802  C CE1    . PHE   A  1 121 ? 25.386 -96.884  -9.049  1.00 28.42  ? 113  PHE   A CE1    1 
ATOM   803  C CE2    . PHE   A  1 121 ? 26.592 -95.973  -10.896 1.00 29.64  ? 113  PHE   A CE2    1 
ATOM   804  C CZ     . PHE   A  1 121 ? 26.573 -96.703  -9.726  1.00 27.26  ? 113  PHE   A CZ     1 
ATOM   805  N N      . GLY   A  1 122 ? 22.966 -91.665  -11.244 1.00 20.22  ? 114  GLY   A N      1 
ATOM   806  C CA     . GLY   A  1 122 ? 23.653 -90.372  -11.317 1.00 19.99  ? 114  GLY   A CA     1 
ATOM   807  C C      . GLY   A  1 122 ? 23.388 -89.515  -10.091 1.00 23.79  ? 114  GLY   A C      1 
ATOM   808  O O      . GLY   A  1 122 ? 24.276 -88.796  -9.616  1.00 24.43  ? 114  GLY   A O      1 
ATOM   809  N N      . ALA   A  1 123 ? 22.156 -89.582  -9.564  1.00 19.85  ? 115  ALA   A N      1 
ATOM   810  C CA     . ALA   A  1 123 ? 21.760 -88.866  -8.344  1.00 18.59  ? 115  ALA   A CA     1 
ATOM   811  C C      . ALA   A  1 123 ? 22.489 -89.514  -7.140  1.00 23.74  ? 115  ALA   A C      1 
ATOM   812  O O      . ALA   A  1 123 ? 22.994 -88.799  -6.269  1.00 23.41  ? 115  ALA   A O      1 
ATOM   813  C CB     . ALA   A  1 123 ? 20.248 -88.942  -8.153  1.00 18.61  ? 115  ALA   A CB     1 
ATOM   814  N N      . TYR   A  1 124 ? 22.574 -90.866  -7.133  1.00 19.50  ? 116  TYR   A N      1 
ATOM   815  C CA     . TYR   A  1 124 ? 23.264 -91.661  -6.112  1.00 20.36  ? 116  TYR   A CA     1 
ATOM   816  C C      . TYR   A  1 124 ? 24.734 -91.265  -6.020  1.00 25.06  ? 116  TYR   A C      1 
ATOM   817  O O      . TYR   A  1 124 ? 25.244 -91.151  -4.921  1.00 25.49  ? 116  TYR   A O      1 
ATOM   818  C CB     . TYR   A  1 124 ? 23.121 -93.162  -6.408  1.00 21.28  ? 116  TYR   A CB     1 
ATOM   819  C CG     . TYR   A  1 124 ? 23.966 -94.069  -5.535  1.00 23.36  ? 116  TYR   A CG     1 
ATOM   820  C CD1    . TYR   A  1 124 ? 23.580 -94.373  -4.230  1.00 25.10  ? 116  TYR   A CD1    1 
ATOM   821  C CD2    . TYR   A  1 124 ? 25.110 -94.688  -6.039  1.00 23.92  ? 116  TYR   A CD2    1 
ATOM   822  C CE1    . TYR   A  1 124 ? 24.315 -95.261  -3.445  1.00 25.87  ? 116  TYR   A CE1    1 
ATOM   823  C CE2    . TYR   A  1 124 ? 25.864 -95.561  -5.256  1.00 24.57  ? 116  TYR   A CE2    1 
ATOM   824  C CZ     . TYR   A  1 124 ? 25.460 -95.849  -3.960  1.00 32.14  ? 116  TYR   A CZ     1 
ATOM   825  O OH     . TYR   A  1 124 ? 26.203 -96.702  -3.176  1.00 30.66  ? 116  TYR   A OH     1 
ATOM   826  N N      . LEU   A  1 125 ? 25.387 -90.996  -7.160  1.00 21.69  ? 117  LEU   A N      1 
ATOM   827  C CA     . LEU   A  1 125 ? 26.794 -90.592  -7.204  1.00 21.10  ? 117  LEU   A CA     1 
ATOM   828  C C      . LEU   A  1 125 ? 27.015 -89.111  -6.968  1.00 25.26  ? 117  LEU   A C      1 
ATOM   829  O O      . LEU   A  1 125 ? 28.152 -88.697  -6.778  1.00 26.30  ? 117  LEU   A O      1 
ATOM   830  C CB     . LEU   A  1 125 ? 27.450 -90.994  -8.542  1.00 20.85  ? 117  LEU   A CB     1 
ATOM   831  C CG     . LEU   A  1 125 ? 27.415 -92.460  -8.950  1.00 24.84  ? 117  LEU   A CG     1 
ATOM   832  C CD1    . LEU   A  1 125 ? 27.761 -92.597  -10.409 1.00 24.93  ? 117  LEU   A CD1    1 
ATOM   833  C CD2    . LEU   A  1 125 ? 28.370 -93.282  -8.125  1.00 25.91  ? 117  LEU   A CD2    1 
ATOM   834  N N      . GLY   A  1 126 ? 25.956 -88.316  -7.025  1.00 20.99  ? 118  GLY   A N      1 
ATOM   835  C CA     . GLY   A  1 126 ? 26.041 -86.870  -6.857  1.00 20.43  ? 118  GLY   A CA     1 
ATOM   836  C C      . GLY   A  1 126 ? 26.726 -86.170  -8.018  1.00 23.45  ? 118  GLY   A C      1 
ATOM   837  O O      . GLY   A  1 126 ? 27.449 -85.193  -7.808  1.00 23.83  ? 118  GLY   A O      1 
ATOM   838  N N      . LEU   A  1 127 ? 26.508 -86.661  -9.254  1.00 19.87  ? 119  LEU   A N      1 
ATOM   839  C CA     . LEU   A  1 127 ? 27.085 -86.071  -10.479 1.00 19.39  ? 119  LEU   A CA     1 
ATOM   840  C C      . LEU   A  1 127 ? 26.628 -84.615  -10.646 1.00 24.10  ? 119  LEU   A C      1 
ATOM   841  O O      . LEU   A  1 127 ? 25.459 -84.316  -10.368 1.00 23.10  ? 119  LEU   A O      1 
ATOM   842  C CB     . LEU   A  1 127 ? 26.703 -86.891  -11.730 1.00 19.01  ? 119  LEU   A CB     1 
ATOM   843  C CG     . LEU   A  1 127 ? 27.115 -88.377  -11.787 1.00 22.33  ? 119  LEU   A CG     1 
ATOM   844  C CD1    . LEU   A  1 127 ? 26.704 -89.003  -13.117 1.00 21.42  ? 119  LEU   A CD1    1 
ATOM   845  C CD2    . LEU   A  1 127 ? 28.609 -88.570  -11.538 1.00 23.00  ? 119  LEU   A CD2    1 
ATOM   846  N N      . PRO   A  1 128 ? 27.525 -83.677  -11.031 1.00 21.89  ? 120  PRO   A N      1 
ATOM   847  C CA     . PRO   A  1 128 ? 27.096 -82.280  -11.173 1.00 21.85  ? 120  PRO   A CA     1 
ATOM   848  C C      . PRO   A  1 128 ? 26.143 -82.050  -12.354 1.00 25.95  ? 120  PRO   A C      1 
ATOM   849  O O      . PRO   A  1 128 ? 25.355 -81.108  -12.321 1.00 25.94  ? 120  PRO   A O      1 
ATOM   850  C CB     . PRO   A  1 128 ? 28.419 -81.533  -11.362 1.00 23.41  ? 120  PRO   A CB     1 
ATOM   851  C CG     . PRO   A  1 128 ? 29.316 -82.522  -12.002 1.00 26.45  ? 120  PRO   A CG     1 
ATOM   852  C CD     . PRO   A  1 128 ? 28.957 -83.829  -11.360 1.00 22.77  ? 120  PRO   A CD     1 
ATOM   853  N N      . ALA   A  1 129 ? 26.247 -82.886  -13.413 1.00 22.34  ? 121  ALA   A N      1 
ATOM   854  C CA     . ALA   A  1 129 ? 25.423 -82.790  -14.617 1.00 20.92  ? 121  ALA   A CA     1 
ATOM   855  C C      . ALA   A  1 129 ? 25.252 -84.144  -15.286 1.00 23.31  ? 121  ALA   A C      1 
ATOM   856  O O      . ALA   A  1 129 ? 26.037 -85.059  -15.050 1.00 23.30  ? 121  ALA   A O      1 
ATOM   857  C CB     . ALA   A  1 129 ? 26.006 -81.773  -15.594 1.00 21.59  ? 121  ALA   A CB     1 
ATOM   858  N N      . PHE   A  1 130 ? 24.187 -84.281  -16.074 1.00 18.74  ? 122  PHE   A N      1 
ATOM   859  C CA     . PHE   A  1 130 ? 23.845 -85.495  -16.797 1.00 18.88  ? 122  PHE   A CA     1 
ATOM   860  C C      . PHE   A  1 130 ? 23.358 -85.095  -18.190 1.00 24.99  ? 122  PHE   A C      1 
ATOM   861  O O      . PHE   A  1 130 ? 22.445 -84.273  -18.313 1.00 24.66  ? 122  PHE   A O      1 
ATOM   862  C CB     . PHE   A  1 130 ? 22.774 -86.293  -16.032 1.00 20.29  ? 122  PHE   A CB     1 
ATOM   863  C CG     . PHE   A  1 130 ? 22.748 -87.763  -16.374 1.00 22.19  ? 122  PHE   A CG     1 
ATOM   864  C CD1    . PHE   A  1 130 ? 22.075 -88.222  -17.505 1.00 24.87  ? 122  PHE   A CD1    1 
ATOM   865  C CD2    . PHE   A  1 130 ? 23.375 -88.696  -15.554 1.00 24.76  ? 122  PHE   A CD2    1 
ATOM   866  C CE1    . PHE   A  1 130 ? 22.039 -89.588  -17.813 1.00 25.63  ? 122  PHE   A CE1    1 
ATOM   867  C CE2    . PHE   A  1 130 ? 23.339 -90.062  -15.865 1.00 27.65  ? 122  PHE   A CE2    1 
ATOM   868  C CZ     . PHE   A  1 130 ? 22.669 -90.498  -16.993 1.00 25.17  ? 122  PHE   A CZ     1 
ATOM   869  N N      . LEU   A  1 131 ? 24.006 -85.650  -19.234 1.00 22.57  ? 123  LEU   A N      1 
ATOM   870  C CA     . LEU   A  1 131 ? 23.720 -85.416  -20.645 1.00 22.06  ? 123  LEU   A CA     1 
ATOM   871  C C      . LEU   A  1 131 ? 22.648 -86.346  -21.185 1.00 25.57  ? 123  LEU   A C      1 
ATOM   872  O O      . LEU   A  1 131 ? 22.746 -87.559  -21.023 1.00 25.03  ? 123  LEU   A O      1 
ATOM   873  C CB     . LEU   A  1 131 ? 24.986 -85.586  -21.489 1.00 22.10  ? 123  LEU   A CB     1 
ATOM   874  C CG     . LEU   A  1 131 ? 25.898 -84.381  -21.617 1.00 27.55  ? 123  LEU   A CG     1 
ATOM   875  C CD1    . LEU   A  1 131 ? 27.300 -84.827  -22.004 1.00 28.94  ? 123  LEU   A CD1    1 
ATOM   876  C CD2    . LEU   A  1 131 ? 25.367 -83.389  -22.653 1.00 26.62  ? 123  LEU   A CD2    1 
ATOM   877  N N      . LEU   A  1 132 ? 21.626 -85.769  -21.831 1.00 21.99  ? 124  LEU   A N      1 
ATOM   878  C CA     . LEU   A  1 132 ? 20.533 -86.502  -22.471 1.00 21.85  ? 124  LEU   A CA     1 
ATOM   879  C C      . LEU   A  1 132 ? 20.396 -85.947  -23.892 1.00 23.52  ? 124  LEU   A C      1 
ATOM   880  O O      . LEU   A  1 132 ? 20.474 -84.740  -24.079 1.00 21.11  ? 124  LEU   A O      1 
ATOM   881  C CB     . LEU   A  1 132 ? 19.191 -86.339  -21.729 1.00 22.03  ? 124  LEU   A CB     1 
ATOM   882  C CG     . LEU   A  1 132 ? 19.123 -86.800  -20.283 1.00 27.25  ? 124  LEU   A CG     1 
ATOM   883  C CD1    . LEU   A  1 132 ? 19.229 -85.613  -19.342 1.00 26.99  ? 124  LEU   A CD1    1 
ATOM   884  C CD2    . LEU   A  1 132 ? 17.824 -87.544  -20.020 1.00 29.62  ? 124  LEU   A CD2    1 
ATOM   885  N N      . PRO   A  1 133 ? 20.144 -86.772  -24.917 1.00 22.98  ? 125  PRO   A N      1 
ATOM   886  C CA     . PRO   A  1 133 ? 20.039 -86.208  -26.267 1.00 23.09  ? 125  PRO   A CA     1 
ATOM   887  C C      . PRO   A  1 133 ? 18.639 -85.812  -26.719 1.00 26.05  ? 125  PRO   A C      1 
ATOM   888  O O      . PRO   A  1 133 ? 17.643 -86.435  -26.337 1.00 25.90  ? 125  PRO   A O      1 
ATOM   889  C CB     . PRO   A  1 133 ? 20.558 -87.342  -27.149 1.00 25.35  ? 125  PRO   A CB     1 
ATOM   890  C CG     . PRO   A  1 133 ? 20.159 -88.594  -26.403 1.00 29.76  ? 125  PRO   A CG     1 
ATOM   891  C CD     . PRO   A  1 133 ? 20.014 -88.246  -24.933 1.00 25.31  ? 125  PRO   A CD     1 
ATOM   892  N N      . LEU   A  1 134 ? 18.587 -84.788  -27.573 1.00 21.47  ? 126  LEU   A N      1 
ATOM   893  C CA     . LEU   A  1 134 ? 17.397 -84.400  -28.328 1.00 21.90  ? 126  LEU   A CA     1 
ATOM   894  C C      . LEU   A  1 134 ? 17.858 -84.619  -29.771 1.00 23.21  ? 126  LEU   A C      1 
ATOM   895  O O      . LEU   A  1 134 ? 18.606 -83.807  -30.317 1.00 22.21  ? 126  LEU   A O      1 
ATOM   896  C CB     . LEU   A  1 134 ? 16.952 -82.943  -28.091 1.00 22.00  ? 126  LEU   A CB     1 
ATOM   897  C CG     . LEU   A  1 134 ? 16.429 -82.573  -26.712 1.00 26.40  ? 126  LEU   A CG     1 
ATOM   898  C CD1    . LEU   A  1 134 ? 16.101 -81.094  -26.656 1.00 26.30  ? 126  LEU   A CD1    1 
ATOM   899  C CD2    . LEU   A  1 134 ? 15.188 -83.382  -26.331 1.00 27.77  ? 126  LEU   A CD2    1 
ATOM   900  N N      . ASN   A  1 135 ? 17.544 -85.786  -30.324 1.00 20.02  ? 127  ASN   A N      1 
ATOM   901  C CA     . ASN   A  1 135 ? 18.009 -86.168  -31.666 1.00 20.11  ? 127  ASN   A CA     1 
ATOM   902  C C      . ASN   A  1 135 ? 16.868 -86.444  -32.634 1.00 25.38  ? 127  ASN   A C      1 
ATOM   903  O O      . ASN   A  1 135 ? 17.097 -86.942  -33.739 1.00 26.10  ? 127  ASN   A O      1 
ATOM   904  C CB     . ASN   A  1 135 ? 18.981 -87.362  -31.571 1.00 20.15  ? 127  ASN   A CB     1 
ATOM   905  C CG     . ASN   A  1 135 ? 18.428 -88.575  -30.871 1.00 34.84  ? 127  ASN   A CG     1 
ATOM   906  O OD1    . ASN   A  1 135 ? 17.228 -88.869  -30.905 1.00 28.98  ? 127  ASN   A OD1    1 
ATOM   907  N ND2    . ASN   A  1 135 ? 19.304 -89.345  -30.266 1.00 25.10  ? 127  ASN   A ND2    1 
ATOM   908  N N      . GLN   A  1 136 ? 15.634 -86.125  -32.219 1.00 21.23  ? 128  GLN   A N      1 
ATOM   909  C CA     . GLN   A  1 136 ? 14.444 -86.297  -33.049 1.00 20.48  ? 128  GLN   A CA     1 
ATOM   910  C C      . GLN   A  1 136 ? 13.393 -85.288  -32.638 1.00 24.00  ? 128  GLN   A C      1 
ATOM   911  O O      . GLN   A  1 136 ? 13.549 -84.631  -31.615 1.00 22.44  ? 128  GLN   A O      1 
ATOM   912  C CB     . GLN   A  1 136 ? 13.913 -87.746  -33.005 1.00 21.15  ? 128  GLN   A CB     1 
ATOM   913  C CG     . GLN   A  1 136 ? 13.570 -88.261  -31.595 1.00 25.91  ? 128  GLN   A CG     1 
ATOM   914  C CD     . GLN   A  1 136 ? 12.973 -89.643  -31.651 1.00 43.30  ? 128  GLN   A CD     1 
ATOM   915  O OE1    . GLN   A  1 136 ? 13.494 -90.543  -32.317 1.00 39.25  ? 128  GLN   A OE1    1 
ATOM   916  N NE2    . GLN   A  1 136 ? 11.873 -89.856  -30.935 1.00 31.03  ? 128  GLN   A NE2    1 
ATOM   917  N N      . GLU   A  1 137 ? 12.340 -85.151  -33.442 1.00 22.91  ? 129  GLU   A N      1 
ATOM   918  C CA     . GLU   A  1 137 ? 11.272 -84.191  -33.184 1.00 23.32  ? 129  GLU   A CA     1 
ATOM   919  C C      . GLU   A  1 137 ? 10.403 -84.553  -31.978 1.00 26.65  ? 129  GLU   A C      1 
ATOM   920  O O      . GLU   A  1 137 ? 10.073 -83.661  -31.214 1.00 26.65  ? 129  GLU   A O      1 
ATOM   921  C CB     . GLU   A  1 137 ? 10.412 -83.973  -34.437 1.00 24.53  ? 129  GLU   A CB     1 
ATOM   922  C CG     . GLU   A  1 137 ? 9.458  -82.791  -34.323 1.00 35.74  ? 129  GLU   A CG     1 
ATOM   923  C CD     . GLU   A  1 137 ? 8.441  -82.680  -35.443 1.00 60.20  ? 129  GLU   A CD     1 
ATOM   924  O OE1    . GLU   A  1 137 ? 8.836  -82.784  -36.629 1.00 53.69  ? 129  GLU   A OE1    1 
ATOM   925  O OE2    . GLU   A  1 137 ? 7.245  -82.475  -35.134 1.00 52.96  ? 129  GLU   A OE2    1 
ATOM   926  N N      . ASP   A  1 138 ? 10.018 -85.826  -31.822 1.00 21.75  ? 130  ASP   A N      1 
ATOM   927  C CA     . ASP   A  1 138 ? 9.165  -86.256  -30.718 1.00 20.73  ? 130  ASP   A CA     1 
ATOM   928  C C      . ASP   A  1 138 ? 9.945  -86.804  -29.515 1.00 23.57  ? 130  ASP   A C      1 
ATOM   929  O O      . ASP   A  1 138 ? 10.437 -87.930  -29.540 1.00 21.71  ? 130  ASP   A O      1 
ATOM   930  C CB     . ASP   A  1 138 ? 8.079  -87.249  -31.187 1.00 22.02  ? 130  ASP   A CB     1 
ATOM   931  C CG     . ASP   A  1 138 ? 7.039  -87.581  -30.116 1.00 29.21  ? 130  ASP   A CG     1 
ATOM   932  O OD1    . ASP   A  1 138 ? 7.037  -86.910  -29.049 1.00 26.30  ? 130  ASP   A OD1    1 
ATOM   933  O OD2    . ASP   A  1 138 ? 6.217  -88.488  -30.351 1.00 35.51  ? 130  ASP   A OD2    1 
ATOM   934  N N      . ASN   A  1 139 ? 10.010 -85.999  -28.444 1.00 20.67  ? 131  ASN   A N      1 
ATOM   935  C CA     . ASN   A  1 139 ? 10.666 -86.344  -27.189 1.00 20.78  ? 131  ASN   A CA     1 
ATOM   936  C C      . ASN   A  1 139 ? 9.686  -86.201  -26.011 1.00 22.77  ? 131  ASN   A C      1 
ATOM   937  O O      . ASN   A  1 139 ? 10.114 -85.933  -24.891 1.00 21.34  ? 131  ASN   A O      1 
ATOM   938  C CB     . ASN   A  1 139 ? 11.928 -85.489  -26.985 1.00 21.17  ? 131  ASN   A CB     1 
ATOM   939  C CG     . ASN   A  1 139 ? 12.910 -85.578  -28.121 1.00 28.86  ? 131  ASN   A CG     1 
ATOM   940  O OD1    . ASN   A  1 139 ? 13.100 -84.630  -28.882 1.00 23.80  ? 131  ASN   A OD1    1 
ATOM   941  N ND2    . ASN   A  1 139 ? 13.561 -86.708  -28.243 1.00 20.66  ? 131  ASN   A ND2    1 
ATOM   942  N N      . THR   A  1 140 ? 8.372  -86.370  -26.276 1.00 19.67  ? 132  THR   A N      1 
ATOM   943  C CA     . THR   A  1 140 ? 7.307  -86.224  -25.274 1.00 20.04  ? 132  THR   A CA     1 
ATOM   944  C C      . THR   A  1 140 ? 7.490  -87.156  -24.085 1.00 22.69  ? 132  THR   A C      1 
ATOM   945  O O      . THR   A  1 140 ? 7.504  -86.681  -22.953 1.00 21.78  ? 132  THR   A O      1 
ATOM   946  C CB     . THR   A  1 140 ? 5.889  -86.356  -25.889 1.00 25.75  ? 132  THR   A CB     1 
ATOM   947  O OG1    . THR   A  1 140 ? 5.816  -85.560  -27.058 1.00 28.17  ? 132  THR   A OG1    1 
ATOM   948  C CG2    . THR   A  1 140 ? 4.804  -85.874  -24.938 1.00 24.59  ? 132  THR   A CG2    1 
ATOM   949  N N      . ASN   A  1 141 ? 7.627  -88.469  -24.335 1.00 18.21  ? 133  ASN   A N      1 
ATOM   950  C CA     . ASN   A  1 141 ? 7.804  -89.433  -23.257 1.00 18.16  ? 133  ASN   A CA     1 
ATOM   951  C C      . ASN   A  1 141 ? 9.137  -89.238  -22.518 1.00 23.60  ? 133  ASN   A C      1 
ATOM   952  O O      . ASN   A  1 141 ? 9.170  -89.407  -21.302 1.00 24.57  ? 133  ASN   A O      1 
ATOM   953  C CB     . ASN   A  1 141 ? 7.601  -90.864  -23.741 1.00 20.60  ? 133  ASN   A CB     1 
ATOM   954  C CG     . ASN   A  1 141 ? 7.126  -91.799  -22.665 1.00 38.52  ? 133  ASN   A CG     1 
ATOM   955  O OD1    . ASN   A  1 141 ? 6.252  -91.467  -21.860 1.00 29.69  ? 133  ASN   A OD1    1 
ATOM   956  N ND2    . ASN   A  1 141 ? 7.674  -93.007  -22.645 1.00 31.32  ? 133  ASN   A ND2    1 
ATOM   957  N N      . LEU   A  1 142 ? 10.200 -88.799  -23.220 1.00 19.91  ? 134  LEU   A N      1 
ATOM   958  C CA     . LEU   A  1 142 ? 11.495 -88.486  -22.599 1.00 19.77  ? 134  LEU   A CA     1 
ATOM   959  C C      . LEU   A  1 142 ? 11.317 -87.299  -21.611 1.00 21.84  ? 134  LEU   A C      1 
ATOM   960  O O      . LEU   A  1 142 ? 11.840 -87.353  -20.496 1.00 20.67  ? 134  LEU   A O      1 
ATOM   961  C CB     . LEU   A  1 142 ? 12.529 -88.132  -23.679 1.00 19.98  ? 134  LEU   A CB     1 
ATOM   962  C CG     . LEU   A  1 142 ? 13.926 -87.709  -23.200 1.00 25.98  ? 134  LEU   A CG     1 
ATOM   963  C CD1    . LEU   A  1 142 ? 14.828 -88.917  -23.029 1.00 26.92  ? 134  LEU   A CD1    1 
ATOM   964  C CD2    . LEU   A  1 142 ? 14.582 -86.796  -24.230 1.00 29.92  ? 134  LEU   A CD2    1 
ATOM   965  N N      . ALA   A  1 143 ? 10.554 -86.249  -22.025 1.00 17.48  ? 135  ALA   A N      1 
ATOM   966  C CA     . ALA   A  1 143 ? 10.247 -85.080  -21.198 1.00 17.02  ? 135  ALA   A CA     1 
ATOM   967  C C      . ALA   A  1 143 ? 9.443  -85.505  -19.976 1.00 21.76  ? 135  ALA   A C      1 
ATOM   968  O O      . ALA   A  1 143 ? 9.724  -85.053  -18.866 1.00 22.24  ? 135  ALA   A O      1 
ATOM   969  C CB     . ALA   A  1 143 ? 9.464  -84.054  -22.010 1.00 17.41  ? 135  ALA   A CB     1 
ATOM   970  N N      . ARG   A  1 144 ? 8.478  -86.416  -20.174 1.00 17.84  ? 136  ARG   A N      1 
ATOM   971  C CA     . ARG   A  1 144 ? 7.635  -86.902  -19.102 1.00 17.74  ? 136  ARG   A CA     1 
ATOM   972  C C      . ARG   A  1 144 ? 8.408  -87.673  -18.041 1.00 21.79  ? 136  ARG   A C      1 
ATOM   973  O O      . ARG   A  1 144 ? 8.217  -87.421  -16.854 1.00 22.24  ? 136  ARG   A O      1 
ATOM   974  C CB     . ARG   A  1 144 ? 6.463  -87.712  -19.645 1.00 15.84  ? 136  ARG   A CB     1 
ATOM   975  C CG     . ARG   A  1 144 ? 5.435  -87.917  -18.549 1.00 20.76  ? 136  ARG   A CG     1 
ATOM   976  C CD     . ARG   A  1 144 ? 4.501  -89.050  -18.807 1.00 29.89  ? 136  ARG   A CD     1 
ATOM   977  N NE     . ARG   A  1 144 ? 5.172  -90.261  -19.274 1.00 39.46  ? 136  ARG   A NE     1 
ATOM   978  C CZ     . ARG   A  1 144 ? 5.413  -91.326  -18.522 1.00 47.64  ? 136  ARG   A CZ     1 
ATOM   979  N NH1    . ARG   A  1 144 ? 5.085  -91.326  -17.236 1.00 40.21  ? 136  ARG   A NH1    1 
ATOM   980  N NH2    . ARG   A  1 144 ? 5.993  -92.396  -19.046 1.00 29.64  ? 136  ARG   A NH2    1 
ATOM   981  N N      . VAL   A  1 145 ? 9.312  -88.558  -18.468 1.00 16.78  ? 137  VAL   A N      1 
ATOM   982  C CA     . VAL   A  1 145 ? 10.159 -89.337  -17.565 1.00 16.16  ? 137  VAL   A CA     1 
ATOM   983  C C      . VAL   A  1 145 ? 11.148 -88.429  -16.830 1.00 19.05  ? 137  VAL   A C      1 
ATOM   984  O O      . VAL   A  1 145 ? 11.339 -88.603  -15.628 1.00 19.84  ? 137  VAL   A O      1 
ATOM   985  C CB     . VAL   A  1 145 ? 10.832 -90.526  -18.297 1.00 19.90  ? 137  VAL   A CB     1 
ATOM   986  C CG1    . VAL   A  1 145 ? 11.744 -91.322  -17.355 1.00 19.92  ? 137  VAL   A CG1    1 
ATOM   987  C CG2    . VAL   A  1 145 ? 9.763  -91.444  -18.887 1.00 19.54  ? 137  VAL   A CG2    1 
ATOM   988  N N      . LEU   A  1 146 ? 11.752 -87.458  -17.530 1.00 15.43  ? 138  LEU   A N      1 
ATOM   989  C CA     . LEU   A  1 146 ? 12.677 -86.534  -16.864 1.00 14.97  ? 138  LEU   A CA     1 
ATOM   990  C C      . LEU   A  1 146 ? 11.948 -85.661  -15.843 1.00 21.22  ? 138  LEU   A C      1 
ATOM   991  O O      . LEU   A  1 146 ? 12.465 -85.467  -14.739 1.00 21.89  ? 138  LEU   A O      1 
ATOM   992  C CB     . LEU   A  1 146 ? 13.474 -85.674  -17.869 1.00 13.52  ? 138  LEU   A CB     1 
ATOM   993  C CG     . LEU   A  1 146 ? 14.568 -84.768  -17.256 1.00 16.70  ? 138  LEU   A CG     1 
ATOM   994  C CD1    . LEU   A  1 146 ? 15.665 -85.605  -16.519 1.00 17.00  ? 138  LEU   A CD1    1 
ATOM   995  C CD2    . LEU   A  1 146 ? 15.168 -83.841  -18.306 1.00 16.52  ? 138  LEU   A CD2    1 
ATOM   996  N N      . THR   A  1 147 ? 10.729 -85.184  -16.184 1.00 19.56  ? 139  THR   A N      1 
ATOM   997  C CA     . THR   A  1 147 ? 9.899  -84.356  -15.280 1.00 19.67  ? 139  THR   A CA     1 
ATOM   998  C C      . THR   A  1 147 ? 9.541  -85.147  -14.034 1.00 23.85  ? 139  THR   A C      1 
ATOM   999  O O      . THR   A  1 147 ? 9.574  -84.594  -12.927 1.00 24.57  ? 139  THR   A O      1 
ATOM   1000 C CB     . THR   A  1 147 ? 8.668  -83.774  -16.017 1.00 24.24  ? 139  THR   A CB     1 
ATOM   1001 O OG1    . THR   A  1 147 ? 9.146  -82.967  -17.082 1.00 27.56  ? 139  THR   A OG1    1 
ATOM   1002 C CG2    . THR   A  1 147 ? 7.788  -82.890  -15.124 1.00 22.62  ? 139  THR   A CG2    1 
ATOM   1003 N N      . ASN   A  1 148 ? 9.233  -86.442  -14.207 1.00 20.03  ? 140  ASN   A N      1 
ATOM   1004 C CA     . ASN   A  1 148 ? 8.890  -87.329  -13.100 1.00 20.25  ? 140  ASN   A CA     1 
ATOM   1005 C C      . ASN   A  1 148 ? 10.076 -87.488  -12.152 1.00 25.62  ? 140  ASN   A C      1 
ATOM   1006 O O      . ASN   A  1 148 ? 9.897  -87.321  -10.954 1.00 25.41  ? 140  ASN   A O      1 
ATOM   1007 C CB     . ASN   A  1 148 ? 8.324  -88.672  -13.588 1.00 17.51  ? 140  ASN   A CB     1 
ATOM   1008 C CG     . ASN   A  1 148 ? 6.970  -88.563  -14.302 1.00 45.30  ? 140  ASN   A CG     1 
ATOM   1009 O OD1    . ASN   A  1 148 ? 6.191  -87.609  -14.135 1.00 32.08  ? 140  ASN   A OD1    1 
ATOM   1010 N ND2    . ASN   A  1 148 ? 6.678  -89.521  -15.166 1.00 42.02  ? 140  ASN   A ND2    1 
ATOM   1011 N N      . HIS   A  1 149 ? 11.297 -87.669  -12.707 1.00 22.48  ? 141  HIS   A N      1 
ATOM   1012 C CA     . HIS   A  1 149 ? 12.544 -87.770  -11.948 1.00 21.77  ? 141  HIS   A CA     1 
ATOM   1013 C C      . HIS   A  1 149 ? 12.865 -86.478  -11.171 1.00 26.65  ? 141  HIS   A C      1 
ATOM   1014 O O      . HIS   A  1 149 ? 13.269 -86.553  -10.011 1.00 26.85  ? 141  HIS   A O      1 
ATOM   1015 C CB     . HIS   A  1 149 ? 13.703 -88.151  -12.881 1.00 21.44  ? 141  HIS   A CB     1 
ATOM   1016 C CG     . HIS   A  1 149 ? 15.044 -88.108  -12.219 1.00 23.56  ? 141  HIS   A CG     1 
ATOM   1017 N ND1    . HIS   A  1 149 ? 15.420 -89.065  -11.288 1.00 24.95  ? 141  HIS   A ND1    1 
ATOM   1018 C CD2    . HIS   A  1 149 ? 16.051 -87.222  -12.370 1.00 23.89  ? 141  HIS   A CD2    1 
ATOM   1019 C CE1    . HIS   A  1 149 ? 16.644 -88.736  -10.913 1.00 23.76  ? 141  HIS   A CE1    1 
ATOM   1020 N NE2    . HIS   A  1 149 ? 17.069 -87.641  -11.547 1.00 24.06  ? 141  HIS   A NE2    1 
ATOM   1021 N N      . ILE   A  1 150 ? 12.661 -85.309  -11.797 1.00 24.78  ? 142  ILE   A N      1 
ATOM   1022 C CA     . ILE   A  1 150 ? 12.900 -84.000  -11.178 1.00 25.26  ? 142  ILE   A CA     1 
ATOM   1023 C C      . ILE   A  1 150 ? 11.988 -83.799  -9.952  1.00 32.16  ? 142  ILE   A C      1 
ATOM   1024 O O      . ILE   A  1 150 ? 12.430 -83.237  -8.950  1.00 31.15  ? 142  ILE   A O      1 
ATOM   1025 C CB     . ILE   A  1 150 ? 12.816 -82.851  -12.231 1.00 27.47  ? 142  ILE   A CB     1 
ATOM   1026 C CG1    . ILE   A  1 150 ? 14.076 -82.852  -13.119 1.00 26.43  ? 142  ILE   A CG1    1 
ATOM   1027 C CG2    . ILE   A  1 150 ? 12.593 -81.457  -11.583 1.00 28.46  ? 142  ILE   A CG2    1 
ATOM   1028 C CD1    . ILE   A  1 150 ? 14.043 -81.926  -14.359 1.00 21.67  ? 142  ILE   A CD1    1 
ATOM   1029 N N      . HIS   A  1 151 ? 10.757 -84.329  -10.012 1.00 32.34  ? 143  HIS   A N      1 
ATOM   1030 C CA     . HIS   A  1 151 ? 9.775  -84.207  -8.939  1.00 34.30  ? 143  HIS   A CA     1 
ATOM   1031 C C      . HIS   A  1 151 ? 9.729  -85.417  -7.986  1.00 41.30  ? 143  HIS   A C      1 
ATOM   1032 O O      . HIS   A  1 151 ? 8.748  -85.588  -7.263  1.00 41.45  ? 143  HIS   A O      1 
ATOM   1033 C CB     . HIS   A  1 151 ? 8.397  -83.900  -9.537  1.00 35.55  ? 143  HIS   A CB     1 
ATOM   1034 C CG     . HIS   A  1 151 ? 8.345  -82.546  -10.156 1.00 39.63  ? 143  HIS   A CG     1 
ATOM   1035 N ND1    . HIS   A  1 151 ? 8.342  -82.383  -11.527 1.00 41.75  ? 143  HIS   A ND1    1 
ATOM   1036 C CD2    . HIS   A  1 151 ? 8.380  -81.326  -9.568  1.00 42.13  ? 143  HIS   A CD2    1 
ATOM   1037 C CE1    . HIS   A  1 151 ? 8.337  -81.075  -11.731 1.00 41.52  ? 143  HIS   A CE1    1 
ATOM   1038 N NE2    . HIS   A  1 151 ? 8.368  -80.399  -10.581 1.00 41.90  ? 143  HIS   A NE2    1 
ATOM   1039 N N      . THR   A  1 152 ? 10.797 -86.226  -7.957  1.00 39.97  ? 144  THR   A N      1 
ATOM   1040 C CA     . THR   A  1 152 ? 10.894 -87.410  -7.104  1.00 41.09  ? 144  THR   A CA     1 
ATOM   1041 C C      . THR   A  1 152 ? 12.195 -87.372  -6.313  1.00 50.10  ? 144  THR   A C      1 
ATOM   1042 O O      . THR   A  1 152 ? 13.266 -87.213  -6.894  1.00 50.01  ? 144  THR   A O      1 
ATOM   1043 C CB     . THR   A  1 152 ? 10.755 -88.692  -7.949  1.00 47.51  ? 144  THR   A CB     1 
ATOM   1044 O OG1    . THR   A  1 152 ? 9.502  -88.666  -8.630  1.00 49.70  ? 144  THR   A OG1    1 
ATOM   1045 C CG2    . THR   A  1 152 ? 10.854 -89.978  -7.116  1.00 45.37  ? 144  THR   A CG2    1 
ATOM   1046 N N      . GLY   A  1 153 ? 12.089 -87.540  -5.001  1.00 50.30  ? 145  GLY   A N      1 
ATOM   1047 C CA     . GLY   A  1 153 ? 13.245 -87.548  -4.114  1.00 51.61  ? 145  GLY   A CA     1 
ATOM   1048 C C      . GLY   A  1 153 ? 13.897 -86.191  -3.950  1.00 58.88  ? 145  GLY   A C      1 
ATOM   1049 O O      . GLY   A  1 153 ? 13.320 -85.160  -4.323  1.00 58.68  ? 145  GLY   A O      1 
ATOM   1050 N N      . HIS   A  1 154 ? 15.110 -86.186  -3.383  1.00 57.60  ? 146  HIS   A N      1 
ATOM   1051 C CA     . HIS   A  1 154 ? 15.837 -84.950  -3.121  1.00 58.31  ? 146  HIS   A CA     1 
ATOM   1052 C C      . HIS   A  1 154 ? 17.254 -84.981  -3.696  1.00 60.91  ? 146  HIS   A C      1 
ATOM   1053 O O      . HIS   A  1 154 ? 18.144 -85.649  -3.162  1.00 60.36  ? 146  HIS   A O      1 
ATOM   1054 C CB     . HIS   A  1 154 ? 15.795 -84.607  -1.617  1.00 59.86  ? 146  HIS   A CB     1 
ATOM   1055 C CG     . HIS   A  1 154 ? 14.392 -84.464  -1.096  1.00 63.89  ? 146  HIS   A CG     1 
ATOM   1056 N ND1    . HIS   A  1 154 ? 13.754 -85.509  -0.437  1.00 65.97  ? 146  HIS   A ND1    1 
ATOM   1057 C CD2    . HIS   A  1 154 ? 13.519 -83.438  -1.233  1.00 65.92  ? 146  HIS   A CD2    1 
ATOM   1058 C CE1    . HIS   A  1 154 ? 12.535 -85.070  -0.165  1.00 65.54  ? 146  HIS   A CE1    1 
ATOM   1059 N NE2    . HIS   A  1 154 ? 12.345 -83.830  -0.626  1.00 65.86  ? 146  HIS   A NE2    1 
ATOM   1060 N N      . HIS   A  1 155 ? 17.426 -84.275  -4.833  1.00 56.22  ? 147  HIS   A N      1 
ATOM   1061 C CA     . HIS   A  1 155 ? 18.667 -84.118  -5.602  1.00 55.29  ? 147  HIS   A CA     1 
ATOM   1062 C C      . HIS   A  1 155 ? 18.629 -82.801  -6.379  1.00 57.21  ? 147  HIS   A C      1 
ATOM   1063 O O      . HIS   A  1 155 ? 17.542 -82.261  -6.600  1.00 56.54  ? 147  HIS   A O      1 
ATOM   1064 C CB     . HIS   A  1 155 ? 18.924 -85.317  -6.539  1.00 56.10  ? 147  HIS   A CB     1 
ATOM   1065 C CG     . HIS   A  1 155 ? 17.727 -85.779  -7.316  1.00 59.42  ? 147  HIS   A CG     1 
ATOM   1066 N ND1    . HIS   A  1 155 ? 17.114 -86.984  -7.038  1.00 61.09  ? 147  HIS   A ND1    1 
ATOM   1067 C CD2    . HIS   A  1 155 ? 17.075 -85.184  -8.344  1.00 61.05  ? 147  HIS   A CD2    1 
ATOM   1068 C CE1    . HIS   A  1 155 ? 16.120 -87.087  -7.905  1.00 60.50  ? 147  HIS   A CE1    1 
ATOM   1069 N NE2    . HIS   A  1 155 ? 16.047 -86.020  -8.700  1.00 60.73  ? 147  HIS   A NE2    1 
ATOM   1070 N N      . SER   A  1 156 ? 19.808 -82.259  -6.748  1.00 52.59  ? 148  SER   A N      1 
ATOM   1071 C CA     . SER   A  1 156 ? 19.893 -80.973  -7.448  1.00 51.35  ? 148  SER   A CA     1 
ATOM   1072 C C      . SER   A  1 156 ? 20.896 -80.977  -8.638  1.00 50.17  ? 148  SER   A C      1 
ATOM   1073 O O      . SER   A  1 156 ? 21.590 -79.986  -8.885  1.00 49.63  ? 148  SER   A O      1 
ATOM   1074 C CB     . SER   A  1 156 ? 20.186 -79.851  -6.453  1.00 56.12  ? 148  SER   A CB     1 
ATOM   1075 O OG     . SER   A  1 156 ? 20.113 -78.573  -7.065  1.00 67.99  ? 148  SER   A OG     1 
ATOM   1076 N N      . SER   A  1 157 ? 20.930 -82.087  -9.389  1.00 42.49  ? 149  SER   A N      1 
ATOM   1077 C CA     . SER   A  1 157 ? 21.784 -82.252  -10.561 1.00 40.03  ? 149  SER   A CA     1 
ATOM   1078 C C      . SER   A  1 157 ? 21.217 -81.506  -11.785 1.00 37.62  ? 149  SER   A C      1 
ATOM   1079 O O      . SER   A  1 157 ? 20.009 -81.323  -11.913 1.00 37.19  ? 149  SER   A O      1 
ATOM   1080 C CB     . SER   A  1 157 ? 21.974 -83.730  -10.874 1.00 43.24  ? 149  SER   A CB     1 
ATOM   1081 O OG     . SER   A  1 157 ? 22.802 -83.974  -12.001 1.00 51.84  ? 149  SER   A OG     1 
ATOM   1082 N N      . MET   A  1 158 ? 22.108 -81.060  -12.659 1.00 29.35  ? 150  MET   A N      1 
ATOM   1083 C CA     . MET   A  1 158 ? 21.744 -80.358  -13.878 1.00 26.77  ? 150  MET   A CA     1 
ATOM   1084 C C      . MET   A  1 158 ? 21.546 -81.345  -15.021 1.00 23.99  ? 150  MET   A C      1 
ATOM   1085 O O      . MET   A  1 158 ? 22.271 -82.330  -15.128 1.00 22.67  ? 150  MET   A O      1 
ATOM   1086 C CB     . MET   A  1 158 ? 22.826 -79.338  -14.257 1.00 28.97  ? 150  MET   A CB     1 
ATOM   1087 C CG     . MET   A  1 158 ? 22.779 -78.066  -13.437 1.00 33.16  ? 150  MET   A CG     1 
ATOM   1088 S SD     . MET   A  1 158 ? 21.243 -77.116  -13.609 1.00 37.12  ? 150  MET   A SD     1 
ATOM   1089 C CE     . MET   A  1 158 ? 21.315 -76.668  -15.353 1.00 33.65  ? 150  MET   A CE     1 
ATOM   1090 N N      . PHE   A  1 159 ? 20.561 -81.085  -15.859 1.00 18.29  ? 151  PHE   A N      1 
ATOM   1091 C CA     . PHE   A  1 159 ? 20.304 -81.881  -17.048 1.00 17.68  ? 151  PHE   A CA     1 
ATOM   1092 C C      . PHE   A  1 159 ? 20.680 -81.078  -18.280 1.00 24.18  ? 151  PHE   A C      1 
ATOM   1093 O O      . PHE   A  1 159 ? 20.133 -79.998  -18.518 1.00 23.81  ? 151  PHE   A O      1 
ATOM   1094 C CB     . PHE   A  1 159 ? 18.868 -82.414  -17.077 1.00 18.61  ? 151  PHE   A CB     1 
ATOM   1095 C CG     . PHE   A  1 159 ? 18.588 -83.202  -15.823 1.00 19.35  ? 151  PHE   A CG     1 
ATOM   1096 C CD1    . PHE   A  1 159 ? 19.158 -84.459  -15.629 1.00 21.89  ? 151  PHE   A CD1    1 
ATOM   1097 C CD2    . PHE   A  1 159 ? 17.830 -82.654  -14.793 1.00 20.59  ? 151  PHE   A CD2    1 
ATOM   1098 C CE1    . PHE   A  1 159 ? 18.962 -85.153  -14.432 1.00 22.71  ? 151  PHE   A CE1    1 
ATOM   1099 C CE2    . PHE   A  1 159 ? 17.621 -83.357  -13.606 1.00 23.13  ? 151  PHE   A CE2    1 
ATOM   1100 C CZ     . PHE   A  1 159 ? 18.197 -84.597  -13.427 1.00 21.27  ? 151  PHE   A CZ     1 
ATOM   1101 N N      . TRP   A  1 160 ? 21.688 -81.569  -19.015 1.00 21.40  ? 152  TRP   A N      1 
ATOM   1102 C CA     . TRP   A  1 160 ? 22.186 -80.924  -20.225 1.00 21.21  ? 152  TRP   A CA     1 
ATOM   1103 C C      . TRP   A  1 160 ? 21.612 -81.642  -21.442 1.00 24.28  ? 152  TRP   A C      1 
ATOM   1104 O O      . TRP   A  1 160 ? 21.957 -82.798  -21.698 1.00 23.44  ? 152  TRP   A O      1 
ATOM   1105 C CB     . TRP   A  1 160 ? 23.721 -80.979  -20.264 1.00 20.16  ? 152  TRP   A CB     1 
ATOM   1106 C CG     . TRP   A  1 160 ? 24.448 -80.130  -19.254 1.00 21.43  ? 152  TRP   A CG     1 
ATOM   1107 C CD1    . TRP   A  1 160 ? 23.915 -79.210  -18.395 1.00 24.08  ? 152  TRP   A CD1    1 
ATOM   1108 C CD2    . TRP   A  1 160 ? 25.863 -80.115  -19.031 1.00 21.59  ? 152  TRP   A CD2    1 
ATOM   1109 N NE1    . TRP   A  1 160 ? 24.914 -78.608  -17.667 1.00 23.40  ? 152  TRP   A NE1    1 
ATOM   1110 C CE2    . TRP   A  1 160 ? 26.125 -79.123  -18.059 1.00 25.43  ? 152  TRP   A CE2    1 
ATOM   1111 C CE3    . TRP   A  1 160 ? 26.944 -80.831  -19.580 1.00 23.32  ? 152  TRP   A CE3    1 
ATOM   1112 C CZ2    . TRP   A  1 160 ? 27.425 -78.854  -17.593 1.00 25.09  ? 152  TRP   A CZ2    1 
ATOM   1113 C CZ3    . TRP   A  1 160 ? 28.233 -80.538  -19.144 1.00 25.19  ? 152  TRP   A CZ3    1 
ATOM   1114 C CH2    . TRP   A  1 160 ? 28.463 -79.569  -18.158 1.00 25.71  ? 152  TRP   A CH2    1 
ATOM   1115 N N      . MET   A  1 161 ? 20.724 -80.969  -22.179 1.00 20.11  ? 153  MET   A N      1 
ATOM   1116 C CA     . MET   A  1 161 ? 20.110 -81.541  -23.382 1.00 18.57  ? 153  MET   A CA     1 
ATOM   1117 C C      . MET   A  1 161 ? 21.029 -81.323  -24.583 1.00 21.86  ? 153  MET   A C      1 
ATOM   1118 O O      . MET   A  1 161 ? 21.255 -80.181  -24.989 1.00 20.13  ? 153  MET   A O      1 
ATOM   1119 C CB     . MET   A  1 161 ? 18.708 -80.944  -23.659 1.00 20.01  ? 153  MET   A CB     1 
ATOM   1120 C CG     . MET   A  1 161 ? 17.732 -81.055  -22.485 1.00 22.24  ? 153  MET   A CG     1 
ATOM   1121 S SD     . MET   A  1 161 ? 17.621 -82.659  -21.640 1.00 24.34  ? 153  MET   A SD     1 
ATOM   1122 C CE     . MET   A  1 161 ? 16.978 -83.692  -22.974 1.00 20.93  ? 153  MET   A CE     1 
ATOM   1123 N N      . ARG   A  1 162 ? 21.609 -82.423  -25.094 1.00 19.67  ? 154  ARG   A N      1 
ATOM   1124 C CA     . ARG   A  1 162 ? 22.504 -82.448  -26.244 1.00 19.81  ? 154  ARG   A CA     1 
ATOM   1125 C C      . ARG   A  1 162 ? 21.662 -82.227  -27.490 1.00 23.21  ? 154  ARG   A C      1 
ATOM   1126 O O      . ARG   A  1 162 ? 20.851 -83.083  -27.870 1.00 23.84  ? 154  ARG   A O      1 
ATOM   1127 C CB     . ARG   A  1 162 ? 23.247 -83.788  -26.317 1.00 21.80  ? 154  ARG   A CB     1 
ATOM   1128 C CG     . ARG   A  1 162 ? 24.335 -83.831  -27.366 1.00 26.98  ? 154  ARG   A CG     1 
ATOM   1129 C CD     . ARG   A  1 162 ? 25.269 -84.979  -27.068 1.00 29.85  ? 154  ARG   A CD     1 
ATOM   1130 N NE     . ARG   A  1 162 ? 26.319 -85.073  -28.074 1.00 34.32  ? 154  ARG   A NE     1 
ATOM   1131 C CZ     . ARG   A  1 162 ? 27.529 -85.573  -27.861 1.00 48.34  ? 154  ARG   A CZ     1 
ATOM   1132 N NH1    . ARG   A  1 162 ? 27.863 -86.036  -26.662 1.00 37.40  ? 154  ARG   A NH1    1 
ATOM   1133 N NH2    . ARG   A  1 162 ? 28.419 -85.609  -28.843 1.00 36.45  ? 154  ARG   A NH2    1 
ATOM   1134 N N      . VAL   A  1 163 ? 21.826 -81.059  -28.094 1.00 18.64  ? 155  VAL   A N      1 
ATOM   1135 C CA     . VAL   A  1 163 ? 21.048 -80.686  -29.272 1.00 18.67  ? 155  VAL   A CA     1 
ATOM   1136 C C      . VAL   A  1 163 ? 21.960 -80.038  -30.333 1.00 21.78  ? 155  VAL   A C      1 
ATOM   1137 O O      . VAL   A  1 163 ? 22.773 -79.162  -30.014 1.00 20.88  ? 155  VAL   A O      1 
ATOM   1138 C CB     . VAL   A  1 163 ? 19.797 -79.836  -28.868 1.00 22.08  ? 155  VAL   A CB     1 
ATOM   1139 C CG1    . VAL   A  1 163 ? 20.190 -78.558  -28.144 1.00 21.53  ? 155  VAL   A CG1    1 
ATOM   1140 C CG2    . VAL   A  1 163 ? 18.875 -79.546  -30.052 1.00 21.63  ? 155  VAL   A CG2    1 
ATOM   1141 N N      . PRO   A  1 164 ? 21.883 -80.490  -31.598 1.00 19.19  ? 156  PRO   A N      1 
ATOM   1142 C CA     . PRO   A  1 164 ? 22.775 -79.913  -32.614 1.00 19.28  ? 156  PRO   A CA     1 
ATOM   1143 C C      . PRO   A  1 164 ? 22.209 -78.641  -33.236 1.00 24.57  ? 156  PRO   A C      1 
ATOM   1144 O O      . PRO   A  1 164 ? 20.990 -78.523  -33.324 1.00 22.76  ? 156  PRO   A O      1 
ATOM   1145 C CB     . PRO   A  1 164 ? 22.868 -81.037  -33.646 1.00 20.99  ? 156  PRO   A CB     1 
ATOM   1146 C CG     . PRO   A  1 164 ? 21.536 -81.724  -33.579 1.00 24.42  ? 156  PRO   A CG     1 
ATOM   1147 C CD     . PRO   A  1 164 ? 21.040 -81.573  -32.158 1.00 19.74  ? 156  PRO   A CD     1 
ATOM   1148 N N      . LEU   A  1 165 ? 23.076 -77.715  -33.716 1.00 24.27  ? 157  LEU   A N      1 
ATOM   1149 C CA     . LEU   A  1 165 ? 22.631 -76.522  -34.457 1.00 24.87  ? 157  LEU   A CA     1 
ATOM   1150 C C      . LEU   A  1 165 ? 21.916 -76.982  -35.740 1.00 26.53  ? 157  LEU   A C      1 
ATOM   1151 O O      . LEU   A  1 165 ? 20.942 -76.365  -36.160 1.00 25.68  ? 157  LEU   A O      1 
ATOM   1152 C CB     . LEU   A  1 165 ? 23.816 -75.648  -34.901 1.00 25.83  ? 157  LEU   A CB     1 
ATOM   1153 C CG     . LEU   A  1 165 ? 24.375 -74.600  -33.986 1.00 32.15  ? 157  LEU   A CG     1 
ATOM   1154 C CD1    . LEU   A  1 165 ? 25.569 -73.923  -34.652 1.00 32.39  ? 157  LEU   A CD1    1 
ATOM   1155 C CD2    . LEU   A  1 165 ? 23.323 -73.544  -33.645 1.00 35.72  ? 157  LEU   A CD2    1 
ATOM   1156 N N      . VAL   A  1 166 ? 22.437 -78.051  -36.382 1.00 21.98  ? 158  VAL   A N      1 
ATOM   1157 C CA     . VAL   A  1 166 ? 21.904 -78.650  -37.615 1.00 21.43  ? 158  VAL   A CA     1 
ATOM   1158 C C      . VAL   A  1 166 ? 21.633 -80.134  -37.371 1.00 23.88  ? 158  VAL   A C      1 
ATOM   1159 O O      . VAL   A  1 166 ? 22.524 -80.856  -36.928 1.00 23.50  ? 158  VAL   A O      1 
ATOM   1160 C CB     . VAL   A  1 166 ? 22.840 -78.413  -38.849 1.00 24.81  ? 158  VAL   A CB     1 
ATOM   1161 C CG1    . VAL   A  1 166 ? 22.329 -79.115  -40.107 1.00 24.35  ? 158  VAL   A CG1    1 
ATOM   1162 C CG2    . VAL   A  1 166 ? 23.027 -76.926  -39.116 1.00 24.55  ? 158  VAL   A CG2    1 
ATOM   1163 N N      . ALA   A  1 167 ? 20.416 -80.586  -37.683 1.00 20.97  ? 159  ALA   A N      1 
ATOM   1164 C CA     . ALA   A  1 167 ? 19.985 -81.978  -37.527 1.00 20.75  ? 159  ALA   A CA     1 
ATOM   1165 C C      . ALA   A  1 167 ? 20.804 -82.887  -38.458 1.00 27.65  ? 159  ALA   A C      1 
ATOM   1166 O O      . ALA   A  1 167 ? 21.042 -82.498  -39.602 1.00 27.22  ? 159  ALA   A O      1 
ATOM   1167 C CB     . ALA   A  1 167 ? 18.504 -82.107  -37.866 1.00 21.16  ? 159  ALA   A CB     1 
ATOM   1168 N N      . PRO   A  1 168 ? 21.250 -84.081  -37.989 1.00 26.15  ? 160  PRO   A N      1 
ATOM   1169 C CA     . PRO   A  1 168 ? 22.018 -84.982  -38.873 1.00 26.46  ? 160  PRO   A CA     1 
ATOM   1170 C C      . PRO   A  1 168 ? 21.335 -85.238  -40.226 1.00 28.80  ? 160  PRO   A C      1 
ATOM   1171 O O      . PRO   A  1 168 ? 22.022 -85.230  -41.233 1.00 27.68  ? 160  PRO   A O      1 
ATOM   1172 C CB     . PRO   A  1 168 ? 22.196 -86.260  -38.044 1.00 28.45  ? 160  PRO   A CB     1 
ATOM   1173 C CG     . PRO   A  1 168 ? 21.290 -86.120  -36.874 1.00 33.24  ? 160  PRO   A CG     1 
ATOM   1174 C CD     . PRO   A  1 168 ? 21.063 -84.668  -36.644 1.00 28.38  ? 160  PRO   A CD     1 
ATOM   1175 N N      . GLU   A  1 169 ? 19.988 -85.366  -40.253 1.00 24.50  ? 161  GLU   A N      1 
ATOM   1176 C CA     . GLU   A  1 169 ? 19.195 -85.539  -41.472 1.00 24.63  ? 161  GLU   A CA     1 
ATOM   1177 C C      . GLU   A  1 169 ? 19.410 -84.363  -42.470 1.00 29.98  ? 161  GLU   A C      1 
ATOM   1178 O O      . GLU   A  1 169 ? 19.340 -84.572  -43.682 1.00 29.32  ? 161  GLU   A O      1 
ATOM   1179 C CB     . GLU   A  1 169 ? 17.699 -85.709  -41.119 1.00 25.55  ? 161  GLU   A CB     1 
ATOM   1180 C CG     . GLU   A  1 169 ? 16.755 -85.953  -42.291 1.00 36.18  ? 161  GLU   A CG     1 
ATOM   1181 C CD     . GLU   A  1 169 ? 17.134 -87.074  -43.248 1.00 58.84  ? 161  GLU   A CD     1 
ATOM   1182 O OE1    . GLU   A  1 169 ? 17.275 -88.232  -42.791 1.00 49.99  ? 161  GLU   A OE1    1 
ATOM   1183 O OE2    . GLU   A  1 169 ? 17.273 -86.795  -44.460 1.00 49.35  ? 161  GLU   A OE2    1 
ATOM   1184 N N      . ASP   A  1 170 ? 19.720 -83.158  -41.954 1.00 26.66  ? 162  ASP   A N      1 
ATOM   1185 C CA     . ASP   A  1 170 ? 19.937 -81.967  -42.781 1.00 26.87  ? 162  ASP   A CA     1 
ATOM   1186 C C      . ASP   A  1 170 ? 21.396 -81.732  -43.145 1.00 30.82  ? 162  ASP   A C      1 
ATOM   1187 O O      . ASP   A  1 170 ? 21.672 -80.849  -43.958 1.00 31.27  ? 162  ASP   A O      1 
ATOM   1188 C CB     . ASP   A  1 170 ? 19.315 -80.712  -42.127 1.00 28.97  ? 162  ASP   A CB     1 
ATOM   1189 C CG     . ASP   A  1 170 ? 17.795 -80.749  -42.010 1.00 40.31  ? 162  ASP   A CG     1 
ATOM   1190 O OD1    . ASP   A  1 170 ? 17.135 -81.278  -42.940 1.00 40.90  ? 162  ASP   A OD1    1 
ATOM   1191 O OD2    . ASP   A  1 170 ? 17.263 -80.210  -41.012 1.00 45.38  ? 162  ASP   A OD2    1 
ATOM   1192 N N      . LEU   A  1 171 ? 22.335 -82.490  -42.545 1.00 26.55  ? 163  LEU   A N      1 
ATOM   1193 C CA     . LEU   A  1 171 ? 23.749 -82.345  -42.895 1.00 26.54  ? 163  LEU   A CA     1 
ATOM   1194 C C      . LEU   A  1 171 ? 24.315 -83.627  -43.566 1.00 31.82  ? 163  LEU   A C      1 
ATOM   1195 O O      . LEU   A  1 171 ? 25.526 -83.704  -43.799 1.00 31.69  ? 163  LEU   A O      1 
ATOM   1196 C CB     . LEU   A  1 171 ? 24.646 -81.841  -41.730 1.00 26.50  ? 163  LEU   A CB     1 
ATOM   1197 C CG     . LEU   A  1 171 ? 24.650 -82.562  -40.370 1.00 31.14  ? 163  LEU   A CG     1 
ATOM   1198 C CD1    . LEU   A  1 171 ? 25.321 -83.953  -40.435 1.00 31.06  ? 163  LEU   A CD1    1 
ATOM   1199 C CD2    . LEU   A  1 171 ? 25.403 -81.727  -39.331 1.00 31.66  ? 163  LEU   A CD2    1 
ATOM   1200 N N      . ARG   A  1 172 ? 23.440 -84.617  -43.885 1.00 28.42  ? 164  ARG   A N      1 
ATOM   1201 C CA     . ARG   A  1 172 ? 23.868 -85.850  -44.563 1.00 29.27  ? 164  ARG   A CA     1 
ATOM   1202 C C      . ARG   A  1 172 ? 24.425 -85.540  -45.967 1.00 36.11  ? 164  ARG   A C      1 
ATOM   1203 O O      . ARG   A  1 172 ? 23.950 -84.605  -46.632 1.00 35.90  ? 164  ARG   A O      1 
ATOM   1204 C CB     . ARG   A  1 172 ? 22.734 -86.909  -44.630 1.00 27.65  ? 164  ARG   A CB     1 
ATOM   1205 C CG     . ARG   A  1 172 ? 21.545 -86.516  -45.498 1.00 30.53  ? 164  ARG   A CG     1 
ATOM   1206 C CD     . ARG   A  1 172 ? 20.459 -87.576  -45.525 1.00 34.31  ? 164  ARG   A CD     1 
ATOM   1207 N NE     . ARG   A  1 172 ? 19.318 -87.164  -46.350 1.00 41.82  ? 164  ARG   A NE     1 
ATOM   1208 C CZ     . ARG   A  1 172 ? 19.227 -87.330  -47.670 1.00 54.79  ? 164  ARG   A CZ     1 
ATOM   1209 N NH1    . ARG   A  1 172 ? 20.217 -87.903  -48.347 1.00 34.92  ? 164  ARG   A NH1    1 
ATOM   1210 N NH2    . ARG   A  1 172 ? 18.149 -86.915  -48.325 1.00 43.03  ? 164  ARG   A NH2    1 
ATOM   1211 N N      . ASP   A  1 173 ? 25.452 -86.308  -46.397 1.00 33.59  ? 165  ASP   A N      1 
ATOM   1212 C CA     . ASP   A  1 173 ? 26.060 -86.172  -47.727 1.00 33.28  ? 165  ASP   A CA     1 
ATOM   1213 C C      . ASP   A  1 173 ? 24.984 -86.498  -48.755 1.00 35.34  ? 165  ASP   A C      1 
ATOM   1214 O O      . ASP   A  1 173 ? 24.159 -87.373  -48.503 1.00 33.95  ? 165  ASP   A O      1 
ATOM   1215 C CB     . ASP   A  1 173 ? 27.249 -87.146  -47.905 1.00 35.34  ? 165  ASP   A CB     1 
ATOM   1216 C CG     . ASP   A  1 173 ? 28.460 -86.915  -47.015 1.00 45.98  ? 165  ASP   A CG     1 
ATOM   1217 O OD1    . ASP   A  1 173 ? 28.545 -85.836  -46.393 1.00 47.25  ? 165  ASP   A OD1    1 
ATOM   1218 O OD2    . ASP   A  1 173 ? 29.338 -87.809  -46.963 1.00 52.20  ? 165  ASP   A OD2    1 
ATOM   1219 N N      . ASP   A  1 174 ? 24.960 -85.773  -49.883 1.00 32.41  ? 166  ASP   A N      1 
ATOM   1220 C CA     . ASP   A  1 174 ? 23.985 -85.999  -50.952 1.00 32.36  ? 166  ASP   A CA     1 
ATOM   1221 C C      . ASP   A  1 174 ? 24.471 -87.213  -51.795 1.00 36.97  ? 166  ASP   A C      1 
ATOM   1222 O O      . ASP   A  1 174 ? 24.962 -87.042  -52.920 1.00 35.95  ? 166  ASP   A O      1 
ATOM   1223 C CB     . ASP   A  1 174 ? 23.812 -84.712  -51.798 1.00 33.70  ? 166  ASP   A CB     1 
ATOM   1224 C CG     . ASP   A  1 174 ? 22.744 -84.769  -52.881 1.00 41.14  ? 166  ASP   A CG     1 
ATOM   1225 O OD1    . ASP   A  1 174 ? 21.752 -85.533  -52.710 1.00 39.81  ? 166  ASP   A OD1    1 
ATOM   1226 O OD2    . ASP   A  1 174 ? 22.883 -84.034  -53.890 1.00 46.88  ? 166  ASP   A OD2    1 
ATOM   1227 N N      . ILE   A  1 175 ? 24.364 -88.442  -51.208 1.00 32.73  ? 167  ILE   A N      1 
ATOM   1228 C CA     . ILE   A  1 175 ? 24.835 -89.691  -51.833 1.00 31.50  ? 167  ILE   A CA     1 
ATOM   1229 C C      . ILE   A  1 175 ? 23.722 -90.761  -51.952 1.00 34.51  ? 167  ILE   A C      1 
ATOM   1230 O O      . ILE   A  1 175 ? 24.010 -91.903  -52.312 1.00 34.35  ? 167  ILE   A O      1 
ATOM   1231 C CB     . ILE   A  1 175 ? 26.131 -90.237  -51.151 1.00 34.14  ? 167  ILE   A CB     1 
ATOM   1232 C CG1    . ILE   A  1 175 ? 25.942 -90.458  -49.615 1.00 34.11  ? 167  ILE   A CG1    1 
ATOM   1233 C CG2    . ILE   A  1 175 ? 27.335 -89.335  -51.473 1.00 33.68  ? 167  ILE   A CG2    1 
ATOM   1234 C CD1    . ILE   A  1 175 ? 27.188 -90.877  -48.787 1.00 34.47  ? 167  ILE   A CD1    1 
ATOM   1235 N N      . ILE   A  1 176 ? 22.457 -90.391  -51.695 1.00 30.29  ? 168  ILE   A N      1 
ATOM   1236 C CA     . ILE   A  1 176 ? 21.328 -91.305  -51.889 1.00 29.24  ? 168  ILE   A CA     1 
ATOM   1237 C C      . ILE   A  1 176 ? 20.626 -90.885  -53.200 1.00 35.18  ? 168  ILE   A C      1 
ATOM   1238 O O      . ILE   A  1 176 ? 19.875 -89.908  -53.217 1.00 34.34  ? 168  ILE   A O      1 
ATOM   1239 C CB     . ILE   A  1 176 ? 20.343 -91.453  -50.684 1.00 31.18  ? 168  ILE   A CB     1 
ATOM   1240 C CG1    . ILE   A  1 176 ? 21.084 -91.712  -49.345 1.00 31.16  ? 168  ILE   A CG1    1 
ATOM   1241 C CG2    . ILE   A  1 176 ? 19.314 -92.566  -50.973 1.00 29.33  ? 168  ILE   A CG2    1 
ATOM   1242 C CD1    . ILE   A  1 176 ? 20.188 -91.653  -48.073 1.00 33.45  ? 168  ILE   A CD1    1 
ATOM   1243 N N      . GLU   A  1 177 ? 20.925 -91.621  -54.293 1.00 33.11  ? 169  GLU   A N      1 
ATOM   1244 C CA     . GLU   A  1 177 ? 20.440 -91.459  -55.662 1.00 33.68  ? 169  GLU   A CA     1 
ATOM   1245 C C      . GLU   A  1 177 ? 18.919 -91.173  -55.751 1.00 39.05  ? 169  GLU   A C      1 
ATOM   1246 O O      . GLU   A  1 177 ? 18.526 -90.244  -56.459 1.00 39.02  ? 169  GLU   A O      1 
ATOM   1247 C CB     . GLU   A  1 177 ? 20.858 -92.702  -56.492 1.00 35.54  ? 169  GLU   A CB     1 
ATOM   1248 C CG     . GLU   A  1 177 ? 20.218 -92.844  -57.868 1.00 51.16  ? 169  GLU   A CG     1 
ATOM   1249 C CD     . GLU   A  1 177 ? 18.909 -93.614  -57.929 1.00 77.35  ? 169  GLU   A CD     1 
ATOM   1250 O OE1    . GLU   A  1 177 ? 18.586 -94.337  -56.957 1.00 58.36  ? 169  GLU   A OE1    1 
ATOM   1251 O OE2    . GLU   A  1 177 ? 18.205 -93.492  -58.959 1.00 80.82  ? 169  GLU   A OE2    1 
ATOM   1252 N N      . ASN   A  1 178 ? 18.080 -91.968  -55.041 1.00 35.88  ? 170  ASN   A N      1 
ATOM   1253 C CA     . ASN   A  1 178 ? 16.615 -91.834  -55.033 1.00 35.60  ? 170  ASN   A CA     1 
ATOM   1254 C C      . ASN   A  1 178 ? 16.059 -91.029  -53.832 1.00 40.83  ? 170  ASN   A C      1 
ATOM   1255 O O      . ASN   A  1 178 ? 14.850 -91.050  -53.587 1.00 41.27  ? 170  ASN   A O      1 
ATOM   1256 C CB     . ASN   A  1 178 ? 15.941 -93.217  -55.129 1.00 34.90  ? 170  ASN   A CB     1 
ATOM   1257 C CG     . ASN   A  1 178 ? 16.254 -94.158  -53.986 1.00 50.51  ? 170  ASN   A CG     1 
ATOM   1258 O OD1    . ASN   A  1 178 ? 17.245 -94.003  -53.267 1.00 39.79  ? 170  ASN   A OD1    1 
ATOM   1259 N ND2    . ASN   A  1 178 ? 15.420 -95.175  -53.807 1.00 42.74  ? 170  ASN   A ND2    1 
ATOM   1260 N N      . ALA   A  1 179 ? 16.928 -90.325  -53.090 1.00 38.15  ? 171  ALA   A N      1 
ATOM   1261 C CA     . ALA   A  1 179 ? 16.508 -89.477  -51.964 1.00 38.72  ? 171  ALA   A CA     1 
ATOM   1262 C C      . ALA   A  1 179 ? 17.439 -88.260  -51.906 1.00 43.77  ? 171  ALA   A C      1 
ATOM   1263 O O      . ALA   A  1 179 ? 18.356 -88.206  -51.072 1.00 42.59  ? 171  ALA   A O      1 
ATOM   1264 C CB     . ALA   A  1 179 ? 16.513 -90.258  -50.652 1.00 39.32  ? 171  ALA   A CB     1 
ATOM   1265 N N      . PRO   A  1 180 ? 17.274 -87.304  -52.858 1.00 42.16  ? 172  PRO   A N      1 
ATOM   1266 C CA     . PRO   A  1 180 ? 18.176 -86.145  -52.882 1.00 42.43  ? 172  PRO   A CA     1 
ATOM   1267 C C      . PRO   A  1 180 ? 17.938 -85.174  -51.734 1.00 46.62  ? 172  PRO   A C      1 
ATOM   1268 O O      . PRO   A  1 180 ? 16.835 -85.106  -51.187 1.00 44.30  ? 172  PRO   A O      1 
ATOM   1269 C CB     . PRO   A  1 180 ? 17.899 -85.486  -54.243 1.00 44.06  ? 172  PRO   A CB     1 
ATOM   1270 C CG     . PRO   A  1 180 ? 16.940 -86.386  -54.953 1.00 48.53  ? 172  PRO   A CG     1 
ATOM   1271 C CD     . PRO   A  1 180 ? 16.257 -87.203  -53.923 1.00 43.92  ? 172  PRO   A CD     1 
ATOM   1272 N N      . THR   A  1 181 ? 18.998 -84.452  -51.358 1.00 45.91  ? 173  THR   A N      1 
ATOM   1273 C CA     . THR   A  1 181 ? 18.943 -83.442  -50.308 1.00 47.72  ? 173  THR   A CA     1 
ATOM   1274 C C      . THR   A  1 181 ? 18.273 -82.201  -50.913 1.00 57.81  ? 173  THR   A C      1 
ATOM   1275 O O      . THR   A  1 181 ? 18.491 -81.908  -52.094 1.00 57.08  ? 173  THR   A O      1 
ATOM   1276 C CB     . THR   A  1 181 ? 20.354 -83.151  -49.757 1.00 52.03  ? 173  THR   A CB     1 
ATOM   1277 O OG1    . THR   A  1 181 ? 21.218 -82.763  -50.830 1.00 49.12  ? 173  THR   A OG1    1 
ATOM   1278 C CG2    . THR   A  1 181 ? 20.954 -84.341  -48.990 1.00 47.25  ? 173  THR   A CG2    1 
ATOM   1279 N N      . THR   A  1 182 ? 17.425 -81.507  -50.130 1.00 59.18  ? 174  THR   A N      1 
ATOM   1280 C CA     . THR   A  1 182 ? 16.716 -80.307  -50.595 1.00 61.16  ? 174  THR   A CA     1 
ATOM   1281 C C      . THR   A  1 182 ? 17.695 -79.157  -50.844 1.00 68.61  ? 174  THR   A C      1 
ATOM   1282 O O      . THR   A  1 182 ? 18.485 -78.815  -49.960 1.00 68.51  ? 174  THR   A O      1 
ATOM   1283 C CB     . THR   A  1 182 ? 15.554 -79.923  -49.653 1.00 73.49  ? 174  THR   A CB     1 
ATOM   1284 O OG1    . THR   A  1 182 ? 16.042 -79.797  -48.313 1.00 75.83  ? 174  THR   A OG1    1 
ATOM   1285 C CG2    . THR   A  1 182 ? 14.394 -80.920  -49.704 1.00 72.52  ? 174  THR   A CG2    1 
ATOM   1286 N N      . HIS   A  1 183 ? 17.670 -78.599  -52.066 1.00 67.40  ? 175  HIS   A N      1 
ATOM   1287 C CA     . HIS   A  1 183 ? 18.540 -77.489  -52.467 1.00 68.25  ? 175  HIS   A CA     1 
ATOM   1288 C C      . HIS   A  1 183 ? 17.855 -76.130  -52.266 1.00 71.29  ? 175  HIS   A C      1 
ATOM   1289 O O      . HIS   A  1 183 ? 18.536 -75.105  -52.183 1.00 71.48  ? 175  HIS   A O      1 
ATOM   1290 C CB     . HIS   A  1 183 ? 19.034 -77.672  -53.909 1.00 69.80  ? 175  HIS   A CB     1 
ATOM   1291 C CG     . HIS   A  1 183 ? 19.703 -78.993  -54.128 1.00 73.89  ? 175  HIS   A CG     1 
ATOM   1292 N ND1    . HIS   A  1 183 ? 21.025 -79.202  -53.771 1.00 75.99  ? 175  HIS   A ND1    1 
ATOM   1293 C CD2    . HIS   A  1 183 ? 19.195 -80.148  -54.618 1.00 76.02  ? 175  HIS   A CD2    1 
ATOM   1294 C CE1    . HIS   A  1 183 ? 21.283 -80.465  -54.070 1.00 75.60  ? 175  HIS   A CE1    1 
ATOM   1295 N NE2    . HIS   A  1 183 ? 20.211 -81.076  -54.580 1.00 75.94  ? 175  HIS   A NE2    1 
ATOM   1296 N N      . THR   A  1 184 ? 16.511 -76.132  -52.177 1.00 66.31  ? 176  THR   A N      1 
ATOM   1297 C CA     . THR   A  1 184 ? 15.700 -74.938  -51.935 1.00 65.60  ? 176  THR   A CA     1 
ATOM   1298 C C      . THR   A  1 184 ? 15.770 -74.567  -50.443 1.00 67.76  ? 176  THR   A C      1 
ATOM   1299 O O      . THR   A  1 184 ? 15.802 -75.464  -49.589 1.00 67.57  ? 176  THR   A O      1 
ATOM   1300 C CB     . THR   A  1 184 ? 14.266 -75.108  -52.498 1.00 75.32  ? 176  THR   A CB     1 
ATOM   1301 O OG1    . THR   A  1 184 ? 13.532 -73.895  -52.313 1.00 77.25  ? 176  THR   A OG1    1 
ATOM   1302 C CG2    . THR   A  1 184 ? 13.502 -76.296  -51.885 1.00 72.97  ? 176  THR   A CG2    1 
ATOM   1303 N N      . GLU   A  1 185 ? 15.831 -73.256  -50.132 1.00 61.89  ? 177  GLU   A N      1 
ATOM   1304 C CA     . GLU   A  1 185 ? 15.915 -72.786  -48.744 1.00 60.30  ? 177  GLU   A CA     1 
ATOM   1305 C C      . GLU   A  1 185 ? 14.614 -73.018  -47.969 1.00 59.50  ? 177  GLU   A C      1 
ATOM   1306 O O      . GLU   A  1 185 ? 13.523 -72.840  -48.517 1.00 58.47  ? 177  GLU   A O      1 
ATOM   1307 C CB     . GLU   A  1 185 ? 16.396 -71.322  -48.641 1.00 61.82  ? 177  GLU   A CB     1 
ATOM   1308 C CG     . GLU   A  1 185 ? 15.495 -70.288  -49.300 1.00 74.68  ? 177  GLU   A CG     1 
ATOM   1309 C CD     . GLU   A  1 185 ? 15.845 -68.847  -48.985 1.00 99.94  ? 177  GLU   A CD     1 
ATOM   1310 O OE1    . GLU   A  1 185 ? 15.806 -68.473  -47.789 1.00 92.59  ? 177  GLU   A OE1    1 
ATOM   1311 O OE2    . GLU   A  1 185 ? 16.127 -68.084  -49.937 1.00 96.16  ? 177  GLU   A OE2    1 
ATOM   1312 N N      . GLU   A  1 186 ? 14.748 -73.464  -46.708 1.00 53.28  ? 178  GLU   A N      1 
ATOM   1313 C CA     . GLU   A  1 186 ? 13.633 -73.733  -45.795 1.00 51.91  ? 178  GLU   A CA     1 
ATOM   1314 C C      . GLU   A  1 186 ? 13.890 -72.957  -44.501 1.00 51.12  ? 178  GLU   A C      1 
ATOM   1315 O O      . GLU   A  1 186 ? 14.431 -73.518  -43.549 1.00 50.38  ? 178  GLU   A O      1 
ATOM   1316 C CB     . GLU   A  1 186 ? 13.506 -75.244  -45.513 1.00 53.50  ? 178  GLU   A CB     1 
ATOM   1317 C CG     . GLU   A  1 186 ? 13.025 -76.076  -46.690 1.00 65.97  ? 178  GLU   A CG     1 
ATOM   1318 C CD     . GLU   A  1 186 ? 12.798 -77.539  -46.362 1.00 92.87  ? 178  GLU   A CD     1 
ATOM   1319 O OE1    . GLU   A  1 186 ? 13.738 -78.194  -45.853 1.00 86.28  ? 178  GLU   A OE1    1 
ATOM   1320 O OE2    . GLU   A  1 186 ? 11.677 -78.033  -46.621 1.00 92.54  ? 178  GLU   A OE2    1 
ATOM   1321 N N      . TYR   A  1 187 ? 13.539 -71.654  -44.489 1.00 44.09  ? 179  TYR   A N      1 
ATOM   1322 C CA     . TYR   A  1 187 ? 13.762 -70.734  -43.366 1.00 42.10  ? 179  TYR   A CA     1 
ATOM   1323 C C      . TYR   A  1 187 ? 13.427 -71.336  -41.981 1.00 44.03  ? 179  TYR   A C      1 
ATOM   1324 O O      . TYR   A  1 187 ? 14.323 -71.427  -41.142 1.00 44.07  ? 179  TYR   A O      1 
ATOM   1325 C CB     . TYR   A  1 187 ? 13.035 -69.386  -43.581 1.00 42.17  ? 179  TYR   A CB     1 
ATOM   1326 C CG     . TYR   A  1 187 ? 13.479 -68.310  -42.610 1.00 42.51  ? 179  TYR   A CG     1 
ATOM   1327 C CD1    . TYR   A  1 187 ? 12.789 -68.089  -41.417 1.00 44.04  ? 179  TYR   A CD1    1 
ATOM   1328 C CD2    . TYR   A  1 187 ? 14.609 -67.535  -42.865 1.00 42.80  ? 179  TYR   A CD2    1 
ATOM   1329 C CE1    . TYR   A  1 187 ? 13.210 -67.118  -40.506 1.00 43.13  ? 179  TYR   A CE1    1 
ATOM   1330 C CE2    . TYR   A  1 187 ? 15.031 -66.553  -41.967 1.00 43.37  ? 179  TYR   A CE2    1 
ATOM   1331 C CZ     . TYR   A  1 187 ? 14.335 -66.357  -40.783 1.00 48.09  ? 179  TYR   A CZ     1 
ATOM   1332 O OH     . TYR   A  1 187 ? 14.758 -65.401  -39.893 1.00 45.36  ? 179  TYR   A OH     1 
ATOM   1333 N N      . SER   A  1 188 ? 12.158 -71.733  -41.752 1.00 38.78  ? 180  SER   A N      1 
ATOM   1334 C CA     . SER   A  1 188 ? 11.705 -72.309  -40.479 1.00 37.84  ? 180  SER   A CA     1 
ATOM   1335 C C      . SER   A  1 188 ? 12.180 -73.758  -40.286 1.00 40.44  ? 180  SER   A C      1 
ATOM   1336 O O      . SER   A  1 188 ? 12.465 -74.165  -39.153 1.00 39.16  ? 180  SER   A O      1 
ATOM   1337 C CB     . SER   A  1 188 ? 10.189 -72.201  -40.345 1.00 40.32  ? 180  SER   A CB     1 
ATOM   1338 O OG     . SER   A  1 188 ? 9.794  -70.838  -40.350 1.00 48.24  ? 180  SER   A OG     1 
ATOM   1339 N N      . GLY   A  1 189 ? 12.259 -74.504  -41.397 1.00 36.01  ? 181  GLY   A N      1 
ATOM   1340 C CA     . GLY   A  1 189 ? 12.738 -75.881  -41.445 1.00 34.71  ? 181  GLY   A CA     1 
ATOM   1341 C C      . GLY   A  1 189 ? 14.175 -76.012  -40.974 1.00 36.43  ? 181  GLY   A C      1 
ATOM   1342 O O      . GLY   A  1 189 ? 14.516 -76.991  -40.313 1.00 35.72  ? 181  GLY   A O      1 
ATOM   1343 N N      . GLU   A  1 190 ? 15.020 -75.011  -41.279 1.00 31.86  ? 182  GLU   A N      1 
ATOM   1344 C CA     . GLU   A  1 190 ? 16.430 -74.957  -40.861 1.00 31.66  ? 182  GLU   A CA     1 
ATOM   1345 C C      . GLU   A  1 190 ? 16.595 -74.646  -39.356 1.00 33.05  ? 182  GLU   A C      1 
ATOM   1346 O O      . GLU   A  1 190 ? 17.674 -74.867  -38.794 1.00 33.16  ? 182  GLU   A O      1 
ATOM   1347 C CB     . GLU   A  1 190 ? 17.216 -73.950  -41.719 1.00 33.31  ? 182  GLU   A CB     1 
ATOM   1348 C CG     . GLU   A  1 190 ? 17.597 -74.486  -43.095 1.00 45.69  ? 182  GLU   A CG     1 
ATOM   1349 C CD     . GLU   A  1 190 ? 17.890 -73.432  -44.149 1.00 69.54  ? 182  GLU   A CD     1 
ATOM   1350 O OE1    . GLU   A  1 190 ? 18.619 -72.461  -43.842 1.00 66.02  ? 182  GLU   A OE1    1 
ATOM   1351 O OE2    . GLU   A  1 190 ? 17.407 -73.591  -45.294 1.00 64.31  ? 182  GLU   A OE2    1 
ATOM   1352 N N      . GLU   A  1 191 ? 15.526 -74.160  -38.704 1.00 26.77  ? 183  GLU   A N      1 
ATOM   1353 C CA     . GLU   A  1 191 ? 15.543 -73.876  -37.264 1.00 26.01  ? 183  GLU   A CA     1 
ATOM   1354 C C      . GLU   A  1 191 ? 14.823 -74.984  -36.496 1.00 27.27  ? 183  GLU   A C      1 
ATOM   1355 O O      . GLU   A  1 191 ? 14.470 -74.779  -35.336 1.00 26.25  ? 183  GLU   A O      1 
ATOM   1356 C CB     . GLU   A  1 191 ? 14.875 -72.524  -36.947 1.00 26.87  ? 183  GLU   A CB     1 
ATOM   1357 C CG     . GLU   A  1 191 ? 15.264 -71.369  -37.854 1.00 33.43  ? 183  GLU   A CG     1 
ATOM   1358 C CD     . GLU   A  1 191 ? 14.404 -70.137  -37.662 1.00 42.12  ? 183  GLU   A CD     1 
ATOM   1359 O OE1    . GLU   A  1 191 ? 13.205 -70.276  -37.326 1.00 28.33  ? 183  GLU   A OE1    1 
ATOM   1360 O OE2    . GLU   A  1 191 ? 14.951 -69.023  -37.802 1.00 38.98  ? 183  GLU   A OE2    1 
ATOM   1361 N N      . LYS   A  1 192 ? 14.593 -76.150  -37.140 1.00 22.46  ? 184  LYS   A N      1 
ATOM   1362 C CA     . LYS   A  1 192 ? 13.868 -77.259  -36.527 1.00 21.55  ? 184  LYS   A CA     1 
ATOM   1363 C C      . LYS   A  1 192 ? 14.467 -77.756  -35.196 1.00 23.20  ? 184  LYS   A C      1 
ATOM   1364 O O      . LYS   A  1 192 ? 13.691 -78.159  -34.349 1.00 23.14  ? 184  LYS   A O      1 
ATOM   1365 C CB     . LYS   A  1 192 ? 13.657 -78.436  -37.508 1.00 23.79  ? 184  LYS   A CB     1 
ATOM   1366 C CG     . LYS   A  1 192 ? 14.922 -79.214  -37.896 1.00 27.95  ? 184  LYS   A CG     1 
ATOM   1367 C CD     . LYS   A  1 192 ? 14.632 -80.588  -38.559 1.00 33.53  ? 184  LYS   A CD     1 
ATOM   1368 C CE     . LYS   A  1 192 ? 13.866 -80.545  -39.866 1.00 27.78  ? 184  LYS   A CE     1 
ATOM   1369 N NZ     . LYS   A  1 192 ? 14.535 -79.696  -40.888 1.00 22.58  ? 184  LYS   A NZ     1 
ATOM   1370 N N      . THR   A  1 193 ? 15.813 -77.741  -34.998 1.00 18.69  ? 185  THR   A N      1 
ATOM   1371 C CA     . THR   A  1 193 ? 16.381 -78.244  -33.734 1.00 17.25  ? 185  THR   A CA     1 
ATOM   1372 C C      . THR   A  1 193 ? 16.104 -77.277  -32.561 1.00 20.77  ? 185  THR   A C      1 
ATOM   1373 O O      . THR   A  1 193 ? 16.032 -77.724  -31.413 1.00 19.74  ? 185  THR   A O      1 
ATOM   1374 C CB     . THR   A  1 193 ? 17.836 -78.641  -33.845 1.00 16.02  ? 185  THR   A CB     1 
ATOM   1375 O OG1    . THR   A  1 193 ? 18.619 -77.462  -33.986 1.00 16.53  ? 185  THR   A OG1    1 
ATOM   1376 C CG2    . THR   A  1 193 ? 18.104 -79.646  -34.981 1.00 16.16  ? 185  THR   A CG2    1 
ATOM   1377 N N      . TRP   A  1 194 ? 15.905 -75.981  -32.851 1.00 16.88  ? 186  TRP   A N      1 
ATOM   1378 C CA     . TRP   A  1 194 ? 15.496 -75.047  -31.802 1.00 17.59  ? 186  TRP   A CA     1 
ATOM   1379 C C      . TRP   A  1 194 ? 14.094 -75.453  -31.302 1.00 21.23  ? 186  TRP   A C      1 
ATOM   1380 O O      . TRP   A  1 194 ? 13.876 -75.451  -30.092 1.00 20.16  ? 186  TRP   A O      1 
ATOM   1381 C CB     . TRP   A  1 194 ? 15.554 -73.575  -32.241 1.00 16.69  ? 186  TRP   A CB     1 
ATOM   1382 C CG     . TRP   A  1 194 ? 15.109 -72.644  -31.152 1.00 17.98  ? 186  TRP   A CG     1 
ATOM   1383 C CD1    . TRP   A  1 194 ? 15.875 -72.137  -30.143 1.00 20.98  ? 186  TRP   A CD1    1 
ATOM   1384 C CD2    . TRP   A  1 194 ? 13.755 -72.258  -30.862 1.00 18.26  ? 186  TRP   A CD2    1 
ATOM   1385 N NE1    . TRP   A  1 194 ? 15.095 -71.394  -29.282 1.00 20.34  ? 186  TRP   A NE1    1 
ATOM   1386 C CE2    . TRP   A  1 194 ? 13.784 -71.482  -29.679 1.00 22.36  ? 186  TRP   A CE2    1 
ATOM   1387 C CE3    . TRP   A  1 194 ? 12.512 -72.496  -31.493 1.00 19.75  ? 186  TRP   A CE3    1 
ATOM   1388 C CZ2    . TRP   A  1 194 ? 12.628 -70.907  -29.132 1.00 21.98  ? 186  TRP   A CZ2    1 
ATOM   1389 C CZ3    . TRP   A  1 194 ? 11.363 -71.958  -30.931 1.00 21.64  ? 186  TRP   A CZ3    1 
ATOM   1390 C CH2    . TRP   A  1 194 ? 11.428 -71.161  -29.773 1.00 22.26  ? 186  TRP   A CH2    1 
ATOM   1391 N N      A MET   A  1 195 ? 13.168 -75.815  -32.226 0.50 17.86  ? 187  MET   A N      1 
ATOM   1392 N N      B MET   A  1 195 ? 13.173 -75.815  -32.235 0.50 19.00  ? 187  MET   A N      1 
ATOM   1393 C CA     A MET   A  1 195 ? 11.809 -76.253  -31.888 0.50 17.37  ? 187  MET   A CA     1 
ATOM   1394 C CA     B MET   A  1 195 ? 11.803 -76.279  -31.967 0.50 19.08  ? 187  MET   A CA     1 
ATOM   1395 C C      A MET   A  1 195 ? 11.820 -77.538  -31.041 0.50 21.11  ? 187  MET   A C      1 
ATOM   1396 C C      B MET   A  1 195 ? 11.817 -77.537  -31.069 0.50 21.99  ? 187  MET   A C      1 
ATOM   1397 O O      A MET   A  1 195 ? 10.977 -77.687  -30.154 0.50 20.20  ? 187  MET   A O      1 
ATOM   1398 O O      B MET   A  1 195 ? 10.976 -77.661  -30.176 0.50 21.22  ? 187  MET   A O      1 
ATOM   1399 C CB     A MET   A  1 195 ? 10.950 -76.416  -33.156 0.50 19.46  ? 187  MET   A CB     1 
ATOM   1400 C CB     B MET   A  1 195 ? 11.066 -76.524  -33.309 0.50 21.65  ? 187  MET   A CB     1 
ATOM   1401 C CG     A MET   A  1 195 ? 9.440  -76.425  -32.886 0.50 22.99  ? 187  MET   A CG     1 
ATOM   1402 C CG     B MET   A  1 195 ? 9.702  -77.222  -33.201 0.50 25.91  ? 187  MET   A CG     1 
ATOM   1403 S SD     A MET   A  1 195 ? 8.787  -74.902  -32.127 0.50 26.88  ? 187  MET   A SD     1 
ATOM   1404 S SD     B MET   A  1 195 ? 9.730  -79.011  -33.563 0.50 31.14  ? 187  MET   A SD     1 
ATOM   1405 C CE     A MET   A  1 195 ? 8.954  -73.765  -33.503 0.50 23.12  ? 187  MET   A CE     1 
ATOM   1406 C CE     B MET   A  1 195 ? 10.142 -79.002  -35.319 0.50 27.66  ? 187  MET   A CE     1 
ATOM   1407 N N      . TRP   A  1 196 ? 12.776 -78.458  -31.306 1.00 18.02  ? 188  TRP   A N      1 
ATOM   1408 C CA     . TRP   A  1 196 ? 12.937 -79.698  -30.521 1.00 17.66  ? 188  TRP   A CA     1 
ATOM   1409 C C      . TRP   A  1 196 ? 13.244 -79.286  -29.082 1.00 19.26  ? 188  TRP   A C      1 
ATOM   1410 O O      . TRP   A  1 196 ? 12.596 -79.768  -28.156 1.00 17.50  ? 188  TRP   A O      1 
ATOM   1411 C CB     . TRP   A  1 196 ? 14.118 -80.545  -31.027 1.00 16.60  ? 188  TRP   A CB     1 
ATOM   1412 C CG     . TRP   A  1 196 ? 14.030 -81.108  -32.418 1.00 17.97  ? 188  TRP   A CG     1 
ATOM   1413 C CD1    . TRP   A  1 196 ? 13.002 -80.987  -33.311 1.00 20.77  ? 188  TRP   A CD1    1 
ATOM   1414 C CD2    . TRP   A  1 196 ? 15.041 -81.887  -33.069 1.00 18.15  ? 188  TRP   A CD2    1 
ATOM   1415 N NE1    . TRP   A  1 196 ? 13.307 -81.653  -34.475 1.00 20.50  ? 188  TRP   A NE1    1 
ATOM   1416 C CE2    . TRP   A  1 196 ? 14.555 -82.217  -34.354 1.00 22.18  ? 188  TRP   A CE2    1 
ATOM   1417 C CE3    . TRP   A  1 196 ? 16.326 -82.324  -32.694 1.00 19.74  ? 188  TRP   A CE3    1 
ATOM   1418 C CZ2    . TRP   A  1 196 ? 15.306 -82.970  -35.268 1.00 21.86  ? 188  TRP   A CZ2    1 
ATOM   1419 C CZ3    . TRP   A  1 196 ? 17.062 -83.086  -33.594 1.00 21.80  ? 188  TRP   A CZ3    1 
ATOM   1420 C CH2    . TRP   A  1 196 ? 16.558 -83.390  -34.867 1.00 22.45  ? 188  TRP   A CH2    1 
ATOM   1421 N N      . TRP   A  1 197 ? 14.197 -78.340  -28.909 1.00 17.22  ? 189  TRP   A N      1 
ATOM   1422 C CA     . TRP   A  1 197 ? 14.530 -77.818  -27.595 1.00 17.42  ? 189  TRP   A CA     1 
ATOM   1423 C C      . TRP   A  1 197 ? 13.327 -77.092  -26.950 1.00 21.31  ? 189  TRP   A C      1 
ATOM   1424 O O      . TRP   A  1 197 ? 12.957 -77.416  -25.832 1.00 21.23  ? 189  TRP   A O      1 
ATOM   1425 C CB     . TRP   A  1 197 ? 15.776 -76.917  -27.642 1.00 16.15  ? 189  TRP   A CB     1 
ATOM   1426 C CG     . TRP   A  1 197 ? 15.874 -75.971  -26.471 1.00 17.18  ? 189  TRP   A CG     1 
ATOM   1427 C CD1    . TRP   A  1 197 ? 15.680 -74.624  -26.501 1.00 19.85  ? 189  TRP   A CD1    1 
ATOM   1428 C CD2    . TRP   A  1 197 ? 16.060 -76.321  -25.082 1.00 16.96  ? 189  TRP   A CD2    1 
ATOM   1429 N NE1    . TRP   A  1 197 ? 15.778 -74.102  -25.233 1.00 19.23  ? 189  TRP   A NE1    1 
ATOM   1430 C CE2    . TRP   A  1 197 ? 16.012 -75.118  -24.341 1.00 20.34  ? 189  TRP   A CE2    1 
ATOM   1431 C CE3    . TRP   A  1 197 ? 16.334 -77.523  -24.402 1.00 18.14  ? 189  TRP   A CE3    1 
ATOM   1432 C CZ2    . TRP   A  1 197 ? 16.215 -75.078  -22.955 1.00 18.96  ? 189  TRP   A CZ2    1 
ATOM   1433 C CZ3    . TRP   A  1 197 ? 16.533 -77.489  -23.022 1.00 19.78  ? 189  TRP   A CZ3    1 
ATOM   1434 C CH2    . TRP   A  1 197 ? 16.484 -76.274  -22.313 1.00 20.30  ? 189  TRP   A CH2    1 
ATOM   1435 N N      . HIS   A  1 198 ? 12.739 -76.123  -27.652 1.00 18.68  ? 190  HIS   A N      1 
ATOM   1436 C CA     . HIS   A  1 198 ? 11.611 -75.329  -27.166 1.00 17.95  ? 190  HIS   A CA     1 
ATOM   1437 C C      . HIS   A  1 198 ? 10.440 -76.188  -26.709 1.00 22.53  ? 190  HIS   A C      1 
ATOM   1438 O O      . HIS   A  1 198 ? 9.881  -75.899  -25.654 1.00 21.32  ? 190  HIS   A O      1 
ATOM   1439 C CB     . HIS   A  1 198 ? 11.159 -74.317  -28.214 1.00 18.14  ? 190  HIS   A CB     1 
ATOM   1440 C CG     . HIS   A  1 198 ? 9.957  -73.519  -27.797 1.00 21.09  ? 190  HIS   A CG     1 
ATOM   1441 N ND1    . HIS   A  1 198 ? 10.015 -72.613  -26.744 1.00 22.13  ? 190  HIS   A ND1    1 
ATOM   1442 C CD2    . HIS   A  1 198 ? 8.703  -73.519  -28.309 1.00 21.98  ? 190  HIS   A CD2    1 
ATOM   1443 C CE1    . HIS   A  1 198 ? 8.807  -72.083  -26.663 1.00 21.18  ? 190  HIS   A CE1    1 
ATOM   1444 N NE2    . HIS   A  1 198 ? 7.979  -72.608  -27.576 1.00 21.84  ? 190  HIS   A NE2    1 
ATOM   1445 N N      . ASN   A  1 199 ? 10.092 -77.248  -27.478 1.00 18.84  ? 191  ASN   A N      1 
ATOM   1446 C CA     . ASN   A  1 199 ? 9.001  -78.150  -27.125 1.00 18.46  ? 191  ASN   A CA     1 
ATOM   1447 C C      . ASN   A  1 199 ? 9.296  -78.943  -25.896 1.00 22.06  ? 191  ASN   A C      1 
ATOM   1448 O O      . ASN   A  1 199 ? 8.408  -79.094  -25.065 1.00 22.76  ? 191  ASN   A O      1 
ATOM   1449 C CB     . ASN   A  1 199 ? 8.628  -79.094  -28.277 1.00 18.66  ? 191  ASN   A CB     1 
ATOM   1450 C CG     . ASN   A  1 199 ? 7.930  -78.415  -29.418 1.00 35.41  ? 191  ASN   A CG     1 
ATOM   1451 O OD1    . ASN   A  1 199 ? 7.494  -77.264  -29.314 1.00 27.94  ? 191  ASN   A OD1    1 
ATOM   1452 N ND2    . ASN   A  1 199 ? 7.816  -79.117  -30.542 1.00 24.17  ? 191  ASN   A ND2    1 
ATOM   1453 N N      . PHE   A  1 200 ? 10.533 -79.465  -25.775 1.00 17.69  ? 192  PHE   A N      1 
ATOM   1454 C CA     . PHE   A  1 200 ? 10.972 -80.269  -24.644 1.00 16.66  ? 192  PHE   A CA     1 
ATOM   1455 C C      . PHE   A  1 200 ? 10.944 -79.445  -23.343 1.00 21.01  ? 192  PHE   A C      1 
ATOM   1456 O O      . PHE   A  1 200 ? 10.425 -79.904  -22.322 1.00 18.74  ? 192  PHE   A O      1 
ATOM   1457 C CB     . PHE   A  1 200 ? 12.380 -80.851  -24.911 1.00 17.19  ? 192  PHE   A CB     1 
ATOM   1458 C CG     . PHE   A  1 200 ? 12.885 -81.739  -23.799 1.00 17.56  ? 192  PHE   A CG     1 
ATOM   1459 C CD1    . PHE   A  1 200 ? 12.585 -83.095  -23.780 1.00 20.07  ? 192  PHE   A CD1    1 
ATOM   1460 C CD2    . PHE   A  1 200 ? 13.621 -81.211  -22.747 1.00 17.96  ? 192  PHE   A CD2    1 
ATOM   1461 C CE1    . PHE   A  1 200 ? 13.063 -83.913  -22.760 1.00 20.21  ? 192  PHE   A CE1    1 
ATOM   1462 C CE2    . PHE   A  1 200 ? 14.034 -82.018  -21.690 1.00 19.91  ? 192  PHE   A CE2    1 
ATOM   1463 C CZ     . PHE   A  1 200 ? 13.756 -83.362  -21.705 1.00 18.50  ? 192  PHE   A CZ     1 
ATOM   1464 N N      . ARG   A  1 201 ? 11.505 -78.232  -23.387 1.00 19.02  ? 193  ARG   A N      1 
ATOM   1465 C CA     . ARG   A  1 201 ? 11.547 -77.387  -22.201 1.00 18.61  ? 193  ARG   A CA     1 
ATOM   1466 C C      . ARG   A  1 201 ? 10.145 -76.851  -21.825 1.00 22.37  ? 193  ARG   A C      1 
ATOM   1467 O O      . ARG   A  1 201 ? 9.902  -76.620  -20.646 1.00 21.46  ? 193  ARG   A O      1 
ATOM   1468 C CB     . ARG   A  1 201 ? 12.604 -76.279  -22.318 1.00 17.52  ? 193  ARG   A CB     1 
ATOM   1469 C CG     . ARG   A  1 201 ? 12.358 -75.276  -23.406 1.00 21.51  ? 193  ARG   A CG     1 
ATOM   1470 C CD     . ARG   A  1 201 ? 11.573 -74.051  -22.952 1.00 25.09  ? 193  ARG   A CD     1 
ATOM   1471 N NE     . ARG   A  1 201 ? 11.500 -73.115  -24.064 1.00 25.00  ? 193  ARG   A NE     1 
ATOM   1472 C CZ     . ARG   A  1 201 ? 12.481 -72.283  -24.378 1.00 35.20  ? 193  ARG   A CZ     1 
ATOM   1473 N NH1    . ARG   A  1 201 ? 13.559 -72.200  -23.609 1.00 22.79  ? 193  ARG   A NH1    1 
ATOM   1474 N NH2    . ARG   A  1 201 ? 12.382 -71.508  -25.446 1.00 22.12  ? 193  ARG   A NH2    1 
ATOM   1475 N N      . THR   A  1 202 ? 9.228  -76.704  -22.819 1.00 18.73  ? 194  THR   A N      1 
ATOM   1476 C CA     . THR   A  1 202 ? 7.837  -76.305  -22.589 1.00 18.16  ? 194  THR   A CA     1 
ATOM   1477 C C      . THR   A  1 202 ? 7.114  -77.428  -21.825 1.00 19.41  ? 194  THR   A C      1 
ATOM   1478 O O      . THR   A  1 202 ? 6.490  -77.158  -20.810 1.00 19.03  ? 194  THR   A O      1 
ATOM   1479 C CB     . THR   A  1 202 ? 7.162  -75.847  -23.891 1.00 21.26  ? 194  THR   A CB     1 
ATOM   1480 O OG1    . THR   A  1 202 ? 7.845  -74.679  -24.362 1.00 22.49  ? 194  THR   A OG1    1 
ATOM   1481 C CG2    . THR   A  1 202 ? 5.696  -75.511  -23.707 1.00 20.68  ? 194  THR   A CG2    1 
ATOM   1482 N N      . LEU   A  1 203 ? 7.263  -78.676  -22.266 1.00 17.60  ? 195  LEU   A N      1 
ATOM   1483 C CA     . LEU   A  1 203 ? 6.678  -79.864  -21.615 1.00 16.82  ? 195  LEU   A CA     1 
ATOM   1484 C C      . LEU   A  1 203 ? 7.175  -80.016  -20.174 1.00 21.35  ? 195  LEU   A C      1 
ATOM   1485 O O      . LEU   A  1 203 ? 6.395  -80.330  -19.274 1.00 20.37  ? 195  LEU   A O      1 
ATOM   1486 C CB     . LEU   A  1 203 ? 7.024  -81.138  -22.404 1.00 16.64  ? 195  LEU   A CB     1 
ATOM   1487 C CG     . LEU   A  1 203 ? 6.336  -81.306  -23.749 1.00 21.03  ? 195  LEU   A CG     1 
ATOM   1488 C CD1    . LEU   A  1 203 ? 7.112  -82.271  -24.622 1.00 21.15  ? 195  LEU   A CD1    1 
ATOM   1489 C CD2    . LEU   A  1 203 ? 4.891  -81.743  -23.590 1.00 21.33  ? 195  LEU   A CD2    1 
ATOM   1490 N N      . CYS   A  1 204 ? 8.474  -79.756  -19.968 1.00 19.72  ? 196  CYS   A N      1 
ATOM   1491 C CA     . CYS   A  1 204 ? 9.156  -79.823  -18.685 1.00 20.50  ? 196  CYS   A CA     1 
ATOM   1492 C C      . CYS   A  1 204 ? 8.916  -78.573  -17.837 1.00 24.92  ? 196  CYS   A C      1 
ATOM   1493 O O      . CYS   A  1 204 ? 9.457  -78.473  -16.744 1.00 24.19  ? 196  CYS   A O      1 
ATOM   1494 C CB     . CYS   A  1 204 ? 10.640 -80.105  -18.880 1.00 20.93  ? 196  CYS   A CB     1 
ATOM   1495 S SG     . CYS   A  1 204 ? 10.986 -81.729  -19.600 1.00 25.01  ? 196  CYS   A SG     1 
ATOM   1496 N N      . ASP   A  1 205 ? 8.094  -77.638  -18.349 1.00 22.44  ? 197  ASP   A N      1 
ATOM   1497 C CA     . ASP   A  1 205 ? 7.628  -76.411  -17.691 1.00 22.39  ? 197  ASP   A CA     1 
ATOM   1498 C C      . ASP   A  1 205 ? 8.764  -75.498  -17.183 1.00 25.18  ? 197  ASP   A C      1 
ATOM   1499 O O      . ASP   A  1 205 ? 8.744  -75.020  -16.035 1.00 23.36  ? 197  ASP   A O      1 
ATOM   1500 C CB     . ASP   A  1 205 ? 6.615  -76.759  -16.578 1.00 24.35  ? 197  ASP   A CB     1 
ATOM   1501 C CG     . ASP   A  1 205 ? 5.711  -75.621  -16.121 1.00 38.11  ? 197  ASP   A CG     1 
ATOM   1502 O OD1    . ASP   A  1 205 ? 5.516  -74.659  -16.903 1.00 39.99  ? 197  ASP   A OD1    1 
ATOM   1503 O OD2    . ASP   A  1 205 ? 5.181  -75.706  -14.997 1.00 45.74  ? 197  ASP   A OD2    1 
ATOM   1504 N N      . TYR   A  1 206 ? 9.734  -75.216  -18.076 1.00 22.70  ? 198  TYR   A N      1 
ATOM   1505 C CA     . TYR   A  1 206 ? 10.866 -74.319  -17.808 1.00 23.04  ? 198  TYR   A CA     1 
ATOM   1506 C C      . TYR   A  1 206 ? 11.633 -74.644  -16.513 1.00 25.28  ? 198  TYR   A C      1 
ATOM   1507 O O      . TYR   A  1 206 ? 11.981 -73.741  -15.761 1.00 25.81  ? 198  TYR   A O      1 
ATOM   1508 C CB     . TYR   A  1 206 ? 10.436 -72.837  -17.841 1.00 25.24  ? 198  TYR   A CB     1 
ATOM   1509 C CG     . TYR   A  1 206 ? 10.014 -72.355  -19.206 1.00 26.83  ? 198  TYR   A CG     1 
ATOM   1510 C CD1    . TYR   A  1 206 ? 8.773  -72.698  -19.735 1.00 28.76  ? 198  TYR   A CD1    1 
ATOM   1511 C CD2    . TYR   A  1 206 ? 10.830 -71.509  -19.950 1.00 27.71  ? 198  TYR   A CD2    1 
ATOM   1512 C CE1    . TYR   A  1 206 ? 8.377  -72.259  -20.994 1.00 29.46  ? 198  TYR   A CE1    1 
ATOM   1513 C CE2    . TYR   A  1 206 ? 10.432 -71.037  -21.203 1.00 28.52  ? 198  TYR   A CE2    1 
ATOM   1514 C CZ     . TYR   A  1 206 ? 9.203  -71.416  -21.718 1.00 36.14  ? 198  TYR   A CZ     1 
ATOM   1515 O OH     . TYR   A  1 206 ? 8.787  -70.966  -22.942 1.00 38.20  ? 198  TYR   A OH     1 
ATOM   1516 N N      . SER   A  1 207 ? 11.923 -75.922  -16.263 1.00 20.84  ? 199  SER   A N      1 
ATOM   1517 C CA     . SER   A  1 207 ? 12.694 -76.305  -15.076 1.00 20.26  ? 199  SER   A CA     1 
ATOM   1518 C C      . SER   A  1 207 ? 14.069 -75.623  -15.117 1.00 24.14  ? 199  SER   A C      1 
ATOM   1519 O O      . SER   A  1 207 ? 14.749 -75.694  -16.141 1.00 23.99  ? 199  SER   A O      1 
ATOM   1520 C CB     . SER   A  1 207 ? 12.871 -77.821  -15.016 1.00 22.38  ? 199  SER   A CB     1 
ATOM   1521 O OG     . SER   A  1 207 ? 13.802 -78.171  -14.004 1.00 29.07  ? 199  SER   A OG     1 
ATOM   1522 N N      . LYS   A  1 208 ? 14.477 -74.967  -14.016 1.00 20.18  ? 200  LYS   A N      1 
ATOM   1523 C CA     . LYS   A  1 208 ? 15.792 -74.316  -13.925 1.00 21.04  ? 200  LYS   A CA     1 
ATOM   1524 C C      . LYS   A  1 208 ? 16.934 -75.364  -14.004 1.00 24.84  ? 200  LYS   A C      1 
ATOM   1525 O O      . LYS   A  1 208 ? 18.079 -75.014  -14.269 1.00 26.32  ? 200  LYS   A O      1 
ATOM   1526 C CB     . LYS   A  1 208 ? 15.905 -73.454  -12.640 1.00 23.91  ? 200  LYS   A CB     1 
ATOM   1527 C CG     . LYS   A  1 208 ? 15.978 -74.263  -11.342 1.00 36.43  ? 200  LYS   A CG     1 
ATOM   1528 C CD     . LYS   A  1 208 ? 16.149 -73.398  -10.099 1.00 48.37  ? 200  LYS   A CD     1 
ATOM   1529 C CE     . LYS   A  1 208 ? 16.298 -74.267  -8.868  1.00 59.09  ? 200  LYS   A CE     1 
ATOM   1530 N NZ     . LYS   A  1 208 ? 16.576 -73.465  -7.645  1.00 70.59  ? 200  LYS   A NZ     1 
ATOM   1531 N N      . ARG   A  1 209 ? 16.611 -76.632  -13.770 1.00 19.95  ? 201  ARG   A N      1 
ATOM   1532 C CA     . ARG   A  1 209 ? 17.578 -77.732  -13.808 1.00 20.04  ? 201  ARG   A CA     1 
ATOM   1533 C C      . ARG   A  1 209 ? 17.847 -78.257  -15.244 1.00 23.77  ? 201  ARG   A C      1 
ATOM   1534 O O      . ARG   A  1 209 ? 18.724 -79.101  -15.416 1.00 24.60  ? 201  ARG   A O      1 
ATOM   1535 C CB     . ARG   A  1 209 ? 17.140 -78.868  -12.872 1.00 17.69  ? 201  ARG   A CB     1 
ATOM   1536 C CG     . ARG   A  1 209 ? 17.169 -78.479  -11.381 1.00 27.66  ? 201  ARG   A CG     1 
ATOM   1537 C CD     . ARG   A  1 209 ? 16.684 -79.594  -10.478 1.00 32.55  ? 201  ARG   A CD     1 
ATOM   1538 N NE     . ARG   A  1 209 ? 17.597 -80.738  -10.497 1.00 40.07  ? 201  ARG   A NE     1 
ATOM   1539 C CZ     . ARG   A  1 209 ? 17.312 -81.948  -10.023 1.00 47.13  ? 201  ARG   A CZ     1 
ATOM   1540 N NH1    . ARG   A  1 209 ? 16.122 -82.196  -9.482  1.00 30.76  ? 201  ARG   A NH1    1 
ATOM   1541 N NH2    . ARG   A  1 209 ? 18.206 -82.923  -10.099 1.00 27.13  ? 201  ARG   A NH2    1 
ATOM   1542 N N      . ILE   A  1 210 ? 17.109 -77.771  -16.263 1.00 18.76  ? 202  ILE   A N      1 
ATOM   1543 C CA     . ILE   A  1 210 ? 17.293 -78.249  -17.642 1.00 18.62  ? 202  ILE   A CA     1 
ATOM   1544 C C      . ILE   A  1 210 ? 17.923 -77.172  -18.517 1.00 22.25  ? 202  ILE   A C      1 
ATOM   1545 O O      . ILE   A  1 210 ? 17.377 -76.081  -18.666 1.00 21.94  ? 202  ILE   A O      1 
ATOM   1546 C CB     . ILE   A  1 210 ? 15.998 -78.846  -18.241 1.00 21.45  ? 202  ILE   A CB     1 
ATOM   1547 C CG1    . ILE   A  1 210 ? 15.403 -79.952  -17.327 1.00 21.28  ? 202  ILE   A CG1    1 
ATOM   1548 C CG2    . ILE   A  1 210 ? 16.195 -79.322  -19.691 1.00 22.08  ? 202  ILE   A CG2    1 
ATOM   1549 C CD1    . ILE   A  1 210 ? 13.933 -80.322  -17.589 1.00 23.29  ? 202  ILE   A CD1    1 
ATOM   1550 N N      . ALA   A  1 211 ? 19.102 -77.473  -19.063 1.00 18.42  ? 203  ALA   A N      1 
ATOM   1551 C CA     . ALA   A  1 211 ? 19.854 -76.538  -19.897 1.00 18.02  ? 203  ALA   A CA     1 
ATOM   1552 C C      . ALA   A  1 211 ? 20.243 -77.162  -21.246 1.00 22.42  ? 203  ALA   A C      1 
ATOM   1553 O O      . ALA   A  1 211 ? 19.874 -78.306  -21.529 1.00 20.38  ? 203  ALA   A O      1 
ATOM   1554 C CB     . ALA   A  1 211 ? 21.079 -76.065  -19.134 1.00 18.85  ? 203  ALA   A CB     1 
ATOM   1555 N N      . VAL   A  1 212 ? 20.923 -76.386  -22.102 1.00 21.37  ? 204  VAL   A N      1 
ATOM   1556 C CA     . VAL   A  1 212 ? 21.337 -76.822  -23.449 1.00 20.86  ? 204  VAL   A CA     1 
ATOM   1557 C C      . VAL   A  1 212 ? 22.841 -77.123  -23.503 1.00 24.37  ? 204  VAL   A C      1 
ATOM   1558 O O      . VAL   A  1 212 ? 23.660 -76.367  -22.967 1.00 23.47  ? 204  VAL   A O      1 
ATOM   1559 C CB     . VAL   A  1 212 ? 20.968 -75.750  -24.524 1.00 24.42  ? 204  VAL   A CB     1 
ATOM   1560 C CG1    . VAL   A  1 212 ? 21.568 -76.071  -25.901 1.00 24.24  ? 204  VAL   A CG1    1 
ATOM   1561 C CG2    . VAL   A  1 212 ? 19.466 -75.549  -24.629 1.00 23.73  ? 204  VAL   A CG2    1 
ATOM   1562 N N      . ALA   A  1 213 ? 23.177 -78.210  -24.201 1.00 21.22  ? 205  ALA   A N      1 
ATOM   1563 C CA     . ALA   A  1 213 ? 24.528 -78.626  -24.582 1.00 20.62  ? 205  ALA   A CA     1 
ATOM   1564 C C      . ALA   A  1 213 ? 24.490 -78.552  -26.131 1.00 23.41  ? 205  ALA   A C      1 
ATOM   1565 O O      . ALA   A  1 213 ? 24.012 -79.460  -26.804 1.00 22.91  ? 205  ALA   A O      1 
ATOM   1566 C CB     . ALA   A  1 213 ? 24.819 -80.035  -24.093 1.00 20.35  ? 205  ALA   A CB     1 
ATOM   1567 N N      . LEU   A  1 214 ? 24.845 -77.392  -26.664 1.00 20.04  ? 206  LEU   A N      1 
ATOM   1568 C CA     . LEU   A  1 214 ? 24.771 -77.117  -28.097 1.00 20.14  ? 206  LEU   A CA     1 
ATOM   1569 C C      . LEU   A  1 214 ? 25.924 -77.757  -28.882 1.00 23.91  ? 206  LEU   A C      1 
ATOM   1570 O O      . LEU   A  1 214 ? 27.086 -77.424  -28.660 1.00 22.51  ? 206  LEU   A O      1 
ATOM   1571 C CB     . LEU   A  1 214 ? 24.662 -75.607  -28.355 1.00 19.74  ? 206  LEU   A CB     1 
ATOM   1572 C CG     . LEU   A  1 214 ? 24.326 -75.181  -29.797 1.00 24.12  ? 206  LEU   A CG     1 
ATOM   1573 C CD1    . LEU   A  1 214 ? 22.896 -75.565  -30.190 1.00 23.35  ? 206  LEU   A CD1    1 
ATOM   1574 C CD2    . LEU   A  1 214 ? 24.563 -73.682  -29.991 1.00 26.94  ? 206  LEU   A CD2    1 
ATOM   1575 N N      . GLU   A  1 215 ? 25.591 -78.693  -29.769 1.00 21.49  ? 207  GLU   A N      1 
ATOM   1576 C CA     . GLU   A  1 215 ? 26.585 -79.400  -30.571 1.00 22.38  ? 207  GLU   A CA     1 
ATOM   1577 C C      . GLU   A  1 215 ? 26.832 -78.681  -31.898 1.00 26.99  ? 207  GLU   A C      1 
ATOM   1578 O O      . GLU   A  1 215 ? 25.905 -78.506  -32.680 1.00 26.47  ? 207  GLU   A O      1 
ATOM   1579 C CB     . GLU   A  1 215 ? 26.163 -80.864  -30.770 1.00 24.23  ? 207  GLU   A CB     1 
ATOM   1580 C CG     . GLU   A  1 215 ? 27.215 -81.724  -31.460 1.00 37.00  ? 207  GLU   A CG     1 
ATOM   1581 C CD     . GLU   A  1 215 ? 27.301 -83.163  -30.986 1.00 58.65  ? 207  GLU   A CD     1 
ATOM   1582 O OE1    . GLU   A  1 215 ? 26.272 -83.700  -30.516 1.00 46.92  ? 207  GLU   A OE1    1 
ATOM   1583 O OE2    . GLU   A  1 215 ? 28.401 -83.754  -31.087 1.00 49.10  ? 207  GLU   A OE2    1 
ATOM   1584 N N      . ILE   A  1 216 ? 28.071 -78.230  -32.116 1.00 24.92  ? 208  ILE   A N      1 
ATOM   1585 C CA     . ILE   A  1 216 ? 28.500 -77.512  -33.324 1.00 25.68  ? 208  ILE   A CA     1 
ATOM   1586 C C      . ILE   A  1 216 ? 28.981 -78.533  -34.359 1.00 30.76  ? 208  ILE   A C      1 
ATOM   1587 O O      . ILE   A  1 216 ? 29.519 -79.565  -33.990 1.00 31.45  ? 208  ILE   A O      1 
ATOM   1588 C CB     . ILE   A  1 216 ? 29.589 -76.440  -32.976 1.00 28.71  ? 208  ILE   A CB     1 
ATOM   1589 C CG1    . ILE   A  1 216 ? 29.203 -75.561  -31.748 1.00 29.39  ? 208  ILE   A CG1    1 
ATOM   1590 C CG2    . ILE   A  1 216 ? 29.984 -75.571  -34.184 1.00 27.86  ? 208  ILE   A CG2    1 
ATOM   1591 C CD1    . ILE   A  1 216 ? 27.751 -74.915  -31.704 1.00 42.69  ? 208  ILE   A CD1    1 
ATOM   1592 N N      . GLY   A  1 217 ? 28.723 -78.261  -35.629 1.00 28.07  ? 209  GLY   A N      1 
ATOM   1593 C CA     . GLY   A  1 217 ? 29.082 -79.124  -36.753 1.00 28.62  ? 209  GLY   A CA     1 
ATOM   1594 C C      . GLY   A  1 217 ? 30.044 -78.431  -37.692 1.00 33.37  ? 209  GLY   A C      1 
ATOM   1595 O O      . GLY   A  1 217 ? 30.336 -77.249  -37.503 1.00 31.06  ? 209  GLY   A O      1 
ATOM   1596 N N      . ALA   A  1 218 ? 30.569 -79.172  -38.688 1.00 33.11  ? 210  ALA   A N      1 
ATOM   1597 C CA     . ALA   A  1 218 ? 31.559 -78.677  -39.655 1.00 34.00  ? 210  ALA   A CA     1 
ATOM   1598 C C      . ALA   A  1 218 ? 31.047 -77.514  -40.484 1.00 39.31  ? 210  ALA   A C      1 
ATOM   1599 O O      . ALA   A  1 218 ? 31.787 -76.559  -40.722 1.00 39.53  ? 210  ALA   A O      1 
ATOM   1600 C CB     . ALA   A  1 218 ? 32.036 -79.809  -40.555 1.00 34.98  ? 210  ALA   A CB     1 
ATOM   1601 N N      . ASP   A  1 219 ? 29.779 -77.570  -40.886 1.00 36.83  ? 211  ASP   A N      1 
ATOM   1602 C CA     . ASP   A  1 219 ? 29.177 -76.496  -41.652 1.00 37.68  ? 211  ASP   A CA     1 
ATOM   1603 C C      . ASP   A  1 219 ? 28.169 -75.764  -40.779 1.00 41.85  ? 211  ASP   A C      1 
ATOM   1604 O O      . ASP   A  1 219 ? 27.173 -76.350  -40.335 1.00 41.58  ? 211  ASP   A O      1 
ATOM   1605 C CB     . ASP   A  1 219 ? 28.569 -77.019  -42.967 1.00 40.24  ? 211  ASP   A CB     1 
ATOM   1606 C CG     . ASP   A  1 219 ? 29.607 -77.631  -43.904 1.00 56.08  ? 211  ASP   A CG     1 
ATOM   1607 O OD1    . ASP   A  1 219 ? 30.571 -76.917  -44.278 1.00 56.98  ? 211  ASP   A OD1    1 
ATOM   1608 O OD2    . ASP   A  1 219 ? 29.471 -78.830  -44.241 1.00 63.79  ? 211  ASP   A OD2    1 
ATOM   1609 N N      . LEU   A  1 220 ? 28.482 -74.497  -40.467 1.00 37.48  ? 212  LEU   A N      1 
ATOM   1610 C CA     . LEU   A  1 220 ? 27.612 -73.660  -39.652 1.00 36.73  ? 212  LEU   A CA     1 
ATOM   1611 C C      . LEU   A  1 220 ? 26.367 -73.299  -40.441 1.00 41.31  ? 212  LEU   A C      1 
ATOM   1612 O O      . LEU   A  1 220 ? 26.476 -73.013  -41.635 1.00 42.00  ? 212  LEU   A O      1 
ATOM   1613 C CB     . LEU   A  1 220 ? 28.322 -72.379  -39.192 1.00 36.36  ? 212  LEU   A CB     1 
ATOM   1614 C CG     . LEU   A  1 220 ? 29.370 -72.507  -38.093 1.00 40.37  ? 212  LEU   A CG     1 
ATOM   1615 C CD1    . LEU   A  1 220 ? 29.839 -71.132  -37.652 1.00 39.81  ? 212  LEU   A CD1    1 
ATOM   1616 C CD2    . LEU   A  1 220 ? 28.844 -73.294  -36.891 1.00 40.69  ? 212  LEU   A CD2    1 
ATOM   1617 N N      . PRO   A  1 221 ? 25.170 -73.291  -39.813 1.00 37.39  ? 213  PRO   A N      1 
ATOM   1618 C CA     . PRO   A  1 221 ? 23.962 -72.911  -40.566 1.00 36.56  ? 213  PRO   A CA     1 
ATOM   1619 C C      . PRO   A  1 221 ? 23.930 -71.401  -40.804 1.00 39.23  ? 213  PRO   A C      1 
ATOM   1620 O O      . PRO   A  1 221 ? 24.864 -70.703  -40.392 1.00 38.55  ? 213  PRO   A O      1 
ATOM   1621 C CB     . PRO   A  1 221 ? 22.833 -73.354  -39.637 1.00 37.91  ? 213  PRO   A CB     1 
ATOM   1622 C CG     . PRO   A  1 221 ? 23.417 -73.218  -38.265 1.00 42.11  ? 213  PRO   A CG     1 
ATOM   1623 C CD     . PRO   A  1 221 ? 24.856 -73.591  -38.397 1.00 38.16  ? 213  PRO   A CD     1 
ATOM   1624 N N      . SER   A  1 222 ? 22.858 -70.884  -41.440 1.00 35.26  ? 214  SER   A N      1 
ATOM   1625 C CA     . SER   A  1 222 ? 22.728 -69.435  -41.658 1.00 35.09  ? 214  SER   A CA     1 
ATOM   1626 C C      . SER   A  1 222 ? 22.614 -68.724  -40.293 1.00 36.58  ? 214  SER   A C      1 
ATOM   1627 O O      . SER   A  1 222 ? 22.345 -69.388  -39.290 1.00 35.45  ? 214  SER   A O      1 
ATOM   1628 C CB     . SER   A  1 222 ? 21.560 -69.100  -42.589 1.00 39.21  ? 214  SER   A CB     1 
ATOM   1629 O OG     . SER   A  1 222 ? 20.534 -70.079  -42.577 1.00 52.49  ? 214  SER   A OG     1 
ATOM   1630 N N      . ASN   A  1 223 ? 22.895 -67.413  -40.243 1.00 32.38  ? 215  ASN   A N      1 
ATOM   1631 C CA     . ASN   A  1 223 ? 22.881 -66.643  -38.995 1.00 32.35  ? 215  ASN   A CA     1 
ATOM   1632 C C      . ASN   A  1 223 ? 21.587 -66.755  -38.207 1.00 37.06  ? 215  ASN   A C      1 
ATOM   1633 O O      . ASN   A  1 223 ? 21.658 -66.898  -36.987 1.00 38.33  ? 215  ASN   A O      1 
ATOM   1634 C CB     . ASN   A  1 223 ? 23.238 -65.185  -39.230 1.00 33.61  ? 215  ASN   A CB     1 
ATOM   1635 C CG     . ASN   A  1 223 ? 24.726 -64.930  -39.270 1.00 66.37  ? 215  ASN   A CG     1 
ATOM   1636 O OD1    . ASN   A  1 223 ? 25.475 -65.545  -40.036 1.00 58.44  ? 215  ASN   A OD1    1 
ATOM   1637 N ND2    . ASN   A  1 223 ? 25.190 -64.007  -38.441 1.00 63.76  ? 215  ASN   A ND2    1 
ATOM   1638 N N      . HIS   A  1 224 ? 20.417 -66.753  -38.889 1.00 32.01  ? 216  HIS   A N      1 
ATOM   1639 C CA     . HIS   A  1 224 ? 19.112 -66.838  -38.226 1.00 31.61  ? 216  HIS   A CA     1 
ATOM   1640 C C      . HIS   A  1 224 ? 18.965 -68.125  -37.393 1.00 35.25  ? 216  HIS   A C      1 
ATOM   1641 O O      . HIS   A  1 224 ? 18.406 -68.080  -36.297 1.00 35.65  ? 216  HIS   A O      1 
ATOM   1642 C CB     . HIS   A  1 224 ? 17.942 -66.631  -39.216 1.00 32.15  ? 216  HIS   A CB     1 
ATOM   1643 C CG     . HIS   A  1 224 ? 17.667 -67.781  -40.146 1.00 35.19  ? 216  HIS   A CG     1 
ATOM   1644 N ND1    . HIS   A  1 224 ? 18.257 -67.861  -41.397 1.00 37.14  ? 216  HIS   A ND1    1 
ATOM   1645 C CD2    . HIS   A  1 224 ? 16.824 -68.828  -39.998 1.00 36.17  ? 216  HIS   A CD2    1 
ATOM   1646 C CE1    . HIS   A  1 224 ? 17.775 -68.963  -41.952 1.00 35.91  ? 216  HIS   A CE1    1 
ATOM   1647 N NE2    . HIS   A  1 224 ? 16.912 -69.578  -41.148 1.00 36.12  ? 216  HIS   A NE2    1 
ATOM   1648 N N      . VAL   A  1 225 ? 19.521 -69.247  -37.889 1.00 30.26  ? 217  VAL   A N      1 
ATOM   1649 C CA     . VAL   A  1 225 ? 19.499 -70.539  -37.201 1.00 29.35  ? 217  VAL   A CA     1 
ATOM   1650 C C      . VAL   A  1 225 ? 20.331 -70.444  -35.916 1.00 31.92  ? 217  VAL   A C      1 
ATOM   1651 O O      . VAL   A  1 225 ? 19.884 -70.925  -34.875 1.00 30.90  ? 217  VAL   A O      1 
ATOM   1652 C CB     . VAL   A  1 225 ? 19.954 -71.709  -38.115 1.00 33.47  ? 217  VAL   A CB     1 
ATOM   1653 C CG1    . VAL   A  1 225 ? 19.918 -73.043  -37.368 1.00 33.62  ? 217  VAL   A CG1    1 
ATOM   1654 C CG2    . VAL   A  1 225 ? 19.107 -71.785  -39.381 1.00 33.21  ? 217  VAL   A CG2    1 
ATOM   1655 N N      . ILE   A  1 226 ? 21.520 -69.801  -35.989 1.00 29.08  ? 218  ILE   A N      1 
ATOM   1656 C CA     . ILE   A  1 226 ? 22.395 -69.577  -34.834 1.00 29.13  ? 218  ILE   A CA     1 
ATOM   1657 C C      . ILE   A  1 226 ? 21.685 -68.657  -33.830 1.00 32.29  ? 218  ILE   A C      1 
ATOM   1658 O O      . ILE   A  1 226 ? 21.564 -69.018  -32.664 1.00 31.71  ? 218  ILE   A O      1 
ATOM   1659 C CB     . ILE   A  1 226 ? 23.812 -69.066  -35.265 1.00 32.43  ? 218  ILE   A CB     1 
ATOM   1660 C CG1    . ILE   A  1 226 ? 24.618 -70.205  -35.926 1.00 33.04  ? 218  ILE   A CG1    1 
ATOM   1661 C CG2    . ILE   A  1 226 ? 24.605 -68.455  -34.091 1.00 32.51  ? 218  ILE   A CG2    1 
ATOM   1662 C CD1    . ILE   A  1 226 ? 25.593 -69.775  -36.989 1.00 39.20  ? 218  ILE   A CD1    1 
ATOM   1663 N N      . ASP   A  1 227 ? 21.151 -67.527  -34.302 1.00 29.48  ? 219  ASP   A N      1 
ATOM   1664 C CA     . ASP   A  1 227 ? 20.473 -66.508  -33.478 1.00 29.72  ? 219  ASP   A CA     1 
ATOM   1665 C C      . ASP   A  1 227 ? 19.225 -67.004  -32.702 1.00 31.81  ? 219  ASP   A C      1 
ATOM   1666 O O      . ASP   A  1 227 ? 18.860 -66.379  -31.700 1.00 29.77  ? 219  ASP   A O      1 
ATOM   1667 C CB     . ASP   A  1 227 ? 20.130 -65.269  -34.320 1.00 31.57  ? 219  ASP   A CB     1 
ATOM   1668 C CG     . ASP   A  1 227 ? 21.343 -64.504  -34.859 1.00 44.74  ? 219  ASP   A CG     1 
ATOM   1669 O OD1    . ASP   A  1 227 ? 22.486 -65.013  -34.727 1.00 44.77  ? 219  ASP   A OD1    1 
ATOM   1670 O OD2    . ASP   A  1 227 ? 21.145 -63.422  -35.448 1.00 50.24  ? 219  ASP   A OD2    1 
ATOM   1671 N N      . ARG   A  1 228 ? 18.614 -68.142  -33.119 1.00 28.03  ? 220  ARG   A N      1 
ATOM   1672 C CA     . ARG   A  1 228 ? 17.469 -68.747  -32.413 1.00 27.85  ? 220  ARG   A CA     1 
ATOM   1673 C C      . ARG   A  1 228 ? 17.860 -69.155  -30.986 1.00 31.07  ? 220  ARG   A C      1 
ATOM   1674 O O      . ARG   A  1 228 ? 17.001 -69.244  -30.116 1.00 30.70  ? 220  ARG   A O      1 
ATOM   1675 C CB     . ARG   A  1 228 ? 16.987 -70.034  -33.122 1.00 27.34  ? 220  ARG   A CB     1 
ATOM   1676 C CG     . ARG   A  1 228 ? 16.201 -69.912  -34.420 1.00 35.89  ? 220  ARG   A CG     1 
ATOM   1677 C CD     . ARG   A  1 228 ? 15.116 -68.860  -34.488 1.00 45.51  ? 220  ARG   A CD     1 
ATOM   1678 N NE     . ARG   A  1 228 ? 14.219 -68.819  -33.337 1.00 47.05  ? 220  ARG   A NE     1 
ATOM   1679 C CZ     . ARG   A  1 228 ? 13.039 -69.420  -33.273 1.00 50.21  ? 220  ARG   A CZ     1 
ATOM   1680 N NH1    . ARG   A  1 228 ? 12.614 -70.169  -34.278 1.00 33.61  ? 220  ARG   A NH1    1 
ATOM   1681 N NH2    . ARG   A  1 228 ? 12.273 -69.275  -32.205 1.00 31.96  ? 220  ARG   A NH2    1 
ATOM   1682 N N      . TRP   A  1 229 ? 19.162 -69.418  -30.770 1.00 26.27  ? 221  TRP   A N      1 
ATOM   1683 C CA     . TRP   A  1 229 ? 19.760 -69.894  -29.530 1.00 24.57  ? 221  TRP   A CA     1 
ATOM   1684 C C      . TRP   A  1 229 ? 20.099 -68.798  -28.549 1.00 29.18  ? 221  TRP   A C      1 
ATOM   1685 O O      . TRP   A  1 229 ? 20.525 -69.086  -27.423 1.00 26.31  ? 221  TRP   A O      1 
ATOM   1686 C CB     . TRP   A  1 229 ? 20.980 -70.759  -29.856 1.00 22.15  ? 221  TRP   A CB     1 
ATOM   1687 C CG     . TRP   A  1 229 ? 20.556 -72.016  -30.543 1.00 21.81  ? 221  TRP   A CG     1 
ATOM   1688 C CD1    . TRP   A  1 229 ? 20.543 -72.248  -31.886 1.00 24.51  ? 221  TRP   A CD1    1 
ATOM   1689 C CD2    . TRP   A  1 229 ? 19.860 -73.114  -29.939 1.00 20.98  ? 221  TRP   A CD2    1 
ATOM   1690 N NE1    . TRP   A  1 229 ? 19.972 -73.473  -32.148 1.00 23.36  ? 221  TRP   A NE1    1 
ATOM   1691 C CE2    . TRP   A  1 229 ? 19.539 -74.024  -30.972 1.00 24.32  ? 221  TRP   A CE2    1 
ATOM   1692 C CE3    . TRP   A  1 229 ? 19.513 -73.440  -28.615 1.00 21.46  ? 221  TRP   A CE3    1 
ATOM   1693 C CZ2    . TRP   A  1 229 ? 18.923 -75.255  -30.719 1.00 23.15  ? 221  TRP   A CZ2    1 
ATOM   1694 C CZ3    . TRP   A  1 229 ? 18.898 -74.660  -28.367 1.00 22.19  ? 221  TRP   A CZ3    1 
ATOM   1695 C CH2    . TRP   A  1 229 ? 18.600 -75.545  -29.414 1.00 22.65  ? 221  TRP   A CH2    1 
ATOM   1696 N N      . LEU   A  1 230 ? 19.879 -67.544  -28.976 1.00 27.45  ? 222  LEU   A N      1 
ATOM   1697 C CA     . LEU   A  1 230 ? 20.106 -66.346  -28.183 1.00 27.61  ? 222  LEU   A CA     1 
ATOM   1698 C C      . LEU   A  1 230 ? 19.021 -66.273  -27.141 1.00 28.76  ? 222  LEU   A C      1 
ATOM   1699 O O      . LEU   A  1 230 ? 17.843 -66.477  -27.455 1.00 28.80  ? 222  LEU   A O      1 
ATOM   1700 C CB     . LEU   A  1 230 ? 20.077 -65.090  -29.071 1.00 28.11  ? 222  LEU   A CB     1 
ATOM   1701 C CG     . LEU   A  1 230 ? 21.336 -64.794  -29.879 1.00 34.29  ? 222  LEU   A CG     1 
ATOM   1702 C CD1    . LEU   A  1 230 ? 21.057 -63.733  -30.943 1.00 38.75  ? 222  LEU   A CD1    1 
ATOM   1703 C CD2    . LEU   A  1 230 ? 22.468 -64.302  -28.977 1.00 34.22  ? 222  LEU   A CD2    1 
ATOM   1704 N N      . GLY   A  1 231 ? 19.432 -66.053  -25.905 1.00 22.83  ? 223  GLY   A N      1 
ATOM   1705 C CA     . GLY   A  1 231 ? 18.516 -66.008  -24.776 1.00 21.39  ? 223  GLY   A CA     1 
ATOM   1706 C C      . GLY   A  1 231 ? 18.220 -67.386  -24.238 1.00 22.74  ? 223  GLY   A C      1 
ATOM   1707 O O      . GLY   A  1 231 ? 17.465 -67.516  -23.275 1.00 23.71  ? 223  GLY   A O      1 
ATOM   1708 N N      . GLU   A  1 232 ? 18.819 -68.438  -24.836 1.00 18.71  ? 224  GLU   A N      1 
ATOM   1709 C CA     . GLU   A  1 232 ? 18.609 -69.814  -24.347 1.00 16.50  ? 224  GLU   A CA     1 
ATOM   1710 C C      . GLU   A  1 232 ? 19.610 -70.183  -23.263 1.00 20.45  ? 224  GLU   A C      1 
ATOM   1711 O O      . GLU   A  1 232 ? 20.738 -69.681  -23.308 1.00 18.61  ? 224  GLU   A O      1 
ATOM   1712 C CB     . GLU   A  1 232 ? 18.629 -70.846  -25.492 1.00 17.32  ? 224  GLU   A CB     1 
ATOM   1713 C CG     . GLU   A  1 232 ? 17.451 -70.707  -26.442 1.00 24.06  ? 224  GLU   A CG     1 
ATOM   1714 C CD     . GLU   A  1 232 ? 16.061 -70.880  -25.849 1.00 32.00  ? 224  GLU   A CD     1 
ATOM   1715 O OE1    . GLU   A  1 232 ? 15.920 -71.328  -24.688 1.00 20.33  ? 224  GLU   A OE1    1 
ATOM   1716 O OE2    . GLU   A  1 232 ? 15.097 -70.643  -26.599 1.00 25.86  ? 224  GLU   A OE2    1 
ATOM   1717 N N      . PRO   A  1 233 ? 19.234 -71.056  -22.283 1.00 18.70  ? 225  PRO   A N      1 
ATOM   1718 C CA     . PRO   A  1 233 ? 20.191 -71.425  -21.219 1.00 19.25  ? 225  PRO   A CA     1 
ATOM   1719 C C      . PRO   A  1 233 ? 21.283 -72.402  -21.705 1.00 23.52  ? 225  PRO   A C      1 
ATOM   1720 O O      . PRO   A  1 233 ? 21.238 -73.593  -21.400 1.00 23.23  ? 225  PRO   A O      1 
ATOM   1721 C CB     . PRO   A  1 233 ? 19.281 -72.041  -20.140 1.00 20.25  ? 225  PRO   A CB     1 
ATOM   1722 C CG     . PRO   A  1 233 ? 18.178 -72.703  -20.961 1.00 24.12  ? 225  PRO   A CG     1 
ATOM   1723 C CD     . PRO   A  1 233 ? 17.925 -71.727  -22.082 1.00 19.90  ? 225  PRO   A CD     1 
ATOM   1724 N N      . ILE   A  1 234 ? 22.266 -71.896  -22.461 1.00 21.30  ? 226  ILE   A N      1 
ATOM   1725 C CA     . ILE   A  1 234 ? 23.360 -72.733  -22.971 1.00 21.07  ? 226  ILE   A CA     1 
ATOM   1726 C C      . ILE   A  1 234 ? 24.429 -72.891  -21.895 1.00 24.99  ? 226  ILE   A C      1 
ATOM   1727 O O      . ILE   A  1 234 ? 25.095 -71.919  -21.530 1.00 24.73  ? 226  ILE   A O      1 
ATOM   1728 C CB     . ILE   A  1 234 ? 23.926 -72.211  -24.328 1.00 24.76  ? 226  ILE   A CB     1 
ATOM   1729 C CG1    . ILE   A  1 234 ? 22.792 -72.059  -25.386 1.00 25.47  ? 226  ILE   A CG1    1 
ATOM   1730 C CG2    . ILE   A  1 234 ? 25.060 -73.131  -24.850 1.00 25.01  ? 226  ILE   A CG2    1 
ATOM   1731 C CD1    . ILE   A  1 234 ? 23.085 -71.043  -26.467 1.00 38.97  ? 226  ILE   A CD1    1 
ATOM   1732 N N      . LYS   A  1 235 ? 24.576 -74.109  -21.367 1.00 21.45  ? 227  LYS   A N      1 
ATOM   1733 C CA     . LYS   A  1 235 ? 25.596 -74.379  -20.351 1.00 21.05  ? 227  LYS   A CA     1 
ATOM   1734 C C      . LYS   A  1 235 ? 26.857 -74.980  -20.965 1.00 24.99  ? 227  LYS   A C      1 
ATOM   1735 O O      . LYS   A  1 235 ? 27.961 -74.787  -20.448 1.00 24.18  ? 227  LYS   A O      1 
ATOM   1736 C CB     . LYS   A  1 235 ? 25.040 -75.270  -19.221 1.00 23.14  ? 227  LYS   A CB     1 
ATOM   1737 C CG     . LYS   A  1 235 ? 24.181 -74.501  -18.215 1.00 29.00  ? 227  LYS   A CG     1 
ATOM   1738 C CD     . LYS   A  1 235 ? 24.963 -73.442  -17.431 1.00 37.98  ? 227  LYS   A CD     1 
ATOM   1739 C CE     . LYS   A  1 235 ? 24.048 -72.442  -16.767 1.00 51.46  ? 227  LYS   A CE     1 
ATOM   1740 N NZ     . LYS   A  1 235 ? 24.811 -71.404  -16.022 1.00 61.96  ? 227  LYS   A NZ     1 
ATOM   1741 N N      . ALA   A  1 236 ? 26.690 -75.710  -22.064 1.00 22.19  ? 228  ALA   A N      1 
ATOM   1742 C CA     . ALA   A  1 236 ? 27.810 -76.352  -22.734 1.00 22.37  ? 228  ALA   A CA     1 
ATOM   1743 C C      . ALA   A  1 236 ? 27.757 -76.211  -24.229 1.00 26.07  ? 228  ALA   A C      1 
ATOM   1744 O O      . ALA   A  1 236 ? 26.679 -76.114  -24.809 1.00 26.04  ? 228  ALA   A O      1 
ATOM   1745 C CB     . ALA   A  1 236 ? 27.886 -77.825  -22.348 1.00 22.95  ? 228  ALA   A CB     1 
ATOM   1746 N N      . ALA   A  1 237 ? 28.936 -76.198  -24.859 1.00 23.49  ? 229  ALA   A N      1 
ATOM   1747 C CA     . ALA   A  1 237 ? 29.097 -76.187  -26.311 1.00 22.86  ? 229  ALA   A CA     1 
ATOM   1748 C C      . ALA   A  1 237 ? 29.965 -77.422  -26.659 1.00 26.26  ? 229  ALA   A C      1 
ATOM   1749 O O      . ALA   A  1 237 ? 31.042 -77.599  -26.089 1.00 24.85  ? 229  ALA   A O      1 
ATOM   1750 C CB     . ALA   A  1 237 ? 29.767 -74.899  -26.763 1.00 23.46  ? 229  ALA   A CB     1 
ATOM   1751 N N      . ILE   A  1 238 ? 29.450 -78.302  -27.524 1.00 22.27  ? 230  ILE   A N      1 
ATOM   1752 C CA     . ILE   A  1 238 ? 30.091 -79.550  -27.931 1.00 22.09  ? 230  ILE   A CA     1 
ATOM   1753 C C      . ILE   A  1 238 ? 30.802 -79.366  -29.267 1.00 28.66  ? 230  ILE   A C      1 
ATOM   1754 O O      . ILE   A  1 238 ? 30.167 -79.082  -30.280 1.00 28.44  ? 230  ILE   A O      1 
ATOM   1755 C CB     . ILE   A  1 238 ? 29.089 -80.737  -27.932 1.00 24.54  ? 230  ILE   A CB     1 
ATOM   1756 C CG1    . ILE   A  1 238 ? 28.547 -80.989  -26.516 1.00 24.80  ? 230  ILE   A CG1    1 
ATOM   1757 C CG2    . ILE   A  1 238 ? 29.736 -82.014  -28.511 1.00 24.78  ? 230  ILE   A CG2    1 
ATOM   1758 C CD1    . ILE   A  1 238 ? 27.380 -81.939  -26.410 1.00 29.19  ? 230  ILE   A CD1    1 
ATOM   1759 N N      . LEU   A  1 239 ? 32.137 -79.503  -29.238 1.00 26.31  ? 231  LEU   A N      1 
ATOM   1760 C CA     . LEU   A  1 239 ? 33.032 -79.338  -30.375 1.00 25.81  ? 231  LEU   A CA     1 
ATOM   1761 C C      . LEU   A  1 239 ? 33.633 -80.666  -30.822 1.00 29.25  ? 231  LEU   A C      1 
ATOM   1762 O O      . LEU   A  1 239 ? 34.582 -81.156  -30.198 1.00 28.84  ? 231  LEU   A O      1 
ATOM   1763 C CB     . LEU   A  1 239 ? 34.148 -78.320  -30.068 1.00 26.30  ? 231  LEU   A CB     1 
ATOM   1764 C CG     . LEU   A  1 239 ? 33.727 -76.918  -29.603 1.00 31.92  ? 231  LEU   A CG     1 
ATOM   1765 C CD1    . LEU   A  1 239 ? 34.942 -76.079  -29.306 1.00 32.49  ? 231  LEU   A CD1    1 
ATOM   1766 C CD2    . LEU   A  1 239 ? 32.845 -76.217  -30.637 1.00 34.42  ? 231  LEU   A CD2    1 
ATOM   1767 N N      . PRO   A  1 240 ? 33.086 -81.281  -31.895 1.00 25.64  ? 232  PRO   A N      1 
ATOM   1768 C CA     . PRO   A  1 240 ? 33.685 -82.521  -32.406 1.00 25.27  ? 232  PRO   A CA     1 
ATOM   1769 C C      . PRO   A  1 240 ? 35.016 -82.201  -33.066 1.00 27.28  ? 232  PRO   A C      1 
ATOM   1770 O O      . PRO   A  1 240 ? 35.153 -81.164  -33.705 1.00 24.50  ? 232  PRO   A O      1 
ATOM   1771 C CB     . PRO   A  1 240 ? 32.651 -83.040  -33.419 1.00 26.86  ? 232  PRO   A CB     1 
ATOM   1772 C CG     . PRO   A  1 240 ? 31.448 -82.148  -33.262 1.00 31.61  ? 232  PRO   A CG     1 
ATOM   1773 C CD     . PRO   A  1 240 ? 31.969 -80.850  -32.750 1.00 26.90  ? 232  PRO   A CD     1 
ATOM   1774 N N      . THR   A  1 241 ? 36.008 -83.068  -32.853 1.00 26.40  ? 233  THR   A N      1 
ATOM   1775 C CA     . THR   A  1 241 ? 37.362 -82.939  -33.414 1.00 26.70  ? 233  THR   A CA     1 
ATOM   1776 C C      . THR   A  1 241 ? 37.335 -82.809  -34.950 1.00 31.71  ? 233  THR   A C      1 
ATOM   1777 O O      . THR   A  1 241 ? 38.177 -82.114  -35.512 1.00 31.38  ? 233  THR   A O      1 
ATOM   1778 C CB     . THR   A  1 241 ? 38.210 -84.136  -33.002 1.00 27.84  ? 233  THR   A CB     1 
ATOM   1779 O OG1    . THR   A  1 241 ? 37.540 -85.315  -33.419 1.00 25.13  ? 233  THR   A OG1    1 
ATOM   1780 C CG2    . THR   A  1 241 ? 38.461 -84.192  -31.512 1.00 27.27  ? 233  THR   A CG2    1 
ATOM   1781 N N      . SER   A  1 242 ? 36.332 -83.434  -35.605 1.00 29.75  ? 234  SER   A N      1 
ATOM   1782 C CA     . SER   A  1 242 ? 36.121 -83.434  -37.057 1.00 30.37  ? 234  SER   A CA     1 
ATOM   1783 C C      . SER   A  1 242 ? 35.801 -82.057  -37.671 1.00 34.90  ? 234  SER   A C      1 
ATOM   1784 O O      . SER   A  1 242 ? 35.882 -81.919  -38.891 1.00 35.14  ? 234  SER   A O      1 
ATOM   1785 C CB     . SER   A  1 242 ? 35.035 -84.438  -37.433 1.00 34.27  ? 234  SER   A CB     1 
ATOM   1786 O OG     . SER   A  1 242 ? 33.771 -84.029  -36.935 1.00 43.22  ? 234  SER   A OG     1 
ATOM   1787 N N      . ILE   A  1 243 ? 35.419 -81.054  -36.849 1.00 31.31  ? 235  ILE   A N      1 
ATOM   1788 C CA     . ILE   A  1 243 ? 35.085 -79.707  -37.339 1.00 30.81  ? 235  ILE   A CA     1 
ATOM   1789 C C      . ILE   A  1 243 ? 36.351 -78.843  -37.455 1.00 34.78  ? 235  ILE   A C      1 
ATOM   1790 O O      . ILE   A  1 243 ? 36.314 -77.758  -38.032 1.00 33.94  ? 235  ILE   A O      1 
ATOM   1791 C CB     . ILE   A  1 243 ? 33.952 -79.012  -36.505 1.00 33.49  ? 235  ILE   A CB     1 
ATOM   1792 C CG1    . ILE   A  1 243 ? 34.489 -78.393  -35.187 1.00 33.53  ? 235  ILE   A CG1    1 
ATOM   1793 C CG2    . ILE   A  1 243 ? 32.776 -79.967  -36.257 1.00 33.90  ? 235  ILE   A CG2    1 
ATOM   1794 C CD1    . ILE   A  1 243 ? 33.606 -77.310  -34.540 1.00 40.88  ? 235  ILE   A CD1    1 
ATOM   1795 N N      . PHE   A  1 244 ? 37.453 -79.313  -36.869 1.00 31.74  ? 236  PHE   A N      1 
ATOM   1796 C CA     . PHE   A  1 244 ? 38.712 -78.587  -36.891 1.00 32.18  ? 236  PHE   A CA     1 
ATOM   1797 C C      . PHE   A  1 244 ? 39.457 -78.770  -38.206 1.00 40.44  ? 236  PHE   A C      1 
ATOM   1798 O O      . PHE   A  1 244 ? 39.636 -79.894  -38.668 1.00 40.66  ? 236  PHE   A O      1 
ATOM   1799 C CB     . PHE   A  1 244 ? 39.599 -79.006  -35.718 1.00 33.12  ? 236  PHE   A CB     1 
ATOM   1800 C CG     . PHE   A  1 244 ? 39.160 -78.469  -34.380 1.00 33.64  ? 236  PHE   A CG     1 
ATOM   1801 C CD1    . PHE   A  1 244 ? 38.138 -79.087  -33.664 1.00 35.91  ? 236  PHE   A CD1    1 
ATOM   1802 C CD2    . PHE   A  1 244 ? 39.794 -77.370  -33.814 1.00 35.53  ? 236  PHE   A CD2    1 
ATOM   1803 C CE1    . PHE   A  1 244 ? 37.742 -78.598  -32.418 1.00 36.67  ? 236  PHE   A CE1    1 
ATOM   1804 C CE2    . PHE   A  1 244 ? 39.394 -76.878  -32.570 1.00 38.30  ? 236  PHE   A CE2    1 
ATOM   1805 C CZ     . PHE   A  1 244 ? 38.374 -77.499  -31.878 1.00 36.22  ? 236  PHE   A CZ     1 
ATOM   1806 N N      . LEU   A  1 245 ? 39.893 -77.655  -38.801 1.00 40.06  ? 237  LEU   A N      1 
ATOM   1807 C CA     . LEU   A  1 245 ? 40.703 -77.639  -40.018 1.00 41.21  ? 237  LEU   A CA     1 
ATOM   1808 C C      . LEU   A  1 245 ? 42.160 -77.836  -39.586 1.00 48.08  ? 237  LEU   A C      1 
ATOM   1809 O O      . LEU   A  1 245 ? 42.457 -77.835  -38.387 1.00 47.97  ? 237  LEU   A O      1 
ATOM   1810 C CB     . LEU   A  1 245 ? 40.567 -76.291  -40.763 1.00 41.16  ? 237  LEU   A CB     1 
ATOM   1811 C CG     . LEU   A  1 245 ? 39.175 -75.817  -41.181 1.00 45.34  ? 237  LEU   A CG     1 
ATOM   1812 C CD1    . LEU   A  1 245 ? 39.211 -74.355  -41.541 1.00 45.25  ? 237  LEU   A CD1    1 
ATOM   1813 C CD2    . LEU   A  1 245 ? 38.637 -76.620  -42.349 1.00 47.16  ? 237  LEU   A CD2    1 
ATOM   1814 N N      . THR   A  1 246 ? 43.069 -77.985  -40.554 1.00 46.96  ? 238  THR   A N      1 
ATOM   1815 C CA     . THR   A  1 246 ? 44.493 -78.168  -40.271 1.00 47.47  ? 238  THR   A CA     1 
ATOM   1816 C C      . THR   A  1 246 ? 45.295 -77.014  -40.876 1.00 52.95  ? 238  THR   A C      1 
ATOM   1817 O O      . THR   A  1 246 ? 44.986 -76.557  -41.981 1.00 52.43  ? 238  THR   A O      1 
ATOM   1818 C CB     . THR   A  1 246 ? 44.954 -79.547  -40.771 1.00 56.26  ? 238  THR   A CB     1 
ATOM   1819 O OG1    . THR   A  1 246 ? 43.974 -80.530  -40.430 1.00 57.30  ? 238  THR   A OG1    1 
ATOM   1820 C CG2    . THR   A  1 246 ? 46.288 -79.961  -40.194 1.00 54.46  ? 238  THR   A CG2    1 
ATOM   1821 N N      . ASN   A  1 247 ? 46.302 -76.528  -40.143 1.00 51.12  ? 239  ASN   A N      1 
ATOM   1822 C CA     . ASN   A  1 247 ? 47.170 -75.464  -40.637 1.00 51.88  ? 239  ASN   A CA     1 
ATOM   1823 C C      . ASN   A  1 247 ? 48.460 -76.059  -41.244 1.00 58.81  ? 239  ASN   A C      1 
ATOM   1824 O O      . ASN   A  1 247 ? 48.629 -77.285  -41.236 1.00 58.05  ? 239  ASN   A O      1 
ATOM   1825 C CB     . ASN   A  1 247 ? 47.443 -74.402  -39.550 1.00 50.17  ? 239  ASN   A CB     1 
ATOM   1826 C CG     . ASN   A  1 247 ? 48.263 -74.824  -38.348 1.00 58.17  ? 239  ASN   A CG     1 
ATOM   1827 O OD1    . ASN   A  1 247 ? 48.666 -75.979  -38.179 1.00 51.70  ? 239  ASN   A OD1    1 
ATOM   1828 N ND2    . ASN   A  1 247 ? 48.527 -73.870  -37.473 1.00 44.12  ? 239  ASN   A ND2    1 
ATOM   1829 N N      . LYS   A  1 248 ? 49.358 -75.194  -41.767 1.00 57.52  ? 240  LYS   A N      1 
ATOM   1830 C CA     . LYS   A  1 248 ? 50.644 -75.575  -42.373 1.00 58.01  ? 240  LYS   A CA     1 
ATOM   1831 C C      . LYS   A  1 248 ? 51.526 -76.430  -41.450 1.00 62.57  ? 240  LYS   A C      1 
ATOM   1832 O O      . LYS   A  1 248 ? 52.251 -77.300  -41.936 1.00 62.77  ? 240  LYS   A O      1 
ATOM   1833 C CB     . LYS   A  1 248 ? 51.415 -74.336  -42.882 1.00 61.07  ? 240  LYS   A CB     1 
ATOM   1834 C CG     . LYS   A  1 248 ? 51.680 -73.257  -41.826 1.00 77.25  ? 240  LYS   A CG     1 
ATOM   1835 C CD     . LYS   A  1 248 ? 52.507 -72.102  -42.376 1.00 87.32  ? 240  LYS   A CD     1 
ATOM   1836 C CE     . LYS   A  1 248 ? 52.666 -70.981  -41.375 1.00 98.16  ? 240  LYS   A CE     1 
ATOM   1837 N NZ     . LYS   A  1 248 ? 53.548 -71.358  -40.237 1.00 106.33 ? 240  LYS   A NZ     1 
ATOM   1838 N N      . LYS   A  1 249 ? 51.439 -76.191  -40.127 1.00 58.77  ? 241  LYS   A N      1 
ATOM   1839 C CA     . LYS   A  1 249 ? 52.207 -76.897  -39.098 1.00 58.49  ? 241  LYS   A CA     1 
ATOM   1840 C C      . LYS   A  1 249 ? 51.546 -78.208  -38.629 1.00 61.21  ? 241  LYS   A C      1 
ATOM   1841 O O      . LYS   A  1 249 ? 52.156 -78.958  -37.865 1.00 60.89  ? 241  LYS   A O      1 
ATOM   1842 C CB     . LYS   A  1 249 ? 52.501 -75.964  -37.909 1.00 61.53  ? 241  LYS   A CB     1 
ATOM   1843 C CG     . LYS   A  1 249 ? 53.271 -74.693  -38.275 1.00 79.91  ? 241  LYS   A CG     1 
ATOM   1844 C CD     . LYS   A  1 249 ? 53.057 -73.571  -37.255 1.00 92.91  ? 241  LYS   A CD     1 
ATOM   1845 C CE     . LYS   A  1 249 ? 51.817 -72.742  -37.526 1.00 104.31 ? 241  LYS   A CE     1 
ATOM   1846 N NZ     . LYS   A  1 249 ? 51.598 -71.716  -36.472 1.00 114.01 ? 241  LYS   A NZ     1 
ATOM   1847 N N      . GLY   A  1 250 ? 50.322 -78.470  -39.091 1.00 57.23  ? 242  GLY   A N      1 
ATOM   1848 C CA     . GLY   A  1 250 ? 49.575 -79.683  -38.764 1.00 56.64  ? 242  GLY   A CA     1 
ATOM   1849 C C      . GLY   A  1 250 ? 48.724 -79.635  -37.505 1.00 58.83  ? 242  GLY   A C      1 
ATOM   1850 O O      . GLY   A  1 250 ? 48.175 -80.662  -37.090 1.00 57.99  ? 242  GLY   A O      1 
ATOM   1851 N N      . PHE   A  1 251 ? 48.610 -78.446  -36.887 1.00 53.99  ? 243  PHE   A N      1 
ATOM   1852 C CA     . PHE   A  1 251 ? 47.840 -78.206  -35.663 1.00 52.79  ? 243  PHE   A CA     1 
ATOM   1853 C C      . PHE   A  1 251 ? 46.344 -77.986  -35.970 1.00 50.76  ? 243  PHE   A C      1 
ATOM   1854 O O      . PHE   A  1 251 ? 46.030 -77.389  -37.005 1.00 49.75  ? 243  PHE   A O      1 
ATOM   1855 C CB     . PHE   A  1 251 ? 48.399 -76.979  -34.922 1.00 55.39  ? 243  PHE   A CB     1 
ATOM   1856 C CG     . PHE   A  1 251 ? 49.714 -77.178  -34.203 1.00 58.00  ? 243  PHE   A CG     1 
ATOM   1857 C CD1    . PHE   A  1 251 ? 50.919 -77.127  -34.895 1.00 61.66  ? 243  PHE   A CD1    1 
ATOM   1858 C CD2    . PHE   A  1 251 ? 49.753 -77.339  -32.823 1.00 61.42  ? 243  PHE   A CD2    1 
ATOM   1859 C CE1    . PHE   A  1 251 ? 52.138 -77.281  -34.226 1.00 62.76  ? 243  PHE   A CE1    1 
ATOM   1860 C CE2    . PHE   A  1 251 ? 50.974 -77.485  -32.152 1.00 64.65  ? 243  PHE   A CE2    1 
ATOM   1861 C CZ     . PHE   A  1 251 ? 52.158 -77.455  -32.860 1.00 62.45  ? 243  PHE   A CZ     1 
ATOM   1862 N N      . PRO   A  1 252 ? 45.404 -78.427  -35.090 1.00 43.69  ? 244  PRO   A N      1 
ATOM   1863 C CA     . PRO   A  1 252 ? 43.977 -78.190  -35.373 1.00 41.80  ? 244  PRO   A CA     1 
ATOM   1864 C C      . PRO   A  1 252 ? 43.575 -76.730  -35.177 1.00 42.55  ? 244  PRO   A C      1 
ATOM   1865 O O      . PRO   A  1 252 ? 43.986 -76.094  -34.205 1.00 42.03  ? 244  PRO   A O      1 
ATOM   1866 C CB     . PRO   A  1 252 ? 43.262 -79.119  -34.400 1.00 43.43  ? 244  PRO   A CB     1 
ATOM   1867 C CG     . PRO   A  1 252 ? 44.191 -79.275  -33.268 1.00 48.25  ? 244  PRO   A CG     1 
ATOM   1868 C CD     . PRO   A  1 252 ? 45.585 -79.154  -33.816 1.00 44.39  ? 244  PRO   A CD     1 
ATOM   1869 N N      . VAL   A  1 253 ? 42.825 -76.184  -36.140 1.00 37.18  ? 245  VAL   A N      1 
ATOM   1870 C CA     . VAL   A  1 253 ? 42.348 -74.794  -36.118 1.00 36.22  ? 245  VAL   A CA     1 
ATOM   1871 C C      . VAL   A  1 253 ? 40.863 -74.743  -36.498 1.00 38.39  ? 245  VAL   A C      1 
ATOM   1872 O O      . VAL   A  1 253 ? 40.295 -75.754  -36.892 1.00 38.39  ? 245  VAL   A O      1 
ATOM   1873 C CB     . VAL   A  1 253 ? 43.207 -73.834  -37.009 1.00 39.66  ? 245  VAL   A CB     1 
ATOM   1874 C CG1    . VAL   A  1 253 ? 44.594 -73.599  -36.417 1.00 39.09  ? 245  VAL   A CG1    1 
ATOM   1875 C CG2    . VAL   A  1 253 ? 43.300 -74.325  -38.452 1.00 39.54  ? 245  VAL   A CG2    1 
ATOM   1876 N N      . LEU   A  1 254 ? 40.243 -73.577  -36.405 1.00 33.83  ? 246  LEU   A N      1 
ATOM   1877 C CA     . LEU   A  1 254 ? 38.849 -73.437  -36.802 1.00 33.38  ? 246  LEU   A CA     1 
ATOM   1878 C C      . LEU   A  1 254 ? 38.755 -72.366  -37.862 1.00 36.91  ? 246  LEU   A C      1 
ATOM   1879 O O      . LEU   A  1 254 ? 39.574 -71.449  -37.864 1.00 36.15  ? 246  LEU   A O      1 
ATOM   1880 C CB     . LEU   A  1 254 ? 37.952 -73.078  -35.590 1.00 32.92  ? 246  LEU   A CB     1 
ATOM   1881 C CG     . LEU   A  1 254 ? 37.681 -74.186  -34.556 1.00 36.51  ? 246  LEU   A CG     1 
ATOM   1882 C CD1    . LEU   A  1 254 ? 37.109 -73.605  -33.267 1.00 36.49  ? 246  LEU   A CD1    1 
ATOM   1883 C CD2    . LEU   A  1 254 ? 36.746 -75.244  -35.098 1.00 36.24  ? 246  LEU   A CD2    1 
ATOM   1884 N N      . SER   A  1 255 ? 37.750 -72.458  -38.744 1.00 34.46  ? 247  SER   A N      1 
ATOM   1885 C CA     . SER   A  1 255 ? 37.498 -71.438  -39.763 1.00 35.24  ? 247  SER   A CA     1 
ATOM   1886 C C      . SER   A  1 255 ? 37.104 -70.113  -39.069 1.00 41.12  ? 247  SER   A C      1 
ATOM   1887 O O      . SER   A  1 255 ? 36.708 -70.132  -37.897 1.00 40.37  ? 247  SER   A O      1 
ATOM   1888 C CB     . SER   A  1 255 ? 36.380 -71.893  -40.698 1.00 39.16  ? 247  SER   A CB     1 
ATOM   1889 O OG     . SER   A  1 255 ? 35.096 -71.638  -40.151 1.00 46.83  ? 247  SER   A OG     1 
ATOM   1890 N N      . LYS   A  1 256 ? 37.202 -68.973  -39.785 1.00 38.88  ? 248  LYS   A N      1 
ATOM   1891 C CA     . LYS   A  1 256 ? 36.833 -67.664  -39.234 1.00 39.11  ? 248  LYS   A CA     1 
ATOM   1892 C C      . LYS   A  1 256 ? 35.394 -67.634  -38.696 1.00 42.51  ? 248  LYS   A C      1 
ATOM   1893 O O      . LYS   A  1 256 ? 35.153 -67.031  -37.652 1.00 41.57  ? 248  LYS   A O      1 
ATOM   1894 C CB     . LYS   A  1 256 ? 37.067 -66.525  -40.251 1.00 42.02  ? 248  LYS   A CB     1 
ATOM   1895 C CG     . LYS   A  1 256 ? 38.546 -66.152  -40.475 1.00 59.75  ? 248  LYS   A CG     1 
ATOM   1896 C CD     . LYS   A  1 256 ? 39.189 -65.356  -39.321 1.00 72.20  ? 248  LYS   A CD     1 
ATOM   1897 C CE     . LYS   A  1 256 ? 38.918 -63.867  -39.373 1.00 85.70  ? 248  LYS   A CE     1 
ATOM   1898 N NZ     . LYS   A  1 256 ? 39.595 -63.144  -38.261 1.00 95.14  ? 248  LYS   A NZ     1 
ATOM   1899 N N      . MET   A  1 257 ? 34.459 -68.311  -39.385 1.00 40.05  ? 249  MET   A N      1 
ATOM   1900 C CA     . MET   A  1 257 ? 33.060 -68.383  -38.968 1.00 40.82  ? 249  MET   A CA     1 
ATOM   1901 C C      . MET   A  1 257 ? 32.878 -69.156  -37.662 1.00 41.07  ? 249  MET   A C      1 
ATOM   1902 O O      . MET   A  1 257 ? 32.063 -68.752  -36.831 1.00 40.00  ? 249  MET   A O      1 
ATOM   1903 C CB     . MET   A  1 257 ? 32.173 -68.931  -40.085 1.00 44.44  ? 249  MET   A CB     1 
ATOM   1904 C CG     . MET   A  1 257 ? 31.722 -67.842  -41.030 1.00 50.39  ? 249  MET   A CG     1 
ATOM   1905 S SD     . MET   A  1 257 ? 30.739 -68.437  -42.423 1.00 57.05  ? 249  MET   A SD     1 
ATOM   1906 C CE     . MET   A  1 257 ? 30.351 -66.861  -43.226 1.00 53.78  ? 249  MET   A CE     1 
ATOM   1907 N N      . HIS   A  1 258 ? 33.675 -70.225  -37.463 1.00 35.48  ? 250  HIS   A N      1 
ATOM   1908 C CA     . HIS   A  1 258 ? 33.649 -71.050  -36.251 1.00 34.35  ? 250  HIS   A CA     1 
ATOM   1909 C C      . HIS   A  1 258 ? 34.206 -70.293  -35.068 1.00 38.25  ? 250  HIS   A C      1 
ATOM   1910 O O      . HIS   A  1 258 ? 33.620 -70.345  -33.989 1.00 38.00  ? 250  HIS   A O      1 
ATOM   1911 C CB     . HIS   A  1 258 ? 34.363 -72.385  -36.464 1.00 34.49  ? 250  HIS   A CB     1 
ATOM   1912 C CG     . HIS   A  1 258 ? 33.531 -73.371  -37.227 1.00 37.79  ? 250  HIS   A CG     1 
ATOM   1913 N ND1    . HIS   A  1 258 ? 32.707 -74.275  -36.579 1.00 39.60  ? 250  HIS   A ND1    1 
ATOM   1914 C CD2    . HIS   A  1 258 ? 33.397 -73.539  -38.561 1.00 39.21  ? 250  HIS   A CD2    1 
ATOM   1915 C CE1    . HIS   A  1 258 ? 32.120 -74.972  -37.537 1.00 38.67  ? 250  HIS   A CE1    1 
ATOM   1916 N NE2    . HIS   A  1 258 ? 32.502 -74.563  -38.745 1.00 38.90  ? 250  HIS   A NE2    1 
ATOM   1917 N N      . GLN   A  1 259 ? 35.289 -69.527  -35.295 1.00 34.69  ? 251  GLN   A N      1 
ATOM   1918 C CA     . GLN   A  1 259 ? 35.946 -68.685  -34.307 1.00 34.29  ? 251  GLN   A CA     1 
ATOM   1919 C C      . GLN   A  1 259 ? 34.978 -67.619  -33.815 1.00 38.38  ? 251  GLN   A C      1 
ATOM   1920 O O      . GLN   A  1 259 ? 34.929 -67.360  -32.614 1.00 37.68  ? 251  GLN   A O      1 
ATOM   1921 C CB     . GLN   A  1 259 ? 37.197 -68.025  -34.903 1.00 35.37  ? 251  GLN   A CB     1 
ATOM   1922 C CG     . GLN   A  1 259 ? 38.382 -68.967  -35.094 1.00 45.79  ? 251  GLN   A CG     1 
ATOM   1923 C CD     . GLN   A  1 259 ? 39.513 -68.272  -35.812 1.00 61.28  ? 251  GLN   A CD     1 
ATOM   1924 O OE1    . GLN   A  1 259 ? 39.971 -67.199  -35.412 1.00 55.43  ? 251  GLN   A OE1    1 
ATOM   1925 N NE2    . GLN   A  1 259 ? 39.979 -68.855  -36.905 1.00 54.60  ? 251  GLN   A NE2    1 
ATOM   1926 N N      . ARG   A  1 260 ? 34.183 -67.033  -34.738 1.00 35.73  ? 252  ARG   A N      1 
ATOM   1927 C CA     . ARG   A  1 260 ? 33.175 -66.015  -34.433 1.00 35.86  ? 252  ARG   A CA     1 
ATOM   1928 C C      . ARG   A  1 260 ? 32.149 -66.559  -33.435 1.00 37.22  ? 252  ARG   A C      1 
ATOM   1929 O O      . ARG   A  1 260 ? 31.833 -65.877  -32.461 1.00 36.45  ? 252  ARG   A O      1 
ATOM   1930 C CB     . ARG   A  1 260 ? 32.474 -65.542  -35.710 1.00 39.07  ? 252  ARG   A CB     1 
ATOM   1931 C CG     . ARG   A  1 260 ? 33.263 -64.500  -36.498 1.00 56.19  ? 252  ARG   A CG     1 
ATOM   1932 C CD     . ARG   A  1 260 ? 32.739 -64.419  -37.919 1.00 72.67  ? 252  ARG   A CD     1 
ATOM   1933 N NE     . ARG   A  1 260 ? 33.599 -63.622  -38.796 1.00 81.88  ? 252  ARG   A NE     1 
ATOM   1934 C CZ     . ARG   A  1 260 ? 33.562 -63.675  -40.124 1.00 96.32  ? 252  ARG   A CZ     1 
ATOM   1935 N NH1    . ARG   A  1 260 ? 32.719 -64.495  -40.741 1.00 80.12  ? 252  ARG   A NH1    1 
ATOM   1936 N NH2    . ARG   A  1 260 ? 34.376 -62.917  -40.846 1.00 86.29  ? 252  ARG   A NH2    1 
ATOM   1937 N N      . LEU   A  1 261 ? 31.669 -67.796  -33.664 1.00 32.37  ? 253  LEU   A N      1 
ATOM   1938 C CA     . LEU   A  1 261 ? 30.734 -68.473  -32.774 1.00 31.67  ? 253  LEU   A CA     1 
ATOM   1939 C C      . LEU   A  1 261 ? 31.380 -68.766  -31.411 1.00 35.06  ? 253  LEU   A C      1 
ATOM   1940 O O      . LEU   A  1 261 ? 30.714 -68.583  -30.395 1.00 34.48  ? 253  LEU   A O      1 
ATOM   1941 C CB     . LEU   A  1 261 ? 30.156 -69.744  -33.427 1.00 31.44  ? 253  LEU   A CB     1 
ATOM   1942 C CG     . LEU   A  1 261 ? 29.093 -70.529  -32.639 1.00 35.88  ? 253  LEU   A CG     1 
ATOM   1943 C CD1    . LEU   A  1 261 ? 27.899 -69.656  -32.251 1.00 35.75  ? 253  LEU   A CD1    1 
ATOM   1944 C CD2    . LEU   A  1 261 ? 28.627 -71.741  -33.410 1.00 37.69  ? 253  LEU   A CD2    1 
ATOM   1945 N N      . ILE   A  1 262 ? 32.674 -69.181  -31.382 1.00 31.51  ? 254  ILE   A N      1 
ATOM   1946 C CA     . ILE   A  1 262 ? 33.411 -69.444  -30.134 1.00 31.02  ? 254  ILE   A CA     1 
ATOM   1947 C C      . ILE   A  1 262 ? 33.422 -68.186  -29.254 1.00 35.27  ? 254  ILE   A C      1 
ATOM   1948 O O      . ILE   A  1 262 ? 33.075 -68.278  -28.082 1.00 35.23  ? 254  ILE   A O      1 
ATOM   1949 C CB     . ILE   A  1 262 ? 34.840 -70.021  -30.378 1.00 33.84  ? 254  ILE   A CB     1 
ATOM   1950 C CG1    . ILE   A  1 262 ? 34.822 -71.396  -31.114 1.00 33.99  ? 254  ILE   A CG1    1 
ATOM   1951 C CG2    . ILE   A  1 262 ? 35.682 -70.084  -29.092 1.00 34.09  ? 254  ILE   A CG2    1 
ATOM   1952 C CD1    . ILE   A  1 262 ? 34.023 -72.570  -30.487 1.00 38.69  ? 254  ILE   A CD1    1 
ATOM   1953 N N      . PHE   A  1 263 ? 33.767 -67.015  -29.831 1.00 32.93  ? 255  PHE   A N      1 
ATOM   1954 C CA     . PHE   A  1 263 ? 33.783 -65.736  -29.118 1.00 33.41  ? 255  PHE   A CA     1 
ATOM   1955 C C      . PHE   A  1 263 ? 32.399 -65.369  -28.571 1.00 37.21  ? 255  PHE   A C      1 
ATOM   1956 O O      . PHE   A  1 263 ? 32.316 -64.821  -27.473 1.00 37.50  ? 255  PHE   A O      1 
ATOM   1957 C CB     . PHE   A  1 263 ? 34.372 -64.604  -29.982 1.00 35.72  ? 255  PHE   A CB     1 
ATOM   1958 C CG     . PHE   A  1 263 ? 35.838 -64.775  -30.322 1.00 38.31  ? 255  PHE   A CG     1 
ATOM   1959 C CD1    . PHE   A  1 263 ? 36.784 -65.001  -29.321 1.00 42.08  ? 255  PHE   A CD1    1 
ATOM   1960 C CD2    . PHE   A  1 263 ? 36.280 -64.678  -31.636 1.00 40.71  ? 255  PHE   A CD2    1 
ATOM   1961 C CE1    . PHE   A  1 263 ? 38.134 -65.182  -29.639 1.00 43.00  ? 255  PHE   A CE1    1 
ATOM   1962 C CE2    . PHE   A  1 263 ? 37.633 -64.854  -31.953 1.00 43.74  ? 255  PHE   A CE2    1 
ATOM   1963 C CZ     . PHE   A  1 263 ? 38.551 -65.105  -30.952 1.00 41.99  ? 255  PHE   A CZ     1 
ATOM   1964 N N      . ARG   A  1 264 ? 31.319 -65.712  -29.307 1.00 32.23  ? 256  ARG   A N      1 
ATOM   1965 C CA     . ARG   A  1 264 ? 29.942 -65.478  -28.862 1.00 31.69  ? 256  ARG   A CA     1 
ATOM   1966 C C      . ARG   A  1 264 ? 29.638 -66.367  -27.638 1.00 33.82  ? 256  ARG   A C      1 
ATOM   1967 O O      . ARG   A  1 264 ? 29.091 -65.882  -26.651 1.00 32.74  ? 256  ARG   A O      1 
ATOM   1968 C CB     . ARG   A  1 264 ? 28.948 -65.767  -29.997 1.00 32.27  ? 256  ARG   A CB     1 
ATOM   1969 C CG     . ARG   A  1 264 ? 28.761 -64.612  -30.979 1.00 41.42  ? 256  ARG   A CG     1 
ATOM   1970 C CD     . ARG   A  1 264 ? 28.009 -65.051  -32.235 1.00 51.17  ? 256  ARG   A CD     1 
ATOM   1971 N NE     . ARG   A  1 264 ? 26.628 -65.468  -31.958 1.00 56.69  ? 256  ARG   A NE     1 
ATOM   1972 C CZ     . ARG   A  1 264 ? 25.547 -64.741  -32.234 1.00 63.38  ? 256  ARG   A CZ     1 
ATOM   1973 N NH1    . ARG   A  1 264 ? 25.667 -63.552  -32.811 1.00 42.56  ? 256  ARG   A NH1    1 
ATOM   1974 N NH2    . ARG   A  1 264 ? 24.337 -65.204  -31.946 1.00 45.92  ? 256  ARG   A NH2    1 
ATOM   1975 N N      . LEU   A  1 265 ? 30.038 -67.650  -27.696 1.00 29.17  ? 257  LEU   A N      1 
ATOM   1976 C CA     . LEU   A  1 265 ? 29.843 -68.616  -26.618 1.00 29.01  ? 257  LEU   A CA     1 
ATOM   1977 C C      . LEU   A  1 265 ? 30.716 -68.354  -25.395 1.00 33.01  ? 257  LEU   A C      1 
ATOM   1978 O O      . LEU   A  1 265 ? 30.305 -68.679  -24.277 1.00 31.31  ? 257  LEU   A O      1 
ATOM   1979 C CB     . LEU   A  1 265 ? 30.024 -70.046  -27.131 1.00 28.95  ? 257  LEU   A CB     1 
ATOM   1980 C CG     . LEU   A  1 265 ? 28.876 -70.574  -27.985 1.00 33.27  ? 257  LEU   A CG     1 
ATOM   1981 C CD1    . LEU   A  1 265 ? 29.363 -71.650  -28.940 1.00 32.81  ? 257  LEU   A CD1    1 
ATOM   1982 C CD2    . LEU   A  1 265 ? 27.714 -71.062  -27.115 1.00 35.74  ? 257  LEU   A CD2    1 
ATOM   1983 N N      . LEU   A  1 266 ? 31.906 -67.738  -25.602 1.00 31.02  ? 258  LEU   A N      1 
ATOM   1984 C CA     . LEU   A  1 266 ? 32.834 -67.371  -24.533 1.00 31.01  ? 258  LEU   A CA     1 
ATOM   1985 C C      . LEU   A  1 266 ? 32.258 -66.248  -23.666 1.00 34.80  ? 258  LEU   A C      1 
ATOM   1986 O O      . LEU   A  1 266 ? 32.526 -66.215  -22.467 1.00 34.05  ? 258  LEU   A O      1 
ATOM   1987 C CB     . LEU   A  1 266 ? 34.218 -66.988  -25.081 1.00 31.13  ? 258  LEU   A CB     1 
ATOM   1988 C CG     . LEU   A  1 266 ? 35.180 -68.149  -25.372 1.00 35.99  ? 258  LEU   A CG     1 
ATOM   1989 C CD1    . LEU   A  1 266 ? 36.355 -67.681  -26.225 1.00 35.94  ? 258  LEU   A CD1    1 
ATOM   1990 C CD2    . LEU   A  1 266 ? 35.699 -68.775  -24.086 1.00 38.60  ? 258  LEU   A CD2    1 
ATOM   1991 N N      . LYS   A  1 267 ? 31.434 -65.360  -24.266 1.00 32.26  ? 259  LYS   A N      1 
ATOM   1992 C CA     . LYS   A  1 267 ? 30.743 -64.271  -23.553 1.00 32.23  ? 259  LYS   A CA     1 
ATOM   1993 C C      . LYS   A  1 267 ? 29.651 -64.848  -22.636 1.00 38.01  ? 259  LYS   A C      1 
ATOM   1994 O O      . LYS   A  1 267 ? 29.381 -64.297  -21.571 1.00 38.32  ? 259  LYS   A O      1 
ATOM   1995 C CB     . LYS   A  1 267 ? 30.142 -63.266  -24.537 1.00 35.25  ? 259  LYS   A CB     1 
ATOM   1996 C CG     . LYS   A  1 267 ? 31.176 -62.352  -25.176 1.00 48.56  ? 259  LYS   A CG     1 
ATOM   1997 C CD     . LYS   A  1 267 ? 30.520 -61.259  -26.003 1.00 58.77  ? 259  LYS   A CD     1 
ATOM   1998 C CE     . LYS   A  1 267 ? 31.527 -60.284  -26.565 1.00 74.06  ? 259  LYS   A CE     1 
ATOM   1999 N NZ     . LYS   A  1 267 ? 32.350 -60.887  -27.654 1.00 87.76  ? 259  LYS   A NZ     1 
ATOM   2000 N N      . LEU   A  1 268 ? 29.083 -66.001  -23.025 1.00 34.84  ? 260  LEU   A N      1 
ATOM   2001 C CA     . LEU   A  1 268 ? 28.075 -66.738  -22.277 1.00 34.77  ? 260  LEU   A CA     1 
ATOM   2002 C C      . LEU   A  1 268 ? 28.701 -67.665  -21.221 1.00 37.94  ? 260  LEU   A C      1 
ATOM   2003 O O      . LEU   A  1 268 ? 27.974 -68.341  -20.481 1.00 37.62  ? 260  LEU   A O      1 
ATOM   2004 C CB     . LEU   A  1 268 ? 27.227 -67.549  -23.276 1.00 34.94  ? 260  LEU   A CB     1 
ATOM   2005 C CG     . LEU   A  1 268 ? 25.721 -67.335  -23.232 1.00 39.49  ? 260  LEU   A CG     1 
ATOM   2006 C CD1    . LEU   A  1 268 ? 25.350 -65.871  -23.442 1.00 39.19  ? 260  LEU   A CD1    1 
ATOM   2007 C CD2    . LEU   A  1 268 ? 25.034 -68.212  -24.250 1.00 42.34  ? 260  LEU   A CD2    1 
ATOM   2008 N N      . GLU   A  1 269 ? 30.050 -67.697  -21.156 1.00 33.59  ? 261  GLU   A N      1 
ATOM   2009 C CA     . GLU   A  1 269 ? 30.842 -68.503  -20.215 1.00 33.45  ? 261  GLU   A CA     1 
ATOM   2010 C C      . GLU   A  1 269 ? 30.413 -69.988  -20.191 1.00 36.19  ? 261  GLU   A C      1 
ATOM   2011 O O      . GLU   A  1 269 ? 30.307 -70.615  -19.128 1.00 36.90  ? 261  GLU   A O      1 
ATOM   2012 C CB     . GLU   A  1 269 ? 30.849 -67.878  -18.803 1.00 35.19  ? 261  GLU   A CB     1 
ATOM   2013 C CG     . GLU   A  1 269 ? 31.469 -66.494  -18.737 1.00 47.24  ? 261  GLU   A CG     1 
ATOM   2014 C CD     . GLU   A  1 269 ? 31.292 -65.814  -17.394 1.00 69.55  ? 261  GLU   A CD     1 
ATOM   2015 O OE1    . GLU   A  1 269 ? 31.948 -66.241  -16.418 1.00 65.41  ? 261  GLU   A OE1    1 
ATOM   2016 O OE2    . GLU   A  1 269 ? 30.501 -64.847  -17.319 1.00 66.62  ? 261  GLU   A OE2    1 
ATOM   2017 N N      . VAL   A  1 270 ? 30.177 -70.543  -21.380 1.00 29.99  ? 262  VAL   A N      1 
ATOM   2018 C CA     . VAL   A  1 270 ? 29.795 -71.938  -21.536 1.00 28.60  ? 262  VAL   A CA     1 
ATOM   2019 C C      . VAL   A  1 270 ? 31.004 -72.840  -21.251 1.00 31.28  ? 262  VAL   A C      1 
ATOM   2020 O O      . VAL   A  1 270 ? 32.153 -72.395  -21.326 1.00 30.19  ? 262  VAL   A O      1 
ATOM   2021 C CB     . VAL   A  1 270 ? 29.157 -72.245  -22.931 1.00 31.51  ? 262  VAL   A CB     1 
ATOM   2022 C CG1    . VAL   A  1 270 ? 28.015 -71.282  -23.254 1.00 30.96  ? 262  VAL   A CG1    1 
ATOM   2023 C CG2    . VAL   A  1 270 ? 30.200 -72.250  -24.053 1.00 30.94  ? 262  VAL   A CG2    1 
ATOM   2024 N N      . GLN   A  1 271 ? 30.737 -74.104  -20.943 1.00 27.58  ? 263  GLN   A N      1 
ATOM   2025 C CA     . GLN   A  1 271 ? 31.790 -75.089  -20.772 1.00 26.94  ? 263  GLN   A CA     1 
ATOM   2026 C C      . GLN   A  1 271 ? 31.954 -75.758  -22.126 1.00 31.00  ? 263  GLN   A C      1 
ATOM   2027 O O      . GLN   A  1 271 ? 30.959 -76.100  -22.764 1.00 30.67  ? 263  GLN   A O      1 
ATOM   2028 C CB     . GLN   A  1 271 ? 31.448 -76.089  -19.672 1.00 27.60  ? 263  GLN   A CB     1 
ATOM   2029 C CG     . GLN   A  1 271 ? 31.603 -75.454  -18.289 1.00 35.85  ? 263  GLN   A CG     1 
ATOM   2030 C CD     . GLN   A  1 271 ? 31.386 -76.441  -17.191 1.00 45.53  ? 263  GLN   A CD     1 
ATOM   2031 O OE1    . GLN   A  1 271 ? 30.274 -76.917  -16.959 1.00 41.74  ? 263  GLN   A OE1    1 
ATOM   2032 N NE2    . GLN   A  1 271 ? 32.445 -76.750  -16.474 1.00 40.60  ? 263  GLN   A NE2    1 
ATOM   2033 N N      . PHE   A  1 272 ? 33.192 -75.847  -22.615 1.00 27.18  ? 264  PHE   A N      1 
ATOM   2034 C CA     . PHE   A  1 272 ? 33.452 -76.439  -23.919 1.00 26.26  ? 264  PHE   A CA     1 
ATOM   2035 C C      . PHE   A  1 272 ? 33.722 -77.894  -23.755 1.00 30.40  ? 264  PHE   A C      1 
ATOM   2036 O O      . PHE   A  1 272 ? 34.428 -78.270  -22.832 1.00 31.20  ? 264  PHE   A O      1 
ATOM   2037 C CB     . PHE   A  1 272 ? 34.603 -75.722  -24.627 1.00 27.61  ? 264  PHE   A CB     1 
ATOM   2038 C CG     . PHE   A  1 272 ? 34.189 -74.343  -25.080 1.00 28.70  ? 264  PHE   A CG     1 
ATOM   2039 C CD1    . PHE   A  1 272 ? 34.345 -73.241  -24.243 1.00 31.32  ? 264  PHE   A CD1    1 
ATOM   2040 C CD2    . PHE   A  1 272 ? 33.564 -74.157  -26.308 1.00 29.16  ? 264  PHE   A CD2    1 
ATOM   2041 C CE1    . PHE   A  1 272 ? 33.927 -71.974  -24.649 1.00 32.05  ? 264  PHE   A CE1    1 
ATOM   2042 C CE2    . PHE   A  1 272 ? 33.145 -72.889  -26.713 1.00 31.61  ? 264  PHE   A CE2    1 
ATOM   2043 C CZ     . PHE   A  1 272 ? 33.344 -71.806  -25.890 1.00 30.36  ? 264  PHE   A CZ     1 
ATOM   2044 N N      . ILE   A  1 273 ? 33.098 -78.722  -24.593 1.00 25.57  ? 265  ILE   A N      1 
ATOM   2045 C CA     . ILE   A  1 273 ? 33.258 -80.171  -24.558 1.00 25.45  ? 265  ILE   A CA     1 
ATOM   2046 C C      . ILE   A  1 273 ? 33.849 -80.633  -25.894 1.00 28.66  ? 265  ILE   A C      1 
ATOM   2047 O O      . ILE   A  1 273 ? 33.327 -80.277  -26.943 1.00 26.81  ? 265  ILE   A O      1 
ATOM   2048 C CB     . ILE   A  1 273 ? 31.934 -80.912  -24.214 1.00 28.28  ? 265  ILE   A CB     1 
ATOM   2049 C CG1    . ILE   A  1 273 ? 31.382 -80.498  -22.824 1.00 27.91  ? 265  ILE   A CG1    1 
ATOM   2050 C CG2    . ILE   A  1 273 ? 32.118 -82.436  -24.300 1.00 29.03  ? 265  ILE   A CG2    1 
ATOM   2051 C CD1    . ILE   A  1 273 ? 29.928 -81.006  -22.549 1.00 28.14  ? 265  ILE   A CD1    1 
ATOM   2052 N N      . ILE   A  1 274 ? 34.935 -81.416  -25.843 1.00 26.36  ? 266  ILE   A N      1 
ATOM   2053 C CA     . ILE   A  1 274 ? 35.596 -81.968  -27.031 1.00 25.80  ? 266  ILE   A CA     1 
ATOM   2054 C C      . ILE   A  1 274 ? 35.167 -83.432  -27.175 1.00 28.71  ? 266  ILE   A C      1 
ATOM   2055 O O      . ILE   A  1 274 ? 35.430 -84.238  -26.279 1.00 27.29  ? 266  ILE   A O      1 
ATOM   2056 C CB     . ILE   A  1 274 ? 37.147 -81.791  -26.993 1.00 28.78  ? 266  ILE   A CB     1 
ATOM   2057 C CG1    . ILE   A  1 274 ? 37.576 -80.308  -26.806 1.00 29.63  ? 266  ILE   A CG1    1 
ATOM   2058 C CG2    . ILE   A  1 274 ? 37.829 -82.432  -28.210 1.00 30.34  ? 266  ILE   A CG2    1 
ATOM   2059 C CD1    . ILE   A  1 274 ? 37.367 -79.311  -28.010 1.00 38.58  ? 266  ILE   A CD1    1 
ATOM   2060 N N      . THR   A  1 275 ? 34.510 -83.761  -28.305 1.00 25.62  ? 267  THR   A N      1 
ATOM   2061 C CA     . THR   A  1 275 ? 34.022 -85.107  -28.623 1.00 25.72  ? 267  THR   A CA     1 
ATOM   2062 C C      . THR   A  1 275 ? 34.750 -85.671  -29.864 1.00 30.72  ? 267  THR   A C      1 
ATOM   2063 O O      . THR   A  1 275 ? 35.279 -84.895  -30.660 1.00 28.90  ? 267  THR   A O      1 
ATOM   2064 C CB     . THR   A  1 275 ? 32.464 -85.118  -28.725 1.00 28.11  ? 267  THR   A CB     1 
ATOM   2065 O OG1    . THR   A  1 275 ? 32.007 -86.463  -28.750 1.00 32.01  ? 267  THR   A OG1    1 
ATOM   2066 C CG2    . THR   A  1 275 ? 31.933 -84.422  -29.952 1.00 23.71  ? 267  THR   A CG2    1 
ATOM   2067 N N      . GLY   A  1 276 ? 34.745 -87.001  -30.011 1.00 30.16  ? 268  GLY   A N      1 
ATOM   2068 C CA     . GLY   A  1 276 ? 35.369 -87.710  -31.130 1.00 30.54  ? 268  GLY   A CA     1 
ATOM   2069 C C      . GLY   A  1 276 ? 36.831 -88.071  -30.929 1.00 36.45  ? 268  GLY   A C      1 
ATOM   2070 O O      . GLY   A  1 276 ? 37.446 -87.630  -29.955 1.00 35.42  ? 268  GLY   A O      1 
ATOM   2071 N N      . THR   A  1 277 ? 37.410 -88.873  -31.855 1.00 35.58  ? 269  THR   A N      1 
ATOM   2072 C CA     . THR   A  1 277 ? 38.825 -89.280  -31.761 1.00 37.00  ? 269  THR   A CA     1 
ATOM   2073 C C      . THR   A  1 277 ? 39.761 -88.224  -32.340 1.00 43.06  ? 269  THR   A C      1 
ATOM   2074 O O      . THR   A  1 277 ? 39.294 -87.256  -32.933 1.00 40.33  ? 269  THR   A O      1 
ATOM   2075 C CB     . THR   A  1 277 ? 39.089 -90.672  -32.390 1.00 46.64  ? 269  THR   A CB     1 
ATOM   2076 O OG1    . THR   A  1 277 ? 38.642 -90.701  -33.747 1.00 42.29  ? 269  THR   A OG1    1 
ATOM   2077 C CG2    . THR   A  1 277 ? 38.487 -91.812  -31.584 1.00 48.30  ? 269  THR   A CG2    1 
ATOM   2078 N N      . ASN   A  1 278 ? 41.085 -88.421  -32.190 1.00 43.99  ? 270  ASN   A N      1 
ATOM   2079 C CA     . ASN   A  1 278 ? 42.078 -87.501  -32.745 1.00 45.83  ? 270  ASN   A CA     1 
ATOM   2080 C C      . ASN   A  1 278 ? 42.154 -87.666  -34.270 1.00 54.12  ? 270  ASN   A C      1 
ATOM   2081 O O      . ASN   A  1 278 ? 42.371 -88.777  -34.761 1.00 54.13  ? 270  ASN   A O      1 
ATOM   2082 C CB     . ASN   A  1 278 ? 43.452 -87.720  -32.102 1.00 46.32  ? 270  ASN   A CB     1 
ATOM   2083 C CG     . ASN   A  1 278 ? 44.427 -86.579  -32.293 1.00 64.47  ? 270  ASN   A CG     1 
ATOM   2084 O OD1    . ASN   A  1 278 ? 44.227 -85.664  -33.106 1.00 55.22  ? 270  ASN   A OD1    1 
ATOM   2085 N ND2    . ASN   A  1 278 ? 45.528 -86.623  -31.556 1.00 56.07  ? 270  ASN   A ND2    1 
ATOM   2086 N N      . HIS   A  1 279 ? 41.936 -86.565  -35.010 1.00 53.54  ? 271  HIS   A N      1 
ATOM   2087 C CA     . HIS   A  1 279 ? 41.996 -86.549  -36.473 1.00 54.86  ? 271  HIS   A CA     1 
ATOM   2088 C C      . HIS   A  1 279 ? 43.283 -85.884  -36.977 1.00 62.00  ? 271  HIS   A C      1 
ATOM   2089 O O      . HIS   A  1 279 ? 43.490 -85.733  -38.184 1.00 61.59  ? 271  HIS   A O      1 
ATOM   2090 C CB     . HIS   A  1 279 ? 40.731 -85.920  -37.068 1.00 55.86  ? 271  HIS   A CB     1 
ATOM   2091 C CG     . HIS   A  1 279 ? 39.524 -86.802  -36.957 1.00 59.62  ? 271  HIS   A CG     1 
ATOM   2092 N ND1    . HIS   A  1 279 ? 38.264 -86.274  -36.753 1.00 61.59  ? 271  HIS   A ND1    1 
ATOM   2093 C CD2    . HIS   A  1 279 ? 39.426 -88.153  -37.025 1.00 61.58  ? 271  HIS   A CD2    1 
ATOM   2094 C CE1    . HIS   A  1 279 ? 37.443 -87.309  -36.716 1.00 61.14  ? 271  HIS   A CE1    1 
ATOM   2095 N NE2    . HIS   A  1 279 ? 38.099 -88.462  -36.861 1.00 61.50  ? 271  HIS   A NE2    1 
ATOM   2096 N N      . HIS   A  1 280 ? 44.155 -85.518  -36.025 1.00 60.93  ? 272  HIS   A N      1 
ATOM   2097 C CA     . HIS   A  1 280 ? 45.468 -84.916  -36.227 1.00 61.65  ? 272  HIS   A CA     1 
ATOM   2098 C C      . HIS   A  1 280 ? 46.459 -85.814  -35.451 1.00 68.28  ? 272  HIS   A C      1 
ATOM   2099 O O      . HIS   A  1 280 ? 47.097 -85.370  -34.495 1.00 67.70  ? 272  HIS   A O      1 
ATOM   2100 C CB     . HIS   A  1 280 ? 45.467 -83.458  -35.711 1.00 62.25  ? 272  HIS   A CB     1 
ATOM   2101 C CG     . HIS   A  1 280 ? 44.515 -82.551  -36.437 1.00 65.50  ? 272  HIS   A CG     1 
ATOM   2102 N ND1    . HIS   A  1 280 ? 43.147 -82.628  -36.240 1.00 67.09  ? 272  HIS   A ND1    1 
ATOM   2103 C CD2    . HIS   A  1 280 ? 44.769 -81.562  -37.325 1.00 67.06  ? 272  HIS   A CD2    1 
ATOM   2104 C CE1    . HIS   A  1 280 ? 42.617 -81.697  -37.015 1.00 66.29  ? 272  HIS   A CE1    1 
ATOM   2105 N NE2    . HIS   A  1 280 ? 43.551 -81.032  -37.688 1.00 66.69  ? 272  HIS   A NE2    1 
ATOM   2106 N N      . SER   A  1 281 ? 46.535 -87.105  -35.863 1.00 67.14  ? 273  SER   A N      1 
ATOM   2107 C CA     . SER   A  1 281 ? 47.337 -88.193  -35.279 1.00 67.78  ? 273  SER   A CA     1 
ATOM   2108 C C      . SER   A  1 281 ? 48.827 -87.877  -35.077 1.00 73.16  ? 273  SER   A C      1 
ATOM   2109 O O      . SER   A  1 281 ? 49.424 -88.382  -34.119 1.00 72.95  ? 273  SER   A O      1 
ATOM   2110 C CB     . SER   A  1 281 ? 47.178 -89.470  -36.097 1.00 71.60  ? 273  SER   A CB     1 
ATOM   2111 O OG     . SER   A  1 281 ? 45.819 -89.877  -36.137 1.00 80.70  ? 273  SER   A OG     1 
ATOM   2112 N N      . GLU   A  1 282 ? 49.417 -87.039  -35.959 1.00 70.17  ? 274  GLU   A N      1 
ATOM   2113 C CA     . GLU   A  1 282 ? 50.822 -86.610  -35.876 1.00 70.22  ? 274  GLU   A CA     1 
ATOM   2114 C C      . GLU   A  1 282 ? 51.044 -85.706  -34.649 1.00 73.40  ? 274  GLU   A C      1 
ATOM   2115 O O      . GLU   A  1 282 ? 52.145 -85.676  -34.095 1.00 73.35  ? 274  GLU   A O      1 
ATOM   2116 C CB     . GLU   A  1 282 ? 51.256 -85.875  -37.163 1.00 71.71  ? 274  GLU   A CB     1 
ATOM   2117 C CG     . GLU   A  1 282 ? 51.372 -86.761  -38.397 1.00 83.00  ? 274  GLU   A CG     1 
ATOM   2118 C CD     . GLU   A  1 282 ? 51.908 -86.082  -39.646 1.00 106.02 ? 274  GLU   A CD     1 
ATOM   2119 O OE1    . GLU   A  1 282 ? 51.383 -85.007  -40.021 1.00 95.77  ? 274  GLU   A OE1    1 
ATOM   2120 O OE2    . GLU   A  1 282 ? 52.836 -86.645  -40.270 1.00 104.24 ? 274  GLU   A OE2    1 
ATOM   2121 N N      . LYS   A  1 283 ? 49.987 -84.982  -34.233 1.00 68.76  ? 275  LYS   A N      1 
ATOM   2122 C CA     . LYS   A  1 283 ? 49.987 -84.067  -33.093 1.00 67.95  ? 275  LYS   A CA     1 
ATOM   2123 C C      . LYS   A  1 283 ? 49.352 -84.715  -31.855 1.00 69.80  ? 275  LYS   A C      1 
ATOM   2124 O O      . LYS   A  1 283 ? 48.574 -85.664  -31.988 1.00 69.35  ? 275  LYS   A O      1 
ATOM   2125 C CB     . LYS   A  1 283 ? 49.237 -82.774  -33.470 1.00 70.69  ? 275  LYS   A CB     1 
ATOM   2126 C CG     . LYS   A  1 283 ? 49.764 -81.512  -32.790 1.00 88.56  ? 275  LYS   A CG     1 
ATOM   2127 C CD     . LYS   A  1 283 ? 50.873 -80.818  -33.600 1.00 101.31 ? 275  LYS   A CD     1 
ATOM   2128 C CE     . LYS   A  1 283 ? 52.282 -81.148  -33.141 1.00 114.00 ? 275  LYS   A CE     1 
ATOM   2129 N NZ     . LYS   A  1 283 ? 52.577 -80.630  -31.776 1.00 123.12 ? 275  LYS   A NZ     1 
ATOM   2130 N N      . GLU   A  1 284 ? 49.691 -84.208  -30.651 1.00 64.75  ? 276  GLU   A N      1 
ATOM   2131 C CA     . GLU   A  1 284 ? 49.129 -84.700  -29.385 1.00 64.08  ? 276  GLU   A CA     1 
ATOM   2132 C C      . GLU   A  1 284 ? 47.656 -84.257  -29.241 1.00 66.17  ? 276  GLU   A C      1 
ATOM   2133 O O      . GLU   A  1 284 ? 47.255 -83.286  -29.891 1.00 66.12  ? 276  GLU   A O      1 
ATOM   2134 C CB     . GLU   A  1 284 ? 49.993 -84.281  -28.178 1.00 65.61  ? 276  GLU   A CB     1 
ATOM   2135 C CG     . GLU   A  1 284 ? 50.240 -82.785  -28.035 1.00 77.16  ? 276  GLU   A CG     1 
ATOM   2136 C CD     . GLU   A  1 284 ? 51.235 -82.394  -26.959 1.00 101.42 ? 276  GLU   A CD     1 
ATOM   2137 O OE1    . GLU   A  1 284 ? 51.154 -82.944  -25.835 1.00 92.21  ? 276  GLU   A OE1    1 
ATOM   2138 O OE2    . GLU   A  1 284 ? 52.080 -81.510  -27.231 1.00 98.75  ? 276  GLU   A OE2    1 
ATOM   2139 N N      . PHE   A  1 285 ? 46.849 -84.974  -28.427 1.00 60.41  ? 277  PHE   A N      1 
ATOM   2140 C CA     . PHE   A  1 285 ? 45.420 -84.665  -28.293 1.00 59.15  ? 277  PHE   A CA     1 
ATOM   2141 C C      . PHE   A  1 285 ? 45.112 -83.300  -27.670 1.00 61.48  ? 277  PHE   A C      1 
ATOM   2142 O O      . PHE   A  1 285 ? 44.161 -82.655  -28.120 1.00 61.90  ? 277  PHE   A O      1 
ATOM   2143 C CB     . PHE   A  1 285 ? 44.636 -85.769  -27.558 1.00 60.62  ? 277  PHE   A CB     1 
ATOM   2144 C CG     . PHE   A  1 285 ? 43.155 -85.702  -27.859 1.00 61.42  ? 277  PHE   A CG     1 
ATOM   2145 C CD1    . PHE   A  1 285 ? 42.287 -85.014  -27.018 1.00 63.61  ? 277  PHE   A CD1    1 
ATOM   2146 C CD2    . PHE   A  1 285 ? 42.637 -86.273  -29.014 1.00 63.10  ? 277  PHE   A CD2    1 
ATOM   2147 C CE1    . PHE   A  1 285 ? 40.931 -84.903  -27.327 1.00 64.33  ? 277  PHE   A CE1    1 
ATOM   2148 C CE2    . PHE   A  1 285 ? 41.277 -86.170  -29.318 1.00 65.59  ? 277  PHE   A CE2    1 
ATOM   2149 C CZ     . PHE   A  1 285 ? 40.435 -85.483  -28.474 1.00 63.55  ? 277  PHE   A CZ     1 
ATOM   2150 N N      . CYS   A  1 286 ? 45.899 -82.853  -26.662 1.00 55.50  ? 278  CYS   A N      1 
ATOM   2151 C CA     . CYS   A  1 286 ? 45.685 -81.570  -25.973 1.00 53.94  ? 278  CYS   A CA     1 
ATOM   2152 C C      . CYS   A  1 286 ? 45.781 -80.331  -26.901 1.00 51.09  ? 278  CYS   A C      1 
ATOM   2153 O O      . CYS   A  1 286 ? 45.481 -79.222  -26.458 1.00 49.94  ? 278  CYS   A O      1 
ATOM   2154 C CB     . CYS   A  1 286 ? 46.601 -81.438  -24.758 1.00 55.09  ? 278  CYS   A CB     1 
ATOM   2155 S SG     . CYS   A  1 286 ? 48.357 -81.218  -25.158 1.00 59.51  ? 278  CYS   A SG     1 
ATOM   2156 N N      . SER   A  1 287 ? 46.169 -80.528  -28.179 1.00 43.66  ? 279  SER   A N      1 
ATOM   2157 C CA     . SER   A  1 287 ? 46.290 -79.471  -29.188 1.00 41.54  ? 279  SER   A CA     1 
ATOM   2158 C C      . SER   A  1 287 ? 44.935 -78.820  -29.527 1.00 41.39  ? 279  SER   A C      1 
ATOM   2159 O O      . SER   A  1 287 ? 44.905 -77.616  -29.768 1.00 40.20  ? 279  SER   A O      1 
ATOM   2160 C CB     . SER   A  1 287 ? 46.967 -80.003  -30.444 1.00 44.20  ? 279  SER   A CB     1 
ATOM   2161 O OG     . SER   A  1 287 ? 46.167 -80.996  -31.061 1.00 52.26  ? 279  SER   A OG     1 
ATOM   2162 N N      . TYR   A  1 288 ? 43.823 -79.605  -29.511 1.00 36.90  ? 280  TYR   A N      1 
ATOM   2163 C CA     . TYR   A  1 288 ? 42.452 -79.110  -29.729 1.00 36.66  ? 280  TYR   A CA     1 
ATOM   2164 C C      . TYR   A  1 288 ? 42.079 -78.170  -28.587 1.00 40.91  ? 280  TYR   A C      1 
ATOM   2165 O O      . TYR   A  1 288 ? 41.415 -77.161  -28.809 1.00 40.82  ? 280  TYR   A O      1 
ATOM   2166 C CB     . TYR   A  1 288 ? 41.429 -80.260  -29.752 1.00 37.21  ? 280  TYR   A CB     1 
ATOM   2167 C CG     . TYR   A  1 288 ? 41.520 -81.184  -30.943 1.00 37.65  ? 280  TYR   A CG     1 
ATOM   2168 C CD1    . TYR   A  1 288 ? 40.957 -80.833  -32.166 1.00 38.70  ? 280  TYR   A CD1    1 
ATOM   2169 C CD2    . TYR   A  1 288 ? 42.091 -82.447  -30.826 1.00 38.42  ? 280  TYR   A CD2    1 
ATOM   2170 C CE1    . TYR   A  1 288 ? 41.017 -81.692  -33.263 1.00 38.27  ? 280  TYR   A CE1    1 
ATOM   2171 C CE2    . TYR   A  1 288 ? 42.146 -83.319  -31.911 1.00 39.32  ? 280  TYR   A CE2    1 
ATOM   2172 C CZ     . TYR   A  1 288 ? 41.617 -82.933  -33.131 1.00 43.63  ? 280  TYR   A CZ     1 
ATOM   2173 O OH     . TYR   A  1 288 ? 41.667 -83.797  -34.194 1.00 43.65  ? 280  TYR   A OH     1 
ATOM   2174 N N      . LEU   A  1 289 ? 42.515 -78.512  -27.366 1.00 38.18  ? 281  LEU   A N      1 
ATOM   2175 C CA     . LEU   A  1 289 ? 42.293 -77.731  -26.162 1.00 38.66  ? 281  LEU   A CA     1 
ATOM   2176 C C      . LEU   A  1 289 ? 43.157 -76.474  -26.145 1.00 43.38  ? 281  LEU   A C      1 
ATOM   2177 O O      . LEU   A  1 289 ? 42.659 -75.406  -25.785 1.00 42.76  ? 281  LEU   A O      1 
ATOM   2178 C CB     . LEU   A  1 289 ? 42.562 -78.600  -24.928 1.00 39.03  ? 281  LEU   A CB     1 
ATOM   2179 C CG     . LEU   A  1 289 ? 41.746 -78.263  -23.704 1.00 44.09  ? 281  LEU   A CG     1 
ATOM   2180 C CD1    . LEU   A  1 289 ? 40.282 -78.557  -23.950 1.00 44.95  ? 281  LEU   A CD1    1 
ATOM   2181 C CD2    . LEU   A  1 289 ? 42.243 -79.037  -22.500 1.00 45.47  ? 281  LEU   A CD2    1 
ATOM   2182 N N      . GLN   A  1 290 ? 44.442 -76.593  -26.570 1.00 41.14  ? 282  GLN   A N      1 
ATOM   2183 C CA     . GLN   A  1 290 ? 45.402 -75.477  -26.658 1.00 40.63  ? 282  GLN   A CA     1 
ATOM   2184 C C      . GLN   A  1 290 ? 44.897 -74.400  -27.610 1.00 42.72  ? 282  GLN   A C      1 
ATOM   2185 O O      . GLN   A  1 290 ? 45.127 -73.215  -27.370 1.00 42.89  ? 282  GLN   A O      1 
ATOM   2186 C CB     . GLN   A  1 290 ? 46.788 -75.962  -27.116 1.00 42.25  ? 282  GLN   A CB     1 
ATOM   2187 C CG     . GLN   A  1 290 ? 47.609 -76.656  -26.038 1.00 63.67  ? 282  GLN   A CG     1 
ATOM   2188 C CD     . GLN   A  1 290 ? 48.987 -77.008  -26.547 1.00 88.75  ? 282  GLN   A CD     1 
ATOM   2189 O OE1    . GLN   A  1 290 ? 49.940 -76.234  -26.418 1.00 86.54  ? 282  GLN   A OE1    1 
ATOM   2190 N NE2    . GLN   A  1 290 ? 49.122 -78.179  -27.153 1.00 81.55  ? 282  GLN   A NE2    1 
ATOM   2191 N N      . TYR   A  1 291 ? 44.196 -74.808  -28.682 1.00 38.19  ? 283  TYR   A N      1 
ATOM   2192 C CA     . TYR   A  1 291 ? 43.636 -73.872  -29.654 1.00 37.59  ? 283  TYR   A CA     1 
ATOM   2193 C C      . TYR   A  1 291 ? 42.484 -73.066  -29.046 1.00 42.01  ? 283  TYR   A C      1 
ATOM   2194 O O      . TYR   A  1 291 ? 42.370 -71.873  -29.323 1.00 40.44  ? 283  TYR   A O      1 
ATOM   2195 C CB     . TYR   A  1 291 ? 43.203 -74.593  -30.939 1.00 37.84  ? 283  TYR   A CB     1 
ATOM   2196 C CG     . TYR   A  1 291 ? 42.647 -73.657  -31.986 1.00 38.43  ? 283  TYR   A CG     1 
ATOM   2197 C CD1    . TYR   A  1 291 ? 43.483 -72.800  -32.698 1.00 40.25  ? 283  TYR   A CD1    1 
ATOM   2198 C CD2    . TYR   A  1 291 ? 41.281 -73.597  -32.240 1.00 38.62  ? 283  TYR   A CD2    1 
ATOM   2199 C CE1    . TYR   A  1 291 ? 42.970 -71.901  -33.631 1.00 41.17  ? 283  TYR   A CE1    1 
ATOM   2200 C CE2    . TYR   A  1 291 ? 40.759 -72.712  -33.179 1.00 39.35  ? 283  TYR   A CE2    1 
ATOM   2201 C CZ     . TYR   A  1 291 ? 41.608 -71.870  -33.878 1.00 47.15  ? 283  TYR   A CZ     1 
ATOM   2202 O OH     . TYR   A  1 291 ? 41.099 -71.007  -34.816 1.00 48.82  ? 283  TYR   A OH     1 
ATOM   2203 N N      . LEU   A  1 292 ? 41.652 -73.720  -28.208 1.00 40.46  ? 284  LEU   A N      1 
ATOM   2204 C CA     . LEU   A  1 292 ? 40.523 -73.103  -27.504 1.00 41.06  ? 284  LEU   A CA     1 
ATOM   2205 C C      . LEU   A  1 292 ? 41.008 -72.052  -26.499 1.00 44.82  ? 284  LEU   A C      1 
ATOM   2206 O O      . LEU   A  1 292 ? 40.428 -70.966  -26.440 1.00 44.64  ? 284  LEU   A O      1 
ATOM   2207 C CB     . LEU   A  1 292 ? 39.664 -74.182  -26.795 1.00 41.55  ? 284  LEU   A CB     1 
ATOM   2208 C CG     . LEU   A  1 292 ? 38.376 -74.694  -27.481 1.00 47.24  ? 284  LEU   A CG     1 
ATOM   2209 C CD1    . LEU   A  1 292 ? 37.268 -73.656  -27.463 1.00 48.13  ? 284  LEU   A CD1    1 
ATOM   2210 C CD2    . LEU   A  1 292 ? 38.626 -75.214  -28.889 1.00 51.02  ? 284  LEU   A CD2    1 
ATOM   2211 N N      . GLU   A  1 293 ? 42.082 -72.358  -25.731 1.00 41.91  ? 285  GLU   A N      1 
ATOM   2212 C CA     . GLU   A  1 293 ? 42.650 -71.408  -24.762 1.00 42.37  ? 285  GLU   A CA     1 
ATOM   2213 C C      . GLU   A  1 293 ? 43.369 -70.256  -25.471 1.00 46.51  ? 285  GLU   A C      1 
ATOM   2214 O O      . GLU   A  1 293 ? 43.353 -69.132  -24.965 1.00 46.07  ? 285  GLU   A O      1 
ATOM   2215 C CB     . GLU   A  1 293 ? 43.517 -72.086  -23.676 1.00 44.06  ? 285  GLU   A CB     1 
ATOM   2216 C CG     . GLU   A  1 293 ? 44.753 -72.817  -24.170 1.00 58.41  ? 285  GLU   A CG     1 
ATOM   2217 C CD     . GLU   A  1 293 ? 45.286 -73.918  -23.272 1.00 86.01  ? 285  GLU   A CD     1 
ATOM   2218 O OE1    . GLU   A  1 293 ? 46.518 -73.949  -23.043 1.00 80.68  ? 285  GLU   A OE1    1 
ATOM   2219 O OE2    . GLU   A  1 293 ? 44.483 -74.771  -22.826 1.00 82.36  ? 285  GLU   A OE2    1 
ATOM   2220 N N      . TYR   A  1 294 ? 43.930 -70.525  -26.675 1.00 43.32  ? 286  TYR   A N      1 
ATOM   2221 C CA     . TYR   A  1 294 ? 44.569 -69.519  -27.528 1.00 43.00  ? 286  TYR   A CA     1 
ATOM   2222 C C      . TYR   A  1 294 ? 43.505 -68.499  -27.938 1.00 45.13  ? 286  TYR   A C      1 
ATOM   2223 O O      . TYR   A  1 294 ? 43.737 -67.301  -27.804 1.00 44.43  ? 286  TYR   A O      1 
ATOM   2224 C CB     . TYR   A  1 294 ? 45.232 -70.174  -28.762 1.00 44.60  ? 286  TYR   A CB     1 
ATOM   2225 C CG     . TYR   A  1 294 ? 45.534 -69.210  -29.891 1.00 47.12  ? 286  TYR   A CG     1 
ATOM   2226 C CD1    . TYR   A  1 294 ? 46.680 -68.420  -29.873 1.00 49.31  ? 286  TYR   A CD1    1 
ATOM   2227 C CD2    . TYR   A  1 294 ? 44.672 -69.087  -30.978 1.00 47.96  ? 286  TYR   A CD2    1 
ATOM   2228 C CE1    . TYR   A  1 294 ? 46.955 -67.522  -30.903 1.00 50.59  ? 286  TYR   A CE1    1 
ATOM   2229 C CE2    . TYR   A  1 294 ? 44.925 -68.177  -32.002 1.00 49.09  ? 286  TYR   A CE2    1 
ATOM   2230 C CZ     . TYR   A  1 294 ? 46.075 -67.405  -31.967 1.00 57.51  ? 286  TYR   A CZ     1 
ATOM   2231 O OH     . TYR   A  1 294 ? 46.343 -66.530  -32.990 1.00 61.35  ? 286  TYR   A OH     1 
ATOM   2232 N N      . LEU   A  1 295 ? 42.331 -68.982  -28.403 1.00 41.20  ? 287  LEU   A N      1 
ATOM   2233 C CA     . LEU   A  1 295 ? 41.200 -68.132  -28.783 1.00 41.38  ? 287  LEU   A CA     1 
ATOM   2234 C C      . LEU   A  1 295 ? 40.724 -67.303  -27.588 1.00 46.69  ? 287  LEU   A C      1 
ATOM   2235 O O      . LEU   A  1 295 ? 40.525 -66.095  -27.725 1.00 45.58  ? 287  LEU   A O      1 
ATOM   2236 C CB     . LEU   A  1 295 ? 40.031 -68.964  -29.349 1.00 41.13  ? 287  LEU   A CB     1 
ATOM   2237 C CG     . LEU   A  1 295 ? 40.214 -69.618  -30.719 1.00 45.10  ? 287  LEU   A CG     1 
ATOM   2238 C CD1    . LEU   A  1 295 ? 38.979 -70.396  -31.094 1.00 45.05  ? 287  LEU   A CD1    1 
ATOM   2239 C CD2    . LEU   A  1 295 ? 40.517 -68.589  -31.810 1.00 45.55  ? 287  LEU   A CD2    1 
ATOM   2240 N N      . SER   A  1 296 ? 40.593 -67.951  -26.410 1.00 45.04  ? 288  SER   A N      1 
ATOM   2241 C CA     . SER   A  1 296 ? 40.180 -67.326  -25.153 1.00 45.78  ? 288  SER   A CA     1 
ATOM   2242 C C      . SER   A  1 296 ? 41.146 -66.229  -24.700 1.00 51.59  ? 288  SER   A C      1 
ATOM   2243 O O      . SER   A  1 296 ? 40.692 -65.200  -24.205 1.00 51.15  ? 288  SER   A O      1 
ATOM   2244 C CB     . SER   A  1 296 ? 40.055 -68.376  -24.060 1.00 49.99  ? 288  SER   A CB     1 
ATOM   2245 O OG     . SER   A  1 296 ? 39.683 -67.798  -22.820 1.00 61.61  ? 288  SER   A OG     1 
ATOM   2246 N N      . GLN   A  1 297 ? 42.467 -66.453  -24.848 1.00 49.56  ? 289  GLN   A N      1 
ATOM   2247 C CA     . GLN   A  1 297 ? 43.488 -65.474  -24.465 1.00 49.96  ? 289  GLN   A CA     1 
ATOM   2248 C C      . GLN   A  1 297 ? 43.528 -64.283  -25.428 1.00 55.96  ? 289  GLN   A C      1 
ATOM   2249 O O      . GLN   A  1 297 ? 43.881 -63.178  -25.015 1.00 55.73  ? 289  GLN   A O      1 
ATOM   2250 C CB     . GLN   A  1 297 ? 44.873 -66.136  -24.365 1.00 51.32  ? 289  GLN   A CB     1 
ATOM   2251 C CG     . GLN   A  1 297 ? 45.091 -66.952  -23.085 1.00 70.94  ? 289  GLN   A CG     1 
ATOM   2252 C CD     . GLN   A  1 297 ? 45.367 -66.100  -21.862 1.00 94.66  ? 289  GLN   A CD     1 
ATOM   2253 O OE1    . GLN   A  1 297 ? 46.351 -65.349  -21.796 1.00 89.87  ? 289  GLN   A OE1    1 
ATOM   2254 N NE2    . GLN   A  1 297 ? 44.524 -66.235  -20.846 1.00 87.98  ? 289  GLN   A NE2    1 
ATOM   2255 N N      . ASN   A  1 298 ? 43.157 -64.507  -26.702 1.00 54.24  ? 290  ASN   A N      1 
ATOM   2256 C CA     . ASN   A  1 298 ? 43.170 -63.486  -27.751 1.00 55.14  ? 290  ASN   A CA     1 
ATOM   2257 C C      . ASN   A  1 298 ? 41.813 -62.784  -27.976 1.00 61.21  ? 290  ASN   A C      1 
ATOM   2258 O O      . ASN   A  1 298 ? 41.657 -62.057  -28.964 1.00 61.76  ? 290  ASN   A O      1 
ATOM   2259 C CB     . ASN   A  1 298 ? 43.723 -64.069  -29.056 1.00 56.42  ? 290  ASN   A CB     1 
ATOM   2260 C CG     . ASN   A  1 298 ? 45.220 -64.245  -29.030 1.00 79.36  ? 290  ASN   A CG     1 
ATOM   2261 O OD1    . ASN   A  1 298 ? 45.737 -65.340  -28.787 1.00 72.82  ? 290  ASN   A OD1    1 
ATOM   2262 N ND2    . ASN   A  1 298 ? 45.954 -63.161  -29.253 1.00 71.36  ? 290  ASN   A ND2    1 
ATOM   2263 N N      . ARG   A  1 299 ? 40.851 -62.965  -27.052 1.00 58.24  ? 291  ARG   A N      1 
ATOM   2264 C CA     . ARG   A  1 299 ? 39.543 -62.312  -27.146 1.00 58.11  ? 291  ARG   A CA     1 
ATOM   2265 C C      . ARG   A  1 299 ? 39.652 -60.834  -26.688 1.00 62.28  ? 291  ARG   A C      1 
ATOM   2266 O O      . ARG   A  1 299 ? 40.606 -60.512  -25.970 1.00 61.40  ? 291  ARG   A O      1 
ATOM   2267 C CB     . ARG   A  1 299 ? 38.471 -63.097  -26.355 1.00 58.02  ? 291  ARG   A CB     1 
ATOM   2268 C CG     . ARG   A  1 299 ? 38.522 -62.935  -24.842 1.00 65.63  ? 291  ARG   A CG     1 
ATOM   2269 C CD     . ARG   A  1 299 ? 37.390 -63.682  -24.177 1.00 73.49  ? 291  ARG   A CD     1 
ATOM   2270 N NE     . ARG   A  1 299 ? 37.850 -64.477  -23.040 1.00 81.62  ? 291  ARG   A NE     1 
ATOM   2271 C CZ     . ARG   A  1 299 ? 37.046 -65.062  -22.158 1.00 98.38  ? 291  ARG   A CZ     1 
ATOM   2272 N NH1    . ARG   A  1 299 ? 35.729 -64.935  -22.263 1.00 87.48  ? 291  ARG   A NH1    1 
ATOM   2273 N NH2    . ARG   A  1 299 ? 37.553 -65.770  -21.159 1.00 86.56  ? 291  ARG   A NH2    1 
ATOM   2274 N N      . PRO   A  1 300 ? 38.714 -59.923  -27.081 1.00 59.64  ? 292  PRO   A N      1 
ATOM   2275 C CA     . PRO   A  1 300 ? 38.831 -58.514  -26.649 1.00 59.36  ? 292  PRO   A CA     1 
ATOM   2276 C C      . PRO   A  1 300 ? 38.856 -58.315  -25.126 1.00 62.40  ? 292  PRO   A C      1 
ATOM   2277 O O      . PRO   A  1 300 ? 38.082 -58.967  -24.414 1.00 62.11  ? 292  PRO   A O      1 
ATOM   2278 C CB     . PRO   A  1 300 ? 37.608 -57.842  -27.288 1.00 61.30  ? 292  PRO   A CB     1 
ATOM   2279 C CG     . PRO   A  1 300 ? 37.239 -58.727  -28.436 1.00 65.85  ? 292  PRO   A CG     1 
ATOM   2280 C CD     . PRO   A  1 300 ? 37.532 -60.112  -27.951 1.00 61.41  ? 292  PRO   A CD     1 
ATOM   2281 N N      . PRO   A  1 301 ? 39.763 -57.454  -24.601 1.00 57.45  ? 293  PRO   A N      1 
ATOM   2282 C CA     . PRO   A  1 301 ? 39.819 -57.252  -23.139 1.00 56.65  ? 293  PRO   A CA     1 
ATOM   2283 C C      . PRO   A  1 301 ? 38.610 -56.479  -22.587 1.00 58.21  ? 293  PRO   A C      1 
ATOM   2284 O O      . PRO   A  1 301 ? 37.963 -55.760  -23.359 1.00 57.29  ? 293  PRO   A O      1 
ATOM   2285 C CB     . PRO   A  1 301 ? 41.142 -56.505  -22.929 1.00 58.53  ? 293  PRO   A CB     1 
ATOM   2286 C CG     . PRO   A  1 301 ? 41.401 -55.815  -24.209 1.00 63.28  ? 293  PRO   A CG     1 
ATOM   2287 C CD     . PRO   A  1 301 ? 40.756 -56.617  -25.307 1.00 58.86  ? 293  PRO   A CD     1 
ATOM   2288 N N      . PRO   A  1 302 ? 38.263 -56.611  -21.278 1.00 53.28  ? 294  PRO   A N      1 
ATOM   2289 C CA     . PRO   A  1 302 ? 37.090 -55.879  -20.762 1.00 52.13  ? 294  PRO   A CA     1 
ATOM   2290 C C      . PRO   A  1 302 ? 37.268 -54.360  -20.736 1.00 52.29  ? 294  PRO   A C      1 
ATOM   2291 O O      . PRO   A  1 302 ? 38.290 -53.868  -20.255 1.00 51.12  ? 294  PRO   A O      1 
ATOM   2292 C CB     . PRO   A  1 302 ? 36.884 -56.462  -19.356 1.00 54.21  ? 294  PRO   A CB     1 
ATOM   2293 C CG     . PRO   A  1 302 ? 38.211 -56.998  -18.959 1.00 59.02  ? 294  PRO   A CG     1 
ATOM   2294 C CD     . PRO   A  1 302 ? 38.897 -57.435  -20.223 1.00 54.66  ? 294  PRO   A CD     1 
ATOM   2295 N N      . ASN   A  1 303 ? 36.276 -53.623  -21.283 1.00 46.60  ? 295  ASN   A N      1 
ATOM   2296 C CA     . ASN   A  1 303 ? 36.276 -52.158  -21.291 1.00 45.15  ? 295  ASN   A CA     1 
ATOM   2297 C C      . ASN   A  1 303 ? 35.899 -51.608  -19.901 1.00 45.99  ? 295  ASN   A C      1 
ATOM   2298 O O      . ASN   A  1 303 ? 35.633 -52.393  -18.985 1.00 44.90  ? 295  ASN   A O      1 
ATOM   2299 C CB     . ASN   A  1 303 ? 35.385 -51.584  -22.422 1.00 45.01  ? 295  ASN   A CB     1 
ATOM   2300 C CG     . ASN   A  1 303 ? 33.959 -52.085  -22.463 1.00 67.30  ? 295  ASN   A CG     1 
ATOM   2301 O OD1    . ASN   A  1 303 ? 33.176 -51.914  -21.524 1.00 59.11  ? 295  ASN   A OD1    1 
ATOM   2302 N ND2    . ASN   A  1 303 ? 33.569 -52.664  -23.589 1.00 61.10  ? 295  ASN   A ND2    1 
ATOM   2303 N N      . ALA   A  1 304 ? 35.905 -50.269  -19.738 1.00 41.14  ? 296  ALA   A N      1 
ATOM   2304 C CA     . ALA   A  1 304 ? 35.590 -49.580  -18.481 1.00 40.39  ? 296  ALA   A CA     1 
ATOM   2305 C C      . ALA   A  1 304 ? 34.220 -49.967  -17.891 1.00 43.53  ? 296  ALA   A C      1 
ATOM   2306 O O      . ALA   A  1 304 ? 34.123 -50.149  -16.674 1.00 44.10  ? 296  ALA   A O      1 
ATOM   2307 C CB     . ALA   A  1 304 ? 35.686 -48.075  -18.665 1.00 40.96  ? 296  ALA   A CB     1 
ATOM   2308 N N      . TYR   A  1 305 ? 33.178 -50.096  -18.749 1.00 38.14  ? 297  TYR   A N      1 
ATOM   2309 C CA     . TYR   A  1 305 ? 31.822 -50.490  -18.351 1.00 36.78  ? 297  TYR   A CA     1 
ATOM   2310 C C      . TYR   A  1 305 ? 31.825 -51.922  -17.809 1.00 40.83  ? 297  TYR   A C      1 
ATOM   2311 O O      . TYR   A  1 305 ? 31.337 -52.155  -16.702 1.00 40.34  ? 297  TYR   A O      1 
ATOM   2312 C CB     . TYR   A  1 305 ? 30.841 -50.352  -19.535 1.00 36.53  ? 297  TYR   A CB     1 
ATOM   2313 C CG     . TYR   A  1 305 ? 29.411 -50.738  -19.216 1.00 36.20  ? 297  TYR   A CG     1 
ATOM   2314 C CD1    . TYR   A  1 305 ? 28.972 -52.053  -19.361 1.00 37.74  ? 297  TYR   A CD1    1 
ATOM   2315 C CD2    . TYR   A  1 305 ? 28.479 -49.779  -18.832 1.00 36.14  ? 297  TYR   A CD2    1 
ATOM   2316 C CE1    . TYR   A  1 305 ? 27.654 -52.409  -19.085 1.00 37.42  ? 297  TYR   A CE1    1 
ATOM   2317 C CE2    . TYR   A  1 305 ? 27.158 -50.124  -18.555 1.00 36.32  ? 297  TYR   A CE2    1 
ATOM   2318 C CZ     . TYR   A  1 305 ? 26.751 -51.440  -18.681 1.00 39.76  ? 297  TYR   A CZ     1 
ATOM   2319 O OH     . TYR   A  1 305 ? 25.451 -51.778  -18.417 1.00 35.95  ? 297  TYR   A OH     1 
ATOM   2320 N N      . GLU   A  1 306 ? 32.391 -52.865  -18.588 1.00 38.51  ? 298  GLU   A N      1 
ATOM   2321 C CA     . GLU   A  1 306 ? 32.507 -54.290  -18.265 1.00 38.75  ? 298  GLU   A CA     1 
ATOM   2322 C C      . GLU   A  1 306 ? 33.329 -54.571  -17.009 1.00 43.37  ? 298  GLU   A C      1 
ATOM   2323 O O      . GLU   A  1 306 ? 33.117 -55.603  -16.381 1.00 42.97  ? 298  GLU   A O      1 
ATOM   2324 C CB     . GLU   A  1 306 ? 33.045 -55.089  -19.461 1.00 40.20  ? 298  GLU   A CB     1 
ATOM   2325 C CG     . GLU   A  1 306 ? 32.110 -55.094  -20.664 1.00 51.47  ? 298  GLU   A CG     1 
ATOM   2326 C CD     . GLU   A  1 306 ? 32.687 -55.619  -21.967 1.00 72.74  ? 298  GLU   A CD     1 
ATOM   2327 O OE1    . GLU   A  1 306 ? 33.875 -55.345  -22.260 1.00 66.13  ? 298  GLU   A OE1    1 
ATOM   2328 O OE2    . GLU   A  1 306 ? 31.925 -56.265  -22.723 1.00 66.22  ? 298  GLU   A OE2    1 
ATOM   2329 N N      . LEU   A  1 307 ? 34.251 -53.657  -16.635 1.00 41.31  ? 299  LEU   A N      1 
ATOM   2330 C CA     . LEU   A  1 307 ? 35.062 -53.777  -15.419 1.00 41.41  ? 299  LEU   A CA     1 
ATOM   2331 C C      . LEU   A  1 307 ? 34.178 -53.673  -14.173 1.00 44.62  ? 299  LEU   A C      1 
ATOM   2332 O O      . LEU   A  1 307 ? 34.407 -54.399  -13.206 1.00 44.20  ? 299  LEU   A O      1 
ATOM   2333 C CB     . LEU   A  1 307 ? 36.160 -52.702  -15.375 1.00 41.86  ? 299  LEU   A CB     1 
ATOM   2334 C CG     . LEU   A  1 307 ? 37.447 -52.998  -16.151 1.00 47.31  ? 299  LEU   A CG     1 
ATOM   2335 C CD1    . LEU   A  1 307 ? 38.219 -51.724  -16.411 1.00 47.73  ? 299  LEU   A CD1    1 
ATOM   2336 C CD2    . LEU   A  1 307 ? 38.332 -53.998  -15.408 1.00 50.05  ? 299  LEU   A CD2    1 
ATOM   2337 N N      . PHE   A  1 308 ? 33.163 -52.782  -14.204 1.00 40.26  ? 300  PHE   A N      1 
ATOM   2338 C CA     . PHE   A  1 308 ? 32.227 -52.581  -13.093 1.00 39.53  ? 300  PHE   A CA     1 
ATOM   2339 C C      . PHE   A  1 308 ? 30.996 -53.496  -13.179 1.00 41.94  ? 300  PHE   A C      1 
ATOM   2340 O O      . PHE   A  1 308 ? 30.513 -53.963  -12.149 1.00 42.04  ? 300  PHE   A O      1 
ATOM   2341 C CB     . PHE   A  1 308 ? 31.788 -51.108  -13.010 1.00 41.30  ? 300  PHE   A CB     1 
ATOM   2342 C CG     . PHE   A  1 308 ? 32.781 -50.187  -12.337 1.00 42.69  ? 300  PHE   A CG     1 
ATOM   2343 C CD1    . PHE   A  1 308 ? 32.673 -49.892  -10.981 1.00 45.47  ? 300  PHE   A CD1    1 
ATOM   2344 C CD2    . PHE   A  1 308 ? 33.813 -49.598  -13.064 1.00 44.51  ? 300  PHE   A CD2    1 
ATOM   2345 C CE1    . PHE   A  1 308 ? 33.585 -49.031  -10.359 1.00 46.58  ? 300  PHE   A CE1    1 
ATOM   2346 C CE2    . PHE   A  1 308 ? 34.729 -48.743  -12.443 1.00 47.54  ? 300  PHE   A CE2    1 
ATOM   2347 C CZ     . PHE   A  1 308 ? 34.608 -48.463  -11.094 1.00 45.97  ? 300  PHE   A CZ     1 
ATOM   2348 N N      . ALA   A  1 309 ? 30.484 -53.733  -14.398 1.00 37.75  ? 301  ALA   A N      1 
ATOM   2349 C CA     . ALA   A  1 309 ? 29.294 -54.553  -14.634 1.00 37.05  ? 301  ALA   A CA     1 
ATOM   2350 C C      . ALA   A  1 309 ? 29.523 -56.067  -14.481 1.00 39.86  ? 301  ALA   A C      1 
ATOM   2351 O O      . ALA   A  1 309 ? 28.552 -56.828  -14.470 1.00 39.21  ? 301  ALA   A O      1 
ATOM   2352 C CB     . ALA   A  1 309 ? 28.693 -54.227  -15.996 1.00 37.57  ? 301  ALA   A CB     1 
ATOM   2353 N N      . LYS   A  1 310 ? 30.798 -56.504  -14.354 1.00 36.38  ? 302  LYS   A N      1 
ATOM   2354 C CA     . LYS   A  1 310 ? 31.164 -57.920  -14.208 1.00 35.76  ? 302  LYS   A CA     1 
ATOM   2355 C C      . LYS   A  1 310 ? 30.562 -58.505  -12.937 1.00 36.62  ? 302  LYS   A C      1 
ATOM   2356 O O      . LYS   A  1 310 ? 30.702 -57.917  -11.867 1.00 36.08  ? 302  LYS   A O      1 
ATOM   2357 C CB     . LYS   A  1 310 ? 32.696 -58.112  -14.254 1.00 39.04  ? 302  LYS   A CB     1 
ATOM   2358 C CG     . LYS   A  1 310 ? 33.160 -59.559  -14.473 1.00 51.34  ? 302  LYS   A CG     1 
ATOM   2359 C CD     . LYS   A  1 310 ? 32.957 -60.038  -15.916 1.00 62.92  ? 302  LYS   A CD     1 
ATOM   2360 C CE     . LYS   A  1 310 ? 33.103 -61.535  -16.065 1.00 76.43  ? 302  LYS   A CE     1 
ATOM   2361 N NZ     . LYS   A  1 310 ? 34.525 -61.970  -15.998 1.00 85.62  ? 302  LYS   A NZ     1 
ATOM   2362 N N      . GLY   A  1 311 ? 29.853 -59.623  -13.089 1.00 31.37  ? 303  GLY   A N      1 
ATOM   2363 C CA     . GLY   A  1 311 ? 29.169 -60.299  -11.991 1.00 30.31  ? 303  GLY   A CA     1 
ATOM   2364 C C      . GLY   A  1 311 ? 27.694 -59.957  -11.864 1.00 32.58  ? 303  GLY   A C      1 
ATOM   2365 O O      . GLY   A  1 311 ? 26.956 -60.662  -11.173 1.00 32.46  ? 303  GLY   A O      1 
ATOM   2366 N N      . TYR   A  1 312 ? 27.243 -58.890  -12.544 1.00 28.48  ? 304  TYR   A N      1 
ATOM   2367 C CA     . TYR   A  1 312 ? 25.851 -58.430  -12.514 1.00 28.66  ? 304  TYR   A CA     1 
ATOM   2368 C C      . TYR   A  1 312 ? 25.012 -58.960  -13.689 1.00 31.74  ? 304  TYR   A C      1 
ATOM   2369 O O      . TYR   A  1 312 ? 23.834 -58.600  -13.788 1.00 31.49  ? 304  TYR   A O      1 
ATOM   2370 C CB     . TYR   A  1 312 ? 25.801 -56.896  -12.545 1.00 30.33  ? 304  TYR   A CB     1 
ATOM   2371 C CG     . TYR   A  1 312 ? 26.202 -56.200  -11.266 1.00 33.28  ? 304  TYR   A CG     1 
ATOM   2372 C CD1    . TYR   A  1 312 ? 25.248 -55.858  -10.310 1.00 35.85  ? 304  TYR   A CD1    1 
ATOM   2373 C CD2    . TYR   A  1 312 ? 27.509 -55.763  -11.069 1.00 34.19  ? 304  TYR   A CD2    1 
ATOM   2374 C CE1    . TYR   A  1 312 ? 25.595 -55.142  -9.165  1.00 38.11  ? 304  TYR   A CE1    1 
ATOM   2375 C CE2    . TYR   A  1 312 ? 27.872 -55.063  -9.918  1.00 35.07  ? 304  TYR   A CE2    1 
ATOM   2376 C CZ     . TYR   A  1 312 ? 26.912 -54.759  -8.967  1.00 44.91  ? 304  TYR   A CZ     1 
ATOM   2377 O OH     . TYR   A  1 312 ? 27.258 -54.077  -7.828  1.00 48.57  ? 304  TYR   A OH     1 
ATOM   2378 N N      . GLU   A  1 313 ? 25.616 -59.764  -14.599 1.00 27.04  ? 305  GLU   A N      1 
ATOM   2379 C CA     . GLU   A  1 313 ? 24.937 -60.288  -15.791 1.00 26.43  ? 305  GLU   A CA     1 
ATOM   2380 C C      . GLU   A  1 313 ? 23.683 -61.044  -15.420 1.00 29.54  ? 305  GLU   A C      1 
ATOM   2381 O O      . GLU   A  1 313 ? 23.731 -61.943  -14.576 1.00 28.43  ? 305  GLU   A O      1 
ATOM   2382 C CB     . GLU   A  1 313 ? 25.859 -61.181  -16.651 1.00 27.60  ? 305  GLU   A CB     1 
ATOM   2383 C CG     . GLU   A  1 313 ? 27.057 -60.447  -17.237 1.00 36.33  ? 305  GLU   A CG     1 
ATOM   2384 C CD     . GLU   A  1 313 ? 28.324 -60.451  -16.397 1.00 55.35  ? 305  GLU   A CD     1 
ATOM   2385 O OE1    . GLU   A  1 313 ? 28.277 -60.879  -15.219 1.00 38.49  ? 305  GLU   A OE1    1 
ATOM   2386 O OE2    . GLU   A  1 313 ? 29.376 -60.027  -16.930 1.00 52.16  ? 305  GLU   A OE2    1 
ATOM   2387 N N      . ASP   A  1 314 ? 22.541 -60.609  -15.990 1.00 26.22  ? 306  ASP   A N      1 
ATOM   2388 C CA     . ASP   A  1 314 ? 21.203 -61.189  -15.804 1.00 25.99  ? 306  ASP   A CA     1 
ATOM   2389 C C      . ASP   A  1 314 ? 20.775 -61.350  -14.328 1.00 29.09  ? 306  ASP   A C      1 
ATOM   2390 O O      . ASP   A  1 314 ? 19.896 -62.158  -14.011 1.00 28.79  ? 306  ASP   A O      1 
ATOM   2391 C CB     . ASP   A  1 314 ? 21.074 -62.510  -16.590 1.00 27.04  ? 306  ASP   A CB     1 
ATOM   2392 C CG     . ASP   A  1 314 ? 21.198 -62.313  -18.093 1.00 31.76  ? 306  ASP   A CG     1 
ATOM   2393 O OD1    . ASP   A  1 314 ? 20.587 -61.353  -18.623 1.00 31.01  ? 306  ASP   A OD1    1 
ATOM   2394 O OD2    . ASP   A  1 314 ? 21.901 -63.116  -18.741 1.00 35.67  ? 306  ASP   A OD2    1 
ATOM   2395 N N      . TYR   A  1 315 ? 21.373 -60.555  -13.435 1.00 25.77  ? 307  TYR   A N      1 
ATOM   2396 C CA     . TYR   A  1 315 ? 21.017 -60.578  -12.031 1.00 25.83  ? 307  TYR   A CA     1 
ATOM   2397 C C      . TYR   A  1 315 ? 19.876 -59.564  -11.843 1.00 27.15  ? 307  TYR   A C      1 
ATOM   2398 O O      . TYR   A  1 315 ? 20.039 -58.384  -12.166 1.00 26.62  ? 307  TYR   A O      1 
ATOM   2399 C CB     . TYR   A  1 315 ? 22.252 -60.276  -11.163 1.00 28.65  ? 307  TYR   A CB     1 
ATOM   2400 C CG     . TYR   A  1 315 ? 21.966 -60.114  -9.691  1.00 33.27  ? 307  TYR   A CG     1 
ATOM   2401 C CD1    . TYR   A  1 315 ? 21.712 -61.218  -8.884  1.00 36.11  ? 307  TYR   A CD1    1 
ATOM   2402 C CD2    . TYR   A  1 315 ? 22.006 -58.862  -9.088  1.00 35.21  ? 307  TYR   A CD2    1 
ATOM   2403 C CE1    . TYR   A  1 315 ? 21.459 -61.075  -7.520  1.00 38.07  ? 307  TYR   A CE1    1 
ATOM   2404 C CE2    . TYR   A  1 315 ? 21.762 -58.707  -7.725  1.00 36.69  ? 307  TYR   A CE2    1 
ATOM   2405 C CZ     . TYR   A  1 315 ? 21.475 -59.814  -6.947  1.00 47.03  ? 307  TYR   A CZ     1 
ATOM   2406 O OH     . TYR   A  1 315 ? 21.230 -59.656  -5.604  1.00 52.13  ? 307  TYR   A OH     1 
ATOM   2407 N N      . LEU   A  1 316 ? 18.702 -60.040  -11.400 1.00 22.03  ? 308  LEU   A N      1 
ATOM   2408 C CA     . LEU   A  1 316 ? 17.526 -59.185  -11.223 1.00 21.37  ? 308  LEU   A CA     1 
ATOM   2409 C C      . LEU   A  1 316 ? 17.624 -58.388  -9.945  1.00 26.05  ? 308  LEU   A C      1 
ATOM   2410 O O      . LEU   A  1 316 ? 17.890 -58.948  -8.875  1.00 24.90  ? 308  LEU   A O      1 
ATOM   2411 C CB     . LEU   A  1 316 ? 16.208 -59.984  -11.218 1.00 20.77  ? 308  LEU   A CB     1 
ATOM   2412 C CG     . LEU   A  1 316 ? 15.807 -60.779  -12.465 1.00 23.92  ? 308  LEU   A CG     1 
ATOM   2413 C CD1    . LEU   A  1 316 ? 14.546 -61.563  -12.183 1.00 23.15  ? 308  LEU   A CD1    1 
ATOM   2414 C CD2    . LEU   A  1 316 ? 15.600 -59.869  -13.696 1.00 23.68  ? 308  LEU   A CD2    1 
ATOM   2415 N N      . GLN   A  1 317 ? 17.404 -57.071  -10.051 1.00 23.13  ? 309  GLN   A N      1 
ATOM   2416 C CA     . GLN   A  1 317 ? 17.431 -56.184  -8.889  1.00 23.24  ? 309  GLN   A CA     1 
ATOM   2417 C C      . GLN   A  1 317 ? 16.103 -55.449  -8.837  1.00 29.85  ? 309  GLN   A C      1 
ATOM   2418 O O      . GLN   A  1 317 ? 15.608 -55.002  -9.871  1.00 28.97  ? 309  GLN   A O      1 
ATOM   2419 C CB     . GLN   A  1 317 ? 18.619 -55.194  -8.969  1.00 24.13  ? 309  GLN   A CB     1 
ATOM   2420 C CG     . GLN   A  1 317 ? 19.965 -55.903  -9.108  1.00 33.48  ? 309  GLN   A CG     1 
ATOM   2421 C CD     . GLN   A  1 317 ? 21.164 -54.999  -9.157  1.00 44.64  ? 309  GLN   A CD     1 
ATOM   2422 O OE1    . GLN   A  1 317 ? 21.473 -54.294  -8.199  1.00 40.05  ? 309  GLN   A OE1    1 
ATOM   2423 N NE2    . GLN   A  1 317 ? 21.936 -55.097  -10.228 1.00 35.27  ? 309  GLN   A NE2    1 
ATOM   2424 N N      . SER   A  1 318 ? 15.500 -55.353  -7.647  1.00 29.17  ? 310  SER   A N      1 
ATOM   2425 C CA     . SER   A  1 318 ? 14.240 -54.630  -7.482  1.00 30.42  ? 310  SER   A CA     1 
ATOM   2426 C C      . SER   A  1 318 ? 14.559 -53.133  -7.583  1.00 34.43  ? 310  SER   A C      1 
ATOM   2427 O O      . SER   A  1 318 ? 15.567 -52.720  -7.004  1.00 36.15  ? 310  SER   A O      1 
ATOM   2428 C CB     . SER   A  1 318 ? 13.596 -54.964  -6.136  1.00 36.03  ? 310  SER   A CB     1 
ATOM   2429 O OG     . SER   A  1 318 ? 14.536 -54.873  -5.080  1.00 48.13  ? 310  SER   A OG     1 
ATOM   2430 N N      . PRO   A  1 319 ? 13.834 -52.316  -8.391  1.00 29.64  ? 311  PRO   A N      1 
ATOM   2431 C CA     . PRO   A  1 319 ? 14.179 -50.887  -8.467  1.00 29.70  ? 311  PRO   A CA     1 
ATOM   2432 C C      . PRO   A  1 319 ? 13.940 -50.228  -7.113  1.00 34.41  ? 311  PRO   A C      1 
ATOM   2433 O O      . PRO   A  1 319 ? 13.040 -50.633  -6.362  1.00 33.13  ? 311  PRO   A O      1 
ATOM   2434 C CB     . PRO   A  1 319 ? 13.237 -50.332  -9.545  1.00 31.25  ? 311  PRO   A CB     1 
ATOM   2435 C CG     . PRO   A  1 319 ? 12.636 -51.527  -10.210 1.00 35.17  ? 311  PRO   A CG     1 
ATOM   2436 C CD     . PRO   A  1 319 ? 12.620 -52.599  -9.174  1.00 31.06  ? 311  PRO   A CD     1 
ATOM   2437 N N      . LEU   A  1 320 ? 14.786 -49.257  -6.776  1.00 31.96  ? 312  LEU   A N      1 
ATOM   2438 C CA     . LEU   A  1 320 ? 14.701 -48.563  -5.495  1.00 31.57  ? 312  LEU   A CA     1 
ATOM   2439 C C      . LEU   A  1 320 ? 13.441 -47.692  -5.372  1.00 30.79  ? 312  LEU   A C      1 
ATOM   2440 O O      . LEU   A  1 320 ? 12.850 -47.332  -6.384  1.00 29.93  ? 312  LEU   A O      1 
ATOM   2441 C CB     . LEU   A  1 320 ? 15.986 -47.737  -5.244  1.00 32.25  ? 312  LEU   A CB     1 
ATOM   2442 C CG     . LEU   A  1 320 ? 16.443 -46.773  -6.358  1.00 36.99  ? 312  LEU   A CG     1 
ATOM   2443 C CD1    . LEU   A  1 320 ? 15.858 -45.390  -6.172  1.00 37.72  ? 312  LEU   A CD1    1 
ATOM   2444 C CD2    . LEU   A  1 320 ? 17.954 -46.675  -6.404  1.00 38.55  ? 312  LEU   A CD2    1 
ATOM   2445 N N      . GLN   A  1 321 ? 13.013 -47.415  -4.125  1.00 25.28  ? 313  GLN   A N      1 
ATOM   2446 C CA     . GLN   A  1 321 ? 11.923 -46.504  -3.802  1.00 23.01  ? 313  GLN   A CA     1 
ATOM   2447 C C      . GLN   A  1 321 ? 12.664 -45.194  -3.582  1.00 24.45  ? 313  GLN   A C      1 
ATOM   2448 O O      . GLN   A  1 321 ? 13.353 -45.052  -2.566  1.00 22.05  ? 313  GLN   A O      1 
ATOM   2449 C CB     . GLN   A  1 321 ? 11.168 -46.945  -2.540  1.00 23.82  ? 313  GLN   A CB     1 
ATOM   2450 C CG     . GLN   A  1 321 ? 10.119 -48.035  -2.787  1.00 31.09  ? 313  GLN   A CG     1 
ATOM   2451 C CD     . GLN   A  1 321 ? 9.002  -47.626  -3.727  1.00 34.33  ? 313  GLN   A CD     1 
ATOM   2452 O OE1    . GLN   A  1 321 ? 8.622  -46.455  -3.822  1.00 25.55  ? 313  GLN   A OE1    1 
ATOM   2453 N NE2    . GLN   A  1 321 ? 8.435  -48.599  -4.434  1.00 25.31  ? 313  GLN   A NE2    1 
ATOM   2454 N N      . PRO   A  1 322 ? 12.684 -44.291  -4.587  1.00 21.80  ? 314  PRO   A N      1 
ATOM   2455 C CA     . PRO   A  1 322 ? 13.513 -43.078  -4.459  1.00 21.99  ? 314  PRO   A CA     1 
ATOM   2456 C C      . PRO   A  1 322 ? 13.115 -42.117  -3.359  1.00 26.47  ? 314  PRO   A C      1 
ATOM   2457 O O      . PRO   A  1 322 ? 13.974 -41.407  -2.853  1.00 24.50  ? 314  PRO   A O      1 
ATOM   2458 C CB     . PRO   A  1 322 ? 13.397 -42.427  -5.834  1.00 23.77  ? 314  PRO   A CB     1 
ATOM   2459 C CG     . PRO   A  1 322 ? 12.083 -42.901  -6.365  1.00 27.70  ? 314  PRO   A CG     1 
ATOM   2460 C CD     . PRO   A  1 322 ? 11.970 -44.311  -5.881  1.00 23.05  ? 314  PRO   A CD     1 
ATOM   2461 N N      . LEU   A  1 323 ? 11.829 -42.093  -2.999  1.00 24.32  ? 315  LEU   A N      1 
ATOM   2462 C CA     . LEU   A  1 323 ? 11.334 -41.146  -2.021  1.00 25.37  ? 315  LEU   A CA     1 
ATOM   2463 C C      . LEU   A  1 323 ? 11.064 -41.766  -0.652  1.00 30.88  ? 315  LEU   A C      1 
ATOM   2464 O O      . LEU   A  1 323 ? 11.400 -41.157  0.359   1.00 31.64  ? 315  LEU   A O      1 
ATOM   2465 C CB     . LEU   A  1 323 ? 10.102 -40.407  -2.586  1.00 25.72  ? 315  LEU   A CB     1 
ATOM   2466 C CG     . LEU   A  1 323 ? 10.342 -39.640  -3.907  1.00 31.06  ? 315  LEU   A CG     1 
ATOM   2467 C CD1    . LEU   A  1 323 ? 9.094  -38.987  -4.395  1.00 31.09  ? 315  LEU   A CD1    1 
ATOM   2468 C CD2    . LEU   A  1 323 ? 11.445 -38.586  -3.763  1.00 34.69  ? 315  LEU   A CD2    1 
ATOM   2469 N N      . MET   A  1 324 ? 10.548 -42.987  -0.615  1.00 28.05  ? 316  MET   A N      1 
ATOM   2470 C CA     . MET   A  1 324 ? 10.225 -43.683  0.631   1.00 28.91  ? 316  MET   A CA     1 
ATOM   2471 C C      . MET   A  1 324 ? 11.439 -44.258  1.374   1.00 30.63  ? 316  MET   A C      1 
ATOM   2472 O O      . MET   A  1 324 ? 11.385 -44.412  2.589   1.00 31.63  ? 316  MET   A O      1 
ATOM   2473 C CB     . MET   A  1 324 ? 9.178  -44.772  0.366   1.00 32.36  ? 316  MET   A CB     1 
ATOM   2474 C CG     . MET   A  1 324 ? 7.950  -44.237  -0.343  1.00 37.90  ? 316  MET   A CG     1 
ATOM   2475 S SD     . MET   A  1 324 ? 6.472  -45.250  -0.197  1.00 44.69  ? 316  MET   A SD     1 
ATOM   2476 C CE     . MET   A  1 324 ? 7.043  -46.804  -0.872  1.00 41.35  ? 316  MET   A CE     1 
ATOM   2477 N N      . ASP   A  1 325 ? 12.513 -44.586  0.655   1.00 24.00  ? 317  ASP   A N      1 
ATOM   2478 C CA     . ASP   A  1 325 ? 13.731 -45.139  1.241   1.00 22.91  ? 317  ASP   A CA     1 
ATOM   2479 C C      . ASP   A  1 325 ? 14.902 -44.188  1.050   1.00 23.57  ? 317  ASP   A C      1 
ATOM   2480 O O      . ASP   A  1 325 ? 14.874 -43.339  0.157   1.00 21.56  ? 317  ASP   A O      1 
ATOM   2481 C CB     . ASP   A  1 325 ? 14.071 -46.504  0.600   1.00 25.38  ? 317  ASP   A CB     1 
ATOM   2482 C CG     . ASP   A  1 325 ? 13.029 -47.608  0.776   1.00 39.90  ? 317  ASP   A CG     1 
ATOM   2483 O OD1    . ASP   A  1 325 ? 12.078 -47.417  1.576   1.00 42.23  ? 317  ASP   A OD1    1 
ATOM   2484 O OD2    . ASP   A  1 325 ? 13.151 -48.652  0.098   1.00 43.78  ? 317  ASP   A OD2    1 
ATOM   2485 N N      . ASN   A  1 326 ? 15.935 -44.350  1.875   1.00 19.67  ? 318  ASN   A N      1 
ATOM   2486 C CA     . ASN   A  1 326 ? 17.155 -43.564  1.783   1.00 19.92  ? 318  ASN   A CA     1 
ATOM   2487 C C      . ASN   A  1 326 ? 18.306 -44.445  1.349   1.00 23.24  ? 318  ASN   A C      1 
ATOM   2488 O O      . ASN   A  1 326 ? 18.460 -45.562  1.843   1.00 22.24  ? 318  ASN   A O      1 
ATOM   2489 C CB     . ASN   A  1 326 ? 17.459 -42.803  3.086   1.00 17.90  ? 318  ASN   A CB     1 
ATOM   2490 C CG     . ASN   A  1 326 ? 16.554 -41.616  3.312   1.00 25.72  ? 318  ASN   A CG     1 
ATOM   2491 O OD1    . ASN   A  1 326 ? 16.280 -40.799  2.412   1.00 23.49  ? 318  ASN   A OD1    1 
ATOM   2492 N ND2    . ASN   A  1 326 ? 16.043 -41.508  4.519   1.00 21.16  ? 318  ASN   A ND2    1 
ATOM   2493 N N      . LEU   A  1 327 ? 19.099 -43.947  0.403   1.00 20.16  ? 319  LEU   A N      1 
ATOM   2494 C CA     . LEU   A  1 327 ? 20.249 -44.670  -0.141  1.00 20.55  ? 319  LEU   A CA     1 
ATOM   2495 C C      . LEU   A  1 327 ? 21.370 -44.888  0.879   1.00 24.53  ? 319  LEU   A C      1 
ATOM   2496 O O      . LEU   A  1 327 ? 21.617 -44.024  1.714   1.00 24.47  ? 319  LEU   A O      1 
ATOM   2497 C CB     . LEU   A  1 327 ? 20.785 -43.938  -1.388  1.00 20.52  ? 319  LEU   A CB     1 
ATOM   2498 C CG     . LEU   A  1 327 ? 19.862 -43.965  -2.615  1.00 24.25  ? 319  LEU   A CG     1 
ATOM   2499 C CD1    . LEU   A  1 327 ? 20.075 -42.755  -3.490  1.00 24.55  ? 319  LEU   A CD1    1 
ATOM   2500 C CD2    . LEU   A  1 327 ? 20.010 -45.250  -3.392  1.00 24.76  ? 319  LEU   A CD2    1 
ATOM   2501 N N      . GLU   A  1 328 ? 22.031 -46.050  0.815   1.00 21.43  ? 320  GLU   A N      1 
ATOM   2502 C CA     . GLU   A  1 328 ? 23.158 -46.397  1.682   1.00 21.33  ? 320  GLU   A CA     1 
ATOM   2503 C C      . GLU   A  1 328 ? 24.421 -45.654  1.262   1.00 25.00  ? 320  GLU   A C      1 
ATOM   2504 O O      . GLU   A  1 328 ? 24.537 -45.232  0.117   1.00 25.47  ? 320  GLU   A O      1 
ATOM   2505 C CB     . GLU   A  1 328 ? 23.399 -47.902  1.665   1.00 23.15  ? 320  GLU   A CB     1 
ATOM   2506 C CG     . GLU   A  1 328 ? 22.324 -48.673  2.414   1.00 37.84  ? 320  GLU   A CG     1 
ATOM   2507 C CD     . GLU   A  1 328 ? 22.485 -50.180  2.378   1.00 69.94  ? 320  GLU   A CD     1 
ATOM   2508 O OE1    . GLU   A  1 328 ? 21.661 -50.846  1.712   1.00 69.44  ? 320  GLU   A OE1    1 
ATOM   2509 O OE2    . GLU   A  1 328 ? 23.421 -50.696  3.031   1.00 72.48  ? 320  GLU   A OE2    1 
ATOM   2510 N N      . SER   A  1 329 ? 25.376 -45.521  2.180   1.00 22.31  ? 321  SER   A N      1 
ATOM   2511 C CA     . SER   A  1 329 ? 26.639 -44.831  1.949   1.00 22.01  ? 321  SER   A CA     1 
ATOM   2512 C C      . SER   A  1 329 ? 27.425 -45.445  0.793   1.00 24.96  ? 321  SER   A C      1 
ATOM   2513 O O      . SER   A  1 329 ? 27.868 -44.708  -0.094  1.00 22.88  ? 321  SER   A O      1 
ATOM   2514 C CB     . SER   A  1 329 ? 27.467 -44.807  3.229   1.00 25.84  ? 321  SER   A CB     1 
ATOM   2515 O OG     . SER   A  1 329 ? 28.737 -44.223  3.008   1.00 33.06  ? 321  SER   A OG     1 
ATOM   2516 N N      . GLN   A  1 330 ? 27.554 -46.790  0.780   1.00 21.03  ? 322  GLN   A N      1 
ATOM   2517 C CA     . GLN   A  1 330 ? 28.268 -47.512  -0.277  1.00 21.00  ? 322  GLN   A CA     1 
ATOM   2518 C C      . GLN   A  1 330 ? 27.586 -47.445  -1.652  1.00 24.88  ? 322  GLN   A C      1 
ATOM   2519 O O      . GLN   A  1 330 ? 28.271 -47.624  -2.656  1.00 25.13  ? 322  GLN   A O      1 
ATOM   2520 C CB     . GLN   A  1 330 ? 28.554 -48.961  0.113   1.00 21.73  ? 322  GLN   A CB     1 
ATOM   2521 C CG     . GLN   A  1 330 ? 29.877 -49.141  0.844   1.00 32.05  ? 322  GLN   A CG     1 
ATOM   2522 C CD     . GLN   A  1 330 ? 30.027 -50.547  1.376   1.00 50.30  ? 322  GLN   A CD     1 
ATOM   2523 O OE1    . GLN   A  1 330 ? 29.992 -51.532  0.636   1.00 50.34  ? 322  GLN   A OE1    1 
ATOM   2524 N NE2    . GLN   A  1 330 ? 30.163 -50.677  2.678   1.00 34.85  ? 322  GLN   A NE2    1 
ATOM   2525 N N      . THR   A  1 331 ? 26.262 -47.185  -1.708  1.00 21.13  ? 323  THR   A N      1 
ATOM   2526 C CA     . THR   A  1 331 ? 25.565 -47.029  -2.990  1.00 20.67  ? 323  THR   A CA     1 
ATOM   2527 C C      . THR   A  1 331 ? 26.050 -45.707  -3.621  1.00 23.25  ? 323  THR   A C      1 
ATOM   2528 O O      . THR   A  1 331 ? 26.435 -45.696  -4.793  1.00 22.32  ? 323  THR   A O      1 
ATOM   2529 C CB     . THR   A  1 331 ? 24.034 -47.122  -2.820  1.00 25.49  ? 323  THR   A CB     1 
ATOM   2530 O OG1    . THR   A  1 331 ? 23.709 -48.377  -2.213  1.00 23.89  ? 323  THR   A OG1    1 
ATOM   2531 C CG2    . THR   A  1 331 ? 23.293 -46.984  -4.145  1.00 20.83  ? 323  THR   A CG2    1 
ATOM   2532 N N      . TYR   A  1 332 ? 26.080 -44.612  -2.822  1.00 19.61  ? 324  TYR   A N      1 
ATOM   2533 C CA     . TYR   A  1 332 ? 26.581 -43.307  -3.266  1.00 18.70  ? 324  TYR   A CA     1 
ATOM   2534 C C      . TYR   A  1 332 ? 28.034 -43.448  -3.676  1.00 25.68  ? 324  TYR   A C      1 
ATOM   2535 O O      . TYR   A  1 332 ? 28.415 -42.904  -4.702  1.00 26.60  ? 324  TYR   A O      1 
ATOM   2536 C CB     . TYR   A  1 332 ? 26.513 -42.255  -2.154  1.00 18.09  ? 324  TYR   A CB     1 
ATOM   2537 C CG     . TYR   A  1 332 ? 25.133 -41.723  -1.843  1.00 18.05  ? 324  TYR   A CG     1 
ATOM   2538 C CD1    . TYR   A  1 332 ? 24.402 -41.026  -2.800  1.00 19.08  ? 324  TYR   A CD1    1 
ATOM   2539 C CD2    . TYR   A  1 332 ? 24.591 -41.843  -0.567  1.00 18.22  ? 324  TYR   A CD2    1 
ATOM   2540 C CE1    . TYR   A  1 332 ? 23.131 -40.532  -2.517  1.00 19.13  ? 324  TYR   A CE1    1 
ATOM   2541 C CE2    . TYR   A  1 332 ? 23.333 -41.324  -0.263  1.00 18.67  ? 324  TYR   A CE2    1 
ATOM   2542 C CZ     . TYR   A  1 332 ? 22.601 -40.682  -1.243  1.00 21.13  ? 324  TYR   A CZ     1 
ATOM   2543 O OH     . TYR   A  1 332 ? 21.364 -40.165  -0.943  1.00 18.98  ? 324  TYR   A OH     1 
ATOM   2544 N N      . GLU   A  1 333 ? 28.831 -44.203  -2.885  1.00 23.06  ? 325  GLU   A N      1 
ATOM   2545 C CA     . GLU   A  1 333 ? 30.250 -44.434  -3.119  1.00 22.80  ? 325  GLU   A CA     1 
ATOM   2546 C C      . GLU   A  1 333 ? 30.563 -45.030  -4.502  1.00 26.17  ? 325  GLU   A C      1 
ATOM   2547 O O      . GLU   A  1 333 ? 31.427 -44.493  -5.201  1.00 26.14  ? 325  GLU   A O      1 
ATOM   2548 C CB     . GLU   A  1 333 ? 30.850 -45.280  -1.991  1.00 23.73  ? 325  GLU   A CB     1 
ATOM   2549 C CG     . GLU   A  1 333 ? 32.351 -45.471  -2.101  1.00 33.11  ? 325  GLU   A CG     1 
ATOM   2550 C CD     . GLU   A  1 333 ? 32.966 -46.432  -1.105  1.00 54.85  ? 325  GLU   A CD     1 
ATOM   2551 O OE1    . GLU   A  1 333 ? 32.303 -47.432  -0.745  1.00 46.96  ? 325  GLU   A OE1    1 
ATOM   2552 O OE2    . GLU   A  1 333 ? 34.132 -46.202  -0.709  1.00 54.31  ? 325  GLU   A OE2    1 
ATOM   2553 N N      . VAL   A  1 334 ? 29.890 -46.128  -4.889  1.00 21.41  ? 326  VAL   A N      1 
ATOM   2554 C CA     . VAL   A  1 334 ? 30.156 -46.781  -6.176  1.00 20.42  ? 326  VAL   A CA     1 
ATOM   2555 C C      . VAL   A  1 334 ? 29.767 -45.896  -7.362  1.00 22.76  ? 326  VAL   A C      1 
ATOM   2556 O O      . VAL   A  1 334 ? 30.525 -45.819  -8.324  1.00 22.53  ? 326  VAL   A O      1 
ATOM   2557 C CB     . VAL   A  1 334 ? 29.562 -48.217  -6.287  1.00 24.39  ? 326  VAL   A CB     1 
ATOM   2558 C CG1    . VAL   A  1 334 ? 28.033 -48.217  -6.236  1.00 23.99  ? 326  VAL   A CG1    1 
ATOM   2559 C CG2    . VAL   A  1 334 ? 30.069 -48.939  -7.543  1.00 23.99  ? 326  VAL   A CG2    1 
ATOM   2560 N N      . PHE   A  1 335 ? 28.616 -45.212  -7.288  1.00 19.11  ? 327  PHE   A N      1 
ATOM   2561 C CA     . PHE   A  1 335 ? 28.162 -44.386  -8.388  1.00 18.74  ? 327  PHE   A CA     1 
ATOM   2562 C C      . PHE   A  1 335 ? 29.007 -43.130  -8.574  1.00 25.02  ? 327  PHE   A C      1 
ATOM   2563 O O      . PHE   A  1 335 ? 29.079 -42.630  -9.694  1.00 25.25  ? 327  PHE   A O      1 
ATOM   2564 C CB     . PHE   A  1 335 ? 26.663 -44.084  -8.282  1.00 19.67  ? 327  PHE   A CB     1 
ATOM   2565 C CG     . PHE   A  1 335 ? 25.820 -45.319  -8.523  1.00 20.23  ? 327  PHE   A CG     1 
ATOM   2566 C CD1    . PHE   A  1 335 ? 25.955 -46.060  -9.695  1.00 21.79  ? 327  PHE   A CD1    1 
ATOM   2567 C CD2    . PHE   A  1 335 ? 24.879 -45.733  -7.587  1.00 21.05  ? 327  PHE   A CD2    1 
ATOM   2568 C CE1    . PHE   A  1 335 ? 25.185 -47.201  -9.911  1.00 21.77  ? 327  PHE   A CE1    1 
ATOM   2569 C CE2    . PHE   A  1 335 ? 24.105 -46.876  -7.809  1.00 23.16  ? 327  PHE   A CE2    1 
ATOM   2570 C CZ     . PHE   A  1 335 ? 24.259 -47.597  -8.969  1.00 20.56  ? 327  PHE   A CZ     1 
ATOM   2571 N N      . GLU   A  1 336 ? 29.723 -42.685  -7.517  1.00 23.31  ? 328  GLU   A N      1 
ATOM   2572 C CA     . GLU   A  1 336 ? 30.621 -41.515  -7.567  1.00 22.89  ? 328  GLU   A CA     1 
ATOM   2573 C C      . GLU   A  1 336 ? 31.849 -41.807  -8.435  1.00 27.51  ? 328  GLU   A C      1 
ATOM   2574 O O      . GLU   A  1 336 ? 32.530 -40.881  -8.865  1.00 26.55  ? 328  GLU   A O      1 
ATOM   2575 C CB     . GLU   A  1 336 ? 31.081 -41.135  -6.165  1.00 23.37  ? 328  GLU   A CB     1 
ATOM   2576 C CG     . GLU   A  1 336 ? 30.134 -40.216  -5.422  1.00 30.19  ? 328  GLU   A CG     1 
ATOM   2577 C CD     . GLU   A  1 336 ? 30.281 -40.282  -3.911  1.00 44.96  ? 328  GLU   A CD     1 
ATOM   2578 O OE1    . GLU   A  1 336 ? 31.354 -40.701  -3.416  1.00 42.17  ? 328  GLU   A OE1    1 
ATOM   2579 O OE2    . GLU   A  1 336 ? 29.314 -39.900  -3.217  1.00 32.67  ? 328  GLU   A OE2    1 
ATOM   2580 N N      . LYS   A  1 337 ? 32.115 -43.098  -8.683  1.00 25.72  ? 329  LYS   A N      1 
ATOM   2581 C CA     . LYS   A  1 337 ? 33.212 -43.594  -9.516  1.00 25.78  ? 329  LYS   A CA     1 
ATOM   2582 C C      . LYS   A  1 337 ? 32.868 -43.615  -11.014 1.00 30.81  ? 329  LYS   A C      1 
ATOM   2583 O O      . LYS   A  1 337 ? 33.709 -44.042  -11.807 1.00 31.15  ? 329  LYS   A O      1 
ATOM   2584 C CB     . LYS   A  1 337 ? 33.673 -44.978  -9.033  1.00 27.71  ? 329  LYS   A CB     1 
ATOM   2585 C CG     . LYS   A  1 337 ? 34.196 -44.980  -7.602  1.00 33.77  ? 329  LYS   A CG     1 
ATOM   2586 C CD     . LYS   A  1 337 ? 34.638 -46.366  -7.158  1.00 42.17  ? 329  LYS   A CD     1 
ATOM   2587 C CE     . LYS   A  1 337 ? 35.082 -46.362  -5.713  1.00 53.00  ? 329  LYS   A CE     1 
ATOM   2588 N NZ     . LYS   A  1 337 ? 35.211 -47.740  -5.169  1.00 62.34  ? 329  LYS   A NZ     1 
ATOM   2589 N N      . ASP   A  1 338 ? 31.664 -43.121  -11.420 1.00 27.44  ? 330  ASP   A N      1 
ATOM   2590 C CA     . ASP   A  1 338 ? 31.280 -43.080  -12.843 1.00 26.63  ? 330  ASP   A CA     1 
ATOM   2591 C C      . ASP   A  1 338 ? 32.283 -42.207  -13.643 1.00 30.97  ? 330  ASP   A C      1 
ATOM   2592 O O      . ASP   A  1 338 ? 32.483 -41.035  -13.303 1.00 28.91  ? 330  ASP   A O      1 
ATOM   2593 C CB     . ASP   A  1 338 ? 29.834 -42.599  -13.058 1.00 27.19  ? 330  ASP   A CB     1 
ATOM   2594 C CG     . ASP   A  1 338 ? 29.312 -42.962  -14.440 1.00 32.20  ? 330  ASP   A CG     1 
ATOM   2595 O OD1    . ASP   A  1 338 ? 29.773 -42.350  -15.435 1.00 32.62  ? 330  ASP   A OD1    1 
ATOM   2596 O OD2    . ASP   A  1 338 ? 28.473 -43.874  -14.535 1.00 31.91  ? 330  ASP   A OD2    1 
ATOM   2597 N N      . PRO   A  1 339 ? 32.932 -42.775  -14.689 1.00 29.04  ? 331  PRO   A N      1 
ATOM   2598 C CA     . PRO   A  1 339 ? 33.978 -42.012  -15.401 1.00 29.29  ? 331  PRO   A CA     1 
ATOM   2599 C C      . PRO   A  1 339 ? 33.509 -40.910  -16.349 1.00 34.35  ? 331  PRO   A C      1 
ATOM   2600 O O      . PRO   A  1 339 ? 34.345 -40.104  -16.781 1.00 35.23  ? 331  PRO   A O      1 
ATOM   2601 C CB     . PRO   A  1 339 ? 34.748 -43.102  -16.154 1.00 31.16  ? 331  PRO   A CB     1 
ATOM   2602 C CG     . PRO   A  1 339 ? 33.716 -44.167  -16.420 1.00 35.12  ? 331  PRO   A CG     1 
ATOM   2603 C CD     . PRO   A  1 339 ? 32.836 -44.163  -15.194 1.00 30.32  ? 331  PRO   A CD     1 
ATOM   2604 N N      . ILE   A  1 340 ? 32.195 -40.846  -16.669 1.00 29.52  ? 332  ILE   A N      1 
ATOM   2605 C CA     . ILE   A  1 340 ? 31.695 -39.870  -17.635 1.00 28.09  ? 332  ILE   A CA     1 
ATOM   2606 C C      . ILE   A  1 340 ? 30.494 -39.052  -17.154 1.00 30.20  ? 332  ILE   A C      1 
ATOM   2607 O O      . ILE   A  1 340 ? 30.331 -37.927  -17.620 1.00 29.46  ? 332  ILE   A O      1 
ATOM   2608 C CB     . ILE   A  1 340 ? 31.404 -40.575  -18.990 1.00 30.89  ? 332  ILE   A CB     1 
ATOM   2609 C CG1    . ILE   A  1 340 ? 31.369 -39.554  -20.174 1.00 32.16  ? 332  ILE   A CG1    1 
ATOM   2610 C CG2    . ILE   A  1 340 ? 30.140 -41.455  -18.922 1.00 30.32  ? 332  ILE   A CG2    1 
ATOM   2611 C CD1    . ILE   A  1 340 ? 31.422 -40.151  -21.598 1.00 37.34  ? 332  ILE   A CD1    1 
ATOM   2612 N N      . LYS   A  1 341 ? 29.639 -39.606  -16.267 1.00 26.26  ? 333  LYS   A N      1 
ATOM   2613 C CA     . LYS   A  1 341 ? 28.442 -38.892  -15.815 1.00 25.43  ? 333  LYS   A CA     1 
ATOM   2614 C C      . LYS   A  1 341 ? 28.734 -37.487  -15.279 1.00 28.32  ? 333  LYS   A C      1 
ATOM   2615 O O      . LYS   A  1 341 ? 28.069 -36.535  -15.687 1.00 27.96  ? 333  LYS   A O      1 
ATOM   2616 C CB     . LYS   A  1 341 ? 27.653 -39.714  -14.774 1.00 27.10  ? 333  LYS   A CB     1 
ATOM   2617 C CG     . LYS   A  1 341 ? 26.204 -39.252  -14.609 1.00 28.58  ? 333  LYS   A CG     1 
ATOM   2618 C CD     . LYS   A  1 341 ? 25.562 -39.839  -13.371 1.00 34.73  ? 333  LYS   A CD     1 
ATOM   2619 C CE     . LYS   A  1 341 ? 25.563 -38.854  -12.222 1.00 40.84  ? 333  LYS   A CE     1 
ATOM   2620 N NZ     . LYS   A  1 341 ? 25.091 -39.481  -10.962 1.00 40.78  ? 333  LYS   A NZ     1 
ATOM   2621 N N      . TYR   A  1 342 ? 29.730 -37.362  -14.385 1.00 24.80  ? 334  TYR   A N      1 
ATOM   2622 C CA     . TYR   A  1 342 ? 30.059 -36.090  -13.748 1.00 25.14  ? 334  TYR   A CA     1 
ATOM   2623 C C      . TYR   A  1 342 ? 30.789 -35.124  -14.682 1.00 29.34  ? 334  TYR   A C      1 
ATOM   2624 O O      . TYR   A  1 342 ? 30.479 -33.931  -14.646 1.00 28.95  ? 334  TYR   A O      1 
ATOM   2625 C CB     . TYR   A  1 342 ? 30.805 -36.294  -12.422 1.00 26.51  ? 334  TYR   A CB     1 
ATOM   2626 C CG     . TYR   A  1 342 ? 30.045 -37.191  -11.461 1.00 28.48  ? 334  TYR   A CG     1 
ATOM   2627 C CD1    . TYR   A  1 342 ? 28.917 -36.729  -10.783 1.00 30.24  ? 334  TYR   A CD1    1 
ATOM   2628 C CD2    . TYR   A  1 342 ? 30.422 -38.517  -11.271 1.00 28.85  ? 334  TYR   A CD2    1 
ATOM   2629 C CE1    . TYR   A  1 342 ? 28.187 -37.566  -9.940  1.00 30.43  ? 334  TYR   A CE1    1 
ATOM   2630 C CE2    . TYR   A  1 342 ? 29.710 -39.356  -10.418 1.00 29.36  ? 334  TYR   A CE2    1 
ATOM   2631 C CZ     . TYR   A  1 342 ? 28.605 -38.872  -9.741  1.00 34.32  ? 334  TYR   A CZ     1 
ATOM   2632 O OH     . TYR   A  1 342 ? 27.910 -39.713  -8.905  1.00 32.97  ? 334  TYR   A OH     1 
ATOM   2633 N N      . SER   A  1 343 ? 31.694 -35.626  -15.558 1.00 26.66  ? 335  SER   A N      1 
ATOM   2634 C CA     . SER   A  1 343 ? 32.379 -34.752  -16.528 1.00 26.10  ? 335  SER   A CA     1 
ATOM   2635 C C      . SER   A  1 343 ? 31.381 -34.196  -17.548 1.00 29.27  ? 335  SER   A C      1 
ATOM   2636 O O      . SER   A  1 343 ? 31.499 -33.031  -17.936 1.00 28.78  ? 335  SER   A O      1 
ATOM   2637 C CB     . SER   A  1 343 ? 33.572 -35.442  -17.185 1.00 28.91  ? 335  SER   A CB     1 
ATOM   2638 O OG     . SER   A  1 343 ? 33.217 -36.578  -17.947 1.00 37.74  ? 335  SER   A OG     1 
ATOM   2639 N N      . GLN   A  1 344 ? 30.333 -34.984  -17.887 1.00 24.20  ? 336  GLN   A N      1 
ATOM   2640 C CA     . GLN   A  1 344 ? 29.259 -34.509  -18.751 1.00 24.24  ? 336  GLN   A CA     1 
ATOM   2641 C C      . GLN   A  1 344 ? 28.444 -33.424  -18.039 1.00 29.13  ? 336  GLN   A C      1 
ATOM   2642 O O      . GLN   A  1 344 ? 28.206 -32.366  -18.628 1.00 28.82  ? 336  GLN   A O      1 
ATOM   2643 C CB     . GLN   A  1 344 ? 28.366 -35.654  -19.256 1.00 25.57  ? 336  GLN   A CB     1 
ATOM   2644 C CG     . GLN   A  1 344 ? 29.006 -36.502  -20.357 1.00 29.58  ? 336  GLN   A CG     1 
ATOM   2645 C CD     . GLN   A  1 344 ? 29.198 -35.753  -21.653 1.00 37.98  ? 336  GLN   A CD     1 
ATOM   2646 O OE1    . GLN   A  1 344 ? 30.267 -35.195  -21.919 1.00 31.68  ? 336  GLN   A OE1    1 
ATOM   2647 N NE2    . GLN   A  1 344 ? 28.175 -35.735  -22.491 1.00 26.97  ? 336  GLN   A NE2    1 
ATOM   2648 N N      . TYR   A  1 345 ? 28.079 -33.647  -16.753 1.00 25.58  ? 337  TYR   A N      1 
ATOM   2649 C CA     . TYR   A  1 345 ? 27.358 -32.638  -15.967 1.00 24.93  ? 337  TYR   A CA     1 
ATOM   2650 C C      . TYR   A  1 345 ? 28.165 -31.329  -15.843 1.00 27.98  ? 337  TYR   A C      1 
ATOM   2651 O O      . TYR   A  1 345 ? 27.599 -30.251  -16.030 1.00 26.22  ? 337  TYR   A O      1 
ATOM   2652 C CB     . TYR   A  1 345 ? 26.970 -33.177  -14.585 1.00 25.98  ? 337  TYR   A CB     1 
ATOM   2653 C CG     . TYR   A  1 345 ? 25.570 -33.746  -14.549 1.00 26.51  ? 337  TYR   A CG     1 
ATOM   2654 C CD1    . TYR   A  1 345 ? 24.471 -32.931  -14.290 1.00 28.00  ? 337  TYR   A CD1    1 
ATOM   2655 C CD2    . TYR   A  1 345 ? 25.341 -35.101  -14.768 1.00 26.60  ? 337  TYR   A CD2    1 
ATOM   2656 C CE1    . TYR   A  1 345 ? 23.180 -33.449  -14.262 1.00 28.40  ? 337  TYR   A CE1    1 
ATOM   2657 C CE2    . TYR   A  1 345 ? 24.054 -35.632  -14.742 1.00 26.59  ? 337  TYR   A CE2    1 
ATOM   2658 C CZ     . TYR   A  1 345 ? 22.977 -34.804  -14.484 1.00 30.10  ? 337  TYR   A CZ     1 
ATOM   2659 O OH     . TYR   A  1 345 ? 21.709 -35.326  -14.464 1.00 24.86  ? 337  TYR   A OH     1 
ATOM   2660 N N      . GLN   A  1 346 ? 29.490 -31.439  -15.586 1.00 25.33  ? 338  GLN   A N      1 
ATOM   2661 C CA     . GLN   A  1 346 ? 30.397 -30.297  -15.481 1.00 25.93  ? 338  GLN   A CA     1 
ATOM   2662 C C      . GLN   A  1 346 ? 30.394 -29.501  -16.788 1.00 30.72  ? 338  GLN   A C      1 
ATOM   2663 O O      . GLN   A  1 346 ? 30.195 -28.287  -16.752 1.00 30.25  ? 338  GLN   A O      1 
ATOM   2664 C CB     . GLN   A  1 346 ? 31.825 -30.760  -15.137 1.00 27.32  ? 338  GLN   A CB     1 
ATOM   2665 C CG     . GLN   A  1 346 ? 32.773 -29.592  -14.835 1.00 32.03  ? 338  GLN   A CG     1 
ATOM   2666 C CD     . GLN   A  1 346 ? 34.201 -30.021  -14.643 1.00 44.22  ? 338  GLN   A CD     1 
ATOM   2667 O OE1    . GLN   A  1 346 ? 34.489 -31.035  -14.004 1.00 34.93  ? 338  GLN   A OE1    1 
ATOM   2668 N NE2    . GLN   A  1 346 ? 35.137 -29.228  -15.170 1.00 37.40  ? 338  GLN   A NE2    1 
ATOM   2669 N N      . GLN   A  1 347 ? 30.551 -30.202  -17.935 1.00 28.32  ? 339  GLN   A N      1 
ATOM   2670 C CA     . GLN   A  1 347 ? 30.549 -29.629  -19.280 1.00 28.32  ? 339  GLN   A CA     1 
ATOM   2671 C C      . GLN   A  1 347 ? 29.236 -28.890  -19.579 1.00 32.69  ? 339  GLN   A C      1 
ATOM   2672 O O      . GLN   A  1 347 ? 29.285 -27.786  -20.116 1.00 33.20  ? 339  GLN   A O      1 
ATOM   2673 C CB     . GLN   A  1 347 ? 30.902 -30.707  -20.329 1.00 29.82  ? 339  GLN   A CB     1 
ATOM   2674 C CG     . GLN   A  1 347 ? 31.215 -30.195  -21.740 1.00 44.95  ? 339  GLN   A CG     1 
ATOM   2675 C CD     . GLN   A  1 347 ? 32.341 -29.189  -21.849 1.00 53.86  ? 339  GLN   A CD     1 
ATOM   2676 O OE1    . GLN   A  1 347 ? 33.363 -29.270  -21.166 1.00 47.78  ? 339  GLN   A OE1    1 
ATOM   2677 N NE2    . GLN   A  1 347 ? 32.190 -28.240  -22.759 1.00 43.87  ? 339  GLN   A NE2    1 
ATOM   2678 N N      . ALA   A  1 348 ? 28.084 -29.444  -19.141 1.00 28.98  ? 340  ALA   A N      1 
ATOM   2679 C CA     . ALA   A  1 348 ? 26.751 -28.839  -19.297 1.00 28.42  ? 340  ALA   A CA     1 
ATOM   2680 C C      . ALA   A  1 348 ? 26.618 -27.542  -18.509 1.00 32.66  ? 340  ALA   A C      1 
ATOM   2681 O O      . ALA   A  1 348 ? 26.067 -26.576  -19.031 1.00 32.37  ? 340  ALA   A O      1 
ATOM   2682 C CB     . ALA   A  1 348 ? 25.666 -29.818  -18.859 1.00 28.96  ? 340  ALA   A CB     1 
ATOM   2683 N N      . ILE   A  1 349 ? 27.103 -27.523  -17.252 1.00 29.94  ? 341  ILE   A N      1 
ATOM   2684 C CA     . ILE   A  1 349 ? 27.052 -26.346  -16.369 1.00 30.12  ? 341  ILE   A CA     1 
ATOM   2685 C C      . ILE   A  1 349 ? 27.989 -25.253  -16.929 1.00 35.82  ? 341  ILE   A C      1 
ATOM   2686 O O      . ILE   A  1 349 ? 27.602 -24.086  -16.964 1.00 33.56  ? 341  ILE   A O      1 
ATOM   2687 C CB     . ILE   A  1 349 ? 27.361 -26.722  -14.888 1.00 32.92  ? 341  ILE   A CB     1 
ATOM   2688 C CG1    . ILE   A  1 349 ? 26.328 -27.762  -14.340 1.00 32.10  ? 341  ILE   A CG1    1 
ATOM   2689 C CG2    . ILE   A  1 349 ? 27.408 -25.469  -13.985 1.00 34.95  ? 341  ILE   A CG2    1 
ATOM   2690 C CD1    . ILE   A  1 349 ? 26.809 -28.584  -13.140 1.00 30.31  ? 341  ILE   A CD1    1 
ATOM   2691 N N      . TYR   A  1 350 ? 29.197 -25.658  -17.393 1.00 35.01  ? 342  TYR   A N      1 
ATOM   2692 C CA     . TYR   A  1 350 ? 30.214 -24.806  -18.011 1.00 36.43  ? 342  TYR   A CA     1 
ATOM   2693 C C      . TYR   A  1 350 ? 29.635 -24.061  -19.218 1.00 41.77  ? 342  TYR   A C      1 
ATOM   2694 O O      . TYR   A  1 350 ? 29.730 -22.832  -19.261 1.00 43.14  ? 342  TYR   A O      1 
ATOM   2695 C CB     . TYR   A  1 350 ? 31.450 -25.647  -18.387 1.00 38.72  ? 342  TYR   A CB     1 
ATOM   2696 C CG     . TYR   A  1 350 ? 32.391 -25.015  -19.392 1.00 42.11  ? 342  TYR   A CG     1 
ATOM   2697 C CD1    . TYR   A  1 350 ? 33.267 -24.000  -19.014 1.00 44.16  ? 342  TYR   A CD1    1 
ATOM   2698 C CD2    . TYR   A  1 350 ? 32.469 -25.491  -20.698 1.00 43.40  ? 342  TYR   A CD2    1 
ATOM   2699 C CE1    . TYR   A  1 350 ? 34.168 -23.447  -19.922 1.00 45.64  ? 342  TYR   A CE1    1 
ATOM   2700 C CE2    . TYR   A  1 350 ? 33.363 -24.941  -21.617 1.00 44.75  ? 342  TYR   A CE2    1 
ATOM   2701 C CZ     . TYR   A  1 350 ? 34.210 -23.917  -21.224 1.00 54.18  ? 342  TYR   A CZ     1 
ATOM   2702 O OH     . TYR   A  1 350 ? 35.098 -23.373  -22.122 1.00 59.19  ? 342  TYR   A OH     1 
ATOM   2703 N N      . LYS   A  1 351 ? 28.979 -24.793  -20.154 1.00 37.01  ? 343  LYS   A N      1 
ATOM   2704 C CA     . LYS   A  1 351 ? 28.336 -24.231  -21.348 1.00 35.95  ? 343  LYS   A CA     1 
ATOM   2705 C C      . LYS   A  1 351 ? 27.202 -23.296  -20.985 1.00 38.23  ? 343  LYS   A C      1 
ATOM   2706 O O      . LYS   A  1 351 ? 27.044 -22.256  -21.630 1.00 38.22  ? 343  LYS   A O      1 
ATOM   2707 C CB     . LYS   A  1 351 ? 27.821 -25.331  -22.291 1.00 38.01  ? 343  LYS   A CB     1 
ATOM   2708 C CG     . LYS   A  1 351 ? 28.897 -25.944  -23.172 1.00 48.03  ? 343  LYS   A CG     1 
ATOM   2709 C CD     . LYS   A  1 351 ? 28.311 -26.542  -24.444 1.00 59.12  ? 343  LYS   A CD     1 
ATOM   2710 C CE     . LYS   A  1 351 ? 29.408 -27.048  -25.351 1.00 75.45  ? 343  LYS   A CE     1 
ATOM   2711 N NZ     . LYS   A  1 351 ? 28.888 -27.478  -26.675 1.00 84.88  ? 343  LYS   A NZ     1 
ATOM   2712 N N      . CYS   A  1 352 ? 26.414 -23.657  -19.950 1.00 32.50  ? 344  CYS   A N      1 
ATOM   2713 C CA     . CYS   A  1 352 ? 25.280 -22.848  -19.494 1.00 31.38  ? 344  CYS   A CA     1 
ATOM   2714 C C      . CYS   A  1 352 ? 25.704 -21.515  -18.871 1.00 35.49  ? 344  CYS   A C      1 
ATOM   2715 O O      . CYS   A  1 352 ? 25.010 -20.512  -19.064 1.00 34.43  ? 344  CYS   A O      1 
ATOM   2716 C CB     . CYS   A  1 352 ? 24.362 -23.635  -18.563 1.00 30.77  ? 344  CYS   A CB     1 
ATOM   2717 S SG     . CYS   A  1 352 ? 22.841 -22.754  -18.123 1.00 34.42  ? 344  CYS   A SG     1 
ATOM   2718 N N      . LEU   A  1 353 ? 26.822 -21.511  -18.122 1.00 32.69  ? 345  LEU   A N      1 
ATOM   2719 C CA     . LEU   A  1 353 ? 27.348 -20.310  -17.469 1.00 33.50  ? 345  LEU   A CA     1 
ATOM   2720 C C      . LEU   A  1 353 ? 27.847 -19.282  -18.488 1.00 39.29  ? 345  LEU   A C      1 
ATOM   2721 O O      . LEU   A  1 353 ? 27.567 -18.102  -18.330 1.00 39.78  ? 345  LEU   A O      1 
ATOM   2722 C CB     . LEU   A  1 353 ? 28.463 -20.656  -16.465 1.00 33.49  ? 345  LEU   A CB     1 
ATOM   2723 C CG     . LEU   A  1 353 ? 28.040 -21.365  -15.178 1.00 37.42  ? 345  LEU   A CG     1 
ATOM   2724 C CD1    . LEU   A  1 353 ? 29.238 -21.921  -14.469 1.00 37.21  ? 345  LEU   A CD1    1 
ATOM   2725 C CD2    . LEU   A  1 353 ? 27.202 -20.455  -14.269 1.00 37.32  ? 345  LEU   A CD2    1 
ATOM   2726 N N      . LEU   A  1 354 ? 28.560 -19.736  -19.536 1.00 37.44  ? 346  LEU   A N      1 
ATOM   2727 C CA     . LEU   A  1 354 ? 29.077 -18.884  -20.611 1.00 37.85  ? 346  LEU   A CA     1 
ATOM   2728 C C      . LEU   A  1 354 ? 27.935 -18.256  -21.411 1.00 44.36  ? 346  LEU   A C      1 
ATOM   2729 O O      . LEU   A  1 354 ? 28.012 -17.072  -21.754 1.00 44.67  ? 346  LEU   A O      1 
ATOM   2730 C CB     . LEU   A  1 354 ? 30.023 -19.667  -21.540 1.00 37.78  ? 346  LEU   A CB     1 
ATOM   2731 C CG     . LEU   A  1 354 ? 31.312 -20.245  -20.922 1.00 42.60  ? 346  LEU   A CG     1 
ATOM   2732 C CD1    . LEU   A  1 354 ? 32.087 -21.041  -21.948 1.00 42.66  ? 346  LEU   A CD1    1 
ATOM   2733 C CD2    . LEU   A  1 354 ? 32.215 -19.148  -20.351 1.00 45.66  ? 346  LEU   A CD2    1 
ATOM   2734 N N      . ASP   A  1 355 ? 26.861 -19.037  -21.670 1.00 41.20  ? 347  ASP   A N      1 
ATOM   2735 C CA     . ASP   A  1 355 ? 25.675 -18.584  -22.398 1.00 41.32  ? 347  ASP   A CA     1 
ATOM   2736 C C      . ASP   A  1 355 ? 24.804 -17.643  -21.565 1.00 45.57  ? 347  ASP   A C      1 
ATOM   2737 O O      . ASP   A  1 355 ? 24.044 -16.859  -22.140 1.00 45.14  ? 347  ASP   A O      1 
ATOM   2738 C CB     . ASP   A  1 355 ? 24.827 -19.783  -22.880 1.00 43.54  ? 347  ASP   A CB     1 
ATOM   2739 C CG     . ASP   A  1 355 ? 25.403 -20.615  -24.018 1.00 55.30  ? 347  ASP   A CG     1 
ATOM   2740 O OD1    . ASP   A  1 355 ? 26.337 -20.131  -24.703 1.00 56.37  ? 347  ASP   A OD1    1 
ATOM   2741 O OD2    . ASP   A  1 355 ? 24.896 -21.734  -24.248 1.00 60.84  ? 347  ASP   A OD2    1 
ATOM   2742 N N      . ARG   A  1 356 ? 24.884 -17.738  -20.219 1.00 42.18  ? 348  ARG   A N      1 
ATOM   2743 C CA     . ARG   A  1 356 ? 24.070 -16.923  -19.317 1.00 41.87  ? 348  ARG   A CA     1 
ATOM   2744 C C      . ARG   A  1 356 ? 24.717 -15.613  -18.896 1.00 47.03  ? 348  ARG   A C      1 
ATOM   2745 O O      . ARG   A  1 356 ? 23.990 -14.642  -18.666 1.00 46.08  ? 348  ARG   A O      1 
ATOM   2746 C CB     . ARG   A  1 356 ? 23.622 -17.718  -18.081 1.00 40.63  ? 348  ARG   A CB     1 
ATOM   2747 C CG     . ARG   A  1 356 ? 22.343 -18.503  -18.339 1.00 46.24  ? 348  ARG   A CG     1 
ATOM   2748 C CD     . ARG   A  1 356 ? 21.743 -19.118  -17.083 1.00 37.62  ? 348  ARG   A CD     1 
ATOM   2749 N NE     . ARG   A  1 356 ? 20.947 -18.171  -16.295 1.00 29.14  ? 348  ARG   A NE     1 
ATOM   2750 C CZ     . ARG   A  1 356 ? 19.667 -17.883  -16.524 1.00 37.78  ? 348  ARG   A CZ     1 
ATOM   2751 N NH1    . ARG   A  1 356 ? 19.027 -18.431  -17.549 1.00 30.11  ? 348  ARG   A NH1    1 
ATOM   2752 N NH2    . ARG   A  1 356 ? 19.021 -17.034  -15.738 1.00 26.09  ? 348  ARG   A NH2    1 
ATOM   2753 N N      . VAL   A  1 357 ? 26.058 -15.581  -18.753 1.00 45.11  ? 349  VAL   A N      1 
ATOM   2754 C CA     . VAL   A  1 357 ? 26.744 -14.361  -18.322 1.00 46.38  ? 349  VAL   A CA     1 
ATOM   2755 C C      . VAL   A  1 357 ? 27.944 -14.013  -19.256 1.00 50.96  ? 349  VAL   A C      1 
ATOM   2756 O O      . VAL   A  1 357 ? 28.891 -14.797  -19.380 1.00 49.72  ? 349  VAL   A O      1 
ATOM   2757 C CB     . VAL   A  1 357 ? 27.116 -14.337  -16.804 1.00 51.48  ? 349  VAL   A CB     1 
ATOM   2758 C CG1    . VAL   A  1 357 ? 25.872 -14.194  -15.937 1.00 51.63  ? 349  VAL   A CG1    1 
ATOM   2759 C CG2    . VAL   A  1 357 ? 27.898 -15.569  -16.379 1.00 51.51  ? 349  VAL   A CG2    1 
ATOM   2760 N N      . PRO   A  1 358 ? 27.901 -12.838  -19.936 1.00 49.32  ? 350  PRO   A N      1 
ATOM   2761 C CA     . PRO   A  1 358 ? 29.008 -12.472  -20.850 1.00 49.73  ? 350  PRO   A CA     1 
ATOM   2762 C C      . PRO   A  1 358 ? 30.301 -12.072  -20.140 1.00 55.17  ? 350  PRO   A C      1 
ATOM   2763 O O      . PRO   A  1 358 ? 30.274 -11.797  -18.939 1.00 54.65  ? 350  PRO   A O      1 
ATOM   2764 C CB     . PRO   A  1 358 ? 28.426 -11.319  -21.664 1.00 51.42  ? 350  PRO   A CB     1 
ATOM   2765 C CG     . PRO   A  1 358 ? 27.415 -10.695  -20.772 1.00 55.88  ? 350  PRO   A CG     1 
ATOM   2766 C CD     . PRO   A  1 358 ? 26.853 -11.795  -19.909 1.00 51.35  ? 350  PRO   A CD     1 
ATOM   2767 N N      . GLU   A  1 359 ? 31.428 -12.034  -20.883 1.00 53.55  ? 351  GLU   A N      1 
ATOM   2768 C CA     . GLU   A  1 359 ? 32.765 -11.677  -20.375 1.00 54.60  ? 351  GLU   A CA     1 
ATOM   2769 C C      . GLU   A  1 359 ? 32.805 -10.354  -19.579 1.00 59.96  ? 351  GLU   A C      1 
ATOM   2770 O O      . GLU   A  1 359 ? 33.493 -10.283  -18.562 1.00 59.84  ? 351  GLU   A O      1 
ATOM   2771 C CB     . GLU   A  1 359 ? 33.797 -11.654  -21.519 1.00 56.17  ? 351  GLU   A CB     1 
ATOM   2772 C CG     . GLU   A  1 359 ? 35.246 -11.730  -21.057 1.00 68.34  ? 351  GLU   A CG     1 
ATOM   2773 C CD     . GLU   A  1 359 ? 35.834 -13.125  -20.971 1.00 96.30  ? 351  GLU   A CD     1 
ATOM   2774 O OE1    . GLU   A  1 359 ? 35.350 -13.930  -20.142 1.00 94.73  ? 351  GLU   A OE1    1 
ATOM   2775 O OE2    . GLU   A  1 359 ? 36.803 -13.404  -21.714 1.00 94.10  ? 351  GLU   A OE2    1 
ATOM   2776 N N      . GLU   A  1 360 ? 32.060 -9.326   -20.033 1.00 57.27  ? 352  GLU   A N      1 
ATOM   2777 C CA     . GLU   A  1 360 ? 31.985 -8.010   -19.383 1.00 57.14  ? 352  GLU   A CA     1 
ATOM   2778 C C      . GLU   A  1 360 ? 31.328 -8.047   -17.993 1.00 61.00  ? 352  GLU   A C      1 
ATOM   2779 O O      . GLU   A  1 360 ? 31.561 -7.144   -17.184 1.00 60.37  ? 352  GLU   A O      1 
ATOM   2780 C CB     . GLU   A  1 360 ? 31.304 -6.963   -20.294 1.00 58.49  ? 352  GLU   A CB     1 
ATOM   2781 C CG     . GLU   A  1 360 ? 29.921 -7.347   -20.812 1.00 69.49  ? 352  GLU   A CG     1 
ATOM   2782 C CD     . GLU   A  1 360 ? 29.862 -8.066   -22.150 1.00 91.24  ? 352  GLU   A CD     1 
ATOM   2783 O OE1    . GLU   A  1 360 ? 30.854 -8.735   -22.528 1.00 81.27  ? 352  GLU   A OE1    1 
ATOM   2784 O OE2    . GLU   A  1 360 ? 28.797 -7.994   -22.805 1.00 86.46  ? 352  GLU   A OE2    1 
ATOM   2785 N N      . GLU   A  1 361 ? 30.523 -9.095   -17.720 1.00 57.45  ? 353  GLU   A N      1 
ATOM   2786 C CA     . GLU   A  1 361 ? 29.804 -9.274   -16.454 1.00 57.05  ? 353  GLU   A CA     1 
ATOM   2787 C C      . GLU   A  1 361 ? 30.381 -10.386  -15.545 1.00 60.57  ? 353  GLU   A C      1 
ATOM   2788 O O      . GLU   A  1 361 ? 29.798 -10.665  -14.496 1.00 60.46  ? 353  GLU   A O      1 
ATOM   2789 C CB     . GLU   A  1 361 ? 28.310 -9.527   -16.729 1.00 58.32  ? 353  GLU   A CB     1 
ATOM   2790 C CG     . GLU   A  1 361 ? 27.570 -8.346   -17.324 1.00 68.51  ? 353  GLU   A CG     1 
ATOM   2791 C CD     . GLU   A  1 361 ? 26.072 -8.558   -17.400 1.00 93.00  ? 353  GLU   A CD     1 
ATOM   2792 O OE1    . GLU   A  1 361 ? 25.386 -8.316   -16.381 1.00 91.19  ? 353  GLU   A OE1    1 
ATOM   2793 O OE2    . GLU   A  1 361 ? 25.585 -8.979   -18.473 1.00 87.84  ? 353  GLU   A OE2    1 
ATOM   2794 N N      . LYS   A  1 362 ? 31.534 -10.986  -15.928 1.00 56.91  ? 354  LYS   A N      1 
ATOM   2795 C CA     . LYS   A  1 362 ? 32.194 -12.105  -15.236 1.00 56.90  ? 354  LYS   A CA     1 
ATOM   2796 C C      . LYS   A  1 362 ? 32.551 -11.860  -13.751 1.00 62.41  ? 354  LYS   A C      1 
ATOM   2797 O O      . LYS   A  1 362 ? 32.734 -12.835  -13.015 1.00 62.39  ? 354  LYS   A O      1 
ATOM   2798 C CB     . LYS   A  1 362 ? 33.441 -12.585  -16.015 1.00 58.79  ? 354  LYS   A CB     1 
ATOM   2799 C CG     . LYS   A  1 362 ? 34.687 -11.707  -15.874 1.00 68.17  ? 354  LYS   A CG     1 
ATOM   2800 C CD     . LYS   A  1 362 ? 35.811 -12.133  -16.815 1.00 74.87  ? 354  LYS   A CD     1 
ATOM   2801 C CE     . LYS   A  1 362 ? 36.838 -13.030  -16.162 1.00 83.68  ? 354  LYS   A CE     1 
ATOM   2802 N NZ     . LYS   A  1 362 ? 37.683 -12.300  -15.181 1.00 92.78  ? 354  LYS   A NZ     1 
ATOM   2803 N N      . ASP   A  1 363 ? 32.659 -10.590  -13.317 1.00 59.77  ? 355  ASP   A N      1 
ATOM   2804 C CA     . ASP   A  1 363 ? 33.024 -10.267  -11.936 1.00 59.89  ? 355  ASP   A CA     1 
ATOM   2805 C C      . ASP   A  1 363 ? 31.915 -9.550   -11.147 1.00 62.52  ? 355  ASP   A C      1 
ATOM   2806 O O      . ASP   A  1 363 ? 32.097 -9.280   -9.957  1.00 62.61  ? 355  ASP   A O      1 
ATOM   2807 C CB     . ASP   A  1 363 ? 34.346 -9.472   -11.899 1.00 62.33  ? 355  ASP   A CB     1 
ATOM   2808 C CG     . ASP   A  1 363 ? 35.567 -10.280  -12.316 1.00 76.66  ? 355  ASP   A CG     1 
ATOM   2809 O OD1    . ASP   A  1 363 ? 35.947 -11.215  -11.572 1.00 77.70  ? 355  ASP   A OD1    1 
ATOM   2810 O OD2    . ASP   A  1 363 ? 36.166 -9.952   -13.364 1.00 83.80  ? 355  ASP   A OD2    1 
ATOM   2811 N N      . THR   A  1 364 ? 30.766 -9.270   -11.789 1.00 57.42  ? 356  THR   A N      1 
ATOM   2812 C CA     . THR   A  1 364 ? 29.646 -8.576   -11.145 1.00 56.56  ? 356  THR   A CA     1 
ATOM   2813 C C      . THR   A  1 364 ? 28.372 -9.451   -11.047 1.00 58.68  ? 356  THR   A C      1 
ATOM   2814 O O      . THR   A  1 364 ? 27.588 -9.272   -10.110 1.00 58.42  ? 356  THR   A O      1 
ATOM   2815 C CB     . THR   A  1 364 ? 29.389 -7.204   -11.813 1.00 65.63  ? 356  THR   A CB     1 
ATOM   2816 O OG1    . THR   A  1 364 ? 28.358 -6.514   -11.105 1.00 67.07  ? 356  THR   A OG1    1 
ATOM   2817 C CG2    . THR   A  1 364 ? 29.029 -7.305   -13.296 1.00 64.06  ? 356  THR   A CG2    1 
ATOM   2818 N N      . ASN   A  1 365 ? 28.167 -10.381  -12.006 1.00 53.15  ? 357  ASN   A N      1 
ATOM   2819 C CA     . ASN   A  1 365 ? 26.996 -11.259  -12.032 1.00 51.76  ? 357  ASN   A CA     1 
ATOM   2820 C C      . ASN   A  1 365 ? 27.287 -12.613  -11.374 1.00 52.59  ? 357  ASN   A C      1 
ATOM   2821 O O      . ASN   A  1 365 ? 28.133 -13.376  -11.853 1.00 52.13  ? 357  ASN   A O      1 
ATOM   2822 C CB     . ASN   A  1 365 ? 26.468 -11.440  -13.461 1.00 51.92  ? 357  ASN   A CB     1 
ATOM   2823 C CG     . ASN   A  1 365 ? 24.986 -11.735  -13.569 1.00 71.57  ? 357  ASN   A CG     1 
ATOM   2824 O OD1    . ASN   A  1 365 ? 24.357 -12.337  -12.688 1.00 67.17  ? 357  ASN   A OD1    1 
ATOM   2825 N ND2    . ASN   A  1 365 ? 24.402 -11.356  -14.692 1.00 61.60  ? 357  ASN   A ND2    1 
ATOM   2826 N N      . VAL   A  1 366 ? 26.599 -12.880  -10.249 1.00 46.32  ? 358  VAL   A N      1 
ATOM   2827 C CA     . VAL   A  1 366 ? 26.708 -14.126  -9.494  1.00 44.26  ? 358  VAL   A CA     1 
ATOM   2828 C C      . VAL   A  1 366 ? 25.474 -14.957  -9.825  1.00 43.63  ? 358  VAL   A C      1 
ATOM   2829 O O      . VAL   A  1 366 ? 24.344 -14.534  -9.565  1.00 42.58  ? 358  VAL   A O      1 
ATOM   2830 C CB     . VAL   A  1 366 ? 26.896 -13.917  -7.965  1.00 47.95  ? 358  VAL   A CB     1 
ATOM   2831 C CG1    . VAL   A  1 366 ? 27.061 -15.254  -7.238  1.00 47.54  ? 358  VAL   A CG1    1 
ATOM   2832 C CG2    . VAL   A  1 366 ? 28.086 -13.009  -7.675  1.00 47.67  ? 358  VAL   A CG2    1 
ATOM   2833 N N      . GLN   A  1 367 ? 25.702 -16.107  -10.467 1.00 37.70  ? 359  GLN   A N      1 
ATOM   2834 C CA     . GLN   A  1 367 ? 24.642 -17.035  -10.863 1.00 36.01  ? 359  GLN   A CA     1 
ATOM   2835 C C      . GLN   A  1 367 ? 24.273 -17.911  -9.672  1.00 36.25  ? 359  GLN   A C      1 
ATOM   2836 O O      . GLN   A  1 367 ? 25.164 -18.444  -9.009  1.00 34.68  ? 359  GLN   A O      1 
ATOM   2837 C CB     . GLN   A  1 367 ? 25.097 -17.908  -12.059 1.00 36.98  ? 359  GLN   A CB     1 
ATOM   2838 C CG     . GLN   A  1 367 ? 25.168 -17.172  -13.403 1.00 41.95  ? 359  GLN   A CG     1 
ATOM   2839 C CD     . GLN   A  1 367 ? 23.808 -16.796  -13.932 1.00 49.02  ? 359  GLN   A CD     1 
ATOM   2840 O OE1    . GLN   A  1 367 ? 23.122 -17.599  -14.562 1.00 35.87  ? 359  GLN   A OE1    1 
ATOM   2841 N NE2    . GLN   A  1 367 ? 23.388 -15.558  -13.693 1.00 45.45  ? 359  GLN   A NE2    1 
ATOM   2842 N N      . VAL   A  1 368 ? 22.968 -18.043  -9.388  1.00 31.96  ? 360  VAL   A N      1 
ATOM   2843 C CA     . VAL   A  1 368 ? 22.487 -18.872  -8.278  1.00 31.63  ? 360  VAL   A CA     1 
ATOM   2844 C C      . VAL   A  1 368 ? 22.212 -20.290  -8.803  1.00 35.00  ? 360  VAL   A C      1 
ATOM   2845 O O      . VAL   A  1 368 ? 21.306 -20.486  -9.616  1.00 34.63  ? 360  VAL   A O      1 
ATOM   2846 C CB     . VAL   A  1 368 ? 21.285 -18.239  -7.513  1.00 35.55  ? 360  VAL   A CB     1 
ATOM   2847 C CG1    . VAL   A  1 368 ? 20.820 -19.130  -6.361  1.00 35.14  ? 360  VAL   A CG1    1 
ATOM   2848 C CG2    . VAL   A  1 368 ? 21.634 -16.838  -6.997  1.00 35.32  ? 360  VAL   A CG2    1 
ATOM   2849 N N      . LEU   A  1 369 ? 23.052 -21.252  -8.377  1.00 30.91  ? 361  LEU   A N      1 
ATOM   2850 C CA     . LEU   A  1 369 ? 22.978 -22.665  -8.743  1.00 30.52  ? 361  LEU   A CA     1 
ATOM   2851 C C      . LEU   A  1 369 ? 22.410 -23.512  -7.601  1.00 32.58  ? 361  LEU   A C      1 
ATOM   2852 O O      . LEU   A  1 369 ? 22.856 -23.400  -6.458  1.00 31.63  ? 361  LEU   A O      1 
ATOM   2853 C CB     . LEU   A  1 369 ? 24.365 -23.199  -9.125  1.00 30.69  ? 361  LEU   A CB     1 
ATOM   2854 C CG     . LEU   A  1 369 ? 24.696 -23.224  -10.602 1.00 36.14  ? 361  LEU   A CG     1 
ATOM   2855 C CD1    . LEU   A  1 369 ? 25.016 -21.814  -11.119 1.00 37.30  ? 361  LEU   A CD1    1 
ATOM   2856 C CD2    . LEU   A  1 369 ? 25.873 -24.123  -10.860 1.00 37.17  ? 361  LEU   A CD2    1 
ATOM   2857 N N      . MET   A  1 370 ? 21.438 -24.367  -7.923  1.00 27.86  ? 362  MET   A N      1 
ATOM   2858 C CA     . MET   A  1 370 ? 20.830 -25.261  -6.941  1.00 26.99  ? 362  MET   A CA     1 
ATOM   2859 C C      . MET   A  1 370 ? 20.965 -26.719  -7.355  1.00 28.40  ? 362  MET   A C      1 
ATOM   2860 O O      . MET   A  1 370 ? 20.419 -27.131  -8.374  1.00 27.01  ? 362  MET   A O      1 
ATOM   2861 C CB     . MET   A  1 370 ? 19.366 -24.889  -6.677  1.00 29.34  ? 362  MET   A CB     1 
ATOM   2862 C CG     . MET   A  1 370 ? 19.207 -23.588  -5.929  1.00 33.30  ? 362  MET   A CG     1 
ATOM   2863 S SD     . MET   A  1 370 ? 17.469 -23.183  -5.688  1.00 38.27  ? 362  MET   A SD     1 
ATOM   2864 C CE     . MET   A  1 370 ? 17.619 -21.571  -5.013  1.00 35.60  ? 362  MET   A CE     1 
ATOM   2865 N N      . VAL   A  1 371 ? 21.719 -27.489  -6.578  1.00 25.01  ? 363  VAL   A N      1 
ATOM   2866 C CA     . VAL   A  1 371 ? 21.878 -28.919  -6.804  1.00 24.08  ? 363  VAL   A CA     1 
ATOM   2867 C C      . VAL   A  1 371 ? 20.730 -29.579  -6.012  1.00 28.45  ? 363  VAL   A C      1 
ATOM   2868 O O      . VAL   A  1 371 ? 20.746 -29.577  -4.780  1.00 27.89  ? 363  VAL   A O      1 
ATOM   2869 C CB     . VAL   A  1 371 ? 23.283 -29.441  -6.410  1.00 26.82  ? 363  VAL   A CB     1 
ATOM   2870 C CG1    . VAL   A  1 371 ? 23.416 -30.931  -6.697  1.00 26.32  ? 363  VAL   A CG1    1 
ATOM   2871 C CG2    . VAL   A  1 371 ? 24.378 -28.661  -7.128  1.00 26.37  ? 363  VAL   A CG2    1 
ATOM   2872 N N      . LEU   A  1 372 ? 19.688 -30.024  -6.735  1.00 24.71  ? 364  LEU   A N      1 
ATOM   2873 C CA     . LEU   A  1 372 ? 18.480 -30.634  -6.176  1.00 23.98  ? 364  LEU   A CA     1 
ATOM   2874 C C      . LEU   A  1 372 ? 18.628 -32.152  -6.132  1.00 28.16  ? 364  LEU   A C      1 
ATOM   2875 O O      . LEU   A  1 372 ? 18.425 -32.840  -7.135  1.00 28.10  ? 364  LEU   A O      1 
ATOM   2876 C CB     . LEU   A  1 372 ? 17.236 -30.191  -6.968  1.00 23.53  ? 364  LEU   A CB     1 
ATOM   2877 C CG     . LEU   A  1 372 ? 16.979 -28.672  -7.068  1.00 27.81  ? 364  LEU   A CG     1 
ATOM   2878 C CD1    . LEU   A  1 372 ? 15.790 -28.391  -7.935  1.00 27.64  ? 364  LEU   A CD1    1 
ATOM   2879 C CD2    . LEU   A  1 372 ? 16.769 -28.037  -5.692  1.00 29.10  ? 364  LEU   A CD2    1 
ATOM   2880 N N      . GLY   A  1 373 ? 19.018 -32.642  -4.961  1.00 25.21  ? 365  GLY   A N      1 
ATOM   2881 C CA     . GLY   A  1 373 ? 19.337 -34.039  -4.694  1.00 23.92  ? 365  GLY   A CA     1 
ATOM   2882 C C      . GLY   A  1 373 ? 20.837 -34.198  -4.798  1.00 25.76  ? 365  GLY   A C      1 
ATOM   2883 O O      . GLY   A  1 373 ? 21.334 -34.915  -5.671  1.00 25.10  ? 365  GLY   A O      1 
ATOM   2884 N N      . ALA   A  1 374 ? 21.569 -33.496  -3.908  1.00 22.20  ? 366  ALA   A N      1 
ATOM   2885 C CA     . ALA   A  1 374 ? 23.033 -33.398  -3.885  1.00 21.78  ? 366  ALA   A CA     1 
ATOM   2886 C C      . ALA   A  1 374 ? 23.793 -34.662  -3.496  1.00 25.91  ? 366  ALA   A C      1 
ATOM   2887 O O      . ALA   A  1 374 ? 25.008 -34.719  -3.701  1.00 24.84  ? 366  ALA   A O      1 
ATOM   2888 C CB     . ALA   A  1 374 ? 23.455 -32.248  -2.977  1.00 22.42  ? 366  ALA   A CB     1 
ATOM   2889 N N      . GLY   A  1 375 ? 23.112 -35.634  -2.888  1.00 22.99  ? 367  GLY   A N      1 
ATOM   2890 C CA     . GLY   A  1 375 ? 23.746 -36.862  -2.416  1.00 21.93  ? 367  GLY   A CA     1 
ATOM   2891 C C      . GLY   A  1 375 ? 24.838 -36.533  -1.420  1.00 24.86  ? 367  GLY   A C      1 
ATOM   2892 O O      . GLY   A  1 375 ? 24.626 -35.714  -0.521  1.00 21.82  ? 367  GLY   A O      1 
ATOM   2893 N N      . ARG   A  1 376 ? 26.026 -37.111  -1.616  1.00 22.91  ? 368  ARG   A N      1 
ATOM   2894 C CA     . ARG   A  1 376 ? 27.187 -36.836  -0.773  1.00 23.32  ? 368  ARG   A CA     1 
ATOM   2895 C C      . ARG   A  1 376 ? 28.046 -35.655  -1.324  1.00 29.27  ? 368  ARG   A C      1 
ATOM   2896 O O      . ARG   A  1 376 ? 29.124 -35.379  -0.782  1.00 29.96  ? 368  ARG   A O      1 
ATOM   2897 C CB     . ARG   A  1 376 ? 28.034 -38.106  -0.579  1.00 23.65  ? 368  ARG   A CB     1 
ATOM   2898 C CG     . ARG   A  1 376 ? 27.287 -39.260  0.104   1.00 23.96  ? 368  ARG   A CG     1 
ATOM   2899 C CD     . ARG   A  1 376 ? 28.220 -40.299  0.672   1.00 25.45  ? 368  ARG   A CD     1 
ATOM   2900 N NE     . ARG   A  1 376 ? 29.312 -40.648  -0.237  1.00 26.31  ? 368  ARG   A NE     1 
ATOM   2901 C CZ     . ARG   A  1 376 ? 30.333 -41.428  0.093   1.00 34.50  ? 368  ARG   A CZ     1 
ATOM   2902 N NH1    . ARG   A  1 376 ? 30.394 -41.976  1.299   1.00 28.34  ? 368  ARG   A NH1    1 
ATOM   2903 N NH2    . ARG   A  1 376 ? 31.293 -41.677  -0.782  1.00 22.80  ? 368  ARG   A NH2    1 
ATOM   2904 N N      . GLY   A  1 377 ? 27.559 -34.997  -2.384  1.00 26.18  ? 369  GLY   A N      1 
ATOM   2905 C CA     . GLY   A  1 377 ? 28.169 -33.816  -2.996  1.00 26.73  ? 369  GLY   A CA     1 
ATOM   2906 C C      . GLY   A  1 377 ? 28.943 -33.900  -4.310  1.00 31.84  ? 369  GLY   A C      1 
ATOM   2907 O O      . GLY   A  1 377 ? 29.691 -32.960  -4.578  1.00 32.34  ? 369  GLY   A O      1 
ATOM   2908 N N      . PRO   A  1 378 ? 28.832 -34.923  -5.199  1.00 29.05  ? 370  PRO   A N      1 
ATOM   2909 C CA     . PRO   A  1 378 ? 29.673 -34.899  -6.418  1.00 28.20  ? 370  PRO   A CA     1 
ATOM   2910 C C      . PRO   A  1 378 ? 29.247 -33.865  -7.464  1.00 30.11  ? 370  PRO   A C      1 
ATOM   2911 O O      . PRO   A  1 378 ? 30.124 -33.287  -8.112  1.00 29.08  ? 370  PRO   A O      1 
ATOM   2912 C CB     . PRO   A  1 378 ? 29.630 -36.336  -6.929  1.00 30.04  ? 370  PRO   A CB     1 
ATOM   2913 C CG     . PRO   A  1 378 ? 28.367 -36.892  -6.398  1.00 35.01  ? 370  PRO   A CG     1 
ATOM   2914 C CD     . PRO   A  1 378 ? 28.019 -36.159  -5.132  1.00 30.77  ? 370  PRO   A CD     1 
ATOM   2915 N N      . LEU   A  1 379 ? 27.931 -33.585  -7.600  1.00 25.73  ? 371  LEU   A N      1 
ATOM   2916 C CA     . LEU   A  1 379 ? 27.457 -32.545  -8.515  1.00 25.65  ? 371  LEU   A CA     1 
ATOM   2917 C C      . LEU   A  1 379 ? 27.798 -31.149  -7.968  1.00 31.26  ? 371  LEU   A C      1 
ATOM   2918 O O      . LEU   A  1 379 ? 27.795 -30.186  -8.739  1.00 30.50  ? 371  LEU   A O      1 
ATOM   2919 C CB     . LEU   A  1 379 ? 25.952 -32.629  -8.823  1.00 25.32  ? 371  LEU   A CB     1 
ATOM   2920 C CG     . LEU   A  1 379 ? 25.429 -33.839  -9.616  1.00 30.10  ? 371  LEU   A CG     1 
ATOM   2921 C CD1    . LEU   A  1 379 ? 23.909 -33.783  -9.722  1.00 29.51  ? 371  LEU   A CD1    1 
ATOM   2922 C CD2    . LEU   A  1 379 ? 26.034 -33.903  -11.015 1.00 31.36  ? 371  LEU   A CD2    1 
ATOM   2923 N N      . VAL   A  1 380 ? 28.055 -31.035  -6.635  1.00 29.03  ? 372  VAL   A N      1 
ATOM   2924 C CA     . VAL   A  1 380 ? 28.440 -29.767  -5.998  1.00 28.94  ? 372  VAL   A CA     1 
ATOM   2925 C C      . VAL   A  1 380 ? 29.866 -29.453  -6.480  1.00 32.59  ? 372  VAL   A C      1 
ATOM   2926 O O      . VAL   A  1 380 ? 30.110 -28.351  -6.977  1.00 32.46  ? 372  VAL   A O      1 
ATOM   2927 C CB     . VAL   A  1 380 ? 28.289 -29.762  -4.448  1.00 32.94  ? 372  VAL   A CB     1 
ATOM   2928 C CG1    . VAL   A  1 380 ? 28.796 -28.450  -3.841  1.00 32.95  ? 372  VAL   A CG1    1 
ATOM   2929 C CG2    . VAL   A  1 380 ? 26.839 -30.001  -4.036  1.00 32.26  ? 372  VAL   A CG2    1 
ATOM   2930 N N      . ASN   A  1 381 ? 30.764 -30.451  -6.412  1.00 28.42  ? 373  ASN   A N      1 
ATOM   2931 C CA     . ASN   A  1 381 ? 32.136 -30.327  -6.902  1.00 29.06  ? 373  ASN   A CA     1 
ATOM   2932 C C      . ASN   A  1 381 ? 32.187 -30.106  -8.411  1.00 35.08  ? 373  ASN   A C      1 
ATOM   2933 O O      . ASN   A  1 381 ? 32.982 -29.285  -8.863  1.00 35.19  ? 373  ASN   A O      1 
ATOM   2934 C CB     . ASN   A  1 381 ? 32.999 -31.507  -6.465  1.00 27.89  ? 373  ASN   A CB     1 
ATOM   2935 C CG     . ASN   A  1 381 ? 33.329 -31.493  -4.988  1.00 50.60  ? 373  ASN   A CG     1 
ATOM   2936 O OD1    . ASN   A  1 381 ? 33.251 -30.461  -4.310  1.00 42.81  ? 373  ASN   A OD1    1 
ATOM   2937 N ND2    . ASN   A  1 381 ? 33.717 -32.639  -4.453  1.00 45.54  ? 373  ASN   A ND2    1 
ATOM   2938 N N      . ALA   A  1 382 ? 31.296 -30.778  -9.181  1.00 32.42  ? 374  ALA   A N      1 
ATOM   2939 C CA     . ALA   A  1 382 ? 31.186 -30.610  -10.628 1.00 32.29  ? 374  ALA   A CA     1 
ATOM   2940 C C      . ALA   A  1 382 ? 30.760 -29.172  -10.967 1.00 35.25  ? 374  ALA   A C      1 
ATOM   2941 O O      . ALA   A  1 382 ? 31.276 -28.607  -11.927 1.00 34.12  ? 374  ALA   A O      1 
ATOM   2942 C CB     . ALA   A  1 382 ? 30.191 -31.606  -11.211 1.00 33.03  ? 374  ALA   A CB     1 
ATOM   2943 N N      . SER   A  1 383 ? 29.842 -28.579  -10.164 1.00 31.79  ? 375  SER   A N      1 
ATOM   2944 C CA     . SER   A  1 383 ? 29.370 -27.201  -10.359 1.00 31.86  ? 375  SER   A CA     1 
ATOM   2945 C C      . SER   A  1 383 ? 30.493 -26.193  -10.096 1.00 37.68  ? 375  SER   A C      1 
ATOM   2946 O O      . SER   A  1 383 ? 30.661 -25.260  -10.879 1.00 37.77  ? 375  SER   A O      1 
ATOM   2947 C CB     . SER   A  1 383 ? 28.165 -26.901  -9.472  1.00 32.57  ? 375  SER   A CB     1 
ATOM   2948 O OG     . SER   A  1 383 ? 27.061 -27.729  -9.797  1.00 34.46  ? 375  SER   A OG     1 
ATOM   2949 N N      . LEU   A  1 384 ? 31.283 -26.412  -9.023  1.00 35.35  ? 376  LEU   A N      1 
ATOM   2950 C CA     . LEU   A  1 384 ? 32.410 -25.556  -8.640  1.00 35.51  ? 376  LEU   A CA     1 
ATOM   2951 C C      . LEU   A  1 384 ? 33.516 -25.601  -9.690  1.00 39.72  ? 376  LEU   A C      1 
ATOM   2952 O O      . LEU   A  1 384 ? 34.012 -24.539  -10.079 1.00 39.09  ? 376  LEU   A O      1 
ATOM   2953 C CB     . LEU   A  1 384 ? 32.963 -25.927  -7.253  1.00 35.58  ? 376  LEU   A CB     1 
ATOM   2954 C CG     . LEU   A  1 384 ? 32.035 -25.691  -6.060  1.00 40.36  ? 376  LEU   A CG     1 
ATOM   2955 C CD1    . LEU   A  1 384 ? 32.479 -26.488  -4.873  1.00 40.44  ? 376  LEU   A CD1    1 
ATOM   2956 C CD2    . LEU   A  1 384 ? 31.971 -24.230  -5.683  1.00 44.11  ? 376  LEU   A CD2    1 
ATOM   2957 N N      . ARG   A  1 385 ? 33.875 -26.818  -10.174 1.00 35.56  ? 377  ARG   A N      1 
ATOM   2958 C CA     . ARG   A  1 385 ? 34.879 -27.008  -11.230 1.00 35.49  ? 377  ARG   A CA     1 
ATOM   2959 C C      . ARG   A  1 385 ? 34.442 -26.328  -12.539 1.00 40.34  ? 377  ARG   A C      1 
ATOM   2960 O O      . ARG   A  1 385 ? 35.291 -25.772  -13.239 1.00 40.72  ? 377  ARG   A O      1 
ATOM   2961 C CB     . ARG   A  1 385 ? 35.143 -28.495  -11.505 1.00 34.44  ? 377  ARG   A CB     1 
ATOM   2962 C CG     . ARG   A  1 385 ? 35.908 -29.226  -10.408 1.00 41.45  ? 377  ARG   A CG     1 
ATOM   2963 C CD     . ARG   A  1 385 ? 36.408 -30.590  -10.867 1.00 45.44  ? 377  ARG   A CD     1 
ATOM   2964 N NE     . ARG   A  1 385 ? 35.334 -31.456  -11.364 1.00 54.77  ? 377  ARG   A NE     1 
ATOM   2965 C CZ     . ARG   A  1 385 ? 34.729 -32.404  -10.651 1.00 65.59  ? 377  ARG   A CZ     1 
ATOM   2966 N NH1    . ARG   A  1 385 ? 35.090 -32.633  -9.393  1.00 46.37  ? 377  ARG   A NH1    1 
ATOM   2967 N NH2    . ARG   A  1 385 ? 33.765 -33.136  -11.194 1.00 51.02  ? 377  ARG   A NH2    1 
ATOM   2968 N N      . ALA   A  1 386 ? 33.127 -26.373  -12.860 1.00 36.10  ? 378  ALA   A N      1 
ATOM   2969 C CA     . ALA   A  1 386 ? 32.564 -25.756  -14.066 1.00 36.45  ? 378  ALA   A CA     1 
ATOM   2970 C C      . ALA   A  1 386 ? 32.633 -24.230  -14.011 1.00 41.46  ? 378  ALA   A C      1 
ATOM   2971 O O      . ALA   A  1 386 ? 32.863 -23.604  -15.046 1.00 40.37  ? 378  ALA   A O      1 
ATOM   2972 C CB     . ALA   A  1 386 ? 31.129 -26.204  -14.277 1.00 37.08  ? 378  ALA   A CB     1 
ATOM   2973 N N      . ALA   A  1 387 ? 32.415 -23.639  -12.815 1.00 39.39  ? 379  ALA   A N      1 
ATOM   2974 C CA     . ALA   A  1 387 ? 32.469 -22.189  -12.587 1.00 39.82  ? 379  ALA   A CA     1 
ATOM   2975 C C      . ALA   A  1 387 ? 33.907 -21.664  -12.688 1.00 44.77  ? 379  ALA   A C      1 
ATOM   2976 O O      . ALA   A  1 387 ? 34.110 -20.545  -13.165 1.00 44.58  ? 379  ALA   A O      1 
ATOM   2977 C CB     . ALA   A  1 387 ? 31.865 -21.839  -11.241 1.00 40.51  ? 379  ALA   A CB     1 
ATOM   2978 N N      . LYS   A  1 388 ? 34.896 -22.487  -12.273 1.00 41.59  ? 380  LYS   A N      1 
ATOM   2979 C CA     . LYS   A  1 388 ? 36.319 -22.175  -12.383 1.00 41.80  ? 380  LYS   A CA     1 
ATOM   2980 C C      . LYS   A  1 388 ? 36.755 -22.250  -13.851 1.00 46.61  ? 380  LYS   A C      1 
ATOM   2981 O O      . LYS   A  1 388 ? 37.554 -21.422  -14.294 1.00 47.30  ? 380  LYS   A O      1 
ATOM   2982 C CB     . LYS   A  1 388 ? 37.167 -23.123  -11.518 1.00 44.20  ? 380  LYS   A CB     1 
ATOM   2983 C CG     . LYS   A  1 388 ? 37.423 -22.580  -10.119 1.00 61.73  ? 380  LYS   A CG     1 
ATOM   2984 C CD     . LYS   A  1 388 ? 38.675 -23.189  -9.499  1.00 74.80  ? 380  LYS   A CD     1 
ATOM   2985 C CE     . LYS   A  1 388 ? 39.141 -22.451  -8.263  1.00 87.17  ? 380  LYS   A CE     1 
ATOM   2986 N NZ     . LYS   A  1 388 ? 39.871 -21.198  -8.599  1.00 96.03  ? 380  LYS   A NZ     1 
ATOM   2987 N N      . GLN   A  1 389 ? 36.205 -23.229  -14.601 1.00 42.30  ? 381  GLN   A N      1 
ATOM   2988 C CA     . GLN   A  1 389 ? 36.464 -23.469  -16.024 1.00 41.50  ? 381  GLN   A CA     1 
ATOM   2989 C C      . GLN   A  1 389 ? 35.897 -22.328  -16.882 1.00 45.53  ? 381  GLN   A C      1 
ATOM   2990 O O      . GLN   A  1 389 ? 36.578 -21.858  -17.793 1.00 45.21  ? 381  GLN   A O      1 
ATOM   2991 C CB     . GLN   A  1 389 ? 35.848 -24.814  -16.450 1.00 42.45  ? 381  GLN   A CB     1 
ATOM   2992 C CG     . GLN   A  1 389 ? 36.502 -25.463  -17.665 1.00 54.27  ? 381  GLN   A CG     1 
ATOM   2993 C CD     . GLN   A  1 389 ? 35.735 -26.662  -18.190 1.00 70.78  ? 381  GLN   A CD     1 
ATOM   2994 O OE1    . GLN   A  1 389 ? 34.964 -27.324  -17.476 1.00 63.08  ? 381  GLN   A OE1    1 
ATOM   2995 N NE2    . GLN   A  1 389 ? 35.940 -26.977  -19.463 1.00 60.72  ? 381  GLN   A NE2    1 
ATOM   2996 N N      . ALA   A  1 390 ? 34.660 -21.886  -16.578 1.00 41.60  ? 382  ALA   A N      1 
ATOM   2997 C CA     . ALA   A  1 390 ? 33.953 -20.813  -17.277 1.00 41.66  ? 382  ALA   A CA     1 
ATOM   2998 C C      . ALA   A  1 390 ? 34.428 -19.416  -16.861 1.00 47.09  ? 382  ALA   A C      1 
ATOM   2999 O O      . ALA   A  1 390 ? 34.080 -18.435  -17.527 1.00 47.24  ? 382  ALA   A O      1 
ATOM   3000 C CB     . ALA   A  1 390 ? 32.455 -20.936  -17.019 1.00 42.18  ? 382  ALA   A CB     1 
ATOM   3001 N N      . ASP   A  1 391 ? 35.203 -19.330  -15.757 1.00 44.60  ? 383  ASP   A N      1 
ATOM   3002 C CA     . ASP   A  1 391 ? 35.678 -18.097  -15.115 1.00 45.24  ? 383  ASP   A CA     1 
ATOM   3003 C C      . ASP   A  1 391 ? 34.468 -17.206  -14.798 1.00 48.20  ? 383  ASP   A C      1 
ATOM   3004 O O      . ASP   A  1 391 ? 34.410 -16.038  -15.200 1.00 47.58  ? 383  ASP   A O      1 
ATOM   3005 C CB     . ASP   A  1 391 ? 36.770 -17.369  -15.940 1.00 48.21  ? 383  ASP   A CB     1 
ATOM   3006 C CG     . ASP   A  1 391 ? 37.655 -16.405  -15.148 1.00 64.45  ? 383  ASP   A CG     1 
ATOM   3007 O OD1    . ASP   A  1 391 ? 37.178 -15.851  -14.123 1.00 64.45  ? 383  ASP   A OD1    1 
ATOM   3008 O OD2    . ASP   A  1 391 ? 38.808 -16.168  -15.578 1.00 74.35  ? 383  ASP   A OD2    1 
ATOM   3009 N N      . ARG   A  1 392 ? 33.465 -17.811  -14.125 1.00 43.97  ? 384  ARG   A N      1 
ATOM   3010 C CA     . ARG   A  1 392 ? 32.213 -17.159  -13.739 1.00 42.90  ? 384  ARG   A CA     1 
ATOM   3011 C C      . ARG   A  1 392 ? 31.926 -17.348  -12.253 1.00 45.66  ? 384  ARG   A C      1 
ATOM   3012 O O      . ARG   A  1 392 ? 32.449 -18.275  -11.629 1.00 44.85  ? 384  ARG   A O      1 
ATOM   3013 C CB     . ARG   A  1 392 ? 31.034 -17.626  -14.617 1.00 42.16  ? 384  ARG   A CB     1 
ATOM   3014 C CG     . ARG   A  1 392 ? 31.181 -17.330  -16.119 1.00 53.41  ? 384  ARG   A CG     1 
ATOM   3015 C CD     . ARG   A  1 392 ? 31.327 -15.845  -16.443 1.00 60.41  ? 384  ARG   A CD     1 
ATOM   3016 N NE     . ARG   A  1 392 ? 31.088 -15.564  -17.858 1.00 61.19  ? 384  ARG   A NE     1 
ATOM   3017 C CZ     . ARG   A  1 392 ? 32.035 -15.522  -18.790 1.00 70.37  ? 384  ARG   A CZ     1 
ATOM   3018 N NH1    . ARG   A  1 392 ? 33.305 -15.736  -18.466 1.00 50.57  ? 384  ARG   A NH1    1 
ATOM   3019 N NH2    . ARG   A  1 392 ? 31.720 -15.269  -20.053 1.00 58.85  ? 384  ARG   A NH2    1 
ATOM   3020 N N      . ARG   A  1 393 ? 31.126 -16.437  -11.685 1.00 42.01  ? 385  ARG   A N      1 
ATOM   3021 C CA     . ARG   A  1 393 ? 30.792 -16.414  -10.263 1.00 41.22  ? 385  ARG   A CA     1 
ATOM   3022 C C      . ARG   A  1 393 ? 29.489 -17.147  -9.983  1.00 42.30  ? 385  ARG   A C      1 
ATOM   3023 O O      . ARG   A  1 393 ? 28.473 -16.864  -10.630 1.00 40.79  ? 385  ARG   A O      1 
ATOM   3024 C CB     . ARG   A  1 393 ? 30.709 -14.961  -9.758  1.00 42.05  ? 385  ARG   A CB     1 
ATOM   3025 C CG     . ARG   A  1 393 ? 32.065 -14.284  -9.556  1.00 53.56  ? 385  ARG   A CG     1 
ATOM   3026 C CD     . ARG   A  1 393 ? 31.913 -12.859  -9.048  1.00 60.52  ? 385  ARG   A CD     1 
ATOM   3027 N NE     . ARG   A  1 393 ? 31.668 -12.805  -7.605  1.00 70.57  ? 385  ARG   A NE     1 
ATOM   3028 C CZ     . ARG   A  1 393 ? 31.282 -11.716  -6.945  1.00 88.03  ? 385  ARG   A CZ     1 
ATOM   3029 N NH1    . ARG   A  1 393 ? 31.064 -10.578  -7.595  1.00 76.81  ? 385  ARG   A NH1    1 
ATOM   3030 N NH2    . ARG   A  1 393 ? 31.080 -11.764  -5.635  1.00 76.55  ? 385  ARG   A NH2    1 
ATOM   3031 N N      . ILE   A  1 394 ? 29.513 -18.079  -9.001  1.00 37.58  ? 386  ILE   A N      1 
ATOM   3032 C CA     . ILE   A  1 394 ? 28.326 -18.853  -8.612  1.00 36.74  ? 386  ILE   A CA     1 
ATOM   3033 C C      . ILE   A  1 394 ? 28.080 -18.868  -7.098  1.00 40.51  ? 386  ILE   A C      1 
ATOM   3034 O O      . ILE   A  1 394 ? 29.024 -18.865  -6.304  1.00 40.02  ? 386  ILE   A O      1 
ATOM   3035 C CB     . ILE   A  1 394 ? 28.297 -20.305  -9.193  1.00 39.34  ? 386  ILE   A CB     1 
ATOM   3036 C CG1    . ILE   A  1 394 ? 29.396 -21.207  -8.569  1.00 39.41  ? 386  ILE   A CG1    1 
ATOM   3037 C CG2    . ILE   A  1 394 ? 28.343 -20.311  -10.732 1.00 39.31  ? 386  ILE   A CG2    1 
ATOM   3038 C CD1    . ILE   A  1 394 ? 29.137 -22.714  -8.641  1.00 45.84  ? 386  ILE   A CD1    1 
ATOM   3039 N N      . LYS   A  1 395 ? 26.792 -18.910  -6.721  1.00 36.92  ? 387  LYS   A N      1 
ATOM   3040 C CA     . LYS   A  1 395 ? 26.310 -19.064  -5.354  1.00 36.77  ? 387  LYS   A CA     1 
ATOM   3041 C C      . LYS   A  1 395 ? 25.592 -20.433  -5.351  1.00 40.39  ? 387  LYS   A C      1 
ATOM   3042 O O      . LYS   A  1 395 ? 24.635 -20.622  -6.112  1.00 40.01  ? 387  LYS   A O      1 
ATOM   3043 C CB     . LYS   A  1 395 ? 25.353 -17.927  -4.967  1.00 38.68  ? 387  LYS   A CB     1 
ATOM   3044 C CG     . LYS   A  1 395 ? 25.057 -17.903  -3.469  1.00 48.39  ? 387  LYS   A CG     1 
ATOM   3045 C CD     . LYS   A  1 395 ? 24.050 -16.844  -3.086  1.00 57.08  ? 387  LYS   A CD     1 
ATOM   3046 C CE     . LYS   A  1 395 ? 23.839 -16.815  -1.592  1.00 64.86  ? 387  LYS   A CE     1 
ATOM   3047 N NZ     . LYS   A  1 395 ? 22.889 -15.744  -1.190  1.00 73.28  ? 387  LYS   A NZ     1 
ATOM   3048 N N      . LEU   A  1 396 ? 26.087 -21.395  -4.544  1.00 36.29  ? 388  LEU   A N      1 
ATOM   3049 C CA     . LEU   A  1 396 ? 25.560 -22.764  -4.520  1.00 35.11  ? 388  LEU   A CA     1 
ATOM   3050 C C      . LEU   A  1 396 ? 24.660 -23.149  -3.351  1.00 36.68  ? 388  LEU   A C      1 
ATOM   3051 O O      . LEU   A  1 396 ? 24.950 -22.839  -2.198  1.00 36.15  ? 388  LEU   A O      1 
ATOM   3052 C CB     . LEU   A  1 396 ? 26.721 -23.768  -4.584  1.00 35.06  ? 388  LEU   A CB     1 
ATOM   3053 C CG     . LEU   A  1 396 ? 27.034 -24.400  -5.926  1.00 39.78  ? 388  LEU   A CG     1 
ATOM   3054 C CD1    . LEU   A  1 396 ? 28.309 -25.178  -5.846  1.00 40.52  ? 388  LEU   A CD1    1 
ATOM   3055 C CD2    . LEU   A  1 396 ? 25.927 -25.337  -6.378  1.00 40.90  ? 388  LEU   A CD2    1 
ATOM   3056 N N      . TYR   A  1 397 ? 23.600 -23.903  -3.667  1.00 32.20  ? 389  TYR   A N      1 
ATOM   3057 C CA     . TYR   A  1 397 ? 22.667 -24.517  -2.723  1.00 30.85  ? 389  TYR   A CA     1 
ATOM   3058 C C      . TYR   A  1 397 ? 22.692 -26.028  -2.984  1.00 33.12  ? 389  TYR   A C      1 
ATOM   3059 O O      . TYR   A  1 397 ? 22.542 -26.446  -4.131  1.00 32.57  ? 389  TYR   A O      1 
ATOM   3060 C CB     . TYR   A  1 397 ? 21.245 -23.979  -2.897  1.00 31.99  ? 389  TYR   A CB     1 
ATOM   3061 C CG     . TYR   A  1 397 ? 21.044 -22.573  -2.383  1.00 35.11  ? 389  TYR   A CG     1 
ATOM   3062 C CD1    . TYR   A  1 397 ? 21.135 -21.478  -3.238  1.00 37.03  ? 389  TYR   A CD1    1 
ATOM   3063 C CD2    . TYR   A  1 397 ? 20.753 -22.334  -1.042  1.00 36.53  ? 389  TYR   A CD2    1 
ATOM   3064 C CE1    . TYR   A  1 397 ? 20.946 -20.179  -2.774  1.00 38.35  ? 389  TYR   A CE1    1 
ATOM   3065 C CE2    . TYR   A  1 397 ? 20.562 -21.036  -0.564  1.00 38.11  ? 389  TYR   A CE2    1 
ATOM   3066 C CZ     . TYR   A  1 397 ? 20.656 -19.961  -1.437  1.00 46.60  ? 389  TYR   A CZ     1 
ATOM   3067 O OH     . TYR   A  1 397 ? 20.461 -18.676  -0.990  1.00 47.42  ? 389  TYR   A OH     1 
ATOM   3068 N N      . ALA   A  1 398 ? 22.925 -26.836  -1.942  1.00 29.14  ? 390  ALA   A N      1 
ATOM   3069 C CA     . ALA   A  1 398 ? 22.980 -28.294  -2.057  1.00 28.58  ? 390  ALA   A CA     1 
ATOM   3070 C C      . ALA   A  1 398 ? 21.841 -28.883  -1.239  1.00 30.00  ? 390  ALA   A C      1 
ATOM   3071 O O      . ALA   A  1 398 ? 21.964 -29.041  -0.031  1.00 30.59  ? 390  ALA   A O      1 
ATOM   3072 C CB     . ALA   A  1 398 ? 24.330 -28.817  -1.575  1.00 29.42  ? 390  ALA   A CB     1 
ATOM   3073 N N      . VAL   A  1 399 ? 20.702 -29.119  -1.904  1.00 24.98  ? 391  VAL   A N      1 
ATOM   3074 C CA     . VAL   A  1 399 ? 19.464 -29.647  -1.329  1.00 23.67  ? 391  VAL   A CA     1 
ATOM   3075 C C      . VAL   A  1 399 ? 19.476 -31.173  -1.372  1.00 28.03  ? 391  VAL   A C      1 
ATOM   3076 O O      . VAL   A  1 399 ? 19.752 -31.754  -2.423  1.00 29.15  ? 391  VAL   A O      1 
ATOM   3077 C CB     . VAL   A  1 399 ? 18.219 -29.041  -2.029  1.00 26.51  ? 391  VAL   A CB     1 
ATOM   3078 C CG1    . VAL   A  1 399 ? 16.938 -29.350  -1.251  1.00 25.38  ? 391  VAL   A CG1    1 
ATOM   3079 C CG2    . VAL   A  1 399 ? 18.381 -27.528  -2.228  1.00 26.31  ? 391  VAL   A CG2    1 
ATOM   3080 N N      . GLU   A  1 400 ? 19.213 -31.820  -0.223  1.00 24.06  ? 392  GLU   A N      1 
ATOM   3081 C CA     . GLU   A  1 400 ? 19.216 -33.280  -0.094  1.00 22.88  ? 392  GLU   A CA     1 
ATOM   3082 C C      . GLU   A  1 400 ? 18.217 -33.724  0.958   1.00 25.60  ? 392  GLU   A C      1 
ATOM   3083 O O      . GLU   A  1 400 ? 18.245 -33.230  2.090   1.00 25.67  ? 392  GLU   A O      1 
ATOM   3084 C CB     . GLU   A  1 400 ? 20.641 -33.810  0.197   1.00 23.78  ? 392  GLU   A CB     1 
ATOM   3085 C CG     . GLU   A  1 400 ? 20.786 -35.321  0.338   1.00 26.49  ? 392  GLU   A CG     1 
ATOM   3086 C CD     . GLU   A  1 400 ? 20.143 -36.130  -0.771  1.00 36.28  ? 392  GLU   A CD     1 
ATOM   3087 O OE1    . GLU   A  1 400 ? 20.593 -36.009  -1.931  1.00 23.53  ? 392  GLU   A OE1    1 
ATOM   3088 O OE2    . GLU   A  1 400 ? 19.112 -36.784  -0.506  1.00 23.79  ? 392  GLU   A OE2    1 
ATOM   3089 N N      . LYS   A  1 401 ? 17.332 -34.661  0.576   1.00 20.85  ? 393  LYS   A N      1 
ATOM   3090 C CA     . LYS   A  1 401 ? 16.284 -35.205  1.448   1.00 21.19  ? 393  LYS   A CA     1 
ATOM   3091 C C      . LYS   A  1 401 ? 16.800 -36.329  2.373   1.00 24.15  ? 393  LYS   A C      1 
ATOM   3092 O O      . LYS   A  1 401 ? 16.216 -36.538  3.433   1.00 24.65  ? 393  LYS   A O      1 
ATOM   3093 C CB     . LYS   A  1 401 ? 15.057 -35.635  0.609   1.00 24.21  ? 393  LYS   A CB     1 
ATOM   3094 C CG     . LYS   A  1 401 ? 14.664 -37.117  0.659   1.00 34.84  ? 393  LYS   A CG     1 
ATOM   3095 C CD     . LYS   A  1 401 ? 15.275 -37.933  -0.427  1.00 41.03  ? 393  LYS   A CD     1 
ATOM   3096 C CE     . LYS   A  1 401 ? 14.405 -39.125  -0.735  1.00 41.99  ? 393  LYS   A CE     1 
ATOM   3097 N NZ     . LYS   A  1 401 ? 14.683 -40.291  0.144   1.00 42.51  ? 393  LYS   A NZ     1 
ATOM   3098 N N      . ASN   A  1 402 ? 17.873 -37.048  1.969   1.00 20.47  ? 394  ASN   A N      1 
ATOM   3099 C CA     . ASN   A  1 402 ? 18.475 -38.124  2.756   1.00 20.38  ? 394  ASN   A CA     1 
ATOM   3100 C C      . ASN   A  1 402 ? 19.306 -37.483  3.884   1.00 27.69  ? 394  ASN   A C      1 
ATOM   3101 O O      . ASN   A  1 402 ? 20.355 -36.889  3.610   1.00 27.49  ? 394  ASN   A O      1 
ATOM   3102 C CB     . ASN   A  1 402 ? 19.322 -39.055  1.873   1.00 18.02  ? 394  ASN   A CB     1 
ATOM   3103 C CG     . ASN   A  1 402 ? 19.948 -40.243  2.570   1.00 26.70  ? 394  ASN   A CG     1 
ATOM   3104 O OD1    . ASN   A  1 402 ? 19.813 -40.456  3.783   1.00 23.96  ? 394  ASN   A OD1    1 
ATOM   3105 N ND2    . ASN   A  1 402 ? 20.648 -41.058  1.809   1.00 22.35  ? 394  ASN   A ND2    1 
ATOM   3106 N N      . PRO   A  1 403 ? 18.829 -37.568  5.155   1.00 24.96  ? 395  PRO   A N      1 
ATOM   3107 C CA     . PRO   A  1 403 ? 19.549 -36.912  6.258   1.00 25.27  ? 395  PRO   A CA     1 
ATOM   3108 C C      . PRO   A  1 403 ? 20.919 -37.499  6.549   1.00 26.92  ? 395  PRO   A C      1 
ATOM   3109 O O      . PRO   A  1 403 ? 21.791 -36.798  7.048   1.00 25.38  ? 395  PRO   A O      1 
ATOM   3110 C CB     . PRO   A  1 403 ? 18.591 -37.059  7.438   1.00 27.49  ? 395  PRO   A CB     1 
ATOM   3111 C CG     . PRO   A  1 403 ? 17.306 -37.546  6.890   1.00 31.76  ? 395  PRO   A CG     1 
ATOM   3112 C CD     . PRO   A  1 403 ? 17.628 -38.272  5.651   1.00 26.82  ? 395  PRO   A CD     1 
ATOM   3113 N N      . ASN   A  1 404 ? 21.116 -38.773  6.198   1.00 23.06  ? 396  ASN   A N      1 
ATOM   3114 C CA     . ASN   A  1 404 ? 22.386 -39.468  6.376   1.00 22.85  ? 396  ASN   A CA     1 
ATOM   3115 C C      . ASN   A  1 404 ? 23.438 -38.931  5.379   1.00 27.92  ? 396  ASN   A C      1 
ATOM   3116 O O      . ASN   A  1 404 ? 24.614 -38.806  5.733   1.00 28.05  ? 396  ASN   A O      1 
ATOM   3117 C CB     . ASN   A  1 404 ? 22.172 -40.944  6.187   1.00 22.06  ? 396  ASN   A CB     1 
ATOM   3118 C CG     . ASN   A  1 404 ? 21.050 -41.513  7.030   1.00 35.55  ? 396  ASN   A CG     1 
ATOM   3119 O OD1    . ASN   A  1 404 ? 21.175 -41.628  8.239   1.00 27.52  ? 396  ASN   A OD1    1 
ATOM   3120 N ND2    . ASN   A  1 404 ? 19.924 -41.867  6.403   1.00 23.56  ? 396  ASN   A ND2    1 
ATOM   3121 N N      . ALA   A  1 405 ? 23.007 -38.608  4.143   1.00 24.26  ? 397  ALA   A N      1 
ATOM   3122 C CA     . ALA   A  1 405 ? 23.872 -38.030  3.109   1.00 23.92  ? 397  ALA   A CA     1 
ATOM   3123 C C      . ALA   A  1 405 ? 24.185 -36.575  3.508   1.00 26.78  ? 397  ALA   A C      1 
ATOM   3124 O O      . ALA   A  1 405 ? 25.292 -36.110  3.260   1.00 26.51  ? 397  ALA   A O      1 
ATOM   3125 C CB     . ALA   A  1 405 ? 23.186 -38.071  1.754   1.00 24.13  ? 397  ALA   A CB     1 
ATOM   3126 N N      . VAL   A  1 406 ? 23.218 -35.886  4.154   1.00 23.29  ? 398  VAL   A N      1 
ATOM   3127 C CA     . VAL   A  1 406 ? 23.356 -34.515  4.670   1.00 23.34  ? 398  VAL   A CA     1 
ATOM   3128 C C      . VAL   A  1 406 ? 24.547 -34.411  5.661   1.00 27.97  ? 398  VAL   A C      1 
ATOM   3129 O O      . VAL   A  1 406 ? 25.221 -33.383  5.666   1.00 28.34  ? 398  VAL   A O      1 
ATOM   3130 C CB     . VAL   A  1 406 ? 22.030 -33.941  5.241   1.00 26.81  ? 398  VAL   A CB     1 
ATOM   3131 C CG1    . VAL   A  1 406 ? 22.246 -32.569  5.896   1.00 26.52  ? 398  VAL   A CG1    1 
ATOM   3132 C CG2    . VAL   A  1 406 ? 20.972 -33.832  4.151   1.00 26.59  ? 398  VAL   A CG2    1 
ATOM   3133 N N      . VAL   A  1 407 ? 24.835 -35.486  6.444   1.00 24.43  ? 399  VAL   A N      1 
ATOM   3134 C CA     . VAL   A  1 407 ? 25.975 -35.544  7.374   1.00 24.47  ? 399  VAL   A CA     1 
ATOM   3135 C C      . VAL   A  1 407 ? 27.287 -35.349  6.586   1.00 29.11  ? 399  VAL   A C      1 
ATOM   3136 O O      . VAL   A  1 407 ? 28.135 -34.567  7.005   1.00 28.42  ? 399  VAL   A O      1 
ATOM   3137 C CB     . VAL   A  1 407 ? 26.002 -36.848  8.234   1.00 27.77  ? 399  VAL   A CB     1 
ATOM   3138 C CG1    . VAL   A  1 407 ? 27.306 -36.983  9.024   1.00 27.12  ? 399  VAL   A CG1    1 
ATOM   3139 C CG2    . VAL   A  1 407 ? 24.805 -36.918  9.172   1.00 27.07  ? 399  VAL   A CG2    1 
ATOM   3140 N N      . THR   A  1 408 ? 27.443 -36.071  5.457   1.00 26.17  ? 400  THR   A N      1 
ATOM   3141 C CA     . THR   A  1 408 ? 28.613 -35.989  4.567   1.00 25.70  ? 400  THR   A CA     1 
ATOM   3142 C C      . THR   A  1 408 ? 28.714 -34.576  3.980   1.00 27.64  ? 400  THR   A C      1 
ATOM   3143 O O      . THR   A  1 408 ? 29.797 -34.000  3.960   1.00 27.56  ? 400  THR   A O      1 
ATOM   3144 C CB     . THR   A  1 408 ? 28.500 -37.035  3.444   1.00 33.24  ? 400  THR   A CB     1 
ATOM   3145 O OG1    . THR   A  1 408 ? 28.071 -38.284  3.995   1.00 36.15  ? 400  THR   A OG1    1 
ATOM   3146 C CG2    . THR   A  1 408 ? 29.800 -37.212  2.675   1.00 28.16  ? 400  THR   A CG2    1 
ATOM   3147 N N      . LEU   A  1 409 ? 27.576 -34.022  3.537   1.00 23.29  ? 401  LEU   A N      1 
ATOM   3148 C CA     . LEU   A  1 409 ? 27.471 -32.697  2.938   1.00 23.02  ? 401  LEU   A CA     1 
ATOM   3149 C C      . LEU   A  1 409 ? 27.872 -31.590  3.902   1.00 28.75  ? 401  LEU   A C      1 
ATOM   3150 O O      . LEU   A  1 409 ? 28.564 -30.654  3.492   1.00 28.63  ? 401  LEU   A O      1 
ATOM   3151 C CB     . LEU   A  1 409 ? 26.036 -32.441  2.463   1.00 22.71  ? 401  LEU   A CB     1 
ATOM   3152 C CG     . LEU   A  1 409 ? 25.581 -33.076  1.159   1.00 26.79  ? 401  LEU   A CG     1 
ATOM   3153 C CD1    . LEU   A  1 409 ? 24.104 -32.820  0.949   1.00 26.14  ? 401  LEU   A CD1    1 
ATOM   3154 C CD2    . LEU   A  1 409 ? 26.365 -32.518  -0.038  1.00 28.76  ? 401  LEU   A CD2    1 
ATOM   3155 N N      . GLU   A  1 410 ? 27.400 -31.670  5.169   1.00 25.54  ? 402  GLU   A N      1 
ATOM   3156 C CA     . GLU   A  1 410 ? 27.674 -30.642  6.179   1.00 24.77  ? 402  GLU   A CA     1 
ATOM   3157 C C      . GLU   A  1 410 ? 29.087 -30.735  6.724   1.00 29.49  ? 402  GLU   A C      1 
ATOM   3158 O O      . GLU   A  1 410 ? 29.657 -29.711  7.092   1.00 29.41  ? 402  GLU   A O      1 
ATOM   3159 C CB     . GLU   A  1 410 ? 26.614 -30.639  7.273   1.00 25.63  ? 402  GLU   A CB     1 
ATOM   3160 C CG     . GLU   A  1 410 ? 25.289 -30.132  6.732   1.00 32.91  ? 402  GLU   A CG     1 
ATOM   3161 C CD     . GLU   A  1 410 ? 24.137 -29.983  7.703   1.00 52.77  ? 402  GLU   A CD     1 
ATOM   3162 O OE1    . GLU   A  1 410 ? 24.006 -30.838  8.607   1.00 47.07  ? 402  GLU   A OE1    1 
ATOM   3163 O OE2    . GLU   A  1 410 ? 23.312 -29.062  7.504   1.00 50.31  ? 402  GLU   A OE2    1 
ATOM   3164 N N      . ASN   A  1 411 ? 29.683 -31.940  6.717   1.00 26.98  ? 403  ASN   A N      1 
ATOM   3165 C CA     . ASN   A  1 411 ? 31.072 -32.115  7.135   1.00 27.30  ? 403  ASN   A CA     1 
ATOM   3166 C C      . ASN   A  1 411 ? 32.010 -31.594  6.044   1.00 33.53  ? 403  ASN   A C      1 
ATOM   3167 O O      . ASN   A  1 411 ? 33.026 -30.965  6.362   1.00 32.91  ? 403  ASN   A O      1 
ATOM   3168 C CB     . ASN   A  1 411 ? 31.378 -33.554  7.518   1.00 25.08  ? 403  ASN   A CB     1 
ATOM   3169 C CG     . ASN   A  1 411 ? 31.028 -33.852  8.954   1.00 36.59  ? 403  ASN   A CG     1 
ATOM   3170 O OD1    . ASN   A  1 411 ? 31.768 -33.525  9.881   1.00 29.80  ? 403  ASN   A OD1    1 
ATOM   3171 N ND2    . ASN   A  1 411 ? 29.885 -34.468  9.174   1.00 27.89  ? 403  ASN   A ND2    1 
ATOM   3172 N N      . TRP   A  1 412 ? 31.630 -31.794  4.762   1.00 31.40  ? 404  TRP   A N      1 
ATOM   3173 C CA     . TRP   A  1 412 ? 32.393 -31.300  3.617   1.00 32.31  ? 404  TRP   A CA     1 
ATOM   3174 C C      . TRP   A  1 412 ? 32.279 -29.770  3.518   1.00 32.55  ? 404  TRP   A C      1 
ATOM   3175 O O      . TRP   A  1 412 ? 33.279 -29.115  3.251   1.00 31.19  ? 404  TRP   A O      1 
ATOM   3176 C CB     . TRP   A  1 412 ? 31.952 -31.979  2.306   1.00 32.87  ? 404  TRP   A CB     1 
ATOM   3177 C CG     . TRP   A  1 412 ? 32.989 -31.920  1.220   1.00 35.10  ? 404  TRP   A CG     1 
ATOM   3178 C CD1    . TRP   A  1 412 ? 33.378 -30.817  0.517   1.00 38.17  ? 404  TRP   A CD1    1 
ATOM   3179 C CD2    . TRP   A  1 412 ? 33.785 -33.007  0.731   1.00 35.41  ? 404  TRP   A CD2    1 
ATOM   3180 N NE1    . TRP   A  1 412 ? 34.342 -31.154  -0.403  1.00 38.13  ? 404  TRP   A NE1    1 
ATOM   3181 C CE2    . TRP   A  1 412 ? 34.621 -32.490  -0.287  1.00 39.61  ? 404  TRP   A CE2    1 
ATOM   3182 C CE3    . TRP   A  1 412 ? 33.857 -34.374  1.033   1.00 36.83  ? 404  TRP   A CE3    1 
ATOM   3183 C CZ2    . TRP   A  1 412 ? 35.528 -33.289  -0.993  1.00 39.11  ? 404  TRP   A CZ2    1 
ATOM   3184 C CZ3    . TRP   A  1 412 ? 34.749 -35.168  0.325   1.00 38.78  ? 404  TRP   A CZ3    1 
ATOM   3185 C CH2    . TRP   A  1 412 ? 35.572 -34.626  -0.674  1.00 39.50  ? 404  TRP   A CH2    1 
ATOM   3186 N N      . GLN   A  1 413 ? 31.080 -29.204  3.749   1.00 27.94  ? 405  GLN   A N      1 
ATOM   3187 C CA     . GLN   A  1 413 ? 30.859 -27.758  3.714   1.00 28.44  ? 405  GLN   A CA     1 
ATOM   3188 C C      . GLN   A  1 413 ? 31.734 -27.021  4.762   1.00 36.02  ? 405  GLN   A C      1 
ATOM   3189 O O      . GLN   A  1 413 ? 32.268 -25.948  4.468   1.00 35.44  ? 405  GLN   A O      1 
ATOM   3190 C CB     . GLN   A  1 413 ? 29.367 -27.441  3.930   1.00 29.40  ? 405  GLN   A CB     1 
ATOM   3191 C CG     . GLN   A  1 413 ? 28.947 -26.010  3.589   1.00 36.46  ? 405  GLN   A CG     1 
ATOM   3192 C CD     . GLN   A  1 413 ? 29.053 -25.014  4.731   1.00 55.75  ? 405  GLN   A CD     1 
ATOM   3193 O OE1    . GLN   A  1 413 ? 29.456 -25.335  5.856   1.00 50.24  ? 405  GLN   A OE1    1 
ATOM   3194 N NE2    . GLN   A  1 413 ? 28.671 -23.770  4.468   1.00 47.52  ? 405  GLN   A NE2    1 
ATOM   3195 N N      . PHE   A  1 414 ? 31.848 -27.581  5.979   1.00 34.42  ? 406  PHE   A N      1 
ATOM   3196 C CA     . PHE   A  1 414 ? 32.623 -26.969  7.051   1.00 35.59  ? 406  PHE   A CA     1 
ATOM   3197 C C      . PHE   A  1 414 ? 34.125 -27.027  6.766   1.00 40.89  ? 406  PHE   A C      1 
ATOM   3198 O O      . PHE   A  1 414 ? 34.816 -26.025  6.923   1.00 40.71  ? 406  PHE   A O      1 
ATOM   3199 C CB     . PHE   A  1 414 ? 32.285 -27.625  8.410   1.00 37.83  ? 406  PHE   A CB     1 
ATOM   3200 C CG     . PHE   A  1 414 ? 33.048 -27.054  9.583   1.00 40.07  ? 406  PHE   A CG     1 
ATOM   3201 C CD1    . PHE   A  1 414 ? 32.606 -25.904  10.227  1.00 43.68  ? 406  PHE   A CD1    1 
ATOM   3202 C CD2    . PHE   A  1 414 ? 34.209 -27.667  10.045  1.00 42.48  ? 406  PHE   A CD2    1 
ATOM   3203 C CE1    . PHE   A  1 414 ? 33.321 -25.367  11.305  1.00 44.81  ? 406  PHE   A CE1    1 
ATOM   3204 C CE2    . PHE   A  1 414 ? 34.926 -27.126  11.118  1.00 45.64  ? 406  PHE   A CE2    1 
ATOM   3205 C CZ     . PHE   A  1 414 ? 34.475 -25.981  11.742  1.00 43.72  ? 406  PHE   A CZ     1 
ATOM   3206 N N      . GLU   A  1 415 ? 34.613 -28.195  6.344   1.00 38.01  ? 407  GLU   A N      1 
ATOM   3207 C CA     . GLU   A  1 415 ? 36.021 -28.459  6.093   1.00 38.36  ? 407  GLU   A CA     1 
ATOM   3208 C C      . GLU   A  1 415 ? 36.573 -27.952  4.762   1.00 44.72  ? 407  GLU   A C      1 
ATOM   3209 O O      . GLU   A  1 415 ? 37.750 -27.587  4.728   1.00 45.04  ? 407  GLU   A O      1 
ATOM   3210 C CB     . GLU   A  1 415 ? 36.303 -29.965  6.221   1.00 39.60  ? 407  GLU   A CB     1 
ATOM   3211 C CG     . GLU   A  1 415 ? 36.180 -30.488  7.642   1.00 50.47  ? 407  GLU   A CG     1 
ATOM   3212 C CD     . GLU   A  1 415 ? 36.198 -31.992  7.831   1.00 68.99  ? 407  GLU   A CD     1 
ATOM   3213 O OE1    . GLU   A  1 415 ? 37.139 -32.652  7.333   1.00 56.07  ? 407  GLU   A OE1    1 
ATOM   3214 O OE2    . GLU   A  1 415 ? 35.304 -32.502  8.544   1.00 68.63  ? 407  GLU   A OE2    1 
ATOM   3215 N N      . GLU   A  1 416 ? 35.771 -27.972  3.664   1.00 41.62  ? 408  GLU   A N      1 
ATOM   3216 C CA     . GLU   A  1 416 ? 36.257 -27.632  2.318   1.00 41.33  ? 408  GLU   A CA     1 
ATOM   3217 C C      . GLU   A  1 416 ? 35.556 -26.476  1.580   1.00 44.77  ? 408  GLU   A C      1 
ATOM   3218 O O      . GLU   A  1 416 ? 36.244 -25.570  1.110   1.00 45.17  ? 408  GLU   A O      1 
ATOM   3219 C CB     . GLU   A  1 416 ? 36.229 -28.880  1.407   1.00 42.78  ? 408  GLU   A CB     1 
ATOM   3220 C CG     . GLU   A  1 416 ? 37.042 -30.074  1.897   1.00 55.01  ? 408  GLU   A CG     1 
ATOM   3221 C CD     . GLU   A  1 416 ? 38.549 -29.921  1.821   1.00 83.69  ? 408  GLU   A CD     1 
ATOM   3222 O OE1    . GLU   A  1 416 ? 39.088 -29.842  0.693   1.00 82.50  ? 408  GLU   A OE1    1 
ATOM   3223 O OE2    . GLU   A  1 416 ? 39.196 -29.900  2.893   1.00 82.66  ? 408  GLU   A OE2    1 
ATOM   3224 N N      . TRP   A  1 417 ? 34.227 -26.538  1.400   1.00 39.74  ? 409  TRP   A N      1 
ATOM   3225 C CA     . TRP   A  1 417 ? 33.491 -25.554  0.608   1.00 38.65  ? 409  TRP   A CA     1 
ATOM   3226 C C      . TRP   A  1 417 ? 33.374 -24.166  1.221   1.00 42.48  ? 409  TRP   A C      1 
ATOM   3227 O O      . TRP   A  1 417 ? 33.645 -23.181  0.532   1.00 42.52  ? 409  TRP   A O      1 
ATOM   3228 C CB     . TRP   A  1 417 ? 32.092 -26.068  0.229   1.00 36.69  ? 409  TRP   A CB     1 
ATOM   3229 C CG     . TRP   A  1 417 ? 32.078 -27.335  -0.580  1.00 37.29  ? 409  TRP   A CG     1 
ATOM   3230 C CD1    . TRP   A  1 417 ? 32.963 -27.706  -1.550  1.00 40.05  ? 409  TRP   A CD1    1 
ATOM   3231 C CD2    . TRP   A  1 417 ? 31.089 -28.374  -0.519  1.00 36.88  ? 409  TRP   A CD2    1 
ATOM   3232 N NE1    . TRP   A  1 417 ? 32.605 -28.925  -2.077  1.00 39.39  ? 409  TRP   A NE1    1 
ATOM   3233 C CE2    . TRP   A  1 417 ? 31.441 -29.345  -1.483  1.00 40.74  ? 409  TRP   A CE2    1 
ATOM   3234 C CE3    . TRP   A  1 417 ? 29.935 -28.579  0.260   1.00 37.77  ? 409  TRP   A CE3    1 
ATOM   3235 C CZ2    . TRP   A  1 417 ? 30.707 -30.529  -1.657  1.00 39.63  ? 409  TRP   A CZ2    1 
ATOM   3236 C CZ3    . TRP   A  1 417 ? 29.198 -29.740  0.072   1.00 39.21  ? 409  TRP   A CZ3    1 
ATOM   3237 C CH2    . TRP   A  1 417 ? 29.574 -30.690  -0.888  1.00 39.78  ? 409  TRP   A CH2    1 
ATOM   3238 N N      . GLY   A  1 418 ? 32.894 -24.094  2.458   1.00 37.90  ? 410  GLY   A N      1 
ATOM   3239 C CA     . GLY   A  1 418 ? 32.667 -22.830  3.142   1.00 37.23  ? 410  GLY   A CA     1 
ATOM   3240 C C      . GLY   A  1 418 ? 31.341 -22.202  2.767   1.00 41.10  ? 410  GLY   A C      1 
ATOM   3241 O O      . GLY   A  1 418 ? 30.434 -22.888  2.279   1.00 39.58  ? 410  GLY   A O      1 
ATOM   3242 N N      . SER   A  1 419 ? 31.237 -20.872  2.982   1.00 38.39  ? 411  SER   A N      1 
ATOM   3243 C CA     . SER   A  1 419 ? 30.049 -20.041  2.744   1.00 38.44  ? 411  SER   A CA     1 
ATOM   3244 C C      . SER   A  1 419 ? 29.459 -20.117  1.324   1.00 40.95  ? 411  SER   A C      1 
ATOM   3245 O O      . SER   A  1 419 ? 28.248 -19.907  1.169   1.00 40.74  ? 411  SER   A O      1 
ATOM   3246 C CB     . SER   A  1 419 ? 30.337 -18.585  3.106   1.00 42.87  ? 411  SER   A CB     1 
ATOM   3247 O OG     . SER   A  1 419 ? 31.422 -18.075  2.345   1.00 51.75  ? 411  SER   A OG     1 
ATOM   3248 N N      . GLN   A  1 420 ? 30.307 -20.376  0.296   1.00 36.11  ? 412  GLN   A N      1 
ATOM   3249 C CA     . GLN   A  1 420 ? 29.887 -20.494  -1.111  1.00 36.01  ? 412  GLN   A CA     1 
ATOM   3250 C C      . GLN   A  1 420 ? 28.743 -21.517  -1.279  1.00 39.40  ? 412  GLN   A C      1 
ATOM   3251 O O      . GLN   A  1 420 ? 27.804 -21.269  -2.040  1.00 39.34  ? 412  GLN   A O      1 
ATOM   3252 C CB     . GLN   A  1 420 ? 31.078 -20.874  -2.011  1.00 37.22  ? 412  GLN   A CB     1 
ATOM   3253 C CG     . GLN   A  1 420 ? 30.790 -20.703  -3.503  1.00 47.90  ? 412  GLN   A CG     1 
ATOM   3254 C CD     . GLN   A  1 420 ? 31.991 -20.899  -4.401  1.00 65.74  ? 412  GLN   A CD     1 
ATOM   3255 O OE1    . GLN   A  1 420 ? 33.023 -21.475  -4.018  1.00 62.78  ? 412  GLN   A OE1    1 
ATOM   3256 N NE2    . GLN   A  1 420 ? 31.855 -20.468  -5.649  1.00 50.92  ? 412  GLN   A NE2    1 
ATOM   3257 N N      . VAL   A  1 421 ? 28.811 -22.632  -0.531  1.00 34.93  ? 413  VAL   A N      1 
ATOM   3258 C CA     . VAL   A  1 421 ? 27.807 -23.698  -0.563  1.00 33.92  ? 413  VAL   A CA     1 
ATOM   3259 C C      . VAL   A  1 421 ? 26.920 -23.669  0.695   1.00 34.07  ? 413  VAL   A C      1 
ATOM   3260 O O      . VAL   A  1 421 ? 27.426 -23.739  1.811   1.00 33.12  ? 413  VAL   A O      1 
ATOM   3261 C CB     . VAL   A  1 421 ? 28.445 -25.098  -0.813  1.00 37.63  ? 413  VAL   A CB     1 
ATOM   3262 C CG1    . VAL   A  1 421 ? 27.389 -26.201  -0.831  1.00 37.42  ? 413  VAL   A CG1    1 
ATOM   3263 C CG2    . VAL   A  1 421 ? 29.253 -25.115  -2.108  1.00 37.28  ? 413  VAL   A CG2    1 
ATOM   3264 N N      . THR   A  1 422 ? 25.604 -23.539  0.497   1.00 29.71  ? 414  THR   A N      1 
ATOM   3265 C CA     . THR   A  1 422 ? 24.614 -23.589  1.568   1.00 29.38  ? 414  THR   A CA     1 
ATOM   3266 C C      . THR   A  1 422 ? 23.983 -24.992  1.492   1.00 32.20  ? 414  THR   A C      1 
ATOM   3267 O O      . THR   A  1 422 ? 23.379 -25.332  0.474   1.00 31.81  ? 414  THR   A O      1 
ATOM   3268 C CB     . THR   A  1 422 ? 23.571 -22.445  1.423   1.00 37.32  ? 414  THR   A CB     1 
ATOM   3269 O OG1    . THR   A  1 422 ? 24.228 -21.173  1.477   1.00 38.36  ? 414  THR   A OG1    1 
ATOM   3270 C CG2    . THR   A  1 422 ? 22.480 -22.498  2.498   1.00 31.79  ? 414  THR   A CG2    1 
ATOM   3271 N N      . VAL   A  1 423 ? 24.147 -25.808  2.543   1.00 28.20  ? 415  VAL   A N      1 
ATOM   3272 C CA     . VAL   A  1 423 ? 23.562 -27.156  2.579   1.00 26.88  ? 415  VAL   A CA     1 
ATOM   3273 C C      . VAL   A  1 423 ? 22.131 -27.061  3.119   1.00 30.48  ? 415  VAL   A C      1 
ATOM   3274 O O      . VAL   A  1 423 ? 21.889 -26.389  4.127   1.00 28.69  ? 415  VAL   A O      1 
ATOM   3275 C CB     . VAL   A  1 423 ? 24.429 -28.175  3.365   1.00 29.52  ? 415  VAL   A CB     1 
ATOM   3276 C CG1    . VAL   A  1 423 ? 23.755 -29.549  3.435   1.00 28.52  ? 415  VAL   A CG1    1 
ATOM   3277 C CG2    . VAL   A  1 423 ? 25.824 -28.294  2.754   1.00 29.15  ? 415  VAL   A CG2    1 
ATOM   3278 N N      . VAL   A  1 424 ? 21.185 -27.715  2.425   1.00 26.88  ? 416  VAL   A N      1 
ATOM   3279 C CA     . VAL   A  1 424 ? 19.773 -27.744  2.802   1.00 26.08  ? 416  VAL   A CA     1 
ATOM   3280 C C      . VAL   A  1 424 ? 19.310 -29.199  2.997   1.00 30.86  ? 416  VAL   A C      1 
ATOM   3281 O O      . VAL   A  1 424 ? 19.363 -30.009  2.058   1.00 29.50  ? 416  VAL   A O      1 
ATOM   3282 C CB     . VAL   A  1 424 ? 18.875 -26.999  1.781   1.00 29.37  ? 416  VAL   A CB     1 
ATOM   3283 C CG1    . VAL   A  1 424 ? 17.407 -27.093  2.175   1.00 28.86  ? 416  VAL   A CG1    1 
ATOM   3284 C CG2    . VAL   A  1 424 ? 19.300 -25.538  1.619   1.00 29.25  ? 416  VAL   A CG2    1 
ATOM   3285 N N      . SER   A  1 425 ? 18.835 -29.508  4.212   1.00 27.13  ? 417  SER   A N      1 
ATOM   3286 C CA     . SER   A  1 425 ? 18.295 -30.818  4.548   1.00 26.78  ? 417  SER   A CA     1 
ATOM   3287 C C      . SER   A  1 425 ? 16.789 -30.752  4.365   1.00 30.95  ? 417  SER   A C      1 
ATOM   3288 O O      . SER   A  1 425 ? 16.077 -30.344  5.277   1.00 31.76  ? 417  SER   A O      1 
ATOM   3289 C CB     . SER   A  1 425 ? 18.652 -31.199  5.975   1.00 28.65  ? 417  SER   A CB     1 
ATOM   3290 O OG     . SER   A  1 425 ? 18.402 -32.583  6.137   1.00 36.64  ? 417  SER   A OG     1 
ATOM   3291 N N      . SER   A  1 426 ? 16.304 -31.091  3.157   1.00 26.51  ? 418  SER   A N      1 
ATOM   3292 C CA     . SER   A  1 426 ? 14.877 -30.996  2.823   1.00 25.44  ? 418  SER   A CA     1 
ATOM   3293 C C      . SER   A  1 426 ? 14.547 -31.721  1.533   1.00 28.72  ? 418  SER   A C      1 
ATOM   3294 O O      . SER   A  1 426 ? 15.434 -31.989  0.719   1.00 28.71  ? 418  SER   A O      1 
ATOM   3295 C CB     . SER   A  1 426 ? 14.486 -29.523  2.647   1.00 28.11  ? 418  SER   A CB     1 
ATOM   3296 O OG     . SER   A  1 426 ? 13.113 -29.339  2.341   1.00 33.04  ? 418  SER   A OG     1 
ATOM   3297 N N      . ASP   A  1 427 ? 13.244 -31.966  1.324   1.00 24.47  ? 419  ASP   A N      1 
ATOM   3298 C CA     . ASP   A  1 427 ? 12.703 -32.486  0.083   1.00 24.43  ? 419  ASP   A CA     1 
ATOM   3299 C C      . ASP   A  1 427 ? 12.581 -31.237  -0.815  1.00 28.62  ? 419  ASP   A C      1 
ATOM   3300 O O      . ASP   A  1 427 ? 12.114 -30.199  -0.341  1.00 28.84  ? 419  ASP   A O      1 
ATOM   3301 C CB     . ASP   A  1 427 ? 11.300 -33.088  0.312   1.00 25.92  ? 419  ASP   A CB     1 
ATOM   3302 C CG     . ASP   A  1 427 ? 10.762 -33.900  -0.864  1.00 31.45  ? 419  ASP   A CG     1 
ATOM   3303 O OD1    . ASP   A  1 427 ? 10.672 -33.347  -1.986  1.00 27.14  ? 419  ASP   A OD1    1 
ATOM   3304 O OD2    . ASP   A  1 427 ? 10.416 -35.079  -0.658  1.00 40.00  ? 419  ASP   A OD2    1 
ATOM   3305 N N      . MET   A  1 428 ? 12.984 -31.331  -2.094  1.00 23.42  ? 420  MET   A N      1 
ATOM   3306 C CA     . MET   A  1 428 ? 12.892 -30.196  -3.019  1.00 22.28  ? 420  MET   A CA     1 
ATOM   3307 C C      . MET   A  1 428 ? 11.458 -29.709  -3.249  1.00 28.34  ? 420  MET   A C      1 
ATOM   3308 O O      . MET   A  1 428 ? 11.265 -28.565  -3.645  1.00 28.50  ? 420  MET   A O      1 
ATOM   3309 C CB     . MET   A  1 428 ? 13.599 -30.487  -4.348  1.00 23.81  ? 420  MET   A CB     1 
ATOM   3310 C CG     . MET   A  1 428 ? 12.893 -31.510  -5.232  1.00 26.12  ? 420  MET   A CG     1 
ATOM   3311 S SD     . MET   A  1 428 ? 13.868 -31.853  -6.702  1.00 29.39  ? 420  MET   A SD     1 
ATOM   3312 C CE     . MET   A  1 428 ? 15.131 -32.927  -6.003  1.00 24.93  ? 420  MET   A CE     1 
ATOM   3313 N N      . ARG   A  1 429 ? 10.465 -30.571  -3.003  1.00 26.23  ? 421  ARG   A N      1 
ATOM   3314 C CA     . ARG   A  1 429 ? 9.047  -30.249  -3.177  1.00 26.21  ? 421  ARG   A CA     1 
ATOM   3315 C C      . ARG   A  1 429 ? 8.480  -29.461  -1.995  1.00 32.95  ? 421  ARG   A C      1 
ATOM   3316 O O      . ARG   A  1 429 ? 7.417  -28.858  -2.133  1.00 32.98  ? 421  ARG   A O      1 
ATOM   3317 C CB     . ARG   A  1 429 ? 8.229  -31.526  -3.386  1.00 23.47  ? 421  ARG   A CB     1 
ATOM   3318 C CG     . ARG   A  1 429 ? 8.646  -32.339  -4.619  1.00 26.99  ? 421  ARG   A CG     1 
ATOM   3319 C CD     . ARG   A  1 429 ? 8.017  -33.715  -4.612  1.00 22.72  ? 421  ARG   A CD     1 
ATOM   3320 N NE     . ARG   A  1 429 ? 8.431  -34.507  -3.450  1.00 29.15  ? 421  ARG   A NE     1 
ATOM   3321 C CZ     . ARG   A  1 429 ? 7.785  -35.585  -3.014  1.00 43.15  ? 421  ARG   A CZ     1 
ATOM   3322 N NH1    . ARG   A  1 429 ? 6.699  -36.017  -3.645  1.00 33.75  ? 421  ARG   A NH1    1 
ATOM   3323 N NH2    . ARG   A  1 429 ? 8.218  -36.238  -1.943  1.00 23.03  ? 421  ARG   A NH2    1 
ATOM   3324 N N      . GLU   A  1 430 ? 9.165  -29.483  -0.835  1.00 31.84  ? 422  GLU   A N      1 
ATOM   3325 C CA     . GLU   A  1 430 ? 8.697  -28.805  0.378   1.00 32.77  ? 422  GLU   A CA     1 
ATOM   3326 C C      . GLU   A  1 430 ? 9.556  -27.609  0.792   1.00 37.24  ? 422  GLU   A C      1 
ATOM   3327 O O      . GLU   A  1 430 ? 9.107  -26.793  1.594   1.00 36.99  ? 422  GLU   A O      1 
ATOM   3328 C CB     . GLU   A  1 430 ? 8.547  -29.805  1.539   1.00 34.63  ? 422  GLU   A CB     1 
ATOM   3329 C CG     . GLU   A  1 430 ? 7.449  -30.844  1.334   1.00 49.25  ? 422  GLU   A CG     1 
ATOM   3330 C CD     . GLU   A  1 430 ? 6.000  -30.415  1.518   1.00 82.84  ? 422  GLU   A CD     1 
ATOM   3331 O OE1    . GLU   A  1 430 ? 5.751  -29.289  2.009   1.00 78.32  ? 422  GLU   A OE1    1 
ATOM   3332 O OE2    . GLU   A  1 430 ? 5.106  -31.233  1.196   1.00 84.47  ? 422  GLU   A OE2    1 
ATOM   3333 N N      . TRP   A  1 431 ? 10.777 -27.496  0.244   1.00 34.11  ? 423  TRP   A N      1 
ATOM   3334 C CA     . TRP   A  1 431 ? 11.703 -26.408  0.557   1.00 33.76  ? 423  TRP   A CA     1 
ATOM   3335 C C      . TRP   A  1 431 ? 11.215 -25.037  0.081   1.00 38.71  ? 423  TRP   A C      1 
ATOM   3336 O O      . TRP   A  1 431 ? 10.832 -24.870  -1.080  1.00 38.11  ? 423  TRP   A O      1 
ATOM   3337 C CB     . TRP   A  1 431 ? 13.101 -26.717  0.005   1.00 32.24  ? 423  TRP   A CB     1 
ATOM   3338 C CG     . TRP   A  1 431 ? 14.152 -25.682  0.291   1.00 33.33  ? 423  TRP   A CG     1 
ATOM   3339 C CD1    . TRP   A  1 431 ? 14.497 -25.175  1.511   1.00 36.22  ? 423  TRP   A CD1    1 
ATOM   3340 C CD2    . TRP   A  1 431 ? 15.085 -25.131  -0.650  1.00 33.13  ? 423  TRP   A CD2    1 
ATOM   3341 N NE1    . TRP   A  1 431 ? 15.543 -24.290  1.377   1.00 35.33  ? 423  TRP   A NE1    1 
ATOM   3342 C CE2    . TRP   A  1 431 ? 15.930 -24.251  0.064   1.00 36.90  ? 423  TRP   A CE2    1 
ATOM   3343 C CE3    . TRP   A  1 431 ? 15.261 -25.258  -2.038  1.00 34.29  ? 423  TRP   A CE3    1 
ATOM   3344 C CZ2    . TRP   A  1 431 ? 16.947 -23.516  -0.563  1.00 36.36  ? 423  TRP   A CZ2    1 
ATOM   3345 C CZ3    . TRP   A  1 431 ? 16.264 -24.529  -2.657  1.00 35.62  ? 423  TRP   A CZ3    1 
ATOM   3346 C CH2    . TRP   A  1 431 ? 17.096 -23.673  -1.924  1.00 36.27  ? 423  TRP   A CH2    1 
ATOM   3347 N N      . VAL   A  1 432 ? 11.196 -24.073  1.009   1.00 36.27  ? 424  VAL   A N      1 
ATOM   3348 C CA     . VAL   A  1 432 ? 10.848 -22.682  0.737   1.00 35.92  ? 424  VAL   A CA     1 
ATOM   3349 C C      . VAL   A  1 432 ? 12.212 -22.037  0.542   1.00 40.48  ? 424  VAL   A C      1 
ATOM   3350 O O      . VAL   A  1 432 ? 12.943 -21.846  1.514   1.00 40.27  ? 424  VAL   A O      1 
ATOM   3351 C CB     . VAL   A  1 432 ? 10.028 -22.009  1.877   1.00 39.58  ? 424  VAL   A CB     1 
ATOM   3352 C CG1    . VAL   A  1 432 ? 9.748  -20.537  1.557   1.00 39.64  ? 424  VAL   A CG1    1 
ATOM   3353 C CG2    . VAL   A  1 432 ? 8.723  -22.757  2.142   1.00 38.92  ? 424  VAL   A CG2    1 
ATOM   3354 N N      . ALA   A  1 433 ? 12.597 -21.813  -0.724  1.00 37.81  ? 425  ALA   A N      1 
ATOM   3355 C CA     . ALA   A  1 433 ? 13.895 -21.231  -1.071  1.00 37.89  ? 425  ALA   A CA     1 
ATOM   3356 C C      . ALA   A  1 433 ? 13.977 -19.736  -0.675  1.00 41.91  ? 425  ALA   A C      1 
ATOM   3357 O O      . ALA   A  1 433 ? 12.974 -19.030  -0.806  1.00 41.63  ? 425  ALA   A O      1 
ATOM   3358 C CB     . ALA   A  1 433 ? 14.163 -21.404  -2.556  1.00 38.48  ? 425  ALA   A CB     1 
ATOM   3359 N N      . PRO   A  1 434 ? 15.139 -19.239  -0.177  1.00 38.20  ? 426  PRO   A N      1 
ATOM   3360 C CA     . PRO   A  1 434 ? 15.225 -17.809  0.189   1.00 37.87  ? 426  PRO   A CA     1 
ATOM   3361 C C      . PRO   A  1 434 ? 15.355 -16.880  -1.023  1.00 42.43  ? 426  PRO   A C      1 
ATOM   3362 O O      . PRO   A  1 434 ? 15.090 -15.681  -0.906  1.00 42.03  ? 426  PRO   A O      1 
ATOM   3363 C CB     . PRO   A  1 434 ? 16.449 -17.743  1.104   1.00 39.43  ? 426  PRO   A CB     1 
ATOM   3364 C CG     . PRO   A  1 434 ? 17.296 -18.893  0.702   1.00 43.86  ? 426  PRO   A CG     1 
ATOM   3365 C CD     . PRO   A  1 434 ? 16.420 -19.938  0.063   1.00 39.68  ? 426  PRO   A CD     1 
ATOM   3366 N N      . GLU   A  1 435 ? 15.755 -17.439  -2.189  1.00 37.98  ? 427  GLU   A N      1 
ATOM   3367 C CA     . GLU   A  1 435 ? 15.899 -16.723  -3.461  1.00 37.17  ? 427  GLU   A CA     1 
ATOM   3368 C C      . GLU   A  1 435 ? 15.707 -17.667  -4.655  1.00 39.99  ? 427  GLU   A C      1 
ATOM   3369 O O      . GLU   A  1 435 ? 15.804 -18.884  -4.496  1.00 39.98  ? 427  GLU   A O      1 
ATOM   3370 C CB     . GLU   A  1 435 ? 17.255 -15.992  -3.544  1.00 38.40  ? 427  GLU   A CB     1 
ATOM   3371 C CG     . GLU   A  1 435 ? 18.470 -16.908  -3.585  1.00 44.99  ? 427  GLU   A CG     1 
ATOM   3372 C CD     . GLU   A  1 435 ? 19.797 -16.178  -3.619  1.00 55.27  ? 427  GLU   A CD     1 
ATOM   3373 O OE1    . GLU   A  1 435 ? 19.950 -15.251  -4.447  1.00 48.01  ? 427  GLU   A OE1    1 
ATOM   3374 O OE2    . GLU   A  1 435 ? 20.685 -16.532  -2.813  1.00 42.83  ? 427  GLU   A OE2    1 
ATOM   3375 N N      . LYS   A  1 436 ? 15.447 -17.104  -5.845  1.00 34.56  ? 428  LYS   A N      1 
ATOM   3376 C CA     . LYS   A  1 436 ? 15.262 -17.891  -7.061  1.00 32.98  ? 428  LYS   A CA     1 
ATOM   3377 C C      . LYS   A  1 436 ? 16.599 -18.322  -7.678  1.00 34.49  ? 428  LYS   A C      1 
ATOM   3378 O O      . LYS   A  1 436 ? 17.629 -17.670  -7.460  1.00 32.21  ? 428  LYS   A O      1 
ATOM   3379 C CB     . LYS   A  1 436 ? 14.348 -17.181  -8.071  1.00 34.90  ? 428  LYS   A CB     1 
ATOM   3380 C CG     . LYS   A  1 436 ? 12.899 -17.095  -7.601  1.00 46.43  ? 428  LYS   A CG     1 
ATOM   3381 C CD     . LYS   A  1 436 ? 11.925 -16.909  -8.744  1.00 55.07  ? 428  LYS   A CD     1 
ATOM   3382 C CE     . LYS   A  1 436 ? 10.499 -17.066  -8.269  1.00 62.26  ? 428  LYS   A CE     1 
ATOM   3383 N NZ     . LYS   A  1 436 ? 9.521  -16.897  -9.378  1.00 70.10  ? 428  LYS   A NZ     1 
ATOM   3384 N N      . ALA   A  1 437 ? 16.587 -19.454  -8.414  1.00 30.47  ? 429  ALA   A N      1 
ATOM   3385 C CA     . ALA   A  1 437 ? 17.794 -19.978  -9.045  1.00 29.95  ? 429  ALA   A CA     1 
ATOM   3386 C C      . ALA   A  1 437 ? 17.862 -19.610  -10.512 1.00 34.65  ? 429  ALA   A C      1 
ATOM   3387 O O      . ALA   A  1 437 ? 16.828 -19.463  -11.175 1.00 34.44  ? 429  ALA   A O      1 
ATOM   3388 C CB     . ALA   A  1 437 ? 17.864 -21.493  -8.892  1.00 30.51  ? 429  ALA   A CB     1 
ATOM   3389 N N      . ASP   A  1 438 ? 19.094 -19.479  -11.013 1.00 31.41  ? 430  ASP   A N      1 
ATOM   3390 C CA     . ASP   A  1 438 ? 19.389 -19.247  -12.417 1.00 31.83  ? 430  ASP   A CA     1 
ATOM   3391 C C      . ASP   A  1 438 ? 19.451 -20.614  -13.085 1.00 35.29  ? 430  ASP   A C      1 
ATOM   3392 O O      . ASP   A  1 438 ? 18.970 -20.767  -14.208 1.00 34.86  ? 430  ASP   A O      1 
ATOM   3393 C CB     . ASP   A  1 438 ? 20.748 -18.559  -12.568 1.00 34.33  ? 430  ASP   A CB     1 
ATOM   3394 C CG     . ASP   A  1 438 ? 20.705 -17.085  -12.229 1.00 49.58  ? 430  ASP   A CG     1 
ATOM   3395 O OD1    . ASP   A  1 438 ? 20.123 -16.306  -13.028 1.00 50.07  ? 430  ASP   A OD1    1 
ATOM   3396 O OD2    . ASP   A  1 438 ? 21.243 -16.706  -11.158 1.00 54.89  ? 430  ASP   A OD2    1 
ATOM   3397 N N      . ILE   A  1 439 ? 20.084 -21.597  -12.386 1.00 30.73  ? 431  ILE   A N      1 
ATOM   3398 C CA     . ILE   A  1 439 ? 20.293 -22.970  -12.832 1.00 30.16  ? 431  ILE   A CA     1 
ATOM   3399 C C      . ILE   A  1 439 ? 19.931 -23.987  -11.733 1.00 32.68  ? 431  ILE   A C      1 
ATOM   3400 O O      . ILE   A  1 439 ? 20.436 -23.905  -10.610 1.00 31.60  ? 431  ILE   A O      1 
ATOM   3401 C CB     . ILE   A  1 439 ? 21.764 -23.211  -13.319 1.00 33.26  ? 431  ILE   A CB     1 
ATOM   3402 C CG1    . ILE   A  1 439 ? 22.275 -22.106  -14.295 1.00 33.10  ? 431  ILE   A CG1    1 
ATOM   3403 C CG2    . ILE   A  1 439 ? 21.927 -24.619  -13.923 1.00 33.88  ? 431  ILE   A CG2    1 
ATOM   3404 C CD1    . ILE   A  1 439 ? 23.792 -22.115  -14.539 1.00 33.68  ? 431  ILE   A CD1    1 
ATOM   3405 N N      . ILE   A  1 440 ? 19.089 -24.972  -12.085 1.00 28.85  ? 432  ILE   A N      1 
ATOM   3406 C CA     . ILE   A  1 440 ? 18.780 -26.104  -11.200 1.00 27.08  ? 432  ILE   A CA     1 
ATOM   3407 C C      . ILE   A  1 440 ? 19.440 -27.326  -11.824 1.00 27.93  ? 432  ILE   A C      1 
ATOM   3408 O O      . ILE   A  1 440 ? 19.255 -27.590  -13.009 1.00 27.55  ? 432  ILE   A O      1 
ATOM   3409 C CB     . ILE   A  1 440 ? 17.293 -26.287  -10.770 1.00 29.67  ? 432  ILE   A CB     1 
ATOM   3410 C CG1    . ILE   A  1 440 ? 16.340 -26.477  -11.972 1.00 29.80  ? 432  ILE   A CG1    1 
ATOM   3411 C CG2    . ILE   A  1 440 ? 16.845 -25.126  -9.853  1.00 29.80  ? 432  ILE   A CG2    1 
ATOM   3412 C CD1    . ILE   A  1 440 ? 14.924 -26.948  -11.621 1.00 33.05  ? 432  ILE   A CD1    1 
ATOM   3413 N N      . VAL   A  1 441 ? 20.351 -27.942  -11.084 1.00 23.97  ? 433  VAL   A N      1 
ATOM   3414 C CA     . VAL   A  1 441 ? 21.099 -29.120  -11.523 1.00 23.48  ? 433  VAL   A CA     1 
ATOM   3415 C C      . VAL   A  1 441 ? 20.553 -30.323  -10.724 1.00 27.26  ? 433  VAL   A C      1 
ATOM   3416 O O      . VAL   A  1 441 ? 20.427 -30.232  -9.504  1.00 26.10  ? 433  VAL   A O      1 
ATOM   3417 C CB     . VAL   A  1 441 ? 22.634 -28.931  -11.316 1.00 26.76  ? 433  VAL   A CB     1 
ATOM   3418 C CG1    . VAL   A  1 441 ? 23.419 -30.164  -11.768 1.00 26.14  ? 433  VAL   A CG1    1 
ATOM   3419 C CG2    . VAL   A  1 441 ? 23.143 -27.678  -12.034 1.00 26.43  ? 433  VAL   A CG2    1 
ATOM   3420 N N      . SER   A  1 442 ? 20.193 -31.426  -11.416 1.00 24.01  ? 434  SER   A N      1 
ATOM   3421 C CA     . SER   A  1 442 ? 19.702 -32.636  -10.735 1.00 22.54  ? 434  SER   A CA     1 
ATOM   3422 C C      . SER   A  1 442 ? 20.045 -33.887  -11.507 1.00 25.47  ? 434  SER   A C      1 
ATOM   3423 O O      . SER   A  1 442 ? 20.267 -33.834  -12.718 1.00 24.38  ? 434  SER   A O      1 
ATOM   3424 C CB     . SER   A  1 442 ? 18.193 -32.566  -10.483 1.00 22.50  ? 434  SER   A CB     1 
ATOM   3425 O OG     . SER   A  1 442 ? 17.429 -32.772  -11.658 1.00 25.55  ? 434  SER   A OG     1 
ATOM   3426 N N      . GLU   A  1 443 ? 20.097 -35.016  -10.793 1.00 20.44  ? 435  GLU   A N      1 
ATOM   3427 C CA     . GLU   A  1 443 ? 20.305 -36.328  -11.367 1.00 18.98  ? 435  GLU   A CA     1 
ATOM   3428 C C      . GLU   A  1 443 ? 19.361 -37.245  -10.608 1.00 21.56  ? 435  GLU   A C      1 
ATOM   3429 O O      . GLU   A  1 443 ? 19.753 -37.933  -9.666  1.00 21.95  ? 435  GLU   A O      1 
ATOM   3430 C CB     . GLU   A  1 443 ? 21.775 -36.771  -11.298 1.00 20.37  ? 435  GLU   A CB     1 
ATOM   3431 C CG     . GLU   A  1 443 ? 22.080 -37.968  -12.189 1.00 30.71  ? 435  GLU   A CG     1 
ATOM   3432 C CD     . GLU   A  1 443 ? 21.582 -39.314  -11.685 1.00 45.99  ? 435  GLU   A CD     1 
ATOM   3433 O OE1    . GLU   A  1 443 ? 22.373 -40.052  -11.054 1.00 26.24  ? 435  GLU   A OE1    1 
ATOM   3434 O OE2    . GLU   A  1 443 ? 20.397 -39.637  -11.932 1.00 38.04  ? 435  GLU   A OE2    1 
ATOM   3435 N N      . LEU   A  1 444 ? 18.103 -37.214  -11.009 1.00 18.31  ? 436  LEU   A N      1 
ATOM   3436 C CA     . LEU   A  1 444 ? 17.015 -37.985  -10.394 1.00 18.08  ? 436  LEU   A CA     1 
ATOM   3437 C C      . LEU   A  1 444 ? 16.518 -39.034  -11.373 1.00 23.08  ? 436  LEU   A C      1 
ATOM   3438 O O      . LEU   A  1 444 ? 15.403 -39.535  -11.231 1.00 22.71  ? 436  LEU   A O      1 
ATOM   3439 C CB     . LEU   A  1 444 ? 15.863 -37.023  -10.033 1.00 17.49  ? 436  LEU   A CB     1 
ATOM   3440 C CG     . LEU   A  1 444 ? 16.236 -35.828  -9.141  1.00 21.15  ? 436  LEU   A CG     1 
ATOM   3441 C CD1    . LEU   A  1 444 ? 15.148 -34.776  -9.167  1.00 20.12  ? 436  LEU   A CD1    1 
ATOM   3442 C CD2    . LEU   A  1 444 ? 16.557 -36.284  -7.712  1.00 22.61  ? 436  LEU   A CD2    1 
ATOM   3443 N N      . LEU   A  1 445 ? 17.331 -39.335  -12.391 1.00 19.83  ? 437  LEU   A N      1 
ATOM   3444 C CA     . LEU   A  1 445 ? 16.929 -40.256  -13.439 1.00 20.07  ? 437  LEU   A CA     1 
ATOM   3445 C C      . LEU   A  1 445 ? 17.043 -41.714  -13.073 1.00 21.59  ? 437  LEU   A C      1 
ATOM   3446 O O      . LEU   A  1 445 ? 17.998 -42.117  -12.423 1.00 20.80  ? 437  LEU   A O      1 
ATOM   3447 C CB     . LEU   A  1 445 ? 17.724 -39.973  -14.714 1.00 21.11  ? 437  LEU   A CB     1 
ATOM   3448 C CG     . LEU   A  1 445 ? 17.667 -38.537  -15.248 1.00 26.58  ? 437  LEU   A CG     1 
ATOM   3449 C CD1    . LEU   A  1 445 ? 18.532 -38.402  -16.452 1.00 27.00  ? 437  LEU   A CD1    1 
ATOM   3450 C CD2    . LEU   A  1 445 ? 16.239 -38.127  -15.580 1.00 28.94  ? 437  LEU   A CD2    1 
ATOM   3451 N N      . GLY   A  1 446 ? 16.080 -42.490  -13.527 1.00 19.02  ? 438  GLY   A N      1 
ATOM   3452 C CA     . GLY   A  1 446 ? 16.091 -43.941  -13.394 1.00 19.03  ? 438  GLY   A CA     1 
ATOM   3453 C C      . GLY   A  1 446 ? 16.474 -44.561  -14.729 1.00 22.53  ? 438  GLY   A C      1 
ATOM   3454 O O      . GLY   A  1 446 ? 16.624 -43.848  -15.725 1.00 22.36  ? 438  GLY   A O      1 
ATOM   3455 N N      . SER   A  1 447 ? 16.623 -45.885  -14.765 1.00 18.84  ? 439  SER   A N      1 
ATOM   3456 C CA     . SER   A  1 447 ? 16.944 -46.679  -15.961 1.00 18.37  ? 439  SER   A CA     1 
ATOM   3457 C C      . SER   A  1 447 ? 15.937 -46.453  -17.088 1.00 21.49  ? 439  SER   A C      1 
ATOM   3458 O O      . SER   A  1 447 ? 16.296 -46.553  -18.261 1.00 19.46  ? 439  SER   A O      1 
ATOM   3459 C CB     . SER   A  1 447 ? 16.961 -48.160  -15.604 1.00 22.88  ? 439  SER   A CB     1 
ATOM   3460 O OG     . SER   A  1 447 ? 17.807 -48.390  -14.487 1.00 32.24  ? 439  SER   A OG     1 
ATOM   3461 N N      . PHE   A  1 448 ? 14.673 -46.138  -16.723 1.00 19.19  ? 440  PHE   A N      1 
ATOM   3462 C CA     . PHE   A  1 448 ? 13.583 -45.869  -17.667 1.00 18.13  ? 440  PHE   A CA     1 
ATOM   3463 C C      . PHE   A  1 448 ? 13.222 -44.374  -17.649 1.00 22.54  ? 440  PHE   A C      1 
ATOM   3464 O O      . PHE   A  1 448 ? 12.080 -44.002  -17.930 1.00 21.76  ? 440  PHE   A O      1 
ATOM   3465 C CB     . PHE   A  1 448 ? 12.365 -46.758  -17.332 1.00 19.36  ? 440  PHE   A CB     1 
ATOM   3466 C CG     . PHE   A  1 448 ? 11.364 -46.950  -18.455 1.00 20.38  ? 440  PHE   A CG     1 
ATOM   3467 C CD1    . PHE   A  1 448 ? 11.784 -47.321  -19.731 1.00 22.87  ? 440  PHE   A CD1    1 
ATOM   3468 C CD2    . PHE   A  1 448 ? 9.999  -46.857  -18.212 1.00 21.77  ? 440  PHE   A CD2    1 
ATOM   3469 C CE1    . PHE   A  1 448 ? 10.859 -47.529  -20.756 1.00 23.69  ? 440  PHE   A CE1    1 
ATOM   3470 C CE2    . PHE   A  1 448 ? 9.074  -47.085  -19.233 1.00 24.66  ? 440  PHE   A CE2    1 
ATOM   3471 C CZ     . PHE   A  1 448 ? 9.510  -47.407  -20.499 1.00 22.97  ? 440  PHE   A CZ     1 
ATOM   3472 N N      . ALA   A  1 449 ? 14.235 -43.529  -17.323 1.00 19.34  ? 441  ALA   A N      1 
ATOM   3473 C CA     . ALA   A  1 449 ? 14.240 -42.065  -17.243 1.00 19.17  ? 441  ALA   A CA     1 
ATOM   3474 C C      . ALA   A  1 449 ? 13.423 -41.499  -16.084 1.00 22.85  ? 441  ALA   A C      1 
ATOM   3475 O O      . ALA   A  1 449 ? 14.008 -40.977  -15.138 1.00 23.46  ? 441  ALA   A O      1 
ATOM   3476 C CB     . ALA   A  1 449 ? 13.818 -41.422  -18.572 1.00 19.90  ? 441  ALA   A CB     1 
ATOM   3477 N N      . ASP   A  1 450 ? 12.091 -41.605  -16.159 1.00 18.00  ? 442  ASP   A N      1 
ATOM   3478 C CA     . ASP   A  1 450 ? 11.153 -41.019  -15.209 1.00 18.23  ? 442  ASP   A CA     1 
ATOM   3479 C C      . ASP   A  1 450 ? 10.676 -41.954  -14.076 1.00 20.30  ? 442  ASP   A C      1 
ATOM   3480 O O      . ASP   A  1 450 ? 9.818  -41.545  -13.289 1.00 18.74  ? 442  ASP   A O      1 
ATOM   3481 C CB     . ASP   A  1 450 ? 9.950  -40.463  -15.999 1.00 20.38  ? 442  ASP   A CB     1 
ATOM   3482 C CG     . ASP   A  1 450 ? 9.289  -41.505  -16.883 1.00 31.86  ? 442  ASP   A CG     1 
ATOM   3483 O OD1    . ASP   A  1 450 ? 8.429  -42.249  -16.377 1.00 31.04  ? 442  ASP   A OD1    1 
ATOM   3484 O OD2    . ASP   A  1 450 ? 9.678  -41.612  -18.066 1.00 39.71  ? 442  ASP   A OD2    1 
ATOM   3485 N N      . ASN   A  1 451 ? 11.233 -43.179  -13.976 1.00 17.67  ? 443  ASN   A N      1 
ATOM   3486 C CA     . ASN   A  1 451 ? 10.832 -44.172  -12.961 1.00 17.75  ? 443  ASN   A CA     1 
ATOM   3487 C C      . ASN   A  1 451 ? 11.375 -43.897  -11.534 1.00 22.75  ? 443  ASN   A C      1 
ATOM   3488 O O      . ASN   A  1 451 ? 10.997 -44.597  -10.585 1.00 22.01  ? 443  ASN   A O      1 
ATOM   3489 C CB     . ASN   A  1 451 ? 11.164 -45.587  -13.418 1.00 15.64  ? 443  ASN   A CB     1 
ATOM   3490 C CG     . ASN   A  1 451 ? 12.626 -45.850  -13.595 1.00 27.07  ? 443  ASN   A CG     1 
ATOM   3491 O OD1    . ASN   A  1 451 ? 13.316 -45.182  -14.363 1.00 22.09  ? 443  ASN   A OD1    1 
ATOM   3492 N ND2    . ASN   A  1 451 ? 13.128 -46.826  -12.872 1.00 18.37  ? 443  ASN   A ND2    1 
ATOM   3493 N N      . GLU   A  1 452 ? 12.205 -42.851  -11.372 1.00 19.87  ? 444  GLU   A N      1 
ATOM   3494 C CA     . GLU   A  1 452 ? 12.684 -42.404  -10.066 1.00 19.20  ? 444  GLU   A CA     1 
ATOM   3495 C C      . GLU   A  1 452 ? 11.984 -41.083  -9.693  1.00 24.25  ? 444  GLU   A C      1 
ATOM   3496 O O      . GLU   A  1 452 ? 12.364 -40.393  -8.747  1.00 25.36  ? 444  GLU   A O      1 
ATOM   3497 C CB     . GLU   A  1 452 ? 14.216 -42.321  -10.003 1.00 20.46  ? 444  GLU   A CB     1 
ATOM   3498 C CG     . GLU   A  1 452 ? 14.886 -43.680  -9.854  1.00 23.49  ? 444  GLU   A CG     1 
ATOM   3499 C CD     . GLU   A  1 452 ? 16.367 -43.660  -9.525  1.00 40.86  ? 444  GLU   A CD     1 
ATOM   3500 O OE1    . GLU   A  1 452 ? 16.934 -42.558  -9.345  1.00 38.26  ? 444  GLU   A OE1    1 
ATOM   3501 O OE2    . GLU   A  1 452 ? 16.965 -44.756  -9.443  1.00 37.66  ? 444  GLU   A OE2    1 
ATOM   3502 N N      . LEU   A  1 453 ? 10.904 -40.779  -10.429 1.00 20.50  ? 445  LEU   A N      1 
ATOM   3503 C CA     . LEU   A  1 453 ? 9.983  -39.646  -10.255 1.00 19.73  ? 445  LEU   A CA     1 
ATOM   3504 C C      . LEU   A  1 453 ? 10.639 -38.255  -10.415 1.00 22.02  ? 445  LEU   A C      1 
ATOM   3505 O O      . LEU   A  1 453 ? 10.202 -37.282  -9.793  1.00 19.39  ? 445  LEU   A O      1 
ATOM   3506 C CB     . LEU   A  1 453 ? 9.187  -39.741  -8.934  1.00 19.49  ? 445  LEU   A CB     1 
ATOM   3507 C CG     . LEU   A  1 453 ? 8.601  -41.120  -8.587  1.00 22.97  ? 445  LEU   A CG     1 
ATOM   3508 C CD1    . LEU   A  1 453 ? 7.776  -41.068  -7.323  1.00 22.45  ? 445  LEU   A CD1    1 
ATOM   3509 C CD2    . LEU   A  1 453 ? 7.821  -41.703  -9.732  1.00 25.18  ? 445  LEU   A CD2    1 
ATOM   3510 N N      . SER   A  1 454 ? 11.619 -38.152  -11.335 1.00 19.72  ? 446  SER   A N      1 
ATOM   3511 C CA     . SER   A  1 454 ? 12.225 -36.869  -11.710 1.00 19.38  ? 446  SER   A CA     1 
ATOM   3512 C C      . SER   A  1 454 ? 11.127 -35.859  -12.174 1.00 23.01  ? 446  SER   A C      1 
ATOM   3513 O O      . SER   A  1 454 ? 11.183 -34.723  -11.709 1.00 22.46  ? 446  SER   A O      1 
ATOM   3514 C CB     . SER   A  1 454 ? 13.286 -37.054  -12.788 1.00 21.26  ? 446  SER   A CB     1 
ATOM   3515 O OG     . SER   A  1 454 ? 13.934 -35.818  -13.041 1.00 25.90  ? 446  SER   A OG     1 
ATOM   3516 N N      . PRO   A  1 455 ? 10.080 -36.240  -12.975 1.00 20.77  ? 447  PRO   A N      1 
ATOM   3517 C CA     . PRO   A  1 455 ? 9.049  -35.249  -13.339 1.00 20.81  ? 447  PRO   A CA     1 
ATOM   3518 C C      . PRO   A  1 455 ? 8.344  -34.617  -12.140 1.00 25.04  ? 447  PRO   A C      1 
ATOM   3519 O O      . PRO   A  1 455 ? 8.250  -33.390  -12.096 1.00 24.14  ? 447  PRO   A O      1 
ATOM   3520 C CB     . PRO   A  1 455 ? 8.074  -36.039  -14.228 1.00 22.14  ? 447  PRO   A CB     1 
ATOM   3521 C CG     . PRO   A  1 455 ? 8.858  -37.161  -14.736 1.00 26.30  ? 447  PRO   A CG     1 
ATOM   3522 C CD     . PRO   A  1 455 ? 9.816  -37.530  -13.652 1.00 22.00  ? 447  PRO   A CD     1 
ATOM   3523 N N      . GLU   A  1 456 ? 7.896  -35.434  -11.157 1.00 21.67  ? 448  GLU   A N      1 
ATOM   3524 C CA     . GLU   A  1 456 ? 7.188  -34.957  -9.960  1.00 21.24  ? 448  GLU   A CA     1 
ATOM   3525 C C      . GLU   A  1 456 ? 8.077  -34.123  -9.044  1.00 24.03  ? 448  GLU   A C      1 
ATOM   3526 O O      . GLU   A  1 456 ? 7.625  -33.114  -8.515  1.00 24.41  ? 448  GLU   A O      1 
ATOM   3527 C CB     . GLU   A  1 456 ? 6.557  -36.127  -9.173  1.00 22.83  ? 448  GLU   A CB     1 
ATOM   3528 C CG     . GLU   A  1 456 ? 5.390  -36.816  -9.875  1.00 31.35  ? 448  GLU   A CG     1 
ATOM   3529 C CD     . GLU   A  1 456 ? 5.681  -37.700  -11.080 1.00 36.51  ? 448  GLU   A CD     1 
ATOM   3530 O OE1    . GLU   A  1 456 ? 6.850  -38.096  -11.281 1.00 22.23  ? 448  GLU   A OE1    1 
ATOM   3531 O OE2    . GLU   A  1 456 ? 4.726  -37.998  -11.828 1.00 28.93  ? 448  GLU   A OE2    1 
ATOM   3532 N N      . CYS   A  1 457 ? 9.334  -34.539  -8.851  1.00 20.46  ? 449  CYS   A N      1 
ATOM   3533 C CA     . CYS   A  1 457 ? 10.273 -33.816  -7.999  1.00 21.20  ? 449  CYS   A CA     1 
ATOM   3534 C C      . CYS   A  1 457 ? 10.618 -32.444  -8.589  1.00 26.67  ? 449  CYS   A C      1 
ATOM   3535 O O      . CYS   A  1 457 ? 10.579 -31.446  -7.863  1.00 25.92  ? 449  CYS   A O      1 
ATOM   3536 C CB     . CYS   A  1 457 ? 11.526 -34.648  -7.730  1.00 21.50  ? 449  CYS   A CB     1 
ATOM   3537 S SG     . CYS   A  1 457 ? 11.234 -36.135  -6.724  1.00 24.94  ? 449  CYS   A SG     1 
ATOM   3538 N N      . LEU   A  1 458 ? 10.939 -32.388  -9.903  1.00 23.90  ? 450  LEU   A N      1 
ATOM   3539 C CA     . LEU   A  1 458 ? 11.291 -31.134  -10.571 1.00 24.09  ? 450  LEU   A CA     1 
ATOM   3540 C C      . LEU   A  1 458 ? 10.092 -30.204  -10.761 1.00 28.73  ? 450  LEU   A C      1 
ATOM   3541 O O      . LEU   A  1 458 ? 10.287 -28.992  -10.796 1.00 28.49  ? 450  LEU   A O      1 
ATOM   3542 C CB     . LEU   A  1 458 ? 12.051 -31.368  -11.889 1.00 24.27  ? 450  LEU   A CB     1 
ATOM   3543 C CG     . LEU   A  1 458 ? 13.437 -32.038  -11.754 1.00 28.75  ? 450  LEU   A CG     1 
ATOM   3544 C CD1    . LEU   A  1 458 ? 14.047 -32.333  -13.111 1.00 27.87  ? 450  LEU   A CD1    1 
ATOM   3545 C CD2    . LEU   A  1 458 ? 14.396 -31.205  -10.884 1.00 31.76  ? 450  LEU   A CD2    1 
ATOM   3546 N N      . ASP   A  1 459 ? 8.860  -30.747  -10.817 1.00 27.10  ? 451  ASP   A N      1 
ATOM   3547 C CA     . ASP   A  1 459 ? 7.631  -29.942  -10.924 1.00 27.81  ? 451  ASP   A CA     1 
ATOM   3548 C C      . ASP   A  1 459 ? 7.378  -29.169  -9.629  1.00 33.47  ? 451  ASP   A C      1 
ATOM   3549 O O      . ASP   A  1 459 ? 6.910  -28.036  -9.680  1.00 33.40  ? 451  ASP   A O      1 
ATOM   3550 C CB     . ASP   A  1 459 ? 6.399  -30.810  -11.248 1.00 29.12  ? 451  ASP   A CB     1 
ATOM   3551 C CG     . ASP   A  1 459 ? 6.258  -31.256  -12.691 1.00 36.93  ? 451  ASP   A CG     1 
ATOM   3552 O OD1    . ASP   A  1 459 ? 7.050  -30.783  -13.552 1.00 34.76  ? 451  ASP   A OD1    1 
ATOM   3553 O OD2    . ASP   A  1 459 ? 5.398  -32.112  -12.956 1.00 45.30  ? 451  ASP   A OD2    1 
ATOM   3554 N N      . GLY   A  1 460 ? 7.693  -29.789  -8.493  1.00 30.76  ? 452  GLY   A N      1 
ATOM   3555 C CA     . GLY   A  1 460 ? 7.549  -29.173  -7.181  1.00 31.27  ? 452  GLY   A CA     1 
ATOM   3556 C C      . GLY   A  1 460 ? 8.694  -28.238  -6.849  1.00 36.18  ? 452  GLY   A C      1 
ATOM   3557 O O      . GLY   A  1 460 ? 8.643  -27.535  -5.843  1.00 36.65  ? 452  GLY   A O      1 
ATOM   3558 N N      . ALA   A  1 461 ? 9.744  -28.235  -7.683  1.00 32.94  ? 453  ALA   A N      1 
ATOM   3559 C CA     . ALA   A  1 461 ? 10.930 -27.405  -7.496  1.00 32.90  ? 453  ALA   A CA     1 
ATOM   3560 C C      . ALA   A  1 461 ? 11.040 -26.242  -8.491  1.00 38.06  ? 453  ALA   A C      1 
ATOM   3561 O O      . ALA   A  1 461 ? 11.822 -25.316  -8.243  1.00 38.41  ? 453  ALA   A O      1 
ATOM   3562 C CB     . ALA   A  1 461 ? 12.176 -28.270  -7.574  1.00 33.38  ? 453  ALA   A CB     1 
ATOM   3563 N N      . GLN   A  1 462 ? 10.275 -26.273  -9.605  1.00 34.46  ? 454  GLN   A N      1 
ATOM   3564 C CA     . GLN   A  1 462 ? 10.383 -25.238  -10.637 1.00 34.61  ? 454  GLN   A CA     1 
ATOM   3565 C C      . GLN   A  1 462 ? 9.859  -23.842  -10.209 1.00 40.19  ? 454  GLN   A C      1 
ATOM   3566 O O      . GLN   A  1 462 ? 10.236 -22.852  -10.844 1.00 40.83  ? 454  GLN   A O      1 
ATOM   3567 C CB     . GLN   A  1 462 ? 9.772  -25.679  -11.975 1.00 35.72  ? 454  GLN   A CB     1 
ATOM   3568 C CG     . GLN   A  1 462 ? 8.251  -25.646  -12.078 1.00 45.50  ? 454  GLN   A CG     1 
ATOM   3569 C CD     . GLN   A  1 462 ? 7.810  -25.877  -13.507 1.00 58.35  ? 454  GLN   A CD     1 
ATOM   3570 O OE1    . GLN   A  1 462 ? 8.460  -26.594  -14.278 1.00 49.21  ? 454  GLN   A OE1    1 
ATOM   3571 N NE2    . GLN   A  1 462 ? 6.690  -25.282  -13.894 1.00 50.06  ? 454  GLN   A NE2    1 
ATOM   3572 N N      . HIS   A  1 463 ? 9.034  -23.755  -9.147  1.00 36.31  ? 455  HIS   A N      1 
ATOM   3573 C CA     . HIS   A  1 463 ? 8.534  -22.471  -8.650  1.00 36.49  ? 455  HIS   A CA     1 
ATOM   3574 C C      . HIS   A  1 463 ? 9.672  -21.572  -8.127  1.00 40.37  ? 455  HIS   A C      1 
ATOM   3575 O O      . HIS   A  1 463 ? 9.538  -20.354  -8.181  1.00 40.93  ? 455  HIS   A O      1 
ATOM   3576 C CB     . HIS   A  1 463 ? 7.430  -22.658  -7.597  1.00 37.46  ? 455  HIS   A CB     1 
ATOM   3577 C CG     . HIS   A  1 463 ? 7.917  -23.207  -6.291  1.00 41.10  ? 455  HIS   A CG     1 
ATOM   3578 N ND1    . HIS   A  1 463 ? 8.011  -22.409  -5.161  1.00 43.13  ? 455  HIS   A ND1    1 
ATOM   3579 C CD2    . HIS   A  1 463 ? 8.341  -24.453  -5.982  1.00 42.91  ? 455  HIS   A CD2    1 
ATOM   3580 C CE1    . HIS   A  1 463 ? 8.475  -23.197  -4.205  1.00 42.52  ? 455  HIS   A CE1    1 
ATOM   3581 N NE2    . HIS   A  1 463 ? 8.695  -24.434  -4.654  1.00 42.76  ? 455  HIS   A NE2    1 
ATOM   3582 N N      . PHE   A  1 464 ? 10.789 -22.156  -7.647  1.00 36.26  ? 456  PHE   A N      1 
ATOM   3583 C CA     . PHE   A  1 464 ? 11.918 -21.350  -7.177  1.00 35.69  ? 456  PHE   A CA     1 
ATOM   3584 C C      . PHE   A  1 464 ? 13.015 -21.205  -8.252  1.00 39.76  ? 456  PHE   A C      1 
ATOM   3585 O O      . PHE   A  1 464 ? 14.150 -20.825  -7.954  1.00 39.24  ? 456  PHE   A O      1 
ATOM   3586 C CB     . PHE   A  1 464 ? 12.471 -21.817  -5.821  1.00 36.79  ? 456  PHE   A CB     1 
ATOM   3587 C CG     . PHE   A  1 464 ? 12.849 -23.269  -5.668  1.00 37.40  ? 456  PHE   A CG     1 
ATOM   3588 C CD1    . PHE   A  1 464 ? 14.038 -23.754  -6.196  1.00 39.88  ? 456  PHE   A CD1    1 
ATOM   3589 C CD2    . PHE   A  1 464 ? 12.070 -24.127  -4.901  1.00 38.66  ? 456  PHE   A CD2    1 
ATOM   3590 C CE1    . PHE   A  1 464 ? 14.408 -25.090  -6.015  1.00 40.65  ? 456  PHE   A CE1    1 
ATOM   3591 C CE2    . PHE   A  1 464 ? 12.444 -25.459  -4.715  1.00 40.68  ? 456  PHE   A CE2    1 
ATOM   3592 C CZ     . PHE   A  1 464 ? 13.612 -25.930  -5.268  1.00 38.67  ? 456  PHE   A CZ     1 
ATOM   3593 N N      . LEU   A  1 465 ? 12.650 -21.478  -9.508  1.00 36.07  ? 457  LEU   A N      1 
ATOM   3594 C CA     . LEU   A  1 465 ? 13.519 -21.292  -10.661 1.00 35.57  ? 457  LEU   A CA     1 
ATOM   3595 C C      . LEU   A  1 465 ? 13.044 -19.996  -11.338 1.00 40.09  ? 457  LEU   A C      1 
ATOM   3596 O O      . LEU   A  1 465 ? 11.833 -19.793  -11.491 1.00 38.96  ? 457  LEU   A O      1 
ATOM   3597 C CB     . LEU   A  1 465 ? 13.412 -22.502  -11.608 1.00 35.40  ? 457  LEU   A CB     1 
ATOM   3598 C CG     . LEU   A  1 465 ? 14.214 -22.491  -12.916 1.00 39.06  ? 457  LEU   A CG     1 
ATOM   3599 C CD1    . LEU   A  1 465 ? 15.709 -22.679  -12.668 1.00 38.27  ? 457  LEU   A CD1    1 
ATOM   3600 C CD2    . LEU   A  1 465 ? 13.707 -23.572  -13.862 1.00 41.29  ? 457  LEU   A CD2    1 
ATOM   3601 N N      . LYS   A  1 466 ? 13.990 -19.105  -11.705 1.00 38.09  ? 458  LYS   A N      1 
ATOM   3602 C CA     . LYS   A  1 466 ? 13.681 -17.827  -12.382 1.00 38.21  ? 458  LYS   A CA     1 
ATOM   3603 C C      . LYS   A  1 466 ? 12.859 -18.056  -13.660 1.00 43.21  ? 458  LYS   A C      1 
ATOM   3604 O O      . LYS   A  1 466 ? 12.904 -19.156  -14.226 1.00 42.72  ? 458  LYS   A O      1 
ATOM   3605 C CB     . LYS   A  1 466 ? 14.978 -17.071  -12.726 1.00 40.32  ? 458  LYS   A CB     1 
ATOM   3606 C CG     . LYS   A  1 466 ? 15.622 -16.382  -11.531 1.00 50.40  ? 458  LYS   A CG     1 
ATOM   3607 C CD     . LYS   A  1 466 ? 16.983 -15.800  -11.874 1.00 60.33  ? 458  LYS   A CD     1 
ATOM   3608 C CE     . LYS   A  1 466 ? 17.691 -15.276  -10.644 1.00 70.10  ? 458  LYS   A CE     1 
ATOM   3609 N NZ     . LYS   A  1 466 ? 18.967 -14.589  -10.980 1.00 76.58  ? 458  LYS   A NZ     1 
ATOM   3610 N N      . ASP   A  1 467 ? 12.112 -17.022  -14.119 1.00 40.45  ? 459  ASP   A N      1 
ATOM   3611 C CA     . ASP   A  1 467 ? 11.298 -17.095  -15.340 1.00 40.21  ? 459  ASP   A CA     1 
ATOM   3612 C C      . ASP   A  1 467 ? 12.141 -17.476  -16.567 1.00 41.68  ? 459  ASP   A C      1 
ATOM   3613 O O      . ASP   A  1 467 ? 11.646 -18.168  -17.451 1.00 41.55  ? 459  ASP   A O      1 
ATOM   3614 C CB     . ASP   A  1 467 ? 10.537 -15.780  -15.583 1.00 43.18  ? 459  ASP   A CB     1 
ATOM   3615 C CG     . ASP   A  1 467 ? 9.483  -15.459  -14.535 1.00 61.93  ? 459  ASP   A CG     1 
ATOM   3616 O OD1    . ASP   A  1 467 ? 8.435  -16.147  -14.513 1.00 63.75  ? 459  ASP   A OD1    1 
ATOM   3617 O OD2    . ASP   A  1 467 ? 9.682  -14.486  -13.770 1.00 70.39  ? 459  ASP   A OD2    1 
ATOM   3618 N N      . ASP   A  1 468 ? 13.418 -17.053  -16.592 1.00 36.65  ? 460  ASP   A N      1 
ATOM   3619 C CA     . ASP   A  1 468 ? 14.377 -17.350  -17.657 1.00 35.97  ? 460  ASP   A CA     1 
ATOM   3620 C C      . ASP   A  1 468 ? 15.367 -18.475  -17.260 1.00 36.75  ? 460  ASP   A C      1 
ATOM   3621 O O      . ASP   A  1 468 ? 16.274 -18.789  -18.033 1.00 35.74  ? 460  ASP   A O      1 
ATOM   3622 C CB     . ASP   A  1 468 ? 15.137 -16.057  -18.059 1.00 38.35  ? 460  ASP   A CB     1 
ATOM   3623 C CG     . ASP   A  1 468 ? 16.276 -15.625  -17.131 1.00 51.09  ? 460  ASP   A CG     1 
ATOM   3624 O OD1    . ASP   A  1 468 ? 16.167 -15.848  -15.898 1.00 52.70  ? 460  ASP   A OD1    1 
ATOM   3625 O OD2    . ASP   A  1 468 ? 17.260 -15.042  -17.634 1.00 56.15  ? 460  ASP   A OD2    1 
ATOM   3626 N N      . GLY   A  1 469 ? 15.193 -19.028  -16.053 1.00 32.20  ? 461  GLY   A N      1 
ATOM   3627 C CA     . GLY   A  1 469 ? 16.039 -20.072  -15.476 1.00 31.73  ? 461  GLY   A CA     1 
ATOM   3628 C C      . GLY   A  1 469 ? 16.141 -21.357  -16.279 1.00 32.68  ? 461  GLY   A C      1 
ATOM   3629 O O      . GLY   A  1 469 ? 15.203 -21.723  -16.988 1.00 32.83  ? 461  GLY   A O      1 
ATOM   3630 N N      . VAL   A  1 470 ? 17.282 -22.055  -16.154 1.00 27.62  ? 462  VAL   A N      1 
ATOM   3631 C CA     . VAL   A  1 470 ? 17.595 -23.306  -16.867 1.00 26.93  ? 462  VAL   A CA     1 
ATOM   3632 C C      . VAL   A  1 470 ? 17.565 -24.523  -15.921 1.00 30.24  ? 462  VAL   A C      1 
ATOM   3633 O O      . VAL   A  1 470 ? 18.032 -24.438  -14.783 1.00 30.01  ? 462  VAL   A O      1 
ATOM   3634 C CB     . VAL   A  1 470 ? 18.972 -23.185  -17.607 1.00 31.03  ? 462  VAL   A CB     1 
ATOM   3635 C CG1    . VAL   A  1 470 ? 19.539 -24.543  -18.039 1.00 30.64  ? 462  VAL   A CG1    1 
ATOM   3636 C CG2    . VAL   A  1 470 ? 18.871 -22.244  -18.809 1.00 31.02  ? 462  VAL   A CG2    1 
ATOM   3637 N N      . SER   A  1 471 ? 17.060 -25.661  -16.423 1.00 25.32  ? 463  SER   A N      1 
ATOM   3638 C CA     . SER   A  1 471 ? 17.082 -26.928  -15.711 1.00 24.05  ? 463  SER   A CA     1 
ATOM   3639 C C      . SER   A  1 471 ? 18.028 -27.866  -16.448 1.00 26.17  ? 463  SER   A C      1 
ATOM   3640 O O      . SER   A  1 471 ? 17.865 -28.087  -17.651 1.00 24.81  ? 463  SER   A O      1 
ATOM   3641 C CB     . SER   A  1 471 ? 15.683 -27.536  -15.619 1.00 26.68  ? 463  SER   A CB     1 
ATOM   3642 O OG     . SER   A  1 471 ? 15.740 -28.878  -15.156 1.00 31.97  ? 463  SER   A OG     1 
ATOM   3643 N N      . ILE   A  1 472 ? 19.035 -28.382  -15.730 1.00 23.35  ? 464  ILE   A N      1 
ATOM   3644 C CA     . ILE   A  1 472 ? 19.984 -29.383  -16.229 1.00 22.63  ? 464  ILE   A CA     1 
ATOM   3645 C C      . ILE   A  1 472 ? 19.637 -30.672  -15.445 1.00 28.23  ? 464  ILE   A C      1 
ATOM   3646 O O      . ILE   A  1 472 ? 19.828 -30.689  -14.227 1.00 27.66  ? 464  ILE   A O      1 
ATOM   3647 C CB     . ILE   A  1 472 ? 21.464 -28.941  -16.071 1.00 24.79  ? 464  ILE   A CB     1 
ATOM   3648 C CG1    . ILE   A  1 472 ? 21.742 -27.668  -16.929 1.00 25.03  ? 464  ILE   A CG1    1 
ATOM   3649 C CG2    . ILE   A  1 472 ? 22.417 -30.097  -16.437 1.00 23.51  ? 464  ILE   A CG2    1 
ATOM   3650 C CD1    . ILE   A  1 472 ? 23.125 -27.059  -16.792 1.00 35.63  ? 464  ILE   A CD1    1 
ATOM   3651 N N      . PRO   A  1 473 ? 19.062 -31.727  -16.072 1.00 25.97  ? 465  PRO   A N      1 
ATOM   3652 C CA     . PRO   A  1 473 ? 18.776 -31.896  -17.510 1.00 25.35  ? 465  PRO   A CA     1 
ATOM   3653 C C      . PRO   A  1 473 ? 17.538 -31.149  -17.983 1.00 26.61  ? 465  PRO   A C      1 
ATOM   3654 O O      . PRO   A  1 473 ? 16.644 -30.855  -17.184 1.00 24.66  ? 465  PRO   A O      1 
ATOM   3655 C CB     . PRO   A  1 473 ? 18.652 -33.421  -17.656 1.00 27.37  ? 465  PRO   A CB     1 
ATOM   3656 C CG     . PRO   A  1 473 ? 18.091 -33.875  -16.338 1.00 31.90  ? 465  PRO   A CG     1 
ATOM   3657 C CD     . PRO   A  1 473 ? 18.694 -32.943  -15.305 1.00 27.95  ? 465  PRO   A CD     1 
ATOM   3658 N N      . GLY   A  1 474 ? 17.547 -30.787  -19.266 1.00 22.98  ? 466  GLY   A N      1 
ATOM   3659 C CA     . GLY   A  1 474 ? 16.459 -30.058  -19.908 1.00 22.65  ? 466  GLY   A CA     1 
ATOM   3660 C C      . GLY   A  1 474 ? 15.360 -30.969  -20.404 1.00 25.87  ? 466  GLY   A C      1 
ATOM   3661 O O      . GLY   A  1 474 ? 14.201 -30.561  -20.468 1.00 25.41  ? 466  GLY   A O      1 
ATOM   3662 N N      . GLU   A  1 475 ? 15.724 -32.203  -20.781 1.00 22.59  ? 467  GLU   A N      1 
ATOM   3663 C CA     . GLU   A  1 475 ? 14.773 -33.218  -21.248 1.00 22.37  ? 467  GLU   A CA     1 
ATOM   3664 C C      . GLU   A  1 475 ? 15.336 -34.625  -21.168 1.00 24.13  ? 467  GLU   A C      1 
ATOM   3665 O O      . GLU   A  1 475 ? 16.550 -34.820  -21.076 1.00 23.89  ? 467  GLU   A O      1 
ATOM   3666 C CB     . GLU   A  1 475 ? 14.190 -32.913  -22.655 1.00 23.75  ? 467  GLU   A CB     1 
ATOM   3667 C CG     . GLU   A  1 475 ? 15.101 -33.188  -23.830 1.00 40.80  ? 467  GLU   A CG     1 
ATOM   3668 C CD     . GLU   A  1 475 ? 14.429 -32.976  -25.173 1.00 68.95  ? 467  GLU   A CD     1 
ATOM   3669 O OE1    . GLU   A  1 475 ? 13.670 -33.872  -25.608 1.00 59.43  ? 467  GLU   A OE1    1 
ATOM   3670 O OE2    . GLU   A  1 475 ? 14.655 -31.909  -25.787 1.00 71.20  ? 467  GLU   A OE2    1 
ATOM   3671 N N      . TYR   A  1 476 ? 14.436 -35.604  -21.157 1.00 19.42  ? 468  TYR   A N      1 
ATOM   3672 C CA     . TYR   A  1 476 ? 14.788 -37.014  -21.144 1.00 18.85  ? 468  TYR   A CA     1 
ATOM   3673 C C      . TYR   A  1 476 ? 13.710 -37.834  -21.796 1.00 22.16  ? 468  TYR   A C      1 
ATOM   3674 O O      . TYR   A  1 476 ? 12.528 -37.473  -21.767 1.00 21.30  ? 468  TYR   A O      1 
ATOM   3675 C CB     . TYR   A  1 476 ? 15.186 -37.539  -19.747 1.00 19.20  ? 468  TYR   A CB     1 
ATOM   3676 C CG     . TYR   A  1 476 ? 14.347 -37.014  -18.611 1.00 19.05  ? 468  TYR   A CG     1 
ATOM   3677 C CD1    . TYR   A  1 476 ? 13.142 -37.618  -18.273 1.00 19.58  ? 468  TYR   A CD1    1 
ATOM   3678 C CD2    . TYR   A  1 476 ? 14.761 -35.914  -17.864 1.00 20.26  ? 468  TYR   A CD2    1 
ATOM   3679 C CE1    . TYR   A  1 476 ? 12.389 -37.173  -17.192 1.00 18.94  ? 468  TYR   A CE1    1 
ATOM   3680 C CE2    . TYR   A  1 476 ? 14.014 -35.457  -16.781 1.00 21.50  ? 468  TYR   A CE2    1 
ATOM   3681 C CZ     . TYR   A  1 476 ? 12.822 -36.084  -16.458 1.00 25.90  ? 468  TYR   A CZ     1 
ATOM   3682 O OH     . TYR   A  1 476 ? 12.070 -35.629  -15.409 1.00 24.01  ? 468  TYR   A OH     1 
ATOM   3683 N N      . THR   A  1 477 ? 14.138 -38.897  -22.453 1.00 19.27  ? 469  THR   A N      1 
ATOM   3684 C CA     . THR   A  1 477 ? 13.257 -39.783  -23.196 1.00 19.46  ? 469  THR   A CA     1 
ATOM   3685 C C      . THR   A  1 477 ? 13.575 -41.227  -22.842 1.00 21.72  ? 469  THR   A C      1 
ATOM   3686 O O      . THR   A  1 477 ? 14.732 -41.628  -22.884 1.00 20.88  ? 469  THR   A O      1 
ATOM   3687 C CB     . THR   A  1 477 ? 13.381 -39.500  -24.731 1.00 24.26  ? 469  THR   A CB     1 
ATOM   3688 O OG1    . THR   A  1 477 ? 13.054 -38.131  -24.995 1.00 26.84  ? 469  THR   A OG1    1 
ATOM   3689 C CG2    . THR   A  1 477 ? 12.484 -40.412  -25.590 1.00 21.59  ? 469  THR   A CG2    1 
ATOM   3690 N N      . SER   A  1 478 ? 12.544 -42.006  -22.526 1.00 18.64  ? 470  SER   A N      1 
ATOM   3691 C CA     . SER   A  1 478 ? 12.701 -43.440  -22.284 1.00 18.55  ? 470  SER   A CA     1 
ATOM   3692 C C      . SER   A  1 478 ? 12.555 -44.187  -23.624 1.00 21.22  ? 470  SER   A C      1 
ATOM   3693 O O      . SER   A  1 478 ? 11.846 -43.728  -24.527 1.00 19.61  ? 470  SER   A O      1 
ATOM   3694 C CB     . SER   A  1 478 ? 11.664 -43.946  -21.289 1.00 18.88  ? 470  SER   A CB     1 
ATOM   3695 O OG     . SER   A  1 478 ? 10.349 -43.652  -21.726 1.00 21.15  ? 470  SER   A OG     1 
ATOM   3696 N N      . PHE   A  1 479 ? 13.218 -45.342  -23.733 1.00 19.46  ? 471  PHE   A N      1 
ATOM   3697 C CA     . PHE   A  1 479 ? 13.183 -46.202  -24.911 1.00 19.90  ? 471  PHE   A CA     1 
ATOM   3698 C C      . PHE   A  1 479 ? 12.800 -47.621  -24.512 1.00 25.57  ? 471  PHE   A C      1 
ATOM   3699 O O      . PHE   A  1 479 ? 13.183 -48.080  -23.436 1.00 26.37  ? 471  PHE   A O      1 
ATOM   3700 C CB     . PHE   A  1 479 ? 14.554 -46.211  -25.609 1.00 21.83  ? 471  PHE   A CB     1 
ATOM   3701 C CG     . PHE   A  1 479 ? 14.832 -44.956  -26.397 1.00 24.13  ? 471  PHE   A CG     1 
ATOM   3702 C CD1    . PHE   A  1 479 ? 15.295 -43.805  -25.763 1.00 27.82  ? 471  PHE   A CD1    1 
ATOM   3703 C CD2    . PHE   A  1 479 ? 14.659 -44.930  -27.775 1.00 26.47  ? 471  PHE   A CD2    1 
ATOM   3704 C CE1    . PHE   A  1 479 ? 15.521 -42.633  -26.489 1.00 29.18  ? 471  PHE   A CE1    1 
ATOM   3705 C CE2    . PHE   A  1 479 ? 14.903 -43.765  -28.504 1.00 29.90  ? 471  PHE   A CE2    1 
ATOM   3706 C CZ     . PHE   A  1 479 ? 15.333 -42.623  -27.857 1.00 28.24  ? 471  PHE   A CZ     1 
ATOM   3707 N N      . LEU   A  1 480 ? 12.068 -48.317  -25.383 1.00 22.01  ? 472  LEU   A N      1 
ATOM   3708 C CA     . LEU   A  1 480 ? 11.678 -49.713  -25.170 1.00 21.37  ? 472  LEU   A CA     1 
ATOM   3709 C C      . LEU   A  1 480 ? 12.073 -50.543  -26.372 1.00 23.19  ? 472  LEU   A C      1 
ATOM   3710 O O      . LEU   A  1 480 ? 11.990 -50.058  -27.498 1.00 22.90  ? 472  LEU   A O      1 
ATOM   3711 C CB     . LEU   A  1 480 ? 10.161 -49.858  -24.992 1.00 21.41  ? 472  LEU   A CB     1 
ATOM   3712 C CG     . LEU   A  1 480 ? 9.545  -49.508  -23.653 1.00 25.61  ? 472  LEU   A CG     1 
ATOM   3713 C CD1    . LEU   A  1 480 ? 8.063  -49.343  -23.818 1.00 25.51  ? 472  LEU   A CD1    1 
ATOM   3714 C CD2    . LEU   A  1 480 ? 9.857  -50.574  -22.584 1.00 24.23  ? 472  LEU   A CD2    1 
ATOM   3715 N N      . ALA   A  1 481 ? 12.425 -51.808  -26.132 1.00 19.17  ? 473  ALA   A N      1 
ATOM   3716 C CA     . ALA   A  1 481 ? 12.759 -52.797  -27.148 1.00 19.92  ? 473  ALA   A CA     1 
ATOM   3717 C C      . ALA   A  1 481 ? 12.217 -54.171  -26.725 1.00 23.64  ? 473  ALA   A C      1 
ATOM   3718 O O      . ALA   A  1 481 ? 12.469 -54.591  -25.596 1.00 23.10  ? 473  ALA   A O      1 
ATOM   3719 C CB     . ALA   A  1 481 ? 14.273 -52.868  -27.349 1.00 20.85  ? 473  ALA   A CB     1 
ATOM   3720 N N      . PRO   A  1 482 ? 11.487 -54.897  -27.604 1.00 20.69  ? 474  PRO   A N      1 
ATOM   3721 C CA     . PRO   A  1 482 ? 11.045 -56.255  -27.240 1.00 20.64  ? 474  PRO   A CA     1 
ATOM   3722 C C      . PRO   A  1 482 ? 12.251 -57.184  -27.174 1.00 24.46  ? 474  PRO   A C      1 
ATOM   3723 O O      . PRO   A  1 482 ? 13.192 -57.020  -27.951 1.00 24.37  ? 474  PRO   A O      1 
ATOM   3724 C CB     . PRO   A  1 482 ? 10.106 -56.646  -28.387 1.00 22.28  ? 474  PRO   A CB     1 
ATOM   3725 C CG     . PRO   A  1 482 ? 10.592 -55.846  -29.551 1.00 26.49  ? 474  PRO   A CG     1 
ATOM   3726 C CD     . PRO   A  1 482 ? 11.112 -54.559  -28.990 1.00 21.62  ? 474  PRO   A CD     1 
ATOM   3727 N N      . ILE   A  1 483 ? 12.252 -58.104  -26.217 1.00 20.69  ? 475  ILE   A N      1 
ATOM   3728 C CA     . ILE   A  1 483 ? 13.359 -59.034  -26.041 1.00 20.57  ? 475  ILE   A CA     1 
ATOM   3729 C C      . ILE   A  1 483 ? 12.898 -60.470  -25.887 1.00 25.15  ? 475  ILE   A C      1 
ATOM   3730 O O      . ILE   A  1 483 ? 11.781 -60.743  -25.440 1.00 23.71  ? 475  ILE   A O      1 
ATOM   3731 C CB     . ILE   A  1 483 ? 14.356 -58.642  -24.899 1.00 23.09  ? 475  ILE   A CB     1 
ATOM   3732 C CG1    . ILE   A  1 483 ? 13.701 -58.712  -23.505 1.00 23.62  ? 475  ILE   A CG1    1 
ATOM   3733 C CG2    . ILE   A  1 483 ? 15.032 -57.283  -25.141 1.00 22.97  ? 475  ILE   A CG2    1 
ATOM   3734 C CD1    . ILE   A  1 483 ? 14.472 -59.499  -22.536 1.00 29.87  ? 475  ILE   A CD1    1 
ATOM   3735 N N      . SER   A  1 484 ? 13.798 -61.393  -26.269 1.00 22.75  ? 476  SER   A N      1 
ATOM   3736 C CA     . SER   A  1 484 ? 13.630 -62.818  -26.076 1.00 21.91  ? 476  SER   A CA     1 
ATOM   3737 C C      . SER   A  1 484 ? 14.741 -63.259  -25.143 1.00 24.18  ? 476  SER   A C      1 
ATOM   3738 O O      . SER   A  1 484 ? 15.907 -62.943  -25.383 1.00 24.08  ? 476  SER   A O      1 
ATOM   3739 C CB     . SER   A  1 484 ? 13.754 -63.574  -27.391 1.00 23.61  ? 476  SER   A CB     1 
ATOM   3740 O OG     . SER   A  1 484 ? 13.434 -64.935  -27.160 1.00 28.33  ? 476  SER   A OG     1 
ATOM   3741 N N      . SER   A  1 485 ? 14.376 -63.972  -24.088 1.00 19.09  ? 477  SER   A N      1 
ATOM   3742 C CA     . SER   A  1 485 ? 15.290 -64.544  -23.105 1.00 19.49  ? 477  SER   A CA     1 
ATOM   3743 C C      . SER   A  1 485 ? 14.547 -65.537  -22.241 1.00 24.51  ? 477  SER   A C      1 
ATOM   3744 O O      . SER   A  1 485 ? 13.862 -65.136  -21.295 1.00 24.64  ? 477  SER   A O      1 
ATOM   3745 C CB     . SER   A  1 485 ? 15.935 -63.473  -22.226 1.00 20.28  ? 477  SER   A CB     1 
ATOM   3746 O OG     . SER   A  1 485 ? 16.788 -64.107  -21.285 1.00 20.03  ? 477  SER   A OG     1 
ATOM   3747 N N      . SER   A  1 486 ? 14.728 -66.840  -22.516 1.00 20.55  ? 478  SER   A N      1 
ATOM   3748 C CA     . SER   A  1 486 ? 14.105 -67.895  -21.724 1.00 20.69  ? 478  SER   A CA     1 
ATOM   3749 C C      . SER   A  1 486 ? 14.763 -67.946  -20.360 1.00 24.60  ? 478  SER   A C      1 
ATOM   3750 O O      . SER   A  1 486 ? 14.112 -68.291  -19.373 1.00 23.56  ? 478  SER   A O      1 
ATOM   3751 C CB     . SER   A  1 486 ? 14.223 -69.238  -22.423 1.00 25.82  ? 478  SER   A CB     1 
ATOM   3752 O OG     . SER   A  1 486 ? 13.231 -69.332  -23.433 1.00 34.04  ? 478  SER   A OG     1 
ATOM   3753 N N      . LYS   A  1 487 ? 16.047 -67.549  -20.304 1.00 22.30  ? 479  LYS   A N      1 
ATOM   3754 C CA     . LYS   A  1 487 ? 16.833 -67.469  -19.074 1.00 22.60  ? 479  LYS   A CA     1 
ATOM   3755 C C      . LYS   A  1 487 ? 16.222 -66.421  -18.108 1.00 23.76  ? 479  LYS   A C      1 
ATOM   3756 O O      . LYS   A  1 487 ? 15.985 -66.740  -16.957 1.00 22.72  ? 479  LYS   A O      1 
ATOM   3757 C CB     . LYS   A  1 487 ? 18.304 -67.121  -19.408 1.00 25.85  ? 479  LYS   A CB     1 
ATOM   3758 C CG     . LYS   A  1 487 ? 19.207 -67.114  -18.178 1.00 33.06  ? 479  LYS   A CG     1 
ATOM   3759 C CD     . LYS   A  1 487 ? 20.411 -66.221  -18.375 1.00 43.07  ? 479  LYS   A CD     1 
ATOM   3760 C CE     . LYS   A  1 487 ? 21.330 -66.233  -17.175 1.00 52.97  ? 479  LYS   A CE     1 
ATOM   3761 N NZ     . LYS   A  1 487 ? 22.011 -67.543  -16.999 1.00 66.48  ? 479  LYS   A NZ     1 
ATOM   3762 N N      . LEU   A  1 488 ? 15.979 -65.185  -18.586 1.00 22.17  ? 480  LEU   A N      1 
ATOM   3763 C CA     . LEU   A  1 488 ? 15.382 -64.114  -17.777 1.00 21.69  ? 480  LEU   A CA     1 
ATOM   3764 C C      . LEU   A  1 488 ? 13.944 -64.429  -17.386 1.00 24.17  ? 480  LEU   A C      1 
ATOM   3765 O O      . LEU   A  1 488 ? 13.545 -64.132  -16.259 1.00 22.50  ? 480  LEU   A O      1 
ATOM   3766 C CB     . LEU   A  1 488 ? 15.484 -62.754  -18.466 1.00 21.38  ? 480  LEU   A CB     1 
ATOM   3767 C CG     . LEU   A  1 488 ? 16.884 -62.135  -18.479 1.00 26.32  ? 480  LEU   A CG     1 
ATOM   3768 C CD1    . LEU   A  1 488 ? 17.008 -61.095  -19.568 1.00 25.98  ? 480  LEU   A CD1    1 
ATOM   3769 C CD2    . LEU   A  1 488 ? 17.252 -61.548  -17.115 1.00 28.53  ? 480  LEU   A CD2    1 
ATOM   3770 N N      . TYR   A  1 489 ? 13.175 -65.053  -18.305 1.00 21.65  ? 481  TYR   A N      1 
ATOM   3771 C CA     . TYR   A  1 489 ? 11.807 -65.472  -18.024 1.00 21.61  ? 481  TYR   A CA     1 
ATOM   3772 C C      . TYR   A  1 489 ? 11.799 -66.394  -16.804 1.00 24.28  ? 481  TYR   A C      1 
ATOM   3773 O O      . TYR   A  1 489 ? 10.941 -66.249  -15.931 1.00 22.53  ? 481  TYR   A O      1 
ATOM   3774 C CB     . TYR   A  1 489 ? 11.147 -66.168  -19.235 1.00 23.02  ? 481  TYR   A CB     1 
ATOM   3775 C CG     . TYR   A  1 489 ? 9.744  -66.649  -18.916 1.00 24.95  ? 481  TYR   A CG     1 
ATOM   3776 C CD1    . TYR   A  1 489 ? 8.690  -65.748  -18.782 1.00 26.21  ? 481  TYR   A CD1    1 
ATOM   3777 C CD2    . TYR   A  1 489 ? 9.481  -67.998  -18.695 1.00 26.31  ? 481  TYR   A CD2    1 
ATOM   3778 C CE1    . TYR   A  1 489 ? 7.407  -66.177  -18.452 1.00 25.95  ? 481  TYR   A CE1    1 
ATOM   3779 C CE2    . TYR   A  1 489 ? 8.197  -68.441  -18.367 1.00 27.89  ? 481  TYR   A CE2    1 
ATOM   3780 C CZ     . TYR   A  1 489 ? 7.165  -67.522  -18.237 1.00 35.63  ? 481  TYR   A CZ     1 
ATOM   3781 O OH     . TYR   A  1 489 ? 5.893  -67.931  -17.917 1.00 38.16  ? 481  TYR   A OH     1 
ATOM   3782 N N      . ASN   A  1 490 ? 12.759 -67.326  -16.742 1.00 21.65  ? 482  ASN   A N      1 
ATOM   3783 C CA     . ASN   A  1 490 ? 12.902 -68.263  -15.624 1.00 22.15  ? 482  ASN   A CA     1 
ATOM   3784 C C      . ASN   A  1 490 ? 13.323 -67.582  -14.320 1.00 24.36  ? 482  ASN   A C      1 
ATOM   3785 O O      . ASN   A  1 490 ? 12.801 -67.920  -13.263 1.00 24.17  ? 482  ASN   A O      1 
ATOM   3786 C CB     . ASN   A  1 490 ? 13.850 -69.403  -15.997 1.00 27.11  ? 482  ASN   A CB     1 
ATOM   3787 C CG     . ASN   A  1 490 ? 13.208 -70.756  -15.886 1.00 46.83  ? 482  ASN   A CG     1 
ATOM   3788 O OD1    . ASN   A  1 490 ? 12.157 -70.921  -15.251 1.00 40.97  ? 482  ASN   A OD1    1 
ATOM   3789 N ND2    . ASN   A  1 490 ? 13.831 -71.761  -16.496 1.00 39.85  ? 482  ASN   A ND2    1 
ATOM   3790 N N      . GLU   A  1 491 ? 14.219 -66.584  -14.403 1.00 21.24  ? 483  GLU   A N      1 
ATOM   3791 C CA     . GLU   A  1 491 ? 14.682 -65.786  -13.256 1.00 21.00  ? 483  GLU   A CA     1 
ATOM   3792 C C      . GLU   A  1 491 ? 13.512 -65.021  -12.613 1.00 21.51  ? 483  GLU   A C      1 
ATOM   3793 O O      . GLU   A  1 491 ? 13.393 -64.999  -11.389 1.00 20.69  ? 483  GLU   A O      1 
ATOM   3794 C CB     . GLU   A  1 491 ? 15.783 -64.798  -13.703 1.00 23.02  ? 483  GLU   A CB     1 
ATOM   3795 C CG     . GLU   A  1 491 ? 17.110 -65.450  -14.069 1.00 36.52  ? 483  GLU   A CG     1 
ATOM   3796 C CD     . GLU   A  1 491 ? 18.029 -65.690  -12.890 1.00 70.77  ? 483  GLU   A CD     1 
ATOM   3797 O OE1    . GLU   A  1 491 ? 18.972 -64.889  -12.704 1.00 83.44  ? 483  GLU   A OE1    1 
ATOM   3798 O OE2    . GLU   A  1 491 ? 17.791 -66.661  -12.136 1.00 68.54  ? 483  GLU   A OE2    1 
ATOM   3799 N N      . VAL   A  1 492 ? 12.632 -64.425  -13.446 1.00 18.03  ? 484  VAL   A N      1 
ATOM   3800 C CA     . VAL   A  1 492 ? 11.446 -63.685  -12.980 1.00 17.69  ? 484  VAL   A CA     1 
ATOM   3801 C C      . VAL   A  1 492 ? 10.461 -64.677  -12.341 1.00 20.73  ? 484  VAL   A C      1 
ATOM   3802 O O      . VAL   A  1 492 ? 9.954  -64.418  -11.258 1.00 20.74  ? 484  VAL   A O      1 
ATOM   3803 C CB     . VAL   A  1 492 ? 10.780 -62.886  -14.136 1.00 20.36  ? 484  VAL   A CB     1 
ATOM   3804 C CG1    . VAL   A  1 492 ? 9.441  -62.306  -13.700 1.00 19.71  ? 484  VAL   A CG1    1 
ATOM   3805 C CG2    . VAL   A  1 492 ? 11.703 -61.779  -14.649 1.00 20.00  ? 484  VAL   A CG2    1 
ATOM   3806 N N      . ARG   A  1 493 ? 10.222 -65.808  -13.011 1.00 18.95  ? 485  ARG   A N      1 
ATOM   3807 C CA     . ARG   A  1 493 ? 9.350  -66.898  -12.548 1.00 21.45  ? 485  ARG   A CA     1 
ATOM   3808 C C      . ARG   A  1 493 ? 9.758  -67.360  -11.131 1.00 28.70  ? 485  ARG   A C      1 
ATOM   3809 O O      . ARG   A  1 493 ? 8.899  -67.509  -10.266 1.00 28.76  ? 485  ARG   A O      1 
ATOM   3810 C CB     . ARG   A  1 493 ? 9.445  -68.067  -13.528 1.00 21.45  ? 485  ARG   A CB     1 
ATOM   3811 C CG     . ARG   A  1 493 ? 8.114  -68.658  -13.919 1.00 38.29  ? 485  ARG   A CG     1 
ATOM   3812 C CD     . ARG   A  1 493 ? 8.282  -69.697  -15.011 1.00 48.20  ? 485  ARG   A CD     1 
ATOM   3813 N NE     . ARG   A  1 493 ? 9.081  -70.831  -14.553 1.00 53.85  ? 485  ARG   A NE     1 
ATOM   3814 C CZ     . ARG   A  1 493 ? 8.646  -72.082  -14.491 1.00 60.84  ? 485  ARG   A CZ     1 
ATOM   3815 N NH1    . ARG   A  1 493 ? 7.419  -72.387  -14.899 1.00 39.84  ? 485  ARG   A NH1    1 
ATOM   3816 N NH2    . ARG   A  1 493 ? 9.440  -73.043  -14.040 1.00 46.87  ? 485  ARG   A NH2    1 
ATOM   3817 N N      . ALA   A  1 494 ? 11.077 -67.482  -10.880 1.00 27.27  ? 486  ALA   A N      1 
ATOM   3818 C CA     . ALA   A  1 494 ? 11.638 -67.872  -9.583  1.00 27.31  ? 486  ALA   A CA     1 
ATOM   3819 C C      . ALA   A  1 494 ? 11.440 -66.801  -8.482  1.00 31.01  ? 486  ALA   A C      1 
ATOM   3820 O O      . ALA   A  1 494 ? 11.663 -67.100  -7.311  1.00 30.75  ? 486  ALA   A O      1 
ATOM   3821 C CB     . ALA   A  1 494 ? 13.115 -68.224  -9.733  1.00 27.75  ? 486  ALA   A CB     1 
ATOM   3822 N N      . CYS   A  1 495 ? 10.983 -65.575  -8.841  1.00 27.24  ? 487  CYS   A N      1 
ATOM   3823 C CA     . CYS   A  1 495 ? 10.738 -64.503  -7.870  1.00 26.58  ? 487  CYS   A CA     1 
ATOM   3824 C C      . CYS   A  1 495 ? 9.372  -64.618  -7.164  1.00 29.00  ? 487  CYS   A C      1 
ATOM   3825 O O      . CYS   A  1 495 ? 9.007  -63.707  -6.423  1.00 27.17  ? 487  CYS   A O      1 
ATOM   3826 C CB     . CYS   A  1 495 ? 10.938 -63.123  -8.491  1.00 27.14  ? 487  CYS   A CB     1 
ATOM   3827 S SG     . CYS   A  1 495 ? 12.652 -62.747  -8.915  1.00 31.21  ? 487  CYS   A SG     1 
ATOM   3828 N N      . ARG   A  1 496 ? 8.636  -65.738  -7.351  1.00 27.30  ? 488  ARG   A N      1 
ATOM   3829 C CA     . ARG   A  1 496 ? 7.361  -65.949  -6.657  1.00 28.31  ? 488  ARG   A CA     1 
ATOM   3830 C C      . ARG   A  1 496 ? 7.616  -65.978  -5.143  1.00 34.20  ? 488  ARG   A C      1 
ATOM   3831 O O      . ARG   A  1 496 ? 8.507  -66.686  -4.676  1.00 34.29  ? 488  ARG   A O      1 
ATOM   3832 C CB     . ARG   A  1 496 ? 6.647  -67.227  -7.132  1.00 28.10  ? 488  ARG   A CB     1 
ATOM   3833 C CG     . ARG   A  1 496 ? 5.275  -67.464  -6.465  1.00 28.92  ? 488  ARG   A CG     1 
ATOM   3834 C CD     . ARG   A  1 496 ? 4.429  -68.486  -7.210  1.00 33.85  ? 488  ARG   A CD     1 
ATOM   3835 N NE     . ARG   A  1 496 ? 4.969  -69.851  -7.129  1.00 38.04  ? 488  ARG   A NE     1 
ATOM   3836 C CZ     . ARG   A  1 496 ? 4.603  -70.758  -6.226  1.00 46.78  ? 488  ARG   A CZ     1 
ATOM   3837 N NH1    . ARG   A  1 496 ? 3.710  -70.454  -5.295  1.00 30.21  ? 488  ARG   A NH1    1 
ATOM   3838 N NH2    . ARG   A  1 496 ? 5.139  -71.971  -6.240  1.00 35.56  ? 488  ARG   A NH2    1 
ATOM   3839 N N      . GLU   A  1 497 ? 6.891  -65.139  -4.404  1.00 30.99  ? 489  GLU   A N      1 
ATOM   3840 C CA     . GLU   A  1 497 ? 7.038  -65.031  -2.960  1.00 31.21  ? 489  GLU   A CA     1 
ATOM   3841 C C      . GLU   A  1 497 ? 5.753  -65.427  -2.266  1.00 34.21  ? 489  GLU   A C      1 
ATOM   3842 O O      . GLU   A  1 497 ? 4.673  -65.259  -2.828  1.00 33.09  ? 489  GLU   A O      1 
ATOM   3843 C CB     . GLU   A  1 497 ? 7.376  -63.586  -2.570  1.00 32.94  ? 489  GLU   A CB     1 
ATOM   3844 C CG     . GLU   A  1 497 ? 8.782  -63.138  -2.934  1.00 46.86  ? 489  GLU   A CG     1 
ATOM   3845 C CD     . GLU   A  1 497 ? 9.026  -61.643  -2.838  1.00 73.64  ? 489  GLU   A CD     1 
ATOM   3846 O OE1    . GLU   A  1 497 ? 8.299  -60.960  -2.079  1.00 57.86  ? 489  GLU   A OE1    1 
ATOM   3847 O OE2    . GLU   A  1 497 ? 9.954  -61.154  -3.522  1.00 78.71  ? 489  GLU   A OE2    1 
ATOM   3848 N N      . LYS   A  1 498 ? 5.868  -65.905  -1.025  1.00 30.95  ? 490  LYS   A N      1 
ATOM   3849 C CA     . LYS   A  1 498 ? 4.724  -66.225  -0.174  1.00 30.99  ? 490  LYS   A CA     1 
ATOM   3850 C C      . LYS   A  1 498 ? 4.105  -64.892  0.292   1.00 34.04  ? 490  LYS   A C      1 
ATOM   3851 O O      . LYS   A  1 498 ? 4.787  -63.867  0.260   1.00 33.86  ? 490  LYS   A O      1 
ATOM   3852 C CB     . LYS   A  1 498 ? 5.161  -67.092  1.039   1.00 33.62  ? 490  LYS   A CB     1 
ATOM   3853 C CG     . LYS   A  1 498 ? 6.148  -66.436  2.008   1.00 44.98  ? 490  LYS   A CG     1 
ATOM   3854 C CD     . LYS   A  1 498 ? 6.523  -67.358  3.181   1.00 54.49  ? 490  LYS   A CD     1 
ATOM   3855 C CE     . LYS   A  1 498 ? 7.707  -68.258  2.903   1.00 65.95  ? 490  LYS   A CE     1 
ATOM   3856 N NZ     . LYS   A  1 498 ? 9.002  -67.528  2.967   1.00 74.36  ? 490  LYS   A NZ     1 
ATOM   3857 N N      . ASP   A  1 499 ? 2.821  -64.910  0.713   1.00 30.05  ? 491  ASP   A N      1 
ATOM   3858 C CA     . ASP   A  1 499 ? 2.083  -63.751  1.248   1.00 29.42  ? 491  ASP   A CA     1 
ATOM   3859 C C      . ASP   A  1 499 ? 1.817  -62.633  0.202   1.00 31.65  ? 491  ASP   A C      1 
ATOM   3860 O O      . ASP   A  1 499 ? 1.683  -61.460  0.563   1.00 30.85  ? 491  ASP   A O      1 
ATOM   3861 C CB     . ASP   A  1 499 ? 2.771  -63.180  2.524   1.00 31.13  ? 491  ASP   A CB     1 
ATOM   3862 C CG     . ASP   A  1 499 ? 3.221  -64.214  3.555   1.00 38.78  ? 491  ASP   A CG     1 
ATOM   3863 O OD1    . ASP   A  1 499 ? 2.667  -65.334  3.558   1.00 36.62  ? 491  ASP   A OD1    1 
ATOM   3864 O OD2    . ASP   A  1 499 ? 4.124  -63.894  4.360   1.00 47.75  ? 491  ASP   A OD2    1 
ATOM   3865 N N      . ARG   A  1 500 ? 1.724  -63.010  -1.084  1.00 26.91  ? 492  ARG   A N      1 
ATOM   3866 C CA     . ARG   A  1 500 ? 1.417  -62.095  -2.191  1.00 25.79  ? 492  ARG   A CA     1 
ATOM   3867 C C      . ARG   A  1 500 ? 0.871  -62.874  -3.394  1.00 26.51  ? 492  ARG   A C      1 
ATOM   3868 O O      . ARG   A  1 500 ? 0.986  -64.099  -3.413  1.00 24.52  ? 492  ARG   A O      1 
ATOM   3869 C CB     . ARG   A  1 500 ? 2.615  -61.181  -2.555  1.00 24.65  ? 492  ARG   A CB     1 
ATOM   3870 C CG     . ARG   A  1 500 ? 3.697  -61.822  -3.423  1.00 25.65  ? 492  ARG   A CG     1 
ATOM   3871 C CD     . ARG   A  1 500 ? 4.577  -60.759  -4.061  1.00 21.48  ? 492  ARG   A CD     1 
ATOM   3872 N NE     . ARG   A  1 500 ? 5.605  -61.329  -4.935  1.00 23.00  ? 492  ARG   A NE     1 
ATOM   3873 C CZ     . ARG   A  1 500 ? 6.712  -60.692  -5.303  1.00 35.07  ? 492  ARG   A CZ     1 
ATOM   3874 N NH1    . ARG   A  1 500 ? 6.960  -59.465  -4.862  1.00 26.55  ? 492  ARG   A NH1    1 
ATOM   3875 N NH2    . ARG   A  1 500 ? 7.588  -61.284  -6.100  1.00 20.95  ? 492  ARG   A NH2    1 
ATOM   3876 N N      . ASP   A  1 501 ? 0.253  -62.173  -4.376  1.00 23.25  ? 493  ASP   A N      1 
ATOM   3877 C CA     . ASP   A  1 501 ? -0.297 -62.765  -5.604  1.00 22.97  ? 493  ASP   A CA     1 
ATOM   3878 C C      . ASP   A  1 501 ? 0.769  -63.643  -6.262  1.00 25.20  ? 493  ASP   A C      1 
ATOM   3879 O O      . ASP   A  1 501 ? 1.908  -63.193  -6.412  1.00 23.80  ? 493  ASP   A O      1 
ATOM   3880 C CB     . ASP   A  1 501 ? -0.770 -61.674  -6.606  1.00 25.12  ? 493  ASP   A CB     1 
ATOM   3881 C CG     . ASP   A  1 501 ? -1.514 -62.193  -7.834  1.00 39.74  ? 493  ASP   A CG     1 
ATOM   3882 O OD1    . ASP   A  1 501 ? -0.913 -62.971  -8.617  1.00 38.37  ? 493  ASP   A OD1    1 
ATOM   3883 O OD2    . ASP   A  1 501 ? -2.667 -61.762  -8.055  1.00 51.49  ? 493  ASP   A OD2    1 
ATOM   3884 N N      . PRO   A  1 502 ? 0.402  -64.887  -6.670  1.00 21.56  ? 494  PRO   A N      1 
ATOM   3885 C CA     . PRO   A  1 502 ? 1.398  -65.799  -7.284  1.00 21.47  ? 494  PRO   A CA     1 
ATOM   3886 C C      . PRO   A  1 502 ? 2.027  -65.362  -8.612  1.00 24.70  ? 494  PRO   A C      1 
ATOM   3887 O O      . PRO   A  1 502 ? 3.008  -65.971  -9.038  1.00 24.23  ? 494  PRO   A O      1 
ATOM   3888 C CB     . PRO   A  1 502 ? 0.633  -67.109  -7.444  1.00 23.17  ? 494  PRO   A CB     1 
ATOM   3889 C CG     . PRO   A  1 502 ? -0.803 -66.743  -7.389  1.00 27.12  ? 494  PRO   A CG     1 
ATOM   3890 C CD     . PRO   A  1 502 ? -0.914 -65.544  -6.514  1.00 21.84  ? 494  PRO   A CD     1 
ATOM   3891 N N      . GLU   A  1 503 ? 1.489  -64.317  -9.260  1.00 21.62  ? 495  GLU   A N      1 
ATOM   3892 C CA     . GLU   A  1 503 ? 2.018  -63.794  -10.523 1.00 21.21  ? 495  GLU   A CA     1 
ATOM   3893 C C      . GLU   A  1 503 ? 2.484  -62.325  -10.413 1.00 23.30  ? 495  GLU   A C      1 
ATOM   3894 O O      . GLU   A  1 503 ? 2.799  -61.713  -11.443 1.00 22.34  ? 495  GLU   A O      1 
ATOM   3895 C CB     . GLU   A  1 503 ? 0.984  -63.943  -11.651 1.00 22.75  ? 495  GLU   A CB     1 
ATOM   3896 C CG     . GLU   A  1 503 ? 0.708  -65.391  -12.042 1.00 35.15  ? 495  GLU   A CG     1 
ATOM   3897 C CD     . GLU   A  1 503 ? -0.328 -65.581  -13.135 1.00 67.33  ? 495  GLU   A CD     1 
ATOM   3898 O OE1    . GLU   A  1 503 ? -1.347 -64.850  -13.140 1.00 59.83  ? 495  GLU   A OE1    1 
ATOM   3899 O OE2    . GLU   A  1 503 ? -0.125 -66.481  -13.982 1.00 71.72  ? 495  GLU   A OE2    1 
ATOM   3900 N N      . ALA   A  1 504 ? 2.537  -61.767  -9.176  1.00 18.35  ? 496  ALA   A N      1 
ATOM   3901 C CA     . ALA   A  1 504 ? 2.963  -60.371  -8.948  1.00 17.74  ? 496  ALA   A CA     1 
ATOM   3902 C C      . ALA   A  1 504 ? 4.347  -60.064  -9.513  1.00 20.34  ? 496  ALA   A C      1 
ATOM   3903 O O      . ALA   A  1 504 ? 4.544  -58.974  -10.044 1.00 20.13  ? 496  ALA   A O      1 
ATOM   3904 C CB     . ALA   A  1 504 ? 2.894  -60.011  -7.473  1.00 18.39  ? 496  ALA   A CB     1 
ATOM   3905 N N      . GLN   A  1 505 ? 5.280  -61.045  -9.461  1.00 16.40  ? 497  GLN   A N      1 
ATOM   3906 C CA     . GLN   A  1 505 ? 6.655  -60.935  -9.972  1.00 16.01  ? 497  GLN   A CA     1 
ATOM   3907 C C      . GLN   A  1 505 ? 6.741  -60.603  -11.472 1.00 19.43  ? 497  GLN   A C      1 
ATOM   3908 O O      . GLN   A  1 505 ? 7.741  -60.042  -11.894 1.00 19.33  ? 497  GLN   A O      1 
ATOM   3909 C CB     . GLN   A  1 505 ? 7.504  -62.184  -9.625  1.00 17.08  ? 497  GLN   A CB     1 
ATOM   3910 C CG     . GLN   A  1 505 ? 7.093  -63.500  -10.315 1.00 19.57  ? 497  GLN   A CG     1 
ATOM   3911 C CD     . GLN   A  1 505 ? 5.955  -64.231  -9.628  1.00 21.09  ? 497  GLN   A CD     1 
ATOM   3912 O OE1    . GLN   A  1 505 ? 5.263  -63.703  -8.754  1.00 18.61  ? 497  GLN   A OE1    1 
ATOM   3913 N NE2    . GLN   A  1 505 ? 5.689  -65.446  -10.061 1.00 17.55  ? 497  GLN   A NE2    1 
ATOM   3914 N N      . PHE   A  1 506 ? 5.713  -60.932  -12.273 1.00 16.88  ? 498  PHE   A N      1 
ATOM   3915 C CA     . PHE   A  1 506 ? 5.694  -60.619  -13.701 1.00 15.99  ? 498  PHE   A CA     1 
ATOM   3916 C C      . PHE   A  1 506 ? 5.153  -59.220  -13.977 1.00 20.96  ? 498  PHE   A C      1 
ATOM   3917 O O      . PHE   A  1 506 ? 5.273  -58.743  -15.103 1.00 21.30  ? 498  PHE   A O      1 
ATOM   3918 C CB     . PHE   A  1 506 ? 4.840  -61.631  -14.487 1.00 17.54  ? 498  PHE   A CB     1 
ATOM   3919 C CG     . PHE   A  1 506 ? 5.367  -63.039  -14.511 1.00 18.57  ? 498  PHE   A CG     1 
ATOM   3920 C CD1    . PHE   A  1 506 ? 6.435  -63.384  -15.329 1.00 20.38  ? 498  PHE   A CD1    1 
ATOM   3921 C CD2    . PHE   A  1 506 ? 4.782  -64.031  -13.729 1.00 21.37  ? 498  PHE   A CD2    1 
ATOM   3922 C CE1    . PHE   A  1 506 ? 6.920  -64.694  -15.353 1.00 21.36  ? 498  PHE   A CE1    1 
ATOM   3923 C CE2    . PHE   A  1 506 ? 5.274  -65.338  -13.744 1.00 23.52  ? 498  PHE   A CE2    1 
ATOM   3924 C CZ     . PHE   A  1 506 ? 6.319  -65.664  -14.580 1.00 21.65  ? 498  PHE   A CZ     1 
ATOM   3925 N N      . GLU   A  1 507 ? 4.544  -58.581  -12.966 1.00 18.51  ? 499  GLU   A N      1 
ATOM   3926 C CA     . GLU   A  1 507 ? 3.891  -57.272  -13.077 1.00 18.10  ? 499  GLU   A CA     1 
ATOM   3927 C C      . GLU   A  1 507 ? 4.727  -56.149  -12.452 1.00 21.59  ? 499  GLU   A C      1 
ATOM   3928 O O      . GLU   A  1 507 ? 4.187  -55.158  -11.957 1.00 21.56  ? 499  GLU   A O      1 
ATOM   3929 C CB     . GLU   A  1 507 ? 2.509  -57.325  -12.410 1.00 19.03  ? 499  GLU   A CB     1 
ATOM   3930 C CG     . GLU   A  1 507 ? 1.531  -58.335  -12.980 1.00 21.37  ? 499  GLU   A CG     1 
ATOM   3931 C CD     . GLU   A  1 507 ? 0.092  -58.027  -12.620 1.00 29.87  ? 499  GLU   A CD     1 
ATOM   3932 O OE1    . GLU   A  1 507 ? -0.198 -57.845  -11.416 1.00 24.99  ? 499  GLU   A OE1    1 
ATOM   3933 O OE2    . GLU   A  1 507 ? -0.730 -57.876  -13.551 1.00 31.09  ? 499  GLU   A OE2    1 
ATOM   3934 N N      . MET   A  1 508 ? 6.043  -56.308  -12.465 1.00 17.45  ? 500  MET   A N      1 
ATOM   3935 C CA     . MET   A  1 508 ? 6.926  -55.301  -11.903 1.00 17.18  ? 500  MET   A CA     1 
ATOM   3936 C C      . MET   A  1 508 ? 8.208  -55.233  -12.694 1.00 19.33  ? 500  MET   A C      1 
ATOM   3937 O O      . MET   A  1 508 ? 8.680  -56.268  -13.150 1.00 18.53  ? 500  MET   A O      1 
ATOM   3938 C CB     . MET   A  1 508 ? 7.192  -55.529  -10.394 1.00 19.95  ? 500  MET   A CB     1 
ATOM   3939 C CG     . MET   A  1 508 ? 7.835  -56.869  -10.061 1.00 24.13  ? 500  MET   A CG     1 
ATOM   3940 S SD     . MET   A  1 508 ? 8.154  -57.056  -8.298  1.00 28.81  ? 500  MET   A SD     1 
ATOM   3941 C CE     . MET   A  1 508 ? 6.483  -57.273  -7.672  1.00 25.60  ? 500  MET   A CE     1 
ATOM   3942 N N      . PRO   A  1 509 ? 8.795  -54.040  -12.877 1.00 16.21  ? 501  PRO   A N      1 
ATOM   3943 C CA     . PRO   A  1 509 ? 10.063 -53.973  -13.609 1.00 15.63  ? 501  PRO   A CA     1 
ATOM   3944 C C      . PRO   A  1 509 ? 11.255 -54.351  -12.722 1.00 19.32  ? 501  PRO   A C      1 
ATOM   3945 O O      . PRO   A  1 509 ? 11.185 -54.256  -11.497 1.00 19.93  ? 501  PRO   A O      1 
ATOM   3946 C CB     . PRO   A  1 509 ? 10.111 -52.512  -14.065 1.00 17.38  ? 501  PRO   A CB     1 
ATOM   3947 C CG     . PRO   A  1 509 ? 9.415  -51.762  -12.959 1.00 22.02  ? 501  PRO   A CG     1 
ATOM   3948 C CD     . PRO   A  1 509 ? 8.358  -52.696  -12.421 1.00 17.74  ? 501  PRO   A CD     1 
ATOM   3949 N N      . TYR   A  1 510 ? 12.354 -54.757  -13.346 1.00 15.95  ? 502  TYR   A N      1 
ATOM   3950 C CA     . TYR   A  1 510 ? 13.590 -55.118  -12.650 1.00 14.96  ? 502  TYR   A CA     1 
ATOM   3951 C C      . TYR   A  1 510 ? 14.748 -54.370  -13.289 1.00 18.77  ? 502  TYR   A C      1 
ATOM   3952 O O      . TYR   A  1 510 ? 14.819 -54.289  -14.503 1.00 18.96  ? 502  TYR   A O      1 
ATOM   3953 C CB     . TYR   A  1 510 ? 13.870 -56.639  -12.776 1.00 14.91  ? 502  TYR   A CB     1 
ATOM   3954 C CG     . TYR   A  1 510 ? 12.817 -57.495  -12.116 1.00 16.12  ? 502  TYR   A CG     1 
ATOM   3955 C CD1    . TYR   A  1 510 ? 11.721 -57.965  -12.836 1.00 16.75  ? 502  TYR   A CD1    1 
ATOM   3956 C CD2    . TYR   A  1 510 ? 12.893 -57.806  -10.761 1.00 16.83  ? 502  TYR   A CD2    1 
ATOM   3957 C CE1    . TYR   A  1 510 ? 10.737 -58.737  -12.228 1.00 15.81  ? 502  TYR   A CE1    1 
ATOM   3958 C CE2    . TYR   A  1 510 ? 11.898 -58.559  -10.135 1.00 17.41  ? 502  TYR   A CE2    1 
ATOM   3959 C CZ     . TYR   A  1 510 ? 10.830 -59.033  -10.878 1.00 22.18  ? 502  TYR   A CZ     1 
ATOM   3960 O OH     . TYR   A  1 510 ? 9.862  -59.793  -10.278 1.00 19.68  ? 502  TYR   A OH     1 
ATOM   3961 N N      . VAL   A  1 511 ? 15.686 -53.900  -12.484 1.00 17.32  ? 503  VAL   A N      1 
ATOM   3962 C CA     . VAL   A  1 511 ? 16.918 -53.283  -12.995 1.00 16.68  ? 503  VAL   A CA     1 
ATOM   3963 C C      . VAL   A  1 511 ? 17.833 -54.495  -13.184 1.00 18.60  ? 503  VAL   A C      1 
ATOM   3964 O O      . VAL   A  1 511 ? 17.998 -55.283  -12.264 1.00 17.33  ? 503  VAL   A O      1 
ATOM   3965 C CB     . VAL   A  1 511 ? 17.511 -52.249  -12.005 1.00 20.00  ? 503  VAL   A CB     1 
ATOM   3966 C CG1    . VAL   A  1 511 ? 18.904 -51.798  -12.444 1.00 20.28  ? 503  VAL   A CG1    1 
ATOM   3967 C CG2    . VAL   A  1 511 ? 16.586 -51.052  -11.843 1.00 19.69  ? 503  VAL   A CG2    1 
ATOM   3968 N N      . VAL   A  1 512 ? 18.371 -54.679  -14.383 1.00 16.78  ? 504  VAL   A N      1 
ATOM   3969 C CA     . VAL   A  1 512 ? 19.180 -55.854  -14.683 1.00 17.02  ? 504  VAL   A CA     1 
ATOM   3970 C C      . VAL   A  1 512 ? 20.169 -55.571  -15.793 1.00 22.17  ? 504  VAL   A C      1 
ATOM   3971 O O      . VAL   A  1 512 ? 19.813 -54.964  -16.799 1.00 22.17  ? 504  VAL   A O      1 
ATOM   3972 C CB     . VAL   A  1 512 ? 18.249 -57.076  -15.013 1.00 20.06  ? 504  VAL   A CB     1 
ATOM   3973 C CG1    . VAL   A  1 512 ? 17.146 -56.698  -16.003 1.00 19.28  ? 504  VAL   A CG1    1 
ATOM   3974 C CG2    . VAL   A  1 512 ? 19.031 -58.297  -15.494 1.00 19.36  ? 504  VAL   A CG2    1 
ATOM   3975 N N      . ARG   A  1 513 ? 21.404 -56.036  -15.623 1.00 21.00  ? 505  ARG   A N      1 
ATOM   3976 C CA     . ARG   A  1 513 ? 22.398 -55.931  -16.672 1.00 21.42  ? 505  ARG   A CA     1 
ATOM   3977 C C      . ARG   A  1 513 ? 22.076 -57.116  -17.610 1.00 24.78  ? 505  ARG   A C      1 
ATOM   3978 O O      . ARG   A  1 513 ? 22.537 -58.234  -17.385 1.00 23.55  ? 505  ARG   A O      1 
ATOM   3979 C CB     . ARG   A  1 513 ? 23.850 -55.944  -16.102 1.00 21.26  ? 505  ARG   A CB     1 
ATOM   3980 C CG     . ARG   A  1 513 ? 25.007 -56.156  -17.135 1.00 27.22  ? 505  ARG   A CG     1 
ATOM   3981 C CD     . ARG   A  1 513 ? 25.091 -55.118  -18.250 1.00 35.43  ? 505  ARG   A CD     1 
ATOM   3982 N NE     . ARG   A  1 513 ? 24.249 -55.463  -19.407 1.00 39.97  ? 505  ARG   A NE     1 
ATOM   3983 C CZ     . ARG   A  1 513 ? 23.633 -54.576  -20.187 1.00 47.44  ? 505  ARG   A CZ     1 
ATOM   3984 N NH1    . ARG   A  1 513 ? 23.768 -53.278  -19.963 1.00 34.52  ? 505  ARG   A NH1    1 
ATOM   3985 N NH2    . ARG   A  1 513 ? 22.887 -54.984  -21.206 1.00 32.87  ? 505  ARG   A NH2    1 
ATOM   3986 N N      . LEU   A  1 514 ? 21.193 -56.867  -18.607 1.00 22.30  ? 506  LEU   A N      1 
ATOM   3987 C CA     . LEU   A  1 514 ? 20.751 -57.863  -19.593 1.00 21.84  ? 506  LEU   A CA     1 
ATOM   3988 C C      . LEU   A  1 514 ? 21.960 -58.424  -20.327 1.00 27.42  ? 506  LEU   A C      1 
ATOM   3989 O O      . LEU   A  1 514 ? 22.826 -57.669  -20.766 1.00 26.08  ? 506  LEU   A O      1 
ATOM   3990 C CB     . LEU   A  1 514 ? 19.755 -57.257  -20.589 1.00 21.11  ? 506  LEU   A CB     1 
ATOM   3991 C CG     . LEU   A  1 514 ? 18.511 -56.575  -20.020 1.00 24.77  ? 506  LEU   A CG     1 
ATOM   3992 C CD1    . LEU   A  1 514 ? 17.901 -55.682  -21.051 1.00 24.74  ? 506  LEU   A CD1    1 
ATOM   3993 C CD2    . LEU   A  1 514 ? 17.474 -57.586  -19.554 1.00 25.13  ? 506  LEU   A CD2    1 
ATOM   3994 N N      . HIS   A  1 515 ? 22.066 -59.741  -20.387 1.00 25.57  ? 507  HIS   A N      1 
ATOM   3995 C CA     . HIS   A  1 515 ? 23.239 -60.370  -20.986 1.00 26.20  ? 507  HIS   A CA     1 
ATOM   3996 C C      . HIS   A  1 515 ? 22.867 -61.500  -21.960 1.00 31.82  ? 507  HIS   A C      1 
ATOM   3997 O O      . HIS   A  1 515 ? 23.196 -61.429  -23.149 1.00 31.65  ? 507  HIS   A O      1 
ATOM   3998 C CB     . HIS   A  1 515 ? 24.158 -60.856  -19.852 1.00 27.00  ? 507  HIS   A CB     1 
ATOM   3999 C CG     . HIS   A  1 515 ? 25.401 -61.533  -20.320 1.00 30.81  ? 507  HIS   A CG     1 
ATOM   4000 N ND1    . HIS   A  1 515 ? 26.428 -60.823  -20.910 1.00 32.82  ? 507  HIS   A ND1    1 
ATOM   4001 C CD2    . HIS   A  1 515 ? 25.748 -62.838  -20.258 1.00 32.46  ? 507  HIS   A CD2    1 
ATOM   4002 C CE1    . HIS   A  1 515 ? 27.364 -61.716  -21.185 1.00 32.31  ? 507  HIS   A CE1    1 
ATOM   4003 N NE2    . HIS   A  1 515 ? 26.997 -62.941  -20.818 1.00 32.40  ? 507  HIS   A NE2    1 
ATOM   4004 N N      . ASN   A  1 516 ? 22.169 -62.523  -21.467 1.00 28.25  ? 508  ASN   A N      1 
ATOM   4005 C CA     . ASN   A  1 516 ? 21.746 -63.626  -22.323 1.00 27.48  ? 508  ASN   A CA     1 
ATOM   4006 C C      . ASN   A  1 516 ? 20.324 -63.383  -22.816 1.00 29.25  ? 508  ASN   A C      1 
ATOM   4007 O O      . ASN   A  1 516 ? 19.339 -63.844  -22.229 1.00 29.67  ? 508  ASN   A O      1 
ATOM   4008 C CB     . ASN   A  1 516 ? 21.902 -64.968  -21.621 1.00 24.27  ? 508  ASN   A CB     1 
ATOM   4009 C CG     . ASN   A  1 516 ? 21.704 -66.156  -22.532 1.00 35.78  ? 508  ASN   A CG     1 
ATOM   4010 O OD1    . ASN   A  1 516 ? 21.475 -67.258  -22.066 1.00 29.05  ? 508  ASN   A OD1    1 
ATOM   4011 N ND2    . ASN   A  1 516 ? 21.792 -65.971  -23.845 1.00 29.19  ? 508  ASN   A ND2    1 
ATOM   4012 N N      . PHE   A  1 517 ? 20.241 -62.633  -23.901 1.00 24.91  ? 509  PHE   A N      1 
ATOM   4013 C CA     . PHE   A  1 517 ? 18.987 -62.231  -24.515 1.00 23.64  ? 509  PHE   A CA     1 
ATOM   4014 C C      . PHE   A  1 517 ? 19.174 -61.924  -25.982 1.00 27.21  ? 509  PHE   A C      1 
ATOM   4015 O O      . PHE   A  1 517 ? 20.294 -61.809  -26.469 1.00 27.79  ? 509  PHE   A O      1 
ATOM   4016 C CB     . PHE   A  1 517 ? 18.396 -60.998  -23.759 1.00 24.31  ? 509  PHE   A CB     1 
ATOM   4017 C CG     . PHE   A  1 517 ? 19.045 -59.675  -24.093 1.00 25.15  ? 509  PHE   A CG     1 
ATOM   4018 C CD1    . PHE   A  1 517 ? 20.320 -59.367  -23.625 1.00 26.85  ? 509  PHE   A CD1    1 
ATOM   4019 C CD2    . PHE   A  1 517 ? 18.383 -58.734  -24.874 1.00 26.39  ? 509  PHE   A CD2    1 
ATOM   4020 C CE1    . PHE   A  1 517 ? 20.926 -58.143  -23.945 1.00 26.80  ? 509  PHE   A CE1    1 
ATOM   4021 C CE2    . PHE   A  1 517 ? 18.976 -57.496  -25.166 1.00 29.07  ? 509  PHE   A CE2    1 
ATOM   4022 C CZ     . PHE   A  1 517 ? 20.250 -57.215  -24.711 1.00 26.69  ? 509  PHE   A CZ     1 
ATOM   4023 N N      . HIS   A  1 518 ? 18.052 -61.718  -26.662 1.00 22.89  ? 510  HIS   A N      1 
ATOM   4024 C CA     . HIS   A  1 518 ? 17.963 -61.356  -28.042 1.00 21.80  ? 510  HIS   A CA     1 
ATOM   4025 C C      . HIS   A  1 518 ? 17.040 -60.158  -28.136 1.00 26.81  ? 510  HIS   A C      1 
ATOM   4026 O O      . HIS   A  1 518 ? 15.871 -60.272  -27.782 1.00 27.59  ? 510  HIS   A O      1 
ATOM   4027 C CB     . HIS   A  1 518 ? 17.391 -62.546  -28.854 1.00 21.95  ? 510  HIS   A CB     1 
ATOM   4028 C CG     . HIS   A  1 518 ? 17.492 -62.377  -30.336 1.00 24.79  ? 510  HIS   A CG     1 
ATOM   4029 N ND1    . HIS   A  1 518 ? 16.828 -63.223  -31.199 1.00 26.17  ? 510  HIS   A ND1    1 
ATOM   4030 C CD2    . HIS   A  1 518 ? 18.185 -61.465  -31.064 1.00 26.78  ? 510  HIS   A CD2    1 
ATOM   4031 C CE1    . HIS   A  1 518 ? 17.120 -62.797  -32.415 1.00 26.03  ? 510  HIS   A CE1    1 
ATOM   4032 N NE2    . HIS   A  1 518 ? 17.936 -61.739  -32.383 1.00 26.41  ? 510  HIS   A NE2    1 
ATOM   4033 N N      . GLN   A  1 519 ? 17.564 -59.007  -28.577 1.00 24.61  ? 511  GLN   A N      1 
ATOM   4034 C CA     . GLN   A  1 519 ? 16.786 -57.799  -28.845 1.00 25.50  ? 511  GLN   A CA     1 
ATOM   4035 C C      . GLN   A  1 519 ? 16.110 -58.080  -30.201 1.00 30.47  ? 511  GLN   A C      1 
ATOM   4036 O O      . GLN   A  1 519 ? 16.795 -58.411  -31.179 1.00 29.69  ? 511  GLN   A O      1 
ATOM   4037 C CB     . GLN   A  1 519 ? 17.703 -56.577  -28.918 1.00 27.51  ? 511  GLN   A CB     1 
ATOM   4038 C CG     . GLN   A  1 519 ? 16.957 -55.245  -28.889 1.00 37.17  ? 511  GLN   A CG     1 
ATOM   4039 C CD     . GLN   A  1 519 ? 17.803 -54.155  -28.284 1.00 48.16  ? 511  GLN   A CD     1 
ATOM   4040 O OE1    . GLN   A  1 519 ? 18.052 -54.108  -27.061 1.00 41.25  ? 511  GLN   A OE1    1 
ATOM   4041 N NE2    . GLN   A  1 519 ? 18.258 -53.254  -29.126 1.00 29.12  ? 511  GLN   A NE2    1 
ATOM   4042 N N      . LEU   A  1 520 ? 14.764 -58.037  -30.233 1.00 26.43  ? 512  LEU   A N      1 
ATOM   4043 C CA     . LEU   A  1 520 ? 13.962 -58.451  -31.390 1.00 24.88  ? 512  LEU   A CA     1 
ATOM   4044 C C      . LEU   A  1 520 ? 13.610 -57.359  -32.390 1.00 28.29  ? 512  LEU   A C      1 
ATOM   4045 O O      . LEU   A  1 520 ? 13.154 -57.666  -33.492 1.00 27.63  ? 512  LEU   A O      1 
ATOM   4046 C CB     . LEU   A  1 520 ? 12.682 -59.148  -30.901 1.00 24.54  ? 512  LEU   A CB     1 
ATOM   4047 C CG     . LEU   A  1 520 ? 12.863 -60.291  -29.906 1.00 28.46  ? 512  LEU   A CG     1 
ATOM   4048 C CD1    . LEU   A  1 520 ? 11.535 -60.802  -29.422 1.00 27.32  ? 512  LEU   A CD1    1 
ATOM   4049 C CD2    . LEU   A  1 520 ? 13.721 -61.418  -30.498 1.00 32.73  ? 512  LEU   A CD2    1 
ATOM   4050 N N      . SER   A  1 521 ? 13.800 -56.096  -32.007 1.00 24.72  ? 513  SER   A N      1 
ATOM   4051 C CA     . SER   A  1 521 ? 13.524 -54.924  -32.829 1.00 24.16  ? 513  SER   A CA     1 
ATOM   4052 C C      . SER   A  1 521 ? 14.267 -53.747  -32.201 1.00 29.76  ? 513  SER   A C      1 
ATOM   4053 O O      . SER   A  1 521 ? 14.479 -53.737  -30.984 1.00 30.51  ? 513  SER   A O      1 
ATOM   4054 C CB     . SER   A  1 521 ? 12.019 -54.651  -32.891 1.00 25.31  ? 513  SER   A CB     1 
ATOM   4055 O OG     . SER   A  1 521 ? 11.680 -53.695  -33.884 1.00 30.01  ? 513  SER   A OG     1 
ATOM   4056 N N      . ALA   A  1 522 ? 14.672 -52.774  -33.027 1.00 27.19  ? 514  ALA   A N      1 
ATOM   4057 C CA     . ALA   A  1 522 ? 15.404 -51.581  -32.606 1.00 27.17  ? 514  ALA   A CA     1 
ATOM   4058 C C      . ALA   A  1 522 ? 14.631 -50.779  -31.531 1.00 30.52  ? 514  ALA   A C      1 
ATOM   4059 O O      . ALA   A  1 522 ? 13.418 -50.589  -31.680 1.00 29.40  ? 514  ALA   A O      1 
ATOM   4060 C CB     . ALA   A  1 522 ? 15.686 -50.694  -33.815 1.00 28.09  ? 514  ALA   A CB     1 
ATOM   4061 N N      . PRO   A  1 523 ? 15.306 -50.283  -30.456 1.00 26.56  ? 515  PRO   A N      1 
ATOM   4062 C CA     . PRO   A  1 523 ? 14.581 -49.498  -29.436 1.00 25.62  ? 515  PRO   A CA     1 
ATOM   4063 C C      . PRO   A  1 523 ? 13.821 -48.322  -30.045 1.00 27.60  ? 515  PRO   A C      1 
ATOM   4064 O O      . PRO   A  1 523 ? 14.285 -47.717  -31.008 1.00 26.66  ? 515  PRO   A O      1 
ATOM   4065 C CB     . PRO   A  1 523 ? 15.690 -49.024  -28.482 1.00 27.18  ? 515  PRO   A CB     1 
ATOM   4066 C CG     . PRO   A  1 523 ? 16.793 -49.992  -28.671 1.00 31.66  ? 515  PRO   A CG     1 
ATOM   4067 C CD     . PRO   A  1 523 ? 16.741 -50.398  -30.123 1.00 27.24  ? 515  PRO   A CD     1 
ATOM   4068 N N      . GLN   A  1 524 ? 12.629 -48.045  -29.519 1.00 23.05  ? 516  GLN   A N      1 
ATOM   4069 C CA     . GLN   A  1 524 ? 11.783 -46.953  -29.984 1.00 22.01  ? 516  GLN   A CA     1 
ATOM   4070 C C      . GLN   A  1 524 ? 11.466 -46.028  -28.813 1.00 26.31  ? 516  GLN   A C      1 
ATOM   4071 O O      . GLN   A  1 524 ? 11.324 -46.521  -27.693 1.00 26.62  ? 516  GLN   A O      1 
ATOM   4072 C CB     . GLN   A  1 524 ? 10.494 -47.496  -30.602 1.00 23.01  ? 516  GLN   A CB     1 
ATOM   4073 C CG     . GLN   A  1 524 ? 10.673 -47.982  -32.049 1.00 28.22  ? 516  GLN   A CG     1 
ATOM   4074 C CD     . GLN   A  1 524 ? 9.351  -48.285  -32.703 1.00 33.71  ? 516  GLN   A CD     1 
ATOM   4075 O OE1    . GLN   A  1 524 ? 8.385  -47.519  -32.605 1.00 28.30  ? 516  GLN   A OE1    1 
ATOM   4076 N NE2    . GLN   A  1 524 ? 9.293  -49.390  -33.420 1.00 23.65  ? 516  GLN   A NE2    1 
ATOM   4077 N N      . PRO   A  1 525 ? 11.380 -44.694  -29.035 1.00 22.96  ? 517  PRO   A N      1 
ATOM   4078 C CA     . PRO   A  1 525 ? 11.079 -43.784  -27.916 1.00 22.75  ? 517  PRO   A CA     1 
ATOM   4079 C C      . PRO   A  1 525 ? 9.683  -44.029  -27.372 1.00 27.03  ? 517  PRO   A C      1 
ATOM   4080 O O      . PRO   A  1 525 ? 8.760  -44.300  -28.139 1.00 26.76  ? 517  PRO   A O      1 
ATOM   4081 C CB     . PRO   A  1 525 ? 11.234 -42.387  -28.527 1.00 24.39  ? 517  PRO   A CB     1 
ATOM   4082 C CG     . PRO   A  1 525 ? 11.066 -42.579  -29.983 1.00 29.08  ? 517  PRO   A CG     1 
ATOM   4083 C CD     . PRO   A  1 525 ? 11.539 -43.957  -30.311 1.00 24.08  ? 517  PRO   A CD     1 
ATOM   4084 N N      . CYS   A  1 526 ? 9.554  -43.986  -26.044 1.00 24.09  ? 518  CYS   A N      1 
ATOM   4085 C CA     . CYS   A  1 526 ? 8.321  -44.261  -25.315 1.00 22.99  ? 518  CYS   A CA     1 
ATOM   4086 C C      . CYS   A  1 526 ? 7.755  -42.961  -24.697 1.00 26.57  ? 518  CYS   A C      1 
ATOM   4087 O O      . CYS   A  1 526 ? 6.828  -42.391  -25.267 1.00 26.76  ? 518  CYS   A O      1 
ATOM   4088 C CB     . CYS   A  1 526 ? 8.573  -45.351  -24.269 1.00 22.79  ? 518  CYS   A CB     1 
ATOM   4089 S SG     . CYS   A  1 526 ? 7.097  -45.891  -23.371 1.00 26.37  ? 518  CYS   A SG     1 
ATOM   4090 N N      . PHE   A  1 527 ? 8.330  -42.471  -23.581 1.00 21.56  ? 519  PHE   A N      1 
ATOM   4091 C CA     . PHE   A  1 527 ? 7.858  -41.256  -22.914 1.00 20.77  ? 519  PHE   A CA     1 
ATOM   4092 C C      . PHE   A  1 527 ? 8.927  -40.184  -22.836 1.00 25.34  ? 519  PHE   A C      1 
ATOM   4093 O O      . PHE   A  1 527 ? 10.099 -40.491  -22.602 1.00 25.75  ? 519  PHE   A O      1 
ATOM   4094 C CB     . PHE   A  1 527 ? 7.322  -41.558  -21.499 1.00 21.80  ? 519  PHE   A CB     1 
ATOM   4095 C CG     . PHE   A  1 527 ? 6.276  -42.648  -21.352 1.00 23.05  ? 519  PHE   A CG     1 
ATOM   4096 C CD1    . PHE   A  1 527 ? 5.192  -42.721  -22.220 1.00 25.37  ? 519  PHE   A CD1    1 
ATOM   4097 C CD2    . PHE   A  1 527 ? 6.335  -43.552  -20.295 1.00 24.99  ? 519  PHE   A CD2    1 
ATOM   4098 C CE1    . PHE   A  1 527 ? 4.209  -43.706  -22.056 1.00 26.78  ? 519  PHE   A CE1    1 
ATOM   4099 C CE2    . PHE   A  1 527 ? 5.359  -44.545  -20.143 1.00 27.68  ? 519  PHE   A CE2    1 
ATOM   4100 C CZ     . PHE   A  1 527 ? 4.293  -44.603  -21.014 1.00 25.39  ? 519  PHE   A CZ     1 
ATOM   4101 N N      . THR   A  1 528 ? 8.510  -38.920  -22.998 1.00 20.98  ? 520  THR   A N      1 
ATOM   4102 C CA     . THR   A  1 528 ? 9.389  -37.756  -22.929 1.00 20.12  ? 520  THR   A CA     1 
ATOM   4103 C C      . THR   A  1 528 ? 8.877  -36.722  -21.922 1.00 22.01  ? 520  THR   A C      1 
ATOM   4104 O O      . THR   A  1 528 ? 7.675  -36.451  -21.847 1.00 20.87  ? 520  THR   A O      1 
ATOM   4105 C CB     . THR   A  1 528 ? 9.600  -37.150  -24.344 1.00 27.03  ? 520  THR   A CB     1 
ATOM   4106 O OG1    . THR   A  1 528 ? 10.119 -38.156  -25.215 1.00 29.01  ? 520  THR   A OG1    1 
ATOM   4107 C CG2    . THR   A  1 528 ? 10.549 -35.948  -24.349 1.00 25.24  ? 520  THR   A CG2    1 
ATOM   4108 N N      . PHE   A  1 529 ? 9.813  -36.118  -21.181 1.00 18.78  ? 521  PHE   A N      1 
ATOM   4109 C CA     . PHE   A  1 529 ? 9.540  -35.044  -20.233 1.00 19.24  ? 521  PHE   A CA     1 
ATOM   4110 C C      . PHE   A  1 529 ? 10.540 -33.923  -20.484 1.00 24.73  ? 521  PHE   A C      1 
ATOM   4111 O O      . PHE   A  1 529 ? 11.694 -34.201  -20.824 1.00 22.96  ? 521  PHE   A O      1 
ATOM   4112 C CB     . PHE   A  1 529 ? 9.604  -35.548  -18.770 1.00 20.97  ? 521  PHE   A CB     1 
ATOM   4113 C CG     . PHE   A  1 529 ? 8.496  -36.519  -18.427 1.00 21.78  ? 521  PHE   A CG     1 
ATOM   4114 C CD1    . PHE   A  1 529 ? 8.634  -37.879  -18.685 1.00 24.47  ? 521  PHE   A CD1    1 
ATOM   4115 C CD2    . PHE   A  1 529 ? 7.305  -36.069  -17.872 1.00 22.98  ? 521  PHE   A CD2    1 
ATOM   4116 C CE1    . PHE   A  1 529 ? 7.592  -38.773  -18.396 1.00 25.81  ? 521  PHE   A CE1    1 
ATOM   4117 C CE2    . PHE   A  1 529 ? 6.261  -36.961  -17.588 1.00 25.57  ? 521  PHE   A CE2    1 
ATOM   4118 C CZ     . PHE   A  1 529 ? 6.413  -38.307  -17.846 1.00 24.13  ? 521  PHE   A CZ     1 
ATOM   4119 N N      . SER   A  1 530 ? 10.075 -32.661  -20.365 1.00 23.77  ? 522  SER   A N      1 
ATOM   4120 C CA     . SER   A  1 530 ? 10.883 -31.445  -20.549 1.00 24.42  ? 522  SER   A CA     1 
ATOM   4121 C C      . SER   A  1 530 ? 10.851 -30.587  -19.287 1.00 28.28  ? 522  SER   A C      1 
ATOM   4122 O O      . SER   A  1 530 ? 9.798  -30.461  -18.665 1.00 28.15  ? 522  SER   A O      1 
ATOM   4123 C CB     . SER   A  1 530 ? 10.359 -30.622  -21.725 1.00 27.83  ? 522  SER   A CB     1 
ATOM   4124 O OG     . SER   A  1 530 ? 10.480 -31.320  -22.951 1.00 41.09  ? 522  SER   A OG     1 
ATOM   4125 N N      . HIS   A  1 531 ? 11.983 -29.971  -18.927 1.00 25.16  ? 523  HIS   A N      1 
ATOM   4126 C CA     . HIS   A  1 531 ? 12.068 -29.119  -17.737 1.00 25.93  ? 523  HIS   A CA     1 
ATOM   4127 C C      . HIS   A  1 531 ? 12.674 -27.733  -18.013 1.00 29.94  ? 523  HIS   A C      1 
ATOM   4128 O O      . HIS   A  1 531 ? 13.720 -27.663  -18.658 1.00 26.84  ? 523  HIS   A O      1 
ATOM   4129 C CB     . HIS   A  1 531 ? 12.814 -29.843  -16.599 1.00 27.07  ? 523  HIS   A CB     1 
ATOM   4130 C CG     . HIS   A  1 531 ? 12.077 -31.051  -16.117 1.00 30.47  ? 523  HIS   A CG     1 
ATOM   4131 N ND1    . HIS   A  1 531 ? 10.968 -30.936  -15.306 1.00 32.34  ? 523  HIS   A ND1    1 
ATOM   4132 C CD2    . HIS   A  1 531 ? 12.261 -32.355  -16.426 1.00 32.40  ? 523  HIS   A CD2    1 
ATOM   4133 C CE1    . HIS   A  1 531 ? 10.531 -32.171  -15.119 1.00 31.87  ? 523  HIS   A CE1    1 
ATOM   4134 N NE2    . HIS   A  1 531 ? 11.281 -33.057  -15.771 1.00 32.08  ? 523  HIS   A NE2    1 
ATOM   4135 N N      . PRO   A  1 532 ? 12.065 -26.614  -17.535 1.00 30.18  ? 524  PRO   A N      1 
ATOM   4136 C CA     . PRO   A  1 532 ? 10.795 -26.501  -16.785 1.00 30.96  ? 524  PRO   A CA     1 
ATOM   4137 C C      . PRO   A  1 532 ? 9.568  -26.767  -17.658 1.00 38.23  ? 524  PRO   A C      1 
ATOM   4138 O O      . PRO   A  1 532 ? 9.655  -26.678  -18.879 1.00 37.65  ? 524  PRO   A O      1 
ATOM   4139 C CB     . PRO   A  1 532 ? 10.822 -25.047  -16.284 1.00 32.56  ? 524  PRO   A CB     1 
ATOM   4140 C CG     . PRO   A  1 532 ? 11.586 -24.308  -17.344 1.00 36.51  ? 524  PRO   A CG     1 
ATOM   4141 C CD     . PRO   A  1 532 ? 12.658 -25.279  -17.788 1.00 32.08  ? 524  PRO   A CD     1 
ATOM   4142 N N      . ASN   A  1 533 ? 8.435  -27.100  -17.033 1.00 38.66  ? 525  ASN   A N      1 
ATOM   4143 C CA     . ASN   A  1 533 ? 7.177  -27.379  -17.728 1.00 40.90  ? 525  ASN   A CA     1 
ATOM   4144 C C      . ASN   A  1 533 ? 6.250  -26.191  -17.462 1.00 50.63  ? 525  ASN   A C      1 
ATOM   4145 O O      . ASN   A  1 533 ? 5.620  -26.124  -16.403 1.00 50.45  ? 525  ASN   A O      1 
ATOM   4146 C CB     . ASN   A  1 533 ? 6.574  -28.709  -17.224 1.00 41.56  ? 525  ASN   A CB     1 
ATOM   4147 C CG     . ASN   A  1 533 ? 5.473  -29.297  -18.074 1.00 67.33  ? 525  ASN   A CG     1 
ATOM   4148 O OD1    . ASN   A  1 533 ? 4.588  -28.606  -18.589 1.00 60.48  ? 525  ASN   A OD1    1 
ATOM   4149 N ND2    . ASN   A  1 533 ? 5.473  -30.615  -18.190 1.00 64.99  ? 525  ASN   A ND2    1 
ATOM   4150 N N      . ARG   A  1 534 ? 6.204  -25.234  -18.415 1.00 51.83  ? 526  ARG   A N      1 
ATOM   4151 C CA     . ARG   A  1 534 ? 5.448  -23.978  -18.301 1.00 53.28  ? 526  ARG   A CA     1 
ATOM   4152 C C      . ARG   A  1 534 ? 3.992  -24.060  -18.811 1.00 61.01  ? 526  ARG   A C      1 
ATOM   4153 O O      . ARG   A  1 534 ? 3.336  -23.022  -18.965 1.00 60.42  ? 526  ARG   A O      1 
ATOM   4154 C CB     . ARG   A  1 534 ? 6.218  -22.821  -18.976 1.00 53.54  ? 526  ARG   A CB     1 
ATOM   4155 C CG     . ARG   A  1 534 ? 7.588  -22.518  -18.352 1.00 63.94  ? 526  ARG   A CG     1 
ATOM   4156 C CD     . ARG   A  1 534 ? 7.515  -21.517  -17.208 1.00 71.11  ? 526  ARG   A CD     1 
ATOM   4157 N NE     . ARG   A  1 534 ? 8.822  -21.299  -16.582 1.00 76.09  ? 526  ARG   A NE     1 
ATOM   4158 C CZ     . ARG   A  1 534 ? 9.117  -21.615  -15.323 1.00 86.10  ? 526  ARG   A CZ     1 
ATOM   4159 N NH1    . ARG   A  1 534 ? 8.198  -22.157  -14.533 1.00 75.41  ? 526  ARG   A NH1    1 
ATOM   4160 N NH2    . ARG   A  1 534 ? 10.331 -21.381  -14.841 1.00 65.10  ? 526  ARG   A NH2    1 
ATOM   4161 N N      . ASP   A  1 535 ? 3.471  -25.288  -19.017 1.00 60.62  ? 527  ASP   A N      1 
ATOM   4162 C CA     . ASP   A  1 535 ? 2.088  -25.516  -19.449 1.00 61.61  ? 527  ASP   A CA     1 
ATOM   4163 C C      . ASP   A  1 535 ? 1.099  -25.155  -18.330 1.00 66.80  ? 527  ASP   A C      1 
ATOM   4164 O O      . ASP   A  1 535 ? 1.425  -25.383  -17.160 1.00 66.18  ? 527  ASP   A O      1 
ATOM   4165 C CB     . ASP   A  1 535 ? 1.886  -26.973  -19.880 1.00 63.95  ? 527  ASP   A CB     1 
ATOM   4166 C CG     . ASP   A  1 535 ? 2.446  -27.259  -21.252 1.00 79.73  ? 527  ASP   A CG     1 
ATOM   4167 O OD1    . ASP   A  1 535 ? 1.768  -26.928  -22.250 1.00 81.08  ? 527  ASP   A OD1    1 
ATOM   4168 O OD2    . ASP   A  1 535 ? 3.571  -27.801  -21.331 1.00 87.59  ? 527  ASP   A OD2    1 
ATOM   4169 N N      . PRO   A  1 536 ? -0.103 -24.598  -18.656 1.00 64.52  ? 528  PRO   A N      1 
ATOM   4170 C CA     . PRO   A  1 536 ? -1.070 -24.248  -17.593 1.00 64.41  ? 528  PRO   A CA     1 
ATOM   4171 C C      . PRO   A  1 536 ? -1.562 -25.454  -16.785 1.00 67.96  ? 528  PRO   A C      1 
ATOM   4172 O O      . PRO   A  1 536 ? -1.774 -25.330  -15.576 1.00 67.86  ? 528  PRO   A O      1 
ATOM   4173 C CB     . PRO   A  1 536 ? -2.214 -23.563  -18.355 1.00 66.26  ? 528  PRO   A CB     1 
ATOM   4174 C CG     . PRO   A  1 536 ? -1.638 -23.190  -19.687 1.00 70.76  ? 528  PRO   A CG     1 
ATOM   4175 C CD     . PRO   A  1 536 ? -0.637 -24.255  -19.991 1.00 66.31  ? 528  PRO   A CD     1 
ATOM   4176 N N      . MET   A  1 537 ? -1.726 -26.618  -17.451 1.00 63.75  ? 529  MET   A N      1 
ATOM   4177 C CA     . MET   A  1 537 ? -2.152 -27.869  -16.824 1.00 63.28  ? 529  MET   A CA     1 
ATOM   4178 C C      . MET   A  1 537 ? -1.047 -28.913  -16.977 1.00 63.79  ? 529  MET   A C      1 
ATOM   4179 O O      . MET   A  1 537 ? -0.881 -29.497  -18.055 1.00 63.60  ? 529  MET   A O      1 
ATOM   4180 C CB     . MET   A  1 537 ? -3.479 -28.386  -17.417 1.00 66.18  ? 529  MET   A CB     1 
ATOM   4181 C CG     . MET   A  1 537 ? -4.710 -27.650  -16.914 1.00 70.54  ? 529  MET   A CG     1 
ATOM   4182 S SD     . MET   A  1 537 ? -5.184 -26.248  -17.958 1.00 75.36  ? 529  MET   A SD     1 
ATOM   4183 C CE     . MET   A  1 537 ? -5.952 -27.105  -19.336 1.00 72.12  ? 529  MET   A CE     1 
ATOM   4184 N N      . ILE   A  1 538 ? -0.268 -29.124  -15.905 1.00 56.70  ? 530  ILE   A N      1 
ATOM   4185 C CA     . ILE   A  1 538 ? 0.816  -30.099  -15.933 1.00 54.44  ? 530  ILE   A CA     1 
ATOM   4186 C C      . ILE   A  1 538 ? 0.249  -31.506  -15.728 1.00 52.73  ? 530  ILE   A C      1 
ATOM   4187 O O      . ILE   A  1 538 ? -0.453 -31.753  -14.738 1.00 52.64  ? 530  ILE   A O      1 
ATOM   4188 C CB     . ILE   A  1 538 ? 1.987  -29.735  -14.971 1.00 57.62  ? 530  ILE   A CB     1 
ATOM   4189 C CG1    . ILE   A  1 538 ? 2.677  -28.421  -15.414 1.00 58.09  ? 530  ILE   A CG1    1 
ATOM   4190 C CG2    . ILE   A  1 538 ? 3.009  -30.881  -14.880 1.00 58.38  ? 530  ILE   A CG2    1 
ATOM   4191 C CD1    . ILE   A  1 538 ? 3.413  -27.655  -14.299 1.00 67.07  ? 530  ILE   A CD1    1 
ATOM   4192 N N      . ASP   A  1 539 ? 0.528  -32.415  -16.688 1.00 43.53  ? 531  ASP   A N      1 
ATOM   4193 C CA     . ASP   A  1 539 ? 0.085  -33.805  -16.614 1.00 40.53  ? 531  ASP   A CA     1 
ATOM   4194 C C      . ASP   A  1 539 ? 1.219  -34.770  -16.948 1.00 35.36  ? 531  ASP   A C      1 
ATOM   4195 O O      . ASP   A  1 539 ? 1.657  -34.846  -18.096 1.00 32.73  ? 531  ASP   A O      1 
ATOM   4196 C CB     . ASP   A  1 539 ? -1.186 -34.067  -17.445 1.00 42.76  ? 531  ASP   A CB     1 
ATOM   4197 C CG     . ASP   A  1 539 ? -1.948 -35.332  -17.055 1.00 55.73  ? 531  ASP   A CG     1 
ATOM   4198 O OD1    . ASP   A  1 539 ? -1.494 -36.046  -16.130 1.00 55.75  ? 531  ASP   A OD1    1 
ATOM   4199 O OD2    . ASP   A  1 539 ? -3.009 -35.595  -17.658 1.00 63.50  ? 531  ASP   A OD2    1 
ATOM   4200 N N      . ASN   A  1 540 ? 1.718  -35.476  -15.915 1.00 27.54  ? 532  ASN   A N      1 
ATOM   4201 C CA     . ASN   A  1 540 ? 2.821  -36.428  -16.051 1.00 25.28  ? 532  ASN   A CA     1 
ATOM   4202 C C      . ASN   A  1 540 ? 2.376  -37.826  -16.482 1.00 25.62  ? 532  ASN   A C      1 
ATOM   4203 O O      . ASN   A  1 540 ? 3.225  -38.678  -16.768 1.00 25.38  ? 532  ASN   A O      1 
ATOM   4204 C CB     . ASN   A  1 540 ? 3.652  -36.465  -14.781 1.00 24.51  ? 532  ASN   A CB     1 
ATOM   4205 C CG     . ASN   A  1 540 ? 4.381  -35.177  -14.497 1.00 35.89  ? 532  ASN   A CG     1 
ATOM   4206 O OD1    . ASN   A  1 540 ? 4.658  -34.852  -13.343 1.00 32.17  ? 532  ASN   A OD1    1 
ATOM   4207 N ND2    . ASN   A  1 540 ? 4.724  -34.427  -15.534 1.00 22.92  ? 532  ASN   A ND2    1 
ATOM   4208 N N      . ASN   A  1 541 ? 1.058  -38.055  -16.554 1.00 20.76  ? 533  ASN   A N      1 
ATOM   4209 C CA     . ASN   A  1 541 ? 0.476  -39.302  -17.043 1.00 20.43  ? 533  ASN   A CA     1 
ATOM   4210 C C      . ASN   A  1 541 ? 0.755  -39.406  -18.527 1.00 25.91  ? 533  ASN   A C      1 
ATOM   4211 O O      . ASN   A  1 541 ? 0.879  -38.383  -19.221 1.00 25.25  ? 533  ASN   A O      1 
ATOM   4212 C CB     . ASN   A  1 541 ? -1.025 -39.366  -16.795 1.00 20.93  ? 533  ASN   A CB     1 
ATOM   4213 C CG     . ASN   A  1 541 ? -1.437 -39.467  -15.350 1.00 35.37  ? 533  ASN   A CG     1 
ATOM   4214 O OD1    . ASN   A  1 541 ? -0.670 -39.856  -14.472 1.00 28.64  ? 533  ASN   A OD1    1 
ATOM   4215 N ND2    . ASN   A  1 541 ? -2.692 -39.165  -15.079 1.00 31.71  ? 533  ASN   A ND2    1 
ATOM   4216 N N      . ARG   A  1 542 ? 0.931  -40.636  -19.009 1.00 22.96  ? 534  ARG   A N      1 
ATOM   4217 C CA     . ARG   A  1 542 ? 1.310  -40.879  -20.393 1.00 22.29  ? 534  ARG   A CA     1 
ATOM   4218 C C      . ARG   A  1 542 ? 0.674  -42.144  -20.921 1.00 26.90  ? 534  ARG   A C      1 
ATOM   4219 O O      . ARG   A  1 542 ? 0.331  -43.025  -20.140 1.00 25.93  ? 534  ARG   A O      1 
ATOM   4220 C CB     . ARG   A  1 542 ? 2.850  -41.012  -20.490 1.00 20.88  ? 534  ARG   A CB     1 
ATOM   4221 C CG     . ARG   A  1 542 ? 3.698  -39.762  -20.253 1.00 23.27  ? 534  ARG   A CG     1 
ATOM   4222 C CD     . ARG   A  1 542 ? 3.529  -38.729  -21.361 1.00 24.70  ? 534  ARG   A CD     1 
ATOM   4223 N NE     . ARG   A  1 542 ? 4.515  -37.647  -21.283 1.00 22.17  ? 534  ARG   A NE     1 
ATOM   4224 C CZ     . ARG   A  1 542 ? 4.376  -36.557  -20.541 1.00 34.60  ? 534  ARG   A CZ     1 
ATOM   4225 N NH1    . ARG   A  1 542 ? 3.306  -36.401  -19.769 1.00 25.04  ? 534  ARG   A NH1    1 
ATOM   4226 N NH2    . ARG   A  1 542 ? 5.312  -35.618  -20.552 1.00 23.37  ? 534  ARG   A NH2    1 
ATOM   4227 N N      . TYR   A  1 543 ? 0.518  -42.232  -22.255 1.00 25.18  ? 535  TYR   A N      1 
ATOM   4228 C CA     . TYR   A  1 543 ? 0.005  -43.402  -22.963 1.00 25.91  ? 535  TYR   A CA     1 
ATOM   4229 C C      . TYR   A  1 543 ? 0.724  -43.481  -24.312 1.00 31.58  ? 535  TYR   A C      1 
ATOM   4230 O O      . TYR   A  1 543 ? 0.694  -42.531  -25.091 1.00 32.28  ? 535  TYR   A O      1 
ATOM   4231 C CB     . TYR   A  1 543 ? -1.532 -43.361  -23.113 1.00 26.98  ? 535  TYR   A CB     1 
ATOM   4232 C CG     . TYR   A  1 543 ? -2.140 -44.463  -23.965 1.00 28.39  ? 535  TYR   A CG     1 
ATOM   4233 C CD1    . TYR   A  1 543 ? -1.585 -45.743  -23.993 1.00 29.29  ? 535  TYR   A CD1    1 
ATOM   4234 C CD2    . TYR   A  1 543 ? -3.309 -44.245  -24.690 1.00 29.79  ? 535  TYR   A CD2    1 
ATOM   4235 C CE1    . TYR   A  1 543 ? -2.146 -46.759  -24.760 1.00 28.83  ? 535  TYR   A CE1    1 
ATOM   4236 C CE2    . TYR   A  1 543 ? -3.888 -45.260  -25.452 1.00 31.09  ? 535  TYR   A CE2    1 
ATOM   4237 C CZ     . TYR   A  1 543 ? -3.314 -46.523  -25.466 1.00 37.26  ? 535  TYR   A CZ     1 
ATOM   4238 O OH     . TYR   A  1 543 ? -3.887 -47.542  -26.190 1.00 37.27  ? 535  TYR   A OH     1 
ATOM   4239 N N      . CYS   A  1 544 ? 1.416  -44.592  -24.548 1.00 28.69  ? 536  CYS   A N      1 
ATOM   4240 C CA     . CYS   A  1 544 ? 2.198  -44.817  -25.753 1.00 29.42  ? 536  CYS   A CA     1 
ATOM   4241 C C      . CYS   A  1 544 ? 1.860  -46.152  -26.381 1.00 28.82  ? 536  CYS   A C      1 
ATOM   4242 O O      . CYS   A  1 544 ? 1.722  -47.148  -25.668 1.00 26.73  ? 536  CYS   A O      1 
ATOM   4243 C CB     . CYS   A  1 544 ? 3.683  -44.726  -25.420 1.00 31.98  ? 536  CYS   A CB     1 
ATOM   4244 S SG     . CYS   A  1 544 ? 4.771  -44.693  -26.865 1.00 37.50  ? 536  CYS   A SG     1 
ATOM   4245 N N      . THR   A  1 545 ? 1.730  -46.174  -27.719 1.00 24.12  ? 537  THR   A N      1 
ATOM   4246 C CA     . THR   A  1 545 ? 1.513  -47.386  -28.515 1.00 23.91  ? 537  THR   A CA     1 
ATOM   4247 C C      . THR   A  1 545 ? 2.741  -47.533  -29.397 1.00 27.27  ? 537  THR   A C      1 
ATOM   4248 O O      . THR   A  1 545 ? 3.063  -46.616  -30.154 1.00 27.46  ? 537  THR   A O      1 
ATOM   4249 C CB     . THR   A  1 545 ? 0.204  -47.343  -29.333 1.00 29.62  ? 537  THR   A CB     1 
ATOM   4250 O OG1    . THR   A  1 545 ? -0.903 -47.267  -28.445 1.00 31.69  ? 537  THR   A OG1    1 
ATOM   4251 C CG2    . THR   A  1 545 ? 0.020  -48.581  -30.204 1.00 27.86  ? 537  THR   A CG2    1 
ATOM   4252 N N      . LEU   A  1 546 ? 3.430  -48.670  -29.279 1.00 23.19  ? 538  LEU   A N      1 
ATOM   4253 C CA     . LEU   A  1 546 ? 4.623  -48.960  -30.062 1.00 23.12  ? 538  LEU   A CA     1 
ATOM   4254 C C      . LEU   A  1 546 ? 4.432  -50.194  -30.937 1.00 26.90  ? 538  LEU   A C      1 
ATOM   4255 O O      . LEU   A  1 546 ? 3.894  -51.203  -30.476 1.00 26.58  ? 538  LEU   A O      1 
ATOM   4256 C CB     . LEU   A  1 546 ? 5.864  -49.111  -29.165 1.00 23.10  ? 538  LEU   A CB     1 
ATOM   4257 C CG     . LEU   A  1 546 ? 6.304  -47.856  -28.402 1.00 28.00  ? 538  LEU   A CG     1 
ATOM   4258 C CD1    . LEU   A  1 546 ? 7.391  -48.180  -27.404 1.00 27.69  ? 538  LEU   A CD1    1 
ATOM   4259 C CD2    . LEU   A  1 546 ? 6.772  -46.744  -29.365 1.00 31.72  ? 538  LEU   A CD2    1 
ATOM   4260 N N      . GLU   A  1 547 ? 4.854  -50.094  -32.204 1.00 22.81  ? 539  GLU   A N      1 
ATOM   4261 C CA     . GLU   A  1 547 ? 4.779  -51.179  -33.180 1.00 22.87  ? 539  GLU   A CA     1 
ATOM   4262 C C      . GLU   A  1 547 ? 6.203  -51.549  -33.581 1.00 25.46  ? 539  GLU   A C      1 
ATOM   4263 O O      . GLU   A  1 547 ? 6.935  -50.741  -34.165 1.00 25.25  ? 539  GLU   A O      1 
ATOM   4264 C CB     . GLU   A  1 547 ? 3.928  -50.777  -34.397 1.00 24.33  ? 539  GLU   A CB     1 
ATOM   4265 C CG     . GLU   A  1 547 ? 2.453  -50.601  -34.077 1.00 36.63  ? 539  GLU   A CG     1 
ATOM   4266 C CD     . GLU   A  1 547 ? 1.531  -51.520  -34.854 1.00 72.90  ? 539  GLU   A CD     1 
ATOM   4267 O OE1    . GLU   A  1 547 ? 1.351  -52.684  -34.426 1.00 79.58  ? 539  GLU   A OE1    1 
ATOM   4268 O OE2    . GLU   A  1 547 ? 0.996  -51.081  -35.897 1.00 68.89  ? 539  GLU   A OE2    1 
ATOM   4269 N N      . PHE   A  1 548 ? 6.598  -52.762  -33.225 1.00 20.59  ? 540  PHE   A N      1 
ATOM   4270 C CA     . PHE   A  1 548 ? 7.936  -53.271  -33.465 1.00 19.85  ? 540  PHE   A CA     1 
ATOM   4271 C C      . PHE   A  1 548 ? 7.991  -54.312  -34.579 1.00 24.99  ? 540  PHE   A C      1 
ATOM   4272 O O      . PHE   A  1 548 ? 7.532  -55.443  -34.374 1.00 24.18  ? 540  PHE   A O      1 
ATOM   4273 C CB     . PHE   A  1 548 ? 8.526  -53.863  -32.190 1.00 20.55  ? 540  PHE   A CB     1 
ATOM   4274 C CG     . PHE   A  1 548 ? 8.816  -52.872  -31.088 1.00 21.81  ? 540  PHE   A CG     1 
ATOM   4275 C CD1    . PHE   A  1 548 ? 9.956  -52.073  -31.130 1.00 24.09  ? 540  PHE   A CD1    1 
ATOM   4276 C CD2    . PHE   A  1 548 ? 7.979  -52.775  -29.981 1.00 23.00  ? 540  PHE   A CD2    1 
ATOM   4277 C CE1    . PHE   A  1 548 ? 10.242 -51.179  -30.094 1.00 24.97  ? 540  PHE   A CE1    1 
ATOM   4278 C CE2    . PHE   A  1 548 ? 8.266  -51.877  -28.944 1.00 25.67  ? 540  PHE   A CE2    1 
ATOM   4279 C CZ     . PHE   A  1 548 ? 9.394  -51.086  -29.010 1.00 23.72  ? 540  PHE   A CZ     1 
ATOM   4280 N N      . PRO   A  1 549 ? 8.590  -53.966  -35.744 1.00 23.35  ? 541  PRO   A N      1 
ATOM   4281 C CA     . PRO   A  1 549 ? 8.736  -54.972  -36.807 1.00 23.77  ? 541  PRO   A CA     1 
ATOM   4282 C C      . PRO   A  1 549 ? 9.736  -56.038  -36.384 1.00 28.37  ? 541  PRO   A C      1 
ATOM   4283 O O      . PRO   A  1 549 ? 10.810 -55.720  -35.866 1.00 29.82  ? 541  PRO   A O      1 
ATOM   4284 C CB     . PRO   A  1 549 ? 9.213  -54.165  -38.023 1.00 25.38  ? 541  PRO   A CB     1 
ATOM   4285 C CG     . PRO   A  1 549 ? 9.768  -52.922  -37.488 1.00 30.17  ? 541  PRO   A CG     1 
ATOM   4286 C CD     . PRO   A  1 549 ? 9.183  -52.667  -36.130 1.00 25.59  ? 541  PRO   A CD     1 
ATOM   4287 N N      . VAL   A  1 550 ? 9.354  -57.298  -36.547 1.00 24.46  ? 542  VAL   A N      1 
ATOM   4288 C CA     . VAL   A  1 550 ? 10.189 -58.442  -36.187 1.00 24.65  ? 542  VAL   A CA     1 
ATOM   4289 C C      . VAL   A  1 550 ? 10.509 -59.240  -37.468 1.00 31.63  ? 542  VAL   A C      1 
ATOM   4290 O O      . VAL   A  1 550 ? 9.599  -59.724  -38.141 1.00 30.43  ? 542  VAL   A O      1 
ATOM   4291 C CB     . VAL   A  1 550 ? 9.517  -59.289  -35.061 1.00 28.02  ? 542  VAL   A CB     1 
ATOM   4292 C CG1    . VAL   A  1 550 ? 10.268 -60.584  -34.792 1.00 27.43  ? 542  VAL   A CG1    1 
ATOM   4293 C CG2    . VAL   A  1 550 ? 9.375  -58.476  -33.769 1.00 28.06  ? 542  VAL   A CG2    1 
ATOM   4294 N N      . GLU   A  1 551 ? 11.799 -59.330  -37.817 1.00 31.29  ? 543  GLU   A N      1 
ATOM   4295 C CA     . GLU   A  1 551 ? 12.252 -60.052  -39.015 1.00 32.42  ? 543  GLU   A CA     1 
ATOM   4296 C C      . GLU   A  1 551 ? 12.870 -61.416  -38.676 1.00 36.14  ? 543  GLU   A C      1 
ATOM   4297 O O      . GLU   A  1 551 ? 13.716 -61.925  -39.418 1.00 36.58  ? 543  GLU   A O      1 
ATOM   4298 C CB     . GLU   A  1 551 ? 13.189 -59.178  -39.878 1.00 34.38  ? 543  GLU   A CB     1 
ATOM   4299 C CG     . GLU   A  1 551 ? 14.462 -58.700  -39.193 1.00 48.48  ? 543  GLU   A CG     1 
ATOM   4300 C CD     . GLU   A  1 551 ? 15.328 -57.766  -40.017 1.00 74.13  ? 543  GLU   A CD     1 
ATOM   4301 O OE1    . GLU   A  1 551 ? 14.876 -56.634  -40.311 1.00 71.46  ? 543  GLU   A OE1    1 
ATOM   4302 O OE2    . GLU   A  1 551 ? 16.479 -58.149  -40.330 1.00 68.56  ? 543  GLU   A OE2    1 
ATOM   4303 N N      . VAL   A  1 552 ? 12.384 -62.038  -37.588 1.00 31.37  ? 544  VAL   A N      1 
ATOM   4304 C CA     . VAL   A  1 552 ? 12.905 -63.302  -37.081 1.00 30.93  ? 544  VAL   A CA     1 
ATOM   4305 C C      . VAL   A  1 552 ? 11.816 -64.141  -36.367 1.00 33.29  ? 544  VAL   A C      1 
ATOM   4306 O O      . VAL   A  1 552 ? 10.857 -63.568  -35.848 1.00 32.91  ? 544  VAL   A O      1 
ATOM   4307 C CB     . VAL   A  1 552 ? 14.099 -62.881  -36.164 1.00 36.25  ? 544  VAL   A CB     1 
ATOM   4308 C CG1    . VAL   A  1 552 ? 13.913 -63.197  -34.680 1.00 36.30  ? 544  VAL   A CG1    1 
ATOM   4309 C CG2    . VAL   A  1 552 ? 15.437 -63.341  -36.706 1.00 36.34  ? 544  VAL   A CG2    1 
ATOM   4310 N N      . ASN   A  1 553 ? 11.942 -65.491  -36.369 1.00 28.46  ? 545  ASN   A N      1 
ATOM   4311 C CA     . ASN   A  1 553 ? 11.051 -66.371  -35.596 1.00 27.68  ? 545  ASN   A CA     1 
ATOM   4312 C C      . ASN   A  1 553 ? 11.636 -66.368  -34.202 1.00 32.56  ? 545  ASN   A C      1 
ATOM   4313 O O      . ASN   A  1 553 ? 12.865 -66.444  -34.070 1.00 32.73  ? 545  ASN   A O      1 
ATOM   4314 C CB     . ASN   A  1 553 ? 11.030 -67.789  -36.123 1.00 27.53  ? 545  ASN   A CB     1 
ATOM   4315 C CG     . ASN   A  1 553 ? 10.348 -67.964  -37.455 1.00 46.91  ? 545  ASN   A CG     1 
ATOM   4316 O OD1    . ASN   A  1 553 ? 9.283  -67.397  -37.727 1.00 36.64  ? 545  ASN   A OD1    1 
ATOM   4317 N ND2    . ASN   A  1 553 ? 10.924 -68.813  -38.290 1.00 39.58  ? 545  ASN   A ND2    1 
ATOM   4318 N N      . THR   A  1 554 ? 10.784 -66.218  -33.161 1.00 27.78  ? 546  THR   A N      1 
ATOM   4319 C CA     . THR   A  1 554 ? 11.235 -66.039  -31.777 1.00 26.44  ? 546  THR   A CA     1 
ATOM   4320 C C      . THR   A  1 554 ? 10.102 -66.207  -30.756 1.00 28.85  ? 546  THR   A C      1 
ATOM   4321 O O      . THR   A  1 554 ? 8.981  -66.583  -31.112 1.00 28.27  ? 546  THR   A O      1 
ATOM   4322 C CB     . THR   A  1 554 ? 11.901 -64.626  -31.670 1.00 29.80  ? 546  THR   A CB     1 
ATOM   4323 O OG1    . THR   A  1 554 ? 12.499 -64.427  -30.389 1.00 26.24  ? 546  THR   A OG1    1 
ATOM   4324 C CG2    . THR   A  1 554 ? 10.947 -63.480  -32.013 1.00 27.50  ? 546  THR   A CG2    1 
ATOM   4325 N N      . VAL   A  1 555 ? 10.416 -65.942  -29.479 1.00 24.99  ? 547  VAL   A N      1 
ATOM   4326 C CA     . VAL   A  1 555 ? 9.472  -65.951  -28.368 1.00 24.15  ? 547  VAL   A CA     1 
ATOM   4327 C C      . VAL   A  1 555 ? 9.710  -64.673  -27.549 1.00 26.44  ? 547  VAL   A C      1 
ATOM   4328 O O      . VAL   A  1 555 ? 10.808 -64.434  -27.061 1.00 25.91  ? 547  VAL   A O      1 
ATOM   4329 C CB     . VAL   A  1 555 ? 9.501  -67.219  -27.492 1.00 28.30  ? 547  VAL   A CB     1 
ATOM   4330 C CG1    . VAL   A  1 555 ? 8.388  -67.198  -26.456 1.00 28.29  ? 547  VAL   A CG1    1 
ATOM   4331 C CG2    . VAL   A  1 555 ? 9.430  -68.497  -28.327 1.00 28.27  ? 547  VAL   A CG2    1 
ATOM   4332 N N      . LEU   A  1 556 ? 8.682  -63.848  -27.433 1.00 20.73  ? 548  LEU   A N      1 
ATOM   4333 C CA     . LEU   A  1 556 ? 8.725  -62.608  -26.668 1.00 18.83  ? 548  LEU   A CA     1 
ATOM   4334 C C      . LEU   A  1 556 ? 8.600  -62.903  -25.168 1.00 21.45  ? 548  LEU   A C      1 
ATOM   4335 O O      . LEU   A  1 556 ? 7.653  -63.575  -24.745 1.00 20.99  ? 548  LEU   A O      1 
ATOM   4336 C CB     . LEU   A  1 556 ? 7.590  -61.679  -27.164 1.00 18.07  ? 548  LEU   A CB     1 
ATOM   4337 C CG     . LEU   A  1 556 ? 7.295  -60.410  -26.357 1.00 20.73  ? 548  LEU   A CG     1 
ATOM   4338 C CD1    . LEU   A  1 556 ? 8.442  -59.382  -26.505 1.00 19.64  ? 548  LEU   A CD1    1 
ATOM   4339 C CD2    . LEU   A  1 556 ? 5.964  -59.799  -26.801 1.00 20.74  ? 548  LEU   A CD2    1 
ATOM   4340 N N      . HIS   A  1 557 ? 9.543  -62.382  -24.362 1.00 17.95  ? 549  HIS   A N      1 
ATOM   4341 C CA     . HIS   A  1 557 ? 9.511  -62.574  -22.910 1.00 18.42  ? 549  HIS   A CA     1 
ATOM   4342 C C      . HIS   A  1 557 ? 9.357  -61.284  -22.108 1.00 20.67  ? 549  HIS   A C      1 
ATOM   4343 O O      . HIS   A  1 557 ? 9.030  -61.334  -20.935 1.00 19.01  ? 549  HIS   A O      1 
ATOM   4344 C CB     . HIS   A  1 557 ? 10.731 -63.357  -22.430 1.00 19.57  ? 549  HIS   A CB     1 
ATOM   4345 C CG     . HIS   A  1 557 ? 10.731 -64.776  -22.896 1.00 22.83  ? 549  HIS   A CG     1 
ATOM   4346 N ND1    . HIS   A  1 557 ? 11.636 -65.219  -23.831 1.00 23.92  ? 549  HIS   A ND1    1 
ATOM   4347 C CD2    . HIS   A  1 557 ? 9.920  -65.803  -22.544 1.00 23.84  ? 549  HIS   A CD2    1 
ATOM   4348 C CE1    . HIS   A  1 557 ? 11.354 -66.497  -24.012 1.00 22.87  ? 549  HIS   A CE1    1 
ATOM   4349 N NE2    . HIS   A  1 557 ? 10.340 -66.892  -23.248 1.00 23.08  ? 549  HIS   A NE2    1 
ATOM   4350 N N      . GLY   A  1 558 ? 9.596  -60.150  -22.739 1.00 18.55  ? 550  GLY   A N      1 
ATOM   4351 C CA     . GLY   A  1 558 ? 9.491  -58.869  -22.057 1.00 18.01  ? 550  GLY   A CA     1 
ATOM   4352 C C      . GLY   A  1 558 ? 10.036 -57.738  -22.890 1.00 20.66  ? 550  GLY   A C      1 
ATOM   4353 O O      . GLY   A  1 558 ? 10.283 -57.904  -24.087 1.00 20.05  ? 550  GLY   A O      1 
ATOM   4354 N N      . PHE   A  1 559 ? 10.216 -56.573  -22.247 1.00 18.03  ? 551  PHE   A N      1 
ATOM   4355 C CA     . PHE   A  1 559 ? 10.717 -55.382  -22.906 1.00 17.45  ? 551  PHE   A CA     1 
ATOM   4356 C C      . PHE   A  1 559 ? 11.853 -54.786  -22.120 1.00 20.54  ? 551  PHE   A C      1 
ATOM   4357 O O      . PHE   A  1 559 ? 11.754 -54.642  -20.907 1.00 18.72  ? 551  PHE   A O      1 
ATOM   4358 C CB     . PHE   A  1 559 ? 9.592  -54.347  -23.142 1.00 18.67  ? 551  PHE   A CB     1 
ATOM   4359 C CG     . PHE   A  1 559 ? 8.509  -54.870  -24.050 1.00 20.16  ? 551  PHE   A CG     1 
ATOM   4360 C CD1    . PHE   A  1 559 ? 7.485  -55.677  -23.548 1.00 22.72  ? 551  PHE   A CD1    1 
ATOM   4361 C CD2    . PHE   A  1 559 ? 8.529  -54.593  -25.420 1.00 21.40  ? 551  PHE   A CD2    1 
ATOM   4362 C CE1    . PHE   A  1 559 ? 6.535  -56.234  -24.407 1.00 23.65  ? 551  PHE   A CE1    1 
ATOM   4363 C CE2    . PHE   A  1 559 ? 7.555  -55.114  -26.267 1.00 23.73  ? 551  PHE   A CE2    1 
ATOM   4364 C CZ     . PHE   A  1 559 ? 6.575  -55.949  -25.759 1.00 22.16  ? 551  PHE   A CZ     1 
ATOM   4365 N N      . ALA   A  1 560 ? 12.941 -54.460  -22.820 1.00 18.50  ? 552  ALA   A N      1 
ATOM   4366 C CA     . ALA   A  1 560 ? 14.095 -53.797  -22.232 1.00 18.39  ? 552  ALA   A CA     1 
ATOM   4367 C C      . ALA   A  1 560 ? 13.786 -52.310  -22.276 1.00 21.36  ? 552  ALA   A C      1 
ATOM   4368 O O      . ALA   A  1 560 ? 13.219 -51.818  -23.245 1.00 20.96  ? 552  ALA   A O      1 
ATOM   4369 C CB     . ALA   A  1 560 ? 15.350 -54.098  -23.033 1.00 18.91  ? 552  ALA   A CB     1 
ATOM   4370 N N      . GLY   A  1 561 ? 14.109 -51.621  -21.202 1.00 19.73  ? 553  GLY   A N      1 
ATOM   4371 C CA     . GLY   A  1 561 ? 13.895 -50.188  -21.096 1.00 19.05  ? 553  GLY   A CA     1 
ATOM   4372 C C      . GLY   A  1 561 ? 15.214 -49.477  -20.926 1.00 20.52  ? 553  GLY   A C      1 
ATOM   4373 O O      . GLY   A  1 561 ? 16.102 -49.943  -20.202 1.00 19.01  ? 553  GLY   A O      1 
ATOM   4374 N N      . TYR   A  1 562 ? 15.357 -48.378  -21.647 1.00 17.36  ? 554  TYR   A N      1 
ATOM   4375 C CA     . TYR   A  1 562 ? 16.563 -47.560  -21.660 1.00 16.73  ? 554  TYR   A CA     1 
ATOM   4376 C C      . TYR   A  1 562 ? 16.127 -46.118  -21.611 1.00 20.77  ? 554  TYR   A C      1 
ATOM   4377 O O      . TYR   A  1 562 ? 14.929 -45.834  -21.560 1.00 20.99  ? 554  TYR   A O      1 
ATOM   4378 C CB     . TYR   A  1 562 ? 17.351 -47.801  -22.966 1.00 17.31  ? 554  TYR   A CB     1 
ATOM   4379 C CG     . TYR   A  1 562 ? 17.631 -49.253  -23.282 1.00 17.88  ? 554  TYR   A CG     1 
ATOM   4380 C CD1    . TYR   A  1 562 ? 18.684 -49.926  -22.673 1.00 18.46  ? 554  TYR   A CD1    1 
ATOM   4381 C CD2    . TYR   A  1 562 ? 16.892 -49.932  -24.248 1.00 18.95  ? 554  TYR   A CD2    1 
ATOM   4382 C CE1    . TYR   A  1 562 ? 18.980 -51.245  -22.994 1.00 17.29  ? 554  TYR   A CE1    1 
ATOM   4383 C CE2    . TYR   A  1 562 ? 17.182 -51.255  -24.583 1.00 20.09  ? 554  TYR   A CE2    1 
ATOM   4384 C CZ     . TYR   A  1 562 ? 18.214 -51.914  -23.936 1.00 23.69  ? 554  TYR   A CZ     1 
ATOM   4385 O OH     . TYR   A  1 562 ? 18.514 -53.215  -24.252 1.00 19.77  ? 554  TYR   A OH     1 
ATOM   4386 N N      . PHE   A  1 563 ? 17.090 -45.206  -21.627 1.00 17.50  ? 555  PHE   A N      1 
ATOM   4387 C CA     . PHE   A  1 563 ? 16.797 -43.782  -21.663 1.00 17.72  ? 555  PHE   A CA     1 
ATOM   4388 C C      . PHE   A  1 563 ? 17.926 -43.003  -22.324 1.00 21.51  ? 555  PHE   A C      1 
ATOM   4389 O O      . PHE   A  1 563 ? 19.060 -43.487  -22.438 1.00 20.52  ? 555  PHE   A O      1 
ATOM   4390 C CB     . PHE   A  1 563 ? 16.466 -43.218  -20.254 1.00 19.10  ? 555  PHE   A CB     1 
ATOM   4391 C CG     . PHE   A  1 563 ? 17.671 -42.891  -19.401 1.00 20.56  ? 555  PHE   A CG     1 
ATOM   4392 C CD1    . PHE   A  1 563 ? 18.305 -43.878  -18.661 1.00 22.12  ? 555  PHE   A CD1    1 
ATOM   4393 C CD2    . PHE   A  1 563 ? 18.186 -41.598  -19.360 1.00 22.89  ? 555  PHE   A CD2    1 
ATOM   4394 C CE1    . PHE   A  1 563 ? 19.444 -43.588  -17.913 1.00 23.71  ? 555  PHE   A CE1    1 
ATOM   4395 C CE2    . PHE   A  1 563 ? 19.334 -41.311  -18.625 1.00 25.56  ? 555  PHE   A CE2    1 
ATOM   4396 C CZ     . PHE   A  1 563 ? 19.939 -42.303  -17.883 1.00 23.50  ? 555  PHE   A CZ     1 
ATOM   4397 N N      . GLU   A  1 564 ? 17.601 -41.776  -22.705 1.00 19.21  ? 556  GLU   A N      1 
ATOM   4398 C CA     . GLU   A  1 564 ? 18.499 -40.761  -23.237 1.00 20.87  ? 556  GLU   A CA     1 
ATOM   4399 C C      . GLU   A  1 564 ? 18.121 -39.502  -22.520 1.00 25.50  ? 556  GLU   A C      1 
ATOM   4400 O O      . GLU   A  1 564 ? 16.930 -39.284  -22.274 1.00 26.08  ? 556  GLU   A O      1 
ATOM   4401 C CB     . GLU   A  1 564 ? 18.227 -40.509  -24.729 1.00 22.46  ? 556  GLU   A CB     1 
ATOM   4402 C CG     . GLU   A  1 564 ? 19.077 -41.331  -25.666 1.00 37.63  ? 556  GLU   A CG     1 
ATOM   4403 C CD     . GLU   A  1 564 ? 19.056 -40.842  -27.103 1.00 61.31  ? 556  GLU   A CD     1 
ATOM   4404 O OE1    . GLU   A  1 564 ? 18.081 -40.156  -27.497 1.00 45.15  ? 556  GLU   A OE1    1 
ATOM   4405 O OE2    . GLU   A  1 564 ? 20.021 -41.153  -27.840 1.00 59.73  ? 556  GLU   A OE2    1 
ATOM   4406 N N      . THR   A  1 565 ? 19.101 -38.639  -22.241 1.00 21.82  ? 557  THR   A N      1 
ATOM   4407 C CA     . THR   A  1 565 ? 18.827 -37.351  -21.610 1.00 21.91  ? 557  THR   A CA     1 
ATOM   4408 C C      . THR   A  1 565 ? 19.647 -36.245  -22.244 1.00 25.71  ? 557  THR   A C      1 
ATOM   4409 O O      . THR   A  1 565 ? 20.802 -36.461  -22.608 1.00 25.23  ? 557  THR   A O      1 
ATOM   4410 C CB     . THR   A  1 565 ? 18.965 -37.390  -20.058 1.00 26.32  ? 557  THR   A CB     1 
ATOM   4411 O OG1    . THR   A  1 565 ? 18.530 -36.143  -19.520 1.00 28.07  ? 557  THR   A OG1    1 
ATOM   4412 C CG2    . THR   A  1 565 ? 20.377 -37.657  -19.575 1.00 22.06  ? 557  THR   A CG2    1 
ATOM   4413 N N      . VAL   A  1 566 ? 19.040 -35.072  -22.372 1.00 22.76  ? 558  VAL   A N      1 
ATOM   4414 C CA     . VAL   A  1 566 ? 19.712 -33.872  -22.850 1.00 23.33  ? 558  VAL   A CA     1 
ATOM   4415 C C      . VAL   A  1 566 ? 20.031 -33.096  -21.571 1.00 25.63  ? 558  VAL   A C      1 
ATOM   4416 O O      . VAL   A  1 566 ? 19.116 -32.603  -20.899 1.00 24.10  ? 558  VAL   A O      1 
ATOM   4417 C CB     . VAL   A  1 566 ? 18.863 -33.039  -23.860 1.00 28.14  ? 558  VAL   A CB     1 
ATOM   4418 C CG1    . VAL   A  1 566 ? 19.503 -31.671  -24.134 1.00 28.24  ? 558  VAL   A CG1    1 
ATOM   4419 C CG2    . VAL   A  1 566 ? 18.649 -33.804  -25.169 1.00 28.15  ? 558  VAL   A CG2    1 
ATOM   4420 N N      . LEU   A  1 567 ? 21.317 -33.034  -21.210 1.00 22.14  ? 559  LEU   A N      1 
ATOM   4421 C CA     . LEU   A  1 567 ? 21.740 -32.273  -20.044 1.00 22.32  ? 559  LEU   A CA     1 
ATOM   4422 C C      . LEU   A  1 567 ? 21.628 -30.787  -20.372 1.00 27.05  ? 559  LEU   A C      1 
ATOM   4423 O O      . LEU   A  1 567 ? 20.867 -30.053  -19.726 1.00 25.32  ? 559  LEU   A O      1 
ATOM   4424 C CB     . LEU   A  1 567 ? 23.164 -32.656  -19.589 1.00 22.80  ? 559  LEU   A CB     1 
ATOM   4425 C CG     . LEU   A  1 567 ? 23.380 -34.091  -19.088 1.00 27.69  ? 559  LEU   A CG     1 
ATOM   4426 C CD1    . LEU   A  1 567 ? 24.785 -34.266  -18.536 1.00 27.42  ? 559  LEU   A CD1    1 
ATOM   4427 C CD2    . LEU   A  1 567 ? 22.355 -34.475  -17.999 1.00 29.10  ? 559  LEU   A CD2    1 
ATOM   4428 N N      . TYR   A  1 568 ? 22.310 -30.372  -21.453 1.00 26.51  ? 560  TYR   A N      1 
ATOM   4429 C CA     . TYR   A  1 568 ? 22.288 -29.003  -21.969 1.00 26.40  ? 560  TYR   A CA     1 
ATOM   4430 C C      . TYR   A  1 568 ? 22.752 -29.022  -23.412 1.00 29.85  ? 560  TYR   A C      1 
ATOM   4431 O O      . TYR   A  1 568 ? 23.874 -29.449  -23.703 1.00 28.31  ? 560  TYR   A O      1 
ATOM   4432 C CB     . TYR   A  1 568 ? 23.162 -28.054  -21.115 1.00 27.45  ? 560  TYR   A CB     1 
ATOM   4433 C CG     . TYR   A  1 568 ? 22.998 -26.588  -21.464 1.00 29.89  ? 560  TYR   A CG     1 
ATOM   4434 C CD1    . TYR   A  1 568 ? 21.820 -25.905  -21.165 1.00 31.23  ? 560  TYR   A CD1    1 
ATOM   4435 C CD2    . TYR   A  1 568 ? 24.035 -25.871  -22.060 1.00 30.92  ? 560  TYR   A CD2    1 
ATOM   4436 C CE1    . TYR   A  1 568 ? 21.664 -24.554  -21.485 1.00 31.69  ? 560  TYR   A CE1    1 
ATOM   4437 C CE2    . TYR   A  1 568 ? 23.895 -24.517  -22.373 1.00 31.63  ? 560  TYR   A CE2    1 
ATOM   4438 C CZ     . TYR   A  1 568 ? 22.709 -23.862  -22.082 1.00 37.21  ? 560  TYR   A CZ     1 
ATOM   4439 O OH     . TYR   A  1 568 ? 22.578 -22.525  -22.370 1.00 36.77  ? 560  TYR   A OH     1 
ATOM   4440 N N      . GLN   A  1 569 ? 21.858 -28.612  -24.318 1.00 27.97  ? 561  GLN   A N      1 
ATOM   4441 C CA     . GLN   A  1 569 ? 22.111 -28.519  -25.764 1.00 28.38  ? 561  GLN   A CA     1 
ATOM   4442 C C      . GLN   A  1 569 ? 22.636 -29.833  -26.358 1.00 34.11  ? 561  GLN   A C      1 
ATOM   4443 O O      . GLN   A  1 569 ? 21.858 -30.775  -26.477 1.00 34.17  ? 561  GLN   A O      1 
ATOM   4444 C CB     . GLN   A  1 569 ? 23.025 -27.311  -26.084 1.00 29.01  ? 561  GLN   A CB     1 
ATOM   4445 C CG     . GLN   A  1 569 ? 22.346 -25.979  -25.751 1.00 34.80  ? 561  GLN   A CG     1 
ATOM   4446 C CD     . GLN   A  1 569 ? 23.238 -24.756  -25.801 1.00 39.73  ? 561  GLN   A CD     1 
ATOM   4447 O OE1    . GLN   A  1 569 ? 24.457 -24.829  -25.945 1.00 34.86  ? 561  GLN   A OE1    1 
ATOM   4448 N NE2    . GLN   A  1 569 ? 22.639 -23.597  -25.619 1.00 25.73  ? 561  GLN   A NE2    1 
ATOM   4449 N N      . ASP   A  1 570 ? 23.943 -29.908  -26.690 1.00 31.26  ? 562  ASP   A N      1 
ATOM   4450 C CA     . ASP   A  1 570 ? 24.574 -31.102  -27.264 1.00 31.31  ? 562  ASP   A CA     1 
ATOM   4451 C C      . ASP   A  1 570 ? 25.217 -32.005  -26.217 1.00 33.40  ? 562  ASP   A C      1 
ATOM   4452 O O      . ASP   A  1 570 ? 25.752 -33.060  -26.573 1.00 33.14  ? 562  ASP   A O      1 
ATOM   4453 C CB     . ASP   A  1 570 ? 25.611 -30.714  -28.340 1.00 33.87  ? 562  ASP   A CB     1 
ATOM   4454 C CG     . ASP   A  1 570 ? 26.783 -29.898  -27.820 1.00 44.95  ? 562  ASP   A CG     1 
ATOM   4455 O OD1    . ASP   A  1 570 ? 26.563 -29.028  -26.941 1.00 44.92  ? 562  ASP   A OD1    1 
ATOM   4456 O OD2    . ASP   A  1 570 ? 27.915 -30.104  -28.316 1.00 52.36  ? 562  ASP   A OD2    1 
ATOM   4457 N N      . ILE   A  1 571 ? 25.193 -31.584  -24.935 1.00 28.45  ? 563  ILE   A N      1 
ATOM   4458 C CA     . ILE   A  1 571 ? 25.739 -32.379  -23.837 1.00 27.24  ? 563  ILE   A CA     1 
ATOM   4459 C C      . ILE   A  1 571 ? 24.629 -33.334  -23.406 1.00 30.15  ? 563  ILE   A C      1 
ATOM   4460 O O      . ILE   A  1 571 ? 23.579 -32.900  -22.932 1.00 30.06  ? 563  ILE   A O      1 
ATOM   4461 C CB     . ILE   A  1 571 ? 26.316 -31.525  -22.674 1.00 29.94  ? 563  ILE   A CB     1 
ATOM   4462 C CG1    . ILE   A  1 571 ? 27.205 -30.340  -23.181 1.00 30.45  ? 563  ILE   A CG1    1 
ATOM   4463 C CG2    . ILE   A  1 571 ? 27.052 -32.405  -21.666 1.00 29.41  ? 563  ILE   A CG2    1 
ATOM   4464 C CD1    . ILE   A  1 571 ? 28.458 -30.728  -24.087 1.00 34.21  ? 563  ILE   A CD1    1 
ATOM   4465 N N      . THR   A  1 572 ? 24.830 -34.623  -23.681 1.00 25.66  ? 564  THR   A N      1 
ATOM   4466 C CA     . THR   A  1 572 ? 23.834 -35.653  -23.424 1.00 25.01  ? 564  THR   A CA     1 
ATOM   4467 C C      . THR   A  1 572 ? 24.420 -36.857  -22.700 1.00 27.41  ? 564  THR   A C      1 
ATOM   4468 O O      . THR   A  1 572 ? 25.642 -37.001  -22.596 1.00 27.31  ? 564  THR   A O      1 
ATOM   4469 C CB     . THR   A  1 572 ? 23.175 -36.116  -24.765 1.00 33.48  ? 564  THR   A CB     1 
ATOM   4470 O OG1    . THR   A  1 572 ? 24.125 -36.831  -25.548 1.00 32.78  ? 564  THR   A OG1    1 
ATOM   4471 C CG2    . THR   A  1 572 ? 22.554 -34.973  -25.578 1.00 29.59  ? 564  THR   A CG2    1 
ATOM   4472 N N      . LEU   A  1 573 ? 23.521 -37.726  -22.202 1.00 22.59  ? 565  LEU   A N      1 
ATOM   4473 C CA     . LEU   A  1 573 ? 23.827 -39.020  -21.598 1.00 21.92  ? 565  LEU   A CA     1 
ATOM   4474 C C      . LEU   A  1 573 ? 22.843 -40.022  -22.210 1.00 24.13  ? 565  LEU   A C      1 
ATOM   4475 O O      . LEU   A  1 573 ? 21.703 -39.664  -22.533 1.00 22.74  ? 565  LEU   A O      1 
ATOM   4476 C CB     . LEU   A  1 573 ? 23.684 -39.020  -20.061 1.00 22.14  ? 565  LEU   A CB     1 
ATOM   4477 C CG     . LEU   A  1 573 ? 24.580 -38.096  -19.229 1.00 25.77  ? 565  LEU   A CG     1 
ATOM   4478 C CD1    . LEU   A  1 573 ? 24.119 -38.087  -17.792 1.00 26.68  ? 565  LEU   A CD1    1 
ATOM   4479 C CD2    . LEU   A  1 573 ? 26.029 -38.538  -19.277 1.00 25.80  ? 565  LEU   A CD2    1 
ATOM   4480 N N      . SER   A  1 574 ? 23.288 -41.262  -22.385 1.00 20.38  ? 566  SER   A N      1 
ATOM   4481 C CA     . SER   A  1 574 ? 22.451 -42.301  -22.964 1.00 19.80  ? 566  SER   A CA     1 
ATOM   4482 C C      . SER   A  1 574 ? 22.798 -43.695  -22.464 1.00 23.37  ? 566  SER   A C      1 
ATOM   4483 O O      . SER   A  1 574 ? 23.976 -44.020  -22.318 1.00 22.69  ? 566  SER   A O      1 
ATOM   4484 C CB     . SER   A  1 574 ? 22.581 -42.275  -24.484 1.00 21.81  ? 566  SER   A CB     1 
ATOM   4485 O OG     . SER   A  1 574 ? 21.738 -43.243  -25.075 1.00 28.07  ? 566  SER   A OG     1 
ATOM   4486 N N      . ILE   A  1 575 ? 21.772 -44.538  -22.255 1.00 20.26  ? 567  ILE   A N      1 
ATOM   4487 C CA     . ILE   A  1 575 ? 21.994 -45.955  -21.943 1.00 20.18  ? 567  ILE   A CA     1 
ATOM   4488 C C      . ILE   A  1 575 ? 21.393 -46.834  -23.076 1.00 23.00  ? 567  ILE   A C      1 
ATOM   4489 O O      . ILE   A  1 575 ? 21.369 -48.060  -22.971 1.00 21.92  ? 567  ILE   A O      1 
ATOM   4490 C CB     . ILE   A  1 575 ? 21.606 -46.423  -20.502 1.00 23.11  ? 567  ILE   A CB     1 
ATOM   4491 C CG1    . ILE   A  1 575 ? 20.078 -46.504  -20.298 1.00 22.16  ? 567  ILE   A CG1    1 
ATOM   4492 C CG2    . ILE   A  1 575 ? 22.293 -45.561  -19.427 1.00 24.41  ? 567  ILE   A CG2    1 
ATOM   4493 C CD1    . ILE   A  1 575 ? 19.668 -47.427  -19.135 1.00 20.52  ? 567  ILE   A CD1    1 
ATOM   4494 N N      . ARG   A  1 576 ? 20.930 -46.199  -24.170 1.00 21.43  ? 568  ARG   A N      1 
ATOM   4495 C CA     . ARG   A  1 576 ? 20.429 -46.910  -25.360 1.00 21.69  ? 568  ARG   A CA     1 
ATOM   4496 C C      . ARG   A  1 576 ? 21.635 -47.672  -25.898 1.00 24.67  ? 568  ARG   A C      1 
ATOM   4497 O O      . ARG   A  1 576 ? 22.685 -47.046  -26.024 1.00 23.56  ? 568  ARG   A O      1 
ATOM   4498 C CB     . ARG   A  1 576 ? 20.040 -45.912  -26.442 1.00 21.89  ? 568  ARG   A CB     1 
ATOM   4499 C CG     . ARG   A  1 576 ? 18.644 -45.377  -26.403 1.00 32.24  ? 568  ARG   A CG     1 
ATOM   4500 C CD     . ARG   A  1 576 ? 18.556 -44.285  -27.458 1.00 39.87  ? 568  ARG   A CD     1 
ATOM   4501 N NE     . ARG   A  1 576 ? 18.401 -44.777  -28.829 1.00 39.89  ? 568  ARG   A NE     1 
ATOM   4502 C CZ     . ARG   A  1 576 ? 18.489 -44.014  -29.917 1.00 46.10  ? 568  ARG   A CZ     1 
ATOM   4503 N NH1    . ARG   A  1 576 ? 18.782 -42.722  -29.812 1.00 31.15  ? 568  ARG   A NH1    1 
ATOM   4504 N NH2    . ARG   A  1 576 ? 18.304 -44.539  -31.119 1.00 30.67  ? 568  ARG   A NH2    1 
ATOM   4505 N N      . PRO   A  1 577 ? 21.568 -48.984  -26.210 1.00 22.98  ? 569  PRO   A N      1 
ATOM   4506 C CA     . PRO   A  1 577 ? 22.788 -49.674  -26.689 1.00 23.49  ? 569  PRO   A CA     1 
ATOM   4507 C C      . PRO   A  1 577 ? 23.508 -49.002  -27.877 1.00 29.01  ? 569  PRO   A C      1 
ATOM   4508 O O      . PRO   A  1 577 ? 24.728 -48.895  -27.833 1.00 29.01  ? 569  PRO   A O      1 
ATOM   4509 C CB     . PRO   A  1 577 ? 22.297 -51.087  -27.015 1.00 24.70  ? 569  PRO   A CB     1 
ATOM   4510 C CG     . PRO   A  1 577 ? 21.098 -51.271  -26.118 1.00 29.08  ? 569  PRO   A CG     1 
ATOM   4511 C CD     . PRO   A  1 577 ? 20.427 -49.919  -26.111 1.00 24.34  ? 569  PRO   A CD     1 
ATOM   4512 N N      . GLU   A  1 578 ? 22.763 -48.492  -28.876 1.00 27.29  ? 570  GLU   A N      1 
ATOM   4513 C CA     . GLU   A  1 578 ? 23.309 -47.850  -30.088 1.00 28.31  ? 570  GLU   A CA     1 
ATOM   4514 C C      . GLU   A  1 578 ? 24.069 -46.540  -29.820 1.00 31.35  ? 570  GLU   A C      1 
ATOM   4515 O O      . GLU   A  1 578 ? 24.991 -46.219  -30.571 1.00 30.85  ? 570  GLU   A O      1 
ATOM   4516 C CB     . GLU   A  1 578 ? 22.235 -47.582  -31.180 1.00 30.18  ? 570  GLU   A CB     1 
ATOM   4517 C CG     . GLU   A  1 578 ? 21.057 -48.532  -31.281 1.00 43.94  ? 570  GLU   A CG     1 
ATOM   4518 C CD     . GLU   A  1 578 ? 19.957 -48.191  -30.296 1.00 64.11  ? 570  GLU   A CD     1 
ATOM   4519 O OE1    . GLU   A  1 578 ? 19.997 -48.744  -29.176 1.00 37.61  ? 570  GLU   A OE1    1 
ATOM   4520 O OE2    . GLU   A  1 578 ? 19.114 -47.316  -30.602 1.00 62.78  ? 570  GLU   A OE2    1 
ATOM   4521 N N      . THR   A  1 579 ? 23.663 -45.771  -28.790 1.00 26.95  ? 571  THR   A N      1 
ATOM   4522 C CA     . THR   A  1 579 ? 24.285 -44.483  -28.461 1.00 26.06  ? 571  THR   A CA     1 
ATOM   4523 C C      . THR   A  1 579 ? 24.845 -44.442  -27.030 1.00 30.05  ? 571  THR   A C      1 
ATOM   4524 O O      . THR   A  1 579 ? 25.058 -43.347  -26.499 1.00 30.35  ? 571  THR   A O      1 
ATOM   4525 C CB     . THR   A  1 579 ? 23.271 -43.336  -28.670 1.00 31.81  ? 571  THR   A CB     1 
ATOM   4526 O OG1    . THR   A  1 579 ? 22.141 -43.518  -27.805 1.00 29.40  ? 571  THR   A OG1    1 
ATOM   4527 C CG2    . THR   A  1 579 ? 22.821 -43.188  -30.118 1.00 26.74  ? 571  THR   A CG2    1 
ATOM   4528 N N      . HIS   A  1 580 ? 25.076 -45.616  -26.404 1.00 25.83  ? 572  HIS   A N      1 
ATOM   4529 C CA     . HIS   A  1 580 ? 25.534 -45.711  -25.016 1.00 24.75  ? 572  HIS   A CA     1 
ATOM   4530 C C      . HIS   A  1 580 ? 26.736 -44.821  -24.698 1.00 29.04  ? 572  HIS   A C      1 
ATOM   4531 O O      . HIS   A  1 580 ? 27.715 -44.832  -25.447 1.00 29.86  ? 572  HIS   A O      1 
ATOM   4532 C CB     . HIS   A  1 580 ? 25.810 -47.169  -24.607 1.00 24.81  ? 572  HIS   A CB     1 
ATOM   4533 C CG     . HIS   A  1 580 ? 25.618 -47.430  -23.138 1.00 27.55  ? 572  HIS   A CG     1 
ATOM   4534 N ND1    . HIS   A  1 580 ? 26.429 -46.838  -22.181 1.00 28.69  ? 572  HIS   A ND1    1 
ATOM   4535 C CD2    . HIS   A  1 580 ? 24.709 -48.215  -22.512 1.00 28.59  ? 572  HIS   A CD2    1 
ATOM   4536 C CE1    . HIS   A  1 580 ? 25.976 -47.265  -21.015 1.00 27.84  ? 572  HIS   A CE1    1 
ATOM   4537 N NE2    . HIS   A  1 580 ? 24.947 -48.098  -21.164 1.00 28.09  ? 572  HIS   A NE2    1 
ATOM   4538 N N      . SER   A  1 581 ? 26.637 -44.026  -23.607 1.00 24.49  ? 573  SER   A N      1 
ATOM   4539 C CA     . SER   A  1 581 ? 27.710 -43.148  -23.134 1.00 23.83  ? 573  SER   A CA     1 
ATOM   4540 C C      . SER   A  1 581 ? 28.860 -44.056  -22.660 1.00 30.15  ? 573  SER   A C      1 
ATOM   4541 O O      . SER   A  1 581 ? 28.600 -44.998  -21.897 1.00 28.27  ? 573  SER   A O      1 
ATOM   4542 C CB     . SER   A  1 581 ? 27.223 -42.259  -21.995 1.00 24.19  ? 573  SER   A CB     1 
ATOM   4543 O OG     . SER   A  1 581 ? 26.250 -41.345  -22.463 1.00 27.98  ? 573  SER   A OG     1 
ATOM   4544 N N      . PRO   A  1 582 ? 30.108 -43.853  -23.171 1.00 28.98  ? 574  PRO   A N      1 
ATOM   4545 C CA     . PRO   A  1 582 ? 31.214 -44.775  -22.823 1.00 28.59  ? 574  PRO   A CA     1 
ATOM   4546 C C      . PRO   A  1 582 ? 31.577 -44.845  -21.344 1.00 31.59  ? 574  PRO   A C      1 
ATOM   4547 O O      . PRO   A  1 582 ? 31.678 -43.823  -20.671 1.00 31.09  ? 574  PRO   A O      1 
ATOM   4548 C CB     . PRO   A  1 582 ? 32.387 -44.273  -23.680 1.00 30.70  ? 574  PRO   A CB     1 
ATOM   4549 C CG     . PRO   A  1 582 ? 31.762 -43.465  -24.769 1.00 35.35  ? 574  PRO   A CG     1 
ATOM   4550 C CD     . PRO   A  1 582 ? 30.553 -42.833  -24.144 1.00 30.94  ? 574  PRO   A CD     1 
ATOM   4551 N N      . GLY   A  1 583 ? 31.743 -46.073  -20.861 1.00 28.03  ? 575  GLY   A N      1 
ATOM   4552 C CA     . GLY   A  1 583 ? 32.106 -46.380  -19.484 1.00 27.72  ? 575  GLY   A CA     1 
ATOM   4553 C C      . GLY   A  1 583 ? 31.035 -46.111  -18.445 1.00 29.49  ? 575  GLY   A C      1 
ATOM   4554 O O      . GLY   A  1 583 ? 31.250 -46.427  -17.278 1.00 28.44  ? 575  GLY   A O      1 
ATOM   4555 N N      . MET   A  1 584 ? 29.880 -45.524  -18.850 1.00 25.04  ? 576  MET   A N      1 
ATOM   4556 C CA     . MET   A  1 584 ? 28.793 -45.163  -17.938 1.00 24.31  ? 576  MET   A CA     1 
ATOM   4557 C C      . MET   A  1 584 ? 28.050 -46.376  -17.383 1.00 28.32  ? 576  MET   A C      1 
ATOM   4558 O O      . MET   A  1 584 ? 27.219 -46.946  -18.077 1.00 28.60  ? 576  MET   A O      1 
ATOM   4559 C CB     . MET   A  1 584 ? 27.820 -44.185  -18.609 1.00 26.26  ? 576  MET   A CB     1 
ATOM   4560 C CG     . MET   A  1 584 ? 26.885 -43.520  -17.622 1.00 29.34  ? 576  MET   A CG     1 
ATOM   4561 S SD     . MET   A  1 584 ? 26.035 -42.109  -18.327 1.00 32.98  ? 576  MET   A SD     1 
ATOM   4562 C CE     . MET   A  1 584 ? 24.699 -42.902  -19.154 1.00 29.42  ? 576  MET   A CE     1 
ATOM   4563 N N      . PHE   A  1 585 ? 28.328 -46.740  -16.125 1.00 24.32  ? 577  PHE   A N      1 
ATOM   4564 C CA     . PHE   A  1 585 ? 27.695 -47.869  -15.434 1.00 22.83  ? 577  PHE   A CA     1 
ATOM   4565 C C      . PHE   A  1 585 ? 26.586 -47.417  -14.441 1.00 23.67  ? 577  PHE   A C      1 
ATOM   4566 O O      . PHE   A  1 585 ? 25.967 -48.263  -13.794 1.00 23.35  ? 577  PHE   A O      1 
ATOM   4567 C CB     . PHE   A  1 585 ? 28.766 -48.700  -14.707 1.00 24.45  ? 577  PHE   A CB     1 
ATOM   4568 C CG     . PHE   A  1 585 ? 29.517 -47.957  -13.621 1.00 26.14  ? 577  PHE   A CG     1 
ATOM   4569 C CD1    . PHE   A  1 585 ? 28.959 -47.784  -12.356 1.00 28.43  ? 577  PHE   A CD1    1 
ATOM   4570 C CD2    . PHE   A  1 585 ? 30.787 -47.438  -13.860 1.00 27.96  ? 577  PHE   A CD2    1 
ATOM   4571 C CE1    . PHE   A  1 585 ? 29.643 -47.077  -11.360 1.00 29.21  ? 577  PHE   A CE1    1 
ATOM   4572 C CE2    . PHE   A  1 585 ? 31.483 -46.757  -12.855 1.00 30.18  ? 577  PHE   A CE2    1 
ATOM   4573 C CZ     . PHE   A  1 585 ? 30.906 -46.581  -11.612 1.00 28.37  ? 577  PHE   A CZ     1 
ATOM   4574 N N      . SER   A  1 586 ? 26.343 -46.103  -14.322 1.00 18.58  ? 578  SER   A N      1 
ATOM   4575 C CA     . SER   A  1 586 ? 25.383 -45.536  -13.363 1.00 18.87  ? 578  SER   A CA     1 
ATOM   4576 C C      . SER   A  1 586 ? 23.940 -46.001  -13.552 1.00 23.83  ? 578  SER   A C      1 
ATOM   4577 O O      . SER   A  1 586 ? 23.128 -45.863  -12.636 1.00 23.23  ? 578  SER   A O      1 
ATOM   4578 C CB     . SER   A  1 586 ? 25.464 -44.019  -13.347 1.00 20.99  ? 578  SER   A CB     1 
ATOM   4579 O OG     . SER   A  1 586 ? 26.636 -43.665  -12.639 1.00 24.96  ? 578  SER   A OG     1 
ATOM   4580 N N      . TRP   A  1 587 ? 23.630 -46.567  -14.719 1.00 19.84  ? 579  TRP   A N      1 
ATOM   4581 C CA     . TRP   A  1 587 ? 22.321 -47.116  -15.000 1.00 19.42  ? 579  TRP   A CA     1 
ATOM   4582 C C      . TRP   A  1 587 ? 22.435 -48.401  -15.782 1.00 23.40  ? 579  TRP   A C      1 
ATOM   4583 O O      . TRP   A  1 587 ? 23.090 -48.457  -16.824 1.00 23.48  ? 579  TRP   A O      1 
ATOM   4584 C CB     . TRP   A  1 587 ? 21.435 -46.140  -15.775 1.00 18.03  ? 579  TRP   A CB     1 
ATOM   4585 C CG     . TRP   A  1 587 ? 21.114 -44.864  -15.063 1.00 19.28  ? 579  TRP   A CG     1 
ATOM   4586 C CD1    . TRP   A  1 587 ? 20.007 -44.602  -14.316 1.00 21.77  ? 579  TRP   A CD1    1 
ATOM   4587 C CD2    . TRP   A  1 587 ? 21.815 -43.619  -15.191 1.00 19.83  ? 579  TRP   A CD2    1 
ATOM   4588 N NE1    . TRP   A  1 587 ? 20.014 -43.294  -13.903 1.00 21.47  ? 579  TRP   A NE1    1 
ATOM   4589 C CE2    . TRP   A  1 587 ? 21.108 -42.662  -14.433 1.00 23.52  ? 579  TRP   A CE2    1 
ATOM   4590 C CE3    . TRP   A  1 587 ? 22.958 -43.211  -15.905 1.00 21.44  ? 579  TRP   A CE3    1 
ATOM   4591 C CZ2    . TRP   A  1 587 ? 21.514 -41.325  -14.349 1.00 23.24  ? 579  TRP   A CZ2    1 
ATOM   4592 C CZ3    . TRP   A  1 587 ? 23.373 -41.893  -15.804 1.00 22.94  ? 579  TRP   A CZ3    1 
ATOM   4593 C CH2    . TRP   A  1 587 ? 22.655 -40.965  -15.034 1.00 23.73  ? 579  TRP   A CH2    1 
ATOM   4594 N N      . PHE   A  1 588 ? 21.768 -49.428  -15.288 1.00 19.84  ? 580  PHE   A N      1 
ATOM   4595 C CA     . PHE   A  1 588 ? 21.631 -50.688  -15.990 1.00 18.53  ? 580  PHE   A CA     1 
ATOM   4596 C C      . PHE   A  1 588 ? 20.271 -50.606  -16.651 1.00 22.25  ? 580  PHE   A C      1 
ATOM   4597 O O      . PHE   A  1 588 ? 19.447 -49.820  -16.187 1.00 21.50  ? 580  PHE   A O      1 
ATOM   4598 C CB     . PHE   A  1 588 ? 21.642 -51.864  -15.005 1.00 19.67  ? 580  PHE   A CB     1 
ATOM   4599 C CG     . PHE   A  1 588 ? 23.004 -52.350  -14.581 1.00 20.99  ? 580  PHE   A CG     1 
ATOM   4600 C CD1    . PHE   A  1 588 ? 24.125 -52.118  -15.374 1.00 23.55  ? 580  PHE   A CD1    1 
ATOM   4601 C CD2    . PHE   A  1 588 ? 23.161 -53.095  -13.418 1.00 22.85  ? 580  PHE   A CD2    1 
ATOM   4602 C CE1    . PHE   A  1 588 ? 25.380 -52.581  -14.985 1.00 24.52  ? 580  PHE   A CE1    1 
ATOM   4603 C CE2    . PHE   A  1 588 ? 24.422 -53.562  -13.034 1.00 25.19  ? 580  PHE   A CE2    1 
ATOM   4604 C CZ     . PHE   A  1 588 ? 25.520 -53.301  -13.820 1.00 22.69  ? 580  PHE   A CZ     1 
ATOM   4605 N N      . PRO   A  1 589 ? 19.976 -51.415  -17.689 1.00 18.64  ? 581  PRO   A N      1 
ATOM   4606 C CA     . PRO   A  1 589 ? 18.629 -51.383  -18.276 1.00 18.88  ? 581  PRO   A CA     1 
ATOM   4607 C C      . PRO   A  1 589 ? 17.525 -51.885  -17.327 1.00 21.88  ? 581  PRO   A C      1 
ATOM   4608 O O      . PRO   A  1 589 ? 17.786 -52.502  -16.291 1.00 19.92  ? 581  PRO   A O      1 
ATOM   4609 C CB     . PRO   A  1 589 ? 18.747 -52.326  -19.487 1.00 20.50  ? 581  PRO   A CB     1 
ATOM   4610 C CG     . PRO   A  1 589 ? 20.204 -52.502  -19.722 1.00 24.80  ? 581  PRO   A CG     1 
ATOM   4611 C CD     . PRO   A  1 589 ? 20.841 -52.389  -18.387 1.00 20.25  ? 581  PRO   A CD     1 
ATOM   4612 N N      . ILE   A  1 590 ? 16.279 -51.608  -17.698 1.00 19.49  ? 582  ILE   A N      1 
ATOM   4613 C CA     . ILE   A  1 590 ? 15.135 -52.083  -16.945 1.00 19.95  ? 582  ILE   A CA     1 
ATOM   4614 C C      . ILE   A  1 590 ? 14.465 -53.196  -17.754 1.00 21.73  ? 582  ILE   A C      1 
ATOM   4615 O O      . ILE   A  1 590 ? 14.586 -53.227  -18.981 1.00 21.49  ? 582  ILE   A O      1 
ATOM   4616 C CB     . ILE   A  1 590 ? 14.191 -50.926  -16.535 1.00 24.53  ? 582  ILE   A CB     1 
ATOM   4617 C CG1    . ILE   A  1 590 ? 13.459 -51.230  -15.223 1.00 26.43  ? 582  ILE   A CG1    1 
ATOM   4618 C CG2    . ILE   A  1 590 ? 13.226 -50.505  -17.641 1.00 25.08  ? 582  ILE   A CG2    1 
ATOM   4619 C CD1    . ILE   A  1 590 ? 13.252 -50.041  -14.341 1.00 37.28  ? 582  ILE   A CD1    1 
ATOM   4620 N N      . LEU   A  1 591 ? 13.816 -54.129  -17.074 1.00 17.10  ? 583  LEU   A N      1 
ATOM   4621 C CA     . LEU   A  1 591 ? 13.093 -55.188  -17.747 1.00 16.13  ? 583  LEU   A CA     1 
ATOM   4622 C C      . LEU   A  1 591 ? 11.649 -55.200  -17.261 1.00 17.73  ? 583  LEU   A C      1 
ATOM   4623 O O      . LEU   A  1 591 ? 11.410 -55.376  -16.075 1.00 15.89  ? 583  LEU   A O      1 
ATOM   4624 C CB     . LEU   A  1 591 ? 13.755 -56.557  -17.516 1.00 16.22  ? 583  LEU   A CB     1 
ATOM   4625 C CG     . LEU   A  1 591 ? 12.976 -57.813  -17.988 1.00 19.81  ? 583  LEU   A CG     1 
ATOM   4626 C CD1    . LEU   A  1 591 ? 12.925 -57.913  -19.506 1.00 19.12  ? 583  LEU   A CD1    1 
ATOM   4627 C CD2    . LEU   A  1 591 ? 13.578 -59.064  -17.402 1.00 22.74  ? 583  LEU   A CD2    1 
ATOM   4628 N N      . PHE   A  1 592 ? 10.707 -55.040  -18.196 1.00 14.69  ? 584  PHE   A N      1 
ATOM   4629 C CA     . PHE   A  1 592 ? 9.277  -55.169  -17.961 1.00 14.47  ? 584  PHE   A CA     1 
ATOM   4630 C C      . PHE   A  1 592 ? 8.926  -56.572  -18.452 1.00 18.99  ? 584  PHE   A C      1 
ATOM   4631 O O      . PHE   A  1 592 ? 8.943  -56.808  -19.657 1.00 18.29  ? 584  PHE   A O      1 
ATOM   4632 C CB     . PHE   A  1 592 ? 8.464  -54.120  -18.736 1.00 15.10  ? 584  PHE   A CB     1 
ATOM   4633 C CG     . PHE   A  1 592 ? 8.603  -52.743  -18.159 1.00 15.79  ? 584  PHE   A CG     1 
ATOM   4634 C CD1    . PHE   A  1 592 ? 7.776  -52.317  -17.126 1.00 18.42  ? 584  PHE   A CD1    1 
ATOM   4635 C CD2    . PHE   A  1 592 ? 9.557  -51.858  -18.653 1.00 17.02  ? 584  PHE   A CD2    1 
ATOM   4636 C CE1    . PHE   A  1 592 ? 7.898  -51.032  -16.596 1.00 18.27  ? 584  PHE   A CE1    1 
ATOM   4637 C CE2    . PHE   A  1 592 ? 9.695  -50.580  -18.102 1.00 18.53  ? 584  PHE   A CE2    1 
ATOM   4638 C CZ     . PHE   A  1 592 ? 8.869  -50.179  -17.078 1.00 16.13  ? 584  PHE   A CZ     1 
ATOM   4639 N N      . PRO   A  1 593 ? 8.659  -57.534  -17.555 1.00 16.61  ? 585  PRO   A N      1 
ATOM   4640 C CA     . PRO   A  1 593 ? 8.306  -58.872  -18.035 1.00 17.09  ? 585  PRO   A CA     1 
ATOM   4641 C C      . PRO   A  1 593 ? 6.851  -58.967  -18.482 1.00 21.59  ? 585  PRO   A C      1 
ATOM   4642 O O      . PRO   A  1 593 ? 6.074  -58.031  -18.279 1.00 19.79  ? 585  PRO   A O      1 
ATOM   4643 C CB     . PRO   A  1 593 ? 8.561  -59.768  -16.817 1.00 18.42  ? 585  PRO   A CB     1 
ATOM   4644 C CG     . PRO   A  1 593 ? 8.656  -58.856  -15.629 1.00 23.52  ? 585  PRO   A CG     1 
ATOM   4645 C CD     . PRO   A  1 593 ? 8.564  -57.436  -16.087 1.00 18.75  ? 585  PRO   A CD     1 
ATOM   4646 N N      . ILE   A  1 594 ? 6.495  -60.099  -19.105 1.00 19.01  ? 586  ILE   A N      1 
ATOM   4647 C CA     . ILE   A  1 594 ? 5.121  -60.468  -19.452 1.00 19.86  ? 586  ILE   A CA     1 
ATOM   4648 C C      . ILE   A  1 594 ? 4.838  -61.844  -18.816 1.00 23.73  ? 586  ILE   A C      1 
ATOM   4649 O O      . ILE   A  1 594 ? 5.752  -62.660  -18.763 1.00 23.17  ? 586  ILE   A O      1 
ATOM   4650 C CB     . ILE   A  1 594 ? 4.738  -60.329  -20.949 1.00 23.44  ? 586  ILE   A CB     1 
ATOM   4651 C CG1    . ILE   A  1 594 ? 5.590  -61.250  -21.870 1.00 24.03  ? 586  ILE   A CG1    1 
ATOM   4652 C CG2    . ILE   A  1 594 ? 4.782  -58.855  -21.392 1.00 24.22  ? 586  ILE   A CG2    1 
ATOM   4653 C CD1    . ILE   A  1 594 ? 5.065  -61.357  -23.331 1.00 27.08  ? 586  ILE   A CD1    1 
ATOM   4654 N N      . LYS   A  1 595 ? 3.625  -62.059  -18.249 1.00 22.27  ? 587  LYS   A N      1 
ATOM   4655 C CA     . LYS   A  1 595 ? 3.229  -63.288  -17.524 1.00 23.29  ? 587  LYS   A CA     1 
ATOM   4656 C C      . LYS   A  1 595 ? 3.408  -64.575  -18.326 1.00 28.14  ? 587  LYS   A C      1 
ATOM   4657 O O      . LYS   A  1 595 ? 3.864  -65.584  -17.779 1.00 28.74  ? 587  LYS   A O      1 
ATOM   4658 C CB     . LYS   A  1 595 ? 1.774  -63.215  -17.033 1.00 26.25  ? 587  LYS   A CB     1 
ATOM   4659 C CG     . LYS   A  1 595 ? 1.521  -62.299  -15.856 1.00 39.76  ? 587  LYS   A CG     1 
ATOM   4660 C CD     . LYS   A  1 595 ? 0.042  -62.303  -15.509 1.00 46.96  ? 587  LYS   A CD     1 
ATOM   4661 C CE     . LYS   A  1 595 ? -0.269 -61.530  -14.252 1.00 53.45  ? 587  LYS   A CE     1 
ATOM   4662 N NZ     . LYS   A  1 595 ? -1.716 -61.601  -13.914 1.00 62.41  ? 587  LYS   A NZ     1 
ATOM   4663 N N      . GLN   A  1 596 ? 3.018  -64.538  -19.605 1.00 23.67  ? 588  GLN   A N      1 
ATOM   4664 C CA     . GLN   A  1 596 ? 3.087  -65.667  -20.518 1.00 22.92  ? 588  GLN   A CA     1 
ATOM   4665 C C      . GLN   A  1 596 ? 3.919  -65.365  -21.755 1.00 25.68  ? 588  GLN   A C      1 
ATOM   4666 O O      . GLN   A  1 596 ? 3.650  -64.386  -22.457 1.00 25.15  ? 588  GLN   A O      1 
ATOM   4667 C CB     . GLN   A  1 596 ? 1.672  -66.138  -20.931 1.00 24.22  ? 588  GLN   A CB     1 
ATOM   4668 C CG     . GLN   A  1 596 ? 0.886  -66.836  -19.810 1.00 35.07  ? 588  GLN   A CG     1 
ATOM   4669 C CD     . GLN   A  1 596 ? 1.556  -68.105  -19.321 1.00 52.56  ? 588  GLN   A CD     1 
ATOM   4670 O OE1    . GLN   A  1 596 ? 2.082  -68.905  -20.103 1.00 46.10  ? 588  GLN   A OE1    1 
ATOM   4671 N NE2    . GLN   A  1 596 ? 1.549  -68.316  -18.012 1.00 46.03  ? 588  GLN   A NE2    1 
ATOM   4672 N N      . PRO   A  1 597 ? 4.910  -66.227  -22.067 1.00 23.14  ? 589  PRO   A N      1 
ATOM   4673 C CA     . PRO   A  1 597 ? 5.689  -66.048  -23.315 1.00 23.05  ? 589  PRO   A CA     1 
ATOM   4674 C C      . PRO   A  1 597 ? 4.793  -66.007  -24.568 1.00 26.22  ? 589  PRO   A C      1 
ATOM   4675 O O      . PRO   A  1 597 ? 3.796  -66.725  -24.628 1.00 26.49  ? 589  PRO   A O      1 
ATOM   4676 C CB     . PRO   A  1 597 ? 6.596  -67.285  -23.337 1.00 24.63  ? 589  PRO   A CB     1 
ATOM   4677 C CG     . PRO   A  1 597 ? 6.660  -67.744  -21.924 1.00 29.03  ? 589  PRO   A CG     1 
ATOM   4678 C CD     . PRO   A  1 597 ? 5.311  -67.458  -21.356 1.00 24.13  ? 589  PRO   A CD     1 
ATOM   4679 N N      . ILE   A  1 598 ? 5.126  -65.143  -25.542 1.00 21.37  ? 590  ILE   A N      1 
ATOM   4680 C CA     . ILE   A  1 598 ? 4.359  -64.976  -26.778 1.00 21.50  ? 590  ILE   A CA     1 
ATOM   4681 C C      . ILE   A  1 598 ? 5.179  -65.356  -28.004 1.00 24.86  ? 590  ILE   A C      1 
ATOM   4682 O O      . ILE   A  1 598 ? 6.237  -64.770  -28.252 1.00 23.40  ? 590  ILE   A O      1 
ATOM   4683 C CB     . ILE   A  1 598 ? 3.763  -63.532  -26.888 1.00 23.91  ? 590  ILE   A CB     1 
ATOM   4684 C CG1    . ILE   A  1 598 ? 2.676  -63.293  -25.809 1.00 23.34  ? 590  ILE   A CG1    1 
ATOM   4685 C CG2    . ILE   A  1 598 ? 3.239  -63.217  -28.320 1.00 24.22  ? 590  ILE   A CG2    1 
ATOM   4686 C CD1    . ILE   A  1 598 ? 2.187  -61.820  -25.690 1.00 24.11  ? 590  ILE   A CD1    1 
ATOM   4687 N N      . THR   A  1 599 ? 4.649  -66.294  -28.803 1.00 22.18  ? 591  THR   A N      1 
ATOM   4688 C CA     . THR   A  1 599 ? 5.250  -66.740  -30.061 1.00 21.56  ? 591  THR   A CA     1 
ATOM   4689 C C      . THR   A  1 599 ? 5.114  -65.657  -31.121 1.00 25.36  ? 591  THR   A C      1 
ATOM   4690 O O      . THR   A  1 599 ? 4.024  -65.114  -31.314 1.00 24.74  ? 591  THR   A O      1 
ATOM   4691 C CB     . THR   A  1 599 ? 4.614  -68.076  -30.499 1.00 30.82  ? 591  THR   A CB     1 
ATOM   4692 O OG1    . THR   A  1 599 ? 4.988  -69.074  -29.559 1.00 30.93  ? 591  THR   A OG1    1 
ATOM   4693 C CG2    . THR   A  1 599 ? 5.052  -68.520  -31.900 1.00 31.80  ? 591  THR   A CG2    1 
ATOM   4694 N N      . VAL   A  1 600 ? 6.235  -65.326  -31.785 1.00 21.95  ? 592  VAL   A N      1 
ATOM   4695 C CA     . VAL   A  1 600 ? 6.281  -64.326  -32.845 1.00 22.67  ? 592  VAL   A CA     1 
ATOM   4696 C C      . VAL   A  1 600 ? 6.963  -64.963  -34.061 1.00 28.22  ? 592  VAL   A C      1 
ATOM   4697 O O      . VAL   A  1 600 ? 8.062  -65.508  -33.943 1.00 28.08  ? 592  VAL   A O      1 
ATOM   4698 C CB     . VAL   A  1 600 ? 6.970  -62.997  -32.425 1.00 26.31  ? 592  VAL   A CB     1 
ATOM   4699 C CG1    . VAL   A  1 600 ? 6.892  -61.958  -33.548 1.00 26.42  ? 592  VAL   A CG1    1 
ATOM   4700 C CG2    . VAL   A  1 600 ? 6.366  -62.437  -31.137 1.00 26.14  ? 592  VAL   A CG2    1 
ATOM   4701 N N      . ARG   A  1 601 ? 6.306  -64.890  -35.217 1.00 25.18  ? 593  ARG   A N      1 
ATOM   4702 C CA     . ARG   A  1 601 ? 6.841  -65.437  -36.455 1.00 25.23  ? 593  ARG   A CA     1 
ATOM   4703 C C      . ARG   A  1 601 ? 7.491  -64.328  -37.259 1.00 30.31  ? 593  ARG   A C      1 
ATOM   4704 O O      . ARG   A  1 601 ? 7.156  -63.152  -37.075 1.00 28.86  ? 593  ARG   A O      1 
ATOM   4705 C CB     . ARG   A  1 601 ? 5.735  -66.105  -37.280 1.00 25.08  ? 593  ARG   A CB     1 
ATOM   4706 C CG     . ARG   A  1 601 ? 5.003  -67.234  -36.565 1.00 36.05  ? 593  ARG   A CG     1 
ATOM   4707 C CD     . ARG   A  1 601 ? 4.004  -67.936  -37.482 1.00 59.86  ? 593  ARG   A CD     1 
ATOM   4708 N NE     . ARG   A  1 601 ? 2.830  -67.109  -37.788 1.00 79.73  ? 593  ARG   A NE     1 
ATOM   4709 C CZ     . ARG   A  1 601 ? 2.619  -66.489  -38.948 1.00 98.35  ? 593  ARG   A CZ     1 
ATOM   4710 N NH1    . ARG   A  1 601 ? 3.500  -66.595  -39.937 1.00 85.65  ? 593  ARG   A NH1    1 
ATOM   4711 N NH2    . ARG   A  1 601 ? 1.527  -65.757  -39.127 1.00 86.75  ? 593  ARG   A NH2    1 
ATOM   4712 N N      . GLU   A  1 602 ? 8.407  -64.703  -38.173 1.00 28.03  ? 594  GLU   A N      1 
ATOM   4713 C CA     . GLU   A  1 602 ? 9.106  -63.771  -39.054 1.00 28.34  ? 594  GLU   A CA     1 
ATOM   4714 C C      . GLU   A  1 602 ? 8.091  -62.879  -39.822 1.00 30.74  ? 594  GLU   A C      1 
ATOM   4715 O O      . GLU   A  1 602 ? 7.092  -63.380  -40.335 1.00 30.77  ? 594  GLU   A O      1 
ATOM   4716 C CB     . GLU   A  1 602 ? 9.997  -64.565  -40.033 1.00 30.07  ? 594  GLU   A CB     1 
ATOM   4717 C CG     . GLU   A  1 602 ? 10.977 -63.698  -40.811 1.00 47.15  ? 594  GLU   A CG     1 
ATOM   4718 C CD     . GLU   A  1 602 ? 11.507 -64.252  -42.124 1.00 78.51  ? 594  GLU   A CD     1 
ATOM   4719 O OE1    . GLU   A  1 602 ? 11.155 -65.397  -42.492 1.00 82.94  ? 594  GLU   A OE1    1 
ATOM   4720 O OE2    . GLU   A  1 602 ? 12.279 -63.526  -42.793 1.00 72.80  ? 594  GLU   A OE2    1 
ATOM   4721 N N      . GLY   A  1 603 ? 8.348  -61.577  -39.858 1.00 26.39  ? 595  GLY   A N      1 
ATOM   4722 C CA     . GLY   A  1 603 ? 7.490  -60.616  -40.545 1.00 26.42  ? 595  GLY   A CA     1 
ATOM   4723 C C      . GLY   A  1 603 ? 6.339  -60.064  -39.726 1.00 30.69  ? 595  GLY   A C      1 
ATOM   4724 O O      . GLY   A  1 603 ? 5.663  -59.139  -40.173 1.00 31.27  ? 595  GLY   A O      1 
ATOM   4725 N N      . GLN   A  1 604 ? 6.081  -60.628  -38.538 1.00 26.86  ? 596  GLN   A N      1 
ATOM   4726 C CA     . GLN   A  1 604 ? 5.006  -60.140  -37.665 1.00 25.64  ? 596  GLN   A CA     1 
ATOM   4727 C C      . GLN   A  1 604 ? 5.450  -58.887  -36.905 1.00 29.24  ? 596  GLN   A C      1 
ATOM   4728 O O      . GLN   A  1 604 ? 6.652  -58.634  -36.754 1.00 28.52  ? 596  GLN   A O      1 
ATOM   4729 C CB     . GLN   A  1 604 ? 4.549  -61.222  -36.688 1.00 26.10  ? 596  GLN   A CB     1 
ATOM   4730 C CG     . GLN   A  1 604 ? 3.693  -62.314  -37.319 1.00 29.84  ? 596  GLN   A CG     1 
ATOM   4731 C CD     . GLN   A  1 604 ? 3.084  -63.240  -36.294 1.00 38.57  ? 596  GLN   A CD     1 
ATOM   4732 O OE1    . GLN   A  1 604 ? 3.721  -63.641  -35.307 1.00 30.97  ? 596  GLN   A OE1    1 
ATOM   4733 N NE2    . GLN   A  1 604 ? 1.841  -63.629  -36.524 1.00 33.70  ? 596  GLN   A NE2    1 
ATOM   4734 N N      . THR   A  1 605 ? 4.474  -58.098  -36.444 1.00 25.71  ? 597  THR   A N      1 
ATOM   4735 C CA     . THR   A  1 605 ? 4.718  -56.884  -35.671 1.00 25.03  ? 597  THR   A CA     1 
ATOM   4736 C C      . THR   A  1 605 ? 4.324  -57.100  -34.209 1.00 26.18  ? 597  THR   A C      1 
ATOM   4737 O O      . THR   A  1 605 ? 3.241  -57.618  -33.929 1.00 24.56  ? 597  THR   A O      1 
ATOM   4738 C CB     . THR   A  1 605 ? 4.004  -55.686  -36.326 1.00 35.85  ? 597  THR   A CB     1 
ATOM   4739 O OG1    . THR   A  1 605 ? 4.609  -55.457  -37.593 1.00 41.03  ? 597  THR   A OG1    1 
ATOM   4740 C CG2    . THR   A  1 605 ? 4.100  -54.399  -35.499 1.00 34.27  ? 597  THR   A CG2    1 
ATOM   4741 N N      . ILE   A  1 606 ? 5.215  -56.717  -33.279 1.00 21.72  ? 598  ILE   A N      1 
ATOM   4742 C CA     . ILE   A  1 606 ? 4.903  -56.754  -31.849 1.00 20.57  ? 598  ILE   A CA     1 
ATOM   4743 C C      . ILE   A  1 606 ? 4.299  -55.391  -31.527 1.00 24.02  ? 598  ILE   A C      1 
ATOM   4744 O O      . ILE   A  1 606 ? 4.931  -54.375  -31.798 1.00 22.92  ? 598  ILE   A O      1 
ATOM   4745 C CB     . ILE   A  1 606 ? 6.123  -57.086  -30.929 1.00 22.42  ? 598  ILE   A CB     1 
ATOM   4746 C CG1    . ILE   A  1 606 ? 6.557  -58.554  -31.130 1.00 22.11  ? 598  ILE   A CG1    1 
ATOM   4747 C CG2    . ILE   A  1 606 ? 5.788  -56.803  -29.426 1.00 21.87  ? 598  ILE   A CG2    1 
ATOM   4748 C CD1    . ILE   A  1 606 ? 7.854  -59.001  -30.414 1.00 21.62  ? 598  ILE   A CD1    1 
ATOM   4749 N N      . CYS   A  1 607 ? 3.068  -55.362  -31.009 1.00 21.90  ? 599  CYS   A N      1 
ATOM   4750 C CA     . CYS   A  1 607 ? 2.454  -54.095  -30.602 1.00 22.80  ? 599  CYS   A CA     1 
ATOM   4751 C C      . CYS   A  1 607 ? 2.356  -54.079  -29.082 1.00 23.87  ? 599  CYS   A C      1 
ATOM   4752 O O      . CYS   A  1 607 ? 1.769  -54.985  -28.494 1.00 21.77  ? 599  CYS   A O      1 
ATOM   4753 C CB     . CYS   A  1 607 ? 1.093  -53.863  -31.257 1.00 24.70  ? 599  CYS   A CB     1 
ATOM   4754 S SG     . CYS   A  1 607 ? 0.317  -52.283  -30.804 1.00 30.00  ? 599  CYS   A SG     1 
ATOM   4755 N N      . VAL   A  1 608 ? 2.961  -53.067  -28.454 1.00 20.93  ? 600  VAL   A N      1 
ATOM   4756 C CA     . VAL   A  1 608 ? 2.923  -52.904  -27.011 1.00 20.45  ? 600  VAL   A CA     1 
ATOM   4757 C C      . VAL   A  1 608 ? 2.336  -51.536  -26.669 1.00 22.60  ? 600  VAL   A C      1 
ATOM   4758 O O      . VAL   A  1 608 ? 2.525  -50.566  -27.404 1.00 20.45  ? 600  VAL   A O      1 
ATOM   4759 C CB     . VAL   A  1 608 ? 4.283  -53.198  -26.313 1.00 24.34  ? 600  VAL   A CB     1 
ATOM   4760 C CG1    . VAL   A  1 608 ? 5.277  -52.055  -26.486 1.00 24.32  ? 600  VAL   A CG1    1 
ATOM   4761 C CG2    . VAL   A  1 608 ? 4.094  -53.528  -24.833 1.00 24.18  ? 600  VAL   A CG2    1 
ATOM   4762 N N      . ARG   A  1 609 ? 1.596  -51.491  -25.567 1.00 19.07  ? 601  ARG   A N      1 
ATOM   4763 C CA     . ARG   A  1 609 ? 0.993  -50.282  -25.034 1.00 18.20  ? 601  ARG   A CA     1 
ATOM   4764 C C      . ARG   A  1 609 ? 1.533  -50.108  -23.638 1.00 20.47  ? 601  ARG   A C      1 
ATOM   4765 O O      . ARG   A  1 609 ? 1.533  -51.058  -22.867 1.00 18.74  ? 601  ARG   A O      1 
ATOM   4766 C CB     . ARG   A  1 609 ? -0.538 -50.388  -24.946 1.00 21.22  ? 601  ARG   A CB     1 
ATOM   4767 C CG     . ARG   A  1 609 ? -1.234 -51.171  -26.040 1.00 29.55  ? 601  ARG   A CG     1 
ATOM   4768 C CD     . ARG   A  1 609 ? -1.606 -50.278  -27.186 1.00 31.91  ? 601  ARG   A CD     1 
ATOM   4769 N NE     . ARG   A  1 609 ? -2.216 -51.040  -28.266 1.00 27.67  ? 601  ARG   A NE     1 
ATOM   4770 C CZ     . ARG   A  1 609 ? -3.246 -50.612  -28.981 1.00 40.18  ? 601  ARG   A CZ     1 
ATOM   4771 N NH1    . ARG   A  1 609 ? -3.786 -49.425  -28.732 1.00 24.08  ? 601  ARG   A NH1    1 
ATOM   4772 N NH2    . ARG   A  1 609 ? -3.749 -51.367  -29.947 1.00 28.21  ? 601  ARG   A NH2    1 
ATOM   4773 N N      . PHE   A  1 610 ? 2.013  -48.910  -23.320 1.00 18.26  ? 602  PHE   A N      1 
ATOM   4774 C CA     . PHE   A  1 610 ? 2.503  -48.568  -21.996 1.00 18.57  ? 602  PHE   A CA     1 
ATOM   4775 C C      . PHE   A  1 610 ? 1.756  -47.346  -21.511 1.00 22.19  ? 602  PHE   A C      1 
ATOM   4776 O O      . PHE   A  1 610 ? 1.514  -46.411  -22.282 1.00 20.98  ? 602  PHE   A O      1 
ATOM   4777 C CB     . PHE   A  1 610 ? 4.027  -48.297  -22.003 1.00 20.02  ? 602  PHE   A CB     1 
ATOM   4778 C CG     . PHE   A  1 610 ? 4.884  -49.477  -21.598 1.00 20.79  ? 602  PHE   A CG     1 
ATOM   4779 C CD1    . PHE   A  1 610 ? 5.074  -50.551  -22.462 1.00 23.60  ? 602  PHE   A CD1    1 
ATOM   4780 C CD2    . PHE   A  1 610 ? 5.550  -49.486  -20.379 1.00 22.32  ? 602  PHE   A CD2    1 
ATOM   4781 C CE1    . PHE   A  1 610 ? 5.899  -51.623  -22.100 1.00 24.35  ? 602  PHE   A CE1    1 
ATOM   4782 C CE2    . PHE   A  1 610 ? 6.357  -50.565  -20.010 1.00 24.40  ? 602  PHE   A CE2    1 
ATOM   4783 C CZ     . PHE   A  1 610 ? 6.539  -51.620  -20.877 1.00 22.52  ? 602  PHE   A CZ     1 
ATOM   4784 N N      . TRP   A  1 611 ? 1.400  -47.355  -20.228 1.00 20.18  ? 603  TRP   A N      1 
ATOM   4785 C CA     . TRP   A  1 611 ? 0.753  -46.238  -19.557 1.00 19.85  ? 603  TRP   A CA     1 
ATOM   4786 C C      . TRP   A  1 611 ? 1.577  -45.827  -18.345 1.00 23.52  ? 603  TRP   A C      1 
ATOM   4787 O O      . TRP   A  1 611 ? 2.017  -46.685  -17.583 1.00 21.73  ? 603  TRP   A O      1 
ATOM   4788 C CB     . TRP   A  1 611 ? -0.656 -46.624  -19.071 1.00 18.51  ? 603  TRP   A CB     1 
ATOM   4789 C CG     . TRP   A  1 611 ? -1.658 -46.924  -20.148 1.00 20.14  ? 603  TRP   A CG     1 
ATOM   4790 C CD1    . TRP   A  1 611 ? -2.573 -46.063  -20.683 1.00 22.97  ? 603  TRP   A CD1    1 
ATOM   4791 C CD2    . TRP   A  1 611 ? -1.886 -48.194  -20.773 1.00 20.50  ? 603  TRP   A CD2    1 
ATOM   4792 N NE1    . TRP   A  1 611 ? -3.365 -46.722  -21.597 1.00 22.63  ? 603  TRP   A NE1    1 
ATOM   4793 C CE2    . TRP   A  1 611 ? -2.968 -48.033  -21.667 1.00 24.48  ? 603  TRP   A CE2    1 
ATOM   4794 C CE3    . TRP   A  1 611 ? -1.319 -49.472  -20.619 1.00 22.37  ? 603  TRP   A CE3    1 
ATOM   4795 C CZ2    . TRP   A  1 611 ? -3.484 -49.097  -22.413 1.00 23.97  ? 603  TRP   A CZ2    1 
ATOM   4796 C CZ3    . TRP   A  1 611 ? -1.815 -50.517  -21.377 1.00 23.93  ? 603  TRP   A CZ3    1 
ATOM   4797 C CH2    . TRP   A  1 611 ? -2.894 -50.327  -22.250 1.00 24.54  ? 603  TRP   A CH2    1 
ATOM   4798 N N      . ARG   A  1 612 ? 1.763  -44.517  -18.151 1.00 20.06  ? 604  ARG   A N      1 
ATOM   4799 C CA     . ARG   A  1 612 ? 2.361  -43.981  -16.931 1.00 19.01  ? 604  ARG   A CA     1 
ATOM   4800 C C      . ARG   A  1 612 ? 1.145  -43.443  -16.179 1.00 22.63  ? 604  ARG   A C      1 
ATOM   4801 O O      . ARG   A  1 612 ? 0.406  -42.620  -16.716 1.00 20.90  ? 604  ARG   A O      1 
ATOM   4802 C CB     . ARG   A  1 612 ? 3.371  -42.862  -17.193 1.00 17.49  ? 604  ARG   A CB     1 
ATOM   4803 C CG     . ARG   A  1 612 ? 4.242  -42.562  -15.965 1.00 18.37  ? 604  ARG   A CG     1 
ATOM   4804 C CD     . ARG   A  1 612 ? 5.154  -41.397  -16.262 1.00 20.89  ? 604  ARG   A CD     1 
ATOM   4805 N NE     . ARG   A  1 612 ? 6.192  -41.203  -15.250 1.00 19.60  ? 604  ARG   A NE     1 
ATOM   4806 C CZ     . ARG   A  1 612 ? 6.097  -40.377  -14.213 1.00 26.92  ? 604  ARG   A CZ     1 
ATOM   4807 N NH1    . ARG   A  1 612 ? 4.982  -39.698  -14.000 1.00 13.35  ? 604  ARG   A NH1    1 
ATOM   4808 N NH2    . ARG   A  1 612 ? 7.110  -40.243  -13.368 1.00 13.20  ? 604  ARG   A NH2    1 
ATOM   4809 N N      . CYS   A  1 613 ? 0.879  -43.993  -15.002 1.00 19.72  ? 605  CYS   A N      1 
ATOM   4810 C CA     . CYS   A  1 613 ? -0.287 -43.627  -14.194 1.00 21.04  ? 605  CYS   A CA     1 
ATOM   4811 C C      . CYS   A  1 613 ? 0.144  -43.053  -12.863 1.00 24.44  ? 605  CYS   A C      1 
ATOM   4812 O O      . CYS   A  1 613 ? 1.284  -43.267  -12.443 1.00 23.28  ? 605  CYS   A O      1 
ATOM   4813 C CB     . CYS   A  1 613 ? -1.230 -44.815  -14.008 1.00 21.90  ? 605  CYS   A CB     1 
ATOM   4814 S SG     . CYS   A  1 613 ? -1.505 -45.789  -15.511 1.00 26.46  ? 605  CYS   A SG     1 
ATOM   4815 N N      . SER   A  1 614 ? -0.772 -42.324  -12.202 1.00 21.75  ? 606  SER   A N      1 
ATOM   4816 C CA     . SER   A  1 614 ? -0.525 -41.684  -10.921 1.00 22.00  ? 606  SER   A CA     1 
ATOM   4817 C C      . SER   A  1 614 ? -1.784 -41.211  -10.205 1.00 28.78  ? 606  SER   A C      1 
ATOM   4818 O O      . SER   A  1 614 ? -2.859 -41.071  -10.793 1.00 29.24  ? 606  SER   A O      1 
ATOM   4819 C CB     . SER   A  1 614 ? 0.414  -40.489  -11.091 1.00 24.16  ? 606  SER   A CB     1 
ATOM   4820 O OG     . SER   A  1 614 ? -0.212 -39.432  -11.800 1.00 32.26  ? 606  SER   A OG     1 
ATOM   4821 N N      . ASN   A  1 615 ? -1.610 -40.975  -8.909  1.00 25.79  ? 607  ASN   A N      1 
ATOM   4822 C CA     . ASN   A  1 615 ? -2.520 -40.327  -7.984  1.00 25.33  ? 607  ASN   A CA     1 
ATOM   4823 C C      . ASN   A  1 615 ? -1.603 -39.445  -7.126  1.00 30.03  ? 607  ASN   A C      1 
ATOM   4824 O O      . ASN   A  1 615 ? -0.416 -39.318  -7.456  1.00 29.60  ? 607  ASN   A O      1 
ATOM   4825 C CB     . ASN   A  1 615 ? -3.394 -41.323  -7.203  1.00 22.47  ? 607  ASN   A CB     1 
ATOM   4826 C CG     . ASN   A  1 615 ? -2.698 -42.348  -6.343  1.00 37.48  ? 607  ASN   A CG     1 
ATOM   4827 O OD1    . ASN   A  1 615 ? -1.636 -42.123  -5.743  1.00 29.76  ? 607  ASN   A OD1    1 
ATOM   4828 N ND2    . ASN   A  1 615 ? -3.363 -43.474  -6.166  1.00 29.80  ? 607  ASN   A ND2    1 
ATOM   4829 N N      . SER   A  1 616 ? -2.120 -38.811  -6.076  1.00 27.85  ? 608  SER   A N      1 
ATOM   4830 C CA     . SER   A  1 616 ? -1.313 -37.931  -5.224  1.00 28.03  ? 608  SER   A CA     1 
ATOM   4831 C C      . SER   A  1 616 ? -0.282 -38.687  -4.364  1.00 31.29  ? 608  SER   A C      1 
ATOM   4832 O O      . SER   A  1 616 ? 0.711  -38.093  -3.935  1.00 31.61  ? 608  SER   A O      1 
ATOM   4833 C CB     . SER   A  1 616 ? -2.220 -37.082  -4.337  1.00 32.32  ? 608  SER   A CB     1 
ATOM   4834 O OG     . SER   A  1 616 ? -3.095 -37.915  -3.592  1.00 43.77  ? 608  SER   A OG     1 
ATOM   4835 N N      . LYS   A  1 617 ? -0.494 -39.994  -4.151  1.00 26.16  ? 609  LYS   A N      1 
ATOM   4836 C CA     . LYS   A  1 617 ? 0.368  -40.822  -3.306  1.00 25.04  ? 609  LYS   A CA     1 
ATOM   4837 C C      . LYS   A  1 617 ? 1.430  -41.636  -4.043  1.00 27.19  ? 609  LYS   A C      1 
ATOM   4838 O O      . LYS   A  1 617 ? 2.480  -41.931  -3.462  1.00 25.17  ? 609  LYS   A O      1 
ATOM   4839 C CB     . LYS   A  1 617 ? -0.492 -41.770  -2.462  1.00 27.00  ? 609  LYS   A CB     1 
ATOM   4840 C CG     . LYS   A  1 617 ? -1.449 -41.057  -1.509  1.00 32.70  ? 609  LYS   A CG     1 
ATOM   4841 C CD     . LYS   A  1 617 ? -2.558 -42.000  -1.123  1.00 39.14  ? 609  LYS   A CD     1 
ATOM   4842 C CE     . LYS   A  1 617 ? -3.151 -41.644  0.206   1.00 43.46  ? 609  LYS   A CE     1 
ATOM   4843 N NZ     . LYS   A  1 617 ? -4.114 -42.683  0.657   1.00 51.49  ? 609  LYS   A NZ     1 
ATOM   4844 N N      . LYS   A  1 618 ? 1.141  -42.063  -5.284  1.00 23.34  ? 610  LYS   A N      1 
ATOM   4845 C CA     . LYS   A  1 618 ? 2.076  -42.926  -6.011  1.00 22.51  ? 610  LYS   A CA     1 
ATOM   4846 C C      . LYS   A  1 618 ? 1.999  -42.800  -7.524  1.00 23.23  ? 610  LYS   A C      1 
ATOM   4847 O O      . LYS   A  1 618 ? 1.090  -42.173  -8.056  1.00 22.39  ? 610  LYS   A O      1 
ATOM   4848 C CB     . LYS   A  1 618 ? 1.913  -44.393  -5.575  1.00 23.92  ? 610  LYS   A CB     1 
ATOM   4849 C CG     . LYS   A  1 618 ? 0.505  -44.940  -5.729  1.00 33.75  ? 610  LYS   A CG     1 
ATOM   4850 C CD     . LYS   A  1 618 ? 0.175  -45.941  -4.648  1.00 42.06  ? 610  LYS   A CD     1 
ATOM   4851 C CE     . LYS   A  1 618 ? -1.180 -46.551  -4.920  1.00 60.33  ? 610  LYS   A CE     1 
ATOM   4852 N NZ     . LYS   A  1 618 ? -1.534 -47.608  -3.934  1.00 70.62  ? 610  LYS   A NZ     1 
ATOM   4853 N N      . VAL   A  1 619 ? 2.999  -43.382  -8.199  1.00 18.50  ? 611  VAL   A N      1 
ATOM   4854 C CA     . VAL   A  1 619 ? 3.161  -43.421  -9.644  1.00 17.59  ? 611  VAL   A CA     1 
ATOM   4855 C C      . VAL   A  1 619 ? 3.433  -44.874  -10.015 1.00 20.23  ? 611  VAL   A C      1 
ATOM   4856 O O      . VAL   A  1 619 ? 4.145  -45.572  -9.288  1.00 19.50  ? 611  VAL   A O      1 
ATOM   4857 C CB     . VAL   A  1 619 ? 4.322  -42.489  -10.115 1.00 21.27  ? 611  VAL   A CB     1 
ATOM   4858 C CG1    . VAL   A  1 619 ? 4.604  -42.636  -11.618 1.00 20.51  ? 611  VAL   A CG1    1 
ATOM   4859 C CG2    . VAL   A  1 619 ? 4.035  -41.027  -9.774  1.00 21.32  ? 611  VAL   A CG2    1 
ATOM   4860 N N      . TRP   A  1 620 ? 2.922  -45.310  -11.169 1.00 17.34  ? 612  TRP   A N      1 
ATOM   4861 C CA     . TRP   A  1 620 ? 3.174  -46.667  -11.652 1.00 17.30  ? 612  TRP   A CA     1 
ATOM   4862 C C      . TRP   A  1 620 ? 3.021  -46.794  -13.170 1.00 19.81  ? 612  TRP   A C      1 
ATOM   4863 O O      . TRP   A  1 620 ? 2.607  -45.854  -13.859 1.00 18.79  ? 612  TRP   A O      1 
ATOM   4864 C CB     . TRP   A  1 620 ? 2.292  -47.695  -10.910 1.00 15.46  ? 612  TRP   A CB     1 
ATOM   4865 C CG     . TRP   A  1 620 ? 0.833  -47.567  -11.237 1.00 16.29  ? 612  TRP   A CG     1 
ATOM   4866 C CD1    . TRP   A  1 620 ? 0.136  -48.285  -12.167 1.00 19.16  ? 612  TRP   A CD1    1 
ATOM   4867 C CD2    . TRP   A  1 620 ? -0.097 -46.641  -10.664 1.00 16.05  ? 612  TRP   A CD2    1 
ATOM   4868 N NE1    . TRP   A  1 620 ? -1.177 -47.888  -12.184 1.00 18.71  ? 612  TRP   A NE1    1 
ATOM   4869 C CE2    . TRP   A  1 620 ? -1.355 -46.890  -11.258 1.00 20.05  ? 612  TRP   A CE2    1 
ATOM   4870 C CE3    . TRP   A  1 620 ? -0.019 -45.700  -9.620  1.00 17.30  ? 612  TRP   A CE3    1 
ATOM   4871 C CZ2    . TRP   A  1 620 ? -2.511 -46.183  -10.895 1.00 18.94  ? 612  TRP   A CZ2    1 
ATOM   4872 C CZ3    . TRP   A  1 620 ? -1.157 -44.978  -9.284  1.00 18.85  ? 612  TRP   A CZ3    1 
ATOM   4873 C CH2    . TRP   A  1 620 ? -2.385 -45.225  -9.917  1.00 19.34  ? 612  TRP   A CH2    1 
ATOM   4874 N N      . TYR   A  1 621 ? 3.398  -47.956  -13.689 1.00 16.18  ? 613  TYR   A N      1 
ATOM   4875 C CA     . TYR   A  1 621 ? 3.233  -48.244  -15.095 1.00 15.91  ? 613  TYR   A CA     1 
ATOM   4876 C C      . TYR   A  1 621 ? 2.278  -49.377  -15.247 1.00 19.52  ? 613  TYR   A C      1 
ATOM   4877 O O      . TYR   A  1 621 ? 2.252  -50.279  -14.418 1.00 18.26  ? 613  TYR   A O      1 
ATOM   4878 C CB     . TYR   A  1 621 ? 4.560  -48.645  -15.766 1.00 17.21  ? 613  TYR   A CB     1 
ATOM   4879 C CG     . TYR   A  1 621 ? 5.641  -47.598  -15.692 1.00 19.53  ? 613  TYR   A CG     1 
ATOM   4880 C CD1    . TYR   A  1 621 ? 5.665  -46.529  -16.581 1.00 20.74  ? 613  TYR   A CD1    1 
ATOM   4881 C CD2    . TYR   A  1 621 ? 6.670  -47.698  -14.762 1.00 21.99  ? 613  TYR   A CD2    1 
ATOM   4882 C CE1    . TYR   A  1 621 ? 6.654  -45.550  -16.506 1.00 22.47  ? 613  TYR   A CE1    1 
ATOM   4883 C CE2    . TYR   A  1 621 ? 7.673  -46.734  -14.687 1.00 23.61  ? 613  TYR   A CE2    1 
ATOM   4884 C CZ     . TYR   A  1 621 ? 7.662  -45.663  -15.562 1.00 30.71  ? 613  TYR   A CZ     1 
ATOM   4885 O OH     . TYR   A  1 621 ? 8.670  -44.736  -15.498 1.00 33.96  ? 613  TYR   A OH     1 
ATOM   4886 N N      . GLU   A  1 622 ? 1.532  -49.360  -16.348 1.00 17.69  ? 614  GLU   A N      1 
ATOM   4887 C CA     . GLU   A  1 622 ? 0.687  -50.458  -16.791 1.00 18.19  ? 614  GLU   A CA     1 
ATOM   4888 C C      . GLU   A  1 622 ? 1.135  -50.757  -18.231 1.00 20.31  ? 614  GLU   A C      1 
ATOM   4889 O O      . GLU   A  1 622 ? 1.569  -49.848  -18.943 1.00 19.47  ? 614  GLU   A O      1 
ATOM   4890 C CB     . GLU   A  1 622 ? -0.807 -50.117  -16.699 1.00 19.84  ? 614  GLU   A CB     1 
ATOM   4891 C CG     . GLU   A  1 622 ? -1.241 -49.817  -15.269 1.00 27.60  ? 614  GLU   A CG     1 
ATOM   4892 C CD     . GLU   A  1 622 ? -2.708 -49.518  -15.024 1.00 43.66  ? 614  GLU   A CD     1 
ATOM   4893 O OE1    . GLU   A  1 622 ? -3.538 -49.828  -15.905 1.00 36.37  ? 614  GLU   A OE1    1 
ATOM   4894 O OE2    . GLU   A  1 622 ? -3.037 -49.040  -13.914 1.00 33.65  ? 614  GLU   A OE2    1 
ATOM   4895 N N      . TRP   A  1 623 ? 1.129  -52.025  -18.620 1.00 16.28  ? 615  TRP   A N      1 
ATOM   4896 C CA     . TRP   A  1 623 ? 1.555  -52.411  -19.959 1.00 16.56  ? 615  TRP   A CA     1 
ATOM   4897 C C      . TRP   A  1 623 ? 0.806  -53.622  -20.481 1.00 19.44  ? 615  TRP   A C      1 
ATOM   4898 O O      . TRP   A  1 623 ? 0.334  -54.439  -19.694 1.00 17.57  ? 615  TRP   A O      1 
ATOM   4899 C CB     . TRP   A  1 623 ? 3.090  -52.600  -20.050 1.00 15.50  ? 615  TRP   A CB     1 
ATOM   4900 C CG     . TRP   A  1 623 ? 3.668  -53.715  -19.216 1.00 16.04  ? 615  TRP   A CG     1 
ATOM   4901 C CD1    . TRP   A  1 623 ? 4.066  -54.942  -19.664 1.00 19.00  ? 615  TRP   A CD1    1 
ATOM   4902 C CD2    . TRP   A  1 623 ? 4.081  -53.637  -17.842 1.00 15.96  ? 615  TRP   A CD2    1 
ATOM   4903 N NE1    . TRP   A  1 623 ? 4.638  -55.660  -18.635 1.00 18.71  ? 615  TRP   A NE1    1 
ATOM   4904 C CE2    . TRP   A  1 623 ? 4.656  -54.885  -17.504 1.00 19.88  ? 615  TRP   A CE2    1 
ATOM   4905 C CE3    . TRP   A  1 623 ? 4.002  -52.639  -16.850 1.00 17.15  ? 615  TRP   A CE3    1 
ATOM   4906 C CZ2    . TRP   A  1 623 ? 5.120  -55.173  -16.210 1.00 19.08  ? 615  TRP   A CZ2    1 
ATOM   4907 C CZ3    . TRP   A  1 623 ? 4.466  -52.924  -15.573 1.00 18.70  ? 615  TRP   A CZ3    1 
ATOM   4908 C CH2    . TRP   A  1 623 ? 5.018  -54.179  -15.265 1.00 19.34  ? 615  TRP   A CH2    1 
ATOM   4909 N N      . ALA   A  1 624 ? 0.678  -53.714  -21.812 1.00 17.84  ? 616  ALA   A N      1 
ATOM   4910 C CA     . ALA   A  1 624 ? 0.020  -54.833  -22.486 1.00 18.23  ? 616  ALA   A CA     1 
ATOM   4911 C C      . ALA   A  1 624 ? 0.519  -55.005  -23.911 1.00 20.61  ? 616  ALA   A C      1 
ATOM   4912 O O      . ALA   A  1 624 ? 0.827  -54.024  -24.587 1.00 19.03  ? 616  ALA   A O      1 
ATOM   4913 C CB     . ALA   A  1 624 ? -1.492 -54.650  -22.483 1.00 19.06  ? 616  ALA   A CB     1 
ATOM   4914 N N      . VAL   A  1 625 ? 0.574  -56.266  -24.364 1.00 18.38  ? 617  VAL   A N      1 
ATOM   4915 C CA     . VAL   A  1 625 ? 0.920  -56.657  -25.737 1.00 17.58  ? 617  VAL   A CA     1 
ATOM   4916 C C      . VAL   A  1 625 ? -0.444 -56.817  -26.445 1.00 22.29  ? 617  VAL   A C      1 
ATOM   4917 O O      . VAL   A  1 625 ? -1.334 -57.441  -25.880 1.00 21.22  ? 617  VAL   A O      1 
ATOM   4918 C CB     . VAL   A  1 625 ? 1.765  -57.969  -25.781 1.00 21.08  ? 617  VAL   A CB     1 
ATOM   4919 C CG1    . VAL   A  1 625 ? 2.045  -58.412  -27.226 1.00 20.45  ? 617  VAL   A CG1    1 
ATOM   4920 C CG2    . VAL   A  1 625 ? 3.078  -57.798  -25.021 1.00 21.17  ? 617  VAL   A CG2    1 
ATOM   4921 N N      . THR   A  1 626 ? -0.623 -56.220  -27.636 1.00 20.71  ? 618  THR   A N      1 
ATOM   4922 C CA     . THR   A  1 626 ? -1.891 -56.306  -28.375 1.00 20.78  ? 618  THR   A CA     1 
ATOM   4923 C C      . THR   A  1 626 ? -1.746 -57.051  -29.723 1.00 25.97  ? 618  THR   A C      1 
ATOM   4924 O O      . THR   A  1 626 ? -2.755 -57.457  -30.311 1.00 26.75  ? 618  THR   A O      1 
ATOM   4925 C CB     . THR   A  1 626 ? -2.540 -54.922  -28.520 1.00 23.62  ? 618  THR   A CB     1 
ATOM   4926 O OG1    . THR   A  1 626 ? -1.594 -54.014  -29.072 1.00 23.44  ? 618  THR   A OG1    1 
ATOM   4927 C CG2    . THR   A  1 626 ? -3.052 -54.374  -27.186 1.00 19.80  ? 618  THR   A CG2    1 
ATOM   4928 N N      . ALA   A  1 627 ? -0.501 -57.250  -30.195 1.00 21.67  ? 619  ALA   A N      1 
ATOM   4929 C CA     . ALA   A  1 627 ? -0.192 -57.995  -31.430 1.00 21.07  ? 619  ALA   A CA     1 
ATOM   4930 C C      . ALA   A  1 627 ? 1.174  -58.695  -31.265 1.00 26.55  ? 619  ALA   A C      1 
ATOM   4931 O O      . ALA   A  1 627 ? 2.033  -58.131  -30.579 1.00 24.82  ? 619  ALA   A O      1 
ATOM   4932 C CB     . ALA   A  1 627 ? -0.180 -57.057  -32.635 1.00 21.49  ? 619  ALA   A CB     1 
ATOM   4933 N N      . PRO   A  1 628 ? 1.411  -59.922  -31.824 1.00 25.47  ? 620  PRO   A N      1 
ATOM   4934 C CA     . PRO   A  1 628 ? 0.509  -60.752  -32.657 1.00 25.93  ? 620  PRO   A CA     1 
ATOM   4935 C C      . PRO   A  1 628 ? -0.702 -61.300  -31.890 1.00 31.39  ? 620  PRO   A C      1 
ATOM   4936 O O      . PRO   A  1 628 ? -1.703 -61.648  -32.512 1.00 31.79  ? 620  PRO   A O      1 
ATOM   4937 C CB     . PRO   A  1 628 ? 1.442  -61.853  -33.185 1.00 27.04  ? 620  PRO   A CB     1 
ATOM   4938 C CG     . PRO   A  1 628 ? 2.483  -61.992  -32.124 1.00 30.56  ? 620  PRO   A CG     1 
ATOM   4939 C CD     . PRO   A  1 628 ? 2.719  -60.585  -31.639 1.00 26.04  ? 620  PRO   A CD     1 
ATOM   4940 N N      . VAL   A  1 629 ? -0.583 -61.420  -30.553 1.00 27.89  ? 621  VAL   A N      1 
ATOM   4941 C CA     . VAL   A  1 629 ? -1.657 -61.830  -29.632 1.00 27.57  ? 621  VAL   A CA     1 
ATOM   4942 C C      . VAL   A  1 629 ? -1.732 -60.847  -28.471 1.00 31.28  ? 621  VAL   A C      1 
ATOM   4943 O O      . VAL   A  1 629 ? -0.761 -60.123  -28.227 1.00 30.40  ? 621  VAL   A O      1 
ATOM   4944 C CB     . VAL   A  1 629 ? -1.657 -63.312  -29.160 1.00 31.17  ? 621  VAL   A CB     1 
ATOM   4945 C CG1    . VAL   A  1 629 ? -1.798 -64.284  -30.336 1.00 31.25  ? 621  VAL   A CG1    1 
ATOM   4946 C CG2    . VAL   A  1 629 ? -0.445 -63.643  -28.297 1.00 30.56  ? 621  VAL   A CG2    1 
ATOM   4947 N N      . CYS   A  1 630 ? -2.889 -60.797  -27.779 1.00 27.46  ? 622  CYS   A N      1 
ATOM   4948 C CA     . CYS   A  1 630 ? -3.069 -59.935  -26.615 1.00 26.98  ? 622  CYS   A CA     1 
ATOM   4949 C C      . CYS   A  1 630 ? -2.557 -60.644  -25.383 1.00 27.35  ? 622  CYS   A C      1 
ATOM   4950 O O      . CYS   A  1 630 ? -2.698 -61.860  -25.243 1.00 26.35  ? 622  CYS   A O      1 
ATOM   4951 C CB     . CYS   A  1 630 ? -4.528 -59.515  -26.435 1.00 27.93  ? 622  CYS   A CB     1 
ATOM   4952 S SG     . CYS   A  1 630 ? -5.026 -58.082  -27.424 1.00 32.88  ? 622  CYS   A SG     1 
ATOM   4953 N N      . SER   A  1 631 ? -1.965 -59.879  -24.488 1.00 21.60  ? 623  SER   A N      1 
ATOM   4954 C CA     . SER   A  1 631 ? -1.585 -60.366  -23.174 1.00 20.86  ? 623  SER   A CA     1 
ATOM   4955 C C      . SER   A  1 631 ? -2.646 -59.756  -22.250 1.00 23.17  ? 623  SER   A C      1 
ATOM   4956 O O      . SER   A  1 631 ? -3.459 -58.934  -22.694 1.00 21.49  ? 623  SER   A O      1 
ATOM   4957 C CB     . SER   A  1 631 ? -0.205 -59.832  -22.788 1.00 22.10  ? 623  SER   A CB     1 
ATOM   4958 O OG     . SER   A  1 631 ? -0.216 -58.426  -22.596 1.00 21.12  ? 623  SER   A OG     1 
ATOM   4959 N N      . ALA   A  1 632 ? -2.609 -60.115  -20.975 1.00 19.47  ? 624  ALA   A N      1 
ATOM   4960 C CA     . ALA   A  1 632 ? -3.410 -59.475  -19.929 1.00 18.99  ? 624  ALA   A CA     1 
ATOM   4961 C C      . ALA   A  1 632 ? -2.798 -58.075  -19.712 1.00 21.93  ? 624  ALA   A C      1 
ATOM   4962 O O      . ALA   A  1 632 ? -1.619 -57.868  -20.015 1.00 21.16  ? 624  ALA   A O      1 
ATOM   4963 C CB     . ALA   A  1 632 ? -3.270 -60.269  -18.640 1.00 19.50  ? 624  ALA   A CB     1 
ATOM   4964 N N      . ILE   A  1 633 ? -3.575 -57.116  -19.196 1.00 19.20  ? 625  ILE   A N      1 
ATOM   4965 C CA     . ILE   A  1 633 ? -3.014 -55.812  -18.825 1.00 18.26  ? 625  ILE   A CA     1 
ATOM   4966 C C      . ILE   A  1 633 ? -2.163 -56.112  -17.562 1.00 20.37  ? 625  ILE   A C      1 
ATOM   4967 O O      . ILE   A  1 633 ? -2.633 -56.791  -16.647 1.00 19.06  ? 625  ILE   A O      1 
ATOM   4968 C CB     . ILE   A  1 633 ? -4.114 -54.735  -18.568 1.00 21.97  ? 625  ILE   A CB     1 
ATOM   4969 C CG1    . ILE   A  1 633 ? -4.738 -54.270  -19.909 1.00 24.41  ? 625  ILE   A CG1    1 
ATOM   4970 C CG2    . ILE   A  1 633 ? -3.546 -53.524  -17.794 1.00 21.68  ? 625  ILE   A CG2    1 
ATOM   4971 C CD1    . ILE   A  1 633 ? -6.179 -53.946  -19.842 1.00 35.72  ? 625  ILE   A CD1    1 
ATOM   4972 N N      . HIS   A  1 634 ? -0.901 -55.676  -17.571 1.00 16.34  ? 626  HIS   A N      1 
ATOM   4973 C CA     . HIS   A  1 634 ? 0.024  -55.903  -16.487 1.00 16.02  ? 626  HIS   A CA     1 
ATOM   4974 C C      . HIS   A  1 634 ? 0.014  -54.736  -15.551 1.00 19.86  ? 626  HIS   A C      1 
ATOM   4975 O O      . HIS   A  1 634 ? -0.048 -53.588  -15.993 1.00 17.78  ? 626  HIS   A O      1 
ATOM   4976 C CB     . HIS   A  1 634 ? 1.438  -56.163  -17.017 1.00 16.70  ? 626  HIS   A CB     1 
ATOM   4977 C CG     . HIS   A  1 634 ? 1.613  -57.542  -17.573 1.00 19.87  ? 626  HIS   A CG     1 
ATOM   4978 N ND1    . HIS   A  1 634 ? 0.827  -58.008  -18.616 1.00 21.13  ? 626  HIS   A ND1    1 
ATOM   4979 C CD2    . HIS   A  1 634 ? 2.475  -58.518  -17.206 1.00 21.47  ? 626  HIS   A CD2    1 
ATOM   4980 C CE1    . HIS   A  1 634 ? 1.229  -59.245  -18.846 1.00 20.50  ? 626  HIS   A CE1    1 
ATOM   4981 N NE2    . HIS   A  1 634 ? 2.209  -59.600  -18.019 1.00 21.11  ? 626  HIS   A NE2    1 
ATOM   4982 N N      . ASN   A  1 635 ? 0.075  -55.054  -14.244 1.00 16.27  ? 627  ASN   A N      1 
ATOM   4983 C CA     . ASN   A  1 635 ? 0.097  -54.142  -13.097 1.00 16.17  ? 627  ASN   A CA     1 
ATOM   4984 C C      . ASN   A  1 635 ? -1.096 -53.176  -13.050 1.00 19.71  ? 627  ASN   A C      1 
ATOM   4985 O O      . ASN   A  1 635 ? -0.883 -51.986  -12.840 1.00 20.00  ? 627  ASN   A O      1 
ATOM   4986 C CB     . ASN   A  1 635 ? 1.433  -53.397  -13.025 1.00 16.18  ? 627  ASN   A CB     1 
ATOM   4987 C CG     . ASN   A  1 635 ? 1.673  -52.739  -11.683 1.00 25.34  ? 627  ASN   A CG     1 
ATOM   4988 O OD1    . ASN   A  1 635 ? 1.344  -53.283  -10.627 1.00 18.41  ? 627  ASN   A OD1    1 
ATOM   4989 N ND2    . ASN   A  1 635 ? 2.179  -51.529  -11.707 1.00 14.64  ? 627  ASN   A ND2    1 
ATOM   4990 N N      . PRO   A  1 636 ? -2.358 -53.619  -13.263 1.00 17.86  ? 628  PRO   A N      1 
ATOM   4991 C CA     . PRO   A  1 636 ? -3.471 -52.653  -13.220 1.00 18.68  ? 628  PRO   A CA     1 
ATOM   4992 C C      . PRO   A  1 636 ? -3.645 -52.048  -11.826 1.00 23.59  ? 628  PRO   A C      1 
ATOM   4993 O O      . PRO   A  1 636 ? -3.529 -52.774  -10.829 1.00 22.51  ? 628  PRO   A O      1 
ATOM   4994 C CB     . PRO   A  1 636 ? -4.679 -53.491  -13.660 1.00 19.91  ? 628  PRO   A CB     1 
ATOM   4995 C CG     . PRO   A  1 636 ? -4.326 -54.882  -13.274 1.00 22.81  ? 628  PRO   A CG     1 
ATOM   4996 C CD     . PRO   A  1 636 ? -2.855 -54.994  -13.504 1.00 18.34  ? 628  PRO   A CD     1 
ATOM   4997 N N      . THR   A  1 637 ? -3.841 -50.709  -11.763 1.00 21.36  ? 629  THR   A N      1 
ATOM   4998 C CA     . THR   A  1 637 ? -3.987 -49.881  -10.541 1.00 21.56  ? 629  THR   A CA     1 
ATOM   4999 C C      . THR   A  1 637 ? -2.722 -49.905  -9.642  1.00 24.51  ? 629  THR   A C      1 
ATOM   5000 O O      . THR   A  1 637 ? -2.781 -49.470  -8.490  1.00 25.31  ? 629  THR   A O      1 
ATOM   5001 C CB     . THR   A  1 637 ? -5.256 -50.229  -9.705  1.00 33.02  ? 629  THR   A CB     1 
ATOM   5002 O OG1    . THR   A  1 637 ? -5.060 -51.461  -8.998  1.00 33.15  ? 629  THR   A OG1    1 
ATOM   5003 C CG2    . THR   A  1 637 ? -6.516 -50.273  -10.522 1.00 31.66  ? 629  THR   A CG2    1 
ATOM   5004 N N      . GLY   A  1 638 ? -1.613 -50.414  -10.173 1.00 19.44  ? 630  GLY   A N      1 
ATOM   5005 C CA     . GLY   A  1 638 ? -0.369 -50.575  -9.432  1.00 19.29  ? 630  GLY   A CA     1 
ATOM   5006 C C      . GLY   A  1 638 ? -0.487 -51.640  -8.358  1.00 23.14  ? 630  GLY   A C      1 
ATOM   5007 O O      . GLY   A  1 638 ? 0.183  -51.554  -7.340  1.00 23.12  ? 630  GLY   A O      1 
ATOM   5008 N N      . ARG   A  1 639 ? -1.338 -52.665  -8.578  1.00 19.99  ? 631  ARG   A N      1 
ATOM   5009 C CA     . ARG   A  1 639 ? -1.599 -53.733  -7.613  1.00 18.76  ? 631  ARG   A CA     1 
ATOM   5010 C C      . ARG   A  1 639 ? -0.341 -54.528  -7.226  1.00 22.09  ? 631  ARG   A C      1 
ATOM   5011 O O      . ARG   A  1 639 ? -0.294 -55.094  -6.137  1.00 20.41  ? 631  ARG   A O      1 
ATOM   5012 C CB     . ARG   A  1 639 ? -2.737 -54.673  -8.089  1.00 18.17  ? 631  ARG   A CB     1 
ATOM   5013 C CG     . ARG   A  1 639 ? -2.382 -55.507  -9.324  1.00 24.00  ? 631  ARG   A CG     1 
ATOM   5014 C CD     . ARG   A  1 639 ? -3.370 -56.610  -9.639  1.00 24.51  ? 631  ARG   A CD     1 
ATOM   5015 N NE     . ARG   A  1 639 ? -2.955 -57.341  -10.836 1.00 24.89  ? 631  ARG   A NE     1 
ATOM   5016 C CZ     . ARG   A  1 639 ? -3.777 -57.995  -11.653 1.00 41.11  ? 631  ARG   A CZ     1 
ATOM   5017 N NH1    . ARG   A  1 639 ? -5.080 -58.041  -11.399 1.00 33.74  ? 631  ARG   A NH1    1 
ATOM   5018 N NH2    . ARG   A  1 639 ? -3.305 -58.593  -12.738 1.00 25.62  ? 631  ARG   A NH2    1 
ATOM   5019 N N      . SER   A  1 640 ? 0.654  -54.584  -8.116  1.00 18.46  ? 632  SER   A N      1 
ATOM   5020 C CA     . SER   A  1 640 ? 1.894  -55.314  -7.851  1.00 18.06  ? 632  SER   A CA     1 
ATOM   5021 C C      . SER   A  1 640 ? 3.085  -54.394  -7.663  1.00 21.09  ? 632  SER   A C      1 
ATOM   5022 O O      . SER   A  1 640 ? 4.007  -54.755  -6.957  1.00 21.09  ? 632  SER   A O      1 
ATOM   5023 C CB     . SER   A  1 640 ? 2.192  -56.288  -8.984  1.00 20.26  ? 632  SER   A CB     1 
ATOM   5024 O OG     . SER   A  1 640 ? 1.153  -57.236  -9.138  1.00 23.04  ? 632  SER   A OG     1 
ATOM   5025 N N      . TYR   A  1 641 ? 3.070  -53.219  -8.290  1.00 19.39  ? 633  TYR   A N      1 
ATOM   5026 C CA     . TYR   A  1 641 ? 4.189  -52.285  -8.255  1.00 19.62  ? 633  TYR   A CA     1 
ATOM   5027 C C      . TYR   A  1 641 ? 3.756  -50.838  -8.317  1.00 21.84  ? 633  TYR   A C      1 
ATOM   5028 O O      . TYR   A  1 641 ? 3.033  -50.460  -9.237  1.00 20.22  ? 633  TYR   A O      1 
ATOM   5029 C CB     . TYR   A  1 641 ? 5.111  -52.559  -9.465  1.00 21.57  ? 633  TYR   A CB     1 
ATOM   5030 C CG     . TYR   A  1 641 ? 6.331  -51.670  -9.504  1.00 24.70  ? 633  TYR   A CG     1 
ATOM   5031 C CD1    . TYR   A  1 641 ? 7.425  -51.919  -8.679  1.00 27.52  ? 633  TYR   A CD1    1 
ATOM   5032 C CD2    . TYR   A  1 641 ? 6.389  -50.568  -10.352 1.00 25.85  ? 633  TYR   A CD2    1 
ATOM   5033 C CE1    . TYR   A  1 641 ? 8.550  -51.096  -8.700  1.00 29.09  ? 633  TYR   A CE1    1 
ATOM   5034 C CE2    . TYR   A  1 641 ? 7.515  -49.743  -10.388 1.00 27.07  ? 633  TYR   A CE2    1 
ATOM   5035 C CZ     . TYR   A  1 641 ? 8.595  -50.017  -9.564  1.00 34.49  ? 633  TYR   A CZ     1 
ATOM   5036 O OH     . TYR   A  1 641 ? 9.716  -49.229  -9.586  1.00 39.11  ? 633  TYR   A OH     1 
ATOM   5037 N N      . THR   A  1 642 ? 4.254  -50.018  -7.368  1.00 18.61  ? 634  THR   A N      1 
ATOM   5038 C CA     . THR   A  1 642 ? 4.088  -48.557  -7.334  1.00 17.88  ? 634  THR   A CA     1 
ATOM   5039 C C      . THR   A  1 642 ? 5.385  -47.920  -6.838  1.00 20.84  ? 634  THR   A C      1 
ATOM   5040 O O      . THR   A  1 642 ? 6.177  -48.557  -6.140  1.00 20.87  ? 634  THR   A O      1 
ATOM   5041 C CB     . THR   A  1 642 ? 2.917  -48.102  -6.453  1.00 24.64  ? 634  THR   A CB     1 
ATOM   5042 O OG1    . THR   A  1 642 ? 3.155  -48.503  -5.105  1.00 23.45  ? 634  THR   A OG1    1 
ATOM   5043 C CG2    . THR   A  1 642 ? 1.555  -48.586  -6.960  1.00 18.82  ? 634  THR   A CG2    1 
ATOM   5044 N N      . ILE   A  1 643 ? 5.588  -46.661  -7.198  1.00 16.81  ? 635  ILE   A N      1 
ATOM   5045 C CA     . ILE   A  1 643 ? 6.725  -45.852  -6.783  1.00 15.62  ? 635  ILE   A CA     1 
ATOM   5046 C C      . ILE   A  1 643 ? 6.080  -44.767  -5.895  1.00 19.35  ? 635  ILE   A C      1 
ATOM   5047 O O      . ILE   A  1 643 ? 5.310  -43.950  -6.385  1.00 19.35  ? 635  ILE   A O      1 
ATOM   5048 C CB     . ILE   A  1 643 ? 7.490  -45.259  -8.017  1.00 17.56  ? 635  ILE   A CB     1 
ATOM   5049 C CG1    . ILE   A  1 643 ? 7.691  -46.298  -9.165  1.00 18.22  ? 635  ILE   A CG1    1 
ATOM   5050 C CG2    . ILE   A  1 643 ? 8.835  -44.704  -7.590  1.00 17.58  ? 635  ILE   A CG2    1 
ATOM   5051 C CD1    . ILE   A  1 643 ? 7.669  -45.624  -10.627 1.00 22.10  ? 635  ILE   A CD1    1 
ATOM   5052 N N      . GLY   A  1 644 ? 6.324  -44.831  -4.595  1.00 18.56  ? 636  GLY   A N      1 
ATOM   5053 C CA     . GLY   A  1 644 ? 5.722  -43.906  -3.643  1.00 18.54  ? 636  GLY   A CA     1 
ATOM   5054 C C      . GLY   A  1 644 ? 6.202  -42.479  -3.775  1.00 23.30  ? 636  GLY   A C      1 
ATOM   5055 O O      . GLY   A  1 644 ? 7.407  -42.237  -3.898  1.00 23.05  ? 636  GLY   A O      1 
ATOM   5056 N N      . LEU   A  1 645 ? 5.248  -41.525  -3.750  1.00 20.20  ? 637  LEU   A N      1 
ATOM   5057 C CA     . LEU   A  1 645 ? 5.507  -40.084  -3.794  1.00 33.91  ? 637  LEU   A CA     1 
ATOM   5058 C C      . LEU   A  1 645 ? 5.798  -39.539  -2.393  1.00 68.93  ? 637  LEU   A C      1 
ATOM   5059 O O      . LEU   A  1 645 ? 5.967  -40.314  -1.447  1.00 34.71  ? 637  LEU   A O      1 
ATOM   5060 C CB     . LEU   A  1 645 ? 4.324  -39.325  -4.421  1.00 33.35  ? 637  LEU   A CB     1 
ATOM   5061 C CG     . LEU   A  1 645 ? 4.336  -39.210  -5.937  1.00 36.61  ? 637  LEU   A CG     1 
ATOM   5062 C CD1    . LEU   A  1 645 ? 3.000  -38.748  -6.453  1.00 35.91  ? 637  LEU   A CD1    1 
ATOM   5063 C CD2    . LEU   A  1 645 ? 5.428  -38.270  -6.402  1.00 38.42  ? 637  LEU   A CD2    1 
ATOM   5064 N N      . PRO   B  2 28  ? 47.541 -121.441 -22.802 1.00 88.27  ? 20   PRO   B N      1 
ATOM   5065 C CA     . PRO   B  2 28  ? 48.464 -120.870 -23.793 1.00 88.06  ? 20   PRO   B CA     1 
ATOM   5066 C C      . PRO   B  2 28  ? 49.079 -119.547 -23.326 1.00 92.54  ? 20   PRO   B C      1 
ATOM   5067 O O      . PRO   B  2 28  ? 48.432 -118.840 -22.548 1.00 92.27  ? 20   PRO   B O      1 
ATOM   5068 C CB     . PRO   B  2 28  ? 47.580 -120.675 -25.030 1.00 89.68  ? 20   PRO   B CB     1 
ATOM   5069 C CG     . PRO   B  2 28  ? 46.475 -121.646 -24.864 1.00 94.04  ? 20   PRO   B CG     1 
ATOM   5070 C CD     . PRO   B  2 28  ? 46.221 -121.738 -23.389 1.00 89.68  ? 20   PRO   B CD     1 
ATOM   5071 N N      . PRO   B  2 29  ? 50.306 -119.172 -23.782 1.00 89.46  ? 21   PRO   B N      1 
ATOM   5072 C CA     . PRO   B  2 29  ? 50.887 -117.886 -23.342 1.00 89.23  ? 21   PRO   B CA     1 
ATOM   5073 C C      . PRO   B  2 29  ? 50.156 -116.672 -23.924 1.00 92.52  ? 21   PRO   B C      1 
ATOM   5074 O O      . PRO   B  2 29  ? 49.481 -116.798 -24.951 1.00 92.21  ? 21   PRO   B O      1 
ATOM   5075 C CB     . PRO   B  2 29  ? 52.343 -117.969 -23.810 1.00 91.00  ? 21   PRO   B CB     1 
ATOM   5076 C CG     . PRO   B  2 29  ? 52.321 -118.896 -24.963 1.00 95.50  ? 21   PRO   B CG     1 
ATOM   5077 C CD     . PRO   B  2 29  ? 51.214 -119.884 -24.710 1.00 91.13  ? 21   PRO   B CD     1 
ATOM   5078 N N      . ASN   B  2 30  ? 50.257 -115.507 -23.235 1.00 88.19  ? 22   ASN   B N      1 
ATOM   5079 C CA     . ASN   B  2 30  ? 49.627 -114.217 -23.581 1.00 87.52  ? 22   ASN   B CA     1 
ATOM   5080 C C      . ASN   B  2 30  ? 48.085 -114.233 -23.427 1.00 90.14  ? 22   ASN   B C      1 
ATOM   5081 O O      . ASN   B  2 30  ? 47.467 -113.167 -23.343 1.00 89.65  ? 22   ASN   B O      1 
ATOM   5082 C CB     . ASN   B  2 30  ? 50.062 -113.725 -24.977 1.00 88.33  ? 22   ASN   B CB     1 
ATOM   5083 C CG     . ASN   B  2 30  ? 49.756 -112.278 -25.277 1.00 109.55 ? 22   ASN   B CG     1 
ATOM   5084 O OD1    . ASN   B  2 30  ? 50.160 -111.360 -24.551 1.00 103.65 ? 22   ASN   B OD1    1 
ATOM   5085 N ND2    . ASN   B  2 30  ? 49.073 -112.045 -26.387 1.00 99.98  ? 22   ASN   B ND2    1 
ATOM   5086 N N      . ALA   B  2 31  ? 47.476 -115.435 -23.359 1.00 85.61  ? 23   ALA   B N      1 
ATOM   5087 C CA     . ALA   B  2 31  ? 46.035 -115.621 -23.194 1.00 84.79  ? 23   ALA   B CA     1 
ATOM   5088 C C      . ALA   B  2 31  ? 45.608 -115.328 -21.747 1.00 87.23  ? 23   ALA   B C      1 
ATOM   5089 O O      . ALA   B  2 31  ? 46.277 -115.794 -20.818 1.00 86.88  ? 23   ALA   B O      1 
ATOM   5090 C CB     . ALA   B  2 31  ? 45.639 -117.038 -23.583 1.00 85.49  ? 23   ALA   B CB     1 
ATOM   5091 N N      . PRO   B  2 32  ? 44.514 -114.553 -21.529 1.00 82.39  ? 24   PRO   B N      1 
ATOM   5092 C CA     . PRO   B  2 32  ? 44.085 -114.262 -20.147 1.00 81.44  ? 24   PRO   B CA     1 
ATOM   5093 C C      . PRO   B  2 32  ? 43.468 -115.470 -19.443 1.00 82.41  ? 24   PRO   B C      1 
ATOM   5094 O O      . PRO   B  2 32  ? 42.807 -116.288 -20.088 1.00 81.87  ? 24   PRO   B O      1 
ATOM   5095 C CB     . PRO   B  2 32  ? 43.075 -113.126 -20.319 1.00 83.41  ? 24   PRO   B CB     1 
ATOM   5096 C CG     . PRO   B  2 32  ? 42.527 -113.316 -21.681 1.00 88.13  ? 24   PRO   B CG     1 
ATOM   5097 C CD     . PRO   B  2 32  ? 43.622 -113.910 -22.519 1.00 83.84  ? 24   PRO   B CD     1 
ATOM   5098 N N      . ALA   B  2 33  ? 43.681 -115.571 -18.114 1.00 76.63  ? 25   ALA   B N      1 
ATOM   5099 C CA     . ALA   B  2 33  ? 43.181 -116.663 -17.270 1.00 75.32  ? 25   ALA   B CA     1 
ATOM   5100 C C      . ALA   B  2 33  ? 41.647 -116.751 -17.219 1.00 76.31  ? 25   ALA   B C      1 
ATOM   5101 O O      . ALA   B  2 33  ? 41.106 -117.833 -16.974 1.00 75.73  ? 25   ALA   B O      1 
ATOM   5102 C CB     . ALA   B  2 33  ? 43.749 -116.537 -15.864 1.00 76.07  ? 25   ALA   B CB     1 
ATOM   5103 N N      . CYS   B  2 34  ? 40.955 -115.619 -17.462 1.00 70.61  ? 26   CYS   B N      1 
ATOM   5104 C CA     . CYS   B  2 34  ? 39.497 -115.544 -17.435 1.00 69.19  ? 26   CYS   B CA     1 
ATOM   5105 C C      . CYS   B  2 34  ? 38.904 -114.875 -18.676 1.00 68.39  ? 26   CYS   B C      1 
ATOM   5106 O O      . CYS   B  2 34  ? 39.423 -113.862 -19.152 1.00 68.03  ? 26   CYS   B O      1 
ATOM   5107 C CB     . CYS   B  2 34  ? 39.019 -114.868 -16.152 1.00 69.83  ? 26   CYS   B CB     1 
ATOM   5108 S SG     . CYS   B  2 34  ? 37.217 -114.825 -15.959 1.00 73.98  ? 26   CYS   B SG     1 
ATOM   5109 N N      . MET   B  2 35  ? 37.796 -115.442 -19.177 1.00 60.89  ? 27   MET   B N      1 
ATOM   5110 C CA     . MET   B  2 35  ? 37.048 -114.913 -20.315 1.00 58.46  ? 27   MET   B CA     1 
ATOM   5111 C C      . MET   B  2 35  ? 35.900 -114.056 -19.771 1.00 56.94  ? 27   MET   B C      1 
ATOM   5112 O O      . MET   B  2 35  ? 35.209 -114.473 -18.831 1.00 56.12  ? 27   MET   B O      1 
ATOM   5113 C CB     . MET   B  2 35  ? 36.488 -116.055 -21.185 1.00 60.65  ? 27   MET   B CB     1 
ATOM   5114 C CG     . MET   B  2 35  ? 35.982 -115.584 -22.536 1.00 64.16  ? 27   MET   B CG     1 
ATOM   5115 S SD     . MET   B  2 35  ? 35.085 -116.827 -23.498 1.00 68.27  ? 27   MET   B SD     1 
ATOM   5116 C CE     . MET   B  2 35  ? 36.424 -117.924 -23.968 1.00 64.96  ? 27   MET   B CE     1 
ATOM   5117 N N      . GLU   B  2 36  ? 35.700 -112.865 -20.368 1.00 49.06  ? 28   GLU   B N      1 
ATOM   5118 C CA     . GLU   B  2 36  ? 34.633 -111.926 -19.994 1.00 46.29  ? 28   GLU   B CA     1 
ATOM   5119 C C      . GLU   B  2 36  ? 33.263 -112.540 -20.280 1.00 45.84  ? 28   GLU   B C      1 
ATOM   5120 O O      . GLU   B  2 36  ? 33.123 -113.292 -21.245 1.00 45.30  ? 28   GLU   B O      1 
ATOM   5121 C CB     . GLU   B  2 36  ? 34.801 -110.535 -20.643 1.00 47.26  ? 28   GLU   B CB     1 
ATOM   5122 C CG     . GLU   B  2 36  ? 35.782 -110.427 -21.801 1.00 53.54  ? 28   GLU   B CG     1 
ATOM   5123 C CD     . GLU   B  2 36  ? 37.239 -110.320 -21.398 1.00 66.97  ? 28   GLU   B CD     1 
ATOM   5124 O OE1    . GLU   B  2 36  ? 37.697 -109.192 -21.108 1.00 49.95  ? 28   GLU   B OE1    1 
ATOM   5125 O OE2    . GLU   B  2 36  ? 37.920 -111.369 -21.359 1.00 66.71  ? 28   GLU   B OE2    1 
ATOM   5126 N N      . ARG   B  2 37  ? 32.288 -112.287 -19.390 1.00 39.22  ? 29   ARG   B N      1 
ATOM   5127 C CA     . ARG   B  2 37  ? 30.931 -112.846 -19.402 1.00 37.85  ? 29   ARG   B CA     1 
ATOM   5128 C C      . ARG   B  2 37  ? 30.139 -112.659 -20.711 1.00 39.15  ? 29   ARG   B C      1 
ATOM   5129 O O      . ARG   B  2 37  ? 29.471 -113.604 -21.145 1.00 38.91  ? 29   ARG   B O      1 
ATOM   5130 C CB     . ARG   B  2 37  ? 30.127 -112.284 -18.204 1.00 38.38  ? 29   ARG   B CB     1 
ATOM   5131 C CG     . ARG   B  2 37  ? 28.638 -112.647 -18.147 1.00 47.35  ? 29   ARG   B CG     1 
ATOM   5132 C CD     . ARG   B  2 37  ? 28.350 -113.894 -17.339 1.00 56.05  ? 29   ARG   B CD     1 
ATOM   5133 N NE     . ARG   B  2 37  ? 26.921 -114.209 -17.330 1.00 57.42  ? 29   ARG   B NE     1 
ATOM   5134 C CZ     . ARG   B  2 37  ? 26.379 -115.206 -16.639 1.00 69.45  ? 29   ARG   B CZ     1 
ATOM   5135 N NH1    . ARG   B  2 37  ? 27.142 -115.998 -15.891 1.00 55.33  ? 29   ARG   B NH1    1 
ATOM   5136 N NH2    . ARG   B  2 37  ? 25.071 -115.421 -16.688 1.00 54.52  ? 29   ARG   B NH2    1 
ATOM   5137 N N      . GLN   B  2 38  ? 30.171 -111.454 -21.307 1.00 33.47  ? 30   GLN   B N      1 
ATOM   5138 C CA     . GLN   B  2 38  ? 29.342 -111.148 -22.473 1.00 32.47  ? 30   GLN   B CA     1 
ATOM   5139 C C      . GLN   B  2 38  ? 29.945 -111.587 -23.825 1.00 36.16  ? 30   GLN   B C      1 
ATOM   5140 O O      . GLN   B  2 38  ? 30.721 -110.850 -24.450 1.00 36.51  ? 30   GLN   B O      1 
ATOM   5141 C CB     . GLN   B  2 38  ? 28.936 -109.660 -22.496 1.00 33.52  ? 30   GLN   B CB     1 
ATOM   5142 C CG     . GLN   B  2 38  ? 27.932 -109.268 -21.396 1.00 38.14  ? 30   GLN   B CG     1 
ATOM   5143 C CD     . GLN   B  2 38  ? 28.528 -109.150 -20.008 1.00 40.46  ? 30   GLN   B CD     1 
ATOM   5144 O OE1    . GLN   B  2 38  ? 29.664 -108.700 -19.813 1.00 34.32  ? 30   GLN   B OE1    1 
ATOM   5145 N NE2    . GLN   B  2 38  ? 27.764 -109.556 -19.011 1.00 29.61  ? 30   GLN   B NE2    1 
ATOM   5146 N N      . LEU   B  2 39  ? 29.533 -112.780 -24.285 1.00 31.01  ? 31   LEU   B N      1 
ATOM   5147 C CA     . LEU   B  2 39  ? 29.942 -113.334 -25.578 1.00 30.67  ? 31   LEU   B CA     1 
ATOM   5148 C C      . LEU   B  2 39  ? 29.194 -112.576 -26.692 1.00 34.02  ? 31   LEU   B C      1 
ATOM   5149 O O      . LEU   B  2 39  ? 27.960 -112.572 -26.722 1.00 32.07  ? 31   LEU   B O      1 
ATOM   5150 C CB     . LEU   B  2 39  ? 29.654 -114.845 -25.650 1.00 30.73  ? 31   LEU   B CB     1 
ATOM   5151 C CG     . LEU   B  2 39  ? 30.348 -115.756 -24.612 1.00 35.05  ? 31   LEU   B CG     1 
ATOM   5152 C CD1    . LEU   B  2 39  ? 29.907 -117.193 -24.775 1.00 34.33  ? 31   LEU   B CD1    1 
ATOM   5153 C CD2    . LEU   B  2 39  ? 31.861 -115.678 -24.729 1.00 38.14  ? 31   LEU   B CD2    1 
ATOM   5154 N N      . GLU   B  2 40  ? 29.949 -111.882 -27.555 1.00 31.27  ? 32   GLU   B N      1 
ATOM   5155 C CA     . GLU   B  2 40  ? 29.394 -111.061 -28.626 1.00 31.68  ? 32   GLU   B CA     1 
ATOM   5156 C C      . GLU   B  2 40  ? 29.347 -111.742 -29.989 1.00 37.57  ? 32   GLU   B C      1 
ATOM   5157 O O      . GLU   B  2 40  ? 28.382 -111.544 -30.731 1.00 37.42  ? 32   GLU   B O      1 
ATOM   5158 C CB     . GLU   B  2 40  ? 30.155 -109.728 -28.723 1.00 32.96  ? 32   GLU   B CB     1 
ATOM   5159 C CG     . GLU   B  2 40  ? 29.396 -108.615 -29.442 1.00 44.92  ? 32   GLU   B CG     1 
ATOM   5160 C CD     . GLU   B  2 40  ? 27.947 -108.407 -29.035 1.00 56.33  ? 32   GLU   B CD     1 
ATOM   5161 O OE1    . GLU   B  2 40  ? 27.692 -108.089 -27.850 1.00 42.09  ? 32   GLU   B OE1    1 
ATOM   5162 O OE2    . GLU   B  2 40  ? 27.063 -108.620 -29.895 1.00 42.74  ? 32   GLU   B OE2    1 
ATOM   5163 N N      . ALA   B  2 41  ? 30.412 -112.481 -30.349 1.00 34.60  ? 33   ALA   B N      1 
ATOM   5164 C CA     . ALA   B  2 41  ? 30.502 -113.129 -31.652 1.00 34.52  ? 33   ALA   B CA     1 
ATOM   5165 C C      . ALA   B  2 41  ? 31.077 -114.541 -31.624 1.00 38.43  ? 33   ALA   B C      1 
ATOM   5166 O O      . ALA   B  2 41  ? 31.877 -114.880 -30.751 1.00 38.06  ? 33   ALA   B O      1 
ATOM   5167 C CB     . ALA   B  2 41  ? 31.283 -112.252 -32.614 1.00 35.39  ? 33   ALA   B CB     1 
ATOM   5168 N N      . ALA   B  2 42  ? 30.631 -115.365 -32.580 1.00 35.09  ? 34   ALA   B N      1 
ATOM   5169 C CA     . ALA   B  2 42  ? 31.048 -116.750 -32.785 1.00 34.59  ? 34   ALA   B CA     1 
ATOM   5170 C C      . ALA   B  2 42  ? 31.119 -116.973 -34.287 1.00 38.40  ? 34   ALA   B C      1 
ATOM   5171 O O      . ALA   B  2 42  ? 30.106 -116.788 -34.971 1.00 37.50  ? 34   ALA   B O      1 
ATOM   5172 C CB     . ALA   B  2 42  ? 30.041 -117.706 -32.164 1.00 35.15  ? 34   ALA   B CB     1 
ATOM   5173 N N      . ARG   B  2 43  ? 32.325 -117.302 -34.812 1.00 34.80  ? 35   ARG   B N      1 
ATOM   5174 C CA     . ARG   B  2 43  ? 32.526 -117.533 -36.251 1.00 34.36  ? 35   ARG   B CA     1 
ATOM   5175 C C      . ARG   B  2 43  ? 33.358 -118.772 -36.550 1.00 37.15  ? 35   ARG   B C      1 
ATOM   5176 O O      . ARG   B  2 43  ? 34.544 -118.817 -36.207 1.00 35.29  ? 35   ARG   B O      1 
ATOM   5177 C CB     . ARG   B  2 43  ? 33.167 -116.308 -36.954 1.00 33.90  ? 35   ARG   B CB     1 
ATOM   5178 C CG     . ARG   B  2 43  ? 32.421 -114.982 -36.840 1.00 41.74  ? 35   ARG   B CG     1 
ATOM   5179 C CD     . ARG   B  2 43  ? 31.068 -114.965 -37.537 1.00 45.95  ? 35   ARG   B CD     1 
ATOM   5180 N NE     . ARG   B  2 43  ? 30.270 -113.838 -37.060 1.00 53.76  ? 35   ARG   B NE     1 
ATOM   5181 C CZ     . ARG   B  2 43  ? 30.313 -112.616 -37.581 1.00 66.65  ? 35   ARG   B CZ     1 
ATOM   5182 N NH1    . ARG   B  2 43  ? 31.084 -112.361 -38.633 1.00 45.34  ? 35   ARG   B NH1    1 
ATOM   5183 N NH2    . ARG   B  2 43  ? 29.581 -111.640 -37.059 1.00 57.24  ? 35   ARG   B NH2    1 
ATOM   5184 N N      . TYR   B  2 44  ? 32.751 -119.754 -37.235 1.00 35.10  ? 36   TYR   B N      1 
ATOM   5185 C CA     . TYR   B  2 44  ? 33.468 -120.959 -37.673 1.00 35.00  ? 36   TYR   B CA     1 
ATOM   5186 C C      . TYR   B  2 44  ? 34.338 -120.627 -38.886 1.00 40.73  ? 36   TYR   B C      1 
ATOM   5187 O O      . TYR   B  2 44  ? 33.916 -119.907 -39.794 1.00 41.17  ? 36   TYR   B O      1 
ATOM   5188 C CB     . TYR   B  2 44  ? 32.501 -122.098 -38.062 1.00 34.79  ? 36   TYR   B CB     1 
ATOM   5189 C CG     . TYR   B  2 44  ? 32.032 -122.967 -36.915 1.00 35.68  ? 36   TYR   B CG     1 
ATOM   5190 C CD1    . TYR   B  2 44  ? 32.936 -123.714 -36.162 1.00 37.14  ? 36   TYR   B CD1    1 
ATOM   5191 C CD2    . TYR   B  2 44  ? 30.675 -123.113 -36.637 1.00 36.33  ? 36   TYR   B CD2    1 
ATOM   5192 C CE1    . TYR   B  2 44  ? 32.505 -124.541 -35.127 1.00 36.80  ? 36   TYR   B CE1    1 
ATOM   5193 C CE2    . TYR   B  2 44  ? 30.232 -123.936 -35.604 1.00 36.83  ? 36   TYR   B CE2    1 
ATOM   5194 C CZ     . TYR   B  2 44  ? 31.150 -124.654 -34.855 1.00 44.90  ? 36   TYR   B CZ     1 
ATOM   5195 O OH     . TYR   B  2 44  ? 30.714 -125.461 -33.829 1.00 46.90  ? 36   TYR   B OH     1 
ATOM   5196 N N      . ARG   B  2 45  ? 35.551 -121.154 -38.889 1.00 38.20  ? 37   ARG   B N      1 
ATOM   5197 C CA     . ARG   B  2 45  ? 36.494 -121.055 -39.994 1.00 38.22  ? 37   ARG   B CA     1 
ATOM   5198 C C      . ARG   B  2 45  ? 36.184 -122.278 -40.886 1.00 42.70  ? 37   ARG   B C      1 
ATOM   5199 O O      . ARG   B  2 45  ? 35.564 -123.228 -40.401 1.00 41.72  ? 37   ARG   B O      1 
ATOM   5200 C CB     . ARG   B  2 45  ? 37.918 -121.133 -39.430 1.00 38.25  ? 37   ARG   B CB     1 
ATOM   5201 C CG     . ARG   B  2 45  ? 38.999 -120.796 -40.427 1.00 43.15  ? 37   ARG   B CG     1 
ATOM   5202 C CD     . ARG   B  2 45  ? 40.322 -120.549 -39.747 1.00 43.98  ? 37   ARG   B CD     1 
ATOM   5203 N NE     . ARG   B  2 45  ? 40.894 -121.739 -39.113 1.00 40.75  ? 37   ARG   B NE     1 
ATOM   5204 C CZ     . ARG   B  2 45  ? 42.129 -121.791 -38.624 1.00 52.68  ? 37   ARG   B CZ     1 
ATOM   5205 N NH1    . ARG   B  2 45  ? 42.928 -120.734 -38.706 1.00 38.16  ? 37   ARG   B NH1    1 
ATOM   5206 N NH2    . ARG   B  2 45  ? 42.580 -122.903 -38.056 1.00 37.52  ? 37   ARG   B NH2    1 
ATOM   5207 N N      . SER   B  2 46  ? 36.591 -122.253 -42.175 1.00 40.45  ? 38   SER   B N      1 
ATOM   5208 C CA     . SER   B  2 46  ? 36.351 -123.347 -43.132 1.00 40.99  ? 38   SER   B CA     1 
ATOM   5209 C C      . SER   B  2 46  ? 36.835 -124.723 -42.628 1.00 46.18  ? 38   SER   B C      1 
ATOM   5210 O O      . SER   B  2 46  ? 36.147 -125.718 -42.849 1.00 45.67  ? 38   SER   B O      1 
ATOM   5211 C CB     . SER   B  2 46  ? 36.956 -123.016 -44.493 1.00 44.90  ? 38   SER   B CB     1 
ATOM   5212 O OG     . SER   B  2 46  ? 38.366 -122.884 -44.409 1.00 55.37  ? 38   SER   B OG     1 
ATOM   5213 N N      . ASP   B  2 47  ? 37.979 -124.763 -41.907 1.00 44.57  ? 39   ASP   B N      1 
ATOM   5214 C CA     . ASP   B  2 47  ? 38.539 -125.992 -41.325 1.00 45.48  ? 39   ASP   B CA     1 
ATOM   5215 C C      . ASP   B  2 47  ? 37.698 -126.543 -40.154 1.00 50.81  ? 39   ASP   B C      1 
ATOM   5216 O O      . ASP   B  2 47  ? 37.697 -127.752 -39.918 1.00 51.34  ? 39   ASP   B O      1 
ATOM   5217 C CB     . ASP   B  2 47  ? 40.016 -125.797 -40.918 1.00 47.62  ? 39   ASP   B CB     1 
ATOM   5218 C CG     . ASP   B  2 47  ? 40.266 -124.983 -39.654 1.00 63.21  ? 39   ASP   B CG     1 
ATOM   5219 O OD1    . ASP   B  2 47  ? 39.425 -124.110 -39.326 1.00 64.54  ? 39   ASP   B OD1    1 
ATOM   5220 O OD2    . ASP   B  2 47  ? 41.315 -125.198 -39.009 1.00 70.07  ? 39   ASP   B OD2    1 
ATOM   5221 N N      . GLY   B  2 48  ? 37.005 -125.652 -39.439 1.00 46.83  ? 40   GLY   B N      1 
ATOM   5222 C CA     . GLY   B  2 48  ? 36.148 -126.019 -38.314 1.00 46.05  ? 40   GLY   B CA     1 
ATOM   5223 C C      . GLY   B  2 48  ? 36.494 -125.372 -36.987 1.00 47.49  ? 40   GLY   B C      1 
ATOM   5224 O O      . GLY   B  2 48  ? 35.803 -125.608 -35.993 1.00 47.05  ? 40   GLY   B O      1 
ATOM   5225 N N      . ALA   B  2 49  ? 37.572 -124.570 -36.955 1.00 42.55  ? 41   ALA   B N      1 
ATOM   5226 C CA     . ALA   B  2 49  ? 38.015 -123.844 -35.764 1.00 42.07  ? 41   ALA   B CA     1 
ATOM   5227 C C      . ALA   B  2 49  ? 37.004 -122.728 -35.434 1.00 45.82  ? 41   ALA   B C      1 
ATOM   5228 O O      . ALA   B  2 49  ? 36.452 -122.100 -36.346 1.00 44.24  ? 41   ALA   B O      1 
ATOM   5229 C CB     . ALA   B  2 49  ? 39.396 -123.250 -35.997 1.00 42.63  ? 41   ALA   B CB     1 
ATOM   5230 N N      . LEU   B  2 50  ? 36.738 -122.520 -34.133 1.00 42.77  ? 42   LEU   B N      1 
ATOM   5231 C CA     . LEU   B  2 50  ? 35.779 -121.530 -33.650 1.00 42.21  ? 42   LEU   B CA     1 
ATOM   5232 C C      . LEU   B  2 50  ? 36.452 -120.263 -33.164 1.00 44.40  ? 42   LEU   B C      1 
ATOM   5233 O O      . LEU   B  2 50  ? 37.370 -120.315 -32.349 1.00 43.81  ? 42   LEU   B O      1 
ATOM   5234 C CB     . LEU   B  2 50  ? 34.882 -122.130 -32.549 1.00 42.38  ? 42   LEU   B CB     1 
ATOM   5235 C CG     . LEU   B  2 50  ? 33.633 -121.332 -32.131 1.00 47.20  ? 42   LEU   B CG     1 
ATOM   5236 C CD1    . LEU   B  2 50  ? 32.598 -121.273 -33.253 1.00 47.53  ? 42   LEU   B CD1    1 
ATOM   5237 C CD2    . LEU   B  2 50  ? 32.994 -121.948 -30.918 1.00 49.40  ? 42   LEU   B CD2    1 
ATOM   5238 N N      . LEU   B  2 51  ? 36.001 -119.127 -33.694 1.00 40.24  ? 43   LEU   B N      1 
ATOM   5239 C CA     . LEU   B  2 51  ? 36.463 -117.799 -33.296 1.00 39.48  ? 43   LEU   B CA     1 
ATOM   5240 C C      . LEU   B  2 51  ? 35.396 -117.240 -32.363 1.00 40.79  ? 43   LEU   B C      1 
ATOM   5241 O O      . LEU   B  2 51  ? 34.204 -117.329 -32.666 1.00 39.24  ? 43   LEU   B O      1 
ATOM   5242 C CB     . LEU   B  2 51  ? 36.661 -116.893 -34.526 1.00 39.53  ? 43   LEU   B CB     1 
ATOM   5243 C CG     . LEU   B  2 51  ? 37.117 -115.441 -34.316 1.00 44.51  ? 43   LEU   B CG     1 
ATOM   5244 C CD1    . LEU   B  2 51  ? 38.507 -115.356 -33.673 1.00 44.97  ? 43   LEU   B CD1    1 
ATOM   5245 C CD2    . LEU   B  2 51  ? 37.122 -114.697 -35.634 1.00 46.03  ? 43   LEU   B CD2    1 
ATOM   5246 N N      . LEU   B  2 52  ? 35.826 -116.750 -31.197 1.00 37.17  ? 44   LEU   B N      1 
ATOM   5247 C CA     . LEU   B  2 52  ? 34.947 -116.176 -30.177 1.00 36.35  ? 44   LEU   B CA     1 
ATOM   5248 C C      . LEU   B  2 52  ? 35.377 -114.772 -29.842 1.00 37.87  ? 44   LEU   B C      1 
ATOM   5249 O O      . LEU   B  2 52  ? 36.564 -114.517 -29.628 1.00 36.90  ? 44   LEU   B O      1 
ATOM   5250 C CB     . LEU   B  2 52  ? 34.930 -117.006 -28.880 1.00 36.55  ? 44   LEU   B CB     1 
ATOM   5251 C CG     . LEU   B  2 52  ? 34.229 -118.363 -28.888 1.00 42.03  ? 44   LEU   B CG     1 
ATOM   5252 C CD1    . LEU   B  2 52  ? 34.313 -119.012 -27.512 1.00 42.77  ? 44   LEU   B CD1    1 
ATOM   5253 C CD2    . LEU   B  2 52  ? 32.763 -118.238 -29.276 1.00 45.39  ? 44   LEU   B CD2    1 
ATOM   5254 N N      . GLY   B  2 53  ? 34.393 -113.880 -29.799 1.00 32.89  ? 45   GLY   B N      1 
ATOM   5255 C CA     . GLY   B  2 53  ? 34.556 -112.489 -29.408 1.00 31.65  ? 45   GLY   B CA     1 
ATOM   5256 C C      . GLY   B  2 53  ? 33.749 -112.254 -28.150 1.00 34.31  ? 45   GLY   B C      1 
ATOM   5257 O O      . GLY   B  2 53  ? 32.588 -112.676 -28.065 1.00 32.97  ? 45   GLY   B O      1 
ATOM   5258 N N      . ALA   B  2 54  ? 34.373 -111.628 -27.150 1.00 30.69  ? 46   ALA   B N      1 
ATOM   5259 C CA     . ALA   B  2 54  ? 33.733 -111.363 -25.864 1.00 30.63  ? 46   ALA   B CA     1 
ATOM   5260 C C      . ALA   B  2 54  ? 34.048 -109.969 -25.331 1.00 35.11  ? 46   ALA   B C      1 
ATOM   5261 O O      . ALA   B  2 54  ? 35.078 -109.386 -25.682 1.00 35.06  ? 46   ALA   B O      1 
ATOM   5262 C CB     . ALA   B  2 54  ? 34.131 -112.421 -24.847 1.00 31.27  ? 46   ALA   B CB     1 
ATOM   5263 N N      . SER   B  2 55  ? 33.135 -109.422 -24.512 1.00 31.01  ? 47   SER   B N      1 
ATOM   5264 C CA     . SER   B  2 55  ? 33.308 -108.112 -23.883 1.00 30.95  ? 47   SER   B CA     1 
ATOM   5265 C C      . SER   B  2 55  ? 32.907 -108.193 -22.435 1.00 33.69  ? 47   SER   B C      1 
ATOM   5266 O O      . SER   B  2 55  ? 32.077 -109.019 -22.057 1.00 33.54  ? 47   SER   B O      1 
ATOM   5267 C CB     . SER   B  2 55  ? 32.423 -107.057 -24.542 1.00 33.66  ? 47   SER   B CB     1 
ATOM   5268 O OG     . SER   B  2 55  ? 32.688 -106.862 -25.915 1.00 39.38  ? 47   SER   B OG     1 
ATOM   5269 N N      . SER   B  2 56  ? 33.482 -107.321 -21.630 1.00 30.19  ? 48   SER   B N      1 
ATOM   5270 C CA     . SER   B  2 56  ? 33.088 -107.161 -20.246 1.00 29.98  ? 48   SER   B CA     1 
ATOM   5271 C C      . SER   B  2 56  ? 32.181 -105.912 -20.277 1.00 31.62  ? 48   SER   B C      1 
ATOM   5272 O O      . SER   B  2 56  ? 32.679 -104.799 -20.471 1.00 29.52  ? 48   SER   B O      1 
ATOM   5273 C CB     . SER   B  2 56  ? 34.313 -106.958 -19.364 1.00 33.98  ? 48   SER   B CB     1 
ATOM   5274 O OG     . SER   B  2 56  ? 33.912 -106.828 -18.012 1.00 49.72  ? 48   SER   B OG     1 
ATOM   5275 N N      . LEU   B  2 57  ? 30.847 -106.113 -20.202 1.00 28.04  ? 49   LEU   B N      1 
ATOM   5276 C CA     . LEU   B  2 57  ? 29.881 -104.997 -20.264 1.00 27.52  ? 49   LEU   B CA     1 
ATOM   5277 C C      . LEU   B  2 57  ? 29.428 -104.492 -18.872 1.00 31.55  ? 49   LEU   B C      1 
ATOM   5278 O O      . LEU   B  2 57  ? 28.530 -103.648 -18.760 1.00 30.14  ? 49   LEU   B O      1 
ATOM   5279 C CB     . LEU   B  2 57  ? 28.673 -105.334 -21.161 1.00 26.88  ? 49   LEU   B CB     1 
ATOM   5280 C CG     . LEU   B  2 57  ? 28.934 -105.787 -22.625 1.00 30.46  ? 49   LEU   B CG     1 
ATOM   5281 C CD1    . LEU   B  2 57  ? 27.652 -105.994 -23.328 1.00 30.62  ? 49   LEU   B CD1    1 
ATOM   5282 C CD2    . LEU   B  2 57  ? 29.729 -104.773 -23.406 1.00 29.98  ? 49   LEU   B CD2    1 
ATOM   5283 N N      . SER   B  2 58  ? 30.072 -105.002 -17.820 1.00 28.70  ? 50   SER   B N      1 
ATOM   5284 C CA     . SER   B  2 58  ? 29.815 -104.628 -16.437 1.00 29.26  ? 50   SER   B CA     1 
ATOM   5285 C C      . SER   B  2 58  ? 31.058 -104.881 -15.574 1.00 35.55  ? 50   SER   B C      1 
ATOM   5286 O O      . SER   B  2 58  ? 32.076 -105.347 -16.089 1.00 36.24  ? 50   SER   B O      1 
ATOM   5287 C CB     . SER   B  2 58  ? 28.591 -105.353 -15.885 1.00 32.04  ? 50   SER   B CB     1 
ATOM   5288 O OG     . SER   B  2 58  ? 28.150 -104.636 -14.746 1.00 41.01  ? 50   SER   B OG     1 
ATOM   5289 N N      . GLY   B  2 59  ? 30.984 -104.518 -14.295 1.00 31.98  ? 51   GLY   B N      1 
ATOM   5290 C CA     . GLY   B  2 59  ? 32.104 -104.644 -13.373 1.00 31.58  ? 51   GLY   B CA     1 
ATOM   5291 C C      . GLY   B  2 59  ? 33.134 -103.559 -13.613 1.00 35.51  ? 51   GLY   B C      1 
ATOM   5292 O O      . GLY   B  2 59  ? 32.921 -102.668 -14.437 1.00 35.50  ? 51   GLY   B O      1 
ATOM   5293 N N      . ARG   B  2 60  ? 34.267 -103.644 -12.909 1.00 31.59  ? 52   ARG   B N      1 
ATOM   5294 C CA     . ARG   B  2 60  ? 35.369 -102.684 -12.935 1.00 30.81  ? 52   ARG   B CA     1 
ATOM   5295 C C      . ARG   B  2 60  ? 35.958 -102.377 -14.323 1.00 35.08  ? 52   ARG   B C      1 
ATOM   5296 O O      . ARG   B  2 60  ? 36.076 -101.201 -14.680 1.00 34.26  ? 52   ARG   B O      1 
ATOM   5297 C CB     . ARG   B  2 60  ? 36.482 -103.165 -11.983 1.00 29.55  ? 52   ARG   B CB     1 
ATOM   5298 C CG     . ARG   B  2 60  ? 37.672 -102.215 -11.848 1.00 36.13  ? 52   ARG   B CG     1 
ATOM   5299 C CD     . ARG   B  2 60  ? 38.815 -102.865 -11.090 1.00 45.52  ? 52   ARG   B CD     1 
ATOM   5300 N NE     . ARG   B  2 60  ? 38.506 -103.034 -9.671  1.00 52.94  ? 52   ARG   B NE     1 
ATOM   5301 C CZ     . ARG   B  2 60  ? 39.030 -102.302 -8.692  1.00 69.24  ? 52   ARG   B CZ     1 
ATOM   5302 N NH1    . ARG   B  2 60  ? 39.919 -101.354 -8.964  1.00 58.04  ? 52   ARG   B NH1    1 
ATOM   5303 N NH2    . ARG   B  2 60  ? 38.681 -102.524 -7.431  1.00 56.99  ? 52   ARG   B NH2    1 
ATOM   5304 N N      . CYS   B  2 61  ? 36.361 -103.424 -15.070 1.00 32.62  ? 53   CYS   B N      1 
ATOM   5305 C CA     A CYS   B  2 61  ? 37.007 -103.265 -16.372 0.50 32.58  ? 53   CYS   B CA     1 
ATOM   5306 C CA     B CYS   B  2 61  ? 37.003 -103.256 -16.370 0.50 32.70  ? 53   CYS   B CA     1 
ATOM   5307 C C      . CYS   B  2 61  ? 36.088 -103.572 -17.539 1.00 34.14  ? 53   CYS   B C      1 
ATOM   5308 O O      . CYS   B  2 61  ? 35.484 -104.642 -17.580 1.00 32.36  ? 53   CYS   B O      1 
ATOM   5309 C CB     A CYS   B  2 61  ? 38.298 -104.078 -16.443 0.50 33.29  ? 53   CYS   B CB     1 
ATOM   5310 C CB     B CYS   B  2 61  ? 38.302 -104.054 -16.435 0.50 33.53  ? 53   CYS   B CB     1 
ATOM   5311 S SG     A CYS   B  2 61  ? 39.290 -103.763 -17.926 0.50 37.32  ? 53   CYS   B SG     1 
ATOM   5312 S SG     B CYS   B  2 61  ? 39.436 -103.722 -15.062 0.50 37.64  ? 53   CYS   B SG     1 
ATOM   5313 N N      . TRP   B  2 62  ? 35.992 -102.629 -18.483 1.00 29.32  ? 54   TRP   B N      1 
ATOM   5314 C CA     . TRP   B  2 62  ? 35.179 -102.766 -19.686 1.00 29.18  ? 54   TRP   B CA     1 
ATOM   5315 C C      . TRP   B  2 62  ? 36.116 -102.966 -20.877 1.00 34.27  ? 54   TRP   B C      1 
ATOM   5316 O O      . TRP   B  2 62  ? 36.385 -102.043 -21.650 1.00 34.26  ? 54   TRP   B O      1 
ATOM   5317 C CB     . TRP   B  2 62  ? 34.242 -101.557 -19.885 1.00 27.41  ? 54   TRP   B CB     1 
ATOM   5318 C CG     . TRP   B  2 62  ? 33.211 -101.353 -18.805 1.00 28.01  ? 54   TRP   B CG     1 
ATOM   5319 C CD1    . TRP   B  2 62  ? 32.870 -102.222 -17.809 1.00 30.76  ? 54   TRP   B CD1    1 
ATOM   5320 C CD2    . TRP   B  2 62  ? 32.343 -100.222 -18.666 1.00 27.63  ? 54   TRP   B CD2    1 
ATOM   5321 N NE1    . TRP   B  2 62  ? 31.869 -101.685 -17.034 1.00 30.16  ? 54   TRP   B NE1    1 
ATOM   5322 C CE2    . TRP   B  2 62  ? 31.518 -100.461 -17.544 1.00 31.61  ? 54   TRP   B CE2    1 
ATOM   5323 C CE3    . TRP   B  2 62  ? 32.194 -99.013  -19.373 1.00 28.88  ? 54   TRP   B CE3    1 
ATOM   5324 C CZ2    . TRP   B  2 62  ? 30.571 -99.527  -17.096 1.00 30.99  ? 54   TRP   B CZ2    1 
ATOM   5325 C CZ3    . TRP   B  2 62  ? 31.248 -98.093  -18.936 1.00 30.33  ? 54   TRP   B CZ3    1 
ATOM   5326 C CH2    . TRP   B  2 62  ? 30.463 -98.344  -17.801 1.00 30.92  ? 54   TRP   B CH2    1 
ATOM   5327 N N      . ALA   B  2 63  ? 36.668 -104.166 -20.974 1.00 31.36  ? 55   ALA   B N      1 
ATOM   5328 C CA     . ALA   B  2 63  ? 37.587 -104.514 -22.055 1.00 31.29  ? 55   ALA   B CA     1 
ATOM   5329 C C      . ALA   B  2 63  ? 36.975 -105.656 -22.874 1.00 34.13  ? 55   ALA   B C      1 
ATOM   5330 O O      . ALA   B  2 63  ? 35.765 -105.888 -22.805 1.00 31.80  ? 55   ALA   B O      1 
ATOM   5331 C CB     . ALA   B  2 63  ? 38.946 -104.908 -21.475 1.00 32.09  ? 55   ALA   B CB     1 
ATOM   5332 N N      . GLY   B  2 64  ? 37.796 -106.321 -23.673 1.00 32.74  ? 56   GLY   B N      1 
ATOM   5333 C CA     . GLY   B  2 64  ? 37.344 -107.418 -24.508 1.00 33.21  ? 56   GLY   B CA     1 
ATOM   5334 C C      . GLY   B  2 64  ? 38.403 -108.472 -24.717 1.00 38.18  ? 56   GLY   B C      1 
ATOM   5335 O O      . GLY   B  2 64  ? 39.546 -108.311 -24.272 1.00 38.63  ? 56   GLY   B O      1 
ATOM   5336 N N      . SER   B  2 65  ? 38.029 -109.548 -25.416 1.00 34.20  ? 57   SER   B N      1 
ATOM   5337 C CA     . SER   B  2 65  ? 38.942 -110.652 -25.706 1.00 34.25  ? 57   SER   B CA     1 
ATOM   5338 C C      . SER   B  2 65  ? 38.577 -111.413 -26.979 1.00 38.90  ? 57   SER   B C      1 
ATOM   5339 O O      . SER   B  2 65  ? 37.397 -111.512 -27.319 1.00 39.00  ? 57   SER   B O      1 
ATOM   5340 C CB     . SER   B  2 65  ? 39.033 -111.603 -24.514 1.00 36.80  ? 57   SER   B CB     1 
ATOM   5341 O OG     . SER   B  2 65  ? 37.760 -112.133 -24.168 1.00 42.49  ? 57   SER   B OG     1 
ATOM   5342 N N      . LEU   B  2 66  ? 39.601 -111.939 -27.679 1.00 35.54  ? 58   LEU   B N      1 
ATOM   5343 C CA     . LEU   B  2 66  ? 39.467 -112.759 -28.893 1.00 35.77  ? 58   LEU   B CA     1 
ATOM   5344 C C      . LEU   B  2 66  ? 39.971 -114.162 -28.587 1.00 40.38  ? 58   LEU   B C      1 
ATOM   5345 O O      . LEU   B  2 66  ? 41.039 -114.303 -27.987 1.00 39.62  ? 58   LEU   B O      1 
ATOM   5346 C CB     . LEU   B  2 66  ? 40.260 -112.163 -30.069 1.00 35.70  ? 58   LEU   B CB     1 
ATOM   5347 C CG     . LEU   B  2 66  ? 39.924 -110.736 -30.482 1.00 39.77  ? 58   LEU   B CG     1 
ATOM   5348 C CD1    . LEU   B  2 66  ? 40.889 -110.244 -31.513 1.00 39.78  ? 58   LEU   B CD1    1 
ATOM   5349 C CD2    . LEU   B  2 66  ? 38.514 -110.636 -31.004 1.00 41.90  ? 58   LEU   B CD2    1 
ATOM   5350 N N      . TRP   B  2 67  ? 39.200 -115.192 -28.972 1.00 38.43  ? 59   TRP   B N      1 
ATOM   5351 C CA     . TRP   B  2 67  ? 39.532 -116.591 -28.692 1.00 39.26  ? 59   TRP   B CA     1 
ATOM   5352 C C      . TRP   B  2 67  ? 39.438 -117.509 -29.893 1.00 44.41  ? 59   TRP   B C      1 
ATOM   5353 O O      . TRP   B  2 67  ? 38.520 -117.378 -30.703 1.00 43.60  ? 59   TRP   B O      1 
ATOM   5354 C CB     . TRP   B  2 67  ? 38.615 -117.148 -27.597 1.00 38.48  ? 59   TRP   B CB     1 
ATOM   5355 C CG     . TRP   B  2 67  ? 38.652 -116.358 -26.331 1.00 39.82  ? 59   TRP   B CG     1 
ATOM   5356 C CD1    . TRP   B  2 67  ? 37.875 -115.284 -26.017 1.00 42.77  ? 59   TRP   B CD1    1 
ATOM   5357 C CD2    . TRP   B  2 67  ? 39.549 -116.544 -25.229 1.00 39.76  ? 59   TRP   B CD2    1 
ATOM   5358 N NE1    . TRP   B  2 67  ? 38.220 -114.799 -24.780 1.00 42.43  ? 59   TRP   B NE1    1 
ATOM   5359 C CE2    . TRP   B  2 67  ? 39.242 -115.554 -24.269 1.00 43.86  ? 59   TRP   B CE2    1 
ATOM   5360 C CE3    . TRP   B  2 67  ? 40.568 -117.471 -24.943 1.00 41.00  ? 59   TRP   B CE3    1 
ATOM   5361 C CZ2    . TRP   B  2 67  ? 39.916 -115.460 -23.047 1.00 43.17  ? 59   TRP   B CZ2    1 
ATOM   5362 C CZ3    . TRP   B  2 67  ? 41.249 -117.366 -23.738 1.00 42.57  ? 59   TRP   B CZ3    1 
ATOM   5363 C CH2    . TRP   B  2 67  ? 40.914 -116.381 -22.800 1.00 43.25  ? 59   TRP   B CH2    1 
ATOM   5364 N N      . LEU   B  2 68  ? 40.353 -118.493 -29.961 1.00 41.93  ? 60   LEU   B N      1 
ATOM   5365 C CA     . LEU   B  2 68  ? 40.362 -119.519 -31.000 1.00 41.66  ? 60   LEU   B CA     1 
ATOM   5366 C C      . LEU   B  2 68  ? 40.261 -120.891 -30.345 1.00 45.28  ? 60   LEU   B C      1 
ATOM   5367 O O      . LEU   B  2 68  ? 41.057 -121.216 -29.467 1.00 44.53  ? 60   LEU   B O      1 
ATOM   5368 C CB     . LEU   B  2 68  ? 41.601 -119.415 -31.909 1.00 41.82  ? 60   LEU   B CB     1 
ATOM   5369 C CG     . LEU   B  2 68  ? 41.755 -120.521 -32.970 1.00 46.78  ? 60   LEU   B CG     1 
ATOM   5370 C CD1    . LEU   B  2 68  ? 40.858 -120.274 -34.168 1.00 46.64  ? 60   LEU   B CD1    1 
ATOM   5371 C CD2    . LEU   B  2 68  ? 43.201 -120.661 -33.403 1.00 50.34  ? 60   LEU   B CD2    1 
ATOM   5372 N N      . PHE   B  2 69  ? 39.257 -121.668 -30.752 1.00 42.54  ? 61   PHE   B N      1 
ATOM   5373 C CA     . PHE   B  2 69  ? 38.994 -123.011 -30.252 1.00 43.29  ? 61   PHE   B CA     1 
ATOM   5374 C C      . PHE   B  2 69  ? 38.990 -123.998 -31.416 1.00 49.73  ? 61   PHE   B C      1 
ATOM   5375 O O      . PHE   B  2 69  ? 38.009 -124.048 -32.166 1.00 48.26  ? 61   PHE   B O      1 
ATOM   5376 C CB     . PHE   B  2 69  ? 37.639 -123.058 -29.513 1.00 45.10  ? 61   PHE   B CB     1 
ATOM   5377 C CG     . PHE   B  2 69  ? 37.669 -122.462 -28.129 1.00 46.98  ? 61   PHE   B CG     1 
ATOM   5378 C CD1    . PHE   B  2 69  ? 37.543 -121.087 -27.941 1.00 50.06  ? 61   PHE   B CD1    1 
ATOM   5379 C CD2    . PHE   B  2 69  ? 37.837 -123.269 -27.011 1.00 49.08  ? 61   PHE   B CD2    1 
ATOM   5380 C CE1    . PHE   B  2 69  ? 37.601 -120.534 -26.660 1.00 50.94  ? 61   PHE   B CE1    1 
ATOM   5381 C CE2    . PHE   B  2 69  ? 37.886 -122.715 -25.731 1.00 51.98  ? 61   PHE   B CE2    1 
ATOM   5382 C CZ     . PHE   B  2 69  ? 37.758 -121.352 -25.563 1.00 50.15  ? 61   PHE   B CZ     1 
ATOM   5383 N N      . LYS   B  2 70  ? 40.078 -124.791 -31.568 1.00 49.14  ? 62   LYS   B N      1 
ATOM   5384 C CA     . LYS   B  2 70  ? 40.138 -125.818 -32.620 1.00 50.21  ? 62   LYS   B CA     1 
ATOM   5385 C C      . LYS   B  2 70  ? 39.121 -126.930 -32.320 1.00 57.32  ? 62   LYS   B C      1 
ATOM   5386 O O      . LYS   B  2 70  ? 38.595 -127.552 -33.248 1.00 57.48  ? 62   LYS   B O      1 
ATOM   5387 C CB     . LYS   B  2 70  ? 41.558 -126.344 -32.832 1.00 52.48  ? 62   LYS   B CB     1 
ATOM   5388 C CG     . LYS   B  2 70  ? 42.388 -125.401 -33.696 1.00 66.13  ? 62   LYS   B CG     1 
ATOM   5389 C CD     . LYS   B  2 70  ? 43.777 -125.939 -33.976 1.00 76.08  ? 62   LYS   B CD     1 
ATOM   5390 C CE     . LYS   B  2 70  ? 44.556 -125.015 -34.880 1.00 84.78  ? 62   LYS   B CE     1 
ATOM   5391 N NZ     . LYS   B  2 70  ? 45.959 -125.473 -35.056 1.00 94.34  ? 62   LYS   B NZ     1 
ATOM   5392 N N      . ASP   B  2 71  ? 38.792 -127.107 -31.019 1.00 55.46  ? 63   ASP   B N      1 
ATOM   5393 C CA     . ASP   B  2 71  ? 37.764 -128.014 -30.514 1.00 56.18  ? 63   ASP   B CA     1 
ATOM   5394 C C      . ASP   B  2 71  ? 36.584 -127.120 -30.045 1.00 61.21  ? 63   ASP   B C      1 
ATOM   5395 O O      . ASP   B  2 71  ? 36.714 -126.452 -29.013 1.00 60.85  ? 63   ASP   B O      1 
ATOM   5396 C CB     . ASP   B  2 71  ? 38.310 -128.898 -29.366 1.00 58.15  ? 63   ASP   B CB     1 
ATOM   5397 C CG     . ASP   B  2 71  ? 37.291 -129.805 -28.682 1.00 70.66  ? 63   ASP   B CG     1 
ATOM   5398 O OD1    . ASP   B  2 71  ? 36.286 -130.183 -29.337 1.00 71.07  ? 63   ASP   B OD1    1 
ATOM   5399 O OD2    . ASP   B  2 71  ? 37.513 -130.164 -27.502 1.00 78.12  ? 63   ASP   B OD2    1 
ATOM   5400 N N      . PRO   B  2 72  ? 35.457 -127.053 -30.808 1.00 58.18  ? 64   PRO   B N      1 
ATOM   5401 C CA     . PRO   B  2 72  ? 34.339 -126.177 -30.400 1.00 57.76  ? 64   PRO   B CA     1 
ATOM   5402 C C      . PRO   B  2 72  ? 33.608 -126.599 -29.126 1.00 60.93  ? 64   PRO   B C      1 
ATOM   5403 O O      . PRO   B  2 72  ? 33.032 -125.742 -28.458 1.00 60.10  ? 64   PRO   B O      1 
ATOM   5404 C CB     . PRO   B  2 72  ? 33.414 -126.195 -31.620 1.00 59.55  ? 64   PRO   B CB     1 
ATOM   5405 C CG     . PRO   B  2 72  ? 33.677 -127.503 -32.265 1.00 64.20  ? 64   PRO   B CG     1 
ATOM   5406 C CD     . PRO   B  2 72  ? 35.148 -127.754 -32.073 1.00 59.83  ? 64   PRO   B CD     1 
ATOM   5407 N N      . CYS   B  2 73  ? 33.623 -127.910 -28.796 1.00 57.48  ? 65   CYS   B N      1 
ATOM   5408 C CA     . CYS   B  2 73  ? 32.977 -128.467 -27.599 1.00 57.18  ? 65   CYS   B CA     1 
ATOM   5409 C C      . CYS   B  2 73  ? 33.620 -128.001 -26.289 1.00 58.31  ? 65   CYS   B C      1 
ATOM   5410 O O      . CYS   B  2 73  ? 32.952 -127.975 -25.257 1.00 57.73  ? 65   CYS   B O      1 
ATOM   5411 C CB     . CYS   B  2 73  ? 32.907 -129.987 -27.680 1.00 58.14  ? 65   CYS   B CB     1 
ATOM   5412 S SG     . CYS   B  2 73  ? 31.753 -130.599 -28.931 1.00 62.45  ? 65   CYS   B SG     1 
ATOM   5413 N N      . ALA   B  2 74  ? 34.906 -127.625 -26.344 1.00 53.66  ? 66   ALA   B N      1 
ATOM   5414 C CA     . ALA   B  2 74  ? 35.694 -127.120 -25.223 1.00 53.17  ? 66   ALA   B CA     1 
ATOM   5415 C C      . ALA   B  2 74  ? 35.274 -125.695 -24.816 1.00 56.47  ? 66   ALA   B C      1 
ATOM   5416 O O      . ALA   B  2 74  ? 35.455 -125.319 -23.658 1.00 55.54  ? 66   ALA   B O      1 
ATOM   5417 C CB     . ALA   B  2 74  ? 37.165 -127.133 -25.594 1.00 53.87  ? 66   ALA   B CB     1 
ATOM   5418 N N      . ALA   B  2 75  ? 34.746 -124.900 -25.779 1.00 52.63  ? 67   ALA   B N      1 
ATOM   5419 C CA     . ALA   B  2 75  ? 34.309 -123.513 -25.575 1.00 51.85  ? 67   ALA   B CA     1 
ATOM   5420 C C      . ALA   B  2 75  ? 33.153 -123.415 -24.568 1.00 54.98  ? 67   ALA   B C      1 
ATOM   5421 O O      . ALA   B  2 75  ? 32.280 -124.286 -24.576 1.00 54.46  ? 67   ALA   B O      1 
ATOM   5422 C CB     . ALA   B  2 75  ? 33.902 -122.891 -26.904 1.00 52.30  ? 67   ALA   B CB     1 
ATOM   5423 N N      . PRO   B  2 76  ? 33.136 -122.409 -23.661 1.00 51.01  ? 68   PRO   B N      1 
ATOM   5424 C CA     . PRO   B  2 76  ? 34.066 -121.280 -23.520 1.00 50.82  ? 68   PRO   B CA     1 
ATOM   5425 C C      . PRO   B  2 76  ? 35.175 -121.448 -22.459 1.00 54.54  ? 68   PRO   B C      1 
ATOM   5426 O O      . PRO   B  2 76  ? 35.635 -120.443 -21.911 1.00 54.35  ? 68   PRO   B O      1 
ATOM   5427 C CB     . PRO   B  2 76  ? 33.111 -120.122 -23.203 1.00 52.47  ? 68   PRO   B CB     1 
ATOM   5428 C CG     . PRO   B  2 76  ? 31.953 -120.776 -22.442 1.00 56.81  ? 68   PRO   B CG     1 
ATOM   5429 C CD     . PRO   B  2 76  ? 32.012 -122.268 -22.716 1.00 52.46  ? 68   PRO   B CD     1 
ATOM   5430 N N      . ASN   B  2 77  ? 35.637 -122.691 -22.193 1.00 50.81  ? 69   ASN   B N      1 
ATOM   5431 C CA     . ASN   B  2 77  ? 36.697 -122.935 -21.204 1.00 50.61  ? 69   ASN   B CA     1 
ATOM   5432 C C      . ASN   B  2 77  ? 38.079 -122.442 -21.681 1.00 54.62  ? 69   ASN   B C      1 
ATOM   5433 O O      . ASN   B  2 77  ? 38.632 -122.972 -22.646 1.00 53.96  ? 69   ASN   B O      1 
ATOM   5434 C CB     . ASN   B  2 77  ? 36.735 -124.408 -20.757 1.00 50.85  ? 69   ASN   B CB     1 
ATOM   5435 C CG     . ASN   B  2 77  ? 37.452 -124.649 -19.437 1.00 70.95  ? 69   ASN   B CG     1 
ATOM   5436 O OD1    . ASN   B  2 77  ? 38.642 -124.328 -19.254 1.00 59.04  ? 69   ASN   B OD1    1 
ATOM   5437 N ND2    . ASN   B  2 77  ? 36.748 -125.267 -18.498 1.00 61.74  ? 69   ASN   B ND2    1 
ATOM   5438 N N      . GLU   B  2 78  ? 38.629 -121.434 -20.976 1.00 51.71  ? 70   GLU   B N      1 
ATOM   5439 C CA     . GLU   B  2 78  ? 39.922 -120.777 -21.235 1.00 51.87  ? 70   GLU   B CA     1 
ATOM   5440 C C      . GLU   B  2 78  ? 41.125 -121.734 -21.259 1.00 56.64  ? 70   GLU   B C      1 
ATOM   5441 O O      . GLU   B  2 78  ? 42.052 -121.525 -22.042 1.00 55.80  ? 70   GLU   B O      1 
ATOM   5442 C CB     . GLU   B  2 78  ? 40.188 -119.645 -20.222 1.00 53.25  ? 70   GLU   B CB     1 
ATOM   5443 C CG     . GLU   B  2 78  ? 39.082 -118.609 -20.090 1.00 64.70  ? 70   GLU   B CG     1 
ATOM   5444 C CD     . GLU   B  2 78  ? 38.001 -118.946 -19.081 1.00 88.43  ? 70   GLU   B CD     1 
ATOM   5445 O OE1    . GLU   B  2 78  ? 36.825 -119.066 -19.494 1.00 84.09  ? 70   GLU   B OE1    1 
ATOM   5446 O OE2    . GLU   B  2 78  ? 38.327 -119.098 -17.881 1.00 86.38  ? 70   GLU   B OE2    1 
ATOM   5447 N N      . GLY   B  2 79  ? 41.104 -122.755 -20.402 1.00 54.24  ? 71   GLY   B N      1 
ATOM   5448 C CA     . GLY   B  2 79  ? 42.176 -123.745 -20.312 1.00 54.53  ? 71   GLY   B CA     1 
ATOM   5449 C C      . GLY   B  2 79  ? 42.193 -124.758 -21.441 1.00 58.91  ? 71   GLY   B C      1 
ATOM   5450 O O      . GLY   B  2 79  ? 43.100 -125.592 -21.512 1.00 59.04  ? 71   GLY   B O      1 
ATOM   5451 N N      . PHE   B  2 80  ? 41.194 -124.687 -22.338 1.00 55.02  ? 72   PHE   B N      1 
ATOM   5452 C CA     . PHE   B  2 80  ? 41.034 -125.592 -23.470 1.00 54.58  ? 72   PHE   B CA     1 
ATOM   5453 C C      . PHE   B  2 80  ? 41.007 -124.853 -24.826 1.00 55.70  ? 72   PHE   B C      1 
ATOM   5454 O O      . PHE   B  2 80  ? 40.549 -125.411 -25.825 1.00 55.05  ? 72   PHE   B O      1 
ATOM   5455 C CB     . PHE   B  2 80  ? 39.788 -126.473 -23.259 1.00 57.14  ? 72   PHE   B CB     1 
ATOM   5456 C CG     . PHE   B  2 80  ? 39.891 -127.456 -22.114 1.00 59.87  ? 72   PHE   B CG     1 
ATOM   5457 C CD1    . PHE   B  2 80  ? 40.288 -128.770 -22.337 1.00 63.78  ? 72   PHE   B CD1    1 
ATOM   5458 C CD2    . PHE   B  2 80  ? 39.587 -127.069 -20.811 1.00 62.91  ? 72   PHE   B CD2    1 
ATOM   5459 C CE1    . PHE   B  2 80  ? 40.386 -129.678 -21.276 1.00 65.16  ? 72   PHE   B CE1    1 
ATOM   5460 C CE2    . PHE   B  2 80  ? 39.699 -127.974 -19.748 1.00 66.16  ? 72   PHE   B CE2    1 
ATOM   5461 C CZ     . PHE   B  2 80  ? 40.091 -129.273 -19.989 1.00 64.40  ? 72   PHE   B CZ     1 
ATOM   5462 N N      . CYS   B  2 81  ? 41.531 -123.613 -24.866 1.00 50.73  ? 73   CYS   B N      1 
ATOM   5463 C CA     . CYS   B  2 81  ? 41.597 -122.816 -26.095 1.00 49.67  ? 73   CYS   B CA     1 
ATOM   5464 C C      . CYS   B  2 81  ? 42.928 -123.017 -26.823 1.00 51.07  ? 73   CYS   B C      1 
ATOM   5465 O O      . CYS   B  2 81  ? 43.933 -123.354 -26.194 1.00 50.99  ? 73   CYS   B O      1 
ATOM   5466 C CB     . CYS   B  2 81  ? 41.322 -121.338 -25.818 1.00 49.86  ? 73   CYS   B CB     1 
ATOM   5467 S SG     . CYS   B  2 81  ? 42.713 -120.437 -25.081 1.00 53.89  ? 73   CYS   B SG     1 
ATOM   5468 N N      . SER   B  2 82  ? 42.925 -122.800 -28.145 1.00 45.06  ? 74   SER   B N      1 
ATOM   5469 C CA     . SER   B  2 82  ? 44.102 -122.894 -29.007 1.00 43.69  ? 74   SER   B CA     1 
ATOM   5470 C C      . SER   B  2 82  ? 44.919 -121.600 -28.913 1.00 46.22  ? 74   SER   B C      1 
ATOM   5471 O O      . SER   B  2 82  ? 46.151 -121.651 -28.935 1.00 45.79  ? 74   SER   B O      1 
ATOM   5472 C CB     . SER   B  2 82  ? 43.685 -123.152 -30.454 1.00 46.56  ? 74   SER   B CB     1 
ATOM   5473 O OG     . SER   B  2 82  ? 42.701 -124.171 -30.542 1.00 53.35  ? 74   SER   B OG     1 
ATOM   5474 N N      . ALA   B  2 83  ? 44.223 -120.436 -28.815 1.00 41.55  ? 75   ALA   B N      1 
ATOM   5475 C CA     . ALA   B  2 83  ? 44.811 -119.092 -28.713 1.00 40.44  ? 75   ALA   B CA     1 
ATOM   5476 C C      . ALA   B  2 83  ? 43.833 -118.101 -28.054 1.00 42.43  ? 75   ALA   B C      1 
ATOM   5477 O O      . ALA   B  2 83  ? 42.618 -118.284 -28.123 1.00 41.21  ? 75   ALA   B O      1 
ATOM   5478 C CB     . ALA   B  2 83  ? 45.208 -118.587 -30.098 1.00 41.01  ? 75   ALA   B CB     1 
ATOM   5479 N N      . GLY   B  2 84  ? 44.383 -117.055 -27.449 1.00 38.96  ? 76   GLY   B N      1 
ATOM   5480 C CA     . GLY   B  2 84  ? 43.622 -116.008 -26.779 1.00 38.18  ? 76   GLY   B CA     1 
ATOM   5481 C C      . GLY   B  2 84  ? 44.404 -114.724 -26.605 1.00 41.41  ? 76   GLY   B C      1 
ATOM   5482 O O      . GLY   B  2 84  ? 45.631 -114.754 -26.450 1.00 41.20  ? 76   GLY   B O      1 
ATOM   5483 N N      . VAL   B  2 85  ? 43.697 -113.578 -26.655 1.00 36.46  ? 77   VAL   B N      1 
ATOM   5484 C CA     . VAL   B  2 85  ? 44.298 -112.254 -26.487 1.00 35.60  ? 77   VAL   B CA     1 
ATOM   5485 C C      . VAL   B  2 85  ? 43.281 -111.261 -25.890 1.00 39.57  ? 77   VAL   B C      1 
ATOM   5486 O O      . VAL   B  2 85  ? 42.071 -111.421 -26.076 1.00 37.61  ? 77   VAL   B O      1 
ATOM   5487 C CB     . VAL   B  2 85  ? 44.979 -111.713 -27.786 1.00 39.11  ? 77   VAL   B CB     1 
ATOM   5488 C CG1    . VAL   B  2 85  ? 43.963 -111.107 -28.759 1.00 38.90  ? 77   VAL   B CG1    1 
ATOM   5489 C CG2    . VAL   B  2 85  ? 46.081 -110.704 -27.460 1.00 38.71  ? 77   VAL   B CG2    1 
ATOM   5490 N N      . GLN   B  2 86  ? 43.792 -110.241 -25.185 1.00 37.07  ? 78   GLN   B N      1 
ATOM   5491 C CA     . GLN   B  2 86  ? 42.991 -109.175 -24.607 1.00 37.23  ? 78   GLN   B CA     1 
ATOM   5492 C C      . GLN   B  2 86  ? 43.052 -107.961 -25.513 1.00 42.56  ? 78   GLN   B C      1 
ATOM   5493 O O      . GLN   B  2 86  ? 44.131 -107.576 -25.984 1.00 42.40  ? 78   GLN   B O      1 
ATOM   5494 C CB     . GLN   B  2 86  ? 43.483 -108.806 -23.200 1.00 38.15  ? 78   GLN   B CB     1 
ATOM   5495 C CG     . GLN   B  2 86  ? 42.947 -109.706 -22.095 1.00 55.34  ? 78   GLN   B CG     1 
ATOM   5496 C CD     . GLN   B  2 86  ? 41.524 -109.389 -21.694 1.00 78.17  ? 78   GLN   B CD     1 
ATOM   5497 O OE1    . GLN   B  2 86  ? 41.169 -108.242 -21.394 1.00 73.93  ? 78   GLN   B OE1    1 
ATOM   5498 N NE2    . GLN   B  2 86  ? 40.680 -110.411 -21.643 1.00 72.10  ? 78   GLN   B NE2    1 
ATOM   5499 N N      . THR   B  2 87  ? 41.888 -107.362 -25.766 1.00 39.74  ? 79   THR   B N      1 
ATOM   5500 C CA     . THR   B  2 87  ? 41.798 -106.134 -26.554 1.00 39.14  ? 79   THR   B CA     1 
ATOM   5501 C C      . THR   B  2 87  ? 41.685 -104.970 -25.565 1.00 42.48  ? 79   THR   B C      1 
ATOM   5502 O O      . THR   B  2 87  ? 41.308 -105.176 -24.407 1.00 42.37  ? 79   THR   B O      1 
ATOM   5503 C CB     . THR   B  2 87  ? 40.659 -106.192 -27.590 1.00 43.68  ? 79   THR   B CB     1 
ATOM   5504 O OG1    . THR   B  2 87  ? 39.424 -106.446 -26.929 1.00 41.68  ? 79   THR   B OG1    1 
ATOM   5505 C CG2    . THR   B  2 87  ? 40.886 -107.248 -28.659 1.00 40.98  ? 79   THR   B CG2    1 
ATOM   5506 N N      . GLU   B  2 88  ? 42.048 -103.764 -26.011 1.00 38.90  ? 80   GLU   B N      1 
ATOM   5507 C CA     . GLU   B  2 88  ? 42.022 -102.530 -25.223 1.00 38.67  ? 80   GLU   B CA     1 
ATOM   5508 C C      . GLU   B  2 88  ? 40.599 -102.220 -24.693 1.00 40.83  ? 80   GLU   B C      1 
ATOM   5509 O O      . GLU   B  2 88  ? 40.447 -101.788 -23.548 1.00 40.02  ? 80   GLU   B O      1 
ATOM   5510 C CB     . GLU   B  2 88  ? 42.524 -101.379 -26.108 1.00 40.22  ? 80   GLU   B CB     1 
ATOM   5511 C CG     . GLU   B  2 88  ? 42.748 -100.056 -25.393 1.00 53.68  ? 80   GLU   B CG     1 
ATOM   5512 C CD     . GLU   B  2 88  ? 42.767 -98.828  -26.286 1.00 80.81  ? 80   GLU   B CD     1 
ATOM   5513 O OE1    . GLU   B  2 88  ? 42.965 -97.713  -25.752 1.00 88.01  ? 80   GLU   B OE1    1 
ATOM   5514 O OE2    . GLU   B  2 88  ? 42.558 -98.973  -27.513 1.00 71.16  ? 80   GLU   B OE2    1 
ATOM   5515 N N      . ALA   B  2 89  ? 39.577 -102.447 -25.544 1.00 35.75  ? 81   ALA   B N      1 
ATOM   5516 C CA     . ALA   B  2 89  ? 38.166 -102.181 -25.276 1.00 34.14  ? 81   ALA   B CA     1 
ATOM   5517 C C      . ALA   B  2 89  ? 37.304 -103.350 -25.731 1.00 36.10  ? 81   ALA   B C      1 
ATOM   5518 O O      . ALA   B  2 89  ? 37.828 -104.330 -26.262 1.00 35.68  ? 81   ALA   B O      1 
ATOM   5519 C CB     . ALA   B  2 89  ? 37.747 -100.910 -25.996 1.00 34.43  ? 81   ALA   B CB     1 
ATOM   5520 N N      . GLY   B  2 90  ? 35.990 -103.237 -25.519 1.00 30.88  ? 82   GLY   B N      1 
ATOM   5521 C CA     . GLY   B  2 90  ? 35.024 -104.267 -25.875 1.00 30.14  ? 82   GLY   B CA     1 
ATOM   5522 C C      . GLY   B  2 90  ? 34.959 -104.554 -27.362 1.00 34.07  ? 82   GLY   B C      1 
ATOM   5523 O O      . GLY   B  2 90  ? 35.339 -103.718 -28.189 1.00 32.70  ? 82   GLY   B O      1 
ATOM   5524 N N      . VAL   B  2 91  ? 34.489 -105.759 -27.690 1.00 30.90  ? 83   VAL   B N      1 
ATOM   5525 C CA     . VAL   B  2 91  ? 34.312 -106.259 -29.045 1.00 30.65  ? 83   VAL   B CA     1 
ATOM   5526 C C      . VAL   B  2 91  ? 32.824 -106.112 -29.345 1.00 34.05  ? 83   VAL   B C      1 
ATOM   5527 O O      . VAL   B  2 91  ? 32.005 -106.810 -28.750 1.00 33.10  ? 83   VAL   B O      1 
ATOM   5528 C CB     . VAL   B  2 91  ? 34.798 -107.738 -29.188 1.00 34.22  ? 83   VAL   B CB     1 
ATOM   5529 C CG1    . VAL   B  2 91  ? 34.593 -108.258 -30.616 1.00 34.11  ? 83   VAL   B CG1    1 
ATOM   5530 C CG2    . VAL   B  2 91  ? 36.262 -107.889 -28.764 1.00 33.82  ? 83   VAL   B CG2    1 
ATOM   5531 N N      . ALA   B  2 92  ? 32.475 -105.179 -30.230 1.00 30.52  ? 84   ALA   B N      1 
ATOM   5532 C CA     . ALA   B  2 92  ? 31.079 -104.967 -30.619 1.00 29.72  ? 84   ALA   B CA     1 
ATOM   5533 C C      . ALA   B  2 92  ? 30.718 -105.892 -31.778 1.00 32.77  ? 84   ALA   B C      1 
ATOM   5534 O O      . ALA   B  2 92  ? 29.555 -106.270 -31.923 1.00 32.04  ? 84   ALA   B O      1 
ATOM   5535 C CB     . ALA   B  2 92  ? 30.854 -103.514 -31.008 1.00 30.09  ? 84   ALA   B CB     1 
ATOM   5536 N N      . ASP   B  2 93  ? 31.729 -106.274 -32.590 1.00 29.51  ? 85   ASP   B N      1 
ATOM   5537 C CA     . ASP   B  2 93  ? 31.584 -107.165 -33.755 1.00 28.74  ? 85   ASP   B CA     1 
ATOM   5538 C C      . ASP   B  2 93  ? 32.955 -107.636 -34.254 1.00 32.34  ? 85   ASP   B C      1 
ATOM   5539 O O      . ASP   B  2 93  ? 33.974 -106.989 -33.992 1.00 30.52  ? 85   ASP   B O      1 
ATOM   5540 C CB     . ASP   B  2 93  ? 30.815 -106.448 -34.903 1.00 29.80  ? 85   ASP   B CB     1 
ATOM   5541 C CG     . ASP   B  2 93  ? 30.278 -107.337 -36.023 1.00 40.07  ? 85   ASP   B CG     1 
ATOM   5542 O OD1    . ASP   B  2 93  ? 29.851 -108.485 -35.727 1.00 40.88  ? 85   ASP   B OD1    1 
ATOM   5543 O OD2    . ASP   B  2 93  ? 30.247 -106.870 -37.191 1.00 39.86  ? 85   ASP   B OD2    1 
ATOM   5544 N N      . LEU   B  2 94  ? 32.970 -108.759 -34.987 1.00 30.75  ? 86   LEU   B N      1 
ATOM   5545 C CA     . LEU   B  2 94  ? 34.178 -109.303 -35.597 1.00 31.54  ? 86   LEU   B CA     1 
ATOM   5546 C C      . LEU   B  2 94  ? 33.875 -110.141 -36.828 1.00 38.47  ? 86   LEU   B C      1 
ATOM   5547 O O      . LEU   B  2 94  ? 32.743 -110.599 -37.022 1.00 38.74  ? 86   LEU   B O      1 
ATOM   5548 C CB     . LEU   B  2 94  ? 35.117 -110.059 -34.615 1.00 31.17  ? 86   LEU   B CB     1 
ATOM   5549 C CG     . LEU   B  2 94  ? 34.593 -111.248 -33.798 1.00 35.60  ? 86   LEU   B CG     1 
ATOM   5550 C CD1    . LEU   B  2 94  ? 34.302 -112.473 -34.666 1.00 35.72  ? 86   LEU   B CD1    1 
ATOM   5551 C CD2    . LEU   B  2 94  ? 35.619 -111.669 -32.799 1.00 37.37  ? 86   LEU   B CD2    1 
ATOM   5552 N N      . THR   B  2 95  ? 34.912 -110.371 -37.637 1.00 35.74  ? 87   THR   B N      1 
ATOM   5553 C CA     . THR   B  2 95  ? 34.828 -111.171 -38.857 1.00 35.52  ? 87   THR   B CA     1 
ATOM   5554 C C      . THR   B  2 95  ? 36.190 -111.768 -39.212 1.00 39.16  ? 87   THR   B C      1 
ATOM   5555 O O      . THR   B  2 95  ? 37.237 -111.169 -38.926 1.00 37.82  ? 87   THR   B O      1 
ATOM   5556 C CB     . THR   B  2 95  ? 34.182 -110.357 -40.015 1.00 40.68  ? 87   THR   B CB     1 
ATOM   5557 O OG1    . THR   B  2 95  ? 34.029 -111.180 -41.172 1.00 41.22  ? 87   THR   B OG1    1 
ATOM   5558 C CG2    . THR   B  2 95  ? 34.954 -109.087 -40.360 1.00 37.68  ? 87   THR   B CG2    1 
ATOM   5559 N N      . TRP   B  2 96  ? 36.164 -112.951 -39.839 1.00 36.32  ? 88   TRP   B N      1 
ATOM   5560 C CA     . TRP   B  2 96  ? 37.374 -113.603 -40.332 1.00 36.25  ? 88   TRP   B CA     1 
ATOM   5561 C C      . TRP   B  2 96  ? 37.835 -112.848 -41.586 1.00 43.70  ? 88   TRP   B C      1 
ATOM   5562 O O      . TRP   B  2 96  ? 37.007 -112.417 -42.389 1.00 44.66  ? 88   TRP   B O      1 
ATOM   5563 C CB     . TRP   B  2 96  ? 37.079 -115.066 -40.717 1.00 33.57  ? 88   TRP   B CB     1 
ATOM   5564 C CG     . TRP   B  2 96  ? 37.082 -116.050 -39.584 1.00 33.35  ? 88   TRP   B CG     1 
ATOM   5565 C CD1    . TRP   B  2 96  ? 36.013 -116.745 -39.105 1.00 35.94  ? 88   TRP   B CD1    1 
ATOM   5566 C CD2    . TRP   B  2 96  ? 38.229 -116.536 -38.870 1.00 32.88  ? 88   TRP   B CD2    1 
ATOM   5567 N NE1    . TRP   B  2 96  ? 36.418 -117.629 -38.130 1.00 35.16  ? 88   TRP   B NE1    1 
ATOM   5568 C CE2    . TRP   B  2 96  ? 37.774 -117.517 -37.962 1.00 36.49  ? 88   TRP   B CE2    1 
ATOM   5569 C CE3    . TRP   B  2 96  ? 39.605 -116.256 -38.928 1.00 34.04  ? 88   TRP   B CE3    1 
ATOM   5570 C CZ2    . TRP   B  2 96  ? 38.645 -118.219 -37.117 1.00 35.94  ? 88   TRP   B CZ2    1 
ATOM   5571 C CZ3    . TRP   B  2 96  ? 40.463 -116.930 -38.072 1.00 35.48  ? 88   TRP   B CZ3    1 
ATOM   5572 C CH2    . TRP   B  2 96  ? 39.982 -117.892 -37.173 1.00 36.14  ? 88   TRP   B CH2    1 
ATOM   5573 N N      . VAL   B  2 97  ? 39.142 -112.662 -41.731 1.00 41.94  ? 89   VAL   B N      1 
ATOM   5574 C CA     . VAL   B  2 97  ? 39.762 -112.055 -42.909 1.00 42.34  ? 89   VAL   B CA     1 
ATOM   5575 C C      . VAL   B  2 97  ? 40.654 -113.180 -43.459 1.00 48.45  ? 89   VAL   B C      1 
ATOM   5576 O O      . VAL   B  2 97  ? 41.844 -113.275 -43.137 1.00 48.70  ? 89   VAL   B O      1 
ATOM   5577 C CB     . VAL   B  2 97  ? 40.529 -110.743 -42.594 1.00 46.27  ? 89   VAL   B CB     1 
ATOM   5578 C CG1    . VAL   B  2 97  ? 41.203 -110.177 -43.843 1.00 46.02  ? 89   VAL   B CG1    1 
ATOM   5579 C CG2    . VAL   B  2 97  ? 39.600 -109.705 -41.982 1.00 46.11  ? 89   VAL   B CG2    1 
ATOM   5580 N N      . GLY   B  2 98  ? 40.025 -114.080 -44.199 1.00 45.68  ? 90   GLY   B N      1 
ATOM   5581 C CA     . GLY   B  2 98  ? 40.686 -115.247 -44.757 1.00 45.59  ? 90   GLY   B CA     1 
ATOM   5582 C C      . GLY   B  2 98  ? 40.648 -116.399 -43.779 1.00 49.62  ? 90   GLY   B C      1 
ATOM   5583 O O      . GLY   B  2 98  ? 39.563 -116.817 -43.350 1.00 50.14  ? 90   GLY   B O      1 
ATOM   5584 N N      . GLU   B  2 99  ? 41.834 -116.905 -43.405 1.00 45.11  ? 91   GLU   B N      1 
ATOM   5585 C CA     . GLU   B  2 99  ? 41.957 -118.037 -42.483 1.00 44.62  ? 91   GLU   B CA     1 
ATOM   5586 C C      . GLU   B  2 99  ? 42.710 -117.674 -41.206 1.00 47.44  ? 91   GLU   B C      1 
ATOM   5587 O O      . GLU   B  2 99  ? 42.552 -118.353 -40.193 1.00 47.05  ? 91   GLU   B O      1 
ATOM   5588 C CB     . GLU   B  2 99  ? 42.620 -119.250 -43.182 1.00 45.98  ? 91   GLU   B CB     1 
ATOM   5589 C CG     . GLU   B  2 99  ? 41.822 -119.831 -44.347 1.00 56.14  ? 91   GLU   B CG     1 
ATOM   5590 C CD     . GLU   B  2 99  ? 40.546 -120.577 -43.997 1.00 77.68  ? 91   GLU   B CD     1 
ATOM   5591 O OE1    . GLU   B  2 99  ? 40.617 -121.557 -43.220 1.00 75.42  ? 91   GLU   B OE1    1 
ATOM   5592 O OE2    . GLU   B  2 99  ? 39.479 -120.213 -44.546 1.00 66.47  ? 91   GLU   B OE2    1 
ATOM   5593 N N      . ARG   B  2 100 ? 43.534 -116.618 -41.256 1.00 43.35  ? 92   ARG   B N      1 
ATOM   5594 C CA     . ARG   B  2 100 ? 44.344 -116.179 -40.122 1.00 43.11  ? 92   ARG   B CA     1 
ATOM   5595 C C      . ARG   B  2 100 ? 44.022 -114.760 -39.620 1.00 44.91  ? 92   ARG   B C      1 
ATOM   5596 O O      . ARG   B  2 100 ? 44.407 -114.422 -38.507 1.00 44.70  ? 92   ARG   B O      1 
ATOM   5597 C CB     . ARG   B  2 100 ? 45.842 -116.321 -40.445 1.00 45.10  ? 92   ARG   B CB     1 
ATOM   5598 C CG     . ARG   B  2 100 ? 46.303 -117.777 -40.465 1.00 57.06  ? 92   ARG   B CG     1 
ATOM   5599 C CD     . ARG   B  2 100 ? 47.798 -117.916 -40.666 1.00 68.61  ? 92   ARG   B CD     1 
ATOM   5600 N NE     . ARG   B  2 100 ? 48.223 -119.304 -40.484 1.00 79.71  ? 92   ARG   B NE     1 
ATOM   5601 C CZ     . ARG   B  2 100 ? 49.479 -119.729 -40.580 1.00 94.55  ? 92   ARG   B CZ     1 
ATOM   5602 N NH1    . ARG   B  2 100 ? 50.457 -118.876 -40.860 1.00 84.77  ? 92   ARG   B NH1    1 
ATOM   5603 N NH2    . ARG   B  2 100 ? 49.766 -121.010 -40.395 1.00 79.03  ? 92   ARG   B NH2    1 
ATOM   5604 N N      . GLY   B  2 101 ? 43.329 -113.959 -40.429 1.00 39.22  ? 93   GLY   B N      1 
ATOM   5605 C CA     . GLY   B  2 101 ? 42.969 -112.592 -40.070 1.00 37.84  ? 93   GLY   B CA     1 
ATOM   5606 C C      . GLY   B  2 101 ? 41.670 -112.490 -39.297 1.00 38.92  ? 93   GLY   B C      1 
ATOM   5607 O O      . GLY   B  2 101 ? 40.728 -113.249 -39.546 1.00 37.83  ? 93   GLY   B O      1 
ATOM   5608 N N      . ILE   B  2 102 ? 41.629 -111.564 -38.324 1.00 34.18  ? 94   ILE   B N      1 
ATOM   5609 C CA     . ILE   B  2 102 ? 40.460 -111.291 -37.475 1.00 32.66  ? 94   ILE   B CA     1 
ATOM   5610 C C      . ILE   B  2 102 ? 40.252 -109.781 -37.453 1.00 33.40  ? 94   ILE   B C      1 
ATOM   5611 O O      . ILE   B  2 102 ? 41.107 -109.042 -36.962 1.00 32.05  ? 94   ILE   B O      1 
ATOM   5612 C CB     . ILE   B  2 102 ? 40.585 -111.901 -36.038 1.00 35.43  ? 94   ILE   B CB     1 
ATOM   5613 C CG1    . ILE   B  2 102 ? 40.828 -113.433 -36.080 1.00 35.88  ? 94   ILE   B CG1    1 
ATOM   5614 C CG2    . ILE   B  2 102 ? 39.351 -111.562 -35.168 1.00 34.50  ? 94   ILE   B CG2    1 
ATOM   5615 C CD1    . ILE   B  2 102 ? 41.847 -113.927 -35.090 1.00 42.94  ? 94   ILE   B CD1    1 
ATOM   5616 N N      . LEU   B  2 103 ? 39.133 -109.326 -38.013 1.00 29.63  ? 95   LEU   B N      1 
ATOM   5617 C CA     . LEU   B  2 103 ? 38.806 -107.899 -38.052 1.00 28.84  ? 95   LEU   B CA     1 
ATOM   5618 C C      . LEU   B  2 103 ? 37.753 -107.591 -36.987 1.00 33.01  ? 95   LEU   B C      1 
ATOM   5619 O O      . LEU   B  2 103 ? 36.704 -108.237 -36.948 1.00 32.44  ? 95   LEU   B O      1 
ATOM   5620 C CB     . LEU   B  2 103 ? 38.353 -107.478 -39.451 1.00 28.38  ? 95   LEU   B CB     1 
ATOM   5621 C CG     . LEU   B  2 103 ? 38.241 -105.982 -39.683 1.00 32.35  ? 95   LEU   B CG     1 
ATOM   5622 C CD1    . LEU   B  2 103 ? 39.610 -105.339 -39.861 1.00 32.05  ? 95   LEU   B CD1    1 
ATOM   5623 C CD2    . LEU   B  2 103 ? 37.379 -105.706 -40.878 1.00 36.48  ? 95   LEU   B CD2    1 
ATOM   5624 N N      . VAL   B  2 104 ? 38.067 -106.635 -36.104 1.00 30.08  ? 96   VAL   B N      1 
ATOM   5625 C CA     . VAL   B  2 104 ? 37.258 -106.277 -34.935 1.00 29.38  ? 96   VAL   B CA     1 
ATOM   5626 C C      . VAL   B  2 104 ? 36.701 -104.848 -34.988 1.00 31.36  ? 96   VAL   B C      1 
ATOM   5627 O O      . VAL   B  2 104 ? 37.425 -103.906 -35.301 1.00 30.59  ? 96   VAL   B O      1 
ATOM   5628 C CB     . VAL   B  2 104 ? 38.077 -106.532 -33.625 1.00 33.29  ? 96   VAL   B CB     1 
ATOM   5629 C CG1    . VAL   B  2 104 ? 37.301 -106.127 -32.365 1.00 33.26  ? 96   VAL   B CG1    1 
ATOM   5630 C CG2    . VAL   B  2 104 ? 38.525 -107.985 -33.525 1.00 32.97  ? 96   VAL   B CG2    1 
ATOM   5631 N N      . ALA   B  2 105 ? 35.417 -104.707 -34.631 1.00 27.72  ? 97   ALA   B N      1 
ATOM   5632 C CA     . ALA   B  2 105 ? 34.723 -103.427 -34.461 1.00 27.35  ? 97   ALA   B CA     1 
ATOM   5633 C C      . ALA   B  2 105 ? 34.815 -103.155 -32.938 1.00 30.89  ? 97   ALA   B C      1 
ATOM   5634 O O      . ALA   B  2 105 ? 34.337 -103.968 -32.142 1.00 31.31  ? 97   ALA   B O      1 
ATOM   5635 C CB     . ALA   B  2 105 ? 33.269 -103.558 -34.902 1.00 28.02  ? 97   ALA   B CB     1 
ATOM   5636 N N      . SER   B  2 106 ? 35.520 -102.082 -32.541 1.00 27.37  ? 98   SER   B N      1 
ATOM   5637 C CA     . SER   B  2 106 ? 35.755 -101.759 -31.132 1.00 28.15  ? 98   SER   B CA     1 
ATOM   5638 C C      . SER   B  2 106 ? 34.945 -100.568 -30.592 1.00 31.95  ? 98   SER   B C      1 
ATOM   5639 O O      . SER   B  2 106 ? 34.627 -99.631  -31.331 1.00 30.95  ? 98   SER   B O      1 
ATOM   5640 C CB     . SER   B  2 106 ? 37.246 -101.538 -30.881 1.00 32.35  ? 98   SER   B CB     1 
ATOM   5641 O OG     . SER   B  2 106 ? 37.527 -101.212 -29.528 1.00 41.33  ? 98   SER   B OG     1 
ATOM   5642 N N      . ASP   B  2 107 ? 34.670 -100.601 -29.269 1.00 28.14  ? 99   ASP   B N      1 
ATOM   5643 C CA     . ASP   B  2 107 ? 33.991 -99.552  -28.500 1.00 27.84  ? 99   ASP   B CA     1 
ATOM   5644 C C      . ASP   B  2 107 ? 34.771 -98.246  -28.538 1.00 31.39  ? 99   ASP   B C      1 
ATOM   5645 O O      . ASP   B  2 107 ? 34.179 -97.180  -28.379 1.00 32.16  ? 99   ASP   B O      1 
ATOM   5646 C CB     . ASP   B  2 107 ? 33.864 -99.981  -27.028 1.00 29.62  ? 99   ASP   B CB     1 
ATOM   5647 C CG     . ASP   B  2 107 ? 32.711 -100.902 -26.715 1.00 41.59  ? 99   ASP   B CG     1 
ATOM   5648 O OD1    . ASP   B  2 107 ? 31.613 -100.692 -27.273 1.00 42.92  ? 99   ASP   B OD1    1 
ATOM   5649 O OD2    . ASP   B  2 107 ? 32.875 -101.772 -25.839 1.00 48.99  ? 99   ASP   B OD2    1 
ATOM   5650 N N      . SER   B  2 108 ? 36.105 -98.330  -28.709 1.00 27.17  ? 100  SER   B N      1 
ATOM   5651 C CA     . SER   B  2 108 ? 37.034 -97.191  -28.762 1.00 26.78  ? 100  SER   B CA     1 
ATOM   5652 C C      . SER   B  2 108 ? 36.911 -96.330  -30.028 1.00 30.79  ? 100  SER   B C      1 
ATOM   5653 O O      . SER   B  2 108 ? 37.515 -95.262  -30.101 1.00 30.50  ? 100  SER   B O      1 
ATOM   5654 C CB     . SER   B  2 108 ? 38.468 -97.697  -28.652 1.00 29.71  ? 100  SER   B CB     1 
ATOM   5655 O OG     . SER   B  2 108 ? 38.780 -98.518  -29.765 1.00 35.19  ? 100  SER   B OG     1 
ATOM   5656 N N      . GLY   B  2 109 ? 36.197 -96.825  -31.029 1.00 28.65  ? 101  GLY   B N      1 
ATOM   5657 C CA     . GLY   B  2 109 ? 36.079 -96.142  -32.307 1.00 29.25  ? 101  GLY   B CA     1 
ATOM   5658 C C      . GLY   B  2 109 ? 37.081 -96.690  -33.307 1.00 33.75  ? 101  GLY   B C      1 
ATOM   5659 O O      . GLY   B  2 109 ? 37.084 -96.291  -34.471 1.00 33.54  ? 101  GLY   B O      1 
ATOM   5660 N N      . ALA   B  2 110 ? 37.905 -97.649  -32.867 1.00 29.33  ? 102  ALA   B N      1 
ATOM   5661 C CA     . ALA   B  2 110 ? 38.900 -98.287  -33.721 1.00 29.14  ? 102  ALA   B CA     1 
ATOM   5662 C C      . ALA   B  2 110 ? 38.352 -99.495  -34.460 1.00 32.02  ? 102  ALA   B C      1 
ATOM   5663 O O      . ALA   B  2 110 ? 37.498 -100.223 -33.948 1.00 30.50  ? 102  ALA   B O      1 
ATOM   5664 C CB     . ALA   B  2 110 ? 40.109 -98.721  -32.892 1.00 29.54  ? 102  ALA   B CB     1 
ATOM   5665 N N      . VAL   B  2 111 ? 38.878 -99.706  -35.670 1.00 29.30  ? 103  VAL   B N      1 
ATOM   5666 C CA     . VAL   B  2 111 ? 38.687 -100.913 -36.461 1.00 29.43  ? 103  VAL   B CA     1 
ATOM   5667 C C      . VAL   B  2 111 ? 40.067 -101.567 -36.313 1.00 34.10  ? 103  VAL   B C      1 
ATOM   5668 O O      . VAL   B  2 111 ? 41.092 -100.901 -36.507 1.00 33.14  ? 103  VAL   B O      1 
ATOM   5669 C CB     . VAL   B  2 111 ? 38.265 -100.660 -37.928 1.00 33.41  ? 103  VAL   B CB     1 
ATOM   5670 C CG1    . VAL   B  2 111 ? 38.453 -101.911 -38.791 1.00 33.09  ? 103  VAL   B CG1    1 
ATOM   5671 C CG2    . VAL   B  2 111 ? 36.816 -100.189 -37.990 1.00 33.09  ? 103  VAL   B CG2    1 
ATOM   5672 N N      . GLU   B  2 112 ? 40.105 -102.805 -35.833 1.00 31.76  ? 104  GLU   B N      1 
ATOM   5673 C CA     . GLU   B  2 112 ? 41.396 -103.433 -35.608 1.00 32.43  ? 104  GLU   B CA     1 
ATOM   5674 C C      . GLU   B  2 112 ? 41.533 -104.776 -36.294 1.00 36.51  ? 104  GLU   B C      1 
ATOM   5675 O O      . GLU   B  2 112 ? 40.600 -105.586 -36.322 1.00 34.78  ? 104  GLU   B O      1 
ATOM   5676 C CB     . GLU   B  2 112 ? 41.770 -103.517 -34.117 1.00 34.22  ? 104  GLU   B CB     1 
ATOM   5677 C CG     . GLU   B  2 112 ? 40.623 -103.779 -33.158 1.00 49.45  ? 104  GLU   B CG     1 
ATOM   5678 C CD     . GLU   B  2 112 ? 40.979 -103.623 -31.692 1.00 76.81  ? 104  GLU   B CD     1 
ATOM   5679 O OE1    . GLU   B  2 112 ? 41.202 -104.656 -31.021 1.00 78.31  ? 104  GLU   B OE1    1 
ATOM   5680 O OE2    . GLU   B  2 112 ? 41.025 -102.468 -31.211 1.00 73.74  ? 104  GLU   B OE2    1 
ATOM   5681 N N      . LEU   B  2 113 ? 42.700 -104.978 -36.896 1.00 34.13  ? 105  LEU   B N      1 
ATOM   5682 C CA     . LEU   B  2 113 ? 43.020 -106.231 -37.557 1.00 34.74  ? 105  LEU   B CA     1 
ATOM   5683 C C      . LEU   B  2 113 ? 44.034 -106.963 -36.710 1.00 39.92  ? 105  LEU   B C      1 
ATOM   5684 O O      . LEU   B  2 113 ? 45.064 -106.405 -36.323 1.00 38.63  ? 105  LEU   B O      1 
ATOM   5685 C CB     . LEU   B  2 113 ? 43.526 -106.023 -38.997 1.00 34.71  ? 105  LEU   B CB     1 
ATOM   5686 C CG     . LEU   B  2 113 ? 43.826 -107.286 -39.836 1.00 38.58  ? 105  LEU   B CG     1 
ATOM   5687 C CD1    . LEU   B  2 113 ? 42.574 -108.105 -40.098 1.00 38.18  ? 105  LEU   B CD1    1 
ATOM   5688 C CD2    . LEU   B  2 113 ? 44.488 -106.915 -41.146 1.00 40.84  ? 105  LEU   B CD2    1 
ATOM   5689 N N      . TRP   B  2 114 ? 43.682 -108.191 -36.369 1.00 39.15  ? 106  TRP   B N      1 
ATOM   5690 C CA     . TRP   B  2 114 ? 44.478 -109.114 -35.588 1.00 40.46  ? 106  TRP   B CA     1 
ATOM   5691 C C      . TRP   B  2 114 ? 44.832 -110.273 -36.506 1.00 46.23  ? 106  TRP   B C      1 
ATOM   5692 O O      . TRP   B  2 114 ? 44.026 -110.657 -37.354 1.00 44.78  ? 106  TRP   B O      1 
ATOM   5693 C CB     . TRP   B  2 114 ? 43.681 -109.605 -34.375 1.00 39.84  ? 106  TRP   B CB     1 
ATOM   5694 C CG     . TRP   B  2 114 ? 43.445 -108.539 -33.344 1.00 41.58  ? 106  TRP   B CG     1 
ATOM   5695 C CD1    . TRP   B  2 114 ? 42.441 -107.616 -33.336 1.00 44.60  ? 106  TRP   B CD1    1 
ATOM   5696 C CD2    . TRP   B  2 114 ? 44.243 -108.277 -32.180 1.00 41.78  ? 106  TRP   B CD2    1 
ATOM   5697 N NE1    . TRP   B  2 114 ? 42.560 -106.795 -32.237 1.00 44.48  ? 106  TRP   B NE1    1 
ATOM   5698 C CE2    . TRP   B  2 114 ? 43.647 -107.190 -31.500 1.00 46.02  ? 106  TRP   B CE2    1 
ATOM   5699 C CE3    . TRP   B  2 114 ? 45.388 -108.877 -31.625 1.00 43.24  ? 106  TRP   B CE3    1 
ATOM   5700 C CZ2    . TRP   B  2 114 ? 44.171 -106.676 -30.308 1.00 45.45  ? 106  TRP   B CZ2    1 
ATOM   5701 C CZ3    . TRP   B  2 114 ? 45.904 -108.371 -30.440 1.00 45.00  ? 106  TRP   B CZ3    1 
ATOM   5702 C CH2    . TRP   B  2 114 ? 45.298 -107.286 -29.792 1.00 45.75  ? 106  TRP   B CH2    1 
ATOM   5703 N N      . GLU   B  2 115 ? 46.041 -110.813 -36.362 1.00 44.94  ? 107  GLU   B N      1 
ATOM   5704 C CA     . GLU   B  2 115 ? 46.491 -111.915 -37.197 1.00 45.56  ? 107  GLU   B CA     1 
ATOM   5705 C C      . GLU   B  2 115 ? 46.983 -113.085 -36.363 1.00 50.59  ? 107  GLU   B C      1 
ATOM   5706 O O      . GLU   B  2 115 ? 47.746 -112.905 -35.414 1.00 49.63  ? 107  GLU   B O      1 
ATOM   5707 C CB     . GLU   B  2 115 ? 47.559 -111.436 -38.187 1.00 47.25  ? 107  GLU   B CB     1 
ATOM   5708 C CG     . GLU   B  2 115 ? 47.491 -112.134 -39.532 1.00 61.86  ? 107  GLU   B CG     1 
ATOM   5709 C CD     . GLU   B  2 115 ? 48.082 -111.337 -40.679 1.00 91.81  ? 107  GLU   B CD     1 
ATOM   5710 O OE1    . GLU   B  2 115 ? 47.300 -110.706 -41.427 1.00 89.17  ? 107  GLU   B OE1    1 
ATOM   5711 O OE2    . GLU   B  2 115 ? 49.326 -111.342 -40.830 1.00 89.88  ? 107  GLU   B OE2    1 
ATOM   5712 N N      . LEU   B  2 116 ? 46.492 -114.279 -36.697 1.00 49.01  ? 108  LEU   B N      1 
ATOM   5713 C CA     . LEU   B  2 116 ? 46.855 -115.554 -36.089 1.00 49.93  ? 108  LEU   B CA     1 
ATOM   5714 C C      . LEU   B  2 116 ? 48.264 -115.880 -36.593 1.00 56.09  ? 108  LEU   B C      1 
ATOM   5715 O O      . LEU   B  2 116 ? 48.505 -115.807 -37.801 1.00 56.27  ? 108  LEU   B O      1 
ATOM   5716 C CB     . LEU   B  2 116 ? 45.854 -116.610 -36.585 1.00 50.00  ? 108  LEU   B CB     1 
ATOM   5717 C CG     . LEU   B  2 116 ? 45.492 -117.784 -35.688 1.00 54.83  ? 108  LEU   B CG     1 
ATOM   5718 C CD1    . LEU   B  2 116 ? 45.036 -117.332 -34.301 1.00 54.77  ? 108  LEU   B CD1    1 
ATOM   5719 C CD2    . LEU   B  2 116 ? 44.380 -118.589 -36.328 1.00 57.31  ? 108  LEU   B CD2    1 
ATOM   5720 N N      . ASP   B  2 117 ? 49.203 -116.187 -35.677 1.00 53.92  ? 109  ASP   B N      1 
ATOM   5721 C CA     . ASP   B  2 117 ? 50.599 -116.482 -36.036 1.00 54.34  ? 109  ASP   B CA     1 
ATOM   5722 C C      . ASP   B  2 117 ? 50.778 -117.837 -36.771 1.00 58.82  ? 109  ASP   B C      1 
ATOM   5723 O O      . ASP   B  2 117 ? 49.808 -118.582 -36.943 1.00 57.57  ? 109  ASP   B O      1 
ATOM   5724 C CB     . ASP   B  2 117 ? 51.528 -116.364 -34.807 1.00 56.13  ? 109  ASP   B CB     1 
ATOM   5725 C CG     . ASP   B  2 117 ? 51.405 -117.437 -33.737 1.00 65.25  ? 109  ASP   B CG     1 
ATOM   5726 O OD1    . ASP   B  2 117 ? 52.355 -117.587 -32.943 1.00 67.66  ? 109  ASP   B OD1    1 
ATOM   5727 O OD2    . ASP   B  2 117 ? 50.335 -118.087 -33.657 1.00 66.20  ? 109  ASP   B OD2    1 
ATOM   5728 N N      . GLU   B  2 118 ? 52.021 -118.122 -37.232 1.00 56.99  ? 110  GLU   B N      1 
ATOM   5729 C CA     . GLU   B  2 118 ? 52.396 -119.336 -37.975 1.00 57.14  ? 110  GLU   B CA     1 
ATOM   5730 C C      . GLU   B  2 118 ? 51.956 -120.639 -37.280 1.00 59.52  ? 110  GLU   B C      1 
ATOM   5731 O O      . GLU   B  2 118 ? 51.355 -121.499 -37.934 1.00 58.74  ? 110  GLU   B O      1 
ATOM   5732 C CB     . GLU   B  2 118 ? 53.903 -119.358 -38.327 1.00 58.90  ? 110  GLU   B CB     1 
ATOM   5733 C CG     . GLU   B  2 118 ? 54.856 -119.113 -37.162 1.00 74.26  ? 110  GLU   B CG     1 
ATOM   5734 C CD     . GLU   B  2 118 ? 56.324 -119.300 -37.495 1.00 102.43 ? 110  GLU   B CD     1 
ATOM   5735 O OE1    . GLU   B  2 118 ? 56.960 -118.324 -37.955 1.00 102.31 ? 110  GLU   B OE1    1 
ATOM   5736 O OE2    . GLU   B  2 118 ? 56.842 -120.421 -37.283 1.00 96.86  ? 110  GLU   B OE2    1 
ATOM   5737 N N      . ASN   B  2 119 ? 52.198 -120.752 -35.956 1.00 55.14  ? 111  ASN   B N      1 
ATOM   5738 C CA     . ASN   B  2 119 ? 51.822 -121.934 -35.173 1.00 54.56  ? 111  ASN   B CA     1 
ATOM   5739 C C      . ASN   B  2 119 ? 50.359 -121.903 -34.696 1.00 55.89  ? 111  ASN   B C      1 
ATOM   5740 O O      . ASN   B  2 119 ? 49.877 -122.903 -34.156 1.00 54.96  ? 111  ASN   B O      1 
ATOM   5741 C CB     . ASN   B  2 119 ? 52.801 -122.194 -34.008 1.00 58.32  ? 111  ASN   B CB     1 
ATOM   5742 C CG     . ASN   B  2 119 ? 53.610 -121.001 -33.552 1.00 89.71  ? 111  ASN   B CG     1 
ATOM   5743 O OD1    . ASN   B  2 119 ? 53.201 -120.243 -32.673 1.00 85.68  ? 111  ASN   B OD1    1 
ATOM   5744 N ND2    . ASN   B  2 119 ? 54.802 -120.839 -34.107 1.00 82.87  ? 111  ASN   B ND2    1 
ATOM   5745 N N      . GLU   B  2 120 ? 49.646 -120.771 -34.945 1.00 51.41  ? 112  GLU   B N      1 
ATOM   5746 C CA     . GLU   B  2 120 ? 48.235 -120.513 -34.596 1.00 50.37  ? 112  GLU   B CA     1 
ATOM   5747 C C      . GLU   B  2 120 ? 47.975 -120.649 -33.081 1.00 52.80  ? 112  GLU   B C      1 
ATOM   5748 O O      . GLU   B  2 120 ? 46.927 -121.143 -32.659 1.00 52.34  ? 112  GLU   B O      1 
ATOM   5749 C CB     . GLU   B  2 120 ? 47.266 -121.370 -35.445 1.00 51.60  ? 112  GLU   B CB     1 
ATOM   5750 C CG     . GLU   B  2 120 ? 47.232 -120.980 -36.918 1.00 58.81  ? 112  GLU   B CG     1 
ATOM   5751 C CD     . GLU   B  2 120 ? 46.088 -121.539 -37.746 1.00 75.90  ? 112  GLU   B CD     1 
ATOM   5752 O OE1    . GLU   B  2 120 ? 45.254 -122.296 -37.196 1.00 63.27  ? 112  GLU   B OE1    1 
ATOM   5753 O OE2    . GLU   B  2 120 ? 46.025 -121.216 -38.955 1.00 70.77  ? 112  GLU   B OE2    1 
ATOM   5754 N N      . THR   B  2 121 ? 48.947 -120.197 -32.272 1.00 48.53  ? 113  THR   B N      1 
ATOM   5755 C CA     . THR   B  2 121 ? 48.908 -120.257 -30.805 1.00 48.09  ? 113  THR   B CA     1 
ATOM   5756 C C      . THR   B  2 121 ? 48.903 -118.857 -30.179 1.00 50.56  ? 113  THR   B C      1 
ATOM   5757 O O      . THR   B  2 121 ? 48.717 -118.718 -28.967 1.00 49.92  ? 113  THR   B O      1 
ATOM   5758 C CB     . THR   B  2 121 ? 50.063 -121.129 -30.276 1.00 55.35  ? 113  THR   B CB     1 
ATOM   5759 O OG1    . THR   B  2 121 ? 51.305 -120.593 -30.739 1.00 52.49  ? 113  THR   B OG1    1 
ATOM   5760 C CG2    . THR   B  2 121 ? 49.924 -122.601 -30.677 1.00 53.41  ? 113  THR   B CG2    1 
ATOM   5761 N N      . LEU   B  2 122 ? 49.117 -117.828 -31.014 1.00 46.11  ? 114  LEU   B N      1 
ATOM   5762 C CA     . LEU   B  2 122 ? 49.123 -116.426 -30.621 1.00 45.81  ? 114  LEU   B CA     1 
ATOM   5763 C C      . LEU   B  2 122 ? 48.237 -115.610 -31.566 1.00 48.55  ? 114  LEU   B C      1 
ATOM   5764 O O      . LEU   B  2 122 ? 47.984 -116.024 -32.704 1.00 47.79  ? 114  LEU   B O      1 
ATOM   5765 C CB     . LEU   B  2 122 ? 50.560 -115.864 -30.610 1.00 46.11  ? 114  LEU   B CB     1 
ATOM   5766 C CG     . LEU   B  2 122 ? 51.463 -116.279 -29.444 1.00 51.21  ? 114  LEU   B CG     1 
ATOM   5767 C CD1    . LEU   B  2 122 ? 52.916 -116.269 -29.860 1.00 51.52  ? 114  LEU   B CD1    1 
ATOM   5768 C CD2    . LEU   B  2 122 ? 51.270 -115.365 -28.236 1.00 52.86  ? 114  LEU   B CD2    1 
ATOM   5769 N N      . ILE   B  2 123 ? 47.733 -114.467 -31.067 1.00 44.12  ? 115  ILE   B N      1 
ATOM   5770 C CA     . ILE   B  2 123 ? 46.903 -113.516 -31.812 1.00 43.06  ? 115  ILE   B CA     1 
ATOM   5771 C C      . ILE   B  2 123 ? 47.609 -112.178 -31.639 1.00 46.98  ? 115  ILE   B C      1 
ATOM   5772 O O      . ILE   B  2 123 ? 47.669 -111.649 -30.524 1.00 47.00  ? 115  ILE   B O      1 
ATOM   5773 C CB     . ILE   B  2 123 ? 45.403 -113.509 -31.356 1.00 45.77  ? 115  ILE   B CB     1 
ATOM   5774 C CG1    . ILE   B  2 123 ? 44.761 -114.915 -31.494 1.00 45.24  ? 115  ILE   B CG1    1 
ATOM   5775 C CG2    . ILE   B  2 123 ? 44.589 -112.463 -32.147 1.00 46.82  ? 115  ILE   B CG2    1 
ATOM   5776 C CD1    . ILE   B  2 123 ? 43.473 -115.168 -30.685 1.00 47.02  ? 115  ILE   B CD1    1 
ATOM   5777 N N      . VAL   B  2 124 ? 48.229 -111.688 -32.724 1.00 43.54  ? 116  VAL   B N      1 
ATOM   5778 C CA     . VAL   B  2 124 ? 49.018 -110.453 -32.735 1.00 43.42  ? 116  VAL   B CA     1 
ATOM   5779 C C      . VAL   B  2 124 ? 48.282 -109.337 -33.492 1.00 48.07  ? 116  VAL   B C      1 
ATOM   5780 O O      . VAL   B  2 124 ? 47.605 -109.614 -34.483 1.00 47.87  ? 116  VAL   B O      1 
ATOM   5781 C CB     . VAL   B  2 124 ? 50.473 -110.717 -33.251 1.00 47.34  ? 116  VAL   B CB     1 
ATOM   5782 C CG1    . VAL   B  2 124 ? 50.512 -111.101 -34.731 1.00 47.01  ? 116  VAL   B CG1    1 
ATOM   5783 C CG2    . VAL   B  2 124 ? 51.409 -109.547 -32.965 1.00 47.20  ? 116  VAL   B CG2    1 
ATOM   5784 N N      . SER   B  2 125 ? 48.392 -108.088 -33.016 1.00 44.68  ? 117  SER   B N      1 
ATOM   5785 C CA     . SER   B  2 125 ? 47.747 -106.961 -33.682 1.00 44.16  ? 117  SER   B CA     1 
ATOM   5786 C C      . SER   B  2 125 ? 48.540 -106.522 -34.912 1.00 47.97  ? 117  SER   B C      1 
ATOM   5787 O O      . SER   B  2 125 ? 49.753 -106.302 -34.820 1.00 47.62  ? 117  SER   B O      1 
ATOM   5788 C CB     . SER   B  2 125 ? 47.562 -105.789 -32.721 1.00 46.44  ? 117  SER   B CB     1 
ATOM   5789 O OG     . SER   B  2 125 ? 46.942 -104.693 -33.375 1.00 52.67  ? 117  SER   B OG     1 
ATOM   5790 N N      . LYS   B  2 126 ? 47.842 -106.389 -36.055 1.00 44.17  ? 118  LYS   B N      1 
ATOM   5791 C CA     . LYS   B  2 126 ? 48.408 -105.912 -37.315 1.00 44.00  ? 118  LYS   B CA     1 
ATOM   5792 C C      . LYS   B  2 126 ? 48.222 -104.380 -37.384 1.00 47.00  ? 118  LYS   B C      1 
ATOM   5793 O O      . LYS   B  2 126 ? 49.186 -103.648 -37.625 1.00 45.68  ? 118  LYS   B O      1 
ATOM   5794 C CB     . LYS   B  2 126 ? 47.751 -106.629 -38.509 1.00 47.12  ? 118  LYS   B CB     1 
ATOM   5795 C CG     . LYS   B  2 126 ? 48.476 -106.425 -39.839 1.00 69.12  ? 118  LYS   B CG     1 
ATOM   5796 C CD     . LYS   B  2 126 ? 49.531 -107.504 -40.113 1.00 81.36  ? 118  LYS   B CD     1 
ATOM   5797 C CE     . LYS   B  2 126 ? 50.167 -107.361 -41.479 1.00 92.13  ? 118  LYS   B CE     1 
ATOM   5798 N NZ     . LYS   B  2 126 ? 49.243 -107.760 -42.576 1.00 100.12 ? 118  LYS   B NZ     1 
ATOM   5799 N N      . PHE   B  2 127 ? 46.979 -103.903 -37.142 1.00 43.24  ? 119  PHE   B N      1 
ATOM   5800 C CA     . PHE   B  2 127 ? 46.654 -102.478 -37.097 1.00 41.99  ? 119  PHE   B CA     1 
ATOM   5801 C C      . PHE   B  2 127 ? 45.495 -102.172 -36.156 1.00 44.86  ? 119  PHE   B C      1 
ATOM   5802 O O      . PHE   B  2 127 ? 44.597 -102.993 -35.963 1.00 44.13  ? 119  PHE   B O      1 
ATOM   5803 C CB     . PHE   B  2 127 ? 46.429 -101.859 -38.500 1.00 43.35  ? 119  PHE   B CB     1 
ATOM   5804 C CG     . PHE   B  2 127 ? 45.150 -102.179 -39.246 1.00 44.41  ? 119  PHE   B CG     1 
ATOM   5805 C CD1    . PHE   B  2 127 ? 43.951 -101.548 -38.912 1.00 46.95  ? 119  PHE   B CD1    1 
ATOM   5806 C CD2    . PHE   B  2 127 ? 45.163 -103.027 -40.346 1.00 45.73  ? 119  PHE   B CD2    1 
ATOM   5807 C CE1    . PHE   B  2 127 ? 42.773 -101.828 -39.614 1.00 47.40  ? 119  PHE   B CE1    1 
ATOM   5808 C CE2    . PHE   B  2 127 ? 43.992 -103.276 -41.074 1.00 48.50  ? 119  PHE   B CE2    1 
ATOM   5809 C CZ     . PHE   B  2 127 ? 42.801 -102.688 -40.692 1.00 46.72  ? 119  PHE   B CZ     1 
ATOM   5810 N N      . CYS   B  2 128 ? 45.528 -100.969 -35.587 1.00 40.71  ? 120  CYS   B N      1 
ATOM   5811 C CA     . CYS   B  2 128 ? 44.496 -100.423 -34.724 1.00 40.15  ? 120  CYS   B CA     1 
ATOM   5812 C C      . CYS   B  2 128 ? 44.382 -98.973  -35.145 1.00 43.21  ? 120  CYS   B C      1 
ATOM   5813 O O      . CYS   B  2 128 ? 45.228 -98.149  -34.775 1.00 43.52  ? 120  CYS   B O      1 
ATOM   5814 C CB     . CYS   B  2 128 ? 44.871 -100.568 -33.250 1.00 40.43  ? 120  CYS   B CB     1 
ATOM   5815 S SG     . CYS   B  2 128 ? 43.593 -99.996  -32.104 1.00 44.10  ? 120  CYS   B SG     1 
ATOM   5816 N N      . LYS   B  2 129 ? 43.405 -98.691  -36.022 1.00 39.04  ? 121  LYS   B N      1 
ATOM   5817 C CA     . LYS   B  2 129 ? 43.192 -97.348  -36.571 1.00 38.58  ? 121  LYS   B CA     1 
ATOM   5818 C C      . LYS   B  2 129 ? 41.916 -96.714  -36.021 1.00 41.37  ? 121  LYS   B C      1 
ATOM   5819 O O      . LYS   B  2 129 ? 40.821 -97.252  -36.198 1.00 39.96  ? 121  LYS   B O      1 
ATOM   5820 C CB     . LYS   B  2 129 ? 43.203 -97.356  -38.118 1.00 40.68  ? 121  LYS   B CB     1 
ATOM   5821 C CG     . LYS   B  2 129 ? 44.484 -97.906  -38.762 1.00 48.83  ? 121  LYS   B CG     1 
ATOM   5822 C CD     . LYS   B  2 129 ? 45.612 -96.887  -38.838 1.00 54.89  ? 121  LYS   B CD     1 
ATOM   5823 C CE     . LYS   B  2 129 ? 46.912 -97.546  -39.215 1.00 60.39  ? 121  LYS   B CE     1 
ATOM   5824 N NZ     . LYS   B  2 129 ? 48.023 -96.566  -39.287 1.00 68.70  ? 121  LYS   B NZ     1 
ATOM   5825 N N      . TYR   B  2 130 ? 42.076 -95.577  -35.332 1.00 38.30  ? 122  TYR   B N      1 
ATOM   5826 C CA     . TYR   B  2 130 ? 40.983 -94.823  -34.714 1.00 37.70  ? 122  TYR   B CA     1 
ATOM   5827 C C      . TYR   B  2 130 ? 40.466 -93.790  -35.710 1.00 40.19  ? 122  TYR   B C      1 
ATOM   5828 O O      . TYR   B  2 130 ? 40.964 -92.662  -35.745 1.00 40.79  ? 122  TYR   B O      1 
ATOM   5829 C CB     . TYR   B  2 130 ? 41.455 -94.146  -33.411 1.00 38.63  ? 122  TYR   B CB     1 
ATOM   5830 C CG     . TYR   B  2 130 ? 42.051 -95.089  -32.391 1.00 40.46  ? 122  TYR   B CG     1 
ATOM   5831 C CD1    . TYR   B  2 130 ? 43.415 -95.370  -32.386 1.00 42.62  ? 122  TYR   B CD1    1 
ATOM   5832 C CD2    . TYR   B  2 130 ? 41.265 -95.651  -31.389 1.00 41.37  ? 122  TYR   B CD2    1 
ATOM   5833 C CE1    . TYR   B  2 130 ? 43.976 -96.226  -31.439 1.00 43.59  ? 122  TYR   B CE1    1 
ATOM   5834 C CE2    . TYR   B  2 130 ? 41.813 -96.510  -30.436 1.00 42.60  ? 122  TYR   B CE2    1 
ATOM   5835 C CZ     . TYR   B  2 130 ? 43.171 -96.794  -30.465 1.00 51.09  ? 122  TYR   B CZ     1 
ATOM   5836 O OH     . TYR   B  2 130 ? 43.725 -97.640  -29.540 1.00 52.77  ? 122  TYR   B OH     1 
ATOM   5837 N N      . GLU   B  2 131 ? 39.496 -94.196  -36.543 1.00 35.41  ? 123  GLU   B N      1 
ATOM   5838 C CA     . GLU   B  2 131 ? 38.898 -93.359  -37.596 1.00 34.79  ? 123  GLU   B CA     1 
ATOM   5839 C C      . GLU   B  2 131 ? 37.436 -92.975  -37.323 1.00 36.18  ? 123  GLU   B C      1 
ATOM   5840 O O      . GLU   B  2 131 ? 36.939 -92.002  -37.894 1.00 35.61  ? 123  GLU   B O      1 
ATOM   5841 C CB     . GLU   B  2 131 ? 39.042 -94.030  -38.978 1.00 36.16  ? 123  GLU   B CB     1 
ATOM   5842 C CG     . GLU   B  2 131 ? 40.478 -94.091  -39.479 1.00 48.39  ? 123  GLU   B CG     1 
ATOM   5843 C CD     . GLU   B  2 131 ? 41.139 -92.763  -39.792 1.00 70.31  ? 123  GLU   B CD     1 
ATOM   5844 O OE1    . GLU   B  2 131 ? 40.603 -92.008  -40.635 1.00 70.16  ? 123  GLU   B OE1    1 
ATOM   5845 O OE2    . GLU   B  2 131 ? 42.211 -92.490  -39.208 1.00 66.97  ? 123  GLU   B OE2    1 
ATOM   5846 N N      . HIS   B  2 132 ? 36.750 -93.750  -36.476 1.00 31.34  ? 124  HIS   B N      1 
ATOM   5847 C CA     . HIS   B  2 132 ? 35.377 -93.475  -36.076 1.00 30.14  ? 124  HIS   B CA     1 
ATOM   5848 C C      . HIS   B  2 132 ? 35.359 -92.616  -34.804 1.00 34.17  ? 124  HIS   B C      1 
ATOM   5849 O O      . HIS   B  2 132 ? 36.260 -92.719  -33.963 1.00 33.97  ? 124  HIS   B O      1 
ATOM   5850 C CB     . HIS   B  2 132 ? 34.564 -94.760  -35.908 1.00 29.66  ? 124  HIS   B CB     1 
ATOM   5851 C CG     . HIS   B  2 132 ? 34.163 -95.395  -37.206 1.00 32.44  ? 124  HIS   B CG     1 
ATOM   5852 N ND1    . HIS   B  2 132 ? 33.264 -94.784  -38.066 1.00 33.87  ? 124  HIS   B ND1    1 
ATOM   5853 C CD2    . HIS   B  2 132 ? 34.517 -96.592  -37.727 1.00 33.45  ? 124  HIS   B CD2    1 
ATOM   5854 C CE1    . HIS   B  2 132 ? 33.090 -95.634  -39.063 1.00 32.91  ? 124  HIS   B CE1    1 
ATOM   5855 N NE2    . HIS   B  2 132 ? 33.832 -96.730  -38.907 1.00 32.99  ? 124  HIS   B NE2    1 
ATOM   5856 N N      . ASP   B  2 133 ? 34.352 -91.745  -34.688 1.00 29.58  ? 125  ASP   B N      1 
ATOM   5857 C CA     . ASP   B  2 133 ? 34.232 -90.834  -33.550 1.00 28.36  ? 125  ASP   B CA     1 
ATOM   5858 C C      . ASP   B  2 133 ? 33.372 -91.377  -32.398 1.00 31.40  ? 125  ASP   B C      1 
ATOM   5859 O O      . ASP   B  2 133 ? 33.206 -90.701  -31.385 1.00 32.32  ? 125  ASP   B O      1 
ATOM   5860 C CB     . ASP   B  2 133 ? 33.744 -89.465  -34.030 1.00 29.87  ? 125  ASP   B CB     1 
ATOM   5861 C CG     . ASP   B  2 133 ? 34.804 -88.704  -34.802 1.00 37.64  ? 125  ASP   B CG     1 
ATOM   5862 O OD1    . ASP   B  2 133 ? 35.974 -88.666  -34.335 1.00 35.24  ? 125  ASP   B OD1    1 
ATOM   5863 O OD2    . ASP   B  2 133 ? 34.462 -88.116  -35.850 1.00 45.17  ? 125  ASP   B OD2    1 
ATOM   5864 N N      . ASP   B  2 134 ? 32.858 -92.597  -32.545 1.00 26.55  ? 126  ASP   B N      1 
ATOM   5865 C CA     . ASP   B  2 134 ? 32.049 -93.294  -31.549 1.00 26.27  ? 126  ASP   B CA     1 
ATOM   5866 C C      . ASP   B  2 134 ? 32.242 -94.797  -31.772 1.00 29.83  ? 126  ASP   B C      1 
ATOM   5867 O O      . ASP   B  2 134 ? 32.962 -95.182  -32.690 1.00 30.03  ? 126  ASP   B O      1 
ATOM   5868 C CB     . ASP   B  2 134 ? 30.563 -92.911  -31.718 1.00 28.04  ? 126  ASP   B CB     1 
ATOM   5869 C CG     . ASP   B  2 134 ? 29.703 -92.956  -30.463 1.00 34.38  ? 126  ASP   B CG     1 
ATOM   5870 O OD1    . ASP   B  2 134 ? 29.979 -93.802  -29.571 1.00 32.47  ? 126  ASP   B OD1    1 
ATOM   5871 O OD2    . ASP   B  2 134 ? 28.704 -92.214  -30.409 1.00 41.41  ? 126  ASP   B OD2    1 
ATOM   5872 N N      . ILE   B  2 135 ? 31.586 -95.635  -30.952 1.00 25.81  ? 127  ILE   B N      1 
ATOM   5873 C CA     . ILE   B  2 135 ? 31.620 -97.100  -31.012 1.00 25.04  ? 127  ILE   B CA     1 
ATOM   5874 C C      . ILE   B  2 135 ? 31.461 -97.610  -32.454 1.00 28.39  ? 127  ILE   B C      1 
ATOM   5875 O O      . ILE   B  2 135 ? 30.553 -97.160  -33.159 1.00 27.52  ? 127  ILE   B O      1 
ATOM   5876 C CB     . ILE   B  2 135 ? 30.532 -97.724  -30.071 1.00 27.34  ? 127  ILE   B CB     1 
ATOM   5877 C CG1    . ILE   B  2 135 ? 30.763 -97.347  -28.577 1.00 28.19  ? 127  ILE   B CG1    1 
ATOM   5878 C CG2    . ILE   B  2 135 ? 30.435 -99.253  -30.248 1.00 26.75  ? 127  ILE   B CG2    1 
ATOM   5879 C CD1    . ILE   B  2 135 ? 29.534 -97.470  -27.677 1.00 30.50  ? 127  ILE   B CD1    1 
ATOM   5880 N N      . VAL   B  2 136 ? 32.331 -98.566  -32.878 1.00 24.80  ? 128  VAL   B N      1 
ATOM   5881 C CA     . VAL   B  2 136 ? 32.217 -99.224  -34.190 1.00 23.39  ? 128  VAL   B CA     1 
ATOM   5882 C C      . VAL   B  2 136 ? 31.294 -100.390 -33.903 1.00 27.41  ? 128  VAL   B C      1 
ATOM   5883 O O      . VAL   B  2 136 ? 31.643 -101.269 -33.125 1.00 27.14  ? 128  VAL   B O      1 
ATOM   5884 C CB     . VAL   B  2 136 ? 33.559 -99.675  -34.827 1.00 26.40  ? 128  VAL   B CB     1 
ATOM   5885 C CG1    . VAL   B  2 136 ? 33.366 -100.057 -36.300 1.00 25.72  ? 128  VAL   B CG1    1 
ATOM   5886 C CG2    . VAL   B  2 136 ? 34.615 -98.593  -34.701 1.00 25.84  ? 128  VAL   B CG2    1 
ATOM   5887 N N      . SER   B  2 137 ? 30.088 -100.357 -34.459 1.00 25.05  ? 129  SER   B N      1 
ATOM   5888 C CA     . SER   B  2 137 ? 29.049 -101.339 -34.169 1.00 25.36  ? 129  SER   B CA     1 
ATOM   5889 C C      . SER   B  2 137 ? 29.014 -102.558 -35.087 1.00 29.44  ? 129  SER   B C      1 
ATOM   5890 O O      . SER   B  2 137 ? 28.492 -103.611 -34.696 1.00 28.96  ? 129  SER   B O      1 
ATOM   5891 C CB     . SER   B  2 137 ? 27.689 -100.646 -34.187 1.00 30.54  ? 129  SER   B CB     1 
ATOM   5892 O OG     . SER   B  2 137 ? 27.475 -100.034 -35.448 1.00 43.43  ? 129  SER   B OG     1 
ATOM   5893 N N      . THR   B  2 138 ? 29.531 -102.412 -36.309 1.00 25.48  ? 130  THR   B N      1 
ATOM   5894 C CA     . THR   B  2 138 ? 29.454 -103.464 -37.331 1.00 25.65  ? 130  THR   B CA     1 
ATOM   5895 C C      . THR   B  2 138 ? 30.628 -103.398 -38.300 1.00 30.18  ? 130  THR   B C      1 
ATOM   5896 O O      . THR   B  2 138 ? 31.103 -102.305 -38.620 1.00 28.92  ? 130  THR   B O      1 
ATOM   5897 C CB     . THR   B  2 138 ? 28.059 -103.402 -38.031 1.00 31.20  ? 130  THR   B CB     1 
ATOM   5898 O OG1    . THR   B  2 138 ? 27.956 -104.364 -39.076 1.00 31.27  ? 130  THR   B OG1    1 
ATOM   5899 C CG2    . THR   B  2 138 ? 27.706 -102.012 -38.553 1.00 29.47  ? 130  THR   B CG2    1 
ATOM   5900 N N      . VAL   B  2 139 ? 31.098 -104.582 -38.748 1.00 28.19  ? 131  VAL   B N      1 
ATOM   5901 C CA     . VAL   B  2 139 ? 32.184 -104.765 -39.729 1.00 28.55  ? 131  VAL   B CA     1 
ATOM   5902 C C      . VAL   B  2 139 ? 31.797 -105.895 -40.694 1.00 33.58  ? 131  VAL   B C      1 
ATOM   5903 O O      . VAL   B  2 139 ? 31.127 -106.847 -40.290 1.00 33.89  ? 131  VAL   B O      1 
ATOM   5904 C CB     . VAL   B  2 139 ? 33.623 -104.960 -39.147 1.00 32.32  ? 131  VAL   B CB     1 
ATOM   5905 C CG1    . VAL   B  2 139 ? 34.218 -103.654 -38.636 1.00 32.35  ? 131  VAL   B CG1    1 
ATOM   5906 C CG2    . VAL   B  2 139 ? 33.682 -106.053 -38.082 1.00 31.84  ? 131  VAL   B CG2    1 
ATOM   5907 N N      . SER   B  2 140 ? 32.190 -105.775 -41.967 1.00 30.41  ? 132  SER   B N      1 
ATOM   5908 C CA     . SER   B  2 140 ? 31.884 -106.782 -42.989 1.00 29.67  ? 132  SER   B CA     1 
ATOM   5909 C C      . SER   B  2 140 ? 32.997 -106.792 -44.031 1.00 34.19  ? 132  SER   B C      1 
ATOM   5910 O O      . SER   B  2 140 ? 33.328 -105.733 -44.568 1.00 33.23  ? 132  SER   B O      1 
ATOM   5911 C CB     . SER   B  2 140 ? 30.539 -106.475 -43.645 1.00 31.90  ? 132  SER   B CB     1 
ATOM   5912 O OG     . SER   B  2 140 ? 30.014 -107.592 -44.342 1.00 38.72  ? 132  SER   B OG     1 
ATOM   5913 N N      . VAL   B  2 141 ? 33.600 -107.976 -44.296 1.00 31.52  ? 133  VAL   B N      1 
ATOM   5914 C CA     . VAL   B  2 141 ? 34.678 -108.091 -45.297 1.00 30.91  ? 133  VAL   B CA     1 
ATOM   5915 C C      . VAL   B  2 141 ? 34.059 -108.173 -46.696 1.00 31.76  ? 133  VAL   B C      1 
ATOM   5916 O O      . VAL   B  2 141 ? 33.132 -108.947 -46.918 1.00 30.14  ? 133  VAL   B O      1 
ATOM   5917 C CB     . VAL   B  2 141 ? 35.693 -109.246 -45.019 1.00 34.91  ? 133  VAL   B CB     1 
ATOM   5918 C CG1    . VAL   B  2 141 ? 36.795 -109.290 -46.071 1.00 34.38  ? 133  VAL   B CG1    1 
ATOM   5919 C CG2    . VAL   B  2 141 ? 36.320 -109.099 -43.648 1.00 35.03  ? 133  VAL   B CG2    1 
ATOM   5920 N N      . LEU   B  2 142 ? 34.568 -107.367 -47.628 1.00 29.47  ? 134  LEU   B N      1 
ATOM   5921 C CA     . LEU   B  2 142 ? 34.083 -107.373 -49.012 1.00 30.27  ? 134  LEU   B CA     1 
ATOM   5922 C C      . LEU   B  2 142 ? 34.539 -108.672 -49.738 1.00 34.75  ? 134  LEU   B C      1 
ATOM   5923 O O      . LEU   B  2 142 ? 35.517 -109.287 -49.303 1.00 32.70  ? 134  LEU   B O      1 
ATOM   5924 C CB     . LEU   B  2 142 ? 34.459 -106.062 -49.734 1.00 30.25  ? 134  LEU   B CB     1 
ATOM   5925 C CG     . LEU   B  2 142 ? 33.743 -104.808 -49.159 1.00 35.09  ? 134  LEU   B CG     1 
ATOM   5926 C CD1    . LEU   B  2 142 ? 34.525 -103.540 -49.419 1.00 35.60  ? 134  LEU   B CD1    1 
ATOM   5927 C CD2    . LEU   B  2 142 ? 32.343 -104.667 -49.713 1.00 37.38  ? 134  LEU   B CD2    1 
ATOM   5928 N N      . SER   B  2 143 ? 33.761 -109.136 -50.746 1.00 33.09  ? 135  SER   B N      1 
ATOM   5929 C CA     . SER   B  2 143 ? 33.946 -110.407 -51.486 1.00 33.90  ? 135  SER   B CA     1 
ATOM   5930 C C      . SER   B  2 143 ? 35.407 -110.790 -51.817 1.00 39.64  ? 135  SER   B C      1 
ATOM   5931 O O      . SER   B  2 143 ? 35.771 -111.949 -51.610 1.00 39.78  ? 135  SER   B O      1 
ATOM   5932 C CB     . SER   B  2 143 ? 33.102 -110.433 -52.755 1.00 37.29  ? 135  SER   B CB     1 
ATOM   5933 O OG     . SER   B  2 143 ? 33.560 -109.492 -53.709 1.00 46.99  ? 135  SER   B OG     1 
ATOM   5934 N N      . SER   B  2 144 ? 36.239 -109.826 -52.282 1.00 36.69  ? 136  SER   B N      1 
ATOM   5935 C CA     . SER   B  2 144 ? 37.652 -110.056 -52.609 1.00 36.93  ? 136  SER   B CA     1 
ATOM   5936 C C      . SER   B  2 144 ? 38.478 -110.485 -51.384 1.00 41.47  ? 136  SER   B C      1 
ATOM   5937 O O      . SER   B  2 144 ? 39.445 -111.243 -51.527 1.00 42.05  ? 136  SER   B O      1 
ATOM   5938 C CB     . SER   B  2 144 ? 38.273 -108.815 -53.245 1.00 40.70  ? 136  SER   B CB     1 
ATOM   5939 O OG     . SER   B  2 144 ? 38.350 -107.728 -52.334 1.00 48.76  ? 136  SER   B OG     1 
ATOM   5940 N N      . GLY   B  2 145 ? 38.093 -109.986 -50.206 1.00 35.88  ? 137  GLY   B N      1 
ATOM   5941 C CA     . GLY   B  2 145 ? 38.770 -110.276 -48.950 1.00 34.57  ? 137  GLY   B CA     1 
ATOM   5942 C C      . GLY   B  2 145 ? 39.910 -109.321 -48.673 1.00 37.47  ? 137  GLY   B C      1 
ATOM   5943 O O      . GLY   B  2 145 ? 40.644 -109.504 -47.700 1.00 37.07  ? 137  GLY   B O      1 
ATOM   5944 N N      . THR   B  2 146 ? 40.065 -108.295 -49.529 1.00 34.08  ? 138  THR   B N      1 
ATOM   5945 C CA     . THR   B  2 146 ? 41.132 -107.288 -49.433 1.00 33.96  ? 138  THR   B CA     1 
ATOM   5946 C C      . THR   B  2 146 ? 40.603 -105.984 -48.839 1.00 37.06  ? 138  THR   B C      1 
ATOM   5947 O O      . THR   B  2 146 ? 41.383 -105.103 -48.471 1.00 36.67  ? 138  THR   B O      1 
ATOM   5948 C CB     . THR   B  2 146 ? 41.752 -107.024 -50.830 1.00 46.62  ? 138  THR   B CB     1 
ATOM   5949 O OG1    . THR   B  2 146 ? 40.741 -106.554 -51.729 1.00 45.62  ? 138  THR   B OG1    1 
ATOM   5950 C CG2    . THR   B  2 146 ? 42.461 -108.255 -51.414 1.00 45.52  ? 138  THR   B CG2    1 
ATOM   5951 N N      . GLN   B  2 147 ? 39.276 -105.844 -48.793 1.00 32.65  ? 139  GLN   B N      1 
ATOM   5952 C CA     . GLN   B  2 147 ? 38.636 -104.627 -48.303 1.00 32.25  ? 139  GLN   B CA     1 
ATOM   5953 C C      . GLN   B  2 147 ? 37.526 -104.923 -47.306 1.00 33.63  ? 139  GLN   B C      1 
ATOM   5954 O O      . GLN   B  2 147 ? 36.963 -106.022 -47.297 1.00 33.23  ? 139  GLN   B O      1 
ATOM   5955 C CB     . GLN   B  2 147 ? 38.092 -103.796 -49.478 1.00 33.58  ? 139  GLN   B CB     1 
ATOM   5956 C CG     . GLN   B  2 147 ? 39.158 -103.114 -50.332 1.00 47.96  ? 139  GLN   B CG     1 
ATOM   5957 C CD     . GLN   B  2 147 ? 38.636 -102.559 -51.639 1.00 62.65  ? 139  GLN   B CD     1 
ATOM   5958 O OE1    . GLN   B  2 147 ? 37.521 -102.854 -52.092 1.00 56.24  ? 139  GLN   B OE1    1 
ATOM   5959 N NE2    . GLN   B  2 147 ? 39.461 -101.766 -52.298 1.00 56.26  ? 139  GLN   B NE2    1 
ATOM   5960 N N      . ALA   B  2 148 ? 37.196 -103.934 -46.475 1.00 28.68  ? 140  ALA   B N      1 
ATOM   5961 C CA     . ALA   B  2 148 ? 36.123 -104.107 -45.505 1.00 28.67  ? 140  ALA   B CA     1 
ATOM   5962 C C      . ALA   B  2 148 ? 35.308 -102.849 -45.294 1.00 31.99  ? 140  ALA   B C      1 
ATOM   5963 O O      . ALA   B  2 148 ? 35.781 -101.737 -45.549 1.00 29.33  ? 140  ALA   B O      1 
ATOM   5964 C CB     . ALA   B  2 148 ? 36.672 -104.616 -44.182 1.00 29.17  ? 140  ALA   B CB     1 
ATOM   5965 N N      . VAL   B  2 149 ? 34.060 -103.043 -44.850 1.00 30.66  ? 141  VAL   B N      1 
ATOM   5966 C CA     . VAL   B  2 149 ? 33.147 -101.949 -44.545 1.00 30.75  ? 141  VAL   B CA     1 
ATOM   5967 C C      . VAL   B  2 149 ? 32.823 -101.954 -43.046 1.00 32.50  ? 141  VAL   B C      1 
ATOM   5968 O O      . VAL   B  2 149 ? 32.531 -103.007 -42.476 1.00 30.93  ? 141  VAL   B O      1 
ATOM   5969 C CB     . VAL   B  2 149 ? 31.891 -101.886 -45.478 1.00 35.46  ? 141  VAL   B CB     1 
ATOM   5970 C CG1    . VAL   B  2 149 ? 31.044 -103.158 -45.425 1.00 35.44  ? 141  VAL   B CG1    1 
ATOM   5971 C CG2    . VAL   B  2 149 ? 31.039 -100.653 -45.198 1.00 35.24  ? 141  VAL   B CG2    1 
ATOM   5972 N N      . SER   B  2 150 ? 32.934 -100.775 -42.413 1.00 28.17  ? 142  SER   B N      1 
ATOM   5973 C CA     . SER   B  2 150 ? 32.587 -100.571 -41.003 1.00 27.39  ? 142  SER   B CA     1 
ATOM   5974 C C      . SER   B  2 150 ? 31.482 -99.526  -40.860 1.00 30.51  ? 142  SER   B C      1 
ATOM   5975 O O      . SER   B  2 150 ? 31.426 -98.570  -41.627 1.00 29.17  ? 142  SER   B O      1 
ATOM   5976 C CB     . SER   B  2 150 ? 33.803 -100.167 -40.179 1.00 28.00  ? 142  SER   B CB     1 
ATOM   5977 O OG     . SER   B  2 150 ? 34.327 -98.920  -40.593 1.00 29.82  ? 142  SER   B OG     1 
ATOM   5978 N N      . GLY   B  2 151 ? 30.592 -99.765  -39.908 1.00 28.29  ? 143  GLY   B N      1 
ATOM   5979 C CA     . GLY   B  2 151 ? 29.488 -98.882  -39.553 1.00 27.59  ? 143  GLY   B CA     1 
ATOM   5980 C C      . GLY   B  2 151 ? 29.661 -98.455  -38.112 1.00 29.89  ? 143  GLY   B C      1 
ATOM   5981 O O      . GLY   B  2 151 ? 30.214 -99.210  -37.305 1.00 28.21  ? 143  GLY   B O      1 
ATOM   5982 N N      . SER   B  2 152 ? 29.216 -97.238  -37.769 1.00 25.91  ? 144  SER   B N      1 
ATOM   5983 C CA     . SER   B  2 152 ? 29.417 -96.749  -36.406 1.00 25.56  ? 144  SER   B CA     1 
ATOM   5984 C C      . SER   B  2 152 ? 28.233 -95.957  -35.842 1.00 29.91  ? 144  SER   B C      1 
ATOM   5985 O O      . SER   B  2 152 ? 27.299 -95.593  -36.572 1.00 28.88  ? 144  SER   B O      1 
ATOM   5986 C CB     . SER   B  2 152 ? 30.711 -95.936  -36.349 1.00 27.49  ? 144  SER   B CB     1 
ATOM   5987 O OG     . SER   B  2 152 ? 30.935 -95.246  -35.129 1.00 34.34  ? 144  SER   B OG     1 
ATOM   5988 N N      . LYS   B  2 153 ? 28.282 -95.699  -34.523 1.00 26.89  ? 145  LYS   B N      1 
ATOM   5989 C CA     . LYS   B  2 153 ? 27.286 -94.876  -33.826 1.00 26.21  ? 145  LYS   B CA     1 
ATOM   5990 C C      . LYS   B  2 153 ? 27.496 -93.414  -34.232 1.00 29.03  ? 145  LYS   B C      1 
ATOM   5991 O O      . LYS   B  2 153 ? 26.578 -92.608  -34.097 1.00 29.22  ? 145  LYS   B O      1 
ATOM   5992 C CB     . LYS   B  2 153 ? 27.367 -95.065  -32.308 1.00 26.96  ? 145  LYS   B CB     1 
ATOM   5993 C CG     . LYS   B  2 153 ? 26.749 -96.381  -31.841 1.00 32.16  ? 145  LYS   B CG     1 
ATOM   5994 C CD     . LYS   B  2 153 ? 26.685 -96.447  -30.325 1.00 36.39  ? 145  LYS   B CD     1 
ATOM   5995 C CE     . LYS   B  2 153 ? 26.212 -97.784  -29.817 1.00 42.26  ? 145  LYS   B CE     1 
ATOM   5996 N NZ     . LYS   B  2 153 ? 24.744 -97.958  -29.954 1.00 48.46  ? 145  LYS   B NZ     1 
ATOM   5997 N N      . ASP   B  2 154 ? 28.695 -93.093  -34.786 1.00 25.06  ? 146  ASP   B N      1 
ATOM   5998 C CA     . ASP   B  2 154 ? 29.075 -91.771  -35.301 1.00 25.15  ? 146  ASP   B CA     1 
ATOM   5999 C C      . ASP   B  2 154 ? 28.363 -91.460  -36.628 1.00 28.16  ? 146  ASP   B C      1 
ATOM   6000 O O      . ASP   B  2 154 ? 28.640 -90.434  -37.247 1.00 27.75  ? 146  ASP   B O      1 
ATOM   6001 C CB     . ASP   B  2 154 ? 30.615 -91.618  -35.423 1.00 27.40  ? 146  ASP   B CB     1 
ATOM   6002 C CG     . ASP   B  2 154 ? 31.290 -92.262  -36.646 1.00 35.31  ? 146  ASP   B CG     1 
ATOM   6003 O OD1    . ASP   B  2 154 ? 30.590 -92.949  -37.433 1.00 35.47  ? 146  ASP   B OD1    1 
ATOM   6004 O OD2    . ASP   B  2 154 ? 32.509 -92.065  -36.821 1.00 38.73  ? 146  ASP   B OD2    1 
ATOM   6005 N N      . ILE   B  2 155 ? 27.476 -92.385  -37.077 1.00 25.27  ? 147  ILE   B N      1 
ATOM   6006 C CA     . ILE   B  2 155 ? 26.589 -92.296  -38.248 1.00 25.29  ? 147  ILE   B CA     1 
ATOM   6007 C C      . ILE   B  2 155 ? 27.341 -92.562  -39.600 1.00 31.47  ? 147  ILE   B C      1 
ATOM   6008 O O      . ILE   B  2 155 ? 26.697 -92.751  -40.626 1.00 31.20  ? 147  ILE   B O      1 
ATOM   6009 C CB     . ILE   B  2 155 ? 25.770 -90.943  -38.248 1.00 27.65  ? 147  ILE   B CB     1 
ATOM   6010 C CG1    . ILE   B  2 155 ? 25.121 -90.658  -36.854 1.00 27.72  ? 147  ILE   B CG1    1 
ATOM   6011 C CG2    . ILE   B  2 155 ? 24.702 -90.937  -39.332 1.00 27.14  ? 147  ILE   B CG2    1 
ATOM   6012 C CD1    . ILE   B  2 155 ? 24.493 -89.224  -36.651 1.00 30.97  ? 147  ILE   B CD1    1 
ATOM   6013 N N      . CYS   B  2 156 ? 28.677 -92.619  -39.582 1.00 31.52  ? 148  CYS   B N      1 
ATOM   6014 C CA     . CYS   B  2 156 ? 29.474 -92.826  -40.792 1.00 33.19  ? 148  CYS   B CA     1 
ATOM   6015 C C      . CYS   B  2 156 ? 29.704 -94.294  -41.143 1.00 35.15  ? 148  CYS   B C      1 
ATOM   6016 O O      . CYS   B  2 156 ? 29.639 -95.187  -40.288 1.00 34.27  ? 148  CYS   B O      1 
ATOM   6017 C CB     . CYS   B  2 156 ? 30.788 -92.059  -40.716 1.00 35.09  ? 148  CYS   B CB     1 
ATOM   6018 S SG     . CYS   B  2 156 ? 30.578 -90.267  -40.553 1.00 40.39  ? 148  CYS   B SG     1 
ATOM   6019 N N      . ILE   B  2 157 ? 29.940 -94.525  -42.434 1.00 30.72  ? 149  ILE   B N      1 
ATOM   6020 C CA     . ILE   B  2 157 ? 30.251 -95.827  -43.018 1.00 29.59  ? 149  ILE   B CA     1 
ATOM   6021 C C      . ILE   B  2 157 ? 31.576 -95.643  -43.735 1.00 33.07  ? 149  ILE   B C      1 
ATOM   6022 O O      . ILE   B  2 157 ? 31.730 -94.701  -44.510 1.00 32.13  ? 149  ILE   B O      1 
ATOM   6023 C CB     . ILE   B  2 157 ? 29.113 -96.349  -43.931 1.00 32.07  ? 149  ILE   B CB     1 
ATOM   6024 C CG1    . ILE   B  2 157 ? 27.973 -96.920  -43.078 1.00 31.72  ? 149  ILE   B CG1    1 
ATOM   6025 C CG2    . ILE   B  2 157 ? 29.631 -97.395  -44.943 1.00 32.87  ? 149  ILE   B CG2    1 
ATOM   6026 C CD1    . ILE   B  2 157 ? 26.664 -97.061  -43.798 1.00 35.86  ? 149  ILE   B CD1    1 
ATOM   6027 N N      . LYS   B  2 158 ? 32.559 -96.479  -43.411 1.00 30.37  ? 150  LYS   B N      1 
ATOM   6028 C CA     . LYS   B  2 158 ? 33.874 -96.351  -44.025 1.00 29.80  ? 150  LYS   B CA     1 
ATOM   6029 C C      . LYS   B  2 158 ? 34.280 -97.605  -44.767 1.00 34.11  ? 150  LYS   B C      1 
ATOM   6030 O O      . LYS   B  2 158 ? 33.932 -98.708  -44.346 1.00 33.15  ? 150  LYS   B O      1 
ATOM   6031 C CB     . LYS   B  2 158 ? 34.926 -95.932  -42.996 1.00 31.29  ? 150  LYS   B CB     1 
ATOM   6032 C CG     . LYS   B  2 158 ? 34.695 -94.528  -42.460 1.00 35.69  ? 150  LYS   B CG     1 
ATOM   6033 C CD     . LYS   B  2 158 ? 35.467 -94.269  -41.186 1.00 37.57  ? 150  LYS   B CD     1 
ATOM   6034 C CE     . LYS   B  2 158 ? 35.022 -92.981  -40.531 1.00 33.00  ? 150  LYS   B CE     1 
ATOM   6035 N NZ     . LYS   B  2 158 ? 35.643 -91.792  -41.167 1.00 33.91  ? 150  LYS   B NZ     1 
ATOM   6036 N N      . VAL   B  2 159 ? 34.965 -97.418  -45.913 1.00 31.65  ? 151  VAL   B N      1 
ATOM   6037 C CA     . VAL   B  2 159 ? 35.489 -98.496  -46.761 1.00 31.76  ? 151  VAL   B CA     1 
ATOM   6038 C C      . VAL   B  2 159 ? 37.005 -98.511  -46.552 1.00 35.26  ? 151  VAL   B C      1 
ATOM   6039 O O      . VAL   B  2 159 ? 37.667 -97.495  -46.745 1.00 34.73  ? 151  VAL   B O      1 
ATOM   6040 C CB     . VAL   B  2 159 ? 35.059 -98.392  -48.249 1.00 35.46  ? 151  VAL   B CB     1 
ATOM   6041 C CG1    . VAL   B  2 159 ? 35.731 -99.479  -49.090 1.00 35.49  ? 151  VAL   B CG1    1 
ATOM   6042 C CG2    . VAL   B  2 159 ? 33.540 -98.488  -48.386 1.00 34.99  ? 151  VAL   B CG2    1 
ATOM   6043 N N      . TRP   B  2 160 ? 37.525 -99.643  -46.075 1.00 32.54  ? 152  TRP   B N      1 
ATOM   6044 C CA     . TRP   B  2 160 ? 38.925 -99.828  -45.712 1.00 33.40  ? 152  TRP   B CA     1 
ATOM   6045 C C      . TRP   B  2 160 ? 39.737 -100.630 -46.720 1.00 38.22  ? 152  TRP   B C      1 
ATOM   6046 O O      . TRP   B  2 160 ? 39.228 -101.582 -47.301 1.00 36.61  ? 152  TRP   B O      1 
ATOM   6047 C CB     . TRP   B  2 160 ? 38.990 -100.575 -44.363 1.00 32.65  ? 152  TRP   B CB     1 
ATOM   6048 C CG     . TRP   B  2 160 ? 38.436 -99.812  -43.198 1.00 34.04  ? 152  TRP   B CG     1 
ATOM   6049 C CD1    . TRP   B  2 160 ? 37.125 -99.701  -42.837 1.00 37.07  ? 152  TRP   B CD1    1 
ATOM   6050 C CD2    . TRP   B  2 160 ? 39.188 -99.111  -42.203 1.00 34.17  ? 152  TRP   B CD2    1 
ATOM   6051 N NE1    . TRP   B  2 160 ? 37.009 -98.921  -41.710 1.00 36.94  ? 152  TRP   B NE1    1 
ATOM   6052 C CE2    . TRP   B  2 160 ? 38.261 -98.553  -41.292 1.00 38.57  ? 152  TRP   B CE2    1 
ATOM   6053 C CE3    . TRP   B  2 160 ? 40.561 -98.878  -42.002 1.00 35.62  ? 152  TRP   B CE3    1 
ATOM   6054 C CZ2    . TRP   B  2 160 ? 38.664 -97.791  -40.184 1.00 38.01  ? 152  TRP   B CZ2    1 
ATOM   6055 C CZ3    . TRP   B  2 160 ? 40.959 -98.128  -40.906 1.00 37.42  ? 152  TRP   B CZ3    1 
ATOM   6056 C CH2    . TRP   B  2 160 ? 40.018 -97.596  -40.008 1.00 38.18  ? 152  TRP   B CH2    1 
ATOM   6057 N N      . ASP   B  2 161 ? 41.020 -100.289 -46.870 1.00 37.45  ? 153  ASP   B N      1 
ATOM   6058 C CA     . ASP   B  2 161 ? 41.963 -101.081 -47.659 1.00 38.28  ? 153  ASP   B CA     1 
ATOM   6059 C C      . ASP   B  2 161 ? 42.807 -101.783 -46.589 1.00 42.23  ? 153  ASP   B C      1 
ATOM   6060 O O      . ASP   B  2 161 ? 43.561 -101.123 -45.867 1.00 41.24  ? 153  ASP   B O      1 
ATOM   6061 C CB     . ASP   B  2 161 ? 42.833 -100.221 -48.593 1.00 40.65  ? 153  ASP   B CB     1 
ATOM   6062 C CG     . ASP   B  2 161 ? 43.664 -101.070 -49.548 1.00 56.81  ? 153  ASP   B CG     1 
ATOM   6063 O OD1    . ASP   B  2 161 ? 44.745 -101.549 -49.132 1.00 57.73  ? 153  ASP   B OD1    1 
ATOM   6064 O OD2    . ASP   B  2 161 ? 43.210 -101.295 -50.690 1.00 64.57  ? 153  ASP   B OD2    1 
ATOM   6065 N N      . LEU   B  2 162 ? 42.614 -103.100 -46.431 1.00 40.53  ? 154  LEU   B N      1 
ATOM   6066 C CA     . LEU   B  2 162 ? 43.262 -103.885 -45.373 1.00 41.39  ? 154  LEU   B CA     1 
ATOM   6067 C C      . LEU   B  2 162 ? 44.799 -103.944 -45.464 1.00 47.85  ? 154  LEU   B C      1 
ATOM   6068 O O      . LEU   B  2 162 ? 45.449 -103.860 -44.420 1.00 47.70  ? 154  LEU   B O      1 
ATOM   6069 C CB     . LEU   B  2 162 ? 42.656 -105.292 -45.268 1.00 41.35  ? 154  LEU   B CB     1 
ATOM   6070 C CG     . LEU   B  2 162 ? 41.155 -105.347 -44.920 1.00 45.81  ? 154  LEU   B CG     1 
ATOM   6071 C CD1    . LEU   B  2 162 ? 40.594 -106.712 -45.164 1.00 45.96  ? 154  LEU   B CD1    1 
ATOM   6072 C CD2    . LEU   B  2 162 ? 40.889 -104.931 -43.477 1.00 48.56  ? 154  LEU   B CD2    1 
ATOM   6073 N N      . ALA   B  2 163 ? 45.377 -104.050 -46.685 1.00 45.58  ? 155  ALA   B N      1 
ATOM   6074 C CA     . ALA   B  2 163 ? 46.836 -104.090 -46.877 1.00 45.46  ? 155  ALA   B CA     1 
ATOM   6075 C C      . ALA   B  2 163 ? 47.490 -102.731 -46.575 1.00 49.20  ? 155  ALA   B C      1 
ATOM   6076 O O      . ALA   B  2 163 ? 48.509 -102.685 -45.882 1.00 49.39  ? 155  ALA   B O      1 
ATOM   6077 C CB     . ALA   B  2 163 ? 47.176 -104.536 -48.293 1.00 46.14  ? 155  ALA   B CB     1 
ATOM   6078 N N      . GLN   B  2 164 ? 46.896 -101.632 -47.082 1.00 44.84  ? 156  GLN   B N      1 
ATOM   6079 C CA     . GLN   B  2 164 ? 47.396 -100.272 -46.863 1.00 44.25  ? 156  GLN   B CA     1 
ATOM   6080 C C      . GLN   B  2 164 ? 47.105 -99.774  -45.441 1.00 45.88  ? 156  GLN   B C      1 
ATOM   6081 O O      . GLN   B  2 164 ? 47.743 -98.819  -44.996 1.00 45.36  ? 156  GLN   B O      1 
ATOM   6082 C CB     . GLN   B  2 164 ? 46.795 -99.300  -47.888 1.00 45.73  ? 156  GLN   B CB     1 
ATOM   6083 C CG     . GLN   B  2 164 ? 47.465 -99.307  -49.256 1.00 63.80  ? 156  GLN   B CG     1 
ATOM   6084 C CD     . GLN   B  2 164 ? 46.776 -98.348  -50.201 1.00 81.99  ? 156  GLN   B CD     1 
ATOM   6085 O OE1    . GLN   B  2 164 ? 46.767 -97.127  -49.999 1.00 77.70  ? 156  GLN   B OE1    1 
ATOM   6086 N NE2    . GLN   B  2 164 ? 46.176 -98.880  -51.253 1.00 73.47  ? 156  GLN   B NE2    1 
ATOM   6087 N N      . GLN   B  2 165 ? 46.137 -100.418 -44.738 1.00 40.89  ? 157  GLN   B N      1 
ATOM   6088 C CA     . GLN   B  2 165 ? 45.688 -100.094 -43.371 1.00 40.57  ? 157  GLN   B CA     1 
ATOM   6089 C C      . GLN   B  2 165 ? 45.127 -98.652  -43.304 1.00 44.06  ? 157  GLN   B C      1 
ATOM   6090 O O      . GLN   B  2 165 ? 45.405 -97.918  -42.353 1.00 44.18  ? 157  GLN   B O      1 
ATOM   6091 C CB     . GLN   B  2 165 ? 46.800 -100.342 -42.313 1.00 41.64  ? 157  GLN   B CB     1 
ATOM   6092 C CG     . GLN   B  2 165 ? 47.602 -101.636 -42.518 1.00 45.00  ? 157  GLN   B CG     1 
ATOM   6093 C CD     . GLN   B  2 165 ? 48.593 -101.955 -41.422 1.00 55.12  ? 157  GLN   B CD     1 
ATOM   6094 O OE1    . GLN   B  2 165 ? 48.969 -101.114 -40.601 1.00 49.14  ? 157  GLN   B OE1    1 
ATOM   6095 N NE2    . GLN   B  2 165 ? 49.062 -103.191 -41.404 1.00 46.86  ? 157  GLN   B NE2    1 
ATOM   6096 N N      . VAL   B  2 166 ? 44.367 -98.244  -44.346 1.00 39.48  ? 158  VAL   B N      1 
ATOM   6097 C CA     . VAL   B  2 166 ? 43.777 -96.900  -44.454 1.00 38.91  ? 158  VAL   B CA     1 
ATOM   6098 C C      . VAL   B  2 166 ? 42.303 -96.925  -44.901 1.00 40.28  ? 158  VAL   B C      1 
ATOM   6099 O O      . VAL   B  2 166 ? 41.816 -97.944  -45.398 1.00 38.38  ? 158  VAL   B O      1 
ATOM   6100 C CB     . VAL   B  2 166 ? 44.608 -95.915  -45.334 1.00 43.13  ? 158  VAL   B CB     1 
ATOM   6101 C CG1    . VAL   B  2 166 ? 45.940 -95.549  -44.689 1.00 43.15  ? 158  VAL   B CG1    1 
ATOM   6102 C CG2    . VAL   B  2 166 ? 44.796 -96.433  -46.757 1.00 42.99  ? 158  VAL   B CG2    1 
ATOM   6103 N N      . VAL   B  2 167 ? 41.615 -95.776  -44.736 1.00 36.65  ? 159  VAL   B N      1 
ATOM   6104 C CA     . VAL   B  2 167 ? 40.224 -95.578  -45.149 1.00 36.37  ? 159  VAL   B CA     1 
ATOM   6105 C C      . VAL   B  2 167 ? 40.250 -95.017  -46.572 1.00 39.89  ? 159  VAL   B C      1 
ATOM   6106 O O      . VAL   B  2 167 ? 40.856 -93.971  -46.812 1.00 38.71  ? 159  VAL   B O      1 
ATOM   6107 C CB     . VAL   B  2 167 ? 39.436 -94.659  -44.165 1.00 39.84  ? 159  VAL   B CB     1 
ATOM   6108 C CG1    . VAL   B  2 167 ? 38.053 -94.310  -44.709 1.00 39.62  ? 159  VAL   B CG1    1 
ATOM   6109 C CG2    . VAL   B  2 167 ? 39.316 -95.305  -42.794 1.00 39.43  ? 159  VAL   B CG2    1 
ATOM   6110 N N      . LEU   B  2 168 ? 39.604 -95.725  -47.500 1.00 37.90  ? 160  LEU   B N      1 
ATOM   6111 C CA     . LEU   B  2 168 ? 39.492 -95.361  -48.914 1.00 38.88  ? 160  LEU   B CA     1 
ATOM   6112 C C      . LEU   B  2 168 ? 38.395 -94.317  -49.122 1.00 44.00  ? 160  LEU   B C      1 
ATOM   6113 O O      . LEU   B  2 168 ? 38.597 -93.362  -49.871 1.00 43.96  ? 160  LEU   B O      1 
ATOM   6114 C CB     . LEU   B  2 168 ? 39.176 -96.602  -49.770 1.00 39.20  ? 160  LEU   B CB     1 
ATOM   6115 C CG     . LEU   B  2 168 ? 40.209 -97.733  -49.786 1.00 44.35  ? 160  LEU   B CG     1 
ATOM   6116 C CD1    . LEU   B  2 168 ? 39.568 -99.027  -50.230 1.00 44.41  ? 160  LEU   B CD1    1 
ATOM   6117 C CD2    . LEU   B  2 168 ? 41.407 -97.386  -50.674 1.00 46.64  ? 160  LEU   B CD2    1 
ATOM   6118 N N      . SER   B  2 169 ? 37.226 -94.518  -48.480 1.00 40.45  ? 161  SER   B N      1 
ATOM   6119 C CA     . SER   B  2 169 ? 36.078 -93.623  -48.594 1.00 39.95  ? 161  SER   B CA     1 
ATOM   6120 C C      . SER   B  2 169 ? 35.299 -93.533  -47.286 1.00 41.07  ? 161  SER   B C      1 
ATOM   6121 O O      . SER   B  2 169 ? 35.138 -94.533  -46.581 1.00 39.33  ? 161  SER   B O      1 
ATOM   6122 C CB     . SER   B  2 169 ? 35.150 -94.090  -49.712 1.00 44.99  ? 161  SER   B CB     1 
ATOM   6123 O OG     . SER   B  2 169 ? 35.803 -94.058  -50.972 1.00 58.59  ? 161  SER   B OG     1 
ATOM   6124 N N      . SER   B  2 170 ? 34.801 -92.329  -46.980 1.00 36.51  ? 162  SER   B N      1 
ATOM   6125 C CA     . SER   B  2 170 ? 34.007 -92.067  -45.785 1.00 35.44  ? 162  SER   B CA     1 
ATOM   6126 C C      . SER   B  2 170 ? 32.651 -91.540  -46.226 1.00 38.25  ? 162  SER   B C      1 
ATOM   6127 O O      . SER   B  2 170 ? 32.575 -90.509  -46.906 1.00 37.51  ? 162  SER   B O      1 
ATOM   6128 C CB     . SER   B  2 170 ? 34.718 -91.079  -44.870 1.00 37.40  ? 162  SER   B CB     1 
ATOM   6129 O OG     . SER   B  2 170 ? 34.261 -91.259  -43.542 1.00 45.76  ? 162  SER   B OG     1 
ATOM   6130 N N      . TYR   B  2 171 ? 31.587 -92.280  -45.879 1.00 33.68  ? 163  TYR   B N      1 
ATOM   6131 C CA     . TYR   B  2 171 ? 30.217 -91.962  -46.257 1.00 33.30  ? 163  TYR   B CA     1 
ATOM   6132 C C      . TYR   B  2 171 ? 29.304 -91.619  -45.070 1.00 35.45  ? 163  TYR   B C      1 
ATOM   6133 O O      . TYR   B  2 171 ? 29.153 -92.429  -44.149 1.00 33.49  ? 163  TYR   B O      1 
ATOM   6134 C CB     . TYR   B  2 171 ? 29.598 -93.136  -47.021 1.00 35.28  ? 163  TYR   B CB     1 
ATOM   6135 C CG     . TYR   B  2 171 ? 30.332 -93.563  -48.273 1.00 37.92  ? 163  TYR   B CG     1 
ATOM   6136 C CD1    . TYR   B  2 171 ? 30.424 -92.717  -49.377 1.00 39.59  ? 163  TYR   B CD1    1 
ATOM   6137 C CD2    . TYR   B  2 171 ? 30.854 -94.849  -48.392 1.00 38.93  ? 163  TYR   B CD2    1 
ATOM   6138 C CE1    . TYR   B  2 171 ? 31.071 -93.119  -50.546 1.00 40.37  ? 163  TYR   B CE1    1 
ATOM   6139 C CE2    . TYR   B  2 171 ? 31.487 -95.269  -49.564 1.00 39.89  ? 163  TYR   B CE2    1 
ATOM   6140 C CZ     . TYR   B  2 171 ? 31.595 -94.400  -50.638 1.00 46.65  ? 163  TYR   B CZ     1 
ATOM   6141 O OH     . TYR   B  2 171 ? 32.223 -94.808  -51.791 1.00 48.44  ? 163  TYR   B OH     1 
ATOM   6142 N N      . ARG   B  2 172 ? 28.645 -90.443  -45.144 1.00 31.42  ? 164  ARG   B N      1 
ATOM   6143 C CA     . ARG   B  2 172 ? 27.663 -89.957  -44.166 1.00 30.68  ? 164  ARG   B CA     1 
ATOM   6144 C C      . ARG   B  2 172 ? 26.325 -89.919  -44.908 1.00 33.09  ? 164  ARG   B C      1 
ATOM   6145 O O      . ARG   B  2 172 ? 25.875 -88.862  -45.343 1.00 32.98  ? 164  ARG   B O      1 
ATOM   6146 C CB     . ARG   B  2 172 ? 28.073 -88.569  -43.613 1.00 31.75  ? 164  ARG   B CB     1 
ATOM   6147 C CG     . ARG   B  2 172 ? 27.091 -87.955  -42.608 1.00 44.51  ? 164  ARG   B CG     1 
ATOM   6148 C CD     . ARG   B  2 172 ? 27.563 -88.097  -41.186 1.00 56.33  ? 164  ARG   B CD     1 
ATOM   6149 N NE     . ARG   B  2 172 ? 28.552 -87.080  -40.832 1.00 66.51  ? 164  ARG   B NE     1 
ATOM   6150 C CZ     . ARG   B  2 172 ? 29.168 -87.015  -39.655 1.00 85.22  ? 164  ARG   B CZ     1 
ATOM   6151 N NH1    . ARG   B  2 172 ? 28.899 -87.905  -38.707 1.00 74.04  ? 164  ARG   B NH1    1 
ATOM   6152 N NH2    . ARG   B  2 172 ? 30.060 -86.063  -39.419 1.00 75.70  ? 164  ARG   B NH2    1 
ATOM   6153 N N      . ALA   B  2 173 ? 25.725 -91.092  -45.113 1.00 29.42  ? 165  ALA   B N      1 
ATOM   6154 C CA     . ALA   B  2 173 ? 24.458 -91.207  -45.838 1.00 28.98  ? 165  ALA   B CA     1 
ATOM   6155 C C      . ALA   B  2 173 ? 23.281 -91.293  -44.884 1.00 31.03  ? 165  ALA   B C      1 
ATOM   6156 O O      . ALA   B  2 173 ? 22.183 -90.828  -45.205 1.00 31.29  ? 165  ALA   B O      1 
ATOM   6157 C CB     . ALA   B  2 173 ? 24.477 -92.429  -46.735 1.00 29.77  ? 165  ALA   B CB     1 
ATOM   6158 N N      . HIS   B  2 174 ? 23.504 -91.952  -43.742 1.00 24.78  ? 166  HIS   B N      1 
ATOM   6159 C CA     . HIS   B  2 174 ? 22.502 -92.130  -42.704 1.00 24.05  ? 166  HIS   B CA     1 
ATOM   6160 C C      . HIS   B  2 174 ? 22.342 -90.860  -41.870 1.00 27.17  ? 166  HIS   B C      1 
ATOM   6161 O O      . HIS   B  2 174 ? 23.166 -89.944  -41.962 1.00 25.47  ? 166  HIS   B O      1 
ATOM   6162 C CB     . HIS   B  2 174 ? 22.829 -93.353  -41.829 1.00 23.89  ? 166  HIS   B CB     1 
ATOM   6163 C CG     . HIS   B  2 174 ? 22.569 -94.643  -42.537 1.00 26.46  ? 166  HIS   B CG     1 
ATOM   6164 N ND1    . HIS   B  2 174 ? 21.280 -95.033  -42.881 1.00 27.61  ? 166  HIS   B ND1    1 
ATOM   6165 C CD2    . HIS   B  2 174 ? 23.442 -95.571  -42.991 1.00 26.97  ? 166  HIS   B CD2    1 
ATOM   6166 C CE1    . HIS   B  2 174 ? 21.413 -96.201  -43.486 1.00 26.52  ? 166  HIS   B CE1    1 
ATOM   6167 N NE2    . HIS   B  2 174 ? 22.691 -96.561  -43.578 1.00 26.53  ? 166  HIS   B NE2    1 
ATOM   6168 N N      . ALA   B  2 175 ? 21.264 -90.801  -41.091 1.00 25.38  ? 167  ALA   B N      1 
ATOM   6169 C CA     . ALA   B  2 175 ? 20.930 -89.668  -40.229 1.00 25.58  ? 167  ALA   B CA     1 
ATOM   6170 C C      . ALA   B  2 175 ? 20.904 -90.076  -38.745 1.00 29.39  ? 167  ALA   B C      1 
ATOM   6171 O O      . ALA   B  2 175 ? 20.606 -89.251  -37.876 1.00 28.57  ? 167  ALA   B O      1 
ATOM   6172 C CB     . ALA   B  2 175 ? 19.590 -89.093  -40.648 1.00 26.30  ? 167  ALA   B CB     1 
ATOM   6173 N N      . ALA   B  2 176 ? 21.212 -91.357  -38.463 1.00 25.36  ? 168  ALA   B N      1 
ATOM   6174 C CA     . ALA   B  2 176 ? 21.266 -91.925  -37.114 1.00 25.16  ? 168  ALA   B CA     1 
ATOM   6175 C C      . ALA   B  2 176 ? 22.265 -93.089  -37.123 1.00 30.01  ? 168  ALA   B C      1 
ATOM   6176 O O      . ALA   B  2 176 ? 22.749 -93.461  -38.207 1.00 30.32  ? 168  ALA   B O      1 
ATOM   6177 C CB     . ALA   B  2 176 ? 19.884 -92.394  -36.676 1.00 25.52  ? 168  ALA   B CB     1 
ATOM   6178 N N      . GLN   B  2 177 ? 22.582 -93.659  -35.933 1.00 24.76  ? 169  GLN   B N      1 
ATOM   6179 C CA     . GLN   B  2 177 ? 23.573 -94.737  -35.797 1.00 23.74  ? 169  GLN   B CA     1 
ATOM   6180 C C      . GLN   B  2 177 ? 23.386 -95.875  -36.781 1.00 26.22  ? 169  GLN   B C      1 
ATOM   6181 O O      . GLN   B  2 177 ? 22.264 -96.306  -37.030 1.00 24.40  ? 169  GLN   B O      1 
ATOM   6182 C CB     . GLN   B  2 177 ? 23.680 -95.278  -34.359 1.00 24.92  ? 169  GLN   B CB     1 
ATOM   6183 C CG     . GLN   B  2 177 ? 22.383 -95.557  -33.634 1.00 32.67  ? 169  GLN   B CG     1 
ATOM   6184 C CD     . GLN   B  2 177 ? 22.650 -96.089  -32.243 1.00 47.57  ? 169  GLN   B CD     1 
ATOM   6185 O OE1    . GLN   B  2 177 ? 23.133 -95.377  -31.347 1.00 40.63  ? 169  GLN   B OE1    1 
ATOM   6186 N NE2    . GLN   B  2 177 ? 22.359 -97.362  -32.038 1.00 34.77  ? 169  GLN   B NE2    1 
ATOM   6187 N N      . VAL   B  2 178 ? 24.504 -96.358  -37.342 1.00 24.36  ? 170  VAL   B N      1 
ATOM   6188 C CA     . VAL   B  2 178 ? 24.488 -97.493  -38.277 1.00 23.83  ? 170  VAL   B CA     1 
ATOM   6189 C C      . VAL   B  2 178 ? 24.389 -98.747  -37.428 1.00 28.38  ? 170  VAL   B C      1 
ATOM   6190 O O      . VAL   B  2 178 ? 25.231 -98.963  -36.554 1.00 29.70  ? 170  VAL   B O      1 
ATOM   6191 C CB     . VAL   B  2 178 ? 25.710 -97.512  -39.236 1.00 26.79  ? 170  VAL   B CB     1 
ATOM   6192 C CG1    . VAL   B  2 178 ? 25.589 -98.647  -40.259 1.00 26.09  ? 170  VAL   B CG1    1 
ATOM   6193 C CG2    . VAL   B  2 178 ? 25.879 -96.170  -39.934 1.00 26.60  ? 170  VAL   B CG2    1 
ATOM   6194 N N      . THR   B  2 179 ? 23.329 -99.529  -37.642 1.00 24.33  ? 171  THR   B N      1 
ATOM   6195 C CA     . THR   B  2 179 ? 23.039 -100.758 -36.912 1.00 25.01  ? 171  THR   B CA     1 
ATOM   6196 C C      . THR   B  2 179 ? 23.743 -101.966 -37.538 1.00 32.77  ? 171  THR   B C      1 
ATOM   6197 O O      . THR   B  2 179 ? 24.295 -102.803 -36.811 1.00 32.55  ? 171  THR   B O      1 
ATOM   6198 C CB     . THR   B  2 179 ? 21.512 -100.993 -36.866 1.00 36.69  ? 171  THR   B CB     1 
ATOM   6199 O OG1    . THR   B  2 179 ? 20.844 -99.757  -36.588 1.00 39.86  ? 171  THR   B OG1    1 
ATOM   6200 C CG2    . THR   B  2 179 ? 21.105 -102.048 -35.827 1.00 35.84  ? 171  THR   B CG2    1 
ATOM   6201 N N      . CYS   B  2 180 ? 23.690 -102.079 -38.877 1.00 31.43  ? 172  CYS   B N      1 
ATOM   6202 C CA     . CYS   B  2 180 ? 24.254 -103.230 -39.586 1.00 32.33  ? 172  CYS   B CA     1 
ATOM   6203 C C      . CYS   B  2 180 ? 24.804 -102.872 -40.968 1.00 34.96  ? 172  CYS   B C      1 
ATOM   6204 O O      . CYS   B  2 180 ? 24.198 -102.077 -41.691 1.00 33.84  ? 172  CYS   B O      1 
ATOM   6205 C CB     . CYS   B  2 180 ? 23.211 -104.347 -39.669 1.00 33.65  ? 172  CYS   B CB     1 
ATOM   6206 S SG     . CYS   B  2 180 ? 23.868 -105.961 -40.179 1.00 38.44  ? 172  CYS   B SG     1 
ATOM   6207 N N      . VAL   B  2 181 ? 25.975 -103.442 -41.307 1.00 30.54  ? 173  VAL   B N      1 
ATOM   6208 C CA     . VAL   B  2 181 ? 26.627 -103.369 -42.624 1.00 28.85  ? 173  VAL   B CA     1 
ATOM   6209 C C      . VAL   B  2 181 ? 26.856 -104.810 -43.090 1.00 31.99  ? 173  VAL   B C      1 
ATOM   6210 O O      . VAL   B  2 181 ? 27.338 -105.638 -42.306 1.00 31.99  ? 173  VAL   B O      1 
ATOM   6211 C CB     . VAL   B  2 181 ? 27.908 -102.491 -42.756 1.00 32.29  ? 173  VAL   B CB     1 
ATOM   6212 C CG1    . VAL   B  2 181 ? 27.629 -101.024 -42.441 1.00 31.81  ? 173  VAL   B CG1    1 
ATOM   6213 C CG2    . VAL   B  2 181 ? 29.090 -103.031 -41.944 1.00 31.99  ? 173  VAL   B CG2    1 
ATOM   6214 N N      . ALA   B  2 182 ? 26.458 -105.128 -44.328 1.00 27.07  ? 174  ALA   B N      1 
ATOM   6215 C CA     . ALA   B  2 182 ? 26.623 -106.478 -44.863 1.00 26.58  ? 174  ALA   B CA     1 
ATOM   6216 C C      . ALA   B  2 182 ? 27.128 -106.441 -46.315 1.00 30.88  ? 174  ALA   B C      1 
ATOM   6217 O O      . ALA   B  2 182 ? 26.420 -105.972 -47.218 1.00 29.30  ? 174  ALA   B O      1 
ATOM   6218 C CB     . ALA   B  2 182 ? 25.319 -107.262 -44.755 1.00 26.85  ? 174  ALA   B CB     1 
ATOM   6219 N N      . ALA   B  2 183 ? 28.378 -106.913 -46.521 1.00 27.04  ? 175  ALA   B N      1 
ATOM   6220 C CA     . ALA   B  2 183 ? 29.000 -106.986 -47.837 1.00 26.57  ? 175  ALA   B CA     1 
ATOM   6221 C C      . ALA   B  2 183 ? 28.313 -108.057 -48.670 1.00 28.96  ? 175  ALA   B C      1 
ATOM   6222 O O      . ALA   B  2 183 ? 27.965 -109.104 -48.126 1.00 27.98  ? 175  ALA   B O      1 
ATOM   6223 C CB     . ALA   B  2 183 ? 30.475 -107.297 -47.694 1.00 27.23  ? 175  ALA   B CB     1 
ATOM   6224 N N      . SER   B  2 184 ? 28.070 -107.793 -49.977 1.00 25.83  ? 176  SER   B N      1 
ATOM   6225 C CA     . SER   B  2 184 ? 27.448 -108.813 -50.836 1.00 26.05  ? 176  SER   B CA     1 
ATOM   6226 C C      . SER   B  2 184 ? 28.397 -110.024 -50.940 1.00 29.63  ? 176  SER   B C      1 
ATOM   6227 O O      . SER   B  2 184 ? 29.616 -109.846 -50.821 1.00 28.77  ? 176  SER   B O      1 
ATOM   6228 C CB     . SER   B  2 184 ? 27.109 -108.270 -52.224 1.00 29.80  ? 176  SER   B CB     1 
ATOM   6229 O OG     . SER   B  2 184 ? 28.281 -108.094 -52.996 1.00 37.34  ? 176  SER   B OG     1 
ATOM   6230 N N      . PRO   B  2 185 ? 27.876 -111.258 -51.065 1.00 27.14  ? 177  PRO   B N      1 
ATOM   6231 C CA     . PRO   B  2 185 ? 28.785 -112.421 -51.123 1.00 28.18  ? 177  PRO   B CA     1 
ATOM   6232 C C      . PRO   B  2 185 ? 29.769 -112.408 -52.295 1.00 33.00  ? 177  PRO   B C      1 
ATOM   6233 O O      . PRO   B  2 185 ? 30.903 -112.851 -52.128 1.00 33.03  ? 177  PRO   B O      1 
ATOM   6234 C CB     . PRO   B  2 185 ? 27.832 -113.618 -51.240 1.00 29.98  ? 177  PRO   B CB     1 
ATOM   6235 C CG     . PRO   B  2 185 ? 26.491 -113.104 -50.811 1.00 33.52  ? 177  PRO   B CG     1 
ATOM   6236 C CD     . PRO   B  2 185 ? 26.464 -111.669 -51.192 1.00 28.22  ? 177  PRO   B CD     1 
ATOM   6237 N N      . HIS   B  2 186 ? 29.357 -111.876 -53.464 1.00 30.35  ? 178  HIS   B N      1 
ATOM   6238 C CA     . HIS   B  2 186 ? 30.192 -111.974 -54.661 1.00 30.65  ? 178  HIS   B CA     1 
ATOM   6239 C C      . HIS   B  2 186 ? 30.575 -110.666 -55.368 1.00 34.66  ? 178  HIS   B C      1 
ATOM   6240 O O      . HIS   B  2 186 ? 31.385 -110.739 -56.292 1.00 33.58  ? 178  HIS   B O      1 
ATOM   6241 C CB     . HIS   B  2 186 ? 29.523 -112.933 -55.661 1.00 31.03  ? 178  HIS   B CB     1 
ATOM   6242 C CG     . HIS   B  2 186 ? 29.112 -114.235 -55.036 1.00 34.38  ? 178  HIS   B CG     1 
ATOM   6243 N ND1    . HIS   B  2 186 ? 30.048 -115.111 -54.508 1.00 36.16  ? 178  HIS   B ND1    1 
ATOM   6244 C CD2    . HIS   B  2 186 ? 27.875 -114.739 -54.821 1.00 36.19  ? 178  HIS   B CD2    1 
ATOM   6245 C CE1    . HIS   B  2 186 ? 29.353 -116.123 -54.009 1.00 35.60  ? 178  HIS   B CE1    1 
ATOM   6246 N NE2    . HIS   B  2 186 ? 28.042 -115.951 -54.186 1.00 35.96  ? 178  HIS   B NE2    1 
ATOM   6247 N N      . LYS   B  2 187 ? 30.050 -109.488 -54.950 1.00 31.94  ? 179  LYS   B N      1 
ATOM   6248 C CA     . LYS   B  2 187 ? 30.393 -108.215 -55.611 1.00 31.77  ? 179  LYS   B CA     1 
ATOM   6249 C C      . LYS   B  2 187 ? 31.102 -107.270 -54.646 1.00 38.06  ? 179  LYS   B C      1 
ATOM   6250 O O      . LYS   B  2 187 ? 30.491 -106.774 -53.696 1.00 37.63  ? 179  LYS   B O      1 
ATOM   6251 C CB     . LYS   B  2 187 ? 29.151 -107.551 -56.233 1.00 34.53  ? 179  LYS   B CB     1 
ATOM   6252 C CG     . LYS   B  2 187 ? 28.400 -108.401 -57.256 1.00 47.91  ? 179  LYS   B CG     1 
ATOM   6253 C CD     . LYS   B  2 187 ? 27.093 -107.738 -57.653 1.00 54.08  ? 179  LYS   B CD     1 
ATOM   6254 C CE     . LYS   B  2 187 ? 26.391 -108.452 -58.772 1.00 61.11  ? 179  LYS   B CE     1 
ATOM   6255 N NZ     . LYS   B  2 187 ? 25.126 -107.763 -59.140 1.00 70.41  ? 179  LYS   B NZ     1 
ATOM   6256 N N      . ASP   B  2 188 ? 32.389 -107.000 -54.905 1.00 36.20  ? 180  ASP   B N      1 
ATOM   6257 C CA     . ASP   B  2 188 ? 33.251 -106.157 -54.075 1.00 37.05  ? 180  ASP   B CA     1 
ATOM   6258 C C      . ASP   B  2 188 ? 32.818 -104.699 -53.932 1.00 40.97  ? 180  ASP   B C      1 
ATOM   6259 O O      . ASP   B  2 188 ? 33.272 -104.021 -53.007 1.00 41.81  ? 180  ASP   B O      1 
ATOM   6260 C CB     . ASP   B  2 188 ? 34.695 -106.213 -54.590 1.00 40.09  ? 180  ASP   B CB     1 
ATOM   6261 C CG     . ASP   B  2 188 ? 35.734 -106.198 -53.491 1.00 54.23  ? 180  ASP   B CG     1 
ATOM   6262 O OD1    . ASP   B  2 188 ? 35.711 -107.110 -52.647 1.00 55.78  ? 180  ASP   B OD1    1 
ATOM   6263 O OD2    . ASP   B  2 188 ? 36.598 -105.296 -53.503 1.00 62.77  ? 180  ASP   B OD2    1 
ATOM   6264 N N      . SER   B  2 189 ? 31.981 -104.203 -54.844 1.00 35.71  ? 181  SER   B N      1 
ATOM   6265 C CA     . SER   B  2 189 ? 31.537 -102.811 -54.799 1.00 34.52  ? 181  SER   B CA     1 
ATOM   6266 C C      . SER   B  2 189 ? 30.111 -102.667 -54.229 1.00 34.35  ? 181  SER   B C      1 
ATOM   6267 O O      . SER   B  2 189 ? 29.630 -101.550 -54.076 1.00 33.46  ? 181  SER   B O      1 
ATOM   6268 C CB     . SER   B  2 189 ? 31.648 -102.180 -56.187 1.00 37.41  ? 181  SER   B CB     1 
ATOM   6269 O OG     . SER   B  2 189 ? 30.743 -102.774 -57.103 1.00 43.75  ? 181  SER   B OG     1 
ATOM   6270 N N      . VAL   B  2 190 ? 29.463 -103.798 -53.902 1.00 28.68  ? 182  VAL   B N      1 
ATOM   6271 C CA     . VAL   B  2 190 ? 28.083 -103.860 -53.438 1.00 27.79  ? 182  VAL   B CA     1 
ATOM   6272 C C      . VAL   B  2 190 ? 27.967 -104.327 -51.978 1.00 32.65  ? 182  VAL   B C      1 
ATOM   6273 O O      . VAL   B  2 190 ? 28.499 -105.377 -51.594 1.00 31.71  ? 182  VAL   B O      1 
ATOM   6274 C CB     . VAL   B  2 190 ? 27.199 -104.703 -54.405 1.00 31.25  ? 182  VAL   B CB     1 
ATOM   6275 C CG1    . VAL   B  2 190 ? 25.756 -104.835 -53.908 1.00 30.90  ? 182  VAL   B CG1    1 
ATOM   6276 C CG2    . VAL   B  2 190 ? 27.223 -104.131 -55.827 1.00 31.16  ? 182  VAL   B CG2    1 
ATOM   6277 N N      . PHE   B  2 191 ? 27.243 -103.533 -51.173 1.00 28.61  ? 183  PHE   B N      1 
ATOM   6278 C CA     . PHE   B  2 191 ? 26.954 -103.847 -49.775 1.00 28.24  ? 183  PHE   B CA     1 
ATOM   6279 C C      . PHE   B  2 191 ? 25.629 -103.233 -49.328 1.00 32.63  ? 183  PHE   B C      1 
ATOM   6280 O O      . PHE   B  2 191 ? 25.079 -102.371 -50.017 1.00 32.09  ? 183  PHE   B O      1 
ATOM   6281 C CB     . PHE   B  2 191 ? 28.112 -103.438 -48.839 1.00 29.53  ? 183  PHE   B CB     1 
ATOM   6282 C CG     . PHE   B  2 191 ? 28.477 -101.972 -48.768 1.00 30.34  ? 183  PHE   B CG     1 
ATOM   6283 C CD1    . PHE   B  2 191 ? 27.950 -101.155 -47.776 1.00 32.85  ? 183  PHE   B CD1    1 
ATOM   6284 C CD2    . PHE   B  2 191 ? 29.426 -101.434 -49.630 1.00 31.73  ? 183  PHE   B CD2    1 
ATOM   6285 C CE1    . PHE   B  2 191 ? 28.341 -99.817  -47.668 1.00 33.45  ? 183  PHE   B CE1    1 
ATOM   6286 C CE2    . PHE   B  2 191 ? 29.802 -100.092 -49.533 1.00 34.28  ? 183  PHE   B CE2    1 
ATOM   6287 C CZ     . PHE   B  2 191 ? 29.263 -99.293  -48.548 1.00 32.33  ? 183  PHE   B CZ     1 
ATOM   6288 N N      . LEU   B  2 192 ? 25.110 -103.698 -48.190 1.00 28.38  ? 184  LEU   B N      1 
ATOM   6289 C CA     . LEU   B  2 192 ? 23.893 -103.179 -47.581 1.00 27.39  ? 184  LEU   B CA     1 
ATOM   6290 C C      . LEU   B  2 192 ? 24.211 -102.527 -46.242 1.00 30.82  ? 184  LEU   B C      1 
ATOM   6291 O O      . LEU   B  2 192 ? 25.173 -102.906 -45.561 1.00 29.79  ? 184  LEU   B O      1 
ATOM   6292 C CB     . LEU   B  2 192 ? 22.880 -104.297 -47.337 1.00 27.07  ? 184  LEU   B CB     1 
ATOM   6293 C CG     . LEU   B  2 192 ? 22.101 -104.826 -48.521 1.00 31.85  ? 184  LEU   B CG     1 
ATOM   6294 C CD1    . LEU   B  2 192 ? 21.505 -106.167 -48.179 1.00 32.17  ? 184  LEU   B CD1    1 
ATOM   6295 C CD2    . LEU   B  2 192 ? 20.997 -103.837 -48.985 1.00 32.67  ? 184  LEU   B CD2    1 
ATOM   6296 N N      . SER   B  2 193 ? 23.379 -101.566 -45.849 1.00 27.30  ? 185  SER   B N      1 
ATOM   6297 C CA     . SER   B  2 193 ? 23.466 -100.921 -44.554 1.00 26.11  ? 185  SER   B CA     1 
ATOM   6298 C C      . SER   B  2 193 ? 22.079 -100.587 -44.049 1.00 31.32  ? 185  SER   B C      1 
ATOM   6299 O O      . SER   B  2 193 ? 21.174 -100.326 -44.842 1.00 31.72  ? 185  SER   B O      1 
ATOM   6300 C CB     . SER   B  2 193 ? 24.351 -99.680  -44.596 1.00 28.22  ? 185  SER   B CB     1 
ATOM   6301 O OG     . SER   B  2 193 ? 23.725 -98.546  -45.171 1.00 28.51  ? 185  SER   B OG     1 
ATOM   6302 N N      . CYS   B  2 194 ? 21.896 -100.643 -42.731 1.00 27.11  ? 186  CYS   B N      1 
ATOM   6303 C CA     . CYS   B  2 194 ? 20.647 -100.249 -42.100 1.00 26.38  ? 186  CYS   B CA     1 
ATOM   6304 C C      . CYS   B  2 194 ? 20.933 -99.419  -40.860 1.00 28.79  ? 186  CYS   B C      1 
ATOM   6305 O O      . CYS   B  2 194 ? 22.045 -99.471  -40.315 1.00 26.90  ? 186  CYS   B O      1 
ATOM   6306 C CB     . CYS   B  2 194 ? 19.697 -101.418 -41.850 1.00 26.92  ? 186  CYS   B CB     1 
ATOM   6307 S SG     . CYS   B  2 194 ? 20.179 -102.524 -40.508 1.00 30.94  ? 186  CYS   B SG     1 
ATOM   6308 N N      . SER   B  2 195 ? 19.987 -98.548  -40.500 1.00 24.87  ? 187  SER   B N      1 
ATOM   6309 C CA     . SER   B  2 195 ? 20.204 -97.607  -39.416 1.00 24.22  ? 187  SER   B CA     1 
ATOM   6310 C C      . SER   B  2 195 ? 18.938 -97.248  -38.650 1.00 29.21  ? 187  SER   B C      1 
ATOM   6311 O O      . SER   B  2 195 ? 17.823 -97.605  -39.055 1.00 28.33  ? 187  SER   B O      1 
ATOM   6312 C CB     . SER   B  2 195 ? 20.907 -96.367  -39.975 1.00 26.66  ? 187  SER   B CB     1 
ATOM   6313 O OG     . SER   B  2 195 ? 20.498 -95.111  -39.461 1.00 31.77  ? 187  SER   B OG     1 
ATOM   6314 N N      . GLU   B  2 196 ? 19.128 -96.527  -37.531 1.00 26.21  ? 188  GLU   B N      1 
ATOM   6315 C CA     . GLU   B  2 196 ? 18.054 -96.029  -36.682 1.00 26.24  ? 188  GLU   B CA     1 
ATOM   6316 C C      . GLU   B  2 196 ? 17.277 -94.886  -37.364 1.00 29.58  ? 188  GLU   B C      1 
ATOM   6317 O O      . GLU   B  2 196 ? 16.215 -94.500  -36.872 1.00 31.27  ? 188  GLU   B O      1 
ATOM   6318 C CB     . GLU   B  2 196 ? 18.578 -95.648  -35.282 1.00 27.61  ? 188  GLU   B CB     1 
ATOM   6319 C CG     . GLU   B  2 196 ? 19.032 -96.865  -34.485 1.00 40.14  ? 188  GLU   B CG     1 
ATOM   6320 C CD     . GLU   B  2 196 ? 18.963 -96.763  -32.972 1.00 70.53  ? 188  GLU   B CD     1 
ATOM   6321 O OE1    . GLU   B  2 196 ? 19.204 -95.662  -32.423 1.00 70.82  ? 188  GLU   B OE1    1 
ATOM   6322 O OE2    . GLU   B  2 196 ? 18.697 -97.806  -32.331 1.00 69.14  ? 188  GLU   B OE2    1 
ATOM   6323 N N      . ASP   B  2 197 ? 17.768 -94.389  -38.524 1.00 24.00  ? 189  ASP   B N      1 
ATOM   6324 C CA     . ASP   B  2 197 ? 17.082 -93.381  -39.341 1.00 22.95  ? 189  ASP   B CA     1 
ATOM   6325 C C      . ASP   B  2 197 ? 15.960 -94.053  -40.180 1.00 28.38  ? 189  ASP   B C      1 
ATOM   6326 O O      . ASP   B  2 197 ? 15.323 -93.394  -41.000 1.00 28.93  ? 189  ASP   B O      1 
ATOM   6327 C CB     . ASP   B  2 197 ? 18.080 -92.585  -40.215 1.00 23.99  ? 189  ASP   B CB     1 
ATOM   6328 C CG     . ASP   B  2 197 ? 18.759 -93.329  -41.371 1.00 27.78  ? 189  ASP   B CG     1 
ATOM   6329 O OD1    . ASP   B  2 197 ? 18.572 -94.558  -41.486 1.00 28.44  ? 189  ASP   B OD1    1 
ATOM   6330 O OD2    . ASP   B  2 197 ? 19.469 -92.678  -42.155 1.00 27.32  ? 189  ASP   B OD2    1 
ATOM   6331 N N      . ASN   B  2 198 ? 15.732 -95.374  -39.960 1.00 25.63  ? 190  ASN   B N      1 
ATOM   6332 C CA     . ASN   B  2 198 ? 14.725 -96.222  -40.615 1.00 26.39  ? 190  ASN   B CA     1 
ATOM   6333 C C      . ASN   B  2 198 ? 15.019 -96.503  -42.121 1.00 31.27  ? 190  ASN   B C      1 
ATOM   6334 O O      . ASN   B  2 198 ? 14.134 -96.975  -42.840 1.00 32.16  ? 190  ASN   B O      1 
ATOM   6335 C CB     . ASN   B  2 198 ? 13.298 -95.681  -40.409 1.00 26.42  ? 190  ASN   B CB     1 
ATOM   6336 C CG     . ASN   B  2 198 ? 12.227 -96.738  -40.450 1.00 41.75  ? 190  ASN   B CG     1 
ATOM   6337 O OD1    . ASN   B  2 198 ? 12.470 -97.918  -40.210 1.00 37.97  ? 190  ASN   B OD1    1 
ATOM   6338 N ND2    . ASN   B  2 198 ? 11.015 -96.337  -40.778 1.00 36.87  ? 190  ASN   B ND2    1 
ATOM   6339 N N      . ARG   B  2 199 ? 16.267 -96.270  -42.572 1.00 27.16  ? 191  ARG   B N      1 
ATOM   6340 C CA     . ARG   B  2 199 ? 16.668 -96.551  -43.950 1.00 27.28  ? 191  ARG   B CA     1 
ATOM   6341 C C      . ARG   B  2 199 ? 17.409 -97.875  -44.074 1.00 32.49  ? 191  ARG   B C      1 
ATOM   6342 O O      . ARG   B  2 199 ? 18.240 -98.208  -43.225 1.00 32.50  ? 191  ARG   B O      1 
ATOM   6343 C CB     . ARG   B  2 199 ? 17.605 -95.461  -44.504 1.00 26.66  ? 191  ARG   B CB     1 
ATOM   6344 C CG     . ARG   B  2 199 ? 16.962 -94.099  -44.764 1.00 25.15  ? 191  ARG   B CG     1 
ATOM   6345 C CD     . ARG   B  2 199 ? 18.000 -93.105  -45.258 1.00 26.73  ? 191  ARG   B CD     1 
ATOM   6346 N NE     . ARG   B  2 199 ? 17.373 -91.839  -45.645 1.00 32.91  ? 191  ARG   B NE     1 
ATOM   6347 C CZ     . ARG   B  2 199 ? 17.571 -90.674  -45.033 1.00 47.93  ? 191  ARG   B CZ     1 
ATOM   6348 N NH1    . ARG   B  2 199 ? 18.428 -90.582  -44.022 1.00 39.16  ? 191  ARG   B NH1    1 
ATOM   6349 N NH2    . ARG   B  2 199 ? 16.941 -89.585  -45.448 1.00 33.94  ? 191  ARG   B NH2    1 
ATOM   6350 N N      . ILE   B  2 200 ? 17.142 -98.593  -45.174 1.00 28.33  ? 192  ILE   B N      1 
ATOM   6351 C CA     . ILE   B  2 200 ? 17.885 -99.763  -45.625 1.00 27.25  ? 192  ILE   B CA     1 
ATOM   6352 C C      . ILE   B  2 200 ? 18.506 -99.264  -46.930 1.00 29.67  ? 192  ILE   B C      1 
ATOM   6353 O O      . ILE   B  2 200 ? 17.777 -98.980  -47.892 1.00 28.83  ? 192  ILE   B O      1 
ATOM   6354 C CB     . ILE   B  2 200 ? 17.048 -101.051 -45.858 1.00 30.29  ? 192  ILE   B CB     1 
ATOM   6355 C CG1    . ILE   B  2 200 ? 16.466 -101.593 -44.537 1.00 30.49  ? 192  ILE   B CG1    1 
ATOM   6356 C CG2    . ILE   B  2 200 ? 17.933 -102.122 -46.561 1.00 30.86  ? 192  ILE   B CG2    1 
ATOM   6357 C CD1    . ILE   B  2 200 ? 15.339 -102.603 -44.685 1.00 42.12  ? 192  ILE   B CD1    1 
ATOM   6358 N N      . LEU   B  2 201 ? 19.835 -99.110  -46.945 1.00 24.92  ? 193  LEU   B N      1 
ATOM   6359 C CA     . LEU   B  2 201 ? 20.553 -98.638  -48.116 1.00 24.79  ? 193  LEU   B CA     1 
ATOM   6360 C C      . LEU   B  2 201 ? 21.301 -99.750  -48.845 1.00 29.66  ? 193  LEU   B C      1 
ATOM   6361 O O      . LEU   B  2 201 ? 21.993 -100.560 -48.216 1.00 26.94  ? 193  LEU   B O      1 
ATOM   6362 C CB     . LEU   B  2 201 ? 21.521 -97.492  -47.770 1.00 24.72  ? 193  LEU   B CB     1 
ATOM   6363 C CG     . LEU   B  2 201 ? 20.904 -96.191  -47.231 1.00 28.62  ? 193  LEU   B CG     1 
ATOM   6364 C CD1    . LEU   B  2 201 ? 21.975 -95.250  -46.803 1.00 27.43  ? 193  LEU   B CD1    1 
ATOM   6365 C CD2    . LEU   B  2 201 ? 20.034 -95.501  -48.283 1.00 32.20  ? 193  LEU   B CD2    1 
ATOM   6366 N N      . LEU   B  2 202 ? 21.139 -99.778  -50.184 1.00 27.74  ? 194  LEU   B N      1 
ATOM   6367 C CA     . LEU   B  2 202 ? 21.833 -100.682 -51.099 1.00 28.25  ? 194  LEU   B CA     1 
ATOM   6368 C C      . LEU   B  2 202 ? 22.927 -99.850  -51.727 1.00 31.86  ? 194  LEU   B C      1 
ATOM   6369 O O      . LEU   B  2 202 ? 22.657 -98.804  -52.314 1.00 30.87  ? 194  LEU   B O      1 
ATOM   6370 C CB     . LEU   B  2 202 ? 20.885 -101.280 -52.156 1.00 29.14  ? 194  LEU   B CB     1 
ATOM   6371 C CG     . LEU   B  2 202 ? 21.532 -102.035 -53.358 1.00 34.38  ? 194  LEU   B CG     1 
ATOM   6372 C CD1    . LEU   B  2 202 ? 22.298 -103.285 -52.906 1.00 34.18  ? 194  LEU   B CD1    1 
ATOM   6373 C CD2    . LEU   B  2 202 ? 20.488 -102.403 -54.389 1.00 36.19  ? 194  LEU   B CD2    1 
ATOM   6374 N N      . TRP   B  2 203 ? 24.168 -100.250 -51.493 1.00 30.02  ? 195  TRP   B N      1 
ATOM   6375 C CA     . TRP   B  2 203 ? 25.338 -99.523  -51.955 1.00 30.31  ? 195  TRP   B CA     1 
ATOM   6376 C C      . TRP   B  2 203 ? 26.011 -100.160 -53.164 1.00 36.19  ? 195  TRP   B C      1 
ATOM   6377 O O      . TRP   B  2 203 ? 26.079 -101.385 -53.266 1.00 34.99  ? 195  TRP   B O      1 
ATOM   6378 C CB     . TRP   B  2 203 ? 26.360 -99.429  -50.829 1.00 29.03  ? 195  TRP   B CB     1 
ATOM   6379 C CG     . TRP   B  2 203 ? 25.912 -98.623  -49.643 1.00 29.87  ? 195  TRP   B CG     1 
ATOM   6380 C CD1    . TRP   B  2 203 ? 25.118 -99.042  -48.613 1.00 32.74  ? 195  TRP   B CD1    1 
ATOM   6381 C CD2    . TRP   B  2 203 ? 26.351 -97.306  -49.303 1.00 29.56  ? 195  TRP   B CD2    1 
ATOM   6382 N NE1    . TRP   B  2 203 ? 25.000 -98.045  -47.672 1.00 31.90  ? 195  TRP   B NE1    1 
ATOM   6383 C CE2    . TRP   B  2 203 ? 25.740 -96.963  -48.075 1.00 33.40  ? 195  TRP   B CE2    1 
ATOM   6384 C CE3    . TRP   B  2 203 ? 27.175 -96.361  -49.937 1.00 30.95  ? 195  TRP   B CE3    1 
ATOM   6385 C CZ2    . TRP   B  2 203 ? 25.923 -95.714  -47.471 1.00 33.03  ? 195  TRP   B CZ2    1 
ATOM   6386 C CZ3    . TRP   B  2 203 ? 27.368 -95.129  -49.332 1.00 32.74  ? 195  TRP   B CZ3    1 
ATOM   6387 C CH2    . TRP   B  2 203 ? 26.748 -94.816  -48.114 1.00 33.46  ? 195  TRP   B CH2    1 
ATOM   6388 N N      . ASP   B  2 204 ? 26.514 -99.303  -54.071 1.00 33.57  ? 196  ASP   B N      1 
ATOM   6389 C CA     . ASP   B  2 204 ? 27.319 -99.651  -55.237 1.00 32.94  ? 196  ASP   B CA     1 
ATOM   6390 C C      . ASP   B  2 204 ? 28.291 -98.501  -55.407 1.00 36.76  ? 196  ASP   B C      1 
ATOM   6391 O O      . ASP   B  2 204 ? 27.915 -97.429  -55.891 1.00 36.40  ? 196  ASP   B O      1 
ATOM   6392 C CB     . ASP   B  2 204 ? 26.492 -99.907  -56.512 1.00 34.75  ? 196  ASP   B CB     1 
ATOM   6393 C CG     . ASP   B  2 204 ? 27.261 -100.692 -57.579 1.00 41.87  ? 196  ASP   B CG     1 
ATOM   6394 O OD1    . ASP   B  2 204 ? 28.485 -100.451 -57.737 1.00 41.43  ? 196  ASP   B OD1    1 
ATOM   6395 O OD2    . ASP   B  2 204 ? 26.641 -101.544 -58.252 1.00 45.88  ? 196  ASP   B OD2    1 
ATOM   6396 N N      . THR   B  2 205 ? 29.538 -98.717  -54.969 1.00 33.47  ? 197  THR   B N      1 
ATOM   6397 C CA     . THR   B  2 205 ? 30.596 -97.704  -54.958 1.00 33.81  ? 197  THR   B CA     1 
ATOM   6398 C C      . THR   B  2 205 ? 31.095 -97.292  -56.360 1.00 38.94  ? 197  THR   B C      1 
ATOM   6399 O O      . THR   B  2 205 ? 31.973 -96.429  -56.454 1.00 39.82  ? 197  THR   B O      1 
ATOM   6400 C CB     . THR   B  2 205 ? 31.744 -98.136  -54.036 1.00 42.33  ? 197  THR   B CB     1 
ATOM   6401 O OG1    . THR   B  2 205 ? 32.279 -99.377  -54.491 1.00 42.22  ? 197  THR   B OG1    1 
ATOM   6402 C CG2    . THR   B  2 205 ? 31.310 -98.242  -52.570 1.00 41.10  ? 197  THR   B CG2    1 
ATOM   6403 N N      . ARG   B  2 206 ? 30.512 -97.851  -57.435 1.00 35.55  ? 198  ARG   B N      1 
ATOM   6404 C CA     . ARG   B  2 206 ? 30.845 -97.484  -58.816 1.00 35.19  ? 198  ARG   B CA     1 
ATOM   6405 C C      . ARG   B  2 206 ? 29.981 -96.298  -59.322 1.00 40.77  ? 198  ARG   B C      1 
ATOM   6406 O O      . ARG   B  2 206 ? 30.210 -95.808  -60.430 1.00 40.01  ? 198  ARG   B O      1 
ATOM   6407 C CB     . ARG   B  2 206 ? 30.727 -98.702  -59.748 1.00 34.17  ? 198  ARG   B CB     1 
ATOM   6408 C CG     . ARG   B  2 206 ? 31.705 -99.830  -59.378 1.00 39.41  ? 198  ARG   B CG     1 
ATOM   6409 C CD     . ARG   B  2 206 ? 31.460 -101.126 -60.129 1.00 40.89  ? 198  ARG   B CD     1 
ATOM   6410 N NE     . ARG   B  2 206 ? 30.130 -101.689 -59.883 1.00 34.79  ? 198  ARG   B NE     1 
ATOM   6411 C CZ     . ARG   B  2 206 ? 29.776 -102.931 -60.202 1.00 48.99  ? 198  ARG   B CZ     1 
ATOM   6412 N NH1    . ARG   B  2 206 ? 30.657 -103.761 -60.755 1.00 35.45  ? 198  ARG   B NH1    1 
ATOM   6413 N NH2    . ARG   B  2 206 ? 28.544 -103.360 -59.955 1.00 30.24  ? 198  ARG   B NH2    1 
ATOM   6414 N N      . CYS   B  2 207 ? 29.016 -95.826  -58.493 1.00 37.79  ? 199  CYS   B N      1 
ATOM   6415 C CA     . CYS   B  2 207 ? 28.113 -94.707  -58.795 1.00 38.22  ? 199  CYS   B CA     1 
ATOM   6416 C C      . CYS   B  2 207 ? 28.545 -93.397  -58.112 1.00 42.58  ? 199  CYS   B C      1 
ATOM   6417 O O      . CYS   B  2 207 ? 29.053 -93.452  -56.988 1.00 41.69  ? 199  CYS   B O      1 
ATOM   6418 C CB     . CYS   B  2 207 ? 26.680 -95.061  -58.414 1.00 38.36  ? 199  CYS   B CB     1 
ATOM   6419 S SG     . CYS   B  2 207 ? 26.053 -96.544  -59.225 1.00 42.22  ? 199  CYS   B SG     1 
ATOM   6420 N N      . PRO   B  2 208 ? 28.284 -92.211  -58.731 1.00 39.90  ? 200  PRO   B N      1 
ATOM   6421 C CA     . PRO   B  2 208 ? 28.623 -90.934  -58.060 1.00 39.10  ? 200  PRO   B CA     1 
ATOM   6422 C C      . PRO   B  2 208 ? 27.829 -90.728  -56.766 1.00 40.76  ? 200  PRO   B C      1 
ATOM   6423 O O      . PRO   B  2 208 ? 28.371 -90.177  -55.807 1.00 40.71  ? 200  PRO   B O      1 
ATOM   6424 C CB     . PRO   B  2 208 ? 28.312 -89.873  -59.123 1.00 41.06  ? 200  PRO   B CB     1 
ATOM   6425 C CG     . PRO   B  2 208 ? 27.337 -90.509  -60.035 1.00 45.81  ? 200  PRO   B CG     1 
ATOM   6426 C CD     . PRO   B  2 208 ? 27.662 -91.974  -60.052 1.00 41.40  ? 200  PRO   B CD     1 
ATOM   6427 N N      . LYS   B  2 209 ? 26.561 -91.213  -56.728 1.00 35.05  ? 201  LYS   B N      1 
ATOM   6428 C CA     . LYS   B  2 209 ? 25.687 -91.235  -55.548 1.00 33.81  ? 201  LYS   B CA     1 
ATOM   6429 C C      . LYS   B  2 209 ? 25.565 -92.739  -55.232 1.00 34.81  ? 201  LYS   B C      1 
ATOM   6430 O O      . LYS   B  2 209 ? 24.694 -93.419  -55.794 1.00 32.60  ? 201  LYS   B O      1 
ATOM   6431 C CB     . LYS   B  2 209 ? 24.318 -90.583  -55.831 1.00 36.10  ? 201  LYS   B CB     1 
ATOM   6432 C CG     . LYS   B  2 209 ? 24.360 -89.063  -55.859 1.00 47.62  ? 201  LYS   B CG     1 
ATOM   6433 C CD     . LYS   B  2 209 ? 22.970 -88.476  -56.020 1.00 55.89  ? 201  LYS   B CD     1 
ATOM   6434 C CE     . LYS   B  2 209 ? 22.986 -86.965  -55.976 1.00 67.57  ? 201  LYS   B CE     1 
ATOM   6435 N NZ     . LYS   B  2 209 ? 21.610 -86.400  -56.003 1.00 76.76  ? 201  LYS   B NZ     1 
ATOM   6436 N N      . PRO   B  2 210 ? 26.505 -93.282  -54.409 1.00 32.24  ? 202  PRO   B N      1 
ATOM   6437 C CA     . PRO   B  2 210 ? 26.566 -94.745  -54.200 1.00 32.43  ? 202  PRO   B CA     1 
ATOM   6438 C C      . PRO   B  2 210 ? 25.386 -95.445  -53.544 1.00 35.77  ? 202  PRO   B C      1 
ATOM   6439 O O      . PRO   B  2 210 ? 25.261 -96.660  -53.706 1.00 34.93  ? 202  PRO   B O      1 
ATOM   6440 C CB     . PRO   B  2 210 ? 27.811 -94.939  -53.326 1.00 34.39  ? 202  PRO   B CB     1 
ATOM   6441 C CG     . PRO   B  2 210 ? 28.569 -93.691  -53.402 1.00 38.89  ? 202  PRO   B CG     1 
ATOM   6442 C CD     . PRO   B  2 210 ? 27.626 -92.598  -53.730 1.00 34.23  ? 202  PRO   B CD     1 
ATOM   6443 N N      . ALA   B  2 211 ? 24.567 -94.731  -52.766 1.00 31.56  ? 203  ALA   B N      1 
ATOM   6444 C CA     . ALA   B  2 211 ? 23.483 -95.396  -52.054 1.00 31.03  ? 203  ALA   B CA     1 
ATOM   6445 C C      . ALA   B  2 211 ? 22.131 -95.283  -52.722 1.00 34.31  ? 203  ALA   B C      1 
ATOM   6446 O O      . ALA   B  2 211 ? 21.855 -94.316  -53.430 1.00 34.34  ? 203  ALA   B O      1 
ATOM   6447 C CB     . ALA   B  2 211 ? 23.413 -94.895  -50.612 1.00 31.78  ? 203  ALA   B CB     1 
ATOM   6448 N N      . SER   B  2 212 ? 21.278 -96.269  -52.462 1.00 30.53  ? 204  SER   B N      1 
ATOM   6449 C CA     . SER   B  2 212 ? 19.912 -96.316  -52.952 1.00 30.35  ? 204  SER   B CA     1 
ATOM   6450 C C      . SER   B  2 212 ? 19.045 -96.843  -51.819 1.00 34.14  ? 204  SER   B C      1 
ATOM   6451 O O      . SER   B  2 212 ? 19.368 -97.873  -51.220 1.00 32.70  ? 204  SER   B O      1 
ATOM   6452 C CB     . SER   B  2 212 ? 19.812 -97.209  -54.188 1.00 35.06  ? 204  SER   B CB     1 
ATOM   6453 O OG     . SER   B  2 212 ? 18.478 -97.304  -54.661 1.00 44.18  ? 204  SER   B OG     1 
ATOM   6454 N N      . GLN   B  2 213 ? 17.973 -96.105  -51.486 1.00 32.53  ? 205  GLN   B N      1 
ATOM   6455 C CA     . GLN   B  2 213 ? 17.025 -96.488  -50.440 1.00 33.21  ? 205  GLN   B CA     1 
ATOM   6456 C C      . GLN   B  2 213 ? 16.124 -97.582  -51.001 1.00 39.39  ? 205  GLN   B C      1 
ATOM   6457 O O      . GLN   B  2 213 ? 15.484 -97.370  -52.033 1.00 39.78  ? 205  GLN   B O      1 
ATOM   6458 C CB     . GLN   B  2 213 ? 16.207 -95.263  -49.982 1.00 34.69  ? 205  GLN   B CB     1 
ATOM   6459 C CG     . GLN   B  2 213 ? 16.236 -95.029  -48.484 1.00 46.41  ? 205  GLN   B CG     1 
ATOM   6460 C CD     . GLN   B  2 213 ? 15.506 -93.764  -48.106 1.00 56.76  ? 205  GLN   B CD     1 
ATOM   6461 O OE1    . GLN   B  2 213 ? 16.024 -92.648  -48.246 1.00 49.84  ? 205  GLN   B OE1    1 
ATOM   6462 N NE2    . GLN   B  2 213 ? 14.288 -93.916  -47.602 1.00 44.61  ? 205  GLN   B NE2    1 
ATOM   6463 N N      . ILE   B  2 214 ? 16.115 -98.767  -50.355 1.00 37.62  ? 206  ILE   B N      1 
ATOM   6464 C CA     . ILE   B  2 214 ? 15.343 -99.935  -50.797 1.00 72.89  ? 206  ILE   B CA     1 
ATOM   6465 C C      . ILE   B  2 214 ? 14.292 -100.339 -49.758 1.00 107.56 ? 206  ILE   B C      1 
ATOM   6466 O O      . ILE   B  2 214 ? 14.612 -100.514 -48.587 1.00 77.47  ? 206  ILE   B O      1 
ATOM   6467 C CB     . ILE   B  2 214 ? 16.299 -101.104 -51.210 1.00 76.07  ? 206  ILE   B CB     1 
ATOM   6468 C CG1    . ILE   B  2 214 ? 17.168 -100.746 -52.461 1.00 76.56  ? 206  ILE   B CG1    1 
ATOM   6469 C CG2    . ILE   B  2 214 ? 15.567 -102.445 -51.390 1.00 77.07  ? 206  ILE   B CG2    1 
ATOM   6470 C CD1    . ILE   B  2 214 ? 16.424 -100.437 -53.864 1.00 83.76  ? 206  ILE   B CD1    1 
ATOM   6471 N N      . ALA   B  2 218 ? 6.935  -96.796  -47.553 1.00 70.71  ? 210  ALA   B N      1 
ATOM   6472 C CA     . ALA   B  2 218 ? 6.237  -96.436  -46.321 1.00 70.46  ? 210  ALA   B CA     1 
ATOM   6473 C C      . ALA   B  2 218 ? 7.080  -96.751  -45.063 1.00 73.40  ? 210  ALA   B C      1 
ATOM   6474 O O      . ALA   B  2 218 ? 7.549  -97.888  -44.917 1.00 73.02  ? 210  ALA   B O      1 
ATOM   6475 C CB     . ALA   B  2 218 ? 4.888  -97.144  -46.251 1.00 71.23  ? 210  ALA   B CB     1 
ATOM   6476 N N      . PRO   B  2 219 ? 7.279  -95.765  -44.145 1.00 68.47  ? 211  PRO   B N      1 
ATOM   6477 C CA     . PRO   B  2 219 ? 8.088  -96.030  -42.940 1.00 67.32  ? 211  PRO   B CA     1 
ATOM   6478 C C      . PRO   B  2 219 ? 7.348  -96.830  -41.864 1.00 67.46  ? 211  PRO   B C      1 
ATOM   6479 O O      . PRO   B  2 219 ? 6.158  -96.600  -41.618 1.00 67.49  ? 211  PRO   B O      1 
ATOM   6480 C CB     . PRO   B  2 219 ? 8.473  -94.622  -42.444 1.00 69.31  ? 211  PRO   B CB     1 
ATOM   6481 C CG     . PRO   B  2 219 ? 7.941  -93.647  -43.485 1.00 74.08  ? 211  PRO   B CG     1 
ATOM   6482 C CD     . PRO   B  2 219 ? 6.821  -94.363  -44.168 1.00 69.90  ? 211  PRO   B CD     1 
ATOM   6483 N N      . GLY   B  2 220 ? 8.075  -97.756  -41.235 1.00 59.97  ? 212  GLY   B N      1 
ATOM   6484 C CA     . GLY   B  2 220 ? 7.571  -98.624  -40.175 1.00 57.33  ? 212  GLY   B CA     1 
ATOM   6485 C C      . GLY   B  2 220 ? 8.586  -98.863  -39.074 1.00 54.93  ? 212  GLY   B C      1 
ATOM   6486 O O      . GLY   B  2 220 ? 9.246  -97.920  -38.620 1.00 54.93  ? 212  GLY   B O      1 
ATOM   6487 N N      . TYR   B  2 221 ? 8.715  -100.134 -38.635 1.00 45.82  ? 213  TYR   B N      1 
ATOM   6488 C CA     . TYR   B  2 221 ? 9.642  -100.541 -37.573 1.00 42.48  ? 213  TYR   B CA     1 
ATOM   6489 C C      . TYR   B  2 221 ? 11.091 -100.550 -38.042 1.00 41.49  ? 213  TYR   B C      1 
ATOM   6490 O O      . TYR   B  2 221 ? 11.373 -100.951 -39.172 1.00 41.34  ? 213  TYR   B O      1 
ATOM   6491 C CB     . TYR   B  2 221 ? 9.221  -101.878 -36.943 1.00 42.56  ? 213  TYR   B CB     1 
ATOM   6492 C CG     . TYR   B  2 221 ? 7.885  -101.794 -36.236 1.00 42.98  ? 213  TYR   B CG     1 
ATOM   6493 C CD1    . TYR   B  2 221 ? 7.709  -100.967 -35.129 1.00 44.51  ? 213  TYR   B CD1    1 
ATOM   6494 C CD2    . TYR   B  2 221 ? 6.784  -102.511 -36.694 1.00 43.70  ? 213  TYR   B CD2    1 
ATOM   6495 C CE1    . TYR   B  2 221 ? 6.477  -100.869 -34.487 1.00 44.76  ? 213  TYR   B CE1    1 
ATOM   6496 C CE2    . TYR   B  2 221 ? 5.545  -102.423 -36.057 1.00 44.56  ? 213  TYR   B CE2    1 
ATOM   6497 C CZ     . TYR   B  2 221 ? 5.398  -101.602 -34.950 1.00 50.68  ? 213  TYR   B CZ     1 
ATOM   6498 O OH     . TYR   B  2 221 ? 4.188  -101.502 -34.306 1.00 51.11  ? 213  TYR   B OH     1 
ATOM   6499 N N      . LEU   B  2 222 ? 12.000 -100.064 -37.180 1.00 33.97  ? 214  LEU   B N      1 
ATOM   6500 C CA     . LEU   B  2 222 ? 13.426 -99.924  -37.463 1.00 31.98  ? 214  LEU   B CA     1 
ATOM   6501 C C      . LEU   B  2 222 ? 14.124 -101.219 -37.888 1.00 33.05  ? 214  LEU   B C      1 
ATOM   6502 O O      . LEU   B  2 222 ? 13.961 -102.237 -37.219 1.00 30.82  ? 214  LEU   B O      1 
ATOM   6503 C CB     . LEU   B  2 222 ? 14.184 -99.286  -36.281 1.00 31.57  ? 214  LEU   B CB     1 
ATOM   6504 C CG     . LEU   B  2 222 ? 13.753 -97.885  -35.831 1.00 35.26  ? 214  LEU   B CG     1 
ATOM   6505 C CD1    . LEU   B  2 222 ? 14.558 -97.434  -34.604 1.00 34.33  ? 214  LEU   B CD1    1 
ATOM   6506 C CD2    . LEU   B  2 222 ? 13.888 -96.874  -36.961 1.00 36.88  ? 214  LEU   B CD2    1 
ATOM   6507 N N      . PRO   B  2 223 ? 14.947 -101.177 -38.963 1.00 28.83  ? 215  PRO   B N      1 
ATOM   6508 C CA     . PRO   B  2 223 ? 15.686 -102.386 -39.366 1.00 28.19  ? 215  PRO   B CA     1 
ATOM   6509 C C      . PRO   B  2 223 ? 16.880 -102.613 -38.440 1.00 31.04  ? 215  PRO   B C      1 
ATOM   6510 O O      . PRO   B  2 223 ? 17.612 -101.666 -38.154 1.00 30.55  ? 215  PRO   B O      1 
ATOM   6511 C CB     . PRO   B  2 223 ? 16.106 -102.078 -40.806 1.00 29.62  ? 215  PRO   B CB     1 
ATOM   6512 C CG     . PRO   B  2 223 ? 16.183 -100.605 -40.877 1.00 34.04  ? 215  PRO   B CG     1 
ATOM   6513 C CD     . PRO   B  2 223 ? 15.255 -100.030 -39.845 1.00 29.89  ? 215  PRO   B CD     1 
ATOM   6514 N N      . THR   B  2 224 ? 17.078 -103.850 -37.957 1.00 27.76  ? 216  THR   B N      1 
ATOM   6515 C CA     . THR   B  2 224 ? 18.167 -104.130 -37.006 1.00 27.97  ? 216  THR   B CA     1 
ATOM   6516 C C      . THR   B  2 224 ? 19.226 -105.152 -37.470 1.00 32.95  ? 216  THR   B C      1 
ATOM   6517 O O      . THR   B  2 224 ? 20.333 -105.168 -36.921 1.00 32.05  ? 216  THR   B O      1 
ATOM   6518 C CB     . THR   B  2 224 ? 17.587 -104.551 -35.643 1.00 32.10  ? 216  THR   B CB     1 
ATOM   6519 O OG1    . THR   B  2 224 ? 16.647 -105.608 -35.832 1.00 30.70  ? 216  THR   B OG1    1 
ATOM   6520 C CG2    . THR   B  2 224 ? 16.941 -103.386 -34.901 1.00 26.07  ? 216  THR   B CG2    1 
ATOM   6521 N N      . SER   B  2 225 ? 18.894 -106.007 -38.450 1.00 29.91  ? 217  SER   B N      1 
ATOM   6522 C CA     . SER   B  2 225 ? 19.809 -107.045 -38.938 1.00 28.69  ? 217  SER   B CA     1 
ATOM   6523 C C      . SER   B  2 225 ? 19.634 -107.286 -40.433 1.00 32.30  ? 217  SER   B C      1 
ATOM   6524 O O      . SER   B  2 225 ? 18.514 -107.206 -40.935 1.00 31.52  ? 217  SER   B O      1 
ATOM   6525 C CB     . SER   B  2 225 ? 19.606 -108.338 -38.154 1.00 30.18  ? 217  SER   B CB     1 
ATOM   6526 O OG     . SER   B  2 225 ? 18.250 -108.747 -38.209 1.00 37.44  ? 217  SER   B OG     1 
ATOM   6527 N N      . LEU   B  2 226 ? 20.742 -107.574 -41.140 1.00 29.05  ? 218  LEU   B N      1 
ATOM   6528 C CA     . LEU   B  2 226 ? 20.753 -107.806 -42.595 1.00 28.95  ? 218  LEU   B CA     1 
ATOM   6529 C C      . LEU   B  2 226 ? 21.537 -109.061 -42.956 1.00 33.88  ? 218  LEU   B C      1 
ATOM   6530 O O      . LEU   B  2 226 ? 22.629 -109.273 -42.420 1.00 34.13  ? 218  LEU   B O      1 
ATOM   6531 C CB     . LEU   B  2 226 ? 21.429 -106.624 -43.329 1.00 28.70  ? 218  LEU   B CB     1 
ATOM   6532 C CG     . LEU   B  2 226 ? 20.877 -105.218 -43.150 1.00 32.66  ? 218  LEU   B CG     1 
ATOM   6533 C CD1    . LEU   B  2 226 ? 21.972 -104.202 -43.350 1.00 32.94  ? 218  LEU   B CD1    1 
ATOM   6534 C CD2    . LEU   B  2 226 ? 19.728 -104.954 -44.093 1.00 33.29  ? 218  LEU   B CD2    1 
ATOM   6535 N N      . ALA   B  2 227 ? 21.029 -109.844 -43.928 1.00 30.32  ? 219  ALA   B N      1 
ATOM   6536 C CA     . ALA   B  2 227 ? 21.732 -111.015 -44.450 1.00 29.85  ? 219  ALA   B CA     1 
ATOM   6537 C C      . ALA   B  2 227 ? 21.408 -111.262 -45.938 1.00 33.11  ? 219  ALA   B C      1 
ATOM   6538 O O      . ALA   B  2 227 ? 20.249 -111.457 -46.305 1.00 30.97  ? 219  ALA   B O      1 
ATOM   6539 C CB     . ALA   B  2 227 ? 21.429 -112.255 -43.616 1.00 30.52  ? 219  ALA   B CB     1 
ATOM   6540 N N      . TRP   B  2 228 ? 22.446 -111.244 -46.781 1.00 30.99  ? 220  TRP   B N      1 
ATOM   6541 C CA     . TRP   B  2 228 ? 22.351 -111.518 -48.219 1.00 31.80  ? 220  TRP   B CA     1 
ATOM   6542 C C      . TRP   B  2 228 ? 22.073 -113.002 -48.418 1.00 36.75  ? 220  TRP   B C      1 
ATOM   6543 O O      . TRP   B  2 228 ? 22.643 -113.821 -47.695 1.00 35.97  ? 220  TRP   B O      1 
ATOM   6544 C CB     . TRP   B  2 228 ? 23.685 -111.210 -48.893 1.00 30.48  ? 220  TRP   B CB     1 
ATOM   6545 C CG     . TRP   B  2 228 ? 23.977 -109.762 -49.105 1.00 31.35  ? 220  TRP   B CG     1 
ATOM   6546 C CD1    . TRP   B  2 228 ? 24.826 -108.981 -48.377 1.00 34.17  ? 220  TRP   B CD1    1 
ATOM   6547 C CD2    . TRP   B  2 228 ? 23.526 -108.957 -50.197 1.00 31.37  ? 220  TRP   B CD2    1 
ATOM   6548 N NE1    . TRP   B  2 228 ? 24.893 -107.721 -48.922 1.00 33.70  ? 220  TRP   B NE1    1 
ATOM   6549 C CE2    . TRP   B  2 228 ? 24.115 -107.682 -50.050 1.00 35.33  ? 220  TRP   B CE2    1 
ATOM   6550 C CE3    . TRP   B  2 228 ? 22.657 -109.184 -51.283 1.00 32.67  ? 220  TRP   B CE3    1 
ATOM   6551 C CZ2    . TRP   B  2 228 ? 23.882 -106.641 -50.960 1.00 34.64  ? 220  TRP   B CZ2    1 
ATOM   6552 C CZ3    . TRP   B  2 228 ? 22.394 -108.140 -52.157 1.00 34.01  ? 220  TRP   B CZ3    1 
ATOM   6553 C CH2    . TRP   B  2 228 ? 22.985 -106.881 -51.980 1.00 34.67  ? 220  TRP   B CH2    1 
ATOM   6554 N N      . HIS   B  2 229 ? 21.200 -113.354 -49.378 1.00 35.40  ? 221  HIS   B N      1 
ATOM   6555 C CA     . HIS   B  2 229 ? 20.918 -114.761 -49.674 1.00 36.28  ? 221  HIS   B CA     1 
ATOM   6556 C C      . HIS   B  2 229 ? 22.200 -115.357 -50.296 1.00 41.43  ? 221  HIS   B C      1 
ATOM   6557 O O      . HIS   B  2 229 ? 22.813 -114.698 -51.145 1.00 41.14  ? 221  HIS   B O      1 
ATOM   6558 C CB     . HIS   B  2 229 ? 19.722 -114.911 -50.625 1.00 37.28  ? 221  HIS   B CB     1 
ATOM   6559 C CG     . HIS   B  2 229 ? 19.251 -116.324 -50.765 1.00 40.85  ? 221  HIS   B CG     1 
ATOM   6560 N ND1    . HIS   B  2 229 ? 19.973 -117.260 -51.491 1.00 42.53  ? 221  HIS   B ND1    1 
ATOM   6561 C CD2    . HIS   B  2 229 ? 18.146 -116.919 -50.264 1.00 42.61  ? 221  HIS   B CD2    1 
ATOM   6562 C CE1    . HIS   B  2 229 ? 19.288 -118.388 -51.404 1.00 41.91  ? 221  HIS   B CE1    1 
ATOM   6563 N NE2    . HIS   B  2 229 ? 18.181 -118.232 -50.680 1.00 42.30  ? 221  HIS   B NE2    1 
ATOM   6564 N N      . PRO   B  2 230 ? 22.675 -116.539 -49.831 1.00 38.24  ? 222  PRO   B N      1 
ATOM   6565 C CA     . PRO   B  2 230 ? 23.956 -117.066 -50.350 1.00 38.32  ? 222  PRO   B CA     1 
ATOM   6566 C C      . PRO   B  2 230 ? 23.982 -117.470 -51.831 1.00 42.25  ? 222  PRO   B C      1 
ATOM   6567 O O      . PRO   B  2 230 ? 25.073 -117.491 -52.401 1.00 40.93  ? 222  PRO   B O      1 
ATOM   6568 C CB     . PRO   B  2 230 ? 24.268 -118.252 -49.429 1.00 39.76  ? 222  PRO   B CB     1 
ATOM   6569 C CG     . PRO   B  2 230 ? 22.958 -118.658 -48.863 1.00 44.09  ? 222  PRO   B CG     1 
ATOM   6570 C CD     . PRO   B  2 230 ? 22.112 -117.417 -48.785 1.00 39.48  ? 222  PRO   B CD     1 
ATOM   6571 N N      . GLN   B  2 231 ? 22.822 -117.757 -52.462 1.00 40.61  ? 223  GLN   B N      1 
ATOM   6572 C CA     . GLN   B  2 231 ? 22.799 -118.142 -53.886 1.00 41.35  ? 223  GLN   B CA     1 
ATOM   6573 C C      . GLN   B  2 231 ? 22.138 -117.125 -54.811 1.00 47.48  ? 223  GLN   B C      1 
ATOM   6574 O O      . GLN   B  2 231 ? 22.637 -116.900 -55.913 1.00 47.99  ? 223  GLN   B O      1 
ATOM   6575 C CB     . GLN   B  2 231 ? 22.174 -119.518 -54.095 1.00 42.66  ? 223  GLN   B CB     1 
ATOM   6576 C CG     . GLN   B  2 231 ? 23.000 -120.651 -53.506 1.00 56.14  ? 223  GLN   B CG     1 
ATOM   6577 C CD     . GLN   B  2 231 ? 22.288 -121.247 -52.329 1.00 74.77  ? 223  GLN   B CD     1 
ATOM   6578 O OE1    . GLN   B  2 231 ? 21.064 -121.426 -52.345 1.00 70.24  ? 223  GLN   B OE1    1 
ATOM   6579 N NE2    . GLN   B  2 231 ? 23.039 -121.567 -51.286 1.00 66.10  ? 223  GLN   B NE2    1 
ATOM   6580 N N      . GLN   B  2 232 ? 21.008 -116.548 -54.388 1.00 44.61  ? 224  GLN   B N      1 
ATOM   6581 C CA     . GLN   B  2 232 ? 20.274 -115.546 -55.158 1.00 44.52  ? 224  GLN   B CA     1 
ATOM   6582 C C      . GLN   B  2 232 ? 20.926 -114.182 -54.895 1.00 50.38  ? 224  GLN   B C      1 
ATOM   6583 O O      . GLN   B  2 232 ? 20.618 -113.512 -53.901 1.00 50.50  ? 224  GLN   B O      1 
ATOM   6584 C CB     . GLN   B  2 232 ? 18.788 -115.571 -54.773 1.00 45.42  ? 224  GLN   B CB     1 
ATOM   6585 C CG     . GLN   B  2 232 ? 18.100 -116.894 -55.082 1.00 51.58  ? 224  GLN   B CG     1 
ATOM   6586 C CD     . GLN   B  2 232 ? 16.817 -117.068 -54.321 1.00 69.96  ? 224  GLN   B CD     1 
ATOM   6587 O OE1    . GLN   B  2 232 ? 15.893 -116.250 -54.403 1.00 68.42  ? 224  GLN   B OE1    1 
ATOM   6588 N NE2    . GLN   B  2 232 ? 16.715 -118.168 -53.591 1.00 58.87  ? 224  GLN   B NE2    1 
ATOM   6589 N N      . SER   B  2 233 ? 21.878 -113.810 -55.778 1.00 47.66  ? 225  SER   B N      1 
ATOM   6590 C CA     . SER   B  2 233 ? 22.727 -112.608 -55.727 1.00 47.77  ? 225  SER   B CA     1 
ATOM   6591 C C      . SER   B  2 233 ? 21.990 -111.261 -55.529 1.00 50.80  ? 225  SER   B C      1 
ATOM   6592 O O      . SER   B  2 233 ? 22.618 -110.288 -55.099 1.00 50.41  ? 225  SER   B O      1 
ATOM   6593 C CB     . SER   B  2 233 ? 23.615 -112.536 -56.968 1.00 52.59  ? 225  SER   B CB     1 
ATOM   6594 O OG     . SER   B  2 233 ? 24.847 -111.896 -56.670 1.00 63.43  ? 225  SER   B OG     1 
ATOM   6595 N N      . GLU   B  2 234 ? 20.685 -111.203 -55.842 1.00 46.44  ? 226  GLU   B N      1 
ATOM   6596 C CA     . GLU   B  2 234 ? 19.883 -109.987 -55.701 1.00 45.87  ? 226  GLU   B CA     1 
ATOM   6597 C C      . GLU   B  2 234 ? 18.895 -110.051 -54.520 1.00 47.24  ? 226  GLU   B C      1 
ATOM   6598 O O      . GLU   B  2 234 ? 18.171 -109.083 -54.274 1.00 46.21  ? 226  GLU   B O      1 
ATOM   6599 C CB     . GLU   B  2 234 ? 19.159 -109.673 -57.025 1.00 47.39  ? 226  GLU   B CB     1 
ATOM   6600 C CG     . GLU   B  2 234 ? 19.918 -108.705 -57.916 1.00 61.26  ? 226  GLU   B CG     1 
ATOM   6601 C CD     . GLU   B  2 234 ? 21.025 -109.300 -58.763 1.00 91.79  ? 226  GLU   B CD     1 
ATOM   6602 O OE1    . GLU   B  2 234 ? 20.720 -110.142 -59.639 1.00 96.35  ? 226  GLU   B OE1    1 
ATOM   6603 O OE2    . GLU   B  2 234 ? 22.193 -108.880 -58.590 1.00 88.91  ? 226  GLU   B OE2    1 
ATOM   6604 N N      . VAL   B  2 235 ? 18.882 -111.182 -53.785 1.00 42.18  ? 227  VAL   B N      1 
ATOM   6605 C CA     . VAL   B  2 235 ? 17.980 -111.417 -52.651 1.00 41.06  ? 227  VAL   B CA     1 
ATOM   6606 C C      . VAL   B  2 235 ? 18.696 -111.247 -51.287 1.00 41.83  ? 227  VAL   B C      1 
ATOM   6607 O O      . VAL   B  2 235 ? 19.860 -111.629 -51.130 1.00 40.42  ? 227  VAL   B O      1 
ATOM   6608 C CB     . VAL   B  2 235 ? 17.253 -112.790 -52.789 1.00 45.01  ? 227  VAL   B CB     1 
ATOM   6609 C CG1    . VAL   B  2 235 ? 16.421 -113.134 -51.555 1.00 44.77  ? 227  VAL   B CG1    1 
ATOM   6610 C CG2    . VAL   B  2 235 ? 16.383 -112.830 -54.043 1.00 44.93  ? 227  VAL   B CG2    1 
ATOM   6611 N N      . PHE   B  2 236 ? 17.980 -110.647 -50.317 1.00 36.79  ? 228  PHE   B N      1 
ATOM   6612 C CA     . PHE   B  2 236 ? 18.442 -110.444 -48.948 1.00 35.56  ? 228  PHE   B CA     1 
ATOM   6613 C C      . PHE   B  2 236 ? 17.287 -110.520 -47.956 1.00 37.21  ? 228  PHE   B C      1 
ATOM   6614 O O      . PHE   B  2 236 ? 16.121 -110.429 -48.345 1.00 36.78  ? 228  PHE   B O      1 
ATOM   6615 C CB     . PHE   B  2 236 ? 19.252 -109.137 -48.790 1.00 37.34  ? 228  PHE   B CB     1 
ATOM   6616 C CG     . PHE   B  2 236 ? 18.454 -107.851 -48.715 1.00 38.95  ? 228  PHE   B CG     1 
ATOM   6617 C CD1    . PHE   B  2 236 ? 18.190 -107.110 -49.859 1.00 41.79  ? 228  PHE   B CD1    1 
ATOM   6618 C CD2    . PHE   B  2 236 ? 18.009 -107.357 -47.488 1.00 40.45  ? 228  PHE   B CD2    1 
ATOM   6619 C CE1    . PHE   B  2 236 ? 17.457 -105.919 -49.786 1.00 42.86  ? 228  PHE   B CE1    1 
ATOM   6620 C CE2    . PHE   B  2 236 ? 17.267 -106.176 -47.417 1.00 43.20  ? 228  PHE   B CE2    1 
ATOM   6621 C CZ     . PHE   B  2 236 ? 17.009 -105.456 -48.563 1.00 41.71  ? 228  PHE   B CZ     1 
ATOM   6622 N N      . VAL   B  2 237 ? 17.622 -110.703 -46.671 1.00 31.97  ? 229  VAL   B N      1 
ATOM   6623 C CA     . VAL   B  2 237 ? 16.656 -110.724 -45.577 1.00 31.25  ? 229  VAL   B CA     1 
ATOM   6624 C C      . VAL   B  2 237 ? 17.000 -109.633 -44.562 1.00 34.15  ? 229  VAL   B C      1 
ATOM   6625 O O      . VAL   B  2 237 ? 18.166 -109.263 -44.419 1.00 32.50  ? 229  VAL   B O      1 
ATOM   6626 C CB     . VAL   B  2 237 ? 16.431 -112.112 -44.905 1.00 35.16  ? 229  VAL   B CB     1 
ATOM   6627 C CG1    . VAL   B  2 237 ? 15.780 -113.104 -45.865 1.00 34.90  ? 229  VAL   B CG1    1 
ATOM   6628 C CG2    . VAL   B  2 237 ? 17.718 -112.679 -44.296 1.00 34.89  ? 229  VAL   B CG2    1 
ATOM   6629 N N      . PHE   B  2 238 ? 15.976 -109.102 -43.888 1.00 31.54  ? 230  PHE   B N      1 
ATOM   6630 C CA     . PHE   B  2 238 ? 16.158 -108.103 -42.843 1.00 31.00  ? 230  PHE   B CA     1 
ATOM   6631 C C      . PHE   B  2 238 ? 15.233 -108.358 -41.661 1.00 32.32  ? 230  PHE   B C      1 
ATOM   6632 O O      . PHE   B  2 238 ? 14.077 -108.745 -41.831 1.00 31.21  ? 230  PHE   B O      1 
ATOM   6633 C CB     . PHE   B  2 238 ? 16.067 -106.652 -43.367 1.00 33.07  ? 230  PHE   B CB     1 
ATOM   6634 C CG     . PHE   B  2 238 ? 14.677 -106.077 -43.525 1.00 35.17  ? 230  PHE   B CG     1 
ATOM   6635 C CD1    . PHE   B  2 238 ? 13.970 -106.240 -44.710 1.00 38.41  ? 230  PHE   B CD1    1 
ATOM   6636 C CD2    . PHE   B  2 238 ? 14.092 -105.336 -42.503 1.00 37.88  ? 230  PHE   B CD2    1 
ATOM   6637 C CE1    . PHE   B  2 238 ? 12.691 -105.693 -44.862 1.00 39.56  ? 230  PHE   B CE1    1 
ATOM   6638 C CE2    . PHE   B  2 238 ? 12.808 -104.796 -42.654 1.00 40.68  ? 230  PHE   B CE2    1 
ATOM   6639 C CZ     . PHE   B  2 238 ? 12.113 -104.987 -43.829 1.00 38.42  ? 230  PHE   B CZ     1 
ATOM   6640 N N      . GLY   B  2 239 ? 15.772 -108.139 -40.477 1.00 28.03  ? 231  GLY   B N      1 
ATOM   6641 C CA     . GLY   B  2 239 ? 15.048 -108.266 -39.225 1.00 27.62  ? 231  GLY   B CA     1 
ATOM   6642 C C      . GLY   B  2 239 ? 14.757 -106.882 -38.683 1.00 30.02  ? 231  GLY   B C      1 
ATOM   6643 O O      . GLY   B  2 239 ? 15.487 -105.932 -38.991 1.00 27.88  ? 231  GLY   B O      1 
ATOM   6644 N N      . ASP   B  2 240 ? 13.682 -106.747 -37.900 1.00 27.24  ? 232  ASP   B N      1 
ATOM   6645 C CA     . ASP   B  2 240 ? 13.360 -105.444 -37.334 1.00 27.64  ? 232  ASP   B CA     1 
ATOM   6646 C C      . ASP   B  2 240 ? 13.279 -105.480 -35.803 1.00 31.66  ? 232  ASP   B C      1 
ATOM   6647 O O      . ASP   B  2 240 ? 13.285 -106.556 -35.198 1.00 31.33  ? 232  ASP   B O      1 
ATOM   6648 C CB     . ASP   B  2 240 ? 12.104 -104.819 -37.994 1.00 29.30  ? 232  ASP   B CB     1 
ATOM   6649 C CG     . ASP   B  2 240 ? 10.746 -105.427 -37.696 1.00 39.88  ? 232  ASP   B CG     1 
ATOM   6650 O OD1    . ASP   B  2 240 ? 10.640 -106.203 -36.731 1.00 42.43  ? 232  ASP   B OD1    1 
ATOM   6651 O OD2    . ASP   B  2 240 ? 9.768  -105.057 -38.382 1.00 45.72  ? 232  ASP   B OD2    1 
ATOM   6652 N N      . GLU   B  2 241 ? 13.213 -104.290 -35.186 1.00 28.11  ? 233  GLU   B N      1 
ATOM   6653 C CA     . GLU   B  2 241 ? 13.105 -104.080 -33.741 1.00 27.90  ? 233  GLU   B CA     1 
ATOM   6654 C C      . GLU   B  2 241 ? 11.849 -104.722 -33.137 1.00 32.31  ? 233  GLU   B C      1 
ATOM   6655 O O      . GLU   B  2 241 ? 11.830 -104.953 -31.935 1.00 32.75  ? 233  GLU   B O      1 
ATOM   6656 C CB     . GLU   B  2 241 ? 13.133 -102.574 -33.420 1.00 29.00  ? 233  GLU   B CB     1 
ATOM   6657 C CG     . GLU   B  2 241 ? 12.019 -101.782 -34.091 1.00 37.49  ? 233  GLU   B CG     1 
ATOM   6658 C CD     . GLU   B  2 241 ? 11.921 -100.320 -33.710 1.00 50.61  ? 233  GLU   B CD     1 
ATOM   6659 O OE1    . GLU   B  2 241 ? 12.703 -99.883  -32.835 1.00 38.41  ? 233  GLU   B OE1    1 
ATOM   6660 O OE2    . GLU   B  2 241 ? 11.073 -99.607  -34.296 1.00 40.93  ? 233  GLU   B OE2    1 
ATOM   6661 N N      . ASN   B  2 242 ? 10.814 -105.000 -33.960 1.00 28.69  ? 234  ASN   B N      1 
ATOM   6662 C CA     . ASN   B  2 242 ? 9.559  -105.604 -33.513 1.00 28.58  ? 234  ASN   B CA     1 
ATOM   6663 C C      . ASN   B  2 242 ? 9.531  -107.149 -33.605 1.00 34.05  ? 234  ASN   B C      1 
ATOM   6664 O O      . ASN   B  2 242 ? 8.493  -107.767 -33.348 1.00 34.24  ? 234  ASN   B O      1 
ATOM   6665 C CB     . ASN   B  2 242 ? 8.375  -104.976 -34.258 1.00 27.96  ? 234  ASN   B CB     1 
ATOM   6666 C CG     . ASN   B  2 242 ? 7.061  -105.084 -33.516 1.00 45.50  ? 234  ASN   B CG     1 
ATOM   6667 O OD1    . ASN   B  2 242 ? 6.963  -104.807 -32.313 1.00 43.05  ? 234  ASN   B OD1    1 
ATOM   6668 N ND2    . ASN   B  2 242 ? 6.023  -105.506 -34.214 1.00 34.48  ? 234  ASN   B ND2    1 
ATOM   6669 N N      . GLY   B  2 243 ? 10.667 -107.754 -33.952 1.00 31.39  ? 235  GLY   B N      1 
ATOM   6670 C CA     . GLY   B  2 243 ? 10.804 -109.205 -34.052 1.00 31.24  ? 235  GLY   B CA     1 
ATOM   6671 C C      . GLY   B  2 243 ? 10.358 -109.853 -35.348 1.00 35.22  ? 235  GLY   B C      1 
ATOM   6672 O O      . GLY   B  2 243 ? 10.230 -111.082 -35.410 1.00 34.29  ? 235  GLY   B O      1 
ATOM   6673 N N      . THR   B  2 244 ? 10.128 -109.043 -36.391 1.00 32.55  ? 236  THR   B N      1 
ATOM   6674 C CA     . THR   B  2 244 ? 9.698  -109.509 -37.710 1.00 32.65  ? 236  THR   B CA     1 
ATOM   6675 C C      . THR   B  2 244 ? 10.909 -109.714 -38.628 1.00 37.30  ? 236  THR   B C      1 
ATOM   6676 O O      . THR   B  2 244 ? 11.842 -108.907 -38.614 1.00 36.53  ? 236  THR   B O      1 
ATOM   6677 C CB     . THR   B  2 244 ? 8.627  -108.543 -38.283 1.00 39.73  ? 236  THR   B CB     1 
ATOM   6678 O OG1    . THR   B  2 244 ? 7.455  -108.631 -37.472 1.00 39.39  ? 236  THR   B OG1    1 
ATOM   6679 C CG2    . THR   B  2 244 ? 8.254  -108.835 -39.746 1.00 37.72  ? 236  THR   B CG2    1 
ATOM   6680 N N      . VAL   B  2 245 ? 10.884 -110.802 -39.416 1.00 35.21  ? 237  VAL   B N      1 
ATOM   6681 C CA     . VAL   B  2 245 ? 11.912 -111.126 -40.419 1.00 35.31  ? 237  VAL   B CA     1 
ATOM   6682 C C      . VAL   B  2 245 ? 11.240 -110.976 -41.792 1.00 38.72  ? 237  VAL   B C      1 
ATOM   6683 O O      . VAL   B  2 245 ? 10.119 -111.453 -41.974 1.00 37.69  ? 237  VAL   B O      1 
ATOM   6684 C CB     . VAL   B  2 245 ? 12.551 -112.530 -40.200 1.00 38.98  ? 237  VAL   B CB     1 
ATOM   6685 C CG1    . VAL   B  2 245 ? 13.555 -112.864 -41.304 1.00 38.91  ? 237  VAL   B CG1    1 
ATOM   6686 C CG2    . VAL   B  2 245 ? 13.224 -112.618 -38.831 1.00 38.36  ? 237  VAL   B CG2    1 
ATOM   6687 N N      . SER   B  2 246 ? 11.891 -110.266 -42.728 1.00 35.99  ? 238  SER   B N      1 
ATOM   6688 C CA     . SER   B  2 246 ? 11.341 -110.023 -44.064 1.00 36.10  ? 238  SER   B CA     1 
ATOM   6689 C C      . SER   B  2 246 ? 12.315 -110.385 -45.180 1.00 40.43  ? 238  SER   B C      1 
ATOM   6690 O O      . SER   B  2 246 ? 13.511 -110.121 -45.057 1.00 38.47  ? 238  SER   B O      1 
ATOM   6691 C CB     . SER   B  2 246 ? 10.910 -108.565 -44.214 1.00 39.62  ? 238  SER   B CB     1 
ATOM   6692 O OG     . SER   B  2 246 ? 10.098 -108.120 -43.138 1.00 48.07  ? 238  SER   B OG     1 
ATOM   6693 N N      . LEU   B  2 247 ? 11.784 -110.950 -46.284 1.00 39.66  ? 239  LEU   B N      1 
ATOM   6694 C CA     . LEU   B  2 247 ? 12.529 -111.349 -47.484 1.00 40.44  ? 239  LEU   B CA     1 
ATOM   6695 C C      . LEU   B  2 247 ? 12.329 -110.292 -48.575 1.00 45.30  ? 239  LEU   B C      1 
ATOM   6696 O O      . LEU   B  2 247 ? 11.187 -109.962 -48.898 1.00 44.35  ? 239  LEU   B O      1 
ATOM   6697 C CB     . LEU   B  2 247 ? 12.065 -112.744 -47.963 1.00 40.93  ? 239  LEU   B CB     1 
ATOM   6698 C CG     . LEU   B  2 247 ? 12.735 -113.307 -49.234 1.00 45.88  ? 239  LEU   B CG     1 
ATOM   6699 C CD1    . LEU   B  2 247 ? 13.883 -114.227 -48.883 1.00 46.34  ? 239  LEU   B CD1    1 
ATOM   6700 C CD2    . LEU   B  2 247 ? 11.734 -114.055 -50.084 1.00 47.52  ? 239  LEU   B CD2    1 
ATOM   6701 N N      . VAL   B  2 248 ? 13.445 -109.745 -49.116 1.00 44.27  ? 240  VAL   B N      1 
ATOM   6702 C CA     . VAL   B  2 248 ? 13.450 -108.675 -50.133 1.00 46.02  ? 240  VAL   B CA     1 
ATOM   6703 C C      . VAL   B  2 248 ? 14.299 -109.038 -51.367 1.00 54.57  ? 240  VAL   B C      1 
ATOM   6704 O O      . VAL   B  2 248 ? 15.386 -109.606 -51.229 1.00 53.47  ? 240  VAL   B O      1 
ATOM   6705 C CB     . VAL   B  2 248 ? 13.924 -107.306 -49.540 1.00 50.01  ? 240  VAL   B CB     1 
ATOM   6706 C CG1    . VAL   B  2 248 ? 13.754 -106.160 -50.537 1.00 49.95  ? 240  VAL   B CG1    1 
ATOM   6707 C CG2    . VAL   B  2 248 ? 13.209 -106.973 -48.239 1.00 49.80  ? 240  VAL   B CG2    1 
ATOM   6708 N N      . ASP   B  2 249 ? 13.809 -108.648 -52.562 1.00 55.55  ? 241  ASP   B N      1 
ATOM   6709 C CA     . ASP   B  2 249 ? 14.498 -108.771 -53.850 1.00 57.49  ? 241  ASP   B CA     1 
ATOM   6710 C C      . ASP   B  2 249 ? 14.813 -107.337 -54.294 1.00 64.99  ? 241  ASP   B C      1 
ATOM   6711 O O      . ASP   B  2 249 ? 13.887 -106.569 -54.569 1.00 65.07  ? 241  ASP   B O      1 
ATOM   6712 C CB     . ASP   B  2 249 ? 13.618 -109.498 -54.888 1.00 59.83  ? 241  ASP   B CB     1 
ATOM   6713 C CG     . ASP   B  2 249 ? 14.347 -109.863 -56.173 1.00 75.60  ? 241  ASP   B CG     1 
ATOM   6714 O OD1    . ASP   B  2 249 ? 14.583 -108.954 -57.005 1.00 77.00  ? 241  ASP   B OD1    1 
ATOM   6715 O OD2    . ASP   B  2 249 ? 14.650 -111.061 -56.363 1.00 82.54  ? 241  ASP   B OD2    1 
ATOM   6716 N N      . THR   B  2 250 ? 16.114 -106.969 -54.309 1.00 64.19  ? 242  THR   B N      1 
ATOM   6717 C CA     . THR   B  2 250 ? 16.640 -105.635 -54.652 1.00 65.46  ? 242  THR   B CA     1 
ATOM   6718 C C      . THR   B  2 250 ? 16.110 -105.041 -55.962 1.00 73.85  ? 242  THR   B C      1 
ATOM   6719 O O      . THR   B  2 250 ? 15.872 -103.831 -56.022 1.00 73.65  ? 242  THR   B O      1 
ATOM   6720 C CB     . THR   B  2 250 ? 18.174 -105.627 -54.662 1.00 72.37  ? 242  THR   B CB     1 
ATOM   6721 O OG1    . THR   B  2 250 ? 18.656 -106.699 -55.474 1.00 68.80  ? 242  THR   B OG1    1 
ATOM   6722 C CG2    . THR   B  2 250 ? 18.775 -105.693 -53.265 1.00 71.63  ? 242  THR   B CG2    1 
ATOM   6723 N N      . LYS   B  2 251 ? 15.946 -105.880 -57.005 1.00 73.72  ? 243  LYS   B N      1 
ATOM   6724 C CA     . LYS   B  2 251 ? 15.452 -105.463 -58.322 1.00 75.03  ? 243  LYS   B CA     1 
ATOM   6725 C C      . LYS   B  2 251 ? 13.971 -105.083 -58.282 1.00 82.75  ? 243  LYS   B C      1 
ATOM   6726 O O      . LYS   B  2 251 ? 13.589 -104.069 -58.871 1.00 82.69  ? 243  LYS   B O      1 
ATOM   6727 C CB     . LYS   B  2 251 ? 15.716 -106.547 -59.389 1.00 77.18  ? 243  LYS   B CB     1 
ATOM   6728 C CG     . LYS   B  2 251 ? 17.198 -106.817 -59.670 1.00 86.42  ? 243  LYS   B CG     1 
ATOM   6729 C CD     . LYS   B  2 251 ? 17.861 -105.730 -60.518 1.00 93.33  ? 243  LYS   B CD     1 
ATOM   6730 C CE     . LYS   B  2 251 ? 19.362 -105.873 -60.543 1.00 98.85  ? 243  LYS   B CE     1 
ATOM   6731 N NZ     . LYS   B  2 251 ? 20.003 -104.792 -61.335 1.00 105.08 ? 243  LYS   B NZ     1 
ATOM   6732 N N      . SER   B  2 252 ? 13.149 -105.883 -57.571 1.00 81.77  ? 244  SER   B N      1 
ATOM   6733 C CA     . SER   B  2 252 ? 11.708 -105.658 -57.426 1.00 82.75  ? 244  SER   B CA     1 
ATOM   6734 C C      . SER   B  2 252 ? 11.373 -104.566 -56.401 1.00 89.12  ? 244  SER   B C      1 
ATOM   6735 O O      . SER   B  2 252 ? 10.384 -103.851 -56.588 1.00 89.08  ? 244  SER   B O      1 
ATOM   6736 C CB     . SER   B  2 252 ? 10.995 -106.960 -57.072 1.00 86.49  ? 244  SER   B CB     1 
ATOM   6737 O OG     . SER   B  2 252 ? 11.160 -107.930 -58.093 1.00 95.03  ? 244  SER   B OG     1 
ATOM   6738 N N      . THR   B  2 253 ? 12.197 -104.445 -55.325 1.00 87.06  ? 245  THR   B N      1 
ATOM   6739 C CA     . THR   B  2 253 ? 12.076 -103.485 -54.210 1.00 87.38  ? 245  THR   B CA     1 
ATOM   6740 C C      . THR   B  2 253 ? 10.678 -103.628 -53.537 1.00 91.86  ? 245  THR   B C      1 
ATOM   6741 O O      . THR   B  2 253 ? 9.876  -102.685 -53.518 1.00 91.61  ? 245  THR   B O      1 
ATOM   6742 C CB     . THR   B  2 253 ? 12.466 -102.044 -54.658 1.00 96.69  ? 245  THR   B CB     1 
ATOM   6743 O OG1    . THR   B  2 253 ? 13.670 -102.098 -55.429 1.00 97.17  ? 245  THR   B OG1    1 
ATOM   6744 C CG2    . THR   B  2 253 ? 12.661 -101.083 -53.482 1.00 94.85  ? 245  THR   B CG2    1 
ATOM   6745 N N      . SER   B  2 254 ? 10.393 -104.845 -53.021 1.00 88.49  ? 246  SER   B N      1 
ATOM   6746 C CA     . SER   B  2 254 ? 9.137  -105.199 -52.341 1.00 88.13  ? 246  SER   B CA     1 
ATOM   6747 C C      . SER   B  2 254 ? 9.344  -106.368 -51.366 1.00 90.59  ? 246  SER   B C      1 
ATOM   6748 O O      . SER   B  2 254 ? 9.878  -107.411 -51.761 1.00 90.24  ? 246  SER   B O      1 
ATOM   6749 C CB     . SER   B  2 254 ? 8.044  -105.550 -53.354 1.00 91.98  ? 246  SER   B CB     1 
ATOM   6750 O OG     . SER   B  2 254 ? 7.599  -104.416 -54.081 1.00 101.29 ? 246  SER   B OG     1 
ATOM   6751 N N      . CYS   B  2 255 ? 8.930  -106.182 -50.094 1.00 85.61  ? 247  CYS   B N      1 
ATOM   6752 C CA     . CYS   B  2 255 ? 9.025  -107.210 -49.052 1.00 84.66  ? 247  CYS   B CA     1 
ATOM   6753 C C      . CYS   B  2 255 ? 7.675  -107.911 -48.851 1.00 84.80  ? 247  CYS   B C      1 
ATOM   6754 O O      . CYS   B  2 255 ? 7.054  -107.818 -47.784 1.00 84.44  ? 247  CYS   B O      1 
ATOM   6755 C CB     . CYS   B  2 255 ? 9.606  -106.665 -47.745 1.00 85.41  ? 247  CYS   B CB     1 
ATOM   6756 S SG     . CYS   B  2 255 ? 8.965  -105.044 -47.241 1.00 89.56  ? 247  CYS   B SG     1 
ATOM   6757 N N      . VAL   B  2 256 ? 7.231  -108.620 -49.909 1.00 78.02  ? 248  VAL   B N      1 
ATOM   6758 C CA     . VAL   B  2 256 ? 5.966  -109.357 -49.957 1.00 76.28  ? 248  VAL   B CA     1 
ATOM   6759 C C      . VAL   B  2 256 ? 5.974  -110.577 -48.993 1.00 75.35  ? 248  VAL   B C      1 
ATOM   6760 O O      . VAL   B  2 256 ? 4.898  -111.015 -48.571 1.00 75.32  ? 248  VAL   B O      1 
ATOM   6761 C CB     . VAL   B  2 256 ? 5.560  -109.718 -51.420 1.00 80.38  ? 248  VAL   B CB     1 
ATOM   6762 C CG1    . VAL   B  2 256 ? 6.368  -110.887 -51.986 1.00 80.27  ? 248  VAL   B CG1    1 
ATOM   6763 C CG2    . VAL   B  2 256 ? 4.057  -109.957 -51.551 1.00 80.15  ? 248  VAL   B CG2    1 
ATOM   6764 N N      . LEU   B  2 257 ? 7.173  -111.094 -48.628 1.00 67.03  ? 249  LEU   B N      1 
ATOM   6765 C CA     . LEU   B  2 257 ? 7.285  -112.215 -47.693 1.00 64.38  ? 249  LEU   B CA     1 
ATOM   6766 C C      . LEU   B  2 257 ? 7.873  -111.773 -46.346 1.00 62.43  ? 249  LEU   B C      1 
ATOM   6767 O O      . LEU   B  2 257 ? 9.007  -111.293 -46.288 1.00 61.40  ? 249  LEU   B O      1 
ATOM   6768 C CB     . LEU   B  2 257 ? 8.067  -113.393 -48.301 1.00 64.34  ? 249  LEU   B CB     1 
ATOM   6769 C CG     . LEU   B  2 257 ? 7.825  -114.766 -47.660 1.00 68.91  ? 249  LEU   B CG     1 
ATOM   6770 C CD1    . LEU   B  2 257 ? 6.506  -115.372 -48.114 1.00 71.54  ? 249  LEU   B CD1    1 
ATOM   6771 C CD2    . LEU   B  2 257 ? 8.951  -115.710 -47.971 1.00 69.07  ? 249  LEU   B CD2    1 
ATOM   6772 N N      . SER   B  2 258 ? 7.074  -111.910 -45.271 1.00 55.11  ? 250  SER   B N      1 
ATOM   6773 C CA     . SER   B  2 258 ? 7.459  -111.545 -43.904 1.00 53.29  ? 250  SER   B CA     1 
ATOM   6774 C C      . SER   B  2 258 ? 6.806  -112.460 -42.867 1.00 53.54  ? 250  SER   B C      1 
ATOM   6775 O O      . SER   B  2 258 ? 5.765  -113.061 -43.145 1.00 53.18  ? 250  SER   B O      1 
ATOM   6776 C CB     . SER   B  2 258 ? 7.138  -110.079 -43.611 1.00 56.25  ? 250  SER   B CB     1 
ATOM   6777 O OG     . SER   B  2 258 ? 5.745  -109.814 -43.628 1.00 65.45  ? 250  SER   B OG     1 
ATOM   6778 N N      . SER   B  2 259 ? 7.424  -112.571 -41.675 1.00 47.20  ? 251  SER   B N      1 
ATOM   6779 C CA     . SER   B  2 259 ? 6.912  -113.399 -40.584 1.00 45.93  ? 251  SER   B CA     1 
ATOM   6780 C C      . SER   B  2 259 ? 7.252  -112.841 -39.200 1.00 46.46  ? 251  SER   B C      1 
ATOM   6781 O O      . SER   B  2 259 ? 8.374  -112.378 -38.971 1.00 45.33  ? 251  SER   B O      1 
ATOM   6782 C CB     . SER   B  2 259 ? 7.424  -114.832 -40.709 1.00 49.81  ? 251  SER   B CB     1 
ATOM   6783 O OG     . SER   B  2 259 ? 6.822  -115.690 -39.751 1.00 58.91  ? 251  SER   B OG     1 
ATOM   6784 N N      . ALA   B  2 260 ? 6.286  -112.922 -38.272 1.00 41.72  ? 252  ALA   B N      1 
ATOM   6785 C CA     . ALA   B  2 260 ? 6.468  -112.511 -36.883 1.00 40.94  ? 252  ALA   B CA     1 
ATOM   6786 C C      . ALA   B  2 260 ? 7.130  -113.694 -36.168 1.00 43.57  ? 252  ALA   B C      1 
ATOM   6787 O O      . ALA   B  2 260 ? 6.450  -114.587 -35.654 1.00 44.58  ? 252  ALA   B O      1 
ATOM   6788 C CB     . ALA   B  2 260 ? 5.127  -112.166 -36.246 1.00 41.53  ? 252  ALA   B CB     1 
ATOM   6789 N N      . VAL   B  2 261 ? 8.471  -113.719 -36.200 1.00 37.41  ? 253  VAL   B N      1 
ATOM   6790 C CA     . VAL   B  2 261 ? 9.299  -114.789 -35.639 1.00 36.05  ? 253  VAL   B CA     1 
ATOM   6791 C C      . VAL   B  2 261 ? 9.576  -114.599 -34.147 1.00 39.45  ? 253  VAL   B C      1 
ATOM   6792 O O      . VAL   B  2 261 ? 9.433  -115.550 -33.374 1.00 39.82  ? 253  VAL   B O      1 
ATOM   6793 C CB     . VAL   B  2 261 ? 10.621 -114.979 -36.444 1.00 38.91  ? 253  VAL   B CB     1 
ATOM   6794 C CG1    . VAL   B  2 261 ? 11.383 -116.213 -35.976 1.00 38.26  ? 253  VAL   B CG1    1 
ATOM   6795 C CG2    . VAL   B  2 261 ? 10.356 -115.055 -37.945 1.00 38.59  ? 253  VAL   B CG2    1 
ATOM   6796 N N      . HIS   B  2 262 ? 10.001 -113.387 -33.749 1.00 34.14  ? 254  HIS   B N      1 
ATOM   6797 C CA     . HIS   B  2 262 ? 10.381 -113.093 -32.371 1.00 33.30  ? 254  HIS   B CA     1 
ATOM   6798 C C      . HIS   B  2 262 ? 9.471  -112.090 -31.669 1.00 38.88  ? 254  HIS   B C      1 
ATOM   6799 O O      . HIS   B  2 262 ? 8.801  -111.291 -32.327 1.00 38.85  ? 254  HIS   B O      1 
ATOM   6800 C CB     . HIS   B  2 262 ? 11.841 -112.629 -32.330 1.00 33.30  ? 254  HIS   B CB     1 
ATOM   6801 C CG     . HIS   B  2 262 ? 12.817 -113.678 -32.766 1.00 36.28  ? 254  HIS   B CG     1 
ATOM   6802 N ND1    . HIS   B  2 262 ? 13.116 -114.766 -31.963 1.00 37.74  ? 254  HIS   B ND1    1 
ATOM   6803 C CD2    . HIS   B  2 262 ? 13.559 -113.753 -33.896 1.00 37.68  ? 254  HIS   B CD2    1 
ATOM   6804 C CE1    . HIS   B  2 262 ? 14.011 -115.473 -32.635 1.00 37.05  ? 254  HIS   B CE1    1 
ATOM   6805 N NE2    . HIS   B  2 262 ? 14.314 -114.900 -33.800 1.00 37.30  ? 254  HIS   B NE2    1 
ATOM   6806 N N      . SER   B  2 263 ? 9.437  -112.149 -30.322 1.00 36.35  ? 255  SER   B N      1 
ATOM   6807 C CA     . SER   B  2 263 ? 8.643  -111.228 -29.515 1.00 36.44  ? 255  SER   B CA     1 
ATOM   6808 C C      . SER   B  2 263 ? 9.433  -109.945 -29.269 1.00 42.74  ? 255  SER   B C      1 
ATOM   6809 O O      . SER   B  2 263 ? 8.867  -108.986 -28.754 1.00 44.28  ? 255  SER   B O      1 
ATOM   6810 C CB     . SER   B  2 263 ? 8.218  -111.870 -28.196 1.00 39.38  ? 255  SER   B CB     1 
ATOM   6811 O OG     . SER   B  2 263 ? 9.323  -112.145 -27.351 1.00 46.95  ? 255  SER   B OG     1 
ATOM   6812 N N      . GLN   B  2 264 ? 10.740 -109.932 -29.627 1.00 37.91  ? 256  GLN   B N      1 
ATOM   6813 C CA     . GLN   B  2 264 ? 11.643 -108.786 -29.486 1.00 36.86  ? 256  GLN   B CA     1 
ATOM   6814 C C      . GLN   B  2 264 ? 12.588 -108.651 -30.682 1.00 39.83  ? 256  GLN   B C      1 
ATOM   6815 O O      . GLN   B  2 264 ? 12.581 -109.508 -31.563 1.00 39.09  ? 256  GLN   B O      1 
ATOM   6816 C CB     . GLN   B  2 264 ? 12.431 -108.864 -28.174 1.00 38.16  ? 256  GLN   B CB     1 
ATOM   6817 C CG     . GLN   B  2 264 ? 11.638 -108.371 -26.973 1.00 54.58  ? 256  GLN   B CG     1 
ATOM   6818 C CD     . GLN   B  2 264 ? 12.505 -108.275 -25.761 1.00 74.62  ? 256  GLN   B CD     1 
ATOM   6819 O OE1    . GLN   B  2 264 ? 13.037 -107.210 -25.433 1.00 71.40  ? 256  GLN   B OE1    1 
ATOM   6820 N NE2    . GLN   B  2 264 ? 12.688 -109.396 -25.087 1.00 68.67  ? 256  GLN   B NE2    1 
ATOM   6821 N N      . CYS   B  2 265 ? 13.409 -107.578 -30.693 1.00 35.69  ? 257  CYS   B N      1 
ATOM   6822 C CA     . CYS   B  2 265 ? 14.405 -107.211 -31.703 1.00 35.53  ? 257  CYS   B CA     1 
ATOM   6823 C C      . CYS   B  2 265 ? 15.148 -108.403 -32.324 1.00 36.36  ? 257  CYS   B C      1 
ATOM   6824 O O      . CYS   B  2 265 ? 15.685 -109.239 -31.588 1.00 34.58  ? 257  CYS   B O      1 
ATOM   6825 C CB     . CYS   B  2 265 ? 15.386 -106.198 -31.116 1.00 37.19  ? 257  CYS   B CB     1 
ATOM   6826 S SG     . CYS   B  2 265 ? 16.810 -105.836 -32.179 1.00 42.27  ? 257  CYS   B SG     1 
ATOM   6827 N N      . VAL   B  2 266 ? 15.195 -108.464 -33.676 1.00 30.89  ? 258  VAL   B N      1 
ATOM   6828 C CA     . VAL   B  2 266 ? 15.947 -109.505 -34.391 1.00 29.83  ? 258  VAL   B CA     1 
ATOM   6829 C C      . VAL   B  2 266 ? 17.393 -108.996 -34.442 1.00 32.68  ? 258  VAL   B C      1 
ATOM   6830 O O      . VAL   B  2 266 ? 17.695 -108.039 -35.158 1.00 31.96  ? 258  VAL   B O      1 
ATOM   6831 C CB     . VAL   B  2 266 ? 15.381 -109.850 -35.796 1.00 33.55  ? 258  VAL   B CB     1 
ATOM   6832 C CG1    . VAL   B  2 266 ? 16.228 -110.933 -36.483 1.00 33.28  ? 258  VAL   B CG1    1 
ATOM   6833 C CG2    . VAL   B  2 266 ? 13.925 -110.288 -35.713 1.00 32.91  ? 258  VAL   B CG2    1 
ATOM   6834 N N      . THR   B  2 267 ? 18.261 -109.610 -33.636 1.00 28.66  ? 259  THR   B N      1 
ATOM   6835 C CA     . THR   B  2 267 ? 19.667 -109.238 -33.481 1.00 28.56  ? 259  THR   B CA     1 
ATOM   6836 C C      . THR   B  2 267 ? 20.526 -109.690 -34.660 1.00 31.45  ? 259  THR   B C      1 
ATOM   6837 O O      . THR   B  2 267 ? 21.373 -108.926 -35.122 1.00 31.56  ? 259  THR   B O      1 
ATOM   6838 C CB     . THR   B  2 267 ? 20.176 -109.746 -32.116 1.00 34.70  ? 259  THR   B CB     1 
ATOM   6839 O OG1    . THR   B  2 267 ? 19.395 -109.109 -31.107 1.00 39.08  ? 259  THR   B OG1    1 
ATOM   6840 C CG2    . THR   B  2 267 ? 21.661 -109.447 -31.870 1.00 31.26  ? 259  THR   B CG2    1 
ATOM   6841 N N      . GLY   B  2 268 ? 20.326 -110.919 -35.115 1.00 27.58  ? 260  GLY   B N      1 
ATOM   6842 C CA     . GLY   B  2 268 ? 21.112 -111.465 -36.213 1.00 26.45  ? 260  GLY   B CA     1 
ATOM   6843 C C      . GLY   B  2 268 ? 20.359 -112.432 -37.093 1.00 29.48  ? 260  GLY   B C      1 
ATOM   6844 O O      . GLY   B  2 268 ? 19.367 -113.039 -36.674 1.00 27.74  ? 260  GLY   B O      1 
ATOM   6845 N N      . LEU   B  2 269 ? 20.837 -112.559 -38.333 1.00 27.31  ? 261  LEU   B N      1 
ATOM   6846 C CA     . LEU   B  2 269 ? 20.274 -113.430 -39.358 1.00 27.58  ? 261  LEU   B CA     1 
ATOM   6847 C C      . LEU   B  2 269 ? 21.436 -114.113 -40.064 1.00 31.90  ? 261  LEU   B C      1 
ATOM   6848 O O      . LEU   B  2 269 ? 22.318 -113.428 -40.597 1.00 30.71  ? 261  LEU   B O      1 
ATOM   6849 C CB     . LEU   B  2 269 ? 19.447 -112.609 -40.356 1.00 27.66  ? 261  LEU   B CB     1 
ATOM   6850 C CG     . LEU   B  2 269 ? 18.113 -112.050 -39.870 1.00 31.59  ? 261  LEU   B CG     1 
ATOM   6851 C CD1    . LEU   B  2 269 ? 17.614 -110.991 -40.824 1.00 31.02  ? 261  LEU   B CD1    1 
ATOM   6852 C CD2    . LEU   B  2 269 ? 17.075 -113.156 -39.702 1.00 32.59  ? 261  LEU   B CD2    1 
ATOM   6853 N N      . VAL   B  2 270 ? 21.490 -115.458 -39.984 1.00 29.35  ? 262  VAL   B N      1 
ATOM   6854 C CA     . VAL   B  2 270 ? 22.590 -116.241 -40.557 1.00 29.55  ? 262  VAL   B CA     1 
ATOM   6855 C C      . VAL   B  2 270 ? 22.069 -117.401 -41.414 1.00 33.74  ? 262  VAL   B C      1 
ATOM   6856 O O      . VAL   B  2 270 ? 21.352 -118.283 -40.918 1.00 33.05  ? 262  VAL   B O      1 
ATOM   6857 C CB     . VAL   B  2 270 ? 23.630 -116.719 -39.493 1.00 33.65  ? 262  VAL   B CB     1 
ATOM   6858 C CG1    . VAL   B  2 270 ? 24.902 -117.249 -40.164 1.00 33.54  ? 262  VAL   B CG1    1 
ATOM   6859 C CG2    . VAL   B  2 270 ? 23.980 -115.607 -38.493 1.00 33.44  ? 262  VAL   B CG2    1 
ATOM   6860 N N      . PHE   B  2 271 ? 22.434 -117.397 -42.708 1.00 30.55  ? 263  PHE   B N      1 
ATOM   6861 C CA     . PHE   B  2 271 ? 22.035 -118.475 -43.618 1.00 29.64  ? 263  PHE   B CA     1 
ATOM   6862 C C      . PHE   B  2 271 ? 22.946 -119.686 -43.434 1.00 33.60  ? 263  PHE   B C      1 
ATOM   6863 O O      . PHE   B  2 271 ? 24.141 -119.512 -43.207 1.00 31.30  ? 263  PHE   B O      1 
ATOM   6864 C CB     . PHE   B  2 271 ? 22.056 -118.003 -45.074 1.00 30.54  ? 263  PHE   B CB     1 
ATOM   6865 C CG     . PHE   B  2 271 ? 20.843 -117.216 -45.500 1.00 30.56  ? 263  PHE   B CG     1 
ATOM   6866 C CD1    . PHE   B  2 271 ? 19.643 -117.858 -45.790 1.00 32.61  ? 263  PHE   B CD1    1 
ATOM   6867 C CD2    . PHE   B  2 271 ? 20.908 -115.836 -45.649 1.00 31.68  ? 263  PHE   B CD2    1 
ATOM   6868 C CE1    . PHE   B  2 271 ? 18.525 -117.128 -46.208 1.00 33.41  ? 263  PHE   B CE1    1 
ATOM   6869 C CE2    . PHE   B  2 271 ? 19.799 -115.109 -46.087 1.00 33.80  ? 263  PHE   B CE2    1 
ATOM   6870 C CZ     . PHE   B  2 271 ? 18.611 -115.757 -46.354 1.00 31.93  ? 263  PHE   B CZ     1 
ATOM   6871 N N      . SER   B  2 272 ? 22.369 -120.902 -43.507 1.00 33.36  ? 264  SER   B N      1 
ATOM   6872 C CA     . SER   B  2 272 ? 23.063 -122.192 -43.394 1.00 34.90  ? 264  SER   B CA     1 
ATOM   6873 C C      . SER   B  2 272 ? 23.935 -122.481 -44.647 1.00 42.93  ? 264  SER   B C      1 
ATOM   6874 O O      . SER   B  2 272 ? 23.676 -121.880 -45.696 1.00 42.21  ? 264  SER   B O      1 
ATOM   6875 C CB     . SER   B  2 272 ? 22.051 -123.314 -43.177 1.00 38.53  ? 264  SER   B CB     1 
ATOM   6876 O OG     . SER   B  2 272 ? 21.432 -123.708 -44.388 1.00 47.79  ? 264  SER   B OG     1 
ATOM   6877 N N      . PRO   B  2 273 ? 24.943 -123.399 -44.590 1.00 42.14  ? 265  PRO   B N      1 
ATOM   6878 C CA     . PRO   B  2 273 ? 25.795 -123.627 -45.774 1.00 42.66  ? 265  PRO   B CA     1 
ATOM   6879 C C      . PRO   B  2 273 ? 25.227 -124.581 -46.839 1.00 48.31  ? 265  PRO   B C      1 
ATOM   6880 O O      . PRO   B  2 273 ? 25.905 -124.833 -47.840 1.00 47.83  ? 265  PRO   B O      1 
ATOM   6881 C CB     . PRO   B  2 273 ? 27.115 -124.150 -45.169 1.00 44.38  ? 265  PRO   B CB     1 
ATOM   6882 C CG     . PRO   B  2 273 ? 26.893 -124.240 -43.669 1.00 48.38  ? 265  PRO   B CG     1 
ATOM   6883 C CD     . PRO   B  2 273 ? 25.418 -124.213 -43.455 1.00 43.62  ? 265  PRO   B CD     1 
ATOM   6884 N N      . HIS   B  2 274 ? 23.985 -125.082 -46.644 1.00 46.26  ? 266  HIS   B N      1 
ATOM   6885 C CA     . HIS   B  2 274 ? 23.281 -126.005 -47.548 1.00 46.97  ? 266  HIS   B CA     1 
ATOM   6886 C C      . HIS   B  2 274 ? 22.986 -125.403 -48.923 1.00 52.42  ? 266  HIS   B C      1 
ATOM   6887 O O      . HIS   B  2 274 ? 22.888 -124.178 -49.048 1.00 52.14  ? 266  HIS   B O      1 
ATOM   6888 C CB     . HIS   B  2 274 ? 21.946 -126.443 -46.927 1.00 47.98  ? 266  HIS   B CB     1 
ATOM   6889 C CG     . HIS   B  2 274 ? 22.066 -127.126 -45.607 1.00 51.59  ? 266  HIS   B CG     1 
ATOM   6890 N ND1    . HIS   B  2 274 ? 22.231 -126.409 -44.440 1.00 53.41  ? 266  HIS   B ND1    1 
ATOM   6891 C CD2    . HIS   B  2 274 ? 21.999 -128.443 -45.306 1.00 53.53  ? 266  HIS   B CD2    1 
ATOM   6892 C CE1    . HIS   B  2 274 ? 22.268 -127.305 -43.472 1.00 52.91  ? 266  HIS   B CE1    1 
ATOM   6893 N NE2    . HIS   B  2 274 ? 22.133 -128.543 -43.945 1.00 53.38  ? 266  HIS   B NE2    1 
ATOM   6894 N N      . SER   B  2 275 ? 22.784 -126.280 -49.944 1.00 49.80  ? 267  SER   B N      1 
ATOM   6895 C CA     . SER   B  2 275 ? 22.420 -125.904 -51.317 1.00 49.68  ? 267  SER   B CA     1 
ATOM   6896 C C      . SER   B  2 275 ? 21.090 -125.142 -51.290 1.00 52.50  ? 267  SER   B C      1 
ATOM   6897 O O      . SER   B  2 275 ? 20.950 -124.140 -51.985 1.00 52.47  ? 267  SER   B O      1 
ATOM   6898 C CB     . SER   B  2 275 ? 22.299 -127.143 -52.202 1.00 54.44  ? 267  SER   B CB     1 
ATOM   6899 O OG     . SER   B  2 275 ? 23.536 -127.829 -52.290 1.00 66.18  ? 267  SER   B OG     1 
ATOM   6900 N N      . VAL   B  2 276 ? 20.125 -125.629 -50.485 1.00 47.71  ? 268  VAL   B N      1 
ATOM   6901 C CA     . VAL   B  2 276 ? 18.831 -124.999 -50.221 1.00 47.45  ? 268  VAL   B CA     1 
ATOM   6902 C C      . VAL   B  2 276 ? 18.997 -124.543 -48.749 1.00 49.68  ? 268  VAL   B C      1 
ATOM   6903 O O      . VAL   B  2 276 ? 18.895 -125.372 -47.833 1.00 49.52  ? 268  VAL   B O      1 
ATOM   6904 C CB     . VAL   B  2 276 ? 17.633 -125.961 -50.446 1.00 52.05  ? 268  VAL   B CB     1 
ATOM   6905 C CG1    . VAL   B  2 276 ? 16.306 -125.276 -50.111 1.00 52.11  ? 268  VAL   B CG1    1 
ATOM   6906 C CG2    . VAL   B  2 276 ? 17.615 -126.483 -51.881 1.00 51.97  ? 268  VAL   B CG2    1 
ATOM   6907 N N      . PRO   B  2 277 ? 19.417 -123.274 -48.517 1.00 44.04  ? 269  PRO   B N      1 
ATOM   6908 C CA     . PRO   B  2 277 ? 19.745 -122.857 -47.147 1.00 43.25  ? 269  PRO   B CA     1 
ATOM   6909 C C      . PRO   B  2 277 ? 18.581 -122.625 -46.202 1.00 45.03  ? 269  PRO   B C      1 
ATOM   6910 O O      . PRO   B  2 277 ? 17.466 -122.278 -46.603 1.00 44.33  ? 269  PRO   B O      1 
ATOM   6911 C CB     . PRO   B  2 277 ? 20.553 -121.576 -47.349 1.00 45.09  ? 269  PRO   B CB     1 
ATOM   6912 C CG     . PRO   B  2 277 ? 20.013 -121.004 -48.607 1.00 49.97  ? 269  PRO   B CG     1 
ATOM   6913 C CD     . PRO   B  2 277 ? 19.672 -122.184 -49.481 1.00 45.35  ? 269  PRO   B CD     1 
ATOM   6914 N N      . PHE   B  2 278 ? 18.878 -122.842 -44.922 1.00 40.37  ? 270  PHE   B N      1 
ATOM   6915 C CA     . PHE   B  2 278 ? 18.009 -122.603 -43.775 1.00 39.68  ? 270  PHE   B CA     1 
ATOM   6916 C C      . PHE   B  2 278 ? 18.458 -121.255 -43.219 1.00 39.40  ? 270  PHE   B C      1 
ATOM   6917 O O      . PHE   B  2 278 ? 19.594 -120.837 -43.468 1.00 37.04  ? 270  PHE   B O      1 
ATOM   6918 C CB     . PHE   B  2 278 ? 18.192 -123.709 -42.725 1.00 42.07  ? 270  PHE   B CB     1 
ATOM   6919 C CG     . PHE   B  2 278 ? 17.827 -125.082 -43.234 1.00 44.57  ? 270  PHE   B CG     1 
ATOM   6920 C CD1    . PHE   B  2 278 ? 16.516 -125.535 -43.180 1.00 48.21  ? 270  PHE   B CD1    1 
ATOM   6921 C CD2    . PHE   B  2 278 ? 18.792 -125.914 -43.793 1.00 47.45  ? 270  PHE   B CD2    1 
ATOM   6922 C CE1    . PHE   B  2 278 ? 16.175 -126.798 -43.671 1.00 49.61  ? 270  PHE   B CE1    1 
ATOM   6923 C CE2    . PHE   B  2 278 ? 18.450 -127.173 -44.289 1.00 50.43  ? 270  PHE   B CE2    1 
ATOM   6924 C CZ     . PHE   B  2 278 ? 17.145 -127.609 -44.221 1.00 48.49  ? 270  PHE   B CZ     1 
ATOM   6925 N N      . LEU   B  2 279 ? 17.573 -120.562 -42.501 1.00 34.44  ? 271  LEU   B N      1 
ATOM   6926 C CA     . LEU   B  2 279 ? 17.913 -119.250 -41.967 1.00 33.01  ? 271  LEU   B CA     1 
ATOM   6927 C C      . LEU   B  2 279 ? 17.774 -119.204 -40.450 1.00 34.90  ? 271  LEU   B C      1 
ATOM   6928 O O      . LEU   B  2 279 ? 16.690 -119.437 -39.914 1.00 34.34  ? 271  LEU   B O      1 
ATOM   6929 C CB     . LEU   B  2 279 ? 17.077 -118.165 -42.669 1.00 32.66  ? 271  LEU   B CB     1 
ATOM   6930 C CG     . LEU   B  2 279 ? 17.230 -116.704 -42.208 1.00 36.68  ? 271  LEU   B CG     1 
ATOM   6931 C CD1    . LEU   B  2 279 ? 18.609 -116.123 -42.592 1.00 36.30  ? 271  LEU   B CD1    1 
ATOM   6932 C CD2    . LEU   B  2 279 ? 16.108 -115.859 -42.781 1.00 36.25  ? 271  LEU   B CD2    1 
ATOM   6933 N N      . ALA   B  2 280 ? 18.888 -118.950 -39.766 1.00 30.29  ? 272  ALA   B N      1 
ATOM   6934 C CA     . ALA   B  2 280 ? 18.899 -118.824 -38.315 1.00 30.31  ? 272  ALA   B CA     1 
ATOM   6935 C C      . ALA   B  2 280 ? 18.634 -117.352 -37.941 1.00 35.56  ? 272  ALA   B C      1 
ATOM   6936 O O      . ALA   B  2 280 ? 19.241 -116.446 -38.526 1.00 34.31  ? 272  ALA   B O      1 
ATOM   6937 C CB     . ALA   B  2 280 ? 20.234 -119.283 -37.754 1.00 30.75  ? 272  ALA   B CB     1 
ATOM   6938 N N      . SER   B  2 281 ? 17.694 -117.124 -37.007 1.00 33.68  ? 273  SER   B N      1 
ATOM   6939 C CA     . SER   B  2 281 ? 17.340 -115.790 -36.508 1.00 33.96  ? 273  SER   B CA     1 
ATOM   6940 C C      . SER   B  2 281 ? 17.471 -115.770 -34.986 1.00 38.51  ? 273  SER   B C      1 
ATOM   6941 O O      . SER   B  2 281 ? 16.878 -116.604 -34.294 1.00 38.38  ? 273  SER   B O      1 
ATOM   6942 C CB     . SER   B  2 281 ? 15.947 -115.363 -36.967 1.00 36.68  ? 273  SER   B CB     1 
ATOM   6943 O OG     . SER   B  2 281 ? 14.922 -116.100 -36.324 1.00 46.84  ? 273  SER   B OG     1 
ATOM   6944 N N      . LEU   B  2 282 ? 18.308 -114.855 -34.483 1.00 34.94  ? 274  LEU   B N      1 
ATOM   6945 C CA     . LEU   B  2 282 ? 18.603 -114.699 -33.063 1.00 34.62  ? 274  LEU   B CA     1 
ATOM   6946 C C      . LEU   B  2 282 ? 18.056 -113.382 -32.544 1.00 37.07  ? 274  LEU   B C      1 
ATOM   6947 O O      . LEU   B  2 282 ? 18.103 -112.374 -33.247 1.00 35.68  ? 274  LEU   B O      1 
ATOM   6948 C CB     . LEU   B  2 282 ? 20.102 -114.860 -32.764 1.00 34.78  ? 274  LEU   B CB     1 
ATOM   6949 C CG     . LEU   B  2 282 ? 21.049 -114.171 -33.700 1.00 40.02  ? 274  LEU   B CG     1 
ATOM   6950 C CD1    . LEU   B  2 282 ? 21.978 -113.268 -32.958 1.00 41.02  ? 274  LEU   B CD1    1 
ATOM   6951 C CD2    . LEU   B  2 282 ? 21.802 -115.161 -34.531 1.00 42.87  ? 274  LEU   B CD2    1 
ATOM   6952 N N      . SER   B  2 283 ? 17.529 -113.400 -31.314 1.00 33.14  ? 275  SER   B N      1 
ATOM   6953 C CA     . SER   B  2 283 ? 16.840 -112.257 -30.738 1.00 32.39  ? 275  SER   B CA     1 
ATOM   6954 C C      . SER   B  2 283 ? 17.190 -111.922 -29.288 1.00 35.42  ? 275  SER   B C      1 
ATOM   6955 O O      . SER   B  2 283 ? 17.863 -112.692 -28.594 1.00 35.04  ? 275  SER   B O      1 
ATOM   6956 C CB     . SER   B  2 283 ? 15.336 -112.490 -30.875 1.00 34.34  ? 275  SER   B CB     1 
ATOM   6957 O OG     . SER   B  2 283 ? 14.509 -111.497 -30.292 1.00 38.55  ? 275  SER   B OG     1 
ATOM   6958 N N      . GLU   B  2 284 ? 16.706 -110.747 -28.843 1.00 30.78  ? 276  GLU   B N      1 
ATOM   6959 C CA     . GLU   B  2 284 ? 16.812 -110.255 -27.473 1.00 29.47  ? 276  GLU   B CA     1 
ATOM   6960 C C      . GLU   B  2 284 ? 15.776 -110.971 -26.591 1.00 32.26  ? 276  GLU   B C      1 
ATOM   6961 O O      . GLU   B  2 284 ? 15.887 -110.927 -25.368 1.00 32.39  ? 276  GLU   B O      1 
ATOM   6962 C CB     . GLU   B  2 284 ? 16.657 -108.727 -27.426 1.00 30.32  ? 276  GLU   B CB     1 
ATOM   6963 C CG     . GLU   B  2 284 ? 17.953 -108.002 -27.750 1.00 36.98  ? 276  GLU   B CG     1 
ATOM   6964 C CD     . GLU   B  2 284 ? 17.844 -106.510 -28.003 1.00 53.41  ? 276  GLU   B CD     1 
ATOM   6965 O OE1    . GLU   B  2 284 ? 16.859 -105.886 -27.546 1.00 35.63  ? 276  GLU   B OE1    1 
ATOM   6966 O OE2    . GLU   B  2 284 ? 18.766 -105.959 -28.646 1.00 47.85  ? 276  GLU   B OE2    1 
ATOM   6967 N N      . ASP   B  2 285 ? 14.810 -111.696 -27.208 1.00 28.58  ? 277  ASP   B N      1 
ATOM   6968 C CA     . ASP   B  2 285 ? 13.837 -112.510 -26.469 1.00 28.69  ? 277  ASP   B CA     1 
ATOM   6969 C C      . ASP   B  2 285 ? 14.498 -113.817 -25.973 1.00 34.02  ? 277  ASP   B C      1 
ATOM   6970 O O      . ASP   B  2 285 ? 13.811 -114.713 -25.480 1.00 34.26  ? 277  ASP   B O      1 
ATOM   6971 C CB     . ASP   B  2 285 ? 12.550 -112.773 -27.289 1.00 30.25  ? 277  ASP   B CB     1 
ATOM   6972 C CG     . ASP   B  2 285 ? 12.665 -113.698 -28.504 1.00 38.41  ? 277  ASP   B CG     1 
ATOM   6973 O OD1    . ASP   B  2 285 ? 13.760 -114.277 -28.723 1.00 35.10  ? 277  ASP   B OD1    1 
ATOM   6974 O OD2    . ASP   B  2 285 ? 11.648 -113.869 -29.217 1.00 46.67  ? 277  ASP   B OD2    1 
ATOM   6975 N N      . CYS   B  2 286 ? 15.841 -113.913 -26.139 1.00 31.29  ? 278  CYS   B N      1 
ATOM   6976 C CA     . CYS   B  2 286 ? 16.731 -114.997 -25.704 1.00 31.86  ? 278  CYS   B CA     1 
ATOM   6977 C C      . CYS   B  2 286 ? 16.548 -116.308 -26.481 1.00 37.52  ? 278  CYS   B C      1 
ATOM   6978 O O      . CYS   B  2 286 ? 17.111 -117.329 -26.081 1.00 39.12  ? 278  CYS   B O      1 
ATOM   6979 C CB     . CYS   B  2 286 ? 16.629 -115.219 -24.195 1.00 31.71  ? 278  CYS   B CB     1 
ATOM   6980 S SG     . CYS   B  2 286 ? 16.748 -113.697 -23.223 1.00 35.51  ? 278  CYS   B SG     1 
ATOM   6981 N N      . SER   B  2 287 ? 15.834 -116.275 -27.613 1.00 33.49  ? 279  SER   B N      1 
ATOM   6982 C CA     . SER   B  2 287 ? 15.640 -117.480 -28.421 1.00 32.89  ? 279  SER   B CA     1 
ATOM   6983 C C      . SER   B  2 287 ? 16.373 -117.451 -29.759 1.00 36.78  ? 279  SER   B C      1 
ATOM   6984 O O      . SER   B  2 287 ? 16.830 -116.401 -30.224 1.00 35.51  ? 279  SER   B O      1 
ATOM   6985 C CB     . SER   B  2 287 ? 14.157 -117.772 -28.631 1.00 34.88  ? 279  SER   B CB     1 
ATOM   6986 O OG     . SER   B  2 287 ? 13.572 -116.855 -29.540 1.00 40.03  ? 279  SER   B OG     1 
ATOM   6987 N N      . LEU   B  2 288 ? 16.489 -118.639 -30.356 1.00 33.66  ? 280  LEU   B N      1 
ATOM   6988 C CA     . LEU   B  2 288 ? 17.060 -118.904 -31.663 1.00 33.35  ? 280  LEU   B CA     1 
ATOM   6989 C C      . LEU   B  2 288 ? 15.954 -119.613 -32.424 1.00 37.12  ? 280  LEU   B C      1 
ATOM   6990 O O      . LEU   B  2 288 ? 15.294 -120.495 -31.870 1.00 36.28  ? 280  LEU   B O      1 
ATOM   6991 C CB     . LEU   B  2 288 ? 18.309 -119.823 -31.546 1.00 33.42  ? 280  LEU   B CB     1 
ATOM   6992 C CG     . LEU   B  2 288 ? 18.727 -120.602 -32.817 1.00 38.02  ? 280  LEU   B CG     1 
ATOM   6993 C CD1    . LEU   B  2 288 ? 19.563 -119.740 -33.750 1.00 38.33  ? 280  LEU   B CD1    1 
ATOM   6994 C CD2    . LEU   B  2 288 ? 19.465 -121.878 -32.463 1.00 39.96  ? 280  LEU   B CD2    1 
ATOM   6995 N N      . ALA   B  2 289 ? 15.749 -119.228 -33.681 1.00 34.27  ? 281  ALA   B N      1 
ATOM   6996 C CA     . ALA   B  2 289 ? 14.764 -119.858 -34.548 1.00 34.07  ? 281  ALA   B CA     1 
ATOM   6997 C C      . ALA   B  2 289 ? 15.412 -120.195 -35.883 1.00 37.41  ? 281  ALA   B C      1 
ATOM   6998 O O      . ALA   B  2 289 ? 16.246 -119.432 -36.373 1.00 36.49  ? 281  ALA   B O      1 
ATOM   6999 C CB     . ALA   B  2 289 ? 13.580 -118.931 -34.760 1.00 34.84  ? 281  ALA   B CB     1 
ATOM   7000 N N      . VAL   B  2 290 ? 15.045 -121.343 -36.459 1.00 34.29  ? 282  VAL   B N      1 
ATOM   7001 C CA     . VAL   B  2 290 ? 15.531 -121.765 -37.773 1.00 33.89  ? 282  VAL   B CA     1 
ATOM   7002 C C      . VAL   B  2 290 ? 14.329 -121.796 -38.709 1.00 38.92  ? 282  VAL   B C      1 
ATOM   7003 O O      . VAL   B  2 290 ? 13.326 -122.448 -38.414 1.00 37.87  ? 282  VAL   B O      1 
ATOM   7004 C CB     . VAL   B  2 290 ? 16.378 -123.068 -37.773 1.00 37.04  ? 282  VAL   B CB     1 
ATOM   7005 C CG1    . VAL   B  2 290 ? 16.783 -123.458 -39.194 1.00 36.82  ? 282  VAL   B CG1    1 
ATOM   7006 C CG2    . VAL   B  2 290 ? 17.624 -122.904 -36.906 1.00 36.45  ? 282  VAL   B CG2    1 
ATOM   7007 N N      . LEU   B  2 291 ? 14.412 -121.016 -39.794 1.00 37.04  ? 283  LEU   B N      1 
ATOM   7008 C CA     . LEU   B  2 291 ? 13.342 -120.856 -40.776 1.00 38.21  ? 283  LEU   B CA     1 
ATOM   7009 C C      . LEU   B  2 291 ? 13.729 -121.394 -42.154 1.00 44.45  ? 283  LEU   B C      1 
ATOM   7010 O O      . LEU   B  2 291 ? 14.916 -121.473 -42.482 1.00 43.68  ? 283  LEU   B O      1 
ATOM   7011 C CB     . LEU   B  2 291 ? 12.954 -119.367 -40.893 1.00 38.28  ? 283  LEU   B CB     1 
ATOM   7012 C CG     . LEU   B  2 291 ? 12.914 -118.550 -39.591 1.00 42.99  ? 283  LEU   B CG     1 
ATOM   7013 C CD1    . LEU   B  2 291 ? 13.150 -117.077 -39.868 1.00 43.10  ? 283  LEU   B CD1    1 
ATOM   7014 C CD2    . LEU   B  2 291 ? 11.615 -118.783 -38.825 1.00 45.14  ? 283  LEU   B CD2    1 
ATOM   7015 N N      . ASP   B  2 292 ? 12.719 -121.749 -42.960 1.00 43.57  ? 284  ASP   B N      1 
ATOM   7016 C CA     . ASP   B  2 292 ? 12.908 -122.234 -44.328 1.00 44.64  ? 284  ASP   B CA     1 
ATOM   7017 C C      . ASP   B  2 292 ? 12.787 -121.078 -45.354 1.00 50.79  ? 284  ASP   B C      1 
ATOM   7018 O O      . ASP   B  2 292 ? 12.792 -119.903 -44.961 1.00 49.82  ? 284  ASP   B O      1 
ATOM   7019 C CB     . ASP   B  2 292 ? 11.948 -123.408 -44.649 1.00 46.56  ? 284  ASP   B CB     1 
ATOM   7020 C CG     . ASP   B  2 292 ? 10.476 -123.164 -44.362 1.00 61.47  ? 284  ASP   B CG     1 
ATOM   7021 O OD1    . ASP   B  2 292 ? 9.928  -122.150 -44.861 1.00 62.60  ? 284  ASP   B OD1    1 
ATOM   7022 O OD2    . ASP   B  2 292 ? 9.856  -124.017 -43.691 1.00 70.23  ? 284  ASP   B OD2    1 
ATOM   7023 N N      . SER   B  2 293 ? 12.675 -121.424 -46.660 1.00 48.66  ? 285  SER   B N      1 
ATOM   7024 C CA     . SER   B  2 293 ? 12.555 -120.500 -47.794 1.00 48.95  ? 285  SER   B CA     1 
ATOM   7025 C C      . SER   B  2 293 ? 11.305 -119.607 -47.734 1.00 52.68  ? 285  SER   B C      1 
ATOM   7026 O O      . SER   B  2 293 ? 11.333 -118.498 -48.268 1.00 52.24  ? 285  SER   B O      1 
ATOM   7027 C CB     . SER   B  2 293 ? 12.576 -121.274 -49.111 1.00 53.29  ? 285  SER   B CB     1 
ATOM   7028 O OG     . SER   B  2 293 ? 11.384 -122.024 -49.289 1.00 64.06  ? 285  SER   B OG     1 
ATOM   7029 N N      . SER   B  2 294 ? 10.211 -120.108 -47.124 1.00 49.13  ? 286  SER   B N      1 
ATOM   7030 C CA     . SER   B  2 294 ? 8.942  -119.389 -46.985 1.00 49.01  ? 286  SER   B CA     1 
ATOM   7031 C C      . SER   B  2 294 ? 8.803  -118.716 -45.598 1.00 52.66  ? 286  SER   B C      1 
ATOM   7032 O O      . SER   B  2 294 ? 7.719  -118.249 -45.238 1.00 52.21  ? 286  SER   B O      1 
ATOM   7033 C CB     . SER   B  2 294 ? 7.769  -120.327 -47.258 1.00 52.62  ? 286  SER   B CB     1 
ATOM   7034 O OG     . SER   B  2 294 ? 7.738  -121.392 -46.323 1.00 61.97  ? 286  SER   B OG     1 
ATOM   7035 N N      . LEU   B  2 295 ? 9.921  -118.663 -44.841 1.00 48.78  ? 287  LEU   B N      1 
ATOM   7036 C CA     . LEU   B  2 295 ? 10.067 -118.087 -43.492 1.00 48.14  ? 287  LEU   B CA     1 
ATOM   7037 C C      . LEU   B  2 295 ? 9.253  -118.837 -42.411 1.00 52.04  ? 287  LEU   B C      1 
ATOM   7038 O O      . LEU   B  2 295 ? 8.978  -118.276 -41.347 1.00 52.17  ? 287  LEU   B O      1 
ATOM   7039 C CB     . LEU   B  2 295 ? 9.791  -116.563 -43.458 1.00 47.74  ? 287  LEU   B CB     1 
ATOM   7040 C CG     . LEU   B  2 295 ? 10.711 -115.677 -44.291 1.00 51.44  ? 287  LEU   B CG     1 
ATOM   7041 C CD1    . LEU   B  2 295 ? 10.141 -114.288 -44.420 1.00 51.48  ? 287  LEU   B CD1    1 
ATOM   7042 C CD2    . LEU   B  2 295 ? 12.122 -115.631 -43.720 1.00 53.17  ? 287  LEU   B CD2    1 
ATOM   7043 N N      . SER   B  2 296 ? 8.934  -120.124 -42.657 1.00 48.24  ? 288  SER   B N      1 
ATOM   7044 C CA     . SER   B  2 296 ? 8.223  -120.975 -41.699 1.00 47.83  ? 288  SER   B CA     1 
ATOM   7045 C C      . SER   B  2 296 ? 9.235  -121.615 -40.748 1.00 50.82  ? 288  SER   B C      1 
ATOM   7046 O O      . SER   B  2 296 ? 10.323 -122.013 -41.179 1.00 49.77  ? 288  SER   B O      1 
ATOM   7047 C CB     . SER   B  2 296 ? 7.423  -122.053 -42.423 1.00 52.28  ? 288  SER   B CB     1 
ATOM   7048 O OG     . SER   B  2 296 ? 6.541  -121.479 -43.375 1.00 63.36  ? 288  SER   B OG     1 
ATOM   7049 N N      . GLU   B  2 297 ? 8.874  -121.708 -39.457 1.00 47.10  ? 289  GLU   B N      1 
ATOM   7050 C CA     . GLU   B  2 297 ? 9.728  -122.249 -38.398 1.00 46.62  ? 289  GLU   B CA     1 
ATOM   7051 C C      . GLU   B  2 297 ? 9.907  -123.774 -38.465 1.00 48.66  ? 289  GLU   B C      1 
ATOM   7052 O O      . GLU   B  2 297 ? 8.930  -124.516 -38.546 1.00 48.00  ? 289  GLU   B O      1 
ATOM   7053 C CB     . GLU   B  2 297 ? 9.206  -121.806 -37.019 1.00 48.08  ? 289  GLU   B CB     1 
ATOM   7054 C CG     . GLU   B  2 297 ? 10.157 -122.075 -35.864 1.00 60.33  ? 289  GLU   B CG     1 
ATOM   7055 C CD     . GLU   B  2 297 ? 9.486  -122.073 -34.505 1.00 86.58  ? 289  GLU   B CD     1 
ATOM   7056 O OE1    . GLU   B  2 297 ? 9.098  -120.981 -34.032 1.00 80.09  ? 289  GLU   B OE1    1 
ATOM   7057 O OE2    . GLU   B  2 297 ? 9.332  -123.169 -33.920 1.00 86.97  ? 289  GLU   B OE2    1 
ATOM   7058 N N      . LEU   B  2 298 ? 11.163 -124.228 -38.386 1.00 44.57  ? 290  LEU   B N      1 
ATOM   7059 C CA     . LEU   B  2 298 ? 11.531 -125.647 -38.394 1.00 44.30  ? 290  LEU   B CA     1 
ATOM   7060 C C      . LEU   B  2 298 ? 12.094 -126.053 -37.035 1.00 46.94  ? 290  LEU   B C      1 
ATOM   7061 O O      . LEU   B  2 298 ? 11.925 -127.201 -36.620 1.00 46.82  ? 290  LEU   B O      1 
ATOM   7062 C CB     . LEU   B  2 298 ? 12.577 -125.945 -39.487 1.00 44.52  ? 290  LEU   B CB     1 
ATOM   7063 C CG     . LEU   B  2 298 ? 12.223 -125.517 -40.912 1.00 49.52  ? 290  LEU   B CG     1 
ATOM   7064 C CD1    . LEU   B  2 298 ? 13.423 -124.952 -41.608 1.00 49.63  ? 290  LEU   B CD1    1 
ATOM   7065 C CD2    . LEU   B  2 298 ? 11.610 -126.656 -41.707 1.00 51.73  ? 290  LEU   B CD2    1 
ATOM   7066 N N      . PHE   B  2 299 ? 12.765 -125.105 -36.350 1.00 41.70  ? 291  PHE   B N      1 
ATOM   7067 C CA     . PHE   B  2 299 ? 13.406 -125.310 -35.056 1.00 41.08  ? 291  PHE   B CA     1 
ATOM   7068 C C      . PHE   B  2 299 ? 13.324 -124.044 -34.188 1.00 44.02  ? 291  PHE   B C      1 
ATOM   7069 O O      . PHE   B  2 299 ? 13.397 -122.925 -34.702 1.00 43.15  ? 291  PHE   B O      1 
ATOM   7070 C CB     . PHE   B  2 299 ? 14.874 -125.707 -35.288 1.00 42.95  ? 291  PHE   B CB     1 
ATOM   7071 C CG     . PHE   B  2 299 ? 15.705 -126.036 -34.069 1.00 44.60  ? 291  PHE   B CG     1 
ATOM   7072 C CD1    . PHE   B  2 299 ? 15.599 -127.275 -33.449 1.00 47.40  ? 291  PHE   B CD1    1 
ATOM   7073 C CD2    . PHE   B  2 299 ? 16.665 -125.145 -33.603 1.00 46.48  ? 291  PHE   B CD2    1 
ATOM   7074 C CE1    . PHE   B  2 299 ? 16.401 -127.596 -32.350 1.00 48.17  ? 291  PHE   B CE1    1 
ATOM   7075 C CE2    . PHE   B  2 299 ? 17.468 -125.467 -32.507 1.00 49.25  ? 291  PHE   B CE2    1 
ATOM   7076 C CZ     . PHE   B  2 299 ? 17.329 -126.690 -31.885 1.00 47.36  ? 291  PHE   B CZ     1 
ATOM   7077 N N      . ARG   B  2 300 ? 13.176 -124.235 -32.873 1.00 39.66  ? 292  ARG   B N      1 
ATOM   7078 C CA     . ARG   B  2 300 ? 13.138 -123.165 -31.878 1.00 38.98  ? 292  ARG   B CA     1 
ATOM   7079 C C      . ARG   B  2 300 ? 13.920 -123.616 -30.654 1.00 41.01  ? 292  ARG   B C      1 
ATOM   7080 O O      . ARG   B  2 300 ? 13.660 -124.693 -30.126 1.00 40.92  ? 292  ARG   B O      1 
ATOM   7081 C CB     . ARG   B  2 300 ? 11.684 -122.790 -31.516 1.00 40.11  ? 292  ARG   B CB     1 
ATOM   7082 C CG     . ARG   B  2 300 ? 11.534 -121.768 -30.369 1.00 44.87  ? 292  ARG   B CG     1 
ATOM   7083 C CD     . ARG   B  2 300 ? 11.769 -120.329 -30.792 1.00 42.58  ? 292  ARG   B CD     1 
ATOM   7084 N NE     . ARG   B  2 300 ? 10.768 -119.886 -31.761 1.00 42.57  ? 292  ARG   B NE     1 
ATOM   7085 C CZ     . ARG   B  2 300 ? 10.639 -118.639 -32.202 1.00 54.20  ? 292  ARG   B CZ     1 
ATOM   7086 N NH1    . ARG   B  2 300 ? 11.437 -117.680 -31.747 1.00 44.09  ? 292  ARG   B NH1    1 
ATOM   7087 N NH2    . ARG   B  2 300 ? 9.701  -118.337 -33.089 1.00 38.58  ? 292  ARG   B NH2    1 
ATOM   7088 N N      . SER   B  2 301 ? 14.893 -122.807 -30.222 1.00 36.53  ? 293  SER   B N      1 
ATOM   7089 C CA     . SER   B  2 301 ? 15.709 -123.114 -29.051 1.00 35.91  ? 293  SER   B CA     1 
ATOM   7090 C C      . SER   B  2 301 ? 15.683 -121.982 -28.023 1.00 39.48  ? 293  SER   B C      1 
ATOM   7091 O O      . SER   B  2 301 ? 15.954 -120.823 -28.362 1.00 38.00  ? 293  SER   B O      1 
ATOM   7092 C CB     . SER   B  2 301 ? 17.145 -123.413 -29.461 1.00 38.74  ? 293  SER   B CB     1 
ATOM   7093 O OG     . SER   B  2 301 ? 17.950 -123.641 -28.316 1.00 46.35  ? 293  SER   B OG     1 
ATOM   7094 N N      . GLN   B  2 302 ? 15.399 -122.345 -26.758 1.00 36.57  ? 294  GLN   B N      1 
ATOM   7095 C CA     . GLN   B  2 302 ? 15.364 -121.437 -25.610 1.00 36.67  ? 294  GLN   B CA     1 
ATOM   7096 C C      . GLN   B  2 302 ? 16.472 -121.784 -24.605 1.00 41.68  ? 294  GLN   B C      1 
ATOM   7097 O O      . GLN   B  2 302 ? 16.348 -121.456 -23.423 1.00 42.23  ? 294  GLN   B O      1 
ATOM   7098 C CB     . GLN   B  2 302 ? 13.985 -121.481 -24.928 1.00 38.07  ? 294  GLN   B CB     1 
ATOM   7099 C CG     . GLN   B  2 302 ? 12.878 -120.789 -25.704 1.00 50.09  ? 294  GLN   B CG     1 
ATOM   7100 C CD     . GLN   B  2 302 ? 11.538 -121.184 -25.161 1.00 72.31  ? 294  GLN   B CD     1 
ATOM   7101 O OE1    . GLN   B  2 302 ? 11.047 -122.292 -25.402 1.00 71.36  ? 294  GLN   B OE1    1 
ATOM   7102 N NE2    . GLN   B  2 302 ? 10.927 -120.299 -24.395 1.00 64.75  ? 294  GLN   B NE2    1 
ATOM   7103 N N      . ALA   B  2 303 ? 17.565 -122.426 -25.082 1.00 38.16  ? 295  ALA   B N      1 
ATOM   7104 C CA     . ALA   B  2 303 ? 18.717 -122.838 -24.266 1.00 38.09  ? 295  ALA   B CA     1 
ATOM   7105 C C      . ALA   B  2 303 ? 19.374 -121.668 -23.525 1.00 41.12  ? 295  ALA   B C      1 
ATOM   7106 O O      . ALA   B  2 303 ? 19.812 -121.828 -22.381 1.00 41.13  ? 295  ALA   B O      1 
ATOM   7107 C CB     . ALA   B  2 303 ? 19.748 -123.550 -25.132 1.00 38.82  ? 295  ALA   B CB     1 
ATOM   7108 N N      . HIS   B  2 304 ? 19.443 -120.497 -24.177 1.00 35.74  ? 296  HIS   B N      1 
ATOM   7109 C CA     . HIS   B  2 304 ? 20.040 -119.308 -23.588 1.00 34.50  ? 296  HIS   B CA     1 
ATOM   7110 C C      . HIS   B  2 304 ? 19.130 -118.646 -22.551 1.00 38.51  ? 296  HIS   B C      1 
ATOM   7111 O O      . HIS   B  2 304 ? 17.910 -118.581 -22.734 1.00 38.63  ? 296  HIS   B O      1 
ATOM   7112 C CB     . HIS   B  2 304 ? 20.459 -118.315 -24.670 1.00 34.46  ? 296  HIS   B CB     1 
ATOM   7113 C CG     . HIS   B  2 304 ? 21.670 -118.740 -25.440 1.00 37.02  ? 296  HIS   B CG     1 
ATOM   7114 N ND1    . HIS   B  2 304 ? 22.946 -118.508 -24.959 1.00 38.20  ? 296  HIS   B ND1    1 
ATOM   7115 C CD2    . HIS   B  2 304 ? 21.761 -119.325 -26.657 1.00 38.06  ? 296  HIS   B CD2    1 
ATOM   7116 C CE1    . HIS   B  2 304 ? 23.769 -118.965 -25.888 1.00 37.58  ? 296  HIS   B CE1    1 
ATOM   7117 N NE2    . HIS   B  2 304 ? 23.102 -119.470 -26.926 1.00 37.87  ? 296  HIS   B NE2    1 
ATOM   7118 N N      . ARG   B  2 305 ? 19.734 -118.168 -21.461 1.00 35.17  ? 297  ARG   B N      1 
ATOM   7119 C CA     . ARG   B  2 305 ? 19.033 -117.486 -20.370 1.00 35.37  ? 297  ARG   B CA     1 
ATOM   7120 C C      . ARG   B  2 305 ? 19.250 -115.950 -20.420 1.00 38.05  ? 297  ARG   B C      1 
ATOM   7121 O O      . ARG   B  2 305 ? 18.796 -115.221 -19.538 1.00 38.11  ? 297  ARG   B O      1 
ATOM   7122 C CB     . ARG   B  2 305 ? 19.377 -118.110 -18.999 1.00 38.20  ? 297  ARG   B CB     1 
ATOM   7123 C CG     . ARG   B  2 305 ? 20.870 -118.323 -18.758 1.00 56.69  ? 297  ARG   B CG     1 
ATOM   7124 C CD     . ARG   B  2 305 ? 21.177 -119.109 -17.493 1.00 70.26  ? 297  ARG   B CD     1 
ATOM   7125 N NE     . ARG   B  2 305 ? 22.586 -118.969 -17.115 1.00 81.33  ? 297  ARG   B NE     1 
ATOM   7126 C CZ     . ARG   B  2 305 ? 23.553 -119.808 -17.476 1.00 95.73  ? 297  ARG   B CZ     1 
ATOM   7127 N NH1    . ARG   B  2 305 ? 23.275 -120.876 -18.214 1.00 81.67  ? 297  ARG   B NH1    1 
ATOM   7128 N NH2    . ARG   B  2 305 ? 24.804 -119.592 -17.093 1.00 83.59  ? 297  ARG   B NH2    1 
ATOM   7129 N N      . ASP   B  2 306 ? 19.909 -115.472 -21.493 1.00 33.21  ? 298  ASP   B N      1 
ATOM   7130 C CA     . ASP   B  2 306 ? 20.179 -114.059 -21.784 1.00 31.83  ? 298  ASP   B CA     1 
ATOM   7131 C C      . ASP   B  2 306 ? 20.248 -113.883 -23.316 1.00 34.81  ? 298  ASP   B C      1 
ATOM   7132 O O      . ASP   B  2 306 ? 20.155 -114.875 -24.042 1.00 35.82  ? 298  ASP   B O      1 
ATOM   7133 C CB     . ASP   B  2 306 ? 21.468 -113.574 -21.081 1.00 32.91  ? 298  ASP   B CB     1 
ATOM   7134 C CG     . ASP   B  2 306 ? 21.498 -112.096 -20.687 1.00 39.01  ? 298  ASP   B CG     1 
ATOM   7135 O OD1    . ASP   B  2 306 ? 20.807 -111.277 -21.353 1.00 38.68  ? 298  ASP   B OD1    1 
ATOM   7136 O OD2    . ASP   B  2 306 ? 22.274 -111.743 -19.768 1.00 41.13  ? 298  ASP   B OD2    1 
ATOM   7137 N N      . PHE   B  2 307 ? 20.384 -112.634 -23.797 1.00 28.80  ? 299  PHE   B N      1 
ATOM   7138 C CA     . PHE   B  2 307 ? 20.424 -112.265 -25.214 1.00 27.45  ? 299  PHE   B CA     1 
ATOM   7139 C C      . PHE   B  2 307 ? 21.339 -113.160 -26.069 1.00 30.47  ? 299  PHE   B C      1 
ATOM   7140 O O      . PHE   B  2 307 ? 22.523 -113.288 -25.758 1.00 29.48  ? 299  PHE   B O      1 
ATOM   7141 C CB     . PHE   B  2 307 ? 20.868 -110.799 -25.370 1.00 28.45  ? 299  PHE   B CB     1 
ATOM   7142 C CG     . PHE   B  2 307 ? 20.010 -109.696 -24.782 1.00 29.13  ? 299  PHE   B CG     1 
ATOM   7143 C CD1    . PHE   B  2 307 ? 18.748 -109.967 -24.266 1.00 31.36  ? 299  PHE   B CD1    1 
ATOM   7144 C CD2    . PHE   B  2 307 ? 20.447 -108.380 -24.792 1.00 31.15  ? 299  PHE   B CD2    1 
ATOM   7145 C CE1    . PHE   B  2 307 ? 17.957 -108.944 -23.737 1.00 32.26  ? 299  PHE   B CE1    1 
ATOM   7146 C CE2    . PHE   B  2 307 ? 19.659 -107.359 -24.249 1.00 33.89  ? 299  PHE   B CE2    1 
ATOM   7147 C CZ     . PHE   B  2 307 ? 18.422 -107.649 -23.724 1.00 31.34  ? 299  PHE   B CZ     1 
ATOM   7148 N N      . VAL   B  2 308 ? 20.789 -113.764 -27.140 1.00 27.38  ? 300  VAL   B N      1 
ATOM   7149 C CA     . VAL   B  2 308 ? 21.553 -114.595 -28.091 1.00 27.42  ? 300  VAL   B CA     1 
ATOM   7150 C C      . VAL   B  2 308 ? 22.213 -113.590 -29.031 1.00 30.32  ? 300  VAL   B C      1 
ATOM   7151 O O      . VAL   B  2 308 ? 21.516 -112.793 -29.670 1.00 31.67  ? 300  VAL   B O      1 
ATOM   7152 C CB     . VAL   B  2 308 ? 20.678 -115.637 -28.839 1.00 32.59  ? 300  VAL   B CB     1 
ATOM   7153 C CG1    . VAL   B  2 308 ? 21.539 -116.567 -29.698 1.00 32.95  ? 300  VAL   B CG1    1 
ATOM   7154 C CG2    . VAL   B  2 308 ? 19.831 -116.450 -27.868 1.00 32.38  ? 300  VAL   B CG2    1 
ATOM   7155 N N      . ARG   B  2 309 ? 23.545 -113.569 -29.057 1.00 25.17  ? 301  ARG   B N      1 
ATOM   7156 C CA     . ARG   B  2 309 ? 24.304 -112.561 -29.798 1.00 25.15  ? 301  ARG   B CA     1 
ATOM   7157 C C      . ARG   B  2 309 ? 24.832 -112.953 -31.183 1.00 32.13  ? 301  ARG   B C      1 
ATOM   7158 O O      . ARG   B  2 309 ? 24.986 -112.078 -32.038 1.00 31.48  ? 301  ARG   B O      1 
ATOM   7159 C CB     . ARG   B  2 309 ? 25.460 -112.075 -28.931 1.00 24.39  ? 301  ARG   B CB     1 
ATOM   7160 C CG     . ARG   B  2 309 ? 24.960 -111.320 -27.717 1.00 30.06  ? 301  ARG   B CG     1 
ATOM   7161 C CD     . ARG   B  2 309 ? 24.821 -109.856 -28.057 1.00 41.48  ? 301  ARG   B CD     1 
ATOM   7162 N NE     . ARG   B  2 309 ? 23.436 -109.430 -28.177 1.00 43.21  ? 301  ARG   B NE     1 
ATOM   7163 C CZ     . ARG   B  2 309 ? 23.068 -108.259 -28.677 1.00 49.75  ? 301  ARG   B CZ     1 
ATOM   7164 N NH1    . ARG   B  2 309 ? 23.978 -107.415 -29.150 1.00 32.35  ? 301  ARG   B NH1    1 
ATOM   7165 N NH2    . ARG   B  2 309 ? 21.788 -107.929 -28.729 1.00 41.42  ? 301  ARG   B NH2    1 
ATOM   7166 N N      . ASP   B  2 310 ? 25.116 -114.235 -31.410 1.00 31.61  ? 302  ASP   B N      1 
ATOM   7167 C CA     . ASP   B  2 310 ? 25.620 -114.703 -32.705 1.00 32.16  ? 302  ASP   B CA     1 
ATOM   7168 C C      . ASP   B  2 310 ? 25.297 -116.163 -32.946 1.00 36.06  ? 302  ASP   B C      1 
ATOM   7169 O O      . ASP   B  2 310 ? 25.019 -116.899 -32.005 1.00 34.50  ? 302  ASP   B O      1 
ATOM   7170 C CB     . ASP   B  2 310 ? 27.141 -114.451 -32.849 1.00 33.93  ? 302  ASP   B CB     1 
ATOM   7171 C CG     . ASP   B  2 310 ? 27.595 -114.155 -34.275 1.00 41.70  ? 302  ASP   B CG     1 
ATOM   7172 O OD1    . ASP   B  2 310 ? 26.786 -114.354 -35.218 1.00 41.83  ? 302  ASP   B OD1    1 
ATOM   7173 O OD2    . ASP   B  2 310 ? 28.746 -113.705 -34.447 1.00 45.75  ? 302  ASP   B OD2    1 
ATOM   7174 N N      . ALA   B  2 311 ? 25.303 -116.568 -34.223 1.00 33.77  ? 303  ALA   B N      1 
ATOM   7175 C CA     . ALA   B  2 311 ? 25.076 -117.946 -34.645 1.00 33.21  ? 303  ALA   B CA     1 
ATOM   7176 C C      . ALA   B  2 311 ? 26.007 -118.253 -35.811 1.00 38.66  ? 303  ALA   B C      1 
ATOM   7177 O O      . ALA   B  2 311 ? 26.165 -117.431 -36.723 1.00 37.97  ? 303  ALA   B O      1 
ATOM   7178 C CB     . ALA   B  2 311 ? 23.627 -118.162 -35.047 1.00 33.65  ? 303  ALA   B CB     1 
ATOM   7179 N N      . THR   B  2 312 ? 26.669 -119.418 -35.748 1.00 35.66  ? 304  THR   B N      1 
ATOM   7180 C CA     . THR   B  2 312 ? 27.592 -119.868 -36.788 1.00 35.23  ? 304  THR   B CA     1 
ATOM   7181 C C      . THR   B  2 312 ? 27.344 -121.345 -37.096 1.00 38.39  ? 304  THR   B C      1 
ATOM   7182 O O      . THR   B  2 312 ? 27.288 -122.171 -36.183 1.00 36.80  ? 304  THR   B O      1 
ATOM   7183 C CB     . THR   B  2 312 ? 29.050 -119.500 -36.462 1.00 42.88  ? 304  THR   B CB     1 
ATOM   7184 O OG1    . THR   B  2 312 ? 29.898 -119.834 -37.567 1.00 42.87  ? 304  THR   B OG1    1 
ATOM   7185 C CG2    . THR   B  2 312 ? 29.556 -120.103 -35.148 1.00 40.82  ? 304  THR   B CG2    1 
ATOM   7186 N N      . TRP   B  2 313 ? 27.114 -121.653 -38.384 1.00 35.78  ? 305  TRP   B N      1 
ATOM   7187 C CA     . TRP   B  2 313 ? 26.860 -123.022 -38.853 1.00 35.19  ? 305  TRP   B CA     1 
ATOM   7188 C C      . TRP   B  2 313 ? 28.193 -123.716 -39.076 1.00 40.29  ? 305  TRP   B C      1 
ATOM   7189 O O      . TRP   B  2 313 ? 29.133 -123.082 -39.570 1.00 38.61  ? 305  TRP   B O      1 
ATOM   7190 C CB     . TRP   B  2 313 ? 26.065 -123.012 -40.157 1.00 32.97  ? 305  TRP   B CB     1 
ATOM   7191 C CG     . TRP   B  2 313 ? 24.676 -122.468 -40.041 1.00 33.27  ? 305  TRP   B CG     1 
ATOM   7192 C CD1    . TRP   B  2 313 ? 24.293 -121.165 -40.163 1.00 35.82  ? 305  TRP   B CD1    1 
ATOM   7193 C CD2    . TRP   B  2 313 ? 23.470 -123.228 -39.872 1.00 32.72  ? 305  TRP   B CD2    1 
ATOM   7194 N NE1    . TRP   B  2 313 ? 22.922 -121.064 -40.078 1.00 34.87  ? 305  TRP   B NE1    1 
ATOM   7195 C CE2    . TRP   B  2 313 ? 22.394 -122.312 -39.873 1.00 36.17  ? 305  TRP   B CE2    1 
ATOM   7196 C CE3    . TRP   B  2 313 ? 23.193 -124.598 -39.728 1.00 33.79  ? 305  TRP   B CE3    1 
ATOM   7197 C CZ2    . TRP   B  2 313 ? 21.062 -122.722 -39.735 1.00 35.59  ? 305  TRP   B CZ2    1 
ATOM   7198 C CZ3    . TRP   B  2 313 ? 21.876 -125.003 -39.568 1.00 35.19  ? 305  TRP   B CZ3    1 
ATOM   7199 C CH2    . TRP   B  2 313 ? 20.826 -124.072 -39.582 1.00 35.85  ? 305  TRP   B CH2    1 
ATOM   7200 N N      . SER   B  2 314 ? 28.292 -125.000 -38.680 1.00 39.53  ? 306  SER   B N      1 
ATOM   7201 C CA     . SER   B  2 314 ? 29.530 -125.765 -38.837 1.00 40.81  ? 306  SER   B CA     1 
ATOM   7202 C C      . SER   B  2 314 ? 29.794 -126.115 -40.305 1.00 45.65  ? 306  SER   B C      1 
ATOM   7203 O O      . SER   B  2 314 ? 28.888 -126.607 -40.987 1.00 45.99  ? 306  SER   B O      1 
ATOM   7204 C CB     . SER   B  2 314 ? 29.523 -127.023 -37.972 1.00 45.96  ? 306  SER   B CB     1 
ATOM   7205 O OG     . SER   B  2 314 ? 30.699 -127.794 -38.169 1.00 56.68  ? 306  SER   B OG     1 
ATOM   7206 N N      . PRO   B  2 315 ? 31.016 -125.849 -40.816 1.00 42.48  ? 307  PRO   B N      1 
ATOM   7207 C CA     . PRO   B  2 315 ? 31.315 -126.211 -42.215 1.00 42.77  ? 307  PRO   B CA     1 
ATOM   7208 C C      . PRO   B  2 315 ? 31.533 -127.723 -42.393 1.00 48.59  ? 307  PRO   B C      1 
ATOM   7209 O O      . PRO   B  2 315 ? 31.353 -128.241 -43.498 1.00 47.76  ? 307  PRO   B O      1 
ATOM   7210 C CB     . PRO   B  2 315 ? 32.575 -125.403 -42.528 1.00 44.21  ? 307  PRO   B CB     1 
ATOM   7211 C CG     . PRO   B  2 315 ? 33.241 -125.224 -41.221 1.00 48.57  ? 307  PRO   B CG     1 
ATOM   7212 C CD     . PRO   B  2 315 ? 32.196 -125.264 -40.142 1.00 44.00  ? 307  PRO   B CD     1 
ATOM   7213 N N      . LEU   B  2 316 ? 31.911 -128.418 -41.297 1.00 46.19  ? 308  LEU   B N      1 
ATOM   7214 C CA     . LEU   B  2 316 ? 32.150 -129.861 -41.240 1.00 46.51  ? 308  LEU   B CA     1 
ATOM   7215 C C      . LEU   B  2 316 ? 30.820 -130.621 -41.173 1.00 51.03  ? 308  LEU   B C      1 
ATOM   7216 O O      . LEU   B  2 316 ? 30.606 -131.537 -41.970 1.00 51.48  ? 308  LEU   B O      1 
ATOM   7217 C CB     . LEU   B  2 316 ? 33.065 -130.218 -40.051 1.00 46.63  ? 308  LEU   B CB     1 
ATOM   7218 C CG     . LEU   B  2 316 ? 34.434 -129.512 -39.996 1.00 51.80  ? 308  LEU   B CG     1 
ATOM   7219 C CD1    . LEU   B  2 316 ? 35.125 -129.767 -38.677 1.00 52.21  ? 308  LEU   B CD1    1 
ATOM   7220 C CD2    . LEU   B  2 316 ? 35.344 -129.927 -41.157 1.00 54.44  ? 308  LEU   B CD2    1 
ATOM   7221 N N      . ASN   B  2 317 ? 29.915 -130.216 -40.259 1.00 46.55  ? 309  ASN   B N      1 
ATOM   7222 C CA     . ASN   B  2 317 ? 28.589 -130.821 -40.112 1.00 45.81  ? 309  ASN   B CA     1 
ATOM   7223 C C      . ASN   B  2 317 ? 27.536 -129.729 -40.277 1.00 50.13  ? 309  ASN   B C      1 
ATOM   7224 O O      . ASN   B  2 317 ? 27.305 -128.927 -39.363 1.00 50.39  ? 309  ASN   B O      1 
ATOM   7225 C CB     . ASN   B  2 317 ? 28.457 -131.549 -38.769 1.00 45.10  ? 309  ASN   B CB     1 
ATOM   7226 C CG     . ASN   B  2 317 ? 27.236 -132.443 -38.612 1.00 62.97  ? 309  ASN   B CG     1 
ATOM   7227 O OD1    . ASN   B  2 317 ? 26.209 -132.318 -39.299 1.00 50.92  ? 309  ASN   B OD1    1 
ATOM   7228 N ND2    . ASN   B  2 317 ? 27.312 -133.358 -37.659 1.00 56.50  ? 309  ASN   B ND2    1 
ATOM   7229 N N      . HIS   B  2 318 ? 26.906 -129.698 -41.461 1.00 45.67  ? 310  HIS   B N      1 
ATOM   7230 C CA     . HIS   B  2 318 ? 25.897 -128.715 -41.854 1.00 45.21  ? 310  HIS   B CA     1 
ATOM   7231 C C      . HIS   B  2 318 ? 24.626 -128.714 -40.975 1.00 51.20  ? 310  HIS   B C      1 
ATOM   7232 O O      . HIS   B  2 318 ? 23.920 -127.705 -40.944 1.00 51.08  ? 310  HIS   B O      1 
ATOM   7233 C CB     . HIS   B  2 318 ? 25.552 -128.875 -43.341 1.00 45.16  ? 310  HIS   B CB     1 
ATOM   7234 C CG     . HIS   B  2 318 ? 26.633 -128.412 -44.272 1.00 47.93  ? 310  HIS   B CG     1 
ATOM   7235 N ND1    . HIS   B  2 318 ? 26.454 -128.432 -45.642 1.00 49.52  ? 310  HIS   B ND1    1 
ATOM   7236 C CD2    . HIS   B  2 318 ? 27.868 -127.920 -44.002 1.00 49.33  ? 310  HIS   B CD2    1 
ATOM   7237 C CE1    . HIS   B  2 318 ? 27.575 -127.952 -46.160 1.00 48.83  ? 310  HIS   B CE1    1 
ATOM   7238 N NE2    . HIS   B  2 318 ? 28.457 -127.636 -45.212 1.00 49.10  ? 310  HIS   B NE2    1 
ATOM   7239 N N      . SER   B  2 319 ? 24.365 -129.807 -40.236 1.00 48.84  ? 311  SER   B N      1 
ATOM   7240 C CA     . SER   B  2 319 ? 23.216 -129.917 -39.331 1.00 49.14  ? 311  SER   B CA     1 
ATOM   7241 C C      . SER   B  2 319 ? 23.475 -129.200 -37.983 1.00 52.09  ? 311  SER   B C      1 
ATOM   7242 O O      . SER   B  2 319 ? 22.531 -128.924 -37.235 1.00 51.14  ? 311  SER   B O      1 
ATOM   7243 C CB     . SER   B  2 319 ? 22.876 -131.384 -39.092 1.00 54.05  ? 311  SER   B CB     1 
ATOM   7244 O OG     . SER   B  2 319 ? 21.638 -131.523 -38.413 1.00 67.14  ? 311  SER   B OG     1 
ATOM   7245 N N      . LEU   B  2 320 ? 24.755 -128.899 -37.689 1.00 48.11  ? 312  LEU   B N      1 
ATOM   7246 C CA     . LEU   B  2 320 ? 25.167 -128.256 -36.447 1.00 47.24  ? 312  LEU   B CA     1 
ATOM   7247 C C      . LEU   B  2 320 ? 25.245 -126.729 -36.532 1.00 47.87  ? 312  LEU   B C      1 
ATOM   7248 O O      . LEU   B  2 320 ? 25.929 -126.170 -37.392 1.00 47.03  ? 312  LEU   B O      1 
ATOM   7249 C CB     . LEU   B  2 320 ? 26.485 -128.848 -35.922 1.00 47.77  ? 312  LEU   B CB     1 
ATOM   7250 C CG     . LEU   B  2 320 ? 26.399 -130.243 -35.277 1.00 53.56  ? 312  LEU   B CG     1 
ATOM   7251 C CD1    . LEU   B  2 320 ? 27.768 -130.891 -35.206 1.00 54.07  ? 312  LEU   B CD1    1 
ATOM   7252 C CD2    . LEU   B  2 320 ? 25.803 -130.176 -33.870 1.00 57.01  ? 312  LEU   B CD2    1 
ATOM   7253 N N      . LEU   B  2 321 ? 24.541 -126.067 -35.610 1.00 42.82  ? 313  LEU   B N      1 
ATOM   7254 C CA     . LEU   B  2 321 ? 24.480 -124.613 -35.486 1.00 41.36  ? 313  LEU   B CA     1 
ATOM   7255 C C      . LEU   B  2 321 ? 24.888 -124.217 -34.069 1.00 42.26  ? 313  LEU   B C      1 
ATOM   7256 O O      . LEU   B  2 321 ? 24.257 -124.648 -33.106 1.00 41.52  ? 313  LEU   B O      1 
ATOM   7257 C CB     . LEU   B  2 321 ? 23.057 -124.129 -35.827 1.00 41.32  ? 313  LEU   B CB     1 
ATOM   7258 C CG     . LEU   B  2 321 ? 22.703 -122.654 -35.610 1.00 45.43  ? 313  LEU   B CG     1 
ATOM   7259 C CD1    . LEU   B  2 321 ? 23.511 -121.739 -36.520 1.00 45.33  ? 313  LEU   B CD1    1 
ATOM   7260 C CD2    . LEU   B  2 321 ? 21.235 -122.439 -35.837 1.00 47.06  ? 313  LEU   B CD2    1 
ATOM   7261 N N      . THR   B  2 322 ? 25.965 -123.428 -33.950 1.00 37.08  ? 314  THR   B N      1 
ATOM   7262 C CA     . THR   B  2 322 ? 26.502 -122.972 -32.671 1.00 36.28  ? 314  THR   B CA     1 
ATOM   7263 C C      . THR   B  2 322 ? 26.059 -121.525 -32.367 1.00 39.26  ? 314  THR   B C      1 
ATOM   7264 O O      . THR   B  2 322 ? 26.213 -120.649 -33.217 1.00 38.77  ? 314  THR   B O      1 
ATOM   7265 C CB     . THR   B  2 322 ? 28.034 -123.157 -32.653 1.00 43.03  ? 314  THR   B CB     1 
ATOM   7266 O OG1    . THR   B  2 322 ? 28.339 -124.536 -32.859 1.00 46.05  ? 314  THR   B OG1    1 
ATOM   7267 C CG2    . THR   B  2 322 ? 28.672 -122.699 -31.358 1.00 39.92  ? 314  THR   B CG2    1 
ATOM   7268 N N      . THR   B  2 323 ? 25.524 -121.280 -31.157 1.00 35.30  ? 315  THR   B N      1 
ATOM   7269 C CA     . THR   B  2 323 ? 25.114 -119.934 -30.727 1.00 34.31  ? 315  THR   B CA     1 
ATOM   7270 C C      . THR   B  2 323 ? 25.820 -119.501 -29.453 1.00 36.02  ? 315  THR   B C      1 
ATOM   7271 O O      . THR   B  2 323 ? 26.100 -120.331 -28.591 1.00 34.97  ? 315  THR   B O      1 
ATOM   7272 C CB     . THR   B  2 323 ? 23.595 -119.809 -30.523 1.00 37.67  ? 315  THR   B CB     1 
ATOM   7273 O OG1    . THR   B  2 323 ? 23.181 -120.673 -29.472 1.00 35.23  ? 315  THR   B OG1    1 
ATOM   7274 C CG2    . THR   B  2 323 ? 22.794 -120.054 -31.789 1.00 34.37  ? 315  THR   B CG2    1 
ATOM   7275 N N      . VAL   B  2 324 ? 26.085 -118.193 -29.335 1.00 32.24  ? 316  VAL   B N      1 
ATOM   7276 C CA     . VAL   B  2 324 ? 26.679 -117.573 -28.148 1.00 32.11  ? 316  VAL   B CA     1 
ATOM   7277 C C      . VAL   B  2 324 ? 25.732 -116.506 -27.580 1.00 37.06  ? 316  VAL   B C      1 
ATOM   7278 O O      . VAL   B  2 324 ? 24.970 -115.888 -28.332 1.00 35.91  ? 316  VAL   B O      1 
ATOM   7279 C CB     . VAL   B  2 324 ? 28.132 -117.063 -28.318 1.00 35.54  ? 316  VAL   B CB     1 
ATOM   7280 C CG1    . VAL   B  2 324 ? 29.092 -118.213 -28.616 1.00 35.52  ? 316  VAL   B CG1    1 
ATOM   7281 C CG2    . VAL   B  2 324 ? 28.233 -115.952 -29.363 1.00 34.89  ? 316  VAL   B CG2    1 
ATOM   7282 N N      . GLY   B  2 325 ? 25.773 -116.332 -26.262 1.00 35.07  ? 317  GLY   B N      1 
ATOM   7283 C CA     . GLY   B  2 325 ? 24.923 -115.371 -25.567 1.00 34.98  ? 317  GLY   B CA     1 
ATOM   7284 C C      . GLY   B  2 325 ? 25.595 -114.619 -24.441 1.00 37.68  ? 317  GLY   B C      1 
ATOM   7285 O O      . GLY   B  2 325 ? 26.721 -114.941 -24.054 1.00 36.86  ? 317  GLY   B O      1 
ATOM   7286 N N      . TRP   B  2 326 ? 24.896 -113.608 -23.896 1.00 34.14  ? 318  TRP   B N      1 
ATOM   7287 C CA     . TRP   B  2 326 ? 25.398 -112.803 -22.776 1.00 33.53  ? 318  TRP   B CA     1 
ATOM   7288 C C      . TRP   B  2 326 ? 25.424 -113.586 -21.457 1.00 36.79  ? 318  TRP   B C      1 
ATOM   7289 O O      . TRP   B  2 326 ? 26.034 -113.146 -20.483 1.00 36.47  ? 318  TRP   B O      1 
ATOM   7290 C CB     . TRP   B  2 326 ? 24.619 -111.482 -22.654 1.00 32.09  ? 318  TRP   B CB     1 
ATOM   7291 C CG     . TRP   B  2 326 ? 25.049 -110.437 -23.648 1.00 33.03  ? 318  TRP   B CG     1 
ATOM   7292 C CD1    . TRP   B  2 326 ? 26.059 -110.537 -24.559 1.00 35.74  ? 318  TRP   B CD1    1 
ATOM   7293 C CD2    . TRP   B  2 326 ? 24.539 -109.101 -23.762 1.00 32.75  ? 318  TRP   B CD2    1 
ATOM   7294 N NE1    . TRP   B  2 326 ? 26.194 -109.359 -25.248 1.00 35.19  ? 318  TRP   B NE1    1 
ATOM   7295 C CE2    . TRP   B  2 326 ? 25.268 -108.461 -24.788 1.00 36.53  ? 318  TRP   B CE2    1 
ATOM   7296 C CE3    . TRP   B  2 326 ? 23.552 -108.371 -23.076 1.00 33.92  ? 318  TRP   B CE3    1 
ATOM   7297 C CZ2    . TRP   B  2 326 ? 24.994 -107.150 -25.197 1.00 35.69  ? 318  TRP   B CZ2    1 
ATOM   7298 C CZ3    . TRP   B  2 326 ? 23.310 -107.059 -23.455 1.00 35.32  ? 318  TRP   B CZ3    1 
ATOM   7299 C CH2    . TRP   B  2 326 ? 24.021 -106.464 -24.506 1.00 35.96  ? 318  TRP   B CH2    1 
ATOM   7300 N N      . ASP   B  2 327 ? 24.801 -114.773 -21.457 1.00 33.09  ? 319  ASP   B N      1 
ATOM   7301 C CA     . ASP   B  2 327 ? 24.752 -115.724 -20.344 1.00 32.32  ? 319  ASP   B CA     1 
ATOM   7302 C C      . ASP   B  2 327 ? 26.024 -116.615 -20.305 1.00 36.93  ? 319  ASP   B C      1 
ATOM   7303 O O      . ASP   B  2 327 ? 26.057 -117.591 -19.553 1.00 36.93  ? 319  ASP   B O      1 
ATOM   7304 C CB     . ASP   B  2 327 ? 23.483 -116.591 -20.460 1.00 33.02  ? 319  ASP   B CB     1 
ATOM   7305 C CG     . ASP   B  2 327 ? 23.372 -117.443 -21.726 1.00 36.25  ? 319  ASP   B CG     1 
ATOM   7306 O OD1    . ASP   B  2 327 ? 24.115 -117.173 -22.701 1.00 34.61  ? 319  ASP   B OD1    1 
ATOM   7307 O OD2    . ASP   B  2 327 ? 22.528 -118.358 -21.748 1.00 39.12  ? 319  ASP   B OD2    1 
ATOM   7308 N N      . HIS   B  2 328 ? 27.056 -116.271 -21.120 1.00 34.09  ? 320  HIS   B N      1 
ATOM   7309 C CA     . HIS   B  2 328 ? 28.353 -116.965 -21.252 1.00 34.33  ? 320  HIS   B CA     1 
ATOM   7310 C C      . HIS   B  2 328 ? 28.207 -118.431 -21.745 1.00 37.14  ? 320  HIS   B C      1 
ATOM   7311 O O      . HIS   B  2 328 ? 29.096 -119.257 -21.540 1.00 36.90  ? 320  HIS   B O      1 
ATOM   7312 C CB     . HIS   B  2 328 ? 29.169 -116.862 -19.949 1.00 35.14  ? 320  HIS   B CB     1 
ATOM   7313 C CG     . HIS   B  2 328 ? 30.648 -116.968 -20.140 1.00 38.70  ? 320  HIS   B CG     1 
ATOM   7314 N ND1    . HIS   B  2 328 ? 31.365 -115.982 -20.795 1.00 40.57  ? 320  HIS   B ND1    1 
ATOM   7315 C CD2    . HIS   B  2 328 ? 31.505 -117.920 -19.705 1.00 40.73  ? 320  HIS   B CD2    1 
ATOM   7316 C CE1    . HIS   B  2 328 ? 32.629 -116.375 -20.758 1.00 40.28  ? 320  HIS   B CE1    1 
ATOM   7317 N NE2    . HIS   B  2 328 ? 32.764 -117.531 -20.105 1.00 40.66  ? 320  HIS   B NE2    1 
ATOM   7318 N N      . GLN   B  2 329 ? 27.091 -118.728 -22.423 1.00 32.86  ? 321  GLN   B N      1 
ATOM   7319 C CA     . GLN   B  2 329 ? 26.795 -120.047 -22.965 1.00 32.57  ? 321  GLN   B CA     1 
ATOM   7320 C C      . GLN   B  2 329 ? 27.172 -120.158 -24.445 1.00 38.03  ? 321  GLN   B C      1 
ATOM   7321 O O      . GLN   B  2 329 ? 26.866 -119.260 -25.237 1.00 37.23  ? 321  GLN   B O      1 
ATOM   7322 C CB     . GLN   B  2 329 ? 25.308 -120.372 -22.803 1.00 33.22  ? 321  GLN   B CB     1 
ATOM   7323 C CG     . GLN   B  2 329 ? 24.972 -121.143 -21.541 1.00 43.86  ? 321  GLN   B CG     1 
ATOM   7324 C CD     . GLN   B  2 329 ? 23.706 -121.935 -21.723 1.00 59.80  ? 321  GLN   B CD     1 
ATOM   7325 O OE1    . GLN   B  2 329 ? 23.739 -123.149 -21.954 1.00 56.39  ? 321  GLN   B OE1    1 
ATOM   7326 N NE2    . GLN   B  2 329 ? 22.559 -121.260 -21.660 1.00 45.78  ? 321  GLN   B NE2    1 
ATOM   7327 N N      . VAL   B  2 330 ? 27.842 -121.268 -24.800 1.00 35.60  ? 322  VAL   B N      1 
ATOM   7328 C CA     . VAL   B  2 330 ? 28.198 -121.654 -26.171 1.00 35.51  ? 322  VAL   B CA     1 
ATOM   7329 C C      . VAL   B  2 330 ? 27.356 -122.914 -26.363 1.00 40.57  ? 322  VAL   B C      1 
ATOM   7330 O O      . VAL   B  2 330 ? 27.686 -123.956 -25.790 1.00 40.81  ? 322  VAL   B O      1 
ATOM   7331 C CB     . VAL   B  2 330 ? 29.718 -121.930 -26.384 1.00 39.07  ? 322  VAL   B CB     1 
ATOM   7332 C CG1    . VAL   B  2 330 ? 30.002 -122.381 -27.817 1.00 38.60  ? 322  VAL   B CG1    1 
ATOM   7333 C CG2    . VAL   B  2 330 ? 30.566 -120.715 -26.035 1.00 38.74  ? 322  VAL   B CG2    1 
ATOM   7334 N N      . VAL   B  2 331 ? 26.218 -122.796 -27.071 1.00 36.73  ? 323  VAL   B N      1 
ATOM   7335 C CA     . VAL   B  2 331 ? 25.295 -123.916 -27.270 1.00 35.99  ? 323  VAL   B CA     1 
ATOM   7336 C C      . VAL   B  2 331 ? 25.440 -124.498 -28.676 1.00 40.46  ? 323  VAL   B C      1 
ATOM   7337 O O      . VAL   B  2 331 ? 25.463 -123.753 -29.659 1.00 39.59  ? 323  VAL   B O      1 
ATOM   7338 C CB     . VAL   B  2 331 ? 23.820 -123.565 -26.922 1.00 39.53  ? 323  VAL   B CB     1 
ATOM   7339 C CG1    . VAL   B  2 331 ? 22.934 -124.813 -26.934 1.00 39.33  ? 323  VAL   B CG1    1 
ATOM   7340 C CG2    . VAL   B  2 331 ? 23.720 -122.858 -25.570 1.00 39.13  ? 323  VAL   B CG2    1 
ATOM   7341 N N      . HIS   B  2 332 ? 25.533 -125.837 -28.757 1.00 36.96  ? 324  HIS   B N      1 
ATOM   7342 C CA     . HIS   B  2 332 ? 25.647 -126.577 -30.012 1.00 36.58  ? 324  HIS   B CA     1 
ATOM   7343 C C      . HIS   B  2 332 ? 24.302 -127.221 -30.323 1.00 42.21  ? 324  HIS   B C      1 
ATOM   7344 O O      . HIS   B  2 332 ? 23.867 -128.125 -29.610 1.00 41.36  ? 324  HIS   B O      1 
ATOM   7345 C CB     . HIS   B  2 332 ? 26.779 -127.607 -29.922 1.00 36.60  ? 324  HIS   B CB     1 
ATOM   7346 C CG     . HIS   B  2 332 ? 28.098 -126.995 -29.574 1.00 39.26  ? 324  HIS   B CG     1 
ATOM   7347 N ND1    . HIS   B  2 332 ? 28.775 -126.183 -30.468 1.00 40.81  ? 324  HIS   B ND1    1 
ATOM   7348 C CD2    . HIS   B  2 332 ? 28.817 -127.085 -28.432 1.00 40.94  ? 324  HIS   B CD2    1 
ATOM   7349 C CE1    . HIS   B  2 332 ? 29.883 -125.812 -29.847 1.00 40.45  ? 324  HIS   B CE1    1 
ATOM   7350 N NE2    . HIS   B  2 332 ? 29.955 -126.333 -28.621 1.00 40.88  ? 324  HIS   B NE2    1 
ATOM   7351 N N      . HIS   B  2 333 ? 23.614 -126.702 -31.352 1.00 41.28  ? 325  HIS   B N      1 
ATOM   7352 C CA     . HIS   B  2 333 ? 22.284 -127.159 -31.764 1.00 42.32  ? 325  HIS   B CA     1 
ATOM   7353 C C      . HIS   B  2 333 ? 22.319 -128.144 -32.927 1.00 47.88  ? 325  HIS   B C      1 
ATOM   7354 O O      . HIS   B  2 333 ? 23.099 -127.969 -33.864 1.00 47.07  ? 325  HIS   B O      1 
ATOM   7355 C CB     . HIS   B  2 333 ? 21.387 -125.965 -32.142 1.00 43.27  ? 325  HIS   B CB     1 
ATOM   7356 C CG     . HIS   B  2 333 ? 21.202 -124.967 -31.041 1.00 46.67  ? 325  HIS   B CG     1 
ATOM   7357 N ND1    . HIS   B  2 333 ? 22.017 -123.853 -30.931 1.00 48.40  ? 325  HIS   B ND1    1 
ATOM   7358 C CD2    . HIS   B  2 333 ? 20.297 -124.948 -30.037 1.00 48.28  ? 325  HIS   B CD2    1 
ATOM   7359 C CE1    . HIS   B  2 333 ? 21.579 -123.193 -29.872 1.00 47.71  ? 325  HIS   B CE1    1 
ATOM   7360 N NE2    . HIS   B  2 333 ? 20.552 -123.817 -29.297 1.00 48.07  ? 325  HIS   B NE2    1 
ATOM   7361 N N      . VAL   B  2 334 ? 21.432 -129.152 -32.874 1.00 45.76  ? 326  VAL   B N      1 
ATOM   7362 C CA     . VAL   B  2 334 ? 21.248 -130.160 -33.915 1.00 46.30  ? 326  VAL   B CA     1 
ATOM   7363 C C      . VAL   B  2 334 ? 19.925 -129.799 -34.592 1.00 51.33  ? 326  VAL   B C      1 
ATOM   7364 O O      . VAL   B  2 334 ? 18.847 -130.023 -34.029 1.00 50.74  ? 326  VAL   B O      1 
ATOM   7365 C CB     . VAL   B  2 334 ? 21.285 -131.620 -33.363 1.00 50.43  ? 326  VAL   B CB     1 
ATOM   7366 C CG1    . VAL   B  2 334 ? 20.969 -132.640 -34.459 1.00 50.26  ? 326  VAL   B CG1    1 
ATOM   7367 C CG2    . VAL   B  2 334 ? 22.633 -131.934 -32.720 1.00 50.17  ? 326  VAL   B CG2    1 
ATOM   7368 N N      . VAL   B  2 335 ? 20.024 -129.172 -35.771 1.00 48.91  ? 327  VAL   B N      1 
ATOM   7369 C CA     . VAL   B  2 335 ? 18.873 -128.707 -36.544 1.00 49.22  ? 327  VAL   B CA     1 
ATOM   7370 C C      . VAL   B  2 335 ? 18.322 -129.854 -37.403 1.00 54.36  ? 327  VAL   B C      1 
ATOM   7371 O O      . VAL   B  2 335 ? 19.082 -130.424 -38.190 1.00 54.13  ? 327  VAL   B O      1 
ATOM   7372 C CB     . VAL   B  2 335 ? 19.228 -127.458 -37.400 1.00 53.12  ? 327  VAL   B CB     1 
ATOM   7373 C CG1    . VAL   B  2 335 ? 17.984 -126.862 -38.056 1.00 52.90  ? 327  VAL   B CG1    1 
ATOM   7374 C CG2    . VAL   B  2 335 ? 19.956 -126.402 -36.571 1.00 52.87  ? 327  VAL   B CG2    1 
ATOM   7375 N N      . PRO   B  2 336 ? 17.014 -130.201 -37.299 1.00 52.05  ? 328  PRO   B N      1 
ATOM   7376 C CA     . PRO   B  2 336 ? 16.482 -131.289 -38.134 1.00 56.22  ? 328  PRO   B CA     1 
ATOM   7377 C C      . PRO   B  2 336 ? 16.144 -130.815 -39.546 1.00 89.85  ? 328  PRO   B C      1 
ATOM   7378 O O      . PRO   B  2 336 ? 17.043 -130.614 -40.361 1.00 57.01  ? 328  PRO   B O      1 
ATOM   7379 C CB     . PRO   B  2 336 ? 15.232 -131.758 -37.370 1.00 57.41  ? 328  PRO   B CB     1 
ATOM   7380 C CG     . PRO   B  2 336 ? 15.078 -130.821 -36.189 1.00 60.53  ? 328  PRO   B CG     1 
ATOM   7381 C CD     . PRO   B  2 336 ? 15.958 -129.639 -36.436 1.00 55.10  ? 328  PRO   B CD     1 
HETATM 7382 N N      . SFG   C  3 .   ? 23.748 -36.094  -6.852  1.00 30.16  ? 701  SFG   A N      1 
HETATM 7383 C CA     . SFG   C  3 .   ? 24.271 -37.448  -6.602  1.00 29.98  ? 701  SFG   A CA     1 
HETATM 7384 C C      . SFG   C  3 .   ? 25.028 -37.987  -7.811  1.00 33.35  ? 701  SFG   A C      1 
HETATM 7385 O O      . SFG   C  3 .   ? 24.931 -37.512  -8.928  1.00 32.98  ? 701  SFG   A O      1 
HETATM 7386 O OXT    . SFG   C  3 .   ? 25.753 -39.025  -7.510  1.00 34.57  ? 701  SFG   A OXT    1 
HETATM 7387 C CB     . SFG   C  3 .   ? 23.112 -38.428  -6.212  1.00 25.99  ? 701  SFG   A CB     1 
HETATM 7388 C CG     . SFG   C  3 .   ? 22.008 -38.462  -7.273  1.00 24.66  ? 701  SFG   A CG     1 
HETATM 7389 C CD     . SFG   C  3 .   ? 20.861 -39.412  -6.931  1.00 22.23  ? 701  SFG   A CD     1 
HETATM 7390 N NE     . SFG   C  3 .   ? 20.530 -40.211  -8.118  1.00 20.46  ? 701  SFG   A NE     1 
HETATM 7391 C "C5'"  . SFG   C  3 .   ? 19.599 -38.693  -6.468  1.00 20.98  ? 701  SFG   A "C5'"  1 
HETATM 7392 C "C4'"  . SFG   C  3 .   ? 19.721 -37.956  -5.147  1.00 23.29  ? 701  SFG   A "C4'"  1 
HETATM 7393 O "O4'"  . SFG   C  3 .   ? 18.608 -37.044  -5.020  1.00 23.12  ? 701  SFG   A "O4'"  1 
HETATM 7394 C "C3'"  . SFG   C  3 .   ? 19.702 -38.844  -3.902  1.00 24.43  ? 701  SFG   A "C3'"  1 
HETATM 7395 O "O3'"  . SFG   C  3 .   ? 20.689 -38.461  -2.956  1.00 28.77  ? 701  SFG   A "O3'"  1 
HETATM 7396 C "C2'"  . SFG   C  3 .   ? 18.284 -38.661  -3.363  1.00 23.17  ? 701  SFG   A "C2'"  1 
HETATM 7397 O "O2'"  . SFG   C  3 .   ? 18.165 -38.810  -1.953  1.00 26.18  ? 701  SFG   A "O2'"  1 
HETATM 7398 C "C1'"  . SFG   C  3 .   ? 17.997 -37.221  -3.759  1.00 20.77  ? 701  SFG   A "C1'"  1 
HETATM 7399 N N9     . SFG   C  3 .   ? 16.583 -36.912  -3.893  1.00 16.50  ? 701  SFG   A N9     1 
HETATM 7400 C C8     . SFG   C  3 .   ? 15.653 -37.651  -4.575  1.00 17.22  ? 701  SFG   A C8     1 
HETATM 7401 N N7     . SFG   C  3 .   ? 14.447 -37.135  -4.564  1.00 19.11  ? 701  SFG   A N7     1 
HETATM 7402 C C5     . SFG   C  3 .   ? 14.593 -35.975  -3.818  1.00 17.90  ? 701  SFG   A C5     1 
HETATM 7403 C C6     . SFG   C  3 .   ? 13.682 -34.972  -3.440  1.00 19.46  ? 701  SFG   A C6     1 
HETATM 7404 N N6     . SFG   C  3 .   ? 12.396 -34.970  -3.798  1.00 21.56  ? 701  SFG   A N6     1 
HETATM 7405 N N1     . SFG   C  3 .   ? 14.152 -33.940  -2.704  1.00 21.14  ? 701  SFG   A N1     1 
HETATM 7406 C C2     . SFG   C  3 .   ? 15.452 -33.918  -2.382  1.00 20.91  ? 701  SFG   A C2     1 
HETATM 7407 N N3     . SFG   C  3 .   ? 16.402 -34.812  -2.675  1.00 17.31  ? 701  SFG   A N3     1 
HETATM 7408 C C4     . SFG   C  3 .   ? 15.905 -35.824  -3.399  1.00 15.94  ? 701  SFG   A C4     1 
HETATM 7409 H HN1    . SFG   C  3 .   ? 23.033 -35.813  -6.189  1.00 30.11  ? 701  SFG   A HN1    1 
HETATM 7410 H HN2    . SFG   C  3 .   ? 23.388 -35.993  -7.796  1.00 30.06  ? 701  SFG   A HN2    1 
HETATM 7411 H HA     . SFG   C  3 .   ? 24.953 -37.359  -5.757  1.00 29.69  ? 701  SFG   A HA     1 
HETATM 7412 H HXT    . SFG   C  3 .   ? 26.241 -39.385  -8.296  1.00 34.38  ? 701  SFG   A HXT    1 
HETATM 7413 H HB1    . SFG   C  3 .   ? 22.726 -38.149  -5.234  1.00 25.46  ? 701  SFG   A HB1    1 
HETATM 7414 H HB2    . SFG   C  3 .   ? 23.519 -39.429  -6.082  1.00 25.77  ? 701  SFG   A HB2    1 
HETATM 7415 H HG1    . SFG   C  3 .   ? 21.620 -37.460  -7.448  1.00 24.68  ? 701  SFG   A HG1    1 
HETATM 7416 H HG2    . SFG   C  3 .   ? 22.435 -38.726  -8.239  1.00 24.69  ? 701  SFG   A HG2    1 
HETATM 7417 H HD     . SFG   C  3 .   ? 21.168 -40.063  -6.114  1.00 22.10  ? 701  SFG   A HD     1 
HETATM 7418 H HNE1   . SFG   C  3 .   ? 20.995 -41.106  -8.224  1.00 20.42  ? 701  SFG   A HNE1   1 
HETATM 7419 H HNE2   . SFG   C  3 .   ? 20.393 -39.710  -8.990  1.00 19.72  ? 701  SFG   A HNE2   1 
HETATM 7420 H "H5'1" . SFG   C  3 .   ? 18.770 -39.397  -6.404  1.00 20.86  ? 701  SFG   A "H5'1" 1 
HETATM 7421 H "H5'2" . SFG   C  3 .   ? 19.258 -37.995  -7.229  1.00 21.09  ? 701  SFG   A "H5'2" 1 
HETATM 7422 H "H4'"  . SFG   C  3 .   ? 20.577 -37.284  -5.172  1.00 23.12  ? 701  SFG   A "H4'"  1 
HETATM 7423 H "H3'"  . SFG   C  3 .   ? 19.851 -39.888  -4.171  1.00 24.50  ? 701  SFG   A "H3'"  1 
HETATM 7424 H "HO3'" . SFG   C  3 .   ? 21.558 -38.457  -3.433  1.00 29.20  ? 701  SFG   A "HO3'" 1 
HETATM 7425 H "H2'"  . SFG   C  3 .   ? 17.591 -39.414  -3.733  1.00 23.62  ? 701  SFG   A "H2'"  1 
HETATM 7426 H "HO2'" . SFG   C  3 .   ? 19.057 -38.773  -1.519  1.00 26.55  ? 701  SFG   A "HO2'" 1 
HETATM 7427 H "H1'"  . SFG   C  3 .   ? 18.438 -36.494  -3.081  1.00 21.36  ? 701  SFG   A "H1'"  1 
HETATM 7428 H H8     . SFG   C  3 .   ? 15.892 -38.581  -5.088  1.00 17.28  ? 701  SFG   A H8     1 
HETATM 7429 H HN61   . SFG   C  3 .   ? 11.777 -34.221  -3.504  1.00 22.54  ? 701  SFG   A HN61   1 
HETATM 7430 H HN62   . SFG   C  3 .   ? 12.003 -35.700  -4.384  1.00 21.46  ? 701  SFG   A HN62   1 
HETATM 7431 H H2     . SFG   C  3 .   ? 15.775 -33.046  -1.816  1.00 20.92  ? 701  SFG   A H2     1 
HETATM 7432 C C1     . A1BLG D  4 .   ? 19.400 -47.252  -10.588 1.00 21.44  ? 702  A1BLG A C1     1 
HETATM 7433 C C2     . A1BLG D  4 .   ? 21.002 -48.896  -11.457 1.00 21.92  ? 702  A1BLG A C2     1 
HETATM 7434 C C3     . A1BLG D  4 .   ? 22.082 -49.873  -11.116 1.00 22.20  ? 702  A1BLG A C3     1 
HETATM 7435 C C4     . A1BLG D  4 .   ? 21.866 -50.766  -10.074 1.00 22.95  ? 702  A1BLG A C4     1 
HETATM 7436 C C5     . A1BLG D  4 .   ? 22.912 -51.560  -9.656  1.00 24.56  ? 702  A1BLG A C5     1 
HETATM 7437 C C6     . A1BLG D  4 .   ? 24.343 -50.665  -11.207 1.00 22.58  ? 702  A1BLG A C6     1 
HETATM 7438 C C7     . A1BLG D  4 .   ? 26.710 -51.429  -11.214 1.00 25.07  ? 702  A1BLG A C7     1 
HETATM 7439 N N1     . A1BLG D  4 .   ? 24.139 -51.522  -10.195 1.00 24.48  ? 702  A1BLG A N1     1 
HETATM 7440 N N2     . A1BLG D  4 .   ? 25.607 -50.632  -11.737 1.00 22.15  ? 702  A1BLG A N2     1 
HETATM 7441 N N3     . A1BLG D  4 .   ? 21.604 -44.178  -11.055 1.00 22.33  ? 702  A1BLG A N3     1 
HETATM 7442 C C8     . A1BLG D  4 .   ? 27.489 -50.853  -10.012 1.00 26.18  ? 702  A1BLG A C8     1 
HETATM 7443 O O1     . A1BLG D  4 .   ? 20.668 -48.701  -12.627 1.00 22.02  ? 702  A1BLG A O1     1 
HETATM 7444 C C11    . A1BLG D  4 .   ? 23.336 -49.833  -11.721 1.00 22.00  ? 702  A1BLG A C11    1 
HETATM 7445 C C10    . A1BLG D  4 .   ? 28.028 -51.443  -12.013 1.00 25.55  ? 702  A1BLG A C10    1 
HETATM 7446 C C9     . A1BLG D  4 .   ? 28.773 -51.379  -10.657 1.00 25.22  ? 702  A1BLG A C9     1 
HETATM 7447 N N      . A1BLG D  4 .   ? 20.424 -48.273  -10.426 1.00 19.35  ? 702  A1BLG A N      1 
HETATM 7448 C C      . A1BLG D  4 .   ? 19.963 -45.953  -11.157 1.00 21.94  ? 702  A1BLG A C      1 
HETATM 7449 O O      . A1BLG D  4 .   ? 18.909 -45.002  -11.305 1.00 22.57  ? 702  A1BLG A O      1 
HETATM 7450 C C12    . A1BLG D  4 .   ? 21.122 -45.367  -10.335 1.00 21.98  ? 702  A1BLG A C12    1 
HETATM 7451 C C20    . A1BLG D  4 .   ? 22.812 -43.624  -10.438 1.00 23.60  ? 702  A1BLG A C20    1 
HETATM 7452 C C19    . A1BLG D  4 .   ? 22.658 -43.359  -8.962  1.00 25.06  ? 702  A1BLG A C19    1 
HETATM 7453 C C14    . A1BLG D  4 .   ? 21.718 -44.084  -8.205  1.00 23.91  ? 702  A1BLG A C14    1 
HETATM 7454 C C13    . A1BLG D  4 .   ? 20.730 -44.993  -8.898  1.00 20.11  ? 702  A1BLG A C13    1 
HETATM 7455 C C18    . A1BLG D  4 .   ? 23.510 -42.465  -8.314  1.00 25.01  ? 702  A1BLG A C18    1 
HETATM 7456 C C17    . A1BLG D  4 .   ? 23.471 -42.319  -6.936  1.00 23.94  ? 702  A1BLG A C17    1 
HETATM 7457 C C16    . A1BLG D  4 .   ? 22.575 -43.053  -6.191  1.00 24.33  ? 702  A1BLG A C16    1 
HETATM 7458 C C15    . A1BLG D  4 .   ? 21.695 -43.921  -6.820  1.00 24.56  ? 702  A1BLG A C15    1 
HETATM 7459 H H4     . A1BLG D  4 .   ? 18.626 -47.635  -11.252 1.00 22.14  ? 702  A1BLG A H4     1 
HETATM 7460 H H3     . A1BLG D  4 .   ? 18.886 -47.045  -9.651  1.00 21.51  ? 702  A1BLG A H3     1 
HETATM 7461 H H6     . A1BLG D  4 .   ? 20.901 -50.843  -9.576  1.00 23.27  ? 702  A1BLG A H6     1 
HETATM 7462 H H7     . A1BLG D  4 .   ? 22.819 -52.262  -8.830  1.00 25.03  ? 702  A1BLG A H7     1 
HETATM 7463 H H9     . A1BLG D  4 .   ? 26.366 -52.443  -11.014 1.00 25.56  ? 702  A1BLG A H9     1 
HETATM 7464 H H8     . A1BLG D  4 .   ? 25.789 -50.036  -12.539 1.00 21.55  ? 702  A1BLG A H8     1 
HETATM 7465 H H25    . A1BLG D  4 .   ? 20.881 -43.468  -11.117 1.00 21.73  ? 702  A1BLG A H25    1 
HETATM 7466 H H11    . A1BLG D  4 .   ? 27.231 -51.305  -9.055  1.00 26.28  ? 702  A1BLG A H11    1 
HETATM 7467 H H10    . A1BLG D  4 .   ? 27.444 -49.775  -9.860  1.00 25.97  ? 702  A1BLG A H10    1 
HETATM 7468 H H16    . A1BLG D  4 .   ? 23.494 -49.169  -12.570 1.00 21.97  ? 702  A1BLG A H16    1 
HETATM 7469 H H14    . A1BLG D  4 .   ? 28.168 -50.591  -12.674 1.00 25.51  ? 702  A1BLG A H14    1 
HETATM 7470 H H15    . A1BLG D  4 .   ? 28.210 -52.331  -12.617 1.00 25.13  ? 702  A1BLG A H15    1 
HETATM 7471 H H13    . A1BLG D  4 .   ? 29.620 -50.696  -10.620 1.00 25.28  ? 702  A1BLG A H13    1 
HETATM 7472 H H12    . A1BLG D  4 .   ? 29.130 -52.335  -10.279 1.00 24.98  ? 702  A1BLG A H12    1 
HETATM 7473 H H5     . A1BLG D  4 .   ? 20.684 -48.463  -9.463  1.00 19.68  ? 702  A1BLG A H5     1 
HETATM 7474 H H      . A1BLG D  4 .   ? 20.343 -46.176  -12.152 1.00 21.64  ? 702  A1BLG A H      1 
HETATM 7475 H H2     . A1BLG D  4 .   ? 18.295 -45.399  -11.977 1.00 22.59  ? 702  A1BLG A H2     1 
HETATM 7476 H H1     . A1BLG D  4 .   ? 21.933 -46.091  -10.281 1.00 21.59  ? 702  A1BLG A H1     1 
HETATM 7477 H H23    . A1BLG D  4 .   ? 23.079 -42.706  -10.960 1.00 24.35  ? 702  A1BLG A H23    1 
HETATM 7478 H H24    . A1BLG D  4 .   ? 23.650 -44.300  -10.592 1.00 23.12  ? 702  A1BLG A H24    1 
HETATM 7479 H H17    . A1BLG D  4 .   ? 20.632 -45.887  -8.285  1.00 20.45  ? 702  A1BLG A H17    1 
HETATM 7480 H H18    . A1BLG D  4 .   ? 19.739 -44.542  -8.878  1.00 19.92  ? 702  A1BLG A H18    1 
HETATM 7481 H H22    . A1BLG D  4 .   ? 24.209 -41.869  -8.898  1.00 25.02  ? 702  A1BLG A H22    1 
HETATM 7482 H H21    . A1BLG D  4 .   ? 24.159 -41.635  -6.443  1.00 23.43  ? 702  A1BLG A H21    1 
HETATM 7483 H H20    . A1BLG D  4 .   ? 22.586 -42.976  -5.105  1.00 24.61  ? 702  A1BLG A H20    1 
HETATM 7484 H H19    . A1BLG D  4 .   ? 20.979 -44.489  -6.229  1.00 24.85  ? 702  A1BLG A H19    1 
HETATM 7485 C C1     . EDO   E  5 .   ? 19.966 -33.080  8.934   1.00 43.26  ? 703  EDO   A C1     1 
HETATM 7486 O O1     . EDO   E  5 .   ? 18.597 -33.302  8.663   1.00 46.09  ? 703  EDO   A O1     1 
HETATM 7487 C C2     . EDO   E  5 .   ? 20.642 -34.431  9.214   1.00 42.75  ? 703  EDO   A C2     1 
HETATM 7488 O O2     . EDO   E  5 .   ? 21.947 -34.510  8.674   1.00 40.60  ? 703  EDO   A O2     1 
HETATM 7489 H H11    . EDO   E  5 .   ? 20.471 -32.510  8.157   1.00 43.18  ? 703  EDO   A H11    1 
HETATM 7490 H H12    . EDO   E  5 .   ? 19.955 -32.466  9.833   1.00 43.15  ? 703  EDO   A H12    1 
HETATM 7491 H HO1    . EDO   E  5 .   ? 18.140 -33.449  9.533   1.00 46.45  ? 703  EDO   A HO1    1 
HETATM 7492 H H21    . EDO   E  5 .   ? 20.771 -34.563  10.286  1.00 43.14  ? 703  EDO   A H21    1 
HETATM 7493 H H22    . EDO   E  5 .   ? 20.012 -35.251  8.878   1.00 43.01  ? 703  EDO   A H22    1 
HETATM 7494 H HO2    . EDO   E  5 .   ? 22.591 -34.446  9.426   1.00 40.43  ? 703  EDO   A HO2    1 
HETATM 7495 C C1     . EDO   F  5 .   ? 25.693 -78.500  -35.720 1.00 35.53  ? 704  EDO   A C1     1 
HETATM 7496 O O1     . EDO   F  5 .   ? 24.691 -79.462  -35.860 1.00 37.62  ? 704  EDO   A O1     1 
HETATM 7497 C C2     . EDO   F  5 .   ? 25.873 -77.637  -37.010 1.00 36.40  ? 704  EDO   A C2     1 
HETATM 7498 O O2     . EDO   F  5 .   ? 26.863 -76.633  -36.840 1.00 34.84  ? 704  EDO   A O2     1 
HETATM 7499 H H11    . EDO   F  5 .   ? 25.551 -77.857  -34.856 1.00 35.36  ? 704  EDO   A H11    1 
HETATM 7500 H H12    . EDO   F  5 .   ? 26.548 -79.135  -35.503 1.00 35.49  ? 704  EDO   A H12    1 
HETATM 7501 H HO1    . EDO   F  5 .   ? 25.052 -80.187  -36.436 1.00 37.82  ? 704  EDO   A HO1    1 
HETATM 7502 H H21    . EDO   F  5 .   ? 26.203 -78.235  -37.859 1.00 36.37  ? 704  EDO   A H21    1 
HETATM 7503 H H22    . EDO   F  5 .   ? 24.928 -77.174  -37.277 1.00 36.49  ? 704  EDO   A H22    1 
HETATM 7504 H HO2    . EDO   F  5 .   ? 27.196 -76.390  -37.743 1.00 34.77  ? 704  EDO   A HO2    1 
HETATM 7505 C C1     . EDO   G  5 .   ? 7.656  -71.220  -31.322 1.00 43.62  ? 705  EDO   A C1     1 
HETATM 7506 O O1     . EDO   G  5 .   ? 7.191  -70.574  -30.151 1.00 43.63  ? 705  EDO   A O1     1 
HETATM 7507 C C2     . EDO   G  5 .   ? 8.260  -70.187  -32.320 1.00 42.64  ? 705  EDO   A C2     1 
HETATM 7508 O O2     . EDO   G  5 .   ? 9.079  -69.267  -31.632 1.00 39.85  ? 705  EDO   A O2     1 
HETATM 7509 H H11    . EDO   G  5 .   ? 8.370  -72.009  -31.090 1.00 43.92  ? 705  EDO   A H11    1 
HETATM 7510 H H12    . EDO   G  5 .   ? 6.776  -71.703  -31.745 1.00 43.50  ? 705  EDO   A H12    1 
HETATM 7511 H HO1    . EDO   G  5 .   ? 6.595  -71.215  -29.681 1.00 43.53  ? 705  EDO   A HO1    1 
HETATM 7512 H H21    . EDO   G  5 .   ? 8.942  -70.678  -33.013 1.00 43.16  ? 705  EDO   A H21    1 
HETATM 7513 H H22    . EDO   G  5 .   ? 7.496  -69.709  -32.930 1.00 42.60  ? 705  EDO   A H22    1 
HETATM 7514 H HO2    . EDO   G  5 .   ? 9.377  -68.589  -32.294 1.00 39.83  ? 705  EDO   A HO2    1 
HETATM 7515 C C1     . EDO   H  5 .   ? 27.486 -49.022  3.621   1.00 35.72  ? 706  EDO   A C1     1 
HETATM 7516 O O1     . EDO   H  5 .   ? 26.402 -48.251  3.198   1.00 31.44  ? 706  EDO   A O1     1 
HETATM 7517 C C2     . EDO   H  5 .   ? 28.646 -48.061  4.008   1.00 36.67  ? 706  EDO   A C2     1 
HETATM 7518 O O2     . EDO   H  5 .   ? 29.736 -48.748  4.594   1.00 35.63  ? 706  EDO   A O2     1 
HETATM 7519 H H11    . EDO   H  5 .   ? 27.234 -49.712  4.423   1.00 36.60  ? 706  EDO   A H11    1 
HETATM 7520 H H12    . EDO   H  5 .   ? 27.711 -49.649  2.762   1.00 36.11  ? 706  EDO   A H12    1 
HETATM 7521 H HO1    . EDO   H  5 .   ? 26.096 -47.719  3.978   1.00 30.73  ? 706  EDO   A HO1    1 
HETATM 7522 H H21    . EDO   H  5 .   ? 29.052 -47.588  3.116   1.00 37.49  ? 706  EDO   A H21    1 
HETATM 7523 H H22    . EDO   H  5 .   ? 28.295 -47.256  4.650   1.00 36.78  ? 706  EDO   A H22    1 
HETATM 7524 H HO2    . EDO   H  5 .   ? 30.313 -48.065  5.026   1.00 35.49  ? 706  EDO   A HO2    1 
HETATM 7525 C C1     . EDO   I  5 .   ? 12.378 -74.809  -11.345 1.00 44.08  ? 707  EDO   A C1     1 
HETATM 7526 O O1     . EDO   I  5 .   ? 11.039 -74.783  -11.791 1.00 45.59  ? 707  EDO   A O1     1 
HETATM 7527 C C2     . EDO   I  5 .   ? 12.752 -76.206  -10.748 1.00 44.99  ? 707  EDO   A C2     1 
HETATM 7528 O O2     . EDO   I  5 .   ? 12.310 -77.290  -11.574 1.00 45.11  ? 707  EDO   A O2     1 
HETATM 7529 H H11    . EDO   I  5 .   ? 13.070 -74.496  -12.122 1.00 43.48  ? 707  EDO   A H11    1 
HETATM 7530 H H12    . EDO   I  5 .   ? 12.418 -74.042  -10.572 1.00 44.18  ? 707  EDO   A H12    1 
HETATM 7531 H HO1    . EDO   I  5 .   ? 10.474 -74.492  -11.028 1.00 45.76  ? 707  EDO   A HO1    1 
HETATM 7532 H H21    . EDO   I  5 .   ? 13.832 -76.329  -10.692 1.00 44.54  ? 707  EDO   A H21    1 
HETATM 7533 H H22    . EDO   I  5 .   ? 12.378 -76.296  -9.729  1.00 45.39  ? 707  EDO   A H22    1 
HETATM 7534 H HO2    . EDO   I  5 .   ? 12.392 -78.123  -11.039 1.00 44.82  ? 707  EDO   A HO2    1 
HETATM 7535 C C1     . EDO   J  5 .   ? 13.647 -68.242  -26.315 1.00 62.89  ? 708  EDO   A C1     1 
HETATM 7536 O O1     . EDO   J  5 .   ? 12.541 -67.467  -26.648 1.00 66.28  ? 708  EDO   A O1     1 
HETATM 7537 C C2     . EDO   J  5 .   ? 14.675 -67.403  -25.543 1.00 60.27  ? 708  EDO   A C2     1 
HETATM 7538 O O2     . EDO   J  5 .   ? 15.444 -66.616  -26.405 1.00 58.34  ? 708  EDO   A O2     1 
HETATM 7539 H H11    . EDO   J  5 .   ? 13.355 -69.123  -25.750 1.00 62.62  ? 708  EDO   A H11    1 
HETATM 7540 H H12    . EDO   J  5 .   ? 14.024 -68.595  -27.271 1.00 62.98  ? 708  EDO   A H12    1 
HETATM 7541 H HO1    . EDO   J  5 .   ? 11.768 -68.007  -26.337 1.00 66.49  ? 708  EDO   A HO1    1 
HETATM 7542 H H21    . EDO   J  5 .   ? 14.150 -66.675  -24.927 1.00 60.47  ? 708  EDO   A H21    1 
HETATM 7543 H H22    . EDO   J  5 .   ? 15.292 -68.022  -24.894 1.00 60.32  ? 708  EDO   A H22    1 
HETATM 7544 H HO2    . EDO   J  5 .   ? 15.734 -65.812  -25.902 1.00 58.21  ? 708  EDO   A HO2    1 
HETATM 7545 C C1     . EDO   K  5 .   ? 21.605 -91.962  -29.684 1.00 47.44  ? 709  EDO   A C1     1 
HETATM 7546 O O1     . EDO   K  5 .   ? 22.700 -91.119  -29.402 1.00 46.26  ? 709  EDO   A O1     1 
HETATM 7547 C C2     . EDO   K  5 .   ? 20.558 -91.806  -28.577 1.00 45.48  ? 709  EDO   A C2     1 
HETATM 7548 O O2     . EDO   K  5 .   ? 19.419 -92.583  -28.885 1.00 43.45  ? 709  EDO   A O2     1 
HETATM 7549 H H11    . EDO   K  5 .   ? 21.178 -91.779  -30.669 1.00 48.04  ? 709  EDO   A H11    1 
HETATM 7550 H H12    . EDO   K  5 .   ? 22.016 -92.970  -29.696 1.00 47.75  ? 709  EDO   A H12    1 
HETATM 7551 H HO1    . EDO   K  5 .   ? 23.111 -91.444  -28.559 1.00 45.91  ? 709  EDO   A HO1    1 
HETATM 7552 H H21    . EDO   K  5 .   ? 20.934 -92.202  -27.636 1.00 45.71  ? 709  EDO   A H21    1 
HETATM 7553 H H22    . EDO   K  5 .   ? 20.320 -90.760  -28.396 1.00 45.55  ? 709  EDO   A H22    1 
HETATM 7554 H HO2    . EDO   K  5 .   ? 19.079 -92.279  -29.767 1.00 43.35  ? 709  EDO   A HO2    1 
HETATM 7555 C C1     . EDO   L  5 .   ? 13.395 -76.908  -18.862 1.00 45.23  ? 710  EDO   A C1     1 
HETATM 7556 O O1     . EDO   L  5 .   ? 12.003 -77.163  -18.784 1.00 46.09  ? 710  EDO   A O1     1 
HETATM 7557 C C2     . EDO   L  5 .   ? 13.747 -75.409  -19.009 1.00 41.18  ? 710  EDO   A C2     1 
HETATM 7558 O O2     . EDO   L  5 .   ? 15.044 -75.238  -19.448 1.00 39.63  ? 710  EDO   A O2     1 
HETATM 7559 H H11    . EDO   L  5 .   ? 13.887 -77.306  -17.978 1.00 45.66  ? 710  EDO   A H11    1 
HETATM 7560 H H12    . EDO   L  5 .   ? 13.731 -77.478  -19.726 1.00 45.15  ? 710  EDO   A H12    1 
HETATM 7561 H HO1    . EDO   L  5 .   ? 11.553 -76.608  -19.470 1.00 46.13  ? 710  EDO   A HO1    1 
HETATM 7562 H H21    . EDO   L  5 .   ? 13.115 -74.938  -19.758 1.00 41.81  ? 710  EDO   A H21    1 
HETATM 7563 H H22    . EDO   L  5 .   ? 13.622 -74.848  -18.087 1.00 41.21  ? 710  EDO   A H22    1 
HETATM 7564 H HO2    . EDO   L  5 .   ? 15.611 -75.113  -18.643 1.00 39.22  ? 710  EDO   A HO2    1 
HETATM 7565 C C1     . EDO   M  5 .   ? 14.855 -67.173  -29.373 1.00 32.86  ? 711  EDO   A C1     1 
HETATM 7566 O O1     . EDO   M  5 .   ? 14.634 -67.960  -30.530 1.00 32.01  ? 711  EDO   A O1     1 
HETATM 7567 C C2     . EDO   M  5 .   ? 15.732 -65.955  -29.726 1.00 31.88  ? 711  EDO   A C2     1 
HETATM 7568 O O2     . EDO   M  5 .   ? 15.072 -65.221  -30.725 1.00 32.10  ? 711  EDO   A O2     1 
HETATM 7569 H H11    . EDO   M  5 .   ? 13.928 -66.876  -28.885 1.00 32.37  ? 711  EDO   A H11    1 
HETATM 7570 H H12    . EDO   M  5 .   ? 15.392 -67.829  -28.691 1.00 32.83  ? 711  EDO   A H12    1 
HETATM 7571 H HO1    . EDO   M  5 .   ? 13.941 -67.479  -31.053 1.00 32.30  ? 711  EDO   A HO1    1 
HETATM 7572 H H21    . EDO   M  5 .   ? 15.839 -65.279  -28.879 1.00 31.79  ? 711  EDO   A H21    1 
HETATM 7573 H H22    . EDO   M  5 .   ? 16.734 -66.259  -30.024 1.00 32.06  ? 711  EDO   A H22    1 
HETATM 7574 H HO2    . EDO   M  5 .   ? 14.704 -64.402  -30.300 1.00 32.22  ? 711  EDO   A HO2    1 
HETATM 7575 C C1     . EDO   N  5 .   ? 16.786 -97.333  -9.361  1.00 40.40  ? 712  EDO   A C1     1 
HETATM 7576 O O1     . EDO   N  5 .   ? 16.032 -97.338  -10.553 1.00 43.91  ? 712  EDO   A O1     1 
HETATM 7577 C C2     . EDO   N  5 .   ? 17.975 -96.384  -9.542  1.00 38.20  ? 712  EDO   A C2     1 
HETATM 7578 O O2     . EDO   N  5 .   ? 19.109 -96.937  -10.179 1.00 32.06  ? 712  EDO   A O2     1 
HETATM 7579 H H11    . EDO   N  5 .   ? 16.194 -97.057  -8.490  1.00 40.20  ? 712  EDO   A H11    1 
HETATM 7580 H H12    . EDO   N  5 .   ? 17.109 -98.362  -9.219  1.00 40.67  ? 712  EDO   A H12    1 
HETATM 7581 H HO1    . EDO   N  5 .   ? 15.503 -96.497  -10.574 1.00 43.73  ? 712  EDO   A HO1    1 
HETATM 7582 H H21    . EDO   N  5 .   ? 17.685 -95.612  -10.250 1.00 38.81  ? 712  EDO   A H21    1 
HETATM 7583 H H22    . EDO   N  5 .   ? 18.222 -95.909  -8.594  1.00 38.82  ? 712  EDO   A H22    1 
HETATM 7584 H HO2    . EDO   N  5 .   ? 19.795 -96.221  -10.228 1.00 30.99  ? 712  EDO   A HO2    1 
HETATM 7585 C C1     . EDO   O  5 .   ? 23.629 -88.747  -24.229 1.00 54.67  ? 713  EDO   A C1     1 
HETATM 7586 O O1     . EDO   O  5 .   ? 24.629 -89.715  -24.031 1.00 55.10  ? 713  EDO   A O1     1 
HETATM 7587 C C2     . EDO   O  5 .   ? 24.215 -87.469  -24.862 1.00 54.37  ? 713  EDO   A C2     1 
HETATM 7588 O O2     . EDO   O  5 .   ? 25.638 -87.455  -24.794 1.00 53.46  ? 713  EDO   A O2     1 
HETATM 7589 H H11    . EDO   O  5 .   ? 22.804 -89.125  -24.829 1.00 54.73  ? 713  EDO   A H11    1 
HETATM 7590 H H12    . EDO   O  5 .   ? 23.229 -88.554  -23.236 1.00 54.64  ? 713  EDO   A H12    1 
HETATM 7591 H HO1    . EDO   O  5 .   ? 24.207 -90.484  -23.567 1.00 55.16  ? 713  EDO   A HO1    1 
HETATM 7592 H H21    . EDO   O  5 .   ? 23.978 -87.436  -25.924 1.00 54.57  ? 713  EDO   A H21    1 
HETATM 7593 H H22    . EDO   O  5 .   ? 23.774 -86.580  -24.412 1.00 54.40  ? 713  EDO   A H22    1 
HETATM 7594 H HO2    . EDO   O  5 .   ? 25.981 -87.689  -25.696 1.00 53.35  ? 713  EDO   A HO2    1 
HETATM 7595 C C1     . EDO   P  5 .   ? 23.768 -68.308  -29.957 1.00 55.79  ? 714  EDO   A C1     1 
HETATM 7596 O O1     . EDO   P  5 .   ? 23.168 -67.586  -31.016 1.00 55.17  ? 714  EDO   A O1     1 
HETATM 7597 C C2     . EDO   P  5 .   ? 25.029 -67.554  -29.478 1.00 55.97  ? 714  EDO   A C2     1 
HETATM 7598 O O2     . EDO   P  5 .   ? 25.408 -68.051  -28.212 1.00 56.30  ? 714  EDO   A O2     1 
HETATM 7599 H H11    . EDO   P  5 .   ? 23.079 -68.491  -29.134 1.00 55.95  ? 714  EDO   A H11    1 
HETATM 7600 H H12    . EDO   P  5 .   ? 24.026 -69.275  -30.386 1.00 55.64  ? 714  EDO   A H12    1 
HETATM 7601 H HO1    . EDO   P  5 .   ? 22.184 -67.650  -30.895 1.00 55.16  ? 714  EDO   A HO1    1 
HETATM 7602 H H21    . EDO   P  5 .   ? 25.880 -67.759  -30.126 1.00 55.96  ? 714  EDO   A H21    1 
HETATM 7603 H H22    . EDO   P  5 .   ? 24.876 -66.476  -29.476 1.00 56.03  ? 714  EDO   A H22    1 
HETATM 7604 H HO2    . EDO   P  5 .   ? 26.227 -67.562  -27.938 1.00 56.44  ? 714  EDO   A HO2    1 
HETATM 7605 C C1     . EDO   Q  5 .   ? 2.709  -31.822  -19.873 1.00 81.96  ? 715  EDO   A C1     1 
HETATM 7606 O O1     . EDO   Q  5 .   ? 2.362  -31.177  -18.666 1.00 81.83  ? 715  EDO   A O1     1 
HETATM 7607 C C2     . EDO   Q  5 .   ? 1.901  -31.229  -21.034 1.00 82.56  ? 715  EDO   A C2     1 
HETATM 7608 O O2     . EDO   Q  5 .   ? 2.212  -31.955  -22.210 1.00 83.19  ? 715  EDO   A O2     1 
HETATM 7609 H H11    . EDO   Q  5 .   ? 3.778  -31.787  -20.079 1.00 81.96  ? 715  EDO   A H11    1 
HETATM 7610 H H12    . EDO   Q  5 .   ? 2.446  -32.867  -19.715 1.00 82.01  ? 715  EDO   A H12    1 
HETATM 7611 H HO1    . EDO   Q  5 .   ? 2.881  -31.611  -17.939 1.00 81.76  ? 715  EDO   A HO1    1 
HETATM 7612 H H21    . EDO   Q  5 .   ? 0.832  -31.371  -20.883 1.00 82.59  ? 715  EDO   A H21    1 
HETATM 7613 H H22    . EDO   Q  5 .   ? 2.076  -30.159  -21.137 1.00 82.53  ? 715  EDO   A H22    1 
HETATM 7614 H HO2    . EDO   Q  5 .   ? 3.162  -31.767  -22.429 1.00 83.21  ? 715  EDO   A HO2    1 
HETATM 7615 C C1     . EDO   R  5 .   ? -0.998 -36.245  -12.940 1.00 75.33  ? 716  EDO   A C1     1 
HETATM 7616 O O1     . EDO   R  5 .   ? -2.369 -36.024  -13.224 1.00 74.90  ? 716  EDO   A O1     1 
HETATM 7617 C C2     . EDO   R  5 .   ? -0.270 -34.885  -12.851 1.00 75.26  ? 716  EDO   A C2     1 
HETATM 7618 O O2     . EDO   R  5 .   ? 1.129  -35.095  -12.793 1.00 74.84  ? 716  EDO   A O2     1 
HETATM 7619 H H11    . EDO   R  5 .   ? -0.850 -36.829  -12.033 1.00 75.53  ? 716  EDO   A H11    1 
HETATM 7620 H H12    . EDO   R  5 .   ? -0.624 -36.843  -13.770 1.00 75.36  ? 716  EDO   A H12    1 
HETATM 7621 H HO1    . EDO   R  5 .   ? -2.774 -35.619  -12.414 1.00 74.90  ? 716  EDO   A HO1    1 
HETATM 7622 H H21    . EDO   R  5 .   ? -0.430 -34.293  -13.750 1.00 75.27  ? 716  EDO   A H21    1 
HETATM 7623 H H22    . EDO   R  5 .   ? -0.640 -34.295  -12.015 1.00 75.41  ? 716  EDO   A H22    1 
HETATM 7624 H HO2    . EDO   R  5 .   ? 1.441  -34.730  -11.924 1.00 74.91  ? 716  EDO   A HO2    1 
HETATM 7625 C C1     . EDO   S  5 .   ? 32.858 -82.877  -2.774  1.00 75.05  ? 717  EDO   A C1     1 
HETATM 7626 O O1     . EDO   S  5 .   ? 32.236 -81.700  -3.270  1.00 75.13  ? 717  EDO   A O1     1 
HETATM 7627 C C2     . EDO   S  5 .   ? 32.513 -83.096  -1.282  1.00 74.89  ? 717  EDO   A C2     1 
HETATM 7628 O O2     . EDO   S  5 .   ? 33.097 -84.313  -0.844  1.00 74.75  ? 717  EDO   A O2     1 
HETATM 7629 H H11    . EDO   S  5 .   ? 32.610 -83.758  -3.362  1.00 74.96  ? 717  EDO   A H11    1 
HETATM 7630 H H12    . EDO   S  5 .   ? 33.925 -82.700  -2.901  1.00 75.16  ? 717  EDO   A H12    1 
HETATM 7631 H HO1    . EDO   S  5 .   ? 31.262 -81.884  -3.329  1.00 75.19  ? 717  EDO   A HO1    1 
HETATM 7632 H H21    . EDO   S  5 .   ? 32.967 -82.329  -0.657  1.00 74.92  ? 717  EDO   A H21    1 
HETATM 7633 H H22    . EDO   S  5 .   ? 31.438 -83.058  -1.111  1.00 74.86  ? 717  EDO   A H22    1 
HETATM 7634 H HO2    . EDO   S  5 .   ? 34.082 -84.191  -0.867  1.00 74.76  ? 717  EDO   A HO2    1 
HETATM 7635 C C1     . EDO   T  5 .   ? 31.869 -46.016  2.783   1.00 39.49  ? 718  EDO   A C1     1 
HETATM 7636 O O1     . EDO   T  5 .   ? 30.713 -45.869  3.583   1.00 37.72  ? 718  EDO   A O1     1 
HETATM 7637 C C2     . EDO   T  5 .   ? 32.077 -44.760  1.947   1.00 40.39  ? 718  EDO   A C2     1 
HETATM 7638 O O2     . EDO   T  5 .   ? 32.270 -43.675  2.827   1.00 40.20  ? 718  EDO   A O2     1 
HETATM 7639 H H11    . EDO   T  5 .   ? 32.757 -46.222  3.378   1.00 39.77  ? 718  EDO   A H11    1 
HETATM 7640 H H12    . EDO   T  5 .   ? 31.677 -46.882  2.152   1.00 39.33  ? 718  EDO   A H12    1 
HETATM 7641 H HO1    . EDO   T  5 .   ? 30.976 -45.368  4.399   1.00 37.61  ? 718  EDO   A HO1    1 
HETATM 7642 H H21    . EDO   T  5 .   ? 32.997 -44.820  1.368   1.00 40.65  ? 718  EDO   A H21    1 
HETATM 7643 H H22    . EDO   T  5 .   ? 31.257 -44.607  1.247   1.00 40.44  ? 718  EDO   A H22    1 
HETATM 7644 H HO2    . EDO   T  5 .   ? 33.146 -43.815  3.272   1.00 40.32  ? 718  EDO   A HO2    1 
HETATM 7645 C C1     . EDO   U  5 .   ? -5.416 -62.657  -30.196 1.00 84.32  ? 719  EDO   A C1     1 
HETATM 7646 O O1     . EDO   U  5 .   ? -5.034 -62.232  -28.897 1.00 83.13  ? 719  EDO   A O1     1 
HETATM 7647 C C2     . EDO   U  5 .   ? -5.074 -61.565  -31.248 1.00 84.99  ? 719  EDO   A C2     1 
HETATM 7648 O O2     . EDO   U  5 .   ? -5.236 -62.099  -32.548 1.00 85.62  ? 719  EDO   A O2     1 
HETATM 7649 H H11    . EDO   U  5 .   ? -4.982 -63.618  -30.469 1.00 84.46  ? 719  EDO   A H11    1 
HETATM 7650 H H12    . EDO   U  5 .   ? -6.493 -62.805  -30.127 1.00 84.44  ? 719  EDO   A H12    1 
HETATM 7651 H HO1    . EDO   U  5 .   ? -5.533 -62.793  -28.248 1.00 83.07  ? 719  EDO   A HO1    1 
HETATM 7652 H H21    . EDO   U  5 .   ? -5.777 -60.735  -31.208 1.00 85.16  ? 719  EDO   A H21    1 
HETATM 7653 H H22    . EDO   U  5 .   ? -4.084 -61.142  -31.092 1.00 84.95  ? 719  EDO   A H22    1 
HETATM 7654 H HO2    . EDO   U  5 .   ? -4.359 -62.475  -32.823 1.00 85.67  ? 719  EDO   A HO2    1 
HETATM 7655 S S      . SO4   V  6 .   ? 31.712 -36.337  -2.728  1.00 79.34  ? 720  SO4   A S      1 
HETATM 7656 O O1     . SO4   V  6 .   ? 32.673 -36.714  -3.769  1.00 79.95  ? 720  SO4   A O1     1 
HETATM 7657 O O2     . SO4   V  6 .   ? 30.388 -36.622  -3.211  1.00 79.38  ? 720  SO4   A O2     1 
HETATM 7658 O O3     . SO4   V  6 .   ? 31.940 -37.127  -1.511  1.00 79.25  ? 720  SO4   A O3     1 
HETATM 7659 O O4     . SO4   V  6 .   ? 31.834 -34.903  -2.426  1.00 79.04  ? 720  SO4   A O4     1 
HETATM 7660 S S      . SO4   W  6 .   ? 31.022 -79.600  -14.267 1.00 84.61  ? 721  SO4   A S      1 
HETATM 7661 O O1     . SO4   W  6 .   ? 32.213 -78.818  -14.605 1.00 84.61  ? 721  SO4   A O1     1 
HETATM 7662 O O2     . SO4   W  6 .   ? 29.865 -79.150  -15.039 1.00 82.95  ? 721  SO4   A O2     1 
HETATM 7663 O O3     . SO4   W  6 .   ? 31.285 -81.010  -14.545 1.00 84.60  ? 721  SO4   A O3     1 
HETATM 7664 O O4     . SO4   W  6 .   ? 30.736 -79.427  -12.840 1.00 86.30  ? 721  SO4   A O4     1 
HETATM 7665 S S      . SO4   X  6 .   ? 14.656 -58.981  -6.601  1.00 151.60 ? 722  SO4   A S      1 
HETATM 7666 O O1     . SO4   X  6 .   ? 14.486 -58.170  -7.805  1.00 151.69 ? 722  SO4   A O1     1 
HETATM 7667 O O2     . SO4   X  6 .   ? 13.341 -59.319  -6.055  1.00 151.52 ? 722  SO4   A O2     1 
HETATM 7668 O O3     . SO4   X  6 .   ? 15.375 -60.210  -6.938  1.00 151.68 ? 722  SO4   A O3     1 
HETATM 7669 O O4     . SO4   X  6 .   ? 15.428 -58.227  -5.612  1.00 151.57 ? 722  SO4   A O4     1 
HETATM 7670 S S      . SO4   Y  6 .   ? 21.119 -58.766  -29.089 1.00 115.42 ? 723  SO4   A S      1 
HETATM 7671 O O1     . SO4   Y  6 .   ? 21.496 -57.352  -29.078 1.00 115.72 ? 723  SO4   A O1     1 
HETATM 7672 O O2     . SO4   Y  6 .   ? 20.130 -59.002  -30.140 1.00 114.80 ? 723  SO4   A O2     1 
HETATM 7673 O O3     . SO4   Y  6 .   ? 22.302 -59.587  -29.339 1.00 115.98 ? 723  SO4   A O3     1 
HETATM 7674 O O4     . SO4   Y  6 .   ? 20.559 -59.121  -27.789 1.00 115.50 ? 723  SO4   A O4     1 
HETATM 7675 S S      . SO4   Z  6 .   ? 2.545  -52.367  -4.009  1.00 129.24 ? 724  SO4   A S      1 
HETATM 7676 O O1     . SO4   Z  6 .   ? 3.938  -52.711  -3.729  1.00 129.24 ? 724  SO4   A O1     1 
HETATM 7677 O O2     . SO4   Z  6 .   ? 2.369  -52.176  -5.438  1.00 129.05 ? 724  SO4   A O2     1 
HETATM 7678 O O3     . SO4   Z  6 .   ? 1.673  -53.452  -3.555  1.00 129.23 ? 724  SO4   A O3     1 
HETATM 7679 O O4     . SO4   Z  6 .   ? 2.198  -51.124  -3.319  1.00 129.56 ? 724  SO4   A O4     1 
HETATM 7680 S S      . SO4   AA 6 .   ? 24.396 -50.804  -5.972  1.00 139.57 ? 725  SO4   A S      1 
HETATM 7681 O O1     . SO4   AA 6 .   ? 25.213 -50.036  -6.905  1.00 139.64 ? 725  SO4   A O1     1 
HETATM 7682 O O2     . SO4   AA 6 .   ? 23.013 -50.323  -6.028  1.00 139.52 ? 725  SO4   A O2     1 
HETATM 7683 O O3     . SO4   AA 6 .   ? 24.448 -52.219  -6.345  1.00 139.61 ? 725  SO4   A O3     1 
HETATM 7684 O O4     . SO4   AA 6 .   ? 24.911 -50.632  -4.614  1.00 139.50 ? 725  SO4   A O4     1 
HETATM 7685 S S      . SO4   BA 6 .   ? 11.520 -25.450  4.661   1.00 123.38 ? 726  SO4   A S      1 
HETATM 7686 O O1     . SO4   BA 6 .   ? 12.256 -24.534  3.790   1.00 123.19 ? 726  SO4   A O1     1 
HETATM 7687 O O2     . SO4   BA 6 .   ? 11.260 -26.704  3.954   1.00 123.31 ? 726  SO4   A O2     1 
HETATM 7688 O O3     . SO4   BA 6 .   ? 12.317 -25.729  5.855   1.00 123.50 ? 726  SO4   A O3     1 
HETATM 7689 O O4     . SO4   BA 6 .   ? 10.249 -24.833  5.051   1.00 123.57 ? 726  SO4   A O4     1 
HETATM 7690 C C1     . PEG   CA 7 .   ? 6.239  -83.511  -29.674 1.00 51.14  ? 727  PEG   A C1     1 
HETATM 7691 O O1     . PEG   CA 7 .   ? 6.462  -82.887  -30.941 1.00 51.29  ? 727  PEG   A O1     1 
HETATM 7692 C C2     . PEG   CA 7 .   ? 6.578  -82.602  -28.527 1.00 49.27  ? 727  PEG   A C2     1 
HETATM 7693 O O2     . PEG   CA 7 .   ? 7.732  -83.059  -27.829 1.00 47.98  ? 727  PEG   A O2     1 
HETATM 7694 C C3     . PEG   CA 7 .   ? 8.942  -82.877  -28.544 1.00 45.54  ? 727  PEG   A C3     1 
HETATM 7695 C C4     . PEG   CA 7 .   ? 10.063 -82.517  -27.631 1.00 42.99  ? 727  PEG   A C4     1 
HETATM 7696 O O4     . PEG   CA 7 .   ? 11.298 -82.333  -28.349 1.00 37.35  ? 727  PEG   A O4     1 
HETATM 7697 H H11    . PEG   CA 7 .   ? 5.220  -83.887  -29.597 1.00 51.37  ? 727  PEG   A H11    1 
HETATM 7698 H H12    . PEG   CA 7 .   ? 6.884  -84.387  -29.693 1.00 51.46  ? 727  PEG   A H12    1 
HETATM 7699 H HO1    . PEG   CA 7 .   ? 5.591  -82.537  -31.266 1.00 51.20  ? 727  PEG   A HO1    1 
HETATM 7700 H H21    . PEG   CA 7 .   ? 6.729  -81.586  -28.889 1.00 49.42  ? 727  PEG   A H21    1 
HETATM 7701 H H22    . PEG   CA 7 .   ? 5.737  -82.539  -27.840 1.00 49.35  ? 727  PEG   A H22    1 
HETATM 7702 H H31    . PEG   CA 7 .   ? 9.186  -83.795  -29.070 1.00 45.73  ? 727  PEG   A H31    1 
HETATM 7703 H H32    . PEG   CA 7 .   ? 8.832  -82.113  -29.311 1.00 45.46  ? 727  PEG   A H32    1 
HETATM 7704 H H41    . PEG   CA 7 .   ? 9.873  -81.549  -27.174 1.00 43.27  ? 727  PEG   A H41    1 
HETATM 7705 H H42    . PEG   CA 7 .   ? 10.156 -83.228  -26.812 1.00 43.02  ? 727  PEG   A H42    1 
HETATM 7706 H HO4    . PEG   CA 7 .   ? 11.845 -81.668  -27.855 1.00 36.50  ? 727  PEG   A HO4    1 
HETATM 7707 C C1     . PEG   DA 7 .   ? 26.117 -91.785  -26.315 1.00 74.81  ? 728  PEG   A C1     1 
HETATM 7708 O O1     . PEG   DA 7 .   ? 26.159 -91.748  -24.902 1.00 74.01  ? 728  PEG   A O1     1 
HETATM 7709 C C2     . PEG   DA 7 .   ? 26.209 -90.422  -26.953 1.00 75.85  ? 728  PEG   A C2     1 
HETATM 7710 O O2     . PEG   DA 7 .   ? 27.484 -89.829  -26.726 1.00 76.72  ? 728  PEG   A O2     1 
HETATM 7711 C C3     . PEG   DA 7 .   ? 28.539 -90.305  -27.555 1.00 78.31  ? 728  PEG   A C3     1 
HETATM 7712 C C4     . PEG   DA 7 .   ? 29.122 -89.179  -28.350 1.00 79.54  ? 728  PEG   A C4     1 
HETATM 7713 O O4     . PEG   DA 7 .   ? 30.527 -89.079  -28.170 1.00 80.65  ? 728  PEG   A O4     1 
HETATM 7714 H H11    . PEG   DA 7 .   ? 26.887 -92.455  -26.690 1.00 75.01  ? 728  PEG   A H11    1 
HETATM 7715 H H12    . PEG   DA 7 .   ? 25.163 -92.261  -26.539 1.00 74.76  ? 728  PEG   A H12    1 
HETATM 7716 H HO1    . PEG   DA 7 .   ? 26.179 -92.686  -24.576 1.00 73.81  ? 728  PEG   A HO1    1 
HETATM 7717 H H21    . PEG   DA 7 .   ? 26.006 -90.498  -28.020 1.00 75.92  ? 728  PEG   A H21    1 
HETATM 7718 H H22    . PEG   DA 7 .   ? 25.429 -89.773  -26.560 1.00 75.97  ? 728  PEG   A H22    1 
HETATM 7719 H H31    . PEG   DA 7 .   ? 29.324 -90.759  -26.954 1.00 78.41  ? 728  PEG   A H31    1 
HETATM 7720 H H32    . PEG   DA 7 .   ? 28.188 -91.095  -28.215 1.00 78.44  ? 728  PEG   A H32    1 
HETATM 7721 H H41    . PEG   DA 7 .   ? 29.002 -89.352  -29.418 1.00 79.65  ? 728  PEG   A H41    1 
HETATM 7722 H H42    . PEG   DA 7 .   ? 28.631 -88.233  -28.130 1.00 79.61  ? 728  PEG   A H42    1 
HETATM 7723 H HO4    . PEG   DA 7 .   ? 30.737 -88.134  -27.951 1.00 80.65  ? 728  PEG   A HO4    1 
HETATM 7724 C C1     . PEG   EA 7 .   ? 17.512 -101.308 -10.743 1.00 68.33  ? 729  PEG   A C1     1 
HETATM 7725 O O1     . PEG   EA 7 .   ? 16.163 -100.887 -10.872 1.00 68.67  ? 729  PEG   A O1     1 
HETATM 7726 C C2     . PEG   EA 7 .   ? 18.462 -100.172 -10.965 1.00 68.51  ? 729  PEG   A C2     1 
HETATM 7727 O O2     . PEG   EA 7 .   ? 19.491 -100.110 -9.987  1.00 68.39  ? 729  PEG   A O2     1 
HETATM 7728 C C3     . PEG   EA 7 .   ? 20.670 -99.419  -10.391 1.00 66.55  ? 729  PEG   A C3     1 
HETATM 7729 C C4     . PEG   EA 7 .   ? 21.718 -100.388 -10.799 1.00 67.09  ? 729  PEG   A C4     1 
HETATM 7730 O O4     . PEG   EA 7 .   ? 21.288 -101.212 -11.852 1.00 67.78  ? 729  PEG   A O4     1 
HETATM 7731 H H11    . PEG   EA 7 .   ? 17.686 -101.850 -9.815  1.00 68.41  ? 729  PEG   A H11    1 
HETATM 7732 H H12    . PEG   EA 7 .   ? 17.621 -102.042 -11.539 1.00 68.40  ? 729  PEG   A H12    1 
HETATM 7733 H HO1    . PEG   EA 7 .   ? 15.618 -101.687 -11.094 1.00 68.81  ? 729  PEG   A HO1    1 
HETATM 7734 H H21    . PEG   EA 7 .   ? 18.953 -100.363 -11.912 1.00 68.62  ? 729  PEG   A H21    1 
HETATM 7735 H H22    . PEG   EA 7 .   ? 17.933 -99.228  -11.082 1.00 68.61  ? 729  PEG   A H22    1 
HETATM 7736 H H31    . PEG   EA 7 .   ? 20.493 -98.730  -11.214 1.00 66.66  ? 729  PEG   A H31    1 
HETATM 7737 H H32    . PEG   EA 7 .   ? 21.034 -98.807  -9.567  1.00 66.24  ? 729  PEG   A H32    1 
HETATM 7738 H H41    . PEG   EA 7 .   ? 22.593 -99.878  -11.199 1.00 67.07  ? 729  PEG   A H41    1 
HETATM 7739 H H42    . PEG   EA 7 .   ? 22.054 -100.983 -9.953  1.00 67.28  ? 729  PEG   A H42    1 
HETATM 7740 H HO4    . PEG   EA 7 .   ? 21.220 -100.643 -12.663 1.00 67.94  ? 729  PEG   A HO4    1 
HETATM 7741 C C1     . EDO   FA 5 .   ? 25.161 -112.651 -45.076 1.00 38.10  ? 401  EDO   B C1     1 
HETATM 7742 O O1     . EDO   FA 5 .   ? 24.748 -113.663 -46.014 1.00 37.98  ? 401  EDO   B O1     1 
HETATM 7743 C C2     . EDO   FA 5 .   ? 25.531 -111.325 -45.778 1.00 34.43  ? 401  EDO   B C2     1 
HETATM 7744 O O2     . EDO   FA 5 .   ? 26.695 -110.785 -45.192 1.00 37.19  ? 401  EDO   B O2     1 
HETATM 7745 H H11    . EDO   FA 5 .   ? 24.423 -112.481 -44.293 1.00 38.34  ? 401  EDO   B H11    1 
HETATM 7746 H H12    . EDO   FA 5 .   ? 26.036 -113.077 -44.588 1.00 38.54  ? 401  EDO   B H12    1 
HETATM 7747 H HO1    . EDO   FA 5 .   ? 23.963 -114.128 -45.622 1.00 37.56  ? 401  EDO   B HO1    1 
HETATM 7748 H H21    . EDO   FA 5 .   ? 25.803 -111.495 -46.819 1.00 34.72  ? 401  EDO   B H21    1 
HETATM 7749 H H22    . EDO   FA 5 .   ? 24.707 -110.614 -45.761 1.00 33.82  ? 401  EDO   B H22    1 
HETATM 7750 H HO2    . EDO   FA 5 .   ? 27.259 -110.410 -45.919 1.00 36.98  ? 401  EDO   B HO2    1 
HETATM 7751 C C1     . EDO   GA 5 .   ? 8.422  -105.920 -29.182 1.00 49.67  ? 402  EDO   B C1     1 
HETATM 7752 O O1     . EDO   GA 5 .   ? 7.512  -106.414 -30.149 1.00 48.44  ? 402  EDO   B O1     1 
HETATM 7753 C C2     . EDO   GA 5 .   ? 9.779  -105.619 -29.849 1.00 50.14  ? 402  EDO   B C2     1 
HETATM 7754 O O2     . EDO   GA 5 .   ? 10.776 -105.321 -28.878 1.00 50.03  ? 402  EDO   B O2     1 
HETATM 7755 H H11    . EDO   GA 5 .   ? 8.032  -105.060 -28.642 1.00 49.80  ? 402  EDO   B H11    1 
HETATM 7756 H H12    . EDO   GA 5 .   ? 8.524  -106.717 -28.450 1.00 49.94  ? 402  EDO   B H12    1 
HETATM 7757 H HO1    . EDO   GA 5 .   ? 7.673  -107.391 -30.233 1.00 48.32  ? 402  EDO   B HO1    1 
HETATM 7758 H H21    . EDO   GA 5 .   ? 10.151 -106.487 -30.391 1.00 50.33  ? 402  EDO   B H21    1 
HETATM 7759 H H22    . EDO   GA 5 .   ? 9.672  -104.829 -30.588 1.00 50.46  ? 402  EDO   B H22    1 
HETATM 7760 H HO2    . EDO   GA 5 .   ? 11.643 -105.246 -29.356 1.00 49.63  ? 402  EDO   B HO2    1 
HETATM 7761 S S      . SO4   HA 6 .   ? 23.416 -129.998 -48.524 1.00 106.33 ? 403  SO4   B S      1 
HETATM 7762 O O1     . SO4   HA 6 .   ? 23.930 -130.846 -49.596 1.00 107.17 ? 403  SO4   B O1     1 
HETATM 7763 O O2     . SO4   HA 6 .   ? 22.447 -129.055 -49.088 1.00 106.23 ? 403  SO4   B O2     1 
HETATM 7764 O O3     . SO4   HA 6 .   ? 22.766 -130.837 -47.512 1.00 105.63 ? 403  SO4   B O3     1 
HETATM 7765 O O4     . SO4   HA 6 .   ? 24.530 -129.264 -47.920 1.00 106.10 ? 403  SO4   B O4     1 
HETATM 7766 O O      . HOH   IA 8 .   ? 2.649  -66.036  -4.271  1.00 48.09  ? 801  HOH   A O      1 
HETATM 7767 O O      . HOH   IA 8 .   ? 19.243 -75.000  -34.567 1.00 21.46  ? 802  HOH   A O      1 
HETATM 7768 O O      . HOH   IA 8 .   ? 24.783 -46.405  -17.320 1.00 29.58  ? 803  HOH   A O      1 
HETATM 7769 O O      . HOH   IA 8 .   ? 23.100 -90.638  -26.866 1.00 36.00  ? 804  HOH   A O      1 
HETATM 7770 O O      . HOH   IA 8 .   ? 25.666 -34.238  -6.185  1.00 30.47  ? 805  HOH   A O      1 
HETATM 7771 O O      . HOH   IA 8 .   ? 5.984  -90.748  -27.759 1.00 33.42  ? 806  HOH   A O      1 
HETATM 7772 O O      . HOH   IA 8 .   ? 10.539 -69.507  -24.283 1.00 42.31  ? 807  HOH   A O      1 
HETATM 7773 O O      . HOH   IA 8 .   ? 21.869 -50.048  -21.275 1.00 25.26  ? 808  HOH   A O      1 
HETATM 7774 O O      . HOH   IA 8 .   ? 22.505 -89.223  -47.535 1.00 43.81  ? 809  HOH   A O      1 
HETATM 7775 O O      . HOH   IA 8 .   ? 5.305  -74.857  -20.154 1.00 22.49  ? 810  HOH   A O      1 
HETATM 7776 O O      . HOH   IA 8 .   ? 6.649  -72.024  -24.144 1.00 34.37  ? 811  HOH   A O      1 
HETATM 7777 O O      . HOH   IA 8 .   ? 26.892 -38.956  -3.837  1.00 23.20  ? 812  HOH   A O      1 
HETATM 7778 O O      . HOH   IA 8 .   ? 19.016 -92.065  -25.944 1.00 33.52  ? 813  HOH   A O      1 
HETATM 7779 O O      . HOH   IA 8 .   ? 7.913  -32.207  -17.914 1.00 40.64  ? 814  HOH   A O      1 
HETATM 7780 O O      . HOH   IA 8 .   ? 9.255  -43.968  -19.265 1.00 23.50  ? 815  HOH   A O      1 
HETATM 7781 O O      . HOH   IA 8 .   ? 9.514  -43.829  -3.446  1.00 24.63  ? 816  HOH   A O      1 
HETATM 7782 O O      . HOH   IA 8 .   ? 21.766 -30.768  10.077  1.00 41.71  ? 817  HOH   A O      1 
HETATM 7783 O O      . HOH   IA 8 .   ? 16.529 -42.219  -2.849  1.00 27.60  ? 818  HOH   A O      1 
HETATM 7784 O O      . HOH   IA 8 .   ? 14.415 -66.428  -37.379 1.00 25.58  ? 819  HOH   A O      1 
HETATM 7785 O O      . HOH   IA 8 .   ? 5.264  -32.674  -7.318  1.00 34.82  ? 820  HOH   A O      1 
HETATM 7786 O O      . HOH   IA 8 .   ? 9.782  -80.993  -31.280 1.00 33.35  ? 821  HOH   A O      1 
HETATM 7787 O O      . HOH   IA 8 .   ? 22.100 -56.786  -12.804 1.00 17.27  ? 822  HOH   A O      1 
HETATM 7788 O O      . HOH   IA 8 .   ? 25.546 -86.264  -30.868 1.00 39.89  ? 823  HOH   A O      1 
HETATM 7789 O O      . HOH   IA 8 .   ? 36.133 -44.979  -12.497 1.00 45.39  ? 824  HOH   A O      1 
HETATM 7790 O O      . HOH   IA 8 .   ? 33.347 -35.678  10.202  1.00 29.30  ? 825  HOH   A O      1 
HETATM 7791 O O      . HOH   IA 8 .   ? 33.873 -29.567  -18.542 1.00 43.27  ? 826  HOH   A O      1 
HETATM 7792 O O      . HOH   IA 8 .   ? 13.234 -40.355  -12.597 1.00 18.17  ? 827  HOH   A O      1 
HETATM 7793 O O      . HOH   IA 8 .   ? 39.599 -82.445  -37.806 1.00 60.02  ? 828  HOH   A O      1 
HETATM 7794 O O      . HOH   IA 8 .   ? 19.815 -34.999  -7.947  1.00 19.79  ? 829  HOH   A O      1 
HETATM 7795 O O      . HOH   IA 8 .   ? 26.583 -40.873  -5.734  1.00 28.06  ? 830  HOH   A O      1 
HETATM 7796 O O      . HOH   IA 8 .   ? 22.049 -88.789  -30.588 1.00 30.76  ? 831  HOH   A O      1 
HETATM 7797 O O      . HOH   IA 8 .   ? 2.103  -37.567  -11.375 1.00 37.28  ? 832  HOH   A O      1 
HETATM 7798 O O      . HOH   IA 8 .   ? 25.791 -108.120 -15.082 1.00 43.93  ? 833  HOH   A O      1 
HETATM 7799 O O      . HOH   IA 8 .   ? 16.601 -66.138  -35.803 1.00 36.13  ? 834  HOH   A O      1 
HETATM 7800 O O      . HOH   IA 8 .   ? 23.773 -49.756  -19.089 1.00 22.13  ? 835  HOH   A O      1 
HETATM 7801 O O      . HOH   IA 8 .   ? 23.678 -83.419  -31.210 1.00 37.21  ? 836  HOH   A O      1 
HETATM 7802 O O      . HOH   IA 8 .   ? 24.265 -33.358  9.545   1.00 24.62  ? 837  HOH   A O      1 
HETATM 7803 O O      . HOH   IA 8 .   ? 18.741 -107.536 -18.469 1.00 33.07  ? 838  HOH   A O      1 
HETATM 7804 O O      . HOH   IA 8 .   ? 14.636 -48.710  -2.160  1.00 38.07  ? 839  HOH   A O      1 
HETATM 7805 O O      . HOH   IA 8 .   ? 10.654 -51.522  -5.453  1.00 47.13  ? 840  HOH   A O      1 
HETATM 7806 O O      . HOH   IA 8 .   ? 24.991 -20.061  -0.868  1.00 39.85  ? 841  HOH   A O      1 
HETATM 7807 O O      . HOH   IA 8 .   ? 26.747 -41.702  -10.781 1.00 22.19  ? 842  HOH   A O      1 
HETATM 7808 O O      . HOH   IA 8 .   ? 13.894 -98.190  -13.022 1.00 23.88  ? 843  HOH   A O      1 
HETATM 7809 O O      . HOH   IA 8 .   ? 6.379  -27.681  -4.338  1.00 44.13  ? 844  HOH   A O      1 
HETATM 7810 O O      . HOH   IA 8 .   ? 18.809 -108.237 -13.911 1.00 41.83  ? 845  HOH   A O      1 
HETATM 7811 O O      . HOH   IA 8 .   ? 15.396 -65.748  -33.404 1.00 27.88  ? 846  HOH   A O      1 
HETATM 7812 O O      . HOH   IA 8 .   ? 21.023 -53.847  -23.452 1.00 28.37  ? 847  HOH   A O      1 
HETATM 7813 O O      . HOH   IA 8 .   ? 33.972 -40.414  -11.125 1.00 35.15  ? 848  HOH   A O      1 
HETATM 7814 O O      . HOH   IA 8 .   ? 21.284 -48.200  -1.015  1.00 22.93  ? 849  HOH   A O      1 
HETATM 7815 O O      . HOH   IA 8 .   ? 24.463 -92.630  -30.805 1.00 32.10  ? 850  HOH   A O      1 
HETATM 7816 O O      . HOH   IA 8 .   ? 30.780 -48.658  -2.637  1.00 35.41  ? 851  HOH   A O      1 
HETATM 7817 O O      . HOH   IA 8 .   ? 6.453  -25.692  -8.391  1.00 43.53  ? 852  HOH   A O      1 
HETATM 7818 O O      . HOH   IA 8 .   ? 25.296 -40.685  -26.970 1.00 46.60  ? 853  HOH   A O      1 
HETATM 7819 O O      . HOH   IA 8 .   ? 29.556 -95.760  -13.454 1.00 37.67  ? 854  HOH   A O      1 
HETATM 7820 O O      . HOH   IA 8 .   ? 21.868 -86.507  -5.347  1.00 49.18  ? 855  HOH   A O      1 
HETATM 7821 O O      . HOH   IA 8 .   ? 37.811 -26.775  -13.114 1.00 44.15  ? 856  HOH   A O      1 
HETATM 7822 O O      . HOH   IA 8 .   ? 41.418 -80.815  -41.303 1.00 51.81  ? 857  HOH   A O      1 
HETATM 7823 O O      . HOH   IA 8 .   ? 20.982 -72.840  -42.557 1.00 37.14  ? 858  HOH   A O      1 
HETATM 7824 O O      . HOH   IA 8 .   ? 20.552 -77.798  -10.116 1.00 52.57  ? 859  HOH   A O      1 
HETATM 7825 O O      . HOH   IA 8 .   ? 15.182 -36.506  -24.530 1.00 25.16  ? 860  HOH   A O      1 
HETATM 7826 O O      . HOH   IA 8 .   ? 27.206 -86.001  -54.047 1.00 45.83  ? 861  HOH   A O      1 
HETATM 7827 O O      . HOH   IA 8 .   ? 19.925 -42.071  -10.506 1.00 23.83  ? 862  HOH   A O      1 
HETATM 7828 O O      . HOH   IA 8 .   ? 43.359 -59.986  -29.417 1.00 62.32  ? 863  HOH   A O      1 
HETATM 7829 O O      . HOH   IA 8 .   ? 11.427 -72.029  -36.249 1.00 42.55  ? 864  HOH   A O      1 
HETATM 7830 O O      . HOH   IA 8 .   ? 26.656 -68.657  -40.412 1.00 48.85  ? 865  HOH   A O      1 
HETATM 7831 O O      . HOH   IA 8 .   ? 11.023 -40.066  -19.855 1.00 23.55  ? 866  HOH   A O      1 
HETATM 7832 O O      . HOH   IA 8 .   ? -0.608 -58.354  -7.391  1.00 28.70  ? 867  HOH   A O      1 
HETATM 7833 O O      . HOH   IA 8 .   ? 2.546  -65.591  -33.816 1.00 46.12  ? 868  HOH   A O      1 
HETATM 7834 O O      . HOH   IA 8 .   ? 17.553 -48.000  1.043   1.00 43.09  ? 869  HOH   A O      1 
HETATM 7835 O O      . HOH   IA 8 .   ? 9.186  -76.184  -13.209 1.00 43.73  ? 870  HOH   A O      1 
HETATM 7836 O O      . HOH   IA 8 .   ? 19.718 -106.390 -16.100 1.00 37.48  ? 871  HOH   A O      1 
HETATM 7837 O O      . HOH   IA 8 .   ? 23.433 -99.178  -20.867 1.00 25.89  ? 872  HOH   A O      1 
HETATM 7838 O O      . HOH   IA 8 .   ? 5.741  -47.421  -33.247 1.00 27.80  ? 873  HOH   A O      1 
HETATM 7839 O O      . HOH   IA 8 .   ? 9.346  -29.144  -13.921 1.00 38.57  ? 874  HOH   A O      1 
HETATM 7840 O O      . HOH   IA 8 .   ? 6.821  -32.690  -15.489 1.00 34.94  ? 875  HOH   A O      1 
HETATM 7841 O O      . HOH   IA 8 .   ? 1.052  -37.493  -8.847  1.00 38.61  ? 876  HOH   A O      1 
HETATM 7842 O O      . HOH   IA 8 .   ? 6.056  -51.568  -5.007  1.00 26.26  ? 877  HOH   A O      1 
HETATM 7843 O O      . HOH   IA 8 .   ? 26.933 -70.683  -19.551 1.00 34.67  ? 878  HOH   A O      1 
HETATM 7844 O O      . HOH   IA 8 .   ? -0.646 -66.177  -16.641 1.00 36.28  ? 879  HOH   A O      1 
HETATM 7845 O O      . HOH   IA 8 .   ? 4.527  -47.189  -3.148  1.00 40.41  ? 880  HOH   A O      1 
HETATM 7846 O O      . HOH   IA 8 .   ? 18.935 -42.231  -7.215  1.00 25.11  ? 881  HOH   A O      1 
HETATM 7847 O O      . HOH   IA 8 .   ? 29.819 -53.305  -7.293  1.00 41.98  ? 882  HOH   A O      1 
HETATM 7848 O O      . HOH   IA 8 .   ? -2.332 -64.565  -10.320 1.00 50.71  ? 883  HOH   A O      1 
HETATM 7849 O O      . HOH   IA 8 .   ? 10.129 -103.095 -19.526 1.00 41.80  ? 884  HOH   A O      1 
HETATM 7850 O O      . HOH   IA 8 .   ? 15.690 -47.139  -9.842  1.00 27.82  ? 885  HOH   A O      1 
HETATM 7851 O O      . HOH   IA 8 .   ? 13.401 -55.741  -36.734 1.00 46.00  ? 886  HOH   A O      1 
HETATM 7852 O O      . HOH   IA 8 .   ? 25.161 -94.475  -18.947 1.00 33.24  ? 887  HOH   A O      1 
HETATM 7853 O O      . HOH   IA 8 .   ? 10.618 -48.840  -7.036  1.00 48.59  ? 888  HOH   A O      1 
HETATM 7854 O O      . HOH   IA 8 .   ? 18.074 -73.891  -17.187 1.00 29.53  ? 889  HOH   A O      1 
HETATM 7855 O O      . HOH   IA 8 .   ? 19.180 -27.961  -20.225 1.00 26.07  ? 890  HOH   A O      1 
HETATM 7856 O O      . HOH   IA 8 .   ? 17.998 -76.916  -37.014 1.00 24.79  ? 891  HOH   A O      1 
HETATM 7857 O O      . HOH   IA 8 .   ? 8.516  -44.788  -32.542 1.00 44.89  ? 892  HOH   A O      1 
HETATM 7858 O O      . HOH   IA 8 .   ? 13.675 -38.863  -6.897  1.00 35.29  ? 893  HOH   A O      1 
HETATM 7859 O O      . HOH   IA 8 .   ? 31.680 -53.766  -9.682  1.00 49.81  ? 894  HOH   A O      1 
HETATM 7860 O O      . HOH   IA 8 .   ? 23.793 -87.296  -40.945 1.00 31.08  ? 895  HOH   A O      1 
HETATM 7861 O O      . HOH   IA 8 .   ? 11.717 -50.959  -33.796 1.00 23.71  ? 896  HOH   A O      1 
HETATM 7862 O O      . HOH   IA 8 .   ? 17.613 -56.600  -5.336  1.00 45.07  ? 897  HOH   A O      1 
HETATM 7863 O O      . HOH   IA 8 .   ? 13.922 -58.545  -35.969 1.00 36.69  ? 898  HOH   A O      1 
HETATM 7864 O O      . HOH   IA 8 .   ? -3.842 -51.339  -6.548  1.00 51.40  ? 899  HOH   A O      1 
HETATM 7865 O O      . HOH   IA 8 .   ? 31.891 -98.385  -24.657 1.00 36.92  ? 900  HOH   A O      1 
HETATM 7866 O O      . HOH   IA 8 .   ? 2.108  -68.683  -3.948  1.00 71.32  ? 901  HOH   A O      1 
HETATM 7867 O O      . HOH   IA 8 .   ? 0.459  -35.440  -20.490 1.00 45.29  ? 902  HOH   A O      1 
HETATM 7868 O O      . HOH   IA 8 .   ? 13.888 -28.177  -21.788 1.00 38.85  ? 903  HOH   A O      1 
HETATM 7869 O O      . HOH   IA 8 .   ? 25.589 -47.182  -33.069 1.00 47.64  ? 904  HOH   A O      1 
HETATM 7870 O O      . HOH   IA 8 .   ? 12.883 -89.477  -26.971 1.00 20.72  ? 905  HOH   A O      1 
HETATM 7871 O O      . HOH   IA 8 .   ? 32.493 -94.651  -17.816 1.00 55.75  ? 906  HOH   A O      1 
HETATM 7872 O O      . HOH   IA 8 .   ? 16.035 -34.289  5.005   1.00 45.09  ? 907  HOH   A O      1 
HETATM 7873 O O      . HOH   IA 8 .   ? 9.574  -26.529  -2.897  1.00 40.40  ? 908  HOH   A O      1 
HETATM 7874 O O      . HOH   IA 8 .   ? 16.192 -88.999  -40.382 1.00 41.72  ? 909  HOH   A O      1 
HETATM 7875 O O      . HOH   IA 8 .   ? 18.333 -54.063  -31.754 1.00 44.95  ? 910  HOH   A O      1 
HETATM 7876 O O      . HOH   IA 8 .   ? 11.352 -81.709  -36.941 1.00 28.47  ? 911  HOH   A O      1 
HETATM 7877 O O      . HOH   IA 8 .   ? 32.093 -35.378  4.617   1.00 24.87  ? 912  HOH   A O      1 
HETATM 7878 O O      . HOH   IA 8 .   ? 16.137 -87.751  -28.238 1.00 30.42  ? 913  HOH   A O      1 
HETATM 7879 O O      . HOH   IA 8 .   ? 39.555 -86.712  -4.183  1.00 58.70  ? 914  HOH   A O      1 
HETATM 7880 O O      . HOH   IA 8 .   ? 28.125 -75.252  -17.449 1.00 42.12  ? 915  HOH   A O      1 
HETATM 7881 O O      . HOH   IA 8 .   ? 32.494 -38.521  -14.457 1.00 29.10  ? 916  HOH   A O      1 
HETATM 7882 O O      . HOH   IA 8 .   ? 13.992 -73.022  -20.728 1.00 26.61  ? 917  HOH   A O      1 
HETATM 7883 O O      . HOH   IA 8 .   ? 14.495 -90.053  -7.600  1.00 44.36  ? 918  HOH   A O      1 
HETATM 7884 O O      . HOH   IA 8 .   ? 33.552 -42.840  -4.560  1.00 46.12  ? 919  HOH   A O      1 
HETATM 7885 O O      . HOH   IA 8 .   ? 4.663  -63.693  -6.052  1.00 23.09  ? 920  HOH   A O      1 
HETATM 7886 O O      . HOH   IA 8 .   ? 10.276 -87.763  -33.783 1.00 29.40  ? 921  HOH   A O      1 
HETATM 7887 O O      . HOH   IA 8 .   ? 8.615  -98.844  -17.448 1.00 30.27  ? 922  HOH   A O      1 
HETATM 7888 O O      . HOH   IA 8 .   ? 31.884 -87.670  -45.871 1.00 42.10  ? 923  HOH   A O      1 
HETATM 7889 O O      . HOH   IA 8 .   ? 21.428 -91.364  -24.986 1.00 30.31  ? 924  HOH   A O      1 
HETATM 7890 O O      . HOH   IA 8 .   ? 18.781 -38.906  -29.874 1.00 41.55  ? 925  HOH   A O      1 
HETATM 7891 O O      . HOH   IA 8 .   ? -2.447 -53.555  -31.677 1.00 38.13  ? 926  HOH   A O      1 
HETATM 7892 O O      . HOH   IA 8 .   ? 9.682  -60.045  -7.445  1.00 27.46  ? 927  HOH   A O      1 
HETATM 7893 O O      . HOH   IA 8 .   ? 18.707 -78.790  -38.957 1.00 19.47  ? 928  HOH   A O      1 
HETATM 7894 O O      . HOH   IA 8 .   ? 31.425 -95.969  -15.399 1.00 37.48  ? 929  HOH   A O      1 
HETATM 7895 O O      . HOH   IA 8 .   ? 26.721 -105.397 -28.165 1.00 44.93  ? 930  HOH   A O      1 
HETATM 7896 O O      . HOH   IA 8 .   ? 34.470 -63.363  -26.467 1.00 31.30  ? 931  HOH   A O      1 
HETATM 7897 O O      . HOH   IA 8 .   ? 8.299  -32.923  -23.634 1.00 54.71  ? 932  HOH   A O      1 
HETATM 7898 O O      . HOH   IA 8 .   ? -5.328 -57.496  -16.415 1.00 27.65  ? 933  HOH   A O      1 
HETATM 7899 O O      . HOH   IA 8 .   ? 34.319 -62.768  -23.344 1.00 54.06  ? 934  HOH   A O      1 
HETATM 7900 O O      . HOH   IA 8 .   ? 19.238 -27.725  -23.868 1.00 37.52  ? 935  HOH   A O      1 
HETATM 7901 O O      . HOH   IA 8 .   ? 16.937 -35.236  -12.906 1.00 18.71  ? 936  HOH   A O      1 
HETATM 7902 O O      . HOH   IA 8 .   ? 11.379 -36.983  1.167   1.00 36.08  ? 937  HOH   A O      1 
HETATM 7903 O O      . HOH   IA 8 .   ? 4.504  -33.754  -18.251 1.00 26.03  ? 938  HOH   A O      1 
HETATM 7904 O O      . HOH   IA 8 .   ? 22.588 -86.773  -12.067 1.00 42.60  ? 939  HOH   A O      1 
HETATM 7905 O O      . HOH   IA 8 .   ? 4.688  -91.190  -14.093 1.00 34.50  ? 940  HOH   A O      1 
HETATM 7906 O O      . HOH   IA 8 .   ? 22.349 -82.311  -46.357 1.00 33.83  ? 941  HOH   A O      1 
HETATM 7907 O O      . HOH   IA 8 .   ? 12.983 -92.811  -30.737 1.00 27.79  ? 942  HOH   A O      1 
HETATM 7908 O O      . HOH   IA 8 .   ? 34.288 -89.066  -28.158 1.00 28.29  ? 943  HOH   A O      1 
HETATM 7909 O O      . HOH   IA 8 .   ? 35.790 -30.227  -2.631  1.00 48.32  ? 944  HOH   A O      1 
HETATM 7910 O O      . HOH   IA 8 .   ? 21.201 -87.919  -51.207 1.00 30.39  ? 945  HOH   A O      1 
HETATM 7911 O O      . HOH   IA 8 .   ? 1.221  -58.716  -35.556 1.00 44.39  ? 946  HOH   A O      1 
HETATM 7912 O O      . HOH   IA 8 .   ? 15.793 -25.797  -19.068 1.00 26.47  ? 947  HOH   A O      1 
HETATM 7913 O O      . HOH   IA 8 .   ? 33.228 -49.956  0.108   1.00 43.79  ? 948  HOH   A O      1 
HETATM 7914 O O      . HOH   IA 8 .   ? 15.680 -46.312  3.886   1.00 32.10  ? 949  HOH   A O      1 
HETATM 7915 O O      . HOH   IA 8 .   ? 21.611 -54.877  -27.720 1.00 41.49  ? 950  HOH   A O      1 
HETATM 7916 O O      . HOH   IA 8 .   ? 17.312 -30.200  -12.822 1.00 26.18  ? 951  HOH   A O      1 
HETATM 7917 O O      . HOH   IA 8 .   ? 13.497 -90.752  -10.082 1.00 27.97  ? 952  HOH   A O      1 
HETATM 7918 O O      . HOH   IA 8 .   ? 16.183 -44.926  -2.472  1.00 34.25  ? 953  HOH   A O      1 
HETATM 7919 O O      . HOH   IA 8 .   ? -3.700 -47.209  -7.047  1.00 42.95  ? 954  HOH   A O      1 
HETATM 7920 O O      . HOH   IA 8 .   ? 15.917 -47.530  -12.556 1.00 18.54  ? 955  HOH   A O      1 
HETATM 7921 O O      . HOH   IA 8 .   ? 15.648 -65.231  -9.682  1.00 43.60  ? 956  HOH   A O      1 
HETATM 7922 O O      . HOH   IA 8 .   ? 18.710 -63.738  -36.875 1.00 37.48  ? 957  HOH   A O      1 
HETATM 7923 O O      . HOH   IA 8 .   ? 15.046 -70.977  -19.346 1.00 33.20  ? 958  HOH   A O      1 
HETATM 7924 O O      . HOH   IA 8 .   ? 27.188 -101.591 -17.247 1.00 24.50  ? 959  HOH   A O      1 
HETATM 7925 O O      . HOH   IA 8 .   ? 7.329  -43.454  -30.451 1.00 47.41  ? 960  HOH   A O      1 
HETATM 7926 O O      . HOH   IA 8 .   ? 12.688 -86.181  -36.074 1.00 32.30  ? 961  HOH   A O      1 
HETATM 7927 O O      . HOH   IA 8 .   ? 37.834 -29.924  -14.576 1.00 54.36  ? 962  HOH   A O      1 
HETATM 7928 O O      . HOH   IA 8 .   ? 5.527  -57.546  -3.313  1.00 35.92  ? 963  HOH   A O      1 
HETATM 7929 O O      . HOH   IA 8 .   ? 24.169 -104.410 -27.471 1.00 32.07  ? 964  HOH   A O      1 
HETATM 7930 O O      . HOH   IA 8 .   ? 23.764 -66.167  -42.659 1.00 39.39  ? 965  HOH   A O      1 
HETATM 7931 O O      . HOH   IA 8 .   ? 3.679  -57.015  -5.245  1.00 32.81  ? 966  HOH   A O      1 
HETATM 7932 O O      . HOH   IA 8 .   ? 19.917 -87.470  -11.848 1.00 19.53  ? 967  HOH   A O      1 
HETATM 7933 O O      . HOH   IA 8 .   ? 41.007 -97.115  -19.441 1.00 45.65  ? 968  HOH   A O      1 
HETATM 7934 O O      . HOH   IA 8 .   ? 13.016 -46.508  -9.116  1.00 32.95  ? 969  HOH   A O      1 
HETATM 7935 O O      . HOH   IA 8 .   ? 19.176 -19.218  -20.300 1.00 39.09  ? 970  HOH   A O      1 
HETATM 7936 O O      . HOH   IA 8 .   ? 1.232  -62.853  -22.343 1.00 26.30  ? 971  HOH   A O      1 
HETATM 7937 O O      . HOH   IA 8 .   ? 31.278 -62.772  -20.058 1.00 51.02  ? 972  HOH   A O      1 
HETATM 7938 O O      . HOH   IA 8 .   ? 14.873 -14.295  -5.844  1.00 46.63  ? 973  HOH   A O      1 
HETATM 7939 O O      . HOH   IA 8 .   ? 9.496  -106.578 -22.506 1.00 42.44  ? 974  HOH   A O      1 
HETATM 7940 O O      . HOH   IA 8 .   ? 0.921  -39.776  -23.705 1.00 27.02  ? 975  HOH   A O      1 
HETATM 7941 O O      . HOH   IA 8 .   ? 34.292 -42.613  -20.600 1.00 44.48  ? 976  HOH   A O      1 
HETATM 7942 O O      . HOH   IA 8 .   ? 16.613 -71.583  -17.225 1.00 34.61  ? 977  HOH   A O      1 
HETATM 7943 O O      . HOH   IA 8 .   ? 14.169 -38.431  4.162   1.00 38.77  ? 978  HOH   A O      1 
HETATM 7944 O O      . HOH   IA 8 .   ? 33.671 -98.595  -22.469 1.00 39.77  ? 979  HOH   A O      1 
HETATM 7945 O O      . HOH   IA 8 .   ? 18.090 -41.407  -0.683  1.00 18.63  ? 980  HOH   A O      1 
HETATM 7946 O O      . HOH   IA 8 .   ? 33.884 -42.889  -0.309  1.00 38.93  ? 981  HOH   A O      1 
HETATM 7947 O O      . HOH   IA 8 .   ? 8.559  -40.016  -26.803 1.00 48.64  ? 982  HOH   A O      1 
HETATM 7948 O O      . HOH   IA 8 .   ? 16.247 -103.700 -23.518 1.00 35.72  ? 983  HOH   A O      1 
HETATM 7949 O O      . HOH   IA 8 .   ? 10.988 -55.553  -8.906  1.00 48.42  ? 984  HOH   A O      1 
HETATM 7950 O O      . HOH   IA 8 .   ? 34.766 -85.590  -34.259 1.00 36.70  ? 985  HOH   A O      1 
HETATM 7951 O O      . HOH   IA 8 .   ? 4.927  -34.721  -5.563  1.00 37.14  ? 986  HOH   A O      1 
HETATM 7952 O O      . HOH   IA 8 .   ? 24.258 -36.709  -28.461 1.00 45.24  ? 987  HOH   A O      1 
HETATM 7953 O O      . HOH   IA 8 .   ? -1.254 -44.467  -27.686 1.00 47.88  ? 988  HOH   A O      1 
HETATM 7954 O O      . HOH   IA 8 .   ? 27.269 -35.189  -25.265 1.00 43.01  ? 989  HOH   A O      1 
HETATM 7955 O O      . HOH   IA 8 .   ? 25.576 -25.040  4.976   1.00 37.82  ? 990  HOH   A O      1 
HETATM 7956 O O      . HOH   IA 8 .   ? 5.827  -103.776 -28.136 1.00 31.26  ? 991  HOH   A O      1 
HETATM 7957 O O      . HOH   IA 8 .   ? 21.506 -84.764  -30.177 1.00 22.99  ? 992  HOH   A O      1 
HETATM 7958 O O      . HOH   IA 8 .   ? 23.758 -99.270  -27.492 1.00 30.23  ? 993  HOH   A O      1 
HETATM 7959 O O      . HOH   IA 8 .   ? 17.651 -72.840  -34.834 1.00 34.56  ? 994  HOH   A O      1 
HETATM 7960 O O      . HOH   IA 8 .   ? 18.466 -62.847  -10.538 1.00 32.18  ? 995  HOH   A O      1 
HETATM 7961 O O      . HOH   IA 8 .   ? 5.714  -38.383  -23.878 1.00 22.75  ? 996  HOH   A O      1 
HETATM 7962 O O      . HOH   IA 8 .   ? 29.567 -67.175  -36.738 1.00 37.11  ? 997  HOH   A O      1 
HETATM 7963 O O      . HOH   IA 8 .   ? 25.505 -76.614  -15.568 1.00 33.16  ? 998  HOH   A O      1 
HETATM 7964 O O      . HOH   IA 8 .   ? 6.336  -83.918  -6.890  1.00 47.04  ? 999  HOH   A O      1 
HETATM 7965 O O      . HOH   IA 8 .   ? 7.086  -49.065  -36.612 1.00 40.77  ? 1000 HOH   A O      1 
HETATM 7966 O O      . HOH   IA 8 .   ? 18.715 -103.661 -14.717 1.00 33.38  ? 1001 HOH   A O      1 
HETATM 7967 O O      . HOH   IA 8 .   ? -6.593 -58.144  -13.956 1.00 32.24  ? 1002 HOH   A O      1 
HETATM 7968 O O      . HOH   IA 8 .   ? 22.942 -52.134  -22.583 1.00 31.99  ? 1003 HOH   A O      1 
HETATM 7969 O O      . HOH   IA 8 .   ? 13.119 -91.959  -28.095 1.00 20.20  ? 1004 HOH   A O      1 
HETATM 7970 O O      . HOH   IA 8 .   ? 17.287 -69.248  -16.019 1.00 46.33  ? 1005 HOH   A O      1 
HETATM 7971 O O      . HOH   IA 8 .   ? 39.464 -97.595  -12.111 1.00 43.64  ? 1006 HOH   A O      1 
HETATM 7972 O O      . HOH   IA 8 .   ? 27.816 -82.187  -7.591  1.00 35.25  ? 1007 HOH   A O      1 
HETATM 7973 O O      . HOH   IA 8 .   ? 30.880 -16.043  -22.830 1.00 49.65  ? 1008 HOH   A O      1 
HETATM 7974 O O      . HOH   IA 8 .   ? 17.114 -49.132  -8.684  1.00 40.09  ? 1009 HOH   A O      1 
HETATM 7975 O O      . HOH   IA 8 .   ? 8.884  -103.891 -21.916 1.00 37.86  ? 1010 HOH   A O      1 
HETATM 7976 O O      . HOH   IA 8 .   ? 4.118  -97.016  -23.540 1.00 33.99  ? 1011 HOH   A O      1 
HETATM 7977 O O      . HOH   IA 8 .   ? 20.275 -46.302  4.145   1.00 41.11  ? 1012 HOH   A O      1 
HETATM 7978 O O      . HOH   IA 8 .   ? 33.163 -48.824  -21.516 1.00 44.69  ? 1013 HOH   A O      1 
HETATM 7979 O O      . HOH   IA 8 .   ? 13.908 -112.121 -21.753 1.00 41.17  ? 1014 HOH   A O      1 
HETATM 7980 O O      . HOH   IA 8 .   ? 14.409 -23.030  -19.634 1.00 37.99  ? 1015 HOH   A O      1 
HETATM 7981 O O      . HOH   IA 8 .   ? 12.936 -40.738  2.970   1.00 47.83  ? 1016 HOH   A O      1 
HETATM 7982 O O      . HOH   IA 8 .   ? 29.193 -81.907  -38.950 1.00 51.84  ? 1017 HOH   A O      1 
HETATM 7983 O O      . HOH   IA 8 .   ? -2.460 -42.834  -17.831 1.00 41.61  ? 1018 HOH   A O      1 
HETATM 7984 O O      . HOH   IA 8 .   ? 9.683  -58.026  -5.199  1.00 34.50  ? 1019 HOH   A O      1 
HETATM 7985 O O      . HOH   IA 8 .   ? 30.796 -27.912  -29.078 1.00 57.25  ? 1020 HOH   A O      1 
HETATM 7986 O O      . HOH   IA 8 .   ? -0.794 -64.042  -24.115 1.00 37.10  ? 1021 HOH   A O      1 
HETATM 7987 O O      . HOH   IA 8 .   ? 20.495 -48.654  -7.340  1.00 28.10  ? 1022 HOH   A O      1 
HETATM 7988 O O      . HOH   IA 8 .   ? 18.788 -92.257  -6.197  1.00 35.69  ? 1023 HOH   A O      1 
HETATM 7989 O O      . HOH   IA 8 .   ? 4.096  -101.649 -30.294 1.00 45.89  ? 1024 HOH   A O      1 
HETATM 7990 O O      . HOH   IA 8 .   ? 34.504 -32.217  -17.746 1.00 34.64  ? 1025 HOH   A O      1 
HETATM 7991 O O      . HOH   IA 8 .   ? 0.717  -66.455  -25.049 1.00 43.25  ? 1026 HOH   A O      1 
HETATM 7992 O O      . HOH   IA 8 .   ? 35.789 -87.258  -1.268  1.00 39.97  ? 1027 HOH   A O      1 
HETATM 7993 O O      . HOH   IA 8 .   ? 34.495 -34.314  -14.017 1.00 47.04  ? 1028 HOH   A O      1 
HETATM 7994 O O      . HOH   IA 8 .   ? 35.417 -92.835  -26.986 1.00 35.89  ? 1029 HOH   A O      1 
HETATM 7995 O O      . HOH   IA 8 .   ? 18.301 -51.427  -7.953  1.00 44.51  ? 1030 HOH   A O      1 
HETATM 7996 O O      . HOH   IA 8 .   ? 1.188  -43.387  -29.132 1.00 52.40  ? 1031 HOH   A O      1 
HETATM 7997 O O      . HOH   IA 8 .   ? 30.735 -13.105  -23.795 1.00 48.41  ? 1032 HOH   A O      1 
HETATM 7998 O O      . HOH   IA 8 .   ? 18.032 -85.795  -37.782 1.00 31.65  ? 1033 HOH   A O      1 
HETATM 7999 O O      . HOH   IA 8 .   ? 10.345 -74.013  -43.903 1.00 45.64  ? 1034 HOH   A O      1 
HETATM 8000 O O      . HOH   IA 8 .   ? 6.532  -33.632  -0.359  1.00 53.01  ? 1035 HOH   A O      1 
HETATM 8001 O O      . HOH   IA 8 .   ? 16.029 -40.094  -7.513  1.00 35.63  ? 1036 HOH   A O      1 
HETATM 8002 O O      . HOH   IA 8 .   ? 36.554 -30.802  -7.206  1.00 42.73  ? 1037 HOH   A O      1 
HETATM 8003 O O      . HOH   IA 8 .   ? 6.870  -32.593  -20.426 1.00 41.36  ? 1038 HOH   A O      1 
HETATM 8004 O O      . HOH   IA 8 .   ? 1.769  -67.421  -27.954 1.00 33.99  ? 1039 HOH   A O      1 
HETATM 8005 O O      . HOH   IA 8 .   ? 34.729 -67.447  -20.453 1.00 56.15  ? 1040 HOH   A O      1 
HETATM 8006 O O      . HOH   IA 8 .   ? 14.202 -53.117  -36.234 1.00 34.83  ? 1041 HOH   A O      1 
HETATM 8007 O O      . HOH   IA 8 .   ? 27.864 -46.994  -29.224 1.00 47.44  ? 1042 HOH   A O      1 
HETATM 8008 O O      . HOH   IA 8 .   ? 9.657  -70.981  -43.715 1.00 45.13  ? 1043 HOH   A O      1 
HETATM 8009 O O      . HOH   IA 8 .   ? 30.284 -48.444  -22.580 1.00 40.88  ? 1044 HOH   A O      1 
HETATM 8010 O O      . HOH   IA 8 .   ? 34.566 -69.243  -42.521 1.00 42.83  ? 1045 HOH   A O      1 
HETATM 8011 O O      . HOH   IA 8 .   ? 19.908 -85.737  -9.724  1.00 49.81  ? 1046 HOH   A O      1 
HETATM 8012 O O      . HOH   IA 8 .   ? -0.206 -62.206  -20.075 1.00 29.33  ? 1047 HOH   A O      1 
HETATM 8013 O O      . HOH   IA 8 .   ? 2.737  -96.730  -20.356 1.00 53.64  ? 1048 HOH   A O      1 
HETATM 8014 O O      . HOH   IA 8 .   ? 47.086 -88.488  -22.183 1.00 55.97  ? 1049 HOH   A O      1 
HETATM 8015 O O      . HOH   IA 8 .   ? -3.407 -45.036  -2.950  1.00 49.43  ? 1050 HOH   A O      1 
HETATM 8016 O O      . HOH   IA 8 .   ? 26.758 -78.402  -13.947 1.00 34.43  ? 1051 HOH   A O      1 
HETATM 8017 O O      . HOH   IA 8 .   ? 13.080 -29.336  -24.228 1.00 43.54  ? 1052 HOH   A O      1 
HETATM 8018 O O      . HOH   IA 8 .   ? 27.245 -65.657  -18.527 1.00 33.51  ? 1053 HOH   A O      1 
HETATM 8019 O O      . HOH   IA 8 .   ? 25.588 -62.813  -25.128 1.00 42.15  ? 1054 HOH   A O      1 
HETATM 8020 O O      . HOH   IA 8 .   ? 26.411 -88.640  -29.820 1.00 41.66  ? 1055 HOH   A O      1 
HETATM 8021 O O      . HOH   IA 8 .   ? 9.494  -56.914  -40.339 1.00 52.66  ? 1056 HOH   A O      1 
HETATM 8022 O O      . HOH   IA 8 .   ? 17.092 -58.492  -34.744 1.00 66.68  ? 1057 HOH   A O      1 
HETATM 8023 O O      . HOH   IA 8 .   ? 17.514 -37.025  -25.811 1.00 38.70  ? 1058 HOH   A O      1 
HETATM 8024 O O      . HOH   IA 8 .   ? 10.703 -59.991  -42.085 1.00 59.57  ? 1059 HOH   A O      1 
HETATM 8025 O O      . HOH   IA 8 .   ? 28.438 -56.781  -18.281 1.00 41.86  ? 1060 HOH   A O      1 
HETATM 8026 O O      . HOH   IA 8 .   ? 9.640  -97.614  -15.077 1.00 42.60  ? 1061 HOH   A O      1 
HETATM 8027 O O      . HOH   IA 8 .   ? 23.298 -86.733  -29.370 1.00 38.55  ? 1062 HOH   A O      1 
HETATM 8028 O O      . HOH   IA 8 .   ? 36.412 -91.002  -28.740 1.00 46.90  ? 1063 HOH   A O      1 
HETATM 8029 O O      . HOH   IA 8 .   ? 17.184 -55.460  -33.780 1.00 55.27  ? 1064 HOH   A O      1 
HETATM 8030 O O      . HOH   IA 8 .   ? 14.823 -101.241 -24.858 1.00 59.39  ? 1065 HOH   A O      1 
HETATM 8031 O O      . HOH   IA 8 .   ? 39.525 -84.269  -39.808 1.00 46.78  ? 1066 HOH   A O      1 
HETATM 8032 O O      . HOH   IA 8 .   ? 5.947  -104.244 -22.051 1.00 43.65  ? 1067 HOH   A O      1 
HETATM 8033 O O      . HOH   IA 8 .   ? 21.060 -85.207  -33.115 1.00 29.71  ? 1068 HOH   A O      1 
HETATM 8034 O O      . HOH   IA 8 .   ? 17.116 -41.417  -5.396  1.00 31.31  ? 1069 HOH   A O      1 
HETATM 8035 O O      . HOH   IA 8 .   ? 17.753 -62.689  -39.217 1.00 48.53  ? 1070 HOH   A O      1 
HETATM 8036 O O      . HOH   IA 8 .   ? 6.503  -90.749  -11.255 1.00 36.39  ? 1071 HOH   A O      1 
HETATM 8037 O O      . HOH   IA 8 .   ? 10.194 -53.712  -7.063  1.00 44.30  ? 1072 HOH   A O      1 
HETATM 8038 O O      . HOH   IA 8 .   ? 16.925 -47.377  -1.535  1.00 36.34  ? 1073 HOH   A O      1 
HETATM 8039 O O      . HOH   IA 8 .   ? 35.612 -44.873  -19.880 1.00 37.99  ? 1074 HOH   A O      1 
HETATM 8040 O O      . HOH   IA 8 .   ? 8.830  -91.730  -12.274 1.00 37.36  ? 1075 HOH   A O      1 
HETATM 8041 O O      . HOH   IA 8 .   ? 14.328 -88.215  -36.731 1.00 42.67  ? 1076 HOH   A O      1 
HETATM 8042 O O      . HOH   IA 8 .   ? 23.585 -84.452  -33.810 1.00 36.95  ? 1077 HOH   A O      1 
HETATM 8043 O O      . HOH   IA 8 .   ? 25.161 -51.526  -23.960 1.00 40.03  ? 1078 HOH   A O      1 
HETATM 8044 O O      . HOH   IA 8 .   ? 22.831 -88.990  -33.321 1.00 41.51  ? 1079 HOH   A O      1 
HETATM 8045 O O      . HOH   IA 8 .   ? 13.714 -95.187  -31.823 1.00 32.02  ? 1080 HOH   A O      1 
HETATM 8046 O O      . HOH   IA 8 .   ? 24.681 -87.048  -33.548 1.00 39.67  ? 1081 HOH   A O      1 
HETATM 8047 O O      . HOH   JA 8 .   ? 31.203 -107.765 -51.237 1.00 29.95  ? 501  HOH   B O      1 
HETATM 8048 O O      . HOH   JA 8 .   ? 13.012 -97.746  -31.292 1.00 29.80  ? 502  HOH   B O      1 
HETATM 8049 O O      . HOH   JA 8 .   ? 30.397 -125.586 -25.957 1.00 45.92  ? 503  HOH   B O      1 
HETATM 8050 O O      . HOH   JA 8 .   ? 18.170 -99.760  -36.356 1.00 25.75  ? 504  HOH   B O      1 
HETATM 8051 O O      . HOH   JA 8 .   ? 37.195 -98.977  -13.672 1.00 30.24  ? 505  HOH   B O      1 
HETATM 8052 O O      . HOH   JA 8 .   ? 29.748 -107.788 -26.148 1.00 41.39  ? 506  HOH   B O      1 
HETATM 8053 O O      . HOH   JA 8 .   ? 42.456 -101.765 -53.232 1.00 105.08 ? 507  HOH   B O      1 
HETATM 8054 O O      . HOH   JA 8 .   ? 44.039 -105.206 -48.955 1.00 60.39  ? 508  HOH   B O      1 
HETATM 8055 O O      . HOH   JA 8 .   ? 14.655 -109.916 -23.185 1.00 44.83  ? 509  HOH   B O      1 
HETATM 8056 O O      . HOH   JA 8 .   ? 34.068 -94.493  -28.650 1.00 42.51  ? 510  HOH   B O      1 
HETATM 8057 O O      . HOH   JA 8 .   ? 49.677 -98.535  -41.000 1.00 44.72  ? 511  HOH   B O      1 
HETATM 8058 O O      . HOH   JA 8 .   ? 37.871 -96.588  -37.041 1.00 43.72  ? 512  HOH   B O      1 
HETATM 8059 O O      . HOH   JA 8 .   ? 24.190 -102.659 -57.978 1.00 37.32  ? 513  HOH   B O      1 
HETATM 8060 O O      . HOH   JA 8 .   ? 40.903 -100.193 -29.596 1.00 41.14  ? 514  HOH   B O      1 
HETATM 8061 O O      . HOH   JA 8 .   ? 12.222 -113.664 -23.550 1.00 37.83  ? 515  HOH   B O      1 
HETATM 8062 O O      . HOH   JA 8 .   ? 47.794 -114.410 -28.048 1.00 45.00  ? 516  HOH   B O      1 
HETATM 8063 O O      . HOH   JA 8 .   ? 26.558 -120.717 -42.953 1.00 44.35  ? 517  HOH   B O      1 
HETATM 8064 O O      . HOH   JA 8 .   ? 11.714 -107.451 -41.051 1.00 33.07  ? 518  HOH   B O      1 
HETATM 8065 O O      . HOH   JA 8 .   ? 23.178 -112.313 -52.409 1.00 53.25  ? 519  HOH   B O      1 
HETATM 8066 O O      . HOH   JA 8 .   ? 26.451 -92.984  -29.085 1.00 40.76  ? 520  HOH   B O      1 
HETATM 8067 O O      . HOH   JA 8 .   ? 24.783 -113.394 -41.758 1.00 32.11  ? 521  HOH   B O      1 
HETATM 8068 O O      . HOH   JA 8 .   ? 33.534 -89.812  -37.963 1.00 53.09  ? 522  HOH   B O      1 
HETATM 8069 O O      . HOH   JA 8 .   ? 21.649 -99.219  -34.039 1.00 37.10  ? 523  HOH   B O      1 
HETATM 8070 O O      . HOH   JA 8 .   ? 5.703  -108.347 -30.809 1.00 55.24  ? 524  HOH   B O      1 
HETATM 8071 O O      . HOH   JA 8 .   ? 38.273 -91.604  -41.997 1.00 46.60  ? 525  HOH   B O      1 
HETATM 8072 O O      . HOH   JA 8 .   ? 32.392 -110.283 -43.164 1.00 35.55  ? 526  HOH   B O      1 
HETATM 8073 O O      . HOH   JA 8 .   ? 6.874  -109.338 -34.898 1.00 48.66  ? 527  HOH   B O      1 
HETATM 8074 O O      . HOH   JA 8 .   ? 24.781 -108.633 -55.320 1.00 59.70  ? 528  HOH   B O      1 
HETATM 8075 O O      . HOH   JA 8 .   ? 27.168 -105.480 -30.851 1.00 37.32  ? 529  HOH   B O      1 
HETATM 8076 O O      . HOH   JA 8 .   ? 46.247 -110.781 -23.893 1.00 38.72  ? 530  HOH   B O      1 
HETATM 8077 O O      . HOH   JA 8 .   ? 27.780 -90.060  -31.824 1.00 48.08  ? 531  HOH   B O      1 
HETATM 8078 O O      . HOH   JA 8 .   ? 26.828 -103.407 -32.531 1.00 38.07  ? 532  HOH   B O      1 
HETATM 8079 O O      . HOH   JA 8 .   ? 18.389 -121.735 -52.847 1.00 52.27  ? 533  HOH   B O      1 
HETATM 8080 O O      . HOH   JA 8 .   ? 34.135 -127.758 -35.608 1.00 49.98  ? 534  HOH   B O      1 
HETATM 8081 O O      . HOH   JA 8 .   ? 26.506 -93.332  -43.308 1.00 28.59  ? 535  HOH   B O      1 
HETATM 8082 O O      . HOH   JA 8 .   ? 18.151 -119.750 -26.979 1.00 27.61  ? 536  HOH   B O      1 
HETATM 8083 O O      . HOH   JA 8 .   ? 44.344 -115.130 -43.469 1.00 52.04  ? 537  HOH   B O      1 
HETATM 8084 O O      . HOH   JA 8 .   ? 47.430 -117.031 -27.151 1.00 47.49  ? 538  HOH   B O      1 
HETATM 8085 O O      . HOH   JA 8 .   ? 20.097 -129.565 -30.449 1.00 50.85  ? 539  HOH   B O      1 
HETATM 8086 O O      . HOH   JA 8 .   ? 20.377 -110.348 -28.746 1.00 32.51  ? 540  HOH   B O      1 
HETATM 8087 O O      . HOH   JA 8 .   ? 22.024 -98.243  -29.341 1.00 42.34  ? 541  HOH   B O      1 
HETATM 8088 O O      . HOH   JA 8 .   ? 35.046 -100.725 -23.734 1.00 35.73  ? 542  HOH   B O      1 
HETATM 8089 O O      . HOH   JA 8 .   ? 44.431 -94.187  -35.965 1.00 47.58  ? 543  HOH   B O      1 
HETATM 8090 O O      . HOH   JA 8 .   ? 47.517 -105.020 -42.874 1.00 44.68  ? 544  HOH   B O      1 
HETATM 8091 O O      . HOH   JA 8 .   ? 26.050 -117.478 -43.557 1.00 49.51  ? 545  HOH   B O      1 
HETATM 8092 O O      . HOH   JA 8 .   ? 24.440 -103.218 -34.031 1.00 31.17  ? 546  HOH   B O      1 
HETATM 8093 O O      . HOH   JA 8 .   ? 3.916  -114.370 -38.736 1.00 49.91  ? 547  HOH   B O      1 
HETATM 8094 O O      . HOH   JA 8 .   ? 25.191 -110.398 -42.753 1.00 38.84  ? 548  HOH   B O      1 
HETATM 8095 O O      . HOH   JA 8 .   ? 45.758 -101.498 -52.210 1.00 54.76  ? 549  HOH   B O      1 
HETATM 8096 O O      . HOH   JA 8 .   ? 26.739 -111.460 -54.448 1.00 35.57  ? 550  HOH   B O      1 
HETATM 8097 O O      . HOH   JA 8 .   ? 20.265 -114.372 -17.269 1.00 52.22  ? 551  HOH   B O      1 
HETATM 8098 O O      . HOH   JA 8 .   ? 33.357 -103.710 -22.998 1.00 27.82  ? 552  HOH   B O      1 
HETATM 8099 O O      . HOH   JA 8 .   ? 30.033 -109.201 -38.802 1.00 40.38  ? 553  HOH   B O      1 
HETATM 8100 O O      . HOH   JA 8 .   ? 24.248 -115.245 -43.705 1.00 28.75  ? 554  HOH   B O      1 
HETATM 8101 O O      . HOH   JA 8 .   ? 32.480 -96.235  -62.108 1.00 44.88  ? 555  HOH   B O      1 
HETATM 8102 O O      . HOH   JA 8 .   ? 20.610 -89.112  -34.986 1.00 25.92  ? 556  HOH   B O      1 
HETATM 8103 O O      . HOH   JA 8 .   ? 39.530 -103.181 -28.766 1.00 42.26  ? 557  HOH   B O      1 
HETATM 8104 O O      . HOH   JA 8 .   ? 23.678 -95.871  -56.994 1.00 46.38  ? 558  HOH   B O      1 
HETATM 8105 O O      . HOH   JA 8 .   ? 14.636 -97.978  -46.578 1.00 32.34  ? 559  HOH   B O      1 
HETATM 8106 O O      . HOH   JA 8 .   ? 31.190 -108.386 -17.320 1.00 47.47  ? 560  HOH   B O      1 
HETATM 8107 O O      . HOH   JA 8 .   ? 31.773 -87.280  -36.723 1.00 42.59  ? 561  HOH   B O      1 
HETATM 8108 O O      . HOH   JA 8 .   ? 15.233 -118.443 -23.974 1.00 39.24  ? 562  HOH   B O      1 
HETATM 8109 O O      . HOH   JA 8 .   ? 27.384 -119.633 -40.523 1.00 33.82  ? 563  HOH   B O      1 
HETATM 8110 O O      . HOH   JA 8 .   ? 7.046  -105.672 -37.317 1.00 43.00  ? 564  HOH   B O      1 
HETATM 8111 O O      . HOH   JA 8 .   ? 15.556 -100.622 -32.273 1.00 33.79  ? 565  HOH   B O      1 
HETATM 8112 O O      . HOH   JA 8 .   ? 7.165  -114.973 -31.458 1.00 63.12  ? 566  HOH   B O      1 
HETATM 8113 O O      . HOH   JA 8 .   ? 13.581 -93.037  -37.319 1.00 41.63  ? 567  HOH   B O      1 
HETATM 8114 O O      . HOH   JA 8 .   ? 35.508 -92.955  -30.397 1.00 53.31  ? 568  HOH   B O      1 
HETATM 8115 O O      . HOH   JA 8 .   ? 20.746 -122.513 -18.818 1.00 62.41  ? 569  HOH   B O      1 
HETATM 8116 O O      . HOH   JA 8 .   ? 28.095 -123.214 -22.391 1.00 42.72  ? 570  HOH   B O      1 
HETATM 8117 O O      . HOH   JA 8 .   ? 34.156 -108.507 -56.977 1.00 52.69  ? 571  HOH   B O      1 
HETATM 8118 O O      . HOH   JA 8 .   ? 28.325 -110.556 -33.937 1.00 45.14  ? 572  HOH   B O      1 
HETATM 8119 O O      . HOH   JA 8 .   ? 43.047 -94.230  -42.355 1.00 55.53  ? 573  HOH   B O      1 
HETATM 8120 O O      . HOH   JA 8 .   ? 31.142 -111.405 -48.437 1.00 46.86  ? 574  HOH   B O      1 
HETATM 8121 O O      . HOH   JA 8 .   ? 9.618  -111.500 -51.320 1.00 49.59  ? 575  HOH   B O      1 
HETATM 8122 O O      . HOH   JA 8 .   ? 33.178 -114.377 -40.212 1.00 32.38  ? 576  HOH   B O      1 
HETATM 8123 O O      . HOH   JA 8 .   ? 17.255 -89.600  -37.687 1.00 42.58  ? 577  HOH   B O      1 
HETATM 8124 O O      . HOH   JA 8 .   ? 25.595 -87.137  -38.922 1.00 40.19  ? 578  HOH   B O      1 
HETATM 8125 O O      . HOH   JA 8 .   ? 35.352 -112.642 -48.292 1.00 41.41  ? 579  HOH   B O      1 
HETATM 8126 O O      . HOH   JA 8 .   ? 23.349 -110.357 -39.110 1.00 39.00  ? 580  HOH   B O      1 
HETATM 8127 O O      . HOH   JA 8 .   ? 35.179 -100.253 -52.882 1.00 51.09  ? 581  HOH   B O      1 
HETATM 8128 O O      . HOH   JA 8 .   ? 20.662 -92.638  -33.198 1.00 45.11  ? 582  HOH   B O      1 
HETATM 8129 O O      . HOH   JA 8 .   ? 15.636 -98.319  -30.589 1.00 34.45  ? 583  HOH   B O      1 
HETATM 8130 O O      . HOH   JA 8 .   ? 34.333 -131.321 -24.771 1.00 49.63  ? 584  HOH   B O      1 
HETATM 8131 O O      . HOH   JA 8 .   ? 26.448 -101.341 -30.800 1.00 41.29  ? 585  HOH   B O      1 
HETATM 8132 O O      . HOH   JA 8 .   ? 27.321 -120.504 -45.666 1.00 62.31  ? 586  HOH   B O      1 
HETATM 8133 O O      . HOH   JA 8 .   ? 30.610 -129.472 -31.890 1.00 51.10  ? 587  HOH   B O      1 
HETATM 8134 O O      . HOH   JA 8 .   ? 26.300 -118.073 -46.350 1.00 43.74  ? 588  HOH   B O      1 
# 
