data_9MGR
# 
_entry.id   9MGR 
# 
_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   9MGR         pdb_00009mgr 10.2210/pdb9mgr/pdb 
WWPDB D_1000290937 ?            ?                   
# 
_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                        9MGR 
_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 
;6-[(1-acetylazetidin-3-yl)amino]-N-[(2R)-2-hydroxy-2-{(3S)-7-[(4-methyl-1,3-oxazol-5-yl)methoxy]-1,2,3,4-tetrahydroisoquinolin-3-yl}ethyl]-2-(4-methylpiperidin-1-yl)pyrimidine-4-carboxamide
;
618.726   1   ?         ? ?             ?                      
4 non-polymer syn "5'-DEOXY-5'-METHYLTHIOADENOSINE" 297.334   1   ?         ? ?             ?                      
5 non-polymer syn 1,2-ETHANEDIOL 62.068    15  ?         ? ?             ?                      
6 water       nat water 18.015    132 ?         ? ?             ?                      
# 
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 
;6-[(1-acetylazetidin-3-yl)amino]-N-[(2R)-2-hydroxy-2-{(3S)-7-[(4-methyl-1,3-oxazol-5-yl)methoxy]-1,2,3,4-tetrahydroisoquinolin-3-yl}ethyl]-2-(4-methylpiperidin-1-yl)pyrimidine-4-carboxamide
;
A1BLF 
4 "5'-DEOXY-5'-METHYLTHIOADENOSINE" MTA   
5 1,2-ETHANEDIOL EDO   
6 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   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 
A1BLF non-polymer         . 
;6-[(1-acetylazetidin-3-yl)amino]-N-[(2R)-2-hydroxy-2-{(3S)-7-[(4-methyl-1,3-oxazol-5-yl)methoxy]-1,2,3,4-tetrahydroisoquinolin-3-yl}ethyl]-2-(4-methylpiperidin-1-yl)pyrimidine-4-carboxamide
;
?                 'C32 H42 N8 O5'   618.726 
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 
MTA   non-polymer         . "5'-DEOXY-5'-METHYLTHIOADENOSINE" ?                 'C11 H15 N5 O3 S' 297.334 
PHE   'L-peptide linking' y PHENYLALANINE ?                 'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE ?                 'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE ?                 'C3 H7 N O3'      105.093 
THR   'L-peptide linking' y THREONINE ?                 'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ?                 'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE ?                 'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE ?                 'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -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  13  ARG ARG 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 ?   ?   ?   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  ?   ?   ?   B . n 
B 2 29  PRO 29  21  ?   ?   ?   B . n 
B 2 30  ASN 30  22  ?   ?   ?   B . n 
B 2 31  ALA 31  23  ?   ?   ?   B . n 
B 2 32  PRO 32  24  ?   ?   ?   B . n 
B 2 33  ALA 33  25  ?   ?   ?   B . n 
B 2 34  CYS 34  26  ?   ?   ?   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 215 207 207 GLY GLY B . n 
B 2 216 CYS 216 208 ?   ?   ?   B . n 
B 2 217 SER 217 209 ?   ?   ?   B . n 
B 2 218 ALA 218 210 ?   ?   ?   B . n 
B 2 219 PRO 219 211 ?   ?   ?   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        A1BLF 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BLF 
_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 A1BLF 1   701 1   A1BLF LIG A . 
D 4 MTA   1   702 1   MTA   MTA A . 
E 5 EDO   1   703 1   EDO   EDO A . 
F 5 EDO   1   704 2   EDO   EDO A . 
G 5 EDO   1   705 3   EDO   EDO A . 
H 5 EDO   1   706 4   EDO   EDO A . 
I 5 EDO   1   707 5   EDO   EDO A . 
J 5 EDO   1   708 6   EDO   EDO A . 
K 5 EDO   1   709 7   EDO   EDO A . 
L 5 EDO   1   710 8   EDO   EDO A . 
M 5 EDO   1   711 10  EDO   EDO A . 
N 5 EDO   1   712 11  EDO   EDO A . 
O 5 EDO   1   713 12  EDO   EDO A . 
P 5 EDO   1   714 13  EDO   EDO A . 
Q 5 EDO   1   715 14  EDO   EDO A . 
R 5 EDO   1   716 15  EDO   EDO A . 
S 5 EDO   1   401 9   EDO   EDO B . 
T 6 HOH   1   801 125 HOH   HOH A . 
T 6 HOH   2   802 107 HOH   HOH A . 
T 6 HOH   3   803 95  HOH   HOH A . 
T 6 HOH   4   804 54  HOH   HOH A . 
T 6 HOH   5   805 90  HOH   HOH A . 
T 6 HOH   6   806 53  HOH   HOH A . 
T 6 HOH   7   807 38  HOH   HOH A . 
T 6 HOH   8   808 58  HOH   HOH A . 
T 6 HOH   9   809 25  HOH   HOH A . 
T 6 HOH   10  810 33  HOH   HOH A . 
T 6 HOH   11  811 128 HOH   HOH A . 
T 6 HOH   12  812 8   HOH   HOH A . 
T 6 HOH   13  813 23  HOH   HOH A . 
T 6 HOH   14  814 122 HOH   HOH A . 
T 6 HOH   15  815 75  HOH   HOH A . 
T 6 HOH   16  816 102 HOH   HOH A . 
T 6 HOH   17  817 48  HOH   HOH A . 
T 6 HOH   18  818 43  HOH   HOH A . 
T 6 HOH   19  819 41  HOH   HOH A . 
T 6 HOH   20  820 121 HOH   HOH A . 
T 6 HOH   21  821 42  HOH   HOH A . 
T 6 HOH   22  822 44  HOH   HOH A . 
T 6 HOH   23  823 40  HOH   HOH A . 
T 6 HOH   24  824 6   HOH   HOH A . 
T 6 HOH   25  825 50  HOH   HOH A . 
T 6 HOH   26  826 59  HOH   HOH A . 
T 6 HOH   27  827 29  HOH   HOH A . 
T 6 HOH   28  828 16  HOH   HOH A . 
T 6 HOH   29  829 51  HOH   HOH A . 
T 6 HOH   30  830 24  HOH   HOH A . 
T 6 HOH   31  831 65  HOH   HOH A . 
T 6 HOH   32  832 55  HOH   HOH A . 
T 6 HOH   33  833 127 HOH   HOH A . 
T 6 HOH   34  834 93  HOH   HOH A . 
T 6 HOH   35  835 30  HOH   HOH A . 
T 6 HOH   36  836 82  HOH   HOH A . 
T 6 HOH   37  837 27  HOH   HOH A . 
T 6 HOH   38  838 52  HOH   HOH A . 
T 6 HOH   39  839 19  HOH   HOH A . 
T 6 HOH   40  840 105 HOH   HOH A . 
T 6 HOH   41  841 83  HOH   HOH A . 
T 6 HOH   42  842 15  HOH   HOH A . 
T 6 HOH   43  843 106 HOH   HOH A . 
T 6 HOH   44  844 3   HOH   HOH A . 
T 6 HOH   45  845 99  HOH   HOH A . 
T 6 HOH   46  846 112 HOH   HOH A . 
T 6 HOH   47  847 36  HOH   HOH A . 
T 6 HOH   48  848 35  HOH   HOH A . 
T 6 HOH   49  849 26  HOH   HOH A . 
T 6 HOH   50  850 37  HOH   HOH A . 
T 6 HOH   51  851 21  HOH   HOH A . 
T 6 HOH   52  852 12  HOH   HOH A . 
T 6 HOH   53  853 73  HOH   HOH A . 
T 6 HOH   54  854 86  HOH   HOH A . 
T 6 HOH   55  855 85  HOH   HOH A . 
T 6 HOH   56  856 101 HOH   HOH A . 
T 6 HOH   57  857 68  HOH   HOH A . 
T 6 HOH   58  858 88  HOH   HOH A . 
T 6 HOH   59  859 87  HOH   HOH A . 
T 6 HOH   60  860 96  HOH   HOH A . 
T 6 HOH   61  861 34  HOH   HOH A . 
T 6 HOH   62  862 1   HOH   HOH A . 
T 6 HOH   63  863 18  HOH   HOH A . 
T 6 HOH   64  864 5   HOH   HOH A . 
T 6 HOH   65  865 32  HOH   HOH A . 
T 6 HOH   66  866 17  HOH   HOH A . 
T 6 HOH   67  867 22  HOH   HOH A . 
T 6 HOH   68  868 20  HOH   HOH A . 
T 6 HOH   69  869 104 HOH   HOH A . 
T 6 HOH   70  870 98  HOH   HOH A . 
T 6 HOH   71  871 28  HOH   HOH A . 
T 6 HOH   72  872 76  HOH   HOH A . 
T 6 HOH   73  873 4   HOH   HOH A . 
T 6 HOH   74  874 64  HOH   HOH A . 
T 6 HOH   75  875 13  HOH   HOH A . 
T 6 HOH   76  876 2   HOH   HOH A . 
T 6 HOH   77  877 111 HOH   HOH A . 
T 6 HOH   78  878 97  HOH   HOH A . 
T 6 HOH   79  879 100 HOH   HOH A . 
T 6 HOH   80  880 14  HOH   HOH A . 
T 6 HOH   81  881 79  HOH   HOH A . 
T 6 HOH   82  882 72  HOH   HOH A . 
T 6 HOH   83  883 11  HOH   HOH A . 
T 6 HOH   84  884 129 HOH   HOH A . 
T 6 HOH   85  885 115 HOH   HOH A . 
T 6 HOH   86  886 78  HOH   HOH A . 
T 6 HOH   87  887 131 HOH   HOH A . 
T 6 HOH   88  888 56  HOH   HOH A . 
T 6 HOH   89  889 67  HOH   HOH A . 
T 6 HOH   90  890 116 HOH   HOH A . 
T 6 HOH   91  891 71  HOH   HOH A . 
T 6 HOH   92  892 120 HOH   HOH A . 
T 6 HOH   93  893 49  HOH   HOH A . 
T 6 HOH   94  894 94  HOH   HOH A . 
T 6 HOH   95  895 103 HOH   HOH A . 
T 6 HOH   96  896 80  HOH   HOH A . 
T 6 HOH   97  897 89  HOH   HOH A . 
T 6 HOH   98  898 47  HOH   HOH A . 
T 6 HOH   99  899 84  HOH   HOH A . 
T 6 HOH   100 900 63  HOH   HOH A . 
T 6 HOH   101 901 45  HOH   HOH A . 
T 6 HOH   102 902 109 HOH   HOH A . 
T 6 HOH   103 903 77  HOH   HOH A . 
T 6 HOH   104 904 108 HOH   HOH A . 
T 6 HOH   105 905 57  HOH   HOH A . 
T 6 HOH   106 906 132 HOH   HOH A . 
T 6 HOH   107 907 130 HOH   HOH A . 
T 6 HOH   108 908 66  HOH   HOH A . 
T 6 HOH   109 909 119 HOH   HOH A . 
T 6 HOH   110 910 74  HOH   HOH A . 
T 6 HOH   111 911 70  HOH   HOH A . 
T 6 HOH   112 912 113 HOH   HOH A . 
T 6 HOH   113 913 46  HOH   HOH A . 
T 6 HOH   114 914 81  HOH   HOH A . 
T 6 HOH   115 915 91  HOH   HOH A . 
U 6 HOH   1   501 60  HOH   HOH B . 
U 6 HOH   2   502 39  HOH   HOH B . 
U 6 HOH   3   503 126 HOH   HOH B . 
U 6 HOH   4   504 10  HOH   HOH B . 
U 6 HOH   5   505 124 HOH   HOH B . 
U 6 HOH   6   506 31  HOH   HOH B . 
U 6 HOH   7   507 62  HOH   HOH B . 
U 6 HOH   8   508 123 HOH   HOH B . 
U 6 HOH   9   509 7   HOH   HOH B . 
U 6 HOH   10  510 9   HOH   HOH B . 
U 6 HOH   11  511 114 HOH   HOH B . 
U 6 HOH   12  512 61  HOH   HOH B . 
U 6 HOH   13  513 118 HOH   HOH B . 
U 6 HOH   14  514 69  HOH   HOH B . 
U 6 HOH   15  515 92  HOH   HOH B . 
U 6 HOH   16  516 117 HOH   HOH B . 
U 6 HOH   17  517 110 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       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0425 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? DIALS  ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? DIALS  ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? .        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                     9MGR 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     102.946 
_cell.length_a_esd                 ? 
_cell.length_b                     137.889 
_cell.length_b_esd                 ? 
_cell.length_c                     178.607 
_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                         9MGR 
_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                   9MGR 
_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             2.84 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.68 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.0 
_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    '10% PEG 4000, 0.1 M  sodium citrate (pH 6.0), 0.2 M magnesium chloride' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-06-21 
_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                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9MGR 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.07 
_reflns.d_resolution_low                               109.15 
_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                                     36863 
_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                           93.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.9 
_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                                0.045 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.160 
_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 
7.41 109.15 ? 42.2 ? ? ? ? 1843 ? ? ? ? ? ? ? ? ? ? ? 13.3 ? ? ? ? 0.012 ? 1 1 0.999 ? ? 100  ? 0.042 ? ? ? ? ? ? ? ? ? 
2.07 2.365  ? 1.9  ? ? ? ? 1843 ? ? ? ? ? ? ? ? ? ? ? 11.1 ? ? ? ? 0.420 ? 2 1 0.758 ? ? 81.5 ? 1.343 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            0.46 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            -0.38 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.09 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               42.548 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.923 
_refine.correlation_coeff_Fo_to_Fc_free          0.875 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 9MGR 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.07 
_refine.ls_d_res_low                             109.15 
_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                     35038 
_refine.ls_number_reflns_R_free                  1825 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    47.64 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.22410 
_refine.ls_R_factor_R_free                       0.27273 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.22165 
_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                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.815 
_refine.pdbx_overall_ESU_R_Free                  0.345 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             6.928 
_refine.overall_SU_ML                            0.180 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.07 
_refine_hist.d_res_low                        109.15 
_refine_hist.number_atoms_solvent             132 
_refine_hist.number_atoms_total               7570 
_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        7313 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         125 
_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' ? 0.002  0.012  7789  ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  7209  ? r_bond_other_d         ? ? 
'X-RAY DIFFRACTION' ? 1.005  1.830  10599 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 0.356  1.758  16637 ? r_angle_other_deg      ? ? 
'X-RAY DIFFRACTION' ? 7.250  5.000  953   ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 5.608  5.000  51    ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.888 10.000 1258  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 0.045  0.200  1154  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.003  0.020  9266  ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1815  ? r_gen_planes_other     ? ? 
'X-RAY DIFFRACTION' ? 1.370  4.380  3773  ? r_mcbond_it            ? ? 
'X-RAY DIFFRACTION' ? 1.370  4.380  3773  ? r_mcbond_other         ? ? 
'X-RAY DIFFRACTION' ? 2.467  7.858  4739  ? r_mcangle_it           ? ? 
'X-RAY DIFFRACTION' ? 2.467  7.859  4740  ? r_mcangle_other        ? ? 
'X-RAY DIFFRACTION' ? 0.995  4.421  4016  ? r_scbond_it            ? ? 
'X-RAY DIFFRACTION' ? 0.995  4.421  4017  ? r_scbond_other         ? ? 
'X-RAY DIFFRACTION' ? 1.845  8.103  5859  ? r_scangle_other        ? ? 
'X-RAY DIFFRACTION' ? 4.455  40.94  8501  ? r_long_range_B_refined ? ? 
'X-RAY DIFFRACTION' ? 4.454  40.94  8500  ? r_long_range_B_other   ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.071 
_refine_ls_shell.d_res_low                        2.125 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             7 
_refine_ls_shell.number_reflns_R_work             140 
_refine_ls_shell.percent_reflns_obs               2.59 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.318 
_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                  0.432 
# 
_struct.entry_id                     9MGR 
_struct.title                        'Crystal structure of PRMT5:MEP50 in complex with MTA and compound 51' 
_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        9MGR 
_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 6 ? 
U N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP 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 9MGR A 10 ? 645 ? O14744 2 ? 637 ? 2 637 
2 2 9MGR 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 9MGR MET A 1 ? UNP O14744 ? ? 'initiating methionine' -7 1  
1 9MGR ASP A 2 ? UNP O14744 ? ? 'expression tag'        -6 2  
1 9MGR TYR A 3 ? UNP O14744 ? ? 'expression tag'        -5 3  
1 9MGR LYS A 4 ? UNP O14744 ? ? 'expression tag'        -4 4  
1 9MGR ASP A 5 ? UNP O14744 ? ? 'expression tag'        -3 5  
1 9MGR ASP A 6 ? UNP O14744 ? ? 'expression tag'        -2 6  
1 9MGR ASP A 7 ? UNP O14744 ? ? 'expression tag'        -1 7  
1 9MGR ASP A 8 ? UNP O14744 ? ? 'expression tag'        0  8  
1 9MGR LYS A 9 ? UNP O14744 ? ? 'expression tag'        1  9  
2 9MGR MET B 1 ? UNP Q9BQA1 ? ? 'initiating methionine' -7 10 
2 9MGR HIS B 2 ? UNP Q9BQA1 ? ? 'expression tag'        -6 11 
2 9MGR HIS B 3 ? UNP Q9BQA1 ? ? 'expression tag'        -5 12 
2 9MGR HIS B 4 ? UNP Q9BQA1 ? ? 'expression tag'        -4 13 
2 9MGR HIS B 5 ? UNP Q9BQA1 ? ? 'expression tag'        -3 14 
2 9MGR HIS B 6 ? UNP Q9BQA1 ? ? 'expression tag'        -2 15 
2 9MGR HIS B 7 ? UNP Q9BQA1 ? ? 'expression tag'        -1 16 
2 9MGR HIS B 8 ? UNP Q9BQA1 ? ? 'expression tag'        0  17 
2 9MGR HIS B 9 ? UNP Q9BQA1 ? ? 'expression tag'        1  18 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   octameric 
_pdbx_struct_assembly.oligomeric_count     8 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 46710  ? 
1 MORE         83     ? 
1 'SSA (A^2)'  130840 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3,4 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U 
# 
_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 -137.8890000000 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 -137.8890000000 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  ? GLY A 45  ? GLU A 25  GLY A 37  1 ? 13 
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 ? LEU A 171 ? ALA A 159 LEU A 163 5 ? 5  
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 PHE A 285 ? ASN A 298 ? PHE A 277 ASN A 290 1 ? 14 
HELX_P HELX_P14 AB5 GLU A 328 ? LYS A 337 ? GLU A 320 LYS A 329 1 ? 10 
HELX_P HELX_P15 AB6 ASP A 338 ? VAL A 357 ? ASP A 330 VAL A 349 1 ? 20 
HELX_P HELX_P16 AB7 PRO A 358 ? LYS A 362 ? PRO A 350 LYS A 354 5 ? 5  
HELX_P HELX_P17 AB8 GLY A 377 ? ASP A 391 ? GLY A 369 ASP A 383 1 ? 15 
HELX_P HELX_P18 AB9 ASN A 402 ? GLU A 416 ? ASN A 394 GLU A 408 1 ? 15 
HELX_P HELX_P19 AC1 TRP A 417 ? SER A 419 ? TRP A 409 SER A 411 5 ? 3  
HELX_P HELX_P20 AC2 ALA A 449 ? GLU A 452 ? ALA A 441 GLU A 444 5 ? 4  
HELX_P HELX_P21 AC3 LEU A 453 ? GLN A 462 ? LEU A 445 GLN A 454 1 ? 10 
HELX_P HELX_P22 AC4 SER A 485 ? ALA A 494 ? SER A 477 ALA A 486 1 ? 10 
HELX_P HELX_P23 AC5 GLU A 503 ? MET A 508 ? GLU A 495 MET A 500 5 ? 6  
HELX_P HELX_P24 AC6 ARG A 576 ? HIS A 580 ? ARG A 568 HIS A 572 5 ? 5  
HELX_P HELX_P25 AC7 ASN A 635 ? ARG A 639 ? ASN A 627 ARG A 631 5 ? 5  
HELX_P HELX_P26 AC8 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 3.44  
2 GLY 72  A . ? GLY 64  A PRO 73  A ? PRO 65  A 1 -3.90 
3 ILE 472 A . ? ILE 464 A PRO 473 A ? PRO 465 A 1 3.43  
4 HIS 531 A . ? HIS 523 A PRO 532 A ? PRO 524 A 1 -4.90 
5 ALA 627 A . ? ALA 619 A PRO 628 A ? PRO 620 A 1 4.17  
6 ALA 75  B . ? ALA 67  B PRO 76  B ? PRO 68  B 1 5.00  
# 
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 ? SER A 442 ? ALA A 429 SER A 434 
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 ? ASP B 117 ? ALA B 102 ASP B 109 
AA8 4 LEU B 122 ? TYR B 130 ? LEU B 114 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 PHE A 130 ? N PHE A 122 O TRP A 160 ? O TRP A 152 
AA1 5 6 N VAL A 163 ? N VAL A 155 O GLU A 215 ? O GLU A 207 
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 VAL A 424 ? O VAL A 416 N ALA A 398 ? N ALA A 390 
AA3 2 3 O VAL A 399 ? O VAL A 391 N VAL A 371 ? N VAL A 363 
AA3 3 4 N LEU A 372 ? N LEU A 364 O VAL A 441 ? O VAL A 433 
AA3 4 5 N SER A 442 ? N SER A 434 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 ARG A 609 ? N ARG A 601 O ALA A 624 ? O ALA A 616 
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 ASP B 93  ? N ASP B 85  O ALA B 105 ? O ALA B 97  
AA8 2 3 N ILE B 102 ? N ILE B 94  O TRP B 114 ? O TRP B 106 
AA8 3 4 N LEU B 113 ? N LEU B 105 O LYS B 126 ? O LYS B 118 
AA9 1 2 N THR B 138 ? N THR B 130 O GLY B 151 ? O GLY B 143 
AA9 2 3 N ALA B 148 ? N ALA B 140 O TRP B 160 ? O TRP B 152 
AA9 3 4 N VAL B 159 ? N VAL B 151 O LEU B 168 ? O LEU B 160 
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 VAL B 245 ? N VAL B 237 O SER B 259 ? O SER B 251 
AB3 1 2 N VAL B 270 ? N VAL B 262 O ALA B 280 ? O ALA B 272 
AB3 2 3 N SER B 281 ? N SER B 273 O ALA B 289 ? O ALA B 281 
AB3 3 4 N VAL B 290 ? N VAL B 282 O LEU B 298 ? O LEU B 290 
AB4 1 2 N ARG B 309 ? N ARG B 301 O VAL B 324 ? O VAL B 316 
AB4 2 3 N LEU B 321 ? N LEU B 313 O HIS B 333 ? O HIS B 325 
# 
_pdbx_entry_details.entry_id                   9MGR 
_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 THR A 67  ? ? -164.44 -165.09 
2  1 HIS A 143 ? ? -94.42  48.95   
3  1 THR A 144 ? ? -161.47 109.50  
4  1 ALA A 171 ? ? -151.24 70.75   
5  1 LEU A 299 ? ? 74.54   -12.00  
6  1 LYS A 329 ? ? -94.62  30.27   
7  1 GLU A 408 ? ? -124.85 -67.21  
8  1 GLU A 435 ? ? -144.95 41.27   
9  1 ALA A 441 ? ? 74.69   -70.18  
10 1 LEU A 445 ? ? 72.43   36.20   
11 1 HIS A 507 ? ? -136.86 -69.51  
12 1 GLN A 561 ? A 53.36   -107.07 
13 1 GLN A 561 ? B 49.25   -103.90 
14 1 ASN A 607 ? ? -127.09 -165.52 
15 1 TYR A 633 ? ? -172.72 124.05  
16 1 PRO B 68  ? ? -97.95  37.69   
17 1 ILE B 147 ? A 85.95   -2.73   
18 1 ILE B 147 ? B 88.42   -9.18   
19 1 ASP B 196 ? ? -162.85 99.96   
20 1 THR B 197 ? ? -69.00  2.71    
21 1 GLU B 226 ? ? 74.95   -4.56   
22 1 CYS B 257 ? A -29.47  138.85  
23 1 CYS B 257 ? B -32.53  139.16  
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     193 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    A 
_pdbx_validate_planes.rmsd            0.074 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
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 HIS 146 ? A HIS 154 
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 PRO 20  ? B PRO 28  
50 1 Y 1 B PRO 21  ? B PRO 29  
51 1 Y 1 B ASN 22  ? B ASN 30  
52 1 Y 1 B ALA 23  ? B ALA 31  
53 1 Y 1 B PRO 24  ? B PRO 32  
54 1 Y 1 B ALA 25  ? B ALA 33  
55 1 Y 1 B CYS 26  ? B CYS 34  
56 1 Y 1 B CYS 208 ? B CYS 216 
57 1 Y 1 B SER 209 ? B SER 217 
58 1 Y 1 B ALA 210 ? B ALA 218 
59 1 Y 1 B PRO 211 ? B PRO 219 
60 1 Y 1 B THR 329 ? B THR 337 
61 1 Y 1 B GLU 330 ? B GLU 338 
62 1 Y 1 B PRO 331 ? B PRO 339 
63 1 Y 1 B LEU 332 ? B LEU 340 
64 1 Y 1 B PRO 333 ? B PRO 341 
65 1 Y 1 B ALA 334 ? B ALA 342 
66 1 Y 1 B PRO 335 ? B PRO 343 
67 1 Y 1 B GLY 336 ? B GLY 344 
68 1 Y 1 B PRO 337 ? B PRO 345 
69 1 Y 1 B ALA 338 ? B ALA 346 
70 1 Y 1 B SER 339 ? B SER 347 
71 1 Y 1 B VAL 340 ? B VAL 348 
72 1 Y 1 B THR 341 ? B THR 349 
73 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 
A1BLF N1     N N N 1   
A1BLF N3     N N N 2   
A1BLF C4     C N N 3   
A1BLF C5     C N N 4   
A1BLF C6     C N N 5   
A1BLF C7     C Y N 6   
A1BLF C8     C Y N 7   
A1BLF C10    C N N 8   
A1BLF C13    C N N 9   
A1BLF C15    C Y N 10  
A1BLF C17    C N N 11  
A1BLF C20    C N N 12  
A1BLF C21    C Y N 13  
A1BLF C22    C Y N 14  
A1BLF C24    C Y N 15  
A1BLF C26    C Y N 16  
A1BLF C28    C Y N 17  
A1BLF C1     C N N 18  
A1BLF C2     C N N 19  
A1BLF C3     C N N 20  
A1BLF N2     N Y N 21  
A1BLF C9     C N N 22  
A1BLF N4     N N N 23  
A1BLF C11    C N N 24  
A1BLF C12    C N N 25  
A1BLF O1     O N N 26  
A1BLF C14    C Y N 27  
A1BLF N5     N Y N 28  
A1BLF C16    C N N 29  
A1BLF O2     O N N 30  
A1BLF N6     N N N 31  
A1BLF C18    C N R 32  
A1BLF O3     O N N 33  
A1BLF C19    C N S 34  
A1BLF C23    C Y N 35  
A1BLF O4     O N N 36  
A1BLF C25    C N N 37  
A1BLF O5     O Y N 38  
A1BLF C27    C Y N 39  
A1BLF N7     N Y N 40  
A1BLF C29    C N N 41  
A1BLF C30    C Y N 42  
A1BLF C31    C Y N 43  
A1BLF C32    C N N 44  
A1BLF N8     N N N 45  
A1BLF H1     H N N 46  
A1BLF H2     H N N 47  
A1BLF H3     H N N 48  
A1BLF H4     H N N 49  
A1BLF H5     H N N 50  
A1BLF H6     H N N 51  
A1BLF H7     H N N 52  
A1BLF H8     H N N 53  
A1BLF H9     H N N 54  
A1BLF H10    H N N 55  
A1BLF H11    H N N 56  
A1BLF H12    H N N 57  
A1BLF H13    H N N 58  
A1BLF H14    H N N 59  
A1BLF H15    H N N 60  
A1BLF H16    H N N 61  
A1BLF H17    H N N 62  
A1BLF H18    H N N 63  
A1BLF H19    H N N 64  
A1BLF H20    H N N 65  
A1BLF H21    H N N 66  
A1BLF H22    H N N 67  
A1BLF H23    H N N 68  
A1BLF H24    H N N 69  
A1BLF H25    H N N 70  
A1BLF H26    H N N 71  
A1BLF H27    H N N 72  
A1BLF H28    H N N 73  
A1BLF H29    H N N 74  
A1BLF H30    H N N 75  
A1BLF H31    H N N 76  
A1BLF H32    H N N 77  
A1BLF H33    H N N 78  
A1BLF H34    H N N 79  
A1BLF H35    H N N 80  
A1BLF H36    H N N 81  
A1BLF H37    H N N 82  
A1BLF H38    H N N 83  
A1BLF H39    H N N 84  
A1BLF H40    H N N 85  
A1BLF H41    H N N 86  
A1BLF H42    H N N 87  
ALA   N      N N N 88  
ALA   CA     C N S 89  
ALA   C      C N N 90  
ALA   O      O N N 91  
ALA   CB     C N N 92  
ALA   OXT    O N N 93  
ALA   H      H N N 94  
ALA   H2     H N N 95  
ALA   HA     H N N 96  
ALA   HB1    H N N 97  
ALA   HB2    H N N 98  
ALA   HB3    H N N 99  
ALA   HXT    H N N 100 
ARG   N      N N N 101 
ARG   CA     C N S 102 
ARG   C      C N N 103 
ARG   O      O N N 104 
ARG   CB     C N N 105 
ARG   CG     C N N 106 
ARG   CD     C N N 107 
ARG   NE     N N N 108 
ARG   CZ     C N N 109 
ARG   NH1    N N N 110 
ARG   NH2    N N N 111 
ARG   OXT    O N N 112 
ARG   H      H N N 113 
ARG   H2     H N N 114 
ARG   HA     H N N 115 
ARG   HB2    H N N 116 
ARG   HB3    H N N 117 
ARG   HG2    H N N 118 
ARG   HG3    H N N 119 
ARG   HD2    H N N 120 
ARG   HD3    H N N 121 
ARG   HE     H N N 122 
ARG   HH11   H N N 123 
ARG   HH12   H N N 124 
ARG   HH21   H N N 125 
ARG   HH22   H N N 126 
ARG   HXT    H N N 127 
ASN   N      N N N 128 
ASN   CA     C N S 129 
ASN   C      C N N 130 
ASN   O      O N N 131 
ASN   CB     C N N 132 
ASN   CG     C N N 133 
ASN   OD1    O N N 134 
ASN   ND2    N N N 135 
ASN   OXT    O N N 136 
ASN   H      H N N 137 
ASN   H2     H N N 138 
ASN   HA     H N N 139 
ASN   HB2    H N N 140 
ASN   HB3    H N N 141 
ASN   HD21   H N N 142 
ASN   HD22   H N N 143 
ASN   HXT    H N N 144 
ASP   N      N N N 145 
ASP   CA     C N S 146 
ASP   C      C N N 147 
ASP   O      O N N 148 
ASP   CB     C N N 149 
ASP   CG     C N N 150 
ASP   OD1    O N N 151 
ASP   OD2    O N N 152 
ASP   OXT    O N N 153 
ASP   H      H N N 154 
ASP   H2     H N N 155 
ASP   HA     H N N 156 
ASP   HB2    H N N 157 
ASP   HB3    H N N 158 
ASP   HD2    H N N 159 
ASP   HXT    H N N 160 
CYS   N      N N N 161 
CYS   CA     C N R 162 
CYS   C      C N N 163 
CYS   O      O N N 164 
CYS   CB     C N N 165 
CYS   SG     S N N 166 
CYS   OXT    O N N 167 
CYS   H      H N N 168 
CYS   H2     H N N 169 
CYS   HA     H N N 170 
CYS   HB2    H N N 171 
CYS   HB3    H N N 172 
CYS   HG     H N N 173 
CYS   HXT    H N N 174 
EDO   C1     C N N 175 
EDO   O1     O N N 176 
EDO   C2     C N N 177 
EDO   O2     O N N 178 
EDO   H11    H N N 179 
EDO   H12    H N N 180 
EDO   HO1    H N N 181 
EDO   H21    H N N 182 
EDO   H22    H N N 183 
EDO   HO2    H N N 184 
GLN   N      N N N 185 
GLN   CA     C N S 186 
GLN   C      C N N 187 
GLN   O      O N N 188 
GLN   CB     C N N 189 
GLN   CG     C N N 190 
GLN   CD     C N N 191 
GLN   OE1    O N N 192 
GLN   NE2    N N N 193 
GLN   OXT    O N N 194 
GLN   H      H N N 195 
GLN   H2     H N N 196 
GLN   HA     H N N 197 
GLN   HB2    H N N 198 
GLN   HB3    H N N 199 
GLN   HG2    H N N 200 
GLN   HG3    H N N 201 
GLN   HE21   H N N 202 
GLN   HE22   H N N 203 
GLN   HXT    H N N 204 
GLU   N      N N N 205 
GLU   CA     C N S 206 
GLU   C      C N N 207 
GLU   O      O N N 208 
GLU   CB     C N N 209 
GLU   CG     C N N 210 
GLU   CD     C N N 211 
GLU   OE1    O N N 212 
GLU   OE2    O N N 213 
GLU   OXT    O N N 214 
GLU   H      H N N 215 
GLU   H2     H N N 216 
GLU   HA     H N N 217 
GLU   HB2    H N N 218 
GLU   HB3    H N N 219 
GLU   HG2    H N N 220 
GLU   HG3    H N N 221 
GLU   HE2    H N N 222 
GLU   HXT    H N N 223 
GLY   N      N N N 224 
GLY   CA     C N N 225 
GLY   C      C N N 226 
GLY   O      O N N 227 
GLY   OXT    O N N 228 
GLY   H      H N N 229 
GLY   H2     H N N 230 
GLY   HA2    H N N 231 
GLY   HA3    H N N 232 
GLY   HXT    H N N 233 
HIS   N      N N N 234 
HIS   CA     C N S 235 
HIS   C      C N N 236 
HIS   O      O N N 237 
HIS   CB     C N N 238 
HIS   CG     C Y N 239 
HIS   ND1    N Y N 240 
HIS   CD2    C Y N 241 
HIS   CE1    C Y N 242 
HIS   NE2    N Y N 243 
HIS   OXT    O N N 244 
HIS   H      H N N 245 
HIS   H2     H N N 246 
HIS   HA     H N N 247 
HIS   HB2    H N N 248 
HIS   HB3    H N N 249 
HIS   HD1    H N N 250 
HIS   HD2    H N N 251 
HIS   HE1    H N N 252 
HIS   HE2    H N N 253 
HIS   HXT    H N N 254 
HOH   O      O N N 255 
HOH   H1     H N N 256 
HOH   H2     H N N 257 
ILE   N      N N N 258 
ILE   CA     C N S 259 
ILE   C      C N N 260 
ILE   O      O N N 261 
ILE   CB     C N S 262 
ILE   CG1    C N N 263 
ILE   CG2    C N N 264 
ILE   CD1    C N N 265 
ILE   OXT    O N N 266 
ILE   H      H N N 267 
ILE   H2     H N N 268 
ILE   HA     H N N 269 
ILE   HB     H N N 270 
ILE   HG12   H N N 271 
ILE   HG13   H N N 272 
ILE   HG21   H N N 273 
ILE   HG22   H N N 274 
ILE   HG23   H N N 275 
ILE   HD11   H N N 276 
ILE   HD12   H N N 277 
ILE   HD13   H N N 278 
ILE   HXT    H N N 279 
LEU   N      N N N 280 
LEU   CA     C N S 281 
LEU   C      C N N 282 
LEU   O      O N N 283 
LEU   CB     C N N 284 
LEU   CG     C N N 285 
LEU   CD1    C N N 286 
LEU   CD2    C N N 287 
LEU   OXT    O N N 288 
LEU   H      H N N 289 
LEU   H2     H N N 290 
LEU   HA     H N N 291 
LEU   HB2    H N N 292 
LEU   HB3    H N N 293 
LEU   HG     H N N 294 
LEU   HD11   H N N 295 
LEU   HD12   H N N 296 
LEU   HD13   H N N 297 
LEU   HD21   H N N 298 
LEU   HD22   H N N 299 
LEU   HD23   H N N 300 
LEU   HXT    H N N 301 
LYS   N      N N N 302 
LYS   CA     C N S 303 
LYS   C      C N N 304 
LYS   O      O N N 305 
LYS   CB     C N N 306 
LYS   CG     C N N 307 
LYS   CD     C N N 308 
LYS   CE     C N N 309 
LYS   NZ     N N N 310 
LYS   OXT    O N N 311 
LYS   H      H N N 312 
LYS   H2     H N N 313 
LYS   HA     H N N 314 
LYS   HB2    H N N 315 
LYS   HB3    H N N 316 
LYS   HG2    H N N 317 
LYS   HG3    H N N 318 
LYS   HD2    H N N 319 
LYS   HD3    H N N 320 
LYS   HE2    H N N 321 
LYS   HE3    H N N 322 
LYS   HZ1    H N N 323 
LYS   HZ2    H N N 324 
LYS   HZ3    H N N 325 
LYS   HXT    H N N 326 
MET   N      N N N 327 
MET   CA     C N S 328 
MET   C      C N N 329 
MET   O      O N N 330 
MET   CB     C N N 331 
MET   CG     C N N 332 
MET   SD     S N N 333 
MET   CE     C N N 334 
MET   OXT    O N N 335 
MET   H      H N N 336 
MET   H2     H N N 337 
MET   HA     H N N 338 
MET   HB2    H N N 339 
MET   HB3    H N N 340 
MET   HG2    H N N 341 
MET   HG3    H N N 342 
MET   HE1    H N N 343 
MET   HE2    H N N 344 
MET   HE3    H N N 345 
MET   HXT    H N N 346 
MTA   CS     C N N 347 
MTA   "S5'"  S N N 348 
MTA   "C5'"  C N N 349 
MTA   "C4'"  C N S 350 
MTA   "O4'"  O N N 351 
MTA   "C2'"  C N R 352 
MTA   "O2'"  O N N 353 
MTA   "C3'"  C N S 354 
MTA   "O3'"  O N N 355 
MTA   "C1'"  C N R 356 
MTA   N9     N Y N 357 
MTA   C8     C Y N 358 
MTA   N7     N Y N 359 
MTA   C5     C Y N 360 
MTA   C6     C Y N 361 
MTA   N6     N N N 362 
MTA   N1     N Y N 363 
MTA   C2     C Y N 364 
MTA   N3     N Y N 365 
MTA   C4     C Y N 366 
MTA   HCS1   H N N 367 
MTA   HCS2   H N N 368 
MTA   HCS3   H N N 369 
MTA   "H5'1" H N N 370 
MTA   "H5'2" H N N 371 
MTA   "H4'"  H N N 372 
MTA   "H2'"  H N N 373 
MTA   "HO2'" H N N 374 
MTA   "H3'"  H N N 375 
MTA   H3T    H N N 376 
MTA   "H1'"  H N N 377 
MTA   H8     H N N 378 
MTA   H61    H N N 379 
MTA   H62    H N N 380 
MTA   H2     H N N 381 
PHE   N      N N N 382 
PHE   CA     C N S 383 
PHE   C      C N N 384 
PHE   O      O N N 385 
PHE   CB     C N N 386 
PHE   CG     C Y N 387 
PHE   CD1    C Y N 388 
PHE   CD2    C Y N 389 
PHE   CE1    C Y N 390 
PHE   CE2    C Y N 391 
PHE   CZ     C Y N 392 
PHE   OXT    O N N 393 
PHE   H      H N N 394 
PHE   H2     H N N 395 
PHE   HA     H N N 396 
PHE   HB2    H N N 397 
PHE   HB3    H N N 398 
PHE   HD1    H N N 399 
PHE   HD2    H N N 400 
PHE   HE1    H N N 401 
PHE   HE2    H N N 402 
PHE   HZ     H N N 403 
PHE   HXT    H N N 404 
PRO   N      N N N 405 
PRO   CA     C N S 406 
PRO   C      C N N 407 
PRO   O      O N N 408 
PRO   CB     C N N 409 
PRO   CG     C N N 410 
PRO   CD     C N N 411 
PRO   OXT    O N N 412 
PRO   H      H N N 413 
PRO   HA     H N N 414 
PRO   HB2    H N N 415 
PRO   HB3    H N N 416 
PRO   HG2    H N N 417 
PRO   HG3    H N N 418 
PRO   HD2    H N N 419 
PRO   HD3    H N N 420 
PRO   HXT    H N N 421 
SER   N      N N N 422 
SER   CA     C N S 423 
SER   C      C N N 424 
SER   O      O N N 425 
SER   CB     C N N 426 
SER   OG     O N N 427 
SER   OXT    O N N 428 
SER   H      H N N 429 
SER   H2     H N N 430 
SER   HA     H N N 431 
SER   HB2    H N N 432 
SER   HB3    H N N 433 
SER   HG     H N N 434 
SER   HXT    H N N 435 
THR   N      N N N 436 
THR   CA     C N S 437 
THR   C      C N N 438 
THR   O      O N N 439 
THR   CB     C N R 440 
THR   OG1    O N N 441 
THR   CG2    C N N 442 
THR   OXT    O N N 443 
THR   H      H N N 444 
THR   H2     H N N 445 
THR   HA     H N N 446 
THR   HB     H N N 447 
THR   HG1    H N N 448 
THR   HG21   H N N 449 
THR   HG22   H N N 450 
THR   HG23   H N N 451 
THR   HXT    H N N 452 
TRP   N      N N N 453 
TRP   CA     C N S 454 
TRP   C      C N N 455 
TRP   O      O N N 456 
TRP   CB     C N N 457 
TRP   CG     C Y N 458 
TRP   CD1    C Y N 459 
TRP   CD2    C Y N 460 
TRP   NE1    N Y N 461 
TRP   CE2    C Y N 462 
TRP   CE3    C Y N 463 
TRP   CZ2    C Y N 464 
TRP   CZ3    C Y N 465 
TRP   CH2    C Y N 466 
TRP   OXT    O N N 467 
TRP   H      H N N 468 
TRP   H2     H N N 469 
TRP   HA     H N N 470 
TRP   HB2    H N N 471 
TRP   HB3    H N N 472 
TRP   HD1    H N N 473 
TRP   HE1    H N N 474 
TRP   HE3    H N N 475 
TRP   HZ2    H N N 476 
TRP   HZ3    H N N 477 
TRP   HH2    H N N 478 
TRP   HXT    H N N 479 
TYR   N      N N N 480 
TYR   CA     C N S 481 
TYR   C      C N N 482 
TYR   O      O N N 483 
TYR   CB     C N N 484 
TYR   CG     C Y N 485 
TYR   CD1    C Y N 486 
TYR   CD2    C Y N 487 
TYR   CE1    C Y N 488 
TYR   CE2    C Y N 489 
TYR   CZ     C Y N 490 
TYR   OH     O N N 491 
TYR   OXT    O N N 492 
TYR   H      H N N 493 
TYR   H2     H N N 494 
TYR   HA     H N N 495 
TYR   HB2    H N N 496 
TYR   HB3    H N N 497 
TYR   HD1    H N N 498 
TYR   HD2    H N N 499 
TYR   HE1    H N N 500 
TYR   HE2    H N N 501 
TYR   HH     H N N 502 
TYR   HXT    H N N 503 
VAL   N      N N N 504 
VAL   CA     C N S 505 
VAL   C      C N N 506 
VAL   O      O N N 507 
VAL   CB     C N N 508 
VAL   CG1    C N N 509 
VAL   CG2    C N N 510 
VAL   OXT    O N N 511 
VAL   H      H N N 512 
VAL   H2     H N N 513 
VAL   HA     H N N 514 
VAL   HB     H N N 515 
VAL   HG11   H N N 516 
VAL   HG12   H N N 517 
VAL   HG13   H N N 518 
VAL   HG21   H N N 519 
VAL   HG22   H N N 520 
VAL   HG23   H N N 521 
VAL   HXT    H N N 522 
# 
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 
A1BLF O2    C16    doub N N 1   
A1BLF C10   C9     sing N N 2   
A1BLF C10   N4     sing N N 3   
A1BLF O1    C12    doub N N 4   
A1BLF N3    C9     sing N N 5   
A1BLF N3    C8     sing N N 6   
A1BLF C14   C8     doub Y N 7   
A1BLF C14   C15    sing Y N 8   
A1BLF C9    C11    sing N N 9   
A1BLF C16   C15    sing N N 10  
A1BLF C16   N6     sing N N 11  
A1BLF O3    C18    sing N N 12  
A1BLF N4    C12    sing N N 13  
A1BLF N4    C11    sing N N 14  
A1BLF C12   C13    sing N N 15  
A1BLF C8    N2     sing Y N 16  
A1BLF C18   C17    sing N N 17  
A1BLF C18   C19    sing N N 18  
A1BLF N8    C32    sing N N 19  
A1BLF N8    C19    sing N N 20  
A1BLF C15   N5     doub Y N 21  
A1BLF C17   N6     sing N N 22  
A1BLF C32   C31    sing N N 23  
A1BLF C19   C20    sing N N 24  
A1BLF N2    C7     doub Y N 25  
A1BLF N5    C7     sing Y N 26  
A1BLF C7    N1     sing N N 27  
A1BLF C31   C30    doub Y N 28  
A1BLF C31   C21    sing Y N 29  
A1BLF C20   C21    sing N N 30  
A1BLF C30   C24    sing Y N 31  
A1BLF N1    C5     sing N N 32  
A1BLF N1    C4     sing N N 33  
A1BLF C21   C22    doub Y N 34  
A1BLF C5    C6     sing N N 35  
A1BLF C4    C3     sing N N 36  
A1BLF C24   O4     sing N N 37  
A1BLF C24   C23    doub Y N 38  
A1BLF C25   O4     sing N N 39  
A1BLF C25   C26    sing N N 40  
A1BLF C6    C2     sing N N 41  
A1BLF C22   C23    sing Y N 42  
A1BLF C3    C2     sing N N 43  
A1BLF C26   C28    doub Y N 44  
A1BLF C26   O5     sing Y N 45  
A1BLF C2    C1     sing N N 46  
A1BLF C29   C28    sing N N 47  
A1BLF C28   N7     sing Y N 48  
A1BLF O5    C27    sing Y N 49  
A1BLF N7    C27    doub Y N 50  
A1BLF N3    H1     sing N N 51  
A1BLF C4    H2     sing N N 52  
A1BLF C4    H3     sing N N 53  
A1BLF C5    H4     sing N N 54  
A1BLF C5    H5     sing N N 55  
A1BLF C6    H6     sing N N 56  
A1BLF C6    H7     sing N N 57  
A1BLF C10   H8     sing N N 58  
A1BLF C10   H9     sing N N 59  
A1BLF C13   H10    sing N N 60  
A1BLF C13   H11    sing N N 61  
A1BLF C13   H12    sing N N 62  
A1BLF C17   H13    sing N N 63  
A1BLF C17   H14    sing N N 64  
A1BLF C20   H15    sing N N 65  
A1BLF C20   H16    sing N N 66  
A1BLF C22   H17    sing N N 67  
A1BLF C1    H18    sing N N 68  
A1BLF C1    H19    sing N N 69  
A1BLF C1    H20    sing N N 70  
A1BLF C2    H21    sing N N 71  
A1BLF C3    H22    sing N N 72  
A1BLF C3    H23    sing N N 73  
A1BLF C9    H24    sing N N 74  
A1BLF C11   H25    sing N N 75  
A1BLF C11   H26    sing N N 76  
A1BLF C14   H27    sing N N 77  
A1BLF N6    H28    sing N N 78  
A1BLF C18   H29    sing N N 79  
A1BLF O3    H30    sing N N 80  
A1BLF C19   H31    sing N N 81  
A1BLF C23   H32    sing N N 82  
A1BLF C25   H33    sing N N 83  
A1BLF C25   H34    sing N N 84  
A1BLF C27   H35    sing N N 85  
A1BLF C29   H36    sing N N 86  
A1BLF C29   H37    sing N N 87  
A1BLF C29   H38    sing N N 88  
A1BLF C30   H39    sing N N 89  
A1BLF C32   H40    sing N N 90  
A1BLF C32   H41    sing N N 91  
A1BLF N8    H42    sing N N 92  
ALA   N     CA     sing N N 93  
ALA   N     H      sing N N 94  
ALA   N     H2     sing N N 95  
ALA   CA    C      sing N N 96  
ALA   CA    CB     sing N N 97  
ALA   CA    HA     sing N N 98  
ALA   C     O      doub N N 99  
ALA   C     OXT    sing N N 100 
ALA   CB    HB1    sing N N 101 
ALA   CB    HB2    sing N N 102 
ALA   CB    HB3    sing N N 103 
ALA   OXT   HXT    sing N N 104 
ARG   N     CA     sing N N 105 
ARG   N     H      sing N N 106 
ARG   N     H2     sing N N 107 
ARG   CA    C      sing N N 108 
ARG   CA    CB     sing N N 109 
ARG   CA    HA     sing N N 110 
ARG   C     O      doub N N 111 
ARG   C     OXT    sing N N 112 
ARG   CB    CG     sing N N 113 
ARG   CB    HB2    sing N N 114 
ARG   CB    HB3    sing N N 115 
ARG   CG    CD     sing N N 116 
ARG   CG    HG2    sing N N 117 
ARG   CG    HG3    sing N N 118 
ARG   CD    NE     sing N N 119 
ARG   CD    HD2    sing N N 120 
ARG   CD    HD3    sing N N 121 
ARG   NE    CZ     sing N N 122 
ARG   NE    HE     sing N N 123 
ARG   CZ    NH1    sing N N 124 
ARG   CZ    NH2    doub N N 125 
ARG   NH1   HH11   sing N N 126 
ARG   NH1   HH12   sing N N 127 
ARG   NH2   HH21   sing N N 128 
ARG   NH2   HH22   sing N N 129 
ARG   OXT   HXT    sing N N 130 
ASN   N     CA     sing N N 131 
ASN   N     H      sing N N 132 
ASN   N     H2     sing N N 133 
ASN   CA    C      sing N N 134 
ASN   CA    CB     sing N N 135 
ASN   CA    HA     sing N N 136 
ASN   C     O      doub N N 137 
ASN   C     OXT    sing N N 138 
ASN   CB    CG     sing N N 139 
ASN   CB    HB2    sing N N 140 
ASN   CB    HB3    sing N N 141 
ASN   CG    OD1    doub N N 142 
ASN   CG    ND2    sing N N 143 
ASN   ND2   HD21   sing N N 144 
ASN   ND2   HD22   sing N N 145 
ASN   OXT   HXT    sing N N 146 
ASP   N     CA     sing N N 147 
ASP   N     H      sing N N 148 
ASP   N     H2     sing N N 149 
ASP   CA    C      sing N N 150 
ASP   CA    CB     sing N N 151 
ASP   CA    HA     sing N N 152 
ASP   C     O      doub N N 153 
ASP   C     OXT    sing N N 154 
ASP   CB    CG     sing N N 155 
ASP   CB    HB2    sing N N 156 
ASP   CB    HB3    sing N N 157 
ASP   CG    OD1    doub N N 158 
ASP   CG    OD2    sing N N 159 
ASP   OD2   HD2    sing N N 160 
ASP   OXT   HXT    sing N N 161 
CYS   N     CA     sing N N 162 
CYS   N     H      sing N N 163 
CYS   N     H2     sing N N 164 
CYS   CA    C      sing N N 165 
CYS   CA    CB     sing N N 166 
CYS   CA    HA     sing N N 167 
CYS   C     O      doub N N 168 
CYS   C     OXT    sing N N 169 
CYS   CB    SG     sing N N 170 
CYS   CB    HB2    sing N N 171 
CYS   CB    HB3    sing N N 172 
CYS   SG    HG     sing N N 173 
CYS   OXT   HXT    sing N N 174 
EDO   C1    O1     sing N N 175 
EDO   C1    C2     sing N N 176 
EDO   C1    H11    sing N N 177 
EDO   C1    H12    sing N N 178 
EDO   O1    HO1    sing N N 179 
EDO   C2    O2     sing N N 180 
EDO   C2    H21    sing N N 181 
EDO   C2    H22    sing N N 182 
EDO   O2    HO2    sing N N 183 
GLN   N     CA     sing N N 184 
GLN   N     H      sing N N 185 
GLN   N     H2     sing N N 186 
GLN   CA    C      sing N N 187 
GLN   CA    CB     sing N N 188 
GLN   CA    HA     sing N N 189 
GLN   C     O      doub N N 190 
GLN   C     OXT    sing N N 191 
GLN   CB    CG     sing N N 192 
GLN   CB    HB2    sing N N 193 
GLN   CB    HB3    sing N N 194 
GLN   CG    CD     sing N N 195 
GLN   CG    HG2    sing N N 196 
GLN   CG    HG3    sing N N 197 
GLN   CD    OE1    doub N N 198 
GLN   CD    NE2    sing N N 199 
GLN   NE2   HE21   sing N N 200 
GLN   NE2   HE22   sing N N 201 
GLN   OXT   HXT    sing N N 202 
GLU   N     CA     sing N N 203 
GLU   N     H      sing N N 204 
GLU   N     H2     sing N N 205 
GLU   CA    C      sing N N 206 
GLU   CA    CB     sing N N 207 
GLU   CA    HA     sing N N 208 
GLU   C     O      doub N N 209 
GLU   C     OXT    sing N N 210 
GLU   CB    CG     sing N N 211 
GLU   CB    HB2    sing N N 212 
GLU   CB    HB3    sing N N 213 
GLU   CG    CD     sing N N 214 
GLU   CG    HG2    sing N N 215 
GLU   CG    HG3    sing N N 216 
GLU   CD    OE1    doub N N 217 
GLU   CD    OE2    sing N N 218 
GLU   OE2   HE2    sing N N 219 
GLU   OXT   HXT    sing N N 220 
GLY   N     CA     sing N N 221 
GLY   N     H      sing N N 222 
GLY   N     H2     sing N N 223 
GLY   CA    C      sing N N 224 
GLY   CA    HA2    sing N N 225 
GLY   CA    HA3    sing N N 226 
GLY   C     O      doub N N 227 
GLY   C     OXT    sing N N 228 
GLY   OXT   HXT    sing N N 229 
HIS   N     CA     sing N N 230 
HIS   N     H      sing N N 231 
HIS   N     H2     sing N N 232 
HIS   CA    C      sing N N 233 
HIS   CA    CB     sing N N 234 
HIS   CA    HA     sing N N 235 
HIS   C     O      doub N N 236 
HIS   C     OXT    sing N N 237 
HIS   CB    CG     sing N N 238 
HIS   CB    HB2    sing N N 239 
HIS   CB    HB3    sing N N 240 
HIS   CG    ND1    sing Y N 241 
HIS   CG    CD2    doub Y N 242 
HIS   ND1   CE1    doub Y N 243 
HIS   ND1   HD1    sing N N 244 
HIS   CD2   NE2    sing Y N 245 
HIS   CD2   HD2    sing N N 246 
HIS   CE1   NE2    sing Y N 247 
HIS   CE1   HE1    sing N N 248 
HIS   NE2   HE2    sing N N 249 
HIS   OXT   HXT    sing N N 250 
HOH   O     H1     sing N N 251 
HOH   O     H2     sing N N 252 
ILE   N     CA     sing N N 253 
ILE   N     H      sing N N 254 
ILE   N     H2     sing N N 255 
ILE   CA    C      sing N N 256 
ILE   CA    CB     sing N N 257 
ILE   CA    HA     sing N N 258 
ILE   C     O      doub N N 259 
ILE   C     OXT    sing N N 260 
ILE   CB    CG1    sing N N 261 
ILE   CB    CG2    sing N N 262 
ILE   CB    HB     sing N N 263 
ILE   CG1   CD1    sing N N 264 
ILE   CG1   HG12   sing N N 265 
ILE   CG1   HG13   sing N N 266 
ILE   CG2   HG21   sing N N 267 
ILE   CG2   HG22   sing N N 268 
ILE   CG2   HG23   sing N N 269 
ILE   CD1   HD11   sing N N 270 
ILE   CD1   HD12   sing N N 271 
ILE   CD1   HD13   sing N N 272 
ILE   OXT   HXT    sing N N 273 
LEU   N     CA     sing N N 274 
LEU   N     H      sing N N 275 
LEU   N     H2     sing N N 276 
LEU   CA    C      sing N N 277 
LEU   CA    CB     sing N N 278 
LEU   CA    HA     sing N N 279 
LEU   C     O      doub N N 280 
LEU   C     OXT    sing N N 281 
LEU   CB    CG     sing N N 282 
LEU   CB    HB2    sing N N 283 
LEU   CB    HB3    sing N N 284 
LEU   CG    CD1    sing N N 285 
LEU   CG    CD2    sing N N 286 
LEU   CG    HG     sing N N 287 
LEU   CD1   HD11   sing N N 288 
LEU   CD1   HD12   sing N N 289 
LEU   CD1   HD13   sing N N 290 
LEU   CD2   HD21   sing N N 291 
LEU   CD2   HD22   sing N N 292 
LEU   CD2   HD23   sing N N 293 
LEU   OXT   HXT    sing N N 294 
LYS   N     CA     sing N N 295 
LYS   N     H      sing N N 296 
LYS   N     H2     sing N N 297 
LYS   CA    C      sing N N 298 
LYS   CA    CB     sing N N 299 
LYS   CA    HA     sing N N 300 
LYS   C     O      doub N N 301 
LYS   C     OXT    sing N N 302 
LYS   CB    CG     sing N N 303 
LYS   CB    HB2    sing N N 304 
LYS   CB    HB3    sing N N 305 
LYS   CG    CD     sing N N 306 
LYS   CG    HG2    sing N N 307 
LYS   CG    HG3    sing N N 308 
LYS   CD    CE     sing N N 309 
LYS   CD    HD2    sing N N 310 
LYS   CD    HD3    sing N N 311 
LYS   CE    NZ     sing N N 312 
LYS   CE    HE2    sing N N 313 
LYS   CE    HE3    sing N N 314 
LYS   NZ    HZ1    sing N N 315 
LYS   NZ    HZ2    sing N N 316 
LYS   NZ    HZ3    sing N N 317 
LYS   OXT   HXT    sing N N 318 
MET   N     CA     sing N N 319 
MET   N     H      sing N N 320 
MET   N     H2     sing N N 321 
MET   CA    C      sing N N 322 
MET   CA    CB     sing N N 323 
MET   CA    HA     sing N N 324 
MET   C     O      doub N N 325 
MET   C     OXT    sing N N 326 
MET   CB    CG     sing N N 327 
MET   CB    HB2    sing N N 328 
MET   CB    HB3    sing N N 329 
MET   CG    SD     sing N N 330 
MET   CG    HG2    sing N N 331 
MET   CG    HG3    sing N N 332 
MET   SD    CE     sing N N 333 
MET   CE    HE1    sing N N 334 
MET   CE    HE2    sing N N 335 
MET   CE    HE3    sing N N 336 
MET   OXT   HXT    sing N N 337 
MTA   CS    "S5'"  sing N N 338 
MTA   CS    HCS1   sing N N 339 
MTA   CS    HCS2   sing N N 340 
MTA   CS    HCS3   sing N N 341 
MTA   "S5'" "C5'"  sing N N 342 
MTA   "C5'" "C4'"  sing N N 343 
MTA   "C5'" "H5'1" sing N N 344 
MTA   "C5'" "H5'2" sing N N 345 
MTA   "C4'" "O4'"  sing N N 346 
MTA   "C4'" "C3'"  sing N N 347 
MTA   "C4'" "H4'"  sing N N 348 
MTA   "O4'" "C1'"  sing N N 349 
MTA   "C2'" "O2'"  sing N N 350 
MTA   "C2'" "C3'"  sing N N 351 
MTA   "C2'" "C1'"  sing N N 352 
MTA   "C2'" "H2'"  sing N N 353 
MTA   "O2'" "HO2'" sing N N 354 
MTA   "C3'" "O3'"  sing N N 355 
MTA   "C3'" "H3'"  sing N N 356 
MTA   "O3'" H3T    sing N N 357 
MTA   "C1'" N9     sing N N 358 
MTA   "C1'" "H1'"  sing N N 359 
MTA   N9    C8     sing Y N 360 
MTA   N9    C4     sing Y N 361 
MTA   C8    N7     doub Y N 362 
MTA   C8    H8     sing N N 363 
MTA   N7    C5     sing Y N 364 
MTA   C5    C6     sing Y N 365 
MTA   C5    C4     doub Y N 366 
MTA   C6    N6     sing N N 367 
MTA   C6    N1     doub Y N 368 
MTA   N6    H61    sing N N 369 
MTA   N6    H62    sing N N 370 
MTA   N1    C2     sing Y N 371 
MTA   C2    N3     doub Y N 372 
MTA   C2    H2     sing N N 373 
MTA   N3    C4     sing Y N 374 
PHE   N     CA     sing N N 375 
PHE   N     H      sing N N 376 
PHE   N     H2     sing N N 377 
PHE   CA    C      sing N N 378 
PHE   CA    CB     sing N N 379 
PHE   CA    HA     sing N N 380 
PHE   C     O      doub N N 381 
PHE   C     OXT    sing N N 382 
PHE   CB    CG     sing N N 383 
PHE   CB    HB2    sing N N 384 
PHE   CB    HB3    sing N N 385 
PHE   CG    CD1    doub Y N 386 
PHE   CG    CD2    sing Y N 387 
PHE   CD1   CE1    sing Y N 388 
PHE   CD1   HD1    sing N N 389 
PHE   CD2   CE2    doub Y N 390 
PHE   CD2   HD2    sing N N 391 
PHE   CE1   CZ     doub Y N 392 
PHE   CE1   HE1    sing N N 393 
PHE   CE2   CZ     sing Y N 394 
PHE   CE2   HE2    sing N N 395 
PHE   CZ    HZ     sing N N 396 
PHE   OXT   HXT    sing N N 397 
PRO   N     CA     sing N N 398 
PRO   N     CD     sing N N 399 
PRO   N     H      sing N N 400 
PRO   CA    C      sing N N 401 
PRO   CA    CB     sing N N 402 
PRO   CA    HA     sing N N 403 
PRO   C     O      doub N N 404 
PRO   C     OXT    sing N N 405 
PRO   CB    CG     sing N N 406 
PRO   CB    HB2    sing N N 407 
PRO   CB    HB3    sing N N 408 
PRO   CG    CD     sing N N 409 
PRO   CG    HG2    sing N N 410 
PRO   CG    HG3    sing N N 411 
PRO   CD    HD2    sing N N 412 
PRO   CD    HD3    sing N N 413 
PRO   OXT   HXT    sing N N 414 
SER   N     CA     sing N N 415 
SER   N     H      sing N N 416 
SER   N     H2     sing N N 417 
SER   CA    C      sing N N 418 
SER   CA    CB     sing N N 419 
SER   CA    HA     sing N N 420 
SER   C     O      doub N N 421 
SER   C     OXT    sing N N 422 
SER   CB    OG     sing N N 423 
SER   CB    HB2    sing N N 424 
SER   CB    HB3    sing N N 425 
SER   OG    HG     sing N N 426 
SER   OXT   HXT    sing N N 427 
THR   N     CA     sing N N 428 
THR   N     H      sing N N 429 
THR   N     H2     sing N N 430 
THR   CA    C      sing N N 431 
THR   CA    CB     sing N N 432 
THR   CA    HA     sing N N 433 
THR   C     O      doub N N 434 
THR   C     OXT    sing N N 435 
THR   CB    OG1    sing N N 436 
THR   CB    CG2    sing N N 437 
THR   CB    HB     sing N N 438 
THR   OG1   HG1    sing N N 439 
THR   CG2   HG21   sing N N 440 
THR   CG2   HG22   sing N N 441 
THR   CG2   HG23   sing N N 442 
THR   OXT   HXT    sing N N 443 
TRP   N     CA     sing N N 444 
TRP   N     H      sing N N 445 
TRP   N     H2     sing N N 446 
TRP   CA    C      sing N N 447 
TRP   CA    CB     sing N N 448 
TRP   CA    HA     sing N N 449 
TRP   C     O      doub N N 450 
TRP   C     OXT    sing N N 451 
TRP   CB    CG     sing N N 452 
TRP   CB    HB2    sing N N 453 
TRP   CB    HB3    sing N N 454 
TRP   CG    CD1    doub Y N 455 
TRP   CG    CD2    sing Y N 456 
TRP   CD1   NE1    sing Y N 457 
TRP   CD1   HD1    sing N N 458 
TRP   CD2   CE2    doub Y N 459 
TRP   CD2   CE3    sing Y N 460 
TRP   NE1   CE2    sing Y N 461 
TRP   NE1   HE1    sing N N 462 
TRP   CE2   CZ2    sing Y N 463 
TRP   CE3   CZ3    doub Y N 464 
TRP   CE3   HE3    sing N N 465 
TRP   CZ2   CH2    doub Y N 466 
TRP   CZ2   HZ2    sing N N 467 
TRP   CZ3   CH2    sing Y N 468 
TRP   CZ3   HZ3    sing N N 469 
TRP   CH2   HH2    sing N N 470 
TRP   OXT   HXT    sing N N 471 
TYR   N     CA     sing N N 472 
TYR   N     H      sing N N 473 
TYR   N     H2     sing N N 474 
TYR   CA    C      sing N N 475 
TYR   CA    CB     sing N N 476 
TYR   CA    HA     sing N N 477 
TYR   C     O      doub N N 478 
TYR   C     OXT    sing N N 479 
TYR   CB    CG     sing N N 480 
TYR   CB    HB2    sing N N 481 
TYR   CB    HB3    sing N N 482 
TYR   CG    CD1    doub Y N 483 
TYR   CG    CD2    sing Y N 484 
TYR   CD1   CE1    sing Y N 485 
TYR   CD1   HD1    sing N N 486 
TYR   CD2   CE2    doub Y N 487 
TYR   CD2   HD2    sing N N 488 
TYR   CE1   CZ     doub Y N 489 
TYR   CE1   HE1    sing N N 490 
TYR   CE2   CZ     sing Y N 491 
TYR   CE2   HE2    sing N N 492 
TYR   CZ    OH     sing N N 493 
TYR   OH    HH     sing N N 494 
TYR   OXT   HXT    sing N N 495 
VAL   N     CA     sing N N 496 
VAL   N     H      sing N N 497 
VAL   N     H2     sing N N 498 
VAL   CA    C      sing N N 499 
VAL   CA    CB     sing N N 500 
VAL   CA    HA     sing N N 501 
VAL   C     O      doub N N 502 
VAL   C     OXT    sing N N 503 
VAL   CB    CG1    sing N N 504 
VAL   CB    CG2    sing N N 505 
VAL   CB    HB     sing N N 506 
VAL   CG1   HG11   sing N N 507 
VAL   CG1   HG12   sing N N 508 
VAL   CG1   HG13   sing N N 509 
VAL   CG2   HG21   sing N N 510 
VAL   CG2   HG22   sing N N 511 
VAL   CG2   HG23   sing N N 512 
VAL   OXT   HXT    sing N N 513 
# 
_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   8VEO 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9MGR 
_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]   0.009714 
_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]   0.007252 
_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]   0.005599 
_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 
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     . ARG   A 1 21  ? -40.683 -67.540  -17.538 1.00 84.99  ? 13  ARG   A N     1 
ATOM   2    C CA    . ARG   A 1 21  ? -39.754 -68.378  -18.345 1.00 83.82  ? 13  ARG   A CA    1 
ATOM   3    C C     . ARG   A 1 21  ? -38.680 -67.481  -18.957 1.00 79.02  ? 13  ARG   A C     1 
ATOM   4    O O     . ARG   A 1 21  ? -37.498 -67.640  -18.661 1.00 80.32  ? 13  ARG   A O     1 
ATOM   5    C CB    . ARG   A 1 21  ? -40.469 -69.169  -19.450 1.00 86.59  ? 13  ARG   A CB    1 
ATOM   6    C CG    . ARG   A 1 21  ? -41.629 -70.054  -19.013 1.00 89.20  ? 13  ARG   A CG    1 
ATOM   7    C CD    . ARG   A 1 21  ? -42.962 -69.316  -18.959 1.00 91.75  ? 13  ARG   A CD    1 
ATOM   8    N NE    . ARG   A 1 21  ? -44.105 -70.226  -18.815 1.00 93.57  ? 13  ARG   A NE    1 
ATOM   9    C CZ    . ARG   A 1 21  ? -44.473 -70.877  -17.713 1.00 92.05  ? 13  ARG   A CZ    1 
ATOM   10   N NH1   . ARG   A 1 21  ? -45.515 -71.692  -17.758 1.00 91.84  ? 13  ARG   A NH1   1 
ATOM   11   N NH2   . ARG   A 1 21  ? -43.813 -70.723  -16.577 1.00 90.54  ? 13  ARG   A NH2   1 
ATOM   12   N N     . VAL   A 1 22  ? -39.110 -66.534  -19.800 1.00 73.39  ? 14  VAL   A N     1 
ATOM   13   C CA    . VAL   A 1 22  ? -38.204 -65.613  -20.466 1.00 68.89  ? 14  VAL   A CA    1 
ATOM   14   C C     . VAL   A 1 22  ? -38.041 -64.369  -19.598 1.00 64.06  ? 14  VAL   A C     1 
ATOM   15   O O     . VAL   A 1 22  ? -38.955 -63.551  -19.511 1.00 63.83  ? 14  VAL   A O     1 
ATOM   16   C CB    . VAL   A 1 22  ? -38.697 -65.235  -21.876 1.00 68.50  ? 14  VAL   A CB    1 
ATOM   17   C CG1   . VAL   A 1 22  ? -37.923 -64.062  -22.470 1.00 68.57  ? 14  VAL   A CG1   1 
ATOM   18   C CG2   . VAL   A 1 22  ? -38.651 -66.427  -22.819 1.00 69.24  ? 14  VAL   A CG2   1 
ATOM   19   N N     . SER   A 1 23  ? -36.870 -64.246  -18.963 1.00 59.46  ? 15  SER   A N     1 
ATOM   20   C CA    . SER   A 1 23  ? -36.448 -62.997  -18.352 1.00 56.23  ? 15  SER   A CA    1 
ATOM   21   C C     . SER   A 1 23  ? -35.971 -62.052  -19.450 1.00 52.84  ? 15  SER   A C     1 
ATOM   22   O O     . SER   A 1 23  ? -35.142 -62.434  -20.271 1.00 51.49  ? 15  SER   A O     1 
ATOM   23   C CB    . SER   A 1 23  ? -35.377 -63.222  -17.318 1.00 55.87  ? 15  SER   A CB    1 
ATOM   24   O OG    . SER   A 1 23  ? -34.894 -61.985  -16.815 1.00 56.27  ? 15  SER   A OG    1 
ATOM   25   N N     . SER   A 1 24  ? -36.504 -60.824  -19.453 1.00 51.13  ? 16  SER   A N     1 
ATOM   26   C CA    . SER   A 1 24  ? -36.333 -59.912  -20.572 1.00 50.85  ? 16  SER   A CA    1 
ATOM   27   C C     . SER   A 1 24  ? -36.208 -58.474  -20.080 1.00 48.47  ? 16  SER   A C     1 
ATOM   28   O O     . SER   A 1 24  ? -36.598 -58.157  -18.959 1.00 49.00  ? 16  SER   A O     1 
ATOM   29   C CB    . SER   A 1 24  ? -37.477 -60.027  -21.536 1.00 52.09  ? 16  SER   A CB    1 
ATOM   30   O OG    . SER   A 1 24  ? -38.595 -59.293  -21.053 1.00 53.50  ? 16  SER   A OG    1 
ATOM   31   N N     . GLY   A 1 25  ? -35.698 -57.603  -20.955 1.00 46.15  ? 17  GLY   A N     1 
ATOM   32   C CA    . GLY   A 1 25  ? -35.460 -56.216  -20.601 1.00 45.91  ? 17  GLY   A CA    1 
ATOM   33   C C     . GLY   A 1 25  ? -35.651 -55.286  -21.794 1.00 45.46  ? 17  GLY   A C     1 
ATOM   34   O O     . GLY   A 1 25  ? -35.461 -55.684  -22.940 1.00 44.95  ? 17  GLY   A O     1 
ATOM   35   N N     . ARG   A 1 26  ? -36.032 -54.041  -21.495 1.00 46.08  ? 18  ARG   A N     1 
ATOM   36   C CA    . ARG   A 1 26  ? -36.211 -53.010  -22.502 1.00 46.40  ? 18  ARG   A CA    1 
ATOM   37   C C     . ARG   A 1 26  ? -34.971 -52.122  -22.523 1.00 44.73  ? 18  ARG   A C     1 
ATOM   38   O O     . ARG   A 1 26  ? -34.551 -51.620  -21.483 1.00 44.97  ? 18  ARG   A O     1 
ATOM   39   C CB    . ARG   A 1 26  ? -37.451 -52.173  -22.168 1.00 47.86  ? 18  ARG   A CB    1 
ATOM   40   C CG    . ARG   A 1 26  ? -37.800 -51.088  -23.177 1.00 48.73  ? 18  ARG   A CG    1 
ATOM   41   C CD    . ARG   A 1 26  ? -38.240 -51.667  -24.511 1.00 49.80  ? 18  ARG   A CD    1 
ATOM   42   N NE    . ARG   A 1 26  ? -38.614 -50.614  -25.462 1.00 50.30  ? 18  ARG   A NE    1 
ATOM   43   C CZ    . ARG   A 1 26  ? -37.977 -50.291  -26.588 1.00 51.45  ? 18  ARG   A CZ    1 
ATOM   44   N NH1   . ARG   A 1 26  ? -36.857 -50.900  -26.944 1.00 51.29  ? 18  ARG   A NH1   1 
ATOM   45   N NH2   . ARG   A 1 26  ? -38.474 -49.344  -27.366 1.00 52.39  ? 18  ARG   A NH2   1 
ATOM   46   N N     . ASP   A 1 27  ? -34.393 -51.941  -23.714 1.00 42.39  ? 19  ASP   A N     1 
ATOM   47   C CA    . ASP   A 1 27  ? -33.320 -50.981  -23.898 1.00 41.05  ? 19  ASP   A CA    1 
ATOM   48   C C     . ASP   A 1 27  ? -33.912 -49.674  -24.417 1.00 40.64  ? 19  ASP   A C     1 
ATOM   49   O O     . ASP   A 1 27  ? -34.625 -49.674  -25.417 1.00 41.00  ? 19  ASP   A O     1 
ATOM   50   C CB    . ASP   A 1 27  ? -32.235 -51.524  -24.813 1.00 39.97  ? 19  ASP   A CB    1 
ATOM   51   C CG    . ASP   A 1 27  ? -31.127 -50.536  -25.144 1.00 38.85  ? 19  ASP   A CG    1 
ATOM   52   O OD1   . ASP   A 1 27  ? -30.631 -49.875  -24.206 1.00 36.74  ? 19  ASP   A OD1   1 
ATOM   53   O OD2   . ASP   A 1 27  ? -30.770 -50.437  -26.334 1.00 37.52  ? 19  ASP   A OD2   1 
ATOM   54   N N     . LEU   A 1 28  ? -33.619 -48.575  -23.711 1.00 39.75  ? 20  LEU   A N     1 
ATOM   55   C CA    . LEU   A 1 28  ? -34.004 -47.241  -24.141 1.00 40.45  ? 20  LEU   A CA    1 
ATOM   56   C C     . LEU   A 1 28  ? -32.763 -46.358  -24.132 1.00 40.58  ? 20  LEU   A C     1 
ATOM   57   O O     . LEU   A 1 28  ? -31.805 -46.631  -23.411 1.00 40.68  ? 20  LEU   A O     1 
ATOM   58   C CB    . LEU   A 1 28  ? -35.078 -46.630  -23.242 1.00 41.07  ? 20  LEU   A CB    1 
ATOM   59   C CG    . LEU   A 1 28  ? -36.333 -47.471  -22.988 1.00 41.48  ? 20  LEU   A CG    1 
ATOM   60   C CD1   . LEU   A 1 28  ? -37.182 -46.776  -21.939 1.00 41.66  ? 20  LEU   A CD1   1 
ATOM   61   C CD2   . LEU   A 1 28  ? -37.147 -47.719  -24.246 1.00 41.17  ? 20  LEU   A CD2   1 
ATOM   62   N N     . ASN   A 1 29  ? -32.809 -45.290  -24.932 1.00 41.08  ? 21  ASN   A N     1 
ATOM   63   C CA    . ASN   A 1 29  ? -31.752 -44.294  -24.951 1.00 41.53  ? 21  ASN   A CA    1 
ATOM   64   C C     . ASN   A 1 29  ? -32.373 -42.907  -24.794 1.00 40.82  ? 21  ASN   A C     1 
ATOM   65   O O     . ASN   A 1 29  ? -31.706 -41.901  -25.018 1.00 40.40  ? 21  ASN   A O     1 
ATOM   66   C CB    . ASN   A 1 29  ? -30.899 -44.460  -26.204 1.00 42.62  ? 21  ASN   A CB    1 
ATOM   67   C CG    . ASN   A 1 29  ? -29.445 -44.136  -25.955 1.00 44.00  ? 21  ASN   A CG    1 
ATOM   68   O OD1   . ASN   A 1 29  ? -28.866 -44.598  -24.963 1.00 43.40  ? 21  ASN   A OD1   1 
ATOM   69   N ND2   . ASN   A 1 29  ? -28.836 -43.356  -26.837 1.00 44.26  ? 21  ASN   A ND2   1 
ATOM   70   N N     . CYS   A 1 30  ? -33.650 -42.878  -24.385 1.00 41.35  ? 22  CYS   A N     1 
ATOM   71   C CA    . CYS   A 1 30  ? -34.380 -41.656  -24.088 1.00 41.53  ? 22  CYS   A CA    1 
ATOM   72   C C     . CYS   A 1 30  ? -35.357 -41.945  -22.952 1.00 41.20  ? 22  CYS   A C     1 
ATOM   73   O O     . CYS   A 1 30  ? -36.269 -42.754  -23.112 1.00 40.19  ? 22  CYS   A O     1 
ATOM   74   C CB    . CYS   A 1 30  ? -35.133 -41.144  -25.312 1.00 41.81  ? 22  CYS   A CB    1 
ATOM   75   S SG    . CYS   A 1 30  ? -36.228 -39.738  -24.974 1.00 41.90  ? 22  CYS   A SG    1 
ATOM   76   N N     . VAL   A 1 31  ? -35.134 -41.294  -21.804 1.00 42.32  ? 23  VAL   A N     1 
ATOM   77   C CA    . VAL   A 1 31  ? -35.965 -41.465  -20.623 1.00 43.38  ? 23  VAL   A CA    1 
ATOM   78   C C     . VAL   A 1 31  ? -36.303 -40.076  -20.089 1.00 44.56  ? 23  VAL   A C     1 
ATOM   79   O O     . VAL   A 1 31  ? -35.489 -39.472  -19.394 1.00 44.98  ? 23  VAL   A O     1 
ATOM   80   C CB    . VAL   A 1 31  ? -35.266 -42.327  -19.551 1.00 43.41  ? 23  VAL   A CB    1 
ATOM   81   C CG1   . VAL   A 1 31  ? -36.022 -42.335  -18.227 1.00 43.13  ? 23  VAL   A CG1   1 
ATOM   82   C CG2   . VAL   A 1 31  ? -35.032 -43.752  -20.039 1.00 43.32  ? 23  VAL   A CG2   1 
ATOM   83   N N     . PRO   A 1 32  ? -37.490 -39.512  -20.419 1.00 45.70  ? 24  PRO   A N     1 
ATOM   84   C CA    . PRO   A 1 32  ? -37.867 -38.187  -19.927 1.00 44.83  ? 24  PRO   A CA    1 
ATOM   85   C C     . PRO   A 1 32  ? -38.006 -38.184  -18.408 1.00 44.71  ? 24  PRO   A C     1 
ATOM   86   O O     . PRO   A 1 32  ? -37.490 -37.290  -17.746 1.00 43.78  ? 24  PRO   A O     1 
ATOM   87   C CB    . PRO   A 1 32  ? -39.191 -37.868  -20.647 1.00 44.89  ? 24  PRO   A CB    1 
ATOM   88   C CG    . PRO   A 1 32  ? -39.255 -38.864  -21.789 1.00 45.38  ? 24  PRO   A CG    1 
ATOM   89   C CD    . PRO   A 1 32  ? -38.523 -40.099  -21.288 1.00 45.81  ? 24  PRO   A CD    1 
ATOM   90   N N     . GLU   A 1 33  ? -38.700 -39.198  -17.873 1.00 45.46  ? 25  GLU   A N     1 
ATOM   91   C CA    . GLU   A 1 33  ? -38.819 -39.382  -16.435 1.00 46.39  ? 25  GLU   A CA    1 
ATOM   92   C C     . GLU   A 1 33  ? -38.707 -40.868  -16.107 1.00 45.26  ? 25  GLU   A C     1 
ATOM   93   O O     . GLU   A 1 33  ? -39.400 -41.691  -16.699 1.00 44.40  ? 25  GLU   A O     1 
ATOM   94   C CB    . GLU   A 1 33  ? -40.124 -38.780  -15.913 1.00 49.16  ? 25  GLU   A CB    1 
ATOM   95   C CG    . GLU   A 1 33  ? -40.154 -37.256  -15.995 1.00 52.32  ? 25  GLU   A CG    1 
ATOM   96   C CD    . GLU   A 1 33  ? -41.165 -36.593  -15.077 1.00 54.85  ? 25  GLU   A CD    1 
ATOM   97   O OE1   . GLU   A 1 33  ? -40.734 -35.850  -14.167 1.00 55.20  ? 25  GLU   A OE1   1 
ATOM   98   O OE2   . GLU   A 1 33  ? -42.380 -36.816  -15.272 1.00 57.26  ? 25  GLU   A OE2   1 
ATOM   99   N N     . ILE   A 1 34  ? -37.841 -41.184  -15.138 1.00 46.17  ? 26  ILE   A N     1 
ATOM   100  C CA    . ILE   A 1 34  ? -37.485 -42.560  -14.822 1.00 47.40  ? 26  ILE   A CA    1 
ATOM   101  C C     . ILE   A 1 34  ? -38.740 -43.335  -14.424 1.00 47.65  ? 26  ILE   A C     1 
ATOM   102  O O     . ILE   A 1 34  ? -38.956 -44.447  -14.900 1.00 47.32  ? 26  ILE   A O     1 
ATOM   103  C CB    . ILE   A 1 34  ? -36.420 -42.642  -13.709 1.00 47.96  ? 26  ILE   A CB    1 
ATOM   104  C CG1   . ILE   A 1 34  ? -35.257 -41.658  -13.916 1.00 48.17  ? 26  ILE   A CG1   1 
ATOM   105  C CG2   . ILE   A 1 34  ? -35.919 -44.080  -13.560 1.00 48.03  ? 26  ILE   A CG2   1 
ATOM   106  C CD1   . ILE   A 1 34  ? -34.066 -41.908  -13.007 1.00 48.23  ? 26  ILE   A CD1   1 
ATOM   107  N N     . ALA   A 1 35  ? -39.549 -42.741  -13.538 1.00 48.28  ? 27  ALA   A N     1 
ATOM   108  C CA    . ALA   A 1 35  ? -40.683 -43.425  -12.940 1.00 49.26  ? 27  ALA   A CA    1 
ATOM   109  C C     . ALA   A 1 35  ? -41.761 -43.686  -13.988 1.00 50.59  ? 27  ALA   A C     1 
ATOM   110  O O     . ALA   A 1 35  ? -42.239 -44.813  -14.109 1.00 50.22  ? 27  ALA   A O     1 
ATOM   111  C CB    . ALA   A 1 35  ? -41.219 -42.617  -11.779 1.00 49.64  ? 27  ALA   A CB    1 
ATOM   112  N N     . ASP   A 1 36  ? -42.137 -42.638  -14.734 1.00 53.12  ? 28  ASP   A N     1 
ATOM   113  C CA    . ASP   A 1 36  ? -43.058 -42.772  -15.853 1.00 54.99  ? 28  ASP   A CA    1 
ATOM   114  C C     . ASP   A 1 36  ? -42.596 -43.918  -16.746 1.00 55.25  ? 28  ASP   A C     1 
ATOM   115  O O     . ASP   A 1 36  ? -43.353 -44.848  -17.022 1.00 56.17  ? 28  ASP   A O     1 
ATOM   116  C CB    . ASP   A 1 36  ? -43.131 -41.507  -16.696 1.00 55.96  ? 28  ASP   A CB    1 
ATOM   117  C CG    . ASP   A 1 36  ? -43.650 -40.259  -15.997 1.00 58.31  ? 28  ASP   A CG    1 
ATOM   118  O OD1   . ASP   A 1 36  ? -44.065 -40.369  -14.824 1.00 60.60  ? 28  ASP   A OD1   1 
ATOM   119  O OD2   . ASP   A 1 36  ? -43.617 -39.183  -16.631 1.00 59.35  ? 28  ASP   A OD2   1 
ATOM   120  N N     . THR   A 1 37  ? -41.331 -43.830  -17.172 1.00 54.79  ? 29  THR   A N     1 
ATOM   121  C CA    . THR   A 1 37  ? -40.741 -44.782  -18.095 1.00 54.58  ? 29  THR   A CA    1 
ATOM   122  C C     . THR   A 1 37  ? -40.765 -46.184  -17.489 1.00 54.31  ? 29  THR   A C     1 
ATOM   123  O O     . THR   A 1 37  ? -41.220 -47.126  -18.133 1.00 55.53  ? 29  THR   A O     1 
ATOM   124  C CB    . THR   A 1 37  ? -39.318 -44.332  -18.422 1.00 54.95  ? 29  THR   A CB    1 
ATOM   125  O OG1   . THR   A 1 37  ? -39.470 -43.078  -19.082 1.00 54.54  ? 29  THR   A OG1   1 
ATOM   126  C CG2   . THR   A 1 37  ? -38.582 -45.314  -19.316 1.00 55.50  ? 29  THR   A CG2   1 
ATOM   127  N N     . LEU   A 1 38  ? -40.268 -46.312  -16.253 1.00 53.48  ? 30  LEU   A N     1 
ATOM   128  C CA    . LEU   A 1 38  ? -40.066 -47.619  -15.647 1.00 52.25  ? 30  LEU   A CA    1 
ATOM   129  C C     . LEU   A 1 38  ? -41.413 -48.315  -15.457 1.00 52.48  ? 30  LEU   A C     1 
ATOM   130  O O     . LEU   A 1 38  ? -41.511 -49.529  -15.620 1.00 52.13  ? 30  LEU   A O     1 
ATOM   131  C CB    . LEU   A 1 38  ? -39.297 -47.505  -14.331 1.00 50.62  ? 30  LEU   A CB    1 
ATOM   132  C CG    . LEU   A 1 38  ? -38.770 -48.821  -13.748 1.00 49.83  ? 30  LEU   A CG    1 
ATOM   133  C CD1   . LEU   A 1 38  ? -37.750 -49.478  -14.669 1.00 49.50  ? 30  LEU   A CD1   1 
ATOM   134  C CD2   . LEU   A 1 38  ? -38.171 -48.598  -12.371 1.00 49.23  ? 30  LEU   A CD2   1 
ATOM   135  N N     . GLY   A 1 39  ? -42.445 -47.538  -15.111 1.00 52.99  ? 31  GLY   A N     1 
ATOM   136  C CA    . GLY   A 1 39  ? -43.799 -48.062  -15.046 1.00 53.95  ? 31  GLY   A CA    1 
ATOM   137  C C     . GLY   A 1 39  ? -44.238 -48.606  -16.403 1.00 54.90  ? 31  GLY   A C     1 
ATOM   138  O O     . GLY   A 1 39  ? -44.692 -49.745  -16.500 1.00 54.76  ? 31  GLY   A O     1 
ATOM   139  N N     . ALA   A 1 40  ? -44.068 -47.778  -17.442 1.00 54.87  ? 32  ALA   A N     1 
ATOM   140  C CA    . ALA   A 1 40  ? -44.451 -48.126  -18.802 1.00 53.88  ? 32  ALA   A CA    1 
ATOM   141  C C     . ALA   A 1 40  ? -43.892 -49.492  -19.197 1.00 53.92  ? 32  ALA   A C     1 
ATOM   142  O O     . ALA   A 1 40  ? -44.615 -50.307  -19.763 1.00 55.38  ? 32  ALA   A O     1 
ATOM   143  C CB    . ALA   A 1 40  ? -43.988 -47.052  -19.762 1.00 53.87  ? 32  ALA   A CB    1 
ATOM   144  N N     . VAL   A 1 41  ? -42.608 -49.733  -18.901 1.00 52.89  ? 33  VAL   A N     1 
ATOM   145  C CA    . VAL   A 1 41  ? -41.947 -50.952  -19.343 1.00 52.20  ? 33  VAL   A CA    1 
ATOM   146  C C     . VAL   A 1 41  ? -42.347 -52.099  -18.418 1.00 51.91  ? 33  VAL   A C     1 
ATOM   147  O O     . VAL   A 1 41  ? -42.456 -53.237  -18.865 1.00 50.73  ? 33  VAL   A O     1 
ATOM   148  C CB    . VAL   A 1 41  ? -40.414 -50.828  -19.453 1.00 51.68  ? 33  VAL   A CB    1 
ATOM   149  C CG1   . VAL   A 1 41  ? -40.007 -49.638  -20.315 1.00 51.62  ? 33  VAL   A CG1   1 
ATOM   150  C CG2   . VAL   A 1 41  ? -39.727 -50.758  -18.096 1.00 52.21  ? 33  VAL   A CG2   1 
ATOM   151  N N     . ALA   A 1 42  ? -42.553 -51.798  -17.130 1.00 53.40  ? 34  ALA   A N     1 
ATOM   152  C CA    . ALA   A 1 42  ? -43.104 -52.775  -16.206 1.00 54.53  ? 34  ALA   A CA    1 
ATOM   153  C C     . ALA   A 1 42  ? -44.481 -53.203  -16.706 1.00 55.93  ? 34  ALA   A C     1 
ATOM   154  O O     . ALA   A 1 42  ? -44.763 -54.394  -16.822 1.00 54.55  ? 34  ALA   A O     1 
ATOM   155  C CB    . ALA   A 1 42  ? -43.168 -52.202  -14.807 1.00 54.24  ? 34  ALA   A CB    1 
ATOM   156  N N     . LYS   A 1 43  ? -45.314 -52.204  -17.022 1.00 58.78  ? 35  LYS   A N     1 
ATOM   157  C CA    . LYS   A 1 43  ? -46.626 -52.414  -17.612 1.00 60.88  ? 35  LYS   A CA    1 
ATOM   158  C C     . LYS   A 1 43  ? -46.512 -53.315  -18.841 1.00 61.82  ? 35  LYS   A C     1 
ATOM   159  O O     . LYS   A 1 43  ? -47.229 -54.308  -18.944 1.00 62.61  ? 35  LYS   A O     1 
ATOM   160  C CB    . LYS   A 1 43  ? -47.235 -51.051  -17.964 1.00 61.78  ? 35  LYS   A CB    1 
ATOM   161  C CG    . LYS   A 1 43  ? -48.587 -51.079  -18.660 1.00 63.05  ? 35  LYS   A CG    1 
ATOM   162  C CD    . LYS   A 1 43  ? -49.721 -51.604  -17.789 1.00 64.14  ? 35  LYS   A CD    1 
ATOM   163  C CE    . LYS   A 1 43  ? -51.040 -51.571  -18.496 1.00 64.85  ? 35  LYS   A CE    1 
ATOM   164  N NZ    . LYS   A 1 43  ? -52.158 -51.678  -17.554 1.00 64.81  ? 35  LYS   A NZ    1 
ATOM   165  N N     . GLN   A 1 44  ? -45.597 -52.961  -19.756 1.00 61.41  ? 36  GLN   A N     1 
ATOM   166  C CA    . GLN   A 1 44  ? -45.413 -53.675  -21.013 1.00 60.35  ? 36  GLN   A CA    1 
ATOM   167  C C     . GLN   A 1 44  ? -45.055 -55.143  -20.770 1.00 58.64  ? 36  GLN   A C     1 
ATOM   168  O O     . GLN   A 1 44  ? -45.382 -55.994  -21.596 1.00 60.15  ? 36  GLN   A O     1 
ATOM   169  C CB    . GLN   A 1 44  ? -44.343 -52.998  -21.872 1.00 60.90  ? 36  GLN   A CB    1 
ATOM   170  C CG    . GLN   A 1 44  ? -44.796 -51.691  -22.515 1.00 61.74  ? 36  GLN   A CG    1 
ATOM   171  C CD    . GLN   A 1 44  ? -43.654 -50.834  -23.024 1.00 62.58  ? 36  GLN   A CD    1 
ATOM   172  O OE1   . GLN   A 1 44  ? -42.491 -51.252  -23.067 1.00 62.79  ? 36  GLN   A OE1   1 
ATOM   173  N NE2   . GLN   A 1 44  ? -43.976 -49.613  -23.423 1.00 62.49  ? 36  GLN   A NE2   1 
ATOM   174  N N     . GLY   A 1 45  ? -44.371 -55.435  -19.655 1.00 55.83  ? 37  GLY   A N     1 
ATOM   175  C CA    . GLY   A 1 45  ? -44.118 -56.808  -19.239 1.00 53.93  ? 37  GLY   A CA    1 
ATOM   176  C C     . GLY   A 1 45  ? -42.631 -57.133  -19.093 1.00 52.21  ? 37  GLY   A C     1 
ATOM   177  O O     . GLY   A 1 45  ? -42.277 -58.285  -18.849 1.00 50.41  ? 37  GLY   A O     1 
ATOM   178  N N     . PHE   A 1 46  ? -41.764 -56.123  -19.234 1.00 50.98  ? 38  PHE   A N     1 
ATOM   179  C CA    . PHE   A 1 46  ? -40.329 -56.314  -19.098 1.00 49.95  ? 38  PHE   A CA    1 
ATOM   180  C C     . PHE   A 1 46  ? -39.969 -56.505  -17.626 1.00 47.90  ? 38  PHE   A C     1 
ATOM   181  O O     . PHE   A 1 46  ? -40.652 -55.981  -16.752 1.00 48.49  ? 38  PHE   A O     1 
ATOM   182  C CB    . PHE   A 1 46  ? -39.608 -55.116  -19.725 1.00 50.06  ? 38  PHE   A CB    1 
ATOM   183  C CG    . PHE   A 1 46  ? -39.790 -55.027  -21.234 1.00 49.86  ? 38  PHE   A CG    1 
ATOM   184  C CD1   . PHE   A 1 46  ? -39.017 -55.807  -22.087 1.00 49.79  ? 38  PHE   A CD1   1 
ATOM   185  C CD2   . PHE   A 1 46  ? -40.735 -54.175  -21.795 1.00 49.81  ? 38  PHE   A CD2   1 
ATOM   186  C CE1   . PHE   A 1 46  ? -39.185 -55.735  -23.461 1.00 50.06  ? 38  PHE   A CE1   1 
ATOM   187  C CE2   . PHE   A 1 46  ? -40.897 -54.106  -23.171 1.00 50.02  ? 38  PHE   A CE2   1 
ATOM   188  C CZ    . PHE   A 1 46  ? -40.123 -54.885  -23.999 1.00 50.08  ? 38  PHE   A CZ    1 
ATOM   189  N N     . ASP   A 1 47  ? -38.890 -57.260  -17.374 1.00 46.71  ? 39  ASP   A N     1 
ATOM   190  C CA    . ASP   A 1 47  ? -38.399 -57.508  -16.027 1.00 45.82  ? 39  ASP   A CA    1 
ATOM   191  C C     . ASP   A 1 47  ? -37.434 -56.409  -15.586 1.00 43.40  ? 39  ASP   A C     1 
ATOM   192  O O     . ASP   A 1 47  ? -37.249 -56.214  -14.387 1.00 43.77  ? 39  ASP   A O     1 
ATOM   193  C CB    . ASP   A 1 47  ? -37.695 -58.851  -15.909 1.00 47.68  ? 39  ASP   A CB    1 
ATOM   194  C CG    . ASP   A 1 47  ? -38.551 -60.082  -16.161 1.00 49.80  ? 39  ASP   A CG    1 
ATOM   195  O OD1   . ASP   A 1 47  ? -39.732 -59.913  -16.527 1.00 51.96  ? 39  ASP   A OD1   1 
ATOM   196  O OD2   . ASP   A 1 47  ? -38.029 -61.203  -15.980 1.00 51.64  ? 39  ASP   A OD2   1 
ATOM   197  N N     . PHE   A 1 48  ? -36.795 -55.720  -16.544 1.00 40.50  ? 40  PHE   A N     1 
ATOM   198  C CA    . PHE   A 1 48  ? -35.820 -54.690  -16.215 1.00 38.18  ? 40  PHE   A CA    1 
ATOM   199  C C     . PHE   A 1 48  ? -35.655 -53.715  -17.380 1.00 36.57  ? 40  PHE   A C     1 
ATOM   200  O O     . PHE   A 1 48  ? -36.224 -53.909  -18.452 1.00 34.94  ? 40  PHE   A O     1 
ATOM   201  C CB    . PHE   A 1 48  ? -34.497 -55.352  -15.813 1.00 37.72  ? 40  PHE   A CB    1 
ATOM   202  C CG    . PHE   A 1 48  ? -33.784 -56.118  -16.919 1.00 37.20  ? 40  PHE   A CG    1 
ATOM   203  C CD1   . PHE   A 1 48  ? -32.864 -55.482  -17.747 1.00 37.38  ? 40  PHE   A CD1   1 
ATOM   204  C CD2   . PHE   A 1 48  ? -34.026 -57.472  -17.119 1.00 37.01  ? 40  PHE   A CD2   1 
ATOM   205  C CE1   . PHE   A 1 48  ? -32.211 -56.182  -18.751 1.00 37.18  ? 40  PHE   A CE1   1 
ATOM   206  C CE2   . PHE   A 1 48  ? -33.371 -58.168  -18.126 1.00 37.08  ? 40  PHE   A CE2   1 
ATOM   207  C CZ    . PHE   A 1 48  ? -32.464 -57.523  -18.938 1.00 36.99  ? 40  PHE   A CZ    1 
ATOM   208  N N     . LEU   A 1 49  ? -34.861 -52.664  -17.141 1.00 35.86  ? 41  LEU   A N     1 
ATOM   209  C CA    . LEU   A 1 49  ? -34.689 -51.566  -18.079 1.00 35.76  ? 41  LEU   A CA    1 
ATOM   210  C C     . LEU   A 1 49  ? -33.208 -51.220  -18.206 1.00 35.54  ? 41  LEU   A C     1 
ATOM   211  O O     . LEU   A 1 49  ? -32.534 -51.012  -17.200 1.00 35.39  ? 41  LEU   A O     1 
ATOM   212  C CB    . LEU   A 1 49  ? -35.484 -50.356  -17.588 1.00 35.44  ? 41  LEU   A CB    1 
ATOM   213  C CG    . LEU   A 1 49  ? -35.127 -49.011  -18.232 1.00 35.35  ? 41  LEU   A CG    1 
ATOM   214  C CD1   . LEU   A 1 49  ? -35.462 -49.012  -19.710 1.00 35.43  ? 41  LEU   A CD1   1 
ATOM   215  C CD2   . LEU   A 1 49  ? -35.813 -47.850  -17.539 1.00 35.64  ? 41  LEU   A CD2   1 
ATOM   216  N N     . CYS   A 1 50  ? -32.728 -51.128  -19.454 1.00 34.86  ? 42  CYS   A N     1 
ATOM   217  C CA    . CYS   A 1 50  ? -31.400 -50.610  -19.743 1.00 34.43  ? 42  CYS   A CA    1 
ATOM   218  C C     . CYS   A 1 50  ? -31.529 -49.143  -20.148 1.00 34.06  ? 42  CYS   A C     1 
ATOM   219  O O     . CYS   A 1 50  ? -32.294 -48.824  -21.052 1.00 33.61  ? 42  CYS   A O     1 
ATOM   220  C CB    . CYS   A 1 50  ? -30.726 -51.408  -20.854 1.00 34.33  ? 42  CYS   A CB    1 
ATOM   221  S SG    . CYS   A 1 50  ? -30.949 -53.200  -20.703 1.00 34.03  ? 42  CYS   A SG    1 
ATOM   222  N N     . MET   A 1 51  ? -30.785 -48.256  -19.478 1.00 34.27  ? 43  MET   A N     1 
ATOM   223  C CA    . MET   A 1 51  ? -30.942 -46.827  -19.699 1.00 34.56  ? 43  MET   A CA    1 
ATOM   224  C C     . MET   A 1 51  ? -29.668 -46.078  -19.319 1.00 34.03  ? 43  MET   A C     1 
ATOM   225  O O     . MET   A 1 51  ? -28.837 -46.599  -18.580 1.00 34.22  ? 43  MET   A O     1 
ATOM   226  C CB    . MET   A 1 51  ? -32.108 -46.272  -18.872 1.00 36.07  ? 43  MET   A CB    1 
ATOM   227  C CG    . MET   A 1 51  ? -32.089 -46.688  -17.412 1.00 36.85  ? 43  MET   A CG    1 
ATOM   228  S SD    . MET   A 1 51  ? -33.200 -45.710  -16.380 1.00 38.32  ? 43  MET   A SD    1 
ATOM   229  C CE    . MET   A 1 51  ? -32.235 -44.217  -16.108 1.00 38.72  ? 43  MET   A CE    1 
ATOM   230  N N     . PRO   A 1 52  ? -29.491 -44.823  -19.796 1.00 33.49  ? 44  PRO   A N     1 
ATOM   231  C CA    . PRO   A 1 52  ? -28.330 -44.010  -19.436 1.00 33.71  ? 44  PRO   A CA    1 
ATOM   232  C C     . PRO   A 1 52  ? -28.479 -43.459  -18.020 1.00 34.50  ? 44  PRO   A C     1 
ATOM   233  O O     . PRO   A 1 52  ? -29.595 -43.224  -17.564 1.00 35.53  ? 44  PRO   A O     1 
ATOM   234  C CB    . PRO   A 1 52  ? -28.304 -42.887  -20.493 1.00 33.76  ? 44  PRO   A CB    1 
ATOM   235  C CG    . PRO   A 1 52  ? -29.447 -43.198  -21.446 1.00 33.90  ? 44  PRO   A CG    1 
ATOM   236  C CD    . PRO   A 1 52  ? -30.400 -44.111  -20.705 1.00 33.80  ? 44  PRO   A CD    1 
ATOM   237  N N     . VAL   A 1 53  ? -27.342 -43.253  -17.343 1.00 34.29  ? 45  VAL   A N     1 
ATOM   238  C CA    . VAL   A 1 53  ? -27.326 -42.720  -15.988 1.00 34.50  ? 45  VAL   A CA    1 
ATOM   239  C C     . VAL   A 1 53  ? -26.974 -41.233  -16.036 1.00 34.33  ? 45  VAL   A C     1 
ATOM   240  O O     . VAL   A 1 53  ? -27.268 -40.499  -15.094 1.00 34.27  ? 45  VAL   A O     1 
ATOM   241  C CB    . VAL   A 1 53  ? -26.390 -43.510  -15.048 1.00 34.92  ? 45  VAL   A CB    1 
ATOM   242  C CG1   . VAL   A 1 53  ? -26.944 -44.898  -14.747 1.00 35.46  ? 45  VAL   A CG1   1 
ATOM   243  C CG2   . VAL   A 1 53  ? -24.962 -43.619  -15.572 1.00 35.04  ? 45  VAL   A CG2   1 
ATOM   244  N N     . PHE   A 1 54  ? -26.320 -40.810  -17.126 1.00 33.75  ? 46  PHE   A N     1 
ATOM   245  C CA    . PHE   A 1 54  ? -26.234 -39.410  -17.516 1.00 33.94  ? 46  PHE   A CA    1 
ATOM   246  C C     . PHE   A 1 54  ? -26.888 -39.281  -18.886 1.00 33.61  ? 46  PHE   A C     1 
ATOM   247  O O     . PHE   A 1 54  ? -26.957 -40.262  -19.622 1.00 34.56  ? 46  PHE   A O     1 
ATOM   248  C CB    . PHE   A 1 54  ? -24.787 -38.913  -17.594 1.00 34.29  ? 46  PHE   A CB    1 
ATOM   249  C CG    . PHE   A 1 54  ? -24.036 -38.926  -16.270 1.00 34.12  ? 46  PHE   A CG    1 
ATOM   250  C CD1   . PHE   A 1 54  ? -23.670 -40.127  -15.673 1.00 34.36  ? 46  PHE   A CD1   1 
ATOM   251  C CD2   . PHE   A 1 54  ? -23.680 -37.740  -15.637 1.00 34.30  ? 46  PHE   A CD2   1 
ATOM   252  C CE1   . PHE   A 1 54  ? -22.987 -40.143  -14.467 1.00 33.89  ? 46  PHE   A CE1   1 
ATOM   253  C CE2   . PHE   A 1 54  ? -22.995 -37.760  -14.431 1.00 34.19  ? 46  PHE   A CE2   1 
ATOM   254  C CZ    . PHE   A 1 54  ? -22.649 -38.961  -13.851 1.00 34.13  ? 46  PHE   A CZ    1 
ATOM   255  N N     . HIS   A 1 55  ? -27.354 -38.075  -19.229 1.00 33.59  ? 47  HIS   A N     1 
ATOM   256  C CA    . HIS   A 1 55  ? -28.035 -37.875  -20.498 1.00 33.22  ? 47  HIS   A CA    1 
ATOM   257  C C     . HIS   A 1 55  ? -27.071 -38.174  -21.648 1.00 31.59  ? 47  HIS   A C     1 
ATOM   258  O O     . HIS   A 1 55  ? -25.978 -37.611  -21.714 1.00 31.10  ? 47  HIS   A O     1 
ATOM   259  C CB    . HIS   A 1 55  ? -28.660 -36.479  -20.604 1.00 34.27  ? 47  HIS   A CB    1 
ATOM   260  C CG    . HIS   A 1 55  ? -29.534 -36.344  -21.807 1.00 35.06  ? 47  HIS   A CG    1 
ATOM   261  N ND1   . HIS   A 1 55  ? -29.048 -36.032  -23.059 1.00 34.44  ? 47  HIS   A ND1   1 
ATOM   262  C CD2   . HIS   A 1 55  ? -30.851 -36.529  -21.960 1.00 35.46  ? 47  HIS   A CD2   1 
ATOM   263  C CE1   . HIS   A 1 55  ? -30.050 -36.016  -23.923 1.00 34.57  ? 47  HIS   A CE1   1 
ATOM   264  N NE2   . HIS   A 1 55  ? -31.154 -36.313  -23.278 1.00 35.04  ? 47  HIS   A NE2   1 
ATOM   265  N N     . PRO   A 1 56  ? -27.449 -39.082  -22.579 1.00 29.98  ? 48  PRO   A N     1 
ATOM   266  C CA    . PRO   A 1 56  ? -26.581 -39.483  -23.691 1.00 29.55  ? 48  PRO   A CA    1 
ATOM   267  C C     . PRO   A 1 56  ? -25.873 -38.363  -24.454 1.00 29.65  ? 48  PRO   A C     1 
ATOM   268  O O     . PRO   A 1 56  ? -24.782 -38.577  -24.976 1.00 29.84  ? 48  PRO   A O     1 
ATOM   269  C CB    . PRO   A 1 56  ? -27.508 -40.272  -24.634 1.00 29.45  ? 48  PRO   A CB    1 
ATOM   270  C CG    . PRO   A 1 56  ? -28.718 -40.659  -23.813 1.00 29.47  ? 48  PRO   A CG    1 
ATOM   271  C CD    . PRO   A 1 56  ? -28.724 -39.813  -22.558 1.00 29.86  ? 48  PRO   A CD    1 
ATOM   272  N N     . ARG   A 1 57  ? -26.504 -37.184  -24.533 1.00 29.96  ? 49  ARG   A N     1 
ATOM   273  C CA    . ARG   A 1 57  ? -25.981 -36.069  -25.311 1.00 30.40  ? 49  ARG   A CA    1 
ATOM   274  C C     . ARG   A 1 57  ? -25.213 -35.076  -24.439 1.00 30.79  ? 49  ARG   A C     1 
ATOM   275  O O     . ARG   A 1 57  ? -24.661 -34.115  -24.965 1.00 29.64  ? 49  ARG   A O     1 
ATOM   276  C CB    . ARG   A 1 57  ? -27.118 -35.333  -26.028 1.00 30.48  ? 49  ARG   A CB    1 
ATOM   277  C CG    . ARG   A 1 57  ? -27.528 -35.956  -27.354 1.00 31.94  ? 49  ARG   A CG    1 
ATOM   278  C CD    . ARG   A 1 57  ? -28.877 -35.455  -27.861 1.00 32.83  ? 49  ARG   A CD    1 
ATOM   279  N NE    . ARG   A 1 57  ? -29.049 -34.000  -27.755 1.00 33.17  ? 49  ARG   A NE    1 
ATOM   280  C CZ    . ARG   A 1 57  ? -30.002 -33.350  -27.082 1.00 33.24  ? 49  ARG   A CZ    1 
ATOM   281  N NH1   . ARG   A 1 57  ? -30.984 -33.999  -26.477 1.00 33.00  ? 49  ARG   A NH1   1 
ATOM   282  N NH2   . ARG   A 1 57  ? -29.971 -32.029  -27.025 1.00 33.73  ? 49  ARG   A NH2   1 
ATOM   283  N N     . PHE   A 1 58  ? -25.161 -35.313  -23.122 1.00 32.18  ? 50  PHE   A N     1 
ATOM   284  C CA    . PHE   A 1 58  ? -24.681 -34.309  -22.183 1.00 34.37  ? 50  PHE   A CA    1 
ATOM   285  C C     . PHE   A 1 58  ? -23.167 -34.425  -22.006 1.00 35.00  ? 50  PHE   A C     1 
ATOM   286  O O     . PHE   A 1 58  ? -22.690 -34.780  -20.930 1.00 34.89  ? 50  PHE   A O     1 
ATOM   287  C CB    . PHE   A 1 58  ? -25.427 -34.491  -20.857 1.00 34.99  ? 50  PHE   A CB    1 
ATOM   288  C CG    . PHE   A 1 58  ? -25.196 -33.391  -19.827 1.00 35.26  ? 50  PHE   A CG    1 
ATOM   289  C CD1   . PHE   A 1 58  ? -25.376 -32.052  -20.160 1.00 35.34  ? 50  PHE   A CD1   1 
ATOM   290  C CD2   . PHE   A 1 58  ? -24.787 -33.699  -18.533 1.00 35.34  ? 50  PHE   A CD2   1 
ATOM   291  C CE1   . PHE   A 1 58  ? -25.167 -31.053  -19.220 1.00 35.21  ? 50  PHE   A CE1   1 
ATOM   292  C CE2   . PHE   A 1 58  ? -24.577 -32.696  -17.599 1.00 35.38  ? 50  PHE   A CE2   1 
ATOM   293  C CZ    . PHE   A 1 58  ? -24.768 -31.377  -17.944 1.00 35.39  ? 50  PHE   A CZ    1 
ATOM   294  N N     . LYS   A 1 59  ? -22.413 -34.099  -23.061 1.00 35.31  ? 51  LYS   A N     1 
ATOM   295  C CA    . LYS   A 1 59  ? -20.967 -34.232  -23.029 1.00 35.45  ? 51  LYS   A CA    1 
ATOM   296  C C     . LYS   A 1 59  ? -20.404 -33.290  -21.967 1.00 34.82  ? 51  LYS   A C     1 
ATOM   297  O O     . LYS   A 1 59  ? -20.808 -32.133  -21.890 1.00 34.34  ? 51  LYS   A O     1 
ATOM   298  C CB    . LYS   A 1 59  ? -20.388 -33.983  -24.425 1.00 37.14  ? 51  LYS   A CB    1 
ATOM   299  C CG    . LYS   A 1 59  ? -18.872 -34.098  -24.521 1.00 39.37  ? 51  LYS   A CG    1 
ATOM   300  C CD    . LYS   A 1 59  ? -18.354 -34.230  -25.948 1.00 40.54  ? 51  LYS   A CD    1 
ATOM   301  C CE    . LYS   A 1 59  ? -16.857 -34.223  -26.024 1.00 41.58  ? 51  LYS   A CE    1 
ATOM   302  N NZ    . LYS   A 1 59  ? -16.384 -34.216  -27.412 1.00 42.38  ? 51  LYS   A NZ    1 
ATOM   303  N N     . ARG   A 1 60  ? -19.478 -33.810  -21.151 1.00 34.79  ? 52  ARG   A N     1 
ATOM   304  C CA    . ARG   A 1 60  ? -18.903 -33.079  -20.032 1.00 34.43  ? 52  ARG   A CA    1 
ATOM   305  C C     . ARG   A 1 60  ? -17.408 -32.878  -20.268 1.00 35.08  ? 52  ARG   A C     1 
ATOM   306  O O     . ARG   A 1 60  ? -16.772 -33.680  -20.946 1.00 34.31  ? 52  ARG   A O     1 
ATOM   307  C CB    . ARG   A 1 60  ? -19.155 -33.847  -18.730 1.00 34.27  ? 52  ARG   A CB    1 
ATOM   308  C CG    . ARG   A 1 60  ? -20.633 -34.031  -18.417 1.00 34.22  ? 52  ARG   A CG    1 
ATOM   309  C CD    . ARG   A 1 60  ? -20.881 -34.842  -17.160 1.00 33.88  ? 52  ARG   A CD    1 
ATOM   310  N NE    . ARG   A 1 60  ? -20.605 -36.277  -17.297 1.00 33.81  ? 52  ARG   A NE    1 
ATOM   311  C CZ    . ARG   A 1 60  ? -21.348 -37.169  -17.948 1.00 34.28  ? 52  ARG   A CZ    1 
ATOM   312  N NH1   . ARG   A 1 60  ? -22.363 -36.789  -18.706 1.00 34.91  ? 52  ARG   A NH1   1 
ATOM   313  N NH2   . ARG   A 1 60  ? -21.059 -38.456  -17.850 1.00 34.63  ? 52  ARG   A NH2   1 
ATOM   314  N N     . GLU   A 1 61  ? -16.865 -31.800  -19.689 1.00 36.87  ? 53  GLU   A N     1 
ATOM   315  C CA    . GLU   A 1 61  ? -15.463 -31.445  -19.836 1.00 38.47  ? 53  GLU   A CA    1 
ATOM   316  C C     . GLU   A 1 61  ? -14.776 -31.551  -18.475 1.00 39.28  ? 53  GLU   A C     1 
ATOM   317  O O     . GLU   A 1 61  ? -15.347 -31.153  -17.463 1.00 38.71  ? 53  GLU   A O     1 
ATOM   318  C CB    . GLU   A 1 61  ? -15.384 -30.037  -20.427 1.00 39.54  ? 53  GLU   A CB    1 
ATOM   319  C CG    . GLU   A 1 61  ? -13.963 -29.513  -20.616 1.00 40.10  ? 53  GLU   A CG    1 
ATOM   320  C CD    . GLU   A 1 61  ? -13.052 -30.437  -21.402 1.00 40.70  ? 53  GLU   A CD    1 
ATOM   321  O OE1   . GLU   A 1 61  ? -13.511 -30.990  -22.424 1.00 40.90  ? 53  GLU   A OE1   1 
ATOM   322  O OE2   . GLU   A 1 61  ? -11.878 -30.588  -20.999 1.00 41.22  ? 53  GLU   A OE2   1 
ATOM   323  N N     . PHE   A 1 62  ? -13.549 -32.090  -18.466 1.00 40.88  ? 54  PHE   A N     1 
ATOM   324  C CA    . PHE   A 1 62  ? -12.846 -32.408  -17.231 1.00 41.41  ? 54  PHE   A CA    1 
ATOM   325  C C     . PHE   A 1 62  ? -11.560 -31.590  -17.087 1.00 44.45  ? 54  PHE   A C     1 
ATOM   326  O O     . PHE   A 1 62  ? -11.131 -31.340  -15.963 1.00 45.22  ? 54  PHE   A O     1 
ATOM   327  C CB    . PHE   A 1 62  ? -12.587 -33.918  -17.187 1.00 39.92  ? 54  PHE   A CB    1 
ATOM   328  C CG    . PHE   A 1 62  ? -13.843 -34.757  -16.990 1.00 38.28  ? 54  PHE   A CG    1 
ATOM   329  C CD1   . PHE   A 1 62  ? -14.322 -35.035  -15.714 1.00 38.19  ? 54  PHE   A CD1   1 
ATOM   330  C CD2   . PHE   A 1 62  ? -14.547 -35.262  -18.079 1.00 38.03  ? 54  PHE   A CD2   1 
ATOM   331  C CE1   . PHE   A 1 62  ? -15.470 -35.795  -15.535 1.00 37.87  ? 54  PHE   A CE1   1 
ATOM   332  C CE2   . PHE   A 1 62  ? -15.694 -36.021  -17.895 1.00 37.65  ? 54  PHE   A CE2   1 
ATOM   333  C CZ    . PHE   A 1 62  ? -16.153 -36.285  -16.624 1.00 37.50  ? 54  PHE   A CZ    1 
ATOM   334  N N     . ILE   A 1 63  ? -10.939 -31.180  -18.202 1.00 48.25  ? 55  ILE   A N     1 
ATOM   335  C CA    . ILE   A 1 63  ? -9.683  -30.443  -18.143 1.00 51.34  ? 55  ILE   A CA    1 
ATOM   336  C C     . ILE   A 1 63  ? -9.938  -28.954  -18.378 1.00 53.95  ? 55  ILE   A C     1 
ATOM   337  O O     . ILE   A 1 63  ? -9.475  -28.116  -17.605 1.00 55.06  ? 55  ILE   A O     1 
ATOM   338  C CB    . ILE   A 1 63  ? -8.647  -30.995  -19.145 1.00 52.16  ? 55  ILE   A CB    1 
ATOM   339  C CG1   . ILE   A 1 63  ? -8.350  -32.486  -18.921 1.00 53.36  ? 55  ILE   A CG1   1 
ATOM   340  C CG2   . ILE   A 1 63  ? -7.361  -30.165  -19.112 1.00 52.40  ? 55  ILE   A CG2   1 
ATOM   341  C CD1   . ILE   A 1 63  ? -9.254  -33.434  -19.689 1.00 53.42  ? 55  ILE   A CD1   1 
ATOM   342  N N     . GLN   A 1 64  ? -10.672 -28.637  -19.451 1.00 55.91  ? 56  GLN   A N     1 
ATOM   343  C CA    . GLN   A 1 64  ? -10.597 -27.328  -20.081 1.00 56.22  ? 56  GLN   A CA    1 
ATOM   344  C C     . GLN   A 1 64  ? -11.641 -26.381  -19.494 1.00 54.51  ? 56  GLN   A C     1 
ATOM   345  O O     . GLN   A 1 64  ? -12.832 -26.684  -19.482 1.00 52.68  ? 56  GLN   A O     1 
ATOM   346  C CB    . GLN   A 1 64  ? -10.767 -27.518  -21.590 1.00 58.27  ? 56  GLN   A CB    1 
ATOM   347  C CG    . GLN   A 1 64  ? -10.015 -26.500  -22.441 1.00 61.39  ? 56  GLN   A CG    1 
ATOM   348  C CD    . GLN   A 1 64  ? -8.564  -26.355  -22.035 1.00 65.58  ? 56  GLN   A CD    1 
ATOM   349  O OE1   . GLN   A 1 64  ? -7.855  -27.344  -21.817 1.00 68.65  ? 56  GLN   A OE1   1 
ATOM   350  N NE2   . GLN   A 1 64  ? -8.114  -25.116  -21.891 1.00 68.27  ? 56  GLN   A NE2   1 
ATOM   351  N N     . GLU   A 1 65  ? -11.165 -25.228  -19.005 1.00 54.48  ? 57  GLU   A N     1 
ATOM   352  C CA    . GLU   A 1 65  ? -12.025 -24.123  -18.613 1.00 54.43  ? 57  GLU   A CA    1 
ATOM   353  C C     . GLU   A 1 65  ? -12.473 -23.393  -19.877 1.00 52.75  ? 57  GLU   A C     1 
ATOM   354  O O     . GLU   A 1 65  ? -11.731 -23.358  -20.856 1.00 52.82  ? 57  GLU   A O     1 
ATOM   355  C CB    . GLU   A 1 65  ? -11.286 -23.182  -17.661 1.00 55.28  ? 57  GLU   A CB    1 
ATOM   356  C CG    . GLU   A 1 65  ? -11.000 -23.807  -16.299 1.00 58.22  ? 57  GLU   A CG    1 
ATOM   357  C CD    . GLU   A 1 65  ? -10.399 -22.854  -15.280 1.00 60.89  ? 57  GLU   A CD    1 
ATOM   358  O OE1   . GLU   A 1 65  ? -9.298  -22.326  -15.544 1.00 62.95  ? 57  GLU   A OE1   1 
ATOM   359  O OE2   . GLU   A 1 65  ? -11.032 -22.641  -14.222 1.00 61.41  ? 57  GLU   A OE2   1 
ATOM   360  N N     . PRO   A 1 66  ? -13.682 -22.784  -19.918 1.00 50.82  ? 58  PRO   A N     1 
ATOM   361  C CA    . PRO   A 1 66  ? -14.589 -22.717  -18.768 1.00 49.51  ? 58  PRO   A CA    1 
ATOM   362  C C     . PRO   A 1 66  ? -15.547 -23.893  -18.577 1.00 47.33  ? 58  PRO   A C     1 
ATOM   363  O O     . PRO   A 1 66  ? -16.147 -24.026  -17.512 1.00 46.60  ? 58  PRO   A O     1 
ATOM   364  C CB    . PRO   A 1 66  ? -15.348 -21.421  -19.105 1.00 50.11  ? 58  PRO   A CB    1 
ATOM   365  C CG    . PRO   A 1 66  ? -15.511 -21.476  -20.608 1.00 50.19  ? 58  PRO   A CG    1 
ATOM   366  C CD    . PRO   A 1 66  ? -14.226 -22.109  -21.107 1.00 50.55  ? 58  PRO   A CD    1 
ATOM   367  N N     . ALA   A 1 67  ? -15.657 -24.750  -19.602 1.00 45.58  ? 59  ALA   A N     1 
ATOM   368  C CA    . ALA   A 1 67  ? -16.693 -25.772  -19.688 1.00 45.34  ? 59  ALA   A CA    1 
ATOM   369  C C     . ALA   A 1 67  ? -16.664 -26.750  -18.511 1.00 44.61  ? 59  ALA   A C     1 
ATOM   370  O O     . ALA   A 1 67  ? -17.694 -27.340  -18.186 1.00 43.42  ? 59  ALA   A O     1 
ATOM   371  C CB    . ALA   A 1 67  ? -16.556 -26.519  -20.996 1.00 45.71  ? 59  ALA   A CB    1 
ATOM   372  N N     . LYS   A 1 68  ? -15.490 -26.944  -17.894 1.00 43.60  ? 60  LYS   A N     1 
ATOM   373  C CA    . LYS   A 1 68  ? -15.349 -27.908  -16.811 1.00 44.45  ? 60  LYS   A CA    1 
ATOM   374  C C     . LYS   A 1 68  ? -16.096 -27.444  -15.560 1.00 42.33  ? 60  LYS   A C     1 
ATOM   375  O O     . LYS   A 1 68  ? -16.479 -28.271  -14.736 1.00 41.70  ? 60  LYS   A O     1 
ATOM   376  C CB    . LYS   A 1 68  ? -13.884 -28.198  -16.462 1.00 45.94  ? 60  LYS   A CB    1 
ATOM   377  C CG    . LYS   A 1 68  ? -13.039 -27.007  -16.027 1.00 47.40  ? 60  LYS   A CG    1 
ATOM   378  C CD    . LYS   A 1 68  ? -11.704 -27.415  -15.420 1.00 48.84  ? 60  LYS   A CD    1 
ATOM   379  C CE    . LYS   A 1 68  ? -11.835 -27.901  -14.011 1.00 50.43  ? 60  LYS   A CE    1 
ATOM   380  N NZ    . LYS   A 1 68  ? -10.562 -28.415  -13.501 1.00 50.92  ? 60  LYS   A NZ    1 
ATOM   381  N N     . ASN   A 1 69  ? -16.309 -26.129  -15.428 1.00 41.35  ? 61  ASN   A N     1 
ATOM   382  C CA    . ASN   A 1 69  ? -16.938 -25.563  -14.245 1.00 41.07  ? 61  ASN   A CA    1 
ATOM   383  C C     . ASN   A 1 69  ? -18.449 -25.459  -14.441 1.00 39.25  ? 61  ASN   A C     1 
ATOM   384  O O     . ASN   A 1 69  ? -19.121 -24.772  -13.675 1.00 37.89  ? 61  ASN   A O     1 
ATOM   385  C CB    . ASN   A 1 69  ? -16.336 -24.206  -13.903 1.00 42.30  ? 61  ASN   A CB    1 
ATOM   386  C CG    . ASN   A 1 69  ? -14.828 -24.254  -13.889 1.00 44.24  ? 61  ASN   A CG    1 
ATOM   387  O OD1   . ASN   A 1 69  ? -14.179 -23.662  -14.760 1.00 46.55  ? 61  ASN   A OD1   1 
ATOM   388  N ND2   . ASN   A 1 69  ? -14.257 -24.975  -12.936 1.00 44.89  ? 61  ASN   A ND2   1 
ATOM   389  N N     . ARG   A 1 70  ? -18.976 -26.136  -15.469 1.00 38.21  ? 62  ARG   A N     1 
ATOM   390  C CA    . ARG   A 1 70  ? -20.410 -26.210  -15.690 1.00 37.90  ? 62  ARG   A CA    1 
ATOM   391  C C     . ARG   A 1 70  ? -21.111 -26.507  -14.366 1.00 37.01  ? 62  ARG   A C     1 
ATOM   392  O O     . ARG   A 1 70  ? -20.917 -27.577  -13.797 1.00 36.88  ? 62  ARG   A O     1 
ATOM   393  C CB    . ARG   A 1 70  ? -20.732 -27.303  -16.714 1.00 37.72  ? 62  ARG   A CB    1 
ATOM   394  C CG    . ARG   A 1 70  ? -22.213 -27.630  -16.866 1.00 37.76  ? 62  ARG   A CG    1 
ATOM   395  C CD    . ARG   A 1 70  ? -22.435 -28.798  -17.808 1.00 37.86  ? 62  ARG   A CD    1 
ATOM   396  N NE    . ARG   A 1 70  ? -21.686 -28.613  -19.056 1.00 38.30  ? 62  ARG   A NE    1 
ATOM   397  C CZ    . ARG   A 1 70  ? -21.424 -29.549  -19.957 1.00 38.38  ? 62  ARG   A CZ    1 
ATOM   398  N NH1   . ARG   A 1 70  ? -21.979 -30.747  -19.869 1.00 38.16  ? 62  ARG   A NH1   1 
ATOM   399  N NH2   . ARG   A 1 70  ? -20.615 -29.267  -20.964 1.00 39.09  ? 62  ARG   A NH2   1 
ATOM   400  N N     . PRO   A 1 71  ? -21.943 -25.579  -13.839 1.00 36.64  ? 63  PRO   A N     1 
ATOM   401  C CA    . PRO   A 1 71  ? -22.689 -25.834  -12.606 1.00 36.70  ? 63  PRO   A CA    1 
ATOM   402  C C     . PRO   A 1 71  ? -23.437 -27.158  -12.688 1.00 35.90  ? 63  PRO   A C     1 
ATOM   403  O O     . PRO   A 1 71  ? -23.998 -27.486  -13.733 1.00 35.22  ? 63  PRO   A O     1 
ATOM   404  C CB    . PRO   A 1 71  ? -23.651 -24.638  -12.503 1.00 37.61  ? 63  PRO   A CB    1 
ATOM   405  C CG    . PRO   A 1 71  ? -22.964 -23.536  -13.284 1.00 37.49  ? 63  PRO   A CG    1 
ATOM   406  C CD    . PRO   A 1 71  ? -22.206 -24.242  -14.396 1.00 37.12  ? 63  PRO   A CD    1 
ATOM   407  N N     . GLY   A 1 72  ? -23.416 -27.912  -11.584 1.00 34.54  ? 64  GLY   A N     1 
ATOM   408  C CA    . GLY   A 1 72  ? -24.228 -29.110  -11.456 1.00 33.97  ? 64  GLY   A CA    1 
ATOM   409  C C     . GLY   A 1 72  ? -25.706 -28.744  -11.346 1.00 33.45  ? 64  GLY   A C     1 
ATOM   410  O O     . GLY   A 1 72  ? -26.056 -27.572  -11.459 1.00 33.14  ? 64  GLY   A O     1 
ATOM   411  N N     . PRO   A 1 73  ? -26.627 -29.710  -11.126 1.00 33.95  ? 65  PRO   A N     1 
ATOM   412  C CA    . PRO   A 1 73  ? -26.288 -31.135  -11.066 1.00 35.00  ? 65  PRO   A CA    1 
ATOM   413  C C     . PRO   A 1 73  ? -25.866 -31.737  -12.404 1.00 35.81  ? 65  PRO   A C     1 
ATOM   414  O O     . PRO   A 1 73  ? -26.333 -31.308  -13.457 1.00 37.21  ? 65  PRO   A O     1 
ATOM   415  C CB    . PRO   A 1 73  ? -27.581 -31.780  -10.538 1.00 34.97  ? 65  PRO   A CB    1 
ATOM   416  C CG    . PRO   A 1 73  ? -28.681 -30.826  -10.951 1.00 34.80  ? 65  PRO   A CG    1 
ATOM   417  C CD    . PRO   A 1 73  ? -28.053 -29.450  -10.875 1.00 34.06  ? 65  PRO   A CD    1 
ATOM   418  N N     . GLN   A 1 74  ? -24.987 -32.745  -12.339 1.00 35.96  ? 66  GLN   A N     1 
ATOM   419  C CA    . GLN   A 1 74  ? -24.434 -33.363  -13.533 1.00 36.73  ? 66  GLN   A CA    1 
ATOM   420  C C     . GLN   A 1 74  ? -25.386 -34.430  -14.072 1.00 36.30  ? 66  GLN   A C     1 
ATOM   421  O O     . GLN   A 1 74  ? -25.252 -34.823  -15.227 1.00 37.63  ? 66  GLN   A O     1 
ATOM   422  C CB    . GLN   A 1 74  ? -23.049 -33.955  -13.269 1.00 37.48  ? 66  GLN   A CB    1 
ATOM   423  C CG    . GLN   A 1 74  ? -21.997 -32.936  -12.840 1.00 37.82  ? 66  GLN   A CG    1 
ATOM   424  C CD    . GLN   A 1 74  ? -21.747 -31.863  -13.878 1.00 39.09  ? 66  GLN   A CD    1 
ATOM   425  O OE1   . GLN   A 1 74  ? -21.535 -32.150  -15.062 1.00 38.72  ? 66  GLN   A OE1   1 
ATOM   426  N NE2   . GLN   A 1 74  ? -21.785 -30.610  -13.446 1.00 39.95  ? 66  GLN   A NE2   1 
ATOM   427  N N     . THR   A 1 75  ? -26.332 -34.900  -13.244 1.00 35.99  ? 67  THR   A N     1 
ATOM   428  C CA    . THR   A 1 75  ? -27.368 -35.814  -13.707 1.00 36.10  ? 67  THR   A CA    1 
ATOM   429  C C     . THR   A 1 75  ? -28.512 -35.887  -12.697 1.00 37.05  ? 67  THR   A C     1 
ATOM   430  O O     . THR   A 1 75  ? -28.630 -35.040  -11.815 1.00 36.10  ? 67  THR   A O     1 
ATOM   431  C CB    . THR   A 1 75  ? -26.771 -37.196  -13.971 1.00 36.28  ? 67  THR   A CB    1 
ATOM   432  O OG1   . THR   A 1 75  ? -27.867 -37.999  -14.395 1.00 36.03  ? 67  THR   A OG1   1 
ATOM   433  C CG2   . THR   A 1 75  ? -26.126 -37.815  -12.743 1.00 36.51  ? 67  THR   A CG2   1 
ATOM   434  N N     . ARG   A 1 76  ? -29.354 -36.916  -12.867 1.00 39.03  ? 68  ARG   A N     1 
ATOM   435  C CA    . ARG   A 1 76  ? -30.509 -37.173  -12.021 1.00 41.70  ? 68  ARG   A CA    1 
ATOM   436  C C     . ARG   A 1 76  ? -30.093 -37.695  -10.647 1.00 42.75  ? 68  ARG   A C     1 
ATOM   437  O O     . ARG   A 1 76  ? -28.965 -38.149  -10.461 1.00 43.32  ? 68  ARG   A O     1 
ATOM   438  C CB    . ARG   A 1 76  ? -31.419 -38.217  -12.678 1.00 43.57  ? 68  ARG   A CB    1 
ATOM   439  C CG    . ARG   A 1 76  ? -32.472 -37.618  -13.594 1.00 46.05  ? 68  ARG   A CG    1 
ATOM   440  C CD    . ARG   A 1 76  ? -33.549 -38.623  -13.949 1.00 48.54  ? 68  ARG   A CD    1 
ATOM   441  N NE    . ARG   A 1 76  ? -33.166 -39.528  -15.039 1.00 50.69  ? 68  ARG   A NE    1 
ATOM   442  C CZ    . ARG   A 1 76  ? -33.659 -39.487  -16.276 1.00 51.42  ? 68  ARG   A CZ    1 
ATOM   443  N NH1   . ARG   A 1 76  ? -34.406 -38.468  -16.671 1.00 50.37  ? 68  ARG   A NH1   1 
ATOM   444  N NH2   . ARG   A 1 76  ? -33.374 -40.456  -17.130 1.00 52.28  ? 68  ARG   A NH2   1 
ATOM   445  N N     . SER   A 1 77  ? -31.052 -37.669  -9.709  1.00 43.31  ? 69  SER   A N     1 
ATOM   446  C CA    . SER   A 1 77  ? -30.820 -38.032  -8.318  1.00 41.61  ? 69  SER   A CA    1 
ATOM   447  C C     . SER   A 1 77  ? -31.138 -39.505  -8.073  1.00 39.52  ? 69  SER   A C     1 
ATOM   448  O O     . SER   A 1 77  ? -32.068 -40.056  -8.656  1.00 36.35  ? 69  SER   A O     1 
ATOM   449  C CB    . SER   A 1 77  ? -31.624 -37.156  -7.390  1.00 42.18  ? 69  SER   A CB    1 
ATOM   450  O OG    . SER   A 1 77  ? -31.612 -37.662  -6.060  1.00 43.28  ? 69  SER   A OG    1 
ATOM   451  N N     . ASP   A 1 78  ? -30.370 -40.104  -7.152  1.00 40.72  ? 70  ASP   A N     1 
ATOM   452  C CA    . ASP   A 1 78  ? -30.557 -41.480  -6.716  1.00 40.81  ? 70  ASP   A CA    1 
ATOM   453  C C     . ASP   A 1 78  ? -31.878 -41.645  -5.966  1.00 38.92  ? 70  ASP   A C     1 
ATOM   454  O O     . ASP   A 1 78  ? -32.401 -42.754  -5.877  1.00 36.85  ? 70  ASP   A O     1 
ATOM   455  C CB    . ASP   A 1 78  ? -29.393 -41.945  -5.853  1.00 42.22  ? 70  ASP   A CB    1 
ATOM   456  C CG    . ASP   A 1 78  ? -29.091 -41.111  -4.613  1.00 43.76  ? 70  ASP   A CG    1 
ATOM   457  O OD1   . ASP   A 1 78  ? -29.665 -40.006  -4.482  1.00 44.75  ? 70  ASP   A OD1   1 
ATOM   458  O OD2   . ASP   A 1 78  ? -28.282 -41.577  -3.782  1.00 43.69  ? 70  ASP   A OD2   1 
ATOM   459  N N     . LEU   A 1 79  ? -32.410 -40.537  -5.433  1.00 39.17  ? 71  LEU   A N     1 
ATOM   460  C CA    . LEU   A 1 79  ? -33.622 -40.558  -4.627  1.00 40.05  ? 71  LEU   A CA    1 
ATOM   461  C C     . LEU   A 1 79  ? -34.860 -40.830  -5.484  1.00 40.79  ? 71  LEU   A C     1 
ATOM   462  O O     . LEU   A 1 79  ? -35.941 -41.046  -4.940  1.00 41.26  ? 71  LEU   A O     1 
ATOM   463  C CB    . LEU   A 1 79  ? -33.747 -39.236  -3.869  1.00 39.19  ? 71  LEU   A CB    1 
ATOM   464  C CG    . LEU   A 1 79  ? -32.775 -39.032  -2.701  1.00 38.88  ? 71  LEU   A CG    1 
ATOM   465  C CD1   . LEU   A 1 79  ? -32.746 -37.583  -2.252  1.00 38.80  ? 71  LEU   A CD1   1 
ATOM   466  C CD2   . LEU   A 1 79  ? -33.133 -39.931  -1.530  1.00 38.15  ? 71  LEU   A CD2   1 
ATOM   467  N N     . LEU   A 1 80  ? -34.703 -40.837  -6.815  1.00 41.36  ? 72  LEU   A N     1 
ATOM   468  C CA    . LEU   A 1 80  ? -35.830 -40.985  -7.724  1.00 41.34  ? 72  LEU   A CA    1 
ATOM   469  C C     . LEU   A 1 80  ? -36.306 -42.437  -7.792  1.00 41.53  ? 72  LEU   A C     1 
ATOM   470  O O     . LEU   A 1 80  ? -37.385 -42.696  -8.323  1.00 41.33  ? 72  LEU   A O     1 
ATOM   471  C CB    . LEU   A 1 80  ? -35.447 -40.440  -9.100  1.00 40.69  ? 72  LEU   A CB    1 
ATOM   472  C CG    . LEU   A 1 80  ? -35.328 -38.915  -9.190  1.00 41.10  ? 72  LEU   A CG    1 
ATOM   473  C CD1   . LEU   A 1 80  ? -34.584 -38.466  -10.436 1.00 40.98  ? 72  LEU   A CD1   1 
ATOM   474  C CD2   . LEU   A 1 80  ? -36.703 -38.273  -9.145  1.00 40.89  ? 72  LEU   A CD2   1 
ATOM   475  N N     . LEU   A 1 81  ? -35.515 -43.376  -7.254  1.00 41.62  ? 73  LEU   A N     1 
ATOM   476  C CA    . LEU   A 1 81  ? -35.926 -44.769  -7.166  1.00 41.17  ? 73  LEU   A CA    1 
ATOM   477  C C     . LEU   A 1 81  ? -35.503 -45.353  -5.822  1.00 40.15  ? 73  LEU   A C     1 
ATOM   478  O O     . LEU   A 1 81  ? -34.558 -44.873  -5.199  1.00 38.83  ? 73  LEU   A O     1 
ATOM   479  C CB    . LEU   A 1 81  ? -35.325 -45.578  -8.315  1.00 41.14  ? 73  LEU   A CB    1 
ATOM   480  C CG    . LEU   A 1 81  ? -35.936 -45.365  -9.703  1.00 41.56  ? 73  LEU   A CG    1 
ATOM   481  C CD1   . LEU   A 1 81  ? -35.070 -46.053  -10.743 1.00 41.92  ? 73  LEU   A CD1   1 
ATOM   482  C CD2   . LEU   A 1 81  ? -37.361 -45.884  -9.777  1.00 41.39  ? 73  LEU   A CD2   1 
ATOM   483  N N     . SER   A 1 82  ? -36.213 -46.407  -5.402  1.00 40.37  ? 74  SER   A N     1 
ATOM   484  C CA    . SER   A 1 82  ? -35.822 -47.187  -4.241  1.00 41.75  ? 74  SER   A CA    1 
ATOM   485  C C     . SER   A 1 82  ? -34.529 -47.937  -4.550  1.00 43.20  ? 74  SER   A C     1 
ATOM   486  O O     . SER   A 1 82  ? -34.303 -48.350  -5.688  1.00 41.76  ? 74  SER   A O     1 
ATOM   487  C CB    . SER   A 1 82  ? -36.915 -48.146  -3.821  1.00 41.78  ? 74  SER   A CB    1 
ATOM   488  O OG    . SER   A 1 82  ? -37.148 -49.136  -4.814  1.00 41.83  ? 74  SER   A OG    1 
ATOM   489  N N     . GLY   A 1 83  ? -33.688 -48.107  -3.524  1.00 43.86  ? 75  GLY   A N     1 
ATOM   490  C CA    . GLY   A 1 83  ? -32.513 -48.955  -3.625  1.00 44.40  ? 75  GLY   A CA    1 
ATOM   491  C C     . GLY   A 1 83  ? -32.867 -50.308  -4.238  1.00 44.62  ? 75  GLY   A C     1 
ATOM   492  O O     . GLY   A 1 83  ? -32.121 -50.836  -5.058  1.00 45.66  ? 75  GLY   A O     1 
ATOM   493  N N     . ARG   A 1 84  ? -34.019 -50.846  -3.822  1.00 45.32  ? 76  ARG   A N     1 
ATOM   494  C CA    . ARG   A 1 84  ? -34.548 -52.097  -4.336  1.00 46.81  ? 76  ARG   A CA    1 
ATOM   495  C C     . ARG   A 1 84  ? -34.568 -52.094  -5.864  1.00 46.50  ? 76  ARG   A C     1 
ATOM   496  O O     . ARG   A 1 84  ? -34.166 -53.072  -6.493  1.00 46.37  ? 76  ARG   A O     1 
ATOM   497  C CB    . ARG   A 1 84  ? -35.966 -52.285  -3.780  1.00 49.87  ? 76  ARG   A CB    1 
ATOM   498  C CG    . ARG   A 1 84  ? -36.637 -53.602  -4.142  1.00 52.83  ? 76  ARG   A CG    1 
ATOM   499  C CD    . ARG   A 1 84  ? -35.844 -54.760  -3.573  1.00 56.28  ? 76  ARG   A CD    1 
ATOM   500  N NE    . ARG   A 1 84  ? -36.242 -56.062  -4.117  1.00 59.45  ? 76  ARG   A NE    1 
ATOM   501  C CZ    . ARG   A 1 84  ? -35.491 -57.157  -4.052  1.00 62.24  ? 76  ARG   A CZ    1 
ATOM   502  N NH1   . ARG   A 1 84  ? -34.289 -57.118  -3.496  1.00 62.08  ? 76  ARG   A NH1   1 
ATOM   503  N NH2   . ARG   A 1 84  ? -35.939 -58.293  -4.560  1.00 63.80  ? 76  ARG   A NH2   1 
ATOM   504  N N     . ASP   A 1 85  ? -35.051 -50.991  -6.447  1.00 44.63  ? 77  ASP   A N     1 
ATOM   505  C CA    . ASP   A 1 85  ? -35.246 -50.884  -7.884  1.00 44.25  ? 77  ASP   A CA    1 
ATOM   506  C C     . ASP   A 1 85  ? -33.902 -50.760  -8.596  1.00 42.39  ? 77  ASP   A C     1 
ATOM   507  O O     . ASP   A 1 85  ? -33.651 -51.475  -9.565  1.00 41.61  ? 77  ASP   A O     1 
ATOM   508  C CB    . ASP   A 1 85  ? -36.177 -49.730  -8.222  1.00 45.37  ? 77  ASP   A CB    1 
ATOM   509  C CG    . ASP   A 1 85  ? -37.622 -49.906  -7.778  1.00 45.81  ? 77  ASP   A CG    1 
ATOM   510  O OD1   . ASP   A 1 85  ? -37.965 -51.013  -7.308  1.00 45.51  ? 77  ASP   A OD1   1 
ATOM   511  O OD2   . ASP   A 1 85  ? -38.392 -48.931  -7.897  1.00 46.60  ? 77  ASP   A OD2   1 
ATOM   512  N N     . TRP   A 1 86  ? -33.056 -49.840  -8.117  1.00 40.24  ? 78  TRP   A N     1 
ATOM   513  C CA    . TRP   A 1 86  ? -31.716 -49.660  -8.655  1.00 39.51  ? 78  TRP   A CA    1 
ATOM   514  C C     . TRP   A 1 86  ? -30.996 -51.005  -8.762  1.00 39.87  ? 78  TRP   A C     1 
ATOM   515  O O     . TRP   A 1 86  ? -30.383 -51.298  -9.786  1.00 40.11  ? 78  TRP   A O     1 
ATOM   516  C CB    . TRP   A 1 86  ? -30.911 -48.693  -7.776  1.00 38.61  ? 78  TRP   A CB    1 
ATOM   517  C CG    . TRP   A 1 86  ? -31.350 -47.251  -7.815  1.00 38.50  ? 78  TRP   A CG    1 
ATOM   518  C CD1   . TRP   A 1 86  ? -31.717 -46.502  -6.735  1.00 38.77  ? 78  TRP   A CD1   1 
ATOM   519  C CD2   . TRP   A 1 86  ? -31.397 -46.358  -8.953  1.00 38.73  ? 78  TRP   A CD2   1 
ATOM   520  N NE1   . TRP   A 1 86  ? -32.019 -45.223  -7.117  1.00 38.74  ? 78  TRP   A NE1   1 
ATOM   521  C CE2   . TRP   A 1 86  ? -31.826 -45.101  -8.469  1.00 38.75  ? 78  TRP   A CE2   1 
ATOM   522  C CE3   . TRP   A 1 86  ? -31.130 -46.491  -10.323 1.00 38.09  ? 78  TRP   A CE3   1 
ATOM   523  C CZ2   . TRP   A 1 86  ? -31.995 -43.997  -9.304  1.00 37.67  ? 78  TRP   A CZ2   1 
ATOM   524  C CZ3   . TRP   A 1 86  ? -31.294 -45.395  -11.145 1.00 37.16  ? 78  TRP   A CZ3   1 
ATOM   525  C CH2   . TRP   A 1 86  ? -31.716 -44.166  -10.641 1.00 36.66  ? 78  TRP   A CH2   1 
ATOM   526  N N     . ASN   A 1 87  ? -31.086 -51.817  -7.699  1.00 39.22  ? 79  ASN   A N     1 
ATOM   527  C CA    . ASN   A 1 87  ? -30.345 -53.065  -7.585  1.00 38.73  ? 79  ASN   A CA    1 
ATOM   528  C C     . ASN   A 1 87  ? -30.867 -54.156  -8.516  1.00 38.35  ? 79  ASN   A C     1 
ATOM   529  O O     . ASN   A 1 87  ? -30.124 -55.080  -8.834  1.00 37.82  ? 79  ASN   A O     1 
ATOM   530  C CB    . ASN   A 1 87  ? -30.430 -53.664  -6.186  1.00 39.29  ? 79  ASN   A CB    1 
ATOM   531  C CG    . ASN   A 1 87  ? -29.551 -52.963  -5.180  1.00 40.21  ? 79  ASN   A CG    1 
ATOM   532  O OD1   . ASN   A 1 87  ? -28.751 -52.092  -5.538  1.00 42.05  ? 79  ASN   A OD1   1 
ATOM   533  N ND2   . ASN   A 1 87  ? -29.673 -53.341  -3.917  1.00 40.69  ? 79  ASN   A ND2   1 
ATOM   534  N N     . THR   A 1 88  ? -32.149 -54.092  -8.894  1.00 39.06  ? 80  THR   A N     1 
ATOM   535  C CA    . THR   A 1 88  ? -32.794 -55.223  -9.544  1.00 39.35  ? 80  THR   A CA    1 
ATOM   536  C C     . THR   A 1 88  ? -33.281 -54.875  -10.950 1.00 38.88  ? 80  THR   A C     1 
ATOM   537  O O     . THR   A 1 88  ? -33.372 -55.766  -11.792 1.00 38.25  ? 80  THR   A O     1 
ATOM   538  C CB    . THR   A 1 88  ? -33.942 -55.722  -8.664  1.00 40.21  ? 80  THR   A CB    1 
ATOM   539  O OG1   . THR   A 1 88  ? -34.827 -54.620  -8.493  1.00 41.12  ? 80  THR   A OG1   1 
ATOM   540  C CG2   . THR   A 1 88  ? -33.466 -56.215  -7.308  1.00 40.32  ? 80  THR   A CG2   1 
ATOM   541  N N     . LEU   A 1 89  ? -33.601 -53.599  -11.206 1.00 39.08  ? 81  LEU   A N     1 
ATOM   542  C CA    . LEU   A 1 89  ? -34.388 -53.237  -12.378 1.00 39.41  ? 81  LEU   A CA    1 
ATOM   543  C C     . LEU   A 1 89  ? -33.583 -52.436  -13.399 1.00 38.77  ? 81  LEU   A C     1 
ATOM   544  O O     . LEU   A 1 89  ? -33.945 -52.424  -14.573 1.00 40.09  ? 81  LEU   A O     1 
ATOM   545  C CB    . LEU   A 1 89  ? -35.623 -52.452  -11.939 1.00 39.85  ? 81  LEU   A CB    1 
ATOM   546  C CG    . LEU   A 1 89  ? -36.588 -53.175  -10.995 1.00 39.66  ? 81  LEU   A CG    1 
ATOM   547  C CD1   . LEU   A 1 89  ? -37.799 -52.298  -10.731 1.00 39.88  ? 81  LEU   A CD1   1 
ATOM   548  C CD2   . LEU   A 1 89  ? -37.016 -54.531  -11.533 1.00 38.95  ? 81  LEU   A CD2   1 
ATOM   549  N N     . ILE   A 1 90  ? -32.521 -51.751  -12.961 1.00 37.49  ? 82  ILE   A N     1 
ATOM   550  C CA    . ILE   A 1 90  ? -31.875 -50.755  -13.800 1.00 36.63  ? 82  ILE   A CA    1 
ATOM   551  C C     . ILE   A 1 90  ? -30.494 -51.252  -14.212 1.00 35.91  ? 82  ILE   A C     1 
ATOM   552  O O     . ILE   A 1 90  ? -29.615 -51.403  -13.368 1.00 37.73  ? 82  ILE   A O     1 
ATOM   553  C CB    . ILE   A 1 90  ? -31.794 -49.397  -13.078 1.00 37.12  ? 82  ILE   A CB    1 
ATOM   554  C CG1   . ILE   A 1 90  ? -33.180 -48.892  -12.654 1.00 37.08  ? 82  ILE   A CG1   1 
ATOM   555  C CG2   . ILE   A 1 90  ? -31.053 -48.365  -13.931 1.00 36.76  ? 82  ILE   A CG2   1 
ATOM   556  C CD1   . ILE   A 1 90  ? -34.134 -48.621  -13.806 1.00 37.23  ? 82  ILE   A CD1   1 
ATOM   557  N N     . VAL   A 1 91  ? -30.328 -51.489  -15.519 1.00 33.97  ? 83  VAL   A N     1 
ATOM   558  C CA    . VAL   A 1 91  ? -29.023 -51.716  -16.117 1.00 32.21  ? 83  VAL   A CA    1 
ATOM   559  C C     . VAL   A 1 91  ? -28.531 -50.386  -16.683 1.00 30.23  ? 83  VAL   A C     1 
ATOM   560  O O     . VAL   A 1 91  ? -29.219 -49.760  -17.484 1.00 30.41  ? 83  VAL   A O     1 
ATOM   561  C CB    . VAL   A 1 91  ? -29.081 -52.806  -17.205 1.00 32.31  ? 83  VAL   A CB    1 
ATOM   562  C CG1   . VAL   A 1 91  ? -27.722 -53.040  -17.855 1.00 32.17  ? 83  VAL   A CG1   1 
ATOM   563  C CG2   . VAL   A 1 91  ? -29.639 -54.117  -16.663 1.00 32.32  ? 83  VAL   A CG2   1 
ATOM   564  N N     . GLY   A 1 92  ? -27.342 -49.959  -16.243 1.00 29.16  ? 84  GLY   A N     1 
ATOM   565  C CA    . GLY   A 1 92  ? -26.739 -48.722  -16.711 1.00 28.63  ? 84  GLY   A CA    1 
ATOM   566  C C     . GLY   A 1 92  ? -26.169 -48.887  -18.117 1.00 28.15  ? 84  GLY   A C     1 
ATOM   567  O O     . GLY   A 1 92  ? -25.992 -50.009  -18.591 1.00 28.68  ? 84  GLY   A O     1 
ATOM   568  N N     . LYS   A 1 93  ? -25.895 -47.755  -18.775 1.00 27.09  ? 85  LYS   A N     1 
ATOM   569  C CA    . LYS   A 1 93  ? -25.330 -47.746  -20.115 1.00 26.89  ? 85  LYS   A CA    1 
ATOM   570  C C     . LYS   A 1 93  ? -24.314 -46.616  -20.225 1.00 25.52  ? 85  LYS   A C     1 
ATOM   571  O O     . LYS   A 1 93  ? -24.622 -45.475  -19.887 1.00 24.52  ? 85  LYS   A O     1 
ATOM   572  C CB    . LYS   A 1 93  ? -26.414 -47.524  -21.173 1.00 27.80  ? 85  LYS   A CB    1 
ATOM   573  C CG    . LYS   A 1 93  ? -27.378 -48.682  -21.387 1.00 28.89  ? 85  LYS   A CG    1 
ATOM   574  C CD    . LYS   A 1 93  ? -28.525 -48.348  -22.336 1.00 29.89  ? 85  LYS   A CD    1 
ATOM   575  C CE    . LYS   A 1 93  ? -28.081 -48.042  -23.733 1.00 30.65  ? 85  LYS   A CE    1 
ATOM   576  N NZ    . LYS   A 1 93  ? -29.192 -47.601  -24.581 1.00 31.34  ? 85  LYS   A NZ    1 
ATOM   577  N N     . LEU   A 1 94  ? -23.111 -46.941  -20.713 1.00 24.91  ? 86  LEU   A N     1 
ATOM   578  C CA    . LEU   A 1 94  ? -22.093 -45.928  -20.944 1.00 25.43  ? 86  LEU   A CA    1 
ATOM   579  C C     . LEU   A 1 94  ? -22.622 -44.919  -21.962 1.00 25.66  ? 86  LEU   A C     1 
ATOM   580  O O     . LEU   A 1 94  ? -23.283 -45.293  -22.927 1.00 26.22  ? 86  LEU   A O     1 
ATOM   581  C CB    . LEU   A 1 94  ? -20.786 -46.556  -21.426 1.00 24.84  ? 86  LEU   A CB    1 
ATOM   582  C CG    . LEU   A 1 94  ? -19.591 -45.602  -21.523 1.00 24.47  ? 86  LEU   A CG    1 
ATOM   583  C CD1   . LEU   A 1 94  ? -19.034 -45.305  -20.142 1.00 24.43  ? 86  LEU   A CD1   1 
ATOM   584  C CD2   . LEU   A 1 94  ? -18.510 -46.144  -22.436 1.00 24.49  ? 86  LEU   A CD2   1 
ATOM   585  N N     . SER   A 1 95  ? -22.328 -43.635  -21.744 1.00 25.88  ? 87  SER   A N     1 
ATOM   586  C CA    . SER   A 1 95  ? -22.770 -42.607  -22.671 1.00 26.20  ? 87  SER   A CA    1 
ATOM   587  C C     . SER   A 1 95  ? -22.019 -42.759  -23.993 1.00 26.43  ? 87  SER   A C     1 
ATOM   588  O O     . SER   A 1 95  ? -20.808 -42.967  -24.004 1.00 26.59  ? 87  SER   A O     1 
ATOM   589  C CB    . SER   A 1 95  ? -22.631 -41.225  -22.082 1.00 26.24  ? 87  SER   A CB    1 
ATOM   590  O OG    . SER   A 1 95  ? -23.621 -41.010  -21.083 1.00 26.29  ? 87  SER   A OG    1 
ATOM   591  N N     . PRO   A 1 96  ? -22.719 -42.664  -25.148 1.00 26.22  ? 88  PRO   A N     1 
ATOM   592  C CA    . PRO   A 1 96  ? -22.130 -43.010  -26.445 1.00 26.19  ? 88  PRO   A CA    1 
ATOM   593  C C     . PRO   A 1 96  ? -20.980 -42.128  -26.923 1.00 26.01  ? 88  PRO   A C     1 
ATOM   594  O O     . PRO   A 1 96  ? -20.235 -42.530  -27.813 1.00 25.60  ? 88  PRO   A O     1 
ATOM   595  C CB    . PRO   A 1 96  ? -23.333 -42.934  -27.401 1.00 26.09  ? 88  PRO   A CB    1 
ATOM   596  C CG    . PRO   A 1 96  ? -24.274 -41.949  -26.741 1.00 26.36  ? 88  PRO   A CG    1 
ATOM   597  C CD    . PRO   A 1 96  ? -24.118 -42.218  -25.258 1.00 26.26  ? 88  PRO   A CD    1 
ATOM   598  N N     . TRP   A 1 97  ? -20.837 -40.938  -26.326 1.00 26.18  ? 89  TRP   A N     1 
ATOM   599  C CA    . TRP   A 1 97  ? -19.807 -39.993  -26.729 1.00 26.38  ? 89  TRP   A CA    1 
ATOM   600  C C     . TRP   A 1 97  ? -18.454 -40.334  -26.102 1.00 27.55  ? 89  TRP   A C     1 
ATOM   601  O O     . TRP   A 1 97  ? -17.438 -39.768  -26.499 1.00 28.15  ? 89  TRP   A O     1 
ATOM   602  C CB    . TRP   A 1 97  ? -20.226 -38.558  -26.376 1.00 25.73  ? 89  TRP   A CB    1 
ATOM   603  C CG    . TRP   A 1 97  ? -20.449 -38.312  -24.906 1.00 25.32  ? 89  TRP   A CG    1 
ATOM   604  C CD1   . TRP   A 1 97  ? -21.629 -38.411  -24.228 1.00 24.94  ? 89  TRP   A CD1   1 
ATOM   605  C CD2   . TRP   A 1 97  ? -19.460 -37.912  -23.931 1.00 24.83  ? 89  TRP   A CD2   1 
ATOM   606  N NE1   . TRP   A 1 97  ? -21.448 -38.104  -22.906 1.00 25.09  ? 89  TRP   A NE1   1 
ATOM   607  C CE2   . TRP   A 1 97  ? -20.129 -37.797  -22.692 1.00 24.94  ? 89  TRP   A CE2   1 
ATOM   608  C CE3   . TRP   A 1 97  ? -18.086 -37.650  -23.983 1.00 24.41  ? 89  TRP   A CE3   1 
ATOM   609  C CZ2   . TRP   A 1 97  ? -19.467 -37.428  -21.522 1.00 24.62  ? 89  TRP   A CZ2   1 
ATOM   610  C CZ3   . TRP   A 1 97  ? -17.435 -37.285  -22.825 1.00 24.43  ? 89  TRP   A CZ3   1 
ATOM   611  C CH2   . TRP   A 1 97  ? -18.117 -37.175  -21.613 1.00 24.34  ? 89  TRP   A CH2   1 
ATOM   612  N N     . ILE   A 1 98  ? -18.446 -41.251  -25.124 1.00 27.88  ? 90  ILE   A N     1 
ATOM   613  C CA    . ILE   A 1 98  ? -17.241 -41.590  -24.383 1.00 28.10  ? 90  ILE   A CA    1 
ATOM   614  C C     . ILE   A 1 98  ? -16.386 -42.531  -25.230 1.00 28.21  ? 90  ILE   A C     1 
ATOM   615  O O     . ILE   A 1 98  ? -16.800 -43.651  -25.520 1.00 27.94  ? 90  ILE   A O     1 
ATOM   616  C CB    . ILE   A 1 98  ? -17.623 -42.199  -23.021 1.00 29.02  ? 90  ILE   A CB    1 
ATOM   617  C CG1   . ILE   A 1 98  ? -18.433 -41.200  -22.184 1.00 28.90  ? 90  ILE   A CG1   1 
ATOM   618  C CG2   . ILE   A 1 98  ? -16.391 -42.698  -22.263 1.00 29.76  ? 90  ILE   A CG2   1 
ATOM   619  C CD1   . ILE   A 1 98  ? -19.193 -41.822  -21.030 1.00 28.63  ? 90  ILE   A CD1   1 
ATOM   620  N N     . ARG   A 1 99  ? -15.198 -42.058  -25.629 1.00 28.52  ? 91  ARG   A N     1 
ATOM   621  C CA    . ARG   A 1 99  ? -14.332 -42.783  -26.548 1.00 29.38  ? 91  ARG   A CA    1 
ATOM   622  C C     . ARG   A 1 99  ? -12.917 -42.859  -25.976 1.00 27.69  ? 91  ARG   A C     1 
ATOM   623  O O     . ARG   A 1 99  ? -12.055 -42.051  -26.317 1.00 26.13  ? 91  ARG   A O     1 
ATOM   624  C CB    . ARG   A 1 99  ? -14.384 -42.110  -27.925 1.00 31.24  ? 91  ARG   A CB    1 
ATOM   625  C CG    . ARG   A 1 99  ? -15.757 -42.173  -28.582 1.00 33.58  ? 91  ARG   A CG    1 
ATOM   626  C CD    . ARG   A 1 99  ? -15.916 -41.123  -29.680 1.00 36.40  ? 91  ARG   A CD    1 
ATOM   627  N NE    . ARG   A 1 99  ? -14.930 -41.308  -30.753 1.00 38.09  ? 91  ARG   A NE    1 
ATOM   628  C CZ    . ARG   A 1 99  ? -14.929 -42.292  -31.652 1.00 38.47  ? 91  ARG   A CZ    1 
ATOM   629  N NH1   . ARG   A 1 99  ? -15.987 -43.072  -31.807 1.00 38.52  ? 91  ARG   A NH1   1 
ATOM   630  N NH2   . ARG   A 1 99  ? -13.871 -42.465  -32.426 1.00 38.57  ? 91  ARG   A NH2   1 
ATOM   631  N N     . PRO   A 1 100 ? -12.639 -43.842  -25.088 1.00 27.58  ? 92  PRO   A N     1 
ATOM   632  C CA    . PRO   A 1 100 ? -11.322 -43.984  -24.459 1.00 27.80  ? 92  PRO   A CA    1 
ATOM   633  C C     . PRO   A 1 100 ? -10.140 -44.290  -25.375 1.00 28.10  ? 92  PRO   A C     1 
ATOM   634  O O     . PRO   A 1 100 ? -8.996  -44.128  -24.961 1.00 27.86  ? 92  PRO   A O     1 
ATOM   635  C CB    . PRO   A 1 100 ? -11.563 -45.143  -23.473 1.00 28.08  ? 92  PRO   A CB    1 
ATOM   636  C CG    . PRO   A 1 100 ? -13.047 -45.106  -23.216 1.00 27.85  ? 92  PRO   A CG    1 
ATOM   637  C CD    . PRO   A 1 100 ? -13.605 -44.834  -24.591 1.00 27.67  ? 92  PRO   A CD    1 
ATOM   638  N N     . ASP   A 1 101 ? -10.420 -44.759  -26.596 1.00 29.44  ? 93  ASP   A N     1 
ATOM   639  C CA    . ASP   A 1 101 ? -9.382  -45.141  -27.541 1.00 30.27  ? 93  ASP   A CA    1 
ATOM   640  C C     . ASP   A 1 101 ? -9.390  -44.210  -28.752 1.00 30.70  ? 93  ASP   A C     1 
ATOM   641  O O     . ASP   A 1 101 ? -8.841  -44.554  -29.796 1.00 31.13  ? 93  ASP   A O     1 
ATOM   642  C CB    . ASP   A 1 101 ? -9.522  -46.604  -27.928 1.00 30.34  ? 93  ASP   A CB    1 
ATOM   643  C CG    . ASP   A 1 101 ? -9.174  -47.576  -26.813 1.00 30.13  ? 93  ASP   A CG    1 
ATOM   644  O OD1   . ASP   A 1 101 ? -7.965  -47.766  -26.562 1.00 30.02  ? 93  ASP   A OD1   1 
ATOM   645  O OD2   . ASP   A 1 101 ? -10.114 -48.094  -26.180 1.00 29.95  ? 93  ASP   A OD2   1 
ATOM   646  N N     . SER   A 1 102 ? -9.996  -43.028  -28.592 1.00 31.25  ? 94  SER   A N     1 
ATOM   647  C CA    . SER   A 1 102 ? -9.933  -41.974  -29.591 1.00 31.81  ? 94  SER   A CA    1 
ATOM   648  C C     . SER   A 1 102 ? -8.486  -41.714  -30.004 1.00 31.96  ? 94  SER   A C     1 
ATOM   649  O O     . SER   A 1 102 ? -7.572  -41.812  -29.191 1.00 31.15  ? 94  SER   A O     1 
ATOM   650  C CB    . SER   A 1 102 ? -10.584 -40.709  -29.080 1.00 32.42  ? 94  SER   A CB    1 
ATOM   651  O OG    . SER   A 1 102 ? -10.241 -39.584  -29.879 1.00 32.66  ? 94  SER   A OG    1 
ATOM   652  N N     . LYS   A 1 103 ? -8.306  -41.367  -31.282 1.00 32.70  ? 95  LYS   A N     1 
ATOM   653  C CA    . LYS   A 1 103 ? -7.009  -41.018  -31.835 1.00 33.70  ? 95  LYS   A CA    1 
ATOM   654  C C     . LYS   A 1 103 ? -6.578  -39.630  -31.364 1.00 33.07  ? 95  LYS   A C     1 
ATOM   655  O O     . LYS   A 1 103 ? -5.409  -39.275  -31.486 1.00 32.76  ? 95  LYS   A O     1 
ATOM   656  C CB    . LYS   A 1 103 ? -7.106  -41.045  -33.363 1.00 35.18  ? 95  LYS   A CB    1 
ATOM   657  C CG    . LYS   A 1 103 ? -7.351  -42.413  -33.982 1.00 36.70  ? 95  LYS   A CG    1 
ATOM   658  C CD    . LYS   A 1 103 ? -6.076  -43.133  -34.405 1.00 38.39  ? 95  LYS   A CD    1 
ATOM   659  C CE    . LYS   A 1 103 ? -6.335  -44.470  -35.029 1.00 40.11  ? 95  LYS   A CE    1 
ATOM   660  N NZ    . LYS   A 1 103 ? -7.180  -44.385  -36.225 1.00 41.30  ? 95  LYS   A NZ    1 
ATOM   661  N N     . VAL   A 1 104 ? -7.535  -38.845  -30.851 1.00 33.26  ? 96  VAL   A N     1 
ATOM   662  C CA    . VAL   A 1 104 ? -7.265  -37.507  -30.352 1.00 33.58  ? 96  VAL   A CA    1 
ATOM   663  C C     . VAL   A 1 104 ? -6.990  -37.591  -28.854 1.00 33.57  ? 96  VAL   A C     1 
ATOM   664  O O     . VAL   A 1 104 ? -7.867  -37.978  -28.084 1.00 33.47  ? 96  VAL   A O     1 
ATOM   665  C CB    . VAL   A 1 104 ? -8.434  -36.546  -30.644 1.00 33.96  ? 96  VAL   A CB    1 
ATOM   666  C CG1   . VAL   A 1 104 ? -8.109  -35.115  -30.235 1.00 34.14  ? 96  VAL   A CG1   1 
ATOM   667  C CG2   . VAL   A 1 104 ? -8.859  -36.587  -32.106 1.00 33.96  ? 96  VAL   A CG2   1 
ATOM   668  N N     . GLU   A 1 105 ? -5.776  -37.189  -28.458 1.00 33.90  ? 97  GLU   A N     1 
ATOM   669  C CA    . GLU   A 1 105 ? -5.314  -37.298  -27.083 1.00 35.30  ? 97  GLU   A CA    1 
ATOM   670  C C     . GLU   A 1 105 ? -6.311  -36.633  -26.137 1.00 36.10  ? 97  GLU   A C     1 
ATOM   671  O O     . GLU   A 1 105 ? -6.692  -37.222  -25.126 1.00 35.63  ? 97  GLU   A O     1 
ATOM   672  C CB    . GLU   A 1 105 ? -3.924  -36.671  -26.976 1.00 35.90  ? 97  GLU   A CB    1 
ATOM   673  C CG    . GLU   A 1 105 ? -3.289  -36.806  -25.595 1.00 36.14  ? 97  GLU   A CG    1 
ATOM   674  C CD    . GLU   A 1 105 ? -1.843  -36.341  -25.533 1.00 37.21  ? 97  GLU   A CD    1 
ATOM   675  O OE1   . GLU   A 1 105 ? -1.280  -35.963  -26.584 1.00 37.91  ? 97  GLU   A OE1   1 
ATOM   676  O OE2   . GLU   A 1 105 ? -1.274  -36.352  -24.422 1.00 37.58  ? 97  GLU   A OE2   1 
ATOM   677  N N     . LYS   A 1 106 ? -6.713  -35.402  -26.479 1.00 36.98  ? 98  LYS   A N     1 
ATOM   678  C CA    . LYS   A 1 106 ? -7.686  -34.637  -25.715 1.00 37.65  ? 98  LYS   A CA    1 
ATOM   679  C C     . LYS   A 1 106 ? -8.900  -35.496  -25.374 1.00 35.48  ? 98  LYS   A C     1 
ATOM   680  O O     . LYS   A 1 106 ? -9.269  -35.616  -24.209 1.00 35.09  ? 98  LYS   A O     1 
ATOM   681  C CB    . LYS   A 1 106 ? -8.190  -33.432  -26.519 1.00 41.26  ? 98  LYS   A CB    1 
ATOM   682  C CG    . LYS   A 1 106 ? -7.188  -32.316  -26.778 1.00 43.68  ? 98  LYS   A CG    1 
ATOM   683  C CD    . LYS   A 1 106 ? -7.677  -31.322  -27.826 1.00 45.66  ? 98  LYS   A CD    1 
ATOM   684  C CE    . LYS   A 1 106 ? -6.807  -30.109  -27.934 1.00 47.43  ? 98  LYS   A CE    1 
ATOM   685  N NZ    . LYS   A 1 106 ? -6.977  -29.204  -26.794 1.00 47.90  ? 98  LYS   A NZ    1 
ATOM   686  N N     . ILE   A 1 107 ? -9.515  -36.077  -26.408 1.00 33.82  ? 99  ILE   A N     1 
ATOM   687  C CA    . ILE   A 1 107 ? -10.754 -36.826  -26.260 1.00 33.70  ? 99  ILE   A CA    1 
ATOM   688  C C     . ILE   A 1 107 ? -10.502 -38.079  -25.422 1.00 33.54  ? 99  ILE   A C     1 
ATOM   689  O O     . ILE   A 1 107 ? -11.339 -38.469  -24.612 1.00 33.58  ? 99  ILE   A O     1 
ATOM   690  C CB    . ILE   A 1 107 ? -11.337 -37.177  -27.642 1.00 33.47  ? 99  ILE   A CB    1 
ATOM   691  C CG1   . ILE   A 1 107 ? -11.722 -35.915  -28.425 1.00 33.47  ? 99  ILE   A CG1   1 
ATOM   692  C CG2   . ILE   A 1 107 ? -12.517 -38.143  -27.510 1.00 33.45  ? 99  ILE   A CG2   1 
ATOM   693  C CD1   . ILE   A 1 107 ? -12.057 -36.161  -29.885 1.00 33.22  ? 99  ILE   A CD1   1 
ATOM   694  N N     A ARG   A 1 108 ? -9.337  -38.697  -25.646 0.60 33.05  ? 100 ARG   A N     1 
ATOM   695  N N     B ARG   A 1 108 ? -9.352  -38.717  -25.654 0.40 33.72  ? 100 ARG   A N     1 
ATOM   696  C CA    A ARG   A 1 108 ? -8.921  -39.898  -24.944 0.60 32.26  ? 100 ARG   A CA    1 
ATOM   697  C CA    B ARG   A 1 108 ? -8.955  -39.911  -24.931 0.40 33.52  ? 100 ARG   A CA    1 
ATOM   698  C C     A ARG   A 1 108 ? -8.907  -39.617  -23.443 0.60 33.25  ? 100 ARG   A C     1 
ATOM   699  C C     B ARG   A 1 108 ? -8.908  -39.620  -23.433 0.40 33.92  ? 100 ARG   A C     1 
ATOM   700  O O     A ARG   A 1 108 ? -9.579  -40.302  -22.676 0.60 33.10  ? 100 ARG   A O     1 
ATOM   701  O O     B ARG   A 1 108 ? -9.558  -40.309  -22.651 0.40 33.77  ? 100 ARG   A O     1 
ATOM   702  C CB    A ARG   A 1 108 ? -7.547  -40.298  -25.497 0.60 31.41  ? 100 ARG   A CB    1 
ATOM   703  C CB    B ARG   A 1 108 ? -7.627  -40.343  -25.560 0.40 33.52  ? 100 ARG   A CB    1 
ATOM   704  C CG    A ARG   A 1 108 ? -7.243  -41.787  -25.549 0.60 30.59  ? 100 ARG   A CG    1 
ATOM   705  C CG    B ARG   A 1 108 ? -6.784  -41.348  -24.793 0.40 33.43  ? 100 ARG   A CG    1 
ATOM   706  C CD    A ARG   A 1 108 ? -6.226  -42.077  -26.640 0.60 29.66  ? 100 ARG   A CD    1 
ATOM   707  C CD    B ARG   A 1 108 ? -5.555  -41.667  -25.626 0.40 33.63  ? 100 ARG   A CD    1 
ATOM   708  N NE    A ARG   A 1 108 ? -4.998  -41.283  -26.513 0.60 28.75  ? 100 ARG   A NE    1 
ATOM   709  N NE    B ARG   A 1 108 ? -4.428  -40.784  -25.311 0.40 33.57  ? 100 ARG   A NE    1 
ATOM   710  C CZ    A ARG   A 1 108 ? -4.207  -40.900  -27.511 0.60 27.37  ? 100 ARG   A CZ    1 
ATOM   711  C CZ    B ARG   A 1 108 ? -3.877  -40.773  -24.112 0.40 33.45  ? 100 ARG   A CZ    1 
ATOM   712  N NH1   A ARG   A 1 108 ? -4.586  -41.041  -28.768 0.60 27.36  ? 100 ARG   A NH1   1 
ATOM   713  N NH1   B ARG   A 1 108 ? -4.400  -41.553  -23.186 0.40 34.08  ? 100 ARG   A NH1   1 
ATOM   714  N NH2   A ARG   A 1 108 ? -3.046  -40.331  -27.245 0.60 26.93  ? 100 ARG   A NH2   1 
ATOM   715  N NH2   B ARG   A 1 108 ? -2.836  -40.003  -23.848 0.40 33.16  ? 100 ARG   A NH2   1 
ATOM   716  N N     . ARG   A 1 109 ? -8.159  -38.578  -23.049 1.00 34.16  ? 101 ARG   A N     1 
ATOM   717  C CA    . ARG   A 1 109 ? -8.045  -38.164  -21.657 1.00 35.18  ? 101 ARG   A CA    1 
ATOM   718  C C     . ARG   A 1 109 ? -9.407  -37.841  -21.047 1.00 32.98  ? 101 ARG   A C     1 
ATOM   719  O O     . ARG   A 1 109 ? -9.674  -38.195  -19.903 1.00 31.94  ? 101 ARG   A O     1 
ATOM   720  C CB    . ARG   A 1 109 ? -7.191  -36.901  -21.503 1.00 37.44  ? 101 ARG   A CB    1 
ATOM   721  C CG    . ARG   A 1 109 ? -5.692  -37.152  -21.507 1.00 40.07  ? 101 ARG   A CG    1 
ATOM   722  C CD    . ARG   A 1 109 ? -4.965  -36.076  -20.716 1.00 42.92  ? 101 ARG   A CD    1 
ATOM   723  N NE    . ARG   A 1 109 ? -3.632  -36.510  -20.284 1.00 45.38  ? 101 ARG   A NE    1 
ATOM   724  C CZ    . ARG   A 1 109 ? -2.593  -36.746  -21.078 1.00 46.34  ? 101 ARG   A CZ    1 
ATOM   725  N NH1   . ARG   A 1 109 ? -2.694  -36.574  -22.384 1.00 45.96  ? 101 ARG   A NH1   1 
ATOM   726  N NH2   . ARG   A 1 109 ? -1.445  -37.149  -20.560 1.00 47.48  ? 101 ARG   A NH2   1 
ATOM   727  N N     . ASN   A 1 110 ? -10.249 -37.145  -21.811 1.00 32.13  ? 102 ASN   A N     1 
ATOM   728  C CA    . ASN   A 1 110 ? -11.533 -36.691  -21.309 1.00 32.18  ? 102 ASN   A CA    1 
ATOM   729  C C     . ASN   A 1 110 ? -12.449 -37.891  -21.085 1.00 31.88  ? 102 ASN   A C     1 
ATOM   730  O O     . ASN   A 1 110 ? -13.122 -37.979  -20.059 1.00 32.40  ? 102 ASN   A O     1 
ATOM   731  C CB    . ASN   A 1 110 ? -12.176 -35.682  -22.251 1.00 32.15  ? 102 ASN   A CB    1 
ATOM   732  C CG    . ASN   A 1 110 ? -13.188 -34.825  -21.531 1.00 32.34  ? 102 ASN   A CG    1 
ATOM   733  O OD1   . ASN   A 1 110 ? -12.805 -33.956  -20.737 1.00 31.94  ? 102 ASN   A OD1   1 
ATOM   734  N ND2   . ASN   A 1 110 ? -14.469 -35.055  -21.781 1.00 32.22  ? 102 ASN   A ND2   1 
ATOM   735  N N     . SER   A 1 111 ? -12.454 -38.807  -22.061 1.00 30.99  ? 103 SER   A N     1 
ATOM   736  C CA    . SER   A 1 111 ? -13.303 -39.987  -22.033 1.00 30.34  ? 103 SER   A CA    1 
ATOM   737  C C     . SER   A 1 111 ? -12.903 -40.915  -20.887 1.00 29.86  ? 103 SER   A C     1 
ATOM   738  O O     . SER   A 1 111 ? -13.762 -41.543  -20.273 1.00 29.79  ? 103 SER   A O     1 
ATOM   739  C CB    . SER   A 1 111 ? -13.253 -40.707  -23.352 1.00 30.00  ? 103 SER   A CB    1 
ATOM   740  O OG    . SER   A 1 111 ? -13.636 -39.851  -24.420 1.00 29.80  ? 103 SER   A OG    1 
ATOM   741  N N     . GLU   A 1 112 ? -11.594 -41.004  -20.619 1.00 29.57  ? 104 GLU   A N     1 
ATOM   742  C CA    . GLU   A 1 112 ? -11.090 -41.750  -19.478 1.00 29.53  ? 104 GLU   A CA    1 
ATOM   743  C C     . GLU   A 1 112 ? -11.835 -41.310  -18.222 1.00 29.32  ? 104 GLU   A C     1 
ATOM   744  O O     . GLU   A 1 112 ? -12.460 -42.132  -17.555 1.00 29.69  ? 104 GLU   A O     1 
ATOM   745  C CB    . GLU   A 1 112 ? -9.583  -41.549  -19.306 1.00 30.06  ? 104 GLU   A CB    1 
ATOM   746  C CG    . GLU   A 1 112 ? -8.743  -42.339  -20.305 1.00 30.35  ? 104 GLU   A CG    1 
ATOM   747  C CD    . GLU   A 1 112 ? -7.264  -41.995  -20.308 1.00 30.99  ? 104 GLU   A CD    1 
ATOM   748  O OE1   . GLU   A 1 112 ? -6.779  -41.374  -19.336 1.00 31.02  ? 104 GLU   A OE1   1 
ATOM   749  O OE2   . GLU   A 1 112 ? -6.595  -42.348  -21.305 1.00 31.11  ? 104 GLU   A OE2   1 
ATOM   750  N N     . ALA   A 1 113 ? -11.769 -40.004  -17.928 1.00 28.84  ? 105 ALA   A N     1 
ATOM   751  C CA    . ALA   A 1 113 ? -12.373 -39.428  -16.736 1.00 27.99  ? 105 ALA   A CA    1 
ATOM   752  C C     . ALA   A 1 113 ? -13.886 -39.637  -16.729 1.00 28.32  ? 105 ALA   A C     1 
ATOM   753  O O     . ALA   A 1 113 ? -14.463 -39.904  -15.676 1.00 29.24  ? 105 ALA   A O     1 
ATOM   754  C CB    . ALA   A 1 113 ? -12.032 -37.958  -16.650 1.00 27.57  ? 105 ALA   A CB    1 
ATOM   755  N N     . ALA   A 1 114 ? -14.517 -39.502  -17.904 1.00 27.86  ? 106 ALA   A N     1 
ATOM   756  C CA    . ALA   A 1 114 ? -15.961 -39.630  -18.041 1.00 27.57  ? 106 ALA   A CA    1 
ATOM   757  C C     . ALA   A 1 114 ? -16.413 -41.062  -17.752 1.00 27.31  ? 106 ALA   A C     1 
ATOM   758  O O     . ALA   A 1 114 ? -17.434 -41.277  -17.101 1.00 26.33  ? 106 ALA   A O     1 
ATOM   759  C CB    . ALA   A 1 114 ? -16.382 -39.201  -19.430 1.00 27.74  ? 106 ALA   A CB    1 
ATOM   760  N N     . MET   A 1 115 ? -15.650 -42.033  -18.263 1.00 27.56  ? 107 MET   A N     1 
ATOM   761  C CA    . MET   A 1 115 ? -15.962 -43.445  -18.101 1.00 27.43  ? 107 MET   A CA    1 
ATOM   762  C C     . MET   A 1 115 ? -15.902 -43.831  -16.625 1.00 27.77  ? 107 MET   A C     1 
ATOM   763  O O     . MET   A 1 115 ? -16.829 -44.452  -16.105 1.00 26.93  ? 107 MET   A O     1 
ATOM   764  C CB    . MET   A 1 115 ? -14.975 -44.295  -18.906 1.00 27.10  ? 107 MET   A CB    1 
ATOM   765  C CG    . MET   A 1 115 ? -15.108 -45.782  -18.689 1.00 26.82  ? 107 MET   A CG    1 
ATOM   766  S SD    . MET   A 1 115 ? -14.013 -46.715  -19.775 1.00 25.80  ? 107 MET   A SD    1 
ATOM   767  C CE    . MET   A 1 115 ? -14.343 -48.330  -19.060 1.00 26.05  ? 107 MET   A CE    1 
ATOM   768  N N     . LEU   A 1 116 ? -14.794 -43.467  -15.965 1.00 28.60  ? 108 LEU   A N     1 
ATOM   769  C CA    . LEU   A 1 116 ? -14.640 -43.678  -14.534 1.00 29.61  ? 108 LEU   A CA    1 
ATOM   770  C C     . LEU   A 1 116 ? -15.840 -43.097  -13.794 1.00 29.39  ? 108 LEU   A C     1 
ATOM   771  O O     . LEU   A 1 116 ? -16.401 -43.745  -12.912 1.00 30.03  ? 108 LEU   A O     1 
ATOM   772  C CB    . LEU   A 1 116 ? -13.332 -43.061  -14.037 1.00 30.83  ? 108 LEU   A CB    1 
ATOM   773  C CG    . LEU   A 1 116 ? -12.076 -43.919  -14.219 1.00 32.75  ? 108 LEU   A CG    1 
ATOM   774  C CD1   . LEU   A 1 116 ? -10.819 -43.138  -13.876 1.00 33.40  ? 108 LEU   A CD1   1 
ATOM   775  C CD2   . LEU   A 1 116 ? -12.157 -45.186  -13.376 1.00 33.61  ? 108 LEU   A CD2   1 
ATOM   776  N N     . GLN   A 1 117 ? -16.222 -41.872  -14.172 1.00 28.56  ? 109 GLN   A N     1 
ATOM   777  C CA    . GLN   A 1 117 ? -17.313 -41.163  -13.528 1.00 28.50  ? 109 GLN   A CA    1 
ATOM   778  C C     . GLN   A 1 117 ? -18.602 -41.973  -13.639 1.00 28.23  ? 109 GLN   A C     1 
ATOM   779  O O     . GLN   A 1 117 ? -19.252 -42.230  -12.630 1.00 29.75  ? 109 GLN   A O     1 
ATOM   780  C CB    . GLN   A 1 117 ? -17.448 -39.779  -14.161 1.00 28.91  ? 109 GLN   A CB    1 
ATOM   781  C CG    . GLN   A 1 117 ? -18.569 -38.925  -13.582 1.00 28.97  ? 109 GLN   A CG    1 
ATOM   782  C CD    . GLN   A 1 117 ? -18.798 -37.660  -14.378 1.00 29.00  ? 109 GLN   A CD    1 
ATOM   783  O OE1   . GLN   A 1 117 ? -19.285 -37.696  -15.513 1.00 28.75  ? 109 GLN   A OE1   1 
ATOM   784  N NE2   . GLN   A 1 117 ? -18.439 -36.527  -13.795 1.00 29.16  ? 109 GLN   A NE2   1 
ATOM   785  N N     . GLU   A 1 118 ? -18.960 -42.369  -14.865 1.00 27.58  ? 110 GLU   A N     1 
ATOM   786  C CA    . GLU   A 1 118 ? -20.221 -43.052  -15.109 1.00 27.39  ? 110 GLU   A CA    1 
ATOM   787  C C     . GLU   A 1 118 ? -20.224 -44.410  -14.409 1.00 27.56  ? 110 GLU   A C     1 
ATOM   788  O O     . GLU   A 1 118 ? -21.252 -44.825  -13.878 1.00 27.97  ? 110 GLU   A O     1 
ATOM   789  C CB    . GLU   A 1 118 ? -20.510 -43.220  -16.602 1.00 27.41  ? 110 GLU   A CB    1 
ATOM   790  C CG    . GLU   A 1 118 ? -20.650 -41.893  -17.343 1.00 27.02  ? 110 GLU   A CG    1 
ATOM   791  C CD    . GLU   A 1 118 ? -21.517 -41.918  -18.591 1.00 26.95  ? 110 GLU   A CD    1 
ATOM   792  O OE1   . GLU   A 1 118 ? -21.804 -43.010  -19.131 1.00 27.16  ? 110 GLU   A OE1   1 
ATOM   793  O OE2   . GLU   A 1 118 ? -21.922 -40.814  -19.014 1.00 25.74  ? 110 GLU   A OE2   1 
ATOM   794  N N     . LEU   A 1 119 ? -19.071 -45.094  -14.422 1.00 27.42  ? 111 LEU   A N     1 
ATOM   795  C CA    . LEU   A 1 119 ? -18.940 -46.400  -13.795 1.00 26.80  ? 111 LEU   A CA    1 
ATOM   796  C C     . LEU   A 1 119 ? -19.153 -46.284  -12.287 1.00 26.87  ? 111 LEU   A C     1 
ATOM   797  O O     . LEU   A 1 119 ? -19.912 -47.061  -11.712 1.00 26.53  ? 111 LEU   A O     1 
ATOM   798  C CB    . LEU   A 1 119 ? -17.580 -47.020  -14.116 1.00 26.16  ? 111 LEU   A CB    1 
ATOM   799  C CG    . LEU   A 1 119 ? -17.417 -47.603  -15.523 1.00 25.93  ? 111 LEU   A CG    1 
ATOM   800  C CD1   . LEU   A 1 119 ? -15.975 -48.023  -15.739 1.00 25.84  ? 111 LEU   A CD1   1 
ATOM   801  C CD2   . LEU   A 1 119 ? -18.354 -48.776  -15.778 1.00 25.71  ? 111 LEU   A CD2   1 
ATOM   802  N N     . ASN   A 1 120 ? -18.482 -45.310  -11.660 1.00 27.07  ? 112 ASN   A N     1 
ATOM   803  C CA    . ASN   A 1 120 ? -18.572 -45.119  -10.223 1.00 28.05  ? 112 ASN   A CA    1 
ATOM   804  C C     . ASN   A 1 120 ? -20.000 -44.764  -9.819  1.00 28.90  ? 112 ASN   A C     1 
ATOM   805  O O     . ASN   A 1 120 ? -20.454 -45.178  -8.754  1.00 29.81  ? 112 ASN   A O     1 
ATOM   806  C CB    . ASN   A 1 120 ? -17.581 -44.079  -9.717  1.00 27.91  ? 112 ASN   A CB    1 
ATOM   807  C CG    . ASN   A 1 120 ? -16.153 -44.564  -9.799  1.00 28.20  ? 112 ASN   A CG    1 
ATOM   808  O OD1   . ASN   A 1 120 ? -15.896 -45.763  -9.649  1.00 28.75  ? 112 ASN   A OD1   1 
ATOM   809  N ND2   . ASN   A 1 120 ? -15.215 -43.665  -10.056 1.00 28.49  ? 112 ASN   A ND2   1 
ATOM   810  N N     . PHE   A 1 121 ? -20.708 -44.006  -10.666 1.00 28.73  ? 113 PHE   A N     1 
ATOM   811  C CA    . PHE   A 1 121 ? -22.090 -43.661  -10.377 1.00 28.52  ? 113 PHE   A CA    1 
ATOM   812  C C     . PHE   A 1 121 ? -22.933 -44.937  -10.400 1.00 28.18  ? 113 PHE   A C     1 
ATOM   813  O O     . PHE   A 1 121 ? -23.733 -45.166  -9.496  1.00 28.41  ? 113 PHE   A O     1 
ATOM   814  C CB    . PHE   A 1 121 ? -22.616 -42.578  -11.323 1.00 28.95  ? 113 PHE   A CB    1 
ATOM   815  C CG    . PHE   A 1 121 ? -23.856 -41.882  -10.778 1.00 29.53  ? 113 PHE   A CG    1 
ATOM   816  C CD1   . PHE   A 1 121 ? -23.771 -41.063  -9.658  1.00 30.12  ? 113 PHE   A CD1   1 
ATOM   817  C CD2   . PHE   A 1 121 ? -25.100 -42.051  -11.376 1.00 30.31  ? 113 PHE   A CD2   1 
ATOM   818  C CE1   . PHE   A 1 121 ? -24.898 -40.437  -9.148  1.00 30.50  ? 113 PHE   A CE1   1 
ATOM   819  C CE2   . PHE   A 1 121 ? -26.223 -41.415  -10.867 1.00 30.41  ? 113 PHE   A CE2   1 
ATOM   820  C CZ    . PHE   A 1 121 ? -26.120 -40.610  -9.756  1.00 30.75  ? 113 PHE   A CZ    1 
ATOM   821  N N     . GLY   A 1 122 ? -22.732 -45.778  -11.421 1.00 27.11  ? 114 GLY   A N     1 
ATOM   822  C CA    . GLY   A 1 122 ? -23.369 -47.084  -11.468 1.00 27.01  ? 114 GLY   A CA    1 
ATOM   823  C C     . GLY   A 1 122 ? -23.145 -47.860  -10.170 1.00 27.31  ? 114 GLY   A C     1 
ATOM   824  O O     . GLY   A 1 122 ? -24.080 -48.429  -9.610  1.00 27.03  ? 114 GLY   A O     1 
ATOM   825  N N     . ALA   A 1 123 ? -21.893 -47.866  -9.697  1.00 27.23  ? 115 ALA   A N     1 
ATOM   826  C CA    . ALA   A 1 123 ? -21.530 -48.579  -8.482  1.00 27.46  ? 115 ALA   A CA    1 
ATOM   827  C C     . ALA   A 1 123 ? -22.230 -47.949  -7.279  1.00 27.17  ? 115 ALA   A C     1 
ATOM   828  O O     . ALA   A 1 123 ? -22.775 -48.657  -6.437  1.00 27.23  ? 115 ALA   A O     1 
ATOM   829  C CB    . ALA   A 1 123 ? -20.026 -48.582  -8.312  1.00 27.54  ? 115 ALA   A CB    1 
ATOM   830  N N     . TYR   A 1 124 ? -22.224 -46.613  -7.231  1.00 27.42  ? 116 TYR   A N     1 
ATOM   831  C CA    . TYR   A 1 124 ? -22.889 -45.855  -6.184  1.00 28.23  ? 116 TYR   A CA    1 
ATOM   832  C C     . TYR   A 1 124 ? -24.364 -46.240  -6.070  1.00 27.53  ? 116 TYR   A C     1 
ATOM   833  O O     . TYR   A 1 124 ? -24.879 -46.371  -4.961  1.00 27.57  ? 116 TYR   A O     1 
ATOM   834  C CB    . TYR   A 1 124 ? -22.717 -44.365  -6.487  1.00 29.16  ? 116 TYR   A CB    1 
ATOM   835  C CG    . TYR   A 1 124 ? -23.542 -43.442  -5.604  1.00 29.99  ? 116 TYR   A CG    1 
ATOM   836  C CD1   . TYR   A 1 124 ? -23.201 -43.230  -4.276  1.00 30.43  ? 116 TYR   A CD1   1 
ATOM   837  C CD2   . TYR   A 1 124 ? -24.638 -42.752  -6.109  1.00 30.78  ? 116 TYR   A CD2   1 
ATOM   838  C CE1   . TYR   A 1 124 ? -23.936 -42.378  -3.467  1.00 30.94  ? 116 TYR   A CE1   1 
ATOM   839  C CE2   . TYR   A 1 124 ? -25.375 -41.888  -5.316  1.00 31.37  ? 116 TYR   A CE2   1 
ATOM   840  C CZ    . TYR   A 1 124 ? -25.027 -41.704  -3.990  1.00 31.52  ? 116 TYR   A CZ    1 
ATOM   841  O OH    . TYR   A 1 124 ? -25.761 -40.854  -3.214  1.00 31.93  ? 116 TYR   A OH    1 
ATOM   842  N N     . LEU   A 1 125 ? -25.035 -46.402  -7.218  1.00 26.68  ? 117 LEU   A N     1 
ATOM   843  C CA    . LEU   A 1 125 ? -26.452 -46.734  -7.260  1.00 26.08  ? 117 LEU   A CA    1 
ATOM   844  C C     . LEU   A 1 125 ? -26.658 -48.211  -6.942  1.00 25.20  ? 117 LEU   A C     1 
ATOM   845  O O     . LEU   A 1 125 ? -27.765 -48.610  -6.601  1.00 25.63  ? 117 LEU   A O     1 
ATOM   846  C CB    . LEU   A 1 125 ? -27.064 -46.419  -8.626  1.00 26.86  ? 117 LEU   A CB    1 
ATOM   847  C CG    . LEU   A 1 125 ? -27.070 -44.955  -9.076  1.00 27.09  ? 117 LEU   A CG    1 
ATOM   848  C CD1   . LEU   A 1 125 ? -27.754 -44.858  -10.426 1.00 27.63  ? 117 LEU   A CD1   1 
ATOM   849  C CD2   . LEU   A 1 125 ? -27.741 -44.031  -8.080  1.00 27.54  ? 117 LEU   A CD2   1 
ATOM   850  N N     . GLY   A 1 126 ? -25.612 -49.024  -7.124  1.00 25.12  ? 118 GLY   A N     1 
ATOM   851  C CA    . GLY   A 1 126 ? -25.684 -50.450  -6.852  1.00 25.31  ? 118 GLY   A CA    1 
ATOM   852  C C     . GLY   A 1 126 ? -26.368 -51.211  -7.987  1.00 25.72  ? 118 GLY   A C     1 
ATOM   853  O O     . GLY   A 1 126 ? -27.078 -52.181  -7.739  1.00 26.65  ? 118 GLY   A O     1 
ATOM   854  N N     . LEU   A 1 127 ? -26.128 -50.783  -9.233  1.00 25.46  ? 119 LEU   A N     1 
ATOM   855  C CA    . LEU   A 1 127 ? -26.755 -51.403  -10.389 1.00 25.45  ? 119 LEU   A CA    1 
ATOM   856  C C     . LEU   A 1 127 ? -26.198 -52.816  -10.555 1.00 25.07  ? 119 LEU   A C     1 
ATOM   857  O O     . LEU   A 1 127 ? -25.000 -53.036  -10.379 1.00 25.28  ? 119 LEU   A O     1 
ATOM   858  C CB    . LEU   A 1 127 ? -26.530 -50.570  -11.651 1.00 25.78  ? 119 LEU   A CB    1 
ATOM   859  C CG    . LEU   A 1 127 ? -26.921 -49.089  -11.578 1.00 26.24  ? 119 LEU   A CG    1 
ATOM   860  C CD1   . LEU   A 1 127 ? -26.574 -48.387  -12.882 1.00 26.23  ? 119 LEU   A CD1   1 
ATOM   861  C CD2   . LEU   A 1 127 ? -28.393 -48.891  -11.242 1.00 26.47  ? 119 LEU   A CD2   1 
ATOM   862  N N     . PRO   A 1 128 ? -27.045 -53.811  -10.910 1.00 24.25  ? 120 PRO   A N     1 
ATOM   863  C CA    . PRO   A 1 128 ? -26.597 -55.200  -11.039 1.00 24.48  ? 120 PRO   A CA    1 
ATOM   864  C C     . PRO   A 1 128 ? -25.786 -55.501  -12.298 1.00 25.10  ? 120 PRO   A C     1 
ATOM   865  O O     . PRO   A 1 128 ? -25.158 -56.553  -12.388 1.00 25.82  ? 120 PRO   A O     1 
ATOM   866  C CB    . PRO   A 1 128 ? -27.926 -55.973  -11.020 1.00 24.22  ? 120 PRO   A CB    1 
ATOM   867  C CG    . PRO   A 1 128 ? -28.911 -55.026  -11.664 1.00 24.12  ? 120 PRO   A CG    1 
ATOM   868  C CD    . PRO   A 1 128 ? -28.474 -53.645  -11.211 1.00 24.01  ? 120 PRO   A CD    1 
ATOM   869  N N     . ALA   A 1 129 ? -25.824 -54.580  -13.268 1.00 25.65  ? 121 ALA   A N     1 
ATOM   870  C CA    . ALA   A 1 129 ? -25.066 -54.716  -14.502 1.00 25.91  ? 121 ALA   A CA    1 
ATOM   871  C C     . ALA   A 1 129 ? -24.958 -53.359  -15.196 1.00 26.26  ? 121 ALA   A C     1 
ATOM   872  O O     . ALA   A 1 129 ? -25.765 -52.464  -14.954 1.00 26.41  ? 121 ALA   A O     1 
ATOM   873  C CB    . ALA   A 1 129 ? -25.714 -55.750  -15.393 1.00 25.69  ? 121 ALA   A CB    1 
ATOM   874  N N     . PHE   A 1 130 ? -23.944 -53.221  -16.058 1.00 27.13  ? 122 PHE   A N     1 
ATOM   875  C CA    . PHE   A 1 130 ? -23.674 -51.978  -16.765 1.00 27.44  ? 122 PHE   A CA    1 
ATOM   876  C C     . PHE   A 1 130 ? -23.145 -52.325  -18.156 1.00 26.75  ? 122 PHE   A C     1 
ATOM   877  O O     . PHE   A 1 130 ? -22.366 -53.264  -18.304 1.00 26.00  ? 122 PHE   A O     1 
ATOM   878  C CB    . PHE   A 1 130 ? -22.708 -51.158  -15.902 1.00 28.25  ? 122 PHE   A CB    1 
ATOM   879  C CG    . PHE   A 1 130 ? -22.504 -49.708  -16.324 1.00 29.98  ? 122 PHE   A CG    1 
ATOM   880  C CD1   . PHE   A 1 130 ? -21.683 -49.385  -17.402 1.00 30.76  ? 122 PHE   A CD1   1 
ATOM   881  C CD2   . PHE   A 1 130 ? -23.109 -48.666  -15.626 1.00 30.22  ? 122 PHE   A CD2   1 
ATOM   882  C CE1   . PHE   A 1 130 ? -21.488 -48.063  -17.779 1.00 30.68  ? 122 PHE   A CE1   1 
ATOM   883  C CE2   . PHE   A 1 130 ? -22.911 -47.346  -16.009 1.00 30.66  ? 122 PHE   A CE2   1 
ATOM   884  C CZ    . PHE   A 1 130 ? -22.101 -47.046  -17.082 1.00 30.45  ? 122 PHE   A CZ    1 
ATOM   885  N N     . LEU   A 1 131 ? -23.585 -51.567  -19.171 1.00 26.35  ? 123 LEU   A N     1 
ATOM   886  C CA    . LEU   A 1 131 ? -23.309 -51.892  -20.563 1.00 25.83  ? 123 LEU   A CA    1 
ATOM   887  C C     . LEU   A 1 131 ? -22.193 -51.002  -21.097 1.00 25.33  ? 123 LEU   A C     1 
ATOM   888  O O     . LEU   A 1 131 ? -22.235 -49.785  -20.931 1.00 25.11  ? 123 LEU   A O     1 
ATOM   889  C CB    . LEU   A 1 131 ? -24.572 -51.736  -21.408 1.00 25.76  ? 123 LEU   A CB    1 
ATOM   890  C CG    . LEU   A 1 131 ? -25.553 -52.912  -21.366 1.00 26.25  ? 123 LEU   A CG    1 
ATOM   891  C CD1   . LEU   A 1 131 ? -26.983 -52.418  -21.484 1.00 26.86  ? 123 LEU   A CD1   1 
ATOM   892  C CD2   . LEU   A 1 131 ? -25.257 -53.918  -22.465 1.00 26.04  ? 123 LEU   A CD2   1 
ATOM   893  N N     . LEU   A 1 132 ? -21.209 -51.635  -21.747 1.00 24.95  ? 124 LEU   A N     1 
ATOM   894  C CA    . LEU   A 1 132 ? -20.196 -50.925  -22.510 1.00 24.89  ? 124 LEU   A CA    1 
ATOM   895  C C     . LEU   A 1 132 ? -20.092 -51.566  -23.892 1.00 24.53  ? 124 LEU   A C     1 
ATOM   896  O O     . LEU   A 1 132 ? -20.074 -52.788  -24.005 1.00 24.64  ? 124 LEU   A O     1 
ATOM   897  C CB    . LEU   A 1 132 ? -18.844 -50.943  -21.800 1.00 24.95  ? 124 LEU   A CB    1 
ATOM   898  C CG    . LEU   A 1 132 ? -18.829 -50.478  -20.341 1.00 25.18  ? 124 LEU   A CG    1 
ATOM   899  C CD1   . LEU   A 1 132 ? -19.104 -51.623  -19.376 1.00 25.15  ? 124 LEU   A CD1   1 
ATOM   900  C CD2   . LEU   A 1 132 ? -17.505 -49.820  -20.013 1.00 25.21  ? 124 LEU   A CD2   1 
ATOM   901  N N     . PRO   A 1 133 ? -20.024 -50.771  -24.984 1.00 24.57  ? 125 PRO   A N     1 
ATOM   902  C CA    . PRO   A 1 133 ? -19.910 -51.329  -26.335 1.00 24.54  ? 125 PRO   A CA    1 
ATOM   903  C C     . PRO   A 1 133 ? -18.505 -51.700  -26.804 1.00 24.12  ? 125 PRO   A C     1 
ATOM   904  O O     . PRO   A 1 133 ? -17.533 -51.044  -26.444 1.00 23.26  ? 125 PRO   A O     1 
ATOM   905  C CB    . PRO   A 1 133 ? -20.476 -50.157  -27.146 1.00 24.75  ? 125 PRO   A CB    1 
ATOM   906  C CG    . PRO   A 1 133 ? -19.923 -48.946  -26.439 1.00 24.46  ? 125 PRO   A CG    1 
ATOM   907  C CD    . PRO   A 1 133 ? -20.090 -49.301  -24.974 1.00 24.32  ? 125 PRO   A CD    1 
ATOM   908  N N     . LEU   A 1 134 ? -18.421 -52.759  -27.617 1.00 24.69  ? 126 LEU   A N     1 
ATOM   909  C CA    . LEU   A 1 134 ? -17.254 -53.004  -28.450 1.00 25.33  ? 126 LEU   A CA    1 
ATOM   910  C C     . LEU   A 1 134 ? -17.645 -52.724  -29.899 1.00 25.54  ? 126 LEU   A C     1 
ATOM   911  O O     . LEU   A 1 134 ? -18.386 -53.497  -30.502 1.00 25.17  ? 126 LEU   A O     1 
ATOM   912  C CB    . LEU   A 1 134 ? -16.733 -54.429  -28.266 1.00 25.90  ? 126 LEU   A CB    1 
ATOM   913  C CG    . LEU   A 1 134 ? -16.343 -54.828  -26.838 1.00 26.29  ? 126 LEU   A CG    1 
ATOM   914  C CD1   . LEU   A 1 134 ? -15.847 -56.262  -26.818 1.00 26.49  ? 126 LEU   A CD1   1 
ATOM   915  C CD2   . LEU   A 1 134 ? -15.293 -53.901  -26.247 1.00 26.59  ? 126 LEU   A CD2   1 
ATOM   916  N N     . ASN   A 1 135 ? -17.149 -51.597  -30.427 1.00 26.42  ? 127 ASN   A N     1 
ATOM   917  C CA    . ASN   A 1 135 ? -17.569 -51.059  -31.712 1.00 27.16  ? 127 ASN   A CA    1 
ATOM   918  C C     . ASN   A 1 135 ? -16.432 -51.114  -32.727 1.00 28.65  ? 127 ASN   A C     1 
ATOM   919  O O     . ASN   A 1 135 ? -16.636 -50.797  -33.896 1.00 29.37  ? 127 ASN   A O     1 
ATOM   920  C CB    . ASN   A 1 135 ? -18.032 -49.614  -31.568 1.00 26.79  ? 127 ASN   A CB    1 
ATOM   921  C CG    . ASN   A 1 135 ? -19.347 -49.506  -30.837 1.00 27.01  ? 127 ASN   A CG    1 
ATOM   922  O OD1   . ASN   A 1 135 ? -20.150 -50.446  -30.853 1.00 27.64  ? 127 ASN   A OD1   1 
ATOM   923  N ND2   . ASN   A 1 135 ? -19.599 -48.366  -30.213 1.00 27.10  ? 127 ASN   A ND2   1 
ATOM   924  N N     . GLN   A 1 136 ? -15.238 -51.504  -32.277 1.00 29.69  ? 128 GLN   A N     1 
ATOM   925  C CA    . GLN   A 1 136 ? -14.061 -51.490  -33.126 1.00 30.53  ? 128 GLN   A CA    1 
ATOM   926  C C     . GLN   A 1 136 ? -13.072 -52.521  -32.595 1.00 31.11  ? 128 GLN   A C     1 
ATOM   927  O O     . GLN   A 1 136 ? -13.333 -53.173  -31.587 1.00 30.65  ? 128 GLN   A O     1 
ATOM   928  C CB    . GLN   A 1 136 ? -13.481 -50.076  -33.160 1.00 31.05  ? 128 GLN   A CB    1 
ATOM   929  C CG    . GLN   A 1 136 ? -13.153 -49.510  -31.783 1.00 32.32  ? 128 GLN   A CG    1 
ATOM   930  C CD    . GLN   A 1 136 ? -12.387 -48.208  -31.844 1.00 33.68  ? 128 GLN   A CD    1 
ATOM   931  O OE1   . GLN   A 1 136 ? -11.248 -48.106  -31.375 1.00 34.37  ? 128 GLN   A OE1   1 
ATOM   932  N NE2   . GLN   A 1 136 ? -13.005 -47.192  -32.427 1.00 34.79  ? 128 GLN   A NE2   1 
ATOM   933  N N     . GLU   A 1 137 ? -11.939 -52.657  -33.290 1.00 31.56  ? 129 GLU   A N     1 
ATOM   934  C CA    . GLU   A 1 137 ? -10.938 -53.648  -32.938 1.00 31.81  ? 129 GLU   A CA    1 
ATOM   935  C C     . GLU   A 1 137 ? -10.212 -53.233  -31.660 1.00 29.77  ? 129 GLU   A C     1 
ATOM   936  O O     . GLU   A 1 137 ? -10.029 -54.050  -30.764 1.00 31.06  ? 129 GLU   A O     1 
ATOM   937  C CB    . GLU   A 1 137 ? -9.956  -53.845  -34.091 1.00 33.73  ? 129 GLU   A CB    1 
ATOM   938  C CG    . GLU   A 1 137 ? -8.899  -54.903  -33.789 1.00 36.13  ? 129 GLU   A CG    1 
ATOM   939  C CD    . GLU   A 1 137 ? -8.135  -55.405  -34.999 1.00 38.64  ? 129 GLU   A CD    1 
ATOM   940  O OE1   . GLU   A 1 137 ? -7.362  -56.369  -34.818 1.00 42.04  ? 129 GLU   A OE1   1 
ATOM   941  O OE2   . GLU   A 1 137 ? -8.304  -54.847  -36.105 1.00 38.72  ? 129 GLU   A OE2   1 
ATOM   942  N N     . ASP   A 1 138 ? -9.799  -51.963  -31.588 1.00 27.68  ? 130 ASP   A N     1 
ATOM   943  C CA    . ASP   A 1 138 ? -8.931  -51.497  -30.521 1.00 26.11  ? 130 ASP   A CA    1 
ATOM   944  C C     . ASP   A 1 138 ? -9.768  -50.924  -29.381 1.00 25.88  ? 130 ASP   A C     1 
ATOM   945  O O     . ASP   A 1 138 ? -10.397 -49.880  -29.533 1.00 26.22  ? 130 ASP   A O     1 
ATOM   946  C CB    . ASP   A 1 138 ? -7.934  -50.472  -31.037 1.00 24.84  ? 130 ASP   A CB    1 
ATOM   947  C CG    . ASP   A 1 138 ? -6.944  -49.954  -30.005 1.00 24.08  ? 130 ASP   A CG    1 
ATOM   948  O OD1   . ASP   A 1 138 ? -6.910  -50.508  -28.889 1.00 23.05  ? 130 ASP   A OD1   1 
ATOM   949  O OD2   . ASP   A 1 138 ? -6.221  -48.994  -30.326 1.00 23.88  ? 130 ASP   A OD2   1 
ATOM   950  N N     . ASN   A 1 139 ? -9.747  -51.607  -28.233 1.00 25.59  ? 131 ASN   A N     1 
ATOM   951  C CA    . ASN   A 1 139 ? -10.441 -51.144  -27.041 1.00 25.47  ? 131 ASN   A CA    1 
ATOM   952  C C     . ASN   A 1 139 ? -9.495  -51.246  -25.846 1.00 25.08  ? 131 ASN   A C     1 
ATOM   953  O O     . ASN   A 1 139 ? -9.928  -51.452  -24.715 1.00 24.36  ? 131 ASN   A O     1 
ATOM   954  C CB    . ASN   A 1 139 ? -11.754 -51.898  -26.858 1.00 25.38  ? 131 ASN   A CB    1 
ATOM   955  C CG    . ASN   A 1 139 ? -12.657 -51.739  -28.059 1.00 25.22  ? 131 ASN   A CG    1 
ATOM   956  O OD1   . ASN   A 1 139 ? -12.807 -52.674  -28.852 1.00 24.86  ? 131 ASN   A OD1   1 
ATOM   957  N ND2   . ASN   A 1 139 ? -13.236 -50.559  -28.231 1.00 25.01  ? 131 ASN   A ND2   1 
ATOM   958  N N     . THR   A 1 140 ? -8.202  -51.045  -26.119 1.00 25.14  ? 132 THR   A N     1 
ATOM   959  C CA    . THR   A 1 140 ? -7.137  -51.304  -25.166 1.00 25.52  ? 132 THR   A CA    1 
ATOM   960  C C     . THR   A 1 140 ? -7.279  -50.379  -23.960 1.00 26.08  ? 132 THR   A C     1 
ATOM   961  O O     . THR   A 1 140 ? -7.319  -50.833  -22.817 1.00 26.53  ? 132 THR   A O     1 
ATOM   962  C CB    . THR   A 1 140 ? -5.800  -51.108  -25.882 1.00 25.73  ? 132 THR   A CB    1 
ATOM   963  O OG1   . THR   A 1 140 ? -5.797  -52.017  -26.979 1.00 25.88  ? 132 THR   A OG1   1 
ATOM   964  C CG2   . THR   A 1 140 ? -4.611  -51.396  -24.986 1.00 25.67  ? 132 THR   A CG2   1 
ATOM   965  N N     . ASN   A 1 141 ? -7.341  -49.074  -24.229 1.00 26.40  ? 133 ASN   A N     1 
ATOM   966  C CA    . ASN   A 1 141 ? -7.383  -48.077  -23.174 1.00 26.55  ? 133 ASN   A CA    1 
ATOM   967  C C     . ASN   A 1 141 ? -8.722  -48.162  -22.444 1.00 26.45  ? 133 ASN   A C     1 
ATOM   968  O O     . ASN   A 1 141 ? -8.792  -47.863  -21.255 1.00 27.06  ? 133 ASN   A O     1 
ATOM   969  C CB    . ASN   A 1 141 ? -7.081  -46.690  -23.728 1.00 26.98  ? 133 ASN   A CB    1 
ATOM   970  C CG    . ASN   A 1 141 ? -6.708  -45.710  -22.643 1.00 27.42  ? 133 ASN   A CG    1 
ATOM   971  O OD1   . ASN   A 1 141 ? -5.972  -46.061  -21.714 1.00 27.34  ? 133 ASN   A OD1   1 
ATOM   972  N ND2   . ASN   A 1 141 ? -7.202  -44.485  -22.738 1.00 28.20  ? 133 ASN   A ND2   1 
ATOM   973  N N     . LEU   A 1 142 ? -9.775  -48.579  -23.159 1.00 26.45  ? 134 LEU   A N     1 
ATOM   974  C CA    . LEU   A 1 142 ? -11.074 -48.824  -22.552 1.00 26.92  ? 134 LEU   A CA    1 
ATOM   975  C C     . LEU   A 1 142 ? -10.955 -49.933  -21.507 1.00 26.99  ? 134 LEU   A C     1 
ATOM   976  O O     . LEU   A 1 142 ? -11.474 -49.804  -20.400 1.00 27.64  ? 134 LEU   A O     1 
ATOM   977  C CB    . LEU   A 1 142 ? -12.091 -49.184  -23.634 1.00 27.31  ? 134 LEU   A CB    1 
ATOM   978  C CG    . LEU   A 1 142 ? -13.468 -49.652  -23.151 1.00 27.87  ? 134 LEU   A CG    1 
ATOM   979  C CD1   . LEU   A 1 142 ? -14.339 -48.484  -22.755 1.00 28.18  ? 134 LEU   A CD1   1 
ATOM   980  C CD2   . LEU   A 1 142 ? -14.158 -50.484  -24.213 1.00 28.87  ? 134 LEU   A CD2   1 
ATOM   981  N N     . ALA   A 1 143 ? -10.272 -51.024  -21.875 1.00 26.39  ? 135 ALA   A N     1 
ATOM   982  C CA    . ALA   A 1 143 ? -10.090 -52.165  -20.991 1.00 25.69  ? 135 ALA   A CA    1 
ATOM   983  C C     . ALA   A 1 143 ? -9.315  -51.751  -19.742 1.00 25.15  ? 135 ALA   A C     1 
ATOM   984  O O     . ALA   A 1 143 ? -9.662  -52.145  -18.630 1.00 25.42  ? 135 ALA   A O     1 
ATOM   985  C CB    . ALA   A 1 143 ? -9.375  -53.278  -21.725 1.00 25.70  ? 135 ALA   A CB    1 
ATOM   986  N N     . ARG   A 1 144 ? -8.260  -50.959  -19.952 1.00 23.98  ? 136 ARG   A N     1 
ATOM   987  C CA    . ARG   A 1 144 ? -7.380  -50.525  -18.880 1.00 23.65  ? 136 ARG   A CA    1 
ATOM   988  C C     . ARG   A 1 144 ? -8.186  -49.775  -17.825 1.00 23.14  ? 136 ARG   A C     1 
ATOM   989  O O     . ARG   A 1 144 ? -8.009  -50.000  -16.630 1.00 24.00  ? 136 ARG   A O     1 
ATOM   990  C CB    . ARG   A 1 144 ? -6.271  -49.675  -19.508 1.00 24.09  ? 136 ARG   A CB    1 
ATOM   991  C CG    . ARG   A 1 144 ? -5.109  -49.317  -18.594 1.00 24.25  ? 136 ARG   A CG    1 
ATOM   992  C CD    . ARG   A 1 144 ? -5.318  -48.023  -17.832 1.00 24.59  ? 136 ARG   A CD    1 
ATOM   993  N NE    . ARG   A 1 144 ? -5.368  -46.873  -18.741 1.00 25.00  ? 136 ARG   A NE    1 
ATOM   994  C CZ    . ARG   A 1 144 ? -5.305  -45.601  -18.370 1.00 24.99  ? 136 ARG   A CZ    1 
ATOM   995  N NH1   . ARG   A 1 144 ? -5.141  -45.286  -17.099 1.00 25.04  ? 136 ARG   A NH1   1 
ATOM   996  N NH2   . ARG   A 1 144 ? -5.383  -44.644  -19.278 1.00 25.27  ? 136 ARG   A NH2   1 
ATOM   997  N N     . VAL   A 1 145 ? -9.083  -48.896  -18.282 1.00 22.56  ? 137 VAL   A N     1 
ATOM   998  C CA    . VAL   A 1 145 ? -9.921  -48.124  -17.381 1.00 22.42  ? 137 VAL   A CA    1 
ATOM   999  C C     . VAL   A 1 145 ? -10.871 -49.076  -16.654 1.00 22.09  ? 137 VAL   A C     1 
ATOM   1000 O O     . VAL   A 1 145 ? -10.979 -49.012  -15.435 1.00 21.13  ? 137 VAL   A O     1 
ATOM   1001 C CB    . VAL   A 1 145 ? -10.681 -46.988  -18.098 1.00 22.40  ? 137 VAL   A CB    1 
ATOM   1002 C CG1   . VAL   A 1 145 ? -11.628 -46.249  -17.159 1.00 22.21  ? 137 VAL   A CG1   1 
ATOM   1003 C CG2   . VAL   A 1 145 ? -9.731  -45.989  -18.749 1.00 22.42  ? 137 VAL   A CG2   1 
ATOM   1004 N N     . LEU   A 1 146 ? -11.546 -49.963  -17.398 1.00 22.44  ? 138 LEU   A N     1 
ATOM   1005 C CA    . LEU   A 1 146 ? -12.484 -50.894  -16.791 1.00 22.80  ? 138 LEU   A CA    1 
ATOM   1006 C C     . LEU   A 1 146 ? -11.761 -51.729  -15.735 1.00 24.53  ? 138 LEU   A C     1 
ATOM   1007 O O     . LEU   A 1 146 ? -12.227 -51.828  -14.602 1.00 24.82  ? 138 LEU   A O     1 
ATOM   1008 C CB    . LEU   A 1 146 ? -13.163 -51.785  -17.830 1.00 22.21  ? 138 LEU   A CB    1 
ATOM   1009 C CG    . LEU   A 1 146 ? -14.175 -52.803  -17.286 1.00 21.70  ? 138 LEU   A CG    1 
ATOM   1010 C CD1   . LEU   A 1 146 ? -15.207 -52.150  -16.380 1.00 21.72  ? 138 LEU   A CD1   1 
ATOM   1011 C CD2   . LEU   A 1 146 ? -14.880 -53.547  -18.410 1.00 21.29  ? 138 LEU   A CD2   1 
ATOM   1012 N N     . THR   A 1 147 ? -10.615 -52.307  -16.116 1.00 25.94  ? 139 THR   A N     1 
ATOM   1013 C CA    . THR   A 1 147 ? -9.842  -53.172  -15.237 1.00 26.88  ? 139 THR   A CA    1 
ATOM   1014 C C     . THR   A 1 147 ? -9.550  -52.455  -13.924 1.00 28.41  ? 139 THR   A C     1 
ATOM   1015 O O     . THR   A 1 147 ? -9.629  -53.058  -12.856 1.00 29.63  ? 139 THR   A O     1 
ATOM   1016 C CB    . THR   A 1 147 ? -8.546  -53.593  -15.928 1.00 27.14  ? 139 THR   A CB    1 
ATOM   1017 O OG1   . THR   A 1 147 ? -8.938  -54.338  -17.075 1.00 27.03  ? 139 THR   A OG1   1 
ATOM   1018 C CG2   . THR   A 1 147 ? -7.675  -54.476  -15.054 1.00 27.57  ? 139 THR   A CG2   1 
ATOM   1019 N N     . ASN   A 1 148 ? -9.192  -51.170  -14.020 1.00 30.26  ? 140 ASN   A N     1 
ATOM   1020 C CA    . ASN   A 1 148 ? -8.815  -50.405  -12.845 1.00 31.30  ? 140 ASN   A CA    1 
ATOM   1021 C C     . ASN   A 1 148 ? -10.033 -50.229  -11.945 1.00 30.86  ? 140 ASN   A C     1 
ATOM   1022 O O     . ASN   A 1 148 ? -9.918  -50.329  -10.726 1.00 30.92  ? 140 ASN   A O     1 
ATOM   1023 C CB    . ASN   A 1 148 ? -8.168  -49.067  -13.193 1.00 32.71  ? 140 ASN   A CB    1 
ATOM   1024 C CG    . ASN   A 1 148 ? -6.774  -49.181  -13.774 1.00 35.55  ? 140 ASN   A CG    1 
ATOM   1025 O OD1   . ASN   A 1 148 ? -6.085  -48.162  -13.897 1.00 37.34  ? 140 ASN   A OD1   1 
ATOM   1026 N ND2   . ASN   A 1 148 ? -6.325  -50.373  -14.149 1.00 37.66  ? 140 ASN   A ND2   1 
ATOM   1027 N N     . HIS   A 1 149 ? -11.192 -49.971  -12.559 1.00 30.41  ? 141 HIS   A N     1 
ATOM   1028 C CA    . HIS   A 1 149 ? -12.433 -49.812  -11.820 1.00 30.28  ? 141 HIS   A CA    1 
ATOM   1029 C C     . HIS   A 1 149 ? -12.786 -51.125  -11.126 1.00 31.46  ? 141 HIS   A C     1 
ATOM   1030 O O     . HIS   A 1 149 ? -13.171 -51.122  -9.958  1.00 32.11  ? 141 HIS   A O     1 
ATOM   1031 C CB    . HIS   A 1 149 ? -13.546 -49.295  -12.738 1.00 29.40  ? 141 HIS   A CB    1 
ATOM   1032 C CG    . HIS   A 1 149 ? -14.913 -49.383  -12.147 1.00 28.69  ? 141 HIS   A CG    1 
ATOM   1033 N ND1   . HIS   A 1 149 ? -15.381 -48.508  -11.192 1.00 28.22  ? 141 HIS   A ND1   1 
ATOM   1034 C CD2   . HIS   A 1 149 ? -15.906 -50.256  -12.370 1.00 28.49  ? 141 HIS   A CD2   1 
ATOM   1035 C CE1   . HIS   A 1 149 ? -16.621 -48.845  -10.863 1.00 28.29  ? 141 HIS   A CE1   1 
ATOM   1036 N NE2   . HIS   A 1 149 ? -16.961 -49.903  -11.568 1.00 28.10  ? 141 HIS   A NE2   1 
ATOM   1037 N N     . ILE   A 1 150 ? -12.638 -52.242  -11.849 1.00 32.26  ? 142 ILE   A N     1 
ATOM   1038 C CA    . ILE   A 1 150 ? -12.889 -53.561  -11.289 1.00 33.13  ? 142 ILE   A CA    1 
ATOM   1039 C C     . ILE   A 1 150 ? -12.067 -53.738  -10.012 1.00 34.98  ? 142 ILE   A C     1 
ATOM   1040 O O     . ILE   A 1 150 ? -12.581 -54.248  -9.020  1.00 36.05  ? 142 ILE   A O     1 
ATOM   1041 C CB    . ILE   A 1 150 ? -12.612 -54.669  -12.325 1.00 32.60  ? 142 ILE   A CB    1 
ATOM   1042 C CG1   . ILE   A 1 150 ? -13.664 -54.655  -13.437 1.00 32.31  ? 142 ILE   A CG1   1 
ATOM   1043 C CG2   . ILE   A 1 150 ? -12.517 -56.044  -11.662 1.00 32.86  ? 142 ILE   A CG2   1 
ATOM   1044 C CD1   . ILE   A 1 150 ? -13.527 -55.771  -14.455 1.00 31.89  ? 142 ILE   A CD1   1 
ATOM   1045 N N     . HIS   A 1 151 ? -10.803 -53.296  -10.035 1.00 36.14  ? 143 HIS   A N     1 
ATOM   1046 C CA    . HIS   A 1 151 ? -9.904  -53.462  -8.904  1.00 38.04  ? 143 HIS   A CA    1 
ATOM   1047 C C     . HIS   A 1 151 ? -9.920  -52.218  -8.016  1.00 40.15  ? 143 HIS   A C     1 
ATOM   1048 O O     . HIS   A 1 151 ? -8.863  -51.712  -7.650  1.00 41.72  ? 143 HIS   A O     1 
ATOM   1049 C CB    . HIS   A 1 151 ? -8.476  -53.725  -9.395  1.00 38.85  ? 143 HIS   A CB    1 
ATOM   1050 C CG    . HIS   A 1 151 ? -8.341  -54.911  -10.287 1.00 39.63  ? 143 HIS   A CG    1 
ATOM   1051 N ND1   . HIS   A 1 151 ? -9.002  -56.101  -10.077 1.00 40.50  ? 143 HIS   A ND1   1 
ATOM   1052 C CD2   . HIS   A 1 151 ? -7.604  -55.083  -11.389 1.00 40.20  ? 143 HIS   A CD2   1 
ATOM   1053 C CE1   . HIS   A 1 151 ? -8.674  -56.955  -11.038 1.00 41.23  ? 143 HIS   A CE1   1 
ATOM   1054 N NE2   . HIS   A 1 151 ? -7.826  -56.355  -11.846 1.00 40.56  ? 143 HIS   A NE2   1 
ATOM   1055 N N     . THR   A 1 152 ? -11.118 -51.738  -7.658  1.00 41.88  ? 144 THR   A N     1 
ATOM   1056 C CA    . THR   A 1 152 ? -11.261 -50.508  -6.892  1.00 42.53  ? 144 THR   A CA    1 
ATOM   1057 C C     . THR   A 1 152 ? -12.651 -50.470  -6.257  1.00 45.08  ? 144 THR   A C     1 
ATOM   1058 O O     . THR   A 1 152 ? -13.647 -50.297  -6.958  1.00 46.22  ? 144 THR   A O     1 
ATOM   1059 C CB    . THR   A 1 152 ? -11.018 -49.305  -7.808  1.00 41.89  ? 144 THR   A CB    1 
ATOM   1060 O OG1   . THR   A 1 152 ? -9.626  -49.289  -8.107  1.00 40.54  ? 144 THR   A OG1   1 
ATOM   1061 C CG2   . THR   A 1 152 ? -11.377 -47.978  -7.163  1.00 41.84  ? 144 THR   A CG2   1 
ATOM   1062 N N     . GLY   A 1 153 ? -12.698 -50.625  -4.926  1.00 48.21  ? 145 GLY   A N     1 
ATOM   1063 C CA    . GLY   A 1 153 ? -13.939 -50.579  -4.166  1.00 48.64  ? 145 GLY   A CA    1 
ATOM   1064 C C     . GLY   A 1 153 ? -14.237 -51.915  -3.509  1.00 48.87  ? 145 GLY   A C     1 
ATOM   1065 O O     . GLY   A 1 153 ? -14.052 -52.943  -4.195  1.00 51.69  ? 145 GLY   A O     1 
ATOM   1066 N N     . HIS   A 1 155 ? -16.898 -55.354  -5.929  1.00 67.00  ? 147 HIS   A N     1 
ATOM   1067 C CA    . HIS   A 1 155 ? -18.362 -55.620  -5.831  1.00 66.74  ? 147 HIS   A CA    1 
ATOM   1068 C C     . HIS   A 1 155 ? -18.663 -56.819  -6.726  1.00 65.84  ? 147 HIS   A C     1 
ATOM   1069 O O     . HIS   A 1 155 ? -17.758 -57.311  -7.394  1.00 66.49  ? 147 HIS   A O     1 
ATOM   1070 C CB    . HIS   A 1 155 ? -19.155 -54.363  -6.209  1.00 67.36  ? 147 HIS   A CB    1 
ATOM   1071 C CG    . HIS   A 1 155 ? -18.462 -53.098  -5.818  1.00 70.16  ? 147 HIS   A CG    1 
ATOM   1072 N ND1   . HIS   A 1 155 ? -18.288 -52.047  -6.694  1.00 71.61  ? 147 HIS   A ND1   1 
ATOM   1073 C CD2   . HIS   A 1 155 ? -17.845 -52.740  -4.683  1.00 70.57  ? 147 HIS   A CD2   1 
ATOM   1074 C CE1   . HIS   A 1 155 ? -17.616 -51.079  -6.087  1.00 71.23  ? 147 HIS   A CE1   1 
ATOM   1075 N NE2   . HIS   A 1 155 ? -17.338 -51.479  -4.864  1.00 72.04  ? 147 HIS   A NE2   1 
ATOM   1076 N N     . SER   A 1 156 ? -19.916 -57.290  -6.745  1.00 63.24  ? 148 SER   A N     1 
ATOM   1077 C CA    . SER   A 1 156 ? -20.281 -58.379  -7.641  1.00 61.59  ? 148 SER   A CA    1 
ATOM   1078 C C     . SER   A 1 156 ? -21.040 -57.842  -8.855  1.00 57.59  ? 148 SER   A C     1 
ATOM   1079 O O     . SER   A 1 156 ? -21.665 -58.612  -9.584  1.00 58.37  ? 148 SER   A O     1 
ATOM   1080 C CB    . SER   A 1 156 ? -21.047 -59.474  -6.925  1.00 62.50  ? 148 SER   A CB    1 
ATOM   1081 O OG    . SER   A 1 156 ? -22.319 -59.030  -6.472  1.00 63.74  ? 148 SER   A OG    1 
ATOM   1082 N N     . SER   A 1 157 ? -20.946 -56.521  -9.079  1.00 51.30  ? 149 SER   A N     1 
ATOM   1083 C CA    . SER   A 1 157 ? -21.524 -55.882  -10.250 1.00 47.48  ? 149 SER   A CA    1 
ATOM   1084 C C     . SER   A 1 157 ? -20.944 -56.501  -11.521 1.00 42.98  ? 149 SER   A C     1 
ATOM   1085 O O     . SER   A 1 157 ? -19.785 -56.909  -11.538 1.00 42.47  ? 149 SER   A O     1 
ATOM   1086 C CB    . SER   A 1 157 ? -21.290 -54.394  -10.224 1.00 47.53  ? 149 SER   A CB    1 
ATOM   1087 O OG    . SER   A 1 157 ? -19.936 -54.085  -10.523 1.00 47.25  ? 149 SER   A OG    1 
ATOM   1088 N N     . MET   A 1 158 ? -21.767 -56.553  -12.574 1.00 37.89  ? 150 MET   A N     1 
ATOM   1089 C CA    . MET   A 1 158 ? -21.403 -57.197  -13.824 1.00 35.24  ? 150 MET   A CA    1 
ATOM   1090 C C     . MET   A 1 158 ? -21.257 -56.149  -14.921 1.00 33.03  ? 150 MET   A C     1 
ATOM   1091 O O     . MET   A 1 158 ? -21.934 -55.125  -14.903 1.00 33.50  ? 150 MET   A O     1 
ATOM   1092 C CB    . MET   A 1 158 ? -22.480 -58.199  -14.251 1.00 35.81  ? 150 MET   A CB    1 
ATOM   1093 C CG    . MET   A 1 158 ? -22.455 -59.512  -13.489 1.00 36.09  ? 150 MET   A CG    1 
ATOM   1094 S SD    . MET   A 1 158 ? -20.988 -60.511  -13.806 1.00 35.76  ? 150 MET   A SD    1 
ATOM   1095 C CE    . MET   A 1 158 ? -20.812 -60.359  -15.589 1.00 34.82  ? 150 MET   A CE    1 
ATOM   1096 N N     . PHE   A 1 159 ? -20.371 -56.426  -15.881 1.00 30.41  ? 151 PHE   A N     1 
ATOM   1097 C CA    . PHE   A 1 159 ? -20.213 -55.579  -17.049 1.00 28.73  ? 151 PHE   A CA    1 
ATOM   1098 C C     . PHE   A 1 159 ? -20.623 -56.383  -18.276 1.00 27.91  ? 151 PHE   A C     1 
ATOM   1099 O O     . PHE   A 1 159 ? -20.118 -57.478  -18.497 1.00 27.77  ? 151 PHE   A O     1 
ATOM   1100 C CB    . PHE   A 1 159 ? -18.780 -55.042  -17.064 1.00 27.74  ? 151 PHE   A CB    1 
ATOM   1101 C CG    . PHE   A 1 159 ? -18.469 -54.285  -15.783 1.00 26.95  ? 151 PHE   A CG    1 
ATOM   1102 C CD1   . PHE   A 1 159 ? -18.984 -53.012  -15.572 1.00 26.79  ? 151 PHE   A CD1   1 
ATOM   1103 C CD2   . PHE   A 1 159 ? -17.711 -54.867  -14.773 1.00 27.00  ? 151 PHE   A CD2   1 
ATOM   1104 C CE1   . PHE   A 1 159 ? -18.724 -52.332  -14.393 1.00 27.07  ? 151 PHE   A CE1   1 
ATOM   1105 C CE2   . PHE   A 1 159 ? -17.451 -54.182  -13.596 1.00 26.66  ? 151 PHE   A CE2   1 
ATOM   1106 C CZ    . PHE   A 1 159 ? -17.956 -52.917  -13.409 1.00 26.87  ? 151 PHE   A CZ    1 
ATOM   1107 N N     . TRP   A 1 160 ? -21.581 -55.839  -19.033 1.00 27.60  ? 152 TRP   A N     1 
ATOM   1108 C CA    . TRP   A 1 160 ? -22.036 -56.452  -20.267 1.00 27.62  ? 152 TRP   A CA    1 
ATOM   1109 C C     . TRP   A 1 160 ? -21.422 -55.714  -21.448 1.00 27.19  ? 152 TRP   A C     1 
ATOM   1110 O O     . TRP   A 1 160 ? -21.736 -54.549  -21.683 1.00 26.55  ? 152 TRP   A O     1 
ATOM   1111 C CB    . TRP   A 1 160 ? -23.567 -56.431  -20.346 1.00 28.23  ? 152 TRP   A CB    1 
ATOM   1112 C CG    . TRP   A 1 160 ? -24.248 -57.296  -19.320 1.00 29.15  ? 152 TRP   A CG    1 
ATOM   1113 C CD1   . TRP   A 1 160 ? -23.670 -58.208  -18.485 1.00 29.69  ? 152 TRP   A CD1   1 
ATOM   1114 C CD2   . TRP   A 1 160 ? -25.665 -57.345  -19.050 1.00 30.07  ? 152 TRP   A CD2   1 
ATOM   1115 N NE1   . TRP   A 1 160 ? -24.622 -58.807  -17.704 1.00 29.96  ? 152 TRP   A NE1   1 
ATOM   1116 C CE2   . TRP   A 1 160 ? -25.854 -58.303  -18.030 1.00 30.56  ? 152 TRP   A CE2   1 
ATOM   1117 C CE3   . TRP   A 1 160 ? -26.781 -56.673  -19.561 1.00 30.51  ? 152 TRP   A CE3   1 
ATOM   1118 C CZ2   . TRP   A 1 160 ? -27.116 -58.604  -17.521 1.00 31.47  ? 152 TRP   A CZ2   1 
ATOM   1119 C CZ3   . TRP   A 1 160 ? -28.028 -56.973  -19.057 1.00 31.04  ? 152 TRP   A CZ3   1 
ATOM   1120 C CH2   . TRP   A 1 160 ? -28.192 -57.929  -18.054 1.00 31.26  ? 152 TRP   A CH2   1 
ATOM   1121 N N     . MET   A 1 161 ? -20.534 -56.403  -22.171 1.00 27.28  ? 153 MET   A N     1 
ATOM   1122 C CA    . MET   A 1 161 ? -19.923 -55.839  -23.361 1.00 27.30  ? 153 MET   A CA    1 
ATOM   1123 C C     . MET   A 1 161 ? -20.858 -56.078  -24.542 1.00 27.60  ? 153 MET   A C     1 
ATOM   1124 O O     . MET   A 1 161 ? -21.146 -57.220  -24.894 1.00 26.76  ? 153 MET   A O     1 
ATOM   1125 C CB    . MET   A 1 161 ? -18.537 -56.444  -23.613 1.00 27.09  ? 153 MET   A CB    1 
ATOM   1126 C CG    . MET   A 1 161 ? -17.637 -56.414  -22.393 1.00 26.99  ? 153 MET   A CG    1 
ATOM   1127 S SD    . MET   A 1 161 ? -17.588 -54.801  -21.586 1.00 26.86  ? 153 MET   A SD    1 
ATOM   1128 C CE    . MET   A 1 161 ? -16.773 -53.820  -22.854 1.00 27.06  ? 153 MET   A CE    1 
ATOM   1129 N N     . ARG   A 1 162 ? -21.357 -54.975  -25.113 1.00 28.32  ? 154 ARG   A N     1 
ATOM   1130 C CA    . ARG   A 1 162 ? -22.218 -55.018  -26.281 1.00 29.19  ? 154 ARG   A CA    1 
ATOM   1131 C C     . ARG   A 1 162 ? -21.354 -55.301  -27.506 1.00 27.57  ? 154 ARG   A C     1 
ATOM   1132 O O     . ARG   A 1 162 ? -20.513 -54.487  -27.878 1.00 26.82  ? 154 ARG   A O     1 
ATOM   1133 C CB    . ARG   A 1 162 ? -22.972 -53.687  -26.377 1.00 30.93  ? 154 ARG   A CB    1 
ATOM   1134 C CG    . ARG   A 1 162 ? -24.154 -53.656  -27.336 1.00 32.46  ? 154 ARG   A CG    1 
ATOM   1135 C CD    . ARG   A 1 162 ? -25.071 -52.504  -26.949 1.00 34.01  ? 154 ARG   A CD    1 
ATOM   1136 N NE    . ARG   A 1 162 ? -26.367 -52.508  -27.637 1.00 35.33  ? 154 ARG   A NE    1 
ATOM   1137 C CZ    . ARG   A 1 162 ? -27.421 -51.767  -27.300 1.00 34.85  ? 154 ARG   A CZ    1 
ATOM   1138 N NH1   . ARG   A 1 162 ? -27.371 -50.960  -26.253 1.00 34.21  ? 154 ARG   A NH1   1 
ATOM   1139 N NH2   . ARG   A 1 162 ? -28.531 -51.845  -28.016 1.00 35.48  ? 154 ARG   A NH2   1 
ATOM   1140 N N     . VAL   A 1 163 ? -21.552 -56.478  -28.102 1.00 27.25  ? 155 VAL   A N     1 
ATOM   1141 C CA    . VAL   A 1 163 ? -20.759 -56.912  -29.238 1.00 27.01  ? 155 VAL   A CA    1 
ATOM   1142 C C     . VAL   A 1 163 ? -21.720 -57.272  -30.362 1.00 27.09  ? 155 VAL   A C     1 
ATOM   1143 O O     . VAL   A 1 163 ? -22.648 -58.052  -30.152 1.00 26.96  ? 155 VAL   A O     1 
ATOM   1144 C CB    . VAL   A 1 163 ? -19.848 -58.113  -28.919 1.00 27.40  ? 155 VAL   A CB    1 
ATOM   1145 C CG1   . VAL   A 1 163 ? -18.846 -58.369  -30.038 1.00 27.56  ? 155 VAL   A CG1   1 
ATOM   1146 C CG2   . VAL   A 1 163 ? -19.125 -57.948  -27.591 1.00 27.74  ? 155 VAL   A CG2   1 
ATOM   1147 N N     . PRO   A 1 164 ? -21.529 -56.719  -31.581 1.00 26.96  ? 156 PRO   A N     1 
ATOM   1148 C CA    . PRO   A 1 164 ? -22.320 -57.137  -32.734 1.00 26.80  ? 156 PRO   A CA    1 
ATOM   1149 C C     . PRO   A 1 164 ? -21.829 -58.487  -33.249 1.00 27.11  ? 156 PRO   A C     1 
ATOM   1150 O O     . PRO   A 1 164 ? -20.632 -58.694  -33.434 1.00 26.05  ? 156 PRO   A O     1 
ATOM   1151 C CB    . PRO   A 1 164 ? -22.111 -55.997  -33.739 1.00 26.71  ? 156 PRO   A CB    1 
ATOM   1152 C CG    . PRO   A 1 164 ? -20.737 -55.449  -33.407 1.00 26.86  ? 156 PRO   A CG    1 
ATOM   1153 C CD    . PRO   A 1 164 ? -20.557 -55.663  -31.911 1.00 26.94  ? 156 PRO   A CD    1 
ATOM   1154 N N     . LEU   A 1 165 ? -22.779 -59.401  -33.458 1.00 27.79  ? 157 LEU   A N     1 
ATOM   1155 C CA    . LEU   A 1 165 ? -22.529 -60.649  -34.158 1.00 28.66  ? 157 LEU   A CA    1 
ATOM   1156 C C     . LEU   A 1 165 ? -21.870 -60.374  -35.511 1.00 28.93  ? 157 LEU   A C     1 
ATOM   1157 O O     . LEU   A 1 165 ? -21.022 -61.144  -35.957 1.00 29.67  ? 157 LEU   A O     1 
ATOM   1158 C CB    . LEU   A 1 165 ? -23.879 -61.348  -34.309 1.00 28.96  ? 157 LEU   A CB    1 
ATOM   1159 C CG    . LEU   A 1 165 ? -23.855 -62.763  -34.889 1.00 29.56  ? 157 LEU   A CG    1 
ATOM   1160 C CD1   . LEU   A 1 165 ? -23.037 -63.710  -34.025 1.00 29.89  ? 157 LEU   A CD1   1 
ATOM   1161 C CD2   . LEU   A 1 165 ? -25.281 -63.262  -35.032 1.00 30.20  ? 157 LEU   A CD2   1 
ATOM   1162 N N     . VAL   A 1 166 ? -22.272 -59.263  -36.143 1.00 28.63  ? 158 VAL   A N     1 
ATOM   1163 C CA    . VAL   A 1 166 ? -21.752 -58.825  -37.429 1.00 28.71  ? 158 VAL   A CA    1 
ATOM   1164 C C     . VAL   A 1 166 ? -21.463 -57.331  -37.320 1.00 28.28  ? 158 VAL   A C     1 
ATOM   1165 O O     . VAL   A 1 166 ? -22.371 -56.538  -37.081 1.00 28.04  ? 158 VAL   A O     1 
ATOM   1166 C CB    . VAL   A 1 166 ? -22.729 -59.119  -38.587 1.00 28.96  ? 158 VAL   A CB    1 
ATOM   1167 C CG1   . VAL   A 1 166 ? -22.258 -58.523  -39.911 1.00 29.17  ? 158 VAL   A CG1   1 
ATOM   1168 C CG2   . VAL   A 1 166 ? -22.997 -60.612  -38.743 1.00 28.59  ? 158 VAL   A CG2   1 
ATOM   1169 N N     . ALA   A 1 167 ? -20.193 -56.959  -37.499 1.00 28.55  ? 159 ALA   A N     1 
ATOM   1170 C CA    . ALA   A 1 167 ? -19.778 -55.572  -37.365 1.00 29.39  ? 159 ALA   A CA    1 
ATOM   1171 C C     . ALA   A 1 167 ? -20.592 -54.701  -38.320 1.00 30.23  ? 159 ALA   A C     1 
ATOM   1172 O O     . ALA   A 1 167 ? -20.911 -55.140  -39.425 1.00 29.10  ? 159 ALA   A O     1 
ATOM   1173 C CB    . ALA   A 1 167 ? -18.290 -55.448  -37.624 1.00 29.46  ? 159 ALA   A CB    1 
ATOM   1174 N N     . PRO   A 1 168 ? -20.953 -53.453  -37.929 1.00 30.95  ? 160 PRO   A N     1 
ATOM   1175 C CA    . PRO   A 1 168 ? -21.790 -52.585  -38.764 1.00 30.18  ? 160 PRO   A CA    1 
ATOM   1176 C C     . PRO   A 1 168 ? -21.271 -52.408  -40.187 1.00 29.79  ? 160 PRO   A C     1 
ATOM   1177 O O     . PRO   A 1 168 ? -22.051 -52.399  -41.140 1.00 29.66  ? 160 PRO   A O     1 
ATOM   1178 C CB    . PRO   A 1 168 ? -21.785 -51.252  -37.997 1.00 30.52  ? 160 PRO   A CB    1 
ATOM   1179 C CG    . PRO   A 1 168 ? -21.544 -51.647  -36.562 1.00 30.67  ? 160 PRO   A CG    1 
ATOM   1180 C CD    . PRO   A 1 168 ? -20.579 -52.814  -36.655 1.00 30.97  ? 160 PRO   A CD    1 
ATOM   1181 N N     . GLU   A 1 169 ? -19.944 -52.277  -40.303 1.00 29.32  ? 161 GLU   A N     1 
ATOM   1182 C CA    . GLU   A 1 169 ? -19.264 -52.085  -41.573 1.00 29.25  ? 161 GLU   A CA    1 
ATOM   1183 C C     . GLU   A 1 169 ? -19.548 -53.234  -42.543 1.00 29.33  ? 161 GLU   A C     1 
ATOM   1184 O O     . GLU   A 1 169 ? -19.488 -53.037  -43.753 1.00 28.99  ? 161 GLU   A O     1 
ATOM   1185 C CB    . GLU   A 1 169 ? -17.764 -51.957  -41.303 1.00 29.03  ? 161 GLU   A CB    1 
ATOM   1186 C CG    . GLU   A 1 169 ? -16.925 -51.731  -42.556 1.00 29.64  ? 161 GLU   A CG    1 
ATOM   1187 C CD    . GLU   A 1 169 ? -17.325 -50.503  -43.354 1.00 29.87  ? 161 GLU   A CD    1 
ATOM   1188 O OE1   . GLU   A 1 169 ? -17.252 -49.385  -42.802 1.00 29.12  ? 161 GLU   A OE1   1 
ATOM   1189 O OE2   . GLU   A 1 169 ? -17.710 -50.665  -44.532 1.00 31.36  ? 161 GLU   A OE2   1 
ATOM   1190 N N     . ASP   A 1 170 ? -19.851 -54.427  -42.011 1.00 29.36  ? 162 ASP   A N     1 
ATOM   1191 C CA    . ASP   A 1 170 ? -20.007 -55.627  -42.819 1.00 30.15  ? 162 ASP   A CA    1 
ATOM   1192 C C     . ASP   A 1 170 ? -21.482 -55.947  -43.065 1.00 30.09  ? 162 ASP   A C     1 
ATOM   1193 O O     . ASP   A 1 170 ? -21.799 -57.020  -43.575 1.00 29.72  ? 162 ASP   A O     1 
ATOM   1194 C CB    . ASP   A 1 170 ? -19.328 -56.815  -42.153 1.00 31.02  ? 162 ASP   A CB    1 
ATOM   1195 C CG    . ASP   A 1 170 ? -17.839 -56.656  -41.882 1.00 31.71  ? 162 ASP   A CG    1 
ATOM   1196 O OD1   . ASP   A 1 170 ? -17.206 -55.810  -42.554 1.00 31.99  ? 162 ASP   A OD1   1 
ATOM   1197 O OD2   . ASP   A 1 170 ? -17.329 -57.359  -40.981 1.00 31.35  ? 162 ASP   A OD2   1 
ATOM   1198 N N     . LEU   A 1 171 ? -22.385 -55.038  -42.679 1.00 30.57  ? 163 LEU   A N     1 
ATOM   1199 C CA    . LEU   A 1 171 ? -23.803 -55.222  -42.952 1.00 31.38  ? 163 LEU   A CA    1 
ATOM   1200 C C     . LEU   A 1 171 ? -24.408 -53.940  -43.524 1.00 32.06  ? 163 LEU   A C     1 
ATOM   1201 O O     . LEU   A 1 171 ? -25.630 -53.816  -43.602 1.00 31.80  ? 163 LEU   A O     1 
ATOM   1202 C CB    . LEU   A 1 171 ? -24.526 -55.681  -41.685 1.00 31.17  ? 163 LEU   A CB    1 
ATOM   1203 C CG    . LEU   A 1 171 ? -24.308 -54.834  -40.427 1.00 31.70  ? 163 LEU   A CG    1 
ATOM   1204 C CD1   . LEU   A 1 171 ? -25.028 -53.498  -40.492 1.00 31.88  ? 163 LEU   A CD1   1 
ATOM   1205 C CD2   . LEU   A 1 171 ? -24.736 -55.607  -39.192 1.00 32.07  ? 163 LEU   A CD2   1 
ATOM   1206 N N     . ARG   A 1 172 ? -23.554 -52.993  -43.935 1.00 32.08  ? 164 ARG   A N     1 
ATOM   1207 C CA    . ARG   A 1 172 ? -24.037 -51.748  -44.506 1.00 33.02  ? 164 ARG   A CA    1 
ATOM   1208 C C     . ARG   A 1 172 ? -24.662 -52.057  -45.864 1.00 32.91  ? 164 ARG   A C     1 
ATOM   1209 O O     . ARG   A 1 172 ? -24.341 -53.070  -46.481 1.00 32.29  ? 164 ARG   A O     1 
ATOM   1210 C CB    . ARG   A 1 172 ? -22.926 -50.693  -44.603 1.00 33.19  ? 164 ARG   A CB    1 
ATOM   1211 C CG    . ARG   A 1 172 ? -21.808 -50.987  -45.592 1.00 33.18  ? 164 ARG   A CG    1 
ATOM   1212 C CD    . ARG   A 1 172 ? -20.702 -49.940  -45.515 1.00 33.88  ? 164 ARG   A CD    1 
ATOM   1213 N NE    . ARG   A 1 172 ? -19.638 -50.213  -46.487 1.00 35.36  ? 164 ARG   A NE    1 
ATOM   1214 C CZ    . ARG   A 1 172 ? -19.771 -50.170  -47.815 1.00 36.84  ? 164 ARG   A CZ    1 
ATOM   1215 N NH1   . ARG   A 1 172 ? -20.868 -49.675  -48.371 1.00 37.53  ? 164 ARG   A NH1   1 
ATOM   1216 N NH2   . ARG   A 1 172 ? -18.790 -50.608  -48.587 1.00 36.10  ? 164 ARG   A NH2   1 
ATOM   1217 N N     . ASP   A 1 173 ? -25.585 -51.187  -46.291 1.00 34.23  ? 165 ASP   A N     1 
ATOM   1218 C CA    . ASP   A 1 173 ? -26.131 -51.226  -47.637 1.00 34.46  ? 165 ASP   A CA    1 
ATOM   1219 C C     . ASP   A 1 173 ? -25.007 -50.932  -48.626 1.00 34.02  ? 165 ASP   A C     1 
ATOM   1220 O O     . ASP   A 1 173 ? -24.159 -50.078  -48.366 1.00 33.05  ? 165 ASP   A O     1 
ATOM   1221 C CB    . ASP   A 1 173 ? -27.271 -50.232  -47.802 1.00 34.94  ? 165 ASP   A CB    1 
ATOM   1222 C CG    . ASP   A 1 173 ? -28.509 -50.502  -46.960 1.00 35.76  ? 165 ASP   A CG    1 
ATOM   1223 O OD1   . ASP   A 1 173 ? -28.617 -51.619  -46.416 1.00 37.73  ? 165 ASP   A OD1   1 
ATOM   1224 O OD2   . ASP   A 1 173 ? -29.349 -49.586  -46.841 1.00 36.11  ? 165 ASP   A OD2   1 
ATOM   1225 N N     . ASP   A 1 174 ? -25.016 -51.658  -49.750 1.00 34.50  ? 166 ASP   A N     1 
ATOM   1226 C CA    . ASP   A 1 174 ? -24.047 -51.466  -50.816 1.00 34.55  ? 166 ASP   A CA    1 
ATOM   1227 C C     . ASP   A 1 174 ? -24.544 -50.340  -51.718 1.00 35.49  ? 166 ASP   A C     1 
ATOM   1228 O O     . ASP   A 1 174 ? -25.003 -50.587  -52.833 1.00 35.62  ? 166 ASP   A O     1 
ATOM   1229 C CB    . ASP   A 1 174 ? -23.811 -52.765  -51.571 1.00 34.51  ? 166 ASP   A CB    1 
ATOM   1230 C CG    . ASP   A 1 174 ? -22.712 -52.734  -52.623 1.00 34.77  ? 166 ASP   A CG    1 
ATOM   1231 O OD1   . ASP   A 1 174 ? -21.942 -51.749  -52.652 1.00 34.10  ? 166 ASP   A OD1   1 
ATOM   1232 O OD2   . ASP   A 1 174 ? -22.643 -53.696  -53.412 1.00 36.01  ? 166 ASP   A OD2   1 
ATOM   1233 N N     . ILE   A 1 175 ? -24.445 -49.106  -51.208 1.00 35.62  ? 167 ILE   A N     1 
ATOM   1234 C CA    . ILE   A 1 175 ? -24.988 -47.933  -51.875 1.00 35.53  ? 167 ILE   A CA    1 
ATOM   1235 C C     . ILE   A 1 175 ? -23.933 -46.832  -51.963 1.00 35.92  ? 167 ILE   A C     1 
ATOM   1236 O O     . ILE   A 1 175 ? -24.236 -45.742  -52.442 1.00 36.71  ? 167 ILE   A O     1 
ATOM   1237 C CB    . ILE   A 1 175 ? -26.271 -47.446  -51.171 1.00 35.88  ? 167 ILE   A CB    1 
ATOM   1238 C CG1   . ILE   A 1 175 ? -26.057 -47.219  -49.662 1.00 36.75  ? 167 ILE   A CG1   1 
ATOM   1239 C CG2   . ILE   A 1 175 ? -27.427 -48.409  -51.448 1.00 35.79  ? 167 ILE   A CG2   1 
ATOM   1240 C CD1   . ILE   A 1 175 ? -27.296 -46.766  -48.908 1.00 36.74  ? 167 ILE   A CD1   1 
ATOM   1241 N N     . ILE   A 1 176 ? -22.702 -47.102  -51.506 1.00 36.47  ? 168 ILE   A N     1 
ATOM   1242 C CA    . ILE   A 1 176 ? -21.585 -46.239  -51.849 1.00 38.27  ? 168 ILE   A CA    1 
ATOM   1243 C C     . ILE   A 1 176 ? -21.017 -46.766  -53.162 1.00 41.64  ? 168 ILE   A C     1 
ATOM   1244 O O     . ILE   A 1 176 ? -20.504 -47.883  -53.211 1.00 42.56  ? 168 ILE   A O     1 
ATOM   1245 C CB    . ILE   A 1 176 ? -20.511 -46.162  -50.748 1.00 37.93  ? 168 ILE   A CB    1 
ATOM   1246 C CG1   . ILE   A 1 176 ? -21.115 -45.994  -49.352 1.00 37.74  ? 168 ILE   A CG1   1 
ATOM   1247 C CG2   . ILE   A 1 176 ? -19.510 -45.050  -51.070 1.00 37.33  ? 168 ILE   A CG2   1 
ATOM   1248 C CD1   . ILE   A 1 176 ? -20.087 -45.797  -48.251 1.00 37.99  ? 168 ILE   A CD1   1 
ATOM   1249 N N     . GLU   A 1 177 ? -21.136 -45.957  -54.221 1.00 44.04  ? 169 GLU   A N     1 
ATOM   1250 C CA    . GLU   A 1 177 ? -20.867 -46.417  -55.574 1.00 45.31  ? 169 GLU   A CA    1 
ATOM   1251 C C     . GLU   A 1 177 ? -19.361 -46.574  -55.783 1.00 45.02  ? 169 GLU   A C     1 
ATOM   1252 O O     . GLU   A 1 177 ? -18.939 -47.409  -56.579 1.00 44.93  ? 169 GLU   A O     1 
ATOM   1253 C CB    . GLU   A 1 177 ? -21.576 -45.517  -56.590 1.00 47.01  ? 169 GLU   A CB    1 
ATOM   1254 C CG    . GLU   A 1 177 ? -21.066 -44.079  -56.667 1.00 47.95  ? 169 GLU   A CG    1 
ATOM   1255 C CD    . GLU   A 1 177 ? -19.764 -43.892  -57.422 1.00 48.69  ? 169 GLU   A CD    1 
ATOM   1256 O OE1   . GLU   A 1 177 ? -18.961 -43.029  -57.006 1.00 49.46  ? 169 GLU   A OE1   1 
ATOM   1257 O OE2   . GLU   A 1 177 ? -19.548 -44.620  -58.415 1.00 48.03  ? 169 GLU   A OE2   1 
ATOM   1258 N N     . ASN   A 1 178 ? -18.560 -45.799  -55.039 1.00 44.73  ? 170 ASN   A N     1 
ATOM   1259 C CA    . ASN   A 1 178 ? -17.108 -45.856  -55.137 1.00 44.42  ? 170 ASN   A CA    1 
ATOM   1260 C C     . ASN   A 1 178 ? -16.496 -46.569  -53.929 1.00 44.84  ? 170 ASN   A C     1 
ATOM   1261 O O     . ASN   A 1 178 ? -15.308 -46.403  -53.655 1.00 45.56  ? 170 ASN   A O     1 
ATOM   1262 C CB    . ASN   A 1 178 ? -16.503 -44.462  -55.275 1.00 44.29  ? 170 ASN   A CB    1 
ATOM   1263 C CG    . ASN   A 1 178 ? -16.804 -43.573  -54.089 1.00 44.06  ? 170 ASN   A CG    1 
ATOM   1264 O OD1   . ASN   A 1 178 ? -17.727 -43.849  -53.314 1.00 44.34  ? 170 ASN   A OD1   1 
ATOM   1265 N ND2   . ASN   A 1 178 ? -16.051 -42.494  -53.938 1.00 42.75  ? 170 ASN   A ND2   1 
ATOM   1266 N N     . ALA   A 1 179 ? -17.303 -47.351  -53.202 1.00 43.72  ? 171 ALA   A N     1 
ATOM   1267 C CA    . ALA   A 1 179 ? -16.805 -48.168  -52.105 1.00 42.92  ? 171 ALA   A CA    1 
ATOM   1268 C C     . ALA   A 1 179 ? -17.697 -49.397  -51.961 1.00 43.18  ? 171 ALA   A C     1 
ATOM   1269 O O     . ALA   A 1 179 ? -18.470 -49.498  -51.012 1.00 43.12  ? 171 ALA   A O     1 
ATOM   1270 C CB    . ALA   A 1 179 ? -16.755 -47.363  -50.823 1.00 42.33  ? 171 ALA   A CB    1 
ATOM   1271 N N     . PRO   A 1 180 ? -17.636 -50.352  -52.916 1.00 43.99  ? 172 PRO   A N     1 
ATOM   1272 C CA    . PRO   A 1 180 ? -18.546 -51.496  -52.905 1.00 44.68  ? 172 PRO   A CA    1 
ATOM   1273 C C     . PRO   A 1 180 ? -18.279 -52.397  -51.703 1.00 46.03  ? 172 PRO   A C     1 
ATOM   1274 O O     . PRO   A 1 180 ? -17.145 -52.501  -51.239 1.00 45.13  ? 172 PRO   A O     1 
ATOM   1275 C CB    . PRO   A 1 180 ? -18.305 -52.211  -54.251 1.00 43.89  ? 172 PRO   A CB    1 
ATOM   1276 C CG    . PRO   A 1 180 ? -16.960 -51.701  -54.737 1.00 43.47  ? 172 PRO   A CG    1 
ATOM   1277 C CD    . PRO   A 1 180 ? -16.700 -50.370  -54.052 1.00 43.57  ? 172 PRO   A CD    1 
ATOM   1278 N N     . THR   A 1 181 ? -19.346 -53.021  -51.196 1.00 48.17  ? 173 THR   A N     1 
ATOM   1279 C CA    . THR   A 1 181 ? -19.223 -54.028  -50.157 1.00 50.84  ? 173 THR   A CA    1 
ATOM   1280 C C     . THR   A 1 181 ? -18.611 -55.271  -50.796 1.00 55.70  ? 173 THR   A C     1 
ATOM   1281 O O     . THR   A 1 181 ? -18.944 -55.603  -51.932 1.00 58.71  ? 173 THR   A O     1 
ATOM   1282 C CB    . THR   A 1 181 ? -20.586 -54.316  -49.523 1.00 49.53  ? 173 THR   A CB    1 
ATOM   1283 O OG1   . THR   A 1 181 ? -21.414 -54.864  -50.543 1.00 48.89  ? 173 THR   A OG1   1 
ATOM   1284 C CG2   . THR   A 1 181 ? -21.243 -53.079  -48.935 1.00 48.41  ? 173 THR   A CG2   1 
ATOM   1285 N N     . THR   A 1 182 ? -17.706 -55.938  -50.070 1.00 60.92  ? 174 THR   A N     1 
ATOM   1286 C CA    . THR   A 1 182 ? -17.010 -57.106  -50.590 1.00 65.28  ? 174 THR   A CA    1 
ATOM   1287 C C     . THR   A 1 182 ? -18.035 -58.174  -50.968 1.00 70.17  ? 174 THR   A C     1 
ATOM   1288 O O     . THR   A 1 182 ? -19.160 -58.162  -50.470 1.00 72.56  ? 174 THR   A O     1 
ATOM   1289 C CB    . THR   A 1 182 ? -16.002 -57.630  -49.564 1.00 64.16  ? 174 THR   A CB    1 
ATOM   1290 O OG1   . THR   A 1 182 ? -15.285 -58.661  -50.234 1.00 63.57  ? 174 THR   A OG1   1 
ATOM   1291 C CG2   . THR   A 1 182 ? -16.651 -58.192  -48.310 1.00 62.83  ? 174 THR   A CG2   1 
ATOM   1292 N N     . HIS   A 1 183 ? -17.635 -59.083  -51.865 1.00 72.99  ? 175 HIS   A N     1 
ATOM   1293 C CA    . HIS   A 1 183 ? -18.466 -60.221  -52.225 1.00 76.40  ? 175 HIS   A CA    1 
ATOM   1294 C C     . HIS   A 1 183 ? -17.635 -61.506  -52.265 1.00 76.13  ? 175 HIS   A C     1 
ATOM   1295 O O     . HIS   A 1 183 ? -18.135 -62.547  -52.689 1.00 77.27  ? 175 HIS   A O     1 
ATOM   1296 C CB    . HIS   A 1 183 ? -19.229 -59.927  -53.525 1.00 79.98  ? 175 HIS   A CB    1 
ATOM   1297 C CG    . HIS   A 1 183 ? -20.325 -60.898  -53.833 1.00 83.52  ? 175 HIS   A CG    1 
ATOM   1298 N ND1   . HIS   A 1 183 ? -21.524 -60.920  -53.152 1.00 84.67  ? 175 HIS   A ND1   1 
ATOM   1299 C CD2   . HIS   A 1 183 ? -20.395 -61.891  -54.732 1.00 84.41  ? 175 HIS   A CD2   1 
ATOM   1300 C CE1   . HIS   A 1 183 ? -22.287 -61.888  -53.639 1.00 84.14  ? 175 HIS   A CE1   1 
ATOM   1301 N NE2   . HIS   A 1 183 ? -21.622 -62.490  -54.600 1.00 84.52  ? 175 HIS   A NE2   1 
ATOM   1302 N N     . THR   A 1 184 ? -16.373 -61.439  -51.816 1.00 73.89  ? 176 THR   A N     1 
ATOM   1303 C CA    . THR   A 1 184 ? -15.604 -62.638  -51.527 1.00 71.29  ? 176 THR   A CA    1 
ATOM   1304 C C     . THR   A 1 184 ? -15.675 -62.904  -50.026 1.00 71.01  ? 176 THR   A C     1 
ATOM   1305 O O     . THR   A 1 184 ? -15.585 -61.981  -49.216 1.00 69.88  ? 176 THR   A O     1 
ATOM   1306 C CB    . THR   A 1 184 ? -14.156 -62.518  -52.006 1.00 69.81  ? 176 THR   A CB    1 
ATOM   1307 O OG1   . THR   A 1 184 ? -13.715 -61.205  -51.676 1.00 68.08  ? 176 THR   A OG1   1 
ATOM   1308 C CG2   . THR   A 1 184 ? -14.017 -62.757  -53.499 1.00 70.29  ? 176 THR   A CG2   1 
ATOM   1309 N N     . GLU   A 1 185 ? -15.856 -64.182  -49.682 1.00 70.42  ? 177 GLU   A N     1 
ATOM   1310 C CA    . GLU   A 1 185 ? -15.832 -64.641  -48.304 1.00 68.00  ? 177 GLU   A CA    1 
ATOM   1311 C C     . GLU   A 1 185 ? -14.416 -64.504  -47.749 1.00 64.42  ? 177 GLU   A C     1 
ATOM   1312 O O     . GLU   A 1 185 ? -13.465 -64.977  -48.369 1.00 64.25  ? 177 GLU   A O     1 
ATOM   1313 C CB    . GLU   A 1 185 ? -16.268 -66.108  -48.283 1.00 67.56  ? 177 GLU   A CB    1 
ATOM   1314 C CG    . GLU   A 1 185 ? -16.230 -66.752  -46.900 1.00 68.70  ? 177 GLU   A CG    1 
ATOM   1315 C CD    . GLU   A 1 185 ? -16.037 -68.257  -46.923 1.00 70.16  ? 177 GLU   A CD    1 
ATOM   1316 O OE1   . GLU   A 1 185 ? -15.080 -68.713  -47.585 1.00 71.58  ? 177 GLU   A OE1   1 
ATOM   1317 O OE2   . GLU   A 1 185 ? -16.825 -68.971  -46.267 1.00 70.13  ? 177 GLU   A OE2   1 
ATOM   1318 N N     . GLU   A 1 186 ? -14.285 -63.837  -46.594 1.00 58.78  ? 178 GLU   A N     1 
ATOM   1319 C CA    . GLU   A 1 186 ? -13.138 -64.046  -45.723 1.00 55.20  ? 178 GLU   A CA    1 
ATOM   1320 C C     . GLU   A 1 186 ? -13.624 -64.799  -44.487 1.00 50.01  ? 178 GLU   A C     1 
ATOM   1321 O O     . GLU   A 1 186 ? -14.457 -64.293  -43.740 1.00 47.99  ? 178 GLU   A O     1 
ATOM   1322 C CB    . GLU   A 1 186 ? -12.399 -62.782  -45.279 1.00 55.92  ? 178 GLU   A CB    1 
ATOM   1323 C CG    . GLU   A 1 186 ? -11.653 -62.063  -46.400 1.00 56.09  ? 178 GLU   A CG    1 
ATOM   1324 C CD    . GLU   A 1 186 ? -12.246 -60.718  -46.785 1.00 56.52  ? 178 GLU   A CD    1 
ATOM   1325 O OE1   . GLU   A 1 186 ? -12.229 -59.809  -45.927 1.00 55.99  ? 178 GLU   A OE1   1 
ATOM   1326 O OE2   . GLU   A 1 186 ? -12.716 -60.573  -47.932 1.00 56.50  ? 178 GLU   A OE2   1 
ATOM   1327 N N     . TYR   A 1 187 ? -13.092 -66.011  -44.291 1.00 44.95  ? 179 TYR   A N     1 
ATOM   1328 C CA    . TYR   A 1 187 ? -13.541 -66.894  -43.227 1.00 41.54  ? 179 TYR   A CA    1 
ATOM   1329 C C     . TYR   A 1 187 ? -13.306 -66.221  -41.876 1.00 38.25  ? 179 TYR   A C     1 
ATOM   1330 O O     . TYR   A 1 187 ? -14.234 -66.081  -41.083 1.00 38.10  ? 179 TYR   A O     1 
ATOM   1331 C CB    . TYR   A 1 187 ? -12.819 -68.239  -43.354 1.00 40.07  ? 179 TYR   A CB    1 
ATOM   1332 C CG    . TYR   A 1 187 ? -13.380 -69.329  -42.452 1.00 39.00  ? 179 TYR   A CG    1 
ATOM   1333 C CD1   . TYR   A 1 187 ? -14.540 -70.013  -42.797 1.00 38.05  ? 179 TYR   A CD1   1 
ATOM   1334 C CD2   . TYR   A 1 187 ? -12.753 -69.672  -41.257 1.00 39.22  ? 179 TYR   A CD2   1 
ATOM   1335 C CE1   . TYR   A 1 187 ? -15.061 -71.005  -41.982 1.00 38.22  ? 179 TYR   A CE1   1 
ATOM   1336 C CE2   . TYR   A 1 187 ? -13.264 -70.663  -40.434 1.00 37.98  ? 179 TYR   A CE2   1 
ATOM   1337 C CZ    . TYR   A 1 187 ? -14.422 -71.329  -40.797 1.00 38.03  ? 179 TYR   A CZ    1 
ATOM   1338 O OH    . TYR   A 1 187 ? -14.941 -72.307  -39.998 1.00 38.60  ? 179 TYR   A OH    1 
ATOM   1339 N N     . SER   A 1 188 ? -12.062 -65.787  -41.646 1.00 35.10  ? 180 SER   A N     1 
ATOM   1340 C CA    . SER   A 1 188 ? -11.659 -65.187  -40.385 1.00 33.80  ? 180 SER   A CA    1 
ATOM   1341 C C     . SER   A 1 188 ? -12.163 -63.749  -40.283 1.00 31.99  ? 180 SER   A C     1 
ATOM   1342 O O     . SER   A 1 188 ? -12.518 -63.294  -39.197 1.00 30.53  ? 180 SER   A O     1 
ATOM   1343 C CB    . SER   A 1 188 ? -10.163 -65.256  -40.220 1.00 34.05  ? 180 SER   A CB    1 
ATOM   1344 O OG    . SER   A 1 188 ? -9.702  -66.592  -40.362 1.00 34.40  ? 180 SER   A OG    1 
ATOM   1345 N N     . GLY   A 1 189 ? -12.188 -63.042  -41.420 1.00 30.46  ? 181 GLY   A N     1 
ATOM   1346 C CA    . GLY   A 1 189 ? -12.712 -61.686  -41.482 1.00 29.75  ? 181 GLY   A CA    1 
ATOM   1347 C C     . GLY   A 1 189 ? -14.149 -61.608  -40.967 1.00 29.52  ? 181 GLY   A C     1 
ATOM   1348 O O     . GLY   A 1 189 ? -14.510 -60.663  -40.268 1.00 29.00  ? 181 GLY   A O     1 
ATOM   1349 N N     . GLU   A 1 190 ? -14.951 -62.628  -41.298 1.00 29.43  ? 182 GLU   A N     1 
ATOM   1350 C CA    . GLU   A 1 190 ? -16.349 -62.683  -40.898 1.00 30.12  ? 182 GLU   A CA    1 
ATOM   1351 C C     . GLU   A 1 190 ? -16.491 -62.956  -39.399 1.00 29.74  ? 182 GLU   A C     1 
ATOM   1352 O O     . GLU   A 1 190 ? -17.607 -62.933  -38.884 1.00 30.16  ? 182 GLU   A O     1 
ATOM   1353 C CB    . GLU   A 1 190 ? -17.079 -63.763  -41.699 1.00 31.31  ? 182 GLU   A CB    1 
ATOM   1354 C CG    . GLU   A 1 190 ? -17.237 -63.436  -43.184 1.00 32.07  ? 182 GLU   A CG    1 
ATOM   1355 C CD    . GLU   A 1 190 ? -17.871 -64.541  -44.017 1.00 32.89  ? 182 GLU   A CD    1 
ATOM   1356 O OE1   . GLU   A 1 190 ? -18.360 -65.531  -43.428 1.00 32.66  ? 182 GLU   A OE1   1 
ATOM   1357 O OE2   . GLU   A 1 190 ? -17.875 -64.416  -45.264 1.00 34.11  ? 182 GLU   A OE2   1 
ATOM   1358 N N     . GLU   A 1 191 ? -15.370 -63.215  -38.706 1.00 29.05  ? 183 GLU   A N     1 
ATOM   1359 C CA    . GLU   A 1 191 ? -15.376 -63.545  -37.286 1.00 28.51  ? 183 GLU   A CA    1 
ATOM   1360 C C     . GLU   A 1 191 ? -14.701 -62.446  -36.463 1.00 28.12  ? 183 GLU   A C     1 
ATOM   1361 O O     . GLU   A 1 191 ? -14.311 -62.684  -35.323 1.00 29.43  ? 183 GLU   A O     1 
ATOM   1362 C CB    . GLU   A 1 191 ? -14.593 -64.832  -37.020 1.00 28.47  ? 183 GLU   A CB    1 
ATOM   1363 C CG    . GLU   A 1 191 ? -15.137 -66.084  -37.706 1.00 28.42  ? 183 GLU   A CG    1 
ATOM   1364 C CD    . GLU   A 1 191 ? -14.227 -67.292  -37.540 1.00 28.27  ? 183 GLU   A CD    1 
ATOM   1365 O OE1   . GLU   A 1 191 ? -13.090 -67.086  -37.058 1.00 28.67  ? 183 GLU   A OE1   1 
ATOM   1366 O OE2   . GLU   A 1 191 ? -14.637 -68.432  -37.859 1.00 26.96  ? 183 GLU   A OE2   1 
ATOM   1367 N N     . LYS   A 1 192 ? -14.582 -61.238  -37.023 1.00 27.36  ? 184 LYS   A N     1 
ATOM   1368 C CA    . LYS   A 1 192 ? -13.734 -60.213  -36.437 1.00 26.70  ? 184 LYS   A CA    1 
ATOM   1369 C C     . LYS   A 1 192 ? -14.293 -59.726  -35.102 1.00 25.98  ? 184 LYS   A C     1 
ATOM   1370 O O     . LYS   A 1 192 ? -13.523 -59.267  -34.261 1.00 26.74  ? 184 LYS   A O     1 
ATOM   1371 C CB    . LYS   A 1 192 ? -13.528 -59.024  -37.383 1.00 26.87  ? 184 LYS   A CB    1 
ATOM   1372 C CG    . LYS   A 1 192 ? -14.784 -58.248  -37.758 1.00 27.51  ? 184 LYS   A CG    1 
ATOM   1373 C CD    . LYS   A 1 192 ? -14.521 -56.938  -38.498 1.00 27.80  ? 184 LYS   A CD    1 
ATOM   1374 C CE    . LYS   A 1 192 ? -13.765 -57.101  -39.782 1.00 27.80  ? 184 LYS   A CE    1 
ATOM   1375 N NZ    . LYS   A 1 192 ? -14.464 -57.966  -40.736 1.00 27.71  ? 184 LYS   A NZ    1 
ATOM   1376 N N     . THR   A 1 193 ? -15.618 -59.802  -34.909 1.00 24.94  ? 185 THR   A N     1 
ATOM   1377 C CA    . THR   A 1 193 ? -16.230 -59.248  -33.707 1.00 24.36  ? 185 THR   A CA    1 
ATOM   1378 C C     . THR   A 1 193 ? -15.936 -60.155  -32.515 1.00 23.86  ? 185 THR   A C     1 
ATOM   1379 O O     . THR   A 1 193 ? -15.817 -59.667  -31.394 1.00 23.12  ? 185 THR   A O     1 
ATOM   1380 C CB    . THR   A 1 193 ? -17.730 -59.012  -33.887 1.00 24.00  ? 185 THR   A CB    1 
ATOM   1381 O OG1   . THR   A 1 193 ? -18.354 -60.276  -34.084 1.00 24.09  ? 185 THR   A OG1   1 
ATOM   1382 C CG2   . THR   A 1 193 ? -18.028 -58.082  -35.049 1.00 24.05  ? 185 THR   A CG2   1 
ATOM   1383 N N     . TRP   A 1 194 ? -15.807 -61.466  -32.758 1.00 23.91  ? 186 TRP   A N     1 
ATOM   1384 C CA    . TRP   A 1 194 ? -15.365 -62.375  -31.714 1.00 24.32  ? 186 TRP   A CA    1 
ATOM   1385 C C     . TRP   A 1 194 ? -13.963 -61.989  -31.243 1.00 24.01  ? 186 TRP   A C     1 
ATOM   1386 O O     . TRP   A 1 194 ? -13.676 -62.067  -30.052 1.00 23.29  ? 186 TRP   A O     1 
ATOM   1387 C CB    . TRP   A 1 194 ? -15.402 -63.843  -32.165 1.00 24.85  ? 186 TRP   A CB    1 
ATOM   1388 C CG    . TRP   A 1 194 ? -14.967 -64.781  -31.070 1.00 25.53  ? 186 TRP   A CG    1 
ATOM   1389 C CD1   . TRP   A 1 194 ? -15.757 -65.375  -30.130 1.00 25.70  ? 186 TRP   A CD1   1 
ATOM   1390 C CD2   . TRP   A 1 194 ? -13.613 -65.178  -30.764 1.00 26.56  ? 186 TRP   A CD2   1 
ATOM   1391 N NE1   . TRP   A 1 194 ? -14.997 -66.127  -29.275 1.00 25.93  ? 186 TRP   A NE1   1 
ATOM   1392 C CE2   . TRP   A 1 194 ? -13.679 -66.023  -29.634 1.00 26.59  ? 186 TRP   A CE2   1 
ATOM   1393 C CE3   . TRP   A 1 194 ? -12.362 -64.905  -31.331 1.00 27.27  ? 186 TRP   A CE3   1 
ATOM   1394 C CZ2   . TRP   A 1 194 ? -12.540 -66.596  -29.070 1.00 27.10  ? 186 TRP   A CZ2   1 
ATOM   1395 C CZ3   . TRP   A 1 194 ? -11.237 -65.470  -30.770 1.00 27.35  ? 186 TRP   A CZ3   1 
ATOM   1396 C CH2   . TRP   A 1 194 ? -11.327 -66.298  -29.651 1.00 27.11  ? 186 TRP   A CH2   1 
ATOM   1397 N N     A MET   A 1 195 ? -13.102 -61.572  -32.180 0.45 23.86  ? 187 MET   A N     1 
ATOM   1398 N N     B MET   A 1 195 ? -13.107 -61.593  -32.194 0.55 23.97  ? 187 MET   A N     1 
ATOM   1399 C CA    A MET   A 1 195 ? -11.729 -61.219  -31.854 0.45 23.98  ? 187 MET   A CA    1 
ATOM   1400 C CA    B MET   A 1 195 ? -11.735 -61.198  -31.907 0.55 24.20  ? 187 MET   A CA    1 
ATOM   1401 C C     A MET   A 1 195 ? -11.691 -59.886  -31.102 0.45 23.94  ? 187 MET   A C     1 
ATOM   1402 C C     B MET   A 1 195 ? -11.720 -59.908  -31.084 0.55 24.06  ? 187 MET   A C     1 
ATOM   1403 O O     A MET   A 1 195 ? -10.788 -59.664  -30.297 0.45 23.66  ? 187 MET   A O     1 
ATOM   1404 O O     B MET   A 1 195 ? -10.876 -59.747  -30.205 0.55 23.63  ? 187 MET   A O     1 
ATOM   1405 C CB    A MET   A 1 195 ? -10.857 -61.153  -33.113 0.45 23.89  ? 187 MET   A CB    1 
ATOM   1406 C CB    B MET   A 1 195 ? -10.939 -61.062  -33.213 0.55 24.30  ? 187 MET   A CB    1 
ATOM   1407 C CG    A MET   A 1 195 ? -9.366  -61.259  -32.832 0.45 23.97  ? 187 MET   A CG    1 
ATOM   1408 C CG    B MET   A 1 195 ? -9.609  -60.331  -33.099 0.55 24.57  ? 187 MET   A CG    1 
ATOM   1409 S SD    A MET   A 1 195 ? -8.846  -62.892  -32.261 0.45 24.22  ? 187 MET   A SD    1 
ATOM   1410 S SD    B MET   A 1 195 ? -9.698  -58.598  -33.598 0.55 25.39  ? 187 MET   A SD    1 
ATOM   1411 C CE    A MET   A 1 195 ? -8.906  -63.852  -33.780 0.45 23.95  ? 187 MET   A CE    1 
ATOM   1412 C CE    B MET   A 1 195 ? -10.073 -58.762  -35.350 0.55 24.63  ? 187 MET   A CE    1 
ATOM   1413 N N     . TRP   A 1 196 ? -12.665 -59.003  -31.366 1.00 23.82  ? 188 TRP   A N     1 
ATOM   1414 C CA    . TRP   A 1 196 ? -12.830 -57.784  -30.585 1.00 23.60  ? 188 TRP   A CA    1 
ATOM   1415 C C     . TRP   A 1 196 ? -13.036 -58.141  -29.114 1.00 23.53  ? 188 TRP   A C     1 
ATOM   1416 O O     . TRP   A 1 196 ? -12.378 -57.594  -28.228 1.00 23.37  ? 188 TRP   A O     1 
ATOM   1417 C CB    . TRP   A 1 196 ? -14.031 -56.968  -31.086 1.00 23.70  ? 188 TRP   A CB    1 
ATOM   1418 C CG    . TRP   A 1 196 ? -13.903 -56.408  -32.477 1.00 23.78  ? 188 TRP   A CG    1 
ATOM   1419 C CD1   . TRP   A 1 196 ? -12.873 -56.573  -33.354 1.00 24.00  ? 188 TRP   A CD1   1 
ATOM   1420 C CD2   . TRP   A 1 196 ? -14.893 -55.613  -33.164 1.00 23.60  ? 188 TRP   A CD2   1 
ATOM   1421 N NE1   . TRP   A 1 196 ? -13.135 -55.914  -34.525 1.00 23.96  ? 188 TRP   A NE1   1 
ATOM   1422 C CE2   . TRP   A 1 196 ? -14.370 -55.324  -34.444 1.00 23.91  ? 188 TRP   A CE2   1 
ATOM   1423 C CE3   . TRP   A 1 196 ? -16.158 -55.120  -32.826 1.00 23.61  ? 188 TRP   A CE3   1 
ATOM   1424 C CZ2   . TRP   A 1 196 ? -15.071 -54.561  -35.377 1.00 23.56  ? 188 TRP   A CZ2   1 
ATOM   1425 C CZ3   . TRP   A 1 196 ? -16.851 -54.370  -33.752 1.00 23.97  ? 188 TRP   A CZ3   1 
ATOM   1426 C CH2   . TRP   A 1 196 ? -16.313 -54.096  -35.010 1.00 23.34  ? 188 TRP   A CH2   1 
ATOM   1427 N N     . TRP   A 1 197 ? -13.978 -59.063  -28.889 1.00 22.91  ? 189 TRP   A N     1 
ATOM   1428 C CA    . TRP   A 1 197 ? -14.323 -59.552  -27.566 1.00 22.43  ? 189 TRP   A CA    1 
ATOM   1429 C C     . TRP   A 1 197 ? -13.149 -60.307  -26.946 1.00 22.21  ? 189 TRP   A C     1 
ATOM   1430 O O     . TRP   A 1 197 ? -12.809 -60.075  -25.788 1.00 21.98  ? 189 TRP   A O     1 
ATOM   1431 C CB    . TRP   A 1 197 ? -15.580 -60.430  -27.658 1.00 22.39  ? 189 TRP   A CB    1 
ATOM   1432 C CG    . TRP   A 1 197 ? -15.755 -61.405  -26.524 1.00 22.33  ? 189 TRP   A CG    1 
ATOM   1433 C CD1   . TRP   A 1 197 ? -15.655 -62.763  -26.600 1.00 22.40  ? 189 TRP   A CD1   1 
ATOM   1434 C CD2   . TRP   A 1 197 ? -16.048 -61.099  -25.143 1.00 22.38  ? 189 TRP   A CD2   1 
ATOM   1435 N NE1   . TRP   A 1 197 ? -15.882 -63.324  -25.373 1.00 22.70  ? 189 TRP   A NE1   1 
ATOM   1436 C CE2   . TRP   A 1 197 ? -16.121 -62.332  -24.459 1.00 22.54  ? 189 TRP   A CE2   1 
ATOM   1437 C CE3   . TRP   A 1 197 ? -16.258 -59.917  -24.423 1.00 22.93  ? 189 TRP   A CE3   1 
ATOM   1438 C CZ2   . TRP   A 1 197 ? -16.387 -62.410  -23.093 1.00 22.80  ? 189 TRP   A CZ2   1 
ATOM   1439 C CZ3   . TRP   A 1 197 ? -16.521 -59.996  -23.073 1.00 22.97  ? 189 TRP   A CZ3   1 
ATOM   1440 C CH2   . TRP   A 1 197 ? -16.579 -61.227  -22.417 1.00 23.14  ? 189 TRP   A CH2   1 
ATOM   1441 N N     . HIS   A 1 198 ? -12.537 -61.205  -27.725 1.00 21.85  ? 190 HIS   A N     1 
ATOM   1442 C CA    . HIS   A 1 198 ? -11.479 -62.064  -27.221 1.00 22.19  ? 190 HIS   A CA    1 
ATOM   1443 C C     . HIS   A 1 198 ? -10.319 -61.232  -26.684 1.00 22.89  ? 190 HIS   A C     1 
ATOM   1444 O O     . HIS   A 1 198 ? -9.856  -61.445  -25.565 1.00 23.33  ? 190 HIS   A O     1 
ATOM   1445 C CB    . HIS   A 1 198 ? -10.959 -62.998  -28.315 1.00 21.86  ? 190 HIS   A CB    1 
ATOM   1446 C CG    . HIS   A 1 198 ? -9.931  -63.950  -27.815 1.00 21.50  ? 190 HIS   A CG    1 
ATOM   1447 N ND1   . HIS   A 1 198 ? -10.179 -64.823  -26.778 1.00 21.31  ? 190 HIS   A ND1   1 
ATOM   1448 C CD2   . HIS   A 1 198 ? -8.680  -64.188  -28.215 1.00 21.36  ? 190 HIS   A CD2   1 
ATOM   1449 C CE1   . HIS   A 1 198 ? -9.097  -65.554  -26.560 1.00 21.42  ? 190 HIS   A CE1   1 
ATOM   1450 N NE2   . HIS   A 1 198 ? -8.172  -65.180  -27.421 1.00 21.50  ? 190 HIS   A NE2   1 
ATOM   1451 N N     . ASN   A 1 199 ? -9.838  -60.300  -27.509 1.00 23.12  ? 191 ASN   A N     1 
ATOM   1452 C CA    . ASN   A 1 199 ? -8.749  -59.424  -27.117 1.00 23.38  ? 191 ASN   A CA    1 
ATOM   1453 C C     . ASN   A 1 199 ? -9.124  -58.674  -25.845 1.00 23.09  ? 191 ASN   A C     1 
ATOM   1454 O O     . ASN   A 1 199 ? -8.313  -58.563  -24.930 1.00 24.07  ? 191 ASN   A O     1 
ATOM   1455 C CB    . ASN   A 1 199 ? -8.394  -58.443  -28.227 1.00 23.79  ? 191 ASN   A CB    1 
ATOM   1456 C CG    . ASN   A 1 199 ? -7.807  -59.133  -29.434 1.00 24.58  ? 191 ASN   A CG    1 
ATOM   1457 O OD1   . ASN   A 1 199 ? -7.440  -60.311  -29.370 1.00 26.14  ? 191 ASN   A OD1   1 
ATOM   1458 N ND2   . ASN   A 1 199 ? -7.709  -58.418  -30.543 1.00 24.97  ? 191 ASN   A ND2   1 
ATOM   1459 N N     . PHE   A 1 200 ? -10.360 -58.168  -25.801 1.00 22.34  ? 192 PHE   A N     1 
ATOM   1460 C CA    . PHE   A 1 200 ? -10.813 -57.341  -24.697 1.00 21.39  ? 192 PHE   A CA    1 
ATOM   1461 C C     . PHE   A 1 200 ? -10.753 -58.117  -23.383 1.00 21.38  ? 192 PHE   A C     1 
ATOM   1462 O O     . PHE   A 1 200 ? -10.193 -57.635  -22.402 1.00 21.71  ? 192 PHE   A O     1 
ATOM   1463 C CB    . PHE   A 1 200 ? -12.239 -56.831  -24.920 1.00 21.12  ? 192 PHE   A CB    1 
ATOM   1464 C CG    . PHE   A 1 200 ? -12.665 -55.849  -23.841 1.00 20.89  ? 192 PHE   A CG    1 
ATOM   1465 C CD1   . PHE   A 1 200 ? -12.145 -54.562  -23.817 1.00 21.19  ? 192 PHE   A CD1   1 
ATOM   1466 C CD2   . PHE   A 1 200 ? -13.554 -56.222  -22.842 1.00 20.82  ? 192 PHE   A CD2   1 
ATOM   1467 C CE1   . PHE   A 1 200 ? -12.512 -53.669  -22.824 1.00 21.31  ? 192 PHE   A CE1   1 
ATOM   1468 C CE2   . PHE   A 1 200 ? -13.916 -55.324  -21.851 1.00 20.95  ? 192 PHE   A CE2   1 
ATOM   1469 C CZ    . PHE   A 1 200 ? -13.396 -54.051  -21.845 1.00 20.97  ? 192 PHE   A CZ    1 
ATOM   1470 N N     A ARG   A 1 201 ? -11.333 -59.320  -23.374 0.20 21.48  ? 193 ARG   A N     1 
ATOM   1471 N N     B ARG   A 1 201 ? -11.351 -59.311  -23.375 0.80 21.13  ? 193 ARG   A N     1 
ATOM   1472 C CA    A ARG   A 1 201 ? -11.428 -60.110  -22.158 0.20 21.52  ? 193 ARG   A CA    1 
ATOM   1473 C CA    B ARG   A 1 201 ? -11.441 -60.123  -22.173 0.80 21.01  ? 193 ARG   A CA    1 
ATOM   1474 C C     A ARG   A 1 201 ? -10.061 -60.679  -21.781 0.20 21.26  ? 193 ARG   A C     1 
ATOM   1475 C C     B ARG   A 1 201 ? -10.062 -60.657  -21.785 0.80 21.03  ? 193 ARG   A C     1 
ATOM   1476 O O     A ARG   A 1 201 ? -9.825  -60.974  -20.611 0.20 21.26  ? 193 ARG   A O     1 
ATOM   1477 O O     B ARG   A 1 201 ? -9.817  -60.897  -20.606 0.80 21.08  ? 193 ARG   A O     1 
ATOM   1478 C CB    A ARG   A 1 201 ? -12.464 -61.223  -22.332 0.20 21.80  ? 193 ARG   A CB    1 
ATOM   1479 C CB    B ARG   A 1 201 ? -12.481 -61.235  -22.349 0.80 20.90  ? 193 ARG   A CB    1 
ATOM   1480 C CG    A ARG   A 1 201 ? -12.080 -62.280  -23.355 0.20 22.04  ? 193 ARG   A CG    1 
ATOM   1481 C CG    B ARG   A 1 201 ? -12.206 -62.243  -23.454 0.80 20.72  ? 193 ARG   A CG    1 
ATOM   1482 C CD    A ARG   A 1 201 ? -13.272 -63.173  -23.598 0.20 22.30  ? 193 ARG   A CD    1 
ATOM   1483 C CD    B ARG   A 1 201 ? -11.379 -63.445  -23.022 0.80 20.58  ? 193 ARG   A CD    1 
ATOM   1484 N NE    A ARG   A 1 201 ? -13.120 -64.171  -24.661 0.20 22.51  ? 193 ARG   A NE    1 
ATOM   1485 N NE    B ARG   A 1 201 ? -11.523 -64.503  -24.026 0.80 20.54  ? 193 ARG   A NE    1 
ATOM   1486 C CZ    A ARG   A 1 201 ? -12.515 -65.337  -24.514 0.20 22.67  ? 193 ARG   A CZ    1 
ATOM   1487 C CZ    B ARG   A 1 201 ? -12.659 -65.127  -24.321 0.80 20.62  ? 193 ARG   A CZ    1 
ATOM   1488 N NH1   A ARG   A 1 201 ? -11.924 -65.627  -23.374 0.20 22.66  ? 193 ARG   A NH1   1 
ATOM   1489 N NH1   B ARG   A 1 201 ? -13.696 -65.070  -23.501 0.80 20.21  ? 193 ARG   A NH1   1 
ATOM   1490 N NH2   A ARG   A 1 201 ? -12.500 -66.208  -25.506 0.20 22.84  ? 193 ARG   A NH2   1 
ATOM   1491 N NH2   B ARG   A 1 201 ? -12.739 -65.844  -25.427 0.80 21.01  ? 193 ARG   A NH2   1 
ATOM   1492 N N     . THR   A 1 202 ? -9.171  -60.839  -22.771 1.00 20.92  ? 194 THR   A N     1 
ATOM   1493 C CA    . THR   A 1 202 ? -7.806  -61.274  -22.504 1.00 20.73  ? 194 THR   A CA    1 
ATOM   1494 C C     . THR   A 1 202 ? -7.058  -60.140  -21.806 1.00 21.13  ? 194 THR   A C     1 
ATOM   1495 O O     . THR   A 1 202 ? -6.434  -60.353  -20.769 1.00 21.54  ? 194 THR   A O     1 
ATOM   1496 C CB    . THR   A 1 202 ? -7.106  -61.720  -23.789 1.00 20.44  ? 194 THR   A CB    1 
ATOM   1497 O OG1   . THR   A 1 202 ? -7.703  -62.969  -24.121 1.00 20.24  ? 194 THR   A OG1   1 
ATOM   1498 C CG2   . THR   A 1 202 ? -5.617  -61.951  -23.608 1.00 20.20  ? 194 THR   A CG2   1 
ATOM   1499 N N     . LEU   A 1 203 ? -7.153  -58.930  -22.366 1.00 21.51  ? 195 LEU   A N     1 
ATOM   1500 C CA    . LEU   A 1 203 ? -6.579  -57.746  -21.746 1.00 21.83  ? 195 LEU   A CA    1 
ATOM   1501 C C     . LEU   A 1 203 ? -7.046  -57.625  -20.293 1.00 22.28  ? 195 LEU   A C     1 
ATOM   1502 O O     . LEU   A 1 203 ? -6.253  -57.270  -19.426 1.00 21.22  ? 195 LEU   A O     1 
ATOM   1503 C CB    . LEU   A 1 203 ? -6.930  -56.493  -22.550 1.00 21.91  ? 195 LEU   A CB    1 
ATOM   1504 C CG    . LEU   A 1 203 ? -6.089  -56.215  -23.802 1.00 22.12  ? 195 LEU   A CG    1 
ATOM   1505 C CD1   . LEU   A 1 203 ? -6.666  -55.032  -24.555 1.00 22.19  ? 195 LEU   A CD1   1 
ATOM   1506 C CD2   . LEU   A 1 203 ? -4.626  -55.948  -23.486 1.00 22.20  ? 195 LEU   A CD2   1 
ATOM   1507 N N     . CYS   A 1 204 ? -8.327  -57.931  -20.035 1.00 23.35  ? 196 CYS   A N     1 
ATOM   1508 C CA    . CYS   A 1 204 ? -8.931  -57.753  -18.721 1.00 24.20  ? 196 CYS   A CA    1 
ATOM   1509 C C     . CYS   A 1 204 ? -8.719  -58.971  -17.820 1.00 24.75  ? 196 CYS   A C     1 
ATOM   1510 O O     . CYS   A 1 204 ? -9.303  -59.039  -16.742 1.00 24.59  ? 196 CYS   A O     1 
ATOM   1511 C CB    . CYS   A 1 204 ? -10.429 -57.482  -18.830 1.00 24.71  ? 196 CYS   A CB    1 
ATOM   1512 S SG    . CYS   A 1 204 ? -10.836 -55.864  -19.535 1.00 25.70  ? 196 CYS   A SG    1 
ATOM   1513 N N     . ASP   A 1 205 ? -7.916  -59.942  -18.271 1.00 25.46  ? 197 ASP   A N     1 
ATOM   1514 C CA    . ASP   A 1 205 ? -7.459  -61.036  -17.426 1.00 25.79  ? 197 ASP   A CA    1 
ATOM   1515 C C     . ASP   A 1 205 ? -8.630  -61.946  -17.055 1.00 24.59  ? 197 ASP   A C     1 
ATOM   1516 O O     . ASP   A 1 205 ? -8.652  -62.521  -15.970 1.00 24.17  ? 197 ASP   A O     1 
ATOM   1517 C CB    . ASP   A 1 205 ? -6.721  -60.500  -16.207 1.00 27.19  ? 197 ASP   A CB    1 
ATOM   1518 C CG    . ASP   A 1 205 ? -5.742  -61.452  -15.534 1.00 28.75  ? 197 ASP   A CG    1 
ATOM   1519 O OD1   . ASP   A 1 205 ? -5.547  -62.572  -16.051 1.00 29.36  ? 197 ASP   A OD1   1 
ATOM   1520 O OD2   . ASP   A 1 205 ? -5.178  -61.056  -14.491 1.00 31.30  ? 197 ASP   A OD2   1 
ATOM   1521 N N     . TYR   A 1 206 ? -9.590  -62.084  -17.976 1.00 23.72  ? 198 TYR   A N     1 
ATOM   1522 C CA    . TYR   A 1 206 ? -10.698 -63.015  -17.827 1.00 23.14  ? 198 TYR   A CA    1 
ATOM   1523 C C     . TYR   A 1 206 ? -11.464 -62.738  -16.536 1.00 22.44  ? 198 TYR   A C     1 
ATOM   1524 O O     . TYR   A 1 206 ? -11.865 -63.668  -15.844 1.00 22.99  ? 198 TYR   A O     1 
ATOM   1525 C CB    . TYR   A 1 206 ? -10.196 -64.463  -17.849 1.00 22.88  ? 198 TYR   A CB    1 
ATOM   1526 C CG    . TYR   A 1 206 ? -9.829  -65.027  -19.213 1.00 22.66  ? 198 TYR   A CG    1 
ATOM   1527 C CD1   . TYR   A 1 206 ? -8.676  -64.626  -19.874 1.00 22.82  ? 198 TYR   A CD1   1 
ATOM   1528 C CD2   . TYR   A 1 206 ? -10.613 -66.003  -19.814 1.00 23.00  ? 198 TYR   A CD2   1 
ATOM   1529 C CE1   . TYR   A 1 206 ? -8.332  -65.152  -21.108 1.00 22.97  ? 198 TYR   A CE1   1 
ATOM   1530 C CE2   . TYR   A 1 206 ? -10.277 -66.545  -21.043 1.00 23.02  ? 198 TYR   A CE2   1 
ATOM   1531 C CZ    . TYR   A 1 206 ? -9.135  -66.115  -21.695 1.00 23.16  ? 198 TYR   A CZ    1 
ATOM   1532 O OH    . TYR   A 1 206 ? -8.800  -66.646  -22.908 1.00 23.45  ? 198 TYR   A OH    1 
ATOM   1533 N N     . SER   A 1 207 ? -11.689 -61.461  -16.217 1.00 22.35  ? 199 SER   A N     1 
ATOM   1534 C CA    . SER   A 1 207 ? -12.521 -61.123  -15.076 1.00 22.58  ? 199 SER   A CA    1 
ATOM   1535 C C     . SER   A 1 207 ? -13.874 -61.806  -15.229 1.00 23.21  ? 199 SER   A C     1 
ATOM   1536 O O     . SER   A 1 207 ? -14.475 -61.752  -16.296 1.00 22.57  ? 199 SER   A O     1 
ATOM   1537 C CB    . SER   A 1 207 ? -12.696 -59.639  -14.922 1.00 22.36  ? 199 SER   A CB    1 
ATOM   1538 O OG    . SER   A 1 207 ? -13.755 -59.353  -14.016 1.00 22.03  ? 199 SER   A OG    1 
ATOM   1539 N N     . LYS   A 1 208 ? -14.355 -62.417  -14.142 1.00 24.47  ? 200 LYS   A N     1 
ATOM   1540 C CA    . LYS   A 1 208 ? -15.659 -63.063  -14.139 1.00 25.79  ? 200 LYS   A CA    1 
ATOM   1541 C C     . LYS   A 1 208 ? -16.790 -62.032  -14.084 1.00 25.09  ? 200 LYS   A C     1 
ATOM   1542 O O     . LYS   A 1 208 ? -17.954 -62.397  -14.229 1.00 25.32  ? 200 LYS   A O     1 
ATOM   1543 C CB    . LYS   A 1 208 ? -15.775 -64.063  -12.982 1.00 27.40  ? 200 LYS   A CB    1 
ATOM   1544 C CG    . LYS   A 1 208 ? -15.575 -63.488  -11.589 1.00 29.11  ? 200 LYS   A CG    1 
ATOM   1545 C CD    . LYS   A 1 208 ? -15.839 -64.495  -10.475 1.00 30.85  ? 200 LYS   A CD    1 
ATOM   1546 C CE    . LYS   A 1 208 ? -15.478 -63.968  -9.119  1.00 32.10  ? 200 LYS   A CE    1 
ATOM   1547 N NZ    . LYS   A 1 208 ? -16.062 -62.646  -8.877  1.00 32.85  ? 200 LYS   A NZ    1 
ATOM   1548 N N     A ARG   A 1 209 ? -16.435 -60.755  -13.880 0.50 24.47  ? 201 ARG   A N     1 
ATOM   1549 N N     B ARG   A 1 209 ? -16.450 -60.756  -13.867 0.50 24.99  ? 201 ARG   A N     1 
ATOM   1550 C CA    A ARG   A 1 209 ? -17.398 -59.666  -13.848 0.50 24.35  ? 201 ARG   A CA    1 
ATOM   1551 C CA    B ARG   A 1 209 ? -17.450 -59.701  -13.853 0.50 25.24  ? 201 ARG   A CA    1 
ATOM   1552 C C     A ARG   A 1 209 ? -17.654 -59.100  -15.246 0.50 24.22  ? 201 ARG   A C     1 
ATOM   1553 C C     B ARG   A 1 209 ? -17.550 -59.035  -15.227 0.50 24.66  ? 201 ARG   A C     1 
ATOM   1554 O O     A ARG   A 1 209 ? -18.395 -58.129  -15.380 0.50 24.66  ? 201 ARG   A O     1 
ATOM   1555 O O     B ARG   A 1 209 ? -18.080 -57.931  -15.329 0.50 24.99  ? 201 ARG   A O     1 
ATOM   1556 C CB    A ARG   A 1 209 ? -16.891 -58.531  -12.953 0.50 24.43  ? 201 ARG   A CB    1 
ATOM   1557 C CB    B ARG   A 1 209 ? -17.131 -58.692  -12.744 0.50 26.10  ? 201 ARG   A CB    1 
ATOM   1558 C CG    A ARG   A 1 209 ? -16.762 -58.900  -11.483 0.50 24.42  ? 201 ARG   A CG    1 
ATOM   1559 C CG    B ARG   A 1 209 ? -17.056 -59.302  -11.350 0.50 26.78  ? 201 ARG   A CG    1 
ATOM   1560 C CD    A ARG   A 1 209 ? -16.204 -57.751  -10.656 0.50 24.60  ? 201 ARG   A CD    1 
ATOM   1561 C CD    B ARG   A 1 209 ? -17.111 -58.248  -10.252 0.50 27.70  ? 201 ARG   A CD    1 
ATOM   1562 N NE    A ARG   A 1 209 ? -17.040 -56.547  -10.718 0.50 24.55  ? 201 ARG   A NE    1 
ATOM   1563 N NE    B ARG   A 1 209 ? -16.354 -58.634  -9.055  0.50 28.26  ? 201 ARG   A NE    1 
ATOM   1564 C CZ    A ARG   A 1 209 ? -16.741 -55.407  -10.112 0.50 24.74  ? 201 ARG   A CZ    1 
ATOM   1565 C CZ    B ARG   A 1 209 ? -16.643 -59.646  -8.246  0.50 28.80  ? 201 ARG   A CZ    1 
ATOM   1566 N NH1   A ARG   A 1 209 ? -15.642 -55.317  -9.385  0.50 24.79  ? 201 ARG   A NH1   1 
ATOM   1567 N NH1   B ARG   A 1 209 ? -17.727 -60.373  -8.444  0.50 29.21  ? 201 ARG   A NH1   1 
ATOM   1568 N NH2   A ARG   A 1 209 ? -17.538 -54.361  -10.234 0.50 24.75  ? 201 ARG   A NH2   1 
ATOM   1569 N NH2   B ARG   A 1 209 ? -15.852 -59.913  -7.224  0.50 28.74  ? 201 ARG   A NH2   1 
ATOM   1570 N N     . ILE   A 1 210 ? -17.050 -59.704  -16.279 1.00 23.57  ? 202 ILE   A N     1 
ATOM   1571 C CA    . ILE   A 1 210 ? -17.170 -59.207  -17.645 1.00 22.51  ? 202 ILE   A CA    1 
ATOM   1572 C C     . ILE   A 1 210 ? -17.804 -60.295  -18.509 1.00 22.06  ? 202 ILE   A C     1 
ATOM   1573 O O     . ILE   A 1 210 ? -17.237 -61.372  -18.670 1.00 21.42  ? 202 ILE   A O     1 
ATOM   1574 C CB    . ILE   A 1 210 ? -15.805 -58.762  -18.204 1.00 22.01  ? 202 ILE   A CB    1 
ATOM   1575 C CG1   . ILE   A 1 210 ? -15.158 -57.677  -17.337 1.00 21.99  ? 202 ILE   A CG1   1 
ATOM   1576 C CG2   . ILE   A 1 210 ? -15.937 -58.312  -19.659 1.00 21.94  ? 202 ILE   A CG2   1 
ATOM   1577 C CD1   . ILE   A 1 210 ? -13.743 -57.307  -17.747 1.00 21.79  ? 202 ILE   A CD1   1 
ATOM   1578 N N     . ALA   A 1 211 ? -18.978 -59.983  -19.071 1.00 22.54  ? 203 ALA   A N     1 
ATOM   1579 C CA    . ALA   A 1 211 ? -19.732 -60.911  -19.897 1.00 23.33  ? 203 ALA   A CA    1 
ATOM   1580 C C     . ALA   A 1 211 ? -20.158 -60.224  -21.193 1.00 24.26  ? 203 ALA   A C     1 
ATOM   1581 O O     . ALA   A 1 211 ? -19.863 -59.047  -21.398 1.00 23.94  ? 203 ALA   A O     1 
ATOM   1582 C CB    . ALA   A 1 211 ? -20.925 -61.416  -19.121 1.00 23.59  ? 203 ALA   A CB    1 
ATOM   1583 N N     . VAL   A 1 212 ? -20.865 -60.975  -22.051 1.00 25.43  ? 204 VAL   A N     1 
ATOM   1584 C CA    . VAL   A 1 212 ? -21.250 -60.509  -23.374 1.00 26.57  ? 204 VAL   A CA    1 
ATOM   1585 C C     . VAL   A 1 212 ? -22.749 -60.214  -23.418 1.00 27.30  ? 204 VAL   A C     1 
ATOM   1586 O O     . VAL   A 1 212 ? -23.561 -60.989  -22.914 1.00 27.11  ? 204 VAL   A O     1 
ATOM   1587 C CB    . VAL   A 1 212 ? -20.883 -61.554  -24.444 1.00 26.45  ? 204 VAL   A CB    1 
ATOM   1588 C CG1   . VAL   A 1 212 ? -21.232 -61.076  -25.848 1.00 26.46  ? 204 VAL   A CG1   1 
ATOM   1589 C CG2   . VAL   A 1 212 ? -19.416 -61.951  -24.362 1.00 26.65  ? 204 VAL   A CG2   1 
ATOM   1590 N N     . ALA   A 1 213 ? -23.088 -59.083  -24.048 1.00 28.43  ? 205 ALA   A N     1 
ATOM   1591 C CA    . ALA   A 1 213 ? -24.428 -58.821  -24.548 1.00 28.71  ? 205 ALA   A CA    1 
ATOM   1592 C C     . ALA   A 1 213 ? -24.377 -58.852  -26.073 1.00 29.05  ? 205 ALA   A C     1 
ATOM   1593 O O     . ALA   A 1 213 ? -23.969 -57.875  -26.697 1.00 29.25  ? 205 ALA   A O     1 
ATOM   1594 C CB    . ALA   A 1 213 ? -24.932 -57.492  -24.028 1.00 28.28  ? 205 ALA   A CB    1 
ATOM   1595 N N     . LEU   A 1 214 ? -24.766 -59.989  -26.661 1.00 29.60  ? 206 LEU   A N     1 
ATOM   1596 C CA    . LEU   A 1 214 ? -24.550 -60.232  -28.079 1.00 30.80  ? 206 LEU   A CA    1 
ATOM   1597 C C     . LEU   A 1 214 ? -25.687 -59.605  -28.883 1.00 31.87  ? 206 LEU   A C     1 
ATOM   1598 O O     . LEU   A 1 214 ? -26.855 -59.913  -28.658 1.00 31.35  ? 206 LEU   A O     1 
ATOM   1599 C CB    . LEU   A 1 214 ? -24.441 -61.732  -28.347 1.00 30.42  ? 206 LEU   A CB    1 
ATOM   1600 C CG    . LEU   A 1 214 ? -24.067 -62.127  -29.779 1.00 31.16  ? 206 LEU   A CG    1 
ATOM   1601 C CD1   . LEU   A 1 214 ? -22.619 -61.783  -30.092 1.00 31.35  ? 206 LEU   A CD1   1 
ATOM   1602 C CD2   . LEU   A 1 214 ? -24.328 -63.603  -30.019 1.00 31.34  ? 206 LEU   A CD2   1 
ATOM   1603 N N     . GLU   A 1 215 ? -25.327 -58.745  -29.842 1.00 33.45  ? 207 GLU   A N     1 
ATOM   1604 C CA    . GLU   A 1 215 ? -26.313 -57.977  -30.583 1.00 35.46  ? 207 GLU   A CA    1 
ATOM   1605 C C     . GLU   A 1 215 ? -26.567 -58.623  -31.945 1.00 36.10  ? 207 GLU   A C     1 
ATOM   1606 O O     . GLU   A 1 215 ? -25.631 -58.912  -32.690 1.00 35.15  ? 207 GLU   A O     1 
ATOM   1607 C CB    . GLU   A 1 215 ? -25.862 -56.523  -30.687 1.00 36.27  ? 207 GLU   A CB    1 
ATOM   1608 C CG    . GLU   A 1 215 ? -27.001 -55.595  -31.096 1.00 37.99  ? 207 GLU   A CG    1 
ATOM   1609 C CD    . GLU   A 1 215 ? -26.748 -54.126  -30.827 1.00 39.27  ? 207 GLU   A CD    1 
ATOM   1610 O OE1   . GLU   A 1 215 ? -27.710 -53.341  -30.953 1.00 40.72  ? 207 GLU   A OE1   1 
ATOM   1611 O OE2   . GLU   A 1 215 ? -25.600 -53.768  -30.490 1.00 41.06  ? 207 GLU   A OE2   1 
ATOM   1612 N N     . ILE   A 1 216 ? -27.856 -58.817  -32.255 1.00 37.19  ? 208 ILE   A N     1 
ATOM   1613 C CA    . ILE   A 1 216 ? -28.300 -59.598  -33.400 1.00 38.45  ? 208 ILE   A CA    1 
ATOM   1614 C C     . ILE   A 1 216 ? -28.901 -58.658  -34.442 1.00 38.81  ? 208 ILE   A C     1 
ATOM   1615 O O     . ILE   A 1 216 ? -29.723 -57.809  -34.109 1.00 39.42  ? 208 ILE   A O     1 
ATOM   1616 C CB    . ILE   A 1 216 ? -29.315 -60.668  -32.951 1.00 39.24  ? 208 ILE   A CB    1 
ATOM   1617 C CG1   . ILE   A 1 216 ? -28.829 -61.432  -31.711 1.00 39.54  ? 208 ILE   A CG1   1 
ATOM   1618 C CG2   . ILE   A 1 216 ? -29.673 -61.614  -34.098 1.00 38.98  ? 208 ILE   A CG2   1 
ATOM   1619 C CD1   . ILE   A 1 216 ? -27.452 -62.059  -31.855 1.00 40.06  ? 208 ILE   A CD1   1 
ATOM   1620 N N     . GLY   A 1 217 ? -28.490 -58.834  -35.704 1.00 38.82  ? 209 GLY   A N     1 
ATOM   1621 C CA    . GLY   A 1 217 ? -28.936 -57.993  -36.804 1.00 39.22  ? 209 GLY   A CA    1 
ATOM   1622 C C     . GLY   A 1 217 ? -29.885 -58.738  -37.740 1.00 40.14  ? 209 GLY   A C     1 
ATOM   1623 O O     . GLY   A 1 217 ? -30.180 -59.916  -37.540 1.00 38.91  ? 209 GLY   A O     1 
ATOM   1624 N N     . ALA   A 1 218 ? -30.342 -58.026  -38.776 1.00 41.89  ? 210 ALA   A N     1 
ATOM   1625 C CA    . ALA   A 1 218 ? -31.354 -58.530  -39.689 1.00 42.66  ? 210 ALA   A CA    1 
ATOM   1626 C C     . ALA   A 1 218 ? -30.814 -59.709  -40.496 1.00 43.36  ? 210 ALA   A C     1 
ATOM   1627 O O     . ALA   A 1 218 ? -31.510 -60.707  -40.663 1.00 43.01  ? 210 ALA   A O     1 
ATOM   1628 C CB    . ALA   A 1 218 ? -31.834 -57.414  -40.591 1.00 42.14  ? 210 ALA   A CB    1 
ATOM   1629 N N     . ASP   A 1 219 ? -29.581 -59.586  -41.001 1.00 44.33  ? 211 ASP   A N     1 
ATOM   1630 C CA    . ASP   A 1 219 ? -28.958 -60.661  -41.758 1.00 45.77  ? 211 ASP   A CA    1 
ATOM   1631 C C     . ASP   A 1 219 ? -27.952 -61.382  -40.865 1.00 43.75  ? 211 ASP   A C     1 
ATOM   1632 O O     . ASP   A 1 219 ? -27.045 -60.762  -40.314 1.00 42.56  ? 211 ASP   A O     1 
ATOM   1633 C CB    . ASP   A 1 219 ? -28.386 -60.151  -43.072 1.00 48.69  ? 211 ASP   A CB    1 
ATOM   1634 C CG    . ASP   A 1 219 ? -29.428 -59.690  -44.084 1.00 52.07  ? 211 ASP   A CG    1 
ATOM   1635 O OD1   . ASP   A 1 219 ? -30.302 -60.512  -44.441 1.00 52.90  ? 211 ASP   A OD1   1 
ATOM   1636 O OD2   . ASP   A 1 219 ? -29.365 -58.511  -44.500 1.00 53.90  ? 211 ASP   A OD2   1 
ATOM   1637 N N     . LEU   A 1 220 ? -28.140 -62.699  -40.719 1.00 42.73  ? 212 LEU   A N     1 
ATOM   1638 C CA    . LEU   A 1 220 ? -27.277 -63.519  -39.886 1.00 42.05  ? 212 LEU   A CA    1 
ATOM   1639 C C     . LEU   A 1 220 ? -26.076 -63.983  -40.705 1.00 42.46  ? 212 LEU   A C     1 
ATOM   1640 O O     . LEU   A 1 220 ? -26.194 -64.237  -41.904 1.00 43.88  ? 212 LEU   A O     1 
ATOM   1641 C CB    . LEU   A 1 220 ? -28.052 -64.709  -39.320 1.00 41.51  ? 212 LEU   A CB    1 
ATOM   1642 C CG    . LEU   A 1 220 ? -29.258 -64.381  -38.434 1.00 41.65  ? 212 LEU   A CG    1 
ATOM   1643 C CD1   . LEU   A 1 220 ? -29.886 -65.663  -37.915 1.00 41.38  ? 212 LEU   A CD1   1 
ATOM   1644 C CD2   . LEU   A 1 220 ? -28.898 -63.467  -37.272 1.00 41.95  ? 212 LEU   A CD2   1 
ATOM   1645 N N     . PRO   A 1 221 ? -24.885 -64.115  -40.076 1.00 41.84  ? 213 PRO   A N     1 
ATOM   1646 C CA    . PRO   A 1 221 ? -23.697 -64.617  -40.767 1.00 41.12  ? 213 PRO   A CA    1 
ATOM   1647 C C     . PRO   A 1 221 ? -23.699 -66.139  -40.882 1.00 41.02  ? 213 PRO   A C     1 
ATOM   1648 O O     . PRO   A 1 221 ? -24.679 -66.793  -40.529 1.00 39.91  ? 213 PRO   A O     1 
ATOM   1649 C CB    . PRO   A 1 221 ? -22.575 -64.090  -39.861 1.00 40.84  ? 213 PRO   A CB    1 
ATOM   1650 C CG    . PRO   A 1 221 ? -23.167 -64.177  -38.474 1.00 41.28  ? 213 PRO   A CG    1 
ATOM   1651 C CD    . PRO   A 1 221 ? -24.625 -63.796  -38.662 1.00 41.65  ? 213 PRO   A CD    1 
ATOM   1652 N N     . SER   A 1 222 ? -22.584 -66.686  -41.382 1.00 41.03  ? 214 SER   A N     1 
ATOM   1653 C CA    . SER   A 1 222 ? -22.406 -68.122  -41.519 1.00 40.66  ? 214 SER   A CA    1 
ATOM   1654 C C     . SER   A 1 222 ? -22.397 -68.782  -40.143 1.00 40.08  ? 214 SER   A C     1 
ATOM   1655 O O     . SER   A 1 222 ? -21.981 -68.170  -39.164 1.00 40.35  ? 214 SER   A O     1 
ATOM   1656 C CB    . SER   A 1 222 ? -21.141 -68.427  -42.272 1.00 40.96  ? 214 SER   A CB    1 
ATOM   1657 O OG    . SER   A 1 222 ? -21.072 -67.666  -43.469 1.00 41.75  ? 214 SER   A OG    1 
ATOM   1658 N N     . ASN   A 1 223 ? -22.833 -70.046  -40.092 1.00 39.81  ? 215 ASN   A N     1 
ATOM   1659 C CA    . ASN   A 1 223 ? -22.954 -70.776  -38.840 1.00 39.75  ? 215 ASN   A CA    1 
ATOM   1660 C C     . ASN   A 1 223 ? -21.631 -70.790  -38.081 1.00 38.38  ? 215 ASN   A C     1 
ATOM   1661 O O     . ASN   A 1 223 ? -21.637 -70.805  -36.854 1.00 39.65  ? 215 ASN   A O     1 
ATOM   1662 C CB    . ASN   A 1 223 ? -23.434 -72.207  -39.049 1.00 40.59  ? 215 ASN   A CB    1 
ATOM   1663 C CG    . ASN   A 1 223 ? -24.855 -72.263  -39.552 1.00 41.93  ? 215 ASN   A CG    1 
ATOM   1664 O OD1   . ASN   A 1 223 ? -25.128 -72.920  -40.562 1.00 44.23  ? 215 ASN   A OD1   1 
ATOM   1665 N ND2   . ASN   A 1 223 ? -25.773 -71.600  -38.863 1.00 42.21  ? 215 ASN   A ND2   1 
ATOM   1666 N N     . HIS   A 1 224 ? -20.507 -70.801  -38.810 1.00 36.55  ? 216 HIS   A N     1 
ATOM   1667 C CA    . HIS   A 1 224 ? -19.199 -70.813  -38.177 1.00 35.85  ? 216 HIS   A CA    1 
ATOM   1668 C C     . HIS   A 1 224 ? -19.056 -69.553  -37.322 1.00 35.65  ? 216 HIS   A C     1 
ATOM   1669 O O     . HIS   A 1 224 ? -18.611 -69.633  -36.180 1.00 35.99  ? 216 HIS   A O     1 
ATOM   1670 C CB    . HIS   A 1 224 ? -18.090 -71.085  -39.207 1.00 35.26  ? 216 HIS   A CB    1 
ATOM   1671 C CG    . HIS   A 1 224 ? -17.711 -69.945  -40.093 1.00 35.26  ? 216 HIS   A CG    1 
ATOM   1672 N ND1   . HIS   A 1 224 ? -16.816 -68.971  -39.708 1.00 34.88  ? 216 HIS   A ND1   1 
ATOM   1673 C CD2   . HIS   A 1 224 ? -18.070 -69.641  -41.349 1.00 35.77  ? 216 HIS   A CD2   1 
ATOM   1674 C CE1   . HIS   A 1 224 ? -16.662 -68.103  -40.698 1.00 35.14  ? 216 HIS   A CE1   1 
ATOM   1675 N NE2   . HIS   A 1 224 ? -17.412 -68.491  -41.706 1.00 35.45  ? 216 HIS   A NE2   1 
ATOM   1676 N N     . VAL   A 1 225 ? -19.519 -68.415  -37.855 1.00 35.37  ? 217 VAL   A N     1 
ATOM   1677 C CA    . VAL   A 1 225 ? -19.424 -67.127  -37.182 1.00 34.73  ? 217 VAL   A CA    1 
ATOM   1678 C C     . VAL   A 1 225 ? -20.246 -67.150  -35.891 1.00 34.85  ? 217 VAL   A C     1 
ATOM   1679 O O     . VAL   A 1 225 ? -19.909 -66.453  -34.935 1.00 34.39  ? 217 VAL   A O     1 
ATOM   1680 C CB    . VAL   A 1 225 ? -19.875 -65.976  -38.106 1.00 34.42  ? 217 VAL   A CB    1 
ATOM   1681 C CG1   . VAL   A 1 225 ? -19.796 -64.615  -37.419 1.00 34.29  ? 217 VAL   A CG1   1 
ATOM   1682 C CG2   . VAL   A 1 225 ? -19.090 -65.945  -39.412 1.00 34.24  ? 217 VAL   A CG2   1 
ATOM   1683 N N     . ILE   A 1 226 ? -21.327 -67.940  -35.879 1.00 34.51  ? 218 ILE   A N     1 
ATOM   1684 C CA    . ILE   A 1 226 ? -22.215 -68.037  -34.731 1.00 34.27  ? 218 ILE   A CA    1 
ATOM   1685 C C     . ILE   A 1 226 ? -21.657 -69.046  -33.731 1.00 34.46  ? 218 ILE   A C     1 
ATOM   1686 O O     . ILE   A 1 226 ? -21.657 -68.791  -32.528 1.00 35.82  ? 218 ILE   A O     1 
ATOM   1687 C CB    . ILE   A 1 226 ? -23.639 -68.407  -35.188 1.00 34.47  ? 218 ILE   A CB    1 
ATOM   1688 C CG1   . ILE   A 1 226 ? -24.259 -67.275  -36.007 1.00 35.37  ? 218 ILE   A CG1   1 
ATOM   1689 C CG2   . ILE   A 1 226 ? -24.524 -68.793  -34.001 1.00 33.91  ? 218 ILE   A CG2   1 
ATOM   1690 C CD1   . ILE   A 1 226 ? -25.456 -67.693  -36.842 1.00 35.76  ? 218 ILE   A CD1   1 
ATOM   1691 N N     . ASP   A 1 227 ? -21.199 -70.196  -34.239 1.00 33.97  ? 219 ASP   A N     1 
ATOM   1692 C CA    . ASP   A 1 227 ? -20.619 -71.240  -33.410 1.00 33.30  ? 219 ASP   A CA    1 
ATOM   1693 C C     . ASP   A 1 227 ? -19.369 -70.712  -32.712 1.00 31.64  ? 219 ASP   A C     1 
ATOM   1694 O O     . ASP   A 1 227 ? -18.912 -71.289  -31.729 1.00 31.76  ? 219 ASP   A O     1 
ATOM   1695 C CB    . ASP   A 1 227 ? -20.312 -72.484  -34.227 1.00 34.64  ? 219 ASP   A CB    1 
ATOM   1696 C CG    . ASP   A 1 227 ? -21.527 -73.202  -34.795 1.00 36.06  ? 219 ASP   A CG    1 
ATOM   1697 O OD1   . ASP   A 1 227 ? -22.649 -72.680  -34.620 1.00 36.84  ? 219 ASP   A OD1   1 
ATOM   1698 O OD2   . ASP   A 1 227 ? -21.340 -74.279  -35.400 1.00 37.39  ? 219 ASP   A OD2   1 
ATOM   1699 N N     . ARG   A 1 228 ? -18.833 -69.602  -33.226 1.00 30.38  ? 220 ARG   A N     1 
ATOM   1700 C CA    . ARG   A 1 228 ? -17.657 -68.968  -32.659 1.00 29.84  ? 220 ARG   A CA    1 
ATOM   1701 C C     . ARG   A 1 228 ? -17.942 -68.502  -31.230 1.00 29.02  ? 220 ARG   A C     1 
ATOM   1702 O O     . ARG   A 1 228 ? -17.021 -68.361  -30.431 1.00 28.93  ? 220 ARG   A O     1 
ATOM   1703 C CB    . ARG   A 1 228 ? -17.261 -67.829  -33.606 1.00 30.14  ? 220 ARG   A CB    1 
ATOM   1704 C CG    . ARG   A 1 228 ? -15.813 -67.374  -33.534 1.00 30.59  ? 220 ARG   A CG    1 
ATOM   1705 C CD    . ARG   A 1 228 ? -14.833 -68.461  -33.936 1.00 30.89  ? 220 ARG   A CD    1 
ATOM   1706 N NE    . ARG   A 1 228 ? -13.502 -67.886  -34.158 1.00 31.63  ? 220 ARG   A NE    1 
ATOM   1707 C CZ    . ARG   A 1 228 ? -12.442 -67.958  -33.355 1.00 31.71  ? 220 ARG   A CZ    1 
ATOM   1708 N NH1   . ARG   A 1 228 ? -12.515 -68.529  -32.164 1.00 32.23  ? 220 ARG   A NH1   1 
ATOM   1709 N NH2   . ARG   A 1 228 ? -11.297 -67.427  -33.747 1.00 31.58  ? 220 ARG   A NH2   1 
ATOM   1710 N N     . TRP   A 1 229 ? -19.226 -68.290  -30.910 1.00 28.13  ? 221 TRP   A N     1 
ATOM   1711 C CA    . TRP   A 1 229 ? -19.641 -67.764  -29.620 1.00 27.18  ? 221 TRP   A CA    1 
ATOM   1712 C C     . TRP   A 1 229 ? -20.032 -68.872  -28.646 1.00 26.73  ? 221 TRP   A C     1 
ATOM   1713 O O     . TRP   A 1 229 ? -20.440 -68.585  -27.522 1.00 25.18  ? 221 TRP   A O     1 
ATOM   1714 C CB    . TRP   A 1 229 ? -20.802 -66.785  -29.825 1.00 27.32  ? 221 TRP   A CB    1 
ATOM   1715 C CG    . TRP   A 1 229 ? -20.368 -65.521  -30.510 1.00 27.28  ? 221 TRP   A CG    1 
ATOM   1716 C CD1   . TRP   A 1 229 ? -20.466 -65.215  -31.835 1.00 27.66  ? 221 TRP   A CD1   1 
ATOM   1717 C CD2   . TRP   A 1 229 ? -19.715 -64.401  -29.880 1.00 27.58  ? 221 TRP   A CD2   1 
ATOM   1718 N NE1   . TRP   A 1 229 ? -19.940 -63.972  -32.070 1.00 27.79  ? 221 TRP   A NE1   1 
ATOM   1719 C CE2   . TRP   A 1 229 ? -19.468 -63.450  -30.893 1.00 27.96  ? 221 TRP   A CE2   1 
ATOM   1720 C CE3   . TRP   A 1 229 ? -19.322 -64.113  -28.568 1.00 27.45  ? 221 TRP   A CE3   1 
ATOM   1721 C CZ2   . TRP   A 1 229 ? -18.848 -62.231  -30.626 1.00 28.09  ? 221 TRP   A CZ2   1 
ATOM   1722 C CZ3   . TRP   A 1 229 ? -18.707 -62.909  -28.308 1.00 27.40  ? 221 TRP   A CZ3   1 
ATOM   1723 C CH2   . TRP   A 1 229 ? -18.474 -61.984  -29.324 1.00 27.60  ? 221 TRP   A CH2   1 
ATOM   1724 N N     . LEU   A 1 230 ? -19.911 -70.130  -29.081 1.00 26.73  ? 222 LEU   A N     1 
ATOM   1725 C CA    . LEU   A 1 230 ? -20.116 -71.263  -28.197 1.00 26.94  ? 222 LEU   A CA    1 
ATOM   1726 C C     . LEU   A 1 230 ? -19.041 -71.255  -27.113 1.00 27.16  ? 222 LEU   A C     1 
ATOM   1727 O O     . LEU   A 1 230 ? -17.860 -71.061  -27.399 1.00 27.86  ? 222 LEU   A O     1 
ATOM   1728 C CB    . LEU   A 1 230 ? -20.094 -72.565  -28.994 1.00 27.59  ? 222 LEU   A CB    1 
ATOM   1729 C CG    . LEU   A 1 230 ? -21.338 -72.854  -29.837 1.00 27.98  ? 222 LEU   A CG    1 
ATOM   1730 C CD1   . LEU   A 1 230 ? -21.067 -73.916  -30.891 1.00 27.90  ? 222 LEU   A CD1   1 
ATOM   1731 C CD2   . LEU   A 1 230 ? -22.475 -73.284  -28.924 1.00 28.10  ? 222 LEU   A CD2   1 
ATOM   1732 N N     . GLY   A 1 231 ? -19.475 -71.447  -25.862 1.00 25.97  ? 223 GLY   A N     1 
ATOM   1733 C CA    . GLY   A 1 231 ? -18.564 -71.523  -24.732 1.00 26.03  ? 223 GLY   A CA    1 
ATOM   1734 C C     . GLY   A 1 231 ? -18.242 -70.153  -24.134 1.00 25.11  ? 223 GLY   A C     1 
ATOM   1735 O O     . GLY   A 1 231 ? -17.548 -70.083  -23.124 1.00 25.13  ? 223 GLY   A O     1 
ATOM   1736 N N     . GLU   A 1 232 ? -18.748 -69.076  -24.751 1.00 24.16  ? 224 GLU   A N     1 
ATOM   1737 C CA    . GLU   A 1 232 ? -18.484 -67.723  -24.288 1.00 24.01  ? 224 GLU   A CA    1 
ATOM   1738 C C     . GLU   A 1 232 ? -19.549 -67.305  -23.278 1.00 24.26  ? 224 GLU   A C     1 
ATOM   1739 O O     . GLU   A 1 232 ? -20.694 -67.740  -23.369 1.00 24.05  ? 224 GLU   A O     1 
ATOM   1740 C CB    . GLU   A 1 232 ? -18.472 -66.733  -25.454 1.00 23.70  ? 224 GLU   A CB    1 
ATOM   1741 C CG    . GLU   A 1 232 ? -17.352 -66.992  -26.455 1.00 23.21  ? 224 GLU   A CG    1 
ATOM   1742 C CD    . GLU   A 1 232 ? -15.957 -66.788  -25.898 1.00 22.97  ? 224 GLU   A CD    1 
ATOM   1743 O OE1   . GLU   A 1 232 ? -15.817 -66.200  -24.804 1.00 22.61  ? 224 GLU   A OE1   1 
ATOM   1744 O OE2   . GLU   A 1 232 ? -15.001 -67.234  -26.567 1.00 23.23  ? 224 GLU   A OE2   1 
ATOM   1745 N N     . PRO   A 1 233 ? -19.207 -66.442  -22.293 1.00 24.93  ? 225 PRO   A N     1 
ATOM   1746 C CA    . PRO   A 1 233 ? -20.165 -66.020  -21.270 1.00 25.85  ? 225 PRO   A CA    1 
ATOM   1747 C C     . PRO   A 1 233 ? -21.193 -65.019  -21.790 1.00 26.84  ? 225 PRO   A C     1 
ATOM   1748 O O     . PRO   A 1 233 ? -21.073 -63.815  -21.566 1.00 27.18  ? 225 PRO   A O     1 
ATOM   1749 C CB    . PRO   A 1 233 ? -19.241 -65.426  -20.188 1.00 25.39  ? 225 PRO   A CB    1 
ATOM   1750 C CG    . PRO   A 1 233 ? -18.098 -64.840  -20.981 1.00 25.01  ? 225 PRO   A CG    1 
ATOM   1751 C CD    . PRO   A 1 233 ? -17.877 -65.837  -22.107 1.00 24.89  ? 225 PRO   A CD    1 
ATOM   1752 N N     . ILE   A 1 234 ? -22.210 -65.541  -22.484 1.00 27.93  ? 226 ILE   A N     1 
ATOM   1753 C CA    . ILE   A 1 234 ? -23.298 -64.722  -22.989 1.00 28.80  ? 226 ILE   A CA    1 
ATOM   1754 C C     . ILE   A 1 234 ? -24.358 -64.608  -21.897 1.00 29.75  ? 226 ILE   A C     1 
ATOM   1755 O O     . ILE   A 1 234 ? -25.014 -65.591  -21.555 1.00 29.86  ? 226 ILE   A O     1 
ATOM   1756 C CB    . ILE   A 1 234 ? -23.854 -65.293  -24.308 1.00 28.95  ? 226 ILE   A CB    1 
ATOM   1757 C CG1   . ILE   A 1 234 ? -22.747 -65.406  -25.359 1.00 29.16  ? 226 ILE   A CG1   1 
ATOM   1758 C CG2   . ILE   A 1 234 ? -25.031 -64.457  -24.817 1.00 28.87  ? 226 ILE   A CG2   1 
ATOM   1759 C CD1   . ILE   A 1 234 ? -23.150 -66.145  -26.620 1.00 29.57  ? 226 ILE   A CD1   1 
ATOM   1760 N N     . LYS   A 1 235 ? -24.488 -63.394  -21.351 1.00 30.72  ? 227 LYS   A N     1 
ATOM   1761 C CA    . LYS   A 1 235 ? -25.463 -63.091  -20.317 1.00 31.72  ? 227 LYS   A CA    1 
ATOM   1762 C C     . LYS   A 1 235 ? -26.726 -62.485  -20.922 1.00 31.51  ? 227 LYS   A C     1 
ATOM   1763 O O     . LYS   A 1 235 ? -27.796 -62.592  -20.326 1.00 30.53  ? 227 LYS   A O     1 
ATOM   1764 C CB    . LYS   A 1 235 ? -24.866 -62.117  -19.296 1.00 32.85  ? 227 LYS   A CB    1 
ATOM   1765 C CG    . LYS   A 1 235 ? -23.834 -62.738  -18.373 1.00 33.91  ? 227 LYS   A CG    1 
ATOM   1766 C CD    . LYS   A 1 235 ? -24.411 -63.808  -17.457 1.00 35.06  ? 227 LYS   A CD    1 
ATOM   1767 C CE    . LYS   A 1 235 ? -23.364 -64.467  -16.628 1.00 36.72  ? 227 LYS   A CE    1 
ATOM   1768 N NZ    . LYS   A 1 235 ? -23.948 -65.566  -15.856 1.00 37.75  ? 227 LYS   A NZ    1 
ATOM   1769 N N     . ALA   A 1 236 ? -26.589 -61.835  -22.087 1.00 31.90  ? 228 ALA   A N     1 
ATOM   1770 C CA    . ALA   A 1 236 ? -27.722 -61.192  -22.732 1.00 32.36  ? 228 ALA   A CA    1 
ATOM   1771 C C     . ALA   A 1 236 ? -27.619 -61.311  -24.249 1.00 32.90  ? 228 ALA   A C     1 
ATOM   1772 O O     . ALA   A 1 236 ? -26.525 -61.424  -24.794 1.00 33.66  ? 228 ALA   A O     1 
ATOM   1773 C CB    . ALA   A 1 236 ? -27.807 -59.745  -22.305 1.00 32.43  ? 228 ALA   A CB    1 
ATOM   1774 N N     . ALA   A 1 237 ? -28.788 -61.300  -24.903 1.00 33.16  ? 229 ALA   A N     1 
ATOM   1775 C CA    . ALA   A 1 237 ? -28.900 -61.221  -26.351 1.00 33.16  ? 229 ALA   A CA    1 
ATOM   1776 C C     . ALA   A 1 237 ? -29.768 -60.017  -26.702 1.00 33.40  ? 229 ALA   A C     1 
ATOM   1777 O O     . ALA   A 1 237 ? -30.866 -59.878  -26.169 1.00 33.65  ? 229 ALA   A O     1 
ATOM   1778 C CB    . ALA   A 1 237 ? -29.488 -62.503  -26.895 1.00 33.07  ? 229 ALA   A CB    1 
ATOM   1779 N N     . ILE   A 1 238 ? -29.265 -59.145  -27.584 1.00 33.93  ? 230 ILE   A N     1 
ATOM   1780 C CA    . ILE   A 1 238 ? -29.957 -57.908  -27.913 1.00 34.20  ? 230 ILE   A CA    1 
ATOM   1781 C C     . ILE   A 1 238 ? -30.659 -58.069  -29.259 1.00 34.73  ? 230 ILE   A C     1 
ATOM   1782 O O     . ILE   A 1 238 ? -30.030 -58.427  -30.252 1.00 34.14  ? 230 ILE   A O     1 
ATOM   1783 C CB    . ILE   A 1 238 ? -28.992 -56.708  -27.889 1.00 33.54  ? 230 ILE   A CB    1 
ATOM   1784 C CG1   . ILE   A 1 238 ? -28.520 -56.423  -26.465 1.00 33.69  ? 230 ILE   A CG1   1 
ATOM   1785 C CG2   . ILE   A 1 238 ? -29.636 -55.474  -28.522 1.00 33.50  ? 230 ILE   A CG2   1 
ATOM   1786 C CD1   . ILE   A 1 238 ? -27.343 -55.470  -26.369 1.00 33.90  ? 230 ILE   A CD1   1 
ATOM   1787 N N     . LEU   A 1 239 ? -31.969 -57.785  -29.258 1.00 35.77  ? 231 LEU   A N     1 
ATOM   1788 C CA    . LEU   A 1 239 ? -32.831 -57.932  -30.421 1.00 35.76  ? 231 LEU   A CA    1 
ATOM   1789 C C     . LEU   A 1 239 ? -33.379 -56.562  -30.811 1.00 34.96  ? 231 LEU   A C     1 
ATOM   1790 O O     . LEU   A 1 239 ? -34.208 -56.007  -30.095 1.00 34.25  ? 231 LEU   A O     1 
ATOM   1791 C CB    . LEU   A 1 239 ? -33.975 -58.887  -30.080 1.00 36.57  ? 231 LEU   A CB    1 
ATOM   1792 C CG    . LEU   A 1 239 ? -33.589 -60.287  -29.593 1.00 37.28  ? 231 LEU   A CG    1 
ATOM   1793 C CD1   . LEU   A 1 239 ? -34.838 -61.028  -29.156 1.00 37.51  ? 231 LEU   A CD1   1 
ATOM   1794 C CD2   . LEU   A 1 239 ? -32.849 -61.081  -30.653 1.00 37.75  ? 231 LEU   A CD2   1 
ATOM   1795 N N     . PRO   A 1 240 ? -32.928 -55.953  -31.931 1.00 35.51  ? 232 PRO   A N     1 
ATOM   1796 C CA    . PRO   A 1 240 ? -33.579 -54.756  -32.463 1.00 36.19  ? 232 PRO   A CA    1 
ATOM   1797 C C     . PRO   A 1 240 ? -34.977 -55.081  -32.983 1.00 38.23  ? 232 PRO   A C     1 
ATOM   1798 O O     . PRO   A 1 240 ? -35.222 -56.186  -33.459 1.00 39.00  ? 232 PRO   A O     1 
ATOM   1799 C CB    . PRO   A 1 240 ? -32.626 -54.284  -33.577 1.00 35.48  ? 232 PRO   A CB    1 
ATOM   1800 C CG    . PRO   A 1 240 ? -31.321 -54.991  -33.276 1.00 35.42  ? 232 PRO   A CG    1 
ATOM   1801 C CD    . PRO   A 1 240 ? -31.739 -56.333  -32.706 1.00 35.13  ? 232 PRO   A CD    1 
ATOM   1802 N N     . THR   A 1 241 ? -35.889 -54.109  -32.882 1.00 40.36  ? 233 THR   A N     1 
ATOM   1803 C CA    . THR   A 1 241 ? -37.237 -54.255  -33.412 1.00 41.35  ? 233 THR   A CA    1 
ATOM   1804 C C     . THR   A 1 241 ? -37.183 -54.472  -34.923 1.00 43.70  ? 233 THR   A C     1 
ATOM   1805 O O     . THR   A 1 241 ? -37.989 -55.220  -35.472 1.00 44.69  ? 233 THR   A O     1 
ATOM   1806 C CB    . THR   A 1 241 ? -38.073 -53.027  -33.054 1.00 40.63  ? 233 THR   A CB    1 
ATOM   1807 O OG1   . THR   A 1 241 ? -37.235 -51.897  -33.281 1.00 39.13  ? 233 THR   A OG1   1 
ATOM   1808 C CG2   . THR   A 1 241 ? -38.545 -53.057  -31.612 1.00 40.89  ? 233 THR   A CG2   1 
ATOM   1809 N N     . SER   A 1 242 ? -36.215 -53.822  -35.581 1.00 45.54  ? 234 SER   A N     1 
ATOM   1810 C CA    . SER   A 1 242 ? -36.097 -53.844  -37.030 1.00 47.02  ? 234 SER   A CA    1 
ATOM   1811 C C     . SER   A 1 242 ? -35.989 -55.267  -37.586 1.00 49.18  ? 234 SER   A C     1 
ATOM   1812 O O     . SER   A 1 242 ? -36.417 -55.505  -38.713 1.00 49.77  ? 234 SER   A O     1 
ATOM   1813 C CB    . SER   A 1 242 ? -34.934 -52.997  -37.475 1.00 47.33  ? 234 SER   A CB    1 
ATOM   1814 O OG    . SER   A 1 242 ? -33.739 -53.382  -36.812 1.00 48.11  ? 234 SER   A OG    1 
ATOM   1815 N N     . ILE   A 1 243 ? -35.444 -56.214  -36.806 1.00 51.58  ? 235 ILE   A N     1 
ATOM   1816 C CA    . ILE   A 1 243 ? -35.131 -57.541  -37.325 1.00 53.68  ? 235 ILE   A CA    1 
ATOM   1817 C C     . ILE   A 1 243 ? -36.377 -58.430  -37.344 1.00 54.52  ? 235 ILE   A C     1 
ATOM   1818 O O     . ILE   A 1 243 ? -36.274 -59.615  -37.658 1.00 52.90  ? 235 ILE   A O     1 
ATOM   1819 C CB    . ILE   A 1 243 ? -33.987 -58.208  -36.531 1.00 54.71  ? 235 ILE   A CB    1 
ATOM   1820 C CG1   . ILE   A 1 243 ? -34.457 -58.748  -35.171 1.00 56.90  ? 235 ILE   A CG1   1 
ATOM   1821 C CG2   . ILE   A 1 243 ? -32.794 -57.261  -36.391 1.00 54.72  ? 235 ILE   A CG2   1 
ATOM   1822 C CD1   . ILE   A 1 243 ? -33.416 -59.564  -34.424 1.00 58.31  ? 235 ILE   A CD1   1 
ATOM   1823 N N     . PHE   A 1 244 ? -37.546 -57.867  -37.010 1.00 56.49  ? 236 PHE   A N     1 
ATOM   1824 C CA    . PHE   A 1 244 ? -38.773 -58.643  -36.921 1.00 56.56  ? 236 PHE   A CA    1 
ATOM   1825 C C     . PHE   A 1 244 ? -39.588 -58.487  -38.203 1.00 56.73  ? 236 PHE   A C     1 
ATOM   1826 O O     . PHE   A 1 244 ? -40.013 -57.386  -38.546 1.00 56.75  ? 236 PHE   A O     1 
ATOM   1827 C CB    . PHE   A 1 244 ? -39.576 -58.213  -35.690 1.00 55.86  ? 236 PHE   A CB    1 
ATOM   1828 C CG    . PHE   A 1 244 ? -38.987 -58.709  -34.377 1.00 55.84  ? 236 PHE   A CG    1 
ATOM   1829 C CD1   . PHE   A 1 244 ? -37.911 -58.055  -33.783 1.00 55.37  ? 236 PHE   A CD1   1 
ATOM   1830 C CD2   . PHE   A 1 244 ? -39.509 -59.831  -33.741 1.00 55.34  ? 236 PHE   A CD2   1 
ATOM   1831 C CE1   . PHE   A 1 244 ? -37.377 -58.512  -32.588 1.00 54.52  ? 236 PHE   A CE1   1 
ATOM   1832 C CE2   . PHE   A 1 244 ? -38.971 -60.283  -32.545 1.00 54.25  ? 236 PHE   A CE2   1 
ATOM   1833 C CZ    . PHE   A 1 244 ? -37.908 -59.622  -31.972 1.00 54.00  ? 236 PHE   A CZ    1 
ATOM   1834 N N     . LEU   A 1 245 ? -39.800 -59.616  -38.889 1.00 57.54  ? 237 LEU   A N     1 
ATOM   1835 C CA    . LEU   A 1 245 ? -40.747 -59.705  -39.988 1.00 58.69  ? 237 LEU   A CA    1 
ATOM   1836 C C     . LEU   A 1 245 ? -42.152 -59.431  -39.457 1.00 62.85  ? 237 LEU   A C     1 
ATOM   1837 O O     . LEU   A 1 245 ? -42.388 -59.517  -38.252 1.00 62.38  ? 237 LEU   A O     1 
ATOM   1838 C CB    . LEU   A 1 245 ? -40.673 -61.093  -40.624 1.00 57.42  ? 237 LEU   A CB    1 
ATOM   1839 C CG    . LEU   A 1 245 ? -39.308 -61.540  -41.159 1.00 56.65  ? 237 LEU   A CG    1 
ATOM   1840 C CD1   . LEU   A 1 245 ? -39.412 -62.961  -41.688 1.00 55.79  ? 237 LEU   A CD1   1 
ATOM   1841 C CD2   . LEU   A 1 245 ? -38.769 -60.608  -42.232 1.00 56.24  ? 237 LEU   A CD2   1 
ATOM   1842 N N     . THR   A 1 246 ? -43.076 -59.103  -40.369 1.00 66.45  ? 238 THR   A N     1 
ATOM   1843 C CA    . THR   A 1 246 ? -44.486 -58.974  -40.035 1.00 68.37  ? 238 THR   A CA    1 
ATOM   1844 C C     . THR   A 1 246 ? -45.244 -60.138  -40.667 1.00 71.15  ? 238 THR   A C     1 
ATOM   1845 O O     . THR   A 1 246 ? -45.004 -60.478  -41.824 1.00 71.89  ? 238 THR   A O     1 
ATOM   1846 C CB    . THR   A 1 246 ? -45.028 -57.631  -40.521 1.00 67.66  ? 238 THR   A CB    1 
ATOM   1847 O OG1   . THR   A 1 246 ? -44.107 -56.643  -40.071 1.00 67.61  ? 238 THR   A OG1   1 
ATOM   1848 C CG2   . THR   A 1 246 ? -46.415 -57.336  -39.977 1.00 67.77  ? 238 THR   A CG2   1 
ATOM   1849 N N     . ASN   A 1 247 ? -46.160 -60.740  -39.898 1.00 74.44  ? 239 ASN   A N     1 
ATOM   1850 C CA    . ASN   A 1 247 ? -46.996 -61.819  -40.401 1.00 77.95  ? 239 ASN   A CA    1 
ATOM   1851 C C     . ASN   A 1 247 ? -48.243 -61.205  -41.038 1.00 82.30  ? 239 ASN   A C     1 
ATOM   1852 O O     . ASN   A 1 247 ? -48.347 -59.985  -41.149 1.00 82.84  ? 239 ASN   A O     1 
ATOM   1853 C CB    . ASN   A 1 247 ? -47.290 -62.852  -39.315 1.00 78.01  ? 239 ASN   A CB    1 
ATOM   1854 C CG    . ASN   A 1 247 ? -48.204 -62.336  -38.228 1.00 78.20  ? 239 ASN   A CG    1 
ATOM   1855 O OD1   . ASN   A 1 247 ? -48.442 -61.127  -38.131 1.00 79.19  ? 239 ASN   A OD1   1 
ATOM   1856 N ND2   . ASN   A 1 247 ? -48.711 -63.231  -37.393 1.00 77.14  ? 239 ASN   A ND2   1 
ATOM   1857 N N     . LYS   A 1 248 ? -49.184 -62.063  -41.452 1.00 85.31  ? 240 LYS   A N     1 
ATOM   1858 C CA    . LYS   A 1 248 ? -50.364 -61.622  -42.179 1.00 86.12  ? 240 LYS   A CA    1 
ATOM   1859 C C     . LYS   A 1 248 ? -51.301 -60.848  -41.254 1.00 87.16  ? 240 LYS   A C     1 
ATOM   1860 O O     . LYS   A 1 248 ? -51.820 -59.803  -41.641 1.00 88.70  ? 240 LYS   A O     1 
ATOM   1861 C CB    . LYS   A 1 248 ? -51.049 -62.815  -42.854 1.00 86.18  ? 240 LYS   A CB    1 
ATOM   1862 C CG    . LYS   A 1 248 ? -50.144 -63.531  -43.847 1.00 86.46  ? 240 LYS   A CG    1 
ATOM   1863 C CD    . LYS   A 1 248 ? -50.827 -63.985  -45.131 1.00 86.23  ? 240 LYS   A CD    1 
ATOM   1864 C CE    . LYS   A 1 248 ? -49.838 -64.164  -46.240 1.00 86.74  ? 240 LYS   A CE    1 
ATOM   1865 N NZ    . LYS   A 1 248 ? -50.497 -64.375  -47.531 1.00 87.00  ? 240 LYS   A NZ    1 
ATOM   1866 N N     . LYS   A 1 249 ? -51.506 -61.364  -40.035 1.00 88.16  ? 241 LYS   A N     1 
ATOM   1867 C CA    . LYS   A 1 249 ? -52.299 -60.675  -39.028 1.00 89.89  ? 241 LYS   A CA    1 
ATOM   1868 C C     . LYS   A 1 249 ? -51.815 -59.232  -38.892 1.00 89.68  ? 241 LYS   A C     1 
ATOM   1869 O O     . LYS   A 1 249 ? -52.622 -58.306  -38.855 1.00 90.34  ? 241 LYS   A O     1 
ATOM   1870 C CB    . LYS   A 1 249 ? -52.204 -61.313  -37.637 1.00 91.35  ? 241 LYS   A CB    1 
ATOM   1871 C CG    . LYS   A 1 249 ? -52.411 -62.820  -37.528 1.00 93.64  ? 241 LYS   A CG    1 
ATOM   1872 C CD    . LYS   A 1 249 ? -52.276 -63.309  -36.090 1.00 96.11  ? 241 LYS   A CD    1 
ATOM   1873 C CE    . LYS   A 1 249 ? -51.657 -64.666  -35.943 1.00 97.25  ? 241 LYS   A CE    1 
ATOM   1874 N NZ    . LYS   A 1 249 ? -52.538 -65.747  -36.387 1.00 98.67  ? 241 LYS   A NZ    1 
ATOM   1875 N N     . GLY   A 1 250 ? -50.486 -59.062  -38.827 1.00 89.96  ? 242 GLY   A N     1 
ATOM   1876 C CA    . GLY   A 1 250 ? -49.863 -57.770  -38.583 1.00 89.92  ? 242 GLY   A CA    1 
ATOM   1877 C C     . GLY   A 1 250 ? -48.907 -57.804  -37.389 1.00 89.16  ? 242 GLY   A C     1 
ATOM   1878 O O     . GLY   A 1 250 ? -48.279 -56.794  -37.075 1.00 84.80  ? 242 GLY   A O     1 
ATOM   1879 N N     . PHE   A 1 251 ? -48.814 -58.965  -36.723 1.00 89.56  ? 243 PHE   A N     1 
ATOM   1880 C CA    . PHE   A 1 251 ? -47.936 -59.151  -35.577 1.00 89.00  ? 243 PHE   A CA    1 
ATOM   1881 C C     . PHE   A 1 251 ? -46.475 -59.155  -36.025 1.00 87.14  ? 243 PHE   A C     1 
ATOM   1882 O O     . PHE   A 1 251 ? -46.186 -59.375  -37.200 1.00 88.22  ? 243 PHE   A O     1 
ATOM   1883 C CB    . PHE   A 1 251 ? -48.209 -60.477  -34.856 1.00 90.39  ? 243 PHE   A CB    1 
ATOM   1884 C CG    . PHE   A 1 251 ? -49.458 -60.577  -33.986 1.00 90.83  ? 243 PHE   A CG    1 
ATOM   1885 C CD1   . PHE   A 1 251 ? -49.970 -59.473  -33.308 1.00 89.92  ? 243 PHE   A CD1   1 
ATOM   1886 C CD2   . PHE   A 1 251 ? -50.093 -61.804  -33.814 1.00 90.56  ? 243 PHE   A CD2   1 
ATOM   1887 C CE1   . PHE   A 1 251 ? -51.098 -59.592  -32.509 1.00 90.18  ? 243 PHE   A CE1   1 
ATOM   1888 C CE2   . PHE   A 1 251 ? -51.220 -61.918  -33.013 1.00 89.87  ? 243 PHE   A CE2   1 
ATOM   1889 C CZ    . PHE   A 1 251 ? -51.719 -60.813  -32.362 1.00 90.52  ? 243 PHE   A CZ    1 
ATOM   1890 N N     . PRO   A 1 252 ? -45.511 -58.928  -35.099 1.00 81.99  ? 244 PRO   A N     1 
ATOM   1891 C CA    . PRO   A 1 252 ? -44.089 -59.105  -35.389 1.00 77.58  ? 244 PRO   A CA    1 
ATOM   1892 C C     . PRO   A 1 252 ? -43.669 -60.554  -35.159 1.00 71.91  ? 244 PRO   A C     1 
ATOM   1893 O O     . PRO   A 1 252 ? -44.116 -61.179  -34.200 1.00 71.07  ? 244 PRO   A O     1 
ATOM   1894 C CB    . PRO   A 1 252 ? -43.389 -58.136  -34.418 1.00 79.42  ? 244 PRO   A CB    1 
ATOM   1895 C CG    . PRO   A 1 252 ? -44.418 -57.818  -33.340 1.00 80.81  ? 244 PRO   A CG    1 
ATOM   1896 C CD    . PRO   A 1 252 ? -45.734 -58.480  -33.717 1.00 81.59  ? 244 PRO   A CD    1 
ATOM   1897 N N     . VAL   A 1 253 ? -42.813 -61.074  -36.050 1.00 67.44  ? 245 VAL   A N     1 
ATOM   1898 C CA    . VAL   A 1 253 ? -42.294 -62.431  -35.946 1.00 63.90  ? 245 VAL   A CA    1 
ATOM   1899 C C     . VAL   A 1 253 ? -40.828 -62.421  -36.378 1.00 59.82  ? 245 VAL   A C     1 
ATOM   1900 O O     . VAL   A 1 253 ? -40.278 -61.363  -36.671 1.00 57.95  ? 245 VAL   A O     1 
ATOM   1901 C CB    . VAL   A 1 253 ? -43.118 -63.437  -36.777 1.00 64.19  ? 245 VAL   A CB    1 
ATOM   1902 C CG1   . VAL   A 1 253 ? -44.574 -63.493  -36.328 1.00 65.06  ? 245 VAL   A CG1   1 
ATOM   1903 C CG2   . VAL   A 1 253 ? -43.032 -63.160  -38.275 1.00 63.68  ? 245 VAL   A CG2   1 
ATOM   1904 N N     . LEU   A 1 254 ? -40.211 -63.610  -36.415 1.00 57.01  ? 246 LEU   A N     1 
ATOM   1905 C CA    . LEU   A 1 254 ? -38.828 -63.764  -36.836 1.00 55.61  ? 246 LEU   A CA    1 
ATOM   1906 C C     . LEU   A 1 254 ? -38.739 -64.851  -37.902 1.00 54.72  ? 246 LEU   A C     1 
ATOM   1907 O O     . LEU   A 1 254 ? -39.560 -65.764  -37.932 1.00 52.93  ? 246 LEU   A O     1 
ATOM   1908 C CB    . LEU   A 1 254 ? -37.942 -64.110  -35.640 1.00 54.09  ? 246 LEU   A CB    1 
ATOM   1909 C CG    . LEU   A 1 254 ? -37.703 -62.995  -34.618 1.00 52.84  ? 246 LEU   A CG    1 
ATOM   1910 C CD1   . LEU   A 1 254 ? -37.077 -63.564  -33.357 1.00 52.91  ? 246 LEU   A CD1   1 
ATOM   1911 C CD2   . LEU   A 1 254 ? -36.826 -61.898  -35.200 1.00 52.12  ? 246 LEU   A CD2   1 
ATOM   1912 N N     . SER   A 1 255 ? -37.718 -64.743  -38.761 1.00 55.03  ? 247 SER   A N     1 
ATOM   1913 C CA    . SER   A 1 255 ? -37.392 -65.795  -39.709 1.00 56.44  ? 247 SER   A CA    1 
ATOM   1914 C C     . SER   A 1 255 ? -37.040 -67.070  -38.948 1.00 58.83  ? 247 SER   A C     1 
ATOM   1915 O O     . SER   A 1 255 ? -36.671 -67.015  -37.778 1.00 59.87  ? 247 SER   A O     1 
ATOM   1916 C CB    . SER   A 1 255 ? -36.261 -65.386  -40.618 1.00 56.53  ? 247 SER   A CB    1 
ATOM   1917 O OG    . SER   A 1 255 ? -35.005 -65.511  -39.965 1.00 56.62  ? 247 SER   A OG    1 
ATOM   1918 N N     . LYS   A 1 256 ? -37.146 -68.213  -39.634 1.00 62.50  ? 248 LYS   A N     1 
ATOM   1919 C CA    . LYS   A 1 256 ? -36.839 -69.505  -39.041 1.00 65.00  ? 248 LYS   A CA    1 
ATOM   1920 C C     . LYS   A 1 256 ? -35.386 -69.545  -38.570 1.00 64.11  ? 248 LYS   A C     1 
ATOM   1921 O O     . LYS   A 1 256 ? -35.085 -70.167  -37.554 1.00 62.21  ? 248 LYS   A O     1 
ATOM   1922 C CB    . LYS   A 1 256 ? -37.096 -70.651  -40.026 1.00 68.09  ? 248 LYS   A CB    1 
ATOM   1923 C CG    . LYS   A 1 256 ? -38.555 -71.032  -40.228 1.00 70.99  ? 248 LYS   A CG    1 
ATOM   1924 C CD    . LYS   A 1 256 ? -38.731 -72.304  -41.050 1.00 73.33  ? 248 LYS   A CD    1 
ATOM   1925 C CE    . LYS   A 1 256 ? -40.162 -72.717  -41.213 1.00 74.52  ? 248 LYS   A CE    1 
ATOM   1926 N NZ    . LYS   A 1 256 ? -40.798 -73.054  -39.936 1.00 74.85  ? 248 LYS   A NZ    1 
ATOM   1927 N N     . MET   A 1 257 ? -34.488 -68.894  -39.321 1.00 63.99  ? 249 MET   A N     1 
ATOM   1928 C CA    . MET   A 1 257 ? -33.077 -68.864  -38.967 1.00 64.43  ? 249 MET   A CA    1 
ATOM   1929 C C     . MET   A 1 257 ? -32.869 -68.111  -37.655 1.00 61.41  ? 249 MET   A C     1 
ATOM   1930 O O     . MET   A 1 257 ? -32.092 -68.553  -36.811 1.00 59.57  ? 249 MET   A O     1 
ATOM   1931 C CB    . MET   A 1 257 ? -32.223 -68.228  -40.072 1.00 67.33  ? 249 MET   A CB    1 
ATOM   1932 C CG    . MET   A 1 257 ? -31.784 -69.199  -41.156 1.00 70.80  ? 249 MET   A CG    1 
ATOM   1933 S SD    . MET   A 1 257 ? -31.077 -70.736  -40.525 1.00 74.81  ? 249 MET   A SD    1 
ATOM   1934 C CE    . MET   A 1 257 ? -29.814 -70.174  -39.374 1.00 75.07  ? 249 MET   A CE    1 
ATOM   1935 N N     . HIS   A 1 258 ? -33.560 -66.975  -37.493 1.00 58.96  ? 250 HIS   A N     1 
ATOM   1936 C CA    . HIS   A 1 258 ? -33.507 -66.214  -36.254 1.00 57.04  ? 250 HIS   A CA    1 
ATOM   1937 C C     . HIS   A 1 258 ? -34.053 -67.053  -35.099 1.00 57.88  ? 250 HIS   A C     1 
ATOM   1938 O O     . HIS   A 1 258 ? -33.571 -66.938  -33.976 1.00 57.48  ? 250 HIS   A O     1 
ATOM   1939 C CB    . HIS   A 1 258 ? -34.233 -64.872  -36.402 1.00 54.23  ? 250 HIS   A CB    1 
ATOM   1940 C CG    . HIS   A 1 258 ? -33.455 -63.858  -37.173 1.00 52.90  ? 250 HIS   A CG    1 
ATOM   1941 N ND1   . HIS   A 1 258 ? -33.352 -63.906  -38.545 1.00 52.47  ? 250 HIS   A ND1   1 
ATOM   1942 C CD2   . HIS   A 1 258 ? -32.729 -62.801  -36.785 1.00 51.47  ? 250 HIS   A CD2   1 
ATOM   1943 C CE1   . HIS   A 1 258 ? -32.600 -62.900  -38.962 1.00 50.65  ? 250 HIS   A CE1   1 
ATOM   1944 N NE2   . HIS   A 1 258 ? -32.213 -62.213  -37.911 1.00 50.47  ? 250 HIS   A NE2   1 
ATOM   1945 N N     . GLN   A 1 259 ? -35.047 -67.901  -35.388 1.00 58.84  ? 251 GLN   A N     1 
ATOM   1946 C CA    . GLN   A 1 259 ? -35.656 -68.753  -34.379 1.00 60.90  ? 251 GLN   A CA    1 
ATOM   1947 C C     . GLN   A 1 259 ? -34.650 -69.794  -33.887 1.00 61.40  ? 251 GLN   A C     1 
ATOM   1948 O O     . GLN   A 1 259 ? -34.487 -69.958  -32.681 1.00 63.23  ? 251 GLN   A O     1 
ATOM   1949 C CB    . GLN   A 1 259 ? -36.942 -69.377  -34.919 1.00 63.92  ? 251 GLN   A CB    1 
ATOM   1950 C CG    . GLN   A 1 259 ? -38.089 -68.383  -35.074 1.00 65.90  ? 251 GLN   A CG    1 
ATOM   1951 C CD    . GLN   A 1 259 ? -39.250 -68.931  -35.876 1.00 67.29  ? 251 GLN   A CD    1 
ATOM   1952 O OE1   . GLN   A 1 259 ? -39.589 -68.419  -36.949 1.00 69.07  ? 251 GLN   A OE1   1 
ATOM   1953 N NE2   . GLN   A 1 259 ? -39.869 -69.986  -35.367 1.00 66.60  ? 251 GLN   A NE2   1 
ATOM   1954 N N     . ARG   A 1 260 ? -33.971 -70.480  -34.818 1.00 61.71  ? 252 ARG   A N     1 
ATOM   1955 C CA    . ARG   A 1 260 ? -32.938 -71.445  -34.462 1.00 61.42  ? 252 ARG   A CA    1 
ATOM   1956 C C     . ARG   A 1 260 ? -31.995 -70.850  -33.419 1.00 56.60  ? 252 ARG   A C     1 
ATOM   1957 O O     . ARG   A 1 260 ? -31.640 -71.515  -32.448 1.00 54.51  ? 252 ARG   A O     1 
ATOM   1958 C CB    . ARG   A 1 260 ? -32.119 -71.903  -35.675 1.00 65.26  ? 252 ARG   A CB    1 
ATOM   1959 C CG    . ARG   A 1 260 ? -32.711 -73.125  -36.360 1.00 69.57  ? 252 ARG   A CG    1 
ATOM   1960 C CD    . ARG   A 1 260 ? -31.983 -73.511  -37.638 1.00 73.83  ? 252 ARG   A CD    1 
ATOM   1961 N NE    . ARG   A 1 260 ? -32.875 -74.280  -38.515 1.00 78.65  ? 252 ARG   A NE    1 
ATOM   1962 C CZ    . ARG   A 1 260 ? -33.906 -73.774  -39.194 1.00 82.51  ? 252 ARG   A CZ    1 
ATOM   1963 N NH1   . ARG   A 1 260 ? -34.727 -74.580  -39.846 1.00 83.28  ? 252 ARG   A NH1   1 
ATOM   1964 N NH2   . ARG   A 1 260 ? -34.131 -72.469  -39.207 1.00 83.21  ? 252 ARG   A NH2   1 
ATOM   1965 N N     . LEU   A 1 261 ? -31.599 -69.593  -33.643 1.00 52.66  ? 253 LEU   A N     1 
ATOM   1966 C CA    . LEU   A 1 261 ? -30.663 -68.906  -32.772 1.00 49.87  ? 253 LEU   A CA    1 
ATOM   1967 C C     . LEU   A 1 261 ? -31.292 -68.675  -31.399 1.00 48.36  ? 253 LEU   A C     1 
ATOM   1968 O O     . LEU   A 1 261 ? -30.630 -68.862  -30.382 1.00 49.67  ? 253 LEU   A O     1 
ATOM   1969 C CB    . LEU   A 1 261 ? -30.233 -67.596  -33.432 1.00 49.29  ? 253 LEU   A CB    1 
ATOM   1970 C CG    . LEU   A 1 261 ? -29.099 -66.828  -32.746 1.00 49.35  ? 253 LEU   A CG    1 
ATOM   1971 C CD1   . LEU   A 1 261 ? -27.971 -67.749  -32.319 1.00 49.98  ? 253 LEU   A CD1   1 
ATOM   1972 C CD2   . LEU   A 1 261 ? -28.562 -65.747  -33.667 1.00 49.19  ? 253 LEU   A CD2   1 
ATOM   1973 N N     . ILE   A 1 262 ? -32.571 -68.283  -31.378 1.00 46.40  ? 254 ILE   A N     1 
ATOM   1974 C CA    . ILE   A 1 262 ? -33.269 -68.011  -30.130 1.00 45.54  ? 254 ILE   A CA    1 
ATOM   1975 C C     . ILE   A 1 262 ? -33.316 -69.279  -29.281 1.00 47.04  ? 254 ILE   A C     1 
ATOM   1976 O O     . ILE   A 1 262 ? -33.099 -69.217  -28.074 1.00 45.09  ? 254 ILE   A O     1 
ATOM   1977 C CB    . ILE   A 1 262 ? -34.676 -67.435  -30.388 1.00 43.95  ? 254 ILE   A CB    1 
ATOM   1978 C CG1   . ILE   A 1 262 ? -34.619 -66.087  -31.109 1.00 43.18  ? 254 ILE   A CG1   1 
ATOM   1979 C CG2   . ILE   A 1 262 ? -35.484 -67.337  -29.093 1.00 44.06  ? 254 ILE   A CG2   1 
ATOM   1980 C CD1   . ILE   A 1 262 ? -33.802 -65.022  -30.400 1.00 42.89  ? 254 ILE   A CD1   1 
ATOM   1981 N N     . PHE   A 1 263 ? -33.590 -70.426  -29.914 1.00 50.69  ? 255 PHE   A N     1 
ATOM   1982 C CA    . PHE   A 1 263 ? -33.693 -71.685  -29.193 1.00 53.25  ? 255 PHE   A CA    1 
ATOM   1983 C C     . PHE   A 1 263 ? -32.327 -72.067  -28.627 1.00 54.14  ? 255 PHE   A C     1 
ATOM   1984 O O     . PHE   A 1 263 ? -32.246 -72.555  -27.501 1.00 57.84  ? 255 PHE   A O     1 
ATOM   1985 C CB    . PHE   A 1 263 ? -34.307 -72.765  -30.090 1.00 55.45  ? 255 PHE   A CB    1 
ATOM   1986 C CG    . PHE   A 1 263 ? -35.785 -72.533  -30.373 1.00 58.80  ? 255 PHE   A CG    1 
ATOM   1987 C CD1   . PHE   A 1 263 ? -36.731 -72.666  -29.361 1.00 61.60  ? 255 PHE   A CD1   1 
ATOM   1988 C CD2   . PHE   A 1 263 ? -36.230 -72.186  -31.645 1.00 60.62  ? 255 PHE   A CD2   1 
ATOM   1989 C CE1   . PHE   A 1 263 ? -38.076 -72.444  -29.613 1.00 62.04  ? 255 PHE   A CE1   1 
ATOM   1990 C CE2   . PHE   A 1 263 ? -37.578 -71.971  -31.892 1.00 61.14  ? 255 PHE   A CE2   1 
ATOM   1991 C CZ    . PHE   A 1 263 ? -38.498 -72.101  -30.876 1.00 61.89  ? 255 PHE   A CZ    1 
ATOM   1992 N N     . ARG   A 1 264 ? -31.261 -71.826  -29.400 1.00 53.11  ? 256 ARG   A N     1 
ATOM   1993 C CA    . ARG   A 1 264 ? -29.902 -72.025  -28.918 1.00 51.85  ? 256 ARG   A CA    1 
ATOM   1994 C C     . ARG   A 1 264 ? -29.661 -71.147  -27.690 1.00 49.67  ? 256 ARG   A C     1 
ATOM   1995 O O     . ARG   A 1 264 ? -29.072 -71.598  -26.711 1.00 49.26  ? 256 ARG   A O     1 
ATOM   1996 C CB    . ARG   A 1 264 ? -28.876 -71.754  -30.026 1.00 53.29  ? 256 ARG   A CB    1 
ATOM   1997 C CG    . ARG   A 1 264 ? -28.721 -72.893  -31.026 1.00 55.70  ? 256 ARG   A CG    1 
ATOM   1998 C CD    . ARG   A 1 264 ? -27.841 -72.555  -32.231 1.00 56.80  ? 256 ARG   A CD    1 
ATOM   1999 N NE    . ARG   A 1 264 ? -26.549 -71.949  -31.876 1.00 57.95  ? 256 ARG   A NE    1 
ATOM   2000 C CZ    . ARG   A 1 264 ? -25.328 -72.420  -32.137 1.00 57.73  ? 256 ARG   A CZ    1 
ATOM   2001 N NH1   . ARG   A 1 264 ? -25.156 -73.603  -32.700 1.00 58.61  ? 256 ARG   A NH1   1 
ATOM   2002 N NH2   . ARG   A 1 264 ? -24.266 -71.698  -31.819 1.00 57.21  ? 256 ARG   A NH2   1 
ATOM   2003 N N     . LEU   A 1 265 ? -30.142 -69.900  -27.745 1.00 48.20  ? 257 LEU   A N     1 
ATOM   2004 C CA    . LEU   A 1 265 ? -29.927 -68.932  -26.679 1.00 47.69  ? 257 LEU   A CA    1 
ATOM   2005 C C     . LEU   A 1 265 ? -30.778 -69.259  -25.453 1.00 48.36  ? 257 LEU   A C     1 
ATOM   2006 O O     . LEU   A 1 265 ? -30.434 -68.848  -24.348 1.00 48.43  ? 257 LEU   A O     1 
ATOM   2007 C CB    . LEU   A 1 265 ? -30.217 -67.526  -27.199 1.00 46.09  ? 257 LEU   A CB    1 
ATOM   2008 C CG    . LEU   A 1 265 ? -29.166 -66.934  -28.144 1.00 44.62  ? 257 LEU   A CG    1 
ATOM   2009 C CD1   . LEU   A 1 265 ? -29.708 -65.714  -28.866 1.00 44.26  ? 257 LEU   A CD1   1 
ATOM   2010 C CD2   . LEU   A 1 265 ? -27.899 -66.582  -27.383 1.00 44.05  ? 257 LEU   A CD2   1 
ATOM   2011 N N     . LEU   A 1 266 ? -31.885 -69.984  -25.645 1.00 50.44  ? 258 LEU   A N     1 
ATOM   2012 C CA    . LEU   A 1 266 ? -32.761 -70.338  -24.538 1.00 52.48  ? 258 LEU   A CA    1 
ATOM   2013 C C     . LEU   A 1 266 ? -32.152 -71.477  -23.718 1.00 53.67  ? 258 LEU   A C     1 
ATOM   2014 O O     . LEU   A 1 266 ? -32.470 -71.611  -22.538 1.00 54.25  ? 258 LEU   A O     1 
ATOM   2015 C CB    . LEU   A 1 266 ? -34.161 -70.681  -25.048 1.00 53.13  ? 258 LEU   A CB    1 
ATOM   2016 C CG    . LEU   A 1 266 ? -35.007 -69.495  -25.527 1.00 54.18  ? 258 LEU   A CG    1 
ATOM   2017 C CD1   . LEU   A 1 266 ? -36.231 -69.983  -26.282 1.00 54.97  ? 258 LEU   A CD1   1 
ATOM   2018 C CD2   . LEU   A 1 266 ? -35.428 -68.592  -24.379 1.00 54.33  ? 258 LEU   A CD2   1 
ATOM   2019 N N     . LYS   A 1 267 ? -31.278 -72.285  -24.335 1.00 54.09  ? 259 LYS   A N     1 
ATOM   2020 C CA    . LYS   A 1 267 ? -30.508 -73.280  -23.603 1.00 54.37  ? 259 LYS   A CA    1 
ATOM   2021 C C     . LYS   A 1 267 ? -29.554 -72.588  -22.631 1.00 52.86  ? 259 LYS   A C     1 
ATOM   2022 O O     . LYS   A 1 267 ? -29.327 -73.076  -21.527 1.00 53.29  ? 259 LYS   A O     1 
ATOM   2023 C CB    . LYS   A 1 267 ? -29.629 -74.159  -24.498 1.00 56.08  ? 259 LYS   A CB    1 
ATOM   2024 C CG    . LYS   A 1 267 ? -30.330 -75.026  -25.527 1.00 58.03  ? 259 LYS   A CG    1 
ATOM   2025 C CD    . LYS   A 1 267 ? -29.323 -75.688  -26.463 1.00 60.16  ? 259 LYS   A CD    1 
ATOM   2026 C CE    . LYS   A 1 267 ? -29.932 -76.596  -27.484 1.00 61.90  ? 259 LYS   A CE    1 
ATOM   2027 N NZ    . LYS   A 1 267 ? -30.505 -77.803  -26.882 1.00 62.78  ? 259 LYS   A NZ    1 
ATOM   2028 N N     . LEU   A 1 268 ? -28.986 -71.457  -23.065 1.00 51.01  ? 260 LEU   A N     1 
ATOM   2029 C CA    . LEU   A 1 268 ? -28.021 -70.718  -22.269 1.00 50.65  ? 260 LEU   A CA    1 
ATOM   2030 C C     . LEU   A 1 268 ? -28.733 -69.760  -21.317 1.00 49.76  ? 260 LEU   A C     1 
ATOM   2031 O O     . LEU   A 1 268 ? -28.082 -69.037  -20.566 1.00 49.31  ? 260 LEU   A O     1 
ATOM   2032 C CB    . LEU   A 1 268 ? -27.061 -69.981  -23.201 1.00 51.06  ? 260 LEU   A CB    1 
ATOM   2033 C CG    . LEU   A 1 268 ? -26.176 -70.867  -24.083 1.00 51.63  ? 260 LEU   A CG    1 
ATOM   2034 C CD1   . LEU   A 1 268 ? -25.333 -70.014  -25.013 1.00 51.92  ? 260 LEU   A CD1   1 
ATOM   2035 C CD2   . LEU   A 1 268 ? -25.289 -71.782  -23.254 1.00 51.73  ? 260 LEU   A CD2   1 
ATOM   2036 N N     . GLU   A 1 269 ? -30.069 -69.749  -21.358 1.00 49.59  ? 261 GLU   A N     1 
ATOM   2037 C CA    . GLU   A 1 269 ? -30.858 -69.024  -20.378 1.00 49.63  ? 261 GLU   A CA    1 
ATOM   2038 C C     . GLU   A 1 269 ? -30.335 -67.594  -20.266 1.00 46.79  ? 261 GLU   A C     1 
ATOM   2039 O O     . GLU   A 1 269 ? -30.082 -67.104  -19.169 1.00 48.54  ? 261 GLU   A O     1 
ATOM   2040 C CB    . GLU   A 1 269 ? -30.788 -69.764  -19.041 1.00 51.68  ? 261 GLU   A CB    1 
ATOM   2041 C CG    . GLU   A 1 269 ? -31.150 -71.242  -19.146 1.00 53.54  ? 261 GLU   A CG    1 
ATOM   2042 C CD    . GLU   A 1 269 ? -30.674 -72.071  -17.968 1.00 55.85  ? 261 GLU   A CD    1 
ATOM   2043 O OE1   . GLU   A 1 269 ? -29.948 -73.061  -18.201 1.00 56.27  ? 261 GLU   A OE1   1 
ATOM   2044 O OE2   . GLU   A 1 269 ? -31.019 -71.718  -16.819 1.00 57.50  ? 261 GLU   A OE2   1 
ATOM   2045 N N     . VAL   A 1 270 ? -30.162 -66.938  -21.418 1.00 43.43  ? 262 VAL   A N     1 
ATOM   2046 C CA    . VAL   A 1 270 ? -29.694 -65.565  -21.449 1.00 42.54  ? 262 VAL   A CA    1 
ATOM   2047 C C     . VAL   A 1 270 ? -30.904 -64.673  -21.193 1.00 42.25  ? 262 VAL   A C     1 
ATOM   2048 O O     . VAL   A 1 270 ? -32.040 -65.125  -21.310 1.00 43.30  ? 262 VAL   A O     1 
ATOM   2049 C CB    . VAL   A 1 270 ? -28.994 -65.190  -22.772 1.00 42.51  ? 262 VAL   A CB    1 
ATOM   2050 C CG1   . VAL   A 1 270 ? -28.054 -66.290  -23.255 1.00 42.20  ? 262 VAL   A CG1   1 
ATOM   2051 C CG2   . VAL   A 1 270 ? -29.985 -64.827  -23.874 1.00 43.23  ? 262 VAL   A CG2   1 
ATOM   2052 N N     . GLN   A 1 271 ? -30.650 -63.412  -20.835 1.00 41.60  ? 263 GLN   A N     1 
ATOM   2053 C CA    . GLN   A 1 271 ? -31.708 -62.419  -20.757 1.00 40.95  ? 263 GLN   A CA    1 
ATOM   2054 C C     . GLN   A 1 271 ? -31.809 -61.738  -22.118 1.00 40.91  ? 263 GLN   A C     1 
ATOM   2055 O O     . GLN   A 1 271 ? -30.799 -61.304  -22.664 1.00 40.22  ? 263 GLN   A O     1 
ATOM   2056 C CB    . GLN   A 1 271 ? -31.441 -61.386  -19.663 1.00 40.77  ? 263 GLN   A CB    1 
ATOM   2057 C CG    . GLN   A 1 271 ? -30.994 -61.987  -18.334 1.00 41.10  ? 263 GLN   A CG    1 
ATOM   2058 C CD    . GLN   A 1 271 ? -31.062 -61.000  -17.191 1.00 40.68  ? 263 GLN   A CD    1 
ATOM   2059 O OE1   . GLN   A 1 271 ? -30.049 -60.450  -16.746 1.00 41.49  ? 263 GLN   A OE1   1 
ATOM   2060 N NE2   . GLN   A 1 271 ? -32.275 -60.744  -16.724 1.00 40.70  ? 263 GLN   A NE2   1 
ATOM   2061 N N     . PHE   A 1 272 ? -33.027 -61.660  -22.662 1.00 41.34  ? 264 PHE   A N     1 
ATOM   2062 C CA    . PHE   A 1 272 ? -33.240 -61.027  -23.953 1.00 41.79  ? 264 PHE   A CA    1 
ATOM   2063 C C     . PHE   A 1 272 ? -33.523 -59.543  -23.743 1.00 41.76  ? 264 PHE   A C     1 
ATOM   2064 O O     . PHE   A 1 272 ? -34.287 -59.166  -22.859 1.00 42.15  ? 264 PHE   A O     1 
ATOM   2065 C CB    . PHE   A 1 272 ? -34.351 -61.739  -24.728 1.00 42.07  ? 264 PHE   A CB    1 
ATOM   2066 C CG    . PHE   A 1 272 ? -33.914 -63.099  -25.252 1.00 42.78  ? 264 PHE   A CG    1 
ATOM   2067 C CD1   . PHE   A 1 272 ? -34.088 -64.247  -24.486 1.00 42.61  ? 264 PHE   A CD1   1 
ATOM   2068 C CD2   . PHE   A 1 272 ? -33.299 -63.220  -26.495 1.00 42.51  ? 264 PHE   A CD2   1 
ATOM   2069 C CE1   . PHE   A 1 272 ? -33.676 -65.483  -24.962 1.00 42.61  ? 264 PHE   A CE1   1 
ATOM   2070 C CE2   . PHE   A 1 272 ? -32.889 -64.459  -26.966 1.00 42.13  ? 264 PHE   A CE2   1 
ATOM   2071 C CZ    . PHE   A 1 272 ? -33.078 -65.586  -26.199 1.00 42.38  ? 264 PHE   A CZ    1 
ATOM   2072 N N     . ILE   A 1 273 ? -32.885 -58.718  -24.575 1.00 42.03  ? 265 ILE   A N     1 
ATOM   2073 C CA    . ILE   A 1 273 ? -33.013 -57.275  -24.507 1.00 42.35  ? 265 ILE   A CA    1 
ATOM   2074 C C     . ILE   A 1 273 ? -33.620 -56.791  -25.820 1.00 43.06  ? 265 ILE   A C     1 
ATOM   2075 O O     . ILE   A 1 273 ? -33.105 -57.104  -26.891 1.00 44.06  ? 265 ILE   A O     1 
ATOM   2076 C CB    . ILE   A 1 273 ? -31.643 -56.632  -24.228 1.00 42.14  ? 265 ILE   A CB    1 
ATOM   2077 C CG1   . ILE   A 1 273 ? -31.158 -56.959  -22.814 1.00 41.32  ? 265 ILE   A CG1   1 
ATOM   2078 C CG2   . ILE   A 1 273 ? -31.675 -55.123  -24.483 1.00 42.19  ? 265 ILE   A CG2   1 
ATOM   2079 C CD1   . ILE   A 1 273 ? -29.700 -56.620  -22.562 1.00 41.37  ? 265 ILE   A CD1   1 
ATOM   2080 N N     . ILE   A 1 274 ? -34.718 -56.032  -25.719 1.00 43.22  ? 266 ILE   A N     1 
ATOM   2081 C CA    . ILE   A 1 274 ? -35.385 -55.460  -26.878 1.00 42.61  ? 266 ILE   A CA    1 
ATOM   2082 C C     . ILE   A 1 274 ? -34.962 -53.999  -26.992 1.00 42.71  ? 266 ILE   A C     1 
ATOM   2083 O O     . ILE   A 1 274 ? -35.074 -53.245  -26.028 1.00 42.12  ? 266 ILE   A O     1 
ATOM   2084 C CB    . ILE   A 1 274 ? -36.915 -55.601  -26.761 1.00 42.51  ? 266 ILE   A CB    1 
ATOM   2085 C CG1   . ILE   A 1 274 ? -37.355 -57.061  -26.590 1.00 41.73  ? 266 ILE   A CG1   1 
ATOM   2086 C CG2   . ILE   A 1 274 ? -37.615 -54.939  -27.949 1.00 42.89  ? 266 ILE   A CG2   1 
ATOM   2087 C CD1   . ILE   A 1 274 ? -37.412 -57.858  -27.879 1.00 42.62  ? 266 ILE   A CD1   1 
ATOM   2088 N N     . THR   A 1 275 ? -34.484 -53.614  -28.181 1.00 43.18  ? 267 THR   A N     1 
ATOM   2089 C CA    . THR   A 1 275 ? -34.028 -52.257  -28.435 1.00 43.26  ? 267 THR   A CA    1 
ATOM   2090 C C     . THR   A 1 275 ? -34.704 -51.734  -29.702 1.00 44.75  ? 267 THR   A C     1 
ATOM   2091 O O     . THR   A 1 275 ? -35.173 -52.517  -30.523 1.00 44.91  ? 267 THR   A O     1 
ATOM   2092 C CB    . THR   A 1 275 ? -32.501 -52.246  -28.527 1.00 42.19  ? 267 THR   A CB    1 
ATOM   2093 O OG1   . THR   A 1 275 ? -32.138 -50.878  -28.681 1.00 42.18  ? 267 THR   A OG1   1 
ATOM   2094 C CG2   . THR   A 1 275 ? -31.958 -53.068  -29.682 1.00 42.30  ? 267 THR   A CG2   1 
ATOM   2095 N N     . GLY   A 1 276 ? -34.770 -50.402  -29.829 1.00 47.53  ? 268 GLY   A N     1 
ATOM   2096 C CA    . GLY   A 1 276 ? -35.357 -49.747  -30.989 1.00 50.60  ? 268 GLY   A CA    1 
ATOM   2097 C C     . GLY   A 1 276 ? -36.810 -49.343  -30.745 1.00 54.62  ? 268 GLY   A C     1 
ATOM   2098 O O     . GLY   A 1 276 ? -37.449 -49.833  -29.816 1.00 56.49  ? 268 GLY   A O     1 
ATOM   2099 N N     . THR   A 1 277 ? -37.321 -48.448  -31.603 1.00 58.08  ? 269 THR   A N     1 
ATOM   2100 C CA    . THR   A 1 277 ? -38.690 -47.962  -31.514 1.00 61.26  ? 269 THR   A CA    1 
ATOM   2101 C C     . THR   A 1 277 ? -39.641 -49.011  -32.083 1.00 65.41  ? 269 THR   A C     1 
ATOM   2102 O O     . THR   A 1 277 ? -39.206 -49.985  -32.696 1.00 63.92  ? 269 THR   A O     1 
ATOM   2103 C CB    . THR   A 1 277 ? -38.833 -46.634  -32.259 1.00 61.14  ? 269 THR   A CB    1 
ATOM   2104 O OG1   . THR   A 1 277 ? -38.500 -46.903  -33.618 1.00 60.66  ? 269 THR   A OG1   1 
ATOM   2105 C CG2   . THR   A 1 277 ? -37.939 -45.543  -31.696 1.00 60.62  ? 269 THR   A CG2   1 
ATOM   2106 N N     . ASN   A 1 278 ? -40.944 -48.783  -31.881 1.00 71.76  ? 270 ASN   A N     1 
ATOM   2107 C CA    . ASN   A 1 278 ? -41.975 -49.682  -32.372 1.00 77.67  ? 270 ASN   A CA    1 
ATOM   2108 C C     . ASN   A 1 278 ? -42.252 -49.381  -33.843 1.00 81.94  ? 270 ASN   A C     1 
ATOM   2109 O O     . ASN   A 1 278 ? -42.697 -48.286  -34.180 1.00 84.97  ? 270 ASN   A O     1 
ATOM   2110 C CB    . ASN   A 1 278 ? -43.257 -49.573  -31.553 1.00 79.68  ? 270 ASN   A CB    1 
ATOM   2111 C CG    . ASN   A 1 278 ? -44.166 -50.763  -31.754 1.00 83.19  ? 270 ASN   A CG    1 
ATOM   2112 O OD1   . ASN   A 1 278 ? -43.941 -51.574  -32.660 1.00 86.26  ? 270 ASN   A OD1   1 
ATOM   2113 N ND2   . ASN   A 1 278 ? -45.196 -50.889  -30.929 1.00 85.05  ? 270 ASN   A ND2   1 
ATOM   2114 N N     . HIS   A 1 279 ? -41.986 -50.370  -34.705 1.00 85.25  ? 271 HIS   A N     1 
ATOM   2115 C CA    . HIS   A 1 279 ? -42.272 -50.269  -36.127 1.00 87.70  ? 271 HIS   A CA    1 
ATOM   2116 C C     . HIS   A 1 279 ? -43.640 -50.884  -36.425 1.00 92.90  ? 271 HIS   A C     1 
ATOM   2117 O O     . HIS   A 1 279 ? -44.278 -50.518  -37.410 1.00 96.52  ? 271 HIS   A O     1 
ATOM   2118 C CB    . HIS   A 1 279 ? -41.129 -50.888  -36.940 1.00 86.47  ? 271 HIS   A CB    1 
ATOM   2119 C CG    . HIS   A 1 279 ? -39.825 -50.178  -36.767 1.00 84.12  ? 271 HIS   A CG    1 
ATOM   2120 N ND1   . HIS   A 1 279 ? -39.742 -48.817  -36.566 1.00 81.90  ? 271 HIS   A ND1   1 
ATOM   2121 C CD2   . HIS   A 1 279 ? -38.564 -50.630  -36.765 1.00 82.51  ? 271 HIS   A CD2   1 
ATOM   2122 C CE1   . HIS   A 1 279 ? -38.470 -48.469  -36.448 1.00 80.73  ? 271 HIS   A CE1   1 
ATOM   2123 N NE2   . HIS   A 1 279 ? -37.737 -49.555  -36.564 1.00 81.35  ? 271 HIS   A NE2   1 
ATOM   2124 N N     . HIS   A 1 280 ? -44.073 -51.826  -35.574 1.00 95.84  ? 272 HIS   A N     1 
ATOM   2125 C CA    . HIS   A 1 280 ? -45.434 -52.338  -35.593 1.00 97.10  ? 272 HIS   A CA    1 
ATOM   2126 C C     . HIS   A 1 280 ? -46.301 -51.478  -34.677 1.00 100.69 ? 272 HIS   A C     1 
ATOM   2127 O O     . HIS   A 1 280 ? -46.617 -51.883  -33.560 1.00 102.72 ? 272 HIS   A O     1 
ATOM   2128 C CB    . HIS   A 1 280 ? -45.461 -53.807  -35.156 1.00 95.58  ? 272 HIS   A CB    1 
ATOM   2129 C CG    . HIS   A 1 280 ? -44.769 -54.729  -36.099 1.00 95.04  ? 272 HIS   A CG    1 
ATOM   2130 N ND1   . HIS   A 1 280 ? -43.406 -54.929  -36.093 1.00 94.41  ? 272 HIS   A ND1   1 
ATOM   2131 C CD2   . HIS   A 1 280 ? -45.252 -55.496  -37.082 1.00 95.72  ? 272 HIS   A CD2   1 
ATOM   2132 C CE1   . HIS   A 1 280 ? -43.088 -55.796  -37.044 1.00 94.41  ? 272 HIS   A CE1   1 
ATOM   2133 N NE2   . HIS   A 1 280 ? -44.196 -56.155  -37.654 1.00 95.84  ? 272 HIS   A NE2   1 
ATOM   2134 N N     . SER   A 1 281 ? -46.684 -50.292  -35.168 1.00 101.46 ? 273 SER   A N     1 
ATOM   2135 C CA    . SER   A 1 281 ? -47.342 -49.286  -34.349 1.00 101.44 ? 273 SER   A CA    1 
ATOM   2136 C C     . SER   A 1 281 ? -48.817 -49.622  -34.126 1.00 104.95 ? 273 SER   A C     1 
ATOM   2137 O O     . SER   A 1 281 ? -49.399 -49.166  -33.144 1.00 104.58 ? 273 SER   A O     1 
ATOM   2138 C CB    . SER   A 1 281 ? -47.180 -47.914  -34.947 1.00 99.49  ? 273 SER   A CB    1 
ATOM   2139 O OG    . SER   A 1 281 ? -45.808 -47.546  -35.001 1.00 98.07  ? 273 SER   A OG    1 
ATOM   2140 N N     . GLU   A 1 282 ? -49.420 -50.407  -35.032 1.00 107.72 ? 274 GLU   A N     1 
ATOM   2141 C CA    . GLU   A 1 282 ? -50.795 -50.850  -34.844 1.00 108.24 ? 274 GLU   A CA    1 
ATOM   2142 C C     . GLU   A 1 282 ? -50.822 -51.894  -33.726 1.00 107.04 ? 274 GLU   A C     1 
ATOM   2143 O O     . GLU   A 1 282 ? -51.799 -51.978  -32.986 1.00 105.71 ? 274 GLU   A O     1 
ATOM   2144 C CB    . GLU   A 1 282 ? -51.467 -51.336  -36.134 1.00 109.62 ? 274 GLU   A CB    1 
ATOM   2145 C CG    . GLU   A 1 282 ? -51.453 -52.847  -36.364 1.00 111.82 ? 274 GLU   A CG    1 
ATOM   2146 C CD    . GLU   A 1 282 ? -50.220 -53.398  -37.057 1.00 114.33 ? 274 GLU   A CD    1 
ATOM   2147 O OE1   . GLU   A 1 282 ? -50.388 -54.130  -38.056 1.00 113.97 ? 274 GLU   A OE1   1 
ATOM   2148 O OE2   . GLU   A 1 282 ? -49.095 -53.095  -36.608 1.00 118.35 ? 274 GLU   A OE2   1 
ATOM   2149 N N     . LYS   A 1 283 ? -49.741 -52.680  -33.617 1.00 107.12 ? 275 LYS   A N     1 
ATOM   2150 C CA    . LYS   A 1 283 ? -49.568 -53.622  -32.523 1.00 106.87 ? 275 LYS   A CA    1 
ATOM   2151 C C     . LYS   A 1 283 ? -48.831 -52.936  -31.375 1.00 107.26 ? 275 LYS   A C     1 
ATOM   2152 O O     . LYS   A 1 283 ? -48.309 -51.834  -31.532 1.00 107.29 ? 275 LYS   A O     1 
ATOM   2153 C CB    . LYS   A 1 283 ? -48.847 -54.886  -33.009 1.00 105.81 ? 275 LYS   A CB    1 
ATOM   2154 C CG    . LYS   A 1 283 ? -49.571 -55.655  -34.113 1.00 105.35 ? 275 LYS   A CG    1 
ATOM   2155 C CD    . LYS   A 1 283 ? -51.022 -56.003  -33.790 1.00 104.27 ? 275 LYS   A CD    1 
ATOM   2156 C CE    . LYS   A 1 283 ? -51.850 -56.367  -34.983 1.00 103.42 ? 275 LYS   A CE    1 
ATOM   2157 N NZ    . LYS   A 1 283 ? -51.689 -57.767  -35.384 1.00 102.86 ? 275 LYS   A NZ    1 
ATOM   2158 N N     . GLU   A 1 284 ? -48.814 -53.603  -30.215 1.00 105.76 ? 276 GLU   A N     1 
ATOM   2159 C CA    . GLU   A 1 284 ? -48.217 -53.056  -29.008 1.00 103.03 ? 276 GLU   A CA    1 
ATOM   2160 C C     . GLU   A 1 284 ? -46.742 -53.447  -28.954 1.00 99.53  ? 276 GLU   A C     1 
ATOM   2161 O O     . GLU   A 1 284 ? -46.239 -54.110  -29.858 1.00 99.70  ? 276 GLU   A O     1 
ATOM   2162 C CB    . GLU   A 1 284 ? -48.969 -53.565  -27.777 1.00 103.59 ? 276 GLU   A CB    1 
ATOM   2163 C CG    . GLU   A 1 284 ? -50.482 -53.388  -27.870 1.00 103.38 ? 276 GLU   A CG    1 
ATOM   2164 C CD    . GLU   A 1 284 ? -51.206 -53.575  -26.550 1.00 103.66 ? 276 GLU   A CD    1 
ATOM   2165 O OE1   . GLU   A 1 284 ? -51.056 -54.654  -25.939 1.00 103.55 ? 276 GLU   A OE1   1 
ATOM   2166 O OE2   . GLU   A 1 284 ? -51.920 -52.640  -26.131 1.00 104.41 ? 276 GLU   A OE2   1 
ATOM   2167 N N     . PHE   A 1 285 ? -46.058 -53.020  -27.886 1.00 96.08  ? 277 PHE   A N     1 
ATOM   2168 C CA    . PHE   A 1 285 ? -44.652 -53.335  -27.698 1.00 92.27  ? 277 PHE   A CA    1 
ATOM   2169 C C     . PHE   A 1 285 ? -44.512 -54.619  -26.882 1.00 87.33  ? 277 PHE   A C     1 
ATOM   2170 O O     . PHE   A 1 285 ? -43.426 -55.191  -26.808 1.00 84.34  ? 277 PHE   A O     1 
ATOM   2171 C CB    . PHE   A 1 285 ? -43.922 -52.163  -27.037 1.00 91.78  ? 277 PHE   A CB    1 
ATOM   2172 C CG    . PHE   A 1 285 ? -42.485 -52.057  -27.520 1.00 90.33  ? 277 PHE   A CG    1 
ATOM   2173 C CD1   . PHE   A 1 285 ? -42.194 -51.390  -28.703 1.00 90.89  ? 277 PHE   A CD1   1 
ATOM   2174 C CD2   . PHE   A 1 285 ? -41.441 -52.656  -26.824 1.00 90.64  ? 277 PHE   A CD2   1 
ATOM   2175 C CE1   . PHE   A 1 285 ? -40.892 -51.303  -29.168 1.00 92.03  ? 277 PHE   A CE1   1 
ATOM   2176 C CE2   . PHE   A 1 285 ? -40.140 -52.568  -27.293 1.00 91.45  ? 277 PHE   A CE2   1 
ATOM   2177 C CZ    . PHE   A 1 285 ? -39.868 -51.893  -28.464 1.00 91.41  ? 277 PHE   A CZ    1 
ATOM   2178 N N     . CYS   A 1 286 ? -45.617 -55.056  -26.267 1.00 84.21  ? 278 CYS   A N     1 
ATOM   2179 C CA    . CYS   A 1 286 ? -45.675 -56.357  -25.623 1.00 83.58  ? 278 CYS   A CA    1 
ATOM   2180 C C     . CYS   A 1 286 ? -45.814 -57.454  -26.680 1.00 79.78  ? 278 CYS   A C     1 
ATOM   2181 O O     . CYS   A 1 286 ? -45.587 -58.624  -26.382 1.00 78.78  ? 278 CYS   A O     1 
ATOM   2182 C CB    . CYS   A 1 286 ? -46.794 -56.399  -24.589 1.00 84.95  ? 278 CYS   A CB    1 
ATOM   2183 S SG    . CYS   A 1 286 ? -48.427 -55.991  -25.259 1.00 88.92  ? 278 CYS   A SG    1 
ATOM   2184 N N     . SER   A 1 287 ? -46.174 -57.069  -27.914 1.00 75.64  ? 279 SER   A N     1 
ATOM   2185 C CA    . SER   A 1 287 ? -46.338 -58.012  -29.011 1.00 72.23  ? 279 SER   A CA    1 
ATOM   2186 C C     . SER   A 1 287 ? -44.992 -58.611  -29.417 1.00 69.05  ? 279 SER   A C     1 
ATOM   2187 O O     . SER   A 1 287 ? -44.930 -59.777  -29.800 1.00 67.81  ? 279 SER   A O     1 
ATOM   2188 C CB    . SER   A 1 287 ? -47.021 -57.366  -30.193 1.00 71.59  ? 279 SER   A CB    1 
ATOM   2189 O OG    . SER   A 1 287 ? -46.166 -56.432  -30.838 1.00 71.00  ? 279 SER   A OG    1 
ATOM   2190 N N     . TYR   A 1 288 ? -43.927 -57.799  -29.355 1.00 66.86  ? 280 TYR   A N     1 
ATOM   2191 C CA    . TYR   A 1 288 ? -42.574 -58.284  -29.581 1.00 64.41  ? 280 TYR   A CA    1 
ATOM   2192 C C     . TYR   A 1 288 ? -42.227 -59.316  -28.512 1.00 63.33  ? 280 TYR   A C     1 
ATOM   2193 O O     . TYR   A 1 288 ? -41.802 -60.426  -28.825 1.00 61.69  ? 280 TYR   A O     1 
ATOM   2194 C CB    . TYR   A 1 288 ? -41.528 -57.166  -29.531 1.00 62.69  ? 280 TYR   A CB    1 
ATOM   2195 C CG    . TYR   A 1 288 ? -41.552 -56.186  -30.695 1.00 61.04  ? 280 TYR   A CG    1 
ATOM   2196 C CD1   . TYR   A 1 288 ? -41.001 -56.522  -31.926 1.00 60.13  ? 280 TYR   A CD1   1 
ATOM   2197 C CD2   . TYR   A 1 288 ? -42.090 -54.912  -30.552 1.00 60.72  ? 280 TYR   A CD2   1 
ATOM   2198 C CE1   . TYR   A 1 288 ? -41.006 -55.630  -32.986 1.00 61.02  ? 280 TYR   A CE1   1 
ATOM   2199 C CE2   . TYR   A 1 288 ? -42.099 -54.010  -31.603 1.00 60.48  ? 280 TYR   A CE2   1 
ATOM   2200 C CZ    . TYR   A 1 288 ? -41.556 -54.370  -32.825 1.00 60.93  ? 280 TYR   A CZ    1 
ATOM   2201 O OH    . TYR   A 1 288 ? -41.563 -53.488  -33.868 1.00 60.35  ? 280 TYR   A OH    1 
ATOM   2202 N N     . LEU   A 1 289 ? -42.428 -58.922  -27.250 1.00 63.66  ? 281 LEU   A N     1 
ATOM   2203 C CA    . LEU   A 1 289 ? -42.074 -59.738  -26.100 1.00 62.59  ? 281 LEU   A CA    1 
ATOM   2204 C C     . LEU   A 1 289 ? -42.924 -61.007  -26.065 1.00 62.86  ? 281 LEU   A C     1 
ATOM   2205 O O     . LEU   A 1 289 ? -42.459 -62.053  -25.615 1.00 61.49  ? 281 LEU   A O     1 
ATOM   2206 C CB    . LEU   A 1 289 ? -42.262 -58.881  -24.848 1.00 62.49  ? 281 LEU   A CB    1 
ATOM   2207 C CG    . LEU   A 1 289 ? -41.719 -59.450  -23.533 1.00 62.27  ? 281 LEU   A CG    1 
ATOM   2208 C CD1   . LEU   A 1 289 ? -40.280 -59.919  -23.652 1.00 62.67  ? 281 LEU   A CD1   1 
ATOM   2209 C CD2   . LEU   A 1 289 ? -41.839 -58.396  -22.445 1.00 62.25  ? 281 LEU   A CD2   1 
ATOM   2210 N N     . GLN   A 1 290 ? -44.169 -60.902  -26.543 1.00 64.73  ? 282 GLN   A N     1 
ATOM   2211 C CA    . GLN   A 1 290 ? -45.072 -62.039  -26.620 1.00 66.73  ? 282 GLN   A CA    1 
ATOM   2212 C C     . GLN   A 1 290 ? -44.521 -63.086  -27.584 1.00 65.29  ? 282 GLN   A C     1 
ATOM   2213 O O     . GLN   A 1 290 ? -44.695 -64.281  -27.357 1.00 64.22  ? 282 GLN   A O     1 
ATOM   2214 C CB    . GLN   A 1 290 ? -46.473 -61.610  -27.058 1.00 69.15  ? 282 GLN   A CB    1 
ATOM   2215 C CG    . GLN   A 1 290 ? -47.338 -61.073  -25.923 1.00 71.41  ? 282 GLN   A CG    1 
ATOM   2216 C CD    . GLN   A 1 290 ? -48.452 -60.169  -26.407 1.00 74.23  ? 282 GLN   A CD    1 
ATOM   2217 O OE1   . GLN   A 1 290 ? -49.191 -60.501  -27.341 1.00 74.92  ? 282 GLN   A OE1   1 
ATOM   2218 N NE2   . GLN   A 1 290 ? -48.575 -59.005  -25.784 1.00 75.18  ? 282 GLN   A NE2   1 
ATOM   2219 N N     . TYR   A 1 291 ? -43.866 -62.632  -28.658 1.00 65.51  ? 283 TYR   A N     1 
ATOM   2220 C CA    . TYR   A 1 291 ? -43.308 -63.552  -29.634 1.00 66.46  ? 283 TYR   A CA    1 
ATOM   2221 C C     . TYR   A 1 291 ? -42.239 -64.412  -28.961 1.00 68.52  ? 283 TYR   A C     1 
ATOM   2222 O O     . TYR   A 1 291 ? -42.154 -65.607  -29.231 1.00 69.62  ? 283 TYR   A O     1 
ATOM   2223 C CB    . TYR   A 1 291 ? -42.731 -62.852  -30.869 1.00 65.78  ? 283 TYR   A CB    1 
ATOM   2224 C CG    . TYR   A 1 291 ? -42.399 -63.828  -31.991 1.00 65.97  ? 283 TYR   A CG    1 
ATOM   2225 C CD1   . TYR   A 1 291 ? -43.349 -64.728  -32.464 1.00 65.91  ? 283 TYR   A CD1   1 
ATOM   2226 C CD2   . TYR   A 1 291 ? -41.123 -63.892  -32.535 1.00 66.78  ? 283 TYR   A CD2   1 
ATOM   2227 C CE1   . TYR   A 1 291 ? -43.051 -65.636  -33.467 1.00 65.86  ? 283 TYR   A CE1   1 
ATOM   2228 C CE2   . TYR   A 1 291 ? -40.812 -64.798  -33.536 1.00 67.03  ? 283 TYR   A CE2   1 
ATOM   2229 C CZ    . TYR   A 1 291 ? -41.777 -65.672  -34.004 1.00 66.79  ? 283 TYR   A CZ    1 
ATOM   2230 O OH    . TYR   A 1 291 ? -41.467 -66.561  -34.993 1.00 68.01  ? 283 TYR   A OH    1 
ATOM   2231 N N     . LEU   A 1 292 ? -41.433 -63.800  -28.081 1.00 69.22  ? 284 LEU   A N     1 
ATOM   2232 C CA    . LEU   A 1 292 ? -40.384 -64.514  -27.368 1.00 68.65  ? 284 LEU   A CA    1 
ATOM   2233 C C     . LEU   A 1 292 ? -41.011 -65.511  -26.400 1.00 68.40  ? 284 LEU   A C     1 
ATOM   2234 O O     . LEU   A 1 292 ? -40.678 -66.694  -26.422 1.00 66.23  ? 284 LEU   A O     1 
ATOM   2235 C CB    . LEU   A 1 292 ? -39.472 -63.550  -26.614 1.00 68.87  ? 284 LEU   A CB    1 
ATOM   2236 C CG    . LEU   A 1 292 ? -38.659 -62.570  -27.464 1.00 69.80  ? 284 LEU   A CG    1 
ATOM   2237 C CD1   . LEU   A 1 292 ? -37.814 -61.701  -26.549 1.00 69.97  ? 284 LEU   A CD1   1 
ATOM   2238 C CD2   . LEU   A 1 292 ? -37.788 -63.284  -28.486 1.00 69.50  ? 284 LEU   A CD2   1 
ATOM   2239 N N     . GLU   A 1 293 ? -41.902 -65.004  -25.540 1.00 70.24  ? 285 GLU   A N     1 
ATOM   2240 C CA    . GLU   A 1 293 ? -42.639 -65.841  -24.610 1.00 71.37  ? 285 GLU   A CA    1 
ATOM   2241 C C     . GLU   A 1 293 ? -43.218 -67.026  -25.379 1.00 70.37  ? 285 GLU   A C     1 
ATOM   2242 O O     . GLU   A 1 293 ? -43.123 -68.161  -24.924 1.00 71.85  ? 285 GLU   A O     1 
ATOM   2243 C CB    . GLU   A 1 293 ? -43.728 -65.036  -23.897 1.00 72.59  ? 285 GLU   A CB    1 
ATOM   2244 C CG    . GLU   A 1 293 ? -43.193 -63.991  -22.919 1.00 72.81  ? 285 GLU   A CG    1 
ATOM   2245 C CD    . GLU   A 1 293 ? -42.629 -64.530  -21.613 1.00 74.72  ? 285 GLU   A CD    1 
ATOM   2246 O OE1   . GLU   A 1 293 ? -42.617 -65.765  -21.411 1.00 76.13  ? 285 GLU   A OE1   1 
ATOM   2247 O OE2   . GLU   A 1 293 ? -42.201 -63.697  -20.785 1.00 74.06  ? 285 GLU   A OE2   1 
ATOM   2248 N N     . TYR   A 1 294 ? -43.775 -66.746  -26.565 1.00 68.92  ? 286 TYR   A N     1 
ATOM   2249 C CA    . TYR   A 1 294 ? -44.386 -67.765  -27.405 1.00 68.91  ? 286 TYR   A CA    1 
ATOM   2250 C C     . TYR   A 1 294 ? -43.359 -68.832  -27.782 1.00 67.97  ? 286 TYR   A C     1 
ATOM   2251 O O     . TYR   A 1 294 ? -43.607 -70.017  -27.575 1.00 68.90  ? 286 TYR   A O     1 
ATOM   2252 C CB    . TYR   A 1 294 ? -45.039 -67.116  -28.631 1.00 69.27  ? 286 TYR   A CB    1 
ATOM   2253 C CG    . TYR   A 1 294 ? -45.314 -68.078  -29.778 1.00 70.81  ? 286 TYR   A CG    1 
ATOM   2254 C CD1   . TYR   A 1 294 ? -46.242 -69.106  -29.647 1.00 70.76  ? 286 TYR   A CD1   1 
ATOM   2255 C CD2   . TYR   A 1 294 ? -44.653 -67.950  -30.996 1.00 71.21  ? 286 TYR   A CD2   1 
ATOM   2256 C CE1   . TYR   A 1 294 ? -46.491 -69.988  -30.686 1.00 70.75  ? 286 TYR   A CE1   1 
ATOM   2257 C CE2   . TYR   A 1 294 ? -44.897 -68.824  -32.043 1.00 71.09  ? 286 TYR   A CE2   1 
ATOM   2258 C CZ    . TYR   A 1 294 ? -45.818 -69.845  -31.888 1.00 70.93  ? 286 TYR   A CZ    1 
ATOM   2259 O OH    . TYR   A 1 294 ? -46.062 -70.705  -32.918 1.00 71.27  ? 286 TYR   A OH    1 
ATOM   2260 N N     . LEU   A 1 295 ? -42.211 -68.409  -28.329 1.00 67.26  ? 287 LEU   A N     1 
ATOM   2261 C CA    . LEU   A 1 295 ? -41.171 -69.337  -28.754 1.00 68.03  ? 287 LEU   A CA    1 
ATOM   2262 C C     . LEU   A 1 295 ? -40.692 -70.174  -27.566 1.00 70.29  ? 287 LEU   A C     1 
ATOM   2263 O O     . LEU   A 1 295 ? -40.351 -71.343  -27.732 1.00 69.87  ? 287 LEU   A O     1 
ATOM   2264 C CB    . LEU   A 1 295 ? -40.001 -68.591  -29.398 1.00 66.73  ? 287 LEU   A CB    1 
ATOM   2265 C CG    . LEU   A 1 295 ? -40.281 -67.875  -30.725 1.00 65.52  ? 287 LEU   A CG    1 
ATOM   2266 C CD1   . LEU   A 1 295 ? -39.057 -67.090  -31.158 1.00 65.14  ? 287 LEU   A CD1   1 
ATOM   2267 C CD2   . LEU   A 1 295 ? -40.700 -68.828  -31.829 1.00 65.89  ? 287 LEU   A CD2   1 
ATOM   2268 N N     . SER   A 1 296 ? -40.685 -69.566  -26.373 1.00 71.97  ? 288 SER   A N     1 
ATOM   2269 C CA    . SER   A 1 296 ? -40.074 -70.147  -25.187 1.00 72.51  ? 288 SER   A CA    1 
ATOM   2270 C C     . SER   A 1 296 ? -40.783 -71.424  -24.734 1.00 74.65  ? 288 SER   A C     1 
ATOM   2271 O O     . SER   A 1 296 ? -40.117 -72.346  -24.272 1.00 75.95  ? 288 SER   A O     1 
ATOM   2272 C CB    . SER   A 1 296 ? -40.010 -69.135  -24.076 1.00 72.09  ? 288 SER   A CB    1 
ATOM   2273 O OG    . SER   A 1 296 ? -39.782 -69.755  -22.818 1.00 72.45  ? 288 SER   A OG    1 
ATOM   2274 N N     . GLN   A 1 297 ? -42.120 -71.469  -24.831 1.00 75.64  ? 289 GLN   A N     1 
ATOM   2275 C CA    . GLN   A 1 297 ? -42.860 -72.692  -24.546 1.00 75.96  ? 289 GLN   A CA    1 
ATOM   2276 C C     . GLN   A 1 297 ? -42.830 -73.603  -25.770 1.00 76.13  ? 289 GLN   A C     1 
ATOM   2277 O O     . GLN   A 1 297 ? -42.849 -74.824  -25.637 1.00 75.86  ? 289 GLN   A O     1 
ATOM   2278 C CB    . GLN   A 1 297 ? -44.329 -72.495  -24.171 1.00 76.49  ? 289 GLN   A CB    1 
ATOM   2279 C CG    . GLN   A 1 297 ? -44.554 -71.743  -22.863 1.00 77.70  ? 289 GLN   A CG    1 
ATOM   2280 C CD    . GLN   A 1 297 ? -44.571 -70.241  -23.037 1.00 78.04  ? 289 GLN   A CD    1 
ATOM   2281 O OE1   . GLN   A 1 297 ? -44.478 -69.723  -24.154 1.00 79.47  ? 289 GLN   A OE1   1 
ATOM   2282 N NE2   . GLN   A 1 297 ? -44.717 -69.521  -21.934 1.00 77.58  ? 289 GLN   A NE2   1 
ATOM   2283 N N     . ASN   A 1 298 ? -42.785 -72.989  -26.958 1.00 78.93  ? 290 ASN   A N     1 
ATOM   2284 C CA    . ASN   A 1 298 ? -42.694 -73.717  -28.214 1.00 82.05  ? 290 ASN   A CA    1 
ATOM   2285 C C     . ASN   A 1 298 ? -41.323 -74.375  -28.366 1.00 83.38  ? 290 ASN   A C     1 
ATOM   2286 O O     . ASN   A 1 298 ? -41.073 -75.034  -29.373 1.00 82.83  ? 290 ASN   A O     1 
ATOM   2287 C CB    . ASN   A 1 298 ? -42.984 -72.808  -29.404 1.00 84.14  ? 290 ASN   A CB    1 
ATOM   2288 C CG    . ASN   A 1 298 ? -44.461 -72.533  -29.571 1.00 86.36  ? 290 ASN   A CG    1 
ATOM   2289 O OD1   . ASN   A 1 298 ? -45.132 -72.123  -28.617 1.00 85.83  ? 290 ASN   A OD1   1 
ATOM   2290 N ND2   . ASN   A 1 298 ? -44.987 -72.761  -30.765 1.00 88.01  ? 290 ASN   A ND2   1 
ATOM   2291 N N     . ARG   A 1 299 ? -40.434 -74.186  -27.381 1.00 84.69  ? 291 ARG   A N     1 
ATOM   2292 C CA    . ARG   A 1 299 ? -39.147 -74.861  -27.377 1.00 84.51  ? 291 ARG   A CA    1 
ATOM   2293 C C     . ARG   A 1 299 ? -39.388 -76.370  -27.400 1.00 87.49  ? 291 ARG   A C     1 
ATOM   2294 O O     . ARG   A 1 299 ? -40.261 -76.865  -26.688 1.00 87.67  ? 291 ARG   A O     1 
ATOM   2295 C CB    . ARG   A 1 299 ? -38.284 -74.421  -26.186 1.00 82.01  ? 291 ARG   A CB    1 
ATOM   2296 C CG    . ARG   A 1 299 ? -38.678 -74.954  -24.815 1.00 79.84  ? 291 ARG   A CG    1 
ATOM   2297 C CD    . ARG   A 1 299 ? -37.640 -74.603  -23.759 1.00 79.05  ? 291 ARG   A CD    1 
ATOM   2298 N NE    . ARG   A 1 299 ? -37.543 -73.168  -23.464 1.00 77.74  ? 291 ARG   A NE    1 
ATOM   2299 C CZ    . ARG   A 1 299 ? -36.590 -72.601  -22.728 1.00 75.86  ? 291 ARG   A CZ    1 
ATOM   2300 N NH1   . ARG   A 1 299 ? -35.563 -73.311  -22.288 1.00 75.02  ? 291 ARG   A NH1   1 
ATOM   2301 N NH2   . ARG   A 1 299 ? -36.652 -71.310  -22.449 1.00 76.22  ? 291 ARG   A NH2   1 
ATOM   2302 N N     . PRO   A 1 300 ? -38.648 -77.142  -28.232 1.00 90.35  ? 292 PRO   A N     1 
ATOM   2303 C CA    . PRO   A 1 300 ? -38.846 -78.591  -28.312 1.00 92.17  ? 292 PRO   A CA    1 
ATOM   2304 C C     . PRO   A 1 300 ? -38.683 -79.241  -26.939 1.00 96.17  ? 292 PRO   A C     1 
ATOM   2305 O O     . PRO   A 1 300 ? -37.714 -78.957  -26.239 1.00 97.93  ? 292 PRO   A O     1 
ATOM   2306 C CB    . PRO   A 1 300 ? -37.793 -79.077  -29.331 1.00 90.22  ? 292 PRO   A CB    1 
ATOM   2307 C CG    . PRO   A 1 300 ? -36.812 -77.928  -29.461 1.00 89.23  ? 292 PRO   A CG    1 
ATOM   2308 C CD    . PRO   A 1 300 ? -37.592 -76.665  -29.141 1.00 89.03  ? 292 PRO   A CD    1 
ATOM   2309 N N     . PRO   A 1 301 ? -39.629 -80.110  -26.504 1.00 101.06 ? 293 PRO   A N     1 
ATOM   2310 C CA    . PRO   A 1 301 ? -39.577 -80.713  -25.168 1.00 103.67 ? 293 PRO   A CA    1 
ATOM   2311 C C     . PRO   A 1 301 ? -38.206 -81.253  -24.760 1.00 105.79 ? 293 PRO   A C     1 
ATOM   2312 O O     . PRO   A 1 301 ? -37.495 -81.830  -25.582 1.00 105.05 ? 293 PRO   A O     1 
ATOM   2313 C CB    . PRO   A 1 301 ? -40.626 -81.836  -25.263 1.00 102.81 ? 293 PRO   A CB    1 
ATOM   2314 C CG    . PRO   A 1 301 ? -41.636 -81.318  -26.258 1.00 101.87 ? 293 PRO   A CG    1 
ATOM   2315 C CD    . PRO   A 1 301 ? -40.815 -80.535  -27.268 1.00 101.66 ? 293 PRO   A CD    1 
ATOM   2316 N N     . PRO   A 1 302 ? -37.801 -81.093  -23.477 1.00 105.44 ? 294 PRO   A N     1 
ATOM   2317 C CA    . PRO   A 1 302 ? -36.500 -81.581  -23.010 1.00 104.02 ? 294 PRO   A CA    1 
ATOM   2318 C C     . PRO   A 1 302 ? -36.466 -83.105  -22.916 1.00 103.01 ? 294 PRO   A C     1 
ATOM   2319 O O     . PRO   A 1 302 ? -37.423 -83.716  -22.445 1.00 104.78 ? 294 PRO   A O     1 
ATOM   2320 C CB    . PRO   A 1 302 ? -36.355 -80.900  -21.638 1.00 104.40 ? 294 PRO   A CB    1 
ATOM   2321 C CG    . PRO   A 1 302 ? -37.780 -80.747  -21.155 1.00 104.95 ? 294 PRO   A CG    1 
ATOM   2322 C CD    . PRO   A 1 302 ? -38.583 -80.448  -22.408 1.00 105.27 ? 294 PRO   A CD    1 
ATOM   2323 N N     . ASN   A 1 303 ? -35.352 -83.704  -23.359 1.00 100.16 ? 295 ASN   A N     1 
ATOM   2324 C CA    . ASN   A 1 303 ? -35.223 -85.154  -23.423 1.00 98.64  ? 295 ASN   A CA    1 
ATOM   2325 C C     . ASN   A 1 303 ? -35.044 -85.707  -22.008 1.00 97.34  ? 295 ASN   A C     1 
ATOM   2326 O O     . ASN   A 1 303 ? -35.128 -84.962  -21.034 1.00 94.95  ? 295 ASN   A O     1 
ATOM   2327 C CB    . ASN   A 1 303 ? -34.158 -85.567  -24.439 1.00 98.18  ? 295 ASN   A CB    1 
ATOM   2328 C CG    . ASN   A 1 303 ? -32.754 -85.147  -24.068 1.00 99.16  ? 295 ASN   A CG    1 
ATOM   2329 O OD1   . ASN   A 1 303 ? -32.452 -84.923  -22.891 1.00 97.46  ? 295 ASN   A OD1   1 
ATOM   2330 N ND2   . ASN   A 1 303 ? -31.871 -85.066  -25.054 1.00 99.64  ? 295 ASN   A ND2   1 
ATOM   2331 N N     . ALA   A 1 304 ? -34.823 -87.025  -21.906 1.00 96.96  ? 296 ALA   A N     1 
ATOM   2332 C CA    . ALA   A 1 304 ? -34.819 -87.726  -20.630 1.00 94.87  ? 296 ALA   A CA    1 
ATOM   2333 C C     . ALA   A 1 304 ? -33.575 -87.374  -19.818 1.00 95.53  ? 296 ALA   A C     1 
ATOM   2334 O O     . ALA   A 1 304 ? -33.669 -87.188  -18.607 1.00 96.78  ? 296 ALA   A O     1 
ATOM   2335 C CB    . ALA   A 1 304 ? -34.921 -89.217  -20.860 1.00 92.86  ? 296 ALA   A CB    1 
ATOM   2336 N N     . TYR   A 1 305 ? -32.417 -87.303  -20.488 1.00 93.22  ? 297 TYR   A N     1 
ATOM   2337 C CA    . TYR   A 1 305 ? -31.182 -86.869  -19.853 1.00 90.17  ? 297 TYR   A CA    1 
ATOM   2338 C C     . TYR   A 1 305 ? -31.326 -85.410  -19.423 1.00 88.95  ? 297 TYR   A C     1 
ATOM   2339 O O     . TYR   A 1 305 ? -30.815 -85.022  -18.376 1.00 88.06  ? 297 TYR   A O     1 
ATOM   2340 C CB    . TYR   A 1 305 ? -29.985 -87.059  -20.789 1.00 88.65  ? 297 TYR   A CB    1 
ATOM   2341 C CG    . TYR   A 1 305 ? -28.632 -86.972  -20.096 1.00 88.10  ? 297 TYR   A CG    1 
ATOM   2342 C CD1   . TYR   A 1 305 ? -28.019 -85.747  -19.854 1.00 86.15  ? 297 TYR   A CD1   1 
ATOM   2343 C CD2   . TYR   A 1 305 ? -27.968 -88.121  -19.684 1.00 87.05  ? 297 TYR   A CD2   1 
ATOM   2344 C CE1   . TYR   A 1 305 ? -26.789 -85.668  -19.220 1.00 83.62  ? 297 TYR   A CE1   1 
ATOM   2345 C CE2   . TYR   A 1 305 ? -26.737 -88.055  -19.052 1.00 86.02  ? 297 TYR   A CE2   1 
ATOM   2346 C CZ    . TYR   A 1 305 ? -26.146 -86.827  -18.821 1.00 83.90  ? 297 TYR   A CZ    1 
ATOM   2347 O OH    . TYR   A 1 305 ? -24.933 -86.772  -18.204 1.00 82.22  ? 297 TYR   A OH    1 
ATOM   2348 N N     . GLU   A 1 306 ? -32.012 -84.609  -20.250 1.00 87.54  ? 298 GLU   A N     1 
ATOM   2349 C CA    . GLU   A 1 306 ? -32.444 -83.276  -19.859 1.00 85.53  ? 298 GLU   A CA    1 
ATOM   2350 C C     . GLU   A 1 306 ? -33.550 -83.413  -18.817 1.00 85.21  ? 298 GLU   A C     1 
ATOM   2351 O O     . GLU   A 1 306 ? -34.174 -84.464  -18.702 1.00 87.00  ? 298 GLU   A O     1 
ATOM   2352 C CB    . GLU   A 1 306 ? -32.915 -82.465  -21.066 1.00 84.65  ? 298 GLU   A CB    1 
ATOM   2353 C CG    . GLU   A 1 306 ? -31.770 -81.989  -21.956 1.00 83.28  ? 298 GLU   A CG    1 
ATOM   2354 C CD    . GLU   A 1 306 ? -32.181 -81.673  -23.382 1.00 83.23  ? 298 GLU   A CD    1 
ATOM   2355 O OE1   . GLU   A 1 306 ? -31.538 -82.205  -24.311 1.00 83.98  ? 298 GLU   A OE1   1 
ATOM   2356 O OE2   . GLU   A 1 306 ? -33.151 -80.910  -23.568 1.00 83.97  ? 298 GLU   A OE2   1 
ATOM   2357 N N     . LEU   A 1 307 ? -33.766 -82.343  -18.048 1.00 84.02  ? 299 LEU   A N     1 
ATOM   2358 C CA    . LEU   A 1 307 ? -34.571 -82.398  -16.838 1.00 83.95  ? 299 LEU   A CA    1 
ATOM   2359 C C     . LEU   A 1 307 ? -33.771 -83.096  -15.742 1.00 82.73  ? 299 LEU   A C     1 
ATOM   2360 O O     . LEU   A 1 307 ? -34.202 -83.108  -14.593 1.00 83.16  ? 299 LEU   A O     1 
ATOM   2361 C CB    . LEU   A 1 307 ? -35.937 -83.068  -17.009 1.00 85.19  ? 299 LEU   A CB    1 
ATOM   2362 C CG    . LEU   A 1 307 ? -36.842 -82.556  -18.137 1.00 84.26  ? 299 LEU   A CG    1 
ATOM   2363 C CD1   . LEU   A 1 307 ? -37.998 -83.516  -18.336 1.00 82.92  ? 299 LEU   A CD1   1 
ATOM   2364 C CD2   . LEU   A 1 307 ? -37.389 -81.168  -17.876 1.00 83.76  ? 299 LEU   A CD2   1 
ATOM   2365 N N     . PHE   A 1 308 ? -32.652 -83.728  -16.123 1.00 82.72  ? 300 PHE   A N     1 
ATOM   2366 C CA    . PHE   A 1 308 ? -31.600 -84.115  -15.200 1.00 83.31  ? 300 PHE   A CA    1 
ATOM   2367 C C     . PHE   A 1 308 ? -30.409 -83.205  -15.486 1.00 81.06  ? 300 PHE   A C     1 
ATOM   2368 O O     . PHE   A 1 308 ? -30.056 -83.006  -16.646 1.00 81.92  ? 300 PHE   A O     1 
ATOM   2369 C CB    . PHE   A 1 308 ? -31.213 -85.592  -15.339 1.00 85.69  ? 300 PHE   A CB    1 
ATOM   2370 C CG    . PHE   A 1 308 ? -32.361 -86.584  -15.494 1.00 88.05  ? 300 PHE   A CG    1 
ATOM   2371 C CD1   . PHE   A 1 308 ? -33.650 -86.289  -15.053 1.00 88.56  ? 300 PHE   A CD1   1 
ATOM   2372 C CD2   . PHE   A 1 308 ? -32.139 -87.829  -16.074 1.00 90.55  ? 300 PHE   A CD2   1 
ATOM   2373 C CE1   . PHE   A 1 308 ? -34.680 -87.206  -15.200 1.00 89.51  ? 300 PHE   A CE1   1 
ATOM   2374 C CE2   . PHE   A 1 308 ? -33.172 -88.745  -16.214 1.00 90.56  ? 300 PHE   A CE2   1 
ATOM   2375 C CZ    . PHE   A 1 308 ? -34.440 -88.432  -15.779 1.00 90.42  ? 300 PHE   A CZ    1 
ATOM   2376 N N     . ALA   A 1 309 ? -29.814 -82.635  -14.432 1.00 78.55  ? 301 ALA   A N     1 
ATOM   2377 C CA    . ALA   A 1 309 ? -28.682 -81.735  -14.582 1.00 76.11  ? 301 ALA   A CA    1 
ATOM   2378 C C     . ALA   A 1 309 ? -29.122 -80.359  -15.072 1.00 74.19  ? 301 ALA   A C     1 
ATOM   2379 O O     . ALA   A 1 309 ? -28.301 -79.613  -15.598 1.00 75.38  ? 301 ALA   A O     1 
ATOM   2380 C CB    . ALA   A 1 309 ? -27.652 -82.333  -15.514 1.00 75.37  ? 301 ALA   A CB    1 
ATOM   2381 N N     . LYS   A 1 310 ? -30.405 -80.020  -14.889 1.00 72.91  ? 302 LYS   A N     1 
ATOM   2382 C CA    . LYS   A 1 310 ? -30.856 -78.655  -15.108 1.00 72.38  ? 302 LYS   A CA    1 
ATOM   2383 C C     . LYS   A 1 310 ? -30.040 -77.718  -14.221 1.00 67.81  ? 302 LYS   A C     1 
ATOM   2384 O O     . LYS   A 1 310 ? -29.581 -76.672  -14.675 1.00 66.16  ? 302 LYS   A O     1 
ATOM   2385 C CB    . LYS   A 1 310 ? -32.334 -78.448  -14.766 1.00 74.89  ? 302 LYS   A CB    1 
ATOM   2386 C CG    . LYS   A 1 310 ? -33.353 -79.241  -15.563 1.00 78.54  ? 302 LYS   A CG    1 
ATOM   2387 C CD    . LYS   A 1 310 ? -34.757 -78.940  -15.050 1.00 82.36  ? 302 LYS   A CD    1 
ATOM   2388 C CE    . LYS   A 1 310 ? -35.850 -79.488  -15.897 1.00 84.92  ? 302 LYS   A CE    1 
ATOM   2389 N NZ    . LYS   A 1 310 ? -37.193 -79.092  -15.466 1.00 85.69  ? 302 LYS   A NZ    1 
ATOM   2390 N N     . GLY   A 1 311 ? -29.862 -78.121  -12.956 1.00 62.80  ? 303 GLY   A N     1 
ATOM   2391 C CA    . GLY   A 1 311 ? -29.161 -77.320  -11.966 1.00 60.21  ? 303 GLY   A CA    1 
ATOM   2392 C C     . GLY   A 1 311 ? -27.693 -77.717  -11.817 1.00 57.60  ? 303 GLY   A C     1 
ATOM   2393 O O     . GLY   A 1 311 ? -26.977 -77.110  -11.024 1.00 58.77  ? 303 GLY   A O     1 
ATOM   2394 N N     . TYR   A 1 312 ? -27.247 -78.726  -12.580 1.00 54.27  ? 304 TYR   A N     1 
ATOM   2395 C CA    . TYR   A 1 312 ? -25.867 -79.185  -12.520 1.00 52.78  ? 304 TYR   A CA    1 
ATOM   2396 C C     . TYR   A 1 312 ? -25.077 -78.680  -13.728 1.00 49.61  ? 304 TYR   A C     1 
ATOM   2397 O O     . TYR   A 1 312 ? -23.917 -79.049  -13.893 1.00 49.75  ? 304 TYR   A O     1 
ATOM   2398 C CB    . TYR   A 1 312 ? -25.783 -80.714  -12.451 1.00 53.52  ? 304 TYR   A CB    1 
ATOM   2399 C CG    . TYR   A 1 312 ? -26.390 -81.339  -11.201 1.00 54.37  ? 304 TYR   A CG    1 
ATOM   2400 C CD1   . TYR   A 1 312 ? -25.749 -81.244  -9.969  1.00 54.98  ? 304 TYR   A CD1   1 
ATOM   2401 C CD2   . TYR   A 1 312 ? -27.588 -82.047  -11.252 1.00 54.55  ? 304 TYR   A CD2   1 
ATOM   2402 C CE1   . TYR   A 1 312 ? -26.291 -81.814  -8.827  1.00 54.72  ? 304 TYR   A CE1   1 
ATOM   2403 C CE2   . TYR   A 1 312 ? -28.139 -82.623  -10.119 1.00 55.52  ? 304 TYR   A CE2   1 
ATOM   2404 C CZ    . TYR   A 1 312 ? -27.489 -82.505  -8.903  1.00 55.47  ? 304 TYR   A CZ    1 
ATOM   2405 O OH    . TYR   A 1 312 ? -28.029 -83.073  -7.788  1.00 56.76  ? 304 TYR   A OH    1 
ATOM   2406 N N     . GLU   A 1 313 ? -25.691 -77.821  -14.554 1.00 47.43  ? 305 GLU   A N     1 
ATOM   2407 C CA    . GLU   A 1 313 ? -25.094 -77.407  -15.815 1.00 45.65  ? 305 GLU   A CA    1 
ATOM   2408 C C     . GLU   A 1 313 ? -23.802 -76.640  -15.551 1.00 42.31  ? 305 GLU   A C     1 
ATOM   2409 O O     . GLU   A 1 313 ? -23.815 -75.625  -14.862 1.00 41.49  ? 305 GLU   A O     1 
ATOM   2410 C CB    . GLU   A 1 313 ? -26.043 -76.525  -16.625 1.00 47.11  ? 305 GLU   A CB    1 
ATOM   2411 C CG    . GLU   A 1 313 ? -27.321 -77.245  -17.043 1.00 49.06  ? 305 GLU   A CG    1 
ATOM   2412 C CD    . GLU   A 1 313 ? -28.307 -76.388  -17.811 1.00 51.35  ? 305 GLU   A CD    1 
ATOM   2413 O OE1   . GLU   A 1 313 ? -29.408 -76.897  -18.114 1.00 54.23  ? 305 GLU   A OE1   1 
ATOM   2414 O OE2   . GLU   A 1 313 ? -27.978 -75.220  -18.106 1.00 51.97  ? 305 GLU   A OE2   1 
ATOM   2415 N N     . ASP   A 1 314 ? -22.694 -77.165  -16.090 1.00 39.83  ? 306 ASP   A N     1 
ATOM   2416 C CA    . ASP   A 1 314 ? -21.367 -76.579  -15.958 1.00 38.54  ? 306 ASP   A CA    1 
ATOM   2417 C C     . ASP   A 1 314 ? -20.930 -76.500  -14.491 1.00 38.46  ? 306 ASP   A C     1 
ATOM   2418 O O     . ASP   A 1 314 ? -19.969 -75.801  -14.175 1.00 37.43  ? 306 ASP   A O     1 
ATOM   2419 C CB    . ASP   A 1 314 ? -21.268 -75.243  -16.683 1.00 37.31  ? 306 ASP   A CB    1 
ATOM   2420 C CG    . ASP   A 1 314 ? -21.438 -75.298  -18.196 1.00 37.12  ? 306 ASP   A CG    1 
ATOM   2421 O OD1   . ASP   A 1 314 ? -20.812 -76.175  -18.828 1.00 36.31  ? 306 ASP   A OD1   1 
ATOM   2422 O OD2   . ASP   A 1 314 ? -22.173 -74.443  -18.739 1.00 37.29  ? 306 ASP   A OD2   1 
ATOM   2423 N N     . TYR   A 1 315 ? -21.609 -77.233  -13.598 1.00 38.40  ? 307 TYR   A N     1 
ATOM   2424 C CA    . TYR   A 1 315 ? -21.202 -77.291  -12.204 1.00 38.69  ? 307 TYR   A CA    1 
ATOM   2425 C C     . TYR   A 1 315 ? -20.042 -78.274  -12.076 1.00 37.38  ? 307 TYR   A C     1 
ATOM   2426 O O     . TYR   A 1 315 ? -20.167 -79.429  -12.475 1.00 38.64  ? 307 TYR   A O     1 
ATOM   2427 C CB    . TYR   A 1 315 ? -22.336 -77.701  -11.262 1.00 40.39  ? 307 TYR   A CB    1 
ATOM   2428 C CG    . TYR   A 1 315 ? -21.836 -77.968  -9.849  1.00 43.65  ? 307 TYR   A CG    1 
ATOM   2429 C CD1   . TYR   A 1 315 ? -21.325 -76.935  -9.071  1.00 44.57  ? 307 TYR   A CD1   1 
ATOM   2430 C CD2   . TYR   A 1 315 ? -21.854 -79.246  -9.301  1.00 44.92  ? 307 TYR   A CD2   1 
ATOM   2431 C CE1   . TYR   A 1 315 ? -20.850 -77.162  -7.790  1.00 45.06  ? 307 TYR   A CE1   1 
ATOM   2432 C CE2   . TYR   A 1 315 ? -21.389 -79.483  -8.017  1.00 45.12  ? 307 TYR   A CE2   1 
ATOM   2433 C CZ    . TYR   A 1 315 ? -20.884 -78.439  -7.262  1.00 45.69  ? 307 TYR   A CZ    1 
ATOM   2434 O OH    . TYR   A 1 315 ? -20.419 -78.655  -5.998  1.00 47.34  ? 307 TYR   A OH    1 
ATOM   2435 N N     . LEU   A 1 316 ? -18.927 -77.808  -11.502 1.00 35.61  ? 308 LEU   A N     1 
ATOM   2436 C CA    . LEU   A 1 316 ? -17.710 -78.600  -11.411 1.00 34.85  ? 308 LEU   A CA    1 
ATOM   2437 C C     . LEU   A 1 316 ? -17.700 -79.378  -10.099 1.00 35.64  ? 308 LEU   A C     1 
ATOM   2438 O O     . LEU   A 1 316 ? -17.855 -78.788  -9.033  1.00 35.70  ? 308 LEU   A O     1 
ATOM   2439 C CB    . LEU   A 1 316 ? -16.487 -77.691  -11.509 1.00 33.93  ? 308 LEU   A CB    1 
ATOM   2440 C CG    . LEU   A 1 316 ? -16.192 -77.095  -12.887 1.00 34.33  ? 308 LEU   A CG    1 
ATOM   2441 C CD1   . LEU   A 1 316 ? -15.042 -76.113  -12.773 1.00 34.16  ? 308 LEU   A CD1   1 
ATOM   2442 C CD2   . LEU   A 1 316 ? -15.875 -78.167  -13.919 1.00 34.21  ? 308 LEU   A CD2   1 
ATOM   2443 N N     . GLN   A 1 317 ? -17.507 -80.700  -10.200 1.00 36.70  ? 309 GLN   A N     1 
ATOM   2444 C CA    . GLN   A 1 317 ? -17.313 -81.556  -9.041  1.00 38.56  ? 309 GLN   A CA    1 
ATOM   2445 C C     . GLN   A 1 317 ? -15.979 -82.278  -9.185  1.00 38.69  ? 309 GLN   A C     1 
ATOM   2446 O O     . GLN   A 1 317 ? -15.710 -82.879  -10.221 1.00 36.81  ? 309 GLN   A O     1 
ATOM   2447 C CB    . GLN   A 1 317 ? -18.373 -82.649  -8.900  1.00 40.88  ? 309 GLN   A CB    1 
ATOM   2448 C CG    . GLN   A 1 317 ? -19.755 -82.261  -9.411  1.00 43.45  ? 309 GLN   A CG    1 
ATOM   2449 C CD    . GLN   A 1 317 ? -20.806 -83.300  -9.090  1.00 44.82  ? 309 GLN   A CD    1 
ATOM   2450 O OE1   . GLN   A 1 317 ? -20.770 -84.431  -9.591  1.00 44.92  ? 309 GLN   A OE1   1 
ATOM   2451 N NE2   . GLN   A 1 317 ? -21.748 -82.925  -8.238  1.00 44.97  ? 309 GLN   A NE2   1 
ATOM   2452 N N     . SER   A 1 318 ? -15.169 -82.234  -8.125  1.00 41.23  ? 310 SER   A N     1 
ATOM   2453 C CA    . SER   A 1 318 ? -13.920 -82.970  -8.072  1.00 43.83  ? 310 SER   A CA    1 
ATOM   2454 C C     . SER   A 1 318 ? -14.256 -84.432  -7.803  1.00 44.66  ? 310 SER   A C     1 
ATOM   2455 O O     . SER   A 1 318 ? -14.920 -84.716  -6.812  1.00 45.99  ? 310 SER   A O     1 
ATOM   2456 C CB    . SER   A 1 318 ? -13.000 -82.419  -7.009  1.00 45.09  ? 310 SER   A CB    1 
ATOM   2457 O OG    . SER   A 1 318 ? -12.523 -81.128  -7.359  1.00 45.99  ? 310 SER   A OG    1 
ATOM   2458 N N     . PRO   A 1 319 ? -13.880 -85.391  -8.683  1.00 47.84  ? 311 PRO   A N     1 
ATOM   2459 C CA    . PRO   A 1 319 ? -14.130 -86.809  -8.425  1.00 49.80  ? 311 PRO   A CA    1 
ATOM   2460 C C     . PRO   A 1 319 ? -13.397 -87.281  -7.171  1.00 53.23  ? 311 PRO   A C     1 
ATOM   2461 O O     . PRO   A 1 319 ? -12.234 -86.934  -6.948  1.00 51.71  ? 311 PRO   A O     1 
ATOM   2462 C CB    . PRO   A 1 319 ? -13.639 -87.527  -9.697  1.00 48.82  ? 311 PRO   A CB    1 
ATOM   2463 C CG    . PRO   A 1 319 ? -13.575 -86.439  -10.745 1.00 47.64  ? 311 PRO   A CG    1 
ATOM   2464 C CD    . PRO   A 1 319 ? -13.230 -85.175  -9.984  1.00 47.88  ? 311 PRO   A CD    1 
ATOM   2465 N N     . LEU   A 1 320 ? -14.112 -88.061  -6.352  1.00 54.24  ? 312 LEU   A N     1 
ATOM   2466 C CA    . LEU   A 1 320 ? -13.569 -88.596  -5.116  1.00 55.76  ? 312 LEU   A CA    1 
ATOM   2467 C C     . LEU   A 1 320 ? -13.435 -90.111  -5.256  1.00 56.38  ? 312 LEU   A C     1 
ATOM   2468 O O     . LEU   A 1 320 ? -14.276 -90.772  -5.865  1.00 56.91  ? 312 LEU   A O     1 
ATOM   2469 C CB    . LEU   A 1 320 ? -14.431 -88.210  -3.911  1.00 55.23  ? 312 LEU   A CB    1 
ATOM   2470 C CG    . LEU   A 1 320 ? -14.657 -86.712  -3.661  1.00 55.07  ? 312 LEU   A CG    1 
ATOM   2471 C CD1   . LEU   A 1 320 ? -13.456 -85.845  -4.043  1.00 55.72  ? 312 LEU   A CD1   1 
ATOM   2472 C CD2   . LEU   A 1 320 ? -15.919 -86.227  -4.356  1.00 54.56  ? 312 LEU   A CD2   1 
ATOM   2473 N N     . GLN   A 1 321 ? -12.325 -90.613  -4.708  1.00 55.18  ? 313 GLN   A N     1 
ATOM   2474 C CA    . GLN   A 1 321 ? -11.988 -92.024  -4.595  1.00 55.57  ? 313 GLN   A CA    1 
ATOM   2475 C C     . GLN   A 1 321 ? -13.107 -92.847  -3.953  1.00 53.69  ? 313 GLN   A C     1 
ATOM   2476 O O     . GLN   A 1 321 ? -13.375 -92.676  -2.765  1.00 53.03  ? 313 GLN   A O     1 
ATOM   2477 C CB    . GLN   A 1 321 ? -10.773 -92.005  -3.664  1.00 55.99  ? 313 GLN   A CB    1 
ATOM   2478 C CG    . GLN   A 1 321 ? -9.558  -91.271  -4.228  1.00 55.26  ? 313 GLN   A CG    1 
ATOM   2479 C CD    . GLN   A 1 321 ? -8.562  -90.841  -3.172  1.00 53.00  ? 313 GLN   A CD    1 
ATOM   2480 O OE1   . GLN   A 1 321 ? -8.834  -90.885  -1.967  1.00 53.49  ? 313 GLN   A OE1   1 
ATOM   2481 N NE2   . GLN   A 1 321 ? -7.398  -90.392  -3.618  1.00 51.99  ? 313 GLN   A NE2   1 
ATOM   2482 N N     . PRO   A 1 322 ? -13.795 -93.762  -4.685  1.00 53.17  ? 314 PRO   A N     1 
ATOM   2483 C CA    . PRO   A 1 322 ? -14.660 -94.762  -4.044  1.00 51.87  ? 314 PRO   A CA    1 
ATOM   2484 C C     . PRO   A 1 322 ? -13.920 -95.830  -3.240  1.00 47.07  ? 314 PRO   A C     1 
ATOM   2485 O O     . PRO   A 1 322 ? -14.511 -96.457  -2.364  1.00 44.93  ? 314 PRO   A O     1 
ATOM   2486 C CB    . PRO   A 1 322 ? -15.447 -95.404  -5.206  1.00 53.49  ? 314 PRO   A CB    1 
ATOM   2487 C CG    . PRO   A 1 322 ? -15.252 -94.462  -6.371  1.00 54.06  ? 314 PRO   A CG    1 
ATOM   2488 C CD    . PRO   A 1 322 ? -13.887 -93.820  -6.154  1.00 53.98  ? 314 PRO   A CD    1 
ATOM   2489 N N     . LEU   A 1 323 ? -12.646 -96.060  -3.576  1.00 44.91  ? 315 LEU   A N     1 
ATOM   2490 C CA    . LEU   A 1 323 ? -11.854 -97.095  -2.935  1.00 44.38  ? 315 LEU   A CA    1 
ATOM   2491 C C     . LEU   A 1 323 ? -11.329 -96.603  -1.586  1.00 45.45  ? 315 LEU   A C     1 
ATOM   2492 O O     . LEU   A 1 323 ? -11.299 -97.361  -0.616  1.00 45.51  ? 315 LEU   A O     1 
ATOM   2493 C CB    . LEU   A 1 323 ? -10.728 -97.504  -3.885  1.00 43.33  ? 315 LEU   A CB    1 
ATOM   2494 C CG    . LEU   A 1 323 ? -10.081 -98.868  -3.634  1.00 42.40  ? 315 LEU   A CG    1 
ATOM   2495 C CD1   . LEU   A 1 323 ? -11.101 -99.992  -3.617  1.00 42.48  ? 315 LEU   A CD1   1 
ATOM   2496 C CD2   . LEU   A 1 323 ? -9.035  -99.113  -4.701  1.00 41.76  ? 315 LEU   A CD2   1 
ATOM   2497 N N     . MET   A 1 324 ? -10.926 -95.328  -1.521  1.00 45.94  ? 316 MET   A N     1 
ATOM   2498 C CA    . MET   A 1 324 ? -10.302 -94.786  -0.324  1.00 45.86  ? 316 MET   A CA    1 
ATOM   2499 C C     . MET   A 1 324 ? -11.349 -94.231  0.638   1.00 41.64  ? 316 MET   A C     1 
ATOM   2500 O O     . MET   A 1 324 ? -11.119 -94.217  1.843   1.00 39.05  ? 316 MET   A O     1 
ATOM   2501 C CB    . MET   A 1 324 ? -9.318  -93.663  -0.664  1.00 50.74  ? 316 MET   A CB    1 
ATOM   2502 C CG    . MET   A 1 324 ? -8.406  -93.272  0.485   1.00 55.27  ? 316 MET   A CG    1 
ATOM   2503 S SD    . MET   A 1 324 ? -7.458  -94.661  1.144   1.00 64.83  ? 316 MET   A SD    1 
ATOM   2504 C CE    . MET   A 1 324 ? -6.729  -95.311  -0.365  1.00 61.81  ? 316 MET   A CE    1 
ATOM   2505 N N     . ASP   A 1 325 ? -12.474 -93.745  0.103   1.00 40.10  ? 317 ASP   A N     1 
ATOM   2506 C CA    . ASP   A 1 325 ? -13.541 -93.199  0.927   1.00 38.89  ? 317 ASP   A CA    1 
ATOM   2507 C C     . ASP   A 1 325 ? -14.777 -94.083  0.819   1.00 35.73  ? 317 ASP   A C     1 
ATOM   2508 O O     . ASP   A 1 325 ? -14.887 -94.900  -0.092  1.00 35.11  ? 317 ASP   A O     1 
ATOM   2509 C CB    . ASP   A 1 325 ? -13.870 -91.768  0.532   1.00 41.21  ? 317 ASP   A CB    1 
ATOM   2510 C CG    . ASP   A 1 325 ? -12.823 -90.725  0.893   1.00 42.80  ? 317 ASP   A CG    1 
ATOM   2511 O OD1   . ASP   A 1 325 ? -11.915 -91.045  1.688   1.00 45.41  ? 317 ASP   A OD1   1 
ATOM   2512 O OD2   . ASP   A 1 325 ? -12.923 -89.602  0.368   1.00 44.52  ? 317 ASP   A OD2   1 
ATOM   2513 N N     . ASN   A 1 326 ? -15.702 -93.904  1.767   1.00 32.82  ? 318 ASN   A N     1 
ATOM   2514 C CA    . ASN   A 1 326 ? -16.967 -94.615  1.752   1.00 32.01  ? 318 ASN   A CA    1 
ATOM   2515 C C     . ASN   A 1 326 ? -18.060 -93.654  1.290   1.00 31.41  ? 318 ASN   A C     1 
ATOM   2516 O O     . ASN   A 1 326 ? -18.108 -92.503  1.717   1.00 30.03  ? 318 ASN   A O     1 
ATOM   2517 C CB    . ASN   A 1 326 ? -17.257 -95.267  3.100   1.00 32.05  ? 318 ASN   A CB    1 
ATOM   2518 C CG    . ASN   A 1 326 ? -16.301 -96.397  3.410   1.00 32.34  ? 318 ASN   A CG    1 
ATOM   2519 O OD1   . ASN   A 1 326 ? -16.009 -97.229  2.542   1.00 32.97  ? 318 ASN   A OD1   1 
ATOM   2520 N ND2   . ASN   A 1 326 ? -15.793 -96.447  4.632   1.00 31.80  ? 318 ASN   A ND2   1 
ATOM   2521 N N     . LEU   A 1 327 ? -18.921 -94.141  0.389   1.00 31.42  ? 319 LEU   A N     1 
ATOM   2522 C CA    . LEU   A 1 327 ? -20.028 -93.354  -0.126  1.00 31.45  ? 319 LEU   A CA    1 
ATOM   2523 C C     . LEU   A 1 327 ? -21.073 -93.166  0.968   1.00 31.71  ? 319 LEU   A C     1 
ATOM   2524 O O     . LEU   A 1 327 ? -21.273 -94.052  1.791   1.00 31.40  ? 319 LEU   A O     1 
ATOM   2525 C CB    . LEU   A 1 327 ? -20.637 -94.060  -1.333  1.00 31.44  ? 319 LEU   A CB    1 
ATOM   2526 C CG    . LEU   A 1 327 ? -19.772 -94.101  -2.594  1.00 31.02  ? 319 LEU   A CG    1 
ATOM   2527 C CD1   . LEU   A 1 327 ? -20.317 -95.170  -3.513  1.00 31.29  ? 319 LEU   A CD1   1 
ATOM   2528 C CD2   . LEU   A 1 327 ? -19.740 -92.749  -3.281  1.00 31.09  ? 319 LEU   A CD2   1 
ATOM   2529 N N     . GLU   A 1 328 ? -21.744 -92.011  0.937   1.00 32.56  ? 320 GLU   A N     1 
ATOM   2530 C CA    . GLU   A 1 328 ? -22.802 -91.698  1.880   1.00 33.88  ? 320 GLU   A CA    1 
ATOM   2531 C C     . GLU   A 1 328 ? -24.093 -92.375  1.431   1.00 33.58  ? 320 GLU   A C     1 
ATOM   2532 O O     . GLU   A 1 328 ? -24.210 -92.804  0.284   1.00 33.81  ? 320 GLU   A O     1 
ATOM   2533 C CB    . GLU   A 1 328 ? -22.929 -90.180  1.995   1.00 35.36  ? 320 GLU   A CB    1 
ATOM   2534 C CG    . GLU   A 1 328 ? -21.656 -89.523  2.522   1.00 37.36  ? 320 GLU   A CG    1 
ATOM   2535 C CD    . GLU   A 1 328 ? -21.721 -88.014  2.674   1.00 40.45  ? 320 GLU   A CD    1 
ATOM   2536 O OE1   . GLU   A 1 328 ? -22.724 -87.409  2.236   1.00 42.03  ? 320 GLU   A OE1   1 
ATOM   2537 O OE2   . GLU   A 1 328 ? -20.764 -87.445  3.247   1.00 43.09  ? 320 GLU   A OE2   1 
ATOM   2538 N N     . SER   A 1 329 ? -25.052 -92.464  2.359   1.00 33.78  ? 321 SER   A N     1 
ATOM   2539 C CA    . SER   A 1 329 ? -26.313 -93.154  2.131   1.00 33.64  ? 321 SER   A CA    1 
ATOM   2540 C C     . SER   A 1 329 ? -27.094 -92.497  0.994   1.00 34.13  ? 321 SER   A C     1 
ATOM   2541 O O     . SER   A 1 329 ? -27.600 -93.195  0.117   1.00 34.09  ? 321 SER   A O     1 
ATOM   2542 C CB    . SER   A 1 329 ? -27.138 -93.207  3.392   1.00 33.12  ? 321 SER   A CB    1 
ATOM   2543 O OG    . SER   A 1 329 ? -28.466 -93.635  3.124   1.00 32.48  ? 321 SER   A OG    1 
ATOM   2544 N N     . GLN   A 1 330 ? -27.187 -91.160  1.016   1.00 33.77  ? 322 GLN   A N     1 
ATOM   2545 C CA    . GLN   A 1 330 ? -27.991 -90.430  0.046   1.00 34.28  ? 322 GLN   A CA    1 
ATOM   2546 C C     . GLN   A 1 330 ? -27.376 -90.481  -1.352  1.00 32.91  ? 322 GLN   A C     1 
ATOM   2547 O O     . GLN   A 1 330 ? -28.088 -90.285  -2.333  1.00 32.27  ? 322 GLN   A O     1 
ATOM   2548 C CB    . GLN   A 1 330 ? -28.236 -88.972  0.438   1.00 35.37  ? 322 GLN   A CB    1 
ATOM   2549 C CG    . GLN   A 1 330 ? -29.643 -88.718  0.964   1.00 36.82  ? 322 GLN   A CG    1 
ATOM   2550 C CD    . GLN   A 1 330 ? -29.778 -87.396  1.685   1.00 38.67  ? 322 GLN   A CD    1 
ATOM   2551 O OE1   . GLN   A 1 330 ? -29.850 -86.322  1.075   1.00 38.87  ? 322 GLN   A OE1   1 
ATOM   2552 N NE2   . GLN   A 1 330 ? -29.826 -87.472  3.007   1.00 40.15  ? 322 GLN   A NE2   1 
ATOM   2553 N N     . THR   A 1 331 ? -26.063 -90.721  -1.442  1.00 31.59  ? 323 THR   A N     1 
ATOM   2554 C CA    . THR   A 1 331 ? -25.402 -90.822  -2.733  1.00 30.30  ? 323 THR   A CA    1 
ATOM   2555 C C     . THR   A 1 331 ? -25.868 -92.097  -3.436  1.00 29.39  ? 323 THR   A C     1 
ATOM   2556 O O     . THR   A 1 331 ? -26.300 -92.040  -4.585  1.00 28.91  ? 323 THR   A O     1 
ATOM   2557 C CB    . THR   A 1 331 ? -23.886 -90.771  -2.548  1.00 30.08  ? 323 THR   A CB    1 
ATOM   2558 O OG1   . THR   A 1 331 ? -23.631 -89.498  -1.963  1.00 29.16  ? 323 THR   A OG1   1 
ATOM   2559 C CG2   . THR   A 1 331 ? -23.123 -90.861  -3.857  1.00 30.29  ? 323 THR   A CG2   1 
ATOM   2560 N N     . TYR   A 1 332 ? -25.787 -93.236  -2.734  1.00 28.87  ? 324 TYR   A N     1 
ATOM   2561 C CA    . TYR   A 1 332 ? -26.289 -94.505  -3.245  1.00 28.25  ? 324 TYR   A CA    1 
ATOM   2562 C C     . TYR   A 1 332 ? -27.758 -94.367  -3.636  1.00 29.91  ? 324 TYR   A C     1 
ATOM   2563 O O     . TYR   A 1 332 ? -28.161 -94.820  -4.706  1.00 29.79  ? 324 TYR   A O     1 
ATOM   2564 C CB    . TYR   A 1 332 ? -26.234 -95.659  -2.241  1.00 27.02  ? 324 TYR   A CB    1 
ATOM   2565 C CG    . TYR   A 1 332 ? -24.857 -96.222  -1.920  1.00 25.57  ? 324 TYR   A CG    1 
ATOM   2566 C CD1   . TYR   A 1 332 ? -24.062 -96.788  -2.910  1.00 25.08  ? 324 TYR   A CD1   1 
ATOM   2567 C CD2   . TYR   A 1 332 ? -24.389 -96.260  -0.614  1.00 24.74  ? 324 TYR   A CD2   1 
ATOM   2568 C CE1   . TYR   A 1 332 ? -22.821 -97.329  -2.619  1.00 24.70  ? 324 TYR   A CE1   1 
ATOM   2569 C CE2   . TYR   A 1 332 ? -23.151 -96.802  -0.307  1.00 24.62  ? 324 TYR   A CE2   1 
ATOM   2570 C CZ    . TYR   A 1 332 ? -22.364 -97.336  -1.312  1.00 24.67  ? 324 TYR   A CZ    1 
ATOM   2571 O OH    . TYR   A 1 332 ? -21.141 -97.862  -1.012  1.00 24.25  ? 324 TYR   A OH    1 
ATOM   2572 N N     . GLU   A 1 333 ? -28.544 -93.754  -2.741  1.00 31.73  ? 325 GLU   A N     1 
ATOM   2573 C CA    . GLU   A 1 333 ? -29.979 -93.588  -2.915  1.00 33.74  ? 325 GLU   A CA    1 
ATOM   2574 C C     . GLU   A 1 333 ? -30.290 -93.000  -4.291  1.00 34.19  ? 325 GLU   A C     1 
ATOM   2575 O O     . GLU   A 1 333 ? -31.215 -93.456  -4.958  1.00 35.07  ? 325 GLU   A O     1 
ATOM   2576 C CB    . GLU   A 1 333 ? -30.517 -92.684  -1.806  1.00 35.11  ? 325 GLU   A CB    1 
ATOM   2577 C CG    . GLU   A 1 333 ? -32.005 -92.360  -1.922  1.00 36.84  ? 325 GLU   A CG    1 
ATOM   2578 C CD    . GLU   A 1 333 ? -32.403 -91.122  -1.138  1.00 39.38  ? 325 GLU   A CD    1 
ATOM   2579 O OE1   . GLU   A 1 333 ? -31.933 -90.018  -1.498  1.00 41.58  ? 325 GLU   A OE1   1 
ATOM   2580 O OE2   . GLU   A 1 333 ? -33.170 -91.258  -0.163  1.00 41.08  ? 325 GLU   A OE2   1 
ATOM   2581 N N     . VAL   A 1 334 ? -29.514 -91.986  -4.693  1.00 34.27  ? 326 VAL   A N     1 
ATOM   2582 C CA    . VAL   A 1 334 ? -29.729 -91.269  -5.941  1.00 34.14  ? 326 VAL   A CA    1 
ATOM   2583 C C     . VAL   A 1 334 ? -29.490 -92.184  -7.143  1.00 34.69  ? 326 VAL   A C     1 
ATOM   2584 O O     . VAL   A 1 334 ? -30.272 -92.165  -8.093  1.00 35.76  ? 326 VAL   A O     1 
ATOM   2585 C CB    . VAL   A 1 334 ? -28.822 -90.021  -5.985  1.00 34.17  ? 326 VAL   A CB    1 
ATOM   2586 C CG1   . VAL   A 1 334 ? -28.615 -89.490  -7.399  1.00 34.74  ? 326 VAL   A CG1   1 
ATOM   2587 C CG2   . VAL   A 1 334 ? -29.347 -88.916  -5.078  1.00 33.82  ? 326 VAL   A CG2   1 
ATOM   2588 N N     . PHE   A 1 335 ? -28.409 -92.972  -7.104  1.00 34.44  ? 327 PHE   A N     1 
ATOM   2589 C CA    . PHE   A 1 335 ? -27.921 -93.662  -8.289  1.00 34.94  ? 327 PHE   A CA    1 
ATOM   2590 C C     . PHE   A 1 335 ? -28.564 -95.039  -8.448  1.00 36.68  ? 327 PHE   A C     1 
ATOM   2591 O O     . PHE   A 1 335 ? -28.503 -95.617  -9.532  1.00 38.57  ? 327 PHE   A O     1 
ATOM   2592 C CB    . PHE   A 1 335 ? -26.395 -93.756  -8.219  1.00 34.83  ? 327 PHE   A CB    1 
ATOM   2593 C CG    . PHE   A 1 335 ? -25.678 -92.443  -8.501  1.00 35.02  ? 327 PHE   A CG    1 
ATOM   2594 C CD1   . PHE   A 1 335 ? -25.922 -91.735  -9.674  1.00 34.87  ? 327 PHE   A CD1   1 
ATOM   2595 C CD2   . PHE   A 1 335 ? -24.785 -91.904  -7.581  1.00 35.24  ? 327 PHE   A CD2   1 
ATOM   2596 C CE1   . PHE   A 1 335 ? -25.273 -90.538  -9.927  1.00 35.09  ? 327 PHE   A CE1   1 
ATOM   2597 C CE2   . PHE   A 1 335 ? -24.140 -90.705  -7.838  1.00 35.20  ? 327 PHE   A CE2   1 
ATOM   2598 C CZ    . PHE   A 1 335 ? -24.385 -90.026  -9.009  1.00 35.46  ? 327 PHE   A CZ    1 
ATOM   2599 N N     . GLU   A 1 336 ? -29.170 -95.558  -7.373  1.00 37.44  ? 328 GLU   A N     1 
ATOM   2600 C CA    . GLU   A 1 336 ? -29.944 -96.790  -7.422  1.00 37.36  ? 328 GLU   A CA    1 
ATOM   2601 C C     . GLU   A 1 336 ? -31.115 -96.673  -8.391  1.00 38.70  ? 328 GLU   A C     1 
ATOM   2602 O O     . GLU   A 1 336 ? -31.550 -97.669  -8.962  1.00 38.53  ? 328 GLU   A O     1 
ATOM   2603 C CB    . GLU   A 1 336 ? -30.583 -97.078  -6.066  1.00 35.59  ? 328 GLU   A CB    1 
ATOM   2604 C CG    . GLU   A 1 336 ? -29.593 -97.601  -5.036  1.00 34.64  ? 328 GLU   A CG    1 
ATOM   2605 C CD    . GLU   A 1 336 ? -30.091 -97.520  -3.607  1.00 33.94  ? 328 GLU   A CD    1 
ATOM   2606 O OE1   . GLU   A 1 336 ? -31.205 -97.009  -3.352  1.00 32.82  ? 328 GLU   A OE1   1 
ATOM   2607 O OE2   . GLU   A 1 336 ? -29.329 -97.972  -2.733  1.00 33.34  ? 328 GLU   A OE2   1 
ATOM   2608 N N     . LYS   A 1 337 ? -31.624 -95.446  -8.540  1.00 41.54  ? 329 LYS   A N     1 
ATOM   2609 C CA    . LYS   A 1 337 ? -32.883 -95.187  -9.216  1.00 43.25  ? 329 LYS   A CA    1 
ATOM   2610 C C     . LYS   A 1 337 ? -32.647 -94.841  -10.684 1.00 44.72  ? 329 LYS   A C     1 
ATOM   2611 O O     . LYS   A 1 337 ? -33.420 -94.084  -11.270 1.00 45.97  ? 329 LYS   A O     1 
ATOM   2612 C CB    . LYS   A 1 337 ? -33.570 -94.041  -8.466  1.00 44.36  ? 329 LYS   A CB    1 
ATOM   2613 C CG    . LYS   A 1 337 ? -33.893 -94.348  -7.009  1.00 45.45  ? 329 LYS   A CG    1 
ATOM   2614 C CD    . LYS   A 1 337 ? -34.128 -93.124  -6.132  1.00 45.95  ? 329 LYS   A CD    1 
ATOM   2615 C CE    . LYS   A 1 337 ? -35.003 -92.087  -6.759  1.00 46.26  ? 329 LYS   A CE    1 
ATOM   2616 N NZ    . LYS   A 1 337 ? -35.373 -91.061  -5.781  1.00 46.40  ? 329 LYS   A NZ    1 
ATOM   2617 N N     . ASP   A 1 338 ? -31.580 -95.394  -11.274 1.00 44.46  ? 330 ASP   A N     1 
ATOM   2618 C CA    . ASP   A 1 338 ? -31.352 -95.262  -12.702 1.00 43.09  ? 330 ASP   A CA    1 
ATOM   2619 C C     . ASP   A 1 338 ? -32.063 -96.419  -13.399 1.00 43.31  ? 330 ASP   A C     1 
ATOM   2620 O O     . ASP   A 1 338 ? -31.631 -97.565  -13.298 1.00 41.76  ? 330 ASP   A O     1 
ATOM   2621 C CB    . ASP   A 1 338 ? -29.870 -95.190  -13.035 1.00 42.55  ? 330 ASP   A CB    1 
ATOM   2622 C CG    . ASP   A 1 338 ? -29.550 -94.820  -14.477 1.00 41.80  ? 330 ASP   A CG    1 
ATOM   2623 O OD1   . ASP   A 1 338 ? -29.928 -95.594  -15.380 1.00 41.82  ? 330 ASP   A OD1   1 
ATOM   2624 O OD2   . ASP   A 1 338 ? -28.932 -93.756  -14.685 1.00 40.49  ? 330 ASP   A OD2   1 
ATOM   2625 N N     . PRO   A 1 339 ? -33.166 -96.160  -14.136 1.00 44.75  ? 331 PRO   A N     1 
ATOM   2626 C CA    . PRO   A 1 339 ? -33.949 -97.238  -14.743 1.00 45.87  ? 331 PRO   A CA    1 
ATOM   2627 C C     . PRO   A 1 339 ? -33.152 -98.058  -15.756 1.00 45.63  ? 331 PRO   A C     1 
ATOM   2628 O O     . PRO   A 1 339 ? -33.227 -99.286  -15.764 1.00 45.30  ? 331 PRO   A O     1 
ATOM   2629 C CB    . PRO   A 1 339 ? -35.119 -96.482  -15.400 1.00 46.47  ? 331 PRO   A CB    1 
ATOM   2630 C CG    . PRO   A 1 339 ? -34.561 -95.100  -15.669 1.00 46.42  ? 331 PRO   A CG    1 
ATOM   2631 C CD    . PRO   A 1 339 ? -33.682 -94.821  -14.467 1.00 45.79  ? 331 PRO   A CD    1 
ATOM   2632 N N     . ILE   A 1 340 ? -32.356 -97.357  -16.575 1.00 44.05  ? 332 ILE   A N     1 
ATOM   2633 C CA    . ILE   A 1 340 ? -31.728 -97.940  -17.750 1.00 42.61  ? 332 ILE   A CA    1 
ATOM   2634 C C     . ILE   A 1 340 ? -30.532 -98.786  -17.315 1.00 40.64  ? 332 ILE   A C     1 
ATOM   2635 O O     . ILE   A 1 340 ? -30.341 -99.894  -17.811 1.00 40.13  ? 332 ILE   A O     1 
ATOM   2636 C CB    . ILE   A 1 340 ? -31.302 -96.851  -18.756 1.00 43.05  ? 332 ILE   A CB    1 
ATOM   2637 C CG1   . ILE   A 1 340 ? -32.348 -95.733  -18.906 1.00 44.40  ? 332 ILE   A CG1   1 
ATOM   2638 C CG2   . ILE   A 1 340 ? -30.944 -97.471  -20.107 1.00 42.94  ? 332 ILE   A CG2   1 
ATOM   2639 C CD1   . ILE   A 1 340 ? -33.670 -96.171  -19.513 1.00 44.99  ? 332 ILE   A CD1   1 
ATOM   2640 N N     . LYS   A 1 341 ? -29.725 -98.246  -16.394 1.00 38.64  ? 333 LYS   A N     1 
ATOM   2641 C CA    . LYS   A 1 341 ? -28.484 -98.884  -15.983 1.00 37.47  ? 333 LYS   A CA    1 
ATOM   2642 C C     . LYS   A 1 341 ? -28.759 -100.321 -15.544 1.00 36.78  ? 333 LYS   A C     1 
ATOM   2643 O O     . LYS   A 1 341 ? -28.058 -101.239 -15.964 1.00 36.70  ? 333 LYS   A O     1 
ATOM   2644 C CB    . LYS   A 1 341 ? -27.819 -98.083  -14.858 1.00 37.22  ? 333 LYS   A CB    1 
ATOM   2645 C CG    . LYS   A 1 341 ? -26.375 -98.445  -14.528 1.00 37.19  ? 333 LYS   A CG    1 
ATOM   2646 C CD    . LYS   A 1 341 ? -26.031 -98.181  -13.067 1.00 37.71  ? 333 LYS   A CD    1 
ATOM   2647 C CE    . LYS   A 1 341 ? -24.578 -97.963  -12.787 1.00 37.81  ? 333 LYS   A CE    1 
ATOM   2648 N NZ    . LYS   A 1 341 ? -24.350 -97.591  -11.389 1.00 37.77  ? 333 LYS   A NZ    1 
ATOM   2649 N N     . TYR   A 1 342 ? -29.800 -100.514 -14.723 1.00 35.50  ? 334 TYR   A N     1 
ATOM   2650 C CA    . TYR   A 1 342 ? -30.044 -101.804 -14.098 1.00 35.08  ? 334 TYR   A CA    1 
ATOM   2651 C C     . TYR   A 1 342 ? -30.870 -102.702 -15.020 1.00 36.26  ? 334 TYR   A C     1 
ATOM   2652 O O     . TYR   A 1 342 ? -30.719 -103.920 -14.963 1.00 36.61  ? 334 TYR   A O     1 
ATOM   2653 C CB    . TYR   A 1 342 ? -30.619 -101.551 -12.701 1.00 34.93  ? 334 TYR   A CB    1 
ATOM   2654 C CG    . TYR   A 1 342 ? -29.652 -100.755 -11.835 1.00 33.87  ? 334 TYR   A CG    1 
ATOM   2655 C CD1   . TYR   A 1 342 ? -28.431 -101.295 -11.444 1.00 32.83  ? 334 TYR   A CD1   1 
ATOM   2656 C CD2   . TYR   A 1 342 ? -29.948 -99.461  -11.425 1.00 33.35  ? 334 TYR   A CD2   1 
ATOM   2657 C CE1   . TYR   A 1 342 ? -27.534 -100.572 -10.674 1.00 32.26  ? 334 TYR   A CE1   1 
ATOM   2658 C CE2   . TYR   A 1 342 ? -29.063 -98.730  -10.651 1.00 32.84  ? 334 TYR   A CE2   1 
ATOM   2659 C CZ    . TYR   A 1 342 ? -27.852 -99.285  -10.275 1.00 32.34  ? 334 TYR   A CZ    1 
ATOM   2660 O OH    . TYR   A 1 342 ? -26.988 -98.549  -9.514  1.00 32.08  ? 334 TYR   A OH    1 
ATOM   2661 N N     . SER   A 1 343 ? -31.727 -102.110 -15.868 1.00 36.20  ? 335 SER   A N     1 
ATOM   2662 C CA    . SER   A 1 343 ? -32.366 -102.842 -16.954 1.00 35.50  ? 335 SER   A CA    1 
ATOM   2663 C C     . SER   A 1 343 ? -31.301 -103.540 -17.791 1.00 35.27  ? 335 SER   A C     1 
ATOM   2664 O O     . SER   A 1 343 ? -31.379 -104.742 -18.032 1.00 35.42  ? 335 SER   A O     1 
ATOM   2665 C CB    . SER   A 1 343 ? -33.193 -101.942 -17.835 1.00 35.87  ? 335 SER   A CB    1 
ATOM   2666 O OG    . SER   A 1 343 ? -34.365 -101.498 -17.170 1.00 37.63  ? 335 SER   A OG    1 
ATOM   2667 N N     . GLN   A 1 344 ? -30.314 -102.747 -18.223 1.00 34.98  ? 336 GLN   A N     1 
ATOM   2668 C CA    . GLN   A 1 344 ? -29.210 -103.225 -19.038 1.00 34.69  ? 336 GLN   A CA    1 
ATOM   2669 C C     . GLN   A 1 344 ? -28.403 -104.275 -18.278 1.00 34.80  ? 336 GLN   A C     1 
ATOM   2670 O O     . GLN   A 1 344 ? -28.004 -105.280 -18.858 1.00 34.59  ? 336 GLN   A O     1 
ATOM   2671 C CB    . GLN   A 1 344 ? -28.364 -102.031 -19.480 1.00 34.50  ? 336 GLN   A CB    1 
ATOM   2672 C CG    . GLN   A 1 344 ? -29.072 -101.125 -20.483 1.00 34.08  ? 336 GLN   A CG    1 
ATOM   2673 C CD    . GLN   A 1 344 ? -29.489 -101.862 -21.738 1.00 33.60  ? 336 GLN   A CD    1 
ATOM   2674 O OE1   . GLN   A 1 344 ? -28.676 -102.130 -22.631 1.00 32.91  ? 336 GLN   A OE1   1 
ATOM   2675 N NE2   . GLN   A 1 344 ? -30.767 -102.206 -21.810 1.00 33.11  ? 336 GLN   A NE2   1 
ATOM   2676 N N     . TYR   A 1 345 ? -28.178 -104.045 -16.981 1.00 35.45  ? 337 TYR   A N     1 
ATOM   2677 C CA    . TYR   A 1 345 ? -27.470 -105.012 -16.154 1.00 36.57  ? 337 TYR   A CA    1 
ATOM   2678 C C     . TYR   A 1 345 ? -28.287 -106.299 -16.029 1.00 38.69  ? 337 TYR   A C     1 
ATOM   2679 O O     . TYR   A 1 345 ? -27.725 -107.391 -16.093 1.00 38.96  ? 337 TYR   A O     1 
ATOM   2680 C CB    . TYR   A 1 345 ? -27.112 -104.423 -14.786 1.00 34.83  ? 337 TYR   A CB    1 
ATOM   2681 C CG    . TYR   A 1 345 ? -25.697 -103.867 -14.708 1.00 33.30  ? 337 TYR   A CG    1 
ATOM   2682 C CD1   . TYR   A 1 345 ? -24.615 -104.719 -14.515 1.00 32.80  ? 337 TYR   A CD1   1 
ATOM   2683 C CD2   . TYR   A 1 345 ? -25.438 -102.505 -14.822 1.00 32.12  ? 337 TYR   A CD2   1 
ATOM   2684 C CE1   . TYR   A 1 345 ? -23.320 -104.233 -14.437 1.00 32.50  ? 337 TYR   A CE1   1 
ATOM   2685 C CE2   . TYR   A 1 345 ? -24.148 -102.007 -14.744 1.00 31.59  ? 337 TYR   A CE2   1 
ATOM   2686 C CZ    . TYR   A 1 345 ? -23.087 -102.874 -14.549 1.00 31.67  ? 337 TYR   A CZ    1 
ATOM   2687 O OH    . TYR   A 1 345 ? -21.811 -102.403 -14.467 1.00 31.11  ? 337 TYR   A OH    1 
ATOM   2688 N N     . GLN   A 1 346 ? -29.608 -106.161 -15.853 1.00 40.09  ? 338 GLN   A N     1 
ATOM   2689 C CA    . GLN   A 1 346 ? -30.498 -107.305 -15.726 1.00 41.65  ? 338 GLN   A CA    1 
ATOM   2690 C C     . GLN   A 1 346 ? -30.427 -108.162 -16.988 1.00 43.14  ? 338 GLN   A C     1 
ATOM   2691 O O     . GLN   A 1 346 ? -30.326 -109.384 -16.906 1.00 42.20  ? 338 GLN   A O     1 
ATOM   2692 C CB    . GLN   A 1 346 ? -31.940 -106.853 -15.494 1.00 42.40  ? 338 GLN   A CB    1 
ATOM   2693 C CG    . GLN   A 1 346 ? -32.852 -107.946 -14.949 1.00 43.10  ? 338 GLN   A CG    1 
ATOM   2694 C CD    . GLN   A 1 346 ? -34.257 -107.454 -14.681 1.00 44.01  ? 338 GLN   A CD    1 
ATOM   2695 O OE1   . GLN   A 1 346 ? -34.462 -106.387 -14.090 1.00 43.58  ? 338 GLN   A OE1   1 
ATOM   2696 N NE2   . GLN   A 1 346 ? -35.243 -108.216 -15.133 1.00 44.85  ? 338 GLN   A NE2   1 
ATOM   2697 N N     . GLN   A 1 347 ? -30.478 -107.498 -18.149 1.00 44.78  ? 339 GLN   A N     1 
ATOM   2698 C CA    . GLN   A 1 347 ? -30.514 -108.176 -19.435 1.00 46.78  ? 339 GLN   A CA    1 
ATOM   2699 C C     . GLN   A 1 347 ? -29.209 -108.938 -19.664 1.00 45.94  ? 339 GLN   A C     1 
ATOM   2700 O O     . GLN   A 1 347 ? -29.233 -110.078 -20.118 1.00 46.19  ? 339 GLN   A O     1 
ATOM   2701 C CB    . GLN   A 1 347 ? -30.777 -107.155 -20.543 1.00 49.05  ? 339 GLN   A CB    1 
ATOM   2702 C CG    . GLN   A 1 347 ? -31.131 -107.760 -21.899 1.00 51.03  ? 339 GLN   A CG    1 
ATOM   2703 C CD    . GLN   A 1 347 ? -32.364 -108.640 -21.862 1.00 52.32  ? 339 GLN   A CD    1 
ATOM   2704 O OE1   . GLN   A 1 347 ? -33.372 -108.309 -21.229 1.00 52.94  ? 339 GLN   A OE1   1 
ATOM   2705 N NE2   . GLN   A 1 347 ? -32.294 -109.781 -22.534 1.00 52.70  ? 339 GLN   A NE2   1 
ATOM   2706 N N     . ALA   A 1 348 ? -28.075 -108.304 -19.342 1.00 45.93  ? 340 ALA   A N     1 
ATOM   2707 C CA    . ALA   A 1 348 ? -26.766 -108.892 -19.580 1.00 46.46  ? 340 ALA   A CA    1 
ATOM   2708 C C     . ALA   A 1 348 ? -26.614 -110.185 -18.782 1.00 47.48  ? 340 ALA   A C     1 
ATOM   2709 O O     . ALA   A 1 348 ? -26.077 -111.170 -19.285 1.00 48.42  ? 340 ALA   A O     1 
ATOM   2710 C CB    . ALA   A 1 348 ? -25.680 -107.898 -19.227 1.00 45.84  ? 340 ALA   A CB    1 
ATOM   2711 N N     . ILE   A 1 349 ? -27.097 -110.158 -17.537 1.00 48.52  ? 341 ILE   A N     1 
ATOM   2712 C CA    . ILE   A 1 349 ? -27.017 -111.297 -16.638 1.00 50.04  ? 341 ILE   A CA    1 
ATOM   2713 C C     . ILE   A 1 349 ? -27.977 -112.381 -17.124 1.00 50.58  ? 341 ILE   A C     1 
ATOM   2714 O O     . ILE   A 1 349 ? -27.640 -113.562 -17.114 1.00 48.76  ? 341 ILE   A O     1 
ATOM   2715 C CB    . ILE   A 1 349 ? -27.313 -110.850 -15.193 1.00 51.06  ? 341 ILE   A CB    1 
ATOM   2716 C CG1   . ILE   A 1 349 ? -26.257 -109.857 -14.693 1.00 50.81  ? 341 ILE   A CG1   1 
ATOM   2717 C CG2   . ILE   A 1 349 ? -27.440 -112.052 -14.254 1.00 51.44  ? 341 ILE   A CG2   1 
ATOM   2718 C CD1   . ILE   A 1 349 ? -26.668 -109.072 -13.462 1.00 50.33  ? 341 ILE   A CD1   1 
ATOM   2719 N N     . TYR   A 1 350 ? -29.172 -111.955 -17.547 1.00 52.08  ? 342 TYR   A N     1 
ATOM   2720 C CA    . TYR   A 1 350 ? -30.187 -112.843 -18.089 1.00 53.04  ? 342 TYR   A CA    1 
ATOM   2721 C C     . TYR   A 1 350 ? -29.624 -113.637 -19.267 1.00 51.73  ? 342 TYR   A C     1 
ATOM   2722 O O     . TYR   A 1 350 ? -29.702 -114.863 -19.281 1.00 52.08  ? 342 TYR   A O     1 
ATOM   2723 C CB    . TYR   A 1 350 ? -31.394 -111.976 -18.463 1.00 54.96  ? 342 TYR   A CB    1 
ATOM   2724 C CG    . TYR   A 1 350 ? -32.426 -112.654 -19.351 1.00 57.96  ? 342 TYR   A CG    1 
ATOM   2725 C CD1   . TYR   A 1 350 ? -33.471 -113.391 -18.807 1.00 59.58  ? 342 TYR   A CD1   1 
ATOM   2726 C CD2   . TYR   A 1 350 ? -32.356 -112.548 -20.736 1.00 59.73  ? 342 TYR   A CD2   1 
ATOM   2727 C CE1   . TYR   A 1 350 ? -34.413 -114.008 -19.614 1.00 60.58  ? 342 TYR   A CE1   1 
ATOM   2728 C CE2   . TYR   A 1 350 ? -33.293 -113.160 -21.554 1.00 60.57  ? 342 TYR   A CE2   1 
ATOM   2729 C CZ    . TYR   A 1 350 ? -34.325 -113.890 -20.990 1.00 61.07  ? 342 TYR   A CZ    1 
ATOM   2730 O OH    . TYR   A 1 350 ? -35.251 -114.494 -21.789 1.00 62.95  ? 342 TYR   A OH    1 
ATOM   2731 N N     . LYS   A 1 351 ? -29.059 -112.927 -20.249 1.00 50.46  ? 343 LYS   A N     1 
ATOM   2732 C CA    . LYS   A 1 351 ? -28.540 -113.548 -21.457 1.00 50.23  ? 343 LYS   A CA    1 
ATOM   2733 C C     . LYS   A 1 351 ? -27.364 -114.465 -21.134 1.00 50.18  ? 343 LYS   A C     1 
ATOM   2734 O O     . LYS   A 1 351 ? -27.196 -115.497 -21.779 1.00 51.49  ? 343 LYS   A O     1 
ATOM   2735 C CB    . LYS   A 1 351 ? -28.063 -112.513 -22.482 1.00 50.92  ? 343 LYS   A CB    1 
ATOM   2736 C CG    . LYS   A 1 351 ? -29.166 -111.745 -23.194 1.00 51.47  ? 343 LYS   A CG    1 
ATOM   2737 C CD    . LYS   A 1 351 ? -28.667 -110.853 -24.325 1.00 52.58  ? 343 LYS   A CD    1 
ATOM   2738 C CE    . LYS   A 1 351 ? -28.017 -111.625 -25.431 1.00 52.95  ? 343 LYS   A CE    1 
ATOM   2739 N NZ    . LYS   A 1 351 ? -27.741 -110.778 -26.594 1.00 53.93  ? 343 LYS   A NZ    1 
ATOM   2740 N N     . CYS   A 1 352 ? -26.544 -114.070 -20.154 1.00 49.26  ? 344 CYS   A N     1 
ATOM   2741 C CA    . CYS   A 1 352 ? -25.369 -114.845 -19.790 1.00 48.20  ? 344 CYS   A CA    1 
ATOM   2742 C C     . CYS   A 1 352 ? -25.783 -116.173 -19.161 1.00 48.81  ? 344 CYS   A C     1 
ATOM   2743 O O     . CYS   A 1 352 ? -25.138 -117.192 -19.395 1.00 49.18  ? 344 CYS   A O     1 
ATOM   2744 C CB    . CYS   A 1 352 ? -24.458 -114.070 -18.848 1.00 47.08  ? 344 CYS   A CB    1 
ATOM   2745 S SG    . CYS   A 1 352 ? -22.948 -114.977 -18.426 1.00 45.51  ? 344 CYS   A SG    1 
ATOM   2746 N N     . LEU   A 1 353 ? -26.861 -116.152 -18.367 1.00 49.25  ? 345 LEU   A N     1 
ATOM   2747 C CA    . LEU   A 1 353 ? -27.382 -117.356 -17.736 1.00 50.95  ? 345 LEU   A CA    1 
ATOM   2748 C C     . LEU   A 1 353 ? -27.790 -118.370 -18.803 1.00 50.53  ? 345 LEU   A C     1 
ATOM   2749 O O     . LEU   A 1 353 ? -27.414 -119.539 -18.722 1.00 50.51  ? 345 LEU   A O     1 
ATOM   2750 C CB    . LEU   A 1 353 ? -28.563 -117.017 -16.826 1.00 51.82  ? 345 LEU   A CB    1 
ATOM   2751 C CG    . LEU   A 1 353 ? -28.238 -116.239 -15.547 1.00 52.11  ? 345 LEU   A CG    1 
ATOM   2752 C CD1   . LEU   A 1 353 ? -29.519 -115.749 -14.886 1.00 51.84  ? 345 LEU   A CD1   1 
ATOM   2753 C CD2   . LEU   A 1 353 ? -27.419 -117.077 -14.578 1.00 51.77  ? 345 LEU   A CD2   1 
ATOM   2754 N N     . LEU   A 1 354 ? -28.559 -117.910 -19.797 1.00 49.05  ? 346 LEU   A N     1 
ATOM   2755 C CA    . LEU   A 1 354 ? -29.071 -118.782 -20.841 1.00 48.22  ? 346 LEU   A CA    1 
ATOM   2756 C C     . LEU   A 1 354 ? -27.914 -119.387 -21.632 1.00 48.63  ? 346 LEU   A C     1 
ATOM   2757 O O     . LEU   A 1 354 ? -27.978 -120.551 -22.019 1.00 51.29  ? 346 LEU   A O     1 
ATOM   2758 C CB    . LEU   A 1 354 ? -30.039 -118.027 -21.751 1.00 47.05  ? 346 LEU   A CB    1 
ATOM   2759 C CG    . LEU   A 1 354 ? -31.279 -117.434 -21.072 1.00 47.22  ? 346 LEU   A CG    1 
ATOM   2760 C CD1   . LEU   A 1 354 ? -32.306 -117.015 -22.111 1.00 47.32  ? 346 LEU   A CD1   1 
ATOM   2761 C CD2   . LEU   A 1 354 ? -31.900 -118.387 -20.064 1.00 47.36  ? 346 LEU   A CD2   1 
ATOM   2762 N N     . ASP   A 1 355 ? -26.854 -118.603 -21.851 1.00 48.97  ? 347 ASP   A N     1 
ATOM   2763 C CA    . ASP   A 1 355 ? -25.692 -119.075 -22.586 1.00 49.61  ? 347 ASP   A CA    1 
ATOM   2764 C C     . ASP   A 1 355 ? -24.909 -120.105 -21.769 1.00 49.27  ? 347 ASP   A C     1 
ATOM   2765 O O     . ASP   A 1 355 ? -24.131 -120.865 -22.338 1.00 48.71  ? 347 ASP   A O     1 
ATOM   2766 C CB    . ASP   A 1 355 ? -24.795 -117.922 -23.010 1.00 50.65  ? 347 ASP   A CB    1 
ATOM   2767 C CG    . ASP   A 1 355 ? -25.437 -116.888 -23.925 1.00 52.08  ? 347 ASP   A CG    1 
ATOM   2768 O OD1   . ASP   A 1 355 ? -26.632 -117.047 -24.252 1.00 54.64  ? 347 ASP   A OD1   1 
ATOM   2769 O OD2   . ASP   A 1 355 ? -24.738 -115.924 -24.295 1.00 53.19  ? 347 ASP   A OD2   1 
ATOM   2770 N N     . ARG   A 1 356 ? -25.107 -120.124 -20.443 1.00 50.21  ? 348 ARG   A N     1 
ATOM   2771 C CA    . ARG   A 1 356 ? -24.271 -120.921 -19.557 1.00 50.93  ? 348 ARG   A CA    1 
ATOM   2772 C C     . ARG   A 1 356 ? -24.962 -122.225 -19.159 1.00 53.04  ? 348 ARG   A C     1 
ATOM   2773 O O     . ARG   A 1 356 ? -24.283 -123.234 -18.981 1.00 53.44  ? 348 ARG   A O     1 
ATOM   2774 C CB    . ARG   A 1 356 ? -23.836 -120.125 -18.318 1.00 49.41  ? 348 ARG   A CB    1 
ATOM   2775 C CG    . ARG   A 1 356 ? -22.684 -119.171 -18.606 1.00 48.65  ? 348 ARG   A CG    1 
ATOM   2776 C CD    . ARG   A 1 356 ? -21.953 -118.654 -17.371 1.00 47.49  ? 348 ARG   A CD    1 
ATOM   2777 N NE    . ARG   A 1 356 ? -21.028 -119.633 -16.781 1.00 46.54  ? 348 ARG   A NE    1 
ATOM   2778 C CZ    . ARG   A 1 356 ? -19.709 -119.686 -16.989 1.00 45.01  ? 348 ARG   A CZ    1 
ATOM   2779 N NH1   . ARG   A 1 356 ? -19.147 -118.945 -17.929 1.00 44.45  ? 348 ARG   A NH1   1 
ATOM   2780 N NH2   . ARG   A 1 356 ? -18.955 -120.513 -16.282 1.00 43.95  ? 348 ARG   A NH2   1 
ATOM   2781 N N     . VAL   A 1 357 ? -26.294 -122.205 -19.010 1.00 54.95  ? 349 VAL   A N     1 
ATOM   2782 C CA    . VAL   A 1 357 ? -27.009 -123.357 -18.483 1.00 56.68  ? 349 VAL   A CA    1 
ATOM   2783 C C     . VAL   A 1 357 ? -28.001 -123.858 -19.530 1.00 57.46  ? 349 VAL   A C     1 
ATOM   2784 O O     . VAL   A 1 357 ? -29.068 -123.270 -19.707 1.00 56.03  ? 349 VAL   A O     1 
ATOM   2785 C CB    . VAL   A 1 357 ? -27.707 -123.048 -17.144 1.00 57.80  ? 349 VAL   A CB    1 
ATOM   2786 C CG1   . VAL   A 1 357 ? -28.364 -124.289 -16.549 1.00 58.37  ? 349 VAL   A CG1   1 
ATOM   2787 C CG2   . VAL   A 1 357 ? -26.744 -122.436 -16.133 1.00 58.12  ? 349 VAL   A CG2   1 
ATOM   2788 N N     . PRO   A 1 358 ? -27.664 -124.945 -20.266 1.00 58.82  ? 350 PRO   A N     1 
ATOM   2789 C CA    . PRO   A 1 358 ? -28.638 -125.666 -21.089 1.00 59.14  ? 350 PRO   A CA    1 
ATOM   2790 C C     . PRO   A 1 358 ? -29.957 -125.917 -20.361 1.00 59.75  ? 350 PRO   A C     1 
ATOM   2791 O O     . PRO   A 1 358 ? -29.960 -126.228 -19.172 1.00 61.77  ? 350 PRO   A O     1 
ATOM   2792 C CB    . PRO   A 1 358 ? -27.903 -126.979 -21.415 1.00 59.38  ? 350 PRO   A CB    1 
ATOM   2793 C CG    . PRO   A 1 358 ? -26.439 -126.600 -21.428 1.00 59.49  ? 350 PRO   A CG    1 
ATOM   2794 C CD    . PRO   A 1 358 ? -26.305 -125.500 -20.386 1.00 59.36  ? 350 PRO   A CD    1 
ATOM   2795 N N     . GLU   A 1 359 ? -31.066 -125.794 -21.098 1.00 61.07  ? 351 GLU   A N     1 
ATOM   2796 C CA    . GLU   A 1 359 ? -32.409 -125.983 -20.569 1.00 62.56  ? 351 GLU   A CA    1 
ATOM   2797 C C     . GLU   A 1 359 ? -32.522 -127.318 -19.832 1.00 63.71  ? 351 GLU   A C     1 
ATOM   2798 O O     . GLU   A 1 359 ? -33.179 -127.403 -18.797 1.00 62.87  ? 351 GLU   A O     1 
ATOM   2799 C CB    . GLU   A 1 359 ? -33.392 -125.886 -21.737 1.00 62.61  ? 351 GLU   A CB    1 
ATOM   2800 C CG    . GLU   A 1 359 ? -34.839 -126.207 -21.371 1.00 62.60  ? 351 GLU   A CG    1 
ATOM   2801 C CD    . GLU   A 1 359 ? -35.428 -125.291 -20.318 1.00 62.19  ? 351 GLU   A CD    1 
ATOM   2802 O OE1   . GLU   A 1 359 ? -35.519 -124.078 -20.592 1.00 62.86  ? 351 GLU   A OE1   1 
ATOM   2803 O OE2   . GLU   A 1 359 ? -35.788 -125.786 -19.229 1.00 62.27  ? 351 GLU   A OE2   1 
ATOM   2804 N N     . GLU   A 1 360 ? -31.882 -128.356 -20.384 1.00 64.71  ? 352 GLU   A N     1 
ATOM   2805 C CA    . GLU   A 1 360 ? -31.883 -129.691 -19.803 1.00 66.13  ? 352 GLU   A CA    1 
ATOM   2806 C C     . GLU   A 1 360 ? -31.261 -129.681 -18.405 1.00 65.99  ? 352 GLU   A C     1 
ATOM   2807 O O     . GLU   A 1 360 ? -31.645 -130.483 -17.555 1.00 66.30  ? 352 GLU   A O     1 
ATOM   2808 C CB    . GLU   A 1 360 ? -31.136 -130.645 -20.738 1.00 68.18  ? 352 GLU   A CB    1 
ATOM   2809 C CG    . GLU   A 1 360 ? -29.637 -130.362 -20.828 1.00 70.69  ? 352 GLU   A CG    1 
ATOM   2810 C CD    . GLU   A 1 360 ? -28.948 -130.740 -22.129 1.00 72.24  ? 352 GLU   A CD    1 
ATOM   2811 O OE1   . GLU   A 1 360 ? -29.621 -131.232 -23.060 1.00 73.32  ? 352 GLU   A OE1   1 
ATOM   2812 O OE2   . GLU   A 1 360 ? -27.718 -130.527 -22.211 1.00 72.54  ? 352 GLU   A OE2   1 
ATOM   2813 N N     . GLU   A 1 361 ? -30.304 -128.768 -18.176 1.00 65.06  ? 353 GLU   A N     1 
ATOM   2814 C CA    . GLU   A 1 361 ? -29.591 -128.672 -16.910 1.00 63.87  ? 353 GLU   A CA    1 
ATOM   2815 C C     . GLU   A 1 361 ? -30.228 -127.624 -15.997 1.00 63.97  ? 353 GLU   A C     1 
ATOM   2816 O O     . GLU   A 1 361 ? -29.608 -127.206 -15.021 1.00 62.88  ? 353 GLU   A O     1 
ATOM   2817 C CB    . GLU   A 1 361 ? -28.126 -128.331 -17.186 1.00 61.99  ? 353 GLU   A CB    1 
ATOM   2818 C CG    . GLU   A 1 361 ? -27.338 -129.497 -17.776 1.00 61.71  ? 353 GLU   A CG    1 
ATOM   2819 C CD    . GLU   A 1 361 ? -25.923 -129.160 -18.208 1.00 62.22  ? 353 GLU   A CD    1 
ATOM   2820 O OE1   . GLU   A 1 361 ? -25.535 -127.976 -18.146 1.00 64.50  ? 353 GLU   A OE1   1 
ATOM   2821 O OE2   . GLU   A 1 361 ? -25.201 -130.094 -18.610 1.00 62.74  ? 353 GLU   A OE2   1 
ATOM   2822 N N     . LYS   A 1 362 ? -31.474 -127.229 -16.297 1.00 64.37  ? 354 LYS   A N     1 
ATOM   2823 C CA    . LYS   A 1 362 ? -32.137 -126.137 -15.600 1.00 65.45  ? 354 LYS   A CA    1 
ATOM   2824 C C     . LYS   A 1 362 ? -31.984 -126.289 -14.089 1.00 66.05  ? 354 LYS   A C     1 
ATOM   2825 O O     . LYS   A 1 362 ? -31.550 -125.355 -13.418 1.00 68.31  ? 354 LYS   A O     1 
ATOM   2826 C CB    . LYS   A 1 362 ? -33.626 -126.059 -15.958 1.00 67.39  ? 354 LYS   A CB    1 
ATOM   2827 C CG    . LYS   A 1 362 ? -34.352 -124.883 -15.324 1.00 69.79  ? 354 LYS   A CG    1 
ATOM   2828 C CD    . LYS   A 1 362 ? -35.761 -124.636 -15.847 1.00 70.77  ? 354 LYS   A CD    1 
ATOM   2829 C CE    . LYS   A 1 362 ? -36.749 -125.641 -15.353 1.00 71.78  ? 354 LYS   A CE    1 
ATOM   2830 N NZ    . LYS   A 1 362 ? -38.119 -125.228 -15.662 1.00 73.15  ? 354 LYS   A NZ    1 
ATOM   2831 N N     . ASP   A 1 363 ? -32.351 -127.464 -13.565 1.00 66.40  ? 355 ASP   A N     1 
ATOM   2832 C CA    . ASP   A 1 363 ? -32.401 -127.686 -12.128 1.00 66.88  ? 355 ASP   A CA    1 
ATOM   2833 C C     . ASP   A 1 363 ? -31.116 -128.339 -11.622 1.00 66.87  ? 355 ASP   A C     1 
ATOM   2834 O O     . ASP   A 1 363 ? -30.853 -128.315 -10.422 1.00 66.75  ? 355 ASP   A O     1 
ATOM   2835 C CB    . ASP   A 1 363 ? -33.649 -128.459 -11.735 1.00 67.96  ? 355 ASP   A CB    1 
ATOM   2836 C CG    . ASP   A 1 363 ? -34.943 -127.663 -11.816 1.00 69.43  ? 355 ASP   A CG    1 
ATOM   2837 O OD1   . ASP   A 1 363 ? -35.355 -127.324 -12.946 1.00 68.59  ? 355 ASP   A OD1   1 
ATOM   2838 O OD2   . ASP   A 1 363 ? -35.516 -127.371 -10.746 1.00 71.65  ? 355 ASP   A OD2   1 
ATOM   2839 N N     . THR   A 1 364 ? -30.313 -128.904 -12.531 1.00 67.74  ? 356 THR   A N     1 
ATOM   2840 C CA    . THR   A 1 364 ? -29.068 -129.553 -12.150 1.00 67.98  ? 356 THR   A CA    1 
ATOM   2841 C C     . THR   A 1 364 ? -28.019 -128.497 -11.795 1.00 68.73  ? 356 THR   A C     1 
ATOM   2842 O O     . THR   A 1 364 ? -27.184 -128.730 -10.922 1.00 67.09  ? 356 THR   A O     1 
ATOM   2843 C CB    . THR   A 1 364 ? -28.573 -130.467 -13.273 1.00 67.50  ? 356 THR   A CB    1 
ATOM   2844 O OG1   . THR   A 1 364 ? -28.142 -129.601 -14.320 1.00 67.85  ? 356 THR   A OG1   1 
ATOM   2845 C CG2   . THR   A 1 364 ? -29.636 -131.425 -13.783 1.00 67.18  ? 356 THR   A CG2   1 
ATOM   2846 N N     . ASN   A 1 365 ? -28.074 -127.336 -12.469 1.00 68.87  ? 357 ASN   A N     1 
ATOM   2847 C CA    . ASN   A 1 365 ? -26.971 -126.386 -12.476 1.00 67.25  ? 357 ASN   A CA    1 
ATOM   2848 C C     . ASN   A 1 365 ? -27.374 -125.075 -11.799 1.00 66.07  ? 357 ASN   A C     1 
ATOM   2849 O O     . ASN   A 1 365 ? -28.215 -124.339 -12.315 1.00 66.25  ? 357 ASN   A O     1 
ATOM   2850 C CB    . ASN   A 1 365 ? -26.487 -126.120 -13.897 1.00 66.82  ? 357 ASN   A CB    1 
ATOM   2851 C CG    . ASN   A 1 365 ? -25.082 -125.566 -13.944 1.00 65.91  ? 357 ASN   A CG    1 
ATOM   2852 O OD1   . ASN   A 1 365 ? -24.429 -125.416 -12.905 1.00 63.40  ? 357 ASN   A OD1   1 
ATOM   2853 N ND2   . ASN   A 1 365 ? -24.594 -125.271 -15.140 1.00 66.21  ? 357 ASN   A ND2   1 
ATOM   2854 N N     . VAL   A 1 366 ? -26.741 -124.798 -10.649 1.00 63.16  ? 358 VAL   A N     1 
ATOM   2855 C CA    . VAL   A 1 366 ? -26.862 -123.530 -9.947  1.00 59.86  ? 358 VAL   A CA    1 
ATOM   2856 C C     . VAL   A 1 366 ? -25.591 -122.720 -10.201 1.00 57.53  ? 358 VAL   A C     1 
ATOM   2857 O O     . VAL   A 1 366 ? -24.508 -123.127 -9.785  1.00 55.17  ? 358 VAL   A O     1 
ATOM   2858 C CB    . VAL   A 1 366 ? -27.083 -123.740 -8.435  1.00 59.03  ? 358 VAL   A CB    1 
ATOM   2859 C CG1   . VAL   A 1 366 ? -27.155 -122.420 -7.675  1.00 58.96  ? 358 VAL   A CG1   1 
ATOM   2860 C CG2   . VAL   A 1 366 ? -28.319 -124.583 -8.143  1.00 58.31  ? 358 VAL   A CG2   1 
ATOM   2861 N N     . GLN   A 1 367 ? -25.736 -121.570 -10.874 1.00 56.56  ? 359 GLN   A N     1 
ATOM   2862 C CA    . GLN   A 1 367 ? -24.603 -120.723 -11.220 1.00 54.89  ? 359 GLN   A CA    1 
ATOM   2863 C C     . GLN   A 1 367 ? -24.199 -119.875 -10.015 1.00 52.53  ? 359 GLN   A C     1 
ATOM   2864 O O     . GLN   A 1 367 ? -25.055 -119.352 -9.305  1.00 52.20  ? 359 GLN   A O     1 
ATOM   2865 C CB    . GLN   A 1 367 ? -24.931 -119.805 -12.400 1.00 54.49  ? 359 GLN   A CB    1 
ATOM   2866 C CG    . GLN   A 1 367 ? -24.987 -120.501 -13.756 1.00 54.39  ? 359 GLN   A CG    1 
ATOM   2867 C CD    . GLN   A 1 367 ? -23.645 -121.027 -14.214 1.00 54.43  ? 359 GLN   A CD    1 
ATOM   2868 O OE1   . GLN   A 1 367 ? -22.919 -120.365 -14.963 1.00 54.55  ? 359 GLN   A OE1   1 
ATOM   2869 N NE2   . GLN   A 1 367 ? -23.286 -122.216 -13.752 1.00 54.62  ? 359 GLN   A NE2   1 
ATOM   2870 N N     . VAL   A 1 368 ? -22.883 -119.733 -9.809  1.00 49.75  ? 360 VAL   A N     1 
ATOM   2871 C CA    . VAL   A 1 368 ? -22.349 -118.954 -8.703  1.00 48.46  ? 360 VAL   A CA    1 
ATOM   2872 C C     . VAL   A 1 368 ? -22.084 -117.529 -9.187  1.00 46.07  ? 360 VAL   A C     1 
ATOM   2873 O O     . VAL   A 1 368 ? -21.137 -117.295 -9.935  1.00 44.84  ? 360 VAL   A O     1 
ATOM   2874 C CB    . VAL   A 1 368 ? -21.074 -119.606 -8.131  1.00 49.04  ? 360 VAL   A CB    1 
ATOM   2875 C CG1   . VAL   A 1 368 ? -20.483 -118.797 -6.982  1.00 48.97  ? 360 VAL   A CG1   1 
ATOM   2876 C CG2   . VAL   A 1 368 ? -21.321 -121.044 -7.688  1.00 48.63  ? 360 VAL   A CG2   1 
ATOM   2877 N N     . LEU   A 1 369 ? -22.934 -116.590 -8.743  1.00 44.67  ? 361 LEU   A N     1 
ATOM   2878 C CA    . LEU   A 1 369 ? -22.789 -115.173 -9.047  1.00 44.42  ? 361 LEU   A CA    1 
ATOM   2879 C C     . LEU   A 1 369 ? -22.144 -114.446 -7.868  1.00 42.82  ? 361 LEU   A C     1 
ATOM   2880 O O     . LEU   A 1 369 ? -22.424 -114.758 -6.713  1.00 43.54  ? 361 LEU   A O     1 
ATOM   2881 C CB    . LEU   A 1 369 ? -24.150 -114.554 -9.366  1.00 44.83  ? 361 LEU   A CB    1 
ATOM   2882 C CG    . LEU   A 1 369 ? -24.580 -114.579 -10.834 1.00 45.73  ? 361 LEU   A CG    1 
ATOM   2883 C CD1   . LEU   A 1 369 ? -24.686 -116.001 -11.352 1.00 45.89  ? 361 LEU   A CD1   1 
ATOM   2884 C CD2   . LEU   A 1 369 ? -25.893 -113.832 -11.002 1.00 45.86  ? 361 LEU   A CD2   1 
ATOM   2885 N N     . MET   A 1 370 ? -21.307 -113.447 -8.176  1.00 40.39  ? 362 MET   A N     1 
ATOM   2886 C CA    . MET   A 1 370 ? -20.697 -112.612 -7.154  1.00 38.91  ? 362 MET   A CA    1 
ATOM   2887 C C     . MET   A 1 370 ? -20.767 -111.145 -7.574  1.00 36.69  ? 362 MET   A C     1 
ATOM   2888 O O     . MET   A 1 370 ? -20.144 -110.747 -8.556  1.00 36.37  ? 362 MET   A O     1 
ATOM   2889 C CB    . MET   A 1 370 ? -19.240 -113.020 -6.916  1.00 39.26  ? 362 MET   A CB    1 
ATOM   2890 C CG    . MET   A 1 370 ? -19.088 -114.401 -6.317  1.00 40.18  ? 362 MET   A CG    1 
ATOM   2891 S SD    . MET   A 1 370 ? -17.359 -114.806 -6.007  1.00 42.10  ? 362 MET   A SD    1 
ATOM   2892 C CE    . MET   A 1 370 ? -17.480 -116.437 -5.261  1.00 42.76  ? 362 MET   A CE    1 
ATOM   2893 N N     . VAL   A 1 371 ? -21.538 -110.356 -6.816  1.00 34.03  ? 363 VAL   A N     1 
ATOM   2894 C CA    . VAL   A 1 371 ? -21.618 -108.918 -7.012  1.00 33.02  ? 363 VAL   A CA    1 
ATOM   2895 C C     . VAL   A 1 371 ? -20.447 -108.283 -6.264  1.00 31.37  ? 363 VAL   A C     1 
ATOM   2896 O O     . VAL   A 1 371 ? -20.364 -108.402 -5.044  1.00 30.93  ? 363 VAL   A O     1 
ATOM   2897 C CB    . VAL   A 1 371 ? -22.963 -108.343 -6.525  1.00 33.49  ? 363 VAL   A CB    1 
ATOM   2898 C CG1   . VAL   A 1 371 ? -23.095 -106.859 -6.846  1.00 33.61  ? 363 VAL   A CG1   1 
ATOM   2899 C CG2   . VAL   A 1 371 ? -24.155 -109.112 -7.084  1.00 33.95  ? 363 VAL   A CG2   1 
ATOM   2900 N N     . LEU   A 1 372 ? -19.548 -107.620 -7.002  1.00 29.65  ? 364 LEU   A N     1 
ATOM   2901 C CA    . LEU   A 1 372 ? -18.305 -107.123 -6.432  1.00 28.91  ? 364 LEU   A CA    1 
ATOM   2902 C C     . LEU   A 1 372 ? -18.377 -105.604 -6.308  1.00 28.44  ? 364 LEU   A C     1 
ATOM   2903 O O     . LEU   A 1 372 ? -18.089 -104.886 -7.263  1.00 28.73  ? 364 LEU   A O     1 
ATOM   2904 C CB    . LEU   A 1 372 ? -17.112 -107.566 -7.277  1.00 28.45  ? 364 LEU   A CB    1 
ATOM   2905 C CG    . LEU   A 1 372 ? -16.908 -109.077 -7.433  1.00 28.05  ? 364 LEU   A CG    1 
ATOM   2906 C CD1   . LEU   A 1 372 ? -15.492 -109.356 -7.903  1.00 27.80  ? 364 LEU   A CD1   1 
ATOM   2907 C CD2   . LEU   A 1 372 ? -17.206 -109.845 -6.155  1.00 28.11  ? 364 LEU   A CD2   1 
ATOM   2908 N N     . GLY   A 1 373 ? -18.735 -105.137 -5.106  1.00 27.27  ? 365 GLY   A N     1 
ATOM   2909 C CA    . GLY   A 1 373 ? -19.076 -103.745 -4.878  1.00 26.79  ? 365 GLY   A CA    1 
ATOM   2910 C C     . GLY   A 1 373 ? -20.591 -103.569 -4.890  1.00 26.62  ? 365 GLY   A C     1 
ATOM   2911 O O     . GLY   A 1 373 ? -21.129 -102.845 -5.724  1.00 26.27  ? 365 GLY   A O     1 
ATOM   2912 N N     . ALA   A 1 374 ? -21.249 -104.231 -3.931  1.00 26.87  ? 366 ALA   A N     1 
ATOM   2913 C CA    . ALA   A 1 374 ? -22.686 -104.461 -3.963  1.00 27.52  ? 366 ALA   A CA    1 
ATOM   2914 C C     . ALA   A 1 374 ? -23.477 -103.249 -3.471  1.00 28.02  ? 366 ALA   A C     1 
ATOM   2915 O O     . ALA   A 1 374 ? -24.675 -103.164 -3.727  1.00 28.60  ? 366 ALA   A O     1 
ATOM   2916 C CB    . ALA   A 1 374 ? -23.014 -105.686 -3.139  1.00 27.42  ? 366 ALA   A CB    1 
ATOM   2917 N N     . GLY   A 1 375 ? -22.818 -102.334 -2.748  1.00 28.34  ? 367 GLY   A N     1 
ATOM   2918 C CA    . GLY   A 1 375 ? -23.472 -101.142 -2.228  1.00 28.99  ? 367 GLY   A CA    1 
ATOM   2919 C C     . GLY   A 1 375 ? -24.696 -101.497 -1.386  1.00 29.77  ? 367 GLY   A C     1 
ATOM   2920 O O     . GLY   A 1 375 ? -24.586 -102.257 -0.427  1.00 29.88  ? 367 GLY   A O     1 
ATOM   2921 N N     . ARG   A 1 376 ? -25.858 -100.951 -1.767  1.00 30.78  ? 368 ARG   A N     1 
ATOM   2922 C CA    . ARG   A 1 376 ? -27.115 -101.254 -1.101  1.00 32.18  ? 368 ARG   A CA    1 
ATOM   2923 C C     . ARG   A 1 376 ? -27.899 -102.310 -1.886  1.00 33.94  ? 368 ARG   A C     1 
ATOM   2924 O O     . ARG   A 1 376 ? -29.077 -102.531 -1.610  1.00 35.59  ? 368 ARG   A O     1 
ATOM   2925 C CB    . ARG   A 1 376 ? -27.946 -99.980  -0.908  1.00 32.09  ? 368 ARG   A CB    1 
ATOM   2926 C CG    . ARG   A 1 376 ? -27.159 -98.783  -0.389  1.00 31.98  ? 368 ARG   A CG    1 
ATOM   2927 C CD    . ARG   A 1 376 ? -28.003 -97.800  0.415   1.00 31.23  ? 368 ARG   A CD    1 
ATOM   2928 N NE    . ARG   A 1 376 ? -29.177 -97.304  -0.313  1.00 30.87  ? 368 ARG   A NE    1 
ATOM   2929 C CZ    . ARG   A 1 376 ? -30.092 -96.472  0.179   1.00 30.85  ? 368 ARG   A CZ    1 
ATOM   2930 N NH1   . ARG   A 1 376 ? -30.002 -96.037  1.425   1.00 30.28  ? 368 ARG   A NH1   1 
ATOM   2931 N NH2   . ARG   A 1 376 ? -31.101 -96.075  -0.578  1.00 30.98  ? 368 ARG   A NH2   1 
ATOM   2932 N N     . GLY   A 1 377 ? -27.244 -102.939 -2.874  1.00 34.40  ? 369 GLY   A N     1 
ATOM   2933 C CA    . GLY   A 1 377 ? -27.704 -104.189 -3.463  1.00 35.16  ? 369 GLY   A CA    1 
ATOM   2934 C C     . GLY   A 1 377 ? -28.530 -104.050 -4.747  1.00 35.22  ? 369 GLY   A C     1 
ATOM   2935 O O     . GLY   A 1 377 ? -29.316 -104.948 -5.047  1.00 34.46  ? 369 GLY   A O     1 
ATOM   2936 N N     . PRO   A 1 378 ? -28.398 -102.981 -5.571  1.00 35.62  ? 370 PRO   A N     1 
ATOM   2937 C CA    . PRO   A 1 378 ? -29.157 -102.907 -6.823  1.00 35.75  ? 370 PRO   A CA    1 
ATOM   2938 C C     . PRO   A 1 378 ? -28.805 -104.003 -7.829  1.00 36.24  ? 370 PRO   A C     1 
ATOM   2939 O O     . PRO   A 1 378 ? -29.688 -104.498 -8.529  1.00 36.90  ? 370 PRO   A O     1 
ATOM   2940 C CB    . PRO   A 1 378 ? -28.884 -101.498 -7.378  1.00 35.64  ? 370 PRO   A CB    1 
ATOM   2941 C CG    . PRO   A 1 378 ? -27.644 -101.020 -6.654  1.00 35.59  ? 370 PRO   A CG    1 
ATOM   2942 C CD    . PRO   A 1 378 ? -27.566 -101.790 -5.346  1.00 35.27  ? 370 PRO   A CD    1 
ATOM   2943 N N     . LEU   A 1 379 ? -27.522 -104.380 -7.903  1.00 36.26  ? 371 LEU   A N     1 
ATOM   2944 C CA    . LEU   A 1 379 ? -27.092 -105.430 -8.816  1.00 36.43  ? 371 LEU   A CA    1 
ATOM   2945 C C     . LEU   A 1 379 ? -27.472 -106.794 -8.252  1.00 37.94  ? 371 LEU   A C     1 
ATOM   2946 O O     . LEU   A 1 379 ? -27.684 -107.736 -9.012  1.00 38.89  ? 371 LEU   A O     1 
ATOM   2947 C CB    . LEU   A 1 379 ? -25.594 -105.371 -9.110  1.00 36.02  ? 371 LEU   A CB    1 
ATOM   2948 C CG    . LEU   A 1 379 ? -25.114 -104.202 -9.975  1.00 35.91  ? 371 LEU   A CG    1 
ATOM   2949 C CD1   . LEU   A 1 379 ? -23.652 -104.412 -10.321 1.00 35.59  ? 371 LEU   A CD1   1 
ATOM   2950 C CD2   . LEU   A 1 379 ? -25.934 -104.017 -11.242 1.00 36.16  ? 371 LEU   A CD2   1 
ATOM   2951 N N     . VAL   A 1 380 ? -27.530 -106.895 -6.919  1.00 39.39  ? 372 VAL   A N     1 
ATOM   2952 C CA    . VAL   A 1 380 ? -28.033 -108.091 -6.263  1.00 38.96  ? 372 VAL   A CA    1 
ATOM   2953 C C     . VAL   A 1 380 ? -29.457 -108.339 -6.757  1.00 39.06  ? 372 VAL   A C     1 
ATOM   2954 O O     . VAL   A 1 380 ? -29.749 -109.405 -7.293  1.00 37.42  ? 372 VAL   A O     1 
ATOM   2955 C CB    . VAL   A 1 380 ? -27.963 -107.967 -4.727  1.00 38.42  ? 372 VAL   A CB    1 
ATOM   2956 C CG1   . VAL   A 1 380 ? -28.688 -109.105 -4.016  1.00 38.48  ? 372 VAL   A CG1   1 
ATOM   2957 C CG2   . VAL   A 1 380 ? -26.524 -107.869 -4.233  1.00 38.13  ? 372 VAL   A CG2   1 
ATOM   2958 N N     . ASN   A 1 381 ? -30.321 -107.326 -6.608  1.00 40.01  ? 373 ASN   A N     1 
ATOM   2959 C CA    . ASN   A 1 381 ? -31.720 -107.436 -6.991  1.00 41.21  ? 373 ASN   A CA    1 
ATOM   2960 C C     . ASN   A 1 381 ? -31.840 -107.701 -8.490  1.00 41.78  ? 373 ASN   A C     1 
ATOM   2961 O O     . ASN   A 1 381 ? -32.618 -108.555 -8.906  1.00 42.80  ? 373 ASN   A O     1 
ATOM   2962 C CB    . ASN   A 1 381 ? -32.520 -106.201 -6.594  1.00 41.48  ? 373 ASN   A CB    1 
ATOM   2963 C CG    . ASN   A 1 381 ? -32.622 -106.046 -5.096  1.00 42.79  ? 373 ASN   A CG    1 
ATOM   2964 O OD1   . ASN   A 1 381 ? -32.887 -107.023 -4.386  1.00 42.14  ? 373 ASN   A OD1   1 
ATOM   2965 N ND2   . ASN   A 1 381 ? -32.405 -104.837 -4.595  1.00 44.31  ? 373 ASN   A ND2   1 
ATOM   2966 N N     . ALA   A 1 382 ? -31.076 -106.954 -9.294  1.00 41.92  ? 374 ALA   A N     1 
ATOM   2967 C CA    . ALA   A 1 382 ? -31.070 -107.140 -10.735 1.00 41.04  ? 374 ALA   A CA    1 
ATOM   2968 C C     . ALA   A 1 382 ? -30.622 -108.556 -11.091 1.00 41.37  ? 374 ALA   A C     1 
ATOM   2969 O O     . ALA   A 1 382 ? -31.074 -109.103 -12.092 1.00 41.61  ? 374 ALA   A O     1 
ATOM   2970 C CB    . ALA   A 1 382 ? -30.188 -106.101 -11.388 1.00 41.55  ? 374 ALA   A CB    1 
ATOM   2971 N N     . SER   A 1 383 ? -29.732 -109.139 -10.275 1.00 41.34  ? 375 SER   A N     1 
ATOM   2972 C CA    . SER   A 1 383 ? -29.281 -110.509 -10.475 1.00 41.67  ? 375 SER   A CA    1 
ATOM   2973 C C     . SER   A 1 383 ? -30.406 -111.496 -10.168 1.00 43.27  ? 375 SER   A C     1 
ATOM   2974 O O     . SER   A 1 383 ? -30.526 -112.524 -10.831 1.00 44.13  ? 375 SER   A O     1 
ATOM   2975 C CB    . SER   A 1 383 ? -28.053 -110.822 -9.650  1.00 41.19  ? 375 SER   A CB    1 
ATOM   2976 O OG    . SER   A 1 383 ? -26.918 -110.094 -10.099 1.00 40.76  ? 375 SER   A OG    1 
ATOM   2977 N N     . LEU   A 1 384 ? -31.214 -111.189 -9.145  1.00 44.35  ? 376 LEU   A N     1 
ATOM   2978 C CA    . LEU   A 1 384 ? -32.352 -112.021 -8.788  1.00 45.17  ? 376 LEU   A CA    1 
ATOM   2979 C C     . LEU   A 1 384 ? -33.409 -111.932 -9.886  1.00 46.39  ? 376 LEU   A C     1 
ATOM   2980 O O     . LEU   A 1 384 ? -33.886 -112.956 -10.371 1.00 47.24  ? 376 LEU   A O     1 
ATOM   2981 C CB    . LEU   A 1 384 ? -32.915 -111.603 -7.430  1.00 45.29  ? 376 LEU   A CB    1 
ATOM   2982 C CG    . LEU   A 1 384 ? -31.984 -111.786 -6.225  1.00 45.91  ? 376 LEU   A CG    1 
ATOM   2983 C CD1   . LEU   A 1 384 ? -32.545 -111.071 -5.006  1.00 45.24  ? 376 LEU   A CD1   1 
ATOM   2984 C CD2   . LEU   A 1 384 ? -31.738 -113.255 -5.911  1.00 45.54  ? 376 LEU   A CD2   1 
ATOM   2985 N N     . ARG   A 1 385 ? -33.755 -110.699 -10.282 1.00 46.83  ? 377 ARG   A N     1 
ATOM   2986 C CA    . ARG   A 1 385 ? -34.737 -110.466 -11.330 1.00 47.72  ? 377 ARG   A CA    1 
ATOM   2987 C C     . ARG   A 1 385 ? -34.301 -111.140 -12.633 1.00 48.66  ? 377 ARG   A C     1 
ATOM   2988 O O     . ARG   A 1 385 ? -35.145 -111.551 -13.426 1.00 49.76  ? 377 ARG   A O     1 
ATOM   2989 C CB    . ARG   A 1 385 ? -34.981 -108.966 -11.536 1.00 47.12  ? 377 ARG   A CB    1 
ATOM   2990 C CG    . ARG   A 1 385 ? -35.760 -108.303 -10.409 1.00 47.21  ? 377 ARG   A CG    1 
ATOM   2991 C CD    . ARG   A 1 385 ? -36.301 -106.935 -10.803 1.00 47.88  ? 377 ARG   A CD    1 
ATOM   2992 N NE    . ARG   A 1 385 ? -35.295 -106.062 -11.421 1.00 48.86  ? 377 ARG   A NE    1 
ATOM   2993 C CZ    . ARG   A 1 385 ? -34.249 -105.496 -10.817 1.00 48.48  ? 377 ARG   A CZ    1 
ATOM   2994 N NH1   . ARG   A 1 385 ? -34.039 -105.662 -9.522  1.00 47.94  ? 377 ARG   A NH1   1 
ATOM   2995 N NH2   . ARG   A 1 385 ? -33.410 -104.751 -11.518 1.00 48.18  ? 377 ARG   A NH2   1 
ATOM   2996 N N     . ALA   A 1 386 ? -32.984 -111.247 -12.846 1.00 49.16  ? 378 ALA   A N     1 
ATOM   2997 C CA    . ALA   A 1 386 ? -32.441 -111.901 -14.026 1.00 49.06  ? 378 ALA   A CA    1 
ATOM   2998 C C     . ALA   A 1 386 ? -32.753 -113.395 -13.996 1.00 50.79  ? 378 ALA   A C     1 
ATOM   2999 O O     . ALA   A 1 386 ? -33.293 -113.931 -14.960 1.00 50.29  ? 378 ALA   A O     1 
ATOM   3000 C CB    . ALA   A 1 386 ? -30.949 -111.661 -14.114 1.00 48.53  ? 378 ALA   A CB    1 
ATOM   3001 N N     . ALA   A 1 387 ? -32.407 -114.049 -12.880 1.00 53.19  ? 379 ALA   A N     1 
ATOM   3002 C CA    . ALA   A 1 387 ? -32.495 -115.497 -12.760 1.00 55.61  ? 379 ALA   A CA    1 
ATOM   3003 C C     . ALA   A 1 387 ? -33.951 -115.964 -12.751 1.00 57.94  ? 379 ALA   A C     1 
ATOM   3004 O O     . ALA   A 1 387 ? -34.249 -117.055 -13.234 1.00 58.20  ? 379 ALA   A O     1 
ATOM   3005 C CB    . ALA   A 1 387 ? -31.767 -115.953 -11.515 1.00 56.10  ? 379 ALA   A CB    1 
ATOM   3006 N N     . LYS   A 1 388 ? -34.843 -115.139 -12.188 1.00 59.73  ? 380 LYS   A N     1 
ATOM   3007 C CA    . LYS   A 1 388 ? -36.272 -115.410 -12.209 1.00 62.39  ? 380 LYS   A CA    1 
ATOM   3008 C C     . LYS   A 1 388 ? -36.759 -115.477 -13.655 1.00 62.38  ? 380 LYS   A C     1 
ATOM   3009 O O     . LYS   A 1 388 ? -37.410 -116.440 -14.051 1.00 62.93  ? 380 LYS   A O     1 
ATOM   3010 C CB    . LYS   A 1 388 ? -37.029 -114.324 -11.435 1.00 65.65  ? 380 LYS   A CB    1 
ATOM   3011 C CG    . LYS   A 1 388 ? -38.531 -114.546 -11.287 1.00 67.62  ? 380 LYS   A CG    1 
ATOM   3012 C CD    . LYS   A 1 388 ? -39.233 -113.532 -10.390 1.00 69.92  ? 380 LYS   A CD    1 
ATOM   3013 C CE    . LYS   A 1 388 ? -39.233 -112.142 -10.957 1.00 71.75  ? 380 LYS   A CE    1 
ATOM   3014 N NZ    . LYS   A 1 388 ? -40.028 -111.216 -10.147 1.00 72.50  ? 380 LYS   A NZ    1 
ATOM   3015 N N     . GLN   A 1 389 ? -36.423 -114.438 -14.430 1.00 62.42  ? 381 GLN   A N     1 
ATOM   3016 C CA    . GLN   A 1 389 ? -36.824 -114.316 -15.822 1.00 62.15  ? 381 GLN   A CA    1 
ATOM   3017 C C     . GLN   A 1 389 ? -36.152 -115.391 -16.675 1.00 60.83  ? 381 GLN   A C     1 
ATOM   3018 O O     . GLN   A 1 389 ? -36.761 -115.915 -17.604 1.00 58.44  ? 381 GLN   A O     1 
ATOM   3019 C CB    . GLN   A 1 389 ? -36.437 -112.914 -16.294 1.00 63.56  ? 381 GLN   A CB    1 
ATOM   3020 C CG    . GLN   A 1 389 ? -36.885 -112.569 -17.710 1.00 64.07  ? 381 GLN   A CG    1 
ATOM   3021 C CD    . GLN   A 1 389 ? -36.117 -111.406 -18.302 1.00 63.48  ? 381 GLN   A CD    1 
ATOM   3022 O OE1   . GLN   A 1 389 ? -35.362 -110.712 -17.611 1.00 62.41  ? 381 GLN   A OE1   1 
ATOM   3023 N NE2   . GLN   A 1 389 ? -36.300 -111.185 -19.596 1.00 63.41  ? 381 GLN   A NE2   1 
ATOM   3024 N N     . ALA   A 1 390 ? -34.889 -115.703 -16.357 1.00 61.70  ? 382 ALA   A N     1 
ATOM   3025 C CA    . ALA   A 1 390 ? -34.104 -116.674 -17.106 1.00 62.24  ? 382 ALA   A CA    1 
ATOM   3026 C C     . ALA   A 1 390 ? -34.549 -118.103 -16.794 1.00 62.69  ? 382 ALA   A C     1 
ATOM   3027 O O     . ALA   A 1 390 ? -34.211 -119.027 -17.532 1.00 60.43  ? 382 ALA   A O     1 
ATOM   3028 C CB    . ALA   A 1 390 ? -32.634 -116.492 -16.791 1.00 62.66  ? 382 ALA   A CB    1 
ATOM   3029 N N     . ASP   A 1 391 ? -35.282 -118.277 -15.687 1.00 65.15  ? 383 ASP   A N     1 
ATOM   3030 C CA    . ASP   A 1 391 ? -35.682 -119.593 -15.217 1.00 66.96  ? 383 ASP   A CA    1 
ATOM   3031 C C     . ASP   A 1 391 ? -34.428 -120.444 -15.024 1.00 65.91  ? 383 ASP   A C     1 
ATOM   3032 O O     . ASP   A 1 391 ? -34.343 -121.561 -15.530 1.00 65.50  ? 383 ASP   A O     1 
ATOM   3033 C CB    . ASP   A 1 391 ? -36.709 -120.227 -16.145 1.00 68.22  ? 383 ASP   A CB    1 
ATOM   3034 C CG    . ASP   A 1 391 ? -37.491 -121.398 -15.564 1.00 69.14  ? 383 ASP   A CG    1 
ATOM   3035 O OD1   . ASP   A 1 391 ? -37.418 -121.606 -14.333 1.00 68.28  ? 383 ASP   A OD1   1 
ATOM   3036 O OD2   . ASP   A 1 391 ? -38.160 -122.102 -16.350 1.00 69.88  ? 383 ASP   A OD2   1 
ATOM   3037 N N     . ARG   A 1 392 ? -33.452 -119.878 -14.305 1.00 64.16  ? 384 ARG   A N     1 
ATOM   3038 C CA    . ARG   A 1 392 ? -32.238 -120.585 -13.932 1.00 63.79  ? 384 ARG   A CA    1 
ATOM   3039 C C     . ARG   A 1 392 ? -31.967 -120.333 -12.451 1.00 63.31  ? 384 ARG   A C     1 
ATOM   3040 O O     . ARG   A 1 392 ? -32.598 -119.475 -11.838 1.00 62.57  ? 384 ARG   A O     1 
ATOM   3041 C CB    . ARG   A 1 392 ? -31.073 -120.152 -14.830 1.00 64.37  ? 384 ARG   A CB    1 
ATOM   3042 C CG    . ARG   A 1 392 ? -31.172 -120.622 -16.276 1.00 64.59  ? 384 ARG   A CG    1 
ATOM   3043 C CD    . ARG   A 1 392 ? -31.183 -122.142 -16.403 1.00 63.85  ? 384 ARG   A CD    1 
ATOM   3044 N NE    . ARG   A 1 392 ? -31.089 -122.593 -17.796 1.00 62.60  ? 384 ARG   A NE    1 
ATOM   3045 C CZ    . ARG   A 1 392 ? -31.997 -122.405 -18.748 1.00 61.20  ? 384 ARG   A CZ    1 
ATOM   3046 N NH1   . ARG   A 1 392 ? -33.155 -121.826 -18.478 1.00 60.73  ? 384 ARG   A NH1   1 
ATOM   3047 N NH2   . ARG   A 1 392 ? -31.744 -122.818 -19.977 1.00 61.34  ? 384 ARG   A NH2   1 
ATOM   3048 N N     . ARG   A 1 393 ? -31.027 -121.101 -11.890 1.00 63.22  ? 385 ARG   A N     1 
ATOM   3049 C CA    . ARG   A 1 393 ? -30.772 -121.102 -10.458 1.00 63.45  ? 385 ARG   A CA    1 
ATOM   3050 C C     . ARG   A 1 393 ? -29.389 -120.508 -10.194 1.00 61.10  ? 385 ARG   A C     1 
ATOM   3051 O O     . ARG   A 1 393 ? -28.439 -120.823 -10.909 1.00 58.14  ? 385 ARG   A O     1 
ATOM   3052 C CB    . ARG   A 1 393 ? -30.890 -122.543 -9.948  1.00 65.70  ? 385 ARG   A CB    1 
ATOM   3053 C CG    . ARG   A 1 393 ? -32.127 -123.280 -10.444 1.00 67.97  ? 385 ARG   A CG    1 
ATOM   3054 C CD    . ARG   A 1 393 ? -32.233 -124.695 -9.899  1.00 70.29  ? 385 ARG   A CD    1 
ATOM   3055 N NE    . ARG   A 1 393 ? -32.141 -124.725 -8.435  1.00 70.83  ? 385 ARG   A NE    1 
ATOM   3056 C CZ    . ARG   A 1 393 ? -31.496 -125.634 -7.706  1.00 71.33  ? 385 ARG   A CZ    1 
ATOM   3057 N NH1   . ARG   A 1 393 ? -31.029 -126.742 -8.260  1.00 70.59  ? 385 ARG   A NH1   1 
ATOM   3058 N NH2   . ARG   A 1 393 ? -31.352 -125.448 -6.405  1.00 71.65  ? 385 ARG   A NH2   1 
ATOM   3059 N N     . ILE   A 1 394 ? -29.287 -119.648 -9.168  1.00 59.53  ? 386 ILE   A N     1 
ATOM   3060 C CA    . ILE   A 1 394 ? -28.044 -118.945 -8.880  1.00 56.88  ? 386 ILE   A CA    1 
ATOM   3061 C C     . ILE   A 1 394 ? -27.799 -118.858 -7.372  1.00 55.45  ? 386 ILE   A C     1 
ATOM   3062 O O     . ILE   A 1 394 ? -28.734 -118.789 -6.576  1.00 54.01  ? 386 ILE   A O     1 
ATOM   3063 C CB    . ILE   A 1 394 ? -28.034 -117.542 -9.515  1.00 56.34  ? 386 ILE   A CB    1 
ATOM   3064 C CG1   . ILE   A 1 394 ? -29.254 -116.719 -9.097  1.00 56.66  ? 386 ILE   A CG1   1 
ATOM   3065 C CG2   . ILE   A 1 394 ? -27.910 -117.628 -11.037 1.00 56.02  ? 386 ILE   A CG2   1 
ATOM   3066 C CD1   . ILE   A 1 394 ? -28.992 -115.226 -9.017  1.00 56.88  ? 386 ILE   A CD1   1 
ATOM   3067 N N     . LYS   A 1 395 ? -26.510 -118.840 -7.010  1.00 53.43  ? 387 LYS   A N     1 
ATOM   3068 C CA    . LYS   A 1 395 ? -26.064 -118.564 -5.655  1.00 51.73  ? 387 LYS   A CA    1 
ATOM   3069 C C     . LYS   A 1 395 ? -25.287 -117.249 -5.655  1.00 50.49  ? 387 LYS   A C     1 
ATOM   3070 O O     . LYS   A 1 395 ? -24.311 -117.106 -6.391  1.00 49.50  ? 387 LYS   A O     1 
ATOM   3071 C CB    . LYS   A 1 395 ? -25.188 -119.716 -5.151  1.00 52.48  ? 387 LYS   A CB    1 
ATOM   3072 C CG    . LYS   A 1 395 ? -24.727 -119.593 -3.706  1.00 53.59  ? 387 LYS   A CG    1 
ATOM   3073 C CD    . LYS   A 1 395 ? -23.890 -120.775 -3.237  1.00 54.69  ? 387 LYS   A CD    1 
ATOM   3074 C CE    . LYS   A 1 395 ? -23.257 -120.540 -1.901  1.00 55.21  ? 387 LYS   A CE    1 
ATOM   3075 N NZ    . LYS   A 1 395 ? -22.399 -121.661 -1.511  1.00 55.67  ? 387 LYS   A NZ    1 
ATOM   3076 N N     . LEU   A 1 396 ? -25.725 -116.305 -4.810  1.00 50.15  ? 388 LEU   A N     1 
ATOM   3077 C CA    . LEU   A 1 396 ? -25.190 -114.951 -4.786  1.00 48.55  ? 388 LEU   A CA    1 
ATOM   3078 C C     . LEU   A 1 396 ? -24.259 -114.754 -3.592  1.00 46.23  ? 388 LEU   A C     1 
ATOM   3079 O O     . LEU   A 1 396 ? -24.572 -115.164 -2.476  1.00 47.09  ? 388 LEU   A O     1 
ATOM   3080 C CB    . LEU   A 1 396 ? -26.339 -113.943 -4.730  1.00 48.58  ? 388 LEU   A CB    1 
ATOM   3081 C CG    . LEU   A 1 396 ? -26.945 -113.533 -6.074  1.00 48.56  ? 388 LEU   A CG    1 
ATOM   3082 C CD1   . LEU   A 1 396 ? -28.280 -112.840 -5.879  1.00 48.38  ? 388 LEU   A CD1   1 
ATOM   3083 C CD2   . LEU   A 1 396 ? -25.987 -112.632 -6.833  1.00 49.12  ? 388 LEU   A CD2   1 
ATOM   3084 N N     . TYR   A 1 397 ? -23.117 -114.109 -3.853  1.00 43.83  ? 389 TYR   A N     1 
ATOM   3085 C CA    . TYR   A 1 397 ? -22.373 -113.394 -2.829  1.00 41.95  ? 389 TYR   A CA    1 
ATOM   3086 C C     . TYR   A 1 397 ? -22.496 -111.906 -3.133  1.00 39.41  ? 389 TYR   A C     1 
ATOM   3087 O O     . TYR   A 1 397 ? -22.532 -111.516 -4.298  1.00 38.97  ? 389 TYR   A O     1 
ATOM   3088 C CB    . TYR   A 1 397 ? -20.896 -113.791 -2.765  1.00 42.43  ? 389 TYR   A CB    1 
ATOM   3089 C CG    . TYR   A 1 397 ? -20.665 -115.267 -2.480  1.00 43.50  ? 389 TYR   A CG    1 
ATOM   3090 C CD1   . TYR   A 1 397 ? -20.906 -116.225 -3.457  1.00 43.57  ? 389 TYR   A CD1   1 
ATOM   3091 C CD2   . TYR   A 1 397 ? -20.202 -115.703 -1.242  1.00 44.82  ? 389 TYR   A CD2   1 
ATOM   3092 C CE1   . TYR   A 1 397 ? -20.702 -117.572 -3.212  1.00 43.80  ? 389 TYR   A CE1   1 
ATOM   3093 C CE2   . TYR   A 1 397 ? -19.990 -117.049 -0.986  1.00 44.63  ? 389 TYR   A CE2   1 
ATOM   3094 C CZ    . TYR   A 1 397 ? -20.242 -117.985 -1.975  1.00 44.62  ? 389 TYR   A CZ    1 
ATOM   3095 O OH    . TYR   A 1 397 ? -20.047 -119.315 -1.754  1.00 45.32  ? 389 TYR   A OH    1 
ATOM   3096 N N     . ALA   A 1 398 ? -22.587 -111.095 -2.074  1.00 37.10  ? 390 ALA   A N     1 
ATOM   3097 C CA    . ALA   A 1 398 ? -22.593 -109.647 -2.198  1.00 35.87  ? 390 ALA   A CA    1 
ATOM   3098 C C     . ALA   A 1 398 ? -21.398 -109.088 -1.432  1.00 34.88  ? 390 ALA   A C     1 
ATOM   3099 O O     . ALA   A 1 398 ? -21.424 -109.023 -0.205  1.00 35.61  ? 390 ALA   A O     1 
ATOM   3100 C CB    . ALA   A 1 398 ? -23.904 -109.082 -1.693  1.00 35.17  ? 390 ALA   A CB    1 
ATOM   3101 N N     . VAL   A 1 399 ? -20.352 -108.704 -2.175  1.00 33.03  ? 391 VAL   A N     1 
ATOM   3102 C CA    . VAL   A 1 399 ? -19.090 -108.276 -1.594  1.00 31.95  ? 391 VAL   A CA    1 
ATOM   3103 C C     . VAL   A 1 399 ? -19.052 -106.748 -1.576  1.00 30.72  ? 391 VAL   A C     1 
ATOM   3104 O O     . VAL   A 1 399 ? -19.159 -106.116 -2.625  1.00 30.31  ? 391 VAL   A O     1 
ATOM   3105 C CB    . VAL   A 1 399 ? -17.911 -108.870 -2.388  1.00 31.88  ? 391 VAL   A CB    1 
ATOM   3106 C CG1   . VAL   A 1 399 ? -16.573 -108.613 -1.704  1.00 31.85  ? 391 VAL   A CG1   1 
ATOM   3107 C CG2   . VAL   A 1 399 ? -18.096 -110.363 -2.640  1.00 32.13  ? 391 VAL   A CG2   1 
ATOM   3108 N N     . GLU   A 1 400 ? -18.906 -106.165 -0.378  1.00 28.98  ? 392 GLU   A N     1 
ATOM   3109 C CA    . GLU   A 1 400 ? -18.934 -104.719 -0.215  1.00 28.37  ? 392 GLU   A CA    1 
ATOM   3110 C C     . GLU   A 1 400 ? -17.949 -104.314 0.876   1.00 28.73  ? 392 GLU   A C     1 
ATOM   3111 O O     . GLU   A 1 400 ? -17.983 -104.867 1.975   1.00 28.98  ? 392 GLU   A O     1 
ATOM   3112 C CB    . GLU   A 1 400 ? -20.349 -104.239 0.115   1.00 27.58  ? 392 GLU   A CB    1 
ATOM   3113 C CG    . GLU   A 1 400 ? -20.456 -102.728 0.306   1.00 27.40  ? 392 GLU   A CG    1 
ATOM   3114 C CD    . GLU   A 1 400 ? -19.834 -101.899 -0.807  1.00 27.01  ? 392 GLU   A CD    1 
ATOM   3115 O OE1   . GLU   A 1 400 ? -20.369 -101.898 -1.938  1.00 26.06  ? 392 GLU   A OE1   1 
ATOM   3116 O OE2   . GLU   A 1 400 ? -18.792 -101.265 -0.539  1.00 26.45  ? 392 GLU   A OE2   1 
ATOM   3117 N N     A LYS   A 1 401 ? -17.079 -103.346 0.563   0.50 29.06  ? 393 LYS   A N     1 
ATOM   3118 N N     B LYS   A 1 401 ? -17.091 -103.335 0.557   0.50 28.61  ? 393 LYS   A N     1 
ATOM   3119 C CA    A LYS   A 1 401 ? -16.043 -102.918 1.487   0.50 29.40  ? 393 LYS   A CA    1 
ATOM   3120 C CA    B LYS   A 1 401 ? -16.031 -102.894 1.452   0.50 28.63  ? 393 LYS   A CA    1 
ATOM   3121 C C     A LYS   A 1 401 ? -16.562 -101.806 2.397   0.50 28.94  ? 393 LYS   A C     1 
ATOM   3122 C C     B LYS   A 1 401 ? -16.535 -101.785 2.373   0.50 28.52  ? 393 LYS   A C     1 
ATOM   3123 O O     A LYS   A 1 401 ? -16.079 -101.662 3.516   0.50 29.36  ? 393 LYS   A O     1 
ATOM   3124 O O     B LYS   A 1 401 ? -16.024 -101.628 3.478   0.50 28.96  ? 393 LYS   A O     1 
ATOM   3125 C CB    A LYS   A 1 401 ? -14.795 -102.420 0.754   0.50 30.04  ? 393 LYS   A CB    1 
ATOM   3126 C CB    B LYS   A 1 401 ? -14.808 -102.439 0.646   0.50 28.67  ? 393 LYS   A CB    1 
ATOM   3127 C CG    A LYS   A 1 401 ? -15.017 -101.165 -0.065  0.50 30.81  ? 393 LYS   A CG    1 
ATOM   3128 C CG    B LYS   A 1 401 ? -14.974 -101.161 -0.166  0.50 28.83  ? 393 LYS   A CG    1 
ATOM   3129 C CD    A LYS   A 1 401 ? -13.835 -100.210 -0.049  0.50 31.47  ? 393 LYS   A CD    1 
ATOM   3130 C CD    B LYS   A 1 401 ? -14.665 -99.872  0.588   0.50 28.79  ? 393 LYS   A CD    1 
ATOM   3131 C CE    A LYS   A 1 401 ? -14.100 -99.013  -0.898  0.50 31.94  ? 393 LYS   A CE    1 
ATOM   3132 C CE    B LYS   A 1 401 ? -14.641 -98.689  -0.331  0.50 28.82  ? 393 LYS   A CE    1 
ATOM   3133 N NZ    A LYS   A 1 401 ? -15.453 -98.483  -0.706  0.50 32.07  ? 393 LYS   A NZ    1 
ATOM   3134 N NZ    B LYS   A 1 401 ? -14.197 -97.459  0.329   0.50 28.52  ? 393 LYS   A NZ    1 
ATOM   3135 N N     . ASN   A 1 402 ? -17.528 -101.018 1.907   1.00 28.40  ? 394 ASN   A N     1 
ATOM   3136 C CA    . ASN   A 1 402 ? -18.129 -99.951  2.691   1.00 28.05  ? 394 ASN   A CA    1 
ATOM   3137 C C     . ASN   A 1 402 ? -18.973 -100.582 3.797   1.00 28.78  ? 394 ASN   A C     1 
ATOM   3138 O O     . ASN   A 1 402 ? -20.086 -101.029 3.533   1.00 29.39  ? 394 ASN   A O     1 
ATOM   3139 C CB    . ASN   A 1 402 ? -18.943 -99.026  1.788   1.00 27.26  ? 394 ASN   A CB    1 
ATOM   3140 C CG    . ASN   A 1 402 ? -19.555 -97.846  2.509   1.00 26.87  ? 394 ASN   A CG    1 
ATOM   3141 O OD1   . ASN   A 1 402 ? -19.522 -97.768  3.742   1.00 27.05  ? 394 ASN   A OD1   1 
ATOM   3142 N ND2   . ASN   A 1 402 ? -20.127 -96.917  1.758   1.00 26.55  ? 394 ASN   A ND2   1 
ATOM   3143 N N     . PRO   A 1 403 ? -18.502 -100.621 5.067   1.00 29.59  ? 395 PRO   A N     1 
ATOM   3144 C CA    . PRO   A 1 403 ? -19.216 -101.353 6.115   1.00 29.93  ? 395 PRO   A CA    1 
ATOM   3145 C C     . PRO   A 1 403 ? -20.551 -100.699 6.463   1.00 30.18  ? 395 PRO   A C     1 
ATOM   3146 O O     . PRO   A 1 403 ? -21.453 -101.355 6.974   1.00 30.90  ? 395 PRO   A O     1 
ATOM   3147 C CB    . PRO   A 1 403 ? -18.221 -101.323 7.284   1.00 30.11  ? 395 PRO   A CB    1 
ATOM   3148 C CG    . PRO   A 1 403 ? -17.496 -100.012 7.097   1.00 29.99  ? 395 PRO   A CG    1 
ATOM   3149 C CD    . PRO   A 1 403 ? -17.330 -99.898  5.592   1.00 29.77  ? 395 PRO   A CD    1 
ATOM   3150 N N     . ASN   A 1 404 ? -20.665 -99.398  6.179   1.00 30.48  ? 396 ASN   A N     1 
ATOM   3151 C CA    . ASN   A 1 404 ? -21.900 -98.670  6.408   1.00 30.95  ? 396 ASN   A CA    1 
ATOM   3152 C C     . ASN   A 1 404 ? -22.996 -99.237  5.509   1.00 31.59  ? 396 ASN   A C     1 
ATOM   3153 O O     . ASN   A 1 404 ? -24.122 -99.431  5.959   1.00 32.07  ? 396 ASN   A O     1 
ATOM   3154 C CB    . ASN   A 1 404 ? -21.716 -97.175  6.184   1.00 31.20  ? 396 ASN   A CB    1 
ATOM   3155 C CG    . ASN   A 1 404 ? -20.527 -96.618  6.931   1.00 31.65  ? 396 ASN   A CG    1 
ATOM   3156 O OD1   . ASN   A 1 404 ? -20.588 -96.451  8.153   1.00 32.99  ? 396 ASN   A OD1   1 
ATOM   3157 N ND2   . ASN   A 1 404 ? -19.445 -96.322  6.227   1.00 31.78  ? 396 ASN   A ND2   1 
ATOM   3158 N N     . ALA   A 1 405 ? -22.650 -99.498  4.241   1.00 31.81  ? 397 ALA   A N     1 
ATOM   3159 C CA    . ALA   A 1 405 ? -23.582 -100.052 3.270   1.00 32.01  ? 397 ALA   A CA    1 
ATOM   3160 C C     . ALA   A 1 405 ? -23.911 -101.503 3.616   1.00 32.47  ? 397 ALA   A C     1 
ATOM   3161 O O     . ALA   A 1 405 ? -25.057 -101.924 3.474   1.00 32.20  ? 397 ALA   A O     1 
ATOM   3162 C CB    . ALA   A 1 405 ? -23.002 -99.939  1.877   1.00 31.81  ? 397 ALA   A CB    1 
ATOM   3163 N N     . VAL   A 1 406 ? -22.893 -102.250 4.067   1.00 32.74  ? 398 VAL   A N     1 
ATOM   3164 C CA    . VAL   A 1 406 ? -23.045 -103.625 4.524   1.00 33.47  ? 398 VAL   A CA    1 
ATOM   3165 C C     . VAL   A 1 406 ? -24.210 -103.740 5.508   1.00 35.00  ? 398 VAL   A C     1 
ATOM   3166 O O     . VAL   A 1 406 ? -24.923 -104.739 5.508   1.00 36.92  ? 398 VAL   A O     1 
ATOM   3167 C CB    . VAL   A 1 406 ? -21.733 -104.131 5.156   1.00 32.84  ? 398 VAL   A CB    1 
ATOM   3168 C CG1   . VAL   A 1 406 ? -21.943 -105.364 6.028   1.00 32.56  ? 398 VAL   A CG1   1 
ATOM   3169 C CG2   . VAL   A 1 406 ? -20.666 -104.399 4.103   1.00 33.00  ? 398 VAL   A CG2   1 
ATOM   3170 N N     . VAL   A 1 407 ? -24.385 -102.728 6.363   1.00 36.10  ? 399 VAL   A N     1 
ATOM   3171 C CA    . VAL   A 1 407 ? -25.486 -102.708 7.312   1.00 37.28  ? 399 VAL   A CA    1 
ATOM   3172 C C     . VAL   A 1 407 ? -26.817 -102.759 6.559   1.00 37.97  ? 399 VAL   A C     1 
ATOM   3173 O O     . VAL   A 1 407 ? -27.756 -103.415 7.008   1.00 38.00  ? 399 VAL   A O     1 
ATOM   3174 C CB    . VAL   A 1 407 ? -25.376 -101.478 8.235   1.00 37.21  ? 399 VAL   A CB    1 
ATOM   3175 C CG1   . VAL   A 1 407 ? -26.692 -101.126 8.918   1.00 37.20  ? 399 VAL   A CG1   1 
ATOM   3176 C CG2   . VAL   A 1 407 ? -24.265 -101.658 9.263   1.00 37.46  ? 399 VAL   A CG2   1 
ATOM   3177 N N     . THR   A 1 408 ? -26.888 -102.070 5.413   1.00 38.63  ? 400 THR   A N     1 
ATOM   3178 C CA    . THR   A 1 408 ? -28.083 -102.079 4.582   1.00 39.66  ? 400 THR   A CA    1 
ATOM   3179 C C     . THR   A 1 408 ? -28.289 -103.476 3.995   1.00 39.24  ? 400 THR   A C     1 
ATOM   3180 O O     . THR   A 1 408 ? -29.412 -103.972 3.967   1.00 38.60  ? 400 THR   A O     1 
ATOM   3181 C CB    . THR   A 1 408 ? -27.980 -101.015 3.487   1.00 39.68  ? 400 THR   A CB    1 
ATOM   3182 O OG1   . THR   A 1 408 ? -27.637 -99.795  4.138   1.00 40.58  ? 400 THR   A OG1   1 
ATOM   3183 C CG2   . THR   A 1 408 ? -29.280 -100.834 2.724   1.00 39.58  ? 400 THR   A CG2   1 
ATOM   3184 N N     . LEU   A 1 409 ? -27.198 -104.102 3.535   1.00 39.37  ? 401 LEU   A N     1 
ATOM   3185 C CA    . LEU   A 1 409 ? -27.266 -105.400 2.881   1.00 40.80  ? 401 LEU   A CA    1 
ATOM   3186 C C     . LEU   A 1 409 ? -27.811 -106.454 3.841   1.00 41.61  ? 401 LEU   A C     1 
ATOM   3187 O O     . LEU   A 1 409 ? -28.636 -107.274 3.446   1.00 42.56  ? 401 LEU   A O     1 
ATOM   3188 C CB    . LEU   A 1 409 ? -25.893 -105.815 2.347   1.00 41.68  ? 401 LEU   A CB    1 
ATOM   3189 C CG    . LEU   A 1 409 ? -25.339 -105.009 1.167   1.00 41.77  ? 401 LEU   A CG    1 
ATOM   3190 C CD1   . LEU   A 1 409 ? -23.934 -105.481 0.827   1.00 41.32  ? 401 LEU   A CD1   1 
ATOM   3191 C CD2   . LEU   A 1 409 ? -26.235 -105.099 -0.059  1.00 41.66  ? 401 LEU   A CD2   1 
ATOM   3192 N N     . GLU   A 1 410 ? -27.338 -106.433 5.094   1.00 41.31  ? 402 GLU   A N     1 
ATOM   3193 C CA    . GLU   A 1 410 ? -27.644 -107.483 6.053   1.00 39.85  ? 402 GLU   A CA    1 
ATOM   3194 C C     . GLU   A 1 410 ? -29.072 -107.332 6.572   1.00 40.30  ? 402 GLU   A C     1 
ATOM   3195 O O     . GLU   A 1 410 ? -29.726 -108.331 6.857   1.00 39.49  ? 402 GLU   A O     1 
ATOM   3196 C CB    . GLU   A 1 410 ? -26.601 -107.502 7.170   1.00 38.97  ? 402 GLU   A CB    1 
ATOM   3197 C CG    . GLU   A 1 410 ? -25.220 -107.925 6.677   1.00 38.82  ? 402 GLU   A CG    1 
ATOM   3198 C CD    . GLU   A 1 410 ? -24.129 -107.905 7.733   1.00 39.15  ? 402 GLU   A CD    1 
ATOM   3199 O OE1   . GLU   A 1 410 ? -24.031 -106.895 8.459   1.00 39.41  ? 402 GLU   A OE1   1 
ATOM   3200 O OE2   . GLU   A 1 410 ? -23.357 -108.881 7.814   1.00 39.18  ? 402 GLU   A OE2   1 
ATOM   3201 N N     . ASN   A 1 411 ? -29.554 -106.088 6.689   1.00 41.96  ? 403 ASN   A N     1 
ATOM   3202 C CA    . ASN   A 1 411 ? -30.954 -105.844 7.001   1.00 44.13  ? 403 ASN   A CA    1 
ATOM   3203 C C     . ASN   A 1 411 ? -31.822 -106.331 5.838   1.00 46.32  ? 403 ASN   A C     1 
ATOM   3204 O O     . ASN   A 1 411 ? -32.879 -106.911 6.069   1.00 47.32  ? 403 ASN   A O     1 
ATOM   3205 C CB    . ASN   A 1 411 ? -31.226 -104.385 7.364   1.00 44.62  ? 403 ASN   A CB    1 
ATOM   3206 C CG    . ASN   A 1 411 ? -30.954 -104.071 8.820   1.00 44.58  ? 403 ASN   A CG    1 
ATOM   3207 O OD1   . ASN   A 1 411 ? -31.863 -103.660 9.551   1.00 43.84  ? 403 ASN   A OD1   1 
ATOM   3208 N ND2   . ASN   A 1 411 ? -29.714 -104.224 9.259   1.00 44.12  ? 403 ASN   A ND2   1 
ATOM   3209 N N     . TRP   A 1 412 ? -31.375 -106.090 4.595   1.00 47.96  ? 404 TRP   A N     1 
ATOM   3210 C CA    . TRP   A 1 412 ? -32.014 -106.653 3.411   1.00 49.80  ? 404 TRP   A CA    1 
ATOM   3211 C C     . TRP   A 1 412 ? -32.009 -108.178 3.477   1.00 48.89  ? 404 TRP   A C     1 
ATOM   3212 O O     . TRP   A 1 412 ? -33.042 -108.814 3.286   1.00 48.56  ? 404 TRP   A O     1 
ATOM   3213 C CB    . TRP   A 1 412 ? -31.313 -106.202 2.118   1.00 52.75  ? 404 TRP   A CB    1 
ATOM   3214 C CG    . TRP   A 1 412 ? -32.066 -105.202 1.279   1.00 56.53  ? 404 TRP   A CG    1 
ATOM   3215 C CD1   . TRP   A 1 412 ? -31.735 -103.896 1.069   1.00 58.61  ? 404 TRP   A CD1   1 
ATOM   3216 C CD2   . TRP   A 1 412 ? -33.270 -105.437 0.514   1.00 58.79  ? 404 TRP   A CD2   1 
ATOM   3217 N NE1   . TRP   A 1 412 ? -32.646 -103.300 0.237   1.00 59.73  ? 404 TRP   A NE1   1 
ATOM   3218 C CE2   . TRP   A 1 412 ? -33.599 -104.218 -0.119  1.00 59.88  ? 404 TRP   A CE2   1 
ATOM   3219 C CE3   . TRP   A 1 412 ? -34.098 -106.546 0.305   1.00 59.11  ? 404 TRP   A CE3   1 
ATOM   3220 C CZ2   . TRP   A 1 412 ? -34.717 -104.083 -0.941  1.00 59.63  ? 404 TRP   A CZ2   1 
ATOM   3221 C CZ3   . TRP   A 1 412 ? -35.203 -106.412 -0.509  1.00 59.37  ? 404 TRP   A CZ3   1 
ATOM   3222 C CH2   . TRP   A 1 412 ? -35.508 -105.196 -1.121  1.00 59.59  ? 404 TRP   A CH2   1 
ATOM   3223 N N     . GLN   A 1 413 ? -30.822 -108.742 3.728   1.00 48.51  ? 405 GLN   A N     1 
ATOM   3224 C CA    . GLN   A 1 413 ? -30.573 -110.165 3.567   1.00 49.08  ? 405 GLN   A CA    1 
ATOM   3225 C C     . GLN   A 1 413 ? -31.463 -110.965 4.513   1.00 51.14  ? 405 GLN   A C     1 
ATOM   3226 O O     . GLN   A 1 413 ? -32.158 -111.884 4.083   1.00 51.34  ? 405 GLN   A O     1 
ATOM   3227 C CB    . GLN   A 1 413 ? -29.088 -110.448 3.804   1.00 48.77  ? 405 GLN   A CB    1 
ATOM   3228 C CG    . GLN   A 1 413 ? -28.642 -111.852 3.409   1.00 48.87  ? 405 GLN   A CG    1 
ATOM   3229 C CD    . GLN   A 1 413 ? -28.947 -112.909 4.448   1.00 48.97  ? 405 GLN   A CD    1 
ATOM   3230 O OE1   . GLN   A 1 413 ? -29.502 -112.631 5.516   1.00 49.13  ? 405 GLN   A OE1   1 
ATOM   3231 N NE2   . GLN   A 1 413 ? -28.572 -114.142 4.145   1.00 49.82  ? 405 GLN   A NE2   1 
ATOM   3232 N N     . PHE   A 1 414 ? -31.413 -110.615 5.804   1.00 53.17  ? 406 PHE   A N     1 
ATOM   3233 C CA    . PHE   A 1 414 ? -32.209 -111.283 6.821   1.00 53.93  ? 406 PHE   A CA    1 
ATOM   3234 C C     . PHE   A 1 414 ? -33.694 -111.073 6.533   1.00 53.80  ? 406 PHE   A C     1 
ATOM   3235 O O     . PHE   A 1 414 ? -34.457 -112.035 6.525   1.00 55.90  ? 406 PHE   A O     1 
ATOM   3236 C CB    . PHE   A 1 414 ? -31.825 -110.785 8.219   1.00 55.58  ? 406 PHE   A CB    1 
ATOM   3237 C CG    . PHE   A 1 414 ? -32.870 -111.043 9.297   1.00 57.60  ? 406 PHE   A CG    1 
ATOM   3238 C CD1   . PHE   A 1 414 ? -33.854 -110.096 9.571   1.00 58.81  ? 406 PHE   A CD1   1 
ATOM   3239 C CD2   . PHE   A 1 414 ? -32.872 -112.226 10.031  1.00 57.28  ? 406 PHE   A CD2   1 
ATOM   3240 C CE1   . PHE   A 1 414 ? -34.811 -110.327 10.548  1.00 58.53  ? 406 PHE   A CE1   1 
ATOM   3241 C CE2   . PHE   A 1 414 ? -33.832 -112.452 11.008  1.00 57.50  ? 406 PHE   A CE2   1 
ATOM   3242 C CZ    . PHE   A 1 414 ? -34.798 -111.503 11.265  1.00 58.48  ? 406 PHE   A CZ    1 
ATOM   3243 N N     . GLU   A 1 415 ? -34.094 -109.817 6.299   1.00 53.00  ? 407 GLU   A N     1 
ATOM   3244 C CA    . GLU   A 1 415 ? -35.499 -109.484 6.125   1.00 52.71  ? 407 GLU   A CA    1 
ATOM   3245 C C     . GLU   A 1 415 ? -36.081 -110.168 4.887   1.00 52.72  ? 407 GLU   A C     1 
ATOM   3246 O O     . GLU   A 1 415 ? -37.187 -110.696 4.959   1.00 54.86  ? 407 GLU   A O     1 
ATOM   3247 C CB    . GLU   A 1 415 ? -35.751 -107.978 6.040   1.00 52.93  ? 407 GLU   A CB    1 
ATOM   3248 C CG    . GLU   A 1 415 ? -35.733 -107.275 7.395   1.00 53.76  ? 407 GLU   A CG    1 
ATOM   3249 C CD    . GLU   A 1 415 ? -36.176 -105.822 7.338   1.00 55.58  ? 407 GLU   A CD    1 
ATOM   3250 O OE1   . GLU   A 1 415 ? -37.241 -105.551 6.739   1.00 56.05  ? 407 GLU   A OE1   1 
ATOM   3251 O OE2   . GLU   A 1 415 ? -35.468 -104.960 7.902   1.00 55.81  ? 407 GLU   A OE2   1 
ATOM   3252 N N     . GLU   A 1 416 ? -35.347 -110.162 3.764   1.00 52.14  ? 408 GLU   A N     1 
ATOM   3253 C CA    . GLU   A 1 416 ? -35.934 -110.504 2.474   1.00 51.73  ? 408 GLU   A CA    1 
ATOM   3254 C C     . GLU   A 1 416 ? -35.171 -111.637 1.786   1.00 51.53  ? 408 GLU   A C     1 
ATOM   3255 O O     . GLU   A 1 416 ? -35.712 -112.726 1.614   1.00 52.83  ? 408 GLU   A O     1 
ATOM   3256 C CB    . GLU   A 1 416 ? -35.987 -109.285 1.552   1.00 52.18  ? 408 GLU   A CB    1 
ATOM   3257 C CG    . GLU   A 1 416 ? -36.662 -108.063 2.172   1.00 53.85  ? 408 GLU   A CG    1 
ATOM   3258 C CD    . GLU   A 1 416 ? -38.165 -108.167 2.353   1.00 55.49  ? 408 GLU   A CD    1 
ATOM   3259 O OE1   . GLU   A 1 416 ? -38.610 -108.962 3.207   1.00 57.31  ? 408 GLU   A OE1   1 
ATOM   3260 O OE2   . GLU   A 1 416 ? -38.893 -107.445 1.638   1.00 54.95  ? 408 GLU   A OE2   1 
ATOM   3261 N N     . TRP   A 1 417 ? -33.924 -111.373 1.377   1.00 50.31  ? 409 TRP   A N     1 
ATOM   3262 C CA    . TRP   A 1 417 ? -33.238 -112.230 0.419   1.00 50.40  ? 409 TRP   A CA    1 
ATOM   3263 C C     . TRP   A 1 417 ? -33.090 -113.656 0.945   1.00 49.71  ? 409 TRP   A C     1 
ATOM   3264 O O     . TRP   A 1 417 ? -33.225 -114.609 0.180   1.00 51.24  ? 409 TRP   A O     1 
ATOM   3265 C CB    . TRP   A 1 417 ? -31.862 -111.659 0.047   1.00 50.99  ? 409 TRP   A CB    1 
ATOM   3266 C CG    . TRP   A 1 417 ? -31.904 -110.351 -0.698  1.00 51.81  ? 409 TRP   A CG    1 
ATOM   3267 C CD1   . TRP   A 1 417 ? -32.896 -109.884 -1.510  1.00 52.41  ? 409 TRP   A CD1   1 
ATOM   3268 C CD2   . TRP   A 1 417 ? -30.881 -109.333 -0.690  1.00 53.11  ? 409 TRP   A CD2   1 
ATOM   3269 N NE1   . TRP   A 1 417 ? -32.567 -108.650 -2.004  1.00 52.99  ? 409 TRP   A NE1   1 
ATOM   3270 C CE2   . TRP   A 1 417 ? -31.338 -108.285 -1.520  1.00 53.58  ? 409 TRP   A CE2   1 
ATOM   3271 C CE3   . TRP   A 1 417 ? -29.634 -109.207 -0.067  1.00 52.97  ? 409 TRP   A CE3   1 
ATOM   3272 C CZ2   . TRP   A 1 417 ? -30.588 -107.132 -1.738  1.00 53.66  ? 409 TRP   A CZ2   1 
ATOM   3273 C CZ3   . TRP   A 1 417 ? -28.894 -108.066 -0.285  1.00 53.49  ? 409 TRP   A CZ3   1 
ATOM   3274 C CH2   . TRP   A 1 417 ? -29.367 -107.044 -1.108  1.00 53.48  ? 409 TRP   A CH2   1 
ATOM   3275 N N     . GLY   A 1 418 ? -32.783 -113.794 2.239   1.00 48.73  ? 410 GLY   A N     1 
ATOM   3276 C CA    . GLY   A 1 418 ? -32.492 -115.094 2.819   1.00 48.46  ? 410 GLY   A CA    1 
ATOM   3277 C C     . GLY   A 1 418 ? -31.076 -115.544 2.468   1.00 48.46  ? 410 GLY   A C     1 
ATOM   3278 O O     . GLY   A 1 418 ? -30.301 -114.780 1.897   1.00 47.46  ? 410 GLY   A O     1 
ATOM   3279 N N     . SER   A 1 419 ? -30.762 -116.805 2.788   1.00 49.33  ? 411 SER   A N     1 
ATOM   3280 C CA    . SER   A 1 419 ? -29.399 -117.311 2.710   1.00 49.60  ? 411 SER   A CA    1 
ATOM   3281 C C     . SER   A 1 419 ? -28.971 -117.559 1.264   1.00 49.07  ? 411 SER   A C     1 
ATOM   3282 O O     . SER   A 1 419 ? -27.850 -118.007 1.030   1.00 47.88  ? 411 SER   A O     1 
ATOM   3283 C CB    . SER   A 1 419 ? -29.237 -118.566 3.533   1.00 50.02  ? 411 SER   A CB    1 
ATOM   3284 O OG    . SER   A 1 419 ? -29.848 -119.680 2.896   1.00 50.42  ? 411 SER   A OG    1 
ATOM   3285 N N     . GLN   A 1 420 ? -29.865 -117.292 0.302   1.00 49.98  ? 412 GLN   A N     1 
ATOM   3286 C CA    . GLN   A 1 420 ? -29.501 -117.326 -1.106  1.00 50.98  ? 412 GLN   A CA    1 
ATOM   3287 C C     . GLN   A 1 420 ? -28.365 -116.335 -1.357  1.00 51.53  ? 412 GLN   A C     1 
ATOM   3288 O O     . GLN   A 1 420 ? -27.442 -116.626 -2.117  1.00 51.19  ? 412 GLN   A O     1 
ATOM   3289 C CB    . GLN   A 1 420 ? -30.696 -116.997 -2.000  1.00 51.20  ? 412 GLN   A CB    1 
ATOM   3290 C CG    . GLN   A 1 420 ? -30.437 -117.249 -3.482  1.00 51.68  ? 412 GLN   A CG    1 
ATOM   3291 C CD    . GLN   A 1 420 ? -31.561 -116.776 -4.377  1.00 52.73  ? 412 GLN   A CD    1 
ATOM   3292 O OE1   . GLN   A 1 420 ? -32.562 -116.212 -3.921  1.00 53.29  ? 412 GLN   A OE1   1 
ATOM   3293 N NE2   . GLN   A 1 420 ? -31.400 -116.998 -5.673  1.00 53.51  ? 412 GLN   A NE2   1 
ATOM   3294 N N     . VAL   A 1 421 ? -28.458 -115.163 -0.712  1.00 51.00  ? 413 VAL   A N     1 
ATOM   3295 C CA    . VAL   A 1 421 ? -27.405 -114.160 -0.733  1.00 49.81  ? 413 VAL   A CA    1 
ATOM   3296 C C     . VAL   A 1 421 ? -26.467 -114.393 0.450   1.00 47.39  ? 413 VAL   A C     1 
ATOM   3297 O O     . VAL   A 1 421 ? -26.922 -114.669 1.558   1.00 45.59  ? 413 VAL   A O     1 
ATOM   3298 C CB    . VAL   A 1 421 ? -28.002 -112.740 -0.681  1.00 50.76  ? 413 VAL   A CB    1 
ATOM   3299 C CG1   . VAL   A 1 421 ? -26.918 -111.668 -0.648  1.00 51.51  ? 413 VAL   A CG1   1 
ATOM   3300 C CG2   . VAL   A 1 421 ? -28.969 -112.483 -1.830  1.00 50.95  ? 413 VAL   A CG2   1 
ATOM   3301 N N     . THR   A 1 422 ? -25.158 -114.261 0.197   1.00 45.90  ? 414 THR   A N     1 
ATOM   3302 C CA    . THR   A 1 422 ? -24.147 -114.241 1.244   1.00 44.45  ? 414 THR   A CA    1 
ATOM   3303 C C     . THR   A 1 422 ? -23.448 -112.883 1.229   1.00 43.73  ? 414 THR   A C     1 
ATOM   3304 O O     . THR   A 1 422 ? -22.564 -112.647 0.405   1.00 44.07  ? 414 THR   A O     1 
ATOM   3305 C CB    . THR   A 1 422 ? -23.150 -115.379 1.030   1.00 42.95  ? 414 THR   A CB    1 
ATOM   3306 O OG1   . THR   A 1 422 ? -23.931 -116.565 1.110   1.00 42.43  ? 414 THR   A OG1   1 
ATOM   3307 C CG2   . THR   A 1 422 ? -22.051 -115.398 2.078   1.00 42.29  ? 414 THR   A CG2   1 
ATOM   3308 N N     . VAL   A 1 423 ? -23.846 -111.999 2.153   1.00 41.35  ? 415 VAL   A N     1 
ATOM   3309 C CA    . VAL   A 1 423 ? -23.197 -110.706 2.307   1.00 39.07  ? 415 VAL   A CA    1 
ATOM   3310 C C     . VAL   A 1 423 ? -21.772 -110.949 2.799   1.00 37.28  ? 415 VAL   A C     1 
ATOM   3311 O O     . VAL   A 1 423 ? -21.574 -111.526 3.863   1.00 37.87  ? 415 VAL   A O     1 
ATOM   3312 C CB    . VAL   A 1 423 ? -23.944 -109.758 3.266   1.00 39.38  ? 415 VAL   A CB    1 
ATOM   3313 C CG1   . VAL   A 1 423 ? -23.269 -108.394 3.351   1.00 39.50  ? 415 VAL   A CG1   1 
ATOM   3314 C CG2   . VAL   A 1 423 ? -25.413 -109.591 2.890   1.00 39.75  ? 415 VAL   A CG2   1 
ATOM   3315 N N     . VAL   A 1 424 ? -20.792 -110.528 1.994   1.00 36.56  ? 416 VAL   A N     1 
ATOM   3316 C CA    . VAL   A 1 424 ? -19.398 -110.507 2.405   1.00 35.92  ? 416 VAL   A CA    1 
ATOM   3317 C C     . VAL   A 1 424 ? -19.007 -109.050 2.630   1.00 35.22  ? 416 VAL   A C     1 
ATOM   3318 O O     . VAL   A 1 424 ? -19.143 -108.224 1.730   1.00 35.06  ? 416 VAL   A O     1 
ATOM   3319 C CB    . VAL   A 1 424 ? -18.470 -111.176 1.374   1.00 36.47  ? 416 VAL   A CB    1 
ATOM   3320 C CG1   . VAL   A 1 424 ? -17.006 -111.112 1.793   1.00 36.12  ? 416 VAL   A CG1   1 
ATOM   3321 C CG2   . VAL   A 1 424 ? -18.882 -112.616 1.096   1.00 37.37  ? 416 VAL   A CG2   1 
ATOM   3322 N N     . SER   A 1 425 ? -18.544 -108.746 3.847   1.00 34.82  ? 417 SER   A N     1 
ATOM   3323 C CA    . SER   A 1 425 ? -18.063 -107.418 4.189   1.00 33.96  ? 417 SER   A CA    1 
ATOM   3324 C C     . SER   A 1 425 ? -16.548 -107.387 4.011   1.00 33.46  ? 417 SER   A C     1 
ATOM   3325 O O     . SER   A 1 425 ? -15.809 -107.704 4.939   1.00 31.90  ? 417 SER   A O     1 
ATOM   3326 C CB    . SER   A 1 425 ? -18.467 -107.040 5.590   1.00 33.61  ? 417 SER   A CB    1 
ATOM   3327 O OG    . SER   A 1 425 ? -17.977 -105.752 5.931   1.00 33.95  ? 417 SER   A OG    1 
ATOM   3328 N N     . SER   A 1 426 ? -16.097 -107.020 2.804   1.00 33.67  ? 418 SER   A N     1 
ATOM   3329 C CA    . SER   A 1 426 ? -14.696 -107.172 2.448   1.00 33.44  ? 418 SER   A CA    1 
ATOM   3330 C C     . SER   A 1 426 ? -14.347 -106.343 1.214   1.00 33.58  ? 418 SER   A C     1 
ATOM   3331 O O     . SER   A 1 426 ? -15.222 -105.941 0.447   1.00 33.53  ? 418 SER   A O     1 
ATOM   3332 C CB    . SER   A 1 426 ? -14.368 -108.629 2.219   1.00 33.25  ? 418 SER   A CB    1 
ATOM   3333 O OG    . SER   A 1 426 ? -12.975 -108.816 2.012   1.00 33.37  ? 418 SER   A OG    1 
ATOM   3334 N N     . ASP   A 1 427 ? -13.042 -106.093 1.051   1.00 32.62  ? 419 ASP   A N     1 
ATOM   3335 C CA    . ASP   A 1 427 ? -12.485 -105.678 -0.221  1.00 32.43  ? 419 ASP   A CA    1 
ATOM   3336 C C     . ASP   A 1 427 ? -12.387 -106.915 -1.108  1.00 32.61  ? 419 ASP   A C     1 
ATOM   3337 O O     . ASP   A 1 427 ? -12.020 -107.987 -0.633  1.00 33.41  ? 419 ASP   A O     1 
ATOM   3338 C CB    . ASP   A 1 427 ? -11.132 -105.011 -0.039  1.00 32.10  ? 419 ASP   A CB    1 
ATOM   3339 C CG    . ASP   A 1 427 ? -10.633 -104.231 -1.247  1.00 31.69  ? 419 ASP   A CG    1 
ATOM   3340 O OD1   . ASP   A 1 427 ? -10.476 -104.845 -2.322  1.00 31.67  ? 419 ASP   A OD1   1 
ATOM   3341 O OD2   . ASP   A 1 427 ? -10.421 -103.010 -1.108  1.00 31.34  ? 419 ASP   A OD2   1 
ATOM   3342 N N     . MET   A 1 428 ? -12.703 -106.758 -2.398  1.00 32.65  ? 420 MET   A N     1 
ATOM   3343 C CA    . MET   A 1 428 ? -12.717 -107.882 -3.320  1.00 33.12  ? 420 MET   A CA    1 
ATOM   3344 C C     . MET   A 1 428 ? -11.293 -108.341 -3.630  1.00 34.90  ? 420 MET   A C     1 
ATOM   3345 O O     . MET   A 1 428 ? -11.096 -109.468 -4.076  1.00 36.38  ? 420 MET   A O     1 
ATOM   3346 C CB    . MET   A 1 428 ? -13.426 -107.519 -4.628  1.00 32.36  ? 420 MET   A CB    1 
ATOM   3347 C CG    . MET   A 1 428 ? -12.673 -106.530 -5.500  1.00 31.79  ? 420 MET   A CG    1 
ATOM   3348 S SD    . MET   A 1 428 ? -13.622 -106.083 -6.966  1.00 30.28  ? 420 MET   A SD    1 
ATOM   3349 C CE    . MET   A 1 428 ? -14.899 -105.049 -6.236  1.00 30.04  ? 420 MET   A CE    1 
ATOM   3350 N N     . ARG   A 1 429 ? -10.311 -107.459 -3.408  1.00 36.04  ? 421 ARG   A N     1 
ATOM   3351 C CA    . ARG   A 1 429 ? -8.914  -107.769 -3.666  1.00 36.91  ? 421 ARG   A CA    1 
ATOM   3352 C C     . ARG   A 1 429 ? -8.321  -108.579 -2.517  1.00 38.77  ? 421 ARG   A C     1 
ATOM   3353 O O     . ARG   A 1 429 ? -7.276  -109.203 -2.683  1.00 38.71  ? 421 ARG   A O     1 
ATOM   3354 C CB    . ARG   A 1 429 ? -8.093  -106.486 -3.825  1.00 36.43  ? 421 ARG   A CB    1 
ATOM   3355 C CG    . ARG   A 1 429 ? -8.494  -105.609 -5.003  1.00 35.93  ? 421 ARG   A CG    1 
ATOM   3356 C CD    . ARG   A 1 429 ? -7.812  -104.254 -4.930  1.00 35.20  ? 421 ARG   A CD    1 
ATOM   3357 N NE    . ARG   A 1 429 ? -8.320  -103.456 -3.809  1.00 34.33  ? 421 ARG   A NE    1 
ATOM   3358 C CZ    . ARG   A 1 429 ? -7.854  -102.270 -3.427  1.00 33.76  ? 421 ARG   A CZ    1 
ATOM   3359 N NH1   . ARG   A 1 429 ? -6.852  -101.705 -4.076  1.00 33.84  ? 421 ARG   A NH1   1 
ATOM   3360 N NH2   . ARG   A 1 429 ? -8.390  -101.649 -2.389  1.00 33.34  ? 421 ARG   A NH2   1 
ATOM   3361 N N     . GLU   A 1 430 ? -8.978  -108.538 -1.352  1.00 41.80  ? 422 GLU   A N     1 
ATOM   3362 C CA    . GLU   A 1 430 ? -8.495  -109.211 -0.156  1.00 44.76  ? 422 GLU   A CA    1 
ATOM   3363 C C     . GLU   A 1 430 ? -9.239  -110.528 0.057   1.00 44.06  ? 422 GLU   A C     1 
ATOM   3364 O O     . GLU   A 1 430 ? -8.620  -111.552 0.334   1.00 43.73  ? 422 GLU   A O     1 
ATOM   3365 C CB    . GLU   A 1 430 ? -8.670  -108.287 1.049   1.00 47.94  ? 422 GLU   A CB    1 
ATOM   3366 C CG    . GLU   A 1 430 ? -7.727  -107.087 1.037   1.00 50.74  ? 422 GLU   A CG    1 
ATOM   3367 C CD    . GLU   A 1 430 ? -6.273  -107.431 1.317   1.00 53.85  ? 422 GLU   A CD    1 
ATOM   3368 O OE1   . GLU   A 1 430 ? -5.641  -108.120 0.487   1.00 55.13  ? 422 GLU   A OE1   1 
ATOM   3369 O OE2   . GLU   A 1 430 ? -5.772  -107.014 2.383   1.00 58.14  ? 422 GLU   A OE2   1 
ATOM   3370 N N     . TRP   A 1 431 ? -10.568 -110.475 -0.076  1.00 43.90  ? 423 TRP   A N     1 
ATOM   3371 C CA    . TRP   A 1 431 ? -11.455 -111.586 0.228   1.00 44.64  ? 423 TRP   A CA    1 
ATOM   3372 C C     . TRP   A 1 431 ? -10.903 -112.916 -0.281  1.00 44.99  ? 423 TRP   A C     1 
ATOM   3373 O O     . TRP   A 1 431 ? -10.450 -113.010 -1.420  1.00 44.05  ? 423 TRP   A O     1 
ATOM   3374 C CB    . TRP   A 1 431 ? -12.832 -111.314 -0.389  1.00 45.76  ? 423 TRP   A CB    1 
ATOM   3375 C CG    . TRP   A 1 431 ? -13.865 -112.364 -0.083  1.00 47.03  ? 423 TRP   A CG    1 
ATOM   3376 C CD1   . TRP   A 1 431 ? -14.068 -113.008 1.101   1.00 47.55  ? 423 TRP   A CD1   1 
ATOM   3377 C CD2   . TRP   A 1 431 ? -14.848 -112.888 -0.999  1.00 48.74  ? 423 TRP   A CD2   1 
ATOM   3378 N NE1   . TRP   A 1 431 ? -15.109 -113.889 0.990   1.00 48.08  ? 423 TRP   A NE1   1 
ATOM   3379 C CE2   . TRP   A 1 431 ? -15.607 -113.841 -0.285  1.00 48.88  ? 423 TRP   A CE2   1 
ATOM   3380 C CE3   . TRP   A 1 431 ? -15.159 -112.646 -2.342  1.00 49.79  ? 423 TRP   A CE3   1 
ATOM   3381 C CZ2   . TRP   A 1 431 ? -16.653 -114.548 -0.876  1.00 50.19  ? 423 TRP   A CZ2   1 
ATOM   3382 C CZ3   . TRP   A 1 431 ? -16.195 -113.344 -2.923  1.00 49.57  ? 423 TRP   A CZ3   1 
ATOM   3383 C CH2   . TRP   A 1 431 ? -16.931 -114.281 -2.198  1.00 49.96  ? 423 TRP   A CH2   1 
ATOM   3384 N N     . VAL   A 1 432 ? -10.964 -113.938 0.584   1.00 45.60  ? 424 VAL   A N     1 
ATOM   3385 C CA    . VAL   A 1 432 ? -10.737 -115.320 0.191   1.00 44.58  ? 424 VAL   A CA    1 
ATOM   3386 C C     . VAL   A 1 432 ? -12.104 -115.984 0.048   1.00 44.72  ? 424 VAL   A C     1 
ATOM   3387 O O     . VAL   A 1 432 ? -12.825 -116.137 1.031   1.00 42.94  ? 424 VAL   A O     1 
ATOM   3388 C CB    . VAL   A 1 432 ? -9.856  -116.096 1.188   1.00 43.77  ? 424 VAL   A CB    1 
ATOM   3389 C CG1   . VAL   A 1 432 ? -9.525  -117.493 0.675   1.00 43.17  ? 424 VAL   A CG1   1 
ATOM   3390 C CG2   . VAL   A 1 432 ? -8.577  -115.341 1.530   1.00 43.79  ? 424 VAL   A CG2   1 
ATOM   3391 N N     . ALA   A 1 433 ? -12.447 -116.372 -1.184  1.00 45.96  ? 425 ALA   A N     1 
ATOM   3392 C CA    . ALA   A 1 433 ? -13.764 -116.906 -1.484  1.00 46.81  ? 425 ALA   A CA    1 
ATOM   3393 C C     . ALA   A 1 433 ? -13.827 -118.380 -1.094  1.00 47.79  ? 425 ALA   A C     1 
ATOM   3394 O O     . ALA   A 1 433 ? -12.818 -119.079 -1.157  1.00 48.33  ? 425 ALA   A O     1 
ATOM   3395 C CB    . ALA   A 1 433 ? -14.072 -116.708 -2.952  1.00 46.94  ? 425 ALA   A CB    1 
ATOM   3396 N N     . PRO   A 1 434 ? -15.009 -118.894 -0.675  1.00 48.80  ? 426 PRO   A N     1 
ATOM   3397 C CA    . PRO   A 1 434 ? -15.179 -120.326 -0.416  1.00 48.36  ? 426 PRO   A CA    1 
ATOM   3398 C C     . PRO   A 1 434 ? -15.105 -121.161 -1.694  1.00 48.69  ? 426 PRO   A C     1 
ATOM   3399 O O     . PRO   A 1 434 ? -14.459 -122.205 -1.719  1.00 50.01  ? 426 PRO   A O     1 
ATOM   3400 C CB    . PRO   A 1 434 ? -16.560 -120.406 0.262   1.00 48.21  ? 426 PRO   A CB    1 
ATOM   3401 C CG    . PRO   A 1 434 ? -17.301 -119.188 -0.242  1.00 48.28  ? 426 PRO   A CG    1 
ATOM   3402 C CD    . PRO   A 1 434 ? -16.238 -118.121 -0.428  1.00 48.55  ? 426 PRO   A CD    1 
ATOM   3403 N N     . GLU   A 1 435 ? -15.764 -120.669 -2.751  1.00 48.47  ? 427 GLU   A N     1 
ATOM   3404 C CA    . GLU   A 1 435 ? -15.809 -121.317 -4.053  1.00 46.10  ? 427 GLU   A CA    1 
ATOM   3405 C C     . GLU   A 1 435 ? -15.606 -120.257 -5.134  1.00 45.85  ? 427 GLU   A C     1 
ATOM   3406 O O     . GLU   A 1 435 ? -15.730 -119.065 -4.860  1.00 45.89  ? 427 GLU   A O     1 
ATOM   3407 C CB    . GLU   A 1 435 ? -17.157 -122.016 -4.232  1.00 45.28  ? 427 GLU   A CB    1 
ATOM   3408 C CG    . GLU   A 1 435 ? -18.341 -121.121 -3.874  1.00 45.76  ? 427 GLU   A CG    1 
ATOM   3409 C CD    . GLU   A 1 435 ? -19.717 -121.677 -4.182  1.00 46.80  ? 427 GLU   A CD    1 
ATOM   3410 O OE1   . GLU   A 1 435 ? -19.821 -122.696 -4.894  1.00 49.14  ? 427 GLU   A OE1   1 
ATOM   3411 O OE2   . GLU   A 1 435 ? -20.696 -121.080 -3.688  1.00 47.14  ? 427 GLU   A OE2   1 
ATOM   3412 N N     . LYS   A 1 436 ? -15.306 -120.696 -6.363  1.00 44.37  ? 428 LYS   A N     1 
ATOM   3413 C CA    . LYS   A 1 436 ? -15.129 -119.780 -7.479  1.00 43.19  ? 428 LYS   A CA    1 
ATOM   3414 C C     . LYS   A 1 436 ? -16.488 -119.361 -8.036  1.00 42.11  ? 428 LYS   A C     1 
ATOM   3415 O O     . LYS   A 1 436 ? -17.504 -120.005 -7.774  1.00 40.83  ? 428 LYS   A O     1 
ATOM   3416 C CB    . LYS   A 1 436 ? -14.285 -120.398 -8.597  1.00 42.62  ? 428 LYS   A CB    1 
ATOM   3417 C CG    . LYS   A 1 436 ? -12.842 -120.701 -8.233  1.00 42.16  ? 428 LYS   A CG    1 
ATOM   3418 C CD    . LYS   A 1 436 ? -11.960 -120.854 -9.466  1.00 42.46  ? 428 LYS   A CD    1 
ATOM   3419 C CE    . LYS   A 1 436 ? -10.668 -121.551 -9.194  1.00 43.00  ? 428 LYS   A CE    1 
ATOM   3420 N NZ    . LYS   A 1 436 ? -9.821  -120.809 -8.259  1.00 43.98  ? 428 LYS   A NZ    1 
ATOM   3421 N N     . ALA   A 1 437 ? -16.482 -118.274 -8.818  1.00 41.07  ? 429 ALA   A N     1 
ATOM   3422 C CA    . ALA   A 1 437 ? -17.694 -117.729 -9.409  1.00 40.86  ? 429 ALA   A CA    1 
ATOM   3423 C C     . ALA   A 1 437 ? -17.771 -118.091 -10.888 1.00 40.16  ? 429 ALA   A C     1 
ATOM   3424 O O     . ALA   A 1 437 ? -16.757 -118.119 -11.583 1.00 39.70  ? 429 ALA   A O     1 
ATOM   3425 C CB    . ALA   A 1 437 ? -17.731 -116.228 -9.225  1.00 40.57  ? 429 ALA   A CB    1 
ATOM   3426 N N     . ASP   A 1 438 ? -18.997 -118.363 -11.348 1.00 40.06  ? 430 ASP   A N     1 
ATOM   3427 C CA    . ASP   A 1 438 ? -19.300 -118.450 -12.767 1.00 41.08  ? 430 ASP   A CA    1 
ATOM   3428 C C     . ASP   A 1 438 ? -19.307 -117.045 -13.362 1.00 39.67  ? 430 ASP   A C     1 
ATOM   3429 O O     . ASP   A 1 438 ? -18.828 -116.838 -14.475 1.00 40.38  ? 430 ASP   A O     1 
ATOM   3430 C CB    . ASP   A 1 438 ? -20.646 -119.119 -13.002 1.00 42.46  ? 430 ASP   A CB    1 
ATOM   3431 C CG    . ASP   A 1 438 ? -20.701 -120.610 -12.702 1.00 42.93  ? 430 ASP   A CG    1 
ATOM   3432 O OD1   . ASP   A 1 438 ? -20.170 -121.389 -13.521 1.00 42.80  ? 430 ASP   A OD1   1 
ATOM   3433 O OD2   . ASP   A 1 438 ? -21.266 -120.981 -11.648 1.00 41.54  ? 430 ASP   A OD2   1 
ATOM   3434 N N     . ILE   A 1 439 ? -19.873 -116.100 -12.600 1.00 38.67  ? 431 ILE   A N     1 
ATOM   3435 C CA    . ILE   A 1 439 ? -20.078 -114.733 -13.045 1.00 37.17  ? 431 ILE   A CA    1 
ATOM   3436 C C     . ILE   A 1 439 ? -19.698 -113.783 -11.912 1.00 36.48  ? 431 ILE   A C     1 
ATOM   3437 O O     . ILE   A 1 439 ? -20.230 -113.893 -10.808 1.00 35.16  ? 431 ILE   A O     1 
ATOM   3438 C CB    . ILE   A 1 439 ? -21.542 -114.514 -13.475 1.00 37.66  ? 431 ILE   A CB    1 
ATOM   3439 C CG1   . ILE   A 1 439 ? -22.013 -115.571 -14.482 1.00 38.28  ? 431 ILE   A CG1   1 
ATOM   3440 C CG2   . ILE   A 1 439 ? -21.747 -113.093 -14.006 1.00 37.53  ? 431 ILE   A CG2   1 
ATOM   3441 C CD1   . ILE   A 1 439 ? -23.491 -115.497 -14.822 1.00 38.35  ? 431 ILE   A CD1   1 
ATOM   3442 N N     . ILE   A 1 440 ? -18.784 -112.849 -12.205 1.00 35.47  ? 432 ILE   A N     1 
ATOM   3443 C CA    . ILE   A 1 440 ? -18.583 -111.678 -11.365 1.00 33.01  ? 432 ILE   A CA    1 
ATOM   3444 C C     . ILE   A 1 440 ? -19.279 -110.499 -12.038 1.00 31.88  ? 432 ILE   A C     1 
ATOM   3445 O O     . ILE   A 1 440 ? -19.174 -110.321 -13.249 1.00 31.91  ? 432 ILE   A O     1 
ATOM   3446 C CB    . ILE   A 1 440 ? -17.092 -111.401 -11.084 1.00 32.80  ? 432 ILE   A CB    1 
ATOM   3447 C CG1   . ILE   A 1 440 ? -16.267 -111.251 -12.371 1.00 33.16  ? 432 ILE   A CG1   1 
ATOM   3448 C CG2   . ILE   A 1 440 ? -16.520 -112.469 -10.150 1.00 33.04  ? 432 ILE   A CG2   1 
ATOM   3449 C CD1   . ILE   A 1 440 ? -14.760 -111.280 -12.166 1.00 33.39  ? 432 ILE   A CD1   1 
ATOM   3450 N N     . VAL   A 1 441 ? -20.009 -109.724 -11.232 1.00 30.74  ? 433 VAL   A N     1 
ATOM   3451 C CA    . VAL   A 1 441 ? -20.796 -108.596 -11.702 1.00 30.11  ? 433 VAL   A CA    1 
ATOM   3452 C C     . VAL   A 1 441 ? -20.356 -107.357 -10.926 1.00 29.99  ? 433 VAL   A C     1 
ATOM   3453 O O     . VAL   A 1 441 ? -20.390 -107.368 -9.696  1.00 28.64  ? 433 VAL   A O     1 
ATOM   3454 C CB    . VAL   A 1 441 ? -22.292 -108.894 -11.485 1.00 29.94  ? 433 VAL   A CB    1 
ATOM   3455 C CG1   . VAL   A 1 441 ? -23.181 -107.754 -11.965 1.00 30.21  ? 433 VAL   A CG1   1 
ATOM   3456 C CG2   . VAL   A 1 441 ? -22.713 -110.205 -12.133 1.00 30.00  ? 433 VAL   A CG2   1 
ATOM   3457 N N     . SER   A 1 442 ? -19.949 -106.295 -11.637 1.00 29.69  ? 434 SER   A N     1 
ATOM   3458 C CA    . SER   A 1 442 ? -19.440 -105.102 -10.976 1.00 29.37  ? 434 SER   A CA    1 
ATOM   3459 C C     . SER   A 1 442 ? -19.993 -103.832 -11.617 1.00 28.86  ? 434 SER   A C     1 
ATOM   3460 O O     . SER   A 1 442 ? -20.560 -103.865 -12.707 1.00 29.58  ? 434 SER   A O     1 
ATOM   3461 C CB    . SER   A 1 442 ? -17.928 -105.099 -10.935 1.00 29.33  ? 434 SER   A CB    1 
ATOM   3462 O OG    . SER   A 1 442 ? -17.364 -105.148 -12.237 1.00 29.41  ? 434 SER   A OG    1 
ATOM   3463 N N     . GLU   A 1 443 ? -19.798 -102.719 -10.899 1.00 28.73  ? 435 GLU   A N     1 
ATOM   3464 C CA    . GLU   A 1 443 ? -20.412 -101.431 -11.177 1.00 28.06  ? 435 GLU   A CA    1 
ATOM   3465 C C     . GLU   A 1 443 ? -19.401 -100.344 -10.818 1.00 27.25  ? 435 GLU   A C     1 
ATOM   3466 O O     . GLU   A 1 443 ? -19.752 -99.322  -10.240 1.00 27.47  ? 435 GLU   A O     1 
ATOM   3467 C CB    . GLU   A 1 443 ? -21.673 -101.444 -10.310 1.00 29.17  ? 435 GLU   A CB    1 
ATOM   3468 C CG    . GLU   A 1 443 ? -22.586 -100.224 -10.394 1.00 29.38  ? 435 GLU   A CG    1 
ATOM   3469 C CD    . GLU   A 1 443 ? -23.773 -100.328 -9.448  1.00 28.99  ? 435 GLU   A CD    1 
ATOM   3470 O OE1   . GLU   A 1 443 ? -23.841 -101.314 -8.680  1.00 28.09  ? 435 GLU   A OE1   1 
ATOM   3471 O OE2   . GLU   A 1 443 ? -24.638 -99.427  -9.477  1.00 28.83  ? 435 GLU   A OE2   1 
ATOM   3472 N N     . LEU   A 1 444 ? -18.133 -100.587 -11.171 1.00 26.72  ? 436 LEU   A N     1 
ATOM   3473 C CA    . LEU   A 1 444 ? -17.006 -99.829  -10.651 1.00 26.48  ? 436 LEU   A CA    1 
ATOM   3474 C C     . LEU   A 1 444 ? -16.548 -98.747  -11.629 1.00 26.61  ? 436 LEU   A C     1 
ATOM   3475 O O     . LEU   A 1 444 ? -15.470 -98.185  -11.445 1.00 26.52  ? 436 LEU   A O     1 
ATOM   3476 C CB    . LEU   A 1 444 ? -15.865 -100.810 -10.389 1.00 26.71  ? 436 LEU   A CB    1 
ATOM   3477 C CG    . LEU   A 1 444 ? -16.116 -101.901 -9.345  1.00 27.13  ? 436 LEU   A CG    1 
ATOM   3478 C CD1   . LEU   A 1 444 ? -14.976 -102.903 -9.407  1.00 27.71  ? 436 LEU   A CD1   1 
ATOM   3479 C CD2   . LEU   A 1 444 ? -16.253 -101.333 -7.943  1.00 26.67  ? 436 LEU   A CD2   1 
ATOM   3480 N N     . LEU   A 1 445 ? -17.341 -98.466  -12.673 1.00 26.34  ? 437 LEU   A N     1 
ATOM   3481 C CA    . LEU   A 1 445 ? -16.897 -97.579  -13.736 1.00 24.99  ? 437 LEU   A CA    1 
ATOM   3482 C C     . LEU   A 1 445 ? -17.209 -96.140  -13.359 1.00 23.94  ? 437 LEU   A C     1 
ATOM   3483 O O     . LEU   A 1 445 ? -18.313 -95.847  -12.912 1.00 23.91  ? 437 LEU   A O     1 
ATOM   3484 C CB    . LEU   A 1 445 ? -17.554 -97.918  -15.071 1.00 25.01  ? 437 LEU   A CB    1 
ATOM   3485 C CG    . LEU   A 1 445 ? -17.351 -99.342  -15.589 1.00 24.86  ? 437 LEU   A CG    1 
ATOM   3486 C CD1   . LEU   A 1 445 ? -17.699 -99.389  -17.062 1.00 24.61  ? 437 LEU   A CD1   1 
ATOM   3487 C CD2   . LEU   A 1 445 ? -15.939 -99.850  -15.341 1.00 25.23  ? 437 LEU   A CD2   1 
ATOM   3488 N N     . GLY   A 1 446 ? -16.231 -95.255  -13.576 1.00 23.46  ? 438 GLY   A N     1 
ATOM   3489 C CA    . GLY   A 1 446 ? -16.449 -93.824  -13.460 1.00 23.21  ? 438 GLY   A CA    1 
ATOM   3490 C C     . GLY   A 1 446 ? -16.847 -93.222  -14.805 1.00 22.64  ? 438 GLY   A C     1 
ATOM   3491 O O     . GLY   A 1 446 ? -17.114 -93.945  -15.762 1.00 22.85  ? 438 GLY   A O     1 
ATOM   3492 N N     . SER   A 1 447 ? -16.859 -91.886  -14.862 1.00 22.05  ? 439 SER   A N     1 
ATOM   3493 C CA    . SER   A 1 447 ? -17.238 -91.148  -16.055 1.00 21.78  ? 439 SER   A CA    1 
ATOM   3494 C C     . SER   A 1 447 ? -16.236 -91.363  -17.183 1.00 21.59  ? 439 SER   A C     1 
ATOM   3495 O O     . SER   A 1 447 ? -16.547 -91.095  -18.337 1.00 20.98  ? 439 SER   A O     1 
ATOM   3496 C CB    . SER   A 1 447 ? -17.368 -89.690  -15.746 1.00 21.44  ? 439 SER   A CB    1 
ATOM   3497 O OG    . SER   A 1 447 ? -18.390 -89.486  -14.784 1.00 21.51  ? 439 SER   A OG    1 
ATOM   3498 N N     . PHE   A 1 448 ? -15.030 -91.816  -16.835 1.00 22.15  ? 440 PHE   A N     1 
ATOM   3499 C CA    . PHE   A 1 448 ? -13.983 -92.045  -17.815 1.00 22.60  ? 440 PHE   A CA    1 
ATOM   3500 C C     . PHE   A 1 448 ? -13.527 -93.495  -17.697 1.00 22.72  ? 440 PHE   A C     1 
ATOM   3501 O O     . PHE   A 1 448 ? -12.387 -93.833  -18.013 1.00 22.25  ? 440 PHE   A O     1 
ATOM   3502 C CB    . PHE   A 1 448 ? -13.004 -90.910  -17.518 1.00 23.12  ? 440 PHE   A CB    1 
ATOM   3503 C CG    . PHE   A 1 448 ? -11.869 -90.755  -18.516 1.00 23.14  ? 440 PHE   A CG    1 
ATOM   3504 C CD1   . PHE   A 1 448 ? -12.088 -90.231  -19.785 1.00 23.33  ? 440 PHE   A CD1   1 
ATOM   3505 C CD2   . PHE   A 1 448 ? -10.572 -91.089  -18.155 1.00 23.57  ? 440 PHE   A CD2   1 
ATOM   3506 C CE1   . PHE   A 1 448 ? -11.036 -90.076  -20.677 1.00 23.44  ? 440 PHE   A CE1   1 
ATOM   3507 C CE2   . PHE   A 1 448 ? -9.525  -90.925  -19.046 1.00 23.22  ? 440 PHE   A CE2   1 
ATOM   3508 C CZ    . PHE   A 1 448 ? -9.758  -90.425  -20.304 1.00 23.39  ? 440 PHE   A CZ    1 
ATOM   3509 N N     . ALA   A 1 449 ? -14.475 -94.315  -17.220 1.00 23.55  ? 441 ALA   A N     1 
ATOM   3510 C CA    . ALA   A 1 449 ? -14.429 -95.769  -17.194 1.00 23.89  ? 441 ALA   A CA    1 
ATOM   3511 C C     . ALA   A 1 449 ? -13.484 -96.266  -16.106 1.00 23.89  ? 441 ALA   A C     1 
ATOM   3512 O O     . ALA   A 1 449 ? -13.939 -96.805  -15.101 1.00 24.47  ? 441 ALA   A O     1 
ATOM   3513 C CB    . ALA   A 1 449 ? -14.084 -96.328  -18.557 1.00 23.80  ? 441 ALA   A CB    1 
ATOM   3514 N N     . ASP   A 1 450 ? -12.179 -96.066  -16.306 1.00 23.92  ? 442 ASP   A N     1 
ATOM   3515 C CA    . ASP   A 1 450 ? -11.171 -96.684  -15.459 1.00 24.44  ? 442 ASP   A CA    1 
ATOM   3516 C C     . ASP   A 1 450 ? -10.762 -95.754  -14.313 1.00 24.19  ? 442 ASP   A C     1 
ATOM   3517 O O     . ASP   A 1 450 ? -9.878  -96.098  -13.531 1.00 23.62  ? 442 ASP   A O     1 
ATOM   3518 C CB    . ASP   A 1 450 ? -9.992  -97.138  -16.305 1.00 24.58  ? 442 ASP   A CB    1 
ATOM   3519 C CG    . ASP   A 1 450 ? -9.282  -96.035  -17.074 1.00 24.70  ? 442 ASP   A CG    1 
ATOM   3520 O OD1   . ASP   A 1 450 ? -8.471  -95.325  -16.449 1.00 24.29  ? 442 ASP   A OD1   1 
ATOM   3521 O OD2   . ASP   A 1 450 ? -9.562  -95.887  -18.284 1.00 25.56  ? 442 ASP   A OD2   1 
ATOM   3522 N N     . ASN   A 1 451 ? -11.420 -94.593  -14.195 1.00 23.99  ? 443 ASN   A N     1 
ATOM   3523 C CA    . ASN   A 1 451 ? -10.987 -93.552  -13.274 1.00 24.17  ? 443 ASN   A CA    1 
ATOM   3524 C C     . ASN   A 1 451 ? -11.248 -93.953  -11.819 1.00 24.60  ? 443 ASN   A C     1 
ATOM   3525 O O     . ASN   A 1 451 ? -10.561 -93.464  -10.929 1.00 25.35  ? 443 ASN   A O     1 
ATOM   3526 C CB    . ASN   A 1 451 ? -11.587 -92.193  -13.628 1.00 24.00  ? 443 ASN   A CB    1 
ATOM   3527 C CG    . ASN   A 1 451 ? -13.087 -92.228  -13.779 1.00 23.88  ? 443 ASN   A CG    1 
ATOM   3528 O OD1   . ASN   A 1 451 ? -13.613 -93.070  -14.516 1.00 24.84  ? 443 ASN   A OD1   1 
ATOM   3529 N ND2   . ASN   A 1 451 ? -13.790 -91.328  -13.108 1.00 23.60  ? 443 ASN   A ND2   1 
ATOM   3530 N N     . GLU   A 1 452 ? -12.214 -94.850  -11.569 1.00 25.02  ? 444 GLU   A N     1 
ATOM   3531 C CA    . GLU   A 1 452 ? -12.473 -95.334  -10.219 1.00 24.64  ? 444 GLU   A CA    1 
ATOM   3532 C C     . GLU   A 1 452 ? -11.713 -96.634  -9.950  1.00 24.54  ? 444 GLU   A C     1 
ATOM   3533 O O     . GLU   A 1 452 ? -11.930 -97.269  -8.922  1.00 25.11  ? 444 GLU   A O     1 
ATOM   3534 C CB    . GLU   A 1 452 ? -13.975 -95.484  -9.979  1.00 25.27  ? 444 GLU   A CB    1 
ATOM   3535 C CG    . GLU   A 1 452 ? -14.736 -94.174  -10.170 1.00 26.18  ? 444 GLU   A CG    1 
ATOM   3536 C CD    . GLU   A 1 452 ? -16.190 -94.172  -9.725  1.00 26.81  ? 444 GLU   A CD    1 
ATOM   3537 O OE1   . GLU   A 1 452 ? -16.732 -95.251  -9.392  1.00 28.41  ? 444 GLU   A OE1   1 
ATOM   3538 O OE2   . GLU   A 1 452 ? -16.779 -93.073  -9.705  1.00 26.13  ? 444 GLU   A OE2   1 
ATOM   3539 N N     . LEU   A 1 453 ? -10.819 -97.019  -10.869 1.00 24.66  ? 445 LEU   A N     1 
ATOM   3540 C CA    . LEU   A 1 453 ? -9.877  -98.110  -10.664 1.00 25.01  ? 445 LEU   A CA    1 
ATOM   3541 C C     . LEU   A 1 453 ? -10.599 -99.457  -10.707 1.00 25.21  ? 445 LEU   A C     1 
ATOM   3542 O O     . LEU   A 1 453 ? -10.224 -100.386 -9.993  1.00 25.61  ? 445 LEU   A O     1 
ATOM   3543 C CB    . LEU   A 1 453 ? -9.101  -97.942  -9.356  1.00 25.13  ? 445 LEU   A CB    1 
ATOM   3544 C CG    . LEU   A 1 453 ? -8.515  -96.552  -9.080  1.00 25.03  ? 445 LEU   A CG    1 
ATOM   3545 C CD1   . LEU   A 1 453 ? -7.636  -96.612  -7.839  1.00 25.05  ? 445 LEU   A CD1   1 
ATOM   3546 C CD2   . LEU   A 1 453 ? -7.743  -95.998  -10.270 1.00 24.68  ? 445 LEU   A CD2   1 
ATOM   3547 N N     . SER   A 1 454 ? -11.611 -99.565  -11.578 1.00 24.88  ? 446 SER   A N     1 
ATOM   3548 C CA    . SER   A 1 454 ? -12.245 -100.840 -11.867 1.00 24.47  ? 446 SER   A CA    1 
ATOM   3549 C C     . SER   A 1 454 ? -11.200 -101.873 -12.285 1.00 23.84  ? 446 SER   A C     1 
ATOM   3550 O O     . SER   A 1 454 ? -11.293 -103.027 -11.876 1.00 23.72  ? 446 SER   A O     1 
ATOM   3551 C CB    . SER   A 1 454 ? -13.318 -100.701 -12.916 1.00 24.59  ? 446 SER   A CB    1 
ATOM   3552 O OG    . SER   A 1 454 ? -13.992 -101.938 -13.107 1.00 24.59  ? 446 SER   A OG    1 
ATOM   3553 N N     . PRO   A 1 455 ? -10.190 -101.520 -13.115 1.00 24.11  ? 447 PRO   A N     1 
ATOM   3554 C CA    . PRO   A 1 455 ? -9.163  -102.486 -13.514 1.00 24.50  ? 447 PRO   A CA    1 
ATOM   3555 C C     . PRO   A 1 455 ? -8.459  -103.181 -12.351 1.00 24.64  ? 447 PRO   A C     1 
ATOM   3556 O O     . PRO   A 1 455 ? -8.308  -104.400 -12.363 1.00 24.42  ? 447 PRO   A O     1 
ATOM   3557 C CB    . PRO   A 1 455 ? -8.190  -101.633 -14.349 1.00 24.25  ? 447 PRO   A CB    1 
ATOM   3558 C CG    . PRO   A 1 455 ? -9.062  -100.538 -14.910 1.00 24.28  ? 447 PRO   A CG    1 
ATOM   3559 C CD    . PRO   A 1 455 ? -10.007 -100.212 -13.767 1.00 24.22  ? 447 PRO   A CD    1 
ATOM   3560 N N     . GLU   A 1 456 ? -8.050  -102.393 -11.349 1.00 25.27  ? 448 GLU   A N     1 
ATOM   3561 C CA    . GLU   A 1 456 ? -7.215  -102.877 -10.261 1.00 25.44  ? 448 GLU   A CA    1 
ATOM   3562 C C     . GLU   A 1 456 ? -8.026  -103.782 -9.338  1.00 25.94  ? 448 GLU   A C     1 
ATOM   3563 O O     . GLU   A 1 456 ? -7.519  -104.794 -8.854  1.00 25.39  ? 448 GLU   A O     1 
ATOM   3564 C CB    . GLU   A 1 456 ? -6.626  -101.715 -9.459  1.00 25.74  ? 448 GLU   A CB    1 
ATOM   3565 C CG    . GLU   A 1 456 ? -5.516  -100.967 -10.192 1.00 26.58  ? 448 GLU   A CG    1 
ATOM   3566 C CD    . GLU   A 1 456 ? -5.942  -100.030 -11.312 1.00 26.87  ? 448 GLU   A CD    1 
ATOM   3567 O OE1   . GLU   A 1 456 ? -7.147  -99.729  -11.458 1.00 26.76  ? 448 GLU   A OE1   1 
ATOM   3568 O OE2   . GLU   A 1 456 ? -5.037  -99.608  -12.060 1.00 27.51  ? 448 GLU   A OE2   1 
ATOM   3569 N N     . CYS   A 1 457 ? -9.278  -103.386 -9.087  1.00 26.59  ? 449 CYS   A N     1 
ATOM   3570 C CA    . CYS   A 1 457 ? -10.169 -104.138 -8.221  1.00 27.16  ? 449 CYS   A CA    1 
ATOM   3571 C C     . CYS   A 1 457 ? -10.438 -105.514 -8.827  1.00 28.69  ? 449 CYS   A C     1 
ATOM   3572 O O     . CYS   A 1 457 ? -10.162 -106.530 -8.196  1.00 29.71  ? 449 CYS   A O     1 
ATOM   3573 C CB    . CYS   A 1 457 ? -11.444 -103.346 -7.958  1.00 27.03  ? 449 CYS   A CB    1 
ATOM   3574 S SG    . CYS   A 1 457 ? -11.156 -101.819 -7.025  1.00 27.41  ? 449 CYS   A SG    1 
ATOM   3575 N N     . LEU   A 1 458 ? -10.942 -105.542 -10.067 1.00 30.30  ? 450 LEU   A N     1 
ATOM   3576 C CA    . LEU   A 1 458 ? -11.316 -106.794 -10.706 1.00 31.29  ? 450 LEU   A CA    1 
ATOM   3577 C C     . LEU   A 1 458 ? -10.082 -107.668 -10.932 1.00 32.41  ? 450 LEU   A C     1 
ATOM   3578 O O     . LEU   A 1 458 ? -10.177 -108.888 -10.822 1.00 34.24  ? 450 LEU   A O     1 
ATOM   3579 C CB    . LEU   A 1 458 ? -12.085 -106.542 -12.003 1.00 31.43  ? 450 LEU   A CB    1 
ATOM   3580 C CG    . LEU   A 1 458 ? -13.452 -105.864 -11.852 1.00 31.94  ? 450 LEU   A CG    1 
ATOM   3581 C CD1   . LEU   A 1 458 ? -14.122 -105.688 -13.205 1.00 31.64  ? 450 LEU   A CD1   1 
ATOM   3582 C CD2   . LEU   A 1 458 ? -14.372 -106.624 -10.909 1.00 32.11  ? 450 LEU   A CD2   1 
ATOM   3583 N N     . ASP   A 1 459 ? -8.929  -107.054 -11.225 1.00 32.26  ? 451 ASP   A N     1 
ATOM   3584 C CA    . ASP   A 1 459 ? -7.678  -107.793 -11.325 1.00 32.71  ? 451 ASP   A CA    1 
ATOM   3585 C C     . ASP   A 1 459 ? -7.427  -108.590 -10.045 1.00 34.13  ? 451 ASP   A C     1 
ATOM   3586 O O     . ASP   A 1 459 ? -7.108  -109.775 -10.104 1.00 34.91  ? 451 ASP   A O     1 
ATOM   3587 C CB    . ASP   A 1 459 ? -6.488  -106.883 -11.594 1.00 32.25  ? 451 ASP   A CB    1 
ATOM   3588 C CG    . ASP   A 1 459 ? -6.319  -106.405 -13.028 1.00 31.97  ? 451 ASP   A CG    1 
ATOM   3589 O OD1   . ASP   A 1 459 ? -7.171  -106.756 -13.873 1.00 32.36  ? 451 ASP   A OD1   1 
ATOM   3590 O OD2   . ASP   A 1 459 ? -5.334  -105.683 -13.284 1.00 31.37  ? 451 ASP   A OD2   1 
ATOM   3591 N N     . GLY   A 1 460 ? -7.568  -107.928 -8.892  1.00 34.95  ? 452 GLY   A N     1 
ATOM   3592 C CA    . GLY   A 1 460 ? -7.313  -108.557 -7.606  1.00 35.91  ? 452 GLY   A CA    1 
ATOM   3593 C C     . GLY   A 1 460 ? -8.382  -109.585 -7.238  1.00 37.40  ? 452 GLY   A C     1 
ATOM   3594 O O     . GLY   A 1 460 ? -8.191  -110.369 -6.312  1.00 39.00  ? 452 GLY   A O     1 
ATOM   3595 N N     . ALA   A 1 461 ? -9.504  -109.570 -7.966  1.00 39.14  ? 453 ALA   A N     1 
ATOM   3596 C CA    . ALA   A 1 461 ? -10.639 -110.427 -7.672  1.00 40.52  ? 453 ALA   A CA    1 
ATOM   3597 C C     . ALA   A 1 461 ? -10.733 -111.608 -8.638  1.00 42.77  ? 453 ALA   A C     1 
ATOM   3598 O O     . ALA   A 1 461 ? -11.435 -112.571 -8.343  1.00 44.87  ? 453 ALA   A O     1 
ATOM   3599 C CB    . ALA   A 1 461 ? -11.905 -109.603 -7.714  1.00 40.31  ? 453 ALA   A CB    1 
ATOM   3600 N N     . GLN   A 1 462 ? -10.042 -111.553 -9.785  1.00 44.40  ? 454 GLN   A N     1 
ATOM   3601 C CA    . GLN   A 1 462 ? -10.331 -112.495 -10.860 1.00 46.20  ? 454 GLN   A CA    1 
ATOM   3602 C C     . GLN   A 1 462 ? -9.826  -113.899 -10.519 1.00 46.29  ? 454 GLN   A C     1 
ATOM   3603 O O     . GLN   A 1 462 ? -10.222 -114.858 -11.180 1.00 47.35  ? 454 GLN   A O     1 
ATOM   3604 C CB    . GLN   A 1 462 ? -9.834  -112.066 -12.244 1.00 46.95  ? 454 GLN   A CB    1 
ATOM   3605 C CG    . GLN   A 1 462 ? -8.320  -111.995 -12.413 1.00 47.47  ? 454 GLN   A CG    1 
ATOM   3606 C CD    . GLN   A 1 462 ? -7.901  -111.664 -13.831 1.00 47.94  ? 454 GLN   A CD    1 
ATOM   3607 O OE1   . GLN   A 1 462 ? -8.719  -111.626 -14.758 1.00 46.70  ? 454 GLN   A OE1   1 
ATOM   3608 N NE2   . GLN   A 1 462 ? -6.611  -111.425 -14.018 1.00 48.52  ? 454 GLN   A NE2   1 
ATOM   3609 N N     . HIS   A 1 463 ? -8.980  -114.030 -9.488  1.00 45.79  ? 455 HIS   A N     1 
ATOM   3610 C CA    . HIS   A 1 463 ? -8.456  -115.331 -9.099  1.00 45.40  ? 455 HIS   A CA    1 
ATOM   3611 C C     . HIS   A 1 463 ? -9.581  -116.272 -8.666  1.00 45.03  ? 455 HIS   A C     1 
ATOM   3612 O O     . HIS   A 1 463 ? -9.415  -117.487 -8.742  1.00 45.01  ? 455 HIS   A O     1 
ATOM   3613 C CB    . HIS   A 1 463 ? -7.368  -115.214 -8.023  1.00 45.97  ? 455 HIS   A CB    1 
ATOM   3614 C CG    . HIS   A 1 463 ? -7.816  -114.653 -6.712  1.00 47.02  ? 455 HIS   A CG    1 
ATOM   3615 N ND1   . HIS   A 1 463 ? -8.604  -115.348 -5.821  1.00 47.63  ? 455 HIS   A ND1   1 
ATOM   3616 C CD2   . HIS   A 1 463 ? -7.580  -113.463 -6.144  1.00 47.66  ? 455 HIS   A CD2   1 
ATOM   3617 C CE1   . HIS   A 1 463 ? -8.828  -114.595 -4.754  1.00 47.78  ? 455 HIS   A CE1   1 
ATOM   3618 N NE2   . HIS   A 1 463 ? -8.217  -113.445 -4.930  1.00 47.98  ? 455 HIS   A NE2   1 
ATOM   3619 N N     . PHE   A 1 464 ? -10.719 -115.720 -8.216  1.00 44.78  ? 456 PHE   A N     1 
ATOM   3620 C CA    . PHE   A 1 464 ? -11.838 -116.546 -7.783  1.00 44.58  ? 456 PHE   A CA    1 
ATOM   3621 C C     . PHE   A 1 464 ? -12.937 -116.568 -8.847  1.00 45.02  ? 456 PHE   A C     1 
ATOM   3622 O O     . PHE   A 1 464 ? -14.083 -116.894 -8.544  1.00 44.67  ? 456 PHE   A O     1 
ATOM   3623 C CB    . PHE   A 1 464 ? -12.352 -116.120 -6.401  1.00 43.67  ? 456 PHE   A CB    1 
ATOM   3624 C CG    . PHE   A 1 464 ? -12.859 -114.692 -6.241  1.00 42.76  ? 456 PHE   A CG    1 
ATOM   3625 C CD1   . PHE   A 1 464 ? -14.117 -114.319 -6.704  1.00 42.58  ? 456 PHE   A CD1   1 
ATOM   3626 C CD2   . PHE   A 1 464 ? -12.099 -113.739 -5.568  1.00 42.42  ? 456 PHE   A CD2   1 
ATOM   3627 C CE1   . PHE   A 1 464 ? -14.580 -113.023 -6.536  1.00 42.85  ? 456 PHE   A CE1   1 
ATOM   3628 C CE2   . PHE   A 1 464 ? -12.568 -112.445 -5.400  1.00 42.03  ? 456 PHE   A CE2   1 
ATOM   3629 C CZ    . PHE   A 1 464 ? -13.808 -112.090 -5.882  1.00 42.52  ? 456 PHE   A CZ    1 
ATOM   3630 N N     . LEU   A 1 465 ? -12.576 -116.256 -10.099 1.00 46.30  ? 457 LEU   A N     1 
ATOM   3631 C CA    . LEU   A 1 465 ? -13.432 -116.540 -11.241 1.00 46.28  ? 457 LEU   A CA    1 
ATOM   3632 C C     . LEU   A 1 465 ? -13.052 -117.913 -11.795 1.00 46.08  ? 457 LEU   A C     1 
ATOM   3633 O O     . LEU   A 1 465 ? -11.869 -118.230 -11.915 1.00 43.91  ? 457 LEU   A O     1 
ATOM   3634 C CB    . LEU   A 1 465 ? -13.265 -115.435 -12.284 1.00 46.77  ? 457 LEU   A CB    1 
ATOM   3635 C CG    . LEU   A 1 465 ? -14.298 -115.396 -13.416 1.00 47.67  ? 457 LEU   A CG    1 
ATOM   3636 C CD1   . LEU   A 1 465 ? -15.701 -115.083 -12.915 1.00 47.52  ? 457 LEU   A CD1   1 
ATOM   3637 C CD2   . LEU   A 1 465 ? -13.885 -114.382 -14.472 1.00 47.79  ? 457 LEU   A CD2   1 
ATOM   3638 N N     . LYS   A 1 466 ? -14.062 -118.733 -12.106 1.00 47.16  ? 458 LYS   A N     1 
ATOM   3639 C CA    . LYS   A 1 466 ? -13.836 -119.996 -12.791 1.00 49.04  ? 458 LYS   A CA    1 
ATOM   3640 C C     . LYS   A 1 466 ? -12.990 -119.736 -14.035 1.00 48.27  ? 458 LYS   A C     1 
ATOM   3641 O O     . LYS   A 1 466 ? -13.105 -118.680 -14.653 1.00 47.72  ? 458 LYS   A O     1 
ATOM   3642 C CB    . LYS   A 1 466 ? -15.162 -120.668 -13.170 1.00 50.30  ? 458 LYS   A CB    1 
ATOM   3643 C CG    . LYS   A 1 466 ? -15.946 -121.256 -12.004 1.00 50.88  ? 458 LYS   A CG    1 
ATOM   3644 C CD    . LYS   A 1 466 ? -17.312 -121.815 -12.381 1.00 51.44  ? 458 LYS   A CD    1 
ATOM   3645 C CE    . LYS   A 1 466 ? -18.141 -122.108 -11.167 1.00 52.41  ? 458 LYS   A CE    1 
ATOM   3646 N NZ    . LYS   A 1 466 ? -19.250 -123.029 -11.431 1.00 53.03  ? 458 LYS   A NZ    1 
ATOM   3647 N N     . ASP   A 1 467 ? -12.161 -120.719 -14.405 1.00 48.36  ? 459 ASP   A N     1 
ATOM   3648 C CA    . ASP   A 1 467 ? -11.236 -120.578 -15.520 1.00 48.77  ? 459 ASP   A CA    1 
ATOM   3649 C C     . ASP   A 1 467 ? -11.987 -120.245 -16.811 1.00 47.03  ? 459 ASP   A C     1 
ATOM   3650 O O     . ASP   A 1 467 ? -11.362 -119.864 -17.797 1.00 46.20  ? 459 ASP   A O     1 
ATOM   3651 C CB    . ASP   A 1 467 ? -10.371 -121.820 -15.683 1.00 50.51  ? 459 ASP   A CB    1 
ATOM   3652 C CG    . ASP   A 1 467 ? -9.457  -122.142 -14.508 1.00 53.06  ? 459 ASP   A CG    1 
ATOM   3653 O OD1   . ASP   A 1 467 ? -9.979  -122.297 -13.382 1.00 55.04  ? 459 ASP   A OD1   1 
ATOM   3654 O OD2   . ASP   A 1 467 ? -8.232  -122.242 -14.726 1.00 54.72  ? 459 ASP   A OD2   1 
ATOM   3655 N N     . ASP   A 1 468 ? -13.321 -120.391 -16.795 1.00 45.90  ? 460 ASP   A N     1 
ATOM   3656 C CA    . ASP   A 1 468 ? -14.163 -120.114 -17.948 1.00 44.89  ? 460 ASP   A CA    1 
ATOM   3657 C C     . ASP   A 1 468 ? -15.277 -119.137 -17.575 1.00 44.07  ? 460 ASP   A C     1 
ATOM   3658 O O     . ASP   A 1 468 ? -16.328 -119.136 -18.210 1.00 45.17  ? 460 ASP   A O     1 
ATOM   3659 C CB    . ASP   A 1 468 ? -14.780 -121.401 -18.473 1.00 46.09  ? 460 ASP   A CB    1 
ATOM   3660 C CG    . ASP   A 1 468 ? -15.923 -121.964 -17.635 1.00 47.81  ? 460 ASP   A CG    1 
ATOM   3661 O OD1   . ASP   A 1 468 ? -15.792 -121.984 -16.392 1.00 48.16  ? 460 ASP   A OD1   1 
ATOM   3662 O OD2   . ASP   A 1 468 ? -16.939 -122.379 -18.232 1.00 48.44  ? 460 ASP   A OD2   1 
ATOM   3663 N N     . GLY   A 1 469 ? -15.046 -118.303 -16.552 1.00 42.81  ? 461 GLY   A N     1 
ATOM   3664 C CA    . GLY   A 1 469 ? -16.094 -117.457 -16.002 1.00 40.47  ? 461 GLY   A CA    1 
ATOM   3665 C C     . GLY   A 1 469 ? -16.267 -116.167 -16.801 1.00 38.76  ? 461 GLY   A C     1 
ATOM   3666 O O     . GLY   A 1 469 ? -15.410 -115.812 -17.607 1.00 38.28  ? 461 GLY   A O     1 
ATOM   3667 N N     . VAL   A 1 470 ? -17.392 -115.483 -16.557 1.00 37.15  ? 462 VAL   A N     1 
ATOM   3668 C CA    . VAL   A 1 470 ? -17.700 -114.205 -17.180 1.00 35.61  ? 462 VAL   A CA    1 
ATOM   3669 C C     . VAL   A 1 470 ? -17.540 -113.100 -16.136 1.00 34.65  ? 462 VAL   A C     1 
ATOM   3670 O O     . VAL   A 1 470 ? -17.967 -113.255 -14.994 1.00 33.87  ? 462 VAL   A O     1 
ATOM   3671 C CB    . VAL   A 1 470 ? -19.128 -114.206 -17.763 1.00 34.83  ? 462 VAL   A CB    1 
ATOM   3672 C CG1   . VAL   A 1 470 ? -19.509 -112.863 -18.378 1.00 34.40  ? 462 VAL   A CG1   1 
ATOM   3673 C CG2   . VAL   A 1 470 ? -19.327 -115.327 -18.774 1.00 34.62  ? 462 VAL   A CG2   1 
ATOM   3674 N N     . SER   A 1 471 ? -16.906 -111.995 -16.546 1.00 33.87  ? 463 SER   A N     1 
ATOM   3675 C CA    . SER   A 1 471 ? -17.004 -110.729 -15.839 1.00 32.61  ? 463 SER   A CA    1 
ATOM   3676 C C     . SER   A 1 471 ? -18.007 -109.832 -16.556 1.00 31.96  ? 463 SER   A C     1 
ATOM   3677 O O     . SER   A 1 471 ? -17.926 -109.655 -17.768 1.00 31.68  ? 463 SER   A O     1 
ATOM   3678 C CB    . SER   A 1 471 ? -15.664 -110.045 -15.725 1.00 32.35  ? 463 SER   A CB    1 
ATOM   3679 O OG    . SER   A 1 471 ? -15.822 -108.661 -15.444 1.00 32.41  ? 463 SER   A OG    1 
ATOM   3680 N N     . ILE   A 1 472 ? -18.953 -109.286 -15.789 1.00 31.47  ? 464 ILE   A N     1 
ATOM   3681 C CA    . ILE   A 1 472 ? -19.839 -108.241 -16.272 1.00 31.46  ? 464 ILE   A CA    1 
ATOM   3682 C C     . ILE   A 1 472 ? -19.541 -106.976 -15.467 1.00 31.40  ? 464 ILE   A C     1 
ATOM   3683 O O     . ILE   A 1 472 ? -19.700 -106.969 -14.248 1.00 32.82  ? 464 ILE   A O     1 
ATOM   3684 C CB    . ILE   A 1 472 ? -21.313 -108.681 -16.177 1.00 31.26  ? 464 ILE   A CB    1 
ATOM   3685 C CG1   . ILE   A 1 472 ? -21.559 -109.948 -17.005 1.00 32.00  ? 464 ILE   A CG1   1 
ATOM   3686 C CG2   . ILE   A 1 472 ? -22.257 -107.544 -16.576 1.00 30.82  ? 464 ILE   A CG2   1 
ATOM   3687 C CD1   . ILE   A 1 472 ? -22.982 -110.480 -16.956 1.00 32.49  ? 464 ILE   A CD1   1 
ATOM   3688 N N     . PRO   A 1 473 ? -19.081 -105.869 -16.097 1.00 30.33  ? 465 PRO   A N     1 
ATOM   3689 C CA    . PRO   A 1 473 ? -18.915 -105.787 -17.550 1.00 29.24  ? 465 PRO   A CA    1 
ATOM   3690 C C     . PRO   A 1 473 ? -17.690 -106.519 -18.087 1.00 28.34  ? 465 PRO   A C     1 
ATOM   3691 O O     . PRO   A 1 473 ? -16.763 -106.818 -17.338 1.00 28.12  ? 465 PRO   A O     1 
ATOM   3692 C CB    . PRO   A 1 473 ? -18.811 -104.272 -17.756 1.00 29.52  ? 465 PRO   A CB    1 
ATOM   3693 C CG    . PRO   A 1 473 ? -18.077 -103.798 -16.529 1.00 29.84  ? 465 PRO   A CG    1 
ATOM   3694 C CD    . PRO   A 1 473 ? -18.691 -104.625 -15.415 1.00 30.35  ? 465 PRO   A CD    1 
ATOM   3695 N N     . GLY   A 1 474 ? -17.707 -106.786 -19.400 1.00 28.00  ? 466 GLY   A N     1 
ATOM   3696 C CA    . GLY   A 1 474 ? -16.661 -107.545 -20.064 1.00 27.65  ? 466 GLY   A CA    1 
ATOM   3697 C C     . GLY   A 1 474 ? -15.526 -106.651 -20.555 1.00 27.46  ? 466 GLY   A C     1 
ATOM   3698 O O     . GLY   A 1 474 ? -14.369 -107.068 -20.568 1.00 27.19  ? 466 GLY   A O     1 
ATOM   3699 N N     . GLU   A 1 475 ? -15.870 -105.427 -20.973 1.00 27.44  ? 467 GLU   A N     1 
ATOM   3700 C CA    . GLU   A 1 475 ? -14.887 -104.480 -21.472 1.00 27.52  ? 467 GLU   A CA    1 
ATOM   3701 C C     . GLU   A 1 475 ? -15.437 -103.064 -21.317 1.00 25.91  ? 467 GLU   A C     1 
ATOM   3702 O O     . GLU   A 1 475 ? -16.650 -102.871 -21.260 1.00 25.05  ? 467 GLU   A O     1 
ATOM   3703 C CB    . GLU   A 1 475 ? -14.516 -104.876 -22.905 1.00 28.83  ? 467 GLU   A CB    1 
ATOM   3704 C CG    . GLU   A 1 475 ? -13.686 -103.848 -23.672 1.00 30.47  ? 467 GLU   A CG    1 
ATOM   3705 C CD    . GLU   A 1 475 ? -14.449 -103.044 -24.710 1.00 31.96  ? 467 GLU   A CD    1 
ATOM   3706 O OE1   . GLU   A 1 475 ? -14.745 -101.842 -24.496 1.00 30.80  ? 467 GLU   A OE1   1 
ATOM   3707 O OE2   . GLU   A 1 475 ? -14.718 -103.654 -25.771 1.00 33.19  ? 467 GLU   A OE2   1 
ATOM   3708 N N     . TYR   A 1 476 ? -14.523 -102.093 -21.195 1.00 24.97  ? 468 TYR   A N     1 
ATOM   3709 C CA    . TYR   A 1 476 ? -14.877 -100.683 -21.226 1.00 24.53  ? 468 TYR   A CA    1 
ATOM   3710 C C     . TYR   A 1 476 ? -13.791 -99.911  -21.974 1.00 23.40  ? 468 TYR   A C     1 
ATOM   3711 O O     . TYR   A 1 476 ? -12.631 -100.323 -21.995 1.00 22.46  ? 468 TYR   A O     1 
ATOM   3712 C CB    . TYR   A 1 476 ? -15.145 -100.130 -19.820 1.00 25.19  ? 468 TYR   A CB    1 
ATOM   3713 C CG    . TYR   A 1 476 ? -14.322 -100.702 -18.671 1.00 26.17  ? 468 TYR   A CG    1 
ATOM   3714 C CD1   . TYR   A 1 476 ? -13.111 -100.135 -18.288 1.00 26.40  ? 468 TYR   A CD1   1 
ATOM   3715 C CD2   . TYR   A 1 476 ? -14.784 -101.790 -17.937 1.00 26.78  ? 468 TYR   A CD2   1 
ATOM   3716 C CE1   . TYR   A 1 476 ? -12.375 -100.646 -17.229 1.00 26.60  ? 468 TYR   A CE1   1 
ATOM   3717 C CE2   . TYR   A 1 476 ? -14.056 -102.312 -16.879 1.00 27.08  ? 468 TYR   A CE2   1 
ATOM   3718 C CZ    . TYR   A 1 476 ? -12.848 -101.740 -16.522 1.00 27.13  ? 468 TYR   A CZ    1 
ATOM   3719 O OH    . TYR   A 1 476 ? -12.139 -102.262 -15.475 1.00 26.72  ? 468 TYR   A OH    1 
ATOM   3720 N N     . THR   A 1 477 ? -14.208 -98.807  -22.610 1.00 22.62  ? 469 THR   A N     1 
ATOM   3721 C CA    . THR   A 1 477 ? -13.315 -97.921  -23.339 1.00 22.47  ? 469 THR   A CA    1 
ATOM   3722 C C     . THR   A 1 477 ? -13.665 -96.476  -22.994 1.00 22.43  ? 469 THR   A C     1 
ATOM   3723 O O     . THR   A 1 477 ? -14.837 -96.110  -22.968 1.00 22.09  ? 469 THR   A O     1 
ATOM   3724 C CB    . THR   A 1 477 ? -13.434 -98.176  -24.842 1.00 22.53  ? 469 THR   A CB    1 
ATOM   3725 O OG1   . THR   A 1 477 ? -12.922 -99.490  -25.044 1.00 23.03  ? 469 THR   A OG1   1 
ATOM   3726 C CG2   . THR   A 1 477 ? -12.642 -97.185  -25.678 1.00 22.20  ? 469 THR   A CG2   1 
ATOM   3727 N N     . SER   A 1 478 ? -12.632 -95.670  -22.728 1.00 22.76  ? 470 SER   A N     1 
ATOM   3728 C CA    . SER   A 1 478 ? -12.795 -94.245  -22.497 1.00 22.71  ? 470 SER   A CA    1 
ATOM   3729 C C     . SER   A 1 478 ? -12.651 -93.497  -23.822 1.00 22.45  ? 470 SER   A C     1 
ATOM   3730 O O     . SER   A 1 478 ? -11.968 -93.968  -24.726 1.00 22.37  ? 470 SER   A O     1 
ATOM   3731 C CB    . SER   A 1 478 ? -11.808 -93.749  -21.466 1.00 22.59  ? 470 SER   A CB    1 
ATOM   3732 O OG    . SER   A 1 478 ? -10.468 -94.035  -21.847 1.00 22.70  ? 470 SER   A OG    1 
ATOM   3733 N N     . PHE   A 1 479 ? -13.314 -92.337  -23.921 1.00 22.80  ? 471 PHE   A N     1 
ATOM   3734 C CA    . PHE   A 1 479 ? -13.255 -91.487  -25.101 1.00 22.88  ? 471 PHE   A CA    1 
ATOM   3735 C C     . PHE   A 1 479 ? -12.916 -90.056  -24.689 1.00 22.72  ? 471 PHE   A C     1 
ATOM   3736 O O     . PHE   A 1 479 ? -13.318 -89.613  -23.617 1.00 22.99  ? 471 PHE   A O     1 
ATOM   3737 C CB    . PHE   A 1 479 ? -14.589 -91.487  -25.853 1.00 23.20  ? 471 PHE   A CB    1 
ATOM   3738 C CG    . PHE   A 1 479 ? -14.923 -92.764  -26.612 1.00 23.62  ? 471 PHE   A CG    1 
ATOM   3739 C CD1   . PHE   A 1 479 ? -15.469 -93.863  -25.957 1.00 24.07  ? 471 PHE   A CD1   1 
ATOM   3740 C CD2   . PHE   A 1 479 ? -14.726 -92.846  -27.987 1.00 23.71  ? 471 PHE   A CD2   1 
ATOM   3741 C CE1   . PHE   A 1 479 ? -15.787 -95.019  -26.654 1.00 23.86  ? 471 PHE   A CE1   1 
ATOM   3742 C CE2   . PHE   A 1 479 ? -15.047 -94.004  -28.678 1.00 23.95  ? 471 PHE   A CE2   1 
ATOM   3743 C CZ    . PHE   A 1 479 ? -15.575 -95.087  -28.011 1.00 23.95  ? 471 PHE   A CZ    1 
ATOM   3744 N N     . LEU   A 1 480 ? -12.202 -89.340  -25.572 1.00 22.71  ? 472 LEU   A N     1 
ATOM   3745 C CA    . LEU   A 1 480 ? -11.810 -87.955  -25.356 1.00 22.49  ? 472 LEU   A CA    1 
ATOM   3746 C C     . LEU   A 1 480 ? -12.267 -87.110  -26.540 1.00 22.07  ? 472 LEU   A C     1 
ATOM   3747 O O     . LEU   A 1 480 ? -12.334 -87.612  -27.655 1.00 22.85  ? 472 LEU   A O     1 
ATOM   3748 C CB    . LEU   A 1 480 ? -10.292 -87.845  -25.208 1.00 22.51  ? 472 LEU   A CB    1 
ATOM   3749 C CG    . LEU   A 1 480 ? -9.692  -88.232  -23.854 1.00 22.36  ? 472 LEU   A CG    1 
ATOM   3750 C CD1   . LEU   A 1 480 ? -8.182  -88.295  -23.992 1.00 22.41  ? 472 LEU   A CD1   1 
ATOM   3751 C CD2   . LEU   A 1 480 ? -10.089 -87.261  -22.755 1.00 22.13  ? 472 LEU   A CD2   1 
ATOM   3752 N N     . ALA   A 1 481 ? -12.533 -85.822  -26.293 1.00 21.55  ? 473 ALA   A N     1 
ATOM   3753 C CA    . ALA   A 1 481 ? -12.775 -84.867  -27.362 1.00 21.71  ? 473 ALA   A CA    1 
ATOM   3754 C C     . ALA   A 1 481 ? -12.324 -83.474  -26.926 1.00 21.56  ? 473 ALA   A C     1 
ATOM   3755 O O     . ALA   A 1 481 ? -12.648 -83.036  -25.825 1.00 21.45  ? 473 ALA   A O     1 
ATOM   3756 C CB    . ALA   A 1 481 ? -14.236 -84.876  -27.754 1.00 21.82  ? 473 ALA   A CB    1 
ATOM   3757 N N     . PRO   A 1 482 ? -11.551 -82.740  -27.761 1.00 21.38  ? 474 PRO   A N     1 
ATOM   3758 C CA    . PRO   A 1 482 ? -11.204 -81.350  -27.461 1.00 21.43  ? 474 PRO   A CA    1 
ATOM   3759 C C     . PRO   A 1 482 ? -12.452 -80.478  -27.390 1.00 21.00  ? 474 PRO   A C     1 
ATOM   3760 O O     . PRO   A 1 482 ? -13.387 -80.681  -28.163 1.00 21.13  ? 474 PRO   A O     1 
ATOM   3761 C CB    . PRO   A 1 482 ? -10.273 -80.943  -28.620 1.00 21.40  ? 474 PRO   A CB    1 
ATOM   3762 C CG    . PRO   A 1 482 ? -10.613 -81.915  -29.729 1.00 21.46  ? 474 PRO   A CG    1 
ATOM   3763 C CD    . PRO   A 1 482 ? -10.946 -83.211  -29.016 1.00 21.50  ? 474 PRO   A CD    1 
ATOM   3764 N N     . ILE   A 1 483 ? -12.454 -79.519  -26.456 1.00 20.39  ? 475 ILE   A N     1 
ATOM   3765 C CA    . ILE   A 1 483 ? -13.551 -78.573  -26.333 1.00 20.47  ? 475 ILE   A CA    1 
ATOM   3766 C C     . ILE   A 1 483 ? -13.014 -77.155  -26.165 1.00 20.40  ? 475 ILE   A C     1 
ATOM   3767 O O     . ILE   A 1 483 ? -11.889 -76.945  -25.715 1.00 19.58  ? 475 ILE   A O     1 
ATOM   3768 C CB    . ILE   A 1 483 ? -14.491 -78.922  -25.167 1.00 20.51  ? 475 ILE   A CB    1 
ATOM   3769 C CG1   . ILE   A 1 483 ? -13.784 -78.823  -23.814 1.00 20.42  ? 475 ILE   A CG1   1 
ATOM   3770 C CG2   . ILE   A 1 483 ? -15.132 -80.293  -25.370 1.00 20.78  ? 475 ILE   A CG2   1 
ATOM   3771 C CD1   . ILE   A 1 483 ? -14.664 -78.272  -22.710 1.00 20.51  ? 475 ILE   A CD1   1 
ATOM   3772 N N     . SER   A 1 484 ? -13.871 -76.198  -26.534 1.00 20.97  ? 476 SER   A N     1 
ATOM   3773 C CA    . SER   A 1 484 ? -13.693 -74.790  -26.233 1.00 21.42  ? 476 SER   A CA    1 
ATOM   3774 C C     . SER   A 1 484 ? -14.796 -74.356  -25.275 1.00 21.85  ? 476 SER   A C     1 
ATOM   3775 O O     . SER   A 1 484 ? -15.976 -74.555  -25.557 1.00 22.76  ? 476 SER   A O     1 
ATOM   3776 C CB    . SER   A 1 484 ? -13.718 -73.954  -27.489 1.00 21.42  ? 476 SER   A CB    1 
ATOM   3777 O OG    . SER   A 1 484 ? -13.623 -72.567  -27.186 1.00 21.55  ? 476 SER   A OG    1 
ATOM   3778 N N     . SER   A 1 485 ? -14.393 -73.797  -24.132 1.00 21.62  ? 477 SER   A N     1 
ATOM   3779 C CA    . SER   A 1 485 ? -15.305 -73.109  -23.236 1.00 21.92  ? 477 SER   A CA    1 
ATOM   3780 C C     . SER   A 1 485 ? -14.507 -72.145  -22.365 1.00 22.20  ? 477 SER   A C     1 
ATOM   3781 O O     . SER   A 1 485 ? -13.853 -72.566  -21.416 1.00 21.77  ? 477 SER   A O     1 
ATOM   3782 C CB    . SER   A 1 485 ? -16.096 -74.086  -22.396 1.00 21.82  ? 477 SER   A CB    1 
ATOM   3783 O OG    . SER   A 1 485 ? -16.986 -73.409  -21.518 1.00 21.24  ? 477 SER   A OG    1 
ATOM   3784 N N     . SER   A 1 486 ? -14.546 -70.855  -22.713 1.00 23.10  ? 478 SER   A N     1 
ATOM   3785 C CA    . SER   A 1 486 ? -13.927 -69.824  -21.896 1.00 23.74  ? 478 SER   A CA    1 
ATOM   3786 C C     . SER   A 1 486 ? -14.634 -69.730  -20.545 1.00 23.89  ? 478 SER   A C     1 
ATOM   3787 O O     . SER   A 1 486 ? -14.058 -69.238  -19.580 1.00 23.82  ? 478 SER   A O     1 
ATOM   3788 C CB    . SER   A 1 486 ? -13.916 -68.489  -22.601 1.00 24.22  ? 478 SER   A CB    1 
ATOM   3789 O OG    . SER   A 1 486 ? -13.000 -68.485  -23.689 1.00 24.88  ? 478 SER   A OG    1 
ATOM   3790 N N     . LYS   A 1 487 ? -15.884 -70.205  -20.493 1.00 24.19  ? 479 LYS   A N     1 
ATOM   3791 C CA    . LYS   A 1 487 ? -16.661 -70.221  -19.266 1.00 24.91  ? 479 LYS   A CA    1 
ATOM   3792 C C     . LYS   A 1 487 ? -16.089 -71.243  -18.285 1.00 24.54  ? 479 LYS   A C     1 
ATOM   3793 O O     . LYS   A 1 487 ? -15.732 -70.891  -17.164 1.00 23.59  ? 479 LYS   A O     1 
ATOM   3794 C CB    . LYS   A 1 487 ? -18.126 -70.545  -19.575 1.00 26.03  ? 479 LYS   A CB    1 
ATOM   3795 C CG    . LYS   A 1 487 ? -19.045 -70.448  -18.370 1.00 27.56  ? 479 LYS   A CG    1 
ATOM   3796 C CD    . LYS   A 1 487 ? -20.335 -71.238  -18.525 1.00 29.07  ? 479 LYS   A CD    1 
ATOM   3797 C CE    . LYS   A 1 487 ? -21.260 -71.031  -17.370 1.00 30.47  ? 479 LYS   A CE    1 
ATOM   3798 N NZ    . LYS   A 1 487 ? -22.469 -71.845  -17.520 1.00 31.46  ? 479 LYS   A NZ    1 
ATOM   3799 N N     . LEU   A 1 488 ? -16.027 -72.511  -18.712 1.00 24.33  ? 480 LEU   A N     1 
ATOM   3800 C CA    . LEU   A 1 488 ? -15.519 -73.590  -17.880 1.00 24.04  ? 480 LEU   A CA    1 
ATOM   3801 C C     . LEU   A 1 488 ? -14.057 -73.330  -17.528 1.00 23.88  ? 480 LEU   A C     1 
ATOM   3802 O O     . LEU   A 1 488 ? -13.642 -73.589  -16.402 1.00 24.35  ? 480 LEU   A O     1 
ATOM   3803 C CB    . LEU   A 1 488 ? -15.685 -74.941  -18.577 1.00 23.99  ? 480 LEU   A CB    1 
ATOM   3804 C CG    . LEU   A 1 488 ? -17.096 -75.541  -18.576 1.00 23.83  ? 480 LEU   A CG    1 
ATOM   3805 C CD1   . LEU   A 1 488 ? -17.199 -76.669  -19.587 1.00 23.74  ? 480 LEU   A CD1   1 
ATOM   3806 C CD2   . LEU   A 1 488 ? -17.493 -76.037  -17.195 1.00 23.71  ? 480 LEU   A CD2   1 
ATOM   3807 N N     . TYR   A 1 489 ? -13.276 -72.834  -18.494 1.00 24.01  ? 481 TYR   A N     1 
ATOM   3808 C CA    . TYR   A 1 489 ? -11.889 -72.482  -18.236 1.00 24.43  ? 481 TYR   A CA    1 
ATOM   3809 C C     . TYR   A 1 489 ? -11.810 -71.545  -17.033 1.00 25.26  ? 481 TYR   A C     1 
ATOM   3810 O O     . TYR   A 1 489 ? -10.929 -71.688  -16.191 1.00 25.34  ? 481 TYR   A O     1 
ATOM   3811 C CB    . TYR   A 1 489 ? -11.206 -71.800  -19.422 1.00 24.29  ? 481 TYR   A CB    1 
ATOM   3812 C CG    . TYR   A 1 489 ? -9.818  -71.272  -19.086 1.00 24.33  ? 481 TYR   A CG    1 
ATOM   3813 C CD1   . TYR   A 1 489 ? -8.738  -72.137  -18.949 1.00 24.31  ? 481 TYR   A CD1   1 
ATOM   3814 C CD2   . TYR   A 1 489 ? -9.586  -69.913  -18.906 1.00 24.90  ? 481 TYR   A CD2   1 
ATOM   3815 C CE1   . TYR   A 1 489 ? -7.471  -71.667  -18.641 1.00 24.52  ? 481 TYR   A CE1   1 
ATOM   3816 C CE2   . TYR   A 1 489 ? -8.324  -69.430  -18.597 1.00 25.19  ? 481 TYR   A CE2   1 
ATOM   3817 C CZ    . TYR   A 1 489 ? -7.264  -70.310  -18.464 1.00 25.19  ? 481 TYR   A CZ    1 
ATOM   3818 O OH    . TYR   A 1 489 ? -6.021  -69.832  -18.160 1.00 25.76  ? 481 TYR   A OH    1 
ATOM   3819 N N     . ASN   A 1 490 ? -12.740 -70.586  -16.973 1.00 25.92  ? 482 ASN   A N     1 
ATOM   3820 C CA    . ASN   A 1 490 ? -12.707 -69.526  -15.983 1.00 26.28  ? 482 ASN   A CA    1 
ATOM   3821 C C     . ASN   A 1 490 ? -13.183 -70.058  -14.631 1.00 25.98  ? 482 ASN   A C     1 
ATOM   3822 O O     . ASN   A 1 490 ? -12.743 -69.578  -13.588 1.00 25.92  ? 482 ASN   A O     1 
ATOM   3823 C CB    . ASN   A 1 490 ? -13.521 -68.328  -16.462 1.00 27.11  ? 482 ASN   A CB    1 
ATOM   3824 C CG    . ASN   A 1 490 ? -12.967 -67.009  -15.977 1.00 28.36  ? 482 ASN   A CG    1 
ATOM   3825 O OD1   . ASN   A 1 490 ? -11.830 -66.946  -15.494 1.00 29.34  ? 482 ASN   A OD1   1 
ATOM   3826 N ND2   . ASN   A 1 490 ? -13.735 -65.940  -16.132 1.00 28.69  ? 482 ASN   A ND2   1 
ATOM   3827 N N     . GLU   A 1 491 ? -14.087 -71.045  -14.655 1.00 26.29  ? 483 GLU   A N     1 
ATOM   3828 C CA    . GLU   A 1 491 ? -14.576 -71.677  -13.438 1.00 27.30  ? 483 GLU   A CA    1 
ATOM   3829 C C     . GLU   A 1 491 ? -13.463 -72.483  -12.773 1.00 27.32  ? 483 GLU   A C     1 
ATOM   3830 O O     . GLU   A 1 491 ? -13.290 -72.423  -11.559 1.00 27.98  ? 483 GLU   A O     1 
ATOM   3831 C CB    . GLU   A 1 491 ? -15.739 -72.627  -13.718 1.00 28.03  ? 483 GLU   A CB    1 
ATOM   3832 C CG    . GLU   A 1 491 ? -17.015 -71.915  -14.154 1.00 28.85  ? 483 GLU   A CG    1 
ATOM   3833 C CD    . GLU   A 1 491 ? -18.202 -72.844  -14.333 1.00 30.22  ? 483 GLU   A CD    1 
ATOM   3834 O OE1   . GLU   A 1 491 ? -18.074 -74.057  -14.057 1.00 30.63  ? 483 GLU   A OE1   1 
ATOM   3835 O OE2   . GLU   A 1 491 ? -19.264 -72.345  -14.754 1.00 31.88  ? 483 GLU   A OE2   1 
ATOM   3836 N N     . VAL   A 1 492 ? -12.738 -73.263  -13.581 1.00 27.53  ? 484 VAL   A N     1 
ATOM   3837 C CA    . VAL   A 1 492 ? -11.586 -74.009  -13.105 1.00 27.37  ? 484 VAL   A CA    1 
ATOM   3838 C C     . VAL   A 1 492 ? -10.601 -73.030  -12.476 1.00 27.44  ? 484 VAL   A C     1 
ATOM   3839 O O     . VAL   A 1 492 ? -10.155 -73.240  -11.354 1.00 27.01  ? 484 VAL   A O     1 
ATOM   3840 C CB    . VAL   A 1 492 ? -10.919 -74.821  -14.233 1.00 27.30  ? 484 VAL   A CB    1 
ATOM   3841 C CG1   . VAL   A 1 492 ? -9.573  -75.400  -13.810 1.00 27.41  ? 484 VAL   A CG1   1 
ATOM   3842 C CG2   . VAL   A 1 492 ? -11.832 -75.927  -14.749 1.00 27.24  ? 484 VAL   A CG2   1 
ATOM   3843 N N     . ARG   A 1 493 ? -10.282 -71.957  -13.207 1.00 27.91  ? 485 ARG   A N     1 
ATOM   3844 C CA    . ARG   A 1 493 ? -9.316  -70.967  -12.757 1.00 29.23  ? 485 ARG   A CA    1 
ATOM   3845 C C     . ARG   A 1 493 ? -9.701  -70.445  -11.373 1.00 28.77  ? 485 ARG   A C     1 
ATOM   3846 O O     . ARG   A 1 493 ? -8.834  -70.228  -10.528 1.00 28.04  ? 485 ARG   A O     1 
ATOM   3847 C CB    . ARG   A 1 493 ? -9.209  -69.838  -13.788 1.00 30.96  ? 485 ARG   A CB    1 
ATOM   3848 C CG    . ARG   A 1 493 ? -7.960  -68.985  -13.618 1.00 33.20  ? 485 ARG   A CG    1 
ATOM   3849 C CD    . ARG   A 1 493 ? -7.719  -68.053  -14.795 1.00 35.01  ? 485 ARG   A CD    1 
ATOM   3850 N NE    . ARG   A 1 493 ? -8.619  -66.895  -14.738 1.00 37.19  ? 485 ARG   A NE    1 
ATOM   3851 C CZ    . ARG   A 1 493 ? -8.262  -65.620  -14.585 1.00 38.44  ? 485 ARG   A CZ    1 
ATOM   3852 N NH1   . ARG   A 1 493 ? -6.987  -65.265  -14.569 1.00 39.03  ? 485 ARG   A NH1   1 
ATOM   3853 N NH2   . ARG   A 1 493 ? -9.197  -64.692  -14.464 1.00 38.43  ? 485 ARG   A NH2   1 
ATOM   3854 N N     . ALA   A 1 494 ? -11.011 -70.289  -11.135 1.00 28.04  ? 486 ALA   A N     1 
ATOM   3855 C CA    . ALA   A 1 494 ? -11.524 -69.770  -9.876  1.00 26.74  ? 486 ALA   A CA    1 
ATOM   3856 C C     . ALA   A 1 494 ? -11.397 -70.785  -8.742  1.00 26.60  ? 486 ALA   A C     1 
ATOM   3857 O O     . ALA   A 1 494 ? -11.825 -70.498  -7.628  1.00 26.00  ? 486 ALA   A O     1 
ATOM   3858 C CB    . ALA   A 1 494 ? -12.966 -69.350  -10.048 1.00 26.59  ? 486 ALA   A CB    1 
ATOM   3859 N N     . CYS   A 1 495 ? -10.811 -71.961  -9.011  1.00 26.69  ? 487 CYS   A N     1 
ATOM   3860 C CA    . CYS   A 1 495 ? -10.706 -73.008  -8.006  1.00 26.61  ? 487 CYS   A CA    1 
ATOM   3861 C C     . CYS   A 1 495 ? -9.349  -73.011  -7.304  1.00 27.63  ? 487 CYS   A C     1 
ATOM   3862 O O     . CYS   A 1 495 ? -8.901  -74.064  -6.856  1.00 26.97  ? 487 CYS   A O     1 
ATOM   3863 C CB    . CYS   A 1 495 ? -10.885 -74.397  -8.610  1.00 26.04  ? 487 CYS   A CB    1 
ATOM   3864 S SG    . CYS   A 1 495 ? -12.600 -74.812  -9.006  1.00 25.31  ? 487 CYS   A SG    1 
ATOM   3865 N N     A ARG   A 1 496 ? -8.692  -71.850  -7.209  0.50 28.41  ? 488 ARG   A N     1 
ATOM   3866 N N     B ARG   A 1 496 ? -8.717  -71.836  -7.191  0.50 28.77  ? 488 ARG   A N     1 
ATOM   3867 C CA    A ARG   A 1 496 ? -7.443  -71.779  -6.471  0.50 29.15  ? 488 ARG   A CA    1 
ATOM   3868 C CA    B ARG   A 1 496 ? -7.473  -71.710  -6.450  0.50 29.79  ? 488 ARG   A CA    1 
ATOM   3869 C C     A ARG   A 1 496 ? -7.761  -71.870  -4.982  0.50 30.15  ? 488 ARG   A C     1 
ATOM   3870 C C     B ARG   A 1 496 ? -7.784  -71.884  -4.967  0.50 30.50  ? 488 ARG   A C     1 
ATOM   3871 O O     A ARG   A 1 496 ? -8.791  -71.373  -4.535  0.50 30.60  ? 488 ARG   A O     1 
ATOM   3872 O O     B ARG   A 1 496 ? -8.843  -71.464  -4.508  0.50 30.90  ? 488 ARG   A O     1 
ATOM   3873 C CB    A ARG   A 1 496 ? -6.616  -70.524  -6.767  0.50 28.94  ? 488 ARG   A CB    1 
ATOM   3874 C CB    B ARG   A 1 496 ? -6.800  -70.358  -6.711  0.50 30.11  ? 488 ARG   A CB    1 
ATOM   3875 C CG    A ARG   A 1 496 ? -5.347  -70.499  -5.927  0.50 28.55  ? 488 ARG   A CG    1 
ATOM   3876 C CG    B ARG   A 1 496 ? -5.296  -70.379  -6.472  0.50 30.25  ? 488 ARG   A CG    1 
ATOM   3877 C CD    A ARG   A 1 496 ? -4.323  -69.489  -6.397  0.50 28.19  ? 488 ARG   A CD    1 
ATOM   3878 C CD    B ARG   A 1 496 ? -4.571  -69.249  -7.192  0.50 30.23  ? 488 ARG   A CD    1 
ATOM   3879 N NE    A ARG   A 1 496 ? -3.325  -69.261  -5.348  0.50 27.46  ? 488 ARG   A NE    1 
ATOM   3880 N NE    B ARG   A 1 496 ? -4.614  -67.970  -6.474  0.50 30.12  ? 488 ARG   A NE    1 
ATOM   3881 C CZ    A ARG   A 1 496 ? -3.197  -68.112  -4.706  0.50 27.15  ? 488 ARG   A CZ    1 
ATOM   3882 C CZ    B ARG   A 1 496 ? -5.156  -66.854  -6.941  0.50 29.92  ? 488 ARG   A CZ    1 
ATOM   3883 N NH1   A ARG   A 1 496 ? -2.305  -67.988  -3.742  0.50 27.14  ? 488 ARG   A NH1   1 
ATOM   3884 N NH1   B ARG   A 1 496 ? -5.049  -65.731  -6.255  0.50 29.85  ? 488 ARG   A NH1   1 
ATOM   3885 N NH2   A ARG   A 1 496 ? -3.975  -67.095  -5.028  0.50 27.05  ? 488 ARG   A NH2   1 
ATOM   3886 N NH2   B ARG   A 1 496 ? -5.783  -66.857  -8.103  0.50 30.19  ? 488 ARG   A NH2   1 
ATOM   3887 N N     . GLU   A 1 497 ? -6.867  -72.531  -4.238  1.00 31.33  ? 489 GLU   A N     1 
ATOM   3888 C CA    . GLU   A 1 497 ? -7.036  -72.758  -2.814  1.00 32.44  ? 489 GLU   A CA    1 
ATOM   3889 C C     . GLU   A 1 497 ? -5.727  -72.463  -2.091  1.00 34.19  ? 489 GLU   A C     1 
ATOM   3890 O O     . GLU   A 1 497 ? -4.644  -72.637  -2.649  1.00 34.99  ? 489 GLU   A O     1 
ATOM   3891 C CB    . GLU   A 1 497 ? -7.447  -74.201  -2.531  1.00 33.01  ? 489 GLU   A CB    1 
ATOM   3892 C CG    . GLU   A 1 497 ? -8.871  -74.524  -2.974  1.00 33.61  ? 489 GLU   A CG    1 
ATOM   3893 C CD    . GLU   A 1 497 ? -9.254  -75.979  -2.781  1.00 33.86  ? 489 GLU   A CD    1 
ATOM   3894 O OE1   . GLU   A 1 497 ? -8.466  -76.732  -2.170  1.00 33.30  ? 489 GLU   A OE1   1 
ATOM   3895 O OE2   . GLU   A 1 497 ? -10.342 -76.360  -3.259  1.00 34.91  ? 489 GLU   A OE2   1 
ATOM   3896 N N     . LYS   A 1 498 ? -5.871  -72.030  -0.835  1.00 35.28  ? 490 LYS   A N     1 
ATOM   3897 C CA    . LYS   A 1 498 ? -4.755  -71.817  0.070   1.00 35.40  ? 490 LYS   A CA    1 
ATOM   3898 C C     . LYS   A 1 498 ? -3.992  -73.129  0.242   1.00 33.16  ? 490 LYS   A C     1 
ATOM   3899 O O     . LYS   A 1 498 ? -4.566  -74.205  0.089   1.00 32.80  ? 490 LYS   A O     1 
ATOM   3900 C CB    . LYS   A 1 498 ? -5.273  -71.352  1.438   1.00 37.68  ? 490 LYS   A CB    1 
ATOM   3901 C CG    . LYS   A 1 498 ? -6.282  -70.201  1.422   1.00 40.10  ? 490 LYS   A CG    1 
ATOM   3902 C CD    . LYS   A 1 498 ? -6.577  -69.578  2.783   1.00 42.08  ? 490 LYS   A CD    1 
ATOM   3903 C CE    . LYS   A 1 498 ? -7.037  -70.557  3.826   1.00 44.64  ? 490 LYS   A CE    1 
ATOM   3904 N NZ    . LYS   A 1 498 ? -8.335  -71.165  3.519   1.00 46.14  ? 490 LYS   A NZ    1 
ATOM   3905 N N     . ASP   A 1 499 ? -2.689  -73.015  0.528   1.00 31.58  ? 491 ASP   A N     1 
ATOM   3906 C CA    . ASP   A 1 499 ? -1.884  -74.111  1.048   1.00 30.31  ? 491 ASP   A CA    1 
ATOM   3907 C C     . ASP   A 1 499 ? -1.697  -75.224  0.018   1.00 29.42  ? 491 ASP   A C     1 
ATOM   3908 O O     . ASP   A 1 499 ? -1.507  -76.377  0.400   1.00 29.76  ? 491 ASP   A O     1 
ATOM   3909 C CB    . ASP   A 1 499 ? -2.482  -74.696  2.320   1.00 30.12  ? 491 ASP   A CB    1 
ATOM   3910 C CG    . ASP   A 1 499 ? -2.767  -73.706  3.440   1.00 29.53  ? 491 ASP   A CG    1 
ATOM   3911 O OD1   . ASP   A 1 499 ? -2.403  -72.521  3.291   1.00 28.56  ? 491 ASP   A OD1   1 
ATOM   3912 O OD2   . ASP   A 1 499 ? -3.361  -74.131  4.451   1.00 29.41  ? 491 ASP   A OD2   1 
ATOM   3913 N N     . ARG   A 1 500 ? -1.745  -74.880  -1.275  1.00 27.72  ? 492 ARG   A N     1 
ATOM   3914 C CA    . ARG   A 1 500 ? -1.403  -75.817  -2.335  1.00 26.94  ? 492 ARG   A CA    1 
ATOM   3915 C C     . ARG   A 1 500 ? -0.913  -75.034  -3.549  1.00 26.82  ? 492 ARG   A C     1 
ATOM   3916 O O     . ARG   A 1 500 ? -1.021  -73.811  -3.589  1.00 26.48  ? 492 ARG   A O     1 
ATOM   3917 C CB    . ARG   A 1 500 ? -2.581  -76.726  -2.710  1.00 25.72  ? 492 ARG   A CB    1 
ATOM   3918 C CG    . ARG   A 1 500 ? -3.664  -76.081  -3.564  1.00 24.68  ? 492 ARG   A CG    1 
ATOM   3919 C CD    . ARG   A 1 500 ? -4.720  -77.079  -3.997  1.00 23.81  ? 492 ARG   A CD    1 
ATOM   3920 N NE    . ARG   A 1 500 ? -5.673  -76.492  -4.946  1.00 23.19  ? 492 ARG   A NE    1 
ATOM   3921 C CZ    . ARG   A 1 500 ? -6.758  -77.095  -5.419  1.00 21.91  ? 492 ARG   A CZ    1 
ATOM   3922 N NH1   . ARG   A 1 500 ? -7.048  -78.333  -5.059  1.00 21.68  ? 492 ARG   A NH1   1 
ATOM   3923 N NH2   . ARG   A 1 500 ? -7.559  -76.451  -6.247  1.00 21.50  ? 492 ARG   A NH2   1 
ATOM   3924 N N     . ASP   A 1 501 ? -0.390  -75.763  -4.539  1.00 27.36  ? 493 ASP   A N     1 
ATOM   3925 C CA    . ASP   A 1 501 ? 0.068   -75.169  -5.783  1.00 28.01  ? 493 ASP   A CA    1 
ATOM   3926 C C     . ASP   A 1 501 ? -1.014  -74.235  -6.323  1.00 27.70  ? 493 ASP   A C     1 
ATOM   3927 O O     . ASP   A 1 501 ? -2.180  -74.618  -6.392  1.00 27.01  ? 493 ASP   A O     1 
ATOM   3928 C CB    . ASP   A 1 501 ? 0.433   -76.237  -6.801  1.00 29.07  ? 493 ASP   A CB    1 
ATOM   3929 C CG    . ASP   A 1 501 ? 1.239   -75.753  -7.997  1.00 30.42  ? 493 ASP   A CG    1 
ATOM   3930 O OD1   . ASP   A 1 501 ? 0.782   -74.799  -8.667  1.00 30.02  ? 493 ASP   A OD1   1 
ATOM   3931 O OD2   . ASP   A 1 501 ? 2.316   -76.340  -8.250  1.00 31.61  ? 493 ASP   A OD2   1 
ATOM   3932 N N     . PRO   A 1 502 ? -0.672  -72.986  -6.719  1.00 27.77  ? 494 PRO   A N     1 
ATOM   3933 C CA    . PRO   A 1 502 ? -1.660  -72.049  -7.264  1.00 27.54  ? 494 PRO   A CA    1 
ATOM   3934 C C     . PRO   A 1 502 ? -2.342  -72.475  -8.564  1.00 27.35  ? 494 PRO   A C     1 
ATOM   3935 O O     . PRO   A 1 502 ? -3.298  -71.833  -8.990  1.00 27.26  ? 494 PRO   A O     1 
ATOM   3936 C CB    . PRO   A 1 502 ? -0.835  -70.764  -7.471  1.00 27.78  ? 494 PRO   A CB    1 
ATOM   3937 C CG    . PRO   A 1 502 ? 0.341   -70.917  -6.538  1.00 27.90  ? 494 PRO   A CG    1 
ATOM   3938 C CD    . PRO   A 1 502 ? 0.671   -72.391  -6.618  1.00 27.79  ? 494 PRO   A CD    1 
ATOM   3939 N N     . GLU   A 1 503 ? -1.837  -73.541  -9.195  1.00 27.55  ? 495 GLU   A N     1 
ATOM   3940 C CA    . GLU   A 1 503 ? -2.362  -74.009  -10.467 1.00 26.99  ? 495 GLU   A CA    1 
ATOM   3941 C C     . GLU   A 1 503 ? -2.812  -75.467  -10.379 1.00 25.50  ? 495 GLU   A C     1 
ATOM   3942 O O     . GLU   A 1 503 ? -3.046  -76.096  -11.408 1.00 25.73  ? 495 GLU   A O     1 
ATOM   3943 C CB    . GLU   A 1 503 ? -1.273  -73.816  -11.519 1.00 28.51  ? 495 GLU   A CB    1 
ATOM   3944 C CG    . GLU   A 1 503 ? -1.125  -72.362  -11.955 1.00 30.15  ? 495 GLU   A CG    1 
ATOM   3945 C CD    . GLU   A 1 503 ? 0.021   -72.091  -12.910 1.00 31.59  ? 495 GLU   A CD    1 
ATOM   3946 O OE1   . GLU   A 1 503 ? 0.866   -72.982  -13.131 1.00 33.13  ? 495 GLU   A OE1   1 
ATOM   3947 O OE2   . GLU   A 1 503 ? 0.057   -70.966  -13.444 1.00 34.42  ? 495 GLU   A OE2   1 
ATOM   3948 N N     . ALA   A 1 504 ? -2.969  -75.989  -9.155  1.00 23.61  ? 496 ALA   A N     1 
ATOM   3949 C CA    . ALA   A 1 504 ? -3.354  -77.377  -8.951  1.00 22.79  ? 496 ALA   A CA    1 
ATOM   3950 C C     . ALA   A 1 504 ? -4.702  -77.679  -9.605  1.00 21.88  ? 496 ALA   A C     1 
ATOM   3951 O O     . ALA   A 1 504 ? -4.918  -78.787  -10.091 1.00 21.11  ? 496 ALA   A O     1 
ATOM   3952 C CB    . ALA   A 1 504 ? -3.392  -77.690  -7.475  1.00 22.73  ? 496 ALA   A CB    1 
ATOM   3953 N N     . GLN   A 1 505 ? -5.598  -76.686  -9.612  1.00 21.20  ? 497 GLN   A N     1 
ATOM   3954 C CA    . GLN   A 1 505 ? -6.955  -76.852  -10.114 1.00 20.78  ? 497 GLN   A CA    1 
ATOM   3955 C C     . GLN   A 1 505 ? -6.969  -77.236  -11.594 1.00 20.50  ? 497 GLN   A C     1 
ATOM   3956 O O     . GLN   A 1 505 ? -7.943  -77.819  -12.057 1.00 20.76  ? 497 GLN   A O     1 
ATOM   3957 C CB    . GLN   A 1 505 ? -7.824  -75.611  -9.885  1.00 20.61  ? 497 GLN   A CB    1 
ATOM   3958 C CG    . GLN   A 1 505 ? -7.264  -74.306  -10.446 1.00 20.54  ? 497 GLN   A CG    1 
ATOM   3959 C CD    . GLN   A 1 505 ? -6.172  -73.693  -9.597  1.00 20.29  ? 497 GLN   A CD    1 
ATOM   3960 O OE1   . GLN   A 1 505 ? -5.700  -74.284  -8.623  1.00 20.30  ? 497 GLN   A OE1   1 
ATOM   3961 N NE2   . GLN   A 1 505 ? -5.739  -72.500  -9.969  1.00 20.75  ? 497 GLN   A NE2   1 
ATOM   3962 N N     . PHE   A 1 506 ? -5.902  -76.911  -12.334 1.00 20.24  ? 498 PHE   A N     1 
ATOM   3963 C CA    . PHE   A 1 506 ? -5.852  -77.197  -13.759 1.00 20.24  ? 498 PHE   A CA    1 
ATOM   3964 C C     . PHE   A 1 506 ? -5.259  -78.576  -14.038 1.00 20.06  ? 498 PHE   A C     1 
ATOM   3965 O O     . PHE   A 1 506 ? -5.305  -79.036  -15.178 1.00 19.92  ? 498 PHE   A O     1 
ATOM   3966 C CB    . PHE   A 1 506 ? -5.001  -76.180  -14.524 1.00 20.60  ? 498 PHE   A CB    1 
ATOM   3967 C CG    . PHE   A 1 506 ? -5.557  -74.765  -14.595 1.00 20.71  ? 498 PHE   A CG    1 
ATOM   3968 C CD1   . PHE   A 1 506 ? -6.632  -74.465  -15.422 1.00 21.24  ? 498 PHE   A CD1   1 
ATOM   3969 C CD2   . PHE   A 1 506 ? -4.967  -73.731  -13.875 1.00 20.70  ? 498 PHE   A CD2   1 
ATOM   3970 C CE1   . PHE   A 1 506 ? -7.123  -73.171  -15.504 1.00 21.36  ? 498 PHE   A CE1   1 
ATOM   3971 C CE2   . PHE   A 1 506 ? -5.460  -72.441  -13.960 1.00 20.99  ? 498 PHE   A CE2   1 
ATOM   3972 C CZ    . PHE   A 1 506 ? -6.537  -72.164  -14.772 1.00 21.39  ? 498 PHE   A CZ    1 
ATOM   3973 N N     . GLU   A 1 507 ? -4.674  -79.221  -13.022 1.00 20.06  ? 499 GLU   A N     1 
ATOM   3974 C CA    . GLU   A 1 507 ? -3.996  -80.492  -13.220 1.00 20.35  ? 499 GLU   A CA    1 
ATOM   3975 C C     . GLU   A 1 507 ? -4.793  -81.625  -12.580 1.00 20.00  ? 499 GLU   A C     1 
ATOM   3976 O O     . GLU   A 1 507 ? -4.210  -82.598  -12.102 1.00 19.72  ? 499 GLU   A O     1 
ATOM   3977 C CB    . GLU   A 1 507 ? -2.585  -80.453  -12.637 1.00 20.90  ? 499 GLU   A CB    1 
ATOM   3978 C CG    . GLU   A 1 507 ? -1.708  -79.346  -13.210 1.00 21.40  ? 499 GLU   A CG    1 
ATOM   3979 C CD    . GLU   A 1 507 ? -0.260  -79.520  -12.802 1.00 22.25  ? 499 GLU   A CD    1 
ATOM   3980 O OE1   . GLU   A 1 507 ? -0.019  -79.717  -11.595 1.00 23.98  ? 499 GLU   A OE1   1 
ATOM   3981 O OE2   . GLU   A 1 507 ? 0.625   -79.485  -13.675 1.00 23.14  ? 499 GLU   A OE2   1 
ATOM   3982 N N     . MET   A 1 508 ? -6.126  -81.495  -12.592 1.00 20.01  ? 500 MET   A N     1 
ATOM   3983 C CA    . MET   A 1 508 ? -7.011  -82.530  -12.081 1.00 20.15  ? 500 MET   A CA    1 
ATOM   3984 C C     . MET   A 1 508 ? -8.312  -82.530  -12.880 1.00 19.90  ? 500 MET   A C     1 
ATOM   3985 O O     . MET   A 1 508 ? -8.793  -81.476  -13.294 1.00 19.79  ? 500 MET   A O     1 
ATOM   3986 C CB    . MET   A 1 508 ? -7.311  -82.336  -10.588 1.00 20.07  ? 500 MET   A CB    1 
ATOM   3987 C CG    . MET   A 1 508 ? -7.670  -80.916  -10.192 1.00 20.44  ? 500 MET   A CG    1 
ATOM   3988 S SD    . MET   A 1 508 ? -7.766  -80.685  -8.405  1.00 20.94  ? 500 MET   A SD    1 
ATOM   3989 C CE    . MET   A 1 508 ? -9.443  -81.290  -8.173  1.00 21.17  ? 500 MET   A CE    1 
ATOM   3990 N N     . PRO   A 1 509 ? -8.914  -83.717  -13.118 1.00 19.78  ? 501 PRO   A N     1 
ATOM   3991 C CA    . PRO   A 1 509 ? -10.193 -83.813  -13.822 1.00 20.04  ? 501 PRO   A CA    1 
ATOM   3992 C C     . PRO   A 1 509 ? -11.392 -83.518  -12.924 1.00 20.04  ? 501 PRO   A C     1 
ATOM   3993 O O     . PRO   A 1 509 ? -11.348 -83.783  -11.728 1.00 20.24  ? 501 PRO   A O     1 
ATOM   3994 C CB    . PRO   A 1 509 ? -10.176 -85.272  -14.293 1.00 19.90  ? 501 PRO   A CB    1 
ATOM   3995 C CG    . PRO   A 1 509 ? -9.480  -85.996  -13.163 1.00 19.91  ? 501 PRO   A CG    1 
ATOM   3996 C CD    . PRO   A 1 509 ? -8.388  -85.034  -12.722 1.00 19.84  ? 501 PRO   A CD    1 
ATOM   3997 N N     . TYR   A 1 510 ? -12.457 -82.979  -13.525 1.00 19.96  ? 502 TYR   A N     1 
ATOM   3998 C CA    . TYR   A 1 510 ? -13.702 -82.701  -12.831 1.00 19.50  ? 502 TYR   A CA    1 
ATOM   3999 C C     . TYR   A 1 510 ? -14.840 -83.438  -13.525 1.00 20.02  ? 502 TYR   A C     1 
ATOM   4000 O O     . TYR   A 1 510 ? -14.841 -83.565  -14.746 1.00 20.80  ? 502 TYR   A O     1 
ATOM   4001 C CB    . TYR   A 1 510 ? -13.998 -81.200  -12.843 1.00 19.10  ? 502 TYR   A CB    1 
ATOM   4002 C CG    . TYR   A 1 510 ? -12.923 -80.345  -12.192 1.00 18.61  ? 502 TYR   A CG    1 
ATOM   4003 C CD1   . TYR   A 1 510 ? -11.812 -79.925  -12.915 1.00 18.45  ? 502 TYR   A CD1   1 
ATOM   4004 C CD2   . TYR   A 1 510 ? -13.018 -79.958  -10.860 1.00 18.08  ? 502 TYR   A CD2   1 
ATOM   4005 C CE1   . TYR   A 1 510 ? -10.827 -79.146  -12.332 1.00 18.25  ? 502 TYR   A CE1   1 
ATOM   4006 C CE2   . TYR   A 1 510 ? -12.038 -79.182  -10.266 1.00 17.93  ? 502 TYR   A CE2   1 
ATOM   4007 C CZ    . TYR   A 1 510 ? -10.942 -78.774  -11.005 1.00 18.01  ? 502 TYR   A CZ    1 
ATOM   4008 O OH    . TYR   A 1 510 ? -9.974  -78.011  -10.431 1.00 18.11  ? 502 TYR   A OH    1 
ATOM   4009 N N     . VAL   A 1 511 ? -15.809 -83.910  -12.737 1.00 20.52  ? 503 VAL   A N     1 
ATOM   4010 C CA    . VAL   A 1 511 ? -17.086 -84.353  -13.269 1.00 21.05  ? 503 VAL   A CA    1 
ATOM   4011 C C     . VAL   A 1 511 ? -17.962 -83.114  -13.427 1.00 22.00  ? 503 VAL   A C     1 
ATOM   4012 O O     . VAL   A 1 511 ? -17.990 -82.257  -12.544 1.00 22.11  ? 503 VAL   A O     1 
ATOM   4013 C CB    . VAL   A 1 511 ? -17.762 -85.415  -12.380 1.00 20.76  ? 503 VAL   A CB    1 
ATOM   4014 C CG1   . VAL   A 1 511 ? -19.216 -85.646  -12.771 1.00 20.91  ? 503 VAL   A CG1   1 
ATOM   4015 C CG2   . VAL   A 1 511 ? -16.998 -86.733  -12.394 1.00 20.48  ? 503 VAL   A CG2   1 
ATOM   4016 N N     . VAL   A 1 512 ? -18.669 -83.028  -14.559 1.00 22.93  ? 504 VAL   A N     1 
ATOM   4017 C CA    . VAL   A 1 512 ? -19.429 -81.836  -14.893 1.00 23.79  ? 504 VAL   A CA    1 
ATOM   4018 C C     . VAL   A 1 512 ? -20.399 -82.157  -16.027 1.00 25.34  ? 504 VAL   A C     1 
ATOM   4019 O O     . VAL   A 1 512 ? -20.028 -82.814  -16.997 1.00 24.52  ? 504 VAL   A O     1 
ATOM   4020 C CB    . VAL   A 1 512 ? -18.477 -80.677  -15.260 1.00 23.62  ? 504 VAL   A CB    1 
ATOM   4021 C CG1   . VAL   A 1 512 ? -17.409 -81.099  -16.261 1.00 23.72  ? 504 VAL   A CG1   1 
ATOM   4022 C CG2   . VAL   A 1 512 ? -19.220 -79.444  -15.763 1.00 23.66  ? 504 VAL   A CG2   1 
ATOM   4023 N N     . ARG   A 1 513 ? -21.648 -81.694  -15.882 1.00 27.16  ? 505 ARG   A N     1 
ATOM   4024 C CA    . ARG   A 1 513 ? -22.590 -81.655  -16.989 1.00 28.36  ? 505 ARG   A CA    1 
ATOM   4025 C C     . ARG   A 1 513 ? -22.176 -80.509  -17.908 1.00 27.99  ? 505 ARG   A C     1 
ATOM   4026 O O     . ARG   A 1 513 ? -22.649 -79.385  -17.759 1.00 28.65  ? 505 ARG   A O     1 
ATOM   4027 C CB    . ARG   A 1 513 ? -24.030 -81.522  -16.472 1.00 29.91  ? 505 ARG   A CB    1 
ATOM   4028 C CG    . ARG   A 1 513 ? -25.113 -81.204  -17.499 1.00 31.42  ? 505 ARG   A CG    1 
ATOM   4029 C CD    . ARG   A 1 513 ? -25.303 -82.252  -18.587 1.00 32.35  ? 505 ARG   A CD    1 
ATOM   4030 N NE    . ARG   A 1 513 ? -24.342 -82.115  -19.691 1.00 32.46  ? 505 ARG   A NE    1 
ATOM   4031 C CZ    . ARG   A 1 513 ? -23.663 -83.097  -20.290 1.00 32.40  ? 505 ARG   A CZ    1 
ATOM   4032 N NH1   . ARG   A 1 513 ? -22.798 -82.812  -21.249 1.00 32.59  ? 505 ARG   A NH1   1 
ATOM   4033 N NH2   . ARG   A 1 513 ? -23.842 -84.358  -19.943 1.00 32.33  ? 505 ARG   A NH2   1 
ATOM   4034 N N     . LEU   A 1 514 ? -21.262 -80.803  -18.838 1.00 28.01  ? 506 LEU   A N     1 
ATOM   4035 C CA    . LEU   A 1 514 ? -20.820 -79.827  -19.821 1.00 28.60  ? 506 LEU   A CA    1 
ATOM   4036 C C     . LEU   A 1 514 ? -22.057 -79.261  -20.510 1.00 29.21  ? 506 LEU   A C     1 
ATOM   4037 O O     . LEU   A 1 514 ? -22.919 -80.022  -20.940 1.00 29.64  ? 506 LEU   A O     1 
ATOM   4038 C CB    . LEU   A 1 514 ? -19.882 -80.464  -20.847 1.00 28.30  ? 506 LEU   A CB    1 
ATOM   4039 C CG    . LEU   A 1 514 ? -18.651 -81.199  -20.306 1.00 28.08  ? 506 LEU   A CG    1 
ATOM   4040 C CD1   . LEU   A 1 514 ? -18.041 -82.047  -21.408 1.00 28.62  ? 506 LEU   A CD1   1 
ATOM   4041 C CD2   . LEU   A 1 514 ? -17.623 -80.239  -19.744 1.00 27.96  ? 506 LEU   A CD2   1 
ATOM   4042 N N     . HIS   A 1 515 ? -22.141 -77.932  -20.611 1.00 30.04  ? 507 HIS   A N     1 
ATOM   4043 C CA    . HIS   A 1 515 ? -23.341 -77.300  -21.135 1.00 30.88  ? 507 HIS   A CA    1 
ATOM   4044 C C     . HIS   A 1 515 ? -22.962 -76.176  -22.098 1.00 30.84  ? 507 HIS   A C     1 
ATOM   4045 O O     . HIS   A 1 515 ? -23.191 -76.298  -23.298 1.00 30.55  ? 507 HIS   A O     1 
ATOM   4046 C CB    . HIS   A 1 515 ? -24.256 -76.887  -19.977 1.00 31.97  ? 507 HIS   A CB    1 
ATOM   4047 C CG    . HIS   A 1 515 ? -25.535 -76.269  -20.421 1.00 32.75  ? 507 HIS   A CG    1 
ATOM   4048 N ND1   . HIS   A 1 515 ? -26.556 -77.008  -20.976 1.00 33.60  ? 507 HIS   A ND1   1 
ATOM   4049 C CD2   . HIS   A 1 515 ? -25.947 -74.997  -20.422 1.00 33.42  ? 507 HIS   A CD2   1 
ATOM   4050 C CE1   . HIS   A 1 515 ? -27.557 -76.198  -21.286 1.00 34.25  ? 507 HIS   A CE1   1 
ATOM   4051 N NE2   . HIS   A 1 515 ? -27.209 -74.973  -20.957 1.00 34.33  ? 507 HIS   A NE2   1 
ATOM   4052 N N     . ASN   A 1 516 ? -22.396 -75.083  -21.573 1.00 31.25  ? 508 ASN   A N     1 
ATOM   4053 C CA    . ASN   A 1 516 ? -21.930 -73.998  -22.421 1.00 31.59  ? 508 ASN   A CA    1 
ATOM   4054 C C     . ASN   A 1 516 ? -20.518 -74.322  -22.902 1.00 30.33  ? 508 ASN   A C     1 
ATOM   4055 O O     . ASN   A 1 516 ? -19.537 -73.952  -22.258 1.00 30.47  ? 508 ASN   A O     1 
ATOM   4056 C CB    . ASN   A 1 516 ? -21.974 -72.643  -21.721 1.00 32.61  ? 508 ASN   A CB    1 
ATOM   4057 C CG    . ASN   A 1 516 ? -21.650 -71.515  -22.674 1.00 33.33  ? 508 ASN   A CG    1 
ATOM   4058 O OD1   . ASN   A 1 516 ? -21.644 -71.717  -23.894 1.00 34.50  ? 508 ASN   A OD1   1 
ATOM   4059 N ND2   . ASN   A 1 516 ? -21.394 -70.325  -22.154 1.00 33.91  ? 508 ASN   A ND2   1 
ATOM   4060 N N     . PHE   A 1 517 ? -20.429 -75.017  -24.040 1.00 29.32  ? 509 PHE   A N     1 
ATOM   4061 C CA    . PHE   A 1 517 ? -19.145 -75.430  -24.581 1.00 28.35  ? 509 PHE   A CA    1 
ATOM   4062 C C     . PHE   A 1 517 ? -19.296 -75.770  -26.062 1.00 27.92  ? 509 PHE   A C     1 
ATOM   4063 O O     . PHE   A 1 517 ? -20.404 -75.805  -26.593 1.00 28.34  ? 509 PHE   A O     1 
ATOM   4064 C CB    . PHE   A 1 517 ? -18.612 -76.626  -23.786 1.00 27.70  ? 509 PHE   A CB    1 
ATOM   4065 C CG    . PHE   A 1 517 ? -19.181 -77.970  -24.218 1.00 26.81  ? 509 PHE   A CG    1 
ATOM   4066 C CD1   . PHE   A 1 517 ? -20.464 -78.354  -23.851 1.00 26.69  ? 509 PHE   A CD1   1 
ATOM   4067 C CD2   . PHE   A 1 517 ? -18.424 -78.848  -24.986 1.00 26.81  ? 509 PHE   A CD2   1 
ATOM   4068 C CE1   . PHE   A 1 517 ? -20.979 -79.577  -24.250 1.00 26.75  ? 509 PHE   A CE1   1 
ATOM   4069 C CE2   . PHE   A 1 517 ? -18.942 -80.072  -25.381 1.00 26.83  ? 509 PHE   A CE2   1 
ATOM   4070 C CZ    . PHE   A 1 517 ? -20.217 -80.434  -25.011 1.00 26.86  ? 509 PHE   A CZ    1 
ATOM   4071 N N     . HIS   A 1 518 ? -18.157 -76.035  -26.707 1.00 27.06  ? 510 HIS   A N     1 
ATOM   4072 C CA    . HIS   A 1 518 ? -18.116 -76.369  -28.119 1.00 26.90  ? 510 HIS   A CA    1 
ATOM   4073 C C     . HIS   A 1 518 ? -17.141 -77.525  -28.320 1.00 26.22  ? 510 HIS   A C     1 
ATOM   4074 O O     . HIS   A 1 518 ? -15.952 -77.378  -28.046 1.00 25.95  ? 510 HIS   A O     1 
ATOM   4075 C CB    . HIS   A 1 518 ? -17.687 -75.136  -28.923 1.00 27.26  ? 510 HIS   A CB    1 
ATOM   4076 C CG    . HIS   A 1 518 ? -17.789 -75.282  -30.402 1.00 27.61  ? 510 HIS   A CG    1 
ATOM   4077 N ND1   . HIS   A 1 518 ? -17.085 -74.466  -31.260 1.00 27.62  ? 510 HIS   A ND1   1 
ATOM   4078 C CD2   . HIS   A 1 518 ? -18.504 -76.111  -31.176 1.00 27.88  ? 510 HIS   A CD2   1 
ATOM   4079 C CE1   . HIS   A 1 518 ? -17.368 -74.805  -32.510 1.00 27.79  ? 510 HIS   A CE1   1 
ATOM   4080 N NE2   . HIS   A 1 518 ? -18.228 -75.801  -32.481 1.00 27.96  ? 510 HIS   A NE2   1 
ATOM   4081 N N     A GLN   A 1 519 ? -17.645 -78.660  -28.819 0.50 26.00  ? 511 GLN   A N     1 
ATOM   4082 N N     B GLN   A 1 519 ? -17.667 -78.680  -28.754 0.50 25.52  ? 511 GLN   A N     1 
ATOM   4083 C CA    A GLN   A 1 519 ? -16.791 -79.798  -29.117 0.50 25.57  ? 511 GLN   A CA    1 
ATOM   4084 C CA    B GLN   A 1 519 ? -16.837 -79.798  -29.171 0.50 24.76  ? 511 GLN   A CA    1 
ATOM   4085 C C     A GLN   A 1 519 ? -16.119 -79.549  -30.466 0.50 25.09  ? 511 GLN   A C     1 
ATOM   4086 C C     B GLN   A 1 519 ? -16.099 -79.400  -30.444 0.50 24.68  ? 511 GLN   A C     1 
ATOM   4087 O O     A GLN   A 1 519 ? -16.793 -79.291  -31.459 0.50 25.20  ? 511 GLN   A O     1 
ATOM   4088 O O     B GLN   A 1 519 ? -16.710 -78.866  -31.365 0.50 24.86  ? 511 GLN   A O     1 
ATOM   4089 C CB    A GLN   A 1 519 ? -17.589 -81.101  -29.069 0.50 25.70  ? 511 GLN   A CB    1 
ATOM   4090 C CB    B GLN   A 1 519 ? -17.664 -81.053  -29.445 0.50 24.23  ? 511 GLN   A CB    1 
ATOM   4091 C CG    A GLN   A 1 519 ? -16.789 -82.285  -28.536 0.50 25.70  ? 511 GLN   A CG    1 
ATOM   4092 C CG    B GLN   A 1 519 ? -16.921 -82.105  -30.262 0.50 23.63  ? 511 GLN   A CG    1 
ATOM   4093 C CD    A GLN   A 1 519 ? -17.654 -83.466  -28.154 0.50 25.63  ? 511 GLN   A CD    1 
ATOM   4094 C CD    B GLN   A 1 519 ? -17.739 -83.352  -30.514 0.50 23.13  ? 511 GLN   A CD    1 
ATOM   4095 O OE1   A GLN   A 1 519 ? -17.881 -83.739  -26.970 0.50 25.68  ? 511 GLN   A OE1   1 
ATOM   4096 O OE1   B GLN   A 1 519 ? -18.070 -83.691  -31.657 0.50 22.39  ? 511 GLN   A OE1   1 
ATOM   4097 N NE2   A GLN   A 1 519 ? -18.155 -84.172  -29.156 0.50 25.64  ? 511 GLN   A NE2   1 
ATOM   4098 N NE2   B GLN   A 1 519 ? -18.071 -84.052  -29.440 0.50 23.09  ? 511 GLN   A NE2   1 
ATOM   4099 N N     . LEU   A 1 520 ? -14.784 -79.647  -30.477 1.00 24.72  ? 512 LEU   A N     1 
ATOM   4100 C CA    . LEU   A 1 520 ? -13.955 -79.189  -31.580 1.00 24.41  ? 512 LEU   A CA    1 
ATOM   4101 C C     . LEU   A 1 520 ? -13.629 -80.324  -32.549 1.00 24.38  ? 512 LEU   A C     1 
ATOM   4102 O O     . LEU   A 1 520 ? -13.152 -80.061  -33.650 1.00 23.84  ? 512 LEU   A O     1 
ATOM   4103 C CB    . LEU   A 1 520 ? -12.683 -78.572  -31.003 1.00 24.27  ? 512 LEU   A CB    1 
ATOM   4104 C CG    . LEU   A 1 520 ? -12.879 -77.387  -30.052 1.00 24.54  ? 512 LEU   A CG    1 
ATOM   4105 C CD1   . LEU   A 1 520 ? -11.525 -76.865  -29.609 1.00 24.58  ? 512 LEU   A CD1   1 
ATOM   4106 C CD2   . LEU   A 1 520 ? -13.713 -76.273  -30.668 1.00 24.75  ? 512 LEU   A CD2   1 
ATOM   4107 N N     . SER   A 1 521 ? -13.861 -81.574  -32.132 1.00 24.24  ? 513 SER   A N     1 
ATOM   4108 C CA    . SER   A 1 521 ? -13.652 -82.721  -33.002 1.00 24.21  ? 513 SER   A CA    1 
ATOM   4109 C C     . SER   A 1 521 ? -14.335 -83.947  -32.404 1.00 24.63  ? 513 SER   A C     1 
ATOM   4110 O O     . SER   A 1 521 ? -14.618 -83.980  -31.210 1.00 25.19  ? 513 SER   A O     1 
ATOM   4111 C CB    . SER   A 1 521 ? -12.184 -82.975  -33.235 1.00 24.31  ? 513 SER   A CB    1 
ATOM   4112 O OG    . SER   A 1 521 ? -11.987 -84.179  -33.964 1.00 23.91  ? 513 SER   A OG    1 
ATOM   4113 N N     . ALA   A 1 522 ? -14.576 -84.957  -33.244 1.00 24.50  ? 514 ALA   A N     1 
ATOM   4114 C CA    . ALA   A 1 522 ? -15.338 -86.128  -32.838 1.00 24.65  ? 514 ALA   A CA    1 
ATOM   4115 C C     . ALA   A 1 522 ? -14.587 -86.890  -31.750 1.00 24.65  ? 514 ALA   A C     1 
ATOM   4116 O O     . ALA   A 1 522 ? -13.371 -87.049  -31.838 1.00 25.17  ? 514 ALA   A O     1 
ATOM   4117 C CB    . ALA   A 1 522 ? -15.601 -87.014  -34.037 1.00 24.54  ? 514 ALA   A CB    1 
ATOM   4118 N N     . PRO   A 1 523 ? -15.274 -87.400  -30.700 1.00 24.41  ? 515 PRO   A N     1 
ATOM   4119 C CA    . PRO   A 1 523 ? -14.606 -88.206  -29.678 1.00 24.03  ? 515 PRO   A CA    1 
ATOM   4120 C C     . PRO   A 1 523 ? -13.835 -89.363  -30.305 1.00 24.02  ? 515 PRO   A C     1 
ATOM   4121 O O     . PRO   A 1 523 ? -14.214 -89.861  -31.361 1.00 24.57  ? 515 PRO   A O     1 
ATOM   4122 C CB    . PRO   A 1 523 ? -15.748 -88.690  -28.775 1.00 23.93  ? 515 PRO   A CB    1 
ATOM   4123 C CG    . PRO   A 1 523 ? -16.827 -87.652  -28.971 1.00 24.48  ? 515 PRO   A CG    1 
ATOM   4124 C CD    . PRO   A 1 523 ? -16.710 -87.223  -30.429 1.00 24.31  ? 515 PRO   A CD    1 
ATOM   4125 N N     . GLN   A 1 524 ? -12.746 -89.770  -29.648 1.00 23.56  ? 516 GLN   A N     1 
ATOM   4126 C CA    . GLN   A 1 524 ? -11.964 -90.909  -30.095 1.00 23.13  ? 516 GLN   A CA    1 
ATOM   4127 C C     . GLN   A 1 524 ? -11.592 -91.773  -28.897 1.00 23.28  ? 516 GLN   A C     1 
ATOM   4128 O O     . GLN   A 1 524 ? -11.383 -91.258  -27.798 1.00 23.13  ? 516 GLN   A O     1 
ATOM   4129 C CB    . GLN   A 1 524 ? -10.679 -90.475  -30.796 1.00 22.93  ? 516 GLN   A CB    1 
ATOM   4130 C CG    . GLN   A 1 524 ? -10.892 -89.809  -32.149 1.00 22.50  ? 516 GLN   A CG    1 
ATOM   4131 C CD    . GLN   A 1 524 ? -9.583  -89.517  -32.849 1.00 22.02  ? 516 GLN   A CD    1 
ATOM   4132 O OE1   . GLN   A 1 524 ? -8.687  -90.365  -32.901 1.00 21.86  ? 516 GLN   A OE1   1 
ATOM   4133 N NE2   . GLN   A 1 524 ? -9.443  -88.306  -33.369 1.00 21.73  ? 516 GLN   A NE2   1 
ATOM   4134 N N     . PRO   A 1 525 ? -11.466 -93.106  -29.086 1.00 23.00  ? 517 PRO   A N     1 
ATOM   4135 C CA    . PRO   A 1 525 ? -11.141 -94.010  -27.985 1.00 22.99  ? 517 PRO   A CA    1 
ATOM   4136 C C     . PRO   A 1 525 ? -9.778  -93.659  -27.399 1.00 22.98  ? 517 PRO   A C     1 
ATOM   4137 O O     . PRO   A 1 525 ? -8.863  -93.288  -28.132 1.00 22.69  ? 517 PRO   A O     1 
ATOM   4138 C CB    . PRO   A 1 525 ? -11.174 -95.406  -28.627 1.00 23.21  ? 517 PRO   A CB    1 
ATOM   4139 C CG    . PRO   A 1 525 ? -10.936 -95.144  -30.099 1.00 23.18  ? 517 PRO   A CG    1 
ATOM   4140 C CD    . PRO   A 1 525 ? -11.592 -93.805  -30.374 1.00 23.01  ? 517 PRO   A CD    1 
ATOM   4141 N N     . CYS   A 1 526 ? -9.666  -93.773  -26.071 1.00 22.76  ? 518 CYS   A N     1 
ATOM   4142 C CA    . CYS   A 1 526 ? -8.448  -93.416  -25.364 1.00 22.83  ? 518 CYS   A CA    1 
ATOM   4143 C C     . CYS   A 1 526 ? -7.838  -94.678  -24.754 1.00 23.19  ? 518 CYS   A C     1 
ATOM   4144 O O     . CYS   A 1 526 ? -6.796  -95.138  -25.218 1.00 23.34  ? 518 CYS   A O     1 
ATOM   4145 C CB    . CYS   A 1 526 ? -8.730  -92.301  -24.362 1.00 22.77  ? 518 CYS   A CB    1 
ATOM   4146 S SG    . CYS   A 1 526 ? -7.278  -91.792  -23.407 1.00 22.61  ? 518 CYS   A SG    1 
ATOM   4147 N N     . PHE   A 1 527 ? -8.506  -95.246  -23.739 1.00 23.17  ? 519 PHE   A N     1 
ATOM   4148 C CA    . PHE   A 1 527 ? -8.013  -96.431  -23.051 1.00 23.36  ? 519 PHE   A CA    1 
ATOM   4149 C C     . PHE   A 1 527 ? -9.110  -97.489  -22.995 1.00 23.18  ? 519 PHE   A C     1 
ATOM   4150 O O     . PHE   A 1 527 ? -10.286 -97.160  -22.850 1.00 23.13  ? 519 PHE   A O     1 
ATOM   4151 C CB    . PHE   A 1 527 ? -7.561  -96.134  -21.617 1.00 23.57  ? 519 PHE   A CB    1 
ATOM   4152 C CG    . PHE   A 1 527 ? -6.434  -95.122  -21.472 1.00 23.71  ? 519 PHE   A CG    1 
ATOM   4153 C CD1   . PHE   A 1 527 ? -5.351  -95.115  -22.346 1.00 24.21  ? 519 PHE   A CD1   1 
ATOM   4154 C CD2   . PHE   A 1 527 ? -6.469  -94.171  -20.460 1.00 24.00  ? 519 PHE   A CD2   1 
ATOM   4155 C CE1   . PHE   A 1 527 ? -4.334  -94.182  -22.204 1.00 24.31  ? 519 PHE   A CE1   1 
ATOM   4156 C CE2   . PHE   A 1 527 ? -5.449  -93.243  -20.321 1.00 24.34  ? 519 PHE   A CE2   1 
ATOM   4157 C CZ    . PHE   A 1 527 ? -4.384  -93.251  -21.192 1.00 24.40  ? 519 PHE   A CZ    1 
ATOM   4158 N N     . THR   A 1 528 ? -8.693  -98.759  -23.077 1.00 22.94  ? 520 THR   A N     1 
ATOM   4159 C CA    . THR   A 1 528 ? -9.605  -99.892  -23.088 1.00 22.96  ? 520 THR   A CA    1 
ATOM   4160 C C     . THR   A 1 528 ? -9.101  -100.944 -22.106 1.00 22.91  ? 520 THR   A C     1 
ATOM   4161 O O     . THR   A 1 528 ? -7.900  -101.189 -22.017 1.00 22.52  ? 520 THR   A O     1 
ATOM   4162 C CB    . THR   A 1 528 ? -9.706  -100.455 -24.507 1.00 22.59  ? 520 THR   A CB    1 
ATOM   4163 O OG1   . THR   A 1 528 ? -10.264 -99.406  -25.290 1.00 22.54  ? 520 THR   A OG1   1 
ATOM   4164 C CG2   . THR   A 1 528 ? -10.589 -101.687 -24.600 1.00 22.33  ? 520 THR   A CG2   1 
ATOM   4165 N N     . PHE   A 1 529 ? -10.039 -101.557 -21.378 1.00 23.71  ? 521 PHE   A N     1 
ATOM   4166 C CA    . PHE   A 1 529 ? -9.754  -102.691 -20.515 1.00 24.71  ? 521 PHE   A CA    1 
ATOM   4167 C C     . PHE   A 1 529 ? -10.797 -103.768 -20.782 1.00 25.90  ? 521 PHE   A C     1 
ATOM   4168 O O     . PHE   A 1 529 ? -11.939 -103.453 -21.107 1.00 25.46  ? 521 PHE   A O     1 
ATOM   4169 C CB    . PHE   A 1 529 ? -9.777  -102.292 -19.035 1.00 24.87  ? 521 PHE   A CB    1 
ATOM   4170 C CG    . PHE   A 1 529 ? -8.628  -101.380 -18.635 1.00 24.56  ? 521 PHE   A CG    1 
ATOM   4171 C CD1   . PHE   A 1 529 ? -8.718  -100.003 -18.810 1.00 24.49  ? 521 PHE   A CD1   1 
ATOM   4172 C CD2   . PHE   A 1 529 ? -7.455  -101.906 -18.106 1.00 24.19  ? 521 PHE   A CD2   1 
ATOM   4173 C CE1   . PHE   A 1 529 ? -7.661  -99.177  -18.460 1.00 24.40  ? 521 PHE   A CE1   1 
ATOM   4174 C CE2   . PHE   A 1 529 ? -6.401  -101.076 -17.765 1.00 24.21  ? 521 PHE   A CE2   1 
ATOM   4175 C CZ    . PHE   A 1 529 ? -6.506  -99.715  -17.941 1.00 24.36  ? 521 PHE   A CZ    1 
ATOM   4176 N N     . SER   A 1 530 ? -10.385 -105.032 -20.637 1.00 28.01  ? 522 SER   A N     1 
ATOM   4177 C CA    . SER   A 1 530 ? -11.292 -106.162 -20.753 1.00 29.57  ? 522 SER   A CA    1 
ATOM   4178 C C     . SER   A 1 530 ? -11.060 -107.127 -19.592 1.00 29.29  ? 522 SER   A C     1 
ATOM   4179 O O     . SER   A 1 530 ? -9.939  -107.257 -19.104 1.00 28.34  ? 522 SER   A O     1 
ATOM   4180 C CB    . SER   A 1 530 ? -11.143 -106.833 -22.096 1.00 30.70  ? 522 SER   A CB    1 
ATOM   4181 O OG    . SER   A 1 530 ? -9.774  -107.057 -22.408 1.00 31.99  ? 522 SER   A OG    1 
ATOM   4182 N N     . HIS   A 1 531 ? -12.141 -107.782 -19.150 1.00 31.24  ? 523 HIS   A N     1 
ATOM   4183 C CA    . HIS   A 1 531 ? -12.120 -108.645 -17.978 1.00 33.64  ? 523 HIS   A CA    1 
ATOM   4184 C C     . HIS   A 1 531 ? -12.867 -109.943 -18.280 1.00 35.20  ? 523 HIS   A C     1 
ATOM   4185 O O     . HIS   A 1 531 ? -13.940 -109.905 -18.878 1.00 34.74  ? 523 HIS   A O     1 
ATOM   4186 C CB    . HIS   A 1 531 ? -12.726 -107.929 -16.763 1.00 33.13  ? 523 HIS   A CB    1 
ATOM   4187 C CG    . HIS   A 1 531 ? -11.982 -106.698 -16.363 1.00 32.85  ? 523 HIS   A CG    1 
ATOM   4188 N ND1   . HIS   A 1 531 ? -10.758 -106.749 -15.733 1.00 32.74  ? 523 HIS   A ND1   1 
ATOM   4189 C CD2   . HIS   A 1 531 ? -12.259 -105.398 -16.534 1.00 32.57  ? 523 HIS   A CD2   1 
ATOM   4190 C CE1   . HIS   A 1 531 ? -10.326 -105.513 -15.522 1.00 32.57  ? 523 HIS   A CE1   1 
ATOM   4191 N NE2   . HIS   A 1 531 ? -11.224 -104.677 -15.997 1.00 32.10  ? 523 HIS   A NE2   1 
ATOM   4192 N N     . PRO   A 1 532 ? -12.347 -111.130 -17.880 1.00 38.77  ? 524 PRO   A N     1 
ATOM   4193 C CA    . PRO   A 1 532 ? -11.030 -111.257 -17.249 1.00 40.74  ? 524 PRO   A CA    1 
ATOM   4194 C C     . PRO   A 1 532 ? -9.871  -110.959 -18.195 1.00 42.92  ? 524 PRO   A C     1 
ATOM   4195 O O     . PRO   A 1 532 ? -10.015 -111.054 -19.411 1.00 43.07  ? 524 PRO   A O     1 
ATOM   4196 C CB    . PRO   A 1 532 ? -11.017 -112.723 -16.781 1.00 40.37  ? 524 PRO   A CB    1 
ATOM   4197 C CG    . PRO   A 1 532 ? -11.917 -113.424 -17.767 1.00 39.86  ? 524 PRO   A CG    1 
ATOM   4198 C CD    . PRO   A 1 532 ? -13.039 -112.425 -17.987 1.00 39.65  ? 524 PRO   A CD    1 
ATOM   4199 N N     . ASN   A 1 533 ? -8.725  -110.605 -17.606 1.00 47.01  ? 525 ASN   A N     1 
ATOM   4200 C CA    . ASN   A 1 533 ? -7.526  -110.276 -18.355 1.00 52.22  ? 525 ASN   A CA    1 
ATOM   4201 C C     . ASN   A 1 533 ? -6.536  -111.428 -18.198 1.00 58.29  ? 525 ASN   A C     1 
ATOM   4202 O O     . ASN   A 1 533 ? -5.905  -111.573 -17.154 1.00 58.27  ? 525 ASN   A O     1 
ATOM   4203 C CB    . ASN   A 1 533 ? -6.977  -108.924 -17.912 1.00 52.91  ? 525 ASN   A CB    1 
ATOM   4204 C CG    . ASN   A 1 533 ? -5.672  -108.570 -18.585 1.00 53.21  ? 525 ASN   A CG    1 
ATOM   4205 O OD1   . ASN   A 1 533 ? -5.216  -109.284 -19.483 1.00 52.69  ? 525 ASN   A OD1   1 
ATOM   4206 N ND2   . ASN   A 1 533 ? -5.057  -107.474 -18.167 1.00 55.24  ? 525 ASN   A ND2   1 
ATOM   4207 N N     . ARG   A 1 534 ? -6.399  -112.229 -19.263 1.00 65.94  ? 526 ARG   A N     1 
ATOM   4208 C CA    . ARG   A 1 534 ? -5.657  -113.480 -19.222 1.00 71.43  ? 526 ARG   A CA    1 
ATOM   4209 C C     . ARG   A 1 534 ? -4.149  -113.234 -19.240 1.00 74.05  ? 526 ARG   A C     1 
ATOM   4210 O O     . ARG   A 1 534 ? -3.379  -114.140 -18.924 1.00 76.23  ? 526 ARG   A O     1 
ATOM   4211 C CB    . ARG   A 1 534 ? -6.057  -114.354 -20.417 1.00 74.06  ? 526 ARG   A CB    1 
ATOM   4212 C CG    . ARG   A 1 534 ? -7.529  -114.739 -20.459 1.00 76.35  ? 526 ARG   A CG    1 
ATOM   4213 C CD    . ARG   A 1 534 ? -7.967  -115.398 -19.158 1.00 78.86  ? 526 ARG   A CD    1 
ATOM   4214 N NE    . ARG   A 1 534 ? -9.340  -115.914 -19.177 1.00 81.03  ? 526 ARG   A NE    1 
ATOM   4215 C CZ    . ARG   A 1 534 ? -9.948  -116.486 -18.138 1.00 80.88  ? 526 ARG   A CZ    1 
ATOM   4216 N NH1   . ARG   A 1 534 ? -9.308  -116.642 -16.989 1.00 81.47  ? 526 ARG   A NH1   1 
ATOM   4217 N NH2   . ARG   A 1 534 ? -11.198 -116.902 -18.251 1.00 79.83  ? 526 ARG   A NH2   1 
ATOM   4218 N N     . ASP   A 1 535 ? -3.742  -112.015 -19.613 1.00 73.59  ? 527 ASP   A N     1 
ATOM   4219 C CA    . ASP   A 1 535 ? -2.339  -111.665 -19.768 1.00 74.58  ? 527 ASP   A CA    1 
ATOM   4220 C C     . ASP   A 1 535 ? -1.550  -112.168 -18.559 1.00 74.78  ? 527 ASP   A C     1 
ATOM   4221 O O     . ASP   A 1 535 ? -1.960  -111.939 -17.423 1.00 74.65  ? 527 ASP   A O     1 
ATOM   4222 C CB    . ASP   A 1 535 ? -2.190  -110.162 -19.952 1.00 76.78  ? 527 ASP   A CB    1 
ATOM   4223 C CG    . ASP   A 1 535 ? -0.951  -109.683 -20.697 1.00 79.18  ? 527 ASP   A CG    1 
ATOM   4224 O OD1   . ASP   A 1 535 ? -0.161  -110.535 -21.148 1.00 80.10  ? 527 ASP   A OD1   1 
ATOM   4225 O OD2   . ASP   A 1 535 ? -0.795  -108.451 -20.833 1.00 80.27  ? 527 ASP   A OD2   1 
ATOM   4226 N N     . PRO   A 1 536 ? -0.415  -112.886 -18.753 1.00 75.23  ? 528 PRO   A N     1 
ATOM   4227 C CA    . PRO   A 1 536 ? 0.421   -113.316 -17.629 1.00 74.12  ? 528 PRO   A CA    1 
ATOM   4228 C C     . PRO   A 1 536 ? 1.063   -112.125 -16.921 1.00 72.51  ? 528 PRO   A C     1 
ATOM   4229 O O     . PRO   A 1 536 ? 1.118   -112.089 -15.694 1.00 71.76  ? 528 PRO   A O     1 
ATOM   4230 C CB    . PRO   A 1 536 ? 1.462   -114.256 -18.272 1.00 74.81  ? 528 PRO   A CB    1 
ATOM   4231 C CG    . PRO   A 1 536 ? 1.523   -113.817 -19.719 1.00 74.57  ? 528 PRO   A CG    1 
ATOM   4232 C CD    . PRO   A 1 536 ? 0.120   -113.333 -20.050 1.00 75.01  ? 528 PRO   A CD    1 
ATOM   4233 N N     . MET   A 1 537 ? 1.546   -111.162 -17.717 1.00 71.79  ? 529 MET   A N     1 
ATOM   4234 C CA    . MET   A 1 537 ? 2.075   -109.909 -17.204 1.00 70.59  ? 529 MET   A CA    1 
ATOM   4235 C C     . MET   A 1 537 ? 1.030   -108.815 -17.411 1.00 65.21  ? 529 MET   A C     1 
ATOM   4236 O O     . MET   A 1 537 ? 0.973   -108.196 -18.472 1.00 63.08  ? 529 MET   A O     1 
ATOM   4237 C CB    . MET   A 1 537 ? 3.388   -109.538 -17.906 1.00 73.19  ? 529 MET   A CB    1 
ATOM   4238 C CG    . MET   A 1 537 ? 4.560   -110.456 -17.585 1.00 74.22  ? 529 MET   A CG    1 
ATOM   4239 S SD    . MET   A 1 537 ? 5.172   -110.310 -15.892 1.00 78.66  ? 529 MET   A SD    1 
ATOM   4240 C CE    . MET   A 1 537 ? 4.158   -111.445 -14.932 1.00 76.28  ? 529 MET   A CE    1 
ATOM   4241 N N     . ILE   A 1 538 ? 0.201   -108.603 -16.382 1.00 59.80  ? 530 ILE   A N     1 
ATOM   4242 C CA    . ILE   A 1 538 ? -0.848  -107.598 -16.416 1.00 56.07  ? 530 ILE   A CA    1 
ATOM   4243 C C     . ILE   A 1 538 ? -0.222  -106.235 -16.126 1.00 50.69  ? 530 ILE   A C     1 
ATOM   4244 O O     . ILE   A 1 538 ? 0.543   -106.099 -15.175 1.00 51.07  ? 530 ILE   A O     1 
ATOM   4245 C CB    . ILE   A 1 538 ? -1.966  -107.943 -15.412 1.00 56.97  ? 530 ILE   A CB    1 
ATOM   4246 C CG1   . ILE   A 1 538 ? -2.625  -109.287 -15.744 1.00 57.69  ? 530 ILE   A CG1   1 
ATOM   4247 C CG2   . ILE   A 1 538 ? -2.999  -106.816 -15.328 1.00 57.21  ? 530 ILE   A CG2   1 
ATOM   4248 C CD1   . ILE   A 1 538 ? -3.551  -109.820 -14.664 1.00 58.23  ? 530 ILE   A CD1   1 
ATOM   4249 N N     . ASP   A 1 539 ? -0.552  -105.239 -16.961 1.00 44.37  ? 531 ASP   A N     1 
ATOM   4250 C CA    . ASP   A 1 539 ? -0.160  -103.859 -16.722 1.00 40.09  ? 531 ASP   A CA    1 
ATOM   4251 C C     . ASP   A 1 539 ? -1.322  -102.934 -17.076 1.00 36.95  ? 531 ASP   A C     1 
ATOM   4252 O O     . ASP   A 1 539 ? -1.780  -102.921 -18.218 1.00 36.08  ? 531 ASP   A O     1 
ATOM   4253 C CB    . ASP   A 1 539 ? 1.093   -103.475 -17.495 1.00 39.08  ? 531 ASP   A CB    1 
ATOM   4254 C CG    . ASP   A 1 539 ? 1.617   -102.072 -17.218 1.00 38.42  ? 531 ASP   A CG    1 
ATOM   4255 O OD1   . ASP   A 1 539 ? 1.027   -101.382 -16.364 1.00 38.22  ? 531 ASP   A OD1   1 
ATOM   4256 O OD2   . ASP   A 1 539 ? 2.612   -101.677 -17.858 1.00 38.00  ? 531 ASP   A OD2   1 
ATOM   4257 N N     . ASN   A 1 540 ? -1.766  -102.146 -16.088 1.00 33.15  ? 532 ASN   A N     1 
ATOM   4258 C CA    . ASN   A 1 540 ? -2.901  -101.250 -16.244 1.00 31.33  ? 532 ASN   A CA    1 
ATOM   4259 C C     . ASN   A 1 540 ? -2.443  -99.837  -16.609 1.00 29.34  ? 532 ASN   A C     1 
ATOM   4260 O O     . ASN   A 1 540 ? -3.276  -98.958  -16.805 1.00 29.07  ? 532 ASN   A O     1 
ATOM   4261 C CB    . ASN   A 1 540 ? -3.765  -101.234 -14.988 1.00 31.77  ? 532 ASN   A CB    1 
ATOM   4262 C CG    . ASN   A 1 540 ? -4.548  -102.513 -14.806 1.00 31.82  ? 532 ASN   A CG    1 
ATOM   4263 O OD1   . ASN   A 1 540 ? -4.687  -103.300 -15.748 1.00 31.74  ? 532 ASN   A OD1   1 
ATOM   4264 N ND2   . ASN   A 1 540 ? -5.090  -102.727 -13.617 1.00 32.06  ? 532 ASN   A ND2   1 
ATOM   4265 N N     . ASN   A 1 541 ? -1.126  -99.611  -16.696 1.00 27.68  ? 533 ASN   A N     1 
ATOM   4266 C CA    . ASN   A 1 541 ? -0.604  -98.343  -17.179 1.00 26.92  ? 533 ASN   A CA    1 
ATOM   4267 C C     . ASN   A 1 541 ? -0.867  -98.234  -18.677 1.00 26.73  ? 533 ASN   A C     1 
ATOM   4268 O O     . ASN   A 1 541 ? -1.049  -99.244  -19.355 1.00 26.73  ? 533 ASN   A O     1 
ATOM   4269 C CB    . ASN   A 1 541 ? 0.880   -98.183  -16.874 1.00 26.71  ? 533 ASN   A CB    1 
ATOM   4270 C CG    . ASN   A 1 541 ? 1.159   -98.113  -15.392 1.00 27.42  ? 533 ASN   A CG    1 
ATOM   4271 O OD1   . ASN   A 1 541 ? 0.251   -97.853  -14.591 1.00 26.92  ? 533 ASN   A OD1   1 
ATOM   4272 N ND2   . ASN   A 1 541 ? 2.411   -98.324  -15.012 1.00 27.45  ? 533 ASN   A ND2   1 
ATOM   4273 N N     . ARG   A 1 542 ? -0.877  -96.993  -19.180 1.00 26.40  ? 534 ARG   A N     1 
ATOM   4274 C CA    . ARG   A 1 542 ? -1.258  -96.712  -20.555 1.00 25.48  ? 534 ARG   A CA    1 
ATOM   4275 C C     . ARG   A 1 542 ? -0.599  -95.420  -21.029 1.00 25.87  ? 534 ARG   A C     1 
ATOM   4276 O O     . ARG   A 1 542 ? -0.349  -94.521  -20.228 1.00 26.19  ? 534 ARG   A O     1 
ATOM   4277 C CB    . ARG   A 1 542 ? -2.774  -96.535  -20.684 1.00 24.78  ? 534 ARG   A CB    1 
ATOM   4278 C CG    . ARG   A 1 542 ? -3.629  -97.779  -20.493 1.00 24.34  ? 534 ARG   A CG    1 
ATOM   4279 C CD    . ARG   A 1 542 ? -3.404  -98.784  -21.607 1.00 24.02  ? 534 ARG   A CD    1 
ATOM   4280 N NE    . ARG   A 1 542 ? -4.418  -99.844  -21.604 1.00 23.87  ? 534 ARG   A NE    1 
ATOM   4281 C CZ    . ARG   A 1 542 ? -4.501  -100.853 -20.742 1.00 23.56  ? 534 ARG   A CZ    1 
ATOM   4282 N NH1   . ARG   A 1 542 ? -3.576  -101.034 -19.815 1.00 24.33  ? 534 ARG   A NH1   1 
ATOM   4283 N NH2   . ARG   A 1 542 ? -5.516  -101.696 -20.824 1.00 23.18  ? 534 ARG   A NH2   1 
ATOM   4284 N N     . TYR   A 1 543 ? -0.339  -95.355  -22.342 1.00 26.21  ? 535 TYR   A N     1 
ATOM   4285 C CA    . TYR   A 1 543 ? 0.088   -94.140  -23.019 1.00 26.13  ? 535 TYR   A CA    1 
ATOM   4286 C C     . TYR   A 1 543 ? -0.554  -94.134  -24.403 1.00 26.90  ? 535 TYR   A C     1 
ATOM   4287 O O     . TYR   A 1 543 ? -0.528  -95.142  -25.101 1.00 27.13  ? 535 TYR   A O     1 
ATOM   4288 C CB    . TYR   A 1 543 ? 1.615   -94.061  -23.092 1.00 25.69  ? 535 TYR   A CB    1 
ATOM   4289 C CG    . TYR   A 1 543 ? 2.196   -92.954  -23.966 1.00 25.65  ? 535 TYR   A CG    1 
ATOM   4290 C CD1   . TYR   A 1 543 ? 1.623   -91.687  -24.030 1.00 24.89  ? 535 TYR   A CD1   1 
ATOM   4291 C CD2   . TYR   A 1 543 ? 3.332   -93.186  -24.734 1.00 25.95  ? 535 TYR   A CD2   1 
ATOM   4292 C CE1   . TYR   A 1 543 ? 2.164   -90.692  -24.828 1.00 25.07  ? 535 TYR   A CE1   1 
ATOM   4293 C CE2   . TYR   A 1 543 ? 3.882   -92.199  -25.536 1.00 25.47  ? 535 TYR   A CE2   1 
ATOM   4294 C CZ    . TYR   A 1 543 ? 3.297   -90.948  -25.582 1.00 25.05  ? 535 TYR   A CZ    1 
ATOM   4295 O OH    . TYR   A 1 543 ? 3.847   -89.980  -26.369 1.00 25.40  ? 535 TYR   A OH    1 
ATOM   4296 N N     . CYS   A 1 544 ? -1.124  -92.986  -24.780 1.00 28.59  ? 536 CYS   A N     1 
ATOM   4297 C CA    . CYS   A 1 544 ? -1.999  -92.879  -25.934 1.00 29.53  ? 536 CYS   A CA    1 
ATOM   4298 C C     . CYS   A 1 544 ? -1.827  -91.507  -26.582 1.00 28.47  ? 536 CYS   A C     1 
ATOM   4299 O O     . CYS   A 1 544 ? -1.947  -90.492  -25.901 1.00 28.04  ? 536 CYS   A O     1 
ATOM   4300 C CB    . CYS   A 1 544 ? -3.442  -93.076  -25.487 1.00 31.27  ? 536 CYS   A CB    1 
ATOM   4301 S SG    . CYS   A 1 544 ? -4.640  -93.070  -26.844 1.00 36.49  ? 536 CYS   A SG    1 
ATOM   4302 N N     . THR   A 1 545 ? -1.537  -91.490  -27.891 1.00 27.84  ? 537 THR   A N     1 
ATOM   4303 C CA    . THR   A 1 545 ? -1.469  -90.256  -28.661 1.00 27.42  ? 537 THR   A CA    1 
ATOM   4304 C C     . THR   A 1 545 ? -2.705  -90.166  -29.551 1.00 28.16  ? 537 THR   A C     1 
ATOM   4305 O O     . THR   A 1 545 ? -2.998  -91.101  -30.288 1.00 28.53  ? 537 THR   A O     1 
ATOM   4306 C CB    . THR   A 1 545 ? -0.190  -90.220  -29.498 1.00 26.70  ? 537 THR   A CB    1 
ATOM   4307 O OG1   . THR   A 1 545 ? 0.877   -90.244  -28.558 1.00 25.77  ? 537 THR   A OG1   1 
ATOM   4308 C CG2   . THR   A 1 545 ? -0.076  -88.964  -30.345 1.00 26.47  ? 537 THR   A CG2   1 
ATOM   4309 N N     . LEU   A 1 546 ? -3.406  -89.028  -29.494 1.00 28.68  ? 538 LEU   A N     1 
ATOM   4310 C CA    . LEU   A 1 546 ? -4.590  -88.815  -30.310 1.00 28.96  ? 538 LEU   A CA    1 
ATOM   4311 C C     . LEU   A 1 546 ? -4.394  -87.583  -31.190 1.00 29.58  ? 538 LEU   A C     1 
ATOM   4312 O O     . LEU   A 1 546 ? -3.660  -86.663  -30.828 1.00 30.09  ? 538 LEU   A O     1 
ATOM   4313 C CB    . LEU   A 1 546 ? -5.827  -88.694  -29.420 1.00 29.29  ? 538 LEU   A CB    1 
ATOM   4314 C CG    . LEU   A 1 546 ? -6.194  -89.951  -28.623 1.00 30.01  ? 538 LEU   A CG    1 
ATOM   4315 C CD1   . LEU   A 1 546 ? -7.292  -89.663  -27.616 1.00 29.95  ? 538 LEU   A CD1   1 
ATOM   4316 C CD2   . LEU   A 1 546 ? -6.612  -91.084  -29.550 1.00 30.19  ? 538 LEU   A CD2   1 
ATOM   4317 N N     . GLU   A 1 547 ? -5.065  -87.602  -32.350 1.00 28.87  ? 539 GLU   A N     1 
ATOM   4318 C CA    . GLU   A 1 547 ? -4.956  -86.577  -33.376 1.00 29.38  ? 539 GLU   A CA    1 
ATOM   4319 C C     . GLU   A 1 547 ? -6.363  -86.117  -33.745 1.00 27.92  ? 539 GLU   A C     1 
ATOM   4320 O O     . GLU   A 1 547 ? -7.127  -86.888  -34.321 1.00 28.05  ? 539 GLU   A O     1 
ATOM   4321 C CB    . GLU   A 1 547 ? -4.305  -87.171  -34.625 1.00 30.87  ? 539 GLU   A CB    1 
ATOM   4322 C CG    . GLU   A 1 547 ? -2.878  -87.677  -34.429 1.00 31.82  ? 539 GLU   A CG    1 
ATOM   4323 C CD    . GLU   A 1 547 ? -1.811  -86.636  -34.704 1.00 32.96  ? 539 GLU   A CD    1 
ATOM   4324 O OE1   . GLU   A 1 547 ? -1.942  -85.926  -35.725 1.00 33.93  ? 539 GLU   A OE1   1 
ATOM   4325 O OE2   . GLU   A 1 547 ? -0.840  -86.557  -33.925 1.00 34.03  ? 539 GLU   A OE2   1 
ATOM   4326 N N     . PHE   A 1 548 ? -6.697  -84.867  -33.410 1.00 27.16  ? 540 PHE   A N     1 
ATOM   4327 C CA    . PHE   A 1 548 ? -8.058  -84.370  -33.542 1.00 27.06  ? 540 PHE   A CA    1 
ATOM   4328 C C     . PHE   A 1 548 ? -8.120  -83.324  -34.650 1.00 27.33  ? 540 PHE   A C     1 
ATOM   4329 O O     . PHE   A 1 548 ? -7.688  -82.192  -34.451 1.00 27.58  ? 540 PHE   A O     1 
ATOM   4330 C CB    . PHE   A 1 548 ? -8.532  -83.775  -32.214 1.00 26.97  ? 540 PHE   A CB    1 
ATOM   4331 C CG    . PHE   A 1 548 ? -8.844  -84.807  -31.139 1.00 26.37  ? 540 PHE   A CG    1 
ATOM   4332 C CD1   . PHE   A 1 548 ? -9.989  -85.592  -31.224 1.00 25.75  ? 540 PHE   A CD1   1 
ATOM   4333 C CD2   . PHE   A 1 548 ? -8.011  -84.970  -30.036 1.00 26.01  ? 540 PHE   A CD2   1 
ATOM   4334 C CE1   . PHE   A 1 548 ? -10.284 -86.522  -30.241 1.00 25.73  ? 540 PHE   A CE1   1 
ATOM   4335 C CE2   . PHE   A 1 548 ? -8.314  -85.900  -29.055 1.00 25.44  ? 540 PHE   A CE2   1 
ATOM   4336 C CZ    . PHE   A 1 548 ? -9.447  -86.673  -29.159 1.00 25.56  ? 540 PHE   A CZ    1 
ATOM   4337 N N     . PRO   A 1 549 ? -8.655  -83.663  -35.847 1.00 27.82  ? 541 PRO   A N     1 
ATOM   4338 C CA    . PRO   A 1 549 ? -8.753  -82.692  -36.936 1.00 27.87  ? 541 PRO   A CA    1 
ATOM   4339 C C     . PRO   A 1 549 ? -9.825  -81.648  -36.633 1.00 27.81  ? 541 PRO   A C     1 
ATOM   4340 O O     . PRO   A 1 549 ? -10.994 -81.988  -36.460 1.00 28.05  ? 541 PRO   A O     1 
ATOM   4341 C CB    . PRO   A 1 549 ? -9.070  -83.532  -38.185 1.00 27.85  ? 541 PRO   A CB    1 
ATOM   4342 C CG    . PRO   A 1 549 ? -9.641  -84.835  -37.653 1.00 27.88  ? 541 PRO   A CG    1 
ATOM   4343 C CD    . PRO   A 1 549 ? -9.175  -84.990  -36.214 1.00 27.54  ? 541 PRO   A CD    1 
ATOM   4344 N N     . VAL   A 1 550 ? -9.400  -80.380  -36.567 1.00 27.68  ? 542 VAL   A N     1 
ATOM   4345 C CA    . VAL   A 1 550 ? -10.281 -79.271  -36.241 1.00 28.24  ? 542 VAL   A CA    1 
ATOM   4346 C C     . VAL   A 1 550 ? -10.515 -78.422  -37.489 1.00 28.86  ? 542 VAL   A C     1 
ATOM   4347 O O     . VAL   A 1 550 ? -9.562  -78.011  -38.149 1.00 28.25  ? 542 VAL   A O     1 
ATOM   4348 C CB    . VAL   A 1 550 ? -9.656  -78.451  -35.097 1.00 28.16  ? 542 VAL   A CB    1 
ATOM   4349 C CG1   . VAL   A 1 550 ? -10.366 -77.120  -34.876 1.00 28.28  ? 542 VAL   A CG1   1 
ATOM   4350 C CG2   . VAL   A 1 550 ? -9.608  -79.257  -33.807 1.00 28.12  ? 542 VAL   A CG2   1 
ATOM   4351 N N     . GLU   A 1 551 ? -11.794 -78.148  -37.781 1.00 29.42  ? 543 GLU   A N     1 
ATOM   4352 C CA    . GLU   A 1 551 ? -12.189 -77.452  -38.994 1.00 29.95  ? 543 GLU   A CA    1 
ATOM   4353 C C     . GLU   A 1 551 ? -12.779 -76.078  -38.673 1.00 29.25  ? 543 GLU   A C     1 
ATOM   4354 O O     . GLU   A 1 551 ? -13.479 -75.506  -39.504 1.00 30.59  ? 543 GLU   A O     1 
ATOM   4355 C CB    . GLU   A 1 551 ? -13.206 -78.293  -39.770 1.00 31.47  ? 543 GLU   A CB    1 
ATOM   4356 C CG    . GLU   A 1 551 ? -12.726 -79.701  -40.120 1.00 32.93  ? 543 GLU   A CG    1 
ATOM   4357 C CD    . GLU   A 1 551 ? -11.298 -79.811  -40.633 1.00 34.47  ? 543 GLU   A CD    1 
ATOM   4358 O OE1   . GLU   A 1 551 ? -10.905 -79.008  -41.508 1.00 36.33  ? 543 GLU   A OE1   1 
ATOM   4359 O OE2   . GLU   A 1 551 ? -10.575 -80.716  -40.165 1.00 35.52  ? 543 GLU   A OE2   1 
ATOM   4360 N N     . VAL   A 1 552 ? -12.483 -75.539  -37.483 1.00 27.46  ? 544 VAL   A N     1 
ATOM   4361 C CA    . VAL   A 1 552 ? -12.938 -74.208  -37.108 1.00 26.83  ? 544 VAL   A CA    1 
ATOM   4362 C C     . VAL   A 1 552 ? -11.768 -73.430  -36.509 1.00 25.64  ? 544 VAL   A C     1 
ATOM   4363 O O     . VAL   A 1 552 ? -10.799 -74.025  -36.045 1.00 25.93  ? 544 VAL   A O     1 
ATOM   4364 C CB    . VAL   A 1 552 ? -14.119 -74.270  -36.117 1.00 27.69  ? 544 VAL   A CB    1 
ATOM   4365 C CG1   . VAL   A 1 552 ? -15.395 -74.777  -36.778 1.00 28.38  ? 544 VAL   A CG1   1 
ATOM   4366 C CG2   . VAL   A 1 552 ? -13.800 -75.100  -34.878 1.00 27.70  ? 544 VAL   A CG2   1 
ATOM   4367 N N     . ASN   A 1 553 ? -11.864 -72.094  -36.530 1.00 24.63  ? 545 ASN   A N     1 
ATOM   4368 C CA    . ASN   A 1 553 ? -11.041 -71.272  -35.656 1.00 24.07  ? 545 ASN   A CA    1 
ATOM   4369 C C     . ASN   A 1 553 ? -11.656 -71.315  -34.262 1.00 23.45  ? 545 ASN   A C     1 
ATOM   4370 O O     . ASN   A 1 553 ? -12.864 -71.152  -34.119 1.00 23.10  ? 545 ASN   A O     1 
ATOM   4371 C CB    . ASN   A 1 553 ? -10.932 -69.818  -36.105 1.00 24.12  ? 545 ASN   A CB    1 
ATOM   4372 C CG    . ASN   A 1 553 ? -10.377 -69.659  -37.501 1.00 24.17  ? 545 ASN   A CG    1 
ATOM   4373 O OD1   . ASN   A 1 553 ? -9.455  -70.378  -37.898 1.00 24.41  ? 545 ASN   A OD1   1 
ATOM   4374 N ND2   . ASN   A 1 553 ? -10.923 -68.722  -38.262 1.00 24.10  ? 545 ASN   A ND2   1 
ATOM   4375 N N     . THR   A 1 554 ? -10.825 -71.532  -33.236 1.00 23.37  ? 546 THR   A N     1 
ATOM   4376 C CA    . THR   A 1 554 ? -11.334 -71.692  -31.883 1.00 22.94  ? 546 THR   A CA    1 
ATOM   4377 C C     . THR   A 1 554 ? -10.219 -71.463  -30.863 1.00 22.75  ? 546 THR   A C     1 
ATOM   4378 O O     . THR   A 1 554 ? -9.116  -71.056  -31.220 1.00 22.49  ? 546 THR   A O     1 
ATOM   4379 C CB    . THR   A 1 554 ? -11.954 -73.085  -31.767 1.00 22.58  ? 546 THR   A CB    1 
ATOM   4380 O OG1   . THR   A 1 554 ? -12.710 -73.066  -30.561 1.00 21.90  ? 546 THR   A OG1   1 
ATOM   4381 C CG2   . THR   A 1 554 ? -10.915 -74.191  -31.780 1.00 22.55  ? 546 THR   A CG2   1 
ATOM   4382 N N     . VAL   A 1 555 ? -10.546 -71.712  -29.589 1.00 22.91  ? 547 VAL   A N     1 
ATOM   4383 C CA    . VAL   A 1 555 ? -9.588  -71.679  -28.495 1.00 23.06  ? 547 VAL   A CA    1 
ATOM   4384 C C     . VAL   A 1 555 ? -9.789  -72.926  -27.639 1.00 22.86  ? 547 VAL   A C     1 
ATOM   4385 O O     . VAL   A 1 555 ? -10.863 -73.115  -27.077 1.00 23.36  ? 547 VAL   A O     1 
ATOM   4386 C CB    . VAL   A 1 555 ? -9.757  -70.396  -27.660 1.00 23.09  ? 547 VAL   A CB    1 
ATOM   4387 C CG1   . VAL   A 1 555 ? -8.907  -70.412  -26.394 1.00 23.20  ? 547 VAL   A CG1   1 
ATOM   4388 C CG2   . VAL   A 1 555 ? -9.469  -69.151  -28.489 1.00 23.08  ? 547 VAL   A CG2   1 
ATOM   4389 N N     . LEU   A 1 556 ? -8.746  -73.760  -27.539 1.00 22.66  ? 548 LEU   A N     1 
ATOM   4390 C CA    . LEU   A 1 556 ? -8.805  -75.005  -26.785 1.00 22.40  ? 548 LEU   A CA    1 
ATOM   4391 C C     . LEU   A 1 556 ? -8.664  -74.706  -25.296 1.00 21.91  ? 548 LEU   A C     1 
ATOM   4392 O O     . LEU   A 1 556 ? -7.767  -73.964  -24.908 1.00 22.37  ? 548 LEU   A O     1 
ATOM   4393 C CB    . LEU   A 1 556 ? -7.692  -75.935  -27.269 1.00 22.54  ? 548 LEU   A CB    1 
ATOM   4394 C CG    . LEU   A 1 556 ? -7.555  -77.275  -26.537 1.00 22.53  ? 548 LEU   A CG    1 
ATOM   4395 C CD1   . LEU   A 1 556 ? -8.747  -78.179  -26.802 1.00 22.79  ? 548 LEU   A CD1   1 
ATOM   4396 C CD2   . LEU   A 1 556 ? -6.259  -77.967  -26.926 1.00 22.15  ? 548 LEU   A CD2   1 
ATOM   4397 N N     . HIS   A 1 557 ? -9.547  -75.298  -24.477 1.00 21.51  ? 549 HIS   A N     1 
ATOM   4398 C CA    . HIS   A 1 557 ? -9.519  -75.104  -23.034 1.00 21.22  ? 549 HIS   A CA    1 
ATOM   4399 C C     . HIS   A 1 557 ? -9.474  -76.423  -22.264 1.00 20.63  ? 549 HIS   A C     1 
ATOM   4400 O O     . HIS   A 1 557 ? -9.287  -76.402  -21.053 1.00 20.28  ? 549 HIS   A O     1 
ATOM   4401 C CB    . HIS   A 1 557 ? -10.743 -74.319  -22.554 1.00 21.58  ? 549 HIS   A CB    1 
ATOM   4402 C CG    . HIS   A 1 557 ? -10.827 -72.931  -23.087 1.00 21.81  ? 549 HIS   A CG    1 
ATOM   4403 N ND1   . HIS   A 1 557 ? -11.728 -72.560  -24.060 1.00 21.68  ? 549 HIS   A ND1   1 
ATOM   4404 C CD2   . HIS   A 1 557 ? -10.156 -71.824  -22.760 1.00 21.94  ? 549 HIS   A CD2   1 
ATOM   4405 C CE1   . HIS   A 1 557 ? -11.587 -71.271  -24.314 1.00 21.80  ? 549 HIS   A CE1   1 
ATOM   4406 N NE2   . HIS   A 1 557 ? -10.635 -70.804  -23.537 1.00 22.15  ? 549 HIS   A NE2   1 
ATOM   4407 N N     . GLY   A 1 558 ? -9.661  -77.563  -22.941 1.00 20.38  ? 550 GLY   A N     1 
ATOM   4408 C CA    . GLY   A 1 558 ? -9.579  -78.850  -22.269 1.00 20.08  ? 550 GLY   A CA    1 
ATOM   4409 C C     . GLY   A 1 558 ? -10.150 -79.979  -23.123 1.00 20.00  ? 550 GLY   A C     1 
ATOM   4410 O O     . GLY   A 1 558 ? -10.446 -79.784  -24.299 1.00 19.68  ? 550 GLY   A O     1 
ATOM   4411 N N     . PHE   A 1 559 ? -10.301 -81.153  -22.498 1.00 19.83  ? 551 PHE   A N     1 
ATOM   4412 C CA    . PHE   A 1 559 ? -10.793 -82.345  -23.168 1.00 19.68  ? 551 PHE   A CA    1 
ATOM   4413 C C     . PHE   A 1 559 ? -11.942 -82.940  -22.363 1.00 19.60  ? 551 PHE   A C     1 
ATOM   4414 O O     . PHE   A 1 559 ? -11.795 -83.199  -21.174 1.00 19.55  ? 551 PHE   A O     1 
ATOM   4415 C CB    . PHE   A 1 559 ? -9.644  -83.345  -23.330 1.00 19.71  ? 551 PHE   A CB    1 
ATOM   4416 C CG    . PHE   A 1 559 ? -8.556  -82.852  -24.271 1.00 20.22  ? 551 PHE   A CG    1 
ATOM   4417 C CD1   . PHE   A 1 559 ? -7.575  -81.972  -23.828 1.00 20.49  ? 551 PHE   A CD1   1 
ATOM   4418 C CD2   . PHE   A 1 559 ? -8.532  -83.253  -25.603 1.00 20.43  ? 551 PHE   A CD2   1 
ATOM   4419 C CE1   . PHE   A 1 559 ? -6.596  -81.507  -24.695 1.00 20.75  ? 551 PHE   A CE1   1 
ATOM   4420 C CE2   . PHE   A 1 559 ? -7.548  -82.790  -26.465 1.00 20.70  ? 551 PHE   A CE2   1 
ATOM   4421 C CZ    . PHE   A 1 559 ? -6.585  -81.915  -26.010 1.00 20.72  ? 551 PHE   A CZ    1 
ATOM   4422 N N     . ALA   A 1 560 ? -13.082 -83.157  -23.027 1.00 20.15  ? 552 ALA   A N     1 
ATOM   4423 C CA    . ALA   A 1 560 ? -14.185 -83.893  -22.433 1.00 20.29  ? 552 ALA   A CA    1 
ATOM   4424 C C     . ALA   A 1 560 ? -13.856 -85.382  -22.446 1.00 20.56  ? 552 ALA   A C     1 
ATOM   4425 O O     . ALA   A 1 560 ? -13.225 -85.871  -23.380 1.00 20.42  ? 552 ALA   A O     1 
ATOM   4426 C CB    . ALA   A 1 560 ? -15.470 -83.617  -23.180 1.00 20.44  ? 552 ALA   A CB    1 
ATOM   4427 N N     . GLY   A 1 561 ? -14.292 -86.083  -21.395 1.00 20.95  ? 553 GLY   A N     1 
ATOM   4428 C CA    . GLY   A 1 561 ? -14.138 -87.523  -21.307 1.00 21.48  ? 553 GLY   A CA    1 
ATOM   4429 C C     . GLY   A 1 561 ? -15.498 -88.207  -21.195 1.00 22.14  ? 553 GLY   A C     1 
ATOM   4430 O O     . GLY   A 1 561 ? -16.377 -87.748  -20.466 1.00 21.93  ? 553 GLY   A O     1 
ATOM   4431 N N     . TYR   A 1 562 ? -15.653 -89.289  -21.963 1.00 22.98  ? 554 TYR   A N     1 
ATOM   4432 C CA    . TYR   A 1 562 ? -16.840 -90.124  -21.927 1.00 23.82  ? 554 TYR   A CA    1 
ATOM   4433 C C     . TYR   A 1 562 ? -16.371 -91.575  -21.853 1.00 24.22  ? 554 TYR   A C     1 
ATOM   4434 O O     . TYR   A 1 562 ? -15.172 -91.840  -21.796 1.00 24.32  ? 554 TYR   A O     1 
ATOM   4435 C CB    . TYR   A 1 562 ? -17.701 -89.869  -23.170 1.00 24.32  ? 554 TYR   A CB    1 
ATOM   4436 C CG    . TYR   A 1 562 ? -17.983 -88.414  -23.526 1.00 24.37  ? 554 TYR   A CG    1 
ATOM   4437 C CD1   . TYR   A 1 562 ? -19.079 -87.739  -23.000 1.00 24.75  ? 554 TYR   A CD1   1 
ATOM   4438 C CD2   . TYR   A 1 562 ? -17.169 -87.725  -24.417 1.00 24.41  ? 554 TYR   A CD2   1 
ATOM   4439 C CE1   . TYR   A 1 562 ? -19.348 -86.422  -23.339 1.00 24.91  ? 554 TYR   A CE1   1 
ATOM   4440 C CE2   . TYR   A 1 562 ? -17.425 -86.407  -24.763 1.00 24.70  ? 554 TYR   A CE2   1 
ATOM   4441 C CZ    . TYR   A 1 562 ? -18.519 -85.753  -24.223 1.00 24.85  ? 554 TYR   A CZ    1 
ATOM   4442 O OH    . TYR   A 1 562 ? -18.770 -84.456  -24.570 1.00 24.93  ? 554 TYR   A OH    1 
ATOM   4443 N N     . PHE   A 1 563 ? -17.316 -92.517  -21.864 1.00 24.41  ? 555 PHE   A N     1 
ATOM   4444 C CA    . PHE   A 1 563 ? -16.950 -93.919  -21.905 1.00 25.21  ? 555 PHE   A CA    1 
ATOM   4445 C C     . PHE   A 1 563 ? -18.093 -94.740  -22.490 1.00 25.19  ? 555 PHE   A C     1 
ATOM   4446 O O     . PHE   A 1 563 ? -19.241 -94.300  -22.501 1.00 24.87  ? 555 PHE   A O     1 
ATOM   4447 C CB    . PHE   A 1 563 ? -16.593 -94.432  -20.507 1.00 26.13  ? 555 PHE   A CB    1 
ATOM   4448 C CG    . PHE   A 1 563 ? -17.792 -94.791  -19.638 1.00 26.59  ? 555 PHE   A CG    1 
ATOM   4449 C CD1   . PHE   A 1 563 ? -18.339 -96.072  -19.674 1.00 26.73  ? 555 PHE   A CD1   1 
ATOM   4450 C CD2   . PHE   A 1 563 ? -18.377 -93.849  -18.799 1.00 26.32  ? 555 PHE   A CD2   1 
ATOM   4451 C CE1   . PHE   A 1 563 ? -19.438 -96.398  -18.894 1.00 26.47  ? 555 PHE   A CE1   1 
ATOM   4452 C CE2   . PHE   A 1 563 ? -19.475 -94.182  -18.019 1.00 26.52  ? 555 PHE   A CE2   1 
ATOM   4453 C CZ    . PHE   A 1 563 ? -20.002 -95.453  -18.067 1.00 26.57  ? 555 PHE   A CZ    1 
ATOM   4454 N N     . GLU   A 1 564 ? -17.734 -95.940  -22.961 1.00 25.46  ? 556 GLU   A N     1 
ATOM   4455 C CA    . GLU   A 1 564 ? -18.680 -96.988  -23.308 1.00 26.01  ? 556 GLU   A CA    1 
ATOM   4456 C C     . GLU   A 1 564 ? -18.218 -98.278  -22.641 1.00 26.19  ? 556 GLU   A C     1 
ATOM   4457 O O     . GLU   A 1 564 ? -17.027 -98.443  -22.379 1.00 25.84  ? 556 GLU   A O     1 
ATOM   4458 C CB    . GLU   A 1 564 ? -18.726 -97.272  -24.810 1.00 26.41  ? 556 GLU   A CB    1 
ATOM   4459 C CG    . GLU   A 1 564 ? -19.088 -96.068  -25.673 1.00 26.95  ? 556 GLU   A CG    1 
ATOM   4460 C CD    . GLU   A 1 564 ? -19.169 -96.403  -27.154 1.00 27.91  ? 556 GLU   A CD    1 
ATOM   4461 O OE1   . GLU   A 1 564 ? -20.169 -96.022  -27.807 1.00 28.39  ? 556 GLU   A OE1   1 
ATOM   4462 O OE2   . GLU   A 1 564 ? -18.226 -97.063  -27.650 1.00 27.35  ? 556 GLU   A OE2   1 
ATOM   4463 N N     . THR   A 1 565 ? -19.163 -99.192  -22.395 1.00 26.87  ? 557 THR   A N     1 
ATOM   4464 C CA    . THR   A 1 565 ? -18.831 -100.491 -21.833 1.00 27.51  ? 557 THR   A CA    1 
ATOM   4465 C C     . THR   A 1 565 ? -19.719 -101.560 -22.461 1.00 28.42  ? 557 THR   A C     1 
ATOM   4466 O O     . THR   A 1 565 ? -20.893 -101.322 -22.744 1.00 28.09  ? 557 THR   A O     1 
ATOM   4467 C CB    . THR   A 1 565 ? -18.971 -100.465 -20.311 1.00 27.87  ? 557 THR   A CB    1 
ATOM   4468 O OG1   . THR   A 1 565 ? -18.520 -101.736 -19.852 1.00 27.68  ? 557 THR   A OG1   1 
ATOM   4469 C CG2   . THR   A 1 565 ? -20.397 -100.224 -19.846 1.00 27.86  ? 557 THR   A CG2   1 
ATOM   4470 N N     . VAL   A 1 566 ? -19.120 -102.734 -22.684 1.00 29.08  ? 558 VAL   A N     1 
ATOM   4471 C CA    . VAL   A 1 566 ? -19.859 -103.941 -22.995 1.00 28.80  ? 558 VAL   A CA    1 
ATOM   4472 C C     . VAL   A 1 566 ? -20.105 -104.668 -21.678 1.00 29.11  ? 558 VAL   A C     1 
ATOM   4473 O O     . VAL   A 1 566 ? -19.166 -105.163 -21.053 1.00 28.65  ? 558 VAL   A O     1 
ATOM   4474 C CB    . VAL   A 1 566 ? -19.113 -104.838 -24.001 1.00 28.88  ? 558 VAL   A CB    1 
ATOM   4475 C CG1   . VAL   A 1 566 ? -19.862 -106.139 -24.262 1.00 29.04  ? 558 VAL   A CG1   1 
ATOM   4476 C CG2   . VAL   A 1 566 ? -18.837 -104.115 -25.314 1.00 28.35  ? 558 VAL   A CG2   1 
ATOM   4477 N N     . LEU   A 1 567 ? -21.374 -104.698 -21.258 1.00 29.53  ? 559 LEU   A N     1 
ATOM   4478 C CA    . LEU   A 1 567 ? -21.786 -105.492 -20.115 1.00 29.75  ? 559 LEU   A CA    1 
ATOM   4479 C C     . LEU   A 1 567 ? -21.689 -106.968 -20.491 1.00 31.20  ? 559 LEU   A C     1 
ATOM   4480 O O     . LEU   A 1 567 ? -21.015 -107.741 -19.812 1.00 31.14  ? 559 LEU   A O     1 
ATOM   4481 C CB    . LEU   A 1 567 ? -23.201 -105.110 -19.686 1.00 29.38  ? 559 LEU   A CB    1 
ATOM   4482 C CG    . LEU   A 1 567 ? -23.431 -103.637 -19.337 1.00 29.16  ? 559 LEU   A CG    1 
ATOM   4483 C CD1   . LEU   A 1 567 ? -24.848 -103.440 -18.829 1.00 29.43  ? 559 LEU   A CD1   1 
ATOM   4484 C CD2   . LEU   A 1 567 ? -22.426 -103.121 -18.321 1.00 29.24  ? 559 LEU   A CD2   1 
ATOM   4485 N N     . TYR   A 1 568 ? -22.357 -107.337 -21.594 1.00 32.68  ? 560 TYR   A N     1 
ATOM   4486 C CA    . TYR   A 1 568 ? -22.328 -108.700 -22.104 1.00 33.66  ? 560 TYR   A CA    1 
ATOM   4487 C C     . TYR   A 1 568 ? -22.813 -108.709 -23.552 1.00 34.02  ? 560 TYR   A C     1 
ATOM   4488 O O     . TYR   A 1 568 ? -23.907 -108.222 -23.838 1.00 33.88  ? 560 TYR   A O     1 
ATOM   4489 C CB    . TYR   A 1 568 ? -23.190 -109.644 -21.259 1.00 33.74  ? 560 TYR   A CB    1 
ATOM   4490 C CG    . TYR   A 1 568 ? -23.035 -111.112 -21.628 1.00 33.94  ? 560 TYR   A CG    1 
ATOM   4491 C CD1   . TYR   A 1 568 ? -21.822 -111.767 -21.439 1.00 34.11  ? 560 TYR   A CD1   1 
ATOM   4492 C CD2   . TYR   A 1 568 ? -24.097 -111.850 -22.143 1.00 34.35  ? 560 TYR   A CD2   1 
ATOM   4493 C CE1   . TYR   A 1 568 ? -21.662 -113.103 -21.771 1.00 33.94  ? 560 TYR   A CE1   1 
ATOM   4494 C CE2   . TYR   A 1 568 ? -23.953 -113.190 -22.469 1.00 33.93  ? 560 TYR   A CE2   1 
ATOM   4495 C CZ    . TYR   A 1 568 ? -22.732 -113.817 -22.283 1.00 33.86  ? 560 TYR   A CZ    1 
ATOM   4496 O OH    . TYR   A 1 568 ? -22.566 -115.135 -22.597 1.00 33.57  ? 560 TYR   A OH    1 
ATOM   4497 N N     A GLN   A 1 569 ? -22.015 -109.309 -24.445 0.50 34.36  ? 561 GLN   A N     1 
ATOM   4498 N N     B GLN   A 1 569 ? -21.956 -109.232 -24.441 0.50 34.04  ? 561 GLN   A N     1 
ATOM   4499 C CA    A GLN   A 1 569 ? -22.364 -109.433 -25.854 0.50 34.78  ? 561 GLN   A CA    1 
ATOM   4500 C CA    B GLN   A 1 569 ? -22.217 -109.325 -25.870 0.50 34.30  ? 561 GLN   A CA    1 
ATOM   4501 C C     A GLN   A 1 569 ? -22.710 -108.053 -26.416 0.50 35.41  ? 561 GLN   A C     1 
ATOM   4502 C C     B GLN   A 1 569 ? -22.701 -107.974 -26.399 0.50 35.16  ? 561 GLN   A C     1 
ATOM   4503 O O     A GLN   A 1 569 ? -21.828 -107.217 -26.595 0.50 36.08  ? 561 GLN   A O     1 
ATOM   4504 O O     B GLN   A 1 569 ? -21.888 -107.067 -26.558 0.50 35.86  ? 561 GLN   A O     1 
ATOM   4505 C CB    A GLN   A 1 569 ? -23.515 -110.418 -26.080 0.50 34.22  ? 561 GLN   A CB    1 
ATOM   4506 C CB    B GLN   A 1 569 ? -23.074 -110.559 -26.151 0.50 33.42  ? 561 GLN   A CB    1 
ATOM   4507 C CG    A GLN   A 1 569 ? -23.189 -111.878 -25.790 0.50 33.99  ? 561 GLN   A CG    1 
ATOM   4508 C CG    B GLN   A 1 569 ? -22.248 -111.843 -26.153 0.50 32.89  ? 561 GLN   A CG    1 
ATOM   4509 C CD    A GLN   A 1 569 ? -24.344 -112.797 -26.125 0.50 34.01  ? 561 GLN   A CD    1 
ATOM   4510 C CD    B GLN   A 1 569 ? -23.046 -113.095 -25.868 0.50 32.55  ? 561 GLN   A CD    1 
ATOM   4511 O OE1   A GLN   A 1 569 ? -25.301 -112.407 -26.803 0.50 34.35  ? 561 GLN   A OE1   1 
ATOM   4512 O OE1   B GLN   A 1 569 ? -24.279 -113.077 -25.793 0.50 32.17  ? 561 GLN   A OE1   1 
ATOM   4513 N NE2   A GLN   A 1 569 ? -24.259 -114.037 -25.667 0.50 33.96  ? 561 GLN   A NE2   1 
ATOM   4514 N NE2   B GLN   A 1 569 ? -22.336 -114.203 -25.708 0.50 32.34  ? 561 GLN   A NE2   1 
ATOM   4515 N N     . ASP   A 1 570 ? -24.008 -107.828 -26.661 1.00 35.69  ? 562 ASP   A N     1 
ATOM   4516 C CA    . ASP   A 1 570 ? -24.511 -106.624 -27.306 1.00 36.69  ? 562 ASP   A CA    1 
ATOM   4517 C C     . ASP   A 1 570 ? -25.260 -105.746 -26.309 1.00 35.80  ? 562 ASP   A C     1 
ATOM   4518 O O     . ASP   A 1 570 ? -25.907 -104.783 -26.711 1.00 35.52  ? 562 ASP   A O     1 
ATOM   4519 C CB    . ASP   A 1 570 ? -25.423 -106.966 -28.473 1.00 38.91  ? 562 ASP   A CB    1 
ATOM   4520 C CG    . ASP   A 1 570 ? -26.791 -107.516 -28.090 1.00 40.64  ? 562 ASP   A CG    1 
ATOM   4521 O OD1   . ASP   A 1 570 ? -26.843 -108.389 -27.194 1.00 40.89  ? 562 ASP   A OD1   1 
ATOM   4522 O OD2   . ASP   A 1 570 ? -27.790 -107.069 -28.695 1.00 41.83  ? 562 ASP   A OD2   1 
ATOM   4523 N N     . ILE   A 1 571 ? -25.193 -106.089 -25.017 1.00 35.48  ? 563 ILE   A N     1 
ATOM   4524 C CA    . ILE   A 1 571 ? -25.782 -105.247 -23.992 1.00 35.38  ? 563 ILE   A CA    1 
ATOM   4525 C C     . ILE   A 1 571 ? -24.719 -104.246 -23.552 1.00 34.20  ? 563 ILE   A C     1 
ATOM   4526 O O     . ILE   A 1 571 ? -23.678 -104.636 -23.025 1.00 33.40  ? 563 ILE   A O     1 
ATOM   4527 C CB    . ILE   A 1 571 ? -26.324 -106.077 -22.815 1.00 37.08  ? 563 ILE   A CB    1 
ATOM   4528 C CG1   . ILE   A 1 571 ? -27.181 -107.255 -23.291 1.00 37.88  ? 563 ILE   A CG1   1 
ATOM   4529 C CG2   . ILE   A 1 571 ? -27.088 -105.183 -21.838 1.00 36.92  ? 563 ILE   A CG2   1 
ATOM   4530 C CD1   . ILE   A 1 571 ? -28.408 -106.851 -24.091 1.00 38.51  ? 563 ILE   A CD1   1 
ATOM   4531 N N     . THR   A 1 572 ? -24.992 -102.958 -23.792 1.00 33.42  ? 564 THR   A N     1 
ATOM   4532 C CA    . THR   A 1 572 ? -23.990 -101.919 -23.631 1.00 32.98  ? 564 THR   A CA    1 
ATOM   4533 C C     . THR   A 1 572 ? -24.574 -100.740 -22.863 1.00 32.44  ? 564 THR   A C     1 
ATOM   4534 O O     . THR   A 1 572 ? -25.790 -100.564 -22.794 1.00 32.84  ? 564 THR   A O     1 
ATOM   4535 C CB    . THR   A 1 572 ? -23.477 -101.478 -25.001 1.00 32.58  ? 564 THR   A CB    1 
ATOM   4536 O OG1   . THR   A 1 572 ? -24.641 -101.159 -25.756 1.00 33.02  ? 564 THR   A OG1   1 
ATOM   4537 C CG2   . THR   A 1 572 ? -22.680 -102.558 -25.707 1.00 32.36  ? 564 THR   A CG2   1 
ATOM   4538 N N     . LEU   A 1 573 ? -23.664 -99.950  -22.284 1.00 31.60  ? 565 LEU   A N     1 
ATOM   4539 C CA    . LEU   A 1 573 ? -23.973 -98.635  -21.752 1.00 30.81  ? 565 LEU   A CA    1 
ATOM   4540 C C     . LEU   A 1 573 ? -22.968 -97.646  -22.335 1.00 28.85  ? 565 LEU   A C     1 
ATOM   4541 O O     . LEU   A 1 573 ? -21.815 -98.001  -22.578 1.00 28.08  ? 565 LEU   A O     1 
ATOM   4542 C CB    . LEU   A 1 573 ? -23.912 -98.650  -20.227 1.00 32.03  ? 565 LEU   A CB    1 
ATOM   4543 C CG    . LEU   A 1 573 ? -24.910 -99.569  -19.515 1.00 33.00  ? 565 LEU   A CG    1 
ATOM   4544 C CD1   . LEU   A 1 573 ? -24.480 -99.771  -18.072 1.00 33.32  ? 565 LEU   A CD1   1 
ATOM   4545 C CD2   . LEU   A 1 573 ? -26.325 -99.015  -19.577 1.00 33.12  ? 565 LEU   A CD2   1 
ATOM   4546 N N     . SER   A 1 574 ? -23.421 -96.407  -22.546 1.00 26.93  ? 566 SER   A N     1 
ATOM   4547 C CA    . SER   A 1 574 ? -22.570 -95.361  -23.083 1.00 26.46  ? 566 SER   A CA    1 
ATOM   4548 C C     . SER   A 1 574 ? -23.024 -93.997  -22.570 1.00 26.16  ? 566 SER   A C     1 
ATOM   4549 O O     . SER   A 1 574 ? -24.209 -93.790  -22.321 1.00 25.30  ? 566 SER   A O     1 
ATOM   4550 C CB    . SER   A 1 574 ? -22.573 -95.404  -24.586 1.00 26.36  ? 566 SER   A CB    1 
ATOM   4551 O OG    . SER   A 1 574 ? -22.016 -94.217  -25.129 1.00 26.49  ? 566 SER   A OG    1 
ATOM   4552 N N     . ILE   A 1 575 ? -22.061 -93.082  -22.404 1.00 26.55  ? 567 ILE   A N     1 
ATOM   4553 C CA    . ILE   A 1 575 ? -22.365 -91.675  -22.186 1.00 27.43  ? 567 ILE   A CA    1 
ATOM   4554 C C     . ILE   A 1 575 ? -21.730 -90.827  -23.288 1.00 28.16  ? 567 ILE   A C     1 
ATOM   4555 O O     . ILE   A 1 575 ? -21.911 -89.611  -23.310 1.00 28.03  ? 567 ILE   A O     1 
ATOM   4556 C CB    . ILE   A 1 575 ? -21.930 -91.224  -20.779 1.00 27.39  ? 567 ILE   A CB    1 
ATOM   4557 C CG1   . ILE   A 1 575 ? -20.414 -91.244  -20.604 1.00 27.05  ? 567 ILE   A CG1   1 
ATOM   4558 C CG2   . ILE   A 1 575 ? -22.634 -92.064  -19.712 1.00 27.65  ? 567 ILE   A CG2   1 
ATOM   4559 C CD1   . ILE   A 1 575 ? -19.930 -90.482  -19.384 1.00 26.98  ? 567 ILE   A CD1   1 
ATOM   4560 N N     . ARG   A 1 576 ? -20.976 -91.482  -24.181 1.00 29.28  ? 568 ARG   A N     1 
ATOM   4561 C CA    . ARG   A 1 576 ? -20.537 -90.899  -25.438 1.00 29.92  ? 568 ARG   A CA    1 
ATOM   4562 C C     . ARG   A 1 576 ? -21.746 -90.299  -26.150 1.00 28.98  ? 568 ARG   A C     1 
ATOM   4563 O O     . ARG   A 1 576 ? -22.678 -91.029  -26.470 1.00 28.30  ? 568 ARG   A O     1 
ATOM   4564 C CB    . ARG   A 1 576 ? -19.890 -92.047  -26.219 1.00 30.74  ? 568 ARG   A CB    1 
ATOM   4565 C CG    . ARG   A 1 576 ? -19.347 -91.722  -27.601 1.00 32.74  ? 568 ARG   A CG    1 
ATOM   4566 C CD    . ARG   A 1 576 ? -19.056 -93.021  -28.337 1.00 33.50  ? 568 ARG   A CD    1 
ATOM   4567 N NE    . ARG   A 1 576 ? -18.553 -92.830  -29.700 1.00 34.32  ? 568 ARG   A NE    1 
ATOM   4568 C CZ    . ARG   A 1 576 ? -18.301 -93.817  -30.556 1.00 34.80  ? 568 ARG   A CZ    1 
ATOM   4569 N NH1   . ARG   A 1 576 ? -18.530 -95.076  -30.219 1.00 35.03  ? 568 ARG   A NH1   1 
ATOM   4570 N NH2   . ARG   A 1 576 ? -17.821 -93.542  -31.755 1.00 35.59  ? 568 ARG   A NH2   1 
ATOM   4571 N N     . PRO   A 1 577 ? -21.780 -88.971  -26.424 1.00 29.62  ? 569 PRO   A N     1 
ATOM   4572 C CA    . PRO   A 1 577 ? -23.008 -88.300  -26.863 1.00 30.00  ? 569 PRO   A CA    1 
ATOM   4573 C C     . PRO   A 1 577 ? -23.650 -88.929  -28.095 1.00 30.69  ? 569 PRO   A C     1 
ATOM   4574 O O     . PRO   A 1 577 ? -24.871 -88.950  -28.213 1.00 31.01  ? 569 PRO   A O     1 
ATOM   4575 C CB    . PRO   A 1 577 ? -22.568 -86.855  -27.149 1.00 29.42  ? 569 PRO   A CB    1 
ATOM   4576 C CG    . PRO   A 1 577 ? -21.293 -86.685  -26.364 1.00 29.48  ? 569 PRO   A CG    1 
ATOM   4577 C CD    . PRO   A 1 577 ? -20.632 -88.051  -26.385 1.00 29.84  ? 569 PRO   A CD    1 
ATOM   4578 N N     . GLU   A 1 578 ? -22.809 -89.434  -29.003 1.00 31.84  ? 570 GLU   A N     1 
ATOM   4579 C CA    . GLU   A 1 578 ? -23.276 -90.028  -30.245 1.00 34.03  ? 570 GLU   A CA    1 
ATOM   4580 C C     . GLU   A 1 578 ? -24.098 -91.283  -29.948 1.00 34.19  ? 570 GLU   A C     1 
ATOM   4581 O O     . GLU   A 1 578 ? -25.102 -91.530  -30.614 1.00 34.68  ? 570 GLU   A O     1 
ATOM   4582 C CB    . GLU   A 1 578 ? -22.125 -90.397  -31.185 1.00 35.30  ? 570 GLU   A CB    1 
ATOM   4583 C CG    . GLU   A 1 578 ? -21.119 -89.278  -31.444 1.00 36.50  ? 570 GLU   A CG    1 
ATOM   4584 C CD    . GLU   A 1 578 ? -20.046 -89.122  -30.375 1.00 37.75  ? 570 GLU   A CD    1 
ATOM   4585 O OE1   . GLU   A 1 578 ? -19.966 -88.024  -29.780 1.00 38.65  ? 570 GLU   A OE1   1 
ATOM   4586 O OE2   . GLU   A 1 578 ? -19.294 -90.092  -30.135 1.00 37.20  ? 570 GLU   A OE2   1 
ATOM   4587 N N     . THR   A 1 579 ? -23.668 -92.065  -28.945 1.00 32.89  ? 571 THR   A N     1 
ATOM   4588 C CA    . THR   A 1 579 ? -24.246 -93.372  -28.673 1.00 32.08  ? 571 THR   A CA    1 
ATOM   4589 C C     . THR   A 1 579 ? -24.787 -93.422  -27.244 1.00 32.33  ? 571 THR   A C     1 
ATOM   4590 O O     . THR   A 1 579 ? -24.899 -94.499  -26.666 1.00 32.20  ? 571 THR   A O     1 
ATOM   4591 C CB    . THR   A 1 579 ? -23.186 -94.453  -28.908 1.00 31.91  ? 571 THR   A CB    1 
ATOM   4592 O OG1   . THR   A 1 579 ? -22.287 -94.439  -27.803 1.00 31.41  ? 571 THR   A OG1   1 
ATOM   4593 C CG2   . THR   A 1 579 ? -22.394 -94.245  -30.187 1.00 31.80  ? 571 THR   A CG2   1 
ATOM   4594 N N     . HIS   A 1 580 ? -25.148 -92.258  -26.691 1.00 32.65  ? 572 HIS   A N     1 
ATOM   4595 C CA    . HIS   A 1 580 ? -25.496 -92.140  -25.285 1.00 32.47  ? 572 HIS   A CA    1 
ATOM   4596 C C     . HIS   A 1 580 ? -26.715 -93.005  -24.978 1.00 32.61  ? 572 HIS   A C     1 
ATOM   4597 O O     . HIS   A 1 580 ? -27.695 -92.969  -25.716 1.00 31.89  ? 572 HIS   A O     1 
ATOM   4598 C CB    . HIS   A 1 580 ? -25.753 -90.672  -24.923 1.00 32.95  ? 572 HIS   A CB    1 
ATOM   4599 C CG    . HIS   A 1 580 ? -25.756 -90.393  -23.455 1.00 33.35  ? 572 HIS   A CG    1 
ATOM   4600 N ND1   . HIS   A 1 580 ? -26.196 -91.291  -22.505 1.00 33.80  ? 572 HIS   A ND1   1 
ATOM   4601 C CD2   . HIS   A 1 580 ? -25.364 -89.305  -22.778 1.00 33.30  ? 572 HIS   A CD2   1 
ATOM   4602 C CE1   . HIS   A 1 580 ? -26.070 -90.753  -21.301 1.00 32.95  ? 572 HIS   A CE1   1 
ATOM   4603 N NE2   . HIS   A 1 580 ? -25.567 -89.548  -21.444 1.00 33.18  ? 572 HIS   A NE2   1 
ATOM   4604 N N     . SER   A 1 581 ? -26.639 -93.777  -23.884 1.00 33.20  ? 573 SER   A N     1 
ATOM   4605 C CA    . SER   A 1 581 ? -27.761 -94.576  -23.416 1.00 32.84  ? 573 SER   A CA    1 
ATOM   4606 C C     . SER   A 1 581 ? -28.894 -93.645  -22.997 1.00 34.01  ? 573 SER   A C     1 
ATOM   4607 O O     . SER   A 1 581 ? -28.710 -92.834  -22.094 1.00 35.03  ? 573 SER   A O     1 
ATOM   4608 C CB    . SER   A 1 581 ? -27.362 -95.479  -22.280 1.00 31.98  ? 573 SER   A CB    1 
ATOM   4609 O OG    . SER   A 1 581 ? -26.262 -96.304  -22.637 1.00 31.85  ? 573 SER   A OG    1 
ATOM   4610 N N     . PRO   A 1 582 ? -30.082 -93.703  -23.645 1.00 35.57  ? 574 PRO   A N     1 
ATOM   4611 C CA    . PRO   A 1 582 ? -31.162 -92.753  -23.363 1.00 35.87  ? 574 PRO   A CA    1 
ATOM   4612 C C     . PRO   A 1 582 ? -31.611 -92.776  -21.906 1.00 36.86  ? 574 PRO   A C     1 
ATOM   4613 O O     . PRO   A 1 582 ? -31.856 -93.846  -21.357 1.00 37.49  ? 574 PRO   A O     1 
ATOM   4614 C CB    . PRO   A 1 582 ? -32.288 -93.204  -24.309 1.00 35.45  ? 574 PRO   A CB    1 
ATOM   4615 C CG    . PRO   A 1 582 ? -31.571 -93.942  -25.413 1.00 35.64  ? 574 PRO   A CG    1 
ATOM   4616 C CD    . PRO   A 1 582 ? -30.443 -94.663  -24.702 1.00 35.67  ? 574 PRO   A CD    1 
ATOM   4617 N N     . GLY   A 1 583 ? -31.689 -91.588  -21.290 1.00 37.35  ? 575 GLY   A N     1 
ATOM   4618 C CA    . GLY   A 1 583 ? -32.263 -91.429  -19.962 1.00 37.71  ? 575 GLY   A CA    1 
ATOM   4619 C C     . GLY   A 1 583 ? -31.228 -91.554  -18.845 1.00 38.12  ? 575 GLY   A C     1 
ATOM   4620 O O     . GLY   A 1 583 ? -31.391 -90.955  -17.784 1.00 39.54  ? 575 GLY   A O     1 
ATOM   4621 N N     . MET   A 1 584 ? -30.165 -92.327  -19.097 1.00 37.23  ? 576 MET   A N     1 
ATOM   4622 C CA    . MET   A 1 584 ? -29.214 -92.724  -18.071 1.00 36.43  ? 576 MET   A CA    1 
ATOM   4623 C C     . MET   A 1 584 ? -28.490 -91.496  -17.520 1.00 36.89  ? 576 MET   A C     1 
ATOM   4624 O O     . MET   A 1 584 ? -27.824 -90.791  -18.272 1.00 37.86  ? 576 MET   A O     1 
ATOM   4625 C CB    . MET   A 1 584 ? -28.199 -93.700  -18.674 1.00 36.04  ? 576 MET   A CB    1 
ATOM   4626 C CG    . MET   A 1 584 ? -27.350 -94.427  -17.658 1.00 35.77  ? 576 MET   A CG    1 
ATOM   4627 S SD    . MET   A 1 584 ? -26.168 -95.518  -18.470 1.00 35.71  ? 576 MET   A SD    1 
ATOM   4628 C CE    . MET   A 1 584 ? -25.091 -94.338  -19.296 1.00 35.58  ? 576 MET   A CE    1 
ATOM   4629 N N     . PHE   A 1 585 ? -28.615 -91.264  -16.204 1.00 36.66  ? 577 PHE   A N     1 
ATOM   4630 C CA    . PHE   A 1 585 ? -28.076 -90.076  -15.552 1.00 36.41  ? 577 PHE   A CA    1 
ATOM   4631 C C     . PHE   A 1 585 ? -26.913 -90.414  -14.617 1.00 34.12  ? 577 PHE   A C     1 
ATOM   4632 O O     . PHE   A 1 585 ? -26.312 -89.511  -14.040 1.00 33.67  ? 577 PHE   A O     1 
ATOM   4633 C CB    . PHE   A 1 585 ? -29.163 -89.368  -14.736 1.00 37.65  ? 577 PHE   A CB    1 
ATOM   4634 C CG    . PHE   A 1 585 ? -29.833 -90.211  -13.658 1.00 39.11  ? 577 PHE   A CG    1 
ATOM   4635 C CD1   . PHE   A 1 585 ? -29.207 -90.447  -12.437 1.00 39.98  ? 577 PHE   A CD1   1 
ATOM   4636 C CD2   . PHE   A 1 585 ? -31.103 -90.745  -13.857 1.00 39.83  ? 577 PHE   A CD2   1 
ATOM   4637 C CE1   . PHE   A 1 585 ? -29.823 -91.212  -11.458 1.00 40.25  ? 577 PHE   A CE1   1 
ATOM   4638 C CE2   . PHE   A 1 585 ? -31.719 -91.502  -12.871 1.00 40.37  ? 577 PHE   A CE2   1 
ATOM   4639 C CZ    . PHE   A 1 585 ? -31.077 -91.735  -11.674 1.00 40.42  ? 577 PHE   A CZ    1 
ATOM   4640 N N     . SER   A 1 586 ? -26.589 -91.704  -14.473 1.00 32.16  ? 578 SER   A N     1 
ATOM   4641 C CA    . SER   A 1 586 ? -25.668 -92.157  -13.442 1.00 30.65  ? 578 SER   A CA    1 
ATOM   4642 C C     . SER   A 1 586 ? -24.246 -91.630  -13.651 1.00 29.18  ? 578 SER   A C     1 
ATOM   4643 O O     . SER   A 1 586 ? -23.453 -91.647  -12.714 1.00 28.97  ? 578 SER   A O     1 
ATOM   4644 C CB    . SER   A 1 586 ? -25.683 -93.664  -13.325 1.00 30.66  ? 578 SER   A CB    1 
ATOM   4645 O OG    . SER   A 1 586 ? -26.802 -94.101  -12.567 1.00 30.57  ? 578 SER   A OG    1 
ATOM   4646 N N     . TRP   A 1 587 ? -23.909 -91.170  -14.863 1.00 27.57  ? 579 TRP   A N     1 
ATOM   4647 C CA    . TRP   A 1 587 ? -22.608 -90.561  -15.105 1.00 26.60  ? 579 TRP   A CA    1 
ATOM   4648 C C     . TRP   A 1 587 ? -22.746 -89.271  -15.907 1.00 26.30  ? 579 TRP   A C     1 
ATOM   4649 O O     . TRP   A 1 587 ? -23.286 -89.292  -17.010 1.00 26.59  ? 579 TRP   A O     1 
ATOM   4650 C CB    . TRP   A 1 587 ? -21.690 -91.508  -15.886 1.00 26.05  ? 579 TRP   A CB    1 
ATOM   4651 C CG    . TRP   A 1 587 ? -21.333 -92.806  -15.216 1.00 25.17  ? 579 TRP   A CG    1 
ATOM   4652 C CD1   . TRP   A 1 587 ? -20.246 -93.064  -14.437 1.00 24.82  ? 579 TRP   A CD1   1 
ATOM   4653 C CD2   . TRP   A 1 587 ? -22.024 -94.060  -15.371 1.00 25.19  ? 579 TRP   A CD2   1 
ATOM   4654 N NE1   . TRP   A 1 587 ? -20.233 -94.379  -14.059 1.00 24.76  ? 579 TRP   A NE1   1 
ATOM   4655 C CE2   . TRP   A 1 587 ? -21.305 -95.018  -14.625 1.00 25.52  ? 579 TRP   A CE2   1 
ATOM   4656 C CE3   . TRP   A 1 587 ? -23.176 -94.461  -16.055 1.00 25.61  ? 579 TRP   A CE3   1 
ATOM   4657 C CZ2   . TRP   A 1 587 ? -21.707 -96.350  -14.548 1.00 25.87  ? 579 TRP   A CZ2   1 
ATOM   4658 C CZ3   . TRP   A 1 587 ? -23.565 -95.779  -15.985 1.00 25.63  ? 579 TRP   A CZ3   1 
ATOM   4659 C CH2   . TRP   A 1 587 ? -22.833 -96.711  -15.252 1.00 25.68  ? 579 TRP   A CH2   1 
ATOM   4660 N N     . PHE   A 1 588 ? -22.204 -88.169  -15.368 1.00 25.64  ? 580 PHE   A N     1 
ATOM   4661 C CA    . PHE   A 1 588 ? -21.938 -86.976  -16.157 1.00 25.50  ? 580 PHE   A CA    1 
ATOM   4662 C C     . PHE   A 1 588 ? -20.587 -87.143  -16.847 1.00 24.44  ? 580 PHE   A C     1 
ATOM   4663 O O     . PHE   A 1 588 ? -19.813 -88.022  -16.476 1.00 23.49  ? 580 PHE   A O     1 
ATOM   4664 C CB    . PHE   A 1 588 ? -21.902 -85.692  -15.320 1.00 26.55  ? 580 PHE   A CB    1 
ATOM   4665 C CG    . PHE   A 1 588 ? -23.235 -85.187  -14.785 1.00 27.68  ? 580 PHE   A CG    1 
ATOM   4666 C CD1   . PHE   A 1 588 ? -24.416 -85.373  -15.495 1.00 28.24  ? 580 PHE   A CD1   1 
ATOM   4667 C CD2   . PHE   A 1 588 ? -23.296 -84.511  -13.570 1.00 28.47  ? 580 PHE   A CD2   1 
ATOM   4668 C CE1   . PHE   A 1 588 ? -25.622 -84.908  -14.999 1.00 28.60  ? 580 PHE   A CE1   1 
ATOM   4669 C CE2   . PHE   A 1 588 ? -24.506 -84.045  -13.078 1.00 28.71  ? 580 PHE   A CE2   1 
ATOM   4670 C CZ    . PHE   A 1 588 ? -25.665 -84.245  -13.794 1.00 28.99  ? 580 PHE   A CZ    1 
ATOM   4671 N N     . PRO   A 1 589 ? -20.269 -86.322  -17.877 1.00 24.02  ? 581 PRO   A N     1 
ATOM   4672 C CA    . PRO   A 1 589 ? -18.922 -86.293  -18.452 1.00 23.46  ? 581 PRO   A CA    1 
ATOM   4673 C C     . PRO   A 1 589 ? -17.856 -85.826  -17.462 1.00 22.70  ? 581 PRO   A C     1 
ATOM   4674 O O     . PRO   A 1 589 ? -18.170 -85.237  -16.429 1.00 22.36  ? 581 PRO   A O     1 
ATOM   4675 C CB    . PRO   A 1 589 ? -19.039 -85.322  -19.643 1.00 23.55  ? 581 PRO   A CB    1 
ATOM   4676 C CG    . PRO   A 1 589 ? -20.520 -85.203  -19.912 1.00 23.61  ? 581 PRO   A CG    1 
ATOM   4677 C CD    . PRO   A 1 589 ? -21.200 -85.424  -18.578 1.00 23.49  ? 581 PRO   A CD    1 
ATOM   4678 N N     . ILE   A 1 590 ? -16.594 -86.100  -17.813 1.00 22.03  ? 582 ILE   A N     1 
ATOM   4679 C CA    . ILE   A 1 590 ? -15.439 -85.594  -17.092 1.00 21.77  ? 582 ILE   A CA    1 
ATOM   4680 C C     . ILE   A 1 590 ? -14.816 -84.486  -17.942 1.00 21.17  ? 582 ILE   A C     1 
ATOM   4681 O O     . ILE   A 1 590 ? -15.025 -84.453  -19.152 1.00 21.15  ? 582 ILE   A O     1 
ATOM   4682 C CB    . ILE   A 1 590 ? -14.457 -86.747  -16.791 1.00 22.17  ? 582 ILE   A CB    1 
ATOM   4683 C CG1   . ILE   A 1 590 ? -13.824 -86.632  -15.408 1.00 22.59  ? 582 ILE   A CG1   1 
ATOM   4684 C CG2   . ILE   A 1 590 ? -13.391 -86.883  -17.878 1.00 22.53  ? 582 ILE   A CG2   1 
ATOM   4685 C CD1   . ILE   A 1 590 ? -13.361 -87.959  -14.838 1.00 22.45  ? 582 ILE   A CD1   1 
ATOM   4686 N N     . LEU   A 1 591 ? -14.067 -83.580  -17.303 1.00 20.53  ? 583 LEU   A N     1 
ATOM   4687 C CA    . LEU   A 1 591 ? -13.341 -82.533  -18.007 1.00 19.87  ? 583 LEU   A CA    1 
ATOM   4688 C C     . LEU   A 1 591 ? -11.893 -82.516  -17.525 1.00 19.41  ? 583 LEU   A C     1 
ATOM   4689 O O     . LEU   A 1 591 ? -11.639 -82.402  -16.327 1.00 19.06  ? 583 LEU   A O     1 
ATOM   4690 C CB    . LEU   A 1 591 ? -13.998 -81.170  -17.793 1.00 19.93  ? 583 LEU   A CB    1 
ATOM   4691 C CG    . LEU   A 1 591 ? -13.149 -79.952  -18.178 1.00 19.98  ? 583 LEU   A CG    1 
ATOM   4692 C CD1   . LEU   A 1 591 ? -12.961 -79.841  -19.682 1.00 19.97  ? 583 LEU   A CD1   1 
ATOM   4693 C CD2   . LEU   A 1 591 ? -13.749 -78.679  -17.620 1.00 19.89  ? 583 LEU   A CD2   1 
ATOM   4694 N N     . PHE   A 1 592 ? -10.962 -82.619  -18.481 1.00 18.93  ? 584 PHE   A N     1 
ATOM   4695 C CA    . PHE   A 1 592 ? -9.544  -82.446  -18.221 1.00 18.91  ? 584 PHE   A CA    1 
ATOM   4696 C C     . PHE   A 1 592 ? -9.127  -81.073  -18.735 1.00 19.20  ? 584 PHE   A C     1 
ATOM   4697 O O     . PHE   A 1 592 ? -9.009  -80.873  -19.944 1.00 19.74  ? 584 PHE   A O     1 
ATOM   4698 C CB    . PHE   A 1 592 ? -8.674  -83.499  -18.913 1.00 18.61  ? 584 PHE   A CB    1 
ATOM   4699 C CG    . PHE   A 1 592 ? -8.821  -84.918  -18.389 1.00 18.33  ? 584 PHE   A CG    1 
ATOM   4700 C CD1   . PHE   A 1 592 ? -9.775  -85.779  -18.924 1.00 18.52  ? 584 PHE   A CD1   1 
ATOM   4701 C CD2   . PHE   A 1 592 ? -7.983  -85.397  -17.388 1.00 18.17  ? 584 PHE   A CD2   1 
ATOM   4702 C CE1   . PHE   A 1 592 ? -9.899  -87.079  -18.451 1.00 18.70  ? 584 PHE   A CE1   1 
ATOM   4703 C CE2   . PHE   A 1 592 ? -8.109  -86.697  -16.919 1.00 18.10  ? 584 PHE   A CE2   1 
ATOM   4704 C CZ    . PHE   A 1 592 ? -9.068  -87.535  -17.447 1.00 18.30  ? 584 PHE   A CZ    1 
ATOM   4705 N N     . PRO   A 1 593 ? -8.894  -80.087  -17.843 1.00 19.32  ? 585 PRO   A N     1 
ATOM   4706 C CA    . PRO   A 1 593 ? -8.494  -78.752  -18.277 1.00 19.49  ? 585 PRO   A CA    1 
ATOM   4707 C C     . PRO   A 1 593 ? -7.027  -78.711  -18.690 1.00 19.98  ? 585 PRO   A C     1 
ATOM   4708 O O     . PRO   A 1 593 ? -6.313  -79.703  -18.554 1.00 19.90  ? 585 PRO   A O     1 
ATOM   4709 C CB    . PRO   A 1 593 ? -8.787  -77.862  -17.060 1.00 19.43  ? 585 PRO   A CB    1 
ATOM   4710 C CG    . PRO   A 1 593 ? -8.764  -78.799  -15.866 1.00 19.42  ? 585 PRO   A CG    1 
ATOM   4711 C CD    . PRO   A 1 593 ? -9.016  -80.205  -16.382 1.00 19.34  ? 585 PRO   A CD    1 
ATOM   4712 N N     . ILE   A 1 594 ? -6.626  -77.553  -19.230 1.00 20.40  ? 586 ILE   A N     1 
ATOM   4713 C CA    . ILE   A 1 594 ? -5.233  -77.206  -19.460 1.00 20.74  ? 586 ILE   A CA    1 
ATOM   4714 C C     . ILE   A 1 594 ? -4.991  -75.810  -18.880 1.00 21.31  ? 586 ILE   A C     1 
ATOM   4715 O O     . ILE   A 1 594 ? -5.902  -74.982  -18.863 1.00 21.13  ? 586 ILE   A O     1 
ATOM   4716 C CB    . ILE   A 1 594 ? -4.886  -77.305  -20.959 1.00 20.69  ? 586 ILE   A CB    1 
ATOM   4717 C CG1   . ILE   A 1 594 ? -5.785  -76.419  -21.828 1.00 20.58  ? 586 ILE   A CG1   1 
ATOM   4718 C CG2   . ILE   A 1 594 ? -4.931  -78.761  -21.423 1.00 20.69  ? 586 ILE   A CG2   1 
ATOM   4719 C CD1   . ILE   A 1 594 ? -5.295  -76.249  -23.253 1.00 20.50  ? 586 ILE   A CD1   1 
ATOM   4720 N N     A LYS   A 1 595 ? -3.757  -75.588  -18.395 0.50 21.54  ? 587 LYS   A N     1 
ATOM   4721 N N     B LYS   A 1 595 ? -3.755  -75.545  -18.443 0.50 21.80  ? 587 LYS   A N     1 
ATOM   4722 C CA    A LYS   A 1 595 ? -3.352  -74.364  -17.717 0.50 21.67  ? 587 LYS   A CA    1 
ATOM   4723 C CA    B LYS   A 1 595 ? -3.438  -74.342  -17.689 0.50 22.10  ? 587 LYS   A CA    1 
ATOM   4724 C C     A LYS   A 1 595 ? -3.620  -73.157  -18.607 0.50 22.23  ? 587 LYS   A C     1 
ATOM   4725 C C     B LYS   A 1 595 ? -3.550  -73.106  -18.579 0.50 22.47  ? 587 LYS   A C     1 
ATOM   4726 O O     A LYS   A 1 595 ? -4.294  -72.215  -18.198 0.50 22.22  ? 587 LYS   A O     1 
ATOM   4727 O O     B LYS   A 1 595 ? -4.075  -72.085  -18.141 0.50 22.45  ? 587 LYS   A O     1 
ATOM   4728 C CB    A LYS   A 1 595 ? -1.845  -74.287  -17.437 0.50 21.53  ? 587 LYS   A CB    1 
ATOM   4729 C CB    B LYS   A 1 595 ? -2.061  -74.514  -17.038 0.50 22.29  ? 587 LYS   A CB    1 
ATOM   4730 C CG    A LYS   A 1 595 ? -1.232  -75.307  -16.490 0.50 21.63  ? 587 LYS   A CG    1 
ATOM   4731 C CG    B LYS   A 1 595 ? -2.090  -75.523  -15.901 0.50 22.71  ? 587 LYS   A CG    1 
ATOM   4732 C CD    A LYS   A 1 595 ? 0.293   -75.249  -16.491 0.50 21.54  ? 587 LYS   A CD    1 
ATOM   4733 C CD    B LYS   A 1 595 ? -0.765  -76.162  -15.504 0.50 23.01  ? 587 LYS   A CD    1 
ATOM   4734 C CE    A LYS   A 1 595 ? 0.933   -76.289  -15.626 0.50 21.55  ? 587 LYS   A CE    1 
ATOM   4735 C CE    B LYS   A 1 595 ? 0.057   -75.282  -14.630 0.50 23.05  ? 587 LYS   A CE    1 
ATOM   4736 N NZ    A LYS   A 1 595 ? 2.392   -76.152  -15.598 0.50 21.42  ? 587 LYS   A NZ    1 
ATOM   4737 N NZ    B LYS   A 1 595 ? 0.955   -76.064  -13.777 0.50 23.05  ? 587 LYS   A NZ    1 
ATOM   4738 N N     . GLN   A 1 596 ? -3.060  -73.207  -19.820 1.00 22.80  ? 588 GLN   A N     1 
ATOM   4739 C CA    . GLN   A 1 596 ? -3.112  -72.100  -20.760 1.00 24.31  ? 588 GLN   A CA    1 
ATOM   4740 C C     . GLN   A 1 596 ? -3.942  -72.503  -21.974 1.00 24.03  ? 588 GLN   A C     1 
ATOM   4741 O O     . GLN   A 1 596 ? -3.678  -73.533  -22.590 1.00 23.90  ? 588 GLN   A O     1 
ATOM   4742 C CB    . GLN   A 1 596 ? -1.697  -71.696  -21.171 1.00 26.08  ? 588 GLN   A CB    1 
ATOM   4743 C CG    . GLN   A 1 596 ? -0.950  -70.916  -20.097 1.00 27.48  ? 588 GLN   A CG    1 
ATOM   4744 C CD    . GLN   A 1 596 ? -1.598  -69.583  -19.783 1.00 29.23  ? 588 GLN   A CD    1 
ATOM   4745 O OE1   . GLN   A 1 596 ? -1.945  -68.810  -20.684 1.00 30.23  ? 588 GLN   A OE1   1 
ATOM   4746 N NE2   . GLN   A 1 596 ? -1.792  -69.308  -18.500 1.00 30.50  ? 588 GLN   A NE2   1 
ATOM   4747 N N     . PRO   A 1 597 ? -4.973  -71.706  -22.340 1.00 23.79  ? 589 PRO   A N     1 
ATOM   4748 C CA    . PRO   A 1 597 ? -5.722  -71.923  -23.577 1.00 23.56  ? 589 PRO   A CA    1 
ATOM   4749 C C     . PRO   A 1 597 ? -4.814  -71.882  -24.803 1.00 23.45  ? 589 PRO   A C     1 
ATOM   4750 O O     . PRO   A 1 597 ? -3.761  -71.254  -24.777 1.00 23.40  ? 589 PRO   A O     1 
ATOM   4751 C CB    . PRO   A 1 597 ? -6.766  -70.795  -23.612 1.00 23.97  ? 589 PRO   A CB    1 
ATOM   4752 C CG    . PRO   A 1 597 ? -6.826  -70.264  -22.196 1.00 23.86  ? 589 PRO   A CG    1 
ATOM   4753 C CD    . PRO   A 1 597 ? -5.489  -70.578  -21.554 1.00 23.88  ? 589 PRO   A CD    1 
ATOM   4754 N N     . ILE   A 1 598 ? -5.245  -72.552  -25.875 1.00 23.56  ? 590 ILE   A N     1 
ATOM   4755 C CA    . ILE   A 1 598 ? -4.437  -72.700  -27.073 1.00 24.10  ? 590 ILE   A CA    1 
ATOM   4756 C C     . ILE   A 1 598 ? -5.294  -72.356  -28.288 1.00 24.50  ? 590 ILE   A C     1 
ATOM   4757 O O     . ILE   A 1 598 ? -6.303  -73.011  -28.548 1.00 24.79  ? 590 ILE   A O     1 
ATOM   4758 C CB    . ILE   A 1 598 ? -3.850  -74.122  -27.172 1.00 24.08  ? 590 ILE   A CB    1 
ATOM   4759 C CG1   . ILE   A 1 598 ? -2.855  -74.404  -26.043 1.00 24.15  ? 590 ILE   A CG1   1 
ATOM   4760 C CG2   . ILE   A 1 598 ? -3.224  -74.361  -28.547 1.00 24.30  ? 590 ILE   A CG2   1 
ATOM   4761 C CD1   . ILE   A 1 598 ? -2.348  -75.835  -25.991 1.00 24.12  ? 590 ILE   A CD1   1 
ATOM   4762 N N     . THR   A 1 599 ? -4.863  -71.334  -29.034 1.00 24.49  ? 591 THR   A N     1 
ATOM   4763 C CA    . THR   A 1 599 ? -5.500  -70.966  -30.287 1.00 24.32  ? 591 THR   A CA    1 
ATOM   4764 C C     . THR   A 1 599 ? -5.380  -72.119  -31.281 1.00 25.35  ? 591 THR   A C     1 
ATOM   4765 O O     . THR   A 1 599 ? -4.308  -72.701  -31.441 1.00 24.70  ? 591 THR   A O     1 
ATOM   4766 C CB    . THR   A 1 599 ? -4.844  -69.697  -30.827 1.00 23.58  ? 591 THR   A CB    1 
ATOM   4767 O OG1   . THR   A 1 599 ? -5.255  -68.687  -29.913 1.00 22.91  ? 591 THR   A OG1   1 
ATOM   4768 C CG2   . THR   A 1 599 ? -5.295  -69.354  -32.236 1.00 23.50  ? 591 THR   A CG2   1 
ATOM   4769 N N     . VAL   A 1 600 ? -6.494  -72.430  -31.952 1.00 26.45  ? 592 VAL   A N     1 
ATOM   4770 C CA    . VAL   A 1 600 ? -6.480  -73.382  -33.049 1.00 27.99  ? 592 VAL   A CA    1 
ATOM   4771 C C     . VAL   A 1 600 ? -7.120  -72.714  -34.262 1.00 29.33  ? 592 VAL   A C     1 
ATOM   4772 O O     . VAL   A 1 600 ? -8.236  -72.209  -34.178 1.00 29.59  ? 592 VAL   A O     1 
ATOM   4773 C CB    . VAL   A 1 600 ? -7.194  -74.701  -32.703 1.00 28.02  ? 592 VAL   A CB    1 
ATOM   4774 C CG1   . VAL   A 1 600 ? -7.035  -75.729  -33.817 1.00 27.98  ? 592 VAL   A CG1   1 
ATOM   4775 C CG2   . VAL   A 1 600 ? -6.718  -75.271  -31.370 1.00 28.57  ? 592 VAL   A CG2   1 
ATOM   4776 N N     . ARG   A 1 601 ? -6.391  -72.710  -35.382 1.00 30.94  ? 593 ARG   A N     1 
ATOM   4777 C CA    . ARG   A 1 601 ? -6.910  -72.199  -36.636 1.00 32.99  ? 593 ARG   A CA    1 
ATOM   4778 C C     . ARG   A 1 601 ? -7.595  -73.331  -37.397 1.00 32.84  ? 593 ARG   A C     1 
ATOM   4779 O O     . ARG   A 1 601 ? -7.213  -74.494  -37.271 1.00 32.00  ? 593 ARG   A O     1 
ATOM   4780 C CB    . ARG   A 1 601 ? -5.797  -71.563  -37.476 1.00 35.30  ? 593 ARG   A CB    1 
ATOM   4781 C CG    . ARG   A 1 601 ? -5.232  -70.293  -36.857 1.00 38.08  ? 593 ARG   A CG    1 
ATOM   4782 C CD    . ARG   A 1 601 ? -4.884  -69.234  -37.893 1.00 42.01  ? 593 ARG   A CD    1 
ATOM   4783 N NE    . ARG   A 1 601 ? -3.643  -69.483  -38.638 1.00 46.23  ? 593 ARG   A NE    1 
ATOM   4784 C CZ    . ARG   A 1 601 ? -3.536  -69.761  -39.940 1.00 51.12  ? 593 ARG   A CZ    1 
ATOM   4785 N NH1   . ARG   A 1 601 ? -4.599  -70.098  -40.656 1.00 52.58  ? 593 ARG   A NH1   1 
ATOM   4786 N NH2   . ARG   A 1 601 ? -2.347  -69.746  -40.520 1.00 52.73  ? 593 ARG   A NH2   1 
ATOM   4787 N N     . GLU   A 1 602 ? -8.618  -72.966  -38.176 1.00 32.81  ? 594 GLU   A N     1 
ATOM   4788 C CA    . GLU   A 1 602 ? -9.299  -73.890  -39.067 1.00 33.85  ? 594 GLU   A CA    1 
ATOM   4789 C C     . GLU   A 1 602 ? -8.261  -74.679  -39.861 1.00 31.96  ? 594 GLU   A C     1 
ATOM   4790 O O     . GLU   A 1 602 ? -7.328  -74.100  -40.412 1.00 31.87  ? 594 GLU   A O     1 
ATOM   4791 C CB    . GLU   A 1 602 ? -10.231 -73.084  -39.973 1.00 36.72  ? 594 GLU   A CB    1 
ATOM   4792 C CG    . GLU   A 1 602 ? -10.753 -73.857  -41.181 1.00 39.52  ? 594 GLU   A CG    1 
ATOM   4793 C CD    . GLU   A 1 602 ? -11.487 -72.989  -42.185 1.00 41.84  ? 594 GLU   A CD    1 
ATOM   4794 O OE1   . GLU   A 1 602 ? -10.923 -71.949  -42.598 1.00 43.53  ? 594 GLU   A OE1   1 
ATOM   4795 O OE2   . GLU   A 1 602 ? -12.617 -73.366  -42.566 1.00 44.05  ? 594 GLU   A OE2   1 
ATOM   4796 N N     . GLY   A 1 603 ? -8.426  -76.005  -39.899 1.00 30.80  ? 595 GLY   A N     1 
ATOM   4797 C CA    . GLY   A 1 603 ? -7.533  -76.872  -40.649 1.00 30.68  ? 595 GLY   A CA    1 
ATOM   4798 C C     . GLY   A 1 603 ? -6.565  -77.641  -39.751 1.00 30.11  ? 595 GLY   A C     1 
ATOM   4799 O O     . GLY   A 1 603 ? -6.214  -78.778  -40.058 1.00 31.31  ? 595 GLY   A O     1 
ATOM   4800 N N     . GLN   A 1 604 ? -6.140  -77.022  -38.643 1.00 29.01  ? 596 GLN   A N     1 
ATOM   4801 C CA    . GLN   A 1 604 ? -5.091  -77.585  -37.808 1.00 28.26  ? 596 GLN   A CA    1 
ATOM   4802 C C     . GLN   A 1 604 ? -5.589  -78.834  -37.082 1.00 27.19  ? 596 GLN   A C     1 
ATOM   4803 O O     . GLN   A 1 604 ? -6.788  -79.008  -36.871 1.00 26.61  ? 596 GLN   A O     1 
ATOM   4804 C CB    . GLN   A 1 604 ? -4.576  -76.541  -36.818 1.00 28.34  ? 596 GLN   A CB    1 
ATOM   4805 C CG    . GLN   A 1 604 ? -3.932  -75.334  -37.490 1.00 28.85  ? 596 GLN   A CG    1 
ATOM   4806 C CD    . GLN   A 1 604 ? -3.336  -74.352  -36.505 1.00 29.46  ? 596 GLN   A CD    1 
ATOM   4807 O OE1   . GLN   A 1 604 ? -4.007  -73.889  -35.576 1.00 30.73  ? 596 GLN   A OE1   1 
ATOM   4808 N NE2   . GLN   A 1 604 ? -2.064  -74.030  -36.689 1.00 29.38  ? 596 GLN   A NE2   1 
ATOM   4809 N N     . THR   A 1 605 ? -4.635  -79.706  -36.732 1.00 26.13  ? 597 THR   A N     1 
ATOM   4810 C CA    . THR   A 1 605 ? -4.892  -80.874  -35.908 1.00 25.88  ? 597 THR   A CA    1 
ATOM   4811 C C     . THR   A 1 605 ? -4.454  -80.572  -34.475 1.00 25.25  ? 597 THR   A C     1 
ATOM   4812 O O     . THR   A 1 605 ? -3.372  -80.031  -34.254 1.00 25.41  ? 597 THR   A O     1 
ATOM   4813 C CB    . THR   A 1 605 ? -4.146  -82.076  -36.485 1.00 26.04  ? 597 THR   A CB    1 
ATOM   4814 O OG1   . THR   A 1 605 ? -4.666  -82.258  -37.797 1.00 25.68  ? 597 THR   A OG1   1 
ATOM   4815 C CG2   . THR   A 1 605 ? -4.359  -83.350  -35.685 1.00 26.21  ? 597 THR   A CG2   1 
ATOM   4816 N N     . ILE   A 1 606 ? -5.322  -80.903  -33.513 1.00 24.62  ? 598 ILE   A N     1 
ATOM   4817 C CA    . ILE   A 1 606 ? -4.955  -80.939  -32.107 1.00 23.91  ? 598 ILE   A CA    1 
ATOM   4818 C C     . ILE   A 1 606 ? -4.383  -82.320  -31.806 1.00 23.06  ? 598 ILE   A C     1 
ATOM   4819 O O     . ILE   A 1 606 ? -5.058  -83.322  -32.024 1.00 22.31  ? 598 ILE   A O     1 
ATOM   4820 C CB    . ILE   A 1 606 ? -6.168  -80.637  -31.209 1.00 24.14  ? 598 ILE   A CB    1 
ATOM   4821 C CG1   . ILE   A 1 606 ? -6.644  -79.194  -31.371 1.00 24.55  ? 598 ILE   A CG1   1 
ATOM   4822 C CG2   . ILE   A 1 606 ? -5.864  -80.969  -29.747 1.00 24.28  ? 598 ILE   A CG2   1 
ATOM   4823 C CD1   . ILE   A 1 606 ? -8.034  -78.941  -30.817 1.00 24.79  ? 598 ILE   A CD1   1 
ATOM   4824 N N     . CYS   A 1 607 ? -3.144  -82.361  -31.306 1.00 22.71  ? 599 CYS   A N     1 
ATOM   4825 C CA    . CYS   A 1 607 ? -2.540  -83.607  -30.863 1.00 22.66  ? 599 CYS   A CA    1 
ATOM   4826 C C     . CYS   A 1 607 ? -2.423  -83.600  -29.341 1.00 21.52  ? 599 CYS   A C     1 
ATOM   4827 O O     . CYS   A 1 607 ? -1.768  -82.724  -28.781 1.00 20.77  ? 599 CYS   A O     1 
ATOM   4828 C CB    . CYS   A 1 607 ? -1.172  -83.823  -31.497 1.00 23.13  ? 599 CYS   A CB    1 
ATOM   4829 S SG    . CYS   A 1 607 ? -0.395  -85.380  -30.994 1.00 24.35  ? 599 CYS   A SG    1 
ATOM   4830 N N     . VAL   A 1 608 ? -3.065  -84.579  -28.689 1.00 21.14  ? 600 VAL   A N     1 
ATOM   4831 C CA    . VAL   A 1 608 ? -3.033  -84.690  -27.239 1.00 21.04  ? 600 VAL   A CA    1 
ATOM   4832 C C     . VAL   A 1 608 ? -2.415  -86.033  -26.857 1.00 21.33  ? 600 VAL   A C     1 
ATOM   4833 O O     . VAL   A 1 608 ? -2.536  -87.019  -27.582 1.00 21.09  ? 600 VAL   A O     1 
ATOM   4834 C CB    . VAL   A 1 608 ? -4.426  -84.515  -26.602 1.00 20.77  ? 600 VAL   A CB    1 
ATOM   4835 C CG1   . VAL   A 1 608 ? -5.350  -85.685  -26.912 1.00 20.87  ? 600 VAL   A CG1   1 
ATOM   4836 C CG2   . VAL   A 1 608 ? -4.343  -84.292  -25.097 1.00 20.79  ? 600 VAL   A CG2   1 
ATOM   4837 N N     . ARG   A 1 609 ? -1.754  -86.038  -25.696 1.00 21.61  ? 601 ARG   A N     1 
ATOM   4838 C CA    . ARG   A 1 609 ? -1.102  -87.212  -25.150 1.00 22.10  ? 601 ARG   A CA    1 
ATOM   4839 C C     . ARG   A 1 609 ? -1.750  -87.528  -23.807 1.00 22.02  ? 601 ARG   A C     1 
ATOM   4840 O O     . ARG   A 1 609 ? -2.009  -86.616  -23.029 1.00 22.00  ? 601 ARG   A O     1 
ATOM   4841 C CB    . ARG   A 1 609 ? 0.383   -86.892  -24.958 1.00 22.78  ? 601 ARG   A CB    1 
ATOM   4842 C CG    . ARG   A 1 609 ? 1.066   -86.274  -26.169 1.00 23.58  ? 601 ARG   A CG    1 
ATOM   4843 C CD    . ARG   A 1 609 ? 1.566   -87.311  -27.160 1.00 23.78  ? 601 ARG   A CD    1 
ATOM   4844 N NE    . ARG   A 1 609 ? 2.270   -86.677  -28.280 1.00 24.11  ? 601 ARG   A NE    1 
ATOM   4845 C CZ    . ARG   A 1 609 ? 3.110   -87.290  -29.107 1.00 23.85  ? 601 ARG   A CZ    1 
ATOM   4846 N NH1   . ARG   A 1 609 ? 3.342   -88.587  -28.987 1.00 23.92  ? 601 ARG   A NH1   1 
ATOM   4847 N NH2   . ARG   A 1 609 ? 3.717   -86.601  -30.057 1.00 23.24  ? 601 ARG   A NH2   1 
ATOM   4848 N N     . PHE   A 1 610 ? -2.007  -88.813  -23.542 1.00 22.23  ? 602 PHE   A N     1 
ATOM   4849 C CA    . PHE   A 1 610 ? -2.640  -89.221  -22.299 1.00 23.20  ? 602 PHE   A CA    1 
ATOM   4850 C C     . PHE   A 1 610 ? -1.924  -90.441  -21.729 1.00 23.17  ? 602 PHE   A C     1 
ATOM   4851 O O     . PHE   A 1 610 ? -1.768  -91.451  -22.410 1.00 23.74  ? 602 PHE   A O     1 
ATOM   4852 C CB    . PHE   A 1 610 ? -4.139  -89.474  -22.496 1.00 23.57  ? 602 PHE   A CB    1 
ATOM   4853 C CG    . PHE   A 1 610 ? -5.025  -88.385  -21.909 1.00 23.65  ? 602 PHE   A CG    1 
ATOM   4854 C CD1   . PHE   A 1 610 ? -5.268  -87.205  -22.603 1.00 23.94  ? 602 PHE   A CD1   1 
ATOM   4855 C CD2   . PHE   A 1 610 ? -5.603  -88.542  -20.654 1.00 24.37  ? 602 PHE   A CD2   1 
ATOM   4856 C CE1   . PHE   A 1 610 ? -6.073  -86.217  -22.058 1.00 23.88  ? 602 PHE   A CE1   1 
ATOM   4857 C CE2   . PHE   A 1 610 ? -6.401  -87.546  -20.110 1.00 24.46  ? 602 PHE   A CE2   1 
ATOM   4858 C CZ    . PHE   A 1 610 ? -6.638  -86.389  -20.816 1.00 24.34  ? 602 PHE   A CZ    1 
ATOM   4859 N N     . TRP   A 1 611 ? -1.502  -90.314  -20.467 1.00 23.22  ? 603 TRP   A N     1 
ATOM   4860 C CA    . TRP   A 1 611 ? -0.925  -91.411  -19.712 1.00 22.79  ? 603 TRP   A CA    1 
ATOM   4861 C C     . TRP   A 1 611 ? -1.871  -91.814  -18.589 1.00 23.28  ? 603 TRP   A C     1 
ATOM   4862 O O     . TRP   A 1 611 ? -2.460  -90.959  -17.933 1.00 23.24  ? 603 TRP   A O     1 
ATOM   4863 C CB    . TRP   A 1 611 ? 0.424   -91.007  -19.106 1.00 22.20  ? 603 TRP   A CB    1 
ATOM   4864 C CG    . TRP   A 1 611 ? 1.498   -90.661  -20.100 1.00 22.11  ? 603 TRP   A CG    1 
ATOM   4865 C CD1   . TRP   A 1 611 ? 2.465   -91.486  -20.593 1.00 21.80  ? 603 TRP   A CD1   1 
ATOM   4866 C CD2   . TRP   A 1 611 ? 1.734   -89.365  -20.689 1.00 21.80  ? 603 TRP   A CD2   1 
ATOM   4867 N NE1   . TRP   A 1 611 ? 3.278   -90.800  -21.456 1.00 21.42  ? 603 TRP   A NE1   1 
ATOM   4868 C CE2   . TRP   A 1 611 ? 2.858   -89.498  -21.529 1.00 21.32  ? 603 TRP   A CE2   1 
ATOM   4869 C CE3   . TRP   A 1 611 ? 1.113   -88.117  -20.584 1.00 21.63  ? 603 TRP   A CE3   1 
ATOM   4870 C CZ2   . TRP   A 1 611 ? 3.366   -88.428  -22.257 1.00 21.58  ? 603 TRP   A CZ2   1 
ATOM   4871 C CZ3   . TRP   A 1 611 ? 1.619   -87.058  -21.303 1.00 21.73  ? 603 TRP   A CZ3   1 
ATOM   4872 C CH2   . TRP   A 1 611 ? 2.733   -87.213  -22.125 1.00 21.60  ? 603 TRP   A CH2   1 
ATOM   4873 N N     . ARG   A 1 612 ? -1.988  -93.127  -18.375 1.00 23.95  ? 604 ARG   A N     1 
ATOM   4874 C CA    . ARG   A 1 612 ? -2.447  -93.666  -17.106 1.00 23.43  ? 604 ARG   A CA    1 
ATOM   4875 C C     . ARG   A 1 612 ? -1.212  -94.190  -16.381 1.00 22.58  ? 604 ARG   A C     1 
ATOM   4876 O O     . ARG   A 1 612 ? -0.481  -95.009  -16.932 1.00 22.43  ? 604 ARG   A O     1 
ATOM   4877 C CB    . ARG   A 1 612 ? -3.493  -94.764  -17.330 1.00 24.00  ? 604 ARG   A CB    1 
ATOM   4878 C CG    . ARG   A 1 612 ? -4.316  -95.152  -16.109 1.00 24.41  ? 604 ARG   A CG    1 
ATOM   4879 C CD    . ARG   A 1 612 ? -5.391  -96.157  -16.500 1.00 24.84  ? 604 ARG   A CD    1 
ATOM   4880 N NE    . ARG   A 1 612 ? -6.355  -96.481  -15.442 1.00 25.15  ? 604 ARG   A NE    1 
ATOM   4881 C CZ    . ARG   A 1 612 ? -6.184  -97.344  -14.443 1.00 25.95  ? 604 ARG   A CZ    1 
ATOM   4882 N NH1   . ARG   A 1 612 ? -5.023  -97.955  -14.260 1.00 26.30  ? 604 ARG   A NH1   1 
ATOM   4883 N NH2   . ARG   A 1 612 ? -7.188  -97.585  -13.617 1.00 26.31  ? 604 ARG   A NH2   1 
ATOM   4884 N N     . CYS   A 1 613 ? -0.976  -93.674  -15.169 1.00 21.70  ? 605 CYS   A N     1 
ATOM   4885 C CA    . CYS   A 1 613 ? 0.221   -93.982  -14.405 1.00 21.39  ? 605 CYS   A CA    1 
ATOM   4886 C C     . CYS   A 1 613 ? -0.164  -94.583  -13.059 1.00 21.35  ? 605 CYS   A C     1 
ATOM   4887 O O     . CYS   A 1 613 ? -1.288  -94.409  -12.594 1.00 20.10  ? 605 CYS   A O     1 
ATOM   4888 C CB    . CYS   A 1 613 ? 1.042   -92.729  -14.137 1.00 21.17  ? 605 CYS   A CB    1 
ATOM   4889 S SG    . CYS   A 1 613 ? 1.517   -91.840  -15.639 1.00 20.67  ? 605 CYS   A SG    1 
ATOM   4890 N N     . SER   A 1 614 ? 0.790   -95.283  -12.439 1.00 22.01  ? 606 SER   A N     1 
ATOM   4891 C CA    . SER   A 1 614 ? 0.543   -95.901  -11.150 1.00 23.13  ? 606 SER   A CA    1 
ATOM   4892 C C     . SER   A 1 614 ? 1.853   -96.200  -10.430 1.00 24.55  ? 606 SER   A C     1 
ATOM   4893 O O     . SER   A 1 614 ? 2.912   -96.297  -11.050 1.00 24.93  ? 606 SER   A O     1 
ATOM   4894 C CB    . SER   A 1 614 ? -0.284  -97.157  -11.299 1.00 22.71  ? 606 SER   A CB    1 
ATOM   4895 O OG    . SER   A 1 614 ? 0.453   -98.180  -11.953 1.00 22.22  ? 606 SER   A OG    1 
ATOM   4896 N N     . ASN   A 1 615 ? 1.743   -96.300  -9.102  1.00 25.74  ? 607 ASN   A N     1 
ATOM   4897 C CA    . ASN   A 1 615 ? 2.652   -97.079  -8.281  1.00 26.62  ? 607 ASN   A CA    1 
ATOM   4898 C C     . ASN   A 1 615 ? 1.774   -98.010  -7.446  1.00 27.71  ? 607 ASN   A C     1 
ATOM   4899 O O     . ASN   A 1 615 ? 0.591   -98.165  -7.741  1.00 27.68  ? 607 ASN   A O     1 
ATOM   4900 C CB    . ASN   A 1 615 ? 3.611   -96.173  -7.514  1.00 27.02  ? 607 ASN   A CB    1 
ATOM   4901 C CG    . ASN   A 1 615 ? 2.913   -95.296  -6.503  1.00 27.79  ? 607 ASN   A CG    1 
ATOM   4902 O OD1   . ASN   A 1 615 ? 1.769   -95.565  -6.120  1.00 29.45  ? 607 ASN   A OD1   1 
ATOM   4903 N ND2   . ASN   A 1 615 ? 3.593   -94.260  -6.034  1.00 27.75  ? 607 ASN   A ND2   1 
ATOM   4904 N N     . SER   A 1 616 ? 2.344   -98.619  -6.401  1.00 29.26  ? 608 SER   A N     1 
ATOM   4905 C CA    . SER   A 1 616 ? 1.624   -99.602  -5.607  1.00 30.23  ? 608 SER   A CA    1 
ATOM   4906 C C     . SER   A 1 616 ? 0.530   -98.950  -4.760  1.00 31.11  ? 608 SER   A C     1 
ATOM   4907 O O     . SER   A 1 616 ? -0.356  -99.646  -4.270  1.00 31.37  ? 608 SER   A O     1 
ATOM   4908 C CB    . SER   A 1 616 ? 2.574   -100.376 -4.737  1.00 30.74  ? 608 SER   A CB    1 
ATOM   4909 O OG    . SER   A 1 616 ? 3.214   -99.510  -3.810  1.00 30.91  ? 608 SER   A OG    1 
ATOM   4910 N N     . LYS   A 1 617 ? 0.595   -97.622  -4.587  1.00 30.97  ? 609 LYS   A N     1 
ATOM   4911 C CA    . LYS   A 1 617 ? -0.275  -96.930  -3.649  1.00 31.32  ? 609 LYS   A CA    1 
ATOM   4912 C C     . LYS   A 1 617 ? -1.363  -96.118  -4.347  1.00 29.95  ? 609 LYS   A C     1 
ATOM   4913 O O     . LYS   A 1 617 ? -2.425  -95.909  -3.763  1.00 28.73  ? 609 LYS   A O     1 
ATOM   4914 C CB    . LYS   A 1 617 ? 0.540   -95.998  -2.750  1.00 32.23  ? 609 LYS   A CB    1 
ATOM   4915 C CG    . LYS   A 1 617 ? 1.566   -96.719  -1.903  1.00 32.84  ? 609 LYS   A CG    1 
ATOM   4916 C CD    . LYS   A 1 617 ? 1.967   -95.924  -0.673  1.00 34.00  ? 609 LYS   A CD    1 
ATOM   4917 C CE    . LYS   A 1 617 ? 3.023   -96.620  0.104   1.00 34.68  ? 609 LYS   A CE    1 
ATOM   4918 N NZ    . LYS   A 1 617 ? 3.552   -95.729  1.136   1.00 35.64  ? 609 LYS   A NZ    1 
ATOM   4919 N N     . LYS   A 1 618 ? -1.101  -95.634  -5.568  1.00 29.19  ? 610 LYS   A N     1 
ATOM   4920 C CA    . LYS   A 1 618 ? -2.029  -94.710  -6.199  1.00 28.74  ? 610 LYS   A CA    1 
ATOM   4921 C C     . LYS   A 1 618 ? -1.951  -94.794  -7.720  1.00 27.24  ? 610 LYS   A C     1 
ATOM   4922 O O     . LYS   A 1 618 ? -0.979  -95.294  -8.283  1.00 27.33  ? 610 LYS   A O     1 
ATOM   4923 C CB    . LYS   A 1 618 ? -1.748  -93.290  -5.698  1.00 30.10  ? 610 LYS   A CB    1 
ATOM   4924 C CG    . LYS   A 1 618 ? -0.383  -92.754  -6.089  1.00 31.88  ? 610 LYS   A CG    1 
ATOM   4925 C CD    . LYS   A 1 618 ? 0.180   -91.654  -5.198  1.00 33.76  ? 610 LYS   A CD    1 
ATOM   4926 C CE    . LYS   A 1 618 ? 1.445   -91.113  -5.802  1.00 35.44  ? 610 LYS   A CE    1 
ATOM   4927 N NZ    . LYS   A 1 618 ? 2.169   -90.187  -4.926  1.00 36.96  ? 610 LYS   A NZ    1 
ATOM   4928 N N     . VAL   A 1 619 ? -3.013  -94.283  -8.354  1.00 25.36  ? 611 VAL   A N     1 
ATOM   4929 C CA    . VAL   A 1 619 ? -3.167  -94.257  -9.798  1.00 24.26  ? 611 VAL   A CA    1 
ATOM   4930 C C     . VAL   A 1 619 ? -3.512  -92.826  -10.194 1.00 23.46  ? 611 VAL   A C     1 
ATOM   4931 O O     . VAL   A 1 619 ? -4.194  -92.131  -9.442  1.00 23.86  ? 611 VAL   A O     1 
ATOM   4932 C CB    . VAL   A 1 619 ? -4.277  -95.245  -10.211 1.00 24.07  ? 611 VAL   A CB    1 
ATOM   4933 C CG1   . VAL   A 1 619 ? -4.579  -95.190  -11.704 1.00 23.98  ? 611 VAL   A CG1   1 
ATOM   4934 C CG2   . VAL   A 1 619 ? -3.960  -96.673  -9.782  1.00 24.11  ? 611 VAL   A CG2   1 
ATOM   4935 N N     . TRP   A 1 620 ? -3.044  -92.384  -11.368 1.00 22.09  ? 612 TRP   A N     1 
ATOM   4936 C CA    . TRP   A 1 620 ? -3.328  -91.029  -11.812 1.00 21.28  ? 612 TRP   A CA    1 
ATOM   4937 C C     . TRP   A 1 620 ? -3.174  -90.901  -13.325 1.00 20.82  ? 612 TRP   A C     1 
ATOM   4938 O O     . TRP   A 1 620 ? -2.597  -91.766  -13.978 1.00 21.22  ? 612 TRP   A O     1 
ATOM   4939 C CB    . TRP   A 1 620 ? -2.435  -90.023  -11.069 1.00 20.79  ? 612 TRP   A CB    1 
ATOM   4940 C CG    . TRP   A 1 620 ? -0.968  -90.105  -11.400 1.00 20.65  ? 612 TRP   A CG    1 
ATOM   4941 C CD1   . TRP   A 1 620 ? -0.303  -89.365  -12.331 1.00 20.88  ? 612 TRP   A CD1   1 
ATOM   4942 C CD2   . TRP   A 1 620 ? 0.024   -90.958  -10.785 1.00 20.78  ? 612 TRP   A CD2   1 
ATOM   4943 N NE1   . TRP   A 1 620 ? 1.024   -89.700  -12.348 1.00 21.02  ? 612 TRP   A NE1   1 
ATOM   4944 C CE2   . TRP   A 1 620 ? 1.256   -90.670  -11.410 1.00 20.58  ? 612 TRP   A CE2   1 
ATOM   4945 C CE3   . TRP   A 1 620 ? -0.007  -91.928  -9.777  1.00 20.84  ? 612 TRP   A CE3   1 
ATOM   4946 C CZ2   . TRP   A 1 620 ? 2.437   -91.320  -11.063 1.00 20.45  ? 612 TRP   A CZ2   1 
ATOM   4947 C CZ3   . TRP   A 1 620 ? 1.164   -92.566  -9.430  1.00 20.76  ? 612 TRP   A CZ3   1 
ATOM   4948 C CH2   . TRP   A 1 620 ? 2.368   -92.264  -10.065 1.00 20.54  ? 612 TRP   A CH2   1 
ATOM   4949 N N     . TYR   A 1 621 ? -3.726  -89.810  -13.867 1.00 20.41  ? 613 TYR   A N     1 
ATOM   4950 C CA    . TYR   A 1 621 ? -3.542  -89.456  -15.263 1.00 20.29  ? 613 TYR   A CA    1 
ATOM   4951 C C     . TYR   A 1 621 ? -2.555  -88.295  -15.355 1.00 20.12  ? 613 TYR   A C     1 
ATOM   4952 O O     . TYR   A 1 621 ? -2.500  -87.449  -14.464 1.00 19.56  ? 613 TYR   A O     1 
ATOM   4953 C CB    . TYR   A 1 621 ? -4.868  -89.076  -15.929 1.00 20.51  ? 613 TYR   A CB    1 
ATOM   4954 C CG    . TYR   A 1 621 ? -5.952  -90.146  -15.904 1.00 20.75  ? 613 TYR   A CG    1 
ATOM   4955 C CD1   . TYR   A 1 621 ? -5.885  -91.262  -16.731 1.00 20.91  ? 613 TYR   A CD1   1 
ATOM   4956 C CD2   . TYR   A 1 621 ? -7.064  -90.019  -15.080 1.00 21.22  ? 613 TYR   A CD2   1 
ATOM   4957 C CE1   . TYR   A 1 621 ? -6.874  -92.232  -16.716 1.00 21.08  ? 613 TYR   A CE1   1 
ATOM   4958 C CE2   . TYR   A 1 621 ? -8.059  -90.982  -15.055 1.00 21.52  ? 613 TYR   A CE2   1 
ATOM   4959 C CZ    . TYR   A 1 621 ? -7.967  -92.089  -15.879 1.00 21.51  ? 613 TYR   A CZ    1 
ATOM   4960 O OH    . TYR   A 1 621 ? -8.954  -93.030  -15.851 1.00 22.12  ? 613 TYR   A OH    1 
ATOM   4961 N N     . GLU   A 1 622 ? -1.754  -88.298  -16.426 1.00 20.12  ? 614 GLU   A N     1 
ATOM   4962 C CA    . GLU   A 1 622 ? -1.007  -87.130  -16.867 1.00 20.25  ? 614 GLU   A CA    1 
ATOM   4963 C C     . GLU   A 1 622 ? -1.421  -86.855  -18.308 1.00 19.54  ? 614 GLU   A C     1 
ATOM   4964 O O     . GLU   A 1 622 ? -1.892  -87.761  -18.989 1.00 19.46  ? 614 GLU   A O     1 
ATOM   4965 C CB    . GLU   A 1 622 ? 0.509   -87.335  -16.822 1.00 20.79  ? 614 GLU   A CB    1 
ATOM   4966 C CG    . GLU   A 1 622 ? 1.011   -87.966  -15.527 1.00 21.13  ? 614 GLU   A CG    1 
ATOM   4967 C CD    . GLU   A 1 622 ? 2.513   -87.906  -15.284 1.00 21.75  ? 614 GLU   A CD    1 
ATOM   4968 O OE1   . GLU   A 1 622 ? 3.269   -87.301  -16.077 1.00 21.77  ? 614 GLU   A OE1   1 
ATOM   4969 O OE2   . GLU   A 1 622 ? 2.926   -88.483  -14.255 1.00 22.29  ? 614 GLU   A OE2   1 
ATOM   4970 N N     . TRP   A 1 623 ? -1.249  -85.614  -18.775 1.00 19.35  ? 615 TRP   A N     1 
ATOM   4971 C CA    . TRP   A 1 623 ? -1.630  -85.290  -20.139 1.00 19.39  ? 615 TRP   A CA    1 
ATOM   4972 C C     . TRP   A 1 623 ? -0.893  -84.059  -20.653 1.00 19.83  ? 615 TRP   A C     1 
ATOM   4973 O O     . TRP   A 1 623 ? -0.422  -83.233  -19.876 1.00 19.94  ? 615 TRP   A O     1 
ATOM   4974 C CB    . TRP   A 1 623 ? -3.151  -85.117  -20.258 1.00 19.04  ? 615 TRP   A CB    1 
ATOM   4975 C CG    . TRP   A 1 623 ? -3.742  -84.017  -19.418 1.00 18.76  ? 615 TRP   A CG    1 
ATOM   4976 C CD1   . TRP   A 1 623 ? -4.042  -82.748  -19.816 1.00 18.95  ? 615 TRP   A CD1   1 
ATOM   4977 C CD2   . TRP   A 1 623 ? -4.137  -84.106  -18.033 1.00 18.64  ? 615 TRP   A CD2   1 
ATOM   4978 N NE1   . TRP   A 1 623 ? -4.586  -82.038  -18.778 1.00 18.70  ? 615 TRP   A NE1   1 
ATOM   4979 C CE2   . TRP   A 1 623 ? -4.659  -82.845  -17.674 1.00 18.61  ? 615 TRP   A CE2   1 
ATOM   4980 C CE3   . TRP   A 1 623 ? -4.098  -85.119  -17.069 1.00 18.57  ? 615 TRP   A CE3   1 
ATOM   4981 C CZ2   . TRP   A 1 623 ? -5.133  -82.577  -16.392 1.00 18.46  ? 615 TRP   A CZ2   1 
ATOM   4982 C CZ3   . TRP   A 1 623 ? -4.569  -84.852  -15.804 1.00 18.51  ? 615 TRP   A CZ3   1 
ATOM   4983 C CH2   . TRP   A 1 623 ? -5.083  -83.600  -15.475 1.00 18.50  ? 615 TRP   A CH2   1 
ATOM   4984 N N     . ALA   A 1 624 ? -0.805  -83.968  -21.985 1.00 20.26  ? 616 ALA   A N     1 
ATOM   4985 C CA    . ALA   A 1 624 ? -0.124  -82.871  -22.650 1.00 21.04  ? 616 ALA   A CA    1 
ATOM   4986 C C     . ALA   A 1 624 ? -0.670  -82.699  -24.064 1.00 21.15  ? 616 ALA   A C     1 
ATOM   4987 O O     . ALA   A 1 624 ? -1.074  -83.671  -24.696 1.00 21.46  ? 616 ALA   A O     1 
ATOM   4988 C CB    . ALA   A 1 624 ? 1.365   -83.129  -22.674 1.00 21.27  ? 616 ALA   A CB    1 
ATOM   4989 N N     . VAL   A 1 625 ? -0.681  -81.446  -24.533 1.00 21.35  ? 617 VAL   A N     1 
ATOM   4990 C CA    . VAL   A 1 625 ? -0.940  -81.122  -25.925 1.00 21.85  ? 617 VAL   A CA    1 
ATOM   4991 C C     . VAL   A 1 625 ? 0.408   -80.928  -26.612 1.00 22.55  ? 617 VAL   A C     1 
ATOM   4992 O O     . VAL   A 1 625 ? 1.284   -80.281  -26.052 1.00 22.75  ? 617 VAL   A O     1 
ATOM   4993 C CB    . VAL   A 1 625 ? -1.820  -79.861  -26.029 1.00 21.76  ? 617 VAL   A CB    1 
ATOM   4994 C CG1   . VAL   A 1 625 ? -1.987  -79.385  -27.469 1.00 21.85  ? 617 VAL   A CG1   1 
ATOM   4995 C CG2   . VAL   A 1 625 ? -3.181  -80.079  -25.382 1.00 21.88  ? 617 VAL   A CG2   1 
ATOM   4996 N N     . THR   A 1 626 ? 0.569   -81.494  -27.815 1.00 23.09  ? 618 THR   A N     1 
ATOM   4997 C CA    . THR   A 1 626 ? 1.837   -81.418  -28.526 1.00 23.65  ? 618 THR   A CA    1 
ATOM   4998 C C     . THR   A 1 626 ? 1.675   -80.640  -29.831 1.00 24.07  ? 618 THR   A C     1 
ATOM   4999 O O     . THR   A 1 626 ? 2.637   -80.031  -30.294 1.00 24.10  ? 618 THR   A O     1 
ATOM   5000 C CB    . THR   A 1 626 ? 2.422   -82.815  -28.749 1.00 23.46  ? 618 THR   A CB    1 
ATOM   5001 O OG1   . THR   A 1 626 ? 1.402   -83.674  -29.249 1.00 23.25  ? 618 THR   A OG1   1 
ATOM   5002 C CG2   . THR   A 1 626 ? 2.972   -83.400  -27.460 1.00 23.58  ? 618 THR   A CG2   1 
ATOM   5003 N N     . ALA   A 1 627 ? 0.464   -80.649  -30.405 1.00 24.74  ? 619 ALA   A N     1 
ATOM   5004 C CA    . ALA   A 1 627 ? 0.156   -79.851  -31.586 1.00 25.06  ? 619 ALA   A CA    1 
ATOM   5005 C C     . ALA   A 1 627 ? -1.196  -79.165  -31.404 1.00 24.95  ? 619 ALA   A C     1 
ATOM   5006 O O     . ALA   A 1 627 ? -2.099  -79.752  -30.815 1.00 24.13  ? 619 ALA   A O     1 
ATOM   5007 C CB    . ALA   A 1 627 ? 0.171   -80.729  -32.819 1.00 24.60  ? 619 ALA   A CB    1 
ATOM   5008 N N     . PRO   A 1 628 ? -1.410  -77.927  -31.914 1.00 26.00  ? 620 PRO   A N     1 
ATOM   5009 C CA    . PRO   A 1 628 ? -0.429  -77.205  -32.732 1.00 26.87  ? 620 PRO   A CA    1 
ATOM   5010 C C     . PRO   A 1 628 ? 0.688   -76.482  -31.981 1.00 28.58  ? 620 PRO   A C     1 
ATOM   5011 O O     . PRO   A 1 628 ? 1.582   -75.912  -32.601 1.00 29.95  ? 620 PRO   A O     1 
ATOM   5012 C CB    . PRO   A 1 628 ? -1.359  -76.207  -33.442 1.00 26.44  ? 620 PRO   A CB    1 
ATOM   5013 C CG    . PRO   A 1 628 ? -2.343  -75.817  -32.371 1.00 25.85  ? 620 PRO   A CG    1 
ATOM   5014 C CD    . PRO   A 1 628 ? -2.647  -77.151  -31.716 1.00 26.13  ? 620 PRO   A CD    1 
ATOM   5015 N N     . VAL   A 1 629 ? 0.598   -76.472  -30.647 1.00 28.79  ? 621 VAL   A N     1 
ATOM   5016 C CA    . VAL   A 1 629 ? 1.681   -76.027  -29.785 1.00 29.11  ? 621 VAL   A CA    1 
ATOM   5017 C C     . VAL   A 1 629 ? 1.738   -76.995  -28.608 1.00 29.11  ? 621 VAL   A C     1 
ATOM   5018 O O     . VAL   A 1 629 ? 0.849   -77.830  -28.458 1.00 29.21  ? 621 VAL   A O     1 
ATOM   5019 C CB    . VAL   A 1 629 ? 1.507   -74.577  -29.299 1.00 28.97  ? 621 VAL   A CB    1 
ATOM   5020 C CG1   . VAL   A 1 629 ? 1.368   -73.603  -30.462 1.00 29.59  ? 621 VAL   A CG1   1 
ATOM   5021 C CG2   . VAL   A 1 629 ? 0.328   -74.434  -28.346 1.00 29.22  ? 621 VAL   A CG2   1 
ATOM   5022 N N     . CYS   A 1 630 ? 2.787   -76.882  -27.788 1.00 28.70  ? 622 CYS   A N     1 
ATOM   5023 C CA    . CYS   A 1 630 ? 2.937   -77.754  -26.637 1.00 28.65  ? 622 CYS   A CA    1 
ATOM   5024 C C     . CYS   A 1 630 ? 2.338   -77.088  -25.405 1.00 27.13  ? 622 CYS   A C     1 
ATOM   5025 O O     . CYS   A 1 630 ? 2.405   -75.869  -25.258 1.00 27.22  ? 622 CYS   A O     1 
ATOM   5026 C CB    . CYS   A 1 630 ? 4.389   -78.142  -26.392 1.00 30.02  ? 622 CYS   A CB    1 
ATOM   5027 S SG    . CYS   A 1 630 ? 4.957   -79.479  -27.474 1.00 34.27  ? 622 CYS   A SG    1 
ATOM   5028 N N     . SER   A 1 631 ? 1.721   -77.912  -24.553 1.00 25.37  ? 623 SER   A N     1 
ATOM   5029 C CA    . SER   A 1 631 ? 1.445   -77.546  -23.176 1.00 23.59  ? 623 SER   A CA    1 
ATOM   5030 C C     . SER   A 1 631 ? 2.549   -78.125  -22.303 1.00 22.73  ? 623 SER   A C     1 
ATOM   5031 O O     . SER   A 1 631 ? 3.403   -78.860  -22.792 1.00 22.39  ? 623 SER   A O     1 
ATOM   5032 C CB    . SER   A 1 631 ? 0.090   -78.039  -22.740 1.00 23.21  ? 623 SER   A CB    1 
ATOM   5033 O OG    . SER   A 1 631 ? 0.016   -79.459  -22.762 1.00 22.46  ? 623 SER   A OG    1 
ATOM   5034 N N     . ALA   A 1 632 ? 2.529   -77.773  -21.017 1.00 22.18  ? 624 ALA   A N     1 
ATOM   5035 C CA    . ALA   A 1 632 ? 3.226   -78.552  -20.010 1.00 21.93  ? 624 ALA   A CA    1 
ATOM   5036 C C     . ALA   A 1 632 ? 2.561   -79.922  -19.912 1.00 21.75  ? 624 ALA   A C     1 
ATOM   5037 O O     . ALA   A 1 632 ? 1.396   -80.077  -20.276 1.00 21.68  ? 624 ALA   A O     1 
ATOM   5038 C CB    . ALA   A 1 632 ? 3.195   -77.832  -18.680 1.00 21.80  ? 624 ALA   A CB    1 
ATOM   5039 N N     . ILE   A 1 633 ? 3.315   -80.918  -19.439 1.00 21.42  ? 625 ILE   A N     1 
ATOM   5040 C CA    . ILE   A 1 633 ? 2.708   -82.149  -18.972 1.00 21.61  ? 625 ILE   A CA    1 
ATOM   5041 C C     . ILE   A 1 633 ? 1.941   -81.820  -17.694 1.00 21.36  ? 625 ILE   A C     1 
ATOM   5042 O O     . ILE   A 1 633 ? 2.494   -81.230  -16.771 1.00 21.66  ? 625 ILE   A O     1 
ATOM   5043 C CB    . ILE   A 1 633 ? 3.762   -83.251  -18.763 1.00 22.03  ? 625 ILE   A CB    1 
ATOM   5044 C CG1   . ILE   A 1 633 ? 4.422   -83.634  -20.088 1.00 22.98  ? 625 ILE   A CG1   1 
ATOM   5045 C CG2   . ILE   A 1 633 ? 3.145   -84.463  -18.064 1.00 22.16  ? 625 ILE   A CG2   1 
ATOM   5046 C CD1   . ILE   A 1 633 ? 5.596   -84.586  -19.954 1.00 23.40  ? 625 ILE   A CD1   1 
ATOM   5047 N N     . HIS   A 1 634 ? 0.657   -82.184  -17.671 1.00 20.83  ? 626 HIS   A N     1 
ATOM   5048 C CA    . HIS   A 1 634 ? -0.223  -81.867  -16.561 1.00 20.51  ? 626 HIS   A CA    1 
ATOM   5049 C C     . HIS   A 1 634 ? -0.211  -83.029  -15.572 1.00 20.73  ? 626 HIS   A C     1 
ATOM   5050 O O     . HIS   A 1 634 ? -0.205  -84.187  -15.979 1.00 21.06  ? 626 HIS   A O     1 
ATOM   5051 C CB    . HIS   A 1 634 ? -1.623  -81.538  -17.089 1.00 20.33  ? 626 HIS   A CB    1 
ATOM   5052 C CG    . HIS   A 1 634 ? -1.723  -80.193  -17.729 1.00 20.09  ? 626 HIS   A CG    1 
ATOM   5053 N ND1   . HIS   A 1 634 ? -1.046  -79.853  -18.879 1.00 20.13  ? 626 HIS   A ND1   1 
ATOM   5054 C CD2   . HIS   A 1 634 ? -2.392  -79.095  -17.357 1.00 20.04  ? 626 HIS   A CD2   1 
ATOM   5055 C CE1   . HIS   A 1 634 ? -1.318  -78.593  -19.189 1.00 19.78  ? 626 HIS   A CE1   1 
ATOM   5056 N NE2   . HIS   A 1 634 ? -2.138  -78.120  -18.284 1.00 19.63  ? 626 HIS   A NE2   1 
ATOM   5057 N N     . ASN   A 1 635 ? -0.181  -82.689  -14.278 1.00 20.79  ? 627 ASN   A N     1 
ATOM   5058 C CA    . ASN   A 1 635 ? -0.260  -83.640  -13.179 1.00 20.83  ? 627 ASN   A CA    1 
ATOM   5059 C C     . ASN   A 1 635 ? 0.948   -84.577  -13.182 1.00 20.53  ? 627 ASN   A C     1 
ATOM   5060 O O     . ASN   A 1 635 ? 0.789   -85.784  -13.033 1.00 20.18  ? 627 ASN   A O     1 
ATOM   5061 C CB    . ASN   A 1 635 ? -1.590  -84.391  -13.189 1.00 21.06  ? 627 ASN   A CB    1 
ATOM   5062 C CG    . ASN   A 1 635 ? -1.842  -85.155  -11.907 1.00 21.57  ? 627 ASN   A CG    1 
ATOM   5063 O OD1   . ASN   A 1 635 ? -2.326  -86.294  -11.927 1.00 21.74  ? 627 ASN   A OD1   1 
ATOM   5064 N ND2   . ASN   A 1 635 ? -1.553  -84.538  -10.777 1.00 21.24  ? 627 ASN   A ND2   1 
ATOM   5065 N N     . PRO   A 1 636 ? 2.195   -84.066  -13.306 1.00 20.99  ? 628 PRO   A N     1 
ATOM   5066 C CA    . PRO   A 1 636 ? 3.379   -84.928  -13.252 1.00 21.44  ? 628 PRO   A CA    1 
ATOM   5067 C C     . PRO   A 1 636 ? 3.575   -85.560  -11.873 1.00 22.18  ? 628 PRO   A C     1 
ATOM   5068 O O     . PRO   A 1 636 ? 3.476   -84.869  -10.863 1.00 22.15  ? 628 PRO   A O     1 
ATOM   5069 C CB    . PRO   A 1 636 ? 4.520   -83.971  -13.631 1.00 21.19  ? 628 PRO   A CB    1 
ATOM   5070 C CG    . PRO   A 1 636 ? 4.024   -82.612  -13.198 1.00 21.13  ? 628 PRO   A CG    1 
ATOM   5071 C CD    . PRO   A 1 636 ? 2.534   -82.644  -13.483 1.00 21.02  ? 628 PRO   A CD    1 
ATOM   5072 N N     A THR   A 1 637 ? 3.885   -86.867  -11.846 0.50 22.60  ? 629 THR   A N     1 
ATOM   5073 N N     B THR   A 1 637 ? 3.808   -86.878  -11.874 0.50 22.49  ? 629 THR   A N     1 
ATOM   5074 C CA    A THR   A 1 637 ? 4.026   -87.678  -10.635 0.50 22.88  ? 629 THR   A CA    1 
ATOM   5075 C CA    B THR   A 1 637 ? 4.031   -87.650  -10.662 0.50 22.71  ? 629 THR   A CA    1 
ATOM   5076 C C     A THR   A 1 637 ? 2.764   -87.650  -9.779  0.50 22.89  ? 629 THR   A C     1 
ATOM   5077 C C     B THR   A 1 637 ? 2.782   -87.626  -9.782  0.50 22.80  ? 629 THR   A C     1 
ATOM   5078 O O     A THR   A 1 637 ? 2.835   -87.936  -8.586  0.50 23.21  ? 629 THR   A O     1 
ATOM   5079 O O     B THR   A 1 637 ? 2.875   -87.887  -8.585  0.50 23.13  ? 629 THR   A O     1 
ATOM   5080 C CB    A THR   A 1 637 ? 5.204   -87.263  -9.753  0.50 23.04  ? 629 THR   A CB    1 
ATOM   5081 C CB    B THR   A 1 637 ? 5.252   -87.092  -9.931  0.50 22.74  ? 629 THR   A CB    1 
ATOM   5082 O OG1   A THR   A 1 637 ? 4.880   -86.006  -9.167  0.50 23.31  ? 629 THR   A OG1   1 
ATOM   5083 O OG1   B THR   A 1 637 ? 6.182   -86.765  -10.958 0.50 23.16  ? 629 THR   A OG1   1 
ATOM   5084 C CG2   A THR   A 1 637 ? 6.514   -87.195  -10.508 0.50 23.18  ? 629 THR   A CG2   1 
ATOM   5085 C CG2   B THR   A 1 637 ? 5.862   -88.082  -8.956  0.50 22.55  ? 629 THR   A CG2   1 
ATOM   5086 N N     . GLY   A 1 638 ? 1.618   -87.325  -10.377 1.00 22.94  ? 630 GLY   A N     1 
ATOM   5087 C CA    . GLY   A 1 638 ? 0.384   -87.186  -9.621  1.00 23.32  ? 630 GLY   A CA    1 
ATOM   5088 C C     . GLY   A 1 638 ? 0.493   -86.123  -8.524  1.00 23.64  ? 630 GLY   A C     1 
ATOM   5089 O O     . GLY   A 1 638 ? -0.129  -86.249  -7.474  1.00 24.50  ? 630 GLY   A O     1 
ATOM   5090 N N     . ARG   A 1 639 ? 1.269   -85.065  -8.782  1.00 23.80  ? 631 ARG   A N     1 
ATOM   5091 C CA    . ARG   A 1 639 ? 1.572   -84.064  -7.772  1.00 24.33  ? 631 ARG   A CA    1 
ATOM   5092 C C     . ARG   A 1 639 ? 0.317   -83.299  -7.354  1.00 24.05  ? 631 ARG   A C     1 
ATOM   5093 O O     . ARG   A 1 639 ? 0.215   -82.881  -6.208  1.00 24.88  ? 631 ARG   A O     1 
ATOM   5094 C CB    . ARG   A 1 639 ? 2.614   -83.059  -8.274  1.00 25.01  ? 631 ARG   A CB    1 
ATOM   5095 C CG    . ARG   A 1 639 ? 2.114   -82.119  -9.361  1.00 25.29  ? 631 ARG   A CG    1 
ATOM   5096 C CD    . ARG   A 1 639 ? 3.164   -81.095  -9.719  1.00 25.72  ? 631 ARG   A CD    1 
ATOM   5097 N NE    . ARG   A 1 639 ? 2.779   -80.339  -10.915 1.00 26.50  ? 631 ARG   A NE    1 
ATOM   5098 C CZ    . ARG   A 1 639 ? 3.613   -79.590  -11.630 1.00 27.84  ? 631 ARG   A CZ    1 
ATOM   5099 N NH1   . ARG   A 1 639 ? 4.872   -79.450  -11.244 1.00 28.42  ? 631 ARG   A NH1   1 
ATOM   5100 N NH2   . ARG   A 1 639 ? 3.193   -78.983  -12.731 1.00 27.52  ? 631 ARG   A NH2   1 
ATOM   5101 N N     . SER   A 1 640 ? -0.602  -83.071  -8.298  1.00 24.43  ? 632 SER   A N     1 
ATOM   5102 C CA    . SER   A 1 640 ? -1.820  -82.317  -8.039  1.00 24.86  ? 632 SER   A CA    1 
ATOM   5103 C C     . SER   A 1 640 ? -2.997  -83.238  -7.736  1.00 25.60  ? 632 SER   A C     1 
ATOM   5104 O O     . SER   A 1 640 ? -4.024  -82.777  -7.246  1.00 25.76  ? 632 SER   A O     1 
ATOM   5105 C CB    . SER   A 1 640 ? -2.172  -81.418  -9.198  1.00 24.72  ? 632 SER   A CB    1 
ATOM   5106 O OG    . SER   A 1 640 ? -1.101  -80.552  -9.536  1.00 24.82  ? 632 SER   A OG    1 
ATOM   5107 N N     . TYR   A 1 641 ? -2.859  -84.533  -8.032  1.00 26.55  ? 633 TYR   A N     1 
ATOM   5108 C CA    . TYR   A 1 641 ? -4.021  -85.398  -8.117  1.00 27.96  ? 633 TYR   A CA    1 
ATOM   5109 C C     . TYR   A 1 641 ? -3.602  -86.855  -8.288  1.00 27.02  ? 633 TYR   A C     1 
ATOM   5110 O O     . TYR   A 1 641 ? -2.876  -87.183  -9.225  1.00 25.96  ? 633 TYR   A O     1 
ATOM   5111 C CB    . TYR   A 1 641 ? -4.872  -84.948  -9.305  1.00 30.83  ? 633 TYR   A CB    1 
ATOM   5112 C CG    . TYR   A 1 641 ? -6.024  -85.894  -9.594  1.00 34.02  ? 633 TYR   A CG    1 
ATOM   5113 C CD1   . TYR   A 1 641 ? -7.221  -85.789  -8.895  1.00 35.83  ? 633 TYR   A CD1   1 
ATOM   5114 C CD2   . TYR   A 1 641 ? -5.905  -86.904  -10.542 1.00 36.08  ? 633 TYR   A CD2   1 
ATOM   5115 C CE1   . TYR   A 1 641 ? -8.275  -86.653  -9.143  1.00 37.48  ? 633 TYR   A CE1   1 
ATOM   5116 C CE2   . TYR   A 1 641 ? -6.949  -87.777  -10.796 1.00 37.41  ? 633 TYR   A CE2   1 
ATOM   5117 C CZ    . TYR   A 1 641 ? -8.136  -87.650  -10.093 1.00 38.12  ? 633 TYR   A CZ    1 
ATOM   5118 O OH    . TYR   A 1 641 ? -9.174  -88.502  -10.336 1.00 41.20  ? 633 TYR   A OH    1 
ATOM   5119 N N     . THR   A 1 642 ? -4.079  -87.713  -7.374  1.00 26.31  ? 634 THR   A N     1 
ATOM   5120 C CA    . THR   A 1 642 ? -3.986  -89.155  -7.532  1.00 26.24  ? 634 THR   A CA    1 
ATOM   5121 C C     . THR   A 1 642 ? -5.258  -89.798  -6.996  1.00 26.11  ? 634 THR   A C     1 
ATOM   5122 O O     . THR   A 1 642 ? -6.075  -89.143  -6.355  1.00 25.73  ? 634 THR   A O     1 
ATOM   5123 C CB    . THR   A 1 642 ? -2.764  -89.723  -6.812  1.00 26.05  ? 634 THR   A CB    1 
ATOM   5124 O OG1   . THR   A 1 642 ? -3.071  -89.608  -5.428  1.00 26.06  ? 634 THR   A OG1   1 
ATOM   5125 C CG2   . THR   A 1 642 ? -1.478  -88.995  -7.153  1.00 26.37  ? 634 THR   A CG2   1 
ATOM   5126 N N     . ILE   A 1 643 ? -5.390  -91.096  -7.277  1.00 26.62  ? 635 ILE   A N     1 
ATOM   5127 C CA    . ILE   A 1 643 ? -6.498  -91.913  -6.816  1.00 27.32  ? 635 ILE   A CA    1 
ATOM   5128 C C     . ILE   A 1 643 ? -5.901  -93.022  -5.952  1.00 27.78  ? 635 ILE   A C     1 
ATOM   5129 O O     . ILE   A 1 643 ? -5.025  -93.755  -6.403  1.00 28.40  ? 635 ILE   A O     1 
ATOM   5130 C CB    . ILE   A 1 643 ? -7.288  -92.474  -8.015  1.00 28.16  ? 635 ILE   A CB    1 
ATOM   5131 C CG1   . ILE   A 1 643 ? -7.526  -91.411  -9.100  1.00 28.31  ? 635 ILE   A CG1   1 
ATOM   5132 C CG2   . ILE   A 1 643 ? -8.599  -93.114  -7.553  1.00 28.22  ? 635 ILE   A CG2   1 
ATOM   5133 C CD1   . ILE   A 1 643 ? -7.517  -91.952  -10.522 1.00 28.43  ? 635 ILE   A CD1   1 
ATOM   5134 N N     . GLY   A 1 644 ? -6.369  -93.132  -4.706  1.00 28.21  ? 636 GLY   A N     1 
ATOM   5135 C CA    . GLY   A 1 644 ? -5.760  -94.021  -3.734  1.00 28.04  ? 636 GLY   A CA    1 
ATOM   5136 C C     . GLY   A 1 644 ? -6.162  -95.473  -3.978  1.00 28.34  ? 636 GLY   A C     1 
ATOM   5137 O O     . GLY   A 1 644 ? -7.342  -95.773  -4.151  1.00 28.74  ? 636 GLY   A O     1 
ATOM   5138 N N     . LEU   A 1 645 ? -5.164  -96.364  -3.998  1.00 28.03  ? 637 LEU   A N     1 
ATOM   5139 C CA    . LEU   A 1 645 ? -5.409  -97.796  -4.067  1.00 28.00  ? 637 LEU   A CA    1 
ATOM   5140 C C     . LEU   A 1 645 ? -5.737  -98.342  -2.665  1.00 27.78  ? 637 LEU   A C     1 
ATOM   5141 O O     . LEU   A 1 645 ? -5.413  -97.645  -1.685  1.00 26.67  ? 637 LEU   A O     1 
ATOM   5142 C CB    . LEU   A 1 645 ? -4.202  -98.511  -4.675  1.00 28.36  ? 637 LEU   A CB    1 
ATOM   5143 C CG    . LEU   A 1 645 ? -4.112  -98.471  -6.203  1.00 27.93  ? 637 LEU   A CG    1 
ATOM   5144 C CD1   . LEU   A 1 645 ? -2.745  -98.902  -6.695  1.00 28.07  ? 637 LEU   A CD1   1 
ATOM   5145 C CD2   . LEU   A 1 645 ? -5.196  -99.348  -6.800  1.00 27.76  ? 637 LEU   A CD2   1 
ATOM   5146 O OXT   . LEU   A 1 645 ? -6.303  -99.453  -2.608  1.00 28.27  ? 637 LEU   A OXT   1 
ATOM   5147 N N     . MET   B 2 35  ? -38.965 -23.773  -20.302 1.00 73.17  ? 27  MET   B N     1 
ATOM   5148 C CA    . MET   B 2 35  ? -37.615 -23.352  -20.769 1.00 74.50  ? 27  MET   B CA    1 
ATOM   5149 C C     . MET   B 2 35  ? -36.554 -24.051  -19.924 1.00 72.98  ? 27  MET   B C     1 
ATOM   5150 O O     . MET   B 2 35  ? -36.515 -23.871  -18.707 1.00 75.52  ? 27  MET   B O     1 
ATOM   5151 C CB    . MET   B 2 35  ? -37.439 -21.832  -20.662 1.00 76.18  ? 27  MET   B CB    1 
ATOM   5152 C CG    . MET   B 2 35  ? -36.031 -21.324  -20.957 1.00 77.83  ? 27  MET   B CG    1 
ATOM   5153 S SD    . MET   B 2 35  ? -35.535 -21.435  -22.689 1.00 80.85  ? 27  MET   B SD    1 
ATOM   5154 C CE    . MET   B 2 35  ? -36.381 -20.018  -23.403 1.00 81.04  ? 27  MET   B CE    1 
ATOM   5155 N N     . GLU   B 2 36  ? -35.697 -24.836  -20.591 1.00 67.09  ? 28  GLU   B N     1 
ATOM   5156 C CA    . GLU   B 2 36  ? -34.613 -25.547  -19.933 1.00 60.85  ? 28  GLU   B CA    1 
ATOM   5157 C C     . GLU   B 2 36  ? -33.288 -24.890  -20.310 1.00 58.30  ? 28  GLU   B C     1 
ATOM   5158 O O     . GLU   B 2 36  ? -33.251 -23.986  -21.142 1.00 60.63  ? 28  GLU   B O     1 
ATOM   5159 C CB    . GLU   B 2 36  ? -34.647 -27.034  -20.286 1.00 58.31  ? 28  GLU   B CB    1 
ATOM   5160 C CG    . GLU   B 2 36  ? -36.041 -27.650  -20.195 1.00 56.97  ? 28  GLU   B CG    1 
ATOM   5161 C CD    . GLU   B 2 36  ? -36.879 -27.539  -21.455 1.00 55.33  ? 28  GLU   B CD    1 
ATOM   5162 O OE1   . GLU   B 2 36  ? -36.441 -26.858  -22.405 1.00 55.70  ? 28  GLU   B OE1   1 
ATOM   5163 O OE2   . GLU   B 2 36  ? -37.968 -28.150  -21.485 1.00 53.30  ? 28  GLU   B OE2   1 
ATOM   5164 N N     . ARG   B 2 37  ? -32.201 -25.374  -19.701 1.00 55.00  ? 29  ARG   B N     1 
ATOM   5165 C CA    . ARG   B 2 37  ? -30.953 -24.631  -19.630 1.00 53.37  ? 29  ARG   B CA    1 
ATOM   5166 C C     . ARG   B 2 37  ? -30.109 -24.811  -20.891 1.00 50.27  ? 29  ARG   B C     1 
ATOM   5167 O O     . ARG   B 2 37  ? -29.441 -23.869  -21.317 1.00 47.61  ? 29  ARG   B O     1 
ATOM   5168 C CB    . ARG   B 2 37  ? -30.181 -25.069  -18.381 1.00 55.22  ? 29  ARG   B CB    1 
ATOM   5169 C CG    . ARG   B 2 37  ? -28.802 -24.438  -18.269 1.00 57.40  ? 29  ARG   B CG    1 
ATOM   5170 C CD    . ARG   B 2 37  ? -28.159 -24.679  -16.916 1.00 59.64  ? 29  ARG   B CD    1 
ATOM   5171 N NE    . ARG   B 2 37  ? -26.789 -24.153  -16.888 1.00 62.10  ? 29  ARG   B NE    1 
ATOM   5172 C CZ    . ARG   B 2 37  ? -26.440 -22.869  -16.962 1.00 62.38  ? 29  ARG   B CZ    1 
ATOM   5173 N NH1   . ARG   B 2 37  ? -27.359 -21.917  -16.968 1.00 61.81  ? 29  ARG   B NH1   1 
ATOM   5174 N NH2   . ARG   B 2 37  ? -25.160 -22.539  -17.008 1.00 62.89  ? 29  ARG   B NH2   1 
ATOM   5175 N N     . GLN   B 2 38  ? -30.125 -26.019  -21.470 1.00 47.69  ? 30  GLN   B N     1 
ATOM   5176 C CA    . GLN   B 2 38  ? -29.222 -26.351  -22.561 1.00 46.53  ? 30  GLN   B CA    1 
ATOM   5177 C C     . GLN   B 2 38  ? -29.824 -25.880  -23.885 1.00 47.40  ? 30  GLN   B C     1 
ATOM   5178 O O     . GLN   B 2 38  ? -30.624 -26.586  -24.497 1.00 46.97  ? 30  GLN   B O     1 
ATOM   5179 C CB    . GLN   B 2 38  ? -28.886 -27.844  -22.572 1.00 44.72  ? 30  GLN   B CB    1 
ATOM   5180 C CG    . GLN   B 2 38  ? -28.042 -28.309  -21.388 1.00 43.43  ? 30  GLN   B CG    1 
ATOM   5181 C CD    . GLN   B 2 38  ? -28.787 -28.347  -20.070 1.00 40.91  ? 30  GLN   B CD    1 
ATOM   5182 O OE1   . GLN   B 2 38  ? -29.852 -28.962  -19.942 1.00 38.19  ? 30  GLN   B OE1   1 
ATOM   5183 N NE2   . GLN   B 2 38  ? -28.218 -27.697  -19.066 1.00 39.91  ? 30  GLN   B NE2   1 
ATOM   5184 N N     . LEU   B 2 39  ? -29.419 -24.676  -24.314 1.00 49.10  ? 31  LEU   B N     1 
ATOM   5185 C CA    . LEU   B 2 39  ? -29.866 -24.098  -25.573 1.00 51.17  ? 31  LEU   B CA    1 
ATOM   5186 C C     . LEU   B 2 39  ? -29.159 -24.803  -26.726 1.00 52.19  ? 31  LEU   B C     1 
ATOM   5187 O O     . LEU   B 2 39  ? -27.940 -24.704  -26.852 1.00 51.31  ? 31  LEU   B O     1 
ATOM   5188 C CB    . LEU   B 2 39  ? -29.569 -22.600  -25.607 1.00 51.82  ? 31  LEU   B CB    1 
ATOM   5189 C CG    . LEU   B 2 39  ? -30.208 -21.742  -24.511 1.00 51.60  ? 31  LEU   B CG    1 
ATOM   5190 C CD1   . LEU   B 2 39  ? -29.660 -20.324  -24.581 1.00 51.26  ? 31  LEU   B CD1   1 
ATOM   5191 C CD2   . LEU   B 2 39  ? -31.723 -21.743  -24.624 1.00 51.45  ? 31  LEU   B CD2   1 
ATOM   5192 N N     . GLU   B 2 40  ? -29.938 -25.481  -27.579 1.00 53.69  ? 32  GLU   B N     1 
ATOM   5193 C CA    . GLU   B 2 40  ? -29.379 -26.320  -28.626 1.00 54.67  ? 32  GLU   B CA    1 
ATOM   5194 C C     . GLU   B 2 40  ? -29.352 -25.574  -29.961 1.00 55.11  ? 32  GLU   B C     1 
ATOM   5195 O O     . GLU   B 2 40  ? -28.312 -25.529  -30.612 1.00 55.94  ? 32  GLU   B O     1 
ATOM   5196 C CB    . GLU   B 2 40  ? -30.158 -27.633  -28.723 1.00 55.59  ? 32  GLU   B CB    1 
ATOM   5197 C CG    . GLU   B 2 40  ? -29.360 -28.760  -29.373 1.00 56.16  ? 32  GLU   B CG    1 
ATOM   5198 C CD    . GLU   B 2 40  ? -28.092 -29.140  -28.626 1.00 56.40  ? 32  GLU   B CD    1 
ATOM   5199 O OE1   . GLU   B 2 40  ? -27.022 -29.168  -29.270 1.00 55.07  ? 32  GLU   B OE1   1 
ATOM   5200 O OE2   . GLU   B 2 40  ? -28.171 -29.393  -27.402 1.00 56.29  ? 32  GLU   B OE2   1 
ATOM   5201 N N     . ALA   B 2 41  ? -30.491 -24.992  -30.364 1.00 54.85  ? 33  ALA   B N     1 
ATOM   5202 C CA    . ALA   B 2 41  ? -30.634 -24.433  -31.702 1.00 54.10  ? 33  ALA   B CA    1 
ATOM   5203 C C     . ALA   B 2 41  ? -31.051 -22.962  -31.655 1.00 52.98  ? 33  ALA   B C     1 
ATOM   5204 O O     . ALA   B 2 41  ? -31.663 -22.513  -30.689 1.00 51.30  ? 33  ALA   B O     1 
ATOM   5205 C CB    . ALA   B 2 41  ? -31.628 -25.256  -32.489 1.00 53.61  ? 33  ALA   B CB    1 
ATOM   5206 N N     . ALA   B 2 42  ? -30.716 -22.232  -32.729 1.00 54.30  ? 34  ALA   B N     1 
ATOM   5207 C CA    . ALA   B 2 42  ? -31.125 -20.847  -32.921 1.00 55.39  ? 34  ALA   B CA    1 
ATOM   5208 C C     . ALA   B 2 42  ? -31.172 -20.528  -34.416 1.00 56.24  ? 34  ALA   B C     1 
ATOM   5209 O O     . ALA   B 2 42  ? -30.142 -20.571  -35.083 1.00 55.55  ? 34  ALA   B O     1 
ATOM   5210 C CB    . ALA   B 2 42  ? -30.177 -19.918  -32.197 1.00 54.78  ? 34  ALA   B CB    1 
ATOM   5211 N N     . ARG   B 2 43  ? -32.371 -20.204  -34.924 1.00 57.88  ? 35  ARG   B N     1 
ATOM   5212 C CA    . ARG   B 2 43  ? -32.593 -20.006  -36.350 1.00 58.12  ? 35  ARG   B CA    1 
ATOM   5213 C C     . ARG   B 2 43  ? -33.566 -18.849  -36.585 1.00 58.45  ? 35  ARG   B C     1 
ATOM   5214 O O     . ARG   B 2 43  ? -34.761 -18.977  -36.323 1.00 57.99  ? 35  ARG   B O     1 
ATOM   5215 C CB    . ARG   B 2 43  ? -33.187 -21.271  -36.984 1.00 57.79  ? 35  ARG   B CB    1 
ATOM   5216 C CG    . ARG   B 2 43  ? -32.431 -22.571  -36.750 1.00 57.75  ? 35  ARG   B CG    1 
ATOM   5217 C CD    . ARG   B 2 43  ? -31.093 -22.659  -37.473 1.00 57.28  ? 35  ARG   B CD    1 
ATOM   5218 N NE    . ARG   B 2 43  ? -30.394 -23.884  -37.068 1.00 57.47  ? 35  ARG   B NE    1 
ATOM   5219 C CZ    . ARG   B 2 43  ? -30.810 -25.126  -37.304 1.00 57.28  ? 35  ARG   B CZ    1 
ATOM   5220 N NH1   . ARG   B 2 43  ? -31.802 -25.360  -38.147 1.00 56.46  ? 35  ARG   B NH1   1 
ATOM   5221 N NH2   . ARG   B 2 43  ? -30.208 -26.146  -36.718 1.00 58.52  ? 35  ARG   B NH2   1 
ATOM   5222 N N     . TYR   B 2 44  ? -33.047 -17.725  -37.100 1.00 58.30  ? 36  TYR   B N     1 
ATOM   5223 C CA    . TYR   B 2 44  ? -33.883 -16.648  -37.611 1.00 57.50  ? 36  TYR   B CA    1 
ATOM   5224 C C     . TYR   B 2 44  ? -34.643 -17.135  -38.843 1.00 58.28  ? 36  TYR   B C     1 
ATOM   5225 O O     . TYR   B 2 44  ? -34.209 -18.070  -39.511 1.00 59.43  ? 36  TYR   B O     1 
ATOM   5226 C CB    . TYR   B 2 44  ? -33.069 -15.422  -38.038 1.00 55.60  ? 36  TYR   B CB    1 
ATOM   5227 C CG    . TYR   B 2 44  ? -32.507 -14.539  -36.931 1.00 54.74  ? 36  TYR   B CG    1 
ATOM   5228 C CD1   . TYR   B 2 44  ? -33.313 -14.028  -35.919 1.00 54.21  ? 36  TYR   B CD1   1 
ATOM   5229 C CD2   . TYR   B 2 44  ? -31.159 -14.201  -36.913 1.00 54.72  ? 36  TYR   B CD2   1 
ATOM   5230 C CE1   . TYR   B 2 44  ? -32.792 -13.210  -34.927 1.00 55.30  ? 36  TYR   B CE1   1 
ATOM   5231 C CE2   . TYR   B 2 44  ? -30.625 -13.388  -35.927 1.00 54.34  ? 36  TYR   B CE2   1 
ATOM   5232 C CZ    . TYR   B 2 44  ? -31.443 -12.891  -34.928 1.00 54.64  ? 36  TYR   B CZ    1 
ATOM   5233 O OH    . TYR   B 2 44  ? -30.910 -12.092  -33.957 1.00 53.03  ? 36  TYR   B OH    1 
ATOM   5234 N N     . ARG   B 2 45  ? -35.773 -16.482  -39.141 1.00 58.80  ? 37  ARG   B N     1 
ATOM   5235 C CA    . ARG   B 2 45  ? -36.463 -16.659  -40.410 1.00 59.31  ? 37  ARG   B CA    1 
ATOM   5236 C C     . ARG   B 2 45  ? -36.469 -15.320  -41.145 1.00 59.81  ? 37  ARG   B C     1 
ATOM   5237 O O     . ARG   B 2 45  ? -35.867 -14.357  -40.675 1.00 57.30  ? 37  ARG   B O     1 
ATOM   5238 C CB    . ARG   B 2 45  ? -37.878 -17.211  -40.198 1.00 59.73  ? 37  ARG   B CB    1 
ATOM   5239 C CG    . ARG   B 2 45  ? -38.860 -16.220  -39.592 1.00 59.75  ? 37  ARG   B CG    1 
ATOM   5240 C CD    . ARG   B 2 45  ? -40.277 -16.760  -39.515 1.00 59.58  ? 37  ARG   B CD    1 
ATOM   5241 N NE    . ARG   B 2 45  ? -41.132 -15.851  -38.745 1.00 59.70  ? 37  ARG   B NE    1 
ATOM   5242 C CZ    . ARG   B 2 45  ? -42.446 -15.958  -38.579 1.00 60.50  ? 37  ARG   B CZ    1 
ATOM   5243 N NH1   . ARG   B 2 45  ? -43.117 -16.962  -39.120 1.00 60.38  ? 37  ARG   B NH1   1 
ATOM   5244 N NH2   . ARG   B 2 45  ? -43.087 -15.049  -37.865 1.00 60.90  ? 37  ARG   B NH2   1 
ATOM   5245 N N     . SER   B 2 46  ? -37.168 -15.275  -42.288 1.00 61.83  ? 38  SER   B N     1 
ATOM   5246 C CA    . SER   B 2 46  ? -37.189 -14.117  -43.170 1.00 61.76  ? 38  SER   B CA    1 
ATOM   5247 C C     . SER   B 2 46  ? -37.426 -12.828  -42.386 1.00 63.07  ? 38  SER   B C     1 
ATOM   5248 O O     . SER   B 2 46  ? -36.606 -11.913  -42.431 1.00 63.61  ? 38  SER   B O     1 
ATOM   5249 C CB    . SER   B 2 46  ? -38.232 -14.284  -44.247 1.00 60.57  ? 38  SER   B CB    1 
ATOM   5250 O OG    . SER   B 2 46  ? -38.076 -15.526  -44.919 1.00 60.58  ? 38  SER   B OG    1 
ATOM   5251 N N     . ASP   B 2 47  ? -38.549 -12.778  -41.658 1.00 63.88  ? 39  ASP   B N     1 
ATOM   5252 C CA    . ASP   B 2 47  ? -39.009 -11.557  -41.015 1.00 63.93  ? 39  ASP   B CA    1 
ATOM   5253 C C     . ASP   B 2 47  ? -38.039 -11.112  -39.920 1.00 62.79  ? 39  ASP   B C     1 
ATOM   5254 O O     . ASP   B 2 47  ? -37.987 -9.928   -39.599 1.00 61.24  ? 39  ASP   B O     1 
ATOM   5255 C CB    . ASP   B 2 47  ? -40.431 -11.702  -40.494 1.00 65.09  ? 39  ASP   B CB    1 
ATOM   5256 C CG    . ASP   B 2 47  ? -40.634 -12.706  -39.368 1.00 67.10  ? 39  ASP   B CG    1 
ATOM   5257 O OD1   . ASP   B 2 47  ? -39.648 -13.365  -38.979 1.00 68.33  ? 39  ASP   B OD1   1 
ATOM   5258 O OD2   . ASP   B 2 47  ? -41.780 -12.820  -38.886 1.00 68.35  ? 39  ASP   B OD2   1 
ATOM   5259 N N     . GLY   B 2 48  ? -37.298 -12.065  -39.335 1.00 64.14  ? 40  GLY   B N     1 
ATOM   5260 C CA    . GLY   B 2 48  ? -36.284 -11.760  -38.335 1.00 64.07  ? 40  GLY   B CA    1 
ATOM   5261 C C     . GLY   B 2 48  ? -36.623 -12.317  -36.951 1.00 61.95  ? 40  GLY   B C     1 
ATOM   5262 O O     . GLY   B 2 48  ? -35.897 -12.063  -35.991 1.00 59.36  ? 40  GLY   B O     1 
ATOM   5263 N N     . ALA   B 2 49  ? -37.727 -13.070  -36.855 1.00 61.97  ? 41  ALA   B N     1 
ATOM   5264 C CA    . ALA   B 2 49  ? -38.108 -13.738  -35.620 1.00 63.57  ? 41  ALA   B CA    1 
ATOM   5265 C C     . ALA   B 2 49  ? -37.143 -14.888  -35.335 1.00 64.60  ? 41  ALA   B C     1 
ATOM   5266 O O     . ALA   B 2 49  ? -36.797 -15.645  -36.239 1.00 66.42  ? 41  ALA   B O     1 
ATOM   5267 C CB    . ALA   B 2 49  ? -39.536 -14.229  -35.722 1.00 63.37  ? 41  ALA   B CB    1 
ATOM   5268 N N     . LEU   B 2 50  ? -36.739 -15.019  -34.065 1.00 64.76  ? 42  LEU   B N     1 
ATOM   5269 C CA    . LEU   B 2 50  ? -35.712 -15.965  -33.658 1.00 63.75  ? 42  LEU   B CA    1 
ATOM   5270 C C     . LEU   B 2 50  ? -36.357 -17.237  -33.113 1.00 62.07  ? 42  LEU   B C     1 
ATOM   5271 O O     . LEU   B 2 50  ? -37.183 -17.174  -32.203 1.00 60.67  ? 42  LEU   B O     1 
ATOM   5272 C CB    . LEU   B 2 50  ? -34.829 -15.292  -32.606 1.00 63.35  ? 42  LEU   B CB    1 
ATOM   5273 C CG    . LEU   B 2 50  ? -33.651 -16.116  -32.075 1.00 63.67  ? 42  LEU   B CG    1 
ATOM   5274 C CD1   . LEU   B 2 50  ? -32.675 -16.501  -33.176 1.00 63.28  ? 42  LEU   B CD1   1 
ATOM   5275 C CD2   . LEU   B 2 50  ? -32.938 -15.348  -30.976 1.00 64.22  ? 42  LEU   B CD2   1 
ATOM   5276 N N     . LEU   B 2 51  ? -35.959 -18.389  -33.671 1.00 61.31  ? 43  LEU   B N     1 
ATOM   5277 C CA    . LEU   B 2 51  ? -36.394 -19.684  -33.172 1.00 60.15  ? 43  LEU   B CA    1 
ATOM   5278 C C     . LEU   B 2 51  ? -35.401 -20.157  -32.113 1.00 58.87  ? 43  LEU   B C     1 
ATOM   5279 O O     . LEU   B 2 51  ? -34.204 -19.901  -32.223 1.00 58.51  ? 43  LEU   B O     1 
ATOM   5280 C CB    . LEU   B 2 51  ? -36.514 -20.692  -34.317 1.00 59.63  ? 43  LEU   B CB    1 
ATOM   5281 C CG    . LEU   B 2 51  ? -37.098 -22.066  -33.965 1.00 59.65  ? 43  LEU   B CG    1 
ATOM   5282 C CD1   . LEU   B 2 51  ? -38.439 -21.970  -33.260 1.00 59.59  ? 43  LEU   B CD1   1 
ATOM   5283 C CD2   . LEU   B 2 51  ? -37.240 -22.920  -35.214 1.00 59.05  ? 43  LEU   B CD2   1 
ATOM   5284 N N     . LEU   B 2 52  ? -35.922 -20.820  -31.074 1.00 57.46  ? 44  LEU   B N     1 
ATOM   5285 C CA    . LEU   B 2 52  ? -35.095 -21.461  -30.066 1.00 55.32  ? 44  LEU   B CA    1 
ATOM   5286 C C     . LEU   B 2 52  ? -35.617 -22.872  -29.814 1.00 51.82  ? 44  LEU   B C     1 
ATOM   5287 O O     . LEU   B 2 52  ? -36.797 -23.059  -29.522 1.00 49.12  ? 44  LEU   B O     1 
ATOM   5288 C CB    . LEU   B 2 52  ? -35.072 -20.650  -28.771 1.00 57.17  ? 44  LEU   B CB    1 
ATOM   5289 C CG    . LEU   B 2 52  ? -34.211 -19.383  -28.765 1.00 59.18  ? 44  LEU   B CG    1 
ATOM   5290 C CD1   . LEU   B 2 52  ? -34.337 -18.688  -27.419 1.00 59.27  ? 44  LEU   B CD1   1 
ATOM   5291 C CD2   . LEU   B 2 52  ? -32.751 -19.674  -29.072 1.00 59.62  ? 44  LEU   B CD2   1 
ATOM   5292 N N     . GLY   B 2 53  ? -34.718 -23.850  -29.970 1.00 50.07  ? 45  GLY   B N     1 
ATOM   5293 C CA    . GLY   B 2 53  ? -34.878 -25.170  -29.387 1.00 48.05  ? 45  GLY   B CA    1 
ATOM   5294 C C     . GLY   B 2 53  ? -34.021 -25.286  -28.129 1.00 45.91  ? 45  GLY   B C     1 
ATOM   5295 O O     . GLY   B 2 53  ? -32.975 -24.647  -28.028 1.00 44.29  ? 45  GLY   B O     1 
ATOM   5296 N N     . ALA   B 2 54  ? -34.482 -26.096  -27.172 1.00 45.06  ? 46  ALA   B N     1 
ATOM   5297 C CA    . ALA   B 2 54  ? -33.781 -26.258  -25.910 1.00 43.22  ? 46  ALA   B CA    1 
ATOM   5298 C C     . ALA   B 2 54  ? -34.113 -27.616  -25.302 1.00 41.39  ? 46  ALA   B C     1 
ATOM   5299 O O     . ALA   B 2 54  ? -35.151 -28.201  -25.609 1.00 41.04  ? 46  ALA   B O     1 
ATOM   5300 C CB    . ALA   B 2 54  ? -34.140 -25.127  -24.972 1.00 43.81  ? 46  ALA   B CB    1 
ATOM   5301 N N     A SER   B 2 55  ? -33.221 -28.105  -24.431 0.50 39.95  ? 47  SER   B N     1 
ATOM   5302 N N     B SER   B 2 55  ? -33.203 -28.095  -24.449 0.50 40.51  ? 47  SER   B N     1 
ATOM   5303 C CA    A SER   B 2 55  ? -33.414 -29.377  -23.754 0.50 39.46  ? 47  SER   B CA    1 
ATOM   5304 C CA    B SER   B 2 55  ? -33.290 -29.416  -23.856 0.50 40.39  ? 47  SER   B CA    1 
ATOM   5305 C C     A SER   B 2 55  ? -32.921 -29.282  -22.314 0.50 39.34  ? 47  SER   B C     1 
ATOM   5306 C C     B SER   B 2 55  ? -32.811 -29.353  -22.411 0.50 40.17  ? 47  SER   B C     1 
ATOM   5307 O O     A SER   B 2 55  ? -32.028 -28.497  -22.006 0.50 38.47  ? 47  SER   B O     1 
ATOM   5308 O O     B SER   B 2 55  ? -31.885 -28.613  -22.093 0.50 39.27  ? 47  SER   B O     1 
ATOM   5309 C CB    A SER   B 2 55  ? -32.715 -30.503  -24.478 0.50 39.24  ? 47  SER   B CB    1 
ATOM   5310 C CB    B SER   B 2 55  ? -32.493 -30.420  -24.659 0.50 40.57  ? 47  SER   B CB    1 
ATOM   5311 O OG    A SER   B 2 55  ? -33.159 -30.618  -25.822 0.50 38.53  ? 47  SER   B OG    1 
ATOM   5312 O OG    B SER   B 2 55  ? -31.324 -29.829  -25.213 0.50 40.39  ? 47  SER   B OG    1 
ATOM   5313 N N     A SER   B 2 56  ? -33.538 -30.083  -21.441 0.50 39.73  ? 48  SER   B N     1 
ATOM   5314 N N     B SER   B 2 56  ? -33.480 -30.109  -21.536 0.50 40.45  ? 48  SER   B N     1 
ATOM   5315 C CA    A SER   B 2 56  ? -32.984 -30.377  -20.130 0.50 39.89  ? 48  SER   B CA    1 
ATOM   5316 C CA    B SER   B 2 56  ? -32.967 -30.360  -20.201 0.50 40.63  ? 48  SER   B CA    1 
ATOM   5317 C C     A SER   B 2 56  ? -32.115 -31.628  -20.238 0.50 39.75  ? 48  SER   B C     1 
ATOM   5318 C C     B SER   B 2 56  ? -32.114 -31.624  -20.241 0.50 40.16  ? 48  SER   B C     1 
ATOM   5319 O O     A SER   B 2 56  ? -32.635 -32.727  -20.421 0.50 39.14  ? 48  SER   B O     1 
ATOM   5320 O O     B SER   B 2 56  ? -32.644 -32.726  -20.374 0.50 39.57  ? 48  SER   B O     1 
ATOM   5321 C CB    A SER   B 2 56  ? -34.075 -30.549  -19.098 0.50 39.87  ? 48  SER   B CB    1 
ATOM   5322 C CB    B SER   B 2 56  ? -34.074 -30.469  -19.179 0.50 40.79  ? 48  SER   B CB    1 
ATOM   5323 O OG    A SER   B 2 56  ? -33.622 -31.317  -17.991 0.50 39.81  ? 48  SER   B OG    1 
ATOM   5324 O OG    B SER   B 2 56  ? -35.164 -31.235  -19.675 0.50 41.18  ? 48  SER   B OG    1 
ATOM   5325 N N     . LEU   B 2 57  ? -30.792 -31.443  -20.140 1.00 39.81  ? 49  LEU   B N     1 
ATOM   5326 C CA    . LEU   B 2 57  ? -29.839 -32.536  -20.264 1.00 40.73  ? 49  LEU   B CA    1 
ATOM   5327 C C     . LEU   B 2 57  ? -29.397 -33.032  -18.885 1.00 41.16  ? 49  LEU   B C     1 
ATOM   5328 O O     . LEU   B 2 57  ? -28.484 -33.850  -18.787 1.00 40.77  ? 49  LEU   B O     1 
ATOM   5329 C CB    . LEU   B 2 57  ? -28.656 -32.051  -21.105 1.00 40.22  ? 49  LEU   B CB    1 
ATOM   5330 C CG    . LEU   B 2 57  ? -28.964 -31.645  -22.553 1.00 39.89  ? 49  LEU   B CG    1 
ATOM   5331 C CD1   . LEU   B 2 57  ? -27.694 -31.288  -23.307 1.00 39.83  ? 49  LEU   B CD1   1 
ATOM   5332 C CD2   . LEU   B 2 57  ? -29.703 -32.733  -23.309 1.00 39.48  ? 49  LEU   B CD2   1 
ATOM   5333 N N     . SER   B 2 58  ? -30.060 -32.548  -17.827 1.00 41.97  ? 50  SER   B N     1 
ATOM   5334 C CA    . SER   B 2 58  ? -29.733 -32.914  -16.458 1.00 42.57  ? 50  SER   B CA    1 
ATOM   5335 C C     . SER   B 2 58  ? -30.915 -32.576  -15.551 1.00 43.74  ? 50  SER   B C     1 
ATOM   5336 O O     . SER   B 2 58  ? -31.728 -31.717  -15.889 1.00 44.61  ? 50  SER   B O     1 
ATOM   5337 C CB    . SER   B 2 58  ? -28.469 -32.221  -16.007 1.00 42.53  ? 50  SER   B CB    1 
ATOM   5338 O OG    . SER   B 2 58  ? -28.169 -32.523  -14.651 1.00 42.34  ? 50  SER   B OG    1 
ATOM   5339 N N     . GLY   B 2 59  ? -31.002 -33.255  -14.400 1.00 43.97  ? 51  GLY   B N     1 
ATOM   5340 C CA    . GLY   B 2 59  ? -32.093 -33.049  -13.459 1.00 44.39  ? 51  GLY   B CA    1 
ATOM   5341 C C     . GLY   B 2 59  ? -33.220 -34.053  -13.692 1.00 45.85  ? 51  GLY   B C     1 
ATOM   5342 O O     . GLY   B 2 59  ? -33.132 -34.881  -14.595 1.00 46.20  ? 51  GLY   B O     1 
ATOM   5343 N N     . ARG   B 2 60  ? -34.287 -33.947  -12.887 1.00 47.78  ? 52  ARG   B N     1 
ATOM   5344 C CA    . ARG   B 2 60  ? -35.314 -34.978  -12.817 1.00 49.37  ? 52  ARG   B CA    1 
ATOM   5345 C C     . ARG   B 2 60  ? -35.848 -35.308  -14.210 1.00 48.00  ? 52  ARG   B C     1 
ATOM   5346 O O     . ARG   B 2 60  ? -35.885 -36.476  -14.591 1.00 47.18  ? 52  ARG   B O     1 
ATOM   5347 C CB    . ARG   B 2 60  ? -36.507 -34.618  -11.920 1.00 51.44  ? 52  ARG   B CB    1 
ATOM   5348 C CG    . ARG   B 2 60  ? -37.557 -35.724  -11.892 1.00 54.12  ? 52  ARG   B CG    1 
ATOM   5349 C CD    . ARG   B 2 60  ? -38.855 -35.364  -11.183 1.00 56.15  ? 52  ARG   B CD    1 
ATOM   5350 N NE    . ARG   B 2 60  ? -38.794 -35.603  -9.736  1.00 58.36  ? 52  ARG   B NE    1 
ATOM   5351 C CZ    . ARG   B 2 60  ? -38.689 -34.670  -8.793  1.00 60.78  ? 52  ARG   B CZ    1 
ATOM   5352 N NH1   . ARG   B 2 60  ? -38.576 -33.393  -9.119  1.00 61.44  ? 52  ARG   B NH1   1 
ATOM   5353 N NH2   . ARG   B 2 60  ? -38.680 -35.019  -7.517  1.00 60.07  ? 52  ARG   B NH2   1 
ATOM   5354 N N     A CYS   B 2 61  ? -36.292 -34.282  -14.946 0.50 48.37  ? 53  CYS   B N     1 
ATOM   5355 N N     B CYS   B 2 61  ? -36.240 -34.267  -14.955 0.50 48.29  ? 53  CYS   B N     1 
ATOM   5356 C CA    A CYS   B 2 61  ? -36.952 -34.495  -16.225 0.50 48.40  ? 53  CYS   B CA    1 
ATOM   5357 C CA    B CYS   B 2 61  ? -36.935 -34.429  -16.221 0.50 48.31  ? 53  CYS   B CA    1 
ATOM   5358 C C     A CYS   B 2 61  ? -36.009 -34.143  -17.373 0.50 47.96  ? 53  CYS   B C     1 
ATOM   5359 C C     B CYS   B 2 61  ? -35.992 -34.127  -17.383 0.50 47.90  ? 53  CYS   B C     1 
ATOM   5360 O O     A CYS   B 2 61  ? -35.483 -33.033  -17.432 0.50 47.39  ? 53  CYS   B O     1 
ATOM   5361 O O     B CYS   B 2 61  ? -35.446 -33.029  -17.466 0.50 47.33  ? 53  CYS   B O     1 
ATOM   5362 C CB    A CYS   B 2 61  ? -38.252 -33.706  -16.328 0.50 48.71  ? 53  CYS   B CB    1 
ATOM   5363 C CB    B CYS   B 2 61  ? -38.152 -33.513  -16.282 0.50 48.56  ? 53  CYS   B CB    1 
ATOM   5364 S SG    A CYS   B 2 61  ? -39.256 -34.166  -17.766 0.50 48.98  ? 53  CYS   B SG    1 
ATOM   5365 S SG    B CYS   B 2 61  ? -39.228 -33.649  -14.830 0.50 48.76  ? 53  CYS   B SG    1 
ATOM   5366 N N     . TRP   B 2 62  ? -35.810 -35.112  -18.275 1.00 48.26  ? 54  TRP   B N     1 
ATOM   5367 C CA    . TRP   B 2 62  ? -35.034 -34.924  -19.491 1.00 47.75  ? 54  TRP   B CA    1 
ATOM   5368 C C     . TRP   B 2 62  ? -35.982 -34.726  -20.670 1.00 47.83  ? 54  TRP   B C     1 
ATOM   5369 O O     . TRP   B 2 62  ? -36.535 -35.687  -21.198 1.00 46.97  ? 54  TRP   B O     1 
ATOM   5370 C CB    . TRP   B 2 62  ? -34.098 -36.118  -19.731 1.00 46.82  ? 54  TRP   B CB    1 
ATOM   5371 C CG    . TRP   B 2 62  ? -33.001 -36.260  -18.709 1.00 46.66  ? 54  TRP   B CG    1 
ATOM   5372 C CD1   . TRP   B 2 62  ? -32.615 -35.349  -17.768 1.00 46.24  ? 54  TRP   B CD1   1 
ATOM   5373 C CD2   . TRP   B 2 62  ? -32.120 -37.393  -18.552 1.00 46.59  ? 54  TRP   B CD2   1 
ATOM   5374 N NE1   . TRP   B 2 62  ? -31.574 -35.839  -17.026 1.00 45.50  ? 54  TRP   B NE1   1 
ATOM   5375 C CE2   . TRP   B 2 62  ? -31.246 -37.088  -17.485 1.00 46.58  ? 54  TRP   B CE2   1 
ATOM   5376 C CE3   . TRP   B 2 62  ? -31.989 -38.627  -19.201 1.00 45.34  ? 54  TRP   B CE3   1 
ATOM   5377 C CZ2   . TRP   B 2 62  ? -30.260 -37.976  -17.059 1.00 46.29  ? 54  TRP   B CZ2   1 
ATOM   5378 C CZ3   . TRP   B 2 62  ? -31.012 -39.501  -18.779 1.00 45.89  ? 54  TRP   B CZ3   1 
ATOM   5379 C CH2   . TRP   B 2 62  ? -30.163 -39.179  -17.720 1.00 46.31  ? 54  TRP   B CH2   1 
ATOM   5380 N N     . ALA   B 2 63  ? -36.162 -33.464  -21.071 1.00 49.35  ? 55  ALA   B N     1 
ATOM   5381 C CA    . ALA   B 2 63  ? -37.112 -33.107  -22.111 1.00 50.68  ? 55  ALA   B CA    1 
ATOM   5382 C C     . ALA   B 2 63  ? -36.660 -31.807  -22.771 1.00 49.29  ? 55  ALA   B C     1 
ATOM   5383 O O     . ALA   B 2 63  ? -35.511 -31.411  -22.603 1.00 47.51  ? 55  ALA   B O     1 
ATOM   5384 C CB    . ALA   B 2 63  ? -38.502 -33.011  -21.514 1.00 51.24  ? 55  ALA   B CB    1 
ATOM   5385 N N     . GLY   B 2 64  ? -37.555 -31.157  -23.527 1.00 50.32  ? 56  GLY   B N     1 
ATOM   5386 C CA    . GLY   B 2 64  ? -37.192 -29.958  -24.265 1.00 51.62  ? 56  GLY   B CA    1 
ATOM   5387 C C     . GLY   B 2 64  ? -38.403 -29.097  -24.618 1.00 52.94  ? 56  GLY   B C     1 
ATOM   5388 O O     . GLY   B 2 64  ? -39.516 -29.358  -24.164 1.00 53.48  ? 56  GLY   B O     1 
ATOM   5389 N N     . SER   B 2 65  ? -38.161 -28.083  -25.457 1.00 52.87  ? 57  SER   B N     1 
ATOM   5390 C CA    . SER   B 2 65  ? -39.115 -27.008  -25.671 1.00 53.04  ? 57  SER   B CA    1 
ATOM   5391 C C     . SER   B 2 65  ? -38.745 -26.208  -26.918 1.00 54.11  ? 57  SER   B C     1 
ATOM   5392 O O     . SER   B 2 65  ? -37.566 -26.013  -27.208 1.00 53.92  ? 57  SER   B O     1 
ATOM   5393 C CB    . SER   B 2 65  ? -39.176 -26.111  -24.463 1.00 52.44  ? 57  SER   B CB    1 
ATOM   5394 O OG    . SER   B 2 65  ? -37.905 -25.532  -24.198 1.00 51.47  ? 57  SER   B OG    1 
ATOM   5395 N N     . LEU   B 2 66  ? -39.773 -25.735  -27.633 1.00 54.69  ? 58  LEU   B N     1 
ATOM   5396 C CA    . LEU   B 2 66  ? -39.597 -24.852  -28.775 1.00 55.76  ? 58  LEU   B CA    1 
ATOM   5397 C C     . LEU   B 2 66  ? -40.121 -23.469  -28.399 1.00 58.16  ? 58  LEU   B C     1 
ATOM   5398 O O     . LEU   B 2 66  ? -41.035 -23.358  -27.585 1.00 57.98  ? 58  LEU   B O     1 
ATOM   5399 C CB    . LEU   B 2 66  ? -40.322 -25.443  -29.984 1.00 54.34  ? 58  LEU   B CB    1 
ATOM   5400 C CG    . LEU   B 2 66  ? -39.894 -26.858  -30.391 1.00 53.05  ? 58  LEU   B CG    1 
ATOM   5401 C CD1   . LEU   B 2 66  ? -40.931 -27.534  -31.275 1.00 52.56  ? 58  LEU   B CD1   1 
ATOM   5402 C CD2   . LEU   B 2 66  ? -38.542 -26.825  -31.085 1.00 52.26  ? 58  LEU   B CD2   1 
ATOM   5403 N N     . TRP   B 2 67  ? -39.519 -22.425  -28.984 1.00 60.93  ? 59  TRP   B N     1 
ATOM   5404 C CA    . TRP   B 2 67  ? -39.786 -21.050  -28.589 1.00 64.24  ? 59  TRP   B CA    1 
ATOM   5405 C C     . TRP   B 2 67  ? -39.678 -20.118  -29.791 1.00 65.70  ? 59  TRP   B C     1 
ATOM   5406 O O     . TRP   B 2 67  ? -38.803 -20.297  -30.633 1.00 67.43  ? 59  TRP   B O     1 
ATOM   5407 C CB    . TRP   B 2 67  ? -38.799 -20.612  -27.499 1.00 66.77  ? 59  TRP   B CB    1 
ATOM   5408 C CG    . TRP   B 2 67  ? -38.935 -21.368  -26.206 1.00 69.76  ? 59  TRP   B CG    1 
ATOM   5409 C CD1   . TRP   B 2 67  ? -38.200 -22.442  -25.796 1.00 71.52  ? 59  TRP   B CD1   1 
ATOM   5410 C CD2   . TRP   B 2 67  ? -39.884 -21.103  -25.153 1.00 72.56  ? 59  TRP   B CD2   1 
ATOM   5411 N NE1   . TRP   B 2 67  ? -38.620 -22.860  -24.562 1.00 72.25  ? 59  TRP   B NE1   1 
ATOM   5412 C CE2   . TRP   B 2 67  ? -39.651 -22.061  -24.142 1.00 72.44  ? 59  TRP   B CE2   1 
ATOM   5413 C CE3   . TRP   B 2 67  ? -40.899 -20.157  -24.966 1.00 73.15  ? 59  TRP   B CE3   1 
ATOM   5414 C CZ2   . TRP   B 2 67  ? -40.398 -22.093  -22.966 1.00 72.14  ? 59  TRP   B CZ2   1 
ATOM   5415 C CZ3   . TRP   B 2 67  ? -41.637 -20.192  -23.803 1.00 73.14  ? 59  TRP   B CZ3   1 
ATOM   5416 C CH2   . TRP   B 2 67  ? -41.389 -21.148  -22.818 1.00 72.52  ? 59  TRP   B CH2   1 
ATOM   5417 N N     . LEU   B 2 68  ? -40.554 -19.106  -29.842 1.00 67.17  ? 60  LEU   B N     1 
ATOM   5418 C CA    . LEU   B 2 68  ? -40.460 -18.052  -30.840 1.00 66.69  ? 60  LEU   B CA    1 
ATOM   5419 C C     . LEU   B 2 68  ? -40.278 -16.712  -30.133 1.00 66.09  ? 60  LEU   B C     1 
ATOM   5420 O O     . LEU   B 2 68  ? -41.020 -16.391  -29.209 1.00 65.49  ? 60  LEU   B O     1 
ATOM   5421 C CB    . LEU   B 2 68  ? -41.690 -18.041  -31.746 1.00 67.02  ? 60  LEU   B CB    1 
ATOM   5422 C CG    . LEU   B 2 68  ? -41.655 -17.052  -32.917 1.00 67.69  ? 60  LEU   B CG    1 
ATOM   5423 C CD1   . LEU   B 2 68  ? -40.390 -17.195  -33.750 1.00 67.49  ? 60  LEU   B CD1   1 
ATOM   5424 C CD2   . LEU   B 2 68  ? -42.883 -17.232  -33.795 1.00 67.41  ? 60  LEU   B CD2   1 
ATOM   5425 N N     . PHE   B 2 69  ? -39.280 -15.946  -30.587 1.00 67.96  ? 61  PHE   B N     1 
ATOM   5426 C CA    . PHE   B 2 69  ? -38.975 -14.638  -30.036 1.00 71.23  ? 61  PHE   B CA    1 
ATOM   5427 C C     . PHE   B 2 69  ? -39.015 -13.591  -31.145 1.00 74.16  ? 61  PHE   B C     1 
ATOM   5428 O O     . PHE   B 2 69  ? -38.062 -13.465  -31.914 1.00 74.63  ? 61  PHE   B O     1 
ATOM   5429 C CB    . PHE   B 2 69  ? -37.601 -14.677  -29.362 1.00 72.37  ? 61  PHE   B CB    1 
ATOM   5430 C CG    . PHE   B 2 69  ? -37.629 -15.150  -27.917 1.00 73.58  ? 61  PHE   B CG    1 
ATOM   5431 C CD1   . PHE   B 2 69  ? -37.591 -16.505  -27.606 1.00 74.70  ? 61  PHE   B CD1   1 
ATOM   5432 C CD2   . PHE   B 2 69  ? -37.688 -14.232  -26.874 1.00 73.81  ? 61  PHE   B CD2   1 
ATOM   5433 C CE1   . PHE   B 2 69  ? -37.615 -16.929  -26.286 1.00 75.14  ? 61  PHE   B CE1   1 
ATOM   5434 C CE2   . PHE   B 2 69  ? -37.713 -14.661  -25.557 1.00 74.47  ? 61  PHE   B CE2   1 
ATOM   5435 C CZ    . PHE   B 2 69  ? -37.673 -16.007  -25.266 1.00 74.92  ? 61  PHE   B CZ    1 
ATOM   5436 N N     . LYS   B 2 70  ? -40.120 -12.836  -31.202 1.00 74.97  ? 62  LYS   B N     1 
ATOM   5437 C CA    . LYS   B 2 70  ? -40.252 -11.728  -32.136 1.00 74.00  ? 62  LYS   B CA    1 
ATOM   5438 C C     . LYS   B 2 70  ? -39.321 -10.589  -31.719 1.00 74.07  ? 62  LYS   B C     1 
ATOM   5439 O O     . LYS   B 2 70  ? -38.921 -9.787   -32.559 1.00 71.84  ? 62  LYS   B O     1 
ATOM   5440 C CB    . LYS   B 2 70  ? -41.723 -11.317  -32.278 1.00 72.83  ? 62  LYS   B CB    1 
ATOM   5441 C CG    . LYS   B 2 70  ? -42.495 -12.199  -33.252 1.00 72.41  ? 62  LYS   B CG    1 
ATOM   5442 C CD    . LYS   B 2 70  ? -44.010 -12.205  -33.090 1.00 72.74  ? 62  LYS   B CD    1 
ATOM   5443 C CE    . LYS   B 2 70  ? -44.657 -13.233  -33.964 1.00 72.93  ? 62  LYS   B CE    1 
ATOM   5444 N NZ    . LYS   B 2 70  ? -45.968 -13.638  -33.449 1.00 73.68  ? 62  LYS   B NZ    1 
ATOM   5445 N N     . ASP   B 2 71  ? -38.981 -10.533  -30.423 1.00 76.06  ? 63  ASP   B N     1 
ATOM   5446 C CA    . ASP   B 2 71  ? -37.898 -9.692   -29.938 1.00 77.36  ? 63  ASP   B CA    1 
ATOM   5447 C C     . ASP   B 2 71  ? -36.663 -10.561  -29.701 1.00 78.29  ? 63  ASP   B C     1 
ATOM   5448 O O     . ASP   B 2 71  ? -36.637 -11.352  -28.761 1.00 78.74  ? 63  ASP   B O     1 
ATOM   5449 C CB    . ASP   B 2 71  ? -38.297 -8.942   -28.676 1.00 77.93  ? 63  ASP   B CB    1 
ATOM   5450 C CG    . ASP   B 2 71  ? -37.264 -7.958   -28.139 1.00 80.38  ? 63  ASP   B CG    1 
ATOM   5451 O OD1   . ASP   B 2 71  ? -36.254 -7.716   -28.839 1.00 81.38  ? 63  ASP   B OD1   1 
ATOM   5452 O OD2   . ASP   B 2 71  ? -37.474 -7.443   -27.020 1.00 80.48  ? 63  ASP   B OD2   1 
ATOM   5453 N N     . PRO   B 2 72  ? -35.605 -10.452  -30.541 1.00 78.16  ? 64  PRO   B N     1 
ATOM   5454 C CA    . PRO   B 2 72  ? -34.353 -11.181  -30.311 1.00 77.21  ? 64  PRO   B CA    1 
ATOM   5455 C C     . PRO   B 2 72  ? -33.666 -10.935  -28.967 1.00 75.57  ? 64  PRO   B C     1 
ATOM   5456 O O     . PRO   B 2 72  ? -32.962 -11.812  -28.469 1.00 74.55  ? 64  PRO   B O     1 
ATOM   5457 C CB    . PRO   B 2 72  ? -33.463 -10.712  -31.481 1.00 78.12  ? 64  PRO   B CB    1 
ATOM   5458 C CG    . PRO   B 2 72  ? -34.440 -10.303  -32.554 1.00 79.26  ? 64  PRO   B CG    1 
ATOM   5459 C CD    . PRO   B 2 72  ? -35.579 -9.666   -31.786 1.00 78.86  ? 64  PRO   B CD    1 
ATOM   5460 N N     . CYS   B 2 73  ? -33.860 -9.738   -28.398 1.00 73.74  ? 65  CYS   B N     1 
ATOM   5461 C CA    . CYS   B 2 73  ? -33.165 -9.328   -27.186 1.00 71.09  ? 65  CYS   B CA    1 
ATOM   5462 C C     . CYS   B 2 73  ? -33.944 -9.715   -25.931 1.00 68.25  ? 65  CYS   B C     1 
ATOM   5463 O O     . CYS   B 2 73  ? -33.404 -9.641   -24.830 1.00 68.16  ? 65  CYS   B O     1 
ATOM   5464 C CB    . CYS   B 2 73  ? -32.901 -7.828   -27.198 1.00 70.26  ? 65  CYS   B CB    1 
ATOM   5465 S SG    . CYS   B 2 73  ? -31.941 -7.297   -28.638 1.00 69.75  ? 65  CYS   B SG    1 
ATOM   5466 N N     . ALA   B 2 74  ? -35.212 -10.116  -26.097 1.00 67.20  ? 66  ALA   B N     1 
ATOM   5467 C CA    . ALA   B 2 74  ? -36.000 -10.641  -24.993 1.00 67.92  ? 66  ALA   B CA    1 
ATOM   5468 C C     . ALA   B 2 74  ? -35.563 -12.072  -24.688 1.00 68.58  ? 66  ALA   B C     1 
ATOM   5469 O O     . ALA   B 2 74  ? -35.795 -12.570  -23.589 1.00 69.13  ? 66  ALA   B O     1 
ATOM   5470 C CB    . ALA   B 2 74  ? -37.475 -10.577  -25.318 1.00 67.32  ? 66  ALA   B CB    1 
ATOM   5471 N N     . ALA   B 2 75  ? -34.937 -12.719  -25.679 1.00 68.09  ? 67  ALA   B N     1 
ATOM   5472 C CA    . ALA   B 2 75  ? -34.424 -14.071  -25.537 1.00 66.18  ? 67  ALA   B CA    1 
ATOM   5473 C C     . ALA   B 2 75  ? -33.194 -14.063  -24.630 1.00 64.31  ? 67  ALA   B C     1 
ATOM   5474 O O     . ALA   B 2 75  ? -32.344 -13.183  -24.757 1.00 62.08  ? 67  ALA   B O     1 
ATOM   5475 C CB    . ALA   B 2 75  ? -34.101 -14.643  -26.900 1.00 66.94  ? 67  ALA   B CB    1 
ATOM   5476 N N     . PRO   B 2 76  ? -33.036 -15.042  -23.706 1.00 63.53  ? 68  PRO   B N     1 
ATOM   5477 C CA    . PRO   B 2 76  ? -33.940 -16.193  -23.589 1.00 63.95  ? 68  PRO   B CA    1 
ATOM   5478 C C     . PRO   B 2 76  ? -35.046 -16.141  -22.533 1.00 65.12  ? 68  PRO   B C     1 
ATOM   5479 O O     . PRO   B 2 76  ? -35.360 -17.162  -21.924 1.00 67.14  ? 68  PRO   B O     1 
ATOM   5480 C CB    . PRO   B 2 76  ? -32.873 -17.250  -23.241 1.00 63.51  ? 68  PRO   B CB    1 
ATOM   5481 C CG    . PRO   B 2 76  ? -31.966 -16.541  -22.257 1.00 63.20  ? 68  PRO   B CG    1 
ATOM   5482 C CD    . PRO   B 2 76  ? -31.926 -15.103  -22.742 1.00 63.25  ? 68  PRO   B CD    1 
ATOM   5483 N N     . ASN   B 2 77  ? -35.650 -14.962  -22.327 1.00 64.56  ? 69  ASN   B N     1 
ATOM   5484 C CA    . ASN   B 2 77  ? -36.612 -14.773  -21.249 1.00 65.78  ? 69  ASN   B CA    1 
ATOM   5485 C C     . ASN   B 2 77  ? -37.977 -15.321  -21.660 1.00 66.63  ? 69  ASN   B C     1 
ATOM   5486 O O     . ASN   B 2 77  ? -38.556 -14.871  -22.643 1.00 69.75  ? 69  ASN   B O     1 
ATOM   5487 C CB    . ASN   B 2 77  ? -36.723 -13.310  -20.835 1.00 66.77  ? 69  ASN   B CB    1 
ATOM   5488 C CG    . ASN   B 2 77  ? -37.548 -13.133  -19.581 1.00 66.50  ? 69  ASN   B CG    1 
ATOM   5489 O OD1   . ASN   B 2 77  ? -38.711 -13.549  -19.537 1.00 65.63  ? 69  ASN   B OD1   1 
ATOM   5490 N ND2   . ASN   B 2 77  ? -36.972 -12.526  -18.553 1.00 66.48  ? 69  ASN   B ND2   1 
ATOM   5491 N N     . GLU   B 2 78  ? -38.516 -16.225  -20.835 1.00 66.86  ? 70  GLU   B N     1 
ATOM   5492 C CA    . GLU   B 2 78  ? -39.653 -17.060  -21.195 1.00 68.05  ? 70  GLU   B CA    1 
ATOM   5493 C C     . GLU   B 2 78  ? -40.916 -16.222  -21.387 1.00 69.51  ? 70  GLU   B C     1 
ATOM   5494 O O     . GLU   B 2 78  ? -41.592 -16.344  -22.406 1.00 68.74  ? 70  GLU   B O     1 
ATOM   5495 C CB    . GLU   B 2 78  ? -39.932 -18.109  -20.117 1.00 68.58  ? 70  GLU   B CB    1 
ATOM   5496 C CG    . GLU   B 2 78  ? -38.741 -19.009  -19.798 1.00 68.56  ? 70  GLU   B CG    1 
ATOM   5497 C CD    . GLU   B 2 78  ? -37.715 -18.426  -18.841 1.00 68.39  ? 70  GLU   B CD    1 
ATOM   5498 O OE1   . GLU   B 2 78  ? -38.073 -18.169  -17.673 1.00 68.73  ? 70  GLU   B OE1   1 
ATOM   5499 O OE2   . GLU   B 2 78  ? -36.560 -18.219  -19.267 1.00 68.29  ? 70  GLU   B OE2   1 
ATOM   5500 N N     . GLY   B 2 79  ? -41.225 -15.374  -20.398 1.00 70.77  ? 71  GLY   B N     1 
ATOM   5501 C CA    . GLY   B 2 79  ? -42.473 -14.627  -20.372 1.00 70.29  ? 71  GLY   B CA    1 
ATOM   5502 C C     . GLY   B 2 79  ? -42.455 -13.406  -21.290 1.00 70.79  ? 71  GLY   B C     1 
ATOM   5503 O O     . GLY   B 2 79  ? -43.412 -12.634  -21.300 1.00 71.13  ? 71  GLY   B O     1 
ATOM   5504 N N     . PHE   B 2 80  ? -41.361 -13.229  -22.045 1.00 70.66  ? 72  PHE   B N     1 
ATOM   5505 C CA    . PHE   B 2 80  ? -41.260 -12.177  -23.044 1.00 70.63  ? 72  PHE   B CA    1 
ATOM   5506 C C     . PHE   B 2 80  ? -41.050 -12.817  -24.415 1.00 70.08  ? 72  PHE   B C     1 
ATOM   5507 O O     . PHE   B 2 80  ? -40.166 -12.414  -25.169 1.00 70.14  ? 72  PHE   B O     1 
ATOM   5508 C CB    . PHE   B 2 80  ? -40.152 -11.217  -22.597 1.00 71.41  ? 72  PHE   B CB    1 
ATOM   5509 C CG    . PHE   B 2 80  ? -40.552 -10.327  -21.427 1.00 72.62  ? 72  PHE   B CG    1 
ATOM   5510 C CD1   . PHE   B 2 80  ? -40.629 -10.835  -20.133 1.00 72.60  ? 72  PHE   B CD1   1 
ATOM   5511 C CD2   . PHE   B 2 80  ? -40.852 -8.982   -21.626 1.00 72.36  ? 72  PHE   B CD2   1 
ATOM   5512 C CE1   . PHE   B 2 80  ? -41.001 -10.023  -19.071 1.00 71.82  ? 72  PHE   B CE1   1 
ATOM   5513 C CE2   . PHE   B 2 80  ? -41.219 -8.173   -20.560 1.00 72.48  ? 72  PHE   B CE2   1 
ATOM   5514 C CZ    . PHE   B 2 80  ? -41.293 -8.694   -19.286 1.00 71.92  ? 72  PHE   B CZ    1 
ATOM   5515 N N     . CYS   B 2 81  ? -41.893 -13.812  -24.722 1.00 68.74  ? 73  CYS   B N     1 
ATOM   5516 C CA    . CYS   B 2 81  ? -41.827 -14.550  -25.972 1.00 66.97  ? 73  CYS   B CA    1 
ATOM   5517 C C     . CYS   B 2 81  ? -43.203 -14.555  -26.633 1.00 66.21  ? 73  CYS   B C     1 
ATOM   5518 O O     . CYS   B 2 81  ? -44.219 -14.361  -25.969 1.00 65.23  ? 73  CYS   B O     1 
ATOM   5519 C CB    . CYS   B 2 81  ? -41.374 -15.987  -25.744 1.00 66.87  ? 73  CYS   B CB    1 
ATOM   5520 S SG    . CYS   B 2 81  ? -42.710 -17.091  -25.211 1.00 67.15  ? 73  CYS   B SG    1 
ATOM   5521 N N     . SER   B 2 82  ? -43.213 -14.810  -27.945 1.00 65.34  ? 74  SER   B N     1 
ATOM   5522 C CA    . SER   B 2 82  ? -44.424 -14.761  -28.747 1.00 65.23  ? 74  SER   B CA    1 
ATOM   5523 C C     . SER   B 2 82  ? -45.157 -16.099  -28.683 1.00 65.84  ? 74  SER   B C     1 
ATOM   5524 O O     . SER   B 2 82  ? -46.384 -16.131  -28.628 1.00 67.30  ? 74  SER   B O     1 
ATOM   5525 C CB    . SER   B 2 82  ? -44.098 -14.389  -30.167 1.00 66.26  ? 74  SER   B CB    1 
ATOM   5526 O OG    . SER   B 2 82  ? -43.032 -13.450  -30.209 1.00 67.07  ? 74  SER   B OG    1 
ATOM   5527 N N     . ALA   B 2 83  ? -44.390 -17.197  -28.712 1.00 65.78  ? 75  ALA   B N     1 
ATOM   5528 C CA    . ALA   B 2 83  ? -44.951 -18.537  -28.654 1.00 64.66  ? 75  ALA   B CA    1 
ATOM   5529 C C     . ALA   B 2 83  ? -43.950 -19.497  -28.017 1.00 64.53  ? 75  ALA   B C     1 
ATOM   5530 O O     . ALA   B 2 83  ? -42.745 -19.257  -28.046 1.00 64.32  ? 75  ALA   B O     1 
ATOM   5531 C CB    . ALA   B 2 83  ? -45.347 -18.984  -30.043 1.00 64.64  ? 75  ALA   B CB    1 
ATOM   5532 N N     . GLY   B 2 84  ? -44.476 -20.584  -27.441 1.00 64.49  ? 76  GLY   B N     1 
ATOM   5533 C CA    . GLY   B 2 84  ? -43.674 -21.572  -26.738 1.00 64.22  ? 76  GLY   B CA    1 
ATOM   5534 C C     . GLY   B 2 84  ? -44.467 -22.858  -26.521 1.00 64.37  ? 76  GLY   B C     1 
ATOM   5535 O O     . GLY   B 2 84  ? -45.685 -22.814  -26.364 1.00 64.51  ? 76  GLY   B O     1 
ATOM   5536 N N     . VAL   B 2 85  ? -43.767 -24.000  -26.522 1.00 64.42  ? 77  VAL   B N     1 
ATOM   5537 C CA    . VAL   B 2 85  ? -44.415 -25.292  -26.371 1.00 64.78  ? 77  VAL   B CA    1 
ATOM   5538 C C     . VAL   B 2 85  ? -43.474 -26.240  -25.631 1.00 66.20  ? 77  VAL   B C     1 
ATOM   5539 O O     . VAL   B 2 85  ? -42.262 -26.030  -25.616 1.00 64.80  ? 77  VAL   B O     1 
ATOM   5540 C CB    . VAL   B 2 85  ? -44.836 -25.864  -27.739 1.00 65.13  ? 77  VAL   B CB    1 
ATOM   5541 C CG1   . VAL   B 2 85  ? -43.652 -26.420  -28.522 1.00 65.47  ? 77  VAL   B CG1   1 
ATOM   5542 C CG2   . VAL   B 2 85  ? -45.928 -26.919  -27.608 1.00 65.19  ? 77  VAL   B CG2   1 
ATOM   5543 N N     . GLN   B 2 86  ? -44.061 -27.275  -25.016 1.00 68.45  ? 78  GLN   B N     1 
ATOM   5544 C CA    . GLN   B 2 86  ? -43.313 -28.303  -24.312 1.00 69.06  ? 78  GLN   B CA    1 
ATOM   5545 C C     . GLN   B 2 86  ? -43.243 -29.556  -25.182 1.00 68.52  ? 78  GLN   B C     1 
ATOM   5546 O O     . GLN   B 2 86  ? -44.251 -29.977  -25.746 1.00 69.59  ? 78  GLN   B O     1 
ATOM   5547 C CB    . GLN   B 2 86  ? -43.999 -28.617  -22.982 1.00 69.76  ? 78  GLN   B CB    1 
ATOM   5548 C CG    . GLN   B 2 86  ? -43.154 -29.435  -22.010 1.00 70.81  ? 78  GLN   B CG    1 
ATOM   5549 C CD    . GLN   B 2 86  ? -42.116 -28.614  -21.275 1.00 72.18  ? 78  GLN   B CD    1 
ATOM   5550 O OE1   . GLN   B 2 86  ? -42.249 -28.335  -20.077 1.00 72.53  ? 78  GLN   B OE1   1 
ATOM   5551 N NE2   . GLN   B 2 86  ? -41.071 -28.212  -21.983 1.00 72.47  ? 78  GLN   B NE2   1 
ATOM   5552 N N     . THR   B 2 87  ? -42.042 -30.141  -25.277 1.00 67.11  ? 79  THR   B N     1 
ATOM   5553 C CA    . THR   B 2 87  ? -41.833 -31.382  -26.005 1.00 64.99  ? 79  THR   B CA    1 
ATOM   5554 C C     . THR   B 2 87  ? -41.603 -32.501  -24.990 1.00 61.72  ? 79  THR   B C     1 
ATOM   5555 O O     . THR   B 2 87  ? -41.001 -32.274  -23.942 1.00 60.53  ? 79  THR   B O     1 
ATOM   5556 C CB    . THR   B 2 87  ? -40.657 -31.226  -26.972 1.00 64.92  ? 79  THR   B CB    1 
ATOM   5557 O OG1   . THR   B 2 87  ? -39.473 -31.178  -26.183 1.00 65.02  ? 79  THR   B OG1   1 
ATOM   5558 C CG2   . THR   B 2 87  ? -40.745 -29.963  -27.809 1.00 65.05  ? 79  THR   B CG2   1 
ATOM   5559 N N     . GLU   B 2 88  ? -42.100 -33.701  -25.310 1.00 59.38  ? 80  GLU   B N     1 
ATOM   5560 C CA    . GLU   B 2 88  ? -41.961 -34.858  -24.437 1.00 58.99  ? 80  GLU   B CA    1 
ATOM   5561 C C     . GLU   B 2 88  ? -40.483 -35.112  -24.145 1.00 57.25  ? 80  GLU   B C     1 
ATOM   5562 O O     . GLU   B 2 88  ? -40.118 -35.394  -23.006 1.00 57.66  ? 80  GLU   B O     1 
ATOM   5563 C CB    . GLU   B 2 88  ? -42.611 -36.099  -25.054 1.00 59.75  ? 80  GLU   B CB    1 
ATOM   5564 C CG    . GLU   B 2 88  ? -41.958 -36.558  -26.356 1.00 61.51  ? 80  GLU   B CG    1 
ATOM   5565 C CD    . GLU   B 2 88  ? -42.601 -37.758  -27.025 1.00 64.38  ? 80  GLU   B CD    1 
ATOM   5566 O OE1   . GLU   B 2 88  ? -43.540 -38.342  -26.442 1.00 67.20  ? 80  GLU   B OE1   1 
ATOM   5567 O OE2   . GLU   B 2 88  ? -42.149 -38.107  -28.138 1.00 64.57  ? 80  GLU   B OE2   1 
ATOM   5568 N N     . ALA   B 2 89  ? -39.647 -34.998  -25.187 1.00 53.40  ? 81  ALA   B N     1 
ATOM   5569 C CA    . ALA   B 2 89  ? -38.229 -35.303  -25.098 1.00 49.49  ? 81  ALA   B CA    1 
ATOM   5570 C C     . ALA   B 2 89  ? -37.418 -34.110  -25.595 1.00 46.94  ? 81  ALA   B C     1 
ATOM   5571 O O     . ALA   B 2 89  ? -37.976 -33.154  -26.126 1.00 47.98  ? 81  ALA   B O     1 
ATOM   5572 C CB    . ALA   B 2 89  ? -37.924 -36.552  -25.893 1.00 48.55  ? 81  ALA   B CB    1 
ATOM   5573 N N     . GLY   B 2 90  ? -36.096 -34.186  -25.415 1.00 44.29  ? 82  GLY   B N     1 
ATOM   5574 C CA    . GLY   B 2 90  ? -35.200 -33.094  -25.753 1.00 42.28  ? 82  GLY   B CA    1 
ATOM   5575 C C     . GLY   B 2 90  ? -35.048 -32.921  -27.262 1.00 41.84  ? 82  GLY   B C     1 
ATOM   5576 O O     . GLY   B 2 90  ? -35.424 -33.794  -28.042 1.00 40.97  ? 82  GLY   B O     1 
ATOM   5577 N N     . VAL   B 2 91  ? -34.483 -31.769  -27.636 1.00 40.86  ? 83  VAL   B N     1 
ATOM   5578 C CA    . VAL   B 2 91  ? -34.260 -31.379  -29.015 1.00 40.30  ? 83  VAL   B CA    1 
ATOM   5579 C C     . VAL   B 2 91  ? -32.766 -31.471  -29.309 1.00 39.97  ? 83  VAL   B C     1 
ATOM   5580 O O     . VAL   B 2 91  ? -31.975 -30.743  -28.714 1.00 39.06  ? 83  VAL   B O     1 
ATOM   5581 C CB    . VAL   B 2 91  ? -34.792 -29.944  -29.211 1.00 41.31  ? 83  VAL   B CB    1 
ATOM   5582 C CG1   . VAL   B 2 91  ? -34.412 -29.350  -30.564 1.00 41.55  ? 83  VAL   B CG1   1 
ATOM   5583 C CG2   . VAL   B 2 91  ? -36.301 -29.871  -29.000 1.00 41.48  ? 83  VAL   B CG2   1 
ATOM   5584 N N     . ALA   B 2 92  ? -32.397 -32.370  -30.231 1.00 40.41  ? 84  ALA   B N     1 
ATOM   5585 C CA    . ALA   B 2 92  ? -31.023 -32.501  -30.691 1.00 40.41  ? 84  ALA   B CA    1 
ATOM   5586 C C     . ALA   B 2 92  ? -30.778 -31.559  -31.867 1.00 41.21  ? 84  ALA   B C     1 
ATOM   5587 O O     . ALA   B 2 92  ? -29.707 -30.966  -31.974 1.00 42.33  ? 84  ALA   B O     1 
ATOM   5588 C CB    . ALA   B 2 92  ? -30.744 -33.935  -31.071 1.00 40.48  ? 84  ALA   B CB    1 
ATOM   5589 N N     . ASP   B 2 93  ? -31.778 -31.440  -32.748 1.00 41.78  ? 85  ASP   B N     1 
ATOM   5590 C CA    . ASP   B 2 93  ? -31.701 -30.538  -33.886 1.00 42.25  ? 85  ASP   B CA    1 
ATOM   5591 C C     . ASP   B 2 93  ? -33.110 -30.076  -34.247 1.00 43.29  ? 85  ASP   B C     1 
ATOM   5592 O O     . ASP   B 2 93  ? -34.096 -30.717  -33.884 1.00 41.43  ? 85  ASP   B O     1 
ATOM   5593 C CB    . ASP   B 2 93  ? -31.010 -31.204  -35.069 1.00 41.02  ? 85  ASP   B CB    1 
ATOM   5594 C CG    . ASP   B 2 93  ? -30.466 -30.275  -36.149 1.00 40.47  ? 85  ASP   B CG    1 
ATOM   5595 O OD1   . ASP   B 2 93  ? -30.440 -29.043  -35.922 1.00 38.51  ? 85  ASP   B OD1   1 
ATOM   5596 O OD2   . ASP   B 2 93  ? -30.071 -30.792  -37.219 1.00 39.40  ? 85  ASP   B OD2   1 
ATOM   5597 N N     . LEU   B 2 94  ? -33.186 -28.945  -34.955 1.00 46.09  ? 86  LEU   B N     1 
ATOM   5598 C CA    . LEU   B 2 94  ? -34.428 -28.488  -35.555 1.00 48.01  ? 86  LEU   B CA    1 
ATOM   5599 C C     . LEU   B 2 94  ? -34.104 -27.669  -36.799 1.00 50.29  ? 86  LEU   B C     1 
ATOM   5600 O O     . LEU   B 2 94  ? -32.944 -27.344  -37.047 1.00 51.17  ? 86  LEU   B O     1 
ATOM   5601 C CB    . LEU   B 2 94  ? -35.265 -27.683  -34.560 1.00 47.50  ? 86  LEU   B CB    1 
ATOM   5602 C CG    . LEU   B 2 94  ? -34.560 -26.524  -33.845 1.00 47.15  ? 86  LEU   B CG    1 
ATOM   5603 C CD1   . LEU   B 2 94  ? -34.221 -25.348  -34.751 1.00 47.32  ? 86  LEU   B CD1   1 
ATOM   5604 C CD2   . LEU   B 2 94  ? -35.427 -26.055  -32.693 1.00 47.24  ? 86  LEU   B CD2   1 
ATOM   5605 N N     . THR   B 2 95  ? -35.144 -27.338  -37.571 1.00 51.36  ? 87  THR   B N     1 
ATOM   5606 C CA    . THR   B 2 95  ? -35.005 -26.373  -38.649 1.00 52.16  ? 87  THR   B CA    1 
ATOM   5607 C C     . THR   B 2 95  ? -36.372 -25.814  -39.029 1.00 51.38  ? 87  THR   B C     1 
ATOM   5608 O O     . THR   B 2 95  ? -37.404 -26.447  -38.808 1.00 49.28  ? 87  THR   B O     1 
ATOM   5609 C CB    . THR   B 2 95  ? -34.312 -27.009  -39.855 1.00 52.34  ? 87  THR   B CB    1 
ATOM   5610 O OG1   . THR   B 2 95  ? -34.212 -25.948  -40.801 1.00 52.07  ? 87  THR   B OG1   1 
ATOM   5611 C CG2   . THR   B 2 95  ? -35.082 -28.187  -40.424 1.00 51.89  ? 87  THR   B CG2   1 
ATOM   5612 N N     . TRP   B 2 96  ? -36.331 -24.610  -39.610 1.00 50.99  ? 88  TRP   B N     1 
ATOM   5613 C CA    . TRP   B 2 96  ? -37.484 -23.977  -40.224 1.00 50.62  ? 88  TRP   B CA    1 
ATOM   5614 C C     . TRP   B 2 96  ? -37.955 -24.792  -41.425 1.00 51.81  ? 88  TRP   B C     1 
ATOM   5615 O O     . TRP   B 2 96  ? -37.140 -25.317  -42.179 1.00 51.98  ? 88  TRP   B O     1 
ATOM   5616 C CB    . TRP   B 2 96  ? -37.116 -22.549  -40.650 1.00 49.69  ? 88  TRP   B CB    1 
ATOM   5617 C CG    . TRP   B 2 96  ? -37.223 -21.531  -39.547 1.00 48.41  ? 88  TRP   B CG    1 
ATOM   5618 C CD1   . TRP   B 2 96  ? -36.228 -20.743  -39.048 1.00 47.98  ? 88  TRP   B CD1   1 
ATOM   5619 C CD2   . TRP   B 2 96  ? -38.424 -21.156  -38.841 1.00 48.06  ? 88  TRP   B CD2   1 
ATOM   5620 N NE1   . TRP   B 2 96  ? -36.718 -19.926  -38.063 1.00 48.43  ? 88  TRP   B NE1   1 
ATOM   5621 C CE2   . TRP   B 2 96  ? -38.062 -20.151  -37.919 1.00 48.39  ? 88  TRP   B CE2   1 
ATOM   5622 C CE3   . TRP   B 2 96  ? -39.759 -21.573  -38.896 1.00 48.49  ? 88  TRP   B CE3   1 
ATOM   5623 C CZ2   . TRP   B 2 96  ? -38.991 -19.562  -37.062 1.00 48.70  ? 88  TRP   B CZ2   1 
ATOM   5624 C CZ3   . TRP   B 2 96  ? -40.676 -20.987  -38.052 1.00 48.16  ? 88  TRP   B CZ3   1 
ATOM   5625 C CH2   . TRP   B 2 96  ? -40.295 -19.994  -37.149 1.00 48.63  ? 88  TRP   B CH2   1 
ATOM   5626 N N     . VAL   B 2 97  ? -39.279 -24.893  -41.579 1.00 53.75  ? 89  VAL   B N     1 
ATOM   5627 C CA    . VAL   B 2 97  ? -39.894 -25.406  -42.791 1.00 55.21  ? 89  VAL   B CA    1 
ATOM   5628 C C     . VAL   B 2 97  ? -40.679 -24.250  -43.410 1.00 58.30  ? 89  VAL   B C     1 
ATOM   5629 O O     . VAL   B 2 97  ? -41.884 -24.121  -43.204 1.00 61.28  ? 89  VAL   B O     1 
ATOM   5630 C CB    . VAL   B 2 97  ? -40.779 -26.637  -42.509 1.00 54.42  ? 89  VAL   B CB    1 
ATOM   5631 C CG1   . VAL   B 2 97  ? -41.493 -27.146  -43.757 1.00 54.50  ? 89  VAL   B CG1   1 
ATOM   5632 C CG2   . VAL   B 2 97  ? -39.981 -27.765  -41.870 1.00 54.60  ? 89  VAL   B CG2   1 
ATOM   5633 N N     . GLY   B 2 98  ? -39.962 -23.391  -44.140 1.00 58.92  ? 90  GLY   B N     1 
ATOM   5634 C CA    . GLY   B 2 98  ? -40.537 -22.174  -44.683 1.00 60.95  ? 90  GLY   B CA    1 
ATOM   5635 C C     . GLY   B 2 98  ? -40.597 -21.084  -43.618 1.00 64.27  ? 90  GLY   B C     1 
ATOM   5636 O O     . GLY   B 2 98  ? -39.561 -20.659  -43.109 1.00 66.03  ? 90  GLY   B O     1 
ATOM   5637 N N     . GLU   B 2 99  ? -41.821 -20.653  -43.287 1.00 67.13  ? 91  GLU   B N     1 
ATOM   5638 C CA    . GLU   B 2 99  ? -42.035 -19.536  -42.379 1.00 68.25  ? 91  GLU   B CA    1 
ATOM   5639 C C     . GLU   B 2 99  ? -42.731 -19.991  -41.096 1.00 67.63  ? 91  GLU   B C     1 
ATOM   5640 O O     . GLU   B 2 99  ? -42.500 -19.401  -40.044 1.00 66.93  ? 91  GLU   B O     1 
ATOM   5641 C CB    . GLU   B 2 99  ? -42.841 -18.438  -43.074 1.00 69.04  ? 91  GLU   B CB    1 
ATOM   5642 C CG    . GLU   B 2 99  ? -42.074 -17.734  -44.191 1.00 69.80  ? 91  GLU   B CG    1 
ATOM   5643 C CD    . GLU   B 2 99  ? -40.891 -16.900  -43.727 1.00 69.63  ? 91  GLU   B CD    1 
ATOM   5644 O OE1   . GLU   B 2 99  ? -41.115 -15.880  -43.042 1.00 69.52  ? 91  GLU   B OE1   1 
ATOM   5645 O OE2   . GLU   B 2 99  ? -39.742 -17.276  -44.047 1.00 68.71  ? 91  GLU   B OE2   1 
ATOM   5646 N N     . ARG   B 2 100 ? -43.580 -21.024  -41.185 1.00 69.04  ? 92  ARG   B N     1 
ATOM   5647 C CA    . ARG   B 2 100 ? -44.425 -21.422  -40.069 1.00 70.58  ? 92  ARG   B CA    1 
ATOM   5648 C C     . ARG   B 2 100 ? -44.044 -22.792  -39.508 1.00 67.65  ? 92  ARG   B C     1 
ATOM   5649 O O     . ARG   B 2 100 ? -44.319 -23.065  -38.342 1.00 67.28  ? 92  ARG   B O     1 
ATOM   5650 C CB    . ARG   B 2 100 ? -45.898 -21.392  -40.490 1.00 74.70  ? 92  ARG   B CB    1 
ATOM   5651 C CG    . ARG   B 2 100 ? -46.432 -19.977  -40.660 1.00 79.39  ? 92  ARG   B CG    1 
ATOM   5652 C CD    . ARG   B 2 100 ? -47.945 -19.907  -40.535 1.00 82.88  ? 92  ARG   B CD    1 
ATOM   5653 N NE    . ARG   B 2 100 ? -48.372 -18.623  -39.966 1.00 86.63  ? 92  ARG   B NE    1 
ATOM   5654 C CZ    . ARG   B 2 100 ? -49.568 -18.372  -39.441 1.00 90.55  ? 92  ARG   B CZ    1 
ATOM   5655 N NH1   . ARG   B 2 100 ? -50.511 -19.300  -39.437 1.00 92.50  ? 92  ARG   B NH1   1 
ATOM   5656 N NH2   . ARG   B 2 100 ? -49.820 -17.185  -38.915 1.00 91.22  ? 92  ARG   B NH2   1 
ATOM   5657 N N     . GLY   B 2 101 ? -43.435 -23.655  -40.331 1.00 65.05  ? 93  GLY   B N     1 
ATOM   5658 C CA    . GLY   B 2 101 ? -43.151 -25.026  -39.933 1.00 62.76  ? 93  GLY   B CA    1 
ATOM   5659 C C     . GLY   B 2 101 ? -41.851 -25.140  -39.138 1.00 60.60  ? 93  GLY   B C     1 
ATOM   5660 O O     . GLY   B 2 101 ? -40.901 -24.400  -39.386 1.00 57.67  ? 93  GLY   B O     1 
ATOM   5661 N N     . ILE   B 2 102 ? -41.828 -26.083  -38.183 1.00 59.42  ? 94  ILE   B N     1 
ATOM   5662 C CA    . ILE   B 2 102 ? -40.655 -26.355  -37.363 1.00 58.01  ? 94  ILE   B CA    1 
ATOM   5663 C C     . ILE   B 2 102 ? -40.415 -27.863  -37.336 1.00 54.39  ? 94  ILE   B C     1 
ATOM   5664 O O     . ILE   B 2 102 ? -41.260 -28.613  -36.853 1.00 53.05  ? 94  ILE   B O     1 
ATOM   5665 C CB    . ILE   B 2 102 ? -40.820 -25.806  -35.933 1.00 58.88  ? 94  ILE   B CB    1 
ATOM   5666 C CG1   . ILE   B 2 102 ? -41.283 -24.343  -35.919 1.00 59.59  ? 94  ILE   B CG1   1 
ATOM   5667 C CG2   . ILE   B 2 102 ? -39.528 -26.001  -35.137 1.00 58.27  ? 94  ILE   B CG2   1 
ATOM   5668 C CD1   . ILE   B 2 102 ? -41.781 -23.863  -34.567 1.00 59.85  ? 94  ILE   B CD1   1 
ATOM   5669 N N     . LEU   B 2 103 ? -39.241 -28.286  -37.825 1.00 52.37  ? 95  LEU   B N     1 
ATOM   5670 C CA    . LEU   B 2 103 ? -38.897 -29.696  -37.934 1.00 51.26  ? 95  LEU   B CA    1 
ATOM   5671 C C     . LEU   B 2 103 ? -37.898 -30.059  -36.838 1.00 48.65  ? 95  LEU   B C     1 
ATOM   5672 O O     . LEU   B 2 103 ? -36.894 -29.371  -36.676 1.00 47.22  ? 95  LEU   B O     1 
ATOM   5673 C CB    . LEU   B 2 103 ? -38.321 -29.949  -39.326 1.00 51.32  ? 95  LEU   B CB    1 
ATOM   5674 C CG    . LEU   B 2 103 ? -38.019 -31.410  -39.674 1.00 51.13  ? 95  LEU   B CG    1 
ATOM   5675 C CD1   . LEU   B 2 103 ? -39.301 -32.187  -39.934 1.00 50.69  ? 95  LEU   B CD1   1 
ATOM   5676 C CD2   . LEU   B 2 103 ? -37.078 -31.489  -40.862 1.00 51.48  ? 95  LEU   B CD2   1 
ATOM   5677 N N     . VAL   B 2 104 ? -38.163 -31.161  -36.122 1.00 46.48  ? 96  VAL   B N     1 
ATOM   5678 C CA    . VAL   B 2 104 ? -37.469 -31.458  -34.877 1.00 45.57  ? 96  VAL   B CA    1 
ATOM   5679 C C     . VAL   B 2 104 ? -36.827 -32.844  -34.941 1.00 42.49  ? 96  VAL   B C     1 
ATOM   5680 O O     . VAL   B 2 104 ? -37.485 -33.827  -35.277 1.00 40.89  ? 96  VAL   B O     1 
ATOM   5681 C CB    . VAL   B 2 104 ? -38.444 -31.356  -33.687 1.00 45.98  ? 96  VAL   B CB    1 
ATOM   5682 C CG1   . VAL   B 2 104 ? -37.744 -31.574  -32.349 1.00 45.97  ? 96  VAL   B CG1   1 
ATOM   5683 C CG2   . VAL   B 2 104 ? -39.194 -30.029  -33.681 1.00 46.18  ? 96  VAL   B CG2   1 
ATOM   5684 N N     . ALA   B 2 105 ? -35.532 -32.894  -34.602 1.00 41.05  ? 97  ALA   B N     1 
ATOM   5685 C CA    . ALA   B 2 105 ? -34.831 -34.135  -34.311 1.00 40.32  ? 97  ALA   B CA    1 
ATOM   5686 C C     . ALA   B 2 105 ? -34.896 -34.401  -32.807 1.00 38.63  ? 97  ALA   B C     1 
ATOM   5687 O O     . ALA   B 2 105 ? -34.272 -33.685  -32.029 1.00 38.27  ? 97  ALA   B O     1 
ATOM   5688 C CB    . ALA   B 2 105 ? -33.398 -34.042  -34.793 1.00 39.72  ? 97  ALA   B CB    1 
ATOM   5689 N N     . SER   B 2 106 ? -35.656 -35.430  -32.414 1.00 38.40  ? 98  SER   B N     1 
ATOM   5690 C CA    . SER   B 2 106 ? -35.901 -35.731  -31.011 1.00 39.11  ? 98  SER   B CA    1 
ATOM   5691 C C     . SER   B 2 106 ? -34.956 -36.827  -30.516 1.00 39.34  ? 98  SER   B C     1 
ATOM   5692 O O     . SER   B 2 106 ? -34.497 -37.660  -31.296 1.00 39.66  ? 98  SER   B O     1 
ATOM   5693 C CB    . SER   B 2 106 ? -37.339 -36.135  -30.801 1.00 39.53  ? 98  SER   B CB    1 
ATOM   5694 O OG    . SER   B 2 106 ? -37.648 -36.265  -29.420 1.00 40.24  ? 98  SER   B OG    1 
ATOM   5695 N N     . ASP   B 2 107 ? -34.692 -36.816  -29.200 1.00 39.52  ? 99  ASP   B N     1 
ATOM   5696 C CA    . ASP   B 2 107 ? -33.998 -37.898  -28.515 1.00 38.43  ? 99  ASP   B CA    1 
ATOM   5697 C C     . ASP   B 2 107 ? -34.809 -39.186  -28.598 1.00 39.65  ? 99  ASP   B C     1 
ATOM   5698 O O     . ASP   B 2 107 ? -34.244 -40.277  -28.610 1.00 41.31  ? 99  ASP   B O     1 
ATOM   5699 C CB    . ASP   B 2 107 ? -33.789 -37.602  -27.039 1.00 37.45  ? 99  ASP   B CB    1 
ATOM   5700 C CG    . ASP   B 2 107 ? -32.834 -36.462  -26.726 1.00 37.15  ? 99  ASP   B CG    1 
ATOM   5701 O OD1   . ASP   B 2 107 ? -31.717 -36.473  -27.276 1.00 37.07  ? 99  ASP   B OD1   1 
ATOM   5702 O OD2   . ASP   B 2 107 ? -33.207 -35.580  -25.924 1.00 36.17  ? 99  ASP   B OD2   1 
ATOM   5703 N N     . SER   B 2 108 ? -36.138 -39.041  -28.641 1.00 40.79  ? 100 SER   B N     1 
ATOM   5704 C CA    . SER   B 2 108 ? -37.061 -40.163  -28.658 1.00 42.62  ? 100 SER   B CA    1 
ATOM   5705 C C     . SER   B 2 108 ? -36.818 -41.081  -29.855 1.00 43.97  ? 100 SER   B C     1 
ATOM   5706 O O     . SER   B 2 108 ? -37.308 -42.209  -29.873 1.00 42.91  ? 100 SER   B O     1 
ATOM   5707 C CB    . SER   B 2 108 ? -38.483 -39.666  -28.656 1.00 43.64  ? 100 SER   B CB    1 
ATOM   5708 O OG    . SER   B 2 108 ? -38.729 -38.814  -29.768 1.00 43.35  ? 100 SER   B OG    1 
ATOM   5709 N N     . GLY   B 2 109 ? -36.079 -40.587  -30.857 1.00 46.54  ? 101 GLY   B N     1 
ATOM   5710 C CA    . GLY   B 2 109 ? -35.931 -41.281  -32.124 1.00 49.39  ? 101 GLY   B CA    1 
ATOM   5711 C C     . GLY   B 2 109 ? -37.022 -40.863  -33.107 1.00 51.19  ? 101 GLY   B C     1 
ATOM   5712 O O     . GLY   B 2 109 ? -37.122 -41.413  -34.202 1.00 51.19  ? 101 GLY   B O     1 
ATOM   5713 N N     . ALA   B 2 110 ? -37.836 -39.882  -32.696 1.00 53.52  ? 102 ALA   B N     1 
ATOM   5714 C CA    . ALA   B 2 110 ? -38.887 -39.348  -33.543 1.00 54.29  ? 102 ALA   B CA    1 
ATOM   5715 C C     . ALA   B 2 110 ? -38.367 -38.136  -34.306 1.00 54.27  ? 102 ALA   B C     1 
ATOM   5716 O O     . ALA   B 2 110 ? -37.531 -37.383  -33.805 1.00 50.91  ? 102 ALA   B O     1 
ATOM   5717 C CB    . ALA   B 2 110 ? -40.095 -38.973  -32.717 1.00 54.22  ? 102 ALA   B CB    1 
ATOM   5718 N N     . VAL   B 2 111 ? -38.878 -37.985  -35.531 1.00 55.06  ? 103 VAL   B N     1 
ATOM   5719 C CA    . VAL   B 2 111 ? -38.833 -36.725  -36.248 1.00 55.09  ? 103 VAL   B CA    1 
ATOM   5720 C C     . VAL   B 2 111 ? -40.230 -36.114  -36.162 1.00 56.08  ? 103 VAL   B C     1 
ATOM   5721 O O     . VAL   B 2 111 ? -41.221 -36.804  -36.398 1.00 54.58  ? 103 VAL   B O     1 
ATOM   5722 C CB    . VAL   B 2 111 ? -38.360 -36.945  -37.697 1.00 54.27  ? 103 VAL   B CB    1 
ATOM   5723 C CG1   . VAL   B 2 111 ? -38.596 -35.725  -38.579 1.00 54.81  ? 103 VAL   B CG1   1 
ATOM   5724 C CG2   . VAL   B 2 111 ? -36.895 -37.365  -37.743 1.00 53.81  ? 103 VAL   B CG2   1 
ATOM   5725 N N     . GLU   B 2 112 ? -40.292 -34.830  -35.784 1.00 59.11  ? 104 GLU   B N     1 
ATOM   5726 C CA    . GLU   B 2 112 ? -41.552 -34.153  -35.521 1.00 62.08  ? 104 GLU   B CA    1 
ATOM   5727 C C     . GLU   B 2 112 ? -41.653 -32.880  -36.355 1.00 61.35  ? 104 GLU   B C     1 
ATOM   5728 O O     . GLU   B 2 112 ? -40.654 -32.196  -36.567 1.00 57.68  ? 104 GLU   B O     1 
ATOM   5729 C CB    . GLU   B 2 112 ? -41.681 -33.774  -34.045 1.00 65.04  ? 104 GLU   B CB    1 
ATOM   5730 C CG    . GLU   B 2 112 ? -42.260 -34.885  -33.175 1.00 67.95  ? 104 GLU   B CG    1 
ATOM   5731 C CD    . GLU   B 2 112 ? -42.376 -34.518  -31.707 1.00 70.90  ? 104 GLU   B CD    1 
ATOM   5732 O OE1   . GLU   B 2 112 ? -43.521 -34.435  -31.212 1.00 72.69  ? 104 GLU   B OE1   1 
ATOM   5733 O OE2   . GLU   B 2 112 ? -41.322 -34.317  -31.062 1.00 71.15  ? 104 GLU   B OE2   1 
ATOM   5734 N N     . LEU   B 2 113 ? -42.880 -32.571  -36.798 1.00 62.99  ? 105 LEU   B N     1 
ATOM   5735 C CA    . LEU   B 2 113 ? -43.174 -31.310  -37.459 1.00 65.22  ? 105 LEU   B CA    1 
ATOM   5736 C C     . LEU   B 2 113 ? -44.208 -30.548  -36.633 1.00 67.60  ? 105 LEU   B C     1 
ATOM   5737 O O     . LEU   B 2 113 ? -45.333 -31.013  -36.461 1.00 67.70  ? 105 LEU   B O     1 
ATOM   5738 C CB    . LEU   B 2 113 ? -43.662 -31.550  -38.887 1.00 64.97  ? 105 LEU   B CB    1 
ATOM   5739 C CG    . LEU   B 2 113 ? -43.923 -30.301  -39.738 1.00 63.77  ? 105 LEU   B CG    1 
ATOM   5740 C CD1   . LEU   B 2 113 ? -42.682 -29.439  -39.907 1.00 62.69  ? 105 LEU   B CD1   1 
ATOM   5741 C CD2   . LEU   B 2 113 ? -44.470 -30.698  -41.098 1.00 63.63  ? 105 LEU   B CD2   1 
ATOM   5742 N N     . TRP   B 2 114 ? -43.792 -29.386  -36.114 1.00 70.89  ? 106 TRP   B N     1 
ATOM   5743 C CA    . TRP   B 2 114 ? -44.673 -28.460  -35.422 1.00 73.68  ? 106 TRP   B CA    1 
ATOM   5744 C C     . TRP   B 2 114 ? -44.921 -27.256  -36.327 1.00 75.67  ? 106 TRP   B C     1 
ATOM   5745 O O     . TRP   B 2 114 ? -44.022 -26.844  -37.057 1.00 75.40  ? 106 TRP   B O     1 
ATOM   5746 C CB    . TRP   B 2 114 ? -44.048 -28.021  -34.089 1.00 74.70  ? 106 TRP   B CB    1 
ATOM   5747 C CG    . TRP   B 2 114 ? -43.713 -29.154  -33.154 1.00 75.98  ? 106 TRP   B CG    1 
ATOM   5748 C CD1   . TRP   B 2 114 ? -42.705 -30.062  -33.296 1.00 75.96  ? 106 TRP   B CD1   1 
ATOM   5749 C CD2   . TRP   B 2 114 ? -44.374 -29.482  -31.912 1.00 77.25  ? 106 TRP   B CD2   1 
ATOM   5750 N NE1   . TRP   B 2 114 ? -42.703 -30.941  -32.247 1.00 76.58  ? 106 TRP   B NE1   1 
ATOM   5751 C CE2   . TRP   B 2 114 ? -43.710 -30.610  -31.380 1.00 77.46  ? 106 TRP   B CE2   1 
ATOM   5752 C CE3   . TRP   B 2 114 ? -45.454 -28.942  -31.204 1.00 78.06  ? 106 TRP   B CE3   1 
ATOM   5753 C CZ2   . TRP   B 2 114 ? -44.093 -31.201  -30.177 1.00 77.75  ? 106 TRP   B CZ2   1 
ATOM   5754 C CZ3   . TRP   B 2 114 ? -45.831 -29.528  -30.014 1.00 78.64  ? 106 TRP   B CZ3   1 
ATOM   5755 C CH2   . TRP   B 2 114 ? -45.158 -30.641  -29.509 1.00 77.95  ? 106 TRP   B CH2   1 
ATOM   5756 N N     . GLU   B 2 115 ? -46.139 -26.699  -36.274 1.00 78.17  ? 107 GLU   B N     1 
ATOM   5757 C CA    . GLU   B 2 115 ? -46.490 -25.533  -37.072 1.00 78.32  ? 107 GLU   B CA    1 
ATOM   5758 C C     . GLU   B 2 115 ? -46.907 -24.383  -36.161 1.00 78.41  ? 107 GLU   B C     1 
ATOM   5759 O O     . GLU   B 2 115 ? -47.446 -24.604  -35.078 1.00 79.82  ? 107 GLU   B O     1 
ATOM   5760 C CB    . GLU   B 2 115 ? -47.630 -25.837  -38.044 1.00 78.64  ? 107 GLU   B CB    1 
ATOM   5761 C CG    . GLU   B 2 115 ? -47.190 -26.580  -39.302 1.00 79.89  ? 107 GLU   B CG    1 
ATOM   5762 C CD    . GLU   B 2 115 ? -46.440 -25.740  -40.320 1.00 81.62  ? 107 GLU   B CD    1 
ATOM   5763 O OE1   . GLU   B 2 115 ? -46.319 -24.514  -40.116 1.00 83.43  ? 107 GLU   B OE1   1 
ATOM   5764 O OE2   . GLU   B 2 115 ? -45.970 -26.318  -41.322 1.00 82.12  ? 107 GLU   B OE2   1 
ATOM   5765 N N     . LEU   B 2 116 ? -46.649 -23.156  -36.630 1.00 78.06  ? 108 LEU   B N     1 
ATOM   5766 C CA    . LEU   B 2 116 ? -47.126 -21.947  -35.978 1.00 77.54  ? 108 LEU   B CA    1 
ATOM   5767 C C     . LEU   B 2 116 ? -48.604 -21.754  -36.308 1.00 79.04  ? 108 LEU   B C     1 
ATOM   5768 O O     . LEU   B 2 116 ? -48.984 -21.756  -37.477 1.00 79.54  ? 108 LEU   B O     1 
ATOM   5769 C CB    . LEU   B 2 116 ? -46.293 -20.747  -36.427 1.00 75.91  ? 108 LEU   B CB    1 
ATOM   5770 C CG    . LEU   B 2 116 ? -44.961 -20.538  -35.701 1.00 73.61  ? 108 LEU   B CG    1 
ATOM   5771 C CD1   . LEU   B 2 116 ? -44.081 -19.545  -36.439 1.00 72.04  ? 108 LEU   B CD1   1 
ATOM   5772 C CD2   . LEU   B 2 116 ? -45.207 -20.069  -34.277 1.00 73.96  ? 108 LEU   B CD2   1 
ATOM   5773 N N     . ASP   B 2 117 ? -49.423 -21.580  -35.262 1.00 81.09  ? 109 ASP   B N     1 
ATOM   5774 C CA    . ASP   B 2 117 ? -50.867 -21.481  -35.403 1.00 81.50  ? 109 ASP   B CA    1 
ATOM   5775 C C     . ASP   B 2 117 ? -51.397 -20.384  -34.484 1.00 81.96  ? 109 ASP   B C     1 
ATOM   5776 O O     . ASP   B 2 117 ? -50.649 -19.818  -33.688 1.00 79.30  ? 109 ASP   B O     1 
ATOM   5777 C CB    . ASP   B 2 117 ? -51.543 -22.811  -35.105 1.00 81.17  ? 109 ASP   B CB    1 
ATOM   5778 C CG    . ASP   B 2 117 ? -51.157 -23.963  -36.021 1.00 80.66  ? 109 ASP   B CG    1 
ATOM   5779 O OD1   . ASP   B 2 117 ? -51.359 -23.831  -37.245 1.00 80.77  ? 109 ASP   B OD1   1 
ATOM   5780 O OD2   . ASP   B 2 117 ? -50.657 -24.982  -35.502 1.00 81.75  ? 109 ASP   B OD2   1 
ATOM   5781 N N     . GLU   B 2 118 ? -52.697 -20.092  -34.625 1.00 84.44  ? 110 GLU   B N     1 
ATOM   5782 C CA    . GLU   B 2 118 ? -53.397 -19.143  -33.774 1.00 87.24  ? 110 GLU   B CA    1 
ATOM   5783 C C     . GLU   B 2 118 ? -52.742 -17.768  -33.902 1.00 87.21  ? 110 GLU   B C     1 
ATOM   5784 O O     . GLU   B 2 118 ? -52.555 -17.070  -32.907 1.00 90.95  ? 110 GLU   B O     1 
ATOM   5785 C CB    . GLU   B 2 118 ? -53.402 -19.668  -32.336 1.00 90.21  ? 110 GLU   B CB    1 
ATOM   5786 C CG    . GLU   B 2 118 ? -54.512 -19.082  -31.467 1.00 91.89  ? 110 GLU   B CG    1 
ATOM   5787 C CD    . GLU   B 2 118 ? -55.876 -19.698  -31.722 1.00 94.36  ? 110 GLU   B CD    1 
ATOM   5788 O OE1   . GLU   B 2 118 ? -56.762 -18.987  -32.241 1.00 96.29  ? 110 GLU   B OE1   1 
ATOM   5789 O OE2   . GLU   B 2 118 ? -56.052 -20.892  -31.395 1.00 95.53  ? 110 GLU   B OE2   1 
ATOM   5790 N N     . ASN   B 2 119 ? -52.405 -17.391  -35.142 1.00 84.32  ? 111 ASN   B N     1 
ATOM   5791 C CA    . ASN   B 2 119 ? -51.674 -16.165  -35.423 1.00 82.75  ? 111 ASN   B CA    1 
ATOM   5792 C C     . ASN   B 2 119 ? -50.303 -16.234  -34.751 1.00 79.59  ? 111 ASN   B C     1 
ATOM   5793 O O     . ASN   B 2 119 ? -49.853 -15.263  -34.145 1.00 77.22  ? 111 ASN   B O     1 
ATOM   5794 C CB    . ASN   B 2 119 ? -52.475 -14.934  -35.009 1.00 84.75  ? 111 ASN   B CB    1 
ATOM   5795 C CG    . ASN   B 2 119 ? -52.073 -13.696  -35.776 1.00 85.95  ? 111 ASN   B CG    1 
ATOM   5796 O OD1   . ASN   B 2 119 ? -50.906 -13.290  -35.741 1.00 86.92  ? 111 ASN   B OD1   1 
ATOM   5797 N ND2   . ASN   B 2 119 ? -53.018 -13.082  -36.474 1.00 86.10  ? 111 ASN   B ND2   1 
ATOM   5798 N N     . GLU   B 2 120 ? -49.657 -17.403  -34.861 1.00 77.60  ? 112 GLU   B N     1 
ATOM   5799 C CA    . GLU   B 2 120 ? -48.305 -17.616  -34.367 1.00 74.82  ? 112 GLU   B CA    1 
ATOM   5800 C C     . GLU   B 2 120 ? -48.219 -17.321  -32.870 1.00 72.84  ? 112 GLU   B C     1 
ATOM   5801 O O     . GLU   B 2 120 ? -47.291 -16.650  -32.421 1.00 71.90  ? 112 GLU   B O     1 
ATOM   5802 C CB    . GLU   B 2 120 ? -47.317 -16.744  -35.141 1.00 73.83  ? 112 GLU   B CB    1 
ATOM   5803 C CG    . GLU   B 2 120 ? -47.452 -16.869  -36.655 1.00 72.23  ? 112 GLU   B CG    1 
ATOM   5804 C CD    . GLU   B 2 120 ? -46.359 -16.150  -37.423 1.00 71.94  ? 112 GLU   B CD    1 
ATOM   5805 O OE1   . GLU   B 2 120 ? -45.616 -15.362  -36.796 1.00 70.29  ? 112 GLU   B OE1   1 
ATOM   5806 O OE2   . GLU   B 2 120 ? -46.239 -16.394  -38.644 1.00 70.11  ? 112 GLU   B OE2   1 
ATOM   5807 N N     . THR   B 2 121 ? -49.199 -17.825  -32.110 1.00 71.38  ? 113 THR   B N     1 
ATOM   5808 C CA    . THR   B 2 121 ? -49.164 -17.760  -30.656 1.00 70.96  ? 113 THR   B CA    1 
ATOM   5809 C C     . THR   B 2 121 ? -49.078 -19.177  -30.093 1.00 69.84  ? 113 THR   B C     1 
ATOM   5810 O O     . THR   B 2 121 ? -48.404 -19.403  -29.090 1.00 69.30  ? 113 THR   B O     1 
ATOM   5811 C CB    . THR   B 2 121 ? -50.380 -16.994  -30.135 1.00 70.43  ? 113 THR   B CB    1 
ATOM   5812 O OG1   . THR   B 2 121 ? -51.524 -17.742  -30.534 1.00 71.26  ? 113 THR   B OG1   1 
ATOM   5813 C CG2   . THR   B 2 121 ? -50.455 -15.580  -30.682 1.00 69.10  ? 113 THR   B CG2   1 
ATOM   5814 N N     . LEU   B 2 122 ? -49.769 -20.123  -30.743 1.00 69.73  ? 114 LEU   B N     1 
ATOM   5815 C CA    . LEU   B 2 122 ? -49.621 -21.538  -30.441 1.00 70.45  ? 114 LEU   B CA    1 
ATOM   5816 C C     . LEU   B 2 122 ? -48.507 -22.131  -31.305 1.00 69.85  ? 114 LEU   B C     1 
ATOM   5817 O O     . LEU   B 2 122 ? -48.122 -21.556  -32.322 1.00 69.91  ? 114 LEU   B O     1 
ATOM   5818 C CB    . LEU   B 2 122 ? -50.941 -22.276  -30.666 1.00 69.75  ? 114 LEU   B CB    1 
ATOM   5819 C CG    . LEU   B 2 122 ? -52.097 -21.933  -29.719 1.00 68.53  ? 114 LEU   B CG    1 
ATOM   5820 C CD1   . LEU   B 2 122 ? -53.328 -22.736  -30.102 1.00 68.69  ? 114 LEU   B CD1   1 
ATOM   5821 C CD2   . LEU   B 2 122 ? -51.752 -22.175  -28.258 1.00 67.73  ? 114 LEU   B CD2   1 
ATOM   5822 N N     . ILE   B 2 123 ? -47.988 -23.281  -30.855 1.00 68.64  ? 115 ILE   B N     1 
ATOM   5823 C CA    . ILE   B 2 123 ? -47.101 -24.130  -31.636 1.00 66.27  ? 115 ILE   B CA    1 
ATOM   5824 C C     . ILE   B 2 123 ? -47.614 -25.560  -31.484 1.00 65.71  ? 115 ILE   B C     1 
ATOM   5825 O O     . ILE   B 2 123 ? -47.686 -26.070  -30.368 1.00 63.45  ? 115 ILE   B O     1 
ATOM   5826 C CB    . ILE   B 2 123 ? -45.634 -23.989  -31.181 1.00 64.69  ? 115 ILE   B CB    1 
ATOM   5827 C CG1   . ILE   B 2 123 ? -45.171 -22.527  -31.196 1.00 63.59  ? 115 ILE   B CG1   1 
ATOM   5828 C CG2   . ILE   B 2 123 ? -44.717 -24.887  -32.015 1.00 64.58  ? 115 ILE   B CG2   1 
ATOM   5829 C CD1   . ILE   B 2 123 ? -43.738 -22.309  -30.743 1.00 63.05  ? 115 ILE   B CD1   1 
ATOM   5830 N N     . VAL   B 2 124 ? -47.978 -26.192  -32.606 1.00 66.93  ? 116 VAL   B N     1 
ATOM   5831 C CA    . VAL   B 2 124 ? -48.785 -27.401  -32.570 1.00 69.35  ? 116 VAL   B CA    1 
ATOM   5832 C C     . VAL   B 2 124 ? -48.103 -28.501  -33.380 1.00 71.00  ? 116 VAL   B C     1 
ATOM   5833 O O     . VAL   B 2 124 ? -47.709 -28.283  -34.524 1.00 70.72  ? 116 VAL   B O     1 
ATOM   5834 C CB    . VAL   B 2 124 ? -50.206 -27.122  -33.098 1.00 68.90  ? 116 VAL   B CB    1 
ATOM   5835 C CG1   . VAL   B 2 124 ? -51.120 -28.332  -32.944 1.00 68.63  ? 116 VAL   B CG1   1 
ATOM   5836 C CG2   . VAL   B 2 124 ? -50.831 -25.901  -32.432 1.00 68.36  ? 116 VAL   B CG2   1 
ATOM   5837 N N     . SER   B 2 125 ? -47.991 -29.686  -32.767 1.00 70.70  ? 117 SER   B N     1 
ATOM   5838 C CA    . SER   B 2 125 ? -47.512 -30.876  -33.448 1.00 70.78  ? 117 SER   B CA    1 
ATOM   5839 C C     . SER   B 2 125 ? -48.393 -31.151  -34.663 1.00 71.55  ? 117 SER   B C     1 
ATOM   5840 O O     . SER   B 2 125 ? -49.616 -31.108  -34.557 1.00 72.81  ? 117 SER   B O     1 
ATOM   5841 C CB    . SER   B 2 125 ? -47.494 -32.063  -32.514 1.00 70.12  ? 117 SER   B CB    1 
ATOM   5842 O OG    . SER   B 2 125 ? -46.948 -33.211  -33.149 1.00 70.20  ? 117 SER   B OG    1 
ATOM   5843 N N     . LYS   B 2 126 ? -47.763 -31.406  -35.814 1.00 72.05  ? 118 LYS   B N     1 
ATOM   5844 C CA    . LYS   B 2 126 ? -48.479 -31.840  -37.003 1.00 73.87  ? 118 LYS   B CA    1 
ATOM   5845 C C     . LYS   B 2 126 ? -48.301 -33.347  -37.169 1.00 72.94  ? 118 LYS   B C     1 
ATOM   5846 O O     . LYS   B 2 126 ? -49.263 -34.052  -37.470 1.00 71.44  ? 118 LYS   B O     1 
ATOM   5847 C CB    . LYS   B 2 126 ? -48.039 -31.080  -38.261 1.00 75.30  ? 118 LYS   B CB    1 
ATOM   5848 C CG    . LYS   B 2 126 ? -48.455 -29.612  -38.314 1.00 76.50  ? 118 LYS   B CG    1 
ATOM   5849 C CD    . LYS   B 2 126 ? -49.961 -29.364  -38.266 1.00 77.43  ? 118 LYS   B CD    1 
ATOM   5850 C CE    . LYS   B 2 126 ? -50.309 -27.907  -38.270 1.00 77.98  ? 118 LYS   B CE    1 
ATOM   5851 N NZ    . LYS   B 2 126 ? -51.750 -27.656  -38.204 1.00 77.92  ? 118 LYS   B NZ    1 
ATOM   5852 N N     . PHE   B 2 127 ? -47.066 -33.828  -36.978 1.00 71.99  ? 119 PHE   B N     1 
ATOM   5853 C CA    . PHE   B 2 127 ? -46.815 -35.258  -36.906 1.00 69.58  ? 119 PHE   B CA    1 
ATOM   5854 C C     . PHE   B 2 127 ? -45.622 -35.532  -35.994 1.00 67.10  ? 119 PHE   B C     1 
ATOM   5855 O O     . PHE   B 2 127 ? -44.818 -34.644  -35.713 1.00 65.34  ? 119 PHE   B O     1 
ATOM   5856 C CB    . PHE   B 2 127 ? -46.604 -35.880  -38.291 1.00 69.21  ? 119 PHE   B CB    1 
ATOM   5857 C CG    . PHE   B 2 127 ? -45.367 -35.435  -39.063 1.00 67.72  ? 119 PHE   B CG    1 
ATOM   5858 C CD1   . PHE   B 2 127 ? -44.120 -35.999  -38.809 1.00 66.19  ? 119 PHE   B CD1   1 
ATOM   5859 C CD2   . PHE   B 2 127 ? -45.462 -34.486  -40.075 1.00 67.37  ? 119 PHE   B CD2   1 
ATOM   5860 C CE1   . PHE   B 2 127 ? -43.000 -35.604  -39.527 1.00 65.89  ? 119 PHE   B CE1   1 
ATOM   5861 C CE2   . PHE   B 2 127 ? -44.341 -34.102  -40.796 1.00 66.66  ? 119 PHE   B CE2   1 
ATOM   5862 C CZ    . PHE   B 2 127 ? -43.113 -34.657  -40.518 1.00 66.19  ? 119 PHE   B CZ    1 
ATOM   5863 N N     . CYS   B 2 128 ? -45.546 -36.791  -35.550 1.00 64.94  ? 120 CYS   B N     1 
ATOM   5864 C CA    . CYS   B 2 128 ? -44.482 -37.290  -34.697 1.00 63.35  ? 120 CYS   B CA    1 
ATOM   5865 C C     . CYS   B 2 128 ? -44.244 -38.754  -35.054 1.00 61.81  ? 120 CYS   B C     1 
ATOM   5866 O O     . CYS   B 2 128 ? -45.022 -39.620  -34.660 1.00 60.36  ? 120 CYS   B O     1 
ATOM   5867 C CB    . CYS   B 2 128 ? -44.860 -37.140  -33.227 1.00 63.21  ? 120 CYS   B CB    1 
ATOM   5868 S SG    . CYS   B 2 128 ? -43.587 -37.722  -32.076 1.00 62.47  ? 120 CYS   B SG    1 
ATOM   5869 N N     . LYS   B 2 129 ? -43.179 -39.018  -35.819 1.00 61.85  ? 121 LYS   B N     1 
ATOM   5870 C CA    . LYS   B 2 129 ? -42.985 -40.323  -36.431 1.00 62.60  ? 121 LYS   B CA    1 
ATOM   5871 C C     . LYS   B 2 129 ? -41.716 -40.979  -35.891 1.00 60.92  ? 121 LYS   B C     1 
ATOM   5872 O O     . LYS   B 2 129 ? -40.604 -40.556  -36.206 1.00 60.74  ? 121 LYS   B O     1 
ATOM   5873 C CB    . LYS   B 2 129 ? -42.963 -40.177  -37.957 1.00 64.24  ? 121 LYS   B CB    1 
ATOM   5874 C CG    . LYS   B 2 129 ? -44.262 -39.657  -38.565 1.00 64.40  ? 121 LYS   B CG    1 
ATOM   5875 C CD    . LYS   B 2 129 ? -45.479 -40.531  -38.285 1.00 63.92  ? 121 LYS   B CD    1 
ATOM   5876 C CE    . LYS   B 2 129 ? -46.667 -40.134  -39.097 1.00 63.20  ? 121 LYS   B CE    1 
ATOM   5877 N NZ    . LYS   B 2 129 ? -47.855 -40.917  -38.753 1.00 63.06  ? 121 LYS   B NZ    1 
ATOM   5878 N N     . TYR   B 2 130 ? -41.917 -42.029  -35.084 1.00 58.07  ? 122 TYR   B N     1 
ATOM   5879 C CA    . TYR   B 2 130 ? -40.832 -42.827  -34.540 1.00 56.04  ? 122 TYR   B CA    1 
ATOM   5880 C C     . TYR   B 2 130 ? -40.418 -43.853  -35.591 1.00 54.57  ? 122 TYR   B C     1 
ATOM   5881 O O     . TYR   B 2 130 ? -40.935 -44.969  -35.606 1.00 53.99  ? 122 TYR   B O     1 
ATOM   5882 C CB    . TYR   B 2 130 ? -41.286 -43.485  -33.231 1.00 55.36  ? 122 TYR   B CB    1 
ATOM   5883 C CG    . TYR   B 2 130 ? -41.858 -42.516  -32.205 1.00 55.50  ? 122 TYR   B CG    1 
ATOM   5884 C CD1   . TYR   B 2 130 ? -41.027 -41.814  -31.341 1.00 56.66  ? 122 TYR   B CD1   1 
ATOM   5885 C CD2   . TYR   B 2 130 ? -43.228 -42.304  -32.100 1.00 55.40  ? 122 TYR   B CD2   1 
ATOM   5886 C CE1   . TYR   B 2 130 ? -41.540 -40.923  -30.410 1.00 56.27  ? 122 TYR   B CE1   1 
ATOM   5887 C CE2   . TYR   B 2 130 ? -43.754 -41.421  -31.171 1.00 55.22  ? 122 TYR   B CE2   1 
ATOM   5888 C CZ    . TYR   B 2 130 ? -42.907 -40.726  -30.326 1.00 55.72  ? 122 TYR   B CZ    1 
ATOM   5889 O OH    . TYR   B 2 130 ? -43.418 -39.855  -29.408 1.00 55.61  ? 122 TYR   B OH    1 
ATOM   5890 N N     . GLU   B 2 131 ? -39.505 -43.450  -36.484 1.00 53.88  ? 123 GLU   B N     1 
ATOM   5891 C CA    . GLU   B 2 131 ? -38.998 -44.333  -37.526 1.00 53.89  ? 123 GLU   B CA    1 
ATOM   5892 C C     . GLU   B 2 131 ? -37.509 -44.617  -37.321 1.00 52.44  ? 123 GLU   B C     1 
ATOM   5893 O O     . GLU   B 2 131 ? -37.020 -45.654  -37.763 1.00 50.82  ? 123 GLU   B O     1 
ATOM   5894 C CB    . GLU   B 2 131 ? -39.317 -43.768  -38.912 1.00 55.16  ? 123 GLU   B CB    1 
ATOM   5895 C CG    . GLU   B 2 131 ? -40.788 -43.915  -39.295 1.00 56.12  ? 123 GLU   B CG    1 
ATOM   5896 C CD    . GLU   B 2 131 ? -41.261 -45.353  -39.437 1.00 56.88  ? 123 GLU   B CD    1 
ATOM   5897 O OE1   . GLU   B 2 131 ? -40.827 -46.024  -40.397 1.00 57.10  ? 123 GLU   B OE1   1 
ATOM   5898 O OE2   . GLU   B 2 131 ? -42.051 -45.809  -38.582 1.00 58.13  ? 123 GLU   B OE2   1 
ATOM   5899 N N     . HIS   B 2 132 ? -36.793 -43.698  -36.658 1.00 51.58  ? 124 HIS   B N     1 
ATOM   5900 C CA    . HIS   B 2 132 ? -35.426 -43.946  -36.224 1.00 49.18  ? 124 HIS   B CA    1 
ATOM   5901 C C     . HIS   B 2 132 ? -35.441 -44.850  -34.991 1.00 47.40  ? 124 HIS   B C     1 
ATOM   5902 O O     . HIS   B 2 132 ? -36.354 -44.770  -34.173 1.00 46.82  ? 124 HIS   B O     1 
ATOM   5903 C CB    . HIS   B 2 132 ? -34.694 -42.624  -35.965 1.00 48.06  ? 124 HIS   B CB    1 
ATOM   5904 C CG    . HIS   B 2 132 ? -34.119 -41.985  -37.185 1.00 47.82  ? 124 HIS   B CG    1 
ATOM   5905 N ND1   . HIS   B 2 132 ? -33.160 -42.597  -37.962 1.00 47.69  ? 124 HIS   B ND1   1 
ATOM   5906 C CD2   . HIS   B 2 132 ? -34.313 -40.773  -37.724 1.00 48.13  ? 124 HIS   B CD2   1 
ATOM   5907 C CE1   . HIS   B 2 132 ? -32.815 -41.783  -38.951 1.00 48.13  ? 124 HIS   B CE1   1 
ATOM   5908 N NE2   . HIS   B 2 132 ? -33.506 -40.670  -38.827 1.00 47.71  ? 124 HIS   B NE2   1 
ATOM   5909 N N     . ASP   B 2 133 ? -34.414 -45.702  -34.866 1.00 46.12  ? 125 ASP   B N     1 
ATOM   5910 C CA    . ASP   B 2 133 ? -34.329 -46.671  -33.783 1.00 44.90  ? 125 ASP   B CA    1 
ATOM   5911 C C     . ASP   B 2 133 ? -33.439 -46.158  -32.649 1.00 41.80  ? 125 ASP   B C     1 
ATOM   5912 O O     . ASP   B 2 133 ? -33.251 -46.856  -31.657 1.00 40.76  ? 125 ASP   B O     1 
ATOM   5913 C CB    . ASP   B 2 133 ? -33.880 -48.035  -34.289 1.00 46.29  ? 125 ASP   B CB    1 
ATOM   5914 C CG    . ASP   B 2 133 ? -34.993 -49.031  -34.584 1.00 48.90  ? 125 ASP   B CG    1 
ATOM   5915 O OD1   . ASP   B 2 133 ? -36.172 -48.621  -34.565 1.00 50.60  ? 125 ASP   B OD1   1 
ATOM   5916 O OD2   . ASP   B 2 133 ? -34.672 -50.221  -34.800 1.00 52.59  ? 125 ASP   B OD2   1 
ATOM   5917 N N     . ASP   B 2 134 ? -32.901 -44.942  -32.793 1.00 39.49  ? 126 ASP   B N     1 
ATOM   5918 C CA    . ASP   B 2 134 ? -32.125 -44.304  -31.741 1.00 37.88  ? 126 ASP   B CA    1 
ATOM   5919 C C     . ASP   B 2 134 ? -32.273 -42.792  -31.912 1.00 36.38  ? 126 ASP   B C     1 
ATOM   5920 O O     . ASP   B 2 134 ? -32.989 -42.345  -32.805 1.00 36.10  ? 126 ASP   B O     1 
ATOM   5921 C CB    . ASP   B 2 134 ? -30.691 -44.819  -31.751 1.00 38.73  ? 126 ASP   B CB    1 
ATOM   5922 C CG    . ASP   B 2 134 ? -29.815 -44.468  -30.553 1.00 40.29  ? 126 ASP   B CG    1 
ATOM   5923 O OD1   . ASP   B 2 134 ? -30.320 -43.824  -29.608 1.00 38.92  ? 126 ASP   B OD1   1 
ATOM   5924 O OD2   . ASP   B 2 134 ? -28.620 -44.831  -30.575 1.00 42.07  ? 126 ASP   B OD2   1 
ATOM   5925 N N     . ILE   B 2 135 ? -31.601 -42.017  -31.050 1.00 35.01  ? 127 ILE   B N     1 
ATOM   5926 C CA    . ILE   B 2 135 ? -31.654 -40.562  -31.079 1.00 33.75  ? 127 ILE   B CA    1 
ATOM   5927 C C     . ILE   B 2 135 ? -31.454 -40.066  -32.509 1.00 33.67  ? 127 ILE   B C     1 
ATOM   5928 O O     . ILE   B 2 135 ? -30.608 -40.581  -33.236 1.00 33.89  ? 127 ILE   B O     1 
ATOM   5929 C CB    . ILE   B 2 135 ? -30.603 -39.945  -30.133 1.00 32.85  ? 127 ILE   B CB    1 
ATOM   5930 C CG1   . ILE   B 2 135 ? -30.893 -40.259  -28.661 1.00 32.64  ? 127 ILE   B CG1   1 
ATOM   5931 C CG2   . ILE   B 2 135 ? -30.473 -38.438  -30.364 1.00 32.52  ? 127 ILE   B CG2   1 
ATOM   5932 C CD1   . ILE   B 2 135 ? -29.782 -39.852  -27.707 1.00 32.09  ? 127 ILE   B CD1   1 
ATOM   5933 N N     . VAL   B 2 136 ? -32.233 -39.042  -32.882 1.00 34.01  ? 128 VAL   B N     1 
ATOM   5934 C CA    . VAL   B 2 136 ? -32.066 -38.340  -34.143 1.00 33.97  ? 128 VAL   B CA    1 
ATOM   5935 C C     . VAL   B 2 136 ? -31.123 -37.164  -33.895 1.00 34.07  ? 128 VAL   B C     1 
ATOM   5936 O O     . VAL   B 2 136 ? -31.459 -36.242  -33.156 1.00 33.79  ? 128 VAL   B O     1 
ATOM   5937 C CB    . VAL   B 2 136 ? -33.416 -37.870  -34.720 1.00 34.22  ? 128 VAL   B CB    1 
ATOM   5938 C CG1   . VAL   B 2 136 ? -33.269 -37.327  -36.137 1.00 34.59  ? 128 VAL   B CG1   1 
ATOM   5939 C CG2   . VAL   B 2 136 ? -34.468 -38.974  -34.685 1.00 34.28  ? 128 VAL   B CG2   1 
ATOM   5940 N N     . SER   B 2 137 ? -29.939 -37.217  -34.514 1.00 34.27  ? 129 SER   B N     1 
ATOM   5941 C CA    . SER   B 2 137 ? -28.871 -36.268  -34.246 1.00 34.64  ? 129 SER   B CA    1 
ATOM   5942 C C     . SER   B 2 137 ? -29.007 -35.020  -35.116 1.00 36.05  ? 129 SER   B C     1 
ATOM   5943 O O     . SER   B 2 137 ? -28.640 -33.930  -34.679 1.00 37.12  ? 129 SER   B O     1 
ATOM   5944 C CB    . SER   B 2 137 ? -27.528 -36.915  -34.446 1.00 34.95  ? 129 SER   B CB    1 
ATOM   5945 O OG    . SER   B 2 137 ? -27.468 -37.561  -35.711 1.00 36.46  ? 129 SER   B OG    1 
ATOM   5946 N N     . THR   B 2 138 ? -29.517 -35.183  -36.346 1.00 36.02  ? 130 THR   B N     1 
ATOM   5947 C CA    . THR   B 2 138 ? -29.493 -34.105  -37.326 1.00 35.69  ? 130 THR   B CA    1 
ATOM   5948 C C     . THR   B 2 138 ? -30.684 -34.208  -38.280 1.00 35.70  ? 130 THR   B C     1 
ATOM   5949 O O     . THR   B 2 138 ? -31.125 -35.306  -38.615 1.00 33.96  ? 130 THR   B O     1 
ATOM   5950 C CB    . THR   B 2 138 ? -28.155 -34.150  -38.066 1.00 34.62  ? 130 THR   B CB    1 
ATOM   5951 O OG1   . THR   B 2 138 ? -28.234 -33.160  -39.086 1.00 33.68  ? 130 THR   B OG1   1 
ATOM   5952 C CG2   . THR   B 2 138 ? -27.859 -35.513  -38.667 1.00 34.58  ? 130 THR   B CG2   1 
ATOM   5953 N N     . VAL   B 2 139 ? -31.198 -33.035  -38.686 1.00 37.07  ? 131 VAL   B N     1 
ATOM   5954 C CA    . VAL   B 2 139 ? -32.163 -32.906  -39.771 1.00 37.19  ? 131 VAL   B CA    1 
ATOM   5955 C C     . VAL   B 2 139 ? -31.721 -31.755  -40.672 1.00 36.97  ? 131 VAL   B C     1 
ATOM   5956 O O     . VAL   B 2 139 ? -30.929 -30.908  -40.262 1.00 35.90  ? 131 VAL   B O     1 
ATOM   5957 C CB    . VAL   B 2 139 ? -33.620 -32.671  -39.321 1.00 38.06  ? 131 VAL   B CB    1 
ATOM   5958 C CG1   . VAL   B 2 139 ? -34.222 -33.894  -38.641 1.00 38.84  ? 131 VAL   B CG1   1 
ATOM   5959 C CG2   . VAL   B 2 139 ? -33.752 -31.435  -38.439 1.00 38.82  ? 131 VAL   B CG2   1 
ATOM   5960 N N     . SER   B 2 140 ? -32.281 -31.731  -41.889 1.00 36.85  ? 132 SER   B N     1 
ATOM   5961 C CA    . SER   B 2 140 ? -31.984 -30.713  -42.883 1.00 37.00  ? 132 SER   B CA    1 
ATOM   5962 C C     . SER   B 2 140 ? -33.088 -30.692  -43.940 1.00 38.12  ? 132 SER   B C     1 
ATOM   5963 O O     . SER   B 2 140 ? -33.463 -31.744  -44.455 1.00 37.42  ? 132 SER   B O     1 
ATOM   5964 C CB    . SER   B 2 140 ? -30.634 -30.963  -43.503 1.00 36.30  ? 132 SER   B CB    1 
ATOM   5965 O OG    . SER   B 2 140 ? -30.331 -29.988  -44.490 1.00 34.99  ? 132 SER   B OG    1 
ATOM   5966 N N     . VAL   B 2 141 ? -33.599 -29.491  -44.256 1.00 39.13  ? 133 VAL   B N     1 
ATOM   5967 C CA    . VAL   B 2 141 ? -34.680 -29.335  -45.220 1.00 41.06  ? 133 VAL   B CA    1 
ATOM   5968 C C     . VAL   B 2 141 ? -34.075 -29.259  -46.619 1.00 40.67  ? 133 VAL   B C     1 
ATOM   5969 O O     . VAL   B 2 141 ? -33.047 -28.615  -46.815 1.00 39.70  ? 133 VAL   B O     1 
ATOM   5970 C CB    . VAL   B 2 141 ? -35.570 -28.100  -44.982 1.00 42.76  ? 133 VAL   B CB    1 
ATOM   5971 C CG1   . VAL   B 2 141 ? -36.859 -28.175  -45.794 1.00 43.27  ? 133 VAL   B CG1   1 
ATOM   5972 C CG2   . VAL   B 2 141 ? -35.888 -27.889  -43.509 1.00 44.11  ? 133 VAL   B CG2   1 
ATOM   5973 N N     . LEU   B 2 142 ? -34.758 -29.881  -47.589 1.00 41.40  ? 134 LEU   B N     1 
ATOM   5974 C CA    . LEU   B 2 142 ? -34.292 -29.918  -48.966 1.00 42.61  ? 134 LEU   B CA    1 
ATOM   5975 C C     . LEU   B 2 142 ? -34.803 -28.693  -49.726 1.00 43.84  ? 134 LEU   B C     1 
ATOM   5976 O O     . LEU   B 2 142 ? -35.708 -28.003  -49.259 1.00 44.13  ? 134 LEU   B O     1 
ATOM   5977 C CB    . LEU   B 2 142 ? -34.720 -31.239  -49.604 1.00 42.11  ? 134 LEU   B CB    1 
ATOM   5978 C CG    . LEU   B 2 142 ? -34.012 -32.486  -49.061 1.00 41.79  ? 134 LEU   B CG    1 
ATOM   5979 C CD1   . LEU   B 2 142 ? -34.661 -33.771  -49.543 1.00 41.73  ? 134 LEU   B CD1   1 
ATOM   5980 C CD2   . LEU   B 2 142 ? -32.535 -32.482  -49.430 1.00 41.39  ? 134 LEU   B CD2   1 
ATOM   5981 N N     A SER   B 2 143 ? -34.218 -28.455  -50.908 0.50 45.21  ? 135 SER   B N     1 
ATOM   5982 N N     B SER   B 2 143 ? -34.203 -28.446  -50.898 0.50 45.16  ? 135 SER   B N     1 
ATOM   5983 C CA    A SER   B 2 143 ? -34.403 -27.223  -51.664 0.50 45.40  ? 135 SER   B CA    1 
ATOM   5984 C CA    B SER   B 2 143 ? -34.409 -27.230  -51.672 0.50 45.30  ? 135 SER   B CA    1 
ATOM   5985 C C     A SER   B 2 143 ? -35.881 -26.858  -51.796 0.50 45.55  ? 135 SER   B C     1 
ATOM   5986 C C     B SER   B 2 143 ? -35.888 -26.866  -51.768 0.50 45.48  ? 135 SER   B C     1 
ATOM   5987 O O     A SER   B 2 143 ? -36.255 -25.713  -51.550 0.50 45.19  ? 135 SER   B O     1 
ATOM   5988 O O     B SER   B 2 143 ? -36.267 -25.734  -51.472 0.50 45.01  ? 135 SER   B O     1 
ATOM   5989 C CB    A SER   B 2 143 ? -33.750 -27.325  -53.020 0.50 45.43  ? 135 SER   B CB    1 
ATOM   5990 C CB    B SER   B 2 143 ? -33.806 -27.364  -53.043 0.50 45.29  ? 135 SER   B CB    1 
ATOM   5991 O OG    A SER   B 2 143 ? -34.287 -28.412  -53.761 0.50 45.36  ? 135 SER   B OG    1 
ATOM   5992 O OG    B SER   B 2 143 ? -32.390 -27.397  -52.961 0.50 45.12  ? 135 SER   B OG    1 
ATOM   5993 N N     . SER   B 2 144 ? -36.707 -27.835  -52.191 1.00 45.73  ? 136 SER   B N     1 
ATOM   5994 C CA    . SER   B 2 144 ? -38.134 -27.628  -52.388 1.00 46.74  ? 136 SER   B CA    1 
ATOM   5995 C C     . SER   B 2 144 ? -38.784 -27.155  -51.091 1.00 48.43  ? 136 SER   B C     1 
ATOM   5996 O O     . SER   B 2 144 ? -39.394 -26.088  -51.055 1.00 49.78  ? 136 SER   B O     1 
ATOM   5997 C CB    . SER   B 2 144 ? -38.809 -28.883  -52.887 1.00 46.57  ? 136 SER   B CB    1 
ATOM   5998 O OG    . SER   B 2 144 ? -38.798 -29.900  -51.894 1.00 45.54  ? 136 SER   B OG    1 
ATOM   5999 N N     . GLY   B 2 145 ? -38.625 -27.961  -50.035 1.00 48.98  ? 137 GLY   B N     1 
ATOM   6000 C CA    . GLY   B 2 145 ? -39.226 -27.682  -48.743 1.00 48.93  ? 137 GLY   B CA    1 
ATOM   6001 C C     . GLY   B 2 145 ? -40.470 -28.534  -48.501 1.00 50.19  ? 137 GLY   B C     1 
ATOM   6002 O O     . GLY   B 2 145 ? -41.209 -28.282  -47.552 1.00 49.90  ? 137 GLY   B O     1 
ATOM   6003 N N     . THR   B 2 146 ? -40.698 -29.526  -49.373 1.00 51.90  ? 138 THR   B N     1 
ATOM   6004 C CA    . THR   B 2 146 ? -41.705 -30.552  -49.141 1.00 53.90  ? 138 THR   B CA    1 
ATOM   6005 C C     . THR   B 2 146 ? -41.032 -31.808  -48.589 1.00 54.47  ? 138 THR   B C     1 
ATOM   6006 O O     . THR   B 2 146 ? -41.715 -32.776  -48.253 1.00 54.07  ? 138 THR   B O     1 
ATOM   6007 C CB    . THR   B 2 146 ? -42.483 -30.846  -50.426 1.00 54.58  ? 138 THR   B CB    1 
ATOM   6008 O OG1   . THR   B 2 146 ? -43.348 -31.941  -50.131 1.00 54.90  ? 138 THR   B OG1   1 
ATOM   6009 C CG2   . THR   B 2 146 ? -41.598 -31.225  -51.600 1.00 54.10  ? 138 THR   B CG2   1 
ATOM   6010 N N     . GLN   B 2 147 ? -39.693 -31.777  -48.496 1.00 54.15  ? 139 GLN   B N     1 
ATOM   6011 C CA    . GLN   B 2 147 ? -38.912 -32.947  -48.129 1.00 52.60  ? 139 GLN   B CA    1 
ATOM   6012 C C     . GLN   B 2 147 ? -37.757 -32.550  -47.213 1.00 50.74  ? 139 GLN   B C     1 
ATOM   6013 O O     . GLN   B 2 147 ? -37.297 -31.409  -47.232 1.00 48.59  ? 139 GLN   B O     1 
ATOM   6014 C CB    . GLN   B 2 147 ? -38.349 -33.639  -49.371 1.00 52.19  ? 139 GLN   B CB    1 
ATOM   6015 C CG    . GLN   B 2 147 ? -39.397 -34.309  -50.253 1.00 51.38  ? 139 GLN   B CG    1 
ATOM   6016 C CD    . GLN   B 2 147 ? -38.801 -34.935  -51.495 1.00 51.24  ? 139 GLN   B CD    1 
ATOM   6017 O OE1   . GLN   B 2 147 ? -38.027 -34.307  -52.223 1.00 48.81  ? 139 GLN   B OE1   1 
ATOM   6018 N NE2   . GLN   B 2 147 ? -39.147 -36.188  -51.748 1.00 51.20  ? 139 GLN   B NE2   1 
ATOM   6019 N N     . ALA   B 2 148 ? -37.293 -33.529  -46.426 1.00 50.14  ? 140 ALA   B N     1 
ATOM   6020 C CA    . ALA   B 2 148 ? -36.174 -33.349  -45.516 1.00 48.55  ? 140 ALA   B CA    1 
ATOM   6021 C C     . ALA   B 2 148 ? -35.466 -34.684  -45.297 1.00 47.38  ? 140 ALA   B C     1 
ATOM   6022 O O     . ALA   B 2 148 ? -36.024 -35.745  -45.582 1.00 46.73  ? 140 ALA   B O     1 
ATOM   6023 C CB    . ALA   B 2 148 ? -36.660 -32.762  -44.209 1.00 48.27  ? 140 ALA   B CB    1 
ATOM   6024 N N     . VAL   B 2 149 ? -34.232 -34.606  -44.782 1.00 46.06  ? 141 VAL   B N     1 
ATOM   6025 C CA    . VAL   B 2 149 ? -33.418 -35.780  -44.510 1.00 44.93  ? 141 VAL   B CA    1 
ATOM   6026 C C     . VAL   B 2 149 ? -32.917 -35.716  -43.067 1.00 41.72  ? 141 VAL   B C     1 
ATOM   6027 O O     . VAL   B 2 149 ? -32.461 -34.669  -42.608 1.00 39.56  ? 141 VAL   B O     1 
ATOM   6028 C CB    . VAL   B 2 149 ? -32.255 -35.903  -45.517 1.00 46.19  ? 141 VAL   B CB    1 
ATOM   6029 C CG1   . VAL   B 2 149 ? -31.371 -34.660  -45.545 1.00 47.13  ? 141 VAL   B CG1   1 
ATOM   6030 C CG2   . VAL   B 2 149 ? -31.411 -37.149  -45.273 1.00 46.57  ? 141 VAL   B CG2   1 
ATOM   6031 N N     . SER   B 2 150 ? -33.007 -36.854  -42.365 1.00 39.98  ? 142 SER   B N     1 
ATOM   6032 C CA    . SER   B 2 150 ? -32.563 -36.966  -40.984 1.00 37.97  ? 142 SER   B CA    1 
ATOM   6033 C C     . SER   B 2 150 ? -31.362 -37.904  -40.890 1.00 37.62  ? 142 SER   B C     1 
ATOM   6034 O O     . SER   B 2 150 ? -31.211 -38.810  -41.708 1.00 36.98  ? 142 SER   B O     1 
ATOM   6035 C CB    . SER   B 2 150 ? -33.686 -37.431  -40.088 1.00 37.01  ? 142 SER   B CB    1 
ATOM   6036 O OG    . SER   B 2 150 ? -34.244 -38.657  -40.542 1.00 36.28  ? 142 SER   B OG    1 
ATOM   6037 N N     . GLY   B 2 151 ? -30.513 -37.659  -39.883 1.00 38.22  ? 143 GLY   B N     1 
ATOM   6038 C CA    . GLY   B 2 151 ? -29.428 -38.555  -39.514 1.00 38.29  ? 143 GLY   B CA    1 
ATOM   6039 C C     . GLY   B 2 151 ? -29.503 -38.892  -38.027 1.00 38.94  ? 143 GLY   B C     1 
ATOM   6040 O O     . GLY   B 2 151 ? -29.806 -38.021  -37.214 1.00 38.99  ? 143 GLY   B O     1 
ATOM   6041 N N     . SER   B 2 152 ? -29.221 -40.157  -37.684 1.00 39.17  ? 144 SER   B N     1 
ATOM   6042 C CA    . SER   B 2 152 ? -29.462 -40.673  -36.344 1.00 38.54  ? 144 SER   B CA    1 
ATOM   6043 C C     . SER   B 2 152 ? -28.263 -41.470  -35.832 1.00 37.86  ? 144 SER   B C     1 
ATOM   6044 O O     . SER   B 2 152 ? -27.366 -41.827  -36.594 1.00 37.20  ? 144 SER   B O     1 
ATOM   6045 C CB    . SER   B 2 152 ? -30.717 -41.509  -36.320 1.00 38.09  ? 144 SER   B CB    1 
ATOM   6046 O OG    . SER   B 2 152 ? -30.829 -42.256  -35.116 1.00 36.46  ? 144 SER   B OG    1 
ATOM   6047 N N     . LYS   B 2 153 ? -28.282 -41.745  -34.521 1.00 36.94  ? 145 LYS   B N     1 
ATOM   6048 C CA    . LYS   B 2 153 ? -27.274 -42.564  -33.864 1.00 35.41  ? 145 LYS   B CA    1 
ATOM   6049 C C     . LYS   B 2 153 ? -27.459 -44.030  -34.240 1.00 33.87  ? 145 LYS   B C     1 
ATOM   6050 O O     . LYS   B 2 153 ? -26.537 -44.822  -34.080 1.00 32.68  ? 145 LYS   B O     1 
ATOM   6051 C CB    . LYS   B 2 153 ? -27.335 -42.408  -32.340 1.00 35.30  ? 145 LYS   B CB    1 
ATOM   6052 C CG    . LYS   B 2 153 ? -26.833 -41.068  -31.826 1.00 35.45  ? 145 LYS   B CG    1 
ATOM   6053 C CD    . LYS   B 2 153 ? -26.789 -40.950  -30.308 1.00 35.62  ? 145 LYS   B CD    1 
ATOM   6054 C CE    . LYS   B 2 153 ? -26.408 -39.577  -29.856 1.00 35.48  ? 145 LYS   B CE    1 
ATOM   6055 N NZ    . LYS   B 2 153 ? -25.101 -39.158  -30.367 1.00 35.62  ? 145 LYS   B NZ    1 
ATOM   6056 N N     . ASP   B 2 154 ? -28.646 -44.374  -34.760 1.00 34.54  ? 146 ASP   B N     1 
ATOM   6057 C CA    . ASP   B 2 154 ? -28.924 -45.706  -35.277 1.00 34.84  ? 146 ASP   B CA    1 
ATOM   6058 C C     . ASP   B 2 154 ? -28.203 -45.969  -36.602 1.00 34.90  ? 146 ASP   B C     1 
ATOM   6059 O O     . ASP   B 2 154 ? -28.388 -47.036  -37.183 1.00 34.19  ? 146 ASP   B O     1 
ATOM   6060 C CB    . ASP   B 2 154 ? -30.419 -45.935  -35.441 1.00 35.30  ? 146 ASP   B CB    1 
ATOM   6061 C CG    . ASP   B 2 154 ? -31.084 -45.162  -36.572 1.00 36.00  ? 146 ASP   B CG    1 
ATOM   6062 O OD1   . ASP   B 2 154 ? -30.400 -44.321  -37.195 1.00 36.34  ? 146 ASP   B OD1   1 
ATOM   6063 O OD2   . ASP   B 2 154 ? -32.279 -45.417  -36.829 1.00 36.41  ? 146 ASP   B OD2   1 
ATOM   6064 N N     A ILE   B 2 155 ? -27.439 -44.975  -37.083 0.50 35.96  ? 147 ILE   B N     1 
ATOM   6065 N N     B ILE   B 2 155 ? -27.419 -44.991  -37.081 0.50 35.88  ? 147 ILE   B N     1 
ATOM   6066 C CA    A ILE   B 2 155 ? -26.485 -45.129  -38.174 0.50 36.77  ? 147 ILE   B CA    1 
ATOM   6067 C CA    B ILE   B 2 155 ? -26.483 -45.169  -38.186 0.50 36.64  ? 147 ILE   B CA    1 
ATOM   6068 C C     A ILE   B 2 155 ? -27.179 -44.953  -39.527 0.50 37.35  ? 147 ILE   B C     1 
ATOM   6069 C C     B ILE   B 2 155 ? -27.173 -44.905  -39.527 0.50 37.23  ? 147 ILE   B C     1 
ATOM   6070 O O     A ILE   B 2 155 ? -26.514 -44.973  -40.561 0.50 36.67  ? 147 ILE   B O     1 
ATOM   6071 O O     B ILE   B 2 155 ? -26.498 -44.813  -40.551 0.50 36.43  ? 147 ILE   B O     1 
ATOM   6072 C CB    A ILE   B 2 155 ? -25.726 -46.470  -38.083 0.50 36.67  ? 147 ILE   B CB    1 
ATOM   6073 C CB    B ILE   B 2 155 ? -25.812 -46.559  -38.152 0.50 36.45  ? 147 ILE   B CB    1 
ATOM   6074 C CG1   A ILE   B 2 155 ? -24.995 -46.615  -36.742 0.50 36.31  ? 147 ILE   B CG1   1 
ATOM   6075 C CG1   B ILE   B 2 155 ? -25.048 -46.792  -36.843 0.50 36.11  ? 147 ILE   B CG1   1 
ATOM   6076 C CG2   A ILE   B 2 155 ? -24.775 -46.645  -39.268 0.50 36.81  ? 147 ILE   B CG2   1 
ATOM   6077 C CG2   B ILE   B 2 155 ? -24.911 -46.760  -39.371 0.50 36.59  ? 147 ILE   B CG2   1 
ATOM   6078 C CD1   A ILE   B 2 155 ? -24.206 -47.903  -36.599 0.50 35.94  ? 147 ILE   B CD1   1 
ATOM   6079 C CD1   B ILE   B 2 155 ? -24.487 -48.194  -36.692 0.50 35.66  ? 147 ILE   B CD1   1 
ATOM   6080 N N     . CYS   B 2 156 ? -28.504 -44.752  -39.518 1.00 37.81  ? 148 CYS   B N     1 
ATOM   6081 C CA    . CYS   B 2 156 ? -29.278 -44.626  -40.746 1.00 38.52  ? 148 CYS   B CA    1 
ATOM   6082 C C     . CYS   B 2 156 ? -29.495 -43.164  -41.130 1.00 39.06  ? 148 CYS   B C     1 
ATOM   6083 O O     . CYS   B 2 156 ? -29.404 -42.266  -40.295 1.00 39.62  ? 148 CYS   B O     1 
ATOM   6084 C CB    . CYS   B 2 156 ? -30.626 -45.323  -40.616 1.00 39.29  ? 148 CYS   B CB    1 
ATOM   6085 S SG    . CYS   B 2 156 ? -30.476 -47.121  -40.454 1.00 41.30  ? 148 CYS   B SG    1 
ATOM   6086 N N     . ILE   B 2 157 ? -29.774 -42.959  -42.425 1.00 39.84  ? 149 ILE   B N     1 
ATOM   6087 C CA    . ILE   B 2 157 ? -30.210 -41.685  -42.974 1.00 39.77  ? 149 ILE   B CA    1 
ATOM   6088 C C     . ILE   B 2 157 ? -31.542 -41.920  -43.683 1.00 41.18  ? 149 ILE   B C     1 
ATOM   6089 O O     . ILE   B 2 157 ? -31.678 -42.880  -44.440 1.00 40.02  ? 149 ILE   B O     1 
ATOM   6090 C CB    . ILE   B 2 157 ? -29.149 -41.098  -43.925 1.00 38.61  ? 149 ILE   B CB    1 
ATOM   6091 C CG1   . ILE   B 2 157 ? -27.855 -40.757  -43.180 1.00 38.60  ? 149 ILE   B CG1   1 
ATOM   6092 C CG2   . ILE   B 2 157 ? -29.701 -39.889  -44.683 1.00 38.38  ? 149 ILE   B CG2   1 
ATOM   6093 C CD1   . ILE   B 2 157 ? -26.730 -40.251  -44.068 1.00 38.47  ? 149 ILE   B CD1   1 
ATOM   6094 N N     . LYS   B 2 158 ? -32.515 -41.035  -43.434 1.00 43.02  ? 150 LYS   B N     1 
ATOM   6095 C CA    . LYS   B 2 158 ? -33.864 -41.205  -43.951 1.00 43.96  ? 150 LYS   B CA    1 
ATOM   6096 C C     . LYS   B 2 158 ? -34.306 -39.943  -44.684 1.00 44.46  ? 150 LYS   B C     1 
ATOM   6097 O O     . LYS   B 2 158 ? -33.972 -38.837  -44.272 1.00 41.95  ? 150 LYS   B O     1 
ATOM   6098 C CB    . LYS   B 2 158 ? -34.824 -41.533  -42.803 1.00 44.75  ? 150 LYS   B CB    1 
ATOM   6099 C CG    . LYS   B 2 158 ? -34.685 -42.944  -42.259 1.00 45.18  ? 150 LYS   B CG    1 
ATOM   6100 C CD    . LYS   B 2 158 ? -35.387 -43.162  -40.926 1.00 45.28  ? 150 LYS   B CD    1 
ATOM   6101 C CE    . LYS   B 2 158 ? -35.100 -44.513  -40.357 1.00 46.00  ? 150 LYS   B CE    1 
ATOM   6102 N NZ    . LYS   B 2 158 ? -35.750 -45.576  -41.127 1.00 46.29  ? 150 LYS   B NZ    1 
ATOM   6103 N N     . VAL   B 2 159 ? -35.065 -40.139  -45.770 1.00 47.51  ? 151 VAL   B N     1 
ATOM   6104 C CA    . VAL   B 2 159 ? -35.620 -39.052  -46.560 1.00 48.83  ? 151 VAL   B CA    1 
ATOM   6105 C C     . VAL   B 2 159 ? -37.129 -39.019  -46.327 1.00 50.07  ? 151 VAL   B C     1 
ATOM   6106 O O     . VAL   B 2 159 ? -37.795 -40.050  -46.429 1.00 48.69  ? 151 VAL   B O     1 
ATOM   6107 C CB    . VAL   B 2 159 ? -35.285 -39.224  -48.055 1.00 49.80  ? 151 VAL   B CB    1 
ATOM   6108 C CG1   . VAL   B 2 159 ? -35.866 -38.099  -48.902 1.00 50.09  ? 151 VAL   B CG1   1 
ATOM   6109 C CG2   . VAL   B 2 159 ? -33.783 -39.346  -48.289 1.00 49.75  ? 151 VAL   B CG2   1 
ATOM   6110 N N     . TRP   B 2 160 ? -37.652 -37.822  -46.030 1.00 51.24  ? 152 TRP   B N     1 
ATOM   6111 C CA    . TRP   B 2 160 ? -39.037 -37.648  -45.621 1.00 52.88  ? 152 TRP   B CA    1 
ATOM   6112 C C     . TRP   B 2 160 ? -39.807 -36.847  -46.669 1.00 53.93  ? 152 TRP   B C     1 
ATOM   6113 O O     . TRP   B 2 160 ? -39.247 -35.954  -47.300 1.00 52.39  ? 152 TRP   B O     1 
ATOM   6114 C CB    . TRP   B 2 160 ? -39.091 -36.927  -44.266 1.00 53.57  ? 152 TRP   B CB    1 
ATOM   6115 C CG    . TRP   B 2 160 ? -38.420 -37.662  -43.136 1.00 53.78  ? 152 TRP   B CG    1 
ATOM   6116 C CD1   . TRP   B 2 160 ? -37.086 -37.704  -42.854 1.00 53.69  ? 152 TRP   B CD1   1 
ATOM   6117 C CD2   . TRP   B 2 160 ? -39.071 -38.441  -42.110 1.00 54.47  ? 152 TRP   B CD2   1 
ATOM   6118 N NE1   . TRP   B 2 160 ? -36.858 -38.468  -41.740 1.00 54.22  ? 152 TRP   B NE1   1 
ATOM   6119 C CE2   . TRP   B 2 160 ? -38.055 -38.930  -41.259 1.00 54.59  ? 152 TRP   B CE2   1 
ATOM   6120 C CE3   . TRP   B 2 160 ? -40.402 -38.775  -41.832 1.00 55.20  ? 152 TRP   B CE3   1 
ATOM   6121 C CZ2   . TRP   B 2 160 ? -38.334 -39.731  -40.154 1.00 55.71  ? 152 TRP   B CZ2   1 
ATOM   6122 C CZ3   . TRP   B 2 160 ? -40.677 -39.564  -40.736 1.00 55.63  ? 152 TRP   B CZ3   1 
ATOM   6123 C CH2   . TRP   B 2 160 ? -39.655 -40.034  -39.910 1.00 55.92  ? 152 TRP   B CH2   1 
ATOM   6124 N N     . ASP   B 2 161 ? -41.092 -37.185  -46.844 1.00 55.22  ? 153 ASP   B N     1 
ATOM   6125 C CA    . ASP   B 2 161 ? -42.054 -36.268  -47.434 1.00 57.95  ? 153 ASP   B CA    1 
ATOM   6126 C C     . ASP   B 2 161 ? -42.867 -35.650  -46.301 1.00 56.77  ? 153 ASP   B C     1 
ATOM   6127 O O     . ASP   B 2 161 ? -43.554 -36.361  -45.569 1.00 55.72  ? 153 ASP   B O     1 
ATOM   6128 C CB    . ASP   B 2 161 ? -42.954 -36.936  -48.463 1.00 61.53  ? 153 ASP   B CB    1 
ATOM   6129 C CG    . ASP   B 2 161 ? -43.817 -35.975  -49.272 1.00 63.97  ? 153 ASP   B CG    1 
ATOM   6130 O OD1   . ASP   B 2 161 ? -43.238 -35.124  -49.982 1.00 66.38  ? 153 ASP   B OD1   1 
ATOM   6131 O OD2   . ASP   B 2 161 ? -45.059 -36.068  -49.177 1.00 63.59  ? 153 ASP   B OD2   1 
ATOM   6132 N N     . LEU   B 2 162 ? -42.776 -34.322  -46.169 1.00 55.81  ? 154 LEU   B N     1 
ATOM   6133 C CA    . LEU   B 2 162 ? -43.340 -33.612  -45.033 1.00 57.20  ? 154 LEU   B CA    1 
ATOM   6134 C C     . LEU   B 2 162 ? -44.863 -33.566  -45.150 1.00 60.07  ? 154 LEU   B C     1 
ATOM   6135 O O     . LEU   B 2 162 ? -45.568 -33.723  -44.154 1.00 64.39  ? 154 LEU   B O     1 
ATOM   6136 C CB    . LEU   B 2 162 ? -42.744 -32.207  -44.959 1.00 56.05  ? 154 LEU   B CB    1 
ATOM   6137 C CG    . LEU   B 2 162 ? -41.214 -32.119  -44.955 1.00 55.59  ? 154 LEU   B CG    1 
ATOM   6138 C CD1   . LEU   B 2 162 ? -40.762 -30.687  -45.172 1.00 55.81  ? 154 LEU   B CD1   1 
ATOM   6139 C CD2   . LEU   B 2 162 ? -40.626 -32.676  -43.671 1.00 55.24  ? 154 LEU   B CD2   1 
ATOM   6140 N N     . ALA   B 2 163 ? -45.358 -33.339  -46.372 1.00 60.68  ? 155 ALA   B N     1 
ATOM   6141 C CA    . ALA   B 2 163 ? -46.788 -33.274  -46.628 1.00 59.75  ? 155 ALA   B CA    1 
ATOM   6142 C C     . ALA   B 2 163 ? -47.432 -34.639  -46.392 1.00 60.41  ? 155 ALA   B C     1 
ATOM   6143 O O     . ALA   B 2 163 ? -48.480 -34.722  -45.754 1.00 59.68  ? 155 ALA   B O     1 
ATOM   6144 C CB    . ALA   B 2 163 ? -47.036 -32.775  -48.033 1.00 58.92  ? 155 ALA   B CB    1 
ATOM   6145 N N     . GLN   B 2 164 ? -46.802 -35.701  -46.914 1.00 62.09  ? 156 GLN   B N     1 
ATOM   6146 C CA    . GLN   B 2 164 ? -47.281 -37.062  -46.718 1.00 63.00  ? 156 GLN   B CA    1 
ATOM   6147 C C     . GLN   B 2 164 ? -47.064 -37.531  -45.281 1.00 62.73  ? 156 GLN   B C     1 
ATOM   6148 O O     . GLN   B 2 164 ? -47.871 -38.307  -44.776 1.00 63.32  ? 156 GLN   B O     1 
ATOM   6149 C CB    . GLN   B 2 164 ? -46.607 -38.090  -47.627 1.00 63.69  ? 156 GLN   B CB    1 
ATOM   6150 C CG    . GLN   B 2 164 ? -47.458 -38.510  -48.820 1.00 64.56  ? 156 GLN   B CG    1 
ATOM   6151 C CD    . GLN   B 2 164 ? -46.659 -39.226  -49.888 1.00 65.96  ? 156 GLN   B CD    1 
ATOM   6152 O OE1   . GLN   B 2 164 ? -45.636 -38.724  -50.369 1.00 68.30  ? 156 GLN   B OE1   1 
ATOM   6153 N NE2   . GLN   B 2 164 ? -47.116 -40.410  -50.271 1.00 65.92  ? 156 GLN   B NE2   1 
ATOM   6154 N N     A GLN   B 2 165 ? -45.978 -37.068  -44.646 0.50 61.82  ? 157 GLN   B N     1 
ATOM   6155 N N     B GLN   B 2 165 ? -45.970 -37.064  -44.663 0.50 62.01  ? 157 GLN   B N     1 
ATOM   6156 C CA    A GLN   B 2 165 ? -45.607 -37.496  -43.306 0.50 61.62  ? 157 GLN   B CA    1 
ATOM   6157 C CA    B GLN   B 2 165 ? -45.563 -37.467  -43.326 0.50 61.95  ? 157 GLN   B CA    1 
ATOM   6158 C C     A GLN   B 2 165 ? -45.148 -38.953  -43.335 0.50 61.94  ? 157 GLN   B C     1 
ATOM   6159 C C     B GLN   B 2 165 ? -45.176 -38.946  -43.353 0.50 62.11  ? 157 GLN   B C     1 
ATOM   6160 O O     A GLN   B 2 165 ? -45.415 -39.701  -42.396 0.50 61.99  ? 157 GLN   B O     1 
ATOM   6161 O O     B GLN   B 2 165 ? -45.517 -39.696  -42.439 0.50 62.02  ? 157 GLN   B O     1 
ATOM   6162 C CB    A GLN   B 2 165 ? -46.755 -37.377  -42.301 0.50 60.58  ? 157 GLN   B CB    1 
ATOM   6163 C CB    B GLN   B 2 165 ? -46.648 -37.139  -42.296 0.50 61.20  ? 157 GLN   B CB    1 
ATOM   6164 C CG    A GLN   B 2 165 ? -47.461 -36.026  -42.305 0.50 59.44  ? 157 GLN   B CG    1 
ATOM   6165 C CG    B GLN   B 2 165 ? -47.566 -38.304  -41.939 0.50 60.39  ? 157 GLN   B CG    1 
ATOM   6166 C CD    A GLN   B 2 165 ? -48.543 -35.932  -41.253 0.50 58.50  ? 157 GLN   B CD    1 
ATOM   6167 C CD    B GLN   B 2 165 ? -48.762 -37.882  -41.115 0.50 59.54  ? 157 GLN   B CD    1 
ATOM   6168 O OE1   A GLN   B 2 165 ? -49.027 -36.945  -40.736 0.50 59.07  ? 157 GLN   B OE1   1 
ATOM   6169 O OE1   B GLN   B 2 165 ? -48.931 -36.705  -40.780 0.50 59.81  ? 157 GLN   B OE1   1 
ATOM   6170 N NE2   A GLN   B 2 165 ? -48.939 -34.710  -40.929 0.50 57.81  ? 157 GLN   B NE2   1 
ATOM   6171 N NE2   B GLN   B 2 165 ? -49.613 -38.844  -40.788 0.50 58.58  ? 157 GLN   B NE2   1 
ATOM   6172 N N     . VAL   B 2 166 ? -44.465 -39.345  -44.420 1.00 61.77  ? 158 VAL   B N     1 
ATOM   6173 C CA    . VAL   B 2 166 ? -43.991 -40.711  -44.594 1.00 60.97  ? 158 VAL   B CA    1 
ATOM   6174 C C     . VAL   B 2 166 ? -42.519 -40.656  -45.001 1.00 59.47  ? 158 VAL   B C     1 
ATOM   6175 O O     . VAL   B 2 166 ? -42.100 -39.734  -45.699 1.00 59.06  ? 158 VAL   B O     1 
ATOM   6176 C CB    . VAL   B 2 166 ? -44.831 -41.505  -45.619 1.00 61.96  ? 158 VAL   B CB    1 
ATOM   6177 C CG1   . VAL   B 2 166 ? -46.327 -41.403  -45.335 1.00 62.43  ? 158 VAL   B CG1   1 
ATOM   6178 C CG2   . VAL   B 2 166 ? -44.537 -41.097  -47.061 1.00 62.13  ? 158 VAL   B CG2   1 
ATOM   6179 N N     . VAL   B 2 167 ? -41.741 -41.645  -44.539 1.00 58.96  ? 159 VAL   B N     1 
ATOM   6180 C CA    . VAL   B 2 167 ? -40.359 -41.815  -44.966 1.00 58.88  ? 159 VAL   B CA    1 
ATOM   6181 C C     . VAL   B 2 167 ? -40.371 -42.448  -46.355 1.00 57.61  ? 159 VAL   B C     1 
ATOM   6182 O O     . VAL   B 2 167 ? -41.103 -43.407  -46.595 1.00 55.56  ? 159 VAL   B O     1 
ATOM   6183 C CB    . VAL   B 2 167 ? -39.509 -42.666  -43.998 1.00 58.98  ? 159 VAL   B CB    1 
ATOM   6184 C CG1   . VAL   B 2 167 ? -38.046 -42.723  -44.428 1.00 58.61  ? 159 VAL   B CG1   1 
ATOM   6185 C CG2   . VAL   B 2 167 ? -39.605 -42.180  -42.557 1.00 59.23  ? 159 VAL   B CG2   1 
ATOM   6186 N N     . LEU   B 2 168 ? -39.537 -41.912  -47.254 1.00 57.77  ? 160 LEU   B N     1 
ATOM   6187 C CA    . LEU   B 2 168 ? -39.464 -42.379  -48.630 1.00 58.37  ? 160 LEU   B CA    1 
ATOM   6188 C C     . LEU   B 2 168 ? -38.352 -43.412  -48.772 1.00 57.00  ? 160 LEU   B C     1 
ATOM   6189 O O     . LEU   B 2 168 ? -38.556 -44.469  -49.369 1.00 56.15  ? 160 LEU   B O     1 
ATOM   6190 C CB    . LEU   B 2 168 ? -39.221 -41.188  -49.556 1.00 59.16  ? 160 LEU   B CB    1 
ATOM   6191 C CG    . LEU   B 2 168 ? -40.344 -40.149  -49.625 1.00 59.18  ? 160 LEU   B CG    1 
ATOM   6192 C CD1   . LEU   B 2 168 ? -39.899 -38.962  -50.450 1.00 58.90  ? 160 LEU   B CD1   1 
ATOM   6193 C CD2   . LEU   B 2 168 ? -41.623 -40.742  -50.193 1.00 59.07  ? 160 LEU   B CD2   1 
ATOM   6194 N N     . SER   B 2 169 ? -37.175 -43.075  -48.233 1.00 55.61  ? 161 SER   B N     1 
ATOM   6195 C CA    . SER   B 2 169 ? -35.984 -43.893  -48.373 1.00 53.93  ? 161 SER   B CA    1 
ATOM   6196 C C     . SER   B 2 169 ? -35.343 -44.101  -47.005 1.00 52.98  ? 161 SER   B C     1 
ATOM   6197 O O     . SER   B 2 169 ? -35.388 -43.211  -46.157 1.00 51.23  ? 161 SER   B O     1 
ATOM   6198 C CB    . SER   B 2 169 ? -35.013 -43.252  -49.326 1.00 53.31  ? 161 SER   B CB    1 
ATOM   6199 O OG    . SER   B 2 169 ? -35.694 -42.672  -50.429 1.00 53.85  ? 161 SER   B OG    1 
ATOM   6200 N N     . SER   B 2 170 ? -34.744 -45.282  -46.813 1.00 52.28  ? 162 SER   B N     1 
ATOM   6201 C CA    . SER   B 2 170 ? -33.934 -45.562  -45.639 1.00 50.33  ? 162 SER   B CA    1 
ATOM   6202 C C     . SER   B 2 170 ? -32.564 -46.072  -46.083 1.00 48.44  ? 162 SER   B C     1 
ATOM   6203 O O     . SER   B 2 170 ? -32.475 -47.041  -46.834 1.00 47.87  ? 162 SER   B O     1 
ATOM   6204 C CB    . SER   B 2 170 ? -34.619 -46.536  -44.722 1.00 49.34  ? 162 SER   B CB    1 
ATOM   6205 O OG    . SER   B 2 170 ? -33.984 -46.546  -43.452 1.00 49.30  ? 162 SER   B OG    1 
ATOM   6206 N N     . TYR   B 2 171 ? -31.506 -45.409  -45.599 1.00 47.04  ? 163 TYR   B N     1 
ATOM   6207 C CA    . TYR   B 2 171 ? -30.155 -45.616  -46.095 1.00 46.14  ? 163 TYR   B CA    1 
ATOM   6208 C C     . TYR   B 2 171 ? -29.213 -45.965  -44.944 1.00 45.47  ? 163 TYR   B C     1 
ATOM   6209 O O     . TYR   B 2 171 ? -28.852 -45.095  -44.151 1.00 44.70  ? 163 TYR   B O     1 
ATOM   6210 C CB    . TYR   B 2 171 ? -29.692 -44.335  -46.796 1.00 46.54  ? 163 TYR   B CB    1 
ATOM   6211 C CG    . TYR   B 2 171 ? -30.416 -43.965  -48.085 1.00 47.17  ? 163 TYR   B CG    1 
ATOM   6212 C CD1   . TYR   B 2 171 ? -30.692 -44.915  -49.064 1.00 47.56  ? 163 TYR   B CD1   1 
ATOM   6213 C CD2   . TYR   B 2 171 ? -30.809 -42.653  -48.331 1.00 47.34  ? 163 TYR   B CD2   1 
ATOM   6214 C CE1   . TYR   B 2 171 ? -31.339 -44.574  -50.241 1.00 47.74  ? 163 TYR   B CE1   1 
ATOM   6215 C CE2   . TYR   B 2 171 ? -31.459 -42.299  -49.502 1.00 47.67  ? 163 TYR   B CE2   1 
ATOM   6216 C CZ    . TYR   B 2 171 ? -31.725 -43.262  -50.461 1.00 48.28  ? 163 TYR   B CZ    1 
ATOM   6217 O OH    . TYR   B 2 171 ? -32.368 -42.915  -51.613 1.00 47.80  ? 163 TYR   B OH    1 
ATOM   6218 N N     . ARG   B 2 172 ? -28.810 -47.241  -44.868 1.00 44.48  ? 164 ARG   B N     1 
ATOM   6219 C CA    . ARG   B 2 172 ? -27.731 -47.653  -43.983 1.00 43.80  ? 164 ARG   B CA    1 
ATOM   6220 C C     . ARG   B 2 172 ? -26.431 -47.672  -44.783 1.00 41.05  ? 164 ARG   B C     1 
ATOM   6221 O O     . ARG   B 2 172 ? -25.933 -48.732  -45.154 1.00 40.01  ? 164 ARG   B O     1 
ATOM   6222 C CB    . ARG   B 2 172 ? -27.982 -49.011  -43.315 1.00 45.32  ? 164 ARG   B CB    1 
ATOM   6223 C CG    . ARG   B 2 172 ? -26.972 -49.314  -42.215 1.00 47.11  ? 164 ARG   B CG    1 
ATOM   6224 C CD    . ARG   B 2 172 ? -27.118 -50.714  -41.645 1.00 48.88  ? 164 ARG   B CD    1 
ATOM   6225 N NE    . ARG   B 2 172 ? -28.400 -50.879  -40.952 1.00 50.76  ? 164 ARG   B NE    1 
ATOM   6226 C CZ    . ARG   B 2 172 ? -28.737 -50.316  -39.793 1.00 52.89  ? 164 ARG   B CZ    1 
ATOM   6227 N NH1   . ARG   B 2 172 ? -27.845 -49.643  -39.082 1.00 54.78  ? 164 ARG   B NH1   1 
ATOM   6228 N NH2   . ARG   B 2 172 ? -29.970 -50.453  -39.334 1.00 52.53  ? 164 ARG   B NH2   1 
ATOM   6229 N N     . ALA   B 2 173 ? -25.895 -46.477  -45.044 1.00 40.20  ? 165 ALA   B N     1 
ATOM   6230 C CA    . ALA   B 2 173 ? -24.672 -46.321  -45.813 1.00 39.87  ? 165 ALA   B CA    1 
ATOM   6231 C C     . ALA   B 2 173 ? -23.464 -46.283  -44.881 1.00 38.27  ? 165 ALA   B C     1 
ATOM   6232 O O     . ALA   B 2 173 ? -22.409 -46.817  -45.215 1.00 38.66  ? 165 ALA   B O     1 
ATOM   6233 C CB    . ALA   B 2 173 ? -24.754 -45.066  -46.652 1.00 40.57  ? 165 ALA   B CB    1 
ATOM   6234 N N     . HIS   B 2 174 ? -23.630 -45.635  -43.721 1.00 36.71  ? 166 HIS   B N     1 
ATOM   6235 C CA    . HIS   B 2 174 ? -22.549 -45.472  -42.764 1.00 35.67  ? 166 HIS   B CA    1 
ATOM   6236 C C     . HIS   B 2 174 ? -22.405 -46.721  -41.896 1.00 35.67  ? 166 HIS   B C     1 
ATOM   6237 O O     . HIS   B 2 174 ? -23.254 -47.612  -41.925 1.00 35.11  ? 166 HIS   B O     1 
ATOM   6238 C CB    . HIS   B 2 174 ? -22.774 -44.230  -41.897 1.00 34.86  ? 166 HIS   B CB    1 
ATOM   6239 C CG    . HIS   B 2 174 ? -22.541 -42.939  -42.602 1.00 33.58  ? 166 HIS   B CG    1 
ATOM   6240 N ND1   . HIS   B 2 174 ? -21.276 -42.474  -42.888 1.00 32.99  ? 166 HIS   B ND1   1 
ATOM   6241 C CD2   . HIS   B 2 174 ? -23.390 -42.019  -43.070 1.00 33.28  ? 166 HIS   B CD2   1 
ATOM   6242 C CE1   . HIS   B 2 174 ? -21.370 -41.302  -43.497 1.00 32.94  ? 166 HIS   B CE1   1 
ATOM   6243 N NE2   . HIS   B 2 174 ? -22.646 -41.007  -43.620 1.00 33.27  ? 166 HIS   B NE2   1 
ATOM   6244 N N     . ALA   B 2 175 ? -21.308 -46.756  -41.127 1.00 35.37  ? 167 ALA   B N     1 
ATOM   6245 C CA    . ALA   B 2 175 ? -20.976 -47.870  -40.254 1.00 35.02  ? 167 ALA   B CA    1 
ATOM   6246 C C     . ALA   B 2 175 ? -20.902 -47.413  -38.795 1.00 35.40  ? 167 ALA   B C     1 
ATOM   6247 O O     . ALA   B 2 175 ? -20.482 -48.176  -37.927 1.00 33.37  ? 167 ALA   B O     1 
ATOM   6248 C CB    . ALA   B 2 175 ? -19.667 -48.478  -40.708 1.00 35.00  ? 167 ALA   B CB    1 
ATOM   6249 N N     . ALA   B 2 176 ? -21.327 -46.169  -38.537 1.00 36.12  ? 168 ALA   B N     1 
ATOM   6250 C CA    . ALA   B 2 176 ? -21.279 -45.574  -37.211 1.00 36.70  ? 168 ALA   B CA    1 
ATOM   6251 C C     . ALA   B 2 176 ? -22.291 -44.432  -37.140 1.00 38.06  ? 168 ALA   B C     1 
ATOM   6252 O O     . ALA   B 2 176 ? -22.971 -44.143  -38.124 1.00 39.02  ? 168 ALA   B O     1 
ATOM   6253 C CB    . ALA   B 2 176 ? -19.874 -45.098  -36.910 1.00 36.17  ? 168 ALA   B CB    1 
ATOM   6254 N N     . GLN   B 2 177 ? -22.386 -43.789  -35.970 1.00 37.77  ? 169 GLN   B N     1 
ATOM   6255 C CA    . GLN   B 2 177 ? -23.372 -42.745  -35.740 1.00 37.64  ? 169 GLN   B CA    1 
ATOM   6256 C C     . GLN   B 2 177 ? -23.263 -41.689  -36.836 1.00 37.15  ? 169 GLN   B C     1 
ATOM   6257 O O     . GLN   B 2 177 ? -22.162 -41.267  -37.182 1.00 36.16  ? 169 GLN   B O     1 
ATOM   6258 C CB    . GLN   B 2 177 ? -23.190 -42.026  -34.404 1.00 38.02  ? 169 GLN   B CB    1 
ATOM   6259 C CG    . GLN   B 2 177 ? -23.102 -42.951  -33.196 1.00 39.57  ? 169 GLN   B CG    1 
ATOM   6260 C CD    . GLN   B 2 177 ? -23.050 -42.208  -31.878 1.00 40.95  ? 169 GLN   B CD    1 
ATOM   6261 O OE1   . GLN   B 2 177 ? -22.409 -41.158  -31.750 1.00 42.21  ? 169 GLN   B OE1   1 
ATOM   6262 N NE2   . GLN   B 2 177 ? -23.743 -42.741  -30.883 1.00 40.40  ? 169 GLN   B NE2   1 
ATOM   6263 N N     . VAL   B 2 178 ? -24.420 -41.273  -37.364 1.00 37.29  ? 170 VAL   B N     1 
ATOM   6264 C CA    . VAL   B 2 178 ? -24.488 -40.179  -38.319 1.00 37.12  ? 170 VAL   B CA    1 
ATOM   6265 C C     . VAL   B 2 178 ? -24.428 -38.870  -37.535 1.00 37.26  ? 170 VAL   B C     1 
ATOM   6266 O O     . VAL   B 2 178 ? -25.262 -38.627  -36.667 1.00 37.73  ? 170 VAL   B O     1 
ATOM   6267 C CB    . VAL   B 2 178 ? -25.755 -40.272  -39.191 1.00 36.84  ? 170 VAL   B CB    1 
ATOM   6268 C CG1   . VAL   B 2 178 ? -25.893 -39.077  -40.129 1.00 36.98  ? 170 VAL   B CG1   1 
ATOM   6269 C CG2   . VAL   B 2 178 ? -25.800 -41.579  -39.976 1.00 36.23  ? 170 VAL   B CG2   1 
ATOM   6270 N N     . THR   B 2 179 ? -23.428 -38.043  -37.853 1.00 37.25  ? 171 THR   B N     1 
ATOM   6271 C CA    . THR   B 2 179 ? -23.136 -36.834  -37.102 1.00 38.09  ? 171 THR   B CA    1 
ATOM   6272 C C     . THR   B 2 179 ? -23.935 -35.658  -37.660 1.00 38.89  ? 171 THR   B C     1 
ATOM   6273 O O     . THR   B 2 179 ? -24.430 -34.830  -36.898 1.00 38.96  ? 171 THR   B O     1 
ATOM   6274 C CB    . THR   B 2 179 ? -21.633 -36.566  -37.179 1.00 39.18  ? 171 THR   B CB    1 
ATOM   6275 O OG1   . THR   B 2 179 ? -20.990 -37.723  -36.653 1.00 40.21  ? 171 THR   B OG1   1 
ATOM   6276 C CG2   . THR   B 2 179 ? -21.211 -35.350  -36.377 1.00 39.27  ? 171 THR   B CG2   1 
ATOM   6277 N N     . CYS   B 2 180 ? -24.044 -35.590  -38.993 1.00 39.05  ? 172 CYS   B N     1 
ATOM   6278 C CA    . CYS   B 2 180 ? -24.488 -34.386  -39.677 1.00 39.45  ? 172 CYS   B CA    1 
ATOM   6279 C C     . CYS   B 2 180 ? -25.066 -34.753  -41.043 1.00 39.37  ? 172 CYS   B C     1 
ATOM   6280 O O     . CYS   B 2 180 ? -24.508 -35.597  -41.743 1.00 38.48  ? 172 CYS   B O     1 
ATOM   6281 C CB    . CYS   B 2 180 ? -23.312 -33.429  -39.838 1.00 40.23  ? 172 CYS   B CB    1 
ATOM   6282 S SG    . CYS   B 2 180 ? -23.777 -31.739  -40.297 1.00 42.23  ? 172 CYS   B SG    1 
ATOM   6283 N N     . VAL   B 2 181 ? -26.196 -34.130  -41.402 1.00 39.68  ? 173 VAL   B N     1 
ATOM   6284 C CA    . VAL   B 2 181 ? -26.726 -34.202  -42.758 1.00 38.80  ? 173 VAL   B CA    1 
ATOM   6285 C C     . VAL   B 2 181 ? -27.054 -32.779  -43.211 1.00 37.77  ? 173 VAL   B C     1 
ATOM   6286 O O     . VAL   B 2 181 ? -27.693 -32.032  -42.475 1.00 37.02  ? 173 VAL   B O     1 
ATOM   6287 C CB    . VAL   B 2 181 ? -27.945 -35.140  -42.892 1.00 38.48  ? 173 VAL   B CB    1 
ATOM   6288 C CG1   . VAL   B 2 181 ? -27.598 -36.572  -42.503 1.00 38.07  ? 173 VAL   B CG1   1 
ATOM   6289 C CG2   . VAL   B 2 181 ? -29.158 -34.658  -42.103 1.00 38.52  ? 173 VAL   B CG2   1 
ATOM   6290 N N     . ALA   B 2 182 ? -26.605 -32.415  -44.421 1.00 37.91  ? 174 ALA   B N     1 
ATOM   6291 C CA    . ALA   B 2 182 ? -26.706 -31.049  -44.914 1.00 38.21  ? 174 ALA   B CA    1 
ATOM   6292 C C     . ALA   B 2 182 ? -27.223 -31.042  -46.353 1.00 39.73  ? 174 ALA   B C     1 
ATOM   6293 O O     . ALA   B 2 182 ? -26.556 -31.536  -47.260 1.00 39.06  ? 174 ALA   B O     1 
ATOM   6294 C CB    . ALA   B 2 182 ? -25.360 -30.365  -44.809 1.00 37.62  ? 174 ALA   B CB    1 
ATOM   6295 N N     . ALA   B 2 183 ? -28.409 -30.447  -46.545 1.00 40.28  ? 175 ALA   B N     1 
ATOM   6296 C CA    . ALA   B 2 183 ? -29.087 -30.433  -47.830 1.00 40.18  ? 175 ALA   B CA    1 
ATOM   6297 C C     . ALA   B 2 183 ? -28.353 -29.522  -48.810 1.00 40.67  ? 175 ALA   B C     1 
ATOM   6298 O O     . ALA   B 2 183 ? -27.900 -28.443  -48.436 1.00 38.89  ? 175 ALA   B O     1 
ATOM   6299 C CB    . ALA   B 2 183 ? -30.517 -29.979  -47.654 1.00 39.44  ? 175 ALA   B CB    1 
ATOM   6300 N N     . SER   B 2 184 ? -28.258 -29.976  -50.065 1.00 42.93  ? 176 SER   B N     1 
ATOM   6301 C CA    . SER   B 2 184 ? -27.859 -29.119  -51.168 1.00 43.56  ? 176 SER   B CA    1 
ATOM   6302 C C     . SER   B 2 184 ? -28.774 -27.897  -51.197 1.00 42.35  ? 176 SER   B C     1 
ATOM   6303 O O     . SER   B 2 184 ? -29.994 -28.046  -51.116 1.00 41.08  ? 176 SER   B O     1 
ATOM   6304 C CB    . SER   B 2 184 ? -27.902 -29.866  -52.482 1.00 44.21  ? 176 SER   B CB    1 
ATOM   6305 O OG    . SER   B 2 184 ? -27.302 -29.111  -53.525 1.00 45.04  ? 176 SER   B OG    1 
ATOM   6306 N N     . PRO   B 2 185 ? -28.219 -26.663  -51.279 1.00 42.40  ? 177 PRO   B N     1 
ATOM   6307 C CA    . PRO   B 2 185 ? -29.035 -25.445  -51.327 1.00 42.87  ? 177 PRO   B CA    1 
ATOM   6308 C C     . PRO   B 2 185 ? -30.135 -25.464  -52.389 1.00 42.69  ? 177 PRO   B C     1 
ATOM   6309 O O     . PRO   B 2 185 ? -31.294 -25.186  -52.082 1.00 42.67  ? 177 PRO   B O     1 
ATOM   6310 C CB    . PRO   B 2 185 ? -28.019 -24.312  -51.595 1.00 42.48  ? 177 PRO   B CB    1 
ATOM   6311 C CG    . PRO   B 2 185 ? -26.678 -24.872  -51.170 1.00 42.26  ? 177 PRO   B CG    1 
ATOM   6312 C CD    . PRO   B 2 185 ? -26.775 -26.382  -51.305 1.00 42.08  ? 177 PRO   B CD    1 
ATOM   6313 N N     . HIS   B 2 186 ? -29.767 -25.828  -53.626 1.00 41.86  ? 178 HIS   B N     1 
ATOM   6314 C CA    . HIS   B 2 186 ? -30.613 -25.599  -54.790 1.00 41.44  ? 178 HIS   B CA    1 
ATOM   6315 C C     . HIS   B 2 186 ? -31.030 -26.908  -55.465 1.00 41.43  ? 178 HIS   B C     1 
ATOM   6316 O O     . HIS   B 2 186 ? -31.624 -26.872  -56.541 1.00 41.24  ? 178 HIS   B O     1 
ATOM   6317 C CB    . HIS   B 2 186 ? -29.892 -24.652  -55.758 1.00 39.05  ? 178 HIS   B CB    1 
ATOM   6318 C CG    . HIS   B 2 186 ? -29.572 -23.328  -55.140 1.00 37.39  ? 178 HIS   B CG    1 
ATOM   6319 N ND1   . HIS   B 2 186 ? -30.517 -22.583  -54.469 1.00 35.36  ? 178 HIS   B ND1   1 
ATOM   6320 C CD2   . HIS   B 2 186 ? -28.436 -22.615  -55.093 1.00 36.50  ? 178 HIS   B CD2   1 
ATOM   6321 C CE1   . HIS   B 2 186 ? -29.958 -21.464  -54.028 1.00 35.26  ? 178 HIS   B CE1   1 
ATOM   6322 N NE2   . HIS   B 2 186 ? -28.696 -21.461  -54.398 1.00 35.47  ? 178 HIS   B NE2   1 
ATOM   6323 N N     . LYS   B 2 187 ? -30.765 -28.052  -54.819 1.00 42.13  ? 179 LYS   B N     1 
ATOM   6324 C CA    . LYS   B 2 187 ? -31.049 -29.356  -55.400 1.00 42.75  ? 179 LYS   B CA    1 
ATOM   6325 C C     . LYS   B 2 187 ? -31.684 -30.273  -54.356 1.00 43.15  ? 179 LYS   B C     1 
ATOM   6326 O O     . LYS   B 2 187 ? -31.184 -30.380  -53.240 1.00 45.46  ? 179 LYS   B O     1 
ATOM   6327 C CB    . LYS   B 2 187 ? -29.756 -29.956  -55.958 1.00 42.69  ? 179 LYS   B CB    1 
ATOM   6328 C CG    . LYS   B 2 187 ? -29.311 -29.349  -57.276 1.00 43.62  ? 179 LYS   B CG    1 
ATOM   6329 C CD    . LYS   B 2 187 ? -27.840 -29.573  -57.595 1.00 43.57  ? 179 LYS   B CD    1 
ATOM   6330 C CE    . LYS   B 2 187 ? -27.574 -29.515  -59.058 1.00 43.86  ? 179 LYS   B CE    1 
ATOM   6331 N NZ    . LYS   B 2 187 ? -26.147 -29.699  -59.327 1.00 44.95  ? 179 LYS   B NZ    1 
ATOM   6332 N N     A ASP   B 2 188 ? -32.772 -30.941  -54.754 0.50 43.71  ? 180 ASP   B N     1 
ATOM   6333 N N     B ASP   B 2 188 ? -32.774 -30.947  -54.745 0.50 43.54  ? 180 ASP   B N     1 
ATOM   6334 C CA    A ASP   B 2 188 ? -33.581 -31.746  -53.855 0.50 44.39  ? 180 ASP   B CA    1 
ATOM   6335 C CA    B ASP   B 2 188 ? -33.566 -31.753  -53.830 0.50 44.11  ? 180 ASP   B CA    1 
ATOM   6336 C C     A ASP   B 2 188 ? -33.331 -33.235  -54.096 0.50 45.18  ? 180 ASP   B C     1 
ATOM   6337 C C     B ASP   B 2 188 ? -33.235 -33.237  -53.949 0.50 45.13  ? 180 ASP   B C     1 
ATOM   6338 O O     A ASP   B 2 188 ? -34.175 -34.061  -53.756 0.50 46.11  ? 180 ASP   B O     1 
ATOM   6339 O O     B ASP   B 2 188 ? -33.925 -34.066  -53.359 0.50 46.40  ? 180 ASP   B O     1 
ATOM   6340 C CB    A ASP   B 2 188 ? -35.052 -31.393  -54.012 0.50 44.80  ? 180 ASP   B CB    1 
ATOM   6341 C CB    B ASP   B 2 188 ? -35.054 -31.567  -54.071 0.50 44.21  ? 180 ASP   B CB    1 
ATOM   6342 C CG    A ASP   B 2 188 ? -36.036 -32.396  -53.431 0.50 44.95  ? 180 ASP   B CG    1 
ATOM   6343 C CG    B ASP   B 2 188 ? -35.669 -30.385  -53.343 0.50 44.06  ? 180 ASP   B CG    1 
ATOM   6344 O OD1   A ASP   B 2 188 ? -36.042 -32.565  -52.194 0.50 44.98  ? 180 ASP   B OD1   1 
ATOM   6345 O OD1   B ASP   B 2 188 ? -35.250 -29.242  -53.621 0.50 43.93  ? 180 ASP   B OD1   1 
ATOM   6346 O OD2   A ASP   B 2 188 ? -36.788 -33.000  -54.225 0.50 44.92  ? 180 ASP   B OD2   1 
ATOM   6347 O OD2   B ASP   B 2 188 ? -36.541 -30.621  -52.484 0.50 43.88  ? 180 ASP   B OD2   1 
ATOM   6348 N N     . SER   B 2 189 ? -32.184 -33.566  -54.706 1.00 45.08  ? 181 SER   B N     1 
ATOM   6349 C CA    . SER   B 2 189 ? -31.752 -34.948  -54.847 1.00 43.83  ? 181 SER   B CA    1 
ATOM   6350 C C     . SER   B 2 189 ? -30.349 -35.121  -54.270 1.00 42.39  ? 181 SER   B C     1 
ATOM   6351 O O     . SER   B 2 189 ? -29.808 -36.224  -54.307 1.00 42.04  ? 181 SER   B O     1 
ATOM   6352 C CB    . SER   B 2 189 ? -31.814 -35.391  -56.290 1.00 44.19  ? 181 SER   B CB    1 
ATOM   6353 O OG    . SER   B 2 189 ? -30.797 -34.770  -57.064 1.00 44.79  ? 181 SER   B OG    1 
ATOM   6354 N N     . VAL   B 2 190 ? -29.791 -34.041  -53.702 1.00 40.18  ? 182 VAL   B N     1 
ATOM   6355 C CA    . VAL   B 2 190 ? -28.385 -33.991  -53.331 1.00 39.74  ? 182 VAL   B CA    1 
ATOM   6356 C C     . VAL   B 2 190 ? -28.244 -33.457  -51.907 1.00 40.52  ? 182 VAL   B C     1 
ATOM   6357 O O     . VAL   B 2 190 ? -28.980 -32.562  -51.496 1.00 40.80  ? 182 VAL   B O     1 
ATOM   6358 C CB    . VAL   B 2 190 ? -27.605 -33.123  -54.338 1.00 38.84  ? 182 VAL   B CB    1 
ATOM   6359 C CG1   . VAL   B 2 190 ? -26.175 -32.844  -53.887 1.00 38.66  ? 182 VAL   B CG1   1 
ATOM   6360 C CG2   . VAL   B 2 190 ? -27.610 -33.745  -55.728 1.00 38.82  ? 182 VAL   B CG2   1 
ATOM   6361 N N     . PHE   B 2 191 ? -27.270 -34.014  -51.174 1.00 40.32  ? 183 PHE   B N     1 
ATOM   6362 C CA    . PHE   B 2 191 ? -26.935 -33.565  -49.832 1.00 39.84  ? 183 PHE   B CA    1 
ATOM   6363 C C     . PHE   B 2 191 ? -25.640 -34.237  -49.384 1.00 39.04  ? 183 PHE   B C     1 
ATOM   6364 O O     . PHE   B 2 191 ? -25.170 -35.180  -50.019 1.00 39.44  ? 183 PHE   B O     1 
ATOM   6365 C CB    . PHE   B 2 191 ? -28.061 -33.868  -48.838 1.00 39.53  ? 183 PHE   B CB    1 
ATOM   6366 C CG    . PHE   B 2 191 ? -28.469 -35.331  -48.750 1.00 39.03  ? 183 PHE   B CG    1 
ATOM   6367 C CD1   . PHE   B 2 191 ? -29.428 -35.852  -49.611 1.00 39.10  ? 183 PHE   B CD1   1 
ATOM   6368 C CD2   . PHE   B 2 191 ? -27.903 -36.175  -47.800 1.00 39.19  ? 183 PHE   B CD2   1 
ATOM   6369 C CE1   . PHE   B 2 191 ? -29.806 -37.184  -49.527 1.00 39.72  ? 183 PHE   B CE1   1 
ATOM   6370 C CE2   . PHE   B 2 191 ? -28.285 -37.506  -47.717 1.00 39.41  ? 183 PHE   B CE2   1 
ATOM   6371 C CZ    . PHE   B 2 191 ? -29.233 -38.009  -48.582 1.00 39.92  ? 183 PHE   B CZ    1 
ATOM   6372 N N     . LEU   B 2 192 ? -25.080 -33.730  -48.281 1.00 37.27  ? 184 LEU   B N     1 
ATOM   6373 C CA    . LEU   B 2 192 ? -23.911 -34.319  -47.653 1.00 37.50  ? 184 LEU   B CA    1 
ATOM   6374 C C     . LEU   B 2 192 ? -24.331 -35.041  -46.378 1.00 37.67  ? 184 LEU   B C     1 
ATOM   6375 O O     . LEU   B 2 192 ? -25.377 -34.748  -45.803 1.00 38.18  ? 184 LEU   B O     1 
ATOM   6376 C CB    . LEU   B 2 192 ? -22.883 -33.236  -47.339 1.00 38.14  ? 184 LEU   B CB    1 
ATOM   6377 C CG    . LEU   B 2 192 ? -22.162 -32.624  -48.541 1.00 39.35  ? 184 LEU   B CG    1 
ATOM   6378 C CD1   . LEU   B 2 192 ? -21.383 -31.390  -48.127 1.00 39.61  ? 184 LEU   B CD1   1 
ATOM   6379 C CD2   . LEU   B 2 192 ? -21.240 -33.639  -49.195 1.00 40.04  ? 184 LEU   B CD2   1 
ATOM   6380 N N     . SER   B 2 193 ? -23.489 -35.988  -45.955 1.00 36.91  ? 185 SER   B N     1 
ATOM   6381 C CA    . SER   B 2 193 ? -23.574 -36.577  -44.631 1.00 35.64  ? 185 SER   B CA    1 
ATOM   6382 C C     . SER   B 2 193 ? -22.164 -36.897  -44.149 1.00 35.50  ? 185 SER   B C     1 
ATOM   6383 O O     . SER   B 2 193 ? -21.255 -37.063  -44.961 1.00 36.81  ? 185 SER   B O     1 
ATOM   6384 C CB    . SER   B 2 193 ? -24.455 -37.804  -44.614 1.00 34.91  ? 185 SER   B CB    1 
ATOM   6385 O OG    . SER   B 2 193 ? -23.860 -38.881  -45.324 1.00 33.91  ? 185 SER   B OG    1 
ATOM   6386 N N     . CYS   B 2 194 ? -21.990 -36.954  -42.826 1.00 34.21  ? 186 CYS   B N     1 
ATOM   6387 C CA    . CYS   B 2 194 ? -20.734 -37.389  -42.242 1.00 33.25  ? 186 CYS   B CA    1 
ATOM   6388 C C     . CYS   B 2 194 ? -21.030 -38.171  -40.966 1.00 32.11  ? 186 CYS   B C     1 
ATOM   6389 O O     . CYS   B 2 194 ? -22.084 -37.996  -40.359 1.00 31.77  ? 186 CYS   B O     1 
ATOM   6390 C CB    . CYS   B 2 194 ? -19.785 -36.215  -42.032 1.00 33.25  ? 186 CYS   B CB    1 
ATOM   6391 S SG    . CYS   B 2 194 ? -20.357 -35.011  -40.807 1.00 34.39  ? 186 CYS   B SG    1 
ATOM   6392 N N     . SER   B 2 195 ? -20.092 -39.047  -40.595 1.00 31.26  ? 187 SER   B N     1 
ATOM   6393 C CA    . SER   B 2 195 ? -20.318 -40.047  -39.566 1.00 31.28  ? 187 SER   B CA    1 
ATOM   6394 C C     . SER   B 2 195 ? -19.033 -40.284  -38.780 1.00 31.58  ? 187 SER   B C     1 
ATOM   6395 O O     . SER   B 2 195 ? -17.953 -39.877  -39.201 1.00 31.08  ? 187 SER   B O     1 
ATOM   6396 C CB    . SER   B 2 195 ? -20.829 -41.326  -40.185 1.00 30.75  ? 187 SER   B CB    1 
ATOM   6397 O OG    . SER   B 2 195 ? -20.937 -42.385  -39.243 1.00 30.18  ? 187 SER   B OG    1 
ATOM   6398 N N     . GLU   B 2 196 ? -19.170 -40.969  -37.641 1.00 33.07  ? 188 GLU   B N     1 
ATOM   6399 C CA    . GLU   B 2 196 ? -18.025 -41.374  -36.841 1.00 33.26  ? 188 GLU   B CA    1 
ATOM   6400 C C     . GLU   B 2 196 ? -17.262 -42.506  -37.529 1.00 32.70  ? 188 GLU   B C     1 
ATOM   6401 O O     . GLU   B 2 196 ? -16.166 -42.848  -37.097 1.00 33.43  ? 188 GLU   B O     1 
ATOM   6402 C CB    . GLU   B 2 196 ? -18.463 -41.743  -35.425 1.00 33.34  ? 188 GLU   B CB    1 
ATOM   6403 C CG    . GLU   B 2 196 ? -18.616 -40.524  -34.520 1.00 34.22  ? 188 GLU   B CG    1 
ATOM   6404 C CD    . GLU   B 2 196 ? -19.301 -40.807  -33.195 1.00 35.12  ? 188 GLU   B CD    1 
ATOM   6405 O OE1   . GLU   B 2 196 ? -19.752 -41.956  -32.985 1.00 36.29  ? 188 GLU   B OE1   1 
ATOM   6406 O OE2   . GLU   B 2 196 ? -19.379 -39.871  -32.372 1.00 34.65  ? 188 GLU   B OE2   1 
ATOM   6407 N N     . ASP   B 2 197 ? -17.819 -43.061  -38.614 1.00 32.40  ? 189 ASP   B N     1 
ATOM   6408 C CA    . ASP   B 2 197 ? -17.106 -44.035  -39.426 1.00 31.88  ? 189 ASP   B CA    1 
ATOM   6409 C C     . ASP   B 2 197 ? -16.033 -43.328  -40.256 1.00 31.60  ? 189 ASP   B C     1 
ATOM   6410 O O     . ASP   B 2 197 ? -15.327 -43.972  -41.027 1.00 30.89  ? 189 ASP   B O     1 
ATOM   6411 C CB    . ASP   B 2 197 ? -18.061 -44.865  -40.272 1.00 31.49  ? 189 ASP   B CB    1 
ATOM   6412 C CG    . ASP   B 2 197 ? -18.714 -44.148  -41.446 1.00 31.21  ? 189 ASP   B CG    1 
ATOM   6413 O OD1   . ASP   B 2 197 ? -18.414 -42.954  -41.644 1.00 31.02  ? 189 ASP   B OD1   1 
ATOM   6414 O OD2   . ASP   B 2 197 ? -19.516 -44.794  -42.155 1.00 30.19  ? 189 ASP   B OD2   1 
ATOM   6415 N N     . ASN   B 2 198 ? -15.950 -41.998  -40.112 1.00 32.09  ? 190 ASN   B N     1 
ATOM   6416 C CA    . ASN   B 2 198 ? -14.904 -41.179  -40.707 1.00 32.93  ? 190 ASN   B CA    1 
ATOM   6417 C C     . ASN   B 2 198 ? -15.163 -40.969  -42.200 1.00 32.81  ? 190 ASN   B C     1 
ATOM   6418 O O     . ASN   B 2 198 ? -14.271 -40.523  -42.920 1.00 33.06  ? 190 ASN   B O     1 
ATOM   6419 C CB    . ASN   B 2 198 ? -13.506 -41.746  -40.471 1.00 32.99  ? 190 ASN   B CB    1 
ATOM   6420 C CG    . ASN   B 2 198 ? -12.428 -40.695  -40.614 1.00 33.27  ? 190 ASN   B CG    1 
ATOM   6421 O OD1   . ASN   B 2 198 ? -12.714 -39.494  -40.564 1.00 33.63  ? 190 ASN   B OD1   1 
ATOM   6422 N ND2   . ASN   B 2 198 ? -11.183 -41.114  -40.774 1.00 33.65  ? 190 ASN   B ND2   1 
ATOM   6423 N N     . ARG   B 2 199 ? -16.387 -41.262  -42.657 1.00 32.84  ? 191 ARG   B N     1 
ATOM   6424 C CA    . ARG   B 2 199 ? -16.756 -41.039  -44.045 1.00 33.26  ? 191 ARG   B CA    1 
ATOM   6425 C C     . ARG   B 2 199 ? -17.482 -39.705  -44.188 1.00 34.86  ? 191 ARG   B C     1 
ATOM   6426 O O     . ARG   B 2 199 ? -18.232 -39.295  -43.305 1.00 33.04  ? 191 ARG   B O     1 
ATOM   6427 C CB    . ARG   B 2 199 ? -17.701 -42.111  -44.595 1.00 32.99  ? 191 ARG   B CB    1 
ATOM   6428 C CG    . ARG   B 2 199 ? -17.064 -43.461  -44.878 1.00 32.75  ? 191 ARG   B CG    1 
ATOM   6429 C CD    . ARG   B 2 199 ? -18.123 -44.422  -45.377 1.00 32.69  ? 191 ARG   B CD    1 
ATOM   6430 N NE    . ARG   B 2 199 ? -17.562 -45.732  -45.723 1.00 33.35  ? 191 ARG   B NE    1 
ATOM   6431 C CZ    . ARG   B 2 199 ? -17.690 -46.848  -45.014 1.00 33.47  ? 191 ARG   B CZ    1 
ATOM   6432 N NH1   . ARG   B 2 199 ? -18.230 -46.825  -43.807 1.00 33.68  ? 191 ARG   B NH1   1 
ATOM   6433 N NH2   . ARG   B 2 199 ? -17.245 -47.989  -45.509 1.00 33.48  ? 191 ARG   B NH2   1 
ATOM   6434 N N     . ILE   B 2 200 ? -17.240 -39.048  -45.328 1.00 37.54  ? 192 ILE   B N     1 
ATOM   6435 C CA    . ILE   B 2 200 ? -18.082 -37.970  -45.814 1.00 37.95  ? 192 ILE   B CA    1 
ATOM   6436 C C     . ILE   B 2 200 ? -18.720 -38.449  -47.114 1.00 38.37  ? 192 ILE   B C     1 
ATOM   6437 O O     . ILE   B 2 200 ? -18.011 -38.729  -48.076 1.00 39.00  ? 192 ILE   B O     1 
ATOM   6438 C CB    . ILE   B 2 200 ? -17.267 -36.679  -46.008 1.00 38.37  ? 192 ILE   B CB    1 
ATOM   6439 C CG1   . ILE   B 2 200 ? -16.630 -36.222  -44.691 1.00 38.43  ? 192 ILE   B CG1   1 
ATOM   6440 C CG2   . ILE   B 2 200 ? -18.128 -35.582  -46.638 1.00 38.97  ? 192 ILE   B CG2   1 
ATOM   6441 C CD1   . ILE   B 2 200 ? -15.677 -35.047  -44.823 1.00 38.44  ? 192 ILE   B CD1   1 
ATOM   6442 N N     . LEU   B 2 201 ? -20.052 -38.571  -47.121 1.00 38.55  ? 193 LEU   B N     1 
ATOM   6443 C CA    . LEU   B 2 201 ? -20.768 -39.059  -48.288 1.00 38.27  ? 193 LEU   B CA    1 
ATOM   6444 C C     . LEU   B 2 201 ? -21.460 -37.891  -48.984 1.00 38.52  ? 193 LEU   B C     1 
ATOM   6445 O O     . LEU   B 2 201 ? -22.250 -37.178  -48.368 1.00 37.00  ? 193 LEU   B O     1 
ATOM   6446 C CB    . LEU   B 2 201 ? -21.778 -40.132  -47.886 1.00 38.27  ? 193 LEU   B CB    1 
ATOM   6447 C CG    . LEU   B 2 201 ? -21.212 -41.362  -47.170 1.00 38.14  ? 193 LEU   B CG    1 
ATOM   6448 C CD1   . LEU   B 2 201 ? -22.311 -42.382  -46.928 1.00 38.00  ? 193 LEU   B CD1   1 
ATOM   6449 C CD2   . LEU   B 2 201 ? -20.067 -41.984  -47.948 1.00 38.27  ? 193 LEU   B CD2   1 
ATOM   6450 N N     . LEU   B 2 202 ? -21.130 -37.700  -50.268 1.00 39.54  ? 194 LEU   B N     1 
ATOM   6451 C CA    . LEU   B 2 202 ? -21.921 -36.864  -51.154 1.00 39.82  ? 194 LEU   B CA    1 
ATOM   6452 C C     . LEU   B 2 202 ? -23.029 -37.735  -51.732 1.00 38.26  ? 194 LEU   B C     1 
ATOM   6453 O O     . LEU   B 2 202 ? -22.759 -38.804  -52.277 1.00 37.52  ? 194 LEU   B O     1 
ATOM   6454 C CB    . LEU   B 2 202 ? -21.056 -36.232  -52.246 1.00 41.45  ? 194 LEU   B CB    1 
ATOM   6455 C CG    . LEU   B 2 202 ? -21.791 -35.635  -53.454 1.00 42.63  ? 194 LEU   B CG    1 
ATOM   6456 C CD1   . LEU   B 2 202 ? -22.868 -34.630  -53.074 1.00 43.08  ? 194 LEU   B CD1   1 
ATOM   6457 C CD2   . LEU   B 2 202 ? -20.785 -34.980  -54.388 1.00 42.94  ? 194 LEU   B CD2   1 
ATOM   6458 N N     . TRP   B 2 203 ? -24.273 -37.278  -51.572 1.00 37.42  ? 195 TRP   B N     1 
ATOM   6459 C CA    . TRP   B 2 203 ? -25.427 -38.040  -52.010 1.00 37.97  ? 195 TRP   B CA    1 
ATOM   6460 C C     . TRP   B 2 203 ? -25.973 -37.475  -53.316 1.00 39.91  ? 195 TRP   B C     1 
ATOM   6461 O O     . TRP   B 2 203 ? -25.705 -36.328  -53.668 1.00 39.85  ? 195 TRP   B O     1 
ATOM   6462 C CB    . TRP   B 2 203 ? -26.498 -38.049  -50.914 1.00 37.85  ? 195 TRP   B CB    1 
ATOM   6463 C CG    . TRP   B 2 203 ? -26.089 -38.828  -49.692 1.00 37.02  ? 195 TRP   B CG    1 
ATOM   6464 C CD1   . TRP   B 2 203 ? -25.258 -38.417  -48.693 1.00 36.71  ? 195 TRP   B CD1   1 
ATOM   6465 C CD2   . TRP   B 2 203 ? -26.504 -40.166  -49.345 1.00 36.40  ? 195 TRP   B CD2   1 
ATOM   6466 N NE1   . TRP   B 2 203 ? -25.125 -39.401  -47.750 1.00 36.51  ? 195 TRP   B NE1   1 
ATOM   6467 C CE2   . TRP   B 2 203 ? -25.877 -40.484  -48.120 1.00 36.47  ? 195 TRP   B CE2   1 
ATOM   6468 C CE3   . TRP   B 2 203 ? -27.339 -41.116  -49.944 1.00 36.46  ? 195 TRP   B CE3   1 
ATOM   6469 C CZ2   . TRP   B 2 203 ? -26.060 -41.712  -47.489 1.00 35.88  ? 195 TRP   B CZ2   1 
ATOM   6470 C CZ3   . TRP   B 2 203 ? -27.521 -42.329  -49.317 1.00 36.82  ? 195 TRP   B CZ3   1 
ATOM   6471 C CH2   . TRP   B 2 203 ? -26.891 -42.620  -48.106 1.00 36.50  ? 195 TRP   B CH2   1 
ATOM   6472 N N     . ASP   B 2 204 ? -26.716 -38.329  -54.028 1.00 41.00  ? 196 ASP   B N     1 
ATOM   6473 C CA    . ASP   B 2 204 ? -27.476 -37.950  -55.205 1.00 40.71  ? 196 ASP   B CA    1 
ATOM   6474 C C     . ASP   B 2 204 ? -28.495 -39.056  -55.460 1.00 41.07  ? 196 ASP   B C     1 
ATOM   6475 O O     . ASP   B 2 204 ? -28.155 -40.091  -56.030 1.00 40.26  ? 196 ASP   B O     1 
ATOM   6476 C CB    . ASP   B 2 204 ? -26.576 -37.694  -56.404 1.00 40.97  ? 196 ASP   B CB    1 
ATOM   6477 C CG    . ASP   B 2 204 ? -27.215 -36.895  -57.533 1.00 41.11  ? 196 ASP   B CG    1 
ATOM   6478 O OD1   . ASP   B 2 204 ? -28.326 -37.270  -57.966 1.00 41.53  ? 196 ASP   B OD1   1 
ATOM   6479 O OD2   . ASP   B 2 204 ? -26.593 -35.906  -57.972 1.00 40.52  ? 196 ASP   B OD2   1 
ATOM   6480 N N     . THR   B 2 205 ? -29.746 -38.824  -55.040 1.00 41.78  ? 197 THR   B N     1 
ATOM   6481 C CA    . THR   B 2 205 ? -30.755 -39.873  -54.991 1.00 42.69  ? 197 THR   B CA    1 
ATOM   6482 C C     . THR   B 2 205 ? -31.167 -40.321  -56.394 1.00 43.06  ? 197 THR   B C     1 
ATOM   6483 O O     . THR   B 2 205 ? -32.045 -41.170  -56.524 1.00 43.30  ? 197 THR   B O     1 
ATOM   6484 C CB    . THR   B 2 205 ? -31.966 -39.398  -54.186 1.00 43.56  ? 197 THR   B CB    1 
ATOM   6485 O OG1   . THR   B 2 205 ? -32.283 -38.092  -54.655 1.00 43.51  ? 197 THR   B OG1   1 
ATOM   6486 C CG2   . THR   B 2 205 ? -31.694 -39.343  -52.694 1.00 44.66  ? 197 THR   B CG2   1 
ATOM   6487 N N     . ARG   B 2 206 ? -30.541 -39.765  -57.439 1.00 43.73  ? 198 ARG   B N     1 
ATOM   6488 C CA    . ARG   B 2 206 ? -30.865 -40.152  -58.803 1.00 44.87  ? 198 ARG   B CA    1 
ATOM   6489 C C     . ARG   B 2 206 ? -30.039 -41.360  -59.241 1.00 45.44  ? 198 ARG   B C     1 
ATOM   6490 O O     . ARG   B 2 206 ? -30.415 -42.034  -60.196 1.00 47.82  ? 198 ARG   B O     1 
ATOM   6491 C CB    . ARG   B 2 206 ? -30.680 -38.979  -59.769 1.00 44.84  ? 198 ARG   B CB    1 
ATOM   6492 C CG    . ARG   B 2 206 ? -31.694 -37.868  -59.531 1.00 45.16  ? 198 ARG   B CG    1 
ATOM   6493 C CD    . ARG   B 2 206 ? -31.398 -36.586  -60.298 1.00 45.19  ? 198 ARG   B CD    1 
ATOM   6494 N NE    . ARG   B 2 206 ? -30.129 -35.971  -59.892 1.00 44.68  ? 198 ARG   B NE    1 
ATOM   6495 C CZ    . ARG   B 2 206 ? -29.759 -34.718  -60.132 1.00 44.44  ? 198 ARG   B CZ    1 
ATOM   6496 N NH1   . ARG   B 2 206 ? -30.594 -33.866  -60.705 1.00 44.62  ? 198 ARG   B NH1   1 
ATOM   6497 N NH2   . ARG   B 2 206 ? -28.554 -34.310  -59.768 1.00 44.36  ? 198 ARG   B NH2   1 
ATOM   6498 N N     . CYS   B 2 207 ? -28.919 -41.627  -58.556 1.00 44.69  ? 199 CYS   B N     1 
ATOM   6499 C CA    . CYS   B 2 207 ? -28.090 -42.781  -58.872 1.00 45.01  ? 199 CYS   B CA    1 
ATOM   6500 C C     . CYS   B 2 207 ? -28.580 -44.002  -58.098 1.00 46.02  ? 199 CYS   B C     1 
ATOM   6501 O O     . CYS   B 2 207 ? -29.066 -43.862  -56.975 1.00 46.75  ? 199 CYS   B O     1 
ATOM   6502 C CB    . CYS   B 2 207 ? -26.628 -42.512  -58.546 1.00 44.83  ? 199 CYS   B CB    1 
ATOM   6503 S SG    . CYS   B 2 207 ? -26.079 -40.872  -59.077 1.00 46.79  ? 199 CYS   B SG    1 
ATOM   6504 N N     . PRO   B 2 208 ? -28.445 -45.233  -58.650 1.00 46.35  ? 200 PRO   B N     1 
ATOM   6505 C CA    . PRO   B 2 208 ? -28.929 -46.441  -57.975 1.00 46.96  ? 200 PRO   B CA    1 
ATOM   6506 C C     . PRO   B 2 208 ? -28.092 -46.773  -56.738 1.00 46.81  ? 200 PRO   B C     1 
ATOM   6507 O O     . PRO   B 2 208 ? -28.592 -47.366  -55.785 1.00 46.11  ? 200 PRO   B O     1 
ATOM   6508 C CB    . PRO   B 2 208 ? -28.859 -47.553  -59.046 1.00 47.39  ? 200 PRO   B CB    1 
ATOM   6509 C CG    . PRO   B 2 208 ? -28.441 -46.853  -60.332 1.00 47.44  ? 200 PRO   B CG    1 
ATOM   6510 C CD    . PRO   B 2 208 ? -27.793 -45.538  -59.933 1.00 47.21  ? 200 PRO   B CD    1 
ATOM   6511 N N     . LYS   B 2 209 ? -26.804 -46.413  -56.790 1.00 46.87  ? 201 LYS   B N     1 
ATOM   6512 C CA    . LYS   B 2 209 ? -25.968 -46.310  -55.607 1.00 45.72  ? 201 LYS   B CA    1 
ATOM   6513 C C     . LYS   B 2 209 ? -25.838 -44.829  -55.258 1.00 43.90  ? 201 LYS   B C     1 
ATOM   6514 O O     . LYS   B 2 209 ? -24.907 -44.160  -55.708 1.00 41.64  ? 201 LYS   B O     1 
ATOM   6515 C CB    . LYS   B 2 209 ? -24.633 -47.019  -55.857 1.00 47.09  ? 201 LYS   B CB    1 
ATOM   6516 C CG    . LYS   B 2 209 ? -24.753 -48.534  -55.933 1.00 48.80  ? 201 LYS   B CG    1 
ATOM   6517 C CD    . LYS   B 2 209 ? -23.427 -49.283  -55.966 1.00 50.11  ? 201 LYS   B CD    1 
ATOM   6518 C CE    . LYS   B 2 209 ? -23.630 -50.766  -55.942 1.00 50.48  ? 201 LYS   B CE    1 
ATOM   6519 N NZ    . LYS   B 2 209 ? -22.369 -51.483  -55.739 1.00 51.27  ? 201 LYS   B NZ    1 
ATOM   6520 N N     . PRO   B 2 210 ? -26.783 -44.274  -54.458 1.00 42.35  ? 202 PRO   B N     1 
ATOM   6521 C CA    . PRO   B 2 210 ? -26.881 -42.825  -54.261 1.00 41.46  ? 202 PRO   B CA    1 
ATOM   6522 C C     . PRO   B 2 210 ? -25.743 -42.137  -53.512 1.00 41.58  ? 202 PRO   B C     1 
ATOM   6523 O O     . PRO   B 2 210 ? -25.662 -40.912  -53.531 1.00 41.72  ? 202 PRO   B O     1 
ATOM   6524 C CB    . PRO   B 2 210 ? -28.220 -42.679  -53.503 1.00 41.25  ? 202 PRO   B CB    1 
ATOM   6525 C CG    . PRO   B 2 210 ? -28.394 -43.992  -52.778 1.00 41.13  ? 202 PRO   B CG    1 
ATOM   6526 C CD    . PRO   B 2 210 ? -27.829 -45.017  -53.735 1.00 41.36  ? 202 PRO   B CD    1 
ATOM   6527 N N     . ALA   B 2 211 ? -24.872 -42.912  -52.856 1.00 42.42  ? 203 ALA   B N     1 
ATOM   6528 C CA    . ALA   B 2 211 ? -23.841 -42.338  -52.006 1.00 43.15  ? 203 ALA   B CA    1 
ATOM   6529 C C     . ALA   B 2 211 ? -22.477 -42.423  -52.687 1.00 42.54  ? 203 ALA   B C     1 
ATOM   6530 O O     . ALA   B 2 211 ? -22.181 -43.393  -53.381 1.00 41.50  ? 203 ALA   B O     1 
ATOM   6531 C CB    . ALA   B 2 211 ? -23.838 -43.032  -50.661 1.00 43.49  ? 203 ALA   B CB    1 
ATOM   6532 N N     . SER   B 2 212 ? -21.656 -41.390  -52.472 1.00 43.07  ? 204 SER   B N     1 
ATOM   6533 C CA    . SER   B 2 212 ? -20.304 -41.339  -53.001 1.00 44.57  ? 204 SER   B CA    1 
ATOM   6534 C C     . SER   B 2 212 ? -19.358 -40.793  -51.935 1.00 45.46  ? 204 SER   B C     1 
ATOM   6535 O O     . SER   B 2 212 ? -19.503 -39.655  -51.493 1.00 46.56  ? 204 SER   B O     1 
ATOM   6536 C CB    . SER   B 2 212 ? -20.246 -40.512  -54.257 1.00 46.43  ? 204 SER   B CB    1 
ATOM   6537 O OG    . SER   B 2 212 ? -18.903 -40.316  -54.679 1.00 48.28  ? 204 SER   B OG    1 
ATOM   6538 N N     . GLN   B 2 213 ? -18.391 -41.625  -51.537 1.00 45.93  ? 205 GLN   B N     1 
ATOM   6539 C CA    . GLN   B 2 213 ? -17.406 -41.269  -50.529 1.00 46.42  ? 205 GLN   B CA    1 
ATOM   6540 C C     . GLN   B 2 213 ? -16.412 -40.287  -51.142 1.00 47.47  ? 205 GLN   B C     1 
ATOM   6541 O O     . GLN   B 2 213 ? -16.093 -40.394  -52.321 1.00 48.84  ? 205 GLN   B O     1 
ATOM   6542 C CB    . GLN   B 2 213 ? -16.780 -42.581  -50.054 1.00 45.45  ? 205 GLN   B CB    1 
ATOM   6543 C CG    . GLN   B 2 213 ? -15.819 -42.448  -48.879 1.00 44.96  ? 205 GLN   B CG    1 
ATOM   6544 C CD    . GLN   B 2 213 ? -15.448 -43.785  -48.269 1.00 44.88  ? 205 GLN   B CD    1 
ATOM   6545 O OE1   . GLN   B 2 213 ? -16.060 -44.823  -48.549 1.00 44.29  ? 205 GLN   B OE1   1 
ATOM   6546 N NE2   . GLN   B 2 213 ? -14.441 -43.768  -47.410 1.00 45.20  ? 205 GLN   B NE2   1 
ATOM   6547 N N     . ILE   B 2 214 ? -15.933 -39.331  -50.339 1.00 49.78  ? 206 ILE   B N     1 
ATOM   6548 C CA    . ILE   B 2 214 ? -15.091 -38.257  -50.843 1.00 52.81  ? 206 ILE   B CA    1 
ATOM   6549 C C     . ILE   B 2 214 ? -14.053 -37.888  -49.787 1.00 55.07  ? 206 ILE   B C     1 
ATOM   6550 O O     . ILE   B 2 214 ? -14.393 -37.334  -48.745 1.00 57.54  ? 206 ILE   B O     1 
ATOM   6551 C CB    . ILE   B 2 214 ? -15.943 -37.045  -51.274 1.00 54.21  ? 206 ILE   B CB    1 
ATOM   6552 C CG1   . ILE   B 2 214 ? -17.175 -36.868  -50.380 1.00 53.30  ? 206 ILE   B CG1   1 
ATOM   6553 C CG2   . ILE   B 2 214 ? -16.334 -37.157  -52.749 1.00 55.28  ? 206 ILE   B CG2   1 
ATOM   6554 C CD1   . ILE   B 2 214 ? -17.995 -35.627  -50.678 1.00 52.95  ? 206 ILE   B CD1   1 
ATOM   6555 N N     . GLY   B 2 215 ? -12.783 -38.200  -50.080 1.00 56.55  ? 207 GLY   B N     1 
ATOM   6556 C CA    . GLY   B 2 215 ? -11.680 -37.913  -49.178 1.00 56.78  ? 207 GLY   B CA    1 
ATOM   6557 C C     . GLY   B 2 215 ? -11.356 -36.431  -49.156 1.00 57.77  ? 207 GLY   B C     1 
ATOM   6558 O O     . GLY   B 2 215 ? -10.883 -35.971  -48.096 1.00 58.54  ? 207 GLY   B O     1 
ATOM   6559 N N     . GLY   B 2 220 ? -7.658  -38.629  -41.774 1.00 54.45  ? 212 GLY   B N     1 
ATOM   6560 C CA    . GLY   B 2 220 ? -8.326  -37.390  -41.330 1.00 53.82  ? 212 GLY   B CA    1 
ATOM   6561 C C     . GLY   B 2 220 ? -9.198  -37.645  -40.104 1.00 53.66  ? 212 GLY   B C     1 
ATOM   6562 O O     . GLY   B 2 220 ? -9.871  -38.673  -40.027 1.00 54.47  ? 212 GLY   B O     1 
ATOM   6563 N N     . TYR   B 2 221 ? -9.175  -36.699  -39.155 1.00 51.85  ? 213 TYR   B N     1 
ATOM   6564 C CA    . TYR   B 2 221 ? -9.910  -36.834  -37.907 1.00 48.56  ? 213 TYR   B CA    1 
ATOM   6565 C C     . TYR   B 2 221 ? -11.407 -36.803  -38.194 1.00 46.23  ? 213 TYR   B C     1 
ATOM   6566 O O     . TYR   B 2 221 ? -11.841 -36.252  -39.204 1.00 46.10  ? 213 TYR   B O     1 
ATOM   6567 C CB    . TYR   B 2 221 ? -9.480  -35.755  -36.910 1.00 48.25  ? 213 TYR   B CB    1 
ATOM   6568 C CG    . TYR   B 2 221 ? -8.119  -36.035  -36.291 1.00 48.88  ? 213 TYR   B CG    1 
ATOM   6569 C CD1   . TYR   B 2 221 ? -7.947  -37.098  -35.413 1.00 49.15  ? 213 TYR   B CD1   1 
ATOM   6570 C CD2   . TYR   B 2 221 ? -7.013  -35.242  -36.577 1.00 48.86  ? 213 TYR   B CD2   1 
ATOM   6571 C CE1   . TYR   B 2 221 ? -6.714  -37.373  -34.846 1.00 48.49  ? 213 TYR   B CE1   1 
ATOM   6572 C CE2   . TYR   B 2 221 ? -5.776  -35.502  -36.010 1.00 48.49  ? 213 TYR   B CE2   1 
ATOM   6573 C CZ    . TYR   B 2 221 ? -5.628  -36.571  -35.143 1.00 48.47  ? 213 TYR   B CZ    1 
ATOM   6574 O OH    . TYR   B 2 221 ? -4.419  -36.843  -34.575 1.00 49.70  ? 213 TYR   B OH    1 
ATOM   6575 N N     . LEU   B 2 222 ? -12.181 -37.409  -37.286 1.00 43.38  ? 214 LEU   B N     1 
ATOM   6576 C CA    . LEU   B 2 222 ? -13.595 -37.654  -37.513 1.00 40.98  ? 214 LEU   B CA    1 
ATOM   6577 C C     . LEU   B 2 222 ? -14.295 -36.344  -37.862 1.00 39.93  ? 214 LEU   B C     1 
ATOM   6578 O O     . LEU   B 2 222 ? -14.082 -35.327  -37.206 1.00 38.94  ? 214 LEU   B O     1 
ATOM   6579 C CB    . LEU   B 2 222 ? -14.232 -38.314  -36.292 1.00 40.25  ? 214 LEU   B CB    1 
ATOM   6580 C CG    . LEU   B 2 222 ? -13.747 -39.727  -35.951 1.00 39.31  ? 214 LEU   B CG    1 
ATOM   6581 C CD1   . LEU   B 2 222 ? -14.557 -40.266  -34.787 1.00 39.11  ? 214 LEU   B CD1   1 
ATOM   6582 C CD2   . LEU   B 2 222 ? -13.829 -40.675  -37.136 1.00 38.20  ? 214 LEU   B CD2   1 
ATOM   6583 N N     . PRO   B 2 223 ? -15.150 -36.337  -38.910 1.00 39.41  ? 215 PRO   B N     1 
ATOM   6584 C CA    . PRO   B 2 223 ? -15.868 -35.132  -39.320 1.00 39.06  ? 215 PRO   B CA    1 
ATOM   6585 C C     . PRO   B 2 223 ? -17.099 -34.901  -38.448 1.00 38.91  ? 215 PRO   B C     1 
ATOM   6586 O O     . PRO   B 2 223 ? -17.854 -35.833  -38.182 1.00 37.25  ? 215 PRO   B O     1 
ATOM   6587 C CB    . PRO   B 2 223 ? -16.216 -35.455  -40.779 1.00 39.16  ? 215 PRO   B CB    1 
ATOM   6588 C CG    . PRO   B 2 223 ? -16.446 -36.951  -40.775 1.00 39.02  ? 215 PRO   B CG    1 
ATOM   6589 C CD    . PRO   B 2 223 ? -15.475 -37.501  -39.749 1.00 39.55  ? 215 PRO   B CD    1 
ATOM   6590 N N     . THR   B 2 224 ? -17.291 -33.644  -38.027 1.00 40.77  ? 216 THR   B N     1 
ATOM   6591 C CA    . THR   B 2 224 ? -18.280 -33.304  -37.016 1.00 41.55  ? 216 THR   B CA    1 
ATOM   6592 C C     . THR   B 2 224 ? -19.363 -32.376  -37.570 1.00 42.50  ? 216 THR   B C     1 
ATOM   6593 O O     . THR   B 2 224 ? -20.474 -32.374  -37.045 1.00 43.12  ? 216 THR   B O     1 
ATOM   6594 C CB    . THR   B 2 224 ? -17.568 -32.682  -35.814 1.00 42.08  ? 216 THR   B CB    1 
ATOM   6595 O OG1   . THR   B 2 224 ? -16.940 -31.494  -36.282 1.00 42.45  ? 216 THR   B OG1   1 
ATOM   6596 C CG2   . THR   B 2 224 ? -16.523 -33.607  -35.215 1.00 41.97  ? 216 THR   B CG2   1 
ATOM   6597 N N     . SER   B 2 225 ? -19.051 -31.589  -38.613 1.00 42.76  ? 217 SER   B N     1 
ATOM   6598 C CA    . SER   B 2 225 ? -19.941 -30.524  -39.060 1.00 42.84  ? 217 SER   B CA    1 
ATOM   6599 C C     . SER   B 2 225 ? -19.817 -30.297  -40.566 1.00 43.29  ? 217 SER   B C     1 
ATOM   6600 O O     . SER   B 2 225 ? -18.744 -30.492  -41.133 1.00 43.93  ? 217 SER   B O     1 
ATOM   6601 C CB    . SER   B 2 225 ? -19.659 -29.255  -38.301 1.00 42.36  ? 217 SER   B CB    1 
ATOM   6602 O OG    . SER   B 2 225 ? -18.288 -28.898  -38.417 1.00 42.37  ? 217 SER   B OG    1 
ATOM   6603 N N     . LEU   B 2 226 ? -20.924 -29.859  -41.191 1.00 43.13  ? 218 LEU   B N     1 
ATOM   6604 C CA    . LEU   B 2 226 ? -20.999 -29.651  -42.632 1.00 42.67  ? 218 LEU   B CA    1 
ATOM   6605 C C     . LEU   B 2 226 ? -21.727 -28.345  -42.948 1.00 43.53  ? 218 LEU   B C     1 
ATOM   6606 O O     . LEU   B 2 226 ? -22.746 -28.035  -42.335 1.00 43.99  ? 218 LEU   B O     1 
ATOM   6607 C CB    . LEU   B 2 226 ? -21.738 -30.818  -43.286 1.00 41.25  ? 218 LEU   B CB    1 
ATOM   6608 C CG    . LEU   B 2 226 ? -21.088 -32.199  -43.167 1.00 40.29  ? 218 LEU   B CG    1 
ATOM   6609 C CD1   . LEU   B 2 226 ? -22.060 -33.260  -43.655 1.00 39.64  ? 218 LEU   B CD1   1 
ATOM   6610 C CD2   . LEU   B 2 226 ? -19.776 -32.262  -43.931 1.00 39.86  ? 218 LEU   B CD2   1 
ATOM   6611 N N     . ALA   B 2 227 ? -21.220 -27.610  -43.947 1.00 44.48  ? 219 ALA   B N     1 
ATOM   6612 C CA    . ALA   B 2 227 ? -21.942 -26.482  -44.516 1.00 44.65  ? 219 ALA   B CA    1 
ATOM   6613 C C     . ALA   B 2 227 ? -21.617 -26.342  -46.002 1.00 45.07  ? 219 ALA   B C     1 
ATOM   6614 O O     . ALA   B 2 227 ? -20.467 -26.100  -46.366 1.00 44.16  ? 219 ALA   B O     1 
ATOM   6615 C CB    . ALA   B 2 227 ? -21.606 -25.216  -43.761 1.00 44.81  ? 219 ALA   B CB    1 
ATOM   6616 N N     . TRP   B 2 228 ? -22.644 -26.501  -46.851 1.00 45.23  ? 220 TRP   B N     1 
ATOM   6617 C CA    . TRP   B 2 228 ? -22.548 -26.139  -48.258 1.00 46.67  ? 220 TRP   B CA    1 
ATOM   6618 C C     . TRP   B 2 228 ? -22.189 -24.661  -48.387 1.00 48.44  ? 220 TRP   B C     1 
ATOM   6619 O O     . TRP   B 2 228 ? -22.546 -23.856  -47.528 1.00 48.56  ? 220 TRP   B O     1 
ATOM   6620 C CB    . TRP   B 2 228 ? -23.871 -26.408  -48.988 1.00 44.88  ? 220 TRP   B CB    1 
ATOM   6621 C CG    . TRP   B 2 228 ? -24.149 -27.849  -49.319 1.00 44.52  ? 220 TRP   B CG    1 
ATOM   6622 C CD1   . TRP   B 2 228 ? -25.016 -28.683  -48.680 1.00 44.11  ? 220 TRP   B CD1   1 
ATOM   6623 C CD2   . TRP   B 2 228 ? -23.583 -28.614  -50.406 1.00 44.99  ? 220 TRP   B CD2   1 
ATOM   6624 N NE1   . TRP   B 2 228 ? -25.028 -29.911  -49.284 1.00 44.65  ? 220 TRP   B NE1   1 
ATOM   6625 C CE2   . TRP   B 2 228 ? -24.159 -29.901  -50.343 1.00 44.90  ? 220 TRP   B CE2   1 
ATOM   6626 C CE3   . TRP   B 2 228 ? -22.650 -28.341  -51.413 1.00 44.85  ? 220 TRP   B CE3   1 
ATOM   6627 C CZ2   . TRP   B 2 228 ? -23.828 -30.906  -51.250 1.00 45.15  ? 220 TRP   B CZ2   1 
ATOM   6628 C CZ3   . TRP   B 2 228 ? -22.322 -29.337  -52.307 1.00 44.75  ? 220 TRP   B CZ3   1 
ATOM   6629 C CH2   . TRP   B 2 228 ? -22.907 -30.600  -52.227 1.00 44.99  ? 220 TRP   B CH2   1 
ATOM   6630 N N     . HIS   B 2 229 ? -21.496 -24.309  -49.475 1.00 51.24  ? 221 HIS   B N     1 
ATOM   6631 C CA    . HIS   B 2 229 ? -21.287 -22.911  -49.814 1.00 53.83  ? 221 HIS   B CA    1 
ATOM   6632 C C     . HIS   B 2 229 ? -22.568 -22.386  -50.458 1.00 53.93  ? 221 HIS   B C     1 
ATOM   6633 O O     . HIS   B 2 229 ? -23.135 -23.048  -51.327 1.00 53.85  ? 221 HIS   B O     1 
ATOM   6634 C CB    . HIS   B 2 229 ? -20.060 -22.737  -50.716 1.00 55.05  ? 221 HIS   B CB    1 
ATOM   6635 C CG    . HIS   B 2 229 ? -19.516 -21.346  -50.719 1.00 56.72  ? 221 HIS   B CG    1 
ATOM   6636 N ND1   . HIS   B 2 229 ? -20.052 -20.326  -51.474 1.00 57.53  ? 221 HIS   B ND1   1 
ATOM   6637 C CD2   . HIS   B 2 229 ? -18.499 -20.803  -50.037 1.00 57.58  ? 221 HIS   B CD2   1 
ATOM   6638 C CE1   . HIS   B 2 229 ? -19.366 -19.213  -51.259 1.00 57.56  ? 221 HIS   B CE1   1 
ATOM   6639 N NE2   . HIS   B 2 229 ? -18.417 -19.480  -50.390 1.00 57.77  ? 221 HIS   B NE2   1 
ATOM   6640 N N     . PRO   B 2 230 ? -23.079 -21.202  -50.041 1.00 55.04  ? 222 PRO   B N     1 
ATOM   6641 C CA    . PRO   B 2 230 ? -24.345 -20.684  -50.565 1.00 56.76  ? 222 PRO   B CA    1 
ATOM   6642 C C     . PRO   B 2 230 ? -24.268 -20.144  -51.993 1.00 58.58  ? 222 PRO   B C     1 
ATOM   6643 O O     . PRO   B 2 230 ? -25.239 -20.244  -52.742 1.00 58.73  ? 222 PRO   B O     1 
ATOM   6644 C CB    . PRO   B 2 230 ? -24.716 -19.587  -49.545 1.00 55.27  ? 222 PRO   B CB    1 
ATOM   6645 C CG    . PRO   B 2 230 ? -23.385 -19.100  -49.013 1.00 54.89  ? 222 PRO   B CG    1 
ATOM   6646 C CD    . PRO   B 2 230 ? -22.474 -20.315  -49.033 1.00 54.75  ? 222 PRO   B CD    1 
ATOM   6647 N N     . GLN   B 2 231 ? -23.109 -19.582  -52.358 1.00 60.79  ? 223 GLN   B N     1 
ATOM   6648 C CA    . GLN   B 2 231 ? -22.925 -18.934  -53.649 1.00 63.49  ? 223 GLN   B CA    1 
ATOM   6649 C C     . GLN   B 2 231 ? -22.528 -19.973  -54.696 1.00 64.41  ? 223 GLN   B C     1 
ATOM   6650 O O     . GLN   B 2 231 ? -23.050 -19.970  -55.809 1.00 65.34  ? 223 GLN   B O     1 
ATOM   6651 C CB    . GLN   B 2 231 ? -21.854 -17.842  -53.591 1.00 64.55  ? 223 GLN   B CB    1 
ATOM   6652 C CG    . GLN   B 2 231 ? -21.888 -16.976  -52.334 1.00 66.14  ? 223 GLN   B CG    1 
ATOM   6653 C CD    . GLN   B 2 231 ? -23.206 -16.265  -52.107 1.00 67.70  ? 223 GLN   B CD    1 
ATOM   6654 O OE1   . GLN   B 2 231 ? -24.061 -16.178  -52.995 1.00 67.72  ? 223 GLN   B OE1   1 
ATOM   6655 N NE2   . GLN   B 2 231 ? -23.375 -15.731  -50.905 1.00 69.55  ? 223 GLN   B NE2   1 
ATOM   6656 N N     . GLN   B 2 232 ? -21.597 -20.856  -54.318 1.00 64.28  ? 224 GLN   B N     1 
ATOM   6657 C CA    . GLN   B 2 232 ? -21.036 -21.838  -55.229 1.00 64.33  ? 224 GLN   B CA    1 
ATOM   6658 C C     . GLN   B 2 232 ? -21.458 -23.226  -54.761 1.00 67.12  ? 224 GLN   B C     1 
ATOM   6659 O O     . GLN   B 2 232 ? -20.983 -23.704  -53.734 1.00 69.59  ? 224 GLN   B O     1 
ATOM   6660 C CB    . GLN   B 2 232 ? -19.507 -21.783  -55.259 1.00 62.99  ? 224 GLN   B CB    1 
ATOM   6661 C CG    . GLN   B 2 232 ? -18.908 -20.472  -54.760 1.00 63.26  ? 224 GLN   B CG    1 
ATOM   6662 C CD    . GLN   B 2 232 ? -17.398 -20.434  -54.850 1.00 64.04  ? 224 GLN   B CD    1 
ATOM   6663 O OE1   . GLN   B 2 232 ? -16.768 -21.268  -55.510 1.00 64.71  ? 224 GLN   B OE1   1 
ATOM   6664 N NE2   . GLN   B 2 232 ? -16.800 -19.452  -54.191 1.00 63.67  ? 224 GLN   B NE2   1 
ATOM   6665 N N     . SER   B 2 233 ? -22.362 -23.869  -55.506 1.00 69.20  ? 225 SER   B N     1 
ATOM   6666 C CA    . SER   B 2 233 ? -22.549 -25.300  -55.346 1.00 71.41  ? 225 SER   B CA    1 
ATOM   6667 C C     . SER   B 2 233 ? -21.240 -25.975  -55.749 1.00 71.41  ? 225 SER   B C     1 
ATOM   6668 O O     . SER   B 2 233 ? -20.350 -25.316  -56.285 1.00 71.50  ? 225 SER   B O     1 
ATOM   6669 C CB    . SER   B 2 233 ? -23.731 -25.815  -56.136 1.00 72.00  ? 225 SER   B CB    1 
ATOM   6670 O OG    . SER   B 2 233 ? -23.473 -25.809  -57.533 1.00 72.22  ? 225 SER   B OG    1 
ATOM   6671 N N     . GLU   B 2 234 ? -21.116 -27.274  -55.455 1.00 70.15  ? 226 GLU   B N     1 
ATOM   6672 C CA    . GLU   B 2 234 ? -19.878 -28.008  -55.677 1.00 70.48  ? 226 GLU   B CA    1 
ATOM   6673 C C     . GLU   B 2 234 ? -18.838 -27.639  -54.614 1.00 69.11  ? 226 GLU   B C     1 
ATOM   6674 O O     . GLU   B 2 234 ? -17.748 -28.209  -54.602 1.00 69.75  ? 226 GLU   B O     1 
ATOM   6675 C CB    . GLU   B 2 234 ? -19.230 -27.748  -57.042 1.00 71.25  ? 226 GLU   B CB    1 
ATOM   6676 C CG    . GLU   B 2 234 ? -20.188 -27.714  -58.230 1.00 71.71  ? 226 GLU   B CG    1 
ATOM   6677 C CD    . GLU   B 2 234 ? -20.746 -29.059  -58.648 1.00 72.81  ? 226 GLU   B CD    1 
ATOM   6678 O OE1   . GLU   B 2 234 ? -20.342 -29.545  -59.726 1.00 72.99  ? 226 GLU   B OE1   1 
ATOM   6679 O OE2   . GLU   B 2 234 ? -21.589 -29.610  -57.911 1.00 75.00  ? 226 GLU   B OE2   1 
ATOM   6680 N N     . VAL   B 2 235 ? -19.163 -26.675  -53.740 1.00 65.85  ? 227 VAL   B N     1 
ATOM   6681 C CA    . VAL   B 2 235 ? -18.254 -26.232  -52.694 1.00 64.20  ? 227 VAL   B CA    1 
ATOM   6682 C C     . VAL   B 2 235 ? -18.952 -26.434  -51.353 1.00 61.31  ? 227 VAL   B C     1 
ATOM   6683 O O     . VAL   B 2 235 ? -20.151 -26.192  -51.232 1.00 60.26  ? 227 VAL   B O     1 
ATOM   6684 C CB    . VAL   B 2 235 ? -17.812 -24.763  -52.861 1.00 64.38  ? 227 VAL   B CB    1 
ATOM   6685 C CG1   . VAL   B 2 235 ? -16.805 -24.347  -51.794 1.00 63.81  ? 227 VAL   B CG1   1 
ATOM   6686 C CG2   . VAL   B 2 235 ? -17.255 -24.486  -54.252 1.00 64.54  ? 227 VAL   B CG2   1 
ATOM   6687 N N     . PHE   B 2 236 ? -18.182 -26.880  -50.354 1.00 60.05  ? 228 PHE   B N     1 
ATOM   6688 C CA    . PHE   B 2 236 ? -18.683 -27.046  -49.000 1.00 57.36  ? 228 PHE   B CA    1 
ATOM   6689 C C     . PHE   B 2 236 ? -17.500 -27.036  -48.035 1.00 55.76  ? 228 PHE   B C     1 
ATOM   6690 O O     . PHE   B 2 236 ? -16.348 -27.110  -48.461 1.00 55.24  ? 228 PHE   B O     1 
ATOM   6691 C CB    . PHE   B 2 236 ? -19.504 -28.335  -48.883 1.00 56.31  ? 228 PHE   B CB    1 
ATOM   6692 C CG    . PHE   B 2 236 ? -18.692 -29.621  -48.799 1.00 56.42  ? 228 PHE   B CG    1 
ATOM   6693 C CD1   . PHE   B 2 236 ? -18.245 -30.100  -47.571 1.00 55.71  ? 228 PHE   B CD1   1 
ATOM   6694 C CD2   . PHE   B 2 236 ? -18.396 -30.362  -49.940 1.00 56.37  ? 228 PHE   B CD2   1 
ATOM   6695 C CE1   . PHE   B 2 236 ? -17.510 -31.273  -47.490 1.00 54.64  ? 228 PHE   B CE1   1 
ATOM   6696 C CE2   . PHE   B 2 236 ? -17.663 -31.538  -49.851 1.00 55.54  ? 228 PHE   B CE2   1 
ATOM   6697 C CZ    . PHE   B 2 236 ? -17.223 -31.990  -48.628 1.00 54.73  ? 228 PHE   B CZ    1 
ATOM   6698 N N     . VAL   B 2 237 ? -17.806 -26.945  -46.736 1.00 54.23  ? 229 VAL   B N     1 
ATOM   6699 C CA    . VAL   B 2 237 ? -16.795 -27.004  -45.692 1.00 54.52  ? 229 VAL   B CA    1 
ATOM   6700 C C     . VAL   B 2 237 ? -17.196 -28.066  -44.671 1.00 54.33  ? 229 VAL   B C     1 
ATOM   6701 O O     . VAL   B 2 237 ? -18.380 -28.354  -44.501 1.00 53.29  ? 229 VAL   B O     1 
ATOM   6702 C CB    . VAL   B 2 237 ? -16.585 -25.639  -45.008 1.00 54.07  ? 229 VAL   B CB    1 
ATOM   6703 C CG1   . VAL   B 2 237 ? -15.905 -24.642  -45.936 1.00 53.73  ? 229 VAL   B CG1   1 
ATOM   6704 C CG2   . VAL   B 2 237 ? -17.885 -25.064  -44.454 1.00 53.86  ? 229 VAL   B CG2   1 
ATOM   6705 N N     . PHE   B 2 238 ? -16.191 -28.636  -43.993 1.00 54.68  ? 230 PHE   B N     1 
ATOM   6706 C CA    . PHE   B 2 238 ? -16.431 -29.564  -42.899 1.00 54.04  ? 230 PHE   B CA    1 
ATOM   6707 C C     . PHE   B 2 238 ? -15.461 -29.253  -41.761 1.00 52.44  ? 230 PHE   B C     1 
ATOM   6708 O O     . PHE   B 2 238 ? -14.328 -28.837  -41.997 1.00 53.65  ? 230 PHE   B O     1 
ATOM   6709 C CB    . PHE   B 2 238 ? -16.313 -31.023  -43.357 1.00 53.73  ? 230 PHE   B CB    1 
ATOM   6710 C CG    . PHE   B 2 238 ? -14.889 -31.524  -43.565 1.00 54.37  ? 230 PHE   B CG    1 
ATOM   6711 C CD1   . PHE   B 2 238 ? -14.245 -31.362  -44.788 1.00 53.91  ? 230 PHE   B CD1   1 
ATOM   6712 C CD2   . PHE   B 2 238 ? -14.197 -32.157  -42.536 1.00 54.79  ? 230 PHE   B CD2   1 
ATOM   6713 C CE1   . PHE   B 2 238 ? -12.948 -31.818  -44.973 1.00 53.74  ? 230 PHE   B CE1   1 
ATOM   6714 C CE2   . PHE   B 2 238 ? -12.899 -32.609  -42.726 1.00 54.52  ? 230 PHE   B CE2   1 
ATOM   6715 C CZ    . PHE   B 2 238 ? -12.277 -32.439  -43.943 1.00 54.47  ? 230 PHE   B CZ    1 
ATOM   6716 N N     . GLY   B 2 239 ? -15.936 -29.452  -40.527 1.00 49.59  ? 231 GLY   B N     1 
ATOM   6717 C CA    . GLY   B 2 239 ? -15.105 -29.349  -39.340 1.00 48.63  ? 231 GLY   B CA    1 
ATOM   6718 C C     . GLY   B 2 239 ? -14.945 -30.718  -38.689 1.00 46.85  ? 231 GLY   B C     1 
ATOM   6719 O O     . GLY   B 2 239 ? -15.858 -31.538  -38.751 1.00 45.83  ? 231 GLY   B O     1 
ATOM   6720 N N     . ASP   B 2 240 ? -13.780 -30.956  -38.075 1.00 45.79  ? 232 ASP   B N     1 
ATOM   6721 C CA    . ASP   B 2 240 ? -13.471 -32.254  -37.498 1.00 46.09  ? 232 ASP   B CA    1 
ATOM   6722 C C     . ASP   B 2 240 ? -13.534 -32.155  -35.974 1.00 46.28  ? 232 ASP   B C     1 
ATOM   6723 O O     . ASP   B 2 240 ? -13.844 -31.101  -35.424 1.00 45.87  ? 232 ASP   B O     1 
ATOM   6724 C CB    . ASP   B 2 240 ? -12.158 -32.795  -38.048 1.00 46.21  ? 232 ASP   B CB    1 
ATOM   6725 C CG    . ASP   B 2 240 ? -10.889 -32.081  -37.604 1.00 47.18  ? 232 ASP   B CG    1 
ATOM   6726 O OD1   . ASP   B 2 240 ? -10.971 -31.237  -36.688 1.00 47.26  ? 232 ASP   B OD1   1 
ATOM   6727 O OD2   . ASP   B 2 240 ? -9.822  -32.380  -38.177 1.00 48.63  ? 232 ASP   B OD2   1 
ATOM   6728 N N     . GLU   B 2 241 ? -13.245 -33.279  -35.308 1.00 47.33  ? 233 GLU   B N     1 
ATOM   6729 C CA    . GLU   B 2 241 ? -13.238 -33.365  -33.855 1.00 47.38  ? 233 GLU   B CA    1 
ATOM   6730 C C     . GLU   B 2 241 ? -11.986 -32.710  -33.271 1.00 47.11  ? 233 GLU   B C     1 
ATOM   6731 O O     . GLU   B 2 241 ? -11.935 -32.443  -32.073 1.00 46.19  ? 233 GLU   B O     1 
ATOM   6732 C CB    . GLU   B 2 241 ? -13.284 -34.829  -33.420 1.00 48.04  ? 233 GLU   B CB    1 
ATOM   6733 C CG    . GLU   B 2 241 ? -12.047 -35.615  -33.848 1.00 49.21  ? 233 GLU   B CG    1 
ATOM   6734 C CD    . GLU   B 2 241 ? -12.128 -37.113  -33.634 1.00 49.47  ? 233 GLU   B CD    1 
ATOM   6735 O OE1   . GLU   B 2 241 ? -13.011 -37.564  -32.873 1.00 48.89  ? 233 GLU   B OE1   1 
ATOM   6736 O OE2   . GLU   B 2 241 ? -11.316 -37.827  -34.261 1.00 50.55  ? 233 GLU   B OE2   1 
ATOM   6737 N N     . ASN   B 2 242 ? -10.978 -32.471  -34.119 1.00 48.24  ? 234 ASN   B N     1 
ATOM   6738 C CA    . ASN   B 2 242 ? -9.704  -31.924  -33.681 1.00 48.69  ? 234 ASN   B CA    1 
ATOM   6739 C C     . ASN   B 2 242 ? -9.708  -30.396  -33.748 1.00 48.61  ? 234 ASN   B C     1 
ATOM   6740 O O     . ASN   B 2 242 ? -8.699  -29.768  -33.436 1.00 47.81  ? 234 ASN   B O     1 
ATOM   6741 C CB    . ASN   B 2 242 ? -8.554  -32.487  -34.510 1.00 49.25  ? 234 ASN   B CB    1 
ATOM   6742 C CG    . ASN   B 2 242 ? -7.237  -32.451  -33.771 1.00 49.39  ? 234 ASN   B CG    1 
ATOM   6743 O OD1   . ASN   B 2 242 ? -7.203  -32.198  -32.561 1.00 50.51  ? 234 ASN   B OD1   1 
ATOM   6744 N ND2   . ASN   B 2 242 ? -6.146  -32.721  -34.471 1.00 49.44  ? 234 ASN   B ND2   1 
ATOM   6745 N N     . GLY   B 2 243 ? -10.834 -29.803  -34.169 1.00 49.31  ? 235 GLY   B N     1 
ATOM   6746 C CA    . GLY   B 2 243 ? -10.985 -28.356  -34.189 1.00 50.07  ? 235 GLY   B CA    1 
ATOM   6747 C C     . GLY   B 2 243 ? -10.374 -27.725  -35.439 1.00 50.55  ? 235 GLY   B C     1 
ATOM   6748 O O     . GLY   B 2 243 ? -9.978  -26.561  -35.416 1.00 50.24  ? 235 GLY   B O     1 
ATOM   6749 N N     . THR   B 2 244 ? -10.308 -28.504  -36.525 1.00 51.19  ? 236 THR   B N     1 
ATOM   6750 C CA    . THR   B 2 244 ? -9.827  -28.021  -37.808 1.00 51.52  ? 236 THR   B CA    1 
ATOM   6751 C C     . THR   B 2 244 ? -11.027 -27.819  -38.728 1.00 52.44  ? 236 THR   B C     1 
ATOM   6752 O O     . THR   B 2 244 ? -11.897 -28.683  -38.807 1.00 51.46  ? 236 THR   B O     1 
ATOM   6753 C CB    . THR   B 2 244 ? -8.832  -29.020  -38.398 1.00 50.87  ? 236 THR   B CB    1 
ATOM   6754 O OG1   . THR   B 2 244 ? -7.736  -29.041  -37.491 1.00 50.70  ? 236 THR   B OG1   1 
ATOM   6755 C CG2   . THR   B 2 244 ? -8.344  -28.629  -39.782 1.00 50.81  ? 236 THR   B CG2   1 
ATOM   6756 N N     . VAL   B 2 245 ? -11.055 -26.670  -39.414 1.00 53.42  ? 237 VAL   B N     1 
ATOM   6757 C CA    . VAL   B 2 245 ? -12.042 -26.414  -40.451 1.00 54.23  ? 237 VAL   B CA    1 
ATOM   6758 C C     . VAL   B 2 245 ? -11.365 -26.628  -41.801 1.00 53.90  ? 237 VAL   B C     1 
ATOM   6759 O O     . VAL   B 2 245 ? -10.211 -26.245  -41.989 1.00 53.03  ? 237 VAL   B O     1 
ATOM   6760 C CB    . VAL   B 2 245 ? -12.654 -25.004  -40.352 1.00 54.66  ? 237 VAL   B CB    1 
ATOM   6761 C CG1   . VAL   B 2 245 ? -13.778 -24.807  -41.363 1.00 54.82  ? 237 VAL   B CG1   1 
ATOM   6762 C CG2   . VAL   B 2 245 ? -13.150 -24.700  -38.943 1.00 55.16  ? 237 VAL   B CG2   1 
ATOM   6763 N N     . SER   B 2 246 ? -12.101 -27.246  -42.731 1.00 53.68  ? 238 SER   B N     1 
ATOM   6764 C CA    . SER   B 2 246 ? -11.565 -27.597  -44.035 1.00 55.16  ? 238 SER   B CA    1 
ATOM   6765 C C     . SER   B 2 246 ? -12.518 -27.148  -45.139 1.00 56.41  ? 238 SER   B C     1 
ATOM   6766 O O     . SER   B 2 246 ? -13.731 -27.097  -44.946 1.00 55.19  ? 238 SER   B O     1 
ATOM   6767 C CB    . SER   B 2 246 ? -11.274 -29.072  -44.119 1.00 54.35  ? 238 SER   B CB    1 
ATOM   6768 O OG    . SER   B 2 246 ? -10.077 -29.390  -43.424 1.00 53.65  ? 238 SER   B OG    1 
ATOM   6769 N N     . LEU   B 2 247 ? -11.928 -26.834  -46.298 1.00 58.56  ? 239 LEU   B N     1 
ATOM   6770 C CA    . LEU   B 2 247 ? -12.637 -26.318  -47.457 1.00 60.07  ? 239 LEU   B CA    1 
ATOM   6771 C C     . LEU   B 2 247 ? -12.426 -27.282  -48.621 1.00 59.19  ? 239 LEU   B C     1 
ATOM   6772 O O     . LEU   B 2 247 ? -11.289 -27.632  -48.928 1.00 57.04  ? 239 LEU   B O     1 
ATOM   6773 C CB    . LEU   B 2 247 ? -12.073 -24.923  -47.727 1.00 61.63  ? 239 LEU   B CB    1 
ATOM   6774 C CG    . LEU   B 2 247 ? -12.399 -24.282  -49.080 1.00 64.09  ? 239 LEU   B CG    1 
ATOM   6775 C CD1   . LEU   B 2 247 ? -13.891 -24.137  -49.329 1.00 64.25  ? 239 LEU   B CD1   1 
ATOM   6776 C CD2   . LEU   B 2 247 ? -11.708 -22.929  -49.151 1.00 64.96  ? 239 LEU   B CD2   1 
ATOM   6777 N N     . VAL   B 2 248 ? -13.527 -27.714  -49.252 1.00 60.37  ? 240 VAL   B N     1 
ATOM   6778 C CA    . VAL   B 2 248 ? -13.478 -28.826  -50.188 1.00 63.63  ? 240 VAL   B CA    1 
ATOM   6779 C C     . VAL   B 2 248 ? -14.245 -28.472  -51.460 1.00 66.96  ? 240 VAL   B C     1 
ATOM   6780 O O     . VAL   B 2 248 ? -15.303 -27.847  -51.404 1.00 65.52  ? 240 VAL   B O     1 
ATOM   6781 C CB    . VAL   B 2 248 ? -14.038 -30.122  -49.566 1.00 62.92  ? 240 VAL   B CB    1 
ATOM   6782 C CG1   . VAL   B 2 248 ? -13.563 -31.355  -50.326 1.00 62.17  ? 240 VAL   B CG1   1 
ATOM   6783 C CG2   . VAL   B 2 248 ? -13.691 -30.249  -48.087 1.00 63.20  ? 240 VAL   B CG2   1 
ATOM   6784 N N     . ASP   B 2 249 ? -13.688 -28.904  -52.599 1.00 72.26  ? 241 ASP   B N     1 
ATOM   6785 C CA    . ASP   B 2 249 ? -14.351 -28.854  -53.892 1.00 75.94  ? 241 ASP   B CA    1 
ATOM   6786 C C     . ASP   B 2 249 ? -14.790 -30.275  -54.244 1.00 76.91  ? 241 ASP   B C     1 
ATOM   6787 O O     . ASP   B 2 249 ? -13.972 -31.192  -54.222 1.00 75.72  ? 241 ASP   B O     1 
ATOM   6788 C CB    . ASP   B 2 249 ? -13.428 -28.240  -54.935 1.00 77.67  ? 241 ASP   B CB    1 
ATOM   6789 C CG    . ASP   B 2 249 ? -13.992 -28.085  -56.341 1.00 79.24  ? 241 ASP   B CG    1 
ATOM   6790 O OD1   . ASP   B 2 249 ? -15.175 -28.432  -56.551 1.00 81.11  ? 241 ASP   B OD1   1 
ATOM   6791 O OD2   . ASP   B 2 249 ? -13.238 -27.618  -57.220 1.00 79.37  ? 241 ASP   B OD2   1 
ATOM   6792 N N     . THR   B 2 250 ? -16.081 -30.448  -54.562 1.00 79.73  ? 242 THR   B N     1 
ATOM   6793 C CA    . THR   B 2 250 ? -16.654 -31.772  -54.764 1.00 82.58  ? 242 THR   B CA    1 
ATOM   6794 C C     . THR   B 2 250 ? -15.981 -32.459  -55.951 1.00 87.68  ? 242 THR   B C     1 
ATOM   6795 O O     . THR   B 2 250 ? -15.632 -33.633  -55.859 1.00 87.87  ? 242 THR   B O     1 
ATOM   6796 C CB    . THR   B 2 250 ? -18.168 -31.699  -54.963 1.00 81.77  ? 242 THR   B CB    1 
ATOM   6797 O OG1   . THR   B 2 250 ? -18.391 -30.825  -56.065 1.00 82.70  ? 242 THR   B OG1   1 
ATOM   6798 C CG2   . THR   B 2 250 ? -18.902 -31.207  -53.728 1.00 82.33  ? 242 THR   B CG2   1 
ATOM   6799 N N     . LYS   B 2 251 ? -15.819 -31.731  -57.063 1.00 93.28  ? 243 LYS   B N     1 
ATOM   6800 C CA    . LYS   B 2 251 ? -15.212 -32.290  -58.262 1.00 97.69  ? 243 LYS   B CA    1 
ATOM   6801 C C     . LYS   B 2 251 ? -13.802 -32.786  -57.947 1.00 99.76  ? 243 LYS   B C     1 
ATOM   6802 O O     . LYS   B 2 251 ? -13.438 -33.900  -58.317 1.00 99.73  ? 243 LYS   B O     1 
ATOM   6803 C CB    . LYS   B 2 251 ? -15.152 -31.278  -59.412 1.00 98.88  ? 243 LYS   B CB    1 
ATOM   6804 C CG    . LYS   B 2 251 ? -16.484 -30.948  -60.069 1.00 100.60 ? 243 LYS   B CG    1 
ATOM   6805 C CD    . LYS   B 2 251 ? -16.338 -30.065  -61.303 1.00 103.25 ? 243 LYS   B CD    1 
ATOM   6806 C CE    . LYS   B 2 251 ? -17.643 -29.761  -61.968 1.00 103.72 ? 243 LYS   B CE    1 
ATOM   6807 N NZ    . LYS   B 2 251 ? -17.462 -28.892  -63.134 1.00 103.46 ? 243 LYS   B NZ    1 
ATOM   6808 N N     . SER   B 2 252 ? -13.021 -31.943  -57.260 1.00 101.87 ? 244 SER   B N     1 
ATOM   6809 C CA    . SER   B 2 252 ? -11.637 -32.251  -56.940 1.00 104.02 ? 244 SER   B CA    1 
ATOM   6810 C C     . SER   B 2 252 ? -11.557 -33.414  -55.951 1.00 108.57 ? 244 SER   B C     1 
ATOM   6811 O O     . SER   B 2 252 ? -10.759 -34.329  -56.142 1.00 111.86 ? 244 SER   B O     1 
ATOM   6812 C CB    . SER   B 2 252 ? -10.926 -31.034  -56.399 1.00 102.27 ? 244 SER   B CB    1 
ATOM   6813 O OG    . SER   B 2 252 ? -11.060 -29.929  -57.282 1.00 100.80 ? 244 SER   B OG    1 
ATOM   6814 N N     . THR   B 2 253 ? -12.392 -33.361  -54.903 1.00 110.78 ? 245 THR   B N     1 
ATOM   6815 C CA    . THR   B 2 253 ? -12.274 -34.221  -53.732 1.00 111.01 ? 245 THR   B CA    1 
ATOM   6816 C C     . THR   B 2 253 ? -10.871 -34.076  -53.138 1.00 111.39 ? 245 THR   B C     1 
ATOM   6817 O O     . THR   B 2 253 ? -10.330 -35.027  -52.575 1.00 110.92 ? 245 THR   B O     1 
ATOM   6818 C CB    . THR   B 2 253 ? -12.604 -35.679  -54.067 1.00 111.22 ? 245 THR   B CB    1 
ATOM   6819 O OG1   . THR   B 2 253 ? -11.482 -36.244  -54.738 1.00 115.37 ? 245 THR   B OG1   1 
ATOM   6820 C CG2   . THR   B 2 253 ? -13.846 -35.826  -54.930 1.00 108.81 ? 245 THR   B CG2   1 
ATOM   6821 N N     . SER   B 2 254 ? -10.298 -32.870  -53.272 1.00 111.35 ? 246 SER   B N     1 
ATOM   6822 C CA    . SER   B 2 254 ? -9.000  -32.532  -52.710 1.00 108.86 ? 246 SER   B CA    1 
ATOM   6823 C C     . SER   B 2 254 ? -9.175  -31.335  -51.781 1.00 107.49 ? 246 SER   B C     1 
ATOM   6824 O O     . SER   B 2 254 ? -9.801  -30.347  -52.163 1.00 108.20 ? 246 SER   B O     1 
ATOM   6825 C CB    . SER   B 2 254 ? -7.988  -32.226  -53.789 1.00 106.91 ? 246 SER   B CB    1 
ATOM   6826 O OG    . SER   B 2 254 ? -7.963  -33.240  -54.785 1.00 106.26 ? 246 SER   B OG    1 
ATOM   6827 N N     . CYS   B 2 255 ? -8.625  -31.435  -50.566 1.00 104.65 ? 247 CYS   B N     1 
ATOM   6828 C CA    . CYS   B 2 255 ? -8.760  -30.375  -49.581 1.00 101.49 ? 247 CYS   B CA    1 
ATOM   6829 C C     . CYS   B 2 255 ? -8.062  -29.117  -50.089 1.00 98.53  ? 247 CYS   B C     1 
ATOM   6830 O O     . CYS   B 2 255 ? -6.845  -29.105  -50.260 1.00 96.92  ? 247 CYS   B O     1 
ATOM   6831 C CB    . CYS   B 2 255 ? -8.192  -30.788  -48.229 1.00 101.46 ? 247 CYS   B CB    1 
ATOM   6832 S SG    . CYS   B 2 255 ? -8.231  -29.453  -47.005 1.00 104.90 ? 247 CYS   B SG    1 
ATOM   6833 N N     . VAL   B 2 256 ? -8.858  -28.068  -50.327 1.00 96.63  ? 248 VAL   B N     1 
ATOM   6834 C CA    . VAL   B 2 256 ? -8.354  -26.817  -50.869 1.00 93.37  ? 248 VAL   B CA    1 
ATOM   6835 C C     . VAL   B 2 256 ? -7.513  -26.140  -49.787 1.00 88.70  ? 248 VAL   B C     1 
ATOM   6836 O O     . VAL   B 2 256 ? -6.383  -25.733  -50.048 1.00 88.86  ? 248 VAL   B O     1 
ATOM   6837 C CB    . VAL   B 2 256 ? -9.471  -25.880  -51.378 1.00 92.34  ? 248 VAL   B CB    1 
ATOM   6838 C CG1   . VAL   B 2 256 ? -8.907  -24.684  -52.138 1.00 91.82  ? 248 VAL   B CG1   1 
ATOM   6839 C CG2   . VAL   B 2 256 ? -10.494 -26.607  -52.246 1.00 90.61  ? 248 VAL   B CG2   1 
ATOM   6840 N N     . LEU   B 2 257 ? -8.070  -26.043  -48.573 1.00 83.02  ? 249 LEU   B N     1 
ATOM   6841 C CA    . LEU   B 2 257 ? -7.402  -25.359  -47.477 1.00 79.81  ? 249 LEU   B CA    1 
ATOM   6842 C C     . LEU   B 2 257 ? -7.899  -25.895  -46.134 1.00 74.01  ? 249 LEU   B C     1 
ATOM   6843 O O     . LEU   B 2 257 ? -9.051  -26.306  -46.012 1.00 71.88  ? 249 LEU   B O     1 
ATOM   6844 C CB    . LEU   B 2 257 ? -7.654  -23.859  -47.622 1.00 80.83  ? 249 LEU   B CB    1 
ATOM   6845 C CG    . LEU   B 2 257 ? -6.976  -22.945  -46.595 1.00 82.90  ? 249 LEU   B CG    1 
ATOM   6846 C CD1   . LEU   B 2 257 ? -5.459  -23.065  -46.611 1.00 82.79  ? 249 LEU   B CD1   1 
ATOM   6847 C CD2   . LEU   B 2 257 ? -7.392  -21.505  -46.840 1.00 83.01  ? 249 LEU   B CD2   1 
ATOM   6848 N N     . SER   B 2 258 ? -7.002  -25.879  -45.139 1.00 69.52  ? 250 SER   B N     1 
ATOM   6849 C CA    . SER   B 2 258 ? -7.309  -26.274  -43.773 1.00 66.32  ? 250 SER   B CA    1 
ATOM   6850 C C     . SER   B 2 258 ? -6.765  -25.231  -42.801 1.00 64.30  ? 250 SER   B C     1 
ATOM   6851 O O     . SER   B 2 258 ? -5.754  -24.589  -43.079 1.00 64.53  ? 250 SER   B O     1 
ATOM   6852 C CB    . SER   B 2 258 ? -6.745  -27.637  -43.457 1.00 65.60  ? 250 SER   B CB    1 
ATOM   6853 O OG    . SER   B 2 258 ? -7.512  -28.665  -44.067 1.00 65.68  ? 250 SER   B OG    1 
ATOM   6854 N N     . SER   B 2 259 ? -7.447  -25.077  -41.660 1.00 61.17  ? 251 SER   B N     1 
ATOM   6855 C CA    . SER   B 2 259 ? -6.999  -24.178  -40.608 1.00 58.68  ? 251 SER   B CA    1 
ATOM   6856 C C     . SER   B 2 259 ? -7.369  -24.747  -39.241 1.00 56.51  ? 251 SER   B C     1 
ATOM   6857 O O     . SER   B 2 259 ? -8.487  -25.220  -39.046 1.00 55.71  ? 251 SER   B O     1 
ATOM   6858 C CB    . SER   B 2 259 ? -7.574  -22.799  -40.789 1.00 58.03  ? 251 SER   B CB    1 
ATOM   6859 O OG    . SER   B 2 259 ? -7.097  -21.916  -39.783 1.00 58.81  ? 251 SER   B OG    1 
ATOM   6860 N N     . ALA   B 2 260 ? -6.412  -24.690  -38.307 1.00 53.95  ? 252 ALA   B N     1 
ATOM   6861 C CA    . ALA   B 2 260 ? -6.660  -25.023  -36.915 1.00 52.91  ? 252 ALA   B CA    1 
ATOM   6862 C C     . ALA   B 2 260 ? -7.312  -23.824  -36.231 1.00 53.98  ? 252 ALA   B C     1 
ATOM   6863 O O     . ALA   B 2 260 ? -6.622  -22.935  -35.736 1.00 55.58  ? 252 ALA   B O     1 
ATOM   6864 C CB    . ALA   B 2 260 ? -5.366  -25.417  -36.240 1.00 52.19  ? 252 ALA   B CB    1 
ATOM   6865 N N     . VAL   B 2 261 ? -8.650  -23.813  -36.223 1.00 54.43  ? 253 VAL   B N     1 
ATOM   6866 C CA    . VAL   B 2 261 ? -9.422  -22.665  -35.774 1.00 55.28  ? 253 VAL   B CA    1 
ATOM   6867 C C     . VAL   B 2 261 ? -9.820  -22.843  -34.311 1.00 56.05  ? 253 VAL   B C     1 
ATOM   6868 O O     . VAL   B 2 261 ? -9.765  -21.886  -33.540 1.00 58.08  ? 253 VAL   B O     1 
ATOM   6869 C CB    . VAL   B 2 261 ? -10.647 -22.469  -36.690 1.00 55.92  ? 253 VAL   B CB    1 
ATOM   6870 C CG1   . VAL   B 2 261 ? -11.651 -21.469  -36.124 1.00 55.55  ? 253 VAL   B CG1   1 
ATOM   6871 C CG2   . VAL   B 2 261 ? -10.224 -22.061  -38.097 1.00 55.81  ? 253 VAL   B CG2   1 
ATOM   6872 N N     . HIS   B 2 262 ? -10.231 -24.062  -33.940 1.00 54.78  ? 254 HIS   B N     1 
ATOM   6873 C CA    . HIS   B 2 262 ? -10.689 -24.343  -32.589 1.00 52.84  ? 254 HIS   B CA    1 
ATOM   6874 C C     . HIS   B 2 262 ? -9.735  -25.317  -31.902 1.00 52.45  ? 254 HIS   B C     1 
ATOM   6875 O O     . HIS   B 2 262 ? -9.025  -26.075  -32.559 1.00 53.00  ? 254 HIS   B O     1 
ATOM   6876 C CB    . HIS   B 2 262 ? -12.136 -24.844  -32.615 1.00 52.31  ? 254 HIS   B CB    1 
ATOM   6877 C CG    . HIS   B 2 262 ? -13.117 -23.802  -33.039 1.00 52.06  ? 254 HIS   B CG    1 
ATOM   6878 N ND1   . HIS   B 2 262 ? -13.437 -22.726  -32.240 1.00 51.59  ? 254 HIS   B ND1   1 
ATOM   6879 C CD2   . HIS   B 2 262 ? -13.835 -23.657  -34.161 1.00 51.64  ? 254 HIS   B CD2   1 
ATOM   6880 C CE1   . HIS   B 2 262 ? -14.326 -21.967  -32.864 1.00 51.40  ? 254 HIS   B CE1   1 
ATOM   6881 N NE2   . HIS   B 2 262 ? -14.584 -22.516  -34.031 1.00 51.59  ? 254 HIS   B NE2   1 
ATOM   6882 N N     . SER   B 2 263 ? -9.742  -25.278  -30.563 1.00 51.94  ? 255 SER   B N     1 
ATOM   6883 C CA    . SER   B 2 263 ? -8.905  -26.137  -29.742 1.00 51.68  ? 255 SER   B CA    1 
ATOM   6884 C C     . SER   B 2 263 ? -9.674  -27.398  -29.360 1.00 50.74  ? 255 SER   B C     1 
ATOM   6885 O O     . SER   B 2 263 ? -9.189  -28.207  -28.572 1.00 50.45  ? 255 SER   B O     1 
ATOM   6886 C CB    . SER   B 2 263 ? -8.434  -25.411  -28.510 1.00 52.31  ? 255 SER   B CB    1 
ATOM   6887 O OG    . SER   B 2 263 ? -9.527  -25.115  -27.650 1.00 52.41  ? 255 SER   B OG    1 
ATOM   6888 N N     . GLN   B 2 264 ? -10.887 -27.529  -29.910 1.00 48.81  ? 256 GLN   B N     1 
ATOM   6889 C CA    . GLN   B 2 264 ? -11.745 -28.671  -29.661 1.00 46.18  ? 256 GLN   B CA    1 
ATOM   6890 C C     . GLN   B 2 264 ? -12.702 -28.834  -30.838 1.00 45.41  ? 256 GLN   B C     1 
ATOM   6891 O O     . GLN   B 2 264 ? -12.771 -27.978  -31.716 1.00 44.89  ? 256 GLN   B O     1 
ATOM   6892 C CB    . GLN   B 2 264 ? -12.526 -28.529  -28.351 1.00 45.62  ? 256 GLN   B CB    1 
ATOM   6893 C CG    . GLN   B 2 264 ? -11.667 -28.633  -27.095 1.00 45.50  ? 256 GLN   B CG    1 
ATOM   6894 C CD    . GLN   B 2 264 ? -12.467 -28.937  -25.847 1.00 45.73  ? 256 GLN   B CD    1 
ATOM   6895 O OE1   . GLN   B 2 264 ? -13.158 -29.958  -25.763 1.00 45.70  ? 256 GLN   B OE1   1 
ATOM   6896 N NE2   . GLN   B 2 264 ? -12.376 -28.059  -24.858 1.00 45.26  ? 256 GLN   B NE2   1 
ATOM   6897 N N     A CYS   B 2 265 ? -13.419 -29.960  -30.824 0.50 45.49  ? 257 CYS   B N     1 
ATOM   6898 N N     B CYS   B 2 265 ? -13.421 -29.963  -30.825 0.50 45.57  ? 257 CYS   B N     1 
ATOM   6899 C CA    A CYS   B 2 265 ? -14.450 -30.318  -31.785 0.50 45.58  ? 257 CYS   B CA    1 
ATOM   6900 C CA    B CYS   B 2 265 ? -14.429 -30.329  -31.807 0.50 45.72  ? 257 CYS   B CA    1 
ATOM   6901 C C     A CYS   B 2 265 ? -15.160 -29.101  -32.376 0.50 45.57  ? 257 CYS   B C     1 
ATOM   6902 C C     B CYS   B 2 265 ? -15.173 -29.120  -32.373 0.50 45.63  ? 257 CYS   B C     1 
ATOM   6903 O O     A CYS   B 2 265 ? -15.490 -28.162  -31.657 0.50 46.04  ? 257 CYS   B O     1 
ATOM   6904 O O     B CYS   B 2 265 ? -15.538 -28.209  -31.635 0.50 46.03  ? 257 CYS   B O     1 
ATOM   6905 C CB    A CYS   B 2 265 ? -15.491 -31.181  -31.085 0.50 45.79  ? 257 CYS   B CB    1 
ATOM   6906 C CB    B CYS   B 2 265 ? -15.443 -31.269  -31.167 0.50 46.07  ? 257 CYS   B CB    1 
ATOM   6907 S SG    A CYS   B 2 265 ? -16.711 -31.909  -32.207 0.50 47.06  ? 257 CYS   B SG    1 
ATOM   6908 S SG    B CYS   B 2 265 ? -17.004 -31.381  -32.078 0.50 47.53  ? 257 CYS   B SG    1 
ATOM   6909 N N     . VAL   B 2 266 ? -15.417 -29.155  -33.691 1.00 45.29  ? 258 VAL   B N     1 
ATOM   6910 C CA    . VAL   B 2 266 ? -16.218 -28.156  -34.383 1.00 44.16  ? 258 VAL   B CA    1 
ATOM   6911 C C     . VAL   B 2 266 ? -17.669 -28.635  -34.398 1.00 44.54  ? 258 VAL   B C     1 
ATOM   6912 O O     . VAL   B 2 266 ? -17.970 -29.672  -34.982 1.00 45.85  ? 258 VAL   B O     1 
ATOM   6913 C CB    . VAL   B 2 266 ? -15.690 -27.938  -35.814 1.00 43.71  ? 258 VAL   B CB    1 
ATOM   6914 C CG1   . VAL   B 2 266 ? -16.524 -26.919  -36.584 1.00 44.47  ? 258 VAL   B CG1   1 
ATOM   6915 C CG2   . VAL   B 2 266 ? -14.220 -27.537  -35.822 1.00 43.27  ? 258 VAL   B CG2   1 
ATOM   6916 N N     . THR   B 2 267 ? -18.566 -27.861  -33.774 1.00 44.51  ? 259 THR   B N     1 
ATOM   6917 C CA    . THR   B 2 267 ? -19.944 -28.280  -33.569 1.00 44.44  ? 259 THR   B CA    1 
ATOM   6918 C C     . THR   B 2 267 ? -20.817 -27.847  -34.746 1.00 44.06  ? 259 THR   B C     1 
ATOM   6919 O O     . THR   B 2 267 ? -21.727 -28.575  -35.135 1.00 43.70  ? 259 THR   B O     1 
ATOM   6920 C CB    . THR   B 2 267 ? -20.465 -27.697  -32.255 1.00 45.23  ? 259 THR   B CB    1 
ATOM   6921 O OG1   . THR   B 2 267 ? -19.528 -28.086  -31.256 1.00 45.32  ? 259 THR   B OG1   1 
ATOM   6922 C CG2   . THR   B 2 267 ? -21.852 -28.206  -31.903 1.00 45.16  ? 259 THR   B CG2   1 
ATOM   6923 N N     . GLY   B 2 268 ? -20.554 -26.651  -35.287 1.00 44.21  ? 260 GLY   B N     1 
ATOM   6924 C CA    . GLY   B 2 268 ? -21.396 -26.079  -36.325 1.00 44.99  ? 260 GLY   B CA    1 
ATOM   6925 C C     . GLY   B 2 268 ? -20.618 -25.128  -37.231 1.00 45.90  ? 260 GLY   B C     1 
ATOM   6926 O O     . GLY   B 2 268 ? -19.618 -24.542  -36.818 1.00 46.39  ? 260 GLY   B O     1 
ATOM   6927 N N     . LEU   B 2 269 ? -21.102 -24.991  -38.472 1.00 46.37  ? 261 LEU   B N     1 
ATOM   6928 C CA    . LEU   B 2 269 ? -20.535 -24.083  -39.456 1.00 47.46  ? 261 LEU   B CA    1 
ATOM   6929 C C     . LEU   B 2 269 ? -21.678 -23.383  -40.186 1.00 48.47  ? 261 LEU   B C     1 
ATOM   6930 O O     . LEU   B 2 269 ? -22.583 -24.048  -40.689 1.00 46.30  ? 261 LEU   B O     1 
ATOM   6931 C CB    . LEU   B 2 269 ? -19.658 -24.871  -40.429 1.00 47.26  ? 261 LEU   B CB    1 
ATOM   6932 C CG    . LEU   B 2 269 ? -18.396 -25.514  -39.846 1.00 46.46  ? 261 LEU   B CG    1 
ATOM   6933 C CD1   . LEU   B 2 269 ? -17.773 -26.457  -40.859 1.00 46.78  ? 261 LEU   B CD1   1 
ATOM   6934 C CD2   . LEU   B 2 269 ? -17.387 -24.467  -39.409 1.00 46.26  ? 261 LEU   B CD2   1 
ATOM   6935 N N     . VAL   B 2 270 ? -21.637 -22.045  -40.233 1.00 50.34  ? 262 VAL   B N     1 
ATOM   6936 C CA    . VAL   B 2 270 ? -22.713 -21.271  -40.837 1.00 51.64  ? 262 VAL   B CA    1 
ATOM   6937 C C     . VAL   B 2 270 ? -22.111 -20.143  -41.673 1.00 51.86  ? 262 VAL   B C     1 
ATOM   6938 O O     . VAL   B 2 270 ? -21.270 -19.384  -41.190 1.00 50.87  ? 262 VAL   B O     1 
ATOM   6939 C CB    . VAL   B 2 270 ? -23.697 -20.718  -39.785 1.00 51.80  ? 262 VAL   B CB    1 
ATOM   6940 C CG1   . VAL   B 2 270 ? -24.908 -20.058  -40.432 1.00 51.23  ? 262 VAL   B CG1   1 
ATOM   6941 C CG2   . VAL   B 2 270 ? -24.152 -21.794  -38.805 1.00 52.38  ? 262 VAL   B CG2   1 
ATOM   6942 N N     . PHE   B 2 271 ? -22.566 -20.043  -42.929 1.00 52.89  ? 263 PHE   B N     1 
ATOM   6943 C CA    . PHE   B 2 271 ? -22.158 -18.971  -43.823 1.00 52.71  ? 263 PHE   B CA    1 
ATOM   6944 C C     . PHE   B 2 271 ? -23.089 -17.775  -43.633 1.00 54.48  ? 263 PHE   B C     1 
ATOM   6945 O O     . PHE   B 2 271 ? -24.275 -17.948  -43.359 1.00 52.05  ? 263 PHE   B O     1 
ATOM   6946 C CB    . PHE   B 2 271 ? -22.150 -19.436  -45.282 1.00 50.40  ? 263 PHE   B CB    1 
ATOM   6947 C CG    . PHE   B 2 271 ? -20.947 -20.281  -45.677 1.00 48.39  ? 263 PHE   B CG    1 
ATOM   6948 C CD1   . PHE   B 2 271 ? -19.708 -19.690  -45.906 1.00 47.55  ? 263 PHE   B CD1   1 
ATOM   6949 C CD2   . PHE   B 2 271 ? -21.062 -21.658  -45.841 1.00 47.52  ? 263 PHE   B CD2   1 
ATOM   6950 C CE1   . PHE   B 2 271 ? -18.612 -20.458  -46.275 1.00 47.68  ? 263 PHE   B CE1   1 
ATOM   6951 C CE2   . PHE   B 2 271 ? -19.964 -22.422  -46.211 1.00 47.21  ? 263 PHE   B CE2   1 
ATOM   6952 C CZ    . PHE   B 2 271 ? -18.742 -21.822  -46.426 1.00 47.10  ? 263 PHE   B CZ    1 
ATOM   6953 N N     . SER   B 2 272 ? -22.536 -16.566  -43.805 1.00 58.58  ? 264 SER   B N     1 
ATOM   6954 C CA    . SER   B 2 272 ? -23.291 -15.334  -43.634 1.00 61.44  ? 264 SER   B CA    1 
ATOM   6955 C C     . SER   B 2 272 ? -24.172 -15.081  -44.855 1.00 63.09  ? 264 SER   B C     1 
ATOM   6956 O O     . SER   B 2 272 ? -23.962 -15.679  -45.909 1.00 62.25  ? 264 SER   B O     1 
ATOM   6957 C CB    . SER   B 2 272 ? -22.375 -14.163  -43.378 1.00 62.17  ? 264 SER   B CB    1 
ATOM   6958 O OG    . SER   B 2 272 ? -21.680 -13.798  -44.561 1.00 63.94  ? 264 SER   B OG    1 
ATOM   6959 N N     . PRO   B 2 273 ? -25.179 -14.180  -44.753 1.00 67.79  ? 265 PRO   B N     1 
ATOM   6960 C CA    . PRO   B 2 273 ? -26.064 -13.871  -45.879 1.00 69.68  ? 265 PRO   B CA    1 
ATOM   6961 C C     . PRO   B 2 273 ? -25.417 -13.092  -47.026 1.00 71.09  ? 265 PRO   B C     1 
ATOM   6962 O O     . PRO   B 2 273 ? -25.950 -13.089  -48.134 1.00 71.12  ? 265 PRO   B O     1 
ATOM   6963 C CB    . PRO   B 2 273 ? -27.204 -13.060  -45.220 1.00 69.27  ? 265 PRO   B CB    1 
ATOM   6964 C CG    . PRO   B 2 273 ? -27.035 -13.275  -43.731 1.00 69.27  ? 265 PRO   B CG    1 
ATOM   6965 C CD    . PRO   B 2 273 ? -25.542 -13.431  -43.541 1.00 69.22  ? 265 PRO   B CD    1 
ATOM   6966 N N     . HIS   B 2 274 ? -24.278 -12.434  -46.757 1.00 73.48  ? 266 HIS   B N     1 
ATOM   6967 C CA    . HIS   B 2 274 ? -23.603 -11.597  -47.740 1.00 75.53  ? 266 HIS   B CA    1 
ATOM   6968 C C     . HIS   B 2 274 ? -23.334 -12.381  -49.024 1.00 75.99  ? 266 HIS   B C     1 
ATOM   6969 O O     . HIS   B 2 274 ? -23.160 -13.598  -48.985 1.00 76.20  ? 266 HIS   B O     1 
ATOM   6970 C CB    . HIS   B 2 274 ? -22.259 -11.070  -47.218 1.00 77.80  ? 266 HIS   B CB    1 
ATOM   6971 C CG    . HIS   B 2 274 ? -22.301 -10.339  -45.916 1.00 80.86  ? 266 HIS   B CG    1 
ATOM   6972 N ND1   . HIS   B 2 274 ? -22.863 -9.090   -45.762 1.00 84.29  ? 266 HIS   B ND1   1 
ATOM   6973 C CD2   . HIS   B 2 274 ? -21.841 -10.686  -44.706 1.00 82.52  ? 266 HIS   B CD2   1 
ATOM   6974 C CE1   . HIS   B 2 274 ? -22.737 -8.706   -44.499 1.00 85.17  ? 266 HIS   B CE1   1 
ATOM   6975 N NE2   . HIS   B 2 274 ? -22.121 -9.662   -43.840 1.00 84.90  ? 266 HIS   B NE2   1 
ATOM   6976 N N     . SER   B 2 275 ? -23.282 -11.659  -50.154 1.00 76.28  ? 267 SER   B N     1 
ATOM   6977 C CA    . SER   B 2 275 ? -22.978 -12.246  -51.452 1.00 74.12  ? 267 SER   B CA    1 
ATOM   6978 C C     . SER   B 2 275 ? -21.580 -12.860  -51.427 1.00 72.43  ? 267 SER   B C     1 
ATOM   6979 O O     . SER   B 2 275 ? -21.349 -13.903  -52.034 1.00 69.50  ? 267 SER   B O     1 
ATOM   6980 C CB    . SER   B 2 275 ? -23.097 -11.234  -52.568 1.00 72.49  ? 267 SER   B CB    1 
ATOM   6981 O OG    . SER   B 2 275 ? -24.352 -10.569  -52.537 1.00 71.82  ? 267 SER   B OG    1 
ATOM   6982 N N     . VAL   B 2 276 ? -20.650 -12.174  -50.750 1.00 72.15  ? 268 VAL   B N     1 
ATOM   6983 C CA    . VAL   B 2 276 ? -19.371 -12.753  -50.373 1.00 72.27  ? 268 VAL   B CA    1 
ATOM   6984 C C     . VAL   B 2 276 ? -19.465 -13.122  -48.893 1.00 72.67  ? 268 VAL   B C     1 
ATOM   6985 O O     . VAL   B 2 276 ? -19.295 -12.260  -48.032 1.00 73.97  ? 268 VAL   B O     1 
ATOM   6986 C CB    . VAL   B 2 276 ? -18.186 -11.803  -50.640 1.00 71.72  ? 268 VAL   B CB    1 
ATOM   6987 C CG1   . VAL   B 2 276 ? -16.849 -12.523  -50.496 1.00 70.91  ? 268 VAL   B CG1   1 
ATOM   6988 C CG2   . VAL   B 2 276 ? -18.288 -11.135  -52.006 1.00 71.52  ? 268 VAL   B CG2   1 
ATOM   6989 N N     . PRO   B 2 277 ? -19.736 -14.404  -48.545 1.00 70.14  ? 269 PRO   B N     1 
ATOM   6990 C CA    . PRO   B 2 277 ? -20.166 -14.754  -47.191 1.00 68.35  ? 269 PRO   B CA    1 
ATOM   6991 C C     . PRO   B 2 277 ? -19.042 -15.029  -46.193 1.00 65.74  ? 269 PRO   B C     1 
ATOM   6992 O O     . PRO   B 2 277 ? -17.959 -15.472  -46.572 1.00 65.55  ? 269 PRO   B O     1 
ATOM   6993 C CB    . PRO   B 2 277 ? -21.014 -16.006  -47.482 1.00 68.62  ? 269 PRO   B CB    1 
ATOM   6994 C CG    . PRO   B 2 277 ? -20.278 -16.697  -48.613 1.00 69.03  ? 269 PRO   B CG    1 
ATOM   6995 C CD    . PRO   B 2 277 ? -19.622 -15.583  -49.419 1.00 69.22  ? 269 PRO   B CD    1 
ATOM   6996 N N     . PHE   B 2 278 ? -19.321 -14.739  -44.916 1.00 63.21  ? 270 PHE   B N     1 
ATOM   6997 C CA    . PHE   B 2 278 ? -18.456 -15.106  -43.807 1.00 61.08  ? 270 PHE   B CA    1 
ATOM   6998 C C     . PHE   B 2 278 ? -18.810 -16.514  -43.342 1.00 57.72  ? 270 PHE   B C     1 
ATOM   6999 O O     . PHE   B 2 278 ? -19.934 -16.963  -43.544 1.00 55.13  ? 270 PHE   B O     1 
ATOM   7000 C CB    . PHE   B 2 278 ? -18.637 -14.133  -42.639 1.00 62.70  ? 270 PHE   B CB    1 
ATOM   7001 C CG    . PHE   B 2 278 ? -18.175 -12.709  -42.907 1.00 64.77  ? 270 PHE   B CG    1 
ATOM   7002 C CD1   . PHE   B 2 278 ? -16.938 -12.459  -43.493 1.00 65.10  ? 270 PHE   B CD1   1 
ATOM   7003 C CD2   . PHE   B 2 278 ? -18.983 -11.624  -42.579 1.00 66.33  ? 270 PHE   B CD2   1 
ATOM   7004 C CE1   . PHE   B 2 278 ? -16.520 -11.159  -43.735 1.00 66.26  ? 270 PHE   B CE1   1 
ATOM   7005 C CE2   . PHE   B 2 278 ? -18.560 -10.326  -42.824 1.00 66.48  ? 270 PHE   B CE2   1 
ATOM   7006 C CZ    . PHE   B 2 278 ? -17.331 -10.097  -43.401 1.00 67.04  ? 270 PHE   B CZ    1 
ATOM   7007 N N     . LEU   B 2 279 ? -17.846 -17.190  -42.704 1.00 55.91  ? 271 LEU   B N     1 
ATOM   7008 C CA    . LEU   B 2 279 ? -18.087 -18.498  -42.117 1.00 54.33  ? 271 LEU   B CA    1 
ATOM   7009 C C     . LEU   B 2 279 ? -17.985 -18.389  -40.598 1.00 52.31  ? 271 LEU   B C     1 
ATOM   7010 O O     . LEU   B 2 279 ? -16.917 -18.093  -40.066 1.00 49.87  ? 271 LEU   B O     1 
ATOM   7011 C CB    . LEU   B 2 279 ? -17.110 -19.538  -42.664 1.00 54.05  ? 271 LEU   B CB    1 
ATOM   7012 C CG    . LEU   B 2 279 ? -17.352 -20.985  -42.217 1.00 53.07  ? 271 LEU   B CG    1 
ATOM   7013 C CD1   . LEU   B 2 279 ? -18.698 -21.497  -42.705 1.00 52.79  ? 271 LEU   B CD1   1 
ATOM   7014 C CD2   . LEU   B 2 279 ? -16.234 -21.900  -42.686 1.00 52.48  ? 271 LEU   B CD2   1 
ATOM   7015 N N     . ALA   B 2 280 ? -19.116 -18.626  -39.921 1.00 52.14  ? 272 ALA   B N     1 
ATOM   7016 C CA    . ALA   B 2 280 ? -19.165 -18.718  -38.470 1.00 52.70  ? 272 ALA   B CA    1 
ATOM   7017 C C     . ALA   B 2 280 ? -18.872 -20.157  -38.048 1.00 52.85  ? 272 ALA   B C     1 
ATOM   7018 O O     . ALA   B 2 280 ? -19.450 -21.086  -38.610 1.00 52.27  ? 272 ALA   B O     1 
ATOM   7019 C CB    . ALA   B 2 280 ? -20.522 -18.265  -37.976 1.00 52.22  ? 272 ALA   B CB    1 
ATOM   7020 N N     . SER   B 2 281 ? -17.982 -20.321  -37.057 1.00 53.76  ? 273 SER   B N     1 
ATOM   7021 C CA    . SER   B 2 281 ? -17.537 -21.634  -36.606 1.00 53.80  ? 273 SER   B CA    1 
ATOM   7022 C C     . SER   B 2 281 ? -17.748 -21.783  -35.099 1.00 52.65  ? 273 SER   B C     1 
ATOM   7023 O O     . SER   B 2 281 ? -17.363 -20.909  -34.326 1.00 51.21  ? 273 SER   B O     1 
ATOM   7024 C CB    . SER   B 2 281 ? -16.094 -21.876  -36.977 1.00 54.49  ? 273 SER   B CB    1 
ATOM   7025 O OG    . SER   B 2 281 ? -15.232 -20.959  -36.317 1.00 55.33  ? 273 SER   B OG    1 
ATOM   7026 N N     . LEU   B 2 282 ? -18.342 -22.921  -34.708 1.00 51.65  ? 274 LEU   B N     1 
ATOM   7027 C CA    . LEU   B 2 282 ? -18.722 -23.208  -33.333 1.00 50.04  ? 274 LEU   B CA    1 
ATOM   7028 C C     . LEU   B 2 282 ? -17.845 -24.330  -32.788 1.00 48.96  ? 274 LEU   B C     1 
ATOM   7029 O O     . LEU   B 2 282 ? -17.356 -25.157  -33.554 1.00 48.93  ? 274 LEU   B O     1 
ATOM   7030 C CB    . LEU   B 2 282 ? -20.187 -23.631  -33.297 1.00 50.09  ? 274 LEU   B CB    1 
ATOM   7031 C CG    . LEU   B 2 282 ? -21.225 -22.548  -33.598 1.00 50.52  ? 274 LEU   B CG    1 
ATOM   7032 C CD1   . LEU   B 2 282 ? -21.222 -22.062  -35.037 1.00 51.10  ? 274 LEU   B CD1   1 
ATOM   7033 C CD2   . LEU   B 2 282 ? -22.575 -23.115  -33.241 1.00 50.84  ? 274 LEU   B CD2   1 
ATOM   7034 N N     . SER   B 2 283 ? -17.691 -24.385  -31.460 1.00 47.09  ? 275 SER   B N     1 
ATOM   7035 C CA    . SER   B 2 283 ? -16.805 -25.370  -30.860 1.00 46.15  ? 275 SER   B CA    1 
ATOM   7036 C C     . SER   B 2 283 ? -17.170 -25.657  -29.406 1.00 46.22  ? 275 SER   B C     1 
ATOM   7037 O O     . SER   B 2 283 ? -17.928 -24.919  -28.779 1.00 45.67  ? 275 SER   B O     1 
ATOM   7038 C CB    . SER   B 2 283 ? -15.371 -24.928  -30.979 1.00 45.24  ? 275 SER   B CB    1 
ATOM   7039 O OG    . SER   B 2 283 ? -14.483 -25.855  -30.368 1.00 44.00  ? 275 SER   B OG    1 
ATOM   7040 N N     . GLU   B 2 284 ? -16.592 -26.755  -28.901 1.00 45.63  ? 276 GLU   B N     1 
ATOM   7041 C CA    . GLU   B 2 284 ? -16.712 -27.164  -27.512 1.00 44.99  ? 276 GLU   B CA    1 
ATOM   7042 C C     . GLU   B 2 284 ? -15.657 -26.459  -26.661 1.00 43.64  ? 276 GLU   B C     1 
ATOM   7043 O O     . GLU   B 2 284 ? -15.702 -26.540  -25.436 1.00 43.14  ? 276 GLU   B O     1 
ATOM   7044 C CB    . GLU   B 2 284 ? -16.585 -28.683  -27.416 1.00 45.00  ? 276 GLU   B CB    1 
ATOM   7045 C CG    . GLU   B 2 284 ? -17.792 -29.413  -27.996 1.00 45.59  ? 276 GLU   B CG    1 
ATOM   7046 C CD    . GLU   B 2 284 ? -17.686 -30.925  -27.975 1.00 46.58  ? 276 GLU   B CD    1 
ATOM   7047 O OE1   . GLU   B 2 284 ? -16.589 -31.448  -27.688 1.00 47.98  ? 276 GLU   B OE1   1 
ATOM   7048 O OE2   . GLU   B 2 284 ? -18.714 -31.582  -28.238 1.00 47.41  ? 276 GLU   B OE2   1 
ATOM   7049 N N     . ASP   B 2 285 ? -14.715 -25.767  -27.317 1.00 43.00  ? 277 ASP   B N     1 
ATOM   7050 C CA    . ASP   B 2 285 ? -13.798 -24.868  -26.633 1.00 43.94  ? 277 ASP   B CA    1 
ATOM   7051 C C     . ASP   B 2 285 ? -14.544 -23.616  -26.169 1.00 44.05  ? 277 ASP   B C     1 
ATOM   7052 O O     . ASP   B 2 285 ? -13.923 -22.694  -25.649 1.00 43.64  ? 277 ASP   B O     1 
ATOM   7053 C CB    . ASP   B 2 285 ? -12.594 -24.535  -27.504 1.00 44.42  ? 277 ASP   B CB    1 
ATOM   7054 C CG    . ASP   B 2 285 ? -12.869 -23.678  -28.733 1.00 46.02  ? 277 ASP   B CG    1 
ATOM   7055 O OD1   . ASP   B 2 285 ? -13.977 -23.111  -28.824 1.00 46.19  ? 277 ASP   B OD1   1 
ATOM   7056 O OD2   . ASP   B 2 285 ? -11.974 -23.593  -29.600 1.00 46.54  ? 277 ASP   B OD2   1 
ATOM   7057 N N     . CYS   B 2 286 ? -15.867 -23.580  -26.397 1.00 45.45  ? 278 CYS   B N     1 
ATOM   7058 C CA    . CYS   B 2 286 ? -16.749 -22.539  -25.888 1.00 46.90  ? 278 CYS   B CA    1 
ATOM   7059 C C     . CYS   B 2 286 ? -16.502 -21.211  -26.601 1.00 49.32  ? 278 CYS   B C     1 
ATOM   7060 O O     . CYS   B 2 286 ? -16.801 -20.152  -26.051 1.00 50.53  ? 278 CYS   B O     1 
ATOM   7061 C CB    . CYS   B 2 286 ? -16.607 -22.350  -24.381 1.00 46.52  ? 278 CYS   B CB    1 
ATOM   7062 S SG    . CYS   B 2 286 ? -17.071 -23.814  -23.425 1.00 45.01  ? 278 CYS   B SG    1 
ATOM   7063 N N     . SER   B 2 287 ? -15.979 -21.272  -27.833 1.00 50.68  ? 279 SER   B N     1 
ATOM   7064 C CA    . SER   B 2 287 ? -15.642 -20.067  -28.571 1.00 50.62  ? 279 SER   B CA    1 
ATOM   7065 C C     . SER   B 2 287 ? -16.380 -20.042  -29.905 1.00 51.27  ? 279 SER   B C     1 
ATOM   7066 O O     . SER   B 2 287 ? -16.756 -21.083  -30.440 1.00 48.96  ? 279 SER   B O     1 
ATOM   7067 C CB    . SER   B 2 287 ? -14.151 -19.930  -28.777 1.00 50.19  ? 279 SER   B CB    1 
ATOM   7068 O OG    . SER   B 2 287 ? -13.702 -20.718  -29.871 1.00 49.06  ? 279 SER   B OG    1 
ATOM   7069 N N     . LEU   B 2 288 ? -16.591 -18.818  -30.400 1.00 54.46  ? 280 LEU   B N     1 
ATOM   7070 C CA    . LEU   B 2 288 ? -17.040 -18.560  -31.756 1.00 55.45  ? 280 LEU   B CA    1 
ATOM   7071 C C     . LEU   B 2 288 ? -15.904 -17.877  -32.510 1.00 55.48  ? 280 LEU   B C     1 
ATOM   7072 O O     . LEU   B 2 288 ? -15.259 -16.984  -31.969 1.00 54.80  ? 280 LEU   B O     1 
ATOM   7073 C CB    . LEU   B 2 288 ? -18.286 -17.674  -31.720 1.00 55.82  ? 280 LEU   B CB    1 
ATOM   7074 C CG    . LEU   B 2 288 ? -18.595 -16.884  -32.998 1.00 55.25  ? 280 LEU   B CG    1 
ATOM   7075 C CD1   . LEU   B 2 288 ? -19.223 -17.770  -34.058 1.00 55.34  ? 280 LEU   B CD1   1 
ATOM   7076 C CD2   . LEU   B 2 288 ? -19.478 -15.685  -32.702 1.00 55.60  ? 280 LEU   B CD2   1 
ATOM   7077 N N     . ALA   B 2 289 ? -15.675 -18.310  -33.754 1.00 55.86  ? 281 ALA   B N     1 
ATOM   7078 C CA    . ALA   B 2 289 ? -14.805 -17.602  -34.678 1.00 57.56  ? 281 ALA   B CA    1 
ATOM   7079 C C     . ALA   B 2 289 ? -15.590 -17.272  -35.943 1.00 57.43  ? 281 ALA   B C     1 
ATOM   7080 O O     . ALA   B 2 289 ? -16.566 -17.947  -36.263 1.00 55.46  ? 281 ALA   B O     1 
ATOM   7081 C CB    . ALA   B 2 289 ? -13.581 -18.432  -34.996 1.00 57.81  ? 281 ALA   B CB    1 
ATOM   7082 N N     . VAL   B 2 290 ? -15.160 -16.219  -36.645 1.00 60.00  ? 282 VAL   B N     1 
ATOM   7083 C CA    . VAL   B 2 290 ? -15.714 -15.892  -37.948 1.00 61.57  ? 282 VAL   B CA    1 
ATOM   7084 C C     . VAL   B 2 290 ? -14.551 -15.772  -38.931 1.00 62.99  ? 282 VAL   B C     1 
ATOM   7085 O O     . VAL   B 2 290 ? -13.515 -15.194  -38.605 1.00 61.41  ? 282 VAL   B O     1 
ATOM   7086 C CB    . VAL   B 2 290 ? -16.595 -14.628  -37.908 1.00 62.15  ? 282 VAL   B CB    1 
ATOM   7087 C CG1   . VAL   B 2 290 ? -17.097 -14.231  -39.292 1.00 62.73  ? 282 VAL   B CG1   1 
ATOM   7088 C CG2   . VAL   B 2 290 ? -17.776 -14.803  -36.960 1.00 62.32  ? 282 VAL   B CG2   1 
ATOM   7089 N N     . LEU   B 2 291 ? -14.748 -16.339  -40.129 1.00 65.48  ? 283 LEU   B N     1 
ATOM   7090 C CA    . LEU   B 2 291 ? -13.669 -16.596  -41.070 1.00 67.21  ? 283 LEU   B CA    1 
ATOM   7091 C C     . LEU   B 2 291 ? -14.037 -16.043  -42.446 1.00 67.18  ? 283 LEU   B C     1 
ATOM   7092 O O     . LEU   B 2 291 ? -15.213 -16.006  -42.806 1.00 66.19  ? 283 LEU   B O     1 
ATOM   7093 C CB    . LEU   B 2 291 ? -13.440 -18.106  -41.125 1.00 68.37  ? 283 LEU   B CB    1 
ATOM   7094 C CG    . LEU   B 2 291 ? -13.194 -18.809  -39.785 1.00 68.87  ? 283 LEU   B CG    1 
ATOM   7095 C CD1   . LEU   B 2 291 ? -13.161 -20.316  -39.972 1.00 69.15  ? 283 LEU   B CD1   1 
ATOM   7096 C CD2   . LEU   B 2 291 ? -11.913 -18.325  -39.130 1.00 68.62  ? 283 LEU   B CD2   1 
ATOM   7097 N N     . ASP   B 2 292 ? -13.013 -15.641  -43.213 1.00 67.89  ? 284 ASP   B N     1 
ATOM   7098 C CA    . ASP   B 2 292 ? -13.198 -15.105  -44.555 1.00 67.84  ? 284 ASP   B CA    1 
ATOM   7099 C C     . ASP   B 2 292 ? -13.219 -16.262  -45.556 1.00 67.17  ? 284 ASP   B C     1 
ATOM   7100 O O     . ASP   B 2 292 ? -13.431 -17.410  -45.171 1.00 65.49  ? 284 ASP   B O     1 
ATOM   7101 C CB    . ASP   B 2 292 ? -12.172 -14.021  -44.859 1.00 67.36  ? 284 ASP   B CB    1 
ATOM   7102 C CG    . ASP   B 2 292 ? -10.726 -14.478  -44.992 1.00 68.15  ? 284 ASP   B CG    1 
ATOM   7103 O OD1   . ASP   B 2 292 ? -10.097 -14.748  -43.950 1.00 68.34  ? 284 ASP   B OD1   1 
ATOM   7104 O OD2   . ASP   B 2 292 ? -10.242 -14.565  -46.139 1.00 70.94  ? 284 ASP   B OD2   1 
ATOM   7105 N N     . SER   B 2 293 ? -13.023 -15.950  -46.846 1.00 68.71  ? 285 SER   B N     1 
ATOM   7106 C CA    . SER   B 2 293 ? -12.982 -16.958  -47.896 1.00 69.13  ? 285 SER   B CA    1 
ATOM   7107 C C     . SER   B 2 293 ? -11.725 -17.812  -47.746 1.00 68.72  ? 285 SER   B C     1 
ATOM   7108 O O     . SER   B 2 293 ? -11.755 -19.014  -47.998 1.00 66.02  ? 285 SER   B O     1 
ATOM   7109 C CB    . SER   B 2 293 ? -13.060 -16.329  -49.265 1.00 70.41  ? 285 SER   B CB    1 
ATOM   7110 O OG    . SER   B 2 293 ? -11.896 -15.566  -49.547 1.00 71.86  ? 285 SER   B OG    1 
ATOM   7111 N N     . SER   B 2 294 ? -10.615 -17.167  -47.368 1.00 70.17  ? 286 SER   B N     1 
ATOM   7112 C CA    . SER   B 2 294 ? -9.489  -17.862  -46.766 1.00 71.06  ? 286 SER   B CA    1 
ATOM   7113 C C     . SER   B 2 294 ? -9.843  -18.167  -45.314 1.00 73.01  ? 286 SER   B C     1 
ATOM   7114 O O     . SER   B 2 294 ? -10.595 -17.423  -44.691 1.00 74.58  ? 286 SER   B O     1 
ATOM   7115 C CB    . SER   B 2 294 ? -8.222  -17.057  -46.864 1.00 71.04  ? 286 SER   B CB    1 
ATOM   7116 O OG    . SER   B 2 294 ? -7.904  -16.783  -48.221 1.00 73.21  ? 286 SER   B OG    1 
ATOM   7117 N N     . LEU   B 2 295 ? -9.275  -19.247  -44.769 1.00 71.28  ? 287 LEU   B N     1 
ATOM   7118 C CA    . LEU   B 2 295 ? -9.709  -19.762  -43.479 1.00 69.91  ? 287 LEU   B CA    1 
ATOM   7119 C C     . LEU   B 2 295 ? -9.118  -18.948  -42.326 1.00 70.38  ? 287 LEU   B C     1 
ATOM   7120 O O     . LEU   B 2 295 ? -9.159  -19.398  -41.182 1.00 71.07  ? 287 LEU   B O     1 
ATOM   7121 C CB    . LEU   B 2 295 ? -9.337  -21.240  -43.358 1.00 68.15  ? 287 LEU   B CB    1 
ATOM   7122 C CG    . LEU   B 2 295 ? -10.095 -22.218  -44.262 1.00 66.41  ? 287 LEU   B CG    1 
ATOM   7123 C CD1   . LEU   B 2 295 ? -9.690  -23.640  -43.901 1.00 67.72  ? 287 LEU   B CD1   1 
ATOM   7124 C CD2   . LEU   B 2 295 ? -11.603 -22.058  -44.178 1.00 63.61  ? 287 LEU   B CD2   1 
ATOM   7125 N N     . SER   B 2 296 ? -8.588  -17.752  -42.615 1.00 70.03  ? 288 SER   B N     1 
ATOM   7126 C CA    . SER   B 2 296 ? -8.009  -16.902  -41.586 1.00 70.30  ? 288 SER   B CA    1 
ATOM   7127 C C     . SER   B 2 296 ? -9.108  -16.244  -40.750 1.00 69.89  ? 288 SER   B C     1 
ATOM   7128 O O     . SER   B 2 296 ? -10.237 -16.075  -41.209 1.00 66.49  ? 288 SER   B O     1 
ATOM   7129 C CB    . SER   B 2 296 ? -7.067  -15.887  -42.188 1.00 69.99  ? 288 SER   B CB    1 
ATOM   7130 O OG    . SER   B 2 296 ? -7.584  -15.359  -43.400 1.00 71.31  ? 288 SER   B OG    1 
ATOM   7131 N N     . GLU   B 2 297 ? -8.742  -15.878  -39.514 1.00 71.67  ? 289 GLU   B N     1 
ATOM   7132 C CA    . GLU   B 2 297 ? -9.675  -15.446  -38.484 1.00 73.25  ? 289 GLU   B CA    1 
ATOM   7133 C C     . GLU   B 2 297 ? -9.892  -13.937  -38.557 1.00 73.45  ? 289 GLU   B C     1 
ATOM   7134 O O     . GLU   B 2 297 ? -8.941  -13.178  -38.734 1.00 73.50  ? 289 GLU   B O     1 
ATOM   7135 C CB    . GLU   B 2 297 ? -9.093  -15.845  -37.127 1.00 74.49  ? 289 GLU   B CB    1 
ATOM   7136 C CG    . GLU   B 2 297 ? -9.889  -15.365  -35.916 1.00 74.99  ? 289 GLU   B CG    1 
ATOM   7137 C CD    . GLU   B 2 297 ? -9.240  -15.746  -34.595 1.00 74.53  ? 289 GLU   B CD    1 
ATOM   7138 O OE1   . GLU   B 2 297 ? -8.310  -16.580  -34.601 1.00 73.16  ? 289 GLU   B OE1   1 
ATOM   7139 O OE2   . GLU   B 2 297 ? -9.646  -15.189  -33.557 1.00 74.81  ? 289 GLU   B OE2   1 
ATOM   7140 N N     . LEU   B 2 298 ? -11.153 -13.517  -38.384 1.00 73.30  ? 290 LEU   B N     1 
ATOM   7141 C CA    . LEU   B 2 298 ? -11.514 -12.108  -38.369 1.00 73.49  ? 290 LEU   B CA    1 
ATOM   7142 C C     . LEU   B 2 298 ? -12.014 -11.706  -36.980 1.00 72.33  ? 290 LEU   B C     1 
ATOM   7143 O O     . LEU   B 2 298 ? -11.605 -10.672  -36.458 1.00 74.09  ? 290 LEU   B O     1 
ATOM   7144 C CB    . LEU   B 2 298 ? -12.559 -11.830  -39.449 1.00 73.84  ? 290 LEU   B CB    1 
ATOM   7145 C CG    . LEU   B 2 298 ? -12.116 -12.062  -40.898 1.00 74.34  ? 290 LEU   B CG    1 
ATOM   7146 C CD1   . LEU   B 2 298 ? -13.284 -11.834  -41.843 1.00 74.49  ? 290 LEU   B CD1   1 
ATOM   7147 C CD2   . LEU   B 2 298 ? -10.942 -11.178  -41.290 1.00 74.61  ? 290 LEU   B CD2   1 
ATOM   7148 N N     . PHE   B 2 299 ? -12.904 -12.522  -36.397 1.00 70.34  ? 291 PHE   B N     1 
ATOM   7149 C CA    . PHE   B 2 299 ? -13.477 -12.251  -35.087 1.00 67.97  ? 291 PHE   B CA    1 
ATOM   7150 C C     . PHE   B 2 299 ? -13.363 -13.506  -34.223 1.00 66.28  ? 291 PHE   B C     1 
ATOM   7151 O O     . PHE   B 2 299 ? -13.094 -14.592  -34.734 1.00 65.50  ? 291 PHE   B O     1 
ATOM   7152 C CB    . PHE   B 2 299 ? -14.904 -11.750  -35.336 1.00 67.74  ? 291 PHE   B CB    1 
ATOM   7153 C CG    . PHE   B 2 299 ? -15.671 -11.254  -34.115 1.00 68.40  ? 291 PHE   B CG    1 
ATOM   7154 C CD1   . PHE   B 2 299 ? -15.271 -10.107  -33.434 1.00 67.57  ? 291 PHE   B CD1   1 
ATOM   7155 C CD2   . PHE   B 2 299 ? -16.819 -11.909  -33.679 1.00 69.24  ? 291 PHE   B CD2   1 
ATOM   7156 C CE1   . PHE   B 2 299 ? -15.980 -9.652   -32.331 1.00 67.53  ? 291 PHE   B CE1   1 
ATOM   7157 C CE2   . PHE   B 2 299 ? -17.527 -11.447  -32.578 1.00 68.61  ? 291 PHE   B CE2   1 
ATOM   7158 C CZ    . PHE   B 2 299 ? -17.107 -10.320  -31.907 1.00 68.05  ? 291 PHE   B CZ    1 
ATOM   7159 N N     . ARG   B 2 300 ? -13.549 -13.335  -32.907 1.00 65.04  ? 292 ARG   B N     1 
ATOM   7160 C CA    . ARG   B 2 300 ? -13.447 -14.422  -31.944 1.00 63.95  ? 292 ARG   B CA    1 
ATOM   7161 C C     . ARG   B 2 300 ? -14.129 -14.001  -30.646 1.00 61.54  ? 292 ARG   B C     1 
ATOM   7162 O O     . ARG   B 2 300 ? -13.847 -12.924  -30.127 1.00 61.69  ? 292 ARG   B O     1 
ATOM   7163 C CB    . ARG   B 2 300 ? -11.971 -14.767  -31.714 1.00 65.12  ? 292 ARG   B CB    1 
ATOM   7164 C CG    . ARG   B 2 300 ? -11.643 -15.771  -30.615 1.00 65.12  ? 292 ARG   B CG    1 
ATOM   7165 C CD    . ARG   B 2 300 ? -12.232 -17.163  -30.814 1.00 65.16  ? 292 ARG   B CD    1 
ATOM   7166 N NE    . ARG   B 2 300 ? -11.855 -17.892  -32.031 1.00 65.34  ? 292 ARG   B NE    1 
ATOM   7167 C CZ    . ARG   B 2 300 ? -10.656 -18.383  -32.339 1.00 65.62  ? 292 ARG   B CZ    1 
ATOM   7168 N NH1   . ARG   B 2 300 ? -9.575  -18.004  -31.679 1.00 65.99  ? 292 ARG   B NH1   1 
ATOM   7169 N NH2   . ARG   B 2 300 ? -10.533 -19.226  -33.349 1.00 65.63  ? 292 ARG   B NH2   1 
ATOM   7170 N N     . SER   B 2 301 ? -15.017 -14.860  -30.127 1.00 61.28  ? 293 SER   B N     1 
ATOM   7171 C CA    . SER   B 2 301 ? -15.796 -14.550  -28.938 1.00 60.80  ? 293 SER   B CA    1 
ATOM   7172 C C     . SER   B 2 301 ? -15.600 -15.634  -27.880 1.00 60.74  ? 293 SER   B C     1 
ATOM   7173 O O     . SER   B 2 301 ? -15.708 -16.822  -28.177 1.00 61.13  ? 293 SER   B O     1 
ATOM   7174 C CB    . SER   B 2 301 ? -17.256 -14.375  -29.282 1.00 60.87  ? 293 SER   B CB    1 
ATOM   7175 O OG    . SER   B 2 301 ? -18.057 -14.279  -28.112 1.00 61.49  ? 293 SER   B OG    1 
ATOM   7176 N N     . GLN   B 2 302 ? -15.324 -15.194  -26.643 1.00 60.08  ? 294 GLN   B N     1 
ATOM   7177 C CA    . GLN   B 2 302 ? -15.163 -16.070  -25.493 1.00 57.84  ? 294 GLN   B CA    1 
ATOM   7178 C C     . GLN   B 2 302 ? -16.364 -15.916  -24.562 1.00 56.80  ? 294 GLN   B C     1 
ATOM   7179 O O     . GLN   B 2 302 ? -16.339 -16.407  -23.436 1.00 56.18  ? 294 GLN   B O     1 
ATOM   7180 C CB    . GLN   B 2 302 ? -13.909 -15.694  -24.701 1.00 58.09  ? 294 GLN   B CB    1 
ATOM   7181 C CG    . GLN   B 2 302 ? -12.688 -15.371  -25.556 1.00 59.57  ? 294 GLN   B CG    1 
ATOM   7182 C CD    . GLN   B 2 302 ? -12.122 -16.578  -26.268 1.00 61.28  ? 294 GLN   B CD    1 
ATOM   7183 O OE1   . GLN   B 2 302 ? -12.829 -17.294  -26.986 1.00 64.03  ? 294 GLN   B OE1   1 
ATOM   7184 N NE2   . GLN   B 2 302 ? -10.833 -16.820  -26.075 1.00 62.97  ? 294 GLN   B NE2   1 
ATOM   7185 N N     . ALA   B 2 303 ? -17.410 -15.235  -25.049 1.00 56.31  ? 295 ALA   B N     1 
ATOM   7186 C CA    . ALA   B 2 303 ? -18.511 -14.777  -24.216 1.00 55.26  ? 295 ALA   B CA    1 
ATOM   7187 C C     . ALA   B 2 303 ? -19.201 -15.953  -23.532 1.00 55.08  ? 295 ALA   B C     1 
ATOM   7188 O O     . ALA   B 2 303 ? -19.542 -15.864  -22.354 1.00 54.33  ? 295 ALA   B O     1 
ATOM   7189 C CB    . ALA   B 2 303 ? -19.488 -13.981  -25.051 1.00 54.90  ? 295 ALA   B CB    1 
ATOM   7190 N N     . HIS   B 2 304 ? -19.411 -17.041  -24.284 1.00 54.82  ? 296 HIS   B N     1 
ATOM   7191 C CA    . HIS   B 2 304 ? -20.003 -18.248  -23.731 1.00 54.20  ? 296 HIS   B CA    1 
ATOM   7192 C C     . HIS   B 2 304 ? -19.034 -18.879  -22.731 1.00 54.74  ? 296 HIS   B C     1 
ATOM   7193 O O     . HIS   B 2 304 ? -17.830 -18.930  -22.976 1.00 55.48  ? 296 HIS   B O     1 
ATOM   7194 C CB    . HIS   B 2 304 ? -20.428 -19.217  -24.841 1.00 52.25  ? 296 HIS   B CB    1 
ATOM   7195 C CG    . HIS   B 2 304 ? -21.716 -18.856  -25.506 1.00 51.05  ? 296 HIS   B CG    1 
ATOM   7196 N ND1   . HIS   B 2 304 ? -22.938 -19.190  -24.963 1.00 49.71  ? 296 HIS   B ND1   1 
ATOM   7197 C CD2   . HIS   B 2 304 ? -21.981 -18.203  -26.645 1.00 50.14  ? 296 HIS   B CD2   1 
ATOM   7198 C CE1   . HIS   B 2 304 ? -23.903 -18.753  -25.758 1.00 49.48  ? 296 HIS   B CE1   1 
ATOM   7199 N NE2   . HIS   B 2 304 ? -23.345 -18.151  -26.786 1.00 50.23  ? 296 HIS   B NE2   1 
ATOM   7200 N N     . ARG   B 2 305 ? -19.581 -19.332  -21.596 1.00 54.24  ? 297 ARG   B N     1 
ATOM   7201 C CA    . ARG   B 2 305 ? -18.814 -20.035  -20.581 1.00 56.58  ? 297 ARG   B CA    1 
ATOM   7202 C C     . ARG   B 2 305 ? -19.058 -21.542  -20.676 1.00 54.30  ? 297 ARG   B C     1 
ATOM   7203 O O     . ARG   B 2 305 ? -18.482 -22.304  -19.905 1.00 52.95  ? 297 ARG   B O     1 
ATOM   7204 C CB    . ARG   B 2 305 ? -19.177 -19.501  -19.190 1.00 58.97  ? 297 ARG   B CB    1 
ATOM   7205 C CG    . ARG   B 2 305 ? -18.664 -18.098  -18.893 1.00 60.83  ? 297 ARG   B CG    1 
ATOM   7206 C CD    . ARG   B 2 305 ? -19.410 -17.448  -17.734 1.00 62.92  ? 297 ARG   B CD    1 
ATOM   7207 N NE    . ARG   B 2 305 ? -20.736 -16.953  -18.129 1.00 65.38  ? 297 ARG   B NE    1 
ATOM   7208 C CZ    . ARG   B 2 305 ? -21.919 -17.524  -17.887 1.00 67.34  ? 297 ARG   B CZ    1 
ATOM   7209 N NH1   . ARG   B 2 305 ? -22.003 -18.715  -17.315 1.00 68.98  ? 297 ARG   B NH1   1 
ATOM   7210 N NH2   . ARG   B 2 305 ? -23.031 -16.904  -18.251 1.00 66.99  ? 297 ARG   B NH2   1 
ATOM   7211 N N     . ASP   B 2 306 ? -19.916 -21.963  -21.618 1.00 53.07  ? 298 ASP   B N     1 
ATOM   7212 C CA    . ASP   B 2 306 ? -20.159 -23.374  -21.881 1.00 50.85  ? 298 ASP   B CA    1 
ATOM   7213 C C     . ASP   B 2 306 ? -20.194 -23.577  -23.397 1.00 48.96  ? 298 ASP   B C     1 
ATOM   7214 O O     . ASP   B 2 306 ? -19.910 -22.646  -24.148 1.00 48.46  ? 298 ASP   B O     1 
ATOM   7215 C CB    . ASP   B 2 306 ? -21.401 -23.848  -21.139 1.00 50.32  ? 298 ASP   B CB    1 
ATOM   7216 C CG    . ASP   B 2 306 ? -21.450 -25.328  -20.782 1.00 50.02  ? 298 ASP   B CG    1 
ATOM   7217 O OD1   . ASP   B 2 306 ? -20.531 -26.068  -21.192 1.00 49.47  ? 298 ASP   B OD1   1 
ATOM   7218 O OD2   . ASP   B 2 306 ? -22.406 -25.730  -20.085 1.00 50.30  ? 298 ASP   B OD2   1 
ATOM   7219 N N     . PHE   B 2 307 ? -20.520 -24.799  -23.840 1.00 47.74  ? 299 PHE   B N     1 
ATOM   7220 C CA    . PHE   B 2 307 ? -20.442 -25.164  -25.247 1.00 48.23  ? 299 PHE   B CA    1 
ATOM   7221 C C     . PHE   B 2 307 ? -21.276 -24.212  -26.101 1.00 48.18  ? 299 PHE   B C     1 
ATOM   7222 O O     . PHE   B 2 307 ? -22.385 -23.843  -25.719 1.00 50.15  ? 299 PHE   B O     1 
ATOM   7223 C CB    . PHE   B 2 307 ? -20.954 -26.583  -25.514 1.00 47.38  ? 299 PHE   B CB    1 
ATOM   7224 C CG    . PHE   B 2 307 ? -20.129 -27.734  -24.953 1.00 46.67  ? 299 PHE   B CG    1 
ATOM   7225 C CD1   . PHE   B 2 307 ? -18.800 -27.568  -24.573 1.00 46.48  ? 299 PHE   B CD1   1 
ATOM   7226 C CD2   . PHE   B 2 307 ? -20.690 -29.001  -24.839 1.00 46.30  ? 299 PHE   B CD2   1 
ATOM   7227 C CE1   . PHE   B 2 307 ? -18.068 -28.635  -24.072 1.00 46.07  ? 299 PHE   B CE1   1 
ATOM   7228 C CE2   . PHE   B 2 307 ? -19.953 -30.064  -24.341 1.00 45.56  ? 299 PHE   B CE2   1 
ATOM   7229 C CZ    . PHE   B 2 307 ? -18.645 -29.879  -23.958 1.00 45.74  ? 299 PHE   B CZ    1 
ATOM   7230 N N     . VAL   B 2 308 ? -20.732 -23.848  -27.269 1.00 47.46  ? 300 VAL   B N     1 
ATOM   7231 C CA    . VAL   B 2 308 ? -21.447 -23.054  -28.256 1.00 46.39  ? 300 VAL   B CA    1 
ATOM   7232 C C     . VAL   B 2 308 ? -22.111 -24.014  -29.242 1.00 46.06  ? 300 VAL   B C     1 
ATOM   7233 O O     . VAL   B 2 308 ? -21.439 -24.839  -29.857 1.00 46.05  ? 300 VAL   B O     1 
ATOM   7234 C CB    . VAL   B 2 308 ? -20.524 -22.057  -28.983 1.00 46.48  ? 300 VAL   B CB    1 
ATOM   7235 C CG1   . VAL   B 2 308 ? -21.322 -21.068  -29.826 1.00 46.53  ? 300 VAL   B CG1   1 
ATOM   7236 C CG2   . VAL   B 2 308 ? -19.614 -21.308  -28.016 1.00 45.68  ? 300 VAL   B CG2   1 
ATOM   7237 N N     . ARG   B 2 309 ? -23.429 -23.858  -29.413 1.00 45.55  ? 301 ARG   B N     1 
ATOM   7238 C CA    . ARG   B 2 309 ? -24.279 -24.908  -29.950 1.00 45.00  ? 301 ARG   B CA    1 
ATOM   7239 C C     . ARG   B 2 309 ? -24.804 -24.572  -31.345 1.00 44.87  ? 301 ARG   B C     1 
ATOM   7240 O O     . ARG   B 2 309 ? -24.818 -25.439  -32.216 1.00 44.37  ? 301 ARG   B O     1 
ATOM   7241 C CB    . ARG   B 2 309 ? -25.425 -25.123  -28.959 1.00 45.20  ? 301 ARG   B CB    1 
ATOM   7242 C CG    . ARG   B 2 309 ? -25.032 -25.964  -27.753 1.00 45.40  ? 301 ARG   B CG    1 
ATOM   7243 C CD    . ARG   B 2 309 ? -24.888 -27.431  -28.136 1.00 44.94  ? 301 ARG   B CD    1 
ATOM   7244 N NE    . ARG   B 2 309 ? -23.521 -27.890  -28.405 1.00 44.29  ? 301 ARG   B NE    1 
ATOM   7245 C CZ    . ARG   B 2 309 ? -23.209 -29.148  -28.709 1.00 43.84  ? 301 ARG   B CZ    1 
ATOM   7246 N NH1   . ARG   B 2 309 ? -24.158 -30.057  -28.869 1.00 42.49  ? 301 ARG   B NH1   1 
ATOM   7247 N NH2   . ARG   B 2 309 ? -21.942 -29.495  -28.863 1.00 44.31  ? 301 ARG   B NH2   1 
ATOM   7248 N N     . ASP   B 2 310 ? -25.262 -23.329  -31.546 1.00 45.26  ? 302 ASP   B N     1 
ATOM   7249 C CA    . ASP   B 2 310 ? -25.808 -22.918  -32.830 1.00 45.44  ? 302 ASP   B CA    1 
ATOM   7250 C C     . ASP   B 2 310 ? -25.443 -21.461  -33.106 1.00 46.17  ? 302 ASP   B C     1 
ATOM   7251 O O     . ASP   B 2 310 ? -24.926 -20.765  -32.236 1.00 46.57  ? 302 ASP   B O     1 
ATOM   7252 C CB    . ASP   B 2 310 ? -27.309 -23.157  -32.897 1.00 44.28  ? 302 ASP   B CB    1 
ATOM   7253 C CG    . ASP   B 2 310 ? -27.885 -23.343  -34.293 1.00 42.56  ? 302 ASP   B CG    1 
ATOM   7254 O OD1   . ASP   B 2 310 ? -27.133 -23.159  -35.269 1.00 41.88  ? 302 ASP   B OD1   1 
ATOM   7255 O OD2   . ASP   B 2 310 ? -29.078 -23.689  -34.395 1.00 41.71  ? 302 ASP   B OD2   1 
ATOM   7256 N N     . ALA   B 2 311 ? -25.684 -21.035  -34.351 1.00 47.92  ? 303 ALA   B N     1 
ATOM   7257 C CA    . ALA   B 2 311 ? -25.440 -19.669  -34.783 1.00 49.74  ? 303 ALA   B CA    1 
ATOM   7258 C C     . ALA   B 2 311 ? -26.323 -19.361  -35.990 1.00 50.52  ? 303 ALA   B C     1 
ATOM   7259 O O     . ALA   B 2 311 ? -26.622 -20.249  -36.788 1.00 51.70  ? 303 ALA   B O     1 
ATOM   7260 C CB    . ALA   B 2 311 ? -23.972 -19.473  -35.096 1.00 49.57  ? 303 ALA   B CB    1 
ATOM   7261 N N     . THR   B 2 312 ? -26.732 -18.093  -36.110 1.00 49.75  ? 304 THR   B N     1 
ATOM   7262 C CA    . THR   B 2 312 ? -27.721 -17.690  -37.096 1.00 49.15  ? 304 THR   B CA    1 
ATOM   7263 C C     . THR   B 2 312 ? -27.583 -16.189  -37.344 1.00 50.75  ? 304 THR   B C     1 
ATOM   7264 O O     . THR   B 2 312 ? -27.631 -15.394  -36.409 1.00 49.36  ? 304 THR   B O     1 
ATOM   7265 C CB    . THR   B 2 312 ? -29.111 -18.102  -36.602 1.00 47.61  ? 304 THR   B CB    1 
ATOM   7266 O OG1   . THR   B 2 312 ? -30.076 -17.568  -37.501 1.00 46.15  ? 304 THR   B OG1   1 
ATOM   7267 C CG2   . THR   B 2 312 ? -29.420 -17.617  -35.197 1.00 47.87  ? 304 THR   B CG2   1 
ATOM   7268 N N     . TRP   B 2 313 ? -27.377 -15.823  -38.617 1.00 54.95  ? 305 TRP   B N     1 
ATOM   7269 C CA    . TRP   B 2 313 ? -27.196 -14.435  -39.014 1.00 56.23  ? 305 TRP   B CA    1 
ATOM   7270 C C     . TRP   B 2 313 ? -28.555 -13.764  -39.177 1.00 59.62  ? 305 TRP   B C     1 
ATOM   7271 O O     . TRP   B 2 313 ? -29.487 -14.371  -39.704 1.00 60.93  ? 305 TRP   B O     1 
ATOM   7272 C CB    . TRP   B 2 313 ? -26.403 -14.343  -40.324 1.00 53.62  ? 305 TRP   B CB    1 
ATOM   7273 C CG    . TRP   B 2 313 ? -25.043 -14.985  -40.271 1.00 51.75  ? 305 TRP   B CG    1 
ATOM   7274 C CD1   . TRP   B 2 313 ? -24.760 -16.312  -40.402 1.00 51.03  ? 305 TRP   B CD1   1 
ATOM   7275 C CD2   . TRP   B 2 313 ? -23.774 -14.317  -40.096 1.00 50.13  ? 305 TRP   B CD2   1 
ATOM   7276 N NE1   . TRP   B 2 313 ? -23.410 -16.520  -40.309 1.00 51.05  ? 305 TRP   B NE1   1 
ATOM   7277 C CE2   . TRP   B 2 313 ? -22.779 -15.318  -40.123 1.00 50.29  ? 305 TRP   B CE2   1 
ATOM   7278 C CE3   . TRP   B 2 313 ? -23.384 -12.984  -39.915 1.00 50.30  ? 305 TRP   B CE3   1 
ATOM   7279 C CZ2   . TRP   B 2 313 ? -21.425 -15.024  -39.978 1.00 50.67  ? 305 TRP   B CZ2   1 
ATOM   7280 C CZ3   . TRP   B 2 313 ? -22.044 -12.695  -39.773 1.00 50.04  ? 305 TRP   B CZ3   1 
ATOM   7281 C CH2   . TRP   B 2 313 ? -21.079 -13.702  -39.806 1.00 50.38  ? 305 TRP   B CH2   1 
ATOM   7282 N N     . SER   B 2 314 ? -28.646 -12.505  -38.735 1.00 62.80  ? 306 SER   B N     1 
ATOM   7283 C CA    . SER   B 2 314 ? -29.870 -11.732  -38.864 1.00 64.53  ? 306 SER   B CA    1 
ATOM   7284 C C     . SER   B 2 314 ? -30.138 -11.432  -40.338 1.00 63.88  ? 306 SER   B C     1 
ATOM   7285 O O     . SER   B 2 314 ? -29.233 -11.026  -41.066 1.00 62.52  ? 306 SER   B O     1 
ATOM   7286 C CB    . SER   B 2 314 ? -29.807 -10.467  -38.046 1.00 66.17  ? 306 SER   B CB    1 
ATOM   7287 O OG    . SER   B 2 314 ? -30.973 -9.677   -38.230 1.00 67.67  ? 306 SER   B OG    1 
ATOM   7288 N N     . PRO   B 2 315 ? -31.383 -11.647  -40.824 1.00 64.17  ? 307 PRO   B N     1 
ATOM   7289 C CA    . PRO   B 2 315 ? -31.760 -11.242  -42.178 1.00 65.70  ? 307 PRO   B CA    1 
ATOM   7290 C C     . PRO   B 2 315 ? -31.811 -9.719   -42.284 1.00 66.39  ? 307 PRO   B C     1 
ATOM   7291 O O     . PRO   B 2 315 ? -31.458 -9.154   -43.317 1.00 67.20  ? 307 PRO   B O     1 
ATOM   7292 C CB    . PRO   B 2 315 ? -33.138 -11.884  -42.443 1.00 65.27  ? 307 PRO   B CB    1 
ATOM   7293 C CG    . PRO   B 2 315 ? -33.618 -12.400  -41.098 1.00 64.25  ? 307 PRO   B CG    1 
ATOM   7294 C CD    . PRO   B 2 315 ? -32.487 -12.284  -40.091 1.00 63.91  ? 307 PRO   B CD    1 
ATOM   7295 N N     . LEU   B 2 316 ? -32.233 -9.076   -41.188 1.00 65.89  ? 308 LEU   B N     1 
ATOM   7296 C CA    . LEU   B 2 316 ? -32.497 -7.647   -41.164 1.00 64.74  ? 308 LEU   B CA    1 
ATOM   7297 C C     . LEU   B 2 316 ? -31.177 -6.882   -41.064 1.00 65.06  ? 308 LEU   B C     1 
ATOM   7298 O O     . LEU   B 2 316 ? -31.073 -5.764   -41.561 1.00 66.50  ? 308 LEU   B O     1 
ATOM   7299 C CB    . LEU   B 2 316 ? -33.436 -7.327   -40.000 1.00 64.07  ? 308 LEU   B CB    1 
ATOM   7300 C CG    . LEU   B 2 316 ? -34.637 -8.264   -39.818 1.00 64.42  ? 308 LEU   B CG    1 
ATOM   7301 C CD1   . LEU   B 2 316 ? -35.579 -7.722   -38.757 1.00 63.41  ? 308 LEU   B CD1   1 
ATOM   7302 C CD2   . LEU   B 2 316 ? -35.384 -8.512   -41.122 1.00 65.49  ? 308 LEU   B CD2   1 
ATOM   7303 N N     . ASN   B 2 317 ? -30.177 -7.494   -40.418 1.00 65.28  ? 309 ASN   B N     1 
ATOM   7304 C CA    . ASN   B 2 317 ? -28.837 -6.934   -40.358 1.00 65.84  ? 309 ASN   B CA    1 
ATOM   7305 C C     . ASN   B 2 317 ? -27.822 -8.047   -40.617 1.00 68.71  ? 309 ASN   B C     1 
ATOM   7306 O O     . ASN   B 2 317 ? -27.740 -9.010   -39.859 1.00 68.37  ? 309 ASN   B O     1 
ATOM   7307 C CB    . ASN   B 2 317 ? -28.598 -6.213   -39.036 1.00 64.82  ? 309 ASN   B CB    1 
ATOM   7308 C CG    . ASN   B 2 317 ? -27.263 -5.506   -38.994 1.00 64.66  ? 309 ASN   B CG    1 
ATOM   7309 O OD1   . ASN   B 2 317 ? -26.366 -5.803   -39.793 1.00 63.15  ? 309 ASN   B OD1   1 
ATOM   7310 N ND2   . ASN   B 2 317 ? -27.103 -4.579   -38.061 1.00 65.34  ? 309 ASN   B ND2   1 
ATOM   7311 N N     . HIS   B 2 318 ? -27.023 -7.877   -41.677 1.00 70.65  ? 310 HIS   B N     1 
ATOM   7312 C CA    . HIS   B 2 318 ? -26.116 -8.914   -42.144 1.00 70.99  ? 310 HIS   B CA    1 
ATOM   7313 C C     . HIS   B 2 318 ? -24.776 -8.852   -41.408 1.00 70.43  ? 310 HIS   B C     1 
ATOM   7314 O O     . HIS   B 2 318 ? -23.854 -9.583   -41.763 1.00 71.97  ? 310 HIS   B O     1 
ATOM   7315 C CB    . HIS   B 2 318 ? -25.961 -8.827   -43.668 1.00 71.06  ? 310 HIS   B CB    1 
ATOM   7316 C CG    . HIS   B 2 318 ? -27.146 -9.320   -44.434 1.00 71.56  ? 310 HIS   B CG    1 
ATOM   7317 N ND1   . HIS   B 2 318 ? -27.105 -9.551   -45.793 1.00 72.18  ? 310 HIS   B ND1   1 
ATOM   7318 C CD2   . HIS   B 2 318 ? -28.396 -9.610   -44.048 1.00 71.68  ? 310 HIS   B CD2   1 
ATOM   7319 C CE1   . HIS   B 2 318 ? -28.293 -9.976   -46.202 1.00 71.32  ? 310 HIS   B CE1   1 
ATOM   7320 N NE2   . HIS   B 2 318 ? -29.090 -10.025  -45.157 1.00 71.71  ? 310 HIS   B NE2   1 
ATOM   7321 N N     . SER   B 2 319 ? -24.664 -7.991   -40.387 1.00 68.09  ? 311 SER   B N     1 
ATOM   7322 C CA    . SER   B 2 319 ? -23.491 -7.979   -39.524 1.00 68.85  ? 311 SER   B CA    1 
ATOM   7323 C C     . SER   B 2 319 ? -23.859 -8.315   -38.077 1.00 70.01  ? 311 SER   B C     1 
ATOM   7324 O O     . SER   B 2 319 ? -22.989 -8.306   -37.208 1.00 67.76  ? 311 SER   B O     1 
ATOM   7325 C CB    . SER   B 2 319 ? -22.769 -6.660   -39.615 1.00 68.12  ? 311 SER   B CB    1 
ATOM   7326 O OG    . SER   B 2 319 ? -23.641 -5.582   -39.305 1.00 68.51  ? 311 SER   B OG    1 
ATOM   7327 N N     . LEU   B 2 320 ? -25.140 -8.615   -37.819 1.00 72.42  ? 312 LEU   B N     1 
ATOM   7328 C CA    . LEU   B 2 320 ? -25.562 -9.138   -36.529 1.00 75.08  ? 312 LEU   B CA    1 
ATOM   7329 C C     . LEU   B 2 320 ? -25.498 -10.663  -36.585 1.00 74.75  ? 312 LEU   B C     1 
ATOM   7330 O O     . LEU   B 2 320 ? -25.938 -11.266  -37.565 1.00 74.64  ? 312 LEU   B O     1 
ATOM   7331 C CB    . LEU   B 2 320 ? -26.967 -8.664   -36.161 1.00 77.84  ? 312 LEU   B CB    1 
ATOM   7332 C CG    . LEU   B 2 320 ? -27.419 -8.973   -34.729 1.00 80.46  ? 312 LEU   B CG    1 
ATOM   7333 C CD1   . LEU   B 2 320 ? -26.795 -7.988   -33.753 1.00 80.91  ? 312 LEU   B CD1   1 
ATOM   7334 C CD2   . LEU   B 2 320 ? -28.934 -8.982   -34.588 1.00 81.69  ? 312 LEU   B CD2   1 
ATOM   7335 N N     . LEU   B 2 321 ? -24.953 -11.271  -35.522 1.00 72.44  ? 313 LEU   B N     1 
ATOM   7336 C CA    . LEU   B 2 321 ? -24.828 -12.718  -35.425 1.00 68.19  ? 313 LEU   B CA    1 
ATOM   7337 C C     . LEU   B 2 321 ? -25.217 -13.163  -34.017 1.00 63.38  ? 313 LEU   B C     1 
ATOM   7338 O O     . LEU   B 2 321 ? -24.789 -12.560  -33.036 1.00 62.36  ? 313 LEU   B O     1 
ATOM   7339 C CB    . LEU   B 2 321 ? -23.399 -13.127  -35.779 1.00 66.95  ? 313 LEU   B CB    1 
ATOM   7340 C CG    . LEU   B 2 321 ? -23.082 -14.625  -35.717 1.00 65.44  ? 313 LEU   B CG    1 
ATOM   7341 C CD1   . LEU   B 2 321 ? -24.026 -15.453  -36.575 1.00 64.54  ? 313 LEU   B CD1   1 
ATOM   7342 C CD2   . LEU   B 2 321 ? -21.642 -14.861  -36.138 1.00 65.04  ? 313 LEU   B CD2   1 
ATOM   7343 N N     . THR   B 2 322 ? -26.019 -14.230  -33.934 1.00 59.76  ? 314 THR   B N     1 
ATOM   7344 C CA    . THR   B 2 322 ? -26.645 -14.641  -32.688 1.00 59.33  ? 314 THR   B CA    1 
ATOM   7345 C C     . THR   B 2 322 ? -26.263 -16.085  -32.367 1.00 57.48  ? 314 THR   B C     1 
ATOM   7346 O O     . THR   B 2 322 ? -26.651 -16.999  -33.092 1.00 57.51  ? 314 THR   B O     1 
ATOM   7347 C CB    . THR   B 2 322 ? -28.157 -14.466  -32.835 1.00 60.27  ? 314 THR   B CB    1 
ATOM   7348 O OG1   . THR   B 2 322 ? -28.343 -13.062  -32.983 1.00 61.87  ? 314 THR   B OG1   1 
ATOM   7349 C CG2   . THR   B 2 322 ? -28.939 -14.969  -31.635 1.00 60.64  ? 314 THR   B CG2   1 
ATOM   7350 N N     . THR   B 2 323 ? -25.521 -16.279  -31.266 1.00 55.16  ? 315 THR   B N     1 
ATOM   7351 C CA    . THR   B 2 323 ? -25.136 -17.605  -30.803 1.00 52.61  ? 315 THR   B CA    1 
ATOM   7352 C C     . THR   B 2 323 ? -26.032 -18.021  -29.638 1.00 51.39  ? 315 THR   B C     1 
ATOM   7353 O O     . THR   B 2 323 ? -26.608 -17.178  -28.955 1.00 50.19  ? 315 THR   B O     1 
ATOM   7354 C CB    . THR   B 2 323 ? -23.667 -17.617  -30.378 1.00 51.62  ? 315 THR   B CB    1 
ATOM   7355 O OG1   . THR   B 2 323 ? -23.569 -16.757  -29.248 1.00 49.94  ? 315 THR   B OG1   1 
ATOM   7356 C CG2   . THR   B 2 323 ? -22.728 -17.140  -31.470 1.00 52.41  ? 315 THR   B CG2   1 
ATOM   7357 N N     . VAL   B 2 324 ? -26.134 -19.336  -29.422 1.00 52.07  ? 316 VAL   B N     1 
ATOM   7358 C CA    . VAL   B 2 324 ? -26.698 -19.875  -28.195 1.00 53.17  ? 316 VAL   B CA    1 
ATOM   7359 C C     . VAL   B 2 324 ? -25.758 -20.962  -27.682 1.00 53.72  ? 316 VAL   B C     1 
ATOM   7360 O O     . VAL   B 2 324 ? -24.959 -21.506  -28.442 1.00 53.17  ? 316 VAL   B O     1 
ATOM   7361 C CB    . VAL   B 2 324 ? -28.136 -20.403  -28.366 1.00 52.73  ? 316 VAL   B CB    1 
ATOM   7362 C CG1   . VAL   B 2 324 ? -29.079 -19.302  -28.831 1.00 52.82  ? 316 VAL   B CG1   1 
ATOM   7363 C CG2   . VAL   B 2 324 ? -28.210 -21.602  -29.303 1.00 52.52  ? 316 VAL   B CG2   1 
ATOM   7364 N N     . GLY   B 2 325 ? -25.863 -21.262  -26.383 1.00 53.76  ? 317 GLY   B N     1 
ATOM   7365 C CA    . GLY   B 2 325 ? -24.956 -22.194  -25.735 1.00 54.24  ? 317 GLY   B CA    1 
ATOM   7366 C C     . GLY   B 2 325 ? -25.609 -22.876  -24.538 1.00 54.14  ? 317 GLY   B C     1 
ATOM   7367 O O     . GLY   B 2 325 ? -26.707 -22.508  -24.126 1.00 55.46  ? 317 GLY   B O     1 
ATOM   7368 N N     . TRP   B 2 326 ? -24.905 -23.863  -23.977 1.00 53.10  ? 318 TRP   B N     1 
ATOM   7369 C CA    . TRP   B 2 326 ? -25.401 -24.611  -22.833 1.00 51.60  ? 318 TRP   B CA    1 
ATOM   7370 C C     . TRP   B 2 326 ? -25.323 -23.784  -21.549 1.00 50.23  ? 318 TRP   B C     1 
ATOM   7371 O O     . TRP   B 2 326 ? -25.887 -24.183  -20.534 1.00 50.56  ? 318 TRP   B O     1 
ATOM   7372 C CB    . TRP   B 2 326 ? -24.644 -25.940  -22.694 1.00 51.22  ? 318 TRP   B CB    1 
ATOM   7373 C CG    . TRP   B 2 326 ? -25.076 -26.990  -23.683 1.00 50.56  ? 318 TRP   B CG    1 
ATOM   7374 C CD1   . TRP   B 2 326 ? -26.061 -26.881  -24.620 1.00 50.56  ? 318 TRP   B CD1   1 
ATOM   7375 C CD2   . TRP   B 2 326 ? -24.567 -28.337  -23.795 1.00 50.18  ? 318 TRP   B CD2   1 
ATOM   7376 N NE1   . TRP   B 2 326 ? -26.185 -28.049  -25.322 1.00 49.54  ? 318 TRP   B NE1   1 
ATOM   7377 C CE2   . TRP   B 2 326 ? -25.287 -28.963  -24.837 1.00 49.37  ? 318 TRP   B CE2   1 
ATOM   7378 C CE3   . TRP   B 2 326 ? -23.581 -29.070  -23.126 1.00 50.00  ? 318 TRP   B CE3   1 
ATOM   7379 C CZ2   . TRP   B 2 326 ? -25.047 -30.280  -25.223 1.00 47.96  ? 318 TRP   B CZ2   1 
ATOM   7380 C CZ3   . TRP   B 2 326 ? -23.349 -30.375  -23.505 1.00 49.51  ? 318 TRP   B CZ3   1 
ATOM   7381 C CH2   . TRP   B 2 326 ? -24.071 -30.968  -24.540 1.00 48.37  ? 318 TRP   B CH2   1 
ATOM   7382 N N     . ASP   B 2 327 ? -24.648 -22.628  -21.601 1.00 49.90  ? 319 ASP   B N     1 
ATOM   7383 C CA    . ASP   B 2 327 ? -24.622 -21.697  -20.483 1.00 49.87  ? 319 ASP   B CA    1 
ATOM   7384 C C     . ASP   B 2 327 ? -25.906 -20.866  -20.438 1.00 51.35  ? 319 ASP   B C     1 
ATOM   7385 O O     . ASP   B 2 327 ? -26.061 -20.021  -19.559 1.00 52.00  ? 319 ASP   B O     1 
ATOM   7386 C CB    . ASP   B 2 327 ? -23.389 -20.807  -20.529 1.00 48.26  ? 319 ASP   B CB    1 
ATOM   7387 C CG    . ASP   B 2 327 ? -23.252 -19.940  -21.770 1.00 47.27  ? 319 ASP   B CG    1 
ATOM   7388 O OD1   . ASP   B 2 327 ? -24.105 -20.065  -22.673 1.00 46.18  ? 319 ASP   B OD1   1 
ATOM   7389 O OD2   . ASP   B 2 327 ? -22.290 -19.150  -21.821 1.00 47.00  ? 319 ASP   B OD2   1 
ATOM   7390 N N     . HIS   B 2 328 ? -26.800 -21.081  -21.412 1.00 52.74  ? 320 HIS   B N     1 
ATOM   7391 C CA    . HIS   B 2 328 ? -28.132 -20.493  -21.426 1.00 53.74  ? 320 HIS   B CA    1 
ATOM   7392 C C     . HIS   B 2 328 ? -28.090 -19.027  -21.860 1.00 53.24  ? 320 HIS   B C     1 
ATOM   7393 O O     . HIS   B 2 328 ? -29.102 -18.336  -21.776 1.00 52.76  ? 320 HIS   B O     1 
ATOM   7394 C CB    . HIS   B 2 328 ? -28.845 -20.673  -20.081 1.00 54.65  ? 320 HIS   B CB    1 
ATOM   7395 C CG    . HIS   B 2 328 ? -30.319 -20.464  -20.174 1.00 56.91  ? 320 HIS   B CG    1 
ATOM   7396 N ND1   . HIS   B 2 328 ? -31.148 -21.374  -20.793 1.00 57.91  ? 320 HIS   B ND1   1 
ATOM   7397 C CD2   . HIS   B 2 328 ? -31.105 -19.454  -19.779 1.00 57.96  ? 320 HIS   B CD2   1 
ATOM   7398 C CE1   . HIS   B 2 328 ? -32.395 -20.931  -20.745 1.00 58.36  ? 320 HIS   B CE1   1 
ATOM   7399 N NE2   . HIS   B 2 328 ? -32.393 -19.767  -20.134 1.00 58.75  ? 320 HIS   B NE2   1 
ATOM   7400 N N     . GLN   B 2 329 ? -26.931 -18.562  -22.341 1.00 52.76  ? 321 GLN   B N     1 
ATOM   7401 C CA    . GLN   B 2 329 ? -26.829 -17.237  -22.927 1.00 52.99  ? 321 GLN   B CA    1 
ATOM   7402 C C     . GLN   B 2 329 ? -27.346 -17.277  -24.362 1.00 52.62  ? 321 GLN   B C     1 
ATOM   7403 O O     . GLN   B 2 329 ? -27.085 -18.231  -25.093 1.00 52.32  ? 321 GLN   B O     1 
ATOM   7404 C CB    . GLN   B 2 329 ? -25.393 -16.717  -22.977 1.00 53.96  ? 321 GLN   B CB    1 
ATOM   7405 C CG    . GLN   B 2 329 ? -24.781 -16.403  -21.617 1.00 55.53  ? 321 GLN   B CG    1 
ATOM   7406 C CD    . GLN   B 2 329 ? -23.420 -15.752  -21.735 1.00 57.16  ? 321 GLN   B CD    1 
ATOM   7407 O OE1   . GLN   B 2 329 ? -22.451 -16.367  -22.193 1.00 57.86  ? 321 GLN   B OE1   1 
ATOM   7408 N NE2   . GLN   B 2 329 ? -23.331 -14.493  -21.332 1.00 58.36  ? 321 GLN   B NE2   1 
ATOM   7409 N N     . VAL   B 2 330 ? -28.109 -16.242  -24.730 1.00 50.69  ? 322 VAL   B N     1 
ATOM   7410 C CA    . VAL   B 2 330 ? -28.309 -15.851  -26.115 1.00 47.94  ? 322 VAL   B CA    1 
ATOM   7411 C C     . VAL   B 2 330 ? -27.462 -14.600  -26.327 1.00 47.16  ? 322 VAL   B C     1 
ATOM   7412 O O     . VAL   B 2 330 ? -27.602 -13.640  -25.575 1.00 48.12  ? 322 VAL   B O     1 
ATOM   7413 C CB    . VAL   B 2 330 ? -29.797 -15.595  -26.424 1.00 46.81  ? 322 VAL   B CB    1 
ATOM   7414 C CG1   . VAL   B 2 330 ? -30.012 -15.096  -27.847 1.00 47.46  ? 322 VAL   B CG1   1 
ATOM   7415 C CG2   . VAL   B 2 330 ? -30.656 -16.825  -26.162 1.00 46.19  ? 322 VAL   B CG2   1 
ATOM   7416 N N     . VAL   B 2 331 ? -26.570 -14.623  -27.323 1.00 46.70  ? 323 VAL   B N     1 
ATOM   7417 C CA    . VAL   B 2 331 ? -25.561 -13.584  -27.459 1.00 47.02  ? 323 VAL   B CA    1 
ATOM   7418 C C     . VAL   B 2 331 ? -25.619 -13.007  -28.870 1.00 49.75  ? 323 VAL   B C     1 
ATOM   7419 O O     . VAL   B 2 331 ? -25.655 -13.752  -29.846 1.00 50.39  ? 323 VAL   B O     1 
ATOM   7420 C CB    . VAL   B 2 331 ? -24.151 -14.110  -27.132 1.00 45.30  ? 323 VAL   B CB    1 
ATOM   7421 C CG1   . VAL   B 2 331 ? -23.098 -13.014  -27.227 1.00 44.94  ? 323 VAL   B CG1   1 
ATOM   7422 C CG2   . VAL   B 2 331 ? -24.100 -14.770  -25.761 1.00 45.43  ? 323 VAL   B CG2   1 
ATOM   7423 N N     . HIS   B 2 332 ? -25.597 -11.669  -28.948 1.00 52.66  ? 324 HIS   B N     1 
ATOM   7424 C CA    . HIS   B 2 332 ? -25.715 -10.938  -30.199 1.00 52.99  ? 324 HIS   B CA    1 
ATOM   7425 C C     . HIS   B 2 332 ? -24.365 -10.308  -30.536 1.00 55.55  ? 324 HIS   B C     1 
ATOM   7426 O O     . HIS   B 2 332 ? -23.923 -9.385   -29.856 1.00 53.34  ? 324 HIS   B O     1 
ATOM   7427 C CB    . HIS   B 2 332 ? -26.828 -9.888   -30.095 1.00 50.61  ? 324 HIS   B CB    1 
ATOM   7428 C CG    . HIS   B 2 332 ? -28.126 -10.435  -29.597 1.00 49.64  ? 324 HIS   B CG    1 
ATOM   7429 N ND1   . HIS   B 2 332 ? -28.939 -11.238  -30.366 1.00 48.58  ? 324 HIS   B ND1   1 
ATOM   7430 C CD2   . HIS   B 2 332 ? -28.738 -10.319  -28.408 1.00 49.07  ? 324 HIS   B CD2   1 
ATOM   7431 C CE1   . HIS   B 2 332 ? -30.012 -11.575  -29.663 1.00 48.42  ? 324 HIS   B CE1   1 
ATOM   7432 N NE2   . HIS   B 2 332 ? -29.911 -11.027  -28.472 1.00 48.21  ? 324 HIS   B NE2   1 
ATOM   7433 N N     . HIS   B 2 333 ? -23.722 -10.825  -31.591 1.00 60.02  ? 325 HIS   B N     1 
ATOM   7434 C CA    . HIS   B 2 333 ? -22.387 -10.406  -31.983 1.00 63.65  ? 325 HIS   B CA    1 
ATOM   7435 C C     . HIS   B 2 333 ? -22.472 -9.415   -33.142 1.00 65.71  ? 325 HIS   B C     1 
ATOM   7436 O O     . HIS   B 2 333 ? -23.306 -9.564   -34.033 1.00 65.08  ? 325 HIS   B O     1 
ATOM   7437 C CB    . HIS   B 2 333 ? -21.530 -11.621  -32.361 1.00 65.48  ? 325 HIS   B CB    1 
ATOM   7438 C CG    . HIS   B 2 333 ? -21.213 -12.526  -31.216 1.00 66.47  ? 325 HIS   B CG    1 
ATOM   7439 N ND1   . HIS   B 2 333 ? -21.996 -13.608  -30.873 1.00 66.31  ? 325 HIS   B ND1   1 
ATOM   7440 C CD2   . HIS   B 2 333 ? -20.197 -12.513  -30.342 1.00 67.08  ? 325 HIS   B CD2   1 
ATOM   7441 C CE1   . HIS   B 2 333 ? -21.461 -14.218  -29.825 1.00 67.11  ? 325 HIS   B CE1   1 
ATOM   7442 N NE2   . HIS   B 2 333 ? -20.369 -13.569  -29.485 1.00 67.30  ? 325 HIS   B NE2   1 
ATOM   7443 N N     . VAL   B 2 334 ? -21.586 -8.411   -33.108 1.00 68.53  ? 326 VAL   B N     1 
ATOM   7444 C CA    . VAL   B 2 334 ? -21.457 -7.420   -34.164 1.00 69.57  ? 326 VAL   B CA    1 
ATOM   7445 C C     . VAL   B 2 334 ? -20.125 -7.659   -34.871 1.00 71.37  ? 326 VAL   B C     1 
ATOM   7446 O O     . VAL   B 2 334 ? -19.072 -7.648   -34.236 1.00 71.13  ? 326 VAL   B O     1 
ATOM   7447 C CB    . VAL   B 2 334 ? -21.580 -5.999   -33.576 1.00 69.11  ? 326 VAL   B CB    1 
ATOM   7448 C CG1   . VAL   B 2 334 ? -20.913 -4.936   -34.442 1.00 68.65  ? 326 VAL   B CG1   1 
ATOM   7449 C CG2   . VAL   B 2 334 ? -23.037 -5.638   -33.307 1.00 68.59  ? 326 VAL   B CG2   1 
ATOM   7450 N N     . VAL   B 2 335 ? -20.195 -7.863   -36.193 1.00 73.20  ? 327 VAL   B N     1 
ATOM   7451 C CA    . VAL   B 2 335 ? -19.115 -8.471   -36.953 1.00 74.82  ? 327 VAL   B CA    1 
ATOM   7452 C C     . VAL   B 2 335 ? -18.489 -7.429   -37.878 1.00 76.80  ? 327 VAL   B C     1 
ATOM   7453 O O     . VAL   B 2 335 ? -19.153 -6.940   -38.792 1.00 78.22  ? 327 VAL   B O     1 
ATOM   7454 C CB    . VAL   B 2 335 ? -19.666 -9.672   -37.748 1.00 75.34  ? 327 VAL   B CB    1 
ATOM   7455 C CG1   . VAL   B 2 335 ? -18.563 -10.435  -38.473 1.00 74.96  ? 327 VAL   B CG1   1 
ATOM   7456 C CG2   . VAL   B 2 335 ? -20.470 -10.620  -36.865 1.00 75.61  ? 327 VAL   B CG2   1 
ATOM   7457 N N     . PRO   B 2 336 ? -17.206 -7.045   -37.664 1.00 77.68  ? 328 PRO   B N     1 
ATOM   7458 C CA    . PRO   B 2 336 ? -16.468 -6.237   -38.639 1.00 77.35  ? 328 PRO   B CA    1 
ATOM   7459 C C     . PRO   B 2 336 ? -16.367 -6.922   -40.000 1.00 76.81  ? 328 PRO   B C     1 
ATOM   7460 O O     . PRO   B 2 336 ? -17.180 -6.587   -40.886 1.00 77.96  ? 328 PRO   B O     1 
ATOM   7461 C CB    . PRO   B 2 336 ? -15.082 -6.047   -37.987 1.00 77.37  ? 328 PRO   B CB    1 
ATOM   7462 C CG    . PRO   B 2 336 ? -15.325 -6.268   -36.510 1.00 77.06  ? 328 PRO   B CG    1 
ATOM   7463 C CD    . PRO   B 2 336 ? -16.422 -7.316   -36.448 1.00 77.37  ? 328 PRO   B CD    1 
HETATM 7464 N N1    . A1BLF C 3 .   ? -23.815 -85.489  -8.490  1.00 29.11  ? 701 A1BLF A N1    1 
HETATM 7465 N N3    . A1BLF C 3 .   ? -26.354 -87.034  -12.098 1.00 33.71  ? 701 A1BLF A N3    1 
HETATM 7466 C C4    . A1BLF C 3 .   ? -22.868 -85.899  -7.434  1.00 29.21  ? 701 A1BLF A C4    1 
HETATM 7467 C C5    . A1BLF C 3 .   ? -25.106 -85.017  -7.958  1.00 29.06  ? 701 A1BLF A C5    1 
HETATM 7468 C C6    . A1BLF C 3 .   ? -25.752 -86.101  -7.089  1.00 29.15  ? 701 A1BLF A C6    1 
HETATM 7469 C C7    . A1BLF C 3 .   ? -23.872 -86.274  -9.642  1.00 29.84  ? 701 A1BLF A C7    1 
HETATM 7470 C C8    . A1BLF C 3 .   ? -25.132 -87.033  -11.451 1.00 31.74  ? 701 A1BLF A C8    1 
HETATM 7471 C C10   . A1BLF C 3 .   ? -28.605 -85.956  -12.548 1.00 38.99  ? 701 A1BLF A C10   1 
HETATM 7472 C C13   . A1BLF C 3 .   ? -30.990 -88.072  -10.265 1.00 42.86  ? 701 A1BLF A C13   1 
HETATM 7473 C C15   . A1BLF C 3 .   ? -22.837 -87.671  -11.189 1.00 28.78  ? 701 A1BLF A C15   1 
HETATM 7474 C C17   . A1BLF C 3 .   ? -19.790 -89.914  -10.897 1.00 25.75  ? 701 A1BLF A C17   1 
HETATM 7475 C C20   . A1BLF C 3 .   ? -20.860 -92.253  -9.113  1.00 26.36  ? 701 A1BLF A C20   1 
HETATM 7476 C C21   . A1BLF C 3 .   ? -21.745 -93.287  -8.433  1.00 26.92  ? 701 A1BLF A C21   1 
HETATM 7477 C C22   . A1BLF C 3 .   ? -21.626 -93.500  -7.055  1.00 26.93  ? 701 A1BLF A C22   1 
HETATM 7478 C C24   . A1BLF C 3 .   ? -23.342 -95.206  -7.128  1.00 27.62  ? 701 A1BLF A C24   1 
HETATM 7479 C C26   . A1BLF C 3 .   ? -25.321 -98.066  -5.963  1.00 26.83  ? 701 A1BLF A C26   1 
HETATM 7480 C C28   . A1BLF C 3 .   ? -24.965 -99.247  -5.399  1.00 26.30  ? 701 A1BLF A C28   1 
HETATM 7481 C C1    . A1BLF C 3 .   ? -25.419 -87.549  -5.053  1.00 28.76  ? 701 A1BLF A C1    1 
HETATM 7482 C C2    . A1BLF C 3 .   ? -24.798 -86.466  -5.944  1.00 28.85  ? 701 A1BLF A C2    1 
HETATM 7483 C C3    . A1BLF C 3 .   ? -23.484 -86.982  -6.540  1.00 29.15  ? 701 A1BLF A C3    1 
HETATM 7484 N N2    . A1BLF C 3 .   ? -25.005 -86.322  -10.330 1.00 31.18  ? 701 A1BLF A N2    1 
HETATM 7485 C C9    . A1BLF C 3 .   ? -27.352 -86.048  -11.663 1.00 37.12  ? 701 A1BLF A C9    1 
HETATM 7486 N N4    . A1BLF C 3 .   ? -29.322 -86.728  -11.515 1.00 40.66  ? 701 A1BLF A N4    1 
HETATM 7487 C C11   . A1BLF C 3 .   ? -28.248 -86.540  -10.517 1.00 38.65  ? 701 A1BLF A C11   1 
HETATM 7488 C C12   . A1BLF C 3 .   ? -30.513 -87.359  -11.502 1.00 42.96  ? 701 A1BLF A C12   1 
HETATM 7489 O O1    . A1BLF C 3 .   ? -31.208 -87.347  -12.498 1.00 45.01  ? 701 A1BLF A O1    1 
HETATM 7490 C C14   . A1BLF C 3 .   ? -24.025 -87.754  -11.924 1.00 30.20  ? 701 A1BLF A C14   1 
HETATM 7491 N N5    . A1BLF C 3 .   ? -22.802 -86.937  -10.072 1.00 29.32  ? 701 A1BLF A N5    1 
HETATM 7492 C C16   . A1BLF C 3 .   ? -21.627 -88.421  -11.601 1.00 27.16  ? 701 A1BLF A C16   1 
HETATM 7493 O O2    . A1BLF C 3 .   ? -21.249 -88.423  -12.758 1.00 25.80  ? 701 A1BLF A O2    1 
HETATM 7494 N N6    . A1BLF C 3 .   ? -20.986 -89.111  -10.634 1.00 25.90  ? 701 A1BLF A N6    1 
HETATM 7495 C C18   . A1BLF C 3 .   ? -20.218 -91.283  -11.437 1.00 25.99  ? 701 A1BLF A C18   1 
HETATM 7496 O O3    . A1BLF C 3 .   ? -19.050 -92.103  -11.554 1.00 25.50  ? 701 A1BLF A O3    1 
HETATM 7497 C C19   . A1BLF C 3 .   ? -21.306 -91.953  -10.559 1.00 26.62  ? 701 A1BLF A C19   1 
HETATM 7498 C C23   . A1BLF C 3 .   ? -22.415 -94.448  -6.411  1.00 27.00  ? 701 A1BLF A C23   1 
HETATM 7499 O O4    . A1BLF C 3 .   ? -24.112 -96.120  -6.461  1.00 27.20  ? 701 A1BLF A O4    1 
HETATM 7500 C C25   . A1BLF C 3 .   ? -24.732 -97.259  -7.093  1.00 27.27  ? 701 A1BLF A C25   1 
HETATM 7501 O O5    . A1BLF C 3 .   ? -26.376 -97.620  -5.267  1.00 27.40  ? 701 A1BLF A O5    1 
HETATM 7502 C C27   . A1BLF C 3 .   ? -26.651 -98.520  -4.318  1.00 27.49  ? 701 A1BLF A C27   1 
HETATM 7503 N N7    . A1BLF C 3 .   ? -25.809 -99.494  -4.402  1.00 26.89  ? 701 A1BLF A N7    1 
HETATM 7504 C C29   . A1BLF C 3 .   ? -23.882 -100.224 -5.735  1.00 26.39  ? 701 A1BLF A C29   1 
HETATM 7505 C C30   . A1BLF C 3 .   ? -23.461 -94.989  -8.498  1.00 26.98  ? 701 A1BLF A C30   1 
HETATM 7506 C C31   . A1BLF C 3 .   ? -22.664 -94.038  -9.141  1.00 27.01  ? 701 A1BLF A C31   1 
HETATM 7507 C C32   . A1BLF C 3 .   ? -22.857 -93.857  -10.624 1.00 27.15  ? 701 A1BLF A C32   1 
HETATM 7508 N N8    . A1BLF C 3 .   ? -21.694 -93.207  -11.243 1.00 26.93  ? 701 A1BLF A N8    1 
HETATM 7509 C CS    . MTA   D 4 .   ? -21.712 -98.327  -6.342  1.00 28.64  ? 702 MTA   A CS    1 
HETATM 7510 S "S5'" . MTA   D 4 .   ? -20.159 -97.612  -6.839  1.00 29.36  ? 702 MTA   A "S5'" 1 
HETATM 7511 C "C5'" . MTA   D 4 .   ? -19.033 -98.969  -6.416  1.00 27.46  ? 702 MTA   A "C5'" 1 
HETATM 7512 C "C4'" . MTA   D 4 .   ? -19.362 -99.742  -5.155  1.00 26.98  ? 702 MTA   A "C4'" 1 
HETATM 7513 O "O4'" . MTA   D 4 .   ? -18.379 -100.787 -4.985  1.00 26.42  ? 702 MTA   A "O4'" 1 
HETATM 7514 C "C2'" . MTA   D 4 .   ? -17.969 -99.241  -3.263  1.00 26.73  ? 702 MTA   A "C2'" 1 
HETATM 7515 O "O2'" . MTA   D 4 .   ? -17.938 -99.157  -1.853  1.00 27.79  ? 702 MTA   A "O2'" 1 
HETATM 7516 C "C3'" . MTA   D 4 .   ? -19.346 -98.929  -3.859  1.00 26.62  ? 702 MTA   A "C3'" 1 
HETATM 7517 O "O3'" . MTA   D 4 .   ? -20.409 -99.339  -3.007  1.00 26.12  ? 702 MTA   A "O3'" 1 
HETATM 7518 C "C1'" . MTA   D 4 .   ? -17.744 -100.673 -3.735  1.00 26.05  ? 702 MTA   A "C1'" 1 
HETATM 7519 N N9    . MTA   D 4 .   ? -16.342 -101.018 -3.926  1.00 25.57  ? 702 MTA   A N9    1 
HETATM 7520 C C8    . MTA   D 4 .   ? -15.406 -100.283 -4.608  1.00 25.91  ? 702 MTA   A C8    1 
HETATM 7521 N N7    . MTA   D 4 .   ? -14.220 -100.837 -4.627  1.00 25.65  ? 702 MTA   A N7    1 
HETATM 7522 C C5    . MTA   D 4 .   ? -14.384 -102.017 -3.922  1.00 25.04  ? 702 MTA   A C5    1 
HETATM 7523 C C6    . MTA   D 4 .   ? -13.487 -103.049 -3.592  1.00 25.50  ? 702 MTA   A C6    1 
HETATM 7524 N N6    . MTA   D 4 .   ? -12.209 -103.061 -3.959  1.00 25.83  ? 702 MTA   A N6    1 
HETATM 7525 N N1    . MTA   D 4 .   ? -13.974 -104.094 -2.884  1.00 26.27  ? 702 MTA   A N1    1 
HETATM 7526 C C2    . MTA   D 4 .   ? -15.266 -104.080 -2.529  1.00 26.22  ? 702 MTA   A C2    1 
HETATM 7527 N N3    . MTA   D 4 .   ? -16.198 -103.163 -2.778  1.00 25.58  ? 702 MTA   A N3    1 
HETATM 7528 C C4    . MTA   D 4 .   ? -15.690 -102.145 -3.490  1.00 25.09  ? 702 MTA   A C4    1 
HETATM 7529 C C1    . EDO   E 5 .   ? -25.129 -57.874  -35.756 1.00 40.67  ? 703 EDO   A C1    1 
HETATM 7530 O O1    . EDO   E 5 .   ? -25.944 -58.999  -36.033 1.00 40.48  ? 703 EDO   A O1    1 
HETATM 7531 C C2    . EDO   E 5 .   ? -25.862 -56.596  -35.571 1.00 40.96  ? 703 EDO   A C2    1 
HETATM 7532 O O2    . EDO   E 5 .   ? -25.027 -55.453  -35.682 1.00 40.99  ? 703 EDO   A O2    1 
HETATM 7533 C C1    . EDO   F 5 .   ? -19.752 -96.126  -10.112 1.00 39.62  ? 704 EDO   A C1    1 
HETATM 7534 O O1    . EDO   F 5 .   ? -19.649 -94.864  -10.746 1.00 38.15  ? 704 EDO   A O1    1 
HETATM 7535 C C2    . EDO   F 5 .   ? -21.066 -96.806  -10.313 1.00 39.12  ? 704 EDO   A C2    1 
HETATM 7536 O O2    . EDO   F 5 .   ? -21.149 -97.643  -11.456 1.00 38.57  ? 704 EDO   A O2    1 
HETATM 7537 C C1    . EDO   G 5 .   ? -15.658 -71.397  -29.613 1.00 28.13  ? 705 EDO   A C1    1 
HETATM 7538 O O1    . EDO   G 5 .   ? -15.371 -72.301  -30.667 1.00 27.71  ? 705 EDO   A O1    1 
HETATM 7539 C C2    . EDO   G 5 .   ? -14.656 -70.310  -29.489 1.00 28.16  ? 705 EDO   A C2    1 
HETATM 7540 O O2    . EDO   G 5 .   ? -14.521 -69.551  -30.675 1.00 28.62  ? 705 EDO   A O2    1 
HETATM 7541 C C1    . EDO   H 5 .   ? -16.068 -71.423  -36.302 1.00 45.99  ? 706 EDO   A C1    1 
HETATM 7542 O O1    . EDO   H 5 .   ? -14.707 -71.033  -36.403 1.00 47.06  ? 706 EDO   A O1    1 
HETATM 7543 C C2    . EDO   H 5 .   ? -16.587 -71.669  -34.920 1.00 45.70  ? 706 EDO   A C2    1 
HETATM 7544 O O2    . EDO   H 5 .   ? -15.633 -72.089  -33.950 1.00 44.67  ? 706 EDO   A O2    1 
HETATM 7545 C C1    . EDO   I 5 .   ? -15.133 -79.224  -7.007  1.00 44.67  ? 707 EDO   A C1    1 
HETATM 7546 O O1    . EDO   I 5 .   ? -16.205 -79.054  -6.099  1.00 44.99  ? 707 EDO   A O1    1 
HETATM 7547 C C2    . EDO   I 5 .   ? -13.985 -78.321  -6.756  1.00 44.68  ? 707 EDO   A C2    1 
HETATM 7548 O O2    . EDO   I 5 .   ? -14.142 -77.034  -7.315  1.00 44.96  ? 707 EDO   A O2    1 
HETATM 7549 C C1    . EDO   J 5 .   ? -4.013  -40.423  -20.553 1.00 48.44  ? 708 EDO   A C1    1 
HETATM 7550 O O1    . EDO   J 5 .   ? -4.427  -39.952  -19.286 1.00 47.88  ? 708 EDO   A O1    1 
HETATM 7551 C C2    . EDO   J 5 .   ? -2.695  -41.101  -20.527 1.00 48.54  ? 708 EDO   A C2    1 
HETATM 7552 O O2    . EDO   J 5 .   ? -1.633  -40.178  -20.541 1.00 49.59  ? 708 EDO   A O2    1 
HETATM 7553 C C1    . EDO   K 5 .   ? -8.827  -99.072  0.469   1.00 43.34  ? 709 EDO   A C1    1 
HETATM 7554 O O1    . EDO   K 5 .   ? -7.449  -99.295  0.704   1.00 43.89  ? 709 EDO   A O1    1 
HETATM 7555 C C2    . EDO   K 5 .   ? -9.657  -100.280 0.718   1.00 43.17  ? 709 EDO   A C2    1 
HETATM 7556 O O2    . EDO   K 5 .   ? -11.040 -100.014 0.855   1.00 42.27  ? 709 EDO   A O2    1 
HETATM 7557 C C1    . EDO   L 5 .   ? 0.866   -94.202  -27.993 1.00 36.90  ? 710 EDO   A C1    1 
HETATM 7558 O O1    . EDO   L 5 .   ? 1.283   -93.030  -28.668 1.00 37.57  ? 710 EDO   A O1    1 
HETATM 7559 C C2    . EDO   L 5 .   ? -0.174  -94.979  -28.723 1.00 36.74  ? 710 EDO   A C2    1 
HETATM 7560 O O2    . EDO   L 5 .   ? -0.978  -94.195  -29.591 1.00 36.41  ? 710 EDO   A O2    1 
HETATM 7561 C C1    . EDO   M 5 .   ? -12.675 -92.660  -34.824 1.00 43.39  ? 711 EDO   A C1    1 
HETATM 7562 O O1    . EDO   M 5 .   ? -13.306 -92.203  -33.643 1.00 42.54  ? 711 EDO   A O1    1 
HETATM 7563 C C2    . EDO   M 5 .   ? -11.503 -93.533  -34.554 1.00 43.39  ? 711 EDO   A C2    1 
HETATM 7564 O O2    . EDO   M 5 .   ? -11.801 -94.672  -33.761 1.00 42.37  ? 711 EDO   A O2    1 
HETATM 7565 C C1    . EDO   N 5 .   ? -20.048 -36.737  -10.835 1.00 34.49  ? 712 EDO   A C1    1 
HETATM 7566 O O1    . EDO   N 5 .   ? -21.244 -36.132  -11.287 1.00 34.19  ? 712 EDO   A O1    1 
HETATM 7567 C C2    . EDO   N 5 .   ? -20.228 -38.107  -10.283 1.00 34.83  ? 712 EDO   A C2    1 
HETATM 7568 O O2    . EDO   N 5 .   ? -21.490 -38.690  -10.557 1.00 35.31  ? 712 EDO   A O2    1 
HETATM 7569 C C1    . EDO   O 5 .   ? -21.347 -50.389  -12.098 1.00 39.66  ? 713 EDO   A C1    1 
HETATM 7570 O O1    . EDO   O 5 .   ? -20.185 -50.727  -11.366 1.00 38.62  ? 713 EDO   A O1    1 
HETATM 7571 C C2    . EDO   O 5 .   ? -22.469 -51.348  -11.905 1.00 40.22  ? 713 EDO   A C2    1 
HETATM 7572 O O2    . EDO   O 5 .   ? -22.292 -52.588  -12.573 1.00 41.25  ? 713 EDO   A O2    1 
HETATM 7573 C C1    . EDO   P 5 .   ? -11.993 -59.135  -9.901  1.00 37.30  ? 714 EDO   A C1    1 
HETATM 7574 O O1    . EDO   P 5 .   ? -13.189 -59.337  -9.164  1.00 37.24  ? 714 EDO   A O1    1 
HETATM 7575 C C2    . EDO   P 5 .   ? -12.063 -59.623  -11.306 1.00 36.91  ? 714 EDO   A C2    1 
HETATM 7576 O O2    . EDO   P 5 .   ? -12.655 -60.907  -11.437 1.00 36.64  ? 714 EDO   A O2    1 
HETATM 7577 C C1    . EDO   Q 5 .   ? -25.103 -70.046  -19.743 1.00 54.02  ? 715 EDO   A C1    1 
HETATM 7578 O O1    . EDO   Q 5 .   ? -24.723 -71.408  -19.718 1.00 53.85  ? 715 EDO   A O1    1 
HETATM 7579 C C2    . EDO   Q 5 .   ? -24.135 -69.174  -20.460 1.00 54.41  ? 715 EDO   A C2    1 
HETATM 7580 O O2    . EDO   Q 5 .   ? -22.798 -69.321  -20.019 1.00 53.47  ? 715 EDO   A O2    1 
HETATM 7581 C C1    . EDO   R 5 .   ? -32.111 -80.830  -12.093 1.00 46.05  ? 716 EDO   A C1    1 
HETATM 7582 O O1    . EDO   R 5 .   ? -30.724 -80.615  -12.280 1.00 44.91  ? 716 EDO   A O1    1 
HETATM 7583 C C2    . EDO   R 5 .   ? -32.568 -82.115  -12.655 1.00 46.08  ? 716 EDO   A C2    1 
HETATM 7584 O O2    . EDO   R 5 .   ? -31.975 -83.263  -12.060 1.00 44.91  ? 716 EDO   A O2    1 
HETATM 7585 C C1    . EDO   S 5 .   ? -12.709 -36.596  -42.285 1.00 60.81  ? 401 EDO   B C1    1 
HETATM 7586 O O1    . EDO   S 5 .   ? -11.369 -36.203  -42.059 1.00 61.58  ? 401 EDO   B O1    1 
HETATM 7587 C C2    . EDO   S 5 .   ? -12.859 -37.584  -43.385 1.00 59.65  ? 401 EDO   B C2    1 
HETATM 7588 O O2    . EDO   S 5 .   ? -11.982 -37.367  -44.473 1.00 59.28  ? 401 EDO   B O2    1 
HETATM 7589 O O     . HOH   T 6 .   ? -9.302  -94.676  -3.597  1.00 34.44  ? 801 HOH   A O     1 
HETATM 7590 O O     . HOH   T 6 .   ? -11.944 -63.082  -12.094 1.00 28.62  ? 802 HOH   A O     1 
HETATM 7591 O O     . HOH   T 6 .   ? -23.475 -104.764 9.386   1.00 30.78  ? 803 HOH   A O     1 
HETATM 7592 O O     . HOH   T 6 .   ? -9.612  -93.777  -19.450 1.00 25.91  ? 804 HOH   A O     1 
HETATM 7593 O O     . HOH   T 6 .   ? -16.812 -100.676 -25.098 1.00 33.89  ? 805 HOH   A O     1 
HETATM 7594 O O     . HOH   T 6 .   ? -13.342 -97.264  -12.768 1.00 32.39  ? 806 HOH   A O     1 
HETATM 7595 O O     . HOH   T 6 .   ? -11.719 -86.630  -33.898 1.00 23.85  ? 807 HOH   A O     1 
HETATM 7596 O O     . HOH   T 6 .   ? -19.592 -31.217  -16.296 1.00 33.11  ? 808 HOH   A O     1 
HETATM 7597 O O     . HOH   T 6 .   ? -17.046 -82.526  -33.626 1.00 35.24  ? 809 HOH   A O     1 
HETATM 7598 O O     . HOH   T 6 .   ? -5.591  -62.616  -20.056 1.00 23.99  ? 810 HOH   A O     1 
HETATM 7599 O O     . HOH   T 6 .   ? -21.984 -81.017  -13.200 1.00 34.47  ? 811 HOH   A O     1 
HETATM 7600 O O     . HOH   T 6 .   ? -6.325  -99.146  -23.879 1.00 19.49  ? 812 HOH   A O     1 
HETATM 7601 O O     . HOH   T 6 .   ? -19.095 -41.128  -10.347 1.00 27.83  ? 813 HOH   A O     1 
HETATM 7602 O O     . HOH   T 6 .   ? -10.405 -68.188  -24.136 1.00 33.23  ? 814 HOH   A O     1 
HETATM 7603 O O     . HOH   T 6 .   ? -8.831  -92.906  -32.833 1.00 31.33  ? 815 HOH   A O     1 
HETATM 7604 O O     . HOH   T 6 .   ? -7.007  -112.055 -8.957  1.00 38.56  ? 816 HOH   A O     1 
HETATM 7605 O O     . HOH   T 6 .   ? -23.187 -38.244  -21.040 1.00 24.84  ? 817 HOH   A O     1 
HETATM 7606 O O     . HOH   T 6 .   ? -21.269 -49.768  -51.160 1.00 24.69  ? 818 HOH   A O     1 
HETATM 7607 O O     . HOH   T 6 .   ? -41.750 -56.706  -41.114 1.00 46.70  ? 819 HOH   A O     1 
HETATM 7608 O O     . HOH   T 6 .   ? -13.810 -69.501  -25.926 1.00 29.67  ? 820 HOH   A O     1 
HETATM 7609 O O     . HOH   T 6 .   ? -18.679 -58.419  -39.045 1.00 23.65  ? 821 HOH   A O     1 
HETATM 7610 O O     . HOH   T 6 .   ? -26.778 -53.452  -50.375 1.00 35.27  ? 822 HOH   A O     1 
HETATM 7611 O O     . HOH   T 6 .   ? -31.284 -128.411 -22.917 1.00 38.34  ? 823 HOH   A O     1 
HETATM 7612 O O     . HOH   T 6 .   ? -5.889  -89.902  -33.301 1.00 19.60  ? 824 HOH   A O     1 
HETATM 7613 O O     . HOH   T 6 .   ? -25.306 -91.150  -17.620 1.00 34.18  ? 825 HOH   A O     1 
HETATM 7614 O O     . HOH   T 6 .   ? -18.660 -29.784  -18.437 1.00 43.34  ? 826 HOH   A O     1 
HETATM 7615 O O     . HOH   T 6 .   ? -4.845  -74.131  -6.129  1.00 19.28  ? 827 HOH   A O     1 
HETATM 7616 O O     . HOH   T 6 .   ? -6.648  -65.410  -23.818 1.00 26.10  ? 828 HOH   A O     1 
HETATM 7617 O O     . HOH   T 6 .   ? -19.664 -102.606 -7.916  1.00 26.48  ? 829 HOH   A O     1 
HETATM 7618 O O     . HOH   T 6 .   ? -16.326 -111.449 -19.071 1.00 27.75  ? 830 HOH   A O     1 
HETATM 7619 O O     . HOH   T 6 .   ? -21.332 -52.569  -29.758 1.00 35.36  ? 831 HOH   A O     1 
HETATM 7620 O O     . HOH   T 6 .   ? -23.903 -103.450 -7.081  1.00 43.27  ? 832 HOH   A O     1 
HETATM 7621 O O     . HOH   T 6 .   ? -25.140 -42.997  -18.834 1.00 39.14  ? 833 HOH   A O     1 
HETATM 7622 O O     . HOH   T 6 .   ? -17.030 -102.645 -13.177 1.00 29.67  ? 834 HOH   A O     1 
HETATM 7623 O O     . HOH   T 6 .   ? -21.239 -83.833  -23.688 1.00 24.94  ? 835 HOH   A O     1 
HETATM 7624 O O     . HOH   T 6 .   ? -32.160 -90.246  -8.247  1.00 34.88  ? 836 HOH   A O     1 
HETATM 7625 O O     . HOH   T 6 .   ? -16.774 -95.052  6.727   1.00 19.84  ? 837 HOH   A O     1 
HETATM 7626 O O     . HOH   T 6 .   ? -17.708 -96.602  -0.960  1.00 30.79  ? 838 HOH   A O     1 
HETATM 7627 O O     . HOH   T 6 .   ? -24.894 -97.182  -27.140 1.00 29.00  ? 839 HOH   A O     1 
HETATM 7628 O O     . HOH   T 6 .   ? -22.986 -55.831  -7.388  1.00 44.21  ? 840 HOH   A O     1 
HETATM 7629 O O     . HOH   T 6 .   ? -33.184 -95.282  -4.126  1.00 37.02  ? 841 HOH   A O     1 
HETATM 7630 O O     . HOH   T 6 .   ? -1.705  -78.798  -36.048 1.00 33.27  ? 842 HOH   A O     1 
HETATM 7631 O O     . HOH   T 6 .   ? -10.360 -57.238  -7.981  1.00 43.73  ? 843 HOH   A O     1 
HETATM 7632 O O     . HOH   T 6 .   ? -7.432  -54.028  -27.956 1.00 27.27  ? 844 HOH   A O     1 
HETATM 7633 O O     . HOH   T 6 .   ? -11.200 -106.556 3.116   1.00 31.67  ? 845 HOH   A O     1 
HETATM 7634 O O     . HOH   T 6 .   ? -26.687 -69.187  -39.966 1.00 32.84  ? 846 HOH   A O     1 
HETATM 7635 O O     . HOH   T 6 .   ? -13.177 -46.357  -10.042 1.00 39.22  ? 847 HOH   A O     1 
HETATM 7636 O O     . HOH   T 6 .   ? -26.260 -79.804  -20.875 1.00 34.94  ? 848 HOH   A O     1 
HETATM 7637 O O     . HOH   T 6 .   ? -12.747 -45.354  -28.069 1.00 30.45  ? 849 HOH   A O     1 
HETATM 7638 O O     . HOH   T 6 .   ? 4.077   -90.307  -7.004  1.00 33.88  ? 850 HOH   A O     1 
HETATM 7639 O O     . HOH   T 6 .   ? -18.176 -63.537  -17.096 1.00 27.37  ? 851 HOH   A O     1 
HETATM 7640 O O     . HOH   T 6 .   ? -23.356 -69.172  -30.284 1.00 25.77  ? 852 HOH   A O     1 
HETATM 7641 O O     . HOH   T 6 .   ? -27.913 -62.591  -17.481 1.00 51.44  ? 853 HOH   A O     1 
HETATM 7642 O O     . HOH   T 6 .   ? -27.968 -98.170  -23.955 1.00 38.66  ? 854 HOH   A O     1 
HETATM 7643 O O     . HOH   T 6 .   ? -33.912 -103.510 -14.036 1.00 38.74  ? 855 HOH   A O     1 
HETATM 7644 O O     . HOH   T 6 .   ? -7.135  -113.232 -1.430  1.00 38.40  ? 856 HOH   A O     1 
HETATM 7645 O O     . HOH   T 6 .   ? -11.433 -55.800  -36.813 1.00 36.38  ? 857 HOH   A O     1 
HETATM 7646 O O     . HOH   T 6 .   ? -22.313 -97.898  -27.397 1.00 34.17  ? 858 HOH   A O     1 
HETATM 7647 O O     . HOH   T 6 .   ? -27.299 -102.343 -25.400 1.00 36.02  ? 859 HOH   A O     1 
HETATM 7648 O O     . HOH   T 6 .   ? -21.576 -107.278 9.918   1.00 32.07  ? 860 HOH   A O     1 
HETATM 7649 O O     . HOH   T 6 .   ? -2.172  -99.666  -11.621 1.00 32.95  ? 861 HOH   A O     1 
HETATM 7650 O O     . HOH   T 6 .   ? -30.657 -58.278  -14.920 1.00 23.83  ? 862 HOH   A O     1 
HETATM 7651 O O     . HOH   T 6 .   ? -14.013 -64.693  -20.641 1.00 22.62  ? 863 HOH   A O     1 
HETATM 7652 O O     . HOH   T 6 .   ? -20.841 -89.816  -1.123  1.00 13.01  ? 864 HOH   A O     1 
HETATM 7653 O O     . HOH   T 6 .   ? -20.987 -45.203  -28.808 1.00 31.76  ? 865 HOH   A O     1 
HETATM 7654 O O     . HOH   T 6 .   ? -10.549 -54.971  -27.999 1.00 32.82  ? 866 HOH   A O     1 
HETATM 7655 O O     . HOH   T 6 .   ? -10.017 -50.039  -33.844 1.00 30.09  ? 867 HOH   A O     1 
HETATM 7656 O O     . HOH   T 6 .   ? -22.206 -55.143  -46.391 1.00 28.94  ? 868 HOH   A O     1 
HETATM 7657 O O     . HOH   T 6 .   ? -16.271 -52.015  -8.892  1.00 44.38  ? 869 HOH   A O     1 
HETATM 7658 O O     . HOH   T 6 .   ? -15.036 -103.913 5.180   1.00 29.53  ? 870 HOH   A O     1 
HETATM 7659 O O     . HOH   T 6 .   ? -16.530 -90.187  -12.421 1.00 26.93  ? 871 HOH   A O     1 
HETATM 7660 O O     . HOH   T 6 .   ? -8.760  -97.913  -27.403 1.00 35.47  ? 872 HOH   A O     1 
HETATM 7661 O O     . HOH   T 6 .   ? 0.518   -101.750 -13.428 1.00 25.01  ? 873 HOH   A O     1 
HETATM 7662 O O     . HOH   T 6 .   ? -22.769 -50.143  -29.375 1.00 35.26  ? 874 HOH   A O     1 
HETATM 7663 O O     . HOH   T 6 .   ? -16.521 -66.168  -17.283 1.00 25.04  ? 875 HOH   A O     1 
HETATM 7664 O O     . HOH   T 6 .   ? -31.123 -92.175  3.104   1.00 27.62  ? 876 HOH   A O     1 
HETATM 7665 O O     . HOH   T 6 .   ? -1.170  -100.223 -9.109  1.00 35.27  ? 877 HOH   A O     1 
HETATM 7666 O O     . HOH   T 6 .   ? -20.792 -103.787 8.698   1.00 30.03  ? 878 HOH   A O     1 
HETATM 7667 O O     . HOH   T 6 .   ? -11.420 -112.944 3.438   1.00 40.94  ? 879 HOH   A O     1 
HETATM 7668 O O     . HOH   T 6 .   ? -26.937 -89.603  3.648   1.00 29.61  ? 880 HOH   A O     1 
HETATM 7669 O O     . HOH   T 6 .   ? -11.564 -95.506  -6.413  1.00 35.94  ? 881 HOH   A O     1 
HETATM 7670 O O     . HOH   T 6 .   ? -25.122 -60.971  -15.553 1.00 37.94  ? 882 HOH   A O     1 
HETATM 7671 O O     . HOH   T 6 .   ? -21.357 -78.324  -28.126 1.00 36.90  ? 883 HOH   A O     1 
HETATM 7672 O O     . HOH   T 6 .   ? -5.796  -69.623  -11.160 1.00 32.94  ? 884 HOH   A O     1 
HETATM 7673 O O     . HOH   T 6 .   ? -10.590 -42.006  -33.322 1.00 26.25  ? 885 HOH   A O     1 
HETATM 7674 O O     . HOH   T 6 .   ? -4.868  -67.105  -19.191 1.00 28.30  ? 886 HOH   A O     1 
HETATM 7675 O O     . HOH   T 6 .   ? -14.473 -79.343  -36.410 1.00 32.45  ? 887 HOH   A O     1 
HETATM 7676 O O     . HOH   T 6 .   ? -10.769 -84.416  -8.142  1.00 26.69  ? 888 HOH   A O     1 
HETATM 7677 O O     . HOH   T 6 .   ? -17.776 -51.973  -38.019 1.00 28.42  ? 889 HOH   A O     1 
HETATM 7678 O O     . HOH   T 6 .   ? -21.358 -67.246  -18.089 1.00 40.40  ? 890 HOH   A O     1 
HETATM 7679 O O     . HOH   T 6 .   ? -6.945  -86.425  -4.942  1.00 29.32  ? 891 HOH   A O     1 
HETATM 7680 O O     . HOH   T 6 .   ? -14.481 -98.275  -7.081  1.00 34.20  ? 892 HOH   A O     1 
HETATM 7681 O O     . HOH   T 6 .   ? -18.286 -33.461  -15.041 1.00 23.29  ? 893 HOH   A O     1 
HETATM 7682 O O     . HOH   T 6 .   ? -16.937 -37.242  -10.890 1.00 26.75  ? 894 HOH   A O     1 
HETATM 7683 O O     . HOH   T 6 .   ? -10.224 -118.528 -5.633  1.00 36.52  ? 895 HOH   A O     1 
HETATM 7684 O O     . HOH   T 6 .   ? 0.120   -75.519  -20.211 1.00 20.60  ? 896 HOH   A O     1 
HETATM 7685 O O     . HOH   T 6 .   ? -17.007 -103.831 -28.347 1.00 29.31  ? 897 HOH   A O     1 
HETATM 7686 O O     . HOH   T 6 .   ? -23.793 -59.898  -43.342 1.00 39.06  ? 898 HOH   A O     1 
HETATM 7687 O O     . HOH   T 6 .   ? -33.029 -100.786 -9.776  1.00 31.93  ? 899 HOH   A O     1 
HETATM 7688 O O     . HOH   T 6 .   ? -24.619 -49.567  -24.480 1.00 26.43  ? 900 HOH   A O     1 
HETATM 7689 O O     . HOH   T 6 .   ? -27.318 -55.172  -46.625 1.00 39.27  ? 901 HOH   A O     1 
HETATM 7690 O O     . HOH   T 6 .   ? -30.910 -80.062  -8.622  1.00 35.06  ? 902 HOH   A O     1 
HETATM 7691 O O     . HOH   T 6 .   ? 2.455   -88.227  -33.333 1.00 30.61  ? 903 HOH   A O     1 
HETATM 7692 O O     . HOH   T 6 .   ? -25.575 -77.478  -7.545  1.00 40.94  ? 904 HOH   A O     1 
HETATM 7693 O O     . HOH   T 6 .   ? -12.542 -73.471  -4.777  1.00 37.14  ? 905 HOH   A O     1 
HETATM 7694 O O     . HOH   T 6 .   ? -36.988 -112.022 -7.665  1.00 34.00  ? 906 HOH   A O     1 
HETATM 7695 O O     . HOH   T 6 .   ? -18.592 -74.413  -39.274 1.00 36.72  ? 907 HOH   A O     1 
HETATM 7696 O O     . HOH   T 6 .   ? -22.480 -52.799  -33.728 1.00 29.98  ? 908 HOH   A O     1 
HETATM 7697 O O     . HOH   T 6 .   ? -24.401 -80.684  -24.834 1.00 34.99  ? 909 HOH   A O     1 
HETATM 7698 O O     . HOH   T 6 .   ? -5.186  -90.189  -36.169 1.00 40.95  ? 910 HOH   A O     1 
HETATM 7699 O O     . HOH   T 6 .   ? -6.507  -51.258  -34.531 1.00 45.86  ? 911 HOH   A O     1 
HETATM 7700 O O     . HOH   T 6 .   ? -12.651 -113.955 -21.556 1.00 32.78  ? 912 HOH   A O     1 
HETATM 7701 O O     . HOH   T 6 .   ? -25.412 -58.051  -47.244 1.00 42.04  ? 913 HOH   A O     1 
HETATM 7702 O O     . HOH   T 6 .   ? -19.675 -89.782  -5.948  1.00 24.61  ? 914 HOH   A O     1 
HETATM 7703 O O     . HOH   T 6 .   ? -13.863 -98.344  -29.801 1.00 28.27  ? 915 HOH   A O     1 
HETATM 7704 O O     . HOH   U 6 .   ? -14.755 -27.801  -23.494 1.00 38.59  ? 501 HOH   B O     1 
HETATM 7705 O O     . HOH   U 6 .   ? -24.695 -24.827  -41.804 1.00 35.56  ? 502 HOH   B O     1 
HETATM 7706 O O     . HOH   U 6 .   ? -20.872 -27.115  -28.792 1.00 33.42  ? 503 HOH   B O     1 
HETATM 7707 O O     . HOH   U 6 .   ? -33.587 -23.383  -40.181 1.00 28.54  ? 504 HOH   B O     1 
HETATM 7708 O O     . HOH   U 6 .   ? -27.406 -35.734  -17.139 1.00 34.75  ? 505 HOH   B O     1 
HETATM 7709 O O     . HOH   U 6 .   ? -23.778 -50.147  -40.904 1.00 27.53  ? 506 HOH   B O     1 
HETATM 7710 O O     . HOH   U 6 .   ? -24.961 -28.786  -55.232 1.00 51.24  ? 507 HOH   B O     1 
HETATM 7711 O O     . HOH   U 6 .   ? -18.272 -17.731  -27.007 1.00 36.43  ? 508 HOH   B O     1 
HETATM 7712 O O     . HOH   U 6 .   ? -14.639 -39.754  -46.586 1.00 33.01  ? 509 HOH   B O     1 
HETATM 7713 O O     . HOH   U 6 .   ? -28.779 -14.149  -22.724 1.00 34.44  ? 510 HOH   B O     1 
HETATM 7714 O O     . HOH   U 6 .   ? -20.544 -44.884  -33.231 1.00 27.09  ? 511 HOH   B O     1 
HETATM 7715 O O     . HOH   U 6 .   ? -26.880 -26.042  -54.785 1.00 38.91  ? 512 HOH   B O     1 
HETATM 7716 O O     . HOH   U 6 .   ? -23.145 -21.742  -58.615 1.00 39.98  ? 513 HOH   B O     1 
HETATM 7717 O O     . HOH   U 6 .   ? -17.159 -47.782  -37.966 1.00 36.43  ? 514 HOH   B O     1 
HETATM 7718 O O     . HOH   U 6 .   ? -36.054 -26.465  -55.888 1.00 39.13  ? 515 HOH   B O     1 
HETATM 7719 O O     . HOH   U 6 .   ? -29.498 -28.991  -15.480 1.00 43.59  ? 516 HOH   B O     1 
HETATM 7720 O O     . HOH   U 6 .   ? -42.103 -32.246  -54.492 1.00 37.48  ? 517 HOH   B O     1 
# 
